data_9ESE
# 
_entry.id   9ESE 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9ESE         pdb_00009ese 10.2210/pdb9ese/pdb 
WWPDB D_1292136138 ?            ?                   
# 
_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       2025-03-05 
_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                        9ESE 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-26 
_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           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              aengus.mac-sweeney@idorsia.com 
_pdbx_contact_author.name_first         Aengus 
_pdbx_contact_author.name_last          'Mac Sweeney' 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7250-9541 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Wicki, M.'       1 ? 
'Mac Sweeney, A.' 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                     'SAR and cellular potency optimization of novel heme-binding IDO1 inhibitors' 
_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 'Cren, S.'        1 ? 
primary 'Lotz, C.'        2 ? 
primary 'Mac Sweeney, A.' 3 ? 
primary 'Lange, R.'       4 ? 
primary 'Kimmerlin, T.'   5 ? 
# 
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 'Indoleamine 2,3-dioxygenase 1'                                                                           
47085.105 2  1.13.11.52 ? ? ? 
2 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE'                                                                         
616.487   2  ?          ? ? ? 
3 non-polymer syn '(~{R})-(2-cyclopropylimidazo[5,1-b][1,3]thiazol-3-yl)-[1-(1~{H}-indol-5-yl)-1,2,3-triazol-4-yl]methanol' 
376.435   2  ?          ? ? ? 
4 water       nat water                                                                                                     18.015 
19 ?          ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'IDO-1,Indoleamine-pyrrole 2,3-dioxygenase' 
# 
_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       
;MGSSHHHHHHSAALEVLFQGPHMWTISKEYHIDEEVGFALPNPQENLPDFYNDWMFIAKHLPDLIESGQLRERVEKLNML
SIDHLTDHKSQRLARLVLGCITMAYVWGKGHGDVRKVLPRNIAVPYCQLSKKLELPPILVYADCVLANWKKKDPNKPLTY
ENMDVLFSFRDGDCSKGFFLVSLLVEIAAASAIKVIPTVFKAMQMQERDTLLKALLEIASCLEKALQVFHQIHDHVNPKA
FFSVLRIYLSGWKGNPQLSDGLVYEGFWEDPKEFAGGSAGQSSVFQCFDVLLGIQQTAGGGHAAQFLQDMRRYMPPAHRN
FLCSLESNPSVREFVLSKGDAGLREAYDACVKALVSLRSYHLQIVTKYILIPASQQPKENKTSEDPSKLEAKGTGGTDLM
NFLKTVRSTTEKSLLKEG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSAALEVLFQGPHMWTISKEYHIDEEVGFALPNPQENLPDFYNDWMFIAKHLPDLIESGQLRERVEKLNML
SIDHLTDHKSQRLARLVLGCITMAYVWGKGHGDVRKVLPRNIAVPYCQLSKKLELPPILVYADCVLANWKKKDPNKPLTY
ENMDVLFSFRDGDCSKGFFLVSLLVEIAAASAIKVIPTVFKAMQMQERDTLLKALLEIASCLEKALQVFHQIHDHVNPKA
FFSVLRIYLSGWKGNPQLSDGLVYEGFWEDPKEFAGGSAGQSSVFQCFDVLLGIQQTAGGGHAAQFLQDMRRYMPPAHRN
FLCSLESNPSVREFVLSKGDAGLREAYDACVKALVSLRSYHLQIVTKYILIPASQQPKENKTSEDPSKLEAKGTGGTDLM
NFLKTVRSTTEKSLLKEG
;
_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 'PROTOPORPHYRIN IX CONTAINING FE'                                                                         HEM   
3 '(~{R})-(2-cyclopropylimidazo[5,1-b][1,3]thiazol-3-yl)-[1-(1~{H}-indol-5-yl)-1,2,3-triazol-4-yl]methanol' A1H6V 
4 water                                                                                                     HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  ALA n 
1 13  ALA n 
1 14  LEU n 
1 15  GLU n 
1 16  VAL n 
1 17  LEU n 
1 18  PHE n 
1 19  GLN n 
1 20  GLY n 
1 21  PRO n 
1 22  HIS n 
1 23  MET n 
1 24  TRP n 
1 25  THR n 
1 26  ILE n 
1 27  SER n 
1 28  LYS n 
1 29  GLU n 
1 30  TYR n 
1 31  HIS n 
1 32  ILE n 
1 33  ASP n 
1 34  GLU n 
1 35  GLU n 
1 36  VAL n 
1 37  GLY n 
1 38  PHE n 
1 39  ALA n 
1 40  LEU n 
1 41  PRO n 
1 42  ASN n 
1 43  PRO n 
1 44  GLN n 
1 45  GLU n 
1 46  ASN n 
1 47  LEU n 
1 48  PRO n 
1 49  ASP n 
1 50  PHE n 
1 51  TYR n 
1 52  ASN n 
1 53  ASP n 
1 54  TRP n 
1 55  MET n 
1 56  PHE n 
1 57  ILE n 
1 58  ALA n 
1 59  LYS n 
1 60  HIS n 
1 61  LEU n 
1 62  PRO n 
1 63  ASP n 
1 64  LEU n 
1 65  ILE n 
1 66  GLU n 
1 67  SER n 
1 68  GLY n 
1 69  GLN n 
1 70  LEU n 
1 71  ARG n 
1 72  GLU n 
1 73  ARG n 
1 74  VAL n 
1 75  GLU n 
1 76  LYS n 
1 77  LEU n 
1 78  ASN n 
1 79  MET n 
1 80  LEU n 
1 81  SER n 
1 82  ILE n 
1 83  ASP n 
1 84  HIS n 
1 85  LEU n 
1 86  THR n 
1 87  ASP n 
1 88  HIS n 
1 89  LYS n 
1 90  SER n 
1 91  GLN n 
1 92  ARG n 
1 93  LEU n 
1 94  ALA n 
1 95  ARG n 
1 96  LEU n 
1 97  VAL n 
1 98  LEU n 
1 99  GLY n 
1 100 CYS n 
1 101 ILE n 
1 102 THR n 
1 103 MET n 
1 104 ALA n 
1 105 TYR n 
1 106 VAL n 
1 107 TRP n 
1 108 GLY n 
1 109 LYS n 
1 110 GLY n 
1 111 HIS n 
1 112 GLY n 
1 113 ASP n 
1 114 VAL n 
1 115 ARG n 
1 116 LYS n 
1 117 VAL n 
1 118 LEU n 
1 119 PRO n 
1 120 ARG n 
1 121 ASN n 
1 122 ILE n 
1 123 ALA n 
1 124 VAL n 
1 125 PRO n 
1 126 TYR n 
1 127 CYS n 
1 128 GLN n 
1 129 LEU n 
1 130 SER n 
1 131 LYS n 
1 132 LYS n 
1 133 LEU n 
1 134 GLU n 
1 135 LEU n 
1 136 PRO n 
1 137 PRO n 
1 138 ILE n 
1 139 LEU n 
1 140 VAL n 
1 141 TYR n 
1 142 ALA n 
1 143 ASP n 
1 144 CYS n 
1 145 VAL n 
1 146 LEU n 
1 147 ALA n 
1 148 ASN n 
1 149 TRP n 
1 150 LYS n 
1 151 LYS n 
1 152 LYS n 
1 153 ASP n 
1 154 PRO n 
1 155 ASN n 
1 156 LYS n 
1 157 PRO n 
1 158 LEU n 
1 159 THR n 
1 160 TYR n 
1 161 GLU n 
1 162 ASN n 
1 163 MET n 
1 164 ASP n 
1 165 VAL n 
1 166 LEU n 
1 167 PHE n 
1 168 SER n 
1 169 PHE n 
1 170 ARG n 
1 171 ASP n 
1 172 GLY n 
1 173 ASP n 
1 174 CYS n 
1 175 SER n 
1 176 LYS n 
1 177 GLY n 
1 178 PHE n 
1 179 PHE n 
1 180 LEU n 
1 181 VAL n 
1 182 SER n 
1 183 LEU n 
1 184 LEU n 
1 185 VAL n 
1 186 GLU n 
1 187 ILE n 
1 188 ALA n 
1 189 ALA n 
1 190 ALA n 
1 191 SER n 
1 192 ALA n 
1 193 ILE n 
1 194 LYS n 
1 195 VAL n 
1 196 ILE n 
1 197 PRO n 
1 198 THR n 
1 199 VAL n 
1 200 PHE n 
1 201 LYS n 
1 202 ALA n 
1 203 MET n 
1 204 GLN n 
1 205 MET n 
1 206 GLN n 
1 207 GLU n 
1 208 ARG n 
1 209 ASP n 
1 210 THR n 
1 211 LEU n 
1 212 LEU n 
1 213 LYS n 
1 214 ALA n 
1 215 LEU n 
1 216 LEU n 
1 217 GLU n 
1 218 ILE n 
1 219 ALA n 
1 220 SER n 
1 221 CYS n 
1 222 LEU n 
1 223 GLU n 
1 224 LYS n 
1 225 ALA n 
1 226 LEU n 
1 227 GLN n 
1 228 VAL n 
1 229 PHE n 
1 230 HIS n 
1 231 GLN n 
1 232 ILE n 
1 233 HIS n 
1 234 ASP n 
1 235 HIS n 
1 236 VAL n 
1 237 ASN n 
1 238 PRO n 
1 239 LYS n 
1 240 ALA n 
1 241 PHE n 
1 242 PHE n 
1 243 SER n 
1 244 VAL n 
1 245 LEU n 
1 246 ARG n 
1 247 ILE n 
1 248 TYR n 
1 249 LEU n 
1 250 SER n 
1 251 GLY n 
1 252 TRP n 
1 253 LYS n 
1 254 GLY n 
1 255 ASN n 
1 256 PRO n 
1 257 GLN n 
1 258 LEU n 
1 259 SER n 
1 260 ASP n 
1 261 GLY n 
1 262 LEU n 
1 263 VAL n 
1 264 TYR n 
1 265 GLU n 
1 266 GLY n 
1 267 PHE n 
1 268 TRP n 
1 269 GLU n 
1 270 ASP n 
1 271 PRO n 
1 272 LYS n 
1 273 GLU n 
1 274 PHE n 
1 275 ALA n 
1 276 GLY n 
1 277 GLY n 
1 278 SER n 
1 279 ALA n 
1 280 GLY n 
1 281 GLN n 
1 282 SER n 
1 283 SER n 
1 284 VAL n 
1 285 PHE n 
1 286 GLN n 
1 287 CYS n 
1 288 PHE n 
1 289 ASP n 
1 290 VAL n 
1 291 LEU n 
1 292 LEU n 
1 293 GLY n 
1 294 ILE n 
1 295 GLN n 
1 296 GLN n 
1 297 THR n 
1 298 ALA n 
1 299 GLY n 
1 300 GLY n 
1 301 GLY n 
1 302 HIS n 
1 303 ALA n 
1 304 ALA n 
1 305 GLN n 
1 306 PHE n 
1 307 LEU n 
1 308 GLN n 
1 309 ASP n 
1 310 MET n 
1 311 ARG n 
1 312 ARG n 
1 313 TYR n 
1 314 MET n 
1 315 PRO n 
1 316 PRO n 
1 317 ALA n 
1 318 HIS n 
1 319 ARG n 
1 320 ASN n 
1 321 PHE n 
1 322 LEU n 
1 323 CYS n 
1 324 SER n 
1 325 LEU n 
1 326 GLU n 
1 327 SER n 
1 328 ASN n 
1 329 PRO n 
1 330 SER n 
1 331 VAL n 
1 332 ARG n 
1 333 GLU n 
1 334 PHE n 
1 335 VAL n 
1 336 LEU n 
1 337 SER n 
1 338 LYS n 
1 339 GLY n 
1 340 ASP n 
1 341 ALA n 
1 342 GLY n 
1 343 LEU n 
1 344 ARG n 
1 345 GLU n 
1 346 ALA n 
1 347 TYR n 
1 348 ASP n 
1 349 ALA n 
1 350 CYS n 
1 351 VAL n 
1 352 LYS n 
1 353 ALA n 
1 354 LEU n 
1 355 VAL n 
1 356 SER n 
1 357 LEU n 
1 358 ARG n 
1 359 SER n 
1 360 TYR n 
1 361 HIS n 
1 362 LEU n 
1 363 GLN n 
1 364 ILE n 
1 365 VAL n 
1 366 THR n 
1 367 LYS n 
1 368 TYR n 
1 369 ILE n 
1 370 LEU n 
1 371 ILE n 
1 372 PRO n 
1 373 ALA n 
1 374 SER n 
1 375 GLN n 
1 376 GLN n 
1 377 PRO n 
1 378 LYS n 
1 379 GLU n 
1 380 ASN n 
1 381 LYS n 
1 382 THR n 
1 383 SER n 
1 384 GLU n 
1 385 ASP n 
1 386 PRO n 
1 387 SER n 
1 388 LYS n 
1 389 LEU n 
1 390 GLU n 
1 391 ALA n 
1 392 LYS n 
1 393 GLY n 
1 394 THR n 
1 395 GLY n 
1 396 GLY n 
1 397 THR n 
1 398 ASP n 
1 399 LEU n 
1 400 MET n 
1 401 ASN n 
1 402 PHE n 
1 403 LEU n 
1 404 LYS n 
1 405 THR n 
1 406 VAL n 
1 407 ARG n 
1 408 SER n 
1 409 THR n 
1 410 THR n 
1 411 GLU n 
1 412 LYS n 
1 413 SER n 
1 414 LEU n 
1 415 LEU n 
1 416 LYS n 
1 417 GLU n 
1 418 GLY n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   418 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'IDO1, IDO, INDO' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1H6V non-polymer         . 
'(~{R})-(2-cyclopropylimidazo[5,1-b][1,3]thiazol-3-yl)-[1-(1~{H}-indol-5-yl)-1,2,3-triazol-4-yl]methanol' ?    'C19 H16 N6 O S'   
376.435 
ALA   'L-peptide linking' y ALANINE ?    'C3 H7 N O2'       89.093  
ARG   'L-peptide linking' y ARGININE ?    'C6 H15 N4 O2 1'   175.209 
ASN   'L-peptide linking' y ASPARAGINE ?    'C4 H8 N2 O3'      132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ?    'C4 H7 N O4'       133.103 
CYS   'L-peptide linking' y CYSTEINE ?    'C3 H7 N O2 S'     121.158 
GLN   'L-peptide linking' y GLUTAMINE ?    'C5 H10 N2 O3'     146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ?    'C5 H9 N O4'       147.129 
GLY   'peptide linking'   y GLYCINE ?    'C2 H5 N O2'       75.067  
HEM   non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE' HEME 'C34 H32 Fe N4 O4' 616.487 
HIS   'L-peptide linking' y HISTIDINE ?    'C6 H10 N3 O2 1'   156.162 
HOH   non-polymer         . WATER ?    'H2 O'             18.015  
ILE   'L-peptide linking' y ISOLEUCINE ?    'C6 H13 N O2'      131.173 
LEU   'L-peptide linking' y LEUCINE ?    'C6 H13 N O2'      131.173 
LYS   'L-peptide linking' y LYSINE ?    'C6 H15 N2 O2 1'   147.195 
MET   'L-peptide linking' y METHIONINE ?    'C5 H11 N O2 S'    149.211 
PHE   'L-peptide linking' y PHENYLALANINE ?    'C9 H11 N O2'      165.189 
PRO   'L-peptide linking' y PROLINE ?    'C5 H9 N O2'       115.130 
SER   'L-peptide linking' y SERINE ?    'C3 H7 N O3'       105.093 
THR   'L-peptide linking' y THREONINE ?    'C4 H9 N O3'       119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ?    'C11 H12 N2 O2'    204.225 
TYR   'L-peptide linking' y TYROSINE ?    'C9 H11 N O3'      181.189 
VAL   'L-peptide linking' y VALINE ?    'C5 H11 N O2'      117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -14 ?   ?   ?   A . n 
A 1 2   GLY 2   -13 ?   ?   ?   A . n 
A 1 3   SER 3   -12 ?   ?   ?   A . n 
A 1 4   SER 4   -11 ?   ?   ?   A . n 
A 1 5   HIS 5   -10 ?   ?   ?   A . n 
A 1 6   HIS 6   -9  ?   ?   ?   A . n 
A 1 7   HIS 7   -8  ?   ?   ?   A . n 
A 1 8   HIS 8   -7  ?   ?   ?   A . n 
A 1 9   HIS 9   -6  ?   ?   ?   A . n 
A 1 10  HIS 10  -5  ?   ?   ?   A . n 
A 1 11  SER 11  -4  ?   ?   ?   A . n 
A 1 12  ALA 12  -3  ?   ?   ?   A . n 
A 1 13  ALA 13  -2  -2  ALA ALA A . n 
A 1 14  LEU 14  -1  -1  LEU LEU A . n 
A 1 15  GLU 15  0   0   GLU GLU A . n 
A 1 16  VAL 16  1   1   VAL VAL A . n 
A 1 17  LEU 17  2   2   LEU LEU A . n 
A 1 18  PHE 18  3   3   PHE PHE A . n 
A 1 19  GLN 19  4   4   GLN GLN A . n 
A 1 20  GLY 20  5   5   GLY GLY A . n 
A 1 21  PRO 21  6   6   PRO PRO A . n 
A 1 22  HIS 22  7   7   HIS HIS A . n 
A 1 23  MET 23  8   8   MET MET A . n 
A 1 24  TRP 24  9   9   TRP TRP A . n 
A 1 25  THR 25  10  10  THR THR A . n 
A 1 26  ILE 26  11  11  ILE ILE A . n 
A 1 27  SER 27  12  12  SER SER A . n 
A 1 28  LYS 28  13  13  LYS LYS A . n 
A 1 29  GLU 29  14  14  GLU GLU A . n 
A 1 30  TYR 30  15  15  TYR TYR A . n 
A 1 31  HIS 31  16  16  HIS HIS A . n 
A 1 32  ILE 32  17  17  ILE ILE A . n 
A 1 33  ASP 33  18  18  ASP ASP A . n 
A 1 34  GLU 34  19  19  GLU GLU A . n 
A 1 35  GLU 35  20  20  GLU GLU A . n 
A 1 36  VAL 36  21  21  VAL VAL A . n 
A 1 37  GLY 37  22  22  GLY GLY A . n 
A 1 38  PHE 38  23  23  PHE PHE A . n 
A 1 39  ALA 39  24  24  ALA ALA A . n 
A 1 40  LEU 40  25  25  LEU LEU A . n 
A 1 41  PRO 41  26  26  PRO PRO A . n 
A 1 42  ASN 42  27  27  ASN ASN A . n 
A 1 43  PRO 43  28  28  PRO PRO A . n 
A 1 44  GLN 44  29  29  GLN GLN A . n 
A 1 45  GLU 45  30  30  GLU GLU A . n 
A 1 46  ASN 46  31  31  ASN ASN A . n 
A 1 47  LEU 47  32  32  LEU LEU A . n 
A 1 48  PRO 48  33  33  PRO PRO A . n 
A 1 49  ASP 49  34  34  ASP ASP A . n 
A 1 50  PHE 50  35  35  PHE PHE A . n 
A 1 51  TYR 51  36  36  TYR TYR A . n 
A 1 52  ASN 52  37  37  ASN ASN A . n 
A 1 53  ASP 53  38  38  ASP ASP A . n 
A 1 54  TRP 54  39  39  TRP TRP A . n 
A 1 55  MET 55  40  40  MET MET A . n 
A 1 56  PHE 56  41  41  PHE PHE A . n 
A 1 57  ILE 57  42  42  ILE ILE A . n 
A 1 58  ALA 58  43  43  ALA ALA A . n 
A 1 59  LYS 59  44  44  LYS LYS A . n 
A 1 60  HIS 60  45  45  HIS HIS A . n 
A 1 61  LEU 61  46  46  LEU LEU A . n 
A 1 62  PRO 62  47  47  PRO PRO A . n 
A 1 63  ASP 63  48  48  ASP ASP A . n 
A 1 64  LEU 64  49  49  LEU LEU A . n 
A 1 65  ILE 65  50  50  ILE ILE A . n 
A 1 66  GLU 66  51  51  GLU GLU A . n 
A 1 67  SER 67  52  52  SER SER A . n 
A 1 68  GLY 68  53  53  GLY GLY A . n 
A 1 69  GLN 69  54  54  GLN GLN A . n 
A 1 70  LEU 70  55  55  LEU LEU A . n 
A 1 71  ARG 71  56  56  ARG ARG A . n 
A 1 72  GLU 72  57  57  GLU GLU A . n 
A 1 73  ARG 73  58  58  ARG ARG A . n 
A 1 74  VAL 74  59  59  VAL VAL A . n 
A 1 75  GLU 75  60  60  GLU GLU A . n 
A 1 76  LYS 76  61  61  LYS LYS A . n 
A 1 77  LEU 77  62  62  LEU LEU A . n 
A 1 78  ASN 78  63  63  ASN ASN A . n 
A 1 79  MET 79  64  64  MET MET A . n 
A 1 80  LEU 80  65  65  LEU LEU A . n 
A 1 81  SER 81  66  66  SER SER A . n 
A 1 82  ILE 82  67  67  ILE ILE A . n 
A 1 83  ASP 83  68  68  ASP ASP A . n 
A 1 84  HIS 84  69  69  HIS HIS A . n 
A 1 85  LEU 85  70  70  LEU LEU A . n 
A 1 86  THR 86  71  71  THR THR A . n 
A 1 87  ASP 87  72  72  ASP ASP A . n 
A 1 88  HIS 88  73  73  HIS HIS A . n 
A 1 89  LYS 89  74  74  LYS LYS A . n 
A 1 90  SER 90  75  75  SER SER A . n 
A 1 91  GLN 91  76  76  GLN GLN A . n 
A 1 92  ARG 92  77  77  ARG ARG A . n 
A 1 93  LEU 93  78  78  LEU LEU A . n 
A 1 94  ALA 94  79  79  ALA ALA A . n 
A 1 95  ARG 95  80  80  ARG ARG A . n 
A 1 96  LEU 96  81  81  LEU LEU A . n 
A 1 97  VAL 97  82  82  VAL VAL A . n 
A 1 98  LEU 98  83  83  LEU LEU A . n 
A 1 99  GLY 99  84  84  GLY GLY A . n 
A 1 100 CYS 100 85  85  CYS CYS A . n 
A 1 101 ILE 101 86  86  ILE ILE A . n 
A 1 102 THR 102 87  87  THR THR A . n 
A 1 103 MET 103 88  88  MET MET A . n 
A 1 104 ALA 104 89  89  ALA ALA A . n 
A 1 105 TYR 105 90  90  TYR TYR A . n 
A 1 106 VAL 106 91  91  VAL VAL A . n 
A 1 107 TRP 107 92  92  TRP TRP A . n 
A 1 108 GLY 108 93  93  GLY GLY A . n 
A 1 109 LYS 109 94  94  LYS LYS A . n 
A 1 110 GLY 110 95  95  GLY GLY A . n 
A 1 111 HIS 111 96  96  HIS HIS A . n 
A 1 112 GLY 112 97  97  GLY GLY A . n 
A 1 113 ASP 113 98  98  ASP ASP A . n 
A 1 114 VAL 114 99  99  VAL VAL A . n 
A 1 115 ARG 115 100 100 ARG ARG A . n 
A 1 116 LYS 116 101 101 LYS LYS A . n 
A 1 117 VAL 117 102 102 VAL VAL A . n 
A 1 118 LEU 118 103 103 LEU LEU A . n 
A 1 119 PRO 119 104 104 PRO PRO A . n 
A 1 120 ARG 120 105 105 ARG ARG A . n 
A 1 121 ASN 121 106 106 ASN ASN A . n 
A 1 122 ILE 122 107 107 ILE ILE A . n 
A 1 123 ALA 123 108 108 ALA ALA A . n 
A 1 124 VAL 124 109 109 VAL VAL A . n 
A 1 125 PRO 125 110 110 PRO PRO A . n 
A 1 126 TYR 126 111 111 TYR TYR A . n 
A 1 127 CYS 127 112 112 CYS CYS A . n 
A 1 128 GLN 128 113 113 GLN GLN A . n 
A 1 129 LEU 129 114 114 LEU LEU A . n 
A 1 130 SER 130 115 115 SER SER A . n 
A 1 131 LYS 131 116 116 LYS LYS A . n 
A 1 132 LYS 132 117 117 LYS LYS A . n 
A 1 133 LEU 133 118 118 LEU LEU A . n 
A 1 134 GLU 134 119 119 GLU GLU A . n 
A 1 135 LEU 135 120 120 LEU LEU A . n 
A 1 136 PRO 136 121 121 PRO PRO A . n 
A 1 137 PRO 137 122 122 PRO PRO A . n 
A 1 138 ILE 138 123 123 ILE ILE A . n 
A 1 139 LEU 139 124 124 LEU LEU A . n 
A 1 140 VAL 140 125 125 VAL VAL A . n 
A 1 141 TYR 141 126 126 TYR TYR A . n 
A 1 142 ALA 142 127 127 ALA ALA A . n 
A 1 143 ASP 143 128 128 ASP ASP A . n 
A 1 144 CYS 144 129 129 CYS CYS A . n 
A 1 145 VAL 145 130 130 VAL VAL A . n 
A 1 146 LEU 146 131 131 LEU LEU A . n 
A 1 147 ALA 147 132 132 ALA ALA A . n 
A 1 148 ASN 148 133 133 ASN ASN A . n 
A 1 149 TRP 149 134 134 TRP TRP A . n 
A 1 150 LYS 150 135 135 LYS LYS A . n 
A 1 151 LYS 151 136 136 LYS LYS A . n 
A 1 152 LYS 152 137 137 LYS LYS A . n 
A 1 153 ASP 153 138 138 ASP ASP A . n 
A 1 154 PRO 154 139 139 PRO PRO A . n 
A 1 155 ASN 155 140 140 ASN ASN A . n 
A 1 156 LYS 156 141 141 LYS LYS A . n 
A 1 157 PRO 157 142 142 PRO PRO A . n 
A 1 158 LEU 158 143 143 LEU LEU A . n 
A 1 159 THR 159 144 144 THR THR A . n 
A 1 160 TYR 160 145 145 TYR TYR A . n 
A 1 161 GLU 161 146 146 GLU GLU A . n 
A 1 162 ASN 162 147 147 ASN ASN A . n 
A 1 163 MET 163 148 148 MET MET A . n 
A 1 164 ASP 164 149 149 ASP ASP A . n 
A 1 165 VAL 165 150 150 VAL VAL A . n 
A 1 166 LEU 166 151 151 LEU LEU A . n 
A 1 167 PHE 167 152 152 PHE PHE A . n 
A 1 168 SER 168 153 153 SER SER A . n 
A 1 169 PHE 169 154 154 PHE PHE A . n 
A 1 170 ARG 170 155 155 ARG ARG A . n 
A 1 171 ASP 171 156 156 ASP ASP A . n 
A 1 172 GLY 172 157 157 GLY GLY A . n 
A 1 173 ASP 173 158 158 ASP ASP A . n 
A 1 174 CYS 174 159 159 CYS CYS A . n 
A 1 175 SER 175 160 160 SER SER A . n 
A 1 176 LYS 176 161 161 LYS LYS A . n 
A 1 177 GLY 177 162 162 GLY GLY A . n 
A 1 178 PHE 178 163 163 PHE PHE A . n 
A 1 179 PHE 179 164 164 PHE PHE A . n 
A 1 180 LEU 180 165 165 LEU LEU A . n 
A 1 181 VAL 181 166 166 VAL VAL A . n 
A 1 182 SER 182 167 167 SER SER A . n 
A 1 183 LEU 183 168 168 LEU LEU A . n 
A 1 184 LEU 184 169 169 LEU LEU A . n 
A 1 185 VAL 185 170 170 VAL VAL A . n 
A 1 186 GLU 186 171 171 GLU GLU A . n 
A 1 187 ILE 187 172 172 ILE ILE A . n 
A 1 188 ALA 188 173 173 ALA ALA A . n 
A 1 189 ALA 189 174 174 ALA ALA A . n 
A 1 190 ALA 190 175 175 ALA ALA A . n 
A 1 191 SER 191 176 176 SER SER A . n 
A 1 192 ALA 192 177 177 ALA ALA A . n 
A 1 193 ILE 193 178 178 ILE ILE A . n 
A 1 194 LYS 194 179 179 LYS LYS A . n 
A 1 195 VAL 195 180 180 VAL VAL A . n 
A 1 196 ILE 196 181 181 ILE ILE A . n 
A 1 197 PRO 197 182 182 PRO PRO A . n 
A 1 198 THR 198 183 183 THR THR A . n 
A 1 199 VAL 199 184 184 VAL VAL A . n 
A 1 200 PHE 200 185 185 PHE PHE A . n 
A 1 201 LYS 201 186 186 LYS LYS A . n 
A 1 202 ALA 202 187 187 ALA ALA A . n 
A 1 203 MET 203 188 188 MET MET A . n 
A 1 204 GLN 204 189 189 GLN GLN A . n 
A 1 205 MET 205 190 190 MET MET A . n 
A 1 206 GLN 206 191 191 GLN GLN A . n 
A 1 207 GLU 207 192 192 GLU GLU A . n 
A 1 208 ARG 208 193 193 ARG ARG A . n 
A 1 209 ASP 209 194 194 ASP ASP A . n 
A 1 210 THR 210 195 195 THR THR A . n 
A 1 211 LEU 211 196 196 LEU LEU A . n 
A 1 212 LEU 212 197 197 LEU LEU A . n 
A 1 213 LYS 213 198 198 LYS LYS A . n 
A 1 214 ALA 214 199 199 ALA ALA A . n 
A 1 215 LEU 215 200 200 LEU LEU A . n 
A 1 216 LEU 216 201 201 LEU LEU A . n 
A 1 217 GLU 217 202 202 GLU GLU A . n 
A 1 218 ILE 218 203 203 ILE ILE A . n 
A 1 219 ALA 219 204 204 ALA ALA A . n 
A 1 220 SER 220 205 205 SER SER A . n 
A 1 221 CYS 221 206 206 CYS CYS A . n 
A 1 222 LEU 222 207 207 LEU LEU A . n 
A 1 223 GLU 223 208 208 GLU GLU A . n 
A 1 224 LYS 224 209 209 LYS LYS A . n 
A 1 225 ALA 225 210 210 ALA ALA A . n 
A 1 226 LEU 226 211 211 LEU LEU A . n 
A 1 227 GLN 227 212 212 GLN GLN A . n 
A 1 228 VAL 228 213 213 VAL VAL A . n 
A 1 229 PHE 229 214 214 PHE PHE A . n 
A 1 230 HIS 230 215 215 HIS HIS A . n 
A 1 231 GLN 231 216 216 GLN GLN A . n 
A 1 232 ILE 232 217 217 ILE ILE A . n 
A 1 233 HIS 233 218 218 HIS HIS A . n 
A 1 234 ASP 234 219 219 ASP ASP A . n 
A 1 235 HIS 235 220 220 HIS HIS A . n 
A 1 236 VAL 236 221 221 VAL VAL A . n 
A 1 237 ASN 237 222 222 ASN ASN A . n 
A 1 238 PRO 238 223 223 PRO PRO A . n 
A 1 239 LYS 239 224 224 LYS LYS A . n 
A 1 240 ALA 240 225 225 ALA ALA A . n 
A 1 241 PHE 241 226 226 PHE PHE A . n 
A 1 242 PHE 242 227 227 PHE PHE A . n 
A 1 243 SER 243 228 228 SER SER A . n 
A 1 244 VAL 244 229 229 VAL VAL A . n 
A 1 245 LEU 245 230 230 LEU LEU A . n 
A 1 246 ARG 246 231 231 ARG ARG A . n 
A 1 247 ILE 247 232 232 ILE ILE A . n 
A 1 248 TYR 248 233 233 TYR TYR A . n 
A 1 249 LEU 249 234 234 LEU LEU A . n 
A 1 250 SER 250 235 235 SER SER A . n 
A 1 251 GLY 251 236 236 GLY GLY A . n 
A 1 252 TRP 252 237 237 TRP TRP A . n 
A 1 253 LYS 253 238 238 LYS LYS A . n 
A 1 254 GLY 254 239 239 GLY GLY A . n 
A 1 255 ASN 255 240 240 ASN ASN A . n 
A 1 256 PRO 256 241 241 PRO PRO A . n 
A 1 257 GLN 257 242 242 GLN GLN A . n 
A 1 258 LEU 258 243 243 LEU LEU A . n 
A 1 259 SER 259 244 244 SER SER A . n 
A 1 260 ASP 260 245 245 ASP ASP A . n 
A 1 261 GLY 261 246 246 GLY GLY A . n 
A 1 262 LEU 262 247 247 LEU LEU A . n 
A 1 263 VAL 263 248 248 VAL VAL A . n 
A 1 264 TYR 264 249 249 TYR TYR A . n 
A 1 265 GLU 265 250 250 GLU GLU A . n 
A 1 266 GLY 266 251 251 GLY GLY A . n 
A 1 267 PHE 267 252 252 PHE PHE A . n 
A 1 268 TRP 268 253 253 TRP TRP A . n 
A 1 269 GLU 269 254 254 GLU GLU A . n 
A 1 270 ASP 270 255 255 ASP ASP A . n 
A 1 271 PRO 271 256 256 PRO PRO A . n 
A 1 272 LYS 272 257 257 LYS LYS A . n 
A 1 273 GLU 273 258 258 GLU GLU A . n 
A 1 274 PHE 274 259 259 PHE PHE A . n 
A 1 275 ALA 275 260 260 ALA ALA A . n 
A 1 276 GLY 276 261 261 GLY GLY A . n 
A 1 277 GLY 277 262 262 GLY GLY A . n 
A 1 278 SER 278 263 263 SER SER A . n 
A 1 279 ALA 279 264 264 ALA ALA A . n 
A 1 280 GLY 280 265 265 GLY GLY A . n 
A 1 281 GLN 281 266 266 GLN GLN A . n 
A 1 282 SER 282 267 267 SER SER A . n 
A 1 283 SER 283 268 268 SER SER A . n 
A 1 284 VAL 284 269 269 VAL VAL A . n 
A 1 285 PHE 285 270 270 PHE PHE A . n 
A 1 286 GLN 286 271 271 GLN GLN A . n 
A 1 287 CYS 287 272 272 CYS CYS A . n 
A 1 288 PHE 288 273 273 PHE PHE A . n 
A 1 289 ASP 289 274 274 ASP ASP A . n 
A 1 290 VAL 290 275 275 VAL VAL A . n 
A 1 291 LEU 291 276 276 LEU LEU A . n 
A 1 292 LEU 292 277 277 LEU LEU A . n 
A 1 293 GLY 293 278 278 GLY GLY A . n 
A 1 294 ILE 294 279 279 ILE ILE A . n 
A 1 295 GLN 295 280 280 GLN GLN A . n 
A 1 296 GLN 296 281 281 GLN GLN A . n 
A 1 297 THR 297 282 282 THR THR A . n 
A 1 298 ALA 298 283 283 ALA ALA A . n 
A 1 299 GLY 299 284 ?   ?   ?   A . n 
A 1 300 GLY 300 285 285 GLY GLY A . n 
A 1 301 GLY 301 286 286 GLY GLY A . n 
A 1 302 HIS 302 287 287 HIS HIS A . n 
A 1 303 ALA 303 288 288 ALA ALA A . n 
A 1 304 ALA 304 289 289 ALA ALA A . n 
A 1 305 GLN 305 290 290 GLN GLN A . n 
A 1 306 PHE 306 291 291 PHE PHE A . n 
A 1 307 LEU 307 292 292 LEU LEU A . n 
A 1 308 GLN 308 293 293 GLN GLN A . n 
A 1 309 ASP 309 294 294 ASP ASP A . n 
A 1 310 MET 310 295 295 MET MET A . n 
A 1 311 ARG 311 296 296 ARG ARG A . n 
A 1 312 ARG 312 297 297 ARG ARG A . n 
A 1 313 TYR 313 298 298 TYR TYR A . n 
A 1 314 MET 314 299 299 MET MET A . n 
A 1 315 PRO 315 300 300 PRO PRO A . n 
A 1 316 PRO 316 301 301 PRO PRO A . n 
A 1 317 ALA 317 302 302 ALA ALA A . n 
A 1 318 HIS 318 303 303 HIS HIS A . n 
A 1 319 ARG 319 304 304 ARG ARG A . n 
A 1 320 ASN 320 305 305 ASN ASN A . n 
A 1 321 PHE 321 306 306 PHE PHE A . n 
A 1 322 LEU 322 307 307 LEU LEU A . n 
A 1 323 CYS 323 308 308 CYS CYS A . n 
A 1 324 SER 324 309 309 SER SER A . n 
A 1 325 LEU 325 310 310 LEU LEU A . n 
A 1 326 GLU 326 311 311 GLU GLU A . n 
A 1 327 SER 327 312 312 SER SER A . n 
A 1 328 ASN 328 313 313 ASN ASN A . n 
A 1 329 PRO 329 314 314 PRO PRO A . n 
A 1 330 SER 330 315 315 SER SER A . n 
A 1 331 VAL 331 316 316 VAL VAL A . n 
A 1 332 ARG 332 317 317 ARG ARG A . n 
A 1 333 GLU 333 318 318 GLU GLU A . n 
A 1 334 PHE 334 319 319 PHE PHE A . n 
A 1 335 VAL 335 320 320 VAL VAL A . n 
A 1 336 LEU 336 321 321 LEU LEU A . n 
A 1 337 SER 337 322 322 SER SER A . n 
A 1 338 LYS 338 323 323 LYS LYS A . n 
A 1 339 GLY 339 324 324 GLY GLY A . n 
A 1 340 ASP 340 325 325 ASP ASP A . n 
A 1 341 ALA 341 326 326 ALA ALA A . n 
A 1 342 GLY 342 327 327 GLY GLY A . n 
A 1 343 LEU 343 328 328 LEU LEU A . n 
A 1 344 ARG 344 329 329 ARG ARG A . n 
A 1 345 GLU 345 330 330 GLU GLU A . n 
A 1 346 ALA 346 331 331 ALA ALA A . n 
A 1 347 TYR 347 332 332 TYR TYR A . n 
A 1 348 ASP 348 333 333 ASP ASP A . n 
A 1 349 ALA 349 334 334 ALA ALA A . n 
A 1 350 CYS 350 335 335 CYS CYS A . n 
A 1 351 VAL 351 336 336 VAL VAL A . n 
A 1 352 LYS 352 337 337 LYS LYS A . n 
A 1 353 ALA 353 338 338 ALA ALA A . n 
A 1 354 LEU 354 339 339 LEU LEU A . n 
A 1 355 VAL 355 340 340 VAL VAL A . n 
A 1 356 SER 356 341 341 SER SER A . n 
A 1 357 LEU 357 342 342 LEU LEU A . n 
A 1 358 ARG 358 343 343 ARG ARG A . n 
A 1 359 SER 359 344 344 SER SER A . n 
A 1 360 TYR 360 345 345 TYR TYR A . n 
A 1 361 HIS 361 346 346 HIS HIS A . n 
A 1 362 LEU 362 347 347 LEU LEU A . n 
A 1 363 GLN 363 348 348 GLN GLN A . n 
A 1 364 ILE 364 349 349 ILE ILE A . n 
A 1 365 VAL 365 350 350 VAL VAL A . n 
A 1 366 THR 366 351 351 THR THR A . n 
A 1 367 LYS 367 352 352 LYS LYS A . n 
A 1 368 TYR 368 353 353 TYR TYR A . n 
A 1 369 ILE 369 354 354 ILE ILE A . n 
A 1 370 LEU 370 355 355 LEU LEU A . n 
A 1 371 ILE 371 356 356 ILE ILE A . n 
A 1 372 PRO 372 357 357 PRO PRO A . n 
A 1 373 ALA 373 358 358 ALA ALA A . n 
A 1 374 SER 374 359 359 SER SER A . n 
A 1 375 GLN 375 360 360 GLN GLN A . n 
A 1 376 GLN 376 361 361 GLN GLN A . n 
A 1 377 PRO 377 362 362 PRO PRO A . n 
A 1 378 LYS 378 363 ?   ?   ?   A . n 
A 1 379 GLU 379 364 ?   ?   ?   A . n 
A 1 380 ASN 380 365 ?   ?   ?   A . n 
A 1 381 LYS 381 366 ?   ?   ?   A . n 
A 1 382 THR 382 367 ?   ?   ?   A . n 
A 1 383 SER 383 368 ?   ?   ?   A . n 
A 1 384 GLU 384 369 ?   ?   ?   A . n 
A 1 385 ASP 385 370 ?   ?   ?   A . n 
A 1 386 PRO 386 371 ?   ?   ?   A . n 
A 1 387 SER 387 372 ?   ?   ?   A . n 
A 1 388 LYS 388 373 ?   ?   ?   A . n 
A 1 389 LEU 389 374 ?   ?   ?   A . n 
A 1 390 GLU 390 375 ?   ?   ?   A . n 
A 1 391 ALA 391 376 ?   ?   ?   A . n 
A 1 392 LYS 392 377 ?   ?   ?   A . n 
A 1 393 GLY 393 378 ?   ?   ?   A . n 
A 1 394 THR 394 379 ?   ?   ?   A . n 
A 1 395 GLY 395 380 ?   ?   ?   A . n 
A 1 396 GLY 396 381 ?   ?   ?   A . n 
A 1 397 THR 397 382 382 THR THR A . n 
A 1 398 ASP 398 383 383 ASP ASP A . n 
A 1 399 LEU 399 384 384 LEU LEU A . n 
A 1 400 MET 400 385 385 MET MET A . n 
A 1 401 ASN 401 386 386 ASN ASN A . n 
A 1 402 PHE 402 387 387 PHE PHE A . n 
A 1 403 LEU 403 388 388 LEU LEU A . n 
A 1 404 LYS 404 389 389 LYS LYS A . n 
A 1 405 THR 405 390 390 THR THR A . n 
A 1 406 VAL 406 391 391 VAL VAL A . n 
A 1 407 ARG 407 392 392 ARG ARG A . n 
A 1 408 SER 408 393 393 SER SER A . n 
A 1 409 THR 409 394 394 THR THR A . n 
A 1 410 THR 410 395 395 THR THR A . n 
A 1 411 GLU 411 396 396 GLU GLU A . n 
A 1 412 LYS 412 397 397 LYS LYS A . n 
A 1 413 SER 413 398 398 SER SER A . n 
A 1 414 LEU 414 399 399 LEU LEU A . n 
A 1 415 LEU 415 400 400 LEU LEU A . n 
A 1 416 LYS 416 401 401 LYS LYS A . n 
A 1 417 GLU 417 402 402 GLU GLU A . n 
A 1 418 GLY 418 403 ?   ?   ?   A . n 
B 1 1   MET 1   -14 ?   ?   ?   B . n 
B 1 2   GLY 2   -13 ?   ?   ?   B . n 
B 1 3   SER 3   -12 ?   ?   ?   B . n 
B 1 4   SER 4   -11 ?   ?   ?   B . n 
B 1 5   HIS 5   -10 ?   ?   ?   B . n 
B 1 6   HIS 6   -9  ?   ?   ?   B . n 
B 1 7   HIS 7   -8  ?   ?   ?   B . n 
B 1 8   HIS 8   -7  ?   ?   ?   B . n 
B 1 9   HIS 9   -6  ?   ?   ?   B . n 
B 1 10  HIS 10  -5  ?   ?   ?   B . n 
B 1 11  SER 11  -4  ?   ?   ?   B . n 
B 1 12  ALA 12  -3  ?   ?   ?   B . n 
B 1 13  ALA 13  -2  ?   ?   ?   B . n 
B 1 14  LEU 14  -1  ?   ?   ?   B . n 
B 1 15  GLU 15  0   ?   ?   ?   B . n 
B 1 16  VAL 16  1   ?   ?   ?   B . n 
B 1 17  LEU 17  2   ?   ?   ?   B . n 
B 1 18  PHE 18  3   ?   ?   ?   B . n 
B 1 19  GLN 19  4   ?   ?   ?   B . n 
B 1 20  GLY 20  5   ?   ?   ?   B . n 
B 1 21  PRO 21  6   ?   ?   ?   B . n 
B 1 22  HIS 22  7   ?   ?   ?   B . n 
B 1 23  MET 23  8   ?   ?   ?   B . n 
B 1 24  TRP 24  9   ?   ?   ?   B . n 
B 1 25  THR 25  10  10  THR THR B . n 
B 1 26  ILE 26  11  11  ILE ILE B . n 
B 1 27  SER 27  12  12  SER SER B . n 
B 1 28  LYS 28  13  13  LYS LYS B . n 
B 1 29  GLU 29  14  14  GLU GLU B . n 
B 1 30  TYR 30  15  15  TYR TYR B . n 
B 1 31  HIS 31  16  16  HIS HIS B . n 
B 1 32  ILE 32  17  17  ILE ILE B . n 
B 1 33  ASP 33  18  18  ASP ASP B . n 
B 1 34  GLU 34  19  19  GLU GLU B . n 
B 1 35  GLU 35  20  20  GLU GLU B . n 
B 1 36  VAL 36  21  21  VAL VAL B . n 
B 1 37  GLY 37  22  22  GLY GLY B . n 
B 1 38  PHE 38  23  23  PHE PHE B . n 
B 1 39  ALA 39  24  24  ALA ALA B . n 
B 1 40  LEU 40  25  25  LEU LEU B . n 
B 1 41  PRO 41  26  26  PRO PRO B . n 
B 1 42  ASN 42  27  27  ASN ASN B . n 
B 1 43  PRO 43  28  28  PRO PRO B . n 
B 1 44  GLN 44  29  29  GLN GLN B . n 
B 1 45  GLU 45  30  30  GLU GLU B . n 
B 1 46  ASN 46  31  31  ASN ASN B . n 
B 1 47  LEU 47  32  32  LEU LEU B . n 
B 1 48  PRO 48  33  33  PRO PRO B . n 
B 1 49  ASP 49  34  34  ASP ASP B . n 
B 1 50  PHE 50  35  35  PHE PHE B . n 
B 1 51  TYR 51  36  36  TYR TYR B . n 
B 1 52  ASN 52  37  37  ASN ASN B . n 
B 1 53  ASP 53  38  38  ASP ASP B . n 
B 1 54  TRP 54  39  39  TRP TRP B . n 
B 1 55  MET 55  40  40  MET MET B . n 
B 1 56  PHE 56  41  41  PHE PHE B . n 
B 1 57  ILE 57  42  42  ILE ILE B . n 
B 1 58  ALA 58  43  43  ALA ALA B . n 
B 1 59  LYS 59  44  44  LYS LYS B . n 
B 1 60  HIS 60  45  45  HIS HIS B . n 
B 1 61  LEU 61  46  46  LEU LEU B . n 
B 1 62  PRO 62  47  47  PRO PRO B . n 
B 1 63  ASP 63  48  48  ASP ASP B . n 
B 1 64  LEU 64  49  49  LEU LEU B . n 
B 1 65  ILE 65  50  50  ILE ILE B . n 
B 1 66  GLU 66  51  51  GLU GLU B . n 
B 1 67  SER 67  52  52  SER SER B . n 
B 1 68  GLY 68  53  53  GLY GLY B . n 
B 1 69  GLN 69  54  54  GLN GLN B . n 
B 1 70  LEU 70  55  55  LEU LEU B . n 
B 1 71  ARG 71  56  56  ARG ARG B . n 
B 1 72  GLU 72  57  57  GLU GLU B . n 
B 1 73  ARG 73  58  58  ARG ARG B . n 
B 1 74  VAL 74  59  59  VAL VAL B . n 
B 1 75  GLU 75  60  60  GLU GLU B . n 
B 1 76  LYS 76  61  61  LYS LYS B . n 
B 1 77  LEU 77  62  62  LEU LEU B . n 
B 1 78  ASN 78  63  63  ASN ASN B . n 
B 1 79  MET 79  64  64  MET MET B . n 
B 1 80  LEU 80  65  65  LEU LEU B . n 
B 1 81  SER 81  66  66  SER SER B . n 
B 1 82  ILE 82  67  67  ILE ILE B . n 
B 1 83  ASP 83  68  68  ASP ASP B . n 
B 1 84  HIS 84  69  69  HIS HIS B . n 
B 1 85  LEU 85  70  70  LEU LEU B . n 
B 1 86  THR 86  71  71  THR THR B . n 
B 1 87  ASP 87  72  72  ASP ASP B . n 
B 1 88  HIS 88  73  73  HIS HIS B . n 
B 1 89  LYS 89  74  74  LYS LYS B . n 
B 1 90  SER 90  75  75  SER SER B . n 
B 1 91  GLN 91  76  76  GLN GLN B . n 
B 1 92  ARG 92  77  77  ARG ARG B . n 
B 1 93  LEU 93  78  78  LEU LEU B . n 
B 1 94  ALA 94  79  79  ALA ALA B . n 
B 1 95  ARG 95  80  80  ARG ARG B . n 
B 1 96  LEU 96  81  81  LEU LEU B . n 
B 1 97  VAL 97  82  82  VAL VAL B . n 
B 1 98  LEU 98  83  83  LEU LEU B . n 
B 1 99  GLY 99  84  84  GLY GLY B . n 
B 1 100 CYS 100 85  85  CYS CYS B . n 
B 1 101 ILE 101 86  86  ILE ILE B . n 
B 1 102 THR 102 87  87  THR THR B . n 
B 1 103 MET 103 88  88  MET MET B . n 
B 1 104 ALA 104 89  89  ALA ALA B . n 
B 1 105 TYR 105 90  90  TYR TYR B . n 
B 1 106 VAL 106 91  91  VAL VAL B . n 
B 1 107 TRP 107 92  92  TRP TRP B . n 
B 1 108 GLY 108 93  93  GLY GLY B . n 
B 1 109 LYS 109 94  94  LYS LYS B . n 
B 1 110 GLY 110 95  95  GLY GLY B . n 
B 1 111 HIS 111 96  96  HIS HIS B . n 
B 1 112 GLY 112 97  97  GLY GLY B . n 
B 1 113 ASP 113 98  98  ASP ASP B . n 
B 1 114 VAL 114 99  99  VAL VAL B . n 
B 1 115 ARG 115 100 100 ARG ARG B . n 
B 1 116 LYS 116 101 101 LYS LYS B . n 
B 1 117 VAL 117 102 102 VAL VAL B . n 
B 1 118 LEU 118 103 103 LEU LEU B . n 
B 1 119 PRO 119 104 104 PRO PRO B . n 
B 1 120 ARG 120 105 105 ARG ARG B . n 
B 1 121 ASN 121 106 106 ASN ASN B . n 
B 1 122 ILE 122 107 107 ILE ILE B . n 
B 1 123 ALA 123 108 108 ALA ALA B . n 
B 1 124 VAL 124 109 109 VAL VAL B . n 
B 1 125 PRO 125 110 110 PRO PRO B . n 
B 1 126 TYR 126 111 111 TYR TYR B . n 
B 1 127 CYS 127 112 112 CYS CYS B . n 
B 1 128 GLN 128 113 113 GLN GLN B . n 
B 1 129 LEU 129 114 114 LEU LEU B . n 
B 1 130 SER 130 115 115 SER SER B . n 
B 1 131 LYS 131 116 116 LYS LYS B . n 
B 1 132 LYS 132 117 117 LYS LYS B . n 
B 1 133 LEU 133 118 118 LEU LEU B . n 
B 1 134 GLU 134 119 119 GLU GLU B . n 
B 1 135 LEU 135 120 120 LEU LEU B . n 
B 1 136 PRO 136 121 121 PRO PRO B . n 
B 1 137 PRO 137 122 122 PRO PRO B . n 
B 1 138 ILE 138 123 123 ILE ILE B . n 
B 1 139 LEU 139 124 124 LEU LEU B . n 
B 1 140 VAL 140 125 125 VAL VAL B . n 
B 1 141 TYR 141 126 126 TYR TYR B . n 
B 1 142 ALA 142 127 127 ALA ALA B . n 
B 1 143 ASP 143 128 128 ASP ASP B . n 
B 1 144 CYS 144 129 129 CYS CYS B . n 
B 1 145 VAL 145 130 130 VAL VAL B . n 
B 1 146 LEU 146 131 131 LEU LEU B . n 
B 1 147 ALA 147 132 132 ALA ALA B . n 
B 1 148 ASN 148 133 133 ASN ASN B . n 
B 1 149 TRP 149 134 134 TRP TRP B . n 
B 1 150 LYS 150 135 135 LYS LYS B . n 
B 1 151 LYS 151 136 136 LYS LYS B . n 
B 1 152 LYS 152 137 137 LYS LYS B . n 
B 1 153 ASP 153 138 138 ASP ASP B . n 
B 1 154 PRO 154 139 139 PRO PRO B . n 
B 1 155 ASN 155 140 140 ASN ASN B . n 
B 1 156 LYS 156 141 141 LYS LYS B . n 
B 1 157 PRO 157 142 142 PRO PRO B . n 
B 1 158 LEU 158 143 143 LEU LEU B . n 
B 1 159 THR 159 144 144 THR THR B . n 
B 1 160 TYR 160 145 145 TYR TYR B . n 
B 1 161 GLU 161 146 146 GLU GLU B . n 
B 1 162 ASN 162 147 147 ASN ASN B . n 
B 1 163 MET 163 148 148 MET MET B . n 
B 1 164 ASP 164 149 149 ASP ASP B . n 
B 1 165 VAL 165 150 150 VAL VAL B . n 
B 1 166 LEU 166 151 151 LEU LEU B . n 
B 1 167 PHE 167 152 152 PHE PHE B . n 
B 1 168 SER 168 153 153 SER SER B . n 
B 1 169 PHE 169 154 154 PHE PHE B . n 
B 1 170 ARG 170 155 155 ARG ARG B . n 
B 1 171 ASP 171 156 156 ASP ASP B . n 
B 1 172 GLY 172 157 157 GLY GLY B . n 
B 1 173 ASP 173 158 158 ASP ASP B . n 
B 1 174 CYS 174 159 159 CYS CYS B . n 
B 1 175 SER 175 160 160 SER SER B . n 
B 1 176 LYS 176 161 161 LYS LYS B . n 
B 1 177 GLY 177 162 162 GLY GLY B . n 
B 1 178 PHE 178 163 163 PHE PHE B . n 
B 1 179 PHE 179 164 164 PHE PHE B . n 
B 1 180 LEU 180 165 165 LEU LEU B . n 
B 1 181 VAL 181 166 166 VAL VAL B . n 
B 1 182 SER 182 167 167 SER SER B . n 
B 1 183 LEU 183 168 168 LEU LEU B . n 
B 1 184 LEU 184 169 169 LEU LEU B . n 
B 1 185 VAL 185 170 170 VAL VAL B . n 
B 1 186 GLU 186 171 171 GLU GLU B . n 
B 1 187 ILE 187 172 172 ILE ILE B . n 
B 1 188 ALA 188 173 173 ALA ALA B . n 
B 1 189 ALA 189 174 174 ALA ALA B . n 
B 1 190 ALA 190 175 175 ALA ALA B . n 
B 1 191 SER 191 176 176 SER SER B . n 
B 1 192 ALA 192 177 177 ALA ALA B . n 
B 1 193 ILE 193 178 178 ILE ILE B . n 
B 1 194 LYS 194 179 179 LYS LYS B . n 
B 1 195 VAL 195 180 180 VAL VAL B . n 
B 1 196 ILE 196 181 181 ILE ILE B . n 
B 1 197 PRO 197 182 182 PRO PRO B . n 
B 1 198 THR 198 183 183 THR THR B . n 
B 1 199 VAL 199 184 184 VAL VAL B . n 
B 1 200 PHE 200 185 185 PHE PHE B . n 
B 1 201 LYS 201 186 186 LYS LYS B . n 
B 1 202 ALA 202 187 187 ALA ALA B . n 
B 1 203 MET 203 188 188 MET MET B . n 
B 1 204 GLN 204 189 189 GLN GLN B . n 
B 1 205 MET 205 190 190 MET MET B . n 
B 1 206 GLN 206 191 191 GLN GLN B . n 
B 1 207 GLU 207 192 192 GLU GLU B . n 
B 1 208 ARG 208 193 193 ARG ARG B . n 
B 1 209 ASP 209 194 194 ASP ASP B . n 
B 1 210 THR 210 195 195 THR THR B . n 
B 1 211 LEU 211 196 196 LEU LEU B . n 
B 1 212 LEU 212 197 197 LEU LEU B . n 
B 1 213 LYS 213 198 198 LYS LYS B . n 
B 1 214 ALA 214 199 199 ALA ALA B . n 
B 1 215 LEU 215 200 200 LEU LEU B . n 
B 1 216 LEU 216 201 201 LEU LEU B . n 
B 1 217 GLU 217 202 202 GLU GLU B . n 
B 1 218 ILE 218 203 203 ILE ILE B . n 
B 1 219 ALA 219 204 204 ALA ALA B . n 
B 1 220 SER 220 205 205 SER SER B . n 
B 1 221 CYS 221 206 206 CYS CYS B . n 
B 1 222 LEU 222 207 207 LEU LEU B . n 
B 1 223 GLU 223 208 208 GLU GLU B . n 
B 1 224 LYS 224 209 209 LYS LYS B . n 
B 1 225 ALA 225 210 210 ALA ALA B . n 
B 1 226 LEU 226 211 211 LEU LEU B . n 
B 1 227 GLN 227 212 212 GLN GLN B . n 
B 1 228 VAL 228 213 213 VAL VAL B . n 
B 1 229 PHE 229 214 214 PHE PHE B . n 
B 1 230 HIS 230 215 215 HIS HIS B . n 
B 1 231 GLN 231 216 216 GLN GLN B . n 
B 1 232 ILE 232 217 217 ILE ILE B . n 
B 1 233 HIS 233 218 218 HIS HIS B . n 
B 1 234 ASP 234 219 219 ASP ASP B . n 
B 1 235 HIS 235 220 220 HIS HIS B . n 
B 1 236 VAL 236 221 221 VAL VAL B . n 
B 1 237 ASN 237 222 222 ASN ASN B . n 
B 1 238 PRO 238 223 223 PRO PRO B . n 
B 1 239 LYS 239 224 224 LYS LYS B . n 
B 1 240 ALA 240 225 225 ALA ALA B . n 
B 1 241 PHE 241 226 226 PHE PHE B . n 
B 1 242 PHE 242 227 227 PHE PHE B . n 
B 1 243 SER 243 228 228 SER SER B . n 
B 1 244 VAL 244 229 229 VAL VAL B . n 
B 1 245 LEU 245 230 230 LEU LEU B . n 
B 1 246 ARG 246 231 231 ARG ARG B . n 
B 1 247 ILE 247 232 232 ILE ILE B . n 
B 1 248 TYR 248 233 233 TYR TYR B . n 
B 1 249 LEU 249 234 234 LEU LEU B . n 
B 1 250 SER 250 235 235 SER SER B . n 
B 1 251 GLY 251 236 236 GLY GLY B . n 
B 1 252 TRP 252 237 237 TRP TRP B . n 
B 1 253 LYS 253 238 238 LYS LYS B . n 
B 1 254 GLY 254 239 239 GLY GLY B . n 
B 1 255 ASN 255 240 240 ASN ASN B . n 
B 1 256 PRO 256 241 241 PRO PRO B . n 
B 1 257 GLN 257 242 242 GLN GLN B . n 
B 1 258 LEU 258 243 243 LEU LEU B . n 
B 1 259 SER 259 244 244 SER SER B . n 
B 1 260 ASP 260 245 245 ASP ASP B . n 
B 1 261 GLY 261 246 246 GLY GLY B . n 
B 1 262 LEU 262 247 247 LEU LEU B . n 
B 1 263 VAL 263 248 248 VAL VAL B . n 
B 1 264 TYR 264 249 249 TYR TYR B . n 
B 1 265 GLU 265 250 250 GLU GLU B . n 
B 1 266 GLY 266 251 251 GLY GLY B . n 
B 1 267 PHE 267 252 252 PHE PHE B . n 
B 1 268 TRP 268 253 253 TRP TRP B . n 
B 1 269 GLU 269 254 254 GLU GLU B . n 
B 1 270 ASP 270 255 255 ASP ASP B . n 
B 1 271 PRO 271 256 256 PRO PRO B . n 
B 1 272 LYS 272 257 257 LYS LYS B . n 
B 1 273 GLU 273 258 258 GLU GLU B . n 
B 1 274 PHE 274 259 259 PHE PHE B . n 
B 1 275 ALA 275 260 260 ALA ALA B . n 
B 1 276 GLY 276 261 261 GLY GLY B . n 
B 1 277 GLY 277 262 262 GLY GLY B . n 
B 1 278 SER 278 263 263 SER SER B . n 
B 1 279 ALA 279 264 264 ALA ALA B . n 
B 1 280 GLY 280 265 265 GLY GLY B . n 
B 1 281 GLN 281 266 266 GLN GLN B . n 
B 1 282 SER 282 267 267 SER SER B . n 
B 1 283 SER 283 268 268 SER SER B . n 
B 1 284 VAL 284 269 269 VAL VAL B . n 
B 1 285 PHE 285 270 270 PHE PHE B . n 
B 1 286 GLN 286 271 271 GLN GLN B . n 
B 1 287 CYS 287 272 272 CYS CYS B . n 
B 1 288 PHE 288 273 273 PHE PHE B . n 
B 1 289 ASP 289 274 274 ASP ASP B . n 
B 1 290 VAL 290 275 275 VAL VAL B . n 
B 1 291 LEU 291 276 276 LEU LEU B . n 
B 1 292 LEU 292 277 277 LEU LEU B . n 
B 1 293 GLY 293 278 278 GLY GLY B . n 
B 1 294 ILE 294 279 279 ILE ILE B . n 
B 1 295 GLN 295 280 280 GLN GLN B . n 
B 1 296 GLN 296 281 281 GLN GLN B . n 
B 1 297 THR 297 282 282 THR THR B . n 
B 1 298 ALA 298 283 283 ALA ALA B . n 
B 1 299 GLY 299 284 284 GLY GLY B . n 
B 1 300 GLY 300 285 285 GLY GLY B . n 
B 1 301 GLY 301 286 286 GLY GLY B . n 
B 1 302 HIS 302 287 287 HIS HIS B . n 
B 1 303 ALA 303 288 288 ALA ALA B . n 
B 1 304 ALA 304 289 289 ALA ALA B . n 
B 1 305 GLN 305 290 290 GLN GLN B . n 
B 1 306 PHE 306 291 291 PHE PHE B . n 
B 1 307 LEU 307 292 292 LEU LEU B . n 
B 1 308 GLN 308 293 293 GLN GLN B . n 
B 1 309 ASP 309 294 294 ASP ASP B . n 
B 1 310 MET 310 295 295 MET MET B . n 
B 1 311 ARG 311 296 296 ARG ARG B . n 
B 1 312 ARG 312 297 297 ARG ARG B . n 
B 1 313 TYR 313 298 298 TYR TYR B . n 
B 1 314 MET 314 299 299 MET MET B . n 
B 1 315 PRO 315 300 300 PRO PRO B . n 
B 1 316 PRO 316 301 301 PRO PRO B . n 
B 1 317 ALA 317 302 302 ALA ALA B . n 
B 1 318 HIS 318 303 303 HIS HIS B . n 
B 1 319 ARG 319 304 304 ARG ARG B . n 
B 1 320 ASN 320 305 305 ASN ASN B . n 
B 1 321 PHE 321 306 306 PHE PHE B . n 
B 1 322 LEU 322 307 307 LEU LEU B . n 
B 1 323 CYS 323 308 308 CYS CYS B . n 
B 1 324 SER 324 309 309 SER SER B . n 
B 1 325 LEU 325 310 310 LEU LEU B . n 
B 1 326 GLU 326 311 311 GLU GLU B . n 
B 1 327 SER 327 312 312 SER SER B . n 
B 1 328 ASN 328 313 313 ASN ASN B . n 
B 1 329 PRO 329 314 314 PRO PRO B . n 
B 1 330 SER 330 315 315 SER SER B . n 
B 1 331 VAL 331 316 316 VAL VAL B . n 
B 1 332 ARG 332 317 317 ARG ARG B . n 
B 1 333 GLU 333 318 318 GLU GLU B . n 
B 1 334 PHE 334 319 319 PHE PHE B . n 
B 1 335 VAL 335 320 320 VAL VAL B . n 
B 1 336 LEU 336 321 321 LEU LEU B . n 
B 1 337 SER 337 322 322 SER SER B . n 
B 1 338 LYS 338 323 323 LYS LYS B . n 
B 1 339 GLY 339 324 324 GLY GLY B . n 
B 1 340 ASP 340 325 325 ASP ASP B . n 
B 1 341 ALA 341 326 326 ALA ALA B . n 
B 1 342 GLY 342 327 327 GLY GLY B . n 
B 1 343 LEU 343 328 328 LEU LEU B . n 
B 1 344 ARG 344 329 329 ARG ARG B . n 
B 1 345 GLU 345 330 330 GLU GLU B . n 
B 1 346 ALA 346 331 331 ALA ALA B . n 
B 1 347 TYR 347 332 332 TYR TYR B . n 
B 1 348 ASP 348 333 333 ASP ASP B . n 
B 1 349 ALA 349 334 334 ALA ALA B . n 
B 1 350 CYS 350 335 335 CYS CYS B . n 
B 1 351 VAL 351 336 336 VAL VAL B . n 
B 1 352 LYS 352 337 337 LYS LYS B . n 
B 1 353 ALA 353 338 338 ALA ALA B . n 
B 1 354 LEU 354 339 339 LEU LEU B . n 
B 1 355 VAL 355 340 340 VAL VAL B . n 
B 1 356 SER 356 341 341 SER SER B . n 
B 1 357 LEU 357 342 342 LEU LEU B . n 
B 1 358 ARG 358 343 343 ARG ARG B . n 
B 1 359 SER 359 344 344 SER SER B . n 
B 1 360 TYR 360 345 345 TYR TYR B . n 
B 1 361 HIS 361 346 346 HIS HIS B . n 
B 1 362 LEU 362 347 347 LEU LEU B . n 
B 1 363 GLN 363 348 348 GLN GLN B . n 
B 1 364 ILE 364 349 349 ILE ILE B . n 
B 1 365 VAL 365 350 350 VAL VAL B . n 
B 1 366 THR 366 351 351 THR THR B . n 
B 1 367 LYS 367 352 352 LYS LYS B . n 
B 1 368 TYR 368 353 353 TYR TYR B . n 
B 1 369 ILE 369 354 354 ILE ILE B . n 
B 1 370 LEU 370 355 355 LEU LEU B . n 
B 1 371 ILE 371 356 356 ILE ILE B . n 
B 1 372 PRO 372 357 357 PRO PRO B . n 
B 1 373 ALA 373 358 358 ALA ALA B . n 
B 1 374 SER 374 359 359 SER SER B . n 
B 1 375 GLN 375 360 360 GLN GLN B . n 
B 1 376 GLN 376 361 ?   ?   ?   B . n 
B 1 377 PRO 377 362 ?   ?   ?   B . n 
B 1 378 LYS 378 363 ?   ?   ?   B . n 
B 1 379 GLU 379 364 ?   ?   ?   B . n 
B 1 380 ASN 380 365 ?   ?   ?   B . n 
B 1 381 LYS 381 366 ?   ?   ?   B . n 
B 1 382 THR 382 367 ?   ?   ?   B . n 
B 1 383 SER 383 368 ?   ?   ?   B . n 
B 1 384 GLU 384 369 ?   ?   ?   B . n 
B 1 385 ASP 385 370 ?   ?   ?   B . n 
B 1 386 PRO 386 371 ?   ?   ?   B . n 
B 1 387 SER 387 372 ?   ?   ?   B . n 
B 1 388 LYS 388 373 ?   ?   ?   B . n 
B 1 389 LEU 389 374 ?   ?   ?   B . n 
B 1 390 GLU 390 375 ?   ?   ?   B . n 
B 1 391 ALA 391 376 ?   ?   ?   B . n 
B 1 392 LYS 392 377 ?   ?   ?   B . n 
B 1 393 GLY 393 378 ?   ?   ?   B . n 
B 1 394 THR 394 379 ?   ?   ?   B . n 
B 1 395 GLY 395 380 ?   ?   ?   B . n 
B 1 396 GLY 396 381 381 GLY GLY B . n 
B 1 397 THR 397 382 382 THR THR B . n 
B 1 398 ASP 398 383 383 ASP ASP B . n 
B 1 399 LEU 399 384 384 LEU LEU B . n 
B 1 400 MET 400 385 385 MET MET B . n 
B 1 401 ASN 401 386 386 ASN ASN B . n 
B 1 402 PHE 402 387 387 PHE PHE B . n 
B 1 403 LEU 403 388 388 LEU LEU B . n 
B 1 404 LYS 404 389 389 LYS LYS B . n 
B 1 405 THR 405 390 390 THR THR B . n 
B 1 406 VAL 406 391 391 VAL VAL B . n 
B 1 407 ARG 407 392 392 ARG ARG B . n 
B 1 408 SER 408 393 393 SER SER B . n 
B 1 409 THR 409 394 394 THR THR B . n 
B 1 410 THR 410 395 395 THR THR B . n 
B 1 411 GLU 411 396 396 GLU GLU B . n 
B 1 412 LYS 412 397 397 LYS LYS B . n 
B 1 413 SER 413 398 398 SER SER B . n 
B 1 414 LEU 414 399 399 LEU LEU B . n 
B 1 415 LEU 415 400 400 LEU LEU B . n 
B 1 416 LYS 416 401 401 LYS LYS B . n 
B 1 417 GLU 417 402 ?   ?   ?   B . n 
B 1 418 GLY 418 403 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1H6V 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1H6V 
_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 HEM   1  501 501 HEM   HEM A . 
D 3 A1H6V 1  502 2   A1H6V LIG A . 
E 2 HEM   1  501 501 HEM   HEM B . 
F 3 A1H6V 1  502 1   A1H6V LIG B . 
G 4 HOH   1  601 26  HOH   HOH A . 
G 4 HOH   2  602 1   HOH   HOH A . 
G 4 HOH   3  603 28  HOH   HOH A . 
G 4 HOH   4  604 5   HOH   HOH A . 
G 4 HOH   5  605 35  HOH   HOH A . 
G 4 HOH   6  606 42  HOH   HOH A . 
G 4 HOH   7  607 11  HOH   HOH A . 
G 4 HOH   8  608 21  HOH   HOH A . 
G 4 HOH   9  609 22  HOH   HOH A . 
G 4 HOH   10 610 4   HOH   HOH A . 
G 4 HOH   11 611 32  HOH   HOH A . 
G 4 HOH   12 612 14  HOH   HOH A . 
G 4 HOH   13 613 13  HOH   HOH A . 
H 4 HOH   1  601 25  HOH   HOH B . 
H 4 HOH   2  602 10  HOH   HOH B . 
H 4 HOH   3  603 2   HOH   HOH B . 
H 4 HOH   4  604 8   HOH   HOH B . 
H 4 HOH   5  605 27  HOH   HOH B . 
H 4 HOH   6  606 34  HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A GLU 0   ? CG  ? A GLU 15  CG  
2   1 Y 1 A GLU 0   ? CD  ? A GLU 15  CD  
3   1 Y 1 A GLU 0   ? OE1 ? A GLU 15  OE1 
4   1 Y 1 A GLU 0   ? OE2 ? A GLU 15  OE2 
5   1 Y 1 A GLN 4   ? CG  ? A GLN 19  CG  
6   1 Y 1 A GLN 4   ? CD  ? A GLN 19  CD  
7   1 Y 1 A GLN 4   ? OE1 ? A GLN 19  OE1 
8   1 Y 1 A GLN 4   ? NE2 ? A GLN 19  NE2 
9   1 Y 1 A LYS 13  ? CG  ? A LYS 28  CG  
10  1 Y 1 A LYS 13  ? CD  ? A LYS 28  CD  
11  1 Y 1 A LYS 13  ? CE  ? A LYS 28  CE  
12  1 Y 1 A LYS 13  ? NZ  ? A LYS 28  NZ  
13  1 Y 1 A GLU 14  ? CG  ? A GLU 29  CG  
14  1 Y 1 A GLU 14  ? CD  ? A GLU 29  CD  
15  1 Y 1 A GLU 14  ? OE1 ? A GLU 29  OE1 
16  1 Y 1 A GLU 14  ? OE2 ? A GLU 29  OE2 
17  1 Y 1 A GLU 19  ? CG  ? A GLU 34  CG  
18  1 Y 1 A GLU 19  ? CD  ? A GLU 34  CD  
19  1 Y 1 A GLU 19  ? OE1 ? A GLU 34  OE1 
20  1 Y 1 A GLU 19  ? OE2 ? A GLU 34  OE2 
21  1 Y 1 A LYS 44  ? CG  ? A LYS 59  CG  
22  1 Y 1 A LYS 44  ? CD  ? A LYS 59  CD  
23  1 Y 1 A LYS 44  ? CE  ? A LYS 59  CE  
24  1 Y 1 A LYS 44  ? NZ  ? A LYS 59  NZ  
25  1 Y 1 A SER 52  ? OG  ? A SER 67  OG  
26  1 Y 1 A LYS 61  ? CG  ? A LYS 76  CG  
27  1 Y 1 A LYS 61  ? CD  ? A LYS 76  CD  
28  1 Y 1 A LYS 61  ? CE  ? A LYS 76  CE  
29  1 Y 1 A LYS 61  ? NZ  ? A LYS 76  NZ  
30  1 Y 1 A SER 66  ? OG  ? A SER 81  OG  
31  1 Y 1 A LYS 101 ? CG  ? A LYS 116 CG  
32  1 Y 1 A LYS 101 ? CD  ? A LYS 116 CD  
33  1 Y 1 A LYS 101 ? CE  ? A LYS 116 CE  
34  1 Y 1 A LYS 101 ? NZ  ? A LYS 116 NZ  
35  1 Y 1 A LYS 116 ? CG  ? A LYS 131 CG  
36  1 Y 1 A LYS 116 ? CD  ? A LYS 131 CD  
37  1 Y 1 A LYS 116 ? CE  ? A LYS 131 CE  
38  1 Y 1 A LYS 116 ? NZ  ? A LYS 131 NZ  
39  1 Y 1 A LYS 117 ? CG  ? A LYS 132 CG  
40  1 Y 1 A LYS 117 ? CD  ? A LYS 132 CD  
41  1 Y 1 A LYS 117 ? CE  ? A LYS 132 CE  
42  1 Y 1 A LYS 117 ? NZ  ? A LYS 132 NZ  
43  1 Y 1 A LYS 141 ? CG  ? A LYS 156 CG  
44  1 Y 1 A LYS 141 ? CD  ? A LYS 156 CD  
45  1 Y 1 A LYS 141 ? CE  ? A LYS 156 CE  
46  1 Y 1 A LYS 141 ? NZ  ? A LYS 156 NZ  
47  1 Y 1 A SER 160 ? OG  ? A SER 175 OG  
48  1 Y 1 A LYS 186 ? CG  ? A LYS 201 CG  
49  1 Y 1 A LYS 186 ? CD  ? A LYS 201 CD  
50  1 Y 1 A LYS 186 ? CE  ? A LYS 201 CE  
51  1 Y 1 A LYS 186 ? NZ  ? A LYS 201 NZ  
52  1 Y 1 A LYS 198 ? CG  ? A LYS 213 CG  
53  1 Y 1 A LYS 198 ? CD  ? A LYS 213 CD  
54  1 Y 1 A LYS 198 ? CE  ? A LYS 213 CE  
55  1 Y 1 A LYS 198 ? NZ  ? A LYS 213 NZ  
56  1 Y 1 A LYS 209 ? CG  ? A LYS 224 CG  
57  1 Y 1 A LYS 209 ? CD  ? A LYS 224 CD  
58  1 Y 1 A LYS 209 ? CE  ? A LYS 224 CE  
59  1 Y 1 A LYS 209 ? NZ  ? A LYS 224 NZ  
60  1 Y 1 A LYS 224 ? CG  ? A LYS 239 CG  
61  1 Y 1 A LYS 224 ? CD  ? A LYS 239 CD  
62  1 Y 1 A LYS 224 ? CE  ? A LYS 239 CE  
63  1 Y 1 A LYS 224 ? NZ  ? A LYS 239 NZ  
64  1 Y 1 A LYS 257 ? CG  ? A LYS 272 CG  
65  1 Y 1 A LYS 257 ? CD  ? A LYS 272 CD  
66  1 Y 1 A LYS 257 ? CE  ? A LYS 272 CE  
67  1 Y 1 A LYS 257 ? NZ  ? A LYS 272 NZ  
68  1 Y 1 A ARG 297 ? CG  ? A ARG 312 CG  
69  1 Y 1 A ARG 297 ? CD  ? A ARG 312 CD  
70  1 Y 1 A ARG 297 ? NE  ? A ARG 312 NE  
71  1 Y 1 A ARG 297 ? CZ  ? A ARG 312 CZ  
72  1 Y 1 A ARG 297 ? NH1 ? A ARG 312 NH1 
73  1 Y 1 A ARG 297 ? NH2 ? A ARG 312 NH2 
74  1 Y 1 A ASN 305 ? CG  ? A ASN 320 CG  
75  1 Y 1 A ASN 305 ? OD1 ? A ASN 320 OD1 
76  1 Y 1 A ASN 305 ? ND2 ? A ASN 320 ND2 
77  1 Y 1 A GLU 318 ? CG  ? A GLU 333 CG  
78  1 Y 1 A GLU 318 ? CD  ? A GLU 333 CD  
79  1 Y 1 A GLU 318 ? OE1 ? A GLU 333 OE1 
80  1 Y 1 A GLU 318 ? OE2 ? A GLU 333 OE2 
81  1 Y 1 A GLU 330 ? CG  ? A GLU 345 CG  
82  1 Y 1 A GLU 330 ? CD  ? A GLU 345 CD  
83  1 Y 1 A GLU 330 ? OE1 ? A GLU 345 OE1 
84  1 Y 1 A GLU 330 ? OE2 ? A GLU 345 OE2 
85  1 Y 1 A LYS 337 ? CG  ? A LYS 352 CG  
86  1 Y 1 A LYS 337 ? CD  ? A LYS 352 CD  
87  1 Y 1 A LYS 337 ? CE  ? A LYS 352 CE  
88  1 Y 1 A LYS 337 ? NZ  ? A LYS 352 NZ  
89  1 Y 1 A LYS 401 ? CG  ? A LYS 416 CG  
90  1 Y 1 A LYS 401 ? CD  ? A LYS 416 CD  
91  1 Y 1 A LYS 401 ? CE  ? A LYS 416 CE  
92  1 Y 1 A LYS 401 ? NZ  ? A LYS 416 NZ  
93  1 Y 1 B LYS 13  ? CD  ? B LYS 28  CD  
94  1 Y 1 B LYS 13  ? CE  ? B LYS 28  CE  
95  1 Y 1 B LYS 13  ? NZ  ? B LYS 28  NZ  
96  1 Y 1 B GLU 19  ? CG  ? B GLU 34  CG  
97  1 Y 1 B GLU 19  ? CD  ? B GLU 34  CD  
98  1 Y 1 B GLU 19  ? OE1 ? B GLU 34  OE1 
99  1 Y 1 B GLU 19  ? OE2 ? B GLU 34  OE2 
100 1 Y 1 B LYS 44  ? CG  ? B LYS 59  CG  
101 1 Y 1 B LYS 44  ? CD  ? B LYS 59  CD  
102 1 Y 1 B LYS 44  ? CE  ? B LYS 59  CE  
103 1 Y 1 B LYS 44  ? NZ  ? B LYS 59  NZ  
104 1 Y 1 B ASP 48  ? CG  ? B ASP 63  CG  
105 1 Y 1 B ASP 48  ? OD1 ? B ASP 63  OD1 
106 1 Y 1 B ASP 48  ? OD2 ? B ASP 63  OD2 
107 1 Y 1 B LEU 49  ? CG  ? B LEU 64  CG  
108 1 Y 1 B LEU 49  ? CD1 ? B LEU 64  CD1 
109 1 Y 1 B LEU 49  ? CD2 ? B LEU 64  CD2 
110 1 Y 1 B GLN 54  ? CG  ? B GLN 69  CG  
111 1 Y 1 B GLN 54  ? CD  ? B GLN 69  CD  
112 1 Y 1 B GLN 54  ? OE1 ? B GLN 69  OE1 
113 1 Y 1 B GLN 54  ? NE2 ? B GLN 69  NE2 
114 1 Y 1 B GLU 57  ? CG  ? B GLU 72  CG  
115 1 Y 1 B GLU 57  ? CD  ? B GLU 72  CD  
116 1 Y 1 B GLU 57  ? OE1 ? B GLU 72  OE1 
117 1 Y 1 B GLU 57  ? OE2 ? B GLU 72  OE2 
118 1 Y 1 B LYS 61  ? CG  ? B LYS 76  CG  
119 1 Y 1 B LYS 61  ? CD  ? B LYS 76  CD  
120 1 Y 1 B LYS 61  ? CE  ? B LYS 76  CE  
121 1 Y 1 B LYS 61  ? NZ  ? B LYS 76  NZ  
122 1 Y 1 B SER 66  ? OG  ? B SER 81  OG  
123 1 Y 1 B ILE 67  ? CG1 ? B ILE 82  CG1 
124 1 Y 1 B ILE 67  ? CG2 ? B ILE 82  CG2 
125 1 Y 1 B ILE 67  ? CD1 ? B ILE 82  CD1 
126 1 Y 1 B ASP 68  ? CG  ? B ASP 83  CG  
127 1 Y 1 B ASP 68  ? OD1 ? B ASP 83  OD1 
128 1 Y 1 B ASP 68  ? OD2 ? B ASP 83  OD2 
129 1 Y 1 B THR 71  ? OG1 ? B THR 86  OG1 
130 1 Y 1 B THR 71  ? CG2 ? B THR 86  CG2 
131 1 Y 1 B SER 75  ? OG  ? B SER 90  OG  
132 1 Y 1 B LYS 94  ? CG  ? B LYS 109 CG  
133 1 Y 1 B LYS 94  ? CD  ? B LYS 109 CD  
134 1 Y 1 B LYS 94  ? CE  ? B LYS 109 CE  
135 1 Y 1 B LYS 94  ? NZ  ? B LYS 109 NZ  
136 1 Y 1 B HIS 96  ? CG  ? B HIS 111 CG  
137 1 Y 1 B HIS 96  ? ND1 ? B HIS 111 ND1 
138 1 Y 1 B HIS 96  ? CD2 ? B HIS 111 CD2 
139 1 Y 1 B HIS 96  ? CE1 ? B HIS 111 CE1 
140 1 Y 1 B HIS 96  ? NE2 ? B HIS 111 NE2 
141 1 Y 1 B ASP 98  ? CG  ? B ASP 113 CG  
142 1 Y 1 B ASP 98  ? OD1 ? B ASP 113 OD1 
143 1 Y 1 B ASP 98  ? OD2 ? B ASP 113 OD2 
144 1 Y 1 B VAL 99  ? CG1 ? B VAL 114 CG1 
145 1 Y 1 B VAL 99  ? CG2 ? B VAL 114 CG2 
146 1 Y 1 B ARG 100 ? CG  ? B ARG 115 CG  
147 1 Y 1 B ARG 100 ? CD  ? B ARG 115 CD  
148 1 Y 1 B ARG 100 ? NE  ? B ARG 115 NE  
149 1 Y 1 B ARG 100 ? CZ  ? B ARG 115 CZ  
150 1 Y 1 B ARG 100 ? NH1 ? B ARG 115 NH1 
151 1 Y 1 B ARG 100 ? NH2 ? B ARG 115 NH2 
152 1 Y 1 B LYS 101 ? CG  ? B LYS 116 CG  
153 1 Y 1 B LYS 101 ? CD  ? B LYS 116 CD  
154 1 Y 1 B LYS 101 ? CE  ? B LYS 116 CE  
155 1 Y 1 B LYS 101 ? NZ  ? B LYS 116 NZ  
156 1 Y 1 B VAL 102 ? CG1 ? B VAL 117 CG1 
157 1 Y 1 B VAL 102 ? CG2 ? B VAL 117 CG2 
158 1 Y 1 B ARG 105 ? CG  ? B ARG 120 CG  
159 1 Y 1 B ARG 105 ? CD  ? B ARG 120 CD  
160 1 Y 1 B ARG 105 ? NE  ? B ARG 120 NE  
161 1 Y 1 B ARG 105 ? CZ  ? B ARG 120 CZ  
162 1 Y 1 B ARG 105 ? NH1 ? B ARG 120 NH1 
163 1 Y 1 B ARG 105 ? NH2 ? B ARG 120 NH2 
164 1 Y 1 B ASN 106 ? CG  ? B ASN 121 CG  
165 1 Y 1 B ASN 106 ? OD1 ? B ASN 121 OD1 
166 1 Y 1 B ASN 106 ? ND2 ? B ASN 121 ND2 
167 1 Y 1 B VAL 109 ? CG1 ? B VAL 124 CG1 
168 1 Y 1 B VAL 109 ? CG2 ? B VAL 124 CG2 
169 1 Y 1 B GLN 113 ? CG  ? B GLN 128 CG  
170 1 Y 1 B GLN 113 ? CD  ? B GLN 128 CD  
171 1 Y 1 B GLN 113 ? OE1 ? B GLN 128 OE1 
172 1 Y 1 B GLN 113 ? NE2 ? B GLN 128 NE2 
173 1 Y 1 B LYS 116 ? CE  ? B LYS 131 CE  
174 1 Y 1 B LYS 116 ? NZ  ? B LYS 131 NZ  
175 1 Y 1 B LYS 117 ? CE  ? B LYS 132 CE  
176 1 Y 1 B LYS 117 ? NZ  ? B LYS 132 NZ  
177 1 Y 1 B LYS 135 ? CE  ? B LYS 150 CE  
178 1 Y 1 B LYS 135 ? NZ  ? B LYS 150 NZ  
179 1 Y 1 B ASN 140 ? CG  ? B ASN 155 CG  
180 1 Y 1 B ASN 140 ? OD1 ? B ASN 155 OD1 
181 1 Y 1 B ASN 140 ? ND2 ? B ASN 155 ND2 
182 1 Y 1 B LYS 141 ? CG  ? B LYS 156 CG  
183 1 Y 1 B LYS 141 ? CD  ? B LYS 156 CD  
184 1 Y 1 B LYS 141 ? CE  ? B LYS 156 CE  
185 1 Y 1 B LYS 141 ? NZ  ? B LYS 156 NZ  
186 1 Y 1 B GLU 146 ? CG  ? B GLU 161 CG  
187 1 Y 1 B GLU 146 ? CD  ? B GLU 161 CD  
188 1 Y 1 B GLU 146 ? OE1 ? B GLU 161 OE1 
189 1 Y 1 B GLU 146 ? OE2 ? B GLU 161 OE2 
190 1 Y 1 B SER 153 ? OG  ? B SER 168 OG  
191 1 Y 1 B ASP 156 ? CG  ? B ASP 171 CG  
192 1 Y 1 B ASP 156 ? OD1 ? B ASP 171 OD1 
193 1 Y 1 B ASP 156 ? OD2 ? B ASP 171 OD2 
194 1 Y 1 B SER 176 ? OG  ? B SER 191 OG  
195 1 Y 1 B LYS 186 ? CG  ? B LYS 201 CG  
196 1 Y 1 B LYS 186 ? CD  ? B LYS 201 CD  
197 1 Y 1 B LYS 186 ? CE  ? B LYS 201 CE  
198 1 Y 1 B LYS 186 ? NZ  ? B LYS 201 NZ  
199 1 Y 1 B GLN 189 ? CG  ? B GLN 204 CG  
200 1 Y 1 B GLN 189 ? CD  ? B GLN 204 CD  
201 1 Y 1 B GLN 189 ? OE1 ? B GLN 204 OE1 
202 1 Y 1 B GLN 189 ? NE2 ? B GLN 204 NE2 
203 1 Y 1 B LYS 198 ? CG  ? B LYS 213 CG  
204 1 Y 1 B LYS 198 ? CD  ? B LYS 213 CD  
205 1 Y 1 B LYS 198 ? CE  ? B LYS 213 CE  
206 1 Y 1 B LYS 198 ? NZ  ? B LYS 213 NZ  
207 1 Y 1 B LYS 209 ? CG  ? B LYS 224 CG  
208 1 Y 1 B LYS 209 ? CD  ? B LYS 224 CD  
209 1 Y 1 B LYS 209 ? CE  ? B LYS 224 CE  
210 1 Y 1 B LYS 209 ? NZ  ? B LYS 224 NZ  
211 1 Y 1 B GLN 212 ? CG  ? B GLN 227 CG  
212 1 Y 1 B GLN 212 ? CD  ? B GLN 227 CD  
213 1 Y 1 B GLN 212 ? OE1 ? B GLN 227 OE1 
214 1 Y 1 B GLN 212 ? NE2 ? B GLN 227 NE2 
215 1 Y 1 B ILE 217 ? CG1 ? B ILE 232 CG1 
216 1 Y 1 B ILE 217 ? CG2 ? B ILE 232 CG2 
217 1 Y 1 B ILE 217 ? CD1 ? B ILE 232 CD1 
218 1 Y 1 B HIS 218 ? CG  ? B HIS 233 CG  
219 1 Y 1 B HIS 218 ? ND1 ? B HIS 233 ND1 
220 1 Y 1 B HIS 218 ? CD2 ? B HIS 233 CD2 
221 1 Y 1 B HIS 218 ? CE1 ? B HIS 233 CE1 
222 1 Y 1 B HIS 218 ? NE2 ? B HIS 233 NE2 
223 1 Y 1 B VAL 221 ? CG1 ? B VAL 236 CG1 
224 1 Y 1 B VAL 221 ? CG2 ? B VAL 236 CG2 
225 1 Y 1 B LYS 224 ? CG  ? B LYS 239 CG  
226 1 Y 1 B LYS 224 ? CD  ? B LYS 239 CD  
227 1 Y 1 B LYS 224 ? CE  ? B LYS 239 CE  
228 1 Y 1 B LYS 224 ? NZ  ? B LYS 239 NZ  
229 1 Y 1 B SER 228 ? OG  ? B SER 243 OG  
230 1 Y 1 B VAL 229 ? CG1 ? B VAL 244 CG1 
231 1 Y 1 B VAL 229 ? CG2 ? B VAL 244 CG2 
232 1 Y 1 B SER 235 ? OG  ? B SER 250 OG  
233 1 Y 1 B LYS 238 ? CG  ? B LYS 253 CG  
234 1 Y 1 B LYS 238 ? CD  ? B LYS 253 CD  
235 1 Y 1 B LYS 238 ? CE  ? B LYS 253 CE  
236 1 Y 1 B LYS 238 ? NZ  ? B LYS 253 NZ  
237 1 Y 1 B SER 244 ? OG  ? B SER 259 OG  
238 1 Y 1 B ASP 245 ? CG  ? B ASP 260 CG  
239 1 Y 1 B ASP 245 ? OD1 ? B ASP 260 OD1 
240 1 Y 1 B ASP 245 ? OD2 ? B ASP 260 OD2 
241 1 Y 1 B GLU 254 ? CG  ? B GLU 269 CG  
242 1 Y 1 B GLU 254 ? CD  ? B GLU 269 CD  
243 1 Y 1 B GLU 254 ? OE1 ? B GLU 269 OE1 
244 1 Y 1 B GLU 254 ? OE2 ? B GLU 269 OE2 
245 1 Y 1 B ASP 255 ? CG  ? B ASP 270 CG  
246 1 Y 1 B ASP 255 ? OD1 ? B ASP 270 OD1 
247 1 Y 1 B ASP 255 ? OD2 ? B ASP 270 OD2 
248 1 Y 1 B LYS 257 ? CG  ? B LYS 272 CG  
249 1 Y 1 B LYS 257 ? CD  ? B LYS 272 CD  
250 1 Y 1 B LYS 257 ? CE  ? B LYS 272 CE  
251 1 Y 1 B LYS 257 ? NZ  ? B LYS 272 NZ  
252 1 Y 1 B HIS 287 ? CG  ? B HIS 302 CG  
253 1 Y 1 B HIS 287 ? ND1 ? B HIS 302 ND1 
254 1 Y 1 B HIS 287 ? CD2 ? B HIS 302 CD2 
255 1 Y 1 B HIS 287 ? CE1 ? B HIS 302 CE1 
256 1 Y 1 B HIS 287 ? NE2 ? B HIS 302 NE2 
257 1 Y 1 B GLN 293 ? CG  ? B GLN 308 CG  
258 1 Y 1 B GLN 293 ? CD  ? B GLN 308 CD  
259 1 Y 1 B GLN 293 ? OE1 ? B GLN 308 OE1 
260 1 Y 1 B GLN 293 ? NE2 ? B GLN 308 NE2 
261 1 Y 1 B ARG 297 ? CG  ? B ARG 312 CG  
262 1 Y 1 B ARG 297 ? CD  ? B ARG 312 CD  
263 1 Y 1 B ARG 297 ? NE  ? B ARG 312 NE  
264 1 Y 1 B ARG 297 ? CZ  ? B ARG 312 CZ  
265 1 Y 1 B ARG 297 ? NH1 ? B ARG 312 NH1 
266 1 Y 1 B ARG 297 ? NH2 ? B ARG 312 NH2 
267 1 Y 1 B GLU 318 ? CG  ? B GLU 333 CG  
268 1 Y 1 B GLU 318 ? CD  ? B GLU 333 CD  
269 1 Y 1 B GLU 318 ? OE1 ? B GLU 333 OE1 
270 1 Y 1 B GLU 318 ? OE2 ? B GLU 333 OE2 
271 1 Y 1 B GLU 330 ? CG  ? B GLU 345 CG  
272 1 Y 1 B GLU 330 ? CD  ? B GLU 345 CD  
273 1 Y 1 B GLU 330 ? OE1 ? B GLU 345 OE1 
274 1 Y 1 B GLU 330 ? OE2 ? B GLU 345 OE2 
275 1 Y 1 B LYS 337 ? CG  ? B LYS 352 CG  
276 1 Y 1 B LYS 337 ? CD  ? B LYS 352 CD  
277 1 Y 1 B LYS 337 ? CE  ? B LYS 352 CE  
278 1 Y 1 B LYS 337 ? NZ  ? B LYS 352 NZ  
279 1 Y 1 B GLN 360 ? CG  ? B GLN 375 CG  
280 1 Y 1 B GLN 360 ? CD  ? B GLN 375 CD  
281 1 Y 1 B GLN 360 ? OE1 ? B GLN 375 OE1 
282 1 Y 1 B GLN 360 ? NE2 ? B GLN 375 NE2 
283 1 Y 1 B THR 382 ? OG1 ? B THR 397 OG1 
284 1 Y 1 B THR 382 ? CG2 ? B THR 397 CG2 
285 1 Y 1 B SER 393 ? OG  ? B SER 408 OG  
286 1 Y 1 B GLU 396 ? CG  ? B GLU 411 CG  
287 1 Y 1 B GLU 396 ? CD  ? B GLU 411 CD  
288 1 Y 1 B GLU 396 ? OE1 ? B GLU 411 OE1 
289 1 Y 1 B GLU 396 ? OE2 ? B GLU 411 OE2 
290 1 Y 1 B LYS 397 ? CG  ? B LYS 412 CG  
291 1 Y 1 B LYS 397 ? CD  ? B LYS 412 CD  
292 1 Y 1 B LYS 397 ? CE  ? B LYS 412 CE  
293 1 Y 1 B LYS 397 ? NZ  ? B LYS 412 NZ  
294 1 Y 1 B LYS 401 ? CG  ? B LYS 416 CG  
295 1 Y 1 B LYS 401 ? CD  ? B LYS 416 CD  
296 1 Y 1 B LYS 401 ? CE  ? B LYS 416 CE  
297 1 Y 1 B LYS 401 ? NZ  ? B LYS 416 NZ  
# 
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   ? ? ? 2.11.8 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .      2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE   ? ? ? .      3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .      4 
# 
_cell.angle_alpha                  90 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9ESE 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     84.949 
_cell.length_a_esd                 ? 
_cell.length_b                     91.073 
_cell.length_b_esd                 ? 
_cell.length_c                     130.355 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9ESE 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9ESE 
_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             2.68 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.06 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '10% w/v PEG 4000, 20% v/v glycerol, 0.1 M MOPS/HEPES-Na pH 7.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 2M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2017-10-20 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.00 
_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                        'SLS BEAMLINE X06DA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.00 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06DA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9ESE 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.54 
_reflns.d_resolution_low                               45.54 
_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                                     64216 
_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                           99.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                .11 
_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                                   .99 
_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                                    2.54 
_reflns_shell.d_res_low                                     2.69 
_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                             10313 
_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                               1.54 
_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                                  .41 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          98.9 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.4216 
_refine.aniso_B[1][2]                            0 
_refine.aniso_B[1][3]                            0 
_refine.aniso_B[2][2]                            -0.1103 
_refine.aniso_B[2][3]                            0 
_refine.aniso_B[3][3]                            -0.3113 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               65.33 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.937 
_refine.correlation_coeff_Fo_to_Fc_free          0.91 
_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                                 9ESE 
_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                            2.539 
_refine.ls_d_res_low                             45.54 
_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                     33978 
_refine.ls_number_reflns_R_free                  1700 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.7 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2402 
_refine.ls_R_factor_R_free                       0.2762 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2384 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            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   0.291 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.284 
_refine.pdbx_overall_SU_R_Blow_DPI               0.436 
_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             0.453 
_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                        9ESE 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.4 
_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                       2.539 
_refine_hist.d_res_low                        45.54 
_refine_hist.number_atoms_solvent             19 
_refine_hist.number_atoms_total               5885 
_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        5726 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         140 
_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 ? 6029 ? t_bond_d                  2  HARMONIC     
'X-RAY DIFFRACTION' ? 0.82  ? 8233 ? t_angle_deg               2  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 1958 ? t_dihedral_angle_d        2  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? 1098 ? t_gen_planes              5  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 6029 ? t_it                      10 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 772  ? t_chiral_improper_torsion 5  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? 4694 ? t_ideal_dist_contact      4  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? 2.51  ? ?    ? t_omega_torsion           ?  ?            
'X-RAY DIFFRACTION' ? 17.35 ? ?    ? t_other_torsion           ?  ?            
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.54 
_refine_ls_shell.d_res_low                        2.56 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                680 
_refine_ls_shell.number_reflns_R_free             34 
_refine_ls_shell.number_reflns_R_work             ? 
_refine_ls_shell.percent_reflns_obs               95.87 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     0.3633 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.3612 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   ? 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.405 
# 
_struct.entry_id                     9ESE 
_struct.title                        'Holo IDO with a bound inhibitor' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9ESE 
_struct_keywords.text            'Inhibitor, heme, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    I23O1_HUMAN 
_struct_ref.pdbx_db_accession          P14902 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;WTISKEYHIDEEVGFALPNPQENLPDFYNDWMFIAKHLPDLIESGQLRERVEKLNMLSIDHLTDHKSQRLARLVLGCITM
AYVWGKGHGDVRKVLPRNIAVPYCQLSKKLELPPILVYADCVLANWKKKDPNKPLTYENMDVLFSFRDGDCSKGFFLVSL
LVEIAAASAIKVIPTVFKAMQMQERDTLLKALLEIASCLEKALQVFHQIHDHVNPKAFFSVLRIYLSGWKGNPQLSDGLV
YEGFWEDPKEFAGGSAGQSSVFQCFDVLLGIQQTAGGGHAAQFLQDMRRYMPPAHRNFLCSLESNPSVREFVLSKGDAGL
REAYDACVKALVSLRSYHLQIVTKYILIPASQQPKENKTSEDPSKLEAKGTGGTDLMNFLKTVRSTTEKSLLKEG
;
_struct_ref.pdbx_align_begin           9 
# 
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 9ESE A 24 ? 418 ? P14902 9 ? 403 ? 9 403 
2 1 9ESE B 24 ? 418 ? P14902 9 ? 403 ? 9 403 
# 
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 9ESE MET A 1  ? UNP P14902 ? ? 'initiating methionine' -14 1  
1 9ESE GLY A 2  ? UNP P14902 ? ? 'expression tag'        -13 2  
1 9ESE SER A 3  ? UNP P14902 ? ? 'expression tag'        -12 3  
1 9ESE SER A 4  ? UNP P14902 ? ? 'expression tag'        -11 4  
1 9ESE HIS A 5  ? UNP P14902 ? ? 'expression tag'        -10 5  
1 9ESE HIS A 6  ? UNP P14902 ? ? 'expression tag'        -9  6  
1 9ESE HIS A 7  ? UNP P14902 ? ? 'expression tag'        -8  7  
1 9ESE HIS A 8  ? UNP P14902 ? ? 'expression tag'        -7  8  
1 9ESE HIS A 9  ? UNP P14902 ? ? 'expression tag'        -6  9  
1 9ESE HIS A 10 ? UNP P14902 ? ? 'expression tag'        -5  10 
1 9ESE SER A 11 ? UNP P14902 ? ? 'expression tag'        -4  11 
1 9ESE ALA A 12 ? UNP P14902 ? ? 'expression tag'        -3  12 
1 9ESE ALA A 13 ? UNP P14902 ? ? 'expression tag'        -2  13 
1 9ESE LEU A 14 ? UNP P14902 ? ? 'expression tag'        -1  14 
1 9ESE GLU A 15 ? UNP P14902 ? ? 'expression tag'        0   15 
1 9ESE VAL A 16 ? UNP P14902 ? ? 'expression tag'        1   16 
1 9ESE LEU A 17 ? UNP P14902 ? ? 'expression tag'        2   17 
1 9ESE PHE A 18 ? UNP P14902 ? ? 'expression tag'        3   18 
1 9ESE GLN A 19 ? UNP P14902 ? ? 'expression tag'        4   19 
1 9ESE GLY A 20 ? UNP P14902 ? ? 'expression tag'        5   20 
1 9ESE PRO A 21 ? UNP P14902 ? ? 'expression tag'        6   21 
1 9ESE HIS A 22 ? UNP P14902 ? ? 'expression tag'        7   22 
1 9ESE MET A 23 ? UNP P14902 ? ? 'expression tag'        8   23 
2 9ESE MET B 1  ? UNP P14902 ? ? 'initiating methionine' -14 24 
2 9ESE GLY B 2  ? UNP P14902 ? ? 'expression tag'        -13 25 
2 9ESE SER B 3  ? UNP P14902 ? ? 'expression tag'        -12 26 
2 9ESE SER B 4  ? UNP P14902 ? ? 'expression tag'        -11 27 
2 9ESE HIS B 5  ? UNP P14902 ? ? 'expression tag'        -10 28 
2 9ESE HIS B 6  ? UNP P14902 ? ? 'expression tag'        -9  29 
2 9ESE HIS B 7  ? UNP P14902 ? ? 'expression tag'        -8  30 
2 9ESE HIS B 8  ? UNP P14902 ? ? 'expression tag'        -7  31 
2 9ESE HIS B 9  ? UNP P14902 ? ? 'expression tag'        -6  32 
2 9ESE HIS B 10 ? UNP P14902 ? ? 'expression tag'        -5  33 
2 9ESE SER B 11 ? UNP P14902 ? ? 'expression tag'        -4  34 
2 9ESE ALA B 12 ? UNP P14902 ? ? 'expression tag'        -3  35 
2 9ESE ALA B 13 ? UNP P14902 ? ? 'expression tag'        -2  36 
2 9ESE LEU B 14 ? UNP P14902 ? ? 'expression tag'        -1  37 
2 9ESE GLU B 15 ? UNP P14902 ? ? 'expression tag'        0   38 
2 9ESE VAL B 16 ? UNP P14902 ? ? 'expression tag'        1   39 
2 9ESE LEU B 17 ? UNP P14902 ? ? 'expression tag'        2   40 
2 9ESE PHE B 18 ? UNP P14902 ? ? 'expression tag'        3   41 
2 9ESE GLN B 19 ? UNP P14902 ? ? 'expression tag'        4   42 
2 9ESE GLY B 20 ? UNP P14902 ? ? 'expression tag'        5   43 
2 9ESE PRO B 21 ? UNP P14902 ? ? 'expression tag'        6   44 
2 9ESE HIS B 22 ? UNP P14902 ? ? 'expression tag'        7   45 
2 9ESE MET B 23 ? UNP P14902 ? ? 'expression tag'        8   46 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 4020  ? 
1 MORE         -56   ? 
1 'SSA (A^2)'  29410 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_pdbx_struct_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 ALA A 13  ? GLY A 20  ? ALA A -2  GLY A 5   1 ? 8  
HELX_P HELX_P2  AA2 SER A 27  ? HIS A 31  ? SER A 12  HIS A 16  5 ? 5  
HELX_P HELX_P3  AA3 PRO A 48  ? PHE A 50  ? PRO A 33  PHE A 35  5 ? 3  
HELX_P HELX_P4  AA4 TYR A 51  ? HIS A 60  ? TYR A 36  HIS A 45  1 ? 10 
HELX_P HELX_P5  AA5 HIS A 60  ? GLY A 68  ? HIS A 45  GLY A 53  1 ? 9  
HELX_P HELX_P6  AA6 GLN A 69  ? LYS A 76  ? GLN A 54  LYS A 61  1 ? 8  
HELX_P HELX_P7  AA7 SER A 81  ? LEU A 85  ? SER A 66  LEU A 70  5 ? 5  
HELX_P HELX_P8  AA8 ASP A 87  ? GLY A 108 ? ASP A 72  GLY A 93  1 ? 22 
HELX_P HELX_P9  AA9 PRO A 119 ? LEU A 133 ? PRO A 104 LEU A 118 1 ? 15 
HELX_P HELX_P10 AB1 VAL A 140 ? VAL A 145 ? VAL A 125 VAL A 130 1 ? 6  
HELX_P HELX_P11 AB2 THR A 159 ? GLU A 161 ? THR A 144 GLU A 146 5 ? 3  
HELX_P HELX_P12 AB3 CYS A 174 ? SER A 191 ? CYS A 159 SER A 176 1 ? 18 
HELX_P HELX_P13 AB4 ALA A 192 ? LYS A 194 ? ALA A 177 LYS A 179 5 ? 3  
HELX_P HELX_P14 AB5 VAL A 195 ? MET A 205 ? VAL A 180 MET A 190 1 ? 11 
HELX_P HELX_P15 AB6 GLU A 207 ? HIS A 230 ? GLU A 192 HIS A 215 1 ? 24 
HELX_P HELX_P16 AB7 GLN A 231 ? VAL A 236 ? GLN A 216 VAL A 221 1 ? 6  
HELX_P HELX_P17 AB8 ASN A 237 ? VAL A 244 ? ASN A 222 VAL A 229 1 ? 8  
HELX_P HELX_P18 AB9 VAL A 244 ? SER A 250 ? VAL A 229 SER A 235 1 ? 7  
HELX_P HELX_P19 AC1 ASN A 255 ? SER A 259 ? ASN A 240 SER A 244 5 ? 5  
HELX_P HELX_P20 AC2 SER A 278 ? GLN A 281 ? SER A 263 GLN A 266 5 ? 4  
HELX_P HELX_P21 AC3 SER A 282 ? LEU A 292 ? SER A 267 LEU A 277 1 ? 11 
HELX_P HELX_P22 AC4 GLY A 301 ? MET A 310 ? GLY A 286 MET A 295 1 ? 10 
HELX_P HELX_P23 AC5 ARG A 311 ? MET A 314 ? ARG A 296 MET A 299 5 ? 4  
HELX_P HELX_P24 AC6 PRO A 315 ? ASN A 328 ? PRO A 300 ASN A 313 1 ? 14 
HELX_P HELX_P25 AC7 SER A 330 ? SER A 337 ? SER A 315 SER A 322 1 ? 8  
HELX_P HELX_P26 AC8 ASP A 340 ? ILE A 369 ? ASP A 325 ILE A 354 1 ? 30 
HELX_P HELX_P27 AC9 ILE A 369 ? GLN A 375 ? ILE A 354 GLN A 360 1 ? 7  
HELX_P HELX_P28 AD1 ASP A 398 ? LYS A 412 ? ASP A 383 LYS A 397 1 ? 15 
HELX_P HELX_P29 AD2 SER B 27  ? HIS B 31  ? SER B 12  HIS B 16  5 ? 5  
HELX_P HELX_P30 AD3 PRO B 48  ? PHE B 50  ? PRO B 33  PHE B 35  5 ? 3  
HELX_P HELX_P31 AD4 TYR B 51  ? HIS B 60  ? TYR B 36  HIS B 45  1 ? 10 
HELX_P HELX_P32 AD5 HIS B 60  ? GLY B 68  ? HIS B 45  GLY B 53  1 ? 9  
HELX_P HELX_P33 AD6 GLN B 69  ? LYS B 76  ? GLN B 54  LYS B 61  1 ? 8  
HELX_P HELX_P34 AD7 SER B 81  ? LEU B 85  ? SER B 66  LEU B 70  5 ? 5  
HELX_P HELX_P35 AD8 ASP B 87  ? GLY B 108 ? ASP B 72  GLY B 93  1 ? 22 
HELX_P HELX_P36 AD9 PRO B 119 ? LEU B 133 ? PRO B 104 LEU B 118 1 ? 15 
HELX_P HELX_P37 AE1 VAL B 140 ? VAL B 145 ? VAL B 125 VAL B 130 1 ? 6  
HELX_P HELX_P38 AE2 THR B 159 ? GLU B 161 ? THR B 144 GLU B 146 5 ? 3  
HELX_P HELX_P39 AE3 CYS B 174 ? SER B 191 ? CYS B 159 SER B 176 1 ? 18 
HELX_P HELX_P40 AE4 ALA B 192 ? LYS B 194 ? ALA B 177 LYS B 179 5 ? 3  
HELX_P HELX_P41 AE5 VAL B 195 ? MET B 205 ? VAL B 180 MET B 190 1 ? 11 
HELX_P HELX_P42 AE6 GLU B 207 ? HIS B 230 ? GLU B 192 HIS B 215 1 ? 24 
HELX_P HELX_P43 AE7 GLN B 231 ? VAL B 236 ? GLN B 216 VAL B 221 1 ? 6  
HELX_P HELX_P44 AE8 ASN B 237 ? VAL B 244 ? ASN B 222 VAL B 229 1 ? 8  
HELX_P HELX_P45 AE9 VAL B 244 ? SER B 250 ? VAL B 229 SER B 235 1 ? 7  
HELX_P HELX_P46 AF1 ASN B 255 ? SER B 259 ? ASN B 240 SER B 244 5 ? 5  
HELX_P HELX_P47 AF2 SER B 278 ? GLN B 281 ? SER B 263 GLN B 266 5 ? 4  
HELX_P HELX_P48 AF3 SER B 282 ? LEU B 292 ? SER B 267 LEU B 277 1 ? 11 
HELX_P HELX_P49 AF4 GLY B 301 ? MET B 310 ? GLY B 286 MET B 295 1 ? 10 
HELX_P HELX_P50 AF5 ARG B 311 ? MET B 314 ? ARG B 296 MET B 299 5 ? 4  
HELX_P HELX_P51 AF6 PRO B 315 ? ASN B 328 ? PRO B 300 ASN B 313 1 ? 14 
HELX_P HELX_P52 AF7 SER B 330 ? SER B 337 ? SER B 315 SER B 322 1 ? 8  
HELX_P HELX_P53 AF8 ASP B 340 ? ILE B 369 ? ASP B 325 ILE B 354 1 ? 30 
HELX_P HELX_P54 AF9 ILE B 369 ? GLN B 375 ? ILE B 354 GLN B 360 1 ? 7  
HELX_P HELX_P55 AG1 THR B 397 ? LYS B 412 ? THR B 382 LYS B 397 1 ? 16 
# 
_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 
disulf1 disulf ? ? A CYS 323 SG  ? ? ? 1_555 B CYS   323 SG ? ? A CYS 308 B CYS   308 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
metalc1 metalc ? ? A HIS 361 NE2 ? ? ? 1_555 C HEM   .   FE ? ? A HIS 346 A HEM   501 1_555 ? ? ? ? ? ? ? 2.006 ? ? 
metalc2 metalc ? ? C HEM .   FE  ? ? ? 1_555 D A1H6V .   N4 ? ? A HEM 501 A A1H6V 502 1_555 ? ? ? ? ? ? ? 1.884 ? ? 
metalc3 metalc ? ? B HIS 361 NE2 ? ? ? 1_555 E HEM   .   FE ? ? B HIS 346 B HEM   501 1_555 ? ? ? ? ? ? ? 2.058 ? ? 
metalc4 metalc ? ? E HEM .   FE  ? ? ? 1_555 F A1H6V .   N4 ? ? B HEM 501 B A1H6V 502 1_555 ? ? ? ? ? ? ? 1.874 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
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 361 ? A HIS 346 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NA ? C HEM   . ? A HEM   501 ? 1_555 88.5  ? 
2  NE2 ? A HIS 361 ? A HIS 346 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NB ? C HEM   . ? A HEM   501 ? 1_555 95.1  ? 
3  NA  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NB ? C HEM   . ? A HEM   501 ? 1_555 90.8  ? 
4  NE2 ? A HIS 361 ? A HIS 346 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NC ? C HEM   . ? A HEM   501 ? 1_555 94.8  ? 
5  NA  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NC ? C HEM   . ? A HEM   501 ? 1_555 176.7 ? 
6  NB  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NC ? C HEM   . ? A HEM   501 ? 1_555 89.1  ? 
7  NE2 ? A HIS 361 ? A HIS 346 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM   . ? A HEM   501 ? 1_555 86.5  ? 
8  NA  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM   . ? A HEM   501 ? 1_555 88.7  ? 
9  NB  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM   . ? A HEM   501 ? 1_555 178.3 ? 
10 NC  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM   . ? A HEM   501 ? 1_555 91.3  ? 
11 NE2 ? A HIS 361 ? A HIS 346 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 N4 ? D A1H6V . ? A A1H6V 502 ? 1_555 177.1 ? 
12 NA  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 N4 ? D A1H6V . ? A A1H6V 502 ? 1_555 94.2  ? 
13 NB  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 N4 ? D A1H6V . ? A A1H6V 502 ? 1_555 83.8  ? 
14 NC  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 N4 ? D A1H6V . ? A A1H6V 502 ? 1_555 82.6  ? 
15 ND  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 N4 ? D A1H6V . ? A A1H6V 502 ? 1_555 94.6  ? 
16 NE2 ? B HIS 361 ? B HIS 346 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 NA ? E HEM   . ? B HEM   501 ? 1_555 87.7  ? 
17 NE2 ? B HIS 361 ? B HIS 346 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 NB ? E HEM   . ? B HEM   501 ? 1_555 93.3  ? 
18 NA  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 NB ? E HEM   . ? B HEM   501 ? 1_555 90.8  ? 
19 NE2 ? B HIS 361 ? B HIS 346 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 NC ? E HEM   . ? B HEM   501 ? 1_555 92.1  ? 
20 NA  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 NC ? E HEM   . ? B HEM   501 ? 1_555 179.8 ? 
21 NB  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 NC ? E HEM   . ? B HEM   501 ? 1_555 89.3  ? 
22 NE2 ? B HIS 361 ? B HIS 346 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 ND ? E HEM   . ? B HEM   501 ? 1_555 85.7  ? 
23 NA  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 ND ? E HEM   . ? B HEM   501 ? 1_555 88.5  ? 
24 NB  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 ND ? E HEM   . ? B HEM   501 ? 1_555 178.8 ? 
25 NC  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 ND ? E HEM   . ? B HEM   501 ? 1_555 91.4  ? 
26 NE2 ? B HIS 361 ? B HIS 346 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 N4 ? F A1H6V . ? B A1H6V 502 ? 1_555 173.5 ? 
27 NA  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 N4 ? F A1H6V . ? B A1H6V 502 ? 1_555 98.4  ? 
28 NB  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 N4 ? F A1H6V . ? B A1H6V 502 ? 1_555 84.3  ? 
29 NC  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 N4 ? F A1H6V . ? B A1H6V 502 ? 1_555 81.9  ? 
30 ND  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 N4 ? F A1H6V . ? B A1H6V 502 ? 1_555 96.8  ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       323 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     B 
_pdbx_modification_feature.modified_residue_label_seq_id      323 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        308 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      B 
_pdbx_modification_feature.modified_residue_auth_seq_id       308 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? parallel      
AA4 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 117 ? LEU A 118 ? VAL A 102 LEU A 103 
AA1 2 VAL A 263 ? TYR A 264 ? VAL A 248 TYR A 249 
AA2 1 LYS A 150 ? LYS A 151 ? LYS A 135 LYS A 136 
AA2 2 MET A 163 ? ASP A 164 ? MET A 148 ASP A 149 
AA3 1 VAL B 117 ? LEU B 118 ? VAL B 102 LEU B 103 
AA3 2 VAL B 263 ? TYR B 264 ? VAL B 248 TYR B 249 
AA4 1 LYS B 150 ? LYS B 151 ? LYS B 135 LYS B 136 
AA4 2 MET B 163 ? ASP B 164 ? MET B 148 ASP B 149 
# 
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 118 ? N LEU A 103 O VAL A 263 ? O VAL A 248 
AA2 1 2 N LYS A 150 ? N LYS A 135 O ASP A 164 ? O ASP A 149 
AA3 1 2 N LEU B 118 ? N LEU B 103 O VAL B 263 ? O VAL B 248 
AA4 1 2 N LYS B 150 ? N LYS B 135 O ASP B 164 ? O ASP B 149 
# 
_pdbx_entry_details.entry_id                   9ESE 
_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   Y 
# 
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 MET A 8   ? ? -105.99 72.09  
2  1 ASN A 27  ? ? 37.10   72.21  
3  1 HIS A 96  ? ? -118.83 51.36  
4  1 ASN A 133 ? ? -91.10  54.20  
5  1 VAL A 229 ? ? -120.80 -73.90 
6  1 ILE A 354 ? ? -124.97 -54.79 
7  1 ASN B 27  ? ? 38.82   71.60  
8  1 ASN B 133 ? ? -91.89  55.35  
9  1 VAL B 229 ? ? -118.92 -72.67 
10 1 ILE B 354 ? ? -125.32 -55.10 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -14 ? A MET 1   
2  1 Y 1 A GLY -13 ? A GLY 2   
3  1 Y 1 A SER -12 ? A SER 3   
4  1 Y 1 A SER -11 ? A SER 4   
5  1 Y 1 A HIS -10 ? A HIS 5   
6  1 Y 1 A HIS -9  ? A HIS 6   
7  1 Y 1 A HIS -8  ? A HIS 7   
8  1 Y 1 A HIS -7  ? A HIS 8   
9  1 Y 1 A HIS -6  ? A HIS 9   
10 1 Y 1 A HIS -5  ? A HIS 10  
11 1 Y 1 A SER -4  ? A SER 11  
12 1 Y 1 A ALA -3  ? A ALA 12  
13 1 Y 1 A GLY 284 ? A GLY 299 
14 1 Y 1 A LYS 363 ? A LYS 378 
15 1 Y 1 A GLU 364 ? A GLU 379 
16 1 Y 1 A ASN 365 ? A ASN 380 
17 1 Y 1 A LYS 366 ? A LYS 381 
18 1 Y 1 A THR 367 ? A THR 382 
19 1 Y 1 A SER 368 ? A SER 383 
20 1 Y 1 A GLU 369 ? A GLU 384 
21 1 Y 1 A ASP 370 ? A ASP 385 
22 1 Y 1 A PRO 371 ? A PRO 386 
23 1 Y 1 A SER 372 ? A SER 387 
24 1 Y 1 A LYS 373 ? A LYS 388 
25 1 Y 1 A LEU 374 ? A LEU 389 
26 1 Y 1 A GLU 375 ? A GLU 390 
27 1 Y 1 A ALA 376 ? A ALA 391 
28 1 Y 1 A LYS 377 ? A LYS 392 
29 1 Y 1 A GLY 378 ? A GLY 393 
30 1 Y 1 A THR 379 ? A THR 394 
31 1 Y 1 A GLY 380 ? A GLY 395 
32 1 Y 1 A GLY 381 ? A GLY 396 
33 1 Y 1 A GLY 403 ? A GLY 418 
34 1 Y 1 B MET -14 ? B MET 1   
35 1 Y 1 B GLY -13 ? B GLY 2   
36 1 Y 1 B SER -12 ? B SER 3   
37 1 Y 1 B SER -11 ? B SER 4   
38 1 Y 1 B HIS -10 ? B HIS 5   
39 1 Y 1 B HIS -9  ? B HIS 6   
40 1 Y 1 B HIS -8  ? B HIS 7   
41 1 Y 1 B HIS -7  ? B HIS 8   
42 1 Y 1 B HIS -6  ? B HIS 9   
43 1 Y 1 B HIS -5  ? B HIS 10  
44 1 Y 1 B SER -4  ? B SER 11  
45 1 Y 1 B ALA -3  ? B ALA 12  
46 1 Y 1 B ALA -2  ? B ALA 13  
47 1 Y 1 B LEU -1  ? B LEU 14  
48 1 Y 1 B GLU 0   ? B GLU 15  
49 1 Y 1 B VAL 1   ? B VAL 16  
50 1 Y 1 B LEU 2   ? B LEU 17  
51 1 Y 1 B PHE 3   ? B PHE 18  
52 1 Y 1 B GLN 4   ? B GLN 19  
53 1 Y 1 B GLY 5   ? B GLY 20  
54 1 Y 1 B PRO 6   ? B PRO 21  
55 1 Y 1 B HIS 7   ? B HIS 22  
56 1 Y 1 B MET 8   ? B MET 23  
57 1 Y 1 B TRP 9   ? B TRP 24  
58 1 Y 1 B GLN 361 ? B GLN 376 
59 1 Y 1 B PRO 362 ? B PRO 377 
60 1 Y 1 B LYS 363 ? B LYS 378 
61 1 Y 1 B GLU 364 ? B GLU 379 
62 1 Y 1 B ASN 365 ? B ASN 380 
63 1 Y 1 B LYS 366 ? B LYS 381 
64 1 Y 1 B THR 367 ? B THR 382 
65 1 Y 1 B SER 368 ? B SER 383 
66 1 Y 1 B GLU 369 ? B GLU 384 
67 1 Y 1 B ASP 370 ? B ASP 385 
68 1 Y 1 B PRO 371 ? B PRO 386 
69 1 Y 1 B SER 372 ? B SER 387 
70 1 Y 1 B LYS 373 ? B LYS 388 
71 1 Y 1 B LEU 374 ? B LEU 389 
72 1 Y 1 B GLU 375 ? B GLU 390 
73 1 Y 1 B ALA 376 ? B ALA 391 
74 1 Y 1 B LYS 377 ? B LYS 392 
75 1 Y 1 B GLY 378 ? B GLY 393 
76 1 Y 1 B THR 379 ? B THR 394 
77 1 Y 1 B GLY 380 ? B GLY 395 
78 1 Y 1 B GLU 402 ? B GLU 417 
79 1 Y 1 B GLY 403 ? B GLY 418 
# 
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 
A1H6V N1   N  Y N 1   
A1H6V N3   N  Y N 2   
A1H6V C4   C  Y N 3   
A1H6V C5   C  Y N 4   
A1H6V C6   C  Y N 5   
A1H6V C7   C  Y N 6   
A1H6V C8   C  Y N 7   
A1H6V C10  C  Y N 8   
A1H6V C13  C  N N 9   
A1H6V C15  C  N N 10  
A1H6V C17  C  Y N 11  
A1H6V O    O  N N 12  
A1H6V C    C  N R 13  
A1H6V C11  C  Y N 14  
A1H6V N5   N  Y N 15  
A1H6V C18  C  Y N 16  
A1H6V N4   N  Y N 17  
A1H6V C16  C  Y N 18  
A1H6V S    S  Y N 19  
A1H6V C12  C  Y N 20  
A1H6V C14  C  N N 21  
A1H6V C1   C  Y N 22  
A1H6V C2   C  Y N 23  
A1H6V N2   N  Y N 24  
A1H6V N    N  Y N 25  
A1H6V C3   C  Y N 26  
A1H6V C9   C  Y N 27  
A1H6V H6   H  N N 28  
A1H6V H3   H  N N 29  
A1H6V H4   H  N N 30  
A1H6V H5   H  N N 31  
A1H6V H8   H  N N 32  
A1H6V H9   H  N N 33  
A1H6V H13  H  N N 34  
A1H6V H12  H  N N 35  
A1H6V H14  H  N N 36  
A1H6V H1   H  N N 37  
A1H6V H    H  N N 38  
A1H6V H15  H  N N 39  
A1H6V H11  H  N N 40  
A1H6V H10  H  N N 41  
A1H6V H2   H  N N 42  
A1H6V H7   H  N N 43  
ALA   N    N  N N 44  
ALA   CA   C  N S 45  
ALA   C    C  N N 46  
ALA   O    O  N N 47  
ALA   CB   C  N N 48  
ALA   OXT  O  N N 49  
ALA   H    H  N N 50  
ALA   H2   H  N N 51  
ALA   HA   H  N N 52  
ALA   HB1  H  N N 53  
ALA   HB2  H  N N 54  
ALA   HB3  H  N N 55  
ALA   HXT  H  N N 56  
ARG   N    N  N N 57  
ARG   CA   C  N S 58  
ARG   C    C  N N 59  
ARG   O    O  N N 60  
ARG   CB   C  N N 61  
ARG   CG   C  N N 62  
ARG   CD   C  N N 63  
ARG   NE   N  N N 64  
ARG   CZ   C  N N 65  
ARG   NH1  N  N N 66  
ARG   NH2  N  N N 67  
ARG   OXT  O  N N 68  
ARG   H    H  N N 69  
ARG   H2   H  N N 70  
ARG   HA   H  N N 71  
ARG   HB2  H  N N 72  
ARG   HB3  H  N N 73  
ARG   HG2  H  N N 74  
ARG   HG3  H  N N 75  
ARG   HD2  H  N N 76  
ARG   HD3  H  N N 77  
ARG   HE   H  N N 78  
ARG   HH11 H  N N 79  
ARG   HH12 H  N N 80  
ARG   HH21 H  N N 81  
ARG   HH22 H  N N 82  
ARG   HXT  H  N N 83  
ASN   N    N  N N 84  
ASN   CA   C  N S 85  
ASN   C    C  N N 86  
ASN   O    O  N N 87  
ASN   CB   C  N N 88  
ASN   CG   C  N N 89  
ASN   OD1  O  N N 90  
ASN   ND2  N  N N 91  
ASN   OXT  O  N N 92  
ASN   H    H  N N 93  
ASN   H2   H  N N 94  
ASN   HA   H  N N 95  
ASN   HB2  H  N N 96  
ASN   HB3  H  N N 97  
ASN   HD21 H  N N 98  
ASN   HD22 H  N N 99  
ASN   HXT  H  N N 100 
ASP   N    N  N N 101 
ASP   CA   C  N S 102 
ASP   C    C  N N 103 
ASP   O    O  N N 104 
ASP   CB   C  N N 105 
ASP   CG   C  N N 106 
ASP   OD1  O  N N 107 
ASP   OD2  O  N N 108 
ASP   OXT  O  N N 109 
ASP   H    H  N N 110 
ASP   H2   H  N N 111 
ASP   HA   H  N N 112 
ASP   HB2  H  N N 113 
ASP   HB3  H  N N 114 
ASP   HD2  H  N N 115 
ASP   HXT  H  N N 116 
CYS   N    N  N N 117 
CYS   CA   C  N R 118 
CYS   C    C  N N 119 
CYS   O    O  N N 120 
CYS   CB   C  N N 121 
CYS   SG   S  N N 122 
CYS   OXT  O  N N 123 
CYS   H    H  N N 124 
CYS   H2   H  N N 125 
CYS   HA   H  N N 126 
CYS   HB2  H  N N 127 
CYS   HB3  H  N N 128 
CYS   HG   H  N N 129 
CYS   HXT  H  N N 130 
GLN   N    N  N N 131 
GLN   CA   C  N S 132 
GLN   C    C  N N 133 
GLN   O    O  N N 134 
GLN   CB   C  N N 135 
GLN   CG   C  N N 136 
GLN   CD   C  N N 137 
GLN   OE1  O  N N 138 
GLN   NE2  N  N N 139 
GLN   OXT  O  N N 140 
GLN   H    H  N N 141 
GLN   H2   H  N N 142 
GLN   HA   H  N N 143 
GLN   HB2  H  N N 144 
GLN   HB3  H  N N 145 
GLN   HG2  H  N N 146 
GLN   HG3  H  N N 147 
GLN   HE21 H  N N 148 
GLN   HE22 H  N N 149 
GLN   HXT  H  N N 150 
GLU   N    N  N N 151 
GLU   CA   C  N S 152 
GLU   C    C  N N 153 
GLU   O    O  N N 154 
GLU   CB   C  N N 155 
GLU   CG   C  N N 156 
GLU   CD   C  N N 157 
GLU   OE1  O  N N 158 
GLU   OE2  O  N N 159 
GLU   OXT  O  N N 160 
GLU   H    H  N N 161 
GLU   H2   H  N N 162 
GLU   HA   H  N N 163 
GLU   HB2  H  N N 164 
GLU   HB3  H  N N 165 
GLU   HG2  H  N N 166 
GLU   HG3  H  N N 167 
GLU   HE2  H  N N 168 
GLU   HXT  H  N N 169 
GLY   N    N  N N 170 
GLY   CA   C  N N 171 
GLY   C    C  N N 172 
GLY   O    O  N N 173 
GLY   OXT  O  N N 174 
GLY   H    H  N N 175 
GLY   H2   H  N N 176 
GLY   HA2  H  N N 177 
GLY   HA3  H  N N 178 
GLY   HXT  H  N N 179 
HEM   CHA  C  N N 180 
HEM   CHB  C  N N 181 
HEM   CHC  C  N N 182 
HEM   CHD  C  N N 183 
HEM   C1A  C  Y N 184 
HEM   C2A  C  Y N 185 
HEM   C3A  C  Y N 186 
HEM   C4A  C  Y N 187 
HEM   CMA  C  N N 188 
HEM   CAA  C  N N 189 
HEM   CBA  C  N N 190 
HEM   CGA  C  N N 191 
HEM   O1A  O  N N 192 
HEM   O2A  O  N N 193 
HEM   C1B  C  N N 194 
HEM   C2B  C  N N 195 
HEM   C3B  C  N N 196 
HEM   C4B  C  N N 197 
HEM   CMB  C  N N 198 
HEM   CAB  C  N N 199 
HEM   CBB  C  N N 200 
HEM   C1C  C  Y N 201 
HEM   C2C  C  Y N 202 
HEM   C3C  C  Y N 203 
HEM   C4C  C  Y N 204 
HEM   CMC  C  N N 205 
HEM   CAC  C  N N 206 
HEM   CBC  C  N N 207 
HEM   C1D  C  N N 208 
HEM   C2D  C  N N 209 
HEM   C3D  C  N N 210 
HEM   C4D  C  N N 211 
HEM   CMD  C  N N 212 
HEM   CAD  C  N N 213 
HEM   CBD  C  N N 214 
HEM   CGD  C  N N 215 
HEM   O1D  O  N N 216 
HEM   O2D  O  N N 217 
HEM   NA   N  Y N 218 
HEM   NB   N  N N 219 
HEM   NC   N  Y N 220 
HEM   ND   N  N N 221 
HEM   FE   FE N N 222 
HEM   HHB  H  N N 223 
HEM   HHC  H  N N 224 
HEM   HHD  H  N N 225 
HEM   HMA  H  N N 226 
HEM   HMAA H  N N 227 
HEM   HMAB H  N N 228 
HEM   HAA  H  N N 229 
HEM   HAAA H  N N 230 
HEM   HBA  H  N N 231 
HEM   HBAA H  N N 232 
HEM   HMB  H  N N 233 
HEM   HMBA H  N N 234 
HEM   HMBB H  N N 235 
HEM   HAB  H  N N 236 
HEM   HBB  H  N N 237 
HEM   HBBA H  N N 238 
HEM   HMC  H  N N 239 
HEM   HMCA H  N N 240 
HEM   HMCB H  N N 241 
HEM   HAC  H  N N 242 
HEM   HBC  H  N N 243 
HEM   HBCA H  N N 244 
HEM   HMD  H  N N 245 
HEM   HMDA H  N N 246 
HEM   HMDB H  N N 247 
HEM   HAD  H  N N 248 
HEM   HADA H  N N 249 
HEM   HBD  H  N N 250 
HEM   HBDA H  N N 251 
HEM   H2A  H  N N 252 
HEM   H2D  H  N N 253 
HEM   HHA  H  N N 254 
HIS   N    N  N N 255 
HIS   CA   C  N S 256 
HIS   C    C  N N 257 
HIS   O    O  N N 258 
HIS   CB   C  N N 259 
HIS   CG   C  Y N 260 
HIS   ND1  N  Y N 261 
HIS   CD2  C  Y N 262 
HIS   CE1  C  Y N 263 
HIS   NE2  N  Y N 264 
HIS   OXT  O  N N 265 
HIS   H    H  N N 266 
HIS   H2   H  N N 267 
HIS   HA   H  N N 268 
HIS   HB2  H  N N 269 
HIS   HB3  H  N N 270 
HIS   HD1  H  N N 271 
HIS   HD2  H  N N 272 
HIS   HE1  H  N N 273 
HIS   HE2  H  N N 274 
HIS   HXT  H  N N 275 
HOH   O    O  N N 276 
HOH   H1   H  N N 277 
HOH   H2   H  N N 278 
ILE   N    N  N N 279 
ILE   CA   C  N S 280 
ILE   C    C  N N 281 
ILE   O    O  N N 282 
ILE   CB   C  N S 283 
ILE   CG1  C  N N 284 
ILE   CG2  C  N N 285 
ILE   CD1  C  N N 286 
ILE   OXT  O  N N 287 
ILE   H    H  N N 288 
ILE   H2   H  N N 289 
ILE   HA   H  N N 290 
ILE   HB   H  N N 291 
ILE   HG12 H  N N 292 
ILE   HG13 H  N N 293 
ILE   HG21 H  N N 294 
ILE   HG22 H  N N 295 
ILE   HG23 H  N N 296 
ILE   HD11 H  N N 297 
ILE   HD12 H  N N 298 
ILE   HD13 H  N N 299 
ILE   HXT  H  N N 300 
LEU   N    N  N N 301 
LEU   CA   C  N S 302 
LEU   C    C  N N 303 
LEU   O    O  N N 304 
LEU   CB   C  N N 305 
LEU   CG   C  N N 306 
LEU   CD1  C  N N 307 
LEU   CD2  C  N N 308 
LEU   OXT  O  N N 309 
LEU   H    H  N N 310 
LEU   H2   H  N N 311 
LEU   HA   H  N N 312 
LEU   HB2  H  N N 313 
LEU   HB3  H  N N 314 
LEU   HG   H  N N 315 
LEU   HD11 H  N N 316 
LEU   HD12 H  N N 317 
LEU   HD13 H  N N 318 
LEU   HD21 H  N N 319 
LEU   HD22 H  N N 320 
LEU   HD23 H  N N 321 
LEU   HXT  H  N N 322 
LYS   N    N  N N 323 
LYS   CA   C  N S 324 
LYS   C    C  N N 325 
LYS   O    O  N N 326 
LYS   CB   C  N N 327 
LYS   CG   C  N N 328 
LYS   CD   C  N N 329 
LYS   CE   C  N N 330 
LYS   NZ   N  N N 331 
LYS   OXT  O  N N 332 
LYS   H    H  N N 333 
LYS   H2   H  N N 334 
LYS   HA   H  N N 335 
LYS   HB2  H  N N 336 
LYS   HB3  H  N N 337 
LYS   HG2  H  N N 338 
LYS   HG3  H  N N 339 
LYS   HD2  H  N N 340 
LYS   HD3  H  N N 341 
LYS   HE2  H  N N 342 
LYS   HE3  H  N N 343 
LYS   HZ1  H  N N 344 
LYS   HZ2  H  N N 345 
LYS   HZ3  H  N N 346 
LYS   HXT  H  N N 347 
MET   N    N  N N 348 
MET   CA   C  N S 349 
MET   C    C  N N 350 
MET   O    O  N N 351 
MET   CB   C  N N 352 
MET   CG   C  N N 353 
MET   SD   S  N N 354 
MET   CE   C  N N 355 
MET   OXT  O  N N 356 
MET   H    H  N N 357 
MET   H2   H  N N 358 
MET   HA   H  N N 359 
MET   HB2  H  N N 360 
MET   HB3  H  N N 361 
MET   HG2  H  N N 362 
MET   HG3  H  N N 363 
MET   HE1  H  N N 364 
MET   HE2  H  N N 365 
MET   HE3  H  N N 366 
MET   HXT  H  N N 367 
PHE   N    N  N N 368 
PHE   CA   C  N S 369 
PHE   C    C  N N 370 
PHE   O    O  N N 371 
PHE   CB   C  N N 372 
PHE   CG   C  Y N 373 
PHE   CD1  C  Y N 374 
PHE   CD2  C  Y N 375 
PHE   CE1  C  Y N 376 
PHE   CE2  C  Y N 377 
PHE   CZ   C  Y N 378 
PHE   OXT  O  N N 379 
PHE   H    H  N N 380 
PHE   H2   H  N N 381 
PHE   HA   H  N N 382 
PHE   HB2  H  N N 383 
PHE   HB3  H  N N 384 
PHE   HD1  H  N N 385 
PHE   HD2  H  N N 386 
PHE   HE1  H  N N 387 
PHE   HE2  H  N N 388 
PHE   HZ   H  N N 389 
PHE   HXT  H  N N 390 
PRO   N    N  N N 391 
PRO   CA   C  N S 392 
PRO   C    C  N N 393 
PRO   O    O  N N 394 
PRO   CB   C  N N 395 
PRO   CG   C  N N 396 
PRO   CD   C  N N 397 
PRO   OXT  O  N N 398 
PRO   H    H  N N 399 
PRO   HA   H  N N 400 
PRO   HB2  H  N N 401 
PRO   HB3  H  N N 402 
PRO   HG2  H  N N 403 
PRO   HG3  H  N N 404 
PRO   HD2  H  N N 405 
PRO   HD3  H  N N 406 
PRO   HXT  H  N N 407 
SER   N    N  N N 408 
SER   CA   C  N S 409 
SER   C    C  N N 410 
SER   O    O  N N 411 
SER   CB   C  N N 412 
SER   OG   O  N N 413 
SER   OXT  O  N N 414 
SER   H    H  N N 415 
SER   H2   H  N N 416 
SER   HA   H  N N 417 
SER   HB2  H  N N 418 
SER   HB3  H  N N 419 
SER   HG   H  N N 420 
SER   HXT  H  N N 421 
THR   N    N  N N 422 
THR   CA   C  N S 423 
THR   C    C  N N 424 
THR   O    O  N N 425 
THR   CB   C  N R 426 
THR   OG1  O  N N 427 
THR   CG2  C  N N 428 
THR   OXT  O  N N 429 
THR   H    H  N N 430 
THR   H2   H  N N 431 
THR   HA   H  N N 432 
THR   HB   H  N N 433 
THR   HG1  H  N N 434 
THR   HG21 H  N N 435 
THR   HG22 H  N N 436 
THR   HG23 H  N N 437 
THR   HXT  H  N N 438 
TRP   N    N  N N 439 
TRP   CA   C  N S 440 
TRP   C    C  N N 441 
TRP   O    O  N N 442 
TRP   CB   C  N N 443 
TRP   CG   C  Y N 444 
TRP   CD1  C  Y N 445 
TRP   CD2  C  Y N 446 
TRP   NE1  N  Y N 447 
TRP   CE2  C  Y N 448 
TRP   CE3  C  Y N 449 
TRP   CZ2  C  Y N 450 
TRP   CZ3  C  Y N 451 
TRP   CH2  C  Y N 452 
TRP   OXT  O  N N 453 
TRP   H    H  N N 454 
TRP   H2   H  N N 455 
TRP   HA   H  N N 456 
TRP   HB2  H  N N 457 
TRP   HB3  H  N N 458 
TRP   HD1  H  N N 459 
TRP   HE1  H  N N 460 
TRP   HE3  H  N N 461 
TRP   HZ2  H  N N 462 
TRP   HZ3  H  N N 463 
TRP   HH2  H  N N 464 
TRP   HXT  H  N N 465 
TYR   N    N  N N 466 
TYR   CA   C  N S 467 
TYR   C    C  N N 468 
TYR   O    O  N N 469 
TYR   CB   C  N N 470 
TYR   CG   C  Y N 471 
TYR   CD1  C  Y N 472 
TYR   CD2  C  Y N 473 
TYR   CE1  C  Y N 474 
TYR   CE2  C  Y N 475 
TYR   CZ   C  Y N 476 
TYR   OH   O  N N 477 
TYR   OXT  O  N N 478 
TYR   H    H  N N 479 
TYR   H2   H  N N 480 
TYR   HA   H  N N 481 
TYR   HB2  H  N N 482 
TYR   HB3  H  N N 483 
TYR   HD1  H  N N 484 
TYR   HD2  H  N N 485 
TYR   HE1  H  N N 486 
TYR   HE2  H  N N 487 
TYR   HH   H  N N 488 
TYR   HXT  H  N N 489 
VAL   N    N  N N 490 
VAL   CA   C  N S 491 
VAL   C    C  N N 492 
VAL   O    O  N N 493 
VAL   CB   C  N N 494 
VAL   CG1  C  N N 495 
VAL   CG2  C  N N 496 
VAL   OXT  O  N N 497 
VAL   H    H  N N 498 
VAL   H2   H  N N 499 
VAL   HA   H  N N 500 
VAL   HB   H  N N 501 
VAL   HG11 H  N N 502 
VAL   HG12 H  N N 503 
VAL   HG13 H  N N 504 
VAL   HG21 H  N N 505 
VAL   HG22 H  N N 506 
VAL   HG23 H  N N 507 
VAL   HXT  H  N N 508 
# 
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 
A1H6V C   O    sing N N 1   
A1H6V C1  C    sing N N 2   
A1H6V C1  N    sing Y N 3   
A1H6V N   N1   doub Y N 4   
A1H6V C2  C1   doub Y N 5   
A1H6V N2  C2   sing Y N 6   
A1H6V N1  N2   sing Y N 7   
A1H6V C3  N2   sing N N 8   
A1H6V C3  C4   sing Y N 9   
A1H6V C4  C5   doub Y N 10  
A1H6V C6  C3   doub Y N 11  
A1H6V C7  C6   sing Y N 12  
A1H6V C7  C8   doub Y N 13  
A1H6V C5  C8   sing Y N 14  
A1H6V C8  N3   sing Y N 15  
A1H6V N3  C9   sing Y N 16  
A1H6V C9  C10  doub Y N 17  
A1H6V C10 C7   sing Y N 18  
A1H6V C11 C    sing N N 19  
A1H6V C11 C12  doub Y N 20  
A1H6V C13 C12  sing N N 21  
A1H6V C13 C14  sing N N 22  
A1H6V C14 C15  sing N N 23  
A1H6V C15 C13  sing N N 24  
A1H6V C12 S    sing Y N 25  
A1H6V S   C16  sing Y N 26  
A1H6V C16 C17  doub Y N 27  
A1H6V C17 N4   sing Y N 28  
A1H6V N4  C18  doub Y N 29  
A1H6V C18 N5   sing Y N 30  
A1H6V C16 N5   sing Y N 31  
A1H6V N5  C11  sing Y N 32  
A1H6V N3  H6   sing N N 33  
A1H6V C4  H3   sing N N 34  
A1H6V C5  H4   sing N N 35  
A1H6V C6  H5   sing N N 36  
A1H6V C10 H8   sing N N 37  
A1H6V C13 H9   sing N N 38  
A1H6V C15 H13  sing N N 39  
A1H6V C15 H12  sing N N 40  
A1H6V C17 H14  sing N N 41  
A1H6V O   H1   sing N N 42  
A1H6V C   H    sing N N 43  
A1H6V C18 H15  sing N N 44  
A1H6V C14 H11  sing N N 45  
A1H6V C14 H10  sing N N 46  
A1H6V C2  H2   sing N N 47  
A1H6V C9  H7   sing N N 48  
ALA   N   CA   sing N N 49  
ALA   N   H    sing N N 50  
ALA   N   H2   sing N N 51  
ALA   CA  C    sing N N 52  
ALA   CA  CB   sing N N 53  
ALA   CA  HA   sing N N 54  
ALA   C   O    doub N N 55  
ALA   C   OXT  sing N N 56  
ALA   CB  HB1  sing N N 57  
ALA   CB  HB2  sing N N 58  
ALA   CB  HB3  sing N N 59  
ALA   OXT HXT  sing N N 60  
ARG   N   CA   sing N N 61  
ARG   N   H    sing N N 62  
ARG   N   H2   sing N N 63  
ARG   CA  C    sing N N 64  
ARG   CA  CB   sing N N 65  
ARG   CA  HA   sing N N 66  
ARG   C   O    doub N N 67  
ARG   C   OXT  sing N N 68  
ARG   CB  CG   sing N N 69  
ARG   CB  HB2  sing N N 70  
ARG   CB  HB3  sing N N 71  
ARG   CG  CD   sing N N 72  
ARG   CG  HG2  sing N N 73  
ARG   CG  HG3  sing N N 74  
ARG   CD  NE   sing N N 75  
ARG   CD  HD2  sing N N 76  
ARG   CD  HD3  sing N N 77  
ARG   NE  CZ   sing N N 78  
ARG   NE  HE   sing N N 79  
ARG   CZ  NH1  sing N N 80  
ARG   CZ  NH2  doub N N 81  
ARG   NH1 HH11 sing N N 82  
ARG   NH1 HH12 sing N N 83  
ARG   NH2 HH21 sing N N 84  
ARG   NH2 HH22 sing N N 85  
ARG   OXT HXT  sing N N 86  
ASN   N   CA   sing N N 87  
ASN   N   H    sing N N 88  
ASN   N   H2   sing N N 89  
ASN   CA  C    sing N N 90  
ASN   CA  CB   sing N N 91  
ASN   CA  HA   sing N N 92  
ASN   C   O    doub N N 93  
ASN   C   OXT  sing N N 94  
ASN   CB  CG   sing N N 95  
ASN   CB  HB2  sing N N 96  
ASN   CB  HB3  sing N N 97  
ASN   CG  OD1  doub N N 98  
ASN   CG  ND2  sing N N 99  
ASN   ND2 HD21 sing N N 100 
ASN   ND2 HD22 sing N N 101 
ASN   OXT HXT  sing N N 102 
ASP   N   CA   sing N N 103 
ASP   N   H    sing N N 104 
ASP   N   H2   sing N N 105 
ASP   CA  C    sing N N 106 
ASP   CA  CB   sing N N 107 
ASP   CA  HA   sing N N 108 
ASP   C   O    doub N N 109 
ASP   C   OXT  sing N N 110 
ASP   CB  CG   sing N N 111 
ASP   CB  HB2  sing N N 112 
ASP   CB  HB3  sing N N 113 
ASP   CG  OD1  doub N N 114 
ASP   CG  OD2  sing N N 115 
ASP   OD2 HD2  sing N N 116 
ASP   OXT HXT  sing N N 117 
CYS   N   CA   sing N N 118 
CYS   N   H    sing N N 119 
CYS   N   H2   sing N N 120 
CYS   CA  C    sing N N 121 
CYS   CA  CB   sing N N 122 
CYS   CA  HA   sing N N 123 
CYS   C   O    doub N N 124 
CYS   C   OXT  sing N N 125 
CYS   CB  SG   sing N N 126 
CYS   CB  HB2  sing N N 127 
CYS   CB  HB3  sing N N 128 
CYS   SG  HG   sing N N 129 
CYS   OXT HXT  sing N N 130 
GLN   N   CA   sing N N 131 
GLN   N   H    sing N N 132 
GLN   N   H2   sing N N 133 
GLN   CA  C    sing N N 134 
GLN   CA  CB   sing N N 135 
GLN   CA  HA   sing N N 136 
GLN   C   O    doub N N 137 
GLN   C   OXT  sing N N 138 
GLN   CB  CG   sing N N 139 
GLN   CB  HB2  sing N N 140 
GLN   CB  HB3  sing N N 141 
GLN   CG  CD   sing N N 142 
GLN   CG  HG2  sing N N 143 
GLN   CG  HG3  sing N N 144 
GLN   CD  OE1  doub N N 145 
GLN   CD  NE2  sing N N 146 
GLN   NE2 HE21 sing N N 147 
GLN   NE2 HE22 sing N N 148 
GLN   OXT HXT  sing N N 149 
GLU   N   CA   sing N N 150 
GLU   N   H    sing N N 151 
GLU   N   H2   sing N N 152 
GLU   CA  C    sing N N 153 
GLU   CA  CB   sing N N 154 
GLU   CA  HA   sing N N 155 
GLU   C   O    doub N N 156 
GLU   C   OXT  sing N N 157 
GLU   CB  CG   sing N N 158 
GLU   CB  HB2  sing N N 159 
GLU   CB  HB3  sing N N 160 
GLU   CG  CD   sing N N 161 
GLU   CG  HG2  sing N N 162 
GLU   CG  HG3  sing N N 163 
GLU   CD  OE1  doub N N 164 
GLU   CD  OE2  sing N N 165 
GLU   OE2 HE2  sing N N 166 
GLU   OXT HXT  sing N N 167 
GLY   N   CA   sing N N 168 
GLY   N   H    sing N N 169 
GLY   N   H2   sing N N 170 
GLY   CA  C    sing N N 171 
GLY   CA  HA2  sing N N 172 
GLY   CA  HA3  sing N N 173 
GLY   C   O    doub N N 174 
GLY   C   OXT  sing N N 175 
GLY   OXT HXT  sing N N 176 
HEM   CHA C1A  sing N N 177 
HEM   CHA C4D  doub N N 178 
HEM   CHA HHA  sing N N 179 
HEM   CHB C4A  sing N N 180 
HEM   CHB C1B  doub N N 181 
HEM   CHB HHB  sing N N 182 
HEM   CHC C4B  sing N N 183 
HEM   CHC C1C  doub N N 184 
HEM   CHC HHC  sing N N 185 
HEM   CHD C4C  doub N N 186 
HEM   CHD C1D  sing N N 187 
HEM   CHD HHD  sing N N 188 
HEM   C1A C2A  doub Y N 189 
HEM   C1A NA   sing Y N 190 
HEM   C2A C3A  sing Y N 191 
HEM   C2A CAA  sing N N 192 
HEM   C3A C4A  doub Y N 193 
HEM   C3A CMA  sing N N 194 
HEM   C4A NA   sing Y N 195 
HEM   CMA HMA  sing N N 196 
HEM   CMA HMAA sing N N 197 
HEM   CMA HMAB sing N N 198 
HEM   CAA CBA  sing N N 199 
HEM   CAA HAA  sing N N 200 
HEM   CAA HAAA sing N N 201 
HEM   CBA CGA  sing N N 202 
HEM   CBA HBA  sing N N 203 
HEM   CBA HBAA sing N N 204 
HEM   CGA O1A  doub N N 205 
HEM   CGA O2A  sing N N 206 
HEM   C1B C2B  sing N N 207 
HEM   C1B NB   sing N N 208 
HEM   C2B C3B  doub N N 209 
HEM   C2B CMB  sing N N 210 
HEM   C3B C4B  sing N N 211 
HEM   C3B CAB  sing N N 212 
HEM   C4B NB   doub N N 213 
HEM   CMB HMB  sing N N 214 
HEM   CMB HMBA sing N N 215 
HEM   CMB HMBB sing N N 216 
HEM   CAB CBB  doub N N 217 
HEM   CAB HAB  sing N N 218 
HEM   CBB HBB  sing N N 219 
HEM   CBB HBBA sing N N 220 
HEM   C1C C2C  sing Y N 221 
HEM   C1C NC   sing Y N 222 
HEM   C2C C3C  doub Y N 223 
HEM   C2C CMC  sing N N 224 
HEM   C3C C4C  sing Y N 225 
HEM   C3C CAC  sing N N 226 
HEM   C4C NC   sing Y N 227 
HEM   CMC HMC  sing N N 228 
HEM   CMC HMCA sing N N 229 
HEM   CMC HMCB sing N N 230 
HEM   CAC CBC  doub N N 231 
HEM   CAC HAC  sing N N 232 
HEM   CBC HBC  sing N N 233 
HEM   CBC HBCA sing N N 234 
HEM   C1D C2D  sing N N 235 
HEM   C1D ND   doub N N 236 
HEM   C2D C3D  doub N N 237 
HEM   C2D CMD  sing N N 238 
HEM   C3D C4D  sing N N 239 
HEM   C3D CAD  sing N N 240 
HEM   C4D ND   sing N N 241 
HEM   CMD HMD  sing N N 242 
HEM   CMD HMDA sing N N 243 
HEM   CMD HMDB sing N N 244 
HEM   CAD CBD  sing N N 245 
HEM   CAD HAD  sing N N 246 
HEM   CAD HADA sing N N 247 
HEM   CBD CGD  sing N N 248 
HEM   CBD HBD  sing N N 249 
HEM   CBD HBDA sing N N 250 
HEM   CGD O1D  doub N N 251 
HEM   CGD O2D  sing N N 252 
HEM   O2A H2A  sing N N 253 
HEM   O2D H2D  sing N N 254 
HEM   FE  NA   sing N N 255 
HEM   FE  NB   sing N N 256 
HEM   FE  NC   sing N N 257 
HEM   FE  ND   sing N N 258 
HIS   N   CA   sing N N 259 
HIS   N   H    sing N N 260 
HIS   N   H2   sing N N 261 
HIS   CA  C    sing N N 262 
HIS   CA  CB   sing N N 263 
HIS   CA  HA   sing N N 264 
HIS   C   O    doub N N 265 
HIS   C   OXT  sing N N 266 
HIS   CB  CG   sing N N 267 
HIS   CB  HB2  sing N N 268 
HIS   CB  HB3  sing N N 269 
HIS   CG  ND1  sing Y N 270 
HIS   CG  CD2  doub Y N 271 
HIS   ND1 CE1  doub Y N 272 
HIS   ND1 HD1  sing N N 273 
HIS   CD2 NE2  sing Y N 274 
HIS   CD2 HD2  sing N N 275 
HIS   CE1 NE2  sing Y N 276 
HIS   CE1 HE1  sing N N 277 
HIS   NE2 HE2  sing N N 278 
HIS   OXT HXT  sing N N 279 
HOH   O   H1   sing N N 280 
HOH   O   H2   sing N N 281 
ILE   N   CA   sing N N 282 
ILE   N   H    sing N N 283 
ILE   N   H2   sing N N 284 
ILE   CA  C    sing N N 285 
ILE   CA  CB   sing N N 286 
ILE   CA  HA   sing N N 287 
ILE   C   O    doub N N 288 
ILE   C   OXT  sing N N 289 
ILE   CB  CG1  sing N N 290 
ILE   CB  CG2  sing N N 291 
ILE   CB  HB   sing N N 292 
ILE   CG1 CD1  sing N N 293 
ILE   CG1 HG12 sing N N 294 
ILE   CG1 HG13 sing N N 295 
ILE   CG2 HG21 sing N N 296 
ILE   CG2 HG22 sing N N 297 
ILE   CG2 HG23 sing N N 298 
ILE   CD1 HD11 sing N N 299 
ILE   CD1 HD12 sing N N 300 
ILE   CD1 HD13 sing N N 301 
ILE   OXT HXT  sing N N 302 
LEU   N   CA   sing N N 303 
LEU   N   H    sing N N 304 
LEU   N   H2   sing N N 305 
LEU   CA  C    sing N N 306 
LEU   CA  CB   sing N N 307 
LEU   CA  HA   sing N N 308 
LEU   C   O    doub N N 309 
LEU   C   OXT  sing N N 310 
LEU   CB  CG   sing N N 311 
LEU   CB  HB2  sing N N 312 
LEU   CB  HB3  sing N N 313 
LEU   CG  CD1  sing N N 314 
LEU   CG  CD2  sing N N 315 
LEU   CG  HG   sing N N 316 
LEU   CD1 HD11 sing N N 317 
LEU   CD1 HD12 sing N N 318 
LEU   CD1 HD13 sing N N 319 
LEU   CD2 HD21 sing N N 320 
LEU   CD2 HD22 sing N N 321 
LEU   CD2 HD23 sing N N 322 
LEU   OXT HXT  sing N N 323 
LYS   N   CA   sing N N 324 
LYS   N   H    sing N N 325 
LYS   N   H2   sing N N 326 
LYS   CA  C    sing N N 327 
LYS   CA  CB   sing N N 328 
LYS   CA  HA   sing N N 329 
LYS   C   O    doub N N 330 
LYS   C   OXT  sing N N 331 
LYS   CB  CG   sing N N 332 
LYS   CB  HB2  sing N N 333 
LYS   CB  HB3  sing N N 334 
LYS   CG  CD   sing N N 335 
LYS   CG  HG2  sing N N 336 
LYS   CG  HG3  sing N N 337 
LYS   CD  CE   sing N N 338 
LYS   CD  HD2  sing N N 339 
LYS   CD  HD3  sing N N 340 
LYS   CE  NZ   sing N N 341 
LYS   CE  HE2  sing N N 342 
LYS   CE  HE3  sing N N 343 
LYS   NZ  HZ1  sing N N 344 
LYS   NZ  HZ2  sing N N 345 
LYS   NZ  HZ3  sing N N 346 
LYS   OXT HXT  sing N N 347 
MET   N   CA   sing N N 348 
MET   N   H    sing N N 349 
MET   N   H2   sing N N 350 
MET   CA  C    sing N N 351 
MET   CA  CB   sing N N 352 
MET   CA  HA   sing N N 353 
MET   C   O    doub N N 354 
MET   C   OXT  sing N N 355 
MET   CB  CG   sing N N 356 
MET   CB  HB2  sing N N 357 
MET   CB  HB3  sing N N 358 
MET   CG  SD   sing N N 359 
MET   CG  HG2  sing N N 360 
MET   CG  HG3  sing N N 361 
MET   SD  CE   sing N N 362 
MET   CE  HE1  sing N N 363 
MET   CE  HE2  sing N N 364 
MET   CE  HE3  sing N N 365 
MET   OXT HXT  sing N N 366 
PHE   N   CA   sing N N 367 
PHE   N   H    sing N N 368 
PHE   N   H2   sing N N 369 
PHE   CA  C    sing N N 370 
PHE   CA  CB   sing N N 371 
PHE   CA  HA   sing N N 372 
PHE   C   O    doub N N 373 
PHE   C   OXT  sing N N 374 
PHE   CB  CG   sing N N 375 
PHE   CB  HB2  sing N N 376 
PHE   CB  HB3  sing N N 377 
PHE   CG  CD1  doub Y N 378 
PHE   CG  CD2  sing Y N 379 
PHE   CD1 CE1  sing Y N 380 
PHE   CD1 HD1  sing N N 381 
PHE   CD2 CE2  doub Y N 382 
PHE   CD2 HD2  sing N N 383 
PHE   CE1 CZ   doub Y N 384 
PHE   CE1 HE1  sing N N 385 
PHE   CE2 CZ   sing Y N 386 
PHE   CE2 HE2  sing N N 387 
PHE   CZ  HZ   sing N N 388 
PHE   OXT HXT  sing N N 389 
PRO   N   CA   sing N N 390 
PRO   N   CD   sing N N 391 
PRO   N   H    sing N N 392 
PRO   CA  C    sing N N 393 
PRO   CA  CB   sing N N 394 
PRO   CA  HA   sing N N 395 
PRO   C   O    doub N N 396 
PRO   C   OXT  sing N N 397 
PRO   CB  CG   sing N N 398 
PRO   CB  HB2  sing N N 399 
PRO   CB  HB3  sing N N 400 
PRO   CG  CD   sing N N 401 
PRO   CG  HG2  sing N N 402 
PRO   CG  HG3  sing N N 403 
PRO   CD  HD2  sing N N 404 
PRO   CD  HD3  sing N N 405 
PRO   OXT HXT  sing N N 406 
SER   N   CA   sing N N 407 
SER   N   H    sing N N 408 
SER   N   H2   sing N N 409 
SER   CA  C    sing N N 410 
SER   CA  CB   sing N N 411 
SER   CA  HA   sing N N 412 
SER   C   O    doub N N 413 
SER   C   OXT  sing N N 414 
SER   CB  OG   sing N N 415 
SER   CB  HB2  sing N N 416 
SER   CB  HB3  sing N N 417 
SER   OG  HG   sing N N 418 
SER   OXT HXT  sing N N 419 
THR   N   CA   sing N N 420 
THR   N   H    sing N N 421 
THR   N   H2   sing N N 422 
THR   CA  C    sing N N 423 
THR   CA  CB   sing N N 424 
THR   CA  HA   sing N N 425 
THR   C   O    doub N N 426 
THR   C   OXT  sing N N 427 
THR   CB  OG1  sing N N 428 
THR   CB  CG2  sing N N 429 
THR   CB  HB   sing N N 430 
THR   OG1 HG1  sing N N 431 
THR   CG2 HG21 sing N N 432 
THR   CG2 HG22 sing N N 433 
THR   CG2 HG23 sing N N 434 
THR   OXT HXT  sing N N 435 
TRP   N   CA   sing N N 436 
TRP   N   H    sing N N 437 
TRP   N   H2   sing N N 438 
TRP   CA  C    sing N N 439 
TRP   CA  CB   sing N N 440 
TRP   CA  HA   sing N N 441 
TRP   C   O    doub N N 442 
TRP   C   OXT  sing N N 443 
TRP   CB  CG   sing N N 444 
TRP   CB  HB2  sing N N 445 
TRP   CB  HB3  sing N N 446 
TRP   CG  CD1  doub Y N 447 
TRP   CG  CD2  sing Y N 448 
TRP   CD1 NE1  sing Y N 449 
TRP   CD1 HD1  sing N N 450 
TRP   CD2 CE2  doub Y N 451 
TRP   CD2 CE3  sing Y N 452 
TRP   NE1 CE2  sing Y N 453 
TRP   NE1 HE1  sing N N 454 
TRP   CE2 CZ2  sing Y N 455 
TRP   CE3 CZ3  doub Y N 456 
TRP   CE3 HE3  sing N N 457 
TRP   CZ2 CH2  doub Y N 458 
TRP   CZ2 HZ2  sing N N 459 
TRP   CZ3 CH2  sing Y N 460 
TRP   CZ3 HZ3  sing N N 461 
TRP   CH2 HH2  sing N N 462 
TRP   OXT HXT  sing N N 463 
TYR   N   CA   sing N N 464 
TYR   N   H    sing N N 465 
TYR   N   H2   sing N N 466 
TYR   CA  C    sing N N 467 
TYR   CA  CB   sing N N 468 
TYR   CA  HA   sing N N 469 
TYR   C   O    doub N N 470 
TYR   C   OXT  sing N N 471 
TYR   CB  CG   sing N N 472 
TYR   CB  HB2  sing N N 473 
TYR   CB  HB3  sing N N 474 
TYR   CG  CD1  doub Y N 475 
TYR   CG  CD2  sing Y N 476 
TYR   CD1 CE1  sing Y N 477 
TYR   CD1 HD1  sing N N 478 
TYR   CD2 CE2  doub Y N 479 
TYR   CD2 HD2  sing N N 480 
TYR   CE1 CZ   doub Y N 481 
TYR   CE1 HE1  sing N N 482 
TYR   CE2 CZ   sing Y N 483 
TYR   CE2 HE2  sing N N 484 
TYR   CZ  OH   sing N N 485 
TYR   OH  HH   sing N N 486 
TYR   OXT HXT  sing N N 487 
VAL   N   CA   sing N N 488 
VAL   N   H    sing N N 489 
VAL   N   H2   sing N N 490 
VAL   CA  C    sing N N 491 
VAL   CA  CB   sing N N 492 
VAL   CA  HA   sing N N 493 
VAL   C   O    doub N N 494 
VAL   C   OXT  sing N N 495 
VAL   CB  CG1  sing N N 496 
VAL   CB  CG2  sing N N 497 
VAL   CB  HB   sing N N 498 
VAL   CG1 HG11 sing N N 499 
VAL   CG1 HG12 sing N N 500 
VAL   CG1 HG13 sing N N 501 
VAL   CG2 HG21 sing N N 502 
VAL   CG2 HG22 sing N N 503 
VAL   CG2 HG23 sing N N 504 
VAL   OXT HXT  sing N N 505 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_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             'experimental model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'internal structure' 
# 
_atom_sites.entry_id                    9ESE 
_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]   0.011772 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010980 
_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]   0.007671 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
FE 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ALA   A 1 13  ? 14.899  -20.625 -1.094  1 65.98  ? -2  ALA   A N   1 
ATOM   2    C  CA  . ALA   A 1 13  ? 15.2    -19.397 -1.843  1 66.66  ? -2  ALA   A CA  1 
ATOM   3    C  C   . ALA   A 1 13  ? 15.66   -18.255 -0.92   1 67.49  ? -2  ALA   A C   1 
ATOM   4    O  O   . ALA   A 1 13  ? 16.525  -17.456 -1.301  1 67.47  ? -2  ALA   A O   1 
ATOM   5    C  CB  . ALA   A 1 13  ? 14.001  -18.959 -2.667  1 66.47  ? -2  ALA   A CB  1 
ATOM   6    N  N   . LEU   A 1 14  ? 15.069  -18.163 0.278   1 67.72  ? -1  LEU   A N   1 
ATOM   7    C  CA  . LEU   A 1 14  ? 15.509  -17.166 1.254   1 68.74  ? -1  LEU   A CA  1 
ATOM   8    C  C   . LEU   A 1 14  ? 16.872  -17.604 1.837   1 69.41  ? -1  LEU   A C   1 
ATOM   9    O  O   . LEU   A 1 14  ? 17.748  -16.762 2.037   1 69.74  ? -1  LEU   A O   1 
ATOM   10   C  CB  . LEU   A 1 14  ? 14.466  -16.992 2.374   1 69.11  ? -1  LEU   A CB  1 
ATOM   11   C  CG  . LEU   A 1 14  ? 14.623  -15.779 3.291   1 70.43  ? -1  LEU   A CG  1 
ATOM   12   C  CD1 . LEU   A 1 14  ? 14.725  -14.488 2.508   1 70.92  ? -1  LEU   A CD1 1 
ATOM   13   C  CD2 . LEU   A 1 14  ? 13.483  -15.691 4.279   1 70.95  ? -1  LEU   A CD2 1 
ATOM   14   N  N   . GLU   A 1 15  ? 17.064  -18.934 2.039   1 69.21  ? 0   GLU   A N   1 
ATOM   15   C  CA  . GLU   A 1 15  ? 18.287  -19.547 2.55    1 69.24  ? 0   GLU   A CA  1 
ATOM   16   C  C   . GLU   A 1 15  ? 19.452  -19.332 1.579   1 69.23  ? 0   GLU   A C   1 
ATOM   17   O  O   . GLU   A 1 15  ? 20.581  -19.13  2.013   1 69.23  ? 0   GLU   A O   1 
ATOM   18   C  CB  . GLU   A 1 15  ? 18.065  -21.052 2.81    1 70.9   ? 0   GLU   A CB  1 
ATOM   19   N  N   . VAL   A 1 16  ? 19.181  -19.389 0.268   1 68.86  ? 1   VAL   A N   1 
ATOM   20   C  CA  . VAL   A 1 16  ? 20.201  -19.141 -0.75   1 68.66  ? 1   VAL   A CA  1 
ATOM   21   C  C   . VAL   A 1 16  ? 20.61   -17.636 -0.748  1 68.53  ? 1   VAL   A C   1 
ATOM   22   O  O   . VAL   A 1 16  ? 21.764  -17.307 -1.006  1 68.49  ? 1   VAL   A O   1 
ATOM   23   C  CB  . VAL   A 1 16  ? 19.732  -19.667 -2.133  1 69.07  ? 1   VAL   A CB  1 
ATOM   24   C  CG1 . VAL   A 1 16  ? 20.527  -19.051 -3.272  1 69.62  ? 1   VAL   A CG1 1 
ATOM   25   C  CG2 . VAL   A 1 16  ? 19.804  -21.188 -2.189  1 69.23  ? 1   VAL   A CG2 1 
ATOM   26   N  N   . LEU   A 1 17  ? 19.69   -16.737 -0.374  1 68.31  ? 2   LEU   A N   1 
ATOM   27   C  CA  . LEU   A 1 17  ? 19.99   -15.315 -0.276  1 68.68  ? 2   LEU   A CA  1 
ATOM   28   C  C   . LEU   A 1 17  ? 20.928  -15.043 0.911   1 69.17  ? 2   LEU   A C   1 
ATOM   29   O  O   . LEU   A 1 17  ? 21.833  -14.218 0.796   1 69.4   ? 2   LEU   A O   1 
ATOM   30   C  CB  . LEU   A 1 17  ? 18.687  -14.522 -0.141  1 68.81  ? 2   LEU   A CB  1 
ATOM   31   C  CG  . LEU   A 1 17  ? 18.636  -13.146 -0.791  1 70.15  ? 2   LEU   A CG  1 
ATOM   32   C  CD1 . LEU   A 1 17  ? 19.01   -13.202 -2.277  1 70.53  ? 2   LEU   A CD1 1 
ATOM   33   C  CD2 . LEU   A 1 17  ? 17.257  -12.527 -0.608  1 70.88  ? 2   LEU   A CD2 1 
ATOM   34   N  N   . PHE   A 1 18  ? 20.766  -15.784 2.021   1 69.12  ? 3   PHE   A N   1 
ATOM   35   C  CA  . PHE   A 1 18  ? 21.607  -15.599 3.205   1 69.28  ? 3   PHE   A CA  1 
ATOM   36   C  C   . PHE   A 1 18  ? 22.884  -16.433 3.235   1 69.09  ? 3   PHE   A C   1 
ATOM   37   O  O   . PHE   A 1 18  ? 23.866  -15.987 3.827   1 69.48  ? 3   PHE   A O   1 
ATOM   38   C  CB  . PHE   A 1 18  ? 20.824  -15.861 4.491   1 69.52  ? 3   PHE   A CB  1 
ATOM   39   C  CG  . PHE   A 1 18  ? 19.563  -15.053 4.664   1 70.86  ? 3   PHE   A CG  1 
ATOM   40   C  CD1 . PHE   A 1 18  ? 19.512  -13.727 4.281   1 71.79  ? 3   PHE   A CD1 1 
ATOM   41   C  CD2 . PHE   A 1 18  ? 18.44   -15.609 5.25    1 71.82  ? 3   PHE   A CD2 1 
ATOM   42   C  CE1 . PHE   A 1 18  ? 18.35   -12.992 4.433   1 72.32  ? 3   PHE   A CE1 1 
ATOM   43   C  CE2 . PHE   A 1 18  ? 17.285  -14.858 5.42    1 72.45  ? 3   PHE   A CE2 1 
ATOM   44   C  CZ  . PHE   A 1 18  ? 17.247  -13.558 5.004   1 72.13  ? 3   PHE   A CZ  1 
ATOM   45   N  N   . GLN   A 1 19  ? 22.872  -17.651 2.682   1 68.39  ? 4   GLN   A N   1 
ATOM   46   C  CA  . GLN   A 1 19  ? 24.057  -18.516 2.731   1 68.51  ? 4   GLN   A CA  1 
ATOM   47   C  C   . GLN   A 1 19  ? 24.736  -18.748 1.361   1 68.4   ? 4   GLN   A C   1 
ATOM   48   O  O   . GLN   A 1 19  ? 25.776  -19.394 1.308   1 68.87  ? 4   GLN   A O   1 
ATOM   49   C  CB  . GLN   A 1 19  ? 23.75   -19.853 3.432   1 69.88  ? 4   GLN   A CB  1 
ATOM   50   N  N   . GLY   A 1 20  ? 24.182  -18.18  0.294   1 67.77  ? 5   GLY   A N   1 
ATOM   51   C  CA  . GLY   A 1 20  ? 24.743  -18.257 -1.048  1 67.62  ? 5   GLY   A CA  1 
ATOM   52   C  C   . GLY   A 1 20  ? 24.198  -19.388 -1.892  1 67.37  ? 5   GLY   A C   1 
ATOM   53   O  O   . GLY   A 1 20  ? 23.365  -20.177 -1.441  1 66.84  ? 5   GLY   A O   1 
ATOM   54   N  N   . PRO   A 1 21  ? 24.664  -19.48  -3.147  1 67.55  ? 6   PRO   A N   1 
ATOM   55   C  CA  . PRO   A 1 21  ? 24.219  -20.584 -4.014  1 68.05  ? 6   PRO   A CA  1 
ATOM   56   C  C   . PRO   A 1 21  ? 24.69   -21.957 -3.52   1 69.25  ? 6   PRO   A C   1 
ATOM   57   O  O   . PRO   A 1 21  ? 25.892  -22.212 -3.355  1 69.68  ? 6   PRO   A O   1 
ATOM   58   C  CB  . PRO   A 1 21  ? 24.84   -20.247 -5.378  1 68.23  ? 6   PRO   A CB  1 
ATOM   59   C  CG  . PRO   A 1 21  ? 25.316  -18.842 -5.273  1 68.38  ? 6   PRO   A CG  1 
ATOM   60   C  CD  . PRO   A 1 21  ? 25.637  -18.613 -3.831  1 66.71  ? 6   PRO   A CD  1 
ATOM   61   N  N   . HIS   A 1 22  ? 23.734  -22.837 -3.265  1 69.79  ? 7   HIS   A N   1 
ATOM   62   C  CA  . HIS   A 1 22  ? 24.027  -24.191 -2.825  1 71.13  ? 7   HIS   A CA  1 
ATOM   63   C  C   . HIS   A 1 22  ? 22.84   -25.049 -3.143  1 71.18  ? 7   HIS   A C   1 
ATOM   64   O  O   . HIS   A 1 22  ? 21.753  -24.779 -2.642  1 71.74  ? 7   HIS   A O   1 
ATOM   65   C  CB  . HIS   A 1 22  ? 24.396  -24.267 -1.33   1 73.36  ? 7   HIS   A CB  1 
ATOM   66   C  CG  . HIS   A 1 22  ? 23.569  -23.406 -0.42   1 77.56  ? 7   HIS   A CG  1 
ATOM   67   N  ND1 . HIS   A 1 22  ? 22.202  -23.598 -0.279  1 79.68  ? 7   HIS   A ND1 1 
ATOM   68   C  CD2 . HIS   A 1 22  ? 23.957  -22.414 0.413   1 79.21  ? 7   HIS   A CD2 1 
ATOM   69   C  CE1 . HIS   A 1 22  ? 21.798  -22.689 0.587   1 80.49  ? 7   HIS   A CE1 1 
ATOM   70   N  NE2 . HIS   A 1 22  ? 22.816  -21.946 1.025   1 80.63  ? 7   HIS   A NE2 1 
ATOM   71   N  N   . MET   A 1 23  ? 23.012  -26.035 -4.022  1 70.74  ? 8   MET   A N   1 
ATOM   72   C  CA  . MET   A 1 23  ? 21.898  -26.892 -4.381  1 70.94  ? 8   MET   A CA  1 
ATOM   73   C  C   . MET   A 1 23  ? 22.032  -28.249 -3.751  1 71.55  ? 8   MET   A C   1 
ATOM   74   O  O   . MET   A 1 23  ? 22.336  -29.225 -4.438  1 71.56  ? 8   MET   A O   1 
ATOM   75   C  CB  . MET   A 1 23  ? 21.723  -26.977 -5.889  1 71.27  ? 8   MET   A CB  1 
ATOM   76   C  CG  . MET   A 1 23  ? 20.329  -27.339 -6.296  1 72.74  ? 8   MET   A CG  1 
ATOM   77   S  SD  . MET   A 1 23  ? 20.134  -26.983 -8.039  1 77.42  ? 8   MET   A SD  1 
ATOM   78   C  CE  . MET   A 1 23  ? 19.186  -25.508 -7.957  1 73.83  ? 8   MET   A CE  1 
ATOM   79   N  N   . TRP   A 1 24  ? 21.824  -28.318 -2.423  1 71.97  ? 9   TRP   A N   1 
ATOM   80   C  CA  . TRP   A 1 24  ? 21.885  -29.604 -1.702  1 72.35  ? 9   TRP   A CA  1 
ATOM   81   C  C   . TRP   A 1 24  ? 20.612  -30.437 -1.85   1 70.17  ? 9   TRP   A C   1 
ATOM   82   O  O   . TRP   A 1 24  ? 20.596  -31.607 -1.471  1 70.17  ? 9   TRP   A O   1 
ATOM   83   C  CB  . TRP   A 1 24  ? 22.2    -29.422 -0.202  1 73.64  ? 9   TRP   A CB  1 
ATOM   84   C  CG  . TRP   A 1 24  ? 23.25   -28.413 0.187   1 75.64  ? 9   TRP   A CG  1 
ATOM   85   C  CD1 . TRP   A 1 24  ? 23.235  -27.62  1.3     1 77.2   ? 9   TRP   A CD1 1 
ATOM   86   C  CD2 . TRP   A 1 24  ? 24.518  -28.186 -0.448  1 76.28  ? 9   TRP   A CD2 1 
ATOM   87   N  NE1 . TRP   A 1 24  ? 24.391  -26.879 1.374   1 77.7   ? 9   TRP   A NE1 1 
ATOM   88   C  CE2 . TRP   A 1 24  ? 25.195  -27.205 0.311   1 77.43  ? 9   TRP   A CE2 1 
ATOM   89   C  CE3 . TRP   A 1 24  ? 25.12   -28.667 -1.617  1 76.82  ? 9   TRP   A CE3 1 
ATOM   90   C  CZ2 . TRP   A 1 24  ? 26.445  -26.715 -0.054  1 78.08  ? 9   TRP   A CZ2 1 
ATOM   91   C  CZ3 . TRP   A 1 24  ? 26.346  -28.166 -1.983  1 77.93  ? 9   TRP   A CZ3 1 
ATOM   92   C  CH2 . TRP   A 1 24  ? 26.99   -27.194 -1.214  1 78.25  ? 9   TRP   A CH2 1 
ATOM   93   N  N   . THR   A 1 25  ? 19.542  -29.823 -2.369  1 68.38  ? 10  THR   A N   1 
ATOM   94   C  CA  . THR   A 1 25  ? 18.251  -30.428 -2.618  1 67.3   ? 10  THR   A CA  1 
ATOM   95   C  C   . THR   A 1 25  ? 17.474  -29.602 -3.646  1 65.25  ? 10  THR   A C   1 
ATOM   96   O  O   . THR   A 1 25  ? 17.638  -28.378 -3.717  1 65.57  ? 10  THR   A O   1 
ATOM   97   C  CB  . THR   A 1 25  ? 17.473  -30.513 -1.312  1 69.55  ? 10  THR   A CB  1 
ATOM   98   O  OG1 . THR   A 1 25  ? 16.308  -31.318 -1.521  1 71.85  ? 10  THR   A OG1 1 
ATOM   99   C  CG2 . THR   A 1 25  ? 17.116  -29.133 -0.747  1 69.69  ? 10  THR   A CG2 1 
ATOM   100  N  N   . ILE   A 1 26  ? 16.628  -30.267 -4.456  1 63.18  ? 11  ILE   A N   1 
ATOM   101  C  CA  . ILE   A 1 26  ? 15.801  -29.54  -5.413  1 61.5   ? 11  ILE   A CA  1 
ATOM   102  C  C   . ILE   A 1 26  ? 14.49   -29.151 -4.751  1 60.58  ? 11  ILE   A C   1 
ATOM   103  O  O   . ILE   A 1 26  ? 13.631  -30.001 -4.494  1 60.49  ? 11  ILE   A O   1 
ATOM   104  C  CB  . ILE   A 1 26  ? 15.59   -30.264 -6.751  1 61.12  ? 11  ILE   A CB  1 
ATOM   105  C  CG1 . ILE   A 1 26  ? 16.948  -30.578 -7.384  1 61.35  ? 11  ILE   A CG1 1 
ATOM   106  C  CG2 . ILE   A 1 26  ? 14.728  -29.393 -7.675  1 61.26  ? 11  ILE   A CG2 1 
ATOM   107  C  CD1 . ILE   A 1 26  ? 16.904  -31.594 -8.322  1 61.93  ? 11  ILE   A CD1 1 
ATOM   108  N  N   . SER   A 1 27  ? 14.339  -27.856 -4.464  1 59.65  ? 12  SER   A N   1 
ATOM   109  C  CA  . SER   A 1 27  ? 13.145  -27.349 -3.819  1 59.01  ? 12  SER   A CA  1 
ATOM   110  C  C   . SER   A 1 27  ? 11.942  -27.444 -4.727  1 58.23  ? 12  SER   A C   1 
ATOM   111  O  O   . SER   A 1 27  ? 12.072  -27.355 -5.956  1 58.86  ? 12  SER   A O   1 
ATOM   112  C  CB  . SER   A 1 27  ? 13.343  -25.912 -3.352  1 60.79  ? 12  SER   A CB  1 
ATOM   113  O  OG  . SER   A 1 27  ? 13.202  -24.973 -4.401  1 64.08  ? 12  SER   A OG  1 
ATOM   114  N  N   . LYS   A 1 28  ? 10.763  -27.631 -4.109  1 56.45  ? 13  LYS   A N   1 
ATOM   115  C  CA  . LYS   A 1 28  ? 9.49    -27.694 -4.802  1 55.13  ? 13  LYS   A CA  1 
ATOM   116  C  C   . LYS   A 1 28  ? 9.207   -26.393 -5.59   1 53.96  ? 13  LYS   A C   1 
ATOM   117  O  O   . LYS   A 1 28  ? 8.505   -26.427 -6.598  1 53.92  ? 13  LYS   A O   1 
ATOM   118  C  CB  . LYS   A 1 28  ? 8.377   -27.983 -3.796  1 56.9   ? 13  LYS   A CB  1 
ATOM   119  N  N   . GLU   A 1 29  ? 9.797   -25.261 -5.15   1 53     ? 14  GLU   A N   1 
ATOM   120  C  CA  . GLU   A 1 29  ? 9.677   -23.963 -5.785  1 52.3   ? 14  GLU   A CA  1 
ATOM   121  C  C   . GLU   A 1 29  ? 10.237  -23.942 -7.229  1 52.32  ? 14  GLU   A C   1 
ATOM   122  O  O   . GLU   A 1 29  ? 9.921   -23.025 -7.989  1 52.43  ? 14  GLU   A O   1 
ATOM   123  C  CB  . GLU   A 1 29  ? 10.298  -22.885 -4.897  1 52.85  ? 14  GLU   A CB  1 
ATOM   124  N  N   . TYR   A 1 30  ? 11.017  -24.962 -7.626  1 52.05  ? 15  TYR   A N   1 
ATOM   125  C  CA  . TYR   A 1 30  ? 11.522  -25.054 -9      1 52.41  ? 15  TYR   A CA  1 
ATOM   126  C  C   . TYR   A 1 30  ? 10.558  -25.755 -9.955  1 53.28  ? 15  TYR   A C   1 
ATOM   127  O  O   . TYR   A 1 30  ? 10.823  -25.764 -11.152 1 53.98  ? 15  TYR   A O   1 
ATOM   128  C  CB  . TYR   A 1 30  ? 12.882  -25.739 -9.062  1 51.97  ? 15  TYR   A CB  1 
ATOM   129  C  CG  . TYR   A 1 30  ? 13.997  -24.896 -8.499  1 52.34  ? 15  TYR   A CG  1 
ATOM   130  C  CD1 . TYR   A 1 30  ? 14.339  -23.68  -9.077  1 52.93  ? 15  TYR   A CD1 1 
ATOM   131  C  CD2 . TYR   A 1 30  ? 14.724  -25.32  -7.396  1 52.81  ? 15  TYR   A CD2 1 
ATOM   132  C  CE1 . TYR   A 1 30  ? 15.383  -22.913 -8.576  1 53.59  ? 15  TYR   A CE1 1 
ATOM   133  C  CE2 . TYR   A 1 30  ? 15.77   -24.565 -6.89   1 53.29  ? 15  TYR   A CE2 1 
ATOM   134  C  CZ  . TYR   A 1 30  ? 16.107  -23.37  -7.49   1 54.13  ? 15  TYR   A CZ  1 
ATOM   135  O  OH  . TYR   A 1 30  ? 17.144  -22.643 -6.973  1 55.41  ? 15  TYR   A OH  1 
ATOM   136  N  N   . HIS   A 1 31  ? 9.465   -26.353 -9.44   1 53.31  ? 16  HIS   A N   1 
ATOM   137  C  CA  . HIS   A 1 31  ? 8.416   -27.02  -10.216 1 53.85  ? 16  HIS   A CA  1 
ATOM   138  C  C   . HIS   A 1 31  ? 8.939   -28.152 -11.085 1 54.4   ? 16  HIS   A C   1 
ATOM   139  O  O   . HIS   A 1 31  ? 8.529   -28.308 -12.236 1 54.54  ? 16  HIS   A O   1 
ATOM   140  C  CB  . HIS   A 1 31  ? 7.585   -26.008 -11.025 1 54.69  ? 16  HIS   A CB  1 
ATOM   141  C  CG  . HIS   A 1 31  ? 6.799   -25.082 -10.145 1 57.57  ? 16  HIS   A CG  1 
ATOM   142  N  ND1 . HIS   A 1 31  ? 7.426   -24.209 -9.279  1 59.39  ? 16  HIS   A ND1 1 
ATOM   143  C  CD2 . HIS   A 1 31  ? 5.461   -24.979 -9.966  1 59.04  ? 16  HIS   A CD2 1 
ATOM   144  C  CE1 . HIS   A 1 31  ? 6.459   -23.583 -8.629  1 59.51  ? 16  HIS   A CE1 1 
ATOM   145  N  NE2 . HIS   A 1 31  ? 5.264   -24.017 -9.001  1 59.76  ? 16  HIS   A NE2 1 
ATOM   146  N  N   . ILE   A 1 32  ? 9.826   -28.964 -10.511 1 54.54  ? 17  ILE   A N   1 
ATOM   147  C  CA  . ILE   A 1 32  ? 10.354  -30.158 -11.156 1 54.69  ? 17  ILE   A CA  1 
ATOM   148  C  C   . ILE   A 1 32  ? 9.714   -31.362 -10.46  1 55.73  ? 17  ILE   A C   1 
ATOM   149  O  O   . ILE   A 1 32  ? 9.76    -31.476 -9.233  1 56.44  ? 17  ILE   A O   1 
ATOM   150  C  CB  . ILE   A 1 32  ? 11.899  -30.217 -11.078 1 54.14  ? 17  ILE   A CB  1 
ATOM   151  C  CG1 . ILE   A 1 32  ? 12.541  -28.95  -11.678 1 54.14  ? 17  ILE   A CG1 1 
ATOM   152  C  CG2 . ILE   A 1 32  ? 12.409  -31.492 -11.749 1 54.33  ? 17  ILE   A CG2 1 
ATOM   153  C  CD1 . ILE   A 1 32  ? 14.026  -28.889 -11.527 1 55.25  ? 17  ILE   A CD1 1 
ATOM   154  N  N   . ASP   A 1 33  ? 9.111   -32.247 -11.233 1 55.74  ? 18  ASP   A N   1 
ATOM   155  C  CA  . ASP   A 1 33  ? 8.444   -33.427 -10.724 1 56.39  ? 18  ASP   A CA  1 
ATOM   156  C  C   . ASP   A 1 33  ? 9.41    -34.596 -10.55  1 57.09  ? 18  ASP   A C   1 
ATOM   157  O  O   . ASP   A 1 33  ? 10.337  -34.76  -11.342 1 57.82  ? 18  ASP   A O   1 
ATOM   158  C  CB  . ASP   A 1 33  ? 7.326   -33.807 -11.688 1 58.28  ? 18  ASP   A CB  1 
ATOM   159  C  CG  . ASP   A 1 33  ? 6.356   -34.79  -11.106 1 63.26  ? 18  ASP   A CG  1 
ATOM   160  O  OD1 . ASP   A 1 33  ? 5.642   -34.415 -10.151 1 64.32  ? 18  ASP   A OD1 1 
ATOM   161  O  OD2 . ASP   A 1 33  ? 6.316   -35.946 -11.595 1 65.13  ? 18  ASP   A OD2 1 
ATOM   162  N  N   . GLU   A 1 34  ? 9.188   -35.422 -9.526  1 56.73  ? 19  GLU   A N   1 
ATOM   163  C  CA  . GLU   A 1 34  ? 10.028  -36.585 -9.279  1 56.73  ? 19  GLU   A CA  1 
ATOM   164  C  C   . GLU   A 1 34  ? 9.954   -37.595 -10.442 1 56.76  ? 19  GLU   A C   1 
ATOM   165  O  O   . GLU   A 1 34  ? 10.949  -38.239 -10.773 1 57.11  ? 19  GLU   A O   1 
ATOM   166  C  CB  . GLU   A 1 34  ? 9.609   -37.259 -7.964  1 58.56  ? 19  GLU   A CB  1 
ATOM   167  N  N   . GLU   A 1 35  ? 8.787   -37.711 -11.069 1 56.27  ? 20  GLU   A N   1 
ATOM   168  C  CA  . GLU   A 1 35  ? 8.553   -38.659 -12.148 1 56.46  ? 20  GLU   A CA  1 
ATOM   169  C  C   . GLU   A 1 35  ? 8.724   -38.077 -13.562 1 56.05  ? 20  GLU   A C   1 
ATOM   170  O  O   . GLU   A 1 35  ? 9.465   -38.649 -14.365 1 56.09  ? 20  GLU   A O   1 
ATOM   171  C  CB  . GLU   A 1 35  ? 7.163   -39.289 -11.975 1 58.98  ? 20  GLU   A CB  1 
ATOM   172  C  CG  . GLU   A 1 35  ? 6.791   -40.325 -13.019 1 64.93  ? 20  GLU   A CG  1 
ATOM   173  C  CD  . GLU   A 1 35  ? 5.35    -40.8   -12.908 1 72.9   ? 20  GLU   A CD  1 
ATOM   174  O  OE1 . GLU   A 1 35  ? 5.076   -41.951 -13.318 1 75.21  ? 20  GLU   A OE1 1 
ATOM   175  O  OE2 . GLU   A 1 35  ? 4.497   -40.031 -12.403 1 74.68  ? 20  GLU   A OE2 1 
ATOM   176  N  N   . VAL   A 1 36  ? 8.049   -36.953 -13.875 1 55.21  ? 21  VAL   A N   1 
ATOM   177  C  CA  . VAL   A 1 36  ? 8.117   -36.386 -15.231 1 54.73  ? 21  VAL   A CA  1 
ATOM   178  C  C   . VAL   A 1 36  ? 9.098   -35.188 -15.387 1 53.74  ? 21  VAL   A C   1 
ATOM   179  O  O   . VAL   A 1 36  ? 9.251   -34.683 -16.496 1 53.56  ? 21  VAL   A O   1 
ATOM   180  C  CB  . VAL   A 1 36  ? 6.703   -36.032 -15.775 1 55.07  ? 21  VAL   A CB  1 
ATOM   181  C  CG1 . VAL   A 1 36  ? 5.809   -37.263 -15.799 1 55.29  ? 21  VAL   A CG1 1 
ATOM   182  C  CG2 . VAL   A 1 36  ? 6.059   -34.944 -14.947 1 55.5   ? 21  VAL   A CG2 1 
ATOM   183  N  N   . GLY   A 1 37  ? 9.755   -34.779 -14.304 1 52.79  ? 22  GLY   A N   1 
ATOM   184  C  CA  . GLY   A 1 37  ? 10.73   -33.698 -14.32  1 52.57  ? 22  GLY   A CA  1 
ATOM   185  C  C   . GLY   A 1 37  ? 10.199  -32.332 -14.71  1 52.38  ? 22  GLY   A C   1 
ATOM   186  O  O   . GLY   A 1 37  ? 9.363   -31.759 -14.006 1 52.91  ? 22  GLY   A O   1 
ATOM   187  N  N   . PHE   A 1 38  ? 10.683  -31.793 -15.838 1 51.23  ? 23  PHE   A N   1 
ATOM   188  C  CA  . PHE   A 1 38  ? 10.225  -30.494 -16.314 1 50.15  ? 23  PHE   A CA  1 
ATOM   189  C  C   . PHE   A 1 38  ? 8.833   -30.546 -16.945 1 50.8   ? 23  PHE   A C   1 
ATOM   190  O  O   . PHE   A 1 38  ? 8.179   -29.514 -17.025 1 51.47  ? 23  PHE   A O   1 
ATOM   191  C  CB  . PHE   A 1 38  ? 11.25   -29.851 -17.241 1 48.85  ? 23  PHE   A CB  1 
ATOM   192  C  CG  . PHE   A 1 38  ? 12.476  -29.365 -16.508 1 47.96  ? 23  PHE   A CG  1 
ATOM   193  C  CD1 . PHE   A 1 38  ? 12.411  -28.273 -15.669 1 48     ? 23  PHE   A CD1 1 
ATOM   194  C  CD2 . PHE   A 1 38  ? 13.694  -30.005 -16.659 1 48.15  ? 23  PHE   A CD2 1 
ATOM   195  C  CE1 . PHE   A 1 38  ? 13.544  -27.819 -15.007 1 48.37  ? 23  PHE   A CE1 1 
ATOM   196  C  CE2 . PHE   A 1 38  ? 14.827  -29.546 -15.992 1 48.49  ? 23  PHE   A CE2 1 
ATOM   197  C  CZ  . PHE   A 1 38  ? 14.742  -28.46  -15.168 1 47.87  ? 23  PHE   A CZ  1 
ATOM   198  N  N   . ALA   A 1 39  ? 8.353   -31.735 -17.353 1 50.79  ? 24  ALA   A N   1 
ATOM   199  C  CA  . ALA   A 1 39  ? 6.998   -31.87  -17.886 1 51.23  ? 24  ALA   A CA  1 
ATOM   200  C  C   . ALA   A 1 39  ? 5.968   -31.558 -16.801 1 52.04  ? 24  ALA   A C   1 
ATOM   201  O  O   . ALA   A 1 39  ? 6.252   -31.679 -15.598 1 52.07  ? 24  ALA   A O   1 
ATOM   202  C  CB  . ALA   A 1 39  ? 6.772   -33.274 -18.427 1 51.18  ? 24  ALA   A CB  1 
ATOM   203  N  N   . LEU   A 1 40  ? 4.79    -31.096 -17.223 1 52.43  ? 25  LEU   A N   1 
ATOM   204  C  CA  . LEU   A 1 40  ? 3.73    -30.789 -16.279 1 53.45  ? 25  LEU   A CA  1 
ATOM   205  C  C   . LEU   A 1 40  ? 3.127   -32.131 -15.866 1 54.69  ? 25  LEU   A C   1 
ATOM   206  O  O   . LEU   A 1 40  ? 2.72    -32.908 -16.728 1 54.57  ? 25  LEU   A O   1 
ATOM   207  C  CB  . LEU   A 1 40  ? 2.68    -29.899 -16.947 1 53.65  ? 25  LEU   A CB  1 
ATOM   208  C  CG  . LEU   A 1 40  ? 1.502   -29.497 -16.08  1 54.8   ? 25  LEU   A CG  1 
ATOM   209  C  CD1 . LEU   A 1 40  ? 1.892   -28.437 -15.099 1 54.49  ? 25  LEU   A CD1 1 
ATOM   210  C  CD2 . LEU   A 1 40  ? 0.352   -29.023 -16.935 1 55.77  ? 25  LEU   A CD2 1 
ATOM   211  N  N   . PRO   A 1 41  ? 3.157   -32.472 -14.568 1 55.65  ? 26  PRO   A N   1 
ATOM   212  C  CA  . PRO   A 1 41  ? 2.59    -33.764 -14.145 1 56.52  ? 26  PRO   A CA  1 
ATOM   213  C  C   . PRO   A 1 41  ? 1.081   -33.759 -14.279 1 58.21  ? 26  PRO   A C   1 
ATOM   214  O  O   . PRO   A 1 41  ? 0.455   -32.736 -14.007 1 58.5   ? 26  PRO   A O   1 
ATOM   215  C  CB  . PRO   A 1 41  ? 3.021   -33.877 -12.683 1 56.66  ? 26  PRO   A CB  1 
ATOM   216  C  CG  . PRO   A 1 41  ? 3.183   -32.47  -12.228 1 56.7   ? 26  PRO   A CG  1 
ATOM   217  C  CD  . PRO   A 1 41  ? 3.629   -31.672 -13.42  1 55.1   ? 26  PRO   A CD  1 
ATOM   218  N  N   . ASN   A 1 42  ? 0.492   -34.87  -14.771 1 59.13  ? 27  ASN   A N   1 
ATOM   219  C  CA  . ASN   A 1 42  ? -0.951  -35.045 -14.986 1 60.45  ? 27  ASN   A CA  1 
ATOM   220  C  C   . ASN   A 1 42  ? -1.658  -33.783 -15.476 1 61.11  ? 27  ASN   A C   1 
ATOM   221  O  O   . ASN   A 1 42  ? -2.309  -33.097 -14.683 1 61.71  ? 27  ASN   A O   1 
ATOM   222  C  CB  . ASN   A 1 42  ? -1.624  -35.58  -13.715 1 63.02  ? 27  ASN   A CB  1 
ATOM   223  C  CG  . ASN   A 1 42  ? -3.094  -35.943 -13.892 1 68.06  ? 27  ASN   A CG  1 
ATOM   224  O  OD1 . ASN   A 1 42  ? -3.536  -36.371 -14.977 1 69.6   ? 27  ASN   A OD1 1 
ATOM   225  N  ND2 . ASN   A 1 42  ? -3.887  -35.781 -12.825 1 68.71  ? 27  ASN   A ND2 1 
ATOM   226  N  N   . PRO   A 1 43  ? -1.441  -33.387 -16.737 1 61.05  ? 28  PRO   A N   1 
ATOM   227  C  CA  . PRO   A 1 43  ? -2.07   -32.157 -17.226 1 61.14  ? 28  PRO   A CA  1 
ATOM   228  C  C   . PRO   A 1 43  ? -3.591  -32.283 -17.304 1 61.72  ? 28  PRO   A C   1 
ATOM   229  O  O   . PRO   A 1 43  ? -4.14   -33.386 -17.426 1 61.58  ? 28  PRO   A O   1 
ATOM   230  C  CB  . PRO   A 1 43  ? -1.421  -31.951 -18.604 1 61.66  ? 28  PRO   A CB  1 
ATOM   231  C  CG  . PRO   A 1 43  ? -0.241  -32.874 -18.638 1 61.96  ? 28  PRO   A CG  1 
ATOM   232  C  CD  . PRO   A 1 43  ? -0.653  -34.035 -17.796 1 60.52  ? 28  PRO   A CD  1 
ATOM   233  N  N   . GLN   A 1 44  ? -4.271  -31.144 -17.197 1 62.16  ? 29  GLN   A N   1 
ATOM   234  C  CA  . GLN   A 1 44  ? -5.721  -31.064 -17.271 1 63.14  ? 29  GLN   A CA  1 
ATOM   235  C  C   . GLN   A 1 44  ? -6.188  -31.285 -18.704 1 64.24  ? 29  GLN   A C   1 
ATOM   236  O  O   . GLN   A 1 44  ? -5.626  -30.697 -19.619 1 64.69  ? 29  GLN   A O   1 
ATOM   237  C  CB  . GLN   A 1 44  ? -6.182  -29.689 -16.794 1 64.8   ? 29  GLN   A CB  1 
ATOM   238  C  CG  . GLN   A 1 44  ? -7.534  -29.725 -16.11  1 69.76  ? 29  GLN   A CG  1 
ATOM   239  C  CD  . GLN   A 1 44  ? -7.826  -28.391 -15.496 1 76.54  ? 29  GLN   A CD  1 
ATOM   240  O  OE1 . GLN   A 1 44  ? -7.201  -28.004 -14.499 1 79.54  ? 29  GLN   A OE1 1 
ATOM   241  N  NE2 . GLN   A 1 44  ? -8.768  -27.654 -16.092 1 77.05  ? 29  GLN   A NE2 1 
ATOM   242  N  N   . GLU   A 1 45  ? -7.211  -32.115 -18.904 1 64.55  ? 30  GLU   A N   1 
ATOM   243  C  CA  . GLU   A 1 45  ? -7.721  -32.401 -20.238 1 65.59  ? 30  GLU   A CA  1 
ATOM   244  C  C   . GLU   A 1 45  ? -8.842  -31.475 -20.662 1 66.35  ? 30  GLU   A C   1 
ATOM   245  O  O   . GLU   A 1 45  ? -8.982  -31.216 -21.857 1 66.38  ? 30  GLU   A O   1 
ATOM   246  C  CB  . GLU   A 1 45  ? -8.242  -33.831 -20.312 1 68.61  ? 30  GLU   A CB  1 
ATOM   247  C  CG  . GLU   A 1 45  ? -7.206  -34.883 -20.01  1 75.66  ? 30  GLU   A CG  1 
ATOM   248  C  CD  . GLU   A 1 45  ? -7.673  -36.266 -20.404 1 86.06  ? 30  GLU   A CD  1 
ATOM   249  O  OE1 . GLU   A 1 45  ? -8.434  -36.386 -21.395 1 88     ? 30  GLU   A OE1 1 
ATOM   250  O  OE2 . GLU   A 1 45  ? -7.271  -37.234 -19.719 1 89.71  ? 30  GLU   A OE2 1 
ATOM   251  N  N   . ASN   A 1 46  ? -9.689  -31.039 -19.707 1 66.47  ? 31  ASN   A N   1 
ATOM   252  C  CA  . ASN   A 1 46  ? -10.836 -30.19  -20.02  1 66.94  ? 31  ASN   A CA  1 
ATOM   253  C  C   . ASN   A 1 46  ? -10.873 -28.913 -19.189 1 67     ? 31  ASN   A C   1 
ATOM   254  O  O   . ASN   A 1 46  ? -10.541 -28.913 -18     1 66.77  ? 31  ASN   A O   1 
ATOM   255  C  CB  . ASN   A 1 46  ? -12.167 -30.949 -19.84  1 68.41  ? 31  ASN   A CB  1 
ATOM   256  C  CG  . ASN   A 1 46  ? -12.165 -32.393 -20.285 1 72.29  ? 31  ASN   A CG  1 
ATOM   257  O  OD1 . ASN   A 1 46  ? -12.149 -32.715 -21.484 1 73.52  ? 31  ASN   A OD1 1 
ATOM   258  N  ND2 . ASN   A 1 46  ? -12.2   -33.296 -19.317 1 73.07  ? 31  ASN   A ND2 1 
ATOM   259  N  N   . LEU   A 1 47  ? -11.291 -27.824 -19.827 1 67.16  ? 32  LEU   A N   1 
ATOM   260  C  CA  . LEU   A 1 47  ? -11.446 -26.524 -19.182 1 67.9   ? 32  LEU   A CA  1 
ATOM   261  C  C   . LEU   A 1 47  ? -12.86  -26.422 -18.57  1 69.67  ? 32  LEU   A C   1 
ATOM   262  O  O   . LEU   A 1 47  ? -13.766 -27.155 -18.995 1 70.28  ? 32  LEU   A O   1 
ATOM   263  C  CB  . LEU   A 1 47  ? -11.27  -25.406 -20.24  1 67.29  ? 32  LEU   A CB  1 
ATOM   264  C  CG  . LEU   A 1 47  ? -9.834  -25.039 -20.633 1 67.7   ? 32  LEU   A CG  1 
ATOM   265  C  CD1 . LEU   A 1 47  ? -9.812  -23.966 -21.697 1 67.45  ? 32  LEU   A CD1 1 
ATOM   266  C  CD2 . LEU   A 1 47  ? -9.004  -24.622 -19.42  1 68.12  ? 32  LEU   A CD2 1 
ATOM   267  N  N   . PRO   A 1 48  ? -13.111 -25.491 -17.615 1 70.25  ? 33  PRO   A N   1 
ATOM   268  C  CA  . PRO   A 1 48  ? -14.496 -25.32  -17.119 1 70.79  ? 33  PRO   A CA  1 
ATOM   269  C  C   . PRO   A 1 48  ? -15.465 -24.97  -18.268 1 71.76  ? 33  PRO   A C   1 
ATOM   270  O  O   . PRO   A 1 48  ? -15.056 -24.378 -19.273 1 72.23  ? 33  PRO   A O   1 
ATOM   271  C  CB  . PRO   A 1 48  ? -14.381 -24.182 -16.101 1 71.15  ? 33  PRO   A CB  1 
ATOM   272  C  CG  . PRO   A 1 48  ? -13.082 -23.501 -16.409 1 71.49  ? 33  PRO   A CG  1 
ATOM   273  C  CD  . PRO   A 1 48  ? -12.178 -24.534 -16.984 1 69.68  ? 33  PRO   A CD  1 
ATOM   274  N  N   . ASP   A 1 49  ? -16.733 -25.369 -18.142 1 71.97  ? 34  ASP   A N   1 
ATOM   275  C  CA  . ASP   A 1 49  ? -17.761 -25.181 -19.171 1 72.45  ? 34  ASP   A CA  1 
ATOM   276  C  C   . ASP   A 1 49  ? -17.841 -23.739 -19.741 1 71.5   ? 34  ASP   A C   1 
ATOM   277  O  O   . ASP   A 1 49  ? -18.234 -23.558 -20.895 1 71.65  ? 34  ASP   A O   1 
ATOM   278  C  CB  . ASP   A 1 49  ? -19.123 -25.675 -18.652 1 75.55  ? 34  ASP   A CB  1 
ATOM   279  C  CG  . ASP   A 1 49  ? -19.219 -27.2   -18.629 1 82.75  ? 34  ASP   A CG  1 
ATOM   280  O  OD1 . ASP   A 1 49  ? -19.581 -27.791 -19.678 1 84.04  ? 34  ASP   A OD1 1 
ATOM   281  O  OD2 . ASP   A 1 49  ? -18.915 -27.805 -17.565 1 85.64  ? 34  ASP   A OD2 1 
ATOM   282  N  N   . PHE   A 1 50  ? -17.4   -22.74  -18.966 1 70.18  ? 35  PHE   A N   1 
ATOM   283  C  CA  . PHE   A 1 50  ? -17.343 -21.337 -19.381 1 69.82  ? 35  PHE   A CA  1 
ATOM   284  C  C   . PHE   A 1 50  ? -16.495 -21.137 -20.665 1 69.13  ? 35  PHE   A C   1 
ATOM   285  O  O   . PHE   A 1 50  ? -16.708 -20.171 -21.401 1 68.77  ? 35  PHE   A O   1 
ATOM   286  C  CB  . PHE   A 1 50  ? -16.738 -20.51  -18.227 1 69.83  ? 35  PHE   A CB  1 
ATOM   287  C  CG  . PHE   A 1 50  ? -16.711 -19.017 -18.429 1 70.86  ? 35  PHE   A CG  1 
ATOM   288  C  CD1 . PHE   A 1 50  ? -17.869 -18.264 -18.312 1 71.79  ? 35  PHE   A CD1 1 
ATOM   289  C  CD2 . PHE   A 1 50  ? -15.523 -18.356 -18.687 1 71.65  ? 35  PHE   A CD2 1 
ATOM   290  C  CE1 . PHE   A 1 50  ? -17.843 -16.886 -18.497 1 72.43  ? 35  PHE   A CE1 1 
ATOM   291  C  CE2 . PHE   A 1 50  ? -15.498 -16.975 -18.861 1 72.42  ? 35  PHE   A CE2 1 
ATOM   292  C  CZ  . PHE   A 1 50  ? -16.658 -16.25  -18.77  1 72.22  ? 35  PHE   A CZ  1 
ATOM   293  N  N   . TYR   A 1 51  ? -15.524 -22.057 -20.924 1 68.48  ? 36  TYR   A N   1 
ATOM   294  C  CA  . TYR   A 1 51  ? -14.608 -21.979 -22.065 1 67.59  ? 36  TYR   A CA  1 
ATOM   295  C  C   . TYR   A 1 51  ? -14.829 -23.063 -23.114 1 68.18  ? 36  TYR   A C   1 
ATOM   296  O  O   . TYR   A 1 51  ? -13.91  -23.353 -23.872 1 68.23  ? 36  TYR   A O   1 
ATOM   297  C  CB  . TYR   A 1 51  ? -13.158 -22.035 -21.581 1 66.4   ? 36  TYR   A CB  1 
ATOM   298  C  CG  . TYR   A 1 51  ? -12.793 -20.952 -20.59  1 65.28  ? 36  TYR   A CG  1 
ATOM   299  C  CD1 . TYR   A 1 51  ? -12.555 -19.656 -21.007 1 65.03  ? 36  TYR   A CD1 1 
ATOM   300  C  CD2 . TYR   A 1 51  ? -12.646 -21.238 -19.238 1 65.5   ? 36  TYR   A CD2 1 
ATOM   301  C  CE1 . TYR   A 1 51  ? -12.16  -18.674 -20.113 1 65.27  ? 36  TYR   A CE1 1 
ATOM   302  C  CE2 . TYR   A 1 51  ? -12.28  -20.256 -18.328 1 65.44  ? 36  TYR   A CE2 1 
ATOM   303  C  CZ  . TYR   A 1 51  ? -12.028 -18.977 -18.772 1 65.7   ? 36  TYR   A CZ  1 
ATOM   304  O  OH  . TYR   A 1 51  ? -11.7   -17.982 -17.89  1 66.45  ? 36  TYR   A OH  1 
ATOM   305  N  N   . ASN   A 1 52  ? -16.043 -23.634 -23.191 1 68.72  ? 37  ASN   A N   1 
ATOM   306  C  CA  . ASN   A 1 52  ? -16.363 -24.671 -24.181 1 69.6   ? 37  ASN   A CA  1 
ATOM   307  C  C   . ASN   A 1 52  ? -16.261 -24.171 -25.628 1 69.79  ? 37  ASN   A C   1 
ATOM   308  O  O   . ASN   A 1 52  ? -16.015 -24.974 -26.534 1 69.95  ? 37  ASN   A O   1 
ATOM   309  C  CB  . ASN   A 1 52  ? -17.728 -25.315 -23.913 1 71.29  ? 37  ASN   A CB  1 
ATOM   310  C  CG  . ASN   A 1 52  ? -17.744 -26.257 -22.726 1 75.83  ? 37  ASN   A CG  1 
ATOM   311  O  OD1 . ASN   A 1 52  ? -16.71  -26.584 -22.122 1 77.43  ? 37  ASN   A OD1 1 
ATOM   312  N  ND2 . ASN   A 1 52  ? -18.929 -26.711 -22.352 1 76.96  ? 37  ASN   A ND2 1 
ATOM   313  N  N   . ASP   A 1 53  ? -16.41  -22.855 -25.848 1 69.63  ? 38  ASP   A N   1 
ATOM   314  C  CA  . ASP   A 1 53  ? -16.281 -22.283 -27.187 1 70.33  ? 38  ASP   A CA  1 
ATOM   315  C  C   . ASP   A 1 53  ? -14.82  -22.309 -27.67  1 69.93  ? 38  ASP   A C   1 
ATOM   316  O  O   . ASP   A 1 53  ? -14.57  -22.463 -28.868 1 70.42  ? 38  ASP   A O   1 
ATOM   317  C  CB  . ASP   A 1 53  ? -16.859 -20.864 -27.241 1 73.14  ? 38  ASP   A CB  1 
ATOM   318  C  CG  . ASP   A 1 53  ? -18.376 -20.795 -27.362 1 79.4   ? 38  ASP   A CG  1 
ATOM   319  O  OD1 . ASP   A 1 53  ? -19.032 -21.876 -27.366 1 80.12  ? 38  ASP   A OD1 1 
ATOM   320  O  OD2 . ASP   A 1 53  ? -18.912 -19.666 -27.456 1 82.23  ? 38  ASP   A OD2 1 
ATOM   321  N  N   . TRP   A 1 54  ? -13.857 -22.178 -26.738 1 68.54  ? 39  TRP   A N   1 
ATOM   322  C  CA  . TRP   A 1 54  ? -12.438 -22.281 -27.068 1 67.36  ? 39  TRP   A CA  1 
ATOM   323  C  C   . TRP   A 1 54  ? -12.134 -23.76  -27.309 1 65.99  ? 39  TRP   A C   1 
ATOM   324  O  O   . TRP   A 1 54  ? -11.542 -24.109 -28.323 1 65.78  ? 39  TRP   A O   1 
ATOM   325  C  CB  . TRP   A 1 54  ? -11.573 -21.781 -25.893 1 67.18  ? 39  TRP   A CB  1 
ATOM   326  C  CG  . TRP   A 1 54  ? -11.571 -20.306 -25.638 1 67.29  ? 39  TRP   A CG  1 
ATOM   327  C  CD1 . TRP   A 1 54  ? -12.159 -19.332 -26.389 1 68.03  ? 39  TRP   A CD1 1 
ATOM   328  C  CD2 . TRP   A 1 54  ? -10.877 -19.635 -24.578 1 67.39  ? 39  TRP   A CD2 1 
ATOM   329  N  NE1 . TRP   A 1 54  ? -11.888 -18.094 -25.852 1 68.38  ? 39  TRP   A NE1 1 
ATOM   330  C  CE2 . TRP   A 1 54  ? -11.107 -18.254 -24.734 1 68.21  ? 39  TRP   A CE2 1 
ATOM   331  C  CE3 . TRP   A 1 54  ? -10.09  -20.069 -23.506 1 67.77  ? 39  TRP   A CE3 1 
ATOM   332  C  CZ2 . TRP   A 1 54  ? -10.55  -17.306 -23.876 1 68.83  ? 39  TRP   A CZ2 1 
ATOM   333  C  CZ3 . TRP   A 1 54  ? -9.548  -19.129 -22.655 1 68.62  ? 39  TRP   A CZ3 1 
ATOM   334  C  CH2 . TRP   A 1 54  ? -9.787  -17.767 -22.838 1 68.84  ? 39  TRP   A CH2 1 
ATOM   335  N  N   . MET   A 1 55  ? -12.57  -24.626 -26.377 1 65.11  ? 40  MET   A N   1 
ATOM   336  C  CA  . MET   A 1 55  ? -12.36  -26.064 -26.418 1 65.29  ? 40  MET   A CA  1 
ATOM   337  C  C   . MET   A 1 55  ? -12.863 -26.698 -27.687 1 65.2   ? 40  MET   A C   1 
ATOM   338  O  O   . MET   A 1 55  ? -12.247 -27.649 -28.162 1 65.49  ? 40  MET   A O   1 
ATOM   339  C  CB  . MET   A 1 55  ? -13.016 -26.763 -25.214 1 66.4   ? 40  MET   A CB  1 
ATOM   340  C  CG  . MET   A 1 55  ? -12.153 -26.834 -23.948 1 69.82  ? 40  MET   A CG  1 
ATOM   341  S  SD  . MET   A 1 55  ? -10.428 -27.367 -24.178 1 74.88  ? 40  MET   A SD  1 
ATOM   342  C  CE  . MET   A 1 55  ? -10.428 -28.908 -23.431 1 71.57  ? 40  MET   A CE  1 
ATOM   343  N  N   . PHE   A 1 56  ? -14     -26.215 -28.227 1 64.56  ? 41  PHE   A N   1 
ATOM   344  C  CA  . PHE   A 1 56  ? -14.547 -26.786 -29.45  1 64.01  ? 41  PHE   A CA  1 
ATOM   345  C  C   . PHE   A 1 56  ? -13.589 -26.535 -30.609 1 63.73  ? 41  PHE   A C   1 
ATOM   346  O  O   . PHE   A 1 56  ? -13.287 -27.46  -31.357 1 64.12  ? 41  PHE   A O   1 
ATOM   347  C  CB  . PHE   A 1 56  ? -15.97  -26.248 -29.761 1 63.79  ? 41  PHE   A CB  1 
ATOM   348  C  CG  . PHE   A 1 56  ? -16.422 -26.593 -31.171 1 63.89  ? 41  PHE   A CG  1 
ATOM   349  C  CD1 . PHE   A 1 56  ? -16.752 -27.894 -31.511 1 64.21  ? 41  PHE   A CD1 1 
ATOM   350  C  CD2 . PHE   A 1 56  ? -16.368 -25.647 -32.186 1 64.14  ? 41  PHE   A CD2 1 
ATOM   351  C  CE1 . PHE   A 1 56  ? -17.057 -28.231 -32.828 1 64.51  ? 41  PHE   A CE1 1 
ATOM   352  C  CE2 . PHE   A 1 56  ? -16.676 -25.991 -33.499 1 64.43  ? 41  PHE   A CE2 1 
ATOM   353  C  CZ  . PHE   A 1 56  ? -17.024 -27.275 -33.811 1 64.03  ? 41  PHE   A CZ  1 
ATOM   354  N  N   . ILE   A 1 57  ? -13.13  -25.286 -30.762 1 63.04  ? 42  ILE   A N   1 
ATOM   355  C  CA  . ILE   A 1 57  ? -12.219 -24.889 -31.838 1 62.83  ? 42  ILE   A CA  1 
ATOM   356  C  C   . ILE   A 1 57  ? -10.898 -25.642 -31.762 1 62.59  ? 42  ILE   A C   1 
ATOM   357  O  O   . ILE   A 1 57  ? -10.463 -26.209 -32.76  1 62.59  ? 42  ILE   A O   1 
ATOM   358  C  CB  . ILE   A 1 57  ? -11.999 -23.359 -31.821 1 63.11  ? 42  ILE   A CB  1 
ATOM   359  C  CG1 . ILE   A 1 57  ? -13.32  -22.622 -32.043 1 64.08  ? 42  ILE   A CG1 1 
ATOM   360  C  CG2 . ILE   A 1 57  ? -10.943 -22.942 -32.836 1 63.26  ? 42  ILE   A CG2 1 
ATOM   361  C  CD1 . ILE   A 1 57  ? -13.246 -21.169 -31.823 1 65.63  ? 42  ILE   A CD1 1 
ATOM   362  N  N   . ALA   A 1 58  ? -10.287 -25.683 -30.564 1 62.07  ? 43  ALA   A N   1 
ATOM   363  C  CA  . ALA   A 1 58  ? -9.007  -26.336 -30.31  1 61.2   ? 43  ALA   A CA  1 
ATOM   364  C  C   . ALA   A 1 58  ? -9.08   -27.838 -30.557 1 60.54  ? 43  ALA   A C   1 
ATOM   365  O  O   . ALA   A 1 58  ? -8.189  -28.394 -31.213 1 61.02  ? 43  ALA   A O   1 
ATOM   366  C  CB  . ALA   A 1 58  ? -8.548  -26.046 -28.889 1 60.95  ? 43  ALA   A CB  1 
ATOM   367  N  N   . LYS   A 1 59  ? -10.154 -28.49  -30.092 1 59.21  ? 44  LYS   A N   1 
ATOM   368  C  CA  . LYS   A 1 59  ? -10.3   -29.931 -30.314 1 58.39  ? 44  LYS   A CA  1 
ATOM   369  C  C   . LYS   A 1 59  ? -10.667 -30.284 -31.762 1 57.71  ? 44  LYS   A C   1 
ATOM   370  O  O   . LYS   A 1 59  ? -10.62  -31.457 -32.122 1 57.76  ? 44  LYS   A O   1 
ATOM   371  C  CB  . LYS   A 1 59  ? -11.277 -30.568 -29.308 1 59.41  ? 44  LYS   A CB  1 
ATOM   372  N  N   . HIS   A 1 60  ? -11.009 -29.288 -32.598 1 57.25  ? 45  HIS   A N   1 
ATOM   373  C  CA  . HIS   A 1 60  ? -11.401 -29.541 -33.982 1 57.41  ? 45  HIS   A CA  1 
ATOM   374  C  C   . HIS   A 1 60  ? -10.599 -28.744 -35.002 1 57.28  ? 45  HIS   A C   1 
ATOM   375  O  O   . HIS   A 1 60  ? -11.139 -28.347 -36.027 1 57.7   ? 45  HIS   A O   1 
ATOM   376  C  CB  . HIS   A 1 60  ? -12.912 -29.32  -34.177 1 57.76  ? 45  HIS   A CB  1 
ATOM   377  C  CG  . HIS   A 1 60  ? -13.745 -30.248 -33.359 1 59.34  ? 45  HIS   A CG  1 
ATOM   378  N  ND1 . HIS   A 1 60  ? -14.39  -29.818 -32.214 1 61.13  ? 45  HIS   A ND1 1 
ATOM   379  C  CD2 . HIS   A 1 60  ? -13.968 -31.569 -33.513 1 60.47  ? 45  HIS   A CD2 1 
ATOM   380  C  CE1 . HIS   A 1 60  ? -14.999 -30.884 -31.718 1 61.4   ? 45  HIS   A CE1 1 
ATOM   381  N  NE2 . HIS   A 1 60  ? -14.78  -31.959 -32.466 1 61.41  ? 45  HIS   A NE2 1 
ATOM   382  N  N   . LEU   A 1 61  ? -9.309  -28.537 -34.747 1 56.59  ? 46  LEU   A N   1 
ATOM   383  C  CA  . LEU   A 1 61  ? -8.45   -27.824 -35.688 1 56.41  ? 46  LEU   A CA  1 
ATOM   384  C  C   . LEU   A 1 61  ? -8.316  -28.556 -37.034 1 56.4   ? 46  LEU   A C   1 
ATOM   385  O  O   . LEU   A 1 61  ? -8.376  -27.886 -38.068 1 56.53  ? 46  LEU   A O   1 
ATOM   386  C  CB  . LEU   A 1 61  ? -7.057  -27.534 -35.098 1 56.42  ? 46  LEU   A CB  1 
ATOM   387  C  CG  . LEU   A 1 61  ? -6.966  -26.591 -33.906 1 57.43  ? 46  LEU   A CG  1 
ATOM   388  C  CD1 . LEU   A 1 61  ? -5.52   -26.4   -33.498 1 57.7   ? 46  LEU   A CD1 1 
ATOM   389  C  CD2 . LEU   A 1 61  ? -7.565  -25.252 -34.226 1 57.82  ? 46  LEU   A CD2 1 
ATOM   390  N  N   . PRO   A 1 62  ? -8.117  -29.902 -37.081 1 55.61  ? 47  PRO   A N   1 
ATOM   391  C  CA  . PRO   A 1 62  ? -7.998  -30.564 -38.385 1 55.5   ? 47  PRO   A CA  1 
ATOM   392  C  C   . PRO   A 1 62  ? -9.204  -30.345 -39.298 1 55.39  ? 47  PRO   A C   1 
ATOM   393  O  O   . PRO   A 1 62  ? -9.032  -30.036 -40.471 1 55.46  ? 47  PRO   A O   1 
ATOM   394  C  CB  . PRO   A 1 62  ? -7.834  -32.047 -38.017 1 56     ? 47  PRO   A CB  1 
ATOM   395  C  CG  . PRO   A 1 62  ? -7.381  -32.06  -36.623 1 56.05  ? 47  PRO   A CG  1 
ATOM   396  C  CD  . PRO   A 1 62  ? -7.998  -30.88  -35.981 1 54.73  ? 47  PRO   A CD  1 
ATOM   397  N  N   . ASP   A 1 63  ? -10.413 -30.478 -38.757 1 55.17  ? 48  ASP   A N   1 
ATOM   398  C  CA  . ASP   A 1 63  ? -11.636 -30.317 -39.536 1 55.33  ? 48  ASP   A CA  1 
ATOM   399  C  C   . ASP   A 1 63  ? -11.967 -28.859 -39.818 1 55.23  ? 48  ASP   A C   1 
ATOM   400  O  O   . ASP   A 1 63  ? -12.33  -28.545 -40.947 1 55.3   ? 48  ASP   A O   1 
ATOM   401  C  CB  . ASP   A 1 63  ? -12.794 -31.064 -38.882 1 56.64  ? 48  ASP   A CB  1 
ATOM   402  C  CG  . ASP   A 1 63  ? -12.467 -32.535 -38.806 1 62.41  ? 48  ASP   A CG  1 
ATOM   403  O  OD1 . ASP   A 1 63  ? -12.022 -33.098 -39.84  1 64.28  ? 48  ASP   A OD1 1 
ATOM   404  O  OD2 . ASP   A 1 63  ? -12.6   -33.116 -37.708 1 64.33  ? 48  ASP   A OD2 1 
ATOM   405  N  N   . LEU   A 1 64  ? -11.795 -27.966 -38.838 1 55.11  ? 49  LEU   A N   1 
ATOM   406  C  CA  . LEU   A 1 64  ? -12.064 -26.549 -39.052 1 55.86  ? 49  LEU   A CA  1 
ATOM   407  C  C   . LEU   A 1 64  ? -11.077 -25.877 -39.992 1 57.36  ? 49  LEU   A C   1 
ATOM   408  O  O   . LEU   A 1 64  ? -11.472 -24.951 -40.687 1 58     ? 49  LEU   A O   1 
ATOM   409  C  CB  . LEU   A 1 64  ? -12.165 -25.784 -37.741 1 55.72  ? 49  LEU   A CB  1 
ATOM   410  C  CG  . LEU   A 1 64  ? -13.352 -26.148 -36.891 1 56.93  ? 49  LEU   A CG  1 
ATOM   411  C  CD1 . LEU   A 1 64  ? -13.209 -25.567 -35.501 1 56.94  ? 49  LEU   A CD1 1 
ATOM   412  C  CD2 . LEU   A 1 64  ? -14.646 -25.73  -37.575 1 57.98  ? 49  LEU   A CD2 1 
ATOM   413  N  N   . ILE   A 1 65  ? -9.802  -26.314 -40.018 1 57.91  ? 50  ILE   A N   1 
ATOM   414  C  CA  . ILE   A 1 65  ? -8.818  -25.713 -40.915 1 58.68  ? 50  ILE   A CA  1 
ATOM   415  C  C   . ILE   A 1 65  ? -9.15   -26.177 -42.334 1 60.61  ? 50  ILE   A C   1 
ATOM   416  O  O   . ILE   A 1 65  ? -9.297  -25.347 -43.234 1 60.99  ? 50  ILE   A O   1 
ATOM   417  C  CB  . ILE   A 1 65  ? -7.344  -26.055 -40.523 1 58.21  ? 50  ILE   A CB  1 
ATOM   418  C  CG1 . ILE   A 1 65  ? -6.905  -25.368 -39.23  1 58.73  ? 50  ILE   A CG1 1 
ATOM   419  C  CG2 . ILE   A 1 65  ? -6.368  -25.73  -41.653 1 58.11  ? 50  ILE   A CG2 1 
ATOM   420  C  CD1 . ILE   A 1 65  ? -5.572  -25.962 -38.63  1 59.46  ? 50  ILE   A CD1 1 
ATOM   421  N  N   . GLU   A 1 66  ? -9.312  -27.504 -42.509 1 61.62  ? 51  GLU   A N   1 
ATOM   422  C  CA  . GLU   A 1 66  ? -9.591  -28.163 -43.786 1 62.98  ? 51  GLU   A CA  1 
ATOM   423  C  C   . GLU   A 1 66  ? -10.875 -27.673 -44.447 1 64.09  ? 51  GLU   A C   1 
ATOM   424  O  O   . GLU   A 1 66  ? -10.912 -27.511 -45.665 1 64.43  ? 51  GLU   A O   1 
ATOM   425  C  CB  . GLU   A 1 66  ? -9.639  -29.684 -43.6   1 64.95  ? 51  GLU   A CB  1 
ATOM   426  C  CG  . GLU   A 1 66  ? -9.315  -30.451 -44.861 1 69.33  ? 51  GLU   A CG  1 
ATOM   427  C  CD  . GLU   A 1 66  ? -9.606  -31.932 -44.766 1 75.29  ? 51  GLU   A CD  1 
ATOM   428  O  OE1 . GLU   A 1 66  ? -9.554  -32.483 -43.639 1 77.66  ? 51  GLU   A OE1 1 
ATOM   429  O  OE2 . GLU   A 1 66  ? -9.892  -32.542 -45.823 1 75.97  ? 51  GLU   A OE2 1 
ATOM   430  N  N   . SER   A 1 67  ? -11.932 -27.444 -43.65  1 64.29  ? 52  SER   A N   1 
ATOM   431  C  CA  . SER   A 1 67  ? -13.205 -26.945 -44.172 1 64.53  ? 52  SER   A CA  1 
ATOM   432  C  C   . SER   A 1 67  ? -13.17  -25.445 -44.517 1 65.73  ? 52  SER   A C   1 
ATOM   433  O  O   . SER   A 1 67  ? -14.001 -24.979 -45.288 1 66.12  ? 52  SER   A O   1 
ATOM   434  C  CB  . SER   A 1 67  ? -14.319 -27.193 -43.166 1 64.65  ? 52  SER   A CB  1 
ATOM   435  N  N   . GLY   A 1 68  ? -12.235 -24.698 -43.943 1 66     ? 53  GLY   A N   1 
ATOM   436  C  CA  . GLY   A 1 68  ? -12.178 -23.252 -44.134 1 66.55  ? 53  GLY   A CA  1 
ATOM   437  C  C   . GLY   A 1 68  ? -13.017 -22.478 -43.12  1 67.21  ? 53  GLY   A C   1 
ATOM   438  O  O   . GLY   A 1 68  ? -13.044 -21.242 -43.135 1 67.97  ? 53  GLY   A O   1 
ATOM   439  N  N   . GLN   A 1 69  ? -13.671 -23.189 -42.194 1 66.68  ? 54  GLN   A N   1 
ATOM   440  C  CA  . GLN   A 1 69  ? -14.499 -22.576 -41.177 1 66.8   ? 54  GLN   A CA  1 
ATOM   441  C  C   . GLN   A 1 69  ? -13.717 -22.062 -39.968 1 66.02  ? 54  GLN   A C   1 
ATOM   442  O  O   . GLN   A 1 69  ? -14.315 -21.404 -39.13  1 66.2   ? 54  GLN   A O   1 
ATOM   443  C  CB  . GLN   A 1 69  ? -15.544 -23.605 -40.696 1 69.49  ? 54  GLN   A CB  1 
ATOM   444  C  CG  . GLN   A 1 69  ? -16.407 -24.179 -41.805 1 74.43  ? 54  GLN   A CG  1 
ATOM   445  C  CD  . GLN   A 1 69  ? -17.346 -23.129 -42.341 1 80.54  ? 54  GLN   A CD  1 
ATOM   446  O  OE1 . GLN   A 1 69  ? -17.051 -22.446 -43.335 1 82.81  ? 54  GLN   A OE1 1 
ATOM   447  N  NE2 . GLN   A 1 69  ? -18.493 -22.962 -41.687 1 81.1   ? 54  GLN   A NE2 1 
ATOM   448  N  N   . LEU   A 1 70  ? -12.41  -22.376 -39.839 1 65.11  ? 55  LEU   A N   1 
ATOM   449  C  CA  . LEU   A 1 70  ? -11.647 -22.015 -38.645 1 64.35  ? 55  LEU   A CA  1 
ATOM   450  C  C   . LEU   A 1 70  ? -11.538 -20.519 -38.375 1 64.01  ? 55  LEU   A C   1 
ATOM   451  O  O   . LEU   A 1 70  ? -11.859 -20.095 -37.259 1 63.97  ? 55  LEU   A O   1 
ATOM   452  C  CB  . LEU   A 1 70  ? -10.25  -22.654 -38.624 1 64.08  ? 55  LEU   A CB  1 
ATOM   453  C  CG  . LEU   A 1 70  ? -9.361  -22.229 -37.431 1 64.58  ? 55  LEU   A CG  1 
ATOM   454  C  CD1 . LEU   A 1 70  ? -9.531  -23.13  -36.258 1 64.72  ? 55  LEU   A CD1 1 
ATOM   455  C  CD2 . LEU   A 1 70  ? -7.974  -22.057 -37.838 1 65.05  ? 55  LEU   A CD2 1 
ATOM   456  N  N   . ARG   A 1 71  ? -11.035 -19.728 -39.336 1 63.61  ? 56  ARG   A N   1 
ATOM   457  C  CA  . ARG   A 1 71  ? -10.859 -18.294 -39.105 1 63.86  ? 56  ARG   A CA  1 
ATOM   458  C  C   . ARG   A 1 71  ? -12.167 -17.603 -38.752 1 65.42  ? 56  ARG   A C   1 
ATOM   459  O  O   . ARG   A 1 71  ? -12.186 -16.765 -37.856 1 65.61  ? 56  ARG   A O   1 
ATOM   460  C  CB  . ARG   A 1 71  ? -10.143 -17.634 -40.277 1 63.6   ? 56  ARG   A CB  1 
ATOM   461  C  CG  . ARG   A 1 71  ? -8.665  -17.972 -40.274 1 63.88  ? 56  ARG   A CG  1 
ATOM   462  C  CD  . ARG   A 1 71  ? -8.01   -17.632 -41.575 1 65.23  ? 56  ARG   A CD  1 
ATOM   463  N  NE  . ARG   A 1 71  ? -6.559  -17.774 -41.507 1 65.76  ? 56  ARG   A NE  1 
ATOM   464  C  CZ  . ARG   A 1 71  ? -5.756  -17.739 -42.563 1 67.51  ? 56  ARG   A CZ  1 
ATOM   465  N  NH1 . ARG   A 1 71  ? -6.255  -17.572 -43.782 1 67.34  ? 56  ARG   A NH1 1 
ATOM   466  N  NH2 . ARG   A 1 71  ? -4.444  -17.858 -42.409 1 67.04  ? 56  ARG   A NH2 1 
ATOM   467  N  N   . GLU   A 1 72  ? -13.276 -18.058 -39.37  1 66.21  ? 57  GLU   A N   1 
ATOM   468  C  CA  . GLU   A 1 72  ? -14.617 -17.573 -39.097 1 67.3   ? 57  GLU   A CA  1 
ATOM   469  C  C   . GLU   A 1 72  ? -15.019 -17.896 -37.652 1 68.18  ? 57  GLU   A C   1 
ATOM   470  O  O   . GLU   A 1 72  ? -15.442 -16.988 -36.947 1 68.7   ? 57  GLU   A O   1 
ATOM   471  C  CB  . GLU   A 1 72  ? -15.627 -18.178 -40.091 1 70.23  ? 57  GLU   A CB  1 
ATOM   472  C  CG  . GLU   A 1 72  ? -17.061 -17.765 -39.815 1 77.42  ? 57  GLU   A CG  1 
ATOM   473  C  CD  . GLU   A 1 72  ? -18.116 -18.792 -40.17  1 87.82  ? 57  GLU   A CD  1 
ATOM   474  O  OE1 . GLU   A 1 72  ? -19.25  -18.682 -39.648 1 90.43  ? 57  GLU   A OE1 1 
ATOM   475  O  OE2 . GLU   A 1 72  ? -17.808 -19.707 -40.968 1 91.16  ? 57  GLU   A OE2 1 
ATOM   476  N  N   . ARG   A 1 73  ? -14.863 -19.16  -37.198 1 68.37  ? 58  ARG   A N   1 
ATOM   477  C  CA  . ARG   A 1 73  ? -15.207 -19.563 -35.827 1 69.42  ? 58  ARG   A CA  1 
ATOM   478  C  C   . ARG   A 1 73  ? -14.435 -18.782 -34.769 1 70.06  ? 58  ARG   A C   1 
ATOM   479  O  O   . ARG   A 1 73  ? -14.974 -18.537 -33.686 1 70.23  ? 58  ARG   A O   1 
ATOM   480  C  CB  . ARG   A 1 73  ? -14.994 -21.066 -35.608 1 71.34  ? 58  ARG   A CB  1 
ATOM   481  C  CG  . ARG   A 1 73  ? -15.845 -21.957 -36.499 1 75.8   ? 58  ARG   A CG  1 
ATOM   482  C  CD  . ARG   A 1 73  ? -17.22  -22.237 -35.944 1 79.83  ? 58  ARG   A CD  1 
ATOM   483  N  NE  . ARG   A 1 73  ? -18.115 -21.103 -36.16  1 84.14  ? 58  ARG   A NE  1 
ATOM   484  C  CZ  . ARG   A 1 73  ? -19.368 -21.042 -35.722 1 87.56  ? 58  ARG   A CZ  1 
ATOM   485  N  NH1 . ARG   A 1 73  ? -19.893 -22.057 -35.041 1 87.27  ? 58  ARG   A NH1 1 
ATOM   486  N  NH2 . ARG   A 1 73  ? -20.106 -19.965 -35.958 1 87.99  ? 58  ARG   A NH2 1 
ATOM   487  N  N   . VAL   A 1 74  ? -13.178 -18.401 -35.077 1 70.09  ? 59  VAL   A N   1 
ATOM   488  C  CA  . VAL   A 1 74  ? -12.358 -17.61  -34.169 1 71.01  ? 59  VAL   A CA  1 
ATOM   489  C  C   . VAL   A 1 74  ? -12.942 -16.199 -34.12  1 71.91  ? 59  VAL   A C   1 
ATOM   490  O  O   . VAL   A 1 74  ? -13.209 -15.686 -33.036 1 72.16  ? 59  VAL   A O   1 
ATOM   491  C  CB  . VAL   A 1 74  ? -10.857 -17.595 -34.582 1 71.56  ? 59  VAL   A CB  1 
ATOM   492  C  CG1 . VAL   A 1 74  ? -10.07  -16.557 -33.783 1 71.84  ? 59  VAL   A CG1 1 
ATOM   493  C  CG2 . VAL   A 1 74  ? -10.233 -18.974 -34.428 1 71.77  ? 59  VAL   A CG2 1 
ATOM   494  N  N   . GLU   A 1 75  ? -13.201 -15.603 -35.299 1 72.21  ? 60  GLU   A N   1 
ATOM   495  C  CA  . GLU   A 1 75  ? -13.778 -14.266 -35.436 1 72.88  ? 60  GLU   A CA  1 
ATOM   496  C  C   . GLU   A 1 75  ? -15.182 -14.142 -34.809 1 74     ? 60  GLU   A C   1 
ATOM   497  O  O   . GLU   A 1 75  ? -15.564 -13.06  -34.37  1 74.25  ? 60  GLU   A O   1 
ATOM   498  C  CB  . GLU   A 1 75  ? -13.782 -13.834 -36.905 1 73.82  ? 60  GLU   A CB  1 
ATOM   499  C  CG  . GLU   A 1 75  ? -12.404 -13.436 -37.407 1 77.13  ? 60  GLU   A CG  1 
ATOM   500  C  CD  . GLU   A 1 75  ? -12.142 -13.694 -38.881 1 82.33  ? 60  GLU   A CD  1 
ATOM   501  O  OE1 . GLU   A 1 75  ? -13.05  -14.223 -39.563 1 84.51  ? 60  GLU   A OE1 1 
ATOM   502  O  OE2 . GLU   A 1 75  ? -11.023 -13.385 -39.353 1 82.7   ? 60  GLU   A OE2 1 
ATOM   503  N  N   . LYS   A 1 76  ? -15.916 -15.254 -34.719 1 74.45  ? 61  LYS   A N   1 
ATOM   504  C  CA  . LYS   A 1 76  ? -17.256 -15.299 -34.13  1 75.51  ? 61  LYS   A CA  1 
ATOM   505  C  C   . LYS   A 1 76  ? -17.262 -15.456 -32.584 1 76.28  ? 61  LYS   A C   1 
ATOM   506  O  O   . LYS   A 1 76  ? -18.331 -15.461 -31.964 1 76.32  ? 61  LYS   A O   1 
ATOM   507  C  CB  . LYS   A 1 76  ? -18.074 -16.433 -34.784 1 77.25  ? 61  LYS   A CB  1 
ATOM   508  N  N   . LEU   A 1 77  ? -16.083 -15.609 -31.966 1 76.65  ? 62  LEU   A N   1 
ATOM   509  C  CA  . LEU   A 1 77  ? -15.989 -15.795 -30.521 1 77.11  ? 62  LEU   A CA  1 
ATOM   510  C  C   . LEU   A 1 77  ? -16.262 -14.512 -29.758 1 77.08  ? 62  LEU   A C   1 
ATOM   511  O  O   . LEU   A 1 77  ? -15.959 -13.415 -30.233 1 77.23  ? 62  LEU   A O   1 
ATOM   512  C  CB  . LEU   A 1 77  ? -14.579 -16.282 -30.125 1 77.5   ? 62  LEU   A CB  1 
ATOM   513  C  CG  . LEU   A 1 77  ? -14.198 -17.717 -30.43  1 78.88  ? 62  LEU   A CG  1 
ATOM   514  C  CD1 . LEU   A 1 77  ? -12.731 -17.953 -30.1   1 79.45  ? 62  LEU   A CD1 1 
ATOM   515  C  CD2 . LEU   A 1 77  ? -15.048 -18.681 -29.653 1 79.34  ? 62  LEU   A CD2 1 
ATOM   516  N  N   . ASN   A 1 78  ? -16.765 -14.659 -28.54  1 76.8   ? 63  ASN   A N   1 
ATOM   517  C  CA  . ASN   A 1 78  ? -16.953 -13.523 -27.648 1 77.18  ? 63  ASN   A CA  1 
ATOM   518  C  C   . ASN   A 1 78  ? -15.741 -13.5   -26.706 1 77.49  ? 63  ASN   A C   1 
ATOM   519  O  O   . ASN   A 1 78  ? -15.311 -14.563 -26.249 1 77.73  ? 63  ASN   A O   1 
ATOM   520  C  CB  . ASN   A 1 78  ? -18.261 -13.659 -26.854 1 77.66  ? 63  ASN   A CB  1 
ATOM   521  C  CG  . ASN   A 1 78  ? -19.495 -13.397 -27.68  1 79.13  ? 63  ASN   A CG  1 
ATOM   522  O  OD1 . ASN   A 1 78  ? -19.505 -12.544 -28.577 1 79.87  ? 63  ASN   A OD1 1 
ATOM   523  N  ND2 . ASN   A 1 78  ? -20.559 -14.123 -27.388 1 78.94  ? 63  ASN   A ND2 1 
ATOM   524  N  N   . MET   A 1 79  ? -15.171 -12.314 -26.442 1 77.28  ? 64  MET   A N   1 
ATOM   525  C  CA  . MET   A 1 79  ? -14.003 -12.224 -25.572 1 77.69  ? 64  MET   A CA  1 
ATOM   526  C  C   . MET   A 1 79  ? -14.314 -12.674 -24.154 1 78.14  ? 64  MET   A C   1 
ATOM   527  O  O   . MET   A 1 79  ? -15.082 -12.016 -23.457 1 78.48  ? 64  MET   A O   1 
ATOM   528  C  CB  . MET   A 1 79  ? -13.423 -10.816 -25.564 1 78.29  ? 64  MET   A CB  1 
ATOM   529  C  CG  . MET   A 1 79  ? -12.12  -10.734 -24.813 1 80.21  ? 64  MET   A CG  1 
ATOM   530  S  SD  . MET   A 1 79  ? -11.701 -9.041  -24.399 1 84.43  ? 64  MET   A SD  1 
ATOM   531  C  CE  . MET   A 1 79  ? -11.478 -8.358  -26.024 1 81.84  ? 64  MET   A CE  1 
ATOM   532  N  N   . LEU   A 1 80  ? -13.727 -13.806 -23.731 1 78.03  ? 65  LEU   A N   1 
ATOM   533  C  CA  . LEU   A 1 80  ? -13.943 -14.352 -22.392 1 78.24  ? 65  LEU   A CA  1 
ATOM   534  C  C   . LEU   A 1 80  ? -12.873 -13.877 -21.409 1 78.76  ? 65  LEU   A C   1 
ATOM   535  O  O   . LEU   A 1 80  ? -11.743 -13.585 -21.807 1 79.17  ? 65  LEU   A O   1 
ATOM   536  C  CB  . LEU   A 1 80  ? -13.96  -15.882 -22.435 1 78.24  ? 65  LEU   A CB  1 
ATOM   537  C  CG  . LEU   A 1 80  ? -15.024 -16.499 -23.32  1 79.54  ? 65  LEU   A CG  1 
ATOM   538  C  CD1 . LEU   A 1 80  ? -14.739 -17.96  -23.574 1 79.85  ? 65  LEU   A CD1 1 
ATOM   539  C  CD2 . LEU   A 1 80  ? -16.402 -16.307 -22.725 1 80.12  ? 65  LEU   A CD2 1 
ATOM   540  N  N   . SER   A 1 81  ? -13.225 -13.804 -20.123 1 78.57  ? 66  SER   A N   1 
ATOM   541  C  CA  . SER   A 1 81  ? -12.278 -13.378 -19.1   1 78.8   ? 66  SER   A CA  1 
ATOM   542  C  C   . SER   A 1 81  ? -11.44  -14.562 -18.648 1 78.96  ? 66  SER   A C   1 
ATOM   543  O  O   . SER   A 1 81  ? -11.963 -15.67  -18.524 1 78.73  ? 66  SER   A O   1 
ATOM   544  C  CB  . SER   A 1 81  ? -13.02  -12.802 -17.896 1 79.7   ? 66  SER   A CB  1 
ATOM   545  N  N   . ILE   A 1 82  ? -10.155 -14.33  -18.354 1 79.03  ? 67  ILE   A N   1 
ATOM   546  C  CA  . ILE   A 1 82  ? -9.311  -15.407 -17.831 1 79.67  ? 67  ILE   A CA  1 
ATOM   547  C  C   . ILE   A 1 82  ? -9.587  -15.692 -16.339 1 80.7   ? 67  ILE   A C   1 
ATOM   548  O  O   . ILE   A 1 82  ? -9.001  -16.625 -15.792 1 81.24  ? 67  ILE   A O   1 
ATOM   549  C  CB  . ILE   A 1 82  ? -7.818  -15.168 -18.115 1 80.03  ? 67  ILE   A CB  1 
ATOM   550  C  CG1 . ILE   A 1 82  ? -7.265  -14.035 -17.254 1 81.08  ? 67  ILE   A CG1 1 
ATOM   551  C  CG2 . ILE   A 1 82  ? -7.603  -14.892 -19.585 1 80.4   ? 67  ILE   A CG2 1 
ATOM   552  C  CD1 . ILE   A 1 82  ? -5.773  -13.932 -17.289 1 82.4   ? 67  ILE   A CD1 1 
ATOM   553  N  N   . ASP   A 1 83  ? -10.506 -14.924 -15.699 1 80.75  ? 68  ASP   A N   1 
ATOM   554  C  CA  . ASP   A 1 83  ? -10.877 -15.026 -14.292 1 81.45  ? 68  ASP   A CA  1 
ATOM   555  C  C   . ASP   A 1 83  ? -11.443 -16.395 -13.877 1 80.72  ? 68  ASP   A C   1 
ATOM   556  O  O   . ASP   A 1 83  ? -11.403 -16.716 -12.69  1 81.05  ? 68  ASP   A O   1 
ATOM   557  C  CB  . ASP   A 1 83  ? -11.843 -13.892 -13.909 1 84.84  ? 68  ASP   A CB  1 
ATOM   558  C  CG  . ASP   A 1 83  ? -11.317 -12.503 -14.259 1 92.42  ? 68  ASP   A CG  1 
ATOM   559  O  OD1 . ASP   A 1 83  ? -10.078 -12.35  -14.393 1 93.65  ? 68  ASP   A OD1 1 
ATOM   560  O  OD2 . ASP   A 1 83  ? -12.145 -11.567 -14.401 1 95.73  ? 68  ASP   A OD2 1 
ATOM   561  N  N   . HIS   A 1 84  ? -11.929 -17.213 -14.827 1 79.56  ? 69  HIS   A N   1 
ATOM   562  C  CA  . HIS   A 1 84  ? -12.452 -18.538 -14.482 1 78.97  ? 69  HIS   A CA  1 
ATOM   563  C  C   . HIS   A 1 84  ? -11.411 -19.665 -14.559 1 77.63  ? 69  HIS   A C   1 
ATOM   564  O  O   . HIS   A 1 84  ? -11.77  -20.838 -14.48  1 77.73  ? 69  HIS   A O   1 
ATOM   565  C  CB  . HIS   A 1 84  ? -13.693 -18.87  -15.301 1 80.49  ? 69  HIS   A CB  1 
ATOM   566  C  CG  . HIS   A 1 84  ? -14.853 -18     -14.943 1 84     ? 69  HIS   A CG  1 
ATOM   567  N  ND1 . HIS   A 1 84  ? -14.858 -16.645 -15.24  1 86.22  ? 69  HIS   A ND1 1 
ATOM   568  C  CD2 . HIS   A 1 84  ? -15.992 -18.309 -14.282 1 85.29  ? 69  HIS   A CD2 1 
ATOM   569  C  CE1 . HIS   A 1 84  ? -16.006 -16.182 -14.775 1 86.8   ? 69  HIS   A CE1 1 
ATOM   570  N  NE2 . HIS   A 1 84  ? -16.722 -17.146 -14.188 1 86.61  ? 69  HIS   A NE2 1 
ATOM   571  N  N   . LEU   A 1 85  ? -10.123 -19.311 -14.677 1 76.21  ? 70  LEU   A N   1 
ATOM   572  C  CA  . LEU   A 1 85  ? -9.021  -20.264 -14.678 1 75.15  ? 70  LEU   A CA  1 
ATOM   573  C  C   . LEU   A 1 85  ? -8.356  -20.082 -13.317 1 74.57  ? 70  LEU   A C   1 
ATOM   574  O  O   . LEU   A 1 85  ? -7.5    -19.215 -13.17  1 74.62  ? 70  LEU   A O   1 
ATOM   575  C  CB  . LEU   A 1 85  ? -8.039  -19.925 -15.802 1 74.69  ? 70  LEU   A CB  1 
ATOM   576  C  CG  . LEU   A 1 85  ? -8.638  -19.91  -17.205 1 75.37  ? 70  LEU   A CG  1 
ATOM   577  C  CD1 . LEU   A 1 85  ? -7.749  -19.142 -18.162 1 75.8   ? 70  LEU   A CD1 1 
ATOM   578  C  CD2 . LEU   A 1 85  ? -8.916  -21.31  -17.694 1 75.56  ? 70  LEU   A CD2 1 
ATOM   579  N  N   . THR   A 1 86  ? -8.808  -20.844 -12.308 1 73.84  ? 71  THR   A N   1 
ATOM   580  C  CA  . THR   A 1 86  ? -8.346  -20.721 -10.922 1 73.72  ? 71  THR   A CA  1 
ATOM   581  C  C   . THR   A 1 86  ? -6.989  -21.388 -10.64  1 73.34  ? 71  THR   A C   1 
ATOM   582  O  O   . THR   A 1 86  ? -6.081  -20.729 -10.117 1 74.09  ? 71  THR   A O   1 
ATOM   583  C  CB  . THR   A 1 86  ? -9.431  -21.247 -9.968  1 75.11  ? 71  THR   A CB  1 
ATOM   584  O  OG1 . THR   A 1 86  ? -9.519  -22.674 -10.108 1 76.15  ? 71  THR   A OG1 1 
ATOM   585  C  CG2 . THR   A 1 86  ? -10.792 -20.607 -10.223 1 75.41  ? 71  THR   A CG2 1 
ATOM   586  N  N   . ASP   A 1 87  ? -6.849  -22.693 -10.953 1 71.67  ? 72  ASP   A N   1 
ATOM   587  C  CA  . ASP   A 1 87  ? -5.604  -23.406 -10.686 1 70.16  ? 72  ASP   A CA  1 
ATOM   588  C  C   . ASP   A 1 87  ? -4.578  -23.249 -11.806 1 67.71  ? 72  ASP   A C   1 
ATOM   589  O  O   . ASP   A 1 87  ? -4.926  -22.839 -12.912 1 68.15  ? 72  ASP   A O   1 
ATOM   590  C  CB  . ASP   A 1 87  ? -5.871  -24.885 -10.349 1 72.22  ? 72  ASP   A CB  1 
ATOM   591  C  CG  . ASP   A 1 87  ? -6.79   -25.596 -11.318 1 78.29  ? 72  ASP   A CG  1 
ATOM   592  O  OD1 . ASP   A 1 87  ? -6.398  -25.774 -12.487 1 78.85  ? 72  ASP   A OD1 1 
ATOM   593  O  OD2 . ASP   A 1 87  ? -7.889  -26     -10.899 1 81.94  ? 72  ASP   A OD2 1 
ATOM   594  N  N   . HIS   A 1 88  ? -3.311  -23.568 -11.514 1 65.03  ? 73  HIS   A N   1 
ATOM   595  C  CA  . HIS   A 1 88  ? -2.216  -23.469 -12.471 1 62.86  ? 73  HIS   A CA  1 
ATOM   596  C  C   . HIS   A 1 88  ? -2.407  -24.429 -13.659 1 60.93  ? 73  HIS   A C   1 
ATOM   597  O  O   . HIS   A 1 88  ? -2.115  -24.053 -14.789 1 61.07  ? 73  HIS   A O   1 
ATOM   598  C  CB  . HIS   A 1 88  ? -0.875  -23.707 -11.742 1 62.56  ? 73  HIS   A CB  1 
ATOM   599  C  CG  . HIS   A 1 88  ? 0.313   -23.881 -12.637 1 63.16  ? 73  HIS   A CG  1 
ATOM   600  N  ND1 . HIS   A 1 88  ? 0.881   -22.808 -13.311 1 64.48  ? 73  HIS   A ND1 1 
ATOM   601  C  CD2 . HIS   A 1 88  ? 1.032   -24.995 -12.909 1 63.8   ? 73  HIS   A CD2 1 
ATOM   602  C  CE1 . HIS   A 1 88  ? 1.917   -23.305 -13.969 1 64.7   ? 73  HIS   A CE1 1 
ATOM   603  N  NE2 . HIS   A 1 88  ? 2.046   -24.615 -13.761 1 64.61  ? 73  HIS   A NE2 1 
ATOM   604  N  N   . LYS   A 1 89  ? -2.926  -25.635 -13.417 1 59.09  ? 74  LYS   A N   1 
ATOM   605  C  CA  . LYS   A 1 89  ? -3.148  -26.607 -14.488 1 58.29  ? 74  LYS   A CA  1 
ATOM   606  C  C   . LYS   A 1 89  ? -4.194  -26.162 -15.507 1 58.26  ? 74  LYS   A C   1 
ATOM   607  O  O   . LYS   A 1 89  ? -4.061  -26.471 -16.688 1 57.99  ? 74  LYS   A O   1 
ATOM   608  C  CB  . LYS   A 1 89  ? -3.475  -27.996 -13.929 1 58.44  ? 74  LYS   A CB  1 
ATOM   609  C  CG  . LYS   A 1 89  ? -2.295  -28.629 -13.218 1 59.97  ? 74  LYS   A CG  1 
ATOM   610  C  CD  . LYS   A 1 89  ? -2.455  -30.128 -13.119 1 63.76  ? 74  LYS   A CD  1 
ATOM   611  C  CE  . LYS   A 1 89  ? -1.347  -30.761 -12.321 1 66.59  ? 74  LYS   A CE  1 
ATOM   612  N  NZ  . LYS   A 1 89  ? -1.562  -32.22  -12.157 1 68.74  ? 74  LYS   A NZ  1 
ATOM   613  N  N   . SER   A 1 90  ? -5.218  -25.422 -15.065 1 58.39  ? 75  SER   A N   1 
ATOM   614  C  CA  . SER   A 1 90  ? -6.24   -24.884 -15.979 1 58.59  ? 75  SER   A CA  1 
ATOM   615  C  C   . SER   A 1 90  ? -5.654  -23.719 -16.798 1 57.7   ? 75  SER   A C   1 
ATOM   616  O  O   . SER   A 1 90  ? -5.952  -23.587 -17.981 1 57.64  ? 75  SER   A O   1 
ATOM   617  C  CB  . SER   A 1 90  ? -7.487  -24.432 -15.219 1 60.19  ? 75  SER   A CB  1 
ATOM   618  O  OG  . SER   A 1 90  ? -7.161  -23.522 -14.182 1 62.81  ? 75  SER   A OG  1 
ATOM   619  N  N   . GLN   A 1 91  ? -4.797  -22.903 -16.173 1 56.74  ? 76  GLN   A N   1 
ATOM   620  C  CA  . GLN   A 1 91  ? -4.11   -21.813 -16.845 1 56.39  ? 76  GLN   A CA  1 
ATOM   621  C  C   . GLN   A 1 91  ? -3.147  -22.348 -17.923 1 55.67  ? 76  GLN   A C   1 
ATOM   622  O  O   . GLN   A 1 91  ? -3.003  -21.739 -18.985 1 56.04  ? 76  GLN   A O   1 
ATOM   623  C  CB  . GLN   A 1 91  ? -3.332  -21.004 -15.816 1 58.02  ? 76  GLN   A CB  1 
ATOM   624  C  CG  . GLN   A 1 91  ? -4.236  -20.167 -14.931 1 61.48  ? 76  GLN   A CG  1 
ATOM   625  C  CD  . GLN   A 1 91  ? -3.563  -19.789 -13.648 1 66.4   ? 76  GLN   A CD  1 
ATOM   626  O  OE1 . GLN   A 1 91  ? -2.333  -19.627 -13.575 1 68.62  ? 76  GLN   A OE1 1 
ATOM   627  N  NE2 . GLN   A 1 91  ? -4.355  -19.664 -12.598 1 66.88  ? 76  GLN   A NE2 1 
ATOM   628  N  N   . ARG   A 1 92  ? -2.497  -23.489 -17.645 1 54.23  ? 77  ARG   A N   1 
ATOM   629  C  CA  . ARG   A 1 92  ? -1.569  -24.128 -18.577 1 53.3   ? 77  ARG   A CA  1 
ATOM   630  C  C   . ARG   A 1 92  ? -2.318  -24.762 -19.748 1 52.72  ? 77  ARG   A C   1 
ATOM   631  O  O   . ARG   A 1 92  ? -1.834  -24.713 -20.88  1 52.3   ? 77  ARG   A O   1 
ATOM   632  C  CB  . ARG   A 1 92  ? -0.679  -25.164 -17.859 1 53.26  ? 77  ARG   A CB  1 
ATOM   633  C  CG  . ARG   A 1 92  ? 0.414   -24.524 -17.007 1 53.45  ? 77  ARG   A CG  1 
ATOM   634  C  CD  . ARG   A 1 92  ? 1.531   -23.898 -17.837 1 53.5   ? 77  ARG   A CD  1 
ATOM   635  N  NE  . ARG   A 1 92  ? 2.22    -24.891 -18.668 1 53.32  ? 77  ARG   A NE  1 
ATOM   636  C  CZ  . ARG   A 1 92  ? 3.238   -25.642 -18.258 1 51.89  ? 77  ARG   A CZ  1 
ATOM   637  N  NH1 . ARG   A 1 92  ? 3.707   -25.519 -17.024 1 50.74  ? 77  ARG   A NH1 1 
ATOM   638  N  NH2 . ARG   A 1 92  ? 3.796   -26.52  -19.081 1 49.7   ? 77  ARG   A NH2 1 
ATOM   639  N  N   . LEU   A 1 93  ? -3.502  -25.34  -19.476 1 52.48  ? 78  LEU   A N   1 
ATOM   640  C  CA  . LEU   A 1 93  ? -4.352  -25.932 -20.503 1 52.54  ? 78  LEU   A CA  1 
ATOM   641  C  C   . LEU   A 1 93  ? -4.885  -24.821 -21.404 1 52.46  ? 78  LEU   A C   1 
ATOM   642  O  O   . LEU   A 1 93  ? -4.82   -24.951 -22.626 1 52.89  ? 78  LEU   A O   1 
ATOM   643  C  CB  . LEU   A 1 93  ? -5.524  -26.729 -19.894 1 52.4   ? 78  LEU   A CB  1 
ATOM   644  C  CG  . LEU   A 1 93  ? -6.538  -27.312 -20.906 1 52.92  ? 78  LEU   A CG  1 
ATOM   645  C  CD1 . LEU   A 1 93  ? -5.871  -28.225 -21.928 1 52.53  ? 78  LEU   A CD1 1 
ATOM   646  C  CD2 . LEU   A 1 93  ? -7.648  -28.036 -20.207 1 53.15  ? 78  LEU   A CD2 1 
ATOM   647  N  N   . ALA   A 1 94  ? -5.336  -23.706 -20.81  1 51.49  ? 79  ALA   A N   1 
ATOM   648  C  CA  . ALA   A 1 94  ? -5.838  -22.573 -21.578 1 50.63  ? 79  ALA   A CA  1 
ATOM   649  C  C   . ALA   A 1 94  ? -4.739  -21.983 -22.477 1 50.52  ? 79  ALA   A C   1 
ATOM   650  O  O   . ALA   A 1 94  ? -5.046  -21.534 -23.574 1 51.4   ? 79  ALA   A O   1 
ATOM   651  C  CB  . ALA   A 1 94  ? -6.411  -21.517 -20.651 1 49.79  ? 79  ALA   A CB  1 
ATOM   652  N  N   . ARG   A 1 95  ? -3.47   -22.032 -22.045 1 49.32  ? 80  ARG   A N   1 
ATOM   653  C  CA  . ARG   A 1 95  ? -2.322  -21.564 -22.834 1 48.79  ? 80  ARG   A CA  1 
ATOM   654  C  C   . ARG   A 1 95  ? -2.102  -22.463 -24.065 1 49.06  ? 80  ARG   A C   1 
ATOM   655  O  O   . ARG   A 1 95  ? -1.749  -21.993 -25.148 1 49.51  ? 80  ARG   A O   1 
ATOM   656  C  CB  . ARG   A 1 95  ? -1.051  -21.59  -21.971 1 48.75  ? 80  ARG   A CB  1 
ATOM   657  C  CG  . ARG   A 1 95  ? -0.514  -20.23  -21.653 1 49.25  ? 80  ARG   A CG  1 
ATOM   658  C  CD  . ARG   A 1 95  ? 0.946   -20.291 -21.247 1 50.14  ? 80  ARG   A CD  1 
ATOM   659  N  NE  . ARG   A 1 95  ? 1.847   -20.502 -22.38  1 50.98  ? 80  ARG   A NE  1 
ATOM   660  C  CZ  . ARG   A 1 95  ? 2.273   -19.541 -23.196 1 51.68  ? 80  ARG   A CZ  1 
ATOM   661  N  NH1 . ARG   A 1 95  ? 1.843   -18.297 -23.048 1 51.93  ? 80  ARG   A NH1 1 
ATOM   662  N  NH2 . ARG   A 1 95  ? 3.1     -19.826 -24.19  1 50.45  ? 80  ARG   A NH2 1 
ATOM   663  N  N   . LEU   A 1 96  ? -2.28   -23.761 -23.876 1 48.71  ? 81  LEU   A N   1 
ATOM   664  C  CA  . LEU   A 1 96  ? -2.129  -24.747 -24.926 1 48.9   ? 81  LEU   A CA  1 
ATOM   665  C  C   . LEU   A 1 96  ? -3.306  -24.608 -25.905 1 48.72  ? 81  LEU   A C   1 
ATOM   666  O  O   . LEU   A 1 96  ? -3.079  -24.551 -27.111 1 48.45  ? 81  LEU   A O   1 
ATOM   667  C  CB  . LEU   A 1 96  ? -2.076  -26.14  -24.274 1 48.79  ? 81  LEU   A CB  1 
ATOM   668  C  CG  . LEU   A 1 96  ? -2.136  -27.343 -25.179 1 49.39  ? 81  LEU   A CG  1 
ATOM   669  C  CD1 . LEU   A 1 96  ? -1.023  -27.325 -26.223 1 49.63  ? 81  LEU   A CD1 1 
ATOM   670  C  CD2 . LEU   A 1 96  ? -2.131  -28.596 -24.355 1 49.3   ? 81  LEU   A CD2 1 
ATOM   671  N  N   . VAL   A 1 97  ? -4.537  -24.478 -25.379 1 48.49  ? 82  VAL   A N   1 
ATOM   672  C  CA  . VAL   A 1 97  ? -5.748  -24.288 -26.172 1 49.1   ? 82  VAL   A CA  1 
ATOM   673  C  C   . VAL   A 1 97  ? -5.645  -23.022 -27.027 1 48.84  ? 82  VAL   A C   1 
ATOM   674  O  O   . VAL   A 1 97  ? -5.71   -23.115 -28.252 1 48.5   ? 82  VAL   A O   1 
ATOM   675  C  CB  . VAL   A 1 97  ? -7.022  -24.318 -25.286 1 50.59  ? 82  VAL   A CB  1 
ATOM   676  C  CG1 . VAL   A 1 97  ? -8.244  -23.759 -26.018 1 51.6   ? 82  VAL   A CG1 1 
ATOM   677  C  CG2 . VAL   A 1 97  ? -7.299  -25.728 -24.797 1 51.03  ? 82  VAL   A CG2 1 
ATOM   678  N  N   . LEU   A 1 98  ? -5.413  -21.859 -26.396 1 48.65  ? 83  LEU   A N   1 
ATOM   679  C  CA  . LEU   A 1 98  ? -5.288  -20.587 -27.107 1 48.97  ? 83  LEU   A CA  1 
ATOM   680  C  C   . LEU   A 1 98  ? -4.101  -20.538 -28.04  1 49.58  ? 83  LEU   A C   1 
ATOM   681  O  O   . LEU   A 1 98  ? -4.181  -19.91  -29.098 1 49.48  ? 83  LEU   A O   1 
ATOM   682  C  CB  . LEU   A 1 98  ? -5.203  -19.429 -26.124 1 49.11  ? 83  LEU   A CB  1 
ATOM   683  C  CG  . LEU   A 1 98  ? -6.452  -19.167 -25.292 1 50.42  ? 83  LEU   A CG  1 
ATOM   684  C  CD1 . LEU   A 1 98  ? -6.191  -18.099 -24.271 1 50.82  ? 83  LEU   A CD1 1 
ATOM   685  C  CD2 . LEU   A 1 98  ? -7.636  -18.812 -26.171 1 50.82  ? 83  LEU   A CD2 1 
ATOM   686  N  N   . GLY   A 1 99  ? -3.008  -21.192 -27.644 1 49.86  ? 84  GLY   A N   1 
ATOM   687  C  CA  . GLY   A 1 99  ? -1.798  -21.238 -28.449 1 50.13  ? 84  GLY   A CA  1 
ATOM   688  C  C   . GLY   A 1 99  ? -2.001  -22.016 -29.727 1 50.32  ? 84  GLY   A C   1 
ATOM   689  O  O   . GLY   A 1 99  ? -1.552  -21.584 -30.786 1 50.99  ? 84  GLY   A O   1 
ATOM   690  N  N   . CYS   A 1 100 ? -2.685  -23.161 -29.636 1 49.86  ? 85  CYS   A N   1 
ATOM   691  C  CA  . CYS   A 1 100 ? -2.988  -24.016 -30.782 1 50.35  ? 85  CYS   A CA  1 
ATOM   692  C  C   . CYS   A 1 100 ? -3.949  -23.316 -31.729 1 51.99  ? 85  CYS   A C   1 
ATOM   693  O  O   . CYS   A 1 100 ? -3.841  -23.483 -32.946 1 52.81  ? 85  CYS   A O   1 
ATOM   694  C  CB  . CYS   A 1 100 ? -3.549  -25.359 -30.323 1 50.35  ? 85  CYS   A CB  1 
ATOM   695  S  SG  . CYS   A 1 100 ? -2.327  -26.453 -29.546 1 51.66  ? 85  CYS   A SG  1 
ATOM   696  N  N   . ILE   A 1 101 ? -4.905  -22.546 -31.179 1 52.01  ? 86  ILE   A N   1 
ATOM   697  C  CA  . ILE   A 1 101 ? -5.849  -21.809 -31.993 1 52.7   ? 86  ILE   A CA  1 
ATOM   698  C  C   . ILE   A 1 101 ? -5.125  -20.659 -32.701 1 53.35  ? 86  ILE   A C   1 
ATOM   699  O  O   . ILE   A 1 101 ? -5.375  -20.42  -33.878 1 53.87  ? 86  ILE   A O   1 
ATOM   700  C  CB  . ILE   A 1 101 ? -7.072  -21.343 -31.157 1 53.18  ? 86  ILE   A CB  1 
ATOM   701  C  CG1 . ILE   A 1 101 ? -7.861  -22.555 -30.629 1 54.13  ? 86  ILE   A CG1 1 
ATOM   702  C  CG2 . ILE   A 1 101 ? -7.984  -20.443 -31.977 1 53.43  ? 86  ILE   A CG2 1 
ATOM   703  C  CD1 . ILE   A 1 101 ? -8.855  -22.215 -29.55  1 55.27  ? 86  ILE   A CD1 1 
ATOM   704  N  N   . THR   A 1 102 ? -4.207  -19.98  -32.007 1 53.14  ? 87  THR   A N   1 
ATOM   705  C  CA  . THR   A 1 102 ? -3.459  -18.874 -32.586 1 54.03  ? 87  THR   A CA  1 
ATOM   706  C  C   . THR   A 1 102 ? -2.595  -19.343 -33.751 1 56.19  ? 87  THR   A C   1 
ATOM   707  O  O   . THR   A 1 102 ? -2.603  -18.704 -34.801 1 57.25  ? 87  THR   A O   1 
ATOM   708  C  CB  . THR   A 1 102 ? -2.643  -18.172 -31.506 1 54.42  ? 87  THR   A CB  1 
ATOM   709  O  OG1 . THR   A 1 102 ? -3.517  -17.721 -30.47  1 55.26  ? 87  THR   A OG1 1 
ATOM   710  C  CG2 . THR   A 1 102 ? -1.802  -17.039 -32.044 1 54.03  ? 87  THR   A CG2 1 
ATOM   711  N  N   . MET   A 1 103 ? -1.897  -20.482 -33.608 1 56.54  ? 88  MET   A N   1 
ATOM   712  C  CA  . MET   A 1 103 ? -1.066  -21     -34.692 1 57.25  ? 88  MET   A CA  1 
ATOM   713  C  C   . MET   A 1 103 ? -1.94   -21.361 -35.897 1 57.22  ? 88  MET   A C   1 
ATOM   714  O  O   . MET   A 1 103 ? -1.587  -21.055 -37.024 1 57.4   ? 88  MET   A O   1 
ATOM   715  C  CB  . MET   A 1 103 ? -0.251  -22.223 -34.231 1 58.88  ? 88  MET   A CB  1 
ATOM   716  C  CG  . MET   A 1 103 ? 0.734   -21.935 -33.1   1 62.77  ? 88  MET   A CG  1 
ATOM   717  S  SD  . MET   A 1 103 ? 1.921   -20.615 -33.46  1 70.51  ? 88  MET   A SD  1 
ATOM   718  C  CE  . MET   A 1 103 ? 3.436   -21.395 -32.985 1 72.82  ? 88  MET   A CE  1 
ATOM   719  N  N   . ALA   A 1 104 ? -3.099  -21.966 -35.652 1 57.2   ? 89  ALA   A N   1 
ATOM   720  C  CA  . ALA   A 1 104 ? -4.018  -22.356 -36.715 1 57.8   ? 89  ALA   A CA  1 
ATOM   721  C  C   . ALA   A 1 104 ? -4.63   -21.144 -37.404 1 58.67  ? 89  ALA   A C   1 
ATOM   722  O  O   . ALA   A 1 104 ? -4.86   -21.174 -38.614 1 58.8   ? 89  ALA   A O   1 
ATOM   723  C  CB  . ALA   A 1 104 ? -5.118  -23.235 -36.153 1 57.62  ? 89  ALA   A CB  1 
ATOM   724  N  N   . TYR   A 1 105 ? -4.913  -20.08  -36.637 1 58.63  ? 90  TYR   A N   1 
ATOM   725  C  CA  . TYR   A 1 105 ? -5.499  -18.869 -37.191 1 58.51  ? 90  TYR   A CA  1 
ATOM   726  C  C   . TYR   A 1 105 ? -4.489  -18.141 -38.076 1 58.06  ? 90  TYR   A C   1 
ATOM   727  O  O   . TYR   A 1 105 ? -4.836  -17.711 -39.175 1 57.73  ? 90  TYR   A O   1 
ATOM   728  C  CB  . TYR   A 1 105 ? -6.024  -17.947 -36.072 1 58.49  ? 90  TYR   A CB  1 
ATOM   729  C  CG  . TYR   A 1 105 ? -6.736  -16.727 -36.613 1 59.67  ? 90  TYR   A CG  1 
ATOM   730  C  CD1 . TYR   A 1 105 ? -8.097  -16.761 -36.904 1 60.7   ? 90  TYR   A CD1 1 
ATOM   731  C  CD2 . TYR   A 1 105 ? -6.046  -15.548 -36.863 1 60.68  ? 90  TYR   A CD2 1 
ATOM   732  C  CE1 . TYR   A 1 105 ? -8.748  -15.655 -37.436 1 61.67  ? 90  TYR   A CE1 1 
ATOM   733  C  CE2 . TYR   A 1 105 ? -6.677  -14.451 -37.427 1 61.91  ? 90  TYR   A CE2 1 
ATOM   734  C  CZ  . TYR   A 1 105 ? -8.031  -14.506 -37.707 1 63.1   ? 90  TYR   A CZ  1 
ATOM   735  O  OH  . TYR   A 1 105 ? -8.659  -13.394 -38.207 1 65.38  ? 90  TYR   A OH  1 
ATOM   736  N  N   . VAL   A 1 106 ? -3.25   -17.989 -37.589 1 57.82  ? 91  VAL   A N   1 
ATOM   737  C  CA  . VAL   A 1 106 ? -2.22   -17.28  -38.332 1 58.02  ? 91  VAL   A CA  1 
ATOM   738  C  C   . VAL   A 1 106 ? -1.851  -17.986 -39.628 1 59.41  ? 91  VAL   A C   1 
ATOM   739  O  O   . VAL   A 1 106 ? -1.71   -17.331 -40.662 1 60.05  ? 91  VAL   A O   1 
ATOM   740  C  CB  . VAL   A 1 106 ? -0.979  -16.989 -37.451 1 57.45  ? 91  VAL   A CB  1 
ATOM   741  C  CG1 . VAL   A 1 106 ? 0.179   -16.438 -38.276 1 57.62  ? 91  VAL   A CG1 1 
ATOM   742  C  CG2 . VAL   A 1 106 ? -1.327  -16.03  -36.329 1 57.53  ? 91  VAL   A CG2 1 
ATOM   743  N  N   . TRP   A 1 107 ? -1.719  -19.313 -39.589 1 59.74  ? 92  TRP   A N   1 
ATOM   744  C  CA  . TRP   A 1 107 ? -1.261  -20.056 -40.75  1 60.1   ? 92  TRP   A CA  1 
ATOM   745  C  C   . TRP   A 1 107 ? -2.36   -20.6   -41.634 1 61.27  ? 92  TRP   A C   1 
ATOM   746  O  O   . TRP   A 1 107 ? -2.127  -20.791 -42.825 1 61.59  ? 92  TRP   A O   1 
ATOM   747  C  CB  . TRP   A 1 107 ? -0.287  -21.171 -40.325 1 59.37  ? 92  TRP   A CB  1 
ATOM   748  C  CG  . TRP   A 1 107 ? 0.898   -20.678 -39.536 1 58.88  ? 92  TRP   A CG  1 
ATOM   749  C  CD1 . TRP   A 1 107 ? 1.255   -21.054 -38.274 1 59.48  ? 92  TRP   A CD1 1 
ATOM   750  C  CD2 . TRP   A 1 107 ? 1.89    -19.73  -39.967 1 58.34  ? 92  TRP   A CD2 1 
ATOM   751  N  NE1 . TRP   A 1 107 ? 2.393   -20.386 -37.884 1 59.53  ? 92  TRP   A NE1 1 
ATOM   752  C  CE2 . TRP   A 1 107 ? 2.8     -19.563 -38.902 1 59.08  ? 92  TRP   A CE2 1 
ATOM   753  C  CE3 . TRP   A 1 107 ? 2.071   -18.976 -41.136 1 58.57  ? 92  TRP   A CE3 1 
ATOM   754  C  CZ2 . TRP   A 1 107 ? 3.871   -18.675 -38.97  1 59.72  ? 92  TRP   A CZ2 1 
ATOM   755  C  CZ3 . TRP   A 1 107 ? 3.129   -18.093 -41.201 1 59.48  ? 92  TRP   A CZ3 1 
ATOM   756  C  CH2 . TRP   A 1 107 ? 4.031   -17.968 -40.139 1 59.79  ? 92  TRP   A CH2 1 
ATOM   757  N  N   . GLY   A 1 108 ? -3.535  -20.841 -41.076 1 62.1   ? 93  GLY   A N   1 
ATOM   758  C  CA  . GLY   A 1 108 ? -4.661  -21.384 -41.827 1 63.88  ? 93  GLY   A CA  1 
ATOM   759  C  C   . GLY   A 1 108 ? -4.338  -22.741 -42.42  1 65.54  ? 93  GLY   A C   1 
ATOM   760  O  O   . GLY   A 1 108 ? -3.848  -23.614 -41.708 1 65.48  ? 93  GLY   A O   1 
ATOM   761  N  N   . LYS   A 1 109 ? -4.543  -22.912 -43.737 1 66.51  ? 94  LYS   A N   1 
ATOM   762  C  CA  . LYS   A 1 109 ? -4.171  -24.165 -44.411 1 67.85  ? 94  LYS   A CA  1 
ATOM   763  C  C   . LYS   A 1 109 ? -2.647  -24.302 -44.638 1 70.08  ? 94  LYS   A C   1 
ATOM   764  O  O   . LYS   A 1 109 ? -2.177  -25.368 -45.026 1 70.57  ? 94  LYS   A O   1 
ATOM   765  C  CB  . LYS   A 1 109 ? -4.951  -24.358 -45.718 1 68.67  ? 94  LYS   A CB  1 
ATOM   766  C  CG  . LYS   A 1 109 ? -6.382  -24.842 -45.509 1 71.36  ? 94  LYS   A CG  1 
ATOM   767  C  CD  . LYS   A 1 109 ? -7.196  -24.818 -46.796 1 74.37  ? 94  LYS   A CD  1 
ATOM   768  C  CE  . LYS   A 1 109 ? -8.564  -25.409 -46.565 1 77.94  ? 94  LYS   A CE  1 
ATOM   769  N  NZ  . LYS   A 1 109 ? -9.522  -25.095 -47.658 1 80.14  ? 94  LYS   A NZ  1 
ATOM   770  N  N   . GLY   A 1 110 ? -1.901  -23.234 -44.378 1 71.51  ? 95  GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 110 ? -0.453  -23.199 -44.464 1 73.7   ? 95  GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 110 ? 0.132   -23.153 -45.85  1 75.91  ? 95  GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 110 ? 1.329   -23.419 -46.021 1 76.58  ? 95  GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 111 ? -0.682  -22.793 -46.835 1 77     ? 96  HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 111 ? -0.195  -22.747 -48.197 1 78.72  ? 96  HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 111 ? -0.292  -21.351 -48.772 1 79.5   ? 96  HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 111 ? -0.809  -21.154 -49.87  1 79.88  ? 96  HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 111 ? -0.857  -23.835 -49.054 1 80.43  ? 96  HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 111 ? -0.362  -25.191 -48.647 1 84.36  ? 96  HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 111 ? 0.999   -25.504 -48.684 1 86.65  ? 96  HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 111 ? -1.032  -26.232 -48.099 1 85.9   ? 96  HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 111 ? 1.1     -26.733 -48.199 1 87.33  ? 96  HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 111 ? -0.094  -27.216 -47.836 1 87.33  ? 96  HIS   A NE2 1 
ATOM   784  N  N   . GLY   A 1 112 ? 0.245   -20.391 -48.026 1 79.48  ? 97  GLY   A N   1 
ATOM   785  C  CA  . GLY   A 1 112 ? 0.299   -19.009 -48.487 1 79.85  ? 97  GLY   A CA  1 
ATOM   786  C  C   . GLY   A 1 112 ? -0.424  -17.943 -47.684 1 79.96  ? 97  GLY   A C   1 
ATOM   787  O  O   . GLY   A 1 112 ? 0.22    -17.022 -47.169 1 80.62  ? 97  GLY   A O   1 
ATOM   788  N  N   . ASP   A 1 113 ? -1.775  -18.008 -47.631 1 78.94  ? 98  ASP   A N   1 
ATOM   789  C  CA  . ASP   A 1 113 ? -2.597  -16.999 -46.953 1 78.22  ? 98  ASP   A CA  1 
ATOM   790  C  C   . ASP   A 1 113 ? -2.364  -16.923 -45.446 1 77.21  ? 98  ASP   A C   1 
ATOM   791  O  O   . ASP   A 1 113 ? -2.874  -17.747 -44.689 1 77.88  ? 98  ASP   A O   1 
ATOM   792  C  CB  . ASP   A 1 113 ? -4.093  -17.191 -47.266 1 79.9   ? 98  ASP   A CB  1 
ATOM   793  C  CG  . ASP   A 1 113 ? -4.982  -16.049 -46.79  1 84.74  ? 98  ASP   A CG  1 
ATOM   794  O  OD1 . ASP   A 1 113 ? -4.501  -14.889 -46.757 1 85.18  ? 98  ASP   A OD1 1 
ATOM   795  O  OD2 . ASP   A 1 113 ? -6.165  -16.311 -46.463 1 87.09  ? 98  ASP   A OD2 1 
ATOM   796  N  N   . VAL   A 1 114 ? -1.621  -15.91  -45.013 1 75.5   ? 99  VAL   A N   1 
ATOM   797  C  CA  . VAL   A 1 114 ? -1.331  -15.704 -43.602 1 74.31  ? 99  VAL   A CA  1 
ATOM   798  C  C   . VAL   A 1 114 ? -2.218  -14.608 -43.029 1 72.78  ? 99  VAL   A C   1 
ATOM   799  O  O   . VAL   A 1 114 ? -2.53   -13.654 -43.727 1 73.16  ? 99  VAL   A O   1 
ATOM   800  C  CB  . VAL   A 1 114 ? 0.165   -15.345 -43.435 1 75.08  ? 99  VAL   A CB  1 
ATOM   801  C  CG1 . VAL   A 1 114 ? 0.479   -14.921 -42.01  1 75.75  ? 99  VAL   A CG1 1 
ATOM   802  C  CG2 . VAL   A 1 114 ? 1.055   -16.506 -43.855 1 75.63  ? 99  VAL   A CG2 1 
ATOM   803  N  N   . ARG   A 1 115 ? -2.615  -14.727 -41.761 1 71.22  ? 100 ARG   A N   1 
ATOM   804  C  CA  . ARG   A 1 115 ? -3.361  -13.674 -41.077 1 70.03  ? 100 ARG   A CA  1 
ATOM   805  C  C   . ARG   A 1 115 ? -2.33   -12.887 -40.259 1 69.16  ? 100 ARG   A C   1 
ATOM   806  O  O   . ARG   A 1 115 ? -1.635  -13.472 -39.427 1 69.28  ? 100 ARG   A O   1 
ATOM   807  C  CB  . ARG   A 1 115 ? -4.407  -14.266 -40.131 1 70.45  ? 100 ARG   A CB  1 
ATOM   808  C  CG  . ARG   A 1 115 ? -5.684  -14.707 -40.8   1 72.69  ? 100 ARG   A CG  1 
ATOM   809  C  CD  . ARG   A 1 115 ? -6.496  -13.56  -41.365 1 75.05  ? 100 ARG   A CD  1 
ATOM   810  N  NE  . ARG   A 1 115 ? -7.587  -14.047 -42.214 1 77.5   ? 100 ARG   A NE  1 
ATOM   811  C  CZ  . ARG   A 1 115 ? -7.456  -14.346 -43.504 1 79.54  ? 100 ARG   A CZ  1 
ATOM   812  N  NH1 . ARG   A 1 115 ? -6.281  -14.201 -44.113 1 78.78  ? 100 ARG   A NH1 1 
ATOM   813  N  NH2 . ARG   A 1 115 ? -8.493  -14.8   -44.196 1 79.51  ? 100 ARG   A NH2 1 
ATOM   814  N  N   . LYS   A 1 116 ? -2.19   -11.582 -40.514 1 68     ? 101 LYS   A N   1 
ATOM   815  C  CA  . LYS   A 1 116 ? -1.223  -10.758 -39.785 1 66.62  ? 101 LYS   A CA  1 
ATOM   816  C  C   . LYS   A 1 116 ? -1.805  -10.111 -38.508 1 65.28  ? 101 LYS   A C   1 
ATOM   817  O  O   . LYS   A 1 116 ? -1.066  -9.46   -37.772 1 65.4   ? 101 LYS   A O   1 
ATOM   818  C  CB  . LYS   A 1 116 ? -0.603  -9.709  -40.716 1 68.02  ? 101 LYS   A CB  1 
ATOM   819  N  N   . VAL   A 1 117 ? -3.112  -10.283 -38.236 1 63.99  ? 102 VAL   A N   1 
ATOM   820  C  CA  . VAL   A 1 117 ? -3.733  -9.705  -37.046 1 63.83  ? 102 VAL   A CA  1 
ATOM   821  C  C   . VAL   A 1 117 ? -4.502  -10.763 -36.276 1 64.09  ? 102 VAL   A C   1 
ATOM   822  O  O   . VAL   A 1 117 ? -5.381  -11.414 -36.838 1 64.39  ? 102 VAL   A O   1 
ATOM   823  C  CB  . VAL   A 1 117 ? -4.641  -8.48   -37.39  1 64.06  ? 102 VAL   A CB  1 
ATOM   824  C  CG1 . VAL   A 1 117 ? -5.592  -8.108  -36.239 1 64.03  ? 102 VAL   A CG1 1 
ATOM   825  C  CG2 . VAL   A 1 117 ? -3.806  -7.274  -37.806 1 64.4   ? 102 VAL   A CG2 1 
ATOM   826  N  N   . LEU   A 1 118 ? -4.221  -10.896 -34.981 1 63.98  ? 103 LEU   A N   1 
ATOM   827  C  CA  . LEU   A 1 118 ? -4.946  -11.834 -34.138 1 64.93  ? 103 LEU   A CA  1 
ATOM   828  C  C   . LEU   A 1 118 ? -6.127  -11.098 -33.502 1 66.14  ? 103 LEU   A C   1 
ATOM   829  O  O   . LEU   A 1 118 ? -5.907  -10.11  -32.815 1 66.44  ? 103 LEU   A O   1 
ATOM   830  C  CB  . LEU   A 1 118 ? -4.009  -12.389 -33.061 1 64.81  ? 103 LEU   A CB  1 
ATOM   831  C  CG  . LEU   A 1 118 ? -4.535  -13.579 -32.288 1 65.46  ? 103 LEU   A CG  1 
ATOM   832  C  CD1 . LEU   A 1 118 ? -4.749  -14.765 -33.2   1 65.33  ? 103 LEU   A CD1 1 
ATOM   833  C  CD2 . LEU   A 1 118 ? -3.592  -13.929 -31.151 1 66.1   ? 103 LEU   A CD2 1 
ATOM   834  N  N   . PRO   A 1 119 ? -7.382  -11.532 -33.759 1 66.82  ? 104 PRO   A N   1 
ATOM   835  C  CA  . PRO   A 1 119 ? -8.556  -10.82  -33.206 1 67.59  ? 104 PRO   A CA  1 
ATOM   836  C  C   . PRO   A 1 119 ? -8.525  -10.626 -31.694 1 68.74  ? 104 PRO   A C   1 
ATOM   837  O  O   . PRO   A 1 119 ? -8.036  -11.495 -30.993 1 68.97  ? 104 PRO   A O   1 
ATOM   838  C  CB  . PRO   A 1 119 ? -9.751  -11.682 -33.651 1 67.93  ? 104 PRO   A CB  1 
ATOM   839  C  CG  . PRO   A 1 119 ? -9.172  -12.977 -34.076 1 68.25  ? 104 PRO   A CG  1 
ATOM   840  C  CD  . PRO   A 1 119 ? -7.796  -12.675 -34.586 1 66.43  ? 104 PRO   A CD  1 
ATOM   841  N  N   . ARG   A 1 120 ? -9.053  -9.503  -31.193 1 69.21  ? 105 ARG   A N   1 
ATOM   842  C  CA  . ARG   A 1 120 ? -8.992  -9.196  -29.771 1 70.42  ? 105 ARG   A CA  1 
ATOM   843  C  C   . ARG   A 1 120 ? -9.746  -10.181 -28.893 1 70.23  ? 105 ARG   A C   1 
ATOM   844  O  O   . ARG   A 1 120 ? -9.291  -10.444 -27.79  1 69.99  ? 105 ARG   A O   1 
ATOM   845  C  CB  . ARG   A 1 120 ? -9.405  -7.745  -29.476 1 73.32  ? 105 ARG   A CB  1 
ATOM   846  C  CG  . ARG   A 1 120 ? -10.886 -7.468  -29.318 1 78.98  ? 105 ARG   A CG  1 
ATOM   847  C  CD  . ARG   A 1 120 ? -11.093 -5.999  -28.962 1 83.69  ? 105 ARG   A CD  1 
ATOM   848  N  NE  . ARG   A 1 120 ? -10.72  -5.114  -30.067 1 87.36  ? 105 ARG   A NE  1 
ATOM   849  C  CZ  . ARG   A 1 120 ? -11.485 -4.886  -31.132 1 92.04  ? 105 ARG   A CZ  1 
ATOM   850  N  NH1 . ARG   A 1 120 ? -11.066 -4.08   -32.097 1 92.66  ? 105 ARG   A NH1 1 
ATOM   851  N  NH2 . ARG   A 1 120 ? -12.668 -5.484  -31.251 1 93.14  ? 105 ARG   A NH2 1 
ATOM   852  N  N   . ASN   A 1 121 ? -10.85  -10.761 -29.376 1 70.59  ? 106 ASN   A N   1 
ATOM   853  C  CA  . ASN   A 1 121 ? -11.631 -11.741 -28.604 1 71.46  ? 106 ASN   A CA  1 
ATOM   854  C  C   . ASN   A 1 121 ? -10.807 -12.992 -28.182 1 71.14  ? 106 ASN   A C   1 
ATOM   855  O  O   . ASN   A 1 121 ? -11.207 -13.724 -27.26  1 70.8   ? 106 ASN   A O   1 
ATOM   856  C  CB  . ASN   A 1 121 ? -12.937 -12.135 -29.329 1 73.89  ? 106 ASN   A CB  1 
ATOM   857  C  CG  . ASN   A 1 121 ? -12.822 -12.337 -30.831 1 78.8   ? 106 ASN   A CG  1 
ATOM   858  O  OD1 . ASN   A 1 121 ? -12.565 -13.456 -31.308 1 80.39  ? 106 ASN   A OD1 1 
ATOM   859  N  ND2 . ASN   A 1 121 ? -13.045 -11.263 -31.61  1 79.25  ? 106 ASN   A ND2 1 
ATOM   860  N  N   . ILE   A 1 122 ? -9.633  -13.204 -28.835 1 70.68  ? 107 ILE   A N   1 
ATOM   861  C  CA  . ILE   A 1 122 ? -8.714  -14.28  -28.489 1 70.22  ? 107 ILE   A CA  1 
ATOM   862  C  C   . ILE   A 1 122 ? -7.35   -13.72  -28.03  1 69.24  ? 107 ILE   A C   1 
ATOM   863  O  O   . ILE   A 1 122 ? -6.821  -14.182 -27.032 1 69.43  ? 107 ILE   A O   1 
ATOM   864  C  CB  . ILE   A 1 122 ? -8.594  -15.358 -29.595 1 71.2   ? 107 ILE   A CB  1 
ATOM   865  C  CG1 . ILE   A 1 122 ? -7.797  -16.545 -29.077 1 72.86  ? 107 ILE   A CG1 1 
ATOM   866  C  CG2 . ILE   A 1 122 ? -8.002  -14.8   -30.893 1 71.6   ? 107 ILE   A CG2 1 
ATOM   867  C  CD1 . ILE   A 1 122 ? -7.749  -17.678 -29.954 1 74.8   ? 107 ILE   A CD1 1 
ATOM   868  N  N   . ALA   A 1 123 ? -6.819  -12.692 -28.704 1 68.42  ? 108 ALA   A N   1 
ATOM   869  C  CA  . ALA   A 1 123 ? -5.526  -12.082 -28.38  1 68.22  ? 108 ALA   A CA  1 
ATOM   870  C  C   . ALA   A 1 123 ? -5.477  -11.414 -27.002 1 68.62  ? 108 ALA   A C   1 
ATOM   871  O  O   . ALA   A 1 123 ? -4.429  -11.444 -26.349 1 69.48  ? 108 ALA   A O   1 
ATOM   872  C  CB  . ALA   A 1 123 ? -5.122  -11.082 -29.454 1 67.92  ? 108 ALA   A CB  1 
ATOM   873  N  N   . VAL   A 1 124 ? -6.582  -10.785 -26.566 1 67.54  ? 109 VAL   A N   1 
ATOM   874  C  CA  . VAL   A 1 124 ? -6.605  -10.132 -25.257 1 66.57  ? 109 VAL   A CA  1 
ATOM   875  C  C   . VAL   A 1 124 ? -6.466  -11.167 -24.136 1 64.97  ? 109 VAL   A C   1 
ATOM   876  O  O   . VAL   A 1 124 ? -5.487  -11.079 -23.395 1 65.17  ? 109 VAL   A O   1 
ATOM   877  C  CB  . VAL   A 1 124 ? -7.801  -9.165  -25.068 1 67.33  ? 109 VAL   A CB  1 
ATOM   878  C  CG1 . VAL   A 1 124 ? -7.971  -8.761  -23.605 1 67.43  ? 109 VAL   A CG1 1 
ATOM   879  C  CG2 . VAL   A 1 124 ? -7.622  -7.939  -25.951 1 68.17  ? 109 VAL   A CG2 1 
ATOM   880  N  N   . PRO   A 1 125 ? -7.343  -12.191 -24.034 1 63.26  ? 110 PRO   A N   1 
ATOM   881  C  CA  . PRO   A 1 125 ? -7.162  -13.178 -22.96  1 62.51  ? 110 PRO   A CA  1 
ATOM   882  C  C   . PRO   A 1 125 ? -5.891  -14.031 -23.106 1 61.92  ? 110 PRO   A C   1 
ATOM   883  O  O   . PRO   A 1 125 ? -5.356  -14.503 -22.097 1 62.24  ? 110 PRO   A O   1 
ATOM   884  C  CB  . PRO   A 1 125 ? -8.461  -14.002 -22.989 1 63.33  ? 110 PRO   A CB  1 
ATOM   885  C  CG  . PRO   A 1 125 ? -9.049  -13.79  -24.325 1 63.92  ? 110 PRO   A CG  1 
ATOM   886  C  CD  . PRO   A 1 125 ? -8.572  -12.455 -24.819 1 62.54  ? 110 PRO   A CD  1 
ATOM   887  N  N   . TYR   A 1 126 ? -5.375  -14.198 -24.343 1 60.45  ? 111 TYR   A N   1 
ATOM   888  C  CA  . TYR   A 1 126 ? -4.154  -14.966 -24.542 1 59.54  ? 111 TYR   A CA  1 
ATOM   889  C  C   . TYR   A 1 126 ? -2.988  -14.212 -23.937 1 59.25  ? 111 TYR   A C   1 
ATOM   890  O  O   . TYR   A 1 126 ? -2.231  -14.79  -23.168 1 59.56  ? 111 TYR   A O   1 
ATOM   891  C  CB  . TYR   A 1 126 ? -3.915  -15.282 -26.03  1 59.09  ? 111 TYR   A CB  1 
ATOM   892  C  CG  . TYR   A 1 126 ? -2.794  -16.267 -26.292 1 59.29  ? 111 TYR   A CG  1 
ATOM   893  C  CD1 . TYR   A 1 126 ? -2.473  -17.249 -25.368 1 59.94  ? 111 TYR   A CD1 1 
ATOM   894  C  CD2 . TYR   A 1 126 ? -2.111  -16.268 -27.498 1 59.92  ? 111 TYR   A CD2 1 
ATOM   895  C  CE1 . TYR   A 1 126 ? -1.461  -18.166 -25.612 1 60.49  ? 111 TYR   A CE1 1 
ATOM   896  C  CE2 . TYR   A 1 126 ? -1.114  -17.198 -27.763 1 60.68  ? 111 TYR   A CE2 1 
ATOM   897  C  CZ  . TYR   A 1 126 ? -0.782  -18.138 -26.811 1 61.27  ? 111 TYR   A CZ  1 
ATOM   898  O  OH  . TYR   A 1 126 ? 0.212   -19.05  -27.053 1 62.47  ? 111 TYR   A OH  1 
ATOM   899  N  N   . CYS   A 1 127 ? -2.871  -12.911 -24.231 1 58.82  ? 112 CYS   A N   1 
ATOM   900  C  CA  . CYS   A 1 127 ? -1.796  -12.093 -23.68  1 58.65  ? 112 CYS   A CA  1 
ATOM   901  C  C   . CYS   A 1 127 ? -1.934  -11.869 -22.178 1 58.79  ? 112 CYS   A C   1 
ATOM   902  O  O   . CYS   A 1 127 ? -0.926  -11.676 -21.499 1 59.25  ? 112 CYS   A O   1 
ATOM   903  C  CB  . CYS   A 1 127 ? -1.709  -10.773 -24.418 1 59.09  ? 112 CYS   A CB  1 
ATOM   904  S  SG  . CYS   A 1 127 ? -1.251  -10.922 -26.156 1 63.35  ? 112 CYS   A SG  1 
ATOM   905  N  N   . GLN   A 1 128 ? -3.17   -11.875 -21.664 1 58.27  ? 113 GLN   A N   1 
ATOM   906  C  CA  . GLN   A 1 128 ? -3.438  -11.708 -20.247 1 58.59  ? 113 GLN   A CA  1 
ATOM   907  C  C   . GLN   A 1 128 ? -2.928  -12.926 -19.489 1 58.72  ? 113 GLN   A C   1 
ATOM   908  O  O   . GLN   A 1 128 ? -2.157  -12.778 -18.544 1 59.52  ? 113 GLN   A O   1 
ATOM   909  C  CB  . GLN   A 1 128 ? -4.945  -11.495 -19.996 1 60.18  ? 113 GLN   A CB  1 
ATOM   910  C  CG  . GLN   A 1 128 ? -5.43   -10.105 -20.352 1 63.94  ? 113 GLN   A CG  1 
ATOM   911  C  CD  . GLN   A 1 128 ? -6.918  -9.941  -20.169 1 69.96  ? 113 GLN   A CD  1 
ATOM   912  O  OE1 . GLN   A 1 128 ? -7.694  -10.907 -20.037 1 71.4   ? 113 GLN   A OE1 1 
ATOM   913  N  NE2 . GLN   A 1 128 ? -7.349  -8.692  -20.154 1 71.68  ? 113 GLN   A NE2 1 
ATOM   914  N  N   . LEU   A 1 129 ? -3.313  -14.125 -19.938 1 57.99  ? 114 LEU   A N   1 
ATOM   915  C  CA  . LEU   A 1 129 ? -2.916  -15.393 -19.347 1 57.98  ? 114 LEU   A CA  1 
ATOM   916  C  C   . LEU   A 1 129 ? -1.409  -15.619 -19.509 1 58.13  ? 114 LEU   A C   1 
ATOM   917  O  O   . LEU   A 1 129 ? -0.758  -16.111 -18.589 1 58.65  ? 114 LEU   A O   1 
ATOM   918  C  CB  . LEU   A 1 129 ? -3.712  -16.49  -20.037 1 58.48  ? 114 LEU   A CB  1 
ATOM   919  C  CG  . LEU   A 1 129 ? -3.424  -17.91  -19.632 1 60.17  ? 114 LEU   A CG  1 
ATOM   920  C  CD1 . LEU   A 1 129 ? -3.941  -18.194 -18.244 1 60.87  ? 114 LEU   A CD1 1 
ATOM   921  C  CD2 . LEU   A 1 129 ? -4.052  -18.848 -20.603 1 60.52  ? 114 LEU   A CD2 1 
ATOM   922  N  N   . SER   A 1 130 ? -0.842  -15.197 -20.646 1 57.41  ? 115 SER   A N   1 
ATOM   923  C  CA  . SER   A 1 130 ? 0.587   -15.291 -20.9   1 57.33  ? 115 SER   A CA  1 
ATOM   924  C  C   . SER   A 1 130 ? 1.365   -14.396 -19.941 1 57.66  ? 115 SER   A C   1 
ATOM   925  O  O   . SER   A 1 130 ? 2.438   -14.783 -19.489 1 58.06  ? 115 SER   A O   1 
ATOM   926  C  CB  . SER   A 1 130 ? 0.89    -14.88  -22.333 1 58.28  ? 115 SER   A CB  1 
ATOM   927  O  OG  . SER   A 1 130 ? 0.385   -15.84  -23.238 1 60.74  ? 115 SER   A OG  1 
ATOM   928  N  N   . LYS   A 1 131 ? 0.849   -13.19  -19.655 1 57.55  ? 116 LYS   A N   1 
ATOM   929  C  CA  . LYS   A 1 131 ? 1.49    -12.254 -18.722 1 57.61  ? 116 LYS   A CA  1 
ATOM   930  C  C   . LYS   A 1 131 ? 1.468   -12.822 -17.299 1 56.35  ? 116 LYS   A C   1 
ATOM   931  O  O   . LYS   A 1 131 ? 2.44    -12.674 -16.576 1 56.31  ? 116 LYS   A O   1 
ATOM   932  C  CB  . LYS   A 1 131 ? 0.786   -10.881 -18.743 1 59.99  ? 116 LYS   A CB  1 
ATOM   933  N  N   . LYS   A 1 132 ? 0.378   -13.489 -16.914 1 55.53  ? 117 LYS   A N   1 
ATOM   934  C  CA  . LYS   A 1 132 ? 0.279   -14.09  -15.585 1 55.43  ? 117 LYS   A CA  1 
ATOM   935  C  C   . LYS   A 1 132 ? 1.326   -15.202 -15.422 1 55.3   ? 117 LYS   A C   1 
ATOM   936  O  O   . LYS   A 1 132 ? 2.035   -15.237 -14.426 1 55.25  ? 117 LYS   A O   1 
ATOM   937  C  CB  . LYS   A 1 132 ? -1.149  -14.62  -15.316 1 56.34  ? 117 LYS   A CB  1 
ATOM   938  N  N   . LEU   A 1 133 ? 1.451   -16.077 -16.432 1 55.13  ? 118 LEU   A N   1 
ATOM   939  C  CA  . LEU   A 1 133 ? 2.375   -17.211 -16.414 1 54.56  ? 118 LEU   A CA  1 
ATOM   940  C  C   . LEU   A 1 133 ? 3.814   -16.881 -16.833 1 54.19  ? 118 LEU   A C   1 
ATOM   941  O  O   . LEU   A 1 133 ? 4.641   -17.79  -16.907 1 54.75  ? 118 LEU   A O   1 
ATOM   942  C  CB  . LEU   A 1 133 ? 1.824   -18.357 -17.279 1 54.44  ? 118 LEU   A CB  1 
ATOM   943  C  CG  . LEU   A 1 133 ? 0.542   -19.03  -16.802 1 55.48  ? 118 LEU   A CG  1 
ATOM   944  C  CD1 . LEU   A 1 133 ? 0.125   -20.104 -17.75  1 55.84  ? 118 LEU   A CD1 1 
ATOM   945  C  CD2 . LEU   A 1 133 ? 0.713   -19.64  -15.437 1 56.24  ? 118 LEU   A CD2 1 
ATOM   946  N  N   . GLU   A 1 134 ? 4.113   -15.608 -17.118 1 53.21  ? 119 GLU   A N   1 
ATOM   947  C  CA  . GLU   A 1 134 ? 5.44    -15.151 -17.54  1 52.51  ? 119 GLU   A CA  1 
ATOM   948  C  C   . GLU   A 1 134 ? 5.974   -15.846 -18.791 1 51.8   ? 119 GLU   A C   1 
ATOM   949  O  O   . GLU   A 1 134 ? 7.182   -16.067 -18.92  1 51.8   ? 119 GLU   A O   1 
ATOM   950  C  CB  . GLU   A 1 134 ? 6.451   -15.245 -16.407 1 54.16  ? 119 GLU   A CB  1 
ATOM   951  C  CG  . GLU   A 1 134 ? 6.037   -14.488 -15.173 1 58.37  ? 119 GLU   A CG  1 
ATOM   952  C  CD  . GLU   A 1 134 ? 7.149   -14.473 -14.155 1 63.95  ? 119 GLU   A CD  1 
ATOM   953  O  OE1 . GLU   A 1 134 ? 8.314   -14.24  -14.557 1 66.27  ? 119 GLU   A OE1 1 
ATOM   954  O  OE2 . GLU   A 1 134 ? 6.864   -14.725 -12.963 1 65.52  ? 119 GLU   A OE2 1 
ATOM   955  N  N   . LEU   A 1 135 ? 5.074   -16.178 -19.716 1 50.86  ? 120 LEU   A N   1 
ATOM   956  C  CA  . LEU   A 1 135 ? 5.439   -16.809 -20.98  1 50.34  ? 120 LEU   A CA  1 
ATOM   957  C  C   . LEU   A 1 135 ? 4.963   -15.945 -22.154 1 50.47  ? 120 LEU   A C   1 
ATOM   958  O  O   . LEU   A 1 135 ? 4.016   -15.172 -22.004 1 50.66  ? 120 LEU   A O   1 
ATOM   959  C  CB  . LEU   A 1 135 ? 4.816   -18.202 -21.048 1 49.87  ? 120 LEU   A CB  1 
ATOM   960  C  CG  . LEU   A 1 135 ? 5.469   -19.242 -20.165 1 49.77  ? 120 LEU   A CG  1 
ATOM   961  C  CD1 . LEU   A 1 135 ? 4.529   -20.406 -19.915 1 49.7   ? 120 LEU   A CD1 1 
ATOM   962  C  CD2 . LEU   A 1 135 ? 6.762   -19.698 -20.759 1 49.67  ? 120 LEU   A CD2 1 
ATOM   963  N  N   . PRO   A 1 136 ? 5.608   -16.027 -23.332 1 50.3   ? 121 PRO   A N   1 
ATOM   964  C  CA  . PRO   A 1 136 ? 5.172   -15.188 -24.467 1 50.12  ? 121 PRO   A CA  1 
ATOM   965  C  C   . PRO   A 1 136 ? 3.841   -15.651 -25.056 1 51.03  ? 121 PRO   A C   1 
ATOM   966  O  O   . PRO   A 1 136 ? 3.48    -16.826 -24.934 1 51.41  ? 121 PRO   A O   1 
ATOM   967  C  CB  . PRO   A 1 136 ? 6.309   -15.35  -25.487 1 50.4   ? 121 PRO   A CB  1 
ATOM   968  C  CG  . PRO   A 1 136 ? 7.431   -16.002 -24.74  1 51.42  ? 121 PRO   A CG  1 
ATOM   969  C  CD  . PRO   A 1 136 ? 6.768   -16.853 -23.7   1 49.8   ? 121 PRO   A CD  1 
ATOM   970  N  N   . PRO   A 1 137 ? 3.095   -14.754 -25.715 1 50.88  ? 122 PRO   A N   1 
ATOM   971  C  CA  . PRO   A 1 137 ? 1.834   -15.169 -26.33  1 51.02  ? 122 PRO   A CA  1 
ATOM   972  C  C   . PRO   A 1 137 ? 2.05    -15.886 -27.674 1 51.36  ? 122 PRO   A C   1 
ATOM   973  O  O   . PRO   A 1 137 ? 1.586   -15.444 -28.722 1 51.64  ? 122 PRO   A O   1 
ATOM   974  C  CB  . PRO   A 1 137 ? 1.068   -13.858 -26.477 1 51.59  ? 122 PRO   A CB  1 
ATOM   975  C  CG  . PRO   A 1 137 ? 2.122   -12.842 -26.649 1 52.13  ? 122 PRO   A CG  1 
ATOM   976  C  CD  . PRO   A 1 137 ? 3.36    -13.324 -25.938 1 50.57  ? 122 PRO   A CD  1 
ATOM   977  N  N   . ILE   A 1 138 ? 2.761   -17.01  -27.628 1 50.62  ? 123 ILE   A N   1 
ATOM   978  C  CA  . ILE   A 1 138 ? 3.015   -17.918 -28.739 1 49.66  ? 123 ILE   A CA  1 
ATOM   979  C  C   . ILE   A 1 138 ? 3.133   -19.325 -28.163 1 49.9   ? 123 ILE   A C   1 
ATOM   980  O  O   . ILE   A 1 138 ? 3.497   -19.501 -26.991 1 50.71  ? 123 ILE   A O   1 
ATOM   981  C  CB  . ILE   A 1 138 ? 4.228   -17.519 -29.617 1 48.98  ? 123 ILE   A CB  1 
ATOM   982  C  CG1 . ILE   A 1 138 ? 4.236   -18.295 -30.964 1 48.98  ? 123 ILE   A CG1 1 
ATOM   983  C  CG2 . ILE   A 1 138 ? 5.549   -17.654 -28.865 1 48.99  ? 123 ILE   A CG2 1 
ATOM   984  C  CD1 . ILE   A 1 138 ? 5.231   -17.842 -31.967 1 49.27  ? 123 ILE   A CD1 1 
ATOM   985  N  N   . LEU   A 1 139 ? 2.773   -20.334 -28.956 1 48.86  ? 124 LEU   A N   1 
ATOM   986  C  CA  . LEU   A 1 139 ? 2.853   -21.715 -28.529 1 48.07  ? 124 LEU   A CA  1 
ATOM   987  C  C   . LEU   A 1 139 ? 4.328   -22.083 -28.275 1 47.28  ? 124 LEU   A C   1 
ATOM   988  O  O   . LEU   A 1 139 ? 5.18    -21.838 -29.132 1 47.82  ? 124 LEU   A O   1 
ATOM   989  C  CB  . LEU   A 1 139 ? 2.252   -22.584 -29.626 1 48.39  ? 124 LEU   A CB  1 
ATOM   990  C  CG  . LEU   A 1 139 ? 1.856   -23.985 -29.235 1 49.74  ? 124 LEU   A CG  1 
ATOM   991  C  CD1 . LEU   A 1 139 ? 0.76    -23.964 -28.191 1 49.88  ? 124 LEU   A CD1 1 
ATOM   992  C  CD2 . LEU   A 1 139 ? 1.436   -24.778 -30.469 1 50.38  ? 124 LEU   A CD2 1 
ATOM   993  N  N   . VAL   A 1 140 ? 4.647   -22.538 -27.052 1 45.79  ? 125 VAL   A N   1 
ATOM   994  C  CA  . VAL   A 1 140 ? 6.024   -22.92  -26.694 1 44.61  ? 125 VAL   A CA  1 
ATOM   995  C  C   . VAL   A 1 140 ? 6.126   -24.443 -26.446 1 44.12  ? 125 VAL   A C   1 
ATOM   996  O  O   . VAL   A 1 140 ? 5.102   -25.136 -26.363 1 44.55  ? 125 VAL   A O   1 
ATOM   997  C  CB  . VAL   A 1 140 ? 6.601   -22.093 -25.506 1 44.07  ? 125 VAL   A CB  1 
ATOM   998  C  CG1 . VAL   A 1 140 ? 6.563   -20.599 -25.794 1 44.2   ? 125 VAL   A CG1 1 
ATOM   999  C  CG2 . VAL   A 1 140 ? 5.897   -22.425 -24.197 1 44.06  ? 125 VAL   A CG2 1 
ATOM   1000 N  N   . TYR   A 1 141 ? 7.361   -24.972 -26.343 1 42.62  ? 126 TYR   A N   1 
ATOM   1001 C  CA  . TYR   A 1 141 ? 7.658   -26.362 -26.045 1 41.21  ? 126 TYR   A CA  1 
ATOM   1002 C  C   . TYR   A 1 141 ? 6.928   -26.802 -24.762 1 40.64  ? 126 TYR   A C   1 
ATOM   1003 O  O   . TYR   A 1 141 ? 6.429   -27.912 -24.708 1 41.24  ? 126 TYR   A O   1 
ATOM   1004 C  CB  . TYR   A 1 141 ? 9.183   -26.481 -25.862 1 40.66  ? 126 TYR   A CB  1 
ATOM   1005 C  CG  . TYR   A 1 141 ? 9.702   -27.869 -25.567 1 40.56  ? 126 TYR   A CG  1 
ATOM   1006 C  CD1 . TYR   A 1 141 ? 9.987   -28.759 -26.596 1 41.19  ? 126 TYR   A CD1 1 
ATOM   1007 C  CD2 . TYR   A 1 141 ? 10.005  -28.254 -24.272 1 41.14  ? 126 TYR   A CD2 1 
ATOM   1008 C  CE1 . TYR   A 1 141 ? 10.504  -30.017 -26.336 1 41.93  ? 126 TYR   A CE1 1 
ATOM   1009 C  CE2 . TYR   A 1 141 ? 10.515  -29.511 -23.996 1 42.16  ? 126 TYR   A CE2 1 
ATOM   1010 C  CZ  . TYR   A 1 141 ? 10.763  -30.394 -25.031 1 43.18  ? 126 TYR   A CZ  1 
ATOM   1011 O  OH  . TYR   A 1 141 ? 11.269  -31.64  -24.757 1 44.46  ? 126 TYR   A OH  1 
ATOM   1012 N  N   . ALA   A 1 142 ? 6.816   -25.92  -23.764 1 40.32  ? 127 ALA   A N   1 
ATOM   1013 C  CA  . ALA   A 1 142 ? 6.117   -26.209 -22.5   1 40.98  ? 127 ALA   A CA  1 
ATOM   1014 C  C   . ALA   A 1 142 ? 4.605   -26.383 -22.67  1 41.8   ? 127 ALA   A C   1 
ATOM   1015 O  O   . ALA   A 1 142 ? 3.964   -27.045 -21.848 1 42.01  ? 127 ALA   A O   1 
ATOM   1016 C  CB  . ALA   A 1 142 ? 6.416   -25.142 -21.453 1 40.99  ? 127 ALA   A CB  1 
ATOM   1017 N  N   . ASP   A 1 143 ? 4.035   -25.834 -23.757 1 41.75  ? 128 ASP   A N   1 
ATOM   1018 C  CA  . ASP   A 1 143 ? 2.625   -26.01  -24.05  1 42.01  ? 128 ASP   A CA  1 
ATOM   1019 C  C   . ASP   A 1 143 ? 2.407   -27.301 -24.842 1 42.68  ? 128 ASP   A C   1 
ATOM   1020 O  O   . ASP   A 1 143 ? 1.772   -28.234 -24.336 1 41.98  ? 128 ASP   A O   1 
ATOM   1021 C  CB  . ASP   A 1 143 ? 2.035   -24.816 -24.843 1 43.21  ? 128 ASP   A CB  1 
ATOM   1022 C  CG  . ASP   A 1 143 ? 2.246   -23.455 -24.252 1 48.2   ? 128 ASP   A CG  1 
ATOM   1023 O  OD1 . ASP   A 1 143 ? 2.033   -23.301 -23.023 1 48.67  ? 128 ASP   A OD1 1 
ATOM   1024 O  OD2 . ASP   A 1 143 ? 2.606   -22.529 -25.019 1 50.63  ? 128 ASP   A OD2 1 
ATOM   1025 N  N   . CYS   A 1 144 ? 2.938   -27.37  -26.081 1 43.57  ? 129 CYS   A N   1 
ATOM   1026 C  CA  . CYS   A 1 144 ? 2.641   -28.508 -26.939 1 45.13  ? 129 CYS   A CA  1 
ATOM   1027 C  C   . CYS   A 1 144 ? 3.429   -29.774 -26.627 1 45.27  ? 129 CYS   A C   1 
ATOM   1028 O  O   . CYS   A 1 144 ? 3.08    -30.822 -27.182 1 45.49  ? 129 CYS   A O   1 
ATOM   1029 C  CB  . CYS   A 1 144 ? 2.763   -28.133 -28.407 1 46.46  ? 129 CYS   A CB  1 
ATOM   1030 S  SG  . CYS   A 1 144 ? 4.338   -27.386 -28.823 1 52.85  ? 129 CYS   A SG  1 
ATOM   1031 N  N   . VAL   A 1 145 ? 4.447   -29.71  -25.748 1 44.22  ? 130 VAL   A N   1 
ATOM   1032 C  CA  . VAL   A 1 145 ? 5.159   -30.924 -25.39  1 43.58  ? 130 VAL   A CA  1 
ATOM   1033 C  C   . VAL   A 1 145 ? 4.92    -31.25  -23.906 1 43.68  ? 130 VAL   A C   1 
ATOM   1034 O  O   . VAL   A 1 145 ? 4.297   -32.26  -23.599 1 43.72  ? 130 VAL   A O   1 
ATOM   1035 C  CB  . VAL   A 1 145 ? 6.656   -30.922 -25.81  1 43.22  ? 130 VAL   A CB  1 
ATOM   1036 C  CG1 . VAL   A 1 145 ? 7.396   -32.125 -25.234 1 43.16  ? 130 VAL   A CG1 1 
ATOM   1037 C  CG2 . VAL   A 1 145 ? 6.803   -30.862 -27.329 1 42.97  ? 130 VAL   A CG2 1 
ATOM   1038 N  N   . LEU   A 1 146 ? 5.322   -30.361 -23     1 43.55  ? 131 LEU   A N   1 
ATOM   1039 C  CA  . LEU   A 1 146 ? 5.225   -30.616 -21.557 1 43.57  ? 131 LEU   A CA  1 
ATOM   1040 C  C   . LEU   A 1 146 ? 3.795   -30.639 -20.985 1 44.61  ? 131 LEU   A C   1 
ATOM   1041 O  O   . LEU   A 1 146 ? 3.578   -31.299 -19.983 1 45.15  ? 131 LEU   A O   1 
ATOM   1042 C  CB  . LEU   A 1 146 ? 6.107   -29.627 -20.775 1 43.15  ? 131 LEU   A CB  1 
ATOM   1043 C  CG  . LEU   A 1 146 ? 7.565   -29.464 -21.288 1 43.51  ? 131 LEU   A CG  1 
ATOM   1044 C  CD1 . LEU   A 1 146 ? 8.314   -28.448 -20.487 1 44.02  ? 131 LEU   A CD1 1 
ATOM   1045 C  CD2 . LEU   A 1 146 ? 8.313   -30.763 -21.264 1 43.66  ? 131 LEU   A CD2 1 
ATOM   1046 N  N   . ALA   A 1 147 ? 2.824   -29.95  -21.597 1 44.94  ? 132 ALA   A N   1 
ATOM   1047 C  CA  . ALA   A 1 147 ? 1.433   -29.938 -21.097 1 45.21  ? 132 ALA   A CA  1 
ATOM   1048 C  C   . ALA   A 1 147 ? 0.425   -30.616 -22.041 1 45.75  ? 132 ALA   A C   1 
ATOM   1049 O  O   . ALA   A 1 147 ? -0.717  -30.818 -21.656 1 45.7   ? 132 ALA   A O   1 
ATOM   1050 C  CB  . ALA   A 1 147 ? 0.98    -28.515 -20.815 1 44.95  ? 132 ALA   A CB  1 
ATOM   1051 N  N   . ASN   A 1 148 ? 0.842   -30.976 -23.254 1 46.28  ? 133 ASN   A N   1 
ATOM   1052 C  CA  . ASN   A 1 148 ? -0.02   -31.572 -24.275 1 47.37  ? 133 ASN   A CA  1 
ATOM   1053 C  C   . ASN   A 1 148 ? -0.044  -33.1   -24.225 1 49.02  ? 133 ASN   A C   1 
ATOM   1054 O  O   . ASN   A 1 148 ? 0.18    -33.746 -25.239 1 49.28  ? 133 ASN   A O   1 
ATOM   1055 C  CB  . ASN   A 1 148 ? 0.438   -31.067 -25.651 1 47.73  ? 133 ASN   A CB  1 
ATOM   1056 C  CG  . ASN   A 1 148 ? -0.509  -31.277 -26.789 1 49.15  ? 133 ASN   A CG  1 
ATOM   1057 O  OD1 . ASN   A 1 148 ? -1.71   -31.476 -26.611 1 49.06  ? 133 ASN   A OD1 1 
ATOM   1058 N  ND2 . ASN   A 1 148 ? 0.025   -31.214 -27.995 1 49.6   ? 133 ASN   A ND2 1 
ATOM   1059 N  N   . TRP   A 1 149 ? -0.357  -33.681 -23.061 1 50.02  ? 134 TRP   A N   1 
ATOM   1060 C  CA  . TRP   A 1 149 ? -0.384  -35.128 -22.93  1 51.33  ? 134 TRP   A CA  1 
ATOM   1061 C  C   . TRP   A 1 149 ? -1.363  -35.631 -21.862 1 53.41  ? 134 TRP   A C   1 
ATOM   1062 O  O   . TRP   A 1 149 ? -1.83   -34.873 -21.022 1 53.16  ? 134 TRP   A O   1 
ATOM   1063 C  CB  . TRP   A 1 149 ? 1.042   -35.663 -22.69  1 51.07  ? 134 TRP   A CB  1 
ATOM   1064 C  CG  . TRP   A 1 149 ? 1.634   -35.271 -21.364 1 51.53  ? 134 TRP   A CG  1 
ATOM   1065 C  CD1 . TRP   A 1 149 ? 2.274   -34.106 -21.056 1 52.26  ? 134 TRP   A CD1 1 
ATOM   1066 C  CD2 . TRP   A 1 149 ? 1.647   -36.062 -20.172 1 51.7   ? 134 TRP   A CD2 1 
ATOM   1067 N  NE1 . TRP   A 1 149 ? 2.675   -34.121 -19.739 1 52.58  ? 134 TRP   A NE1 1 
ATOM   1068 C  CE2 . TRP   A 1 149 ? 2.322   -35.32  -19.181 1 52.47  ? 134 TRP   A CE2 1 
ATOM   1069 C  CE3 . TRP   A 1 149 ? 1.172   -37.336 -19.848 1 52.19  ? 134 TRP   A CE3 1 
ATOM   1070 C  CZ2 . TRP   A 1 149 ? 2.525   -35.812 -17.893 1 53.09  ? 134 TRP   A CZ2 1 
ATOM   1071 C  CZ3 . TRP   A 1 149 ? 1.343   -37.803 -18.562 1 52.97  ? 134 TRP   A CZ3 1 
ATOM   1072 C  CH2 . TRP   A 1 149 ? 2.018   -37.046 -17.603 1 53.13  ? 134 TRP   A CH2 1 
ATOM   1073 N  N   . LYS   A 1 150 ? -1.669  -36.926 -21.911 1 55.5   ? 135 LYS   A N   1 
ATOM   1074 C  CA  . LYS   A 1 150 ? -2.544  -37.587 -20.954 1 58.2   ? 135 LYS   A CA  1 
ATOM   1075 C  C   . LYS   A 1 150 ? -2.247  -39.09  -20.923 1 60.12  ? 135 LYS   A C   1 
ATOM   1076 O  O   . LYS   A 1 150 ? -1.766  -39.662 -21.903 1 60.37  ? 135 LYS   A O   1 
ATOM   1077 C  CB  . LYS   A 1 150 ? -4.024  -37.381 -21.34  1 61.09  ? 135 LYS   A CB  1 
ATOM   1078 C  CG  . LYS   A 1 150 ? -4.353  -37.852 -22.765 1 66.28  ? 135 LYS   A CG  1 
ATOM   1079 C  CD  . LYS   A 1 150 ? -5.845  -38.009 -23.008 1 71.9   ? 135 LYS   A CD  1 
ATOM   1080 C  CE  . LYS   A 1 150 ? -6.402  -39.257 -22.363 1 76.22  ? 135 LYS   A CE  1 
ATOM   1081 N  NZ  . LYS   A 1 150 ? -7.768  -39.572 -22.854 1 78.24  ? 135 LYS   A NZ  1 
ATOM   1082 N  N   . LYS   A 1 151 ? -2.544  -39.733 -19.796 1 61.33  ? 136 LYS   A N   1 
ATOM   1083 C  CA  . LYS   A 1 151 ? -2.43   -41.183 -19.675 1 62.73  ? 136 LYS   A CA  1 
ATOM   1084 C  C   . LYS   A 1 151 ? -3.809  -41.736 -20.069 1 64.19  ? 136 LYS   A C   1 
ATOM   1085 O  O   . LYS   A 1 151 ? -4.83   -41.251 -19.577 1 64.11  ? 136 LYS   A O   1 
ATOM   1086 C  CB  . LYS   A 1 151 ? -2.125  -41.583 -18.221 1 64.32  ? 136 LYS   A CB  1 
ATOM   1087 C  CG  . LYS   A 1 151 ? -0.709  -42.073 -17.982 1 68.13  ? 136 LYS   A CG  1 
ATOM   1088 C  CD  . LYS   A 1 151 ? -0.571  -42.574 -16.559 1 72.92  ? 136 LYS   A CD  1 
ATOM   1089 C  CE  . LYS   A 1 151 ? 0.832   -42.97  -16.191 1 77.26  ? 136 LYS   A CE  1 
ATOM   1090 N  NZ  . LYS   A 1 151 ? 0.851   -43.695 -14.887 1 79.45  ? 136 LYS   A NZ  1 
ATOM   1091 N  N   . LYS   A 1 152 ? -3.846  -42.721 -20.977 1 65.33  ? 137 LYS   A N   1 
ATOM   1092 C  CA  . LYS   A 1 152 ? -5.093  -43.36  -21.412 1 66.41  ? 137 LYS   A CA  1 
ATOM   1093 C  C   . LYS   A 1 152 ? -5.679  -44.094 -20.205 1 67.95  ? 137 LYS   A C   1 
ATOM   1094 O  O   . LYS   A 1 152 ? -6.83   -43.858 -19.85  1 68.81  ? 137 LYS   A O   1 
ATOM   1095 C  CB  . LYS   A 1 152 ? -4.833  -44.334 -22.583 1 67.41  ? 137 LYS   A CB  1 
ATOM   1096 C  CG  . LYS   A 1 152 ? -4.516  -43.656 -23.914 1 69.59  ? 137 LYS   A CG  1 
ATOM   1097 C  CD  . LYS   A 1 152 ? -3.944  -44.652 -24.893 1 72.61  ? 137 LYS   A CD  1 
ATOM   1098 C  CE  . LYS   A 1 152 ? -3.893  -44.119 -26.301 1 75.9   ? 137 LYS   A CE  1 
ATOM   1099 N  NZ  . LYS   A 1 152 ? -3.148  -45.039 -27.204 1 78.19  ? 137 LYS   A NZ  1 
ATOM   1100 N  N   . ASP   A 1 153 ? -4.844  -44.883 -19.511 1 68.32  ? 138 ASP   A N   1 
ATOM   1101 C  CA  . ASP   A 1 153 ? -5.201  -45.603 -18.294 1 69.28  ? 138 ASP   A CA  1 
ATOM   1102 C  C   . ASP   A 1 153 ? -4.269  -45.119 -17.191 1 69.69  ? 138 ASP   A C   1 
ATOM   1103 O  O   . ASP   A 1 153 ? -3.059  -45.348 -17.252 1 69.38  ? 138 ASP   A O   1 
ATOM   1104 C  CB  . ASP   A 1 153 ? -5.054  -47.13  -18.501 1 71.53  ? 138 ASP   A CB  1 
ATOM   1105 C  CG  . ASP   A 1 153 ? -5.291  -47.987 -17.262 1 76.02  ? 138 ASP   A CG  1 
ATOM   1106 O  OD1 . ASP   A 1 153 ? -5.912  -47.49  -16.304 1 76.78  ? 138 ASP   A OD1 1 
ATOM   1107 O  OD2 . ASP   A 1 153 ? -4.839  -49.147 -17.25  1 78.35  ? 138 ASP   A OD2 1 
ATOM   1108 N  N   . PRO   A 1 154 ? -4.825  -44.456 -16.163 1 70.29  ? 139 PRO   A N   1 
ATOM   1109 C  CA  . PRO   A 1 154 ? -3.976  -43.956 -15.063 1 70.76  ? 139 PRO   A CA  1 
ATOM   1110 C  C   . PRO   A 1 154 ? -3.235  -45.052 -14.285 1 71.81  ? 139 PRO   A C   1 
ATOM   1111 O  O   . PRO   A 1 154 ? -2.2    -44.794 -13.679 1 71.86  ? 139 PRO   A O   1 
ATOM   1112 C  CB  . PRO   A 1 154 ? -4.964  -43.19  -14.167 1 71.09  ? 139 PRO   A CB  1 
ATOM   1113 C  CG  . PRO   A 1 154 ? -6.18   -42.955 -15.003 1 71.26  ? 139 PRO   A CG  1 
ATOM   1114 C  CD  . PRO   A 1 154 ? -6.244  -44.105 -15.962 1 69.86  ? 139 PRO   A CD  1 
ATOM   1115 N  N   . ASN   A 1 155 ? -3.757  -46.279 -14.308 1 72.6   ? 140 ASN   A N   1 
ATOM   1116 C  CA  . ASN   A 1 155 ? -3.128  -47.406 -13.62  1 73.63  ? 140 ASN   A CA  1 
ATOM   1117 C  C   . ASN   A 1 155 ? -1.973  -48.04  -14.41  1 73.35  ? 140 ASN   A C   1 
ATOM   1118 O  O   . ASN   A 1 155 ? -1.183  -48.785 -13.839 1 73.69  ? 140 ASN   A O   1 
ATOM   1119 C  CB  . ASN   A 1 155 ? -4.184  -48.441 -13.221 1 75.69  ? 140 ASN   A CB  1 
ATOM   1120 C  CG  . ASN   A 1 155 ? -5.155  -47.891 -12.189 1 79.7   ? 140 ASN   A CG  1 
ATOM   1121 O  OD1 . ASN   A 1 155 ? -6.381  -47.984 -12.337 1 80.47  ? 140 ASN   A OD1 1 
ATOM   1122 N  ND2 . ASN   A 1 155 ? -4.615  -47.28  -11.126 1 80.74  ? 140 ASN   A ND2 1 
ATOM   1123 N  N   . LYS   A 1 156 ? -1.859  -47.741 -15.705 1 72.74  ? 141 LYS   A N   1 
ATOM   1124 C  CA  . LYS   A 1 156 ? -0.777  -48.262 -16.534 1 72.58  ? 141 LYS   A CA  1 
ATOM   1125 C  C   . LYS   A 1 156 ? 0.419   -47.258 -16.537 1 72.26  ? 141 LYS   A C   1 
ATOM   1126 O  O   . LYS   A 1 156 ? 0.235   -46.081 -16.195 1 72.68  ? 141 LYS   A O   1 
ATOM   1127 C  CB  . LYS   A 1 156 ? -1.307  -48.596 -17.939 1 74.13  ? 141 LYS   A CB  1 
ATOM   1128 N  N   . PRO   A 1 157 ? 1.652   -47.683 -16.875 1 71.26  ? 142 PRO   A N   1 
ATOM   1129 C  CA  . PRO   A 1 157 ? 2.798   -46.759 -16.779 1 70.37  ? 142 PRO   A CA  1 
ATOM   1130 C  C   . PRO   A 1 157 ? 2.927   -45.715 -17.899 1 69.23  ? 142 PRO   A C   1 
ATOM   1131 O  O   . PRO   A 1 157 ? 2.164   -45.713 -18.865 1 69.07  ? 142 PRO   A O   1 
ATOM   1132 C  CB  . PRO   A 1 157 ? 3.995   -47.714 -16.751 1 71.21  ? 142 PRO   A CB  1 
ATOM   1133 C  CG  . PRO   A 1 157 ? 3.557   -48.84  -17.609 1 72.02  ? 142 PRO   A CG  1 
ATOM   1134 C  CD  . PRO   A 1 157 ? 2.091   -49.035 -17.273 1 70.75  ? 142 PRO   A CD  1 
ATOM   1135 N  N   . LEU   A 1 158 ? 3.919   -44.815 -17.756 1 67.97  ? 143 LEU   A N   1 
ATOM   1136 C  CA  . LEU   A 1 158 ? 4.222   -43.785 -18.735 1 66.86  ? 143 LEU   A CA  1 
ATOM   1137 C  C   . LEU   A 1 158 ? 4.972   -44.363 -19.922 1 65.77  ? 143 LEU   A C   1 
ATOM   1138 O  O   . LEU   A 1 158 ? 6.184   -44.193 -20.053 1 65.82  ? 143 LEU   A O   1 
ATOM   1139 C  CB  . LEU   A 1 158 ? 5.036   -42.658 -18.099 1 66.97  ? 143 LEU   A CB  1 
ATOM   1140 C  CG  . LEU   A 1 158 ? 4.245   -41.634 -17.334 1 68.33  ? 143 LEU   A CG  1 
ATOM   1141 C  CD1 . LEU   A 1 158 ? 5.168   -40.704 -16.627 1 68.82  ? 143 LEU   A CD1 1 
ATOM   1142 C  CD2 . LEU   A 1 158 ? 3.304   -40.871 -18.254 1 68.96  ? 143 LEU   A CD2 1 
ATOM   1143 N  N   . THR   A 1 159 ? 4.242   -45.054 -20.791 1 64.7   ? 144 THR   A N   1 
ATOM   1144 C  CA  . THR   A 1 159 ? 4.778   -45.629 -22.024 1 63.97  ? 144 THR   A CA  1 
ATOM   1145 C  C   . THR   A 1 159 ? 3.998   -45.051 -23.213 1 62.48  ? 144 THR   A C   1 
ATOM   1146 O  O   . THR   A 1 159 ? 2.89    -44.564 -23.024 1 62.35  ? 144 THR   A O   1 
ATOM   1147 C  CB  . THR   A 1 159 ? 4.721   -47.161 -21.961 1 65.77  ? 144 THR   A CB  1 
ATOM   1148 O  OG1 . THR   A 1 159 ? 3.426   -47.584 -21.515 1 67.35  ? 144 THR   A OG1 1 
ATOM   1149 C  CG2 . THR   A 1 159 ? 5.78    -47.731 -21.069 1 65.91  ? 144 THR   A CG2 1 
ATOM   1150 N  N   . TYR   A 1 160 ? 4.553   -45.094 -24.432 1 61.59  ? 145 TYR   A N   1 
ATOM   1151 C  CA  . TYR   A 1 160 ? 3.875   -44.542 -25.618 1 61.21  ? 145 TYR   A CA  1 
ATOM   1152 C  C   . TYR   A 1 160 ? 2.475   -45.129 -25.81  1 62.13  ? 145 TYR   A C   1 
ATOM   1153 O  O   . TYR   A 1 160 ? 1.525   -44.398 -26.094 1 62.59  ? 145 TYR   A O   1 
ATOM   1154 C  CB  . TYR   A 1 160 ? 4.719   -44.752 -26.895 1 60.33  ? 145 TYR   A CB  1 
ATOM   1155 C  CG  . TYR   A 1 160 ? 4.218   -43.966 -28.087 1 60.2   ? 145 TYR   A CG  1 
ATOM   1156 C  CD1 . TYR   A 1 160 ? 4.716   -42.701 -28.37  1 60.69  ? 145 TYR   A CD1 1 
ATOM   1157 C  CD2 . TYR   A 1 160 ? 3.217   -44.47  -28.909 1 60.54  ? 145 TYR   A CD2 1 
ATOM   1158 C  CE1 . TYR   A 1 160 ? 4.226   -41.953 -29.434 1 61.19  ? 145 TYR   A CE1 1 
ATOM   1159 C  CE2 . TYR   A 1 160 ? 2.702   -43.721 -29.961 1 61.07  ? 145 TYR   A CE2 1 
ATOM   1160 C  CZ  . TYR   A 1 160 ? 3.228   -42.473 -30.24  1 61.74  ? 145 TYR   A CZ  1 
ATOM   1161 O  OH  . TYR   A 1 160 ? 2.758   -41.747 -31.309 1 62.28  ? 145 TYR   A OH  1 
ATOM   1162 N  N   . GLU   A 1 161 ? 2.34    -46.443 -25.598 1 62.31  ? 146 GLU   A N   1 
ATOM   1163 C  CA  . GLU   A 1 161 ? 1.072   -47.158 -25.763 1 62.59  ? 146 GLU   A CA  1 
ATOM   1164 C  C   . GLU   A 1 161 ? -0.012  -46.706 -24.806 1 62.43  ? 146 GLU   A C   1 
ATOM   1165 O  O   . GLU   A 1 161 ? -1.188  -46.752 -25.152 1 62.66  ? 146 GLU   A O   1 
ATOM   1166 C  CB  . GLU   A 1 161 ? 1.301   -48.667 -25.677 1 65.45  ? 146 GLU   A CB  1 
ATOM   1167 C  CG  . GLU   A 1 161 ? 1.883   -49.243 -26.958 1 71.32  ? 146 GLU   A CG  1 
ATOM   1168 C  CD  . GLU   A 1 161 ? 3.113   -48.554 -27.527 1 77.96  ? 146 GLU   A CD  1 
ATOM   1169 O  OE1 . GLU   A 1 161 ? 4.124   -48.444 -26.794 1 79.65  ? 146 GLU   A OE1 1 
ATOM   1170 O  OE2 . GLU   A 1 161 ? 3.054   -48.105 -28.697 1 79.17  ? 146 GLU   A OE2 1 
ATOM   1171 N  N   . ASN   A 1 162 ? 0.37    -46.214 -23.631 1 61.94  ? 147 ASN   A N   1 
ATOM   1172 C  CA  . ASN   A 1 162 ? -0.591  -45.731 -22.647 1 61.84  ? 147 ASN   A CA  1 
ATOM   1173 C  C   . ASN   A 1 162 ? -0.736  -44.195 -22.643 1 61.71  ? 147 ASN   A C   1 
ATOM   1174 O  O   . ASN   A 1 162 ? -1.286  -43.641 -21.684 1 61.82  ? 147 ASN   A O   1 
ATOM   1175 C  CB  . ASN   A 1 162 ? -0.192  -46.232 -21.26  1 62.57  ? 147 ASN   A CB  1 
ATOM   1176 C  CG  . ASN   A 1 162 ? -1.194  -45.909 -20.195 1 64.98  ? 147 ASN   A CG  1 
ATOM   1177 O  OD1 . ASN   A 1 162 ? -2.4    -46.1   -20.37  1 66.57  ? 147 ASN   A OD1 1 
ATOM   1178 N  ND2 . ASN   A 1 162 ? -0.721  -45.369 -19.089 1 64.89  ? 147 ASN   A ND2 1 
ATOM   1179 N  N   . MET   A 1 163 ? -0.238  -43.498 -23.686 1 61.05  ? 148 MET   A N   1 
ATOM   1180 C  CA  . MET   A 1 163 ? -0.322  -42.036 -23.707 1 60.94  ? 148 MET   A CA  1 
ATOM   1181 C  C   . MET   A 1 163 ? -0.889  -41.483 -25.002 1 60.88  ? 148 MET   A C   1 
ATOM   1182 O  O   . MET   A 1 163 ? -0.856  -42.146 -26.04  1 61.37  ? 148 MET   A O   1 
ATOM   1183 C  CB  . MET   A 1 163 ? 1.053   -41.395 -23.417 1 61.24  ? 148 MET   A CB  1 
ATOM   1184 C  CG  . MET   A 1 163 ? 1.624   -41.738 -22.066 1 63.07  ? 148 MET   A CG  1 
ATOM   1185 S  SD  . MET   A 1 163 ? 3.412   -41.433 -22.011 1 65.62  ? 148 MET   A SD  1 
ATOM   1186 C  CE  . MET   A 1 163 ? 3.408   -39.715 -21.779 1 63.5   ? 148 MET   A CE  1 
ATOM   1187 N  N   . ASP   A 1 164 ? -1.369  -40.236 -24.944 1 60.06  ? 149 ASP   A N   1 
ATOM   1188 C  CA  . ASP   A 1 164 ? -1.905  -39.511 -26.09  1 59.86  ? 149 ASP   A CA  1 
ATOM   1189 C  C   . ASP   A 1 164 ? -1.715  -38.004 -25.906 1 58.68  ? 149 ASP   A C   1 
ATOM   1190 O  O   . ASP   A 1 164 ? -1.548  -37.539 -24.781 1 58.5   ? 149 ASP   A O   1 
ATOM   1191 C  CB  . ASP   A 1 164 ? -3.404  -39.808 -26.251 1 62.52  ? 149 ASP   A CB  1 
ATOM   1192 C  CG  . ASP   A 1 164 ? -3.822  -39.99  -27.692 1 69.91  ? 149 ASP   A CG  1 
ATOM   1193 O  OD1 . ASP   A 1 164 ? -3.713  -39.013 -28.472 1 70.67  ? 149 ASP   A OD1 1 
ATOM   1194 O  OD2 . ASP   A 1 164 ? -4.245  -41.117 -28.051 1 74.09  ? 149 ASP   A OD2 1 
ATOM   1195 N  N   . VAL   A 1 165 ? -1.763  -37.235 -27.007 1 57.56  ? 150 VAL   A N   1 
ATOM   1196 C  CA  . VAL   A 1 165 ? -1.7    -35.782 -26.915 1 57.13  ? 150 VAL   A CA  1 
ATOM   1197 C  C   . VAL   A 1 165 ? -3.125  -35.214 -26.764 1 56.92  ? 150 VAL   A C   1 
ATOM   1198 O  O   . VAL   A 1 165 ? -4.096  -35.879 -27.127 1 58.12  ? 150 VAL   A O   1 
ATOM   1199 C  CB  . VAL   A 1 165 ? -0.944  -35.105 -28.094 1 57.35  ? 150 VAL   A CB  1 
ATOM   1200 C  CG1 . VAL   A 1 165 ? 0.494   -35.59  -28.18  1 57.66  ? 150 VAL   A CG1 1 
ATOM   1201 C  CG2 . VAL   A 1 165 ? -1.681  -35.297 -29.42  1 57.41  ? 150 VAL   A CG2 1 
ATOM   1202 N  N   . LEU   A 1 166 ? -3.257  -33.995 -26.239 1 55.41  ? 151 LEU   A N   1 
ATOM   1203 C  CA  . LEU   A 1 166 ? -4.559  -33.365 -26.115 1 54.44  ? 151 LEU   A CA  1 
ATOM   1204 C  C   . LEU   A 1 166 ? -4.987  -32.7   -27.444 1 54.21  ? 151 LEU   A C   1 
ATOM   1205 O  O   . LEU   A 1 166 ? -6.166  -32.739 -27.794 1 54.05  ? 151 LEU   A O   1 
ATOM   1206 C  CB  . LEU   A 1 166 ? -4.56   -32.347 -24.969 1 54.18  ? 151 LEU   A CB  1 
ATOM   1207 C  CG  . LEU   A 1 166 ? -4.104  -32.864 -23.61  1 55.13  ? 151 LEU   A CG  1 
ATOM   1208 C  CD1 . LEU   A 1 166 ? -4.158  -31.77  -22.569 1 55.08  ? 151 LEU   A CD1 1 
ATOM   1209 C  CD2 . LEU   A 1 166 ? -4.921  -34.072 -23.155 1 55.79  ? 151 LEU   A CD2 1 
ATOM   1210 N  N   . PHE   A 1 167 ? -4.043  -32.095 -28.183 1 54.25  ? 152 PHE   A N   1 
ATOM   1211 C  CA  . PHE   A 1 167 ? -4.383  -31.399 -29.426 1 54.81  ? 152 PHE   A CA  1 
ATOM   1212 C  C   . PHE   A 1 167 ? -3.457  -31.682 -30.593 1 54.57  ? 152 PHE   A C   1 
ATOM   1213 O  O   . PHE   A 1 167 ? -2.255  -31.85  -30.42  1 54.22  ? 152 PHE   A O   1 
ATOM   1214 C  CB  . PHE   A 1 167 ? -4.468  -29.878 -29.195 1 55.34  ? 152 PHE   A CB  1 
ATOM   1215 C  CG  . PHE   A 1 167 ? -5.329  -29.481 -28.016 1 56.82  ? 152 PHE   A CG  1 
ATOM   1216 C  CD1 . PHE   A 1 167 ? -6.711  -29.527 -28.099 1 57.84  ? 152 PHE   A CD1 1 
ATOM   1217 C  CD2 . PHE   A 1 167 ? -4.757  -29.151 -26.797 1 57.71  ? 152 PHE   A CD2 1 
ATOM   1218 C  CE1 . PHE   A 1 167 ? -7.504  -29.222 -26.994 1 58.63  ? 152 PHE   A CE1 1 
ATOM   1219 C  CE2 . PHE   A 1 167 ? -5.549  -28.845 -25.695 1 58.4   ? 152 PHE   A CE2 1 
ATOM   1220 C  CZ  . PHE   A 1 167 ? -6.919  -28.889 -25.799 1 58.28  ? 152 PHE   A CZ  1 
ATOM   1221 N  N   . SER   A 1 168 ? -4.032  -31.684 -31.795 1 54.85  ? 153 SER   A N   1 
ATOM   1222 C  CA  . SER   A 1 168 ? -3.345  -31.843 -33.081 1 55.61  ? 153 SER   A CA  1 
ATOM   1223 C  C   . SER   A 1 168 ? -3.721  -30.687 -34.018 1 55.86  ? 153 SER   A C   1 
ATOM   1224 O  O   . SER   A 1 168 ? -4.686  -29.976 -33.744 1 56.25  ? 153 SER   A O   1 
ATOM   1225 C  CB  . SER   A 1 168 ? -3.717  -33.175 -33.719 1 57.19  ? 153 SER   A CB  1 
ATOM   1226 O  OG  . SER   A 1 168 ? -3.201  -34.212 -32.906 1 60.52  ? 153 SER   A OG  1 
ATOM   1227 N  N   . PHE   A 1 169 ? -2.968  -30.478 -35.105 1 55.64  ? 154 PHE   A N   1 
ATOM   1228 C  CA  . PHE   A 1 169 ? -3.279  -29.387 -36.032 1 55.94  ? 154 PHE   A CA  1 
ATOM   1229 C  C   . PHE   A 1 169 ? -4.075  -29.852 -37.235 1 56.8   ? 154 PHE   A C   1 
ATOM   1230 O  O   . PHE   A 1 169 ? -5.102  -29.272 -37.556 1 57.15  ? 154 PHE   A O   1 
ATOM   1231 C  CB  . PHE   A 1 169 ? -2.018  -28.643 -36.455 1 55.53  ? 154 PHE   A CB  1 
ATOM   1232 C  CG  . PHE   A 1 169 ? -1.458  -27.804 -35.342 1 55.93  ? 154 PHE   A CG  1 
ATOM   1233 C  CD1 . PHE   A 1 169 ? -2.084  -26.635 -34.953 1 56.56  ? 154 PHE   A CD1 1 
ATOM   1234 C  CD2 . PHE   A 1 169 ? -0.298  -28.18  -34.684 1 56.24  ? 154 PHE   A CD2 1 
ATOM   1235 C  CE1 . PHE   A 1 169 ? -1.565  -25.863 -33.924 1 56.93  ? 154 PHE   A CE1 1 
ATOM   1236 C  CE2 . PHE   A 1 169 ? 0.223   -27.394 -33.666 1 56.59  ? 154 PHE   A CE2 1 
ATOM   1237 C  CZ  . PHE   A 1 169 ? -0.419  -26.251 -33.286 1 56.43  ? 154 PHE   A CZ  1 
ATOM   1238 N  N   . ARG   A 1 170 ? -3.592  -30.887 -37.912 1 57.12  ? 155 ARG   A N   1 
ATOM   1239 C  CA  . ARG   A 1 170 ? -4.213  -31.466 -39.095 1 57.52  ? 155 ARG   A CA  1 
ATOM   1240 C  C   . ARG   A 1 170 ? -4.239  -32.986 -38.99  1 58.75  ? 155 ARG   A C   1 
ATOM   1241 O  O   . ARG   A 1 170 ? -3.498  -33.562 -38.204 1 58.41  ? 155 ARG   A O   1 
ATOM   1242 C  CB  . ARG   A 1 170 ? -3.421  -31.061 -40.358 1 57.24  ? 155 ARG   A CB  1 
ATOM   1243 C  CG  . ARG   A 1 170 ? -3.324  -29.562 -40.573 1 57.56  ? 155 ARG   A CG  1 
ATOM   1244 C  CD  . ARG   A 1 170 ? -4.665  -28.923 -40.848 1 59.31  ? 155 ARG   A CD  1 
ATOM   1245 N  NE  . ARG   A 1 170 ? -5.258  -29.434 -42.081 1 61.99  ? 155 ARG   A NE  1 
ATOM   1246 C  CZ  . ARG   A 1 170 ? -5.018  -28.942 -43.294 1 63.39  ? 155 ARG   A CZ  1 
ATOM   1247 N  NH1 . ARG   A 1 170 ? -4.203  -27.901 -43.449 1 61.09  ? 155 ARG   A NH1 1 
ATOM   1248 N  NH2 . ARG   A 1 170 ? -5.591  -29.484 -44.361 1 64.48  ? 155 ARG   A NH2 1 
ATOM   1249 N  N   . ASP   A 1 171 ? -5.095  -33.645 -39.791 1 60.28  ? 156 ASP   A N   1 
ATOM   1250 C  CA  . ASP   A 1 171 ? -5.13   -35.102 -39.825 1 61.76  ? 156 ASP   A CA  1 
ATOM   1251 C  C   . ASP   A 1 171 ? -3.855  -35.56  -40.535 1 60.93  ? 156 ASP   A C   1 
ATOM   1252 O  O   . ASP   A 1 171 ? -3.454  -34.97  -41.553 1 60.37  ? 156 ASP   A O   1 
ATOM   1253 C  CB  . ASP   A 1 171 ? -6.379  -35.611 -40.561 1 66.3   ? 156 ASP   A CB  1 
ATOM   1254 C  CG  . ASP   A 1 171 ? -7.669  -35.107 -39.942 1 76.48  ? 156 ASP   A CG  1 
ATOM   1255 O  OD1 . ASP   A 1 171 ? -7.882  -35.358 -38.716 1 78.07  ? 156 ASP   A OD1 1 
ATOM   1256 O  OD2 . ASP   A 1 171 ? -8.477  -34.456 -40.68  1 80.37  ? 156 ASP   A OD2 1 
ATOM   1257 N  N   . GLY   A 1 172 ? -3.186  -36.54  -39.932 1 60.17  ? 157 GLY   A N   1 
ATOM   1258 C  CA  . GLY   A 1 172 ? -1.951  -37.084 -40.466 1 59.95  ? 157 GLY   A CA  1 
ATOM   1259 C  C   . GLY   A 1 172 ? -0.739  -36.197 -40.283 1 59.5   ? 157 GLY   A C   1 
ATOM   1260 O  O   . GLY   A 1 172 ? 0.277   -36.416 -40.935 1 59.7   ? 157 GLY   A O   1 
ATOM   1261 N  N   . ASP   A 1 173 ? -0.808  -35.205 -39.38  1 58.52  ? 158 ASP   A N   1 
ATOM   1262 C  CA  . ASP   A 1 173 ? 0.331   -34.309 -39.132 1 57.66  ? 158 ASP   A CA  1 
ATOM   1263 C  C   . ASP   A 1 173 ? 1.45    -34.933 -38.297 1 57.25  ? 158 ASP   A C   1 
ATOM   1264 O  O   . ASP   A 1 173 ? 2.491   -34.309 -38.152 1 57.75  ? 158 ASP   A O   1 
ATOM   1265 C  CB  . ASP   A 1 173 ? -0.123  -32.995 -38.472 1 58     ? 158 ASP   A CB  1 
ATOM   1266 C  CG  . ASP   A 1 173 ? -0.767  -33.149 -37.101 1 59.38  ? 158 ASP   A CG  1 
ATOM   1267 O  OD1 . ASP   A 1 173 ? -0.925  -34.3   -36.64  1 59.39  ? 158 ASP   A OD1 1 
ATOM   1268 O  OD2 . ASP   A 1 173 ? -1.146  -32.125 -36.507 1 59.94  ? 158 ASP   A OD2 1 
ATOM   1269 N  N   . CYS   A 1 174 ? 1.223   -36.122 -37.72  1 56.46  ? 159 CYS   A N   1 
ATOM   1270 C  CA  . CYS   A 1 174 ? 2.162   -36.838 -36.862 1 56.42  ? 159 CYS   A CA  1 
ATOM   1271 C  C   . CYS   A 1 174 ? 2.478   -36.101 -35.55  1 55.69  ? 159 CYS   A C   1 
ATOM   1272 O  O   . CYS   A 1 174 ? 3.484   -36.394 -34.912 1 56.01  ? 159 CYS   A O   1 
ATOM   1273 C  CB  . CYS   A 1 174 ? 3.427   -37.209 -37.623 1 57.81  ? 159 CYS   A CB  1 
ATOM   1274 S  SG  . CYS   A 1 174 ? 3.157   -38.412 -38.95  1 62.69  ? 159 CYS   A SG  1 
ATOM   1275 N  N   . SER   A 1 175 ? 1.588   -35.183 -35.132 1 54.23  ? 160 SER   A N   1 
ATOM   1276 C  CA  . SER   A 1 175 ? 1.714   -34.38  -33.929 1 52.58  ? 160 SER   A CA  1 
ATOM   1277 C  C   . SER   A 1 175 ? 1.817   -35.273 -32.715 1 51.57  ? 160 SER   A C   1 
ATOM   1278 O  O   . SER   A 1 175 ? 2.641   -35.003 -31.859 1 52.09  ? 160 SER   A O   1 
ATOM   1279 C  CB  . SER   A 1 175 ? 0.522   -33.437 -33.785 1 52.46  ? 160 SER   A CB  1 
ATOM   1280 N  N   . LYS   A 1 176 ? 1.043   -36.37  -32.654 1 50     ? 161 LYS   A N   1 
ATOM   1281 C  CA  . LYS   A 1 176 ? 1.102   -37.277 -31.508 1 48.95  ? 161 LYS   A CA  1 
ATOM   1282 C  C   . LYS   A 1 176 ? 2.497   -37.886 -31.36  1 49.01  ? 161 LYS   A C   1 
ATOM   1283 O  O   . LYS   A 1 176 ? 3.085   -37.847 -30.281 1 49.2   ? 161 LYS   A O   1 
ATOM   1284 C  CB  . LYS   A 1 176 ? 0.029   -38.373 -31.61  1 49.5   ? 161 LYS   A CB  1 
ATOM   1285 C  CG  . LYS   A 1 176 ? 0.024   -39.311 -30.404 1 51.64  ? 161 LYS   A CG  1 
ATOM   1286 C  CD  . LYS   A 1 176 ? -1.011  -40.397 -30.531 1 54.22  ? 161 LYS   A CD  1 
ATOM   1287 C  CE  . LYS   A 1 176 ? -0.759  -41.534 -29.58  1 57.09  ? 161 LYS   A CE  1 
ATOM   1288 N  NZ  . LYS   A 1 176 ? -1.594  -42.716 -29.907 1 58.71  ? 161 LYS   A NZ  1 
ATOM   1289 N  N   . GLY   A 1 177 ? 3.044   -38.36  -32.469 1 48.57  ? 162 GLY   A N   1 
ATOM   1290 C  CA  . GLY   A 1 177 ? 4.361   -38.965 -32.482 1 48.37  ? 162 GLY   A CA  1 
ATOM   1291 C  C   . GLY   A 1 177 ? 5.472   -37.989 -32.187 1 48.39  ? 162 GLY   A C   1 
ATOM   1292 O  O   . GLY   A 1 177 ? 6.335   -38.279 -31.373 1 48.72  ? 162 GLY   A O   1 
ATOM   1293 N  N   . PHE   A 1 178 ? 5.453   -36.815 -32.826 1 47.96  ? 163 PHE   A N   1 
ATOM   1294 C  CA  . PHE   A 1 178 ? 6.482   -35.808 -32.622 1 47.62  ? 163 PHE   A CA  1 
ATOM   1295 C  C   . PHE   A 1 178 ? 6.496   -35.306 -31.179 1 47.63  ? 163 PHE   A C   1 
ATOM   1296 O  O   . PHE   A 1 178 ? 7.565   -35.202 -30.58  1 48.19  ? 163 PHE   A O   1 
ATOM   1297 C  CB  . PHE   A 1 178 ? 6.27    -34.628 -33.587 1 47.21  ? 163 PHE   A CB  1 
ATOM   1298 C  CG  . PHE   A 1 178 ? 7.427   -33.656 -33.617 1 47.17  ? 163 PHE   A CG  1 
ATOM   1299 C  CD1 . PHE   A 1 178 ? 8.728   -34.107 -33.733 1 47.15  ? 163 PHE   A CD1 1 
ATOM   1300 C  CD2 . PHE   A 1 178 ? 7.209   -32.293 -33.531 1 47.42  ? 163 PHE   A CD2 1 
ATOM   1301 C  CE1 . PHE   A 1 178 ? 9.787   -33.21  -33.772 1 47.66  ? 163 PHE   A CE1 1 
ATOM   1302 C  CE2 . PHE   A 1 178 ? 8.271   -31.401 -33.575 1 47.77  ? 163 PHE   A CE2 1 
ATOM   1303 C  CZ  . PHE   A 1 178 ? 9.552   -31.861 -33.693 1 47.34  ? 163 PHE   A CZ  1 
ATOM   1304 N  N   . PHE   A 1 179 ? 5.319   -34.99  -30.628 1 46.61  ? 164 PHE   A N   1 
ATOM   1305 C  CA  . PHE   A 1 179 ? 5.234   -34.459 -29.28  1 46.26  ? 164 PHE   A CA  1 
ATOM   1306 C  C   . PHE   A 1 179 ? 5.481   -35.512 -28.197 1 47.25  ? 164 PHE   A C   1 
ATOM   1307 O  O   . PHE   A 1 179 ? 6.211   -35.226 -27.245 1 47.01  ? 164 PHE   A O   1 
ATOM   1308 C  CB  . PHE   A 1 179 ? 3.907   -33.716 -29.049 1 45.12  ? 164 PHE   A CB  1 
ATOM   1309 C  CG  . PHE   A 1 179 ? 3.642   -32.544 -29.964 1 45.24  ? 164 PHE   A CG  1 
ATOM   1310 C  CD1 . PHE   A 1 179 ? 4.686   -31.843 -30.544 1 45.73  ? 164 PHE   A CD1 1 
ATOM   1311 C  CD2 . PHE   A 1 179 ? 2.346   -32.143 -30.247 1 46.03  ? 164 PHE   A CD2 1 
ATOM   1312 C  CE1 . PHE   A 1 179 ? 4.436   -30.782 -31.413 1 46.15  ? 164 PHE   A CE1 1 
ATOM   1313 C  CE2 . PHE   A 1 179 ? 2.1     -31.065 -31.096 1 46.34  ? 164 PHE   A CE2 1 
ATOM   1314 C  CZ  . PHE   A 1 179 ? 3.145   -30.395 -31.674 1 45.99  ? 164 PHE   A CZ  1 
ATOM   1315 N  N   . LEU   A 1 180 ? 4.882   -36.72  -28.322 1 47.87  ? 165 LEU   A N   1 
ATOM   1316 C  CA  . LEU   A 1 180 ? 5.06    -37.739 -27.281 1 48.75  ? 165 LEU   A CA  1 
ATOM   1317 C  C   . LEU   A 1 180 ? 6.46    -38.289 -27.249 1 47.93  ? 165 LEU   A C   1 
ATOM   1318 O  O   . LEU   A 1 180 ? 6.939   -38.613 -26.17  1 47.39  ? 165 LEU   A O   1 
ATOM   1319 C  CB  . LEU   A 1 180 ? 4.054   -38.898 -27.373 1 50.11  ? 165 LEU   A CB  1 
ATOM   1320 C  CG  . LEU   A 1 180 ? 2.581   -38.583 -27.167 1 53.1   ? 165 LEU   A CG  1 
ATOM   1321 C  CD1 . LEU   A 1 180 ? 1.758   -39.866 -27.218 1 54.43  ? 165 LEU   A CD1 1 
ATOM   1322 C  CD2 . LEU   A 1 180 ? 2.327   -37.837 -25.855 1 54     ? 165 LEU   A CD2 1 
ATOM   1323 N  N   . VAL   A 1 181 ? 7.114   -38.413 -28.412 1 47.69  ? 166 VAL   A N   1 
ATOM   1324 C  CA  . VAL   A 1 181 ? 8.481   -38.922 -28.44  1 48.2   ? 166 VAL   A CA  1 
ATOM   1325 C  C   . VAL   A 1 181 ? 9.426   -37.889 -27.804 1 48.16  ? 166 VAL   A C   1 
ATOM   1326 O  O   . VAL   A 1 181 ? 10.293  -38.283 -27.026 1 48.91  ? 166 VAL   A O   1 
ATOM   1327 C  CB  . VAL   A 1 181 ? 8.932   -39.445 -29.826 1 49.33  ? 166 VAL   A CB  1 
ATOM   1328 C  CG1 . VAL   A 1 181 ? 10.432  -39.719 -29.857 1 50.35  ? 166 VAL   A CG1 1 
ATOM   1329 C  CG2 . VAL   A 1 181 ? 8.151   -40.704 -30.196 1 49.97  ? 166 VAL   A CG2 1 
ATOM   1330 N  N   . SER   A 1 182 ? 9.18    -36.569 -28.015 1 47.03  ? 167 SER   A N   1 
ATOM   1331 C  CA  . SER   A 1 182 ? 9.971   -35.519 -27.351 1 46.31  ? 167 SER   A CA  1 
ATOM   1332 C  C   . SER   A 1 182 ? 9.752   -35.62  -25.837 1 45.39  ? 167 SER   A C   1 
ATOM   1333 O  O   . SER   A 1 182 ? 10.709  -35.615 -25.078 1 46.01  ? 167 SER   A O   1 
ATOM   1334 C  CB  . SER   A 1 182 ? 9.57    -34.13  -27.841 1 47.01  ? 167 SER   A CB  1 
ATOM   1335 O  OG  . SER   A 1 182 ? 10.022  -33.872 -29.162 1 49.46  ? 167 SER   A OG  1 
ATOM   1336 N  N   . LEU   A 1 183 ? 8.504   -35.774 -25.418 1 44.11  ? 168 LEU   A N   1 
ATOM   1337 C  CA  . LEU   A 1 183 ? 8.115   -35.902 -24.026 1 43.88  ? 168 LEU   A CA  1 
ATOM   1338 C  C   . LEU   A 1 183 ? 8.733   -37.118 -23.354 1 44.92  ? 168 LEU   A C   1 
ATOM   1339 O  O   . LEU   A 1 183 ? 9.203   -37.012 -22.23  1 44.93  ? 168 LEU   A O   1 
ATOM   1340 C  CB  . LEU   A 1 183 ? 6.585   -35.985 -23.93  1 43.15  ? 168 LEU   A CB  1 
ATOM   1341 C  CG  . LEU   A 1 183 ? 6.037   -36.077 -22.533 1 44.04  ? 168 LEU   A CG  1 
ATOM   1342 C  CD1 . LEU   A 1 183 ? 6.282   -34.78  -21.74  1 44.29  ? 168 LEU   A CD1 1 
ATOM   1343 C  CD2 . LEU   A 1 183 ? 4.601   -36.427 -22.558 1 44.74  ? 168 LEU   A CD2 1 
ATOM   1344 N  N   . LEU   A 1 184 ? 8.737   -38.275 -24.02  1 45.72  ? 169 LEU   A N   1 
ATOM   1345 C  CA  . LEU   A 1 184 ? 9.3     -39.494 -23.448 1 46.19  ? 169 LEU   A CA  1 
ATOM   1346 C  C   . LEU   A 1 184 ? 10.819  -39.378 -23.282 1 46.86  ? 169 LEU   A C   1 
ATOM   1347 O  O   . LEU   A 1 184 ? 11.349  -39.876 -22.298 1 47.34  ? 169 LEU   A O   1 
ATOM   1348 C  CB  . LEU   A 1 184 ? 8.866   -40.733 -24.247 1 46.2   ? 169 LEU   A CB  1 
ATOM   1349 C  CG  . LEU   A 1 184 ? 7.38    -41.096 -24.063 1 46.7   ? 169 LEU   A CG  1 
ATOM   1350 C  CD1 . LEU   A 1 184 ? 6.888   -42.036 -25.145 1 46.65  ? 169 LEU   A CD1 1 
ATOM   1351 C  CD2 . LEU   A 1 184 ? 7.11    -41.621 -22.67  1 47.19  ? 169 LEU   A CD2 1 
ATOM   1352 N  N   . VAL   A 1 185 ? 11.505  -38.662 -24.192 1 46.7   ? 170 VAL   A N   1 
ATOM   1353 C  CA  . VAL   A 1 185 ? 12.938  -38.39  -24.088 1 47.27  ? 170 VAL   A CA  1 
ATOM   1354 C  C   . VAL   A 1 185 ? 13.192  -37.413 -22.924 1 48.83  ? 170 VAL   A C   1 
ATOM   1355 O  O   . VAL   A 1 185 ? 14.157  -37.581 -22.176 1 49.46  ? 170 VAL   A O   1 
ATOM   1356 C  CB  . VAL   A 1 185 ? 13.495  -37.85  -25.426 1 47.65  ? 170 VAL   A CB  1 
ATOM   1357 C  CG1 . VAL   A 1 185 ? 14.889  -37.259 -25.249 1 47.6   ? 170 VAL   A CG1 1 
ATOM   1358 C  CG2 . VAL   A 1 185 ? 13.5    -38.945 -26.498 1 48.07  ? 170 VAL   A CG2 1 
ATOM   1359 N  N   . GLU   A 1 186 ? 12.308  -36.414 -22.75  1 49.12  ? 171 GLU   A N   1 
ATOM   1360 C  CA  . GLU   A 1 186 ? 12.363  -35.451 -21.655 1 49.56  ? 171 GLU   A CA  1 
ATOM   1361 C  C   . GLU   A 1 186 ? 12.269  -36.159 -20.319 1 50.45  ? 171 GLU   A C   1 
ATOM   1362 O  O   . GLU   A 1 186 ? 13.011  -35.815 -19.401 1 51.3   ? 171 GLU   A O   1 
ATOM   1363 C  CB  . GLU   A 1 186 ? 11.191  -34.475 -21.735 1 50.68  ? 171 GLU   A CB  1 
ATOM   1364 C  CG  . GLU   A 1 186 ? 11.565  -33.148 -22.321 1 55.18  ? 171 GLU   A CG  1 
ATOM   1365 C  CD  . GLU   A 1 186 ? 11.965  -32.076 -21.334 1 60.56  ? 171 GLU   A CD  1 
ATOM   1366 O  OE1 . GLU   A 1 186 ? 12.453  -31.028 -21.804 1 63.36  ? 171 GLU   A OE1 1 
ATOM   1367 O  OE2 . GLU   A 1 186 ? 11.81   -32.268 -20.107 1 62.33  ? 171 GLU   A OE2 1 
ATOM   1368 N  N   . ILE   A 1 187 ? 11.33   -37.109 -20.191 1 49.88  ? 172 ILE   A N   1 
ATOM   1369 C  CA  . ILE   A 1 187 ? 11.118  -37.841 -18.948 1 49.58  ? 172 ILE   A CA  1 
ATOM   1370 C  C   . ILE   A 1 187 ? 12.268  -38.814 -18.697 1 50.06  ? 172 ILE   A C   1 
ATOM   1371 O  O   . ILE   A 1 187 ? 12.673  -38.995 -17.545 1 50.86  ? 172 ILE   A O   1 
ATOM   1372 C  CB  . ILE   A 1 187 ? 9.734   -38.526 -18.95  1 48.87  ? 172 ILE   A CB  1 
ATOM   1373 C  CG1 . ILE   A 1 187 ? 8.623   -37.489 -19.045 1 49.07  ? 172 ILE   A CG1 1 
ATOM   1374 C  CG2 . ILE   A 1 187 ? 9.544   -39.385 -17.735 1 48.85  ? 172 ILE   A CG2 1 
ATOM   1375 C  CD1 . ILE   A 1 187 ? 7.292   -38.1   -19.451 1 50.2   ? 172 ILE   A CD1 1 
ATOM   1376 N  N   . ALA   A 1 188 ? 12.841  -39.395 -19.77  1 49.17  ? 173 ALA   A N   1 
ATOM   1377 C  CA  . ALA   A 1 188 ? 13.964  -40.307 -19.654 1 48.67  ? 173 ALA   A CA  1 
ATOM   1378 C  C   . ALA   A 1 188 ? 15.166  -39.558 -19.104 1 49.77  ? 173 ALA   A C   1 
ATOM   1379 O  O   . ALA   A 1 188 ? 15.805  -40.045 -18.178 1 50.32  ? 173 ALA   A O   1 
ATOM   1380 C  CB  . ALA   A 1 188 ? 14.274  -40.924 -21.009 1 48.18  ? 173 ALA   A CB  1 
ATOM   1381 N  N   . ALA   A 1 189 ? 15.431  -38.342 -19.615 1 50.21  ? 174 ALA   A N   1 
ATOM   1382 C  CA  . ALA   A 1 189 ? 16.535  -37.497 -19.16  1 51     ? 174 ALA   A CA  1 
ATOM   1383 C  C   . ALA   A 1 189 ? 16.308  -36.946 -17.736 1 51.86  ? 174 ALA   A C   1 
ATOM   1384 O  O   . ALA   A 1 189 ? 17.264  -36.742 -16.993 1 52.26  ? 174 ALA   A O   1 
ATOM   1385 C  CB  . ALA   A 1 189 ? 16.739  -36.352 -20.138 1 50.89  ? 174 ALA   A CB  1 
ATOM   1386 N  N   . ALA   A 1 190 ? 15.048  -36.726 -17.364 1 52.08  ? 175 ALA   A N   1 
ATOM   1387 C  CA  . ALA   A 1 190 ? 14.631  -36.205 -16.065 1 53.04  ? 175 ALA   A CA  1 
ATOM   1388 C  C   . ALA   A 1 190 ? 15.02   -37.091 -14.9   1 53.99  ? 175 ALA   A C   1 
ATOM   1389 O  O   . ALA   A 1 190 ? 15.128  -36.601 -13.776 1 54.53  ? 175 ALA   A O   1 
ATOM   1390 C  CB  . ALA   A 1 190 ? 13.126  -35.994 -16.05  1 53.31  ? 175 ALA   A CB  1 
ATOM   1391 N  N   . SER   A 1 191 ? 15.192  -38.39  -15.137 1 54.14  ? 176 SER   A N   1 
ATOM   1392 C  CA  . SER   A 1 191 ? 15.609  -39.307 -14.083 1 54.83  ? 176 SER   A CA  1 
ATOM   1393 C  C   . SER   A 1 191 ? 16.998  -38.931 -13.529 1 54.73  ? 176 SER   A C   1 
ATOM   1394 O  O   . SER   A 1 191 ? 17.289  -39.253 -12.389 1 55.97  ? 176 SER   A O   1 
ATOM   1395 C  CB  . SER   A 1 191 ? 15.571  -40.75  -14.573 1 57.1   ? 176 SER   A CB  1 
ATOM   1396 O  OG  . SER   A 1 191 ? 16.107  -40.875 -15.88  1 61.38  ? 176 SER   A OG  1 
ATOM   1397 N  N   . ALA   A 1 192 ? 17.822  -38.199 -14.291 1 53.19  ? 177 ALA   A N   1 
ATOM   1398 C  CA  . ALA   A 1 192 ? 19.121  -37.753 -13.831 1 52.46  ? 177 ALA   A CA  1 
ATOM   1399 C  C   . ALA   A 1 192 ? 19.066  -36.456 -12.993 1 52.5   ? 177 ALA   A C   1 
ATOM   1400 O  O   . ALA   A 1 192 ? 20.046  -36.136 -12.322 1 52.75  ? 177 ALA   A O   1 
ATOM   1401 C  CB  . ALA   A 1 192 ? 20.039  -37.565 -15.02  1 52.12  ? 177 ALA   A CB  1 
ATOM   1402 N  N   . ILE   A 1 193 ? 17.95   -35.703 -13.042 1 51.97  ? 178 ILE   A N   1 
ATOM   1403 C  CA  . ILE   A 1 193 ? 17.8    -34.444 -12.315 1 52.28  ? 178 ILE   A CA  1 
ATOM   1404 C  C   . ILE   A 1 193 ? 17.949  -34.637 -10.819 1 53.09  ? 178 ILE   A C   1 
ATOM   1405 O  O   . ILE   A 1 193 ? 18.625  -33.846 -10.173 1 53.47  ? 178 ILE   A O   1 
ATOM   1406 C  CB  . ILE   A 1 193 ? 16.486  -33.702 -12.684 1 52.84  ? 178 ILE   A CB  1 
ATOM   1407 C  CG1 . ILE   A 1 193 ? 16.47   -33.295 -14.162 1 53.52  ? 178 ILE   A CG1 1 
ATOM   1408 C  CG2 . ILE   A 1 193 ? 16.277  -32.475 -11.808 1 53.43  ? 178 ILE   A CG2 1 
ATOM   1409 C  CD1 . ILE   A 1 193 ? 15.125  -32.817 -14.617 1 54.52  ? 178 ILE   A CD1 1 
ATOM   1410 N  N   . LYS   A 1 194 ? 17.361  -35.711 -10.265 1 53.2   ? 179 LYS   A N   1 
ATOM   1411 C  CA  . LYS   A 1 194 ? 17.466  -36.003 -8.835  1 53.37  ? 179 LYS   A CA  1 
ATOM   1412 C  C   . LYS   A 1 194 ? 18.909  -36.282 -8.375  1 53.9   ? 179 LYS   A C   1 
ATOM   1413 O  O   . LYS   A 1 194 ? 19.186  -36.252 -7.174  1 54.64  ? 179 LYS   A O   1 
ATOM   1414 C  CB  . LYS   A 1 194 ? 16.573  -37.188 -8.462  1 54.9   ? 179 LYS   A CB  1 
ATOM   1415 C  CG  . LYS   A 1 194 ? 16.909  -38.475 -9.191  1 58.22  ? 179 LYS   A CG  1 
ATOM   1416 C  CD  . LYS   A 1 194 ? 16.025  -39.601 -8.703  1 62.12  ? 179 LYS   A CD  1 
ATOM   1417 C  CE  . LYS   A 1 194 ? 15.925  -40.733 -9.693  1 66.41  ? 179 LYS   A CE  1 
ATOM   1418 N  NZ  . LYS   A 1 194 ? 14.828  -40.498 -10.672 1 69.77  ? 179 LYS   A NZ  1 
ATOM   1419 N  N   . VAL   A 1 195 ? 19.818  -36.588 -9.318  1 52.67  ? 180 VAL   A N   1 
ATOM   1420 C  CA  . VAL   A 1 195 ? 21.214  -36.847 -9.005  1 51.8   ? 180 VAL   A CA  1 
ATOM   1421 C  C   . VAL   A 1 195 ? 22.026  -35.546 -8.843  1 51.6   ? 180 VAL   A C   1 
ATOM   1422 O  O   . VAL   A 1 195 ? 23.1    -35.579 -8.239  1 51.81  ? 180 VAL   A O   1 
ATOM   1423 C  CB  . VAL   A 1 195 ? 21.82   -37.799 -10.058 1 51.46  ? 180 VAL   A CB  1 
ATOM   1424 C  CG1 . VAL   A 1 195 ? 23.276  -38.084 -9.757  1 51.76  ? 180 VAL   A CG1 1 
ATOM   1425 C  CG2 . VAL   A 1 195 ? 21.021  -39.092 -10.137 1 51.01  ? 180 VAL   A CG2 1 
ATOM   1426 N  N   . ILE   A 1 196 ? 21.509  -34.405 -9.366  1 50.95  ? 181 ILE   A N   1 
ATOM   1427 C  CA  . ILE   A 1 196 ? 22.147  -33.088 -9.287  1 50.72  ? 181 ILE   A CA  1 
ATOM   1428 C  C   . ILE   A 1 196 ? 22.478  -32.679 -7.824  1 51.09  ? 181 ILE   A C   1 
ATOM   1429 O  O   . ILE   A 1 196 ? 23.648  -32.406 -7.549  1 50.96  ? 181 ILE   A O   1 
ATOM   1430 C  CB  . ILE   A 1 196 ? 21.33   -32.017 -10.054 1 50.63  ? 181 ILE   A CB  1 
ATOM   1431 C  CG1 . ILE   A 1 196 ? 21.359  -32.298 -11.566 1 51.3   ? 181 ILE   A CG1 1 
ATOM   1432 C  CG2 . ILE   A 1 196 ? 21.813  -30.595 -9.737  1 50.63  ? 181 ILE   A CG2 1 
ATOM   1433 C  CD1 . ILE   A 1 196 ? 20.423  -31.41  -12.379 1 52.5   ? 181 ILE   A CD1 1 
ATOM   1434 N  N   . PRO   A 1 197 ? 21.531  -32.721 -6.856  1 51.19  ? 182 PRO   A N   1 
ATOM   1435 C  CA  . PRO   A 1 197 ? 21.903  -32.391 -5.468  1 51.34  ? 182 PRO   A CA  1 
ATOM   1436 C  C   . PRO   A 1 197 ? 23.061  -33.248 -4.915  1 51.59  ? 182 PRO   A C   1 
ATOM   1437 O  O   . PRO   A 1 197 ? 23.902  -32.753 -4.152  1 51.77  ? 182 PRO   A O   1 
ATOM   1438 C  CB  . PRO   A 1 197 ? 20.607  -32.603 -4.678  1 51.83  ? 182 PRO   A CB  1 
ATOM   1439 C  CG  . PRO   A 1 197 ? 19.656  -33.267 -5.589  1 52.13  ? 182 PRO   A CG  1 
ATOM   1440 C  CD  . PRO   A 1 197 ? 20.089  -33.011 -6.981  1 50.6   ? 182 PRO   A CD  1 
ATOM   1441 N  N   . THR   A 1 198 ? 23.125  -34.527 -5.319  1 51.02  ? 183 THR   A N   1 
ATOM   1442 C  CA  . THR   A 1 198 ? 24.19   -35.437 -4.891  1 50.54  ? 183 THR   A CA  1 
ATOM   1443 C  C   . THR   A 1 198 ? 25.532  -34.966 -5.425  1 50.81  ? 183 THR   A C   1 
ATOM   1444 O  O   . THR   A 1 198 ? 26.523  -35.046 -4.731  1 51.45  ? 183 THR   A O   1 
ATOM   1445 C  CB  . THR   A 1 198 ? 23.893  -36.866 -5.37   1 51.25  ? 183 THR   A CB  1 
ATOM   1446 O  OG1 . THR   A 1 198 ? 22.576  -37.245 -4.978  1 52.71  ? 183 THR   A OG1 1 
ATOM   1447 C  CG2 . THR   A 1 198 ? 24.873  -37.868 -4.836  1 51.1   ? 183 THR   A CG2 1 
ATOM   1448 N  N   . VAL   A 1 199 ? 25.567  -34.484 -6.658  1 50.53  ? 184 VAL   A N   1 
ATOM   1449 C  CA  . VAL   A 1 199 ? 26.776  -33.987 -7.298  1 50.39  ? 184 VAL   A CA  1 
ATOM   1450 C  C   . VAL   A 1 199 ? 27.313  -32.761 -6.573  1 50.85  ? 184 VAL   A C   1 
ATOM   1451 O  O   . VAL   A 1 199 ? 28.507  -32.701 -6.303  1 51.47  ? 184 VAL   A O   1 
ATOM   1452 C  CB  . VAL   A 1 199 ? 26.505  -33.715 -8.799  1 50.09  ? 184 VAL   A CB  1 
ATOM   1453 C  CG1 . VAL   A 1 199 ? 27.622  -32.909 -9.438  1 49.98  ? 184 VAL   A CG1 1 
ATOM   1454 C  CG2 . VAL   A 1 199 ? 26.278  -35.033 -9.546  1 50.28  ? 184 VAL   A CG2 1 
ATOM   1455 N  N   . PHE   A 1 200 ? 26.445  -31.805 -6.231  1 50.68  ? 185 PHE   A N   1 
ATOM   1456 C  CA  . PHE   A 1 200 ? 26.883  -30.59  -5.551  1 51.07  ? 185 PHE   A CA  1 
ATOM   1457 C  C   . PHE   A 1 200 ? 27.3    -30.848 -4.121  1 51.19  ? 185 PHE   A C   1 
ATOM   1458 O  O   . PHE   A 1 200 ? 28.282  -30.263 -3.667  1 51.68  ? 185 PHE   A O   1 
ATOM   1459 C  CB  . PHE   A 1 200 ? 25.835  -29.464 -5.653  1 51.09  ? 185 PHE   A CB  1 
ATOM   1460 C  CG  . PHE   A 1 200 ? 25.795  -28.874 -7.046  1 51.89  ? 185 PHE   A CG  1 
ATOM   1461 C  CD1 . PHE   A 1 200 ? 26.96   -28.447 -7.669  1 52.81  ? 185 PHE   A CD1 1 
ATOM   1462 C  CD2 . PHE   A 1 200 ? 24.609  -28.817 -7.759  1 52.57  ? 185 PHE   A CD2 1 
ATOM   1463 C  CE1 . PHE   A 1 200 ? 26.937  -27.961 -8.97   1 53.8   ? 185 PHE   A CE1 1 
ATOM   1464 C  CE2 . PHE   A 1 200 ? 24.583  -28.311 -9.054  1 53.83  ? 185 PHE   A CE2 1 
ATOM   1465 C  CZ  . PHE   A 1 200 ? 25.746  -27.882 -9.652  1 53.88  ? 185 PHE   A CZ  1 
ATOM   1466 N  N   . LYS   A 1 201 ? 26.588  -31.741 -3.423  1 50.74  ? 186 LYS   A N   1 
ATOM   1467 C  CA  . LYS   A 1 201 ? 26.929  -32.076 -2.052  1 51.11  ? 186 LYS   A CA  1 
ATOM   1468 C  C   . LYS   A 1 201 ? 28.224  -32.85  -2.014  1 52     ? 186 LYS   A C   1 
ATOM   1469 O  O   . LYS   A 1 201 ? 29.046  -32.568 -1.154  1 52.23  ? 186 LYS   A O   1 
ATOM   1470 C  CB  . LYS   A 1 201 ? 25.801  -32.843 -1.354  1 52.53  ? 186 LYS   A CB  1 
ATOM   1471 N  N   . ALA   A 1 202 ? 28.45   -33.771 -2.974  1 52.36  ? 187 ALA   A N   1 
ATOM   1472 C  CA  . ALA   A 1 202 ? 29.689  -34.552 -3.035  1 53.19  ? 187 ALA   A CA  1 
ATOM   1473 C  C   . ALA   A 1 202 ? 30.9    -33.682 -3.323  1 54.23  ? 187 ALA   A C   1 
ATOM   1474 O  O   . ALA   A 1 202 ? 31.968  -33.957 -2.792  1 54.2   ? 187 ALA   A O   1 
ATOM   1475 C  CB  . ALA   A 1 202 ? 29.588  -35.658 -4.07   1 53.12  ? 187 ALA   A CB  1 
ATOM   1476 N  N   . MET   A 1 203 ? 30.748  -32.63  -4.14   1 55.07  ? 188 MET   A N   1 
ATOM   1477 C  CA  . MET   A 1 203 ? 31.86   -31.724 -4.411  1 56.32  ? 188 MET   A CA  1 
ATOM   1478 C  C   . MET   A 1 203 ? 32.182  -30.902 -3.152  1 58.08  ? 188 MET   A C   1 
ATOM   1479 O  O   . MET   A 1 203 ? 33.354  -30.779 -2.782  1 58.51  ? 188 MET   A O   1 
ATOM   1480 C  CB  . MET   A 1 203 ? 31.524  -30.783 -5.56   1 56.29  ? 188 MET   A CB  1 
ATOM   1481 C  CG  . MET   A 1 203 ? 31.619  -31.414 -6.916  1 56.49  ? 188 MET   A CG  1 
ATOM   1482 S  SD  . MET   A 1 203 ? 30.881  -30.338 -8.161  1 53.96  ? 188 MET   A SD  1 
ATOM   1483 C  CE  . MET   A 1 203 ? 31.878  -28.935 -8.015  1 51.83  ? 188 MET   A CE  1 
ATOM   1484 N  N   . GLN   A 1 204 ? 31.144  -30.379 -2.478  1 58.99  ? 189 GLN   A N   1 
ATOM   1485 C  CA  . GLN   A 1 204 ? 31.288  -29.585 -1.254  1 60.53  ? 189 GLN   A CA  1 
ATOM   1486 C  C   . GLN   A 1 204 ? 31.986  -30.417 -0.172  1 61.05  ? 189 GLN   A C   1 
ATOM   1487 O  O   . GLN   A 1 204 ? 33.014  -30.012 0.357   1 60.91  ? 189 GLN   A O   1 
ATOM   1488 C  CB  . GLN   A 1 204 ? 29.899  -29.091 -0.784  1 63.18  ? 189 GLN   A CB  1 
ATOM   1489 C  CG  . GLN   A 1 204 ? 29.817  -28.61  0.659   1 69.42  ? 189 GLN   A CG  1 
ATOM   1490 C  CD  . GLN   A 1 204 ? 30.442  -27.248 0.816   1 78.4   ? 189 GLN   A CD  1 
ATOM   1491 O  OE1 . GLN   A 1 204 ? 30.327  -26.377 -0.062  1 81.31  ? 189 GLN   A OE1 1 
ATOM   1492 N  NE2 . GLN   A 1 204 ? 31.118  -27.024 1.942   1 80.3   ? 189 GLN   A NE2 1 
ATOM   1493 N  N   . MET   A 1 205 ? 31.454  -31.607 0.098   1 61.48  ? 190 MET   A N   1 
ATOM   1494 C  CA  . MET   A 1 205 ? 31.982  -32.51  1.102   1 62.22  ? 190 MET   A CA  1 
ATOM   1495 C  C   . MET   A 1 205 ? 33.243  -33.238 0.696   1 62.12  ? 190 MET   A C   1 
ATOM   1496 O  O   . MET   A 1 205 ? 33.766  -33.989 1.516   1 62.84  ? 190 MET   A O   1 
ATOM   1497 C  CB  . MET   A 1 205 ? 30.933  -33.553 1.453   1 63.84  ? 190 MET   A CB  1 
ATOM   1498 C  CG  . MET   A 1 205 ? 29.743  -33.012 2.163   1 68.69  ? 190 MET   A CG  1 
ATOM   1499 S  SD  . MET   A 1 205 ? 28.878  -34.455 2.84    1 85.3   ? 190 MET   A SD  1 
ATOM   1500 C  CE  . MET   A 1 205 ? 30.086  -35.006 4.119   1 84.84  ? 190 MET   A CE  1 
ATOM   1501 N  N   . GLN   A 1 206 ? 33.692  -33.093 -0.559  1 61.34  ? 191 GLN   A N   1 
ATOM   1502 C  CA  . GLN   A 1 206 ? 34.871  -33.764 -1.078  1 61.07  ? 191 GLN   A CA  1 
ATOM   1503 C  C   . GLN   A 1 206 ? 34.707  -35.273 -1.002  1 60.29  ? 191 GLN   A C   1 
ATOM   1504 O  O   . GLN   A 1 206 ? 35.602  -35.967 -0.551  1 60.93  ? 191 GLN   A O   1 
ATOM   1505 C  CB  . GLN   A 1 206 ? 36.145  -33.287 -0.363  1 63.14  ? 191 GLN   A CB  1 
ATOM   1506 C  CG  . GLN   A 1 206 ? 36.59   -31.877 -0.749  1 67.54  ? 191 GLN   A CG  1 
ATOM   1507 C  CD  . GLN   A 1 206 ? 37.409  -31.851 -2.018  1 73.9   ? 191 GLN   A CD  1 
ATOM   1508 O  OE1 . GLN   A 1 206 ? 37.973  -32.863 -2.463  1 76.02  ? 191 GLN   A OE1 1 
ATOM   1509 N  NE2 . GLN   A 1 206 ? 37.501  -30.683 -2.634  1 75.79  ? 191 GLN   A NE2 1 
ATOM   1510 N  N   . GLU   A 1 207 ? 33.545  -35.781 -1.413  1 58.97  ? 192 GLU   A N   1 
ATOM   1511 C  CA  . GLU   A 1 207 ? 33.248  -37.205 -1.432  1 58.25  ? 192 GLU   A CA  1 
ATOM   1512 C  C   . GLU   A 1 207 ? 33.49   -37.711 -2.839  1 57.35  ? 192 GLU   A C   1 
ATOM   1513 O  O   . GLU   A 1 207 ? 32.577  -37.751 -3.659  1 57.39  ? 192 GLU   A O   1 
ATOM   1514 C  CB  . GLU   A 1 207 ? 31.799  -37.454 -1.026  1 60.38  ? 192 GLU   A CB  1 
ATOM   1515 C  CG  . GLU   A 1 207 ? 31.49   -37.035 0.393   1 66.28  ? 192 GLU   A CG  1 
ATOM   1516 C  CD  . GLU   A 1 207 ? 32.004  -37.979 1.459   1 76.49  ? 192 GLU   A CD  1 
ATOM   1517 O  OE1 . GLU   A 1 207 ? 32.327  -39.145 1.13    1 78.36  ? 192 GLU   A OE1 1 
ATOM   1518 O  OE2 . GLU   A 1 207 ? 32.067  -37.555 2.636   1 80.26  ? 192 GLU   A OE2 1 
ATOM   1519 N  N   . ARG   A 1 208 ? 34.738  -38.069 -3.122  1 56.32  ? 193 ARG   A N   1 
ATOM   1520 C  CA  . ARG   A 1 208 ? 35.178  -38.521 -4.437  1 55.3   ? 193 ARG   A CA  1 
ATOM   1521 C  C   . ARG   A 1 208 ? 34.389  -39.725 -4.991  1 55.18  ? 193 ARG   A C   1 
ATOM   1522 O  O   . ARG   A 1 208 ? 34.018  -39.713 -6.169  1 55.66  ? 193 ARG   A O   1 
ATOM   1523 C  CB  . ARG   A 1 208 ? 36.695  -38.801 -4.405  1 54.24  ? 193 ARG   A CB  1 
ATOM   1524 C  CG  . ARG   A 1 208 ? 37.305  -39.203 -5.735  1 53.17  ? 193 ARG   A CG  1 
ATOM   1525 C  CD  . ARG   A 1 208 ? 37.353  -40.705 -5.848  1 53.17  ? 193 ARG   A CD  1 
ATOM   1526 N  NE  . ARG   A 1 208 ? 38.01   -41.152 -7.069  1 53.44  ? 193 ARG   A NE  1 
ATOM   1527 C  CZ  . ARG   A 1 208 ? 37.969  -42.397 -7.53   1 53.65  ? 193 ARG   A CZ  1 
ATOM   1528 N  NH1 . ARG   A 1 208 ? 37.254  -43.32  -6.901  1 52.5   ? 193 ARG   A NH1 1 
ATOM   1529 N  NH2 . ARG   A 1 208 ? 38.599  -42.717 -8.652  1 53.23  ? 193 ARG   A NH2 1 
ATOM   1530 N  N   . ASP   A 1 209 ? 34.173  -40.765 -4.174  1 54.21  ? 194 ASP   A N   1 
ATOM   1531 C  CA  . ASP   A 1 209 ? 33.496  -41.967 -4.661  1 53.89  ? 194 ASP   A CA  1 
ATOM   1532 C  C   . ASP   A 1 209 ? 32.039  -41.707 -4.96   1 53.86  ? 194 ASP   A C   1 
ATOM   1533 O  O   . ASP   A 1 209 ? 31.513  -42.245 -5.936  1 53.95  ? 194 ASP   A O   1 
ATOM   1534 C  CB  . ASP   A 1 209 ? 33.639  -43.14  -3.678  1 54.81  ? 194 ASP   A CB  1 
ATOM   1535 C  CG  . ASP   A 1 209 ? 35.062  -43.605 -3.426  1 57.08  ? 194 ASP   A CG  1 
ATOM   1536 O  OD1 . ASP   A 1 209 ? 35.898  -43.499 -4.349  1 56.94  ? 194 ASP   A OD1 1 
ATOM   1537 O  OD2 . ASP   A 1 209 ? 35.332  -44.09  -2.311  1 58.75  ? 194 ASP   A OD2 1 
ATOM   1538 N  N   . THR   A 1 210 ? 31.386  -40.888 -4.114  1 53.4   ? 195 THR   A N   1 
ATOM   1539 C  CA  . THR   A 1 210 ? 29.995  -40.5   -4.269  1 53.29  ? 195 THR   A CA  1 
ATOM   1540 C  C   . THR   A 1 210 ? 29.829  -39.732 -5.587  1 53.26  ? 195 THR   A C   1 
ATOM   1541 O  O   . THR   A 1 210 ? 28.923  -40.03  -6.349  1 53.9   ? 195 THR   A O   1 
ATOM   1542 C  CB  . THR   A 1 210 ? 29.577  -39.633 -3.076  1 54.27  ? 195 THR   A CB  1 
ATOM   1543 O  OG1 . THR   A 1 210 ? 29.691  -40.397 -1.88   1 54.72  ? 195 THR   A OG1 1 
ATOM   1544 C  CG2 . THR   A 1 210 ? 28.169  -39.083 -3.224  1 54.41  ? 195 THR   A CG2 1 
ATOM   1545 N  N   . LEU   A 1 211 ? 30.721  -38.779 -5.868  1 52.5   ? 196 LEU   A N   1 
ATOM   1546 C  CA  . LEU   A 1 211 ? 30.667  -38     -7.098  1 52.27  ? 196 LEU   A CA  1 
ATOM   1547 C  C   . LEU   A 1 211 ? 30.853  -38.898 -8.325  1 53.02  ? 196 LEU   A C   1 
ATOM   1548 O  O   . LEU   A 1 211 ? 30.221  -38.659 -9.358  1 54.04  ? 196 LEU   A O   1 
ATOM   1549 C  CB  . LEU   A 1 211 ? 31.718  -36.881 -7.071  1 51.41  ? 196 LEU   A CB  1 
ATOM   1550 C  CG  . LEU   A 1 211 ? 31.711  -35.919 -8.247  1 51.22  ? 196 LEU   A CG  1 
ATOM   1551 C  CD1 . LEU   A 1 211 ? 30.387  -35.188 -8.361  1 51.46  ? 196 LEU   A CD1 1 
ATOM   1552 C  CD2 . LEU   A 1 211 ? 32.827  -34.94  -8.133  1 51.26  ? 196 LEU   A CD2 1 
ATOM   1553 N  N   . LEU   A 1 212 ? 31.673  -39.949 -8.209  1 52.22  ? 197 LEU   A N   1 
ATOM   1554 C  CA  . LEU   A 1 212 ? 31.881  -40.879 -9.314  1 52.21  ? 197 LEU   A CA  1 
ATOM   1555 C  C   . LEU   A 1 212 ? 30.607  -41.684 -9.609  1 52.15  ? 197 LEU   A C   1 
ATOM   1556 O  O   . LEU   A 1 212 ? 30.21   -41.805 -10.769 1 52.6   ? 197 LEU   A O   1 
ATOM   1557 C  CB  . LEU   A 1 212 ? 33.056  -41.815 -9.008  1 52.05  ? 197 LEU   A CB  1 
ATOM   1558 C  CG  . LEU   A 1 212 ? 33.903  -42.177 -10.209 1 52.74  ? 197 LEU   A CG  1 
ATOM   1559 C  CD1 . LEU   A 1 212 ? 35.3    -42.458 -9.805  1 53.08  ? 197 LEU   A CD1 1 
ATOM   1560 C  CD2 . LEU   A 1 212 ? 33.348  -43.352 -10.919 1 53.08  ? 197 LEU   A CD2 1 
ATOM   1561 N  N   . LYS   A 1 213 ? 29.963  -42.219 -8.564  1 51.53  ? 198 LYS   A N   1 
ATOM   1562 C  CA  . LYS   A 1 213 ? 28.729  -42.977 -8.713  1 51.66  ? 198 LYS   A CA  1 
ATOM   1563 C  C   . LYS   A 1 213 ? 27.634  -42.078 -9.274  1 51.79  ? 198 LYS   A C   1 
ATOM   1564 O  O   . LYS   A 1 213 ? 26.892  -42.506 -10.155 1 52.01  ? 198 LYS   A O   1 
ATOM   1565 C  CB  . LYS   A 1 213 ? 28.287  -43.577 -7.365  1 53.29  ? 198 LYS   A CB  1 
ATOM   1566 N  N   . ALA   A 1 214 ? 27.56   -40.822 -8.781  1 51.49  ? 199 ALA   A N   1 
ATOM   1567 C  CA  . ALA   A 1 214 ? 26.591  -39.817 -9.215  1 51.52  ? 199 ALA   A CA  1 
ATOM   1568 C  C   . ALA   A 1 214 ? 26.783  -39.458 -10.68  1 51.58  ? 199 ALA   A C   1 
ATOM   1569 O  O   . ALA   A 1 214 ? 25.791  -39.405 -11.407 1 52.01  ? 199 ALA   A O   1 
ATOM   1570 C  CB  . ALA   A 1 214 ? 26.686  -38.566 -8.351  1 51.43  ? 199 ALA   A CB  1 
ATOM   1571 N  N   . LEU   A 1 215 ? 28.041  -39.235 -11.132 1 50.62  ? 200 LEU   A N   1 
ATOM   1572 C  CA  . LEU   A 1 215 ? 28.27   -38.905 -12.535 1 50.46  ? 200 LEU   A CA  1 
ATOM   1573 C  C   . LEU   A 1 215 ? 27.928  -40.107 -13.422 1 51.57  ? 200 LEU   A C   1 
ATOM   1574 O  O   . LEU   A 1 215 ? 27.33   -39.932 -14.481 1 52.34  ? 200 LEU   A O   1 
ATOM   1575 C  CB  . LEU   A 1 215 ? 29.696  -38.42  -12.789 1 49.83  ? 200 LEU   A CB  1 
ATOM   1576 C  CG  . LEU   A 1 215 ? 30.045  -37.034 -12.264 1 49.84  ? 200 LEU   A CG  1 
ATOM   1577 C  CD1 . LEU   A 1 215 ? 31.524  -36.769 -12.352 1 49.64  ? 200 LEU   A CD1 1 
ATOM   1578 C  CD2 . LEU   A 1 215 ? 29.271  -35.963 -12.995 1 50     ? 200 LEU   A CD2 1 
ATOM   1579 N  N   . LEU   A 1 216 ? 28.25   -41.321 -12.972 1 51.42  ? 201 LEU   A N   1 
ATOM   1580 C  CA  . LEU   A 1 216 ? 27.939  -42.529 -13.729 1 52.09  ? 201 LEU   A CA  1 
ATOM   1581 C  C   . LEU   A 1 216 ? 26.432  -42.779 -13.802 1 52.58  ? 201 LEU   A C   1 
ATOM   1582 O  O   . LEU   A 1 216 ? 25.953  -43.31  -14.808 1 52.68  ? 201 LEU   A O   1 
ATOM   1583 C  CB  . LEU   A 1 216 ? 28.645  -43.758 -13.14  1 52.16  ? 201 LEU   A CB  1 
ATOM   1584 C  CG  . LEU   A 1 216 ? 30.14   -43.85  -13.39  1 52.71  ? 201 LEU   A CG  1 
ATOM   1585 C  CD1 . LEU   A 1 216 ? 30.712  -45.051 -12.703 1 53.13  ? 201 LEU   A CD1 1 
ATOM   1586 C  CD2 . LEU   A 1 216 ? 30.441  -43.919 -14.865 1 52.68  ? 201 LEU   A CD2 1 
ATOM   1587 N  N   . GLU   A 1 217 ? 25.684  -42.39  -12.75  1 52.22  ? 202 GLU   A N   1 
ATOM   1588 C  CA  . GLU   A 1 217 ? 24.24   -42.536 -12.725 1 52.05  ? 202 GLU   A CA  1 
ATOM   1589 C  C   . GLU   A 1 217 ? 23.589  -41.553 -13.706 1 52.27  ? 202 GLU   A C   1 
ATOM   1590 O  O   . GLU   A 1 217 ? 22.65   -41.92  -14.407 1 52.62  ? 202 GLU   A O   1 
ATOM   1591 C  CB  . GLU   A 1 217 ? 23.706  -42.375 -11.304 1 53.82  ? 202 GLU   A CB  1 
ATOM   1592 C  CG  . GLU   A 1 217 ? 22.208  -42.57  -11.153 1 59.24  ? 202 GLU   A CG  1 
ATOM   1593 C  CD  . GLU   A 1 217 ? 21.639  -43.823 -11.784 1 70.56  ? 202 GLU   A CD  1 
ATOM   1594 O  OE1 . GLU   A 1 217 ? 22.297  -44.889 -11.7   1 74.07  ? 202 GLU   A OE1 1 
ATOM   1595 O  OE2 . GLU   A 1 217 ? 20.532  -43.739 -12.369 1 73.66  ? 202 GLU   A OE2 1 
ATOM   1596 N  N   . ILE   A 1 218 ? 24.121  -40.329 -13.808 1 51.83  ? 203 ILE   A N   1 
ATOM   1597 C  CA  . ILE   A 1 218 ? 23.607  -39.346 -14.762 1 51.91  ? 203 ILE   A CA  1 
ATOM   1598 C  C   . ILE   A 1 218 ? 23.854  -39.855 -16.198 1 52.22  ? 203 ILE   A C   1 
ATOM   1599 O  O   . ILE   A 1 218 ? 22.971  -39.781 -17.039 1 52.24  ? 203 ILE   A O   1 
ATOM   1600 C  CB  . ILE   A 1 218 ? 24.241  -37.956 -14.502 1 51.87  ? 203 ILE   A CB  1 
ATOM   1601 C  CG1 . ILE   A 1 218 ? 23.683  -37.323 -13.226 1 52.43  ? 203 ILE   A CG1 1 
ATOM   1602 C  CG2 . ILE   A 1 218 ? 24.074  -37.024 -15.696 1 52.31  ? 203 ILE   A CG2 1 
ATOM   1603 C  CD1 . ILE   A 1 218 ? 24.47   -36.103 -12.74  1 53.38  ? 203 ILE   A CD1 1 
ATOM   1604 N  N   . ALA   A 1 219 ? 25.031  -40.427 -16.445 1 52.36  ? 204 ALA   A N   1 
ATOM   1605 C  CA  . ALA   A 1 219 ? 25.383  -40.968 -17.743 1 52.6   ? 204 ALA   A CA  1 
ATOM   1606 C  C   . ALA   A 1 219 ? 24.429  -42.079 -18.169 1 52.68  ? 204 ALA   A C   1 
ATOM   1607 O  O   . ALA   A 1 219 ? 24.004  -42.087 -19.323 1 52.71  ? 204 ALA   A O   1 
ATOM   1608 C  CB  . ALA   A 1 219 ? 26.813  -41.477 -17.725 1 52.48  ? 204 ALA   A CB  1 
ATOM   1609 N  N   . SER   A 1 220 ? 24.068  -42.989 -17.246 1 52.31  ? 205 SER   A N   1 
ATOM   1610 C  CA  . SER   A 1 220 ? 23.169  -44.094 -17.56  1 52.71  ? 205 SER   A CA  1 
ATOM   1611 C  C   . SER   A 1 220 ? 21.748  -43.607 -17.893 1 53.1   ? 205 SER   A C   1 
ATOM   1612 O  O   . SER   A 1 220 ? 21.077  -44.198 -18.731 1 53.5   ? 205 SER   A O   1 
ATOM   1613 C  CB  . SER   A 1 220 ? 23.169  -45.134 -16.443 1 54.25  ? 205 SER   A CB  1 
ATOM   1614 O  OG  . SER   A 1 220 ? 22.166  -44.926 -15.46  1 57.17  ? 205 SER   A OG  1 
ATOM   1615 N  N   . CYS   A 1 221 ? 21.313  -42.521 -17.261 1 52.85  ? 206 CYS   A N   1 
ATOM   1616 C  CA  . CYS   A 1 221 ? 20.026  -41.899 -17.524 1 53.14  ? 206 CYS   A CA  1 
ATOM   1617 C  C   . CYS   A 1 221 ? 20.029  -41.302 -18.938 1 53.69  ? 206 CYS   A C   1 
ATOM   1618 O  O   . CYS   A 1 221 ? 19.076  -41.498 -19.686 1 54.39  ? 206 CYS   A O   1 
ATOM   1619 C  CB  . CYS   A 1 221 ? 19.735  -40.834 -16.471 1 53.9   ? 206 CYS   A CB  1 
ATOM   1620 S  SG  . CYS   A 1 221 ? 19.303  -41.499 -14.838 1 57.36  ? 206 CYS   A SG  1 
ATOM   1621 N  N   . LEU   A 1 222 ? 21.108  -40.612 -19.315 1 53.34  ? 207 LEU   A N   1 
ATOM   1622 C  CA  . LEU   A 1 222 ? 21.259  -40.024 -20.647 1 53.92  ? 207 LEU   A CA  1 
ATOM   1623 C  C   . LEU   A 1 222 ? 21.465  -41.082 -21.74  1 55.11  ? 207 LEU   A C   1 
ATOM   1624 O  O   . LEU   A 1 222 ? 21.177  -40.828 -22.91  1 55.25  ? 207 LEU   A O   1 
ATOM   1625 C  CB  . LEU   A 1 222 ? 22.405  -38.997 -20.678 1 53.41  ? 207 LEU   A CB  1 
ATOM   1626 C  CG  . LEU   A 1 222 ? 22.338  -37.878 -19.632 1 54.06  ? 207 LEU   A CG  1 
ATOM   1627 C  CD1 . LEU   A 1 222 ? 23.553  -36.995 -19.705 1 54.21  ? 207 LEU   A CD1 1 
ATOM   1628 C  CD2 . LEU   A 1 222 ? 21.087  -37.046 -19.786 1 54.5   ? 207 LEU   A CD2 1 
ATOM   1629 N  N   . GLU   A 1 223 ? 21.993  -42.25  -21.37  1 55.67  ? 208 GLU   A N   1 
ATOM   1630 C  CA  . GLU   A 1 223 ? 22.174  -43.368 -22.294 1 56.35  ? 208 GLU   A CA  1 
ATOM   1631 C  C   . GLU   A 1 223 ? 20.807  -44.022 -22.526 1 57.36  ? 208 GLU   A C   1 
ATOM   1632 O  O   . GLU   A 1 223 ? 20.466  -44.335 -23.67  1 58.12  ? 208 GLU   A O   1 
ATOM   1633 C  CB  . GLU   A 1 223 ? 23.173  -44.377 -21.722 1 58.03  ? 208 GLU   A CB  1 
ATOM   1634 C  CG  . GLU   A 1 223 ? 24.617  -43.943 -21.909 1 61.54  ? 208 GLU   A CG  1 
ATOM   1635 C  CD  . GLU   A 1 223 ? 25.615  -44.589 -20.97  1 65.8   ? 208 GLU   A CD  1 
ATOM   1636 O  OE1 . GLU   A 1 223 ? 25.221  -45.512 -20.217 1 65.67  ? 208 GLU   A OE1 1 
ATOM   1637 O  OE2 . GLU   A 1 223 ? 26.791  -44.15  -20.972 1 67.4   ? 208 GLU   A OE2 1 
ATOM   1638 N  N   . LYS   A 1 224 ? 20.002  -44.171 -21.45  1 56.9   ? 209 LYS   A N   1 
ATOM   1639 C  CA  . LYS   A 1 224 ? 18.653  -44.706 -21.528 1 57.19  ? 209 LYS   A CA  1 
ATOM   1640 C  C   . LYS   A 1 224 ? 17.752  -43.774 -22.357 1 57.42  ? 209 LYS   A C   1 
ATOM   1641 O  O   . LYS   A 1 224 ? 16.853  -44.256 -23.039 1 57.59  ? 209 LYS   A O   1 
ATOM   1642 C  CB  . LYS   A 1 224 ? 18.067  -44.939 -20.115 1 58.61  ? 209 LYS   A CB  1 
ATOM   1643 N  N   . ALA   A 1 225 ? 18.008  -42.455 -22.332 1 57.01  ? 210 ALA   A N   1 
ATOM   1644 C  CA  . ALA   A 1 225 ? 17.234  -41.485 -23.105 1 57.04  ? 210 ALA   A CA  1 
ATOM   1645 C  C   . ALA   A 1 225 ? 17.463  -41.624 -24.613 1 57     ? 210 ALA   A C   1 
ATOM   1646 O  O   . ALA   A 1 225 ? 16.556  -41.321 -25.385 1 57.13  ? 210 ALA   A O   1 
ATOM   1647 C  CB  . ALA   A 1 225 ? 17.56   -40.076 -22.654 1 57.1   ? 210 ALA   A CB  1 
ATOM   1648 N  N   . LEU   A 1 226 ? 18.654  -42.089 -25.037 1 56.34  ? 211 LEU   A N   1 
ATOM   1649 C  CA  . LEU   A 1 226 ? 18.933  -42.312 -26.459 1 56.47  ? 211 LEU   A CA  1 
ATOM   1650 C  C   . LEU   A 1 226 ? 18.163  -43.533 -26.999 1 57.06  ? 211 LEU   A C   1 
ATOM   1651 O  O   . LEU   A 1 226 ? 17.717  -43.546 -28.151 1 56.53  ? 211 LEU   A O   1 
ATOM   1652 C  CB  . LEU   A 1 226 ? 20.441  -42.452 -26.717 1 56.09  ? 211 LEU   A CB  1 
ATOM   1653 C  CG  . LEU   A 1 226 ? 20.872  -42.653 -28.175 1 56.91  ? 211 LEU   A CG  1 
ATOM   1654 C  CD1 . LEU   A 1 226 ? 20.31   -41.582 -29.084 1 57.88  ? 211 LEU   A CD1 1 
ATOM   1655 C  CD2 . LEU   A 1 226 ? 22.352  -42.633 -28.296 1 57     ? 211 LEU   A CD2 1 
ATOM   1656 N  N   . GLN   A 1 227 ? 17.977  -44.541 -26.146 1 57.57  ? 212 GLN   A N   1 
ATOM   1657 C  CA  . GLN   A 1 227 ? 17.214  -45.718 -26.512 1 58.4   ? 212 GLN   A CA  1 
ATOM   1658 C  C   . GLN   A 1 227 ? 15.753  -45.357 -26.722 1 58.62  ? 212 GLN   A C   1 
ATOM   1659 O  O   . GLN   A 1 227 ? 15.143  -45.814 -27.69  1 59.03  ? 212 GLN   A O   1 
ATOM   1660 C  CB  . GLN   A 1 227 ? 17.433  -46.827 -25.475 1 60.4   ? 212 GLN   A CB  1 
ATOM   1661 C  CG  . GLN   A 1 227 ? 18.907  -47.303 -25.462 1 64.24  ? 212 GLN   A CG  1 
ATOM   1662 C  CD  . GLN   A 1 227 ? 19.383  -47.814 -26.825 1 69.03  ? 212 GLN   A CD  1 
ATOM   1663 O  OE1 . GLN   A 1 227 ? 20.34   -47.303 -27.426 1 69.77  ? 212 GLN   A OE1 1 
ATOM   1664 N  NE2 . GLN   A 1 227 ? 18.7    -48.817 -27.361 1 70.43  ? 212 GLN   A NE2 1 
ATOM   1665 N  N   . VAL   A 1 228 ? 15.219  -44.469 -25.867 1 58.34  ? 213 VAL   A N   1 
ATOM   1666 C  CA  . VAL   A 1 228 ? 13.851  -43.955 -25.958 1 58.07  ? 213 VAL   A CA  1 
ATOM   1667 C  C   . VAL   A 1 228 ? 13.668  -43.226 -27.297 1 59.05  ? 213 VAL   A C   1 
ATOM   1668 O  O   . VAL   A 1 228 ? 12.7    -43.475 -27.992 1 59.88  ? 213 VAL   A O   1 
ATOM   1669 C  CB  . VAL   A 1 228 ? 13.531  -43.047 -24.74  1 57.35  ? 213 VAL   A CB  1 
ATOM   1670 C  CG1 . VAL   A 1 228 ? 12.274  -42.225 -24.965 1 57.6   ? 213 VAL   A CG1 1 
ATOM   1671 C  CG2 . VAL   A 1 228 ? 13.425  -43.86  -23.454 1 56.68  ? 213 VAL   A CG2 1 
ATOM   1672 N  N   . PHE   A 1 229 ? 14.63   -42.396 -27.689 1 59.27  ? 214 PHE   A N   1 
ATOM   1673 C  CA  . PHE   A 1 229 ? 14.628  -41.631 -28.942 1 59.81  ? 214 PHE   A CA  1 
ATOM   1674 C  C   . PHE   A 1 229 ? 14.328  -42.489 -30.182 1 59.87  ? 214 PHE   A C   1 
ATOM   1675 O  O   . PHE   A 1 229 ? 13.677  -42.014 -31.097 1 60.18  ? 214 PHE   A O   1 
ATOM   1676 C  CB  . PHE   A 1 229 ? 15.988  -40.923 -29.119 1 59.79  ? 214 PHE   A CB  1 
ATOM   1677 C  CG  . PHE   A 1 229 ? 15.993  -39.606 -29.862 1 60.57  ? 214 PHE   A CG  1 
ATOM   1678 C  CD1 . PHE   A 1 229 ? 15.572  -39.53  -31.178 1 61.52  ? 214 PHE   A CD1 1 
ATOM   1679 C  CD2 . PHE   A 1 229 ? 16.509  -38.467 -29.275 1 61.41  ? 214 PHE   A CD2 1 
ATOM   1680 C  CE1 . PHE   A 1 229 ? 15.589  -38.323 -31.866 1 62.32  ? 214 PHE   A CE1 1 
ATOM   1681 C  CE2 . PHE   A 1 229 ? 16.544  -37.265 -29.969 1 62.3   ? 214 PHE   A CE2 1 
ATOM   1682 C  CZ  . PHE   A 1 229 ? 16.1    -37.205 -31.268 1 62.22  ? 214 PHE   A CZ  1 
ATOM   1683 N  N   . HIS   A 1 230 ? 14.775  -43.746 -30.209 1 59.62  ? 215 HIS   A N   1 
ATOM   1684 C  CA  . HIS   A 1 230 ? 14.586  -44.628 -31.363 1 59.59  ? 215 HIS   A CA  1 
ATOM   1685 C  C   . HIS   A 1 230 ? 13.13   -44.752 -31.854 1 58.27  ? 215 HIS   A C   1 
ATOM   1686 O  O   . HIS   A 1 230 ? 12.921  -45.008 -33.039 1 58.26  ? 215 HIS   A O   1 
ATOM   1687 C  CB  . HIS   A 1 230 ? 15.196  -46.014 -31.098 1 60.94  ? 215 HIS   A CB  1 
ATOM   1688 C  CG  . HIS   A 1 230 ? 16.681  -45.982 -30.891 1 65.49  ? 215 HIS   A CG  1 
ATOM   1689 N  ND1 . HIS   A 1 230 ? 17.481  -44.991 -31.462 1 67.95  ? 215 HIS   A ND1 1 
ATOM   1690 C  CD2 . HIS   A 1 230 ? 17.473  -46.82  -30.178 1 67.08  ? 215 HIS   A CD2 1 
ATOM   1691 C  CE1 . HIS   A 1 230 ? 18.721  -45.26  -31.073 1 68.33  ? 215 HIS   A CE1 1 
ATOM   1692 N  NE2 . HIS   A 1 230 ? 18.767  -46.349 -30.302 1 68.22  ? 215 HIS   A NE2 1 
ATOM   1693 N  N   . GLN   A 1 231 ? 12.138  -44.512 -30.972 1 57.17  ? 216 GLN   A N   1 
ATOM   1694 C  CA  . GLN   A 1 231 ? 10.712  -44.572 -31.315 1 56.81  ? 216 GLN   A CA  1 
ATOM   1695 C  C   . GLN   A 1 231 ? 10.281  -43.547 -32.348 1 57.32  ? 216 GLN   A C   1 
ATOM   1696 O  O   . GLN   A 1 231 ? 9.228   -43.708 -32.937 1 58.05  ? 216 GLN   A O   1 
ATOM   1697 C  CB  . GLN   A 1 231 ? 9.842   -44.385 -30.08  1 57.01  ? 216 GLN   A CB  1 
ATOM   1698 C  CG  . GLN   A 1 231 ? 10.117  -45.371 -28.991 1 59.23  ? 216 GLN   A CG  1 
ATOM   1699 C  CD  . GLN   A 1 231 ? 9.418   -44.945 -27.735 1 62.93  ? 216 GLN   A CD  1 
ATOM   1700 O  OE1 . GLN   A 1 231 ? 8.229   -45.179 -27.551 1 64.21  ? 216 GLN   A OE1 1 
ATOM   1701 N  NE2 . GLN   A 1 231 ? 10.14   -44.296 -26.843 1 63.55  ? 216 GLN   A NE2 1 
ATOM   1702 N  N   . ILE   A 1 232 ? 11.067  -42.494 -32.573 1 57.31  ? 217 ILE   A N   1 
ATOM   1703 C  CA  . ILE   A 1 232 ? 10.719  -41.437 -33.522 1 57.63  ? 217 ILE   A CA  1 
ATOM   1704 C  C   . ILE   A 1 232 ? 10.382  -41.974 -34.916 1 58.51  ? 217 ILE   A C   1 
ATOM   1705 O  O   . ILE   A 1 232 ? 9.492   -41.436 -35.571 1 59.01  ? 217 ILE   A O   1 
ATOM   1706 C  CB  . ILE   A 1 232 ? 11.812  -40.334 -33.575 1 57.29  ? 217 ILE   A CB  1 
ATOM   1707 C  CG1 . ILE   A 1 232 ? 11.3    -39.061 -34.287 1 57.87  ? 217 ILE   A CG1 1 
ATOM   1708 C  CG2 . ILE   A 1 232 ? 13.079  -40.848 -34.222 1 57.6   ? 217 ILE   A CG2 1 
ATOM   1709 C  CD1 . ILE   A 1 232 ? 10.401  -38.176 -33.43  1 58.54  ? 217 ILE   A CD1 1 
ATOM   1710 N  N   . HIS   A 1 233 ? 11.047  -43.053 -35.348 1 58.53  ? 218 HIS   A N   1 
ATOM   1711 C  CA  . HIS   A 1 233 ? 10.819  -43.606 -36.675 1 59.06  ? 218 HIS   A CA  1 
ATOM   1712 C  C   . HIS   A 1 233 ? 9.444   -44.25  -36.834 1 59.25  ? 218 HIS   A C   1 
ATOM   1713 O  O   . HIS   A 1 233 ? 8.852   -44.149 -37.911 1 59.29  ? 218 HIS   A O   1 
ATOM   1714 C  CB  . HIS   A 1 233 ? 11.932  -44.589 -37.049 1 59.74  ? 218 HIS   A CB  1 
ATOM   1715 C  CG  . HIS   A 1 233 ? 13.294  -43.986 -36.951 1 61.8   ? 218 HIS   A CG  1 
ATOM   1716 N  ND1 . HIS   A 1 233 ? 13.786  -43.15  -37.94  1 63.56  ? 218 HIS   A ND1 1 
ATOM   1717 C  CD2 . HIS   A 1 233 ? 14.223  -44.103 -35.972 1 62.64  ? 218 HIS   A CD2 1 
ATOM   1718 C  CE1 . HIS   A 1 233 ? 14.996  -42.794 -37.536 1 63.87  ? 218 HIS   A CE1 1 
ATOM   1719 N  NE2 . HIS   A 1 233 ? 15.304  -43.345 -36.359 1 63.65  ? 218 HIS   A NE2 1 
ATOM   1720 N  N   . ASP   A 1 234 ? 8.93    -44.874 -35.76  1 58.83  ? 219 ASP   A N   1 
ATOM   1721 C  CA  . ASP   A 1 234 ? 7.65    -45.571 -35.785 1 59.4   ? 219 ASP   A CA  1 
ATOM   1722 C  C   . ASP   A 1 234 ? 6.421   -44.698 -35.639 1 59.62  ? 219 ASP   A C   1 
ATOM   1723 O  O   . ASP   A 1 234 ? 5.3     -45.221 -35.778 1 59.78  ? 219 ASP   A O   1 
ATOM   1724 C  CB  . ASP   A 1 234 ? 7.584   -46.623 -34.675 1 61.46  ? 219 ASP   A CB  1 
ATOM   1725 C  CG  . ASP   A 1 234 ? 8.661   -47.651 -34.772 1 66.7   ? 219 ASP   A CG  1 
ATOM   1726 O  OD1 . ASP   A 1 234 ? 8.927   -48.125 -35.909 1 67.17  ? 219 ASP   A OD1 1 
ATOM   1727 O  OD2 . ASP   A 1 234 ? 9.261   -47.972 -33.721 1 69.4   ? 219 ASP   A OD2 1 
ATOM   1728 N  N   . HIS   A 1 235 ? 6.593   -43.419 -35.27  1 59.13  ? 220 HIS   A N   1 
ATOM   1729 C  CA  . HIS   A 1 235 ? 5.424   -42.573 -35.026 1 58.96  ? 220 HIS   A CA  1 
ATOM   1730 C  C   . HIS   A 1 235 ? 5.439   -41.247 -35.788 1 59.17  ? 220 HIS   A C   1 
ATOM   1731 O  O   . HIS   A 1 235 ? 4.513   -40.462 -35.615 1 59.56  ? 220 HIS   A O   1 
ATOM   1732 C  CB  . HIS   A 1 235 ? 5.228   -42.357 -33.517 1 59.11  ? 220 HIS   A CB  1 
ATOM   1733 C  CG  . HIS   A 1 235 ? 5.312   -43.628 -32.714 1 61.3   ? 220 HIS   A CG  1 
ATOM   1734 N  ND1 . HIS   A 1 235 ? 4.339   -44.614 -32.813 1 62.78  ? 220 HIS   A ND1 1 
ATOM   1735 C  CD2 . HIS   A 1 235 ? 6.281   -44.057 -31.871 1 62.57  ? 220 HIS   A CD2 1 
ATOM   1736 C  CE1 . HIS   A 1 235 ? 4.73    -45.587 -32.009 1 63.48  ? 220 HIS   A CE1 1 
ATOM   1737 N  NE2 . HIS   A 1 235 ? 5.893   -45.296 -31.416 1 63.85  ? 220 HIS   A NE2 1 
ATOM   1738 N  N   . VAL   A 1 236 ? 6.454   -41.001 -36.638 1 59.11  ? 221 VAL   A N   1 
ATOM   1739 C  CA  . VAL   A 1 236 ? 6.582   -39.778 -37.44  1 60.34  ? 221 VAL   A CA  1 
ATOM   1740 C  C   . VAL   A 1 236 ? 7.066   -40.164 -38.849 1 62.04  ? 221 VAL   A C   1 
ATOM   1741 O  O   . VAL   A 1 236 ? 7.965   -40.986 -38.964 1 62.57  ? 221 VAL   A O   1 
ATOM   1742 C  CB  . VAL   A 1 236 ? 7.574   -38.751 -36.794 1 60.57  ? 221 VAL   A CB  1 
ATOM   1743 C  CG1 . VAL   A 1 236 ? 7.637   -37.447 -37.584 1 60.7   ? 221 VAL   A CG1 1 
ATOM   1744 C  CG2 . VAL   A 1 236 ? 7.244   -38.468 -35.335 1 60.78  ? 221 VAL   A CG2 1 
ATOM   1745 N  N   . ASN   A 1 237 ? 6.491   -39.587 -39.913 1 62.9   ? 222 ASN   A N   1 
ATOM   1746 C  CA  . ASN   A 1 237 ? 6.958   -39.855 -41.278 1 64.02  ? 222 ASN   A CA  1 
ATOM   1747 C  C   . ASN   A 1 237 ? 7.463   -38.559 -41.912 1 64.38  ? 222 ASN   A C   1 
ATOM   1748 O  O   . ASN   A 1 237 ? 6.854   -37.508 -41.724 1 64.49  ? 222 ASN   A O   1 
ATOM   1749 C  CB  . ASN   A 1 237 ? 5.904   -40.575 -42.145 1 65.75  ? 222 ASN   A CB  1 
ATOM   1750 C  CG  . ASN   A 1 237 ? 4.736   -39.747 -42.622 1 69.78  ? 222 ASN   A CG  1 
ATOM   1751 O  OD1 . ASN   A 1 237 ? 3.653   -39.78  -42.028 1 71.52  ? 222 ASN   A OD1 1 
ATOM   1752 N  ND2 . ASN   A 1 237 ? 4.906   -39.024 -43.735 1 70.34  ? 222 ASN   A ND2 1 
ATOM   1753 N  N   . PRO   A 1 238 ? 8.607   -38.613 -42.615 1 64.29  ? 223 PRO   A N   1 
ATOM   1754 C  CA  . PRO   A 1 238 ? 9.187   -37.388 -43.198 1 64.09  ? 223 PRO   A CA  1 
ATOM   1755 C  C   . PRO   A 1 238 ? 8.257   -36.492 -44.005 1 64.38  ? 223 PRO   A C   1 
ATOM   1756 O  O   . PRO   A 1 238 ? 8.332   -35.276 -43.849 1 64.71  ? 223 PRO   A O   1 
ATOM   1757 C  CB  . PRO   A 1 238 ? 10.324  -37.918 -44.07  1 64.79  ? 223 PRO   A CB  1 
ATOM   1758 C  CG  . PRO   A 1 238 ? 10.733  -39.184 -43.409 1 65.26  ? 223 PRO   A CG  1 
ATOM   1759 C  CD  . PRO   A 1 238 ? 9.466   -39.789 -42.859 1 63.79  ? 223 PRO   A CD  1 
ATOM   1760 N  N   . LYS   A 1 239 ? 7.389   -37.068 -44.856 1 64.31  ? 224 LYS   A N   1 
ATOM   1761 C  CA  . LYS   A 1 239 ? 6.473   -36.281 -45.691 1 64.53  ? 224 LYS   A CA  1 
ATOM   1762 C  C   . LYS   A 1 239 ? 5.473   -35.457 -44.865 1 64.46  ? 224 LYS   A C   1 
ATOM   1763 O  O   . LYS   A 1 239 ? 5.296   -34.264 -45.121 1 64.5   ? 224 LYS   A O   1 
ATOM   1764 C  CB  . LYS   A 1 239 ? 5.744   -37.179 -46.71  1 66.16  ? 224 LYS   A CB  1 
ATOM   1765 N  N   . ALA   A 1 240 ? 4.842   -36.087 -43.867 1 64.06  ? 225 ALA   A N   1 
ATOM   1766 C  CA  . ALA   A 1 240 ? 3.874   -35.411 -43.013 1 64.24  ? 225 ALA   A CA  1 
ATOM   1767 C  C   . ALA   A 1 240 ? 4.533   -34.356 -42.134 1 64.24  ? 225 ALA   A C   1 
ATOM   1768 O  O   . ALA   A 1 240 ? 3.956   -33.289 -41.923 1 64.65  ? 225 ALA   A O   1 
ATOM   1769 C  CB  . ALA   A 1 240 ? 3.158   -36.426 -42.147 1 64.25  ? 225 ALA   A CB  1 
ATOM   1770 N  N   . PHE   A 1 241 ? 5.736   -34.647 -41.628 1 63.46  ? 226 PHE   A N   1 
ATOM   1771 C  CA  . PHE   A 1 241 ? 6.451   -33.695 -40.787 1 63.24  ? 226 PHE   A CA  1 
ATOM   1772 C  C   . PHE   A 1 241 ? 6.884   -32.476 -41.587 1 63.36  ? 226 PHE   A C   1 
ATOM   1773 O  O   . PHE   A 1 241 ? 6.685   -31.359 -41.14  1 63.29  ? 226 PHE   A O   1 
ATOM   1774 C  CB  . PHE   A 1 241 ? 7.656   -34.353 -40.079 1 62.66  ? 226 PHE   A CB  1 
ATOM   1775 C  CG  . PHE   A 1 241 ? 8.433   -33.383 -39.214 1 62.93  ? 226 PHE   A CG  1 
ATOM   1776 C  CD1 . PHE   A 1 241 ? 8.008   -33.076 -37.934 1 63.34  ? 226 PHE   A CD1 1 
ATOM   1777 C  CD2 . PHE   A 1 241 ? 9.563   -32.742 -39.699 1 63.3   ? 226 PHE   A CD2 1 
ATOM   1778 C  CE1 . PHE   A 1 241 ? 8.703   -32.159 -37.156 1 63.7   ? 226 PHE   A CE1 1 
ATOM   1779 C  CE2 . PHE   A 1 241 ? 10.25   -31.826 -38.918 1 63.68  ? 226 PHE   A CE2 1 
ATOM   1780 C  CZ  . PHE   A 1 241 ? 9.828   -31.553 -37.648 1 63.43  ? 226 PHE   A CZ  1 
ATOM   1781 N  N   . PHE   A 1 242 ? 7.485   -32.683 -42.759 1 63.57  ? 227 PHE   A N   1 
ATOM   1782 C  CA  . PHE   A 1 242 ? 7.98    -31.581 -43.58  1 63.95  ? 227 PHE   A CA  1 
ATOM   1783 C  C   . PHE   A 1 242 ? 6.894   -30.766 -44.266 1 64.22  ? 227 PHE   A C   1 
ATOM   1784 O  O   . PHE   A 1 242 ? 6.975   -29.541 -44.268 1 64.44  ? 227 PHE   A O   1 
ATOM   1785 C  CB  . PHE   A 1 242 ? 8.999   -32.077 -44.62  1 63.9   ? 227 PHE   A CB  1 
ATOM   1786 C  CG  . PHE   A 1 242 ? 9.675   -30.963 -45.392 1 64.58  ? 227 PHE   A CG  1 
ATOM   1787 C  CD1 . PHE   A 1 242 ? 10.712  -30.238 -44.831 1 65.42  ? 227 PHE   A CD1 1 
ATOM   1788 C  CD2 . PHE   A 1 242 ? 9.268   -30.639 -46.676 1 65.22  ? 227 PHE   A CD2 1 
ATOM   1789 C  CE1 . PHE   A 1 242 ? 11.334  -29.219 -45.544 1 66.12  ? 227 PHE   A CE1 1 
ATOM   1790 C  CE2 . PHE   A 1 242 ? 9.878   -29.608 -47.377 1 65.88  ? 227 PHE   A CE2 1 
ATOM   1791 C  CZ  . PHE   A 1 242 ? 10.905  -28.905 -46.81  1 65.85  ? 227 PHE   A CZ  1 
ATOM   1792 N  N   . SER   A 1 243 ? 5.913   -31.421 -44.884 1 64.34  ? 228 SER   A N   1 
ATOM   1793 C  CA  . SER   A 1 243 ? 4.87    -30.696 -45.616 1 64.84  ? 228 SER   A CA  1 
ATOM   1794 C  C   . SER   A 1 243 ? 3.689   -30.218 -44.76  1 64.91  ? 228 SER   A C   1 
ATOM   1795 O  O   . SER   A 1 243 ? 2.934   -29.363 -45.224 1 65.41  ? 228 SER   A O   1 
ATOM   1796 C  CB  . SER   A 1 243 ? 4.368   -31.526 -46.794 1 65.89  ? 228 SER   A CB  1 
ATOM   1797 O  OG  . SER   A 1 243 ? 3.75    -32.722 -46.347 1 67.9   ? 228 SER   A OG  1 
ATOM   1798 N  N   . VAL   A 1 244 ? 3.495   -30.776 -43.543 1 64.14  ? 229 VAL   A N   1 
ATOM   1799 C  CA  . VAL   A 1 244 ? 2.345   -30.39  -42.73  1 63.63  ? 229 VAL   A CA  1 
ATOM   1800 C  C   . VAL   A 1 244 ? 2.737   -29.795 -41.345 1 63.37  ? 229 VAL   A C   1 
ATOM   1801 O  O   . VAL   A 1 244 ? 2.639   -28.583 -41.188 1 63.46  ? 229 VAL   A O   1 
ATOM   1802 C  CB  . VAL   A 1 244 ? 1.317   -31.542 -42.617 1 63.82  ? 229 VAL   A CB  1 
ATOM   1803 C  CG1 . VAL   A 1 244 ? 0.067   -31.096 -41.868 1 64.09  ? 229 VAL   A CG1 1 
ATOM   1804 C  CG2 . VAL   A 1 244 ? 0.974   -32.114 -43.989 1 64.09  ? 229 VAL   A CG2 1 
ATOM   1805 N  N   . LEU   A 1 245 ? 3.193   -30.608 -40.368 1 62.84  ? 230 LEU   A N   1 
ATOM   1806 C  CA  . LEU   A 1 245 ? 3.491   -30.174 -39.002 1 62.92  ? 230 LEU   A CA  1 
ATOM   1807 C  C   . LEU   A 1 245 ? 4.375   -28.938 -38.892 1 63.37  ? 230 LEU   A C   1 
ATOM   1808 O  O   . LEU   A 1 245 ? 4.109   -28.082 -38.057 1 63.64  ? 230 LEU   A O   1 
ATOM   1809 C  CB  . LEU   A 1 245 ? 4.093   -31.33  -38.191 1 62.74  ? 230 LEU   A CB  1 
ATOM   1810 C  CG  . LEU   A 1 245 ? 4.123   -31.171 -36.668 1 63.21  ? 230 LEU   A CG  1 
ATOM   1811 C  CD1 . LEU   A 1 245 ? 2.743   -30.975 -36.11  1 63.56  ? 230 LEU   A CD1 1 
ATOM   1812 C  CD2 . LEU   A 1 245 ? 4.709   -32.379 -36.026 1 63.52  ? 230 LEU   A CD2 1 
ATOM   1813 N  N   . ARG   A 1 246 ? 5.405   -28.842 -39.732 1 63.33  ? 231 ARG   A N   1 
ATOM   1814 C  CA  . ARG   A 1 246 ? 6.379   -27.745 -39.787 1 63.81  ? 231 ARG   A CA  1 
ATOM   1815 C  C   . ARG   A 1 246 ? 5.704   -26.363 -39.851 1 63.69  ? 231 ARG   A C   1 
ATOM   1816 O  O   . ARG   A 1 246 ? 6.148   -25.414 -39.188 1 64.02  ? 231 ARG   A O   1 
ATOM   1817 C  CB  . ARG   A 1 246 ? 7.311   -27.972 -41.003 1 65.5   ? 231 ARG   A CB  1 
ATOM   1818 C  CG  . ARG   A 1 246 ? 8.092   -26.776 -41.498 1 69.18  ? 231 ARG   A CG  1 
ATOM   1819 C  CD  . ARG   A 1 246 ? 7.96    -26.613 -43.007 1 73.45  ? 231 ARG   A CD  1 
ATOM   1820 N  NE  . ARG   A 1 246 ? 9.196   -26.197 -43.666 1 78.76  ? 231 ARG   A NE  1 
ATOM   1821 C  CZ  . ARG   A 1 246 ? 9.742   -24.983 -43.573 1 83.01  ? 231 ARG   A CZ  1 
ATOM   1822 N  NH1 . ARG   A 1 246 ? 10.863  -24.702 -44.228 1 83.58  ? 231 ARG   A NH1 1 
ATOM   1823 N  NH2 . ARG   A 1 246 ? 9.186   -24.05  -42.804 1 83.58  ? 231 ARG   A NH2 1 
ATOM   1824 N  N   . ILE   A 1 247 ? 4.635   -26.264 -40.651 1 62.91  ? 232 ILE   A N   1 
ATOM   1825 C  CA  . ILE   A 1 247 ? 3.879   -25.031 -40.844 1 62.89  ? 232 ILE   A CA  1 
ATOM   1826 C  C   . ILE   A 1 247 ? 3.4     -24.438 -39.507 1 61.93  ? 232 ILE   A C   1 
ATOM   1827 O  O   . ILE   A 1 247 ? 3.643   -23.272 -39.221 1 61.87  ? 232 ILE   A O   1 
ATOM   1828 C  CB  . ILE   A 1 247 ? 2.659   -25.303 -41.771 1 63.84  ? 232 ILE   A CB  1 
ATOM   1829 C  CG1 . ILE   A 1 247 ? 3.052   -25.842 -43.155 1 65.34  ? 232 ILE   A CG1 1 
ATOM   1830 C  CG2 . ILE   A 1 247 ? 1.779   -24.078 -41.873 1 64.32  ? 232 ILE   A CG2 1 
ATOM   1831 C  CD1 . ILE   A 1 247 ? 1.779   -26.404 -43.929 1 66.56  ? 232 ILE   A CD1 1 
ATOM   1832 N  N   . TYR   A 1 248 ? 2.747   -25.263 -38.694 1 61.13  ? 233 TYR   A N   1 
ATOM   1833 C  CA  . TYR   A 1 248 ? 2.108   -24.877 -37.446 1 61.18  ? 233 TYR   A CA  1 
ATOM   1834 C  C   . TYR   A 1 248 ? 3.103   -24.637 -36.29  1 62.01  ? 233 TYR   A C   1 
ATOM   1835 O  O   . TYR   A 1 248 ? 2.759   -23.966 -35.31  1 62.43  ? 233 TYR   A O   1 
ATOM   1836 C  CB  . TYR   A 1 248 ? 1.012   -25.899 -37.104 1 60.31  ? 233 TYR   A CB  1 
ATOM   1837 C  CG  . TYR   A 1 248 ? -0.02   -25.96  -38.211 1 60.37  ? 233 TYR   A CG  1 
ATOM   1838 C  CD1 . TYR   A 1 248 ? -0.986  -24.974 -38.339 1 60.8   ? 233 TYR   A CD1 1 
ATOM   1839 C  CD2 . TYR   A 1 248 ? 0.07    -26.908 -39.222 1 60.78  ? 233 TYR   A CD2 1 
ATOM   1840 C  CE1 . TYR   A 1 248 ? -1.881  -24.972 -39.4   1 61.29  ? 233 TYR   A CE1 1 
ATOM   1841 C  CE2 . TYR   A 1 248 ? -0.808  -26.903 -40.299 1 61.41  ? 233 TYR   A CE2 1 
ATOM   1842 C  CZ  . TYR   A 1 248 ? -1.782  -25.93  -40.387 1 62.15  ? 233 TYR   A CZ  1 
ATOM   1843 O  OH  . TYR   A 1 248 ? -2.66   -25.914 -41.447 1 63.55  ? 233 TYR   A OH  1 
ATOM   1844 N  N   . LEU   A 1 249 ? 4.345   -25.127 -36.435 1 61.77  ? 234 LEU   A N   1 
ATOM   1845 C  CA  . LEU   A 1 249 ? 5.419   -24.893 -35.473 1 61.81  ? 234 LEU   A CA  1 
ATOM   1846 C  C   . LEU   A 1 249 ? 6.096   -23.532 -35.711 1 61.63  ? 234 LEU   A C   1 
ATOM   1847 O  O   . LEU   A 1 249 ? 6.809   -23.062 -34.823 1 62.24  ? 234 LEU   A O   1 
ATOM   1848 C  CB  . LEU   A 1 249 ? 6.487   -26     -35.583 1 61.75  ? 234 LEU   A CB  1 
ATOM   1849 C  CG  . LEU   A 1 249 ? 6.012   -27.413 -35.31  1 62.76  ? 234 LEU   A CG  1 
ATOM   1850 C  CD1 . LEU   A 1 249 ? 7.13    -28.398 -35.541 1 63.16  ? 234 LEU   A CD1 1 
ATOM   1851 C  CD2 . LEU   A 1 249 ? 5.449   -27.552 -33.89  1 63.24  ? 234 LEU   A CD2 1 
ATOM   1852 N  N   . SER   A 1 250 ? 5.928   -22.935 -36.916 1 60.71  ? 235 SER   A N   1 
ATOM   1853 C  CA  . SER   A 1 250 ? 6.549   -21.669 -37.287 1 60.36  ? 235 SER   A CA  1 
ATOM   1854 C  C   . SER   A 1 250 ? 6.091   -20.483 -36.46  1 59.35  ? 235 SER   A C   1 
ATOM   1855 O  O   . SER   A 1 250 ? 4.907   -20.351 -36.156 1 59.34  ? 235 SER   A O   1 
ATOM   1856 C  CB  . SER   A 1 250 ? 6.351   -21.388 -38.772 1 62.32  ? 235 SER   A CB  1 
ATOM   1857 O  OG  . SER   A 1 250 ? 7.264   -22.14  -39.554 1 66.06  ? 235 SER   A OG  1 
ATOM   1858 N  N   . GLY   A 1 251 ? 7.04    -19.625 -36.11  1 58.25  ? 236 GLY   A N   1 
ATOM   1859 C  CA  . GLY   A 1 251 ? 6.758   -18.422 -35.344 1 57.83  ? 236 GLY   A CA  1 
ATOM   1860 C  C   . GLY   A 1 251 ? 6.828   -17.169 -36.191 1 57.2   ? 236 GLY   A C   1 
ATOM   1861 O  O   . GLY   A 1 251 ? 6.804   -17.23  -37.426 1 56.76  ? 236 GLY   A O   1 
ATOM   1862 N  N   . TRP   A 1 252 ? 6.901   -16.017 -35.527 1 56.64  ? 237 TRP   A N   1 
ATOM   1863 C  CA  . TRP   A 1 252 ? 6.935   -14.742 -36.23  1 56.28  ? 237 TRP   A CA  1 
ATOM   1864 C  C   . TRP   A 1 252 ? 8.101   -13.875 -35.796 1 57.49  ? 237 TRP   A C   1 
ATOM   1865 O  O   . TRP   A 1 252 ? 7.935   -12.682 -35.596 1 57.99  ? 237 TRP   A O   1 
ATOM   1866 C  CB  . TRP   A 1 252 ? 5.587   -13.982 -36.158 1 55.03  ? 237 TRP   A CB  1 
ATOM   1867 C  CG  . TRP   A 1 252 ? 4.717   -14.288 -34.969 1 53.85  ? 237 TRP   A CG  1 
ATOM   1868 C  CD1 . TRP   A 1 252 ? 4.62    -13.571 -33.813 1 54.01  ? 237 TRP   A CD1 1 
ATOM   1869 C  CD2 . TRP   A 1 252 ? 3.775   -15.365 -34.856 1 53.42  ? 237 TRP   A CD2 1 
ATOM   1870 N  NE1 . TRP   A 1 252 ? 3.679   -14.138 -32.985 1 54.04  ? 237 TRP   A NE1 1 
ATOM   1871 C  CE2 . TRP   A 1 252 ? 3.147   -15.242 -33.602 1 53.79  ? 237 TRP   A CE2 1 
ATOM   1872 C  CE3 . TRP   A 1 252 ? 3.402   -16.426 -35.697 1 53.85  ? 237 TRP   A CE3 1 
ATOM   1873 C  CZ2 . TRP   A 1 252 ? 2.185   -16.151 -33.163 1 54.24  ? 237 TRP   A CZ2 1 
ATOM   1874 C  CZ3 . TRP   A 1 252 ? 2.43    -17.309 -35.271 1 54.17  ? 237 TRP   A CZ3 1 
ATOM   1875 C  CH2 . TRP   A 1 252 ? 1.838   -17.172 -34.017 1 54.24  ? 237 TRP   A CH2 1 
ATOM   1876 N  N   . LYS   A 1 253 ? 9.289   -14.461 -35.695 1 57.96  ? 238 LYS   A N   1 
ATOM   1877 C  CA  . LYS   A 1 253 ? 10.493  -13.722 -35.366 1 59.31  ? 238 LYS   A CA  1 
ATOM   1878 C  C   . LYS   A 1 253 ? 11.437  -13.962 -36.531 1 61.43  ? 238 LYS   A C   1 
ATOM   1879 O  O   . LYS   A 1 253 ? 11.928  -15.075 -36.693 1 62.07  ? 238 LYS   A O   1 
ATOM   1880 C  CB  . LYS   A 1 253 ? 11.115  -14.263 -34.076 1 60.35  ? 238 LYS   A CB  1 
ATOM   1881 C  CG  . LYS   A 1 253 ? 11.902  -13.236 -33.296 1 63.71  ? 238 LYS   A CG  1 
ATOM   1882 C  CD  . LYS   A 1 253 ? 13.397  -13.436 -33.454 1 67.75  ? 238 LYS   A CD  1 
ATOM   1883 C  CE  . LYS   A 1 253 ? 14.132  -13.158 -32.164 1 70.74  ? 238 LYS   A CE  1 
ATOM   1884 N  NZ  . LYS   A 1 253 ? 13.523  -12.023 -31.418 1 72.44  ? 238 LYS   A NZ  1 
ATOM   1885 N  N   . GLY   A 1 254 ? 11.643  -12.953 -37.365 1 62.29  ? 239 GLY   A N   1 
ATOM   1886 C  CA  . GLY   A 1 254 ? 12.508  -13.09  -38.527 1 63.59  ? 239 GLY   A CA  1 
ATOM   1887 C  C   . GLY   A 1 254 ? 11.912  -13.954 -39.623 1 65.18  ? 239 GLY   A C   1 
ATOM   1888 O  O   . GLY   A 1 254 ? 12.64   -14.602 -40.381 1 65.57  ? 239 GLY   A O   1 
ATOM   1889 N  N   . ASN   A 1 255 ? 10.582  -13.981 -39.711 1 65.78  ? 240 ASN   A N   1 
ATOM   1890 C  CA  . ASN   A 1 255 ? 9.874   -14.751 -40.717 1 67.21  ? 240 ASN   A CA  1 
ATOM   1891 C  C   . ASN   A 1 255 ? 9.408   -13.799 -41.802 1 69.07  ? 240 ASN   A C   1 
ATOM   1892 O  O   . ASN   A 1 255 ? 8.687   -12.846 -41.518 1 69.39  ? 240 ASN   A O   1 
ATOM   1893 C  CB  . ASN   A 1 255 ? 8.669   -15.464 -40.092 1 67.81  ? 240 ASN   A CB  1 
ATOM   1894 C  CG  . ASN   A 1 255 ? 8.028   -16.52  -40.97  1 70.38  ? 240 ASN   A CG  1 
ATOM   1895 O  OD1 . ASN   A 1 255 ? 8.044   -16.466 -42.207 1 71.11  ? 240 ASN   A OD1 1 
ATOM   1896 N  ND2 . ASN   A 1 255 ? 7.429   -17.505 -40.337 1 71.11  ? 240 ASN   A ND2 1 
ATOM   1897 N  N   . PRO   A 1 256 ? 9.765   -14.063 -43.065 1 69.98  ? 241 PRO   A N   1 
ATOM   1898 C  CA  . PRO   A 1 256 ? 9.336   -13.164 -44.151 1 70.72  ? 241 PRO   A CA  1 
ATOM   1899 C  C   . PRO   A 1 256 ? 7.819   -13.112 -44.381 1 71.74  ? 241 PRO   A C   1 
ATOM   1900 O  O   . PRO   A 1 256 ? 7.328   -12.178 -45.01  1 71.85  ? 241 PRO   A O   1 
ATOM   1901 C  CB  . PRO   A 1 256 ? 10.091  -13.697 -45.367 1 71.27  ? 241 PRO   A CB  1 
ATOM   1902 C  CG  . PRO   A 1 256 ? 11.209  -14.528 -44.802 1 71.5   ? 241 PRO   A CG  1 
ATOM   1903 C  CD  . PRO   A 1 256 ? 10.64   -15.132 -43.566 1 69.69  ? 241 PRO   A CD  1 
ATOM   1904 N  N   . GLN   A 1 257 ? 7.071   -14.099 -43.863 1 72.25  ? 242 GLN   A N   1 
ATOM   1905 C  CA  . GLN   A 1 257 ? 5.615   -14.116 -43.987 1 73.14  ? 242 GLN   A CA  1 
ATOM   1906 C  C   . GLN   A 1 257 ? 4.945   -13.139 -43.014 1 74.41  ? 242 GLN   A C   1 
ATOM   1907 O  O   . GLN   A 1 257 ? 3.836   -12.69  -43.285 1 75.11  ? 242 GLN   A O   1 
ATOM   1908 C  CB  . GLN   A 1 257 ? 5.058   -15.533 -43.832 1 74.04  ? 242 GLN   A CB  1 
ATOM   1909 C  CG  . GLN   A 1 257 ? 5.698   -16.51  -44.802 1 76.88  ? 242 GLN   A CG  1 
ATOM   1910 C  CD  . GLN   A 1 257 ? 5.101   -17.884 -44.691 1 81.05  ? 242 GLN   A CD  1 
ATOM   1911 O  OE1 . GLN   A 1 257 ? 5.718   -18.813 -44.159 1 83.24  ? 242 GLN   A OE1 1 
ATOM   1912 N  NE2 . GLN   A 1 257 ? 3.887   -18.046 -45.189 1 81.07  ? 242 GLN   A NE2 1 
ATOM   1913 N  N   . LEU   A 1 258 ? 5.607   -12.811 -41.886 1 74.56  ? 243 LEU   A N   1 
ATOM   1914 C  CA  . LEU   A 1 258 ? 5.14    -11.832 -40.901 1 75.09  ? 243 LEU   A CA  1 
ATOM   1915 C  C   . LEU   A 1 258 ? 6.386   -11.042 -40.517 1 75.41  ? 243 LEU   A C   1 
ATOM   1916 O  O   . LEU   A 1 258 ? 6.885   -11.161 -39.395 1 75.8   ? 243 LEU   A O   1 
ATOM   1917 C  CB  . LEU   A 1 258 ? 4.523   -12.504 -39.661 1 75.39  ? 243 LEU   A CB  1 
ATOM   1918 C  CG  . LEU   A 1 258 ? 3.159   -13.126 -39.841 1 77.23  ? 243 LEU   A CG  1 
ATOM   1919 C  CD1 . LEU   A 1 258 ? 3.292   -14.587 -40.069 1 78.11  ? 243 LEU   A CD1 1 
ATOM   1920 C  CD2 . LEU   A 1 258 ? 2.305   -12.924 -38.608 1 77.97  ? 243 LEU   A CD2 1 
ATOM   1921 N  N   . SER   A 1 259 ? 6.935   -10.291 -41.485 1 75.05  ? 244 SER   A N   1 
ATOM   1922 C  CA  . SER   A 1 259 ? 8.188   -9.563  -41.328 1 75.2   ? 244 SER   A CA  1 
ATOM   1923 C  C   . SER   A 1 259 ? 8.265   -8.681  -40.084 1 74.84  ? 244 SER   A C   1 
ATOM   1924 O  O   . SER   A 1 259 ? 9.346   -8.577  -39.502 1 75.24  ? 244 SER   A O   1 
ATOM   1925 C  CB  . SER   A 1 259 ? 8.519   -8.76   -42.583 1 76.81  ? 244 SER   A CB  1 
ATOM   1926 O  OG  . SER   A 1 259 ? 7.727   -7.589  -42.686 1 79.61  ? 244 SER   A OG  1 
ATOM   1927 N  N   . ASP   A 1 260 ? 7.148   -8.075  -39.652 1 74.01  ? 245 ASP   A N   1 
ATOM   1928 C  CA  . ASP   A 1 260 ? 7.178   -7.217  -38.451 1 73.66  ? 245 ASP   A CA  1 
ATOM   1929 C  C   . ASP   A 1 260 ? 6.589   -7.862  -37.184 1 71.94  ? 245 ASP   A C   1 
ATOM   1930 O  O   . ASP   A 1 260 ? 6.563   -7.228  -36.131 1 72.32  ? 245 ASP   A O   1 
ATOM   1931 C  CB  . ASP   A 1 260 ? 6.499   -5.86   -38.715 1 76.56  ? 245 ASP   A CB  1 
ATOM   1932 C  CG  . ASP   A 1 260 ? 6.892   -5.232  -40.036 1 83.24  ? 245 ASP   A CG  1 
ATOM   1933 O  OD1 . ASP   A 1 260 ? 8.103   -4.928  -40.215 1 84.24  ? 245 ASP   A OD1 1 
ATOM   1934 O  OD2 . ASP   A 1 260 ? 5.994   -5.064  -40.905 1 85.86  ? 245 ASP   A OD2 1 
ATOM   1935 N  N   . GLY   A 1 261 ? 6.131   -9.101  -37.285 1 69.94  ? 246 GLY   A N   1 
ATOM   1936 C  CA  . GLY   A 1 261 ? 5.536   -9.795  -36.155 1 68.47  ? 246 GLY   A CA  1 
ATOM   1937 C  C   . GLY   A 1 261 ? 4.042   -9.954  -36.306 1 66.69  ? 246 GLY   A C   1 
ATOM   1938 O  O   . GLY   A 1 261 ? 3.504   -9.82   -37.407 1 66.95  ? 246 GLY   A O   1 
ATOM   1939 N  N   . LEU   A 1 262 ? 3.362   -10.251 -35.21  1 64.95  ? 247 LEU   A N   1 
ATOM   1940 C  CA  . LEU   A 1 262 ? 1.919   -10.443 -35.227 1 64.2   ? 247 LEU   A CA  1 
ATOM   1941 C  C   . LEU   A 1 262 ? 1.242   -9.342  -34.421 1 65.29  ? 247 LEU   A C   1 
ATOM   1942 O  O   . LEU   A 1 262 ? 1.764   -8.939  -33.377 1 66.04  ? 247 LEU   A O   1 
ATOM   1943 C  CB  . LEU   A 1 262 ? 1.57    -11.807 -34.626 1 62.84  ? 247 LEU   A CB  1 
ATOM   1944 C  CG  . LEU   A 1 262 ? 0.112   -12.194 -34.643 1 62.92  ? 247 LEU   A CG  1 
ATOM   1945 C  CD1 . LEU   A 1 262 ? -0.359  -12.5   -36.038 1 62.99  ? 247 LEU   A CD1 1 
ATOM   1946 C  CD2 . LEU   A 1 262 ? -0.145  -13.367 -33.738 1 63.4   ? 247 LEU   A CD2 1 
ATOM   1947 N  N   . VAL   A 1 263 ? 0.078   -8.86   -34.884 1 64.77  ? 248 VAL   A N   1 
ATOM   1948 C  CA  . VAL   A 1 263 ? -0.648  -7.846  -34.146 1 64.71  ? 248 VAL   A CA  1 
ATOM   1949 C  C   . VAL   A 1 263 ? -1.526  -8.535  -33.122 1 64.79  ? 248 VAL   A C   1 
ATOM   1950 O  O   . VAL   A 1 263 ? -2.334  -9.389  -33.474 1 64.64  ? 248 VAL   A O   1 
ATOM   1951 C  CB  . VAL   A 1 263 ? -1.458  -6.92   -35.072 1 65.19  ? 248 VAL   A CB  1 
ATOM   1952 C  CG1 . VAL   A 1 263 ? -2.147  -5.814  -34.281 1 64.92  ? 248 VAL   A CG1 1 
ATOM   1953 C  CG2 . VAL   A 1 263 ? -0.567  -6.34   -36.16  1 65.9   ? 248 VAL   A CG2 1 
ATOM   1954 N  N   . TYR   A 1 264 ? -1.345  -8.195  -31.848 1 65.07  ? 249 TYR   A N   1 
ATOM   1955 C  CA  . TYR   A 1 264 ? -2.167  -8.768  -30.783 1 65.64  ? 249 TYR   A CA  1 
ATOM   1956 C  C   . TYR   A 1 264 ? -3.238  -7.731  -30.472 1 67.49  ? 249 TYR   A C   1 
ATOM   1957 O  O   . TYR   A 1 264 ? -3.074  -6.936  -29.546 1 68.19  ? 249 TYR   A O   1 
ATOM   1958 C  CB  . TYR   A 1 264 ? -1.298  -9.101  -29.549 1 64.55  ? 249 TYR   A CB  1 
ATOM   1959 C  CG  . TYR   A 1 264 ? -0.375  -10.28  -29.78  1 63.48  ? 249 TYR   A CG  1 
ATOM   1960 C  CD1 . TYR   A 1 264 ? 0.903   -10.1   -30.294 1 63.47  ? 249 TYR   A CD1 1 
ATOM   1961 C  CD2 . TYR   A 1 264 ? -0.808  -11.58  -29.558 1 63.48  ? 249 TYR   A CD2 1 
ATOM   1962 C  CE1 . TYR   A 1 264 ? 1.738   -11.184 -30.549 1 63.86  ? 249 TYR   A CE1 1 
ATOM   1963 C  CE2 . TYR   A 1 264 ? 0.017   -12.67  -29.814 1 63.68  ? 249 TYR   A CE2 1 
ATOM   1964 C  CZ  . TYR   A 1 264 ? 1.287   -12.468 -30.313 1 64.07  ? 249 TYR   A CZ  1 
ATOM   1965 O  OH  . TYR   A 1 264 ? 2.102   -13.546 -30.542 1 64.64  ? 249 TYR   A OH  1 
ATOM   1966 N  N   . GLU   A 1 265 ? -4.279  -7.673  -31.327 1 68.14  ? 250 GLU   A N   1 
ATOM   1967 C  CA  . GLU   A 1 265 ? -5.38   -6.708  -31.271 1 69.3   ? 250 GLU   A CA  1 
ATOM   1968 C  C   . GLU   A 1 265 ? -5.956  -6.48   -29.884 1 70.69  ? 250 GLU   A C   1 
ATOM   1969 O  O   . GLU   A 1 265 ? -6.327  -7.432  -29.195 1 70.94  ? 250 GLU   A O   1 
ATOM   1970 C  CB  . GLU   A 1 265 ? -6.494  -7.102  -32.248 1 71.16  ? 250 GLU   A CB  1 
ATOM   1971 C  CG  . GLU   A 1 265 ? -7.589  -6.067  -32.403 1 75.47  ? 250 GLU   A CG  1 
ATOM   1972 C  CD  . GLU   A 1 265 ? -8.692  -6.501  -33.346 1 81.66  ? 250 GLU   A CD  1 
ATOM   1973 O  OE1 . GLU   A 1 265 ? -9.55   -7.306  -32.918 1 82.42  ? 250 GLU   A OE1 1 
ATOM   1974 O  OE2 . GLU   A 1 265 ? -8.691  -6.053  -34.515 1 84.1   ? 250 GLU   A OE2 1 
ATOM   1975 N  N   . GLY   A 1 266 ? -5.998  -5.216  -29.478 1 71.35  ? 251 GLY   A N   1 
ATOM   1976 C  CA  . GLY   A 1 266 ? -6.541  -4.83   -28.181 1 72.47  ? 251 GLY   A CA  1 
ATOM   1977 C  C   . GLY   A 1 266 ? -5.619  -5.048  -26.996 1 73.19  ? 251 GLY   A C   1 
ATOM   1978 O  O   . GLY   A 1 266 ? -6.052  -4.928  -25.845 1 73.67  ? 251 GLY   A O   1 
ATOM   1979 N  N   . PHE   A 1 267 ? -4.347  -5.391  -27.264 1 72.74  ? 252 PHE   A N   1 
ATOM   1980 C  CA  . PHE   A 1 267 ? -3.371  -5.618  -26.21  1 72.43  ? 252 PHE   A CA  1 
ATOM   1981 C  C   . PHE   A 1 267 ? -2.118  -4.804  -26.491 1 73.24  ? 252 PHE   A C   1 
ATOM   1982 O  O   . PHE   A 1 267 ? -1.6    -4.139  -25.594 1 73.24  ? 252 PHE   A O   1 
ATOM   1983 C  CB  . PHE   A 1 267 ? -3.05   -7.109  -26.057 1 71.27  ? 252 PHE   A CB  1 
ATOM   1984 C  CG  . PHE   A 1 267 ? -2.472  -7.404  -24.697 1 70.84  ? 252 PHE   A CG  1 
ATOM   1985 C  CD1 . PHE   A 1 267 ? -3.3    -7.689  -23.624 1 70.94  ? 252 PHE   A CD1 1 
ATOM   1986 C  CD2 . PHE   A 1 267 ? -1.103  -7.343  -24.478 1 71.07  ? 252 PHE   A CD2 1 
ATOM   1987 C  CE1 . PHE   A 1 267 ? -2.767  -7.942  -22.371 1 71.28  ? 252 PHE   A CE1 1 
ATOM   1988 C  CE2 . PHE   A 1 267 ? -0.576  -7.589  -23.222 1 71.11  ? 252 PHE   A CE2 1 
ATOM   1989 C  CZ  . PHE   A 1 267 ? -1.409  -7.894  -22.18  1 70.83  ? 252 PHE   A CZ  1 
ATOM   1990 N  N   . TRP   A 1 268 ? -1.641  -4.844  -27.734 1 73.81  ? 253 TRP   A N   1 
ATOM   1991 C  CA  . TRP   A 1 268 ? -0.479  -4.073  -28.129 1 75.46  ? 253 TRP   A CA  1 
ATOM   1992 C  C   . TRP   A 1 268 ? -0.769  -3.198  -29.346 1 76.39  ? 253 TRP   A C   1 
ATOM   1993 O  O   . TRP   A 1 268 ? -1.662  -3.496  -30.147 1 76.76  ? 253 TRP   A O   1 
ATOM   1994 C  CB  . TRP   A 1 268 ? 0.737   -4.972  -28.368 1 76.18  ? 253 TRP   A CB  1 
ATOM   1995 C  CG  . TRP   A 1 268 ? 1.369   -5.476  -27.105 1 77.75  ? 253 TRP   A CG  1 
ATOM   1996 C  CD1 . TRP   A 1 268 ? 1.779   -4.736  -26.033 1 78.95  ? 253 TRP   A CD1 1 
ATOM   1997 C  CD2 . TRP   A 1 268 ? 1.697   -6.836  -26.803 1 78.33  ? 253 TRP   A CD2 1 
ATOM   1998 N  NE1 . TRP   A 1 268 ? 2.319   -5.557  -25.07  1 79.32  ? 253 TRP   A NE1 1 
ATOM   1999 C  CE2 . TRP   A 1 268 ? 2.292   -6.851  -25.522 1 79.17  ? 253 TRP   A CE2 1 
ATOM   2000 C  CE3 . TRP   A 1 268 ? 1.555   -8.044  -27.496 1 78.82  ? 253 TRP   A CE3 1 
ATOM   2001 C  CZ2 . TRP   A 1 268 ? 2.739   -8.03   -24.924 1 79.7   ? 253 TRP   A CZ2 1 
ATOM   2002 C  CZ3 . TRP   A 1 268 ? 1.993   -9.208  -26.901 1 79.62  ? 253 TRP   A CZ3 1 
ATOM   2003 C  CH2 . TRP   A 1 268 ? 2.581   -9.195  -25.632 1 79.73  ? 253 TRP   A CH2 1 
ATOM   2004 N  N   . GLU   A 1 269 ? -0.024  -2.099  -29.463 1 76.58  ? 254 GLU   A N   1 
ATOM   2005 C  CA  . GLU   A 1 269 ? -0.175  -1.143  -30.55  1 77.2   ? 254 GLU   A CA  1 
ATOM   2006 C  C   . GLU   A 1 269 ? 0.594   -1.631  -31.788 1 77.04  ? 254 GLU   A C   1 
ATOM   2007 O  O   . GLU   A 1 269 ? 0.038   -1.711  -32.885 1 77.43  ? 254 GLU   A O   1 
ATOM   2008 C  CB  . GLU   A 1 269 ? 0.329   0.246   -30.088 1 79.83  ? 254 GLU   A CB  1 
ATOM   2009 C  CG  . GLU   A 1 269 ? -0.712  1.347   -30.173 1 84.58  ? 254 GLU   A CG  1 
ATOM   2010 C  CD  . GLU   A 1 269 ? -1.091  1.713   -31.593 1 90.31  ? 254 GLU   A CD  1 
ATOM   2011 O  OE1 . GLU   A 1 269 ? -0.186  1.904   -32.442 1 90.73  ? 254 GLU   A OE1 1 
ATOM   2012 O  OE2 . GLU   A 1 269 ? -2.309  1.8     -31.857 1 92.9   ? 254 GLU   A OE2 1 
ATOM   2013 N  N   . ASP   A 1 270 ? 1.87    -1.969  -31.598 1 76.32  ? 255 ASP   A N   1 
ATOM   2014 C  CA  . ASP   A 1 270 ? 2.757   -2.443  -32.652 1 75.97  ? 255 ASP   A CA  1 
ATOM   2015 C  C   . ASP   A 1 270 ? 2.766   -3.99   -32.719 1 74.9   ? 255 ASP   A C   1 
ATOM   2016 O  O   . ASP   A 1 270 ? 2.458   -4.652  -31.725 1 74.93  ? 255 ASP   A O   1 
ATOM   2017 C  CB  . ASP   A 1 270 ? 4.175   -1.89   -32.398 1 77.9   ? 255 ASP   A CB  1 
ATOM   2018 C  CG  . ASP   A 1 270 ? 4.236   -0.371  -32.36  1 82.83  ? 255 ASP   A CG  1 
ATOM   2019 O  OD1 . ASP   A 1 270 ? 3.79    0.273   -33.355 1 83.6   ? 255 ASP   A OD1 1 
ATOM   2020 O  OD2 . ASP   A 1 270 ? 4.732   0.178   -31.344 1 84.48  ? 255 ASP   A OD2 1 
ATOM   2021 N  N   . PRO   A 1 271 ? 3.087   -4.588  -33.885 1 73.73  ? 256 PRO   A N   1 
ATOM   2022 C  CA  . PRO   A 1 271 ? 3.126   -6.055  -33.955 1 72.87  ? 256 PRO   A CA  1 
ATOM   2023 C  C   . PRO   A 1 271 ? 4.367   -6.615  -33.252 1 71.41  ? 256 PRO   A C   1 
ATOM   2024 O  O   . PRO   A 1 271 ? 5.485   -6.144  -33.481 1 71.38  ? 256 PRO   A O   1 
ATOM   2025 C  CB  . PRO   A 1 271 ? 3.13    -6.338  -35.455 1 73.76  ? 256 PRO   A CB  1 
ATOM   2026 C  CG  . PRO   A 1 271 ? 3.8     -5.153  -36.051 1 74.35  ? 256 PRO   A CG  1 
ATOM   2027 C  CD  . PRO   A 1 271 ? 3.478   -3.972  -35.167 1 73.04  ? 256 PRO   A CD  1 
ATOM   2028 N  N   . LYS   A 1 272 ? 4.168   -7.612  -32.375 1 69.76  ? 257 LYS   A N   1 
ATOM   2029 C  CA  . LYS   A 1 272 ? 5.282   -8.192  -31.631 1 68.54  ? 257 LYS   A CA  1 
ATOM   2030 C  C   . LYS   A 1 272 ? 5.82    -9.492  -32.26  1 66.83  ? 257 LYS   A C   1 
ATOM   2031 O  O   . LYS   A 1 272 ? 5.044   -10.337 -32.704 1 67.26  ? 257 LYS   A O   1 
ATOM   2032 C  CB  . LYS   A 1 272 ? 4.897   -8.373  -30.157 1 70.17  ? 257 LYS   A CB  1 
ATOM   2033 N  N   . GLU   A 1 273 ? 7.153   -9.632  -32.313 1 64.73  ? 258 GLU   A N   1 
ATOM   2034 C  CA  . GLU   A 1 273 ? 7.843   -10.796 -32.867 1 63.05  ? 258 GLU   A CA  1 
ATOM   2035 C  C   . GLU   A 1 273 ? 8.2     -11.812 -31.783 1 62.31  ? 258 GLU   A C   1 
ATOM   2036 O  O   . GLU   A 1 273 ? 8.894   -11.471 -30.818 1 63.45  ? 258 GLU   A O   1 
ATOM   2037 C  CB  . GLU   A 1 273 ? 9.157   -10.367 -33.513 1 63.88  ? 258 GLU   A CB  1 
ATOM   2038 C  CG  . GLU   A 1 273 ? 9.009   -9.738  -34.878 1 66.31  ? 258 GLU   A CG  1 
ATOM   2039 C  CD  . GLU   A 1 273 ? 10.294  -9.808  -35.666 1 68.39  ? 258 GLU   A CD  1 
ATOM   2040 O  OE1 . GLU   A 1 273 ? 11.319  -9.305  -35.159 1 68.86  ? 258 GLU   A OE1 1 
ATOM   2041 O  OE2 . GLU   A 1 273 ? 10.286  -10.388 -36.774 1 69.84  ? 258 GLU   A OE2 1 
ATOM   2042 N  N   . PHE   A 1 274 ? 7.789   -13.071 -31.96  1 60.06  ? 259 PHE   A N   1 
ATOM   2043 C  CA  . PHE   A 1 274 ? 8.129   -14.133 -31.026 1 58.12  ? 259 PHE   A CA  1 
ATOM   2044 C  C   . PHE   A 1 274 ? 8.57    -15.34  -31.81  1 56.44  ? 259 PHE   A C   1 
ATOM   2045 O  O   . PHE   A 1 274 ? 7.996   -15.649 -32.856 1 56.75  ? 259 PHE   A O   1 
ATOM   2046 C  CB  . PHE   A 1 274 ? 6.93    -14.505 -30.15  1 58.08  ? 259 PHE   A CB  1 
ATOM   2047 C  CG  . PHE   A 1 274 ? 6.467   -13.389 -29.255 1 58.86  ? 259 PHE   A CG  1 
ATOM   2048 C  CD1 . PHE   A 1 274 ? 7.236   -12.977 -28.184 1 59.88  ? 259 PHE   A CD1 1 
ATOM   2049 C  CD2 . PHE   A 1 274 ? 5.283   -12.722 -29.508 1 59.69  ? 259 PHE   A CD2 1 
ATOM   2050 C  CE1 . PHE   A 1 274 ? 6.816   -11.93  -27.372 1 60.77  ? 259 PHE   A CE1 1 
ATOM   2051 C  CE2 . PHE   A 1 274 ? 4.872   -11.669 -28.703 1 60.43  ? 259 PHE   A CE2 1 
ATOM   2052 C  CZ  . PHE   A 1 274 ? 5.636   -11.282 -27.64  1 60.46  ? 259 PHE   A CZ  1 
ATOM   2053 N  N   . ALA   A 1 275 ? 9.571   -16.045 -31.299 1 54.82  ? 260 ALA   A N   1 
ATOM   2054 C  CA  . ALA   A 1 275 ? 10.105  -17.254 -31.92  1 53.59  ? 260 ALA   A CA  1 
ATOM   2055 C  C   . ALA   A 1 275 ? 9.134   -18.424 -31.751 1 53.2   ? 260 ALA   A C   1 
ATOM   2056 O  O   . ALA   A 1 275 ? 8.455   -18.536 -30.718 1 53.79  ? 260 ALA   A O   1 
ATOM   2057 C  CB  . ALA   A 1 275 ? 11.455  -17.601 -31.303 1 52.84  ? 260 ALA   A CB  1 
ATOM   2058 N  N   . GLY   A 1 276 ? 9.078   -19.292 -32.758 1 51.96  ? 261 GLY   A N   1 
ATOM   2059 C  CA  . GLY   A 1 276 ? 8.205   -20.455 -32.71  1 51.74  ? 261 GLY   A CA  1 
ATOM   2060 C  C   . GLY   A 1 276 ? 8.683   -21.501 -31.729 1 51.85  ? 261 GLY   A C   1 
ATOM   2061 O  O   . GLY   A 1 276 ? 9.833   -21.457 -31.28  1 52.26  ? 261 GLY   A O   1 
ATOM   2062 N  N   . GLY   A 1 277 ? 7.809   -22.459 -31.416 1 51.44  ? 262 GLY   A N   1 
ATOM   2063 C  CA  . GLY   A 1 277 ? 8.102   -23.556 -30.497 1 51.19  ? 262 GLY   A CA  1 
ATOM   2064 C  C   . GLY   A 1 277 ? 9.369   -24.295 -30.858 1 50.87  ? 262 GLY   A C   1 
ATOM   2065 O  O   . GLY   A 1 277 ? 9.575   -24.658 -32.022 1 51.86  ? 262 GLY   A O   1 
ATOM   2066 N  N   . SER   A 1 278 ? 10.26   -24.434 -29.892 1 49.75  ? 263 SER   A N   1 
ATOM   2067 C  CA  . SER   A 1 278 ? 11.542  -25.059 -30.138 1 49.41  ? 263 SER   A CA  1 
ATOM   2068 C  C   . SER   A 1 278 ? 11.982  -26.014 -29.06  1 48.47  ? 263 SER   A C   1 
ATOM   2069 O  O   . SER   A 1 278 ? 11.83   -25.71  -27.883 1 48.81  ? 263 SER   A O   1 
ATOM   2070 C  CB  . SER   A 1 278 ? 12.612  -23.989 -30.326 1 50.86  ? 263 SER   A CB  1 
ATOM   2071 O  OG  . SER   A 1 278 ? 13.878  -24.565 -30.603 1 53.82  ? 263 SER   A OG  1 
ATOM   2072 N  N   . ALA   A 1 279 ? 12.626  -27.123 -29.453 1 47.07  ? 264 ALA   A N   1 
ATOM   2073 C  CA  . ALA   A 1 279 ? 13.234  -28.013 -28.475 1 46.14  ? 264 ALA   A CA  1 
ATOM   2074 C  C   . ALA   A 1 279 ? 14.457  -27.329 -27.781 1 46.42  ? 264 ALA   A C   1 
ATOM   2075 O  O   . ALA   A 1 279 ? 14.874  -27.764 -26.717 1 46.59  ? 264 ALA   A O   1 
ATOM   2076 C  CB  . ALA   A 1 279 ? 13.61   -29.313 -29.112 1 45.33  ? 264 ALA   A CB  1 
ATOM   2077 N  N   . GLY   A 1 280 ? 14.938  -26.205 -28.326 1 46.21  ? 265 GLY   A N   1 
ATOM   2078 C  CA  . GLY   A 1 280 ? 15.942  -25.365 -27.688 1 46.5   ? 265 GLY   A CA  1 
ATOM   2079 C  C   . GLY   A 1 280 ? 15.404  -24.696 -26.424 1 46.61  ? 265 GLY   A C   1 
ATOM   2080 O  O   . GLY   A 1 280 ? 16.172  -24.092 -25.668 1 46.4   ? 265 GLY   A O   1 
ATOM   2081 N  N   . GLN   A 1 281 ? 14.058  -24.804 -26.183 1 46.09  ? 266 GLN   A N   1 
ATOM   2082 C  CA  . GLN   A 1 281 ? 13.354  -24.337 -24.991 1 45.91  ? 266 GLN   A CA  1 
ATOM   2083 C  C   . GLN   A 1 281 ? 13.239  -25.46  -23.939 1 45.84  ? 266 GLN   A C   1 
ATOM   2084 O  O   . GLN   A 1 281 ? 12.603  -25.236 -22.91  1 46.95  ? 266 GLN   A O   1 
ATOM   2085 C  CB  . GLN   A 1 281 ? 11.932  -23.838 -25.334 1 46.67  ? 266 GLN   A CB  1 
ATOM   2086 C  CG  . GLN   A 1 281 ? 11.887  -22.646 -26.266 1 48.09  ? 266 GLN   A CG  1 
ATOM   2087 C  CD  . GLN   A 1 281 ? 10.562  -22.457 -26.966 1 50.73  ? 266 GLN   A CD  1 
ATOM   2088 O  OE1 . GLN   A 1 281 ? 9.64    -23.272 -26.861 1 51.64  ? 266 GLN   A OE1 1 
ATOM   2089 N  NE2 . GLN   A 1 281 ? 10.447  -21.387 -27.756 1 51.48  ? 266 GLN   A NE2 1 
ATOM   2090 N  N   . SER   A 1 282 ? 13.789  -26.663 -24.202 1 44.5   ? 267 SER   A N   1 
ATOM   2091 C  CA  . SER   A 1 282 ? 13.775  -27.767 -23.264 1 44.69  ? 267 SER   A CA  1 
ATOM   2092 C  C   . SER   A 1 282 ? 14.75   -27.464 -22.128 1 45.4   ? 267 SER   A C   1 
ATOM   2093 O  O   . SER   A 1 282 ? 15.926  -27.178 -22.376 1 45.21  ? 267 SER   A O   1 
ATOM   2094 C  CB  . SER   A 1 282 ? 14.163  -29.063 -23.969 1 45.31  ? 267 SER   A CB  1 
ATOM   2095 O  OG  . SER   A 1 282 ? 14.518  -30.094 -23.061 1 47     ? 267 SER   A OG  1 
ATOM   2096 N  N   . SER   A 1 283 ? 14.268  -27.521 -20.887 1 46.07  ? 268 SER   A N   1 
ATOM   2097 C  CA  . SER   A 1 283 ? 15.119  -27.234 -19.732 1 46.85  ? 268 SER   A CA  1 
ATOM   2098 C  C   . SER   A 1 283 ? 16.036  -28.397 -19.385 1 47.15  ? 268 SER   A C   1 
ATOM   2099 O  O   . SER   A 1 283 ? 17.087  -28.162 -18.804 1 48.09  ? 268 SER   A O   1 
ATOM   2100 C  CB  . SER   A 1 283 ? 14.273  -26.892 -18.511 1 48.03  ? 268 SER   A CB  1 
ATOM   2101 O  OG  . SER   A 1 283 ? 13.478  -25.745 -18.742 1 51.15  ? 268 SER   A OG  1 
ATOM   2102 N  N   . VAL   A 1 284 ? 15.648  -29.636 -19.716 1 46.29  ? 269 VAL   A N   1 
ATOM   2103 C  CA  . VAL   A 1 284 ? 16.433  -30.802 -19.342 1 46.14  ? 269 VAL   A CA  1 
ATOM   2104 C  C   . VAL   A 1 284 ? 17.761  -30.848 -20.08  1 45.71  ? 269 VAL   A C   1 
ATOM   2105 O  O   . VAL   A 1 284 ? 18.785  -31.061 -19.438 1 45.42  ? 269 VAL   A O   1 
ATOM   2106 C  CB  . VAL   A 1 284 ? 15.633  -32.124 -19.428 1 46.35  ? 269 VAL   A CB  1 
ATOM   2107 C  CG1 . VAL   A 1 284 ? 15.426  -32.601 -20.856 1 46.34  ? 269 VAL   A CG1 1 
ATOM   2108 C  CG2 . VAL   A 1 284 ? 16.221  -33.194 -18.53  1 47.08  ? 269 VAL   A CG2 1 
ATOM   2109 N  N   . PHE   A 1 285 ? 17.767  -30.551 -21.378 1 45.65  ? 270 PHE   A N   1 
ATOM   2110 C  CA  . PHE   A 1 285 ? 19.003  -30.539 -22.144 1 45.97  ? 270 PHE   A CA  1 
ATOM   2111 C  C   . PHE   A 1 285 ? 19.877  -29.365 -21.783 1 45.54  ? 270 PHE   A C   1 
ATOM   2112 O  O   . PHE   A 1 285 ? 21.1    -29.518 -21.691 1 45.73  ? 270 PHE   A O   1 
ATOM   2113 C  CB  . PHE   A 1 285 ? 18.742  -30.63  -23.641 1 46.75  ? 270 PHE   A CB  1 
ATOM   2114 C  CG  . PHE   A 1 285 ? 18.261  -32.012 -24.001 1 48.87  ? 270 PHE   A CG  1 
ATOM   2115 C  CD1 . PHE   A 1 285 ? 16.906  -32.308 -24.032 1 49.9   ? 270 PHE   A CD1 1 
ATOM   2116 C  CD2 . PHE   A 1 285 ? 19.162  -33.024 -24.287 1 50.39  ? 270 PHE   A CD2 1 
ATOM   2117 C  CE1 . PHE   A 1 285 ? 16.461  -33.585 -24.349 1 50.77  ? 270 PHE   A CE1 1 
ATOM   2118 C  CE2 . PHE   A 1 285 ? 18.711  -34.309 -24.588 1 51.42  ? 270 PHE   A CE2 1 
ATOM   2119 C  CZ  . PHE   A 1 285 ? 17.365  -34.577 -24.623 1 50.91  ? 270 PHE   A CZ  1 
ATOM   2120 N  N   . GLN   A 1 286 ? 19.263  -28.208 -21.521 1 44.73  ? 271 GLN   A N   1 
ATOM   2121 C  CA  . GLN   A 1 286 ? 20.036  -27.041 -21.13  1 44.3   ? 271 GLN   A CA  1 
ATOM   2122 C  C   . GLN   A 1 286 ? 20.659  -27.243 -19.749 1 44.46  ? 271 GLN   A C   1 
ATOM   2123 O  O   . GLN   A 1 286 ? 21.801  -26.863 -19.54  1 43.53  ? 271 GLN   A O   1 
ATOM   2124 C  CB  . GLN   A 1 286 ? 19.185  -25.765 -21.186 1 44.51  ? 271 GLN   A CB  1 
ATOM   2125 C  CG  . GLN   A 1 286 ? 18.922  -25.317 -22.604 1 45.24  ? 271 GLN   A CG  1 
ATOM   2126 C  CD  . GLN   A 1 286 ? 18.909  -23.818 -22.734 1 46.83  ? 271 GLN   A CD  1 
ATOM   2127 O  OE1 . GLN   A 1 286 ? 19.626  -23.112 -22.022 1 46.69  ? 271 GLN   A OE1 1 
ATOM   2128 N  NE2 . GLN   A 1 286 ? 18.097  -23.299 -23.667 1 46.88  ? 271 GLN   A NE2 1 
ATOM   2129 N  N   . CYS   A 1 287 ? 19.941  -27.904 -18.835 1 45.81  ? 272 CYS   A N   1 
ATOM   2130 C  CA  . CYS   A 1 287 ? 20.442  -28.1   -17.489 1 47.29  ? 272 CYS   A CA  1 
ATOM   2131 C  C   . CYS   A 1 287 ? 21.623  -29.076 -17.426 1 47.42  ? 272 CYS   A C   1 
ATOM   2132 O  O   . CYS   A 1 287 ? 22.488  -28.892 -16.579 1 47.1   ? 272 CYS   A O   1 
ATOM   2133 C  CB  . CYS   A 1 287 ? 19.316  -28.448 -16.517 1 49.27  ? 272 CYS   A CB  1 
ATOM   2134 S  SG  . CYS   A 1 287 ? 19.145  -30.201 -16.11  1 55.04  ? 272 CYS   A SG  1 
ATOM   2135 N  N   . PHE   A 1 288 ? 21.694  -30.059 -18.34  1 47.82  ? 273 PHE   A N   1 
ATOM   2136 C  CA  . PHE   A 1 288 ? 22.826  -30.981 -18.337 1 48.14  ? 273 PHE   A CA  1 
ATOM   2137 C  C   . PHE   A 1 288 ? 24.041  -30.342 -18.992 1 47.81  ? 273 PHE   A C   1 
ATOM   2138 O  O   . PHE   A 1 288 ? 25.147  -30.597 -18.534 1 48.43  ? 273 PHE   A O   1 
ATOM   2139 C  CB  . PHE   A 1 288 ? 22.471  -32.367 -18.875 1 48.53  ? 273 PHE   A CB  1 
ATOM   2140 C  CG  . PHE   A 1 288 ? 21.739  -33.102 -17.778 1 49.68  ? 273 PHE   A CG  1 
ATOM   2141 C  CD1 . PHE   A 1 288 ? 22.304  -33.246 -16.522 1 50.8   ? 273 PHE   A CD1 1 
ATOM   2142 C  CD2 . PHE   A 1 288 ? 20.44   -33.53  -17.958 1 50.88  ? 273 PHE   A CD2 1 
ATOM   2143 C  CE1 . PHE   A 1 288 ? 21.602  -33.86  -15.486 1 51.41  ? 273 PHE   A CE1 1 
ATOM   2144 C  CE2 . PHE   A 1 288 ? 19.732  -34.11  -16.915 1 51.7   ? 273 PHE   A CE2 1 
ATOM   2145 C  CZ  . PHE   A 1 288 ? 20.318  -34.269 -15.687 1 51.23  ? 273 PHE   A CZ  1 
ATOM   2146 N  N   . ASP   A 1 289 ? 23.853  -29.418 -19.941 1 46.91  ? 274 ASP   A N   1 
ATOM   2147 C  CA  . ASP   A 1 289 ? 24.959  -28.649 -20.501 1 46.85  ? 274 ASP   A CA  1 
ATOM   2148 C  C   . ASP   A 1 289 ? 25.507  -27.7   -19.43  1 46.76  ? 274 ASP   A C   1 
ATOM   2149 O  O   . ASP   A 1 289 ? 26.716  -27.521 -19.346 1 46.6   ? 274 ASP   A O   1 
ATOM   2150 C  CB  . ASP   A 1 289 ? 24.504  -27.822 -21.703 1 48.48  ? 274 ASP   A CB  1 
ATOM   2151 C  CG  . ASP   A 1 289 ? 24.187  -28.648 -22.923 1 54.9   ? 274 ASP   A CG  1 
ATOM   2152 O  OD1 . ASP   A 1 289 ? 24.849  -29.69  -23.123 1 56.15  ? 274 ASP   A OD1 1 
ATOM   2153 O  OD2 . ASP   A 1 289 ? 23.278  -28.252 -23.685 1 57.95  ? 274 ASP   A OD2 1 
ATOM   2154 N  N   . VAL   A 1 290 ? 24.631  -27.095 -18.615 1 46.93  ? 275 VAL   A N   1 
ATOM   2155 C  CA  . VAL   A 1 290 ? 25.07   -26.208 -17.539 1 47.73  ? 275 VAL   A CA  1 
ATOM   2156 C  C   . VAL   A 1 290 ? 25.817  -27.035 -16.481 1 48.71  ? 275 VAL   A C   1 
ATOM   2157 O  O   . VAL   A 1 290 ? 26.93   -26.681 -16.103 1 49.03  ? 275 VAL   A O   1 
ATOM   2158 C  CB  . VAL   A 1 290 ? 23.898  -25.405 -16.919 1 48.13  ? 275 VAL   A CB  1 
ATOM   2159 C  CG1 . VAL   A 1 290 ? 24.351  -24.699 -15.643 1 48.86  ? 275 VAL   A CG1 1 
ATOM   2160 C  CG2 . VAL   A 1 290 ? 23.322  -24.398 -17.919 1 47.71  ? 275 VAL   A CG2 1 
ATOM   2161 N  N   . LEU   A 1 291 ? 25.23   -28.162 -16.06  1 49.01  ? 276 LEU   A N   1 
ATOM   2162 C  CA  . LEU   A 1 291 ? 25.821  -29.063 -15.074 1 49.83  ? 276 LEU   A CA  1 
ATOM   2163 C  C   . LEU   A 1 291 ? 27.198  -29.541 -15.491 1 50.92  ? 276 LEU   A C   1 
ATOM   2164 O  O   . LEU   A 1 291 ? 28.119  -29.511 -14.678 1 51.95  ? 276 LEU   A O   1 
ATOM   2165 C  CB  . LEU   A 1 291 ? 24.911  -30.278 -14.834 1 49.77  ? 276 LEU   A CB  1 
ATOM   2166 C  CG  . LEU   A 1 291 ? 25.396  -31.251 -13.781 1 50.98  ? 276 LEU   A CG  1 
ATOM   2167 C  CD1 . LEU   A 1 291 ? 25.334  -30.628 -12.402 1 51.63  ? 276 LEU   A CD1 1 
ATOM   2168 C  CD2 . LEU   A 1 291 ? 24.582  -32.519 -13.806 1 51.99  ? 276 LEU   A CD2 1 
ATOM   2169 N  N   . LEU   A 1 292 ? 27.36   -29.946 -16.751 1 50.84  ? 277 LEU   A N   1 
ATOM   2170 C  CA  . LEU   A 1 292 ? 28.642  -30.46  -17.208 1 51.68  ? 277 LEU   A CA  1 
ATOM   2171 C  C   . LEU   A 1 292 ? 29.627  -29.386 -17.707 1 54.12  ? 277 LEU   A C   1 
ATOM   2172 O  O   . LEU   A 1 292 ? 30.703  -29.729 -18.188 1 54.89  ? 277 LEU   A O   1 
ATOM   2173 C  CB  . LEU   A 1 292 ? 28.425  -31.547 -18.252 1 50.92  ? 277 LEU   A CB  1 
ATOM   2174 C  CG  . LEU   A 1 292 ? 27.52   -32.691 -17.779 1 50.94  ? 277 LEU   A CG  1 
ATOM   2175 C  CD1 . LEU   A 1 292 ? 27.084  -33.558 -18.934 1 51.23  ? 277 LEU   A CD1 1 
ATOM   2176 C  CD2 . LEU   A 1 292 ? 28.129  -33.469 -16.617 1 50.3   ? 277 LEU   A CD2 1 
ATOM   2177 N  N   . GLY   A 1 293 ? 29.286  -28.109 -17.56  1 55.02  ? 278 GLY   A N   1 
ATOM   2178 C  CA  . GLY   A 1 293 ? 30.16   -27.025 -17.984 1 56.35  ? 278 GLY   A CA  1 
ATOM   2179 C  C   . GLY   A 1 293 ? 30.328  -26.882 -19.483 1 57.99  ? 278 GLY   A C   1 
ATOM   2180 O  O   . GLY   A 1 293 ? 31.307  -26.3   -19.944 1 58.15  ? 278 GLY   A O   1 
ATOM   2181 N  N   . ILE   A 1 294 ? 29.398  -27.42  -20.259 1 59.45  ? 279 ILE   A N   1 
ATOM   2182 C  CA  . ILE   A 1 294 ? 29.421  -27.288 -21.716 1 61.46  ? 279 ILE   A CA  1 
ATOM   2183 C  C   . ILE   A 1 294 ? 28.844  -25.914 -21.97  1 64.32  ? 279 ILE   A C   1 
ATOM   2184 O  O   . ILE   A 1 294 ? 27.643  -25.717 -21.777 1 65.22  ? 279 ILE   A O   1 
ATOM   2185 C  CB  . ILE   A 1 294 ? 28.55   -28.398 -22.344 1 61.32  ? 279 ILE   A CB  1 
ATOM   2186 C  CG1 . ILE   A 1 294 ? 29.045  -29.783 -21.897 1 61.81  ? 279 ILE   A CG1 1 
ATOM   2187 C  CG2 . ILE   A 1 294 ? 28.518  -28.268 -23.856 1 61.6   ? 279 ILE   A CG2 1 
ATOM   2188 C  CD1 . ILE   A 1 294 ? 28.051  -30.785 -21.976 1 62.88  ? 279 ILE   A CD1 1 
ATOM   2189 N  N   . GLN   A 1 295 ? 29.694  -24.936 -22.275 1 65.82  ? 280 GLN   A N   1 
ATOM   2190 C  CA  . GLN   A 1 295 ? 29.243  -23.551 -22.416 1 67.91  ? 280 GLN   A CA  1 
ATOM   2191 C  C   . GLN   A 1 295 ? 28.487  -23.294 -23.709 1 69.01  ? 280 GLN   A C   1 
ATOM   2192 O  O   . GLN   A 1 295 ? 28.974  -22.582 -24.587 1 69     ? 280 GLN   A O   1 
ATOM   2193 C  CB  . GLN   A 1 295 ? 30.422  -22.588 -22.236 1 70.4   ? 280 GLN   A CB  1 
ATOM   2194 C  CG  . GLN   A 1 295 ? 30.761  -22.35  -20.765 1 75.03  ? 280 GLN   A CG  1 
ATOM   2195 C  CD  . GLN   A 1 295 ? 32.196  -21.934 -20.583 1 82.08  ? 280 GLN   A CD  1 
ATOM   2196 O  OE1 . GLN   A 1 295 ? 33.022  -22.684 -20.05  1 84.71  ? 280 GLN   A OE1 1 
ATOM   2197 N  NE2 . GLN   A 1 295 ? 32.535  -20.731 -21.03  1 83.26  ? 280 GLN   A NE2 1 
ATOM   2198 N  N   . GLN   A 1 296 ? 27.279  -23.865 -23.809 1 69.75  ? 281 GLN   A N   1 
ATOM   2199 C  CA  . GLN   A 1 296 ? 26.415  -23.748 -24.976 1 70.82  ? 281 GLN   A CA  1 
ATOM   2200 C  C   . GLN   A 1 296 ? 25.961  -22.342 -25.19  1 72.47  ? 281 GLN   A C   1 
ATOM   2201 O  O   . GLN   A 1 296 ? 25.827  -21.938 -26.335 1 72.87  ? 281 GLN   A O   1 
ATOM   2202 C  CB  . GLN   A 1 296 ? 25.185  -24.659 -24.862 1 71.31  ? 281 GLN   A CB  1 
ATOM   2203 C  CG  . GLN   A 1 296 ? 25.524  -26.127 -24.879 1 72.96  ? 281 GLN   A CG  1 
ATOM   2204 C  CD  . GLN   A 1 296 ? 25.848  -26.663 -26.243 1 76.42  ? 281 GLN   A CD  1 
ATOM   2205 O  OE1 . GLN   A 1 296 ? 25.987  -25.933 -27.236 1 78.38  ? 281 GLN   A OE1 1 
ATOM   2206 N  NE2 . GLN   A 1 296 ? 25.983  -27.968 -26.318 1 76.52  ? 281 GLN   A NE2 1 
ATOM   2207 N  N   . THR   A 1 297 ? 25.706  -21.599 -24.102 1 73.19  ? 282 THR   A N   1 
ATOM   2208 C  CA  . THR   A 1 297 ? 25.255  -20.216 -24.159 1 74.51  ? 282 THR   A CA  1 
ATOM   2209 C  C   . THR   A 1 297 ? 26.41   -19.184 -24.19  1 75.77  ? 282 THR   A C   1 
ATOM   2210 O  O   . THR   A 1 297 ? 26.143  -17.986 -24.281 1 76.42  ? 282 THR   A O   1 
ATOM   2211 C  CB  . THR   A 1 297 ? 24.268  -19.952 -23.028 1 75.9   ? 282 THR   A CB  1 
ATOM   2212 O  OG1 . THR   A 1 297 ? 24.859  -20.343 -21.784 1 77.35  ? 282 THR   A OG1 1 
ATOM   2213 C  CG2 . THR   A 1 297 ? 22.927  -20.668 -23.245 1 75.99  ? 282 THR   A CG2 1 
ATOM   2214 N  N   . ALA   A 1 298 ? 27.677  -19.634 -24.164 1 76.02  ? 283 ALA   A N   1 
ATOM   2215 C  CA  . ALA   A 1 298 ? 28.834  -18.739 -24.211 1 76.53  ? 283 ALA   A CA  1 
ATOM   2216 C  C   . ALA   A 1 298 ? 29.474  -18.678 -25.602 1 77.14  ? 283 ALA   A C   1 
ATOM   2217 O  O   . ALA   A 1 298 ? 29.427  -19.646 -26.361 1 77.56  ? 283 ALA   A O   1 
ATOM   2218 C  CB  . ALA   A 1 298 ? 29.867  -19.175 -23.189 1 76.49  ? 283 ALA   A CB  1 
ATOM   2219 N  N   . GLY   A 1 300 ? 29.151  -15.841 -27.835 1 75.64  ? 285 GLY   A N   1 
ATOM   2220 C  CA  . GLY   A 1 300 ? 28.798  -14.761 -28.747 1 75.95  ? 285 GLY   A CA  1 
ATOM   2221 C  C   . GLY   A 1 300 ? 28.148  -15.177 -30.056 1 75.95  ? 285 GLY   A C   1 
ATOM   2222 O  O   . GLY   A 1 300 ? 27.544  -14.34  -30.742 1 76.28  ? 285 GLY   A O   1 
ATOM   2223 N  N   . GLY   A 1 301 ? 28.268  -16.461 -30.404 1 75.19  ? 286 GLY   A N   1 
ATOM   2224 C  CA  . GLY   A 1 301 ? 27.729  -17.014 -31.645 1 74.65  ? 286 GLY   A CA  1 
ATOM   2225 C  C   . GLY   A 1 301 ? 26.217  -17.133 -31.699 1 73.65  ? 286 GLY   A C   1 
ATOM   2226 O  O   . GLY   A 1 301 ? 25.546  -17.038 -30.667 1 73.8   ? 286 GLY   A O   1 
ATOM   2227 N  N   . HIS   A 1 302 ? 25.671  -17.363 -32.905 1 72.37  ? 287 HIS   A N   1 
ATOM   2228 C  CA  . HIS   A 1 302 ? 24.225  -17.495 -33.096 1 72     ? 287 HIS   A CA  1 
ATOM   2229 C  C   . HIS   A 1 302 ? 23.595  -18.621 -32.278 1 69.14  ? 287 HIS   A C   1 
ATOM   2230 O  O   . HIS   A 1 302 ? 22.526  -18.416 -31.712 1 68.92  ? 287 HIS   A O   1 
ATOM   2231 C  CB  . HIS   A 1 302 ? 23.874  -17.668 -34.585 1 74.94  ? 287 HIS   A CB  1 
ATOM   2232 C  CG  . HIS   A 1 302 ? 23.866  -16.39  -35.367 1 80.83  ? 287 HIS   A CG  1 
ATOM   2233 N  ND1 . HIS   A 1 302 ? 22.676  -15.743 -35.689 1 83.68  ? 287 HIS   A ND1 1 
ATOM   2234 C  CD2 . HIS   A 1 302 ? 24.903  -15.68  -35.876 1 82.76  ? 287 HIS   A CD2 1 
ATOM   2235 C  CE1 . HIS   A 1 302 ? 23.029  -14.668 -36.38  1 84.49  ? 287 HIS   A CE1 1 
ATOM   2236 N  NE2 . HIS   A 1 302 ? 24.359  -14.59  -36.524 1 84.34  ? 287 HIS   A NE2 1 
ATOM   2237 N  N   . ALA   A 1 303 ? 24.251  -19.798 -32.216 1 66.78  ? 288 ALA   A N   1 
ATOM   2238 C  CA  . ALA   A 1 303 ? 23.771  -20.965 -31.475 1 64.92  ? 288 ALA   A CA  1 
ATOM   2239 C  C   . ALA   A 1 303 ? 23.652  -20.65  -29.986 1 63.15  ? 288 ALA   A C   1 
ATOM   2240 O  O   . ALA   A 1 303 ? 22.651  -20.99  -29.357 1 62.92  ? 288 ALA   A O   1 
ATOM   2241 C  CB  . ALA   A 1 303 ? 24.702  -22.154 -31.699 1 64.74  ? 288 ALA   A CB  1 
ATOM   2242 N  N   . ALA   A 1 304 ? 24.647  -19.947 -29.446 1 61.7   ? 289 ALA   A N   1 
ATOM   2243 C  CA  . ALA   A 1 304 ? 24.694  -19.543 -28.051 1 60.6   ? 289 ALA   A CA  1 
ATOM   2244 C  C   . ALA   A 1 304 ? 23.599  -18.527 -27.736 1 59.15  ? 289 ALA   A C   1 
ATOM   2245 O  O   . ALA   A 1 304 ? 22.959  -18.596 -26.686 1 59.17  ? 289 ALA   A O   1 
ATOM   2246 C  CB  . ALA   A 1 304 ? 26.071  -18.958 -27.741 1 60.69  ? 289 ALA   A CB  1 
ATOM   2247 N  N   . GLN   A 1 305 ? 23.381  -17.586 -28.654 1 57.6   ? 290 GLN   A N   1 
ATOM   2248 C  CA  . GLN   A 1 305 ? 22.385  -16.549 -28.493 1 56.39  ? 290 GLN   A CA  1 
ATOM   2249 C  C   . GLN   A 1 305 ? 20.995  -17.155 -28.542 1 54.39  ? 290 GLN   A C   1 
ATOM   2250 O  O   . GLN   A 1 305 ? 20.163  -16.837 -27.705 1 55.04  ? 290 GLN   A O   1 
ATOM   2251 C  CB  . GLN   A 1 305 ? 22.548  -15.479 -29.586 1 58.71  ? 290 GLN   A CB  1 
ATOM   2252 C  CG  . GLN   A 1 305 ? 21.598  -14.287 -29.422 1 61.78  ? 290 GLN   A CG  1 
ATOM   2253 C  CD  . GLN   A 1 305 ? 21.912  -13.499 -28.161 1 65.08  ? 290 GLN   A CD  1 
ATOM   2254 O  OE1 . GLN   A 1 305 ? 23.073  -13.161 -27.874 1 66.3   ? 290 GLN   A OE1 1 
ATOM   2255 N  NE2 . GLN   A 1 305 ? 20.886  -13.194 -27.382 1 64.6   ? 290 GLN   A NE2 1 
ATOM   2256 N  N   . PHE   A 1 306 ? 20.753  -18.054 -29.48  1 52.07  ? 291 PHE   A N   1 
ATOM   2257 C  CA  . PHE   A 1 306 ? 19.465  -18.712 -29.624 1 50.73  ? 291 PHE   A CA  1 
ATOM   2258 C  C   . PHE   A 1 306 ? 19.068  -19.485 -28.375 1 49.46  ? 291 PHE   A C   1 
ATOM   2259 O  O   . PHE   A 1 306 ? 17.943  -19.344 -27.909 1 50.12  ? 291 PHE   A O   1 
ATOM   2260 C  CB  . PHE   A 1 306 ? 19.464  -19.628 -30.868 1 50.58  ? 291 PHE   A CB  1 
ATOM   2261 C  CG  . PHE   A 1 306 ? 18.183  -20.399 -31.037 1 51.24  ? 291 PHE   A CG  1 
ATOM   2262 C  CD1 . PHE   A 1 306 ? 17.008  -19.753 -31.376 1 52.13  ? 291 PHE   A CD1 1 
ATOM   2263 C  CD2 . PHE   A 1 306 ? 18.139  -21.759 -30.794 1 51.94  ? 291 PHE   A CD2 1 
ATOM   2264 C  CE1 . PHE   A 1 306 ? 15.819  -20.461 -31.501 1 52.83  ? 291 PHE   A CE1 1 
ATOM   2265 C  CE2 . PHE   A 1 306 ? 16.948  -22.462 -30.908 1 52.81  ? 291 PHE   A CE2 1 
ATOM   2266 C  CZ  . PHE   A 1 306 ? 15.798  -21.812 -31.271 1 52.56  ? 291 PHE   A CZ  1 
ATOM   2267 N  N   . LEU   A 1 307 ? 19.977  -20.288 -27.825 1 47.96  ? 292 LEU   A N   1 
ATOM   2268 C  CA  . LEU   A 1 307 ? 19.701  -21.075 -26.637 1 46.85  ? 292 LEU   A CA  1 
ATOM   2269 C  C   . LEU   A 1 307 ? 19.496  -20.214 -25.408 1 47.61  ? 292 LEU   A C   1 
ATOM   2270 O  O   . LEU   A 1 307 ? 18.688  -20.575 -24.548 1 47.58  ? 292 LEU   A O   1 
ATOM   2271 C  CB  . LEU   A 1 307 ? 20.782  -22.126 -26.411 1 46.02  ? 292 LEU   A CB  1 
ATOM   2272 C  CG  . LEU   A 1 307 ? 20.849  -23.204 -27.489 1 46.43  ? 292 LEU   A CG  1 
ATOM   2273 C  CD1 . LEU   A 1 307 ? 22.062  -24.096 -27.306 1 46.12  ? 292 LEU   A CD1 1 
ATOM   2274 C  CD2 . LEU   A 1 307 ? 19.55   -24.01  -27.567 1 46.37  ? 292 LEU   A CD2 1 
ATOM   2275 N  N   . GLN   A 1 308 ? 20.187  -19.064 -25.322 1 48.21  ? 293 GLN   A N   1 
ATOM   2276 C  CA  . GLN   A 1 308 ? 19.991  -18.157 -24.193 1 49.3   ? 293 GLN   A CA  1 
ATOM   2277 C  C   . GLN   A 1 308 ? 18.625  -17.485 -24.327 1 49.25  ? 293 GLN   A C   1 
ATOM   2278 O  O   . GLN   A 1 308 ? 17.868  -17.447 -23.36  1 49.19  ? 293 GLN   A O   1 
ATOM   2279 C  CB  . GLN   A 1 308 ? 21.123  -17.135 -24.102 1 52.44  ? 293 GLN   A CB  1 
ATOM   2280 C  CG  . GLN   A 1 308 ? 21.025  -16.2   -22.899 1 59.26  ? 293 GLN   A CG  1 
ATOM   2281 C  CD  . GLN   A 1 308 ? 21.203  -16.871 -21.542 1 66.99  ? 293 GLN   A CD  1 
ATOM   2282 O  OE1 . GLN   A 1 308 ? 20.464  -16.587 -20.566 1 69.71  ? 293 GLN   A OE1 1 
ATOM   2283 N  NE2 . GLN   A 1 308 ? 22.197  -17.75  -21.43  1 66.71  ? 293 GLN   A NE2 1 
ATOM   2284 N  N   . ASP   A 1 309 ? 18.265  -17.047 -25.545 1 49.22  ? 294 ASP   A N   1 
ATOM   2285 C  CA  . ASP   A 1 309 ? 16.954  -16.439 -25.8   1 49.62  ? 294 ASP   A CA  1 
ATOM   2286 C  C   . ASP   A 1 309 ? 15.826  -17.402 -25.49  1 48.77  ? 294 ASP   A C   1 
ATOM   2287 O  O   . ASP   A 1 309 ? 14.809  -16.992 -24.943 1 49.09  ? 294 ASP   A O   1 
ATOM   2288 C  CB  . ASP   A 1 309 ? 16.819  -15.961 -27.254 1 52.62  ? 294 ASP   A CB  1 
ATOM   2289 C  CG  . ASP   A 1 309 ? 17.708  -14.802 -27.636 1 60.51  ? 294 ASP   A CG  1 
ATOM   2290 O  OD1 . ASP   A 1 309 ? 18.407  -14.268 -26.741 1 62.24  ? 294 ASP   A OD1 1 
ATOM   2291 O  OD2 . ASP   A 1 309 ? 17.73   -14.438 -28.846 1 63.59  ? 294 ASP   A OD2 1 
ATOM   2292 N  N   . MET   A 1 310 ? 16.007  -18.684 -25.808 1 47.95  ? 295 MET   A N   1 
ATOM   2293 C  CA  . MET   A 1 310 ? 14.977  -19.695 -25.563 1 47.28  ? 295 MET   A CA  1 
ATOM   2294 C  C   . MET   A 1 310 ? 14.672  -19.938 -24.091 1 46.72  ? 295 MET   A C   1 
ATOM   2295 O  O   . MET   A 1 310 ? 13.615  -20.467 -23.792 1 46.86  ? 295 MET   A O   1 
ATOM   2296 C  CB  . MET   A 1 310 ? 15.295  -21.001 -26.287 1 47.14  ? 295 MET   A CB  1 
ATOM   2297 C  CG  . MET   A 1 310 ? 15.242  -20.877 -27.789 1 47.73  ? 295 MET   A CG  1 
ATOM   2298 S  SD  . MET   A 1 310 ? 13.659  -20.283 -28.428 1 47.37  ? 295 MET   A SD  1 
ATOM   2299 C  CE  . MET   A 1 310 ? 14.078  -18.566 -28.824 1 42.82  ? 295 MET   A CE  1 
ATOM   2300 N  N   . ARG   A 1 311 ? 15.532  -19.487 -23.18  1 46.68  ? 296 ARG   A N   1 
ATOM   2301 C  CA  . ARG   A 1 311 ? 15.247  -19.563 -21.749 1 47.25  ? 296 ARG   A CA  1 
ATOM   2302 C  C   . ARG   A 1 311 ? 14.08   -18.652 -21.379 1 48.21  ? 296 ARG   A C   1 
ATOM   2303 O  O   . ARG   A 1 311 ? 13.352  -18.972 -20.449 1 49.16  ? 296 ARG   A O   1 
ATOM   2304 C  CB  . ARG   A 1 311 ? 16.469  -19.195 -20.919 1 47.75  ? 296 ARG   A CB  1 
ATOM   2305 C  CG  . ARG   A 1 311 ? 17.606  -20.153 -21.146 1 50.11  ? 296 ARG   A CG  1 
ATOM   2306 C  CD  . ARG   A 1 311 ? 18.659  -19.964 -20.101 1 53.14  ? 296 ARG   A CD  1 
ATOM   2307 N  NE  . ARG   A 1 311 ? 19.789  -20.859 -20.323 1 55.94  ? 296 ARG   A NE  1 
ATOM   2308 C  CZ  . ARG   A 1 311 ? 20.87   -20.912 -19.554 1 57.49  ? 296 ARG   A CZ  1 
ATOM   2309 N  NH1 . ARG   A 1 311 ? 20.99   -20.104 -18.509 1 56.02  ? 296 ARG   A NH1 1 
ATOM   2310 N  NH2 . ARG   A 1 311 ? 21.839  -21.777 -19.824 1 58.06  ? 296 ARG   A NH2 1 
ATOM   2311 N  N   . ARG   A 1 312 ? 13.872  -17.533 -22.108 1 47.84  ? 297 ARG   A N   1 
ATOM   2312 C  CA  . ARG   A 1 312 ? 12.738  -16.632 -21.842 1 47.93  ? 297 ARG   A CA  1 
ATOM   2313 C  C   . ARG   A 1 312 ? 11.385  -17.259 -22.223 1 47.3   ? 297 ARG   A C   1 
ATOM   2314 O  O   . ARG   A 1 312 ? 10.341  -16.783 -21.799 1 47.51  ? 297 ARG   A O   1 
ATOM   2315 C  CB  . ARG   A 1 312 ? 12.945  -15.283 -22.547 1 49.8   ? 297 ARG   A CB  1 
ATOM   2316 N  N   . TYR   A 1 313 ? 11.415  -18.344 -23.005 1 46.7   ? 298 TYR   A N   1 
ATOM   2317 C  CA  . TYR   A 1 313 ? 10.257  -19.111 -23.451 1 45.69  ? 298 TYR   A CA  1 
ATOM   2318 C  C   . TYR   A 1 313 ? 9.993   -20.365 -22.568 1 45.25  ? 298 TYR   A C   1 
ATOM   2319 O  O   . TYR   A 1 313 ? 9.114   -21.171 -22.903 1 45.13  ? 298 TYR   A O   1 
ATOM   2320 C  CB  . TYR   A 1 313 ? 10.471  -19.546 -24.9   1 44.89  ? 298 TYR   A CB  1 
ATOM   2321 C  CG  . TYR   A 1 313 ? 10.502  -18.41  -25.894 1 44.56  ? 298 TYR   A CG  1 
ATOM   2322 C  CD1 . TYR   A 1 313 ? 11.618  -17.596 -26.015 1 45.03  ? 298 TYR   A CD1 1 
ATOM   2323 C  CD2 . TYR   A 1 313 ? 9.439   -18.189 -26.759 1 45.15  ? 298 TYR   A CD2 1 
ATOM   2324 C  CE1 . TYR   A 1 313 ? 11.657  -16.56  -26.935 1 45.86  ? 298 TYR   A CE1 1 
ATOM   2325 C  CE2 . TYR   A 1 313 ? 9.469   -17.158 -27.69  1 45.69  ? 298 TYR   A CE2 1 
ATOM   2326 C  CZ  . TYR   A 1 313 ? 10.581  -16.35  -27.78  1 46.58  ? 298 TYR   A CZ  1 
ATOM   2327 O  OH  . TYR   A 1 313 ? 10.617  -15.333 -28.698 1 48.05  ? 298 TYR   A OH  1 
ATOM   2328 N  N   . MET   A 1 314 ? 10.753  -20.537 -21.459 1 44.26  ? 299 MET   A N   1 
ATOM   2329 C  CA  . MET   A 1 314 ? 10.565  -21.64  -20.518 1 43.89  ? 299 MET   A CA  1 
ATOM   2330 C  C   . MET   A 1 314 ? 9.711   -21.164 -19.349 1 44.01  ? 299 MET   A C   1 
ATOM   2331 O  O   . MET   A 1 314 ? 9.803   -19.99  -18.983 1 44.06  ? 299 MET   A O   1 
ATOM   2332 C  CB  . MET   A 1 314 ? 11.925  -22.066 -19.934 1 43.56  ? 299 MET   A CB  1 
ATOM   2333 C  CG  . MET   A 1 314 ? 12.869  -22.601 -20.935 1 45.01  ? 299 MET   A CG  1 
ATOM   2334 S  SD  . MET   A 1 314 ? 14.466  -22.949 -20.156 1 46.19  ? 299 MET   A SD  1 
ATOM   2335 C  CE  . MET   A 1 314 ? 15.392  -23.483 -21.562 1 36.72  ? 299 MET   A CE  1 
ATOM   2336 N  N   . PRO   A 1 315 ? 9.003   -22.062 -18.614 1 43.95  ? 300 PRO   A N   1 
ATOM   2337 C  CA  . PRO   A 1 315 ? 8.299   -21.611 -17.388 1 44.24  ? 300 PRO   A CA  1 
ATOM   2338 C  C   . PRO   A 1 315 ? 9.262   -20.882 -16.44  1 45.6   ? 300 PRO   A C   1 
ATOM   2339 O  O   . PRO   A 1 315 ? 10.462  -21.18  -16.428 1 45.24  ? 300 PRO   A O   1 
ATOM   2340 C  CB  . PRO   A 1 315 ? 7.767   -22.915 -16.786 1 44.11  ? 300 PRO   A CB  1 
ATOM   2341 C  CG  . PRO   A 1 315 ? 7.621   -23.833 -17.965 1 44.07  ? 300 PRO   A CG  1 
ATOM   2342 C  CD  . PRO   A 1 315 ? 8.806   -23.507 -18.845 1 42.74  ? 300 PRO   A CD  1 
ATOM   2343 N  N   . PRO   A 1 316 ? 8.785   -19.825 -15.755 1 46.67  ? 301 PRO   A N   1 
ATOM   2344 C  CA  . PRO   A 1 316 ? 9.7     -19.016 -14.927 1 46.56  ? 301 PRO   A CA  1 
ATOM   2345 C  C   . PRO   A 1 316 ? 10.479  -19.817 -13.883 1 46.76  ? 301 PRO   A C   1 
ATOM   2346 O  O   . PRO   A 1 316 ? 11.673  -19.579 -13.735 1 47.41  ? 301 PRO   A O   1 
ATOM   2347 C  CB  . PRO   A 1 316 ? 8.787   -17.944 -14.323 1 47.25  ? 301 PRO   A CB  1 
ATOM   2348 C  CG  . PRO   A 1 316 ? 7.379   -18.529 -14.422 1 47.73  ? 301 PRO   A CG  1 
ATOM   2349 C  CD  . PRO   A 1 316 ? 7.397   -19.319 -15.693 1 46.33  ? 301 PRO   A CD  1 
ATOM   2350 N  N   . ALA   A 1 317 ? 9.849   -20.805 -13.228 1 46.26  ? 302 ALA   A N   1 
ATOM   2351 C  CA  . ALA   A 1 317 ? 10.524  -21.642 -12.232 1 46.67  ? 302 ALA   A CA  1 
ATOM   2352 C  C   . ALA   A 1 317 ? 11.679  -22.446 -12.867 1 46.97  ? 302 ALA   A C   1 
ATOM   2353 O  O   . ALA   A 1 317 ? 12.737  -22.616 -12.26  1 47.2   ? 302 ALA   A O   1 
ATOM   2354 C  CB  . ALA   A 1 317 ? 9.523   -22.591 -11.586 1 46.75  ? 302 ALA   A CB  1 
ATOM   2355 N  N   . HIS   A 1 318 ? 11.48   -22.913 -14.102 1 46.25  ? 303 HIS   A N   1 
ATOM   2356 C  CA  . HIS   A 1 318 ? 12.496  -23.685 -14.824 1 45.38  ? 303 HIS   A CA  1 
ATOM   2357 C  C   . HIS   A 1 318 ? 13.637  -22.82  -15.319 1 45.33  ? 303 HIS   A C   1 
ATOM   2358 O  O   . HIS   A 1 318 ? 14.77   -23.267 -15.356 1 45.29  ? 303 HIS   A O   1 
ATOM   2359 C  CB  . HIS   A 1 318 ? 11.85   -24.489 -15.965 1 44.77  ? 303 HIS   A CB  1 
ATOM   2360 C  CG  . HIS   A 1 318 ? 10.749  -25.408 -15.511 1 44.84  ? 303 HIS   A CG  1 
ATOM   2361 N  ND1 . HIS   A 1 318 ? 9.972   -26.083 -16.423 1 45.46  ? 303 HIS   A ND1 1 
ATOM   2362 C  CD2 . HIS   A 1 318 ? 10.332  -25.737 -14.256 1 45     ? 303 HIS   A CD2 1 
ATOM   2363 C  CE1 . HIS   A 1 318 ? 9.119   -26.796 -15.706 1 45.48  ? 303 HIS   A CE1 1 
ATOM   2364 N  NE2 . HIS   A 1 318 ? 9.306   -26.626 -14.401 1 45.31  ? 303 HIS   A NE2 1 
ATOM   2365 N  N   . ARG   A 1 319 ? 13.352  -21.582 -15.657 1 45.97  ? 304 ARG   A N   1 
ATOM   2366 C  CA  . ARG   A 1 319 ? 14.356  -20.614 -16.057 1 47.98  ? 304 ARG   A CA  1 
ATOM   2367 C  C   . ARG   A 1 319 ? 15.234  -20.299 -14.809 1 49.05  ? 304 ARG   A C   1 
ATOM   2368 O  O   . ARG   A 1 319 ? 16.466  -20.276 -14.911 1 49     ? 304 ARG   A O   1 
ATOM   2369 C  CB  . ARG   A 1 319 ? 13.634  -19.356 -16.537 1 50.29  ? 304 ARG   A CB  1 
ATOM   2370 C  CG  . ARG   A 1 319 ? 14.445  -18.47  -17.446 1 55.26  ? 304 ARG   A CG  1 
ATOM   2371 C  CD  . ARG   A 1 319 ? 13.74   -17.141 -17.721 1 59.44  ? 304 ARG   A CD  1 
ATOM   2372 N  NE  . ARG   A 1 319 ? 12.338  -17.317 -18.124 1 62.8   ? 304 ARG   A NE  1 
ATOM   2373 C  CZ  . ARG   A 1 319 ? 11.306  -16.719 -17.529 1 65.71  ? 304 ARG   A CZ  1 
ATOM   2374 N  NH1 . ARG   A 1 319 ? 11.509  -15.896 -16.5   1 66.6   ? 304 ARG   A NH1 1 
ATOM   2375 N  NH2 . ARG   A 1 319 ? 10.063  -16.954 -17.944 1 64.14  ? 304 ARG   A NH2 1 
ATOM   2376 N  N   . ASN   A 1 320 ? 14.582  -20.12  -13.623 1 49.72  ? 305 ASN   A N   1 
ATOM   2377 C  CA  . ASN   A 1 320 ? 15.24   -19.876 -12.336 1 50.79  ? 305 ASN   A CA  1 
ATOM   2378 C  C   . ASN   A 1 320 ? 16.121  -21.067 -11.966 1 51.61  ? 305 ASN   A C   1 
ATOM   2379 O  O   . ASN   A 1 320 ? 17.198  -20.873 -11.423 1 52.08  ? 305 ASN   A O   1 
ATOM   2380 C  CB  . ASN   A 1 320 ? 14.207  -19.631 -11.228 1 52.26  ? 305 ASN   A CB  1 
ATOM   2381 N  N   . PHE   A 1 321 ? 15.668  -22.303 -12.258 1 51.64  ? 306 PHE   A N   1 
ATOM   2382 C  CA  . PHE   A 1 321 ? 16.45   -23.505 -11.994 1 51.66  ? 306 PHE   A CA  1 
ATOM   2383 C  C   . PHE   A 1 321 ? 17.765  -23.479 -12.753 1 51.74  ? 306 PHE   A C   1 
ATOM   2384 O  O   . PHE   A 1 321 ? 18.808  -23.749 -12.158 1 52.46  ? 306 PHE   A O   1 
ATOM   2385 C  CB  . PHE   A 1 321 ? 15.656  -24.783 -12.308 1 51.53  ? 306 PHE   A CB  1 
ATOM   2386 C  CG  . PHE   A 1 321 ? 16.436  -26.035 -11.985 1 52.57  ? 306 PHE   A CG  1 
ATOM   2387 C  CD1 . PHE   A 1 321 ? 16.644  -26.425 -10.671 1 53.48  ? 306 PHE   A CD1 1 
ATOM   2388 C  CD2 . PHE   A 1 321 ? 17.009  -26.79  -12.987 1 53.45  ? 306 PHE   A CD2 1 
ATOM   2389 C  CE1 . PHE   A 1 321 ? 17.369  -27.57  -10.374 1 54.07  ? 306 PHE   A CE1 1 
ATOM   2390 C  CE2 . PHE   A 1 321 ? 17.736  -27.932 -12.685 1 54.18  ? 306 PHE   A CE2 1 
ATOM   2391 C  CZ  . PHE   A 1 321 ? 17.91   -28.314 -11.378 1 53.94  ? 306 PHE   A CZ  1 
ATOM   2392 N  N   . LEU   A 1 322 ? 17.731  -23.142 -14.047 1 51.17  ? 307 LEU   A N   1 
ATOM   2393 C  CA  . LEU   A 1 322 ? 18.947  -23.086 -14.849 1 51.56  ? 307 LEU   A CA  1 
ATOM   2394 C  C   . LEU   A 1 322 ? 19.956  -22.074 -14.34  1 52.12  ? 307 LEU   A C   1 
ATOM   2395 O  O   . LEU   A 1 322 ? 21.155  -22.351 -14.36  1 52.35  ? 307 LEU   A O   1 
ATOM   2396 C  CB  . LEU   A 1 322 ? 18.631  -22.777 -16.318 1 51.71  ? 307 LEU   A CB  1 
ATOM   2397 C  CG  . LEU   A 1 322 ? 17.856  -23.802 -17.088 1 53.05  ? 307 LEU   A CG  1 
ATOM   2398 C  CD1 . LEU   A 1 322 ? 17.736  -23.397 -18.539 1 53.36  ? 307 LEU   A CD1 1 
ATOM   2399 C  CD2 . LEU   A 1 322 ? 18.503  -25.142 -17.002 1 53.64  ? 307 LEU   A CD2 1 
ATOM   2400 N  N   . CYS   A 1 323 ? 19.485  -20.896 -13.924 1 52.4   ? 308 CYS   A N   1 
ATOM   2401 C  CA  . CYS   A 1 323 ? 20.395  -19.866 -13.436 1 53.61  ? 308 CYS   A CA  1 
ATOM   2402 C  C   . CYS   A 1 323 ? 20.986  -20.261 -12.072 1 53.45  ? 308 CYS   A C   1 
ATOM   2403 O  O   . CYS   A 1 323 ? 22.165  -19.992 -11.813 1 53.26  ? 308 CYS   A O   1 
ATOM   2404 C  CB  . CYS   A 1 323 ? 19.745  -18.48  -13.429 1 55.73  ? 308 CYS   A CB  1 
ATOM   2405 S  SG  . CYS   A 1 323 ? 18.586  -18.194 -12.07  1 64.04  ? 308 CYS   A SG  1 
ATOM   2406 N  N   . SER   A 1 324 ? 20.199  -20.971 -11.231 1 52.92  ? 309 SER   A N   1 
ATOM   2407 C  CA  . SER   A 1 324 ? 20.693  -21.488 -9.957  1 52.61  ? 309 SER   A CA  1 
ATOM   2408 C  C   . SER   A 1 324 ? 21.794  -22.507 -10.189 1 52.3   ? 309 SER   A C   1 
ATOM   2409 O  O   . SER   A 1 324 ? 22.768  -22.515 -9.429  1 52.75  ? 309 SER   A O   1 
ATOM   2410 C  CB  . SER   A 1 324 ? 19.569  -22.118 -9.156  1 53.7   ? 309 SER   A CB  1 
ATOM   2411 O  OG  . SER   A 1 324 ? 18.582  -21.137 -8.896  1 56.49  ? 309 SER   A OG  1 
ATOM   2412 N  N   . LEU   A 1 325 ? 21.689  -23.323 -11.252 1 51.27  ? 310 LEU   A N   1 
ATOM   2413 C  CA  . LEU   A 1 325 ? 22.751  -24.265 -11.578 1 51.52  ? 310 LEU   A CA  1 
ATOM   2414 C  C   . LEU   A 1 325 ? 24.028  -23.51  -11.971 1 52.26  ? 310 LEU   A C   1 
ATOM   2415 O  O   . LEU   A 1 325 ? 25.123  -23.926 -11.591 1 53.45  ? 310 LEU   A O   1 
ATOM   2416 C  CB  . LEU   A 1 325 ? 22.336  -25.179 -12.734 1 51.48  ? 310 LEU   A CB  1 
ATOM   2417 C  CG  . LEU   A 1 325 ? 21.374  -26.308 -12.466 1 52.03  ? 310 LEU   A CG  1 
ATOM   2418 C  CD1 . LEU   A 1 325 ? 21.229  -27.14  -13.699 1 52.53  ? 310 LEU   A CD1 1 
ATOM   2419 C  CD2 . LEU   A 1 325 ? 21.837  -27.181 -11.307 1 51.94  ? 310 LEU   A CD2 1 
ATOM   2420 N  N   . GLU   A 1 326 ? 23.895  -22.425 -12.746 1 51.56  ? 311 GLU   A N   1 
ATOM   2421 C  CA  . GLU   A 1 326 ? 25.028  -21.595 -13.146 1 52.03  ? 311 GLU   A CA  1 
ATOM   2422 C  C   . GLU   A 1 326 ? 25.692  -20.9   -11.952 1 52.42  ? 311 GLU   A C   1 
ATOM   2423 O  O   . GLU   A 1 326 ? 26.885  -20.628 -11.983 1 52.65  ? 311 GLU   A O   1 
ATOM   2424 C  CB  . GLU   A 1 326 ? 24.595  -20.549 -14.189 1 53.89  ? 311 GLU   A CB  1 
ATOM   2425 C  CG  . GLU   A 1 326 ? 24.185  -21.166 -15.508 1 57.24  ? 311 GLU   A CG  1 
ATOM   2426 C  CD  . GLU   A 1 326 ? 23.727  -20.174 -16.555 1 61.94  ? 311 GLU   A CD  1 
ATOM   2427 O  OE1 . GLU   A 1 326 ? 23.074  -19.173 -16.183 1 62.46  ? 311 GLU   A OE1 1 
ATOM   2428 O  OE2 . GLU   A 1 326 ? 23.998  -20.414 -17.754 1 64.01  ? 311 GLU   A OE2 1 
ATOM   2429 N  N   . SER   A 1 327 ? 24.919  -20.611 -10.906 1 52.83  ? 312 SER   A N   1 
ATOM   2430 C  CA  . SER   A 1 327 ? 25.408  -19.989 -9.676  1 53.15  ? 312 SER   A CA  1 
ATOM   2431 C  C   . SER   A 1 327 ? 26.262  -20.951 -8.807  1 52.39  ? 312 SER   A C   1 
ATOM   2432 O  O   . SER   A 1 327 ? 27.059  -20.51  -7.985  1 51.96  ? 312 SER   A O   1 
ATOM   2433 C  CB  . SER   A 1 327 ? 24.23   -19.451 -8.873  1 55.04  ? 312 SER   A CB  1 
ATOM   2434 O  OG  . SER   A 1 327 ? 23.644  -18.35  -9.545  1 58.42  ? 312 SER   A OG  1 
ATOM   2435 N  N   . ASN   A 1 328 ? 26.059  -22.255 -8.972  1 52.2   ? 313 ASN   A N   1 
ATOM   2436 C  CA  . ASN   A 1 328 ? 26.763  -23.291 -8.227  1 52.41  ? 313 ASN   A CA  1 
ATOM   2437 C  C   . ASN   A 1 328 ? 28.133  -23.559 -8.833  1 52.51  ? 313 ASN   A C   1 
ATOM   2438 O  O   . ASN   A 1 328 ? 28.371  -23.223 -9.998  1 53.12  ? 313 ASN   A O   1 
ATOM   2439 C  CB  . ASN   A 1 328 ? 25.913  -24.57  -8.168  1 53.47  ? 313 ASN   A CB  1 
ATOM   2440 C  CG  . ASN   A 1 328 ? 24.867  -24.529 -7.094  1 56.28  ? 313 ASN   A CG  1 
ATOM   2441 O  OD1 . ASN   A 1 328 ? 23.792  -23.977 -7.28   1 57.11  ? 313 ASN   A OD1 1 
ATOM   2442 N  ND2 . ASN   A 1 328 ? 25.158  -25.113 -5.945  1 57.31  ? 313 ASN   A ND2 1 
ATOM   2443 N  N   . PRO   A 1 329 ? 29.065  -24.127 -8.04   1 51.88  ? 314 PRO   A N   1 
ATOM   2444 C  CA  . PRO   A 1 329 ? 30.413  -24.391 -8.559  1 51.6   ? 314 PRO   A CA  1 
ATOM   2445 C  C   . PRO   A 1 329 ? 30.436  -25.308 -9.769  1 51.71  ? 314 PRO   A C   1 
ATOM   2446 O  O   . PRO   A 1 329 ? 29.526  -26.117 -9.979  1 51.64  ? 314 PRO   A O   1 
ATOM   2447 C  CB  . PRO   A 1 329 ? 31.127  -25.054 -7.378  1 52.07  ? 314 PRO   A CB  1 
ATOM   2448 C  CG  . PRO   A 1 329 ? 30.361  -24.665 -6.183  1 52.51  ? 314 PRO   A CG  1 
ATOM   2449 C  CD  . PRO   A 1 329 ? 28.94   -24.546 -6.632  1 51.3   ? 314 PRO   A CD  1 
ATOM   2450 N  N   . SER   A 1 330 ? 31.496  -25.162 -10.563 1 51.73  ? 315 SER   A N   1 
ATOM   2451 C  CA  . SER   A 1 330 ? 31.723  -25.919 -11.778 1 52.15  ? 315 SER   A CA  1 
ATOM   2452 C  C   . SER   A 1 330 ? 32.155  -27.351 -11.496 1 52.18  ? 315 SER   A C   1 
ATOM   2453 O  O   . SER   A 1 330 ? 33.221  -27.59  -10.919 1 52.9   ? 315 SER   A O   1 
ATOM   2454 C  CB  . SER   A 1 330 ? 32.761  -25.217 -12.653 1 54.28  ? 315 SER   A CB  1 
ATOM   2455 O  OG  . SER   A 1 330 ? 32.972  -25.874 -13.895 1 58.46  ? 315 SER   A OG  1 
ATOM   2456 N  N   . VAL   A 1 331 ? 31.332  -28.302 -11.942 1 51.39  ? 316 VAL   A N   1 
ATOM   2457 C  CA  . VAL   A 1 331 ? 31.615  -29.724 -11.875 1 50.89  ? 316 VAL   A CA  1 
ATOM   2458 C  C   . VAL   A 1 331 ? 32.813  -30.016 -12.81  1 51.43  ? 316 VAL   A C   1 
ATOM   2459 O  O   . VAL   A 1 331 ? 33.711  -30.771 -12.439 1 51.73  ? 316 VAL   A O   1 
ATOM   2460 C  CB  . VAL   A 1 331 ? 30.353  -30.532 -12.281 1 50.91  ? 316 VAL   A CB  1 
ATOM   2461 C  CG1 . VAL   A 1 331 ? 30.612  -32.039 -12.2   1 51.08  ? 316 VAL   A CG1 1 
ATOM   2462 C  CG2 . VAL   A 1 331 ? 29.143  -30.128 -11.42  1 50.87  ? 316 VAL   A CG2 1 
ATOM   2463 N  N   . ARG   A 1 332 ? 32.847  -29.389 -14.005 1 51.1   ? 317 ARG   A N   1 
ATOM   2464 C  CA  . ARG   A 1 332 ? 33.94   -29.602 -14.94  1 51.35  ? 317 ARG   A CA  1 
ATOM   2465 C  C   . ARG   A 1 332 ? 35.277  -29.127 -14.346 1 52.14  ? 317 ARG   A C   1 
ATOM   2466 O  O   . ARG   A 1 332 ? 36.272  -29.835 -14.456 1 52.57  ? 317 ARG   A O   1 
ATOM   2467 C  CB  . ARG   A 1 332 ? 33.643  -28.899 -16.273 1 51.81  ? 317 ARG   A CB  1 
ATOM   2468 C  CG  . ARG   A 1 332 ? 34.77   -28.994 -17.266 1 52.57  ? 317 ARG   A CG  1 
ATOM   2469 C  CD  . ARG   A 1 332 ? 34.405  -28.315 -18.556 1 54.86  ? 317 ARG   A CD  1 
ATOM   2470 N  NE  . ARG   A 1 332 ? 35.573  -28.151 -19.419 1 57.26  ? 317 ARG   A NE  1 
ATOM   2471 C  CZ  . ARG   A 1 332 ? 36.012  -29.072 -20.269 1 57.91  ? 317 ARG   A CZ  1 
ATOM   2472 N  NH1 . ARG   A 1 332 ? 37.093  -28.844 -21.004 1 57.98  ? 317 ARG   A NH1 1 
ATOM   2473 N  NH2 . ARG   A 1 332 ? 35.369  -30.224 -20.396 1 56.42  ? 317 ARG   A NH2 1 
ATOM   2474 N  N   . GLU   A 1 333 ? 35.305  -27.936 -13.726 1 52.14  ? 318 GLU   A N   1 
ATOM   2475 C  CA  . GLU   A 1 333 ? 36.529  -27.41  -13.132 1 52.03  ? 318 GLU   A CA  1 
ATOM   2476 C  C   . GLU   A 1 333 ? 37.006  -28.313 -11.999 1 52.04  ? 318 GLU   A C   1 
ATOM   2477 O  O   . GLU   A 1 333 ? 38.2    -28.599 -11.909 1 52.58  ? 318 GLU   A O   1 
ATOM   2478 C  CB  . GLU   A 1 333 ? 36.343  -25.966 -12.662 1 53.89  ? 318 GLU   A CB  1 
ATOM   2479 N  N   . PHE   A 1 334 ? 36.069  -28.833 -11.196 1 51.56  ? 319 PHE   A N   1 
ATOM   2480 C  CA  . PHE   A 1 334 ? 36.375  -29.744 -10.098 1 51.31  ? 319 PHE   A CA  1 
ATOM   2481 C  C   . PHE   A 1 334 ? 37.012  -31.024 -10.621 1 51.93  ? 319 PHE   A C   1 
ATOM   2482 O  O   . PHE   A 1 334 ? 37.999  -31.476 -10.063 1 52.12  ? 319 PHE   A O   1 
ATOM   2483 C  CB  . PHE   A 1 334 ? 35.095  -30.082 -9.323  1 50.53  ? 319 PHE   A CB  1 
ATOM   2484 C  CG  . PHE   A 1 334 ? 35.287  -30.855 -8.04   1 50.7   ? 319 PHE   A CG  1 
ATOM   2485 C  CD1 . PHE   A 1 334 ? 35.333  -32.239 -8.044  1 50.99  ? 319 PHE   A CD1 1 
ATOM   2486 C  CD2 . PHE   A 1 334 ? 35.345  -30.199 -6.818  1 51.16  ? 319 PHE   A CD2 1 
ATOM   2487 C  CE1 . PHE   A 1 334 ? 35.497  -32.948 -6.862  1 51.44  ? 319 PHE   A CE1 1 
ATOM   2488 C  CE2 . PHE   A 1 334 ? 35.46   -30.915 -5.634  1 51.54  ? 319 PHE   A CE2 1 
ATOM   2489 C  CZ  . PHE   A 1 334 ? 35.549  -32.284 -5.667  1 51.31  ? 319 PHE   A CZ  1 
ATOM   2490 N  N   . VAL   A 1 335 ? 36.442  -31.615 -11.671 1 52.12  ? 320 VAL   A N   1 
ATOM   2491 C  CA  . VAL   A 1 335 ? 36.949  -32.859 -12.226 1 52.98  ? 320 VAL   A CA  1 
ATOM   2492 C  C   . VAL   A 1 335 ? 38.324  -32.659 -12.854 1 54.14  ? 320 VAL   A C   1 
ATOM   2493 O  O   . VAL   A 1 335 ? 39.221  -33.474 -12.635 1 53.81  ? 320 VAL   A O   1 
ATOM   2494 C  CB  . VAL   A 1 335 ? 35.91   -33.498 -13.18  1 53.1   ? 320 VAL   A CB  1 
ATOM   2495 C  CG1 . VAL   A 1 335 ? 36.52   -34.621 -13.992 1 53.11  ? 320 VAL   A CG1 1 
ATOM   2496 C  CG2 . VAL   A 1 335 ? 34.709  -34.008 -12.388 1 53.61  ? 320 VAL   A CG2 1 
ATOM   2497 N  N   . LEU   A 1 336 ? 38.506  -31.54  -13.569 1 55.28  ? 321 LEU   A N   1 
ATOM   2498 C  CA  . LEU   A 1 336 ? 39.779  -31.199 -14.191 1 56.91  ? 321 LEU   A CA  1 
ATOM   2499 C  C   . LEU   A 1 336 ? 40.867  -31.045 -13.133 1 58.53  ? 321 LEU   A C   1 
ATOM   2500 O  O   . LEU   A 1 336 ? 41.978  -31.533 -13.309 1 59.58  ? 321 LEU   A O   1 
ATOM   2501 C  CB  . LEU   A 1 336 ? 39.643  -29.883 -14.979 1 57.3   ? 321 LEU   A CB  1 
ATOM   2502 C  CG  . LEU   A 1 336 ? 39.162  -30.019 -16.416 1 59.48  ? 321 LEU   A CG  1 
ATOM   2503 C  CD1 . LEU   A 1 336 ? 38.906  -28.658 -17.036 1 60.16  ? 321 LEU   A CD1 1 
ATOM   2504 C  CD2 . LEU   A 1 336 ? 40.163  -30.783 -17.257 1 60.42  ? 321 LEU   A CD2 1 
ATOM   2505 N  N   . SER   A 1 337 ? 40.534  -30.402 -12.012 1 58.58  ? 322 SER   A N   1 
ATOM   2506 C  CA  . SER   A 1 337 ? 41.483  -30.131 -10.943 1 58.73  ? 322 SER   A CA  1 
ATOM   2507 C  C   . SER   A 1 337 ? 41.881  -31.332 -10.086 1 59.77  ? 322 SER   A C   1 
ATOM   2508 O  O   . SER   A 1 337 ? 42.592  -31.115 -9.099  1 60.62  ? 322 SER   A O   1 
ATOM   2509 C  CB  . SER   A 1 337 ? 40.912  -29.051 -10.022 1 58.47  ? 322 SER   A CB  1 
ATOM   2510 O  OG  . SER   A 1 337 ? 39.929  -29.546 -9.125  1 58.68  ? 322 SER   A OG  1 
ATOM   2511 N  N   . LYS   A 1 338 ? 41.379  -32.551 -10.371 1 59.51  ? 323 LYS   A N   1 
ATOM   2512 C  CA  . LYS   A 1 338 ? 41.642  -33.657 -9.46   1 59.96  ? 323 LYS   A CA  1 
ATOM   2513 C  C   . LYS   A 1 338 ? 42.722  -34.647 -9.886  1 60.56  ? 323 LYS   A C   1 
ATOM   2514 O  O   . LYS   A 1 338 ? 43.234  -35.34  -8.991  1 61.34  ? 323 LYS   A O   1 
ATOM   2515 C  CB  . LYS   A 1 338 ? 40.369  -34.417 -9.096  1 61.22  ? 323 LYS   A CB  1 
ATOM   2516 C  CG  . LYS   A 1 338 ? 39.389  -33.619 -8.236  1 65.3   ? 323 LYS   A CG  1 
ATOM   2517 C  CD  . LYS   A 1 338 ? 39.969  -33.041 -6.96   1 69.65  ? 323 LYS   A CD  1 
ATOM   2518 C  CE  . LYS   A 1 338 ? 39.284  -31.741 -6.633  1 74.62  ? 323 LYS   A CE  1 
ATOM   2519 N  NZ  . LYS   A 1 338 ? 39.45   -31.354 -5.205  1 78.08  ? 323 LYS   A NZ  1 
ATOM   2520 N  N   . GLY   A 1 339 ? 43.073  -34.735 -11.182 1 59.25  ? 324 GLY   A N   1 
ATOM   2521 C  CA  . GLY   A 1 339 ? 44.099  -35.687 -11.625 1 58.43  ? 324 GLY   A CA  1 
ATOM   2522 C  C   . GLY   A 1 339 ? 43.722  -37.125 -11.286 1 57.6   ? 324 GLY   A C   1 
ATOM   2523 O  O   . GLY   A 1 339 ? 44.531  -37.918 -10.782 1 58.13  ? 324 GLY   A O   1 
ATOM   2524 N  N   . ASP   A 1 340 ? 42.439  -37.426 -11.496 1 55.79  ? 325 ASP   A N   1 
ATOM   2525 C  CA  . ASP   A 1 340 ? 41.781  -38.673 -11.162 1 54.58  ? 325 ASP   A CA  1 
ATOM   2526 C  C   . ASP   A 1 340 ? 41.183  -39.21  -12.439 1 54.68  ? 325 ASP   A C   1 
ATOM   2527 O  O   . ASP   A 1 340 ? 40.187  -38.666 -12.9   1 55.75  ? 325 ASP   A O   1 
ATOM   2528 C  CB  . ASP   A 1 340 ? 40.652  -38.311 -10.184 1 54.01  ? 325 ASP   A CB  1 
ATOM   2529 C  CG  . ASP   A 1 340 ? 39.969  -39.445 -9.49   1 54.3   ? 325 ASP   A CG  1 
ATOM   2530 O  OD1 . ASP   A 1 340 ? 39.863  -40.526 -10.09  1 53.93  ? 325 ASP   A OD1 1 
ATOM   2531 O  OD2 . ASP   A 1 340 ? 39.517  -39.244 -8.354  1 55.95  ? 325 ASP   A OD2 1 
ATOM   2532 N  N   . ALA   A 1 341 ? 41.766  -40.247 -13.02  1 53.91  ? 326 ALA   A N   1 
ATOM   2533 C  CA  . ALA   A 1 341 ? 41.279  -40.806 -14.281 1 53.89  ? 326 ALA   A CA  1 
ATOM   2534 C  C   . ALA   A 1 341 ? 39.868  -41.362 -14.183 1 54.08  ? 326 ALA   A C   1 
ATOM   2535 O  O   . ALA   A 1 341 ? 39.098  -41.198 -15.118 1 54.35  ? 326 ALA   A O   1 
ATOM   2536 C  CB  . ALA   A 1 341 ? 42.228  -41.879 -14.793 1 53.49  ? 326 ALA   A CB  1 
ATOM   2537 N  N   . GLY   A 1 342 ? 39.539  -41.994 -13.064 1 53.85  ? 327 GLY   A N   1 
ATOM   2538 C  CA  . GLY   A 1 342 ? 38.22   -42.571 -12.853 1 54.66  ? 327 GLY   A CA  1 
ATOM   2539 C  C   . GLY   A 1 342 ? 37.105  -41.543 -12.842 1 55.43  ? 327 GLY   A C   1 
ATOM   2540 O  O   . GLY   A 1 342 ? 36.049  -41.757 -13.442 1 55.67  ? 327 GLY   A O   1 
ATOM   2541 N  N   . LEU   A 1 343 ? 37.343  -40.42  -12.16  1 55.38  ? 328 LEU   A N   1 
ATOM   2542 C  CA  . LEU   A 1 343 ? 36.426  -39.291 -12.063 1 55.38  ? 328 LEU   A CA  1 
ATOM   2543 C  C   . LEU   A 1 343 ? 36.278  -38.624 -13.433 1 54.94  ? 328 LEU   A C   1 
ATOM   2544 O  O   . LEU   A 1 343 ? 35.175  -38.229 -13.807 1 54.91  ? 328 LEU   A O   1 
ATOM   2545 C  CB  . LEU   A 1 343 ? 36.985  -38.296 -11.046 1 55.93  ? 328 LEU   A CB  1 
ATOM   2546 C  CG  . LEU   A 1 343 ? 35.979  -37.436 -10.296 1 58.28  ? 328 LEU   A CG  1 
ATOM   2547 C  CD1 . LEU   A 1 343 ? 34.932  -38.286 -9.565  1 58.51  ? 328 LEU   A CD1 1 
ATOM   2548 C  CD2 . LEU   A 1 343 ? 36.697  -36.507 -9.329  1 59.36  ? 328 LEU   A CD2 1 
ATOM   2549 N  N   . ARG   A 1 344 ? 37.377  -38.531 -14.191 1 54.58  ? 329 ARG   A N   1 
ATOM   2550 C  CA  . ARG   A 1 344 ? 37.356  -37.976 -15.535 1 55.03  ? 329 ARG   A CA  1 
ATOM   2551 C  C   . ARG   A 1 344 ? 36.6    -38.873 -16.484 1 54.93  ? 329 ARG   A C   1 
ATOM   2552 O  O   . ARG   A 1 344 ? 35.932  -38.364 -17.376 1 55.46  ? 329 ARG   A O   1 
ATOM   2553 C  CB  . ARG   A 1 344 ? 38.766  -37.76  -16.067 1 57.33  ? 329 ARG   A CB  1 
ATOM   2554 C  CG  . ARG   A 1 344 ? 39.506  -36.592 -15.423 1 62.35  ? 329 ARG   A CG  1 
ATOM   2555 C  CD  . ARG   A 1 344 ? 40.679  -36.127 -16.278 1 68.5   ? 329 ARG   A CD  1 
ATOM   2556 N  NE  . ARG   A 1 344 ? 41.548  -37.238 -16.681 1 74.29  ? 329 ARG   A NE  1 
ATOM   2557 C  CZ  . ARG   A 1 344 ? 42.582  -37.675 -15.971 1 78.61  ? 329 ARG   A CZ  1 
ATOM   2558 N  NH1 . ARG   A 1 344 ? 42.895  -37.098 -14.816 1 78.96  ? 329 ARG   A NH1 1 
ATOM   2559 N  NH2 . ARG   A 1 344 ? 43.312  -38.695 -16.409 1 78.96  ? 329 ARG   A NH2 1 
ATOM   2560 N  N   . GLU   A 1 345 ? 36.69   -40.201 -16.296 1 54.25  ? 330 GLU   A N   1 
ATOM   2561 C  CA  . GLU   A 1 345 ? 36.004  -41.194 -17.112 1 53.96  ? 330 GLU   A CA  1 
ATOM   2562 C  C   . GLU   A 1 345 ? 34.502  -41.117 -16.881 1 53.61  ? 330 GLU   A C   1 
ATOM   2563 O  O   . GLU   A 1 345 ? 33.748  -41.22  -17.842 1 54.21  ? 330 GLU   A O   1 
ATOM   2564 C  CB  . GLU   A 1 345 ? 36.519  -42.604 -16.805 1 55.88  ? 330 GLU   A CB  1 
ATOM   2565 N  N   . ALA   A 1 346 ? 34.066  -40.914 -15.618 1 52.55  ? 331 ALA   A N   1 
ATOM   2566 C  CA  . ALA   A 1 346 ? 32.653  -40.791 -15.249 1 52     ? 331 ALA   A CA  1 
ATOM   2567 C  C   . ALA   A 1 346 ? 32.075  -39.483 -15.798 1 51.55  ? 331 ALA   A C   1 
ATOM   2568 O  O   . ALA   A 1 346 ? 30.945  -39.464 -16.276 1 51.43  ? 331 ALA   A O   1 
ATOM   2569 C  CB  . ALA   A 1 346 ? 32.495  -40.836 -13.737 1 51.72  ? 331 ALA   A CB  1 
ATOM   2570 N  N   . TYR   A 1 347 ? 32.86   -38.393 -15.745 1 50.95  ? 332 TYR   A N   1 
ATOM   2571 C  CA  . TYR   A 1 347 ? 32.441  -37.098 -16.274 1 50.23  ? 332 TYR   A CA  1 
ATOM   2572 C  C   . TYR   A 1 347 ? 32.27   -37.205 -17.781 1 50.71  ? 332 TYR   A C   1 
ATOM   2573 O  O   . TYR   A 1 347 ? 31.296  -36.693 -18.317 1 51.15  ? 332 TYR   A O   1 
ATOM   2574 C  CB  . TYR   A 1 347 ? 33.466  -36.002 -15.921 1 49.23  ? 332 TYR   A CB  1 
ATOM   2575 C  CG  . TYR   A 1 347 ? 33.237  -34.706 -16.672 1 48.62  ? 332 TYR   A CG  1 
ATOM   2576 C  CD1 . TYR   A 1 347 ? 32.349  -33.754 -16.198 1 48.98  ? 332 TYR   A CD1 1 
ATOM   2577 C  CD2 . TYR   A 1 347 ? 33.878  -34.456 -17.877 1 48.84  ? 332 TYR   A CD2 1 
ATOM   2578 C  CE1 . TYR   A 1 347 ? 32.117  -32.578 -16.899 1 49.68  ? 332 TYR   A CE1 1 
ATOM   2579 C  CE2 . TYR   A 1 347 ? 33.676  -33.276 -18.572 1 49.58  ? 332 TYR   A CE2 1 
ATOM   2580 C  CZ  . TYR   A 1 347 ? 32.781  -32.346 -18.089 1 50.78  ? 332 TYR   A CZ  1 
ATOM   2581 O  OH  . TYR   A 1 347 ? 32.553  -31.188 -18.793 1 53.02  ? 332 TYR   A OH  1 
ATOM   2582 N  N   . ASP   A 1 348 ? 33.219  -37.865 -18.458 1 50.75  ? 333 ASP   A N   1 
ATOM   2583 C  CA  . ASP   A 1 348 ? 33.21   -38.061 -19.904 1 51.28  ? 333 ASP   A CA  1 
ATOM   2584 C  C   . ASP   A 1 348 ? 32.073  -38.968 -20.36  1 51.82  ? 333 ASP   A C   1 
ATOM   2585 O  O   . ASP   A 1 348 ? 31.643  -38.869 -21.501 1 51.8   ? 333 ASP   A O   1 
ATOM   2586 C  CB  . ASP   A 1 348 ? 34.546  -38.632 -20.37  1 52.87  ? 333 ASP   A CB  1 
ATOM   2587 C  CG  . ASP   A 1 348 ? 35.58   -37.599 -20.757 1 58.28  ? 333 ASP   A CG  1 
ATOM   2588 O  OD1 . ASP   A 1 348 ? 35.346  -36.392 -20.502 1 58.3   ? 333 ASP   A OD1 1 
ATOM   2589 O  OD2 . ASP   A 1 348 ? 36.621  -37.992 -21.333 1 61.79  ? 333 ASP   A OD2 1 
ATOM   2590 N  N   . ALA   A 1 349 ? 31.593  -39.86  -19.484 1 51.7   ? 334 ALA   A N   1 
ATOM   2591 C  CA  . ALA   A 1 349 ? 30.49   -40.74  -19.816 1 51.59  ? 334 ALA   A CA  1 
ATOM   2592 C  C   . ALA   A 1 349 ? 29.204  -39.899 -19.995 1 52.13  ? 334 ALA   A C   1 
ATOM   2593 O  O   . ALA   A 1 349 ? 28.405  -40.215 -20.869 1 52.81  ? 334 ALA   A O   1 
ATOM   2594 C  CB  . ALA   A 1 349 ? 30.318  -41.785 -18.729 1 51.1   ? 334 ALA   A CB  1 
ATOM   2595 N  N   . CYS   A 1 350 ? 29.038  -38.816 -19.203 1 51.5   ? 335 CYS   A N   1 
ATOM   2596 C  CA  . CYS   A 1 350 ? 27.914  -37.883 -19.27  1 51.36  ? 335 CYS   A CA  1 
ATOM   2597 C  C   . CYS   A 1 350 ? 27.991  -37.079 -20.569 1 51.61  ? 335 CYS   A C   1 
ATOM   2598 O  O   . CYS   A 1 350 ? 26.995  -36.936 -21.277 1 52.14  ? 335 CYS   A O   1 
ATOM   2599 C  CB  . CYS   A 1 350 ? 27.93   -36.956 -18.061 1 51.13  ? 335 CYS   A CB  1 
ATOM   2600 S  SG  . CYS   A 1 350 ? 27.623  -37.778 -16.485 1 53.34  ? 335 CYS   A SG  1 
ATOM   2601 N  N   . VAL   A 1 351 ? 29.175  -36.544 -20.866 1 50.85  ? 336 VAL   A N   1 
ATOM   2602 C  CA  . VAL   A 1 351 ? 29.417  -35.757 -22.06  1 50.4   ? 336 VAL   A CA  1 
ATOM   2603 C  C   . VAL   A 1 351 ? 29.222  -36.608 -23.309 1 50.69  ? 336 VAL   A C   1 
ATOM   2604 O  O   . VAL   A 1 351 ? 28.483  -36.19  -24.19  1 51.44  ? 336 VAL   A O   1 
ATOM   2605 C  CB  . VAL   A 1 351 ? 30.803  -35.069 -21.997 1 50.28  ? 336 VAL   A CB  1 
ATOM   2606 C  CG1 . VAL   A 1 351 ? 31.062  -34.238 -23.239 1 50.54  ? 336 VAL   A CG1 1 
ATOM   2607 C  CG2 . VAL   A 1 351 ? 30.92   -34.203 -20.75  1 49.97  ? 336 VAL   A CG2 1 
ATOM   2608 N  N   . LYS   A 1 352 ? 29.766  -37.84  -23.336 1 50.26  ? 337 LYS   A N   1 
ATOM   2609 C  CA  . LYS   A 1 352 ? 29.62   -38.787 -24.458 1 49.81  ? 337 LYS   A CA  1 
ATOM   2610 C  C   . LYS   A 1 352 ? 28.159  -39.135 -24.691 1 49.98  ? 337 LYS   A C   1 
ATOM   2611 O  O   . LYS   A 1 352 ? 27.745  -39.21  -25.843 1 50.87  ? 337 LYS   A O   1 
ATOM   2612 C  CB  . LYS   A 1 352 ? 30.434  -40.08  -24.258 1 50.22  ? 337 LYS   A CB  1 
ATOM   2613 N  N   . ALA   A 1 353 ? 27.364  -39.303 -23.624 1 48.44  ? 338 ALA   A N   1 
ATOM   2614 C  CA  . ALA   A 1 353 ? 25.948  -39.611 -23.776 1 47.42  ? 338 ALA   A CA  1 
ATOM   2615 C  C   . ALA   A 1 353 ? 25.184  -38.45  -24.444 1 48.16  ? 338 ALA   A C   1 
ATOM   2616 O  O   . ALA   A 1 353 ? 24.19   -38.676 -25.142 1 48.78  ? 338 ALA   A O   1 
ATOM   2617 C  CB  . ALA   A 1 353 ? 25.347  -39.948 -22.432 1 46.56  ? 338 ALA   A CB  1 
ATOM   2618 N  N   . LEU   A 1 354 ? 25.658  -37.217 -24.251 1 47.81  ? 339 LEU   A N   1 
ATOM   2619 C  CA  . LEU   A 1 354 ? 25.064  -36.048 -24.866 1 47.96  ? 339 LEU   A CA  1 
ATOM   2620 C  C   . LEU   A 1 354 ? 25.493  -35.961 -26.317 1 48.28  ? 339 LEU   A C   1 
ATOM   2621 O  O   . LEU   A 1 354 ? 24.676  -35.644 -27.159 1 47.77  ? 339 LEU   A O   1 
ATOM   2622 C  CB  . LEU   A 1 354 ? 25.426  -34.777 -24.092 1 47.77  ? 339 LEU   A CB  1 
ATOM   2623 C  CG  . LEU   A 1 354 ? 24.54   -34.472 -22.857 1 48.41  ? 339 LEU   A CG  1 
ATOM   2624 C  CD1 . LEU   A 1 354 ? 25.032  -33.251 -22.099 1 49.24  ? 339 LEU   A CD1 1 
ATOM   2625 C  CD2 . LEU   A 1 354 ? 23.085  -34.328 -23.218 1 48.15  ? 339 LEU   A CD2 1 
ATOM   2626 N  N   . VAL   A 1 355 ? 26.762  -36.277 -26.625 1 49.17  ? 340 VAL   A N   1 
ATOM   2627 C  CA  . VAL   A 1 355 ? 27.253  -36.298 -28.007 1 49.87  ? 340 VAL   A CA  1 
ATOM   2628 C  C   . VAL   A 1 355 ? 26.506  -37.391 -28.804 1 50.76  ? 340 VAL   A C   1 
ATOM   2629 O  O   . VAL   A 1 355 ? 26.133  -37.176 -29.952 1 50.83  ? 340 VAL   A O   1 
ATOM   2630 C  CB  . VAL   A 1 355 ? 28.775  -36.518 -28.079 1 50.32  ? 340 VAL   A CB  1 
ATOM   2631 C  CG1 . VAL   A 1 355 ? 29.253  -36.495 -29.522 1 51.33  ? 340 VAL   A CG1 1 
ATOM   2632 C  CG2 . VAL   A 1 355 ? 29.513  -35.477 -27.27  1 50.5   ? 340 VAL   A CG2 1 
ATOM   2633 N  N   . SER   A 1 356 ? 26.251  -38.537 -28.177 1 51.04  ? 341 SER   A N   1 
ATOM   2634 C  CA  . SER   A 1 356 ? 25.532  -39.622 -28.81  1 52.09  ? 341 SER   A CA  1 
ATOM   2635 C  C   . SER   A 1 356 ? 24.101  -39.207 -29.165 1 53.04  ? 341 SER   A C   1 
ATOM   2636 O  O   . SER   A 1 356 ? 23.63   -39.485 -30.283 1 54.19  ? 341 SER   A O   1 
ATOM   2637 C  CB  . SER   A 1 356 ? 25.527  -40.846 -27.902 1 53.79  ? 341 SER   A CB  1 
ATOM   2638 O  OG  . SER   A 1 356 ? 26.849  -41.32  -27.72  1 57.35  ? 341 SER   A OG  1 
ATOM   2639 N  N   . LEU   A 1 357 ? 23.417  -38.526 -28.225 1 51.9   ? 342 LEU   A N   1 
ATOM   2640 C  CA  . LEU   A 1 357 ? 22.053  -38.072 -28.432 1 51.5   ? 342 LEU   A CA  1 
ATOM   2641 C  C   . LEU   A 1 357 ? 22.008  -37.073 -29.579 1 51.18  ? 342 LEU   A C   1 
ATOM   2642 O  O   . LEU   A 1 357 ? 21.175  -37.202 -30.472 1 50.89  ? 342 LEU   A O   1 
ATOM   2643 C  CB  . LEU   A 1 357 ? 21.509  -37.413 -27.151 1 51.6   ? 342 LEU   A CB  1 
ATOM   2644 C  CG  . LEU   A 1 357 ? 20.903  -38.339 -26.139 1 52.73  ? 342 LEU   A CG  1 
ATOM   2645 C  CD1 . LEU   A 1 357 ? 20.84   -37.69  -24.778 1 53.05  ? 342 LEU   A CD1 1 
ATOM   2646 C  CD2 . LEU   A 1 357 ? 19.527  -38.744 -26.568 1 53.5   ? 342 LEU   A CD2 1 
ATOM   2647 N  N   . ARG   A 1 358 ? 22.932  -36.098 -29.568 1 50.98  ? 343 ARG   A N   1 
ATOM   2648 C  CA  . ARG   A 1 358 ? 22.98   -35.036 -30.561 1 51.24  ? 343 ARG   A CA  1 
ATOM   2649 C  C   . ARG   A 1 358 ? 23.386  -35.523 -31.939 1 52.79  ? 343 ARG   A C   1 
ATOM   2650 O  O   . ARG   A 1 358 ? 22.949  -34.948 -32.932 1 53.39  ? 343 ARG   A O   1 
ATOM   2651 C  CB  . ARG   A 1 358 ? 23.863  -33.889 -30.067 1 51.05  ? 343 ARG   A CB  1 
ATOM   2652 C  CG  . ARG   A 1 358 ? 23.254  -33.239 -28.836 1 52.6   ? 343 ARG   A CG  1 
ATOM   2653 C  CD  . ARG   A 1 358 ? 23.931  -31.952 -28.428 1 54.27  ? 343 ARG   A CD  1 
ATOM   2654 N  NE  . ARG   A 1 358 ? 23.04   -31.131 -27.607 1 54.56  ? 343 ARG   A NE  1 
ATOM   2655 C  CZ  . ARG   A 1 358 ? 23.267  -30.801 -26.339 1 54.63  ? 343 ARG   A CZ  1 
ATOM   2656 N  NH1 . ARG   A 1 358 ? 24.379  -31.196 -25.731 1 53.96  ? 343 ARG   A NH1 1 
ATOM   2657 N  NH2 . ARG   A 1 358 ? 22.392  -30.059 -25.674 1 53.65  ? 343 ARG   A NH2 1 
ATOM   2658 N  N   . SER   A 1 359 ? 24.186  -36.591 -32.005 1 53.34  ? 344 SER   A N   1 
ATOM   2659 C  CA  . SER   A 1 359 ? 24.616  -37.195 -33.256 1 54.29  ? 344 SER   A CA  1 
ATOM   2660 C  C   . SER   A 1 359 ? 23.482  -38.029 -33.865 1 55.11  ? 344 SER   A C   1 
ATOM   2661 O  O   . SER   A 1 359 ? 23.311  -38.04  -35.089 1 55.2   ? 344 SER   A O   1 
ATOM   2662 C  CB  . SER   A 1 359 ? 25.835  -38.072 -33.021 1 55.72  ? 344 SER   A CB  1 
ATOM   2663 O  OG  . SER   A 1 359 ? 26.998  -37.268 -33.067 1 58.45  ? 344 SER   A OG  1 
ATOM   2664 N  N   . TYR   A 1 360 ? 22.718  -38.736 -33.014 1 55.31  ? 345 TYR   A N   1 
ATOM   2665 C  CA  . TYR   A 1 360 ? 21.571  -39.494 -33.488 1 56.09  ? 345 TYR   A CA  1 
ATOM   2666 C  C   . TYR   A 1 360 ? 20.491  -38.512 -33.979 1 56     ? 345 TYR   A C   1 
ATOM   2667 O  O   . TYR   A 1 360 ? 19.87   -38.749 -35.018 1 56.58  ? 345 TYR   A O   1 
ATOM   2668 C  CB  . TYR   A 1 360 ? 21.018  -40.38  -32.375 1 56.88  ? 345 TYR   A CB  1 
ATOM   2669 C  CG  . TYR   A 1 360 ? 19.926  -41.31  -32.852 1 58.82  ? 345 TYR   A CG  1 
ATOM   2670 C  CD1 . TYR   A 1 360 ? 20.231  -42.478 -33.541 1 59.92  ? 345 TYR   A CD1 1 
ATOM   2671 C  CD2 . TYR   A 1 360 ? 18.584  -41.018 -32.627 1 60.1   ? 345 TYR   A CD2 1 
ATOM   2672 C  CE1 . TYR   A 1 360 ? 19.23   -43.332 -33.996 1 60.94  ? 345 TYR   A CE1 1 
ATOM   2673 C  CE2 . TYR   A 1 360 ? 17.575  -41.865 -33.077 1 61.16  ? 345 TYR   A CE2 1 
ATOM   2674 C  CZ  . TYR   A 1 360 ? 17.902  -43.021 -33.762 1 62     ? 345 TYR   A CZ  1 
ATOM   2675 O  OH  . TYR   A 1 360 ? 16.907  -43.861 -34.203 1 63.52  ? 345 TYR   A OH  1 
ATOM   2676 N  N   . HIS   A 1 361 ? 20.298  -37.397 -33.245 1 54.63  ? 346 HIS   A N   1 
ATOM   2677 C  CA  . HIS   A 1 361 ? 19.354  -36.35  -33.578 1 53.66  ? 346 HIS   A CA  1 
ATOM   2678 C  C   . HIS   A 1 361 ? 19.671  -35.743 -34.944 1 54.49  ? 346 HIS   A C   1 
ATOM   2679 O  O   . HIS   A 1 361 ? 18.748  -35.504 -35.709 1 54.67  ? 346 HIS   A O   1 
ATOM   2680 C  CB  . HIS   A 1 361 ? 19.389  -35.28  -32.494 1 52.28  ? 346 HIS   A CB  1 
ATOM   2681 C  CG  . HIS   A 1 361 ? 18.442  -34.147 -32.701 1 51.07  ? 346 HIS   A CG  1 
ATOM   2682 N  ND1 . HIS   A 1 361 ? 18.862  -32.953 -33.251 1 52.17  ? 346 HIS   A ND1 1 
ATOM   2683 C  CD2 . HIS   A 1 361 ? 17.138  -34.039 -32.357 1 51.55  ? 346 HIS   A CD2 1 
ATOM   2684 C  CE1 . HIS   A 1 361 ? 17.801  -32.162 -33.24  1 52.6   ? 346 HIS   A CE1 1 
ATOM   2685 N  NE2 . HIS   A 1 361 ? 16.736  -32.775 -32.72  1 52.12  ? 346 HIS   A NE2 1 
ATOM   2686 N  N   . LEU   A 1 362 ? 20.961  -35.541 -35.28  1 54.89  ? 347 LEU   A N   1 
ATOM   2687 C  CA  . LEU   A 1 362 ? 21.372  -34.988 -36.582 1 55.58  ? 347 LEU   A CA  1 
ATOM   2688 C  C   . LEU   A 1 362 ? 20.991  -35.924 -37.737 1 57.18  ? 347 LEU   A C   1 
ATOM   2689 O  O   . LEU   A 1 362 ? 20.661  -35.461 -38.827 1 57.41  ? 347 LEU   A O   1 
ATOM   2690 C  CB  . LEU   A 1 362 ? 22.872  -34.732 -36.603 1 55.37  ? 347 LEU   A CB  1 
ATOM   2691 C  CG  . LEU   A 1 362 ? 23.308  -33.381 -36.089 1 56.81  ? 347 LEU   A CG  1 
ATOM   2692 C  CD1 . LEU   A 1 362 ? 24.767  -33.403 -35.672 1 57.12  ? 347 LEU   A CD1 1 
ATOM   2693 C  CD2 . LEU   A 1 362 ? 23.044  -32.288 -37.116 1 57.45  ? 347 LEU   A CD2 1 
ATOM   2694 N  N   . GLN   A 1 363 ? 21.042  -37.24  -37.493 1 57.99  ? 348 GLN   A N   1 
ATOM   2695 C  CA  . GLN   A 1 363 ? 20.647  -38.239 -38.474 1 59.3   ? 348 GLN   A CA  1 
ATOM   2696 C  C   . GLN   A 1 363 ? 19.13   -38.205 -38.663 1 60.27  ? 348 GLN   A C   1 
ATOM   2697 O  O   . GLN   A 1 363 ? 18.657  -38.366 -39.79  1 61.1   ? 348 GLN   A O   1 
ATOM   2698 C  CB  . GLN   A 1 363 ? 21.109  -39.638 -38.042 1 61.4   ? 348 GLN   A CB  1 
ATOM   2699 C  CG  . GLN   A 1 363 ? 22.591  -39.89  -38.311 1 66.4   ? 348 GLN   A CG  1 
ATOM   2700 C  CD  . GLN   A 1 363 ? 23.17   -40.951 -37.401 1 73.92  ? 348 GLN   A CD  1 
ATOM   2701 O  OE1 . GLN   A 1 363 ? 24.298  -40.824 -36.887 1 76.63  ? 348 GLN   A OE1 1 
ATOM   2702 N  NE2 . GLN   A 1 363 ? 22.41   -42.02  -37.158 1 75.46  ? 348 GLN   A NE2 1 
ATOM   2703 N  N   . ILE   A 1 364 ? 18.368  -37.979 -37.572 1 59.68  ? 349 ILE   A N   1 
ATOM   2704 C  CA  . ILE   A 1 364 ? 16.919  -37.859 -37.607 1 59.67  ? 349 ILE   A CA  1 
ATOM   2705 C  C   . ILE   A 1 364 ? 16.543  -36.599 -38.407 1 59.13  ? 349 ILE   A C   1 
ATOM   2706 O  O   . ILE   A 1 364 ? 15.7    -36.667 -39.291 1 59.49  ? 349 ILE   A O   1 
ATOM   2707 C  CB  . ILE   A 1 364 ? 16.351  -37.818 -36.165 1 60.51  ? 349 ILE   A CB  1 
ATOM   2708 C  CG1 . ILE   A 1 364 ? 16.596  -39.137 -35.411 1 61.53  ? 349 ILE   A CG1 1 
ATOM   2709 C  CG2 . ILE   A 1 364 ? 14.871  -37.461 -36.158 1 61.13  ? 349 ILE   A CG2 1 
ATOM   2710 C  CD1 . ILE   A 1 364 ? 16.075  -40.373 -36.083 1 62.63  ? 349 ILE   A CD1 1 
ATOM   2711 N  N   . VAL   A 1 365 ? 17.206  -35.471 -38.14  1 58.26  ? 350 VAL   A N   1 
ATOM   2712 C  CA  . VAL   A 1 365 ? 16.956  -34.214 -38.842 1 58     ? 350 VAL   A CA  1 
ATOM   2713 C  C   . VAL   A 1 365 ? 17.321  -34.315 -40.34  1 58.28  ? 350 VAL   A C   1 
ATOM   2714 O  O   . VAL   A 1 365 ? 16.701  -33.647 -41.164 1 58.54  ? 350 VAL   A O   1 
ATOM   2715 C  CB  . VAL   A 1 365 ? 17.638  -33.02  -38.119 1 58.4   ? 350 VAL   A CB  1 
ATOM   2716 C  CG1 . VAL   A 1 365 ? 17.501  -31.724 -38.906 1 58.54  ? 350 VAL   A CG1 1 
ATOM   2717 C  CG2 . VAL   A 1 365 ? 17.067  -32.846 -36.718 1 58.97  ? 350 VAL   A CG2 1 
ATOM   2718 N  N   . THR   A 1 366 ? 18.268  -35.193 -40.703 1 57.97  ? 351 THR   A N   1 
ATOM   2719 C  CA  . THR   A 1 366 ? 18.632  -35.424 -42.105 1 58.16  ? 351 THR   A CA  1 
ATOM   2720 C  C   . THR   A 1 366 ? 17.472  -36.172 -42.82  1 57.91  ? 351 THR   A C   1 
ATOM   2721 O  O   . THR   A 1 366 ? 17.067  -35.795 -43.917 1 58.02  ? 351 THR   A O   1 
ATOM   2722 C  CB  . THR   A 1 366 ? 19.941  -36.226 -42.162 1 59.49  ? 351 THR   A CB  1 
ATOM   2723 O  OG1 . THR   A 1 366 ? 20.985  -35.436 -41.592 1 60.57  ? 351 THR   A OG1 1 
ATOM   2724 C  CG2 . THR   A 1 366 ? 20.317  -36.644 -43.572 1 59.74  ? 351 THR   A CG2 1 
ATOM   2725 N  N   . LYS   A 1 367 ? 16.913  -37.187 -42.159 1 57.05  ? 352 LYS   A N   1 
ATOM   2726 C  CA  . LYS   A 1 367 ? 15.818  -37.997 -42.662 1 57.21  ? 352 LYS   A CA  1 
ATOM   2727 C  C   . LYS   A 1 367 ? 14.502  -37.219 -42.751 1 59.38  ? 352 LYS   A C   1 
ATOM   2728 O  O   . LYS   A 1 367 ? 13.746  -37.384 -43.712 1 60.49  ? 352 LYS   A O   1 
ATOM   2729 C  CB  . LYS   A 1 367 ? 15.636  -39.23  -41.74  1 56.46  ? 352 LYS   A CB  1 
ATOM   2730 C  CG  . LYS   A 1 367 ? 14.413  -40.097 -42.03  1 56.9   ? 352 LYS   A CG  1 
ATOM   2731 C  CD  . LYS   A 1 367 ? 14.258  -41.267 -41.053 1 57.92  ? 352 LYS   A CD  1 
ATOM   2732 C  CE  . LYS   A 1 367 ? 12.939  -41.995 -41.219 1 58.52  ? 352 LYS   A CE  1 
ATOM   2733 N  NZ  . LYS   A 1 367 ? 12.751  -43.082 -40.216 1 57.95  ? 352 LYS   A NZ  1 
ATOM   2734 N  N   . TYR   A 1 368 ? 14.207  -36.403 -41.741 1 59.56  ? 353 TYR   A N   1 
ATOM   2735 C  CA  . TYR   A 1 368 ? 12.936  -35.703 -41.644 1 60.09  ? 353 TYR   A CA  1 
ATOM   2736 C  C   . TYR   A 1 368 ? 12.906  -34.29  -42.194 1 61.83  ? 353 TYR   A C   1 
ATOM   2737 O  O   . TYR   A 1 368 ? 11.817  -33.779 -42.419 1 61.94  ? 353 TYR   A O   1 
ATOM   2738 C  CB  . TYR   A 1 368 ? 12.463  -35.69  -40.185 1 59.34  ? 353 TYR   A CB  1 
ATOM   2739 C  CG  . TYR   A 1 368 ? 11.953  -37.032 -39.712 1 59.02  ? 353 TYR   A CG  1 
ATOM   2740 C  CD1 . TYR   A 1 368 ? 12.806  -37.957 -39.131 1 59.53  ? 353 TYR   A CD1 1 
ATOM   2741 C  CD2 . TYR   A 1 368 ? 10.629  -37.393 -39.885 1 59.24  ? 353 TYR   A CD2 1 
ATOM   2742 C  CE1 . TYR   A 1 368 ? 12.354  -39.211 -38.738 1 59.83  ? 353 TYR   A CE1 1 
ATOM   2743 C  CE2 . TYR   A 1 368 ? 10.172  -38.65  -39.519 1 59.91  ? 353 TYR   A CE2 1 
ATOM   2744 C  CZ  . TYR   A 1 368 ? 11.032  -39.552 -38.925 1 60.21  ? 353 TYR   A CZ  1 
ATOM   2745 O  OH  . TYR   A 1 368 ? 10.56   -40.77  -38.504 1 60.85  ? 353 TYR   A OH  1 
ATOM   2746 N  N   . ILE   A 1 369 ? 14.061  -33.626 -42.346 1 63.13  ? 354 ILE   A N   1 
ATOM   2747 C  CA  . ILE   A 1 369 ? 14.077  -32.247 -42.832 1 64.72  ? 354 ILE   A CA  1 
ATOM   2748 C  C   . ILE   A 1 369 ? 14.968  -32.067 -44.061 1 66.75  ? 354 ILE   A C   1 
ATOM   2749 O  O   . ILE   A 1 369 ? 14.506  -31.559 -45.073 1 66.9   ? 354 ILE   A O   1 
ATOM   2750 C  CB  . ILE   A 1 369 ? 14.425  -31.231 -41.709 1 64.78  ? 354 ILE   A CB  1 
ATOM   2751 C  CG1 . ILE   A 1 369 ? 13.366  -31.251 -40.581 1 65.41  ? 354 ILE   A CG1 1 
ATOM   2752 C  CG2 . ILE   A 1 369 ? 14.589  -29.818 -42.285 1 64.95  ? 354 ILE   A CG2 1 
ATOM   2753 C  CD1 . ILE   A 1 369 ? 13.67   -30.362 -39.379 1 66.22  ? 354 ILE   A CD1 1 
ATOM   2754 N  N   . LEU   A 1 370 ? 16.234  -32.462 -43.968 1 68.11  ? 355 LEU   A N   1 
ATOM   2755 C  CA  . LEU   A 1 370 ? 17.194  -32.294 -45.053 1 69.97  ? 355 LEU   A CA  1 
ATOM   2756 C  C   . LEU   A 1 370 ? 16.795  -32.985 -46.352 1 71.25  ? 355 LEU   A C   1 
ATOM   2757 O  O   . LEU   A 1 370 ? 16.805  -32.343 -47.396 1 71.46  ? 355 LEU   A O   1 
ATOM   2758 C  CB  . LEU   A 1 370 ? 18.596  -32.76  -44.624 1 70.52  ? 355 LEU   A CB  1 
ATOM   2759 C  CG  . LEU   A 1 370 ? 19.535  -31.743 -43.983 1 72.66  ? 355 LEU   A CG  1 
ATOM   2760 C  CD1 . LEU   A 1 370 ? 20.927  -32.313 -43.922 1 73.06  ? 355 LEU   A CD1 1 
ATOM   2761 C  CD2 . LEU   A 1 370 ? 19.563  -30.423 -44.751 1 73.9   ? 355 LEU   A CD2 1 
ATOM   2762 N  N   . ILE   A 1 371 ? 16.475  -34.284 -46.296 1 71.85  ? 356 ILE   A N   1 
ATOM   2763 C  CA  . ILE   A 1 371 ? 16.112  -35.057 -47.475 1 73.16  ? 356 ILE   A CA  1 
ATOM   2764 C  C   . ILE   A 1 371 ? 14.757  -34.599 -48.054 1 74.98  ? 356 ILE   A C   1 
ATOM   2765 O  O   . ILE   A 1 371 ? 14.726  -34.259 -49.243 1 74.73  ? 356 ILE   A O   1 
ATOM   2766 C  CB  . ILE   A 1 371 ? 16.208  -36.582 -47.201 1 73.07  ? 356 ILE   A CB  1 
ATOM   2767 C  CG1 . ILE   A 1 371 ? 17.675  -37     -47.058 1 73.3   ? 356 ILE   A CG1 1 
ATOM   2768 C  CG2 . ILE   A 1 371 ? 15.519  -37.395 -48.283 1 73.43  ? 356 ILE   A CG2 1 
ATOM   2769 C  CD1 . ILE   A 1 371 ? 17.851  -38.339 -46.453 1 73.94  ? 356 ILE   A CD1 1 
ATOM   2770 N  N   . PRO   A 1 372 ? 13.67   -34.456 -47.25  1 76.48  ? 357 PRO   A N   1 
ATOM   2771 C  CA  . PRO   A 1 372 ? 12.412  -33.958 -47.825 1 77.65  ? 357 PRO   A CA  1 
ATOM   2772 C  C   . PRO   A 1 372 ? 12.541  -32.592 -48.5   1 79.82  ? 357 PRO   A C   1 
ATOM   2773 O  O   . PRO   A 1 372 ? 11.826  -32.324 -49.458 1 79.99  ? 357 PRO   A O   1 
ATOM   2774 C  CB  . PRO   A 1 372 ? 11.476  -33.908 -46.613 1 77.85  ? 357 PRO   A CB  1 
ATOM   2775 C  CG  . PRO   A 1 372 ? 12.023  -34.91  -45.66  1 77.95  ? 357 PRO   A CG  1 
ATOM   2776 C  CD  . PRO   A 1 372 ? 13.503  -34.783 -45.815 1 76.17  ? 357 PRO   A CD  1 
ATOM   2777 N  N   . ALA   A 1 373 ? 13.465  -31.74  -48.025 1 81.61  ? 358 ALA   A N   1 
ATOM   2778 C  CA  . ALA   A 1 373 ? 13.692  -30.41  -48.61  1 83.81  ? 358 ALA   A CA  1 
ATOM   2779 C  C   . ALA   A 1 373 ? 14.306  -30.491 -50.008 1 86.42  ? 358 ALA   A C   1 
ATOM   2780 O  O   . ALA   A 1 373 ? 14.039  -29.631 -50.854 1 86.41  ? 358 ALA   A O   1 
ATOM   2781 C  CB  . ALA   A 1 373 ? 14.579  -29.569 -47.702 1 83.57  ? 358 ALA   A CB  1 
ATOM   2782 N  N   . SER   A 1 374 ? 15.138  -31.522 -50.237 1 88.25  ? 359 SER   A N   1 
ATOM   2783 C  CA  . SER   A 1 374 ? 15.812  -31.775 -51.51  1 90.26  ? 359 SER   A CA  1 
ATOM   2784 C  C   . SER   A 1 374 ? 14.88   -32.423 -52.551 1 92.03  ? 359 SER   A C   1 
ATOM   2785 O  O   . SER   A 1 374 ? 15.187  -32.371 -53.744 1 92.3   ? 359 SER   A O   1 
ATOM   2786 C  CB  . SER   A 1 374 ? 17.034  -32.662 -51.294 1 91.5   ? 359 SER   A CB  1 
ATOM   2787 O  OG  . SER   A 1 374 ? 16.644  -33.949 -50.839 1 93.75  ? 359 SER   A OG  1 
ATOM   2788 N  N   . GLN   A 1 375 ? 13.762  -33.043 -52.106 1 92.9   ? 360 GLN   A N   1 
ATOM   2789 C  CA  . GLN   A 1 375 ? 12.788  -33.694 -52.987 1 94.11  ? 360 GLN   A CA  1 
ATOM   2790 C  C   . GLN   A 1 375 ? 11.626  -32.735 -53.218 1 95.99  ? 360 GLN   A C   1 
ATOM   2791 O  O   . GLN   A 1 375 ? 10.493  -32.99  -52.807 1 96.1   ? 360 GLN   A O   1 
ATOM   2792 C  CB  . GLN   A 1 375 ? 12.306  -35.015 -52.376 1 94.67  ? 360 GLN   A CB  1 
ATOM   2793 C  CG  . GLN   A 1 375 ? 13.448  -35.935 -51.975 1 96.53  ? 360 GLN   A CG  1 
ATOM   2794 C  CD  . GLN   A 1 375 ? 12.982  -37.224 -51.354 1 99.33  ? 360 GLN   A CD  1 
ATOM   2795 O  OE1 . GLN   A 1 375 ? 11.841  -37.358 -50.899 1 99.91  ? 360 GLN   A OE1 1 
ATOM   2796 N  NE2 . GLN   A 1 375 ? 13.871  -38.205 -51.32  1 99.85  ? 360 GLN   A NE2 1 
ATOM   2797 N  N   . GLN   A 1 376 ? 11.953  -31.594 -53.829 1 97.29  ? 361 GLN   A N   1 
ATOM   2798 C  CA  . GLN   A 1 376 ? 11.014  -30.523 -54.115 1 99.11  ? 361 GLN   A CA  1 
ATOM   2799 C  C   . GLN   A 1 376 ? 11.581  -29.613 -55.207 1 100.64 ? 361 GLN   A C   1 
ATOM   2800 O  O   . GLN   A 1 376 ? 12.77   -29.29  -55.188 1 100.83 ? 361 GLN   A O   1 
ATOM   2801 C  CB  . GLN   A 1 376 ? 10.746  -29.706 -52.84  1 100.77 ? 361 GLN   A CB  1 
ATOM   2802 C  CG  . GLN   A 1 376 ? 9.346   -29.92  -52.276 1 104.09 ? 361 GLN   A CG  1 
ATOM   2803 C  CD  . GLN   A 1 376 ? 9.115   -29.195 -50.973 1 108.35 ? 361 GLN   A CD  1 
ATOM   2804 O  OE1 . GLN   A 1 376 ? 9.908   -28.344 -50.542 1 109.51 ? 361 GLN   A OE1 1 
ATOM   2805 N  NE2 . GLN   A 1 376 ? 8.008   -29.516 -50.317 1 109.09 ? 361 GLN   A NE2 1 
ATOM   2806 N  N   . PRO   A 1 377 ? 10.736  -29.171 -56.157 1 101.53 ? 362 PRO   A N   1 
ATOM   2807 C  CA  . PRO   A 1 377 ? 11.238  -28.283 -57.223 1 102.11 ? 362 PRO   A CA  1 
ATOM   2808 C  C   . PRO   A 1 377 ? 11.431  -26.831 -56.773 1 102.62 ? 362 PRO   A C   1 
ATOM   2809 O  O   . PRO   A 1 377 ? 12.255  -26.104 -57.334 1 102.85 ? 362 PRO   A O   1 
ATOM   2810 C  CB  . PRO   A 1 377 ? 10.174  -28.404 -58.322 1 102.88 ? 362 PRO   A CB  1 
ATOM   2811 C  CG  . PRO   A 1 377 ? 8.914   -28.807 -57.607 1 103.18 ? 362 PRO   A CG  1 
ATOM   2812 C  CD  . PRO   A 1 377 ? 9.297   -29.478 -56.311 1 101.36 ? 362 PRO   A CD  1 
ATOM   2813 N  N   . THR   A 1 397 ? 21.777  -26.112 -44.789 1 80.92  ? 382 THR   A N   1 
ATOM   2814 C  CA  . THR   A 1 397 ? 20.79   -25.308 -44.07  1 81.11  ? 382 THR   A CA  1 
ATOM   2815 C  C   . THR   A 1 397 ? 21.344  -24.716 -42.762 1 80.69  ? 382 THR   A C   1 
ATOM   2816 O  O   . THR   A 1 397 ? 22.331  -25.211 -42.211 1 80.69  ? 382 THR   A O   1 
ATOM   2817 C  CB  . THR   A 1 397 ? 19.495  -26.102 -43.846 1 82.62  ? 382 THR   A CB  1 
ATOM   2818 O  OG1 . THR   A 1 397 ? 19.814  -27.319 -43.175 1 84.21  ? 382 THR   A OG1 1 
ATOM   2819 C  CG2 . THR   A 1 397 ? 18.752  -26.391 -45.134 1 82.86  ? 382 THR   A CG2 1 
ATOM   2820 N  N   . ASP   A 1 398 ? 20.694  -23.647 -42.277 1 79.98  ? 383 ASP   A N   1 
ATOM   2821 C  CA  . ASP   A 1 398 ? 21.053  -22.965 -41.042 1 79.48  ? 383 ASP   A CA  1 
ATOM   2822 C  C   . ASP   A 1 398 ? 20.795  -23.847 -39.837 1 77.77  ? 383 ASP   A C   1 
ATOM   2823 O  O   . ASP   A 1 398 ? 21.583  -23.809 -38.894 1 77.84  ? 383 ASP   A O   1 
ATOM   2824 C  CB  . ASP   A 1 398 ? 20.261  -21.661 -40.907 1 81.91  ? 383 ASP   A CB  1 
ATOM   2825 C  CG  . ASP   A 1 398 ? 21.143  -20.441 -40.927 1 87.93  ? 383 ASP   A CG  1 
ATOM   2826 O  OD1 . ASP   A 1 398 ? 20.817  -19.468 -40.212 1 89.21  ? 383 ASP   A OD1 1 
ATOM   2827 O  OD2 . ASP   A 1 398 ? 22.18   -20.463 -41.648 1 90.07  ? 383 ASP   A OD2 1 
ATOM   2828 N  N   . LEU   A 1 399 ? 19.7    -24.633 -39.853 1 76.22  ? 384 LEU   A N   1 
ATOM   2829 C  CA  . LEU   A 1 399 ? 19.422  -25.519 -38.721 1 75.15  ? 384 LEU   A CA  1 
ATOM   2830 C  C   . LEU   A 1 399 ? 20.436  -26.664 -38.632 1 73.95  ? 384 LEU   A C   1 
ATOM   2831 O  O   . LEU   A 1 399 ? 20.717  -27.131 -37.53  1 73.97  ? 384 LEU   A O   1 
ATOM   2832 C  CB  . LEU   A 1 399 ? 17.983  -26.024 -38.651 1 75.03  ? 384 LEU   A CB  1 
ATOM   2833 C  CG  . LEU   A 1 399 ? 17.415  -26.629 -39.885 1 76.39  ? 384 LEU   A CG  1 
ATOM   2834 C  CD1 . LEU   A 1 399 ? 17.343  -28.141 -39.766 1 76.73  ? 384 LEU   A CD1 1 
ATOM   2835 C  CD2 . LEU   A 1 399 ? 16.037  -26.079 -40.134 1 77.2   ? 384 LEU   A CD2 1 
ATOM   2836 N  N   . MET   A 1 400 ? 21.028  -27.068 -39.763 1 72.55  ? 385 MET   A N   1 
ATOM   2837 C  CA  . MET   A 1 400 ? 22.061  -28.084 -39.751 1 71.58  ? 385 MET   A CA  1 
ATOM   2838 C  C   . MET   A 1 400 ? 23.299  -27.558 -39.049 1 70.11  ? 385 MET   A C   1 
ATOM   2839 O  O   . MET   A 1 400 ? 23.86   -28.252 -38.202 1 70.3   ? 385 MET   A O   1 
ATOM   2840 C  CB  . MET   A 1 400 ? 22.384  -28.53  -41.173 1 72.42  ? 385 MET   A CB  1 
ATOM   2841 C  CG  . MET   A 1 400 ? 22.463  -30.014 -41.311 1 75.22  ? 385 MET   A CG  1 
ATOM   2842 S  SD  . MET   A 1 400 ? 21.119  -30.975 -40.555 1 80.7   ? 385 MET   A SD  1 
ATOM   2843 C  CE  . MET   A 1 400 ? 21.91   -32.497 -40.466 1 78.8   ? 385 MET   A CE  1 
ATOM   2844 N  N   . ASN   A 1 401 ? 23.68   -26.31  -39.352 1 68.57  ? 386 ASN   A N   1 
ATOM   2845 C  CA  . ASN   A 1 401 ? 24.83   -25.662 -38.74  1 67.63  ? 386 ASN   A CA  1 
ATOM   2846 C  C   . ASN   A 1 401 ? 24.604  -25.427 -37.262 1 65.36  ? 386 ASN   A C   1 
ATOM   2847 O  O   . ASN   A 1 401 ? 25.546  -25.567 -36.486 1 65.47  ? 386 ASN   A O   1 
ATOM   2848 C  CB  . ASN   A 1 401 ? 25.129  -24.329 -39.425 1 69.89  ? 386 ASN   A CB  1 
ATOM   2849 C  CG  . ASN   A 1 401 ? 25.548  -24.485 -40.864 1 74.37  ? 386 ASN   A CG  1 
ATOM   2850 O  OD1 . ASN   A 1 401 ? 26.131  -25.513 -41.265 1 75.29  ? 386 ASN   A OD1 1 
ATOM   2851 N  ND2 . ASN   A 1 401 ? 25.249  -23.46  -41.667 1 75.29  ? 386 ASN   A ND2 1 
ATOM   2852 N  N   . PHE   A 1 402 ? 23.366  -25.057 -36.866 1 63.06  ? 387 PHE   A N   1 
ATOM   2853 C  CA  . PHE   A 1 402 ? 23.029  -24.807 -35.462 1 61.03  ? 387 PHE   A CA  1 
ATOM   2854 C  C   . PHE   A 1 402 ? 23.223  -26.091 -34.66  1 59.99  ? 387 PHE   A C   1 
ATOM   2855 O  O   . PHE   A 1 402 ? 23.879  -26.064 -33.619 1 60.13  ? 387 PHE   A O   1 
ATOM   2856 C  CB  . PHE   A 1 402 ? 21.583  -24.256 -35.291 1 59.74  ? 387 PHE   A CB  1 
ATOM   2857 C  CG  . PHE   A 1 402 ? 21.075  -24.346 -33.869 1 59.08  ? 387 PHE   A CG  1 
ATOM   2858 C  CD1 . PHE   A 1 402 ? 21.557  -23.495 -32.893 1 58.96  ? 387 PHE   A CD1 1 
ATOM   2859 C  CD2 . PHE   A 1 402 ? 20.182  -25.342 -33.492 1 59.56  ? 387 PHE   A CD2 1 
ATOM   2860 C  CE1 . PHE   A 1 402 ? 21.149  -23.621 -31.579 1 59.46  ? 387 PHE   A CE1 1 
ATOM   2861 C  CE2 . PHE   A 1 402 ? 19.779  -25.472 -32.172 1 59.84  ? 387 PHE   A CE2 1 
ATOM   2862 C  CZ  . PHE   A 1 402 ? 20.259  -24.608 -31.227 1 59.44  ? 387 PHE   A CZ  1 
ATOM   2863 N  N   . LEU   A 1 403 ? 22.653  -27.202 -35.142 1 58.58  ? 388 LEU   A N   1 
ATOM   2864 C  CA  . LEU   A 1 403 ? 22.741  -28.47  -34.447 1 57.87  ? 388 LEU   A CA  1 
ATOM   2865 C  C   . LEU   A 1 403 ? 24.171  -28.978 -34.41  1 57.3   ? 388 LEU   A C   1 
ATOM   2866 O  O   . LEU   A 1 403 ? 24.608  -29.479 -33.375 1 57.66  ? 388 LEU   A O   1 
ATOM   2867 C  CB  . LEU   A 1 403 ? 21.809  -29.493 -35.096 1 57.95  ? 388 LEU   A CB  1 
ATOM   2868 C  CG  . LEU   A 1 403 ? 20.318  -29.196 -34.97  1 59.26  ? 388 LEU   A CG  1 
ATOM   2869 C  CD1 . LEU   A 1 403 ? 19.501  -30.183 -35.786 1 59.95  ? 388 LEU   A CD1 1 
ATOM   2870 C  CD2 . LEU   A 1 403 ? 19.87   -29.199 -33.509 1 59.71  ? 388 LEU   A CD2 1 
ATOM   2871 N  N   . LYS   A 1 404 ? 24.916  -28.806 -35.514 1 56.52  ? 389 LYS   A N   1 
ATOM   2872 C  CA  . LYS   A 1 404 ? 26.314  -29.227 -35.598 1 55.95  ? 389 LYS   A CA  1 
ATOM   2873 C  C   . LYS   A 1 404 ? 27.194  -28.416 -34.661 1 55.21  ? 389 LYS   A C   1 
ATOM   2874 O  O   . LYS   A 1 404 ? 28.126  -28.971 -34.097 1 56.23  ? 389 LYS   A O   1 
ATOM   2875 C  CB  . LYS   A 1 404 ? 26.839  -29.147 -37.033 1 57.43  ? 389 LYS   A CB  1 
ATOM   2876 C  CG  . LYS   A 1 404 ? 26.393  -30.291 -37.925 1 60.97  ? 389 LYS   A CG  1 
ATOM   2877 C  CD  . LYS   A 1 404 ? 27.158  -30.219 -39.232 1 65.74  ? 389 LYS   A CD  1 
ATOM   2878 C  CE  . LYS   A 1 404 ? 26.301  -30.17  -40.474 1 70.52  ? 389 LYS   A CE  1 
ATOM   2879 N  NZ  . LYS   A 1 404 ? 27.117  -29.794 -41.665 1 72.88  ? 389 LYS   A NZ  1 
ATOM   2880 N  N   . THR   A 1 405 ? 26.901  -27.128 -34.477 1 53.65  ? 390 THR   A N   1 
ATOM   2881 C  CA  . THR   A 1 405 ? 27.648  -26.272 -33.556 1 53.17  ? 390 THR   A CA  1 
ATOM   2882 C  C   . THR   A 1 405 ? 27.376  -26.676 -32.119 1 52.18  ? 390 THR   A C   1 
ATOM   2883 O  O   . THR   A 1 405 ? 28.294  -26.68  -31.309 1 52.53  ? 390 THR   A O   1 
ATOM   2884 C  CB  . THR   A 1 405 ? 27.301  -24.805 -33.799 1 54.76  ? 390 THR   A CB  1 
ATOM   2885 O  OG1 . THR   A 1 405 ? 27.772  -24.447 -35.098 1 56.47  ? 390 THR   A OG1 1 
ATOM   2886 C  CG2 . THR   A 1 405 ? 27.888  -23.88  -32.751 1 54.5   ? 390 THR   A CG2 1 
ATOM   2887 N  N   . VAL   A 1 406 ? 26.122  -27.028 -31.8   1 51.13  ? 391 VAL   A N   1 
ATOM   2888 C  CA  . VAL   A 1 406 ? 25.737  -27.475 -30.46  1 50.39  ? 391 VAL   A CA  1 
ATOM   2889 C  C   . VAL   A 1 406 ? 26.403  -28.809 -30.154 1 49.88  ? 391 VAL   A C   1 
ATOM   2890 O  O   . VAL   A 1 406 ? 26.987  -28.977 -29.08  1 49.22  ? 391 VAL   A O   1 
ATOM   2891 C  CB  . VAL   A 1 406 ? 24.198  -27.504 -30.276 1 50.47  ? 391 VAL   A CB  1 
ATOM   2892 C  CG1 . VAL   A 1 406 ? 23.795  -28.298 -29.041 1 50.39  ? 391 VAL   A CG1 1 
ATOM   2893 C  CG2 . VAL   A 1 406 ? 23.64   -26.086 -30.204 1 50.67  ? 391 VAL   A CG2 1 
ATOM   2894 N  N   . ARG   A 1 407 ? 26.398  -29.723 -31.128 1 50.07  ? 392 ARG   A N   1 
ATOM   2895 C  CA  . ARG   A 1 407 ? 27.043  -31.016 -30.958 1 51.02  ? 392 ARG   A CA  1 
ATOM   2896 C  C   . ARG   A 1 407 ? 28.561  -30.885 -30.833 1 51.56  ? 392 ARG   A C   1 
ATOM   2897 O  O   . ARG   A 1 407 ? 29.154  -31.513 -29.968 1 51.65  ? 392 ARG   A O   1 
ATOM   2898 C  CB  . ARG   A 1 407 ? 26.69   -31.965 -32.101 1 52.86  ? 392 ARG   A CB  1 
ATOM   2899 C  CG  . ARG   A 1 407 ? 27.238  -33.363 -31.863 1 56.36  ? 392 ARG   A CG  1 
ATOM   2900 C  CD  . ARG   A 1 407 ? 27.493  -34.096 -33.163 1 60.54  ? 392 ARG   A CD  1 
ATOM   2901 N  NE  . ARG   A 1 407 ? 28.445  -35.192 -32.991 1 64.94  ? 392 ARG   A NE  1 
ATOM   2902 C  CZ  . ARG   A 1 407 ? 29.769  -35.045 -32.957 1 66.4   ? 392 ARG   A CZ  1 
ATOM   2903 N  NH1 . ARG   A 1 407 ? 30.315  -33.837 -33.075 1 65.51  ? 392 ARG   A NH1 1 
ATOM   2904 N  NH2 . ARG   A 1 407 ? 30.556  -36.103 -32.789 1 65.39  ? 392 ARG   A NH2 1 
ATOM   2905 N  N   . SER   A 1 408 ? 29.178  -30.045 -31.659 1 52.28  ? 393 SER   A N   1 
ATOM   2906 C  CA  . SER   A 1 408 ? 30.621  -29.799 -31.641 1 53.72  ? 393 SER   A CA  1 
ATOM   2907 C  C   . SER   A 1 408 ? 31.06   -29.249 -30.276 1 53.99  ? 393 SER   A C   1 
ATOM   2908 O  O   . SER   A 1 408 ? 32.081  -29.684 -29.746 1 54.27  ? 393 SER   A O   1 
ATOM   2909 C  CB  . SER   A 1 408 ? 31.006  -28.839 -32.773 1 56.2   ? 393 SER   A CB  1 
ATOM   2910 O  OG  . SER   A 1 408 ? 32.182  -28.071 -32.55  1 59.97  ? 393 SER   A OG  1 
ATOM   2911 N  N   . THR   A 1 409 ? 30.284  -28.308 -29.711 1 53.51  ? 394 THR   A N   1 
ATOM   2912 C  CA  . THR   A 1 409 ? 30.562  -27.724 -28.404 1 53.79  ? 394 THR   A CA  1 
ATOM   2913 C  C   . THR   A 1 409 ? 30.521  -28.804 -27.322 1 54.78  ? 394 THR   A C   1 
ATOM   2914 O  O   . THR   A 1 409 ? 31.311  -28.763 -26.39  1 55.32  ? 394 THR   A O   1 
ATOM   2915 C  CB  . THR   A 1 409 ? 29.562  -26.597 -28.128 1 54.53  ? 394 THR   A CB  1 
ATOM   2916 O  OG1 . THR   A 1 409 ? 29.635  -25.643 -29.189 1 55.26  ? 394 THR   A OG1 1 
ATOM   2917 C  CG2 . THR   A 1 409 ? 29.791  -25.909 -26.781 1 54.42  ? 394 THR   A CG2 1 
ATOM   2918 N  N   . THR   A 1 410 ? 29.623  -29.792 -27.458 1 54.86  ? 395 THR   A N   1 
ATOM   2919 C  CA  . THR   A 1 410 ? 29.526  -30.889 -26.505 1 54.63  ? 395 THR   A CA  1 
ATOM   2920 C  C   . THR   A 1 410 ? 30.733  -31.795 -26.647 1 55.28  ? 395 THR   A C   1 
ATOM   2921 O  O   . THR   A 1 410 ? 31.309  -32.201 -25.647 1 55.54  ? 395 THR   A O   1 
ATOM   2922 C  CB  . THR   A 1 410 ? 28.238  -31.696 -26.714 1 54.52  ? 395 THR   A CB  1 
ATOM   2923 O  OG1 . THR   A 1 410 ? 27.126  -30.821 -26.85  1 54.92  ? 395 THR   A OG1 1 
ATOM   2924 C  CG2 . THR   A 1 410 ? 27.99   -32.671 -25.585 1 54.43  ? 395 THR   A CG2 1 
ATOM   2925 N  N   . GLU   A 1 411 ? 31.12   -32.115 -27.886 1 55.22  ? 396 GLU   A N   1 
ATOM   2926 C  CA  . GLU   A 1 411 ? 32.243  -32.994 -28.151 1 55.24  ? 396 GLU   A CA  1 
ATOM   2927 C  C   . GLU   A 1 411 ? 33.548  -32.401 -27.643 1 54.93  ? 396 GLU   A C   1 
ATOM   2928 O  O   . GLU   A 1 411 ? 34.339  -33.093 -27.01  1 54.65  ? 396 GLU   A O   1 
ATOM   2929 C  CB  . GLU   A 1 411 ? 32.314  -33.329 -29.645 1 57.61  ? 396 GLU   A CB  1 
ATOM   2930 C  CG  . GLU   A 1 411 ? 32.986  -34.663 -29.916 1 63.25  ? 396 GLU   A CG  1 
ATOM   2931 C  CD  . GLU   A 1 411 ? 34.483  -34.559 -30.122 1 70.31  ? 396 GLU   A CD  1 
ATOM   2932 O  OE1 . GLU   A 1 411 ? 34.945  -33.487 -30.58  1 71.71  ? 396 GLU   A OE1 1 
ATOM   2933 O  OE2 . GLU   A 1 411 ? 35.195  -35.545 -29.817 1 72.48  ? 396 GLU   A OE2 1 
ATOM   2934 N  N   . LYS   A 1 412 ? 33.753  -31.115 -27.875 1 55.14  ? 397 LYS   A N   1 
ATOM   2935 C  CA  . LYS   A 1 412 ? 34.964  -30.425 -27.449 1 55.79  ? 397 LYS   A CA  1 
ATOM   2936 C  C   . LYS   A 1 412 ? 35.101  -30.293 -25.924 1 56.4   ? 397 LYS   A C   1 
ATOM   2937 O  O   . LYS   A 1 412 ? 36.177  -29.928 -25.453 1 57.66  ? 397 LYS   A O   1 
ATOM   2938 C  CB  . LYS   A 1 412 ? 35.079  -29.067 -28.143 1 57.65  ? 397 LYS   A CB  1 
ATOM   2939 C  CG  . LYS   A 1 412 ? 35.421  -29.17  -29.619 1 62.51  ? 397 LYS   A CG  1 
ATOM   2940 C  CD  . LYS   A 1 412 ? 35.329  -27.79  -30.303 1 68.81  ? 397 LYS   A CD  1 
ATOM   2941 C  CE  . LYS   A 1 412 ? 35.74   -27.793 -31.76  1 73.37  ? 397 LYS   A CE  1 
ATOM   2942 N  NZ  . LYS   A 1 412 ? 35.035  -28.847 -32.544 1 76.23  ? 397 LYS   A NZ  1 
ATOM   2943 N  N   . SER   A 1 413 ? 34.036  -30.594 -25.153 1 55.44  ? 398 SER   A N   1 
ATOM   2944 C  CA  . SER   A 1 413 ? 34.049  -30.592 -23.687 1 54.91  ? 398 SER   A CA  1 
ATOM   2945 C  C   . SER   A 1 413 ? 34.645  -31.895 -23.105 1 55.35  ? 398 SER   A C   1 
ATOM   2946 O  O   . SER   A 1 413 ? 34.805  -31.987 -21.888 1 55.07  ? 398 SER   A O   1 
ATOM   2947 C  CB  . SER   A 1 413 ? 32.637  -30.435 -23.129 1 54.9   ? 398 SER   A CB  1 
ATOM   2948 O  OG  . SER   A 1 413 ? 32.026  -29.242 -23.569 1 55.67  ? 398 SER   A OG  1 
ATOM   2949 N  N   . LEU   A 1 414 ? 34.904  -32.914 -23.936 1 56.13  ? 399 LEU   A N   1 
ATOM   2950 C  CA  . LEU   A 1 414 ? 35.489  -34.164 -23.466 1 57.59  ? 399 LEU   A CA  1 
ATOM   2951 C  C   . LEU   A 1 414 ? 36.896  -33.908 -22.946 1 59.26  ? 399 LEU   A C   1 
ATOM   2952 O  O   . LEU   A 1 414 ? 37.649  -33.144 -23.551 1 59.47  ? 399 LEU   A O   1 
ATOM   2953 C  CB  . LEU   A 1 414 ? 35.509  -35.208 -24.589 1 57.51  ? 399 LEU   A CB  1 
ATOM   2954 C  CG  . LEU   A 1 414 ? 34.151  -35.839 -24.886 1 58.29  ? 399 LEU   A CG  1 
ATOM   2955 C  CD1 . LEU   A 1 414 ? 34.163  -36.546 -26.202 1 58.53  ? 399 LEU   A CD1 1 
ATOM   2956 C  CD2 . LEU   A 1 414 ? 33.743  -36.797 -23.797 1 58.93  ? 399 LEU   A CD2 1 
ATOM   2957 N  N   . LEU   A 1 415 ? 37.216  -34.466 -21.783 1 60.43  ? 400 LEU   A N   1 
ATOM   2958 C  CA  . LEU   A 1 415 ? 38.531  -34.29  -21.176 1 62.22  ? 400 LEU   A CA  1 
ATOM   2959 C  C   . LEU   A 1 415 ? 39.55   -35.186 -21.899 1 65.74  ? 400 LEU   A C   1 
ATOM   2960 O  O   . LEU   A 1 415 ? 40.669  -34.751 -22.185 1 66.41  ? 400 LEU   A O   1 
ATOM   2961 C  CB  . LEU   A 1 415 ? 38.483  -34.623 -19.684 1 61.37  ? 400 LEU   A CB  1 
ATOM   2962 C  CG  . LEU   A 1 415 ? 37.382  -33.972 -18.881 1 61.78  ? 400 LEU   A CG  1 
ATOM   2963 C  CD1 . LEU   A 1 415 ? 37.401  -34.464 -17.486 1 61.84  ? 400 LEU   A CD1 1 
ATOM   2964 C  CD2 . LEU   A 1 415 ? 37.489  -32.468 -18.905 1 62.2   ? 400 LEU   A CD2 1 
ATOM   2965 N  N   . LYS   A 1 416 ? 39.161  -36.426 -22.186 1 67.56  ? 401 LYS   A N   1 
ATOM   2966 C  CA  . LYS   A 1 416 ? 39.965  -37.357 -22.951 1 70.08  ? 401 LYS   A CA  1 
ATOM   2967 C  C   . LYS   A 1 416 ? 39.059  -37.781 -24.114 1 73.25  ? 401 LYS   A C   1 
ATOM   2968 O  O   . LYS   A 1 416 ? 37.921  -38.226 -23.876 1 73.79  ? 401 LYS   A O   1 
ATOM   2969 C  CB  . LYS   A 1 416 ? 40.373  -38.554 -22.091 1 71.9   ? 401 LYS   A CB  1 
ATOM   2970 N  N   . GLU   A 1 417 ? 39.533  -37.587 -25.374 1 74.76  ? 402 GLU   A N   1 
ATOM   2971 C  CA  . GLU   A 1 417 ? 38.794  -37.888 -26.619 1 76.22  ? 402 GLU   A CA  1 
ATOM   2972 C  C   . GLU   A 1 417 ? 37.961  -39.196 -26.592 1 76.85  ? 402 GLU   A C   1 
ATOM   2973 O  O   . GLU   A 1 417 ? 38.425  -40.241 -26.13  1 77.14  ? 402 GLU   A O   1 
ATOM   2974 C  CB  . GLU   A 1 417 ? 39.73   -37.89  -27.842 1 79.25  ? 402 GLU   A CB  1 
ATOM   2975 C  CG  . GLU   A 1 417 ? 40.758  -36.768 -27.865 1 85.86  ? 402 GLU   A CG  1 
ATOM   2976 C  CD  . GLU   A 1 417 ? 41.737  -36.823 -29.026 1 94.58  ? 402 GLU   A CD  1 
ATOM   2977 O  OE1 . GLU   A 1 417 ? 41.603  -37.722 -29.889 1 95.52  ? 402 GLU   A OE1 1 
ATOM   2978 O  OE2 . GLU   A 1 417 ? 42.642  -35.957 -29.072 1 98.28  ? 402 GLU   A OE2 1 
ATOM   2979 N  N   . THR   B 1 25  ? 21.028  -11.521 6.513   1 71.92  ? 10  THR   B N   1 
ATOM   2980 C  CA  . THR   B 1 25  ? 21.811  -10.709 5.578   1 72.42  ? 10  THR   B CA  1 
ATOM   2981 C  C   . THR   B 1 25  ? 22.338  -11.487 4.376   1 71.93  ? 10  THR   B C   1 
ATOM   2982 O  O   . THR   B 1 25  ? 22.715  -12.656 4.503   1 72.21  ? 10  THR   B O   1 
ATOM   2983 C  CB  . THR   B 1 25  ? 23.011  -10.047 6.276   1 74.12  ? 10  THR   B CB  1 
ATOM   2984 O  OG1 . THR   B 1 25  ? 23.908  -11.055 6.755   1 74.81  ? 10  THR   B OG1 1 
ATOM   2985 C  CG2 . THR   B 1 25  ? 22.592  -9.1    7.383   1 75.06  ? 10  THR   B CG2 1 
ATOM   2986 N  N   . ILE   B 1 26  ? 22.437  -10.783 3.237   1 70.77  ? 11  ILE   B N   1 
ATOM   2987 C  CA  . ILE   B 1 26  ? 22.981  -11.208 1.942   1 69.69  ? 11  ILE   B CA  1 
ATOM   2988 C  C   . ILE   B 1 26  ? 24.382  -11.835 2.102   1 68.94  ? 11  ILE   B C   1 
ATOM   2989 O  O   . ILE   B 1 26  ? 25.269  -11.227 2.708   1 69.17  ? 11  ILE   B O   1 
ATOM   2990 C  CB  . ILE   B 1 26  ? 23.012  -9.938  1.072   1 69.28  ? 11  ILE   B CB  1 
ATOM   2991 C  CG1 . ILE   B 1 26  ? 21.588  -9.474  0.752   1 69.75  ? 11  ILE   B CG1 1 
ATOM   2992 C  CG2 . ILE   B 1 26  ? 23.851  -10.108 -0.172  1 69.37  ? 11  ILE   B CG2 1 
ATOM   2993 C  CD1 . ILE   B 1 26  ? 21.483  -8.046  0.573   1 70.92  ? 11  ILE   B CD1 1 
ATOM   2994 N  N   . SER   B 1 27  ? 24.538  -13.074 1.624   1 67.77  ? 12  SER   B N   1 
ATOM   2995 C  CA  . SER   B 1 27  ? 25.764  -13.85  1.731   1 67.25  ? 12  SER   B CA  1 
ATOM   2996 C  C   . SER   B 1 27  ? 26.949  -13.175 1.081   1 66.97  ? 12  SER   B C   1 
ATOM   2997 O  O   . SER   B 1 27  ? 26.804  -12.5   0.058   1 67.11  ? 12  SER   B O   1 
ATOM   2998 C  CB  . SER   B 1 27  ? 25.568  -15.231 1.118   1 67.84  ? 12  SER   B CB  1 
ATOM   2999 O  OG  . SER   B 1 27  ? 26.753  -16.01  1.091   1 69.77  ? 12  SER   B OG  1 
ATOM   3000 N  N   . LYS   B 1 28  ? 28.129  -13.39  1.675   1 66.13  ? 13  LYS   B N   1 
ATOM   3001 C  CA  . LYS   B 1 28  ? 29.4    -12.859 1.211   1 66.06  ? 13  LYS   B CA  1 
ATOM   3002 C  C   . LYS   B 1 28  ? 29.717  -13.311 -0.231  1 65.61  ? 13  LYS   B C   1 
ATOM   3003 O  O   . LYS   B 1 28  ? 30.362  -12.573 -0.99   1 65.74  ? 13  LYS   B O   1 
ATOM   3004 C  CB  . LYS   B 1 28  ? 30.513  -13.301 2.172   1 67.83  ? 13  LYS   B CB  1 
ATOM   3005 C  CG  . LYS   B 1 28  ? 30.263  -12.901 3.618   1 72.01  ? 13  LYS   B CG  1 
ATOM   3006 N  N   . GLU   B 1 29  ? 29.242  -14.516 -0.604  1 64.47  ? 14  GLU   B N   1 
ATOM   3007 C  CA  . GLU   B 1 29  ? 29.421  -15.1   -1.92   1 63.97  ? 14  GLU   B CA  1 
ATOM   3008 C  C   . GLU   B 1 29  ? 28.84   -14.215 -3.05   1 63.64  ? 14  GLU   B C   1 
ATOM   3009 O  O   . GLU   B 1 29  ? 29.184  -14.409 -4.216  1 63.77  ? 14  GLU   B O   1 
ATOM   3010 C  CB  . GLU   B 1 29  ? 28.775  -16.488 -1.96   1 65.86  ? 14  GLU   B CB  1 
ATOM   3011 C  CG  . GLU   B 1 29  ? 29.451  -17.554 -1.123  1 71.23  ? 14  GLU   B CG  1 
ATOM   3012 C  CD  . GLU   B 1 29  ? 28.811  -18.921 -1.319  1 79.67  ? 14  GLU   B CD  1 
ATOM   3013 O  OE1 . GLU   B 1 29  ? 28.691  -19.358 -2.487  1 81.12  ? 14  GLU   B OE1 1 
ATOM   3014 O  OE2 . GLU   B 1 29  ? 28.417  -19.551 -0.31   1 82.15  ? 14  GLU   B OE2 1 
ATOM   3015 N  N   . TYR   B 1 30  ? 27.958  -13.256 -2.718  1 62.88  ? 15  TYR   B N   1 
ATOM   3016 C  CA  . TYR   B 1 30  ? 27.382  -12.358 -3.719  1 62.45  ? 15  TYR   B CA  1 
ATOM   3017 C  C   . TYR   B 1 30  ? 28.235  -11.12  -4.011  1 62.73  ? 15  TYR   B C   1 
ATOM   3018 O  O   . TYR   B 1 30  ? 27.925  -10.401 -4.954  1 63.05  ? 15  TYR   B O   1 
ATOM   3019 C  CB  . TYR   B 1 30  ? 25.97   -11.931 -3.332  1 61.74  ? 15  TYR   B CB  1 
ATOM   3020 C  CG  . TYR   B 1 30  ? 24.979  -13.064 -3.411  1 61.84  ? 15  TYR   B CG  1 
ATOM   3021 C  CD1 . TYR   B 1 30  ? 24.779  -13.756 -4.593  1 62.08  ? 15  TYR   B CD1 1 
ATOM   3022 C  CD2 . TYR   B 1 30  ? 24.263  -13.467 -2.293  1 62.56  ? 15  TYR   B CD2 1 
ATOM   3023 C  CE1 . TYR   B 1 30  ? 23.878  -14.805 -4.67   1 62.45  ? 15  TYR   B CE1 1 
ATOM   3024 C  CE2 . TYR   B 1 30  ? 23.36   -14.522 -2.356  1 62.94  ? 15  TYR   B CE2 1 
ATOM   3025 C  CZ  . TYR   B 1 30  ? 23.176  -15.191 -3.548  1 63.23  ? 15  TYR   B CZ  1 
ATOM   3026 O  OH  . TYR   B 1 30  ? 22.29   -16.233 -3.626  1 64.32  ? 15  TYR   B OH  1 
ATOM   3027 N  N   . HIS   B 1 31  ? 29.283  -10.863 -3.209  1 62.46  ? 16  HIS   B N   1 
ATOM   3028 C  CA  . HIS   B 1 31  ? 30.207  -9.746  -3.384  1 62.53  ? 16  HIS   B CA  1 
ATOM   3029 C  C   . HIS   B 1 31  ? 29.52   -8.385  -3.41   1 61.87  ? 16  HIS   B C   1 
ATOM   3030 O  O   . HIS   B 1 31  ? 29.841  -7.535  -4.242  1 61.84  ? 16  HIS   B O   1 
ATOM   3031 C  CB  . HIS   B 1 31  ? 31.111  -9.946  -4.61   1 63.73  ? 16  HIS   B CB  1 
ATOM   3032 C  CG  . HIS   B 1 31  ? 32.025  -11.124 -4.485  1 66.85  ? 16  HIS   B CG  1 
ATOM   3033 N  ND1 . HIS   B 1 31  ? 31.535  -12.398 -4.283  1 69.32  ? 16  HIS   B ND1 1 
ATOM   3034 C  CD2 . HIS   B 1 31  ? 33.37   -11.185 -4.554  1 68.28  ? 16  HIS   B CD2 1 
ATOM   3035 C  CE1 . HIS   B 1 31  ? 32.591  -13.19  -4.224  1 69.84  ? 16  HIS   B CE1 1 
ATOM   3036 N  NE2 . HIS   B 1 31  ? 33.715  -12.508 -4.399  1 69.73  ? 16  HIS   B NE2 1 
ATOM   3037 N  N   . ILE   B 1 32  ? 28.587  -8.181  -2.48   1 61.21  ? 17  ILE   B N   1 
ATOM   3038 C  CA  . ILE   B 1 32  ? 27.92   -6.904  -2.293  1 61.34  ? 17  ILE   B CA  1 
ATOM   3039 C  C   . ILE   B 1 32  ? 28.464  -6.307  -0.995  1 62.6   ? 17  ILE   B C   1 
ATOM   3040 O  O   . ILE   B 1 32  ? 28.484  -6.976  0.037   1 63     ? 17  ILE   B O   1 
ATOM   3041 C  CB  . ILE   B 1 32  ? 26.388  -7.039  -2.243  1 61.13  ? 17  ILE   B CB  1 
ATOM   3042 C  CG1 . ILE   B 1 32  ? 25.873  -7.723  -3.507  1 61.96  ? 17  ILE   B CG1 1 
ATOM   3043 C  CG2 . ILE   B 1 32  ? 25.739  -5.667  -2.046  1 61.25  ? 17  ILE   B CG2 1 
ATOM   3044 C  CD1 . ILE   B 1 32  ? 24.432  -8.014  -3.481  1 63.2   ? 17  ILE   B CD1 1 
ATOM   3045 N  N   . ASP   B 1 33  ? 28.95   -5.072  -1.058  1 62.91  ? 18  ASP   B N   1 
ATOM   3046 C  CA  . ASP   B 1 33  ? 29.524  -4.389  0.079   1 63.58  ? 18  ASP   B CA  1 
ATOM   3047 C  C   . ASP   B 1 33  ? 28.459  -3.653  0.884   1 64.63  ? 18  ASP   B C   1 
ATOM   3048 O  O   . ASP   B 1 33  ? 27.513  -3.116  0.312   1 64.8   ? 18  ASP   B O   1 
ATOM   3049 C  CB  . ASP   B 1 33  ? 30.579  -3.411  -0.415  1 64.42  ? 18  ASP   B CB  1 
ATOM   3050 C  CG  . ASP   B 1 33  ? 31.472  -2.912  0.678   1 67.11  ? 18  ASP   B CG  1 
ATOM   3051 O  OD1 . ASP   B 1 33  ? 32.254  -3.719  1.205   1 67.01  ? 18  ASP   B OD1 1 
ATOM   3052 O  OD2 . ASP   B 1 33  ? 31.382  -1.705  1.013   1 69.03  ? 18  ASP   B OD2 1 
ATOM   3053 N  N   . GLU   B 1 34  ? 28.62   -3.602  2.213   1 65     ? 19  GLU   B N   1 
ATOM   3054 C  CA  . GLU   B 1 34  ? 27.666  -2.896  3.068   1 65.53  ? 19  GLU   B CA  1 
ATOM   3055 C  C   . GLU   B 1 34  ? 27.629  -1.396  2.763   1 65.96  ? 19  GLU   B C   1 
ATOM   3056 O  O   . GLU   B 1 34  ? 26.564  -0.776  2.835   1 66.47  ? 19  GLU   B O   1 
ATOM   3057 C  CB  . GLU   B 1 34  ? 28.005  -3.131  4.548   1 67.56  ? 19  GLU   B CB  1 
ATOM   3058 N  N   . GLU   B 1 35  ? 28.787  -0.82   2.395   1 65.65  ? 20  GLU   B N   1 
ATOM   3059 C  CA  . GLU   B 1 35  ? 28.919  0.599   2.105   1 65.61  ? 20  GLU   B CA  1 
ATOM   3060 C  C   . GLU   B 1 35  ? 28.768  0.974   0.624   1 64.54  ? 20  GLU   B C   1 
ATOM   3061 O  O   . GLU   B 1 35  ? 27.975  1.854   0.307   1 64.58  ? 20  GLU   B O   1 
ATOM   3062 C  CB  . GLU   B 1 35  ? 30.252  1.113   2.661   1 69.27  ? 20  GLU   B CB  1 
ATOM   3063 C  CG  . GLU   B 1 35  ? 30.485  2.604   2.469   1 76.57  ? 20  GLU   B CG  1 
ATOM   3064 C  CD  . GLU   B 1 35  ? 31.85   3.074   2.934   1 86.08  ? 20  GLU   B CD  1 
ATOM   3065 O  OE1 . GLU   B 1 35  ? 31.985  4.277   3.257   1 89.18  ? 20  GLU   B OE1 1 
ATOM   3066 O  OE2 . GLU   B 1 35  ? 32.784  2.238   2.982   1 88.48  ? 20  GLU   B OE2 1 
ATOM   3067 N  N   . VAL   B 1 36  ? 29.536  0.339   -0.278  1 63.4   ? 21  VAL   B N   1 
ATOM   3068 C  CA  . VAL   B 1 36  ? 29.502  0.703   -1.698  1 62.43  ? 21  VAL   B CA  1 
ATOM   3069 C  C   . VAL   B 1 36  ? 28.629  -0.228  -2.581  1 60.78  ? 21  VAL   B C   1 
ATOM   3070 O  O   . VAL   B 1 36  ? 28.495  0.039   -3.773  1 60.9   ? 21  VAL   B O   1 
ATOM   3071 C  CB  . VAL   B 1 36  ? 30.937  0.86    -2.284  1 63.36  ? 21  VAL   B CB  1 
ATOM   3072 C  CG1 . VAL   B 1 36  ? 31.716  1.939   -1.546  1 64     ? 21  VAL   B CG1 1 
ATOM   3073 C  CG2 . VAL   B 1 36  ? 31.698  -0.452  -2.249  1 63.51  ? 21  VAL   B CG2 1 
ATOM   3074 N  N   . GLY   B 1 37  ? 28.036  -1.271  -2      1 59.16  ? 22  GLY   B N   1 
ATOM   3075 C  CA  . GLY   B 1 37  ? 27.153  -2.197  -2.707  1 58.07  ? 22  GLY   B CA  1 
ATOM   3076 C  C   . GLY   B 1 37  ? 27.789  -2.999  -3.822  1 56.82  ? 22  GLY   B C   1 
ATOM   3077 O  O   . GLY   B 1 37  ? 28.685  -3.807  -3.575  1 56.53  ? 22  GLY   B O   1 
ATOM   3078 N  N   . PHE   B 1 38  ? 27.335  -2.785  -5.06   1 56.21  ? 23  PHE   B N   1 
ATOM   3079 C  CA  . PHE   B 1 38  ? 27.901  -3.491  -6.206  1 56.44  ? 23  PHE   B CA  1 
ATOM   3080 C  C   . PHE   B 1 38  ? 29.283  -2.952  -6.631  1 56.55  ? 23  PHE   B C   1 
ATOM   3081 O  O   . PHE   B 1 38  ? 30.02   -3.661  -7.315  1 55.59  ? 23  PHE   B O   1 
ATOM   3082 C  CB  . PHE   B 1 38  ? 26.927  -3.546  -7.385  1 55.99  ? 23  PHE   B CB  1 
ATOM   3083 C  CG  . PHE   B 1 38  ? 25.787  -4.498  -7.154  1 56.43  ? 23  PHE   B CG  1 
ATOM   3084 C  CD1 . PHE   B 1 38  ? 25.996  -5.861  -7.127  1 57.35  ? 23  PHE   B CD1 1 
ATOM   3085 C  CD2 . PHE   B 1 38  ? 24.508  -4.03   -6.94   1 57.45  ? 23  PHE   B CD2 1 
ATOM   3086 C  CE1 . PHE   B 1 38  ? 24.935  -6.738  -6.91   1 58.31  ? 23  PHE   B CE1 1 
ATOM   3087 C  CE2 . PHE   B 1 38  ? 23.452  -4.905  -6.717  1 58.09  ? 23  PHE   B CE2 1 
ATOM   3088 C  CZ  . PHE   B 1 38  ? 23.672  -6.252  -6.695  1 57.87  ? 23  PHE   B CZ  1 
ATOM   3089 N  N   . ALA   B 1 39  ? 29.644  -1.719  -6.206  1 57.42  ? 24  ALA   B N   1 
ATOM   3090 C  CA  . ALA   B 1 39  ? 30.968  -1.162  -6.497  1 58.42  ? 24  ALA   B CA  1 
ATOM   3091 C  C   . ALA   B 1 39  ? 32.043  -1.961  -5.776  1 59.29  ? 24  ALA   B C   1 
ATOM   3092 O  O   . ALA   B 1 39  ? 31.768  -2.597  -4.754  1 59.65  ? 24  ALA   B O   1 
ATOM   3093 C  CB  . ALA   B 1 39  ? 31.04   0.294   -6.082  1 58.5   ? 24  ALA   B CB  1 
ATOM   3094 N  N   . LEU   B 1 40  ? 33.244  -2.009  -6.355  1 59.64  ? 25  LEU   B N   1 
ATOM   3095 C  CA  . LEU   B 1 40  ? 34.345  -2.746  -5.753  1 60.83  ? 25  LEU   B CA  1 
ATOM   3096 C  C   . LEU   B 1 40  ? 34.847  -1.895  -4.597  1 62.75  ? 25  LEU   B C   1 
ATOM   3097 O  O   . LEU   B 1 40  ? 35.179  -0.728  -4.805  1 63.09  ? 25  LEU   B O   1 
ATOM   3098 C  CB  . LEU   B 1 40  ? 35.464  -2.973  -6.788  1 60.64  ? 25  LEU   B CB  1 
ATOM   3099 C  CG  . LEU   B 1 40  ? 36.687  -3.748  -6.3    1 61.57  ? 25  LEU   B CG  1 
ATOM   3100 C  CD1 . LEU   B 1 40  ? 36.379  -5.226  -6.178  1 61.76  ? 25  LEU   B CD1 1 
ATOM   3101 C  CD2 . LEU   B 1 40  ? 37.862  -3.545  -7.231  1 61.83  ? 25  LEU   B CD2 1 
ATOM   3102 N  N   . PRO   B 1 41  ? 34.813  -2.41   -3.356  1 63.78  ? 26  PRO   B N   1 
ATOM   3103 C  CA  . PRO   B 1 41  ? 35.289  -1.599  -2.222  1 64.85  ? 26  PRO   B CA  1 
ATOM   3104 C  C   . PRO   B 1 41  ? 36.799  -1.417  -2.292  1 66.81  ? 26  PRO   B C   1 
ATOM   3105 O  O   . PRO   B 1 41  ? 37.503  -2.354  -2.659  1 66.8   ? 26  PRO   B O   1 
ATOM   3106 C  CB  . PRO   B 1 41  ? 34.876  -2.417  -0.998  1 64.93  ? 26  PRO   B CB  1 
ATOM   3107 C  CG  . PRO   B 1 41  ? 34.816  -3.813  -1.489  1 65.14  ? 26  PRO   B CG  1 
ATOM   3108 C  CD  . PRO   B 1 41  ? 34.411  -3.765  -2.935  1 63.33  ? 26  PRO   B CD  1 
ATOM   3109 N  N   . ASN   B 1 42  ? 37.292  -0.19   -2.011  1 68.18  ? 27  ASN   B N   1 
ATOM   3110 C  CA  . ASN   B 1 42  ? 38.715  0.178   -2.021  1 69.9   ? 27  ASN   B CA  1 
ATOM   3111 C  C   . ASN   B 1 42  ? 39.509  -0.467  -3.153  1 70.78  ? 27  ASN   B C   1 
ATOM   3112 O  O   . ASN   B 1 42  ? 40.244  -1.434  -2.918  1 71.16  ? 27  ASN   B O   1 
ATOM   3113 C  CB  . ASN   B 1 42  ? 39.368  -0.139  -0.668  1 72.31  ? 27  ASN   B CB  1 
ATOM   3114 C  CG  . ASN   B 1 42  ? 38.954  0.797   0.43    1 77.88  ? 27  ASN   B CG  1 
ATOM   3115 O  OD1 . ASN   B 1 42  ? 38.907  2.018   0.243   1 80.1   ? 27  ASN   B OD1 1 
ATOM   3116 N  ND2 . ASN   B 1 42  ? 38.65   0.249   1.608   1 79.14  ? 27  ASN   B ND2 1 
ATOM   3117 N  N   . PRO   B 1 43  ? 39.294  -0.026  -4.402  1 70.76  ? 28  PRO   B N   1 
ATOM   3118 C  CA  . PRO   B 1 43  ? 40      -0.662  -5.519  1 71.14  ? 28  PRO   B CA  1 
ATOM   3119 C  C   . PRO   B 1 43  ? 41.507  -0.431  -5.465  1 72.39  ? 28  PRO   B C   1 
ATOM   3120 O  O   . PRO   B 1 43  ? 41.967  0.567   -4.907  1 72.64  ? 28  PRO   B O   1 
ATOM   3121 C  CB  . PRO   B 1 43  ? 39.349  -0.031  -6.755  1 71.28  ? 28  PRO   B CB  1 
ATOM   3122 C  CG  . PRO   B 1 43  ? 38.091  0.634   -6.253  1 71.38  ? 28  PRO   B CG  1 
ATOM   3123 C  CD  . PRO   B 1 43  ? 38.424  1.066   -4.869  1 69.87  ? 28  PRO   B CD  1 
ATOM   3124 N  N   . GLN   B 1 44  ? 42.274  -1.374  -6.024  1 73.11  ? 29  GLN   B N   1 
ATOM   3125 C  CA  . GLN   B 1 44  ? 43.731  -1.308  -6.055  1 74.32  ? 29  GLN   B CA  1 
ATOM   3126 C  C   . GLN   B 1 44  ? 44.171  -0.243  -7.043  1 75.47  ? 29  GLN   B C   1 
ATOM   3127 O  O   . GLN   B 1 44  ? 43.628  -0.175  -8.143  1 75.55  ? 29  GLN   B O   1 
ATOM   3128 C  CB  . GLN   B 1 44  ? 44.302  -2.669  -6.465  1 75.99  ? 29  GLN   B CB  1 
ATOM   3129 C  CG  . GLN   B 1 44  ? 45.657  -2.967  -5.856  1 79.51  ? 29  GLN   B CG  1 
ATOM   3130 C  CD  . GLN   B 1 44  ? 46.06   -4.391  -6.143  1 84.38  ? 29  GLN   B CD  1 
ATOM   3131 O  OE1 . GLN   B 1 44  ? 45.485  -5.344  -5.602  1 86.79  ? 29  GLN   B OE1 1 
ATOM   3132 N  NE2 . GLN   B 1 44  ? 47.051  -4.572  -7.007  1 84.27  ? 29  GLN   B NE2 1 
ATOM   3133 N  N   . GLU   B 1 45  ? 45.137  0.604   -6.656  1 76.05  ? 30  GLU   B N   1 
ATOM   3134 C  CA  . GLU   B 1 45  ? 45.61   1.669   -7.532  1 76.75  ? 30  GLU   B CA  1 
ATOM   3135 C  C   . GLU   B 1 45  ? 46.782  1.236   -8.394  1 77.4   ? 30  GLU   B C   1 
ATOM   3136 O  O   . GLU   B 1 45  ? 46.911  1.729   -9.508  1 77.29  ? 30  GLU   B O   1 
ATOM   3137 C  CB  . GLU   B 1 45  ? 46.014  2.907   -6.724  1 79.1   ? 30  GLU   B CB  1 
ATOM   3138 C  CG  . GLU   B 1 45  ? 44.874  3.555   -5.96   1 84.81  ? 30  GLU   B CG  1 
ATOM   3139 C  CD  . GLU   B 1 45  ? 45.209  4.962   -5.503  1 92.39  ? 30  GLU   B CD  1 
ATOM   3140 O  OE1 . GLU   B 1 45  ? 45.926  5.67    -6.247  1 92.81  ? 30  GLU   B OE1 1 
ATOM   3141 O  OE2 . GLU   B 1 45  ? 44.761  5.357   -4.401  1 95.69  ? 30  GLU   B OE2 1 
ATOM   3142 N  N   . ASN   B 1 46  ? 47.672  0.374   -7.868  1 77.99  ? 31  ASN   B N   1 
ATOM   3143 C  CA  . ASN   B 1 46  ? 48.861  -0.053  -8.608  1 79.18  ? 31  ASN   B CA  1 
ATOM   3144 C  C   . ASN   B 1 46  ? 49.021  -1.575  -8.666  1 80.14  ? 31  ASN   B C   1 
ATOM   3145 O  O   . ASN   B 1 46  ? 48.739  -2.278  -7.695  1 80.05  ? 31  ASN   B O   1 
ATOM   3146 C  CB  . ASN   B 1 46  ? 50.147  0.577   -8.035  1 80.56  ? 31  ASN   B CB  1 
ATOM   3147 C  CG  . ASN   B 1 46  ? 50.022  2.008   -7.536  1 84.13  ? 31  ASN   B CG  1 
ATOM   3148 O  OD1 . ASN   B 1 46  ? 49.944  2.974   -8.315  1 85.34  ? 31  ASN   B OD1 1 
ATOM   3149 N  ND2 . ASN   B 1 46  ? 50.005  2.177   -6.214  1 84.63  ? 31  ASN   B ND2 1 
ATOM   3150 N  N   . LEU   B 1 47  ? 49.492  -2.074  -9.814  1 80.78  ? 32  LEU   B N   1 
ATOM   3151 C  CA  . LEU   B 1 47  ? 49.757  -3.496  -10.063 1 81.68  ? 32  LEU   B CA  1 
ATOM   3152 C  C   . LEU   B 1 47  ? 51.189  -3.861  -9.611  1 82.96  ? 32  LEU   B C   1 
ATOM   3153 O  O   . LEU   B 1 47  ? 52.052  -2.975  -9.513  1 83.05  ? 32  LEU   B O   1 
ATOM   3154 C  CB  . LEU   B 1 47  ? 49.629  -3.777  -11.582 1 81.68  ? 32  LEU   B CB  1 
ATOM   3155 C  CG  . LEU   B 1 47  ? 48.224  -3.894  -12.163 1 82.92  ? 32  LEU   B CG  1 
ATOM   3156 C  CD1 . LEU   B 1 47  ? 48.275  -4.142  -13.663 1 83.29  ? 32  LEU   B CD1 1 
ATOM   3157 C  CD2 . LEU   B 1 47  ? 47.44   -4.99   -11.478 1 83.48  ? 32  LEU   B CD2 1 
ATOM   3158 N  N   . PRO   B 1 48  ? 51.495  -5.164  -9.395  1 83.66  ? 33  PRO   B N   1 
ATOM   3159 C  CA  . PRO   B 1 48  ? 52.881  -5.537  -9.057  1 84.37  ? 33  PRO   B CA  1 
ATOM   3160 C  C   . PRO   B 1 48  ? 53.872  -5.115  -10.151 1 85.45  ? 33  PRO   B C   1 
ATOM   3161 O  O   . PRO   B 1 48  ? 53.493  -5.022  -11.321 1 85.69  ? 33  PRO   B O   1 
ATOM   3162 C  CB  . PRO   B 1 48  ? 52.82   -7.068  -8.917  1 84.99  ? 33  PRO   B CB  1 
ATOM   3163 C  CG  . PRO   B 1 48  ? 51.577  -7.492  -9.626  1 85.16  ? 33  PRO   B CG  1 
ATOM   3164 C  CD  . PRO   B 1 48  ? 50.617  -6.35   -9.483  1 83.29  ? 33  PRO   B CD  1 
ATOM   3165 N  N   . ASP   B 1 49  ? 55.139  -4.851  -9.774  1 85.82  ? 34  ASP   B N   1 
ATOM   3166 C  CA  . ASP   B 1 49  ? 56.195  -4.384  -10.686 1 86.29  ? 34  ASP   B CA  1 
ATOM   3167 C  C   . ASP   B 1 49  ? 56.315  -5.177  -12     1 85.4   ? 34  ASP   B C   1 
ATOM   3168 O  O   . ASP   B 1 49  ? 56.712  -4.616  -13.024 1 85.43  ? 34  ASP   B O   1 
ATOM   3169 C  CB  . ASP   B 1 49  ? 57.551  -4.321  -9.967  1 89.12  ? 34  ASP   B CB  1 
ATOM   3170 C  CG  . ASP   B 1 49  ? 57.649  -3.151  -9.008  1 95.38  ? 34  ASP   B CG  1 
ATOM   3171 O  OD1 . ASP   B 1 49  ? 57.957  -2.022  -9.474  1 96.84  ? 34  ASP   B OD1 1 
ATOM   3172 O  OD2 . ASP   B 1 49  ? 57.413  -3.357  -7.794  1 97.51  ? 34  ASP   B OD2 1 
ATOM   3173 N  N   . PHE   B 1 50  ? 55.92   -6.449  -11.982 1 84.51  ? 35  PHE   B N   1 
ATOM   3174 C  CA  . PHE   B 1 50  ? 55.939  -7.31   -13.156 1 84.48  ? 35  PHE   B CA  1 
ATOM   3175 C  C   . PHE   B 1 50  ? 55.104  -6.745  -14.327 1 84.39  ? 35  PHE   B C   1 
ATOM   3176 O  O   . PHE   B 1 50  ? 55.381  -7.065  -15.487 1 84.43  ? 35  PHE   B O   1 
ATOM   3177 C  CB  . PHE   B 1 50  ? 55.425  -8.694  -12.751 1 84.56  ? 35  PHE   B CB  1 
ATOM   3178 C  CG  . PHE   B 1 50  ? 55.513  -9.757  -13.817 1 85.59  ? 35  PHE   B CG  1 
ATOM   3179 C  CD1 . PHE   B 1 50  ? 56.721  -10.359 -14.121 1 86.36  ? 35  PHE   B CD1 1 
ATOM   3180 C  CD2 . PHE   B 1 50  ? 54.377  -10.194 -14.477 1 86.7   ? 35  PHE   B CD2 1 
ATOM   3181 C  CE1 . PHE   B 1 50  ? 56.798  -11.347 -15.096 1 87.22  ? 35  PHE   B CE1 1 
ATOM   3182 C  CE2 . PHE   B 1 50  ? 54.454  -11.185 -15.451 1 87.52  ? 35  PHE   B CE2 1 
ATOM   3183 C  CZ  . PHE   B 1 50  ? 55.666  -11.751 -15.759 1 87.25  ? 35  PHE   B CZ  1 
ATOM   3184 N  N   . TYR   B 1 51  ? 54.09   -5.894  -14.019 1 83.9   ? 36  TYR   B N   1 
ATOM   3185 C  CA  . TYR   B 1 51  ? 53.17   -5.302  -15.001 1 83.4   ? 36  TYR   B CA  1 
ATOM   3186 C  C   . TYR   B 1 51  ? 53.321  -3.792  -15.172 1 83.32  ? 36  TYR   B C   1 
ATOM   3187 O  O   . TYR   B 1 51  ? 52.372  -3.138  -15.622 1 83.04  ? 36  TYR   B O   1 
ATOM   3188 C  CB  . TYR   B 1 51  ? 51.716  -5.614  -14.62  1 82.87  ? 36  TYR   B CB  1 
ATOM   3189 C  CG  . TYR   B 1 51  ? 51.43   -7.089  -14.494 1 82.87  ? 36  TYR   B CG  1 
ATOM   3190 C  CD1 . TYR   B 1 51  ? 51.31   -7.892  -15.62  1 83.51  ? 36  TYR   B CD1 1 
ATOM   3191 C  CD2 . TYR   B 1 51  ? 51.279  -7.684  -13.251 1 83.27  ? 36  TYR   B CD2 1 
ATOM   3192 C  CE1 . TYR   B 1 51  ? 51.016  -9.243  -15.516 1 84.21  ? 36  TYR   B CE1 1 
ATOM   3193 C  CE2 . TYR   B 1 51  ? 51.027  -9.044  -13.132 1 84.02  ? 36  TYR   B CE2 1 
ATOM   3194 C  CZ  . TYR   B 1 51  ? 50.875  -9.818  -14.269 1 85.11  ? 36  TYR   B CZ  1 
ATOM   3195 O  OH  . TYR   B 1 51  ? 50.624  -11.169 -14.183 1 86.81  ? 36  TYR   B OH  1 
ATOM   3196 N  N   . ASN   B 1 52  ? 54.503  -3.238  -14.85  1 83.27  ? 37  ASN   B N   1 
ATOM   3197 C  CA  . ASN   B 1 52  ? 54.751  -1.796  -14.996 1 83.46  ? 37  ASN   B CA  1 
ATOM   3198 C  C   . ASN   B 1 52  ? 54.657  -1.317  -16.455 1 82.71  ? 37  ASN   B C   1 
ATOM   3199 O  O   . ASN   B 1 52  ? 54.348  -0.149  -16.696 1 82.56  ? 37  ASN   B O   1 
ATOM   3200 C  CB  . ASN   B 1 52  ? 56.094  -1.397  -14.37  1 85.05  ? 37  ASN   B CB  1 
ATOM   3201 C  CG  . ASN   B 1 52  ? 56.096  -1.387  -12.858 1 88.99  ? 37  ASN   B CG  1 
ATOM   3202 O  OD1 . ASN   B 1 52  ? 55.057  -1.526  -12.203 1 90.5   ? 37  ASN   B OD1 1 
ATOM   3203 N  ND2 . ASN   B 1 52  ? 57.271  -1.236  -12.262 1 89.9   ? 37  ASN   B ND2 1 
ATOM   3204 N  N   . ASP   B 1 53  ? 54.894  -2.225  -17.424 1 82.06  ? 38  ASP   B N   1 
ATOM   3205 C  CA  . ASP   B 1 53  ? 54.791  -1.904  -18.848 1 82.02  ? 38  ASP   B CA  1 
ATOM   3206 C  C   . ASP   B 1 53  ? 53.334  -1.651  -19.262 1 81.64  ? 38  ASP   B C   1 
ATOM   3207 O  O   . ASP   B 1 53  ? 53.078  -0.813  -20.126 1 82.13  ? 38  ASP   B O   1 
ATOM   3208 C  CB  . ASP   B 1 53  ? 55.424  -3.006  -19.709 1 83.82  ? 38  ASP   B CB  1 
ATOM   3209 C  CG  . ASP   B 1 53  ? 56.944  -2.994  -19.754 1 88.21  ? 38  ASP   B CG  1 
ATOM   3210 O  OD1 . ASP   B 1 53  ? 57.555  -2.075  -19.146 1 88.3   ? 38  ASP   B OD1 1 
ATOM   3211 O  OD2 . ASP   B 1 53  ? 57.524  -3.9    -20.399 1 90.37  ? 38  ASP   B OD2 1 
ATOM   3212 N  N   . TRP   B 1 54  ? 52.379  -2.366  -18.634 1 80.38  ? 39  TRP   B N   1 
ATOM   3213 C  CA  . TRP   B 1 54  ? 50.956  -2.159  -18.879 1 79.25  ? 39  TRP   B CA  1 
ATOM   3214 C  C   . TRP   B 1 54  ? 50.55   -0.853  -18.184 1 78.73  ? 39  TRP   B C   1 
ATOM   3215 O  O   . TRP   B 1 54  ? 49.921  0.01    -18.79  1 78.96  ? 39  TRP   B O   1 
ATOM   3216 C  CB  . TRP   B 1 54  ? 50.136  -3.319  -18.278 1 78.67  ? 39  TRP   B CB  1 
ATOM   3217 C  CG  . TRP   B 1 54  ? 50.237  -4.644  -18.975 1 78.44  ? 39  TRP   B CG  1 
ATOM   3218 C  CD1 . TRP   B 1 54  ? 50.89   -4.927  -20.139 1 78.95  ? 39  TRP   B CD1 1 
ATOM   3219 C  CD2 . TRP   B 1 54  ? 49.619  -5.864  -18.555 1 78.24  ? 39  TRP   B CD2 1 
ATOM   3220 N  NE1 . TRP   B 1 54  ? 50.736  -6.254  -20.457 1 79.13  ? 39  TRP   B NE1 1 
ATOM   3221 C  CE2 . TRP   B 1 54  ? 49.954  -6.852  -19.503 1 78.86  ? 39  TRP   B CE2 1 
ATOM   3222 C  CE3 . TRP   B 1 54  ? 48.812  -6.219  -17.468 1 78.66  ? 39  TRP   B CE3 1 
ATOM   3223 C  CZ2 . TRP   B 1 54  ? 49.494  -8.165  -19.406 1 79.42  ? 39  TRP   B CZ2 1 
ATOM   3224 C  CZ3 . TRP   B 1 54  ? 48.355  -7.519  -17.376 1 79.45  ? 39  TRP   B CZ3 1 
ATOM   3225 C  CH2 . TRP   B 1 54  ? 48.705  -8.478  -18.332 1 79.57  ? 39  TRP   B CH2 1 
ATOM   3226 N  N   . MET   B 1 55  ? 50.947  -0.703  -16.92  1 77.98  ? 40  MET   B N   1 
ATOM   3227 C  CA  . MET   B 1 55  ? 50.631  0.447   -16.104 1 78.01  ? 40  MET   B CA  1 
ATOM   3228 C  C   . MET   B 1 55  ? 51.095  1.754   -16.684 1 77.77  ? 40  MET   B C   1 
ATOM   3229 O  O   . MET   B 1 55  ? 50.426  2.767   -16.492 1 77.88  ? 40  MET   B O   1 
ATOM   3230 C  CB  . MET   B 1 55  ? 51.213  0.26    -14.712 1 79     ? 40  MET   B CB  1 
ATOM   3231 C  CG  . MET   B 1 55  ? 50.361  0.833   -13.663 1 81.88  ? 40  MET   B CG  1 
ATOM   3232 S  SD  . MET   B 1 55  ? 48.712  0.103   -13.534 1 86.19  ? 40  MET   B SD  1 
ATOM   3233 C  CE  . MET   B 1 55  ? 48.254  0.819   -12.123 1 84.81  ? 40  MET   B CE  1 
ATOM   3234 N  N   . PHE   B 1 56  ? 52.247  1.75    -17.379 1 77.39  ? 41  PHE   B N   1 
ATOM   3235 C  CA  . PHE   B 1 56  ? 52.756  2.978   -17.972 1 77.39  ? 41  PHE   B CA  1 
ATOM   3236 C  C   . PHE   B 1 56  ? 51.808  3.443   -19.085 1 76.58  ? 41  PHE   B C   1 
ATOM   3237 O  O   . PHE   B 1 56  ? 51.435  4.615   -19.127 1 76.56  ? 41  PHE   B O   1 
ATOM   3238 C  CB  . PHE   B 1 56  ? 54.213  2.812   -18.48  1 77.7   ? 41  PHE   B CB  1 
ATOM   3239 C  CG  . PHE   B 1 56  ? 54.646  3.962   -19.362 1 78.53  ? 41  PHE   B CG  1 
ATOM   3240 C  CD1 . PHE   B 1 56  ? 54.897  5.214   -18.822 1 79.33  ? 41  PHE   B CD1 1 
ATOM   3241 C  CD2 . PHE   B 1 56  ? 54.665  3.827   -20.742 1 79.47  ? 41  PHE   B CD2 1 
ATOM   3242 C  CE1 . PHE   B 1 56  ? 55.202  6.295   -19.638 1 80.08  ? 41  PHE   B CE1 1 
ATOM   3243 C  CE2 . PHE   B 1 56  ? 54.964  4.907   -21.556 1 80.28  ? 41  PHE   B CE2 1 
ATOM   3244 C  CZ  . PHE   B 1 56  ? 55.238  6.135   -21     1 80.1   ? 41  PHE   B CZ  1 
ATOM   3245 N  N   . ILE   B 1 57  ? 51.433  2.516   -19.98  1 75.64  ? 42  ILE   B N   1 
ATOM   3246 C  CA  . ILE   B 1 57  ? 50.542  2.797   -21.103 1 74.99  ? 42  ILE   B CA  1 
ATOM   3247 C  C   . ILE   B 1 57  ? 49.171  3.284   -20.633 1 74.44  ? 42  ILE   B C   1 
ATOM   3248 O  O   . ILE   B 1 57  ? 48.686  4.305   -21.118 1 74.48  ? 42  ILE   B O   1 
ATOM   3249 C  CB  . ILE   B 1 57  ? 50.422  1.541   -22.003 1 75.12  ? 42  ILE   B CB  1 
ATOM   3250 C  CG1 . ILE   B 1 57  ? 51.793  1.144   -22.587 1 75.49  ? 42  ILE   B CG1 1 
ATOM   3251 C  CG2 . ILE   B 1 57  ? 49.379  1.749   -23.095 1 75.67  ? 42  ILE   B CG2 1 
ATOM   3252 C  CD1 . ILE   B 1 57  ? 51.805  -0.152  -23.325 1 76.31  ? 42  ILE   B CD1 1 
ATOM   3253 N  N   . ALA   B 1 58  ? 48.568  2.567   -19.666 1 73.88  ? 43  ALA   B N   1 
ATOM   3254 C  CA  . ALA   B 1 58  ? 47.249  2.87    -19.116 1 73.61  ? 43  ALA   B CA  1 
ATOM   3255 C  C   . ALA   B 1 58  ? 47.22   4.212   -18.403 1 73.41  ? 43  ALA   B C   1 
ATOM   3256 O  O   . ALA   B 1 58  ? 46.292  4.999   -18.612 1 73.41  ? 43  ALA   B O   1 
ATOM   3257 C  CB  . ALA   B 1 58  ? 46.81   1.76    -18.178 1 73.76  ? 43  ALA   B CB  1 
ATOM   3258 N  N   . LYS   B 1 59  ? 48.254  4.508   -17.6   1 73.38  ? 44  LYS   B N   1 
ATOM   3259 C  CA  . LYS   B 1 59  ? 48.314  5.795   -16.902 1 73.89  ? 44  LYS   B CA  1 
ATOM   3260 C  C   . LYS   B 1 59  ? 48.646  6.98    -17.834 1 74.32  ? 44  LYS   B C   1 
ATOM   3261 O  O   . LYS   B 1 59  ? 48.524  8.129   -17.42  1 73.92  ? 44  LYS   B O   1 
ATOM   3262 C  CB  . LYS   B 1 59  ? 49.273  5.735   -15.703 1 75.36  ? 44  LYS   B CB  1 
ATOM   3263 N  N   . HIS   B 1 60  ? 49.039  6.71    -19.09  1 75.04  ? 45  HIS   B N   1 
ATOM   3264 C  CA  . HIS   B 1 60  ? 49.389  7.766   -20.036 1 76.15  ? 45  HIS   B CA  1 
ATOM   3265 C  C   . HIS   B 1 60  ? 48.593  7.713   -21.337 1 76.24  ? 45  HIS   B C   1 
ATOM   3266 O  O   . HIS   B 1 60  ? 49.131  8.065   -22.38  1 76.6   ? 45  HIS   B O   1 
ATOM   3267 C  CB  . HIS   B 1 60  ? 50.91   7.769   -20.305 1 77.46  ? 45  HIS   B CB  1 
ATOM   3268 C  CG  . HIS   B 1 60  ? 51.705  8.069   -19.071 1 80.43  ? 45  HIS   B CG  1 
ATOM   3269 N  ND1 . HIS   B 1 60  ? 52.394  7.08    -18.396 1 82.52  ? 45  HIS   B ND1 1 
ATOM   3270 C  CD2 . HIS   B 1 60  ? 51.82   9.23    -18.382 1 81.67  ? 45  HIS   B CD2 1 
ATOM   3271 C  CE1 . HIS   B 1 60  ? 52.928  7.672   -17.338 1 83.11  ? 45  HIS   B CE1 1 
ATOM   3272 N  NE2 . HIS   B 1 60  ? 52.608  8.965   -17.287 1 82.94  ? 45  HIS   B NE2 1 
ATOM   3273 N  N   . LEU   B 1 61  ? 47.316  7.301   -21.278 1 75.81  ? 46  LEU   B N   1 
ATOM   3274 C  CA  . LEU   B 1 61  ? 46.464  7.257   -22.464 1 76.11  ? 46  LEU   B CA  1 
ATOM   3275 C  C   . LEU   B 1 61  ? 46.253  8.638   -23.106 1 76.65  ? 46  LEU   B C   1 
ATOM   3276 O  O   . LEU   B 1 61  ? 46.345  8.714   -24.33  1 76.94  ? 46  LEU   B O   1 
ATOM   3277 C  CB  . LEU   B 1 61  ? 45.104  6.593   -22.191 1 76.08  ? 46  LEU   B CB  1 
ATOM   3278 C  CG  . LEU   B 1 61  ? 45.09   5.112   -21.844 1 77.24  ? 46  LEU   B CG  1 
ATOM   3279 C  CD1 . LEU   B 1 61  ? 43.66   4.627   -21.694 1 77.91  ? 46  LEU   B CD1 1 
ATOM   3280 C  CD2 . LEU   B 1 61  ? 45.775  4.281   -22.907 1 77.53  ? 46  LEU   B CD2 1 
ATOM   3281 N  N   . PRO   B 1 62  ? 45.959  9.737   -22.351 1 76.31  ? 47  PRO   B N   1 
ATOM   3282 C  CA  . PRO   B 1 62  ? 45.752  11.034  -23.02  1 76.25  ? 47  PRO   B CA  1 
ATOM   3283 C  C   . PRO   B 1 62  ? 46.95   11.482  -23.862 1 76.21  ? 47  PRO   B C   1 
ATOM   3284 O  O   . PRO   B 1 62  ? 46.761  11.914  -24.999 1 76.51  ? 47  PRO   B O   1 
ATOM   3285 C  CB  . PRO   B 1 62  ? 45.465  11.997  -21.857 1 76.72  ? 47  PRO   B CB  1 
ATOM   3286 C  CG  . PRO   B 1 62  ? 45.026  11.132  -20.748 1 76.95  ? 47  PRO   B CG  1 
ATOM   3287 C  CD  . PRO   B 1 62  ? 45.791  9.864   -20.89  1 75.46  ? 47  PRO   B CD  1 
ATOM   3288 N  N   . ASP   B 1 63  ? 48.18   11.349  -23.323 1 75.45  ? 48  ASP   B N   1 
ATOM   3289 C  CA  . ASP   B 1 63  ? 49.382  11.756  -24.046 1 75.02  ? 48  ASP   B CA  1 
ATOM   3290 C  C   . ASP   B 1 63  ? 49.768  10.768  -25.147 1 74.4   ? 48  ASP   B C   1 
ATOM   3291 O  O   . ASP   B 1 63  ? 50.093  11.206  -26.248 1 74.59  ? 48  ASP   B O   1 
ATOM   3292 C  CB  . ASP   B 1 63  ? 50.556  12.011  -23.086 1 76.21  ? 48  ASP   B CB  1 
ATOM   3293 N  N   . LEU   B 1 64  ? 49.706  9.45    -24.875 1 73.44  ? 49  LEU   B N   1 
ATOM   3294 C  CA  . LEU   B 1 64  ? 50.066  8.443   -25.877 1 73.19  ? 49  LEU   B CA  1 
ATOM   3295 C  C   . LEU   B 1 64  ? 49.089  8.368   -27.042 1 73.08  ? 49  LEU   B C   1 
ATOM   3296 O  O   . LEU   B 1 64  ? 49.505  8.029   -28.147 1 72.95  ? 49  LEU   B O   1 
ATOM   3297 C  CB  . LEU   B 1 64  ? 50.272  7.06    -25.255 1 73.27  ? 49  LEU   B CB  1 
ATOM   3298 N  N   . ILE   B 1 65  ? 47.798  8.664   -26.812 1 72.99  ? 50  ILE   B N   1 
ATOM   3299 C  CA  . ILE   B 1 65  ? 46.812  8.645   -27.897 1 73.1   ? 50  ILE   B CA  1 
ATOM   3300 C  C   . ILE   B 1 65  ? 47.064  9.856   -28.772 1 73.22  ? 50  ILE   B C   1 
ATOM   3301 O  O   . ILE   B 1 65  ? 47.209  9.709   -29.984 1 73.38  ? 50  ILE   B O   1 
ATOM   3302 C  CB  . ILE   B 1 65  ? 45.325  8.602   -27.407 1 73.05  ? 50  ILE   B CB  1 
ATOM   3303 C  CG1 . ILE   B 1 65  ? 44.955  7.258   -26.783 1 73.5   ? 50  ILE   B CG1 1 
ATOM   3304 C  CG2 . ILE   B 1 65  ? 44.357  8.946   -28.534 1 73.3   ? 50  ILE   B CG2 1 
ATOM   3305 C  CD1 . ILE   B 1 65  ? 43.629  7.319   -26.013 1 74.34  ? 50  ILE   B CD1 1 
ATOM   3306 N  N   . GLU   B 1 66  ? 47.144  11.046  -28.144 1 73.23  ? 51  GLU   B N   1 
ATOM   3307 C  CA  . GLU   B 1 66  ? 47.35   12.343  -28.808 1 73.81  ? 51  GLU   B CA  1 
ATOM   3308 C  C   . GLU   B 1 66  ? 48.611  12.37   -29.665 1 73.84  ? 51  GLU   B C   1 
ATOM   3309 O  O   . GLU   B 1 66  ? 48.584  12.863  -30.795 1 73.91  ? 51  GLU   B O   1 
ATOM   3310 C  CB  . GLU   B 1 66  ? 47.358  13.49   -27.774 1 75.65  ? 51  GLU   B CB  1 
ATOM   3311 C  CG  . GLU   B 1 66  ? 47.083  14.858  -28.369 1 80.46  ? 51  GLU   B CG  1 
ATOM   3312 C  CD  . GLU   B 1 66  ? 48.322  15.53   -28.929 1 88.75  ? 51  GLU   B CD  1 
ATOM   3313 O  OE1 . GLU   B 1 66  ? 49.405  15.385  -28.315 1 90.3   ? 51  GLU   B OE1 1 
ATOM   3314 O  OE2 . GLU   B 1 66  ? 48.22   16.171  -30     1 91.68  ? 51  GLU   B OE2 1 
ATOM   3315 N  N   . SER   B 1 67  ? 49.703  11.826  -29.133 1 73.58  ? 52  SER   B N   1 
ATOM   3316 C  CA  . SER   B 1 67  ? 50.966  11.787  -29.846 1 73.92  ? 52  SER   B CA  1 
ATOM   3317 C  C   . SER   B 1 67  ? 51.003  10.761  -30.982 1 74.53  ? 52  SER   B C   1 
ATOM   3318 O  O   . SER   B 1 67  ? 51.828  10.885  -31.879 1 75.19  ? 52  SER   B O   1 
ATOM   3319 C  CB  . SER   B 1 67  ? 52.11   11.518  -28.875 1 74.47  ? 52  SER   B CB  1 
ATOM   3320 O  OG  . SER   B 1 67  ? 52.081  10.179  -28.412 1 76.17  ? 52  SER   B OG  1 
ATOM   3321 N  N   . GLY   B 1 68  ? 50.139  9.759   -30.936 1 74.16  ? 53  GLY   B N   1 
ATOM   3322 C  CA  . GLY   B 1 68  ? 50.141  8.683   -31.921 1 74.48  ? 53  GLY   B CA  1 
ATOM   3323 C  C   . GLY   B 1 68  ? 51.083  7.544   -31.557 1 74.72  ? 53  GLY   B C   1 
ATOM   3324 O  O   . GLY   B 1 68  ? 51.196  6.562   -32.297 1 74.56  ? 53  GLY   B O   1 
ATOM   3325 N  N   . GLN   B 1 69  ? 51.766  7.657   -30.403 1 74.81  ? 54  GLN   B N   1 
ATOM   3326 C  CA  . GLN   B 1 69  ? 52.705  6.658   -29.925 1 75.2   ? 54  GLN   B CA  1 
ATOM   3327 C  C   . GLN   B 1 69  ? 52.033  5.475   -29.226 1 75.44  ? 54  GLN   B C   1 
ATOM   3328 O  O   . GLN   B 1 69  ? 52.706  4.485   -28.975 1 75.64  ? 54  GLN   B O   1 
ATOM   3329 C  CB  . GLN   B 1 69  ? 53.741  7.308   -28.995 1 76.56  ? 54  GLN   B CB  1 
ATOM   3330 N  N   . LEU   B 1 70  ? 50.723  5.555   -28.919 1 75.06  ? 55  LEU   B N   1 
ATOM   3331 C  CA  . LEU   B 1 70  ? 50.011  4.49    -28.212 1 74.71  ? 55  LEU   B CA  1 
ATOM   3332 C  C   . LEU   B 1 70  ? 50.015  3.136   -28.93  1 74.44  ? 55  LEU   B C   1 
ATOM   3333 O  O   . LEU   B 1 70  ? 50.397  2.149   -28.313 1 74.07  ? 55  LEU   B O   1 
ATOM   3334 C  CB  . LEU   B 1 70  ? 48.573  4.914   -27.863 1 74.93  ? 55  LEU   B CB  1 
ATOM   3335 C  CG  . LEU   B 1 70  ? 47.718  3.832   -27.226 1 76.04  ? 55  LEU   B CG  1 
ATOM   3336 C  CD1 . LEU   B 1 70  ? 47.829  3.851   -25.73  1 76.36  ? 55  LEU   B CD1 1 
ATOM   3337 C  CD2 . LEU   B 1 70  ? 46.353  3.895   -27.73  1 76.31  ? 55  LEU   B CD2 1 
ATOM   3338 N  N   . ARG   B 1 71  ? 49.552  3.065   -30.187 1 74.83  ? 56  ARG   B N   1 
ATOM   3339 C  CA  . ARG   B 1 71  ? 49.495  1.794   -30.908 1 76.16  ? 56  ARG   B CA  1 
ATOM   3340 C  C   . ARG   B 1 71  ? 50.856  1.116   -31.009 1 77.88  ? 56  ARG   B C   1 
ATOM   3341 O  O   . ARG   B 1 71  ? 50.959  -0.095  -30.826 1 77.87  ? 56  ARG   B O   1 
ATOM   3342 C  CB  . ARG   B 1 71  ? 48.829  1.967   -32.274 1 77.07  ? 56  ARG   B CB  1 
ATOM   3343 C  CG  . ARG   B 1 71  ? 47.332  2.178   -32.149 1 78.87  ? 56  ARG   B CG  1 
ATOM   3344 C  CD  . ARG   B 1 71  ? 46.703  2.685   -33.424 1 81.41  ? 56  ARG   B CD  1 
ATOM   3345 N  NE  . ARG   B 1 71  ? 45.243  2.652   -33.351 1 83.76  ? 56  ARG   B NE  1 
ATOM   3346 C  CZ  . ARG   B 1 71  ? 44.429  3.194   -34.251 1 85.74  ? 56  ARG   B CZ  1 
ATOM   3347 N  NH1 . ARG   B 1 71  ? 44.923  3.821   -35.313 1 85.32  ? 56  ARG   B NH1 1 
ATOM   3348 N  NH2 . ARG   B 1 71  ? 43.113  3.102   -34.104 1 85.32  ? 56  ARG   B NH2 1 
ATOM   3349 N  N   . GLU   B 1 72  ? 51.907  1.923   -31.187 1 79.12  ? 57  GLU   B N   1 
ATOM   3350 C  CA  . GLU   B 1 72  ? 53.286  1.454   -31.239 1 80.36  ? 57  GLU   B CA  1 
ATOM   3351 C  C   . GLU   B 1 72  ? 53.712  0.863   -29.887 1 80.97  ? 57  GLU   B C   1 
ATOM   3352 O  O   . GLU   B 1 72  ? 54.219  -0.253  -29.871 1 81.14  ? 57  GLU   B O   1 
ATOM   3353 C  CB  . GLU   B 1 72  ? 54.227  2.595   -31.666 1 82.77  ? 57  GLU   B CB  1 
ATOM   3354 N  N   . ARG   B 1 73  ? 53.458  1.574   -28.758 1 81.15  ? 58  ARG   B N   1 
ATOM   3355 C  CA  . ARG   B 1 73  ? 53.805  1.09    -27.414 1 82.09  ? 58  ARG   B CA  1 
ATOM   3356 C  C   . ARG   B 1 73  ? 53.104  -0.23   -27.081 1 82.74  ? 58  ARG   B C   1 
ATOM   3357 O  O   . ARG   B 1 73  ? 53.678  -1.058  -26.369 1 83.04  ? 58  ARG   B O   1 
ATOM   3358 C  CB  . ARG   B 1 73  ? 53.48   2.126   -26.329 1 83.57  ? 58  ARG   B CB  1 
ATOM   3359 C  CG  . ARG   B 1 73  ? 54.179  3.456   -26.492 1 87.31  ? 58  ARG   B CG  1 
ATOM   3360 C  CD  . ARG   B 1 73  ? 55.557  3.534   -25.868 1 91.65  ? 58  ARG   B CD  1 
ATOM   3361 N  NE  . ARG   B 1 73  ? 56.129  4.859   -26.121 1 95.97  ? 58  ARG   B NE  1 
ATOM   3362 C  CZ  . ARG   B 1 73  ? 56.382  5.767   -25.182 1 99.09  ? 58  ARG   B CZ  1 
ATOM   3363 N  NH1 . ARG   B 1 73  ? 56.176  5.484   -23.903 1 99.12  ? 58  ARG   B NH1 1 
ATOM   3364 N  NH2 . ARG   B 1 73  ? 56.88   6.953   -25.513 1 99.18  ? 58  ARG   B NH2 1 
ATOM   3365 N  N   . VAL   B 1 74  ? 51.869  -0.425  -27.59  1 82.55  ? 59  VAL   B N   1 
ATOM   3366 C  CA  . VAL   B 1 74  ? 51.118  -1.659  -27.377 1 82.94  ? 59  VAL   B CA  1 
ATOM   3367 C  C   . VAL   B 1 74  ? 51.801  -2.769  -28.18  1 83.25  ? 59  VAL   B C   1 
ATOM   3368 O  O   . VAL   B 1 74  ? 52.115  -3.826  -27.629 1 83.37  ? 59  VAL   B O   1 
ATOM   3369 C  CB  . VAL   B 1 74  ? 49.619  -1.5    -27.762 1 83.65  ? 59  VAL   B CB  1 
ATOM   3370 C  CG1 . VAL   B 1 74  ? 48.902  -2.841  -27.783 1 83.94  ? 59  VAL   B CG1 1 
ATOM   3371 C  CG2 . VAL   B 1 74  ? 48.907  -0.532  -26.828 1 84.1   ? 59  VAL   B CG2 1 
ATOM   3372 N  N   . GLU   B 1 75  ? 52.089  -2.503  -29.468 1 83.15  ? 60  GLU   B N   1 
ATOM   3373 C  CA  . GLU   B 1 75  ? 52.762  -3.448  -30.364 1 83.54  ? 60  GLU   B CA  1 
ATOM   3374 C  C   . GLU   B 1 75  ? 54.18   -3.838  -29.894 1 83.68  ? 60  GLU   B C   1 
ATOM   3375 O  O   . GLU   B 1 75  ? 54.652  -4.938  -30.187 1 83.83  ? 60  GLU   B O   1 
ATOM   3376 C  CB  . GLU   B 1 75  ? 52.791  -2.902  -31.795 1 85.7   ? 60  GLU   B CB  1 
ATOM   3377 C  CG  . GLU   B 1 75  ? 51.448  -3.001  -32.493 1 90.74  ? 60  GLU   B CG  1 
ATOM   3378 C  CD  . GLU   B 1 75  ? 51.161  -1.919  -33.515 1 97.92  ? 60  GLU   B CD  1 
ATOM   3379 O  OE1 . GLU   B 1 75  ? 52.022  -1.031  -33.712 1 99.17  ? 60  GLU   B OE1 1 
ATOM   3380 O  OE2 . GLU   B 1 75  ? 50.06   -1.949  -34.109 1 101.05 ? 60  GLU   B OE2 1 
ATOM   3381 N  N   . LYS   B 1 76  ? 54.836  -2.955  -29.136 1 83.42  ? 61  LYS   B N   1 
ATOM   3382 C  CA  . LYS   B 1 76  ? 56.174  -3.197  -28.605 1 83.78  ? 61  LYS   B CA  1 
ATOM   3383 C  C   . LYS   B 1 76  ? 56.185  -4.027  -27.298 1 84.39  ? 61  LYS   B C   1 
ATOM   3384 O  O   . LYS   B 1 76  ? 57.258  -4.368  -26.808 1 84.56  ? 61  LYS   B O   1 
ATOM   3385 C  CB  . LYS   B 1 76  ? 56.899  -1.855  -28.389 1 84.94  ? 61  LYS   B CB  1 
ATOM   3386 N  N   . LEU   B 1 77  ? 55.012  -4.323  -26.721 1 84.61  ? 62  LEU   B N   1 
ATOM   3387 C  CA  . LEU   B 1 77  ? 54.921  -5.067  -25.464 1 85.25  ? 62  LEU   B CA  1 
ATOM   3388 C  C   . LEU   B 1 77  ? 55.295  -6.533  -25.614 1 85.84  ? 62  LEU   B C   1 
ATOM   3389 O  O   . LEU   B 1 77  ? 55.086  -7.137  -26.667 1 85.83  ? 62  LEU   B O   1 
ATOM   3390 C  CB  . LEU   B 1 77  ? 53.491  -5.002  -24.891 1 85.28  ? 62  LEU   B CB  1 
ATOM   3391 C  CG  . LEU   B 1 77  ? 53.02   -3.695  -24.279 1 86.47  ? 62  LEU   B CG  1 
ATOM   3392 C  CD1 . LEU   B 1 77  ? 51.559  -3.784  -23.907 1 86.92  ? 62  LEU   B CD1 1 
ATOM   3393 C  CD2 . LEU   B 1 77  ? 53.825  -3.342  -23.053 1 87.04  ? 62  LEU   B CD2 1 
ATOM   3394 N  N   . ASN   B 1 78  ? 55.802  -7.116  -24.534 1 86.23  ? 63  ASN   B N   1 
ATOM   3395 C  CA  . ASN   B 1 78  ? 56.092  -8.543  -24.492 1 87.15  ? 63  ASN   B CA  1 
ATOM   3396 C  C   . ASN   B 1 78  ? 54.902  -9.205  -23.787 1 87.28  ? 63  ASN   B C   1 
ATOM   3397 O  O   . ASN   B 1 78  ? 54.403  -8.669  -22.792 1 87.57  ? 63  ASN   B O   1 
ATOM   3398 C  CB  . ASN   B 1 78  ? 57.399  -8.817  -23.745 1 88.72  ? 63  ASN   B CB  1 
ATOM   3399 C  CG  . ASN   B 1 78  ? 58.622  -8.481  -24.564 1 92.41  ? 63  ASN   B CG  1 
ATOM   3400 O  OD1 . ASN   B 1 78  ? 58.65   -8.682  -25.791 1 93.65  ? 63  ASN   B OD1 1 
ATOM   3401 N  ND2 . ASN   B 1 78  ? 59.656  -7.959  -23.905 1 92.95  ? 63  ASN   B ND2 1 
ATOM   3402 N  N   . MET   B 1 79  ? 54.414  -10.329 -24.321 1 86.81  ? 64  MET   B N   1 
ATOM   3403 C  CA  . MET   B 1 79  ? 53.269  -11.01  -23.737 1 86.96  ? 64  MET   B CA  1 
ATOM   3404 C  C   . MET   B 1 79  ? 53.547  -11.496 -22.316 1 87.42  ? 64  MET   B C   1 
ATOM   3405 O  O   . MET   B 1 79  ? 54.359  -12.401 -22.123 1 87.94  ? 64  MET   B O   1 
ATOM   3406 C  CB  . MET   B 1 79  ? 52.835  -12.171 -24.62  1 87.18  ? 64  MET   B CB  1 
ATOM   3407 C  CG  . MET   B 1 79  ? 51.572  -12.813 -24.151 1 88.76  ? 64  MET   B CG  1 
ATOM   3408 S  SD  . MET   B 1 79  ? 51.358  -14.437 -24.91  1 91.4   ? 64  MET   B SD  1 
ATOM   3409 C  CE  . MET   B 1 79  ? 51.127  -13.97  -26.62  1 89.42  ? 64  MET   B CE  1 
ATOM   3410 N  N   . LEU   B 1 80  ? 52.882  -10.884 -21.32  1 86.99  ? 65  LEU   B N   1 
ATOM   3411 C  CA  . LEU   B 1 80  ? 53.061  -11.242 -19.911 1 86.98  ? 65  LEU   B CA  1 
ATOM   3412 C  C   . LEU   B 1 80  ? 52.051  -12.297 -19.451 1 87.09  ? 65  LEU   B C   1 
ATOM   3413 O  O   . LEU   B 1 80  ? 50.955  -12.385 -19.999 1 87.25  ? 65  LEU   B O   1 
ATOM   3414 C  CB  . LEU   B 1 80  ? 52.95   -9.993  -19.023 1 86.98  ? 65  LEU   B CB  1 
ATOM   3415 C  CG  . LEU   B 1 80  ? 53.965  -8.901  -19.311 1 88.25  ? 65  LEU   B CG  1 
ATOM   3416 C  CD1 . LEU   B 1 80  ? 53.58   -7.602  -18.625 1 88.61  ? 65  LEU   B CD1 1 
ATOM   3417 C  CD2 . LEU   B 1 80  ? 55.36   -9.335  -18.903 1 88.89  ? 65  LEU   B CD2 1 
ATOM   3418 N  N   . SER   B 1 81  ? 52.413  -13.092 -18.435 1 86.89  ? 66  SER   B N   1 
ATOM   3419 C  CA  . SER   B 1 81  ? 51.505  -14.103 -17.898 1 87.05  ? 66  SER   B CA  1 
ATOM   3420 C  C   . SER   B 1 81  ? 50.588  -13.47  -16.852 1 87.19  ? 66  SER   B C   1 
ATOM   3421 O  O   . SER   B 1 81  ? 51.034  -12.622 -16.076 1 87.28  ? 66  SER   B O   1 
ATOM   3422 C  CB  . SER   B 1 81  ? 52.289  -15.239 -17.249 1 87.81  ? 66  SER   B CB  1 
ATOM   3423 N  N   . ILE   B 1 82  ? 49.319  -13.901 -16.799 1 86.7   ? 67  ILE   B N   1 
ATOM   3424 C  CA  . ILE   B 1 82  ? 48.399  -13.4   -15.769 1 86.24  ? 67  ILE   B CA  1 
ATOM   3425 C  C   . ILE   B 1 82  ? 48.665  -14.043 -14.385 1 85.82  ? 67  ILE   B C   1 
ATOM   3426 O  O   . ILE   B 1 82  ? 48.042  -13.635 -13.406 1 85.78  ? 67  ILE   B O   1 
ATOM   3427 C  CB  . ILE   B 1 82  ? 46.931  -13.551 -16.2   1 86.35  ? 67  ILE   B CB  1 
ATOM   3428 N  N   . ASP   B 1 83  ? 49.617  -15.014 -14.303 1 85.29  ? 68  ASP   B N   1 
ATOM   3429 C  CA  . ASP   B 1 83  ? 50      -15.745 -13.097 1 85.16  ? 68  ASP   B CA  1 
ATOM   3430 C  C   . ASP   B 1 83  ? 50.478  -14.861 -11.931 1 85.11  ? 68  ASP   B C   1 
ATOM   3431 O  O   . ASP   B 1 83  ? 50.417  -15.313 -10.791 1 85.4   ? 68  ASP   B O   1 
ATOM   3432 C  CB  . ASP   B 1 83  ? 51.044  -16.819 -13.424 1 86.25  ? 68  ASP   B CB  1 
ATOM   3433 N  N   . HIS   B 1 84  ? 50.915  -13.612 -12.189 1 84.58  ? 69  HIS   B N   1 
ATOM   3434 C  CA  . HIS   B 1 84  ? 51.36   -12.728 -11.105 1 84.62  ? 69  HIS   B CA  1 
ATOM   3435 C  C   . HIS   B 1 84  ? 50.263  -11.814 -10.535 1 83.99  ? 69  HIS   B C   1 
ATOM   3436 O  O   . HIS   B 1 84  ? 50.555  -10.904 -9.758  1 84.06  ? 69  HIS   B O   1 
ATOM   3437 C  CB  . HIS   B 1 84  ? 52.582  -11.921 -11.521 1 86.12  ? 69  HIS   B CB  1 
ATOM   3438 C  CG  . HIS   B 1 84  ? 53.785  -12.784 -11.723 1 88.96  ? 69  HIS   B CG  1 
ATOM   3439 N  ND1 . HIS   B 1 84  ? 53.863  -13.673 -12.782 1 90.75  ? 69  HIS   B ND1 1 
ATOM   3440 C  CD2 . HIS   B 1 84  ? 54.906  -12.895 -10.974 1 90.23  ? 69  HIS   B CD2 1 
ATOM   3441 C  CE1 . HIS   B 1 84  ? 55.03   -14.28  -12.655 1 91.3   ? 69  HIS   B CE1 1 
ATOM   3442 N  NE2 . HIS   B 1 84  ? 55.692  -13.847 -11.58  1 91.33  ? 69  HIS   B NE2 1 
ATOM   3443 N  N   . LEU   B 1 85  ? 49.002  -12.083 -10.885 1 83.21  ? 70  LEU   B N   1 
ATOM   3444 C  CA  . LEU   B 1 85  ? 47.853  -11.368 -10.346 1 82.68  ? 70  LEU   B CA  1 
ATOM   3445 C  C   . LEU   B 1 85  ? 47.226  -12.361 -9.371  1 82.25  ? 70  LEU   B C   1 
ATOM   3446 O  O   . LEU   B 1 85  ? 46.439  -13.208 -9.788  1 82.14  ? 70  LEU   B O   1 
ATOM   3447 C  CB  . LEU   B 1 85  ? 46.876  -11.036 -11.482 1 82.41  ? 70  LEU   B CB  1 
ATOM   3448 C  CG  . LEU   B 1 85  ? 47.45   -10.163 -12.594 1 82.66  ? 70  LEU   B CG  1 
ATOM   3449 C  CD1 . LEU   B 1 85  ? 46.618  -10.254 -13.846 1 82.76  ? 70  LEU   B CD1 1 
ATOM   3450 C  CD2 . LEU   B 1 85  ? 47.602  -8.728  -12.136 1 82.91  ? 70  LEU   B CD2 1 
ATOM   3451 N  N   . THR   B 1 86  ? 47.651  -12.317 -8.095  1 81.87  ? 71  THR   B N   1 
ATOM   3452 C  CA  . THR   B 1 86  ? 47.226  -13.268 -7.066  1 81.99  ? 71  THR   B CA  1 
ATOM   3453 C  C   . THR   B 1 86  ? 45.833  -12.982 -6.484  1 81.85  ? 71  THR   B C   1 
ATOM   3454 O  O   . THR   B 1 86  ? 44.98   -13.877 -6.484  1 82.09  ? 71  THR   B O   1 
ATOM   3455 C  CB  . THR   B 1 86  ? 48.293  -13.372 -5.965  1 83.11  ? 71  THR   B CB  1 
ATOM   3456 N  N   . ASP   B 1 87  ? 45.6    -11.759 -5.974  1 81.08  ? 72  ASP   B N   1 
ATOM   3457 C  CA  . ASP   B 1 87  ? 44.309  -11.428 -5.377  1 80.7   ? 72  ASP   B CA  1 
ATOM   3458 C  C   . ASP   B 1 87  ? 43.276  -10.951 -6.404  1 79.71  ? 72  ASP   B C   1 
ATOM   3459 O  O   . ASP   B 1 87  ? 43.635  -10.593 -7.524  1 80.27  ? 72  ASP   B O   1 
ATOM   3460 C  CB  . ASP   B 1 87  ? 44.472  -10.425 -4.218  1 82.7   ? 72  ASP   B CB  1 
ATOM   3461 C  CG  . ASP   B 1 87  ? 45.331  -9.229  -4.548  1 87.84  ? 72  ASP   B CG  1 
ATOM   3462 O  OD1 . ASP   B 1 87  ? 44.908  -8.415  -5.383  1 89.14  ? 72  ASP   B OD1 1 
ATOM   3463 O  OD2 . ASP   B 1 87  ? 46.423  -9.099  -3.954  1 90.05  ? 72  ASP   B OD2 1 
ATOM   3464 N  N   . HIS   B 1 88  ? 41.994  -10.955 -6.021  1 77.98  ? 73  HIS   B N   1 
ATOM   3465 C  CA  . HIS   B 1 88  ? 40.893  -10.53  -6.877  1 76.49  ? 73  HIS   B CA  1 
ATOM   3466 C  C   . HIS   B 1 88  ? 41      -9.039  -7.244  1 74.69  ? 73  HIS   B C   1 
ATOM   3467 O  O   . HIS   B 1 88  ? 40.71   -8.684  -8.382  1 74.51  ? 73  HIS   B O   1 
ATOM   3468 C  CB  . HIS   B 1 88  ? 39.551  -10.855 -6.184  1 77.05  ? 73  HIS   B CB  1 
ATOM   3469 C  CG  . HIS   B 1 88  ? 38.336  -10.262 -6.833  1 78.73  ? 73  HIS   B CG  1 
ATOM   3470 N  ND1 . HIS   B 1 88  ? 37.815  -10.784 -8.008  1 80.28  ? 73  HIS   B ND1 1 
ATOM   3471 C  CD2 . HIS   B 1 88  ? 37.554  -9.232  -6.428  1 79.58  ? 73  HIS   B CD2 1 
ATOM   3472 C  CE1 . HIS   B 1 88  ? 36.75   -10.048 -8.287  1 80.52  ? 73  HIS   B CE1 1 
ATOM   3473 N  NE2 . HIS   B 1 88  ? 36.549  -9.106  -7.363  1 80.45  ? 73  HIS   B NE2 1 
ATOM   3474 N  N   . LYS   B 1 89  ? 41.444  -8.179  -6.305  1 72.98  ? 74  LYS   B N   1 
ATOM   3475 C  CA  . LYS   B 1 89  ? 41.579  -6.746  -6.569  1 71.85  ? 74  LYS   B CA  1 
ATOM   3476 C  C   . LYS   B 1 89  ? 42.637  -6.423  -7.621  1 71.55  ? 74  LYS   B C   1 
ATOM   3477 O  O   . LYS   B 1 89  ? 42.471  -5.461  -8.376  1 71.89  ? 74  LYS   B O   1 
ATOM   3478 C  CB  . LYS   B 1 89  ? 41.813  -5.949  -5.282  1 72.24  ? 74  LYS   B CB  1 
ATOM   3479 C  CG  . LYS   B 1 89  ? 40.586  -5.903  -4.394  1 74.35  ? 74  LYS   B CG  1 
ATOM   3480 C  CD  . LYS   B 1 89  ? 40.624  -4.732  -3.436  1 76.77  ? 74  LYS   B CD  1 
ATOM   3481 C  CE  . LYS   B 1 89  ? 39.485  -4.785  -2.45   1 79.24  ? 74  LYS   B CE  1 
ATOM   3482 N  NZ  . LYS   B 1 89  ? 39.576  -3.704  -1.431  1 80.7   ? 74  LYS   B NZ  1 
ATOM   3483 N  N   . SER   B 1 90  ? 43.713  -7.229  -7.687  1 70.64  ? 75  SER   B N   1 
ATOM   3484 C  CA  . SER   B 1 90  ? 44.754  -7.046  -8.698  1 70.08  ? 75  SER   B CA  1 
ATOM   3485 C  C   . SER   B 1 90  ? 44.234  -7.513  -10.062 1 69.22  ? 75  SER   B C   1 
ATOM   3486 O  O   . SER   B 1 90  ? 44.512  -6.875  -11.074 1 69.47  ? 75  SER   B O   1 
ATOM   3487 C  CB  . SER   B 1 90  ? 46.032  -7.794  -8.32   1 71.04  ? 75  SER   B CB  1 
ATOM   3488 N  N   . GLN   B 1 91  ? 43.455  -8.602  -10.087 1 68.07  ? 76  GLN   B N   1 
ATOM   3489 C  CA  . GLN   B 1 91  ? 42.837  -9.12   -11.306 1 67.21  ? 76  GLN   B CA  1 
ATOM   3490 C  C   . GLN   B 1 91  ? 41.828  -8.113  -11.881 1 65.71  ? 76  GLN   B C   1 
ATOM   3491 O  O   . GLN   B 1 91  ? 41.716  -7.984  -13.101 1 65.7   ? 76  GLN   B O   1 
ATOM   3492 C  CB  . GLN   B 1 91  ? 42.139  -10.445 -11.004 1 68.73  ? 76  GLN   B CB  1 
ATOM   3493 C  CG  . GLN   B 1 91  ? 43.106  -11.578 -10.759 1 72.88  ? 76  GLN   B CG  1 
ATOM   3494 C  CD  . GLN   B 1 91  ? 42.471  -12.696 -9.97   1 79.48  ? 76  GLN   B CD  1 
ATOM   3495 O  OE1 . GLN   B 1 91  ? 41.258  -12.944 -10.039 1 81.55  ? 76  GLN   B OE1 1 
ATOM   3496 N  NE2 . GLN   B 1 91  ? 43.279  -13.391 -9.183  1 80.41  ? 76  GLN   B NE2 1 
ATOM   3497 N  N   . ARG   B 1 92  ? 41.104  -7.402  -10.999 1 64.27  ? 77  ARG   B N   1 
ATOM   3498 C  CA  . ARG   B 1 92  ? 40.112  -6.397  -11.384 1 63.52  ? 77  ARG   B CA  1 
ATOM   3499 C  C   . ARG   B 1 92  ? 40.783  -5.13   -11.906 1 63.3   ? 77  ARG   B C   1 
ATOM   3500 O  O   . ARG   B 1 92  ? 40.284  -4.518  -12.856 1 63.17  ? 77  ARG   B O   1 
ATOM   3501 C  CB  . ARG   B 1 92  ? 39.16   -6.074  -10.218 1 63.44  ? 77  ARG   B CB  1 
ATOM   3502 C  CG  . ARG   B 1 92  ? 38.121  -7.163  -9.955  1 63.75  ? 77  ARG   B CG  1 
ATOM   3503 C  CD  . ARG   B 1 92  ? 37.051  -7.254  -11.034 1 64.65  ? 77  ARG   B CD  1 
ATOM   3504 N  NE  . ARG   B 1 92  ? 36.284  -6.012  -11.15  1 65.51  ? 77  ARG   B NE  1 
ATOM   3505 C  CZ  . ARG   B 1 92  ? 35.229  -5.705  -10.401 1 66.46  ? 77  ARG   B CZ  1 
ATOM   3506 N  NH1 . ARG   B 1 92  ? 34.781  -6.562  -9.49   1 66.42  ? 77  ARG   B NH1 1 
ATOM   3507 N  NH2 . ARG   B 1 92  ? 34.608  -4.543  -10.563 1 65.21  ? 77  ARG   B NH2 1 
ATOM   3508 N  N   . LEU   B 1 93  ? 41.924  -4.746  -11.299 1 63.02  ? 78  LEU   B N   1 
ATOM   3509 C  CA  . LEU   B 1 93  ? 42.71   -3.587  -11.741 1 62.46  ? 78  LEU   B CA  1 
ATOM   3510 C  C   . LEU   B 1 93  ? 43.323  -3.908  -13.101 1 61.86  ? 78  LEU   B C   1 
ATOM   3511 O  O   . LEU   B 1 93  ? 43.251  -3.081  -13.997 1 61.73  ? 78  LEU   B O   1 
ATOM   3512 C  CB  . LEU   B 1 93  ? 43.811  -3.225  -10.735 1 62.36  ? 78  LEU   B CB  1 
ATOM   3513 C  CG  . LEU   B 1 93  ? 44.767  -2.099  -11.155 1 63.41  ? 78  LEU   B CG  1 
ATOM   3514 C  CD1 . LEU   B 1 93  ? 44.02   -0.795  -11.44  1 63.88  ? 78  LEU   B CD1 1 
ATOM   3515 C  CD2 . LEU   B 1 93  ? 45.84   -1.889  -10.124 1 63.76  ? 78  LEU   B CD2 1 
ATOM   3516 N  N   . ALA   B 1 94  ? 43.855  -5.131  -13.278 1 61.32  ? 79  ALA   B N   1 
ATOM   3517 C  CA  . ALA   B 1 94  ? 44.437  -5.539  -14.553 1 61.21  ? 79  ALA   B CA  1 
ATOM   3518 C  C   . ALA   B 1 94  ? 43.392  -5.54   -15.667 1 61.15  ? 79  ALA   B C   1 
ATOM   3519 O  O   . ALA   B 1 94  ? 43.73   -5.216  -16.807 1 61.84  ? 79  ALA   B O   1 
ATOM   3520 C  CB  . ALA   B 1 94  ? 45.097  -6.903  -14.435 1 61.03  ? 79  ALA   B CB  1 
ATOM   3521 N  N   . ARG   B 1 95  ? 42.123  -5.849  -15.337 1 59.86  ? 80  ARG   B N   1 
ATOM   3522 C  CA  . ARG   B 1 95  ? 41.014  -5.831  -16.292 1 58.85  ? 80  ARG   B CA  1 
ATOM   3523 C  C   . ARG   B 1 95  ? 40.717  -4.396  -16.746 1 58.44  ? 80  ARG   B C   1 
ATOM   3524 O  O   . ARG   B 1 95  ? 40.415  -4.16   -17.911 1 58.83  ? 80  ARG   B O   1 
ATOM   3525 C  CB  . ARG   B 1 95  ? 39.758  -6.43   -15.643 1 58.81  ? 80  ARG   B CB  1 
ATOM   3526 C  CG  . ARG   B 1 95  ? 39.378  -7.768  -16.242 1 59.22  ? 80  ARG   B CG  1 
ATOM   3527 C  CD  . ARG   B 1 95  ? 37.934  -8.105  -15.969 1 58.96  ? 80  ARG   B CD  1 
ATOM   3528 N  NE  . ARG   B 1 95  ? 37.001  -7.319  -16.777 1 58.55  ? 80  ARG   B NE  1 
ATOM   3529 C  CZ  . ARG   B 1 95  ? 36.641  -7.626  -18.02  1 57.37  ? 80  ARG   B CZ  1 
ATOM   3530 N  NH1 . ARG   B 1 95  ? 37.186  -8.666  -18.64  1 54.83  ? 80  ARG   B NH1 1 
ATOM   3531 N  NH2 . ARG   B 1 95  ? 35.758  -6.873  -18.667 1 56.06  ? 80  ARG   B NH2 1 
ATOM   3532 N  N   . LEU   B 1 96  ? 40.772  -3.453  -15.81  1 57.75  ? 81  LEU   B N   1 
ATOM   3533 C  CA  . LEU   B 1 96  ? 40.542  -2.048  -16.063 1 58.08  ? 81  LEU   B CA  1 
ATOM   3534 C  C   . LEU   B 1 96  ? 41.724  -1.487  -16.893 1 59.74  ? 81  LEU   B C   1 
ATOM   3535 O  O   . LEU   B 1 96  ? 41.503  -0.811  -17.903 1 60.67  ? 81  LEU   B O   1 
ATOM   3536 C  CB  . LEU   B 1 96  ? 40.388  -1.33   -14.713 1 57.45  ? 81  LEU   B CB  1 
ATOM   3537 C  CG  . LEU   B 1 96  ? 40.343  0.186   -14.722 1 58.19  ? 81  LEU   B CG  1 
ATOM   3538 C  CD1 . LEU   B 1 96  ? 39.219  0.709   -15.58  1 58.88  ? 81  LEU   B CD1 1 
ATOM   3539 C  CD2 . LEU   B 1 96  ? 40.221  0.721   -13.327 1 58.46  ? 81  LEU   B CD2 1 
ATOM   3540 N  N   . VAL   B 1 97  ? 42.965  -1.82   -16.503 1 59.4   ? 82  VAL   B N   1 
ATOM   3541 C  CA  . VAL   B 1 97  ? 44.169  -1.41   -17.208 1 59.65  ? 82  VAL   B CA  1 
ATOM   3542 C  C   . VAL   B 1 97  ? 44.144  -1.929  -18.656 1 60.12  ? 82  VAL   B C   1 
ATOM   3543 O  O   . VAL   B 1 97  ? 44.17   -1.118  -19.576 1 59.81  ? 82  VAL   B O   1 
ATOM   3544 C  CB  . VAL   B 1 97  ? 45.444  -1.841  -16.427 1 60.27  ? 82  VAL   B CB  1 
ATOM   3545 C  CG1 . VAL   B 1 97  ? 46.693  -1.806  -17.308 1 60.93  ? 82  VAL   B CG1 1 
ATOM   3546 C  CG2 . VAL   B 1 97  ? 45.638  -0.984  -15.184 1 60.45  ? 82  VAL   B CG2 1 
ATOM   3547 N  N   . LEU   B 1 98  ? 44.035  -3.257  -18.858 1 60.8   ? 83  LEU   B N   1 
ATOM   3548 C  CA  . LEU   B 1 98  ? 43.999  -3.866  -20.196 1 61.84  ? 83  LEU   B CA  1 
ATOM   3549 C  C   . LEU   B 1 98  ? 42.791  -3.435  -21.015 1 62.84  ? 83  LEU   B C   1 
ATOM   3550 O  O   . LEU   B 1 98  ? 42.886  -3.301  -22.234 1 63.2   ? 83  LEU   B O   1 
ATOM   3551 C  CB  . LEU   B 1 98  ? 44.01   -5.39   -20.101 1 62.19  ? 83  LEU   B CB  1 
ATOM   3552 C  CG  . LEU   B 1 98  ? 45.276  -6.027  -19.558 1 63.94  ? 83  LEU   B CG  1 
ATOM   3553 C  CD1 . LEU   B 1 98  ? 45.108  -7.516  -19.436 1 64.43  ? 83  LEU   B CD1 1 
ATOM   3554 C  CD2 . LEU   B 1 98  ? 46.465  -5.721  -20.448 1 64.82  ? 83  LEU   B CD2 1 
ATOM   3555 N  N   . GLY   B 1 99  ? 41.664  -3.231  -20.346 1 63.06  ? 84  GLY   B N   1 
ATOM   3556 C  CA  . GLY   B 1 99  ? 40.445  -2.805  -21.012 1 63.69  ? 84  GLY   B CA  1 
ATOM   3557 C  C   . GLY   B 1 99  ? 40.555  -1.397  -21.552 1 64.11  ? 84  GLY   B C   1 
ATOM   3558 O  O   . GLY   B 1 99  ? 40.125  -1.14   -22.677 1 64.72  ? 84  GLY   B O   1 
ATOM   3559 N  N   . CYS   B 1 100 ? 41.148  -0.479  -20.761 1 63.56  ? 85  CYS   B N   1 
ATOM   3560 C  CA  . CYS   B 1 100 ? 41.363  0.913   -21.167 1 63.82  ? 85  CYS   B CA  1 
ATOM   3561 C  C   . CYS   B 1 100 ? 42.361  0.991   -22.328 1 64.48  ? 85  CYS   B C   1 
ATOM   3562 O  O   . CYS   B 1 100 ? 42.218  1.836   -23.208 1 64.28  ? 85  CYS   B O   1 
ATOM   3563 C  CB  . CYS   B 1 100 ? 41.833  1.754   -19.985 1 63.76  ? 85  CYS   B CB  1 
ATOM   3564 S  SG  . CYS   B 1 100 ? 40.556  2.086   -18.751 1 65.46  ? 85  CYS   B SG  1 
ATOM   3565 N  N   . ILE   B 1 101 ? 43.385  0.124   -22.31  1 64.76  ? 86  ILE   B N   1 
ATOM   3566 C  CA  . ILE   B 1 101 ? 44.375  0.086   -23.366 1 65.43  ? 86  ILE   B CA  1 
ATOM   3567 C  C   . ILE   B 1 101 ? 43.738  -0.473  -24.643 1 65.88  ? 86  ILE   B C   1 
ATOM   3568 O  O   . ILE   B 1 101 ? 43.975  0.062   -25.721 1 66.22  ? 86  ILE   B O   1 
ATOM   3569 C  CB  . ILE   B 1 101 ? 45.631  -0.706  -22.917 1 66.06  ? 86  ILE   B CB  1 
ATOM   3570 C  CG1 . ILE   B 1 101 ? 46.338  -0.002  -21.734 1 66.91  ? 86  ILE   B CG1 1 
ATOM   3571 C  CG2 . ILE   B 1 101 ? 46.594  -0.901  -24.077 1 66.45  ? 86  ILE   B CG2 1 
ATOM   3572 C  CD1 . ILE   B 1 101 ? 47.363  -0.878  -21.018 1 68.01  ? 86  ILE   B CD1 1 
ATOM   3573 N  N   . THR   B 1 102 ? 42.898  -1.51   -24.524 1 65.63  ? 87  THR   B N   1 
ATOM   3574 C  CA  . THR   B 1 102 ? 42.227  -2.101  -25.676 1 66.19  ? 87  THR   B CA  1 
ATOM   3575 C  C   . THR   B 1 102 ? 41.298  -1.1    -26.371 1 67.18  ? 87  THR   B C   1 
ATOM   3576 O  O   . THR   B 1 102 ? 41.321  -0.997  -27.594 1 67.3   ? 87  THR   B O   1 
ATOM   3577 C  CB  . THR   B 1 102 ? 41.496  -3.369  -25.267 1 66.95  ? 87  THR   B CB  1 
ATOM   3578 O  OG1 . THR   B 1 102 ? 42.433  -4.287  -24.702 1 67.4   ? 87  THR   B OG1 1 
ATOM   3579 C  CG2 . THR   B 1 102 ? 40.745  -4.007  -26.43  1 67.17  ? 87  THR   B CG2 1 
ATOM   3580 N  N   . MET   B 1 103 ? 40.525  -0.321  -25.596 1 67.76  ? 88  MET   B N   1 
ATOM   3581 C  CA  . MET   B 1 103 ? 39.631  0.683   -26.174 1 68.57  ? 88  MET   B CA  1 
ATOM   3582 C  C   . MET   B 1 103 ? 40.434  1.759   -26.893 1 69.42  ? 88  MET   B C   1 
ATOM   3583 O  O   . MET   B 1 103 ? 40.08   2.157   -28     1 69.59  ? 88  MET   B O   1 
ATOM   3584 C  CB  . MET   B 1 103 ? 38.729  1.316   -25.096 1 69.34  ? 88  MET   B CB  1 
ATOM   3585 C  CG  . MET   B 1 103 ? 37.798  0.327   -24.409 1 71.72  ? 88  MET   B CG  1 
ATOM   3586 S  SD  . MET   B 1 103 ? 36.763  -0.654  -25.53  1 75.63  ? 88  MET   B SD  1 
ATOM   3587 C  CE  . MET   B 1 103 ? 35.174  -0.408  -24.79  1 77.28  ? 88  MET   B CE  1 
ATOM   3588 N  N   . ALA   B 1 104 ? 41.538  2.2     -26.28  1 69.7   ? 89  ALA   B N   1 
ATOM   3589 C  CA  . ALA   B 1 104 ? 42.403  3.215   -26.855 1 70.49  ? 89  ALA   B CA  1 
ATOM   3590 C  C   . ALA   B 1 104 ? 43.111  2.7     -28.12  1 71.05  ? 89  ALA   B C   1 
ATOM   3591 O  O   . ALA   B 1 104 ? 43.31   3.465   -29.055 1 71.18  ? 89  ALA   B O   1 
ATOM   3592 C  CB  . ALA   B 1 104 ? 43.423  3.656   -25.825 1 70.81  ? 89  ALA   B CB  1 
ATOM   3593 N  N   . TYR   B 1 105 ? 43.491  1.42    -28.148 1 71.07  ? 90  TYR   B N   1 
ATOM   3594 C  CA  . TYR   B 1 105 ? 44.16   0.832   -29.299 1 71.57  ? 90  TYR   B CA  1 
ATOM   3595 C  C   . TYR   B 1 105 ? 43.195  0.707   -30.477 1 71.52  ? 90  TYR   B C   1 
ATOM   3596 O  O   . TYR   B 1 105 ? 43.555  1.042   -31.602 1 71.84  ? 90  TYR   B O   1 
ATOM   3597 C  CB  . TYR   B 1 105 ? 44.77   -0.543  -28.945 1 72.02  ? 90  TYR   B CB  1 
ATOM   3598 C  CG  . TYR   B 1 105 ? 45.565  -1.149  -30.083 1 73.48  ? 90  TYR   B CG  1 
ATOM   3599 C  CD1 . TYR   B 1 105 ? 46.914  -0.869  -30.241 1 74.74  ? 90  TYR   B CD1 1 
ATOM   3600 C  CD2 . TYR   B 1 105 ? 44.965  -1.991  -31.008 1 74.64  ? 90  TYR   B CD2 1 
ATOM   3601 C  CE1 . TYR   B 1 105 ? 47.64   -1.394  -31.305 1 75.79  ? 90  TYR   B CE1 1 
ATOM   3602 C  CE2 . TYR   B 1 105 ? 45.672  -2.497  -32.089 1 75.69  ? 90  TYR   B CE2 1 
ATOM   3603 C  CZ  . TYR   B 1 105 ? 47.014  -2.211  -32.227 1 76.86  ? 90  TYR   B CZ  1 
ATOM   3604 O  OH  . TYR   B 1 105 ? 47.716  -2.761  -33.273 1 78.67  ? 90  TYR   B OH  1 
ATOM   3605 N  N   . VAL   B 1 106 ? 41.985  0.204   -30.229 1 70.99  ? 91  VAL   B N   1 
ATOM   3606 C  CA  . VAL   B 1 106 ? 41.005  0.015   -31.289 1 70.94  ? 91  VAL   B CA  1 
ATOM   3607 C  C   . VAL   B 1 106 ? 40.549  1.337   -31.897 1 71.16  ? 91  VAL   B C   1 
ATOM   3608 O  O   . VAL   B 1 106 ? 40.443  1.432   -33.115 1 71.12  ? 91  VAL   B O   1 
ATOM   3609 C  CB  . VAL   B 1 106 ? 39.815  -0.853  -30.813 1 71.21  ? 91  VAL   B CB  1 
ATOM   3610 C  CG1 . VAL   B 1 106 ? 38.694  -0.875  -31.839 1 71.81  ? 91  VAL   B CG1 1 
ATOM   3611 C  CG2 . VAL   B 1 106 ? 40.271  -2.271  -30.508 1 71.63  ? 91  VAL   B CG2 1 
ATOM   3612 N  N   . TRP   B 1 107 ? 40.314  2.36    -31.066 1 71.2   ? 92  TRP   B N   1 
ATOM   3613 C  CA  . TRP   B 1 107 ? 39.782  3.621   -31.566 1 72.09  ? 92  TRP   B CA  1 
ATOM   3614 C  C   . TRP   B 1 107 ? 40.823  4.672   -31.897 1 73.36  ? 92  TRP   B C   1 
ATOM   3615 O  O   . TRP   B 1 107 ? 40.549  5.547   -32.716 1 73.58  ? 92  TRP   B O   1 
ATOM   3616 C  CB  . TRP   B 1 107 ? 38.714  4.192   -30.606 1 71.89  ? 92  TRP   B CB  1 
ATOM   3617 C  CG  . TRP   B 1 107 ? 37.588  3.234   -30.307 1 72.13  ? 92  TRP   B CG  1 
ATOM   3618 C  CD1 . TRP   B 1 107 ? 37.238  2.736   -29.085 1 72.78  ? 92  TRP   B CD1 1 
ATOM   3619 C  CD2 . TRP   B 1 107 ? 36.689  2.635   -31.256 1 72.07  ? 92  TRP   B CD2 1 
ATOM   3620 N  NE1 . TRP   B 1 107 ? 36.182  1.863   -29.215 1 72.94  ? 92  TRP   B NE1 1 
ATOM   3621 C  CE2 . TRP   B 1 107 ? 35.827  1.784   -30.537 1 72.79  ? 92  TRP   B CE2 1 
ATOM   3622 C  CE3 . TRP   B 1 107 ? 36.54   2.726   -32.647 1 72.53  ? 92  TRP   B CE3 1 
ATOM   3623 C  CZ2 . TRP   B 1 107 ? 34.829  1.035   -31.162 1 73.61  ? 92  TRP   B CZ2 1 
ATOM   3624 C  CZ3 . TRP   B 1 107 ? 35.56   1.976   -33.264 1 73.48  ? 92  TRP   B CZ3 1 
ATOM   3625 C  CH2 . TRP   B 1 107 ? 34.705  1.157   -32.523 1 73.79  ? 92  TRP   B CH2 1 
ATOM   3626 N  N   . GLY   B 1 108 ? 41.994  4.596   -31.277 1 73.96  ? 93  GLY   B N   1 
ATOM   3627 C  CA  . GLY   B 1 108 ? 43.06   5.568   -31.49  1 74.89  ? 93  GLY   B CA  1 
ATOM   3628 C  C   . GLY   B 1 108 ? 42.627  6.97    -31.117 1 75.98  ? 93  GLY   B C   1 
ATOM   3629 O  O   . GLY   B 1 108 ? 42.081  7.185   -30.035 1 76.04  ? 93  GLY   B O   1 
ATOM   3630 N  N   . LYS   B 1 109 ? 42.795  7.921   -32.041 1 76.82  ? 94  LYS   B N   1 
ATOM   3631 C  CA  . LYS   B 1 109 ? 42.341  9.299   -31.809 1 77.92  ? 94  LYS   B CA  1 
ATOM   3632 C  C   . LYS   B 1 109 ? 40.799  9.46    -31.937 1 79.04  ? 94  LYS   B C   1 
ATOM   3633 O  O   . LYS   B 1 109 ? 40.266  10.517  -31.611 1 78.78  ? 94  LYS   B O   1 
ATOM   3634 C  CB  . LYS   B 1 109 ? 43.093  10.286  -32.714 1 79.36  ? 94  LYS   B CB  1 
ATOM   3635 N  N   . GLY   B 1 110 ? 40.116  8.408   -32.396 1 80.09  ? 95  GLY   B N   1 
ATOM   3636 C  CA  . GLY   B 1 110 ? 38.669  8.358   -32.533 1 81.65  ? 95  GLY   B CA  1 
ATOM   3637 C  C   . GLY   B 1 110 ? 38.093  9.16    -33.674 1 83.18  ? 95  GLY   B C   1 
ATOM   3638 O  O   . GLY   B 1 110 ? 36.897  9.462   -33.678 1 83.77  ? 95  GLY   B O   1 
ATOM   3639 N  N   . HIS   B 1 111 ? 38.927  9.504   -34.65  1 83.64  ? 96  HIS   B N   1 
ATOM   3640 C  CA  . HIS   B 1 111 ? 38.483  10.297  -35.779 1 84.41  ? 96  HIS   B CA  1 
ATOM   3641 C  C   . HIS   B 1 111 ? 38.502  9.479   -37.07  1 84.85  ? 96  HIS   B C   1 
ATOM   3642 O  O   . HIS   B 1 111 ? 38.908  9.991   -38.115 1 85.09  ? 96  HIS   B O   1 
ATOM   3643 C  CB  . HIS   B 1 111 ? 39.34   11.566  -35.893 1 85.16  ? 96  HIS   B CB  1 
ATOM   3644 N  N   . GLY   B 1 112 ? 38.082  8.217   -36.991 1 84.69  ? 97  GLY   B N   1 
ATOM   3645 C  CA  . GLY   B 1 112 ? 38.038  7.365   -38.173 1 85.21  ? 97  GLY   B CA  1 
ATOM   3646 C  C   . GLY   B 1 112 ? 38.892  6.109   -38.197 1 85.51  ? 97  GLY   B C   1 
ATOM   3647 O  O   . GLY   B 1 112 ? 38.344  5.014   -38.339 1 85.72  ? 97  GLY   B O   1 
ATOM   3648 N  N   . ASP   B 1 113 ? 40.239  6.248   -38.137 1 85.29  ? 98  ASP   B N   1 
ATOM   3649 C  CA  . ASP   B 1 113 ? 41.163  5.107   -38.229 1 85.38  ? 98  ASP   B CA  1 
ATOM   3650 C  C   . ASP   B 1 113 ? 41.017  4.087   -37.105 1 84.92  ? 98  ASP   B C   1 
ATOM   3651 O  O   . ASP   B 1 113 ? 41.513  4.307   -36.005 1 85.37  ? 98  ASP   B O   1 
ATOM   3652 C  CB  . ASP   B 1 113 ? 42.622  5.565   -38.348 1 86.78  ? 98  ASP   B CB  1 
ATOM   3653 N  N   . VAL   B 1 114 ? 40.362  2.959   -37.401 1 83.88  ? 99  VAL   B N   1 
ATOM   3654 C  CA  . VAL   B 1 114 ? 40.133  1.895   -36.437 1 83.22  ? 99  VAL   B CA  1 
ATOM   3655 C  C   . VAL   B 1 114 ? 41.118  0.749   -36.636 1 82.96  ? 99  VAL   B C   1 
ATOM   3656 O  O   . VAL   B 1 114 ? 41.491  0.453   -37.764 1 83.32  ? 99  VAL   B O   1 
ATOM   3657 C  CB  . VAL   B 1 114 ? 38.679  1.389   -36.546 1 83.44  ? 99  VAL   B CB  1 
ATOM   3658 N  N   . ARG   B 1 115 ? 41.529  0.093   -35.546 1 82.27  ? 100 ARG   B N   1 
ATOM   3659 C  CA  . ARG   B 1 115 ? 42.395  -1.08   -35.623 1 81.9   ? 100 ARG   B CA  1 
ATOM   3660 C  C   . ARG   B 1 115 ? 41.48   -2.292  -35.499 1 81.53  ? 100 ARG   B C   1 
ATOM   3661 O  O   . ARG   B 1 115 ? 40.759  -2.406  -34.511 1 81.91  ? 100 ARG   B O   1 
ATOM   3662 C  CB  . ARG   B 1 115 ? 43.434  -1.082  -34.492 1 82.94  ? 100 ARG   B CB  1 
ATOM   3663 N  N   . LYS   B 1 116 ? 41.463  -3.172  -36.505 1 80.78  ? 101 LYS   B N   1 
ATOM   3664 C  CA  . LYS   B 1 116 ? 40.592  -4.35   -36.48  1 80.46  ? 101 LYS   B CA  1 
ATOM   3665 C  C   . LYS   B 1 116 ? 41.233  -5.6    -35.829 1 79.78  ? 101 LYS   B C   1 
ATOM   3666 O  O   . LYS   B 1 116 ? 40.556  -6.612  -35.667 1 79.67  ? 101 LYS   B O   1 
ATOM   3667 C  CB  . LYS   B 1 116 ? 40.072  -4.664  -37.896 1 82.06  ? 101 LYS   B CB  1 
ATOM   3668 N  N   . VAL   B 1 117 ? 42.519  -5.533  -35.453 1 79.35  ? 102 VAL   B N   1 
ATOM   3669 C  CA  . VAL   B 1 117 ? 43.196  -6.669  -34.824 1 79.51  ? 102 VAL   B CA  1 
ATOM   3670 C  C   . VAL   B 1 117 ? 43.893  -6.261  -33.53  1 79.6   ? 102 VAL   B C   1 
ATOM   3671 O  O   . VAL   B 1 117 ? 44.677  -5.316  -33.525 1 79.85  ? 102 VAL   B O   1 
ATOM   3672 C  CB  . VAL   B 1 117 ? 44.19   -7.36   -35.788 1 80.09  ? 102 VAL   B CB  1 
ATOM   3673 N  N   . LEU   B 1 118 ? 43.628  -6.977  -32.439 1 79.23  ? 103 LEU   B N   1 
ATOM   3674 C  CA  . LEU   B 1 118 ? 44.274  -6.703  -31.158 1 79.13  ? 103 LEU   B CA  1 
ATOM   3675 C  C   . LEU   B 1 118 ? 45.503  -7.599  -31.065 1 79.55  ? 103 LEU   B C   1 
ATOM   3676 O  O   . LEU   B 1 118 ? 45.375  -8.82   -31.145 1 79.55  ? 103 LEU   B O   1 
ATOM   3677 C  CB  . LEU   B 1 118 ? 43.31   -6.984  -29.996 1 78.73  ? 103 LEU   B CB  1 
ATOM   3678 C  CG  . LEU   B 1 118 ? 43.74   -6.451  -28.639 1 79.48  ? 103 LEU   B CG  1 
ATOM   3679 C  CD1 . LEU   B 1 118 ? 43.84   -4.936  -28.642 1 79.5   ? 103 LEU   B CD1 1 
ATOM   3680 C  CD2 . LEU   B 1 118 ? 42.786  -6.899  -27.568 1 80.21  ? 103 LEU   B CD2 1 
ATOM   3681 N  N   . PRO   B 1 119 ? 46.707  -7.007  -30.942 1 79.74  ? 104 PRO   B N   1 
ATOM   3682 C  CA  . PRO   B 1 119 ? 47.939  -7.823  -30.898 1 80.01  ? 104 PRO   B CA  1 
ATOM   3683 C  C   . PRO   B 1 119 ? 47.947  -8.894  -29.812 1 80.6   ? 104 PRO   B C   1 
ATOM   3684 O  O   . PRO   B 1 119 ? 47.409  -8.662  -28.745 1 81     ? 104 PRO   B O   1 
ATOM   3685 C  CB  . PRO   B 1 119 ? 49.044  -6.788  -30.678 1 80.62  ? 104 PRO   B CB  1 
ATOM   3686 C  CG  . PRO   B 1 119 ? 48.34   -5.537  -30.223 1 80.95  ? 104 PRO   B CG  1 
ATOM   3687 C  CD  . PRO   B 1 119 ? 47.003  -5.566  -30.861 1 79.29  ? 104 PRO   B CD  1 
ATOM   3688 N  N   . ARG   B 1 120 ? 48.556  -10.055 -30.077 1 80.64  ? 105 ARG   B N   1 
ATOM   3689 C  CA  . ARG   B 1 120 ? 48.562  -11.175 -29.141 1 81.12  ? 105 ARG   B CA  1 
ATOM   3690 C  C   . ARG   B 1 120 ? 49.233  -10.875 -27.809 1 81.38  ? 105 ARG   B C   1 
ATOM   3691 O  O   . ARG   B 1 120 ? 48.769  -11.369 -26.783 1 81.79  ? 105 ARG   B O   1 
ATOM   3692 C  CB  . ARG   B 1 120 ? 49.161  -12.436 -29.781 1 82.25  ? 105 ARG   B CB  1 
ATOM   3693 N  N   . ASN   B 1 121 ? 50.285  -10.045 -27.803 1 80.98  ? 106 ASN   B N   1 
ATOM   3694 C  CA  . ASN   B 1 121 ? 50.982  -9.698  -26.567 1 81.04  ? 106 ASN   B CA  1 
ATOM   3695 C  C   . ASN   B 1 121 ? 50.071  -9.01   -25.514 1 80.89  ? 106 ASN   B C   1 
ATOM   3696 O  O   . ASN   B 1 121 ? 50.413  -8.982  -24.323 1 81.11  ? 106 ASN   B O   1 
ATOM   3697 C  CB  . ASN   B 1 121 ? 52.23   -8.875  -26.868 1 82.11  ? 106 ASN   B CB  1 
ATOM   3698 N  N   . ILE   B 1 122 ? 48.899  -8.494  -25.946 1 80.25  ? 107 ILE   B N   1 
ATOM   3699 C  CA  . ILE   B 1 122 ? 47.913  -7.902  -25.044 1 79.88  ? 107 ILE   B CA  1 
ATOM   3700 C  C   . ILE   B 1 122 ? 46.602  -8.712  -25.054 1 79.23  ? 107 ILE   B C   1 
ATOM   3701 O  O   . ILE   B 1 122 ? 46.055  -8.973  -23.987 1 79.11  ? 107 ILE   B O   1 
ATOM   3702 C  CB  . ILE   B 1 122 ? 47.689  -6.385  -25.264 1 80.35  ? 107 ILE   B CB  1 
ATOM   3703 C  CG1 . ILE   B 1 122 ? 46.798  -5.809  -24.144 1 81.46  ? 107 ILE   B CG1 1 
ATOM   3704 C  CG2 . ILE   B 1 122 ? 47.109  -6.092  -26.646 1 80.82  ? 107 ILE   B CG2 1 
ATOM   3705 C  CD1 . ILE   B 1 122 ? 46.617  -4.359  -24.143 1 82.62  ? 107 ILE   B CD1 1 
ATOM   3706 N  N   . ALA   B 1 123 ? 46.137  -9.161  -26.239 1 78.71  ? 108 ALA   B N   1 
ATOM   3707 C  CA  . ALA   B 1 123 ? 44.903  -9.934  -26.395 1 78.77  ? 108 ALA   B CA  1 
ATOM   3708 C  C   . ALA   B 1 123 ? 44.923  -11.29  -25.697 1 78.86  ? 108 ALA   B C   1 
ATOM   3709 O  O   . ALA   B 1 123 ? 43.889  -11.716 -25.186 1 79.01  ? 108 ALA   B O   1 
ATOM   3710 C  CB  . ALA   B 1 123 ? 44.569  -10.115 -27.868 1 78.87  ? 108 ALA   B CB  1 
ATOM   3711 N  N   . VAL   B 1 124 ? 46.07   -11.984 -25.699 1 78.77  ? 109 VAL   B N   1 
ATOM   3712 C  CA  . VAL   B 1 124 ? 46.164  -13.288 -25.042 1 79.07  ? 109 VAL   B CA  1 
ATOM   3713 C  C   . VAL   B 1 124 ? 45.955  -13.151 -23.523 1 79     ? 109 VAL   B C   1 
ATOM   3714 O  O   . VAL   B 1 124 ? 44.992  -13.729 -23.014 1 78.93  ? 109 VAL   B O   1 
ATOM   3715 C  CB  . VAL   B 1 124 ? 47.435  -14.094 -25.415 1 79.64  ? 109 VAL   B CB  1 
ATOM   3716 N  N   . PRO   B 1 125 ? 46.759  -12.341 -22.79  1 78.69  ? 110 PRO   B N   1 
ATOM   3717 C  CA  . PRO   B 1 125 ? 46.515  -12.206 -21.344 1 78.57  ? 110 PRO   B CA  1 
ATOM   3718 C  C   . PRO   B 1 125 ? 45.195  -11.513 -20.99  1 78.31  ? 110 PRO   B C   1 
ATOM   3719 O  O   . PRO   B 1 125 ? 44.652  -11.778 -19.913 1 78.82  ? 110 PRO   B O   1 
ATOM   3720 C  CB  . PRO   B 1 125 ? 47.739  -11.438 -20.829 1 79.29  ? 110 PRO   B CB  1 
ATOM   3721 C  CG  . PRO   B 1 125 ? 48.306  -10.762 -22     1 79.67  ? 110 PRO   B CG  1 
ATOM   3722 C  CD  . PRO   B 1 125 ? 47.953  -11.578 -23.21  1 78.2   ? 110 PRO   B CD  1 
ATOM   3723 N  N   . TYR   B 1 126 ? 44.658  -10.658 -21.889 1 77.1   ? 111 TYR   B N   1 
ATOM   3724 C  CA  . TYR   B 1 126 ? 43.38   -10.005 -21.624 1 76.33  ? 111 TYR   B CA  1 
ATOM   3725 C  C   . TYR   B 1 126 ? 42.276  -11.057 -21.641 1 75.26  ? 111 TYR   B C   1 
ATOM   3726 O  O   . TYR   B 1 126 ? 41.493  -11.11  -20.696 1 75.36  ? 111 TYR   B O   1 
ATOM   3727 C  CB  . TYR   B 1 126 ? 43.092  -8.877  -22.627 1 76.32  ? 111 TYR   B CB  1 
ATOM   3728 C  CG  . TYR   B 1 126 ? 41.895  -8.013  -22.274 1 77.25  ? 111 TYR   B CG  1 
ATOM   3729 C  CD1 . TYR   B 1 126 ? 41.518  -7.815  -20.951 1 78.39  ? 111 TYR   B CD1 1 
ATOM   3730 C  CD2 . TYR   B 1 126 ? 41.192  -7.331  -23.255 1 78.09  ? 111 TYR   B CD2 1 
ATOM   3731 C  CE1 . TYR   B 1 126 ? 40.436  -7.006  -20.62  1 79.34  ? 111 TYR   B CE1 1 
ATOM   3732 C  CE2 . TYR   B 1 126 ? 40.125  -6.499  -22.934 1 79.02  ? 111 TYR   B CE2 1 
ATOM   3733 C  CZ  . TYR   B 1 126 ? 39.738  -6.352  -21.615 1 80     ? 111 TYR   B CZ  1 
ATOM   3734 O  OH  . TYR   B 1 126 ? 38.675  -5.549  -21.28  1 81.14  ? 111 TYR   B OH  1 
ATOM   3735 N  N   . CYS   B 1 127 ? 42.251  -11.927 -22.669 1 73.8   ? 112 CYS   B N   1 
ATOM   3736 C  CA  . CYS   B 1 127 ? 41.253  -12.985 -22.764 1 73.05  ? 112 CYS   B CA  1 
ATOM   3737 C  C   . CYS   B 1 127 ? 41.43   -14.059 -21.689 1 72.65  ? 112 CYS   B C   1 
ATOM   3738 O  O   . CYS   B 1 127 ? 40.459  -14.69  -21.289 1 72.73  ? 112 CYS   B O   1 
ATOM   3739 C  CB  . CYS   B 1 127 ? 41.256  -13.601 -24.151 1 73.55  ? 112 CYS   B CB  1 
ATOM   3740 S  SG  . CYS   B 1 127 ? 40.784  -12.476 -25.481 1 77.93  ? 112 CYS   B SG  1 
ATOM   3741 N  N   . GLN   B 1 128 ? 42.665  -14.282 -21.241 1 72.12  ? 113 GLN   B N   1 
ATOM   3742 C  CA  . GLN   B 1 128 ? 42.963  -15.256 -20.204 1 71.81  ? 113 GLN   B CA  1 
ATOM   3743 C  C   . GLN   B 1 128 ? 42.389  -14.765 -18.871 1 71.25  ? 113 GLN   B C   1 
ATOM   3744 O  O   . GLN   B 1 128 ? 41.657  -15.506 -18.225 1 71     ? 113 GLN   B O   1 
ATOM   3745 C  CB  . GLN   B 1 128 ? 44.483  -15.49  -20.111 1 72.93  ? 113 GLN   B CB  1 
ATOM   3746 N  N   . LEU   B 1 129 ? 42.681  -13.503 -18.495 1 70.91  ? 114 LEU   B N   1 
ATOM   3747 C  CA  . LEU   B 1 129 ? 42.199  -12.851 -17.269 1 71     ? 114 LEU   B CA  1 
ATOM   3748 C  C   . LEU   B 1 129 ? 40.672  -12.683 -17.304 1 71     ? 114 LEU   B C   1 
ATOM   3749 O  O   . LEU   B 1 129 ? 40.003  -12.857 -16.284 1 71.33  ? 114 LEU   B O   1 
ATOM   3750 C  CB  . LEU   B 1 129 ? 42.88   -11.489 -17.125 1 71.06  ? 114 LEU   B CB  1 
ATOM   3751 C  CG  . LEU   B 1 129 ? 42.463  -10.621 -15.95  1 72.19  ? 114 LEU   B CG  1 
ATOM   3752 C  CD1 . LEU   B 1 129 ? 42.952  -11.19  -14.642 1 72.65  ? 114 LEU   B CD1 1 
ATOM   3753 C  CD2 . LEU   B 1 129 ? 42.983  -9.229  -16.125 1 72.63  ? 114 LEU   B CD2 1 
ATOM   3754 N  N   . SER   B 1 130 ? 40.124  -12.392 -18.488 1 70.21  ? 115 SER   B N   1 
ATOM   3755 C  CA  . SER   B 1 130 ? 38.693  -12.27  -18.694 1 69.85  ? 115 SER   B CA  1 
ATOM   3756 C  C   . SER   B 1 130 ? 38.014  -13.612 -18.481 1 69.86  ? 115 SER   B C   1 
ATOM   3757 O  O   . SER   B 1 130 ? 36.931  -13.646 -17.913 1 70.47  ? 115 SER   B O   1 
ATOM   3758 C  CB  . SER   B 1 130 ? 38.4    -11.766 -20.103 1 70.48  ? 115 SER   B CB  1 
ATOM   3759 O  OG  . SER   B 1 130 ? 38.805  -10.415 -20.226 1 72.28  ? 115 SER   B OG  1 
ATOM   3760 N  N   . LYS   B 1 131 ? 38.628  -14.713 -18.945 1 69.12  ? 116 LYS   B N   1 
ATOM   3761 C  CA  . LYS   B 1 131 ? 38.075  -16.057 -18.769 1 68.91  ? 116 LYS   B CA  1 
ATOM   3762 C  C   . LYS   B 1 131 ? 38.092  -16.456 -17.289 1 68.72  ? 116 LYS   B C   1 
ATOM   3763 O  O   . LYS   B 1 131 ? 37.145  -17.088 -16.818 1 69.19  ? 116 LYS   B O   1 
ATOM   3764 C  CB  . LYS   B 1 131 ? 38.839  -17.094 -19.616 1 70.24  ? 116 LYS   B CB  1 
ATOM   3765 C  CG  . LYS   B 1 131 ? 38.189  -18.48  -19.634 1 73.08  ? 116 LYS   B CG  1 
ATOM   3766 C  CD  . LYS   B 1 131 ? 38.855  -19.427 -20.615 1 76.79  ? 116 LYS   B CD  1 
ATOM   3767 N  N   . LYS   B 1 132 ? 39.137  -16.064 -16.553 1 67.97  ? 117 LYS   B N   1 
ATOM   3768 C  CA  . LYS   B 1 132 ? 39.226  -16.377 -15.135 1 68.28  ? 117 LYS   B CA  1 
ATOM   3769 C  C   . LYS   B 1 132 ? 38.107  -15.674 -14.364 1 68.41  ? 117 LYS   B C   1 
ATOM   3770 O  O   . LYS   B 1 132 ? 37.425  -16.306 -13.561 1 68.53  ? 117 LYS   B O   1 
ATOM   3771 C  CB  . LYS   B 1 132 ? 40.606  -15.994 -14.574 1 70.11  ? 117 LYS   B CB  1 
ATOM   3772 C  CG  . LYS   B 1 132 ? 40.989  -16.768 -13.316 1 74.38  ? 117 LYS   B CG  1 
ATOM   3773 C  CD  . LYS   B 1 132 ? 42.295  -16.253 -12.723 1 79.06  ? 117 LYS   B CD  1 
ATOM   3774 N  N   . LEU   B 1 133 ? 37.886  -14.384 -14.652 1 68.14  ? 118 LEU   B N   1 
ATOM   3775 C  CA  . LEU   B 1 133 ? 36.868  -13.569 -13.993 1 67.98  ? 118 LEU   B CA  1 
ATOM   3776 C  C   . LEU   B 1 133 ? 35.457  -13.697 -14.578 1 67.31  ? 118 LEU   B C   1 
ATOM   3777 O  O   . LEU   B 1 133 ? 34.566  -12.989 -14.128 1 67.64  ? 118 LEU   B O   1 
ATOM   3778 C  CB  . LEU   B 1 133 ? 37.292  -12.088 -13.98  1 68.25  ? 118 LEU   B CB  1 
ATOM   3779 C  CG  . LEU   B 1 133 ? 38.492  -11.727 -13.113 1 69.82  ? 118 LEU   B CG  1 
ATOM   3780 C  CD1 . LEU   B 1 133 ? 38.784  -10.259 -13.2   1 70.5   ? 118 LEU   B CD1 1 
ATOM   3781 C  CD2 . LEU   B 1 133 ? 38.243  -12.064 -11.659 1 70.56  ? 118 LEU   B CD2 1 
ATOM   3782 N  N   . GLU   B 1 134 ? 35.256  -14.561 -15.575 1 66.45  ? 119 GLU   B N   1 
ATOM   3783 C  CA  . GLU   B 1 134 ? 33.966  -14.776 -16.237 1 66.34  ? 119 GLU   B CA  1 
ATOM   3784 C  C   . GLU   B 1 134 ? 33.361  -13.506 -16.847 1 65.86  ? 119 GLU   B C   1 
ATOM   3785 O  O   . GLU   B 1 134 ? 32.139  -13.338 -16.864 1 66.46  ? 119 GLU   B O   1 
ATOM   3786 C  CB  . GLU   B 1 134 ? 32.959  -15.473 -15.318 1 68.69  ? 119 GLU   B CB  1 
ATOM   3787 C  CG  . GLU   B 1 134 ? 33.466  -16.768 -14.716 1 74.2   ? 119 GLU   B CG  1 
ATOM   3788 C  CD  . GLU   B 1 134 ? 32.425  -17.428 -13.833 1 80.99  ? 119 GLU   B CD  1 
ATOM   3789 O  OE1 . GLU   B 1 134 ? 31.246  -17.484 -14.259 1 83.1   ? 119 GLU   B OE1 1 
ATOM   3790 O  OE2 . GLU   B 1 134 ? 32.78   -17.865 -12.712 1 81.4   ? 119 GLU   B OE2 1 
ATOM   3791 N  N   . LEU   B 1 135 ? 34.207  -12.624 -17.354 1 64.83  ? 120 LEU   B N   1 
ATOM   3792 C  CA  . LEU   B 1 135 ? 33.765  -11.391 -17.997 1 64.64  ? 120 LEU   B CA  1 
ATOM   3793 C  C   . LEU   B 1 135 ? 34.271  -11.336 -19.45  1 64.71  ? 120 LEU   B C   1 
ATOM   3794 O  O   . LEU   B 1 135 ? 35.273  -11.977 -19.766 1 65.13  ? 120 LEU   B O   1 
ATOM   3795 C  CB  . LEU   B 1 135 ? 34.287  -10.194 -17.198 1 64.46  ? 120 LEU   B CB  1 
ATOM   3796 C  CG  . LEU   B 1 135 ? 33.559  -9.926  -15.896 1 65.14  ? 120 LEU   B CG  1 
ATOM   3797 C  CD1 . LEU   B 1 135 ? 34.405  -9.078  -14.971 1 65.42  ? 120 LEU   B CD1 1 
ATOM   3798 C  CD2 . LEU   B 1 135 ? 32.222  -9.28   -16.156 1 65.25  ? 120 LEU   B CD2 1 
ATOM   3799 N  N   . PRO   B 1 136 ? 33.605  -10.599 -20.361 1 64.24  ? 121 PRO   B N   1 
ATOM   3800 C  CA  . PRO   B 1 136 ? 34.088  -10.546 -21.751 1 63.76  ? 121 PRO   B CA  1 
ATOM   3801 C  C   . PRO   B 1 136 ? 35.365  -9.727  -21.897 1 62.65  ? 121 PRO   B C   1 
ATOM   3802 O  O   . PRO   B 1 136 ? 35.633  -8.852  -21.079 1 62.77  ? 121 PRO   B O   1 
ATOM   3803 C  CB  . PRO   B 1 136 ? 32.92   -9.89   -22.515 1 64.87  ? 121 PRO   B CB  1 
ATOM   3804 C  CG  . PRO   B 1 136 ? 31.756  -9.923  -21.567 1 65.61  ? 121 PRO   B CG  1 
ATOM   3805 C  CD  . PRO   B 1 136 ? 32.378  -9.804  -20.205 1 64.04  ? 121 PRO   B CD  1 
ATOM   3806 N  N   . PRO   B 1 137 ? 36.17   -9.987  -22.948 1 61.44  ? 122 PRO   B N   1 
ATOM   3807 C  CA  . PRO   B 1 137 ? 37.386  -9.192  -23.145 1 60.07  ? 122 PRO   B CA  1 
ATOM   3808 C  C   . PRO   B 1 137 ? 37.092  -7.834  -23.786 1 58.76  ? 122 PRO   B C   1 
ATOM   3809 O  O   . PRO   B 1 137 ? 37.558  -7.522  -24.88  1 59.31  ? 122 PRO   B O   1 
ATOM   3810 C  CB  . PRO   B 1 137 ? 38.247  -10.084 -24.033 1 61.01  ? 122 PRO   B CB  1 
ATOM   3811 C  CG  . PRO   B 1 137 ? 37.277  -10.879 -24.828 1 61.94  ? 122 PRO   B CG  1 
ATOM   3812 C  CD  . PRO   B 1 137 ? 36.018  -11.017 -23.996 1 60.79  ? 122 PRO   B CD  1 
ATOM   3813 N  N   . ILE   B 1 138 ? 36.329  -7.016  -23.078 1 56.99  ? 123 ILE   B N   1 
ATOM   3814 C  CA  . ILE   B 1 138 ? 35.982  -5.645  -23.436 1 55.83  ? 123 ILE   B CA  1 
ATOM   3815 C  C   . ILE   B 1 138 ? 35.743  -4.867  -22.129 1 54.44  ? 123 ILE   B C   1 
ATOM   3816 O  O   . ILE   B 1 138 ? 35.385  -5.452  -21.107 1 54.41  ? 123 ILE   B O   1 
ATOM   3817 C  CB  . ILE   B 1 138 ? 34.796  -5.535  -24.445 1 55.57  ? 123 ILE   B CB  1 
ATOM   3818 C  CG1 . ILE   B 1 138 ? 34.717  -4.115  -25.061 1 55.77  ? 123 ILE   B CG1 1 
ATOM   3819 C  CG2 . ILE   B 1 138 ? 33.472  -5.97   -23.814 1 55.68  ? 123 ILE   B CG2 1 
ATOM   3820 C  CD1 . ILE   B 1 138 ? 33.737  -3.945  -26.187 1 56.68  ? 123 ILE   B CD1 1 
ATOM   3821 N  N   . LEU   B 1 139 ? 36.01   -3.565  -22.146 1 52.91  ? 124 LEU   B N   1 
ATOM   3822 C  CA  . LEU   B 1 139 ? 35.807  -2.714  -20.984 1 51.88  ? 124 LEU   B CA  1 
ATOM   3823 C  C   . LEU   B 1 139 ? 34.305  -2.682  -20.627 1 51.41  ? 124 LEU   B C   1 
ATOM   3824 O  O   . LEU   B 1 139 ? 33.464  -2.404  -21.493 1 51.61  ? 124 LEU   B O   1 
ATOM   3825 C  CB  . LEU   B 1 139 ? 36.3    -1.303  -21.311 1 51.42  ? 124 LEU   B CB  1 
ATOM   3826 C  CG  . LEU   B 1 139 ? 36.558  -0.392  -20.136 1 52.56  ? 124 LEU   B CG  1 
ATOM   3827 C  CD1 . LEU   B 1 139 ? 37.684  -0.941  -19.261 1 52.46  ? 124 LEU   B CD1 1 
ATOM   3828 C  CD2 . LEU   B 1 139 ? 36.868  1.008   -20.613 1 53.52  ? 124 LEU   B CD2 1 
ATOM   3829 N  N   . VAL   B 1 140 ? 33.968  -3.055  -19.381 1 50.23  ? 125 VAL   B N   1 
ATOM   3830 C  CA  . VAL   B 1 140 ? 32.577  -3.062  -18.919 1 49.52  ? 125 VAL   B CA  1 
ATOM   3831 C  C   . VAL   B 1 140 ? 32.357  -1.992  -17.818 1 49.99  ? 125 VAL   B C   1 
ATOM   3832 O  O   . VAL   B 1 140 ? 33.315  -1.414  -17.31  1 50.25  ? 125 VAL   B O   1 
ATOM   3833 C  CB  . VAL   B 1 140 ? 32.089  -4.485  -18.49  1 48.79  ? 125 VAL   B CB  1 
ATOM   3834 C  CG1 . VAL   B 1 140 ? 32.254  -5.497  -19.617 1 49.01  ? 125 VAL   B CG1 1 
ATOM   3835 C  CG2 . VAL   B 1 140 ? 32.783  -4.961  -17.213 1 48.6   ? 125 VAL   B CG2 1 
ATOM   3836 N  N   . TYR   B 1 141 ? 31.092  -1.732  -17.454 1 49.92  ? 126 TYR   B N   1 
ATOM   3837 C  CA  . TYR   B 1 141 ? 30.682  -0.82   -16.39  1 49.86  ? 126 TYR   B CA  1 
ATOM   3838 C  C   . TYR   B 1 141 ? 31.406  -1.183  -15.075 1 50.73  ? 126 TYR   B C   1 
ATOM   3839 O  O   . TYR   B 1 141 ? 31.823  -0.297  -14.339 1 50.93  ? 126 TYR   B O   1 
ATOM   3840 C  CB  . TYR   B 1 141 ? 29.163  -0.964  -16.218 1 49.2   ? 126 TYR   B CB  1 
ATOM   3841 C  CG  . TYR   B 1 141 ? 28.537  -0.08   -15.167 1 49.49  ? 126 TYR   B CG  1 
ATOM   3842 C  CD1 . TYR   B 1 141 ? 28.146  1.216   -15.467 1 50.42  ? 126 TYR   B CD1 1 
ATOM   3843 C  CD2 . TYR   B 1 141 ? 28.229  -0.575  -13.908 1 50.13  ? 126 TYR   B CD2 1 
ATOM   3844 C  CE1 . TYR   B 1 141 ? 27.527  2.022   -14.52  1 51.36  ? 126 TYR   B CE1 1 
ATOM   3845 C  CE2 . TYR   B 1 141 ? 27.616  0.22    -12.951 1 51.21  ? 126 TYR   B CE2 1 
ATOM   3846 C  CZ  . TYR   B 1 141 ? 27.27   1.525   -13.257 1 52.44  ? 126 TYR   B CZ  1 
ATOM   3847 O  OH  . TYR   B 1 141 ? 26.632  2.322   -12.329 1 54.3   ? 126 TYR   B OH  1 
ATOM   3848 N  N   . ALA   B 1 142 ? 31.588  -2.487  -14.805 1 51.07  ? 127 ALA   B N   1 
ATOM   3849 C  CA  . ALA   B 1 142 ? 32.26   -2.951  -13.598 1 52.18  ? 127 ALA   B CA  1 
ATOM   3850 C  C   . ALA   B 1 142 ? 33.751  -2.588  -13.56  1 53.9   ? 127 ALA   B C   1 
ATOM   3851 O  O   . ALA   B 1 142 ? 34.337  -2.51   -12.474 1 54.62  ? 127 ALA   B O   1 
ATOM   3852 C  CB  . ALA   B 1 142 ? 32.062  -4.451  -13.421 1 51.87  ? 127 ALA   B CB  1 
ATOM   3853 N  N   . ASP   B 1 143 ? 34.36   -2.343  -14.735 1 53.98  ? 128 ASP   B N   1 
ATOM   3854 C  CA  . ASP   B 1 143 ? 35.753  -1.937  -14.804 1 54.09  ? 128 ASP   B CA  1 
ATOM   3855 C  C   . ASP   B 1 143 ? 35.85   -0.408  -14.662 1 54.43  ? 128 ASP   B C   1 
ATOM   3856 O  O   . ASP   B 1 143 ? 36.407  0.069   -13.674 1 54.93  ? 128 ASP   B O   1 
ATOM   3857 C  CB  . ASP   B 1 143 ? 36.425  -2.389  -16.124 1 54.57  ? 128 ASP   B CB  1 
ATOM   3858 C  CG  . ASP   B 1 143 ? 36.31   -3.847  -16.491 1 57.54  ? 128 ASP   B CG  1 
ATOM   3859 O  OD1 . ASP   B 1 143 ? 36.525  -4.696  -15.615 1 58.27  ? 128 ASP   B OD1 1 
ATOM   3860 O  OD2 . ASP   B 1 143 ? 36.044  -4.138  -17.671 1 59.57  ? 128 ASP   B OD2 1 
ATOM   3861 N  N   . CYS   B 1 144 ? 35.298  0.363   -15.624 1 53.95  ? 129 CYS   B N   1 
ATOM   3862 C  CA  . CYS   B 1 144 ? 35.463  1.811   -15.615 1 54.56  ? 129 CYS   B CA  1 
ATOM   3863 C  C   . CYS   B 1 144 ? 34.571  2.565   -14.647 1 54.93  ? 129 CYS   B C   1 
ATOM   3864 O  O   . CYS   B 1 144 ? 34.8    3.761   -14.474 1 55.47  ? 129 CYS   B O   1 
ATOM   3865 C  CB  . CYS   B 1 144 ? 35.338  2.38    -17.019 1 55.7   ? 129 CYS   B CB  1 
ATOM   3866 S  SG  . CYS   B 1 144 ? 33.802  1.929   -17.843 1 60.69  ? 129 CYS   B SG  1 
ATOM   3867 N  N   . VAL   B 1 145 ? 33.583  1.921   -14.014 1 54.61  ? 130 VAL   B N   1 
ATOM   3868 C  CA  . VAL   B 1 145 ? 32.765  2.623   -13.03  1 54.74  ? 130 VAL   B CA  1 
ATOM   3869 C  C   . VAL   B 1 145 ? 32.99   2.03    -11.644 1 55.34  ? 130 VAL   B C   1 
ATOM   3870 O  O   . VAL   B 1 145 ? 33.516  2.713   -10.768 1 55.7   ? 130 VAL   B O   1 
ATOM   3871 C  CB  . VAL   B 1 145 ? 31.273  2.75    -13.413 1 55.07  ? 130 VAL   B CB  1 
ATOM   3872 C  CG1 . VAL   B 1 145 ? 30.452  3.311   -12.258 1 55.6   ? 130 VAL   B CG1 1 
ATOM   3873 C  CG2 . VAL   B 1 145 ? 31.096  3.596   -14.669 1 55.19  ? 130 VAL   B CG2 1 
ATOM   3874 N  N   . LEU   B 1 146 ? 32.697  0.74    -11.47  1 55.35  ? 131 LEU   B N   1 
ATOM   3875 C  CA  . LEU   B 1 146 ? 32.788  0.092   -10.161 1 55.71  ? 131 LEU   B CA  1 
ATOM   3876 C  C   . LEU   B 1 146 ? 34.217  -0.104  -9.623  1 56.73  ? 131 LEU   B C   1 
ATOM   3877 O  O   . LEU   B 1 146 ? 34.39   -0.11   -8.407  1 57.21  ? 131 LEU   B O   1 
ATOM   3878 C  CB  . LEU   B 1 146 ? 32.014  -1.244  -10.158 1 54.95  ? 131 LEU   B CB  1 
ATOM   3879 C  CG  . LEU   B 1 146 ? 30.589  -1.186  -10.703 1 54.74  ? 131 LEU   B CG  1 
ATOM   3880 C  CD1 . LEU   B 1 146 ? 29.961  -2.538  -10.715 1 54.97  ? 131 LEU   B CD1 1 
ATOM   3881 C  CD2 . LEU   B 1 146 ? 29.724  -0.208  -9.919  1 54.77  ? 131 LEU   B CD2 1 
ATOM   3882 N  N   . ALA   B 1 147 ? 35.227  -0.251  -10.493 1 57.01  ? 132 ALA   B N   1 
ATOM   3883 C  CA  . ALA   B 1 147 ? 36.611  -0.434  -10.033 1 57.94  ? 132 ALA   B CA  1 
ATOM   3884 C  C   . ALA   B 1 147 ? 37.54   0.769   -10.343 1 59.31  ? 132 ALA   B C   1 
ATOM   3885 O  O   . ALA   B 1 147 ? 38.671  0.795   -9.88   1 59.51  ? 132 ALA   B O   1 
ATOM   3886 C  CB  . ALA   B 1 147 ? 37.198  -1.712  -10.627 1 57.74  ? 132 ALA   B CB  1 
ATOM   3887 N  N   . ASN   B 1 148 ? 37.063  1.754   -11.11  1 60.16  ? 133 ASN   B N   1 
ATOM   3888 C  CA  . ASN   B 1 148 ? 37.853  2.901   -11.531 1 61.71  ? 133 ASN   B CA  1 
ATOM   3889 C  C   . ASN   B 1 148 ? 37.743  4.097   -10.58  1 64.17  ? 133 ASN   B C   1 
ATOM   3890 O  O   . ASN   B 1 148 ? 37.418  5.207   -11.018 1 64.37  ? 133 ASN   B O   1 
ATOM   3891 C  CB  . ASN   B 1 148 ? 37.419  3.278   -12.948 1 61.73  ? 133 ASN   B CB  1 
ATOM   3892 C  CG  . ASN   B 1 148 ? 38.33   4.2     -13.697 1 62.41  ? 133 ASN   B CG  1 
ATOM   3893 O  OD1 . ASN   B 1 148 ? 39.515  4.33    -13.397 1 62.44  ? 133 ASN   B OD1 1 
ATOM   3894 N  ND2 . ASN   B 1 148 ? 37.781  4.838   -14.704 1 62.76  ? 133 ASN   B ND2 1 
ATOM   3895 N  N   . TRP   B 1 149 ? 38.04   3.891   -9.288  1 65.96  ? 134 TRP   B N   1 
ATOM   3896 C  CA  . TRP   B 1 149 ? 37.935  4.986   -8.327  1 68.45  ? 134 TRP   B CA  1 
ATOM   3897 C  C   . TRP   B 1 149 ? 38.883  4.858   -7.136  1 70.36  ? 134 TRP   B C   1 
ATOM   3898 O  O   . TRP   B 1 149 ? 39.444  3.787   -6.888  1 70.53  ? 134 TRP   B O   1 
ATOM   3899 C  CB  . TRP   B 1 149 ? 36.475  5.152   -7.869  1 68.94  ? 134 TRP   B CB  1 
ATOM   3900 C  CG  . TRP   B 1 149 ? 35.955  4.006   -7.056  1 70.36  ? 134 TRP   B CG  1 
ATOM   3901 C  CD1 . TRP   B 1 149 ? 35.411  2.845   -7.523  1 71.47  ? 134 TRP   B CD1 1 
ATOM   3902 C  CD2 . TRP   B 1 149 ? 35.907  3.926   -5.623  1 71.19  ? 134 TRP   B CD2 1 
ATOM   3903 N  NE1 . TRP   B 1 149 ? 35.04   2.038   -6.47   1 71.98  ? 134 TRP   B NE1 1 
ATOM   3904 C  CE2 . TRP   B 1 149 ? 35.318  2.688   -5.291  1 72.05  ? 134 TRP   B CE2 1 
ATOM   3905 C  CE3 . TRP   B 1 149 ? 36.288  4.792   -4.586  1 72.1   ? 134 TRP   B CE3 1 
ATOM   3906 C  CZ2 . TRP   B 1 149 ? 35.116  2.29    -3.963  1 72.83  ? 134 TRP   B CZ2 1 
ATOM   3907 C  CZ3 . TRP   B 1 149 ? 36.107  4.385   -3.276  1 72.98  ? 134 TRP   B CZ3 1 
ATOM   3908 C  CH2 . TRP   B 1 149 ? 35.526  3.148   -2.976  1 73.02  ? 134 TRP   B CH2 1 
ATOM   3909 N  N   . LYS   B 1 150 ? 39.071  5.971   -6.411  1 71.62  ? 135 LYS   B N   1 
ATOM   3910 C  CA  . LYS   B 1 150 ? 39.915  6.034   -5.221  1 73.54  ? 135 LYS   B CA  1 
ATOM   3911 C  C   . LYS   B 1 150 ? 39.491  7.206   -4.332  1 75.22  ? 135 LYS   B C   1 
ATOM   3912 O  O   . LYS   B 1 150 ? 38.92   8.194   -4.812  1 75.33  ? 135 LYS   B O   1 
ATOM   3913 C  CB  . LYS   B 1 150 ? 41.401  6.197   -5.608  1 75.42  ? 135 LYS   B CB  1 
ATOM   3914 C  CG  . LYS   B 1 150 ? 41.668  7.427   -6.475  1 79.52  ? 135 LYS   B CG  1 
ATOM   3915 C  CD  . LYS   B 1 150 ? 43.142  7.789   -6.526  1 83.8   ? 135 LYS   B CD  1 
ATOM   3916 N  N   . LYS   B 1 151 ? 39.788  7.108   -3.033  1 76.17  ? 136 LYS   B N   1 
ATOM   3917 C  CA  . LYS   B 1 151 ? 39.541  8.213   -2.113  1 77.61  ? 136 LYS   B CA  1 
ATOM   3918 C  C   . LYS   B 1 151 ? 40.844  9.043   -2.068  1 79.21  ? 136 LYS   B C   1 
ATOM   3919 O  O   . LYS   B 1 151 ? 41.933  8.472   -1.933  1 79.6   ? 136 LYS   B O   1 
ATOM   3920 C  CB  . LYS   B 1 151 ? 39.227  7.677   -0.713  1 79.11  ? 136 LYS   B CB  1 
ATOM   3921 C  CG  . LYS   B 1 151 ? 37.771  7.78    -0.292  1 82.11  ? 136 LYS   B CG  1 
ATOM   3922 C  CD  . LYS   B 1 151 ? 37.628  7.327   1.152   1 85.41  ? 136 LYS   B CD  1 
ATOM   3923 C  CE  . LYS   B 1 151 ? 36.202  7.269   1.632   1 88.29  ? 136 LYS   B CE  1 
ATOM   3924 N  NZ  . LYS   B 1 151 ? 36.155  7.053   3.101   1 90.22  ? 136 LYS   B NZ  1 
ATOM   3925 N  N   . LYS   B 1 152 ? 40.746  10.373  -2.215  1 79.98  ? 137 LYS   B N   1 
ATOM   3926 C  CA  . LYS   B 1 152 ? 41.911  11.268  -2.147  1 81.02  ? 137 LYS   B CA  1 
ATOM   3927 C  C   . LYS   B 1 152 ? 42.47   11.204  -0.717  1 82.89  ? 137 LYS   B C   1 
ATOM   3928 O  O   . LYS   B 1 152 ? 43.658  10.954  -0.531  1 83.19  ? 137 LYS   B O   1 
ATOM   3929 C  CB  . LYS   B 1 152 ? 41.518  12.711  -2.516  1 81.16  ? 137 LYS   B CB  1 
ATOM   3930 C  CG  . LYS   B 1 152 ? 41.23   12.927  -3.993  1 82.05  ? 137 LYS   B CG  1 
ATOM   3931 C  CD  . LYS   B 1 152 ? 40.542  14.258  -4.209  1 83.66  ? 137 LYS   B CD  1 
ATOM   3932 C  CE  . LYS   B 1 152 ? 40.518  14.656  -5.655  1 85.83  ? 137 LYS   B CE  1 
ATOM   3933 N  NZ  . LYS   B 1 152 ? 39.652  15.839  -5.863  1 87.31  ? 137 LYS   B NZ  1 
ATOM   3934 N  N   . ASP   B 1 153 ? 41.584  11.334  0.282   1 83.94  ? 138 ASP   B N   1 
ATOM   3935 C  CA  . ASP   B 1 153 ? 41.909  11.216  1.698   1 85.56  ? 138 ASP   B CA  1 
ATOM   3936 C  C   . ASP   B 1 153 ? 41.071  10.062  2.264   1 87.12  ? 138 ASP   B C   1 
ATOM   3937 O  O   . ASP   B 1 153 ? 39.838  10.151  2.314   1 87.3   ? 138 ASP   B O   1 
ATOM   3938 C  CB  . ASP   B 1 153 ? 41.583  12.53   2.438   1 87.06  ? 138 ASP   B CB  1 
ATOM   3939 C  CG  . ASP   B 1 153 ? 41.783  12.493  3.945   1 90.58  ? 138 ASP   B CG  1 
ATOM   3940 O  OD1 . ASP   B 1 153 ? 42.507  11.589  4.431   1 90.68  ? 138 ASP   B OD1 1 
ATOM   3941 O  OD2 . ASP   B 1 153 ? 41.211  13.365  4.641   1 92.53  ? 138 ASP   B OD2 1 
ATOM   3942 N  N   . PRO   B 1 154 ? 41.728  8.979   2.706   1 87.89  ? 139 PRO   B N   1 
ATOM   3943 C  CA  . PRO   B 1 154 ? 40.976  7.838   3.26    1 88.62  ? 139 PRO   B CA  1 
ATOM   3944 C  C   . PRO   B 1 154 ? 40.154  8.17    4.511   1 89.89  ? 139 PRO   B C   1 
ATOM   3945 O  O   . PRO   B 1 154 ? 39.153  7.507   4.79    1 90.21  ? 139 PRO   B O   1 
ATOM   3946 C  CB  . PRO   B 1 154 ? 42.065  6.798   3.56    1 89.27  ? 139 PRO   B CB  1 
ATOM   3947 C  CG  . PRO   B 1 154 ? 43.275  7.236   2.783   1 89.54  ? 139 PRO   B CG  1 
ATOM   3948 C  CD  . PRO   B 1 154 ? 43.182  8.729   2.698   1 87.75  ? 139 PRO   B CD  1 
ATOM   3949 N  N   . ASN   B 1 155 ? 40.566  9.198   5.262   1 90.34  ? 140 ASN   B N   1 
ATOM   3950 C  CA  . ASN   B 1 155 ? 39.858  9.613   6.47    1 91.05  ? 140 ASN   B CA  1 
ATOM   3951 C  C   . ASN   B 1 155 ? 38.613  10.471  6.178   1 91.68  ? 140 ASN   B C   1 
ATOM   3952 O  O   . ASN   B 1 155 ? 37.777  10.644  7.064   1 92.19  ? 140 ASN   B O   1 
ATOM   3953 C  CB  . ASN   B 1 155 ? 40.807  10.322  7.44    1 91.98  ? 140 ASN   B CB  1 
ATOM   3954 N  N   . LYS   B 1 156 ? 38.479  11.002  4.952   1 91.48  ? 141 LYS   B N   1 
ATOM   3955 C  CA  . LYS   B 1 156 ? 37.321  11.816  4.573   1 91.82  ? 141 LYS   B CA  1 
ATOM   3956 C  C   . LYS   B 1 156 ? 36.22   10.926  3.937   1 91.98  ? 141 LYS   B C   1 
ATOM   3957 O  O   . LYS   B 1 156 ? 36.523  9.816   3.495   1 92.54  ? 141 LYS   B O   1 
ATOM   3958 C  CB  . LYS   B 1 156 ? 37.759  12.974  3.658   1 93.4   ? 141 LYS   B CB  1 
ATOM   3959 N  N   . PRO   B 1 157 ? 34.942  11.355  3.897   1 91.31  ? 142 PRO   B N   1 
ATOM   3960 C  CA  . PRO   B 1 157 ? 33.883  10.476  3.372   1 91.04  ? 142 PRO   B CA  1 
ATOM   3961 C  C   . PRO   B 1 157 ? 33.824  10.279  1.847   1 90.58  ? 142 PRO   B C   1 
ATOM   3962 O  O   . PRO   B 1 157 ? 34.55   10.929  1.092   1 90.83  ? 142 PRO   B O   1 
ATOM   3963 C  CB  . PRO   B 1 157 ? 32.608  11.152  3.891   1 91.78  ? 142 PRO   B CB  1 
ATOM   3964 C  CG  . PRO   B 1 157 ? 32.954  12.589  3.903   1 92.27  ? 142 PRO   B CG  1 
ATOM   3965 C  CD  . PRO   B 1 157 ? 34.373  12.616  4.41    1 90.78  ? 142 PRO   B CD  1 
ATOM   3966 N  N   . LEU   B 1 158 ? 32.924  9.379   1.395   1 89.52  ? 143 LEU   B N   1 
ATOM   3967 C  CA  . LEU   B 1 158 ? 32.702  9.088   -0.014  1 88.9   ? 143 LEU   B CA  1 
ATOM   3968 C  C   . LEU   B 1 158 ? 31.863  10.184  -0.659  1 88.42  ? 143 LEU   B C   1 
ATOM   3969 O  O   . LEU   B 1 158 ? 30.671  10.01   -0.909  1 88.58  ? 143 LEU   B O   1 
ATOM   3970 C  CB  . LEU   B 1 158 ? 32.011  7.731   -0.185  1 88.99  ? 143 LEU   B CB  1 
ATOM   3971 C  CG  . LEU   B 1 158 ? 32.905  6.518   -0.136  1 90.42  ? 143 LEU   B CG  1 
ATOM   3972 C  CD1 . LEU   B 1 158 ? 32.081  5.247   -0.114  1 90.91  ? 143 LEU   B CD1 1 
ATOM   3973 C  CD2 . LEU   B 1 158 ? 33.865  6.522   -1.303  1 91.11  ? 143 LEU   B CD2 1 
ATOM   3974 N  N   . THR   B 1 159 ? 32.49   11.321  -0.919  1 87.67  ? 144 THR   B N   1 
ATOM   3975 C  CA  . THR   B 1 159 ? 31.856  12.459  -1.573  1 87.22  ? 144 THR   B CA  1 
ATOM   3976 C  C   . THR   B 1 159 ? 32.655  12.788  -2.843  1 86.21  ? 144 THR   B C   1 
ATOM   3977 O  O   . THR   B 1 159 ? 33.813  12.384  -2.958  1 86.27  ? 144 THR   B O   1 
ATOM   3978 C  CB  . THR   B 1 159 ? 31.756  13.631  -0.591  1 88.9   ? 144 THR   B CB  1 
ATOM   3979 O  OG1 . THR   B 1 159 ? 30.845  14.61   -1.094  1 90.25  ? 144 THR   B OG1 1 
ATOM   3980 C  CG2 . THR   B 1 159 ? 33.12   14.242  -0.253  1 89.37  ? 144 THR   B CG2 1 
ATOM   3981 N  N   . TYR   B 1 160 ? 32.05   13.499  -3.806  1 85.3   ? 145 TYR   B N   1 
ATOM   3982 C  CA  . TYR   B 1 160 ? 32.734  13.823  -5.065  1 85.03  ? 145 TYR   B CA  1 
ATOM   3983 C  C   . TYR   B 1 160 ? 34.065  14.541  -4.852  1 84.58  ? 145 TYR   B C   1 
ATOM   3984 O  O   . TYR   B 1 160 ? 35.068  14.197  -5.488  1 84.68  ? 145 TYR   B O   1 
ATOM   3985 C  CB  . TYR   B 1 160 ? 31.825  14.645  -5.989  1 85.18  ? 145 TYR   B CB  1 
ATOM   3986 C  CG  . TYR   B 1 160 ? 32.367  14.762  -7.398  1 85.96  ? 145 TYR   B CG  1 
ATOM   3987 C  CD1 . TYR   B 1 160 ? 31.991  13.865  -8.386  1 86.9   ? 145 TYR   B CD1 1 
ATOM   3988 C  CD2 . TYR   B 1 160 ? 33.26   15.768  -7.74   1 86.77  ? 145 TYR   B CD2 1 
ATOM   3989 C  CE1 . TYR   B 1 160 ? 32.496  13.96   -9.675  1 87.74  ? 145 TYR   B CE1 1 
ATOM   3990 C  CE2 . TYR   B 1 160 ? 33.794  15.855  -9.017  1 87.55  ? 145 TYR   B CE2 1 
ATOM   3991 C  CZ  . TYR   B 1 160 ? 33.391  14.964  -9.989  1 88.53  ? 145 TYR   B CZ  1 
ATOM   3992 O  OH  . TYR   B 1 160 ? 33.901  15.064  -11.256 1 89.88  ? 145 TYR   B OH  1 
ATOM   3993 N  N   . GLU   B 1 161 ? 34.078  15.504  -3.913  1 83.84  ? 146 GLU   B N   1 
ATOM   3994 C  CA  . GLU   B 1 161 ? 35.26   16.297  -3.591  1 83.34  ? 146 GLU   B CA  1 
ATOM   3995 C  C   . GLU   B 1 161 ? 36.422  15.457  -3.083  1 82.37  ? 146 GLU   B C   1 
ATOM   3996 O  O   . GLU   B 1 161 ? 37.574  15.806  -3.328  1 82.79  ? 146 GLU   B O   1 
ATOM   3997 C  CB  . GLU   B 1 161 ? 34.903  17.405  -2.594  1 85.6   ? 146 GLU   B CB  1 
ATOM   3998 N  N   . ASN   B 1 162 ? 36.132  14.336  -2.414  1 81.08  ? 147 ASN   B N   1 
ATOM   3999 C  CA  . ASN   B 1 162 ? 37.174  13.465  -1.877  1 80.52  ? 147 ASN   B CA  1 
ATOM   4000 C  C   . ASN   B 1 162 ? 37.474  12.246  -2.772  1 79.8   ? 147 ASN   B C   1 
ATOM   4001 O  O   . ASN   B 1 162 ? 38.121  11.3    -2.311  1 80.02  ? 147 ASN   B O   1 
ATOM   4002 C  CB  . ASN   B 1 162 ? 36.785  13.013  -0.464  1 81.34  ? 147 ASN   B CB  1 
ATOM   4003 C  CG  . ASN   B 1 162 ? 37.843  12.21   0.227   1 84.18  ? 147 ASN   B CG  1 
ATOM   4004 O  OD1 . ASN   B 1 162 ? 39.015  12.572  0.233   1 85.08  ? 147 ASN   B OD1 1 
ATOM   4005 N  ND2 . ASN   B 1 162 ? 37.461  11.075  0.779   1 85.4   ? 147 ASN   B ND2 1 
ATOM   4006 N  N   . MET   B 1 163 ? 37.002  12.242  -4.034  1 78.57  ? 148 MET   B N   1 
ATOM   4007 C  CA  . MET   B 1 163 ? 37.232  11.086  -4.903  1 77.89  ? 148 MET   B CA  1 
ATOM   4008 C  C   . MET   B 1 163 ? 37.812  11.444  -6.257  1 76.65  ? 148 MET   B C   1 
ATOM   4009 O  O   . MET   B 1 163 ? 37.681  12.579  -6.717  1 76.41  ? 148 MET   B O   1 
ATOM   4010 C  CB  . MET   B 1 163 ? 35.94   10.26   -5.077  1 78.71  ? 148 MET   B CB  1 
ATOM   4011 C  CG  . MET   B 1 163 ? 35.402  9.679   -3.804  1 80.64  ? 148 MET   B CG  1 
ATOM   4012 S  SD  . MET   B 1 163 ? 33.675  9.255   -4.039  1 86.15  ? 148 MET   B SD  1 
ATOM   4013 C  CE  . MET   B 1 163 ? 33.856  7.68    -4.831  1 84.9   ? 148 MET   B CE  1 
ATOM   4014 N  N   . ASP   B 1 164 ? 38.425  10.446  -6.907  1 75.72  ? 149 ASP   B N   1 
ATOM   4015 C  CA  . ASP   B 1 164 ? 38.996  10.558  -8.239  1 75.35  ? 149 ASP   B CA  1 
ATOM   4016 C  C   . ASP   B 1 164 ? 38.94   9.208   -8.975  1 74.08  ? 149 ASP   B C   1 
ATOM   4017 O  O   . ASP   B 1 164 ? 38.835  8.154   -8.342  1 74.42  ? 149 ASP   B O   1 
ATOM   4018 C  CB  . ASP   B 1 164 ? 40.455  11.044  -8.15   1 77.48  ? 149 ASP   B CB  1 
ATOM   4019 C  CG  . ASP   B 1 164 ? 40.803  12.077  -9.209  1 82.35  ? 149 ASP   B CG  1 
ATOM   4020 O  OD1 . ASP   B 1 164 ? 40.756  11.732  -10.427 1 82.34  ? 149 ASP   B OD1 1 
ATOM   4021 O  OD2 . ASP   B 1 164 ? 41.103  13.236  -8.829  1 85.02  ? 149 ASP   B OD2 1 
ATOM   4022 N  N   . VAL   B 1 165 ? 39.033  9.233   -10.31  1 72.52  ? 150 VAL   B N   1 
ATOM   4023 C  CA  . VAL   B 1 165 ? 39.096  7.992   -11.09  1 71.21  ? 150 VAL   B CA  1 
ATOM   4024 C  C   . VAL   B 1 165 ? 40.569  7.563   -11.254 1 69.38  ? 150 VAL   B C   1 
ATOM   4025 O  O   . VAL   B 1 165 ? 41.46   8.396   -11.123 1 69.46  ? 150 VAL   B O   1 
ATOM   4026 C  CB  . VAL   B 1 165 ? 38.358  8.076   -12.459 1 71.69  ? 150 VAL   B CB  1 
ATOM   4027 C  CG1 . VAL   B 1 165 ? 36.885  8.412   -12.273 1 71.96  ? 150 VAL   B CG1 1 
ATOM   4028 C  CG2 . VAL   B 1 165 ? 39.032  9.07    -13.4   1 72.05  ? 150 VAL   B CG2 1 
ATOM   4029 N  N   . LEU   B 1 166 ? 40.826  6.278   -11.527 1 67.78  ? 151 LEU   B N   1 
ATOM   4030 C  CA  . LEU   B 1 166 ? 42.188  5.799   -11.74  1 67.05  ? 151 LEU   B CA  1 
ATOM   4031 C  C   . LEU   B 1 166 ? 42.672  6.087   -13.174 1 66.81  ? 151 LEU   B C   1 
ATOM   4032 O  O   . LEU   B 1 166 ? 43.846  6.414   -13.371 1 67.18  ? 151 LEU   B O   1 
ATOM   4033 C  CB  . LEU   B 1 166 ? 42.304  4.298   -11.441 1 66.86  ? 151 LEU   B CB  1 
ATOM   4034 C  CG  . LEU   B 1 166 ? 41.824  3.849   -10.068 1 68.06  ? 151 LEU   B CG  1 
ATOM   4035 C  CD1 . LEU   B 1 166 ? 41.998  2.353   -9.904  1 68.54  ? 151 LEU   B CD1 1 
ATOM   4036 C  CD2 . LEU   B 1 166 ? 42.54   4.597   -8.946  1 68.39  ? 151 LEU   B CD2 1 
ATOM   4037 N  N   . PHE   B 1 167 ? 41.78   5.965   -14.172 1 65.65  ? 152 PHE   B N   1 
ATOM   4038 C  CA  . PHE   B 1 167 ? 42.165  6.175   -15.557 1 65.14  ? 152 PHE   B CA  1 
ATOM   4039 C  C   . PHE   B 1 167 ? 41.183  7.013   -16.355 1 65.64  ? 152 PHE   B C   1 
ATOM   4040 O  O   . PHE   B 1 167 ? 39.962  6.897   -16.191 1 65.85  ? 152 PHE   B O   1 
ATOM   4041 C  CB  . PHE   B 1 167 ? 42.391  4.833   -16.279 1 64.65  ? 152 PHE   B CB  1 
ATOM   4042 C  CG  . PHE   B 1 167 ? 43.292  3.87    -15.548 1 65.02  ? 152 PHE   B CG  1 
ATOM   4043 C  CD1 . PHE   B 1 167 ? 44.666  4.049   -15.54  1 65.61  ? 152 PHE   B CD1 1 
ATOM   4044 C  CD2 . PHE   B 1 167 ? 42.764  2.822   -14.82  1 65.34  ? 152 PHE   B CD2 1 
ATOM   4045 C  CE1 . PHE   B 1 167 ? 45.485  3.184   -14.83  1 66.06  ? 152 PHE   B CE1 1 
ATOM   4046 C  CE2 . PHE   B 1 167 ? 43.587  1.962   -14.113 1 65.84  ? 152 PHE   B CE2 1 
ATOM   4047 C  CZ  . PHE   B 1 167 ? 44.937  2.15    -14.12  1 65.65  ? 152 PHE   B CZ  1 
ATOM   4048 N  N   . SER   B 1 168 ? 41.734  7.829   -17.271 1 65.49  ? 153 SER   B N   1 
ATOM   4049 C  CA  . SER   B 1 168 ? 40.985  8.645   -18.229 1 65.56  ? 153 SER   B CA  1 
ATOM   4050 C  C   . SER   B 1 168 ? 41.466  8.289   -19.651 1 65.87  ? 153 SER   B C   1 
ATOM   4051 O  O   . SER   B 1 168 ? 42.497  7.616   -19.81  1 66.03  ? 153 SER   B O   1 
ATOM   4052 C  CB  . SER   B 1 168 ? 41.179  10.129  -17.945 1 66.22  ? 153 SER   B CB  1 
ATOM   4053 N  N   . PHE   B 1 169 ? 40.714  8.703   -20.678 1 65.95  ? 154 PHE   B N   1 
ATOM   4054 C  CA  . PHE   B 1 169 ? 41.111  8.4     -22.049 1 66.91  ? 154 PHE   B CA  1 
ATOM   4055 C  C   . PHE   B 1 169 ? 41.876  9.55    -22.677 1 68.38  ? 154 PHE   B C   1 
ATOM   4056 O  O   . PHE   B 1 169 ? 42.967  9.354   -23.204 1 68.45  ? 154 PHE   B O   1 
ATOM   4057 C  CB  . PHE   B 1 169 ? 39.909  7.964   -22.898 1 66.38  ? 154 PHE   B CB  1 
ATOM   4058 C  CG  . PHE   B 1 169 ? 39.453  6.568   -22.555 1 66.27  ? 154 PHE   B CG  1 
ATOM   4059 C  CD1 . PHE   B 1 169 ? 40.194  5.464   -22.942 1 66.39  ? 154 PHE   B CD1 1 
ATOM   4060 C  CD2 . PHE   B 1 169 ? 38.289  6.361   -21.834 1 66.66  ? 154 PHE   B CD2 1 
ATOM   4061 C  CE1 . PHE   B 1 169 ? 39.771  4.181   -22.63  1 66.92  ? 154 PHE   B CE1 1 
ATOM   4062 C  CE2 . PHE   B 1 169 ? 37.866  5.077   -21.529 1 67.17  ? 154 PHE   B CE2 1 
ATOM   4063 C  CZ  . PHE   B 1 169 ? 38.612  3.995   -21.926 1 66.84  ? 154 PHE   B CZ  1 
ATOM   4064 N  N   . ARG   B 1 170 ? 41.295  10.744  -22.621 1 69.36  ? 155 ARG   B N   1 
ATOM   4065 C  CA  . ARG   B 1 170 ? 41.862  11.969  -23.16  1 70.91  ? 155 ARG   B CA  1 
ATOM   4066 C  C   . ARG   B 1 170 ? 41.696  13.088  -22.137 1 72.28  ? 155 ARG   B C   1 
ATOM   4067 O  O   . ARG   B 1 170 ? 40.823  13.004  -21.277 1 72.74  ? 155 ARG   B O   1 
ATOM   4068 C  CB  . ARG   B 1 170 ? 41.124  12.368  -24.457 1 72.43  ? 155 ARG   B CB  1 
ATOM   4069 C  CG  . ARG   B 1 170 ? 41.105  11.278  -25.538 1 75.84  ? 155 ARG   B CG  1 
ATOM   4070 C  CD  . ARG   B 1 170 ? 42.49   10.992  -26.082 1 79.15  ? 155 ARG   B CD  1 
ATOM   4071 N  NE  . ARG   B 1 170 ? 43.051  12.17   -26.744 1 82.35  ? 155 ARG   B NE  1 
ATOM   4072 C  CZ  . ARG   B 1 170 ? 42.842  12.482  -28.021 1 84.39  ? 155 ARG   B CZ  1 
ATOM   4073 N  NH1 . ARG   B 1 170 ? 42.103  11.693  -28.794 1 84.21  ? 155 ARG   B NH1 1 
ATOM   4074 N  NH2 . ARG   B 1 170 ? 43.379  13.579  -28.538 1 84.03  ? 155 ARG   B NH2 1 
ATOM   4075 N  N   . ASP   B 1 171 ? 42.514  14.146  -22.225 1 72.73  ? 156 ASP   B N   1 
ATOM   4076 C  CA  . ASP   B 1 171 ? 42.349  15.286  -21.325 1 73.2   ? 156 ASP   B CA  1 
ATOM   4077 C  C   . ASP   B 1 171 ? 41.056  16.024  -21.761 1 73.54  ? 156 ASP   B C   1 
ATOM   4078 O  O   . ASP   B 1 171 ? 40.772  16.138  -22.958 1 73.82  ? 156 ASP   B O   1 
ATOM   4079 C  CB  . ASP   B 1 171 ? 43.585  16.198  -21.342 1 74.79  ? 156 ASP   B CB  1 
ATOM   4080 N  N   . GLY   B 1 172 ? 40.239  16.417  -20.793 1 73.18  ? 157 GLY   B N   1 
ATOM   4081 C  CA  . GLY   B 1 172 ? 38.98   17.095  -21.08  1 73.19  ? 157 GLY   B CA  1 
ATOM   4082 C  C   . GLY   B 1 172 ? 37.842  16.193  -21.527 1 72.89  ? 157 GLY   B C   1 
ATOM   4083 O  O   . GLY   B 1 172 ? 36.808  16.692  -21.977 1 72.91  ? 157 GLY   B O   1 
ATOM   4084 N  N   . ASP   B 1 173 ? 37.999  14.862  -21.389 1 72.45  ? 158 ASP   B N   1 
ATOM   4085 C  CA  . ASP   B 1 173 ? 36.945  13.907  -21.779 1 72.56  ? 158 ASP   B CA  1 
ATOM   4086 C  C   . ASP   B 1 173 ? 35.768  13.831  -20.781 1 72.86  ? 158 ASP   B C   1 
ATOM   4087 O  O   . ASP   B 1 173 ? 34.784  13.161  -21.071 1 72.94  ? 158 ASP   B O   1 
ATOM   4088 C  CB  . ASP   B 1 173 ? 37.527  12.491  -22.021 1 73.22  ? 158 ASP   B CB  1 
ATOM   4089 C  CG  . ASP   B 1 173 ? 38.163  11.834  -20.807 1 75.49  ? 158 ASP   B CG  1 
ATOM   4090 O  OD1 . ASP   B 1 173 ? 38.211  12.481  -19.738 1 76.05  ? 158 ASP   B OD1 1 
ATOM   4091 O  OD2 . ASP   B 1 173 ? 38.644  10.68   -20.934 1 76.49  ? 158 ASP   B OD2 1 
ATOM   4092 N  N   . CYS   B 1 174 ? 35.893  14.482  -19.602 1 72.81  ? 159 CYS   B N   1 
ATOM   4093 C  CA  . CYS   B 1 174 ? 34.895  14.467  -18.525 1 73.07  ? 159 CYS   B CA  1 
ATOM   4094 C  C   . CYS   B 1 174 ? 34.682  13.072  -17.925 1 72.17  ? 159 CYS   B C   1 
ATOM   4095 O  O   . CYS   B 1 174 ? 33.649  12.843  -17.294 1 72.31  ? 159 CYS   B O   1 
ATOM   4096 C  CB  . CYS   B 1 174 ? 33.571  15.098  -18.959 1 74.84  ? 159 CYS   B CB  1 
ATOM   4097 S  SG  . CYS   B 1 174 ? 33.639  16.89   -19.224 1 80.29  ? 159 CYS   B SG  1 
ATOM   4098 N  N   . SER   B 1 175 ? 35.655  12.151  -18.115 1 71.05  ? 160 SER   B N   1 
ATOM   4099 C  CA  . SER   B 1 175 ? 35.614  10.782  -17.623 1 70.53  ? 160 SER   B CA  1 
ATOM   4100 C  C   . SER   B 1 175 ? 35.463  10.766  -16.124 1 70.39  ? 160 SER   B C   1 
ATOM   4101 O  O   . SER   B 1 175 ? 34.684  9.973   -15.618 1 70.87  ? 160 SER   B O   1 
ATOM   4102 C  CB  . SER   B 1 175 ? 36.868  10.015  -18.025 1 71.46  ? 160 SER   B CB  1 
ATOM   4103 O  OG  . SER   B 1 175 ? 38.029  10.703  -17.602 1 74.42  ? 160 SER   B OG  1 
ATOM   4104 N  N   . LYS   B 1 176 ? 36.138  11.676  -15.404 1 69.54  ? 161 LYS   B N   1 
ATOM   4105 C  CA  . LYS   B 1 176 ? 36.014  11.722  -13.951 1 69.32  ? 161 LYS   B CA  1 
ATOM   4106 C  C   . LYS   B 1 176 ? 34.565  11.999  -13.526 1 68.53  ? 161 LYS   B C   1 
ATOM   4107 O  O   . LYS   B 1 176 ? 34.019  11.263  -12.707 1 68.97  ? 161 LYS   B O   1 
ATOM   4108 C  CB  . LYS   B 1 176 ? 36.971  12.747  -13.346 1 71.14  ? 161 LYS   B CB  1 
ATOM   4109 C  CG  . LYS   B 1 176 ? 36.913  12.78   -11.835 1 75.55  ? 161 LYS   B CG  1 
ATOM   4110 C  CD  . LYS   B 1 176 ? 37.839  13.834  -11.274 1 80.42  ? 161 LYS   B CD  1 
ATOM   4111 C  CE  . LYS   B 1 176 ? 37.504  14.166  -9.85   1 84.56  ? 161 LYS   B CE  1 
ATOM   4112 N  NZ  . LYS   B 1 176 ? 38.26   15.352  -9.391  1 87.29  ? 161 LYS   B NZ  1 
ATOM   4113 N  N   . GLY   B 1 177 ? 33.941  12.99   -14.155 1 66.86  ? 162 GLY   B N   1 
ATOM   4114 C  CA  . GLY   B 1 177 ? 32.565  13.367  -13.862 1 65.57  ? 162 GLY   B CA  1 
ATOM   4115 C  C   . GLY   B 1 177 ? 31.562  12.303  -14.23  1 63.94  ? 162 GLY   B C   1 
ATOM   4116 O  O   . GLY   B 1 177 ? 30.689  11.978  -13.434 1 64.07  ? 162 GLY   B O   1 
ATOM   4117 N  N   . PHE   B 1 178 ? 31.685  11.738  -15.433 1 62.34  ? 163 PHE   B N   1 
ATOM   4118 C  CA  . PHE   B 1 178 ? 30.764  10.706  -15.898 1 60.41  ? 163 PHE   B CA  1 
ATOM   4119 C  C   . PHE   B 1 178 ? 30.847  9.449   -15.039 1 59.49  ? 163 PHE   B C   1 
ATOM   4120 O  O   . PHE   B 1 178 ? 29.812  8.918   -14.639 1 59.52  ? 163 PHE   B O   1 
ATOM   4121 C  CB  . PHE   B 1 178 ? 31.035  10.36   -17.368 1 59.18  ? 163 PHE   B CB  1 
ATOM   4122 C  CG  . PHE   B 1 178 ? 29.957  9.508   -17.994 1 58.54  ? 163 PHE   B CG  1 
ATOM   4123 C  CD1 . PHE   B 1 178 ? 28.622  9.837   -17.849 1 58.6   ? 163 PHE   B CD1 1 
ATOM   4124 C  CD2 . PHE   B 1 178 ? 30.28   8.381   -18.729 1 58.9   ? 163 PHE   B CD2 1 
ATOM   4125 C  CE1 . PHE   B 1 178 ? 27.633  9.071   -18.444 1 59.06  ? 163 PHE   B CE1 1 
ATOM   4126 C  CE2 . PHE   B 1 178 ? 29.289  7.619   -19.331 1 59.07  ? 163 PHE   B CE2 1 
ATOM   4127 C  CZ  . PHE   B 1 178 ? 27.972  7.972   -19.185 1 58.65  ? 163 PHE   B CZ  1 
ATOM   4128 N  N   . PHE   B 1 179 ? 32.067  8.981   -14.75  1 58.39  ? 164 PHE   B N   1 
ATOM   4129 C  CA  . PHE   B 1 179 ? 32.247  7.763   -13.983 1 58.13  ? 164 PHE   B CA  1 
ATOM   4130 C  C   . PHE   B 1 179 ? 31.934  7.933   -12.502 1 58.71  ? 164 PHE   B C   1 
ATOM   4131 O  O   . PHE   B 1 179 ? 31.252  7.077   -11.943 1 59.16  ? 164 PHE   B O   1 
ATOM   4132 C  CB  . PHE   B 1 179 ? 33.643  7.155   -14.197 1 57.81  ? 164 PHE   B CB  1 
ATOM   4133 C  CG  . PHE   B 1 179 ? 33.996  6.789   -15.629 1 58.51  ? 164 PHE   B CG  1 
ATOM   4134 C  CD1 . PHE   B 1 179 ? 33.007  6.497   -16.556 1 59.4   ? 164 PHE   B CD1 1 
ATOM   4135 C  CD2 . PHE   B 1 179 ? 35.319  6.737   -16.042 1 59.07  ? 164 PHE   B CD2 1 
ATOM   4136 C  CE1 . PHE   B 1 179 ? 33.336  6.17    -17.867 1 60.03  ? 164 PHE   B CE1 1 
ATOM   4137 C  CE2 . PHE   B 1 179 ? 35.645  6.407   -17.351 1 59.67  ? 164 PHE   B CE2 1 
ATOM   4138 C  CZ  . PHE   B 1 179 ? 34.652  6.13    -18.256 1 59.67  ? 164 PHE   B CZ  1 
ATOM   4139 N  N   . LEU   B 1 180 ? 32.393  9.026   -11.865 1 58.74  ? 165 LEU   B N   1 
ATOM   4140 C  CA  . LEU   B 1 180 ? 32.14   9.224   -10.439 1 59.37  ? 165 LEU   B CA  1 
ATOM   4141 C  C   . LEU   B 1 180 ? 30.698  9.516   -10.139 1 59.91  ? 165 LEU   B C   1 
ATOM   4142 O  O   . LEU   B 1 180 ? 30.223  9.079   -9.1    1 60     ? 165 LEU   B O   1 
ATOM   4143 C  CB  . LEU   B 1 180 ? 33.022  10.309  -9.806  1 59.84  ? 165 LEU   B CB  1 
ATOM   4144 C  CG  . LEU   B 1 180 ? 34.526  10.041  -9.755  1 61.23  ? 165 LEU   B CG  1 
ATOM   4145 C  CD1 . LEU   B 1 180 ? 35.25   11.245  -9.197  1 61.98  ? 165 LEU   B CD1 1 
ATOM   4146 C  CD2 . LEU   B 1 180 ? 34.847  8.769   -8.967  1 61.16  ? 165 LEU   B CD2 1 
ATOM   4147 N  N   . VAL   B 1 181 ? 29.992  10.253  -11.017 1 60.14  ? 166 VAL   B N   1 
ATOM   4148 C  CA  . VAL   B 1 181 ? 28.582  10.552  -10.765 1 60.81  ? 166 VAL   B CA  1 
ATOM   4149 C  C   . VAL   B 1 181 ? 27.749  9.26    -10.889 1 61.5   ? 166 VAL   B C   1 
ATOM   4150 O  O   . VAL   B 1 181 ? 26.87   9.025   -10.051 1 61.73  ? 166 VAL   B O   1 
ATOM   4151 C  CB  . VAL   B 1 181 ? 28.012  11.756  -11.562 1 61.17  ? 166 VAL   B CB  1 
ATOM   4152 C  CG1 . VAL   B 1 181 ? 26.495  11.855  -11.407 1 61.59  ? 166 VAL   B CG1 1 
ATOM   4153 C  CG2 . VAL   B 1 181 ? 28.657  13.054  -11.098 1 61.41  ? 166 VAL   B CG2 1 
ATOM   4154 N  N   . SER   B 1 182 ? 28.107  8.363   -11.842 1 61.22  ? 167 SER   B N   1 
ATOM   4155 C  CA  . SER   B 1 182 ? 27.443  7.059   -11.966 1 61.14  ? 167 SER   B CA  1 
ATOM   4156 C  C   . SER   B 1 182 ? 27.705  6.256   -10.698 1 61.17  ? 167 SER   B C   1 
ATOM   4157 O  O   . SER   B 1 182 ? 26.77   5.717   -10.118 1 61.95  ? 167 SER   B O   1 
ATOM   4158 C  CB  . SER   B 1 182 ? 27.963  6.283   -13.178 1 62.09  ? 167 SER   B CB  1 
ATOM   4159 O  OG  . SER   B 1 182 ? 27.491  6.828   -14.396 1 64.15  ? 167 SER   B OG  1 
ATOM   4160 N  N   . LEU   B 1 183 ? 28.963  6.24    -10.237 1 60.36  ? 168 LEU   B N   1 
ATOM   4161 C  CA  . LEU   B 1 183 ? 29.378  5.545   -9.027  1 60.15  ? 168 LEU   B CA  1 
ATOM   4162 C  C   . LEU   B 1 183 ? 28.675  6.076   -7.77   1 61.17  ? 168 LEU   B C   1 
ATOM   4163 O  O   . LEU   B 1 183 ? 28.238  5.28    -6.947  1 62.1   ? 168 LEU   B O   1 
ATOM   4164 C  CB  . LEU   B 1 183 ? 30.883  5.658   -8.866  1 59.39  ? 168 LEU   B CB  1 
ATOM   4165 C  CG  . LEU   B 1 183 ? 31.455  4.947   -7.671  1 59.86  ? 168 LEU   B CG  1 
ATOM   4166 C  CD1 . LEU   B 1 183 ? 31.341  3.45    -7.829  1 60.12  ? 168 LEU   B CD1 1 
ATOM   4167 C  CD2 . LEU   B 1 183 ? 32.862  5.373   -7.433  1 60.01  ? 168 LEU   B CD2 1 
ATOM   4168 N  N   . LEU   B 1 184 ? 28.54   7.392   -7.627  1 60.9   ? 169 LEU   B N   1 
ATOM   4169 C  CA  . LEU   B 1 184 ? 27.89   7.97    -6.46   1 61.48  ? 169 LEU   B CA  1 
ATOM   4170 C  C   . LEU   B 1 184 ? 26.4    7.642   -6.422  1 61.9   ? 169 LEU   B C   1 
ATOM   4171 O  O   . LEU   B 1 184 ? 25.863  7.413   -5.343  1 62.36  ? 169 LEU   B O   1 
ATOM   4172 C  CB  . LEU   B 1 184 ? 28.18   9.473   -6.356  1 61.77  ? 169 LEU   B CB  1 
ATOM   4173 C  CG  . LEU   B 1 184 ? 29.638  9.791   -5.956  1 62.74  ? 169 LEU   B CG  1 
ATOM   4174 C  CD1 . LEU   B 1 184 ? 30.004  11.234  -6.252  1 62.75  ? 169 LEU   B CD1 1 
ATOM   4175 C  CD2 . LEU   B 1 184 ? 29.915  9.426   -4.509  1 63.17  ? 169 LEU   B CD2 1 
ATOM   4176 N  N   . VAL   B 1 185 ? 25.749  7.552   -7.593  1 61.58  ? 170 VAL   B N   1 
ATOM   4177 C  CA  . VAL   B 1 185 ? 24.35   7.145   -7.687  1 61.73  ? 170 VAL   B CA  1 
ATOM   4178 C  C   . VAL   B 1 185 ? 24.229  5.635   -7.361  1 61.24  ? 170 VAL   B C   1 
ATOM   4179 O  O   . VAL   B 1 185 ? 23.278  5.226   -6.698  1 61.43  ? 170 VAL   B O   1 
ATOM   4180 C  CB  . VAL   B 1 185 ? 23.754  7.485   -9.071  1 63.04  ? 170 VAL   B CB  1 
ATOM   4181 C  CG1 . VAL   B 1 185 ? 22.404  6.796   -9.283  1 63.82  ? 170 VAL   B CG1 1 
ATOM   4182 C  CG2 . VAL   B 1 185 ? 23.606  8.988   -9.238  1 63.6   ? 170 VAL   B CG2 1 
ATOM   4183 N  N   . GLU   B 1 186 ? 25.213  4.824   -7.787  1 60.44  ? 171 GLU   B N   1 
ATOM   4184 C  CA  . GLU   B 1 186 ? 25.274  3.393   -7.511  1 60.24  ? 171 GLU   B CA  1 
ATOM   4185 C  C   . GLU   B 1 186 ? 25.333  3.151   -6.01   1 60.9   ? 171 GLU   B C   1 
ATOM   4186 O  O   . GLU   B 1 186 ? 24.651  2.261   -5.505  1 61.63  ? 171 GLU   B O   1 
ATOM   4187 C  CB  . GLU   B 1 186 ? 26.525  2.78    -8.152  1 60.76  ? 171 GLU   B CB  1 
ATOM   4188 C  CG  . GLU   B 1 186 ? 26.256  2.071   -9.456  1 63.28  ? 171 GLU   B CG  1 
ATOM   4189 C  CD  . GLU   B 1 186 ? 25.972  0.592   -9.353  1 65.55  ? 171 GLU   B CD  1 
ATOM   4190 O  OE1 . GLU   B 1 186 ? 25.549  0.005   -10.371 1 63.82  ? 171 GLU   B OE1 1 
ATOM   4191 O  OE2 . GLU   B 1 186 ? 26.154  0.018   -8.258  1 68.82  ? 171 GLU   B OE2 1 
ATOM   4192 N  N   . ILE   B 1 187 ? 26.168  3.929   -5.304  1 60.27  ? 172 ILE   B N   1 
ATOM   4193 C  CA  . ILE   B 1 187 ? 26.336  3.813   -3.865  1 60.12  ? 172 ILE   B CA  1 
ATOM   4194 C  C   . ILE   B 1 187 ? 25.092  4.33    -3.127  1 60.92  ? 172 ILE   B C   1 
ATOM   4195 O  O   . ILE   B 1 187 ? 24.688  3.747   -2.114  1 61.49  ? 172 ILE   B O   1 
ATOM   4196 C  CB  . ILE   B 1 187 ? 27.651  4.507   -3.418  1 59.53  ? 172 ILE   B CB  1 
ATOM   4197 C  CG1 . ILE   B 1 187 ? 28.857  3.858   -4.077  1 59.97  ? 172 ILE   B CG1 1 
ATOM   4198 C  CG2 . ILE   B 1 187 ? 27.807  4.481   -1.92   1 59.63  ? 172 ILE   B CG2 1 
ATOM   4199 C  CD1 . ILE   B 1 187 ? 30.099  4.691   -4.002  1 61.12  ? 172 ILE   B CD1 1 
ATOM   4200 N  N   . ALA   B 1 188 ? 24.453  5.384   -3.656  1 60.93  ? 173 ALA   B N   1 
ATOM   4201 C  CA  . ALA   B 1 188 ? 23.23   5.932   -3.064  1 61.8   ? 173 ALA   B CA  1 
ATOM   4202 C  C   . ALA   B 1 188 ? 22.102  4.898   -3.116  1 62.25  ? 173 ALA   B C   1 
ATOM   4203 O  O   . ALA   B 1 188 ? 21.407  4.7     -2.12   1 62.74  ? 173 ALA   B O   1 
ATOM   4204 C  CB  . ALA   B 1 188 ? 22.805  7.201   -3.794  1 62     ? 173 ALA   B CB  1 
ATOM   4205 N  N   . ALA   B 1 189 ? 21.963  4.202   -4.261  1 62.05  ? 174 ALA   B N   1 
ATOM   4206 C  CA  . ALA   B 1 189 ? 20.952  3.166   -4.459  1 62.3   ? 174 ALA   B CA  1 
ATOM   4207 C  C   . ALA   B 1 189 ? 21.248  1.917   -3.626  1 62.32  ? 174 ALA   B C   1 
ATOM   4208 O  O   . ALA   B 1 189 ? 20.318  1.241   -3.195  1 62.51  ? 174 ALA   B O   1 
ATOM   4209 C  CB  . ALA   B 1 189 ? 20.875  2.797   -5.93   1 62.34  ? 174 ALA   B CB  1 
ATOM   4210 N  N   . ALA   B 1 190 ? 22.54   1.623   -3.396  1 61.96  ? 175 ALA   B N   1 
ATOM   4211 C  CA  . ALA   B 1 190 ? 23.019  0.484   -2.624  1 62.38  ? 175 ALA   B CA  1 
ATOM   4212 C  C   . ALA   B 1 190 ? 22.525  0.464   -1.183  1 62.7   ? 175 ALA   B C   1 
ATOM   4213 O  O   . ALA   B 1 190 ? 22.487  -0.605  -0.569  1 63.1   ? 175 ALA   B O   1 
ATOM   4214 C  CB  . ALA   B 1 190 ? 24.532  0.446   -2.638  1 62.63  ? 175 ALA   B CB  1 
ATOM   4215 N  N   . SER   B 1 191 ? 22.169  1.63    -0.629  1 62.33  ? 176 SER   B N   1 
ATOM   4216 C  CA  . SER   B 1 191 ? 21.648  1.703   0.736   1 62.31  ? 176 SER   B CA  1 
ATOM   4217 C  C   . SER   B 1 191 ? 20.33   0.895   0.876   1 62.1   ? 176 SER   B C   1 
ATOM   4218 O  O   . SER   B 1 191 ? 20.007  0.436   1.968   1 62.37  ? 176 SER   B O   1 
ATOM   4219 C  CB  . SER   B 1 191 ? 21.438  3.16    1.147   1 63.11  ? 176 SER   B CB  1 
ATOM   4220 N  N   . ALA   B 1 192 ? 19.591  0.695   -0.23   1 61.17  ? 177 ALA   B N   1 
ATOM   4221 C  CA  . ALA   B 1 192 ? 18.36   -0.077  -0.203  1 60.77  ? 177 ALA   B CA  1 
ATOM   4222 C  C   . ALA   B 1 192 ? 18.582  -1.599  -0.327  1 60.2   ? 177 ALA   B C   1 
ATOM   4223 O  O   . ALA   B 1 192 ? 17.659  -2.368  -0.039  1 60.58  ? 177 ALA   B O   1 
ATOM   4224 C  CB  . ALA   B 1 192 ? 17.423  0.412   -1.292  1 60.93  ? 177 ALA   B CB  1 
ATOM   4225 N  N   . ILE   B 1 193 ? 19.779  -2.035  -0.759  1 59.03  ? 178 ILE   B N   1 
ATOM   4226 C  CA  . ILE   B 1 193 ? 20.086  -3.448  -0.933  1 58.86  ? 178 ILE   B CA  1 
ATOM   4227 C  C   . ILE   B 1 193 ? 19.973  -4.214  0.371   1 59.07  ? 178 ILE   B C   1 
ATOM   4228 O  O   . ILE   B 1 193 ? 19.416  -5.307  0.385   1 59.62  ? 178 ILE   B O   1 
ATOM   4229 C  CB  . ILE   B 1 193 ? 21.453  -3.685  -1.635  1 58.95  ? 178 ILE   B CB  1 
ATOM   4230 C  CG1 . ILE   B 1 193 ? 21.466  -3.103  -3.046  1 59.6   ? 178 ILE   B CG1 1 
ATOM   4231 C  CG2 . ILE   B 1 193 ? 21.808  -5.175  -1.676  1 59.28  ? 178 ILE   B CG2 1 
ATOM   4232 C  CD1 . ILE   B 1 193 ? 22.835  -3.118  -3.674  1 61.07  ? 178 ILE   B CD1 1 
ATOM   4233 N  N   . LYS   B 1 194 ? 20.454  -3.635  1.478   1 58.79  ? 179 LYS   B N   1 
ATOM   4234 C  CA  . LYS   B 1 194 ? 20.36   -4.288  2.788   1 58.97  ? 179 LYS   B CA  1 
ATOM   4235 C  C   . LYS   B 1 194 ? 18.919  -4.519  3.253   1 59.34  ? 179 LYS   B C   1 
ATOM   4236 O  O   . LYS   B 1 194 ? 18.691  -5.327  4.143   1 60.17  ? 179 LYS   B O   1 
ATOM   4237 C  CB  . LYS   B 1 194 ? 21.124  -3.497  3.848   1 60.84  ? 179 LYS   B CB  1 
ATOM   4238 C  CG  . LYS   B 1 194 ? 20.623  -2.073  4.03    1 65.91  ? 179 LYS   B CG  1 
ATOM   4239 C  CD  . LYS   B 1 194 ? 21.345  -1.374  5.175   1 71.27  ? 179 LYS   B CD  1 
ATOM   4240 C  CE  . LYS   B 1 194 ? 21.3    0.127   5.072   1 75.97  ? 179 LYS   B CE  1 
ATOM   4241 N  NZ  . LYS   B 1 194 ? 22.404  0.648   4.219   1 79.46  ? 179 LYS   B NZ  1 
ATOM   4242 N  N   . VAL   B 1 195 ? 17.955  -3.806  2.676   1 58.88  ? 180 VAL   B N   1 
ATOM   4243 C  CA  . VAL   B 1 195 ? 16.547  -3.934  3.027   1 59.01  ? 180 VAL   B CA  1 
ATOM   4244 C  C   . VAL   B 1 195 ? 15.891  -5.146  2.335   1 58.87  ? 180 VAL   B C   1 
ATOM   4245 O  O   . VAL   B 1 195 ? 14.849  -5.613  2.801   1 59     ? 180 VAL   B O   1 
ATOM   4246 C  CB  . VAL   B 1 195 ? 15.794  -2.605  2.74    1 59.68  ? 180 VAL   B CB  1 
ATOM   4247 C  CG1 . VAL   B 1 195 ? 14.345  -2.657  3.224   1 59.93  ? 180 VAL   B CG1 1 
ATOM   4248 C  CG2 . VAL   B 1 195 ? 16.525  -1.417  3.364   1 59.87  ? 180 VAL   B CG2 1 
ATOM   4249 N  N   . ILE   B 1 196 ? 16.507  -5.659  1.24    1 58.32  ? 181 ILE   B N   1 
ATOM   4250 C  CA  . ILE   B 1 196 ? 16.01   -6.791  0.466   1 58.56  ? 181 ILE   B CA  1 
ATOM   4251 C  C   . ILE   B 1 196 ? 15.764  -8.039  1.351   1 59.39  ? 181 ILE   B C   1 
ATOM   4252 O  O   . ILE   B 1 196 ? 14.631  -8.531  1.362   1 59.46  ? 181 ILE   B O   1 
ATOM   4253 C  CB  . ILE   B 1 196 ? 16.91   -7.073  -0.762  1 58.58  ? 181 ILE   B CB  1 
ATOM   4254 C  CG1 . ILE   B 1 196 ? 16.808  -5.927  -1.794  1 58.8   ? 181 ILE   B CG1 1 
ATOM   4255 C  CG2 . ILE   B 1 196 ? 16.573  -8.423  -1.395  1 59.06  ? 181 ILE   B CG2 1 
ATOM   4256 C  CD1 . ILE   B 1 196 ? 17.78   -6.027  -2.939  1 59.59  ? 181 ILE   B CD1 1 
ATOM   4257 N  N   . PRO   B 1 197 ? 16.736  -8.512  2.172   1 59.62  ? 182 PRO   B N   1 
ATOM   4258 C  CA  . PRO   B 1 197 ? 16.443  -9.669  3.037   1 59.54  ? 182 PRO   B CA  1 
ATOM   4259 C  C   . PRO   B 1 197 ? 15.223  -9.463  3.939   1 59.13  ? 182 PRO   B C   1 
ATOM   4260 O  O   . PRO   B 1 197 ? 14.47   -10.41  4.158   1 59.17  ? 182 PRO   B O   1 
ATOM   4261 C  CB  . PRO   B 1 197 ? 17.736  -9.854  3.854   1 60.43  ? 182 PRO   B CB  1 
ATOM   4262 C  CG  . PRO   B 1 197 ? 18.592  -8.677  3.577   1 60.79  ? 182 PRO   B CG  1 
ATOM   4263 C  CD  . PRO   B 1 197 ? 18.15   -8.086  2.294   1 59.15  ? 182 PRO   B CD  1 
ATOM   4264 N  N   . THR   B 1 198 ? 15.015  -8.226  4.438   1 58.62  ? 183 THR   B N   1 
ATOM   4265 C  CA  . THR   B 1 198 ? 13.881  -7.883  5.301   1 58.82  ? 183 THR   B CA  1 
ATOM   4266 C  C   . THR   B 1 198 ? 12.561  -8.04   4.543   1 58.94  ? 183 THR   B C   1 
ATOM   4267 O  O   . THR   B 1 198 ? 11.577  -8.52   5.106   1 59.39  ? 183 THR   B O   1 
ATOM   4268 C  CB  . THR   B 1 198 ? 14.017  -6.452  5.816   1 60.41  ? 183 THR   B CB  1 
ATOM   4269 O  OG1 . THR   B 1 198 ? 15.286  -6.297  6.439   1 61.88  ? 183 THR   B OG1 1 
ATOM   4270 C  CG2 . THR   B 1 198 ? 12.926  -6.075  6.787   1 60.8   ? 183 THR   B CG2 1 
ATOM   4271 N  N   . VAL   B 1 199 ? 12.541  -7.642  3.265   1 57.89  ? 184 VAL   B N   1 
ATOM   4272 C  CA  . VAL   B 1 199 ? 11.356  -7.749  2.422   1 56.99  ? 184 VAL   B CA  1 
ATOM   4273 C  C   . VAL   B 1 199 ? 10.938  -9.204  2.229   1 57.15  ? 184 VAL   B C   1 
ATOM   4274 O  O   . VAL   B 1 199 ? 9.757   -9.534  2.376   1 57.76  ? 184 VAL   B O   1 
ATOM   4275 C  CB  . VAL   B 1 199 ? 11.603  -7.021  1.083   1 56.23  ? 184 VAL   B CB  1 
ATOM   4276 C  CG1 . VAL   B 1 199 ? 10.539  -7.354  0.048   1 55.92  ? 184 VAL   B CG1 1 
ATOM   4277 C  CG2 . VAL   B 1 199 ? 11.693  -5.523  1.305   1 56.32  ? 184 VAL   B CG2 1 
ATOM   4278 N  N   . PHE   B 1 200 ? 11.9    -10.079 1.922   1 56.47  ? 185 PHE   B N   1 
ATOM   4279 C  CA  . PHE   B 1 200 ? 11.599  -11.481 1.679   1 56.24  ? 185 PHE   B CA  1 
ATOM   4280 C  C   . PHE   B 1 200 ? 11.259  -12.238 2.936   1 57.2   ? 185 PHE   B C   1 
ATOM   4281 O  O   . PHE   B 1 200 ? 10.387  -13.099 2.898   1 57.39  ? 185 PHE   B O   1 
ATOM   4282 C  CB  . PHE   B 1 200 ? 12.718  -12.151 0.906   1 55.71  ? 185 PHE   B CB  1 
ATOM   4283 C  CG  . PHE   B 1 200 ? 12.747  -11.696 -0.524  1 56.15  ? 185 PHE   B CG  1 
ATOM   4284 C  CD1 . PHE   B 1 200 ? 11.622  -11.795 -1.32   1 57.04  ? 185 PHE   B CD1 1 
ATOM   4285 C  CD2 . PHE   B 1 200 ? 13.901  -11.17  -1.078  1 56.97  ? 185 PHE   B CD2 1 
ATOM   4286 C  CE1 . PHE   B 1 200 ? 11.647  -11.377 -2.644  1 57.97  ? 185 PHE   B CE1 1 
ATOM   4287 C  CE2 . PHE   B 1 200 ? 13.927  -10.757 -2.405  1 57.78  ? 185 PHE   B CE2 1 
ATOM   4288 C  CZ  . PHE   B 1 200 ? 12.801  -10.867 -3.184  1 57.69  ? 185 PHE   B CZ  1 
ATOM   4289 N  N   . LYS   B 1 201 ? 11.912  -11.905 4.059   1 57.76  ? 186 LYS   B N   1 
ATOM   4290 C  CA  . LYS   B 1 201 ? 11.612  -12.545 5.334   1 58.58  ? 186 LYS   B CA  1 
ATOM   4291 C  C   . LYS   B 1 201 ? 10.249  -12.093 5.822   1 59.99  ? 186 LYS   B C   1 
ATOM   4292 O  O   . LYS   B 1 201 ? 9.514   -12.915 6.345   1 61.2   ? 186 LYS   B O   1 
ATOM   4293 C  CB  . LYS   B 1 201 ? 12.692  -12.262 6.386   1 60.14  ? 186 LYS   B CB  1 
ATOM   4294 N  N   . ALA   B 1 202 ? 9.869   -10.815 5.607   1 59.9   ? 187 ALA   B N   1 
ATOM   4295 C  CA  . ALA   B 1 202 ? 8.559   -10.325 6.024   1 60.33  ? 187 ALA   B CA  1 
ATOM   4296 C  C   . ALA   B 1 202 ? 7.44    -10.969 5.218   1 61.44  ? 187 ALA   B C   1 
ATOM   4297 O  O   . ALA   B 1 202 ? 6.361   -11.185 5.759   1 62.07  ? 187 ALA   B O   1 
ATOM   4298 C  CB  . ALA   B 1 202 ? 8.489   -8.815  5.911   1 60.22  ? 187 ALA   B CB  1 
ATOM   4299 N  N   . MET   B 1 203 ? 7.678   -11.288 3.94    1 61.52  ? 188 MET   B N   1 
ATOM   4300 C  CA  . MET   B 1 203 ? 6.662   -11.957 3.131   1 62.13  ? 188 MET   B CA  1 
ATOM   4301 C  C   . MET   B 1 203 ? 6.502   -13.395 3.614   1 62.83  ? 188 MET   B C   1 
ATOM   4302 O  O   . MET   B 1 203 ? 5.374   -13.858 3.777   1 63.14  ? 188 MET   B O   1 
ATOM   4303 C  CB  . MET   B 1 203 ? 7.034   -11.951 1.649   1 62.68  ? 188 MET   B CB  1 
ATOM   4304 C  CG  . MET   B 1 203 ? 6.827   -10.627 0.963   1 64.05  ? 188 MET   B CG  1 
ATOM   4305 S  SD  . MET   B 1 203 ? 7.687   -10.632 -0.631  1 66.8   ? 188 MET   B SD  1 
ATOM   4306 C  CE  . MET   B 1 203 ? 6.843   -11.91  -1.468  1 62.36  ? 188 MET   B CE  1 
ATOM   4307 N  N   . GLN   B 1 204 ? 7.621   -14.083 3.883   1 63.13  ? 189 GLN   B N   1 
ATOM   4308 C  CA  . GLN   B 1 204 ? 7.629   -15.473 4.354   1 64.12  ? 189 GLN   B CA  1 
ATOM   4309 C  C   . GLN   B 1 204 ? 6.911   -15.57  5.691   1 65.64  ? 189 GLN   B C   1 
ATOM   4310 O  O   . GLN   B 1 204 ? 5.977   -16.35  5.829   1 66.21  ? 189 GLN   B O   1 
ATOM   4311 C  CB  . GLN   B 1 204 ? 9.073   -16.025 4.46    1 64.67  ? 189 GLN   B CB  1 
ATOM   4312 N  N   . MET   B 1 205 ? 7.297   -14.726 6.651   1 66.09  ? 190 MET   B N   1 
ATOM   4313 C  CA  . MET   B 1 205 ? 6.688   -14.701 7.975   1 66.79  ? 190 MET   B CA  1 
ATOM   4314 C  C   . MET   B 1 205 ? 5.32    -14.052 8.035   1 66.73  ? 190 MET   B C   1 
ATOM   4315 O  O   . MET   B 1 205 ? 4.734   -14.014 9.117   1 67.56  ? 190 MET   B O   1 
ATOM   4316 C  CB  . MET   B 1 205 ? 7.608   -13.982 8.972   1 68.19  ? 190 MET   B CB  1 
ATOM   4317 C  CG  . MET   B 1 205 ? 8.975   -14.623 9.151   1 71.97  ? 190 MET   B CG  1 
ATOM   4318 S  SD  . MET   B 1 205 ? 9.012   -16.439 9.272   1 81.93  ? 190 MET   B SD  1 
ATOM   4319 C  CE  . MET   B 1 205 ? 10.248  -16.839 7.92    1 79.94  ? 190 MET   B CE  1 
ATOM   4320 N  N   . GLN   B 1 206 ? 4.843   -13.477 6.923   1 65.55  ? 191 GLN   B N   1 
ATOM   4321 C  CA  . GLN   B 1 206 ? 3.575   -12.78  6.857   1 65.16  ? 191 GLN   B CA  1 
ATOM   4322 C  C   . GLN   B 1 206 ? 3.549   -11.611 7.833   1 63.82  ? 191 GLN   B C   1 
ATOM   4323 O  O   . GLN   B 1 206 ? 2.572   -11.43  8.53    1 64.12  ? 191 GLN   B O   1 
ATOM   4324 C  CB  . GLN   B 1 206 ? 2.404   -13.744 7.068   1 67.57  ? 191 GLN   B CB  1 
ATOM   4325 C  CG  . GLN   B 1 206 ? 2.132   -14.67  5.886   1 72.73  ? 191 GLN   B CG  1 
ATOM   4326 C  CD  . GLN   B 1 206 ? 1.248   -14.029 4.834   1 79.12  ? 191 GLN   B CD  1 
ATOM   4327 O  OE1 . GLN   B 1 206 ? 0.53    -13.044 5.086   1 80.52  ? 191 GLN   B OE1 1 
ATOM   4328 N  NE2 . GLN   B 1 206 ? 1.277   -14.581 3.619   1 80.6   ? 191 GLN   B NE2 1 
ATOM   4329 N  N   . GLU   B 1 207 ? 4.628   -10.83  7.89    1 62.34  ? 192 GLU   B N   1 
ATOM   4330 C  CA  . GLU   B 1 207 ? 4.748   -9.667  8.755   1 61.61  ? 192 GLU   B CA  1 
ATOM   4331 C  C   . GLU   B 1 207 ? 4.412   -8.441  7.939   1 60.71  ? 192 GLU   B C   1 
ATOM   4332 O  O   . GLU   B 1 207 ? 5.302   -7.804  7.371   1 61.63  ? 192 GLU   B O   1 
ATOM   4333 C  CB  . GLU   B 1 207 ? 6.173   -9.556  9.302   1 64.06  ? 192 GLU   B CB  1 
ATOM   4334 C  CG  . GLU   B 1 207 ? 6.56    -10.698 10.218  1 69.3   ? 192 GLU   B CG  1 
ATOM   4335 C  CD  . GLU   B 1 207 ? 5.917   -10.644 11.591  1 76.7   ? 192 GLU   B CD  1 
ATOM   4336 O  OE1 . GLU   B 1 207 ? 5.494   -9.541  12.011  1 77.08  ? 192 GLU   B OE1 1 
ATOM   4337 O  OE2 . GLU   B 1 207 ? 5.85    -11.704 12.255  1 80.05  ? 192 GLU   B OE2 1 
ATOM   4338 N  N   . ARG   B 1 208 ? 3.124   -8.128  7.859   1 58.51  ? 193 ARG   B N   1 
ATOM   4339 C  CA  . ARG   B 1 208 ? 2.598   -7.027  7.077   1 56.75  ? 193 ARG   B CA  1 
ATOM   4340 C  C   . ARG   B 1 208 ? 3.211   -5.667  7.417   1 56.93  ? 193 ARG   B C   1 
ATOM   4341 O  O   . ARG   B 1 208 ? 3.542   -4.9    6.509   1 57.14  ? 193 ARG   B O   1 
ATOM   4342 C  CB  . ARG   B 1 208 ? 1.066   -7.007  7.208   1 55.38  ? 193 ARG   B CB  1 
ATOM   4343 C  CG  . ARG   B 1 208 ? 0.362   -5.948  6.385   1 53.88  ? 193 ARG   B CG  1 
ATOM   4344 C  CD  . ARG   B 1 208 ? 0.138   -4.714  7.207   1 53.58  ? 193 ARG   B CD  1 
ATOM   4345 N  NE  . ARG   B 1 208 ? -0.617  -3.685  6.501   1 54.17  ? 193 ARG   B NE  1 
ATOM   4346 C  CZ  . ARG   B 1 208 ? -0.776  -2.441  6.941   1 54.46  ? 193 ARG   B CZ  1 
ATOM   4347 N  NH1 . ARG   B 1 208 ? -0.194  -2.048  8.067   1 53.93  ? 193 ARG   B NH1 1 
ATOM   4348 N  NH2 . ARG   B 1 208 ? -1.492  -1.569  6.239   1 53.02  ? 193 ARG   B NH2 1 
ATOM   4349 N  N   . ASP   B 1 209 ? 3.322   -5.344  8.711   1 56.55  ? 194 ASP   B N   1 
ATOM   4350 C  CA  . ASP   B 1 209 ? 3.826   -4.04   9.125   1 56.5   ? 194 ASP   B CA  1 
ATOM   4351 C  C   . ASP   B 1 209 ? 5.301   -3.871  8.791   1 57.02  ? 194 ASP   B C   1 
ATOM   4352 O  O   . ASP   B 1 209 ? 5.719   -2.792  8.362   1 57.6   ? 194 ASP   B O   1 
ATOM   4353 C  CB  . ASP   B 1 209 ? 3.559   -3.812  10.62   1 57.66  ? 194 ASP   B CB  1 
ATOM   4354 C  CG  . ASP   B 1 209 ? 2.083   -3.82   11.003  1 60.89  ? 194 ASP   B CG  1 
ATOM   4355 O  OD1 . ASP   B 1 209 ? 1.253   -3.363  10.189  1 60.93  ? 194 ASP   B OD1 1 
ATOM   4356 O  OD2 . ASP   B 1 209 ? 1.763   -4.279  12.116  1 62.85  ? 194 ASP   B OD2 1 
ATOM   4357 N  N   . THR   B 1 210 ? 6.083   -4.948  8.973   1 56.45  ? 195 THR   B N   1 
ATOM   4358 C  CA  . THR   B 1 210 ? 7.501   -4.979  8.672   1 56.26  ? 195 THR   B CA  1 
ATOM   4359 C  C   . THR   B 1 210 ? 7.715   -4.743  7.169   1 57.38  ? 195 THR   B C   1 
ATOM   4360 O  O   . THR   B 1 210 ? 8.562   -3.94   6.787   1 57.44  ? 195 THR   B O   1 
ATOM   4361 C  CB  . THR   B 1 210 ? 8.072   -6.33   9.09    1 56.24  ? 195 THR   B CB  1 
ATOM   4362 O  OG1 . THR   B 1 210 ? 7.912   -6.486  10.488  1 56.54  ? 195 THR   B OG1 1 
ATOM   4363 C  CG2 . THR   B 1 210 ? 9.537   -6.492  8.694   1 56.22  ? 195 THR   B CG2 1 
ATOM   4364 N  N   . LEU   B 1 211 ? 6.927   -5.422  6.322   1 57.73  ? 196 LEU   B N   1 
ATOM   4365 C  CA  . LEU   B 1 211 ? 7.04    -5.267  4.885   1 58.73  ? 196 LEU   B CA  1 
ATOM   4366 C  C   . LEU   B 1 211 ? 6.707   -3.834  4.456   1 59.96  ? 196 LEU   B C   1 
ATOM   4367 O  O   . LEU   B 1 211 ? 7.324   -3.312  3.526   1 60.7   ? 196 LEU   B O   1 
ATOM   4368 C  CB  . LEU   B 1 211 ? 6.131   -6.279  4.182   1 58.88  ? 196 LEU   B CB  1 
ATOM   4369 C  CG  . LEU   B 1 211 ? 6.195   -6.309  2.664   1 60.06  ? 196 LEU   B CG  1 
ATOM   4370 C  CD1 . LEU   B 1 211 ? 7.59    -6.635  2.181   1 60.46  ? 196 LEU   B CD1 1 
ATOM   4371 C  CD2 . LEU   B 1 211 ? 5.182   -7.274  2.099   1 60.38  ? 196 LEU   B CD2 1 
ATOM   4372 N  N   . LEU   B 1 212 ? 5.772   -3.18   5.152   1 60.12  ? 197 LEU   B N   1 
ATOM   4373 C  CA  . LEU   B 1 212 ? 5.405   -1.797  4.847   1 60.53  ? 197 LEU   B CA  1 
ATOM   4374 C  C   . LEU   B 1 212 ? 6.575   -0.849  5.162   1 60.47  ? 197 LEU   B C   1 
ATOM   4375 O  O   . LEU   B 1 212 ? 6.926   -0.016  4.325   1 60.73  ? 197 LEU   B O   1 
ATOM   4376 C  CB  . LEU   B 1 212 ? 4.139   -1.394  5.622   1 60.69  ? 197 LEU   B CB  1 
ATOM   4377 C  CG  . LEU   B 1 212 ? 3.212   -0.458  4.874   1 62.14  ? 197 LEU   B CG  1 
ATOM   4378 C  CD1 . LEU   B 1 212 ? 1.798   -0.626  5.323   1 62.56  ? 197 LEU   B CD1 1 
ATOM   4379 C  CD2 . LEU   B 1 212 ? 3.622   0.953   5.052   1 62.69  ? 197 LEU   B CD2 1 
ATOM   4380 N  N   . LYS   B 1 213 ? 7.189   -1.001  6.352   1 59.67  ? 198 LYS   B N   1 
ATOM   4381 C  CA  . LYS   B 1 213 ? 8.321   -0.18   6.758   1 59.44  ? 198 LYS   B CA  1 
ATOM   4382 C  C   . LYS   B 1 213 ? 9.502   -0.409  5.803   1 59.19  ? 198 LYS   B C   1 
ATOM   4383 O  O   . LYS   B 1 213 ? 10.148  0.554   5.403   1 59.16  ? 198 LYS   B O   1 
ATOM   4384 C  CB  . LYS   B 1 213 ? 8.717   -0.486  8.214   1 60.66  ? 198 LYS   B CB  1 
ATOM   4385 N  N   . ALA   B 1 214 ? 9.74    -1.681  5.413   1 58.77  ? 199 ALA   B N   1 
ATOM   4386 C  CA  . ALA   B 1 214 ? 10.793  -2.084  4.486   1 58.72  ? 199 ALA   B CA  1 
ATOM   4387 C  C   . ALA   B 1 214 ? 10.58   -1.49   3.097   1 59.19  ? 199 ALA   B C   1 
ATOM   4388 O  O   . ALA   B 1 214 ? 11.527  -0.937  2.539   1 59.72  ? 199 ALA   B O   1 
ATOM   4389 C  CB  . ALA   B 1 214 ? 10.896  -3.598  4.404   1 58.37  ? 199 ALA   B CB  1 
ATOM   4390 N  N   . LEU   B 1 215 ? 9.352   -1.54   2.559   1 58.89  ? 200 LEU   B N   1 
ATOM   4391 C  CA  . LEU   B 1 215 ? 9.093   -0.945  1.246   1 59.46  ? 200 LEU   B CA  1 
ATOM   4392 C  C   . LEU   B 1 215 ? 9.278   0.577   1.293   1 59.71  ? 200 LEU   B C   1 
ATOM   4393 O  O   . LEU   B 1 215 ? 9.836   1.162   0.361   1 59.74  ? 200 LEU   B O   1 
ATOM   4394 C  CB  . LEU   B 1 215 ? 7.697   -1.312  0.713   1 59.66  ? 200 LEU   B CB  1 
ATOM   4395 C  CG  . LEU   B 1 215 ? 7.539   -2.759  0.237   1 60.75  ? 200 LEU   B CG  1 
ATOM   4396 C  CD1 . LEU   B 1 215 ? 6.095   -3.075  -0.067  1 60.7   ? 200 LEU   B CD1 1 
ATOM   4397 C  CD2 . LEU   B 1 215 ? 8.43    -3.047  -0.965  1 61.19  ? 200 LEU   B CD2 1 
ATOM   4398 N  N   . LEU   B 1 216 ? 8.851   1.21    2.4     1 59.6   ? 201 LEU   B N   1 
ATOM   4399 C  CA  . LEU   B 1 216 ? 9.001   2.652   2.572   1 59.71  ? 201 LEU   B CA  1 
ATOM   4400 C  C   . LEU   B 1 216 ? 10.471  3.059   2.713   1 60.69  ? 201 LEU   B C   1 
ATOM   4401 O  O   . LEU   B 1 216 ? 10.859  4.13    2.248   1 61.28  ? 201 LEU   B O   1 
ATOM   4402 C  CB  . LEU   B 1 216 ? 8.179   3.14    3.769   1 59.28  ? 201 LEU   B CB  1 
ATOM   4403 C  CG  . LEU   B 1 216 ? 6.673   3.193   3.561   1 60.08  ? 201 LEU   B CG  1 
ATOM   4404 C  CD1 . LEU   B 1 216 ? 5.999   3.668   4.795   1 60.92  ? 201 LEU   B CD1 1 
ATOM   4405 C  CD2 . LEU   B 1 216 ? 6.3     4.103   2.406   1 60.32  ? 201 LEU   B CD2 1 
ATOM   4406 N  N   . GLU   B 1 217 ? 11.287  2.197   3.331   1 60.7   ? 202 GLU   B N   1 
ATOM   4407 C  CA  . GLU   B 1 217 ? 12.707  2.442   3.487   1 61.46  ? 202 GLU   B CA  1 
ATOM   4408 C  C   . GLU   B 1 217 ? 13.423  2.347   2.125   1 61.56  ? 202 GLU   B C   1 
ATOM   4409 O  O   . GLU   B 1 217 ? 14.307  3.155   1.84    1 61.96  ? 202 GLU   B O   1 
ATOM   4410 C  CB  . GLU   B 1 217 ? 13.306  1.479   4.525   1 64.18  ? 202 GLU   B CB  1 
ATOM   4411 C  CG  . GLU   B 1 217 ? 14.784  1.685   4.811   1 71.62  ? 202 GLU   B CG  1 
ATOM   4412 C  CD  . GLU   B 1 217 ? 15.22   3.111   5.1     1 82.94  ? 202 GLU   B CD  1 
ATOM   4413 O  OE1 . GLU   B 1 217 ? 14.476  3.836   5.802   1 85.95  ? 202 GLU   B OE1 1 
ATOM   4414 O  OE2 . GLU   B 1 217 ? 16.312  3.503   4.621   1 85.97  ? 202 GLU   B OE2 1 
ATOM   4415 N  N   . ILE   B 1 218 ? 13.009  1.406   1.269   1 60.81  ? 203 ILE   B N   1 
ATOM   4416 C  CA  . ILE   B 1 218 ? 13.591  1.278   -0.059  1 60.98  ? 203 ILE   B CA  1 
ATOM   4417 C  C   . ILE   B 1 218 ? 13.247  2.533   -0.887  1 62.55  ? 203 ILE   B C   1 
ATOM   4418 O  O   . ILE   B 1 218 ? 14.119  3.086   -1.557  1 63.43  ? 203 ILE   B O   1 
ATOM   4419 C  CB  . ILE   B 1 218 ? 13.142  -0.043  -0.738  1 60.21  ? 203 ILE   B CB  1 
ATOM   4420 C  CG1 . ILE   B 1 218 ? 13.829  -1.246  -0.092  1 59.67  ? 203 ILE   B CG1 1 
ATOM   4421 C  CG2 . ILE   B 1 218 ? 13.382  -0.02   -2.26   1 60.55  ? 203 ILE   B CG2 1 
ATOM   4422 C  CD1 . ILE   B 1 218 ? 13.245  -2.536  -0.469  1 60.11  ? 203 ILE   B CD1 1 
ATOM   4423 N  N   . ALA   B 1 219 ? 12.008  3.013   -0.786  1 62.7   ? 204 ALA   B N   1 
ATOM   4424 C  CA  . ALA   B 1 219 ? 11.571  4.198   -1.505  1 63.63  ? 204 ALA   B CA  1 
ATOM   4425 C  C   . ALA   B 1 219 ? 12.39   5.426   -1.124  1 65.44  ? 204 ALA   B C   1 
ATOM   4426 O  O   . ALA   B 1 219 ? 12.792  6.178   -2.013  1 66.08  ? 204 ALA   B O   1 
ATOM   4427 C  CB  . ALA   B 1 219 ? 10.101  4.45    -1.242  1 63.5   ? 204 ALA   B CB  1 
ATOM   4428 N  N   . SER   B 1 220 ? 12.684  5.609   0.18    1 65.98  ? 205 SER   B N   1 
ATOM   4429 C  CA  . SER   B 1 220 ? 13.464  6.752   0.65    1 67.01  ? 205 SER   B CA  1 
ATOM   4430 C  C   . SER   B 1 220 ? 14.918  6.709   0.144   1 68.08  ? 205 SER   B C   1 
ATOM   4431 O  O   . SER   B 1 220 ? 15.509  7.759   -0.133  1 68.63  ? 205 SER   B O   1 
ATOM   4432 C  CB  . SER   B 1 220 ? 13.391  6.876   2.172   1 68.45  ? 205 SER   B CB  1 
ATOM   4433 O  OG  . SER   B 1 220 ? 14.441  6.209   2.856   1 71.37  ? 205 SER   B OG  1 
ATOM   4434 N  N   . CYS   B 1 221 ? 15.474  5.496   -0.01   1 68.03  ? 206 CYS   B N   1 
ATOM   4435 C  CA  . CYS   B 1 221 ? 16.818  5.299   -0.543  1 68.31  ? 206 CYS   B CA  1 
ATOM   4436 C  C   . CYS   B 1 221 ? 16.853  5.694   -2.016  1 68.78  ? 206 CYS   B C   1 
ATOM   4437 O  O   . CYS   B 1 221 ? 17.793  6.355   -2.455  1 69.15  ? 206 CYS   B O   1 
ATOM   4438 C  CB  . CYS   B 1 221 ? 17.265  3.857   -0.353  1 68.64  ? 206 CYS   B CB  1 
ATOM   4439 S  SG  . CYS   B 1 221 ? 17.645  3.424   1.357   1 71.49  ? 206 CYS   B SG  1 
ATOM   4440 N  N   . LEU   B 1 222 ? 15.826  5.292   -2.775  1 68.59  ? 207 LEU   B N   1 
ATOM   4441 C  CA  . LEU   B 1 222 ? 15.725  5.627   -4.193  1 69.36  ? 207 LEU   B CA  1 
ATOM   4442 C  C   . LEU   B 1 222 ? 15.414  7.105   -4.416  1 70.2   ? 207 LEU   B C   1 
ATOM   4443 O  O   . LEU   B 1 222 ? 15.72   7.638   -5.478  1 70.2   ? 207 LEU   B O   1 
ATOM   4444 C  CB  . LEU   B 1 222 ? 14.68   4.742   -4.894  1 69.51  ? 207 LEU   B CB  1 
ATOM   4445 C  CG  . LEU   B 1 222 ? 14.879  3.234   -4.76   1 70.79  ? 207 LEU   B CG  1 
ATOM   4446 C  CD1 . LEU   B 1 222 ? 13.727  2.475   -5.387  1 71.24  ? 207 LEU   B CD1 1 
ATOM   4447 C  CD2 . LEU   B 1 222 ? 16.21   2.795   -5.344  1 71.46  ? 207 LEU   B CD2 1 
ATOM   4448 N  N   . GLU   B 1 223 ? 14.777  7.758   -3.435  1 70.84  ? 208 GLU   B N   1 
ATOM   4449 C  CA  . GLU   B 1 223 ? 14.485  9.187   -3.481  1 71.6   ? 208 GLU   B CA  1 
ATOM   4450 C  C   . GLU   B 1 223 ? 15.798  9.953   -3.21   1 72.36  ? 208 GLU   B C   1 
ATOM   4451 O  O   . GLU   B 1 223 ? 16.105  10.925  -3.906  1 72.38  ? 208 GLU   B O   1 
ATOM   4452 C  CB  . GLU   B 1 223 ? 13.389  9.539   -2.461  1 72.98  ? 208 GLU   B CB  1 
ATOM   4453 C  CG  . GLU   B 1 223 ? 11.988  9.19    -2.948  1 76.25  ? 208 GLU   B CG  1 
ATOM   4454 C  CD  . GLU   B 1 223 ? 10.922  9.002   -1.878  1 80.77  ? 208 GLU   B CD  1 
ATOM   4455 O  OE1 . GLU   B 1 223 ? 11.213  9.276   -0.69   1 81.27  ? 208 GLU   B OE1 1 
ATOM   4456 O  OE2 . GLU   B 1 223 ? 9.798   8.569   -2.228  1 81.98  ? 208 GLU   B OE2 1 
ATOM   4457 N  N   . LYS   B 1 224 ? 16.597  9.472   -2.238  1 72.86  ? 209 LYS   B N   1 
ATOM   4458 C  CA  . LYS   B 1 224 ? 17.898  10.05   -1.908  1 73.86  ? 209 LYS   B CA  1 
ATOM   4459 C  C   . LYS   B 1 224 ? 18.89   9.905   -3.091  1 75.06  ? 209 LYS   B C   1 
ATOM   4460 O  O   . LYS   B 1 224 ? 19.73   10.776  -3.296  1 75.66  ? 209 LYS   B O   1 
ATOM   4461 C  CB  . LYS   B 1 224 ? 18.46   9.412   -0.622  1 75     ? 209 LYS   B CB  1 
ATOM   4462 N  N   . ALA   B 1 225 ? 18.761  8.836   -3.884  1 75.48  ? 210 ALA   B N   1 
ATOM   4463 C  CA  . ALA   B 1 225 ? 19.615  8.603   -5.05   1 76.43  ? 210 ALA   B CA  1 
ATOM   4464 C  C   . ALA   B 1 225 ? 19.347  9.604   -6.177  1 77.23  ? 210 ALA   B C   1 
ATOM   4465 O  O   . ALA   B 1 225 ? 20.253  9.895   -6.953  1 77.21  ? 210 ALA   B O   1 
ATOM   4466 C  CB  . ALA   B 1 225 ? 19.442  7.176   -5.559  1 76.57  ? 210 ALA   B CB  1 
ATOM   4467 N  N   . LEU   B 1 226 ? 18.119  10.129  -6.274  1 78.17  ? 211 LEU   B N   1 
ATOM   4468 C  CA  . LEU   B 1 226 ? 17.79   11.126  -7.293  1 79.88  ? 211 LEU   B CA  1 
ATOM   4469 C  C   . LEU   B 1 226 ? 18.43   12.483  -6.963  1 82.08  ? 211 LEU   B C   1 
ATOM   4470 O  O   . LEU   B 1 226 ? 18.845  13.213  -7.87   1 82.29  ? 211 LEU   B O   1 
ATOM   4471 C  CB  . LEU   B 1 226 ? 16.269  11.25   -7.485  1 79.68  ? 211 LEU   B CB  1 
ATOM   4472 C  CG  . LEU   B 1 226 ? 15.785  12.226  -8.56   1 81.01  ? 211 LEU   B CG  1 
ATOM   4473 C  CD1 . LEU   B 1 226 ? 16.43   11.962  -9.901  1 81.6   ? 211 LEU   B CD1 1 
ATOM   4474 C  CD2 . LEU   B 1 226 ? 14.302  12.137  -8.734  1 81.62  ? 211 LEU   B CD2 1 
ATOM   4475 N  N   . GLN   B 1 227 ? 18.55   12.801  -5.662  1 83.31  ? 212 GLN   B N   1 
ATOM   4476 C  CA  . GLN   B 1 227 ? 19.198  14.029  -5.227  1 85     ? 212 GLN   B CA  1 
ATOM   4477 C  C   . GLN   B 1 227 ? 20.695  13.978  -5.602  1 86.67  ? 212 GLN   B C   1 
ATOM   4478 O  O   . GLN   B 1 227 ? 21.244  14.972  -6.088  1 86.99  ? 212 GLN   B O   1 
ATOM   4479 C  CB  . GLN   B 1 227 ? 19.002  14.227  -3.719  1 86.45  ? 212 GLN   B CB  1 
ATOM   4480 N  N   . VAL   B 1 228 ? 21.33   12.8    -5.429  1 87.39  ? 213 VAL   B N   1 
ATOM   4481 C  CA  . VAL   B 1 228 ? 22.729  12.559  -5.783  1 88.48  ? 213 VAL   B CA  1 
ATOM   4482 C  C   . VAL   B 1 228 ? 22.934  12.813  -7.283  1 90.15  ? 213 VAL   B C   1 
ATOM   4483 O  O   . VAL   B 1 228 ? 23.856  13.526  -7.662  1 90.53  ? 213 VAL   B O   1 
ATOM   4484 C  CB  . VAL   B 1 228 ? 23.159  11.127  -5.366  1 88.58  ? 213 VAL   B CB  1 
ATOM   4485 C  CG1 . VAL   B 1 228 ? 24.487  10.723  -6.007  1 89.08  ? 213 VAL   B CG1 1 
ATOM   4486 C  CG2 . VAL   B 1 228 ? 23.226  11.002  -3.849  1 88.63  ? 213 VAL   B CG2 1 
ATOM   4487 N  N   . PHE   B 1 229 ? 22.026  12.297  -8.12   1 91.1   ? 214 PHE   B N   1 
ATOM   4488 C  CA  . PHE   B 1 229 ? 22.056  12.442  -9.578  1 92.45  ? 214 PHE   B CA  1 
ATOM   4489 C  C   . PHE   B 1 229 ? 22.252  13.887  -10.053 1 93.77  ? 214 PHE   B C   1 
ATOM   4490 O  O   . PHE   B 1 229 ? 22.928  14.104  -11.057 1 94.33  ? 214 PHE   B O   1 
ATOM   4491 C  CB  . PHE   B 1 229 ? 20.761  11.871  -10.186 1 92.5   ? 214 PHE   B CB  1 
ATOM   4492 C  CG  . PHE   B 1 229 ? 20.875  11.265  -11.566 1 93.49  ? 214 PHE   B CG  1 
ATOM   4493 C  CD1 . PHE   B 1 229 ? 21.256  12.035  -12.65  1 94.53  ? 214 PHE   B CD1 1 
ATOM   4494 C  CD2 . PHE   B 1 229 ? 20.535  9.945   -11.79  1 94.56  ? 214 PHE   B CD2 1 
ATOM   4495 C  CE1 . PHE   B 1 229 ? 21.355  11.484  -13.917 1 95.37  ? 214 PHE   B CE1 1 
ATOM   4496 C  CE2 . PHE   B 1 229 ? 20.617  9.399   -13.065 1 95.37  ? 214 PHE   B CE2 1 
ATOM   4497 C  CZ  . PHE   B 1 229 ? 21.011  10.177  -14.121 1 95.21  ? 214 PHE   B CZ  1 
ATOM   4498 N  N   . HIS   B 1 230 ? 21.688  14.874  -9.339  1 94.09  ? 215 HIS   B N   1 
ATOM   4499 C  CA  . HIS   B 1 230 ? 21.763  16.282  -9.743  1 94.72  ? 215 HIS   B CA  1 
ATOM   4500 C  C   . HIS   B 1 230 ? 23.187  16.802  -10.055 1 94.15  ? 215 HIS   B C   1 
ATOM   4501 O  O   . HIS   B 1 230 ? 23.323  17.702  -10.887 1 94.06  ? 215 HIS   B O   1 
ATOM   4502 C  CB  . HIS   B 1 230 ? 21.057  17.177  -8.713  1 96.41  ? 215 HIS   B CB  1 
ATOM   4503 C  CG  . HIS   B 1 230 ? 19.585  16.893  -8.589  1 100.22 ? 215 HIS   B CG  1 
ATOM   4504 N  ND1 . HIS   B 1 230 ? 18.847  16.395  -9.658  1 102.46 ? 215 HIS   B ND1 1 
ATOM   4505 C  CD2 . HIS   B 1 230 ? 18.755  17.061  -7.531  1 101.75 ? 215 HIS   B CD2 1 
ATOM   4506 C  CE1 . HIS   B 1 230 ? 17.606  16.266  -9.213  1 103.04 ? 215 HIS   B CE1 1 
ATOM   4507 N  NE2 . HIS   B 1 230 ? 17.498  16.658  -7.942  1 102.96 ? 215 HIS   B NE2 1 
ATOM   4508 N  N   . GLN   B 1 231 ? 24.233  16.187  -9.46   1 93.35  ? 216 GLN   B N   1 
ATOM   4509 C  CA  . GLN   B 1 231 ? 25.631  16.562  -9.68   1 93.15  ? 216 GLN   B CA  1 
ATOM   4510 C  C   . GLN   B 1 231 ? 26.112  16.386  -11.109 1 93.27  ? 216 GLN   B C   1 
ATOM   4511 O  O   . GLN   B 1 231 ? 27.138  16.948  -11.456 1 93.32  ? 216 GLN   B O   1 
ATOM   4512 C  CB  . GLN   B 1 231 ? 26.566  15.757  -8.781  1 93.89  ? 216 GLN   B CB  1 
ATOM   4513 C  CG  . GLN   B 1 231 ? 26.261  15.857  -7.314  1 95.88  ? 216 GLN   B CG  1 
ATOM   4514 C  CD  . GLN   B 1 231 ? 27.05   14.801  -6.597  1 99.35  ? 216 GLN   B CD  1 
ATOM   4515 O  OE1 . GLN   B 1 231 ? 28.244  14.958  -6.327  1 100.7  ? 216 GLN   B OE1 1 
ATOM   4516 N  NE2 . GLN   B 1 231 ? 26.405  13.69   -6.29   1 99.88  ? 216 GLN   B NE2 1 
ATOM   4517 N  N   . ILE   B 1 232 ? 25.415  15.603  -11.932 1 93.32  ? 217 ILE   B N   1 
ATOM   4518 C  CA  . ILE   B 1 232 ? 25.832  15.357  -13.316 1 93.84  ? 217 ILE   B CA  1 
ATOM   4519 C  C   . ILE   B 1 232 ? 26.07   16.641  -14.124 1 94.07  ? 217 ILE   B C   1 
ATOM   4520 O  O   . ILE   B 1 232 ? 26.985  16.683  -14.952 1 94.27  ? 217 ILE   B O   1 
ATOM   4521 C  CB  . ILE   B 1 232 ? 24.843  14.414  -14.035 1 94.3   ? 217 ILE   B CB  1 
ATOM   4522 N  N   . HIS   B 1 233 ? 25.268  17.687  -13.865 1 93.8   ? 218 HIS   B N   1 
ATOM   4523 C  CA  . HIS   B 1 233 ? 25.397  18.955  -14.579 1 93.95  ? 218 HIS   B CA  1 
ATOM   4524 C  C   . HIS   B 1 233 ? 26.697  19.7    -14.256 1 93.91  ? 218 HIS   B C   1 
ATOM   4525 O  O   . HIS   B 1 233 ? 27.266  20.345  -15.138 1 94.09  ? 218 HIS   B O   1 
ATOM   4526 C  CB  . HIS   B 1 233 ? 24.176  19.85   -14.331 1 94.51  ? 218 HIS   B CB  1 
ATOM   4527 N  N   . ASP   B 1 234 ? 27.178  19.586  -13.01  1 93.38  ? 219 ASP   B N   1 
ATOM   4528 C  CA  . ASP   B 1 234 ? 28.378  20.28   -12.566 1 93.48  ? 219 ASP   B CA  1 
ATOM   4529 C  C   . ASP   B 1 234 ? 29.689  19.617  -12.931 1 93.24  ? 219 ASP   B C   1 
ATOM   4530 O  O   . ASP   B 1 234 ? 30.734  20.233  -12.702 1 93.95  ? 219 ASP   B O   1 
ATOM   4531 C  CB  . ASP   B 1 234 ? 28.356  20.466  -11.046 1 95.32  ? 219 ASP   B CB  1 
ATOM   4532 C  CG  . ASP   B 1 234 ? 27.149  21.21   -10.538 1 99.69  ? 219 ASP   B CG  1 
ATOM   4533 O  OD1 . ASP   B 1 234 ? 26.751  22.204  -11.183 1 100.26 ? 219 ASP   B OD1 1 
ATOM   4534 O  OD2 . ASP   B 1 234 ? 26.604  20.802  -9.495  1 101.88 ? 219 ASP   B OD2 1 
ATOM   4535 N  N   . HIS   B 1 235 ? 29.674  18.366  -13.419 1 92.19  ? 220 HIS   B N   1 
ATOM   4536 C  CA  . HIS   B 1 235 ? 30.937  17.669  -13.7   1 91.82  ? 220 HIS   B CA  1 
ATOM   4537 C  C   . HIS   B 1 235 ? 31.044  17.053  -15.1   1 91.75  ? 220 HIS   B C   1 
ATOM   4538 O  O   . HIS   B 1 235 ? 32.041  16.396  -15.409 1 92.19  ? 220 HIS   B O   1 
ATOM   4539 C  CB  . HIS   B 1 235 ? 31.219  16.617  -12.622 1 92.22  ? 220 HIS   B CB  1 
ATOM   4540 C  CG  . HIS   B 1 235 ? 31.045  17.142  -11.228 1 93.8   ? 220 HIS   B CG  1 
ATOM   4541 N  ND1 . HIS   B 1 235 ? 31.902  18.093  -10.702 1 95.54  ? 220 HIS   B ND1 1 
ATOM   4542 C  CD2 . HIS   B 1 235 ? 30.078  16.879  -10.321 1 94.65  ? 220 HIS   B CD2 1 
ATOM   4543 C  CE1 . HIS   B 1 235 ? 31.448  18.352  -9.486  1 95.85  ? 220 HIS   B CE1 1 
ATOM   4544 N  NE2 . HIS   B 1 235 ? 30.359  17.642  -9.21   1 95.69  ? 220 HIS   B NE2 1 
ATOM   4545 N  N   . VAL   B 1 236 ? 30.051  17.289  -15.953 1 91.19  ? 221 VAL   B N   1 
ATOM   4546 C  CA  . VAL   B 1 236 ? 30.061  16.795  -17.324 1 91.18  ? 221 VAL   B CA  1 
ATOM   4547 C  C   . VAL   B 1 236 ? 29.524  17.904  -18.24  1 91.03  ? 221 VAL   B C   1 
ATOM   4548 O  O   . VAL   B 1 236 ? 28.571  18.6    -17.866 1 91.04  ? 221 VAL   B O   1 
ATOM   4549 C  CB  . VAL   B 1 236 ? 29.221  15.498  -17.466 1 91.78  ? 221 VAL   B CB  1 
ATOM   4550 N  N   . ASN   B 1 237 ? 30.134  18.084  -19.426 1 90.52  ? 222 ASN   B N   1 
ATOM   4551 C  CA  . ASN   B 1 237 ? 29.639  19.068  -20.384 1 90.54  ? 222 ASN   B CA  1 
ATOM   4552 C  C   . ASN   B 1 237 ? 29.235  18.358  -21.671 1 90.38  ? 222 ASN   B C   1 
ATOM   4553 O  O   . ASN   B 1 237 ? 29.931  17.44   -22.116 1 90.34  ? 222 ASN   B O   1 
ATOM   4554 C  CB  . ASN   B 1 237 ? 30.622  20.231  -20.618 1 91.93  ? 222 ASN   B CB  1 
ATOM   4555 C  CG  . ASN   B 1 237 ? 31.849  19.929  -21.458 1 95.29  ? 222 ASN   B CG  1 
ATOM   4556 O  OD1 . ASN   B 1 237 ? 32.943  19.674  -20.931 1 96.4   ? 222 ASN   B OD1 1 
ATOM   4557 N  ND2 . ASN   B 1 237 ? 31.71   20.003  -22.784 1 95.52  ? 222 ASN   B ND2 1 
ATOM   4558 N  N   . PRO   B 1 238 ? 28.073  18.739  -22.246 1 90.27  ? 223 PRO   B N   1 
ATOM   4559 C  CA  . PRO   B 1 238 ? 27.577  18.051  -23.456 1 90.23  ? 223 PRO   B CA  1 
ATOM   4560 C  C   . PRO   B 1 238 ? 28.578  17.861  -24.6   1 90.25  ? 223 PRO   B C   1 
ATOM   4561 O  O   . PRO   B 1 238 ? 28.615  16.775  -25.176 1 89.99  ? 223 PRO   B O   1 
ATOM   4562 C  CB  . PRO   B 1 238 ? 26.382  18.914  -23.886 1 90.71  ? 223 PRO   B CB  1 
ATOM   4563 C  CG  . PRO   B 1 238 ? 25.884  19.523  -22.624 1 91.09  ? 223 PRO   B CG  1 
ATOM   4564 C  CD  . PRO   B 1 238 ? 27.122  19.774  -21.786 1 89.69  ? 223 PRO   B CD  1 
ATOM   4565 N  N   . LYS   B 1 239 ? 29.382  18.899  -24.925 1 90.23  ? 224 LYS   B N   1 
ATOM   4566 C  CA  . LYS   B 1 239 ? 30.359  18.835  -26.02  1 90.41  ? 224 LYS   B CA  1 
ATOM   4567 C  C   . LYS   B 1 239 ? 31.449  17.77   -25.808 1 90.05  ? 224 LYS   B C   1 
ATOM   4568 O  O   . LYS   B 1 239 ? 31.726  16.983  -26.715 1 90.2   ? 224 LYS   B O   1 
ATOM   4569 C  CB  . LYS   B 1 239 ? 30.978  20.217  -26.287 1 92.19  ? 224 LYS   B CB  1 
ATOM   4570 N  N   . ALA   B 1 240 ? 32.047  17.729  -24.614 1 89.24  ? 225 ALA   B N   1 
ATOM   4571 C  CA  . ALA   B 1 240 ? 33.1    16.763  -24.311 1 88.92  ? 225 ALA   B CA  1 
ATOM   4572 C  C   . ALA   B 1 240 ? 32.562  15.34   -24.246 1 88.5   ? 225 ALA   B C   1 
ATOM   4573 O  O   . ALA   B 1 240 ? 33.236  14.405  -24.68  1 88.42  ? 225 ALA   B O   1 
ATOM   4574 C  CB  . ALA   B 1 240 ? 33.767  17.124  -23     1 89.05  ? 225 ALA   B CB  1 
ATOM   4575 N  N   . PHE   B 1 241 ? 31.347  15.174  -23.703 1 88.07  ? 226 PHE   B N   1 
ATOM   4576 C  CA  . PHE   B 1 241 ? 30.734  13.854  -23.603 1 87.83  ? 226 PHE   B CA  1 
ATOM   4577 C  C   . PHE   B 1 241 ? 30.39   13.303  -24.993 1 88     ? 226 PHE   B C   1 
ATOM   4578 O  O   . PHE   B 1 241 ? 30.703  12.151  -25.298 1 87.92  ? 226 PHE   B O   1 
ATOM   4579 C  CB  . PHE   B 1 241 ? 29.475  13.887  -22.701 1 87.24  ? 226 PHE   B CB  1 
ATOM   4580 C  CG  . PHE   B 1 241 ? 28.784  12.547  -22.619 1 87.34  ? 226 PHE   B CG  1 
ATOM   4581 C  CD1 . PHE   B 1 241 ? 29.279  11.543  -21.805 1 87.83  ? 226 PHE   B CD1 1 
ATOM   4582 C  CD2 . PHE   B 1 241 ? 27.675  12.27   -23.402 1 87.89  ? 226 PHE   B CD2 1 
ATOM   4583 C  CE1 . PHE   B 1 241 ? 28.663  10.299  -21.758 1 88.4   ? 226 PHE   B CE1 1 
ATOM   4584 C  CE2 . PHE   B 1 241 ? 27.079  11.015  -23.371 1 88.38  ? 226 PHE   B CE2 1 
ATOM   4585 C  CZ  . PHE   B 1 241 ? 27.559  10.047  -22.53  1 88.06  ? 226 PHE   B CZ  1 
ATOM   4586 N  N   . PHE   B 1 242 ? 29.724  14.124  -25.821 1 88.07  ? 227 PHE   B N   1 
ATOM   4587 C  CA  . PHE   B 1 242 ? 29.283  13.711  -27.149 1 88.4   ? 227 PHE   B CA  1 
ATOM   4588 C  C   . PHE   B 1 242 ? 30.419  13.528  -28.149 1 87.84  ? 227 PHE   B C   1 
ATOM   4589 O  O   . PHE   B 1 242 ? 30.443  12.527  -28.861 1 88.02  ? 227 PHE   B O   1 
ATOM   4590 C  CB  . PHE   B 1 242 ? 28.214  14.685  -27.696 1 88.75  ? 227 PHE   B CB  1 
ATOM   4591 C  CG  . PHE   B 1 242 ? 27.597  14.244  -28.998 1 89.94  ? 227 PHE   B CG  1 
ATOM   4592 C  CD1 . PHE   B 1 242 ? 26.619  13.266  -29.022 1 91.06  ? 227 PHE   B CD1 1 
ATOM   4593 C  CD2 . PHE   B 1 242 ? 28.007  14.795  -30.2   1 90.85  ? 227 PHE   B CD2 1 
ATOM   4594 C  CE1 . PHE   B 1 242 ? 26.067  12.846  -30.226 1 91.95  ? 227 PHE   B CE1 1 
ATOM   4595 C  CE2 . PHE   B 1 242 ? 27.46   14.367  -31.402 1 91.62  ? 227 PHE   B CE2 1 
ATOM   4596 C  CZ  . PHE   B 1 242 ? 26.5    13.391  -31.41  1 91.6   ? 227 PHE   B CZ  1 
ATOM   4597 N  N   . SER   B 1 243 ? 31.341  14.498  -28.226 1 87.03  ? 228 SER   B N   1 
ATOM   4598 C  CA  . SER   B 1 243 ? 32.419  14.443  -29.209 1 86.91  ? 228 SER   B CA  1 
ATOM   4599 C  C   . SER   B 1 243 ? 33.66   13.652  -28.787 1 86.42  ? 228 SER   B C   1 
ATOM   4600 O  O   . SER   B 1 243 ? 34.429  13.259  -29.667 1 86.71  ? 228 SER   B O   1 
ATOM   4601 C  CB  . SER   B 1 243 ? 32.826  15.85   -29.641 1 88.1   ? 228 SER   B CB  1 
ATOM   4602 N  N   . VAL   B 1 244 ? 33.875  13.42   -27.474 1 85.24  ? 229 VAL   B N   1 
ATOM   4603 C  CA  . VAL   B 1 244 ? 35.086  12.723  -27.047 1 84.31  ? 229 VAL   B CA  1 
ATOM   4604 C  C   . VAL   B 1 244 ? 34.808  11.385  -26.303 1 83.08  ? 229 VAL   B C   1 
ATOM   4605 O  O   . VAL   B 1 244 ? 35.055  10.328  -26.886 1 83.22  ? 229 VAL   B O   1 
ATOM   4606 C  CB  . VAL   B 1 244 ? 36.041  13.661  -26.256 1 84.93  ? 229 VAL   B CB  1 
ATOM   4607 N  N   . LEU   B 1 245 ? 34.315  11.421  -25.042 1 81.58  ? 230 LEU   B N   1 
ATOM   4608 C  CA  . LEU   B 1 245 ? 34.111  10.238  -24.208 1 80.52  ? 230 LEU   B CA  1 
ATOM   4609 C  C   . LEU   B 1 245 ? 33.365  9.079   -24.882 1 79.98  ? 230 LEU   B C   1 
ATOM   4610 O  O   . LEU   B 1 245 ? 33.762  7.925   -24.723 1 80.18  ? 230 LEU   B O   1 
ATOM   4611 C  CB  . LEU   B 1 245 ? 33.414  10.638  -22.903 1 80.08  ? 230 LEU   B CB  1 
ATOM   4612 C  CG  . LEU   B 1 245 ? 33.447  9.615   -21.778 1 80.75  ? 230 LEU   B CG  1 
ATOM   4613 C  CD1 . LEU   B 1 245 ? 34.887  9.213   -21.421 1 80.9   ? 230 LEU   B CD1 1 
ATOM   4614 C  CD2 . LEU   B 1 245 ? 32.749  10.154  -20.573 1 81.24  ? 230 LEU   B CD2 1 
ATOM   4615 N  N   . ARG   B 1 246 ? 32.297  9.397   -25.63  1 79.07  ? 231 ARG   B N   1 
ATOM   4616 C  CA  . ARG   B 1 246 ? 31.443  8.45    -26.342 1 78.59  ? 231 ARG   B CA  1 
ATOM   4617 C  C   . ARG   B 1 246 ? 32.259  7.461   -27.206 1 77.39  ? 231 ARG   B C   1 
ATOM   4618 O  O   . ARG   B 1 246 ? 31.947  6.27    -27.24  1 77.07  ? 231 ARG   B O   1 
ATOM   4619 C  CB  . ARG   B 1 246 ? 30.405  9.237   -27.186 1 80.31  ? 231 ARG   B CB  1 
ATOM   4620 C  CG  . ARG   B 1 246 ? 29.715  8.405   -28.268 1 83.99  ? 231 ARG   B CG  1 
ATOM   4621 C  CD  . ARG   B 1 246 ? 28.831  9.174   -29.214 1 87.83  ? 231 ARG   B CD  1 
ATOM   4622 N  NE  . ARG   B 1 246 ? 29.551  10.054  -30.131 1 91.85  ? 231 ARG   B NE  1 
ATOM   4623 C  CZ  . ARG   B 1 246 ? 29.06   10.506  -31.283 1 94.99  ? 231 ARG   B CZ  1 
ATOM   4624 N  NH1 . ARG   B 1 246 ? 29.78   11.325  -32.042 1 95.11  ? 231 ARG   B NH1 1 
ATOM   4625 N  NH2 . ARG   B 1 246 ? 27.843  10.149  -31.682 1 95     ? 231 ARG   B NH2 1 
ATOM   4626 N  N   . ILE   B 1 247 ? 33.292  7.967   -27.9   1 76.48  ? 232 ILE   B N   1 
ATOM   4627 C  CA  . ILE   B 1 247 ? 34.157  7.179   -28.78  1 76.01  ? 232 ILE   B CA  1 
ATOM   4628 C  C   . ILE   B 1 247 ? 34.756  5.966   -28.067 1 75.17  ? 232 ILE   B C   1 
ATOM   4629 O  O   . ILE   B 1 247 ? 34.655  4.845   -28.556 1 75.05  ? 232 ILE   B O   1 
ATOM   4630 C  CB  . ILE   B 1 247 ? 35.29   8.082   -29.352 1 76.9   ? 232 ILE   B CB  1 
ATOM   4631 C  CG1 . ILE   B 1 247 ? 34.727  9.251   -30.176 1 78.09  ? 232 ILE   B CG1 1 
ATOM   4632 C  CG2 . ILE   B 1 247 ? 36.336  7.265   -30.122 1 77.34  ? 232 ILE   B CG2 1 
ATOM   4633 C  CD1 . ILE   B 1 247 ? 34.002  8.843   -31.428 1 79.28  ? 232 ILE   B CD1 1 
ATOM   4634 N  N   . TYR   B 1 248 ? 35.36   6.196   -26.901 1 74.48  ? 233 TYR   B N   1 
ATOM   4635 C  CA  . TYR   B 1 248 ? 36.08   5.195   -26.128 1 74.36  ? 233 TYR   B CA  1 
ATOM   4636 C  C   . TYR   B 1 248 ? 35.162  4.197   -25.392 1 74.08  ? 233 TYR   B C   1 
ATOM   4637 O  O   . TYR   B 1 248 ? 35.596  3.089   -25.053 1 74.04  ? 233 TYR   B O   1 
ATOM   4638 C  CB  . TYR   B 1 248 ? 37.064  5.914   -25.201 1 74.27  ? 233 TYR   B CB  1 
ATOM   4639 C  CG  . TYR   B 1 248 ? 38.067  6.707   -26.017 1 74.81  ? 233 TYR   B CG  1 
ATOM   4640 C  CD1 . TYR   B 1 248 ? 39.111  6.068   -26.677 1 75.58  ? 233 TYR   B CD1 1 
ATOM   4641 C  CD2 . TYR   B 1 248 ? 37.883  8.065   -26.253 1 75.46  ? 233 TYR   B CD2 1 
ATOM   4642 C  CE1 . TYR   B 1 248 ? 39.993  6.773   -27.482 1 76.43  ? 233 TYR   B CE1 1 
ATOM   4643 C  CE2 . TYR   B 1 248 ? 38.758  8.782   -27.059 1 76.19  ? 233 TYR   B CE2 1 
ATOM   4644 C  CZ  . TYR   B 1 248 ? 39.821  8.132   -27.664 1 77.23  ? 233 TYR   B CZ  1 
ATOM   4645 O  OH  . TYR   B 1 248 ? 40.711  8.818   -28.456 1 78.54  ? 233 TYR   B OH  1 
ATOM   4646 N  N   . LEU   B 1 249 ? 33.883  4.562   -25.214 1 73.36  ? 234 LEU   B N   1 
ATOM   4647 C  CA  . LEU   B 1 249 ? 32.876  3.682   -24.632 1 72.88  ? 234 LEU   B CA  1 
ATOM   4648 C  C   . LEU   B 1 249 ? 32.305  2.718   -25.703 1 71.7   ? 234 LEU   B C   1 
ATOM   4649 O  O   . LEU   B 1 249 ? 31.686  1.738   -25.328 1 72.01  ? 234 LEU   B O   1 
ATOM   4650 C  CB  . LEU   B 1 249 ? 31.719  4.507   -24.039 1 73.4   ? 234 LEU   B CB  1 
ATOM   4651 C  CG  . LEU   B 1 249 ? 32.072  5.541   -22.971 1 75.27  ? 234 LEU   B CG  1 
ATOM   4652 C  CD1 . LEU   B 1 249 ? 30.836  6.375   -22.578 1 76.13  ? 234 LEU   B CD1 1 
ATOM   4653 C  CD2 . LEU   B 1 249 ? 32.687  4.881   -21.766 1 75.7   ? 234 LEU   B CD2 1 
ATOM   4654 N  N   . SER   B 1 250 ? 32.467  3.005   -27.014 1 70.26  ? 235 SER   B N   1 
ATOM   4655 C  CA  . SER   B 1 250 ? 31.942  2.182   -28.106 1 69.4   ? 235 SER   B CA  1 
ATOM   4656 C  C   . SER   B 1 250 ? 32.527  0.778   -28.17  1 68.63  ? 235 SER   B C   1 
ATOM   4657 O  O   . SER   B 1 250 ? 33.72   0.575   -27.957 1 68.49  ? 235 SER   B O   1 
ATOM   4658 C  CB  . SER   B 1 250 ? 32.12   2.881   -29.448 1 70.34  ? 235 SER   B CB  1 
ATOM   4659 N  N   . GLY   B 1 251 ? 31.67   -0.187  -28.451 1 68.17  ? 236 GLY   B N   1 
ATOM   4660 C  CA  . GLY   B 1 251 ? 32.075  -1.581  -28.557 1 68.36  ? 236 GLY   B CA  1 
ATOM   4661 C  C   . GLY   B 1 251 ? 32.086  -2.075  -29.983 1 68.41  ? 236 GLY   B C   1 
ATOM   4662 O  O   . GLY   B 1 251 ? 32.079  -1.272  -30.918 1 68.49  ? 236 GLY   B O   1 
ATOM   4663 N  N   . TRP   B 1 252 ? 32.118  -3.391  -30.167 1 68.39  ? 237 TRP   B N   1 
ATOM   4664 C  CA  . TRP   B 1 252 ? 32.169  -3.973  -31.513 1 69.08  ? 237 TRP   B CA  1 
ATOM   4665 C  C   . TRP   B 1 252 ? 31.079  -5.023  -31.749 1 71.29  ? 237 TRP   B C   1 
ATOM   4666 O  O   . TRP   B 1 252 ? 31.35   -6.078  -32.308 1 71.83  ? 237 TRP   B O   1 
ATOM   4667 C  CB  . TRP   B 1 252 ? 33.576  -4.518  -31.879 1 67.69  ? 237 TRP   B CB  1 
ATOM   4668 C  CG  . TRP   B 1 252 ? 34.457  -4.924  -30.725 1 66.53  ? 237 TRP   B CG  1 
ATOM   4669 C  CD1 . TRP   B 1 252 ? 34.646  -6.185  -30.243 1 66.9   ? 237 TRP   B CD1 1 
ATOM   4670 C  CD2 . TRP   B 1 252 ? 35.305  -4.066  -29.946 1 65.82  ? 237 TRP   B CD2 1 
ATOM   4671 N  NE1 . TRP   B 1 252 ? 35.553  -6.166  -29.209 1 66.88  ? 237 TRP   B NE1 1 
ATOM   4672 C  CE2 . TRP   B 1 252 ? 35.963  -4.876  -28.997 1 66.56  ? 237 TRP   B CE2 1 
ATOM   4673 C  CE3 . TRP   B 1 252 ? 35.559  -2.688  -29.945 1 65.89  ? 237 TRP   B CE3 1 
ATOM   4674 C  CZ2 . TRP   B 1 252 ? 36.857  -4.353  -28.061 1 67     ? 237 TRP   B CZ2 1 
ATOM   4675 C  CZ3 . TRP   B 1 252 ? 36.439  -2.171  -29.014 1 66.55  ? 237 TRP   B CZ3 1 
ATOM   4676 C  CH2 . TRP   B 1 252 ? 37.079  -2.998  -28.089 1 66.84  ? 237 TRP   B CH2 1 
ATOM   4677 N  N   . LYS   B 1 253 ? 29.849  -4.728  -31.332 1 72.21  ? 238 LYS   B N   1 
ATOM   4678 C  CA  . LYS   B 1 253 ? 28.714  -5.618  -31.552 1 73.76  ? 238 LYS   B CA  1 
ATOM   4679 C  C   . LYS   B 1 253 ? 27.728  -4.818  -32.368 1 75.51  ? 238 LYS   B C   1 
ATOM   4680 O  O   . LYS   B 1 253 ? 27.127  -3.887  -31.842 1 75.75  ? 238 LYS   B O   1 
ATOM   4681 C  CB  . LYS   B 1 253 ? 28.059  -6.036  -30.223 1 75.24  ? 238 LYS   B CB  1 
ATOM   4682 N  N   . GLY   B 1 254 ? 27.601  -5.141  -33.651 1 76.53  ? 239 GLY   B N   1 
ATOM   4683 C  CA  . GLY   B 1 254 ? 26.701  -4.421  -34.542 1 77.81  ? 239 GLY   B CA  1 
ATOM   4684 C  C   . GLY   B 1 254 ? 27.179  -3.018  -34.864 1 79.06  ? 239 GLY   B C   1 
ATOM   4685 O  O   . GLY   B 1 254 ? 26.368  -2.126  -35.123 1 79.21  ? 239 GLY   B O   1 
ATOM   4686 N  N   . ASN   B 1 255 ? 28.504  -2.81   -34.84  1 79.81  ? 240 ASN   B N   1 
ATOM   4687 C  CA  . ASN   B 1 255 ? 29.117  -1.526  -35.149 1 81.1   ? 240 ASN   B CA  1 
ATOM   4688 C  C   . ASN   B 1 255 ? 29.643  -1.589  -36.577 1 82.75  ? 240 ASN   B C   1 
ATOM   4689 O  O   . ASN   B 1 255 ? 30.451  -2.46   -36.907 1 82.96  ? 240 ASN   B O   1 
ATOM   4690 C  CB  . ASN   B 1 255 ? 30.267  -1.237  -34.176 1 81.56  ? 240 ASN   B CB  1 
ATOM   4691 C  CG  . ASN   B 1 255 ? 30.789  0.178   -34.209 1 83.97  ? 240 ASN   B CG  1 
ATOM   4692 O  OD1 . ASN   B 1 255 ? 30.752  0.868   -35.228 1 85.23  ? 240 ASN   B OD1 1 
ATOM   4693 N  ND2 . ASN   B 1 255 ? 31.303  0.649   -33.086 1 84.25  ? 240 ASN   B ND2 1 
ATOM   4694 N  N   . PRO   B 1 256 ? 29.224  -0.646  -37.434 1 83.55  ? 241 PRO   B N   1 
ATOM   4695 C  CA  . PRO   B 1 256 ? 29.704  -0.654  -38.827 1 84.19  ? 241 PRO   B CA  1 
ATOM   4696 C  C   . PRO   B 1 256 ? 31.207  -0.426  -38.983 1 85.21  ? 241 PRO   B C   1 
ATOM   4697 O  O   . PRO   B 1 256 ? 31.757  -0.752  -40.033 1 85.42  ? 241 PRO   B O   1 
ATOM   4698 C  CB  . PRO   B 1 256 ? 28.887  0.458   -39.491 1 84.75  ? 241 PRO   B CB  1 
ATOM   4699 C  CG  . PRO   B 1 256 ? 27.725  0.702   -38.564 1 84.97  ? 241 PRO   B CG  1 
ATOM   4700 C  CD  . PRO   B 1 256 ? 28.254  0.439   -37.2   1 83.21  ? 241 PRO   B CD  1 
ATOM   4701 N  N   . GLN   B 1 257 ? 31.878  0.108   -37.942 1 85.71  ? 242 GLN   B N   1 
ATOM   4702 C  CA  . GLN   B 1 257 ? 33.326  0.328   -37.967 1 86.48  ? 242 GLN   B CA  1 
ATOM   4703 C  C   . GLN   B 1 257 ? 34.113  -0.977  -37.783 1 87.49  ? 242 GLN   B C   1 
ATOM   4704 O  O   . GLN   B 1 257 ? 35.249  -1.061  -38.238 1 88.03  ? 242 GLN   B O   1 
ATOM   4705 C  CB  . GLN   B 1 257 ? 33.741  1.391   -36.952 1 87.59  ? 242 GLN   B CB  1 
ATOM   4706 C  CG  . GLN   B 1 257 ? 32.982  2.695   -37.145 1 90.47  ? 242 GLN   B CG  1 
ATOM   4707 C  CD  . GLN   B 1 257 ? 33.445  3.766   -36.199 1 94.92  ? 242 GLN   B CD  1 
ATOM   4708 O  OE1 . GLN   B 1 257 ? 32.752  4.13    -35.246 1 96.59  ? 242 GLN   B OE1 1 
ATOM   4709 N  NE2 . GLN   B 1 257 ? 34.632  4.292   -36.439 1 95.81  ? 242 GLN   B NE2 1 
ATOM   4710 N  N   . LEU   B 1 258 ? 33.517  -1.991  -37.127 1 87.57  ? 243 LEU   B N   1 
ATOM   4711 C  CA  . LEU   B 1 258 ? 34.101  -3.327  -36.948 1 87.97  ? 243 LEU   B CA  1 
ATOM   4712 C  C   . LEU   B 1 258 ? 32.933  -4.295  -37.156 1 88.15  ? 243 LEU   B C   1 
ATOM   4713 O  O   . LEU   B 1 258 ? 32.452  -4.924  -36.207 1 88.51  ? 243 LEU   B O   1 
ATOM   4714 C  CB  . LEU   B 1 258 ? 34.701  -3.514  -35.543 1 88.36  ? 243 LEU   B CB  1 
ATOM   4715 C  CG  . LEU   B 1 258 ? 36.001  -2.797  -35.247 1 90.25  ? 243 LEU   B CG  1 
ATOM   4716 C  CD1 . LEU   B 1 258 ? 35.734  -1.486  -34.541 1 91.18  ? 243 LEU   B CD1 1 
ATOM   4717 C  CD2 . LEU   B 1 258 ? 36.89   -3.645  -34.362 1 90.81  ? 243 LEU   B CD2 1 
ATOM   4718 N  N   . SER   B 1 259 ? 32.419  -4.342  -38.393 1 87.62  ? 244 SER   B N   1 
ATOM   4719 C  CA  . SER   B 1 259 ? 31.246  -5.134  -38.759 1 87.47  ? 244 SER   B CA  1 
ATOM   4720 C  C   . SER   B 1 259 ? 31.281  -6.601  -38.308 1 86.81  ? 244 SER   B C   1 
ATOM   4721 O  O   . SER   B 1 259 ? 30.232  -7.14   -37.956 1 86.85  ? 244 SER   B O   1 
ATOM   4722 C  CB  . SER   B 1 259 ? 30.985  -5.046  -40.259 1 88.78  ? 244 SER   B CB  1 
ATOM   4723 N  N   . ASP   B 1 260 ? 32.461  -7.239  -38.29  1 86.09  ? 245 ASP   B N   1 
ATOM   4724 C  CA  . ASP   B 1 260 ? 32.556  -8.643  -37.869 1 86.05  ? 245 ASP   B CA  1 
ATOM   4725 C  C   . ASP   B 1 260 ? 33.086  -8.854  -36.422 1 85.66  ? 245 ASP   B C   1 
ATOM   4726 O  O   . ASP   B 1 260 ? 33.172  -9.991  -35.949 1 85.58  ? 245 ASP   B O   1 
ATOM   4727 C  CB  . ASP   B 1 260 ? 33.391  -9.452  -38.881 1 87.47  ? 245 ASP   B CB  1 
ATOM   4728 N  N   . GLY   B 1 261 ? 33.421  -7.769  -35.738 1 85.04  ? 246 GLY   B N   1 
ATOM   4729 C  CA  . GLY   B 1 261 ? 33.966  -7.838  -34.394 1 85.03  ? 246 GLY   B CA  1 
ATOM   4730 C  C   . GLY   B 1 261 ? 35.443  -7.508  -34.372 1 84.97  ? 246 GLY   B C   1 
ATOM   4731 O  O   . GLY   B 1 261 ? 35.966  -6.91   -35.315 1 85.3   ? 246 GLY   B O   1 
ATOM   4732 N  N   . LEU   B 1 262 ? 36.131  -7.887  -33.293 1 84.27  ? 247 LEU   B N   1 
ATOM   4733 C  CA  . LEU   B 1 262 ? 37.556  -7.613  -33.153 1 84.03  ? 247 LEU   B CA  1 
ATOM   4734 C  C   . LEU   B 1 262 ? 38.33   -8.914  -33.141 1 83.78  ? 247 LEU   B C   1 
ATOM   4735 O  O   . LEU   B 1 262 ? 37.862  -9.898  -32.565 1 83.92  ? 247 LEU   B O   1 
ATOM   4736 C  CB  . LEU   B 1 262 ? 37.799  -6.864  -31.838 1 84.3   ? 247 LEU   B CB  1 
ATOM   4737 C  CG  . LEU   B 1 262 ? 39.228  -6.436  -31.554 1 85.6   ? 247 LEU   B CG  1 
ATOM   4738 C  CD1 . LEU   B 1 262 ? 39.636  -5.305  -32.464 1 86.13  ? 247 LEU   B CD1 1 
ATOM   4739 C  CD2 . LEU   B 1 262 ? 39.397  -6.043  -30.102 1 86.11  ? 247 LEU   B CD2 1 
ATOM   4740 N  N   . VAL   B 1 263 ? 39.515  -8.931  -33.757 1 83.35  ? 248 VAL   B N   1 
ATOM   4741 C  CA  . VAL   B 1 263 ? 40.336  -10.133 -33.755 1 83.52  ? 248 VAL   B CA  1 
ATOM   4742 C  C   . VAL   B 1 263 ? 41.165  -10.159 -32.487 1 84.04  ? 248 VAL   B C   1 
ATOM   4743 O  O   . VAL   B 1 263 ? 41.898  -9.212  -32.22  1 83.83  ? 248 VAL   B O   1 
ATOM   4744 C  CB  . VAL   B 1 263 ? 41.212  -10.236 -35.015 1 83.69  ? 248 VAL   B CB  1 
ATOM   4745 C  CG1 . VAL   B 1 263 ? 41.994  -11.542 -35.022 1 83.94  ? 248 VAL   B CG1 1 
ATOM   4746 C  CG2 . VAL   B 1 263 ? 40.36   -10.108 -36.268 1 84.02  ? 248 VAL   B CG2 1 
ATOM   4747 N  N   . TYR   B 1 264 ? 41.022  -11.214 -31.679 1 84.48  ? 249 TYR   B N   1 
ATOM   4748 C  CA  . TYR   B 1 264 ? 41.806  -11.353 -30.451 1 85.24  ? 249 TYR   B CA  1 
ATOM   4749 C  C   . TYR   B 1 264 ? 42.952  -12.301 -30.781 1 85.19  ? 249 TYR   B C   1 
ATOM   4750 O  O   . TYR   B 1 264 ? 42.868  -13.502 -30.515 1 85.36  ? 249 TYR   B O   1 
ATOM   4751 C  CB  . TYR   B 1 264 ? 40.931  -11.885 -29.293 1 85.81  ? 249 TYR   B CB  1 
ATOM   4752 C  CG  . TYR   B 1 264 ? 39.924  -10.865 -28.796 1 86.87  ? 249 TYR   B CG  1 
ATOM   4753 C  CD1 . TYR   B 1 264 ? 38.658  -10.779 -29.355 1 87.77  ? 249 TYR   B CD1 1 
ATOM   4754 C  CD2 . TYR   B 1 264 ? 40.263  -9.945  -27.811 1 87.77  ? 249 TYR   B CD2 1 
ATOM   4755 C  CE1 . TYR   B 1 264 ? 37.744  -9.821  -28.93  1 88.65  ? 249 TYR   B CE1 1 
ATOM   4756 C  CE2 . TYR   B 1 264 ? 39.358  -8.983  -27.379 1 88.63  ? 249 TYR   B CE2 1 
ATOM   4757 C  CZ  . TYR   B 1 264 ? 38.1    -8.921  -27.943 1 89.5   ? 249 TYR   B CZ  1 
ATOM   4758 O  OH  . TYR   B 1 264 ? 37.201  -7.977  -27.506 1 90.8   ? 249 TYR   B OH  1 
ATOM   4759 N  N   . GLU   B 1 265 ? 43.984  -11.76  -31.452 1 84.74  ? 250 GLU   B N   1 
ATOM   4760 C  CA  . GLU   B 1 265 ? 45.151  -12.491 -31.951 1 84.59  ? 250 GLU   B CA  1 
ATOM   4761 C  C   . GLU   B 1 265 ? 45.758  -13.47  -30.958 1 84.12  ? 250 GLU   B C   1 
ATOM   4762 O  O   . GLU   B 1 265 ? 46.048  -13.107 -29.816 1 84.3   ? 250 GLU   B O   1 
ATOM   4763 C  CB  . GLU   B 1 265 ? 46.216  -11.508 -32.457 1 86.61  ? 250 GLU   B CB  1 
ATOM   4764 C  CG  . GLU   B 1 265 ? 47.385  -12.164 -33.167 1 90.27  ? 250 GLU   B CG  1 
ATOM   4765 C  CD  . GLU   B 1 265 ? 48.439  -11.177 -33.619 1 94.54  ? 250 GLU   B CD  1 
ATOM   4766 O  OE1 . GLU   B 1 265 ? 49.219  -10.712 -32.756 1 94.73  ? 250 GLU   B OE1 1 
ATOM   4767 O  OE2 . GLU   B 1 265 ? 48.479  -10.855 -34.828 1 96.51  ? 250 GLU   B OE2 1 
ATOM   4768 N  N   . GLY   B 1 266 ? 45.912  -14.714 -31.395 1 83.4   ? 251 GLY   B N   1 
ATOM   4769 C  CA  . GLY   B 1 266 ? 46.496  -15.766 -30.571 1 83.5   ? 251 GLY   B CA  1 
ATOM   4770 C  C   . GLY   B 1 266 ? 45.577  -16.373 -29.528 1 83.29  ? 251 GLY   B C   1 
ATOM   4771 O  O   . GLY   B 1 266 ? 46.025  -17.144 -28.678 1 83.25  ? 251 GLY   B O   1 
ATOM   4772 N  N   . PHE   B 1 267 ? 44.286  -16.026 -29.573 1 83.02  ? 252 PHE   B N   1 
ATOM   4773 C  CA  . PHE   B 1 267 ? 43.309  -16.552 -28.637 1 83.16  ? 252 PHE   B CA  1 
ATOM   4774 C  C   . PHE   B 1 267 ? 42.121  -17.116 -29.408 1 83.52  ? 252 PHE   B C   1 
ATOM   4775 O  O   . PHE   B 1 267 ? 41.652  -18.215 -29.107 1 83.53  ? 252 PHE   B O   1 
ATOM   4776 C  CB  . PHE   B 1 267 ? 42.865  -15.471 -27.64  1 83.04  ? 252 PHE   B CB  1 
ATOM   4777 C  CG  . PHE   B 1 267 ? 42.267  -16.073 -26.396 1 83.63  ? 252 PHE   B CG  1 
ATOM   4778 C  CD1 . PHE   B 1 267 ? 43.066  -16.407 -25.319 1 84.31  ? 252 PHE   B CD1 1 
ATOM   4779 C  CD2 . PHE   B 1 267 ? 40.911  -16.353 -26.322 1 84.46  ? 252 PHE   B CD2 1 
ATOM   4780 C  CE1 . PHE   B 1 267 ? 42.517  -16.99  -24.183 1 85.07  ? 252 PHE   B CE1 1 
ATOM   4781 C  CE2 . PHE   B 1 267 ? 40.366  -16.937 -25.187 1 85.09  ? 252 PHE   B CE2 1 
ATOM   4782 C  CZ  . PHE   B 1 267 ? 41.171  -17.247 -24.122 1 84.87  ? 252 PHE   B CZ  1 
ATOM   4783 N  N   . TRP   B 1 268 ? 41.641  -16.371 -30.407 1 83.62  ? 253 TRP   B N   1 
ATOM   4784 C  CA  . TRP   B 1 268 ? 40.54   -16.826 -31.238 1 84.4   ? 253 TRP   B CA  1 
ATOM   4785 C  C   . TRP   B 1 268 ? 40.907  -16.75  -32.723 1 85.12  ? 253 TRP   B C   1 
ATOM   4786 O  O   . TRP   B 1 268 ? 41.751  -15.944 -33.126 1 85.2   ? 253 TRP   B O   1 
ATOM   4787 C  CB  . TRP   B 1 268 ? 39.255  -16.042 -30.944 1 84.38  ? 253 TRP   B CB  1 
ATOM   4788 C  CG  . TRP   B 1 268 ? 38.588  -16.435 -29.658 1 85.06  ? 253 TRP   B CG  1 
ATOM   4789 C  CD1 . TRP   B 1 268 ? 38.234  -17.692 -29.267 1 85.84  ? 253 TRP   B CD1 1 
ATOM   4790 C  CD2 . TRP   B 1 268 ? 38.154  -15.552 -28.614 1 85.21  ? 253 TRP   B CD2 1 
ATOM   4791 N  NE1 . TRP   B 1 268 ? 37.633  -17.651 -28.032 1 86.14  ? 253 TRP   B NE1 1 
ATOM   4792 C  CE2 . TRP   B 1 268 ? 37.567  -16.347 -27.61  1 85.96  ? 253 TRP   B CE2 1 
ATOM   4793 C  CE3 . TRP   B 1 268 ? 38.209  -14.164 -28.428 1 85.7   ? 253 TRP   B CE3 1 
ATOM   4794 C  CZ2 . TRP   B 1 268 ? 37.032  -15.798 -26.446 1 86.55  ? 253 TRP   B CZ2 1 
ATOM   4795 C  CZ3 . TRP   B 1 268 ? 37.69   -13.624 -27.268 1 86.43  ? 253 TRP   B CZ3 1 
ATOM   4796 C  CH2 . TRP   B 1 268 ? 37.108  -14.435 -26.295 1 86.59  ? 253 TRP   B CH2 1 
ATOM   4797 N  N   . GLU   B 1 269 ? 40.282  -17.604 -33.538 1 85.31  ? 254 GLU   B N   1 
ATOM   4798 C  CA  . GLU   B 1 269 ? 40.543  -17.615 -34.975 1 85.8   ? 254 GLU   B CA  1 
ATOM   4799 C  C   . GLU   B 1 269 ? 39.678  -16.558 -35.67  1 85.79  ? 254 GLU   B C   1 
ATOM   4800 O  O   . GLU   B 1 269 ? 40.19   -15.747 -36.447 1 85.97  ? 254 GLU   B O   1 
ATOM   4801 C  CB  . GLU   B 1 269 ? 40.288  -19.017 -35.567 1 88.24  ? 254 GLU   B CB  1 
ATOM   4802 N  N   . ASP   B 1 270 ? 38.371  -16.55  -35.357 1 85.3   ? 255 ASP   B N   1 
ATOM   4803 C  CA  . ASP   B 1 270 ? 37.404  -15.611 -35.919 1 85.23  ? 255 ASP   B CA  1 
ATOM   4804 C  C   . ASP   B 1 270 ? 37.27   -14.338 -35.045 1 84.51  ? 255 ASP   B C   1 
ATOM   4805 O  O   . ASP   B 1 270 ? 37.536  -14.392 -33.839 1 84.59  ? 255 ASP   B O   1 
ATOM   4806 C  CB  . ASP   B 1 270 ? 36.045  -16.32  -36.062 1 87.06  ? 255 ASP   B CB  1 
ATOM   4807 N  N   . PRO   B 1 271 ? 36.886  -13.178 -35.629 1 83.46  ? 256 PRO   B N   1 
ATOM   4808 C  CA  . PRO   B 1 271 ? 36.736  -11.968 -34.8   1 82.55  ? 256 PRO   B CA  1 
ATOM   4809 C  C   . PRO   B 1 271 ? 35.469  -12.031 -33.944 1 81.45  ? 256 PRO   B C   1 
ATOM   4810 O  O   . PRO   B 1 271 ? 34.386  -12.355 -34.449 1 82.12  ? 256 PRO   B O   1 
ATOM   4811 C  CB  . PRO   B 1 271 ? 36.69   -10.831 -35.823 1 83.38  ? 256 PRO   B CB  1 
ATOM   4812 C  CG  . PRO   B 1 271 ? 36.161  -11.46  -37.065 1 84.08  ? 256 PRO   B CG  1 
ATOM   4813 C  CD  . PRO   B 1 271 ? 36.543  -12.922 -37.045 1 82.73  ? 256 PRO   B CD  1 
ATOM   4814 N  N   . LYS   B 1 272 ? 35.603  -11.755 -32.639 1 79.37  ? 257 LYS   B N   1 
ATOM   4815 C  CA  . LYS   B 1 272 ? 34.462  -11.821 -31.735 1 77.67  ? 257 LYS   B CA  1 
ATOM   4816 C  C   . LYS   B 1 272 ? 33.818  -10.452 -31.47  1 75.88  ? 257 LYS   B C   1 
ATOM   4817 O  O   . LYS   B 1 272 ? 34.518  -9.454  -31.282 1 75.84  ? 257 LYS   B O   1 
ATOM   4818 C  CB  . LYS   B 1 272 ? 34.856  -12.524 -30.438 1 79.31  ? 257 LYS   B CB  1 
ATOM   4819 N  N   . GLU   B 1 273 ? 32.476  -10.413 -31.473 1 74.22  ? 258 GLU   B N   1 
ATOM   4820 C  CA  . GLU   B 1 273 ? 31.673  -9.214  -31.241 1 72.9   ? 258 GLU   B CA  1 
ATOM   4821 C  C   . GLU   B 1 273 ? 31.272  -9.073  -29.777 1 71.37  ? 258 GLU   B C   1 
ATOM   4822 O  O   . GLU   B 1 273 ? 30.635  -9.971  -29.235 1 71.55  ? 258 GLU   B O   1 
ATOM   4823 C  CB  . GLU   B 1 273 ? 30.382  -9.288  -32.058 1 74.88  ? 258 GLU   B CB  1 
ATOM   4824 C  CG  . GLU   B 1 273 ? 30.55   -8.959  -33.523 1 80.32  ? 258 GLU   B CG  1 
ATOM   4825 C  CD  . GLU   B 1 273 ? 29.25   -8.516  -34.158 1 87.57  ? 258 GLU   B CD  1 
ATOM   4826 O  OE1 . GLU   B 1 273 ? 28.27   -9.292  -34.092 1 89.12  ? 258 GLU   B OE1 1 
ATOM   4827 O  OE2 . GLU   B 1 273 ? 29.2    -7.387  -34.699 1 90.18  ? 258 GLU   B OE2 1 
ATOM   4828 N  N   . PHE   B 1 274 ? 31.584  -7.929  -29.153 1 69.71  ? 259 PHE   B N   1 
ATOM   4829 C  CA  . PHE   B 1 274 ? 31.185  -7.66   -27.772 1 68.37  ? 259 PHE   B CA  1 
ATOM   4830 C  C   . PHE   B 1 274 ? 30.612  -6.268  -27.678 1 67.24  ? 259 PHE   B C   1 
ATOM   4831 O  O   . PHE   B 1 274 ? 31.119  -5.347  -28.313 1 67.78  ? 259 PHE   B O   1 
ATOM   4832 C  CB  . PHE   B 1 274 ? 32.361  -7.792  -26.8   1 67.9   ? 259 PHE   B CB  1 
ATOM   4833 C  CG  . PHE   B 1 274 ? 32.913  -9.188  -26.735 1 68.16  ? 259 PHE   B CG  1 
ATOM   4834 C  CD1 . PHE   B 1 274 ? 32.188  -10.21  -26.153 1 68.56  ? 259 PHE   B CD1 1 
ATOM   4835 C  CD2 . PHE   B 1 274 ? 34.138  -9.491  -27.302 1 68.73  ? 259 PHE   B CD2 1 
ATOM   4836 C  CE1 . PHE   B 1 274 ? 32.686  -11.503 -26.125 1 69.19  ? 259 PHE   B CE1 1 
ATOM   4837 C  CE2 . PHE   B 1 274 ? 34.627  -10.789 -27.285 1 69.08  ? 259 PHE   B CE2 1 
ATOM   4838 C  CZ  . PHE   B 1 274 ? 33.9    -11.786 -26.698 1 68.86  ? 259 PHE   B CZ  1 
ATOM   4839 N  N   . ALA   B 1 275 ? 29.573  -6.099  -26.866 1 65.41  ? 260 ALA   B N   1 
ATOM   4840 C  CA  . ALA   B 1 275 ? 28.942  -4.805  -26.671 1 63.86  ? 260 ALA   B CA  1 
ATOM   4841 C  C   . ALA   B 1 275 ? 29.811  -3.902  -25.788 1 62.45  ? 260 ALA   B C   1 
ATOM   4842 O  O   . ALA   B 1 275 ? 30.513  -4.374  -24.887 1 62.64  ? 260 ALA   B O   1 
ATOM   4843 C  CB  . ALA   B 1 275 ? 27.567  -4.987  -26.048 1 63.6   ? 260 ALA   B CB  1 
ATOM   4844 N  N   . GLY   B 1 276 ? 29.752  -2.605  -26.055 1 60.79  ? 261 GLY   B N   1 
ATOM   4845 C  CA  . GLY   B 1 276 ? 30.506  -1.637  -25.283 1 59.52  ? 261 GLY   B CA  1 
ATOM   4846 C  C   . GLY   B 1 276 ? 29.94   -1.426  -23.898 1 58.22  ? 261 GLY   B C   1 
ATOM   4847 O  O   . GLY   B 1 276 ? 28.807  -1.821  -23.611 1 58.23  ? 261 GLY   B O   1 
ATOM   4848 N  N   . GLY   B 1 277 ? 30.729  -0.776  -23.045 1 57.09  ? 262 GLY   B N   1 
ATOM   4849 C  CA  . GLY   B 1 277 ? 30.376  -0.455  -21.667 1 56.17  ? 262 GLY   B CA  1 
ATOM   4850 C  C   . GLY   B 1 277 ? 29.061  0.273   -21.576 1 55.1   ? 262 GLY   B C   1 
ATOM   4851 O  O   . GLY   B 1 277 ? 28.811  1.222   -22.334 1 55.3   ? 262 GLY   B O   1 
ATOM   4852 N  N   . SER   B 1 278 ? 28.177  -0.232  -20.725 1 53.7   ? 263 SER   B N   1 
ATOM   4853 C  CA  . SER   B 1 278 ? 26.852  0.343   -20.602 1 52.94  ? 263 SER   B CA  1 
ATOM   4854 C  C   . SER   B 1 278 ? 26.364  0.398   -19.172 1 52.8   ? 263 SER   B C   1 
ATOM   4855 O  O   . SER   B 1 278 ? 26.58   -0.547  -18.411 1 53.39  ? 263 SER   B O   1 
ATOM   4856 C  CB  . SER   B 1 278 ? 25.864  -0.465  -21.44  1 53.32  ? 263 SER   B CB  1 
ATOM   4857 O  OG  . SER   B 1 278 ? 24.557  0.076   -21.371 1 54.26  ? 263 SER   B OG  1 
ATOM   4858 N  N   . ALA   B 1 279 ? 25.612  1.452   -18.831 1 51.74  ? 264 ALA   B N   1 
ATOM   4859 C  CA  . ALA   B 1 279 ? 24.951  1.508   -17.533 1 51.42  ? 264 ALA   B CA  1 
ATOM   4860 C  C   . ALA   B 1 279 ? 23.819  0.429   -17.44  1 51.64  ? 264 ALA   B C   1 
ATOM   4861 O  O   . ALA   B 1 279 ? 23.399  0.09    -16.341 1 51.92  ? 264 ALA   B O   1 
ATOM   4862 C  CB  . ALA   B 1 279 ? 24.421  2.898   -17.256 1 51.15  ? 264 ALA   B CB  1 
ATOM   4863 N  N   . GLY   B 1 280 ? 23.411  -0.155  -18.572 1 51.35  ? 265 GLY   B N   1 
ATOM   4864 C  CA  . GLY   B 1 280 ? 22.505  -1.293  -18.619 1 51.79  ? 265 GLY   B CA  1 
ATOM   4865 C  C   . GLY   B 1 280 ? 23.127  -2.542  -18.005 1 52.27  ? 265 GLY   B C   1 
ATOM   4866 O  O   . GLY   B 1 280 ? 22.43   -3.544  -17.813 1 53.14  ? 265 GLY   B O   1 
ATOM   4867 N  N   . GLN   B 1 281 ? 24.448  -2.493  -17.686 1 51.76  ? 266 GLN   B N   1 
ATOM   4868 C  CA  . GLN   B 1 281 ? 25.222  -3.536  -16.993 1 52.09  ? 266 GLN   B CA  1 
ATOM   4869 C  C   . GLN   B 1 281 ? 25.277  -3.289  -15.46  1 52.71  ? 266 GLN   B C   1 
ATOM   4870 O  O   . GLN   B 1 281 ? 25.96   -4.042  -14.761 1 52.21  ? 266 GLN   B O   1 
ATOM   4871 C  CB  . GLN   B 1 281 ? 26.666  -3.604  -17.527 1 52.16  ? 266 GLN   B CB  1 
ATOM   4872 C  CG  . GLN   B 1 281 ? 26.77   -3.977  -18.985 1 54.09  ? 266 GLN   B CG  1 
ATOM   4873 C  CD  . GLN   B 1 281 ? 28.107  -3.615  -19.602 1 59     ? 266 GLN   B CD  1 
ATOM   4874 O  OE1 . GLN   B 1 281 ? 28.963  -2.944  -19     1 60.03  ? 266 GLN   B OE1 1 
ATOM   4875 N  NE2 . GLN   B 1 281 ? 28.302  -4.012  -20.858 1 59.78  ? 266 GLN   B NE2 1 
ATOM   4876 N  N   . SER   B 1 282 ? 24.614  -2.218  -14.958 1 53.37  ? 267 SER   B N   1 
ATOM   4877 C  CA  . SER   B 1 282 ? 24.54   -1.878  -13.54  1 54.81  ? 267 SER   B CA  1 
ATOM   4878 C  C   . SER   B 1 282 ? 23.602  -2.883  -12.866 1 56.24  ? 267 SER   B C   1 
ATOM   4879 O  O   . SER   B 1 282 ? 22.46   -3.066  -13.301 1 56.67  ? 267 SER   B O   1 
ATOM   4880 C  CB  . SER   B 1 282 ? 24.008  -0.454  -13.349 1 55.99  ? 267 SER   B CB  1 
ATOM   4881 O  OG  . SER   B 1 282 ? 23.533  -0.207  -12.032 1 58.49  ? 267 SER   B OG  1 
ATOM   4882 N  N   . SER   B 1 283 ? 24.088  -3.536  -11.812 1 56.61  ? 268 SER   B N   1 
ATOM   4883 C  CA  . SER   B 1 283 ? 23.3    -4.523  -11.095 1 57.16  ? 268 SER   B CA  1 
ATOM   4884 C  C   . SER   B 1 283 ? 22.294  -3.884  -10.155 1 58.44  ? 268 SER   B C   1 
ATOM   4885 O  O   . SER   B 1 283 ? 21.284  -4.521  -9.869  1 58.97  ? 268 SER   B O   1 
ATOM   4886 C  CB  . SER   B 1 283 ? 24.203  -5.454  -10.304 1 57.68  ? 268 SER   B CB  1 
ATOM   4887 O  OG  . SER   B 1 283 ? 25.07   -6.172  -11.162 1 59.55  ? 268 SER   B OG  1 
ATOM   4888 N  N   . VAL   B 1 284 ? 22.562  -2.651  -9.648  1 58.87  ? 269 VAL   B N   1 
ATOM   4889 C  CA  . VAL   B 1 284 ? 21.648  -2.02   -8.695  1 59.62  ? 269 VAL   B CA  1 
ATOM   4890 C  C   . VAL   B 1 284 ? 20.316  -1.704  -9.313  1 59.44  ? 269 VAL   B C   1 
ATOM   4891 O  O   . VAL   B 1 284 ? 19.291  -1.994  -8.691  1 59.94  ? 269 VAL   B O   1 
ATOM   4892 C  CB  . VAL   B 1 284 ? 22.156  -0.8    -7.886  1 61.04  ? 269 VAL   B CB  1 
ATOM   4893 C  CG1 . VAL   B 1 284 ? 23.091  -1.182  -6.772  1 61.63  ? 269 VAL   B CG1 1 
ATOM   4894 C  CG2 . VAL   B 1 284 ? 22.674  0.346   -8.75   1 61.81  ? 269 VAL   B CG2 1 
ATOM   4895 N  N   . PHE   B 1 285 ? 20.308  -1.154  -10.524 1 58.62  ? 270 PHE   B N   1 
ATOM   4896 C  CA  . PHE   B 1 285 ? 19.043  -0.818  -11.164 1 58.52  ? 270 PHE   B CA  1 
ATOM   4897 C  C   . PHE   B 1 285 ? 18.292  -2.057  -11.621 1 57.12  ? 270 PHE   B C   1 
ATOM   4898 O  O   . PHE   B 1 285 ? 17.059  -2.103  -11.514 1 56.72  ? 270 PHE   B O   1 
ATOM   4899 C  CB  . PHE   B 1 285 ? 19.237  0.205   -12.274 1 59.32  ? 270 PHE   B CB  1 
ATOM   4900 C  CG  . PHE   B 1 285 ? 19.577  1.555   -11.685 1 61.04  ? 270 PHE   B CG  1 
ATOM   4901 C  CD1 . PHE   B 1 285 ? 20.899  1.929   -11.476 1 62.03  ? 270 PHE   B CD1 1 
ATOM   4902 C  CD2 . PHE   B 1 285 ? 18.574  2.437   -11.307 1 62.11  ? 270 PHE   B CD2 1 
ATOM   4903 C  CE1 . PHE   B 1 285 ? 21.211  3.164   -10.915 1 62.91  ? 270 PHE   B CE1 1 
ATOM   4904 C  CE2 . PHE   B 1 285 ? 18.89   3.674   -10.748 1 62.93  ? 270 PHE   B CE2 1 
ATOM   4905 C  CZ  . PHE   B 1 285 ? 20.205  4.029   -10.556 1 62.72  ? 270 PHE   B CZ  1 
ATOM   4906 N  N   . GLN   B 1 286 ? 19.032  -3.082  -12.074 1 55.89  ? 271 GLN   B N   1 
ATOM   4907 C  CA  . GLN   B 1 286 ? 18.397  -4.32   -12.489 1 55.43  ? 271 GLN   B CA  1 
ATOM   4908 C  C   . GLN   B 1 286 ? 17.781  -5.044  -11.287 1 56.02  ? 271 GLN   B C   1 
ATOM   4909 O  O   . GLN   B 1 286 ? 16.684  -5.576  -11.394 1 55.46  ? 271 GLN   B O   1 
ATOM   4910 C  CB  . GLN   B 1 286 ? 19.369  -5.215  -13.269 1 54.74  ? 271 GLN   B CB  1 
ATOM   4911 C  CG  . GLN   B 1 286 ? 19.648  -4.688  -14.662 1 54.94  ? 271 GLN   B CG  1 
ATOM   4912 C  CD  . GLN   B 1 286 ? 19.802  -5.787  -15.686 1 56.11  ? 271 GLN   B CD  1 
ATOM   4913 O  OE1 . GLN   B 1 286 ? 19.2    -6.836  -15.569 1 56.1   ? 271 GLN   B OE1 1 
ATOM   4914 N  NE2 . GLN   B 1 286 ? 20.607  -5.569  -16.729 1 56.08  ? 271 GLN   B NE2 1 
ATOM   4915 N  N   . CYS   B 1 287 ? 18.445  -4.981  -10.131 1 56.85  ? 272 CYS   B N   1 
ATOM   4916 C  CA  . CYS   B 1 287 ? 17.964  -5.656  -8.943  1 58.28  ? 272 CYS   B CA  1 
ATOM   4917 C  C   . CYS   B 1 287 ? 16.704  -5.007  -8.356  1 58.2   ? 272 CYS   B C   1 
ATOM   4918 O  O   . CYS   B 1 287 ? 15.896  -5.73   -7.797  1 58.65  ? 272 CYS   B O   1 
ATOM   4919 C  CB  . CYS   B 1 287 ? 19.082  -5.844  -7.91   1 60.63  ? 272 CYS   B CB  1 
ATOM   4920 S  SG  . CYS   B 1 287 ? 19.164  -4.582  -6.615  1 67.53  ? 272 CYS   B SG  1 
ATOM   4921 N  N   . PHE   B 1 288 ? 16.506  -3.688  -8.519  1 57.77  ? 273 PHE   B N   1 
ATOM   4922 C  CA  . PHE   B 1 288 ? 15.288  -3.052  -8.02   1 57.66  ? 273 PHE   B CA  1 
ATOM   4923 C  C   . PHE   B 1 288 ? 14.113  -3.312  -8.954  1 56.24  ? 273 PHE   B C   1 
ATOM   4924 O  O   . PHE   B 1 288 ? 12.999  -3.473  -8.475  1 56.02  ? 273 PHE   B O   1 
ATOM   4925 C  CB  . PHE   B 1 288 ? 15.489  -1.571  -7.655  1 58.95  ? 273 PHE   B CB  1 
ATOM   4926 C  CG  . PHE   B 1 288 ? 16.167  -1.536  -6.298  1 61.12  ? 273 PHE   B CG  1 
ATOM   4927 C  CD1 . PHE   B 1 288 ? 15.622  -2.215  -5.217  1 62.68  ? 273 PHE   B CD1 1 
ATOM   4928 C  CD2 . PHE   B 1 288 ? 17.414  -0.953  -6.14   1 62.36  ? 273 PHE   B CD2 1 
ATOM   4929 C  CE1 . PHE   B 1 288 ? 16.297  -2.285  -4.001  1 63.9   ? 273 PHE   B CE1 1 
ATOM   4930 C  CE2 . PHE   B 1 288 ? 18.091  -1.034  -4.922  1 63.45  ? 273 PHE   B CE2 1 
ATOM   4931 C  CZ  . PHE   B 1 288 ? 17.534  -1.71   -3.868  1 63.63  ? 273 PHE   B CZ  1 
ATOM   4932 N  N   . ASP   B 1 289 ? 14.36   -3.489  -10.254 1 55.7   ? 274 ASP   B N   1 
ATOM   4933 C  CA  . ASP   B 1 289 ? 13.317  -3.888  -11.192 1 55.53  ? 274 ASP   B CA  1 
ATOM   4934 C  C   . ASP   B 1 289 ? 12.9    -5.337  -10.895 1 54.8   ? 274 ASP   B C   1 
ATOM   4935 O  O   . ASP   B 1 289 ? 11.724  -5.655  -10.981 1 54.58  ? 274 ASP   B O   1 
ATOM   4936 C  CB  . ASP   B 1 289 ? 13.818  -3.79   -12.628 1 57.78  ? 274 ASP   B CB  1 
ATOM   4937 C  CG  . ASP   B 1 289 ? 14.001  -2.368  -13.104 1 65.11  ? 274 ASP   B CG  1 
ATOM   4938 O  OD1 . ASP   B 1 289 ? 13.203  -1.499  -12.695 1 66.42  ? 274 ASP   B OD1 1 
ATOM   4939 O  OD2 . ASP   B 1 289 ? 14.934  -2.124  -13.905 1 68.75  ? 274 ASP   B OD2 1 
ATOM   4940 N  N   . VAL   B 1 290 ? 13.86   -6.214  -10.545 1 54.42  ? 275 VAL   B N   1 
ATOM   4941 C  CA  . VAL   B 1 290 ? 13.559  -7.605  -10.207 1 54.52  ? 275 VAL   B CA  1 
ATOM   4942 C  C   . VAL   B 1 290 ? 12.764  -7.623  -8.9    1 55.79  ? 275 VAL   B C   1 
ATOM   4943 O  O   . VAL   B 1 290 ? 11.696  -8.237  -8.831  1 56.54  ? 275 VAL   B O   1 
ATOM   4944 C  CB  . VAL   B 1 290 ? 14.818  -8.498  -10.13  1 54.53  ? 275 VAL   B CB  1 
ATOM   4945 C  CG1 . VAL   B 1 290 ? 14.481  -9.865  -9.553  1 55.28  ? 275 VAL   B CG1 1 
ATOM   4946 C  CG2 . VAL   B 1 290 ? 15.467  -8.659  -11.501 1 54.62  ? 275 VAL   B CG2 1 
ATOM   4947 N  N   . LEU   B 1 291 ? 13.244  -6.89   -7.891  1 55.76  ? 276 LEU   B N   1 
ATOM   4948 C  CA  . LEU   B 1 291 ? 12.592  -6.779  -6.595  1 55.95  ? 276 LEU   B CA  1 
ATOM   4949 C  C   . LEU   B 1 291 ? 11.15   -6.305  -6.697  1 56.7   ? 276 LEU   B C   1 
ATOM   4950 O  O   . LEU   B 1 291 ? 10.27   -6.913  -6.102  1 56.95  ? 276 LEU   B O   1 
ATOM   4951 C  CB  . LEU   B 1 291 ? 13.374  -5.833  -5.68   1 55.78  ? 276 LEU   B CB  1 
ATOM   4952 C  CG  . LEU   B 1 291 ? 12.833  -5.718  -4.265  1 57.28  ? 276 LEU   B CG  1 
ATOM   4953 C  CD1 . LEU   B 1 291 ? 12.966  -7.035  -3.52   1 57.43  ? 276 LEU   B CD1 1 
ATOM   4954 C  CD2 . LEU   B 1 291 ? 13.549  -4.642  -3.516  1 58.18  ? 276 LEU   B CD2 1 
ATOM   4955 N  N   . LEU   B 1 292 ? 10.899  -5.253  -7.476  1 56.83  ? 277 LEU   B N   1 
ATOM   4956 C  CA  . LEU   B 1 292 ? 9.558   -4.704  -7.583  1 57.24  ? 277 LEU   B CA  1 
ATOM   4957 C  C   . LEU   B 1 292 ? 8.673   -5.368  -8.655  1 57.98  ? 277 LEU   B C   1 
ATOM   4958 O  O   . LEU   B 1 292 ? 7.556   -4.912  -8.885  1 58.3   ? 277 LEU   B O   1 
ATOM   4959 C  CB  . LEU   B 1 292 ? 9.641   -3.189  -7.777  1 57.41  ? 277 LEU   B CB  1 
ATOM   4960 C  CG  . LEU   B 1 292 ? 10.434  -2.461  -6.684  1 58.85  ? 277 LEU   B CG  1 
ATOM   4961 C  CD1 . LEU   B 1 292 ? 10.724  -1.02   -7.068  1 59.49  ? 277 LEU   B CD1 1 
ATOM   4962 C  CD2 . LEU   B 1 292 ? 9.768   -2.602  -5.316  1 59.31  ? 277 LEU   B CD2 1 
ATOM   4963 N  N   . GLY   B 1 293 ? 9.147   -6.441  -9.276  1 58.2   ? 278 GLY   B N   1 
ATOM   4964 C  CA  . GLY   B 1 293 ? 8.371   -7.156  -10.28  1 59.35  ? 278 GLY   B CA  1 
ATOM   4965 C  C   . GLY   B 1 293 ? 8.181   -6.427  -11.592 1 60.86  ? 278 GLY   B C   1 
ATOM   4966 O  O   . GLY   B 1 293 ? 7.25    -6.728  -12.337 1 61.18  ? 278 GLY   B O   1 
ATOM   4967 N  N   . ILE   B 1 294 ? 9.024   -5.436  -11.868 1 61.76  ? 279 ILE   B N   1 
ATOM   4968 C  CA  . ILE   B 1 294 ? 8.973   -4.683  -13.114 1 63.41  ? 279 ILE   B CA  1 
ATOM   4969 C  C   . ILE   B 1 294 ? 9.688   -5.571  -14.116 1 66.42  ? 279 ILE   B C   1 
ATOM   4970 O  O   . ILE   B 1 294 ? 10.915  -5.75   -14.028 1 67.36  ? 279 ILE   B O   1 
ATOM   4971 C  CB  . ILE   B 1 294 ? 9.693   -3.331  -12.926 1 63.15  ? 279 ILE   B CB  1 
ATOM   4972 C  CG1 . ILE   B 1 294 ? 9.069   -2.543  -11.758 1 63.2   ? 279 ILE   B CG1 1 
ATOM   4973 C  CG2 . ILE   B 1 294 ? 9.692   -2.523  -14.219 1 63.38  ? 279 ILE   B CG2 1 
ATOM   4974 C  CD1 . ILE   B 1 294 ? 9.941   -1.601  -11.178 1 63.91  ? 279 ILE   B CD1 1 
ATOM   4975 N  N   . GLN   B 1 295 ? 8.923   -6.216  -14.999 1 67.51  ? 280 GLN   B N   1 
ATOM   4976 C  CA  . GLN   B 1 295 ? 9.499   -7.171  -15.939 1 69.08  ? 280 GLN   B CA  1 
ATOM   4977 C  C   . GLN   B 1 295 ? 10.234  -6.5    -17.087 1 70.23  ? 280 GLN   B C   1 
ATOM   4978 O  O   . GLN   B 1 295 ? 9.786   -6.545  -18.237 1 70.57  ? 280 GLN   B O   1 
ATOM   4979 C  CB  . GLN   B 1 295 ? 8.418   -8.131  -16.448 1 71.13  ? 280 GLN   B CB  1 
ATOM   4980 C  CG  . GLN   B 1 295 ? 8.041   -9.212  -15.442 1 74.3   ? 280 GLN   B CG  1 
ATOM   4981 C  CD  . GLN   B 1 295 ? 6.63    -9.708  -15.665 1 78.64  ? 280 GLN   B CD  1 
ATOM   4982 O  OE1 . GLN   B 1 295 ? 5.726   -9.448  -14.864 1 79.93  ? 280 GLN   B OE1 1 
ATOM   4983 N  NE2 . GLN   B 1 295 ? 6.402   -10.421 -16.769 1 79.34  ? 280 GLN   B NE2 1 
ATOM   4984 N  N   . GLN   B 1 296 ? 11.384  -5.898  -16.774 1 70.77  ? 281 GLN   B N   1 
ATOM   4985 C  CA  . GLN   B 1 296 ? 12.202  -5.189  -17.748 1 71.82  ? 281 GLN   B CA  1 
ATOM   4986 C  C   . GLN   B 1 296 ? 12.772  -6.097  -18.789 1 73.13  ? 281 GLN   B C   1 
ATOM   4987 O  O   . GLN   B 1 296 ? 12.876  -5.692  -19.94  1 73.54  ? 281 GLN   B O   1 
ATOM   4988 C  CB  . GLN   B 1 296 ? 13.337  -4.423  -17.067 1 72.4   ? 281 GLN   B CB  1 
ATOM   4989 C  CG  . GLN   B 1 296 ? 12.846  -3.283  -16.207 1 73.72  ? 281 GLN   B CG  1 
ATOM   4990 C  CD  . GLN   B 1 296 ? 12.438  -2.062  -16.98  1 75.65  ? 281 GLN   B CD  1 
ATOM   4991 O  OE1 . GLN   B 1 296 ? 12.339  -2.055  -18.217 1 76.79  ? 281 GLN   B OE1 1 
ATOM   4992 N  NE2 . GLN   B 1 296 ? 12.179  -1      -16.25  1 75.84  ? 281 GLN   B NE2 1 
ATOM   4993 N  N   . THR   B 1 297 ? 13.158  -7.313  -18.382 1 73.67  ? 282 THR   B N   1 
ATOM   4994 C  CA  . THR   B 1 297 ? 13.75   -8.324  -19.251 1 74.52  ? 282 THR   B CA  1 
ATOM   4995 C  C   . THR   B 1 297 ? 12.697  -9.209  -19.969 1 75     ? 282 THR   B C   1 
ATOM   4996 O  O   . THR   B 1 297 ? 13.073  -10.041 -20.794 1 75.11  ? 282 THR   B O   1 
ATOM   4997 C  CB  . THR   B 1 297 ? 14.783  -9.144  -18.454 1 75.86  ? 282 THR   B CB  1 
ATOM   4998 O  OG1 . THR   B 1 297 ? 14.195  -9.598  -17.225 1 76.84  ? 282 THR   B OG1 1 
ATOM   4999 C  CG2 . THR   B 1 297 ? 16.05   -8.344  -18.144 1 76.09  ? 282 THR   B CG2 1 
ATOM   5000 N  N   . ALA   B 1 298 ? 11.395  -8.995  -19.709 1 75.18  ? 283 ALA   B N   1 
ATOM   5001 C  CA  . ALA   B 1 298 ? 10.319  -9.765  -20.332 1 76.01  ? 283 ALA   B CA  1 
ATOM   5002 C  C   . ALA   B 1 298 ? 9.625   -9.001  -21.467 1 76.53  ? 283 ALA   B C   1 
ATOM   5003 O  O   . ALA   B 1 298 ? 9.608   -7.771  -21.466 1 76.98  ? 283 ALA   B O   1 
ATOM   5004 C  CB  . ALA   B 1 298 ? 9.293   -10.15  -19.276 1 76.44  ? 283 ALA   B CB  1 
ATOM   5005 N  N   . GLY   B 1 299 ? 9.027   -9.727  -22.404 1 76.36  ? 284 GLY   B N   1 
ATOM   5006 C  CA  . GLY   B 1 299 ? 8.292   -9.103  -23.5   1 76.96  ? 284 GLY   B CA  1 
ATOM   5007 C  C   . GLY   B 1 299 ? 8.843   -9.345  -24.893 1 77.42  ? 284 GLY   B C   1 
ATOM   5008 O  O   . GLY   B 1 299 ? 8.151   -9.089  -25.887 1 77.85  ? 284 GLY   B O   1 
ATOM   5009 N  N   . GLY   B 1 300 ? 10.097  -9.791  -24.976 1 76.8   ? 285 GLY   B N   1 
ATOM   5010 C  CA  . GLY   B 1 300 ? 10.734  -10.077 -26.26  1 76.71  ? 285 GLY   B CA  1 
ATOM   5011 C  C   . GLY   B 1 300 ? 11.17   -8.877  -27.087 1 76.05  ? 285 GLY   B C   1 
ATOM   5012 O  O   . GLY   B 1 300 ? 11.732  -9.039  -28.176 1 76.26  ? 285 GLY   B O   1 
ATOM   5013 N  N   . GLY   B 1 301 ? 10.924  -7.673  -26.57  1 74.75  ? 286 GLY   B N   1 
ATOM   5014 C  CA  . GLY   B 1 301 ? 11.315  -6.429  -27.222 1 73.71  ? 286 GLY   B CA  1 
ATOM   5015 C  C   . GLY   B 1 301 ? 12.802  -6.147  -27.134 1 72.24  ? 286 GLY   B C   1 
ATOM   5016 O  O   . GLY   B 1 301 ? 13.515  -6.793  -26.362 1 72.37  ? 286 GLY   B O   1 
ATOM   5017 N  N   . HIS   B 1 302 ? 13.282  -5.173  -27.922 1 70.66  ? 287 HIS   B N   1 
ATOM   5018 C  CA  . HIS   B 1 302 ? 14.702  -4.825  -27.961 1 69.35  ? 287 HIS   B CA  1 
ATOM   5019 C  C   . HIS   B 1 302 ? 15.274  -4.372  -26.603 1 67.33  ? 287 HIS   B C   1 
ATOM   5020 O  O   . HIS   B 1 302 ? 16.379  -4.783  -26.242 1 67.37  ? 287 HIS   B O   1 
ATOM   5021 C  CB  . HIS   B 1 302 ? 14.978  -3.789  -29.058 1 70.19  ? 287 HIS   B CB  1 
ATOM   5022 N  N   . ALA   B 1 303 ? 14.522  -3.561  -25.849 1 65.44  ? 288 ALA   B N   1 
ATOM   5023 C  CA  . ALA   B 1 303 ? 14.962  -3.073  -24.539 1 64.07  ? 288 ALA   B CA  1 
ATOM   5024 C  C   . ALA   B 1 303 ? 15.14   -4.224  -23.556 1 62.93  ? 288 ALA   B C   1 
ATOM   5025 O  O   . ALA   B 1 303 ? 16.129  -4.262  -22.825 1 63.24  ? 288 ALA   B O   1 
ATOM   5026 C  CB  . ALA   B 1 303 ? 13.961  -2.067  -23.996 1 63.78  ? 288 ALA   B CB  1 
ATOM   5027 N  N   . ALA   B 1 304 ? 14.211  -5.19   -23.585 1 61.72  ? 289 ALA   B N   1 
ATOM   5028 C  CA  . ALA   B 1 304 ? 14.242  -6.378  -22.737 1 60.82  ? 289 ALA   B CA  1 
ATOM   5029 C  C   . ALA   B 1 304 ? 15.422  -7.275  -23.097 1 59.69  ? 289 ALA   B C   1 
ATOM   5030 O  O   . ALA   B 1 304 ? 16.085  -7.814  -22.207 1 59.98  ? 289 ALA   B O   1 
ATOM   5031 C  CB  . ALA   B 1 304 ? 12.934  -7.146  -22.886 1 60.76  ? 289 ALA   B CB  1 
ATOM   5032 N  N   . GLN   B 1 305 ? 15.686  -7.421  -24.404 1 58.52  ? 290 GLN   B N   1 
ATOM   5033 C  CA  . GLN   B 1 305 ? 16.764  -8.242  -24.925 1 58.22  ? 290 GLN   B CA  1 
ATOM   5034 C  C   . GLN   B 1 305 ? 18.095  -7.657  -24.494 1 57.52  ? 290 GLN   B C   1 
ATOM   5035 O  O   . GLN   B 1 305 ? 18.942  -8.385  -23.981 1 57.79  ? 290 GLN   B O   1 
ATOM   5036 C  CB  . GLN   B 1 305 ? 16.678  -8.312  -26.462 1 59.76  ? 290 GLN   B CB  1 
ATOM   5037 C  CG  . GLN   B 1 305 ? 17.777  -9.154  -27.104 1 63.09  ? 290 GLN   B CG  1 
ATOM   5038 C  CD  . GLN   B 1 305 ? 17.54   -10.603 -26.824 1 66.21  ? 290 GLN   B CD  1 
ATOM   5039 O  OE1 . GLN   B 1 305 ? 16.44   -11.104 -27.041 1 67.64  ? 290 GLN   B OE1 1 
ATOM   5040 N  NE2 . GLN   B 1 305 ? 18.559  -11.305 -26.337 1 66.37  ? 290 GLN   B NE2 1 
ATOM   5041 N  N   . PHE   B 1 306 ? 18.258  -6.332  -24.658 1 56.53  ? 291 PHE   B N   1 
ATOM   5042 C  CA  . PHE   B 1 306 ? 19.482  -5.632  -24.3   1 55.7   ? 291 PHE   B CA  1 
ATOM   5043 C  C   . PHE   B 1 306 ? 19.833  -5.783  -22.818 1 55.59  ? 291 PHE   B C   1 
ATOM   5044 O  O   . PHE   B 1 306 ? 20.974  -6.102  -22.494 1 56.16  ? 291 PHE   B O   1 
ATOM   5045 C  CB  . PHE   B 1 306 ? 19.388  -4.158  -24.706 1 54.82  ? 291 PHE   B CB  1 
ATOM   5046 C  CG  . PHE   B 1 306 ? 20.6    -3.359  -24.301 1 54.87  ? 291 PHE   B CG  1 
ATOM   5047 C  CD1 . PHE   B 1 306 ? 21.822  -3.565  -24.917 1 55.21  ? 291 PHE   B CD1 1 
ATOM   5048 C  CD2 . PHE   B 1 306 ? 20.527  -2.426  -23.28  1 54.87  ? 291 PHE   B CD2 1 
ATOM   5049 C  CE1 . PHE   B 1 306 ? 22.936  -2.837  -24.534 1 55.12  ? 291 PHE   B CE1 1 
ATOM   5050 C  CE2 . PHE   B 1 306 ? 21.644  -1.707  -22.902 1 54.93  ? 291 PHE   B CE2 1 
ATOM   5051 C  CZ  . PHE   B 1 306 ? 22.839  -1.918  -23.53  1 54.51  ? 291 PHE   B CZ  1 
ATOM   5052 N  N   . LEU   B 1 307 ? 18.862  -5.573  -21.932 1 54.61  ? 292 LEU   B N   1 
ATOM   5053 C  CA  . LEU   B 1 307 ? 19.098  -5.665  -20.5   1 54.19  ? 292 LEU   B CA  1 
ATOM   5054 C  C   . LEU   B 1 307 ? 19.412  -7.074  -20.044 1 54.77  ? 292 LEU   B C   1 
ATOM   5055 O  O   . LEU   B 1 307 ? 20.175  -7.249  -19.093 1 55.02  ? 292 LEU   B O   1 
ATOM   5056 C  CB  . LEU   B 1 307 ? 17.922  -5.066  -19.719 1 53.63  ? 292 LEU   B CB  1 
ATOM   5057 C  CG  . LEU   B 1 307 ? 17.736  -3.56   -19.903 1 54.05  ? 292 LEU   B CG  1 
ATOM   5058 C  CD1 . LEU   B 1 307 ? 16.449  -3.074  -19.252 1 54.2   ? 292 LEU   B CD1 1 
ATOM   5059 C  CD2 . LEU   B 1 307 ? 18.939  -2.789  -19.382 1 54.41  ? 292 LEU   B CD2 1 
ATOM   5060 N  N   . GLN   B 1 308 ? 18.844  -8.085  -20.717 1 55.02  ? 293 GLN   B N   1 
ATOM   5061 C  CA  . GLN   B 1 308 ? 19.137  -9.476  -20.369 1 55.34  ? 293 GLN   B CA  1 
ATOM   5062 C  C   . GLN   B 1 308 ? 20.555  -9.797  -20.836 1 55.61  ? 293 GLN   B C   1 
ATOM   5063 O  O   . GLN   B 1 308 ? 21.339  -10.366 -20.075 1 55.93  ? 293 GLN   B O   1 
ATOM   5064 C  CB  . GLN   B 1 308 ? 18.112  -10.443 -20.995 1 56.45  ? 293 GLN   B CB  1 
ATOM   5065 N  N   . ASP   B 1 309 ? 20.913  -9.378  -22.066 1 55.46  ? 294 ASP   B N   1 
ATOM   5066 C  CA  . ASP   B 1 309 ? 22.261  -9.604  -22.604 1 55.73  ? 294 ASP   B CA  1 
ATOM   5067 C  C   . ASP   B 1 309 ? 23.323  -8.959  -21.719 1 54.75  ? 294 ASP   B C   1 
ATOM   5068 O  O   . ASP   B 1 309 ? 24.38   -9.547  -21.506 1 54.73  ? 294 ASP   B O   1 
ATOM   5069 C  CB  . ASP   B 1 309 ? 22.388  -9.066  -24.042 1 58.55  ? 294 ASP   B CB  1 
ATOM   5070 C  CG  . ASP   B 1 309 ? 21.556  -9.799  -25.102 1 65.11  ? 294 ASP   B CG  1 
ATOM   5071 O  OD1 . ASP   B 1 309 ? 20.891  -10.809 -24.755 1 65.89  ? 294 ASP   B OD1 1 
ATOM   5072 O  OD2 . ASP   B 1 309 ? 21.562  -9.353  -26.277 1 67.78  ? 294 ASP   B OD2 1 
ATOM   5073 N  N   . MET   B 1 310 ? 23.023  -7.765  -21.168 1 53.75  ? 295 MET   B N   1 
ATOM   5074 C  CA  . MET   B 1 310 ? 23.961  -7.039  -20.32  1 53.11  ? 295 MET   B CA  1 
ATOM   5075 C  C   . MET   B 1 310 ? 24.27   -7.718  -19.001 1 52.3   ? 295 MET   B C   1 
ATOM   5076 O  O   . MET   B 1 310 ? 25.274  -7.374  -18.384 1 52.36  ? 295 MET   B O   1 
ATOM   5077 C  CB  . MET   B 1 310 ? 23.518  -5.593  -20.106 1 53.73  ? 295 MET   B CB  1 
ATOM   5078 C  CG  . MET   B 1 310 ? 23.574  -4.766  -21.373 1 55.99  ? 295 MET   B CG  1 
ATOM   5079 S  SD  . MET   B 1 310 ? 25.191  -4.736  -22.193 1 59.94  ? 295 MET   B SD  1 
ATOM   5080 C  CE  . MET   B 1 310 ? 24.897  -5.853  -23.575 1 53.15  ? 295 MET   B CE  1 
ATOM   5081 N  N   . ARG   B 1 311 ? 23.473  -8.717  -18.594 1 51.64  ? 296 ARG   B N   1 
ATOM   5082 C  CA  . ARG   B 1 311 ? 23.773  -9.476  -17.379 1 51.55  ? 296 ARG   B CA  1 
ATOM   5083 C  C   . ARG   B 1 311 ? 25.022  -10.333 -17.545 1 51.58  ? 296 ARG   B C   1 
ATOM   5084 O  O   . ARG   B 1 311 ? 25.734  -10.564 -16.563 1 51.34  ? 296 ARG   B O   1 
ATOM   5085 C  CB  . ARG   B 1 311 ? 22.603  -10.348 -16.973 1 51.83  ? 296 ARG   B CB  1 
ATOM   5086 C  CG  . ARG   B 1 311 ? 21.408  -9.535  -16.605 1 53.2   ? 296 ARG   B CG  1 
ATOM   5087 C  CD  . ARG   B 1 311 ? 20.441  -10.395 -15.848 1 55.97  ? 296 ARG   B CD  1 
ATOM   5088 N  NE  . ARG   B 1 311 ? 19.239  -9.643  -15.504 1 58.15  ? 296 ARG   B NE  1 
ATOM   5089 C  CZ  . ARG   B 1 311 ? 18.202  -10.142 -14.851 1 58.31  ? 296 ARG   B CZ  1 
ATOM   5090 N  NH1 . ARG   B 1 311 ? 18.204  -11.411 -14.458 1 56.37  ? 296 ARG   B NH1 1 
ATOM   5091 N  NH2 . ARG   B 1 311 ? 17.151  -9.376  -14.584 1 58.84  ? 296 ARG   B NH2 1 
ATOM   5092 N  N   . ARG   B 1 312 ? 25.305  -10.786 -18.787 1 51.46  ? 297 ARG   B N   1 
ATOM   5093 C  CA  . ARG   B 1 312 ? 26.511  -11.557 -19.073 1 52.22  ? 297 ARG   B CA  1 
ATOM   5094 C  C   . ARG   B 1 312 ? 27.796  -10.704 -18.93  1 52.66  ? 297 ARG   B C   1 
ATOM   5095 O  O   . ARG   B 1 312 ? 28.887  -11.252 -18.801 1 53.52  ? 297 ARG   B O   1 
ATOM   5096 C  CB  . ARG   B 1 312 ? 26.413  -12.175 -20.476 1 53.96  ? 297 ARG   B CB  1 
ATOM   5097 N  N   . TYR   B 1 313 ? 27.661  -9.373  -18.942 1 52.35  ? 298 TYR   B N   1 
ATOM   5098 C  CA  . TYR   B 1 313 ? 28.733  -8.398  -18.789 1 52.93  ? 298 TYR   B CA  1 
ATOM   5099 C  C   . TYR   B 1 313 ? 28.901  -7.904  -17.332 1 53.03  ? 298 TYR   B C   1 
ATOM   5100 O  O   . TYR   B 1 313 ? 29.692  -6.983  -17.091 1 53.45  ? 298 TYR   B O   1 
ATOM   5101 C  CB  . TYR   B 1 313 ? 28.46   -7.197  -19.691 1 53.31  ? 298 TYR   B CB  1 
ATOM   5102 C  CG  . TYR   B 1 313 ? 28.514  -7.495  -21.173 1 53.88  ? 298 TYR   B CG  1 
ATOM   5103 C  CD1 . TYR   B 1 313 ? 27.474  -8.158  -21.807 1 54.38  ? 298 TYR   B CD1 1 
ATOM   5104 C  CD2 . TYR   B 1 313 ? 29.581  -7.068  -21.949 1 54.91  ? 298 TYR   B CD2 1 
ATOM   5105 C  CE1 . TYR   B 1 313 ? 27.52   -8.441  -23.163 1 55.34  ? 298 TYR   B CE1 1 
ATOM   5106 C  CE2 . TYR   B 1 313 ? 29.635  -7.337  -23.311 1 55.8   ? 298 TYR   B CE2 1 
ATOM   5107 C  CZ  . TYR   B 1 313 ? 28.6    -8.02   -23.915 1 56.79  ? 298 TYR   B CZ  1 
ATOM   5108 O  OH  . TYR   B 1 313 ? 28.638  -8.268  -25.262 1 59.16  ? 298 TYR   B OH  1 
ATOM   5109 N  N   . MET   B 1 314 ? 28.164  -8.501  -16.366 1 52.24  ? 299 MET   B N   1 
ATOM   5110 C  CA  . MET   B 1 314 ? 28.269  -8.168  -14.941 1 51.74  ? 299 MET   B CA  1 
ATOM   5111 C  C   . MET   B 1 314 ? 29.182  -9.175  -14.257 1 51.28  ? 299 MET   B C   1 
ATOM   5112 O  O   . MET   B 1 314 ? 29.209  -10.336 -14.677 1 50.81  ? 299 MET   B O   1 
ATOM   5113 C  CB  . MET   B 1 314 ? 26.895  -8.288  -14.269 1 52.07  ? 299 MET   B CB  1 
ATOM   5114 C  CG  . MET   B 1 314 ? 25.889  -7.355  -14.783 1 54.29  ? 299 MET   B CG  1 
ATOM   5115 S  SD  . MET   B 1 314 ? 24.319  -7.661  -13.949 1 58.6   ? 299 MET   B SD  1 
ATOM   5116 C  CE  . MET   B 1 314 ? 23.298  -6.475  -14.8   1 54.28  ? 299 MET   B CE  1 
ATOM   5117 N  N   . PRO   B 1 315 ? 29.84   -8.83   -13.116 1 51.26  ? 300 PRO   B N   1 
ATOM   5118 C  CA  . PRO   B 1 315 ? 30.631  -9.854  -12.392 1 51.28  ? 300 PRO   B CA  1 
ATOM   5119 C  C   . PRO   B 1 315 ? 29.77   -11.079 -12.08  1 51.66  ? 300 PRO   B C   1 
ATOM   5120 O  O   . PRO   B 1 315 ? 28.552  -10.951 -11.902 1 51.89  ? 300 PRO   B O   1 
ATOM   5121 C  CB  . PRO   B 1 315 ? 31.084  -9.126  -11.118 1 51.85  ? 300 PRO   B CB  1 
ATOM   5122 C  CG  . PRO   B 1 315 ? 31.078  -7.671  -11.499 1 52.08  ? 300 PRO   B CG  1 
ATOM   5123 C  CD  . PRO   B 1 315 ? 29.897  -7.522  -12.432 1 50.58  ? 300 PRO   B CD  1 
ATOM   5124 N  N   . PRO   B 1 316 ? 30.349  -12.291 -12.161 1 51.63  ? 301 PRO   B N   1 
ATOM   5125 C  CA  . PRO   B 1 316 ? 29.538  -13.505 -11.968 1 50.87  ? 301 PRO   B CA  1 
ATOM   5126 C  C   . PRO   B 1 316 ? 28.774  -13.546 -10.658 1 50.38  ? 301 PRO   B C   1 
ATOM   5127 O  O   . PRO   B 1 316 ? 27.62   -13.936 -10.68  1 51.17  ? 301 PRO   B O   1 
ATOM   5128 C  CB  . PRO   B 1 316 ? 30.553  -14.637 -12.098 1 51.67  ? 301 PRO   B CB  1 
ATOM   5129 C  CG  . PRO   B 1 316 ? 31.899  -13.99  -11.807 1 52.15  ? 301 PRO   B CG  1 
ATOM   5130 C  CD  . PRO   B 1 316 ? 31.771  -12.618 -12.393 1 50.97  ? 301 PRO   B CD  1 
ATOM   5131 N  N   . ALA   B 1 317 ? 29.357  -13.074 -9.548  1 49.61  ? 302 ALA   B N   1 
ATOM   5132 C  CA  . ALA   B 1 317 ? 28.667  -13.028 -8.251  1 49.12  ? 302 ALA   B CA  1 
ATOM   5133 C  C   . ALA   B 1 317 ? 27.425  -12.116 -8.292  1 48.58  ? 302 ALA   B C   1 
ATOM   5134 O  O   . ALA   B 1 317 ? 26.41   -12.422 -7.679  1 47.56  ? 302 ALA   B O   1 
ATOM   5135 C  CB  . ALA   B 1 317 ? 29.623  -12.544 -7.181  1 48.99  ? 302 ALA   B CB  1 
ATOM   5136 N  N   . HIS   B 1 318 ? 27.511  -11.007 -9.032  1 49.3   ? 303 HIS   B N   1 
ATOM   5137 C  CA  . HIS   B 1 318 ? 26.396  -10.066 -9.159  1 50.31  ? 303 HIS   B CA  1 
ATOM   5138 C  C   . HIS   B 1 318 ? 25.316  -10.579 -10.074 1 51.15  ? 303 HIS   B C   1 
ATOM   5139 O  O   . HIS   B 1 318 ? 24.144  -10.335 -9.824  1 51.38  ? 303 HIS   B O   1 
ATOM   5140 C  CB  . HIS   B 1 318 ? 26.899  -8.685  -9.589  1 50.95  ? 303 HIS   B CB  1 
ATOM   5141 C  CG  . HIS   B 1 318 ? 27.923  -8.095  -8.659  1 52.3   ? 303 HIS   B CG  1 
ATOM   5142 N  ND1 . HIS   B 1 318 ? 28.588  -6.926  -8.979  1 54.05  ? 303 HIS   B ND1 1 
ATOM   5143 C  CD2 . HIS   B 1 318 ? 28.352  -8.522  -7.443  1 52.81  ? 303 HIS   B CD2 1 
ATOM   5144 C  CE1 . HIS   B 1 318 ? 29.392  -6.689  -7.954  1 54.34  ? 303 HIS   B CE1 1 
ATOM   5145 N  NE2 . HIS   B 1 318 ? 29.277  -7.619  -7.006  1 53.83  ? 303 HIS   B NE2 1 
ATOM   5146 N  N   . ARG   B 1 319 ? 25.695  -11.335 -11.101 1 51.69  ? 304 ARG   B N   1 
ATOM   5147 C  CA  . ARG   B 1 319 ? 24.766  -11.998 -12.002 1 52.48  ? 304 ARG   B CA  1 
ATOM   5148 C  C   . ARG   B 1 319 ? 24.016  -13.073 -11.179 1 51.9   ? 304 ARG   B C   1 
ATOM   5149 O  O   . ARG   B 1 319 ? 22.802  -13.167 -11.287 1 52.59  ? 304 ARG   B O   1 
ATOM   5150 C  CB  . ARG   B 1 319 ? 25.56   -12.655 -13.13  1 55.31  ? 304 ARG   B CB  1 
ATOM   5151 C  CG  . ARG   B 1 319 ? 24.775  -12.854 -14.408 1 61.94  ? 304 ARG   B CG  1 
ATOM   5152 C  CD  . ARG   B 1 319 ? 25.552  -13.686 -15.418 1 68.27  ? 304 ARG   B CD  1 
ATOM   5153 N  NE  . ARG   B 1 319 ? 26.926  -13.203 -15.614 1 74.18  ? 304 ARG   B NE  1 
ATOM   5154 C  CZ  . ARG   B 1 319 ? 28.015  -13.958 -15.463 1 78.42  ? 304 ARG   B CZ  1 
ATOM   5155 N  NH1 . ARG   B 1 319 ? 27.904  -15.234 -15.11  1 80.52  ? 304 ARG   B NH1 1 
ATOM   5156 N  NH2 . ARG   B 1 319 ? 29.222  -13.434 -15.641 1 77.63  ? 304 ARG   B NH2 1 
ATOM   5157 N  N   . ASN   B 1 320 ? 24.734  -13.837 -10.317 1 50.8   ? 305 ASN   B N   1 
ATOM   5158 C  CA  . ASN   B 1 320 ? 24.167  -14.847 -9.415  1 50.28  ? 305 ASN   B CA  1 
ATOM   5159 C  C   . ASN   B 1 320 ? 23.189  -14.204 -8.431  1 50.17  ? 305 ASN   B C   1 
ATOM   5160 O  O   . ASN   B 1 320 ? 22.159  -14.795 -8.115  1 50.28  ? 305 ASN   B O   1 
ATOM   5161 C  CB  . ASN   B 1 320 ? 25.271  -15.544 -8.62   1 50.82  ? 305 ASN   B CB  1 
ATOM   5162 C  CG  . ASN   B 1 320 ? 26.188  -16.4   -9.442  1 53.48  ? 305 ASN   B CG  1 
ATOM   5163 O  OD1 . ASN   B 1 320 ? 25.941  -16.647 -10.63  1 54.98  ? 305 ASN   B OD1 1 
ATOM   5164 N  ND2 . ASN   B 1 320 ? 27.252  -16.899 -8.812  1 53.21  ? 305 ASN   B ND2 1 
ATOM   5165 N  N   . PHE   B 1 321 ? 23.51   -12.999 -7.938  1 50.1   ? 306 PHE   B N   1 
ATOM   5166 C  CA  . PHE   B 1 321 ? 22.62   -12.286 -7.033  1 50.81  ? 306 PHE   B CA  1 
ATOM   5167 C  C   . PHE   B 1 321 ? 21.273  -11.979 -7.693  1 51.87  ? 306 PHE   B C   1 
ATOM   5168 O  O   . PHE   B 1 321 ? 20.232  -12.202 -7.071  1 51.43  ? 306 PHE   B O   1 
ATOM   5169 C  CB  . PHE   B 1 321 ? 23.264  -11.01  -6.508  1 50.32  ? 306 PHE   B CB  1 
ATOM   5170 C  CG  . PHE   B 1 321 ? 22.363  -10.276 -5.547  1 50.87  ? 306 PHE   B CG  1 
ATOM   5171 C  CD1 . PHE   B 1 321 ? 22.155  -10.756 -4.265  1 51.49  ? 306 PHE   B CD1 1 
ATOM   5172 C  CD2 . PHE   B 1 321 ? 21.691  -9.123  -5.938  1 51.48  ? 306 PHE   B CD2 1 
ATOM   5173 C  CE1 . PHE   B 1 321 ? 21.32   -10.075 -3.378  1 51.74  ? 306 PHE   B CE1 1 
ATOM   5174 C  CE2 . PHE   B 1 321 ? 20.845  -8.452  -5.053  1 52     ? 306 PHE   B CE2 1 
ATOM   5175 C  CZ  . PHE   B 1 321 ? 20.669  -8.93   -3.778  1 51.42  ? 306 PHE   B CZ  1 
ATOM   5176 N  N   . LEU   B 1 322 ? 21.293  -11.481 -8.95   1 52.78  ? 307 LEU   B N   1 
ATOM   5177 C  CA  . LEU   B 1 322 ? 20.069  -11.166 -9.681  1 53.95  ? 307 LEU   B CA  1 
ATOM   5178 C  C   . LEU   B 1 322 ? 19.206  -12.385 -9.881  1 54.49  ? 307 LEU   B C   1 
ATOM   5179 O  O   . LEU   B 1 322 ? 17.992  -12.278 -9.764  1 55.08  ? 307 LEU   B O   1 
ATOM   5180 C  CB  . LEU   B 1 322 ? 20.37   -10.53  -11.046 1 54.81  ? 307 LEU   B CB  1 
ATOM   5181 C  CG  . LEU   B 1 322 ? 21.003  -9.145  -11.037 1 57.51  ? 307 LEU   B CG  1 
ATOM   5182 C  CD1 . LEU   B 1 322 ? 21.101  -8.587  -12.452 1 58.4   ? 307 LEU   B CD1 1 
ATOM   5183 C  CD2 . LEU   B 1 322 ? 20.211  -8.174  -10.173 1 58.15  ? 307 LEU   B CD2 1 
ATOM   5184 N  N   . CYS   B 1 323 ? 19.808  -13.535 -10.196 1 54.4   ? 308 CYS   B N   1 
ATOM   5185 C  CA  . CYS   B 1 323 ? 19.075  -14.781 -10.416 1 55.35  ? 308 CYS   B CA  1 
ATOM   5186 C  C   . CYS   B 1 323 ? 18.428  -15.258 -9.107  1 55.07  ? 308 CYS   B C   1 
ATOM   5187 O  O   . CYS   B 1 323 ? 17.291  -15.74  -9.119  1 55.09  ? 308 CYS   B O   1 
ATOM   5188 C  CB  . CYS   B 1 323 ? 20.002  -15.833 -11.031 1 57.2   ? 308 CYS   B CB  1 
ATOM   5189 S  SG  . CYS   B 1 323 ? 19.701  -17.54  -10.503 1 63.23  ? 308 CYS   B SG  1 
ATOM   5190 N  N   . SER   B 1 324 ? 19.151  -15.125 -7.989  1 54.3   ? 309 SER   B N   1 
ATOM   5191 C  CA  . SER   B 1 324 ? 18.63   -15.487 -6.673  1 53.92  ? 309 SER   B CA  1 
ATOM   5192 C  C   . SER   B 1 324 ? 17.435  -14.629 -6.304  1 53.67  ? 309 SER   B C   1 
ATOM   5193 O  O   . SER   B 1 324 ? 16.511  -15.13  -5.675  1 54.53  ? 309 SER   B O   1 
ATOM   5194 C  CB  . SER   B 1 324 ? 19.722  -15.376 -5.619  1 55.43  ? 309 SER   B CB  1 
ATOM   5195 O  OG  . SER   B 1 324 ? 20.818  -16.204 -5.982  1 57.65  ? 309 SER   B OG  1 
ATOM   5196 N  N   . LEU   B 1 325 ? 17.413  -13.357 -6.727  1 53.02  ? 310 LEU   B N   1 
ATOM   5197 C  CA  . LEU   B 1 325 ? 16.26   -12.497 -6.49   1 53.33  ? 310 LEU   B CA  1 
ATOM   5198 C  C   . LEU   B 1 325 ? 15.08   -12.998 -7.31   1 54.38  ? 310 LEU   B C   1 
ATOM   5199 O  O   . LEU   B 1 325 ? 13.96   -13.001 -6.82   1 55.64  ? 310 LEU   B O   1 
ATOM   5200 C  CB  . LEU   B 1 325 ? 16.546  -11.04  -6.876  1 53.13  ? 310 LEU   B CB  1 
ATOM   5201 C  CG  . LEU   B 1 325 ? 17.413  -10.199 -5.975  1 53.86  ? 310 LEU   B CG  1 
ATOM   5202 C  CD1 . LEU   B 1 325 ? 17.424  -8.763  -6.474  1 53.79  ? 310 LEU   B CD1 1 
ATOM   5203 C  CD2 . LEU   B 1 325 ? 16.959  -10.292 -4.505  1 54.36  ? 310 LEU   B CD2 1 
ATOM   5204 N  N   . GLU   B 1 326 ? 15.314  -13.399 -8.56   1 54.18  ? 311 GLU   B N   1 
ATOM   5205 C  CA  . GLU   B 1 326 ? 14.274  -13.943 -9.426  1 54.76  ? 311 GLU   B CA  1 
ATOM   5206 C  C   . GLU   B 1 326 ? 13.721  -15.285 -8.898  1 55     ? 311 GLU   B C   1 
ATOM   5207 O  O   . GLU   B 1 326 ? 12.562  -15.599 -9.13   1 55.9   ? 311 GLU   B O   1 
ATOM   5208 C  CB  . GLU   B 1 326 ? 14.801  -14.095 -10.856 1 57.25  ? 311 GLU   B CB  1 
ATOM   5209 C  CG  . GLU   B 1 326 ? 15.095  -12.763 -11.515 1 62.3   ? 311 GLU   B CG  1 
ATOM   5210 C  CD  . GLU   B 1 326 ? 15.641  -12.852 -12.924 1 69.35  ? 311 GLU   B CD  1 
ATOM   5211 O  OE1 . GLU   B 1 326 ? 16.435  -13.783 -13.193 1 72.09  ? 311 GLU   B OE1 1 
ATOM   5212 O  OE2 . GLU   B 1 326 ? 15.293  -11.98  -13.755 1 70.92  ? 311 GLU   B OE2 1 
ATOM   5213 N  N   . SER   B 1 327 ? 14.535  -16.055 -8.183  1 54.48  ? 312 SER   B N   1 
ATOM   5214 C  CA  . SER   B 1 327 ? 14.137  -17.322 -7.567  1 54.89  ? 312 SER   B CA  1 
ATOM   5215 C  C   . SER   B 1 327 ? 13.195  -17.132 -6.359  1 55.17  ? 312 SER   B C   1 
ATOM   5216 O  O   . SER   B 1 327 ? 12.451  -18.054 -5.989  1 55.37  ? 312 SER   B O   1 
ATOM   5217 C  CB  . SER   B 1 327 ? 15.372  -18.13  -7.164  1 55.86  ? 312 SER   B CB  1 
ATOM   5218 O  OG  . SER   B 1 327 ? 15.996  -18.666 -8.325  1 58.16  ? 312 SER   B OG  1 
ATOM   5219 N  N   . ASN   B 1 328 ? 13.237  -15.946 -5.736  1 54.77  ? 313 ASN   B N   1 
ATOM   5220 C  CA  . ASN   B 1 328 ? 12.388  -15.619 -4.597  1 54.73  ? 313 ASN   B CA  1 
ATOM   5221 C  C   . ASN   B 1 328 ? 10.986  -15.208 -5.064  1 53.71  ? 313 ASN   B C   1 
ATOM   5222 O  O   . ASN   B 1 328 ? 10.798  -14.816 -6.217  1 53.45  ? 313 ASN   B O   1 
ATOM   5223 C  CB  . ASN   B 1 328 ? 13.045  -14.531 -3.757  1 56.71  ? 313 ASN   B CB  1 
ATOM   5224 C  CG  . ASN   B 1 328 ? 14.084  -15.074 -2.823  1 62.08  ? 313 ASN   B CG  1 
ATOM   5225 O  OD1 . ASN   B 1 328 ? 15.251  -15.27  -3.193  1 64.28  ? 313 ASN   B OD1 1 
ATOM   5226 N  ND2 . ASN   B 1 328 ? 13.679  -15.338 -1.587  1 63.35  ? 313 ASN   B ND2 1 
ATOM   5227 N  N   . PRO   B 1 329 ? 9.972   -15.32  -4.19   1 53.12  ? 314 PRO   B N   1 
ATOM   5228 C  CA  . PRO   B 1 329 ? 8.611   -14.955 -4.609  1 52.61  ? 314 PRO   B CA  1 
ATOM   5229 C  C   . PRO   B 1 329 ? 8.482   -13.486 -4.997  1 52.84  ? 314 PRO   B C   1 
ATOM   5230 O  O   . PRO   B 1 329 ? 9.27    -12.649 -4.579  1 52.69  ? 314 PRO   B O   1 
ATOM   5231 C  CB  . PRO   B 1 329 ? 7.746   -15.305 -3.394  1 52.79  ? 314 PRO   B CB  1 
ATOM   5232 C  CG  . PRO   B 1 329 ? 8.586   -16.165 -2.534  1 53.44  ? 314 PRO   B CG  1 
ATOM   5233 C  CD  . PRO   B 1 329 ? 10.007  -15.777 -2.788  1 52.41  ? 314 PRO   B CD  1 
ATOM   5234 N  N   . SER   B 1 330 ? 7.472   -13.184 -5.804  1 52.96  ? 315 SER   B N   1 
ATOM   5235 C  CA  . SER   B 1 330 ? 7.192   -11.849 -6.29   1 53.64  ? 315 SER   B CA  1 
ATOM   5236 C  C   . SER   B 1 330 ? 6.611   -10.946 -5.203  1 54.12  ? 315 SER   B C   1 
ATOM   5237 O  O   . SER   B 1 330 ? 5.548   -11.228 -4.65   1 54.48  ? 315 SER   B O   1 
ATOM   5238 C  CB  . SER   B 1 330 ? 6.229   -11.93  -7.473  1 55.66  ? 315 SER   B CB  1 
ATOM   5239 O  OG  . SER   B 1 330 ? 5.906   -10.671 -8.041  1 58.8   ? 315 SER   B OG  1 
ATOM   5240 N  N   . VAL   B 1 331 ? 7.306   -9.838  -4.92   1 53.87  ? 316 VAL   B N   1 
ATOM   5241 C  CA  . VAL   B 1 331 ? 6.848   -8.818  -3.982  1 53.4   ? 316 VAL   B CA  1 
ATOM   5242 C  C   . VAL   B 1 331 ? 5.592   -8.145  -4.587  1 53.49  ? 316 VAL   B C   1 
ATOM   5243 O  O   . VAL   B 1 331 ? 4.628   -7.897  -3.869  1 53.77  ? 316 VAL   B O   1 
ATOM   5244 C  CB  . VAL   B 1 331 ? 7.966   -7.787  -3.719  1 53.33  ? 316 VAL   B CB  1 
ATOM   5245 C  CG1 . VAL   B 1 331 ? 7.521   -6.731  -2.723  1 53.69  ? 316 VAL   B CG1 1 
ATOM   5246 C  CG2 . VAL   B 1 331 ? 9.235   -8.471  -3.245  1 53.38  ? 316 VAL   B CG2 1 
ATOM   5247 N  N   . ARG   B 1 332 ? 5.58    -7.899  -5.908  1 53.04  ? 317 ARG   B N   1 
ATOM   5248 C  CA  . ARG   B 1 332 ? 4.423   -7.292  -6.556  1 53.13  ? 317 ARG   B CA  1 
ATOM   5249 C  C   . ARG   B 1 332 ? 3.187   -8.195  -6.449  1 53.82  ? 317 ARG   B C   1 
ATOM   5250 O  O   . ARG   B 1 332 ? 2.104   -7.709  -6.132  1 54.12  ? 317 ARG   B O   1 
ATOM   5251 C  CB  . ARG   B 1 332 ? 4.744   -6.969  -8.016  1 53.41  ? 317 ARG   B CB  1 
ATOM   5252 C  CG  . ARG   B 1 332 ? 3.566   -6.431  -8.79   1 53.81  ? 317 ARG   B CG  1 
ATOM   5253 C  CD  . ARG   B 1 332 ? 3.929   -6.055  -10.192 1 55.39  ? 317 ARG   B CD  1 
ATOM   5254 N  NE  . ARG   B 1 332 ? 3.231   -4.822  -10.56  1 57.06  ? 317 ARG   B NE  1 
ATOM   5255 C  CZ  . ARG   B 1 332 ? 2.078   -4.787  -11.219 1 60.21  ? 317 ARG   B CZ  1 
ATOM   5256 N  NH1 . ARG   B 1 332 ? 1.492   -5.915  -11.611 1 60.77  ? 317 ARG   B NH1 1 
ATOM   5257 N  NH2 . ARG   B 1 332 ? 1.499   -3.628  -11.492 1 60.29  ? 317 ARG   B NH2 1 
ATOM   5258 N  N   . GLU   B 1 333 ? 3.347   -9.503  -6.693  1 54.15  ? 318 GLU   B N   1 
ATOM   5259 C  CA  . GLU   B 1 333 ? 2.22    -10.434 -6.599  1 55.08  ? 318 GLU   B CA  1 
ATOM   5260 C  C   . GLU   B 1 333 ? 1.683   -10.489 -5.174  1 55.38  ? 318 GLU   B C   1 
ATOM   5261 O  O   . GLU   B 1 333 ? 0.471   -10.456 -4.981  1 56.12  ? 318 GLU   B O   1 
ATOM   5262 C  CB  . GLU   B 1 333 ? 2.584   -11.833 -7.119  1 57.07  ? 318 GLU   B CB  1 
ATOM   5263 N  N   . PHE   B 1 334 ? 2.578   -10.471 -4.186  1 54.97  ? 319 PHE   B N   1 
ATOM   5264 C  CA  . PHE   B 1 334 ? 2.217   -10.49  -2.778  1 55.29  ? 319 PHE   B CA  1 
ATOM   5265 C  C   . PHE   B 1 334 ? 1.404   -9.262  -2.416  1 55.99  ? 319 PHE   B C   1 
ATOM   5266 O  O   . PHE   B 1 334 ? 0.385   -9.389  -1.761  1 56.34  ? 319 PHE   B O   1 
ATOM   5267 C  CB  . PHE   B 1 334 ? 3.481   -10.571 -1.909  1 55.01  ? 319 PHE   B CB  1 
ATOM   5268 C  CG  . PHE   B 1 334 ? 3.239   -10.794 -0.43   1 55.67  ? 319 PHE   B CG  1 
ATOM   5269 C  CD1 . PHE   B 1 334 ? 3.015   -9.722  0.426   1 56.37  ? 319 PHE   B CD1 1 
ATOM   5270 C  CD2 . PHE   B 1 334 ? 3.303   -12.064 0.116   1 56.13  ? 319 PHE   B CD2 1 
ATOM   5271 C  CE1 . PHE   B 1 334 ? 2.821   -9.925  1.788   1 56.95  ? 319 PHE   B CE1 1 
ATOM   5272 C  CE2 . PHE   B 1 334 ? 3.132   -12.26  1.486   1 57.03  ? 319 PHE   B CE2 1 
ATOM   5273 C  CZ  . PHE   B 1 334 ? 2.884   -11.189 2.312   1 56.75  ? 319 PHE   B CZ  1 
ATOM   5274 N  N   . VAL   B 1 335 ? 1.841   -8.081  -2.842  1 56.37  ? 320 VAL   B N   1 
ATOM   5275 C  CA  . VAL   B 1 335 ? 1.152   -6.836  -2.538  1 57.15  ? 320 VAL   B CA  1 
ATOM   5276 C  C   . VAL   B 1 335 ? -0.22   -6.775  -3.223  1 58.77  ? 320 VAL   B C   1 
ATOM   5277 O  O   . VAL   B 1 335 ? -1.217  -6.394  -2.599  1 59.17  ? 320 VAL   B O   1 
ATOM   5278 C  CB  . VAL   B 1 335 ? 2.062   -5.631  -2.858  1 57.23  ? 320 VAL   B CB  1 
ATOM   5279 C  CG1 . VAL   B 1 335 ? 1.282   -4.324  -2.823  1 57.89  ? 320 VAL   B CG1 1 
ATOM   5280 C  CG2 . VAL   B 1 335 ? 3.245   -5.578  -1.89   1 57.06  ? 320 VAL   B CG2 1 
ATOM   5281 N  N   . LEU   B 1 336 ? -0.289  -7.23   -4.474  1 59.45  ? 321 LEU   B N   1 
ATOM   5282 C  CA  . LEU   B 1 336 ? -1.547  -7.265  -5.208  1 60.87  ? 321 LEU   B CA  1 
ATOM   5283 C  C   . LEU   B 1 336 ? -2.555  -8.203  -4.516  1 61.99  ? 321 LEU   B C   1 
ATOM   5284 O  O   . LEU   B 1 336 ? -3.737  -7.885  -4.417  1 62.81  ? 321 LEU   B O   1 
ATOM   5285 C  CB  . LEU   B 1 336 ? -1.286  -7.774  -6.631  1 61.46  ? 321 LEU   B CB  1 
ATOM   5286 C  CG  . LEU   B 1 336 ? -0.91   -6.721  -7.651  1 63.59  ? 321 LEU   B CG  1 
ATOM   5287 C  CD1 . LEU   B 1 336 ? -0.504  -7.361  -8.967  1 64.12  ? 321 LEU   B CD1 1 
ATOM   5288 C  CD2 . LEU   B 1 336 ? -2.064  -5.759  -7.872  1 64.36  ? 321 LEU   B CD2 1 
ATOM   5289 N  N   . SER   B 1 337 ? -2.081  -9.352  -4.024  1 61.45  ? 322 SER   B N   1 
ATOM   5290 C  CA  . SER   B 1 337 ? -2.931  -10.355 -3.4    1 61.1   ? 322 SER   B CA  1 
ATOM   5291 C  C   . SER   B 1 337 ? -3.425  -10.01  -1.994  1 61.4   ? 322 SER   B C   1 
ATOM   5292 O  O   . SER   B 1 337 ? -4.038  -10.884 -1.374  1 62.05  ? 322 SER   B O   1 
ATOM   5293 C  CB  . SER   B 1 337 ? -2.182  -11.687 -3.328  1 61.5   ? 322 SER   B CB  1 
ATOM   5294 O  OG  . SER   B 1 337 ? -1.226  -11.738 -2.275  1 62.4   ? 322 SER   B OG  1 
ATOM   5295 N  N   . LYS   B 1 338 ? -3.114  -8.816  -1.45   1 60.62  ? 323 LYS   B N   1 
ATOM   5296 C  CA  . LYS   B 1 338 ? -3.468  -8.547  -0.059  1 60.15  ? 323 LYS   B CA  1 
ATOM   5297 C  C   . LYS   B 1 338 ? -4.67   -7.654  0.171   1 60.08  ? 323 LYS   B C   1 
ATOM   5298 O  O   . LYS   B 1 338 ? -5.211  -7.711  1.282   1 61.13  ? 323 LYS   B O   1 
ATOM   5299 C  CB  . LYS   B 1 338 ? -2.274  -8.008  0.739   1 61.07  ? 323 LYS   B CB  1 
ATOM   5300 C  CG  . LYS   B 1 338 ? -1.16   -9.019  0.966   1 63.63  ? 323 LYS   B CG  1 
ATOM   5301 C  CD  . LYS   B 1 338 ? -1.604  -10.314 1.619   1 68.09  ? 323 LYS   B CD  1 
ATOM   5302 C  CE  . LYS   B 1 338 ? -0.777  -11.462 1.091   1 73.65  ? 323 LYS   B CE  1 
ATOM   5303 N  NZ  . LYS   B 1 338 ? -0.859  -12.678 1.945   1 76.84  ? 323 LYS   B NZ  1 
ATOM   5304 N  N   . GLY   B 1 339 ? -5.084  -6.838  -0.814  1 58.46  ? 324 GLY   B N   1 
ATOM   5305 C  CA  . GLY   B 1 339 ? -6.217  -5.922  -0.645  1 57.17  ? 324 GLY   B CA  1 
ATOM   5306 C  C   . GLY   B 1 339 ? -6.002  -4.967  0.515   1 55.96  ? 324 GLY   B C   1 
ATOM   5307 O  O   . GLY   B 1 339 ? -6.89   -4.749  1.346   1 56.22  ? 324 GLY   B O   1 
ATOM   5308 N  N   . ASP   B 1 340 ? -4.77   -4.456  0.599   1 54.67  ? 325 ASP   B N   1 
ATOM   5309 C  CA  . ASP   B 1 340 ? -4.227  -3.599  1.646   1 53.86  ? 325 ASP   B CA  1 
ATOM   5310 C  C   . ASP   B 1 340 ? -3.747  -2.322  0.99    1 53.65  ? 325 ASP   B C   1 
ATOM   5311 O  O   . ASP   B 1 340 ? -2.718  -2.342  0.329   1 53.74  ? 325 ASP   B O   1 
ATOM   5312 C  CB  . ASP   B 1 340 ? -3.023  -4.327  2.223   1 54.19  ? 325 ASP   B CB  1 
ATOM   5313 C  CG  . ASP   B 1 340 ? -2.466  -3.785  3.503   1 57.04  ? 325 ASP   B CG  1 
ATOM   5314 O  OD1 . ASP   B 1 340 ? -2.482  -2.553  3.68    1 57.57  ? 325 ASP   B OD1 1 
ATOM   5315 O  OD2 . ASP   B 1 340 ? -1.973  -4.594  4.318   1 58.55  ? 325 ASP   B OD2 1 
ATOM   5316 N  N   . ALA   B 1 341 ? -4.482  -1.22   1.16    1 53.21  ? 326 ALA   B N   1 
ATOM   5317 C  CA  . ALA   B 1 341 ? -4.141  0.049   0.534   1 53.04  ? 326 ALA   B CA  1 
ATOM   5318 C  C   . ALA   B 1 341 ? -2.797  0.611   0.998   1 53.26  ? 326 ALA   B C   1 
ATOM   5319 O  O   . ALA   B 1 341 ? -2.054  1.162   0.188   1 52.99  ? 326 ALA   B O   1 
ATOM   5320 C  CB  . ALA   B 1 341 ? -5.251  1.054   0.76    1 52.49  ? 326 ALA   B CB  1 
ATOM   5321 N  N   . GLY   B 1 342 ? -2.491  0.444   2.279   1 53.5   ? 327 GLY   B N   1 
ATOM   5322 C  CA  . GLY   B 1 342 ? -1.247  0.939   2.854   1 54.61  ? 327 GLY   B CA  1 
ATOM   5323 C  C   . GLY   B 1 342 ? -0.013  0.272   2.283   1 55.83  ? 327 GLY   B C   1 
ATOM   5324 O  O   . GLY   B 1 342 ? 0.985   0.933   1.991   1 56.6   ? 327 GLY   B O   1 
ATOM   5325 N  N   . LEU   B 1 343 ? -0.087  -1.044  2.118   1 55.97  ? 328 LEU   B N   1 
ATOM   5326 C  CA  . LEU   B 1 343 ? 0.959   -1.87   1.543   1 56.78  ? 328 LEU   B CA  1 
ATOM   5327 C  C   . LEU   B 1 343 ? 1.13    -1.518  0.051   1 58.24  ? 328 LEU   B C   1 
ATOM   5328 O  O   . LEU   B 1 343 ? 2.263   -1.461  -0.441  1 58.71  ? 328 LEU   B O   1 
ATOM   5329 C  CB  . LEU   B 1 343 ? 0.567   -3.346  1.709   1 56.43  ? 328 LEU   B CB  1 
ATOM   5330 C  CG  . LEU   B 1 343 ? 1.687   -4.356  1.817   1 57.36  ? 328 LEU   B CG  1 
ATOM   5331 C  CD1 . LEU   B 1 343 ? 2.666   -3.999  2.953   1 57.8   ? 328 LEU   B CD1 1 
ATOM   5332 C  CD2 . LEU   B 1 343 ? 1.13    -5.745  1.98    1 57.34  ? 328 LEU   B CD2 1 
ATOM   5333 N  N   . ARG   B 1 344 ? 0.011   -1.253  -0.653  1 58.47  ? 329 ARG   B N   1 
ATOM   5334 C  CA  . ARG   B 1 344 ? 0.038   -0.84   -2.05   1 59.48  ? 329 ARG   B CA  1 
ATOM   5335 C  C   . ARG   B 1 344 ? 0.673   0.532   -2.198  1 60.39  ? 329 ARG   B C   1 
ATOM   5336 O  O   . ARG   B 1 344 ? 1.385   0.759   -3.174  1 60.86  ? 329 ARG   B O   1 
ATOM   5337 C  CB  . ARG   B 1 344 ? -1.365  -0.821  -2.655  1 60.52  ? 329 ARG   B CB  1 
ATOM   5338 C  CG  . ARG   B 1 344 ? -1.927  -2.204  -2.92   1 63.79  ? 329 ARG   B CG  1 
ATOM   5339 C  CD  . ARG   B 1 344 ? -3.071  -2.181  -3.918  1 67.18  ? 329 ARG   B CD  1 
ATOM   5340 N  NE  . ARG   B 1 344 ? -4.113  -1.221  -3.553  1 70.57  ? 329 ARG   B NE  1 
ATOM   5341 C  CZ  . ARG   B 1 344 ? -5.145  -1.495  -2.757  1 73.08  ? 329 ARG   B CZ  1 
ATOM   5342 N  NH1 . ARG   B 1 344 ? -5.289  -2.71   -2.237  1 72.59  ? 329 ARG   B NH1 1 
ATOM   5343 N  NH2 . ARG   B 1 344 ? -6.041  -0.556  -2.475  1 72.84  ? 329 ARG   B NH2 1 
ATOM   5344 N  N   . GLU   B 1 345 ? 0.423   1.438   -1.231  1 60.29  ? 330 GLU   B N   1 
ATOM   5345 C  CA  . GLU   B 1 345 ? 0.966   2.793   -1.212  1 60.46  ? 330 GLU   B CA  1 
ATOM   5346 C  C   . GLU   B 1 345 ? 2.49    2.77    -1.037  1 60.56  ? 330 GLU   B C   1 
ATOM   5347 O  O   . GLU   B 1 345 ? 3.195   3.527   -1.706  1 61.06  ? 330 GLU   B O   1 
ATOM   5348 C  CB  . GLU   B 1 345 ? 0.296   3.631   -0.11   1 61.96  ? 330 GLU   B CB  1 
ATOM   5349 N  N   . ALA   B 1 346 ? 2.99    1.892   -0.15   1 59.77  ? 331 ALA   B N   1 
ATOM   5350 C  CA  . ALA   B 1 346 ? 4.421   1.723   0.108   1 59.34  ? 331 ALA   B CA  1 
ATOM   5351 C  C   . ALA   B 1 346 ? 5.122   1.109   -1.114  1 59.15  ? 331 ALA   B C   1 
ATOM   5352 O  O   . ALA   B 1 346 ? 6.231   1.509   -1.463  1 59.88  ? 331 ALA   B O   1 
ATOM   5353 C  CB  . ALA   B 1 346 ? 4.63    0.835   1.328   1 59.15  ? 331 ALA   B CB  1 
ATOM   5354 N  N   . TYR   B 1 347 ? 4.468   0.152   -1.772  1 58.01  ? 332 TYR   B N   1 
ATOM   5355 C  CA  . TYR   B 1 347 ? 5.015   -0.486  -2.963  1 57.27  ? 332 TYR   B CA  1 
ATOM   5356 C  C   . TYR   B 1 347 ? 5.125   0.551   -4.083  1 58.59  ? 332 TYR   B C   1 
ATOM   5357 O  O   . TYR   B 1 347 ? 6.13    0.595   -4.781  1 59.3   ? 332 TYR   B O   1 
ATOM   5358 C  CB  . TYR   B 1 347 ? 4.134   -1.682  -3.397  1 55.57  ? 332 TYR   B CB  1 
ATOM   5359 C  CG  . TYR   B 1 347 ? 4.485   -2.213  -4.768  1 54.29  ? 332 TYR   B CG  1 
ATOM   5360 C  CD1 . TYR   B 1 347 ? 5.511   -3.129  -4.937  1 54.21  ? 332 TYR   B CD1 1 
ATOM   5361 C  CD2 . TYR   B 1 347 ? 3.835   -1.75   -5.901  1 54.3   ? 332 TYR   B CD2 1 
ATOM   5362 C  CE1 . TYR   B 1 347 ? 5.871   -3.582  -6.195  1 54.66  ? 332 TYR   B CE1 1 
ATOM   5363 C  CE2 . TYR   B 1 347 ? 4.168   -2.213  -7.163  1 54.79  ? 332 TYR   B CE2 1 
ATOM   5364 C  CZ  . TYR   B 1 347 ? 5.2     -3.118  -7.309  1 55.67  ? 332 TYR   B CZ  1 
ATOM   5365 O  OH  . TYR   B 1 347 ? 5.56    -3.574  -8.554  1 57.49  ? 332 TYR   B OH  1 
ATOM   5366 N  N   . ASP   B 1 348 ? 4.082   1.362   -4.26   1 58.87  ? 333 ASP   B N   1 
ATOM   5367 C  CA  . ASP   B 1 348 ? 4.011   2.403   -5.283  1 59.11  ? 333 ASP   B CA  1 
ATOM   5368 C  C   . ASP   B 1 348 ? 5.008   3.535   -5.045  1 59.46  ? 333 ASP   B C   1 
ATOM   5369 O  O   . ASP   B 1 348 ? 5.394   4.211   -5.998  1 59.72  ? 333 ASP   B O   1 
ATOM   5370 C  CB  . ASP   B 1 348 ? 2.592   2.966   -5.36   1 60.3   ? 333 ASP   B CB  1 
ATOM   5371 C  CG  . ASP   B 1 348 ? 1.679   2.246   -6.332  1 65.3   ? 333 ASP   B CG  1 
ATOM   5372 O  OD1 . ASP   B 1 348 ? 2.069   1.169   -6.838  1 65.34  ? 333 ASP   B OD1 1 
ATOM   5373 O  OD2 . ASP   B 1 348 ? 0.58    2.758   -6.596  1 69.11  ? 333 ASP   B OD2 1 
ATOM   5374 N  N   . ALA   B 1 349 ? 5.415   3.753   -3.785  1 59.1   ? 334 ALA   B N   1 
ATOM   5375 C  CA  . ALA   B 1 349 ? 6.393   4.772   -3.459  1 59.62  ? 334 ALA   B CA  1 
ATOM   5376 C  C   . ALA   B 1 349 ? 7.754   4.392   -4.073  1 60.36  ? 334 ALA   B C   1 
ATOM   5377 O  O   . ALA   B 1 349 ? 8.468   5.274   -4.549  1 60.93  ? 334 ALA   B O   1 
ATOM   5378 C  CB  . ALA   B 1 349 ? 6.512   4.906   -1.953  1 59.83  ? 334 ALA   B CB  1 
ATOM   5379 N  N   . CYS   B 1 350 ? 8.091   3.072   -4.079  1 60.04  ? 335 CYS   B N   1 
ATOM   5380 C  CA  . CYS   B 1 350 ? 9.297   2.491   -4.666  1 59.87  ? 335 CYS   B CA  1 
ATOM   5381 C  C   . CYS   B 1 350 ? 9.263   2.648   -6.186  1 60.51  ? 335 CYS   B C   1 
ATOM   5382 O  O   . CYS   B 1 350 ? 10.234  3.082   -6.791  1 60.32  ? 335 CYS   B O   1 
ATOM   5383 C  CB  . CYS   B 1 350 ? 9.422   1.023   -4.277  1 59.42  ? 335 CYS   B CB  1 
ATOM   5384 S  SG  . CYS   B 1 350 ? 9.674   0.748   -2.514  1 61.12  ? 335 CYS   B SG  1 
ATOM   5385 N  N   . VAL   B 1 351 ? 8.143   2.285   -6.792  1 61.23  ? 336 VAL   B N   1 
ATOM   5386 C  CA  . VAL   B 1 351 ? 7.965   2.356   -8.229  1 62.47  ? 336 VAL   B CA  1 
ATOM   5387 C  C   . VAL   B 1 351 ? 8.038   3.803   -8.707  1 63.64  ? 336 VAL   B C   1 
ATOM   5388 O  O   . VAL   B 1 351 ? 8.803   4.079   -9.635  1 64.32  ? 336 VAL   B O   1 
ATOM   5389 C  CB  . VAL   B 1 351 ? 6.677   1.62    -8.667  1 62.75  ? 336 VAL   B CB  1 
ATOM   5390 C  CG1 . VAL   B 1 351 ? 6.495   1.686   -10.175 1 63.23  ? 336 VAL   B CG1 1 
ATOM   5391 C  CG2 . VAL   B 1 351 ? 6.702   0.17    -8.192  1 62.77  ? 336 VAL   B CG2 1 
ATOM   5392 N  N   . LYS   B 1 352 ? 7.354   4.736   -8.005  1 63.29  ? 337 LYS   B N   1 
ATOM   5393 C  CA  . LYS   B 1 352 ? 7.379   6.166   -8.336  1 63.18  ? 337 LYS   B CA  1 
ATOM   5394 C  C   . LYS   B 1 352 ? 8.786   6.74    -8.252  1 63.14  ? 337 LYS   B C   1 
ATOM   5395 O  O   . LYS   B 1 352 ? 9.17    7.511   -9.121  1 63.81  ? 337 LYS   B O   1 
ATOM   5396 C  CB  . LYS   B 1 352 ? 6.411   6.968   -7.455  1 64.5   ? 337 LYS   B CB  1 
ATOM   5397 N  N   . ALA   B 1 353 ? 9.575   6.322   -7.261  1 62.42  ? 338 ALA   B N   1 
ATOM   5398 C  CA  . ALA   B 1 353 ? 10.959  6.784   -7.129  1 62.47  ? 338 ALA   B CA  1 
ATOM   5399 C  C   . ALA   B 1 353 ? 11.841  6.317   -8.311  1 62.67  ? 338 ALA   B C   1 
ATOM   5400 O  O   . ALA   B 1 353 ? 12.801  6.997   -8.671  1 63.04  ? 338 ALA   B O   1 
ATOM   5401 C  CB  . ALA   B 1 353 ? 11.55   6.307   -5.808  1 62.4   ? 338 ALA   B CB  1 
ATOM   5402 N  N   . LEU   B 1 354 ? 11.517  5.158   -8.903  1 62.19  ? 339 LEU   B N   1 
ATOM   5403 C  CA  . LEU   B 1 354 ? 12.237  4.627   -10.053 1 62.35  ? 339 LEU   B CA  1 
ATOM   5404 C  C   . LEU   B 1 354 ? 11.815  5.386   -11.301 1 62.17  ? 339 LEU   B C   1 
ATOM   5405 O  O   . LEU   B 1 354 ? 12.661  5.687   -12.135 1 62.08  ? 339 LEU   B O   1 
ATOM   5406 C  CB  . LEU   B 1 354 ? 11.935  3.141   -10.228 1 62.92  ? 339 LEU   B CB  1 
ATOM   5407 C  CG  . LEU   B 1 354 ? 13.072  2.167   -10.172 1 65.06  ? 339 LEU   B CG  1 
ATOM   5408 C  CD1 . LEU   B 1 354 ? 13.79   2.239   -8.877  1 66.16  ? 339 LEU   B CD1 1 
ATOM   5409 C  CD2 . LEU   B 1 354 ? 12.551  0.777   -10.343 1 65.89  ? 339 LEU   B CD2 1 
ATOM   5410 N  N   . VAL   B 1 355 ? 10.512  5.714   -11.43  1 62.06  ? 340 VAL   B N   1 
ATOM   5411 C  CA  . VAL   B 1 355 ? 10.024  6.506   -12.552 1 62.26  ? 340 VAL   B CA  1 
ATOM   5412 C  C   . VAL   B 1 355 ? 10.642  7.899   -12.499 1 62.37  ? 340 VAL   B C   1 
ATOM   5413 O  O   . VAL   B 1 355 ? 11.054  8.408   -13.531 1 63.11  ? 340 VAL   B O   1 
ATOM   5414 C  CB  . VAL   B 1 355 ? 8.486   6.578   -12.598 1 62.95  ? 340 VAL   B CB  1 
ATOM   5415 C  CG1 . VAL   B 1 355 ? 8.015   7.385   -13.812 1 63.37  ? 340 VAL   B CG1 1 
ATOM   5416 C  CG2 . VAL   B 1 355 ? 7.87    5.182   -12.611 1 63.38  ? 340 VAL   B CG2 1 
ATOM   5417 N  N   . SER   B 1 356 ? 10.765  8.483   -11.305 1 61.96  ? 341 SER   B N   1 
ATOM   5418 C  CA  . SER   B 1 356 ? 11.382  9.789   -11.135 1 62.88  ? 341 SER   B CA  1 
ATOM   5419 C  C   . SER   B 1 356 ? 12.866  9.795   -11.562 1 63.65  ? 341 SER   B C   1 
ATOM   5420 O  O   . SER   B 1 356 ? 13.306  10.726  -12.248 1 64.17  ? 341 SER   B O   1 
ATOM   5421 C  CB  . SER   B 1 356 ? 11.239  10.258  -9.696  1 64.04  ? 341 SER   B CB  1 
ATOM   5422 O  OG  . SER   B 1 356 ? 9.866   10.457  -9.412  1 66.39  ? 341 SER   B OG  1 
ATOM   5423 N  N   . LEU   B 1 357 ? 13.617  8.747   -11.184 1 63.2   ? 342 LEU   B N   1 
ATOM   5424 C  CA  . LEU   B 1 357 ? 15.022  8.615   -11.551 1 63.25  ? 342 LEU   B CA  1 
ATOM   5425 C  C   . LEU   B 1 357 ? 15.162  8.507   -13.064 1 63.38  ? 342 LEU   B C   1 
ATOM   5426 O  O   . LEU   B 1 357 ? 15.968  9.216   -13.661 1 63.76  ? 342 LEU   B O   1 
ATOM   5427 C  CB  . LEU   B 1 357 ? 15.621  7.372   -10.892 1 63.44  ? 342 LEU   B CB  1 
ATOM   5428 C  CG  . LEU   B 1 357 ? 16.166  7.563   -9.508  1 65.47  ? 342 LEU   B CG  1 
ATOM   5429 C  CD1 . LEU   B 1 357 ? 16.313  6.234   -8.818  1 66.22  ? 342 LEU   B CD1 1 
ATOM   5430 C  CD2 . LEU   B 1 357 ? 17.511  8.271   -9.555  1 66.52  ? 342 LEU   B CD2 1 
ATOM   5431 N  N   . ARG   B 1 358 ? 14.35   7.654   -13.685 1 63.19  ? 343 ARG   B N   1 
ATOM   5432 C  CA  . ARG   B 1 358 ? 14.406  7.424   -15.124 1 63.71  ? 343 ARG   B CA  1 
ATOM   5433 C  C   . ARG   B 1 358 ? 13.924  8.615   -15.949 1 64.59  ? 343 ARG   B C   1 
ATOM   5434 O  O   . ARG   B 1 358 ? 14.387  8.811   -17.073 1 64.37  ? 343 ARG   B O   1 
ATOM   5435 C  CB  . ARG   B 1 358 ? 13.656  6.136   -15.49  1 63.82  ? 343 ARG   B CB  1 
ATOM   5436 C  CG  . ARG   B 1 358 ? 14.316  4.927   -14.861 1 64.77  ? 343 ARG   B CG  1 
ATOM   5437 C  CD  . ARG   B 1 358 ? 13.773  3.62    -15.385 1 65.94  ? 343 ARG   B CD  1 
ATOM   5438 N  NE  . ARG   B 1 358 ? 14.76   2.556   -15.216 1 66.1   ? 343 ARG   B NE  1 
ATOM   5439 C  CZ  . ARG   B 1 358 ? 14.607  1.51    -14.417 1 66.99  ? 343 ARG   B CZ  1 
ATOM   5440 N  NH1 . ARG   B 1 358 ? 13.483  1.347   -13.732 1 67.49  ? 343 ARG   B NH1 1 
ATOM   5441 N  NH2 . ARG   B 1 358 ? 15.562  0.6     -14.319 1 66.19  ? 343 ARG   B NH2 1 
ATOM   5442 N  N   . SER   B 1 359 ? 13.015  9.416   -15.384 1 65.1   ? 344 SER   B N   1 
ATOM   5443 C  CA  . SER   B 1 359 ? 12.5    10.613  -16.033 1 65.85  ? 344 SER   B CA  1 
ATOM   5444 C  C   . SER   B 1 359 ? 13.528  11.737  -15.964 1 66.84  ? 344 SER   B C   1 
ATOM   5445 O  O   . SER   B 1 359 ? 13.662  12.497  -16.921 1 66.93  ? 344 SER   B O   1 
ATOM   5446 C  CB  . SER   B 1 359 ? 11.191  11.047  -15.389 1 66.26  ? 344 SER   B CB  1 
ATOM   5447 O  OG  . SER   B 1 359 ? 10.124  10.328  -15.978 1 67.84  ? 344 SER   B OG  1 
ATOM   5448 N  N   . TYR   B 1 360 ? 14.244  11.851  -14.838 1 67.39  ? 345 TYR   B N   1 
ATOM   5449 C  CA  . TYR   B 1 360 ? 15.294  12.846  -14.712 1 68.79  ? 345 TYR   B CA  1 
ATOM   5450 C  C   . TYR   B 1 360 ? 16.457  12.474  -15.654 1 69.28  ? 345 TYR   B C   1 
ATOM   5451 O  O   . TYR   B 1 360 ? 17.02   13.345  -16.319 1 69.88  ? 345 TYR   B O   1 
ATOM   5452 C  CB  . TYR   B 1 360 ? 15.782  12.927  -13.272 1 69.73  ? 345 TYR   B CB  1 
ATOM   5453 C  CG  . TYR   B 1 360 ? 16.751  14.063  -13.061 1 72.33  ? 345 TYR   B CG  1 
ATOM   5454 C  CD1 . TYR   B 1 360 ? 16.302  15.368  -12.915 1 74.25  ? 345 TYR   B CD1 1 
ATOM   5455 C  CD2 . TYR   B 1 360 ? 18.117  13.835  -13.015 1 74.23  ? 345 TYR   B CD2 1 
ATOM   5456 C  CE1 . TYR   B 1 360 ? 17.19   16.421  -12.731 1 75.9   ? 345 TYR   B CE1 1 
ATOM   5457 C  CE2 . TYR   B 1 360 ? 19.018  14.878  -12.824 1 75.84  ? 345 TYR   B CE2 1 
ATOM   5458 C  CZ  . TYR   B 1 360 ? 18.551  16.174  -12.69  1 77.2   ? 345 TYR   B CZ  1 
ATOM   5459 O  OH  . TYR   B 1 360 ? 19.434  17.215  -12.501 1 79.3   ? 345 TYR   B OH  1 
ATOM   5460 N  N   . HIS   B 1 361 ? 16.787  11.172  -15.73  1 68.51  ? 346 HIS   B N   1 
ATOM   5461 C  CA  . HIS   B 1 361 ? 17.821  10.632  -16.592 1 67.88  ? 346 HIS   B CA  1 
ATOM   5462 C  C   . HIS   B 1 361 ? 17.524  10.952  -18.058 1 68.02  ? 346 HIS   B C   1 
ATOM   5463 O  O   . HIS   B 1 361 ? 18.439  11.325  -18.772 1 68.41  ? 346 HIS   B O   1 
ATOM   5464 C  CB  . HIS   B 1 361 ? 17.917  9.121   -16.362 1 67.78  ? 346 HIS   B CB  1 
ATOM   5465 C  CG  . HIS   B 1 361 ? 18.956  8.419   -17.173 1 68.15  ? 346 HIS   B CG  1 
ATOM   5466 N  ND1 . HIS   B 1 361 ? 18.628  7.759   -18.34  1 69.53  ? 346 HIS   B ND1 1 
ATOM   5467 C  CD2 . HIS   B 1 361 ? 20.272  8.234   -16.922 1 68.56  ? 346 HIS   B CD2 1 
ATOM   5468 C  CE1 . HIS   B 1 361 ? 19.758  7.233   -18.784 1 69.81  ? 346 HIS   B CE1 1 
ATOM   5469 N  NE2 . HIS   B 1 361 ? 20.773  7.493   -17.961 1 69.43  ? 346 HIS   B NE2 1 
ATOM   5470 N  N   . LEU   B 1 362 ? 16.255  10.869  -18.496 1 67.79  ? 347 LEU   B N   1 
ATOM   5471 C  CA  . LEU   B 1 362 ? 15.852  11.192  -19.877 1 68.22  ? 347 LEU   B CA  1 
ATOM   5472 C  C   . LEU   B 1 362 ? 16.104  12.664  -20.221 1 68.26  ? 347 LEU   B C   1 
ATOM   5473 O  O   . LEU   B 1 362 ? 16.437  12.986  -21.361 1 67.84  ? 347 LEU   B O   1 
ATOM   5474 C  CB  . LEU   B 1 362 ? 14.364  10.88   -20.097 1 68.48  ? 347 LEU   B CB  1 
ATOM   5475 C  CG  . LEU   B 1 362 ? 14.056  9.485   -20.564 1 70.36  ? 347 LEU   B CG  1 
ATOM   5476 C  CD1 . LEU   B 1 362 ? 12.617  9.12    -20.29  1 71.1   ? 347 LEU   B CD1 1 
ATOM   5477 C  CD2 . LEU   B 1 362 ? 14.403  9.306   -22.02  1 71.04  ? 347 LEU   B CD2 1 
ATOM   5478 N  N   . GLN   B 1 363 ? 15.92   13.551  -19.235 1 68.53  ? 348 GLN   B N   1 
ATOM   5479 C  CA  . GLN   B 1 363 ? 16.165  14.979  -19.405 1 69.41  ? 348 GLN   B CA  1 
ATOM   5480 C  C   . GLN   B 1 363 ? 17.664  15.246  -19.536 1 70.19  ? 348 GLN   B C   1 
ATOM   5481 O  O   . GLN   B 1 363 ? 18.065  16.078  -20.35  1 71.02  ? 348 GLN   B O   1 
ATOM   5482 C  CB  . GLN   B 1 363 ? 15.566  15.765  -18.242 1 71.08  ? 348 GLN   B CB  1 
ATOM   5483 C  CG  . GLN   B 1 363 ? 14.059  15.979  -18.394 1 74.7   ? 348 GLN   B CG  1 
ATOM   5484 C  CD  . GLN   B 1 363 ? 13.366  16.192  -17.072 1 80.15  ? 348 GLN   B CD  1 
ATOM   5485 O  OE1 . GLN   B 1 363 ? 12.274  15.657  -16.832 1 81.03  ? 348 GLN   B OE1 1 
ATOM   5486 N  NE2 . GLN   B 1 363 ? 13.995  16.959  -16.173 1 81.66  ? 348 GLN   B NE2 1 
ATOM   5487 N  N   . ILE   B 1 364 ? 18.489  14.511  -18.766 1 69.58  ? 349 ILE   B N   1 
ATOM   5488 C  CA  . ILE   B 1 364 ? 19.938  14.58   -18.831 1 69.4   ? 349 ILE   B CA  1 
ATOM   5489 C  C   . ILE   B 1 364 ? 20.396  14.093  -20.221 1 69.42  ? 349 ILE   B C   1 
ATOM   5490 O  O   . ILE   B 1 364 ? 21.174  14.772  -20.876 1 69.81  ? 349 ILE   B O   1 
ATOM   5491 C  CB  . ILE   B 1 364 ? 20.554  13.711  -17.698 1 69.99  ? 349 ILE   B CB  1 
ATOM   5492 C  CG1 . ILE   B 1 364 ? 20.204  14.257  -16.297 1 70.73  ? 349 ILE   B CG1 1 
ATOM   5493 C  CG2 . ILE   B 1 364 ? 22.065  13.547  -17.876 1 70.61  ? 349 ILE   B CG2 1 
ATOM   5494 C  CD1 . ILE   B 1 364 ? 20.621  15.667  -16.052 1 71.77  ? 349 ILE   B CD1 1 
ATOM   5495 N  N   . VAL   B 1 365 ? 19.87   12.95   -20.694 1 68.69  ? 350 VAL   B N   1 
ATOM   5496 C  CA  . VAL   B 1 365 ? 20.218  12.389  -22     1 68.26  ? 350 VAL   B CA  1 
ATOM   5497 C  C   . VAL   B 1 365 ? 19.783  13.315  -23.154 1 68.59  ? 350 VAL   B C   1 
ATOM   5498 O  O   . VAL   B 1 365 ? 20.422  13.318  -24.203 1 68.83  ? 350 VAL   B O   1 
ATOM   5499 C  CB  . VAL   B 1 365 ? 19.693  10.937  -22.142 1 68.3   ? 350 VAL   B CB  1 
ATOM   5500 C  CG1 . VAL   B 1 365 ? 19.933  10.378  -23.536 1 68.55  ? 350 VAL   B CG1 1 
ATOM   5501 C  CG2 . VAL   B 1 365 ? 20.321  10.026  -21.102 1 68.49  ? 350 VAL   B CG2 1 
ATOM   5502 N  N   . THR   B 1 366 ? 18.744  14.143  -22.95  1 68.69  ? 351 THR   B N   1 
ATOM   5503 C  CA  . THR   B 1 366 ? 18.3    15.103  -23.967 1 69.14  ? 351 THR   B CA  1 
ATOM   5504 C  C   . THR   B 1 366 ? 19.343  16.233  -24.089 1 69.09  ? 351 THR   B C   1 
ATOM   5505 O  O   . THR   B 1 366 ? 19.741  16.599  -25.193 1 68.58  ? 351 THR   B O   1 
ATOM   5506 C  CB  . THR   B 1 366 ? 16.901  15.638  -23.607 1 70.48  ? 351 THR   B CB  1 
ATOM   5507 O  OG1 . THR   B 1 366 ? 15.964  14.559  -23.605 1 71.66  ? 351 THR   B OG1 1 
ATOM   5508 C  CG2 . THR   B 1 366 ? 16.416  16.703  -24.57  1 70.42  ? 351 THR   B CG2 1 
ATOM   5509 N  N   . LYS   B 1 367 ? 19.813  16.736  -22.941 1 69.57  ? 352 LYS   B N   1 
ATOM   5510 C  CA  . LYS   B 1 367 ? 20.829  17.785  -22.853 1 70.79  ? 352 LYS   B CA  1 
ATOM   5511 C  C   . LYS   B 1 367 ? 22.218  17.321  -23.342 1 71.97  ? 352 LYS   B C   1 
ATOM   5512 O  O   . LYS   B 1 367 ? 22.924  18.092  -23.987 1 72.67  ? 352 LYS   B O   1 
ATOM   5513 C  CB  . LYS   B 1 367 ? 20.93   18.285  -21.394 1 72.74  ? 352 LYS   B CB  1 
ATOM   5514 C  CG  . LYS   B 1 367 ? 22.12   19.223  -21.102 1 77.37  ? 352 LYS   B CG  1 
ATOM   5515 C  CD  . LYS   B 1 367 ? 22.239  19.608  -19.62  1 82.03  ? 352 LYS   B CD  1 
ATOM   5516 C  CE  . LYS   B 1 367 ? 23.51   20.371  -19.307 1 85.45  ? 352 LYS   B CE  1 
ATOM   5517 N  NZ  . LYS   B 1 367 ? 23.631  20.676  -17.853 1 87.74  ? 352 LYS   B NZ  1 
ATOM   5518 N  N   . TYR   B 1 368 ? 22.617  16.087  -23.009 1 72.16  ? 353 TYR   B N   1 
ATOM   5519 C  CA  . TYR   B 1 368 ? 23.947  15.56   -23.309 1 72.85  ? 353 TYR   B CA  1 
ATOM   5520 C  C   . TYR   B 1 368 ? 24.086  14.752  -24.586 1 73.7   ? 353 TYR   B C   1 
ATOM   5521 O  O   . TYR   B 1 368 ? 25.22   14.554  -25.043 1 74.11  ? 353 TYR   B O   1 
ATOM   5522 C  CB  . TYR   B 1 368 ? 24.462  14.719  -22.133 1 72.77  ? 353 TYR   B CB  1 
ATOM   5523 C  CG  . TYR   B 1 368 ? 24.876  15.559  -20.952 1 73.25  ? 353 TYR   B CG  1 
ATOM   5524 C  CD1 . TYR   B 1 368 ? 23.963  15.911  -19.971 1 73.98  ? 353 TYR   B CD1 1 
ATOM   5525 C  CD2 . TYR   B 1 368 ? 26.175  16.019  -20.826 1 74.21  ? 353 TYR   B CD2 1 
ATOM   5526 C  CE1 . TYR   B 1 368 ? 24.326  16.713  -18.905 1 74.92  ? 353 TYR   B CE1 1 
ATOM   5527 C  CE2 . TYR   B 1 368 ? 26.55   16.826  -19.767 1 75.11  ? 353 TYR   B CE2 1 
ATOM   5528 C  CZ  . TYR   B 1 368 ? 25.621  17.171  -18.805 1 75.94  ? 353 TYR   B CZ  1 
ATOM   5529 O  OH  . TYR   B 1 368 ? 25.988  17.942  -17.733 1 77.42  ? 353 TYR   B OH  1 
ATOM   5530 N  N   . ILE   B 1 369 ? 22.984  14.226  -25.133 1 73.93  ? 354 ILE   B N   1 
ATOM   5531 C  CA  . ILE   B 1 369 ? 23.077  13.407  -26.341 1 75     ? 354 ILE   B CA  1 
ATOM   5532 C  C   . ILE   B 1 369 ? 22.18   13.916  -27.462 1 76.04  ? 354 ILE   B C   1 
ATOM   5533 O  O   . ILE   B 1 369 ? 22.669  14.162  -28.563 1 76.39  ? 354 ILE   B O   1 
ATOM   5534 C  CB  . ILE   B 1 369 ? 22.858  11.891  -26.058 1 75.66  ? 354 ILE   B CB  1 
ATOM   5535 C  CG1 . ILE   B 1 369 ? 23.965  11.332  -25.124 1 76.76  ? 354 ILE   B CG1 1 
ATOM   5536 C  CG2 . ILE   B 1 369 ? 22.8    11.091  -27.371 1 76.05  ? 354 ILE   B CG2 1 
ATOM   5537 C  CD1 . ILE   B 1 369 ? 23.788  9.916   -24.703 1 77.9   ? 354 ILE   B CD1 1 
ATOM   5538 N  N   . LEU   B 1 370 ? 20.884  14.067  -27.197 1 76.37  ? 355 LEU   B N   1 
ATOM   5539 C  CA  . LEU   B 1 370 ? 19.929  14.498  -28.206 1 76.99  ? 355 LEU   B CA  1 
ATOM   5540 C  C   . LEU   B 1 370 ? 20.252  15.874  -28.835 1 77.54  ? 355 LEU   B C   1 
ATOM   5541 O  O   . LEU   B 1 370 ? 20.316  15.998  -30.06  1 77.27  ? 355 LEU   B O   1 
ATOM   5542 C  CB  . LEU   B 1 370 ? 18.52   14.474  -27.588 1 77.08  ? 355 LEU   B CB  1 
ATOM   5543 C  CG  . LEU   B 1 370 ? 17.342  14.112  -28.486 1 78.27  ? 355 LEU   B CG  1 
ATOM   5544 C  CD1 . LEU   B 1 370 ? 16.877  15.294  -29.293 1 78.79  ? 355 LEU   B CD1 1 
ATOM   5545 C  CD2 . LEU   B 1 370 ? 17.605  12.869  -29.331 1 78.56  ? 355 LEU   B CD2 1 
ATOM   5546 N  N   . ILE   B 1 371 ? 20.431  16.891  -27.999 1 78.21  ? 356 ILE   B N   1 
ATOM   5547 C  CA  . ILE   B 1 371 ? 20.705  18.241  -28.46  1 79.38  ? 356 ILE   B CA  1 
ATOM   5548 C  C   . ILE   B 1 371 ? 22.109  18.351  -29.097 1 80.92  ? 356 ILE   B C   1 
ATOM   5549 O  O   . ILE   B 1 371 ? 22.172  18.812  -30.241 1 81.42  ? 356 ILE   B O   1 
ATOM   5550 C  CB  . ILE   B 1 371 ? 20.423  19.268  -27.343 1 79.58  ? 356 ILE   B CB  1 
ATOM   5551 C  CG1 . ILE   B 1 371 ? 18.906  19.341  -27.083 1 79.84  ? 356 ILE   B CG1 1 
ATOM   5552 C  CG2 . ILE   B 1 371 ? 21.007  20.637  -27.681 1 80.25  ? 356 ILE   B CG2 1 
ATOM   5553 C  CD1 . ILE   B 1 371 ? 18.533  20.001  -25.859 1 80.86  ? 356 ILE   B CD1 1 
ATOM   5554 N  N   . PRO   B 1 372 ? 23.215  17.841  -28.493 1 81.28  ? 357 PRO   B N   1 
ATOM   5555 C  CA  . PRO   B 1 372 ? 24.516  17.89   -29.187 1 81.6   ? 357 PRO   B CA  1 
ATOM   5556 C  C   . PRO   B 1 372 ? 24.513  17.198  -30.545 1 82.07  ? 357 PRO   B C   1 
ATOM   5557 O  O   . PRO   B 1 372 ? 25.264  17.613  -31.422 1 82.42  ? 357 PRO   B O   1 
ATOM   5558 C  CB  . PRO   B 1 372 ? 25.461  17.167  -28.227 1 82.27  ? 357 PRO   B CB  1 
ATOM   5559 C  CG  . PRO   B 1 372 ? 24.842  17.356  -26.911 1 82.64  ? 357 PRO   B CG  1 
ATOM   5560 C  CD  . PRO   B 1 372 ? 23.366  17.247  -27.156 1 80.89  ? 357 PRO   B CD  1 
ATOM   5561 N  N   . ALA   B 1 373 ? 23.668  16.168  -30.735 1 82.01  ? 358 ALA   B N   1 
ATOM   5562 C  CA  . ALA   B 1 373 ? 23.569  15.478  -32.022 1 82.6   ? 358 ALA   B CA  1 
ATOM   5563 C  C   . ALA   B 1 373 ? 22.964  16.379  -33.108 1 82.99  ? 358 ALA   B C   1 
ATOM   5564 O  O   . ALA   B 1 373 ? 23.321  16.252  -34.279 1 83.38  ? 358 ALA   B O   1 
ATOM   5565 C  CB  . ALA   B 1 373 ? 22.755  14.201  -31.879 1 82.78  ? 358 ALA   B CB  1 
ATOM   5566 N  N   . SER   B 1 374 ? 22.066  17.297  -32.713 1 82.71  ? 359 SER   B N   1 
ATOM   5567 C  CA  . SER   B 1 374 ? 21.425  18.256  -33.61  1 82.93  ? 359 SER   B CA  1 
ATOM   5568 C  C   . SER   B 1 374 ? 22.316  19.471  -33.945 1 83.61  ? 359 SER   B C   1 
ATOM   5569 O  O   . SER   B 1 374 ? 22.019  20.196  -34.894 1 84.1   ? 359 SER   B O   1 
ATOM   5570 C  CB  . SER   B 1 374 ? 20.127  18.751  -32.994 1 83.31  ? 359 SER   B CB  1 
ATOM   5571 O  OG  . SER   B 1 374 ? 20.371  19.477  -31.803 1 84.59  ? 359 SER   B OG  1 
ATOM   5572 N  N   . GLN   B 1 375 ? 23.376  19.716  -33.153 1 83.41  ? 360 GLN   B N   1 
ATOM   5573 C  CA  . GLN   B 1 375 ? 24.3    20.833  -33.362 1 83.45  ? 360 GLN   B CA  1 
ATOM   5574 C  C   . GLN   B 1 375 ? 25.642  20.368  -33.955 1 83.31  ? 360 GLN   B C   1 
ATOM   5575 O  O   . GLN   B 1 375 ? 25.759  19.304  -34.567 1 83.11  ? 360 GLN   B O   1 
ATOM   5576 C  CB  . GLN   B 1 375 ? 24.539  21.587  -32.041 1 84.74  ? 360 GLN   B CB  1 
ATOM   5577 N  N   . GLY   B 1 396 ? 21.256  7.457   -31.194 1 83.87  ? 381 GLY   B N   1 
ATOM   5578 C  CA  . GLY   B 1 396 ? 20.837  8.807   -30.824 1 84.43  ? 381 GLY   B CA  1 
ATOM   5579 C  C   . GLY   B 1 396 ? 19.349  8.88    -30.537 1 84.74  ? 381 GLY   B C   1 
ATOM   5580 O  O   . GLY   B 1 396 ? 18.931  9.049   -29.386 1 84.86  ? 381 GLY   B O   1 
ATOM   5581 N  N   . THR   B 1 397 ? 18.531  8.747   -31.587 1 84.39  ? 382 THR   B N   1 
ATOM   5582 C  CA  . THR   B 1 397 ? 17.077  8.702   -31.41  1 84.3   ? 382 THR   B CA  1 
ATOM   5583 C  C   . THR   B 1 397 ? 16.672  7.319   -30.843 1 83.92  ? 382 THR   B C   1 
ATOM   5584 O  O   . THR   B 1 397 ? 15.672  7.222   -30.128 1 84.62  ? 382 THR   B O   1 
ATOM   5585 C  CB  . THR   B 1 397 ? 16.347  9.019   -32.722 1 85.34  ? 382 THR   B CB  1 
ATOM   5586 N  N   . ASP   B 1 398 ? 17.45   6.254   -31.158 1 82.43  ? 383 ASP   B N   1 
ATOM   5587 C  CA  . ASP   B 1 398 ? 17.221  4.895   -30.682 1 81.13  ? 383 ASP   B CA  1 
ATOM   5588 C  C   . ASP   B 1 398 ? 17.446  4.794   -29.175 1 79.11  ? 383 ASP   B C   1 
ATOM   5589 O  O   . ASP   B 1 398 ? 16.724  4.063   -28.499 1 79.08  ? 383 ASP   B O   1 
ATOM   5590 C  CB  . ASP   B 1 398 ? 18.144  3.92    -31.411 1 83.21  ? 383 ASP   B CB  1 
ATOM   5591 C  CG  . ASP   B 1 398 ? 17.377  2.948   -32.264 1 88.5   ? 383 ASP   B CG  1 
ATOM   5592 O  OD1 . ASP   B 1 398 ? 17.778  1.768   -32.326 1 89.64  ? 383 ASP   B OD1 1 
ATOM   5593 O  OD2 . ASP   B 1 398 ? 16.362  3.358   -32.853 1 91.08  ? 383 ASP   B OD2 1 
ATOM   5594 N  N   . LEU   B 1 399 ? 18.445  5.529   -28.647 1 77.25  ? 384 LEU   B N   1 
ATOM   5595 C  CA  . LEU   B 1 399 ? 18.722  5.541   -27.208 1 75.96  ? 384 LEU   B CA  1 
ATOM   5596 C  C   . LEU   B 1 399 ? 17.561  6.178   -26.441 1 74.68  ? 384 LEU   B C   1 
ATOM   5597 O  O   . LEU   B 1 399 ? 17.287  5.79    -25.309 1 74.88  ? 384 LEU   B O   1 
ATOM   5598 C  CB  . LEU   B 1 399 ? 20.034  6.291   -26.874 1 75.92  ? 384 LEU   B CB  1 
ATOM   5599 C  CG  . LEU   B 1 399 ? 21.27   6.031   -27.741 1 76.96  ? 384 LEU   B CG  1 
ATOM   5600 C  CD1 . LEU   B 1 399 ? 22.31   7.059   -27.477 1 77.33  ? 384 LEU   B CD1 1 
ATOM   5601 C  CD2 . LEU   B 1 399 ? 21.866  4.645   -27.486 1 77.48  ? 384 LEU   B CD2 1 
ATOM   5602 N  N   . MET   B 1 400 ? 16.88   7.159   -27.053 1 73.43  ? 385 MET   B N   1 
ATOM   5603 C  CA  . MET   B 1 400 ? 15.727  7.801   -26.445 1 72.91  ? 385 MET   B CA  1 
ATOM   5604 C  C   . MET   B 1 400 ? 14.604  6.788   -26.301 1 72.04  ? 385 MET   B C   1 
ATOM   5605 O  O   . MET   B 1 400 ? 13.993  6.708   -25.249 1 72.27  ? 385 MET   B O   1 
ATOM   5606 C  CB  . MET   B 1 400 ? 15.23   9       -27.286 1 73.54  ? 385 MET   B CB  1 
ATOM   5607 C  CG  . MET   B 1 400 ? 16.03   10.284  -27.151 1 75.26  ? 385 MET   B CG  1 
ATOM   5608 S  SD  . MET   B 1 400 ? 16.757  10.628  -25.538 1 77.66  ? 385 MET   B SD  1 
ATOM   5609 C  CE  . MET   B 1 400 ? 15.425  11.501  -24.692 1 74.65  ? 385 MET   B CE  1 
ATOM   5610 N  N   . ASN   B 1 401 ? 14.355  5.996   -27.345 1 70.86  ? 386 ASN   B N   1 
ATOM   5611 C  CA  . ASN   B 1 401 ? 13.317  4.976   -27.341 1 70.23  ? 386 ASN   B CA  1 
ATOM   5612 C  C   . ASN   B 1 401 ? 13.61   3.877   -26.343 1 68.5   ? 386 ASN   B C   1 
ATOM   5613 O  O   . ASN   B 1 401 ? 12.688  3.375   -25.701 1 68.77  ? 386 ASN   B O   1 
ATOM   5614 C  CB  . ASN   B 1 401 ? 13.14   4.382   -28.737 1 72.23  ? 386 ASN   B CB  1 
ATOM   5615 C  CG  . ASN   B 1 401 ? 12.635  5.386   -29.737 1 76.72  ? 386 ASN   B CG  1 
ATOM   5616 O  OD1 . ASN   B 1 401 ? 11.894  6.321   -29.395 1 78.29  ? 386 ASN   B OD1 1 
ATOM   5617 N  ND2 . ASN   B 1 401 ? 13.031  5.219   -30.995 1 77.8   ? 386 ASN   B ND2 1 
ATOM   5618 N  N   . PHE   B 1 402 ? 14.886  3.495   -26.205 1 66.86  ? 387 PHE   B N   1 
ATOM   5619 C  CA  . PHE   B 1 402 ? 15.284  2.454   -25.255 1 65.43  ? 387 PHE   B CA  1 
ATOM   5620 C  C   . PHE   B 1 402 ? 14.964  2.915   -23.829 1 64.49  ? 387 PHE   B C   1 
ATOM   5621 O  O   . PHE   B 1 402 ? 14.33   2.177   -23.076 1 65.48  ? 387 PHE   B O   1 
ATOM   5622 C  CB  . PHE   B 1 402 ? 16.789  2.085   -25.401 1 64.51  ? 387 PHE   B CB  1 
ATOM   5623 C  CG  . PHE   B 1 402 ? 17.32   1.298   -24.219 1 64.35  ? 387 PHE   B CG  1 
ATOM   5624 C  CD1 . PHE   B 1 402 ? 16.956  -0.024  -24.025 1 64.89  ? 387 PHE   B CD1 1 
ATOM   5625 C  CD2 . PHE   B 1 402 ? 18.106  1.909   -23.255 1 64.53  ? 387 PHE   B CD2 1 
ATOM   5626 C  CE1 . PHE   B 1 402 ? 17.38   -0.723  -22.898 1 65.36  ? 387 PHE   B CE1 1 
ATOM   5627 C  CE2 . PHE   B 1 402 ? 18.524  1.212   -22.129 1 64.88  ? 387 PHE   B CE2 1 
ATOM   5628 C  CZ  . PHE   B 1 402 ? 18.165  -0.1    -21.959 1 64.81  ? 387 PHE   B CZ  1 
ATOM   5629 N  N   . LEU   B 1 403 ? 15.396  4.127   -23.475 1 62.49  ? 388 LEU   B N   1 
ATOM   5630 C  CA  . LEU   B 1 403 ? 15.176  4.669   -22.151 1 61.55  ? 388 LEU   B CA  1 
ATOM   5631 C  C   . LEU   B 1 403 ? 13.691  4.912   -21.879 1 60.4   ? 388 LEU   B C   1 
ATOM   5632 O  O   . LEU   B 1 403 ? 13.229  4.652   -20.772 1 60.37  ? 388 LEU   B O   1 
ATOM   5633 C  CB  . LEU   B 1 403 ? 15.981  5.955   -21.963 1 61.82  ? 388 LEU   B CB  1 
ATOM   5634 C  CG  . LEU   B 1 403 ? 17.494  5.793   -22.016 1 63.28  ? 388 LEU   B CG  1 
ATOM   5635 C  CD1 . LEU   B 1 403 ? 18.182  7.143   -22.018 1 63.33  ? 388 LEU   B CD1 1 
ATOM   5636 C  CD2 . LEU   B 1 403 ? 17.999  4.908   -20.868 1 64.13  ? 388 LEU   B CD2 1 
ATOM   5637 N  N   . LYS   B 1 404 ? 12.944  5.374   -22.889 1 59.36  ? 389 LYS   B N   1 
ATOM   5638 C  CA  . LYS   B 1 404 ? 11.51   5.62    -22.762 1 58.98  ? 389 LYS   B CA  1 
ATOM   5639 C  C   . LYS   B 1 404 ? 10.741  4.316   -22.579 1 58.95  ? 389 LYS   B C   1 
ATOM   5640 O  O   . LYS   B 1 404 ? 9.767   4.3     -21.842 1 59.24  ? 389 LYS   B O   1 
ATOM   5641 C  CB  . LYS   B 1 404 ? 10.959  6.376   -23.97  1 59.46  ? 389 LYS   B CB  1 
ATOM   5642 C  CG  . LYS   B 1 404 ? 11.224  7.863   -23.953 1 61.56  ? 389 LYS   B CG  1 
ATOM   5643 C  CD  . LYS   B 1 404 ? 10.508  8.484   -25.146 1 65.08  ? 389 LYS   B CD  1 
ATOM   5644 C  CE  . LYS   B 1 404 ? 11.34   9.437   -25.963 1 67.07  ? 389 LYS   B CE  1 
ATOM   5645 N  NZ  . LYS   B 1 404 ? 11.048  9.347   -27.421 1 67.95  ? 389 LYS   B NZ  1 
ATOM   5646 N  N   . THR   B 1 405 ? 11.176  3.227   -23.226 1 58.43  ? 390 THR   B N   1 
ATOM   5647 C  CA  . THR   B 1 405 ? 10.537  1.924   -23.067 1 58.27  ? 390 THR   B CA  1 
ATOM   5648 C  C   . THR   B 1 405 ? 10.793  1.384   -21.662 1 58.13  ? 390 THR   B C   1 
ATOM   5649 O  O   . THR   B 1 405 ? 9.881   0.836   -21.047 1 58.76  ? 390 THR   B O   1 
ATOM   5650 C  CB  . THR   B 1 405 ? 11.052  0.958   -24.124 1 59.5   ? 390 THR   B CB  1 
ATOM   5651 O  OG1 . THR   B 1 405 ? 10.592  1.404   -25.402 1 61.19  ? 390 THR   B OG1 1 
ATOM   5652 C  CG2 . THR   B 1 405 ? 10.598  -0.473  -23.876 1 59.4   ? 390 THR   B CG2 1 
ATOM   5653 N  N   . VAL   B 1 406 ? 12.022  1.56    -21.148 1 57     ? 391 VAL   B N   1 
ATOM   5654 C  CA  . VAL   B 1 406 ? 12.38   1.134   -19.805 1 56.8   ? 391 VAL   B CA  1 
ATOM   5655 C  C   . VAL   B 1 406 ? 11.569  1.932   -18.787 1 57.4   ? 391 VAL   B C   1 
ATOM   5656 O  O   . VAL   B 1 406 ? 10.995  1.341   -17.878 1 58.08  ? 391 VAL   B O   1 
ATOM   5657 C  CB  . VAL   B 1 406 ? 13.915  1.231   -19.567 1 56.69  ? 391 VAL   B CB  1 
ATOM   5658 C  CG1 . VAL   B 1 406 ? 14.257  1.149   -18.088 1 56.54  ? 391 VAL   B CG1 1 
ATOM   5659 C  CG2 . VAL   B 1 406 ? 14.656  0.149   -20.35  1 57.09  ? 391 VAL   B CG2 1 
ATOM   5660 N  N   . ARG   B 1 407 ? 11.461  3.255   -18.976 1 57.37  ? 392 ARG   B N   1 
ATOM   5661 C  CA  . ARG   B 1 407 ? 10.697  4.107   -18.076 1 58.04  ? 392 ARG   B CA  1 
ATOM   5662 C  C   . ARG   B 1 407 ? 9.199   3.791   -18.126 1 57.94  ? 392 ARG   B C   1 
ATOM   5663 O  O   . ARG   B 1 407 ? 8.563   3.713   -17.082 1 57.87  ? 392 ARG   B O   1 
ATOM   5664 C  CB  . ARG   B 1 407 ? 10.929  5.586   -18.39  1 60.41  ? 392 ARG   B CB  1 
ATOM   5665 C  CG  . ARG   B 1 407 ? 10.217  6.492   -17.395 1 64.41  ? 392 ARG   B CG  1 
ATOM   5666 C  CD  . ARG   B 1 407 ? 9.978   7.889   -17.882 1 67.83  ? 392 ARG   B CD  1 
ATOM   5667 N  NE  . ARG   B 1 407 ? 9.327   7.984   -19.185 1 71.24  ? 392 ARG   B NE  1 
ATOM   5668 C  CZ  . ARG   B 1 407 ? 9.066   9.138   -19.799 1 73.7   ? 392 ARG   B CZ  1 
ATOM   5669 N  NH1 . ARG   B 1 407 ? 9.387   10.293  -19.224 1 72.36  ? 392 ARG   B NH1 1 
ATOM   5670 N  NH2 . ARG   B 1 407 ? 8.491   9.146   -20.996 1 74.2   ? 392 ARG   B NH2 1 
ATOM   5671 N  N   . SER   B 1 408 ? 8.65    3.564   -19.328 1 57.88  ? 393 SER   B N   1 
ATOM   5672 C  CA  . SER   B 1 408 ? 7.235   3.245   -19.517 1 58.16  ? 393 SER   B CA  1 
ATOM   5673 C  C   . SER   B 1 408 ? 6.874   1.936   -18.804 1 58.91  ? 393 SER   B C   1 
ATOM   5674 O  O   . SER   B 1 408 ? 5.832   1.861   -18.144 1 59.16  ? 393 SER   B O   1 
ATOM   5675 C  CB  . SER   B 1 408 ? 6.887   3.17    -20.999 1 58.68  ? 393 SER   B CB  1 
ATOM   5676 N  N   . THR   B 1 409 ? 7.756   0.928   -18.899 1 58.62  ? 394 THR   B N   1 
ATOM   5677 C  CA  . THR   B 1 409 ? 7.578   -0.359  -18.223 1 58.75  ? 394 THR   B CA  1 
ATOM   5678 C  C   . THR   B 1 409 ? 7.547   -0.162  -16.692 1 59.14  ? 394 THR   B C   1 
ATOM   5679 O  O   . THR   B 1 409 ? 6.789   -0.837  -16.004 1 59.85  ? 394 THR   B O   1 
ATOM   5680 C  CB  . THR   B 1 409 ? 8.679   -1.328  -18.661 1 59.36  ? 394 THR   B CB  1 
ATOM   5681 O  OG1 . THR   B 1 409 ? 8.655   -1.437  -20.088 1 59.56  ? 394 THR   B OG1 1 
ATOM   5682 C  CG2 . THR   B 1 409 ? 8.549   -2.706  -18.015 1 59.71  ? 394 THR   B CG2 1 
ATOM   5683 N  N   . THR   B 1 410 ? 8.336   0.784   -16.17  1 58.46  ? 395 THR   B N   1 
ATOM   5684 C  CA  . THR   B 1 410 ? 8.348   1.078   -14.743 1 58.3   ? 395 THR   B CA  1 
ATOM   5685 C  C   . THR   B 1 410 ? 7.045   1.764   -14.352 1 59.71  ? 395 THR   B C   1 
ATOM   5686 O  O   . THR   B 1 410 ? 6.452   1.421   -13.334 1 59.85  ? 395 THR   B O   1 
ATOM   5687 C  CB  . THR   B 1 410 ? 9.544   1.964   -14.374 1 57.53  ? 395 THR   B CB  1 
ATOM   5688 O  OG1 . THR   B 1 410 ? 10.73   1.443   -14.969 1 57.58  ? 395 THR   B OG1 1 
ATOM   5689 C  CG2 . THR   B 1 410 ? 9.719   2.095   -12.872 1 57.22  ? 395 THR   B CG2 1 
ATOM   5690 N  N   . GLU   B 1 411 ? 6.592   2.729   -15.163 1 60.46  ? 396 GLU   B N   1 
ATOM   5691 C  CA  . GLU   B 1 411 ? 5.366   3.464   -14.883 1 61.64  ? 396 GLU   B CA  1 
ATOM   5692 C  C   . GLU   B 1 411 ? 4.148   2.546   -14.89  1 62.29  ? 396 GLU   B C   1 
ATOM   5693 O  O   . GLU   B 1 411 ? 3.312   2.625   -13.993 1 62.32  ? 396 GLU   B O   1 
ATOM   5694 C  CB  . GLU   B 1 411 ? 5.192   4.626   -15.88  1 63.99  ? 396 GLU   B CB  1 
ATOM   5695 N  N   . LYS   B 1 412 ? 4.076   1.642   -15.876 1 62.7   ? 397 LYS   B N   1 
ATOM   5696 C  CA  . LYS   B 1 412 ? 2.971   0.696   -16.012 1 63.55  ? 397 LYS   B CA  1 
ATOM   5697 C  C   . LYS   B 1 412 ? 2.894   -0.335  -14.862 1 65.06  ? 397 LYS   B C   1 
ATOM   5698 O  O   . LYS   B 1 412 ? 1.88    -1.018  -14.732 1 65.96  ? 397 LYS   B O   1 
ATOM   5699 C  CB  . LYS   B 1 412 ? 2.999   0.014   -17.386 1 64.62  ? 397 LYS   B CB  1 
ATOM   5700 N  N   . SER   B 1 413 ? 3.936   -0.427  -14.018 1 65.14  ? 398 SER   B N   1 
ATOM   5701 C  CA  . SER   B 1 413 ? 3.959   -1.314  -12.856 1 65.71  ? 398 SER   B CA  1 
ATOM   5702 C  C   . SER   B 1 413 ? 3.234   -0.718  -11.636 1 66.96  ? 398 SER   B C   1 
ATOM   5703 O  O   . SER   B 1 413 ? 3.09    -1.409  -10.626 1 67.57  ? 398 SER   B O   1 
ATOM   5704 C  CB  . SER   B 1 413 ? 5.395   -1.642  -12.459 1 66.4   ? 398 SER   B CB  1 
ATOM   5705 O  OG  . SER   B 1 413 ? 6.088   -2.268  -13.523 1 68.41  ? 398 SER   B OG  1 
ATOM   5706 N  N   . LEU   B 1 414 ? 2.824   0.56    -11.691 1 67.17  ? 399 LEU   B N   1 
ATOM   5707 C  CA  . LEU   B 1 414 ? 2.11    1.182   -10.58  1 67.94  ? 399 LEU   B CA  1 
ATOM   5708 C  C   . LEU   B 1 414 ? 0.763   0.481   -10.382 1 69.13  ? 399 LEU   B C   1 
ATOM   5709 O  O   . LEU   B 1 414 ? 0.094   0.138   -11.361 1 69.41  ? 399 LEU   B O   1 
ATOM   5710 C  CB  . LEU   B 1 414 ? 1.909   2.689   -10.831 1 67.44  ? 399 LEU   B CB  1 
ATOM   5711 C  CG  . LEU   B 1 414 ? 3.16    3.533   -10.616 1 68.04  ? 399 LEU   B CG  1 
ATOM   5712 C  CD1 . LEU   B 1 414 ? 3.034   4.88    -11.266 1 68.33  ? 399 LEU   B CD1 1 
ATOM   5713 C  CD2 . LEU   B 1 414 ? 3.468   3.696   -9.147  1 68.32  ? 399 LEU   B CD2 1 
ATOM   5714 N  N   . LEU   B 1 415 ? 0.415   0.185   -9.131  1 69.49  ? 400 LEU   B N   1 
ATOM   5715 C  CA  . LEU   B 1 415 ? -0.847  -0.48   -8.839  1 70.44  ? 400 LEU   B CA  1 
ATOM   5716 C  C   . LEU   B 1 415 ? -1.989  0.546   -8.907  1 71.99  ? 400 LEU   B C   1 
ATOM   5717 O  O   . LEU   B 1 415 ? -3.033  0.279   -9.517  1 72.17  ? 400 LEU   B O   1 
ATOM   5718 C  CB  . LEU   B 1 415 ? -0.81   -1.126  -7.445  1 69.94  ? 400 LEU   B CB  1 
ATOM   5719 C  CG  . LEU   B 1 415 ? 0.38    -1.99   -7.15   1 70.76  ? 400 LEU   B CG  1 
ATOM   5720 C  CD1 . LEU   B 1 415 ? 0.354   -2.436  -5.736  1 71.38  ? 400 LEU   B CD1 1 
ATOM   5721 C  CD2 . LEU   B 1 415 ? 0.457   -3.166  -8.089  1 71.11  ? 400 LEU   B CD2 1 
ATOM   5722 N  N   . LYS   B 1 416 ? -1.759  1.733   -8.289  1 72.66  ? 401 LYS   B N   1 
ATOM   5723 C  CA  . LYS   B 1 416 ? -2.704  2.845   -8.136  1 73.82  ? 401 LYS   B CA  1 
ATOM   5724 C  C   . LYS   B 1 416 ? -3.855  2.465   -7.176  1 74.65  ? 401 LYS   B C   1 
ATOM   5725 O  O   . LYS   B 1 416 ? -3.681  1.601   -6.3    1 75.01  ? 401 LYS   B O   1 
ATOM   5726 C  CB  . LYS   B 1 416 ? -3.203  3.417   -9.485  1 75.43  ? 401 LYS   B CB  1 
HETATM 5727 C  CHA . HEM   C 2 .   ? 16.616  -29     -31.841 1 48.84  ? 501 HEM   A CHA 1 
HETATM 5728 C  CHB . HEM   C 2 .   ? 14.322  -31.212 -35.488 1 49.17  ? 501 HEM   A CHB 1 
HETATM 5729 C  CHC . HEM   C 2 .   ? 13.186  -34.959 -32.612 1 48.34  ? 501 HEM   A CHC 1 
HETATM 5730 C  CHD . HEM   C 2 .   ? 15.431  -32.68  -28.928 1 47.73  ? 501 HEM   A CHD 1 
HETATM 5731 C  C1A . HEM   C 2 .   ? 16.005  -29.24  -33.088 1 49.61  ? 501 HEM   A C1A 1 
HETATM 5732 C  C2A . HEM   C 2 .   ? 16.002  -28.302 -34.2   1 50.25  ? 501 HEM   A C2A 1 
HETATM 5733 C  C3A . HEM   C 2 .   ? 15.357  -28.933 -35.247 1 49.78  ? 501 HEM   A C3A 1 
HETATM 5734 C  C4A . HEM   C 2 .   ? 14.968  -30.244 -34.757 1 49.32  ? 501 HEM   A C4A 1 
HETATM 5735 C  CMA . HEM   C 2 .   ? 15.112  -28.415 -36.631 1 49.53  ? 501 HEM   A CMA 1 
HETATM 5736 C  CAA . HEM   C 2 .   ? 16.626  -26.934 -34.245 1 51.46  ? 501 HEM   A CAA 1 
HETATM 5737 C  CBA . HEM   C 2 .   ? 15.927  -25.887 -33.378 1 52.13  ? 501 HEM   A CBA 1 
HETATM 5738 C  CGA . HEM   C 2 .   ? 14.659  -25.315 -33.948 1 52.53  ? 501 HEM   A CGA 1 
HETATM 5739 O  O1A . HEM   C 2 .   ? 13.702  -25.075 -33.246 1 51.86  ? 501 HEM   A O1A 1 
HETATM 5740 O  O2A . HEM   C 2 .   ? 14.687  -25.036 -35.23  1 53.49  ? 501 HEM   A O2A 1 
HETATM 5741 C  C1B . HEM   C 2 .   ? 13.868  -32.477 -35.052 1 49.14  ? 501 HEM   A C1B 1 
HETATM 5742 C  C2B . HEM   C 2 .   ? 13.236  -33.457 -35.91  1 49.35  ? 501 HEM   A C2B 1 
HETATM 5743 C  C3B . HEM   C 2 .   ? 12.914  -34.509 -35.08  1 49.46  ? 501 HEM   A C3B 1 
HETATM 5744 C  C4B . HEM   C 2 .   ? 13.347  -34.184 -33.754 1 48.87  ? 501 HEM   A C4B 1 
HETATM 5745 C  CMB . HEM   C 2 .   ? 13.04   -33.317 -37.391 1 49.14  ? 501 HEM   A CMB 1 
HETATM 5746 C  CAB . HEM   C 2 .   ? 12.225  -35.739 -35.478 1 50.18  ? 501 HEM   A CAB 1 
HETATM 5747 C  CBB . HEM   C 2 .   ? 11.089  -35.865 -36.162 1 50.09  ? 501 HEM   A CBB 1 
HETATM 5748 C  C1C . HEM   C 2 .   ? 13.632  -34.626 -31.301 1 47.94  ? 501 HEM   A C1C 1 
HETATM 5749 C  C2C . HEM   C 2 .   ? 13.285  -35.362 -30.095 1 47.45  ? 501 HEM   A C2C 1 
HETATM 5750 C  C3C . HEM   C 2 .   ? 13.897  -34.689 -29.065 1 47.03  ? 501 HEM   A C3C 1 
HETATM 5751 C  C4C . HEM   C 2 .   ? 14.615  -33.581 -29.632 1 47.83  ? 501 HEM   A C4C 1 
HETATM 5752 C  CMC . HEM   C 2 .   ? 12.468  -36.619 -30.048 1 47.66  ? 501 HEM   A CMC 1 
HETATM 5753 C  CAC . HEM   C 2 .   ? 13.841  -35.03  -27.643 1 46.49  ? 501 HEM   A CAC 1 
HETATM 5754 C  CBC . HEM   C 2 .   ? 13.619  -34.256 -26.616 1 46.41  ? 501 HEM   A CBC 1 
HETATM 5755 C  C1D . HEM   C 2 .   ? 16.069  -31.523 -29.426 1 47.52  ? 501 HEM   A C1D 1 
HETATM 5756 C  C2D . HEM   C 2 .   ? 16.894  -30.623 -28.636 1 47.46  ? 501 HEM   A C2D 1 
HETATM 5757 C  C3D . HEM   C 2 .   ? 17.234  -29.579 -29.471 1 48.07  ? 501 HEM   A C3D 1 
HETATM 5758 C  C4D . HEM   C 2 .   ? 16.601  -29.853 -30.752 1 48.36  ? 501 HEM   A C4D 1 
HETATM 5759 C  CMD . HEM   C 2 .   ? 17.205  -30.775 -27.176 1 46.74  ? 501 HEM   A CMD 1 
HETATM 5760 C  CAD . HEM   C 2 .   ? 18.059  -28.374 -29.116 1 48.61  ? 501 HEM   A CAD 1 
HETATM 5761 C  CBD . HEM   C 2 .   ? 19.5    -28.469 -29.601 1 49.3   ? 501 HEM   A CBD 1 
HETATM 5762 C  CGD . HEM   C 2 .   ? 20.337  -29.456 -28.839 1 49.97  ? 501 HEM   A CGD 1 
HETATM 5763 O  O1D . HEM   C 2 .   ? 20.963  -30.336 -29.392 1 50.71  ? 501 HEM   A O1D 1 
HETATM 5764 O  O2D . HEM   C 2 .   ? 20.348  -29.27  -27.537 1 50.07  ? 501 HEM   A O2D 1 
HETATM 5765 N  NA  . HEM   C 2 .   ? 15.371  -30.395 -33.439 1 49.38  ? 501 HEM   A NA  1 
HETATM 5766 N  NB  . HEM   C 2 .   ? 13.938  -32.926 -33.77  1 49.09  ? 501 HEM   A NB  1 
HETATM 5767 N  NC  . HEM   C 2 .   ? 14.424  -33.565 -31.011 1 48.12  ? 501 HEM   A NC  1 
HETATM 5768 N  ND  . HEM   C 2 .   ? 15.911  -31.055 -30.692 1 48.16  ? 501 HEM   A ND  1 
HETATM 5769 FE FE  . HEM   C 2 .   ? 14.946  -32.011 -32.236 1 49.07  ? 501 HEM   A FE  1 
HETATM 5770 N  N1  . A1H6V D 3 .   ? 11.127  -28.932 -36.042 1 54.16  ? 502 A1H6V A N1  1 
HETATM 5771 N  N3  . A1H6V D 3 .   ? 12.249  -26.379 -41.628 1 59.32  ? 502 A1H6V A N3  1 
HETATM 5772 C  C4  . A1H6V D 3 .   ? 12.009  -25.996 -37.945 1 58.36  ? 502 A1H6V A C4  1 
HETATM 5773 C  C5  . A1H6V D 3 .   ? 12.355  -25.631 -39.236 1 58.96  ? 502 A1H6V A C5  1 
HETATM 5774 C  C6  . A1H6V D 3 .   ? 10.97   -28.04  -38.75  1 58.45  ? 502 A1H6V A C6  1 
HETATM 5775 C  C7  . A1H6V D 3 .   ? 11.315  -27.687 -40.058 1 59.17  ? 502 A1H6V A C7  1 
HETATM 5776 C  C8  . A1H6V D 3 .   ? 12.002  -26.477 -40.28  1 59.1   ? 502 A1H6V A C8  1 
HETATM 5777 C  C10 . A1H6V D 3 .   ? 11.166  -28.315 -41.344 1 59.58  ? 502 A1H6V A C10 1 
HETATM 5778 C  C13 . A1H6V D 3 .   ? 8.473   -28.004 -31.096 1 49.08  ? 502 A1H6V A C13 1 
HETATM 5779 C  C15 . A1H6V D 3 .   ? 7.136   -28.407 -30.542 1 48.72  ? 502 A1H6V A C15 1 
HETATM 5780 C  C17 . A1H6V D 3 .   ? 12.17   -31.774 -30.999 1 49.23  ? 502 A1H6V A C17 1 
HETATM 5781 O  O   . A1H6V D 3 .   ? 12.374  -27.092 -32.338 1 51.22  ? 502 A1H6V A O   1 
HETATM 5782 C  C   . A1H6V D 3 .   ? 11.098  -27.535 -32.709 1 51.36  ? 502 A1H6V A C   1 
HETATM 5783 C  C11 . A1H6V D 3 .   ? 10.756  -28.77  -31.909 1 50.11  ? 502 A1H6V A C11 1 
HETATM 5784 N  N5  . A1H6V D 3 .   ? 11.638  -29.841 -31.789 1 49.53  ? 502 A1H6V A N5  1 
HETATM 5785 C  C18 . A1H6V D 3 .   ? 12.887  -30.206 -32.233 1 49.11  ? 502 A1H6V A C18 1 
HETATM 5786 N  N4  . A1H6V D 3 .   ? 13.236  -31.381 -31.759 1 49.01  ? 502 A1H6V A N4  1 
HETATM 5787 C  C16 . A1H6V D 3 .   ? 11.171  -30.877 -30.992 1 49.49  ? 502 A1H6V A C16 1 
HETATM 5788 S  S   . A1H6V D 3 .   ? 9.58    -30.488 -30.408 1 49.96  ? 502 A1H6V A S   1 
HETATM 5789 C  C12 . A1H6V D 3 .   ? 9.611   -28.952 -31.229 1 49.75  ? 502 A1H6V A C12 1 
HETATM 5790 C  C14 . A1H6V D 3 .   ? 8.025   -27.494 -29.756 1 48.76  ? 502 A1H6V A C14 1 
HETATM 5791 C  C1  . A1H6V D 3 .   ? 11.059  -27.767 -34.199 1 52.96  ? 502 A1H6V A C1  1 
HETATM 5792 C  C2  . A1H6V D 3 .   ? 11.069  -26.866 -35.223 1 53.81  ? 502 A1H6V A C2  1 
HETATM 5793 N  N2  . A1H6V D 3 .   ? 11.116  -27.612 -36.349 1 55.06  ? 502 A1H6V A N2  1 
HETATM 5794 N  N   . A1H6V D 3 .   ? 11.094  -29.024 -34.735 1 53.48  ? 502 A1H6V A N   1 
HETATM 5795 C  C3  . A1H6V D 3 .   ? 11.328  -27.19  -37.697 1 57.4   ? 502 A1H6V A C3  1 
HETATM 5796 C  C9  . A1H6V D 3 .   ? 11.744  -27.491 -42.255 1 59.57  ? 502 A1H6V A C9  1 
HETATM 5797 C  CHA . HEM   E 2 .   ? 21.312  4.025   -19.62  1 56.5   ? 501 HEM   B CHA 1 
HETATM 5798 C  CHB . HEM   E 2 .   ? 23.197  8.239   -21.06  1 56.67  ? 501 HEM   B CHB 1 
HETATM 5799 C  CHC . HEM   E 2 .   ? 24.076  9.527   -16.478 1 56.06  ? 501 HEM   B CHC 1 
HETATM 5800 C  CHD . HEM   E 2 .   ? 22.277  5.228   -15.03  1 55.11  ? 501 HEM   B CHD 1 
HETATM 5801 C  C1A . HEM   E 2 .   ? 21.839  5.047   -20.437 1 56.73  ? 501 HEM   B C1A 1 
HETATM 5802 C  C2A . HEM   E 2 .   ? 21.887  4.999   -21.888 1 57.48  ? 501 HEM   B C2A 1 
HETATM 5803 C  C3A . HEM   E 2 .   ? 22.424  6.198   -22.301 1 57.27  ? 501 HEM   B C3A 1 
HETATM 5804 C  C4A . HEM   E 2 .   ? 22.694  6.962   -21.095 1 56.8   ? 501 HEM   B C4A 1 
HETATM 5805 C  CMA . HEM   E 2 .   ? 22.702  6.658   -23.701 1 57.13  ? 501 HEM   B CMA 1 
HETATM 5806 C  CAA . HEM   E 2 .   ? 21.41   3.884   -22.779 1 58.72  ? 501 HEM   B CAA 1 
HETATM 5807 C  CBA . HEM   E 2 .   ? 22.308  2.648   -22.758 1 59.97  ? 501 HEM   B CBA 1 
HETATM 5808 C  CGA . HEM   E 2 .   ? 23.547  2.797   -23.595 1 60.98  ? 501 HEM   B CGA 1 
HETATM 5809 O  O1A . HEM   E 2 .   ? 23.519  3.195   -24.753 1 61.31  ? 501 HEM   B O1A 1 
HETATM 5810 O  O2A . HEM   E 2 .   ? 24.656  2.524   -22.949 1 61.31  ? 501 HEM   B O2A 1 
HETATM 5811 C  C1B . HEM   E 2 .   ? 23.537  9.007   -19.937 1 56.55  ? 501 HEM   B C1B 1 
HETATM 5812 C  C2B . HEM   E 2 .   ? 24.056  10.356  -20.008 1 56.6   ? 501 HEM   B C2B 1 
HETATM 5813 C  C3B . HEM   E 2 .   ? 24.314  10.712  -18.706 1 56.63  ? 501 HEM   B C3B 1 
HETATM 5814 C  C4B . HEM   E 2 .   ? 23.951  9.606   -17.861 1 56.52  ? 501 HEM   B C4B 1 
HETATM 5815 C  CMB . HEM   E 2 .   ? 24.235  11.147  -21.268 1 56.58  ? 501 HEM   B CMB 1 
HETATM 5816 C  CAB . HEM   E 2 .   ? 24.887  11.983  -18.264 1 56.76  ? 501 HEM   B CAB 1 
HETATM 5817 C  CBB . HEM   E 2 .   ? 25.982  12.563  -18.72  1 56.99  ? 501 HEM   B CBB 1 
HETATM 5818 C  C1C . HEM   E 2 .   ? 23.719  8.417   -15.657 1 55.32  ? 501 HEM   B C1C 1 
HETATM 5819 C  C2C . HEM   E 2 .   ? 24.033  8.297   -14.242 1 54.71  ? 501 HEM   B C2C 1 
HETATM 5820 C  C3C . HEM   E 2 .   ? 23.536  7.073   -13.855 1 54.44  ? 501 HEM   B C3C 1 
HETATM 5821 C  C4C . HEM   E 2 .   ? 22.922  6.469   -15.004 1 55.05  ? 501 HEM   B C4C 1 
HETATM 5822 C  CMC . HEM   E 2 .   ? 24.715  9.34    -13.411 1 54.42  ? 501 HEM   B CMC 1 
HETATM 5823 C  CAC . HEM   E 2 .   ? 23.615  6.483   -12.517 1 53.44  ? 501 HEM   B CAC 1 
HETATM 5824 C  CBC . HEM   E 2 .   ? 23.974  5.281   -12.175 1 52.84  ? 501 HEM   B CBC 1 
HETATM 5825 C  C1D . HEM   E 2 .   ? 21.751  4.556   -16.157 1 55.37  ? 501 HEM   B C1D 1 
HETATM 5826 C  C2D . HEM   E 2 .   ? 21.038  3.289   -16.108 1 55.11  ? 501 HEM   B C2D 1 
HETATM 5827 C  C3D . HEM   E 2 .   ? 20.745  2.959   -17.414 1 55.36  ? 501 HEM   B C3D 1 
HETATM 5828 C  C4D . HEM   E 2 .   ? 21.298  4.019   -18.238 1 55.96  ? 501 HEM   B C4D 1 
HETATM 5829 C  CMD . HEM   E 2 .   ? 20.765  2.494   -14.87  1 54.46  ? 501 HEM   B CMD 1 
HETATM 5830 C  CAD . HEM   E 2 .   ? 20.033  1.722   -17.892 1 55.24  ? 501 HEM   B CAD 1 
HETATM 5831 C  CBD . HEM   E 2 .   ? 18.559  1.95    -18.242 1 55.42  ? 501 HEM   B CBD 1 
HETATM 5832 C  CGD . HEM   E 2 .   ? 17.659  2.232   -17.068 1 55.82  ? 501 HEM   B CGD 1 
HETATM 5833 O  O1D . HEM   E 2 .   ? 16.922  3.197   -17.021 1 56.19  ? 501 HEM   B O1D 1 
HETATM 5834 O  O2D . HEM   E 2 .   ? 17.702  1.334   -16.113 1 55.79  ? 501 HEM   B O2D 1 
HETATM 5835 N  NA  . HEM   E 2 .   ? 22.337  6.23    -19.98  1 56.43  ? 501 HEM   B NA  1 
HETATM 5836 N  NB  . HEM   E 2 .   ? 23.471  8.575   -18.654 1 56.49  ? 501 HEM   B NB  1 
HETATM 5837 N  NC  . HEM   E 2 .   ? 23.054  7.323   -16.097 1 55.34  ? 501 HEM   B NC  1 
HETATM 5838 N  ND  . HEM   E 2 .   ? 21.894  4.984   -17.435 1 55.89  ? 501 HEM   B ND  1 
HETATM 5839 FE FE  . HEM   E 2 .   ? 22.701  6.778   -18.033 1 56.08  ? 501 HEM   B FE  1 
HETATM 5840 N  N1  . A1H6V F 3 .   ? 26.744  7.026   -22.912 1 71.34  ? 502 A1H6V B N1  1 
HETATM 5841 N  N3  . A1H6V F 3 .   ? 25.509  7.754   -29.007 1 75.2   ? 502 A1H6V B N3  1 
HETATM 5842 C  C4  . A1H6V F 3 .   ? 26.361  5.473   -26.205 1 74.41  ? 502 A1H6V B C4  1 
HETATM 5843 C  C5  . A1H6V F 3 .   ? 25.99   5.804   -27.497 1 74.99  ? 502 A1H6V B C5  1 
HETATM 5844 C  C6  . A1H6V F 3 .   ? 26.529  7.823   -25.596 1 73.95  ? 502 A1H6V B C6  1 
HETATM 5845 C  C7  . A1H6V F 3 .   ? 26.153  8.174   -26.894 1 74.74  ? 502 A1H6V B C7  1 
HETATM 5846 C  C8  . A1H6V F 3 .   ? 25.891  7.151   -27.831 1 75.05  ? 502 A1H6V B C8  1 
HETATM 5847 C  C10 . A1H6V F 3 .   ? 25.908  9.42    -27.569 1 75     ? 502 A1H6V B C10 1 
HETATM 5848 C  C13 . A1H6V F 3 .   ? 29.622  3.757   -19.312 1 61.18  ? 502 A1H6V B C13 1 
HETATM 5849 C  C15 . A1H6V F 3 .   ? 30.809  3.561   -18.416 1 61.13  ? 502 A1H6V B C15 1 
HETATM 5850 C  C17 . A1H6V F 3 .   ? 25.523  6.168   -17.034 1 60.44  ? 502 A1H6V B C17 1 
HETATM 5851 O  O   . A1H6V F 3 .   ? 25.771  3.351   -21.01  1 65.59  ? 502 A1H6V B O   1 
HETATM 5852 C  C   . A1H6V F 3 .   ? 27.008  4.021   -20.936 1 65.86  ? 502 A1H6V B C   1 
HETATM 5853 C  C11 . A1H6V F 3 .   ? 27.238  4.556   -19.543 1 62.72  ? 502 A1H6V B C11 1 
HETATM 5854 N  N5  . A1H6V F 3 .   ? 26.239  5.205   -18.828 1 61.09  ? 502 A1H6V B N5  1 
HETATM 5855 C  C18 . A1H6V F 3 .   ? 24.954  5.654   -19.015 1 60.84  ? 502 A1H6V B C18 1 
HETATM 5856 N  N4  . A1H6V F 3 .   ? 24.498  6.256   -17.934 1 60.72  ? 502 A1H6V B N4  1 
HETATM 5857 C  C16 . A1H6V F 3 .   ? 26.596  5.529   -17.523 1 60.53  ? 502 A1H6V B C16 1 
HETATM 5858 S  S   . A1H6V F 3 .   ? 28.218  4.985   -17.218 1 60.71  ? 502 A1H6V B S   1 
HETATM 5859 C  C12 . A1H6V F 3 .   ? 28.368  4.383   -18.842 1 61.53  ? 502 A1H6V B C12 1 
HETATM 5860 C  C14 . A1H6V F 3 .   ? 30.029  2.375   -18.889 1 61.03  ? 502 A1H6V B C14 1 
HETATM 5861 C  C1  . A1H6V F 3 .   ? 27.048  5.055   -22.023 1 69.12  ? 502 A1H6V B C1  1 
HETATM 5862 C  C2  . A1H6V F 3 .   ? 27.06   4.873   -23.375 1 70.67  ? 502 A1H6V B C2  1 
HETATM 5863 N  N2  . A1H6V F 3 .   ? 26.864  6.105   -23.899 1 71.96  ? 502 A1H6V B N2  1 
HETATM 5864 N  N   . A1H6V F 3 .   ? 26.857  6.385   -21.772 1 70.47  ? 502 A1H6V B N   1 
HETATM 5865 C  C3  . A1H6V F 3 .   ? 26.624  6.471   -25.257 1 73.49  ? 502 A1H6V B C3  1 
HETATM 5866 C  C9  . A1H6V F 3 .   ? 25.522  9.116   -28.834 1 75.13  ? 502 A1H6V B C9  1 
HETATM 5867 O  O   . HOH   G 4 .   ? 14.845  -36.836 -11.344 1 57.07  ? 601 HOH   A O   1 
HETATM 5868 O  O   . HOH   G 4 .   ? 1.005   -24.698 -21.265 1 37.93  ? 602 HOH   A O   1 
HETATM 5869 O  O   . HOH   G 4 .   ? 21.816  -26.329 -24.25  1 51.03  ? 603 HOH   A O   1 
HETATM 5870 O  O   . HOH   G 4 .   ? 10.509  -25.468 -21.402 1 40.89  ? 604 HOH   A O   1 
HETATM 5871 O  O   . HOH   G 4 .   ? 8.982   -12.18  -38.254 1 54.47  ? 605 HOH   A O   1 
HETATM 5872 O  O   . HOH   G 4 .   ? 6.897   -29.898 -13.486 1 52.28  ? 606 HOH   A O   1 
HETATM 5873 O  O   . HOH   G 4 .   ? 17.086  -27.439 -24.74  1 34.89  ? 607 HOH   A O   1 
HETATM 5874 O  O   . HOH   G 4 .   ? -2.917  -28.636 -17.781 1 54.21  ? 608 HOH   A O   1 
HETATM 5875 O  O   . HOH   G 4 .   ? 10.835  -26.484 -19.035 1 46.88  ? 609 HOH   A O   1 
HETATM 5876 O  O   . HOH   G 4 .   ? 11.677  -28.724 -20.456 1 46.7   ? 610 HOH   A O   1 
HETATM 5877 O  O   . HOH   G 4 .   ? 30.671  -27.565 -14.829 1 60     ? 611 HOH   A O   1 
HETATM 5878 O  O   . HOH   G 4 .   ? -10.16  -21.191 -41.856 1 59.96  ? 612 HOH   A O   1 
HETATM 5879 O  O   . HOH   G 4 .   ? 13.632  -34.605 -10.275 1 51.08  ? 613 HOH   A O   1 
HETATM 5880 O  O   . HOH   H 4 .   ? 15.841  7.296   -18.556 1 45.78  ? 601 HOH   B O   1 
HETATM 5881 O  O   . HOH   H 4 .   ? 37.662  -4.669  -13.301 1 48.59  ? 602 HOH   B O   1 
HETATM 5882 O  O   . HOH   H 4 .   ? 25.896  -0.366  -5.675  1 55.87  ? 603 HOH   B O   1 
HETATM 5883 O  O   . HOH   H 4 .   ? 26.439  -2.483  -10.501 1 39.12  ? 604 HOH   B O   1 
HETATM 5884 O  O   . HOH   H 4 .   ? 22.415  -7.341  3.944   1 60.14  ? 605 HOH   B O   1 
HETATM 5885 O  O   . HOH   H 4 .   ? 32.643  -9.691  -7.863  1 51.62  ? 606 HOH   B O   1 
# 
