data_9F5R
# 
_entry.id   9F5R 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9F5R         pdb_00009f5r 10.2210/pdb9f5r/pdb 
WWPDB D_1292136894 ?            ?                   
# 
_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       2025-05-14 
_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                        9F5R 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-30 
_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    CASP 
_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)-[1-[2,5-bis(fluoranyl)-4-methoxy-phenyl]-1,2,3-triazol-4-yl]-(6-cyclopropylimidazo[1,5-a]pyrazin-5-yl)methanol' 398.366   2   
?          ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE' 78.133    3   ?          ? ? ? 
5 water       nat water 18.015    350 ?          ? ? ? 
# 
_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)-[1-[2,5-bis(fluoranyl)-4-methoxy-phenyl]-1,2,3-triazol-4-yl]-(6-cyclopropylimidazo[1,5-a]pyrazin-5-yl)methanol' A1H93 
4 'DIMETHYL SULFOXIDE'                                                                                                 DMS   
5 water                                                                                                                HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   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 
A1H93 non-polymer         . 
'(R)-[1-[2,5-bis(fluoranyl)-4-methoxy-phenyl]-1,2,3-triazol-4-yl]-(6-cyclopropylimidazo[1,5-a]pyrazin-5-yl)methanol' ?    
'C19 H16 F2 N6 O2' 398.366 
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 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE' ?    'C2 H6 O S'        78.133  
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  ?   ?   ?   A . n 
A 1 14  LEU 14  -1  ?   ?   ?   A . n 
A 1 15  GLU 15  0   ?   ?   ?   A . n 
A 1 16  VAL 16  1   ?   ?   ?   A . n 
A 1 17  LEU 17  2   ?   ?   ?   A . n 
A 1 18  PHE 18  3   ?   ?   ?   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 299 284 284 GLY GLY 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 ?   ?   ?   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 391 376 376 ALA ALA A . n 
A 1 392 LYS 392 377 377 LYS LYS A . n 
A 1 393 GLY 393 378 378 GLY GLY A . n 
A 1 394 THR 394 379 379 THR THR A . n 
A 1 395 GLY 395 380 380 GLY GLY A . n 
A 1 396 GLY 396 381 381 GLY GLY 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 418 403 403 GLY GLY 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  ?   ?   ?   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 376 361 361 GLN GLN 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 387 372 372 SER SER B . n 
B 1 388 LYS 388 373 373 LYS LYS B . n 
B 1 389 LEU 389 374 374 LEU LEU B . n 
B 1 390 GLU 390 375 375 GLU GLU B . n 
B 1 391 ALA 391 376 376 ALA ALA B . n 
B 1 392 LYS 392 377 377 LYS LYS B . n 
B 1 393 GLY 393 378 378 GLY GLY B . n 
B 1 394 THR 394 379 379 THR THR B . n 
B 1 395 GLY 395 380 380 GLY GLY 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 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 A1H93 ? ? A1H93 ? ? 'SUBJECT OF INVESTIGATION' ? 
2 HEM   ? ? HEM   ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 HEM   1   501 501 HEM   HEM A . 
D 3 A1H93 1   502 502 A1H93 LIG A . 
E 4 DMS   1   503 503 DMS   DMS A . 
F 2 HEM   1   501 501 HEM   HEM B . 
G 3 A1H93 1   502 502 A1H93 LIG B . 
H 4 DMS   1   503 503 DMS   DMS B . 
I 4 DMS   1   504 504 DMS   DMS B . 
J 5 HOH   1   601 318 HOH   HOH A . 
J 5 HOH   2   602 310 HOH   HOH A . 
J 5 HOH   3   603 329 HOH   HOH A . 
J 5 HOH   4   604 32  HOH   HOH A . 
J 5 HOH   5   605 332 HOH   HOH A . 
J 5 HOH   6   606 306 HOH   HOH A . 
J 5 HOH   7   607 210 HOH   HOH A . 
J 5 HOH   8   608 322 HOH   HOH A . 
J 5 HOH   9   609 52  HOH   HOH A . 
J 5 HOH   10  610 206 HOH   HOH A . 
J 5 HOH   11  611 73  HOH   HOH A . 
J 5 HOH   12  612 340 HOH   HOH A . 
J 5 HOH   13  613 126 HOH   HOH A . 
J 5 HOH   14  614 33  HOH   HOH A . 
J 5 HOH   15  615 105 HOH   HOH A . 
J 5 HOH   16  616 314 HOH   HOH A . 
J 5 HOH   17  617 111 HOH   HOH A . 
J 5 HOH   18  618 155 HOH   HOH A . 
J 5 HOH   19  619 353 HOH   HOH A . 
J 5 HOH   20  620 92  HOH   HOH A . 
J 5 HOH   21  621 34  HOH   HOH A . 
J 5 HOH   22  622 196 HOH   HOH A . 
J 5 HOH   23  623 361 HOH   HOH A . 
J 5 HOH   24  624 53  HOH   HOH A . 
J 5 HOH   25  625 208 HOH   HOH A . 
J 5 HOH   26  626 20  HOH   HOH A . 
J 5 HOH   27  627 93  HOH   HOH A . 
J 5 HOH   28  628 2   HOH   HOH A . 
J 5 HOH   29  629 1   HOH   HOH A . 
J 5 HOH   30  630 304 HOH   HOH A . 
J 5 HOH   31  631 69  HOH   HOH A . 
J 5 HOH   32  632 311 HOH   HOH A . 
J 5 HOH   33  633 56  HOH   HOH A . 
J 5 HOH   34  634 148 HOH   HOH A . 
J 5 HOH   35  635 21  HOH   HOH A . 
J 5 HOH   36  636 29  HOH   HOH A . 
J 5 HOH   37  637 252 HOH   HOH A . 
J 5 HOH   38  638 82  HOH   HOH A . 
J 5 HOH   39  639 57  HOH   HOH A . 
J 5 HOH   40  640 103 HOH   HOH A . 
J 5 HOH   41  641 214 HOH   HOH A . 
J 5 HOH   42  642 371 HOH   HOH A . 
J 5 HOH   43  643 76  HOH   HOH A . 
J 5 HOH   44  644 6   HOH   HOH A . 
J 5 HOH   45  645 19  HOH   HOH A . 
J 5 HOH   46  646 71  HOH   HOH A . 
J 5 HOH   47  647 347 HOH   HOH A . 
J 5 HOH   48  648 95  HOH   HOH A . 
J 5 HOH   49  649 80  HOH   HOH A . 
J 5 HOH   50  650 39  HOH   HOH A . 
J 5 HOH   51  651 390 HOH   HOH A . 
J 5 HOH   52  652 41  HOH   HOH A . 
J 5 HOH   53  653 43  HOH   HOH A . 
J 5 HOH   54  654 63  HOH   HOH A . 
J 5 HOH   55  655 387 HOH   HOH A . 
J 5 HOH   56  656 231 HOH   HOH A . 
J 5 HOH   57  657 256 HOH   HOH A . 
J 5 HOH   58  658 42  HOH   HOH A . 
J 5 HOH   59  659 110 HOH   HOH A . 
J 5 HOH   60  660 75  HOH   HOH A . 
J 5 HOH   61  661 60  HOH   HOH A . 
J 5 HOH   62  662 134 HOH   HOH A . 
J 5 HOH   63  663 327 HOH   HOH A . 
J 5 HOH   64  664 199 HOH   HOH A . 
J 5 HOH   65  665 79  HOH   HOH A . 
J 5 HOH   66  666 344 HOH   HOH A . 
J 5 HOH   67  667 301 HOH   HOH A . 
J 5 HOH   68  668 297 HOH   HOH A . 
J 5 HOH   69  669 370 HOH   HOH A . 
J 5 HOH   70  670 40  HOH   HOH A . 
J 5 HOH   71  671 67  HOH   HOH A . 
J 5 HOH   72  672 336 HOH   HOH A . 
J 5 HOH   73  673 321 HOH   HOH A . 
J 5 HOH   74  674 362 HOH   HOH A . 
J 5 HOH   75  675 8   HOH   HOH A . 
J 5 HOH   76  676 359 HOH   HOH A . 
J 5 HOH   77  677 123 HOH   HOH A . 
J 5 HOH   78  678 330 HOH   HOH A . 
J 5 HOH   79  679 232 HOH   HOH A . 
J 5 HOH   80  680 108 HOH   HOH A . 
J 5 HOH   81  681 58  HOH   HOH A . 
J 5 HOH   82  682 174 HOH   HOH A . 
J 5 HOH   83  683 26  HOH   HOH A . 
J 5 HOH   84  684 49  HOH   HOH A . 
J 5 HOH   85  685 296 HOH   HOH A . 
J 5 HOH   86  686 182 HOH   HOH A . 
J 5 HOH   87  687 17  HOH   HOH A . 
J 5 HOH   88  688 10  HOH   HOH A . 
J 5 HOH   89  689 253 HOH   HOH A . 
J 5 HOH   90  690 11  HOH   HOH A . 
J 5 HOH   91  691 331 HOH   HOH A . 
J 5 HOH   92  692 300 HOH   HOH A . 
J 5 HOH   93  693 115 HOH   HOH A . 
J 5 HOH   94  694 233 HOH   HOH A . 
J 5 HOH   95  695 62  HOH   HOH A . 
J 5 HOH   96  696 156 HOH   HOH A . 
J 5 HOH   97  697 295 HOH   HOH A . 
J 5 HOH   98  698 307 HOH   HOH A . 
J 5 HOH   99  699 138 HOH   HOH A . 
J 5 HOH   100 700 142 HOH   HOH A . 
J 5 HOH   101 701 9   HOH   HOH A . 
J 5 HOH   102 702 228 HOH   HOH A . 
J 5 HOH   103 703 96  HOH   HOH A . 
J 5 HOH   104 704 367 HOH   HOH A . 
J 5 HOH   105 705 240 HOH   HOH A . 
J 5 HOH   106 706 143 HOH   HOH A . 
J 5 HOH   107 707 317 HOH   HOH A . 
J 5 HOH   108 708 16  HOH   HOH A . 
J 5 HOH   109 709 334 HOH   HOH A . 
J 5 HOH   110 710 167 HOH   HOH A . 
J 5 HOH   111 711 177 HOH   HOH A . 
J 5 HOH   112 712 202 HOH   HOH A . 
J 5 HOH   113 713 135 HOH   HOH A . 
J 5 HOH   114 714 159 HOH   HOH A . 
J 5 HOH   115 715 151 HOH   HOH A . 
J 5 HOH   116 716 173 HOH   HOH A . 
J 5 HOH   117 717 154 HOH   HOH A . 
J 5 HOH   118 718 147 HOH   HOH A . 
J 5 HOH   119 719 113 HOH   HOH A . 
J 5 HOH   120 720 117 HOH   HOH A . 
J 5 HOH   121 721 70  HOH   HOH A . 
J 5 HOH   122 722 262 HOH   HOH A . 
J 5 HOH   123 723 101 HOH   HOH A . 
J 5 HOH   124 724 129 HOH   HOH A . 
J 5 HOH   125 725 78  HOH   HOH A . 
J 5 HOH   126 726 59  HOH   HOH A . 
J 5 HOH   127 727 44  HOH   HOH A . 
J 5 HOH   128 728 35  HOH   HOH A . 
J 5 HOH   129 729 81  HOH   HOH A . 
J 5 HOH   130 730 366 HOH   HOH A . 
J 5 HOH   131 731 205 HOH   HOH A . 
J 5 HOH   132 732 47  HOH   HOH A . 
J 5 HOH   133 733 12  HOH   HOH A . 
J 5 HOH   134 734 74  HOH   HOH A . 
J 5 HOH   135 735 27  HOH   HOH A . 
J 5 HOH   136 736 365 HOH   HOH A . 
J 5 HOH   137 737 22  HOH   HOH A . 
J 5 HOH   138 738 152 HOH   HOH A . 
J 5 HOH   139 739 221 HOH   HOH A . 
J 5 HOH   140 740 268 HOH   HOH A . 
J 5 HOH   141 741 246 HOH   HOH A . 
J 5 HOH   142 742 223 HOH   HOH A . 
J 5 HOH   143 743 339 HOH   HOH A . 
J 5 HOH   144 744 234 HOH   HOH A . 
J 5 HOH   145 745 184 HOH   HOH A . 
J 5 HOH   146 746 392 HOH   HOH A . 
J 5 HOH   147 747 85  HOH   HOH A . 
J 5 HOH   148 748 128 HOH   HOH A . 
J 5 HOH   149 749 363 HOH   HOH A . 
J 5 HOH   150 750 207 HOH   HOH A . 
J 5 HOH   151 751 239 HOH   HOH A . 
J 5 HOH   152 752 171 HOH   HOH A . 
J 5 HOH   153 753 77  HOH   HOH A . 
J 5 HOH   154 754 66  HOH   HOH A . 
J 5 HOH   155 755 145 HOH   HOH A . 
J 5 HOH   156 756 325 HOH   HOH A . 
J 5 HOH   157 757 61  HOH   HOH A . 
J 5 HOH   158 758 348 HOH   HOH A . 
J 5 HOH   159 759 38  HOH   HOH A . 
J 5 HOH   160 760 163 HOH   HOH A . 
J 5 HOH   161 761 18  HOH   HOH A . 
J 5 HOH   162 762 358 HOH   HOH A . 
J 5 HOH   163 763 181 HOH   HOH A . 
J 5 HOH   164 764 136 HOH   HOH A . 
J 5 HOH   165 765 187 HOH   HOH A . 
J 5 HOH   166 766 384 HOH   HOH A . 
J 5 HOH   167 767 250 HOH   HOH A . 
J 5 HOH   168 768 86  HOH   HOH A . 
J 5 HOH   169 769 168 HOH   HOH A . 
J 5 HOH   170 770 190 HOH   HOH A . 
J 5 HOH   171 771 37  HOH   HOH A . 
J 5 HOH   172 772 241 HOH   HOH A . 
J 5 HOH   173 773 373 HOH   HOH A . 
J 5 HOH   174 774 139 HOH   HOH A . 
J 5 HOH   175 775 374 HOH   HOH A . 
J 5 HOH   176 776 180 HOH   HOH A . 
J 5 HOH   177 777 235 HOH   HOH A . 
J 5 HOH   178 778 342 HOH   HOH A . 
J 5 HOH   179 779 369 HOH   HOH A . 
J 5 HOH   180 780 165 HOH   HOH A . 
J 5 HOH   181 781 309 HOH   HOH A . 
J 5 HOH   182 782 287 HOH   HOH A . 
J 5 HOH   183 783 227 HOH   HOH A . 
J 5 HOH   184 784 284 HOH   HOH A . 
J 5 HOH   185 785 283 HOH   HOH A . 
J 5 HOH   186 786 357 HOH   HOH A . 
J 5 HOH   187 787 328 HOH   HOH A . 
J 5 HOH   188 788 308 HOH   HOH A . 
J 5 HOH   189 789 179 HOH   HOH A . 
J 5 HOH   190 790 289 HOH   HOH A . 
J 5 HOH   191 791 102 HOH   HOH A . 
J 5 HOH   192 792 280 HOH   HOH A . 
J 5 HOH   193 793 335 HOH   HOH A . 
J 5 HOH   194 794 388 HOH   HOH A . 
J 5 HOH   195 795 169 HOH   HOH A . 
J 5 HOH   196 796 279 HOH   HOH A . 
J 5 HOH   197 797 275 HOH   HOH A . 
J 5 HOH   198 798 281 HOH   HOH A . 
J 5 HOH   199 799 393 HOH   HOH A . 
J 5 HOH   200 800 272 HOH   HOH A . 
J 5 HOH   201 801 125 HOH   HOH A . 
J 5 HOH   202 802 254 HOH   HOH A . 
J 5 HOH   203 803 274 HOH   HOH A . 
J 5 HOH   204 804 158 HOH   HOH A . 
J 5 HOH   205 805 265 HOH   HOH A . 
J 5 HOH   206 806 277 HOH   HOH A . 
K 5 HOH   1   601 144 HOH   HOH B . 
K 5 HOH   2   602 116 HOH   HOH B . 
K 5 HOH   3   603 313 HOH   HOH B . 
K 5 HOH   4   604 380 HOH   HOH B . 
K 5 HOH   5   605 383 HOH   HOH B . 
K 5 HOH   6   606 368 HOH   HOH B . 
K 5 HOH   7   607 242 HOH   HOH B . 
K 5 HOH   8   608 36  HOH   HOH B . 
K 5 HOH   9   609 195 HOH   HOH B . 
K 5 HOH   10  610 15  HOH   HOH B . 
K 5 HOH   11  611 350 HOH   HOH B . 
K 5 HOH   12  612 319 HOH   HOH B . 
K 5 HOH   13  613 385 HOH   HOH B . 
K 5 HOH   14  614 3   HOH   HOH B . 
K 5 HOH   15  615 326 HOH   HOH B . 
K 5 HOH   16  616 376 HOH   HOH B . 
K 5 HOH   17  617 338 HOH   HOH B . 
K 5 HOH   18  618 121 HOH   HOH B . 
K 5 HOH   19  619 341 HOH   HOH B . 
K 5 HOH   20  620 379 HOH   HOH B . 
K 5 HOH   21  621 333 HOH   HOH B . 
K 5 HOH   22  622 87  HOH   HOH B . 
K 5 HOH   23  623 119 HOH   HOH B . 
K 5 HOH   24  624 354 HOH   HOH B . 
K 5 HOH   25  625 257 HOH   HOH B . 
K 5 HOH   26  626 352 HOH   HOH B . 
K 5 HOH   27  627 178 HOH   HOH B . 
K 5 HOH   28  628 5   HOH   HOH B . 
K 5 HOH   29  629 337 HOH   HOH B . 
K 5 HOH   30  630 209 HOH   HOH B . 
K 5 HOH   31  631 64  HOH   HOH B . 
K 5 HOH   32  632 372 HOH   HOH B . 
K 5 HOH   33  633 28  HOH   HOH B . 
K 5 HOH   34  634 118 HOH   HOH B . 
K 5 HOH   35  635 351 HOH   HOH B . 
K 5 HOH   36  636 99  HOH   HOH B . 
K 5 HOH   37  637 375 HOH   HOH B . 
K 5 HOH   38  638 315 HOH   HOH B . 
K 5 HOH   39  639 193 HOH   HOH B . 
K 5 HOH   40  640 189 HOH   HOH B . 
K 5 HOH   41  641 217 HOH   HOH B . 
K 5 HOH   42  642 203 HOH   HOH B . 
K 5 HOH   43  643 346 HOH   HOH B . 
K 5 HOH   44  644 222 HOH   HOH B . 
K 5 HOH   45  645 349 HOH   HOH B . 
K 5 HOH   46  646 364 HOH   HOH B . 
K 5 HOH   47  647 293 HOH   HOH B . 
K 5 HOH   48  648 65  HOH   HOH B . 
K 5 HOH   49  649 292 HOH   HOH B . 
K 5 HOH   50  650 312 HOH   HOH B . 
K 5 HOH   51  651 191 HOH   HOH B . 
K 5 HOH   52  652 25  HOH   HOH B . 
K 5 HOH   53  653 55  HOH   HOH B . 
K 5 HOH   54  654 188 HOH   HOH B . 
K 5 HOH   55  655 303 HOH   HOH B . 
K 5 HOH   56  656 247 HOH   HOH B . 
K 5 HOH   57  657 161 HOH   HOH B . 
K 5 HOH   58  658 291 HOH   HOH B . 
K 5 HOH   59  659 229 HOH   HOH B . 
K 5 HOH   60  660 263 HOH   HOH B . 
K 5 HOH   61  661 294 HOH   HOH B . 
K 5 HOH   62  662 89  HOH   HOH B . 
K 5 HOH   63  663 200 HOH   HOH B . 
K 5 HOH   64  664 298 HOH   HOH B . 
K 5 HOH   65  665 224 HOH   HOH B . 
K 5 HOH   66  666 260 HOH   HOH B . 
K 5 HOH   67  667 50  HOH   HOH B . 
K 5 HOH   68  668 149 HOH   HOH B . 
K 5 HOH   69  669 166 HOH   HOH B . 
K 5 HOH   70  670 98  HOH   HOH B . 
K 5 HOH   71  671 127 HOH   HOH B . 
K 5 HOH   72  672 120 HOH   HOH B . 
K 5 HOH   73  673 4   HOH   HOH B . 
K 5 HOH   74  674 226 HOH   HOH B . 
K 5 HOH   75  675 185 HOH   HOH B . 
K 5 HOH   76  676 305 HOH   HOH B . 
K 5 HOH   77  677 271 HOH   HOH B . 
K 5 HOH   78  678 230 HOH   HOH B . 
K 5 HOH   79  679 381 HOH   HOH B . 
K 5 HOH   80  680 299 HOH   HOH B . 
K 5 HOH   81  681 24  HOH   HOH B . 
K 5 HOH   82  682 323 HOH   HOH B . 
K 5 HOH   83  683 140 HOH   HOH B . 
K 5 HOH   84  684 389 HOH   HOH B . 
K 5 HOH   85  685 192 HOH   HOH B . 
K 5 HOH   86  686 216 HOH   HOH B . 
K 5 HOH   87  687 186 HOH   HOH B . 
K 5 HOH   88  688 194 HOH   HOH B . 
K 5 HOH   89  689 345 HOH   HOH B . 
K 5 HOH   90  690 360 HOH   HOH B . 
K 5 HOH   91  691 386 HOH   HOH B . 
K 5 HOH   92  692 48  HOH   HOH B . 
K 5 HOH   93  693 201 HOH   HOH B . 
K 5 HOH   94  694 395 HOH   HOH B . 
K 5 HOH   95  695 243 HOH   HOH B . 
K 5 HOH   96  696 198 HOH   HOH B . 
K 5 HOH   97  697 106 HOH   HOH B . 
K 5 HOH   98  698 132 HOH   HOH B . 
K 5 HOH   99  699 7   HOH   HOH B . 
K 5 HOH   100 700 324 HOH   HOH B . 
K 5 HOH   101 701 249 HOH   HOH B . 
K 5 HOH   102 702 100 HOH   HOH B . 
K 5 HOH   103 703 302 HOH   HOH B . 
K 5 HOH   104 704 130 HOH   HOH B . 
K 5 HOH   105 705 114 HOH   HOH B . 
K 5 HOH   106 706 183 HOH   HOH B . 
K 5 HOH   107 707 131 HOH   HOH B . 
K 5 HOH   108 708 72  HOH   HOH B . 
K 5 HOH   109 709 97  HOH   HOH B . 
K 5 HOH   110 710 219 HOH   HOH B . 
K 5 HOH   111 711 91  HOH   HOH B . 
K 5 HOH   112 712 153 HOH   HOH B . 
K 5 HOH   113 713 122 HOH   HOH B . 
K 5 HOH   114 714 378 HOH   HOH B . 
K 5 HOH   115 715 112 HOH   HOH B . 
K 5 HOH   116 716 84  HOH   HOH B . 
K 5 HOH   117 717 176 HOH   HOH B . 
K 5 HOH   118 718 285 HOH   HOH B . 
K 5 HOH   119 719 107 HOH   HOH B . 
K 5 HOH   120 720 172 HOH   HOH B . 
K 5 HOH   121 721 259 HOH   HOH B . 
K 5 HOH   122 722 104 HOH   HOH B . 
K 5 HOH   123 723 94  HOH   HOH B . 
K 5 HOH   124 724 88  HOH   HOH B . 
K 5 HOH   125 725 377 HOH   HOH B . 
K 5 HOH   126 726 355 HOH   HOH B . 
K 5 HOH   127 727 267 HOH   HOH B . 
K 5 HOH   128 728 269 HOH   HOH B . 
K 5 HOH   129 729 215 HOH   HOH B . 
K 5 HOH   130 730 255 HOH   HOH B . 
K 5 HOH   131 731 316 HOH   HOH B . 
K 5 HOH   132 732 382 HOH   HOH B . 
K 5 HOH   133 733 278 HOH   HOH B . 
K 5 HOH   134 734 237 HOH   HOH B . 
K 5 HOH   135 735 146 HOH   HOH B . 
K 5 HOH   136 736 391 HOH   HOH B . 
K 5 HOH   137 737 276 HOH   HOH B . 
K 5 HOH   138 738 273 HOH   HOH B . 
K 5 HOH   139 739 320 HOH   HOH B . 
K 5 HOH   140 740 290 HOH   HOH B . 
K 5 HOH   141 741 288 HOH   HOH B . 
K 5 HOH   142 742 286 HOH   HOH B . 
K 5 HOH   143 743 394 HOH   HOH B . 
K 5 HOH   144 744 356 HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLN 4   ? CG  ? A GLN 19  CG  
2  1 Y 1 A GLN 4   ? CD  ? A GLN 19  CD  
3  1 Y 1 A GLN 4   ? OE1 ? A GLN 19  OE1 
4  1 Y 1 A GLN 4   ? NE2 ? A GLN 19  NE2 
5  1 Y 1 A HIS 7   ? CG  ? A HIS 22  CG  
6  1 Y 1 A HIS 7   ? ND1 ? A HIS 22  ND1 
7  1 Y 1 A HIS 7   ? CD2 ? A HIS 22  CD2 
8  1 Y 1 A HIS 7   ? CE1 ? A HIS 22  CE1 
9  1 Y 1 A HIS 7   ? NE2 ? A HIS 22  NE2 
10 1 Y 1 A TRP 9   ? CG  ? A TRP 24  CG  
11 1 Y 1 A TRP 9   ? CD1 ? A TRP 24  CD1 
12 1 Y 1 A TRP 9   ? CD2 ? A TRP 24  CD2 
13 1 Y 1 A TRP 9   ? NE1 ? A TRP 24  NE1 
14 1 Y 1 A TRP 9   ? CE2 ? A TRP 24  CE2 
15 1 Y 1 A TRP 9   ? CE3 ? A TRP 24  CE3 
16 1 Y 1 A TRP 9   ? CZ2 ? A TRP 24  CZ2 
17 1 Y 1 A TRP 9   ? CZ3 ? A TRP 24  CZ3 
18 1 Y 1 A TRP 9   ? CH2 ? A TRP 24  CH2 
19 1 Y 1 A LYS 13  ? CG  ? A LYS 28  CG  
20 1 Y 1 A LYS 13  ? CD  ? A LYS 28  CD  
21 1 Y 1 A LYS 13  ? CE  ? A LYS 28  CE  
22 1 Y 1 A LYS 13  ? NZ  ? A LYS 28  NZ  
23 1 Y 1 A GLU 14  ? CD  ? A GLU 29  CD  
24 1 Y 1 A GLU 14  ? OE1 ? A GLU 29  OE1 
25 1 Y 1 A GLU 14  ? OE2 ? A GLU 29  OE2 
26 1 Y 1 A GLU 19  ? CG  ? A GLU 34  CG  
27 1 Y 1 A GLU 19  ? CD  ? A GLU 34  CD  
28 1 Y 1 A GLU 19  ? OE1 ? A GLU 34  OE1 
29 1 Y 1 A GLU 19  ? OE2 ? A GLU 34  OE2 
30 1 Y 1 A LYS 116 ? NZ  ? A LYS 131 NZ  
31 1 Y 1 A LYS 186 ? CE  ? A LYS 201 CE  
32 1 Y 1 A LYS 186 ? NZ  ? A LYS 201 NZ  
33 1 Y 1 A LYS 224 ? CD  ? A LYS 239 CD  
34 1 Y 1 A LYS 224 ? CE  ? A LYS 239 CE  
35 1 Y 1 A LYS 224 ? NZ  ? A LYS 239 NZ  
36 1 Y 1 A GLU 318 ? CD  ? A GLU 333 CD  
37 1 Y 1 A GLU 318 ? OE1 ? A GLU 333 OE1 
38 1 Y 1 A GLU 318 ? OE2 ? A GLU 333 OE2 
39 1 Y 1 A LYS 337 ? CD  ? A LYS 352 CD  
40 1 Y 1 A LYS 337 ? CE  ? A LYS 352 CE  
41 1 Y 1 A LYS 337 ? NZ  ? A LYS 352 NZ  
42 1 Y 1 A GLN 361 ? CD  ? A GLN 376 CD  
43 1 Y 1 A GLN 361 ? OE1 ? A GLN 376 OE1 
44 1 Y 1 A GLN 361 ? NE2 ? A GLN 376 NE2 
45 1 Y 1 A LYS 377 ? CG  ? A LYS 392 CG  
46 1 Y 1 A LYS 377 ? CD  ? A LYS 392 CD  
47 1 Y 1 A LYS 377 ? CE  ? A LYS 392 CE  
48 1 Y 1 A LYS 377 ? NZ  ? A LYS 392 NZ  
49 1 Y 1 B LYS 13  ? CG  ? B LYS 28  CG  
50 1 Y 1 B LYS 13  ? CD  ? B LYS 28  CD  
51 1 Y 1 B LYS 13  ? CE  ? B LYS 28  CE  
52 1 Y 1 B LYS 13  ? NZ  ? B LYS 28  NZ  
53 1 Y 1 B GLU 14  ? CD  ? B GLU 29  CD  
54 1 Y 1 B GLU 14  ? OE1 ? B GLU 29  OE1 
55 1 Y 1 B GLU 14  ? OE2 ? B GLU 29  OE2 
56 1 Y 1 B GLU 19  ? CG  ? B GLU 34  CG  
57 1 Y 1 B GLU 19  ? CD  ? B GLU 34  CD  
58 1 Y 1 B GLU 19  ? OE1 ? B GLU 34  OE1 
59 1 Y 1 B GLU 19  ? OE2 ? B GLU 34  OE2 
60 1 Y 1 B LYS 116 ? NZ  ? B LYS 131 NZ  
61 1 Y 1 B LYS 186 ? CE  ? B LYS 201 CE  
62 1 Y 1 B LYS 186 ? NZ  ? B LYS 201 NZ  
63 1 Y 1 B LYS 224 ? CD  ? B LYS 239 CD  
64 1 Y 1 B LYS 224 ? CE  ? B LYS 239 CE  
65 1 Y 1 B LYS 224 ? NZ  ? B LYS 239 NZ  
66 1 Y 1 B LYS 337 ? CD  ? B LYS 352 CD  
67 1 Y 1 B LYS 337 ? CE  ? B LYS 352 CE  
68 1 Y 1 B LYS 337 ? NZ  ? B LYS 352 NZ  
69 1 Y 1 B LEU 374 ? CG  ? B LEU 389 CG  
70 1 Y 1 B LEU 374 ? CD1 ? B LEU 389 CD1 
71 1 Y 1 B LEU 374 ? CD2 ? B LEU 389 CD2 
72 1 Y 1 B LYS 401 ? CG  ? B LYS 416 CG  
73 1 Y 1 B LYS 401 ? CD  ? B LYS 416 CD  
74 1 Y 1 B LYS 401 ? CE  ? B LYS 416 CE  
75 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'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .      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                     9F5R 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     84.922 
_cell.length_a_esd                 ? 
_cell.length_b                     92.293 
_cell.length_b_esd                 ? 
_cell.length_c                     131.637 
_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                         9F5R 
_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                   9F5R 
_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             2.74 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.09 
_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 8000, 20% v/v ethylene glycol 0.02 M of each carboxylic acid 0.1 M MES/imidazole pH 6.5.
Carboxylic acids 0sodium formate, ammonium acetate, trisodium citrate, sodium potassium
l-tartrate, sodium oxamate
;
_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 EIGER2 X CdTe 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-02-21 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.8856 
_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                        'ESRF BEAMLINE ID23-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.8856 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID23-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9F5R 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.694 
_reflns.d_resolution_low                               75.57 
_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                                     82644 
_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                           71.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.155 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.994 
_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                                    1.694 
_reflns_shell.d_res_low                                     1.842 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.6 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4132 
_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                               1.61 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.715 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -0.3791 
_refine.aniso_B[1][2]                            0 
_refine.aniso_B[1][3]                            0 
_refine.aniso_B[2][2]                            0.4465 
_refine.aniso_B[2][3]                            0 
_refine.aniso_B[3][3]                            -0.0674 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               30.63 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.942 
_refine.correlation_coeff_Fo_to_Fc_free          0.93 
_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                                 9F5R 
_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                            1.694 
_refine.ls_d_res_low                             24.48 
_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                     82595 
_refine.ls_number_reflns_R_free                  4164 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    71.7 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2184 
_refine.ls_R_factor_R_free                       0.2388 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2173 
_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   0.127 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.127 
_refine.pdbx_overall_SU_R_Blow_DPI               0.141 
_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             0.14 
_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                        9F5R 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.27 
_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                       1.694 
_refine_hist.d_res_low                        24.48 
_refine_hist.number_atoms_solvent             350 
_refine_hist.number_atoms_total               6504 
_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        5998 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         156 
_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' ? 0.01  ? 6380 ? t_bond_d                  2  HARMONIC     
'X-RAY DIFFRACTION' ? 0.95  ? 8670 ? t_angle_deg               2  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 2228 ? t_dihedral_angle_d        2  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? 1140 ? t_gen_planes              5  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 6380 ? t_it                      10 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 788  ? t_chiral_improper_torsion 5  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? 5591 ? t_ideal_dist_contact      4  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? 3.2   ? ?    ? t_omega_torsion           ?  ?            
'X-RAY DIFFRACTION' ? 16.02 ? ?    ? t_other_torsion           ?  ?            
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.694 
_refine_ls_shell.d_res_low                        1.79 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             81 
_refine_ls_shell.number_reflns_R_work             ? 
_refine_ls_shell.percent_reflns_obs               9.91 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2827 
_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                  0.3137 
# 
_struct.entry_id                     9F5R 
_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               Y 
# 
_struct_keywords.entry_id        9F5R 
_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 4 ? 
F N N 2 ? 
G N N 3 ? 
H N N 4 ? 
I N N 4 ? 
J N N 5 ? 
K N N 5 ? 
# 
_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 9F5R A 24 ? 418 ? P14902 9 ? 403 ? 9 403 
2 1 9F5R 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 9F5R MET A 1  ? UNP P14902 ? ? 'initiating methionine' -14 1  
1 9F5R GLY A 2  ? UNP P14902 ? ? 'expression tag'        -13 2  
1 9F5R SER A 3  ? UNP P14902 ? ? 'expression tag'        -12 3  
1 9F5R SER A 4  ? UNP P14902 ? ? 'expression tag'        -11 4  
1 9F5R HIS A 5  ? UNP P14902 ? ? 'expression tag'        -10 5  
1 9F5R HIS A 6  ? UNP P14902 ? ? 'expression tag'        -9  6  
1 9F5R HIS A 7  ? UNP P14902 ? ? 'expression tag'        -8  7  
1 9F5R HIS A 8  ? UNP P14902 ? ? 'expression tag'        -7  8  
1 9F5R HIS A 9  ? UNP P14902 ? ? 'expression tag'        -6  9  
1 9F5R HIS A 10 ? UNP P14902 ? ? 'expression tag'        -5  10 
1 9F5R SER A 11 ? UNP P14902 ? ? 'expression tag'        -4  11 
1 9F5R ALA A 12 ? UNP P14902 ? ? 'expression tag'        -3  12 
1 9F5R ALA A 13 ? UNP P14902 ? ? 'expression tag'        -2  13 
1 9F5R LEU A 14 ? UNP P14902 ? ? 'expression tag'        -1  14 
1 9F5R GLU A 15 ? UNP P14902 ? ? 'expression tag'        0   15 
1 9F5R VAL A 16 ? UNP P14902 ? ? 'expression tag'        1   16 
1 9F5R LEU A 17 ? UNP P14902 ? ? 'expression tag'        2   17 
1 9F5R PHE A 18 ? UNP P14902 ? ? 'expression tag'        3   18 
1 9F5R GLN A 19 ? UNP P14902 ? ? 'expression tag'        4   19 
1 9F5R GLY A 20 ? UNP P14902 ? ? 'expression tag'        5   20 
1 9F5R PRO A 21 ? UNP P14902 ? ? 'expression tag'        6   21 
1 9F5R HIS A 22 ? UNP P14902 ? ? 'expression tag'        7   22 
1 9F5R MET A 23 ? UNP P14902 ? ? 'expression tag'        8   23 
2 9F5R MET B 1  ? UNP P14902 ? ? 'initiating methionine' -14 24 
2 9F5R GLY B 2  ? UNP P14902 ? ? 'expression tag'        -13 25 
2 9F5R SER B 3  ? UNP P14902 ? ? 'expression tag'        -12 26 
2 9F5R SER B 4  ? UNP P14902 ? ? 'expression tag'        -11 27 
2 9F5R HIS B 5  ? UNP P14902 ? ? 'expression tag'        -10 28 
2 9F5R HIS B 6  ? UNP P14902 ? ? 'expression tag'        -9  29 
2 9F5R HIS B 7  ? UNP P14902 ? ? 'expression tag'        -8  30 
2 9F5R HIS B 8  ? UNP P14902 ? ? 'expression tag'        -7  31 
2 9F5R HIS B 9  ? UNP P14902 ? ? 'expression tag'        -6  32 
2 9F5R HIS B 10 ? UNP P14902 ? ? 'expression tag'        -5  33 
2 9F5R SER B 11 ? UNP P14902 ? ? 'expression tag'        -4  34 
2 9F5R ALA B 12 ? UNP P14902 ? ? 'expression tag'        -3  35 
2 9F5R ALA B 13 ? UNP P14902 ? ? 'expression tag'        -2  36 
2 9F5R LEU B 14 ? UNP P14902 ? ? 'expression tag'        -1  37 
2 9F5R GLU B 15 ? UNP P14902 ? ? 'expression tag'        0   38 
2 9F5R VAL B 16 ? UNP P14902 ? ? 'expression tag'        1   39 
2 9F5R LEU B 17 ? UNP P14902 ? ? 'expression tag'        2   40 
2 9F5R PHE B 18 ? UNP P14902 ? ? 'expression tag'        3   41 
2 9F5R GLN B 19 ? UNP P14902 ? ? 'expression tag'        4   42 
2 9F5R GLY B 20 ? UNP P14902 ? ? 'expression tag'        5   43 
2 9F5R PRO B 21 ? UNP P14902 ? ? 'expression tag'        6   44 
2 9F5R HIS B 22 ? UNP P14902 ? ? 'expression tag'        7   45 
2 9F5R MET B 23 ? UNP P14902 ? ? 'expression tag'        8   46 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,J   
2 1 B,F,G,H,I,K 
# 
_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 SER A 27  ? HIS A 31  ? SER A 12  HIS A 16  5 ? 5  
HELX_P HELX_P2  AA2 PRO A 48  ? PHE A 50  ? PRO A 33  PHE A 35  5 ? 3  
HELX_P HELX_P3  AA3 TYR A 51  ? HIS A 60  ? TYR A 36  HIS A 45  1 ? 10 
HELX_P HELX_P4  AA4 HIS A 60  ? SER A 67  ? HIS A 45  SER A 52  1 ? 8  
HELX_P HELX_P5  AA5 GLN A 69  ? LEU A 77  ? GLN A 54  LEU A 62  1 ? 9  
HELX_P HELX_P6  AA6 SER A 81  ? LEU A 85  ? SER A 66  LEU A 70  5 ? 5  
HELX_P HELX_P7  AA7 ASP A 87  ? GLY A 108 ? ASP A 72  GLY A 93  1 ? 22 
HELX_P HELX_P8  AA8 PRO A 119 ? GLU A 134 ? PRO A 104 GLU A 119 1 ? 16 
HELX_P HELX_P9  AA9 VAL A 140 ? VAL A 145 ? VAL A 125 VAL A 130 1 ? 6  
HELX_P HELX_P10 AB1 THR A 159 ? GLU A 161 ? THR A 144 GLU A 146 5 ? 3  
HELX_P HELX_P11 AB2 CYS A 174 ? SER A 191 ? CYS A 159 SER A 176 1 ? 18 
HELX_P HELX_P12 AB3 ALA A 192 ? LYS A 194 ? ALA A 177 LYS A 179 5 ? 3  
HELX_P HELX_P13 AB4 VAL A 195 ? MET A 205 ? VAL A 180 MET A 190 1 ? 11 
HELX_P HELX_P14 AB5 GLU A 207 ? HIS A 230 ? GLU A 192 HIS A 215 1 ? 24 
HELX_P HELX_P15 AB6 GLN A 231 ? VAL A 236 ? GLN A 216 VAL A 221 1 ? 6  
HELX_P HELX_P16 AB7 ASN A 237 ? VAL A 244 ? ASN A 222 VAL A 229 1 ? 8  
HELX_P HELX_P17 AB8 VAL A 244 ? SER A 250 ? VAL A 229 SER A 235 1 ? 7  
HELX_P HELX_P18 AB9 ASN A 255 ? SER A 259 ? ASN A 240 SER A 244 5 ? 5  
HELX_P HELX_P19 AC1 SER A 278 ? GLN A 281 ? SER A 263 GLN A 266 5 ? 4  
HELX_P HELX_P20 AC2 SER A 282 ? LEU A 292 ? SER A 267 LEU A 277 1 ? 11 
HELX_P HELX_P21 AC3 GLY A 301 ? ARG A 312 ? GLY A 286 ARG A 297 1 ? 12 
HELX_P HELX_P22 AC4 PRO A 315 ? ASN A 328 ? PRO A 300 ASN A 313 1 ? 14 
HELX_P HELX_P23 AC5 SER A 330 ? SER A 337 ? SER A 315 SER A 322 1 ? 8  
HELX_P HELX_P24 AC6 ASP A 340 ? ILE A 369 ? ASP A 325 ILE A 354 1 ? 30 
HELX_P HELX_P25 AC7 ILE A 369 ? GLN A 375 ? ILE A 354 GLN A 360 1 ? 7  
HELX_P HELX_P26 AC8 ASP A 398 ? LYS A 412 ? ASP A 383 LYS A 397 1 ? 15 
HELX_P HELX_P27 AC9 SER B 27  ? HIS B 31  ? SER B 12  HIS B 16  5 ? 5  
HELX_P HELX_P28 AD1 PRO B 48  ? PHE B 50  ? PRO B 33  PHE B 35  5 ? 3  
HELX_P HELX_P29 AD2 TYR B 51  ? HIS B 60  ? TYR B 36  HIS B 45  1 ? 10 
HELX_P HELX_P30 AD3 HIS B 60  ? SER B 67  ? HIS B 45  SER B 52  1 ? 8  
HELX_P HELX_P31 AD4 GLN B 69  ? LEU B 77  ? GLN B 54  LEU B 62  1 ? 9  
HELX_P HELX_P32 AD5 SER B 81  ? LEU B 85  ? SER B 66  LEU B 70  5 ? 5  
HELX_P HELX_P33 AD6 ASP B 87  ? GLY B 108 ? ASP B 72  GLY B 93  1 ? 22 
HELX_P HELX_P34 AD7 PRO B 119 ? GLU B 134 ? PRO B 104 GLU B 119 1 ? 16 
HELX_P HELX_P35 AD8 VAL B 140 ? VAL B 145 ? VAL B 125 VAL B 130 1 ? 6  
HELX_P HELX_P36 AD9 THR B 159 ? GLU B 161 ? THR B 144 GLU B 146 5 ? 3  
HELX_P HELX_P37 AE1 CYS B 174 ? SER B 191 ? CYS B 159 SER B 176 1 ? 18 
HELX_P HELX_P38 AE2 ALA B 192 ? LYS B 194 ? ALA B 177 LYS B 179 5 ? 3  
HELX_P HELX_P39 AE3 VAL B 195 ? MET B 205 ? VAL B 180 MET B 190 1 ? 11 
HELX_P HELX_P40 AE4 GLU B 207 ? HIS B 230 ? GLU B 192 HIS B 215 1 ? 24 
HELX_P HELX_P41 AE5 GLN B 231 ? VAL B 236 ? GLN B 216 VAL B 221 1 ? 6  
HELX_P HELX_P42 AE6 ASN B 237 ? VAL B 244 ? ASN B 222 VAL B 229 1 ? 8  
HELX_P HELX_P43 AE7 VAL B 244 ? SER B 250 ? VAL B 229 SER B 235 1 ? 7  
HELX_P HELX_P44 AE8 ASN B 255 ? SER B 259 ? ASN B 240 SER B 244 5 ? 5  
HELX_P HELX_P45 AE9 SER B 278 ? GLN B 281 ? SER B 263 GLN B 266 5 ? 4  
HELX_P HELX_P46 AF1 SER B 282 ? LEU B 292 ? SER B 267 LEU B 277 1 ? 11 
HELX_P HELX_P47 AF2 GLY B 301 ? ARG B 312 ? GLY B 286 ARG B 297 1 ? 12 
HELX_P HELX_P48 AF3 PRO B 315 ? ASN B 328 ? PRO B 300 ASN B 313 1 ? 14 
HELX_P HELX_P49 AF4 SER B 330 ? SER B 337 ? SER B 315 SER B 322 1 ? 8  
HELX_P HELX_P50 AF5 ASP B 340 ? ILE B 369 ? ASP B 325 ILE B 354 1 ? 30 
HELX_P HELX_P51 AF6 ILE B 369 ? GLN B 375 ? ILE B 354 GLN B 360 1 ? 7  
HELX_P HELX_P52 AF7 ASP B 398 ? LYS B 412 ? ASP B 383 LYS B 397 1 ? 15 
# 
_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 ? ? ? ? ? ? ? 2.852 ? ? 
metalc1 metalc ? ? A HIS 361 NE2 ? ? ? 1_555 C HEM   .   FE ? ? A HIS 346 A HEM   501 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
metalc2 metalc ? ? C HEM .   FE  ? ? ? 1_555 D A1H93 .   N5 ? ? A HEM 501 A A1H93 502 1_555 ? ? ? ? ? ? ? 2.015 ? ? 
metalc3 metalc ? ? B HIS 361 NE2 ? ? ? 1_555 F HEM   .   FE ? ? B HIS 346 B HEM   501 1_555 ? ? ? ? ? ? ? 2.049 ? ? 
metalc4 metalc ? ? F HEM .   FE  ? ? ? 1_555 G A1H93 .   N5 ? ? B HEM 501 B A1H93 502 1_555 ? ? ? ? ? ? ? 1.988 ? ? 
# 
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 89.0  ? 
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 89.8  ? 
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 89.6  ? 
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 93.7  ? 
5  NA  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NC ? C HEM   . ? A HEM   501 ? 1_555 177.2 ? 
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 91.1  ? 
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 89.5  ? 
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 89.7  ? 
9  NB  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM   . ? A HEM   501 ? 1_555 179.1 ? 
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 89.6  ? 
11 NE2 ? A HIS 361 ? A HIS 346 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 N5 ? D A1H93 . ? A A1H93 502 ? 1_555 177.9 ? 
12 NA  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 N5 ? D A1H93 . ? A A1H93 502 ? 1_555 92.1  ? 
13 NB  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 N5 ? D A1H93 . ? A A1H93 502 ? 1_555 88.4  ? 
14 NC  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 N5 ? D A1H93 . ? A A1H93 502 ? 1_555 85.3  ? 
15 ND  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 N5 ? D A1H93 . ? A A1H93 502 ? 1_555 92.3  ? 
16 NE2 ? B HIS 361 ? B HIS 346 ? 1_555 FE ? F HEM . ? B HEM 501 ? 1_555 NA ? F HEM   . ? B HEM   501 ? 1_555 89.0  ? 
17 NE2 ? B HIS 361 ? B HIS 346 ? 1_555 FE ? F HEM . ? B HEM 501 ? 1_555 NB ? F HEM   . ? B HEM   501 ? 1_555 88.9  ? 
18 NA  ? F HEM .   ? B HEM 501 ? 1_555 FE ? F HEM . ? B HEM 501 ? 1_555 NB ? F HEM   . ? B HEM   501 ? 1_555 90.3  ? 
19 NE2 ? B HIS 361 ? B HIS 346 ? 1_555 FE ? F HEM . ? B HEM 501 ? 1_555 NC ? F HEM   . ? B HEM   501 ? 1_555 92.0  ? 
20 NA  ? F HEM .   ? B HEM 501 ? 1_555 FE ? F HEM . ? B HEM 501 ? 1_555 NC ? F HEM   . ? B HEM   501 ? 1_555 178.7 ? 
21 NB  ? F HEM .   ? B HEM 501 ? 1_555 FE ? F HEM . ? B HEM 501 ? 1_555 NC ? F HEM   . ? B HEM   501 ? 1_555 90.6  ? 
22 NE2 ? B HIS 361 ? B HIS 346 ? 1_555 FE ? F HEM . ? B HEM 501 ? 1_555 ND ? F HEM   . ? B HEM   501 ? 1_555 88.4  ? 
23 NA  ? F HEM .   ? B HEM 501 ? 1_555 FE ? F HEM . ? B HEM 501 ? 1_555 ND ? F HEM   . ? B HEM   501 ? 1_555 89.7  ? 
24 NB  ? F HEM .   ? B HEM 501 ? 1_555 FE ? F HEM . ? B HEM 501 ? 1_555 ND ? F HEM   . ? B HEM   501 ? 1_555 177.3 ? 
25 NC  ? F HEM .   ? B HEM 501 ? 1_555 FE ? F HEM . ? B HEM 501 ? 1_555 ND ? F HEM   . ? B HEM   501 ? 1_555 89.5  ? 
26 NE2 ? B HIS 361 ? B HIS 346 ? 1_555 FE ? F HEM . ? B HEM 501 ? 1_555 N5 ? G A1H93 . ? B A1H93 502 ? 1_555 177.3 ? 
27 NA  ? F HEM .   ? B HEM 501 ? 1_555 FE ? F HEM . ? B HEM 501 ? 1_555 N5 ? G A1H93 . ? B A1H93 502 ? 1_555 93.1  ? 
28 NB  ? F HEM .   ? B HEM 501 ? 1_555 FE ? F HEM . ? B HEM 501 ? 1_555 N5 ? G A1H93 . ? B A1H93 502 ? 1_555 89.4  ? 
29 NC  ? F HEM .   ? B HEM 501 ? 1_555 FE ? F HEM . ? B HEM 501 ? 1_555 N5 ? G A1H93 . ? B A1H93 502 ? 1_555 85.9  ? 
30 ND  ? F HEM .   ? B HEM 501 ? 1_555 FE ? F HEM . ? B HEM 501 ? 1_555 N5 ? G A1H93 . ? B A1H93 502 ? 1_555 93.3  ? 
# 
_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                   9F5R 
_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 ASN A 27  ? A 36.01   65.90  
2  1 ASN A 27  ? B 35.09   66.85  
3  1 ASN A 133 ? ? -105.36 55.05  
4  1 ILE A 354 ? ? -120.80 -60.08 
5  1 LYS A 401 ? ? -128.80 -73.78 
6  1 GLU A 402 ? ? -31.95  113.30 
7  1 ASN B 27  ? A 37.13   66.12  
8  1 ASN B 27  ? B 35.43   67.40  
9  1 ASN B 133 ? ? -103.28 54.71  
10 1 ILE B 354 ? ? -120.27 -58.46 
# 
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 ALA -2  ? A ALA 13  
14 1 Y 1 A LEU -1  ? A LEU 14  
15 1 Y 1 A GLU 0   ? A GLU 15  
16 1 Y 1 A VAL 1   ? A VAL 16  
17 1 Y 1 A LEU 2   ? A LEU 17  
18 1 Y 1 A PHE 3   ? A PHE 18  
19 1 Y 1 A PRO 362 ? A PRO 377 
20 1 Y 1 A LYS 363 ? A LYS 378 
21 1 Y 1 A GLU 364 ? A GLU 379 
22 1 Y 1 A ASN 365 ? A ASN 380 
23 1 Y 1 A LYS 366 ? A LYS 381 
24 1 Y 1 A THR 367 ? A THR 382 
25 1 Y 1 A SER 368 ? A SER 383 
26 1 Y 1 A GLU 369 ? A GLU 384 
27 1 Y 1 A ASP 370 ? A ASP 385 
28 1 Y 1 A PRO 371 ? A PRO 386 
29 1 Y 1 A SER 372 ? A SER 387 
30 1 Y 1 A LYS 373 ? A LYS 388 
31 1 Y 1 A LEU 374 ? A LEU 389 
32 1 Y 1 A GLU 375 ? A GLU 390 
33 1 Y 1 B MET -14 ? B MET 1   
34 1 Y 1 B GLY -13 ? B GLY 2   
35 1 Y 1 B SER -12 ? B SER 3   
36 1 Y 1 B SER -11 ? B SER 4   
37 1 Y 1 B HIS -10 ? B HIS 5   
38 1 Y 1 B HIS -9  ? B HIS 6   
39 1 Y 1 B HIS -8  ? B HIS 7   
40 1 Y 1 B HIS -7  ? B HIS 8   
41 1 Y 1 B HIS -6  ? B HIS 9   
42 1 Y 1 B HIS -5  ? B HIS 10  
43 1 Y 1 B SER -4  ? B SER 11  
44 1 Y 1 B ALA -3  ? B ALA 12  
45 1 Y 1 B ALA -2  ? B ALA 13  
46 1 Y 1 B LEU -1  ? B LEU 14  
47 1 Y 1 B GLU 0   ? B GLU 15  
48 1 Y 1 B VAL 1   ? B VAL 16  
49 1 Y 1 B LEU 2   ? B LEU 17  
50 1 Y 1 B PHE 3   ? B PHE 18  
51 1 Y 1 B GLN 4   ? B GLN 19  
52 1 Y 1 B GLY 5   ? B GLY 20  
53 1 Y 1 B PRO 6   ? B PRO 21  
54 1 Y 1 B HIS 7   ? B HIS 22  
55 1 Y 1 B MET 8   ? B MET 23  
56 1 Y 1 B TRP 9   ? B TRP 24  
57 1 Y 1 B THR 10  ? B THR 25  
58 1 Y 1 B PRO 362 ? B PRO 377 
59 1 Y 1 B LYS 363 ? B LYS 378 
60 1 Y 1 B GLU 364 ? B GLU 379 
61 1 Y 1 B ASN 365 ? B ASN 380 
62 1 Y 1 B LYS 366 ? B LYS 381 
63 1 Y 1 B THR 367 ? B THR 382 
64 1 Y 1 B SER 368 ? B SER 383 
65 1 Y 1 B GLU 369 ? B GLU 384 
66 1 Y 1 B ASP 370 ? B ASP 385 
67 1 Y 1 B PRO 371 ? B PRO 386 
68 1 Y 1 B GLU 402 ? B GLU 417 
69 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 
A1H93 N1   N  Y N 1   
A1H93 N3   N  Y N 2   
A1H93 C4   C  Y N 3   
A1H93 C5   C  Y N 4   
A1H93 C6   C  Y N 5   
A1H93 C7   C  N R 6   
A1H93 C8   C  Y N 7   
A1H93 C10  C  N N 8   
A1H93 C13  C  Y N 9   
A1H93 C15  C  Y N 10  
A1H93 C17  C  Y N 11  
A1H93 C1   C  N N 12  
A1H93 O1   O  N N 13  
A1H93 C2   C  Y N 14  
A1H93 C3   C  Y N 15  
A1H93 N2   N  Y N 16  
A1H93 C9   C  Y N 17  
A1H93 C11  C  N N 18  
A1H93 C12  C  N N 19  
A1H93 N4   N  Y N 20  
A1H93 C14  C  Y N 21  
A1H93 N5   N  Y N 22  
A1H93 C16  C  Y N 23  
A1H93 N6   N  Y N 24  
A1H93 O2   O  N N 25  
A1H93 C18  C  Y N 26  
A1H93 F1   F  N N 27  
A1H93 C19  C  Y N 28  
A1H93 F2   F  N N 29  
A1H93 H5   H  N N 30  
A1H93 H6   H  N N 31  
A1H93 H11  H  N N 32  
A1H93 H15  H  N N 33  
A1H93 H3   H  N N 34  
A1H93 H2   H  N N 35  
A1H93 H1   H  N N 36  
A1H93 H4   H  N N 37  
A1H93 H8   H  N N 38  
A1H93 H7   H  N N 39  
A1H93 H10  H  N N 40  
A1H93 H9   H  N N 41  
A1H93 H14  H  N N 42  
A1H93 H16  H  N N 43  
A1H93 H12  H  N N 44  
A1H93 H17  H  N N 45  
ALA   N    N  N N 46  
ALA   CA   C  N S 47  
ALA   C    C  N N 48  
ALA   O    O  N N 49  
ALA   CB   C  N N 50  
ALA   OXT  O  N N 51  
ALA   H    H  N N 52  
ALA   H2   H  N N 53  
ALA   HA   H  N N 54  
ALA   HB1  H  N N 55  
ALA   HB2  H  N N 56  
ALA   HB3  H  N N 57  
ALA   HXT  H  N N 58  
ARG   N    N  N N 59  
ARG   CA   C  N S 60  
ARG   C    C  N N 61  
ARG   O    O  N N 62  
ARG   CB   C  N N 63  
ARG   CG   C  N N 64  
ARG   CD   C  N N 65  
ARG   NE   N  N N 66  
ARG   CZ   C  N N 67  
ARG   NH1  N  N N 68  
ARG   NH2  N  N N 69  
ARG   OXT  O  N N 70  
ARG   H    H  N N 71  
ARG   H2   H  N N 72  
ARG   HA   H  N N 73  
ARG   HB2  H  N N 74  
ARG   HB3  H  N N 75  
ARG   HG2  H  N N 76  
ARG   HG3  H  N N 77  
ARG   HD2  H  N N 78  
ARG   HD3  H  N N 79  
ARG   HE   H  N N 80  
ARG   HH11 H  N N 81  
ARG   HH12 H  N N 82  
ARG   HH21 H  N N 83  
ARG   HH22 H  N N 84  
ARG   HXT  H  N N 85  
ASN   N    N  N N 86  
ASN   CA   C  N S 87  
ASN   C    C  N N 88  
ASN   O    O  N N 89  
ASN   CB   C  N N 90  
ASN   CG   C  N N 91  
ASN   OD1  O  N N 92  
ASN   ND2  N  N N 93  
ASN   OXT  O  N N 94  
ASN   H    H  N N 95  
ASN   H2   H  N N 96  
ASN   HA   H  N N 97  
ASN   HB2  H  N N 98  
ASN   HB3  H  N N 99  
ASN   HD21 H  N N 100 
ASN   HD22 H  N N 101 
ASN   HXT  H  N N 102 
ASP   N    N  N N 103 
ASP   CA   C  N S 104 
ASP   C    C  N N 105 
ASP   O    O  N N 106 
ASP   CB   C  N N 107 
ASP   CG   C  N N 108 
ASP   OD1  O  N N 109 
ASP   OD2  O  N N 110 
ASP   OXT  O  N N 111 
ASP   H    H  N N 112 
ASP   H2   H  N N 113 
ASP   HA   H  N N 114 
ASP   HB2  H  N N 115 
ASP   HB3  H  N N 116 
ASP   HD2  H  N N 117 
ASP   HXT  H  N N 118 
CYS   N    N  N N 119 
CYS   CA   C  N R 120 
CYS   C    C  N N 121 
CYS   O    O  N N 122 
CYS   CB   C  N N 123 
CYS   SG   S  N N 124 
CYS   OXT  O  N N 125 
CYS   H    H  N N 126 
CYS   H2   H  N N 127 
CYS   HA   H  N N 128 
CYS   HB2  H  N N 129 
CYS   HB3  H  N N 130 
CYS   HG   H  N N 131 
CYS   HXT  H  N N 132 
DMS   S    S  N N 133 
DMS   O    O  N N 134 
DMS   C1   C  N N 135 
DMS   C2   C  N N 136 
DMS   H11  H  N N 137 
DMS   H12  H  N N 138 
DMS   H13  H  N N 139 
DMS   H21  H  N N 140 
DMS   H22  H  N N 141 
DMS   H23  H  N N 142 
GLN   N    N  N N 143 
GLN   CA   C  N S 144 
GLN   C    C  N N 145 
GLN   O    O  N N 146 
GLN   CB   C  N N 147 
GLN   CG   C  N N 148 
GLN   CD   C  N N 149 
GLN   OE1  O  N N 150 
GLN   NE2  N  N N 151 
GLN   OXT  O  N N 152 
GLN   H    H  N N 153 
GLN   H2   H  N N 154 
GLN   HA   H  N N 155 
GLN   HB2  H  N N 156 
GLN   HB3  H  N N 157 
GLN   HG2  H  N N 158 
GLN   HG3  H  N N 159 
GLN   HE21 H  N N 160 
GLN   HE22 H  N N 161 
GLN   HXT  H  N N 162 
GLU   N    N  N N 163 
GLU   CA   C  N S 164 
GLU   C    C  N N 165 
GLU   O    O  N N 166 
GLU   CB   C  N N 167 
GLU   CG   C  N N 168 
GLU   CD   C  N N 169 
GLU   OE1  O  N N 170 
GLU   OE2  O  N N 171 
GLU   OXT  O  N N 172 
GLU   H    H  N N 173 
GLU   H2   H  N N 174 
GLU   HA   H  N N 175 
GLU   HB2  H  N N 176 
GLU   HB3  H  N N 177 
GLU   HG2  H  N N 178 
GLU   HG3  H  N N 179 
GLU   HE2  H  N N 180 
GLU   HXT  H  N N 181 
GLY   N    N  N N 182 
GLY   CA   C  N N 183 
GLY   C    C  N N 184 
GLY   O    O  N N 185 
GLY   OXT  O  N N 186 
GLY   H    H  N N 187 
GLY   H2   H  N N 188 
GLY   HA2  H  N N 189 
GLY   HA3  H  N N 190 
GLY   HXT  H  N N 191 
HEM   CHA  C  N N 192 
HEM   CHB  C  N N 193 
HEM   CHC  C  N N 194 
HEM   CHD  C  N N 195 
HEM   C1A  C  Y N 196 
HEM   C2A  C  Y N 197 
HEM   C3A  C  Y N 198 
HEM   C4A  C  Y N 199 
HEM   CMA  C  N N 200 
HEM   CAA  C  N N 201 
HEM   CBA  C  N N 202 
HEM   CGA  C  N N 203 
HEM   O1A  O  N N 204 
HEM   O2A  O  N N 205 
HEM   C1B  C  N N 206 
HEM   C2B  C  N N 207 
HEM   C3B  C  N N 208 
HEM   C4B  C  N N 209 
HEM   CMB  C  N N 210 
HEM   CAB  C  N N 211 
HEM   CBB  C  N N 212 
HEM   C1C  C  Y N 213 
HEM   C2C  C  Y N 214 
HEM   C3C  C  Y N 215 
HEM   C4C  C  Y N 216 
HEM   CMC  C  N N 217 
HEM   CAC  C  N N 218 
HEM   CBC  C  N N 219 
HEM   C1D  C  N N 220 
HEM   C2D  C  N N 221 
HEM   C3D  C  N N 222 
HEM   C4D  C  N N 223 
HEM   CMD  C  N N 224 
HEM   CAD  C  N N 225 
HEM   CBD  C  N N 226 
HEM   CGD  C  N N 227 
HEM   O1D  O  N N 228 
HEM   O2D  O  N N 229 
HEM   NA   N  Y N 230 
HEM   NB   N  N N 231 
HEM   NC   N  Y N 232 
HEM   ND   N  N N 233 
HEM   FE   FE N N 234 
HEM   HHB  H  N N 235 
HEM   HHC  H  N N 236 
HEM   HHD  H  N N 237 
HEM   HMA  H  N N 238 
HEM   HMAA H  N N 239 
HEM   HMAB H  N N 240 
HEM   HAA  H  N N 241 
HEM   HAAA H  N N 242 
HEM   HBA  H  N N 243 
HEM   HBAA H  N N 244 
HEM   HMB  H  N N 245 
HEM   HMBA H  N N 246 
HEM   HMBB H  N N 247 
HEM   HAB  H  N N 248 
HEM   HBB  H  N N 249 
HEM   HBBA H  N N 250 
HEM   HMC  H  N N 251 
HEM   HMCA H  N N 252 
HEM   HMCB H  N N 253 
HEM   HAC  H  N N 254 
HEM   HBC  H  N N 255 
HEM   HBCA H  N N 256 
HEM   HMD  H  N N 257 
HEM   HMDA H  N N 258 
HEM   HMDB H  N N 259 
HEM   HAD  H  N N 260 
HEM   HADA H  N N 261 
HEM   HBD  H  N N 262 
HEM   HBDA H  N N 263 
HEM   H2A  H  N N 264 
HEM   H2D  H  N N 265 
HEM   HHA  H  N N 266 
HIS   N    N  N N 267 
HIS   CA   C  N S 268 
HIS   C    C  N N 269 
HIS   O    O  N N 270 
HIS   CB   C  N N 271 
HIS   CG   C  Y N 272 
HIS   ND1  N  Y N 273 
HIS   CD2  C  Y N 274 
HIS   CE1  C  Y N 275 
HIS   NE2  N  Y N 276 
HIS   OXT  O  N N 277 
HIS   H    H  N N 278 
HIS   H2   H  N N 279 
HIS   HA   H  N N 280 
HIS   HB2  H  N N 281 
HIS   HB3  H  N N 282 
HIS   HD1  H  N N 283 
HIS   HD2  H  N N 284 
HIS   HE1  H  N N 285 
HIS   HE2  H  N N 286 
HIS   HXT  H  N N 287 
HOH   O    O  N N 288 
HOH   H1   H  N N 289 
HOH   H2   H  N N 290 
ILE   N    N  N N 291 
ILE   CA   C  N S 292 
ILE   C    C  N N 293 
ILE   O    O  N N 294 
ILE   CB   C  N S 295 
ILE   CG1  C  N N 296 
ILE   CG2  C  N N 297 
ILE   CD1  C  N N 298 
ILE   OXT  O  N N 299 
ILE   H    H  N N 300 
ILE   H2   H  N N 301 
ILE   HA   H  N N 302 
ILE   HB   H  N N 303 
ILE   HG12 H  N N 304 
ILE   HG13 H  N N 305 
ILE   HG21 H  N N 306 
ILE   HG22 H  N N 307 
ILE   HG23 H  N N 308 
ILE   HD11 H  N N 309 
ILE   HD12 H  N N 310 
ILE   HD13 H  N N 311 
ILE   HXT  H  N N 312 
LEU   N    N  N N 313 
LEU   CA   C  N S 314 
LEU   C    C  N N 315 
LEU   O    O  N N 316 
LEU   CB   C  N N 317 
LEU   CG   C  N N 318 
LEU   CD1  C  N N 319 
LEU   CD2  C  N N 320 
LEU   OXT  O  N N 321 
LEU   H    H  N N 322 
LEU   H2   H  N N 323 
LEU   HA   H  N N 324 
LEU   HB2  H  N N 325 
LEU   HB3  H  N N 326 
LEU   HG   H  N N 327 
LEU   HD11 H  N N 328 
LEU   HD12 H  N N 329 
LEU   HD13 H  N N 330 
LEU   HD21 H  N N 331 
LEU   HD22 H  N N 332 
LEU   HD23 H  N N 333 
LEU   HXT  H  N N 334 
LYS   N    N  N N 335 
LYS   CA   C  N S 336 
LYS   C    C  N N 337 
LYS   O    O  N N 338 
LYS   CB   C  N N 339 
LYS   CG   C  N N 340 
LYS   CD   C  N N 341 
LYS   CE   C  N N 342 
LYS   NZ   N  N N 343 
LYS   OXT  O  N N 344 
LYS   H    H  N N 345 
LYS   H2   H  N N 346 
LYS   HA   H  N N 347 
LYS   HB2  H  N N 348 
LYS   HB3  H  N N 349 
LYS   HG2  H  N N 350 
LYS   HG3  H  N N 351 
LYS   HD2  H  N N 352 
LYS   HD3  H  N N 353 
LYS   HE2  H  N N 354 
LYS   HE3  H  N N 355 
LYS   HZ1  H  N N 356 
LYS   HZ2  H  N N 357 
LYS   HZ3  H  N N 358 
LYS   HXT  H  N N 359 
MET   N    N  N N 360 
MET   CA   C  N S 361 
MET   C    C  N N 362 
MET   O    O  N N 363 
MET   CB   C  N N 364 
MET   CG   C  N N 365 
MET   SD   S  N N 366 
MET   CE   C  N N 367 
MET   OXT  O  N N 368 
MET   H    H  N N 369 
MET   H2   H  N N 370 
MET   HA   H  N N 371 
MET   HB2  H  N N 372 
MET   HB3  H  N N 373 
MET   HG2  H  N N 374 
MET   HG3  H  N N 375 
MET   HE1  H  N N 376 
MET   HE2  H  N N 377 
MET   HE3  H  N N 378 
MET   HXT  H  N N 379 
PHE   N    N  N N 380 
PHE   CA   C  N S 381 
PHE   C    C  N N 382 
PHE   O    O  N N 383 
PHE   CB   C  N N 384 
PHE   CG   C  Y N 385 
PHE   CD1  C  Y N 386 
PHE   CD2  C  Y N 387 
PHE   CE1  C  Y N 388 
PHE   CE2  C  Y N 389 
PHE   CZ   C  Y N 390 
PHE   OXT  O  N N 391 
PHE   H    H  N N 392 
PHE   H2   H  N N 393 
PHE   HA   H  N N 394 
PHE   HB2  H  N N 395 
PHE   HB3  H  N N 396 
PHE   HD1  H  N N 397 
PHE   HD2  H  N N 398 
PHE   HE1  H  N N 399 
PHE   HE2  H  N N 400 
PHE   HZ   H  N N 401 
PHE   HXT  H  N N 402 
PRO   N    N  N N 403 
PRO   CA   C  N S 404 
PRO   C    C  N N 405 
PRO   O    O  N N 406 
PRO   CB   C  N N 407 
PRO   CG   C  N N 408 
PRO   CD   C  N N 409 
PRO   OXT  O  N N 410 
PRO   H    H  N N 411 
PRO   HA   H  N N 412 
PRO   HB2  H  N N 413 
PRO   HB3  H  N N 414 
PRO   HG2  H  N N 415 
PRO   HG3  H  N N 416 
PRO   HD2  H  N N 417 
PRO   HD3  H  N N 418 
PRO   HXT  H  N N 419 
SER   N    N  N N 420 
SER   CA   C  N S 421 
SER   C    C  N N 422 
SER   O    O  N N 423 
SER   CB   C  N N 424 
SER   OG   O  N N 425 
SER   OXT  O  N N 426 
SER   H    H  N N 427 
SER   H2   H  N N 428 
SER   HA   H  N N 429 
SER   HB2  H  N N 430 
SER   HB3  H  N N 431 
SER   HG   H  N N 432 
SER   HXT  H  N N 433 
THR   N    N  N N 434 
THR   CA   C  N S 435 
THR   C    C  N N 436 
THR   O    O  N N 437 
THR   CB   C  N R 438 
THR   OG1  O  N N 439 
THR   CG2  C  N N 440 
THR   OXT  O  N N 441 
THR   H    H  N N 442 
THR   H2   H  N N 443 
THR   HA   H  N N 444 
THR   HB   H  N N 445 
THR   HG1  H  N N 446 
THR   HG21 H  N N 447 
THR   HG22 H  N N 448 
THR   HG23 H  N N 449 
THR   HXT  H  N N 450 
TRP   N    N  N N 451 
TRP   CA   C  N S 452 
TRP   C    C  N N 453 
TRP   O    O  N N 454 
TRP   CB   C  N N 455 
TRP   CG   C  Y N 456 
TRP   CD1  C  Y N 457 
TRP   CD2  C  Y N 458 
TRP   NE1  N  Y N 459 
TRP   CE2  C  Y N 460 
TRP   CE3  C  Y N 461 
TRP   CZ2  C  Y N 462 
TRP   CZ3  C  Y N 463 
TRP   CH2  C  Y N 464 
TRP   OXT  O  N N 465 
TRP   H    H  N N 466 
TRP   H2   H  N N 467 
TRP   HA   H  N N 468 
TRP   HB2  H  N N 469 
TRP   HB3  H  N N 470 
TRP   HD1  H  N N 471 
TRP   HE1  H  N N 472 
TRP   HE3  H  N N 473 
TRP   HZ2  H  N N 474 
TRP   HZ3  H  N N 475 
TRP   HH2  H  N N 476 
TRP   HXT  H  N N 477 
TYR   N    N  N N 478 
TYR   CA   C  N S 479 
TYR   C    C  N N 480 
TYR   O    O  N N 481 
TYR   CB   C  N N 482 
TYR   CG   C  Y N 483 
TYR   CD1  C  Y N 484 
TYR   CD2  C  Y N 485 
TYR   CE1  C  Y N 486 
TYR   CE2  C  Y N 487 
TYR   CZ   C  Y N 488 
TYR   OH   O  N N 489 
TYR   OXT  O  N N 490 
TYR   H    H  N N 491 
TYR   H2   H  N N 492 
TYR   HA   H  N N 493 
TYR   HB2  H  N N 494 
TYR   HB3  H  N N 495 
TYR   HD1  H  N N 496 
TYR   HD2  H  N N 497 
TYR   HE1  H  N N 498 
TYR   HE2  H  N N 499 
TYR   HH   H  N N 500 
TYR   HXT  H  N N 501 
VAL   N    N  N N 502 
VAL   CA   C  N S 503 
VAL   C    C  N N 504 
VAL   O    O  N N 505 
VAL   CB   C  N N 506 
VAL   CG1  C  N N 507 
VAL   CG2  C  N N 508 
VAL   OXT  O  N N 509 
VAL   H    H  N N 510 
VAL   H2   H  N N 511 
VAL   HA   H  N N 512 
VAL   HB   H  N N 513 
VAL   HG11 H  N N 514 
VAL   HG12 H  N N 515 
VAL   HG13 H  N N 516 
VAL   HG21 H  N N 517 
VAL   HG22 H  N N 518 
VAL   HG23 H  N N 519 
VAL   HXT  H  N N 520 
# 
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 
A1H93 C1  O1   sing N N 1   
A1H93 O1  C2   sing N N 2   
A1H93 C2  C3   doub Y N 3   
A1H93 C3  C4   sing Y N 4   
A1H93 C4  C5   doub Y N 5   
A1H93 C5  N1   sing N N 6   
A1H93 N1  N2   sing Y N 7   
A1H93 N2  N3   doub Y N 8   
A1H93 N3  C6   sing Y N 9   
A1H93 C6  C7   sing N N 10  
A1H93 C7  C8   sing N N 11  
A1H93 C8  C9   doub Y N 12  
A1H93 C9  C10  sing N N 13  
A1H93 C10 C11  sing N N 14  
A1H93 C11 C12  sing N N 15  
A1H93 C9  N4   sing Y N 16  
A1H93 N4  C13  doub Y N 17  
A1H93 C13 C14  sing Y N 18  
A1H93 C14 C15  doub Y N 19  
A1H93 C15 N5   sing Y N 20  
A1H93 N5  C16  doub Y N 21  
A1H93 C16 N6   sing Y N 22  
A1H93 C7  O2   sing N N 23  
A1H93 C6  C17  doub Y N 24  
A1H93 C5  C18  sing Y N 25  
A1H93 C4  F1   sing N N 26  
A1H93 C2  C19  sing Y N 27  
A1H93 C19 F2   sing N N 28  
A1H93 C17 N1   sing Y N 29  
A1H93 C19 C18  doub Y N 30  
A1H93 N6  C8   sing Y N 31  
A1H93 C12 C10  sing N N 32  
A1H93 N6  C14  sing Y N 33  
A1H93 C7  H5   sing N N 34  
A1H93 C10 H6   sing N N 35  
A1H93 C13 H11  sing N N 36  
A1H93 C17 H15  sing N N 37  
A1H93 C1  H3   sing N N 38  
A1H93 C1  H2   sing N N 39  
A1H93 C1  H1   sing N N 40  
A1H93 C3  H4   sing N N 41  
A1H93 C11 H8   sing N N 42  
A1H93 C11 H7   sing N N 43  
A1H93 C12 H10  sing N N 44  
A1H93 C12 H9   sing N N 45  
A1H93 O2  H14  sing N N 46  
A1H93 C18 H16  sing N N 47  
A1H93 C15 H12  sing N N 48  
A1H93 C16 H17  sing N N 49  
ALA   N   CA   sing N N 50  
ALA   N   H    sing N N 51  
ALA   N   H2   sing N N 52  
ALA   CA  C    sing N N 53  
ALA   CA  CB   sing N N 54  
ALA   CA  HA   sing N N 55  
ALA   C   O    doub N N 56  
ALA   C   OXT  sing N N 57  
ALA   CB  HB1  sing N N 58  
ALA   CB  HB2  sing N N 59  
ALA   CB  HB3  sing N N 60  
ALA   OXT HXT  sing N N 61  
ARG   N   CA   sing N N 62  
ARG   N   H    sing N N 63  
ARG   N   H2   sing N N 64  
ARG   CA  C    sing N N 65  
ARG   CA  CB   sing N N 66  
ARG   CA  HA   sing N N 67  
ARG   C   O    doub N N 68  
ARG   C   OXT  sing N N 69  
ARG   CB  CG   sing N N 70  
ARG   CB  HB2  sing N N 71  
ARG   CB  HB3  sing N N 72  
ARG   CG  CD   sing N N 73  
ARG   CG  HG2  sing N N 74  
ARG   CG  HG3  sing N N 75  
ARG   CD  NE   sing N N 76  
ARG   CD  HD2  sing N N 77  
ARG   CD  HD3  sing N N 78  
ARG   NE  CZ   sing N N 79  
ARG   NE  HE   sing N N 80  
ARG   CZ  NH1  sing N N 81  
ARG   CZ  NH2  doub N N 82  
ARG   NH1 HH11 sing N N 83  
ARG   NH1 HH12 sing N N 84  
ARG   NH2 HH21 sing N N 85  
ARG   NH2 HH22 sing N N 86  
ARG   OXT HXT  sing N N 87  
ASN   N   CA   sing N N 88  
ASN   N   H    sing N N 89  
ASN   N   H2   sing N N 90  
ASN   CA  C    sing N N 91  
ASN   CA  CB   sing N N 92  
ASN   CA  HA   sing N N 93  
ASN   C   O    doub N N 94  
ASN   C   OXT  sing N N 95  
ASN   CB  CG   sing N N 96  
ASN   CB  HB2  sing N N 97  
ASN   CB  HB3  sing N N 98  
ASN   CG  OD1  doub N N 99  
ASN   CG  ND2  sing N N 100 
ASN   ND2 HD21 sing N N 101 
ASN   ND2 HD22 sing N N 102 
ASN   OXT HXT  sing N N 103 
ASP   N   CA   sing N N 104 
ASP   N   H    sing N N 105 
ASP   N   H2   sing N N 106 
ASP   CA  C    sing N N 107 
ASP   CA  CB   sing N N 108 
ASP   CA  HA   sing N N 109 
ASP   C   O    doub N N 110 
ASP   C   OXT  sing N N 111 
ASP   CB  CG   sing N N 112 
ASP   CB  HB2  sing N N 113 
ASP   CB  HB3  sing N N 114 
ASP   CG  OD1  doub N N 115 
ASP   CG  OD2  sing N N 116 
ASP   OD2 HD2  sing N N 117 
ASP   OXT HXT  sing N N 118 
CYS   N   CA   sing N N 119 
CYS   N   H    sing N N 120 
CYS   N   H2   sing N N 121 
CYS   CA  C    sing N N 122 
CYS   CA  CB   sing N N 123 
CYS   CA  HA   sing N N 124 
CYS   C   O    doub N N 125 
CYS   C   OXT  sing N N 126 
CYS   CB  SG   sing N N 127 
CYS   CB  HB2  sing N N 128 
CYS   CB  HB3  sing N N 129 
CYS   SG  HG   sing N N 130 
CYS   OXT HXT  sing N N 131 
DMS   S   O    doub N N 132 
DMS   S   C1   sing N N 133 
DMS   S   C2   sing N N 134 
DMS   C1  H11  sing N N 135 
DMS   C1  H12  sing N N 136 
DMS   C1  H13  sing N N 137 
DMS   C2  H21  sing N N 138 
DMS   C2  H22  sing N N 139 
DMS   C2  H23  sing N N 140 
GLN   N   CA   sing N N 141 
GLN   N   H    sing N N 142 
GLN   N   H2   sing N N 143 
GLN   CA  C    sing N N 144 
GLN   CA  CB   sing N N 145 
GLN   CA  HA   sing N N 146 
GLN   C   O    doub N N 147 
GLN   C   OXT  sing N N 148 
GLN   CB  CG   sing N N 149 
GLN   CB  HB2  sing N N 150 
GLN   CB  HB3  sing N N 151 
GLN   CG  CD   sing N N 152 
GLN   CG  HG2  sing N N 153 
GLN   CG  HG3  sing N N 154 
GLN   CD  OE1  doub N N 155 
GLN   CD  NE2  sing N N 156 
GLN   NE2 HE21 sing N N 157 
GLN   NE2 HE22 sing N N 158 
GLN   OXT HXT  sing N N 159 
GLU   N   CA   sing N N 160 
GLU   N   H    sing N N 161 
GLU   N   H2   sing N N 162 
GLU   CA  C    sing N N 163 
GLU   CA  CB   sing N N 164 
GLU   CA  HA   sing N N 165 
GLU   C   O    doub N N 166 
GLU   C   OXT  sing N N 167 
GLU   CB  CG   sing N N 168 
GLU   CB  HB2  sing N N 169 
GLU   CB  HB3  sing N N 170 
GLU   CG  CD   sing N N 171 
GLU   CG  HG2  sing N N 172 
GLU   CG  HG3  sing N N 173 
GLU   CD  OE1  doub N N 174 
GLU   CD  OE2  sing N N 175 
GLU   OE2 HE2  sing N N 176 
GLU   OXT HXT  sing N N 177 
GLY   N   CA   sing N N 178 
GLY   N   H    sing N N 179 
GLY   N   H2   sing N N 180 
GLY   CA  C    sing N N 181 
GLY   CA  HA2  sing N N 182 
GLY   CA  HA3  sing N N 183 
GLY   C   O    doub N N 184 
GLY   C   OXT  sing N N 185 
GLY   OXT HXT  sing N N 186 
HEM   CHA C1A  sing N N 187 
HEM   CHA C4D  doub N N 188 
HEM   CHA HHA  sing N N 189 
HEM   CHB C4A  sing N N 190 
HEM   CHB C1B  doub N N 191 
HEM   CHB HHB  sing N N 192 
HEM   CHC C4B  sing N N 193 
HEM   CHC C1C  doub N N 194 
HEM   CHC HHC  sing N N 195 
HEM   CHD C4C  doub N N 196 
HEM   CHD C1D  sing N N 197 
HEM   CHD HHD  sing N N 198 
HEM   C1A C2A  doub Y N 199 
HEM   C1A NA   sing Y N 200 
HEM   C2A C3A  sing Y N 201 
HEM   C2A CAA  sing N N 202 
HEM   C3A C4A  doub Y N 203 
HEM   C3A CMA  sing N N 204 
HEM   C4A NA   sing Y N 205 
HEM   CMA HMA  sing N N 206 
HEM   CMA HMAA sing N N 207 
HEM   CMA HMAB sing N N 208 
HEM   CAA CBA  sing N N 209 
HEM   CAA HAA  sing N N 210 
HEM   CAA HAAA sing N N 211 
HEM   CBA CGA  sing N N 212 
HEM   CBA HBA  sing N N 213 
HEM   CBA HBAA sing N N 214 
HEM   CGA O1A  doub N N 215 
HEM   CGA O2A  sing N N 216 
HEM   C1B C2B  sing N N 217 
HEM   C1B NB   sing N N 218 
HEM   C2B C3B  doub N N 219 
HEM   C2B CMB  sing N N 220 
HEM   C3B C4B  sing N N 221 
HEM   C3B CAB  sing N N 222 
HEM   C4B NB   doub N N 223 
HEM   CMB HMB  sing N N 224 
HEM   CMB HMBA sing N N 225 
HEM   CMB HMBB sing N N 226 
HEM   CAB CBB  doub N N 227 
HEM   CAB HAB  sing N N 228 
HEM   CBB HBB  sing N N 229 
HEM   CBB HBBA sing N N 230 
HEM   C1C C2C  sing Y N 231 
HEM   C1C NC   sing Y N 232 
HEM   C2C C3C  doub Y N 233 
HEM   C2C CMC  sing N N 234 
HEM   C3C C4C  sing Y N 235 
HEM   C3C CAC  sing N N 236 
HEM   C4C NC   sing Y N 237 
HEM   CMC HMC  sing N N 238 
HEM   CMC HMCA sing N N 239 
HEM   CMC HMCB sing N N 240 
HEM   CAC CBC  doub N N 241 
HEM   CAC HAC  sing N N 242 
HEM   CBC HBC  sing N N 243 
HEM   CBC HBCA sing N N 244 
HEM   C1D C2D  sing N N 245 
HEM   C1D ND   doub N N 246 
HEM   C2D C3D  doub N N 247 
HEM   C2D CMD  sing N N 248 
HEM   C3D C4D  sing N N 249 
HEM   C3D CAD  sing N N 250 
HEM   C4D ND   sing N N 251 
HEM   CMD HMD  sing N N 252 
HEM   CMD HMDA sing N N 253 
HEM   CMD HMDB sing N N 254 
HEM   CAD CBD  sing N N 255 
HEM   CAD HAD  sing N N 256 
HEM   CAD HADA sing N N 257 
HEM   CBD CGD  sing N N 258 
HEM   CBD HBD  sing N N 259 
HEM   CBD HBDA sing N N 260 
HEM   CGD O1D  doub N N 261 
HEM   CGD O2D  sing N N 262 
HEM   O2A H2A  sing N N 263 
HEM   O2D H2D  sing N N 264 
HEM   FE  NA   sing N N 265 
HEM   FE  NB   sing N N 266 
HEM   FE  NC   sing N N 267 
HEM   FE  ND   sing N N 268 
HIS   N   CA   sing N N 269 
HIS   N   H    sing N N 270 
HIS   N   H2   sing N N 271 
HIS   CA  C    sing N N 272 
HIS   CA  CB   sing N N 273 
HIS   CA  HA   sing N N 274 
HIS   C   O    doub N N 275 
HIS   C   OXT  sing N N 276 
HIS   CB  CG   sing N N 277 
HIS   CB  HB2  sing N N 278 
HIS   CB  HB3  sing N N 279 
HIS   CG  ND1  sing Y N 280 
HIS   CG  CD2  doub Y N 281 
HIS   ND1 CE1  doub Y N 282 
HIS   ND1 HD1  sing N N 283 
HIS   CD2 NE2  sing Y N 284 
HIS   CD2 HD2  sing N N 285 
HIS   CE1 NE2  sing Y N 286 
HIS   CE1 HE1  sing N N 287 
HIS   NE2 HE2  sing N N 288 
HIS   OXT HXT  sing N N 289 
HOH   O   H1   sing N N 290 
HOH   O   H2   sing N N 291 
ILE   N   CA   sing N N 292 
ILE   N   H    sing N N 293 
ILE   N   H2   sing N N 294 
ILE   CA  C    sing N N 295 
ILE   CA  CB   sing N N 296 
ILE   CA  HA   sing N N 297 
ILE   C   O    doub N N 298 
ILE   C   OXT  sing N N 299 
ILE   CB  CG1  sing N N 300 
ILE   CB  CG2  sing N N 301 
ILE   CB  HB   sing N N 302 
ILE   CG1 CD1  sing N N 303 
ILE   CG1 HG12 sing N N 304 
ILE   CG1 HG13 sing N N 305 
ILE   CG2 HG21 sing N N 306 
ILE   CG2 HG22 sing N N 307 
ILE   CG2 HG23 sing N N 308 
ILE   CD1 HD11 sing N N 309 
ILE   CD1 HD12 sing N N 310 
ILE   CD1 HD13 sing N N 311 
ILE   OXT HXT  sing N N 312 
LEU   N   CA   sing N N 313 
LEU   N   H    sing N N 314 
LEU   N   H2   sing N N 315 
LEU   CA  C    sing N N 316 
LEU   CA  CB   sing N N 317 
LEU   CA  HA   sing N N 318 
LEU   C   O    doub N N 319 
LEU   C   OXT  sing N N 320 
LEU   CB  CG   sing N N 321 
LEU   CB  HB2  sing N N 322 
LEU   CB  HB3  sing N N 323 
LEU   CG  CD1  sing N N 324 
LEU   CG  CD2  sing N N 325 
LEU   CG  HG   sing N N 326 
LEU   CD1 HD11 sing N N 327 
LEU   CD1 HD12 sing N N 328 
LEU   CD1 HD13 sing N N 329 
LEU   CD2 HD21 sing N N 330 
LEU   CD2 HD22 sing N N 331 
LEU   CD2 HD23 sing N N 332 
LEU   OXT HXT  sing N N 333 
LYS   N   CA   sing N N 334 
LYS   N   H    sing N N 335 
LYS   N   H2   sing N N 336 
LYS   CA  C    sing N N 337 
LYS   CA  CB   sing N N 338 
LYS   CA  HA   sing N N 339 
LYS   C   O    doub N N 340 
LYS   C   OXT  sing N N 341 
LYS   CB  CG   sing N N 342 
LYS   CB  HB2  sing N N 343 
LYS   CB  HB3  sing N N 344 
LYS   CG  CD   sing N N 345 
LYS   CG  HG2  sing N N 346 
LYS   CG  HG3  sing N N 347 
LYS   CD  CE   sing N N 348 
LYS   CD  HD2  sing N N 349 
LYS   CD  HD3  sing N N 350 
LYS   CE  NZ   sing N N 351 
LYS   CE  HE2  sing N N 352 
LYS   CE  HE3  sing N N 353 
LYS   NZ  HZ1  sing N N 354 
LYS   NZ  HZ2  sing N N 355 
LYS   NZ  HZ3  sing N N 356 
LYS   OXT HXT  sing N N 357 
MET   N   CA   sing N N 358 
MET   N   H    sing N N 359 
MET   N   H2   sing N N 360 
MET   CA  C    sing N N 361 
MET   CA  CB   sing N N 362 
MET   CA  HA   sing N N 363 
MET   C   O    doub N N 364 
MET   C   OXT  sing N N 365 
MET   CB  CG   sing N N 366 
MET   CB  HB2  sing N N 367 
MET   CB  HB3  sing N N 368 
MET   CG  SD   sing N N 369 
MET   CG  HG2  sing N N 370 
MET   CG  HG3  sing N N 371 
MET   SD  CE   sing N N 372 
MET   CE  HE1  sing N N 373 
MET   CE  HE2  sing N N 374 
MET   CE  HE3  sing N N 375 
MET   OXT HXT  sing N N 376 
PHE   N   CA   sing N N 377 
PHE   N   H    sing N N 378 
PHE   N   H2   sing N N 379 
PHE   CA  C    sing N N 380 
PHE   CA  CB   sing N N 381 
PHE   CA  HA   sing N N 382 
PHE   C   O    doub N N 383 
PHE   C   OXT  sing N N 384 
PHE   CB  CG   sing N N 385 
PHE   CB  HB2  sing N N 386 
PHE   CB  HB3  sing N N 387 
PHE   CG  CD1  doub Y N 388 
PHE   CG  CD2  sing Y N 389 
PHE   CD1 CE1  sing Y N 390 
PHE   CD1 HD1  sing N N 391 
PHE   CD2 CE2  doub Y N 392 
PHE   CD2 HD2  sing N N 393 
PHE   CE1 CZ   doub Y N 394 
PHE   CE1 HE1  sing N N 395 
PHE   CE2 CZ   sing Y N 396 
PHE   CE2 HE2  sing N N 397 
PHE   CZ  HZ   sing N N 398 
PHE   OXT HXT  sing N N 399 
PRO   N   CA   sing N N 400 
PRO   N   CD   sing N N 401 
PRO   N   H    sing N N 402 
PRO   CA  C    sing N N 403 
PRO   CA  CB   sing N N 404 
PRO   CA  HA   sing N N 405 
PRO   C   O    doub N N 406 
PRO   C   OXT  sing N N 407 
PRO   CB  CG   sing N N 408 
PRO   CB  HB2  sing N N 409 
PRO   CB  HB3  sing N N 410 
PRO   CG  CD   sing N N 411 
PRO   CG  HG2  sing N N 412 
PRO   CG  HG3  sing N N 413 
PRO   CD  HD2  sing N N 414 
PRO   CD  HD3  sing N N 415 
PRO   OXT HXT  sing N N 416 
SER   N   CA   sing N N 417 
SER   N   H    sing N N 418 
SER   N   H2   sing N N 419 
SER   CA  C    sing N N 420 
SER   CA  CB   sing N N 421 
SER   CA  HA   sing N N 422 
SER   C   O    doub N N 423 
SER   C   OXT  sing N N 424 
SER   CB  OG   sing N N 425 
SER   CB  HB2  sing N N 426 
SER   CB  HB3  sing N N 427 
SER   OG  HG   sing N N 428 
SER   OXT HXT  sing N N 429 
THR   N   CA   sing N N 430 
THR   N   H    sing N N 431 
THR   N   H2   sing N N 432 
THR   CA  C    sing N N 433 
THR   CA  CB   sing N N 434 
THR   CA  HA   sing N N 435 
THR   C   O    doub N N 436 
THR   C   OXT  sing N N 437 
THR   CB  OG1  sing N N 438 
THR   CB  CG2  sing N N 439 
THR   CB  HB   sing N N 440 
THR   OG1 HG1  sing N N 441 
THR   CG2 HG21 sing N N 442 
THR   CG2 HG22 sing N N 443 
THR   CG2 HG23 sing N N 444 
THR   OXT HXT  sing N N 445 
TRP   N   CA   sing N N 446 
TRP   N   H    sing N N 447 
TRP   N   H2   sing N N 448 
TRP   CA  C    sing N N 449 
TRP   CA  CB   sing N N 450 
TRP   CA  HA   sing N N 451 
TRP   C   O    doub N N 452 
TRP   C   OXT  sing N N 453 
TRP   CB  CG   sing N N 454 
TRP   CB  HB2  sing N N 455 
TRP   CB  HB3  sing N N 456 
TRP   CG  CD1  doub Y N 457 
TRP   CG  CD2  sing Y N 458 
TRP   CD1 NE1  sing Y N 459 
TRP   CD1 HD1  sing N N 460 
TRP   CD2 CE2  doub Y N 461 
TRP   CD2 CE3  sing Y N 462 
TRP   NE1 CE2  sing Y N 463 
TRP   NE1 HE1  sing N N 464 
TRP   CE2 CZ2  sing Y N 465 
TRP   CE3 CZ3  doub Y N 466 
TRP   CE3 HE3  sing N N 467 
TRP   CZ2 CH2  doub Y N 468 
TRP   CZ2 HZ2  sing N N 469 
TRP   CZ3 CH2  sing Y N 470 
TRP   CZ3 HZ3  sing N N 471 
TRP   CH2 HH2  sing N N 472 
TRP   OXT HXT  sing N N 473 
TYR   N   CA   sing N N 474 
TYR   N   H    sing N N 475 
TYR   N   H2   sing N N 476 
TYR   CA  C    sing N N 477 
TYR   CA  CB   sing N N 478 
TYR   CA  HA   sing N N 479 
TYR   C   O    doub N N 480 
TYR   C   OXT  sing N N 481 
TYR   CB  CG   sing N N 482 
TYR   CB  HB2  sing N N 483 
TYR   CB  HB3  sing N N 484 
TYR   CG  CD1  doub Y N 485 
TYR   CG  CD2  sing Y N 486 
TYR   CD1 CE1  sing Y N 487 
TYR   CD1 HD1  sing N N 488 
TYR   CD2 CE2  doub Y N 489 
TYR   CD2 HD2  sing N N 490 
TYR   CE1 CZ   doub Y N 491 
TYR   CE1 HE1  sing N N 492 
TYR   CE2 CZ   sing Y N 493 
TYR   CE2 HE2  sing N N 494 
TYR   CZ  OH   sing N N 495 
TYR   OH  HH   sing N N 496 
TYR   OXT HXT  sing N N 497 
VAL   N   CA   sing N N 498 
VAL   N   H    sing N N 499 
VAL   N   H2   sing N N 500 
VAL   CA  C    sing N N 501 
VAL   CA  CB   sing N N 502 
VAL   CA  HA   sing N N 503 
VAL   C   O    doub N N 504 
VAL   C   OXT  sing N N 505 
VAL   CB  CG1  sing N N 506 
VAL   CB  CG2  sing N N 507 
VAL   CB  HB   sing N N 508 
VAL   CG1 HG11 sing N N 509 
VAL   CG1 HG12 sing N N 510 
VAL   CG1 HG13 sing N N 511 
VAL   CG2 HG21 sing N N 512 
VAL   CG2 HG22 sing N N 513 
VAL   CG2 HG23 sing N N 514 
VAL   OXT HXT  sing N N 515 
# 
_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                    9F5R 
_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]   0.011776 
_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]   0.010835 
_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]   0.007597 
_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  
F  
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   . GLN   A 1 19  ? -22.86  17.719  2.471   1   53.88 ? 4   GLN   A N   1 
ATOM   2    C  CA  . GLN   A 1 19  ? -23.768 18.867  2.545   1   54.74 ? 4   GLN   A CA  1 
ATOM   3    C  C   . GLN   A 1 19  ? -24.487 19.142  1.221   1   55.44 ? 4   GLN   A C   1 
ATOM   4    O  O   . GLN   A 1 19  ? -25.634 19.596  1.226   1   55.97 ? 4   GLN   A O   1 
ATOM   5    C  CB  . GLN   A 1 19  ? -23.047 20.131  3.055   1   56.29 ? 4   GLN   A CB  1 
ATOM   6    N  N   . GLY   A 1 20  ? -23.833 18.846  0.101   1   55.14 ? 5   GLY   A N   1 
ATOM   7    C  CA  . GLY   A 1 20  ? -24.451 19.027  -1.207  1   55.29 ? 5   GLY   A CA  1 
ATOM   8    C  C   . GLY   A 1 20  ? -23.792 20.065  -2.091  1   55.36 ? 5   GLY   A C   1 
ATOM   9    O  O   . GLY   A 1 20  ? -22.915 20.816  -1.654  1   55.38 ? 5   GLY   A O   1 
ATOM   10   N  N   . PRO   A 1 21  ? -24.226 20.125  -3.361  1   55.13 ? 6   PRO   A N   1 
ATOM   11   C  CA  . PRO   A 1 21  ? -23.624 21.082  -4.306  1   55    ? 6   PRO   A CA  1 
ATOM   12   C  C   . PRO   A 1 21  ? -24.065 22.528  -4.107  1   54.83 ? 6   PRO   A C   1 
ATOM   13   O  O   . PRO   A 1 21  ? -25.014 22.966  -4.752  1   55.53 ? 6   PRO   A O   1 
ATOM   14   C  CB  . PRO   A 1 21  ? -24.068 20.564  -5.682  1   55.68 ? 6   PRO   A CB  1 
ATOM   15   C  CG  . PRO   A 1 21  ? -24.886 19.344  -5.443  1   56.12 ? 6   PRO   A CG  1 
ATOM   16   C  CD  . PRO   A 1 21  ? -25.258 19.295  -4.002  1   54.56 ? 6   PRO   A CD  1 
ATOM   17   N  N   . HIS   A 1 22  ? -23.36  23.28   -3.256  1   53.78 ? 7   HIS   A N   1 
ATOM   18   C  CA  . HIS   A 1 22  ? -23.712 24.672  -3.005  1   53.38 ? 7   HIS   A CA  1 
ATOM   19   C  C   . HIS   A 1 22  ? -22.564 25.615  -3.316  1   52.84 ? 7   HIS   A C   1 
ATOM   20   O  O   . HIS   A 1 22  ? -21.619 25.73   -2.534  1   53.65 ? 7   HIS   A O   1 
ATOM   21   C  CB  . HIS   A 1 22  ? -24.189 24.856  -1.563  1   54.33 ? 7   HIS   A CB  1 
ATOM   22   N  N   . MET   A 1 23  ? -22.669 26.323  -4.442  1   51.34 ? 8   MET   A N   1 
ATOM   23   C  CA  . MET   A 1 23  ? -21.687 27.297  -4.92   1   50.34 ? 8   MET   A CA  1 
ATOM   24   C  C   . MET   A 1 23  ? -21.873 28.647  -4.177  1   48.58 ? 8   MET   A C   1 
ATOM   25   O  O   . MET   A 1 23  ? -22.172 29.659  -4.8    1   48.25 ? 8   MET   A O   1 
ATOM   26   C  CB  . MET   A 1 23  ? -21.874 27.479  -6.444  1   51.51 ? 8   MET   A CB  1 
ATOM   27   C  CG  . MET   A 1 23  ? -20.765 28.241  -7.152  1   54.61 ? 8   MET   A CG  1 
ATOM   28   S  SD  . MET   A 1 23  ? -19.329 27.223  -7.494  1   64.04 ? 8   MET   A SD  1 
ATOM   29   C  CE  . MET   A 1 23  ? -20.047 25.983  -8.58   1   59.64 ? 8   MET   A CE  1 
ATOM   30   N  N   . TRP   A 1 24  ? -21.693 28.655  -2.849  1   47.43 ? 9   TRP   A N   1 
ATOM   31   C  CA  . TRP   A 1 24  ? -21.806 29.875  -2.022  1   46.71 ? 9   TRP   A CA  1 
ATOM   32   C  C   . TRP   A 1 24  ? -20.525 30.755  -2.041  1   45.27 ? 9   TRP   A C   1 
ATOM   33   O  O   . TRP   A 1 24  ? -20.543 31.918  -1.618  1   45.18 ? 9   TRP   A O   1 
ATOM   34   C  CB  . TRP   A 1 24  ? -22.191 29.511  -0.575  1   46.77 ? 9   TRP   A CB  1 
ATOM   35   N  N   . THR   A 1 25  ? -19.421 30.182  -2.525  1   43.69 ? 10  THR   A N   1 
ATOM   36   C  CA  . THR   A 1 25  ? -18.121 30.817  -2.685  1   43.1  ? 10  THR   A CA  1 
ATOM   37   C  C   . THR   A 1 25  ? -17.434 30.127  -3.88   1   40.85 ? 10  THR   A C   1 
ATOM   38   O  O   . THR   A 1 25  ? -17.734 28.959  -4.172  1   41.18 ? 10  THR   A O   1 
ATOM   39   C  CB  . THR   A 1 25  ? -17.278 30.595  -1.391  1   46.15 ? 10  THR   A CB  1 
ATOM   40   O  OG1 . THR   A 1 25  ? -17.764 31.448  -0.349  1   48.59 ? 10  THR   A OG1 1 
ATOM   41   C  CG2 . THR   A 1 25  ? -15.806 30.874  -1.59   1   47.17 ? 10  THR   A CG2 1 
ATOM   42   N  N   . ILE   A 1 26  ? -16.516 30.826  -4.564  1   38.63 ? 11  ILE   A N   1 
ATOM   43   C  CA  . ILE   A 1 26  ? -15.732 30.146  -5.59   1   36.48 ? 11  ILE   A CA  1 
ATOM   44   C  C   . ILE   A 1 26  ? -14.425 29.681  -4.953  1   34.44 ? 11  ILE   A C   1 
ATOM   45   O  O   . ILE   A 1 26  ? -13.534 30.482  -4.68   1   33.54 ? 11  ILE   A O   1 
ATOM   46   C  CB  . ILE   A 1 26  ? -15.545 30.9    -6.889  1   36.36 ? 11  ILE   A CB  1 
ATOM   47   C  CG1 . ILE   A 1 26  ? -16.927 31.182  -7.509  1   36.57 ? 11  ILE   A CG1 1 
ATOM   48   C  CG2 . ILE   A 1 26  ? -14.668 30.043  -7.819  1   36.39 ? 11  ILE   A CG2 1 
ATOM   49   C  CD1 . ILE   A 1 26  ? -16.893 32.091  -8.52   1   36.78 ? 11  ILE   A CD1 1 
ATOM   50   N  N   . SER   A 1 27  ? -14.36  28.384  -4.657  1   33.38 ? 12  SER   A N   1 
ATOM   51   C  CA  . SER   A 1 27  ? -13.209 27.732  -4.05   1   33.32 ? 12  SER   A CA  1 
ATOM   52   C  C   . SER   A 1 27  ? -11.941 27.977  -4.883  1   32.3  ? 12  SER   A C   1 
ATOM   53   O  O   . SER   A 1 27  ? -11.999 27.995  -6.122  1   31.65 ? 12  SER   A O   1 
ATOM   54   C  CB  . SER   A 1 27  ? -13.478 26.24   -3.973  1   35.87 ? 12  SER   A CB  1 
ATOM   55   O  OG  . SER   A 1 27  ? -12.347 25.529  -3.503  1   39.87 ? 12  SER   A OG  1 
ATOM   56   N  N   . LYS   A 1 28  ? -10.802 28.177  -4.197  1   31.11 ? 13  LYS   A N   1 
ATOM   57   C  CA  . LYS   A 1 28  ? -9.521  28.369  -4.854  1   30.51 ? 13  LYS   A CA  1 
ATOM   58   C  C   . LYS   A 1 28  ? -9.102  27.127  -5.669  1   29.02 ? 13  LYS   A C   1 
ATOM   59   O  O   . LYS   A 1 28  ? -8.287  27.249  -6.589  1   28.88 ? 13  LYS   A O   1 
ATOM   60   C  CB  . LYS   A 1 28  ? -8.427  28.772  -3.828  1   32.9  ? 13  LYS   A CB  1 
ATOM   61   N  N   . GLU   A 1 29  ? -9.672  25.945  -5.361  1   28.45 ? 14  GLU   A N   1 
ATOM   62   C  CA  . GLU   A 1 29  ? -9.368  24.721  -6.087  1   28.7  ? 14  GLU   A CA  1 
ATOM   63   C  C   . GLU   A 1 29  ? -9.918  24.713  -7.533  1   27.18 ? 14  GLU   A C   1 
ATOM   64   O  O   . GLU   A 1 29  ? -9.583  23.803  -8.299  1   27.36 ? 14  GLU   A O   1 
ATOM   65   C  CB  . GLU   A 1 29  ? -9.814  23.479  -5.299  1   33.57 ? 14  GLU   A CB  1 
ATOM   66   C  CG  . GLU   A 1 29  ? -11.282 23.143  -5.459  1   42.37 ? 14  GLU   A CG  1 
ATOM   67   N  N   . TYR   A 1 30  ? -10.754 25.705  -7.905  1   25.34 ? 15  TYR   A N   1 
ATOM   68   C  CA  . TYR   A 1 30  ? -11.25  25.831  -9.276  1   24.44 ? 15  TYR   A CA  1 
ATOM   69   C  C   . TYR   A 1 30  ? -10.241 26.596  -10.156 1   25.68 ? 15  TYR   A C   1 
ATOM   70   O  O   . TYR   A 1 30  ? -10.435 26.636  -11.368 1   26.47 ? 15  TYR   A O   1 
ATOM   71   C  CB  . TYR   A 1 30  ? -12.633 26.495  -9.309  1   22.96 ? 15  TYR   A CB  1 
ATOM   72   C  CG  . TYR   A 1 30  ? -13.701 25.594  -8.735  1   23.16 ? 15  TYR   A CG  1 
ATOM   73   C  CD1 . TYR   A 1 30  ? -13.929 24.331  -9.261  1   22.92 ? 15  TYR   A CD1 1 
ATOM   74   C  CD2 . TYR   A 1 30  ? -14.495 26.011  -7.674  1   24.82 ? 15  TYR   A CD2 1 
ATOM   75   C  CE1 . TYR   A 1 30  ? -14.923 23.506  -8.754  1   23.93 ? 15  TYR   A CE1 1 
ATOM   76   C  CE2 . TYR   A 1 30  ? -15.507 25.198  -7.166  1   25.45 ? 15  TYR   A CE2 1 
ATOM   77   C  CZ  . TYR   A 1 30  ? -15.721 23.948  -7.714  1   25.77 ? 15  TYR   A CZ  1 
ATOM   78   O  OH  . TYR   A 1 30  ? -16.732 23.149  -7.24   1   27.72 ? 15  TYR   A OH  1 
ATOM   79   N  N   . HIS   A 1 31  ? -9.23   27.283  -9.543  1   24.85 ? 16  HIS   A N   1 
ATOM   80   C  CA  . HIS   A 1 31  ? -8.207  28.013  -10.285 1   25.97 ? 16  HIS   A CA  1 
ATOM   81   C  C   . HIS   A 1 31  ? -8.793  29.097  -11.191 1   26.08 ? 16  HIS   A C   1 
ATOM   82   O  O   . HIS   A 1 31  ? -8.456  29.223  -12.377 1   25.83 ? 16  HIS   A O   1 
ATOM   83   C  CB  . HIS   A 1 31  ? -7.29   27.041  -11.038 1   27.69 ? 16  HIS   A CB  1 
ATOM   84   C  CG  . HIS   A 1 31  ? -6.537  26.146  -10.097 1   31.56 ? 16  HIS   A CG  1 
ATOM   85   N  ND1 . HIS   A 1 31  ? -5.582  26.657  -9.217  1   34.98 ? 16  HIS   A ND1 1 
ATOM   86   C  CD2 . HIS   A 1 31  ? -6.628  24.809  -9.91   1   33.03 ? 16  HIS   A CD2 1 
ATOM   87   C  CE1 . HIS   A 1 31  ? -5.119  25.613  -8.541  1   35.23 ? 16  HIS   A CE1 1 
ATOM   88   N  NE2 . HIS   A 1 31  ? -5.726  24.481  -8.913  1   34.33 ? 16  HIS   A NE2 1 
ATOM   89   N  N   . ILE   A 1 32  ? -9.656  29.897  -10.605 1   25.41 ? 17  ILE   A N   1 
ATOM   90   C  CA  . ILE   A 1 32  ? -10.257 31.024  -11.295 1   25.35 ? 17  ILE   A CA  1 
ATOM   91   C  C   . ILE   A 1 32  ? -9.677  32.256  -10.602 1   25.97 ? 17  ILE   A C   1 
ATOM   92   O  O   . ILE   A 1 32  ? -9.848  32.443  -9.4    1   26.65 ? 17  ILE   A O   1 
ATOM   93   C  CB  . ILE   A 1 32  ? -11.808 30.99   -11.209 1   24.81 ? 17  ILE   A CB  1 
ATOM   94   C  CG1 . ILE   A 1 32  ? -12.376 29.715  -11.86  1   24.78 ? 17  ILE   A CG1 1 
ATOM   95   C  CG2 . ILE   A 1 32  ? -12.412 32.278  -11.831 1   24.41 ? 17  ILE   A CG2 1 
ATOM   96   C  CD1 . ILE   A 1 32  ? -13.905 29.527  -11.563 1   26.68 ? 17  ILE   A CD1 1 
ATOM   97   N  N   . ASP   A 1 33  ? -8.953  33.053  -11.349 1   25.42 ? 18  ASP   A N   1 
ATOM   98   C  CA  . ASP   A 1 33  ? -8.305  34.243  -10.863 1   25.74 ? 18  ASP   A CA  1 
ATOM   99   C  C   . ASP   A 1 33  ? -9.299  35.389  -10.726 1   27.21 ? 18  ASP   A C   1 
ATOM   100  O  O   . ASP   A 1 33  ? -10.205 35.53   -11.53  1   26.46 ? 18  ASP   A O   1 
ATOM   101  C  CB  . ASP   A 1 33  ? -7.185  34.626  -11.829 1   25.84 ? 18  ASP   A CB  1 
ATOM   102  C  CG  . ASP   A 1 33  ? -6.276  35.685  -11.257 1   29.69 ? 18  ASP   A CG  1 
ATOM   103  O  OD1 . ASP   A 1 33  ? -5.562  35.381  -10.277 1   30.67 ? 18  ASP   A OD1 1 
ATOM   104  O  OD2 . ASP   A 1 33  ? -6.293  36.816  -11.776 1   29.92 ? 18  ASP   A OD2 1 
ATOM   105  N  N   . GLU   A 1 34  ? -9.112  36.231  -9.709  1   29.07 ? 19  GLU   A N   1 
ATOM   106  C  CA  . GLU   A 1 34  ? -9.98   37.379  -9.476  1   30.2  ? 19  GLU   A CA  1 
ATOM   107  C  C   . GLU   A 1 34  ? -9.89   38.38   -10.615 1   30.58 ? 19  GLU   A C   1 
ATOM   108  O  O   . GLU   A 1 34  ? -10.884 39.029  -10.939 1   31.34 ? 19  GLU   A O   1 
ATOM   109  C  CB  . GLU   A 1 34  ? -9.597  38.072  -8.151  1   33.39 ? 19  GLU   A CB  1 
ATOM   110  N  N   . GLU   A 1 35  ? -8.706  38.515  -11.23  1   30.28 ? 20  GLU   A N   1 
ATOM   111  C  CA  . GLU   A 1 35  ? -8.517  39.471  -12.309 1   29.84 ? 20  GLU   A CA  1 
ATOM   112  C  C   . GLU   A 1 35  ? -8.733  38.907  -13.704 1   28.39 ? 20  GLU   A C   1 
ATOM   113  O  O   . GLU   A 1 35  ? -9.399  39.547  -14.508 1   28.75 ? 20  GLU   A O   1 
ATOM   114  C  CB  . GLU   A 1 35  ? -7.125  40.106  -12.211 1   32.61 ? 20  GLU   A CB  1 
ATOM   115  C  CG  . GLU   A 1 35  ? -6.911  41.229  -13.203 1   38.7  ? 20  GLU   A CG  1 
ATOM   116  C  CD  . GLU   A 1 35  ? -5.516  41.826  -13.161 1   46.27 ? 20  GLU   A CD  1 
ATOM   117  O  OE1 . GLU   A 1 35  ? -4.564  41.112  -12.766 1   45.58 ? 20  GLU   A OE1 1 
ATOM   118  O  OE2 . GLU   A 1 35  ? -5.374  43.007  -13.549 1   50.98 ? 20  GLU   A OE2 1 
ATOM   119  N  N   . VAL   A 1 36  ? -8.161  37.728  -14.014 1   26.96 ? 21  VAL   A N   1 
ATOM   120  C  CA  . VAL   A 1 36  ? -8.241  37.204  -15.382 1   25.74 ? 21  VAL   A CA  1 
ATOM   121  C  C   . VAL   A 1 36  ? -9.13   35.96   -15.558 1   25.17 ? 21  VAL   A C   1 
ATOM   122  O  O   . VAL   A 1 36  ? -9.153  35.38   -16.658 1   25.29 ? 21  VAL   A O   1 
ATOM   123  C  CB  . VAL   A 1 36  ? -6.823  36.967  -15.948 1   25.71 ? 21  VAL   A CB  1 
ATOM   124  C  CG1 . VAL   A 1 36  ? -6.039  38.276  -16.006 1   27.11 ? 21  VAL   A CG1 1 
ATOM   125  C  CG2 . VAL   A 1 36  ? -6.061  35.923  -15.141 1   25.35 ? 21  VAL   A CG2 1 
ATOM   126  N  N   . GLY   A 1 37  ? -9.877  35.581  -14.513 1   23.49 ? 22  GLY   A N   1 
ATOM   127  C  CA  . GLY   A 1 37  ? -10.819 34.473  -14.566 1   22.76 ? 22  GLY   A CA  1 
ATOM   128  C  C   . GLY   A 1 37  ? -10.177 33.144  -14.879 1   23.16 ? 22  GLY   A C   1 
ATOM   129  O  O   . GLY   A 1 37  ? -9.293  32.71   -14.145 1   22.98 ? 22  GLY   A O   1 
ATOM   130  N  N   . PHE   A 1 38  ? -10.622 32.479  -15.97  1   22.25 ? 23  PHE   A N   1 
ATOM   131  C  CA  . PHE   A 1 38  ? -10.073 31.189  -16.414 1   21.49 ? 23  PHE   A CA  1 
ATOM   132  C  C   . PHE   A 1 38  ? -8.693  31.299  -17.088 1   21.28 ? 23  PHE   A C   1 
ATOM   133  O  O   . PHE   A 1 38  ? -8.026  30.273  -17.255 1   21.75 ? 23  PHE   A O   1 
ATOM   134  C  CB  . PHE   A 1 38  ? -11.047 30.497  -17.386 1   21.16 ? 23  PHE   A CB  1 
ATOM   135  C  CG  . PHE   A 1 38  ? -12.354 30.124  -16.709 1   21.06 ? 23  PHE   A CG  1 
ATOM   136  C  CD1 . PHE   A 1 38  ? -12.429 29.016  -15.87  1   21.9  ? 23  PHE   A CD1 1 
ATOM   137  C  CD2 . PHE   A 1 38  ? -13.485 30.892  -16.881 1   22.14 ? 23  PHE   A CD2 1 
ATOM   138  C  CE1 . PHE   A 1 38  ? -13.613 28.687  -15.216 1   23.02 ? 23  PHE   A CE1 1 
ATOM   139  C  CE2 . PHE   A 1 38  ? -14.683 30.549  -16.235 1   23.62 ? 23  PHE   A CE2 1 
ATOM   140  C  CZ  . PHE   A 1 38  ? -14.745 29.442  -15.427 1   22.97 ? 23  PHE   A CZ  1 
ATOM   141  N  N   . ALA   A 1 39  ? -8.262  32.493  -17.462 1   20.44 ? 24  ALA   A N   1 
ATOM   142  C  CA  . ALA   A 1 39  ? -6.934  32.671  -18.045 1   20.54 ? 24  ALA   A CA  1 
ATOM   143  C  C   . ALA   A 1 39  ? -5.853  32.374  -16.963 1   20.69 ? 24  ALA   A C   1 
ATOM   144  O  O   . ALA   A 1 39  ? -6.119  32.456  -15.755 1   19.82 ? 24  ALA   A O   1 
ATOM   145  C  CB  . ALA   A 1 39  ? -6.764  34.092  -18.561 1   20.16 ? 24  ALA   A CB  1 
ATOM   146  N  N   . LEU   A 1 40  ? -4.664  31.973  -17.411 1   20.8  ? 25  LEU   A N   1 
ATOM   147  C  CA  . LEU   A 1 40  ? -3.574  31.665  -16.501 1   20.84 ? 25  LEU   A CA  1 
ATOM   148  C  C   . LEU   A 1 40  ? -2.98   33.009  -16.062 1   23.85 ? 25  LEU   A C   1 
ATOM   149  O  O   . LEU   A 1 40  ? -2.557  33.809  -16.907 1   24.56 ? 25  LEU   A O   1 
ATOM   150  C  CB  . LEU   A 1 40  ? -2.527  30.812  -17.225 1   20.41 ? 25  LEU   A CB  1 
ATOM   151  C  CG  . LEU   A 1 40  ? -1.288  30.401  -16.386 1   21.47 ? 25  LEU   A CG  1 
ATOM   152  C  CD1 . LEU   A 1 40  ? -1.677  29.353  -15.308 1   22.39 ? 25  LEU   A CD1 1 
ATOM   153  C  CD2 . LEU   A 1 40  ? -0.211  29.814  -17.301 1   21.19 ? 25  LEU   A CD2 1 
ATOM   154  N  N   . PRO   A 1 41  ? -2.985  33.307  -14.751 1   25.43 ? 26  PRO   A N   1 
ATOM   155  C  CA  . PRO   A 1 41  ? -2.446  34.604  -14.306 1   26.44 ? 26  PRO   A CA  1 
ATOM   156  C  C   . PRO   A 1 41  ? -0.948  34.659  -14.503 1   26.72 ? 26  PRO   A C   1 
ATOM   157  O  O   . PRO   A 1 41  ? -0.292  33.659  -14.28  1   28.03 ? 26  PRO   A O   1 
ATOM   158  C  CB  . PRO   A 1 41  ? -2.806  34.666  -12.809 1   27.3  ? 26  PRO   A CB  1 
ATOM   159  C  CG  . PRO   A 1 41  ? -3.632  33.469  -12.524 1   27.35 ? 26  PRO   A CG  1 
ATOM   160  C  CD  . PRO   A 1 41  ? -3.481  32.487  -13.627 1   25.2  ? 26  PRO   A CD  1 
ATOM   161  N  N   A ASN   A 1 42  ? -0.402  35.807  -14.944 0.5 26.63 ? 27  ASN   A N   1 
ATOM   162  N  N   B ASN   A 1 42  ? -0.411  35.801  -14.967 0.5 26.16 ? 27  ASN   A N   1 
ATOM   163  C  CA  A ASN   A 1 42  ? 1.04    36.025  -15.165 0.5 27.12 ? 27  ASN   A CA  1 
ATOM   164  C  CA  B ASN   A 1 42  ? 1.026   36.03   -15.208 0.5 26.2  ? 27  ASN   A CA  1 
ATOM   165  C  C   A ASN   A 1 42  ? 1.786   34.789  -15.704 0.5 26.04 ? 27  ASN   A C   1 
ATOM   166  C  C   B ASN   A 1 42  ? 1.788   34.8    -15.713 0.5 25.6  ? 27  ASN   A C   1 
ATOM   167  O  O   A ASN   A 1 42  ? 2.564   34.172  -14.972 0.5 26.01 ? 27  ASN   A O   1 
ATOM   168  O  O   B ASN   A 1 42  ? 2.572   34.207  -14.97  0.5 25.54 ? 27  ASN   A O   1 
ATOM   169  C  CB  A ASN   A 1 42  ? 1.697   36.541  -13.871 0.5 29.42 ? 27  ASN   A CB  1 
ATOM   170  C  CB  B ASN   A 1 42  ? 1.686   36.603  -13.954 0.5 27.24 ? 27  ASN   A CB  1 
ATOM   171  C  CG  A ASN   A 1 42  ? 3.147   36.959  -13.987 0.5 34.6  ? 27  ASN   A CG  1 
ATOM   172  C  CG  B ASN   A 1 42  ? 1.043   37.891  -13.538 0.5 29.87 ? 27  ASN   A CG  1 
ATOM   173  O  OD1 A ASN   A 1 42  ? 3.9     36.91   -13.005 0.5 37.25 ? 27  ASN   A OD1 1 
ATOM   174  O  OD1 B ASN   A 1 42  ? 1.057   38.877  -14.276 0.5 31.86 ? 27  ASN   A OD1 1 
ATOM   175  N  ND2 A ASN   A 1 42  ? 3.587   37.373  -15.173 0.5 35.1  ? 27  ASN   A ND2 1 
ATOM   176  N  ND2 B ASN   A 1 42  ? 0.412   37.895  -12.384 0.5 30.02 ? 27  ASN   A ND2 1 
ATOM   177  N  N   . PRO   A 1 43  ? 1.473   34.351  -16.936 1   24.87 ? 28  PRO   A N   1 
ATOM   178  C  CA  . PRO   A 1 43  ? 2.12    33.14   -17.467 1   24.09 ? 28  PRO   A CA  1 
ATOM   179  C  C   . PRO   A 1 43  ? 3.636   33.218  -17.486 1   23.46 ? 28  PRO   A C   1 
ATOM   180  O  O   . PRO   A 1 43  ? 4.183   34.302  -17.671 1   23.96 ? 28  PRO   A O   1 
ATOM   181  C  CB  . PRO   A 1 43  ? 1.567   33.049  -18.903 1   24.13 ? 28  PRO   A CB  1 
ATOM   182  C  CG  . PRO   A 1 43  ? 0.283   33.806  -18.881 1   24.24 ? 28  PRO   A CG  1 
ATOM   183  C  CD  . PRO   A 1 43  ? 0.545   34.939  -17.924 1   23.57 ? 28  PRO   A CD  1 
ATOM   184  N  N   . GLN   A 1 44  ? 4.296   32.078  -17.289 1   22.99 ? 29  GLN   A N   1 
ATOM   185  C  CA  . GLN   A 1 44  ? 5.754   31.986  -17.333 1   23.44 ? 29  GLN   A CA  1 
ATOM   186  C  C   . GLN   A 1 44  ? 6.19    32.202  -18.773 1   22.77 ? 29  GLN   A C   1 
ATOM   187  O  O   . GLN   A 1 44  ? 5.51    31.737  -19.699 1   21.9  ? 29  GLN   A O   1 
ATOM   188  C  CB  . GLN   A 1 44  ? 6.217   30.618  -16.814 1   24.7  ? 29  GLN   A CB  1 
ATOM   189  C  CG  . GLN   A 1 44  ? 7.711   30.564  -16.508 1   27.79 ? 29  GLN   A CG  1 
ATOM   190  C  CD  . GLN   A 1 44  ? 8.005   29.366  -15.657 1   32.88 ? 29  GLN   A CD  1 
ATOM   191  O  OE1 . GLN   A 1 44  ? 7.286   29.091  -14.674 1   34.82 ? 29  GLN   A OE1 1 
ATOM   192  N  NE2 . GLN   A 1 44  ? 9.049   28.612  -16.033 1   32.96 ? 29  GLN   A NE2 1 
ATOM   193  N  N   . GLU   A 1 45  ? 7.295   32.926  -18.971 1   22.17 ? 30  GLU   A N   1 
ATOM   194  C  CA  A GLU   A 1 45  ? 7.807   33.239  -20.303 0.5 23    ? 30  GLU   A CA  1 
ATOM   195  C  CA  B GLU   A 1 45  ? 7.8     33.221  -20.316 0.5 23.21 ? 30  GLU   A CA  1 
ATOM   196  C  C   . GLU   A 1 45  ? 9.036   32.402  -20.68  1   24.21 ? 30  GLU   A C   1 
ATOM   197  O  O   . GLU   A 1 45  ? 9.236   32.08   -21.848 1   24.67 ? 30  GLU   A O   1 
ATOM   198  C  CB  A GLU   A 1 45  ? 8.136   34.736  -20.37  0.5 24.73 ? 30  GLU   A CB  1 
ATOM   199  C  CB  B GLU   A 1 45  ? 8.096   34.722  -20.486 0.5 25.71 ? 30  GLU   A CB  1 
ATOM   200  C  CG  A GLU   A 1 45  ? 6.982   35.605  -19.905 0.5 28.54 ? 30  GLU   A CG  1 
ATOM   201  C  CG  B GLU   A 1 45  ? 8.414   35.082  -21.931 0.5 30.9  ? 30  GLU   A CG  1 
ATOM   202  C  CD  A GLU   A 1 45  ? 7.318   37.076  -19.813 0.5 34.87 ? 30  GLU   A CD  1 
ATOM   203  C  CD  B GLU   A 1 45  ? 8.879   36.5    -22.184 0.5 34.99 ? 30  GLU   A CD  1 
ATOM   204  O  OE1 A GLU   A 1 45  ? 6.74    37.765  -18.943 0.5 36.73 ? 30  GLU   A OE1 1 
ATOM   205  O  OE1 B GLU   A 1 45  ? 8.803   37.322  -21.245 0.5 35.39 ? 30  GLU   A OE1 1 
ATOM   206  O  OE2 A GLU   A 1 45  ? 8.161   37.539  -20.613 0.5 36.56 ? 30  GLU   A OE2 1 
ATOM   207  O  OE2 B GLU   A 1 45  ? 9.319   36.789  -23.319 0.5 37.12 ? 30  GLU   A OE2 1 
ATOM   208  N  N   . ASN   A 1 46  ? 9.853   32.042  -19.686 1   24.7  ? 31  ASN   A N   1 
ATOM   209  C  CA  . ASN   A 1 46  ? 11.064  31.262  -19.937 1   25.89 ? 31  ASN   A CA  1 
ATOM   210  C  C   . ASN   A 1 46  ? 11.022  29.93   -19.24  1   24.97 ? 31  ASN   A C   1 
ATOM   211  O  O   . ASN   A 1 46  ? 10.493  29.834  -18.133 1   24.45 ? 31  ASN   A O   1 
ATOM   212  C  CB  . ASN   A 1 46  ? 12.3    32.056  -19.443 1   28.44 ? 31  ASN   A CB  1 
ATOM   213  C  CG  . ASN   A 1 46  ? 12.383  33.422  -20.066 1   35.12 ? 31  ASN   A CG  1 
ATOM   214  O  OD1 . ASN   A 1 46  ? 12.485  33.564  -21.291 1   36.68 ? 31  ASN   A OD1 1 
ATOM   215  N  ND2 . ASN   A 1 46  ? 12.29   34.457  -19.23  1   37.37 ? 31  ASN   A ND2 1 
ATOM   216  N  N   . LEU   A 1 47  ? 11.529  28.89   -19.904 1   24.56 ? 32  LEU   A N   1 
ATOM   217  C  CA  . LEU   A 1 47  ? 11.627  27.579  -19.279 1   26.23 ? 32  LEU   A CA  1 
ATOM   218  C  C   . LEU   A 1 47  ? 13.039  27.462  -18.632 1   28.06 ? 32  LEU   A C   1 
ATOM   219  O  O   . LEU   A 1 47  ? 13.945  28.182  -19.059 1   28.55 ? 32  LEU   A O   1 
ATOM   220  C  CB  . LEU   A 1 47  ? 11.503  26.482  -20.366 1   25.63 ? 32  LEU   A CB  1 
ATOM   221  C  CG  . LEU   A 1 47  ? 10.101  26.187  -20.9   1   26.01 ? 32  LEU   A CG  1 
ATOM   222  C  CD1 . LEU   A 1 47  ? 10.163  25.144  -21.997 1   25.77 ? 32  LEU   A CD1 1 
ATOM   223  C  CD2 . LEU   A 1 47  ? 9.161   25.702  -19.779 1   26.83 ? 32  LEU   A CD2 1 
ATOM   224  N  N   . PRO   A 1 48  ? 13.308  26.485  -17.725 1   29.06 ? 33  PRO   A N   1 
ATOM   225  C  CA  . PRO   A 1 48  ? 14.697  26.288  -17.26  1   29.44 ? 33  PRO   A CA  1 
ATOM   226  C  C   . PRO   A 1 48  ? 15.669  26.085  -18.453 1   29.33 ? 33  PRO   A C   1 
ATOM   227  O  O   . PRO   A 1 48  ? 15.243  25.688  -19.549 1   29.04 ? 33  PRO   A O   1 
ATOM   228  C  CB  . PRO   A 1 48  ? 14.602  25.021  -16.398 1   29.8  ? 33  PRO   A CB  1 
ATOM   229  C  CG  . PRO   A 1 48  ? 13.186  24.996  -15.914 1   30.5  ? 33  PRO   A CG  1 
ATOM   230  C  CD  . PRO   A 1 48  ? 12.382  25.528  -17.081 1   29.31 ? 33  PRO   A CD  1 
ATOM   231  N  N   . ASP   A 1 49  ? 16.959  26.405  -18.267 1   28.58 ? 34  ASP   A N   1 
ATOM   232  C  CA  . ASP   A 1 49  ? 17.978  26.309  -19.328 1   28.19 ? 34  ASP   A CA  1 
ATOM   233  C  C   . ASP   A 1 49  ? 18.054  24.933  -19.989 1   25.88 ? 34  ASP   A C   1 
ATOM   234  O  O   . ASP   A 1 49  ? 18.465  24.825  -21.139 1   24.52 ? 34  ASP   A O   1 
ATOM   235  C  CB  . ASP   A 1 49  ? 19.374  26.662  -18.772 1   31.68 ? 34  ASP   A CB  1 
ATOM   236  C  CG  . ASP   A 1 49  ? 19.533  28.112  -18.376 1   40.57 ? 34  ASP   A CG  1 
ATOM   237  O  OD1 . ASP   A 1 49  ? 18.747  28.957  -18.88  1   40.17 ? 34  ASP   A OD1 1 
ATOM   238  O  OD2 . ASP   A 1 49  ? 20.444  28.408  -17.544 1   45.23 ? 34  ASP   A OD2 1 
ATOM   239  N  N   . PHE   A 1 50  ? 17.691  23.882  -19.247 1   25.7  ? 35  PHE   A N   1 
ATOM   240  C  CA  . PHE   A 1 50  ? 17.693  22.509  -19.73  1   25.79 ? 35  PHE   A CA  1 
ATOM   241  C  C   . PHE   A 1 50  ? 16.856  22.363  -21.039 1   24.39 ? 35  PHE   A C   1 
ATOM   242  O  O   . PHE   A 1 50  ? 17.204  21.572  -21.921 1   24.01 ? 35  PHE   A O   1 
ATOM   243  C  CB  . PHE   A 1 50  ? 17.088  21.613  -18.636 1   27.21 ? 35  PHE   A CB  1 
ATOM   244  C  CG  . PHE   A 1 50  ? 17.147  20.126  -18.892 1   29.97 ? 35  PHE   A CG  1 
ATOM   245  C  CD1 . PHE   A 1 50  ? 18.296  19.4    -18.605 1   32.54 ? 35  PHE   A CD1 1 
ATOM   246  C  CD2 . PHE   A 1 50  ? 16.035  19.438  -19.33  1   31.24 ? 35  PHE   A CD2 1 
ATOM   247  C  CE1 . PHE   A 1 50  ? 18.338  18.021  -18.798 1   33.5  ? 35  PHE   A CE1 1 
ATOM   248  C  CE2 . PHE   A 1 50  ? 16.082  18.068  -19.536 1   32.95 ? 35  PHE   A CE2 1 
ATOM   249  C  CZ  . PHE   A 1 50  ? 17.235  17.364  -19.269 1   33.2  ? 35  PHE   A CZ  1 
ATOM   250  N  N   . TYR   A 1 51  ? 15.83   23.207  -21.192 1   23.74 ? 36  TYR   A N   1 
ATOM   251  C  CA  . TYR   A 1 51  ? 14.897  23.149  -22.337 1   23.33 ? 36  TYR   A CA  1 
ATOM   252  C  C   . TYR   A 1 51  ? 15.173  24.176  -23.42  1   23.77 ? 36  TYR   A C   1 
ATOM   253  O  O   . TYR   A 1 51  ? 14.323  24.379  -24.289 1   23.62 ? 36  TYR   A O   1 
ATOM   254  C  CB  . TYR   A 1 51  ? 13.472  23.331  -21.8   1   22.83 ? 36  TYR   A CB  1 
ATOM   255  C  CG  . TYR   A 1 51  ? 13.114  22.245  -20.808 1   22.9  ? 36  TYR   A CG  1 
ATOM   256  C  CD1 . TYR   A 1 51  ? 12.924  20.934  -21.225 1   22.87 ? 36  TYR   A CD1 1 
ATOM   257  C  CD2 . TYR   A 1 51  ? 13.043  22.512  -19.445 1   23.29 ? 36  TYR   A CD2 1 
ATOM   258  C  CE1 . TYR   A 1 51  ? 12.588  19.935  -20.323 1   23.28 ? 36  TYR   A CE1 1 
ATOM   259  C  CE2 . TYR   A 1 51  ? 12.722  21.511  -18.528 1   23.96 ? 36  TYR   A CE2 1 
ATOM   260  C  CZ  . TYR   A 1 51  ? 12.486  20.224  -18.975 1   24.35 ? 36  TYR   A CZ  1 
ATOM   261  O  OH  . TYR   A 1 51  ? 12.169  19.209  -18.088 1   25.57 ? 36  TYR   A OH  1 
ATOM   262  N  N   . ASN   A 1 52  ? 16.363  24.837  -23.393 1   24.66 ? 37  ASN   A N   1 
ATOM   263  C  CA  . ASN   A 1 52  ? 16.704  25.841  -24.422 1   24.55 ? 37  ASN   A CA  1 
ATOM   264  C  C   . ASN   A 1 52  ? 16.479  25.373  -25.869 1   23.39 ? 37  ASN   A C   1 
ATOM   265  O  O   . ASN   A 1 52  ? 16.09   26.197  -26.711 1   23.08 ? 37  ASN   A O   1 
ATOM   266  C  CB  . ASN   A 1 52  ? 18.133  26.363  -24.257 1   26.46 ? 37  ASN   A CB  1 
ATOM   267  C  CG  . ASN   A 1 52  ? 18.29   27.344  -23.117 1   31.76 ? 37  ASN   A CG  1 
ATOM   268  O  OD1 . ASN   A 1 52  ? 17.329  27.958  -22.635 1   32.69 ? 37  ASN   A OD1 1 
ATOM   269  N  ND2 . ASN   A 1 52  ? 19.532  27.512  -22.653 1   33.34 ? 37  ASN   A ND2 1 
ATOM   270  N  N   . ASP   A 1 53  ? 16.735  24.08   -26.166 1   22.42 ? 38  ASP   A N   1 
ATOM   271  C  CA  . ASP   A 1 53  ? 16.572  23.563  -27.527 1   22.98 ? 38  ASP   A CA  1 
ATOM   272  C  C   . ASP   A 1 53  ? 15.106  23.599  -27.976 1   22.29 ? 38  ASP   A C   1 
ATOM   273  O  O   . ASP   A 1 53  ? 14.833  23.825  -29.162 1   22.57 ? 38  ASP   A O   1 
ATOM   274  C  CB  . ASP   A 1 53  ? 17.139  22.147  -27.689 1   25.29 ? 38  ASP   A CB  1 
ATOM   275  C  CG  . ASP   A 1 53  ? 18.661  22.057  -27.617 1   32.45 ? 38  ASP   A CG  1 
ATOM   276  O  OD1 . ASP   A 1 53  ? 19.325  23.113  -27.686 1   31.28 ? 38  ASP   A OD1 1 
ATOM   277  O  OD2 . ASP   A 1 53  ? 19.177  20.935  -27.468 1   36.1  ? 38  ASP   A OD2 1 
ATOM   278  N  N   . TRP   A 1 54  ? 14.166  23.378  -27.028 1   20.37 ? 39  TRP   A N   1 
ATOM   279  C  CA  . TRP   A 1 54  ? 12.746  23.49   -27.337 1   18.63 ? 39  TRP   A CA  1 
ATOM   280  C  C   . TRP   A 1 54  ? 12.414  24.935  -27.575 1   17.77 ? 39  TRP   A C   1 
ATOM   281  O  O   . TRP   A 1 54  ? 11.664  25.253  -28.514 1   17.91 ? 39  TRP   A O   1 
ATOM   282  C  CB  . TRP   A 1 54  ? 11.874  23.023  -26.143 1   18.03 ? 39  TRP   A CB  1 
ATOM   283  C  CG  . TRP   A 1 54  ? 11.872  21.561  -25.837 1   17.26 ? 39  TRP   A CG  1 
ATOM   284  C  CD1 . TRP   A 1 54  ? 12.488  20.563  -26.527 1   17.42 ? 39  TRP   A CD1 1 
ATOM   285  C  CD2 . TRP   A 1 54  ? 11.145  20.936  -24.781 1   16.99 ? 39  TRP   A CD2 1 
ATOM   286  N  NE1 . TRP   A 1 54  ? 12.183  19.352  -25.96  1   18.13 ? 39  TRP   A NE1 1 
ATOM   287  C  CE2 . TRP   A 1 54  ? 11.41   19.561  -24.848 1   17.54 ? 39  TRP   A CE2 1 
ATOM   288  C  CE3 . TRP   A 1 54  ? 10.359  21.42   -23.731 1   18.35 ? 39  TRP   A CE3 1 
ATOM   289  C  CZ2 . TRP   A 1 54  ? 10.859  18.648  -23.939 1   18.35 ? 39  TRP   A CZ2 1 
ATOM   290  C  CZ3 . TRP   A 1 54  ? 9.825   20.516  -22.832 1   19.15 ? 39  TRP   A CZ3 1 
ATOM   291  C  CH2 . TRP   A 1 54  ? 10.082  19.152  -22.94  1   18.85 ? 39  TRP   A CH2 1 
ATOM   292  N  N   . MET   A 1 55  ? 12.875  25.821  -26.674 1   17.65 ? 40  MET   A N   1 
ATOM   293  C  CA  . MET   A 1 55  ? 12.562  27.241  -26.721 1   18.91 ? 40  MET   A CA  1 
ATOM   294  C  C   . MET   A 1 55  ? 13.039  27.898  -27.983 1   19.58 ? 40  MET   A C   1 
ATOM   295  O  O   . MET   A 1 55  ? 12.303  28.705  -28.547 1   19.48 ? 40  MET   A O   1 
ATOM   296  C  CB  . MET   A 1 55  ? 13.106  27.998  -25.508 1   21.3  ? 40  MET   A CB  1 
ATOM   297  C  CG  . MET   A 1 55  ? 12.402  27.641  -24.214 1   29.1  ? 40  MET   A CG  1 
ATOM   298  S  SD  . MET   A 1 55  ? 10.714  28.292  -23.885 1   36.05 ? 40  MET   A SD  1 
ATOM   299  C  CE  . MET   A 1 55  ? 10.54   29.628  -25.015 1   13.6  ? 40  MET   A CE  1 
ATOM   300  N  N   . PHE   A 1 56  ? 14.25   27.545  -28.474 1   19.98 ? 41  PHE   A N   1 
ATOM   301  C  CA  . PHE   A 1 56  ? 14.74   28.137  -29.722 1   19.67 ? 41  PHE   A CA  1 
ATOM   302  C  C   . PHE   A 1 56  ? 13.779  27.799  -30.873 1   19.26 ? 41  PHE   A C   1 
ATOM   303  O  O   . PHE   A 1 56  ? 13.385  28.693  -31.626 1   20.22 ? 41  PHE   A O   1 
ATOM   304  C  CB  . PHE   A 1 56  ? 16.16   27.649  -30.065 1   20.87 ? 41  PHE   A CB  1 
ATOM   305  C  CG  . PHE   A 1 56  ? 16.562  28.094  -31.458 1   22.15 ? 41  PHE   A CG  1 
ATOM   306  C  CD1 . PHE   A 1 56  ? 16.865  29.42   -31.715 1   22.9  ? 41  PHE   A CD1 1 
ATOM   307  C  CD2 . PHE   A 1 56  ? 16.52   27.209  -32.528 1   23.5  ? 41  PHE   A CD2 1 
ATOM   308  C  CE1 . PHE   A 1 56  ? 17.138  29.849  -33.016 1   23.84 ? 41  PHE   A CE1 1 
ATOM   309  C  CE2 . PHE   A 1 56  ? 16.845  27.63   -33.818 1   24    ? 41  PHE   A CE2 1 
ATOM   310  C  CZ  . PHE   A 1 56  ? 17.129  28.95   -34.054 1   23.1  ? 41  PHE   A CZ  1 
ATOM   311  N  N   . ILE   A 1 57  ? 13.368  26.519  -30.989 1   18.45 ? 42  ILE   A N   1 
ATOM   312  C  CA  . ILE   A 1 57  ? 12.45   26.147  -32.071 1   17.65 ? 42  ILE   A CA  1 
ATOM   313  C  C   . ILE   A 1 57  ? 11.098  26.886  -31.947 1   17.81 ? 42  ILE   A C   1 
ATOM   314  O  O   . ILE   A 1 57  ? 10.639  27.523  -32.899 1   17.05 ? 42  ILE   A O   1 
ATOM   315  C  CB  . ILE   A 1 57  ? 12.291  24.626  -32.131 1   17.99 ? 42  ILE   A CB  1 
ATOM   316  C  CG1 . ILE   A 1 57  ? 13.675  23.946  -32.431 1   18.64 ? 42  ILE   A CG1 1 
ATOM   317  C  CG2 . ILE   A 1 57  ? 11.254  24.257  -33.224 1   18.42 ? 42  ILE   A CG2 1 
ATOM   318  C  CD1 . ILE   A 1 57  ? 13.641  22.446  -32.432 1   19.37 ? 42  ILE   A CD1 1 
ATOM   319  N  N   . ALA   A 1 58  ? 10.464  26.812  -30.762 1   18.17 ? 43  ALA   A N   1 
ATOM   320  C  CA  . ALA   A 1 58  ? 9.17    27.458  -30.534 1   18.88 ? 43  ALA   A CA  1 
ATOM   321  C  C   . ALA   A 1 58  ? 9.179   28.975  -30.795 1   19.71 ? 43  ALA   A C   1 
ATOM   322  O  O   . ALA   A 1 58  ? 8.237   29.505  -31.388 1   20.69 ? 43  ALA   A O   1 
ATOM   323  C  CB  . ALA   A 1 58  ? 8.667   27.158  -29.136 1   18.66 ? 43  ALA   A CB  1 
ATOM   324  N  N   . LYS   A 1 59  ? 10.246  29.651  -30.415 1   19.02 ? 44  LYS   A N   1 
ATOM   325  C  CA  . LYS   A 1 59  ? 10.378  31.082  -30.637 1   20.15 ? 44  LYS   A CA  1 
ATOM   326  C  C   . LYS   A 1 59  ? 10.696  31.471  -32.094 1   20.04 ? 44  LYS   A C   1 
ATOM   327  O  O   . LYS   A 1 59  ? 10.656  32.665  -32.413 1   21.41 ? 44  LYS   A O   1 
ATOM   328  C  CB  . LYS   A 1 59  ? 11.485  31.644  -29.725 1   22.65 ? 44  LYS   A CB  1 
ATOM   329  C  CG  . LYS   A 1 59  ? 11.016  31.832  -28.288 1   28.64 ? 44  LYS   A CG  1 
ATOM   330  C  CD  . LYS   A 1 59  ? 12.204  31.942  -27.294 1   35.89 ? 44  LYS   A CD  1 
ATOM   331  C  CE  . LYS   A 1 59  ? 13.102  33.128  -27.501 1   42.16 ? 44  LYS   A CE  1 
ATOM   332  N  NZ  . LYS   A 1 59  ? 12.453  34.383  -27.038 1   45.94 ? 44  LYS   A NZ  1 
ATOM   333  N  N   . HIS   A 1 60  ? 11.1    30.52   -32.941 1   18.3  ? 45  HIS   A N   1 
ATOM   334  C  CA  . HIS   A 1 60  ? 11.489  30.855  -34.315 1   17.97 ? 45  HIS   A CA  1 
ATOM   335  C  C   . HIS   A 1 60  ? 10.682  30.078  -35.353 1   17.73 ? 45  HIS   A C   1 
ATOM   336  O  O   . HIS   A 1 60  ? 11.206  29.766  -36.428 1   17.22 ? 45  HIS   A O   1 
ATOM   337  C  CB  . HIS   A 1 60  ? 13.011  30.68   -34.517 1   18.32 ? 45  HIS   A CB  1 
ATOM   338  C  CG  . HIS   A 1 60  ? 13.796  31.617  -33.655 1   20.42 ? 45  HIS   A CG  1 
ATOM   339  N  ND1 . HIS   A 1 60  ? 14.194  31.26   -32.375 1   21.16 ? 45  HIS   A ND1 1 
ATOM   340  C  CD2 . HIS   A 1 60  ? 14.206  32.89   -33.905 1   21.21 ? 45  HIS   A CD2 1 
ATOM   341  C  CE1 . HIS   A 1 60  ? 14.854  32.309  -31.895 1   21.85 ? 45  HIS   A CE1 1 
ATOM   342  N  NE2 . HIS   A 1 60  ? 14.859  33.324  -32.773 1   22.59 ? 45  HIS   A NE2 1 
ATOM   343  N  N   . LEU   A 1 61  ? 9.409   29.731  -35.025 1   16.07 ? 46  LEU   A N   1 
ATOM   344  C  CA  . LEU   A 1 61  ? 8.579   28.983  -35.992 1   16.88 ? 46  LEU   A CA  1 
ATOM   345  C  C   . LEU   A 1 61  ? 8.412   29.729  -37.324 1   18.49 ? 46  LEU   A C   1 
ATOM   346  O  O   . LEU   A 1 61  ? 8.567   29.101  -38.362 1   18.37 ? 46  LEU   A O   1 
ATOM   347  C  CB  . LEU   A 1 61  ? 7.189   28.61   -35.431 1   16.37 ? 46  LEU   A CB  1 
ATOM   348  C  CG  . LEU   A 1 61  ? 7.25    27.652  -34.249 1   18.47 ? 46  LEU   A CG  1 
ATOM   349  C  CD1 . LEU   A 1 61  ? 5.827   27.414  -33.659 1   18.45 ? 46  LEU   A CD1 1 
ATOM   350  C  CD2 . LEU   A 1 61  ? 7.927   26.303  -34.651 1   18.98 ? 46  LEU   A CD2 1 
ATOM   351  N  N   . PRO   A 1 62  ? 8.155   31.06   -37.345 1   18.46 ? 47  PRO   A N   1 
ATOM   352  C  CA  . PRO   A 1 62  ? 8.035   31.742  -38.647 1   18.61 ? 47  PRO   A CA  1 
ATOM   353  C  C   . PRO   A 1 62  ? 9.254   31.512  -39.579 1   18.73 ? 47  PRO   A C   1 
ATOM   354  O  O   . PRO   A 1 62  ? 9.074   31.14   -40.727 1   18.14 ? 47  PRO   A O   1 
ATOM   355  C  CB  . PRO   A 1 62  ? 7.896   33.212  -38.247 1   19.48 ? 47  PRO   A CB  1 
ATOM   356  C  CG  . PRO   A 1 62  ? 7.203   33.17   -36.882 1   19.85 ? 47  PRO   A CG  1 
ATOM   357  C  CD  . PRO   A 1 62  ? 7.863   31.983  -36.218 1   18.15 ? 47  PRO   A CD  1 
ATOM   358  N  N   . ASP   A 1 63  ? 10.486  31.647  -39.054 1   18.06 ? 48  ASP   A N   1 
ATOM   359  C  CA  . ASP   A 1 63  ? 11.698  31.527  -39.859 1   19.07 ? 48  ASP   A CA  1 
ATOM   360  C  C   . ASP   A 1 63  ? 11.99   30.1    -40.197 1   19.38 ? 48  ASP   A C   1 
ATOM   361  O  O   . ASP   A 1 63  ? 12.425  29.825  -41.322 1   20.54 ? 48  ASP   A O   1 
ATOM   362  C  CB  . ASP   A 1 63  ? 12.893  32.134  -39.107 1   21.41 ? 48  ASP   A CB  1 
ATOM   363  C  CG  . ASP   A 1 63  ? 12.711  33.601  -38.848 1   26.5  ? 48  ASP   A CG  1 
ATOM   364  O  OD1 . ASP   A 1 63  ? 12.152  34.288  -39.721 1   24.99 ? 48  ASP   A OD1 1 
ATOM   365  O  OD2 . ASP   A 1 63  ? 13.132  34.063  -37.775 1   31.17 ? 48  ASP   A OD2 1 
ATOM   366  N  N   . LEU   A 1 64  ? 11.838  29.191  -39.22  1   18.45 ? 49  LEU   A N   1 
ATOM   367  C  CA  . LEU   A 1 64  ? 12.146  27.779  -39.464 1   19.57 ? 49  LEU   A CA  1 
ATOM   368  C  C   . LEU   A 1 64  ? 11.159  27.121  -40.431 1   20.74 ? 49  LEU   A C   1 
ATOM   369  O  O   . LEU   A 1 64  ? 11.559  26.288  -41.258 1   21.64 ? 49  LEU   A O   1 
ATOM   370  C  CB  . LEU   A 1 64  ? 12.226  27.009  -38.153 1   19.39 ? 49  LEU   A CB  1 
ATOM   371  C  CG  . LEU   A 1 64  ? 13.369  27.433  -37.217 1   19.81 ? 49  LEU   A CG  1 
ATOM   372  C  CD1 . LEU   A 1 64  ? 13.219  26.763  -35.846 1   19.26 ? 49  LEU   A CD1 1 
ATOM   373  C  CD2 . LEU   A 1 64  ? 14.772  27.097  -37.88  1   21.02 ? 49  LEU   A CD2 1 
ATOM   374  N  N   . ILE   A 1 65  ? 9.878   27.499  -40.356 1   20.53 ? 50  ILE   A N   1 
ATOM   375  C  CA  . ILE   A 1 65  ? 8.87    26.959  -41.274 1   20.63 ? 50  ILE   A CA  1 
ATOM   376  C  C   . ILE   A 1 65  ? 9.151   27.479  -42.69  1   22.49 ? 50  ILE   A C   1 
ATOM   377  O  O   . ILE   A 1 65  ? 9.281   26.682  -43.633 1   22.91 ? 50  ILE   A O   1 
ATOM   378  C  CB  . ILE   A 1 65  ? 7.417   27.317  -40.83  1   19.61 ? 50  ILE   A CB  1 
ATOM   379  C  CG1 . ILE   A 1 65  ? 7.043   26.588  -39.517 1   18.45 ? 50  ILE   A CG1 1 
ATOM   380  C  CG2 . ILE   A 1 65  ? 6.419   26.972  -41.952 1   20.77 ? 50  ILE   A CG2 1 
ATOM   381  C  CD1 . ILE   A 1 65  ? 5.718   27.123  -38.889 1   17.61 ? 50  ILE   A CD1 1 
ATOM   382  N  N   . GLU   A 1 66  ? 9.268   28.817  -42.834 1   22.78 ? 51  GLU   A N   1 
ATOM   383  C  CA  . GLU   A 1 66  ? 9.47    29.455  -44.134 1   23.65 ? 51  GLU   A CA  1 
ATOM   384  C  C   . GLU   A 1 66  ? 10.705  28.937  -44.85  1   24    ? 51  GLU   A C   1 
ATOM   385  O  O   . GLU   A 1 66  ? 10.678  28.74   -46.059 1   24.94 ? 51  GLU   A O   1 
ATOM   386  C  CB  . GLU   A 1 66  ? 9.533   30.97   -43.998 1   25.67 ? 51  GLU   A CB  1 
ATOM   387  C  CG  . GLU   A 1 66  ? 9.491   31.609  -45.362 1   31.94 ? 51  GLU   A CG  1 
ATOM   388  C  CD  . GLU   A 1 66  ? 9.649   33.107  -45.409 1   39.04 ? 51  GLU   A CD  1 
ATOM   389  O  OE1 . GLU   A 1 66  ? 9.607   33.772  -44.35  1   39.36 ? 51  GLU   A OE1 1 
ATOM   390  O  OE2 . GLU   A 1 66  ? 9.825   33.617  -46.538 1   43.12 ? 51  GLU   A OE2 1 
ATOM   391  N  N   . SER   A 1 67  ? 11.772  28.669  -44.098 1   23.5  ? 52  SER   A N   1 
ATOM   392  C  CA  . SER   A 1 67  ? 13.019  28.163  -44.678 1   23.71 ? 52  SER   A CA  1 
ATOM   393  C  C   . SER   A 1 67  ? 13.05   26.659  -44.932 1   24.83 ? 52  SER   A C   1 
ATOM   394  O  O   . SER   A 1 67  ? 13.987  26.187  -45.544 1   25.93 ? 52  SER   A O   1 
ATOM   395  C  CB  . SER   A 1 67  ? 14.211  28.573  -43.822 1   24.61 ? 52  SER   A CB  1 
ATOM   396  O  OG  . SER   A 1 67  ? 14.202  27.835  -42.612 1   25.62 ? 52  SER   A OG  1 
ATOM   397  N  N   . GLY   A 1 68  ? 12.049  25.911  -44.484 1   24.44 ? 53  GLY   A N   1 
ATOM   398  C  CA  . GLY   A 1 68  ? 12.024  24.457  -44.664 1   23.84 ? 53  GLY   A CA  1 
ATOM   399  C  C   . GLY   A 1 68  ? 12.962  23.732  -43.702 1   23.95 ? 53  GLY   A C   1 
ATOM   400  O  O   . GLY   A 1 68  ? 13.298  22.567  -43.927 1   25.47 ? 53  GLY   A O   1 
ATOM   401  N  N   . GLN   A 1 69  ? 13.411  24.397  -42.622 1   22.43 ? 54  GLN   A N   1 
ATOM   402  C  CA  . GLN   A 1 69  ? 14.343  23.781  -41.675 1   22.99 ? 54  GLN   A CA  1 
ATOM   403  C  C   . GLN   A 1 69  ? 13.648  23.259  -40.405 1   22.94 ? 54  GLN   A C   1 
ATOM   404  O  O   . GLN   A 1 69  ? 14.317  22.647  -39.567 1   23.64 ? 54  GLN   A O   1 
ATOM   405  C  CB  . GLN   A 1 69  ? 15.38   24.824  -41.209 1   26.32 ? 54  GLN   A CB  1 
ATOM   406  C  CG  . GLN   A 1 69  ? 16.274  25.351  -42.335 1   34.23 ? 54  GLN   A CG  1 
ATOM   407  C  CD  . GLN   A 1 69  ? 17.518  24.524  -42.544 1   45.26 ? 54  GLN   A CD  1 
ATOM   408  O  OE1 . GLN   A 1 69  ? 17.47   23.305  -42.84  1   49.19 ? 54  GLN   A OE1 1 
ATOM   409  N  NE2 . GLN   A 1 69  ? 18.659  25.187  -42.443 1   47.29 ? 54  GLN   A NE2 1 
ATOM   410  N  N   . LEU   A 1 70  ? 12.366  23.61   -40.19  1   21.9  ? 55  LEU   A N   1 
ATOM   411  C  CA  . LEU   A 1 70  ? 11.672  23.238  -38.959 1   20.61 ? 55  LEU   A CA  1 
ATOM   412  C  C   . LEU   A 1 70  ? 11.718  21.724  -38.668 1   21.42 ? 55  LEU   A C   1 
ATOM   413  O  O   . LEU   A 1 70  ? 12.117  21.32   -37.572 1   20.66 ? 55  LEU   A O   1 
ATOM   414  C  CB  . LEU   A 1 70  ? 10.229  23.778  -38.997 1   20.3  ? 55  LEU   A CB  1 
ATOM   415  C  CG  . LEU   A 1 70  ? 9.33    23.638  -37.731 1   21.26 ? 55  LEU   A CG  1 
ATOM   416  C  CD1 . LEU   A 1 70  ? 8.638   22.313  -37.683 1   21.12 ? 55  LEU   A CD1 1 
ATOM   417  C  CD2 . LEU   A 1 70  ? 10.103  23.93   -36.45  1   21.78 ? 55  LEU   A CD2 1 
ATOM   418  N  N   . ARG   A 1 71  ? 11.292  20.903  -39.631 1   21.87 ? 56  ARG   A N   1 
ATOM   419  C  CA  . ARG   A 1 71  ? 11.221  19.469  -39.401 1   22.72 ? 56  ARG   A CA  1 
ATOM   420  C  C   . ARG   A 1 71  ? 12.584  18.855  -39.039 1   23.58 ? 56  ARG   A C   1 
ATOM   421  O  O   . ARG   A 1 71  ? 12.661  18.075  -38.089 1   22.91 ? 56  ARG   A O   1 
ATOM   422  C  CB  . ARG   A 1 71  ? 10.54   18.79   -40.584 1   23.58 ? 56  ARG   A CB  1 
ATOM   423  C  CG  . ARG   A 1 71  ? 9.05    19.153  -40.563 1   25.59 ? 56  ARG   A CG  1 
ATOM   424  C  CD  . ARG   A 1 71  ? 8.352   18.932  -41.851 1   26.59 ? 56  ARG   A CD  1 
ATOM   425  N  NE  . ARG   A 1 71  ? 6.893   18.976  -41.708 1   25.69 ? 56  ARG   A NE  1 
ATOM   426  C  CZ  . ARG   A 1 71  ? 6.058   18.924  -42.74  1   27.69 ? 56  ARG   A CZ  1 
ATOM   427  N  NH1 . ARG   A 1 71  ? 6.527   18.898  -43.986 1   28.38 ? 56  ARG   A NH1 1 
ATOM   428  N  NH2 . ARG   A 1 71  ? 4.746   18.898  -42.539 1   27.02 ? 56  ARG   A NH2 1 
ATOM   429  N  N   . GLU   A 1 72  ? 13.663  19.291  -39.728 1   23.46 ? 57  GLU   A N   1 
ATOM   430  C  CA  . GLU   A 1 72  ? 15.012  18.819  -39.479 1   24.14 ? 57  GLU   A CA  1 
ATOM   431  C  C   . GLU   A 1 72  ? 15.456  19.231  -38.091 1   23.78 ? 57  GLU   A C   1 
ATOM   432  O  O   . GLU   A 1 72  ? 16.027  18.417  -37.394 1   24.23 ? 57  GLU   A O   1 
ATOM   433  C  CB  . GLU   A 1 72  ? 15.984  19.388  -40.55  1   26.35 ? 57  GLU   A CB  1 
ATOM   434  C  CG  . GLU   A 1 72  ? 17.427  18.946  -40.363 1   33.94 ? 57  GLU   A CG  1 
ATOM   435  C  CD  . GLU   A 1 72  ? 18.408  19.668  -41.261 1   48.74 ? 57  GLU   A CD  1 
ATOM   436  O  OE1 . GLU   A 1 72  ? 19.317  20.343  -40.726 1   53.1  ? 57  GLU   A OE1 1 
ATOM   437  O  OE2 . GLU   A 1 72  ? 18.248  19.589  -42.502 1   54.26 ? 57  GLU   A OE2 1 
ATOM   438  N  N   . ARG   A 1 73  ? 15.173  20.469  -37.659 1   23.06 ? 58  ARG   A N   1 
ATOM   439  C  CA  . ARG   A 1 73  ? 15.572  20.924  -36.324 1   23.07 ? 58  ARG   A CA  1 
ATOM   440  C  C   . ARG   A 1 73  ? 14.827  20.103  -35.243 1   22.27 ? 58  ARG   A C   1 
ATOM   441  O  O   . ARG   A 1 73  ? 15.398  19.804  -34.18  1   21.56 ? 58  ARG   A O   1 
ATOM   442  C  CB  . ARG   A 1 73  ? 15.264  22.419  -36.141 1   25.75 ? 58  ARG   A CB  1 
ATOM   443  C  CG  . ARG   A 1 73  ? 16.087  23.344  -37.066 1   32.89 ? 58  ARG   A CG  1 
ATOM   444  C  CD  . ARG   A 1 73  ? 17.57   23.389  -36.691 1   38.99 ? 58  ARG   A CD  1 
ATOM   445  N  NE  . ARG   A 1 73  ? 18.396  22.561  -37.566 1   45.03 ? 58  ARG   A NE  1 
ATOM   446  C  CZ  . ARG   A 1 73  ? 19.528  21.964  -37.186 1   49.01 ? 58  ARG   A CZ  1 
ATOM   447  N  NH1 . ARG   A 1 73  ? 19.942  22.045  -35.923 1   47.76 ? 58  ARG   A NH1 1 
ATOM   448  N  NH2 . ARG   A 1 73  ? 20.232  21.252  -38.054 1   49.95 ? 58  ARG   A NH2 1 
ATOM   449  N  N   . VAL   A 1 74  ? 13.557  19.773  -35.511 1   21.29 ? 59  VAL   A N   1 
ATOM   450  C  CA  . VAL   A 1 74  ? 12.775  18.978  -34.557 1   21.24 ? 59  VAL   A CA  1 
ATOM   451  C  C   . VAL   A 1 74  ? 13.361  17.563  -34.494 1   22.84 ? 59  VAL   A C   1 
ATOM   452  O  O   . VAL   A 1 74  ? 13.544  17.026  -33.412 1   23.02 ? 59  VAL   A O   1 
ATOM   453  C  CB  . VAL   A 1 74  ? 11.272  18.985  -34.885 1   21.56 ? 59  VAL   A CB  1 
ATOM   454  C  CG1 . VAL   A 1 74  ? 10.531  17.917  -34.081 1   20.77 ? 59  VAL   A CG1 1 
ATOM   455  C  CG2 . VAL   A 1 74  ? 10.664  20.385  -34.621 1   21.41 ? 59  VAL   A CG2 1 
ATOM   456  N  N   . GLU   A 1 75  ? 13.682  16.987  -35.649 1   23.96 ? 60  GLU   A N   1 
ATOM   457  C  CA  . GLU   A 1 75  ? 14.241  15.627  -35.727 1   23.87 ? 60  GLU   A CA  1 
ATOM   458  C  C   . GLU   A 1 75  ? 15.64   15.52   -35.106 1   25.02 ? 60  GLU   A C   1 
ATOM   459  O  O   . GLU   A 1 75  ? 16.041  14.432  -34.69  1   24.48 ? 60  GLU   A O   1 
ATOM   460  C  CB  . GLU   A 1 75  ? 14.198  15.114  -37.172 1   23.88 ? 60  GLU   A CB  1 
ATOM   461  C  CG  . GLU   A 1 75  ? 12.791  14.838  -37.676 1   23.09 ? 60  GLU   A CG  1 
ATOM   462  C  CD  . GLU   A 1 75  ? 12.61   14.974  -39.176 1   26.3  ? 60  GLU   A CD  1 
ATOM   463  O  OE1 . GLU   A 1 75  ? 13.623  15.146  -39.885 1   30.91 ? 60  GLU   A OE1 1 
ATOM   464  O  OE2 . GLU   A 1 75  ? 11.458  14.913  -39.655 1   26.36 ? 60  GLU   A OE2 1 
ATOM   465  N  N   . LYS   A 1 76  ? 16.384  16.655  -34.998 1   24.73 ? 61  LYS   A N   1 
ATOM   466  C  CA  . LYS   A 1 76  ? 17.697  16.669  -34.365 1   25.66 ? 61  LYS   A CA  1 
ATOM   467  C  C   . LYS   A 1 76  ? 17.634  16.764  -32.833 1   25.42 ? 61  LYS   A C   1 
ATOM   468  O  O   . LYS   A 1 76  ? 18.646  16.511  -32.159 1   25.83 ? 61  LYS   A O   1 
ATOM   469  C  CB  . LYS   A 1 76  ? 18.56   17.819  -34.925 1   28.61 ? 61  LYS   A CB  1 
ATOM   470  C  CG  . LYS   A 1 76  ? 18.878  17.664  -36.415 1   36.9  ? 61  LYS   A CG  1 
ATOM   471  C  CD  . LYS   A 1 76  ? 19.921  16.594  -36.737 1   44.26 ? 61  LYS   A CD  1 
ATOM   472  C  CE  . LYS   A 1 76  ? 20.252  16.583  -38.221 1   49.68 ? 61  LYS   A CE  1 
ATOM   473  N  NZ  . LYS   A 1 76  ? 20.423  17.962  -38.776 1   52.62 ? 61  LYS   A NZ  1 
ATOM   474  N  N   . LEU   A 1 77  ? 16.459  17.121  -32.258 1   24.48 ? 62  LEU   A N   1 
ATOM   475  C  CA  . LEU   A 1 77  ? 16.358  17.217  -30.8   1   23.71 ? 62  LEU   A CA  1 
ATOM   476  C  C   . LEU   A 1 77  ? 16.706  15.915  -30.086 1   23.71 ? 62  LEU   A C   1 
ATOM   477  O  O   . LEU   A 1 77  ? 16.315  14.852  -30.546 1   23.24 ? 62  LEU   A O   1 
ATOM   478  C  CB  . LEU   A 1 77  ? 14.933  17.591  -30.381 1   22.94 ? 62  LEU   A CB  1 
ATOM   479  C  CG  . LEU   A 1 77  ? 14.489  19.018  -30.592 1   22.63 ? 62  LEU   A CG  1 
ATOM   480  C  CD1 . LEU   A 1 77  ? 12.974  19.144  -30.258 1   21.41 ? 62  LEU   A CD1 1 
ATOM   481  C  CD2 . LEU   A 1 77  ? 15.295  19.928  -29.701 1   23.68 ? 62  LEU   A CD2 1 
ATOM   482  N  N   . ASN   A 1 78  ? 17.323  16.013  -28.915 1   23.81 ? 63  ASN   A N   1 
ATOM   483  C  CA  . ASN   A 1 78  ? 17.48   14.869  -28.032 1   25.16 ? 63  ASN   A CA  1 
ATOM   484  C  C   . ASN   A 1 78  ? 16.166  14.783  -27.195 1   25.36 ? 63  ASN   A C   1 
ATOM   485  O  O   . ASN   A 1 78  ? 15.486  15.809  -27.025 1   24.83 ? 63  ASN   A O   1 
ATOM   486  C  CB  . ASN   A 1 78  ? 18.667  15.092  -27.071 1   27.51 ? 63  ASN   A CB  1 
ATOM   487  C  CG  . ASN   A 1 78  ? 19.969  15.072  -27.817 1   32.5  ? 63  ASN   A CG  1 
ATOM   488  O  OD1 . ASN   A 1 78  ? 20.202  14.205  -28.664 1   33.52 ? 63  ASN   A OD1 1 
ATOM   489  N  ND2 . ASN   A 1 78  ? 20.799  16.061  -27.574 1   34.46 ? 63  ASN   A ND2 1 
ATOM   490  N  N   . MET   A 1 79  ? 15.824  13.598  -26.664 1   25.34 ? 64  MET   A N   1 
ATOM   491  C  CA  . MET   A 1 79  ? 14.619  13.471  -25.838 1   26.56 ? 64  MET   A CA  1 
ATOM   492  C  C   . MET   A 1 79  ? 14.928  14.087  -24.491 1   27.91 ? 64  MET   A C   1 
ATOM   493  O  O   . MET   A 1 79  ? 15.816  13.619  -23.795 1   29.49 ? 64  MET   A O   1 
ATOM   494  C  CB  . MET   A 1 79  ? 14.176  12.019  -25.649 1   26.94 ? 64  MET   A CB  1 
ATOM   495  C  CG  . MET   A 1 79  ? 12.71   11.898  -25.122 1   27.45 ? 64  MET   A CG  1 
ATOM   496  S  SD  . MET   A 1 79  ? 12.267  10.175  -24.857 1   38.9  ? 64  MET   A SD  1 
ATOM   497  C  CE  . MET   A 1 79  ? 12.075  9.588   -26.506 1   31.73 ? 64  MET   A CE  1 
ATOM   498  N  N   . LEU   A 1 80  ? 14.217  15.143  -24.131 1   26.4  ? 65  LEU   A N   1 
ATOM   499  C  CA  . LEU   A 1 80  ? 14.421  15.817  -22.874 1   26.33 ? 65  LEU   A CA  1 
ATOM   500  C  C   . LEU   A 1 80  ? 13.364  15.385  -21.87  1   27.83 ? 65  LEU   A C   1 
ATOM   501  O  O   . LEU   A 1 80  ? 12.163  15.386  -22.179 1   28.36 ? 65  LEU   A O   1 
ATOM   502  C  CB  . LEU   A 1 80  ? 14.36   17.34   -23.089 1   25.89 ? 65  LEU   A CB  1 
ATOM   503  C  CG  . LEU   A 1 80  ? 15.482  17.917  -23.972 1   26.4  ? 65  LEU   A CG  1 
ATOM   504  C  CD1 . LEU   A 1 80  ? 15.386  19.447  -24.02  1   26.6  ? 65  LEU   A CD1 1 
ATOM   505  C  CD2 . LEU   A 1 80  ? 16.901  17.479  -23.434 1   27.22 ? 65  LEU   A CD2 1 
ATOM   506  N  N   . SER   A 1 81  ? 13.816  14.989  -20.668 1   27.1  ? 66  SER   A N   1 
ATOM   507  C  CA  . SER   A 1 81  ? 12.926  14.571  -19.597 1   27.11 ? 66  SER   A CA  1 
ATOM   508  C  C   . SER   A 1 81  ? 12.063  15.743  -19.115 1   26.36 ? 66  SER   A C   1 
ATOM   509  O  O   . SER   A 1 81  ? 12.554  16.865  -19.026 1   26.46 ? 66  SER   A O   1 
ATOM   510  C  CB  . SER   A 1 81  ? 13.75   14.047  -18.42  1   28.79 ? 66  SER   A CB  1 
ATOM   511  O  OG  . SER   A 1 81  ? 12.952  13.869  -17.257 1   31.23 ? 66  SER   A OG  1 
ATOM   512  N  N   . ILE   A 1 82  ? 10.815  15.464  -18.708 1   26.05 ? 67  ILE   A N   1 
ATOM   513  C  CA  . ILE   A 1 82  ? 9.944   16.517  -18.162 1   26.39 ? 67  ILE   A CA  1 
ATOM   514  C  C   . ILE   A 1 82  ? 10.134  16.742  -16.667 1   26.97 ? 67  ILE   A C   1 
ATOM   515  O  O   . ILE   A 1 82  ? 9.501   17.643  -16.129 1   26.94 ? 67  ILE   A O   1 
ATOM   516  C  CB  . ILE   A 1 82  ? 8.447   16.311  -18.49  1   26.62 ? 67  ILE   A CB  1 
ATOM   517  C  CG1 . ILE   A 1 82  ? 7.886   15.052  -17.766 1   27.67 ? 67  ILE   A CG1 1 
ATOM   518  C  CG2 . ILE   A 1 82  ? 8.218   16.265  -19.993 1   26.65 ? 67  ILE   A CG2 1 
ATOM   519  C  CD1 . ILE   A 1 82  ? 6.37    15.01   -17.588 1   29.12 ? 67  ILE   A CD1 1 
ATOM   520  N  N   . ASP   A 1 83  ? 11.024  15.977  -15.992 1   27.7  ? 68  ASP   A N   1 
ATOM   521  C  CA  . ASP   A 1 83  ? 11.217  16.07   -14.54  1   29.13 ? 68  ASP   A CA  1 
ATOM   522  C  C   . ASP   A 1 83  ? 11.688  17.423  -14.034 1   29.66 ? 68  ASP   A C   1 
ATOM   523  O  O   . ASP   A 1 83  ? 11.382  17.769  -12.89  1   30.52 ? 68  ASP   A O   1 
ATOM   524  C  CB  . ASP   A 1 83  ? 12.149  14.961  -14.047 1   32.52 ? 68  ASP   A CB  1 
ATOM   525  C  CG  . ASP   A 1 83  ? 11.622  13.561  -14.32  1   41.44 ? 68  ASP   A CG  1 
ATOM   526  O  OD1 . ASP   A 1 83  ? 10.417  13.422  -14.603 1   44.84 ? 68  ASP   A OD1 1 
ATOM   527  O  OD2 . ASP   A 1 83  ? 12.42   12.604  -14.264 1   46.69 ? 68  ASP   A OD2 1 
ATOM   528  N  N   . HIS   A 1 84  ? 12.309  18.229  -14.902 1   29.28 ? 69  HIS   A N   1 
ATOM   529  C  CA  . HIS   A 1 84  ? 12.791  19.569  -14.559 1   30.45 ? 69  HIS   A CA  1 
ATOM   530  C  C   . HIS   A 1 84  ? 11.703  20.673  -14.668 1   30.12 ? 69  HIS   A C   1 
ATOM   531  O  O   . HIS   A 1 84  ? 11.996  21.838  -14.408 1   30.15 ? 69  HIS   A O   1 
ATOM   532  C  CB  . HIS   A 1 84  ? 14.048  19.908  -15.382 1   33.03 ? 69  HIS   A CB  1 
ATOM   533  C  CG  . HIS   A 1 84  ? 15.073  18.817  -15.29  1   38.3  ? 69  HIS   A CG  1 
ATOM   534  N  ND1 . HIS   A 1 84  ? 15.889  18.688  -14.178 1   41.31 ? 69  HIS   A ND1 1 
ATOM   535  C  CD2 . HIS   A 1 84  ? 15.282  17.757  -16.109 1   39.94 ? 69  HIS   A CD2 1 
ATOM   536  C  CE1 . HIS   A 1 84  ? 16.617  17.601  -14.391 1   42.03 ? 69  HIS   A CE1 1 
ATOM   537  N  NE2 . HIS   A 1 84  ? 16.283  17.004  -15.539 1   41.41 ? 69  HIS   A NE2 1 
ATOM   538  N  N   . LEU   A 1 85  ? 10.45   20.307  -15.003 1   29.11 ? 70  LEU   A N   1 
ATOM   539  C  CA  . LEU   A 1 85  ? 9.315   21.251  -15.025 1   28.78 ? 70  LEU   A CA  1 
ATOM   540  C  C   . LEU   A 1 85  ? 8.559   20.973  -13.693 1   30.22 ? 70  LEU   A C   1 
ATOM   541  O  O   . LEU   A 1 85  ? 7.72    20.074  -13.613 1   30.08 ? 70  LEU   A O   1 
ATOM   542  C  CB  . LEU   A 1 85  ? 8.423   20.962  -16.241 1   27.38 ? 70  LEU   A CB  1 
ATOM   543  C  CG  . LEU   A 1 85  ? 9.132   21.059  -17.594 1   26.84 ? 70  LEU   A CG  1 
ATOM   544  C  CD1 . LEU   A 1 85  ? 8.285   20.402  -18.697 1   27.69 ? 70  LEU   A CD1 1 
ATOM   545  C  CD2 . LEU   A 1 85  ? 9.441   22.512  -17.943 1   25.93 ? 70  LEU   A CD2 1 
ATOM   546  N  N   . THR   A 1 86  ? 8.929   21.697  -12.653 1   31.21 ? 71  THR   A N   1 
ATOM   547  C  CA  . THR   A 1 86  ? 8.532   21.436  -11.268 1   33.4  ? 71  THR   A CA  1 
ATOM   548  C  C   . THR   A 1 86  ? 7.331   22.186  -10.723 1   34.52 ? 71  THR   A C   1 
ATOM   549  O  O   . THR   A 1 86  ? 6.936   21.926  -9.59   1   36.46 ? 71  THR   A O   1 
ATOM   550  C  CB  . THR   A 1 86  ? 9.74    21.717  -10.353 1   34.84 ? 71  THR   A CB  1 
ATOM   551  O  OG1 . THR   A 1 86  ? 10.189  23.058  -10.592 1   36.41 ? 71  THR   A OG1 1 
ATOM   552  C  CG2 . THR   A 1 86  ? 10.88   20.786  -10.628 1   35.92 ? 71  THR   A CG2 1 
ATOM   553  N  N   . ASP   A 1 87  ? 6.766   23.115  -11.478 1   33.31 ? 72  ASP   A N   1 
ATOM   554  C  CA  . ASP   A 1 87  ? 5.582   23.847  -11.029 1   31.42 ? 72  ASP   A CA  1 
ATOM   555  C  C   . ASP   A 1 87  ? 4.561   23.95   -12.169 1   29.59 ? 72  ASP   A C   1 
ATOM   556  O  O   . ASP   A 1 87  ? 4.918   23.78   -13.336 1   30.01 ? 72  ASP   A O   1 
ATOM   557  C  CB  . ASP   A 1 87  ? 5.957   25.219  -10.438 1   33.43 ? 72  ASP   A CB  1 
ATOM   558  C  CG  . ASP   A 1 87  ? 6.687   26.153  -11.387 1   40.82 ? 72  ASP   A CG  1 
ATOM   559  O  OD1 . ASP   A 1 87  ? 6.352   26.165  -12.584 1   41.87 ? 72  ASP   A OD1 1 
ATOM   560  O  OD2 . ASP   A 1 87  ? 7.573   26.896  -10.924 1   44.79 ? 72  ASP   A OD2 1 
ATOM   561  N  N   . HIS   A 1 88  ? 3.317   24.254  -11.835 1   27.06 ? 73  HIS   A N   1 
ATOM   562  C  CA  . HIS   A 1 88  ? 2.221   24.355  -12.792 1   25.93 ? 73  HIS   A CA  1 
ATOM   563  C  C   . HIS   A 1 88  ? 2.515   25.311  -13.972 1   24.5  ? 73  HIS   A C   1 
ATOM   564  O  O   . HIS   A 1 88  ? 2.242   24.948  -15.106 1   25.15 ? 73  HIS   A O   1 
ATOM   565  C  CB  . HIS   A 1 88  ? 0.923   24.79   -12.073 1   26.13 ? 73  HIS   A CB  1 
ATOM   566  C  CG  . HIS   A 1 88  ? -0.265  24.828  -12.99  1   26.18 ? 73  HIS   A CG  1 
ATOM   567  N  ND1 . HIS   A 1 88  ? -0.795  23.675  -13.523 1   27.32 ? 73  HIS   A ND1 1 
ATOM   568  C  CD2 . HIS   A 1 88  ? -0.965  25.886  -13.456 1   27.5  ? 73  HIS   A CD2 1 
ATOM   569  C  CE1 . HIS   A 1 88  ? -1.816  24.056  -14.28  1   27.83 ? 73  HIS   A CE1 1 
ATOM   570  N  NE2 . HIS   A 1 88  ? -1.947  25.379  -14.283 1   28.63 ? 73  HIS   A NE2 1 
ATOM   571  N  N   . LYS   A 1 89  ? 2.998   26.535  -13.702 1   23.14 ? 74  LYS   A N   1 
ATOM   572  C  CA  . LYS   A 1 89  ? 3.248   27.505  -14.763 1   22.27 ? 74  LYS   A CA  1 
ATOM   573  C  C   . LYS   A 1 89  ? 4.331   27.049  -15.746 1   21.81 ? 74  LYS   A C   1 
ATOM   574  O  O   . LYS   A 1 89  ? 4.205   27.318  -16.947 1   21.29 ? 74  LYS   A O   1 
ATOM   575  C  CB  . LYS   A 1 89  ? 3.577   28.884  -14.2   1   24.35 ? 74  LYS   A CB  1 
ATOM   576  C  CG  . LYS   A 1 89  ? 2.383   29.525  -13.525 1   27.38 ? 74  LYS   A CG  1 
ATOM   577  C  CD  . LYS   A 1 89  ? 2.583   30.994  -13.356 1   31.66 ? 74  LYS   A CD  1 
ATOM   578  C  CE  . LYS   A 1 89  ? 1.463   31.585  -12.54  1   34.27 ? 74  LYS   A CE  1 
ATOM   579  N  NZ  . LYS   A 1 89  ? 1.649   33.045  -12.407 1   36.97 ? 74  LYS   A NZ  1 
ATOM   580  N  N   . SER   A 1 90  ? 5.392   26.37   -15.255 1   21.19 ? 75  SER   A N   1 
ATOM   581  C  CA  . SER   A 1 90  ? 6.429   25.88   -16.184 1   20.86 ? 75  SER   A CA  1 
ATOM   582  C  C   . SER   A 1 90  ? 5.856   24.715  -17.011 1   19.12 ? 75  SER   A C   1 
ATOM   583  O  O   . SER   A 1 90  ? 6.214   24.567  -18.173 1   19.37 ? 75  SER   A O   1 
ATOM   584  C  CB  . SER   A 1 90  ? 7.717   25.485  -15.449 1   23.78 ? 75  SER   A CB  1 
ATOM   585  O  OG  . SER   A 1 90  ? 7.506   24.298  -14.703 1   29.52 ? 75  SER   A OG  1 
ATOM   586  N  N   . GLN   A 1 91  ? 4.99    23.88   -16.43  1   18.43 ? 76  GLN   A N   1 
ATOM   587  C  CA  . GLN   A 1 91  ? 4.375   22.772  -17.17  1   18.28 ? 76  GLN   A CA  1 
ATOM   588  C  C   . GLN   A 1 91  ? 3.385   23.329  -18.245 1   18.16 ? 76  GLN   A C   1 
ATOM   589  O  O   . GLN   A 1 91  ? 3.31    22.798  -19.332 1   19.11 ? 76  GLN   A O   1 
ATOM   590  C  CB  . GLN   A 1 91  ? 3.634   21.834  -16.202 1   19.97 ? 76  GLN   A CB  1 
ATOM   591  C  CG  . GLN   A 1 91  ? 4.583   21.031  -15.299 1   23.74 ? 76  GLN   A CG  1 
ATOM   592  C  CD  . GLN   A 1 91  ? 3.877   20.453  -14.07  1   29.2  ? 76  GLN   A CD  1 
ATOM   593  O  OE1 . GLN   A 1 91  ? 2.673   20.529  -13.912 1   28.71 ? 76  GLN   A OE1 1 
ATOM   594  N  NE2 . GLN   A 1 91  ? 4.64    19.892  -13.136 1   32.47 ? 76  GLN   A NE2 1 
ATOM   595  N  N   . ARG   A 1 92  ? 2.657   24.403  -17.93  1   16.86 ? 77  ARG   A N   1 
ATOM   596  C  CA  . ARG   A 1 92  ? 1.719   25.041  -18.878 1   16.24 ? 77  ARG   A CA  1 
ATOM   597  C  C   . ARG   A 1 92  ? 2.536   25.719  -20.023 1   16.08 ? 77  ARG   A C   1 
ATOM   598  O  O   . ARG   A 1 92  ? 2.145   25.629  -21.18  1   14.65 ? 77  ARG   A O   1 
ATOM   599  C  CB  . ARG   A 1 92  ? 0.851   26.072  -18.158 1   15.46 ? 77  ARG   A CB  1 
ATOM   600  C  CG  . ARG   A 1 92  ? -0.306  25.449  -17.323 1   15.93 ? 77  ARG   A CG  1 
ATOM   601  C  CD  . ARG   A 1 92  ? -1.425  24.775  -18.174 1   16.04 ? 77  ARG   A CD  1 
ATOM   602  N  NE  . ARG   A 1 92  ? -2.183  25.76   -18.964 1   16.05 ? 77  ARG   A NE  1 
ATOM   603  C  CZ  . ARG   A 1 92  ? -3.149  26.527  -18.462 1   20    ? 77  ARG   A CZ  1 
ATOM   604  N  NH1 . ARG   A 1 92  ? -3.57   26.346  -17.212 1   21.71 ? 77  ARG   A NH1 1 
ATOM   605  N  NH2 . ARG   A 1 92  ? -3.76   27.422  -19.228 1   20.02 ? 77  ARG   A NH2 1 
ATOM   606  N  N   . LEU   A 1 93  ? 3.668   26.349  -19.705 1   16.61 ? 78  LEU   A N   1 
ATOM   607  C  CA  . LEU   A 1 93  ? 4.516   26.97   -20.728 1   17.21 ? 78  LEU   A CA  1 
ATOM   608  C  C   . LEU   A 1 93  ? 5.092   25.888  -21.623 1   18.02 ? 78  LEU   A C   1 
ATOM   609  O  O   . LEU   A 1 93  ? 5.08    26.039  -22.85  1   19.15 ? 78  LEU   A O   1 
ATOM   610  C  CB  . LEU   A 1 93  ? 5.66    27.812  -20.11  1   17.51 ? 78  LEU   A CB  1 
ATOM   611  C  CG  . LEU   A 1 93  ? 6.735   28.348  -21.119 1   18.03 ? 78  LEU   A CG  1 
ATOM   612  C  CD1 . LEU   A 1 93  ? 6.105   29.196  -22.227 1   18.4  ? 78  LEU   A CD1 1 
ATOM   613  C  CD2 . LEU   A 1 93  ? 7.753   29.199  -20.395 1   18.82 ? 78  LEU   A CD2 1 
ATOM   614  N  N   . ALA   A 1 94  ? 5.53    24.754  -21.024 1   17.69 ? 79  ALA   A N   1 
ATOM   615  C  CA  . ALA   A 1 94  ? 6.096   23.676  -21.816 1   17.17 ? 79  ALA   A CA  1 
ATOM   616  C  C   . ALA   A 1 94  ? 5.034   23.075  -22.73  1   16.55 ? 79  ALA   A C   1 
ATOM   617  O  O   . ALA   A 1 94  ? 5.369   22.676  -23.839 1   17.35 ? 79  ALA   A O   1 
ATOM   618  C  CB  . ALA   A 1 94  ? 6.677   22.609  -20.923 1   16.98 ? 79  ALA   A CB  1 
ATOM   619  N  N   . ARG   A 1 95  ? 3.767   22.986  -22.277 1   15.39 ? 80  ARG   A N   1 
ATOM   620  C  CA  . ARG   A 1 95  ? 2.677   22.482  -23.136 1   15.68 ? 80  ARG   A CA  1 
ATOM   621  C  C   . ARG   A 1 95  ? 2.493   23.407  -24.324 1   15.33 ? 80  ARG   A C   1 
ATOM   622  O  O   . ARG   A 1 95  ? 2.21    22.939  -25.418 1   16.58 ? 80  ARG   A O   1 
ATOM   623  C  CB  . ARG   A 1 95  ? 1.332   22.485  -22.35  1   16.4  ? 80  ARG   A CB  1 
ATOM   624  C  CG  . ARG   A 1 95  ? 0.885   21.125  -21.937 1   18.38 ? 80  ARG   A CG  1 
ATOM   625  C  CD  . ARG   A 1 95  ? -0.593  21.162  -21.549 1   18.44 ? 80  ARG   A CD  1 
ATOM   626  N  NE  . ARG   A 1 95  ? -1.513  21.39   -22.668 1   16.73 ? 80  ARG   A NE  1 
ATOM   627  C  CZ  . ARG   A 1 95  ? -1.963  20.431  -23.474 1   16.33 ? 80  ARG   A CZ  1 
ATOM   628  N  NH1 . ARG   A 1 95  ? -1.519  19.181  -23.344 1   14.42 ? 80  ARG   A NH1 1 
ATOM   629  N  NH2 . ARG   A 1 95  ? -2.822  20.721  -24.444 1   15.11 ? 80  ARG   A NH2 1 
ATOM   630  N  N   . LEU   A 1 96  ? 2.552   24.711  -24.094 1   15.67 ? 81  LEU   A N   1 
ATOM   631  C  CA  . LEU   A 1 96  ? 2.34    25.693  -25.157 1   17.25 ? 81  LEU   A CA  1 
ATOM   632  C  C   . LEU   A 1 96  ? 3.527   25.598  -26.174 1   17.46 ? 81  LEU   A C   1 
ATOM   633  O  O   . LEU   A 1 96  ? 3.299   25.615  -27.38  1   17.02 ? 81  LEU   A O   1 
ATOM   634  C  CB  . LEU   A 1 96  ? 2.276   27.075  -24.524 1   16.93 ? 81  LEU   A CB  1 
ATOM   635  C  CG  . LEU   A 1 96  ? 2.306   28.269  -25.458 1   18.54 ? 81  LEU   A CG  1 
ATOM   636  C  CD1 . LEU   A 1 96  ? 1.126   28.235  -26.516 1   18.81 ? 81  LEU   A CD1 1 
ATOM   637  C  CD2 . LEU   A 1 96  ? 2.234   29.548  -24.632 1   20.14 ? 81  LEU   A CD2 1 
ATOM   638  N  N   . VAL   A 1 97  ? 4.777   25.467  -25.666 1   17.38 ? 82  VAL   A N   1 
ATOM   639  C  CA  . VAL   A 1 97  ? 5.985   25.309  -26.487 1   17.54 ? 82  VAL   A CA  1 
ATOM   640  C  C   . VAL   A 1 97  ? 5.857   24.026  -27.329 1   17.64 ? 82  VAL   A C   1 
ATOM   641  O  O   . VAL   A 1 97  ? 5.971   24.096  -28.546 1   18.69 ? 82  VAL   A O   1 
ATOM   642  C  CB  . VAL   A 1 97  ? 7.26    25.246  -25.592 1   18.38 ? 82  VAL   A CB  1 
ATOM   643  C  CG1 . VAL   A 1 97  ? 8.477   24.691  -26.37  1   18.85 ? 82  VAL   A CG1 1 
ATOM   644  C  CG2 . VAL   A 1 97  ? 7.574   26.621  -25.021 1   18.91 ? 82  VAL   A CG2 1 
ATOM   645  N  N   . LEU   A 1 98  ? 5.596   22.868  -26.692 1   16.77 ? 83  LEU   A N   1 
ATOM   646  C  CA  . LEU   A 1 98  ? 5.525   21.603  -27.418 1   16.83 ? 83  LEU   A CA  1 
ATOM   647  C  C   . LEU   A 1 98  ? 4.343   21.556  -28.384 1   16.38 ? 83  LEU   A C   1 
ATOM   648  O  O   . LEU   A 1 98  ? 4.457   20.967  -29.449 1   15.78 ? 83  LEU   A O   1 
ATOM   649  C  CB  . LEU   A 1 98  ? 5.467   20.428  -26.441 1   17.14 ? 83  LEU   A CB  1 
ATOM   650  C  CG  . LEU   A 1 98  ? 6.767   20.252  -25.591 1   18.8  ? 83  LEU   A CG  1 
ATOM   651  C  CD1 . LEU   A 1 98  ? 6.535   19.256  -24.487 1   17.63 ? 83  LEU   A CD1 1 
ATOM   652  C  CD2 . LEU   A 1 98  ? 7.952   19.81   -26.487 1   19.69 ? 83  LEU   A CD2 1 
ATOM   653  N  N   . GLY   A 1 99  ? 3.224   22.16   -27.981 1   15.76 ? 84  GLY   A N   1 
ATOM   654  C  CA  . GLY   A 1 99  ? 2.011   22.185  -28.806 1   15.92 ? 84  GLY   A CA  1 
ATOM   655  C  C   . GLY   A 1 99  ? 2.225   23.013  -30.055 1   15.72 ? 84  GLY   A C   1 
ATOM   656  O  O   . GLY   A 1 99  ? 1.763   22.618  -31.112 1   16.09 ? 84  GLY   A O   1 
ATOM   657  N  N   . CYS   A 1 100 ? 2.88    24.19   -29.941 1   15.85 ? 85  CYS   A N   1 
ATOM   658  C  CA  . CYS   A 1 100 ? 3.18    25.026  -31.121 1   15.74 ? 85  CYS   A CA  1 
ATOM   659  C  C   . CYS   A 1 100 ? 4.152   24.315  -32.057 1   15.14 ? 85  CYS   A C   1 
ATOM   660  O  O   . CYS   A 1 100 ? 3.934   24.296  -33.257 1   15.52 ? 85  CYS   A O   1 
ATOM   661  C  CB  . CYS   A 1 100 ? 3.732   26.384  -30.714 1   16.12 ? 85  CYS   A CB  1 
ATOM   662  S  SG  . CYS   A 1 100 ? 2.49    27.464  -29.964 1   18.57 ? 85  CYS   A SG  1 
ATOM   663  N  N   . ILE   A 1 101 ? 5.157   23.652  -31.491 1   14.5  ? 86  ILE   A N   1 
ATOM   664  C  CA  . ILE   A 1 101 ? 6.143   22.911  -32.297 1   15.48 ? 86  ILE   A CA  1 
ATOM   665  C  C   . ILE   A 1 101 ? 5.417   21.772  -33.024 1   15.75 ? 86  ILE   A C   1 
ATOM   666  O  O   . ILE   A 1 101 ? 5.73    21.507  -34.189 1   16.93 ? 86  ILE   A O   1 
ATOM   667  C  CB  . ILE   A 1 101 ? 7.26    22.339  -31.368 1   16.1  ? 86  ILE   A CB  1 
ATOM   668  C  CG1 . ILE   A 1 101 ? 8.153   23.51   -30.837 1   15.93 ? 86  ILE   A CG1 1 
ATOM   669  C  CG2 . ILE   A 1 101 ? 8.154   21.316  -32.145 1   16.91 ? 86  ILE   A CG2 1 
ATOM   670  C  CD1 . ILE   A 1 101 ? 9.172   23.057  -29.796 1   16.96 ? 86  ILE   A CD1 1 
ATOM   671  N  N   . THR   A 1 102 ? 4.477   21.068  -32.334 1   14.79 ? 87  THR   A N   1 
ATOM   672  C  CA  . THR   A 1 102 ? 3.764   19.959  -32.946 1   14.76 ? 87  THR   A CA  1 
ATOM   673  C  C   . THR   A 1 102 ? 2.929   20.429  -34.137 1   16.17 ? 87  THR   A C   1 
ATOM   674  O  O   . THR   A 1 102 ? 2.919   19.775  -35.18  1   17.43 ? 87  THR   A O   1 
ATOM   675  C  CB  . THR   A 1 102 ? 2.934   19.205  -31.876 1   16.66 ? 87  THR   A CB  1 
ATOM   676  O  OG1 . THR   A 1 102 ? 3.82    18.614  -30.908 1   18.21 ? 87  THR   A OG1 1 
ATOM   677  C  CG2 . THR   A 1 102 ? 1.985   18.196  -32.465 1   17.35 ? 87  THR   A CG2 1 
ATOM   678  N  N   . MET   A 1 103 ? 2.209   21.559  -34.01  1   15.93 ? 88  MET   A N   1 
ATOM   679  C  CA  A MET   A 1 103 ? 1.413   22.083  -35.125 0.5 16.61 ? 88  MET   A CA  1 
ATOM   680  C  CA  B MET   A 1 103 ? 1.396   22.069  -35.126 0.5 16.14 ? 88  MET   A CA  1 
ATOM   681  C  C   . MET   A 1 103 ? 2.307   22.412  -36.324 1   17.79 ? 88  MET   A C   1 
ATOM   682  O  O   . MET   A 1 103 ? 1.969   22.084  -37.464 1   20.17 ? 88  MET   A O   1 
ATOM   683  C  CB  A MET   A 1 103 ? 0.618   23.324  -34.677 0.5 17.2  ? 88  MET   A CB  1 
ATOM   684  C  CB  B MET   A 1 103 ? 0.568   23.298  -34.689 0.5 15.7  ? 88  MET   A CB  1 
ATOM   685  C  CG  A MET   A 1 103 ? -0.606  22.965  -33.876 0.5 18.78 ? 88  MET   A CG  1 
ATOM   686  C  CG  B MET   A 1 103 ? -0.189  23.097  -33.382 0.5 14.98 ? 88  MET   A CG  1 
ATOM   687  S  SD  A MET   A 1 103 ? -1.757  21.932  -34.832 0.5 23.42 ? 88  MET   A SD  1 
ATOM   688  S  SD  B MET   A 1 103 ? -1.201  21.596  -33.246 0.5 15    ? 88  MET   A SD  1 
ATOM   689  C  CE  A MET   A 1 103 ? -2.788  21.449  -33.614 0.5 25.14 ? 88  MET   A CE  1 
ATOM   690  C  CE  B MET   A 1 103 ? -2.501  22.013  -34.28  0.5 18.58 ? 88  MET   A CE  1 
ATOM   691  N  N   . ALA   A 1 104 ? 3.443   23.048  -36.063 1   17.38 ? 89  ALA   A N   1 
ATOM   692  C  CA  . ALA   A 1 104 ? 4.383   23.442  -37.111 1   18.36 ? 89  ALA   A CA  1 
ATOM   693  C  C   . ALA   A 1 104 ? 4.98    22.196  -37.77  1   19.7  ? 89  ALA   A C   1 
ATOM   694  O  O   . ALA   A 1 104 ? 5.082   22.148  -38.989 1   20.65 ? 89  ALA   A O   1 
ATOM   695  C  CB  . ALA   A 1 104 ? 5.492   24.296  -36.525 1   17.84 ? 89  ALA   A CB  1 
ATOM   696  N  N   . TYR   A 1 105 ? 5.285   21.165  -36.964 1   19.16 ? 90  TYR   A N   1 
ATOM   697  C  CA  . TYR   A 1 105 ? 5.862   19.933  -37.481 1   19.35 ? 90  TYR   A CA  1 
ATOM   698  C  C   . TYR   A 1 105 ? 4.843   19.184  -38.358 1   18.79 ? 90  TYR   A C   1 
ATOM   699  O  O   . TYR   A 1 105 ? 5.194   18.729  -39.449 1   19.3  ? 90  TYR   A O   1 
ATOM   700  C  CB  . TYR   A 1 105 ? 6.387   19.046  -36.325 1   18.87 ? 90  TYR   A CB  1 
ATOM   701  C  CG  . TYR   A 1 105 ? 7.153   17.848  -36.841 1   19.62 ? 90  TYR   A CG  1 
ATOM   702  C  CD1 . TYR   A 1 105 ? 8.499   17.955  -37.191 1   21.46 ? 90  TYR   A CD1 1 
ATOM   703  C  CD2 . TYR   A 1 105 ? 6.505   16.646  -37.103 1   20.08 ? 90  TYR   A CD2 1 
ATOM   704  C  CE1 . TYR   A 1 105 ? 9.201   16.86   -37.712 1   22.67 ? 90  TYR   A CE1 1 
ATOM   705  C  CE2 . TYR   A 1 105 ? 7.183   15.568  -37.662 1   21.74 ? 90  TYR   A CE2 1 
ATOM   706  C  CZ  . TYR   A 1 105 ? 8.524   15.685  -37.982 1   23.38 ? 90  TYR   A CZ  1 
ATOM   707  O  OH  . TYR   A 1 105 ? 9.192   14.588  -38.484 1   26.6  ? 90  TYR   A OH  1 
ATOM   708  N  N   . VAL   A 1 106 ? 3.625   19.016  -37.87  1   17.18 ? 91  VAL   A N   1 
ATOM   709  C  CA  . VAL   A 1 106 ? 2.598   18.29   -38.616 1   18.66 ? 91  VAL   A CA  1 
ATOM   710  C  C   . VAL   A 1 106 ? 2.218   18.995  -39.921 1   21.21 ? 91  VAL   A C   1 
ATOM   711  O  O   . VAL   A 1 106 ? 2.184   18.346  -40.976 1   22.51 ? 91  VAL   A O   1 
ATOM   712  C  CB  . VAL   A 1 106 ? 1.342   17.991  -37.747 1   19.05 ? 91  VAL   A CB  1 
ATOM   713  C  CG1 . VAL   A 1 106 ? 0.186   17.467  -38.606 1   19.01 ? 91  VAL   A CG1 1 
ATOM   714  C  CG2 . VAL   A 1 106 ? 1.675   17.012  -36.616 1   20.13 ? 91  VAL   A CG2 1 
ATOM   715  N  N   . TRP   A 1 107 ? 1.927   20.308  -39.862 1   19.75 ? 92  TRP   A N   1 
ATOM   716  C  CA  . TRP   A 1 107 ? 1.44    21.025  -41.035 1   19.02 ? 92  TRP   A CA  1 
ATOM   717  C  C   . TRP   A 1 107 ? 2.544   21.601  -41.957 1   19.99 ? 92  TRP   A C   1 
ATOM   718  O  O   . TRP   A 1 107 ? 2.257   21.879  -43.119 1   19.72 ? 92  TRP   A O   1 
ATOM   719  C  CB  . TRP   A 1 107 ? 0.449   22.148  -40.593 1   18.05 ? 92  TRP   A CB  1 
ATOM   720  C  CG  . TRP   A 1 107 ? -0.729  21.626  -39.804 1   18.8  ? 92  TRP   A CG  1 
ATOM   721  C  CD1 . TRP   A 1 107 ? -1.1    21.981  -38.538 1   19.54 ? 92  TRP   A CD1 1 
ATOM   722  C  CD2 . TRP   A 1 107 ? -1.635  20.59   -40.216 1   19.71 ? 92  TRP   A CD2 1 
ATOM   723  N  NE1 . TRP   A 1 107 ? -2.18   21.212  -38.131 1   20.55 ? 92  TRP   A NE1 1 
ATOM   724  C  CE2 . TRP   A 1 107 ? -2.55   20.384  -39.159 1   20.72 ? 92  TRP   A CE2 1 
ATOM   725  C  CE3 . TRP   A 1 107 ? -1.802  19.86   -41.407 1   21.94 ? 92  TRP   A CE3 1 
ATOM   726  C  CZ2 . TRP   A 1 107 ? -3.59   19.464  -39.242 1   23.19 ? 92  TRP   A CZ2 1 
ATOM   727  C  CZ3 . TRP   A 1 107 ? -2.827  18.932  -41.477 1   23.69 ? 92  TRP   A CZ3 1 
ATOM   728  C  CH2 . TRP   A 1 107 ? -3.703  18.739  -40.396 1   23.94 ? 92  TRP   A CH2 1 
ATOM   729  N  N   . GLY   A 1 108 ? 3.721   21.882  -41.413 1   20.53 ? 93  GLY   A N   1 
ATOM   730  C  CA  . GLY   A 1 108 ? 4.826   22.47   -42.178 1   22.56 ? 93  GLY   A CA  1 
ATOM   731  C  C   . GLY   A 1 108 ? 4.428   23.823  -42.731 1   24.99 ? 93  GLY   A C   1 
ATOM   732  O  O   . GLY   A 1 108 ? 3.818   24.615  -42.011 1   24.89 ? 93  GLY   A O   1 
ATOM   733  N  N   . LYS   A 1 109 ? 4.648   24.063  -44.028 1   27.13 ? 94  LYS   A N   1 
ATOM   734  C  CA  . LYS   A 1 109 ? 4.22    25.31   -44.693 1   29.61 ? 94  LYS   A CA  1 
ATOM   735  C  C   . LYS   A 1 109 ? 2.714   25.364  -44.994 1   32.13 ? 94  LYS   A C   1 
ATOM   736  O  O   . LYS   A 1 109 ? 2.25    26.37   -45.523 1   32.21 ? 94  LYS   A O   1 
ATOM   737  C  CB  . LYS   A 1 109 ? 5.001   25.552  -46.002 1   31.36 ? 94  LYS   A CB  1 
ATOM   738  C  CG  . LYS   A 1 109 ? 6.502   25.638  -45.805 1   34.12 ? 94  LYS   A CG  1 
ATOM   739  C  CD  . LYS   A 1 109 ? 7.217   25.982  -47.097 1   36.2  ? 94  LYS   A CD  1 
ATOM   740  C  CE  . LYS   A 1 109 ? 8.71    25.954  -46.915 1   39.22 ? 94  LYS   A CE  1 
ATOM   741  N  NZ  . LYS   A 1 109 ? 9.427   26.277  -48.169 1   42.18 ? 94  LYS   A NZ  1 
ATOM   742  N  N   . GLY   A 1 110 ? 1.981   24.292  -44.7   1   33.6  ? 95  GLY   A N   1 
ATOM   743  C  CA  . GLY   A 1 110 ? 0.539   24.232  -44.871 1   36.4  ? 95  GLY   A CA  1 
ATOM   744  C  C   . GLY   A 1 110 ? 0.05    24.03   -46.288 1   39.78 ? 95  GLY   A C   1 
ATOM   745  O  O   . GLY   A 1 110 ? -1.065  24.451  -46.61  1   40.98 ? 95  GLY   A O   1 
ATOM   746  N  N   . HIS   A 1 111 ? 0.839   23.358  -47.137 1   41.13 ? 96  HIS   A N   1 
ATOM   747  C  CA  . HIS   A 1 111 ? 0.438   23.178  -48.53  1   43.71 ? 96  HIS   A CA  1 
ATOM   748  C  C   . HIS   A 1 111 ? 0.35    21.725  -48.954 1   44.08 ? 96  HIS   A C   1 
ATOM   749  O  O   . HIS   A 1 111 ? 0.717   21.38   -50.072 1   44.42 ? 96  HIS   A O   1 
ATOM   750  C  CB  . HIS   A 1 111 ? 1.335   23.994  -49.477 1   46.59 ? 96  HIS   A CB  1 
ATOM   751  C  CG  . HIS   A 1 111 ? 1.2     25.464  -49.238 1   52.11 ? 96  HIS   A CG  1 
ATOM   752  N  ND1 . HIS   A 1 111 ? -0.041  26.093  -49.296 1   54.62 ? 96  HIS   A ND1 1 
ATOM   753  C  CD2 . HIS   A 1 111 ? 2.141   26.378  -48.895 1   54.21 ? 96  HIS   A CD2 1 
ATOM   754  C  CE1 . HIS   A 1 111 ? 0.188   27.363  -48.999 1   55.56 ? 96  HIS   A CE1 1 
ATOM   755  N  NE2 . HIS   A 1 111 ? 1.489   27.586  -48.76  1   55.7  ? 96  HIS   A NE2 1 
ATOM   756  N  N   . GLY   A 1 112 ? -0.172  20.888  -48.071 1   43.73 ? 97  GLY   A N   1 
ATOM   757  C  CA  . GLY   A 1 112 ? -0.395  19.488  -48.393 1   43.57 ? 97  GLY   A CA  1 
ATOM   758  C  C   . GLY   A 1 112 ? 0.667   18.501  -47.972 1   43.35 ? 97  GLY   A C   1 
ATOM   759  O  O   . GLY   A 1 112 ? 0.376   17.31   -47.922 1   44.69 ? 97  GLY   A O   1 
ATOM   760  N  N   . ASP   A 1 113 ? 1.888   18.952  -47.662 1   42.24 ? 98  ASP   A N   1 
ATOM   761  C  CA  . ASP   A 1 113 ? 2.942   18.01   -47.257 1   41.72 ? 98  ASP   A CA  1 
ATOM   762  C  C   . ASP   A 1 113 ? 2.892   17.878  -45.744 1   38.96 ? 98  ASP   A C   1 
ATOM   763  O  O   . ASP   A 1 113 ? 3.484   18.682  -45.035 1   38.73 ? 98  ASP   A O   1 
ATOM   764  C  CB  . ASP   A 1 113 ? 4.333   18.442  -47.757 1   44.79 ? 98  ASP   A CB  1 
ATOM   765  C  CG  . ASP   A 1 113 ? 5.412   17.443  -47.379 1   52.22 ? 98  ASP   A CG  1 
ATOM   766  O  OD1 . ASP   A 1 113 ? 5.119   16.222  -47.37  1   53.96 ? 98  ASP   A OD1 1 
ATOM   767  O  OD2 . ASP   A 1 113 ? 6.541   17.88   -47.071 1   55.33 ? 98  ASP   A OD2 1 
ATOM   768  N  N   . VAL   A 1 114 ? 2.116   16.905  -45.262 1   36.51 ? 99  VAL   A N   1 
ATOM   769  C  CA  . VAL   A 1 114 ? 1.873   16.713  -43.84  1   35.12 ? 99  VAL   A CA  1 
ATOM   770  C  C   . VAL   A 1 114 ? 2.67    15.556  -43.233 1   32.28 ? 99  VAL   A C   1 
ATOM   771  O  O   . VAL   A 1 114 ? 2.851   14.527  -43.886 1   34.24 ? 99  VAL   A O   1 
ATOM   772  C  CB  . VAL   A 1 114 ? 0.342   16.534  -43.598 1   36.69 ? 99  VAL   A CB  1 
ATOM   773  C  CG1 . VAL   A 1 114 ? -0.225  15.429  -44.464 1   37.98 ? 99  VAL   A CG1 1 
ATOM   774  C  CG2 . VAL   A 1 114 ? 0.022   16.241  -42.142 1   37.27 ? 99  VAL   A CG2 1 
ATOM   775  N  N   . ARG   A 1 115 ? 3.124   15.706  -41.988 1   27.37 ? 100 ARG   A N   1 
ATOM   776  C  CA  A ARG   A 1 115 ? 3.804   14.616  -41.299 0.5 25.91 ? 100 ARG   A CA  1 
ATOM   777  C  CA  B ARG   A 1 115 ? 3.801   14.619  -41.292 0.5 25.77 ? 100 ARG   A CA  1 
ATOM   778  C  C   . ARG   A 1 115 ? 2.76    13.897  -40.443 1   25.73 ? 100 ARG   A C   1 
ATOM   779  O  O   . ARG   A 1 115 ? 2.056   14.535  -39.647 1   24.53 ? 100 ARG   A O   1 
ATOM   780  C  CB  A ARG   A 1 115 ? 4.986   15.12   -40.45  0.5 25.74 ? 100 ARG   A CB  1 
ATOM   781  C  CB  B ARG   A 1 115 ? 4.956   15.136  -40.42  0.5 25.23 ? 100 ARG   A CB  1 
ATOM   782  C  CG  A ARG   A 1 115 ? 6.183   15.624  -41.283 0.5 26.61 ? 100 ARG   A CG  1 
ATOM   783  C  CG  B ARG   A 1 115 ? 6.158   15.646  -41.228 0.5 25.52 ? 100 ARG   A CG  1 
ATOM   784  C  CD  A ARG   A 1 115 ? 6.975   14.487  -41.939 0.5 28.91 ? 100 ARG   A CD  1 
ATOM   785  C  CD  B ARG   A 1 115 ? 6.837   14.529  -42.019 0.5 27.25 ? 100 ARG   A CD  1 
ATOM   786  N  NE  A ARG   A 1 115 ? 7.869   14.965  -43.006 0.5 31.01 ? 100 ARG   A NE  1 
ATOM   787  N  NE  B ARG   A 1 115 ? 7.878   15.045  -42.918 0.5 28.72 ? 100 ARG   A NE  1 
ATOM   788  C  CZ  A ARG   A 1 115 ? 9.185   15.106  -42.881 0.5 32.11 ? 100 ARG   A CZ  1 
ATOM   789  C  CZ  B ARG   A 1 115 ? 7.657   15.456  -44.163 0.5 28.8  ? 100 ARG   A CZ  1 
ATOM   790  N  NH1 A ARG   A 1 115 ? 9.789   14.792  -41.743 0.5 29.84 ? 100 ARG   A NH1 1 
ATOM   791  N  NH1 B ARG   A 1 115 ? 6.442   15.378  -44.689 0.5 27.39 ? 100 ARG   A NH1 1 
ATOM   792  N  NH2 A ARG   A 1 115 ? 9.907   15.569  -43.893 0.5 34.18 ? 100 ARG   A NH2 1 
ATOM   793  N  NH2 B ARG   A 1 115 ? 8.652   15.931  -44.896 0.5 28.35 ? 100 ARG   A NH2 1 
ATOM   794  N  N   . LYS   A 1 116 ? 2.654   12.581  -40.612 1   25.24 ? 101 LYS   A N   1 
ATOM   795  C  CA  . LYS   A 1 116 ? 1.715   11.739  -39.875 1   25.36 ? 101 LYS   A CA  1 
ATOM   796  C  C   . LYS   A 1 116 ? 2.34    11.044  -38.648 1   24.35 ? 101 LYS   A C   1 
ATOM   797  O  O   . LYS   A 1 116 ? 1.66    10.282  -37.962 1   24.79 ? 101 LYS   A O   1 
ATOM   798  C  CB  . LYS   A 1 116 ? 1.144   10.673  -40.817 1   28.39 ? 101 LYS   A CB  1 
ATOM   799  C  CG  . LYS   A 1 116 ? 0.46    11.266  -42.028 1   33.63 ? 101 LYS   A CG  1 
ATOM   800  C  CD  . LYS   A 1 116 ? -0.871  10.552  -42.289 1   40.32 ? 101 LYS   A CD  1 
ATOM   801  C  CE  . LYS   A 1 116 ? -1.472  10.841  -43.648 1   45.33 ? 101 LYS   A CE  1 
ATOM   802  N  NZ  . LYS   A 1 116 ? -0.992  12.117  -44.218 1   48.13 ? 101 LYS   A NZ  1 
ATOM   803  N  N   . VAL   A 1 117 ? 3.613   11.248  -38.4   1   23.32 ? 102 VAL   A N   1 
ATOM   804  C  CA  . VAL   A 1 117 ? 4.304   10.667  -37.258 1   22.2  ? 102 VAL   A CA  1 
ATOM   805  C  C   . VAL   A 1 117 ? 5.021   11.784  -36.539 1   22.34 ? 102 VAL   A C   1 
ATOM   806  O  O   . VAL   A 1 117 ? 5.841   12.475  -37.138 1   23.45 ? 102 VAL   A O   1 
ATOM   807  C  CB  . VAL   A 1 117 ? 5.307   9.526   -37.648 1   21.4  ? 102 VAL   A CB  1 
ATOM   808  C  CG1 . VAL   A 1 117 ? 6.012   8.984   -36.404 1   21.07 ? 102 VAL   A CG1 1 
ATOM   809  C  CG2 . VAL   A 1 117 ? 4.597   8.395   -38.392 1   21.23 ? 102 VAL   A CG2 1 
ATOM   810  N  N   . LEU   A 1 118 ? 4.726   11.964  -35.251 1   21.32 ? 103 LEU   A N   1 
ATOM   811  C  CA  . LEU   A 1 118 ? 5.401   12.968  -34.439 1   20.6  ? 103 LEU   A CA  1 
ATOM   812  C  C   . LEU   A 1 118 ? 6.616   12.247  -33.811 1   20.98 ? 103 LEU   A C   1 
ATOM   813  O  O   . LEU   A 1 118 ? 6.41    11.257  -33.121 1   19.95 ? 103 LEU   A O   1 
ATOM   814  C  CB  . LEU   A 1 118 ? 4.442   13.46   -33.344 1   19.67 ? 103 LEU   A CB  1 
ATOM   815  C  CG  . LEU   A 1 118 ? 4.925   14.638  -32.52  1   20.3  ? 103 LEU   A CG  1 
ATOM   816  C  CD1 . LEU   A 1 118 ? 5.137   15.873  -33.413 1   19.89 ? 103 LEU   A CD1 1 
ATOM   817  C  CD2 . LEU   A 1 118 ? 3.931   14.936  -31.368 1   19.83 ? 103 LEU   A CD2 1 
ATOM   818  N  N   . PRO   A 1 119 ? 7.86    12.711  -34.062 1   22.06 ? 104 PRO   A N   1 
ATOM   819  C  CA  . PRO   A 1 119 ? 9.041   12.016  -33.512 1   22.08 ? 104 PRO   A CA  1 
ATOM   820  C  C   . PRO   A 1 119 ? 9.031   11.838  -32.018 1   20.82 ? 104 PRO   A C   1 
ATOM   821  O  O   . PRO   A 1 119 ? 8.588   12.724  -31.287 1   20.52 ? 104 PRO   A O   1 
ATOM   822  C  CB  . PRO   A 1 119 ? 10.244  12.862  -33.982 1   23.77 ? 104 PRO   A CB  1 
ATOM   823  C  CG  . PRO   A 1 119 ? 9.736   13.69   -35.086 1   24.59 ? 104 PRO   A CG  1 
ATOM   824  C  CD  . PRO   A 1 119 ? 8.247   13.87   -34.88  1   22.22 ? 104 PRO   A CD  1 
ATOM   825  N  N   . ARG   A 1 120 ? 9.528   10.666  -31.554 1   20.07 ? 105 ARG   A N   1 
ATOM   826  C  CA  . ARG   A 1 120 ? 9.559   10.343  -30.137 1   19.71 ? 105 ARG   A CA  1 
ATOM   827  C  C   . ARG   A 1 120 ? 10.233  11.389  -29.266 1   19.72 ? 105 ARG   A C   1 
ATOM   828  O  O   . ARG   A 1 120 ? 9.811   11.571  -28.129 1   20.16 ? 105 ARG   A O   1 
ATOM   829  C  CB  . ARG   A 1 120 ? 10.222  8.977   -29.9   1   21.44 ? 105 ARG   A CB  1 
ATOM   830  C  CG  . ARG   A 1 120 ? 11.738  9.005   -30.229 1   25.13 ? 105 ARG   A CG  1 
ATOM   831  C  CD  . ARG   A 1 120 ? 12.337  7.681   -30.727 1   28.82 ? 105 ARG   A CD  1 
ATOM   832  N  NE  . ARG   A 1 120 ? 11.758  6.624   -29.964 1   31.32 ? 105 ARG   A NE  1 
ATOM   833  C  CZ  . ARG   A 1 120 ? 11.02   5.643   -30.447 1   30.03 ? 105 ARG   A CZ  1 
ATOM   834  N  NH1 . ARG   A 1 120 ? 10.985  5.409   -31.753 1   27.01 ? 105 ARG   A NH1 1 
ATOM   835  N  NH2 . ARG   A 1 120 ? 10.427  4.803   -29.627 1   30.9  ? 105 ARG   A NH2 1 
ATOM   836  N  N   . ASN   A 1 121 ? 11.248  12.092  -29.776 1   19.07 ? 106 ASN   A N   1 
ATOM   837  C  CA  . ASN   A 1 121 ? 11.965  13.095  -28.974 1   20.15 ? 106 ASN   A CA  1 
ATOM   838  C  C   . ASN   A 1 121 ? 11.038  14.188  -28.465 1   21.44 ? 106 ASN   A C   1 
ATOM   839  O  O   . ASN   A 1 121 ? 11.322  14.741  -27.403 1   23.35 ? 106 ASN   A O   1 
ATOM   840  C  CB  . ASN   A 1 121 ? 13.184  13.707  -29.711 1   20.7  ? 106 ASN   A CB  1 
ATOM   841  C  CG  . ASN   A 1 121 ? 12.857  14.31   -31.093 1   26.16 ? 106 ASN   A CG  1 
ATOM   842  O  OD1 . ASN   A 1 121 ? 11.696  14.545  -31.441 1   29.23 ? 106 ASN   A OD1 1 
ATOM   843  N  ND2 . ASN   A 1 121 ? 13.853  14.494  -31.987 1   24.29 ? 106 ASN   A ND2 1 
ATOM   844  N  N   . ILE   A 1 122 ? 9.963   14.514  -29.22  1   20.01 ? 107 ILE   A N   1 
ATOM   845  C  CA  . ILE   A 1 122 ? 8.95    15.467  -28.732 1   21.33 ? 107 ILE   A CA  1 
ATOM   846  C  C   . ILE   A 1 122 ? 7.645   14.769  -28.289 1   19.44 ? 107 ILE   A C   1 
ATOM   847  O  O   . ILE   A 1 122 ? 7.042   15.204  -27.311 1   18.75 ? 107 ILE   A O   1 
ATOM   848  C  CB  . ILE   A 1 122 ? 8.67    16.637  -29.676 1   25.38 ? 107 ILE   A CB  1 
ATOM   849  C  CG1 . ILE   A 1 122 ? 8.442   16.19   -31.108 1   28.85 ? 107 ILE   A CG1 1 
ATOM   850  C  CG2 . ILE   A 1 122 ? 9.763   17.713  -29.582 1   26.83 ? 107 ILE   A CG2 1 
ATOM   851  C  CD1 . ILE   A 1 122 ? 7.983   17.337  -31.971 1   31.96 ? 107 ILE   A CD1 1 
ATOM   852  N  N   . ALA   A 1 123 ? 7.191   13.715  -28.999 1   18.06 ? 108 ALA   A N   1 
ATOM   853  C  CA  . ALA   A 1 123 ? 5.962   13.034  -28.654 1   18.65 ? 108 ALA   A CA  1 
ATOM   854  C  C   . ALA   A 1 123 ? 5.948   12.48   -27.26  1   18.52 ? 108 ALA   A C   1 
ATOM   855  O  O   . ALA   A 1 123 ? 4.947   12.635  -26.539 1   17.35 ? 108 ALA   A O   1 
ATOM   856  C  CB  . ALA   A 1 123 ? 5.637   11.929  -29.67  1   19.44 ? 108 ALA   A CB  1 
ATOM   857  N  N   . VAL   A 1 124 ? 7.07    11.853  -26.835 1   18.57 ? 109 VAL   A N   1 
ATOM   858  C  CA  . VAL   A 1 124 ? 7.123   11.278  -25.499 1   19.05 ? 109 VAL   A CA  1 
ATOM   859  C  C   . VAL   A 1 124 ? 7.009   12.351  -24.396 1   18.29 ? 109 VAL   A C   1 
ATOM   860  O  O   . VAL   A 1 124 ? 6.07    12.229  -23.59  1   19.01 ? 109 VAL   A O   1 
ATOM   861  C  CB  . VAL   A 1 124 ? 8.347   10.333  -25.33  1   20.83 ? 109 VAL   A CB  1 
ATOM   862  C  CG1 . VAL   A 1 124 ? 8.602   10.002  -23.854 1   22.29 ? 109 VAL   A CG1 1 
ATOM   863  C  CG2 . VAL   A 1 124 ? 8.149   9.067   -26.156 1   20.46 ? 109 VAL   A CG2 1 
ATOM   864  N  N   . PRO   A 1 125 ? 7.868   13.405  -24.323 1   17.71 ? 110 PRO   A N   1 
ATOM   865  C  CA  . PRO   A 1 125 ? 7.681   14.403  -23.262 1   17.43 ? 110 PRO   A CA  1 
ATOM   866  C  C   . PRO   A 1 125 ? 6.343   15.15   -23.366 1   18.07 ? 110 PRO   A C   1 
ATOM   867  O  O   . PRO   A 1 125 ? 5.728   15.486  -22.335 1   18.01 ? 110 PRO   A O   1 
ATOM   868  C  CB  . PRO   A 1 125 ? 8.869   15.369  -23.423 1   17.45 ? 110 PRO   A CB  1 
ATOM   869  C  CG  . PRO   A 1 125 ? 9.419   15.14   -24.8   1   18.4  ? 110 PRO   A CG  1 
ATOM   870  C  CD  . PRO   A 1 125 ? 9.054   13.711  -25.159 1   17    ? 110 PRO   A CD  1 
ATOM   871  N  N   . TYR   A 1 126 ? 5.864   15.363  -24.599 1   17.6  ? 111 TYR   A N   1 
ATOM   872  C  CA  . TYR   A 1 126 ? 4.588   16.063  -24.796 1   17.43 ? 111 TYR   A CA  1 
ATOM   873  C  C   . TYR   A 1 126 ? 3.441   15.233  -24.209 1   17.88 ? 111 TYR   A C   1 
ATOM   874  O  O   . TYR   A 1 126 ? 2.628   15.759  -23.449 1   17.22 ? 111 TYR   A O   1 
ATOM   875  C  CB  . TYR   A 1 126 ? 4.358   16.298  -26.279 1   17.09 ? 111 TYR   A CB  1 
ATOM   876  C  CG  . TYR   A 1 126 ? 3.206   17.218  -26.627 1   16.5  ? 111 TYR   A CG  1 
ATOM   877  C  CD1 . TYR   A 1 126 ? 2.724   18.153  -25.71  1   16.77 ? 111 TYR   A CD1 1 
ATOM   878  C  CD2 . TYR   A 1 126 ? 2.626   17.183  -27.881 1   17.28 ? 111 TYR   A CD2 1 
ATOM   879  C  CE1 . TYR   A 1 126 ? 1.688   19.031  -26.048 1   16.07 ? 111 TYR   A CE1 1 
ATOM   880  C  CE2 . TYR   A 1 126 ? 1.625   18.077  -28.242 1   17.58 ? 111 TYR   A CE2 1 
ATOM   881  C  CZ  . TYR   A 1 126 ? 1.108   18.947  -27.304 1   17.02 ? 111 TYR   A CZ  1 
ATOM   882  O  OH  . TYR   A 1 126 ? 0.107   19.787  -27.708 1   15.55 ? 111 TYR   A OH  1 
ATOM   883  N  N   . CYS   A 1 127 ? 3.393   13.933  -24.534 1   18.67 ? 112 CYS   A N   1 
ATOM   884  C  CA  . CYS   A 1 127 ? 2.359   13.067  -24.005 1   20    ? 112 CYS   A CA  1 
ATOM   885  C  C   . CYS   A 1 127 ? 2.482   12.906  -22.507 1   21.63 ? 112 CYS   A C   1 
ATOM   886  O  O   . CYS   A 1 127 ? 1.453   12.877  -21.822 1   22.05 ? 112 CYS   A O   1 
ATOM   887  C  CB  . CYS   A 1 127 ? 2.375   11.719  -24.705 1   19.86 ? 112 CYS   A CB  1 
ATOM   888  S  SG  . CYS   A 1 127 ? 1.749   11.755  -26.391 1   21.94 ? 112 CYS   A SG  1 
ATOM   889  N  N   . GLN   A 1 128 ? 3.732   12.831  -21.967 1   21.36 ? 113 GLN   A N   1 
ATOM   890  C  CA  . GLN   A 1 128 ? 3.903   12.681  -20.521 1   20.85 ? 113 GLN   A CA  1 
ATOM   891  C  C   . GLN   A 1 128 ? 3.364   13.9    -19.786 1   21.57 ? 113 GLN   A C   1 
ATOM   892  O  O   . GLN   A 1 128 ? 2.633   13.768  -18.807 1   21.34 ? 113 GLN   A O   1 
ATOM   893  C  CB  . GLN   A 1 128 ? 5.376   12.428  -20.158 1   21.66 ? 113 GLN   A CB  1 
ATOM   894  C  CG  . GLN   A 1 128 ? 5.847   11.024  -20.586 1   25.29 ? 113 GLN   A CG  1 
ATOM   895  C  CD  . GLN   A 1 128 ? 7.343   10.864  -20.471 1   31.33 ? 113 GLN   A CD  1 
ATOM   896  O  OE1 . GLN   A 1 128 ? 8.109   11.851  -20.471 1   33.75 ? 113 GLN   A OE1 1 
ATOM   897  N  NE2 . GLN   A 1 128 ? 7.788   9.607   -20.387 1   29.13 ? 113 GLN   A NE2 1 
ATOM   898  N  N   . LEU   A 1 129 ? 3.711   15.079  -20.281 1   21.57 ? 114 LEU   A N   1 
ATOM   899  C  CA  . LEU   A 1 129 ? 3.276   16.337  -19.695 1   22.12 ? 114 LEU   A CA  1 
ATOM   900  C  C   . LEU   A 1 129 ? 1.73    16.499  -19.849 1   20.12 ? 114 LEU   A C   1 
ATOM   901  O  O   . LEU   A 1 129 ? 1.043   16.936  -18.93  1   20.14 ? 114 LEU   A O   1 
ATOM   902  C  CB  . LEU   A 1 129 ? 4.015   17.465  -20.426 1   23.11 ? 114 LEU   A CB  1 
ATOM   903  C  CG  . LEU   A 1 129 ? 3.797   18.844  -19.89  1   27.94 ? 114 LEU   A CG  1 
ATOM   904  C  CD1 . LEU   A 1 129 ? 4.296   18.938  -18.44  1   29.62 ? 114 LEU   A CD1 1 
ATOM   905  C  CD2 . LEU   A 1 129 ? 4.545   19.867  -20.754 1   29.58 ? 114 LEU   A CD2 1 
ATOM   906  N  N   . SER   A 1 130 ? 1.195   16.14   -21.007 1   19.09 ? 115 SER   A N   1 
ATOM   907  C  CA  . SER   A 1 130 ? -0.249  16.214  -21.268 1   18.82 ? 115 SER   A CA  1 
ATOM   908  C  C   . SER   A 1 130 ? -1.001  15.268  -20.295 1   19.33 ? 115 SER   A C   1 
ATOM   909  O  O   . SER   A 1 130 ? -1.965  15.696  -19.659 1   18.32 ? 115 SER   A O   1 
ATOM   910  C  CB  . SER   A 1 130 ? -0.542  15.851  -22.717 1   17.32 ? 115 SER   A CB  1 
ATOM   911  O  OG  . SER   A 1 130 ? 0.065   16.847  -23.535 1   18.84 ? 115 SER   A OG  1 
ATOM   912  N  N   . LYS   A 1 131 ? -0.481  14.042  -20.075 1   20.22 ? 116 LYS   A N   1 
ATOM   913  C  CA  . LYS   A 1 131 ? -1.101  13.11   -19.133 1   22.71 ? 116 LYS   A CA  1 
ATOM   914  C  C   . LYS   A 1 131 ? -1.127  13.699  -17.721 1   23.42 ? 116 LYS   A C   1 
ATOM   915  O  O   . LYS   A 1 131 ? -2.152  13.645  -17.045 1   24.39 ? 116 LYS   A O   1 
ATOM   916  C  CB  . LYS   A 1 131 ? -0.353  11.755  -19.131 1   26.86 ? 116 LYS   A CB  1 
ATOM   917  C  CG  . LYS   A 1 131 ? -0.922  10.74   -18.12  1   33.26 ? 116 LYS   A CG  1 
ATOM   918  C  CD  . LYS   A 1 131 ? -0.074  9.449   -18.091 1   37.78 ? 116 LYS   A CD  1 
ATOM   919  C  CE  . LYS   A 1 131 ? -0.766  8.334   -17.347 1   42.38 ? 116 LYS   A CE  1 
ATOM   920  N  N   . LYS   A 1 132 ? -0.018  14.298  -17.308 1   23.64 ? 117 LYS   A N   1 
ATOM   921  C  CA  . LYS   A 1 132 ? 0.143   14.945  -16.016 1   24.28 ? 117 LYS   A CA  1 
ATOM   922  C  C   . LYS   A 1 132 ? -0.895  16.078  -15.794 1   23.7  ? 117 LYS   A C   1 
ATOM   923  O  O   . LYS   A 1 132 ? -1.5    16.187  -14.713 1   23.21 ? 117 LYS   A O   1 
ATOM   924  C  CB  . LYS   A 1 132 ? 1.573   15.489  -15.93  1   27.56 ? 117 LYS   A CB  1 
ATOM   925  C  CG  . LYS   A 1 132 ? 1.946   16.135  -14.617 1   34.74 ? 117 LYS   A CG  1 
ATOM   926  C  CD  . LYS   A 1 132 ? 3.463   16.362  -14.581 1   41.36 ? 117 LYS   A CD  1 
ATOM   927  C  CE  . LYS   A 1 132 ? 4.066   16.236  -13.198 1   46.61 ? 117 LYS   A CE  1 
ATOM   928  N  NZ  . LYS   A 1 132 ? 5.534   15.95   -13.268 1   49.89 ? 117 LYS   A NZ  1 
ATOM   929  N  N   . LEU   A 1 133 ? -1.093  16.921  -16.813 1   22.63 ? 118 LEU   A N   1 
ATOM   930  C  CA  . LEU   A 1 133 ? -2.047  18.032  -16.713 1   22.7  ? 118 LEU   A CA  1 
ATOM   931  C  C   . LEU   A 1 133 ? -3.492  17.657  -17.097 1   22.27 ? 118 LEU   A C   1 
ATOM   932  O  O   . LEU   A 1 133 ? -4.353  18.547  -17.093 1   23.03 ? 118 LEU   A O   1 
ATOM   933  C  CB  . LEU   A 1 133 ? -1.578  19.214  -17.594 1   22.97 ? 118 LEU   A CB  1 
ATOM   934  C  CG  . LEU   A 1 133 ? -0.223  19.839  -17.207 1   26.41 ? 118 LEU   A CG  1 
ATOM   935  C  CD1 . LEU   A 1 133 ? 0.179   20.917  -18.161 1   26.77 ? 118 LEU   A CD1 1 
ATOM   936  C  CD2 . LEU   A 1 133 ? -0.248  20.405  -15.825 1   28.12 ? 118 LEU   A CD2 1 
ATOM   937  N  N   . GLU   A 1 134 ? -3.753  16.368  -17.449 1   20.37 ? 119 GLU   A N   1 
ATOM   938  C  CA  . GLU   A 1 134 ? -5.062  15.847  -17.878 1   20.59 ? 119 GLU   A CA  1 
ATOM   939  C  C   . GLU   A 1 134 ? -5.621  16.609  -19.071 1   20.81 ? 119 GLU   A C   1 
ATOM   940  O  O   . GLU   A 1 134 ? -6.801  16.984  -19.114 1   21.26 ? 119 GLU   A O   1 
ATOM   941  C  CB  . GLU   A 1 134 ? -6.094  15.845  -16.733 1   23.17 ? 119 GLU   A CB  1 
ATOM   942  C  CG  . GLU   A 1 134 ? -5.65   15.095  -15.506 1   30.72 ? 119 GLU   A CG  1 
ATOM   943  C  CD  . GLU   A 1 134 ? -6.768  15.062  -14.478 1   36.38 ? 119 GLU   A CD  1 
ATOM   944  O  OE1 . GLU   A 1 134 ? -7.893  14.638  -14.828 1   35.8  ? 119 GLU   A OE1 1 
ATOM   945  O  OE2 . GLU   A 1 134 ? -6.521  15.495  -13.331 1   40.7  ? 119 GLU   A OE2 1 
ATOM   946  N  N   . LEU   A 1 135 ? -4.765  16.88   -20.029 1   19.77 ? 120 LEU   A N   1 
ATOM   947  C  CA  . LEU   A 1 135 ? -5.135  17.581  -21.242 1   19.24 ? 120 LEU   A CA  1 
ATOM   948  C  C   . LEU   A 1 135 ? -4.6    16.726  -22.408 1   19.11 ? 120 LEU   A C   1 
ATOM   949  O  O   . LEU   A 1 135 ? -3.624  15.992  -22.242 1   18.45 ? 120 LEU   A O   1 
ATOM   950  C  CB  . LEU   A 1 135 ? -4.469  18.966  -21.266 1   18.74 ? 120 LEU   A CB  1 
ATOM   951  C  CG  . LEU   A 1 135 ? -5.164  20.074  -20.429 1   19.51 ? 120 LEU   A CG  1 
ATOM   952  C  CD1 . LEU   A 1 135 ? -4.284  21.329  -20.361 1   20.34 ? 120 LEU   A CD1 1 
ATOM   953  C  CD2 . LEU   A 1 135 ? -6.505  20.442  -21.042 1   18.75 ? 120 LEU   A CD2 1 
ATOM   954  N  N   . PRO   A 1 136 ? -5.27   16.784  -23.555 1   18.07 ? 121 PRO   A N   1 
ATOM   955  C  CA  . PRO   A 1 136 ? -4.807  16.012  -24.692 1   18.71 ? 121 PRO   A CA  1 
ATOM   956  C  C   . PRO   A 1 136 ? -3.511  16.581  -25.291 1   18.56 ? 121 PRO   A C   1 
ATOM   957  O  O   . PRO   A 1 136 ? -3.244  17.795  -25.142 1   16.78 ? 121 PRO   A O   1 
ATOM   958  C  CB  . PRO   A 1 136 ? -5.978  16.148  -25.68  1   19.76 ? 121 PRO   A CB  1 
ATOM   959  C  CG  . PRO   A 1 136 ? -6.538  17.517  -25.37  1   20.28 ? 121 PRO   A CG  1 
ATOM   960  C  CD  . PRO   A 1 136 ? -6.46   17.595  -23.889 1   18.09 ? 121 PRO   A CD  1 
ATOM   961  N  N   . PRO   A 1 137 ? -2.723  15.703  -25.958 1   18.63 ? 122 PRO   A N   1 
ATOM   962  C  CA  . PRO   A 1 137 ? -1.473  16.136  -26.587 1   18.76 ? 122 PRO   A CA  1 
ATOM   963  C  C   . PRO   A 1 137 ? -1.686  16.839  -27.93  1   17.68 ? 122 PRO   A C   1 
ATOM   964  O  O   . PRO   A 1 137 ? -1.237  16.394  -29.006 1   17.52 ? 122 PRO   A O   1 
ATOM   965  C  CB  . PRO   A 1 137 ? -0.677  14.825  -26.728 1   19.49 ? 122 PRO   A CB  1 
ATOM   966  C  CG  . PRO   A 1 137 ? -1.725  13.807  -26.985 1   19.26 ? 122 PRO   A CG  1 
ATOM   967  C  CD  . PRO   A 1 137 ? -2.937  14.246  -26.143 1   19.11 ? 122 PRO   A CD  1 
ATOM   968  N  N   . ILE   A 1 138 ? -2.373  17.973  -27.857 1   15.94 ? 123 ILE   A N   1 
ATOM   969  C  CA  . ILE   A 1 138 ? -2.62   18.834  -28.999 1   14.86 ? 123 ILE   A CA  1 
ATOM   970  C  C   . ILE   A 1 138 ? -2.825  20.245  -28.4   1   14.2  ? 123 ILE   A C   1 
ATOM   971  O  O   . ILE   A 1 138 ? -3.247  20.385  -27.246 1   13.77 ? 123 ILE   A O   1 
ATOM   972  C  CB  . ILE   A 1 138 ? -3.832  18.377  -29.859 1   14.24 ? 123 ILE   A CB  1 
ATOM   973  C  CG1 . ILE   A 1 138 ? -3.895  19.185  -31.167 1   14.77 ? 123 ILE   A CG1 1 
ATOM   974  C  CG2 . ILE   A 1 138 ? -5.197  18.51   -29.07  1   15.07 ? 123 ILE   A CG2 1 
ATOM   975  C  CD1 . ILE   A 1 138 ? -4.867  18.592  -32.253 1   15.22 ? 123 ILE   A CD1 1 
ATOM   976  N  N   . LEU   A 1 139 ? -2.468  21.277  -29.153 1   13.84 ? 124 LEU   A N   1 
ATOM   977  C  CA  . LEU   A 1 139 ? -2.692  22.649  -28.722 1   15.81 ? 124 LEU   A CA  1 
ATOM   978  C  C   . LEU   A 1 139 ? -4.203  22.9    -28.445 1   16.11 ? 124 LEU   A C   1 
ATOM   979  O  O   . LEU   A 1 139 ? -5.072  22.614  -29.296 1   15.48 ? 124 LEU   A O   1 
ATOM   980  C  CB  . LEU   A 1 139 ? -2.194  23.581  -29.834 1   17.34 ? 124 LEU   A CB  1 
ATOM   981  C  CG  . LEU   A 1 139 ? -1.826  24.983  -29.44  1   20.46 ? 124 LEU   A CG  1 
ATOM   982  C  CD1 . LEU   A 1 139 ? -0.677  24.987  -28.398 1   18.16 ? 124 LEU   A CD1 1 
ATOM   983  C  CD2 . LEU   A 1 139 ? -1.442  25.807  -30.703 1   21.83 ? 124 LEU   A CD2 1 
ATOM   984  N  N   . VAL   A 1 140 ? -4.514  23.367  -27.224 1   14.98 ? 125 VAL   A N   1 
ATOM   985  C  CA  . VAL   A 1 140 ? -5.89   23.696  -26.854 1   14.79 ? 125 VAL   A CA  1 
ATOM   986  C  C   . VAL   A 1 140 ? -6.005  25.215  -26.614 1   15.05 ? 125 VAL   A C   1 
ATOM   987  O  O   . VAL   A 1 140 ? -4.983  25.921  -26.496 1   14.66 ? 125 VAL   A O   1 
ATOM   988  C  CB  . VAL   A 1 140 ? -6.401  22.868  -25.626 1   15.03 ? 125 VAL   A CB  1 
ATOM   989  C  CG1 . VAL   A 1 140 ? -6.28   21.354  -25.913 1   15.98 ? 125 VAL   A CG1 1 
ATOM   990  C  CG2 . VAL   A 1 140 ? -5.616  23.233  -24.365 1   14.79 ? 125 VAL   A CG2 1 
ATOM   991  N  N   . TYR   A 1 141 ? -7.235  25.719  -26.528 1   15.61 ? 126 TYR   A N   1 
ATOM   992  C  CA  . TYR   A 1 141 ? -7.55   27.132  -26.215 1   15.18 ? 126 TYR   A CA  1 
ATOM   993  C  C   . TYR   A 1 141 ? -6.799  27.566  -24.914 1   15.12 ? 126 TYR   A C   1 
ATOM   994  O  O   . TYR   A 1 141 ? -6.238  28.647  -24.877 1   15.66 ? 126 TYR   A O   1 
ATOM   995  C  CB  . TYR   A 1 141 ? -9.044  27.248  -26.028 1   14.57 ? 126 TYR   A CB  1 
ATOM   996  C  CG  . TYR   A 1 141 ? -9.559  28.644  -25.749 1   15.6  ? 126 TYR   A CG  1 
ATOM   997  C  CD1 . TYR   A 1 141 ? -9.778  29.545  -26.784 1   17.1  ? 126 TYR   A CD1 1 
ATOM   998  C  CD2 . TYR   A 1 141 ? -9.976  29.008  -24.477 1   16.79 ? 126 TYR   A CD2 1 
ATOM   999  C  CE1 . TYR   A 1 141 ? -10.292 30.817  -26.541 1   16.58 ? 126 TYR   A CE1 1 
ATOM   1000 C  CE2 . TYR   A 1 141 ? -10.526 30.272  -24.227 1   16.96 ? 126 TYR   A CE2 1 
ATOM   1001 C  CZ  . TYR   A 1 141 ? -10.678 31.171  -25.263 1   17.41 ? 126 TYR   A CZ  1 
ATOM   1002 O  OH  . TYR   A 1 141 ? -11.245 32.411  -25.019 1   17.44 ? 126 TYR   A OH  1 
ATOM   1003 N  N   . ALA   A 1 142 ? -6.759  26.714  -23.887 1   14.43 ? 127 ALA   A N   1 
ATOM   1004 C  CA  . ALA   A 1 142 ? -5.994  27.039  -22.64  1   15.56 ? 127 ALA   A CA  1 
ATOM   1005 C  C   . ALA   A 1 142 ? -4.485  27.233  -22.861 1   15.62 ? 127 ALA   A C   1 
ATOM   1006 O  O   . ALA   A 1 142 ? -3.809  27.876  -22.052 1   17.65 ? 127 ALA   A O   1 
ATOM   1007 C  CB  . ALA   A 1 142 ? -6.253  25.989  -21.545 1   15.55 ? 127 ALA   A CB  1 
ATOM   1008 N  N   . ASP   A 1 143 ? -3.93   26.649  -23.926 1   14.19 ? 128 ASP   A N   1 
ATOM   1009 C  CA  . ASP   A 1 143 ? -2.539  26.881  -24.267 1   14.11 ? 128 ASP   A CA  1 
ATOM   1010 C  C   . ASP   A 1 143 ? -2.398  28.182  -25.062 1   14.85 ? 128 ASP   A C   1 
ATOM   1011 O  O   . ASP   A 1 143 ? -1.739  29.109  -24.579 1   15.25 ? 128 ASP   A O   1 
ATOM   1012 C  CB  . ASP   A 1 143 ? -1.957  25.742  -25.094 1   15.26 ? 128 ASP   A CB  1 
ATOM   1013 C  CG  . ASP   A 1 143 ? -2.053  24.366  -24.47  1   17.96 ? 128 ASP   A CG  1 
ATOM   1014 O  OD1 . ASP   A 1 143 ? -1.73   24.231  -23.259 1   17.83 ? 128 ASP   A OD1 1 
ATOM   1015 O  OD2 . ASP   A 1 143 ? -2.398  23.432  -25.193 1   18.02 ? 128 ASP   A OD2 1 
ATOM   1016 N  N   . CYS   A 1 144 ? -2.942  28.232  -26.291 1   13.92 ? 129 CYS   A N   1 
ATOM   1017 C  CA  . CYS   A 1 144 ? -2.607  29.311  -27.195 1   16.42 ? 129 CYS   A CA  1 
ATOM   1018 C  C   . CYS   A 1 144 ? -3.356  30.606  -26.952 1   15.95 ? 129 CYS   A C   1 
ATOM   1019 O  O   . CYS   A 1 144 ? -2.924  31.618  -27.505 1   15.26 ? 129 CYS   A O   1 
ATOM   1020 C  CB  . CYS   A 1 144 ? -2.703  28.874  -28.647 1   18.79 ? 129 CYS   A CB  1 
ATOM   1021 S  SG  . CYS   A 1 144 ? -4.339  28.3    -29.116 1   22.26 ? 129 CYS   A SG  1 
ATOM   1022 N  N   . VAL   A 1 145 ? -4.339  30.623  -26.05  1   15.61 ? 130 VAL   A N   1 
ATOM   1023 C  CA  . VAL   A 1 145 ? -5      31.865  -25.672 1   17.01 ? 130 VAL   A CA  1 
ATOM   1024 C  C   . VAL   A 1 145 ? -4.723  32.141  -24.181 1   17.65 ? 130 VAL   A C   1 
ATOM   1025 O  O   . VAL   A 1 145 ? -4.14   33.175  -23.833 1   17.15 ? 130 VAL   A O   1 
ATOM   1026 C  CB  . VAL   A 1 145 ? -6.517  31.872  -26.003 1   17.74 ? 130 VAL   A CB  1 
ATOM   1027 C  CG1 . VAL   A 1 145 ? -7.205  33.157  -25.463 1   18.02 ? 130 VAL   A CG1 1 
ATOM   1028 C  CG2 . VAL   A 1 145 ? -6.766  31.706  -27.522 1   18.34 ? 130 VAL   A CG2 1 
ATOM   1029 N  N   . LEU   A 1 146 ? -5.168  31.227  -23.297 1   16.99 ? 131 LEU   A N   1 
ATOM   1030 C  CA  . LEU   A 1 146 ? -5.102  31.486  -21.86  1   16.91 ? 131 LEU   A CA  1 
ATOM   1031 C  C   . LEU   A 1 146 ? -3.701  31.534  -21.229 1   16.8  ? 131 LEU   A C   1 
ATOM   1032 O  O   . LEU   A 1 146 ? -3.57   32.162  -20.183 1   16.64 ? 131 LEU   A O   1 
ATOM   1033 C  CB  . LEU   A 1 146 ? -5.972  30.461  -21.103 1   17.07 ? 131 LEU   A CB  1 
ATOM   1034 C  CG  . LEU   A 1 146 ? -7.432  30.339  -21.595 1   17.43 ? 131 LEU   A CG  1 
ATOM   1035 C  CD1 . LEU   A 1 146 ? -8.204  29.382  -20.729 1   17.73 ? 131 LEU   A CD1 1 
ATOM   1036 C  CD2 . LEU   A 1 146 ? -8.159  31.714  -21.549 1   19.22 ? 131 LEU   A CD2 1 
ATOM   1037 N  N   . ALA   A 1 147 ? -2.681  30.862  -21.803 1   16.69 ? 132 ALA   A N   1 
ATOM   1038 C  CA  . ALA   A 1 147 ? -1.318  30.846  -21.223 1   17.37 ? 132 ALA   A CA  1 
ATOM   1039 C  C   . ALA   A 1 147 ? -0.279  31.519  -22.182 1   17.1  ? 132 ALA   A C   1 
ATOM   1040 O  O   . ALA   A 1 147 ? 0.92    31.524  -21.893 1   17.75 ? 132 ALA   A O   1 
ATOM   1041 C  CB  . ALA   A 1 147 ? -0.886  29.395  -20.974 1   17.02 ? 132 ALA   A CB  1 
ATOM   1042 N  N   . ASN   A 1 148 ? -0.73   32.046  -23.32  1   17.63 ? 133 ASN   A N   1 
ATOM   1043 C  CA  . ASN   A 1 148 ? 0.146   32.551  -24.375 1   17.62 ? 133 ASN   A CA  1 
ATOM   1044 C  C   . ASN   A 1 148 ? 0.147   34.077  -24.383 1   18.64 ? 133 ASN   A C   1 
ATOM   1045 O  O   . ASN   A 1 148 ? -0.13   34.707  -25.415 1   18.82 ? 133 ASN   A O   1 
ATOM   1046 C  CB  . ASN   A 1 148 ? -0.345  31.993  -25.721 1   16.81 ? 133 ASN   A CB  1 
ATOM   1047 C  CG  . ASN   A 1 148 ? 0.563   32.276  -26.907 1   17.92 ? 133 ASN   A CG  1 
ATOM   1048 O  OD1 . ASN   A 1 148 ? 1.748   32.575  -26.747 1   18.35 ? 133 ASN   A OD1 1 
ATOM   1049 N  ND2 . ASN   A 1 148 ? 0.022   32.162  -28.123 1   15.99 ? 133 ASN   A ND2 1 
ATOM   1050 N  N   . TRP   A 1 149 ? 0.465   34.672  -23.224 1   17.77 ? 134 TRP   A N   1 
ATOM   1051 C  CA  . TRP   A 1 149 ? 0.433   36.116  -23.119 1   18.58 ? 134 TRP   A CA  1 
ATOM   1052 C  C   . TRP   A 1 149 ? 1.372   36.632  -22.04  1   19.25 ? 134 TRP   A C   1 
ATOM   1053 O  O   . TRP   A 1 149 ? 1.782   35.893  -21.151 1   17.52 ? 134 TRP   A O   1 
ATOM   1054 C  CB  . TRP   A 1 149 ? -1.006  36.615  -22.862 1   19    ? 134 TRP   A CB  1 
ATOM   1055 C  CG  . TRP   A 1 149 ? -1.569  36.252  -21.522 1   19.33 ? 134 TRP   A CG  1 
ATOM   1056 C  CD1 . TRP   A 1 149 ? -2.186  35.085  -21.173 1   19.93 ? 134 TRP   A CD1 1 
ATOM   1057 C  CD2 . TRP   A 1 149 ? -1.567  37.07   -20.349 1   20.05 ? 134 TRP   A CD2 1 
ATOM   1058 N  NE1 . TRP   A 1 149 ? -2.641  35.161  -19.873 1   20    ? 134 TRP   A NE1 1 
ATOM   1059 C  CE2 . TRP   A 1 149 ? -2.257  36.362  -19.339 1   20.87 ? 134 TRP   A CE2 1 
ATOM   1060 C  CE3 . TRP   A 1 149 ? -1.089  38.359  -20.063 1   21.02 ? 134 TRP   A CE3 1 
ATOM   1061 C  CZ2 . TRP   A 1 149 ? -2.465  36.897  -18.064 1   22.17 ? 134 TRP   A CZ2 1 
ATOM   1062 C  CZ3 . TRP   A 1 149 ? -1.305  38.885  -18.812 1   22.29 ? 134 TRP   A CZ3 1 
ATOM   1063 C  CH2 . TRP   A 1 149 ? -1.956  38.147  -17.818 1   22.73 ? 134 TRP   A CH2 1 
ATOM   1064 N  N   . LYS   A 1 150 ? 1.662   37.937  -22.111 1   21.14 ? 135 LYS   A N   1 
ATOM   1065 C  CA  . LYS   A 1 150 ? 2.474   38.643  -21.144 1   22.62 ? 135 LYS   A CA  1 
ATOM   1066 C  C   . LYS   A 1 150 ? 2.075   40.121  -21.13  1   24.74 ? 135 LYS   A C   1 
ATOM   1067 O  O   . LYS   A 1 150 ? 1.473   40.645  -22.088 1   24.29 ? 135 LYS   A O   1 
ATOM   1068 C  CB  . LYS   A 1 150 ? 3.98    38.522  -21.48  1   24.43 ? 135 LYS   A CB  1 
ATOM   1069 C  CG  . LYS   A 1 150 ? 4.382   39.204  -22.801 1   30.68 ? 135 LYS   A CG  1 
ATOM   1070 C  CD  . LYS   A 1 150 ? 5.862   39.016  -23.149 1   37.42 ? 135 LYS   A CD  1 
ATOM   1071 C  CE  . LYS   A 1 150 ? 6.096   39.224  -24.636 1   44.67 ? 135 LYS   A CE  1 
ATOM   1072 N  NZ  . LYS   A 1 150 ? 7.066   38.243  -25.241 1   48.97 ? 135 LYS   A NZ  1 
ATOM   1073 N  N   . LYS   A 1 151 ? 2.403   40.792  -20.031 1   26.12 ? 136 LYS   A N   1 
ATOM   1074 C  CA  . LYS   A 1 151 ? 2.284   42.243  -19.973 1   27.67 ? 136 LYS   A CA  1 
ATOM   1075 C  C   . LYS   A 1 151 ? 3.664   42.751  -20.422 1   29.6  ? 136 LYS   A C   1 
ATOM   1076 O  O   . LYS   A 1 151 ? 4.694   42.183  -20.034 1   30.23 ? 136 LYS   A O   1 
ATOM   1077 C  CB  . LYS   A 1 151 ? 2.062   42.725  -18.539 1   28.98 ? 136 LYS   A CB  1 
ATOM   1078 C  CG  . LYS   A 1 151 ? 0.624   42.744  -18.065 1   29.85 ? 136 LYS   A CG  1 
ATOM   1079 C  CD  . LYS   A 1 151 ? 0.548   43.419  -16.721 1   33.17 ? 136 LYS   A CD  1 
ATOM   1080 C  CE  . LYS   A 1 151 ? -0.858  43.503  -16.203 1   37.88 ? 136 LYS   A CE  1 
ATOM   1081 N  NZ  . LYS   A 1 151 ? -0.958  44.441  -15.048 1   39.59 ? 136 LYS   A NZ  1 
ATOM   1082 N  N   . LYS   A 1 152 ? 3.693   43.801  -21.231 1   30.82 ? 137 LYS   A N   1 
ATOM   1083 C  CA  . LYS   A 1 152 ? 4.954   44.437  -21.629 1   32.42 ? 137 LYS   A CA  1 
ATOM   1084 C  C   . LYS   A 1 152 ? 5.514   45.176  -20.38  1   34.71 ? 137 LYS   A C   1 
ATOM   1085 O  O   . LYS   A 1 152 ? 6.691   45.051  -20.056 1   35.65 ? 137 LYS   A O   1 
ATOM   1086 C  CB  . LYS   A 1 152 ? 4.712   45.437  -22.767 1   32.14 ? 137 LYS   A CB  1 
ATOM   1087 C  CG  . LYS   A 1 152 ? 4.361   44.798  -24.098 1   33.09 ? 137 LYS   A CG  1 
ATOM   1088 C  CD  . LYS   A 1 152 ? 3.968   45.876  -25.078 1   35.12 ? 137 LYS   A CD  1 
ATOM   1089 C  CE  . LYS   A 1 152 ? 3.668   45.331  -26.439 1   37.49 ? 137 LYS   A CE  1 
ATOM   1090 N  NZ  . LYS   A 1 152 ? 2.974   46.345  -27.267 1   40.55 ? 137 LYS   A NZ  1 
ATOM   1091 N  N   . ASP   A 1 153 ? 4.639   45.866  -19.646 1   35.32 ? 138 ASP   A N   1 
ATOM   1092 C  CA  . ASP   A 1 153 ? 4.968   46.594  -18.429 1   36.19 ? 138 ASP   A CA  1 
ATOM   1093 C  C   . ASP   A 1 153 ? 4.042   46.108  -17.299 1   37.16 ? 138 ASP   A C   1 
ATOM   1094 O  O   . ASP   A 1 153 ? 2.846   46.404  -17.3   1   36.38 ? 138 ASP   A O   1 
ATOM   1095 C  CB  . ASP   A 1 153 ? 4.778   48.103  -18.654 1   36.99 ? 138 ASP   A CB  1 
ATOM   1096 C  CG  . ASP   A 1 153 ? 5.267   48.982  -17.51  1   41.3  ? 138 ASP   A CG  1 
ATOM   1097 O  OD1 . ASP   A 1 153 ? 5.582   48.437  -16.431 1   42.06 ? 138 ASP   A OD1 1 
ATOM   1098 O  OD2 . ASP   A 1 153 ? 5.325   50.212  -17.694 1   43.42 ? 138 ASP   A OD2 1 
ATOM   1099 N  N   . PRO   A 1 154 ? 4.609   45.41   -16.299 1   38.83 ? 139 PRO   A N   1 
ATOM   1100 C  CA  . PRO   A 1 154 ? 3.785   44.891  -15.192 1   39.69 ? 139 PRO   A CA  1 
ATOM   1101 C  C   . PRO   A 1 154 ? 3.044   45.942  -14.367 1   40.29 ? 139 PRO   A C   1 
ATOM   1102 O  O   . PRO   A 1 154 ? 2.043   45.624  -13.725 1   40.36 ? 139 PRO   A O   1 
ATOM   1103 C  CB  . PRO   A 1 154 ? 4.784   44.117  -14.326 1   40.87 ? 139 PRO   A CB  1 
ATOM   1104 C  CG  . PRO   A 1 154 ? 5.974   43.879  -15.192 1   41.47 ? 139 PRO   A CG  1 
ATOM   1105 C  CD  . PRO   A 1 154 ? 6.025   45.018  -16.164 1   39.22 ? 139 PRO   A CD  1 
ATOM   1106 N  N   . ASN   A 1 155 ? 3.519   47.193  -14.388 1   40.41 ? 140 ASN   A N   1 
ATOM   1107 C  CA  . ASN   A 1 155 ? 2.865   48.266  -13.635 1   40.59 ? 140 ASN   A CA  1 
ATOM   1108 C  C   . ASN   A 1 155 ? 1.713   48.935  -14.397 1   39.47 ? 140 ASN   A C   1 
ATOM   1109 O  O   . ASN   A 1 155 ? 1.043   49.81   -13.85  1   39.92 ? 140 ASN   A O   1 
ATOM   1110 C  CB  . ASN   A 1 155 ? 3.896   49.291  -13.153 1   43.19 ? 140 ASN   A CB  1 
ATOM   1111 C  CG  . ASN   A 1 155 ? 5.03    48.651  -12.374 1   48.18 ? 140 ASN   A CG  1 
ATOM   1112 O  OD1 . ASN   A 1 155 ? 4.81    47.967  -11.366 1   50.34 ? 140 ASN   A OD1 1 
ATOM   1113 N  ND2 . ASN   A 1 155 ? 6.263   48.833  -12.84  1   49    ? 140 ASN   A ND2 1 
ATOM   1114 N  N   . LYS   A 1 156 ? 1.445   48.499  -15.633 1   37.73 ? 141 LYS   A N   1 
ATOM   1115 C  CA  . LYS   A 1 156 ? 0.362   49.03   -16.453 1   36.34 ? 141 LYS   A CA  1 
ATOM   1116 C  C   . LYS   A 1 156 ? -0.779  47.987  -16.6   1   35.51 ? 141 LYS   A C   1 
ATOM   1117 O  O   . LYS   A 1 156 ? -0.544  46.785  -16.436 1   34.47 ? 141 LYS   A O   1 
ATOM   1118 C  CB  . LYS   A 1 156 ? 0.921   49.491  -17.812 1   37.36 ? 141 LYS   A CB  1 
ATOM   1119 C  CG  . LYS   A 1 156 ? 1.795   50.727  -17.671 1   40.73 ? 141 LYS   A CG  1 
ATOM   1120 C  CD  . LYS   A 1 156 ? 2.31    51.233  -19.003 1   44.99 ? 141 LYS   A CD  1 
ATOM   1121 C  CE  . LYS   A 1 156 ? 3.039   52.553  -18.854 1   48.81 ? 141 LYS   A CE  1 
ATOM   1122 N  NZ  . LYS   A 1 156 ? 3.388   53.138  -20.175 1   50.52 ? 141 LYS   A NZ  1 
ATOM   1123 N  N   . PRO   A 1 157 ? -2.023  48.445  -16.857 1   35.15 ? 142 PRO   A N   1 
ATOM   1124 C  CA  . PRO   A 1 157 ? -3.164  47.509  -16.933 1   34.33 ? 142 PRO   A CA  1 
ATOM   1125 C  C   . PRO   A 1 157 ? -3.175  46.5    -18.099 1   32.36 ? 142 PRO   A C   1 
ATOM   1126 O  O   . PRO   A 1 157 ? -2.328  46.517  -18.99  1   31.33 ? 142 PRO   A O   1 
ATOM   1127 C  CB  . PRO   A 1 157 ? -4.375  48.448  -17.009 1   35.63 ? 142 PRO   A CB  1 
ATOM   1128 C  CG  . PRO   A 1 157 ? -3.833  49.716  -17.578 1   36.42 ? 142 PRO   A CG  1 
ATOM   1129 C  CD  . PRO   A 1 157 ? -2.469  49.846  -17.004 1   34.81 ? 142 PRO   A CD  1 
ATOM   1130 N  N   . LEU   A 1 158 ? -4.148  45.582  -18.052 1   31.43 ? 143 LEU   A N   1 
ATOM   1131 C  CA  . LEU   A 1 158 ? -4.342  44.569  -19.071 1   31.01 ? 143 LEU   A CA  1 
ATOM   1132 C  C   . LEU   A 1 158 ? -5.092  45.163  -20.267 1   29.44 ? 143 LEU   A C   1 
ATOM   1133 O  O   . LEU   A 1 158 ? -6.291  45.007  -20.388 1   29.62 ? 143 LEU   A O   1 
ATOM   1134 C  CB  . LEU   A 1 158 ? -5.136  43.407  -18.493 1   31.8  ? 143 LEU   A CB  1 
ATOM   1135 C  CG  . LEU   A 1 158 ? -4.402  42.525  -17.53  1   34.18 ? 143 LEU   A CG  1 
ATOM   1136 C  CD1 . LEU   A 1 158 ? -5.377  41.653  -16.776 1   34.68 ? 143 LEU   A CD1 1 
ATOM   1137 C  CD2 . LEU   A 1 158 ? -3.37   41.68   -18.255 1   34.89 ? 143 LEU   A CD2 1 
ATOM   1138 N  N   . THR   A 1 159 ? -4.384  45.881  -21.117 1   28.19 ? 144 THR   A N   1 
ATOM   1139 C  CA  . THR   A 1 159 ? -4.95   46.431  -22.35  1   27.85 ? 144 THR   A CA  1 
ATOM   1140 C  C   . THR   A 1 159 ? -4.131  45.862  -23.511 1   26.15 ? 144 THR   A C   1 
ATOM   1141 O  O   . THR   A 1 159 ? -2.982  45.477  -23.306 1   25.85 ? 144 THR   A O   1 
ATOM   1142 C  CB  . THR   A 1 159 ? -4.842  47.971  -22.363 1   29.87 ? 144 THR   A CB  1 
ATOM   1143 O  OG1 . THR   A 1 159 ? -3.466  48.323  -22.338 1   32.51 ? 144 THR   A OG1 1 
ATOM   1144 C  CG2 . THR   A 1 159 ? -5.525  48.614  -21.182 1   30.5  ? 144 THR   A CG2 1 
ATOM   1145 N  N   . TYR   A 1 160 ? -4.669  45.886  -24.732 1   25.39 ? 145 TYR   A N   1 
ATOM   1146 C  CA  . TYR   A 1 160 ? -3.952  45.414  -25.919 1   25.46 ? 145 TYR   A CA  1 
ATOM   1147 C  C   . TYR   A 1 160 ? -2.574  46.057  -26.073 1   26.54 ? 145 TYR   A C   1 
ATOM   1148 O  O   . TYR   A 1 160 ? -1.586  45.365  -26.324 1   25.81 ? 145 TYR   A O   1 
ATOM   1149 C  CB  . TYR   A 1 160 ? -4.801  45.658  -27.185 1   24.13 ? 145 TYR   A CB  1 
ATOM   1150 C  CG  . TYR   A 1 160 ? -4.254  44.921  -28.385 1   23.43 ? 145 TYR   A CG  1 
ATOM   1151 C  CD1 . TYR   A 1 160 ? -3.289  45.496  -29.199 1   22.76 ? 145 TYR   A CD1 1 
ATOM   1152 C  CD2 . TYR   A 1 160 ? -4.683  43.627  -28.692 1   22.99 ? 145 TYR   A CD2 1 
ATOM   1153 C  CE1 . TYR   A 1 160 ? -2.705  44.781  -30.233 1   23.18 ? 145 TYR   A CE1 1 
ATOM   1154 C  CE2 . TYR   A 1 160 ? -4.156  42.932  -29.773 1   22.28 ? 145 TYR   A CE2 1 
ATOM   1155 C  CZ  . TYR   A 1 160 ? -3.19   43.525  -30.561 1   23.34 ? 145 TYR   A CZ  1 
ATOM   1156 O  OH  . TYR   A 1 160 ? -2.675  42.835  -31.625 1   24.87 ? 145 TYR   A OH  1 
ATOM   1157 N  N   . GLU   A 1 161 ? -2.498  47.39   -25.838 1   27.11 ? 146 GLU   A N   1 
ATOM   1158 C  CA  . GLU   A 1 161 ? -1.244  48.147  -25.955 1   27.23 ? 146 GLU   A CA  1 
ATOM   1159 C  C   . GLU   A 1 161 ? -0.164  47.673  -25.005 1   26.04 ? 146 GLU   A C   1 
ATOM   1160 O  O   . GLU   A 1 161 ? 1.018   47.721  -25.332 1   26.71 ? 146 GLU   A O   1 
ATOM   1161 C  CB  . GLU   A 1 161 ? -1.509  49.65   -25.732 1   31.95 ? 146 GLU   A CB  1 
ATOM   1162 C  CG  . GLU   A 1 161 ? -1.937  50.371  -26.996 1   39    ? 146 GLU   A CG  1 
ATOM   1163 C  CD  . GLU   A 1 161 ? -3.149  49.806  -27.699 1   47.59 ? 146 GLU   A CD  1 
ATOM   1164 O  OE1 . GLU   A 1 161 ? -4.194  49.618  -27.031 1   50.53 ? 146 GLU   A OE1 1 
ATOM   1165 O  OE2 . GLU   A 1 161 ? -3.05   49.544  -28.921 1   50.14 ? 146 GLU   A OE2 1 
ATOM   1166 N  N   . ASN   A 1 162 ? -0.568  47.205  -23.83  1   24.84 ? 147 ASN   A N   1 
ATOM   1167 C  CA  . ASN   A 1 162 ? 0.387   46.718  -22.845 1   24.88 ? 147 ASN   A CA  1 
ATOM   1168 C  C   . ASN   A 1 162 ? 0.524   45.195  -22.867 1   24.95 ? 147 ASN   A C   1 
ATOM   1169 O  O   . ASN   A 1 162 ? 1.039   44.634  -21.91  1   24.68 ? 147 ASN   A O   1 
ATOM   1170 C  CB  . ASN   A 1 162 ? 0.013   47.205  -21.441 1   25.42 ? 147 ASN   A CB  1 
ATOM   1171 C  CG  . ASN   A 1 162 ? 1.122   46.95   -20.461 1   27.93 ? 147 ASN   A CG  1 
ATOM   1172 O  OD1 . ASN   A 1 162 ? 2.31    47.089  -20.783 1   30.28 ? 147 ASN   A OD1 1 
ATOM   1173 N  ND2 . ASN   A 1 162 ? 0.775   46.459  -19.289 1   27.5  ? 147 ASN   A ND2 1 
ATOM   1174 N  N   . MET   A 1 163 ? 0.103   44.517  -23.965 1   24.81 ? 148 MET   A N   1 
ATOM   1175 C  CA  . MET   A 1 163 ? 0.185   43.051  -23.99  1   24.53 ? 148 MET   A CA  1 
ATOM   1176 C  C   . MET   A 1 163 ? 0.835   42.487  -25.232 1   24.67 ? 148 MET   A C   1 
ATOM   1177 O  O   . MET   A 1 163 ? 0.907   43.144  -26.258 1   25.56 ? 148 MET   A O   1 
ATOM   1178 C  CB  . MET   A 1 163 ? -1.222  42.445  -23.774 1   24.81 ? 148 MET   A CB  1 
ATOM   1179 C  CG  . MET   A 1 163 ? -1.778  42.711  -22.374 1   26.74 ? 148 MET   A CG  1 
ATOM   1180 S  SD  . MET   A 1 163 ? -3.562  42.415  -22.236 1   28.73 ? 148 MET   A SD  1 
ATOM   1181 C  CE  . MET   A 1 163 ? -3.54   40.616  -21.889 1   27.69 ? 148 MET   A CE  1 
ATOM   1182 N  N   . ASP   A 1 164 ? 1.299   41.25   -25.146 1   24.35 ? 149 ASP   A N   1 
ATOM   1183 C  CA  . ASP   A 1 164 ? 1.824   40.532  -26.311 1   24.94 ? 149 ASP   A CA  1 
ATOM   1184 C  C   . ASP   A 1 164 ? 1.624   39.031  -26.139 1   22.54 ? 149 ASP   A C   1 
ATOM   1185 O  O   . ASP   A 1 164 ? 1.334   38.577  -25.039 1   22.32 ? 149 ASP   A O   1 
ATOM   1186 C  CB  . ASP   A 1 164 ? 3.303   40.83   -26.553 1   28.74 ? 149 ASP   A CB  1 
ATOM   1187 C  CG  . ASP   A 1 164 ? 3.636   40.899  -28.031 1   36    ? 149 ASP   A CG  1 
ATOM   1188 O  OD1 . ASP   A 1 164 ? 3.02    40.135  -28.825 1   34.08 ? 149 ASP   A OD1 1 
ATOM   1189 O  OD2 . ASP   A 1 164 ? 4.496   41.715  -28.4   1   40.58 ? 149 ASP   A OD2 1 
ATOM   1190 N  N   . VAL   A 1 165 ? 1.693   38.284  -27.228 1   21.5  ? 150 VAL   A N   1 
ATOM   1191 C  CA  . VAL   A 1 165 ? 1.62    36.823  -27.158 1   20.6  ? 150 VAL   A CA  1 
ATOM   1192 C  C   . VAL   A 1 165 ? 3.049   36.311  -26.987 1   21.29 ? 150 VAL   A C   1 
ATOM   1193 O  O   . VAL   A 1 165 ? 4.019   37.034  -27.263 1   21.85 ? 150 VAL   A O   1 
ATOM   1194 C  CB  . VAL   A 1 165 ? 0.942   36.177  -28.392 1   20.49 ? 150 VAL   A CB  1 
ATOM   1195 C  CG1 . VAL   A 1 165 ? -0.513  36.614  -28.504 1   20.52 ? 150 VAL   A CG1 1 
ATOM   1196 C  CG2 . VAL   A 1 165 ? 1.716   36.485  -29.678 1   21.41 ? 150 VAL   A CG2 1 
ATOM   1197 N  N   . LEU   A 1 166 ? 3.194   35.063  -26.53  1   20.2  ? 151 LEU   A N   1 
ATOM   1198 C  CA  . LEU   A 1 166 ? 4.489   34.467  -26.392 1   19.75 ? 151 LEU   A CA  1 
ATOM   1199 C  C   . LEU   A 1 166 ? 4.948   33.823  -27.703 1   19.49 ? 151 LEU   A C   1 
ATOM   1200 O  O   . LEU   A 1 166 ? 6.139   33.94   -28.03  1   19.28 ? 151 LEU   A O   1 
ATOM   1201 C  CB  . LEU   A 1 166 ? 4.545   33.483  -25.221 1   20    ? 151 LEU   A CB  1 
ATOM   1202 C  CG  . LEU   A 1 166 ? 4.094   34.061  -23.859 1   22.63 ? 151 LEU   A CG  1 
ATOM   1203 C  CD1 . LEU   A 1 166 ? 4.158   32.972  -22.773 1   23.54 ? 151 LEU   A CD1 1 
ATOM   1204 C  CD2 . LEU   A 1 166 ? 4.963   35.276  -23.448 1   22.6  ? 151 LEU   A CD2 1 
ATOM   1205 N  N   . PHE   A 1 167 ? 4.025   33.157  -28.455 1   18.63 ? 152 PHE   A N   1 
ATOM   1206 C  CA  . PHE   A 1 167 ? 4.393   32.448  -29.677 1   18.89 ? 152 PHE   A CA  1 
ATOM   1207 C  C   . PHE   A 1 167 ? 3.435   32.677  -30.838 1   18.26 ? 152 PHE   A C   1 
ATOM   1208 O  O   . PHE   A 1 167 ? 2.236   32.766  -30.653 1   17.6  ? 152 PHE   A O   1 
ATOM   1209 C  CB  . PHE   A 1 167 ? 4.46    30.923  -29.424 1   19.05 ? 152 PHE   A CB  1 
ATOM   1210 C  CG  . PHE   A 1 167 ? 5.36    30.58   -28.254 1   19.54 ? 152 PHE   A CG  1 
ATOM   1211 C  CD1 . PHE   A 1 167 ? 6.729   30.451  -28.424 1   20.72 ? 152 PHE   A CD1 1 
ATOM   1212 C  CD2 . PHE   A 1 167 ? 4.833   30.39   -26.988 1   19.95 ? 152 PHE   A CD2 1 
ATOM   1213 C  CE1 . PHE   A 1 167 ? 7.561   30.176  -27.346 1   21.35 ? 152 PHE   A CE1 1 
ATOM   1214 C  CE2 . PHE   A 1 167 ? 5.667   30.085  -25.904 1   20.17 ? 152 PHE   A CE2 1 
ATOM   1215 C  CZ  . PHE   A 1 167 ? 7.025   30.013  -26.088 1   21.02 ? 152 PHE   A CZ  1 
ATOM   1216 N  N   . SER   A 1 168 ? 4.006   32.73   -32.053 1   17.59 ? 153 SER   A N   1 
ATOM   1217 C  CA  . SER   A 1 168 ? 3.28    32.862  -33.315 1   19.19 ? 153 SER   A CA  1 
ATOM   1218 C  C   . SER   A 1 168 ? 3.731   31.738  -34.258 1   18.89 ? 153 SER   A C   1 
ATOM   1219 O  O   . SER   A 1 168 ? 4.781   31.142  -34.024 1   19.9  ? 153 SER   A O   1 
ATOM   1220 C  CB  . SER   A 1 168 ? 3.601   34.217  -33.937 1   22.42 ? 153 SER   A CB  1 
ATOM   1221 O  OG  . SER   A 1 168 ? 3.08    35.218  -33.076 1   25.77 ? 153 SER   A OG  1 
ATOM   1222 N  N   . PHE   A 1 169 ? 2.971   31.472  -35.337 1   17.46 ? 154 PHE   A N   1 
ATOM   1223 C  CA  . PHE   A 1 169 ? 3.358   30.421  -36.274 1   17.25 ? 154 PHE   A CA  1 
ATOM   1224 C  C   . PHE   A 1 169 ? 4.123   30.956  -37.498 1   18.29 ? 154 PHE   A C   1 
ATOM   1225 O  O   . PHE   A 1 169 ? 5.116   30.347  -37.906 1   19.19 ? 154 PHE   A O   1 
ATOM   1226 C  CB  . PHE   A 1 169 ? 2.098   29.635  -36.735 1   16.56 ? 154 PHE   A CB  1 
ATOM   1227 C  CG  . PHE   A 1 169 ? 1.499   28.854  -35.596 1   17.64 ? 154 PHE   A CG  1 
ATOM   1228 C  CD1 . PHE   A 1 169 ? 2.079   27.656  -35.172 1   17.95 ? 154 PHE   A CD1 1 
ATOM   1229 C  CD2 . PHE   A 1 169 ? 0.4     29.34   -34.907 1   18.1  ? 154 PHE   A CD2 1 
ATOM   1230 C  CE1 . PHE   A 1 169 ? 1.525   26.933  -34.12  1   18.73 ? 154 PHE   A CE1 1 
ATOM   1231 C  CE2 . PHE   A 1 169 ? -0.143  28.62   -33.841 1   19.18 ? 154 PHE   A CE2 1 
ATOM   1232 C  CZ  . PHE   A 1 169 ? 0.45    27.435  -33.437 1   19.24 ? 154 PHE   A CZ  1 
ATOM   1233 N  N   . ARG   A 1 170 ? 3.606   32.012  -38.142 1   17.98 ? 155 ARG   A N   1 
ATOM   1234 C  CA  . ARG   A 1 170 ? 4.204   32.576  -39.356 1   18.47 ? 155 ARG   A CA  1 
ATOM   1235 C  C   . ARG   A 1 170 ? 4.14    34.079  -39.288 1   19.18 ? 155 ARG   A C   1 
ATOM   1236 O  O   . ARG   A 1 170 ? 3.253   34.636  -38.626 1   19.59 ? 155 ARG   A O   1 
ATOM   1237 C  CB  . ARG   A 1 170 ? 3.413   32.18   -40.623 1   18.75 ? 155 ARG   A CB  1 
ATOM   1238 C  CG  . ARG   A 1 170 ? 3.165   30.697  -40.823 1   20.53 ? 155 ARG   A CG  1 
ATOM   1239 C  CD  . ARG   A 1 170 ? 4.455   29.937  -41.106 1   22.8  ? 155 ARG   A CD  1 
ATOM   1240 N  NE  . ARG   A 1 170 ? 5.115   30.409  -42.316 1   24.67 ? 155 ARG   A NE  1 
ATOM   1241 C  CZ  . ARG   A 1 170 ? 4.83    29.982  -43.542 1   27.99 ? 155 ARG   A CZ  1 
ATOM   1242 N  NH1 . ARG   A 1 170 ? 3.941   29.01   -43.726 1   26.56 ? 155 ARG   A NH1 1 
ATOM   1243 N  NH2 . ARG   A 1 170 ? 5.476   30.474  -44.584 1   28.26 ? 155 ARG   A NH2 1 
ATOM   1244 N  N   . ASP   A 1 171 ? 5.065   34.753  -39.998 1   19.44 ? 156 ASP   A N   1 
ATOM   1245 C  CA  A ASP   A 1 171 ? 5.004   36.216  -39.996 0.5 19.76 ? 156 ASP   A CA  1 
ATOM   1246 C  CA  B ASP   A 1 171 ? 5.117   36.195  -40.155 0.5 19.88 ? 156 ASP   A CA  1 
ATOM   1247 C  C   . ASP   A 1 171 ? 3.777   36.666  -40.765 1   19.57 ? 156 ASP   A C   1 
ATOM   1248 O  O   . ASP   A 1 171 ? 3.364   36.07   -41.761 1   18.55 ? 156 ASP   A O   1 
ATOM   1249 C  CB  A ASP   A 1 171 ? 6.305   36.902  -40.438 0.5 21.49 ? 156 ASP   A CB  1 
ATOM   1250 C  CB  B ASP   A 1 171 ? 6.237   36.451  -41.187 0.5 21.52 ? 156 ASP   A CB  1 
ATOM   1251 C  CG  A ASP   A 1 171 ? 7.477   36.519  -39.557 0.5 24.54 ? 156 ASP   A CG  1 
ATOM   1252 C  CG  B ASP   A 1 171 ? 6.677   37.88   -41.299 0.5 25.99 ? 156 ASP   A CG  1 
ATOM   1253 O  OD1 A ASP   A 1 171 ? 7.445   36.838  -38.333 0.5 24.48 ? 156 ASP   A OD1 1 
ATOM   1254 O  OD1 B ASP   A 1 171 ? 6.691   38.569  -40.269 0.5 26.41 ? 156 ASP   A OD1 1 
ATOM   1255 O  OD2 A ASP   A 1 171 ? 8.405   35.897  -40.071 0.5 25.49 ? 156 ASP   A OD2 1 
ATOM   1256 O  OD2 B ASP   A 1 171 ? 7.064   38.293  -42.416 0.5 29.8  ? 156 ASP   A OD2 1 
ATOM   1257 N  N   . GLY   A 1 172 ? 3.105   37.659  -40.188 1   20.54 ? 157 GLY   A N   1 
ATOM   1258 C  CA  . GLY   A 1 172 ? 1.858   38.163  -40.769 1   21.58 ? 157 GLY   A CA  1 
ATOM   1259 C  C   . GLY   A 1 172 ? 0.654   37.253  -40.564 1   21.49 ? 157 GLY   A C   1 
ATOM   1260 O  O   . GLY   A 1 172 ? -0.352  37.414  -41.252 1   22.14 ? 157 GLY   A O   1 
ATOM   1261 N  N   . ASP   A 1 173 ? 0.73    36.276  -39.628 1   19.67 ? 158 ASP   A N   1 
ATOM   1262 C  CA  . ASP   A 1 173 ? -0.407  35.362  -39.394 1   18.13 ? 158 ASP   A CA  1 
ATOM   1263 C  C   . ASP   A 1 173 ? -1.521  35.987  -38.542 1   18.58 ? 158 ASP   A C   1 
ATOM   1264 O  O   . ASP   A 1 173 ? -2.536  35.342  -38.369 1   19.32 ? 158 ASP   A O   1 
ATOM   1265 C  CB  . ASP   A 1 173 ? 0.014   34      -38.784 1   17.11 ? 158 ASP   A CB  1 
ATOM   1266 C  CG  . ASP   A 1 173 ? 0.684   34.03   -37.414 1   18.96 ? 158 ASP   A CG  1 
ATOM   1267 O  OD1 . ASP   A 1 173 ? 0.777   35.118  -36.816 1   19.4  ? 158 ASP   A OD1 1 
ATOM   1268 O  OD2 . ASP   A 1 173 ? 1.136   32.951  -36.942 1   19.48 ? 158 ASP   A OD2 1 
ATOM   1269 N  N   . CYS   A 1 174 ? -1.302  37.185  -37.943 1   18.07 ? 159 CYS   A N   1 
ATOM   1270 C  CA  . CYS   A 1 174 ? -2.316  37.815  -37.071 1   18.62 ? 159 CYS   A CA  1 
ATOM   1271 C  C   . CYS   A 1 174 ? -2.615  36.988  -35.81  1   18.15 ? 159 CYS   A C   1 
ATOM   1272 O  O   . CYS   A 1 174 ? -3.647  37.18   -35.176 1   18.51 ? 159 CYS   A O   1 
ATOM   1273 C  CB  . CYS   A 1 174 ? -3.598  38.166  -37.842 1   20.59 ? 159 CYS   A CB  1 
ATOM   1274 S  SG  . CYS   A 1 174 ? -3.351  39.376  -39.17  1   25.31 ? 159 CYS   A SG  1 
ATOM   1275 N  N   . SER   A 1 175 ? -1.676  36.096  -35.403 1   18.59 ? 160 SER   A N   1 
ATOM   1276 C  CA  . SER   A 1 175 ? -1.873  35.303  -34.205 1   18.23 ? 160 SER   A CA  1 
ATOM   1277 C  C   . SER   A 1 175 ? -1.895  36.199  -32.979 1   17.75 ? 160 SER   A C   1 
ATOM   1278 O  O   . SER   A 1 175 ? -2.702  35.946  -32.098 1   17.16 ? 160 SER   A O   1 
ATOM   1279 C  CB  . SER   A 1 175 ? -0.808  34.221  -34.075 1   18.07 ? 160 SER   A CB  1 
ATOM   1280 O  OG  . SER   A 1 175 ? 0.473   34.813  -33.974 1   20.29 ? 160 SER   A OG  1 
ATOM   1281 N  N   . LYS   A 1 176 ? -1.108  37.297  -32.95  1   17.23 ? 161 LYS   A N   1 
ATOM   1282 C  CA  . LYS   A 1 176 ? -1.154  38.194  -31.793 1   17.58 ? 161 LYS   A CA  1 
ATOM   1283 C  C   . LYS   A 1 176 ? -2.55   38.811  -31.64  1   18.03 ? 161 LYS   A C   1 
ATOM   1284 O  O   . LYS   A 1 176 ? -3.157  38.686  -30.578 1   18.26 ? 161 LYS   A O   1 
ATOM   1285 C  CB  . LYS   A 1 176 ? -0.077  39.292  -31.88  1   19.38 ? 161 LYS   A CB  1 
ATOM   1286 C  CG  . LYS   A 1 176 ? -0.173  40.284  -30.714 1   22.03 ? 161 LYS   A CG  1 
ATOM   1287 C  CD  . LYS   A 1 176 ? 0.72    41.51   -30.92  1   26.04 ? 161 LYS   A CD  1 
ATOM   1288 C  CE  . LYS   A 1 176 ? 0.433   42.546  -29.859 1   29.61 ? 161 LYS   A CE  1 
ATOM   1289 N  NZ  . LYS   A 1 176 ? 1.613   43.436  -29.643 1   33.2  ? 161 LYS   A NZ  1 
ATOM   1290 N  N   . GLY   A 1 177 ? -3.101  39.379  -32.727 1   17.47 ? 162 GLY   A N   1 
ATOM   1291 C  CA  . GLY   A 1 177 ? -4.423  39.972  -32.672 1   16.54 ? 162 GLY   A CA  1 
ATOM   1292 C  C   . GLY   A 1 177 ? -5.518  38.977  -32.322 1   16.74 ? 162 GLY   A C   1 
ATOM   1293 O  O   . GLY   A 1 177 ? -6.359  39.256  -31.476 1   16.14 ? 162 GLY   A O   1 
ATOM   1294 N  N   . PHE   A 1 178 ? -5.509  37.813  -32.969 1   16.03 ? 163 PHE   A N   1 
ATOM   1295 C  CA  . PHE   A 1 178 ? -6.553  36.803  -32.751 1   17.01 ? 163 PHE   A CA  1 
ATOM   1296 C  C   . PHE   A 1 178 ? -6.528  36.237  -31.326 1   16.74 ? 163 PHE   A C   1 
ATOM   1297 O  O   . PHE   A 1 178 ? -7.567  36.201  -30.648 1   17.64 ? 163 PHE   A O   1 
ATOM   1298 C  CB  . PHE   A 1 178 ? -6.375  35.679  -33.776 1   17.28 ? 163 PHE   A CB  1 
ATOM   1299 C  CG  . PHE   A 1 178 ? -7.392  34.563  -33.677 1   17.56 ? 163 PHE   A CG  1 
ATOM   1300 C  CD1 . PHE   A 1 178 ? -8.742  34.803  -33.93  1   17.42 ? 163 PHE   A CD1 1 
ATOM   1301 C  CD2 . PHE   A 1 178 ? -6.987  33.252  -33.433 1   18    ? 163 PHE   A CD2 1 
ATOM   1302 C  CE1 . PHE   A 1 178 ? -9.675  33.758  -33.904 1   18.48 ? 163 PHE   A CE1 1 
ATOM   1303 C  CE2 . PHE   A 1 178 ? -7.931  32.202  -33.422 1   18.6  ? 163 PHE   A CE2 1 
ATOM   1304 C  CZ  . PHE   A 1 178 ? -9.256  32.467  -33.659 1   18.49 ? 163 PHE   A CZ  1 
ATOM   1305 N  N   . PHE   A 1 179 ? -5.344  35.798  -30.871 1   16.44 ? 164 PHE   A N   1 
ATOM   1306 C  CA  . PHE   A 1 179 ? -5.212  35.258  -29.521 1   16.2  ? 164 PHE   A CA  1 
ATOM   1307 C  C   . PHE   A 1 179 ? -5.492  36.32   -28.455 1   15.98 ? 164 PHE   A C   1 
ATOM   1308 O  O   . PHE   A 1 179 ? -6.231  36.045  -27.514 1   14.18 ? 164 PHE   A O   1 
ATOM   1309 C  CB  . PHE   A 1 179 ? -3.852  34.604  -29.306 1   15.6  ? 164 PHE   A CB  1 
ATOM   1310 C  CG  . PHE   A 1 179 ? -3.564  33.398  -30.197 1   15.95 ? 164 PHE   A CG  1 
ATOM   1311 C  CD1 . PHE   A 1 179 ? -4.599  32.641  -30.729 1   17.14 ? 164 PHE   A CD1 1 
ATOM   1312 C  CD2 . PHE   A 1 179 ? -2.259  33.035  -30.499 1   17.53 ? 164 PHE   A CD2 1 
ATOM   1313 C  CE1 . PHE   A 1 179 ? -4.331  31.513  -31.521 1   17.92 ? 164 PHE   A CE1 1 
ATOM   1314 C  CE2 . PHE   A 1 179 ? -1.988  31.911  -31.296 1   18.29 ? 164 PHE   A CE2 1 
ATOM   1315 C  CZ  . PHE   A 1 179 ? -3.031  31.172  -31.807 1   17.66 ? 164 PHE   A CZ  1 
ATOM   1316 N  N   . LEU   A 1 180 ? -4.901  37.521  -28.615 1   15.91 ? 165 LEU   A N   1 
ATOM   1317 C  CA  . LEU   A 1 180 ? -5.061  38.582  -27.632 1   17.63 ? 165 LEU   A CA  1 
ATOM   1318 C  C   . LEU   A 1 180 ? -6.482  39.159  -27.524 1   16.76 ? 165 LEU   A C   1 
ATOM   1319 O  O   . LEU   A 1 180 ? -6.923  39.414  -26.414 1   17.69 ? 165 LEU   A O   1 
ATOM   1320 C  CB  . LEU   A 1 180 ? -4.038  39.689  -27.894 1   19.32 ? 165 LEU   A CB  1 
ATOM   1321 C  CG  . LEU   A 1 180 ? -2.999  40.004  -26.814 1   24.8  ? 165 LEU   A CG  1 
ATOM   1322 C  CD1 . LEU   A 1 180 ? -2.362  38.756  -26.206 1   25.07 ? 165 LEU   A CD1 1 
ATOM   1323 C  CD2 . LEU   A 1 180 ? -1.931  40.98   -27.348 1   25.88 ? 165 LEU   A CD2 1 
ATOM   1324 N  N   . VAL   A 1 181 ? -7.219  39.344  -28.64  1   15.8  ? 166 VAL   A N   1 
ATOM   1325 C  CA  . VAL   A 1 181 ? -8.576  39.857  -28.575 1   15.28 ? 166 VAL   A CA  1 
ATOM   1326 C  C   . VAL   A 1 181 ? -9.51   38.787  -27.954 1   15.48 ? 166 VAL   A C   1 
ATOM   1327 O  O   . VAL   A 1 181 ? -10.297 39.112  -27.061 1   14.3  ? 166 VAL   A O   1 
ATOM   1328 C  CB  . VAL   A 1 181 ? -9.072  40.4    -29.929 1   15.94 ? 166 VAL   A CB  1 
ATOM   1329 C  CG1 . VAL   A 1 181 ? -10.551 40.751  -29.859 1   16.39 ? 166 VAL   A CG1 1 
ATOM   1330 C  CG2 . VAL   A 1 181 ? -8.225  41.627  -30.335 1   17.59 ? 166 VAL   A CG2 1 
ATOM   1331 N  N   . SER   A 1 182 ? -9.25   37.48   -28.253 1   14.8  ? 167 SER   A N   1 
ATOM   1332 C  CA  . SER   A 1 182 ? -9.967  36.366  -27.634 1   16.1  ? 167 SER   A CA  1 
ATOM   1333 C  C   . SER   A 1 182 ? -9.709  36.425  -26.118 1   17.13 ? 167 SER   A C   1 
ATOM   1334 O  O   . SER   A 1 182 ? -10.667 36.385  -25.341 1   18.08 ? 167 SER   A O   1 
ATOM   1335 C  CB  . SER   A 1 182 ? -9.434  35.033  -28.185 1   17.63 ? 167 SER   A CB  1 
ATOM   1336 O  OG  . SER   A 1 182 ? -9.926  34.787  -29.489 1   19.37 ? 167 SER   A OG  1 
ATOM   1337 N  N   . LEU   A 1 183 ? -8.438  36.609  -25.715 1   18.24 ? 168 LEU   A N   1 
ATOM   1338 C  CA  . LEU   A 1 183 ? -8.058  36.696  -24.31  1   18.36 ? 168 LEU   A CA  1 
ATOM   1339 C  C   . LEU   A 1 183 ? -8.746  37.896  -23.641 1   18.75 ? 168 LEU   A C   1 
ATOM   1340 O  O   . LEU   A 1 183 ? -9.322  37.745  -22.571 1   18.47 ? 168 LEU   A O   1 
ATOM   1341 C  CB  . LEU   A 1 183 ? -6.538  36.804  -24.168 1   18.58 ? 168 LEU   A CB  1 
ATOM   1342 C  CG  . LEU   A 1 183 ? -6.016  36.991  -22.734 1   20.51 ? 168 LEU   A CG  1 
ATOM   1343 C  CD1 . LEU   A 1 183 ? -6.376  35.791  -21.844 1   20.71 ? 168 LEU   A CD1 1 
ATOM   1344 C  CD2 . LEU   A 1 183 ? -4.529  37.257  -22.716 1   20.52 ? 168 LEU   A CD2 1 
ATOM   1345 N  N   . LEU   A 1 184 ? -8.724  39.069  -24.286 1   18.51 ? 169 LEU   A N   1 
ATOM   1346 C  CA  . LEU   A 1 184 ? -9.354  40.278  -23.714 1   18.86 ? 169 LEU   A CA  1 
ATOM   1347 C  C   . LEU   A 1 184 ? -10.85  40.116  -23.483 1   18.76 ? 169 LEU   A C   1 
ATOM   1348 O  O   . LEU   A 1 184 ? -11.356 40.58   -22.471 1   19.52 ? 169 LEU   A O   1 
ATOM   1349 C  CB  . LEU   A 1 184 ? -9.033  41.515  -24.584 1   18.39 ? 169 LEU   A CB  1 
ATOM   1350 C  CG  . LEU   A 1 184 ? -7.558  41.942  -24.453 1   19.34 ? 169 LEU   A CG  1 
ATOM   1351 C  CD1 . LEU   A 1 184 ? -7.14   42.913  -25.542 1   18.5  ? 169 LEU   A CD1 1 
ATOM   1352 C  CD2 . LEU   A 1 184 ? -7.246  42.416  -23.032 1   21.48 ? 169 LEU   A CD2 1 
ATOM   1353 N  N   . VAL   A 1 185 ? -11.585 39.497  -24.45  1   17.59 ? 170 VAL   A N   1 
ATOM   1354 C  CA  . VAL   A 1 185 ? -12.998 39.238  -24.316 1   18.46 ? 170 VAL   A CA  1 
ATOM   1355 C  C   . VAL   A 1 185 ? -13.231 38.254  -23.172 1   20.23 ? 170 VAL   A C   1 
ATOM   1356 O  O   . VAL   A 1 185 ? -14.076 38.498  -22.295 1   20.91 ? 170 VAL   A O   1 
ATOM   1357 C  CB  . VAL   A 1 185 ? -13.6   38.735  -25.649 1   17.3  ? 170 VAL   A CB  1 
ATOM   1358 C  CG1 . VAL   A 1 185 ? -15.008 38.179  -25.445 1   17.13 ? 170 VAL   A CG1 1 
ATOM   1359 C  CG2 . VAL   A 1 185 ? -13.598 39.856  -26.674 1   16.36 ? 170 VAL   A CG2 1 
ATOM   1360 N  N   . GLU   A 1 186 ? -12.416 37.182  -23.139 1   20.8  ? 171 GLU   A N   1 
ATOM   1361 C  CA  . GLU   A 1 186 ? -12.449 36.151  -22.106 1   21.59 ? 171 GLU   A CA  1 
ATOM   1362 C  C   . GLU   A 1 186 ? -12.288 36.797  -20.703 1   23.49 ? 171 GLU   A C   1 
ATOM   1363 O  O   . GLU   A 1 186 ? -13.081 36.493  -19.791 1   25.8  ? 171 GLU   A O   1 
ATOM   1364 C  CB  . GLU   A 1 186 ? -11.333 35.113  -22.391 1   22.74 ? 171 GLU   A CB  1 
ATOM   1365 C  CG  . GLU   A 1 186 ? -11.122 34.094  -21.294 1   23.31 ? 171 GLU   A CG  1 
ATOM   1366 C  CD  . GLU   A 1 186 ? -11.937 32.828  -21.423 1   23.61 ? 171 GLU   A CD  1 
ATOM   1367 O  OE1 . GLU   A 1 186 ? -12.351 32.475  -22.556 1   21.86 ? 171 GLU   A OE1 1 
ATOM   1368 O  OE2 . GLU   A 1 186 ? -12.191 32.204  -20.369 1   25.99 ? 171 GLU   A OE2 1 
ATOM   1369 N  N   . ILE   A 1 187 ? -11.349 37.731  -20.558 1   22.39 ? 172 ILE   A N   1 
ATOM   1370 C  CA  . ILE   A 1 187 ? -11.116 38.436  -19.3   1   22.98 ? 172 ILE   A CA  1 
ATOM   1371 C  C   . ILE   A 1 187 ? -12.294 39.367  -18.961 1   22.9  ? 172 ILE   A C   1 
ATOM   1372 O  O   . ILE   A 1 187 ? -12.701 39.415  -17.812 1   23.3  ? 172 ILE   A O   1 
ATOM   1373 C  CB  . ILE   A 1 187 ? -9.781  39.218  -19.317 1   22.99 ? 172 ILE   A CB  1 
ATOM   1374 C  CG1 . ILE   A 1 187 ? -8.572  38.252  -19.321 1   23.05 ? 172 ILE   A CG1 1 
ATOM   1375 C  CG2 . ILE   A 1 187 ? -9.678  40.178  -18.115 1   23.81 ? 172 ILE   A CG2 1 
ATOM   1376 C  CD1 . ILE   A 1 187 ? -7.263  38.954  -19.626 1   23.57 ? 172 ILE   A CD1 1 
ATOM   1377 N  N   . ALA   A 1 188 ? -12.85  40.085  -19.953 1   22.85 ? 173 ALA   A N   1 
ATOM   1378 C  CA  . ALA   A 1 188 ? -13.981 40.969  -19.715 1   22.85 ? 173 ALA   A CA  1 
ATOM   1379 C  C   . ALA   A 1 188 ? -15.195 40.182  -19.201 1   23.35 ? 173 ALA   A C   1 
ATOM   1380 O  O   . ALA   A 1 188 ? -15.865 40.623  -18.257 1   23.57 ? 173 ALA   A O   1 
ATOM   1381 C  CB  . ALA   A 1 188 ? -14.334 41.738  -20.981 1   21.9  ? 173 ALA   A CB  1 
ATOM   1382 N  N   . ALA   A 1 189 ? -15.484 39.023  -19.819 1   22.83 ? 174 ALA   A N   1 
ATOM   1383 C  CA  . ALA   A 1 189 ? -16.615 38.202  -19.375 1   23.77 ? 174 ALA   A CA  1 
ATOM   1384 C  C   . ALA   A 1 189 ? -16.388 37.64   -17.967 1   24.46 ? 174 ALA   A C   1 
ATOM   1385 O  O   . ALA   A 1 189 ? -17.345 37.501  -17.17  1   24.1  ? 174 ALA   A O   1 
ATOM   1386 C  CB  . ALA   A 1 189 ? -16.885 37.083  -20.375 1   24.19 ? 174 ALA   A CB  1 
ATOM   1387 N  N   . ALA   A 1 190 ? -15.13  37.321  -17.652 1   25.72 ? 175 ALA   A N   1 
ATOM   1388 C  CA  . ALA   A 1 190 ? -14.733 36.801  -16.339 1   27.36 ? 175 ALA   A CA  1 
ATOM   1389 C  C   . ALA   A 1 190 ? -15.046 37.748  -15.201 1   27.5  ? 175 ALA   A C   1 
ATOM   1390 O  O   . ALA   A 1 190 ? -15.164 37.263  -14.082 1   27.73 ? 175 ALA   A O   1 
ATOM   1391 C  CB  . ALA   A 1 190 ? -13.252 36.458  -16.308 1   27.63 ? 175 ALA   A CB  1 
ATOM   1392 N  N   . SER   A 1 191 ? -15.193 39.064  -15.452 1   27.34 ? 176 SER   A N   1 
ATOM   1393 C  CA  . SER   A 1 191 ? -15.529 39.986  -14.342 1   28.45 ? 176 SER   A CA  1 
ATOM   1394 C  C   . SER   A 1 191 ? -16.91  39.663  -13.716 1   28.18 ? 176 SER   A C   1 
ATOM   1395 O  O   . SER   A 1 191 ? -17.163 40.038  -12.583 1   29.2  ? 176 SER   A O   1 
ATOM   1396 C  CB  . SER   A 1 191 ? -15.44  41.45   -14.767 1   30.99 ? 176 SER   A CB  1 
ATOM   1397 O  OG  . SER   A 1 191 ? -16.421 41.734  -15.755 1   36.58 ? 176 SER   A OG  1 
ATOM   1398 N  N   . ALA   A 1 192 ? -17.779 38.923  -14.443 1   27.01 ? 177 ALA   A N   1 
ATOM   1399 C  CA  . ALA   A 1 192 ? -19.083 38.485  -13.957 1   25.82 ? 177 ALA   A CA  1 
ATOM   1400 C  C   . ALA   A 1 192 ? -19.003 37.202  -13.103 1   24.78 ? 177 ALA   A C   1 
ATOM   1401 O  O   . ALA   A 1 192 ? -19.962 36.883  -12.4   1   24.09 ? 177 ALA   A O   1 
ATOM   1402 C  CB  . ALA   A 1 192 ? -20.022 38.267  -15.131 1   25.44 ? 177 ALA   A CB  1 
ATOM   1403 N  N   . ILE   A 1 193 ? -17.876 36.449  -13.153 1   24.27 ? 178 ILE   A N   1 
ATOM   1404 C  CA  . ILE   A 1 193 ? -17.776 35.193  -12.402 1   24.5  ? 178 ILE   A CA  1 
ATOM   1405 C  C   . ILE   A 1 193 ? -17.939 35.402  -10.915 1   26.34 ? 178 ILE   A C   1 
ATOM   1406 O  O   . ILE   A 1 193 ? -18.588 34.589  -10.253 1   27    ? 178 ILE   A O   1 
ATOM   1407 C  CB  . ILE   A 1 193 ? -16.441 34.449  -12.719 1   24.07 ? 178 ILE   A CB  1 
ATOM   1408 C  CG1 . ILE   A 1 193 ? -16.359 34.105  -14.225 1   24.77 ? 178 ILE   A CG1 1 
ATOM   1409 C  CG2 . ILE   A 1 193 ? -16.306 33.212  -11.849 1   23.17 ? 178 ILE   A CG2 1 
ATOM   1410 C  CD1 . ILE   A 1 193 ? -14.974 33.552  -14.621 1   25.44 ? 178 ILE   A CD1 1 
ATOM   1411 N  N   . LYS   A 1 194 ? -17.318 36.463  -10.377 1   27.53 ? 179 LYS   A N   1 
ATOM   1412 C  CA  . LYS   A 1 194 ? -17.402 36.771  -8.943  1   29.58 ? 179 LYS   A CA  1 
ATOM   1413 C  C   . LYS   A 1 194 ? -18.846 37.004  -8.465  1   30.43 ? 179 LYS   A C   1 
ATOM   1414 O  O   . LYS   A 1 194 ? -19.108 36.915  -7.266  1   31.47 ? 179 LYS   A O   1 
ATOM   1415 C  CB  . LYS   A 1 194 ? -16.537 37.997  -8.583  1   31.99 ? 179 LYS   A CB  1 
ATOM   1416 C  CG  . LYS   A 1 194 ? -17.011 39.303  -9.217  1   36.15 ? 179 LYS   A CG  1 
ATOM   1417 C  CD  . LYS   A 1 194 ? -16.336 40.503  -8.571  1   41.13 ? 179 LYS   A CD  1 
ATOM   1418 C  CE  . LYS   A 1 194 ? -15.251 41.099  -9.438  1   46.49 ? 179 LYS   A CE  1 
ATOM   1419 N  NZ  . LYS   A 1 194 ? -15.8   42.034  -10.463 1   49.3  ? 179 LYS   A NZ  1 
ATOM   1420 N  N   . VAL   A 1 195 ? -19.78  37.283  -9.395  1   29.41 ? 180 VAL   A N   1 
ATOM   1421 C  CA  . VAL   A 1 195 ? -21.188 37.5    -9.089  1   29.27 ? 180 VAL   A CA  1 
ATOM   1422 C  C   . VAL   A 1 195 ? -21.963 36.162  -8.93   1   29.32 ? 180 VAL   A C   1 
ATOM   1423 O  O   . VAL   A 1 195 ? -23.027 36.114  -8.28   1   29.33 ? 180 VAL   A O   1 
ATOM   1424 C  CB  . VAL   A 1 195 ? -21.831 38.425  -10.158 1   30.11 ? 180 VAL   A CB  1 
ATOM   1425 C  CG1 . VAL   A 1 195 ? -23.256 38.79   -9.76   1   30.95 ? 180 VAL   A CG1 1 
ATOM   1426 C  CG2 . VAL   A 1 195 ? -21.004 39.696  -10.359 1   30.39 ? 180 VAL   A CG2 1 
ATOM   1427 N  N   . ILE   A 1 196 ? -21.425 35.053  -9.484  1   27.58 ? 181 ILE   A N   1 
ATOM   1428 C  CA  . ILE   A 1 196 ? -22.086 33.761  -9.382  1   27.23 ? 181 ILE   A CA  1 
ATOM   1429 C  C   . ILE   A 1 196 ? -22.417 33.356  -7.93   1   27.58 ? 181 ILE   A C   1 
ATOM   1430 O  O   . ILE   A 1 196 ? -23.568 32.989  -7.702  1   27.08 ? 181 ILE   A O   1 
ATOM   1431 C  CB  . ILE   A 1 196 ? -21.305 32.658  -10.143 1   27.29 ? 181 ILE   A CB  1 
ATOM   1432 C  CG1 . ILE   A 1 196 ? -21.337 32.956  -11.666 1   27.25 ? 181 ILE   A CG1 1 
ATOM   1433 C  CG2 . ILE   A 1 196 ? -21.861 31.254  -9.841  1   27.88 ? 181 ILE   A CG2 1 
ATOM   1434 C  CD1 . ILE   A 1 196 ? -20.467 31.99   -12.505 1   27.47 ? 181 ILE   A CD1 1 
ATOM   1435 N  N   . PRO   A 1 197 ? -21.499 33.457  -6.929  1   28.05 ? 182 PRO   A N   1 
ATOM   1436 C  CA  . PRO   A 1 197 ? -21.888 33.066  -5.561  1   28.23 ? 182 PRO   A CA  1 
ATOM   1437 C  C   . PRO   A 1 197 ? -22.998 33.955  -5.002  1   28.7  ? 182 PRO   A C   1 
ATOM   1438 O  O   . PRO   A 1 197 ? -23.789 33.482  -4.21   1   28.52 ? 182 PRO   A O   1 
ATOM   1439 C  CB  . PRO   A 1 197 ? -20.585 33.192  -4.752  1   28.8  ? 182 PRO   A CB  1 
ATOM   1440 C  CG  . PRO   A 1 197 ? -19.487 33.202  -5.774  1   29.28 ? 182 PRO   A CG  1 
ATOM   1441 C  CD  . PRO   A 1 197 ? -20.075 33.861  -6.983  1   27.4  ? 182 PRO   A CD  1 
ATOM   1442 N  N   . THR   A 1 198 ? -23.056 35.223  -5.417  1   29.45 ? 183 THR   A N   1 
ATOM   1443 C  CA  . THR   A 1 198 ? -24.115 36.154  -5.009  1   30.25 ? 183 THR   A CA  1 
ATOM   1444 C  C   . THR   A 1 198 ? -25.448 35.677  -5.553  1   29.69 ? 183 THR   A C   1 
ATOM   1445 O  O   . THR   A 1 198 ? -26.438 35.704  -4.819  1   30.37 ? 183 THR   A O   1 
ATOM   1446 C  CB  . THR   A 1 198 ? -23.817 37.56   -5.513  1   32.79 ? 183 THR   A CB  1 
ATOM   1447 O  OG1 . THR   A 1 198 ? -22.52  37.928  -5.086  1   34.49 ? 183 THR   A OG1 1 
ATOM   1448 C  CG2 . THR   A 1 198 ? -24.82  38.608  -4.985  1   33.42 ? 183 THR   A CG2 1 
ATOM   1449 N  N   . VAL   A 1 199 ? -25.479 35.186  -6.806  1   28.46 ? 184 VAL   A N   1 
ATOM   1450 C  CA  . VAL   A 1 199 ? -26.694 34.644  -7.43   1   28.27 ? 184 VAL   A CA  1 
ATOM   1451 C  C   . VAL   A 1 199 ? -27.231 33.446  -6.649  1   29.09 ? 184 VAL   A C   1 
ATOM   1452 O  O   . VAL   A 1 199 ? -28.392 33.464  -6.241  1   29.34 ? 184 VAL   A O   1 
ATOM   1453 C  CB  . VAL   A 1 199 ? -26.49  34.329  -8.936  1   28.21 ? 184 VAL   A CB  1 
ATOM   1454 C  CG1 . VAL   A 1 199 ? -27.678 33.576  -9.517  1   27.62 ? 184 VAL   A CG1 1 
ATOM   1455 C  CG2 . VAL   A 1 199 ? -26.21  35.61   -9.736  1   28.95 ? 184 VAL   A CG2 1 
ATOM   1456 N  N   . PHE   A 1 200 ? -26.398 32.41   -6.41   1   28.85 ? 185 PHE   A N   1 
ATOM   1457 C  CA  . PHE   A 1 200 ? -26.85  31.22   -5.688  1   29.13 ? 185 PHE   A CA  1 
ATOM   1458 C  C   . PHE   A 1 200 ? -27.256 31.476  -4.246  1   28.95 ? 185 PHE   A C   1 
ATOM   1459 O  O   . PHE   A 1 200 ? -28.181 30.829  -3.743  1   28.26 ? 185 PHE   A O   1 
ATOM   1460 C  CB  . PHE   A 1 200 ? -25.791 30.096  -5.756  1   29.33 ? 185 PHE   A CB  1 
ATOM   1461 C  CG  . PHE   A 1 200 ? -25.69  29.507  -7.14   1   29.83 ? 185 PHE   A CG  1 
ATOM   1462 C  CD1 . PHE   A 1 200 ? -26.806 28.989  -7.77   1   30.65 ? 185 PHE   A CD1 1 
ATOM   1463 C  CD2 . PHE   A 1 200 ? -24.495 29.517  -7.829  1   30.8  ? 185 PHE   A CD2 1 
ATOM   1464 C  CE1 . PHE   A 1 200 ? -26.728 28.479  -9.054  1   31.2  ? 185 PHE   A CE1 1 
ATOM   1465 C  CE2 . PHE   A 1 200 ? -24.409 28.958  -9.099  1   31.61 ? 185 PHE   A CE2 1 
ATOM   1466 C  CZ  . PHE   A 1 200 ? -25.531 28.474  -9.715  1   31.18 ? 185 PHE   A CZ  1 
ATOM   1467 N  N   . LYS   A 1 201 ? -26.554 32.394  -3.587  1   29.54 ? 186 LYS   A N   1 
ATOM   1468 C  CA  . LYS   A 1 201 ? -26.82  32.747  -2.211  1   31.15 ? 186 LYS   A CA  1 
ATOM   1469 C  C   . LYS   A 1 201 ? -28.144 33.517  -2.136  1   31.04 ? 186 LYS   A C   1 
ATOM   1470 O  O   . LYS   A 1 201 ? -28.991 33.195  -1.303  1   30.4  ? 186 LYS   A O   1 
ATOM   1471 C  CB  . LYS   A 1 201 ? -25.655 33.577  -1.635  1   34.44 ? 186 LYS   A CB  1 
ATOM   1472 C  CG  . LYS   A 1 201 ? -25.9   34.072  -0.221  1   41.87 ? 186 LYS   A CG  1 
ATOM   1473 C  CD  . LYS   A 1 201 ? -25.975 32.912  0.777   1   48.73 ? 186 LYS   A CD  1 
ATOM   1474 N  N   . ALA   A 1 202 ? -28.353 34.478  -3.059  1   30.92 ? 187 ALA   A N   1 
ATOM   1475 C  CA  . ALA   A 1 202 ? -29.617 35.224  -3.098  1   31.37 ? 187 ALA   A CA  1 
ATOM   1476 C  C   . ALA   A 1 202 ? -30.806 34.287  -3.343  1   32.89 ? 187 ALA   A C   1 
ATOM   1477 O  O   . ALA   A 1 202 ? -31.847 34.467  -2.709  1   33.24 ? 187 ALA   A O   1 
ATOM   1478 C  CB  . ALA   A 1 202 ? -29.57  36.306  -4.153  1   30.58 ? 187 ALA   A CB  1 
ATOM   1479 N  N   . MET   A 1 203 ? -30.646 33.252  -4.192  1   32.89 ? 188 MET   A N   1 
ATOM   1480 C  CA  . MET   A 1 203 ? -31.734 32.296  -4.414  1   33.95 ? 188 MET   A CA  1 
ATOM   1481 C  C   . MET   A 1 203 ? -32.032 31.473  -3.155  1   36.12 ? 188 MET   A C   1 
ATOM   1482 O  O   . MET   A 1 203 ? -33.2   31.339  -2.775  1   36.56 ? 188 MET   A O   1 
ATOM   1483 C  CB  . MET   A 1 203 ? -31.423 31.347  -5.566  1   34.33 ? 188 MET   A CB  1 
ATOM   1484 C  CG  . MET   A 1 203 ? -31.493 31.985  -6.934  1   37.33 ? 188 MET   A CG  1 
ATOM   1485 S  SD  . MET   A 1 203 ? -30.58  30.982  -8.146  1   43.99 ? 188 MET   A SD  1 
ATOM   1486 C  CE  . MET   A 1 203 ? -31.445 29.479  -8.059  1   42.51 ? 188 MET   A CE  1 
ATOM   1487 N  N   . GLN   A 1 204 ? -30.987 30.927  -2.499  1   36.73 ? 189 GLN   A N   1 
ATOM   1488 C  CA  . GLN   A 1 204 ? -31.138 30.101  -1.304  1   38.01 ? 189 GLN   A CA  1 
ATOM   1489 C  C   . GLN   A 1 204 ? -31.785 30.892  -0.159  1   38.42 ? 189 GLN   A C   1 
ATOM   1490 O  O   . GLN   A 1 204 ? -32.694 30.386  0.498   1   38.79 ? 189 GLN   A O   1 
ATOM   1491 C  CB  . GLN   A 1 204 ? -29.763 29.528  -0.887  1   40.76 ? 189 GLN   A CB  1 
ATOM   1492 C  CG  . GLN   A 1 204 ? -29.731 28.752  0.431   1   46.61 ? 189 GLN   A CG  1 
ATOM   1493 C  CD  . GLN   A 1 204 ? -30.429 27.414  0.375   1   54.81 ? 189 GLN   A CD  1 
ATOM   1494 O  OE1 . GLN   A 1 204 ? -31.072 26.985  1.347   1   58.76 ? 189 GLN   A OE1 1 
ATOM   1495 N  NE2 . GLN   A 1 204 ? -30.322 26.714  -0.752  1   56.02 ? 189 GLN   A NE2 1 
ATOM   1496 N  N   . MET   A 1 205 ? -31.324 32.125  0.057   1   38.27 ? 190 MET   A N   1 
ATOM   1497 C  CA  . MET   A 1 205 ? -31.842 33.015  1.093   1   38.65 ? 190 MET   A CA  1 
ATOM   1498 C  C   . MET   A 1 205 ? -33.096 33.778  0.675   1   38.5  ? 190 MET   A C   1 
ATOM   1499 O  O   . MET   A 1 205 ? -33.52  34.662  1.423   1   39.61 ? 190 MET   A O   1 
ATOM   1500 C  CB  . MET   A 1 205 ? -30.757 34.033  1.5     1   40.06 ? 190 MET   A CB  1 
ATOM   1501 C  CG  . MET   A 1 205 ? -29.526 33.399  2.084   1   45.06 ? 190 MET   A CG  1 
ATOM   1502 S  SD  . MET   A 1 205 ? -29.901 32.463  3.592   1   61.24 ? 190 MET   A SD  1 
ATOM   1503 C  CE  . MET   A 1 205 ? -28.857 31.015  3.33    1   62.29 ? 190 MET   A CE  1 
ATOM   1504 N  N   . GLN   A 1 206 ? -33.653 33.505  -0.527  1   37.05 ? 191 GLN   A N   1 
ATOM   1505 C  CA  . GLN   A 1 206 ? -34.816 34.194  -1.077  1   36.35 ? 191 GLN   A CA  1 
ATOM   1506 C  C   . GLN   A 1 206 ? -34.672 35.726  -0.988  1   34.94 ? 191 GLN   A C   1 
ATOM   1507 O  O   . GLN   A 1 206 ? -35.527 36.408  -0.418  1   36.2  ? 191 GLN   A O   1 
ATOM   1508 C  CB  . GLN   A 1 206 ? -36.109 33.691  -0.417  1   37.92 ? 191 GLN   A CB  1 
ATOM   1509 C  CG  . GLN   A 1 206 ? -36.442 32.231  -0.749  1   41.78 ? 191 GLN   A CG  1 
ATOM   1510 C  CD  . GLN   A 1 206 ? -37.18  32.106  -2.069  1   49.39 ? 191 GLN   A CD  1 
ATOM   1511 O  OE1 . GLN   A 1 206 ? -37.843 33.043  -2.549  1   52.67 ? 191 GLN   A OE1 1 
ATOM   1512 N  NE2 . GLN   A 1 206 ? -37.094 30.942  -2.698  1   50.59 ? 191 GLN   A NE2 1 
ATOM   1513 N  N   . GLU   A 1 207 ? -33.552 36.249  -1.479  1   32.13 ? 192 GLU   A N   1 
ATOM   1514 C  CA  . GLU   A 1 207 ? -33.269 37.675  -1.488  1   30.79 ? 192 GLU   A CA  1 
ATOM   1515 C  C   . GLU   A 1 207 ? -33.498 38.196  -2.896  1   30.76 ? 192 GLU   A C   1 
ATOM   1516 O  O   . GLU   A 1 207 ? -32.569 38.262  -3.707  1   31.35 ? 192 GLU   A O   1 
ATOM   1517 C  CB  . GLU   A 1 207 ? -31.837 37.97   -1.002  1   32.95 ? 192 GLU   A CB  1 
ATOM   1518 C  CG  . GLU   A 1 207 ? -31.558 37.592  0.446   1   38.79 ? 192 GLU   A CG  1 
ATOM   1519 C  CD  . GLU   A 1 207 ? -32.002 38.623  1.473   1   50.54 ? 192 GLU   A CD  1 
ATOM   1520 O  OE1 . GLU   A 1 207 ? -32.327 39.768  1.076   1   50.84 ? 192 GLU   A OE1 1 
ATOM   1521 O  OE2 . GLU   A 1 207 ? -32.008 38.288  2.682   1   55    ? 192 GLU   A OE2 1 
ATOM   1522 N  N   . ARG   A 1 208 ? -34.749 38.594  -3.194  1   29.68 ? 193 ARG   A N   1 
ATOM   1523 C  CA  . ARG   A 1 208 ? -35.152 39.053  -4.524  1   28.29 ? 193 ARG   A CA  1 
ATOM   1524 C  C   . ARG   A 1 208 ? -34.369 40.274  -5.038  1   27.47 ? 193 ARG   A C   1 
ATOM   1525 O  O   . ARG   A 1 208 ? -33.951 40.281  -6.204  1   27.78 ? 193 ARG   A O   1 
ATOM   1526 C  CB  . ARG   A 1 208 ? -36.665 39.315  -4.569  1   27.98 ? 193 ARG   A CB  1 
ATOM   1527 C  CG  . ARG   A 1 208 ? -37.208 39.787  -5.911  1   28.11 ? 193 ARG   A CG  1 
ATOM   1528 C  CD  . ARG   A 1 208 ? -37.256 41.304  -6.03   1   28.31 ? 193 ARG   A CD  1 
ATOM   1529 N  NE  . ARG   A 1 208 ? -37.956 41.716  -7.243  1   27.89 ? 193 ARG   A NE  1 
ATOM   1530 C  CZ  . ARG   A 1 208 ? -37.993 42.96   -7.703  1   27.1  ? 193 ARG   A CZ  1 
ATOM   1531 N  NH1 . ARG   A 1 208 ? -37.361 43.931  -7.062  1   26.9  ? 193 ARG   A NH1 1 
ATOM   1532 N  NH2 . ARG   A 1 208 ? -38.678 43.245  -8.8    1   27.27 ? 193 ARG   A NH2 1 
ATOM   1533 N  N   . ASP   A 1 209 ? -34.211 41.305  -4.203  1   25.8  ? 194 ASP   A N   1 
ATOM   1534 C  CA  . ASP   A 1 209 ? -33.529 42.508  -4.641  1   25.82 ? 194 ASP   A CA  1 
ATOM   1535 C  C   . ASP   A 1 209 ? -32.047 42.246  -4.918  1   25.98 ? 194 ASP   A C   1 
ATOM   1536 O  O   . ASP   A 1 209 ? -31.503 42.812  -5.861  1   25.51 ? 194 ASP   A O   1 
ATOM   1537 C  CB  . ASP   A 1 209 ? -33.705 43.639  -3.635  1   26.64 ? 194 ASP   A CB  1 
ATOM   1538 C  CG  . ASP   A 1 209 ? -35.149 44.075  -3.452  1   29.81 ? 194 ASP   A CG  1 
ATOM   1539 O  OD1 . ASP   A 1 209 ? -35.966 43.878  -4.391  1   29.19 ? 194 ASP   A OD1 1 
ATOM   1540 O  OD2 . ASP   A 1 209 ? -35.463 44.614  -2.382  1   31.06 ? 194 ASP   A OD2 1 
ATOM   1541 N  N   . THR   A 1 210 ? -31.404 41.412  -4.081  1   26.86 ? 195 THR   A N   1 
ATOM   1542 C  CA  . THR   A 1 210 ? -29.995 41.041  -4.251  1   27.99 ? 195 THR   A CA  1 
ATOM   1543 C  C   . THR   A 1 210 ? -29.804 40.262  -5.554  1   26.89 ? 195 THR   A C   1 
ATOM   1544 O  O   . THR   A 1 210 ? -28.863 40.538  -6.307  1   27.14 ? 195 THR   A O   1 
ATOM   1545 C  CB  . THR   A 1 210 ? -29.52  40.208  -3.039  1   30.89 ? 195 THR   A CB  1 
ATOM   1546 O  OG1 . THR   A 1 210 ? -29.75  40.98   -1.853  1   32.25 ? 195 THR   A OG1 1 
ATOM   1547 C  CG2 . THR   A 1 210 ? -28.035 39.84   -3.138  1   31.13 ? 195 THR   A CG2 1 
ATOM   1548 N  N   . LEU   A 1 211 ? -30.717 39.322  -5.838  1   25.67 ? 196 LEU   A N   1 
ATOM   1549 C  CA  . LEU   A 1 211 ? -30.681 38.531  -7.058  1   25.1  ? 196 LEU   A CA  1 
ATOM   1550 C  C   . LEU   A 1 211 ? -30.827 39.411  -8.286  1   25.35 ? 196 LEU   A C   1 
ATOM   1551 O  O   . LEU   A 1 211 ? -30.047 39.281  -9.247  1   25.48 ? 196 LEU   A O   1 
ATOM   1552 C  CB  . LEU   A 1 211 ? -31.761 37.434  -7.052  1   25.07 ? 196 LEU   A CB  1 
ATOM   1553 C  CG  . LEU   A 1 211 ? -31.862 36.574  -8.318  1   26.06 ? 196 LEU   A CG  1 
ATOM   1554 C  CD1 . LEU   A 1 211 ? -30.513 35.888  -8.641  1   26.77 ? 196 LEU   A CD1 1 
ATOM   1555 C  CD2 . LEU   A 1 211 ? -32.942 35.5    -8.157  1   26.34 ? 196 LEU   A CD2 1 
ATOM   1556 N  N   . LEU   A 1 212 ? -31.762 40.349  -8.248  1   24.8  ? 197 LEU   A N   1 
ATOM   1557 C  CA  . LEU   A 1 212 ? -32.006 41.235  -9.386  1   26.12 ? 197 LEU   A CA  1 
ATOM   1558 C  C   . LEU   A 1 212 ? -30.766 42.082  -9.681  1   26.03 ? 197 LEU   A C   1 
ATOM   1559 O  O   . LEU   A 1 212 ? -30.363 42.237  -10.845 1   26.24 ? 197 LEU   A O   1 
ATOM   1560 C  CB  . LEU   A 1 212 ? -33.23  42.129  -9.072  1   27.24 ? 197 LEU   A CB  1 
ATOM   1561 C  CG  . LEU   A 1 212 ? -33.879 42.883  -10.239 1   28.92 ? 197 LEU   A CG  1 
ATOM   1562 C  CD1 . LEU   A 1 212 ? -35.331 43.214  -9.915  1   28.89 ? 197 LEU   A CD1 1 
ATOM   1563 C  CD2 . LEU   A 1 212 ? -33.166 44.183  -10.51  1   30.38 ? 197 LEU   A CD2 1 
ATOM   1564 N  N   . LYS   A 1 213 ? -30.171 42.632  -8.617  1   25.34 ? 198 LYS   A N   1 
ATOM   1565 C  CA  . LYS   A 1 213 ? -28.993 43.466  -8.736  1   25.59 ? 198 LYS   A CA  1 
ATOM   1566 C  C   . LYS   A 1 213 ? -27.805 42.626  -9.322  1   24.46 ? 198 LYS   A C   1 
ATOM   1567 O  O   . LYS   A 1 213 ? -27.094 43.103  -10.191 1   24.45 ? 198 LYS   A O   1 
ATOM   1568 C  CB  . LYS   A 1 213 ? -28.644 44.015  -7.358  1   28.98 ? 198 LYS   A CB  1 
ATOM   1569 C  CG  . LYS   A 1 213 ? -27.489 44.995  -7.384  1   37.04 ? 198 LYS   A CG  1 
ATOM   1570 C  CD  . LYS   A 1 213 ? -26.974 45.324  -5.986  1   44.08 ? 198 LYS   A CD  1 
ATOM   1571 C  CE  . LYS   A 1 213 ? -25.851 46.341  -6.05   1   49.59 ? 198 LYS   A CE  1 
ATOM   1572 N  NZ  . LYS   A 1 213 ? -24.962 46.262  -4.859  1   52.51 ? 198 LYS   A NZ  1 
ATOM   1573 N  N   . ALA   A 1 214 ? -27.634 41.404  -8.845  1   23.95 ? 199 ALA   A N   1 
ATOM   1574 C  CA  . ALA   A 1 214 ? -26.582 40.495  -9.313  1   24.94 ? 199 ALA   A CA  1 
ATOM   1575 C  C   . ALA   A 1 214 ? -26.755 40.182  -10.815 1   25.19 ? 199 ALA   A C   1 
ATOM   1576 O  O   . ALA   A 1 214 ? -25.777 40.308  -11.563 1   26.16 ? 199 ALA   A O   1 
ATOM   1577 C  CB  . ALA   A 1 214 ? -26.59  39.211  -8.494  1   25.3  ? 199 ALA   A CB  1 
ATOM   1578 N  N   . LEU   A 1 215 ? -27.993 39.834  -11.265 1   24.09 ? 200 LEU   A N   1 
ATOM   1579 C  CA  . LEU   A 1 215 ? -28.261 39.577  -12.681 1   23.54 ? 200 LEU   A CA  1 
ATOM   1580 C  C   . LEU   A 1 215 ? -27.94  40.806  -13.558 1   23.71 ? 200 LEU   A C   1 
ATOM   1581 O  O   . LEU   A 1 215 ? -27.332 40.657  -14.622 1   22.48 ? 200 LEU   A O   1 
ATOM   1582 C  CB  . LEU   A 1 215 ? -29.683 39.062  -12.901 1   23.1  ? 200 LEU   A CB  1 
ATOM   1583 C  CG  . LEU   A 1 215 ? -29.995 37.68   -12.281 1   23.96 ? 200 LEU   A CG  1 
ATOM   1584 C  CD1 . LEU   A 1 215 ? -31.49  37.342  -12.351 1   23.63 ? 200 LEU   A CD1 1 
ATOM   1585 C  CD2 . LEU   A 1 215 ? -29.199 36.566  -12.977 1   24.18 ? 200 LEU   A CD2 1 
ATOM   1586 N  N   . LEU   A 1 216 ? -28.306 42.026  -13.109 1   24.39 ? 201 LEU   A N   1 
ATOM   1587 C  CA  . LEU   A 1 216 ? -27.964 43.245  -13.865 1   25.21 ? 201 LEU   A CA  1 
ATOM   1588 C  C   . LEU   A 1 216 ? -26.446 43.474  -13.957 1   24.39 ? 201 LEU   A C   1 
ATOM   1589 O  O   . LEU   A 1 216 ? -25.957 44.031  -14.944 1   24.35 ? 201 LEU   A O   1 
ATOM   1590 C  CB  . LEU   A 1 216 ? -28.657 44.493  -13.26  1   26.16 ? 201 LEU   A CB  1 
ATOM   1591 C  CG  . LEU   A 1 216 ? -30.191 44.54   -13.41  1   27.97 ? 201 LEU   A CG  1 
ATOM   1592 C  CD1 . LEU   A 1 216 ? -30.779 45.804  -12.698 1   29.02 ? 201 LEU   A CD1 1 
ATOM   1593 C  CD2 . LEU   A 1 216 ? -30.605 44.491  -14.87  1   27.68 ? 201 LEU   A CD2 1 
ATOM   1594 N  N   . GLU   A 1 217 ? -25.711 43.091  -12.918 1   23.42 ? 202 GLU   A N   1 
ATOM   1595 C  CA  . GLU   A 1 217 ? -24.269 43.239  -12.9   1   24.02 ? 202 GLU   A CA  1 
ATOM   1596 C  C   . GLU   A 1 217 ? -23.633 42.247  -13.898 1   23.84 ? 202 GLU   A C   1 
ATOM   1597 O  O   . GLU   A 1 217 ? -22.726 42.634  -14.648 1   25.06 ? 202 GLU   A O   1 
ATOM   1598 C  CB  . GLU   A 1 217 ? -23.726 43.061  -11.48  1   26.52 ? 202 GLU   A CB  1 
ATOM   1599 C  CG  . GLU   A 1 217 ? -22.222 43.224  -11.34  1   33.76 ? 202 GLU   A CG  1 
ATOM   1600 C  CD  . GLU   A 1 217 ? -21.599 44.477  -11.933 1   46.16 ? 202 GLU   A CD  1 
ATOM   1601 O  OE1 . GLU   A 1 217 ? -22.263 45.539  -11.94  1   49.01 ? 202 GLU   A OE1 1 
ATOM   1602 O  OE2 . GLU   A 1 217 ? -20.427 44.397  -12.376 1   50.26 ? 202 GLU   A OE2 1 
ATOM   1603 N  N   . ILE   A 1 218 ? -24.174 41.031  -13.99  1   22.81 ? 203 ILE   A N   1 
ATOM   1604 C  CA  . ILE   A 1 218 ? -23.698 40.014  -14.938 1   23.07 ? 203 ILE   A CA  1 
ATOM   1605 C  C   . ILE   A 1 218 ? -23.966 40.519  -16.347 1   23.6  ? 203 ILE   A C   1 
ATOM   1606 O  O   . ILE   A 1 218 ? -23.054 40.515  -17.178 1   23.48 ? 203 ILE   A O   1 
ATOM   1607 C  CB  . ILE   A 1 218 ? -24.358 38.642  -14.671 1   23.24 ? 203 ILE   A CB  1 
ATOM   1608 C  CG1 . ILE   A 1 218 ? -23.817 38.033  -13.365 1   23.41 ? 203 ILE   A CG1 1 
ATOM   1609 C  CG2 . ILE   A 1 218 ? -24.153 37.682  -15.865 1   23.84 ? 203 ILE   A CG2 1 
ATOM   1610 C  CD1 . ILE   A 1 218 ? -24.623 36.837  -12.91  1   24.19 ? 203 ILE   A CD1 1 
ATOM   1611 N  N   . ALA   A 1 219 ? -25.182 41.041  -16.596 1   23.39 ? 204 ALA   A N   1 
ATOM   1612 C  CA  . ALA   A 1 219 ? -25.54  41.6    -17.893 1   24.14 ? 204 ALA   A CA  1 
ATOM   1613 C  C   . ALA   A 1 219 ? -24.563 42.735  -18.287 1   24.94 ? 204 ALA   A C   1 
ATOM   1614 O  O   . ALA   A 1 219 ? -24.058 42.743  -19.408 1   24.81 ? 204 ALA   A O   1 
ATOM   1615 C  CB  . ALA   A 1 219 ? -26.978 42.124  -17.868 1   23.88 ? 204 ALA   A CB  1 
ATOM   1616 N  N   . SER   A 1 220 ? -24.244 43.629  -17.346 1   24.82 ? 205 SER   A N   1 
ATOM   1617 C  CA  . SER   A 1 220 ? -23.31  44.726  -17.572 1   25.96 ? 205 SER   A CA  1 
ATOM   1618 C  C   . SER   A 1 220 ? -21.928 44.213  -18.016 1   25.1  ? 205 SER   A C   1 
ATOM   1619 O  O   . SER   A 1 220 ? -21.316 44.772  -18.924 1   24.54 ? 205 SER   A O   1 
ATOM   1620 C  CB  . SER   A 1 220 ? -23.162 45.559  -16.3   1   29.35 ? 205 SER   A CB  1 
ATOM   1621 O  OG  . SER   A 1 220 ? -22.316 46.671  -16.543 1   35.08 ? 205 SER   A OG  1 
ATOM   1622 N  N   . CYS   A 1 221 ? -21.438 43.148  -17.375 1   25.18 ? 206 CYS   A N   1 
ATOM   1623 C  CA  . CYS   A 1 221 ? -20.159 42.551  -17.711 1   24.77 ? 206 CYS   A CA  1 
ATOM   1624 C  C   . CYS   A 1 221 ? -20.157 41.988  -19.117 1   24.07 ? 206 CYS   A C   1 
ATOM   1625 O  O   . CYS   A 1 221 ? -19.191 42.208  -19.876 1   23.91 ? 206 CYS   A O   1 
ATOM   1626 C  CB  . CYS   A 1 221 ? -19.768 41.495  -16.689 1   26    ? 206 CYS   A CB  1 
ATOM   1627 S  SG  . CYS   A 1 221 ? -19.411 42.146  -15.047 1   30.73 ? 206 CYS   A SG  1 
ATOM   1628 N  N   . LEU   A 1 222 ? -21.206 41.241  -19.468 1   23.51 ? 207 LEU   A N   1 
ATOM   1629 C  CA  . LEU   A 1 222 ? -21.355 40.659  -20.8   1   23.42 ? 207 LEU   A CA  1 
ATOM   1630 C  C   . LEU   A 1 222 ? -21.53  41.724  -21.883 1   23.31 ? 207 LEU   A C   1 
ATOM   1631 O  O   . LEU   A 1 222 ? -21.031 41.551  -23.009 1   23.12 ? 207 LEU   A O   1 
ATOM   1632 C  CB  . LEU   A 1 222 ? -22.484 39.63   -20.81  1   23.33 ? 207 LEU   A CB  1 
ATOM   1633 C  CG  . LEU   A 1 222 ? -22.224 38.457  -19.885 1   25.37 ? 207 LEU   A CG  1 
ATOM   1634 C  CD1 . LEU   A 1 222 ? -23.488 37.6    -19.695 1   26.09 ? 207 LEU   A CD1 1 
ATOM   1635 C  CD2 . LEU   A 1 222 ? -21.103 37.582  -20.444 1   26.09 ? 207 LEU   A CD2 1 
ATOM   1636 N  N   . GLU   A 1 223 ? -22.176 42.856  -21.539 1   22.19 ? 208 GLU   A N   1 
ATOM   1637 C  CA  . GLU   A 1 223 ? -22.315 43.996  -22.44  1   23.59 ? 208 GLU   A CA  1 
ATOM   1638 C  C   . GLU   A 1 223 ? -20.941 44.629  -22.68  1   24.38 ? 208 GLU   A C   1 
ATOM   1639 O  O   . GLU   A 1 223 ? -20.613 44.938  -23.823 1   25.14 ? 208 GLU   A O   1 
ATOM   1640 C  CB  . GLU   A 1 223 ? -23.294 45.047  -21.857 1   24.79 ? 208 GLU   A CB  1 
ATOM   1641 C  CG  . GLU   A 1 223 ? -24.743 44.576  -21.896 1   30    ? 208 GLU   A CG  1 
ATOM   1642 C  CD  . GLU   A 1 223 ? -25.697 45.347  -20.998 1   34.57 ? 208 GLU   A CD  1 
ATOM   1643 O  OE1 . GLU   A 1 223 ? -25.268 46.345  -20.375 1   35.78 ? 208 GLU   A OE1 1 
ATOM   1644 O  OE2 . GLU   A 1 223 ? -26.876 44.942  -20.914 1   33.82 ? 208 GLU   A OE2 1 
ATOM   1645 N  N   . LYS   A 1 224 ? -20.112 44.769  -21.622 1   23.64 ? 209 LYS   A N   1 
ATOM   1646 C  CA  . LYS   A 1 224 ? -18.754 45.295  -21.766 1   24.34 ? 209 LYS   A CA  1 
ATOM   1647 C  C   . LYS   A 1 224 ? -17.901 44.337  -22.627 1   23.75 ? 209 LYS   A C   1 
ATOM   1648 O  O   . LYS   A 1 224 ? -17.133 44.807  -23.43  1   24.3  ? 209 LYS   A O   1 
ATOM   1649 C  CB  . LYS   A 1 224 ? -18.086 45.491  -20.389 1   27.98 ? 209 LYS   A CB  1 
ATOM   1650 C  CG  . LYS   A 1 224 ? -18.64  46.668  -19.592 1   35.02 ? 209 LYS   A CG  1 
ATOM   1651 C  CD  . LYS   A 1 224 ? -18.065 46.631  -18.155 1   43.42 ? 209 LYS   A CD  1 
ATOM   1652 C  CE  . LYS   A 1 224 ? -18.312 47.91   -17.379 1   50.35 ? 209 LYS   A CE  1 
ATOM   1653 N  NZ  . LYS   A 1 224 ? -19.723 48.37   -17.506 1   54.65 ? 209 LYS   A NZ  1 
ATOM   1654 N  N   . ALA   A 1 225 ? -18.076 43.012  -22.502 1   23.53 ? 210 ALA   A N   1 
ATOM   1655 C  CA  . ALA   A 1 225 ? -17.314 42.051  -23.316 1   23.98 ? 210 ALA   A CA  1 
ATOM   1656 C  C   . ALA   A 1 225 ? -17.554 42.27   -24.835 1   24.59 ? 210 ALA   A C   1 
ATOM   1657 O  O   . ALA   A 1 225 ? -16.623 42.12   -25.625 1   24.8  ? 210 ALA   A O   1 
ATOM   1658 C  CB  . ALA   A 1 225 ? -17.657 40.62   -22.916 1   23.01 ? 210 ALA   A CB  1 
ATOM   1659 N  N   . LEU   A 1 226 ? -18.763 42.679  -25.234 1   24.96 ? 211 LEU   A N   1 
ATOM   1660 C  CA  . LEU   A 1 226 ? -19.063 42.954  -26.643 1   24.52 ? 211 LEU   A CA  1 
ATOM   1661 C  C   . LEU   A 1 226 ? -18.265 44.156  -27.148 1   22.92 ? 211 LEU   A C   1 
ATOM   1662 O  O   . LEU   A 1 226 ? -17.698 44.109  -28.245 1   21.44 ? 211 LEU   A O   1 
ATOM   1663 C  CB  . LEU   A 1 226 ? -20.568 43.173  -26.843 1   25.37 ? 211 LEU   A CB  1 
ATOM   1664 C  CG  . LEU   A 1 226 ? -21.04  43.59   -28.239 1   27.26 ? 211 LEU   A CG  1 
ATOM   1665 C  CD1 . LEU   A 1 226 ? -20.673 42.549  -29.269 1   27.77 ? 211 LEU   A CD1 1 
ATOM   1666 C  CD2 . LEU   A 1 226 ? -22.555 43.806  -28.249 1   28.64 ? 211 LEU   A CD2 1 
ATOM   1667 N  N   . GLN   A 1 227 ? -18.133 45.2    -26.326 1   23.6  ? 212 GLN   A N   1 
ATOM   1668 C  CA  . GLN   A 1 227 ? -17.335 46.375  -26.722 1   24.05 ? 212 GLN   A CA  1 
ATOM   1669 C  C   . GLN   A 1 227 ? -15.88  45.995  -26.92  1   23.13 ? 212 GLN   A C   1 
ATOM   1670 O  O   . GLN   A 1 227 ? -15.257 46.438  -27.889 1   22.63 ? 212 GLN   A O   1 
ATOM   1671 C  CB  . GLN   A 1 227 ? -17.504 47.545  -25.724 1   26.85 ? 212 GLN   A CB  1 
ATOM   1672 C  CG  . GLN   A 1 227 ? -18.971 47.989  -25.574 1   32.26 ? 212 GLN   A CG  1 
ATOM   1673 C  CD  . GLN   A 1 227 ? -19.544 48.448  -26.9   1   38.01 ? 212 GLN   A CD  1 
ATOM   1674 O  OE1 . GLN   A 1 227 ? -18.977 49.311  -27.581 1   40.04 ? 212 GLN   A OE1 1 
ATOM   1675 N  NE2 . GLN   A 1 227 ? -20.65  47.84   -27.315 1   37.85 ? 212 GLN   A NE2 1 
ATOM   1676 N  N   . VAL   A 1 228 ? -15.353 45.098  -26.036 1   22.62 ? 213 VAL   A N   1 
ATOM   1677 C  CA  . VAL   A 1 228 ? -13.974 44.608  -26.132 1   22.28 ? 213 VAL   A CA  1 
ATOM   1678 C  C   . VAL   A 1 228 ? -13.758 43.86   -27.456 1   22.22 ? 213 VAL   A C   1 
ATOM   1679 O  O   . VAL   A 1 228 ? -12.736 44.048  -28.107 1   21.76 ? 213 VAL   A O   1 
ATOM   1680 C  CB  . VAL   A 1 228 ? -13.587 43.759  -24.897 1   22.91 ? 213 VAL   A CB  1 
ATOM   1681 C  CG1 . VAL   A 1 228 ? -12.261 43.036  -25.107 1   22.58 ? 213 VAL   A CG1 1 
ATOM   1682 C  CG2 . VAL   A 1 228 ? -13.533 44.62   -23.643 1   23.72 ? 213 VAL   A CG2 1 
ATOM   1683 N  N   . PHE   A 1 229 ? -14.761 43.081  -27.896 1   21.97 ? 214 PHE   A N   1 
ATOM   1684 C  CA  . PHE   A 1 229 ? -14.738 42.35   -29.167 1   23.74 ? 214 PHE   A CA  1 
ATOM   1685 C  C   . PHE   A 1 229 ? -14.475 43.24   -30.397 1   23.83 ? 214 PHE   A C   1 
ATOM   1686 O  O   . PHE   A 1 229 ? -13.877 42.771  -31.359 1   23.44 ? 214 PHE   A O   1 
ATOM   1687 C  CB  . PHE   A 1 229 ? -16.086 41.676  -29.377 1   24.57 ? 214 PHE   A CB  1 
ATOM   1688 C  CG  . PHE   A 1 229 ? -16.103 40.284  -29.951 1   26.65 ? 214 PHE   A CG  1 
ATOM   1689 C  CD1 . PHE   A 1 229 ? -15.411 39.985  -31.115 1   27.85 ? 214 PHE   A CD1 1 
ATOM   1690 C  CD2 . PHE   A 1 229 ? -16.89  39.305  -29.39  1   28.65 ? 214 PHE   A CD2 1 
ATOM   1691 C  CE1 . PHE   A 1 229 ? -15.5   38.722  -31.69  1   29.49 ? 214 PHE   A CE1 1 
ATOM   1692 C  CE2 . PHE   A 1 229 ? -16.949 38.034  -29.949 1   30.32 ? 214 PHE   A CE2 1 
ATOM   1693 C  CZ  . PHE   A 1 229 ? -16.296 37.768  -31.119 1   29.74 ? 214 PHE   A CZ  1 
ATOM   1694 N  N   . HIS   A 1 230 ? -14.985 44.48   -30.397 1   22.68 ? 215 HIS   A N   1 
ATOM   1695 C  CA  . HIS   A 1 230 ? -14.83  45.379  -31.547 1   23.87 ? 215 HIS   A CA  1 
ATOM   1696 C  C   . HIS   A 1 230 ? -13.374 45.581  -31.983 1   23    ? 215 HIS   A C   1 
ATOM   1697 O  O   . HIS   A 1 230 ? -13.144 45.829  -33.142 1   23.31 ? 215 HIS   A O   1 
ATOM   1698 C  CB  . HIS   A 1 230 ? -15.508 46.757  -31.284 1   25.37 ? 215 HIS   A CB  1 
ATOM   1699 C  CG  . HIS   A 1 230 ? -16.984 46.684  -31.04  1   30.97 ? 215 HIS   A CG  1 
ATOM   1700 N  ND1 . HIS   A 1 230 ? -17.709 47.819  -30.679 1   34.75 ? 215 HIS   A ND1 1 
ATOM   1701 C  CD2 . HIS   A 1 230 ? -17.839 45.629  -31.126 1   31.87 ? 215 HIS   A CD2 1 
ATOM   1702 C  CE1 . HIS   A 1 230 ? -18.964 47.412  -30.539 1   34.81 ? 215 HIS   A CE1 1 
ATOM   1703 N  NE2 . HIS   A 1 230 ? -19.09  46.101  -30.796 1   33.74 ? 215 HIS   A NE2 1 
ATOM   1704 N  N   . GLN   A 1 231 ? -12.39  45.431  -31.061 1   22.71 ? 216 GLN   A N   1 
ATOM   1705 C  CA  . GLN   A 1 231 ? -10.971 45.539  -31.356 1   22.88 ? 216 GLN   A CA  1 
ATOM   1706 C  C   . GLN   A 1 231 ? -10.473 44.528  -32.372 1   21.09 ? 216 GLN   A C   1 
ATOM   1707 O  O   . GLN   A 1 231 ? -9.417  44.736  -32.926 1   20.58 ? 216 GLN   A O   1 
ATOM   1708 C  CB  . GLN   A 1 231 ? -10.135 45.359  -30.082 1   26.18 ? 216 GLN   A CB  1 
ATOM   1709 C  CG  . GLN   A 1 231 ? -10.419 46.393  -29.039 1   30.27 ? 216 GLN   A CG  1 
ATOM   1710 C  CD  . GLN   A 1 231 ? -9.611  46.023  -27.825 1   33.51 ? 216 GLN   A CD  1 
ATOM   1711 O  OE1 . GLN   A 1 231 ? -8.405  46.256  -27.764 1   30.93 ? 216 GLN   A OE1 1 
ATOM   1712 N  NE2 . GLN   A 1 231 ? -10.267 45.403  -26.854 1   35.54 ? 216 GLN   A NE2 1 
ATOM   1713 N  N   . ILE   A 1 232 ? -11.222 43.423  -32.624 1   21.22 ? 217 ILE   A N   1 
ATOM   1714 C  CA  . ILE   A 1 232 ? -10.782 42.405  -33.6   1   20.01 ? 217 ILE   A CA  1 
ATOM   1715 C  C   . ILE   A 1 232 ? -10.404 43.007  -34.962 1   19.72 ? 217 ILE   A C   1 
ATOM   1716 O  O   . ILE   A 1 232 ? -9.425  42.586  -35.556 1   19.16 ? 217 ILE   A O   1 
ATOM   1717 C  CB  . ILE   A 1 232 ? -11.878 41.295  -33.749 1   19.52 ? 217 ILE   A CB  1 
ATOM   1718 C  CG1 . ILE   A 1 232 ? -11.301 39.983  -34.357 1   20.01 ? 217 ILE   A CG1 1 
ATOM   1719 C  CG2 . ILE   A 1 232 ? -13.12  41.781  -34.51  1   19.76 ? 217 ILE   A CG2 1 
ATOM   1720 C  CD1 . ILE   A 1 232 ? -10.274 39.253  -33.397 1   19.67 ? 217 ILE   A CD1 1 
ATOM   1721 N  N   . HIS   A 1 233 ? -11.173 44.029  -35.451 1   19.92 ? 218 HIS   A N   1 
ATOM   1722 C  CA  . HIS   A 1 233 ? -10.956 44.582  -36.791 1   19.51 ? 218 HIS   A CA  1 
ATOM   1723 C  C   . HIS   A 1 233 ? -9.607  45.262  -36.961 1   20.42 ? 218 HIS   A C   1 
ATOM   1724 O  O   . HIS   A 1 233 ? -9.023  45.177  -38.037 1   21.02 ? 218 HIS   A O   1 
ATOM   1725 C  CB  . HIS   A 1 233 ? -12.125 45.523  -37.223 1   17.91 ? 218 HIS   A CB  1 
ATOM   1726 C  CG  . HIS   A 1 233 ? -13.468 44.856  -37.096 1   18.74 ? 218 HIS   A CG  1 
ATOM   1727 N  ND1 . HIS   A 1 233 ? -13.927 43.971  -38.06  1   19.66 ? 218 HIS   A ND1 1 
ATOM   1728 C  CD2 . HIS   A 1 233 ? -14.377 44.926  -36.082 1   18.46 ? 218 HIS   A CD2 1 
ATOM   1729 C  CE1 . HIS   A 1 233 ? -15.108 43.553  -37.621 1   20.8  ? 218 HIS   A CE1 1 
ATOM   1730 N  NE2 . HIS   A 1 233 ? -15.409 44.102  -36.42  1   20.52 ? 218 HIS   A NE2 1 
ATOM   1731 N  N   . ASP   A 1 234 ? -9.096  45.904  -35.902 1   20.74 ? 219 ASP   A N   1 
ATOM   1732 C  CA  . ASP   A 1 234 ? -7.817  46.599  -35.956 1   21.12 ? 219 ASP   A CA  1 
ATOM   1733 C  C   . ASP   A 1 234 ? -6.593  45.662  -35.919 1   20.74 ? 219 ASP   A C   1 
ATOM   1734 O  O   . ASP   A 1 234 ? -5.494  46.091  -36.274 1   20.15 ? 219 ASP   A O   1 
ATOM   1735 C  CB  . ASP   A 1 234 ? -7.717  47.544  -34.755 1   23.66 ? 219 ASP   A CB  1 
ATOM   1736 C  CG  . ASP   A 1 234 ? -8.746  48.655  -34.816 1   29.04 ? 219 ASP   A CG  1 
ATOM   1737 O  OD1 . ASP   A 1 234 ? -9.05   49.118  -35.939 1   27.87 ? 219 ASP   A OD1 1 
ATOM   1738 O  OD2 . ASP   A 1 234 ? -9.281  49.032  -33.749 1   32.32 ? 219 ASP   A OD2 1 
ATOM   1739 N  N   . HIS   A 1 235 ? -6.77   44.394  -35.468 1   19.49 ? 220 HIS   A N   1 
ATOM   1740 C  CA  . HIS   A 1 235 ? -5.629  43.532  -35.255 1   18.61 ? 220 HIS   A CA  1 
ATOM   1741 C  C   . HIS   A 1 235 ? -5.613  42.223  -36.047 1   18.21 ? 220 HIS   A C   1 
ATOM   1742 O  O   . HIS   A 1 235 ? -4.663  41.457  -35.912 1   19.39 ? 220 HIS   A O   1 
ATOM   1743 C  CB  . HIS   A 1 235 ? -5.482  43.249  -33.757 1   19.44 ? 220 HIS   A CB  1 
ATOM   1744 C  CG  . HIS   A 1 235 ? -5.429  44.485  -32.924 1   20.88 ? 220 HIS   A CG  1 
ATOM   1745 N  ND1 . HIS   A 1 235 ? -4.424  45.442  -33.107 1   22.16 ? 220 HIS   A ND1 1 
ATOM   1746 C  CD2 . HIS   A 1 235 ? -6.276  44.912  -31.954 1   20.85 ? 220 HIS   A CD2 1 
ATOM   1747 C  CE1 . HIS   A 1 235 ? -4.718  46.428  -32.269 1   22.56 ? 220 HIS   A CE1 1 
ATOM   1748 N  NE2 . HIS   A 1 235 ? -5.806  46.146  -31.536 1   22.33 ? 220 HIS   A NE2 1 
ATOM   1749 N  N   . VAL   A 1 236 ? -6.642  41.945  -36.846 1   18.07 ? 221 VAL   A N   1 
ATOM   1750 C  CA  . VAL   A 1 236 ? -6.677  40.738  -37.661 1   19.79 ? 221 VAL   A CA  1 
ATOM   1751 C  C   . VAL   A 1 236 ? -7.176  41.123  -39.031 1   21.15 ? 221 VAL   A C   1 
ATOM   1752 O  O   . VAL   A 1 236 ? -8.124  41.907  -39.124 1   21.43 ? 221 VAL   A O   1 
ATOM   1753 C  CB  . VAL   A 1 236 ? -7.599  39.632  -37.047 1   20.07 ? 221 VAL   A CB  1 
ATOM   1754 C  CG1 . VAL   A 1 236 ? -7.5    38.33   -37.857 1   20.63 ? 221 VAL   A CG1 1 
ATOM   1755 C  CG2 . VAL   A 1 236 ? -7.252  39.373  -35.572 1   19.11 ? 221 VAL   A CG2 1 
ATOM   1756 N  N   . ASN   A 1 237 ? -6.546  40.616  -40.101 1   21.4  ? 222 ASN   A N   1 
ATOM   1757 C  CA  . ASN   A 1 237 ? -7.082  40.842  -41.441 1   23.53 ? 222 ASN   A CA  1 
ATOM   1758 C  C   . ASN   A 1 237 ? -7.556  39.529  -42.02  1   24.16 ? 222 ASN   A C   1 
ATOM   1759 O  O   . ASN   A 1 237 ? -6.935  38.482  -41.769 1   24.81 ? 222 ASN   A O   1 
ATOM   1760 C  CB  . ASN   A 1 237 ? -6.142  41.623  -42.366 1   26.2  ? 222 ASN   A CB  1 
ATOM   1761 C  CG  . ASN   A 1 237 ? -4.945  40.877  -42.806 1   30.19 ? 222 ASN   A CG  1 
ATOM   1762 O  OD1 . ASN   A 1 237 ? -3.893  40.971  -42.162 1   34.21 ? 222 ASN   A OD1 1 
ATOM   1763 N  ND2 . ASN   A 1 237 ? -5.066  40.147  -43.914 1   28.67 ? 222 ASN   A ND2 1 
ATOM   1764 N  N   . PRO   A 1 238 ? -8.669  39.554  -42.776 1   23.8  ? 223 PRO   A N   1 
ATOM   1765 C  CA  . PRO   A 1 238 ? -9.242  38.306  -43.291 1   23.13 ? 223 PRO   A CA  1 
ATOM   1766 C  C   . PRO   A 1 238 ? -8.326  37.454  -44.148 1   22.76 ? 223 PRO   A C   1 
ATOM   1767 O  O   . PRO   A 1 238 ? -8.29   36.236  -43.967 1   22.38 ? 223 PRO   A O   1 
ATOM   1768 C  CB  . PRO   A 1 238 ? -10.475 38.789  -44.075 1   23.7  ? 223 PRO   A CB  1 
ATOM   1769 C  CG  . PRO   A 1 238 ? -10.86  40.062  -43.392 1   24.33 ? 223 PRO   A CG  1 
ATOM   1770 C  CD  . PRO   A 1 238 ? -9.557  40.706  -43.068 1   23.46 ? 223 PRO   A CD  1 
ATOM   1771 N  N   . LYS   A 1 239 ? -7.574  38.075  -45.073 1   22.96 ? 224 LYS   A N   1 
ATOM   1772 C  CA  . LYS   A 1 239 ? -6.689  37.289  -45.945 1   22.89 ? 224 LYS   A CA  1 
ATOM   1773 C  C   . LYS   A 1 239 ? -5.635  36.505  -45.154 1   22.54 ? 224 LYS   A C   1 
ATOM   1774 O  O   . LYS   A 1 239 ? -5.44   35.304  -45.396 1   23.58 ? 224 LYS   A O   1 
ATOM   1775 C  CB  . LYS   A 1 239 ? -6.032  38.18   -47.008 1   26.2  ? 224 LYS   A CB  1 
ATOM   1776 C  CG  . LYS   A 1 239 ? -5.222  37.344  -48.037 1   31.58 ? 224 LYS   A CG  1 
ATOM   1777 N  N   . ALA   A 1 240 ? -4.959  37.162  -44.224 1   21.5  ? 225 ALA   A N   1 
ATOM   1778 C  CA  . ALA   A 1 240 ? -3.94   36.497  -43.41  1   21.2  ? 225 ALA   A CA  1 
ATOM   1779 C  C   . ALA   A 1 240 ? -4.58   35.439  -42.502 1   21.54 ? 225 ALA   A C   1 
ATOM   1780 O  O   . ALA   A 1 240 ? -4.03   34.337  -42.374 1   22.37 ? 225 ALA   A O   1 
ATOM   1781 C  CB  . ALA   A 1 240 ? -3.211  37.518  -42.574 1   21.38 ? 225 ALA   A CB  1 
ATOM   1782 N  N   . PHE   A 1 241 ? -5.717  35.762  -41.841 1   20.29 ? 226 PHE   A N   1 
ATOM   1783 C  CA  . PHE   A 1 241 ? -6.369  34.801  -40.944 1   19.94 ? 226 PHE   A CA  1 
ATOM   1784 C  C   . PHE   A 1 241 ? -6.723  33.503  -41.683 1   20.13 ? 226 PHE   A C   1 
ATOM   1785 O  O   . PHE   A 1 241 ? -6.317  32.399  -41.275 1   20.4  ? 226 PHE   A O   1 
ATOM   1786 C  CB  . PHE   A 1 241 ? -7.631  35.419  -40.273 1   19.65 ? 226 PHE   A CB  1 
ATOM   1787 C  CG  . PHE   A 1 241 ? -8.3    34.431  -39.342 1   19.59 ? 226 PHE   A CG  1 
ATOM   1788 C  CD1 . PHE   A 1 241 ? -7.79   34.196  -38.071 1   19.62 ? 226 PHE   A CD1 1 
ATOM   1789 C  CD2 . PHE   A 1 241 ? -9.357  33.647  -39.779 1   20.34 ? 226 PHE   A CD2 1 
ATOM   1790 C  CE1 . PHE   A 1 241 ? -8.373  33.254  -37.23  1   19.82 ? 226 PHE   A CE1 1 
ATOM   1791 C  CE2 . PHE   A 1 241 ? -9.937  32.691  -38.936 1   20.83 ? 226 PHE   A CE2 1 
ATOM   1792 C  CZ  . PHE   A 1 241 ? -9.419  32.492  -37.67  1   19.86 ? 226 PHE   A CZ  1 
ATOM   1793 N  N   . PHE   A 1 242 ? -7.431  33.627  -42.789 1   19.4  ? 227 PHE   A N   1 
ATOM   1794 C  CA  . PHE   A 1 242 ? -7.903  32.475  -43.536 1   20.85 ? 227 PHE   A CA  1 
ATOM   1795 C  C   . PHE   A 1 242 ? -6.803  31.749  -44.324 1   22.83 ? 227 PHE   A C   1 
ATOM   1796 O  O   . PHE   A 1 242 ? -6.816  30.523  -44.347 1   23.93 ? 227 PHE   A O   1 
ATOM   1797 C  CB  . PHE   A 1 242 ? -9.081  32.877  -44.468 1   21.07 ? 227 PHE   A CB  1 
ATOM   1798 C  CG  . PHE   A 1 242 ? -9.688  31.706  -45.206 1   21.85 ? 227 PHE   A CG  1 
ATOM   1799 C  CD1 . PHE   A 1 242 ? -10.598 30.866  -44.577 1   22.79 ? 227 PHE   A CD1 1 
ATOM   1800 C  CD2 . PHE   A 1 242 ? -9.292  31.4    -46.504 1   23.38 ? 227 PHE   A CD2 1 
ATOM   1801 C  CE1 . PHE   A 1 242 ? -11.141 29.774  -45.247 1   24.32 ? 227 PHE   A CE1 1 
ATOM   1802 C  CE2 . PHE   A 1 242 ? -9.814  30.287  -47.168 1   24.38 ? 227 PHE   A CE2 1 
ATOM   1803 C  CZ  . PHE   A 1 242 ? -10.717 29.474  -46.53  1   24.59 ? 227 PHE   A CZ  1 
ATOM   1804 N  N   . SER   A 1 243 ? -5.906  32.466  -45.011 1   23.78 ? 228 SER   A N   1 
ATOM   1805 C  CA  . SER   A 1 243 ? -4.885  31.765  -45.814 1   25.62 ? 228 SER   A CA  1 
ATOM   1806 C  C   . SER   A 1 243 ? -3.647  31.327  -44.995 1   26.78 ? 228 SER   A C   1 
ATOM   1807 O  O   . SER   A 1 243 ? -2.96   30.402  -45.406 1   28.05 ? 228 SER   A O   1 
ATOM   1808 C  CB  . SER   A 1 243 ? -4.466  32.605  -47.014 1   27.58 ? 228 SER   A CB  1 
ATOM   1809 O  OG  . SER   A 1 243 ? -3.842  33.794  -46.569 1   31.1  ? 228 SER   A OG  1 
ATOM   1810 N  N   . VAL   A 1 244 ? -3.349  31.991  -43.87  1   25.96 ? 229 VAL   A N   1 
ATOM   1811 C  CA  . VAL   A 1 244 ? -2.153  31.671  -43.091 1   25.4  ? 229 VAL   A CA  1 
ATOM   1812 C  C   . VAL   A 1 244 ? -2.477  31.021  -41.739 1   25.44 ? 229 VAL   A C   1 
ATOM   1813 O  O   . VAL   A 1 244 ? -2.164  29.845  -41.565 1   27.03 ? 229 VAL   A O   1 
ATOM   1814 C  CB  . VAL   A 1 244 ? -1.217  32.903  -42.947 1   26.33 ? 229 VAL   A CB  1 
ATOM   1815 C  CG1 . VAL   A 1 244 ? 0.044   32.545  -42.171 1   27.18 ? 229 VAL   A CG1 1 
ATOM   1816 C  CG2 . VAL   A 1 244 ? -0.875  33.513  -44.308 1   26.74 ? 229 VAL   A CG2 1 
ATOM   1817 N  N   . LEU   A 1 245 ? -3.113  31.745  -40.781 1   23.23 ? 230 LEU   A N   1 
ATOM   1818 C  CA  . LEU   A 1 245 ? -3.348  31.225  -39.445 1   21.7  ? 230 LEU   A CA  1 
ATOM   1819 C  C   . LEU   A 1 245 ? -4.176  29.95   -39.387 1   20.4  ? 230 LEU   A C   1 
ATOM   1820 O  O   . LEU   A 1 245 ? -3.871  29.058  -38.588 1   20    ? 230 LEU   A O   1 
ATOM   1821 C  CB  . LEU   A 1 245 ? -3.983  32.311  -38.54  1   21.27 ? 230 LEU   A CB  1 
ATOM   1822 C  CG  . LEU   A 1 245 ? -3.987  32.004  -37.03  1   22.1  ? 230 LEU   A CG  1 
ATOM   1823 C  CD1 . LEU   A 1 245 ? -2.597  31.587  -36.524 1   21.56 ? 230 LEU   A CD1 1 
ATOM   1824 C  CD2 . LEU   A 1 245 ? -4.488  33.214  -36.224 1   22.49 ? 230 LEU   A CD2 1 
ATOM   1825 N  N   . ARG   A 1 246 ? -5.241  29.874  -40.204 1   18.5  ? 231 ARG   A N   1 
ATOM   1826 C  CA  . ARG   A 1 246 ? -6.158  28.748  -40.264 1   20.05 ? 231 ARG   A CA  1 
ATOM   1827 C  C   . ARG   A 1 246 ? -5.45   27.371  -40.271 1   20.49 ? 231 ARG   A C   1 
ATOM   1828 O  O   . ARG   A 1 246 ? -5.87   26.458  -39.556 1   21.02 ? 231 ARG   A O   1 
ATOM   1829 C  CB  . ARG   A 1 246 ? -7.078  28.916  -41.485 1   21.98 ? 231 ARG   A CB  1 
ATOM   1830 C  CG  . ARG   A 1 246 ? -7.808  27.685  -41.936 1   27.45 ? 231 ARG   A CG  1 
ATOM   1831 C  CD  . ARG   A 1 246 ? -8.768  28.046  -43.029 1   33.22 ? 231 ARG   A CD  1 
ATOM   1832 N  NE  . ARG   A 1 246 ? -8.154  27.923  -44.339 1   39.48 ? 231 ARG   A NE  1 
ATOM   1833 C  CZ  . ARG   A 1 246 ? -8.422  26.947  -45.199 1   45.32 ? 231 ARG   A CZ  1 
ATOM   1834 N  NH1 . ARG   A 1 246 ? -7.839  26.928  -46.391 1   46.71 ? 231 ARG   A NH1 1 
ATOM   1835 N  NH2 . ARG   A 1 246 ? -9.305  25.998  -44.889 1   45.25 ? 231 ARG   A NH2 1 
ATOM   1836 N  N   . ILE   A 1 247 ? -4.397  27.234  -41.082 1   20.83 ? 232 ILE   A N   1 
ATOM   1837 C  CA  . ILE   A 1 247 ? -3.619  25.995  -41.203 1   22.91 ? 232 ILE   A CA  1 
ATOM   1838 C  C   . ILE   A 1 247 ? -3.184  25.454  -39.823 1   20.78 ? 232 ILE   A C   1 
ATOM   1839 O  O   . ILE   A 1 247 ? -3.391  24.293  -39.519 1   21.93 ? 232 ILE   A O   1 
ATOM   1840 C  CB  . ILE   A 1 247 ? -2.335  26.315  -42.065 1   25.99 ? 232 ILE   A CB  1 
ATOM   1841 C  CG1 . ILE   A 1 247 ? -2.668  26.704  -43.535 1   28.95 ? 232 ILE   A CG1 1 
ATOM   1842 C  CG2 . ILE   A 1 247 ? -1.295  25.177  -41.976 1   26.7  ? 232 ILE   A CG2 1 
ATOM   1843 C  CD1 . ILE   A 1 247 ? -4      26.072  -44.218 1   32.35 ? 232 ILE   A CD1 1 
ATOM   1844 N  N   . TYR   A 1 248 ? -2.621  26.324  -38.987 1   19    ? 233 TYR   A N   1 
ATOM   1845 C  CA  . TYR   A 1 248 ? -2.037  25.933  -37.706 1   19.03 ? 233 TYR   A CA  1 
ATOM   1846 C  C   . TYR   A 1 248 ? -3.08   25.746  -36.582 1   20.41 ? 233 TYR   A C   1 
ATOM   1847 O  O   . TYR   A 1 248 ? -2.73   25.23   -35.512 1   20.54 ? 233 TYR   A O   1 
ATOM   1848 C  CB  . TYR   A 1 248 ? -0.923  26.899  -37.321 1   18.18 ? 233 TYR   A CB  1 
ATOM   1849 C  CG  . TYR   A 1 248 ? 0.114   26.984  -38.433 1   18.61 ? 233 TYR   A CG  1 
ATOM   1850 C  CD1 . TYR   A 1 248 ? 1.06    25.981  -38.607 1   19.11 ? 233 TYR   A CD1 1 
ATOM   1851 C  CD2 . TYR   A 1 248 ? 0.038   27.973  -39.41  1   19.57 ? 233 TYR   A CD2 1 
ATOM   1852 C  CE1 . TYR   A 1 248 ? 1.928   25.979  -39.698 1   19.4  ? 233 TYR   A CE1 1 
ATOM   1853 C  CE2 . TYR   A 1 248 ? 0.919   27.997  -40.49  1   19.74 ? 233 TYR   A CE2 1 
ATOM   1854 C  CZ  . TYR   A 1 248 ? 1.872   27.006  -40.623 1   20.82 ? 233 TYR   A CZ  1 
ATOM   1855 O  OH  . TYR   A 1 248 ? 2.713   27.013  -41.722 1   22.83 ? 233 TYR   A OH  1 
ATOM   1856 N  N   . LEU   A 1 249 ? -4.333  26.18   -36.821 1   19.75 ? 234 LEU   A N   1 
ATOM   1857 C  CA  . LEU   A 1 249 ? -5.417  25.969  -35.85  1   20.05 ? 234 LEU   A CA  1 
ATOM   1858 C  C   . LEU   A 1 249 ? -6.034  24.554  -36.052 1   21.45 ? 234 LEU   A C   1 
ATOM   1859 O  O   . LEU   A 1 249 ? -6.799  24.109  -35.191 1   22.69 ? 234 LEU   A O   1 
ATOM   1860 C  CB  . LEU   A 1 249 ? -6.544  27.013  -36.049 1   20.9  ? 234 LEU   A CB  1 
ATOM   1861 C  CG  . LEU   A 1 249 ? -6.173  28.492  -35.942 1   22.3  ? 234 LEU   A CG  1 
ATOM   1862 C  CD1 . LEU   A 1 249 ? -7.4    29.383  -36.172 1   22.57 ? 234 LEU   A CD1 1 
ATOM   1863 C  CD2 . LEU   A 1 249 ? -5.46   28.817  -34.609 1   22.57 ? 234 LEU   A CD2 1 
ATOM   1864 N  N   . SER   A 1 250 ? -5.771  23.884  -37.196 1   21.35 ? 235 SER   A N   1 
ATOM   1865 C  CA  . SER   A 1 250 ? -6.383  22.592  -37.515 1   22.63 ? 235 SER   A CA  1 
ATOM   1866 C  C   . SER   A 1 250 ? -5.877  21.443  -36.687 1   21.33 ? 235 SER   A C   1 
ATOM   1867 O  O   . SER   A 1 250 ? -4.689  21.349  -36.482 1   21.35 ? 235 SER   A O   1 
ATOM   1868 C  CB  . SER   A 1 250 ? -6.133  22.232  -38.97  1   26.72 ? 235 SER   A CB  1 
ATOM   1869 O  OG  . SER   A 1 250 ? -6.89   23.124  -39.762 1   32.7  ? 235 SER   A OG  1 
ATOM   1870 N  N   . GLY   A 1 251 ? -6.777  20.535  -36.319 1   20.25 ? 236 GLY   A N   1 
ATOM   1871 C  CA  . GLY   A 1 251 ? -6.393  19.341  -35.584 1   20.69 ? 236 GLY   A CA  1 
ATOM   1872 C  C   . GLY   A 1 251 ? -6.471  18.11   -36.465 1   19.99 ? 236 GLY   A C   1 
ATOM   1873 O  O   . GLY   A 1 251 ? -6.413  18.194  -37.714 1   19.4  ? 236 GLY   A O   1 
ATOM   1874 N  N   . TRP   A 1 252 ? -6.558  16.947  -35.81  1   19.01 ? 237 TRP   A N   1 
ATOM   1875 C  CA  . TRP   A 1 252 ? -6.585  15.69   -36.538 1   19.52 ? 237 TRP   A CA  1 
ATOM   1876 C  C   . TRP   A 1 252 ? -7.696  14.798  -35.996 1   21.71 ? 237 TRP   A C   1 
ATOM   1877 O  O   . TRP   A 1 252 ? -7.413  13.737  -35.467 1   22.24 ? 237 TRP   A O   1 
ATOM   1878 C  CB  . TRP   A 1 252 ? -5.215  14.965  -36.517 1   17.83 ? 237 TRP   A CB  1 
ATOM   1879 C  CG  . TRP   A 1 252 ? -4.344  15.229  -35.316 1   16.48 ? 237 TRP   A CG  1 
ATOM   1880 C  CD1 . TRP   A 1 252 ? -4.239  14.477  -34.184 1   16.19 ? 237 TRP   A CD1 1 
ATOM   1881 C  CD2 . TRP   A 1 252 ? -3.448  16.343  -35.147 1   15.69 ? 237 TRP   A CD2 1 
ATOM   1882 N  NE1 . TRP   A 1 252 ? -3.299  15.026  -33.337 1   15.85 ? 237 TRP   A NE1 1 
ATOM   1883 C  CE2 . TRP   A 1 252 ? -2.799  16.173  -33.907 1   15.88 ? 237 TRP   A CE2 1 
ATOM   1884 C  CE3 . TRP   A 1 252 ? -3.095  17.44   -35.955 1   15.73 ? 237 TRP   A CE3 1 
ATOM   1885 C  CZ2 . TRP   A 1 252 ? -1.844  17.06   -33.444 1   16.89 ? 237 TRP   A CZ2 1 
ATOM   1886 C  CZ3 . TRP   A 1 252 ? -2.129  18.32   -35.487 1   16.59 ? 237 TRP   A CZ3 1 
ATOM   1887 C  CH2 . TRP   A 1 252 ? -1.53   18.14   -34.243 1   16.52 ? 237 TRP   A CH2 1 
ATOM   1888 N  N   . LYS   A 1 253 ? -8.95   15.246  -36.107 1   22.5  ? 238 LYS   A N   1 
ATOM   1889 C  CA  . LYS   A 1 253 ? -10.109 14.439  -35.732 1   23.59 ? 238 LYS   A CA  1 
ATOM   1890 C  C   . LYS   A 1 253 ? -11.122 14.715  -36.827 1   25.75 ? 238 LYS   A C   1 
ATOM   1891 O  O   . LYS   A 1 253 ? -11.573 15.854  -36.968 1   25.96 ? 238 LYS   A O   1 
ATOM   1892 C  CB  . LYS   A 1 253 ? -10.67  14.801  -34.365 1   23.26 ? 238 LYS   A CB  1 
ATOM   1893 C  CG  . LYS   A 1 253 ? -11.784 13.816  -33.91  1   25.9  ? 238 LYS   A CG  1 
ATOM   1894 C  CD  . LYS   A 1 253 ? -12.291 14.214  -32.544 1   30.13 ? 238 LYS   A CD  1 
ATOM   1895 C  CE  . LYS   A 1 253 ? -13.572 13.503  -32.17  1   35.84 ? 238 LYS   A CE  1 
ATOM   1896 N  NZ  . LYS   A 1 253 ? -13.28  12.114  -31.785 1   39.02 ? 238 LYS   A NZ  1 
ATOM   1897 N  N   . GLY   A 1 254 ? -11.402 13.705  -37.65  1   26.62 ? 239 GLY   A N   1 
ATOM   1898 C  CA  . GLY   A 1 254 ? -12.277 13.886  -38.81  1   27.93 ? 239 GLY   A CA  1 
ATOM   1899 C  C   . GLY   A 1 254 ? -11.598 14.734  -39.883 1   28.61 ? 239 GLY   A C   1 
ATOM   1900 O  O   . GLY   A 1 254 ? -12.268 15.432  -40.658 1   28.16 ? 239 GLY   A O   1 
ATOM   1901 N  N   . ASN   A 1 255 ? -10.245 14.75   -39.89  1   29.28 ? 240 ASN   A N   1 
ATOM   1902 C  CA  . ASN   A 1 255 ? -9.506  15.545  -40.865 1   29.93 ? 240 ASN   A CA  1 
ATOM   1903 C  C   . ASN   A 1 255 ? -9.067  14.648  -42.002 1   31.42 ? 240 ASN   A C   1 
ATOM   1904 O  O   . ASN   A 1 255 ? -8.27   13.75   -41.771 1   31.38 ? 240 ASN   A O   1 
ATOM   1905 C  CB  . ASN   A 1 255 ? -8.293  16.226  -40.223 1   29.08 ? 240 ASN   A CB  1 
ATOM   1906 C  CG  . ASN   A 1 255 ? -7.731  17.328  -41.093 1   31.08 ? 240 ASN   A CG  1 
ATOM   1907 O  OD1 . ASN   A 1 255 ? -7.847  17.305  -42.32  1   32.46 ? 240 ASN   A OD1 1 
ATOM   1908 N  ND2 . ASN   A 1 255 ? -7.117  18.332  -40.477 1   29.04 ? 240 ASN   A ND2 1 
ATOM   1909 N  N   . PRO   A 1 256 ? -9.533  14.898  -43.247 1   32.94 ? 241 PRO   A N   1 
ATOM   1910 C  CA  . PRO   A 1 256 ? -9.115  14.042  -44.377 1   33.45 ? 241 PRO   A CA  1 
ATOM   1911 C  C   . PRO   A 1 256 ? -7.602  14.04   -44.639 1   33.98 ? 241 PRO   A C   1 
ATOM   1912 O  O   . PRO   A 1 256 ? -7.092  13.083  -45.204 1   34.48 ? 241 PRO   A O   1 
ATOM   1913 C  CB  . PRO   A 1 256 ? -9.894  14.615  -45.574 1   34.06 ? 241 PRO   A CB  1 
ATOM   1914 C  CG  . PRO   A 1 256 ? -11.018 15.368  -44.986 1   34.69 ? 241 PRO   A CG  1 
ATOM   1915 C  CD  . PRO   A 1 256 ? -10.501 15.921  -43.678 1   32.85 ? 241 PRO   A CD  1 
ATOM   1916 N  N   . GLN   A 1 257 ? -6.881  15.083  -44.204 1   33.51 ? 242 GLN   A N   1 
ATOM   1917 C  CA  . GLN   A 1 257 ? -5.425  15.124  -44.374 1   33.35 ? 242 GLN   A CA  1 
ATOM   1918 C  C   . GLN   A 1 257 ? -4.689  14.163  -43.414 1   33.14 ? 242 GLN   A C   1 
ATOM   1919 O  O   . GLN   A 1 257 ? -3.564  13.785  -43.702 1   33.26 ? 242 GLN   A O   1 
ATOM   1920 C  CB  . GLN   A 1 257 ? -4.883  16.554  -44.238 1   34.58 ? 242 GLN   A CB  1 
ATOM   1921 C  CG  . GLN   A 1 257 ? -5.382  17.484  -45.33  1   37.44 ? 242 GLN   A CG  1 
ATOM   1922 C  CD  . GLN   A 1 257 ? -4.621  18.793  -45.323 1   40.68 ? 242 GLN   A CD  1 
ATOM   1923 O  OE1 . GLN   A 1 257 ? -5.089  19.812  -44.79  1   42.3  ? 242 GLN   A OE1 1 
ATOM   1924 N  NE2 . GLN   A 1 257 ? -3.445  18.793  -45.917 1   40.11 ? 242 GLN   A NE2 1 
ATOM   1925 N  N   . LEU   A 1 258 ? -5.32   13.773  -42.288 1   33.11 ? 243 LEU   A N   1 
ATOM   1926 C  CA  . LEU   A 1 258 ? -4.792  12.808  -41.306 1   33.02 ? 243 LEU   A CA  1 
ATOM   1927 C  C   . LEU   A 1 258 ? -5.994  11.986  -40.83  1   32.74 ? 243 LEU   A C   1 
ATOM   1928 O  O   . LEU   A 1 258 ? -6.383  12.041  -39.653 1   32.8  ? 243 LEU   A O   1 
ATOM   1929 C  CB  . LEU   A 1 258 ? -4.14   13.49   -40.092 1   33.48 ? 243 LEU   A CB  1 
ATOM   1930 C  CG  . LEU   A 1 258 ? -2.759  14.018  -40.222 1   36.24 ? 243 LEU   A CG  1 
ATOM   1931 C  CD1 . LEU   A 1 258 ? -2.82   15.412  -40.66  1   37.66 ? 243 LEU   A CD1 1 
ATOM   1932 C  CD2 . LEU   A 1 258 ? -2.045  13.982  -38.865 1   36.72 ? 243 LEU   A CD2 1 
ATOM   1933 N  N   . SER   A 1 259 ? -6.615  11.227  -41.756 1   32.29 ? 244 SER   A N   1 
ATOM   1934 C  CA  . SER   A 1 259 ? -7.837  10.475  -41.477 1   32.16 ? 244 SER   A CA  1 
ATOM   1935 C  C   . SER   A 1 259 ? -7.771  9.502   -40.295 1   31.77 ? 244 SER   A C   1 
ATOM   1936 O  O   . SER   A 1 259 ? -8.81   9.241   -39.704 1   32.59 ? 244 SER   A O   1 
ATOM   1937 C  CB  . SER   A 1 259 ? -8.321  9.743   -42.723 1   34.21 ? 244 SER   A CB  1 
ATOM   1938 O  OG  . SER   A 1 259 ? -7.34   8.832   -43.189 1   37.15 ? 244 SER   A OG  1 
ATOM   1939 N  N   . ASP   A 1 260 ? -6.589  8.978   -39.93  1   30.79 ? 245 ASP   A N   1 
ATOM   1940 C  CA  . ASP   A 1 260 ? -6.494  8.081   -38.761 1   30.39 ? 245 ASP   A CA  1 
ATOM   1941 C  C   . ASP   A 1 260 ? -5.962  8.765   -37.487 1   28.27 ? 245 ASP   A C   1 
ATOM   1942 O  O   . ASP   A 1 260 ? -5.898  8.138   -36.431 1   27.55 ? 245 ASP   A O   1 
ATOM   1943 C  CB  . ASP   A 1 260 ? -5.586  6.877   -39.097 1   33.2  ? 245 ASP   A CB  1 
ATOM   1944 C  CG  . ASP   A 1 260 ? -6.119  6.126   -40.296 1   38.66 ? 245 ASP   A CG  1 
ATOM   1945 O  OD1 . ASP   A 1 260 ? -7.29   5.706   -40.251 1   39.88 ? 245 ASP   A OD1 1 
ATOM   1946 O  OD2 . ASP   A 1 260 ? -5.379  6.006   -41.298 1   41.08 ? 245 ASP   A OD2 1 
ATOM   1947 N  N   . GLY   A 1 261 ? -5.578  10.034  -37.597 1   26.47 ? 246 GLY   A N   1 
ATOM   1948 C  CA  . GLY   A 1 261 ? -4.984  10.744  -36.487 1   25.06 ? 246 GLY   A CA  1 
ATOM   1949 C  C   . GLY   A 1 261 ? -3.481  10.789  -36.618 1   24.13 ? 246 GLY   A C   1 
ATOM   1950 O  O   . GLY   A 1 261 ? -2.905  10.57   -37.697 1   24.3  ? 246 GLY   A O   1 
ATOM   1951 N  N   . LEU   A 1 262 ? -2.822  11.101  -35.509 1   22.92 ? 247 LEU   A N   1 
ATOM   1952 C  CA  . LEU   A 1 262 ? -1.391  11.284  -35.499 1   21.42 ? 247 LEU   A CA  1 
ATOM   1953 C  C   . LEU   A 1 262 ? -0.706  10.192  -34.687 1   20.5  ? 247 LEU   A C   1 
ATOM   1954 O  O   . LEU   A 1 262 ? -1.222  9.824   -33.632 1   20.82 ? 247 LEU   A O   1 
ATOM   1955 C  CB  . LEU   A 1 262 ? -1.114  12.652  -34.85  1   20.59 ? 247 LEU   A CB  1 
ATOM   1956 C  CG  . LEU   A 1 262 ? 0.336   13.12   -34.866 1   21.08 ? 247 LEU   A CG  1 
ATOM   1957 C  CD1 . LEU   A 1 262 ? 0.835   13.381  -36.28  1   20.82 ? 247 LEU   A CD1 1 
ATOM   1958 C  CD2 . LEU   A 1 262 ? 0.505   14.373  -34.007 1   20.5  ? 247 LEU   A CD2 1 
ATOM   1959 N  N   . VAL   A 1 263 ? 0.444   9.693   -35.164 1   19.69 ? 248 VAL   A N   1 
ATOM   1960 C  CA  . VAL   A 1 263 ? 1.204   8.727   -34.376 1   20.34 ? 248 VAL   A CA  1 
ATOM   1961 C  C   . VAL   A 1 263 ? 2.097   9.487   -33.407 1   19.14 ? 248 VAL   A C   1 
ATOM   1962 O  O   . VAL   A 1 263 ? 2.947   10.266  -33.839 1   20.49 ? 248 VAL   A O   1 
ATOM   1963 C  CB  . VAL   A 1 263 ? 2.054   7.753   -35.255 1   21.77 ? 248 VAL   A CB  1 
ATOM   1964 C  CG1 . VAL   A 1 263 ? 2.834   6.782   -34.374 1   21.9  ? 248 VAL   A CG1 1 
ATOM   1965 C  CG2 . VAL   A 1 263 ? 1.165   6.999   -36.237 1   22.82 ? 248 VAL   A CG2 1 
ATOM   1966 N  N   . TYR   A 1 264 ? 1.928   9.264   -32.099 1   17.72 ? 249 TYR   A N   1 
ATOM   1967 C  CA  . TYR   A 1 264 ? 2.8     9.858   -31.083 1   18.37 ? 249 TYR   A CA  1 
ATOM   1968 C  C   . TYR   A 1 264 ? 3.856   8.796   -30.808 1   19.14 ? 249 TYR   A C   1 
ATOM   1969 O  O   . TYR   A 1 264 ? 3.68    7.94    -29.94  1   18.63 ? 249 TYR   A O   1 
ATOM   1970 C  CB  . TYR   A 1 264 ? 1.992   10.181  -29.804 1   18.37 ? 249 TYR   A CB  1 
ATOM   1971 C  CG  . TYR   A 1 264 ? 1.001   11.307  -30.049 1   18.39 ? 249 TYR   A CG  1 
ATOM   1972 C  CD1 . TYR   A 1 264 ? -0.212  11.065  -30.679 1   18.94 ? 249 TYR   A CD1 1 
ATOM   1973 C  CD2 . TYR   A 1 264 ? 1.315   12.619  -29.727 1   18.61 ? 249 TYR   A CD2 1 
ATOM   1974 C  CE1 . TYR   A 1 264 ? -1.113  12.096  -30.939 1   19.54 ? 249 TYR   A CE1 1 
ATOM   1975 C  CE2 . TYR   A 1 264 ? 0.424   13.662  -29.994 1   18.96 ? 249 TYR   A CE2 1 
ATOM   1976 C  CZ  . TYR   A 1 264 ? -0.789  13.393  -30.599 1   19.53 ? 249 TYR   A CZ  1 
ATOM   1977 O  OH  . TYR   A 1 264 ? -1.699  14.408  -30.852 1   21.64 ? 249 TYR   A OH  1 
ATOM   1978 N  N   . GLU   A 1 265 ? 4.925   8.819   -31.615 1   18.6  ? 250 GLU   A N   1 
ATOM   1979 C  CA  . GLU   A 1 265 ? 5.955   7.789   -31.612 1   18.66 ? 250 GLU   A CA  1 
ATOM   1980 C  C   . GLU   A 1 265 ? 6.571   7.574   -30.267 1   19.1  ? 250 GLU   A C   1 
ATOM   1981 O  O   . GLU   A 1 265 ? 6.924   8.532   -29.592 1   19.11 ? 250 GLU   A O   1 
ATOM   1982 C  CB  . GLU   A 1 265 ? 7.025   8.169   -32.647 1   19.6  ? 250 GLU   A CB  1 
ATOM   1983 C  CG  . GLU   A 1 265 ? 8.112   7.111   -32.796 1   22.21 ? 250 GLU   A CG  1 
ATOM   1984 C  CD  . GLU   A 1 265 ? 9.118   7.579   -33.822 1   24.72 ? 250 GLU   A CD  1 
ATOM   1985 O  OE1 . GLU   A 1 265 ? 9.88    8.519   -33.507 1   23.38 ? 250 GLU   A OE1 1 
ATOM   1986 O  OE2 . GLU   A 1 265 ? 9.127   7.027   -34.943 1   28.24 ? 250 GLU   A OE2 1 
ATOM   1987 N  N   . GLY   A 1 266 ? 6.637   6.31    -29.838 1   20.11 ? 251 GLY   A N   1 
ATOM   1988 C  CA  . GLY   A 1 266 ? 7.199   6.002   -28.531 1   20.69 ? 251 GLY   A CA  1 
ATOM   1989 C  C   . GLY   A 1 266 ? 6.203   6.099   -27.383 1   21.43 ? 251 GLY   A C   1 
ATOM   1990 O  O   . GLY   A 1 266 ? 6.531   5.727   -26.247 1   21.95 ? 251 GLY   A O   1 
ATOM   1991 N  N   . PHE   A 1 267 ? 4.982   6.616   -27.641 1   20.85 ? 252 PHE   A N   1 
ATOM   1992 C  CA  . PHE   A 1 267 ? 3.997   6.744   -26.542 1   21.21 ? 252 PHE   A CA  1 
ATOM   1993 C  C   . PHE   A 1 267 ? 2.829   5.822   -26.765 1   21.45 ? 252 PHE   A C   1 
ATOM   1994 O  O   . PHE   A 1 267 ? 2.468   5.083   -25.86  1   21.67 ? 252 PHE   A O   1 
ATOM   1995 C  CB  . PHE   A 1 267 ? 3.543   8.209   -26.309 1   20.81 ? 252 PHE   A CB  1 
ATOM   1996 C  CG  . PHE   A 1 267 ? 2.989   8.41    -24.915 1   20.95 ? 252 PHE   A CG  1 
ATOM   1997 C  CD1 . PHE   A 1 267 ? 3.835   8.664   -23.845 1   21.69 ? 252 PHE   A CD1 1 
ATOM   1998 C  CD2 . PHE   A 1 267 ? 1.624   8.317   -24.671 1   21.25 ? 252 PHE   A CD2 1 
ATOM   1999 C  CE1 . PHE   A 1 267 ? 3.322   8.837   -22.561 1   22.33 ? 252 PHE   A CE1 1 
ATOM   2000 C  CE2 . PHE   A 1 267 ? 1.11    8.519   -23.391 1   21.42 ? 252 PHE   A CE2 1 
ATOM   2001 C  CZ  . PHE   A 1 267 ? 1.967   8.759   -22.344 1   21.83 ? 252 PHE   A CZ  1 
ATOM   2002 N  N   . TRP   A 1 268 ? 2.19    5.891   -27.944 1   21.54 ? 253 TRP   A N   1 
ATOM   2003 C  CA  . TRP   A 1 268 ? 1.065   5.022   -28.249 1   22.83 ? 253 TRP   A CA  1 
ATOM   2004 C  C   . TRP   A 1 268 ? 1.359   4.26    -29.519 1   24.76 ? 253 TRP   A C   1 
ATOM   2005 O  O   . TRP   A 1 268 ? 1.99    4.789   -30.434 1   24.49 ? 253 TRP   A O   1 
ATOM   2006 C  CB  . TRP   A 1 268 ? -0.228  5.819   -28.461 1   22.81 ? 253 TRP   A CB  1 
ATOM   2007 C  CG  . TRP   A 1 268 ? -0.818  6.39    -27.215 1   23.87 ? 253 TRP   A CG  1 
ATOM   2008 C  CD1 . TRP   A 1 268 ? -1.22   5.707   -26.099 1   24.92 ? 253 TRP   A CD1 1 
ATOM   2009 C  CD2 . TRP   A 1 268 ? -1.167  7.764   -26.999 1   23.94 ? 253 TRP   A CD2 1 
ATOM   2010 N  NE1 . TRP   A 1 268 ? -1.789  6.576   -25.193 1   25.34 ? 253 TRP   A NE1 1 
ATOM   2011 C  CE2 . TRP   A 1 268 ? -1.753  7.851   -25.714 1   24.99 ? 253 TRP   A CE2 1 
ATOM   2012 C  CE3 . TRP   A 1 268 ? -1.015  8.93    -27.754 1   23.72 ? 253 TRP   A CE3 1 
ATOM   2013 C  CZ2 . TRP   A 1 268 ? -2.202  9.066   -25.18  1   25.7  ? 253 TRP   A CZ2 1 
ATOM   2014 C  CZ3 . TRP   A 1 268 ? -1.493  10.122  -27.239 1   24.99 ? 253 TRP   A CZ3 1 
ATOM   2015 C  CH2 . TRP   A 1 268 ? -2.065  10.188  -25.963 1   24.97 ? 253 TRP   A CH2 1 
ATOM   2016 N  N   . GLU   A 1 269 ? 0.865   3.022   -29.567 1   26.05 ? 254 GLU   A N   1 
ATOM   2017 C  CA  . GLU   A 1 269 ? 1       2.092   -30.675 1   27.99 ? 254 GLU   A CA  1 
ATOM   2018 C  C   . GLU   A 1 269 ? 0.238   2.585   -31.923 1   28.99 ? 254 GLU   A C   1 
ATOM   2019 O  O   . GLU   A 1 269 ? 0.803   2.64    -33.018 1   31.47 ? 254 GLU   A O   1 
ATOM   2020 C  CB  . GLU   A 1 269 ? 0.45    0.721   -30.184 1   30.37 ? 254 GLU   A CB  1 
ATOM   2021 C  CG  . GLU   A 1 269 ? 0.083   -0.271  -31.28  1   32.96 ? 254 GLU   A CG  1 
ATOM   2022 C  CD  . GLU   A 1 269 ? 1.28    -1.061  -31.786 1   34.4  ? 254 GLU   A CD  1 
ATOM   2023 O  OE1 . GLU   A 1 269 ? 2.312   -1.112  -31.074 1   29.25 ? 254 GLU   A OE1 1 
ATOM   2024 O  OE2 . GLU   A 1 269 ? 1.175   -1.638  -32.894 1   34.33 ? 254 GLU   A OE2 1 
ATOM   2025 N  N   . ASP   A 1 270 ? -1.033  2.941   -31.76  1   27.28 ? 255 ASP   A N   1 
ATOM   2026 C  CA  . ASP   A 1 270 ? -1.887  3.339   -32.887 1   26.49 ? 255 ASP   A CA  1 
ATOM   2027 C  C   . ASP   A 1 270 ? -1.968  4.876   -33.026 1   24.87 ? 255 ASP   A C   1 
ATOM   2028 O  O   . ASP   A 1 270 ? -1.799  5.58    -32.039 1   23.73 ? 255 ASP   A O   1 
ATOM   2029 C  CB  . ASP   A 1 270 ? -3.3    2.767   -32.679 1   28.44 ? 255 ASP   A CB  1 
ATOM   2030 C  CG  . ASP   A 1 270 ? -3.334  1.255   -32.524 1   34.63 ? 255 ASP   A CG  1 
ATOM   2031 O  OD1 . ASP   A 1 270 ? -2.794  0.569   -33.392 1   34.44 ? 255 ASP   A OD1 1 
ATOM   2032 O  OD2 . ASP   A 1 270 ? -3.911  0.775   -31.528 1   38.1  ? 255 ASP   A OD2 1 
ATOM   2033 N  N   . PRO   A 1 271 ? -2.281  5.401   -34.224 1   24.97 ? 256 PRO   A N   1 
ATOM   2034 C  CA  . PRO   A 1 271 ? -2.486  6.864   -34.337 1   24.06 ? 256 PRO   A CA  1 
ATOM   2035 C  C   . PRO   A 1 271 ? -3.731  7.269   -33.528 1   23.06 ? 256 PRO   A C   1 
ATOM   2036 O  O   . PRO   A 1 271 ? -4.673  6.473   -33.367 1   22.51 ? 256 PRO   A O   1 
ATOM   2037 C  CB  . PRO   A 1 271 ? -2.657  7.088   -35.84  1   25.19 ? 256 PRO   A CB  1 
ATOM   2038 C  CG  . PRO   A 1 271 ? -3.119  5.773   -36.375 1   26.42 ? 256 PRO   A CG  1 
ATOM   2039 C  CD  . PRO   A 1 271 ? -2.541  4.707   -35.501 1   24.52 ? 256 PRO   A CD  1 
ATOM   2040 N  N   . LYS   A 1 272 ? -3.715  8.479   -32.962 1   21.48 ? 257 LYS   A N   1 
ATOM   2041 C  CA  . LYS   A 1 272 ? -4.803  8.972   -32.132 1   20.19 ? 257 LYS   A CA  1 
ATOM   2042 C  C   . LYS   A 1 272 ? -5.366  10.259  -32.72  1   20.7  ? 257 LYS   A C   1 
ATOM   2043 O  O   . LYS   A 1 272 ? -4.605  11.108  -33.212 1   20.76 ? 257 LYS   A O   1 
ATOM   2044 C  CB  . LYS   A 1 272 ? -4.303  9.267   -30.717 1   21.83 ? 257 LYS   A CB  1 
ATOM   2045 C  CG  . LYS   A 1 272 ? -3.664  8.082   -30.005 1   24.53 ? 257 LYS   A CG  1 
ATOM   2046 C  CD  . LYS   A 1 272 ? -4.675  6.998   -29.683 1   25.03 ? 257 LYS   A CD  1 
ATOM   2047 C  CE  . LYS   A 1 272 ? -3.996  5.779   -29.086 1   27.33 ? 257 LYS   A CE  1 
ATOM   2048 N  NZ  . LYS   A 1 272 ? -4.865  4.599   -29.215 1   28.9  ? 257 LYS   A NZ  1 
ATOM   2049 N  N   . GLU   A 1 273 ? -6.681  10.424  -32.619 1   20.06 ? 258 GLU   A N   1 
ATOM   2050 C  CA  . GLU   A 1 273 ? -7.343  11.611  -33.139 1   19.34 ? 258 GLU   A CA  1 
ATOM   2051 C  C   . GLU   A 1 273 ? -7.653  12.569  -32.012 1   19.12 ? 258 GLU   A C   1 
ATOM   2052 O  O   . GLU   A 1 273 ? -8.195  12.157  -30.986 1   19.25 ? 258 GLU   A O   1 
ATOM   2053 C  CB  . GLU   A 1 273 ? -8.654  11.232  -33.837 1   20.83 ? 258 GLU   A CB  1 
ATOM   2054 C  CG  . GLU   A 1 273 ? -8.456  10.545  -35.16  1   26.13 ? 258 GLU   A CG  1 
ATOM   2055 C  CD  . GLU   A 1 273 ? -9.772  10.392  -35.895 1   33.42 ? 258 GLU   A CD  1 
ATOM   2056 O  OE1 . GLU   A 1 273 ? -10.653 9.675   -35.371 1   38.12 ? 258 GLU   A OE1 1 
ATOM   2057 O  OE2 . GLU   A 1 273 ? -9.936  11.006  -36.971 1   34.38 ? 258 GLU   A OE2 1 
ATOM   2058 N  N   . PHE   A 1 274 ? -7.343  13.849  -32.208 1   17.69 ? 259 PHE   A N   1 
ATOM   2059 C  CA  . PHE   A 1 274 ? -7.702  14.893  -31.254 1   16.79 ? 259 PHE   A CA  1 
ATOM   2060 C  C   . PHE   A 1 274 ? -8.214  16.096  -32.058 1   16.86 ? 259 PHE   A C   1 
ATOM   2061 O  O   . PHE   A 1 274 ? -7.668  16.423  -33.128 1   16.91 ? 259 PHE   A O   1 
ATOM   2062 C  CB  . PHE   A 1 274 ? -6.518  15.296  -30.343 1   16.83 ? 259 PHE   A CB  1 
ATOM   2063 C  CG  . PHE   A 1 274 ? -6.042  14.187  -29.43  1   16.91 ? 259 PHE   A CG  1 
ATOM   2064 C  CD1 . PHE   A 1 274 ? -6.806  13.788  -28.339 1   18.23 ? 259 PHE   A CD1 1 
ATOM   2065 C  CD2 . PHE   A 1 274 ? -4.878  13.487  -29.709 1   17.39 ? 259 PHE   A CD2 1 
ATOM   2066 C  CE1 . PHE   A 1 274 ? -6.395  12.722  -27.523 1   19.48 ? 259 PHE   A CE1 1 
ATOM   2067 C  CE2 . PHE   A 1 274 ? -4.459  12.438  -28.881 1   18.8  ? 259 PHE   A CE2 1 
ATOM   2068 C  CZ  . PHE   A 1 274 ? -5.248  12.034  -27.817 1   18.14 ? 259 PHE   A CZ  1 
ATOM   2069 N  N   . ALA   A 1 275 ? -9.263  16.751  -31.554 1   16.2  ? 260 ALA   A N   1 
ATOM   2070 C  CA  . ALA   A 1 275 ? -9.816  17.922  -32.25  1   16.62 ? 260 ALA   A CA  1 
ATOM   2071 C  C   . ALA   A 1 275 ? -8.827  19.105  -32.07  1   16.04 ? 260 ALA   A C   1 
ATOM   2072 O  O   . ALA   A 1 275 ? -8.118  19.174  -31.063 1   16.05 ? 260 ALA   A O   1 
ATOM   2073 C  CB  . ALA   A 1 275 ? -11.179 18.297  -31.629 1   17.18 ? 260 ALA   A CB  1 
ATOM   2074 N  N   . GLY   A 1 276 ? -8.816  20.016  -33.035 1   16.2  ? 261 GLY   A N   1 
ATOM   2075 C  CA  . GLY   A 1 276 ? -7.979  21.209  -32.984 1   16.23 ? 261 GLY   A CA  1 
ATOM   2076 C  C   . GLY   A 1 276 ? -8.506  22.19   -31.942 1   15.74 ? 261 GLY   A C   1 
ATOM   2077 O  O   . GLY   A 1 276 ? -9.61   22.007  -31.384 1   15.25 ? 261 GLY   A O   1 
ATOM   2078 N  N   . GLY   A 1 277 ? -7.686  23.19   -31.576 1   15.03 ? 262 GLY   A N   1 
ATOM   2079 C  CA  . GLY   A 1 277 ? -8.087  24.145  -30.543 1   16.07 ? 262 GLY   A CA  1 
ATOM   2080 C  C   . GLY   A 1 277 ? -9.355  24.865  -30.931 1   16.12 ? 262 GLY   A C   1 
ATOM   2081 O  O   . GLY   A 1 277 ? -9.553  25.125  -32.112 1   17.11 ? 262 GLY   A O   1 
ATOM   2082 N  N   . SER   A 1 278 ? -10.24  25.152  -29.968 1   15.76 ? 263 SER   A N   1 
ATOM   2083 C  CA  . SER   A 1 278 ? -11.496 25.789  -30.277 1   17.29 ? 263 SER   A CA  1 
ATOM   2084 C  C   . SER   A 1 278 ? -11.948 26.705  -29.157 1   17    ? 263 SER   A C   1 
ATOM   2085 O  O   . SER   A 1 278 ? -11.763 26.346  -27.99  1   16.16 ? 263 SER   A O   1 
ATOM   2086 C  CB  . SER   A 1 278 ? -12.576 24.715  -30.468 1   20.15 ? 263 SER   A CB  1 
ATOM   2087 O  OG  . SER   A 1 278 ? -13.855 25.28   -30.722 1   23.04 ? 263 SER   A OG  1 
ATOM   2088 N  N   . ALA   A 1 279 ? -12.637 27.836  -29.497 1   15.24 ? 264 ALA   A N   1 
ATOM   2089 C  CA  . ALA   A 1 279 ? -13.214 28.646  -28.434 1   15.02 ? 264 ALA   A CA  1 
ATOM   2090 C  C   . ALA   A 1 279 ? -14.439 27.942  -27.818 1   15.87 ? 264 ALA   A C   1 
ATOM   2091 O  O   . ALA   A 1 279 ? -14.921 28.392  -26.796 1   17.11 ? 264 ALA   A O   1 
ATOM   2092 C  CB  . ALA   A 1 279 ? -13.538 30.049  -28.895 1   14.51 ? 264 ALA   A CB  1 
ATOM   2093 N  N   . GLY   A 1 280 ? -14.894 26.795  -28.375 1   15.47 ? 265 GLY   A N   1 
ATOM   2094 C  CA  . GLY   A 1 280 ? -15.84  25.93   -27.694 1   16.39 ? 265 GLY   A CA  1 
ATOM   2095 C  C   . GLY   A 1 280 ? -15.207 25.373  -26.414 1   16.66 ? 265 GLY   A C   1 
ATOM   2096 O  O   . GLY   A 1 280 ? -15.923 24.9    -25.532 1   18.3  ? 265 GLY   A O   1 
ATOM   2097 N  N   . GLN   A 1 281 ? -13.868 25.481  -26.267 1   15.92 ? 266 GLN   A N   1 
ATOM   2098 C  CA  . GLN   A 1 281 ? -13.135 25.106  -25.048 1   16.15 ? 266 GLN   A CA  1 
ATOM   2099 C  C   . GLN   A 1 281 ? -13.076 26.266  -24.044 1   17.54 ? 266 GLN   A C   1 
ATOM   2100 O  O   . GLN   A 1 281 ? -12.478 26.102  -22.98  1   18.38 ? 266 GLN   A O   1 
ATOM   2101 C  CB  . GLN   A 1 281 ? -11.709 24.598  -25.392 1   16.44 ? 266 GLN   A CB  1 
ATOM   2102 C  CG  . GLN   A 1 281 ? -11.741 23.425  -26.351 1   17.55 ? 266 GLN   A CG  1 
ATOM   2103 C  CD  . GLN   A 1 281 ? -10.448 23.226  -27.128 1   18.07 ? 266 GLN   A CD  1 
ATOM   2104 O  OE1 . GLN   A 1 281 ? -9.529  24.068  -27.127 1   18.68 ? 266 GLN   A OE1 1 
ATOM   2105 N  NE2 . GLN   A 1 281 ? -10.352 22.136  -27.863 1   16.43 ? 266 GLN   A NE2 1 
ATOM   2106 N  N   . SER   A 1 282 ? -13.632 27.452  -24.382 1   17.71 ? 267 SER   A N   1 
ATOM   2107 C  CA  . SER   A 1 282 ? -13.651 28.557  -23.433 1   18.11 ? 267 SER   A CA  1 
ATOM   2108 C  C   . SER   A 1 282 ? -14.64  28.188  -22.311 1   17.02 ? 267 SER   A C   1 
ATOM   2109 O  O   . SER   A 1 282 ? -15.814 27.939  -22.576 1   16.8  ? 267 SER   A O   1 
ATOM   2110 C  CB  . SER   A 1 282 ? -14.11  29.849  -24.101 1   19.44 ? 267 SER   A CB  1 
ATOM   2111 O  OG  . SER   A 1 282 ? -14.436 30.793  -23.093 1   21.51 ? 267 SER   A OG  1 
ATOM   2112 N  N   . SER   A 1 283 ? -14.161 28.187  -21.078 1   16.9  ? 268 SER   A N   1 
ATOM   2113 C  CA  . SER   A 1 283 ? -15.004 27.873  -19.933 1   17.96 ? 268 SER   A CA  1 
ATOM   2114 C  C   . SER   A 1 283 ? -15.892 29.06   -19.548 1   19.24 ? 268 SER   A C   1 
ATOM   2115 O  O   . SER   A 1 283 ? -16.914 28.827  -18.905 1   18.91 ? 268 SER   A O   1 
ATOM   2116 C  CB  . SER   A 1 283 ? -14.145 27.505  -18.72  1   19.71 ? 268 SER   A CB  1 
ATOM   2117 O  OG  . SER   A 1 283 ? -13.285 26.413  -19.001 1   20.33 ? 268 SER   A OG  1 
ATOM   2118 N  N   . VAL   A 1 284 ? -15.506 30.31   -19.866 1   18.71 ? 269 VAL   A N   1 
ATOM   2119 C  CA  . VAL   A 1 284 ? -16.324 31.457  -19.425 1   19.17 ? 269 VAL   A CA  1 
ATOM   2120 C  C   . VAL   A 1 284 ? -17.648 31.517  -20.205 1   20.2  ? 269 VAL   A C   1 
ATOM   2121 O  O   . VAL   A 1 284 ? -18.701 31.723  -19.586 1   20.23 ? 269 VAL   A O   1 
ATOM   2122 C  CB  . VAL   A 1 284 ? -15.572 32.801  -19.401 1   20.06 ? 269 VAL   A CB  1 
ATOM   2123 C  CG1 . VAL   A 1 284 ? -15.359 33.363  -20.817 1   19.55 ? 269 VAL   A CG1 1 
ATOM   2124 C  CG2 . VAL   A 1 284 ? -16.311 33.809  -18.505 1   21.55 ? 269 VAL   A CG2 1 
ATOM   2125 N  N   . PHE   A 1 285 ? -17.63  31.217  -21.507 1   20.96 ? 270 PHE   A N   1 
ATOM   2126 C  CA  . PHE   A 1 285 ? -18.887 31.208  -22.278 1   22.48 ? 270 PHE   A CA  1 
ATOM   2127 C  C   . PHE   A 1 285 ? -19.739 30.006  -21.907 1   22.95 ? 270 PHE   A C   1 
ATOM   2128 O  O   . PHE   A 1 285 ? -20.948 30.173  -21.708 1   23.88 ? 270 PHE   A O   1 
ATOM   2129 C  CB  . PHE   A 1 285 ? -18.65  31.309  -23.773 1   24.14 ? 270 PHE   A CB  1 
ATOM   2130 C  CG  . PHE   A 1 285 ? -18.223 32.706  -24.135 1   26.74 ? 270 PHE   A CG  1 
ATOM   2131 C  CD1 . PHE   A 1 285 ? -19.167 33.697  -24.373 1   28.96 ? 270 PHE   A CD1 1 
ATOM   2132 C  CD2 . PHE   A 1 285 ? -16.882 33.049  -24.177 1   27.37 ? 270 PHE   A CD2 1 
ATOM   2133 C  CE1 . PHE   A 1 285 ? -18.767 34.988  -24.682 1   30.3  ? 270 PHE   A CE1 1 
ATOM   2134 C  CE2 . PHE   A 1 285 ? -16.486 34.345  -24.483 1   28.68 ? 270 PHE   A CE2 1 
ATOM   2135 C  CZ  . PHE   A 1 285 ? -17.428 35.305  -24.725 1   29.8  ? 270 PHE   A CZ  1 
ATOM   2136 N  N   . GLN   A 1 286 ? -19.127 28.812  -21.711 1   21.4  ? 271 GLN   A N   1 
ATOM   2137 C  CA  . GLN   A 1 286 ? -19.928 27.653  -21.279 1   20.79 ? 271 GLN   A CA  1 
ATOM   2138 C  C   . GLN   A 1 286 ? -20.522 27.913  -19.878 1   21.96 ? 271 GLN   A C   1 
ATOM   2139 O  O   . GLN   A 1 286 ? -21.647 27.499  -19.593 1   21.48 ? 271 GLN   A O   1 
ATOM   2140 C  CB  . GLN   A 1 286 ? -19.1   26.353  -21.287 1   20.39 ? 271 GLN   A CB  1 
ATOM   2141 C  CG  . GLN   A 1 286 ? -18.647 25.913  -22.694 1   19.27 ? 271 GLN   A CG  1 
ATOM   2142 C  CD  . GLN   A 1 286 ? -18.753 24.425  -22.887 1   19.56 ? 271 GLN   A CD  1 
ATOM   2143 O  OE1 . GLN   A 1 286 ? -19.542 23.751  -22.228 1   22.29 ? 271 GLN   A OE1 1 
ATOM   2144 N  NE2 . GLN   A 1 286 ? -17.99  23.876  -23.823 1   15.49 ? 271 GLN   A NE2 1 
ATOM   2145 N  N   . CYS   A 1 287 ? -19.775 28.634  -19.03  1   21.95 ? 272 CYS   A N   1 
ATOM   2146 C  CA  . CYS   A 1 287 ? -20.147 28.987  -17.667 1   23.03 ? 272 CYS   A CA  1 
ATOM   2147 C  C   . CYS   A 1 287 ? -21.466 29.79   -17.609 1   22.54 ? 272 CYS   A C   1 
ATOM   2148 O  O   . CYS   A 1 287 ? -22.36  29.432  -16.839 1   21.96 ? 272 CYS   A O   1 
ATOM   2149 C  CB  . CYS   A 1 287 ? -18.984 29.716  -16.985 1   25.15 ? 272 CYS   A CB  1 
ATOM   2150 S  SG  . CYS   A 1 287 ? -19.433 30.708  -15.543 1   33.13 ? 272 CYS   A SG  1 
ATOM   2151 N  N   . PHE   A 1 288 ? -21.583 30.844  -18.403 1   22.52 ? 273 PHE   A N   1 
ATOM   2152 C  CA  . PHE   A 1 288 ? -22.791 31.662  -18.388 1   22.23 ? 273 PHE   A CA  1 
ATOM   2153 C  C   . PHE   A 1 288 ? -23.965 30.941  -19.07  1   21.09 ? 273 PHE   A C   1 
ATOM   2154 O  O   . PHE   A 1 288 ? -25.095 31.113  -18.607 1   20.99 ? 273 PHE   A O   1 
ATOM   2155 C  CB  . PHE   A 1 288 ? -22.532 33.086  -18.92  1   22.78 ? 273 PHE   A CB  1 
ATOM   2156 C  CG  . PHE   A 1 288 ? -21.72  33.796  -17.863 1   24.49 ? 273 PHE   A CG  1 
ATOM   2157 C  CD1 . PHE   A 1 288 ? -22.263 34.063  -16.614 1   26.06 ? 273 PHE   A CD1 1 
ATOM   2158 C  CD2 . PHE   A 1 288 ? -20.382 34.067  -18.066 1   25.38 ? 273 PHE   A CD2 1 
ATOM   2159 C  CE1 . PHE   A 1 288 ? -21.486 34.623  -15.606 1   27.27 ? 273 PHE   A CE1 1 
ATOM   2160 C  CE2 . PHE   A 1 288 ? -19.601 34.625  -17.056 1   26.47 ? 273 PHE   A CE2 1 
ATOM   2161 C  CZ  . PHE   A 1 288 ? -20.151 34.87   -15.826 1   27.14 ? 273 PHE   A CZ  1 
ATOM   2162 N  N   . ASP   A 1 289 ? -23.712 30.048  -20.06  1   20.37 ? 274 ASP   A N   1 
ATOM   2163 C  CA  . ASP   A 1 289 ? -24.816 29.262  -20.627 1   21.44 ? 274 ASP   A CA  1 
ATOM   2164 C  C   . ASP   A 1 289 ? -25.365 28.31   -19.548 1   22.54 ? 274 ASP   A C   1 
ATOM   2165 O  O   . ASP   A 1 289 ? -26.591 28.164  -19.436 1   22.56 ? 274 ASP   A O   1 
ATOM   2166 C  CB  . ASP   A 1 289 ? -24.391 28.462  -21.834 1   23.94 ? 274 ASP   A CB  1 
ATOM   2167 C  CG  . ASP   A 1 289 ? -24.245 29.289  -23.096 1   31.35 ? 274 ASP   A CG  1 
ATOM   2168 O  OD1 . ASP   A 1 289 ? -24.944 30.309  -23.22  1   30.95 ? 274 ASP   A OD1 1 
ATOM   2169 O  OD2 . ASP   A 1 289 ? -23.445 28.894  -23.976 1   35.12 ? 274 ASP   A OD2 1 
ATOM   2170 N  N   . VAL   A 1 290 ? -24.46  27.676  -18.737 1   21.6  ? 275 VAL   A N   1 
ATOM   2171 C  CA  . VAL   A 1 290 ? -24.913 26.778  -17.672 1   22.14 ? 275 VAL   A CA  1 
ATOM   2172 C  C   . VAL   A 1 290 ? -25.667 27.578  -16.598 1   22.83 ? 275 VAL   A C   1 
ATOM   2173 O  O   . VAL   A 1 290 ? -26.758 27.187  -16.181 1   23.68 ? 275 VAL   A O   1 
ATOM   2174 C  CB  . VAL   A 1 290 ? -23.743 25.985  -17.034 1   23.43 ? 275 VAL   A CB  1 
ATOM   2175 C  CG1 . VAL   A 1 290 ? -24.234 25.222  -15.809 1   24.61 ? 275 VAL   A CG1 1 
ATOM   2176 C  CG2 . VAL   A 1 290 ? -23.121 25.016  -18.035 1   23.8  ? 275 VAL   A CG2 1 
ATOM   2177 N  N   . LEU   A 1 291 ? -25.082 28.688  -16.14  1   22.74 ? 276 LEU   A N   1 
ATOM   2178 C  CA  . LEU   A 1 291 ? -25.669 29.533  -15.107 1   23.92 ? 276 LEU   A CA  1 
ATOM   2179 C  C   . LEU   A 1 291 ? -27.103 29.969  -15.477 1   25.28 ? 276 LEU   A C   1 
ATOM   2180 O  O   . LEU   A 1 291 ? -28.012 29.858  -14.658 1   25.97 ? 276 LEU   A O   1 
ATOM   2181 C  CB  . LEU   A 1 291 ? -24.789 30.777  -14.885 1   23.85 ? 276 LEU   A CB  1 
ATOM   2182 C  CG  . LEU   A 1 291 ? -25.323 31.766  -13.847 1   25.65 ? 276 LEU   A CG  1 
ATOM   2183 C  CD1 . LEU   A 1 291 ? -25.273 31.153  -12.455 1   27.01 ? 276 LEU   A CD1 1 
ATOM   2184 C  CD2 . LEU   A 1 291 ? -24.53  33.059  -13.878 1   25.92 ? 276 LEU   A CD2 1 
ATOM   2185 N  N   . LEU   A 1 292 ? -27.299 30.418  -16.722 1   24.46 ? 277 LEU   A N   1 
ATOM   2186 C  CA  . LEU   A 1 292 ? -28.607 30.906  -17.155 1   23.51 ? 277 LEU   A CA  1 
ATOM   2187 C  C   . LEU   A 1 292 ? -29.564 29.825  -17.682 1   24.51 ? 277 LEU   A C   1 
ATOM   2188 O  O   . LEU   A 1 292 ? -30.641 30.164  -18.193 1   24.75 ? 277 LEU   A O   1 
ATOM   2189 C  CB  . LEU   A 1 292 ? -28.404 32.016  -18.202 1   22.18 ? 277 LEU   A CB  1 
ATOM   2190 C  CG  . LEU   A 1 292 ? -27.578 33.203  -17.692 1   22.8  ? 277 LEU   A CG  1 
ATOM   2191 C  CD1 . LEU   A 1 292 ? -27.087 34.064  -18.844 1   23.1  ? 277 LEU   A CD1 1 
ATOM   2192 C  CD2 . LEU   A 1 292 ? -28.364 34.032  -16.637 1   22.59 ? 277 LEU   A CD2 1 
ATOM   2193 N  N   . GLY   A 1 293 ? -29.18  28.547  -17.584 1   23.72 ? 278 GLY   A N   1 
ATOM   2194 C  CA  . GLY   A 1 293 ? -30.052 27.461  -18.022 1   23.74 ? 278 GLY   A CA  1 
ATOM   2195 C  C   . GLY   A 1 293 ? -30.274 27.394  -19.51  1   25.27 ? 278 GLY   A C   1 
ATOM   2196 O  O   . GLY   A 1 293 ? -31.255 26.815  -19.976 1   25.55 ? 278 GLY   A O   1 
ATOM   2197 N  N   . ILE   A 1 294 ? -29.331 27.954  -20.291 1   25.74 ? 279 ILE   A N   1 
ATOM   2198 C  CA  . ILE   A 1 294 ? -29.342 27.88   -21.734 1   27.91 ? 279 ILE   A CA  1 
ATOM   2199 C  C   . ILE   A 1 294 ? -28.729 26.513  -21.918 1   32.06 ? 279 ILE   A C   1 
ATOM   2200 O  O   . ILE   A 1 294 ? -27.517 26.353  -21.715 1   34.11 ? 279 ILE   A O   1 
ATOM   2201 C  CB  . ILE   A 1 294 ? -28.47  29.01   -22.289 1   27.78 ? 279 ILE   A CB  1 
ATOM   2202 C  CG1 . ILE   A 1 294 ? -29.09  30.407  -21.903 1   28.44 ? 279 ILE   A CG1 1 
ATOM   2203 C  CG2 . ILE   A 1 294 ? -28.335 28.857  -23.786 1   27.95 ? 279 ILE   A CG2 1 
ATOM   2204 C  CD1 . ILE   A 1 294 ? -28.189 31.549  -22.132 1   29.12 ? 279 ILE   A CD1 1 
ATOM   2205 N  N   . GLN   A 1 295 ? -29.561 25.505  -22.151 1   32.88 ? 280 GLN   A N   1 
ATOM   2206 C  CA  A GLN   A 1 295 ? -29.081 24.122  -22.203 0.5 33.64 ? 280 GLN   A CA  1 
ATOM   2207 C  CA  B GLN   A 1 295 ? -29.084 24.119  -22.2   0.5 33.78 ? 280 GLN   A CA  1 
ATOM   2208 C  C   . GLN   A 1 295 ? -28.348 23.804  -23.492 1   33.44 ? 280 GLN   A C   1 
ATOM   2209 O  O   . GLN   A 1 295 ? -28.832 23.026  -24.308 1   33.02 ? 280 GLN   A O   1 
ATOM   2210 C  CB  A GLN   A 1 295 ? -30.232 23.14   -21.945 0.5 35.46 ? 280 GLN   A CB  1 
ATOM   2211 C  CB  B GLN   A 1 295 ? -30.242 23.137  -21.955 0.5 36.02 ? 280 GLN   A CB  1 
ATOM   2212 C  CG  A GLN   A 1 295 ? -30.911 23.347  -20.6   0.5 38.98 ? 280 GLN   A CG  1 
ATOM   2213 C  CG  B GLN   A 1 295 ? -30.872 23.252  -20.574 0.5 40.4  ? 280 GLN   A CG  1 
ATOM   2214 C  CD  A GLN   A 1 295 ? -30.325 22.477  -19.519 0.5 43.57 ? 280 GLN   A CD  1 
ATOM   2215 C  CD  B GLN   A 1 295 ? -32.09  22.37   -20.46  0.5 46.17 ? 280 GLN   A CD  1 
ATOM   2216 O  OE1 A GLN   A 1 295 ? -29.151 22.095  -19.55  0.5 44.67 ? 280 GLN   A OE1 1 
ATOM   2217 O  OE1 B GLN   A 1 295 ? -32.129 21.245  -20.977 0.5 47.9  ? 280 GLN   A OE1 1 
ATOM   2218 N  NE2 A GLN   A 1 295 ? -31.14  22.145  -18.534 0.5 44.77 ? 280 GLN   A NE2 1 
ATOM   2219 N  NE2 B GLN   A 1 295 ? -33.117 22.863  -19.787 0.5 47.4  ? 280 GLN   A NE2 1 
ATOM   2220 N  N   . GLN   A 1 296 ? -27.177 24.413  -23.679 1   32.93 ? 281 GLN   A N   1 
ATOM   2221 C  CA  . GLN   A 1 296 ? -26.389 24.199  -24.889 1   33.07 ? 281 GLN   A CA  1 
ATOM   2222 C  C   . GLN   A 1 296 ? -25.937 22.778  -25.025 1   34.47 ? 281 GLN   A C   1 
ATOM   2223 O  O   . GLN   A 1 296 ? -25.721 22.371  -26.14  1   35.09 ? 281 GLN   A O   1 
ATOM   2224 C  CB  . GLN   A 1 296 ? -25.143 25.11   -24.94  1   32.67 ? 281 GLN   A CB  1 
ATOM   2225 C  CG  . GLN   A 1 296 ? -25.428 26.593  -24.993 1   32.49 ? 281 GLN   A CG  1 
ATOM   2226 C  CD  . GLN   A 1 296 ? -25.964 27.104  -26.305 1   31.95 ? 281 GLN   A CD  1 
ATOM   2227 O  OE1 . GLN   A 1 296 ? -26.21  26.366  -27.266 1   31.14 ? 281 GLN   A OE1 1 
ATOM   2228 N  NE2 . GLN   A 1 296 ? -26.166 28.4    -26.366 1   30.47 ? 281 GLN   A NE2 1 
ATOM   2229 N  N   . THR   A 1 297 ? -25.757 22.031  -23.92  1   35.63 ? 282 THR   A N   1 
ATOM   2230 C  CA  . THR   A 1 297 ? -25.3   20.639  -23.994 1   37.24 ? 282 THR   A CA  1 
ATOM   2231 C  C   . THR   A 1 297 ? -26.432 19.597  -23.918 1   39.33 ? 282 THR   A C   1 
ATOM   2232 O  O   . THR   A 1 297 ? -26.147 18.39   -23.908 1   38.98 ? 282 THR   A O   1 
ATOM   2233 C  CB  . THR   A 1 297 ? -24.238 20.378  -22.941 1   37.65 ? 282 THR   A CB  1 
ATOM   2234 O  OG1 . THR   A 1 297 ? -24.779 20.716  -21.665 1   38.82 ? 282 THR   A OG1 1 
ATOM   2235 C  CG2 . THR   A 1 297 ? -22.982 21.183  -23.189 1   37.46 ? 282 THR   A CG2 1 
ATOM   2236 N  N   . ALA   A 1 298 ? -27.701 20.046  -23.897 1   40.33 ? 283 ALA   A N   1 
ATOM   2237 C  CA  . ALA   A 1 298 ? -28.821 19.114  -23.818 1   42.08 ? 283 ALA   A CA  1 
ATOM   2238 C  C   . ALA   A 1 298 ? -29.172 18.537  -25.183 1   43.15 ? 283 ALA   A C   1 
ATOM   2239 O  O   . ALA   A 1 298 ? -28.983 19.188  -26.211 1   42.6  ? 283 ALA   A O   1 
ATOM   2240 C  CB  . ALA   A 1 298 ? -30.036 19.791  -23.218 1   42.12 ? 283 ALA   A CB  1 
ATOM   2241 N  N   . GLY   A 1 299 ? -29.698 17.317  -25.171 1   43.95 ? 284 GLY   A N   1 
ATOM   2242 C  CA  . GLY   A 1 299 ? -30.058 16.628  -26.4   1   45.12 ? 284 GLY   A CA  1 
ATOM   2243 C  C   . GLY   A 1 299 ? -28.874 15.918  -27.025 1   45.87 ? 284 GLY   A C   1 
ATOM   2244 O  O   . GLY   A 1 299 ? -27.743 16      -26.531 1   46.56 ? 284 GLY   A O   1 
ATOM   2245 N  N   . GLY   A 1 300 ? -29.127 15.245  -28.132 1   45.49 ? 285 GLY   A N   1 
ATOM   2246 C  CA  . GLY   A 1 300 ? -28.082 14.514  -28.835 1   44.85 ? 285 GLY   A CA  1 
ATOM   2247 C  C   . GLY   A 1 300 ? -27.668 15.122  -30.158 1   43.42 ? 285 GLY   A C   1 
ATOM   2248 O  O   . GLY   A 1 300 ? -27.078 14.433  -30.996 1   44.76 ? 285 GLY   A O   1 
ATOM   2249 N  N   . GLY   A 1 301 ? -27.95  16.407  -30.348 1   40.23 ? 286 GLY   A N   1 
ATOM   2250 C  CA  . GLY   A 1 301 ? -27.566 17.094  -31.574 1   37.81 ? 286 GLY   A CA  1 
ATOM   2251 C  C   . GLY   A 1 301 ? -26.077 17.383  -31.656 1   34.29 ? 286 GLY   A C   1 
ATOM   2252 O  O   . GLY   A 1 301 ? -25.367 17.271  -30.658 1   33.63 ? 286 GLY   A O   1 
ATOM   2253 N  N   . HIS   A 1 302 ? -25.597 17.756  -32.84  1   32.54 ? 287 HIS   A N   1 
ATOM   2254 C  CA  . HIS   A 1 302 ? -24.183 18.018  -33.086 1   32.11 ? 287 HIS   A CA  1 
ATOM   2255 C  C   . HIS   A 1 302 ? -23.583 19.135  -32.216 1   28.39 ? 287 HIS   A C   1 
ATOM   2256 O  O   . HIS   A 1 302 ? -22.502 18.948  -31.663 1   26.87 ? 287 HIS   A O   1 
ATOM   2257 C  CB  . HIS   A 1 302 ? -23.949 18.345  -34.567 1   36.24 ? 287 HIS   A CB  1 
ATOM   2258 C  CG  . HIS   A 1 302 ? -24.058 17.161  -35.473 1   44.66 ? 287 HIS   A CG  1 
ATOM   2259 N  ND1 . HIS   A 1 302 ? -25.106 17.038  -36.384 1   48.05 ? 287 HIS   A ND1 1 
ATOM   2260 C  CD2 . HIS   A 1 302 ? -23.252 16.078  -35.581 1   47.39 ? 287 HIS   A CD2 1 
ATOM   2261 C  CE1 . HIS   A 1 302 ? -24.897 15.893  -37.019 1   49.15 ? 287 HIS   A CE1 1 
ATOM   2262 N  NE2 . HIS   A 1 302 ? -23.795 15.276  -36.569 1   49.42 ? 287 HIS   A NE2 1 
ATOM   2263 N  N   . ALA   A 1 303 ? -24.295 20.291  -32.082 1   26.15 ? 288 ALA   A N   1 
ATOM   2264 C  CA  . ALA   A 1 303 ? -23.778 21.424  -31.323 1   24.28 ? 288 ALA   A CA  1 
ATOM   2265 C  C   . ALA   A 1 303 ? -23.617 21.066  -29.849 1   23.32 ? 288 ALA   A C   1 
ATOM   2266 O  O   . ALA   A 1 303 ? -22.591 21.351  -29.242 1   22.54 ? 288 ALA   A O   1 
ATOM   2267 C  CB  . ALA   A 1 303 ? -24.702 22.643  -31.504 1   23.43 ? 288 ALA   A CB  1 
ATOM   2268 N  N   . ALA   A 1 304 ? -24.627 20.384  -29.276 1   23.28 ? 289 ALA   A N   1 
ATOM   2269 C  CA  . ALA   A 1 304 ? -24.563 19.972  -27.879 1   23.06 ? 289 ALA   A CA  1 
ATOM   2270 C  C   . ALA   A 1 304 ? -23.434 18.945  -27.646 1   21.95 ? 289 ALA   A C   1 
ATOM   2271 O  O   . ALA   A 1 304 ? -22.717 19.036  -26.65  1   21.74 ? 289 ALA   A O   1 
ATOM   2272 C  CB  . ALA   A 1 304 ? -25.905 19.377  -27.458 1   24.19 ? 289 ALA   A CB  1 
ATOM   2273 N  N   . GLN   A 1 305 ? -23.288 17.972  -28.543 1   20.51 ? 290 GLN   A N   1 
ATOM   2274 C  CA  . GLN   A 1 305 ? -22.246 16.961  -28.417 1   19.85 ? 290 GLN   A CA  1 
ATOM   2275 C  C   . GLN   A 1 305 ? -20.857 17.62   -28.513 1   18.89 ? 290 GLN   A C   1 
ATOM   2276 O  O   . GLN   A 1 305 ? -19.958 17.269  -27.749 1   18.2  ? 290 GLN   A O   1 
ATOM   2277 C  CB  . GLN   A 1 305 ? -22.383 15.9    -29.521 1   20.93 ? 290 GLN   A CB  1 
ATOM   2278 C  CG  . GLN   A 1 305 ? -21.334 14.79   -29.398 1   22.18 ? 290 GLN   A CG  1 
ATOM   2279 C  CD  . GLN   A 1 305 ? -21.666 13.889  -28.224 1   28.02 ? 290 GLN   A CD  1 
ATOM   2280 O  OE1 . GLN   A 1 305 ? -22.76  13.313  -28.154 1   29.21 ? 290 GLN   A OE1 1 
ATOM   2281 N  NE2 . GLN   A 1 305 ? -20.729 13.737  -27.273 1   27.17 ? 290 GLN   A NE2 1 
ATOM   2282 N  N   . PHE   A 1 306 ? -20.693 18.559  -29.432 1   17.91 ? 291 PHE   A N   1 
ATOM   2283 C  CA  . PHE   A 1 306 ? -19.415 19.262  -29.605 1   18.54 ? 291 PHE   A CA  1 
ATOM   2284 C  C   . PHE   A 1 306 ? -19.002 20.045  -28.345 1   18.48 ? 291 PHE   A C   1 
ATOM   2285 O  O   . PHE   A 1 306 ? -17.881 19.895  -27.85  1   18.24 ? 291 PHE   A O   1 
ATOM   2286 C  CB  . PHE   A 1 306 ? -19.438 20.149  -30.858 1   19.03 ? 291 PHE   A CB  1 
ATOM   2287 C  CG  . PHE   A 1 306 ? -18.146 20.92   -31.075 1   20.6  ? 291 PHE   A CG  1 
ATOM   2288 C  CD1 . PHE   A 1 306 ? -17.002 20.279  -31.556 1   21.65 ? 291 PHE   A CD1 1 
ATOM   2289 C  CD2 . PHE   A 1 306 ? -18.056 22.27   -30.74  1   21.61 ? 291 PHE   A CD2 1 
ATOM   2290 C  CE1 . PHE   A 1 306 ? -15.8   20.984  -31.708 1   23.33 ? 291 PHE   A CE1 1 
ATOM   2291 C  CE2 . PHE   A 1 306 ? -16.853 22.98   -30.915 1   22.82 ? 291 PHE   A CE2 1 
ATOM   2292 C  CZ  . PHE   A 1 306 ? -15.739 22.333  -31.389 1   23.2  ? 291 PHE   A CZ  1 
ATOM   2293 N  N   . LEU   A 1 307 ? -19.931 20.849  -27.783 1   18.47 ? 292 LEU   A N   1 
ATOM   2294 C  CA  . LEU   A 1 307 ? -19.613 21.626  -26.58  1   17.79 ? 292 LEU   A CA  1 
ATOM   2295 C  C   . LEU   A 1 307 ? -19.344 20.733  -25.384 1   17.66 ? 292 LEU   A C   1 
ATOM   2296 O  O   . LEU   A 1 307 ? -18.451 21.057  -24.584 1   18.75 ? 292 LEU   A O   1 
ATOM   2297 C  CB  . LEU   A 1 307 ? -20.724 22.651  -26.286 1   18.65 ? 292 LEU   A CB  1 
ATOM   2298 C  CG  . LEU   A 1 307 ? -20.733 23.795  -27.301 1   21.35 ? 292 LEU   A CG  1 
ATOM   2299 C  CD1 . LEU   A 1 307 ? -22.046 24.598  -27.22  1   22.95 ? 292 LEU   A CD1 1 
ATOM   2300 C  CD2 . LEU   A 1 307 ? -19.475 24.689  -27.132 1   21.41 ? 292 LEU   A CD2 1 
ATOM   2301 N  N   . GLN   A 1 308 ? -20.086 19.609  -25.243 1   16.95 ? 293 GLN   A N   1 
ATOM   2302 C  CA  . GLN   A 1 308 ? -19.777 18.685  -24.147 1   18.47 ? 293 GLN   A CA  1 
ATOM   2303 C  C   . GLN   A 1 308 ? -18.375 18.047  -24.38  1   18.45 ? 293 GLN   A C   1 
ATOM   2304 O  O   . GLN   A 1 308 ? -17.546 17.995  -23.465 1   19.71 ? 293 GLN   A O   1 
ATOM   2305 C  CB  . GLN   A 1 308 ? -20.838 17.565  -24.033 1   22.35 ? 293 GLN   A CB  1 
ATOM   2306 C  CG  . GLN   A 1 308 ? -20.557 16.659  -22.836 1   30.18 ? 293 GLN   A CG  1 
ATOM   2307 C  CD  . GLN   A 1 308 ? -20.753 17.332  -21.493 1   38.64 ? 293 GLN   A CD  1 
ATOM   2308 O  OE1 . GLN   A 1 308 ? -20.018 17.075  -20.521 1   43.2  ? 293 GLN   A OE1 1 
ATOM   2309 N  NE2 . GLN   A 1 308 ? -21.741 18.2    -21.397 1   38.02 ? 293 GLN   A NE2 1 
ATOM   2310 N  N   . ASP   A 1 309 ? -18.092 17.615  -25.6   1   17.91 ? 294 ASP   A N   1 
ATOM   2311 C  CA  . ASP   A 1 309 ? -16.773 17.054  -25.934 1   17.78 ? 294 ASP   A CA  1 
ATOM   2312 C  C   . ASP   A 1 309 ? -15.624 18.031  -25.63  1   17.8  ? 294 ASP   A C   1 
ATOM   2313 O  O   . ASP   A 1 309 ? -14.567 17.608  -25.181 1   16.47 ? 294 ASP   A O   1 
ATOM   2314 C  CB  . ASP   A 1 309 ? -16.693 16.639  -27.414 1   18.61 ? 294 ASP   A CB  1 
ATOM   2315 C  CG  . ASP   A 1 309 ? -17.481 15.388  -27.757 1   23.03 ? 294 ASP   A CG  1 
ATOM   2316 O  OD1 . ASP   A 1 309 ? -18.003 14.739  -26.821 1   23.08 ? 294 ASP   A OD1 1 
ATOM   2317 O  OD2 . ASP   A 1 309 ? -17.607 15.078  -28.973 1   25.19 ? 294 ASP   A OD2 1 
ATOM   2318 N  N   . MET   A 1 310 ? -15.835 19.33   -25.908 1   17.29 ? 295 MET   A N   1 
ATOM   2319 C  CA  . MET   A 1 310 ? -14.796 20.334  -25.674 1   17.72 ? 295 MET   A CA  1 
ATOM   2320 C  C   . MET   A 1 310 ? -14.463 20.507  -24.212 1   18.21 ? 295 MET   A C   1 
ATOM   2321 O  O   . MET   A 1 310 ? -13.385 20.99   -23.913 1   18.8  ? 295 MET   A O   1 
ATOM   2322 C  CB  . MET   A 1 310 ? -15.132 21.668  -26.346 1   17.26 ? 295 MET   A CB  1 
ATOM   2323 C  CG  . MET   A 1 310 ? -15.092 21.605  -27.846 1   18.53 ? 295 MET   A CG  1 
ATOM   2324 S  SD  . MET   A 1 310 ? -13.545 21.014  -28.638 1   22.36 ? 295 MET   A SD  1 
ATOM   2325 C  CE  . MET   A 1 310 ? -13.986 19.267  -29.033 1   20.16 ? 295 MET   A CE  1 
ATOM   2326 N  N   . ARG   A 1 311 ? -15.349 20.049  -23.275 1   18.23 ? 296 ARG   A N   1 
ATOM   2327 C  CA  . ARG   A 1 311 ? -15.027 20.126  -21.86  1   18.94 ? 296 ARG   A CA  1 
ATOM   2328 C  C   . ARG   A 1 311 ? -13.816 19.28   -21.471 1   19.71 ? 296 ARG   A C   1 
ATOM   2329 O  O   . ARG   A 1 311 ? -13.06  19.692  -20.607 1   20.14 ? 296 ARG   A O   1 
ATOM   2330 C  CB  . ARG   A 1 311 ? -16.234 19.797  -20.985 1   20.47 ? 296 ARG   A CB  1 
ATOM   2331 C  CG  . ARG   A 1 311 ? -17.335 20.812  -21.203 1   21.76 ? 296 ARG   A CG  1 
ATOM   2332 C  CD  . ARG   A 1 311 ? -18.404 20.607  -20.159 1   25.66 ? 296 ARG   A CD  1 
ATOM   2333 N  NE  . ARG   A 1 311 ? -19.476 21.577  -20.352 1   27.33 ? 296 ARG   A NE  1 
ATOM   2334 C  CZ  . ARG   A 1 311 ? -20.556 21.66   -19.585 1   30.87 ? 296 ARG   A CZ  1 
ATOM   2335 N  NH1 . ARG   A 1 311 ? -20.734 20.805  -18.582 1   30.32 ? 296 ARG   A NH1 1 
ATOM   2336 N  NH2 . ARG   A 1 311 ? -21.482 22.571  -19.836 1   30.97 ? 296 ARG   A NH2 1 
ATOM   2337 N  N   . ARG   A 1 312 ? -13.588 18.141  -22.127 1   20.47 ? 297 ARG   A N   1 
ATOM   2338 C  CA  . ARG   A 1 312 ? -12.39  17.323  -21.85  1   22.21 ? 297 ARG   A CA  1 
ATOM   2339 C  C   . ARG   A 1 312 ? -11.076 17.931  -22.413 1   21.23 ? 297 ARG   A C   1 
ATOM   2340 O  O   . ARG   A 1 312 ? -9.995  17.382  -22.209 1   21.48 ? 297 ARG   A O   1 
ATOM   2341 C  CB  . ARG   A 1 312 ? -12.604 15.886  -22.336 1   26.79 ? 297 ARG   A CB  1 
ATOM   2342 C  CG  . ARG   A 1 312 ? -13.689 15.15   -21.51  1   34.26 ? 297 ARG   A CG  1 
ATOM   2343 C  CD  . ARG   A 1 312 ? -13.145 14.404  -20.28  1   39.79 ? 297 ARG   A CD  1 
ATOM   2344 N  NE  . ARG   A 1 312 ? -14.204 13.972  -19.353 1   44.55 ? 297 ARG   A NE  1 
ATOM   2345 C  CZ  . ARG   A 1 312 ? -13.991 13.598  -18.087 1   48.64 ? 297 ARG   A CZ  1 
ATOM   2346 N  NH1 . ARG   A 1 312 ? -12.758 13.565  -17.594 1   49.13 ? 297 ARG   A NH1 1 
ATOM   2347 N  NH2 . ARG   A 1 312 ? -15.011 13.22   -17.315 1   46.9  ? 297 ARG   A NH2 1 
ATOM   2348 N  N   . TYR   A 1 313 ? -11.181 19.058  -23.135 1   19.37 ? 298 TYR   A N   1 
ATOM   2349 C  CA  . TYR   A 1 313 ? -10.041 19.814  -23.662 1   18.34 ? 298 TYR   A CA  1 
ATOM   2350 C  C   . TYR   A 1 313 ? -9.77   21.087  -22.795 1   17.53 ? 298 TYR   A C   1 
ATOM   2351 O  O   . TYR   A 1 313 ? -8.901  21.909  -23.143 1   17.41 ? 298 TYR   A O   1 
ATOM   2352 C  CB  . TYR   A 1 313 ? -10.312 20.228  -25.103 1   17.62 ? 298 TYR   A CB  1 
ATOM   2353 C  CG  . TYR   A 1 313 ? -10.313 19.088  -26.094 1   16.9  ? 298 TYR   A CG  1 
ATOM   2354 C  CD1 . TYR   A 1 313 ? -11.366 18.182  -26.144 1   18.14 ? 298 TYR   A CD1 1 
ATOM   2355 C  CD2 . TYR   A 1 313 ? -9.303  18.969  -27.047 1   17.6  ? 298 TYR   A CD2 1 
ATOM   2356 C  CE1 . TYR   A 1 313 ? -11.369 17.13   -27.059 1   18.73 ? 298 TYR   A CE1 1 
ATOM   2357 C  CE2 . TYR   A 1 313 ? -9.311  17.947  -27.982 1   17.33 ? 298 TYR   A CE2 1 
ATOM   2358 C  CZ  . TYR   A 1 313 ? -10.323 17.008  -27.963 1   18.71 ? 298 TYR   A CZ  1 
ATOM   2359 O  OH  . TYR   A 1 313 ? -10.342 16.02   -28.915 1   19.51 ? 298 TYR   A OH  1 
ATOM   2360 N  N   . MET   A 1 314 ? -10.53  21.253  -21.685 1   16.48 ? 299 MET   A N   1 
ATOM   2361 C  CA  . MET   A 1 314 ? -10.333 22.341  -20.745 1   17.01 ? 299 MET   A CA  1 
ATOM   2362 C  C   . MET   A 1 314 ? -9.476  21.828  -19.584 1   17.83 ? 299 MET   A C   1 
ATOM   2363 O  O   . MET   A 1 314 ? -9.574  20.664  -19.239 1   19.1  ? 299 MET   A O   1 
ATOM   2364 C  CB  . MET   A 1 314 ? -11.691 22.744  -20.154 1   16.56 ? 299 MET   A CB  1 
ATOM   2365 C  CG  . MET   A 1 314 ? -12.704 23.223  -21.176 1   17.35 ? 299 MET   A CG  1 
ATOM   2366 S  SD  . MET   A 1 314 ? -14.228 23.687  -20.271 1   19.78 ? 299 MET   A SD  1 
ATOM   2367 C  CE  . MET   A 1 314 ? -15.213 24.271  -21.671 1   13.95 ? 299 MET   A CE  1 
ATOM   2368 N  N   . PRO   A 1 315 ? -8.776  22.714  -18.86  1   17.83 ? 300 PRO   A N   1 
ATOM   2369 C  CA  . PRO   A 1 315 ? -8.053  22.284  -17.658 1   18.3  ? 300 PRO   A CA  1 
ATOM   2370 C  C   . PRO   A 1 315 ? -9.02   21.619  -16.663 1   20.03 ? 300 PRO   A C   1 
ATOM   2371 O  O   . PRO   A 1 315 ? -10.208 22.002  -16.598 1   19.87 ? 300 PRO   A O   1 
ATOM   2372 C  CB  . PRO   A 1 315 ? -7.456  23.587  -17.108 1   18.68 ? 300 PRO   A CB  1 
ATOM   2373 C  CG  . PRO   A 1 315 ? -7.4    24.516  -18.309 1   19.39 ? 300 PRO   A CG  1 
ATOM   2374 C  CD  . PRO   A 1 315 ? -8.621  24.158  -19.109 1   17.61 ? 300 PRO   A CD  1 
ATOM   2375 N  N   . PRO   A 1 316 ? -8.54   20.569  -15.964 1   20.41 ? 301 PRO   A N   1 
ATOM   2376 C  CA  . PRO   A 1 316 ? -9.42   19.77   -15.107 1   20.58 ? 301 PRO   A CA  1 
ATOM   2377 C  C   . PRO   A 1 316 ? -10.226 20.531  -14.058 1   21.4  ? 301 PRO   A C   1 
ATOM   2378 O  O   . PRO   A 1 316 ? -11.393 20.194  -13.855 1   22.21 ? 301 PRO   A O   1 
ATOM   2379 C  CB  . PRO   A 1 316 ? -8.456  18.749  -14.458 1   21.88 ? 301 PRO   A CB  1 
ATOM   2380 C  CG  . PRO   A 1 316 ? -7.084  19.286  -14.677 1   23.16 ? 301 PRO   A CG  1 
ATOM   2381 C  CD  . PRO   A 1 316 ? -7.192  19.976  -16.031 1   20.96 ? 301 PRO   A CD  1 
ATOM   2382 N  N   . ALA   A 1 317 ? -9.634  21.533  -13.407 1   21.54 ? 302 ALA   A N   1 
ATOM   2383 C  CA  . ALA   A 1 317 ? -10.357 22.318  -12.406 1   22.05 ? 302 ALA   A CA  1 
ATOM   2384 C  C   . ALA   A 1 317 ? -11.506 23.134  -13.057 1   21.59 ? 302 ALA   A C   1 
ATOM   2385 O  O   . ALA   A 1 317 ? -12.546 23.38   -12.434 1   20.22 ? 302 ALA   A O   1 
ATOM   2386 C  CB  . ALA   A 1 317 ? -9.398  23.282  -11.725 1   21.99 ? 302 ALA   A CB  1 
ATOM   2387 N  N   . HIS   A 1 318 ? -11.305 23.567  -14.29  1   21.3  ? 303 HIS   A N   1 
ATOM   2388 C  CA  . HIS   A 1 318 ? -12.287 24.364  -15.034 1   21.4  ? 303 HIS   A CA  1 
ATOM   2389 C  C   . HIS   A 1 318 ? -13.434 23.507  -15.532 1   20.89 ? 303 HIS   A C   1 
ATOM   2390 O  O   . HIS   A 1 318 ? -14.586 23.907  -15.452 1   20.55 ? 303 HIS   A O   1 
ATOM   2391 C  CB  . HIS   A 1 318 ? -11.592 25.153  -16.162 1   21.13 ? 303 HIS   A CB  1 
ATOM   2392 C  CG  . HIS   A 1 318 ? -10.55  26.126  -15.678 1   22.3  ? 303 HIS   A CG  1 
ATOM   2393 N  ND1 . HIS   A 1 318 ? -9.75   26.811  -16.571 1   23.22 ? 303 HIS   A ND1 1 
ATOM   2394 C  CD2 . HIS   A 1 318 ? -10.235 26.531  -14.418 1   22.87 ? 303 HIS   A CD2 1 
ATOM   2395 C  CE1 . HIS   A 1 318 ? -8.988  27.613  -15.835 1   23.57 ? 303 HIS   A CE1 1 
ATOM   2396 N  NE2 . HIS   A 1 318 ? -9.236  27.471  -14.536 1   23.31 ? 303 HIS   A NE2 1 
ATOM   2397 N  N   . ARG   A 1 319 ? -13.136 22.294  -15.942 1   20.87 ? 304 ARG   A N   1 
ATOM   2398 C  CA  . ARG   A 1 319 ? -14.095 21.279  -16.307 1   22.98 ? 304 ARG   A CA  1 
ATOM   2399 C  C   . ARG   A 1 319 ? -14.955 20.951  -15.04  1   23.53 ? 304 ARG   A C   1 
ATOM   2400 O  O   . ARG   A 1 319 ? -16.177 20.864  -15.131 1   24.31 ? 304 ARG   A O   1 
ATOM   2401 C  CB  . ARG   A 1 319 ? -13.275 20.038  -16.705 1   25.4  ? 304 ARG   A CB  1 
ATOM   2402 C  CG  . ARG   A 1 319 ? -13.977 18.934  -17.46  1   31.41 ? 304 ARG   A CG  1 
ATOM   2403 C  CD  . ARG   A 1 319 ? -12.993 17.767  -17.737 1   34.2  ? 304 ARG   A CD  1 
ATOM   2404 N  NE  . ARG   A 1 319 ? -11.653 18.226  -18.152 1   36.33 ? 304 ARG   A NE  1 
ATOM   2405 C  CZ  . ARG   A 1 319 ? -10.557 17.465  -18.113 1   37.48 ? 304 ARG   A CZ  1 
ATOM   2406 N  NH1 . ARG   A 1 319 ? -10.629 16.207  -17.694 1   39.99 ? 304 ARG   A NH1 1 
ATOM   2407 N  NH2 . ARG   A 1 319 ? -9.377  17.967  -18.459 1   29.92 ? 304 ARG   A NH2 1 
ATOM   2408 N  N   . ASN   A 1 320 ? -14.312 20.841  -13.866 1   23.28 ? 305 ASN   A N   1 
ATOM   2409 C  CA  . ASN   A 1 320 ? -14.958 20.542  -12.588 1   24.05 ? 305 ASN   A CA  1 
ATOM   2410 C  C   . ASN   A 1 320 ? -15.891 21.699  -12.186 1   24.3  ? 305 ASN   A C   1 
ATOM   2411 O  O   . ASN   A 1 320 ? -16.963 21.466  -11.628 1   24.13 ? 305 ASN   A O   1 
ATOM   2412 C  CB  . ASN   A 1 320 ? -13.899 20.378  -11.481 1   26.81 ? 305 ASN   A CB  1 
ATOM   2413 C  CG  . ASN   A 1 320 ? -13.066 19.12   -11.557 1   31.98 ? 305 ASN   A CG  1 
ATOM   2414 O  OD1 . ASN   A 1 320 ? -13.362 18.221  -12.319 1   34.46 ? 305 ASN   A OD1 1 
ATOM   2415 N  ND2 . ASN   A 1 320 ? -11.995 19.013  -10.756 1   34.02 ? 305 ASN   A ND2 1 
ATOM   2416 N  N   . PHE   A 1 321 ? -15.455 22.945  -12.423 1   23.86 ? 306 PHE   A N   1 
ATOM   2417 C  CA  . PHE   A 1 321 ? -16.246 24.142  -12.118 1   23.56 ? 306 PHE   A CA  1 
ATOM   2418 C  C   . PHE   A 1 321 ? -17.543 24.102  -12.907 1   22.98 ? 306 PHE   A C   1 
ATOM   2419 O  O   . PHE   A 1 321 ? -18.594 24.323  -12.321 1   23.29 ? 306 PHE   A O   1 
ATOM   2420 C  CB  . PHE   A 1 321 ? -15.463 25.42   -12.42  1   23.07 ? 306 PHE   A CB  1 
ATOM   2421 C  CG  . PHE   A 1 321 ? -16.25  26.666  -12.107 1   25.02 ? 306 PHE   A CG  1 
ATOM   2422 C  CD1 . PHE   A 1 321 ? -16.485 27.044  -10.798 1   26.21 ? 306 PHE   A CD1 1 
ATOM   2423 C  CD2 . PHE   A 1 321 ? -16.861 27.395  -13.121 1   25.99 ? 306 PHE   A CD2 1 
ATOM   2424 C  CE1 . PHE   A 1 321 ? -17.241 28.176  -10.506 1   27.34 ? 306 PHE   A CE1 1 
ATOM   2425 C  CE2 . PHE   A 1 321 ? -17.624 28.519  -12.824 1   26.75 ? 306 PHE   A CE2 1 
ATOM   2426 C  CZ  . PHE   A 1 321 ? -17.789 28.914  -11.52  1   26.89 ? 306 PHE   A CZ  1 
ATOM   2427 N  N   . LEU   A 1 322 ? -17.482 23.729  -14.187 1   22.37 ? 307 LEU   A N   1 
ATOM   2428 C  CA  . LEU   A 1 322 ? -18.683 23.652  -15.008 1   23.46 ? 307 LEU   A CA  1 
ATOM   2429 C  C   . LEU   A 1 322 ? -19.682 22.588  -14.527 1   25.26 ? 307 LEU   A C   1 
ATOM   2430 O  O   . LEU   A 1 322 ? -20.878 22.896  -14.385 1   24.45 ? 307 LEU   A O   1 
ATOM   2431 C  CB  . LEU   A 1 322 ? -18.333 23.42   -16.468 1   23.11 ? 307 LEU   A CB  1 
ATOM   2432 C  CG  . LEU   A 1 322 ? -17.675 24.586  -17.182 1   24.39 ? 307 LEU   A CG  1 
ATOM   2433 C  CD1 . LEU   A 1 322 ? -17.331 24.191  -18.613 1   24.45 ? 307 LEU   A CD1 1 
ATOM   2434 C  CD2 . LEU   A 1 322 ? -18.623 25.779  -17.221 1   24.17 ? 307 LEU   A CD2 1 
ATOM   2435 N  N   . CYS   A 1 323 ? -19.206 21.341  -14.27  1   27.06 ? 308 CYS   A N   1 
ATOM   2436 C  CA  . CYS   A 1 323 ? -20.198 20.347  -13.842 1   29    ? 308 CYS   A CA  1 
ATOM   2437 C  C   . CYS   A 1 323 ? -20.704 20.651  -12.385 1   28.51 ? 308 CYS   A C   1 
ATOM   2438 O  O   . CYS   A 1 323 ? -21.858 20.375  -12.082 1   28.64 ? 308 CYS   A O   1 
ATOM   2439 C  CB  . CYS   A 1 323 ? -19.758 18.906  -14.073 1   33.27 ? 308 CYS   A CB  1 
ATOM   2440 S  SG  . CYS   A 1 323 ? -18.179 18.492  -13.311 1   43.76 ? 308 CYS   A SG  1 
ATOM   2441 N  N   . SER   A 1 324 ? -19.927 21.389  -11.58  1   27.86 ? 309 SER   A N   1 
ATOM   2442 C  CA  . SER   A 1 324 ? -20.349 21.869  -10.271 1   28.49 ? 309 SER   A CA  1 
ATOM   2443 C  C   . SER   A 1 324 ? -21.476 22.915  -10.431 1   29.4  ? 309 SER   A C   1 
ATOM   2444 O  O   . SER   A 1 324 ? -22.458 22.857  -9.685  1   29.66 ? 309 SER   A O   1 
ATOM   2445 C  CB  . SER   A 1 324 ? -19.174 22.489  -9.524  1   29.03 ? 309 SER   A CB  1 
ATOM   2446 O  OG  . SER   A 1 324 ? -18.278 21.433  -9.224  1   32.75 ? 309 SER   A OG  1 
ATOM   2447 N  N   . LEU   A 1 325 ? -21.338 23.861  -11.388 1   28.72 ? 310 LEU   A N   1 
ATOM   2448 C  CA  . LEU   A 1 325 ? -22.401 24.842  -11.694 1   29.16 ? 310 LEU   A CA  1 
ATOM   2449 C  C   . LEU   A 1 325 ? -23.693 24.115  -12.113 1   28.03 ? 310 LEU   A C   1 
ATOM   2450 O  O   . LEU   A 1 325 ? -24.793 24.543  -11.758 1   27.2  ? 310 LEU   A O   1 
ATOM   2451 C  CB  . LEU   A 1 325 ? -21.993 25.737  -12.878 1   30.11 ? 310 LEU   A CB  1 
ATOM   2452 C  CG  . LEU   A 1 325 ? -21.211 27.001  -12.643 1   33.06 ? 310 LEU   A CG  1 
ATOM   2453 C  CD1 . LEU   A 1 325 ? -21.147 27.792  -13.96  1   34.13 ? 310 LEU   A CD1 1 
ATOM   2454 C  CD2 . LEU   A 1 325 ? -21.821 27.851  -11.522 1   33    ? 310 LEU   A CD2 1 
ATOM   2455 N  N   . GLU   A 1 326 ? -23.566 23.048  -12.906 1   27.44 ? 311 GLU   A N   1 
ATOM   2456 C  CA  . GLU   A 1 326 ? -24.72  22.272  -13.372 1   27.67 ? 311 GLU   A CA  1 
ATOM   2457 C  C   . GLU   A 1 326 ? -25.446 21.562  -12.237 1   27.46 ? 311 GLU   A C   1 
ATOM   2458 O  O   . GLU   A 1 326 ? -26.619 21.256  -12.381 1   27.82 ? 311 GLU   A O   1 
ATOM   2459 C  CB  . GLU   A 1 326 ? -24.29  21.217  -14.403 1   29.83 ? 311 GLU   A CB  1 
ATOM   2460 C  CG  . GLU   A 1 326 ? -24.115 21.763  -15.796 1   33.5  ? 311 GLU   A CG  1 
ATOM   2461 C  CD  . GLU   A 1 326 ? -23.46  20.795  -16.762 1   39.3  ? 311 GLU   A CD  1 
ATOM   2462 O  OE1 . GLU   A 1 326 ? -22.738 19.881  -16.304 1   36.89 ? 311 GLU   A OE1 1 
ATOM   2463 O  OE2 . GLU   A 1 326 ? -23.638 20.978  -17.987 1   41.66 ? 311 GLU   A OE2 1 
ATOM   2464 N  N   . SER   A 1 327 ? -24.737 21.252  -11.133 1   26.51 ? 312 SER   A N   1 
ATOM   2465 C  CA  . SER   A 1 327 ? -25.3   20.581  -9.959  1   27.02 ? 312 SER   A CA  1 
ATOM   2466 C  C   . SER   A 1 327 ? -26.088 21.54   -9.037  1   27.23 ? 312 SER   A C   1 
ATOM   2467 O  O   . SER   A 1 327 ? -26.828 21.093  -8.163  1   27.04 ? 312 SER   A O   1 
ATOM   2468 C  CB  . SER   A 1 327 ? -24.175 19.923  -9.168  1   29.31 ? 312 SER   A CB  1 
ATOM   2469 O  OG  . SER   A 1 327 ? -23.417 19.044  -9.994  1   34.11 ? 312 SER   A OG  1 
ATOM   2470 N  N   . ASN   A 1 328 ? -25.901 22.847  -9.211  1   27.17 ? 313 ASN   A N   1 
ATOM   2471 C  CA  . ASN   A 1 328 ? -26.595 23.859  -8.434  1   27.93 ? 313 ASN   A CA  1 
ATOM   2472 C  C   . ASN   A 1 328 ? -28.017 24.076  -8.93   1   27.63 ? 313 ASN   A C   1 
ATOM   2473 O  O   . ASN   A 1 328 ? -28.345 23.714  -10.06  1   26.39 ? 313 ASN   A O   1 
ATOM   2474 C  CB  . ASN   A 1 328 ? -25.79  25.15   -8.447  1   28.82 ? 313 ASN   A CB  1 
ATOM   2475 C  CG  . ASN   A 1 328 ? -24.766 25.144  -7.363  1   32.16 ? 313 ASN   A CG  1 
ATOM   2476 O  OD1 . ASN   A 1 328 ? -24.954 25.729  -6.288  1   35.46 ? 313 ASN   A OD1 1 
ATOM   2477 N  ND2 . ASN   A 1 328 ? -23.681 24.424  -7.601  1   29.62 ? 313 ASN   A ND2 1 
ATOM   2478 N  N   . PRO   A 1 329 ? -28.912 24.649  -8.081  1   28.35 ? 314 PRO   A N   1 
ATOM   2479 C  CA  . PRO   A 1 329 ? -30.289 24.888  -8.536  1   27.97 ? 314 PRO   A CA  1 
ATOM   2480 C  C   . PRO   A 1 329 ? -30.345 25.792  -9.747  1   26.81 ? 314 PRO   A C   1 
ATOM   2481 O  O   . PRO   A 1 329 ? -29.456 26.635  -9.963  1   26.48 ? 314 PRO   A O   1 
ATOM   2482 C  CB  . PRO   A 1 329 ? -30.974 25.532  -7.318  1   29.15 ? 314 PRO   A CB  1 
ATOM   2483 C  CG  . PRO   A 1 329 ? -30.118 25.158  -6.146  1   29.64 ? 314 PRO   A CG  1 
ATOM   2484 C  CD  . PRO   A 1 329 ? -28.706 25.126  -6.699  1   27.96 ? 314 PRO   A CD  1 
ATOM   2485 N  N   . SER   A 1 330 ? -31.377 25.605  -10.554 1   25.73 ? 315 SER   A N   1 
ATOM   2486 C  CA  . SER   A 1 330 ? -31.548 26.372  -11.769 1   25.67 ? 315 SER   A CA  1 
ATOM   2487 C  C   . SER   A 1 330 ? -31.97  27.828  -11.521 1   26.09 ? 315 SER   A C   1 
ATOM   2488 O  O   . SER   A 1 330 ? -33.014 28.093  -10.894 1   25.53 ? 315 SER   A O   1 
ATOM   2489 C  CB  . SER   A 1 330 ? -32.547 25.673  -12.688 1   26.88 ? 315 SER   A CB  1 
ATOM   2490 O  OG  . SER   A 1 330 ? -32.8   26.425  -13.866 1   29.67 ? 315 SER   A OG  1 
ATOM   2491 N  N   . VAL   A 1 331 ? -31.165 28.773  -12.029 1   25.88 ? 316 VAL   A N   1 
ATOM   2492 C  CA  . VAL   A 1 331 ? -31.452 30.202  -11.972 1   26.61 ? 316 VAL   A CA  1 
ATOM   2493 C  C   . VAL   A 1 331 ? -32.665 30.493  -12.879 1   26.77 ? 316 VAL   A C   1 
ATOM   2494 O  O   . VAL   A 1 331 ? -33.583 31.23   -12.489 1   26.9  ? 316 VAL   A O   1 
ATOM   2495 C  CB  . VAL   A 1 331 ? -30.194 31.003  -12.408 1   27.69 ? 316 VAL   A CB  1 
ATOM   2496 C  CG1 . VAL   A 1 331 ? -30.503 32.486  -12.569 1   27.93 ? 316 VAL   A CG1 1 
ATOM   2497 C  CG2 . VAL   A 1 331 ? -29.044 30.782  -11.424 1   28.11 ? 316 VAL   A CG2 1 
ATOM   2498 N  N   . ARG   A 1 332 ? -32.68  29.891  -14.079 1   26.06 ? 317 ARG   A N   1 
ATOM   2499 C  CA  . ARG   A 1 332 ? -33.773 30.046  -15.029 1   26.67 ? 317 ARG   A CA  1 
ATOM   2500 C  C   . ARG   A 1 332 ? -35.106 29.574  -14.4   1   27.36 ? 317 ARG   A C   1 
ATOM   2501 O  O   . ARG   A 1 332 ? -36.091 30.295  -14.488 1   27.67 ? 317 ARG   A O   1 
ATOM   2502 C  CB  . ARG   A 1 332 ? -33.51  29.234  -16.297 1   27.21 ? 317 ARG   A CB  1 
ATOM   2503 C  CG  . ARG   A 1 332 ? -34.66  29.339  -17.29  1   28.91 ? 317 ARG   A CG  1 
ATOM   2504 C  CD  . ARG   A 1 332 ? -34.424 28.5    -18.537 1   31.05 ? 317 ARG   A CD  1 
ATOM   2505 N  NE  . ARG   A 1 332 ? -35.545 28.565  -19.484 1   32.39 ? 317 ARG   A NE  1 
ATOM   2506 C  CZ  . ARG   A 1 332 ? -35.781 29.584  -20.3   1   31.04 ? 317 ARG   A CZ  1 
ATOM   2507 N  NH1 . ARG   A 1 332 ? -35.006 30.653  -20.274 1   30.24 ? 317 ARG   A NH1 1 
ATOM   2508 N  NH2 . ARG   A 1 332 ? -36.818 29.554  -21.128 1   29.41 ? 317 ARG   A NH2 1 
ATOM   2509 N  N   . GLU   A 1 333 ? -35.126 28.375  -13.801 1   27.08 ? 318 GLU   A N   1 
ATOM   2510 C  CA  . GLU   A 1 333 ? -36.357 27.863  -13.187 1   28.44 ? 318 GLU   A CA  1 
ATOM   2511 C  C   . GLU   A 1 333 ? -36.82  28.736  -12.031 1   28.53 ? 318 GLU   A C   1 
ATOM   2512 O  O   . GLU   A 1 333 ? -38.022 28.978  -11.88  1   29.96 ? 318 GLU   A O   1 
ATOM   2513 C  CB  . GLU   A 1 333 ? -36.169 26.411  -12.744 1   31.57 ? 318 GLU   A CB  1 
ATOM   2514 C  CG  . GLU   A 1 333 ? -36.124 25.447  -13.921 1   39.66 ? 318 GLU   A CG  1 
ATOM   2515 N  N   . PHE   A 1 334 ? -35.876 29.241  -11.22  1   27.91 ? 319 PHE   A N   1 
ATOM   2516 C  CA  . PHE   A 1 334 ? -36.199 30.142  -10.127 1   28.41 ? 319 PHE   A CA  1 
ATOM   2517 C  C   . PHE   A 1 334 ? -36.903 31.406  -10.653 1   28.11 ? 319 PHE   A C   1 
ATOM   2518 O  O   . PHE   A 1 334 ? -37.964 31.763  -10.137 1   28.17 ? 319 PHE   A O   1 
ATOM   2519 C  CB  . PHE   A 1 334 ? -34.934 30.523  -9.361  1   29.2  ? 319 PHE   A CB  1 
ATOM   2520 C  CG  . PHE   A 1 334 ? -35.153 31.311  -8.089  1   31.08 ? 319 PHE   A CG  1 
ATOM   2521 C  CD1 . PHE   A 1 334 ? -35.266 32.689  -8.117  1   32.46 ? 319 PHE   A CD1 1 
ATOM   2522 C  CD2 . PHE   A 1 334 ? -35.178 30.677  -6.861  1   32.49 ? 319 PHE   A CD2 1 
ATOM   2523 C  CE1 . PHE   A 1 334 ? -35.437 33.415  -6.941  1   33.25 ? 319 PHE   A CE1 1 
ATOM   2524 C  CE2 . PHE   A 1 334 ? -35.321 31.404  -5.688  1   33.76 ? 319 PHE   A CE2 1 
ATOM   2525 C  CZ  . PHE   A 1 334 ? -35.421 32.77   -5.731  1   33.75 ? 319 PHE   A CZ  1 
ATOM   2526 N  N   . VAL   A 1 335 ? -36.325 32.064  -11.678 1   26.49 ? 320 VAL   A N   1 
ATOM   2527 C  CA  . VAL   A 1 335 ? -36.899 33.29   -12.247 1   27.12 ? 320 VAL   A CA  1 
ATOM   2528 C  C   . VAL   A 1 335 ? -38.234 33.02   -12.964 1   28.51 ? 320 VAL   A C   1 
ATOM   2529 O  O   . VAL   A 1 335 ? -39.179 33.787  -12.807 1   28.65 ? 320 VAL   A O   1 
ATOM   2530 C  CB  . VAL   A 1 335 ? -35.885 33.998  -13.178 1   27.73 ? 320 VAL   A CB  1 
ATOM   2531 C  CG1 . VAL   A 1 335 ? -36.536 35.177  -13.898 1   28.57 ? 320 VAL   A CG1 1 
ATOM   2532 C  CG2 . VAL   A 1 335 ? -34.664 34.478  -12.381 1   28.13 ? 320 VAL   A CG2 1 
ATOM   2533 N  N   . LEU   A 1 336 ? -38.324 31.928  -13.722 1   30.18 ? 321 LEU   A N   1 
ATOM   2534 C  CA  . LEU   A 1 336 ? -39.549 31.575  -14.436 1   33.82 ? 321 LEU   A CA  1 
ATOM   2535 C  C   . LEU   A 1 336 ? -40.749 31.374  -13.497 1   36.27 ? 321 LEU   A C   1 
ATOM   2536 O  O   . LEU   A 1 336 ? -41.897 31.581  -13.908 1   37.16 ? 321 LEU   A O   1 
ATOM   2537 C  CB  . LEU   A 1 336 ? -39.351 30.267  -15.197 1   35.09 ? 321 LEU   A CB  1 
ATOM   2538 C  CG  . LEU   A 1 336 ? -39.159 30.367  -16.689 1   38.81 ? 321 LEU   A CG  1 
ATOM   2539 C  CD1 . LEU   A 1 336 ? -38.99  28.986  -17.29  1   40.52 ? 321 LEU   A CD1 1 
ATOM   2540 C  CD2 . LEU   A 1 336 ? -40.329 31.067  -17.37  1   40.17 ? 321 LEU   A CD2 1 
ATOM   2541 N  N   . SER   A 1 337 ? -40.493 30.923  -12.27  1   36.68 ? 322 SER   A N   1 
ATOM   2542 C  CA  . SER   A 1 337 ? -41.572 30.607  -11.342 1   37.91 ? 322 SER   A CA  1 
ATOM   2543 C  C   . SER   A 1 337 ? -41.997 31.778  -10.444 1   39.77 ? 322 SER   A C   1 
ATOM   2544 O  O   . SER   A 1 337 ? -42.845 31.567  -9.575  1   40.27 ? 322 SER   A O   1 
ATOM   2545 C  CB  . SER   A 1 337 ? -41.155 29.428  -10.466 1   37.7  ? 322 SER   A CB  1 
ATOM   2546 O  OG  . SER   A 1 337 ? -40.161 29.828  -9.535  1   39.03 ? 322 SER   A OG  1 
ATOM   2547 N  N   . LYS   A 1 338 ? -41.417 32.983  -10.62  1   39.78 ? 323 LYS   A N   1 
ATOM   2548 C  CA  . LYS   A 1 338 ? -41.684 34.078  -9.703  1   39.91 ? 323 LYS   A CA  1 
ATOM   2549 C  C   . LYS   A 1 338 ? -42.745 35.125  -10.091 1   40.16 ? 323 LYS   A C   1 
ATOM   2550 O  O   . LYS   A 1 338 ? -43.126 35.886  -9.189  1   42.2  ? 323 LYS   A O   1 
ATOM   2551 C  CB  . LYS   A 1 338 ? -40.401 34.83   -9.348  1   40.76 ? 323 LYS   A CB  1 
ATOM   2552 C  CG  . LYS   A 1 338 ? -39.4   34.022  -8.519  1   44    ? 323 LYS   A CG  1 
ATOM   2553 C  CD  . LYS   A 1 338 ? -39.92  33.554  -7.181  1   47.43 ? 323 LYS   A CD  1 
ATOM   2554 C  CE  . LYS   A 1 338 ? -39.037 32.483  -6.593  1   49.61 ? 323 LYS   A CE  1 
ATOM   2555 N  NZ  . LYS   A 1 338 ? -39.073 31.253  -7.431  1   51.28 ? 323 LYS   A NZ  1 
ATOM   2556 N  N   . GLY   A 1 339 ? -43.19  35.22   -11.35  1   37.53 ? 324 GLY   A N   1 
ATOM   2557 C  CA  . GLY   A 1 339 ? -44.176 36.243  -11.738 1   35.22 ? 324 GLY   A CA  1 
ATOM   2558 C  C   . GLY   A 1 339 ? -43.744 37.664  -11.37  1   32.82 ? 324 GLY   A C   1 
ATOM   2559 O  O   . GLY   A 1 339 ? -44.505 38.459  -10.794 1   32.22 ? 324 GLY   A O   1 
ATOM   2560 N  N   . ASP   A 1 340 ? -42.465 37.955  -11.617 1   30.75 ? 325 ASP   A N   1 
ATOM   2561 C  CA  . ASP   A 1 340 ? -41.825 39.189  -11.196 1   28.79 ? 325 ASP   A CA  1 
ATOM   2562 C  C   . ASP   A 1 340 ? -41.179 39.795  -12.416 1   29.04 ? 325 ASP   A C   1 
ATOM   2563 O  O   . ASP   A 1 340 ? -40.151 39.276  -12.869 1   28.88 ? 325 ASP   A O   1 
ATOM   2564 C  CB  . ASP   A 1 340 ? -40.773 38.812  -10.131 1   27.45 ? 325 ASP   A CB  1 
ATOM   2565 C  CG  . ASP   A 1 340 ? -39.988 39.947  -9.497  1   29.37 ? 325 ASP   A CG  1 
ATOM   2566 O  OD1 . ASP   A 1 340 ? -39.774 40.986  -10.175 1   29.88 ? 325 ASP   A OD1 1 
ATOM   2567 O  OD2 . ASP   A 1 340 ? -39.543 39.784  -8.35   1   30.26 ? 325 ASP   A OD2 1 
ATOM   2568 N  N   . ALA   A 1 341 ? -41.796 40.854  -12.977 1   28.08 ? 326 ALA   A N   1 
ATOM   2569 C  CA  . ALA   A 1 341 ? -41.315 41.493  -14.191 1   28.9  ? 326 ALA   A CA  1 
ATOM   2570 C  C   . ALA   A 1 341 ? -39.887 42.037  -14.066 1   29.05 ? 326 ALA   A C   1 
ATOM   2571 O  O   . ALA   A 1 341 ? -39.096 41.879  -14.995 1   29.77 ? 326 ALA   A O   1 
ATOM   2572 C  CB  . ALA   A 1 341 ? -42.273 42.592  -14.646 1   28.44 ? 326 ALA   A CB  1 
ATOM   2573 N  N   . GLY   A 1 342 ? -39.565 42.655  -12.943 1   28.13 ? 327 GLY   A N   1 
ATOM   2574 C  CA  . GLY   A 1 342 ? -38.22  43.171  -12.714 1   28.06 ? 327 GLY   A CA  1 
ATOM   2575 C  C   . GLY   A 1 342 ? -37.157 42.074  -12.747 1   27.8  ? 327 GLY   A C   1 
ATOM   2576 O  O   . GLY   A 1 342 ? -36.088 42.256  -13.338 1   27.31 ? 327 GLY   A O   1 
ATOM   2577 N  N   . LEU   A 1 343 ? -37.44  40.93   -12.121 1   26.92 ? 328 LEU   A N   1 
ATOM   2578 C  CA  . LEU   A 1 343 ? -36.502 39.802  -12.079 1   27.03 ? 328 LEU   A CA  1 
ATOM   2579 C  C   . LEU   A 1 343 ? -36.354 39.133  -13.449 1   26.3  ? 328 LEU   A C   1 
ATOM   2580 O  O   . LEU   A 1 343 ? -35.24  38.771  -13.826 1   26.27 ? 328 LEU   A O   1 
ATOM   2581 C  CB  . LEU   A 1 343 ? -36.995 38.766  -11.064 1   27.77 ? 328 LEU   A CB  1 
ATOM   2582 C  CG  . LEU   A 1 343 ? -35.959 37.884  -10.379 1   29.88 ? 328 LEU   A CG  1 
ATOM   2583 C  CD1 . LEU   A 1 343 ? -34.79  38.719  -9.761  1   29.96 ? 328 LEU   A CD1 1 
ATOM   2584 C  CD2 . LEU   A 1 343 ? -36.635 37.043  -9.304  1   31.09 ? 328 LEU   A CD2 1 
ATOM   2585 N  N   . ARG   A 1 344 ? -37.469 39.013  -14.203 1   25.7  ? 329 ARG   A N   1 
ATOM   2586 C  CA  . ARG   A 1 344 ? -37.47  38.43   -15.538 1   25.22 ? 329 ARG   A CA  1 
ATOM   2587 C  C   . ARG   A 1 344 ? -36.689 39.313  -16.488 1   25.22 ? 329 ARG   A C   1 
ATOM   2588 O  O   . ARG   A 1 344 ? -35.941 38.798  -17.328 1   24.55 ? 329 ARG   A O   1 
ATOM   2589 C  CB  . ARG   A 1 344 ? -38.908 38.206  -16.046 1   26.35 ? 329 ARG   A CB  1 
ATOM   2590 C  CG  . ARG   A 1 344 ? -39.607 37.043  -15.353 1   29.55 ? 329 ARG   A CG  1 
ATOM   2591 C  CD  . ARG   A 1 344 ? -41.089 37.004  -15.649 1   34.61 ? 329 ARG   A CD  1 
ATOM   2592 N  NE  . ARG   A 1 344 ? -41.369 36.179  -16.809 1   39.18 ? 329 ARG   A NE  1 
ATOM   2593 C  CZ  . ARG   A 1 344 ? -41.661 34.882  -16.756 1   42.98 ? 329 ARG   A CZ  1 
ATOM   2594 N  NH1 . ARG   A 1 344 ? -41.741 34.257  -15.583 1   43.51 ? 329 ARG   A NH1 1 
ATOM   2595 N  NH2 . ARG   A 1 344 ? -41.908 34.206  -17.869 1   43.16 ? 329 ARG   A NH2 1 
ATOM   2596 N  N   . GLU   A 1 345 ? -36.824 40.65   -16.349 1   25.32 ? 330 GLU   A N   1 
ATOM   2597 C  CA  . GLU   A 1 345 ? -36.093 41.573  -17.207 1   26.23 ? 330 GLU   A CA  1 
ATOM   2598 C  C   . GLU   A 1 345 ? -34.599 41.506  -16.963 1   25.46 ? 330 GLU   A C   1 
ATOM   2599 O  O   . GLU   A 1 345 ? -33.834 41.621  -17.919 1   25.23 ? 330 GLU   A O   1 
ATOM   2600 C  CB  . GLU   A 1 345 ? -36.561 43.013  -16.987 1   30.03 ? 330 GLU   A CB  1 
ATOM   2601 C  CG  . GLU   A 1 345 ? -37.861 43.334  -17.697 1   39.35 ? 330 GLU   A CG  1 
ATOM   2602 C  CD  . GLU   A 1 345 ? -38.354 44.713  -17.295 1   52.52 ? 330 GLU   A CD  1 
ATOM   2603 O  OE1 . GLU   A 1 345 ? -37.557 45.677  -17.394 1   56.25 ? 330 GLU   A OE1 1 
ATOM   2604 O  OE2 . GLU   A 1 345 ? -39.521 44.828  -16.853 1   56.07 ? 330 GLU   A OE2 1 
ATOM   2605 N  N   . ALA   A 1 346 ? -34.179 41.37   -15.69  1   24.62 ? 331 ALA   A N   1 
ATOM   2606 C  CA  . ALA   A 1 346 ? -32.762 41.301  -15.348 1   24.5  ? 331 ALA   A CA  1 
ATOM   2607 C  C   . ALA   A 1 346 ? -32.16  39.988  -15.897 1   24.07 ? 331 ALA   A C   1 
ATOM   2608 O  O   . ALA   A 1 346 ? -31.059 40.022  -16.443 1   24.11 ? 331 ALA   A O   1 
ATOM   2609 C  CB  . ALA   A 1 346 ? -32.583 41.382  -13.853 1   24.72 ? 331 ALA   A CB  1 
ATOM   2610 N  N   . TYR   A 1 347 ? -32.905 38.87   -15.819 1   23.25 ? 332 TYR   A N   1 
ATOM   2611 C  CA  . TYR   A 1 347 ? -32.484 37.582  -16.378 1   22.69 ? 332 TYR   A CA  1 
ATOM   2612 C  C   . TYR   A 1 347 ? -32.354 37.723  -17.9   1   23.89 ? 332 TYR   A C   1 
ATOM   2613 O  O   . TYR   A 1 347 ? -31.345 37.304  -18.48  1   23.51 ? 332 TYR   A O   1 
ATOM   2614 C  CB  . TYR   A 1 347 ? -33.486 36.469  -16.009 1   20.97 ? 332 TYR   A CB  1 
ATOM   2615 C  CG  . TYR   A 1 347 ? -33.257 35.177  -16.768 1   20.56 ? 332 TYR   A CG  1 
ATOM   2616 C  CD1 . TYR   A 1 347 ? -32.355 34.227  -16.308 1   21.01 ? 332 TYR   A CD1 1 
ATOM   2617 C  CD2 . TYR   A 1 347 ? -33.919 34.921  -17.961 1   20.14 ? 332 TYR   A CD2 1 
ATOM   2618 C  CE1 . TYR   A 1 347 ? -32.131 33.047  -17.009 1   22.23 ? 332 TYR   A CE1 1 
ATOM   2619 C  CE2 . TYR   A 1 347 ? -33.711 33.742  -18.666 1   21.02 ? 332 TYR   A CE2 1 
ATOM   2620 C  CZ  . TYR   A 1 347 ? -32.807 32.807  -18.19  1   22.17 ? 332 TYR   A CZ  1 
ATOM   2621 O  OH  . TYR   A 1 347 ? -32.55  31.647  -18.897 1   22.79 ? 332 TYR   A OH  1 
ATOM   2622 N  N   . ASP   A 1 348 ? -33.356 38.342  -18.547 1   23.54 ? 333 ASP   A N   1 
ATOM   2623 C  CA  . ASP   A 1 348 ? -33.328 38.536  -19.987 1   23.38 ? 333 ASP   A CA  1 
ATOM   2624 C  C   . ASP   A 1 348 ? -32.215 39.461  -20.433 1   23.72 ? 333 ASP   A C   1 
ATOM   2625 O  O   . ASP   A 1 348 ? -31.713 39.299  -21.537 1   23.09 ? 333 ASP   A O   1 
ATOM   2626 C  CB  . ASP   A 1 348 ? -34.672 39.033  -20.52  1   24.76 ? 333 ASP   A CB  1 
ATOM   2627 C  CG  . ASP   A 1 348 ? -35.687 37.951  -20.777 1   28.46 ? 333 ASP   A CG  1 
ATOM   2628 O  OD1 . ASP   A 1 348 ? -35.393 36.763  -20.481 1   27.84 ? 333 ASP   A OD1 1 
ATOM   2629 O  OD2 . ASP   A 1 348 ? -36.785 38.28   -21.282 1   31.16 ? 333 ASP   A OD2 1 
ATOM   2630 N  N   . ALA   A 1 349 ? -31.804 40.424  -19.592 1   23.26 ? 334 ALA   A N   1 
ATOM   2631 C  CA  . ALA   A 1 349 ? -30.706 41.323  -19.95  1   23.19 ? 334 ALA   A CA  1 
ATOM   2632 C  C   . ALA   A 1 349 ? -29.397 40.477  -20.109 1   22.54 ? 334 ALA   A C   1 
ATOM   2633 O  O   . ALA   A 1 349 ? -28.594 40.771  -20.985 1   21.57 ? 334 ALA   A O   1 
ATOM   2634 C  CB  . ALA   A 1 349 ? -30.525 42.378  -18.878 1   23.08 ? 334 ALA   A CB  1 
ATOM   2635 N  N   . CYS   A 1 350 ? -29.244 39.409  -19.283 1   21.79 ? 335 CYS   A N   1 
ATOM   2636 C  CA  . CYS   A 1 350 ? -28.098 38.503  -19.336 1   22.01 ? 335 CYS   A CA  1 
ATOM   2637 C  C   . CYS   A 1 350 ? -28.135 37.688  -20.615 1   22.34 ? 335 CYS   A C   1 
ATOM   2638 O  O   . CYS   A 1 350 ? -27.13  37.635  -21.346 1   22.07 ? 335 CYS   A O   1 
ATOM   2639 C  CB  . CYS   A 1 350 ? -28.075 37.603  -18.104 1   22.66 ? 335 CYS   A CB  1 
ATOM   2640 S  SG  . CYS   A 1 350 ? -27.644 38.464  -16.563 1   25.24 ? 335 CYS   A SG  1 
ATOM   2641 N  N   . VAL   A 1 351 ? -29.297 37.075  -20.905 1   21.88 ? 336 VAL   A N   1 
ATOM   2642 C  CA  . VAL   A 1 351 ? -29.494 36.251  -22.105 1   22.36 ? 336 VAL   A CA  1 
ATOM   2643 C  C   . VAL   A 1 351 ? -29.316 37.101  -23.353 1   22.57 ? 336 VAL   A C   1 
ATOM   2644 O  O   . VAL   A 1 351 ? -28.62  36.677  -24.285 1   21.63 ? 336 VAL   A O   1 
ATOM   2645 C  CB  . VAL   A 1 351 ? -30.862 35.554  -22.073 1   22.93 ? 336 VAL   A CB  1 
ATOM   2646 C  CG1 . VAL   A 1 351 ? -31.13  34.806  -23.364 1   22.84 ? 336 VAL   A CG1 1 
ATOM   2647 C  CG2 . VAL   A 1 351 ? -30.976 34.607  -20.877 1   23    ? 336 VAL   A CG2 1 
ATOM   2648 N  N   . LYS   A 1 352 ? -29.883 38.335  -23.345 1   21.94 ? 337 LYS   A N   1 
ATOM   2649 C  CA  . LYS   A 1 352 ? -29.747 39.277  -24.444 1   22.75 ? 337 LYS   A CA  1 
ATOM   2650 C  C   . LYS   A 1 352 ? -28.301 39.62   -24.708 1   22.57 ? 337 LYS   A C   1 
ATOM   2651 O  O   . LYS   A 1 352 ? -27.897 39.649  -25.863 1   22.73 ? 337 LYS   A O   1 
ATOM   2652 C  CB  . LYS   A 1 352 ? -30.531 40.577  -24.186 1   26.24 ? 337 LYS   A CB  1 
ATOM   2653 C  CG  . LYS   A 1 352 ? -30.575 41.501  -25.4   1   31.57 ? 337 LYS   A CG  1 
ATOM   2654 N  N   . ALA   A 1 353 ? -27.496 39.865  -23.65  1   21.51 ? 338 ALA   A N   1 
ATOM   2655 C  CA  . ALA   A 1 353 ? -26.091 40.18   -23.829 1   20.37 ? 338 ALA   A CA  1 
ATOM   2656 C  C   . ALA   A 1 353 ? -25.35  39.004  -24.517 1   19.29 ? 338 ALA   A C   1 
ATOM   2657 O  O   . ALA   A 1 353 ? -24.51  39.255  -25.38  1   19.39 ? 338 ALA   A O   1 
ATOM   2658 C  CB  . ALA   A 1 353 ? -25.454 40.518  -22.494 1   19.79 ? 338 ALA   A CB  1 
ATOM   2659 N  N   . LEU   A 1 354 ? -25.711 37.755  -24.207 1   18.51 ? 339 LEU   A N   1 
ATOM   2660 C  CA  . LEU   A 1 354 ? -25.109 36.593  -24.885 1   20.11 ? 339 LEU   A CA  1 
ATOM   2661 C  C   . LEU   A 1 354 ? -25.595 36.497  -26.339 1   19.3  ? 339 LEU   A C   1 
ATOM   2662 O  O   . LEU   A 1 354 ? -24.8   36.165  -27.23  1   20.15 ? 339 LEU   A O   1 
ATOM   2663 C  CB  . LEU   A 1 354 ? -25.427 35.271  -24.172 1   21.51 ? 339 LEU   A CB  1 
ATOM   2664 C  CG  . LEU   A 1 354 ? -24.662 35.023  -22.866 1   23.73 ? 339 LEU   A CG  1 
ATOM   2665 C  CD1 . LEU   A 1 354 ? -25.176 33.786  -22.199 1   23.8  ? 339 LEU   A CD1 1 
ATOM   2666 C  CD2 . LEU   A 1 354 ? -23.159 34.953  -23.129 1   24.89 ? 339 LEU   A CD2 1 
ATOM   2667 N  N   . VAL   A 1 355 ? -26.871 36.786  -26.603 1   17.85 ? 340 VAL   A N   1 
ATOM   2668 C  CA  . VAL   A 1 355 ? -27.399 36.798  -27.989 1   18.29 ? 340 VAL   A CA  1 
ATOM   2669 C  C   . VAL   A 1 355 ? -26.639 37.877  -28.792 1   18.65 ? 340 VAL   A C   1 
ATOM   2670 O  O   . VAL   A 1 355 ? -26.206 37.609  -29.914 1   18.73 ? 340 VAL   A O   1 
ATOM   2671 C  CB  . VAL   A 1 355 ? -28.923 37.088  -28.066 1   18.68 ? 340 VAL   A CB  1 
ATOM   2672 C  CG1 . VAL   A 1 355 ? -29.378 37.289  -29.514 1   18.73 ? 340 VAL   A CG1 1 
ATOM   2673 C  CG2 . VAL   A 1 355 ? -29.721 35.991  -27.391 1   19.34 ? 340 VAL   A CG2 1 
ATOM   2674 N  N   . SER   A 1 356 ? -26.443 39.068  -28.2   1   19.1  ? 341 SER   A N   1 
ATOM   2675 C  CA  . SER   A 1 356 ? -25.738 40.149  -28.887 1   19.97 ? 341 SER   A CA  1 
ATOM   2676 C  C   . SER   A 1 356 ? -24.312 39.743  -29.238 1   20.17 ? 341 SER   A C   1 
ATOM   2677 O  O   . SER   A 1 356 ? -23.846 40.056  -30.335 1   21.85 ? 341 SER   A O   1 
ATOM   2678 C  CB  . SER   A 1 356 ? -25.748 41.413  -28.039 1   22.87 ? 341 SER   A CB  1 
ATOM   2679 O  OG  . SER   A 1 356 ? -27.095 41.833  -27.849 1   24.87 ? 341 SER   A OG  1 
ATOM   2680 N  N   . LEU   A 1 357 ? -23.591 39.103  -28.284 1   19.06 ? 342 LEU   A N   1 
ATOM   2681 C  CA  . LEU   A 1 357 ? -22.234 38.625  -28.495 1   19.64 ? 342 LEU   A CA  1 
ATOM   2682 C  C   . LEU   A 1 357 ? -22.217 37.629  -29.659 1   18.15 ? 342 LEU   A C   1 
ATOM   2683 O  O   . LEU   A 1 357 ? -21.389 37.758  -30.559 1   18.05 ? 342 LEU   A O   1 
ATOM   2684 C  CB  . LEU   A 1 357 ? -21.708 37.944  -27.207 1   20.23 ? 342 LEU   A CB  1 
ATOM   2685 C  CG  . LEU   A 1 357 ? -21.057 38.894  -26.222 1   23.22 ? 342 LEU   A CG  1 
ATOM   2686 C  CD1 . LEU   A 1 357 ? -21.007 38.303  -24.836 1   24.04 ? 342 LEU   A CD1 1 
ATOM   2687 C  CD2 . LEU   A 1 357 ? -19.654 39.283  -26.707 1   24.54 ? 342 LEU   A CD2 1 
ATOM   2688 N  N   . ARG   A 1 358 ? -23.135 36.66   -29.642 1   17.26 ? 343 ARG   A N   1 
ATOM   2689 C  CA  . ARG   A 1 358 ? -23.172 35.615  -30.672 1   18.34 ? 343 ARG   A CA  1 
ATOM   2690 C  C   . ARG   A 1 358 ? -23.552 36.137  -32.057 1   19.76 ? 343 ARG   A C   1 
ATOM   2691 O  O   . ARG   A 1 358 ? -23.004 35.672  -33.069 1   20.19 ? 343 ARG   A O   1 
ATOM   2692 C  CB  . ARG   A 1 358 ? -24.088 34.472  -30.223 1   18.1  ? 343 ARG   A CB  1 
ATOM   2693 C  CG  . ARG   A 1 358 ? -23.422 33.768  -29.039 1   17.52 ? 343 ARG   A CG  1 
ATOM   2694 C  CD  . ARG   A 1 358 ? -24.146 32.578  -28.461 1   16.52 ? 343 ARG   A CD  1 
ATOM   2695 N  NE  . ARG   A 1 358 ? -23.177 31.796  -27.675 1   19.94 ? 343 ARG   A NE  1 
ATOM   2696 C  CZ  . ARG   A 1 358 ? -23.371 31.354  -26.436 1   23.06 ? 343 ARG   A CZ  1 
ATOM   2697 N  NH1 . ARG   A 1 358 ? -24.536 31.549  -25.827 1   19.8  ? 343 ARG   A NH1 1 
ATOM   2698 N  NH2 . ARG   A 1 358 ? -22.411 30.677  -25.806 1   20.8  ? 343 ARG   A NH2 1 
ATOM   2699 N  N   . SER   A 1 359 ? -24.444 37.13   -32.099 1   18.51 ? 344 SER   A N   1 
ATOM   2700 C  CA  . SER   A 1 359 ? -24.868 37.766  -33.354 1   19.09 ? 344 SER   A CA  1 
ATOM   2701 C  C   . SER   A 1 359 ? -23.681 38.548  -33.941 1   18.04 ? 344 SER   A C   1 
ATOM   2702 O  O   . SER   A 1 359 ? -23.417 38.433  -35.143 1   18.07 ? 344 SER   A O   1 
ATOM   2703 C  CB  . SER   A 1 359 ? -26.041 38.726  -33.106 1   20.69 ? 344 SER   A CB  1 
ATOM   2704 O  OG  . SER   A 1 359 ? -27.202 38.018  -32.696 1   23.82 ? 344 SER   A OG  1 
ATOM   2705 N  N   . TYR   A 1 360 ? -22.916 39.281  -33.083 1   17.4  ? 345 TYR   A N   1 
ATOM   2706 C  CA  . TYR   A 1 360 ? -21.763 40.029  -33.56  1   18.72 ? 345 TYR   A CA  1 
ATOM   2707 C  C   . TYR   A 1 360 ? -20.673 39.031  -34.055 1   19.47 ? 345 TYR   A C   1 
ATOM   2708 O  O   . TYR   A 1 360 ? -20.049 39.223  -35.106 1   19.06 ? 345 TYR   A O   1 
ATOM   2709 C  CB  . TYR   A 1 360 ? -21.19  40.892  -32.422 1   19.66 ? 345 TYR   A CB  1 
ATOM   2710 C  CG  . TYR   A 1 360 ? -20.087 41.819  -32.893 1   21.78 ? 345 TYR   A CG  1 
ATOM   2711 C  CD1 . TYR   A 1 360 ? -20.374 42.942  -33.656 1   23.14 ? 345 TYR   A CD1 1 
ATOM   2712 C  CD2 . TYR   A 1 360 ? -18.755 41.581  -32.559 1   22.96 ? 345 TYR   A CD2 1 
ATOM   2713 C  CE1 . TYR   A 1 360 ? -19.364 43.798  -34.094 1   23.78 ? 345 TYR   A CE1 1 
ATOM   2714 C  CE2 . TYR   A 1 360 ? -17.738 42.426  -32.995 1   23.85 ? 345 TYR   A CE2 1 
ATOM   2715 C  CZ  . TYR   A 1 360 ? -18.046 43.529  -33.768 1   25.15 ? 345 TYR   A CZ  1 
ATOM   2716 O  OH  . TYR   A 1 360 ? -17.029 44.333  -34.217 1   27.44 ? 345 TYR   A OH  1 
ATOM   2717 N  N   . HIS   A 1 361 ? -20.478 37.945  -33.292 1   19.31 ? 346 HIS   A N   1 
ATOM   2718 C  CA  . HIS   A 1 361 ? -19.499 36.905  -33.641 1   19.36 ? 346 HIS   A CA  1 
ATOM   2719 C  C   . HIS   A 1 361 ? -19.88  36.264  -34.991 1   19.38 ? 346 HIS   A C   1 
ATOM   2720 O  O   . HIS   A 1 361 ? -18.99  36.075  -35.815 1   19.59 ? 346 HIS   A O   1 
ATOM   2721 C  CB  . HIS   A 1 361 ? -19.414 35.883  -32.51  1   19.03 ? 346 HIS   A CB  1 
ATOM   2722 C  CG  . HIS   A 1 361 ? -18.449 34.771  -32.743 1   18.44 ? 346 HIS   A CG  1 
ATOM   2723 N  ND1 . HIS   A 1 361 ? -18.882 33.54   -33.233 1   18.73 ? 346 HIS   A ND1 1 
ATOM   2724 C  CD2 . HIS   A 1 361 ? -17.119 34.711  -32.503 1   19.8  ? 346 HIS   A CD2 1 
ATOM   2725 C  CE1 . HIS   A 1 361 ? -17.813 32.757  -33.228 1   18.57 ? 346 HIS   A CE1 1 
ATOM   2726 N  NE2 . HIS   A 1 361 ? -16.712 33.441  -32.874 1   20.51 ? 346 HIS   A NE2 1 
ATOM   2727 N  N   . LEU   A 1 362 ? -21.176 36.047  -35.285 1   20.33 ? 347 LEU   A N   1 
ATOM   2728 C  CA  . LEU   A 1 362 ? -21.579 35.56   -36.634 1   21.16 ? 347 LEU   A CA  1 
ATOM   2729 C  C   . LEU   A 1 362 ? -21.125 36.513  -37.75  1   21.05 ? 347 LEU   A C   1 
ATOM   2730 O  O   . LEU   A 1 362 ? -20.618 36.054  -38.763 1   20.07 ? 347 LEU   A O   1 
ATOM   2731 C  CB  . LEU   A 1 362 ? -23.084 35.291  -36.739 1   22.98 ? 347 LEU   A CB  1 
ATOM   2732 C  CG  . LEU   A 1 362 ? -23.486 33.924  -36.213 1   25.65 ? 347 LEU   A CG  1 
ATOM   2733 C  CD1 . LEU   A 1 362 ? -24.949 33.87   -35.887 1   27.01 ? 347 LEU   A CD1 1 
ATOM   2734 C  CD2 . LEU   A 1 362 ? -23.042 32.821  -37.156 1   26.46 ? 347 LEU   A CD2 1 
ATOM   2735 N  N   . GLN   A 1 363 ? -21.236 37.842  -37.539 1   21.59 ? 348 GLN   A N   1 
ATOM   2736 C  CA  . GLN   A 1 363 ? -20.737 38.823  -38.534 1   22.6  ? 348 GLN   A CA  1 
ATOM   2737 C  C   . GLN   A 1 363 ? -19.215 38.727  -38.679 1   21.36 ? 348 GLN   A C   1 
ATOM   2738 O  O   . GLN   A 1 363 ? -18.688 38.863  -39.778 1   21.13 ? 348 GLN   A O   1 
ATOM   2739 C  CB  . GLN   A 1 363 ? -21.114 40.262  -38.143 1   25.76 ? 348 GLN   A CB  1 
ATOM   2740 C  CG  . GLN   A 1 363 ? -22.623 40.489  -38.132 1   33.78 ? 348 GLN   A CG  1 
ATOM   2741 C  CD  . GLN   A 1 363 ? -23.024 41.81   -37.498 1   44.69 ? 348 GLN   A CD  1 
ATOM   2742 O  OE1 . GLN   A 1 363 ? -22.189 42.633  -37.084 1   48.22 ? 348 GLN   A OE1 1 
ATOM   2743 N  NE2 . GLN   A 1 363 ? -24.32  42.048  -37.41  1   47    ? 348 GLN   A NE2 1 
ATOM   2744 N  N   . ILE   A 1 364 ? -18.496 38.527  -37.563 1   20.3  ? 349 ILE   A N   1 
ATOM   2745 C  CA  . ILE   A 1 364 ? -17.053 38.379  -37.577 1   20.07 ? 349 ILE   A CA  1 
ATOM   2746 C  C   . ILE   A 1 364 ? -16.64  37.148  -38.397 1   19.36 ? 349 ILE   A C   1 
ATOM   2747 O  O   . ILE   A 1 364 ? -15.744 37.227  -39.255 1   17.99 ? 349 ILE   A O   1 
ATOM   2748 C  CB  . ILE   A 1 364 ? -16.56  38.301  -36.112 1   21.49 ? 349 ILE   A CB  1 
ATOM   2749 C  CG1 . ILE   A 1 364 ? -16.643 39.668  -35.414 1   22.79 ? 349 ILE   A CG1 1 
ATOM   2750 C  CG2 . ILE   A 1 364 ? -15.14  37.733  -36.005 1   22.37 ? 349 ILE   A CG2 1 
ATOM   2751 C  CD1 . ILE   A 1 364 ? -16.16  40.855  -36.228 1   24.58 ? 349 ILE   A CD1 1 
ATOM   2752 N  N   . VAL   A 1 365 ? -17.33  36.034  -38.177 1   20.03 ? 350 VAL   A N   1 
ATOM   2753 C  CA  . VAL   A 1 365 ? -17.038 34.799  -38.899 1   20.92 ? 350 VAL   A CA  1 
ATOM   2754 C  C   . VAL   A 1 365 ? -17.322 34.946  -40.39  1   21.27 ? 350 VAL   A C   1 
ATOM   2755 O  O   . VAL   A 1 365 ? -16.548 34.437  -41.209 1   20.61 ? 350 VAL   A O   1 
ATOM   2756 C  CB  . VAL   A 1 365 ? -17.785 33.6    -38.27  1   22.28 ? 350 VAL   A CB  1 
ATOM   2757 C  CG1 . VAL   A 1 365 ? -17.669 32.358  -39.155 1   23.26 ? 350 VAL   A CG1 1 
ATOM   2758 C  CG2 . VAL   A 1 365 ? -17.234 33.312  -36.865 1   22.54 ? 350 VAL   A CG2 1 
ATOM   2759 N  N   . THR   A 1 366 ? -18.378 35.709  -40.753 1   20.91 ? 351 THR   A N   1 
ATOM   2760 C  CA  . THR   A 1 366 ? -18.68  35.976  -42.16  1   21.44 ? 351 THR   A CA  1 
ATOM   2761 C  C   . THR   A 1 366 ? -17.517 36.769  -42.782 1   20.72 ? 351 THR   A C   1 
ATOM   2762 O  O   . THR   A 1 366 ? -17.055 36.414  -43.861 1   21.63 ? 351 THR   A O   1 
ATOM   2763 C  CB  . THR   A 1 366 ? -20.002 36.766  -42.302 1   23.08 ? 351 THR   A CB  1 
ATOM   2764 O  OG1 . THR   A 1 366 ? -21.086 35.971  -41.805 1   24.08 ? 351 THR   A OG1 1 
ATOM   2765 C  CG2 . THR   A 1 366 ? -20.282 37.171  -43.755 1   24.12 ? 351 THR   A CG2 1 
ATOM   2766 N  N   . LYS   A 1 367 ? -16.989 37.784  -42.075 1   19.6  ? 352 LYS   A N   1 
ATOM   2767 C  CA  . LYS   A 1 367 ? -15.855 38.558  -42.583 1   19.65 ? 352 LYS   A CA  1 
ATOM   2768 C  C   . LYS   A 1 367 ? -14.529 37.762  -42.682 1   20.44 ? 352 LYS   A C   1 
ATOM   2769 O  O   . LYS   A 1 367 ? -13.774 37.917  -43.648 1   21.24 ? 352 LYS   A O   1 
ATOM   2770 C  CB  . LYS   A 1 367 ? -15.634 39.798  -41.676 1   19.72 ? 352 LYS   A CB  1 
ATOM   2771 C  CG  . LYS   A 1 367 ? -14.431 40.651  -42.046 1   21.62 ? 352 LYS   A CG  1 
ATOM   2772 C  CD  . LYS   A 1 367 ? -14.339 41.939  -41.222 1   24.98 ? 352 LYS   A CD  1 
ATOM   2773 C  CE  . LYS   A 1 367 ? -13.011 42.639  -41.457 1   26.38 ? 352 LYS   A CE  1 
ATOM   2774 N  NZ  . LYS   A 1 367 ? -12.8   43.814  -40.574 1   25.44 ? 352 LYS   A NZ  1 
ATOM   2775 N  N   . TYR   A 1 368 ? -14.199 36.99   -41.645 1   19.1  ? 353 TYR   A N   1 
ATOM   2776 C  CA  . TYR   A 1 368 ? -12.898 36.362  -41.547 1   19.9  ? 353 TYR   A CA  1 
ATOM   2777 C  C   . TYR   A 1 368 ? -12.802 34.986  -42.154 1   20.68 ? 353 TYR   A C   1 
ATOM   2778 O  O   . TYR   A 1 368 ? -11.692 34.55   -42.456 1   21.38 ? 353 TYR   A O   1 
ATOM   2779 C  CB  . TYR   A 1 368 ? -12.422 36.361  -40.081 1   19    ? 353 TYR   A CB  1 
ATOM   2780 C  CG  . TYR   A 1 368 ? -11.982 37.743  -39.653 1   19.3  ? 353 TYR   A CG  1 
ATOM   2781 C  CD1 . TYR   A 1 368 ? -12.873 38.623  -39.045 1   19.94 ? 353 TYR   A CD1 1 
ATOM   2782 C  CD2 . TYR   A 1 368 ? -10.711 38.205  -39.945 1   19.8  ? 353 TYR   A CD2 1 
ATOM   2783 C  CE1 . TYR   A 1 368 ? -12.49  39.905  -38.689 1   20.42 ? 353 TYR   A CE1 1 
ATOM   2784 C  CE2 . TYR   A 1 368 ? -10.307 39.478  -39.576 1   20.46 ? 353 TYR   A CE2 1 
ATOM   2785 C  CZ  . TYR   A 1 368 ? -11.216 40.345  -38.987 1   21.35 ? 353 TYR   A CZ  1 
ATOM   2786 O  OH  . TYR   A 1 368 ? -10.822 41.602  -38.604 1   22.41 ? 353 TYR   A OH  1 
ATOM   2787 N  N   . ILE   A 1 369 ? -13.929 34.291  -42.312 1   20.97 ? 354 ILE   A N   1 
ATOM   2788 C  CA  . ILE   A 1 369 ? -13.94  32.951  -42.862 1   20.85 ? 354 ILE   A CA  1 
ATOM   2789 C  C   . ILE   A 1 369 ? -14.794 32.829  -44.14  1   23.4  ? 354 ILE   A C   1 
ATOM   2790 O  O   . ILE   A 1 369 ? -14.259 32.407  -45.161 1   23.36 ? 354 ILE   A O   1 
ATOM   2791 C  CB  . ILE   A 1 369 ? -14.339 31.87   -41.809 1   19.52 ? 354 ILE   A CB  1 
ATOM   2792 C  CG1 . ILE   A 1 369 ? -13.3   31.805  -40.634 1   19.84 ? 354 ILE   A CG1 1 
ATOM   2793 C  CG2 . ILE   A 1 369 ? -14.477 30.477  -42.503 1   18.99 ? 354 ILE   A CG2 1 
ATOM   2794 C  CD1 . ILE   A 1 369 ? -13.731 30.848  -39.53  1   20.35 ? 354 ILE   A CD1 1 
ATOM   2795 N  N   . LEU   A 1 370 ? -16.093 33.119  -44.078 1   24.77 ? 355 LEU   A N   1 
ATOM   2796 C  CA  . LEU   A 1 370 ? -16.976 32.896  -45.234 1   27.14 ? 355 LEU   A CA  1 
ATOM   2797 C  C   . LEU   A 1 370 ? -16.58  33.649  -46.505 1   28.07 ? 355 LEU   A C   1 
ATOM   2798 O  O   . LEU   A 1 370 ? -16.497 33.026  -47.563 1   28.63 ? 355 LEU   A O   1 
ATOM   2799 C  CB  . LEU   A 1 370 ? -18.438 33.166  -44.9   1   28.36 ? 355 LEU   A CB  1 
ATOM   2800 C  CG  . LEU   A 1 370 ? -19.05  32.36   -43.778 1   31.3  ? 355 LEU   A CG  1 
ATOM   2801 C  CD1 . LEU   A 1 370 ? -20.55  32.711  -43.66  1   32.03 ? 355 LEU   A CD1 1 
ATOM   2802 C  CD2 . LEU   A 1 370 ? -18.826 30.843  -43.973 1   31.54 ? 355 LEU   A CD2 1 
ATOM   2803 N  N   . ILE   A 1 371 ? -16.329 34.945  -46.414 1   28.05 ? 356 ILE   A N   1 
ATOM   2804 C  CA  . ILE   A 1 371 ? -15.966 35.751  -47.569 1   29.45 ? 356 ILE   A CA  1 
ATOM   2805 C  C   . ILE   A 1 371 ? -14.6   35.332  -48.12  1   29.94 ? 356 ILE   A C   1 
ATOM   2806 O  O   . ILE   A 1 371 ? -14.564 34.949  -49.286 1   30.18 ? 356 ILE   A O   1 
ATOM   2807 C  CB  . ILE   A 1 371 ? -16.108 37.265  -47.284 1   30.72 ? 356 ILE   A CB  1 
ATOM   2808 C  CG1 . ILE   A 1 371 ? -17.604 37.634  -47.169 1   32.27 ? 356 ILE   A CG1 1 
ATOM   2809 C  CG2 . ILE   A 1 371 ? -15.425 38.102  -48.353 1   31.38 ? 356 ILE   A CG2 1 
ATOM   2810 C  CD1 . ILE   A 1 371 ? -17.85  39.021  -46.694 1   33.55 ? 356 ILE   A CD1 1 
ATOM   2811 N  N   . PRO   A 1 372 ? -13.515 35.22   -47.308 1   29.91 ? 357 PRO   A N   1 
ATOM   2812 C  CA  . PRO   A 1 372 ? -12.254 34.688  -47.855 1   30.42 ? 357 PRO   A CA  1 
ATOM   2813 C  C   . PRO   A 1 372 ? -12.405 33.28   -48.436 1   31.67 ? 357 PRO   A C   1 
ATOM   2814 O  O   . PRO   A 1 372 ? -11.828 33.03   -49.484 1   32.97 ? 357 PRO   A O   1 
ATOM   2815 C  CB  . PRO   A 1 372 ? -11.293 34.722  -46.646 1   30.78 ? 357 PRO   A CB  1 
ATOM   2816 C  CG  . PRO   A 1 372 ? -11.89  35.756  -45.722 1   30.69 ? 357 PRO   A CG  1 
ATOM   2817 C  CD  . PRO   A 1 372 ? -13.363 35.611  -45.891 1   29.18 ? 357 PRO   A CD  1 
ATOM   2818 N  N   . ALA   A 1 373 ? -13.213 32.388  -47.827 1   31.48 ? 358 ALA   A N   1 
ATOM   2819 C  CA  . ALA   A 1 373 ? -13.422 31.045  -48.385 1   33.45 ? 358 ALA   A CA  1 
ATOM   2820 C  C   . ALA   A 1 373 ? -14.1   31.117  -49.756 1   36.26 ? 358 ALA   A C   1 
ATOM   2821 O  O   . ALA   A 1 373 ? -13.783 30.316  -50.639 1   35.54 ? 358 ALA   A O   1 
ATOM   2822 C  CB  . ALA   A 1 373 ? -14.256 30.178  -47.453 1   32.95 ? 358 ALA   A CB  1 
ATOM   2823 N  N   . SER   A 1 374 ? -15.029 32.08   -49.931 1   38.3  ? 359 SER   A N   1 
ATOM   2824 C  CA  . SER   A 1 374 ? -15.731 32.257  -51.206 1   41.24 ? 359 SER   A CA  1 
ATOM   2825 C  C   . SER   A 1 374 ? -14.792 32.742  -52.325 1   44.7  ? 359 SER   A C   1 
ATOM   2826 O  O   . SER   A 1 374 ? -15.101 32.546  -53.499 1   46.03 ? 359 SER   A O   1 
ATOM   2827 C  CB  . SER   A 1 374 ? -16.899 33.23   -51.051 1   40.64 ? 359 SER   A CB  1 
ATOM   2828 O  OG  . SER   A 1 374 ? -16.437 34.567  -50.937 1   41.05 ? 359 SER   A OG  1 
ATOM   2829 N  N   . GLN   A 1 375 ? -13.692 33.408  -51.966 1   46.11 ? 360 GLN   A N   1 
ATOM   2830 C  CA  . GLN   A 1 375 ? -12.7   33.914  -52.906 1   48.48 ? 360 GLN   A CA  1 
ATOM   2831 C  C   . GLN   A 1 375 ? -11.497 32.958  -53.088 1   51.47 ? 360 GLN   A C   1 
ATOM   2832 O  O   . GLN   A 1 375 ? -10.565 33.31   -53.8   1   52.14 ? 360 GLN   A O   1 
ATOM   2833 C  CB  . GLN   A 1 375 ? -12.183 35.28   -52.429 1   49.39 ? 360 GLN   A CB  1 
ATOM   2834 C  CG  . GLN   A 1 375 ? -13.259 36.359  -52.288 1   51.44 ? 360 GLN   A CG  1 
ATOM   2835 C  CD  . GLN   A 1 375 ? -12.816 37.512  -51.407 1   55.25 ? 360 GLN   A CD  1 
ATOM   2836 O  OE1 . GLN   A 1 375 ? -11.791 37.456  -50.709 1   57.95 ? 360 GLN   A OE1 1 
ATOM   2837 N  NE2 . GLN   A 1 375 ? -13.589 38.581  -51.396 1   54.89 ? 360 GLN   A NE2 1 
ATOM   2838 N  N   . GLN   A 1 376 ? -11.49  31.783  -52.416 1   53.29 ? 361 GLN   A N   1 
ATOM   2839 C  CA  . GLN   A 1 376 ? -10.391 30.815  -52.465 1   55.17 ? 361 GLN   A CA  1 
ATOM   2840 C  C   . GLN   A 1 376 ? -10.353 30.133  -53.825 1   56.63 ? 361 GLN   A C   1 
ATOM   2841 O  O   . GLN   A 1 376 ? -11.343 29.532  -54.24  1   57.42 ? 361 GLN   A O   1 
ATOM   2842 C  CB  . GLN   A 1 376 ? -10.55  29.761  -51.34  1   57.17 ? 361 GLN   A CB  1 
ATOM   2843 C  CG  . GLN   A 1 376 ? -9.304  28.933  -51.049 1   60.98 ? 361 GLN   A CG  1 
ATOM   2844 N  N   . ALA   A 1 391 ? -17.985 25.85   -45.103 1   37.12 ? 376 ALA   A N   1 
ATOM   2845 C  CA  . ALA   A 1 391 ? -16.817 26.011  -44.232 1   36.64 ? 376 ALA   A CA  1 
ATOM   2846 C  C   . ALA   A 1 391 ? -16.917 25.021  -43.073 1   36.2  ? 376 ALA   A C   1 
ATOM   2847 O  O   . ALA   A 1 391 ? -17.907 25.044  -42.337 1   35.52 ? 376 ALA   A O   1 
ATOM   2848 C  CB  . ALA   A 1 391 ? -16.756 27.443  -43.709 1   36.66 ? 376 ALA   A CB  1 
ATOM   2849 N  N   . LYS   A 1 392 ? -15.919 24.139  -42.912 1   36.21 ? 377 LYS   A N   1 
ATOM   2850 C  CA  . LYS   A 1 392 ? -15.971 23.147  -41.826 1   36.6  ? 377 LYS   A CA  1 
ATOM   2851 C  C   . LYS   A 1 392 ? -15.23  23.63   -40.584 1   36.7  ? 377 LYS   A C   1 
ATOM   2852 O  O   . LYS   A 1 392 ? -14.145 24.177  -40.696 1   35.85 ? 377 LYS   A O   1 
ATOM   2853 C  CB  . LYS   A 1 392 ? -15.438 21.778  -42.287 1   37.85 ? 377 LYS   A CB  1 
ATOM   2854 N  N   . GLY   A 1 393 ? -15.828 23.434  -39.414 1   37.8  ? 378 GLY   A N   1 
ATOM   2855 C  CA  . GLY   A 1 393 ? -15.192 23.838  -38.163 1   39.09 ? 378 GLY   A CA  1 
ATOM   2856 C  C   . GLY   A 1 393 ? -14.411 22.715  -37.506 1   39.54 ? 378 GLY   A C   1 
ATOM   2857 O  O   . GLY   A 1 393 ? -14.234 21.646  -38.105 1   40.13 ? 378 GLY   A O   1 
ATOM   2858 N  N   . THR   A 1 394 ? -13.948 22.946  -36.252 1   38.62 ? 379 THR   A N   1 
ATOM   2859 C  CA  . THR   A 1 394 ? -13.191 22.002  -35.413 1   38.03 ? 379 THR   A CA  1 
ATOM   2860 C  C   . THR   A 1 394 ? -13.896 20.636  -35.204 1   39.82 ? 379 THR   A C   1 
ATOM   2861 O  O   . THR   A 1 394 ? -13.238 19.606  -35.002 1   39.58 ? 379 THR   A O   1 
ATOM   2862 C  CB  . THR   A 1 394 ? -12.91  22.677  -34.072 1   37.19 ? 379 THR   A CB  1 
ATOM   2863 O  OG1 . THR   A 1 394 ? -12.176 23.881  -34.32  1   36.71 ? 379 THR   A OG1 1 
ATOM   2864 C  CG2 . THR   A 1 394 ? -12.173 21.774  -33.079 1   36.46 ? 379 THR   A CG2 1 
ATOM   2865 N  N   . GLY   A 1 395 ? -15.221 20.643  -35.241 1   40.83 ? 380 GLY   A N   1 
ATOM   2866 C  CA  . GLY   A 1 395 ? -16     19.421  -35.063 1   42.8  ? 380 GLY   A CA  1 
ATOM   2867 C  C   . GLY   A 1 395 ? -16.214 18.604  -36.328 1   44.68 ? 380 GLY   A C   1 
ATOM   2868 O  O   . GLY   A 1 395 ? -16.92  17.587  -36.297 1   45.75 ? 380 GLY   A O   1 
ATOM   2869 N  N   . GLY   A 1 396 ? -15.62  19.043  -37.443 1   44.73 ? 381 GLY   A N   1 
ATOM   2870 C  CA  . GLY   A 1 396 ? -15.743 18.365  -38.729 1   45.08 ? 381 GLY   A CA  1 
ATOM   2871 C  C   . GLY   A 1 396 ? -17.023 18.665  -39.489 1   45.15 ? 381 GLY   A C   1 
ATOM   2872 O  O   . GLY   A 1 396 ? -17.201 18.17   -40.608 1   45.94 ? 381 GLY   A O   1 
ATOM   2873 N  N   . THR   A 1 397 ? -17.939 19.461  -38.888 1   43.77 ? 382 THR   A N   1 
ATOM   2874 C  CA  . THR   A 1 397 ? -19.22  19.835  -39.499 1   42.98 ? 382 THR   A CA  1 
ATOM   2875 C  C   . THR   A 1 397 ? -19.303 21.363  -39.75  1   40.59 ? 382 THR   A C   1 
ATOM   2876 O  O   . THR   A 1 397 ? -18.5   22.124  -39.199 1   40.91 ? 382 THR   A O   1 
ATOM   2877 C  CB  . THR   A 1 397 ? -20.407 19.314  -38.664 1   45.21 ? 382 THR   A CB  1 
ATOM   2878 O  OG1 . THR   A 1 397 ? -20.521 20.08   -37.461 1   46.48 ? 382 THR   A OG1 1 
ATOM   2879 C  CG2 . THR   A 1 397 ? -20.312 17.808  -38.355 1   45.66 ? 382 THR   A CG2 1 
ATOM   2880 N  N   . ASP   A 1 398 ? -20.256 21.803  -40.596 1   37.66 ? 383 ASP   A N   1 
ATOM   2881 C  CA  . ASP   A 1 398 ? -20.439 23.21   -40.964 1   36.1  ? 383 ASP   A CA  1 
ATOM   2882 C  C   . ASP   A 1 398 ? -20.424 24.161  -39.759 1   31.97 ? 383 ASP   A C   1 
ATOM   2883 O  O   . ASP   A 1 398 ? -21.252 24.043  -38.855 1   30.53 ? 383 ASP   A O   1 
ATOM   2884 C  CB  . ASP   A 1 398 ? -21.723 23.392  -41.785 1   39.42 ? 383 ASP   A CB  1 
ATOM   2885 C  CG  . ASP   A 1 398 ? -21.839 24.74   -42.451 1   46.91 ? 383 ASP   A CG  1 
ATOM   2886 O  OD1 . ASP   A 1 398 ? -22.176 25.717  -41.758 1   47.48 ? 383 ASP   A OD1 1 
ATOM   2887 O  OD2 . ASP   A 1 398 ? -21.621 24.814  -43.679 1   51.45 ? 383 ASP   A OD2 1 
ATOM   2888 N  N   . LEU   A 1 399 ? -19.451 25.076  -39.749 1   29.89 ? 384 LEU   A N   1 
ATOM   2889 C  CA  . LEU   A 1 399 ? -19.296 25.98   -38.622 1   28.93 ? 384 LEU   A CA  1 
ATOM   2890 C  C   . LEU   A 1 399 ? -20.419 27.007  -38.54  1   27.75 ? 384 LEU   A C   1 
ATOM   2891 O  O   . LEU   A 1 399 ? -20.779 27.36   -37.43  1   27.05 ? 384 LEU   A O   1 
ATOM   2892 C  CB  . LEU   A 1 399 ? -17.895 26.625  -38.582 1   28.71 ? 384 LEU   A CB  1 
ATOM   2893 C  CG  . LEU   A 1 399 ? -17.465 27.462  -39.772 1   28.99 ? 384 LEU   A CG  1 
ATOM   2894 C  CD1 . LEU   A 1 399 ? -17.766 28.929  -39.512 1   29.28 ? 384 LEU   A CD1 1 
ATOM   2895 C  CD2 . LEU   A 1 399 ? -15.951 27.333  -40.015 1   29.11 ? 384 LEU   A CD2 1 
ATOM   2896 N  N   . MET   A 1 400 ? -21     27.466  -39.685 1   27.42 ? 385 MET   A N   1 
ATOM   2897 C  CA  . MET   A 1 400 ? -22.099 28.437  -39.632 1   27.56 ? 385 MET   A CA  1 
ATOM   2898 C  C   . MET   A 1 400 ? -23.342 27.844  -38.998 1   27.22 ? 385 MET   A C   1 
ATOM   2899 O  O   . MET   A 1 400 ? -23.972 28.494  -38.172 1   26.62 ? 385 MET   A O   1 
ATOM   2900 C  CB  . MET   A 1 400 ? -22.41  29.034  -41.01  1   29.17 ? 385 MET   A CB  1 
ATOM   2901 C  CG  . MET   A 1 400 ? -21.381 30.038  -41.456 1   32.52 ? 385 MET   A CG  1 
ATOM   2902 S  SD  . MET   A 1 400 ? -21.143 31.45   -40.313 1   39.5  ? 385 MET   A SD  1 
ATOM   2903 C  CE  . MET   A 1 400 ? -22.498 32.425  -40.7   1   38.31 ? 385 MET   A CE  1 
ATOM   2904 N  N   . ASN   A 1 401 ? -23.648 26.586  -39.33  1   26.98 ? 386 ASN   A N   1 
ATOM   2905 C  CA  . ASN   A 1 401 ? -24.762 25.84   -38.766 1   27.52 ? 386 ASN   A CA  1 
ATOM   2906 C  C   . ASN   A 1 401 ? -24.578 25.669  -37.266 1   25.19 ? 386 ASN   A C   1 
ATOM   2907 O  O   . ASN   A 1 401 ? -25.521 25.921  -36.497 1   25.51 ? 386 ASN   A O   1 
ATOM   2908 C  CB  . ASN   A 1 401 ? -24.894 24.463  -39.457 1   31.51 ? 386 ASN   A CB  1 
ATOM   2909 C  CG  . ASN   A 1 401 ? -25.546 24.553  -40.826 1   39.39 ? 386 ASN   A CG  1 
ATOM   2910 O  OD1 . ASN   A 1 401 ? -26.115 25.603  -41.201 1   42.26 ? 386 ASN   A OD1 1 
ATOM   2911 N  ND2 . ASN   A 1 401 ? -25.488 23.454  -41.601 1   40.33 ? 386 ASN   A ND2 1 
ATOM   2912 N  N   . PHE   A 1 402 ? -23.35  25.304  -36.837 1   22.73 ? 387 PHE   A N   1 
ATOM   2913 C  CA  . PHE   A 1 402 ? -23.033 25.185  -35.413 1   21.14 ? 387 PHE   A CA  1 
ATOM   2914 C  C   . PHE   A 1 402 ? -23.296 26.518  -34.696 1   19.69 ? 387 PHE   A C   1 
ATOM   2915 O  O   . PHE   A 1 402 ? -24.072 26.547  -33.743 1   19.83 ? 387 PHE   A O   1 
ATOM   2916 C  CB  . PHE   A 1 402 ? -21.573 24.724  -35.181 1   20.43 ? 387 PHE   A CB  1 
ATOM   2917 C  CG  . PHE   A 1 402 ? -21.085 24.891  -33.743 1   20.12 ? 387 PHE   A CG  1 
ATOM   2918 C  CD1 . PHE   A 1 402 ? -21.519 24.034  -32.741 1   19.55 ? 387 PHE   A CD1 1 
ATOM   2919 C  CD2 . PHE   A 1 402 ? -20.188 25.896  -33.408 1   20.38 ? 387 PHE   A CD2 1 
ATOM   2920 C  CE1 . PHE   A 1 402 ? -21.047 24.163  -31.443 1   19.89 ? 387 PHE   A CE1 1 
ATOM   2921 C  CE2 . PHE   A 1 402 ? -19.718 26.03   -32.1   1   19.98 ? 387 PHE   A CE2 1 
ATOM   2922 C  CZ  . PHE   A 1 402 ? -20.175 25.183  -31.122 1   18.92 ? 387 PHE   A CZ  1 
ATOM   2923 N  N   . LEU   A 1 403 ? -22.694 27.601  -35.183 1   18.33 ? 388 LEU   A N   1 
ATOM   2924 C  CA  . LEU   A 1 403 ? -22.821 28.911  -34.556 1   18.94 ? 388 LEU   A CA  1 
ATOM   2925 C  C   . LEU   A 1 403 ? -24.263 29.435  -34.488 1   19.9  ? 388 LEU   A C   1 
ATOM   2926 O  O   . LEU   A 1 403 ? -24.668 30.001  -33.466 1   18.78 ? 388 LEU   A O   1 
ATOM   2927 C  CB  . LEU   A 1 403 ? -21.901 29.918  -35.285 1   18.91 ? 388 LEU   A CB  1 
ATOM   2928 C  CG  . LEU   A 1 403 ? -20.404 29.677  -35.089 1   20.52 ? 388 LEU   A CG  1 
ATOM   2929 C  CD1 . LEU   A 1 403 ? -19.613 30.683  -35.895 1   21.54 ? 388 LEU   A CD1 1 
ATOM   2930 C  CD2 . LEU   A 1 403 ? -20.005 29.778  -33.603 1   20.35 ? 388 LEU   A CD2 1 
ATOM   2931 N  N   . LYS   A 1 404 ? -25.036 29.24   -35.581 1   20.64 ? 389 LYS   A N   1 
ATOM   2932 C  CA  . LYS   A 1 404 ? -26.426 29.664  -35.644 1   21.28 ? 389 LYS   A CA  1 
ATOM   2933 C  C   . LYS   A 1 404 ? -27.283 28.845  -34.708 1   21.44 ? 389 LYS   A C   1 
ATOM   2934 O  O   . LYS   A 1 404 ? -28.141 29.431  -34.073 1   20.9  ? 389 LYS   A O   1 
ATOM   2935 C  CB  . LYS   A 1 404 ? -26.954 29.602  -37.069 1   24.06 ? 389 LYS   A CB  1 
ATOM   2936 C  CG  . LYS   A 1 404 ? -26.304 30.677  -37.911 1   29.9  ? 389 LYS   A CG  1 
ATOM   2937 C  CD  . LYS   A 1 404 ? -27.014 30.856  -39.216 1   37.19 ? 389 LYS   A CD  1 
ATOM   2938 C  CE  . LYS   A 1 404 ? -26.65  29.799  -40.195 1   44.61 ? 389 LYS   A CE  1 
ATOM   2939 N  NZ  . LYS   A 1 404 ? -27.002 30.212  -41.585 1   49.73 ? 389 LYS   A NZ  1 
ATOM   2940 N  N   . THR   A 1 405 ? -26.978 27.537  -34.53  1   20.7  ? 390 THR   A N   1 
ATOM   2941 C  CA  . THR   A 1 405 ? -27.685 26.686  -33.585 1   21.14 ? 390 THR   A CA  1 
ATOM   2942 C  C   . THR   A 1 405 ? -27.42  27.17   -32.164 1   22.12 ? 390 THR   A C   1 
ATOM   2943 O  O   . THR   A 1 405 ? -28.361 27.34   -31.404 1   22.87 ? 390 THR   A O   1 
ATOM   2944 C  CB  . THR   A 1 405 ? -27.267 25.219  -33.753 1   22.74 ? 390 THR   A CB  1 
ATOM   2945 O  OG1 . THR   A 1 405 ? -27.745 24.78   -35.026 1   25.18 ? 390 THR   A OG1 1 
ATOM   2946 C  CG2 . THR   A 1 405 ? -27.835 24.33   -32.662 1   22.14 ? 390 THR   A CG2 1 
ATOM   2947 N  N   . VAL   A 1 406 ? -26.156 27.453  -31.819 1   21.5  ? 391 VAL   A N   1 
ATOM   2948 C  CA  . VAL   A 1 406 ? -25.79  27.974  -30.492 1   20.47 ? 391 VAL   A CA  1 
ATOM   2949 C  C   . VAL   A 1 406 ? -26.485 29.326  -30.229 1   20.31 ? 391 VAL   A C   1 
ATOM   2950 O  O   . VAL   A 1 406 ? -27.073 29.521  -29.152 1   20.35 ? 391 VAL   A O   1 
ATOM   2951 C  CB  . VAL   A 1 406 ? -24.258 28.027  -30.306 1   20.13 ? 391 VAL   A CB  1 
ATOM   2952 C  CG1 . VAL   A 1 406 ? -23.887 28.688  -28.98  1   20.43 ? 391 VAL   A CG1 1 
ATOM   2953 C  CG2 . VAL   A 1 406 ? -23.672 26.62   -30.382 1   18.83 ? 391 VAL   A CG2 1 
ATOM   2954 N  N   . ARG   A 1 407 ? -26.465 30.215  -31.214 1   19.76 ? 392 ARG   A N   1 
ATOM   2955 C  CA  . ARG   A 1 407 ? -27.156 31.508  -31.07  1   21.66 ? 392 ARG   A CA  1 
ATOM   2956 C  C   . ARG   A 1 407 ? -28.68  31.334  -30.885 1   21.99 ? 392 ARG   A C   1 
ATOM   2957 O  O   . ARG   A 1 407 ? -29.268 31.977  -30.014 1   21.55 ? 392 ARG   A O   1 
ATOM   2958 C  CB  . ARG   A 1 407 ? -26.891 32.437  -32.259 1   22.05 ? 392 ARG   A CB  1 
ATOM   2959 C  CG  . ARG   A 1 407 ? -27.463 33.834  -31.987 1   24.6  ? 392 ARG   A CG  1 
ATOM   2960 C  CD  . ARG   A 1 407 ? -27.697 34.627  -33.274 1   29.51 ? 392 ARG   A CD  1 
ATOM   2961 N  NE  . ARG   A 1 407 ? -28.66  35.707  -33.048 1   32.13 ? 392 ARG   A NE  1 
ATOM   2962 C  CZ  . ARG   A 1 407 ? -29.985 35.558  -33.072 1   31.59 ? 392 ARG   A CZ  1 
ATOM   2963 N  NH1 . ARG   A 1 407 ? -30.523 34.387  -33.395 1   28.93 ? 392 ARG   A NH1 1 
ATOM   2964 N  NH2 . ARG   A 1 407 ? -30.777 36.581  -32.789 1   29.43 ? 392 ARG   A NH2 1 
ATOM   2965 N  N   . SER   A 1 408 ? -29.309 30.482  -31.712 1   22.08 ? 393 SER   A N   1 
ATOM   2966 C  CA  . SER   A 1 408 ? -30.741 30.217  -31.678 1   23.43 ? 393 SER   A CA  1 
ATOM   2967 C  C   . SER   A 1 408 ? -31.161 29.635  -30.321 1   23.36 ? 393 SER   A C   1 
ATOM   2968 O  O   . SER   A 1 408 ? -32.134 30.098  -29.743 1   23.08 ? 393 SER   A O   1 
ATOM   2969 C  CB  . SER   A 1 408 ? -31.115 29.27   -32.826 1   26.17 ? 393 SER   A CB  1 
ATOM   2970 O  OG  . SER   A 1 408 ? -32.447 28.796  -32.72  1   29.45 ? 393 SER   A OG  1 
ATOM   2971 N  N   . THR   A 1 409 ? -30.376 28.674  -29.761 1   22.85 ? 394 THR   A N   1 
ATOM   2972 C  CA  . THR   A 1 409 ? -30.666 28.112  -28.439 1   22.67 ? 394 THR   A CA  1 
ATOM   2973 C  C   . THR   A 1 409 ? -30.636 29.219  -27.373 1   22.17 ? 394 THR   A C   1 
ATOM   2974 O  O   . THR   A 1 409 ? -31.463 29.231  -26.45  1   22.4  ? 394 THR   A O   1 
ATOM   2975 C  CB  . THR   A 1 409 ? -29.651 26.981  -28.155 1   24.84 ? 394 THR   A CB  1 
ATOM   2976 O  OG1 . THR   A 1 409 ? -29.769 26.017  -29.207 1   26.28 ? 394 THR   A OG1 1 
ATOM   2977 C  CG2 . THR   A 1 409 ? -29.858 26.321  -26.805 1   25.03 ? 394 THR   A CG2 1 
ATOM   2978 N  N   . THR   A 1 410 ? -29.703 30.179  -27.51  1   21.7  ? 395 THR   A N   1 
ATOM   2979 C  CA  . THR   A 1 410 ? -29.611 31.302  -26.575 1   21.62 ? 395 THR   A CA  1 
ATOM   2980 C  C   . THR   A 1 410 ? -30.826 32.229  -26.731 1   22.56 ? 395 THR   A C   1 
ATOM   2981 O  O   . THR   A 1 410 ? -31.461 32.563  -25.728 1   21.82 ? 395 THR   A O   1 
ATOM   2982 C  CB  . THR   A 1 410 ? -28.314 32.124  -26.824 1   20.62 ? 395 THR   A CB  1 
ATOM   2983 O  OG1 . THR   A 1 410 ? -27.21  31.232  -26.953 1   18.5  ? 395 THR   A OG1 1 
ATOM   2984 C  CG2 . THR   A 1 410 ? -28.094 33.146  -25.752 1   20.39 ? 395 THR   A CG2 1 
ATOM   2985 N  N   . GLU   A 1 411 ? -31.158 32.635  -27.987 1   22.99 ? 396 GLU   A N   1 
ATOM   2986 C  CA  . GLU   A 1 411 ? -32.306 33.536  -28.236 1   24.21 ? 396 GLU   A CA  1 
ATOM   2987 C  C   . GLU   A 1 411 ? -33.61  32.925  -27.717 1   24.33 ? 396 GLU   A C   1 
ATOM   2988 O  O   . GLU   A 1 411 ? -34.448 33.639  -27.145 1   24.16 ? 396 GLU   A O   1 
ATOM   2989 C  CB  . GLU   A 1 411 ? -32.428 33.876  -29.726 1   26.12 ? 396 GLU   A CB  1 
ATOM   2990 C  CG  . GLU   A 1 411 ? -33.331 35.081  -30.001 1   31.92 ? 396 GLU   A CG  1 
ATOM   2991 C  CD  . GLU   A 1 411 ? -34.783 34.722  -30.305 1   40.19 ? 396 GLU   A CD  1 
ATOM   2992 O  OE1 . GLU   A 1 411 ? -35.067 33.526  -30.548 1   40.76 ? 396 GLU   A OE1 1 
ATOM   2993 O  OE2 . GLU   A 1 411 ? -35.64  35.636  -30.285 1   43.22 ? 396 GLU   A OE2 1 
ATOM   2994 N  N   . LYS   A 1 412 ? -33.765 31.615  -27.88  1   24.65 ? 397 LYS   A N   1 
ATOM   2995 C  CA  . LYS   A 1 412 ? -34.971 30.913  -27.428 1   26.48 ? 397 LYS   A CA  1 
ATOM   2996 C  C   . LYS   A 1 412 ? -35.096 30.77   -25.916 1   27.39 ? 397 LYS   A C   1 
ATOM   2997 O  O   . LYS   A 1 412 ? -36.165 30.41   -25.43  1   27.29 ? 397 LYS   A O   1 
ATOM   2998 C  CB  . LYS   A 1 412 ? -35.103 29.565  -28.122 1   30.14 ? 397 LYS   A CB  1 
ATOM   2999 C  CG  . LYS   A 1 412 ? -35.55  29.752  -29.574 1   35.54 ? 397 LYS   A CG  1 
ATOM   3000 C  CD  . LYS   A 1 412 ? -35.265 28.533  -30.428 1   43.13 ? 397 LYS   A CD  1 
ATOM   3001 C  CE  . LYS   A 1 412 ? -35.662 28.81   -31.864 1   49.15 ? 397 LYS   A CE  1 
ATOM   3002 N  NZ  . LYS   A 1 412 ? -35.062 27.816  -32.792 1   53.75 ? 397 LYS   A NZ  1 
ATOM   3003 N  N   . SER   A 1 413 ? -34.04  31.117  -25.156 1   26.88 ? 398 SER   A N   1 
ATOM   3004 C  CA  . SER   A 1 413 ? -34.085 31.127  -23.695 1   25.82 ? 398 SER   A CA  1 
ATOM   3005 C  C   . SER   A 1 413 ? -34.642 32.442  -23.128 1   25.68 ? 398 SER   A C   1 
ATOM   3006 O  O   . SER   A 1 413 ? -34.845 32.54   -21.914 1   25.95 ? 398 SER   A O   1 
ATOM   3007 C  CB  . SER   A 1 413 ? -32.697 30.87   -23.118 1   25.4  ? 398 SER   A CB  1 
ATOM   3008 O  OG  . SER   A 1 413 ? -32.259 29.617  -23.607 1   26.57 ? 398 SER   A OG  1 
ATOM   3009 N  N   . LEU   A 1 414 ? -34.894 33.451  -23.973 1   25.87 ? 399 LEU   A N   1 
ATOM   3010 C  CA  . LEU   A 1 414 ? -35.483 34.707  -23.513 1   27.19 ? 399 LEU   A CA  1 
ATOM   3011 C  C   . LEU   A 1 414 ? -36.89  34.432  -22.968 1   29.15 ? 399 LEU   A C   1 
ATOM   3012 O  O   . LEU   A 1 414 ? -37.612 33.591  -23.511 1   29.13 ? 399 LEU   A O   1 
ATOM   3013 C  CB  . LEU   A 1 414 ? -35.546 35.747  -24.646 1   27.08 ? 399 LEU   A CB  1 
ATOM   3014 C  CG  . LEU   A 1 414 ? -34.196 36.377  -25.024 1   27.89 ? 399 LEU   A CG  1 
ATOM   3015 C  CD1 . LEU   A 1 414 ? -34.304 37.176  -26.314 1   28.7  ? 399 LEU   A CD1 1 
ATOM   3016 C  CD2 . LEU   A 1 414 ? -33.696 37.264  -23.921 1   27.51 ? 399 LEU   A CD2 1 
ATOM   3017 N  N   . LEU   A 1 415 ? -37.201 35.005  -21.828 1   31.12 ? 400 LEU   A N   1 
ATOM   3018 C  CA  . LEU   A 1 415 ? -38.512 34.812  -21.207 1   34.14 ? 400 LEU   A CA  1 
ATOM   3019 C  C   . LEU   A 1 415 ? -39.579 35.675  -21.914 1   38.97 ? 400 LEU   A C   1 
ATOM   3020 O  O   . LEU   A 1 415 ? -40.75  35.29   -21.913 1   40.1  ? 400 LEU   A O   1 
ATOM   3021 C  CB  . LEU   A 1 415 ? -38.46  35.131  -19.707 1   33.11 ? 400 LEU   A CB  1 
ATOM   3022 C  CG  . LEU   A 1 415 ? -37.44  34.34   -18.899 1   33.71 ? 400 LEU   A CG  1 
ATOM   3023 C  CD1 . LEU   A 1 415 ? -37.409 34.798  -17.461 1   33.58 ? 400 LEU   A CD1 1 
ATOM   3024 C  CD2 . LEU   A 1 415 ? -37.632 32.834  -19.055 1   33.83 ? 400 LEU   A CD2 1 
ATOM   3025 N  N   . LYS   A 1 416 ? -39.186 36.802  -22.536 1   41.5  ? 401 LYS   A N   1 
ATOM   3026 C  CA  . LYS   A 1 416 ? -40.139 37.681  -23.19  1   45.67 ? 401 LYS   A CA  1 
ATOM   3027 C  C   . LYS   A 1 416 ? -39.756 38.03   -24.636 1   50.28 ? 401 LYS   A C   1 
ATOM   3028 O  O   . LYS   A 1 416 ? -40.403 37.491  -25.539 1   51.28 ? 401 LYS   A O   1 
ATOM   3029 C  CB  . LYS   A 1 416 ? -40.382 38.941  -22.328 1   47.84 ? 401 LYS   A CB  1 
ATOM   3030 C  CG  . LYS   A 1 416 ? -41.272 40.003  -22.919 1   52.78 ? 401 LYS   A CG  1 
ATOM   3031 C  CD  . LYS   A 1 416 ? -41.442 41.12   -21.895 1   58.62 ? 401 LYS   A CD  1 
ATOM   3032 C  CE  . LYS   A 1 416 ? -40.775 42.401  -22.33  1   63.55 ? 401 LYS   A CE  1 
ATOM   3033 N  NZ  . LYS   A 1 416 ? -39.516 42.143  -23.081 1   66.86 ? 401 LYS   A NZ  1 
ATOM   3034 N  N   . GLU   A 1 417 ? -38.725 38.912  -24.874 1   52.72 ? 402 GLU   A N   1 
ATOM   3035 C  CA  . GLU   A 1 417 ? -38.321 39.443  -26.198 1   54.84 ? 402 GLU   A CA  1 
ATOM   3036 C  C   . GLU   A 1 417 ? -38.543 38.478  -27.36  1   56.12 ? 402 GLU   A C   1 
ATOM   3037 O  O   . GLU   A 1 417 ? -37.899 37.432  -27.441 1   57.01 ? 402 GLU   A O   1 
ATOM   3038 C  CB  . GLU   A 1 417 ? -36.868 39.973  -26.208 1   58.18 ? 402 GLU   A CB  1 
ATOM   3039 C  CG  . GLU   A 1 417 ? -36.319 40.416  -27.563 1   63.89 ? 402 GLU   A CG  1 
ATOM   3040 C  CD  . GLU   A 1 417 ? -36.719 41.787  -28.091 1   72.24 ? 402 GLU   A CD  1 
ATOM   3041 O  OE1 . GLU   A 1 417 ? -35.809 42.544  -28.503 1   74.19 ? 402 GLU   A OE1 1 
ATOM   3042 O  OE2 . GLU   A 1 417 ? -37.934 42.1    -28.119 1   73.68 ? 402 GLU   A OE2 1 
ATOM   3043 N  N   . GLY   A 1 418 ? -39.462 38.841  -28.243 1   55.89 ? 403 GLY   A N   1 
ATOM   3044 C  CA  . GLY   A 1 418 ? -39.755 38.027  -29.404 1   55.9  ? 403 GLY   A CA  1 
ATOM   3045 C  C   . GLY   A 1 418 ? -40.545 38.829  -30.418 1   55.49 ? 403 GLY   A C   1 
ATOM   3046 O  O   . GLY   A 1 418 ? -41.788 38.715  -30.396 1   55.02 ? 403 GLY   A O   1 
ATOM   3047 O  OXT . GLY   A 1 418 ? -39.925 39.537  -31.251 1   54.06 ? 403 GLY   A OXT 1 
ATOM   3048 N  N   . ILE   B 1 26  ? -22.096 11.587  2.85    1   43.42 ? 11  ILE   B N   1 
ATOM   3049 C  CA  . ILE   B 1 26  ? -22.702 11.776  1.52    1   42.44 ? 11  ILE   B CA  1 
ATOM   3050 C  C   . ILE   B 1 26  ? -24.075 12.42   1.663   1   40.86 ? 11  ILE   B C   1 
ATOM   3051 O  O   . ILE   B 1 26  ? -24.979 11.824  2.244   1   41.3  ? 11  ILE   B O   1 
ATOM   3052 C  CB  . ILE   B 1 26  ? -22.748 10.445  0.749   1   42.41 ? 11  ILE   B CB  1 
ATOM   3053 C  CG1 . ILE   B 1 26  ? -21.32  9.996   0.407   1   42.86 ? 11  ILE   B CG1 1 
ATOM   3054 C  CG2 . ILE   B 1 26  ? -23.609 10.575  -0.52   1   42.95 ? 11  ILE   B CG2 1 
ATOM   3055 C  CD1 . ILE   B 1 26  ? -21.205 8.645   0.06    1   43.7  ? 11  ILE   B CD1 1 
ATOM   3056 N  N   . SER   B 1 27  ? -24.205 13.643  1.167   1   39.4  ? 12  SER   B N   1 
ATOM   3057 C  CA  . SER   B 1 27  ? -25.421 14.434  1.211   1   39.41 ? 12  SER   B CA  1 
ATOM   3058 C  C   . SER   B 1 27  ? -26.625 13.681  0.644   1   38.28 ? 12  SER   B C   1 
ATOM   3059 O  O   . SER   B 1 27  ? -26.501 12.963  -0.353  1   37.5  ? 12  SER   B O   1 
ATOM   3060 C  CB  . SER   B 1 27  ? -25.227 15.72   0.419   1   41.04 ? 12  SER   B CB  1 
ATOM   3061 O  OG  . SER   B 1 27  ? -26.418 16.491  0.361   1   43.94 ? 12  SER   B OG  1 
ATOM   3062 N  N   . LYS   B 1 28  ? -27.784 13.873  1.277   1   37.45 ? 13  LYS   B N   1 
ATOM   3063 C  CA  . LYS   B 1 28  ? -29.039 13.277  0.843   1   37.29 ? 13  LYS   B CA  1 
ATOM   3064 C  C   . LYS   B 1 28  ? -29.469 13.798  -0.553  1   36.2  ? 13  LYS   B C   1 
ATOM   3065 O  O   . LYS   B 1 28  ? -30.23  13.121  -1.245  1   35.65 ? 13  LYS   B O   1 
ATOM   3066 C  CB  . LYS   B 1 28  ? -30.141 13.503  1.905   1   39.13 ? 13  LYS   B CB  1 
ATOM   3067 N  N   . GLU   B 1 29  ? -28.947 14.965  -0.989  1   35.66 ? 14  GLU   B N   1 
ATOM   3068 C  CA  . GLU   B 1 29  ? -29.291 15.491  -2.308  1   35.49 ? 14  GLU   B CA  1 
ATOM   3069 C  C   . GLU   B 1 29  ? -28.674 14.671  -3.479  1   34.06 ? 14  GLU   B C   1 
ATOM   3070 O  O   . GLU   B 1 29  ? -28.997 14.916  -4.64   1   33.9  ? 14  GLU   B O   1 
ATOM   3071 C  CB  . GLU   B 1 29  ? -28.965 16.982  -2.417  1   38.98 ? 14  GLU   B CB  1 
ATOM   3072 C  CG  . GLU   B 1 29  ? -27.503 17.262  -2.642  1   46.85 ? 14  GLU   B CG  1 
ATOM   3073 N  N   . TYR   B 1 30  ? -27.813 13.692  -3.17   1   32.63 ? 15  TYR   B N   1 
ATOM   3074 C  CA  . TYR   B 1 30  ? -27.245 12.795  -4.186  1   32.09 ? 15  TYR   B CA  1 
ATOM   3075 C  C   . TYR   B 1 30  ? -28.134 11.57   -4.429  1   32.14 ? 15  TYR   B C   1 
ATOM   3076 O  O   . TYR   B 1 30  ? -27.882 10.826  -5.382  1   32.04 ? 15  TYR   B O   1 
ATOM   3077 C  CB  . TYR   B 1 30  ? -25.837 12.335  -3.796  1   31.43 ? 15  TYR   B CB  1 
ATOM   3078 C  CG  . TYR   B 1 30  ? -24.856 13.478  -3.866  1   31.78 ? 15  TYR   B CG  1 
ATOM   3079 C  CD1 . TYR   B 1 30  ? -24.703 14.213  -5.032  1   31.83 ? 15  TYR   B CD1 1 
ATOM   3080 C  CD2 . TYR   B 1 30  ? -24.114 13.853  -2.754  1   32.29 ? 15  TYR   B CD2 1 
ATOM   3081 C  CE1 . TYR   B 1 30  ? -23.819 15.278  -5.098  1   32.95 ? 15  TYR   B CE1 1 
ATOM   3082 C  CE2 . TYR   B 1 30  ? -23.22  14.914  -2.812  1   32.99 ? 15  TYR   B CE2 1 
ATOM   3083 C  CZ  . TYR   B 1 30  ? -23.069 15.616  -3.99   1   34.11 ? 15  TYR   B CZ  1 
ATOM   3084 O  OH  . TYR   B 1 30  ? -22.21  16.68   -4.069  1   36.32 ? 15  TYR   B OH  1 
ATOM   3085 N  N   . HIS   B 1 31  ? -29.116 11.319  -3.546  1   31.5  ? 16  HIS   B N   1 
ATOM   3086 C  CA  . HIS   B 1 31  ? -30.061 10.232  -3.704  1   31.81 ? 16  HIS   B CA  1 
ATOM   3087 C  C   . HIS   B 1 31  ? -29.387 8.886   -3.792  1   31.44 ? 16  HIS   B C   1 
ATOM   3088 O  O   . HIS   B 1 31  ? -29.684 8.082   -4.668  1   31.24 ? 16  HIS   B O   1 
ATOM   3089 C  CB  . HIS   B 1 31  ? -31.01  10.504  -4.882  1   33.9  ? 16  HIS   B CB  1 
ATOM   3090 C  CG  . HIS   B 1 31  ? -31.881 11.704  -4.646  1   38.04 ? 16  HIS   B CG  1 
ATOM   3091 N  ND1 . HIS   B 1 31  ? -32.843 11.712  -3.645  1   40.32 ? 16  HIS   B ND1 1 
ATOM   3092 C  CD2 . HIS   B 1 31  ? -31.899 12.9    -5.277  1   40.28 ? 16  HIS   B CD2 1 
ATOM   3093 C  CE1 . HIS   B 1 31  ? -33.399 12.913  -3.689  1   41.69 ? 16  HIS   B CE1 1 
ATOM   3094 N  NE2 . HIS   B 1 31  ? -32.867 13.666  -4.654  1   41.8  ? 16  HIS   B NE2 1 
ATOM   3095 N  N   . ILE   B 1 32  ? -28.467 8.645   -2.857  1   31.26 ? 17  ILE   B N   1 
ATOM   3096 C  CA  . ILE   B 1 32  ? -27.795 7.369   -2.715  1   32.18 ? 17  ILE   B CA  1 
ATOM   3097 C  C   . ILE   B 1 32  ? -28.358 6.771   -1.425  1   33.79 ? 17  ILE   B C   1 
ATOM   3098 O  O   . ILE   B 1 32  ? -28.249 7.366   -0.349  1   34.17 ? 17  ILE   B O   1 
ATOM   3099 C  CB  . ILE   B 1 32  ? -26.262 7.537   -2.641  1   32.07 ? 17  ILE   B CB  1 
ATOM   3100 C  CG1 . ILE   B 1 32  ? -25.733 8.216   -3.921  1   33.49 ? 17  ILE   B CG1 1 
ATOM   3101 C  CG2 . ILE   B 1 32  ? -25.592 6.198   -2.398  1   31.72 ? 17  ILE   B CG2 1 
ATOM   3102 C  CD1 . ILE   B 1 32  ? -24.272 8.631   -3.832  1   35.05 ? 17  ILE   B CD1 1 
ATOM   3103 N  N   . ASP   B 1 33  ? -29.038 5.65    -1.551  1   34.18 ? 18  ASP   B N   1 
ATOM   3104 C  CA  . ASP   B 1 33  ? -29.649 4.974   -0.43   1   34.66 ? 18  ASP   B CA  1 
ATOM   3105 C  C   . ASP   B 1 33  ? -28.613 4.21    0.383   1   35.97 ? 18  ASP   B C   1 
ATOM   3106 O  O   . ASP   B 1 33  ? -27.673 3.656   -0.185  1   36.04 ? 18  ASP   B O   1 
ATOM   3107 C  CB  . ASP   B 1 33  ? -30.712 4.008   -0.94   1   34.72 ? 18  ASP   B CB  1 
ATOM   3108 C  CG  . ASP   B 1 33  ? -31.585 3.472   0.179   1   36.84 ? 18  ASP   B CG  1 
ATOM   3109 O  OD1 . ASP   B 1 33  ? -32.355 4.266   0.763   1   36.62 ? 18  ASP   B OD1 1 
ATOM   3110 O  OD2 . ASP   B 1 33  ? -31.481 2.268   0.481   1   38.58 ? 18  ASP   B OD2 1 
ATOM   3111 N  N   . GLU   B 1 34  ? -28.778 4.172   1.721   1   36.42 ? 19  GLU   B N   1 
ATOM   3112 C  CA  . GLU   B 1 34  ? -27.834 3.449   2.574   1   37.07 ? 19  GLU   B CA  1 
ATOM   3113 C  C   . GLU   B 1 34  ? -27.825 1.961   2.28    1   37.5  ? 19  GLU   B C   1 
ATOM   3114 O  O   . GLU   B 1 34  ? -26.789 1.319   2.419   1   38.53 ? 19  GLU   B O   1 
ATOM   3115 C  CB  . GLU   B 1 34  ? -28.174 3.671   4.059   1   39.06 ? 19  GLU   B CB  1 
ATOM   3116 N  N   . GLU   B 1 35  ? -28.977 1.4     1.908   1   36.9  ? 20  GLU   B N   1 
ATOM   3117 C  CA  . GLU   B 1 35  ? -29.089 -0.029  1.662   1   36.59 ? 20  GLU   B CA  1 
ATOM   3118 C  C   . GLU   B 1 35  ? -28.885 -0.426  0.209   1   35.17 ? 20  GLU   B C   1 
ATOM   3119 O  O   . GLU   B 1 35  ? -28.191 -1.399  -0.041  1   35.55 ? 20  GLU   B O   1 
ATOM   3120 C  CB  . GLU   B 1 35  ? -30.445 -0.556  2.163   1   38.91 ? 20  GLU   B CB  1 
ATOM   3121 C  CG  . GLU   B 1 35  ? -30.574 -2.066  2.075   1   43.74 ? 20  GLU   B CG  1 
ATOM   3122 C  CD  . GLU   B 1 35  ? -31.931 -2.618  2.481   1   51    ? 20  GLU   B CD  1 
ATOM   3123 O  OE1 . GLU   B 1 35  ? -32.926 -1.858  2.42    1   52.51 ? 20  GLU   B OE1 1 
ATOM   3124 O  OE2 . GLU   B 1 35  ? -32     -3.817  2.847   1   51.39 ? 20  GLU   B OE2 1 
ATOM   3125 N  N   . VAL   B 1 36  ? -29.527 0.273   -0.744  1   33.78 ? 21  VAL   B N   1 
ATOM   3126 C  CA  . VAL   B 1 36  ? -29.447 -0.145  -2.15   1   32.19 ? 21  VAL   B CA  1 
ATOM   3127 C  C   . VAL   B 1 36  ? -28.604 0.785   -3.058  1   30.51 ? 21  VAL   B C   1 
ATOM   3128 O  O   . VAL   B 1 36  ? -28.612 0.588   -4.273  1   30.49 ? 21  VAL   B O   1 
ATOM   3129 C  CB  . VAL   B 1 36  ? -30.855 -0.375  -2.727  1   32.09 ? 21  VAL   B CB  1 
ATOM   3130 C  CG1 . VAL   B 1 36  ? -31.58  -1.462  -1.94   1   33.09 ? 21  VAL   B CG1 1 
ATOM   3131 C  CG2 . VAL   B 1 36  ? -31.674 0.909   -2.732  1   31.49 ? 21  VAL   B CG2 1 
ATOM   3132 N  N   . GLY   B 1 37  ? -27.9   1.758   -2.474  1   28.69 ? 22  GLY   B N   1 
ATOM   3133 C  CA  . GLY   B 1 37  ? -27.011 2.662   -3.205  1   27.9  ? 22  GLY   B CA  1 
ATOM   3134 C  C   . GLY   B 1 37  ? -27.675 3.488   -4.277  1   27.2  ? 22  GLY   B C   1 
ATOM   3135 O  O   . GLY   B 1 37  ? -28.579 4.263   -3.973  1   28.02 ? 22  GLY   B O   1 
ATOM   3136 N  N   . PHE   B 1 38  ? -27.232 3.353   -5.544  1   25.69 ? 23  PHE   B N   1 
ATOM   3137 C  CA  . PHE   B 1 38  ? -27.836 4.112   -6.645  1   25.51 ? 23  PHE   B CA  1 
ATOM   3138 C  C   . PHE   B 1 38  ? -29.211 3.567   -7.098  1   26.02 ? 23  PHE   B C   1 
ATOM   3139 O  O   . PHE   B 1 38  ? -29.938 4.269   -7.807  1   26.1  ? 23  PHE   B O   1 
ATOM   3140 C  CB  . PHE   B 1 38  ? -26.884 4.192   -7.852  1   25.55 ? 23  PHE   B CB  1 
ATOM   3141 C  CG  . PHE   B 1 38  ? -25.625 4.986   -7.56   1   25.82 ? 23  PHE   B CG  1 
ATOM   3142 C  CD1 . PHE   B 1 38  ? -25.644 6.371   -7.571  1   27.08 ? 23  PHE   B CD1 1 
ATOM   3143 C  CD2 . PHE   B 1 38  ? -24.444 4.346   -7.234  1   26.47 ? 23  PHE   B CD2 1 
ATOM   3144 C  CE1 . PHE   B 1 38  ? -24.492 7.105   -7.283  1   27.28 ? 23  PHE   B CE1 1 
ATOM   3145 C  CE2 . PHE   B 1 38  ? -23.289 5.084   -6.935  1   27.02 ? 23  PHE   B CE2 1 
ATOM   3146 C  CZ  . PHE   B 1 38  ? -23.321 6.457   -6.983  1   26.83 ? 23  PHE   B CZ  1 
ATOM   3147 N  N   . ALA   B 1 39  ? -29.565 2.343   -6.693  1   26.49 ? 24  ALA   B N   1 
ATOM   3148 C  CA  . ALA   B 1 39  ? -30.883 1.789   -7.03   1   28.11 ? 24  ALA   B CA  1 
ATOM   3149 C  C   . ALA   B 1 39  ? -31.988 2.617   -6.359  1   30.06 ? 24  ALA   B C   1 
ATOM   3150 O  O   . ALA   B 1 39  ? -31.742 3.3     -5.344  1   30.39 ? 24  ALA   B O   1 
ATOM   3151 C  CB  . ALA   B 1 39  ? -30.983 0.335   -6.589  1   27.54 ? 24  ALA   B CB  1 
ATOM   3152 N  N   . LEU   B 1 40  ? -33.188 2.609   -6.956  1   29.96 ? 25  LEU   B N   1 
ATOM   3153 C  CA  . LEU   B 1 40  ? -34.32  3.328   -6.377  1   30.98 ? 25  LEU   B CA  1 
ATOM   3154 C  C   . LEU   B 1 40  ? -34.848 2.485   -5.211  1   33.03 ? 25  LEU   B C   1 
ATOM   3155 O  O   . LEU   B 1 40  ? -35.172 1.311   -5.391  1   32.91 ? 25  LEU   B O   1 
ATOM   3156 C  CB  . LEU   B 1 40  ? -35.415 3.514   -7.437  1   30.57 ? 25  LEU   B CB  1 
ATOM   3157 C  CG  . LEU   B 1 40  ? -36.664 4.29    -7.019  1   30.08 ? 25  LEU   B CG  1 
ATOM   3158 C  CD1 . LEU   B 1 40  ? -36.346 5.769   -6.806  1   29.92 ? 25  LEU   B CD1 1 
ATOM   3159 C  CD2 . LEU   B 1 40  ? -37.732 4.165   -8.08   1   29.95 ? 25  LEU   B CD2 1 
ATOM   3160 N  N   . PRO   B 1 41  ? -34.853 3.039   -3.988  1   34.65 ? 26  PRO   B N   1 
ATOM   3161 C  CA  . PRO   B 1 41  ? -35.343 2.26    -2.833  1   34.99 ? 26  PRO   B CA  1 
ATOM   3162 C  C   . PRO   B 1 41  ? -36.84  2.022   -2.944  1   35.1  ? 26  PRO   B C   1 
ATOM   3163 O  O   . PRO   B 1 41  ? -37.552 2.94    -3.353  1   34.47 ? 26  PRO   B O   1 
ATOM   3164 C  CB  . PRO   B 1 41  ? -35.072 3.179   -1.63   1   36.21 ? 26  PRO   B CB  1 
ATOM   3165 C  CG  . PRO   B 1 41  ? -34.253 4.314   -2.143  1   36.76 ? 26  PRO   B CG  1 
ATOM   3166 C  CD  . PRO   B 1 41  ? -34.476 4.417   -3.612  1   34.92 ? 26  PRO   B CD  1 
ATOM   3167 N  N   A ASN   B 1 42  ? -37.326 0.808   -2.604  0.5 35.38 ? 27  ASN   B N   1 
ATOM   3168 N  N   B ASN   B 1 42  ? -37.313 0.798   -2.625  0.5 34.99 ? 27  ASN   B N   1 
ATOM   3169 C  CA  A ASN   B 1 42  ? -38.754 0.428   -2.63   0.5 36.48 ? 27  ASN   B CA  1 
ATOM   3170 C  CA  B ASN   B 1 42  ? -38.728 0.384   -2.663  0.5 35.74 ? 27  ASN   B CA  1 
ATOM   3171 C  C   A ASN   B 1 42  ? -39.528 1.043   -3.807  0.5 35.82 ? 27  ASN   B C   1 
ATOM   3172 C  C   B ASN   B 1 42  ? -39.527 1.018   -3.803  0.5 35.47 ? 27  ASN   B C   1 
ATOM   3173 O  O   A ASN   B 1 42  ? -40.329 1.96    -3.605  0.5 35.65 ? 27  ASN   B O   1 
ATOM   3174 O  O   B ASN   B 1 42  ? -40.336 1.919   -3.574  0.5 35.31 ? 27  ASN   B O   1 
ATOM   3175 C  CB  A ASN   B 1 42  ? -39.43  0.795   -1.281  0.5 39.05 ? 27  ASN   B CB  1 
ATOM   3176 C  CB  B ASN   B 1 42  ? -39.401 0.657   -1.315  0.5 37.35 ? 27  ASN   B CB  1 
ATOM   3177 C  CG  A ASN   B 1 42  ? -40.881 0.372   -1.134  0.5 43.87 ? 27  ASN   B CG  1 
ATOM   3178 C  CG  B ASN   B 1 42  ? -38.688 -0.01   -0.173  0.5 40.09 ? 27  ASN   B CG  1 
ATOM   3179 O  OD1 A ASN   B 1 42  ? -41.676 1.028   -0.442  0.5 45.68 ? 27  ASN   B OD1 1 
ATOM   3180 O  OD1 B ASN   B 1 42  ? -38.574 -1.241  -0.112  0.5 41.48 ? 27  ASN   B OD1 1 
ATOM   3181 N  ND2 A ASN   B 1 42  ? -41.268 -0.72   -1.789  0.5 44.94 ? 27  ASN   B ND2 1 
ATOM   3182 N  ND2 B ASN   B 1 42  ? -38.17  0.797   0.742   0.5 40.39 ? 27  ASN   B ND2 1 
ATOM   3183 N  N   . PRO   B 1 43  ? -39.206 0.651   -5.051  1   35.25 ? 28  PRO   B N   1 
ATOM   3184 C  CA  . PRO   B 1 43  ? -39.902 1.261   -6.197  1   34.85 ? 28  PRO   B CA  1 
ATOM   3185 C  C   . PRO   B 1 43  ? -41.428 1.104   -6.141  1   34.93 ? 28  PRO   B C   1 
ATOM   3186 O  O   . PRO   B 1 43  ? -41.918 0.079   -5.653  1   34.07 ? 28  PRO   B O   1 
ATOM   3187 C  CB  . PRO   B 1 43  ? -39.32  0.502   -7.399  1   35.5  ? 28  PRO   B CB  1 
ATOM   3188 C  CG  . PRO   B 1 43  ? -37.995 -0.037  -6.921  1   36.07 ? 28  PRO   B CG  1 
ATOM   3189 C  CD  . PRO   B 1 43  ? -38.249 -0.389  -5.485  1   34.65 ? 28  PRO   B CD  1 
ATOM   3190 N  N   . GLN   B 1 44  ? -42.156 2.117   -6.62   1   35.83 ? 29  GLN   B N   1 
ATOM   3191 C  CA  . GLN   B 1 44  ? -43.62  2.086   -6.695  1   37.78 ? 29  GLN   B CA  1 
ATOM   3192 C  C   . GLN   B 1 44  ? -44.018 1.015   -7.723  1   38.97 ? 29  GLN   B C   1 
ATOM   3193 O  O   . GLN   B 1 44  ? -43.356 0.862   -8.758  1   38.39 ? 29  GLN   B O   1 
ATOM   3194 C  CB  . GLN   B 1 44  ? -44.152 3.458   -7.114  1   40.49 ? 29  GLN   B CB  1 
ATOM   3195 C  CG  . GLN   B 1 44  ? -45.651 3.646   -6.877  1   46.2  ? 29  GLN   B CG  1 
ATOM   3196 C  CD  . GLN   B 1 44  ? -46.003 5.103   -6.958  1   52.4  ? 29  GLN   B CD  1 
ATOM   3197 O  OE1 . GLN   B 1 44  ? -45.336 5.955   -6.361  1   54.74 ? 29  GLN   B OE1 1 
ATOM   3198 N  NE2 . GLN   B 1 44  ? -47.051 5.43    -7.706  1   53.89 ? 29  GLN   B NE2 1 
ATOM   3199 N  N   . GLU   B 1 45  ? -45.079 0.258   -7.427  1   39.62 ? 30  GLU   B N   1 
ATOM   3200 C  CA  A GLU   B 1 45  ? -45.538 -0.815  -8.303  0.5 40.57 ? 30  GLU   B CA  1 
ATOM   3201 C  CA  B GLU   B 1 45  ? -45.53  -0.802  -8.326  0.5 40.66 ? 30  GLU   B CA  1 
ATOM   3202 C  C   . GLU   B 1 45  ? -46.801 -0.424  -9.085  1   41.71 ? 30  GLU   B C   1 
ATOM   3203 O  O   . GLU   B 1 45  ? -47.001 -0.881  -10.216 1   42.11 ? 30  GLU   B O   1 
ATOM   3204 C  CB  A GLU   B 1 45  ? -45.784 -2.088  -7.478  0.5 42.38 ? 30  GLU   B CB  1 
ATOM   3205 C  CB  B GLU   B 1 45  ? -45.737 -2.121  -7.568  0.5 42.78 ? 30  GLU   B CB  1 
ATOM   3206 C  CG  A GLU   B 1 45  ? -44.605 -2.463  -6.597  0.5 45.9  ? 30  GLU   B CG  1 
ATOM   3207 C  CG  B GLU   B 1 45  ? -46     -3.297  -8.494  0.5 46.93 ? 30  GLU   B CG  1 
ATOM   3208 C  CD  A GLU   B 1 45  ? -44.859 -3.612  -5.644  0.5 51.3  ? 30  GLU   B CD  1 
ATOM   3209 C  CD  B GLU   B 1 45  ? -46.326 -4.608  -7.814  0.5 51.06 ? 30  GLU   B CD  1 
ATOM   3210 O  OE1 A GLU   B 1 45  ? -44.247 -3.628  -4.551  0.5 52.95 ? 30  GLU   B OE1 1 
ATOM   3211 O  OE1 B GLU   B 1 45  ? -46.194 -4.686  -6.571  0.5 51.9  ? 30  GLU   B OE1 1 
ATOM   3212 O  OE2 A GLU   B 1 45  ? -45.668 -4.502  -5.991  0.5 52.14 ? 30  GLU   B OE2 1 
ATOM   3213 O  OE2 B GLU   B 1 45  ? -46.702 -5.564  -8.529  0.5 52.41 ? 30  GLU   B OE2 1 
ATOM   3214 N  N   . ASN   B 1 46  ? -47.654 0.434   -8.493  1   42.27 ? 31  ASN   B N   1 
ATOM   3215 C  CA  . ASN   B 1 46  ? -48.889 0.852   -9.158  1   42.77 ? 31  ASN   B CA  1 
ATOM   3216 C  C   . ASN   B 1 46  ? -48.934 2.345   -9.414  1   42.18 ? 31  ASN   B C   1 
ATOM   3217 O  O   . ASN   B 1 46  ? -48.426 3.124   -8.613  1   42.43 ? 31  ASN   B O   1 
ATOM   3218 C  CB  . ASN   B 1 46  ? -50.11  0.429   -8.327  1   44.86 ? 31  ASN   B CB  1 
ATOM   3219 C  CG  . ASN   B 1 46  ? -50.085 -1.025  -7.947  1   50.13 ? 31  ASN   B CG  1 
ATOM   3220 O  OD1 . ASN   B 1 46  ? -50.122 -1.918  -8.802  1   51.71 ? 31  ASN   B OD1 1 
ATOM   3221 N  ND2 . ASN   B 1 46  ? -49.982 -1.299  -6.653  1   52.37 ? 31  ASN   B ND2 1 
ATOM   3222 N  N   . LEU   B 1 47  ? -49.506 2.753   -10.541 1   41.41 ? 32  LEU   B N   1 
ATOM   3223 C  CA  . LEU   B 1 47  ? -49.669 4.176   -10.858 1   42.07 ? 32  LEU   B CA  1 
ATOM   3224 C  C   . LEU   B 1 47  ? -51.093 4.609   -10.422 1   44.47 ? 32  LEU   B C   1 
ATOM   3225 O  O   . LEU   B 1 47  ? -51.966 3.741   -10.275 1   44.71 ? 32  LEU   B O   1 
ATOM   3226 C  CB  . LEU   B 1 47  ? -49.55  4.389   -12.384 1   41.46 ? 32  LEU   B CB  1 
ATOM   3227 C  CG  . LEU   B 1 47  ? -48.147 4.349   -13.017 1   41.65 ? 32  LEU   B CG  1 
ATOM   3228 C  CD1 . LEU   B 1 47  ? -48.239 4.514   -14.522 1   41.15 ? 32  LEU   B CD1 1 
ATOM   3229 C  CD2 . LEU   B 1 47  ? -47.257 5.447   -12.441 1   42.3  ? 32  LEU   B CD2 1 
ATOM   3230 N  N   . PRO   B 1 48  ? -51.411 5.923   -10.31  1   45.96 ? 33  PRO   B N   1 
ATOM   3231 C  CA  . PRO   B 1 48  ? -52.815 6.31    -10.055 1   47.25 ? 33  PRO   B CA  1 
ATOM   3232 C  C   . PRO   B 1 48  ? -53.765 5.713   -11.123 1   48.68 ? 33  PRO   B C   1 
ATOM   3233 O  O   . PRO   B 1 48  ? -53.322 5.406   -12.241 1   49.24 ? 33  PRO   B O   1 
ATOM   3234 C  CB  . PRO   B 1 48  ? -52.777 7.843   -10.143 1   47.89 ? 33  PRO   B CB  1 
ATOM   3235 C  CG  . PRO   B 1 48  ? -51.365 8.211   -9.83   1   48.22 ? 33  PRO   B CG  1 
ATOM   3236 C  CD  . PRO   B 1 48  ? -50.548 7.112   -10.459 1   46.05 ? 33  PRO   B CD  1 
ATOM   3237 N  N   . ASP   B 1 49  ? -55.056 5.506   -10.777 1   48.66 ? 34  ASP   B N   1 
ATOM   3238 C  CA  . ASP   B 1 49  ? -56.05  4.918   -11.687 1   48.69 ? 34  ASP   B CA  1 
ATOM   3239 C  C   . ASP   B 1 49  ? -56.15  5.621   -13.029 1   46.88 ? 34  ASP   B C   1 
ATOM   3240 O  O   . ASP   B 1 49  ? -56.511 4.992   -14.022 1   46.7  ? 34  ASP   B O   1 
ATOM   3241 C  CB  . ASP   B 1 49  ? -57.441 4.9     -11.034 1   52.69 ? 34  ASP   B CB  1 
ATOM   3242 C  CG  . ASP   B 1 49  ? -57.6   3.915   -9.902  1   60.84 ? 34  ASP   B CG  1 
ATOM   3243 O  OD1 . ASP   B 1 49  ? -56.714 3.034   -9.746  1   61.94 ? 34  ASP   B OD1 1 
ATOM   3244 O  OD2 . ASP   B 1 49  ? -58.618 4.012   -9.175  1   64.93 ? 34  ASP   B OD2 1 
ATOM   3245 N  N   . PHE   B 1 50  ? -55.848 6.919   -13.063 1   45.71 ? 35  PHE   B N   1 
ATOM   3246 C  CA  . PHE   B 1 50  ? -55.875 7.722   -14.286 1   45.77 ? 35  PHE   B CA  1 
ATOM   3247 C  C   . PHE   B 1 50  ? -55.022 7.091   -15.418 1   45.62 ? 35  PHE   B C   1 
ATOM   3248 O  O   . PHE   B 1 50  ? -55.358 7.205   -16.597 1   46.13 ? 35  PHE   B O   1 
ATOM   3249 C  CB  . PHE   B 1 50  ? -55.338 9.124   -13.96  1   45.88 ? 35  PHE   B CB  1 
ATOM   3250 C  CG  . PHE   B 1 50  ? -55.459 10.153  -15.056 1   47.01 ? 35  PHE   B CG  1 
ATOM   3251 C  CD1 . PHE   B 1 50  ? -56.641 10.847  -15.249 1   47.99 ? 35  PHE   B CD1 1 
ATOM   3252 C  CD2 . PHE   B 1 50  ? -54.368 10.486  -15.839 1   48.03 ? 35  PHE   B CD2 1 
ATOM   3253 C  CE1 . PHE   B 1 50  ? -56.744 11.811  -16.246 1   48.93 ? 35  PHE   B CE1 1 
ATOM   3254 C  CE2 . PHE   B 1 50  ? -54.472 11.45   -16.833 1   48.92 ? 35  PHE   B CE2 1 
ATOM   3255 C  CZ  . PHE   B 1 50  ? -55.658 12.109  -17.029 1   48.95 ? 35  PHE   B CZ  1 
ATOM   3256 N  N   . TYR   B 1 51  ? -53.947 6.395   -15.039 1   44.33 ? 36  TYR   B N   1 
ATOM   3257 C  CA  . TYR   B 1 51  ? -53     5.787   -15.973 1   43.34 ? 36  TYR   B CA  1 
ATOM   3258 C  C   . TYR   B 1 51  ? -53.215 4.302   -16.226 1   43.22 ? 36  TYR   B C   1 
ATOM   3259 O  O   . TYR   B 1 51  ? -52.333 3.666   -16.804 1   43.19 ? 36  TYR   B O   1 
ATOM   3260 C  CB  . TYR   B 1 51  ? -51.576 6.021   -15.446 1   41.96 ? 36  TYR   B CB  1 
ATOM   3261 C  CG  . TYR   B 1 51  ? -51.272 7.494   -15.329 1   40.68 ? 36  TYR   B CG  1 
ATOM   3262 C  CD1 . TYR   B 1 51  ? -51.125 8.28    -16.459 1   41.1  ? 36  TYR   B CD1 1 
ATOM   3263 C  CD2 . TYR   B 1 51  ? -51.238 8.12    -14.094 1   40.75 ? 36  TYR   B CD2 1 
ATOM   3264 C  CE1 . TYR   B 1 51  ? -50.863 9.636   -16.365 1   42.03 ? 36  TYR   B CE1 1 
ATOM   3265 C  CE2 . TYR   B 1 51  ? -51.002 9.482   -13.985 1   41.28 ? 36  TYR   B CE2 1 
ATOM   3266 C  CZ  . TYR   B 1 51  ? -50.804 10.237  -15.126 1   42.7  ? 36  TYR   B CZ  1 
ATOM   3267 O  OH  . TYR   B 1 51  ? -50.534 11.588  -15.078 1   44.03 ? 36  TYR   B OH  1 
ATOM   3268 N  N   . ASN   B 1 52  ? -54.371 3.74    -15.824 1   42.41 ? 37  ASN   B N   1 
ATOM   3269 C  CA  . ASN   B 1 52  ? -54.653 2.314   -16.034 1   42.08 ? 37  ASN   B CA  1 
ATOM   3270 C  C   . ASN   B 1 52  ? -54.437 1.829   -17.476 1   40.43 ? 37  ASN   B C   1 
ATOM   3271 O  O   . ASN   B 1 52  ? -54.035 0.686   -17.667 1   39.99 ? 37  ASN   B O   1 
ATOM   3272 C  CB  . ASN   B 1 52  ? -56.075 1.951   -15.592 1   44.78 ? 37  ASN   B CB  1 
ATOM   3273 C  CG  . ASN   B 1 52  ? -56.245 1.805   -14.11  1   50.37 ? 37  ASN   B CG  1 
ATOM   3274 O  OD1 . ASN   B 1 52  ? -55.284 1.598   -13.353 1   51.58 ? 37  ASN   B OD1 1 
ATOM   3275 N  ND2 . ASN   B 1 52  ? -57.486 1.917   -13.659 1   52.25 ? 37  ASN   B ND2 1 
ATOM   3276 N  N   . ASP   B 1 53  ? -54.699 2.681   -18.482 1   39.38 ? 38  ASP   B N   1 
ATOM   3277 C  CA  . ASP   B 1 53  ? -54.525 2.287   -19.885 1   39.68 ? 38  ASP   B CA  1 
ATOM   3278 C  C   . ASP   B 1 53  ? -53.039 2.059   -20.226 1   39.56 ? 38  ASP   B C   1 
ATOM   3279 O  O   . ASP   B 1 53  ? -52.72  1.191   -21.036 1   39.62 ? 38  ASP   B O   1 
ATOM   3280 C  CB  . ASP   B 1 53  ? -55.15  3.32    -20.845 1   41.05 ? 38  ASP   B CB  1 
ATOM   3281 C  CG  . ASP   B 1 53  ? -56.675 3.381   -20.776 1   44.28 ? 38  ASP   B CG  1 
ATOM   3282 O  OD1 . ASP   B 1 53  ? -57.286 2.429   -20.226 1   44.24 ? 38  ASP   B OD1 1 
ATOM   3283 O  OD2 . ASP   B 1 53  ? -57.25  4.382   -21.264 1   45.64 ? 38  ASP   B OD2 1 
ATOM   3284 N  N   . TRP   B 1 54  ? -52.141 2.833   -19.597 1   39.1  ? 39  TRP   B N   1 
ATOM   3285 C  CA  . TRP   B 1 54  ? -50.701 2.629   -19.764 1   38.02 ? 39  TRP   B CA  1 
ATOM   3286 C  C   . TRP   B 1 54  ? -50.312 1.332   -19.073 1   37.8  ? 39  TRP   B C   1 
ATOM   3287 O  O   . TRP   B 1 54  ? -49.591 0.511   -19.649 1   38.56 ? 39  TRP   B O   1 
ATOM   3288 C  CB  . TRP   B 1 54  ? -49.917 3.768   -19.099 1   36.94 ? 39  TRP   B CB  1 
ATOM   3289 C  CG  . TRP   B 1 54  ? -49.97  5.105   -19.764 1   36.14 ? 39  TRP   B CG  1 
ATOM   3290 C  CD1 . TRP   B 1 54  ? -50.59  5.435   -20.933 1   36.7  ? 39  TRP   B CD1 1 
ATOM   3291 C  CD2 . TRP   B 1 54  ? -49.318 6.283   -19.308 1   35.85 ? 39  TRP   B CD2 1 
ATOM   3292 N  NE1 . TRP   B 1 54  ? -50.366 6.753   -21.23  1   36.89 ? 39  TRP   B NE1 1 
ATOM   3293 C  CE2 . TRP   B 1 54  ? -49.6   7.305   -20.236 1   36.56 ? 39  TRP   B CE2 1 
ATOM   3294 C  CE3 . TRP   B 1 54  ? -48.516 6.576   -18.198 1   36.16 ? 39  TRP   B CE3 1 
ATOM   3295 C  CZ2 . TRP   B 1 54  ? -49.096 8.598   -20.095 1   37.22 ? 39  TRP   B CZ2 1 
ATOM   3296 C  CZ3 . TRP   B 1 54  ? -48.035 7.86    -18.051 1   37.02 ? 39  TRP   B CZ3 1 
ATOM   3297 C  CH2 . TRP   B 1 54  ? -48.323 8.855   -18.991 1   37.17 ? 39  TRP   B CH2 1 
ATOM   3298 N  N   . MET   B 1 55  ? -50.763 1.165   -17.822 1   37.18 ? 40  MET   B N   1 
ATOM   3299 C  CA  . MET   B 1 55  ? -50.415 0.016   -16.997 1   37.45 ? 40  MET   B CA  1 
ATOM   3300 C  C   . MET   B 1 55  ? -50.859 -1.3    -17.558 1   37.93 ? 40  MET   B C   1 
ATOM   3301 O  O   . MET   B 1 55  ? -50.104 -2.276  -17.479 1   37.97 ? 40  MET   B O   1 
ATOM   3302 C  CB  . MET   B 1 55  ? -50.913 0.179   -15.57  1   38    ? 40  MET   B CB  1 
ATOM   3303 C  CG  . MET   B 1 55  ? -50.31  -0.818  -14.632 1   40.76 ? 40  MET   B CG  1 
ATOM   3304 S  SD  . MET   B 1 55  ? -48.49  -0.67   -14.454 1   45.08 ? 40  MET   B SD  1 
ATOM   3305 C  CE  . MET   B 1 55  ? -48.395 0.913   -13.826 1   42.02 ? 40  MET   B CE  1 
ATOM   3306 N  N   . PHE   B 1 56  ? -52.077 -1.358  -18.157 1   37.56 ? 41  PHE   B N   1 
ATOM   3307 C  CA  . PHE   B 1 56  ? -52.541 -2.607  -18.758 1   37.75 ? 41  PHE   B CA  1 
ATOM   3308 C  C   . PHE   B 1 56  ? -51.575 -3.045  -19.88  1   35.52 ? 41  PHE   B C   1 
ATOM   3309 O  O   . PHE   B 1 56  ? -51.171 -4.203  -19.912 1   35.94 ? 41  PHE   B O   1 
ATOM   3310 C  CB  . PHE   B 1 56  ? -53.986 -2.484  -19.313 1   39.56 ? 41  PHE   B CB  1 
ATOM   3311 C  CG  . PHE   B 1 56  ? -54.364 -3.7    -20.131 1   42.11 ? 41  PHE   B CG  1 
ATOM   3312 C  CD1 . PHE   B 1 56  ? -54.67  -4.9    -19.516 1   43.67 ? 41  PHE   B CD1 1 
ATOM   3313 C  CD2 . PHE   B 1 56  ? -54.294 -3.673  -21.518 1   43.78 ? 41  PHE   B CD2 1 
ATOM   3314 C  CE1 . PHE   B 1 56  ? -54.935 -6.04   -20.274 1   44.75 ? 41  PHE   B CE1 1 
ATOM   3315 C  CE2 . PHE   B 1 56  ? -54.564 -4.814  -22.268 1   44.49 ? 41  PHE   B CE2 1 
ATOM   3316 C  CZ  . PHE   B 1 56  ? -54.878 -5.985  -21.642 1   44.38 ? 41  PHE   B CZ  1 
ATOM   3317 N  N   . ILE   B 1 57  ? -51.195 -2.114  -20.761 1   33.77 ? 42  ILE   B N   1 
ATOM   3318 C  CA  . ILE   B 1 57  ? -50.28  -2.446  -21.854 1   33.07 ? 42  ILE   B CA  1 
ATOM   3319 C  C   . ILE   B 1 57  ? -48.912 -2.926  -21.316 1   32.88 ? 42  ILE   B C   1 
ATOM   3320 O  O   . ILE   B 1 57  ? -48.466 -4.022  -21.658 1   32.03 ? 42  ILE   B O   1 
ATOM   3321 C  CB  . ILE   B 1 57  ? -50.142 -1.264  -22.831 1   32.89 ? 42  ILE   B CB  1 
ATOM   3322 C  CG1 . ILE   B 1 57  ? -51.506 -0.92   -23.471 1   32.47 ? 42  ILE   B CG1 1 
ATOM   3323 C  CG2 . ILE   B 1 57  ? -49.076 -1.58   -23.897 1   33.37 ? 42  ILE   B CG2 1 
ATOM   3324 C  CD1 . ILE   B 1 57  ? -51.441 0.309   -24.393 1   32.28 ? 42  ILE   B CD1 1 
ATOM   3325 N  N   . ALA   B 1 58  ? -48.292 -2.13   -20.422 1   33.1  ? 43  ALA   B N   1 
ATOM   3326 C  CA  . ALA   B 1 58  ? -46.978 -2.459  -19.846 1   32.71 ? 43  ALA   B CA  1 
ATOM   3327 C  C   . ALA   B 1 58  ? -46.953 -3.801  -19.126 1   32.45 ? 43  ALA   B C   1 
ATOM   3328 O  O   . ALA   B 1 58  ? -46.019 -4.565  -19.307 1   32.94 ? 43  ALA   B O   1 
ATOM   3329 C  CB  . ALA   B 1 58  ? -46.504 -1.346  -18.929 1   32.3  ? 43  ALA   B CB  1 
ATOM   3330 N  N   . LYS   B 1 59  ? -48.006 -4.133  -18.39  1   32.18 ? 44  LYS   B N   1 
ATOM   3331 C  CA  . LYS   B 1 59  ? -48.113 -5.411  -17.693 1   33.26 ? 44  LYS   B CA  1 
ATOM   3332 C  C   . LYS   B 1 59  ? -48.402 -6.617  -18.592 1   33.78 ? 44  LYS   B C   1 
ATOM   3333 O  O   . LYS   B 1 59  ? -48.285 -7.753  -18.125 1   34.35 ? 44  LYS   B O   1 
ATOM   3334 C  CB  . LYS   B 1 59  ? -49.213 -5.327  -16.624 1   36.89 ? 44  LYS   B CB  1 
ATOM   3335 C  CG  . LYS   B 1 59  ? -48.763 -4.597  -15.362 1   43.03 ? 44  LYS   B CG  1 
ATOM   3336 C  CD  . LYS   B 1 59  ? -49.955 -4.173  -14.504 1   50.53 ? 44  LYS   B CD  1 
ATOM   3337 C  CE  . LYS   B 1 59  ? -50.811 -5.32   -13.994 1   55.05 ? 44  LYS   B CE  1 
ATOM   3338 N  NZ  . LYS   B 1 59  ? -50.113 -6.136  -12.958 1   57.98 ? 44  LYS   B NZ  1 
ATOM   3339 N  N   . HIS   B 1 60  ? -48.8   -6.398  -19.85  1   33.91 ? 45  HIS   B N   1 
ATOM   3340 C  CA  . HIS   B 1 60  ? -49.127 -7.528  -20.735 1   34.71 ? 45  HIS   B CA  1 
ATOM   3341 C  C   . HIS   B 1 60  ? -48.282 -7.548  -22.008 1   34.08 ? 45  HIS   B C   1 
ATOM   3342 O  O   . HIS   B 1 60  ? -48.76  -8.007  -23.045 1   33.14 ? 45  HIS   B O   1 
ATOM   3343 C  CB  . HIS   B 1 60  ? -50.641 -7.528  -21.051 1   35.85 ? 45  HIS   B CB  1 
ATOM   3344 C  CG  . HIS   B 1 60  ? -51.471 -7.782  -19.833 1   40.22 ? 45  HIS   B CG  1 
ATOM   3345 N  ND1 . HIS   B 1 60  ? -51.909 -6.741  -19.023 1   42.59 ? 45  HIS   B ND1 1 
ATOM   3346 C  CD2 . HIS   B 1 60  ? -51.845 -8.957  -19.278 1   41.54 ? 45  HIS   B CD2 1 
ATOM   3347 C  CE1 . HIS   B 1 60  ? -52.555 -7.318  -18.026 1   43.1  ? 45  HIS   B CE1 1 
ATOM   3348 N  NE2 . HIS   B 1 60  ? -52.546 -8.649  -18.14  1   43.08 ? 45  HIS   B NE2 1 
ATOM   3349 N  N   . LEU   B 1 61  ? -47.019 -7.018  -21.952 1   33.06 ? 46  LEU   B N   1 
ATOM   3350 C  CA  . LEU   B 1 61  ? -46.181 -6.997  -23.149 1   31.88 ? 46  LEU   B CA  1 
ATOM   3351 C  C   . LEU   B 1 61  ? -45.958 -8.372  -23.749 1   31.6  ? 46  LEU   B C   1 
ATOM   3352 O  O   . LEU   B 1 61  ? -46.114 -8.482  -24.96  1   31.08 ? 46  LEU   B O   1 
ATOM   3353 C  CB  . LEU   B 1 61  ? -44.844 -6.271  -22.949 1   30.88 ? 46  LEU   B CB  1 
ATOM   3354 C  CG  . LEU   B 1 61  ? -44.952 -4.789  -22.643 1   31.07 ? 46  LEU   B CG  1 
ATOM   3355 C  CD1 . LEU   B 1 61  ? -43.564 -4.178  -22.331 1   30.27 ? 46  LEU   B CD1 1 
ATOM   3356 C  CD2 . LEU   B 1 61  ? -45.639 -4.016  -23.788 1   30.67 ? 46  LEU   B CD2 1 
ATOM   3357 N  N   . PRO   B 1 62  ? -45.642 -9.44   -22.971 1   31.69 ? 47  PRO   B N   1 
ATOM   3358 C  CA  . PRO   B 1 62  ? -45.454 -10.752 -23.597 1   32.26 ? 47  PRO   B CA  1 
ATOM   3359 C  C   . PRO   B 1 62  ? -46.637 -11.198 -24.476 1   33.47 ? 47  PRO   B C   1 
ATOM   3360 O  O   . PRO   B 1 62  ? -46.419 -11.601 -25.618 1   33.31 ? 47  PRO   B O   1 
ATOM   3361 C  CB  . PRO   B 1 62  ? -45.259 -11.69  -22.39  1   33.16 ? 47  PRO   B CB  1 
ATOM   3362 C  CG  . PRO   B 1 62  ? -44.608 -10.814 -21.346 1   33.73 ? 47  PRO   B CG  1 
ATOM   3363 C  CD  . PRO   B 1 62  ? -45.35  -9.499  -21.518 1   31.76 ? 47  PRO   B CD  1 
ATOM   3364 N  N   . ASP   B 1 63  ? -47.884 -11.05  -23.978 1   34.41 ? 48  ASP   B N   1 
ATOM   3365 C  CA  . ASP   B 1 63  ? -49.069 -11.471 -24.727 1   35.57 ? 48  ASP   B CA  1 
ATOM   3366 C  C   . ASP   B 1 63  ? -49.375 -10.539 -25.861 1   34.11 ? 48  ASP   B C   1 
ATOM   3367 O  O   . ASP   B 1 63  ? -49.723 -11.015 -26.928 1   35.31 ? 48  ASP   B O   1 
ATOM   3368 C  CB  . ASP   B 1 63  ? -50.3   -11.568 -23.811 1   40.84 ? 48  ASP   B CB  1 
ATOM   3369 C  CG  . ASP   B 1 63  ? -50.119 -12.554 -22.69  1   53.06 ? 48  ASP   B CG  1 
ATOM   3370 O  OD1 . ASP   B 1 63  ? -49.478 -13.608 -22.928 1   55.83 ? 48  ASP   B OD1 1 
ATOM   3371 O  OD2 . ASP   B 1 63  ? -50.621 -12.276 -21.562 1   58.03 ? 48  ASP   B OD2 1 
ATOM   3372 N  N   . LEU   B 1 64  ? -49.325 -9.222  -25.632 1   32.23 ? 49  LEU   B N   1 
ATOM   3373 C  CA  . LEU   B 1 64  ? -49.672 -8.258  -26.658 1   31.31 ? 49  LEU   B CA  1 
ATOM   3374 C  C   . LEU   B 1 64  ? -48.674 -8.264  -27.823 1   30.99 ? 49  LEU   B C   1 
ATOM   3375 O  O   . LEU   B 1 64  ? -49.068 -8.07   -28.993 1   30.14 ? 49  LEU   B O   1 
ATOM   3376 C  CB  . LEU   B 1 64  ? -49.812 -6.858  -26.069 1   31.38 ? 49  LEU   B CB  1 
ATOM   3377 C  CG  . LEU   B 1 64  ? -50.959 -6.656  -25.073 1   32.2  ? 49  LEU   B CG  1 
ATOM   3378 C  CD1 . LEU   B 1 64  ? -50.87  -5.289  -24.431 1   31.81 ? 49  LEU   B CD1 1 
ATOM   3379 C  CD2 . LEU   B 1 64  ? -52.357 -6.806  -25.797 1   32.82 ? 49  LEU   B CD2 1 
ATOM   3380 N  N   . ILE   B 1 65  ? -47.377 -8.46   -27.514 1   29.3  ? 50  ILE   B N   1 
ATOM   3381 C  CA  . ILE   B 1 65  ? -46.372 -8.513  -28.566 1   29.1  ? 50  ILE   B CA  1 
ATOM   3382 C  C   . ILE   B 1 65  ? -46.577 -9.785  -29.391 1   29.98 ? 50  ILE   B C   1 
ATOM   3383 O  O   . ILE   B 1 65  ? -46.704 -9.699  -30.613 1   31.17 ? 50  ILE   B O   1 
ATOM   3384 C  CB  . ILE   B 1 65  ? -44.906 -8.447  -28.022 1   28.33 ? 50  ILE   B CB  1 
ATOM   3385 C  CG1 . ILE   B 1 65  ? -44.612 -7.098  -27.373 1   28.58 ? 50  ILE   B CG1 1 
ATOM   3386 C  CG2 . ILE   B 1 65  ? -43.908 -8.743  -29.167 1   28.21 ? 50  ILE   B CG2 1 
ATOM   3387 C  CD1 . ILE   B 1 65  ? -43.283 -7.083  -26.622 1   28.92 ? 50  ILE   B CD1 1 
ATOM   3388 N  N   . GLU   B 1 66  ? -46.612 -10.955 -28.73  1   30.58 ? 51  GLU   B N   1 
ATOM   3389 C  CA  . GLU   B 1 66  ? -46.738 -12.249 -29.401 1   31.92 ? 51  GLU   B CA  1 
ATOM   3390 C  C   . GLU   B 1 66  ? -47.965 -12.303 -30.312 1   32.32 ? 51  GLU   B C   1 
ATOM   3391 O  O   . GLU   B 1 66  ? -47.883 -12.839 -31.411 1   32.58 ? 51  GLU   B O   1 
ATOM   3392 C  CB  . GLU   B 1 66  ? -46.796 -13.402 -28.382 1   35.29 ? 51  GLU   B CB  1 
ATOM   3393 C  CG  . GLU   B 1 66  ? -46.778 -14.793 -29.012 1   41.06 ? 51  GLU   B CG  1 
ATOM   3394 C  CD  . GLU   B 1 66  ? -48.13  -15.355 -29.442 1   50.15 ? 51  GLU   B CD  1 
ATOM   3395 O  OE1 . GLU   B 1 66  ? -49.166 -14.828 -28.975 1   51.67 ? 51  GLU   B OE1 1 
ATOM   3396 O  OE2 . GLU   B 1 66  ? -48.157 -16.301 -30.262 1   52.05 ? 51  GLU   B OE2 1 
ATOM   3397 N  N   . SER   B 1 67  ? -49.071 -11.716 -29.859 1   32.12 ? 52  SER   B N   1 
ATOM   3398 C  CA  . SER   B 1 67  ? -50.325 -11.731 -30.597 1   32.99 ? 52  SER   B CA  1 
ATOM   3399 C  C   . SER   B 1 67  ? -50.461 -10.656 -31.651 1   34.49 ? 52  SER   B C   1 
ATOM   3400 O  O   . SER   B 1 67  ? -51.437 -10.675 -32.381 1   35.06 ? 52  SER   B O   1 
ATOM   3401 C  CB  . SER   B 1 67  ? -51.512 -11.682 -29.639 1   34    ? 52  SER   B CB  1 
ATOM   3402 O  OG  . SER   B 1 67  ? -51.643 -10.39  -29.078 1   37.28 ? 52  SER   B OG  1 
ATOM   3403 N  N   . GLY   B 1 68  ? -49.514 -9.723  -31.737 1   34.69 ? 53  GLY   B N   1 
ATOM   3404 C  CA  . GLY   B 1 68  ? -49.576 -8.653  -32.717 1   35.31 ? 53  GLY   B CA  1 
ATOM   3405 C  C   . GLY   B 1 68  ? -50.578 -7.567  -32.384 1   36.83 ? 53  GLY   B C   1 
ATOM   3406 O  O   . GLY   B 1 68  ? -50.918 -6.751  -33.245 1   37.87 ? 53  GLY   B O   1 
ATOM   3407 N  N   . GLN   B 1 69  ? -51.008 -7.494  -31.125 1   36.89 ? 54  GLN   B N   1 
ATOM   3408 C  CA  . GLN   B 1 69  ? -51.966 -6.474  -30.697 1   38.05 ? 54  GLN   B CA  1 
ATOM   3409 C  C   . GLN   B 1 69  ? -51.319 -5.251  -30.065 1   37.97 ? 54  GLN   B C   1 
ATOM   3410 O  O   . GLN   B 1 69  ? -51.998 -4.252  -29.853 1   38.62 ? 54  GLN   B O   1 
ATOM   3411 C  CB  . GLN   B 1 69  ? -52.929 -7.079  -29.672 1   40.74 ? 54  GLN   B CB  1 
ATOM   3412 C  CG  . GLN   B 1 69  ? -53.809 -8.165  -30.241 1   46.62 ? 54  GLN   B CG  1 
ATOM   3413 C  CD  . GLN   B 1 69  ? -54.727 -8.712  -29.193 1   53.17 ? 54  GLN   B CD  1 
ATOM   3414 O  OE1 . GLN   B 1 69  ? -54.358 -9.605  -28.409 1   53.63 ? 54  GLN   B OE1 1 
ATOM   3415 N  NE2 . GLN   B 1 69  ? -55.958 -8.192  -29.167 1   56.09 ? 54  GLN   B NE2 1 
ATOM   3416 N  N   . LEU   B 1 70  ? -50.041 -5.337  -29.686 1   36.66 ? 55  LEU   B N   1 
ATOM   3417 C  CA  . LEU   B 1 70  ? -49.358 -4.255  -28.994 1   35.25 ? 55  LEU   B CA  1 
ATOM   3418 C  C   . LEU   B 1 70  ? -49.425 -2.918  -29.736 1   35.48 ? 55  LEU   B C   1 
ATOM   3419 O  O   . LEU   B 1 70  ? -49.845 -1.931  -29.143 1   35.55 ? 55  LEU   B O   1 
ATOM   3420 C  CB  . LEU   B 1 70  ? -47.889 -4.677  -28.684 1   34.28 ? 55  LEU   B CB  1 
ATOM   3421 C  CG  . LEU   B 1 70  ? -47.021 -3.745  -27.818 1   34.42 ? 55  LEU   B CG  1 
ATOM   3422 C  CD1 . LEU   B 1 70  ? -46.393 -2.641  -28.625 1   34.16 ? 55  LEU   B CD1 1 
ATOM   3423 C  CD2 . LEU   B 1 70  ? -47.774 -3.209  -26.628 1   34.73 ? 55  LEU   B CD2 1 
ATOM   3424 N  N   . ARG   B 1 71  ? -49.02  -2.878  -31.009 1   35.95 ? 56  ARG   B N   1 
ATOM   3425 C  CA  . ARG   B 1 71  ? -49.003 -1.631  -31.762 1   37.54 ? 56  ARG   B CA  1 
ATOM   3426 C  C   . ARG   B 1 71  ? -50.381 -0.969  -31.863 1   39.83 ? 56  ARG   B C   1 
ATOM   3427 O  O   . ARG   B 1 71  ? -50.494 0.238   -31.62  1   39.77 ? 56  ARG   B O   1 
ATOM   3428 C  CB  . ARG   B 1 71  ? -48.347 -1.833  -33.125 1   37.57 ? 56  ARG   B CB  1 
ATOM   3429 C  CG  . ARG   B 1 71  ? -46.841 -2.045  -32.935 1   38.36 ? 56  ARG   B CG  1 
ATOM   3430 C  CD  . ARG   B 1 71  ? -46.149 -2.68   -34.12  1   38.94 ? 56  ARG   B CD  1 
ATOM   3431 N  NE  . ARG   B 1 71  ? -44.697 -2.506  -34.045 1   38.68 ? 56  ARG   B NE  1 
ATOM   3432 C  CZ  . ARG   B 1 71  ? -43.836 -2.959  -34.955 1   38.41 ? 56  ARG   B CZ  1 
ATOM   3433 N  NH1 . ARG   B 1 71  ? -44.272 -3.624  -36.023 1   34.68 ? 56  ARG   B NH1 1 
ATOM   3434 N  NH2 . ARG   B 1 71  ? -42.536 -2.744  -34.809 1   37.72 ? 56  ARG   B NH2 1 
ATOM   3435 N  N   . GLU   B 1 72  ? -51.423 -1.778  -32.112 1   41.29 ? 57  GLU   B N   1 
ATOM   3436 C  CA  . GLU   B 1 72  ? -52.796 -1.304  -32.2   1   42.86 ? 57  GLU   B CA  1 
ATOM   3437 C  C   . GLU   B 1 72  ? -53.261 -0.753  -30.859 1   42.12 ? 57  GLU   B C   1 
ATOM   3438 O  O   . GLU   B 1 72  ? -53.826 0.33    -30.837 1   42.57 ? 57  GLU   B O   1 
ATOM   3439 C  CB  . GLU   B 1 72  ? -53.729 -2.426  -32.682 1   48.18 ? 57  GLU   B CB  1 
ATOM   3440 C  CG  . GLU   B 1 72  ? -55.158 -1.953  -32.888 1   59.15 ? 57  GLU   B CG  1 
ATOM   3441 C  CD  . GLU   B 1 72  ? -56.113 -3.076  -33.232 1   72.99 ? 57  GLU   B CD  1 
ATOM   3442 O  OE1 . GLU   B 1 72  ? -56.982 -3.406  -32.39  1   77.03 ? 57  GLU   B OE1 1 
ATOM   3443 O  OE2 . GLU   B 1 72  ? -55.981 -3.636  -34.345 1   76.41 ? 57  GLU   B OE2 1 
ATOM   3444 N  N   . ARG   B 1 73  ? -52.978 -1.444  -29.743 1   41.41 ? 58  ARG   B N   1 
ATOM   3445 C  CA  . ARG   B 1 73  ? -53.361 -0.964  -28.408 1   41.54 ? 58  ARG   B CA  1 
ATOM   3446 C  C   . ARG   B 1 73  ? -52.649 0.35    -28.074 1   41.1  ? 58  ARG   B C   1 
ATOM   3447 O  O   . ARG   B 1 73  ? -53.232 1.213   -27.418 1   41.09 ? 58  ARG   B O   1 
ATOM   3448 C  CB  . ARG   B 1 73  ? -53.04  -1.994  -27.313 1   43.62 ? 58  ARG   B CB  1 
ATOM   3449 C  CG  . ARG   B 1 73  ? -53.747 -3.325  -27.443 1   48.14 ? 58  ARG   B CG  1 
ATOM   3450 C  CD  . ARG   B 1 73  ? -55.221 -3.296  -27.095 1   53.16 ? 58  ARG   B CD  1 
ATOM   3451 N  NE  . ARG   B 1 73  ? -55.745 -4.665  -27.125 1   57.43 ? 58  ARG   B NE  1 
ATOM   3452 C  CZ  . ARG   B 1 73  ? -55.801 -5.474  -26.07  1   60.57 ? 58  ARG   B CZ  1 
ATOM   3453 N  NH1 . ARG   B 1 73  ? -55.428 -5.04   -24.872 1   60.52 ? 58  ARG   B NH1 1 
ATOM   3454 N  NH2 . ARG   B 1 73  ? -56.259 -6.713  -26.199 1   60.75 ? 58  ARG   B NH2 1 
ATOM   3455 N  N   . VAL   B 1 74  ? -51.393 0.508   -28.523 1   40.31 ? 59  VAL   B N   1 
ATOM   3456 C  CA  . VAL   B 1 74  ? -50.667 1.748   -28.275 1   40.45 ? 59  VAL   B CA  1 
ATOM   3457 C  C   . VAL   B 1 74  ? -51.289 2.884   -29.111 1   40.97 ? 59  VAL   B C   1 
ATOM   3458 O  O   . VAL   B 1 74  ? -51.487 3.995   -28.613 1   40.44 ? 59  VAL   B O   1 
ATOM   3459 C  CB  . VAL   B 1 74  ? -49.149 1.57    -28.539 1   40.06 ? 59  VAL   B CB  1 
ATOM   3460 C  CG1 . VAL   B 1 74  ? -48.454 2.914   -28.61  1   40.49 ? 59  VAL   B CG1 1 
ATOM   3461 C  CG2 . VAL   B 1 74  ? -48.518 0.681   -27.471 1   39.17 ? 59  VAL   B CG2 1 
ATOM   3462 N  N   . GLU   B 1 75  ? -51.617 2.588   -30.377 1   41.8  ? 60  GLU   B N   1 
ATOM   3463 C  CA  . GLU   B 1 75  ? -52.232 3.554   -31.292 1   43.07 ? 60  GLU   B CA  1 
ATOM   3464 C  C   . GLU   B 1 75  ? -53.645 3.985   -30.844 1   44.06 ? 60  GLU   B C   1 
ATOM   3465 O  O   . GLU   B 1 75  ? -54.076 5.083   -31.189 1   44.33 ? 60  GLU   B O   1 
ATOM   3466 C  CB  . GLU   B 1 75  ? -52.224 3.027   -32.736 1   44.97 ? 60  GLU   B CB  1 
ATOM   3467 C  CG  . GLU   B 1 75  ? -50.834 2.991   -33.353 1   49.32 ? 60  GLU   B CG  1 
ATOM   3468 C  CD  . GLU   B 1 75  ? -50.623 1.951   -34.44  1   55.53 ? 60  GLU   B CD  1 
ATOM   3469 O  OE1 . GLU   B 1 75  ? -51.621 1.332   -34.869 1   56.15 ? 60  GLU   B OE1 1 
ATOM   3470 O  OE2 . GLU   B 1 75  ? -49.461 1.75    -34.865 1   57.72 ? 60  GLU   B OE2 1 
ATOM   3471 N  N   . LYS   B 1 76  ? -54.334 3.15    -30.047 1   44.61 ? 61  LYS   B N   1 
ATOM   3472 C  CA  . LYS   B 1 76  ? -55.666 3.472   -29.532 1   45.83 ? 61  LYS   B CA  1 
ATOM   3473 C  C   . LYS   B 1 76  ? -55.641 4.373   -28.299 1   46.79 ? 61  LYS   B C   1 
ATOM   3474 O  O   . LYS   B 1 76  ? -56.665 4.974   -27.972 1   47.16 ? 61  LYS   B O   1 
ATOM   3475 C  CB  . LYS   B 1 76  ? -56.458 2.189   -29.205 1   47.85 ? 61  LYS   B CB  1 
ATOM   3476 C  CG  . LYS   B 1 76  ? -56.796 1.332   -30.427 1   52.3  ? 61  LYS   B CG  1 
ATOM   3477 C  CD  . LYS   B 1 76  ? -57.862 1.942   -31.325 1   56.98 ? 61  LYS   B CD  1 
ATOM   3478 C  CE  . LYS   B 1 76  ? -58.122 1.084   -32.537 1   61.39 ? 61  LYS   B CE  1 
ATOM   3479 N  NZ  . LYS   B 1 76  ? -58.221 -0.359  -32.175 1   64.34 ? 61  LYS   B NZ  1 
ATOM   3480 N  N   . LEU   B 1 77  ? -54.506 4.45    -27.585 1   46.5  ? 62  LEU   B N   1 
ATOM   3481 C  CA  . LEU   B 1 77  ? -54.415 5.257   -26.364 1   46.2  ? 62  LEU   B CA  1 
ATOM   3482 C  C   . LEU   B 1 77  ? -54.825 6.694   -26.535 1   46.36 ? 62  LEU   B C   1 
ATOM   3483 O  O   . LEU   B 1 77  ? -54.488 7.288   -27.538 1   45.86 ? 62  LEU   B O   1 
ATOM   3484 C  CB  . LEU   B 1 77  ? -52.961 5.275   -25.857 1   45.6  ? 62  LEU   B CB  1 
ATOM   3485 C  CG  . LEU   B 1 77  ? -52.495 4.059   -25.104 1   46.03 ? 62  LEU   B CG  1 
ATOM   3486 C  CD1 . LEU   B 1 77  ? -51.023 4.191   -24.758 1   46.54 ? 62  LEU   B CD1 1 
ATOM   3487 C  CD2 . LEU   B 1 77  ? -53.29  3.88    -23.834 1   45.97 ? 62  LEU   B CD2 1 
ATOM   3488 N  N   . ASN   B 1 78  ? -55.494 7.27    -25.53  1   47.36 ? 63  ASN   B N   1 
ATOM   3489 C  CA  . ASN   B 1 78  ? -55.769 8.709   -25.521 1   49.16 ? 63  ASN   B CA  1 
ATOM   3490 C  C   . ASN   B 1 78  ? -54.548 9.395   -24.888 1   50.26 ? 63  ASN   B C   1 
ATOM   3491 O  O   . ASN   B 1 78  ? -53.828 8.751   -24.122 1   50.49 ? 63  ASN   B O   1 
ATOM   3492 C  CB  . ASN   B 1 78  ? -57.029 9.023   -24.714 1   50.85 ? 63  ASN   B CB  1 
ATOM   3493 C  CG  . ASN   B 1 78  ? -58.258 8.51    -25.414 1   54.56 ? 63  ASN   B CG  1 
ATOM   3494 O  OD1 . ASN   B 1 78  ? -58.441 8.737   -26.616 1   55.46 ? 63  ASN   B OD1 1 
ATOM   3495 N  ND2 . ASN   B 1 78  ? -59.095 7.767   -24.695 1   55.68 ? 63  ASN   B ND2 1 
ATOM   3496 N  N   . MET   B 1 79  ? -54.293 10.677  -25.215 1   50.77 ? 64  MET   B N   1 
ATOM   3497 C  CA  . MET   B 1 79  ? -53.14  11.376  -24.651 1   51.72 ? 64  MET   B CA  1 
ATOM   3498 C  C   . MET   B 1 79  ? -53.415 11.673  -23.195 1   51.97 ? 64  MET   B C   1 
ATOM   3499 O  O   . MET   B 1 79  ? -54.353 12.405  -22.887 1   52.39 ? 64  MET   B O   1 
ATOM   3500 C  CB  . MET   B 1 79  ? -52.795 12.666  -25.419 1   52.59 ? 64  MET   B CB  1 
ATOM   3501 C  CG  . MET   B 1 79  ? -51.383 13.166  -25.148 1   54.68 ? 64  MET   B CG  1 
ATOM   3502 S  SD  . MET   B 1 79  ? -50.986 14.709  -26.019 1   58.04 ? 64  MET   B SD  1 
ATOM   3503 C  CE  . MET   B 1 79  ? -50.824 14.143  -27.695 1   52.99 ? 64  MET   B CE  1 
ATOM   3504 N  N   . LEU   B 1 80  ? -52.637 11.072  -22.296 1   51.21 ? 65  LEU   B N   1 
ATOM   3505 C  CA  . LEU   B 1 80  ? -52.822 11.294  -20.871 1   51.32 ? 65  LEU   B CA  1 
ATOM   3506 C  C   . LEU   B 1 80  ? -51.828 12.306  -20.347 1   50.98 ? 65  LEU   B C   1 
ATOM   3507 O  O   . LEU   B 1 80  ? -50.641 12.22   -20.648 1   50.95 ? 65  LEU   B O   1 
ATOM   3508 C  CB  . LEU   B 1 80  ? -52.72  9.981   -20.094 1   51.94 ? 65  LEU   B CB  1 
ATOM   3509 C  CG  . LEU   B 1 80  ? -53.775 8.934   -20.428 1   54.42 ? 65  LEU   B CG  1 
ATOM   3510 C  CD1 . LEU   B 1 80  ? -53.588 7.693   -19.555 1   54.86 ? 65  LEU   B CD1 1 
ATOM   3511 C  CD2 . LEU   B 1 80  ? -55.217 9.507   -20.263 1   55.17 ? 65  LEU   B CD2 1 
ATOM   3512 N  N   . SER   B 1 81  ? -52.315 13.29   -19.596 1   50.48 ? 66  SER   B N   1 
ATOM   3513 C  CA  . SER   B 1 81  ? -51.47  14.329  -19.025 1   50.71 ? 66  SER   B CA  1 
ATOM   3514 C  C   . SER   B 1 81  ? -50.562 13.736  -17.948 1   50.6  ? 66  SER   B C   1 
ATOM   3515 O  O   . SER   B 1 81  ? -50.993 12.863  -17.198 1   50.93 ? 66  SER   B O   1 
ATOM   3516 C  CB  . SER   B 1 81  ? -52.339 15.426  -18.413 1   51.7  ? 66  SER   B CB  1 
ATOM   3517 O  OG  . SER   B 1 81  ? -51.6   16.313  -17.59  1   53.59 ? 66  SER   B OG  1 
ATOM   3518 N  N   . ILE   B 1 82  ? -49.336 14.252  -17.823 1   50.26 ? 67  ILE   B N   1 
ATOM   3519 C  CA  . ILE   B 1 82  ? -48.427 13.778  -16.773 1   50.55 ? 67  ILE   B CA  1 
ATOM   3520 C  C   . ILE   B 1 82  ? -48.624 14.495  -15.423 1   51.1  ? 67  ILE   B C   1 
ATOM   3521 O  O   . ILE   B 1 82  ? -47.96  14.125  -14.46  1   51.07 ? 67  ILE   B O   1 
ATOM   3522 C  CB  . ILE   B 1 82  ? -46.946 13.833  -17.214 1   50.38 ? 67  ILE   B CB  1 
ATOM   3523 C  CG1 . ILE   B 1 82  ? -46.495 15.286  -17.449 1   50.96 ? 67  ILE   B CG1 1 
ATOM   3524 C  CG2 . ILE   B 1 82  ? -46.714 12.963  -18.436 1   50.42 ? 67  ILE   B CG2 1 
ATOM   3525 C  CD1 . ILE   B 1 82  ? -45.011 15.497  -17.374 1   51.99 ? 67  ILE   B CD1 1 
ATOM   3526 N  N   . ASP   B 1 83  ? -49.549 15.479  -15.332 1   51.38 ? 68  ASP   B N   1 
ATOM   3527 C  CA  . ASP   B 1 83  ? -49.774 16.255  -14.107 1   52.38 ? 68  ASP   B CA  1 
ATOM   3528 C  C   . ASP   B 1 83  ? -50.223 15.434  -12.896 1   52.91 ? 68  ASP   B C   1 
ATOM   3529 O  O   . ASP   B 1 83  ? -50.011 15.855  -11.755 1   53.78 ? 68  ASP   B O   1 
ATOM   3530 C  CB  . ASP   B 1 83  ? -50.747 17.407  -14.365 1   55.17 ? 68  ASP   B CB  1 
ATOM   3531 C  CG  . ASP   B 1 83  ? -50.295 18.353  -15.463 1   62.73 ? 68  ASP   B CG  1 
ATOM   3532 O  OD1 . ASP   B 1 83  ? -49.09  18.332  -15.81  1   63.48 ? 68  ASP   B OD1 1 
ATOM   3533 O  OD2 . ASP   B 1 83  ? -51.153 19.104  -15.993 1   66.63 ? 68  ASP   B OD2 1 
ATOM   3534 N  N   . HIS   B 1 84  ? -50.779 14.242  -13.127 1   52.17 ? 69  HIS   B N   1 
ATOM   3535 C  CA  . HIS   B 1 84  ? -51.227 13.38   -12.035 1   52.24 ? 69  HIS   B CA  1 
ATOM   3536 C  C   . HIS   B 1 84  ? -50.121 12.476  -11.459 1   51.61 ? 69  HIS   B C   1 
ATOM   3537 O  O   . HIS   B 1 84  ? -50.401 11.677  -10.567 1   51.81 ? 69  HIS   B O   1 
ATOM   3538 C  CB  . HIS   B 1 84  ? -52.463 12.574  -12.455 1   54.06 ? 69  HIS   B CB  1 
ATOM   3539 C  CG  . HIS   B 1 84  ? -53.529 13.458  -13.027 1   57.89 ? 69  HIS   B CG  1 
ATOM   3540 N  ND1 . HIS   B 1 84  ? -54.38  14.182  -12.208 1   60.19 ? 69  HIS   B ND1 1 
ATOM   3541 C  CD2 . HIS   B 1 84  ? -53.76  13.807  -14.316 1   59.39 ? 69  HIS   B CD2 1 
ATOM   3542 C  CE1 . HIS   B 1 84  ? -55.136 14.9    -13.024 1   60.91 ? 69  HIS   B CE1 1 
ATOM   3543 N  NE2 . HIS   B 1 84  ? -54.794 14.713  -14.302 1   60.74 ? 69  HIS   B NE2 1 
ATOM   3544 N  N   . LEU   B 1 85  ? -48.86  12.621  -11.936 1   50.61 ? 70  LEU   B N   1 
ATOM   3545 C  CA  . LEU   B 1 85  ? -47.707 11.896  -11.387 1   50.19 ? 70  LEU   B CA  1 
ATOM   3546 C  C   . LEU   B 1 85  ? -47.024 12.94   -10.475 1   50.26 ? 70  LEU   B C   1 
ATOM   3547 O  O   . LEU   B 1 85  ? -46.245 13.773  -10.938 1   50.27 ? 70  LEU   B O   1 
ATOM   3548 C  CB  . LEU   B 1 85  ? -46.786 11.447  -12.533 1   49.63 ? 70  LEU   B CB  1 
ATOM   3549 C  CG  . LEU   B 1 85  ? -47.431 10.518  -13.551 1   49.66 ? 70  LEU   B CG  1 
ATOM   3550 C  CD1 . LEU   B 1 85  ? -46.604 10.438  -14.813 1   49.5  ? 70  LEU   B CD1 1 
ATOM   3551 C  CD2 . LEU   B 1 85  ? -47.666 9.139   -12.957 1   49.81 ? 70  LEU   B CD2 1 
ATOM   3552 N  N   . THR   B 1 86  ? -47.409 12.946  -9.197  1   50.18 ? 71  THR   B N   1 
ATOM   3553 C  CA  . THR   B 1 86  ? -47.072 13.996  -8.236  1   50.78 ? 71  THR   B CA  1 
ATOM   3554 C  C   . THR   B 1 86  ? -45.827 13.799  -7.37   1   50.82 ? 71  THR   B C   1 
ATOM   3555 O  O   . THR   B 1 86  ? -45.446 14.725  -6.648  1   51.91 ? 71  THR   B O   1 
ATOM   3556 C  CB  . THR   B 1 86  ? -48.283 14.224  -7.33   1   52.08 ? 71  THR   B CB  1 
ATOM   3557 O  OG1 . THR   B 1 86  ? -48.646 12.976  -6.721  1   52.7  ? 71  THR   B OG1 1 
ATOM   3558 C  CG2 . THR   B 1 86  ? -49.466 14.78   -8.1    1   52.67 ? 71  THR   B CG2 1 
ATOM   3559 N  N   . ASP   B 1 87  ? -45.209 12.624  -7.413  1   49.43 ? 72  ASP   B N   1 
ATOM   3560 C  CA  . ASP   B 1 87  ? -43.994 12.38   -6.649  1   48.16 ? 72  ASP   B CA  1 
ATOM   3561 C  C   . ASP   B 1 87  ? -42.947 11.662  -7.509  1   46.5  ? 72  ASP   B C   1 
ATOM   3562 O  O   . ASP   B 1 87  ? -43.294 11.067  -8.541  1   46.38 ? 72  ASP   B O   1 
ATOM   3563 C  CB  . ASP   B 1 87  ? -44.295 11.648  -5.337  1   49.88 ? 72  ASP   B CB  1 
ATOM   3564 C  CG  . ASP   B 1 87  ? -44.938 10.295  -5.497  1   55.66 ? 72  ASP   B CG  1 
ATOM   3565 O  OD1 . ASP   B 1 87  ? -44.588 9.585   -6.454  1   56.68 ? 72  ASP   B OD1 1 
ATOM   3566 O  OD2 . ASP   B 1 87  ? -45.773 9.929   -4.637  1   58.33 ? 72  ASP   B OD2 1 
ATOM   3567 N  N   . HIS   B 1 88  ? -41.678 11.708  -7.081  1   44.29 ? 73  HIS   B N   1 
ATOM   3568 C  CA  . HIS   B 1 88  ? -40.567 11.089  -7.804  1   42.91 ? 73  HIS   B CA  1 
ATOM   3569 C  C   . HIS   B 1 88  ? -40.771 9.597   -8.144  1   41.21 ? 73  HIS   B C   1 
ATOM   3570 O  O   . HIS   B 1 88  ? -40.488 9.201   -9.27   1   41.22 ? 73  HIS   B O   1 
ATOM   3571 C  CB  . HIS   B 1 88  ? -39.254 11.288  -7.031  1   42.81 ? 73  HIS   B CB  1 
ATOM   3572 C  CG  . HIS   B 1 88  ? -38.059 10.739  -7.735  1   43.43 ? 73  HIS   B CG  1 
ATOM   3573 N  ND1 . HIS   B 1 88  ? -37.541 11.359  -8.862  1   44.96 ? 73  HIS   B ND1 1 
ATOM   3574 C  CD2 . HIS   B 1 88  ? -37.318 9.646   -7.454  1   44.24 ? 73  HIS   B CD2 1 
ATOM   3575 C  CE1 . HIS   B 1 88  ? -36.497 10.634  -9.219  1   45.32 ? 73  HIS   B CE1 1 
ATOM   3576 N  NE2 . HIS   B 1 88  ? -36.325 9.591   -8.403  1   45.45 ? 73  HIS   B NE2 1 
ATOM   3577 N  N   . LYS   B 1 89  ? -41.236 8.78    -7.19   1   39.61 ? 74  LYS   B N   1 
ATOM   3578 C  CA  . LYS   B 1 89  ? -41.421 7.357   -7.426  1   38.98 ? 74  LYS   B CA  1 
ATOM   3579 C  C   . LYS   B 1 89  ? -42.488 7.041   -8.484  1   39.06 ? 74  LYS   B C   1 
ATOM   3580 O  O   . LYS   B 1 89  ? -42.325 6.086   -9.257  1   38.5  ? 74  LYS   B O   1 
ATOM   3581 C  CB  . LYS   B 1 89  ? -41.691 6.601   -6.126  1   39.65 ? 74  LYS   B CB  1 
ATOM   3582 C  CG  . LYS   B 1 89  ? -40.469 6.545   -5.226  1   41.72 ? 74  LYS   B CG  1 
ATOM   3583 C  CD  . LYS   B 1 89  ? -40.589 5.449   -4.214  1   43.76 ? 74  LYS   B CD  1 
ATOM   3584 C  CE  . LYS   B 1 89  ? -39.453 5.532   -3.228  1   45.49 ? 74  LYS   B CE  1 
ATOM   3585 N  NZ  . LYS   B 1 89  ? -39.551 4.448   -2.219  1   46.82 ? 74  LYS   B NZ  1 
ATOM   3586 N  N   . SER   B 1 90  ? -43.567 7.837   -8.525  1   38.78 ? 75  SER   B N   1 
ATOM   3587 C  CA  . SER   B 1 90  ? -44.603 7.625   -9.529  1   38.66 ? 75  SER   B CA  1 
ATOM   3588 C  C   . SER   B 1 90  ? -44.083 8.083   -10.896 1   37.22 ? 75  SER   B C   1 
ATOM   3589 O  O   . SER   B 1 90  ? -44.405 7.453   -11.896 1   37.68 ? 75  SER   B O   1 
ATOM   3590 C  CB  . SER   B 1 90  ? -45.91  8.328   -9.151  1   41.13 ? 75  SER   B CB  1 
ATOM   3591 O  OG  . SER   B 1 90  ? -45.789 9.733   -9.296  1   44.65 ? 75  SER   B OG  1 
ATOM   3592 N  N   . GLN   B 1 91  ? -43.245 9.137   -10.948 1   35.41 ? 76  GLN   B N   1 
ATOM   3593 C  CA  . GLN   B 1 91  ? -42.669 9.599   -12.209 1   34.62 ? 76  GLN   B CA  1 
ATOM   3594 C  C   . GLN   B 1 91  ? -41.647 8.568   -12.746 1   33.35 ? 76  GLN   B C   1 
ATOM   3595 O  O   . GLN   B 1 91  ? -41.595 8.348   -13.953 1   33.21 ? 76  GLN   B O   1 
ATOM   3596 C  CB  . GLN   B 1 91  ? -42.012 10.969  -12.032 1   36.96 ? 76  GLN   B CB  1 
ATOM   3597 C  CG  . GLN   B 1 91  ? -43.016 12.095  -11.768 1   42.81 ? 76  GLN   B CG  1 
ATOM   3598 C  CD  . GLN   B 1 91  ? -42.397 13.33   -11.158 1   49.66 ? 76  GLN   B CD  1 
ATOM   3599 O  OE1 . GLN   B 1 91  ? -41.18  13.433  -10.989 1   52.64 ? 76  GLN   B OE1 1 
ATOM   3600 N  NE2 . GLN   B 1 91  ? -43.226 14.294  -10.78  1   50.2  ? 76  GLN   B NE2 1 
ATOM   3601 N  N   . ARG   B 1 92  ? -40.871 7.921   -11.843 1   31.89 ? 77  ARG   B N   1 
ATOM   3602 C  CA  . ARG   B 1 92  ? -39.897 6.893   -12.219 1   30.8  ? 77  ARG   B CA  1 
ATOM   3603 C  C   . ARG   B 1 92  ? -40.63  5.629   -12.714 1   30.75 ? 77  ARG   B C   1 
ATOM   3604 O  O   . ARG   B 1 92  ? -40.206 5.024   -13.692 1   30.48 ? 77  ARG   B O   1 
ATOM   3605 C  CB  . ARG   B 1 92  ? -38.972 6.55    -11.037 1   30.09 ? 77  ARG   B CB  1 
ATOM   3606 C  CG  . ARG   B 1 92  ? -37.897 7.617   -10.755 1   28.57 ? 77  ARG   B CG  1 
ATOM   3607 C  CD  . ARG   B 1 92  ? -36.788 7.705   -11.82  1   27.35 ? 77  ARG   B CD  1 
ATOM   3608 N  NE  . ARG   B 1 92  ? -35.979 6.482   -11.843 1   26.9  ? 77  ARG   B NE  1 
ATOM   3609 C  CZ  . ARG   B 1 92  ? -34.97  6.233   -11.008 1   28.32 ? 77  ARG   B CZ  1 
ATOM   3610 N  NH1 . ARG   B 1 92  ? -34.598 7.141   -10.115 1   29.94 ? 77  ARG   B NH1 1 
ATOM   3611 N  NH2 . ARG   B 1 92  ? -34.297 5.095   -11.092 1   26.65 ? 77  ARG   B NH2 1 
ATOM   3612 N  N   . LEU   B 1 93  ? -41.731 5.238   -12.048 1   30.54 ? 78  LEU   B N   1 
ATOM   3613 C  CA  . LEU   B 1 93  ? -42.521 4.08    -12.488 1   30.42 ? 78  LEU   B CA  1 
ATOM   3614 C  C   . LEU   B 1 93  ? -43.139 4.378   -13.858 1   29.97 ? 78  LEU   B C   1 
ATOM   3615 O  O   . LEU   B 1 93  ? -43.119 3.514   -14.736 1   30.18 ? 78  LEU   B O   1 
ATOM   3616 C  CB  . LEU   B 1 93  ? -43.638 3.732   -11.463 1   31.06 ? 78  LEU   B CB  1 
ATOM   3617 C  CG  . LEU   B 1 93  ? -44.645 2.646   -11.91  1   33.37 ? 78  LEU   B CG  1 
ATOM   3618 C  CD1 . LEU   B 1 93  ? -43.941 1.332   -12.262 1   33.67 ? 78  LEU   B CD1 1 
ATOM   3619 C  CD2 . LEU   B 1 93  ? -45.686 2.39    -10.825 1   34.4  ? 78  LEU   B CD2 1 
ATOM   3620 N  N   . ALA   B 1 94  ? -43.639 5.603   -14.062 1   29.36 ? 79  ALA   B N   1 
ATOM   3621 C  CA  . ALA   B 1 94  ? -44.245 5.962   -15.339 1   29.18 ? 79  ALA   B CA  1 
ATOM   3622 C  C   . ALA   B 1 94  ? -43.198 5.952   -16.46  1   29.06 ? 79  ALA   B C   1 
ATOM   3623 O  O   . ALA   B 1 94  ? -43.519 5.593   -17.587 1   29.3  ? 79  ALA   B O   1 
ATOM   3624 C  CB  . ALA   B 1 94  ? -44.902 7.315   -15.253 1   29.04 ? 79  ALA   B CB  1 
ATOM   3625 N  N   . ARG   B 1 95  ? -41.956 6.351   -16.161 1   28.04 ? 80  ARG   B N   1 
ATOM   3626 C  CA  . ARG   B 1 95  ? -40.878 6.312   -17.156 1   27.53 ? 80  ARG   B CA  1 
ATOM   3627 C  C   . ARG   B 1 95  ? -40.606 4.853   -17.541 1   26.03 ? 80  ARG   B C   1 
ATOM   3628 O  O   . ARG   B 1 95  ? -40.317 4.575   -18.696 1   26.79 ? 80  ARG   B O   1 
ATOM   3629 C  CB  . ARG   B 1 95  ? -39.596 6.902   -16.553 1   28.38 ? 80  ARG   B CB  1 
ATOM   3630 C  CG  . ARG   B 1 95  ? -39.227 8.257   -17.123 1   29.62 ? 80  ARG   B CG  1 
ATOM   3631 C  CD  . ARG   B 1 95  ? -37.773 8.593   -16.82  1   31.2  ? 80  ARG   B CD  1 
ATOM   3632 N  NE  . ARG   B 1 95  ? -36.81  7.776   -17.561 1   29.68 ? 80  ARG   B NE  1 
ATOM   3633 C  CZ  . ARG   B 1 95  ? -36.369 8.063   -18.784 1   28.13 ? 80  ARG   B CZ  1 
ATOM   3634 N  NH1 . ARG   B 1 95  ? -36.875 9.095   -19.459 1   25.69 ? 80  ARG   B NH1 1 
ATOM   3635 N  NH2 . ARG   B 1 95  ? -35.448 7.3     -19.358 1   25.68 ? 80  ARG   B NH2 1 
ATOM   3636 N  N   . LEU   B 1 96  ? -40.629 3.944   -16.567 1   24.49 ? 81  LEU   B N   1 
ATOM   3637 C  CA  . LEU   B 1 96  ? -40.358 2.534   -16.796 1   25.06 ? 81  LEU   B CA  1 
ATOM   3638 C  C   . LEU   B 1 96  ? -41.495 1.935   -17.659 1   27.06 ? 81  LEU   B C   1 
ATOM   3639 O  O   . LEU   B 1 96  ? -41.24  1.18    -18.603 1   27.37 ? 81  LEU   B O   1 
ATOM   3640 C  CB  . LEU   B 1 96  ? -40.247 1.823   -15.435 1   24.29 ? 81  LEU   B CB  1 
ATOM   3641 C  CG  . LEU   B 1 96  ? -40.173 0.312   -15.427 1   25.42 ? 81  LEU   B CG  1 
ATOM   3642 C  CD1 . LEU   B 1 96  ? -38.984 -0.223  -16.285 1   24.38 ? 81  LEU   B CD1 1 
ATOM   3643 C  CD2 . LEU   B 1 96  ? -40.067 -0.201  -14.009 1   26.2  ? 81  LEU   B CD2 1 
ATOM   3644 N  N   . VAL   B 1 97  ? -42.749 2.294   -17.337 1   27.44 ? 82  VAL   B N   1 
ATOM   3645 C  CA  . VAL   B 1 97  ? -43.936 1.863   -18.089 1   27.33 ? 82  VAL   B CA  1 
ATOM   3646 C  C   . VAL   B 1 97  ? -43.85  2.365   -19.535 1   27.05 ? 82  VAL   B C   1 
ATOM   3647 O  O   . VAL   B 1 97  ? -43.922 1.55    -20.446 1   28.13 ? 82  VAL   B O   1 
ATOM   3648 C  CB  . VAL   B 1 97  ? -45.234 2.38    -17.38  1   27.48 ? 82  VAL   B CB  1 
ATOM   3649 C  CG1 . VAL   B 1 97  ? -46.459 2.311   -18.325 1   27.4  ? 82  VAL   B CG1 1 
ATOM   3650 C  CG2 . VAL   B 1 97  ? -45.485 1.611   -16.088 1   27.6  ? 82  VAL   B CG2 1 
ATOM   3651 N  N   . LEU   B 1 98  ? -43.69  3.687   -19.747 1   26.47 ? 83  LEU   B N   1 
ATOM   3652 C  CA  . LEU   B 1 98  ? -43.633 4.277   -21.078 1   27.17 ? 83  LEU   B CA  1 
ATOM   3653 C  C   . LEU   B 1 98  ? -42.433 3.804   -21.882 1   27.18 ? 83  LEU   B C   1 
ATOM   3654 O  O   . LEU   B 1 98  ? -42.53  3.623   -23.107 1   27.86 ? 83  LEU   B O   1 
ATOM   3655 C  CB  . LEU   B 1 98  ? -43.667 5.808   -21.007 1   28.29 ? 83  LEU   B CB  1 
ATOM   3656 C  CG  . LEU   B 1 98  ? -44.959 6.404   -20.447 1   30.95 ? 83  LEU   B CG  1 
ATOM   3657 C  CD1 . LEU   B 1 98  ? -44.81  7.895   -20.208 1   31.6  ? 83  LEU   B CD1 1 
ATOM   3658 C  CD2 . LEU   B 1 98  ? -46.141 6.162   -21.401 1   32.69 ? 83  LEU   B CD2 1 
ATOM   3659 N  N   . GLY   B 1 99  ? -41.308 3.613   -21.194 1   25.95 ? 84  GLY   B N   1 
ATOM   3660 C  CA  . GLY   B 1 99  ? -40.094 3.143   -21.841 1   25.6  ? 84  GLY   B CA  1 
ATOM   3661 C  C   . GLY   B 1 99  ? -40.221 1.726   -22.35  1   25.06 ? 84  GLY   B C   1 
ATOM   3662 O  O   . GLY   B 1 99  ? -39.751 1.443   -23.445 1   26.09 ? 84  GLY   B O   1 
ATOM   3663 N  N   . CYS   B 1 100 ? -40.795 0.814   -21.548 1   24.25 ? 85  CYS   B N   1 
ATOM   3664 C  CA  . CYS   B 1 100 ? -41.007 -0.576  -21.951 1   25.14 ? 85  CYS   B CA  1 
ATOM   3665 C  C   . CYS   B 1 100 ? -42.002 -0.644  -23.131 1   26.38 ? 85  CYS   B C   1 
ATOM   3666 O  O   . CYS   B 1 100 ? -41.812 -1.413  -24.076 1   26.61 ? 85  CYS   B O   1 
ATOM   3667 C  CB  . CYS   B 1 100 ? -41.485 -1.43   -20.781 1   25.25 ? 85  CYS   B CB  1 
ATOM   3668 S  SG  . CYS   B 1 100 ? -40.213 -1.763  -19.531 1   28.87 ? 85  CYS   B SG  1 
ATOM   3669 N  N   . ILE   B 1 101 ? -43.048 0.181   -23.083 1   26.25 ? 86  ILE   B N   1 
ATOM   3670 C  CA  . ILE   B 1 101 ? -44.039 0.232   -24.161 1   26.98 ? 86  ILE   B CA  1 
ATOM   3671 C  C   . ILE   B 1 101 ? -43.375 0.724   -25.439 1   26.85 ? 86  ILE   B C   1 
ATOM   3672 O  O   . ILE   B 1 101 ? -43.618 0.167   -26.499 1   26.44 ? 86  ILE   B O   1 
ATOM   3673 C  CB  . ILE   B 1 101 ? -45.213 1.146   -23.738 1   28.47 ? 86  ILE   B CB  1 
ATOM   3674 C  CG1 . ILE   B 1 101 ? -46.019 0.5     -22.585 1   29.73 ? 86  ILE   B CG1 1 
ATOM   3675 C  CG2 . ILE   B 1 101 ? -46.126 1.474   -24.925 1   30.26 ? 86  ILE   B CG2 1 
ATOM   3676 C  CD1 . ILE   B 1 101 ? -47.136 1.493   -21.999 1   31.28 ? 86  ILE   B CD1 1 
ATOM   3677 N  N   . THR   B 1 102 ? -42.507 1.756   -25.335 1   26.34 ? 87  THR   B N   1 
ATOM   3678 C  CA  . THR   B 1 102 ? -41.802 2.297   -26.492 1   25.48 ? 87  THR   B CA  1 
ATOM   3679 C  C   . THR   B 1 102 ? -40.916 1.254   -27.155 1   25.55 ? 87  THR   B C   1 
ATOM   3680 O  O   . THR   B 1 102 ? -40.956 1.144   -28.375 1   25.37 ? 87  THR   B O   1 
ATOM   3681 C  CB  . THR   B 1 102 ? -41.045 3.576   -26.108 1   25.99 ? 87  THR   B CB  1 
ATOM   3682 O  OG1 . THR   B 1 102 ? -41.989 4.556   -25.677 1   26.83 ? 87  THR   B OG1 1 
ATOM   3683 C  CG2 . THR   B 1 102 ? -40.219 4.127   -27.243 1   25.96 ? 87  THR   B CG2 1 
ATOM   3684 N  N   . MET   B 1 103 ? -40.124 0.453   -26.358 1   25.15 ? 88  MET   B N   1 
ATOM   3685 C  CA  . MET   B 1 103 ? -39.265 -0.6    -26.929 1   24.7  ? 88  MET   B CA  1 
ATOM   3686 C  C   . MET   B 1 103 ? -40.112 -1.613  -27.677 1   24.57 ? 88  MET   B C   1 
ATOM   3687 O  O   . MET   B 1 103 ? -39.753 -2.015  -28.774 1   23.48 ? 88  MET   B O   1 
ATOM   3688 C  CB  . MET   B 1 103 ? -38.468 -1.356  -25.837 1   25.29 ? 88  MET   B CB  1 
ATOM   3689 C  CG  . MET   B 1 103 ? -37.455 -0.497  -25.077 1   29.63 ? 88  MET   B CG  1 
ATOM   3690 S  SD  . MET   B 1 103 ? -36.397 0.54    -26.165 1   38.18 ? 88  MET   B SD  1 
ATOM   3691 C  CE  . MET   B 1 103 ? -36.991 2.127   -25.541 1   37.55 ? 88  MET   B CE  1 
ATOM   3692 N  N   . ALA   B 1 104 ? -41.224 -2.056  -27.063 1   25.17 ? 89  ALA   B N   1 
ATOM   3693 C  CA  . ALA   B 1 104 ? -42.106 -3.04   -27.661 1   26.55 ? 89  ALA   B CA  1 
ATOM   3694 C  C   . ALA   B 1 104 ? -42.748 -2.465  -28.941 1   27.23 ? 89  ALA   B C   1 
ATOM   3695 O  O   . ALA   B 1 104 ? -42.856 -3.175  -29.927 1   27.87 ? 89  ALA   B O   1 
ATOM   3696 C  CB  . ALA   B 1 104 ? -43.183 -3.44   -26.662 1   26.66 ? 89  ALA   B CB  1 
ATOM   3697 N  N   . TYR   B 1 105 ? -43.127 -1.2    -28.936 1   27.31 ? 90  TYR   B N   1 
ATOM   3698 C  CA  . TYR   B 1 105 ? -43.745 -0.572  -30.098 1   29.03 ? 90  TYR   B CA  1 
ATOM   3699 C  C   . TYR   B 1 105 ? -42.747 -0.469  -31.264 1   28.85 ? 90  TYR   B C   1 
ATOM   3700 O  O   . TYR   B 1 105 ? -43.075 -0.84   -32.401 1   28.61 ? 90  TYR   B O   1 
ATOM   3701 C  CB  . TYR   B 1 105 ? -44.321 0.814   -29.741 1   30.39 ? 90  TYR   B CB  1 
ATOM   3702 C  CG  . TYR   B 1 105 ? -45.126 1.408   -30.877 1   32.57 ? 90  TYR   B CG  1 
ATOM   3703 C  CD1 . TYR   B 1 105 ? -46.448 1.041   -31.084 1   34.36 ? 90  TYR   B CD1 1 
ATOM   3704 C  CD2 . TYR   B 1 105 ? -44.54  2.252   -31.799 1   33.91 ? 90  TYR   B CD2 1 
ATOM   3705 C  CE1 . TYR   B 1 105 ? -47.176 1.538   -32.162 1   35.41 ? 90  TYR   B CE1 1 
ATOM   3706 C  CE2 . TYR   B 1 105 ? -45.244 2.728   -32.893 1   35.62 ? 90  TYR   B CE2 1 
ATOM   3707 C  CZ  . TYR   B 1 105 ? -46.564 2.369   -33.075 1   36.73 ? 90  TYR   B CZ  1 
ATOM   3708 O  OH  . TYR   B 1 105 ? -47.251 2.909   -34.139 1   39.07 ? 90  TYR   B OH  1 
ATOM   3709 N  N   . VAL   B 1 106 ? -41.538 0.041   -30.986 1   27.87 ? 91  VAL   B N   1 
ATOM   3710 C  CA  . VAL   B 1 106 ? -40.548 0.221   -32.042 1   27.94 ? 91  VAL   B CA  1 
ATOM   3711 C  C   . VAL   B 1 106 ? -40.1   -1.118  -32.636 1   27.67 ? 91  VAL   B C   1 
ATOM   3712 O  O   . VAL   B 1 106 ? -40.033 -1.252  -33.854 1   28.06 ? 91  VAL   B O   1 
ATOM   3713 C  CB  . VAL   B 1 106 ? -39.347 1.064   -31.541 1   28.92 ? 91  VAL   B CB  1 
ATOM   3714 C  CG1 . VAL   B 1 106 ? -38.19  1.039   -32.544 1   29.53 ? 91  VAL   B CG1 1 
ATOM   3715 C  CG2 . VAL   B 1 106 ? -39.772 2.496   -31.248 1   29.61 ? 91  VAL   B CG2 1 
ATOM   3716 N  N   . TRP   B 1 107 ? -39.758 -2.096  -31.788 1   27.36 ? 92  TRP   B N   1 
ATOM   3717 C  CA  . TRP   B 1 107 ? -39.194 -3.36   -32.254 1   27.32 ? 92  TRP   B CA  1 
ATOM   3718 C  C   . TRP   B 1 107 ? -40.227 -4.427  -32.623 1   28.24 ? 92  TRP   B C   1 
ATOM   3719 O  O   . TRP   B 1 107 ? -39.895 -5.365  -33.361 1   27.77 ? 92  TRP   B O   1 
ATOM   3720 C  CB  . TRP   B 1 107 ? -38.168 -3.919  -31.226 1   26.69 ? 92  TRP   B CB  1 
ATOM   3721 C  CG  . TRP   B 1 107 ? -37.057 -2.948  -30.907 1   26.69 ? 92  TRP   B CG  1 
ATOM   3722 C  CD1 . TRP   B 1 107 ? -36.737 -2.434  -29.685 1   26.66 ? 92  TRP   B CD1 1 
ATOM   3723 C  CD2 . TRP   B 1 107 ? -36.154 -2.346  -31.843 1   27.19 ? 92  TRP   B CD2 1 
ATOM   3724 N  NE1 . TRP   B 1 107 ? -35.729 -1.51   -29.809 1   26.72 ? 92  TRP   B NE1 1 
ATOM   3725 C  CE2 . TRP   B 1 107 ? -35.341 -1.447  -31.124 1   27.25 ? 92  TRP   B CE2 1 
ATOM   3726 C  CE3 . TRP   B 1 107 ? -35.986 -2.446  -33.231 1   28.52 ? 92  TRP   B CE3 1 
ATOM   3727 C  CZ2 . TRP   B 1 107 ? -34.377 -0.656  -31.743 1   28.23 ? 92  TRP   B CZ2 1 
ATOM   3728 C  CZ3 . TRP   B 1 107 ? -35.012 -1.679  -33.837 1   29.59 ? 92  TRP   B CZ3 1 
ATOM   3729 C  CH2 . TRP   B 1 107 ? -34.224 -0.794  -33.096 1   29.27 ? 92  TRP   B CH2 1 
ATOM   3730 N  N   . GLY   B 1 108 ? -41.419 -4.341  -32.048 1   27.98 ? 93  GLY   B N   1 
ATOM   3731 C  CA  . GLY   B 1 108 ? -42.476 -5.323  -32.277 1   28.83 ? 93  GLY   B CA  1 
ATOM   3732 C  C   . GLY   B 1 108 ? -42.047 -6.687  -31.8   1   29.54 ? 93  GLY   B C   1 
ATOM   3733 O  O   . GLY   B 1 108 ? -41.469 -6.811  -30.723 1   28.92 ? 93  GLY   B O   1 
ATOM   3734 N  N   . LYS   B 1 109 ? -42.203 -7.696  -32.664 1   30.3  ? 94  LYS   B N   1 
ATOM   3735 C  CA  . LYS   B 1 109 ? -41.77  -9.064  -32.38  1   32.36 ? 94  LYS   B CA  1 
ATOM   3736 C  C   . LYS   B 1 109 ? -40.26  -9.277  -32.563 1   34.26 ? 94  LYS   B C   1 
ATOM   3737 O  O   . LYS   B 1 109 ? -39.796 -10.39  -32.37  1   34.02 ? 94  LYS   B O   1 
ATOM   3738 C  CB  . LYS   B 1 109 ? -42.538 -10.07  -33.262 1   33.79 ? 94  LYS   B CB  1 
ATOM   3739 C  CG  . LYS   B 1 109 ? -44.035 -10.004 -33.062 1   37.82 ? 94  LYS   B CG  1 
ATOM   3740 C  CD  . LYS   B 1 109 ? -44.74  -10.958 -34.001 1   43.27 ? 94  LYS   B CD  1 
ATOM   3741 C  CE  . LYS   B 1 109 ? -46.223 -10.918 -33.831 1   46.93 ? 94  LYS   B CE  1 
ATOM   3742 N  NZ  . LYS   B 1 109 ? -46.868 -11.977 -34.636 1   50    ? 94  LYS   B NZ  1 
ATOM   3743 N  N   . GLY   B 1 110 ? -39.535 -8.242  -32.981 1   36.26 ? 95  GLY   B N   1 
ATOM   3744 C  CA  . GLY   B 1 110 ? -38.092 -8.276  -33.16  1   39.24 ? 95  GLY   B CA  1 
ATOM   3745 C  C   . GLY   B 1 110 ? -37.594 -9.064  -34.343 1   42.25 ? 95  GLY   B C   1 
ATOM   3746 O  O   . GLY   B 1 110 ? -36.516 -9.661  -34.274 1   43.07 ? 95  GLY   B O   1 
ATOM   3747 N  N   . HIS   B 1 111 ? -38.342 -9.035  -35.449 1   43.62 ? 96  HIS   B N   1 
ATOM   3748 C  CA  . HIS   B 1 111 ? -37.922 -9.732  -36.651 1   45.63 ? 96  HIS   B CA  1 
ATOM   3749 C  C   . HIS   B 1 111 ? -37.731 -8.803  -37.85  1   46.17 ? 96  HIS   B C   1 
ATOM   3750 O  O   . HIS   B 1 111 ? -37.958 -9.207  -38.987 1   46.66 ? 96  HIS   B O   1 
ATOM   3751 C  CB  . HIS   B 1 111 ? -38.872 -10.89  -36.953 1   48.11 ? 96  HIS   B CB  1 
ATOM   3752 C  CG  . HIS   B 1 111 ? -38.806 -11.935 -35.887 1   53.4  ? 96  HIS   B CG  1 
ATOM   3753 N  ND1 . HIS   B 1 111 ? -37.602 -12.539 -35.545 1   56.41 ? 96  HIS   B ND1 1 
ATOM   3754 C  CD2 . HIS   B 1 111 ? -39.784 -12.426 -35.09  1   55.43 ? 96  HIS   B CD2 1 
ATOM   3755 C  CE1 . HIS   B 1 111 ? -37.886 -13.371 -34.554 1   57.34 ? 96  HIS   B CE1 1 
ATOM   3756 N  NE2 . HIS   B 1 111 ? -39.188 -13.34  -34.245 1   57.22 ? 96  HIS   B NE2 1 
ATOM   3757 N  N   . GLY   B 1 112 ? -37.311 -7.57   -37.589 1   45.96 ? 97  GLY   B N   1 
ATOM   3758 C  CA  . GLY   B 1 112 ? -37.024 -6.621  -38.653 1   46.46 ? 97  GLY   B CA  1 
ATOM   3759 C  C   . GLY   B 1 112 ? -38.106 -5.64   -39.039 1   46.84 ? 97  GLY   B C   1 
ATOM   3760 O  O   . GLY   B 1 112 ? -37.811 -4.692  -39.77  1   47.51 ? 97  GLY   B O   1 
ATOM   3761 N  N   . ASP   B 1 113 ? -39.364 -5.853  -38.604 1   46.46 ? 98  ASP   B N   1 
ATOM   3762 C  CA  . ASP   B 1 113 ? -40.433 -4.915  -38.948 1   46.39 ? 98  ASP   B CA  1 
ATOM   3763 C  C   . ASP   B 1 113 ? -40.483 -3.857  -37.862 1   45.84 ? 98  ASP   B C   1 
ATOM   3764 O  O   . ASP   B 1 113 ? -41.122 -4.053  -36.827 1   46.48 ? 98  ASP   B O   1 
ATOM   3765 C  CB  . ASP   B 1 113 ? -41.791 -5.611  -39.123 1   48.4  ? 98  ASP   B CB  1 
ATOM   3766 C  CG  . ASP   B 1 113 ? -42.886 -4.632  -39.516 1   53.69 ? 98  ASP   B CG  1 
ATOM   3767 O  OD1 . ASP   B 1 113 ? -42.599 -3.704  -40.311 1   54.64 ? 98  ASP   B OD1 1 
ATOM   3768 O  OD2 . ASP   B 1 113 ? -44.016 -4.778  -39.02  1   55.93 ? 98  ASP   B OD2 1 
ATOM   3769 N  N   . VAL   B 1 114 ? -39.788 -2.746  -38.092 1   44.43 ? 99  VAL   B N   1 
ATOM   3770 C  CA  . VAL   B 1 114 ? -39.634 -1.678  -37.12  1   43.77 ? 99  VAL   B CA  1 
ATOM   3771 C  C   . VAL   B 1 114 ? -40.507 -0.445  -37.369 1   43.18 ? 99  VAL   B C   1 
ATOM   3772 O  O   . VAL   B 1 114 ? -40.711 -0.049  -38.512 1   43.99 ? 99  VAL   B O   1 
ATOM   3773 C  CB  . VAL   B 1 114 ? -38.137 -1.295  -37.036 1   44.67 ? 99  VAL   B CB  1 
ATOM   3774 C  CG1 . VAL   B 1 114 ? -37.574 -0.949  -38.408 1   45.45 ? 99  VAL   B CG1 1 
ATOM   3775 C  CG2 . VAL   B 1 114 ? -37.913 -0.15   -36.077 1   45.16 ? 99  VAL   B CG2 1 
ATOM   3776 N  N   . ARG   B 1 115 ? -41.028 0.158   -36.29  1   41.56 ? 100 ARG   B N   1 
ATOM   3777 C  CA  . ARG   B 1 115 ? -41.806 1.379   -36.36  1   41.09 ? 100 ARG   B CA  1 
ATOM   3778 C  C   . ARG   B 1 115 ? -40.855 2.541   -36.203 1   40.54 ? 100 ARG   B C   1 
ATOM   3779 O  O   . ARG   B 1 115 ? -40.119 2.615   -35.213 1   40.52 ? 100 ARG   B O   1 
ATOM   3780 C  CB  . ARG   B 1 115 ? -42.848 1.436   -35.224 1   42.43 ? 100 ARG   B CB  1 
ATOM   3781 C  CG  . ARG   B 1 115 ? -44.037 0.506   -35.401 1   45.98 ? 100 ARG   B CG  1 
ATOM   3782 C  CD  . ARG   B 1 115 ? -45.135 1.114   -36.253 1   50.31 ? 100 ARG   B CD  1 
ATOM   3783 N  NE  . ARG   B 1 115 ? -45.477 0.212   -37.35  1   54.21 ? 100 ARG   B NE  1 
ATOM   3784 C  CZ  . ARG   B 1 115 ? -46.597 -0.497  -37.426 1   56.88 ? 100 ARG   B CZ  1 
ATOM   3785 N  NH1 . ARG   B 1 115 ? -47.538 -0.368  -36.498 1   56.43 ? 100 ARG   B NH1 1 
ATOM   3786 N  NH2 . ARG   B 1 115 ? -46.807 -1.303  -38.456 1   57.63 ? 100 ARG   B NH2 1 
ATOM   3787 N  N   . LYS   B 1 116 ? -40.879 3.465   -37.162 1   39.77 ? 101 LYS   B N   1 
ATOM   3788 C  CA  . LYS   B 1 116 ? -40.043 4.661   -37.156 1   39.42 ? 101 LYS   B CA  1 
ATOM   3789 C  C   . LYS   B 1 116 ? -40.723 5.895   -36.555 1   38.45 ? 101 LYS   B C   1 
ATOM   3790 O  O   . LYS   B 1 116 ? -40.08  6.935   -36.443 1   38.52 ? 101 LYS   B O   1 
ATOM   3791 C  CB  . LYS   B 1 116 ? -39.549 4.959   -38.576 1   42.28 ? 101 LYS   B CB  1 
ATOM   3792 C  CG  . LYS   B 1 116 ? -38.772 3.786   -39.155 1   47.52 ? 101 LYS   B CG  1 
ATOM   3793 C  CD  . LYS   B 1 116 ? -38.575 3.874   -40.641 1   53.26 ? 101 LYS   B CD  1 
ATOM   3794 C  CE  . LYS   B 1 116 ? -38.116 2.527   -41.166 1   58.43 ? 101 LYS   B CE  1 
ATOM   3795 N  NZ  . LYS   B 1 116 ? -37.056 1.915   -40.302 1   61.18 ? 101 LYS   B NZ  1 
ATOM   3796 N  N   . VAL   B 1 117 ? -42.01  5.805   -36.194 1   37.36 ? 102 VAL   B N   1 
ATOM   3797 C  CA  . VAL   B 1 117 ? -42.727 6.934   -35.619 1   37.64 ? 102 VAL   B CA  1 
ATOM   3798 C  C   . VAL   B 1 117 ? -43.398 6.474   -34.331 1   38.2  ? 102 VAL   B C   1 
ATOM   3799 O  O   . VAL   B 1 117 ? -44.136 5.508   -34.348 1   38.43 ? 102 VAL   B O   1 
ATOM   3800 C  CB  . VAL   B 1 117 ? -43.785 7.526   -36.616 1   37.58 ? 102 VAL   B CB  1 
ATOM   3801 C  CG1 . VAL   B 1 117 ? -44.575 8.664   -35.969 1   37.64 ? 102 VAL   B CG1 1 
ATOM   3802 C  CG2 . VAL   B 1 117 ? -43.13  8.003   -37.911 1   37.73 ? 102 VAL   B CG2 1 
ATOM   3803 N  N   . LEU   B 1 118 ? -43.161 7.162   -33.226 1   38.8  ? 103 LEU   B N   1 
ATOM   3804 C  CA  . LEU   B 1 118 ? -43.798 6.854   -31.952 1   39.79 ? 103 LEU   B CA  1 
ATOM   3805 C  C   . LEU   B 1 118 ? -45.056 7.735   -31.892 1   41.35 ? 103 LEU   B C   1 
ATOM   3806 O  O   . LEU   B 1 118 ? -44.931 8.948   -31.985 1   41.81 ? 103 LEU   B O   1 
ATOM   3807 C  CB  . LEU   B 1 118 ? -42.847 7.206   -30.793 1   39.42 ? 103 LEU   B CB  1 
ATOM   3808 C  CG  . LEU   B 1 118 ? -43.294 6.755   -29.405 1   40.34 ? 103 LEU   B CG  1 
ATOM   3809 C  CD1 . LEU   B 1 118 ? -43.435 5.236   -29.34  1   40.12 ? 103 LEU   B CD1 1 
ATOM   3810 C  CD2 . LEU   B 1 118 ? -42.337 7.269   -28.336 1   40.82 ? 103 LEU   B CD2 1 
ATOM   3811 N  N   . PRO   B 1 119 ? -46.26  7.159   -31.769 1   42.31 ? 104 PRO   B N   1 
ATOM   3812 C  CA  . PRO   B 1 119 ? -47.488 7.987   -31.78  1   43.49 ? 104 PRO   B CA  1 
ATOM   3813 C  C   . PRO   B 1 119 ? -47.534 9.071   -30.723 1   44.65 ? 104 PRO   B C   1 
ATOM   3814 O  O   . PRO   B 1 119 ? -47.093 8.839   -29.606 1   44.88 ? 104 PRO   B O   1 
ATOM   3815 C  CB  . PRO   B 1 119 ? -48.606 6.971   -31.561 1   44.01 ? 104 PRO   B CB  1 
ATOM   3816 C  CG  . PRO   B 1 119 ? -48.023 5.661   -31.984 1   44.03 ? 104 PRO   B CG  1 
ATOM   3817 C  CD  . PRO   B 1 119 ? -46.57  5.722   -31.664 1   42.09 ? 104 PRO   B CD  1 
ATOM   3818 N  N   . ARG   B 1 120 ? -48.092 10.243  -31.07  1   45.09 ? 105 ARG   B N   1 
ATOM   3819 C  CA  . ARG   B 1 120 ? -48.176 11.404  -30.187 1   45.83 ? 105 ARG   B CA  1 
ATOM   3820 C  C   . ARG   B 1 120 ? -48.803 11.143  -28.848 1   46.24 ? 105 ARG   B C   1 
ATOM   3821 O  O   . ARG   B 1 120 ? -48.39  11.748  -27.86  1   47.01 ? 105 ARG   B O   1 
ATOM   3822 C  CB  . ARG   B 1 120 ? -48.915 12.562  -30.882 1   47.9  ? 105 ARG   B CB  1 
ATOM   3823 C  CG  . ARG   B 1 120 ? -50.41  12.296  -31.112 1   51.74 ? 105 ARG   B CG  1 
ATOM   3824 C  CD  . ARG   B 1 120 ? -51.034 13.112  -32.235 1   55.13 ? 105 ARG   B CD  1 
ATOM   3825 N  NE  . ARG   B 1 120 ? -50.435 14.44   -32.33  1   57.77 ? 105 ARG   B NE  1 
ATOM   3826 C  CZ  . ARG   B 1 120 ? -49.8   14.899  -33.402 1   60.03 ? 105 ARG   B CZ  1 
ATOM   3827 N  NH1 . ARG   B 1 120 ? -49.773 14.187  -34.523 1   60.08 ? 105 ARG   B NH1 1 
ATOM   3828 N  NH2 . ARG   B 1 120 ? -49.23  16.096  -33.38  1   59.36 ? 105 ARG   B NH2 1 
ATOM   3829 N  N   . ASN   B 1 121 ? -49.791 10.251  -28.791 1   45.89 ? 106 ASN   B N   1 
ATOM   3830 C  CA  . ASN   B 1 121 ? -50.49  9.988   -27.545 1   46.41 ? 106 ASN   B CA  1 
ATOM   3831 C  C   . ASN   B 1 121 ? -49.562 9.368   -26.486 1   45.99 ? 106 ASN   B C   1 
ATOM   3832 O  O   . ASN   B 1 121 ? -49.851 9.533   -25.303 1   46.29 ? 106 ASN   B O   1 
ATOM   3833 C  CB  . ASN   B 1 121 ? -51.786 9.218   -27.793 1   48.41 ? 106 ASN   B CB  1 
ATOM   3834 C  CG  . ASN   B 1 121 ? -52.843 10.126  -28.487 1   53.36 ? 106 ASN   B CG  1 
ATOM   3835 O  OD1 . ASN   B 1 121 ? -52.688 11.353  -28.619 1   54.36 ? 106 ASN   B OD1 1 
ATOM   3836 N  ND2 . ASN   B 1 121 ? -53.949 9.563   -28.955 1   54.17 ? 106 ASN   B ND2 1 
ATOM   3837 N  N   . ILE   B 1 122 ? -48.425 8.734   -26.886 1   45.07 ? 107 ILE   B N   1 
ATOM   3838 C  CA  . ILE   B 1 122 ? -47.417 8.278   -25.913 1   44.43 ? 107 ILE   B CA  1 
ATOM   3839 C  C   . ILE   B 1 122 ? -46.155 9.128   -25.976 1   42.83 ? 107 ILE   B C   1 
ATOM   3840 O  O   . ILE   B 1 122 ? -45.569 9.391   -24.931 1   43.11 ? 107 ILE   B O   1 
ATOM   3841 C  CB  . ILE   B 1 122 ? -47.045 6.789   -25.912 1   45.57 ? 107 ILE   B CB  1 
ATOM   3842 C  CG1 . ILE   B 1 122 ? -46.806 6.252   -27.314 1   46.71 ? 107 ILE   B CG1 1 
ATOM   3843 C  CG2 . ILE   B 1 122 ? -48.037 5.957   -25.14  1   46.57 ? 107 ILE   B CG2 1 
ATOM   3844 C  CD1 . ILE   B 1 122 ? -46.141 4.856   -27.242 1   49.16 ? 107 ILE   B CD1 1 
ATOM   3845 N  N   . ALA   B 1 123 ? -45.718 9.533   -27.184 1   41.24 ? 108 ALA   B N   1 
ATOM   3846 C  CA  . ALA   B 1 123 ? -44.505 10.328  -27.355 1   40.9  ? 108 ALA   B CA  1 
ATOM   3847 C  C   . ALA   B 1 123 ? -44.536 11.627  -26.58  1   40.47 ? 108 ALA   B C   1 
ATOM   3848 O  O   . ALA   B 1 123 ? -43.541 11.98   -25.95  1   40.35 ? 108 ALA   B O   1 
ATOM   3849 C  CB  . ALA   B 1 123 ? -44.231 10.598  -28.827 1   40.96 ? 108 ALA   B CB  1 
ATOM   3850 N  N   . VAL   B 1 124 ? -45.672 12.343  -26.612 1   39.36 ? 109 VAL   B N   1 
ATOM   3851 C  CA  . VAL   B 1 124 ? -45.779 13.614  -25.916 1   38.58 ? 109 VAL   B CA  1 
ATOM   3852 C  C   . VAL   B 1 124 ? -45.635 13.446  -24.384 1   38    ? 109 VAL   B C   1 
ATOM   3853 O  O   . VAL   B 1 124 ? -44.702 14.047  -23.837 1   38.55 ? 109 VAL   B O   1 
ATOM   3854 C  CB  . VAL   B 1 124 ? -47.037 14.422  -26.344 1   39.02 ? 109 VAL   B CB  1 
ATOM   3855 C  CG1 . VAL   B 1 124 ? -47.275 15.606  -25.41  1   39.51 ? 109 VAL   B CG1 1 
ATOM   3856 C  CG2 . VAL   B 1 124 ? -46.896 14.894  -27.788 1   38.86 ? 109 VAL   B CG2 1 
ATOM   3857 N  N   . PRO   B 1 125 ? -46.447 12.621  -23.677 1   36.8  ? 110 PRO   B N   1 
ATOM   3858 C  CA  . PRO   B 1 125 ? -46.243 12.492  -22.226 1   35.78 ? 110 PRO   B CA  1 
ATOM   3859 C  C   . PRO   B 1 125 ? -44.88  11.882  -21.864 1   35.43 ? 110 PRO   B C   1 
ATOM   3860 O  O   . PRO   B 1 125 ? -44.301 12.225  -20.831 1   35.21 ? 110 PRO   B O   1 
ATOM   3861 C  CB  . PRO   B 1 125 ? -47.404 11.605  -21.762 1   36.48 ? 110 PRO   B CB  1 
ATOM   3862 C  CG  . PRO   B 1 125 ? -47.917 10.929  -22.984 1   37.56 ? 110 PRO   B CG  1 
ATOM   3863 C  CD  . PRO   B 1 125 ? -47.614 11.836  -24.139 1   36.02 ? 110 PRO   B CD  1 
ATOM   3864 N  N   . TYR   B 1 126 ? -44.356 10.994  -22.724 1   34.36 ? 111 TYR   B N   1 
ATOM   3865 C  CA  . TYR   B 1 126 ? -43.051 10.382  -22.485 1   33.02 ? 111 TYR   B CA  1 
ATOM   3866 C  C   . TYR   B 1 126 ? -41.964 11.441  -22.544 1   33.48 ? 111 TYR   B C   1 
ATOM   3867 O  O   . TYR   B 1 126 ? -41.158 11.535  -21.616 1   33.71 ? 111 TYR   B O   1 
ATOM   3868 C  CB  . TYR   B 1 126 ? -42.804 9.263   -23.502 1   31.33 ? 111 TYR   B CB  1 
ATOM   3869 C  CG  . TYR   B 1 126 ? -41.597 8.391   -23.22  1   29.79 ? 111 TYR   B CG  1 
ATOM   3870 C  CD1 . TYR   B 1 126 ? -41.102 8.241   -21.927 1   29.35 ? 111 TYR   B CD1 1 
ATOM   3871 C  CD2 . TYR   B 1 126 ? -41     7.661   -24.231 1   30.19 ? 111 TYR   B CD2 1 
ATOM   3872 C  CE1 . TYR   B 1 126 ? -40.019 7.412   -21.658 1   29.27 ? 111 TYR   B CE1 1 
ATOM   3873 C  CE2 . TYR   B 1 126 ? -39.928 6.812   -23.974 1   30.24 ? 111 TYR   B CE2 1 
ATOM   3874 C  CZ  . TYR   B 1 126 ? -39.424 6.714   -22.692 1   29.75 ? 111 TYR   B CZ  1 
ATOM   3875 O  OH  . TYR   B 1 126 ? -38.376 5.866   -22.466 1   28.33 ? 111 TYR   B OH  1 
ATOM   3876 N  N   . CYS   B 1 127 ? -41.95  12.262  -23.598 1   33.62 ? 112 CYS   B N   1 
ATOM   3877 C  CA  . CYS   B 1 127 ? -40.97  13.328  -23.723 1   34.59 ? 112 CYS   B CA  1 
ATOM   3878 C  C   . CYS   B 1 127 ? -41.115 14.373  -22.615 1   35.88 ? 112 CYS   B C   1 
ATOM   3879 O  O   . CYS   B 1 127 ? -40.101 14.857  -22.104 1   35.77 ? 112 CYS   B O   1 
ATOM   3880 C  CB  . CYS   B 1 127 ? -41.03  13.972  -25.097 1   35.15 ? 112 CYS   B CB  1 
ATOM   3881 S  SG  . CYS   B 1 127 ? -40.404 12.938  -26.455 1   38.2  ? 112 CYS   B SG  1 
ATOM   3882 N  N   . GLN   B 1 128 ? -42.362 14.696  -22.219 1   36.8  ? 113 GLN   B N   1 
ATOM   3883 C  CA  . GLN   B 1 128 ? -42.604 15.677  -21.151 1   37.17 ? 113 GLN   B CA  1 
ATOM   3884 C  C   . GLN   B 1 128 ? -42.06  15.157  -19.823 1   36.82 ? 113 GLN   B C   1 
ATOM   3885 O  O   . GLN   B 1 128 ? -41.365 15.892  -19.12  1   37.28 ? 113 GLN   B O   1 
ATOM   3886 C  CB  . GLN   B 1 128 ? -44.104 16.01   -21.022 1   38.83 ? 113 GLN   B CB  1 
ATOM   3887 C  CG  . GLN   B 1 128 ? -44.605 16.857  -22.182 1   42.57 ? 113 GLN   B CG  1 
ATOM   3888 C  CD  . GLN   B 1 128 ? -46.109 16.988  -22.198 1   47.76 ? 113 GLN   B CD  1 
ATOM   3889 O  OE1 . GLN   B 1 128 ? -46.854 16.188  -21.591 1   48.29 ? 113 GLN   B OE1 1 
ATOM   3890 N  NE2 . GLN   B 1 128 ? -46.587 18.01   -22.914 1   48.73 ? 113 GLN   B NE2 1 
ATOM   3891 N  N   . LEU   B 1 129 ? -42.357 13.901  -19.493 1   35.87 ? 114 LEU   B N   1 
ATOM   3892 C  CA  . LEU   B 1 129 ? -41.892 13.264  -18.262 1   36.33 ? 114 LEU   B CA  1 
ATOM   3893 C  C   . LEU   B 1 129 ? -40.353 13.14   -18.264 1   36.33 ? 114 LEU   B C   1 
ATOM   3894 O  O   . LEU   B 1 129 ? -39.698 13.393  -17.246 1   36.9  ? 114 LEU   B O   1 
ATOM   3895 C  CB  . LEU   B 1 129 ? -42.535 11.877  -18.134 1   36.46 ? 114 LEU   B CB  1 
ATOM   3896 C  CG  . LEU   B 1 129 ? -42.27  11.125  -16.833 1   37.98 ? 114 LEU   B CG  1 
ATOM   3897 C  CD1 . LEU   B 1 129 ? -42.75  11.915  -15.623 1   38.97 ? 114 LEU   B CD1 1 
ATOM   3898 C  CD2 . LEU   B 1 129 ? -42.932 9.766   -16.85  1   37.91 ? 114 LEU   B CD2 1 
ATOM   3899 N  N   . SER   B 1 130 ? -39.786 12.786  -19.419 1   35.24 ? 115 SER   B N   1 
ATOM   3900 C  CA  . SER   B 1 130 ? -38.347 12.658  -19.583 1   34.55 ? 115 SER   B CA  1 
ATOM   3901 C  C   . SER   B 1 130 ? -37.674 14.015  -19.348 1   35.33 ? 115 SER   B C   1 
ATOM   3902 O  O   . SER   B 1 130 ? -36.72  14.09   -18.575 1   35.15 ? 115 SER   B O   1 
ATOM   3903 C  CB  . SER   B 1 130 ? -38.021 12.091  -20.961 1   32.31 ? 115 SER   B CB  1 
ATOM   3904 O  OG  . SER   B 1 130 ? -38.534 10.77   -21.04  1   30.84 ? 115 SER   B OG  1 
ATOM   3905 N  N   . LYS   B 1 131 ? -38.227 15.101  -19.918 1   35.78 ? 116 LYS   B N   1 
ATOM   3906 C  CA  . LYS   B 1 131 ? -37.684 16.452  -19.723 1   37.02 ? 116 LYS   B CA  1 
ATOM   3907 C  C   . LYS   B 1 131 ? -37.693 16.825  -18.244 1   37.84 ? 116 LYS   B C   1 
ATOM   3908 O  O   . LYS   B 1 131 ? -36.685 17.308  -17.725 1   39.35 ? 116 LYS   B O   1 
ATOM   3909 C  CB  . LYS   B 1 131 ? -38.484 17.491  -20.538 1   39.9  ? 116 LYS   B CB  1 
ATOM   3910 C  CG  . LYS   B 1 131 ? -37.974 18.923  -20.37  1   44.41 ? 116 LYS   B CG  1 
ATOM   3911 C  CD  . LYS   B 1 131 ? -38.464 19.811  -21.504 1   49.91 ? 116 LYS   B CD  1 
ATOM   3912 C  CE  . LYS   B 1 131 ? -37.779 21.159  -21.551 1   53.76 ? 116 LYS   B CE  1 
ATOM   3913 N  N   . LYS   B 1 132 ? -38.792 16.525  -17.557 1   37.25 ? 117 LYS   B N   1 
ATOM   3914 C  CA  . LYS   B 1 132 ? -38.983 16.769  -16.135 1   38.01 ? 117 LYS   B CA  1 
ATOM   3915 C  C   . LYS   B 1 132 ? -37.899 16.07   -15.287 1   38.3  ? 117 LYS   B C   1 
ATOM   3916 O  O   . LYS   B 1 132 ? -37.333 16.688  -14.382 1   38.44 ? 117 LYS   B O   1 
ATOM   3917 C  CB  . LYS   B 1 132 ? -40.376 16.272  -15.732 1   40.55 ? 117 LYS   B CB  1 
ATOM   3918 C  CG  . LYS   B 1 132 ? -40.759 16.517  -14.286 1   46.33 ? 117 LYS   B CG  1 
ATOM   3919 C  CD  . LYS   B 1 132 ? -42.252 16.264  -14.092 1   51.86 ? 117 LYS   B CD  1 
ATOM   3920 C  CE  . LYS   B 1 132 ? -42.862 17.174  -13.052 1   56.92 ? 117 LYS   B CE  1 
ATOM   3921 N  NZ  . LYS   B 1 132 ? -44.325 17.376  -13.279 1   59.93 ? 117 LYS   B NZ  1 
ATOM   3922 N  N   . LEU   B 1 133 ? -37.61  14.786  -15.588 1   37.47 ? 118 LEU   B N   1 
ATOM   3923 C  CA  . LEU   B 1 133 ? -36.61  14.025  -14.847 1   36.83 ? 118 LEU   B CA  1 
ATOM   3924 C  C   . LEU   B 1 133 ? -35.171 14.183  -15.375 1   35.35 ? 118 LEU   B C   1 
ATOM   3925 O  O   . LEU   B 1 133 ? -34.271 13.544  -14.835 1   35.36 ? 118 LEU   B O   1 
ATOM   3926 C  CB  . LEU   B 1 133 ? -36.995 12.537  -14.812 1   37.5  ? 118 LEU   B CB  1 
ATOM   3927 C  CG  . LEU   B 1 133 ? -38.284 12.184  -14.096 1   39.93 ? 118 LEU   B CG  1 
ATOM   3928 C  CD1 . LEU   B 1 133 ? -38.564 10.712  -14.18  1   40.27 ? 118 LEU   B CD1 1 
ATOM   3929 C  CD2 . LEU   B 1 133 ? -38.232 12.582  -12.647 1   41.47 ? 118 LEU   B CD2 1 
ATOM   3930 N  N   . GLU   B 1 134 ? -34.959 15.013  -16.413 1   33.88 ? 119 GLU   B N   1 
ATOM   3931 C  CA  . GLU   B 1 134 ? -33.673 15.254  -17.061 1   33.41 ? 119 GLU   B CA  1 
ATOM   3932 C  C   . GLU   B 1 134 ? -33.043 13.959  -17.575 1   33.78 ? 119 GLU   B C   1 
ATOM   3933 O  O   . GLU   B 1 134 ? -31.842 13.738  -17.433 1   33.93 ? 119 GLU   B O   1 
ATOM   3934 C  CB  . GLU   B 1 134 ? -32.693 16.023  -16.165 1   34.66 ? 119 GLU   B CB  1 
ATOM   3935 C  CG  . GLU   B 1 134 ? -33.245 17.327  -15.632 1   38.99 ? 119 GLU   B CG  1 
ATOM   3936 C  CD  . GLU   B 1 134 ? -32.195 18.067  -14.826 1   44.45 ? 119 GLU   B CD  1 
ATOM   3937 O  OE1 . GLU   B 1 134 ? -31.101 18.314  -15.385 1   45.91 ? 119 GLU   B OE1 1 
ATOM   3938 O  OE2 . GLU   B 1 134 ? -32.449 18.369  -13.637 1   45.72 ? 119 GLU   B OE2 1 
ATOM   3939 N  N   . LEU   B 1 135 ? -33.864 13.11   -18.171 1   32.94 ? 120 LEU   B N   1 
ATOM   3940 C  CA  . LEU   B 1 135 ? -33.435 11.847  -18.747 1   32.07 ? 120 LEU   B CA  1 
ATOM   3941 C  C   . LEU   B 1 135 ? -33.956 11.808  -20.186 1   32.34 ? 120 LEU   B C   1 
ATOM   3942 O  O   . LEU   B 1 135 ? -34.985 12.431  -20.503 1   32.07 ? 120 LEU   B O   1 
ATOM   3943 C  CB  . LEU   B 1 135 ? -34.026 10.688  -17.93  1   31.18 ? 120 LEU   B CB  1 
ATOM   3944 C  CG  . LEU   B 1 135 ? -33.302 10.35   -16.596 1   30.5  ? 120 LEU   B CG  1 
ATOM   3945 C  CD1 . LEU   B 1 135 ? -34.1   9.341   -15.777 1   29.69 ? 120 LEU   B CD1 1 
ATOM   3946 C  CD2 . LEU   B 1 135 ? -31.914 9.81    -16.846 1   30.19 ? 120 LEU   B CD2 1 
ATOM   3947 N  N   . PRO   B 1 136 ? -33.232 11.131  -21.092 1   31.28 ? 121 PRO   B N   1 
ATOM   3948 C  CA  . PRO   B 1 136 ? -33.706 11.034  -22.481 1   29.95 ? 121 PRO   B CA  1 
ATOM   3949 C  C   . PRO   B 1 136 ? -34.948 10.156  -22.602 1   28.5  ? 121 PRO   B C   1 
ATOM   3950 O  O   . PRO   B 1 136 ? -35.168 9.268   -21.76  1   27.75 ? 121 PRO   B O   1 
ATOM   3951 C  CB  . PRO   B 1 136 ? -32.52  10.382  -23.2   1   31.13 ? 121 PRO   B CB  1 
ATOM   3952 C  CG  . PRO   B 1 136 ? -31.884 9.548   -22.136 1   31.95 ? 121 PRO   B CG  1 
ATOM   3953 C  CD  . PRO   B 1 136 ? -31.99  10.357  -20.881 1   30.31 ? 121 PRO   B CD  1 
ATOM   3954 N  N   . PRO   B 1 137 ? -35.768 10.398  -23.66  1   28.03 ? 122 PRO   B N   1 
ATOM   3955 C  CA  . PRO   B 1 137 ? -36.975 9.577   -23.876 1   27.65 ? 122 PRO   B CA  1 
ATOM   3956 C  C   . PRO   B 1 137 ? -36.703 8.207   -24.496 1   26.6  ? 122 PRO   B C   1 
ATOM   3957 O  O   . PRO   B 1 137 ? -37.171 7.877   -25.609 1   27.03 ? 122 PRO   B O   1 
ATOM   3958 C  CB  . PRO   B 1 137 ? -37.819 10.439  -24.819 1   28.37 ? 122 PRO   B CB  1 
ATOM   3959 C  CG  . PRO   B 1 137 ? -36.83  11.191  -25.628 1   28.77 ? 122 PRO   B CG  1 
ATOM   3960 C  CD  . PRO   B 1 137 ? -35.622 11.43   -24.711 1   27.51 ? 122 PRO   B CD  1 
ATOM   3961 N  N   . ILE   B 1 138 ? -35.981 7.386   -23.743 1   24.69 ? 123 ILE   B N   1 
ATOM   3962 C  CA  . ILE   B 1 138 ? -35.666 6.004   -24.088 1   23.89 ? 123 ILE   B CA  1 
ATOM   3963 C  C   . ILE   B 1 138 ? -35.422 5.268   -22.77  1   23.37 ? 123 ILE   B C   1 
ATOM   3964 O  O   . ILE   B 1 138 ? -35.064 5.891   -21.759 1   23.74 ? 123 ILE   B O   1 
ATOM   3965 C  CB  . ILE   B 1 138 ? -34.471 5.904   -25.08  1   24.05 ? 123 ILE   B CB  1 
ATOM   3966 C  CG1 . ILE   B 1 138 ? -34.353 4.472   -25.653 1   24.64 ? 123 ILE   B CG1 1 
ATOM   3967 C  CG2 . ILE   B 1 138 ? -33.144 6.394   -24.418 1   24.49 ? 123 ILE   B CG2 1 
ATOM   3968 C  CD1 . ILE   B 1 138 ? -33.384 4.328   -26.827 1   25.49 ? 123 ILE   B CD1 1 
ATOM   3969 N  N   . LEU   B 1 139 ? -35.693 3.968   -22.742 1   22.2  ? 124 LEU   B N   1 
ATOM   3970 C  CA  . LEU   B 1 139 ? -35.464 3.14    -21.564 1   22.51 ? 124 LEU   B CA  1 
ATOM   3971 C  C   . LEU   B 1 139 ? -33.957 3.174   -21.189 1   21.85 ? 124 LEU   B C   1 
ATOM   3972 O  O   . LEU   B 1 139 ? -33.102 2.932   -22.045 1   22.18 ? 124 LEU   B O   1 
ATOM   3973 C  CB  . LEU   B 1 139 ? -35.911 1.708   -21.871 1   22.71 ? 124 LEU   B CB  1 
ATOM   3974 C  CG  . LEU   B 1 139 ? -36.156 0.786   -20.696 1   24.98 ? 124 LEU   B CG  1 
ATOM   3975 C  CD1 . LEU   B 1 139 ? -37.285 1.309   -19.827 1   25.5  ? 124 LEU   B CD1 1 
ATOM   3976 C  CD2 . LEU   B 1 139 ? -36.4   -0.677  -21.181 1   25.28 ? 124 LEU   B CD2 1 
ATOM   3977 N  N   . VAL   B 1 140 ? -33.649 3.582   -19.957 1   21.4  ? 125 VAL   B N   1 
ATOM   3978 C  CA  . VAL   B 1 140 ? -32.258 3.612   -19.48  1   21.11 ? 125 VAL   B CA  1 
ATOM   3979 C  C   . VAL   B 1 140 ? -32.063 2.539   -18.376 1   21.44 ? 125 VAL   B C   1 
ATOM   3980 O  O   . VAL   B 1 140 ? -33.046 1.986   -17.836 1   21.53 ? 125 VAL   B O   1 
ATOM   3981 C  CB  . VAL   B 1 140 ? -31.823 5.048   -19.02  1   21.29 ? 125 VAL   B CB  1 
ATOM   3982 C  CG1 . VAL   B 1 140 ? -32.005 6.076   -20.137 1   21.4  ? 125 VAL   B CG1 1 
ATOM   3983 C  CG2 . VAL   B 1 140 ? -32.572 5.478   -17.764 1   21.59 ? 125 VAL   B CG2 1 
ATOM   3984 N  N   . TYR   B 1 141 ? -30.802 2.284   -17.992 1   20.22 ? 126 TYR   B N   1 
ATOM   3985 C  CA  . TYR   B 1 141 ? -30.432 1.373   -16.903 1   19.41 ? 126 TYR   B CA  1 
ATOM   3986 C  C   . TYR   B 1 141 ? -31.18  1.76    -15.607 1   19.17 ? 126 TYR   B C   1 
ATOM   3987 O  O   . TYR   B 1 141 ? -31.662 0.872   -14.907 1   18.85 ? 126 TYR   B O   1 
ATOM   3988 C  CB  . TYR   B 1 141 ? -28.928 1.488   -16.683 1   18.71 ? 126 TYR   B CB  1 
ATOM   3989 C  CG  . TYR   B 1 141 ? -28.348 0.583   -15.622 1   19.22 ? 126 TYR   B CG  1 
ATOM   3990 C  CD1 . TYR   B 1 141 ? -28.057 -0.743  -15.901 1   20.52 ? 126 TYR   B CD1 1 
ATOM   3991 C  CD2 . TYR   B 1 141 ? -27.931 1.093   -14.402 1   20.45 ? 126 TYR   B CD2 1 
ATOM   3992 C  CE1 . TYR   B 1 141 ? -27.457 -1.565  -14.957 1   21.13 ? 126 TYR   B CE1 1 
ATOM   3993 C  CE2 . TYR   B 1 141 ? -27.298 0.288   -13.46  1   20.82 ? 126 TYR   B CE2 1 
ATOM   3994 C  CZ  . TYR   B 1 141 ? -27.075 -1.043  -13.738 1   21.8  ? 126 TYR   B CZ  1 
ATOM   3995 O  OH  . TYR   B 1 141 ? -26.431 -1.845  -12.817 1   23.25 ? 126 TYR   B OH  1 
ATOM   3996 N  N   . ALA   B 1 142 ? -31.317 3.072   -15.314 1   20.18 ? 127 ALA   B N   1 
ATOM   3997 C  CA  . ALA   B 1 142 ? -32.041 3.51    -14.109 1   22.38 ? 127 ALA   B CA  1 
ATOM   3998 C  C   . ALA   B 1 142 ? -33.534 3.151   -14.134 1   23.74 ? 127 ALA   B C   1 
ATOM   3999 O  O   . ALA   B 1 142 ? -34.173 3.096   -13.077 1   25.07 ? 127 ALA   B O   1 
ATOM   4000 C  CB  . ALA   B 1 142 ? -31.84  4.998   -13.847 1   22.32 ? 127 ALA   B CB  1 
ATOM   4001 N  N   . ASP   B 1 143 ? -34.096 2.921   -15.33  1   22.82 ? 128 ASP   B N   1 
ATOM   4002 C  CA  . ASP   B 1 143 ? -35.473 2.465   -15.432 1   22.42 ? 128 ASP   B CA  1 
ATOM   4003 C  C   . ASP   B 1 143 ? -35.538 0.949   -15.295 1   22.72 ? 128 ASP   B C   1 
ATOM   4004 O  O   . ASP   B 1 143 ? -36.129 0.449   -14.328 1   23.76 ? 128 ASP   B O   1 
ATOM   4005 C  CB  . ASP   B 1 143 ? -36.121 2.869   -16.778 1   22.2  ? 128 ASP   B CB  1 
ATOM   4006 C  CG  . ASP   B 1 143 ? -36.082 4.326   -17.116 1   24.17 ? 128 ASP   B CG  1 
ATOM   4007 O  OD1 . ASP   B 1 143 ? -36.417 5.153   -16.237 1   25.58 ? 128 ASP   B OD1 1 
ATOM   4008 O  OD2 . ASP   B 1 143 ? -35.764 4.648   -18.266 1   24.12 ? 128 ASP   B OD2 1 
ATOM   4009 N  N   . CYS   B 1 144 ? -34.961 0.186   -16.269 1   21.88 ? 129 CYS   B N   1 
ATOM   4010 C  CA  . CYS   B 1 144 ? -35.202 -1.253  -16.314 1   22.11 ? 129 CYS   B CA  1 
ATOM   4011 C  C   . CYS   B 1 144 ? -34.394 -2.07   -15.363 1   21.24 ? 129 CYS   B C   1 
ATOM   4012 O  O   . CYS   B 1 144 ? -34.714 -3.244  -15.191 1   20.88 ? 129 CYS   B O   1 
ATOM   4013 C  CB  . CYS   B 1 144 ? -35.099 -1.795  -17.733 1   23.8  ? 129 CYS   B CB  1 
ATOM   4014 S  SG  . CYS   B 1 144 ? -33.48  -1.538  -18.501 1   26.03 ? 129 CYS   B SG  1 
ATOM   4015 N  N   . VAL   B 1 145 ? -33.419 -1.466  -14.652 1   20.99 ? 130 VAL   B N   1 
ATOM   4016 C  CA  . VAL   B 1 145 ? -32.696 -2.209  -13.617 1   20.79 ? 130 VAL   B CA  1 
ATOM   4017 C  C   . VAL   B 1 145 ? -32.973 -1.57   -12.236 1   22.73 ? 130 VAL   B C   1 
ATOM   4018 O  O   . VAL   B 1 145 ? -33.491 -2.235  -11.329 1   23.34 ? 130 VAL   B O   1 
ATOM   4019 C  CB  . VAL   B 1 145 ? -31.181 -2.338  -13.903 1   20.08 ? 130 VAL   B CB  1 
ATOM   4020 C  CG1 . VAL   B 1 145 ? -30.437 -3.007  -12.722 1   19.88 ? 130 VAL   B CG1 1 
ATOM   4021 C  CG2 . VAL   B 1 145 ? -30.93  -3.089  -15.202 1   19.9  ? 130 VAL   B CG2 1 
ATOM   4022 N  N   . LEU   B 1 146 ? -32.624 -0.287  -12.077 1   22.02 ? 131 LEU   B N   1 
ATOM   4023 C  CA  . LEU   B 1 146 ? -32.698 0.365   -10.781 1   23.21 ? 131 LEU   B CA  1 
ATOM   4024 C  C   . LEU   B 1 146 ? -34.109 0.605   -10.228 1   24.06 ? 131 LEU   B C   1 
ATOM   4025 O  O   . LEU   B 1 146 ? -34.25  0.679   -9.012  1   24.08 ? 131 LEU   B O   1 
ATOM   4026 C  CB  . LEU   B 1 146 ? -31.912 1.684   -10.796 1   22.77 ? 131 LEU   B CB  1 
ATOM   4027 C  CG  . LEU   B 1 146 ? -30.462 1.575   -11.276 1   24.89 ? 131 LEU   B CG  1 
ATOM   4028 C  CD1 . LEU   B 1 146 ? -29.782 2.938   -11.174 1   24.63 ? 131 LEU   B CD1 1 
ATOM   4029 C  CD2 . LEU   B 1 146 ? -29.671 0.55    -10.424 1   26.36 ? 131 LEU   B CD2 1 
ATOM   4030 N  N   . ALA   B 1 147 ? -35.12  0.777   -11.094 1   24.11 ? 132 ALA   B N   1 
ATOM   4031 C  CA  . ALA   B 1 147 ? -36.492 1.017   -10.608 1   25.62 ? 132 ALA   B CA  1 
ATOM   4032 C  C   . ALA   B 1 147 ? -37.455 -0.154  -10.928 1   26.78 ? 132 ALA   B C   1 
ATOM   4033 O  O   . ALA   B 1 147 ? -38.641 -0.059  -10.627 1   28.16 ? 132 ALA   B O   1 
ATOM   4034 C  CB  . ALA   B 1 147 ? -37.029 2.292   -11.242 1   26.15 ? 132 ALA   B CB  1 
ATOM   4035 N  N   . ASN   B 1 148 ? -36.958 -1.231  -11.544 1   26.25 ? 133 ASN   B N   1 
ATOM   4036 C  CA  . ASN   B 1 148 ? -37.766 -2.35   -12.034 1   26.5  ? 133 ASN   B CA  1 
ATOM   4037 C  C   . ASN   B 1 148 ? -37.677 -3.559  -11.125 1   27.16 ? 133 ASN   B C   1 
ATOM   4038 O  O   . ASN   B 1 148 ? -37.33  -4.663  -11.569 1   27.35 ? 133 ASN   B O   1 
ATOM   4039 C  CB  . ASN   B 1 148 ? -37.315 -2.679  -13.466 1   26.58 ? 133 ASN   B CB  1 
ATOM   4040 C  CG  . ASN   B 1 148 ? -38.174 -3.684  -14.209 1   29.34 ? 133 ASN   B CG  1 
ATOM   4041 O  OD1 . ASN   B 1 148 ? -39.335 -3.905  -13.867 1   28.8  ? 133 ASN   B OD1 1 
ATOM   4042 N  ND2 . ASN   B 1 148 ? -37.602 -4.328  -15.232 1   28.51 ? 133 ASN   B ND2 1 
ATOM   4043 N  N   . TRP   B 1 149 ? -37.98  -3.353  -9.839  1   27.59 ? 134 TRP   B N   1 
ATOM   4044 C  CA  . TRP   B 1 149 ? -37.89  -4.442  -8.885  1   29.44 ? 134 TRP   B CA  1 
ATOM   4045 C  C   . TRP   B 1 149 ? -38.832 -4.274  -7.688  1   30.8  ? 134 TRP   B C   1 
ATOM   4046 O  O   . TRP   B 1 149 ? -39.332 -3.185  -7.433  1   29.76 ? 134 TRP   B O   1 
ATOM   4047 C  CB  . TRP   B 1 149 ? -36.434 -4.603  -8.402  1   30.04 ? 134 TRP   B CB  1 
ATOM   4048 C  CG  . TRP   B 1 149 ? -35.932 -3.47   -7.554  1   31.94 ? 134 TRP   B CG  1 
ATOM   4049 C  CD1 . TRP   B 1 149 ? -35.376 -2.301  -7.985  1   33.26 ? 134 TRP   B CD1 1 
ATOM   4050 C  CD2 . TRP   B 1 149 ? -35.92  -3.419  -6.12   1   33.04 ? 134 TRP   B CD2 1 
ATOM   4051 N  NE1 . TRP   B 1 149 ? -34.985 -1.538  -6.906  1   33.99 ? 134 TRP   B NE1 1 
ATOM   4052 C  CE2 . TRP   B 1 149 ? -35.306 -2.206  -5.749  1   34.27 ? 134 TRP   B CE2 1 
ATOM   4053 C  CE3 . TRP   B 1 149 ? -36.341 -4.3    -5.112  1   34.12 ? 134 TRP   B CE3 1 
ATOM   4054 C  CZ2 . TRP   B 1 149 ? -35.126 -1.846  -4.411  1   35.37 ? 134 TRP   B CZ2 1 
ATOM   4055 C  CZ3 . TRP   B 1 149 ? -36.18  -3.933  -3.793  1   35.29 ? 134 TRP   B CZ3 1 
ATOM   4056 C  CH2 . TRP   B 1 149 ? -35.588 -2.715  -3.453  1   35.49 ? 134 TRP   B CH2 1 
ATOM   4057 N  N   . LYS   B 1 150 ? -39.036 -5.374  -6.955  1   33.23 ? 135 LYS   B N   1 
ATOM   4058 C  CA  . LYS   B 1 150 ? -39.836 -5.429  -5.735  1   35.49 ? 135 LYS   B CA  1 
ATOM   4059 C  C   . LYS   B 1 150 ? -39.365 -6.589  -4.869  1   37.22 ? 135 LYS   B C   1 
ATOM   4060 O  O   . LYS   B 1 150 ? -38.713 -7.532  -5.344  1   37.52 ? 135 LYS   B O   1 
ATOM   4061 C  CB  . LYS   B 1 150 ? -41.349 -5.601  -6.061  1   37.28 ? 135 LYS   B CB  1 
ATOM   4062 C  CG  . LYS   B 1 150 ? -41.681 -6.952  -6.701  1   43.03 ? 135 LYS   B CG  1 
ATOM   4063 C  CD  . LYS   B 1 150 ? -43.146 -7.057  -7.114  1   51.02 ? 135 LYS   B CD  1 
ATOM   4064 C  CE  . LYS   B 1 150 ? -43.352 -8.174  -8.112  1   57.92 ? 135 LYS   B CE  1 
ATOM   4065 N  NZ  . LYS   B 1 150 ? -44.354 -7.812  -9.163  1   62.75 ? 135 LYS   B NZ  1 
ATOM   4066 N  N   . LYS   B 1 151 ? -39.707 -6.527  -3.587  1   38.13 ? 136 LYS   B N   1 
ATOM   4067 C  CA  . LYS   B 1 151 ? -39.494 -7.647  -2.689  1   39.39 ? 136 LYS   B CA  1 
ATOM   4068 C  C   . LYS   B 1 151 ? -40.812 -8.445  -2.73   1   40.43 ? 136 LYS   B C   1 
ATOM   4069 O  O   . LYS   B 1 151 ? -41.888 -7.848  -2.765  1   41.28 ? 136 LYS   B O   1 
ATOM   4070 C  CB  . LYS   B 1 151 ? -39.292 -7.157  -1.244  1   41.74 ? 136 LYS   B CB  1 
ATOM   4071 C  CG  . LYS   B 1 151 ? -37.87  -6.792  -0.874  1   45.05 ? 136 LYS   B CG  1 
ATOM   4072 C  CD  . LYS   B 1 151 ? -37.802 -6.498  0.615   1   49.72 ? 136 LYS   B CD  1 
ATOM   4073 C  CE  . LYS   B 1 151 ? -36.405 -6.176  1.076   1   53.77 ? 136 LYS   B CE  1 
ATOM   4074 N  NZ  . LYS   B 1 151 ? -36.302 -6.228  2.558   1   55.58 ? 136 LYS   B NZ  1 
ATOM   4075 N  N   . LYS   B 1 152 ? -40.737 -9.766  -2.734  1   41.21 ? 137 LYS   B N   1 
ATOM   4076 C  CA  . LYS   B 1 152 ? -41.937 -10.61  -2.655  1   42.63 ? 137 LYS   B CA  1 
ATOM   4077 C  C   . LYS   B 1 152 ? -42.489 -10.473 -1.218  1   45.12 ? 137 LYS   B C   1 
ATOM   4078 O  O   . LYS   B 1 152 ? -43.683 -10.24  -1.033  1   45.79 ? 137 LYS   B O   1 
ATOM   4079 C  CB  . LYS   B 1 152 ? -41.594 -12.081 -2.944  1   42.62 ? 137 LYS   B CB  1 
ATOM   4080 C  CG  . LYS   B 1 152 ? -41.229 -12.362 -4.389  1   44.29 ? 137 LYS   B CG  1 
ATOM   4081 C  CD  . LYS   B 1 152 ? -40.723 -13.778 -4.522  1   46.75 ? 137 LYS   B CD  1 
ATOM   4082 C  CE  . LYS   B 1 152 ? -40.413 -14.136 -5.944  1   49.18 ? 137 LYS   B CE  1 
ATOM   4083 N  NZ  . LYS   B 1 152 ? -39.666 -15.414 -5.993  1   51.08 ? 137 LYS   B NZ  1 
ATOM   4084 N  N   . ASP   B 1 153 ? -41.597 -10.555 -0.215  1   46.27 ? 138 ASP   B N   1 
ATOM   4085 C  CA  . ASP   B 1 153 ? -41.918 -10.422 1.2     1   47.99 ? 138 ASP   B CA  1 
ATOM   4086 C  C   . ASP   B 1 153 ? -41.063 -9.291  1.8     1   49.1  ? 138 ASP   B C   1 
ATOM   4087 O  O   . ASP   B 1 153 ? -39.854 -9.447  1.946   1   48.83 ? 138 ASP   B O   1 
ATOM   4088 C  CB  . ASP   B 1 153 ? -41.632 -11.753 1.921   1   50.07 ? 138 ASP   B CB  1 
ATOM   4089 C  CG  . ASP   B 1 153 ? -42.066 -11.802 3.378   1   55.82 ? 138 ASP   B CG  1 
ATOM   4090 O  OD1 . ASP   B 1 153 ? -42.468 -10.744 3.918   1   55.62 ? 138 ASP   B OD1 1 
ATOM   4091 O  OD2 . ASP   B 1 153 ? -42.003 -12.9   3.98    1   59.68 ? 138 ASP   B OD2 1 
ATOM   4092 N  N   . PRO   B 1 154 ? -41.699 -8.184  2.216   1   50.31 ? 139 PRO   B N   1 
ATOM   4093 C  CA  . PRO   B 1 154 ? -40.945 -7.054  2.797   1   51.2  ? 139 PRO   B CA  1 
ATOM   4094 C  C   . PRO   B 1 154 ? -40.151 -7.363  4.066   1   52.68 ? 139 PRO   B C   1 
ATOM   4095 O  O   . PRO   B 1 154 ? -39.177 -6.668  4.369   1   53.09 ? 139 PRO   B O   1 
ATOM   4096 C  CB  . PRO   B 1 154 ? -42.028 -6.006  3.082   1   51.65 ? 139 PRO   B CB  1 
ATOM   4097 C  CG  . PRO   B 1 154 ? -43.181 -6.384  2.223   1   51.96 ? 139 PRO   B CG  1 
ATOM   4098 C  CD  . PRO   B 1 154 ? -43.139 -7.88   2.116   1   50.3  ? 139 PRO   B CD  1 
ATOM   4099 N  N   . ASN   B 1 155 ? -40.547 -8.4    4.805   1   53.05 ? 140 ASN   B N   1 
ATOM   4100 C  CA  . ASN   B 1 155 ? -39.83  -8.778  6.029   1   53.81 ? 140 ASN   B CA  1 
ATOM   4101 C  C   . ASN   B 1 155 ? -38.61  -9.677  5.777   1   53.17 ? 140 ASN   B C   1 
ATOM   4102 O  O   . ASN   B 1 155 ? -37.891 -10.017 6.72    1   53.94 ? 140 ASN   B O   1 
ATOM   4103 C  CB  . ASN   B 1 155 ? -40.792 -9.41   7.048   1   56.23 ? 140 ASN   B CB  1 
ATOM   4104 C  CG  . ASN   B 1 155 ? -41.99  -8.533  7.321   1   61.14 ? 140 ASN   B CG  1 
ATOM   4105 O  OD1 . ASN   B 1 155 ? -41.861 -7.36   7.706   1   62.83 ? 140 ASN   B OD1 1 
ATOM   4106 N  ND2 . ASN   B 1 155 ? -43.182 -9.071  7.091   1   61.95 ? 140 ASN   B ND2 1 
ATOM   4107 N  N   . LYS   B 1 156 ? -38.361 -10.049 4.512   1   51.58 ? 141 LYS   B N   1 
ATOM   4108 C  CA  . LYS   B 1 156 ? -37.23  -10.878 4.138   1   50.66 ? 141 LYS   B CA  1 
ATOM   4109 C  C   . LYS   B 1 156 ? -36.161 -10.051 3.389   1   48.93 ? 141 LYS   B C   1 
ATOM   4110 O  O   . LYS   B 1 156 ? -36.47  -9.005  2.817   1   48.45 ? 141 LYS   B O   1 
ATOM   4111 C  CB  . LYS   B 1 156 ? -37.716 -12.094 3.347   1   52.94 ? 141 LYS   B CB  1 
ATOM   4112 C  CG  . LYS   B 1 156 ? -38.501 -13.065 4.221   1   58.12 ? 141 LYS   B CG  1 
ATOM   4113 C  CD  . LYS   B 1 156 ? -38.933 -14.304 3.449   1   63.25 ? 141 LYS   B CD  1 
ATOM   4114 C  CE  . LYS   B 1 156 ? -39.575 -15.346 4.336   1   66.92 ? 141 LYS   B CE  1 
ATOM   4115 N  NZ  . LYS   B 1 156 ? -39.766 -16.636 3.616   1   68.71 ? 141 LYS   B NZ  1 
ATOM   4116 N  N   . PRO   B 1 157 ? -34.891 -10.48  3.434   1   47.94 ? 142 PRO   B N   1 
ATOM   4117 C  CA  . PRO   B 1 157 ? -33.819 -9.676  2.829   1   47.19 ? 142 PRO   B CA  1 
ATOM   4118 C  C   . PRO   B 1 157 ? -33.829 -9.522  1.293   1   46.12 ? 142 PRO   B C   1 
ATOM   4119 O  O   . PRO   B 1 157 ? -34.657 -10.102 0.578   1   45.78 ? 142 PRO   B O   1 
ATOM   4120 C  CB  . PRO   B 1 157 ? -32.55  -10.383 3.313   1   48.12 ? 142 PRO   B CB  1 
ATOM   4121 C  CG  . PRO   B 1 157 ? -32.974 -11.791 3.556   1   48.99 ? 142 PRO   B CG  1 
ATOM   4122 C  CD  . PRO   B 1 157 ? -34.348 -11.669 4.12    1   47.45 ? 142 PRO   B CD  1 
ATOM   4123 N  N   . LEU   B 1 158 ? -32.894 -8.693  0.789   1   44.81 ? 143 LEU   B N   1 
ATOM   4124 C  CA  . LEU   B 1 158 ? -32.734 -8.451  -0.629  1   43.7  ? 143 LEU   B CA  1 
ATOM   4125 C  C   . LEU   B 1 158 ? -31.905 -9.553  -1.243  1   42.36 ? 143 LEU   B C   1 
ATOM   4126 O  O   . LEU   B 1 158 ? -30.697 -9.397  -1.446  1   42.51 ? 143 LEU   B O   1 
ATOM   4127 C  CB  . LEU   B 1 158 ? -32.061 -7.101  -0.856  1   43.93 ? 143 LEU   B CB  1 
ATOM   4128 C  CG  . LEU   B 1 158 ? -32.919 -5.889  -0.619  1   45.27 ? 143 LEU   B CG  1 
ATOM   4129 C  CD1 . LEU   B 1 158 ? -32.056 -4.653  -0.493  1   46.3  ? 143 LEU   B CD1 1 
ATOM   4130 C  CD2 . LEU   B 1 158 ? -33.934 -5.727  -1.724  1   45.35 ? 143 LEU   B CD2 1 
ATOM   4131 N  N   . THR   B 1 159 ? -32.543 -10.698 -1.501  1   40.42 ? 144 THR   B N   1 
ATOM   4132 C  CA  . THR   B 1 159 ? -31.911 -11.842 -2.157  1   39.16 ? 144 THR   B CA  1 
ATOM   4133 C  C   . THR   B 1 159 ? -32.716 -12.14  -3.419  1   37.93 ? 144 THR   B C   1 
ATOM   4134 O  O   . THR   B 1 159 ? -33.878 -11.76  -3.504  1   37.99 ? 144 THR   B O   1 
ATOM   4135 C  CB  . THR   B 1 159 ? -31.906 -13.071 -1.237  1   40.65 ? 144 THR   B CB  1 
ATOM   4136 O  OG1 . THR   B 1 159 ? -33.26  -13.456 -0.977  1   41.55 ? 144 THR   B OG1 1 
ATOM   4137 C  CG2 . THR   B 1 159 ? -31.189 -12.813 0.067   1   41.31 ? 144 THR   B CG2 1 
ATOM   4138 N  N   . TYR   B 1 160 ? -32.138 -12.882 -4.367  1   36.99 ? 145 TYR   B N   1 
ATOM   4139 C  CA  . TYR   B 1 160 ? -32.825 -13.246 -5.604  1   36.42 ? 145 TYR   B CA  1 
ATOM   4140 C  C   . TYR   B 1 160 ? -34.149 -13.968 -5.326  1   37.02 ? 145 TYR   B C   1 
ATOM   4141 O  O   . TYR   B 1 160 ? -35.166 -13.619 -5.917  1   36.39 ? 145 TYR   B O   1 
ATOM   4142 C  CB  . TYR   B 1 160 ? -31.93  -14.129 -6.476  1   35.78 ? 145 TYR   B CB  1 
ATOM   4143 C  CG  . TYR   B 1 160 ? -32.51  -14.315 -7.859  1   36.1  ? 145 TYR   B CG  1 
ATOM   4144 C  CD1 . TYR   B 1 160 ? -33.397 -15.352 -8.131  1   36.37 ? 145 TYR   B CD1 1 
ATOM   4145 C  CD2 . TYR   B 1 160 ? -32.193 -13.442 -8.889  1   36.68 ? 145 TYR   B CD2 1 
ATOM   4146 C  CE1 . TYR   B 1 160 ? -33.987 -15.485 -9.38   1   37.41 ? 145 TYR   B CE1 1 
ATOM   4147 C  CE2 . TYR   B 1 160 ? -32.722 -13.606 -10.161 1   37.53 ? 145 TYR   B CE2 1 
ATOM   4148 C  CZ  . TYR   B 1 160 ? -33.612 -14.637 -10.406 1   38.5  ? 145 TYR   B CZ  1 
ATOM   4149 O  OH  . TYR   B 1 160 ? -34.146 -14.79  -11.657 1   39.23 ? 145 TYR   B OH  1 
ATOM   4150 N  N   . GLU   B 1 161 ? -34.135 -14.9   -4.369  1   37.81 ? 146 GLU   B N   1 
ATOM   4151 C  CA  . GLU   B 1 161 ? -35.304 -15.692 -3.968  1   39.39 ? 146 GLU   B CA  1 
ATOM   4152 C  C   . GLU   B 1 161 ? -36.455 -14.832 -3.506  1   39.56 ? 146 GLU   B C   1 
ATOM   4153 O  O   . GLU   B 1 161 ? -37.61  -15.162 -3.764  1   40.22 ? 146 GLU   B O   1 
ATOM   4154 C  CB  . GLU   B 1 161 ? -34.912 -16.69  -2.857  1   43.15 ? 146 GLU   B CB  1 
ATOM   4155 C  CG  . GLU   B 1 161 ? -34.308 -17.983 -3.373  1   51.27 ? 146 GLU   B CG  1 
ATOM   4156 C  CD  . GLU   B 1 161 ? -33.152 -17.845 -4.348  1   62.05 ? 146 GLU   B CD  1 
ATOM   4157 O  OE1 . GLU   B 1 161 ? -32.144 -17.186 -3.995  1   63.31 ? 146 GLU   B OE1 1 
ATOM   4158 O  OE2 . GLU   B 1 161 ? -33.262 -18.391 -5.472  1   65.87 ? 146 GLU   B OE2 1 
ATOM   4159 N  N   . ASN   B 1 162 ? -36.152 -13.723 -2.833  1   39.12 ? 147 ASN   B N   1 
ATOM   4160 C  CA  . ASN   B 1 162 ? -37.189 -12.833 -2.331  1   38.93 ? 147 ASN   B CA  1 
ATOM   4161 C  C   . ASN   B 1 162 ? -37.438 -11.632 -3.257  1   38.18 ? 147 ASN   B C   1 
ATOM   4162 O  O   . ASN   B 1 162 ? -38.024 -10.645 -2.814  1   39.02 ? 147 ASN   B O   1 
ATOM   4163 C  CB  . ASN   B 1 162 ? -36.846 -12.362 -0.916  1   40.11 ? 147 ASN   B CB  1 
ATOM   4164 C  CG  . ASN   B 1 162 ? -37.99  -11.639 -0.285  1   43.29 ? 147 ASN   B CG  1 
ATOM   4165 O  OD1 . ASN   B 1 162 ? -39.139 -12.051 -0.414  1   45.41 ? 147 ASN   B OD1 1 
ATOM   4166 N  ND2 . ASN   B 1 162 ? -37.728 -10.5   0.324   1   43.95 ? 147 ASN   B ND2 1 
ATOM   4167 N  N   . MET   B 1 163 ? -37.029 -11.705 -4.537  1   36.47 ? 148 MET   B N   1 
ATOM   4168 C  CA  . MET   B 1 163 ? -37.221 -10.556 -5.422  1   36.18 ? 148 MET   B CA  1 
ATOM   4169 C  C   . MET   B 1 163 ? -37.866 -10.896 -6.753  1   35.37 ? 148 MET   B C   1 
ATOM   4170 O  O   . MET   B 1 163 ? -37.838 -12.049 -7.183  1   35.64 ? 148 MET   B O   1 
ATOM   4171 C  CB  . MET   B 1 163 ? -35.879 -9.825  -5.63   1   36.59 ? 148 MET   B CB  1 
ATOM   4172 C  CG  . MET   B 1 163 ? -35.358 -9.151  -4.363  1   38.79 ? 148 MET   B CG  1 
ATOM   4173 S  SD  . MET   B 1 163 ? -33.617 -8.682  -4.497  1   41.78 ? 148 MET   B SD  1 
ATOM   4174 C  CE  . MET   B 1 163 ? -33.808 -7.075  -5.232  1   36.89 ? 148 MET   B CE  1 
ATOM   4175 N  N   . ASP   B 1 164 ? -38.419 -9.875  -7.414  1   34.25 ? 149 ASP   B N   1 
ATOM   4176 C  CA  . ASP   B 1 164 ? -38.95  -10.01  -8.748  1   34.27 ? 149 ASP   B CA  1 
ATOM   4177 C  C   . ASP   B 1 164 ? -38.836 -8.683  -9.498  1   33.45 ? 149 ASP   B C   1 
ATOM   4178 O  O   . ASP   B 1 164 ? -38.648 -7.628  -8.888  1   33.47 ? 149 ASP   B O   1 
ATOM   4179 C  CB  . ASP   B 1 164 ? -40.407 -10.486 -8.72   1   36.76 ? 149 ASP   B CB  1 
ATOM   4180 C  CG  . ASP   B 1 164 ? -40.715 -11.447 -9.855  1   43.73 ? 149 ASP   B CG  1 
ATOM   4181 O  OD1 . ASP   B 1 164 ? -40.144 -11.271 -10.963 1   43.51 ? 149 ASP   B OD1 1 
ATOM   4182 O  OD2 . ASP   B 1 164 ? -41.505 -12.381 -9.637  1   47.74 ? 149 ASP   B OD2 1 
ATOM   4183 N  N   . VAL   B 1 165 ? -38.936 -8.732  -10.83  1   32.11 ? 150 VAL   B N   1 
ATOM   4184 C  CA  . VAL   B 1 165 ? -38.956 -7.52   -11.639 1   31.43 ? 150 VAL   B CA  1 
ATOM   4185 C  C   . VAL   B 1 165 ? -40.412 -7.079  -11.771 1   30.85 ? 150 VAL   B C   1 
ATOM   4186 O  O   . VAL   B 1 165 ? -41.328 -7.871  -11.511 1   31.32 ? 150 VAL   B O   1 
ATOM   4187 C  CB  . VAL   B 1 165 ? -38.298 -7.723  -13.033 1   32.2  ? 150 VAL   B CB  1 
ATOM   4188 C  CG1 . VAL   B 1 165 ? -36.832 -8.078  -12.891 1   32.41 ? 150 VAL   B CG1 1 
ATOM   4189 C  CG2 . VAL   B 1 165 ? -39.044 -8.798  -13.845 1   33.41 ? 150 VAL   B CG2 1 
ATOM   4190 N  N   . LEU   B 1 166 ? -40.638 -5.827  -12.169 1   29.61 ? 151 LEU   B N   1 
ATOM   4191 C  CA  . LEU   B 1 166 ? -41.986 -5.341  -12.39  1   29.17 ? 151 LEU   B CA  1 
ATOM   4192 C  C   . LEU   B 1 166 ? -42.444 -5.641  -13.822 1   30.68 ? 151 LEU   B C   1 
ATOM   4193 O  O   . LEU   B 1 166 ? -43.615 -5.958  -14.024 1   31.28 ? 151 LEU   B O   1 
ATOM   4194 C  CB  . LEU   B 1 166 ? -42.103 -3.843  -12.065 1   27.91 ? 151 LEU   B CB  1 
ATOM   4195 C  CG  . LEU   B 1 166 ? -41.638 -3.435  -10.638 1   28.41 ? 151 LEU   B CG  1 
ATOM   4196 C  CD1 . LEU   B 1 166 ? -41.797 -1.939  -10.421 1   27.2  ? 151 LEU   B CD1 1 
ATOM   4197 C  CD2 . LEU   B 1 166 ? -42.437 -4.189  -9.562  1   29.13 ? 151 LEU   B CD2 1 
ATOM   4198 N  N   . PHE   B 1 167 ? -41.55  -5.495  -14.832 1   30.47 ? 152 PHE   B N   1 
ATOM   4199 C  CA  . PHE   B 1 167 ? -41.929 -5.701  -16.227 1   30.78 ? 152 PHE   B CA  1 
ATOM   4200 C  C   . PHE   B 1 167 ? -40.915 -6.539  -17.011 1   31.38 ? 152 PHE   B C   1 
ATOM   4201 O  O   . PHE   B 1 167 ? -39.697 -6.398  -16.825 1   31.39 ? 152 PHE   B O   1 
ATOM   4202 C  CB  . PHE   B 1 167 ? -42.116 -4.361  -16.958 1   31.02 ? 152 PHE   B CB  1 
ATOM   4203 C  CG  . PHE   B 1 167 ? -43.047 -3.408  -16.248 1   31.98 ? 152 PHE   B CG  1 
ATOM   4204 C  CD1 . PHE   B 1 167 ? -44.424 -3.495  -16.423 1   33.17 ? 152 PHE   B CD1 1 
ATOM   4205 C  CD2 . PHE   B 1 167 ? -42.552 -2.455  -15.37  1   32.4  ? 152 PHE   B CD2 1 
ATOM   4206 C  CE1 . PHE   B 1 167 ? -45.285 -2.639  -15.728 1   33.85 ? 152 PHE   B CE1 1 
ATOM   4207 C  CE2 . PHE   B 1 167 ? -43.411 -1.601  -14.678 1   33.07 ? 152 PHE   B CE2 1 
ATOM   4208 C  CZ  . PHE   B 1 167 ? -44.775 -1.697  -14.862 1   33.58 ? 152 PHE   B CZ  1 
ATOM   4209 N  N   . SER   B 1 168 ? -41.439 -7.376  -17.922 1   30.31 ? 153 SER   B N   1 
ATOM   4210 C  CA  . SER   B 1 168 ? -40.691 -8.199  -18.865 1   29.75 ? 153 SER   B CA  1 
ATOM   4211 C  C   . SER   B 1 168 ? -41.206 -7.903  -20.279 1   28.36 ? 153 SER   B C   1 
ATOM   4212 O  O   . SER   B 1 168 ? -42.262 -7.275  -20.433 1   28.25 ? 153 SER   B O   1 
ATOM   4213 C  CB  . SER   B 1 168 ? -40.89  -9.673  -18.544 1   31.97 ? 153 SER   B CB  1 
ATOM   4214 O  OG  . SER   B 1 168 ? -40.293 -9.94   -17.289 1   35.82 ? 153 SER   B OG  1 
ATOM   4215 N  N   . PHE   B 1 169 ? -40.465 -8.328  -21.315 1   27.1  ? 154 PHE   B N   1 
ATOM   4216 C  CA  . PHE   B 1 169 ? -40.883 -8.065  -22.684 1   26.59 ? 154 PHE   B CA  1 
ATOM   4217 C  C   . PHE   B 1 169 ? -41.578 -9.285  -23.307 1   27.18 ? 154 PHE   B C   1 
ATOM   4218 O  O   . PHE   B 1 169 ? -42.618 -9.138  -23.931 1   28.26 ? 154 PHE   B O   1 
ATOM   4219 C  CB  . PHE   B 1 169 ? -39.681 -7.618  -23.54  1   25.74 ? 154 PHE   B CB  1 
ATOM   4220 C  CG  . PHE   B 1 169 ? -39.147 -6.273  -23.134 1   25.84 ? 154 PHE   B CG  1 
ATOM   4221 C  CD1 . PHE   B 1 169 ? -39.773 -5.11   -23.546 1   26.09 ? 154 PHE   B CD1 1 
ATOM   4222 C  CD2 . PHE   B 1 169 ? -38.048 -6.168  -22.284 1   26.11 ? 154 PHE   B CD2 1 
ATOM   4223 C  CE1 . PHE   B 1 169 ? -39.29  -3.869  -23.159 1   26.9  ? 154 PHE   B CE1 1 
ATOM   4224 C  CE2 . PHE   B 1 169 ? -37.583 -4.932  -21.882 1   26.38 ? 154 PHE   B CE2 1 
ATOM   4225 C  CZ  . PHE   B 1 169 ? -38.198 -3.786  -22.32  1   26.88 ? 154 PHE   B CZ  1 
ATOM   4226 N  N   . ARG   B 1 170 ? -40.984 -10.468 -23.184 1   27.12 ? 155 ARG   B N   1 
ATOM   4227 C  CA  . ARG   B 1 170 ? -41.516 -11.699 -23.786 1   27.83 ? 155 ARG   B CA  1 
ATOM   4228 C  C   . ARG   B 1 170 ? -41.373 -12.844 -22.814 1   28.79 ? 155 ARG   B C   1 
ATOM   4229 O  O   . ARG   B 1 170 ? -40.484 -12.833 -21.94  1   28.26 ? 155 ARG   B O   1 
ATOM   4230 C  CB  . ARG   B 1 170 ? -40.701 -12.105 -25.049 1   28.19 ? 155 ARG   B CB  1 
ATOM   4231 C  CG  . ARG   B 1 170 ? -40.548 -11.029 -26.11  1   31.07 ? 155 ARG   B CG  1 
ATOM   4232 C  CD  . ARG   B 1 170 ? -41.872 -10.636 -26.743 1   33.24 ? 155 ARG   B CD  1 
ATOM   4233 N  NE  . ARG   B 1 170 ? -42.489 -11.781 -27.416 1   33.33 ? 155 ARG   B NE  1 
ATOM   4234 C  CZ  . ARG   B 1 170 ? -42.235 -12.136 -28.669 1   35.93 ? 155 ARG   B CZ  1 
ATOM   4235 N  NH1 . ARG   B 1 170 ? -41.396 -11.424 -29.413 1   35.37 ? 155 ARG   B NH1 1 
ATOM   4236 N  NH2 . ARG   B 1 170 ? -42.827 -13.199 -29.195 1   37.44 ? 155 ARG   B NH2 1 
ATOM   4237 N  N   . ASP   B 1 171 ? -42.222 -13.873 -22.982 1   28.87 ? 156 ASP   B N   1 
ATOM   4238 C  CA  A ASP   B 1 171 ? -42.106 -15.037 -22.11  0.5 29.17 ? 156 ASP   B CA  1 
ATOM   4239 C  CA  B ASP   B 1 171 ? -42.173 -15.102 -22.194 0.5 29.71 ? 156 ASP   B CA  1 
ATOM   4240 C  C   . ASP   B 1 171 ? -40.82  -15.783 -22.457 1   29.27 ? 156 ASP   B C   1 
ATOM   4241 O  O   . ASP   B 1 171 ? -40.434 -15.89  -23.614 1   30.03 ? 156 ASP   B O   1 
ATOM   4242 C  CB  A ASP   B 1 171 ? -43.378 -15.915 -22.13  0.5 30.83 ? 156 ASP   B CB  1 
ATOM   4243 C  CB  B ASP   B 1 171 ? -43.313 -16.026 -22.691 0.5 32.82 ? 156 ASP   B CB  1 
ATOM   4244 C  CG  A ASP   B 1 171 ? -44.597 -15.163 -21.62  0.5 33.75 ? 156 ASP   B CG  1 
ATOM   4245 C  CG  B ASP   B 1 171 ? -43.627 -17.18  -21.771 0.5 39.73 ? 156 ASP   B CG  1 
ATOM   4246 O  OD1 A ASP   B 1 171 ? -44.571 -14.701 -20.454 0.5 32.45 ? 156 ASP   B OD1 1 
ATOM   4247 O  OD1 B ASP   B 1 171 ? -43.578 -16.985 -20.539 0.5 40.46 ? 156 ASP   B OD1 1 
ATOM   4248 O  OD2 A ASP   B 1 171 ? -45.559 -15.013 -22.39  0.5 36.93 ? 156 ASP   B OD2 1 
ATOM   4249 O  OD2 B ASP   B 1 171 ? -43.949 -18.277 -22.283 0.5 43.69 ? 156 ASP   B OD2 1 
ATOM   4250 N  N   . GLY   B 1 172 ? -40.09  -16.179 -21.427 1   28.45 ? 157 GLY   B N   1 
ATOM   4251 C  CA  . GLY   B 1 172 ? -38.799 -16.843 -21.609 1   28.03 ? 157 GLY   B CA  1 
ATOM   4252 C  C   . GLY   B 1 172 ? -37.656 -15.917 -22.036 1   26.63 ? 157 GLY   B C   1 
ATOM   4253 O  O   . GLY   B 1 172 ? -36.629 -16.391 -22.521 1   26.67 ? 157 GLY   B O   1 
ATOM   4254 N  N   . ASP   B 1 173 ? -37.803 -14.598 -21.857 1   25.47 ? 158 ASP   B N   1 
ATOM   4255 C  CA  . ASP   B 1 173 ? -36.715 -13.66  -22.231 1   23.7  ? 158 ASP   B CA  1 
ATOM   4256 C  C   . ASP   B 1 173 ? -35.575 -13.583 -21.195 1   24.76 ? 158 ASP   B C   1 
ATOM   4257 O  O   . ASP   B 1 173 ? -34.589 -12.89  -21.452 1   25.53 ? 158 ASP   B O   1 
ATOM   4258 C  CB  . ASP   B 1 173 ? -37.241 -12.238 -22.569 1   22.58 ? 158 ASP   B CB  1 
ATOM   4259 C  CG  . ASP   B 1 173 ? -37.916 -11.465 -21.457 1   23.32 ? 158 ASP   B CG  1 
ATOM   4260 O  OD1 . ASP   B 1 173 ? -37.961 -11.978 -20.322 1   23.49 ? 158 ASP   B OD1 1 
ATOM   4261 O  OD2 . ASP   B 1 173 ? -38.455 -10.359 -21.739 1   24.31 ? 158 ASP   B OD2 1 
ATOM   4262 N  N   . CYS   B 1 174 ? -35.734 -14.19  -20.014 1   24.6  ? 159 CYS   B N   1 
ATOM   4263 C  CA  . CYS   B 1 174 ? -34.733 -14.113 -18.934 1   26.23 ? 159 CYS   B CA  1 
ATOM   4264 C  C   . CYS   B 1 174 ? -34.492 -12.673 -18.424 1   26.32 ? 159 CYS   B C   1 
ATOM   4265 O  O   . CYS   B 1 174 ? -33.448 -12.397 -17.827 1   26.18 ? 159 CYS   B O   1 
ATOM   4266 C  CB  . CYS   B 1 174 ? -33.432 -14.798 -19.331 1   28.43 ? 159 CYS   B CB  1 
ATOM   4267 S  SG  . CYS   B 1 174 ? -33.583 -16.581 -19.584 1   33.96 ? 159 CYS   B SG  1 
ATOM   4268 N  N   . SER   B 1 175 ? -35.465 -11.767 -18.643 1   26.17 ? 160 SER   B N   1 
ATOM   4269 C  CA  . SER   B 1 175 ? -35.354 -10.401 -18.169 1   26.84 ? 160 SER   B CA  1 
ATOM   4270 C  C   . SER   B 1 175 ? -35.302 -10.355 -16.659 1   27.71 ? 160 SER   B C   1 
ATOM   4271 O  O   . SER   B 1 175 ? -34.554 -9.553  -16.124 1   27.52 ? 160 SER   B O   1 
ATOM   4272 C  CB  . SER   B 1 175 ? -36.475 -9.52   -18.704 1   28.74 ? 160 SER   B CB  1 
ATOM   4273 O  OG  . SER   B 1 175 ? -37.724 -9.975  -18.227 1   32.27 ? 160 SER   B OG  1 
ATOM   4274 N  N   . LYS   B 1 176 ? -35.997 -11.291 -15.954 1   27.47 ? 161 LYS   B N   1 
ATOM   4275 C  CA  . LYS   B 1 176 ? -35.936 -11.301 -14.501 1   26.69 ? 161 LYS   B CA  1 
ATOM   4276 C  C   . LYS   B 1 176 ? -34.497 -11.578 -14.021 1   25.53 ? 161 LYS   B C   1 
ATOM   4277 O  O   . LYS   B 1 176 ? -33.955 -10.793 -13.253 1   25.27 ? 161 LYS   B O   1 
ATOM   4278 C  CB  . LYS   B 1 176 ? -36.94  -12.292 -13.895 1   27.66 ? 161 LYS   B CB  1 
ATOM   4279 C  CG  . LYS   B 1 176 ? -36.839 -12.366 -12.389 1   32.33 ? 161 LYS   B CG  1 
ATOM   4280 C  CD  . LYS   B 1 176 ? -37.675 -13.516 -11.791 1   36.23 ? 161 LYS   B CD  1 
ATOM   4281 C  CE  . LYS   B 1 176 ? -37.321 -13.709 -10.345 1   40.23 ? 161 LYS   B CE  1 
ATOM   4282 N  NZ  . LYS   B 1 176 ? -38.384 -14.446 -9.602  1   43    ? 161 LYS   B NZ  1 
ATOM   4283 N  N   . GLY   B 1 177 ? -33.89  -12.647 -14.517 1   24.4  ? 162 GLY   B N   1 
ATOM   4284 C  CA  . GLY   B 1 177 ? -32.526 -13.013 -14.165 1   24.3  ? 162 GLY   B CA  1 
ATOM   4285 C  C   . GLY   B 1 177 ? -31.508 -11.946 -14.536 1   24.49 ? 162 GLY   B C   1 
ATOM   4286 O  O   . GLY   B 1 177 ? -30.632 -11.625 -13.732 1   24.04 ? 162 GLY   B O   1 
ATOM   4287 N  N   . PHE   B 1 178 ? -31.62  -11.377 -15.749 1   23.65 ? 163 PHE   B N   1 
ATOM   4288 C  CA  . PHE   B 1 178 ? -30.643 -10.377 -16.199 1   23.95 ? 163 PHE   B CA  1 
ATOM   4289 C  C   . PHE   B 1 178 ? -30.753 -9.065  -15.401 1   24.19 ? 163 PHE   B C   1 
ATOM   4290 O  O   . PHE   B 1 178 ? -29.743 -8.563  -14.888 1   24    ? 163 PHE   B O   1 
ATOM   4291 C  CB  . PHE   B 1 178 ? -30.834 -10.133 -17.69  1   23.7  ? 163 PHE   B CB  1 
ATOM   4292 C  CG  . PHE   B 1 178 ? -29.892 -9.128  -18.312 1   23.9  ? 163 PHE   B CG  1 
ATOM   4293 C  CD1 . PHE   B 1 178 ? -28.531 -9.373  -18.36  1   24.86 ? 163 PHE   B CD1 1 
ATOM   4294 C  CD2 . PHE   B 1 178 ? -30.378 -7.956  -18.882 1   23.97 ? 163 PHE   B CD2 1 
ATOM   4295 C  CE1 . PHE   B 1 178 ? -27.664 -8.469  -18.98  1   25.04 ? 163 PHE   B CE1 1 
ATOM   4296 C  CE2 . PHE   B 1 178 ? -29.519 -7.065  -19.522 1   24.3  ? 163 PHE   B CE2 1 
ATOM   4297 C  CZ  . PHE   B 1 178 ? -28.168 -7.325  -19.562 1   24.11 ? 163 PHE   B CZ  1 
ATOM   4298 N  N   . PHE   B 1 179 ? -31.974 -8.523  -15.272 1   23.65 ? 164 PHE   B N   1 
ATOM   4299 C  CA  . PHE   B 1 179 ? -32.168 -7.269  -14.549 1   23.71 ? 164 PHE   B CA  1 
ATOM   4300 C  C   . PHE   B 1 179 ? -31.857 -7.43   -13.069 1   24.41 ? 164 PHE   B C   1 
ATOM   4301 O  O   . PHE   B 1 179 ? -31.186 -6.576  -12.482 1   22.86 ? 164 PHE   B O   1 
ATOM   4302 C  CB  . PHE   B 1 179 ? -33.57  -6.694  -14.76  1   22.67 ? 164 PHE   B CB  1 
ATOM   4303 C  CG  . PHE   B 1 179 ? -33.911 -6.316  -16.185 1   23.8  ? 164 PHE   B CG  1 
ATOM   4304 C  CD1 . PHE   B 1 179 ? -32.914 -5.972  -17.09  1   23.82 ? 164 PHE   B CD1 1 
ATOM   4305 C  CD2 . PHE   B 1 179 ? -35.226 -6.301  -16.62  1   24.98 ? 164 PHE   B CD2 1 
ATOM   4306 C  CE1 . PHE   B 1 179 ? -33.229 -5.614  -18.397 1   24.83 ? 164 PHE   B CE1 1 
ATOM   4307 C  CE2 . PHE   B 1 179 ? -35.545 -5.927  -17.924 1   25.56 ? 164 PHE   B CE2 1 
ATOM   4308 C  CZ  . PHE   B 1 179 ? -34.542 -5.602  -18.813 1   25.14 ? 164 PHE   B CZ  1 
ATOM   4309 N  N   . LEU   B 1 180 ? -32.361 -8.523  -12.459 1   24.76 ? 165 LEU   B N   1 
ATOM   4310 C  CA  . LEU   B 1 180 ? -32.161 -8.773  -11.039 1   25.87 ? 165 LEU   B CA  1 
ATOM   4311 C  C   . LEU   B 1 180 ? -30.712 -9.051  -10.628 1   25.67 ? 165 LEU   B C   1 
ATOM   4312 O  O   . LEU   B 1 180 ? -30.298 -8.535  -9.599  1   26.74 ? 165 LEU   B O   1 
ATOM   4313 C  CB  . LEU   B 1 180 ? -33.093 -9.913  -10.574 1   27.29 ? 165 LEU   B CB  1 
ATOM   4314 C  CG  . LEU   B 1 180 ? -34.187 -9.57   -9.546  1   30.25 ? 165 LEU   B CG  1 
ATOM   4315 C  CD1 . LEU   B 1 180 ? -34.894 -8.228  -9.817  1   30.45 ? 165 LEU   B CD1 1 
ATOM   4316 C  CD2 . LEU   B 1 180 ? -35.153 -10.745 -9.359  1   31.46 ? 165 LEU   B CD2 1 
ATOM   4317 N  N   . VAL   B 1 181 ? -29.945 -9.843  -11.396 1   23.78 ? 166 VAL   B N   1 
ATOM   4318 C  CA  . VAL   B 1 181 ? -28.554 -10.106 -11.07  1   23.52 ? 166 VAL   B CA  1 
ATOM   4319 C  C   . VAL   B 1 181 ? -27.709 -8.812  -11.24  1   22.13 ? 166 VAL   B C   1 
ATOM   4320 O  O   . VAL   B 1 181 ? -26.896 -8.494  -10.363 1   21.4  ? 166 VAL   B O   1 
ATOM   4321 C  CB  . VAL   B 1 181 ? -27.983 -11.317 -11.833 1   24.73 ? 166 VAL   B CB  1 
ATOM   4322 C  CG1 . VAL   B 1 181 ? -26.475 -11.467 -11.588 1   24.63 ? 166 VAL   B CG1 1 
ATOM   4323 C  CG2 . VAL   B 1 181 ? -28.721 -12.587 -11.407 1   25.73 ? 166 VAL   B CG2 1 
ATOM   4324 N  N   . SER   B 1 182 ? -28.042 -7.993  -12.253 1   21.42 ? 167 SER   B N   1 
ATOM   4325 C  CA  . SER   B 1 182 ? -27.4   -6.676  -12.439 1   22.44 ? 167 SER   B CA  1 
ATOM   4326 C  C   . SER   B 1 182 ? -27.689 -5.812  -11.189 1   23.18 ? 167 SER   B C   1 
ATOM   4327 O  O   . SER   B 1 182 ? -26.774 -5.197  -10.632 1   23.47 ? 167 SER   B O   1 
ATOM   4328 C  CB  . SER   B 1 182 ? -27.99  -5.961  -13.663 1   23.61 ? 167 SER   B CB  1 
ATOM   4329 O  OG  . SER   B 1 182 ? -27.535 -6.57   -14.851 1   26.44 ? 167 SER   B OG  1 
ATOM   4330 N  N   . LEU   B 1 183 ? -28.954 -5.8    -10.745 1   22.98 ? 168 LEU   B N   1 
ATOM   4331 C  CA  . LEU   B 1 183 ? -29.369 -5.024  -9.585  1   23.28 ? 168 LEU   B CA  1 
ATOM   4332 C  C   . LEU   B 1 183 ? -28.644 -5.534  -8.328  1   24.9  ? 168 LEU   B C   1 
ATOM   4333 O  O   . LEU   B 1 183 ? -28.132 -4.72   -7.56   1   25.18 ? 168 LEU   B O   1 
ATOM   4334 C  CB  . LEU   B 1 183 ? -30.882 -5.108  -9.406  1   22.81 ? 168 LEU   B CB  1 
ATOM   4335 C  CG  . LEU   B 1 183 ? -31.448 -4.468  -8.153  1   23.26 ? 168 LEU   B CG  1 
ATOM   4336 C  CD1 . LEU   B 1 183 ? -31.204 -2.971  -8.141  1   23.06 ? 168 LEU   B CD1 1 
ATOM   4337 C  CD2 . LEU   B 1 183 ? -32.909 -4.84   -7.965  1   22.71 ? 168 LEU   B CD2 1 
ATOM   4338 N  N   . LEU   B 1 184 ? -28.546 -6.851  -8.145  1   25.18 ? 169 LEU   B N   1 
ATOM   4339 C  CA  . LEU   B 1 184 ? -27.879 -7.41   -6.972  1   26.04 ? 169 LEU   B CA  1 
ATOM   4340 C  C   . LEU   B 1 184 ? -26.393 -7.06   -6.889  1   25.72 ? 169 LEU   B C   1 
ATOM   4341 O  O   . LEU   B 1 184 ? -25.881 -6.831  -5.8    1   26.2  ? 169 LEU   B O   1 
ATOM   4342 C  CB  . LEU   B 1 184 ? -28.095 -8.921  -6.906  1   27.43 ? 169 LEU   B CB  1 
ATOM   4343 C  CG  . LEU   B 1 184 ? -29.523 -9.31   -6.52   1   30.31 ? 169 LEU   B CG  1 
ATOM   4344 C  CD1 . LEU   B 1 184 ? -29.779 -10.785 -6.785  1   30.85 ? 169 LEU   B CD1 1 
ATOM   4345 C  CD2 . LEU   B 1 184 ? -29.835 -8.908  -5.084  1   31.37 ? 169 LEU   B CD2 1 
ATOM   4346 N  N   . VAL   B 1 185 ? -25.687 -7.082  -8.023  1   24.65 ? 170 VAL   B N   1 
ATOM   4347 C  CA  . VAL   B 1 185 ? -24.279 -6.692  -8.078  1   24.07 ? 170 VAL   B CA  1 
ATOM   4348 C  C   . VAL   B 1 185 ? -24.173 -5.203  -7.761  1   24.36 ? 170 VAL   B C   1 
ATOM   4349 O  O   . VAL   B 1 185 ? -23.335 -4.79   -6.945  1   25.44 ? 170 VAL   B O   1 
ATOM   4350 C  CB  . VAL   B 1 185 ? -23.674 -7.042  -9.457  1   24.02 ? 170 VAL   B CB  1 
ATOM   4351 C  CG1 . VAL   B 1 185 ? -22.309 -6.356  -9.649  1   23.5  ? 170 VAL   B CG1 1 
ATOM   4352 C  CG2 . VAL   B 1 185 ? -23.553 -8.562  -9.61   1   24.23 ? 170 VAL   B CG2 1 
ATOM   4353 N  N   . GLU   B 1 186 ? -25.051 -4.397  -8.364  1   23.85 ? 171 GLU   B N   1 
ATOM   4354 C  CA  . GLU   B 1 186 ? -25.128 -2.96   -8.157  1   25.34 ? 171 GLU   B CA  1 
ATOM   4355 C  C   . GLU   B 1 186 ? -25.291 -2.629  -6.646  1   27.84 ? 171 GLU   B C   1 
ATOM   4356 O  O   . GLU   B 1 186 ? -24.57  -1.771  -6.11   1   28.23 ? 171 GLU   B O   1 
ATOM   4357 C  CB  . GLU   B 1 186 ? -26.279 -2.4    -9.017  1   25.7  ? 171 GLU   B CB  1 
ATOM   4358 C  CG  . GLU   B 1 186 ? -26.587 -0.942  -8.835  1   28.19 ? 171 GLU   B CG  1 
ATOM   4359 C  CD  . GLU   B 1 186 ? -25.804 0.028   -9.71   1   25.69 ? 171 GLU   B CD  1 
ATOM   4360 O  OE1 . GLU   B 1 186 ? -25.387 -0.347  -10.831 1   22.7  ? 171 GLU   B OE1 1 
ATOM   4361 O  OE2 . GLU   B 1 186 ? -25.621 1.18    -9.266  1   24.97 ? 171 GLU   B OE2 1 
ATOM   4362 N  N   . ILE   B 1 187 ? -26.161 -3.391  -5.946  1   28.26 ? 172 ILE   B N   1 
ATOM   4363 C  CA  . ILE   B 1 187 ? -26.382 -3.236  -4.514  1   30.2  ? 172 ILE   B CA  1 
ATOM   4364 C  C   . ILE   B 1 187 ? -25.145 -3.69   -3.701  1   30.26 ? 172 ILE   B C   1 
ATOM   4365 O  O   . ILE   B 1 187 ? -24.772 -3.005  -2.741  1   31.13 ? 172 ILE   B O   1 
ATOM   4366 C  CB  . ILE   B 1 187 ? -27.672 -3.985  -4.055  1   31.89 ? 172 ILE   B CB  1 
ATOM   4367 C  CG1 . ILE   B 1 187 ? -28.94  -3.32   -4.638  1   33.03 ? 172 ILE   B CG1 1 
ATOM   4368 C  CG2 . ILE   B 1 187 ? -27.755 -4.077  -2.52   1   32.16 ? 172 ILE   B CG2 1 
ATOM   4369 C  CD1 . ILE   B 1 187 ? -30.202 -4.143  -4.46   1   33.98 ? 172 ILE   B CD1 1 
ATOM   4370 N  N   . ALA   B 1 188 ? -24.514 -4.823  -4.078  1   29.05 ? 173 ALA   B N   1 
ATOM   4371 C  CA  . ALA   B 1 188 ? -23.319 -5.307  -3.376  1   29.24 ? 173 ALA   B CA  1 
ATOM   4372 C  C   . ALA   B 1 188 ? -22.153 -4.286  -3.487  1   30.73 ? 173 ALA   B C   1 
ATOM   4373 O  O   . ALA   B 1 188 ? -21.448 -4.044  -2.499  1   30.92 ? 173 ALA   B O   1 
ATOM   4374 C  CB  . ALA   B 1 188 ? -22.867 -6.644  -3.927  1   28.64 ? 173 ALA   B CB  1 
ATOM   4375 N  N   . ALA   B 1 189 ? -21.946 -3.711  -4.679  1   30.75 ? 174 ALA   B N   1 
ATOM   4376 C  CA  . ALA   B 1 189 ? -20.871 -2.726  -4.869  1   31.48 ? 174 ALA   B CA  1 
ATOM   4377 C  C   . ALA   B 1 189 ? -21.148 -1.446  -4.09   1   32.25 ? 174 ALA   B C   1 
ATOM   4378 O  O   . ALA   B 1 189 ? -20.211 -0.802  -3.6    1   31.1  ? 174 ALA   B O   1 
ATOM   4379 C  CB  . ALA   B 1 189 ? -20.68  -2.42   -6.34   1   31.35 ? 174 ALA   B CB  1 
ATOM   4380 N  N   . ALA   B 1 190 ? -22.439 -1.094  -3.943  1   33.26 ? 175 ALA   B N   1 
ATOM   4381 C  CA  . ALA   B 1 190 ? -22.871 0.077   -3.183  1   34.67 ? 175 ALA   B CA  1 
ATOM   4382 C  C   . ALA   B 1 190 ? -22.458 0.023   -1.705  1   34.41 ? 175 ALA   B C   1 
ATOM   4383 O  O   . ALA   B 1 190 ? -22.413 1.074   -1.087  1   34.3  ? 175 ALA   B O   1 
ATOM   4384 C  CB  . ALA   B 1 190 ? -24.379 0.27    -3.294  1   34.99 ? 175 ALA   B CB  1 
ATOM   4385 N  N   . SER   B 1 191 ? -22.159 -1.165  -1.137  1   34.05 ? 176 SER   B N   1 
ATOM   4386 C  CA  . SER   B 1 191 ? -21.721 -1.226  0.265   1   34.64 ? 176 SER   B CA  1 
ATOM   4387 C  C   . SER   B 1 191 ? -20.37  -0.496  0.491   1   34.59 ? 176 SER   B C   1 
ATOM   4388 O  O   . SER   B 1 191 ? -20.067 -0.114  1.611   1   35.08 ? 176 SER   B O   1 
ATOM   4389 C  CB  . SER   B 1 191 ? -21.647 -2.662  0.764   1   37.16 ? 176 SER   B CB  1 
ATOM   4390 O  OG  . SER   B 1 191 ? -20.646 -3.399  0.085   1   40.56 ? 176 SER   B OG  1 
ATOM   4391 N  N   . ALA   B 1 192 ? -19.595 -0.264  -0.581  1   33.28 ? 177 ALA   B N   1 
ATOM   4392 C  CA  . ALA   B 1 192 ? -18.339 0.464   -0.518  1   32.95 ? 177 ALA   B CA  1 
ATOM   4393 C  C   . ALA   B 1 192 ? -18.538 1.994   -0.592  1   32.66 ? 177 ALA   B C   1 
ATOM   4394 O  O   . ALA   B 1 192 ? -17.629 2.734   -0.214  1   32.22 ? 177 ALA   B O   1 
ATOM   4395 C  CB  . ALA   B 1 192 ? -17.41  -0.013  -1.622  1   32.14 ? 177 ALA   B CB  1 
ATOM   4396 N  N   . ILE   B 1 193 ? -19.702 2.474   -1.072  1   31.91 ? 178 ILE   B N   1 
ATOM   4397 C  CA  . ILE   B 1 193 ? -19.956 3.909   -1.207  1   32.43 ? 178 ILE   B CA  1 
ATOM   4398 C  C   . ILE   B 1 193 ? -19.837 4.651   0.113   1   32.46 ? 178 ILE   B C   1 
ATOM   4399 O  O   . ILE   B 1 193 ? -19.275 5.751   0.143   1   32.82 ? 178 ILE   B O   1 
ATOM   4400 C  CB  . ILE   B 1 193 ? -21.339 4.19    -1.852  1   33.65 ? 178 ILE   B CB  1 
ATOM   4401 C  CG1 . ILE   B 1 193 ? -21.456 3.545   -3.241  1   35.94 ? 178 ILE   B CG1 1 
ATOM   4402 C  CG2 . ILE   B 1 193 ? -21.67  5.673   -1.865  1   33.94 ? 178 ILE   B CG2 1 
ATOM   4403 C  CD1 . ILE   B 1 193 ? -20.644 4.164   -4.302  1   39.07 ? 178 ILE   B CD1 1 
ATOM   4404 N  N   . LYS   B 1 194 ? -20.373 4.071   1.194   1   31.91 ? 179 LYS   B N   1 
ATOM   4405 C  CA  . LYS   B 1 194 ? -20.317 4.682   2.522   1   32.62 ? 179 LYS   B CA  1 
ATOM   4406 C  C   . LYS   B 1 194 ? -18.869 4.891   3.026   1   32.52 ? 179 LYS   B C   1 
ATOM   4407 O  O   . LYS   B 1 194 ? -18.644 5.704   3.926   1   33.91 ? 179 LYS   B O   1 
ATOM   4408 C  CB  . LYS   B 1 194 ? -21.12  3.849   3.538   1   34.46 ? 179 LYS   B CB  1 
ATOM   4409 C  CG  . LYS   B 1 194 ? -20.5   2.492   3.837   1   39.62 ? 179 LYS   B CG  1 
ATOM   4410 C  CD  . LYS   B 1 194 ? -21.111 1.888   5.103   1   45.55 ? 179 LYS   B CD  1 
ATOM   4411 C  CE  . LYS   B 1 194 ? -22.045 0.752   4.795   1   50.42 ? 179 LYS   B CE  1 
ATOM   4412 N  NZ  . LYS   B 1 194 ? -21.293 -0.522  4.617   1   53.91 ? 179 LYS   B NZ  1 
ATOM   4413 N  N   . VAL   B 1 195 ? -17.908 4.181   2.445   1   30.89 ? 180 VAL   B N   1 
ATOM   4414 C  CA  . VAL   B 1 195 ? -16.493 4.309   2.798   1   30.75 ? 180 VAL   B CA  1 
ATOM   4415 C  C   . VAL   B 1 195 ? -15.845 5.541   2.106   1   30.4  ? 180 VAL   B C   1 
ATOM   4416 O  O   . VAL   B 1 195 ? -14.819 6.051   2.576   1   31.03 ? 180 VAL   B O   1 
ATOM   4417 C  CB  . VAL   B 1 195 ? -15.727 2.994   2.483   1   30.56 ? 180 VAL   B CB  1 
ATOM   4418 C  CG1 . VAL   B 1 195 ? -14.305 3.055   3.01    1   30.11 ? 180 VAL   B CG1 1 
ATOM   4419 C  CG2 . VAL   B 1 195 ? -16.45  1.784   3.076   1   31.15 ? 180 VAL   B CG2 1 
ATOM   4420 N  N   . ILE   B 1 196 ? -16.448 6.04    1.021   1   29.22 ? 181 ILE   B N   1 
ATOM   4421 C  CA  . ILE   B 1 196 ? -15.893 7.17    0.279   1   29.52 ? 181 ILE   B CA  1 
ATOM   4422 C  C   . ILE   B 1 196 ? -15.619 8.407   1.163   1   31.42 ? 181 ILE   B C   1 
ATOM   4423 O  O   . ILE   B 1 196 ? -14.494 8.917   1.09    1   31.48 ? 181 ILE   B O   1 
ATOM   4424 C  CB  . ILE   B 1 196 ? -16.727 7.511   -0.977  1   29.28 ? 181 ILE   B CB  1 
ATOM   4425 C  CG1 . ILE   B 1 196 ? -16.629 6.346   -1.996  1   29.77 ? 181 ILE   B CG1 1 
ATOM   4426 C  CG2 . ILE   B 1 196 ? -16.285 8.852   -1.605  1   29.47 ? 181 ILE   B CG2 1 
ATOM   4427 C  CD1 . ILE   B 1 196 ? -17.518 6.553   -3.261  1   31.53 ? 181 ILE   B CD1 1 
ATOM   4428 N  N   . PRO   B 1 197 ? -16.555 8.885   2.022   1   32.15 ? 182 PRO   B N   1 
ATOM   4429 C  CA  . PRO   B 1 197 ? -16.234 10.056  2.854   1   32.42 ? 182 PRO   B CA  1 
ATOM   4430 C  C   . PRO   B 1 197 ? -15.08  9.784   3.818   1   31.94 ? 182 PRO   B C   1 
ATOM   4431 O  O   . PRO   B 1 197 ? -14.34  10.707  4.125   1   32.2  ? 182 PRO   B O   1 
ATOM   4432 C  CB  . PRO   B 1 197 ? -17.553 10.341  3.603   1   33.53 ? 182 PRO   B CB  1 
ATOM   4433 C  CG  . PRO   B 1 197 ? -18.615 9.625   2.833   1   33.67 ? 182 PRO   B CG  1 
ATOM   4434 C  CD  . PRO   B 1 197 ? -17.947 8.427   2.251   1   32.17 ? 182 PRO   B CD  1 
ATOM   4435 N  N   . THR   B 1 198 ? -14.918 8.528   4.272   1   31.38 ? 183 THR   B N   1 
ATOM   4436 C  CA  . THR   B 1 198 ? -13.806 8.131   5.151   1   31.69 ? 183 THR   B CA  1 
ATOM   4437 C  C   . THR   B 1 198 ? -12.482 8.272   4.377   1   30.37 ? 183 THR   B C   1 
ATOM   4438 O  O   . THR   B 1 198 ? -11.513 8.785   4.926   1   30.2  ? 183 THR   B O   1 
ATOM   4439 C  CB  . THR   B 1 198 ? -13.977 6.694   5.631   1   33.52 ? 183 THR   B CB  1 
ATOM   4440 O  OG1 . THR   B 1 198 ? -15.259 6.563   6.24    1   35.3  ? 183 THR   B OG1 1 
ATOM   4441 C  CG2 . THR   B 1 198 ? -12.902 6.283   6.631   1   34.27 ? 183 THR   B CG2 1 
ATOM   4442 N  N   . VAL   B 1 199 ? -12.456 7.859   3.102   1   29.27 ? 184 VAL   B N   1 
ATOM   4443 C  CA  . VAL   B 1 199 ? -11.268 7.985   2.253   1   29.31 ? 184 VAL   B CA  1 
ATOM   4444 C  C   . VAL   B 1 199 ? -10.829 9.451   2.131   1   29.83 ? 184 VAL   B C   1 
ATOM   4445 O  O   . VAL   B 1 199 ? -9.68   9.77    2.452   1   29.51 ? 184 VAL   B O   1 
ATOM   4446 C  CB  . VAL   B 1 199 ? -11.446 7.298   0.867   1   29.45 ? 184 VAL   B CB  1 
ATOM   4447 C  CG1 . VAL   B 1 199 ? -10.271 7.591   -0.061  1   29.51 ? 184 VAL   B CG1 1 
ATOM   4448 C  CG2 . VAL   B 1 199 ? -11.628 5.788   1.022   1   29.97 ? 184 VAL   B CG2 1 
ATOM   4449 N  N   . PHE   B 1 200 ? -11.729 10.346  1.697   1   29.45 ? 185 PHE   B N   1 
ATOM   4450 C  CA  . PHE   B 1 200 ? -11.374 11.761  1.534   1   30.61 ? 185 PHE   B CA  1 
ATOM   4451 C  C   . PHE   B 1 200 ? -11.022 12.493  2.823   1   31.52 ? 185 PHE   B C   1 
ATOM   4452 O  O   . PHE   B 1 200 ? -10.16  13.379  2.808   1   31.58 ? 185 PHE   B O   1 
ATOM   4453 C  CB  . PHE   B 1 200 ? -12.473 12.515  0.789   1   30.93 ? 185 PHE   B CB  1 
ATOM   4454 C  CG  . PHE   B 1 200 ? -12.54  12.076  -0.652  1   32.08 ? 185 PHE   B CG  1 
ATOM   4455 C  CD1 . PHE   B 1 200 ? -11.434 12.186  -1.476  1   32.74 ? 185 PHE   B CD1 1 
ATOM   4456 C  CD2 . PHE   B 1 200 ? -13.701 11.536  -1.173  1   33.92 ? 185 PHE   B CD2 1 
ATOM   4457 C  CE1 . PHE   B 1 200 ? -11.483 11.759  -2.791  1   34.26 ? 185 PHE   B CE1 1 
ATOM   4458 C  CE2 . PHE   B 1 200 ? -13.757 11.129  -2.5    1   35.04 ? 185 PHE   B CE2 1 
ATOM   4459 C  CZ  . PHE   B 1 200 ? -12.652 11.237  -3.299  1   34.61 ? 185 PHE   B CZ  1 
ATOM   4460 N  N   . LYS   B 1 201 ? -11.679 12.135  3.919   1   31.88 ? 186 LYS   B N   1 
ATOM   4461 C  CA  . LYS   B 1 201 ? -11.423 12.734  5.215   1   33.29 ? 186 LYS   B CA  1 
ATOM   4462 C  C   . LYS   B 1 201 ? -10.046 12.261  5.727   1   33.47 ? 186 LYS   B C   1 
ATOM   4463 O  O   . LYS   B 1 201 ? -9.259  13.08   6.211   1   33.2  ? 186 LYS   B O   1 
ATOM   4464 C  CB  . LYS   B 1 201 ? -12.535 12.349  6.203   1   36.19 ? 186 LYS   B CB  1 
ATOM   4465 C  CG  . LYS   B 1 201 ? -12.291 12.83   7.621   1   41.82 ? 186 LYS   B CG  1 
ATOM   4466 C  CD  . LYS   B 1 201 ? -12.352 14.345  7.708   1   48.13 ? 186 LYS   B CD  1 
ATOM   4467 N  N   . ALA   B 1 202 ? -9.731  10.956  5.571   1   33.44 ? 187 ALA   B N   1 
ATOM   4468 C  CA  . ALA   B 1 202 ? -8.428  10.432  5.983   1   34.06 ? 187 ALA   B CA  1 
ATOM   4469 C  C   . ALA   B 1 202 ? -7.309  11.104  5.187   1   35.06 ? 187 ALA   B C   1 
ATOM   4470 O  O   . ALA   B 1 202 ? -6.265  11.398  5.758   1   35.05 ? 187 ALA   B O   1 
ATOM   4471 C  CB  . ALA   B 1 202 ? -8.368  8.932   5.805   1   33.97 ? 187 ALA   B CB  1 
ATOM   4472 N  N   . MET   B 1 203 ? -7.534  11.402  3.895   1   35.13 ? 188 MET   B N   1 
ATOM   4473 C  CA  . MET   B 1 203 ? -6.523  12.098  3.102   1   35.83 ? 188 MET   B CA  1 
ATOM   4474 C  C   . MET   B 1 203 ? -6.31   13.524  3.609   1   37.89 ? 188 MET   B C   1 
ATOM   4475 O  O   . MET   B 1 203 ? -5.169  13.915  3.829   1   37.9  ? 188 MET   B O   1 
ATOM   4476 C  CB  . MET   B 1 203 ? -6.891  12.119  1.621   1   35    ? 188 MET   B CB  1 
ATOM   4477 C  CG  . MET   B 1 203 ? -6.701  10.791  0.933   1   35.78 ? 188 MET   B CG  1 
ATOM   4478 S  SD  . MET   B 1 203 ? -7.644  10.701  -0.612  1   35.76 ? 188 MET   B SD  1 
ATOM   4479 C  CE  . MET   B 1 203 ? -6.957  12.093  -1.522  1   32.2  ? 188 MET   B CE  1 
ATOM   4480 N  N   . GLN   B 1 204 ? -7.398  14.283  3.827   1   38.84 ? 189 GLN   B N   1 
ATOM   4481 C  CA  . GLN   B 1 204 ? -7.319  15.667  4.285   1   41.05 ? 189 GLN   B CA  1 
ATOM   4482 C  C   . GLN   B 1 204 ? -6.67   15.789  5.663   1   42.48 ? 189 GLN   B C   1 
ATOM   4483 O  O   . GLN   B 1 204 ? -5.831  16.662  5.876   1   42.9  ? 189 GLN   B O   1 
ATOM   4484 C  CB  . GLN   B 1 204 ? -8.704  16.321  4.283   1   43.67 ? 189 GLN   B CB  1 
ATOM   4485 C  CG  . GLN   B 1 204 ? -8.606  17.797  3.929   1   49.92 ? 189 GLN   B CG  1 
ATOM   4486 C  CD  . GLN   B 1 204 ? -9.361  18.656  4.894   1   58.02 ? 189 GLN   B CD  1 
ATOM   4487 O  OE1 . GLN   B 1 204 ? -10.406 18.261  5.427   1   59.82 ? 189 GLN   B OE1 1 
ATOM   4488 N  NE2 . GLN   B 1 204 ? -8.857  19.87   5.127   1   60.2  ? 189 GLN   B NE2 1 
ATOM   4489 N  N   . MET   B 1 205 ? -7.032  14.892  6.583   1   42.58 ? 190 MET   B N   1 
ATOM   4490 C  CA  . MET   B 1 205 ? -6.481  14.856  7.933   1   43.16 ? 190 MET   B CA  1 
ATOM   4491 C  C   . MET   B 1 205 ? -5.159  14.088  8.026   1   42.56 ? 190 MET   B C   1 
ATOM   4492 O  O   . MET   B 1 205 ? -4.692  13.853  9.134   1   43.29 ? 190 MET   B O   1 
ATOM   4493 C  CB  . MET   B 1 205 ? -7.495  14.222  8.897   1   45.09 ? 190 MET   B CB  1 
ATOM   4494 C  CG  . MET   B 1 205 ? -8.802  14.989  9       1   50.12 ? 190 MET   B CG  1 
ATOM   4495 S  SD  . MET   B 1 205 ? -8.575  16.677  9.6     1   65.26 ? 190 MET   B SD  1 
ATOM   4496 C  CE  . MET   B 1 205 ? -9.708  17.539  8.58    1   65.12 ? 190 MET   B CE  1 
ATOM   4497 N  N   . GLN   B 1 206 ? -4.593  13.631  6.889   1   41.01 ? 191 GLN   B N   1 
ATOM   4498 C  CA  . GLN   B 1 206 ? -3.366  12.853  6.82    1   40.56 ? 191 GLN   B CA  1 
ATOM   4499 C  C   . GLN   B 1 206 ? -3.391  11.661  7.788   1   39.49 ? 191 GLN   B C   1 
ATOM   4500 O  O   . GLN   B 1 206 ? -2.461  11.482  8.56    1   40.27 ? 191 GLN   B O   1 
ATOM   4501 C  CB  . GLN   B 1 206 ? -2.139  13.761  7.039   1   42.22 ? 191 GLN   B CB  1 
ATOM   4502 C  CG  . GLN   B 1 206 ? -1.928  14.785  5.915   1   46.34 ? 191 GLN   B CG  1 
ATOM   4503 C  CD  . GLN   B 1 206 ? -1.169  14.208  4.751   1   52.48 ? 191 GLN   B CD  1 
ATOM   4504 O  OE1 . GLN   B 1 206 ? -0.372  13.281  4.905   1   55.73 ? 191 GLN   B OE1 1 
ATOM   4505 N  NE2 . GLN   B 1 206 ? -1.383  14.739  3.553   1   53.42 ? 191 GLN   B NE2 1 
ATOM   4506 N  N   . GLU   B 1 207 ? -4.484  10.892  7.798   1   36.71 ? 192 GLU   B N   1 
ATOM   4507 C  CA  . GLU   B 1 207 ? -4.635  9.744   8.662   1   35.64 ? 192 GLU   B CA  1 
ATOM   4508 C  C   . GLU   B 1 207 ? -4.329  8.481   7.849   1   34.63 ? 192 GLU   B C   1 
ATOM   4509 O  O   . GLU   B 1 207 ? -5.233  7.889   7.247   1   34.26 ? 192 GLU   B O   1 
ATOM   4510 C  CB  . GLU   B 1 207 ? -6.057  9.699   9.248   1   38.53 ? 192 GLU   B CB  1 
ATOM   4511 C  CG  . GLU   B 1 207 ? -6.378  10.846  10.189  1   44.2  ? 192 GLU   B CG  1 
ATOM   4512 C  CD  . GLU   B 1 207 ? -5.872  10.701  11.618  1   53.59 ? 192 GLU   B CD  1 
ATOM   4513 O  OE1 . GLU   B 1 207 ? -5.462  9.58    11.999  1   55.38 ? 192 GLU   B OE1 1 
ATOM   4514 O  OE2 . GLU   B 1 207 ? -5.913  11.707  12.367  1   57.4  ? 192 GLU   B OE2 1 
ATOM   4515 N  N   . ARG   B 1 208 ? -3.039  8.093   7.808   1   33.05 ? 193 ARG   B N   1 
ATOM   4516 C  CA  . ARG   B 1 208 ? -2.546  6.961   7.036   1   31.76 ? 193 ARG   B CA  1 
ATOM   4517 C  C   . ARG   B 1 208 ? -3.216  5.625   7.376   1   31.86 ? 193 ARG   B C   1 
ATOM   4518 O  O   . ARG   B 1 208 ? -3.561  4.861   6.463   1   32.16 ? 193 ARG   B O   1 
ATOM   4519 C  CB  . ARG   B 1 208 ? -1.016  6.853   7.182   1   31.6  ? 193 ARG   B CB  1 
ATOM   4520 C  CG  . ARG   B 1 208 ? -0.387  5.701   6.41    1   31.07 ? 193 ARG   B CG  1 
ATOM   4521 C  CD  . ARG   B 1 208 ? -0.207  4.419   7.207   1   29.63 ? 193 ARG   B CD  1 
ATOM   4522 N  NE  . ARG   B 1 208 ? 0.592   3.463   6.451   1   28.71 ? 193 ARG   B NE  1 
ATOM   4523 C  CZ  . ARG   B 1 208 ? 0.782   2.197   6.791   1   27.95 ? 193 ARG   B CZ  1 
ATOM   4524 N  NH1 . ARG   B 1 208 ? 0.21    1.702   7.877   1   29.04 ? 193 ARG   B NH1 1 
ATOM   4525 N  NH2 . ARG   B 1 208 ? 1.544   1.414   6.045   1   25.18 ? 193 ARG   B NH2 1 
ATOM   4526 N  N   . ASP   B 1 209 ? -3.331  5.304   8.673   1   31.1  ? 194 ASP   B N   1 
ATOM   4527 C  CA  . ASP   B 1 209 ? -3.904  4.031   9.067   1   31.01 ? 194 ASP   B CA  1 
ATOM   4528 C  C   . ASP   B 1 209 ? -5.391  3.965   8.726   1   30.08 ? 194 ASP   B C   1 
ATOM   4529 O  O   . ASP   B 1 209 ? -5.857  2.91    8.325   1   30.16 ? 194 ASP   B O   1 
ATOM   4530 C  CB  . ASP   B 1 209 ? -3.63   3.732   10.54   1   32.45 ? 194 ASP   B CB  1 
ATOM   4531 C  CG  . ASP   B 1 209 ? -2.141  3.725   10.847  1   34.6  ? 194 ASP   B CG  1 
ATOM   4532 O  OD1 . ASP   B 1 209 ? -1.375  3.111   10.064  1   35.21 ? 194 ASP   B OD1 1 
ATOM   4533 O  OD2 . ASP   B 1 209 ? -1.739  4.378   11.823  1   34.18 ? 194 ASP   B OD2 1 
ATOM   4534 N  N   . THR   B 1 210 ? -6.122  5.077   8.9     1   30.04 ? 195 THR   B N   1 
ATOM   4535 C  CA  . THR   B 1 210 ? -7.554  5.162   8.576   1   30.31 ? 195 THR   B CA  1 
ATOM   4536 C  C   . THR   B 1 210 ? -7.751  4.955   7.068   1   29.68 ? 195 THR   B C   1 
ATOM   4537 O  O   . THR   B 1 210 ? -8.635  4.192   6.662   1   29.85 ? 195 THR   B O   1 
ATOM   4538 C  CB  . THR   B 1 210 ? -8.101  6.525   9.02    1   32.02 ? 195 THR   B CB  1 
ATOM   4539 O  OG1 . THR   B 1 210 ? -7.857  6.668   10.409  1   34.23 ? 195 THR   B OG1 1 
ATOM   4540 C  CG2 . THR   B 1 210 ? -9.601  6.694   8.727   1   31.91 ? 195 THR   B CG2 1 
ATOM   4541 N  N   . LEU   B 1 211 ? -6.911  5.615   6.244   1   28.8  ? 196 LEU   B N   1 
ATOM   4542 C  CA  . LEU   B 1 211 ? -6.959  5.492   4.795   1   28.89 ? 196 LEU   B CA  1 
ATOM   4543 C  C   . LEU   B 1 211 ? -6.693  4.067   4.354   1   28.48 ? 196 LEU   B C   1 
ATOM   4544 O  O   . LEU   B 1 211 ? -7.422  3.532   3.51    1   28.29 ? 196 LEU   B O   1 
ATOM   4545 C  CB  . LEU   B 1 211 ? -5.974  6.461   4.113   1   28.92 ? 196 LEU   B CB  1 
ATOM   4546 C  CG  . LEU   B 1 211 ? -5.899  6.37    2.586   1   30.06 ? 196 LEU   B CG  1 
ATOM   4547 C  CD1 . LEU   B 1 211 ? -7.291  6.584   1.939   1   30.28 ? 196 LEU   B CD1 1 
ATOM   4548 C  CD2 . LEU   B 1 211 ? -4.974  7.434   2.019   1   30.21 ? 196 LEU   B CD2 1 
ATOM   4549 N  N   . LEU   B 1 212 ? -5.691  3.421   4.939   1   27.98 ? 197 LEU   B N   1 
ATOM   4550 C  CA  . LEU   B 1 212 ? -5.341  2.045   4.569   1   28.67 ? 197 LEU   B CA  1 
ATOM   4551 C  C   . LEU   B 1 212 ? -6.503  1.096   4.875   1   28.39 ? 197 LEU   B C   1 
ATOM   4552 O  O   . LEU   B 1 212 ? -6.858  0.233   4.06    1   28.38 ? 197 LEU   B O   1 
ATOM   4553 C  CB  . LEU   B 1 212 ? -4.06   1.617   5.332   1   29.46 ? 197 LEU   B CB  1 
ATOM   4554 C  CG  . LEU   B 1 212 ? -3.302  0.401   4.808   1   32.38 ? 197 LEU   B CG  1 
ATOM   4555 C  CD1 . LEU   B 1 212 ? -1.825  0.447   5.239   1   33.34 ? 197 LEU   B CD1 1 
ATOM   4556 C  CD2 . LEU   B 1 212 ? -3.905  -0.873  5.337   1   33.46 ? 197 LEU   B CD2 1 
ATOM   4557 N  N   . LYS   B 1 213 ? -7.094  1.267   6.054   1   28.26 ? 198 LYS   B N   1 
ATOM   4558 C  CA  . LYS   B 1 213 ? -8.212  0.439   6.505   1   27.99 ? 198 LYS   B CA  1 
ATOM   4559 C  C   . LYS   B 1 213 ? -9.42   0.654   5.556   1   27.48 ? 198 LYS   B C   1 
ATOM   4560 O  O   . LYS   B 1 213 ? -10.063 -0.32   5.156   1   27.68 ? 198 LYS   B O   1 
ATOM   4561 C  CB  . LYS   B 1 213 ? -8.583  0.836   7.939   1   30.24 ? 198 LYS   B CB  1 
ATOM   4562 C  CG  . LYS   B 1 213 ? -9.712  -0.008  8.522   1   35.46 ? 198 LYS   B CG  1 
ATOM   4563 C  CD  . LYS   B 1 213 ? -10.293 0.556   9.801   1   42.02 ? 198 LYS   B CD  1 
ATOM   4564 C  CE  . LYS   B 1 213 ? -11.165 -0.489  10.471  1   48.29 ? 198 LYS   B CE  1 
ATOM   4565 N  NZ  . LYS   B 1 213 ? -11.943 0.085   11.605  1   52.02 ? 198 LYS   B NZ  1 
ATOM   4566 N  N   . ALA   B 1 214 ? -9.684  1.921   5.169   1   26.75 ? 199 ALA   B N   1 
ATOM   4567 C  CA  . ALA   B 1 214 ? -10.78  2.27    4.265   1   26.59 ? 199 ALA   B CA  1 
ATOM   4568 C  C   . ALA   B 1 214 ? -10.61  1.631   2.891   1   27.07 ? 199 ALA   B C   1 
ATOM   4569 O  O   . ALA   B 1 214 ? -11.563 1.022   2.396   1   27.86 ? 199 ALA   B O   1 
ATOM   4570 C  CB  . ALA   B 1 214 ? -10.927 3.775   4.161   1   26.36 ? 199 ALA   B CB  1 
ATOM   4571 N  N   . LEU   B 1 215 ? -9.393  1.691   2.305   1   26.57 ? 200 LEU   B N   1 
ATOM   4572 C  CA  . LEU   B 1 215 ? -9.097  1.054   1.017   1   27.08 ? 200 LEU   B CA  1 
ATOM   4573 C  C   . LEU   B 1 215 ? -9.274  -0.482  1.081   1   28.5  ? 200 LEU   B C   1 
ATOM   4574 O  O   . LEU   B 1 215 ? -9.847  -1.076  0.153   1   29.28 ? 200 LEU   B O   1 
ATOM   4575 C  CB  . LEU   B 1 215 ? -7.695  1.429   0.505   1   26.55 ? 200 LEU   B CB  1 
ATOM   4576 C  CG  . LEU   B 1 215 ? -7.515  2.925   0.148   1   26.69 ? 200 LEU   B CG  1 
ATOM   4577 C  CD1 . LEU   B 1 215 ? -6.043  3.254   -0.128  1   26.57 ? 200 LEU   B CD1 1 
ATOM   4578 C  CD2 . LEU   B 1 215 ? -8.362  3.323   -1.084  1   26.36 ? 200 LEU   B CD2 1 
ATOM   4579 N  N   . LEU   B 1 216 ? -8.844  -1.128  2.183   1   27.65 ? 201 LEU   B N   1 
ATOM   4580 C  CA  . LEU   B 1 216 ? -9.044  -2.585  2.324   1   27.92 ? 201 LEU   B CA  1 
ATOM   4581 C  C   . LEU   B 1 216 ? -10.553 -2.94   2.447   1   27.61 ? 201 LEU   B C   1 
ATOM   4582 O  O   . LEU   B 1 216 ? -10.968 -4.019  2.036   1   27.69 ? 201 LEU   B O   1 
ATOM   4583 C  CB  . LEU   B 1 216 ? -8.257  -3.142  3.541   1   28.26 ? 201 LEU   B CB  1 
ATOM   4584 C  CG  . LEU   B 1 216 ? -6.736  -3.155  3.4     1   29.69 ? 201 LEU   B CG  1 
ATOM   4585 C  CD1 . LEU   B 1 216 ? -6.036  -3.694  4.681   1   31.01 ? 201 LEU   B CD1 1 
ATOM   4586 C  CD2 . LEU   B 1 216 ? -6.293  -3.963  2.206   1   29.58 ? 201 LEU   B CD2 1 
ATOM   4587 N  N   . GLU   B 1 217 ? -11.347 -2.049  3.036   1   27.42 ? 202 GLU   B N   1 
ATOM   4588 C  CA  . GLU   B 1 217 ? -12.773 -2.269  3.18    1   28.48 ? 202 GLU   B CA  1 
ATOM   4589 C  C   . GLU   B 1 217 ? -13.458 -2.153  1.799   1   29.32 ? 202 GLU   B C   1 
ATOM   4590 O  O   . GLU   B 1 217 ? -14.314 -2.986  1.466   1   30.02 ? 202 GLU   B O   1 
ATOM   4591 C  CB  . GLU   B 1 217 ? -13.366 -1.29   4.197   1   31.65 ? 202 GLU   B CB  1 
ATOM   4592 C  CG  . GLU   B 1 217 ? -14.85  -1.479  4.457   1   37.93 ? 202 GLU   B CG  1 
ATOM   4593 C  CD  . GLU   B 1 217 ? -15.342 -2.881  4.778   1   47.62 ? 202 GLU   B CD  1 
ATOM   4594 O  OE1 . GLU   B 1 217 ? -14.582 -3.663  5.393   1   51.12 ? 202 GLU   B OE1 1 
ATOM   4595 O  OE2 . GLU   B 1 217 ? -16.503 -3.193  4.424   1   50.45 ? 202 GLU   B OE2 1 
ATOM   4596 N  N   . ILE   B 1 218 ? -13.017 -1.193  0.966   1   28.43 ? 203 ILE   B N   1 
ATOM   4597 C  CA  . ILE   B 1 218 ? -13.537 -1.035  -0.39   1   28.42 ? 203 ILE   B CA  1 
ATOM   4598 C  C   . ILE   B 1 218 ? -13.163 -2.274  -1.208  1   28.73 ? 203 ILE   B C   1 
ATOM   4599 O  O   . ILE   B 1 218 ? -14.037 -2.846  -1.87   1   30    ? 203 ILE   B O   1 
ATOM   4600 C  CB  . ILE   B 1 218 ? -13.028 0.273   -1.04   1   28.57 ? 203 ILE   B CB  1 
ATOM   4601 C  CG1 . ILE   B 1 218 ? -13.65  1.495   -0.34   1   28.29 ? 203 ILE   B CG1 1 
ATOM   4602 C  CG2 . ILE   B 1 218 ? -13.312 0.284   -2.545  1   29.35 ? 203 ILE   B CG2 1 
ATOM   4603 C  CD1 . ILE   B 1 218 ? -12.987 2.775   -0.7    1   29.9  ? 203 ILE   B CD1 1 
ATOM   4604 N  N   . ALA   B 1 219 ? -11.919 -2.756  -1.084  1   27.54 ? 204 ALA   B N   1 
ATOM   4605 C  CA  . ALA   B 1 219 ? -11.472 -3.957  -1.785  1   28.46 ? 204 ALA   B CA  1 
ATOM   4606 C  C   . ALA   B 1 219 ? -12.354 -5.168  -1.392  1   29.86 ? 204 ALA   B C   1 
ATOM   4607 O  O   . ALA   B 1 219 ? -12.82  -5.905  -2.268  1   28.95 ? 204 ALA   B O   1 
ATOM   4608 C  CB  . ALA   B 1 219 ? -9.997  -4.244  -1.485  1   28.27 ? 204 ALA   B CB  1 
ATOM   4609 N  N   . SER   B 1 220 ? -12.658 -5.29   -0.091  1   30.73 ? 205 SER   B N   1 
ATOM   4610 C  CA  . SER   B 1 220 ? -13.523 -6.357  0.426   1   32.59 ? 205 SER   B CA  1 
ATOM   4611 C  C   . SER   B 1 220 ? -14.918 -6.332  -0.218  1   32.42 ? 205 SER   B C   1 
ATOM   4612 O  O   . SER   B 1 220 ? -15.441 -7.385  -0.592  1   33.15 ? 205 SER   B O   1 
ATOM   4613 C  CB  . SER   B 1 220 ? -13.651 -6.243  1.94    1   35.09 ? 205 SER   B CB  1 
ATOM   4614 O  OG  . SER   B 1 220 ? -14.302 -7.402  2.427   1   38.94 ? 205 SER   B OG  1 
ATOM   4615 N  N   . CYS   B 1 221 ? -15.505 -5.141  -0.348  1   31.32 ? 206 CYS   B N   1 
ATOM   4616 C  CA  . CYS   B 1 221 ? -16.818 -4.948  -0.97   1   31.58 ? 206 CYS   B CA  1 
ATOM   4617 C  C   . CYS   B 1 221 ? -16.827 -5.378  -2.428  1   30.65 ? 206 CYS   B C   1 
ATOM   4618 O  O   . CYS   B 1 221 ? -17.772 -6.044  -2.879  1   30.05 ? 206 CYS   B O   1 
ATOM   4619 C  CB  . CYS   B 1 221 ? -17.276 -3.505  -0.823  1   32.79 ? 206 CYS   B CB  1 
ATOM   4620 S  SG  . CYS   B 1 221 ? -17.643 -3.017  0.883   1   38.63 ? 206 CYS   B SG  1 
ATOM   4621 N  N   . LEU   B 1 222 ? -15.788 -4.968  -3.177  1   29.97 ? 207 LEU   B N   1 
ATOM   4622 C  CA  . LEU   B 1 222 ? -15.637 -5.316  -4.584  1   30.07 ? 207 LEU   B CA  1 
ATOM   4623 C  C   . LEU   B 1 222 ? -15.401 -6.81   -4.775  1   30.19 ? 207 LEU   B C   1 
ATOM   4624 O  O   . LEU   B 1 222 ? -15.911 -7.394  -5.739  1   29.62 ? 207 LEU   B O   1 
ATOM   4625 C  CB  . LEU   B 1 222 ? -14.559 -4.446  -5.244  1   30.19 ? 207 LEU   B CB  1 
ATOM   4626 C  CG  . LEU   B 1 222 ? -14.925 -2.955  -5.235  1   32.21 ? 207 LEU   B CG  1 
ATOM   4627 C  CD1 . LEU   B 1 222 ? -13.731 -2.078  -5.585  1   33.05 ? 207 LEU   B CD1 1 
ATOM   4628 C  CD2 . LEU   B 1 222 ? -16.094 -2.677  -6.167  1   33.35 ? 207 LEU   B CD2 1 
ATOM   4629 N  N   . GLU   B 1 223 ? -14.67  -7.448  -3.831  1   30.08 ? 208 GLU   B N   1 
ATOM   4630 C  CA  . GLU   B 1 223 ? -14.465 -8.9    -3.829  1   31.07 ? 208 GLU   B CA  1 
ATOM   4631 C  C   . GLU   B 1 223 ? -15.813 -9.621  -3.605  1   32.26 ? 208 GLU   B C   1 
ATOM   4632 O  O   . GLU   B 1 223 ? -16.125 -10.59  -4.299  1   33.31 ? 208 GLU   B O   1 
ATOM   4633 C  CB  . GLU   B 1 223 ? -13.425 -9.298  -2.749  1   32.61 ? 208 GLU   B CB  1 
ATOM   4634 C  CG  . GLU   B 1 223 ? -12.003 -8.87   -3.1    1   36.18 ? 208 GLU   B CG  1 
ATOM   4635 C  CD  . GLU   B 1 223 ? -11.009 -8.795  -1.949  1   42.55 ? 208 GLU   B CD  1 
ATOM   4636 O  OE1 . GLU   B 1 223 ? -11.378 -9.18   -0.814  1   43.11 ? 208 GLU   B OE1 1 
ATOM   4637 O  OE2 . GLU   B 1 223 ? -9.858  -8.355  -2.186  1   42.99 ? 208 GLU   B OE2 1 
ATOM   4638 N  N   . LYS   B 1 224 ? -16.645 -9.114  -2.685  1   32.62 ? 209 LYS   B N   1 
ATOM   4639 C  CA  . LYS   B 1 224 ? -17.977 -9.695  -2.443  1   33.26 ? 209 LYS   B CA  1 
ATOM   4640 C  C   . LYS   B 1 224 ? -18.909 -9.523  -3.675  1   33.36 ? 209 LYS   B C   1 
ATOM   4641 O  O   . LYS   B 1 224 ? -19.684 -10.436 -3.991  1   33.74 ? 209 LYS   B O   1 
ATOM   4642 C  CB  . LYS   B 1 224 ? -18.634 -9.062  -1.2    1   35.56 ? 209 LYS   B CB  1 
ATOM   4643 C  CG  . LYS   B 1 224 ? -17.977 -9.469  0.118   1   42    ? 209 LYS   B CG  1 
ATOM   4644 C  CD  . LYS   B 1 224 ? -18.489 -8.626  1.28    1   48.04 ? 209 LYS   B CD  1 
ATOM   4645 C  CE  . LYS   B 1 224 ? -18.13  -9.225  2.624   1   53.29 ? 209 LYS   B CE  1 
ATOM   4646 N  NZ  . LYS   B 1 224 ? -16.683 -9.563  2.711   1   56.13 ? 209 LYS   B NZ  1 
ATOM   4647 N  N   . ALA   B 1 225 ? -18.828 -8.369  -4.373  1   32.14 ? 210 ALA   B N   1 
ATOM   4648 C  CA  . ALA   B 1 225 ? -19.653 -8.152  -5.571  1   32.04 ? 210 ALA   B CA  1 
ATOM   4649 C  C   . ALA   B 1 225 ? -19.397 -9.221  -6.654  1   32.54 ? 210 ALA   B C   1 
ATOM   4650 O  O   . ALA   B 1 225 ? -20.334 -9.587  -7.371  1   32.62 ? 210 ALA   B O   1 
ATOM   4651 C  CB  . ALA   B 1 225 ? -19.429 -6.753  -6.142  1   31.29 ? 210 ALA   B CB  1 
ATOM   4652 N  N   . LEU   B 1 226 ? -18.16  -9.769  -6.724  1   32.36 ? 211 LEU   B N   1 
ATOM   4653 C  CA  . LEU   B 1 226 ? -17.812 -10.8   -7.703  1   33.37 ? 211 LEU   B CA  1 
ATOM   4654 C  C   . LEU   B 1 226 ? -18.566 -12.098 -7.398  1   34.39 ? 211 LEU   B C   1 
ATOM   4655 O  O   . LEU   B 1 226 ? -19.07  -12.743 -8.316  1   33.85 ? 211 LEU   B O   1 
ATOM   4656 C  CB  . LEU   B 1 226 ? -16.288 -11.042 -7.741  1   33.6  ? 211 LEU   B CB  1 
ATOM   4657 C  CG  . LEU   B 1 226 ? -15.787 -12.184 -8.636  1   35.08 ? 211 LEU   B CG  1 
ATOM   4658 C  CD1 . LEU   B 1 226 ? -16.175 -11.968 -10.072 1   35.19 ? 211 LEU   B CD1 1 
ATOM   4659 C  CD2 . LEU   B 1 226 ? -14.272 -12.348 -8.538  1   36    ? 211 LEU   B CD2 1 
ATOM   4660 N  N   . GLN   B 1 227 ? -18.685 -12.453 -6.111  1   35.04 ? 212 GLN   B N   1 
ATOM   4661 C  CA  . GLN   B 1 227 ? -19.421 -13.673 -5.736  1   35.75 ? 212 GLN   B CA  1 
ATOM   4662 C  C   . GLN   B 1 227 ? -20.889 -13.543 -6.133  1   35.31 ? 212 GLN   B C   1 
ATOM   4663 O  O   . GLN   B 1 227 ? -21.45  -14.494 -6.678  1   35.27 ? 212 GLN   B O   1 
ATOM   4664 C  CB  . GLN   B 1 227 ? -19.249 -13.986 -4.234  1   38.28 ? 212 GLN   B CB  1 
ATOM   4665 C  CG  . GLN   B 1 227 ? -17.773 -14.188 -3.837  1   43.9  ? 212 GLN   B CG  1 
ATOM   4666 C  CD  . GLN   B 1 227 ? -17.151 -15.334 -4.617  1   50.55 ? 212 GLN   B CD  1 
ATOM   4667 O  OE1 . GLN   B 1 227 ? -17.682 -16.457 -4.636  1   53.33 ? 212 GLN   B OE1 1 
ATOM   4668 N  NE2 . GLN   B 1 227 ? -16.044 -15.065 -5.317  1   51.01 ? 212 GLN   B NE2 1 
ATOM   4669 N  N   . VAL   B 1 228 ? -21.479 -12.331 -5.943  1   34.38 ? 213 VAL   B N   1 
ATOM   4670 C  CA  . VAL   B 1 228 ? -22.859 -12.039 -6.33   1   34.37 ? 213 VAL   B CA  1 
ATOM   4671 C  C   . VAL   B 1 228 ? -23.084 -12.271 -7.832  1   35.27 ? 213 VAL   B C   1 
ATOM   4672 O  O   . VAL   B 1 228 ? -24.094 -12.852 -8.233  1   35.36 ? 213 VAL   B O   1 
ATOM   4673 C  CB  . VAL   B 1 228 ? -23.301 -10.631 -5.868  1   33.85 ? 213 VAL   B CB  1 
ATOM   4674 C  CG1 . VAL   B 1 228 ? -24.662 -10.253 -6.454  1   34.07 ? 213 VAL   B CG1 1 
ATOM   4675 C  CG2 . VAL   B 1 228 ? -23.328 -10.551 -4.344  1   33.62 ? 213 VAL   B CG2 1 
ATOM   4676 N  N   . PHE   B 1 229 ? -22.097 -11.894 -8.648  1   35.22 ? 214 PHE   B N   1 
ATOM   4677 C  CA  . PHE   B 1 229 ? -22.121 -12.064 -10.089 1   35.77 ? 214 PHE   B CA  1 
ATOM   4678 C  C   . PHE   B 1 229 ? -22.335 -13.519 -10.556 1   35.05 ? 214 PHE   B C   1 
ATOM   4679 O  O   . PHE   B 1 229 ? -22.936 -13.742 -11.616 1   33.79 ? 214 PHE   B O   1 
ATOM   4680 C  CB  . PHE   B 1 229 ? -20.8   -11.557 -10.646 1   37.14 ? 214 PHE   B CB  1 
ATOM   4681 C  CG  . PHE   B 1 229 ? -20.877 -10.758 -11.916 1   39.91 ? 214 PHE   B CG  1 
ATOM   4682 C  CD1 . PHE   B 1 229 ? -21.529 -11.254 -13.026 1   41.64 ? 214 PHE   B CD1 1 
ATOM   4683 C  CD2 . PHE   B 1 229 ? -20.232 -9.542  -12.024 1   42.05 ? 214 PHE   B CD2 1 
ATOM   4684 C  CE1 . PHE   B 1 229 ? -21.547 -10.546 -14.211 1   42.93 ? 214 PHE   B CE1 1 
ATOM   4685 C  CE2 . PHE   B 1 229 ? -20.273 -8.824  -13.212 1   42.94 ? 214 PHE   B CE2 1 
ATOM   4686 C  CZ  . PHE   B 1 229 ? -20.883 -9.359  -14.306 1   42.79 ? 214 PHE   B CZ  1 
ATOM   4687 N  N   . HIS   B 1 230 ? -21.796 -14.499 -9.805  1   35.08 ? 215 HIS   B N   1 
ATOM   4688 C  CA  . HIS   B 1 230 ? -21.874 -15.913 -10.185 1   35.81 ? 215 HIS   B CA  1 
ATOM   4689 C  C   . HIS   B 1 230 ? -23.311 -16.389 -10.422 1   34.91 ? 215 HIS   B C   1 
ATOM   4690 O  O   . HIS   B 1 230 ? -23.508 -17.311 -11.205 1   35.19 ? 215 HIS   B O   1 
ATOM   4691 C  CB  . HIS   B 1 230 ? -21.158 -16.827 -9.161  1   37.84 ? 215 HIS   B CB  1 
ATOM   4692 C  CG  . HIS   B 1 230 ? -19.689 -16.554 -8.989  1   42.71 ? 215 HIS   B CG  1 
ATOM   4693 N  ND1 . HIS   B 1 230 ? -18.943 -17.208 -8.017  1   45.59 ? 215 HIS   B ND1 1 
ATOM   4694 C  CD2 . HIS   B 1 230 ? -18.87  -15.72  -9.675  1   44.22 ? 215 HIS   B CD2 1 
ATOM   4695 C  CE1 . HIS   B 1 230 ? -17.703 -16.754 -8.148  1   46.12 ? 215 HIS   B CE1 1 
ATOM   4696 N  NE2 . HIS   B 1 230 ? -17.615 -15.853 -9.13   1   45.9  ? 215 HIS   B NE2 1 
ATOM   4697 N  N   . GLN   B 1 231 ? -24.3   -15.755 -9.774  1   34.08 ? 216 GLN   B N   1 
ATOM   4698 C  CA  . GLN   B 1 231 ? -25.717 -16.081 -9.912  1   34.09 ? 216 GLN   B CA  1 
ATOM   4699 C  C   . GLN   B 1 231 ? -26.257 -15.929 -11.339 1   33.04 ? 216 GLN   B C   1 
ATOM   4700 O  O   . GLN   B 1 231 ? -27.293 -16.493 -11.648 1   32.75 ? 216 GLN   B O   1 
ATOM   4701 C  CB  . GLN   B 1 231 ? -26.568 -15.196 -9.004  1   36.24 ? 216 GLN   B CB  1 
ATOM   4702 C  CG  . GLN   B 1 231 ? -26.306 -15.396 -7.543  1   40.25 ? 216 GLN   B CG  1 
ATOM   4703 C  CD  . GLN   B 1 231 ? -27.131 -14.389 -6.816  1   43.61 ? 216 GLN   B CD  1 
ATOM   4704 O  OE1 . GLN   B 1 231 ? -28.337 -14.553 -6.657  1   43.82 ? 216 GLN   B OE1 1 
ATOM   4705 N  NE2 . GLN   B 1 231 ? -26.51  -13.297 -6.405  1   45.11 ? 216 GLN   B NE2 1 
ATOM   4706 N  N   . ILE   B 1 232 ? -25.576 -15.189 -12.206 1   31.97 ? 217 ILE   B N   1 
ATOM   4707 C  CA  . ILE   B 1 232 ? -26.019 -15.001 -13.585 1   31.37 ? 217 ILE   B CA  1 
ATOM   4708 C  C   . ILE   B 1 232 ? -26.303 -16.343 -14.316 1   31.95 ? 217 ILE   B C   1 
ATOM   4709 O  O   . ILE   B 1 232 ? -27.299 -16.444 -15.032 1   31.42 ? 217 ILE   B O   1 
ATOM   4710 C  CB  . ILE   B 1 232 ? -25.003 -14.116 -14.366 1   30.56 ? 217 ILE   B CB  1 
ATOM   4711 C  CG1 . ILE   B 1 232 ? -25.641 -13.498 -15.612 1   30.53 ? 217 ILE   B CG1 1 
ATOM   4712 C  CG2 . ILE   B 1 232 ? -23.718 -14.871 -14.704 1   30.45 ? 217 ILE   B CG2 1 
ATOM   4713 C  CD1 . ILE   B 1 232 ? -26.701 -12.415 -15.281 1   30.89 ? 217 ILE   B CD1 1 
ATOM   4714 N  N   . HIS   B 1 233 ? -25.463 -17.377 -14.083 1   32.24 ? 218 HIS   B N   1 
ATOM   4715 C  CA  . HIS   B 1 233 ? -25.576 -18.657 -14.795 1   33.42 ? 218 HIS   B CA  1 
ATOM   4716 C  C   . HIS   B 1 233 ? -26.846 -19.429 -14.488 1   35.41 ? 218 HIS   B C   1 
ATOM   4717 O  O   . HIS   B 1 233 ? -27.375 -20.118 -15.37  1   35.75 ? 218 HIS   B O   1 
ATOM   4718 C  CB  . HIS   B 1 233 ? -24.326 -19.537 -14.577 1   33.39 ? 218 HIS   B CB  1 
ATOM   4719 C  CG  . HIS   B 1 233 ? -23.057 -18.825 -14.928 1   33.74 ? 218 HIS   B CG  1 
ATOM   4720 N  ND1 . HIS   B 1 233 ? -22.653 -18.66  -16.242 1   34.58 ? 218 HIS   B ND1 1 
ATOM   4721 C  CD2 . HIS   B 1 233 ? -22.174 -18.195 -14.121 1   34.71 ? 218 HIS   B CD2 1 
ATOM   4722 C  CE1 . HIS   B 1 233 ? -21.526 -17.967 -16.188 1   35.16 ? 218 HIS   B CE1 1 
ATOM   4723 N  NE2 . HIS   B 1 233 ? -21.208 -17.649 -14.938 1   35.34 ? 218 HIS   B NE2 1 
ATOM   4724 N  N   . ASP   B 1 234 ? -27.363 -19.278 -13.263 1   35.65 ? 219 ASP   B N   1 
ATOM   4725 C  CA  . ASP   B 1 234 ? -28.559 -19.985 -12.833 1   36.34 ? 219 ASP   B CA  1 
ATOM   4726 C  C   . ASP   B 1 234 ? -29.848 -19.353 -13.331 1   36.65 ? 219 ASP   B C   1 
ATOM   4727 O  O   . ASP   B 1 234 ? -30.889 -20.018 -13.312 1   37.65 ? 219 ASP   B O   1 
ATOM   4728 C  CB  . ASP   B 1 234 ? -28.593 -20.03  -11.302 1   38.73 ? 219 ASP   B CB  1 
ATOM   4729 C  CG  . ASP   B 1 234 ? -27.399 -20.746 -10.707 1   45.54 ? 219 ASP   B CG  1 
ATOM   4730 O  OD1 . ASP   B 1 234 ? -26.911 -21.703 -11.337 1   45.81 ? 219 ASP   B OD1 1 
ATOM   4731 O  OD2 . ASP   B 1 234 ? -26.932 -20.326 -9.618  1   49.48 ? 219 ASP   B OD2 1 
ATOM   4732 N  N   . HIS   B 1 235 ? -29.818 -18.061 -13.733 1   34.5  ? 220 HIS   B N   1 
ATOM   4733 C  CA  . HIS   B 1 235 ? -31.051 -17.371 -14.074 1   33.15 ? 220 HIS   B CA  1 
ATOM   4734 C  C   . HIS   B 1 235 ? -31.15  -16.828 -15.476 1   31.56 ? 220 HIS   B C   1 
ATOM   4735 O  O   . HIS   B 1 235 ? -32.159 -16.202 -15.798 1   32.27 ? 220 HIS   B O   1 
ATOM   4736 C  CB  . HIS   B 1 235 ? -31.303 -16.243 -13.069 1   34.68 ? 220 HIS   B CB  1 
ATOM   4737 C  CG  . HIS   B 1 235 ? -31.231 -16.712 -11.65  1   39.34 ? 220 HIS   B CG  1 
ATOM   4738 N  ND1 . HIS   B 1 235 ? -32.102 -17.678 -11.167 1   41.93 ? 220 HIS   B ND1 1 
ATOM   4739 C  CD2 . HIS   B 1 235 ? -30.373 -16.367 -10.664 1   40.67 ? 220 HIS   B CD2 1 
ATOM   4740 C  CE1 . HIS   B 1 235 ? -31.74  -17.894 -9.914  1   42.3  ? 220 HIS   B CE1 1 
ATOM   4741 N  NE2 . HIS   B 1 235 ? -30.717 -17.117 -9.562  1   42.03 ? 220 HIS   B NE2 1 
ATOM   4742 N  N   . VAL   B 1 236 ? -30.109 -16.998 -16.297 1   30.13 ? 221 VAL   B N   1 
ATOM   4743 C  CA  . VAL   B 1 236 ? -30.149 -16.523 -17.675 1   29.12 ? 221 VAL   B CA  1 
ATOM   4744 C  C   . VAL   B 1 236 ? -29.592 -17.618 -18.551 1   29.16 ? 221 VAL   B C   1 
ATOM   4745 O  O   . VAL   B 1 236 ? -28.578 -18.215 -18.183 1   28.67 ? 221 VAL   B O   1 
ATOM   4746 C  CB  . VAL   B 1 236 ? -29.315 -15.216 -17.875 1   28.26 ? 221 VAL   B CB  1 
ATOM   4747 C  CG1 . VAL   B 1 236 ? -29.502 -14.676 -19.294 1   28.21 ? 221 VAL   B CG1 1 
ATOM   4748 C  CG2 . VAL   B 1 236 ? -29.708 -14.154 -16.857 1   27.52 ? 221 VAL   B CG2 1 
ATOM   4749 N  N   . ASN   B 1 237 ? -30.224 -17.895 -19.708 1   29.32 ? 222 ASN   B N   1 
ATOM   4750 C  CA  . ASN   B 1 237 ? -29.606 -18.854 -20.631 1   30.22 ? 222 ASN   B CA  1 
ATOM   4751 C  C   . ASN   B 1 237 ? -29.202 -18.118 -21.895 1   29.56 ? 222 ASN   B C   1 
ATOM   4752 O  O   . ASN   B 1 237 ? -29.903 -17.19  -22.32  1   29.48 ? 222 ASN   B O   1 
ATOM   4753 C  CB  . ASN   B 1 237 ? -30.465 -20.094 -20.884 1   33.64 ? 222 ASN   B CB  1 
ATOM   4754 C  CG  . ASN   B 1 237 ? -31.711 -19.825 -21.656 1   38.51 ? 222 ASN   B CG  1 
ATOM   4755 O  OD1 . ASN   B 1 237 ? -32.781 -19.614 -21.082 1   42.02 ? 222 ASN   B OD1 1 
ATOM   4756 N  ND2 . ASN   B 1 237 ? -31.602 -19.831 -22.97  1   38.31 ? 222 ASN   B ND2 1 
ATOM   4757 N  N   . PRO   B 1 238 ? -28.053 -18.498 -22.49  1   29.49 ? 223 PRO   B N   1 
ATOM   4758 C  CA  . PRO   B 1 238 ? -27.555 -17.774 -23.667 1   29.38 ? 223 PRO   B CA  1 
ATOM   4759 C  C   . PRO   B 1 238 ? -28.509 -17.674 -24.847 1   31.03 ? 223 PRO   B C   1 
ATOM   4760 O  O   . PRO   B 1 238 ? -28.607 -16.599 -25.463 1   31.96 ? 223 PRO   B O   1 
ATOM   4761 C  CB  . PRO   B 1 238 ? -26.278 -18.537 -24.041 1   29.45 ? 223 PRO   B CB  1 
ATOM   4762 C  CG  . PRO   B 1 238 ? -25.819 -19.145 -22.775 1   30.11 ? 223 PRO   B CG  1 
ATOM   4763 C  CD  . PRO   B 1 238 ? -27.093 -19.529 -22.048 1   28.96 ? 223 PRO   B CD  1 
ATOM   4764 N  N   . LYS   B 1 239 ? -29.217 -18.773 -25.173 1   30.94 ? 224 LYS   B N   1 
ATOM   4765 C  CA  . LYS   B 1 239 ? -30.118 -18.751 -26.321 1   30.88 ? 224 LYS   B CA  1 
ATOM   4766 C  C   . LYS   B 1 239 ? -31.234 -17.72  -26.157 1   29.27 ? 224 LYS   B C   1 
ATOM   4767 O  O   . LYS   B 1 239 ? -31.484 -16.924 -27.064 1   29.44 ? 224 LYS   B O   1 
ATOM   4768 C  CB  . LYS   B 1 239 ? -30.699 -20.163 -26.602 1   34.2  ? 224 LYS   B CB  1 
ATOM   4769 C  CG  . LYS   B 1 239 ? -31.53  -20.198 -27.887 1   39.1  ? 224 LYS   B CG  1 
ATOM   4770 N  N   . ALA   B 1 240 ? -31.888 -17.715 -24.998 1   27.35 ? 225 ALA   B N   1 
ATOM   4771 C  CA  . ALA   B 1 240 ? -32.962 -16.76  -24.735 1   26.3  ? 225 ALA   B CA  1 
ATOM   4772 C  C   . ALA   B 1 240 ? -32.423 -15.342 -24.666 1   25.3  ? 225 ALA   B C   1 
ATOM   4773 O  O   . ALA   B 1 240 ? -33.002 -14.433 -25.262 1   25.79 ? 225 ALA   B O   1 
ATOM   4774 C  CB  . ALA   B 1 240 ? -33.662 -17.114 -23.438 1   26.07 ? 225 ALA   B CB  1 
ATOM   4775 N  N   . PHE   B 1 241 ? -31.303 -15.128 -23.956 1   24.46 ? 226 PHE   B N   1 
ATOM   4776 C  CA  . PHE   B 1 241 ? -30.73  -13.787 -23.846 1   23    ? 226 PHE   B CA  1 
ATOM   4777 C  C   . PHE   B 1 241 ? -30.432 -13.181 -25.223 1   23.13 ? 226 PHE   B C   1 
ATOM   4778 O  O   . PHE   B 1 241 ? -30.916 -12.09  -25.542 1   24.27 ? 226 PHE   B O   1 
ATOM   4779 C  CB  . PHE   B 1 241 ? -29.452 -13.811 -22.963 1   21.59 ? 226 PHE   B CB  1 
ATOM   4780 C  CG  . PHE   B 1 241 ? -28.886 -12.405 -22.851 1   21.53 ? 226 PHE   B CG  1 
ATOM   4781 C  CD1 . PHE   B 1 241 ? -29.425 -11.498 -21.965 1   21.85 ? 226 PHE   B CD1 1 
ATOM   4782 C  CD2 . PHE   B 1 241 ? -27.851 -11.986 -23.674 1   21.69 ? 226 PHE   B CD2 1 
ATOM   4783 C  CE1 . PHE   B 1 241 ? -28.922 -10.195 -21.878 1   22.05 ? 226 PHE   B CE1 1 
ATOM   4784 C  CE2 . PHE   B 1 241 ? -27.328 -10.698 -23.565 1   21.69 ? 226 PHE   B CE2 1 
ATOM   4785 C  CZ  . PHE   B 1 241 ? -27.897 -9.797  -22.697 1   21.56 ? 226 PHE   B CZ  1 
ATOM   4786 N  N   . PHE   B 1 242 ? -29.664 -13.908 -26.052 1   23.08 ? 227 PHE   B N   1 
ATOM   4787 C  CA  . PHE   B 1 242 ? -29.258 -13.387 -27.348 1   23.77 ? 227 PHE   B CA  1 
ATOM   4788 C  C   . PHE   B 1 242 ? -30.396 -13.352 -28.393 1   25.21 ? 227 PHE   B C   1 
ATOM   4789 O  O   . PHE   B 1 242 ? -30.476 -12.393 -29.148 1   24.75 ? 227 PHE   B O   1 
ATOM   4790 C  CB  . PHE   B 1 242 ? -28.031 -14.164 -27.875 1   23.5  ? 227 PHE   B CB  1 
ATOM   4791 C  CG  . PHE   B 1 242 ? -27.494 -13.597 -29.173 1   23.82 ? 227 PHE   B CG  1 
ATOM   4792 C  CD1 . PHE   B 1 242 ? -26.664 -12.494 -29.174 1   23.77 ? 227 PHE   B CD1 1 
ATOM   4793 C  CD2 . PHE   B 1 242 ? -27.859 -14.147 -30.39  1   24.84 ? 227 PHE   B CD2 1 
ATOM   4794 C  CE1 . PHE   B 1 242 ? -26.202 -11.957 -30.371 1   25.49 ? 227 PHE   B CE1 1 
ATOM   4795 C  CE2 . PHE   B 1 242 ? -27.436 -13.579 -31.583 1   25.45 ? 227 PHE   B CE2 1 
ATOM   4796 C  CZ  . PHE   B 1 242 ? -26.609 -12.495 -31.571 1   25.51 ? 227 PHE   B CZ  1 
ATOM   4797 N  N   . SER   B 1 243 ? -31.226 -14.4   -28.477 1   27.92 ? 228 SER   B N   1 
ATOM   4798 C  CA  . SER   B 1 243 ? -32.267 -14.426 -29.526 1   31.19 ? 228 SER   B CA  1 
ATOM   4799 C  C   . SER   B 1 243 ? -33.556 -13.695 -29.133 1   34.5  ? 228 SER   B C   1 
ATOM   4800 O  O   . SER   B 1 243 ? -34.284 -13.233 -30.023 1   37.05 ? 228 SER   B O   1 
ATOM   4801 C  CB  . SER   B 1 243 ? -32.547 -15.855 -29.972 1   33.34 ? 228 SER   B CB  1 
ATOM   4802 O  OG  . SER   B 1 243 ? -33.076 -16.601 -28.888 1   37.62 ? 228 SER   B OG  1 
ATOM   4803 N  N   . VAL   B 1 244 ? -33.844 -13.563 -27.823 1   33.57 ? 229 VAL   B N   1 
ATOM   4804 C  CA  . VAL   B 1 244 ? -35.072 -12.896 -27.391 1   33.51 ? 229 VAL   B CA  1 
ATOM   4805 C  C   . VAL   B 1 244 ? -34.836 -11.518 -26.701 1   31.85 ? 229 VAL   B C   1 
ATOM   4806 O  O   . VAL   B 1 244 ? -35.222 -10.49  -27.256 1   32.94 ? 229 VAL   B O   1 
ATOM   4807 C  CB  . VAL   B 1 244 ? -35.933 -13.842 -26.512 1   35.4  ? 229 VAL   B CB  1 
ATOM   4808 C  CG1 . VAL   B 1 244 ? -37.251 -13.166 -26.111 1   36.51 ? 229 VAL   B CG1 1 
ATOM   4809 C  CG2 . VAL   B 1 244 ? -36.186 -15.176 -27.218 1   36.27 ? 229 VAL   B CG2 1 
ATOM   4810 N  N   . LEU   B 1 245 ? -34.187 -11.485 -25.524 1   28.81 ? 230 LEU   B N   1 
ATOM   4811 C  CA  . LEU   B 1 245 ? -34.014 -10.239 -24.771 1   27.54 ? 230 LEU   B CA  1 
ATOM   4812 C  C   . LEU   B 1 245 ? -33.287 -9.136  -25.494 1   27.17 ? 230 LEU   B C   1 
ATOM   4813 O  O   . LEU   B 1 245 ? -33.702 -7.966  -25.414 1   27.86 ? 230 LEU   B O   1 
ATOM   4814 C  CB  . LEU   B 1 245 ? -33.345 -10.498 -23.413 1   26.82 ? 230 LEU   B CB  1 
ATOM   4815 C  CG  . LEU   B 1 245 ? -33.399 -9.35   -22.402 1   28.25 ? 230 LEU   B CG  1 
ATOM   4816 C  CD1 . LEU   B 1 245 ? -34.847 -8.765  -22.248 1   28.84 ? 230 LEU   B CD1 1 
ATOM   4817 C  CD2 . LEU   B 1 245 ? -32.834 -9.793  -21.057 1   29.2  ? 230 LEU   B CD2 1 
ATOM   4818 N  N   . ARG   B 1 246 ? -32.187 -9.481  -26.173 1   25.38 ? 231 ARG   B N   1 
ATOM   4819 C  CA  . ARG   B 1 246 ? -31.327 -8.55   -26.895 1   25.24 ? 231 ARG   B CA  1 
ATOM   4820 C  C   . ARG   B 1 246 ? -32.091 -7.486  -27.705 1   25.14 ? 231 ARG   B C   1 
ATOM   4821 O  O   . ARG   B 1 246 ? -31.762 -6.309  -27.647 1   24.77 ? 231 ARG   B O   1 
ATOM   4822 C  CB  . ARG   B 1 246 ? -30.375 -9.379  -27.798 1   26.28 ? 231 ARG   B CB  1 
ATOM   4823 C  CG  . ARG   B 1 246 ? -29.718 -8.614  -28.908 1   30.86 ? 231 ARG   B CG  1 
ATOM   4824 C  CD  . ARG   B 1 246 ? -28.712 -9.465  -29.614 1   34.56 ? 231 ARG   B CD  1 
ATOM   4825 N  NE  . ARG   B 1 246 ? -29.289 -10.184 -30.736 1   38.43 ? 231 ARG   B NE  1 
ATOM   4826 C  CZ  . ARG   B 1 246 ? -29.095 -9.87   -32.011 1   42.72 ? 231 ARG   B CZ  1 
ATOM   4827 N  NH1 . ARG   B 1 246 ? -29.646 -10.6   -32.97  1   43.4  ? 231 ARG   B NH1 1 
ATOM   4828 N  NH2 . ARG   B 1 246 ? -28.339 -8.829  -32.339 1   44.49 ? 231 ARG   B NH2 1 
ATOM   4829 N  N   . ILE   B 1 247 ? -33.111 -7.918  -28.472 1   26.38 ? 232 ILE   B N   1 
ATOM   4830 C  CA  . ILE   B 1 247 ? -33.947 -7.071  -29.323 1   27.65 ? 232 ILE   B CA  1 
ATOM   4831 C  C   . ILE   B 1 247 ? -34.458 -5.844  -28.551 1   25.84 ? 232 ILE   B C   1 
ATOM   4832 O  O   . ILE   B 1 247 ? -34.34  -4.711  -29.023 1   26.18 ? 232 ILE   B O   1 
ATOM   4833 C  CB  . ILE   B 1 247 ? -35.168 -7.936  -29.808 1   30.96 ? 232 ILE   B CB  1 
ATOM   4834 C  CG1 . ILE   B 1 247 ? -34.742 -9.135  -30.725 1   34.32 ? 232 ILE   B CG1 1 
ATOM   4835 C  CG2 . ILE   B 1 247 ? -36.267 -7.083  -30.432 1   32.14 ? 232 ILE   B CG2 1 
ATOM   4836 C  CD1 . ILE   B 1 247 ? -33.489 -8.916  -31.68  1   36.57 ? 232 ILE   B CD1 1 
ATOM   4837 N  N   . TYR   B 1 248 ? -35.019 -6.075  -27.363 1   23.96 ? 233 TYR   B N   1 
ATOM   4838 C  CA  . TYR   B 1 248 ? -35.667 -5.022  -26.593 1   25.1  ? 233 TYR   B CA  1 
ATOM   4839 C  C   . TYR   B 1 248 ? -34.694 -4.119  -25.817 1   27.61 ? 233 TYR   B C   1 
ATOM   4840 O  O   . TYR   B 1 248 ? -35.101 -3.064  -25.314 1   28.84 ? 233 TYR   B O   1 
ATOM   4841 C  CB  . TYR   B 1 248 ? -36.727 -5.643  -25.679 1   24.79 ? 233 TYR   B CB  1 
ATOM   4842 C  CG  . TYR   B 1 248 ? -37.733 -6.423  -26.504 1   25.8  ? 233 TYR   B CG  1 
ATOM   4843 C  CD1 . TYR   B 1 248 ? -38.691 -5.764  -27.272 1   26.46 ? 233 TYR   B CD1 1 
ATOM   4844 C  CD2 . TYR   B 1 248 ? -37.608 -7.8    -26.661 1   26.25 ? 233 TYR   B CD2 1 
ATOM   4845 C  CE1 . TYR   B 1 248 ? -39.55  -6.469  -28.115 1   27.32 ? 233 TYR   B CE1 1 
ATOM   4846 C  CE2 . TYR   B 1 248 ? -38.457 -8.513  -27.499 1   27.11 ? 233 TYR   B CE2 1 
ATOM   4847 C  CZ  . TYR   B 1 248 ? -39.445 -7.846  -28.202 1   28.44 ? 233 TYR   B CZ  1 
ATOM   4848 O  OH  . TYR   B 1 248 ? -40.278 -8.555  -29.036 1   30.44 ? 233 TYR   B OH  1 
ATOM   4849 N  N   . LEU   B 1 249 ? -33.428 -4.521  -25.718 1   27.78 ? 234 LEU   B N   1 
ATOM   4850 C  CA  . LEU   B 1 249 ? -32.413 -3.688  -25.068 1   28.38 ? 234 LEU   B CA  1 
ATOM   4851 C  C   . LEU   B 1 249 ? -31.886 -2.616  -26.07  1   29.32 ? 234 LEU   B C   1 
ATOM   4852 O  O   . LEU   B 1 249 ? -31.317 -1.625  -25.629 1   29.51 ? 234 LEU   B O   1 
ATOM   4853 C  CB  . LEU   B 1 249 ? -31.223 -4.555  -24.599 1   28.58 ? 234 LEU   B CB  1 
ATOM   4854 C  CG  . LEU   B 1 249 ? -31.504 -5.73   -23.673 1   30.45 ? 234 LEU   B CG  1 
ATOM   4855 C  CD1 . LEU   B 1 249 ? -30.215 -6.511  -23.351 1   31.67 ? 234 LEU   B CD1 1 
ATOM   4856 C  CD2 . LEU   B 1 249 ? -32.241 -5.283  -22.416 1   31.59 ? 234 LEU   B CD2 1 
ATOM   4857 N  N   . SER   B 1 250 ? -32.108 -2.794  -27.401 1   29.3  ? 235 SER   B N   1 
ATOM   4858 C  CA  . SER   B 1 250 ? -31.567 -1.915  -28.437 1   29.87 ? 235 SER   B CA  1 
ATOM   4859 C  C   . SER   B 1 250 ? -32.163 -0.544  -28.5   1   29.11 ? 235 SER   B C   1 
ATOM   4860 O  O   . SER   B 1 250 ? -33.372 -0.4    -28.4   1   29.41 ? 235 SER   B O   1 
ATOM   4861 C  CB  . SER   B 1 250 ? -31.724 -2.555  -29.809 1   32.41 ? 235 SER   B CB  1 
ATOM   4862 O  OG  . SER   B 1 250 ? -30.97  -3.745  -29.839 1   37.72 ? 235 SER   B OG  1 
ATOM   4863 N  N   . GLY   B 1 251 ? -31.331 0.436   -28.803 1   27.89 ? 236 GLY   B N   1 
ATOM   4864 C  CA  . GLY   B 1 251 ? -31.789 1.798   -28.986 1   28.29 ? 236 GLY   B CA  1 
ATOM   4865 C  C   . GLY   B 1 251 ? -31.697 2.252   -30.428 1   29.09 ? 236 GLY   B C   1 
ATOM   4866 O  O   . GLY   B 1 251 ? -31.647 1.431   -31.348 1   29.24 ? 236 GLY   B O   1 
ATOM   4867 N  N   . TRP   B 1 252 ? -31.664 3.563   -30.639 1   28.81 ? 237 TRP   B N   1 
ATOM   4868 C  CA  . TRP   B 1 252 ? -31.649 4.105   -31.991 1   29.73 ? 237 TRP   B CA  1 
ATOM   4869 C  C   . TRP   B 1 252 ? -30.605 5.2     -32.156 1   32.37 ? 237 TRP   B C   1 
ATOM   4870 O  O   . TRP   B 1 252 ? -30.947 6.336   -32.441 1   32.91 ? 237 TRP   B O   1 
ATOM   4871 C  CB  . TRP   B 1 252 ? -33.059 4.578   -32.453 1   27.98 ? 237 TRP   B CB  1 
ATOM   4872 C  CG  . TRP   B 1 252 ? -33.966 5.075   -31.367 1   26.03 ? 237 TRP   B CG  1 
ATOM   4873 C  CD1 . TRP   B 1 252 ? -34.124 6.363   -30.944 1   26.22 ? 237 TRP   B CD1 1 
ATOM   4874 C  CD2 . TRP   B 1 252 ? -34.835 4.272   -30.552 1   25.15 ? 237 TRP   B CD2 1 
ATOM   4875 N  NE1 . TRP   B 1 252 ? -35.063 6.414   -29.927 1   25.88 ? 237 TRP   B NE1 1 
ATOM   4876 C  CE2 . TRP   B 1 252 ? -35.489 5.138   -29.651 1   25.41 ? 237 TRP   B CE2 1 
ATOM   4877 C  CE3 . TRP   B 1 252 ? -35.107 2.9     -30.485 1   25.07 ? 237 TRP   B CE3 1 
ATOM   4878 C  CZ2 . TRP   B 1 252 ? -36.405 4.675   -28.714 1   25.68 ? 237 TRP   B CZ2 1 
ATOM   4879 C  CZ3 . TRP   B 1 252 ? -36.018 2.444   -29.553 1   24.96 ? 237 TRP   B CZ3 1 
ATOM   4880 C  CH2 . TRP   B 1 252 ? -36.627 3.317   -28.664 1   25.34 ? 237 TRP   B CH2 1 
ATOM   4881 N  N   . LYS   B 1 253 ? -29.338 4.866   -31.941 1   33.42 ? 238 LYS   B N   1 
ATOM   4882 C  CA  . LYS   B 1 253 ? -28.24  5.803   -32.158 1   34.81 ? 238 LYS   B CA  1 
ATOM   4883 C  C   . LYS   B 1 253 ? -27.168 4.966   -32.814 1   37.69 ? 238 LYS   B C   1 
ATOM   4884 O  O   . LYS   B 1 253 ? -26.683 4.021   -32.2   1   38.55 ? 238 LYS   B O   1 
ATOM   4885 C  CB  . LYS   B 1 253 ? -27.736 6.408   -30.852 1   35.28 ? 238 LYS   B CB  1 
ATOM   4886 C  CG  . LYS   B 1 253 ? -26.677 7.49    -31.078 1   37.92 ? 238 LYS   B CG  1 
ATOM   4887 C  CD  . LYS   B 1 253 ? -26.159 8.034   -29.763 1   41.21 ? 238 LYS   B CD  1 
ATOM   4888 C  CE  . LYS   B 1 253 ? -24.923 8.887   -29.951 1   44.35 ? 238 LYS   B CE  1 
ATOM   4889 N  NZ  . LYS   B 1 253 ? -25.233 10.11   -30.735 1   45.78 ? 238 LYS   B NZ  1 
ATOM   4890 N  N   . GLY   B 1 254 ? -26.866 5.253   -34.074 1   39.11 ? 239 GLY   B N   1 
ATOM   4891 C  CA  . GLY   B 1 254 ? -25.929 4.444   -34.842 1   40.43 ? 239 GLY   B CA  1 
ATOM   4892 C  C   . GLY   B 1 254 ? -26.5   3.066   -35.156 1   41.69 ? 239 GLY   B C   1 
ATOM   4893 O  O   . GLY   B 1 254 ? -25.746 2.109   -35.357 1   42.85 ? 239 GLY   B O   1 
ATOM   4894 N  N   . ASN   B 1 255 ? -27.835 2.935   -35.171 1   41    ? 240 ASN   B N   1 
ATOM   4895 C  CA  . ASN   B 1 255 ? -28.483 1.654   -35.425 1   40.88 ? 240 ASN   B CA  1 
ATOM   4896 C  C   . ASN   B 1 255 ? -28.915 1.604   -36.874 1   42.15 ? 240 ASN   B C   1 
ATOM   4897 O  O   . ASN   B 1 255 ? -29.752 2.397   -37.276 1   42.48 ? 240 ASN   B O   1 
ATOM   4898 C  CB  . ASN   B 1 255 ? -29.703 1.469   -34.5   1   39.53 ? 240 ASN   B CB  1 
ATOM   4899 C  CG  . ASN   B 1 255 ? -30.207 0.054   -34.48  1   38.97 ? 240 ASN   B CG  1 
ATOM   4900 O  OD1 . ASN   B 1 255 ? -30.014 -0.702  -35.429 1   39.55 ? 240 ASN   B OD1 1 
ATOM   4901 N  ND2 . ASN   B 1 255 ? -30.87  -0.344  -33.411 1   37.13 ? 240 ASN   B ND2 1 
ATOM   4902 N  N   . PRO   B 1 256 ? -28.396 0.648   -37.663 1   43.11 ? 241 PRO   B N   1 
ATOM   4903 C  CA  . PRO   B 1 256 ? -28.79  0.577   -39.082 1   43.7  ? 241 PRO   B CA  1 
ATOM   4904 C  C   . PRO   B 1 256 ? -30.286 0.352   -39.314 1   44.43 ? 241 PRO   B C   1 
ATOM   4905 O  O   . PRO   B 1 256 ? -30.801 0.748   -40.36  1   44.56 ? 241 PRO   B O   1 
ATOM   4906 C  CB  . PRO   B 1 256 ? -27.936 -0.574  -39.639 1   44.42 ? 241 PRO   B CB  1 
ATOM   4907 C  CG  . PRO   B 1 256 ? -26.807 -0.752  -38.659 1   44.78 ? 241 PRO   B CG  1 
ATOM   4908 C  CD  . PRO   B 1 256 ? -27.375 -0.366  -37.322 1   43    ? 241 PRO   B CD  1 
ATOM   4909 N  N   . GLN   B 1 257 ? -30.997 -0.226  -38.325 1   44.72 ? 242 GLN   B N   1 
ATOM   4910 C  CA  . GLN   B 1 257 ? -32.442 -0.442  -38.427 1   45.64 ? 242 GLN   B CA  1 
ATOM   4911 C  C   . GLN   B 1 257 ? -33.257 0.866   -38.323 1   46.45 ? 242 GLN   B C   1 
ATOM   4912 O  O   . GLN   B 1 257 ? -34.384 0.926   -38.821 1   47.15 ? 242 GLN   B O   1 
ATOM   4913 C  CB  . GLN   B 1 257 ? -32.916 -1.476  -37.4   1   47.19 ? 242 GLN   B CB  1 
ATOM   4914 C  CG  . GLN   B 1 257 ? -32.321 -2.853  -37.619 1   50.57 ? 242 GLN   B CG  1 
ATOM   4915 C  CD  . GLN   B 1 257 ? -33.062 -3.899  -36.828 1   57.17 ? 242 GLN   B CD  1 
ATOM   4916 O  OE1 . GLN   B 1 257 ? -32.641 -4.321  -35.75  1   59.3  ? 242 GLN   B OE1 1 
ATOM   4917 N  NE2 . GLN   B 1 257 ? -34.19  -4.344  -37.344 1   58.49 ? 242 GLN   B NE2 1 
ATOM   4918 N  N   . LEU   B 1 258 ? -32.694 1.903   -37.673 1   46.06 ? 243 LEU   B N   1 
ATOM   4919 C  CA  . LEU   B 1 258 ? -33.303 3.233   -37.543 1   46.49 ? 243 LEU   B CA  1 
ATOM   4920 C  C   . LEU   B 1 258 ? -32.151 4.241   -37.669 1   46.23 ? 243 LEU   B C   1 
ATOM   4921 O  O   . LEU   B 1 258 ? -31.821 4.942   -36.71  1   45.77 ? 243 LEU   B O   1 
ATOM   4922 C  CB  . LEU   B 1 258 ? -34.008 3.441   -36.189 1   47.29 ? 243 LEU   B CB  1 
ATOM   4923 C  CG  . LEU   B 1 258 ? -35.37  2.89    -35.994 1   49.84 ? 243 LEU   B CG  1 
ATOM   4924 C  CD1 . LEU   B 1 258 ? -35.244 1.544   -35.432 1   50.96 ? 243 LEU   B CD1 1 
ATOM   4925 C  CD2 . LEU   B 1 258 ? -36.141 3.728   -34.977 1   50.55 ? 243 LEU   B CD2 1 
ATOM   4926 N  N   . SER   B 1 259 ? -31.514 4.287   -38.848 1   46.46 ? 244 SER   B N   1 
ATOM   4927 C  CA  . SER   B 1 259 ? -30.336 5.116   -39.097 1   47.4  ? 244 SER   B CA  1 
ATOM   4928 C  C   . SER   B 1 259 ? -30.491 6.606   -38.775 1   47.68 ? 244 SER   B C   1 
ATOM   4929 O  O   . SER   B 1 259 ? -29.491 7.232   -38.456 1   48.17 ? 244 SER   B O   1 
ATOM   4930 C  CB  . SER   B 1 259 ? -29.835 4.938   -40.526 1   49.74 ? 244 SER   B CB  1 
ATOM   4931 O  OG  . SER   B 1 259 ? -30.822 5.302   -41.478 1   53.52 ? 244 SER   B OG  1 
ATOM   4932 N  N   . ASP   B 1 260 ? -31.701 7.175   -38.83  1   47.44 ? 245 ASP   B N   1 
ATOM   4933 C  CA  . ASP   B 1 260 ? -31.898 8.595   -38.486 1   47.49 ? 245 ASP   B CA  1 
ATOM   4934 C  C   . ASP   B 1 260 ? -32.495 8.826   -37.092 1   46.11 ? 245 ASP   B C   1 
ATOM   4935 O  O   . ASP   B 1 260 ? -32.651 9.974   -36.677 1   46.72 ? 245 ASP   B O   1 
ATOM   4936 C  CB  . ASP   B 1 260 ? -32.801 9.272   -39.522 1   51.12 ? 245 ASP   B CB  1 
ATOM   4937 C  CG  . ASP   B 1 260 ? -32.227 9.171   -40.908 1   58.94 ? 245 ASP   B CG  1 
ATOM   4938 O  OD1 . ASP   B 1 260 ? -31.078 9.624   -41.104 1   59.96 ? 245 ASP   B OD1 1 
ATOM   4939 O  OD2 . ASP   B 1 260 ? -32.914 8.611   -41.795 1   62.96 ? 245 ASP   B OD2 1 
ATOM   4940 N  N   . GLY   B 1 261 ? -32.845 7.755   -36.394 1   44.18 ? 246 GLY   B N   1 
ATOM   4941 C  CA  . GLY   B 1 261 ? -33.462 7.862   -35.09  1   42.84 ? 246 GLY   B CA  1 
ATOM   4942 C  C   . GLY   B 1 261 ? -34.95  7.637   -35.151 1   41.86 ? 246 GLY   B C   1 
ATOM   4943 O  O   . GLY   B 1 261 ? -35.477 7.098   -36.128 1   42.02 ? 246 GLY   B O   1 
ATOM   4944 N  N   . LEU   B 1 262 ? -35.644 8.041   -34.089 1   40.47 ? 247 LEU   B N   1 
ATOM   4945 C  CA  . LEU   B 1 262 ? -37.067 7.821   -33.945 1   38.86 ? 247 LEU   B CA  1 
ATOM   4946 C  C   . LEU   B 1 262 ? -37.819 9.134   -33.96  1   38.03 ? 247 LEU   B C   1 
ATOM   4947 O  O   . LEU   B 1 262 ? -37.346 10.101  -33.378 1   38.17 ? 247 LEU   B O   1 
ATOM   4948 C  CB  . LEU   B 1 262 ? -37.298 7.125   -32.593 1   38.37 ? 247 LEU   B CB  1 
ATOM   4949 C  CG  . LEU   B 1 262 ? -38.724 6.685   -32.291 1   39.17 ? 247 LEU   B CG  1 
ATOM   4950 C  CD1 . LEU   B 1 262 ? -39.169 5.572   -33.256 1   39.87 ? 247 LEU   B CD1 1 
ATOM   4951 C  CD2 . LEU   B 1 262 ? -38.888 6.263   -30.83  1   38.86 ? 247 LEU   B CD2 1 
ATOM   4952 N  N   . VAL   B 1 263 ? -38.994 9.173   -34.603 1   37.17 ? 248 VAL   B N   1 
ATOM   4953 C  CA  . VAL   B 1 263 ? -39.818 10.384  -34.586 1   36.77 ? 248 VAL   B CA  1 
ATOM   4954 C  C   . VAL   B 1 263 ? -40.694 10.342  -33.343 1   35.65 ? 248 VAL   B C   1 
ATOM   4955 O  O   . VAL   B 1 263 ? -41.467 9.416   -33.191 1   35.76 ? 248 VAL   B O   1 
ATOM   4956 C  CB  . VAL   B 1 263 ? -40.687 10.548  -35.867 1   37.33 ? 248 VAL   B CB  1 
ATOM   4957 C  CG1 . VAL   B 1 263 ? -41.542 11.809  -35.778 1   38.04 ? 248 VAL   B CG1 1 
ATOM   4958 C  CG2 . VAL   B 1 263 ? -39.815 10.575  -37.117 1   37.39 ? 248 VAL   B CG2 1 
ATOM   4959 N  N   . TYR   B 1 264 ? -40.581 11.331  -32.455 1   35.4  ? 249 TYR   B N   1 
ATOM   4960 C  CA  . TYR   B 1 264 ? -41.435 11.436  -31.271 1   36.17 ? 249 TYR   B CA  1 
ATOM   4961 C  C   . TYR   B 1 264 ? -42.558 12.386  -31.695 1   39.05 ? 249 TYR   B C   1 
ATOM   4962 O  O   . TYR   B 1 264 ? -42.463 13.593  -31.492 1   39.39 ? 249 TYR   B O   1 
ATOM   4963 C  CB  . TYR   B 1 264 ? -40.659 12.025  -30.083 1   35.07 ? 249 TYR   B CB  1 
ATOM   4964 C  CG  . TYR   B 1 264 ? -39.595 11.069  -29.581 1   34.32 ? 249 TYR   B CG  1 
ATOM   4965 C  CD1 . TYR   B 1 264 ? -38.396 10.918  -30.257 1   34.47 ? 249 TYR   B CD1 1 
ATOM   4966 C  CD2 . TYR   B 1 264 ? -39.84  10.235  -28.5   1   34.95 ? 249 TYR   B CD2 1 
ATOM   4967 C  CE1 . TYR   B 1 264 ? -37.444 9.996   -29.846 1   34.99 ? 249 TYR   B CE1 1 
ATOM   4968 C  CE2 . TYR   B 1 264 ? -38.892 9.311   -28.073 1   35.4  ? 249 TYR   B CE2 1 
ATOM   4969 C  CZ  . TYR   B 1 264 ? -37.697 9.189   -28.755 1   35.64 ? 249 TYR   B CZ  1 
ATOM   4970 O  OH  . TYR   B 1 264 ? -36.734 8.295   -28.331 1   35.48 ? 249 TYR   B OH  1 
ATOM   4971 N  N   . GLU   B 1 265 ? -43.576 11.837  -32.364 1   40.44 ? 250 GLU   B N   1 
ATOM   4972 C  CA  . GLU   B 1 265 ? -44.674 12.6    -32.956 1   41.45 ? 250 GLU   B CA  1 
ATOM   4973 C  C   . GLU   B 1 265 ? -45.319 13.577  -32.009 1   41.9  ? 250 GLU   B C   1 
ATOM   4974 O  O   . GLU   B 1 265 ? -45.655 13.212  -30.898 1   41.83 ? 250 GLU   B O   1 
ATOM   4975 C  CB  . GLU   B 1 265 ? -45.709 11.626  -33.519 1   44.32 ? 250 GLU   B CB  1 
ATOM   4976 C  CG  . GLU   B 1 265 ? -46.841 12.296  -34.266 1   48.52 ? 250 GLU   B CG  1 
ATOM   4977 C  CD  . GLU   B 1 265 ? -47.816 11.269  -34.789 1   52.37 ? 250 GLU   B CD  1 
ATOM   4978 O  OE1 . GLU   B 1 265 ? -48.557 10.672  -33.97  1   51.16 ? 250 GLU   B OE1 1 
ATOM   4979 O  OE2 . GLU   B 1 265 ? -47.815 11.04   -36.02  1   55.74 ? 250 GLU   B OE2 1 
ATOM   4980 N  N   . GLY   B 1 266 ? -45.444 14.824  -32.428 1   42.91 ? 251 GLY   B N   1 
ATOM   4981 C  CA  . GLY   B 1 266 ? -46.066 15.845  -31.589 1   44.15 ? 251 GLY   B CA  1 
ATOM   4982 C  C   . GLY   B 1 266 ? -45.128 16.529  -30.62  1   44.99 ? 251 GLY   B C   1 
ATOM   4983 O  O   . GLY   B 1 266 ? -45.514 17.518  -29.993 1   45.23 ? 251 GLY   B O   1 
ATOM   4984 N  N   . PHE   B 1 267 ? -43.889 16.019  -30.476 1   45.01 ? 252 PHE   B N   1 
ATOM   4985 C  CA  . PHE   B 1 267 ? -42.92  16.661  -29.588 1   45.31 ? 252 PHE   B CA  1 
ATOM   4986 C  C   . PHE   B 1 267 ? -41.789 17.31   -30.39  1   46.37 ? 252 PHE   B C   1 
ATOM   4987 O  O   . PHE   B 1 267 ? -41.466 18.464  -30.148 1   46.32 ? 252 PHE   B O   1 
ATOM   4988 C  CB  . PHE   B 1 267 ? -42.385 15.699  -28.525 1   44.68 ? 252 PHE   B CB  1 
ATOM   4989 C  CG  . PHE   B 1 267 ? -41.829 16.435  -27.324 1   44.5  ? 252 PHE   B CG  1 
ATOM   4990 C  CD1 . PHE   B 1 267 ? -42.659 16.841  -26.294 1   44.54 ? 252 PHE   B CD1 1 
ATOM   4991 C  CD2 . PHE   B 1 267 ? -40.479 16.72   -27.229 1   44.82 ? 252 PHE   B CD2 1 
ATOM   4992 C  CE1 . PHE   B 1 267 ? -42.148 17.517  -25.191 1   45.15 ? 252 PHE   B CE1 1 
ATOM   4993 C  CE2 . PHE   B 1 267 ? -39.969 17.388  -26.118 1   45.38 ? 252 PHE   B CE2 1 
ATOM   4994 C  CZ  . PHE   B 1 267 ? -40.807 17.786  -25.109 1   44.91 ? 252 PHE   B CZ  1 
ATOM   4995 N  N   . TRP   B 1 268 ? -41.19  16.576  -31.335 1   47.27 ? 253 TRP   B N   1 
ATOM   4996 C  CA  . TRP   B 1 268 ? -40.126 17.096  -32.2   1   48.87 ? 253 TRP   B CA  1 
ATOM   4997 C  C   . TRP   B 1 268 ? -40.497 16.8    -33.652 1   50.85 ? 253 TRP   B C   1 
ATOM   4998 O  O   . TRP   B 1 268 ? -41.09  15.764  -33.931 1   50.96 ? 253 TRP   B O   1 
ATOM   4999 C  CB  . TRP   B 1 268 ? -38.772 16.436  -31.899 1   48.72 ? 253 TRP   B CB  1 
ATOM   5000 C  CG  . TRP   B 1 268 ? -38.165 16.789  -30.574 1   49.51 ? 253 TRP   B CG  1 
ATOM   5001 C  CD1 . TRP   B 1 268 ? -37.795 18.03   -30.147 1   50.41 ? 253 TRP   B CD1 1 
ATOM   5002 C  CD2 . TRP   B 1 268 ? -37.742 15.869  -29.552 1   49.47 ? 253 TRP   B CD2 1 
ATOM   5003 N  NE1 . TRP   B 1 268 ? -37.214 17.948  -28.899 1   50.67 ? 253 TRP   B NE1 1 
ATOM   5004 C  CE2 . TRP   B 1 268 ? -37.166 16.631  -28.514 1   50.36 ? 253 TRP   B CE2 1 
ATOM   5005 C  CE3 . TRP   B 1 268 ? -37.813 14.476  -29.404 1   49.58 ? 253 TRP   B CE3 1 
ATOM   5006 C  CZ2 . TRP   B 1 268 ? -36.666 16.046  -27.348 1   50.88 ? 253 TRP   B CZ2 1 
ATOM   5007 C  CZ3 . TRP   B 1 268 ? -37.296 13.898  -28.259 1   50.3  ? 253 TRP   B CZ3 1 
ATOM   5008 C  CH2 . TRP   B 1 268 ? -36.753 14.679  -27.238 1   50.7  ? 253 TRP   B CH2 1 
ATOM   5009 N  N   . GLU   B 1 269 ? -40.141 17.684  -34.58  1   52.2  ? 254 GLU   B N   1 
ATOM   5010 C  CA  . GLU   B 1 269 ? -40.469 17.467  -35.997 1   53.52 ? 254 GLU   B CA  1 
ATOM   5011 C  C   . GLU   B 1 269 ? -39.584 16.388  -36.626 1   53.61 ? 254 GLU   B C   1 
ATOM   5012 O  O   . GLU   B 1 269 ? -40.088 15.512  -37.332 1   54.27 ? 254 GLU   B O   1 
ATOM   5013 C  CB  . GLU   B 1 269 ? -40.344 18.778  -36.798 1   57.15 ? 254 GLU   B CB  1 
ATOM   5014 C  CG  . GLU   B 1 269 ? -41.103 19.946  -36.19  1   63.75 ? 254 GLU   B CG  1 
ATOM   5015 C  CD  . GLU   B 1 269 ? -40.627 21.312  -36.65  1   70.97 ? 254 GLU   B CD  1 
ATOM   5016 O  OE1 . GLU   B 1 269 ? -40.912 22.306  -35.943 1   72.41 ? 254 GLU   B OE1 1 
ATOM   5017 O  OE2 . GLU   B 1 269 ? -39.955 21.387  -37.706 1   72.87 ? 254 GLU   B OE2 1 
ATOM   5018 N  N   . ASP   B 1 270 ? -38.268 16.457  -36.382 1   52.56 ? 255 ASP   B N   1 
ATOM   5019 C  CA  . ASP   B 1 270 ? -37.291 15.54   -36.973 1   52.02 ? 255 ASP   B CA  1 
ATOM   5020 C  C   . ASP   B 1 270 ? -36.987 14.327  -36.085 1   50    ? 255 ASP   B C   1 
ATOM   5021 O  O   . ASP   B 1 270 ? -37.143 14.404  -34.86  1   50.22 ? 255 ASP   B O   1 
ATOM   5022 C  CB  . ASP   B 1 270 ? -35.994 16.309  -37.27  1   55.19 ? 255 ASP   B CB  1 
ATOM   5023 C  CG  . ASP   B 1 270 ? -36.207 17.539  -38.136 1   61.56 ? 255 ASP   B CG  1 
ATOM   5024 O  OD1 . ASP   B 1 270 ? -36.793 17.395  -39.241 1   62.37 ? 255 ASP   B OD1 1 
ATOM   5025 O  OD2 . ASP   B 1 270 ? -35.79  18.647  -37.711 1   64.1  ? 255 ASP   B OD2 1 
ATOM   5026 N  N   . PRO   B 1 271 ? -36.558 13.194  -36.681 1   47.86 ? 256 PRO   B N   1 
ATOM   5027 C  CA  . PRO   B 1 271 ? -36.225 12.028  -35.849 1   46.52 ? 256 PRO   B CA  1 
ATOM   5028 C  C   . PRO   B 1 271 ? -35.01  12.31   -34.964 1   44.86 ? 256 PRO   B C   1 
ATOM   5029 O  O   . PRO   B 1 271 ? -34.131 13.089  -35.342 1   45.47 ? 256 PRO   B O   1 
ATOM   5030 C  CB  . PRO   B 1 271 ? -35.968 10.916  -36.869 1   47.2  ? 256 PRO   B CB  1 
ATOM   5031 C  CG  . PRO   B 1 271 ? -35.563 11.616  -38.101 1   48.03 ? 256 PRO   B CG  1 
ATOM   5032 C  CD  . PRO   B 1 271 ? -36.306 12.931  -38.11  1   47.01 ? 256 PRO   B CD  1 
ATOM   5033 N  N   . LYS   B 1 272 ? -34.99  11.724  -33.759 1   42.58 ? 257 LYS   B N   1 
ATOM   5034 C  CA  . LYS   B 1 272 ? -33.908 11.941  -32.802 1   40.29 ? 257 LYS   B CA  1 
ATOM   5035 C  C   . LYS   B 1 272 ? -33.245 10.612  -32.444 1   38.38 ? 257 LYS   B C   1 
ATOM   5036 O  O   . LYS   B 1 272 ? -33.917 9.6     -32.276 1   37.51 ? 257 LYS   B O   1 
ATOM   5037 C  CB  . LYS   B 1 272 ? -34.438 12.591  -31.517 1   41.31 ? 257 LYS   B CB  1 
ATOM   5038 C  CG  . LYS   B 1 272 ? -35.184 13.903  -31.734 1   44.55 ? 257 LYS   B CG  1 
ATOM   5039 C  CD  . LYS   B 1 272 ? -34.27  15.012  -32.211 1   48.03 ? 257 LYS   B CD  1 
ATOM   5040 C  CE  . LYS   B 1 272 ? -35.034 16.274  -32.538 1   50.89 ? 257 LYS   B CE  1 
ATOM   5041 N  NZ  . LYS   B 1 272 ? -34.285 17.14   -33.488 1   53.21 ? 257 LYS   B NZ  1 
ATOM   5042 N  N   . GLU   B 1 273 ? -31.93  10.644  -32.277 1   37.25 ? 258 GLU   B N   1 
ATOM   5043 C  CA  . GLU   B 1 273 ? -31.178 9.454   -31.919 1   36.21 ? 258 GLU   B CA  1 
ATOM   5044 C  C   . GLU   B 1 273 ? -30.872 9.427   -30.446 1   34.81 ? 258 GLU   B C   1 
ATOM   5045 O  O   . GLU   B 1 273 ? -30.379 10.429  -29.909 1   35.29 ? 258 GLU   B O   1 
ATOM   5046 C  CB  . GLU   B 1 273 ? -29.866 9.4     -32.695 1   38.3  ? 258 GLU   B CB  1 
ATOM   5047 C  CG  . GLU   B 1 273 ? -30.04  9.081   -34.163 1   43.68 ? 258 GLU   B CG  1 
ATOM   5048 C  CD  . GLU   B 1 273 ? -28.712 8.821   -34.84  1   50.02 ? 258 GLU   B CD  1 
ATOM   5049 O  OE1 . GLU   B 1 273 ? -27.893 9.765   -34.909 1   51.86 ? 258 GLU   B OE1 1 
ATOM   5050 O  OE2 . GLU   B 1 273 ? -28.478 7.673   -35.282 1   51.79 ? 258 GLU   B OE2 1 
ATOM   5051 N  N   . PHE   B 1 274 ? -31.139 8.282   -29.79  1   32.58 ? 259 PHE   B N   1 
ATOM   5052 C  CA  . PHE   B 1 274 ? -30.784 8.066   -28.39  1   31.17 ? 259 PHE   B CA  1 
ATOM   5053 C  C   . PHE   B 1 274 ? -30.202 6.661   -28.255 1   28.4  ? 259 PHE   B C   1 
ATOM   5054 O  O   . PHE   B 1 274 ? -30.712 5.72    -28.879 1   27.57 ? 259 PHE   B O   1 
ATOM   5055 C  CB  . PHE   B 1 274 ? -31.977 8.249   -27.437 1   31.51 ? 259 PHE   B CB  1 
ATOM   5056 C  CG  . PHE   B 1 274 ? -32.511 9.658   -27.41  1   32.71 ? 259 PHE   B CG  1 
ATOM   5057 C  CD1 . PHE   B 1 274 ? -31.798 10.678  -26.797 1   33.33 ? 259 PHE   B CD1 1 
ATOM   5058 C  CD2 . PHE   B 1 274 ? -33.692 9.978   -28.058 1   33.72 ? 259 PHE   B CD2 1 
ATOM   5059 C  CE1 . PHE   B 1 274 ? -32.27  11.988  -26.815 1   33.95 ? 259 PHE   B CE1 1 
ATOM   5060 C  CE2 . PHE   B 1 274 ? -34.167 11.286  -28.065 1   34.24 ? 259 PHE   B CE2 1 
ATOM   5061 C  CZ  . PHE   B 1 274 ? -33.445 12.285  -27.459 1   33.63 ? 259 PHE   B CZ  1 
ATOM   5062 N  N   . ALA   B 1 275 ? -29.144 6.515   -27.445 1   26.6  ? 260 ALA   B N   1 
ATOM   5063 C  CA  . ALA   B 1 275 ? -28.545 5.2     -27.243 1   26.58 ? 260 ALA   B CA  1 
ATOM   5064 C  C   . ALA   B 1 275 ? -29.462 4.318   -26.397 1   25.79 ? 260 ALA   B C   1 
ATOM   5065 O  O   . ALA   B 1 275 ? -30.158 4.832   -25.533 1   26.78 ? 260 ALA   B O   1 
ATOM   5066 C  CB  . ALA   B 1 275 ? -27.189 5.34    -26.555 1   26.77 ? 260 ALA   B CB  1 
ATOM   5067 N  N   . GLY   B 1 276 ? -29.435 3.002   -26.619 1   24.93 ? 261 GLY   B N   1 
ATOM   5068 C  CA  . GLY   B 1 276 ? -30.21  2.065   -25.808 1   24.03 ? 261 GLY   B CA  1 
ATOM   5069 C  C   . GLY   B 1 276 ? -29.643 1.936   -24.409 1   23.5  ? 261 GLY   B C   1 
ATOM   5070 O  O   . GLY   B 1 276 ? -28.577 2.477   -24.114 1   24.27 ? 261 GLY   B O   1 
ATOM   5071 N  N   . GLY   B 1 277 ? -30.382 1.295   -23.513 1   22.02 ? 262 GLY   B N   1 
ATOM   5072 C  CA  . GLY   B 1 277 ? -29.965 1.141   -22.127 1   21.77 ? 262 GLY   B CA  1 
ATOM   5073 C  C   . GLY   B 1 277 ? -28.653 0.398   -22.021 1   20.59 ? 262 GLY   B C   1 
ATOM   5074 O  O   . GLY   B 1 277 ? -28.391 -0.523  -22.806 1   20.38 ? 262 GLY   B O   1 
ATOM   5075 N  N   . SER   B 1 278 ? -27.801 0.812   -21.082 1   19.66 ? 263 SER   B N   1 
ATOM   5076 C  CA  . SER   B 1 278 ? -26.487 0.205   -20.959 1   19.82 ? 263 SER   B CA  1 
ATOM   5077 C  C   . SER   B 1 278 ? -26.014 0.199   -19.547 1   20.32 ? 263 SER   B C   1 
ATOM   5078 O  O   . SER   B 1 278 ? -26.234 1.179   -18.853 1   20.83 ? 263 SER   B O   1 
ATOM   5079 C  CB  . SER   B 1 278 ? -25.472 1.003   -21.806 1   20.09 ? 263 SER   B CB  1 
ATOM   5080 O  OG  . SER   B 1 278 ? -24.155 0.495   -21.695 1   21.39 ? 263 SER   B OG  1 
ATOM   5081 N  N   . ALA   B 1 279 ? -25.274 -0.861  -19.127 1   20.39 ? 264 ALA   B N   1 
ATOM   5082 C  CA  . ALA   B 1 279 ? -24.65  -0.83   -17.813 1   19.49 ? 264 ALA   B CA  1 
ATOM   5083 C  C   . ALA   B 1 279 ? -23.471 0.18    -17.796 1   19.93 ? 264 ALA   B C   1 
ATOM   5084 O  O   . ALA   B 1 279 ? -22.974 0.479   -16.73  1   20.49 ? 264 ALA   B O   1 
ATOM   5085 C  CB  . ALA   B 1 279 ? -24.23  -2.21   -17.356 1   19.04 ? 264 ALA   B CB  1 
ATOM   5086 N  N   . GLY   B 1 280 ? -23.083 0.758   -18.938 1   20.49 ? 265 GLY   B N   1 
ATOM   5087 C  CA  . GLY   B 1 280 ? -22.182 1.915   -18.964 1   21.39 ? 265 GLY   B CA  1 
ATOM   5088 C  C   . GLY   B 1 280 ? -22.859 3.114   -18.276 1   21.17 ? 265 GLY   B C   1 
ATOM   5089 O  O   . GLY   B 1 280 ? -22.197 4.089   -17.93  1   21.38 ? 265 GLY   B O   1 
ATOM   5090 N  N   . GLN   B 1 281 ? -24.208 3.044   -18.047 1   20.33 ? 266 GLN   B N   1 
ATOM   5091 C  CA  . GLN   B 1 281 ? -24.988 4.036   -17.299 1   19.2  ? 266 GLN   B CA  1 
ATOM   5092 C  C   . GLN   B 1 281 ? -24.993 3.75    -15.808 1   19.37 ? 266 GLN   B C   1 
ATOM   5093 O  O   . GLN   B 1 281 ? -25.587 4.521   -15.058 1   20.33 ? 266 GLN   B O   1 
ATOM   5094 C  CB  . GLN   B 1 281 ? -26.435 4.16    -17.857 1   19.59 ? 266 GLN   B CB  1 
ATOM   5095 C  CG  . GLN   B 1 281 ? -26.46  4.509   -19.328 1   18.85 ? 266 GLN   B CG  1 
ATOM   5096 C  CD  . GLN   B 1 281 ? -27.743 4.118   -20.048 1   20.88 ? 266 GLN   B CD  1 
ATOM   5097 O  OE1 . GLN   B 1 281 ? -28.615 3.41    -19.524 1   21.8  ? 266 GLN   B OE1 1 
ATOM   5098 N  NE2 . GLN   B 1 281 ? -27.858 4.513   -21.293 1   20.07 ? 266 GLN   B NE2 1 
ATOM   5099 N  N   . SER   B 1 282 ? -24.362 2.643   -15.348 1   20.12 ? 267 SER   B N   1 
ATOM   5100 C  CA  . SER   B 1 282 ? -24.296 2.356   -13.924 1   20.62 ? 267 SER   B CA  1 
ATOM   5101 C  C   . SER   B 1 282 ? -23.357 3.393   -13.285 1   20.63 ? 267 SER   B C   1 
ATOM   5102 O  O   . SER   B 1 282 ? -22.198 3.538   -13.71  1   22.47 ? 267 SER   B O   1 
ATOM   5103 C  CB  . SER   B 1 282 ? -23.766 0.948   -13.661 1   22.12 ? 267 SER   B CB  1 
ATOM   5104 O  OG  . SER   B 1 282 ? -23.441 0.816   -12.286 1   24.11 ? 267 SER   B OG  1 
ATOM   5105 N  N   . SER   B 1 283 ? -23.854 4.098   -12.283 1   19.27 ? 268 SER   B N   1 
ATOM   5106 C  CA  . SER   B 1 283 ? -23.06  5.102   -11.576 1   20.62 ? 268 SER   B CA  1 
ATOM   5107 C  C   . SER   B 1 283 ? -22.11  4.455   -10.581 1   23.4  ? 268 SER   B C   1 
ATOM   5108 O  O   . SER   B 1 283 ? -21.106 5.081   -10.269 1   24.31 ? 268 SER   B O   1 
ATOM   5109 C  CB  . SER   B 1 283 ? -23.97  6.063   -10.819 1   20.43 ? 268 SER   B CB  1 
ATOM   5110 O  OG  . SER   B 1 283 ? -24.867 6.702   -11.713 1   23.29 ? 268 SER   B OG  1 
ATOM   5111 N  N   . VAL   B 1 284 ? -22.419 3.248   -10.041 1   23.86 ? 269 VAL   B N   1 
ATOM   5112 C  CA  . VAL   B 1 284 ? -21.539 2.643   -9.029  1   24.68 ? 269 VAL   B CA  1 
ATOM   5113 C  C   . VAL   B 1 284 ? -20.2   2.216   -9.656  1   23.98 ? 269 VAL   B C   1 
ATOM   5114 O  O   . VAL   B 1 284 ? -19.151 2.451   -9.037  1   23.54 ? 269 VAL   B O   1 
ATOM   5115 C  CB  . VAL   B 1 284 ? -22.203 1.517   -8.172  1   26.36 ? 269 VAL   B CB  1 
ATOM   5116 C  CG1 . VAL   B 1 284 ? -22.366 0.219   -8.964  1   27.34 ? 269 VAL   B CG1 1 
ATOM   5117 C  CG2 . VAL   B 1 284 ? -21.399 1.253   -6.891  1   27.56 ? 269 VAL   B CG2 1 
ATOM   5118 N  N   . PHE   B 1 285 ? -20.219 1.643   -10.874 1   22.79 ? 270 PHE   B N   1 
ATOM   5119 C  CA  . PHE   B 1 285 ? -18.957 1.256   -11.503 1   23.64 ? 270 PHE   B CA  1 
ATOM   5120 C  C   . PHE   B 1 285 ? -18.159 2.484   -11.951 1   23.17 ? 270 PHE   B C   1 
ATOM   5121 O  O   . PHE   B 1 285 ? -16.944 2.527   -11.722 1   23.77 ? 270 PHE   B O   1 
ATOM   5122 C  CB  . PHE   B 1 285 ? -19.138 0.218   -12.606 1   24.84 ? 270 PHE   B CB  1 
ATOM   5123 C  CG  . PHE   B 1 285 ? -19.455 -1.123  -11.991 1   27.24 ? 270 PHE   B CG  1 
ATOM   5124 C  CD1 . PHE   B 1 285 ? -18.44  -1.974  -11.579 1   29.43 ? 270 PHE   B CD1 1 
ATOM   5125 C  CD2 . PHE   B 1 285 ? -20.766 -1.505  -11.76  1   28.98 ? 270 PHE   B CD2 1 
ATOM   5126 C  CE1 . PHE   B 1 285 ? -18.731 -3.203  -10.99  1   31.02 ? 270 PHE   B CE1 1 
ATOM   5127 C  CE2 . PHE   B 1 285 ? -21.059 -2.731  -11.165 1   30.71 ? 270 PHE   B CE2 1 
ATOM   5128 C  CZ  . PHE   B 1 285 ? -20.04  -3.58   -10.798 1   30.88 ? 270 PHE   B CZ  1 
ATOM   5129 N  N   . GLN   B 1 286 ? -18.835 3.509   -12.496 1   21.43 ? 271 GLN   B N   1 
ATOM   5130 C  CA  . GLN   B 1 286 ? -18.117 4.743   -12.879 1   21.52 ? 271 GLN   B CA  1 
ATOM   5131 C  C   . GLN   B 1 286 ? -17.521 5.416   -11.619 1   22.7  ? 271 GLN   B C   1 
ATOM   5132 O  O   . GLN   B 1 286 ? -16.447 5.981   -11.67  1   22.26 ? 271 GLN   B O   1 
ATOM   5133 C  CB  . GLN   B 1 286 ? -19.02  5.711   -13.661 1   21.18 ? 271 GLN   B CB  1 
ATOM   5134 C  CG  . GLN   B 1 286 ? -19.482 5.157   -15.039 1   21.47 ? 271 GLN   B CG  1 
ATOM   5135 C  CD  . GLN   B 1 286 ? -19.454 6.224   -16.116 1   23.79 ? 271 GLN   B CD  1 
ATOM   5136 O  OE1 . GLN   B 1 286 ? -18.698 7.2     -16.029 1   24.9  ? 271 GLN   B OE1 1 
ATOM   5137 N  NE2 . GLN   B 1 286 ? -20.257 6.064   -17.174 1   19.59 ? 271 GLN   B NE2 1 
ATOM   5138 N  N   . CYS   B 1 287 ? -18.225 5.299   -10.494 1   23.49 ? 272 CYS   B N   1 
ATOM   5139 C  CA  A CYS   B 1 287 ? -17.847 5.884   -9.236  0.6 25.06 ? 272 CYS   B CA  1 
ATOM   5140 C  CA  B CYS   B 1 287 ? -17.821 5.855   -9.209  0.4 24.84 ? 272 CYS   B CA  1 
ATOM   5141 C  C   . CYS   B 1 287 ? -16.518 5.306   -8.696  1   25.67 ? 272 CYS   B C   1 
ATOM   5142 O  O   . CYS   B 1 287 ? -15.679 6.088   -8.274  1   25.75 ? 272 CYS   B O   1 
ATOM   5143 C  CB  A CYS   B 1 287 ? -19.017 5.759   -8.253  0.6 26.49 ? 272 CYS   B CB  1 
ATOM   5144 C  CB  B CYS   B 1 287 ? -18.924 5.702   -8.168  0.4 25.79 ? 272 CYS   B CB  1 
ATOM   5145 S  SG  A CYS   B 1 287 ? -18.568 5.761   -6.505  0.6 32.09 ? 272 CYS   B SG  1 
ATOM   5146 S  SG  B CYS   B 1 287 ? -20.067 7.093   -8.109  0.4 29.41 ? 272 CYS   B SG  1 
ATOM   5147 N  N   . PHE   B 1 288 ? -16.319 3.973   -8.745  1   25.31 ? 273 PHE   B N   1 
ATOM   5148 C  CA  . PHE   B 1 288 ? -15.059 3.407   -8.248  1   26.69 ? 273 PHE   B CA  1 
ATOM   5149 C  C   . PHE   B 1 288 ? -13.898 3.681   -9.231  1   24.33 ? 273 PHE   B C   1 
ATOM   5150 O  O   . PHE   B 1 288 ? -12.773 3.881   -8.765  1   23.61 ? 273 PHE   B O   1 
ATOM   5151 C  CB  . PHE   B 1 288 ? -15.203 1.943   -7.821  1   29.57 ? 273 PHE   B CB  1 
ATOM   5152 C  CG  . PHE   B 1 288 ? -15.995 1.948   -6.528  1   33.3  ? 273 PHE   B CG  1 
ATOM   5153 C  CD1 . PHE   B 1 288 ? -15.485 2.546   -5.388  1   35.9  ? 273 PHE   B CD1 1 
ATOM   5154 C  CD2 . PHE   B 1 288 ? -17.299 1.49    -6.493  1   35.89 ? 273 PHE   B CD2 1 
ATOM   5155 C  CE1 . PHE   B 1 288 ? -16.247 2.637   -4.224  1   37.45 ? 273 PHE   B CE1 1 
ATOM   5156 C  CE2 . PHE   B 1 288 ? -18.066 1.602   -5.334  1   37.26 ? 273 PHE   B CE2 1 
ATOM   5157 C  CZ  . PHE   B 1 288 ? -17.544 2.203   -4.221  1   37.3  ? 273 PHE   B CZ  1 
ATOM   5158 N  N   . ASP   B 1 289 ? -14.167 3.807   -10.554 1   22.1  ? 274 ASP   B N   1 
ATOM   5159 C  CA  . ASP   B 1 289 ? -13.119 4.209   -11.482 1   22.09 ? 274 ASP   B CA  1 
ATOM   5160 C  C   . ASP   B 1 289 ? -12.695 5.659   -11.174 1   22.08 ? 274 ASP   B C   1 
ATOM   5161 O  O   . ASP   B 1 289 ? -11.499 5.949   -11.183 1   22.31 ? 274 ASP   B O   1 
ATOM   5162 C  CB  . ASP   B 1 289 ? -13.564 4.099   -12.934 1   24.24 ? 274 ASP   B CB  1 
ATOM   5163 C  CG  . ASP   B 1 289 ? -13.606 2.66    -13.424 1   29.97 ? 274 ASP   B CG  1 
ATOM   5164 O  OD1 . ASP   B 1 289 ? -12.801 1.835   -12.925 1   30.18 ? 274 ASP   B OD1 1 
ATOM   5165 O  OD2 . ASP   B 1 289 ? -14.413 2.367   -14.33  1   31.32 ? 274 ASP   B OD2 1 
ATOM   5166 N  N   . VAL   B 1 290 ? -13.654 6.553   -10.871 1   21.54 ? 275 VAL   B N   1 
ATOM   5167 C  CA  . VAL   B 1 290 ? -13.307 7.949   -10.538 1   22.83 ? 275 VAL   B CA  1 
ATOM   5168 C  C   . VAL   B 1 290 ? -12.528 7.968   -9.193  1   23.76 ? 275 VAL   B C   1 
ATOM   5169 O  O   . VAL   B 1 290 ? -11.476 8.584   -9.096  1   24.11 ? 275 VAL   B O   1 
ATOM   5170 C  CB  . VAL   B 1 290 ? -14.549 8.887   -10.452 1   23    ? 275 VAL   B CB  1 
ATOM   5171 C  CG1 . VAL   B 1 290 ? -14.167 10.252  -9.864  1   23.31 ? 275 VAL   B CG1 1 
ATOM   5172 C  CG2 . VAL   B 1 290 ? -15.221 9.057   -11.816 1   23.55 ? 275 VAL   B CG2 1 
ATOM   5173 N  N   . LEU   B 1 291 ? -13.066 7.308   -8.158  1   23.93 ? 276 LEU   B N   1 
ATOM   5174 C  CA  . LEU   B 1 291 ? -12.445 7.25    -6.848  1   25.46 ? 276 LEU   B CA  1 
ATOM   5175 C  C   . LEU   B 1 291 ? -10.973 6.785   -6.909  1   26.16 ? 276 LEU   B C   1 
ATOM   5176 O  O   . LEU   B 1 291 ? -10.097 7.419   -6.312  1   27.41 ? 276 LEU   B O   1 
ATOM   5177 C  CB  . LEU   B 1 291 ? -13.244 6.301   -5.942  1   26.31 ? 276 LEU   B CB  1 
ATOM   5178 C  CG  . LEU   B 1 291 ? -12.693 6.142   -4.532  1   28.53 ? 276 LEU   B CG  1 
ATOM   5179 C  CD1 . LEU   B 1 291 ? -12.807 7.455   -3.747  1   29.56 ? 276 LEU   B CD1 1 
ATOM   5180 C  CD2 . LEU   B 1 291 ? -13.424 5.076   -3.81   1   29.58 ? 276 LEU   B CD2 1 
ATOM   5181 N  N   . LEU   B 1 292 ? -10.697 5.724   -7.664  1   24.52 ? 277 LEU   B N   1 
ATOM   5182 C  CA  . LEU   B 1 292 ? -9.351  5.168   -7.755  1   24.08 ? 277 LEU   B CA  1 
ATOM   5183 C  C   . LEU   B 1 292 ? -8.462  5.809   -8.828  1   24.73 ? 277 LEU   B C   1 
ATOM   5184 O  O   . LEU   B 1 292 ? -7.353  5.322   -9.068  1   25.87 ? 277 LEU   B O   1 
ATOM   5185 C  CB  . LEU   B 1 292 ? -9.44   3.63    -7.947  1   24.08 ? 277 LEU   B CB  1 
ATOM   5186 C  CG  . LEU   B 1 292 ? -10.211 2.915   -6.825  1   24.51 ? 277 LEU   B CG  1 
ATOM   5187 C  CD1 . LEU   B 1 292 ? -10.593 1.466   -7.222  1   24.28 ? 277 LEU   B CD1 1 
ATOM   5188 C  CD2 . LEU   B 1 292 ? -9.429  2.959   -5.518  1   25.62 ? 277 LEU   B CD2 1 
ATOM   5189 N  N   . GLY   B 1 293 ? -8.931  6.887   -9.469  1   24.02 ? 278 GLY   B N   1 
ATOM   5190 C  CA  . GLY   B 1 293 ? -8.14   7.601   -10.477 1   24.26 ? 278 GLY   B CA  1 
ATOM   5191 C  C   . GLY   B 1 293 ? -7.87   6.82    -11.738 1   25.28 ? 278 GLY   B C   1 
ATOM   5192 O  O   . GLY   B 1 293 ? -6.9    7.096   -12.453 1   24.53 ? 278 GLY   B O   1 
ATOM   5193 N  N   . ILE   B 1 294 ? -8.722  5.807   -12.012 1   25.8  ? 279 ILE   B N   1 
ATOM   5194 C  CA  . ILE   B 1 294 ? -8.657  4.999   -13.208 1   27.76 ? 279 ILE   B CA  1 
ATOM   5195 C  C   . ILE   B 1 294 ? -9.375  5.908   -14.176 1   31.75 ? 279 ILE   B C   1 
ATOM   5196 O  O   . ILE   B 1 294 ? -10.597 6.06    -14.092 1   33.55 ? 279 ILE   B O   1 
ATOM   5197 C  CB  . ILE   B 1 294 ? -9.443  3.679   -12.961 1   27.19 ? 279 ILE   B CB  1 
ATOM   5198 C  CG1 . ILE   B 1 294 ? -8.742  2.846   -11.85  1   27.53 ? 279 ILE   B CG1 1 
ATOM   5199 C  CG2 . ILE   B 1 294 ? -9.537  2.877   -14.257 1   27.59 ? 279 ILE   B CG2 1 
ATOM   5200 C  CD1 . ILE   B 1 294 ? -9.546  1.7     -11.347 1   28.82 ? 279 ILE   B CD1 1 
ATOM   5201 N  N   . GLN   B 1 295 ? -8.621  6.611   -14.994 1   31.84 ? 280 GLN   B N   1 
ATOM   5202 C  CA  . GLN   B 1 295 ? -9.184  7.631   -15.864 1   31.59 ? 280 GLN   B CA  1 
ATOM   5203 C  C   . GLN   B 1 295 ? -9.867  7.012   -17.081 1   30.36 ? 280 GLN   B C   1 
ATOM   5204 O  O   . GLN   B 1 295 ? -9.335  7.063   -18.2   1   30.38 ? 280 GLN   B O   1 
ATOM   5205 C  CB  . GLN   B 1 295 ? -8.067  8.603   -16.26  1   33.87 ? 280 GLN   B CB  1 
ATOM   5206 C  CG  . GLN   B 1 295 ? -7.418  9.278   -15.05  1   39.44 ? 280 GLN   B CG  1 
ATOM   5207 C  CD  . GLN   B 1 295 ? -6.322  10.242  -15.447 1   46.67 ? 280 GLN   B CD  1 
ATOM   5208 O  OE1 . GLN   B 1 295 ? -6.231  11.361  -14.93  1   50.23 ? 280 GLN   B OE1 1 
ATOM   5209 N  NE2 . GLN   B 1 295 ? -5.462  9.843   -16.383 1   47.17 ? 280 GLN   B NE2 1 
ATOM   5210 N  N   . GLN   B 1 296 ? -11.015 6.385   -16.854 1   29.27 ? 281 GLN   B N   1 
ATOM   5211 C  CA  . GLN   B 1 296 ? -11.743 5.711   -17.942 1   28.51 ? 281 GLN   B CA  1 
ATOM   5212 C  C   . GLN   B 1 296 ? -12.236 6.661   -18.995 1   28.35 ? 281 GLN   B C   1 
ATOM   5213 O  O   . GLN   B 1 296 ? -12.381 6.25    -20.14  1   28.87 ? 281 GLN   B O   1 
ATOM   5214 C  CB  . GLN   B 1 296 ? -12.939 4.896   -17.421 1   28.36 ? 281 GLN   B CB  1 
ATOM   5215 C  CG  . GLN   B 1 296 ? -12.581 3.704   -16.555 1   29.18 ? 281 GLN   B CG  1 
ATOM   5216 C  CD  . GLN   B 1 296 ? -11.971 2.533   -17.285 1   28.64 ? 281 GLN   B CD  1 
ATOM   5217 O  OE1 . GLN   B 1 296 ? -11.74  2.555   -18.493 1   28.11 ? 281 GLN   B OE1 1 
ATOM   5218 N  NE2 . GLN   B 1 296 ? -11.661 1.495   -16.543 1   29.4  ? 281 GLN   B NE2 1 
ATOM   5219 N  N   . THR   B 1 297 ? -12.513 7.92    -18.623 1   27.68 ? 282 THR   B N   1 
ATOM   5220 C  CA  . THR   B 1 297 ? -13.027 8.913   -19.56  1   28.73 ? 282 THR   B CA  1 
ATOM   5221 C  C   . THR   B 1 297 ? -11.934 9.795   -20.191 1   29.84 ? 282 THR   B C   1 
ATOM   5222 O  O   . THR   B 1 297 ? -12.258 10.684  -20.975 1   29.89 ? 282 THR   B O   1 
ATOM   5223 C  CB  . THR   B 1 297 ? -14.116 9.737   -18.862 1   30.4  ? 282 THR   B CB  1 
ATOM   5224 O  OG1 . THR   B 1 297 ? -13.556 10.321  -17.67  1   31.69 ? 282 THR   B OG1 1 
ATOM   5225 C  CG2 . THR   B 1 297 ? -15.334 8.871   -18.503 1   30.89 ? 282 THR   B CG2 1 
ATOM   5226 N  N   . ALA   B 1 298 ? -10.648 9.528   -19.884 1   29.68 ? 283 ALA   B N   1 
ATOM   5227 C  CA  . ALA   B 1 298 ? -9.556  10.33   -20.427 1   30.84 ? 283 ALA   B CA  1 
ATOM   5228 C  C   . ALA   B 1 298 ? -9.168  9.849   -21.83  1   31.1  ? 283 ALA   B C   1 
ATOM   5229 O  O   . ALA   B 1 298 ? -9.355  8.678   -22.187 1   30.64 ? 283 ALA   B O   1 
ATOM   5230 C  CB  . ALA   B 1 298 ? -8.351  10.278  -19.495 1   31.25 ? 283 ALA   B CB  1 
ATOM   5231 N  N   . GLY   B 1 299 ? -8.616  10.758  -22.608 1   31.38 ? 284 GLY   B N   1 
ATOM   5232 C  CA  . GLY   B 1 299 ? -8.22   10.459  -23.972 1   32.21 ? 284 GLY   B CA  1 
ATOM   5233 C  C   . GLY   B 1 299 ? -9.397  10.635  -24.919 1   33.14 ? 284 GLY   B C   1 
ATOM   5234 O  O   . GLY   B 1 299 ? -10.536 10.934  -24.504 1   34.52 ? 284 GLY   B O   1 
ATOM   5235 N  N   . GLY   B 1 300 ? -9.129  10.414  -26.183 1   32.47 ? 285 GLY   B N   1 
ATOM   5236 C  CA  . GLY   B 1 300 ? -10.156 10.562  -27.201 1   32.47 ? 285 GLY   B CA  1 
ATOM   5237 C  C   . GLY   B 1 300 ? -10.632 9.253   -27.795 1   31.66 ? 285 GLY   B C   1 
ATOM   5238 O  O   . GLY   B 1 300 ? -11.249 9.256   -28.859 1   32.17 ? 285 GLY   B O   1 
ATOM   5239 N  N   . GLY   B 1 301 ? -10.353 8.142   -27.118 1   30.1  ? 286 GLY   B N   1 
ATOM   5240 C  CA  . GLY   B 1 301 ? -10.781 6.835   -27.608 1   28.57 ? 286 GLY   B CA  1 
ATOM   5241 C  C   . GLY   B 1 301 ? -12.277 6.602   -27.515 1   27.07 ? 286 GLY   B C   1 
ATOM   5242 O  O   . GLY   B 1 301 ? -13.005 7.341   -26.825 1   26.28 ? 286 GLY   B O   1 
ATOM   5243 N  N   . HIS   B 1 302 ? -12.754 5.563   -28.225 1   26.06 ? 287 HIS   B N   1 
ATOM   5244 C  CA  . HIS   B 1 302 ? -14.171 5.209   -28.237 1   27.21 ? 287 HIS   B CA  1 
ATOM   5245 C  C   . HIS   B 1 302 ? -14.728 4.814   -26.852 1   24.32 ? 287 HIS   B C   1 
ATOM   5246 O  O   . HIS   B 1 302 ? -15.843 5.215   -26.507 1   23.56 ? 287 HIS   B O   1 
ATOM   5247 C  CB  . HIS   B 1 302 ? -14.426 4.085   -29.24  1   31.86 ? 287 HIS   B CB  1 
ATOM   5248 C  CG  . HIS   B 1 302 ? -14.356 4.525   -30.663 1   40.71 ? 287 HIS   B CG  1 
ATOM   5249 N  ND1 . HIS   B 1 302 ? -13.327 4.114   -31.499 1   44.45 ? 287 HIS   B ND1 1 
ATOM   5250 C  CD2 . HIS   B 1 302 ? -15.199 5.32    -31.365 1   43.61 ? 287 HIS   B CD2 1 
ATOM   5251 C  CE1 . HIS   B 1 302 ? -13.575 4.669   -32.677 1   45.5  ? 287 HIS   B CE1 1 
ATOM   5252 N  NE2 . HIS   B 1 302 ? -14.69  5.405   -32.648 1   45.56 ? 287 HIS   B NE2 1 
ATOM   5253 N  N   . ALA   B 1 303 ? -13.968 4.034   -26.06  1   22.39 ? 288 ALA   B N   1 
ATOM   5254 C  CA  . ALA   B 1 303 ? -14.466 3.61    -24.733 1   21.83 ? 288 ALA   B CA  1 
ATOM   5255 C  C   . ALA   B 1 303 ? -14.651 4.806   -23.782 1   21.19 ? 288 ALA   B C   1 
ATOM   5256 O  O   . ALA   B 1 303 ? -15.677 4.927   -23.116 1   19.84 ? 288 ALA   B O   1 
ATOM   5257 C  CB  . ALA   B 1 303 ? -13.52  2.577   -24.129 1   21.91 ? 288 ALA   B CB  1 
ATOM   5258 N  N   . ALA   B 1 304 ? -13.681 5.735   -23.773 1   20.76 ? 289 ALA   B N   1 
ATOM   5259 C  CA  . ALA   B 1 304 ? -13.783 6.944   -22.961 1   21.17 ? 289 ALA   B CA  1 
ATOM   5260 C  C   . ALA   B 1 304 ? -14.974 7.801   -23.423 1   20.59 ? 289 ALA   B C   1 
ATOM   5261 O  O   . ALA   B 1 304 ? -15.73  8.309   -22.586 1   20.84 ? 289 ALA   B O   1 
ATOM   5262 C  CB  . ALA   B 1 304 ? -12.475 7.767   -23.088 1   21.54 ? 289 ALA   B CB  1 
ATOM   5263 N  N   . GLN   B 1 305 ? -15.147 7.96    -24.741 1   19.75 ? 290 GLN   B N   1 
ATOM   5264 C  CA  . GLN   B 1 305 ? -16.263 8.76    -25.29  1   19.55 ? 290 GLN   B CA  1 
ATOM   5265 C  C   . GLN   B 1 305 ? -17.621 8.147   -24.878 1   19.43 ? 290 GLN   B C   1 
ATOM   5266 O  O   . GLN   B 1 305 ? -18.53  8.867   -24.479 1   18.48 ? 290 GLN   B O   1 
ATOM   5267 C  CB  . GLN   B 1 305 ? -16.172 8.815   -26.828 1   20.96 ? 290 GLN   B CB  1 
ATOM   5268 C  CG  . GLN   B 1 305 ? -17.28  9.655   -27.482 1   23.97 ? 290 GLN   B CG  1 
ATOM   5269 C  CD  . GLN   B 1 305 ? -16.977 11.119  -27.238 1   26.86 ? 290 GLN   B CD  1 
ATOM   5270 O  OE1 . GLN   B 1 305 ? -15.908 11.606  -27.63  1   27.01 ? 290 GLN   B OE1 1 
ATOM   5271 N  NE2 . GLN   B 1 305 ? -17.887 11.833  -26.57  1   25.89 ? 290 GLN   B NE2 1 
ATOM   5272 N  N   . PHE   B 1 306 ? -17.738 6.835   -24.992 1   18.88 ? 291 PHE   B N   1 
ATOM   5273 C  CA  . PHE   B 1 306 ? -18.978 6.126   -24.649 1   18.96 ? 291 PHE   B CA  1 
ATOM   5274 C  C   . PHE   B 1 306 ? -19.345 6.288   -23.166 1   18.92 ? 291 PHE   B C   1 
ATOM   5275 O  O   . PHE   B 1 306 ? -20.468 6.669   -22.864 1   19.21 ? 291 PHE   B O   1 
ATOM   5276 C  CB  . PHE   B 1 306 ? -18.866 4.635   -25.056 1   19.16 ? 291 PHE   B CB  1 
ATOM   5277 C  CG  . PHE   B 1 306 ? -20.115 3.853   -24.704 1   19.82 ? 291 PHE   B CG  1 
ATOM   5278 C  CD1 . PHE   B 1 306 ? -21.286 4.006   -25.449 1   20.8  ? 291 PHE   B CD1 1 
ATOM   5279 C  CD2 . PHE   B 1 306 ? -20.142 3.023   -23.591 1   20.6  ? 291 PHE   B CD2 1 
ATOM   5280 C  CE1 . PHE   B 1 306 ? -22.459 3.355   -25.065 1   21.89 ? 291 PHE   B CE1 1 
ATOM   5281 C  CE2 . PHE   B 1 306 ? -21.311 2.345   -23.23  1   21.72 ? 291 PHE   B CE2 1 
ATOM   5282 C  CZ  . PHE   B 1 306 ? -22.459 2.518   -23.973 1   21.7  ? 291 PHE   B CZ  1 
ATOM   5283 N  N   . LEU   B 1 307 ? -18.386 6.048   -22.237 1   18.69 ? 292 LEU   B N   1 
ATOM   5284 C  CA  . LEU   B 1 307 ? -18.659 6.196   -20.805 1   18.96 ? 292 LEU   B CA  1 
ATOM   5285 C  C   . LEU   B 1 307 ? -18.996 7.627   -20.411 1   19.87 ? 292 LEU   B C   1 
ATOM   5286 O  O   . LEU   B 1 307 ? -19.866 7.852   -19.553 1   19.89 ? 292 LEU   B O   1 
ATOM   5287 C  CB  . LEU   B 1 307 ? -17.499 5.644   -19.963 1   19.07 ? 292 LEU   B CB  1 
ATOM   5288 C  CG  . LEU   B 1 307 ? -17.408 4.105   -20.008 1   21.1  ? 292 LEU   B CG  1 
ATOM   5289 C  CD1 . LEU   B 1 307 ? -16.055 3.615   -19.503 1   21.97 ? 292 LEU   B CD1 1 
ATOM   5290 C  CD2 . LEU   B 1 307 ? -18.547 3.483   -19.237 1   21.71 ? 292 LEU   B CD2 1 
ATOM   5291 N  N   . GLN   B 1 308 ? -18.321 8.613   -21.036 1   20.63 ? 293 GLN   B N   1 
ATOM   5292 C  CA  . GLN   B 1 308 ? -18.67  10.014  -20.746 1   21.7  ? 293 GLN   B CA  1 
ATOM   5293 C  C   . GLN   B 1 308 ? -20.088 10.3    -21.279 1   22.27 ? 293 GLN   B C   1 
ATOM   5294 O  O   . GLN   B 1 308 ? -20.911 10.861  -20.567 1   23.59 ? 293 GLN   B O   1 
ATOM   5295 C  CB  . GLN   B 1 308 ? -17.657 10.984  -21.384 1   23.39 ? 293 GLN   B CB  1 
ATOM   5296 C  CG  . GLN   B 1 308 ? -17.957 12.461  -21.023 1   27.95 ? 293 GLN   B CG  1 
ATOM   5297 C  CD  . GLN   B 1 308 ? -17.823 12.768  -19.533 1   33.52 ? 293 GLN   B CD  1 
ATOM   5298 O  OE1 . GLN   B 1 308 ? -18.624 13.528  -18.935 1   38.51 ? 293 GLN   B OE1 1 
ATOM   5299 N  NE2 . GLN   B 1 308 ? -16.827 12.185  -18.892 1   33.11 ? 293 GLN   B NE2 1 
ATOM   5300 N  N   . ASP   B 1 309 ? -20.387 9.859   -22.511 1   21.69 ? 294 ASP   B N   1 
ATOM   5301 C  CA  . ASP   B 1 309 ? -21.736 10.053  -23.084 1   21.2  ? 294 ASP   B CA  1 
ATOM   5302 C  C   . ASP   B 1 309 ? -22.835 9.404   -22.208 1   21.48 ? 294 ASP   B C   1 
ATOM   5303 O  O   . ASP   B 1 309 ? -23.902 9.995   -22.042 1   22.16 ? 294 ASP   B O   1 
ATOM   5304 C  CB  . ASP   B 1 309 ? -21.832 9.491   -24.504 1   21.74 ? 294 ASP   B CB  1 
ATOM   5305 C  CG  . ASP   B 1 309 ? -21.051 10.252  -25.566 1   27.31 ? 294 ASP   B CG  1 
ATOM   5306 O  OD1 . ASP   B 1 309 ? -20.513 11.346  -25.246 1   27.31 ? 294 ASP   B OD1 1 
ATOM   5307 O  OD2 . ASP   B 1 309 ? -20.941 9.735   -26.717 1   30.29 ? 294 ASP   B OD2 1 
ATOM   5308 N  N   . MET   B 1 310 ? -22.559 8.222   -21.616 1   20.68 ? 295 MET   B N   1 
ATOM   5309 C  CA  . MET   B 1 310 ? -23.563 7.541   -20.778 1   20.71 ? 295 MET   B CA  1 
ATOM   5310 C  C   . MET   B 1 310 ? -23.897 8.284   -19.505 1   21.77 ? 295 MET   B C   1 
ATOM   5311 O  O   . MET   B 1 310 ? -24.934 7.989   -18.907 1   22.69 ? 295 MET   B O   1 
ATOM   5312 C  CB  . MET   B 1 310 ? -23.183 6.089   -20.467 1   20.69 ? 295 MET   B CB  1 
ATOM   5313 C  CG  . MET   B 1 310 ? -23.198 5.2     -21.676 1   22.86 ? 295 MET   B CG  1 
ATOM   5314 S  SD  . MET   B 1 310 ? -24.756 5.112   -22.64  1   25.58 ? 295 MET   B SD  1 
ATOM   5315 C  CE  . MET   B 1 310 ? -24.395 6.229   -24.028 1   22.57 ? 295 MET   B CE  1 
ATOM   5316 N  N   . ARG   B 1 311 ? -23.061 9.258   -19.077 1   22.06 ? 296 ARG   B N   1 
ATOM   5317 C  CA  . ARG   B 1 311 ? -23.383 10.039  -17.882 1   23.38 ? 296 ARG   B CA  1 
ATOM   5318 C  C   . ARG   B 1 311 ? -24.66  10.859  -18.026 1   24.54 ? 296 ARG   B C   1 
ATOM   5319 O  O   . ARG   B 1 311 ? -25.408 11.004  -17.065 1   23.81 ? 296 ARG   B O   1 
ATOM   5320 C  CB  . ARG   B 1 311 ? -22.214 10.914  -17.448 1   24.57 ? 296 ARG   B CB  1 
ATOM   5321 C  CG  . ARG   B 1 311 ? -21.044 10.046  -17.013 1   26.56 ? 296 ARG   B CG  1 
ATOM   5322 C  CD  . ARG   B 1 311 ? -19.976 10.89   -16.367 1   28.12 ? 296 ARG   B CD  1 
ATOM   5323 N  NE  . ARG   B 1 311 ? -18.874 10.064  -15.89  1   28.16 ? 296 ARG   B NE  1 
ATOM   5324 C  CZ  . ARG   B 1 311 ? -17.808 10.534  -15.253 1   32.6  ? 296 ARG   B CZ  1 
ATOM   5325 N  NH1 . ARG   B 1 311 ? -17.678 11.841  -15.031 1   31.48 ? 296 ARG   B NH1 1 
ATOM   5326 N  NH2 . ARG   B 1 311 ? -16.84  9.707   -14.87  1   32.32 ? 296 ARG   B NH2 1 
ATOM   5327 N  N   . ARG   B 1 312 ? -24.946 11.335  -19.239 1   25.78 ? 297 ARG   B N   1 
ATOM   5328 C  CA  . ARG   B 1 312 ? -26.185 12.085  -19.497 1   27.09 ? 297 ARG   B CA  1 
ATOM   5329 C  C   . ARG   B 1 312 ? -27.453 11.186  -19.513 1   25.43 ? 297 ARG   B C   1 
ATOM   5330 O  O   . ARG   B 1 312 ? -28.568 11.686  -19.633 1   25.11 ? 297 ARG   B O   1 
ATOM   5331 C  CB  . ARG   B 1 312 ? -26.053 12.857  -20.814 1   31.39 ? 297 ARG   B CB  1 
ATOM   5332 C  CG  . ARG   B 1 312 ? -25.002 13.979  -20.751 1   39.75 ? 297 ARG   B CG  1 
ATOM   5333 C  CD  . ARG   B 1 312 ? -25.562 15.248  -20.12  1   46.48 ? 297 ARG   B CD  1 
ATOM   5334 N  NE  . ARG   B 1 312 ? -24.619 16.369  -20.186 1   51.9  ? 297 ARG   B NE  1 
ATOM   5335 C  CZ  . ARG   B 1 312 ? -24.715 17.471  -19.441 1   55.2  ? 297 ARG   B CZ  1 
ATOM   5336 N  NH1 . ARG   B 1 312 ? -25.697 17.597  -18.547 1   55.84 ? 297 ARG   B NH1 1 
ATOM   5337 N  NH2 . ARG   B 1 312 ? -23.816 18.445  -19.566 1   53.78 ? 297 ARG   B NH2 1 
ATOM   5338 N  N   . TYR   B 1 313 ? -27.281 9.865   -19.417 1   23.62 ? 298 TYR   B N   1 
ATOM   5339 C  CA  . TYR   B 1 313 ? -28.358 8.887   -19.348 1   23.11 ? 298 TYR   B CA  1 
ATOM   5340 C  C   . TYR   B 1 313 ? -28.587 8.401   -17.895 1   23.21 ? 298 TYR   B C   1 
ATOM   5341 O  O   . TYR   B 1 313 ? -29.384 7.477   -17.665 1   23.48 ? 298 TYR   B O   1 
ATOM   5342 C  CB  . TYR   B 1 313 ? -28.023 7.687   -20.259 1   22.39 ? 298 TYR   B CB  1 
ATOM   5343 C  CG  . TYR   B 1 313 ? -28.073 7.995   -21.743 1   22.44 ? 298 TYR   B CG  1 
ATOM   5344 C  CD1 . TYR   B 1 313 ? -27.063 8.72    -22.358 1   23.08 ? 298 TYR   B CD1 1 
ATOM   5345 C  CD2 . TYR   B 1 313 ? -29.103 7.517   -22.538 1   22.65 ? 298 TYR   B CD2 1 
ATOM   5346 C  CE1 . TYR   B 1 313 ? -27.107 9.008   -23.711 1   23.48 ? 298 TYR   B CE1 1 
ATOM   5347 C  CE2 . TYR   B 1 313 ? -29.13  7.753   -23.906 1   22.99 ? 298 TYR   B CE2 1 
ATOM   5348 C  CZ  . TYR   B 1 313 ? -28.135 8.51    -24.488 1   24.74 ? 298 TYR   B CZ  1 
ATOM   5349 O  OH  . TYR   B 1 313 ? -28.17  8.77    -25.834 1   26.61 ? 298 TYR   B OH  1 
ATOM   5350 N  N   . MET   B 1 314 ? -27.855 8.998   -16.918 1   22.35 ? 299 MET   B N   1 
ATOM   5351 C  CA  . MET   B 1 314 ? -27.978 8.717   -15.502 1   22.21 ? 299 MET   B CA  1 
ATOM   5352 C  C   . MET   B 1 314 ? -28.891 9.752   -14.875 1   22.35 ? 299 MET   B C   1 
ATOM   5353 O  O   . MET   B 1 314 ? -28.89  10.898  -15.314 1   23.4  ? 299 MET   B O   1 
ATOM   5354 C  CB  . MET   B 1 314 ? -26.591 8.85    -14.811 1   22.26 ? 299 MET   B CB  1 
ATOM   5355 C  CG  . MET   B 1 314 ? -25.53  7.938   -15.372 1   22.42 ? 299 MET   B CG  1 
ATOM   5356 S  SD  . MET   B 1 314 ? -24.003 8.177   -14.371 1   23.06 ? 299 MET   B SD  1 
ATOM   5357 C  CE  . MET   B 1 314 ? -22.96  6.923   -15.159 1   16.93 ? 299 MET   B CE  1 
ATOM   5358 N  N   . PRO   B 1 315 ? -29.583 9.424   -13.78  1   22.08 ? 300 PRO   B N   1 
ATOM   5359 C  CA  . PRO   B 1 315 ? -30.372 10.446  -13.068 1   23.38 ? 300 PRO   B CA  1 
ATOM   5360 C  C   . PRO   B 1 315 ? -29.479 11.647  -12.671 1   25.55 ? 300 PRO   B C   1 
ATOM   5361 O  O   . PRO   B 1 315 ? -28.277 11.481  -12.389 1   24.99 ? 300 PRO   B O   1 
ATOM   5362 C  CB  . PRO   B 1 315 ? -30.885 9.696   -11.824 1   24.16 ? 300 PRO   B CB  1 
ATOM   5363 C  CG  . PRO   B 1 315 ? -30.887 8.256   -12.212 1   24.04 ? 300 PRO   B CG  1 
ATOM   5364 C  CD  . PRO   B 1 315 ? -29.679 8.101   -13.133 1   22.09 ? 300 PRO   B CD  1 
ATOM   5365 N  N   . PRO   B 1 316 ? -30.028 12.869  -12.769 1   26.61 ? 301 PRO   B N   1 
ATOM   5366 C  CA  . PRO   B 1 316 ? -29.219 14.066  -12.531 1   26.6  ? 301 PRO   B CA  1 
ATOM   5367 C  C   . PRO   B 1 316 ? -28.479 14.098  -11.199 1   26.07 ? 301 PRO   B C   1 
ATOM   5368 O  O   . PRO   B 1 316 ? -27.336 14.522  -11.205 1   25.91 ? 301 PRO   B O   1 
ATOM   5369 C  CB  . PRO   B 1 316 ? -30.23  15.226  -12.671 1   27.84 ? 301 PRO   B CB  1 
ATOM   5370 C  CG  . PRO   B 1 316 ? -31.578 14.58   -12.487 1   28.91 ? 301 PRO   B CG  1 
ATOM   5371 C  CD  . PRO   B 1 316 ? -31.406 13.229  -13.154 1   26.89 ? 301 PRO   B CD  1 
ATOM   5372 N  N   . ALA   B 1 317 ? -29.09  13.652  -10.084 1   25.3  ? 302 ALA   B N   1 
ATOM   5373 C  CA  . ALA   B 1 317 ? -28.399 13.639  -8.789  1   26.37 ? 302 ALA   B CA  1 
ATOM   5374 C  C   . ALA   B 1 317 ? -27.158 12.718  -8.799  1   26.2  ? 302 ALA   B C   1 
ATOM   5375 O  O   . ALA   B 1 317 ? -26.156 13.003  -8.125  1   26.51 ? 302 ALA   B O   1 
ATOM   5376 C  CB  . ALA   B 1 317 ? -29.352 13.179  -7.697  1   26.69 ? 302 ALA   B CB  1 
ATOM   5377 N  N   . HIS   B 1 318 ? -27.236 11.614  -9.55   1   25.22 ? 303 HIS   B N   1 
ATOM   5378 C  CA  . HIS   B 1 318 ? -26.148 10.633  -9.676  1   24.85 ? 303 HIS   B CA  1 
ATOM   5379 C  C   . HIS   B 1 318 ? -25.034 11.14   -10.575 1   24.76 ? 303 HIS   B C   1 
ATOM   5380 O  O   . HIS   B 1 318 ? -23.863 10.973  -10.268 1   24.66 ? 303 HIS   B O   1 
ATOM   5381 C  CB  . HIS   B 1 318 ? -26.721 9.278   -10.138 1   25.27 ? 303 HIS   B CB  1 
ATOM   5382 C  CG  . HIS   B 1 318 ? -27.701 8.68    -9.161  1   26.88 ? 303 HIS   B CG  1 
ATOM   5383 N  ND1 . HIS   B 1 318 ? -28.427 7.537   -9.475  1   28.44 ? 303 HIS   B ND1 1 
ATOM   5384 C  CD2 . HIS   B 1 318 ? -28.023 9.059   -7.899  1   27.9  ? 303 HIS   B CD2 1 
ATOM   5385 C  CE1 . HIS   B 1 318 ? -29.157 7.267   -8.405  1   28.69 ? 303 HIS   B CE1 1 
ATOM   5386 N  NE2 . HIS   B 1 318 ? -28.962 8.162   -7.437  1   28.84 ? 303 HIS   B NE2 1 
ATOM   5387 N  N   . ARG   B 1 319 ? -25.393 11.829  -11.632 1   24.36 ? 304 ARG   B N   1 
ATOM   5388 C  CA  . ARG   B 1 319 ? -24.463 12.519  -12.522 1   25.69 ? 304 ARG   B CA  1 
ATOM   5389 C  C   . ARG   B 1 319 ? -23.724 13.617  -11.673 1   25.68 ? 304 ARG   B C   1 
ATOM   5390 O  O   . ARG   B 1 319 ? -22.515 13.79   -11.807 1   26.04 ? 304 ARG   B O   1 
ATOM   5391 C  CB  . ARG   B 1 319 ? -25.316 13.188  -13.61  1   28.78 ? 304 ARG   B CB  1 
ATOM   5392 C  CG  . ARG   B 1 319 ? -24.626 13.534  -14.925 1   35.09 ? 304 ARG   B CG  1 
ATOM   5393 C  CD  . ARG   B 1 319 ? -25.618 14.226  -15.902 1   39.7  ? 304 ARG   B CD  1 
ATOM   5394 N  NE  . ARG   B 1 319 ? -26.938 13.584  -15.923 1   43.31 ? 304 ARG   B NE  1 
ATOM   5395 C  CZ  . ARG   B 1 319 ? -28.054 14.164  -16.368 1   45.1  ? 304 ARG   B CZ  1 
ATOM   5396 N  NH1 . ARG   B 1 319 ? -28.018 15.398  -16.859 1   45.59 ? 304 ARG   B NH1 1 
ATOM   5397 N  NH2 . ARG   B 1 319 ? -29.216 13.513  -16.32  1   41.94 ? 304 ARG   B NH2 1 
ATOM   5398 N  N   . ASN   B 1 320 ? -24.452 14.316  -10.758 1   24.36 ? 305 ASN   B N   1 
ATOM   5399 C  CA  . ASN   B 1 320 ? -23.887 15.356  -9.889  1   24.04 ? 305 ASN   B CA  1 
ATOM   5400 C  C   . ASN   B 1 320 ? -22.892 14.734  -8.881  1   22.8  ? 305 ASN   B C   1 
ATOM   5401 O  O   . ASN   B 1 320 ? -21.884 15.348  -8.531  1   21.43 ? 305 ASN   B O   1 
ATOM   5402 C  CB  . ASN   B 1 320 ? -25.013 16.049  -9.079  1   24.87 ? 305 ASN   B CB  1 
ATOM   5403 C  CG  . ASN   B 1 320 ? -25.916 16.929  -9.877  1   27.18 ? 305 ASN   B CG  1 
ATOM   5404 O  OD1 . ASN   B 1 320 ? -25.643 17.217  -11.051 1   28.78 ? 305 ASN   B OD1 1 
ATOM   5405 N  ND2 . ASN   B 1 320 ? -26.993 17.385  -9.239  1   26.89 ? 305 ASN   B ND2 1 
ATOM   5406 N  N   . PHE   B 1 321 ? -23.222 13.551  -8.366  1   22.5  ? 306 PHE   B N   1 
ATOM   5407 C  CA  . PHE   B 1 321 ? -22.369 12.819  -7.445  1   23.76 ? 306 PHE   B CA  1 
ATOM   5408 C  C   . PHE   B 1 321 ? -21.039 12.481  -8.138  1   24.15 ? 306 PHE   B C   1 
ATOM   5409 O  O   . PHE   B 1 321 ? -19.985 12.715  -7.546  1   23.6  ? 306 PHE   B O   1 
ATOM   5410 C  CB  . PHE   B 1 321 ? -23.041 11.544  -6.934  1   24.07 ? 306 PHE   B CB  1 
ATOM   5411 C  CG  . PHE   B 1 321 ? -22.153 10.807  -5.966  1   25.33 ? 306 PHE   B CG  1 
ATOM   5412 C  CD1 . PHE   B 1 321 ? -21.928 11.303  -4.69   1   26.64 ? 306 PHE   B CD1 1 
ATOM   5413 C  CD2 . PHE   B 1 321 ? -21.471 9.664   -6.357  1   26.79 ? 306 PHE   B CD2 1 
ATOM   5414 C  CE1 . PHE   B 1 321 ? -21.096 10.629  -3.802  1   27.44 ? 306 PHE   B CE1 1 
ATOM   5415 C  CE2 . PHE   B 1 321 ? -20.655 8.979   -5.465  1   27.45 ? 306 PHE   B CE2 1 
ATOM   5416 C  CZ  . PHE   B 1 321 ? -20.475 9.464   -4.192  1   27.37 ? 306 PHE   B CZ  1 
ATOM   5417 N  N   . LEU   B 1 322 ? -21.085 12.021  -9.405  1   23.76 ? 307 LEU   B N   1 
ATOM   5418 C  CA  . LEU   B 1 322 ? -19.86  11.74   -10.157 1   24.68 ? 307 LEU   B CA  1 
ATOM   5419 C  C   . LEU   B 1 322 ? -18.988 13      -10.319 1   25.32 ? 307 LEU   B C   1 
ATOM   5420 O  O   . LEU   B 1 322 ? -17.791 12.931  -10.053 1   24.63 ? 307 LEU   B O   1 
ATOM   5421 C  CB  . LEU   B 1 322 ? -20.145 11.105  -11.509 1   25.29 ? 307 LEU   B CB  1 
ATOM   5422 C  CG  . LEU   B 1 322 ? -20.639 9.639   -11.443 1   27.87 ? 307 LEU   B CG  1 
ATOM   5423 C  CD1 . LEU   B 1 322 ? -20.92  9.089   -12.834 1   28.56 ? 307 LEU   B CD1 1 
ATOM   5424 C  CD2 . LEU   B 1 322 ? -19.59  8.743   -10.855 1   28.88 ? 307 LEU   B CD2 1 
ATOM   5425 N  N   . CYS   B 1 323 ? -19.59  14.15   -10.702 1   25.14 ? 308 CYS   B N   1 
ATOM   5426 C  CA  . CYS   B 1 323 ? -18.891 15.457  -10.817 1   26.27 ? 308 CYS   B CA  1 
ATOM   5427 C  C   . CYS   B 1 323 ? -18.181 15.795  -9.509  1   27.64 ? 308 CYS   B C   1 
ATOM   5428 O  O   . CYS   B 1 323 ? -17.061 16.261  -9.503  1   28.29 ? 308 CYS   B O   1 
ATOM   5429 C  CB  . CYS   B 1 323 ? -19.897 16.563  -11.173 1   25.9  ? 308 CYS   B CB  1 
ATOM   5430 S  SG  . CYS   B 1 323 ? -19.35  18.251  -10.722 1   29.18 ? 308 CYS   B SG  1 
ATOM   5431 N  N   . SER   B 1 324 ? -18.888 15.626  -8.415  1   28.57 ? 309 SER   B N   1 
ATOM   5432 C  CA  . SER   B 1 324 ? -18.456 15.942  -7.079  1   29.99 ? 309 SER   B CA  1 
ATOM   5433 C  C   . SER   B 1 324 ? -17.255 15.072  -6.676  1   30.44 ? 309 SER   B C   1 
ATOM   5434 O  O   . SER   B 1 324 ? -16.271 15.596  -6.138  1   30.04 ? 309 SER   B O   1 
ATOM   5435 C  CB  . SER   B 1 324 ? -19.64  15.782  -6.14   1   33.71 ? 309 SER   B CB  1 
ATOM   5436 O  OG  . SER   B 1 324 ? -19.294 15.783  -4.771  1   40.22 ? 309 SER   B OG  1 
ATOM   5437 N  N   . LEU   B 1 325 ? -17.304 13.766  -6.992  1   29.71 ? 310 LEU   B N   1 
ATOM   5438 C  CA  . LEU   B 1 325 ? -16.185 12.858  -6.738  1   30.72 ? 310 LEU   B CA  1 
ATOM   5439 C  C   . LEU   B 1 325 ? -14.956 13.302  -7.541  1   31.32 ? 310 LEU   B C   1 
ATOM   5440 O  O   . LEU   B 1 325 ? -13.829 13.228  -7.049  1   31.8  ? 310 LEU   B O   1 
ATOM   5441 C  CB  . LEU   B 1 325 ? -16.538 11.442  -7.221  1   31.21 ? 310 LEU   B CB  1 
ATOM   5442 C  CG  . LEU   B 1 325 ? -17.211 10.473  -6.3    1   33.41 ? 310 LEU   B CG  1 
ATOM   5443 C  CD1 . LEU   B 1 325 ? -17.14  9.074   -6.916  1   33.44 ? 310 LEU   B CD1 1 
ATOM   5444 C  CD2 . LEU   B 1 325 ? -16.532 10.457  -4.91   1   34.15 ? 310 LEU   B CD2 1 
ATOM   5445 N  N   . GLU   B 1 326 ? -15.169 13.692  -8.802  1   31.48 ? 311 GLU   B N   1 
ATOM   5446 C  CA  . GLU   B 1 326 ? -14.103 14.138  -9.696  1   32.89 ? 311 GLU   B CA  1 
ATOM   5447 C  C   . GLU   B 1 326 ? -13.447 15.434  -9.238  1   33.35 ? 311 GLU   B C   1 
ATOM   5448 O  O   . GLU   B 1 326 ? -12.301 15.68   -9.606  1   34.66 ? 311 GLU   B O   1 
ATOM   5449 C  CB  . GLU   B 1 326 ? -14.637 14.338  -11.103 1   35.83 ? 311 GLU   B CB  1 
ATOM   5450 C  CG  . GLU   B 1 326 ? -14.703 13.074  -11.908 1   40.9  ? 311 GLU   B CG  1 
ATOM   5451 C  CD  . GLU   B 1 326 ? -15.338 13.255  -13.271 1   47.23 ? 311 GLU   B CD  1 
ATOM   5452 O  OE1 . GLU   B 1 326 ? -16.133 14.21   -13.444 1   47.81 ? 311 GLU   B OE1 1 
ATOM   5453 O  OE2 . GLU   B 1 326 ? -15.041 12.434  -14.167 1   49.45 ? 311 GLU   B OE2 1 
ATOM   5454 N  N   . SER   B 1 327 ? -14.156 16.252  -8.473  1   32.92 ? 312 SER   B N   1 
ATOM   5455 C  CA  . SER   B 1 327 ? -13.657 17.522  -7.944  1   34.36 ? 312 SER   B CA  1 
ATOM   5456 C  C   . SER   B 1 327 ? -12.772 17.347  -6.705  1   34.05 ? 312 SER   B C   1 
ATOM   5457 O  O   . SER   B 1 327 ? -12.085 18.279  -6.305  1   33.91 ? 312 SER   B O   1 
ATOM   5458 C  CB  . SER   B 1 327 ? -14.826 18.449  -7.635  1   37.36 ? 312 SER   B CB  1 
ATOM   5459 O  OG  . SER   B 1 327 ? -15.545 18.671  -8.844  1   42.63 ? 312 SER   B OG  1 
ATOM   5460 N  N   . ASN   B 1 328 ? -12.81  16.163  -6.085  1   33.19 ? 313 ASN   B N   1 
ATOM   5461 C  CA  . ASN   B 1 328 ? -12.011 15.873  -4.921  1   32.99 ? 313 ASN   B CA  1 
ATOM   5462 C  C   . ASN   B 1 328 ? -10.595 15.507  -5.332  1   32.95 ? 313 ASN   B C   1 
ATOM   5463 O  O   . ASN   B 1 328 ? -10.35  15.089  -6.476  1   32.33 ? 313 ASN   B O   1 
ATOM   5464 C  CB  . ASN   B 1 328 ? -12.678 14.763  -4.107  1   34.2  ? 313 ASN   B CB  1 
ATOM   5465 C  CG  . ASN   B 1 328 ? -13.7   15.32   -3.156  1   37.83 ? 313 ASN   B CG  1 
ATOM   5466 O  OD1 . ASN   B 1 328 ? -13.432 15.545  -1.965  1   38.95 ? 313 ASN   B OD1 1 
ATOM   5467 N  ND2 . ASN   B 1 328 ? -14.875 15.622  -3.676  1   37.58 ? 313 ASN   B ND2 1 
ATOM   5468 N  N   . PRO   B 1 329 ? -9.621  15.659  -4.411  1   33.36 ? 314 PRO   B N   1 
ATOM   5469 C  CA  . PRO   B 1 329 ? -8.249  15.273  -4.747  1   32.75 ? 314 PRO   B CA  1 
ATOM   5470 C  C   . PRO   B 1 329 ? -8.133  13.805  -5.143  1   31.73 ? 314 PRO   B C   1 
ATOM   5471 O  O   . PRO   B 1 329 ? -8.937  12.97   -4.745  1   31.36 ? 314 PRO   B O   1 
ATOM   5472 C  CB  . PRO   B 1 329 ? -7.451  15.589  -3.47   1   34.33 ? 314 PRO   B CB  1 
ATOM   5473 C  CG  . PRO   B 1 329 ? -8.333  16.446  -2.633  1   35.2  ? 314 PRO   B CG  1 
ATOM   5474 C  CD  . PRO   B 1 329 ? -9.743  16.11   -3.01   1   33.62 ? 314 PRO   B CD  1 
ATOM   5475 N  N   . SER   B 1 330 ? -7.141  13.503  -5.96   1   31.16 ? 315 SER   B N   1 
ATOM   5476 C  CA  . SER   B 1 330 ? -6.917  12.156  -6.449  1   30.58 ? 315 SER   B CA  1 
ATOM   5477 C  C   . SER   B 1 330 ? -6.391  11.21   -5.339  1   29.98 ? 315 SER   B C   1 
ATOM   5478 O  O   . SER   B 1 330 ? -5.378  11.493  -4.69   1   28.89 ? 315 SER   B O   1 
ATOM   5479 C  CB  . SER   B 1 330 ? -5.946  12.2    -7.621  1   31.85 ? 315 SER   B CB  1 
ATOM   5480 O  OG  . SER   B 1 330 ? -5.567  10.905  -8.061  1   33.9  ? 315 SER   B OG  1 
ATOM   5481 N  N   . VAL   B 1 331 ? -7.1    10.101  -5.116  1   28.84 ? 316 VAL   B N   1 
ATOM   5482 C  CA  . VAL   B 1 331 ? -6.692  9.064   -4.173  1   28.48 ? 316 VAL   B CA  1 
ATOM   5483 C  C   . VAL   B 1 331 ? -5.425  8.388   -4.719  1   27.88 ? 316 VAL   B C   1 
ATOM   5484 O  O   . VAL   B 1 331 ? -4.475  8.147   -3.965  1   27.75 ? 316 VAL   B O   1 
ATOM   5485 C  CB  . VAL   B 1 331 ? -7.841  8.036   -3.977  1   29.2  ? 316 VAL   B CB  1 
ATOM   5486 C  CG1 . VAL   B 1 331 ? -7.363  6.821   -3.209  1   29.94 ? 316 VAL   B CG1 1 
ATOM   5487 C  CG2 . VAL   B 1 331 ? -9.038  8.686   -3.279  1   29.6  ? 316 VAL   B CG2 1 
ATOM   5488 N  N   . ARG   B 1 332 ? -5.402  8.089   -6.029  1   26.75 ? 317 ARG   B N   1 
ATOM   5489 C  CA  . ARG   B 1 332 ? -4.266  7.465   -6.688  1   27.28 ? 317 ARG   B CA  1 
ATOM   5490 C  C   . ARG   B 1 332 ? -2.994  8.34    -6.518  1   27.57 ? 317 ARG   B C   1 
ATOM   5491 O  O   . ARG   B 1 332 ? -1.948  7.814   -6.149  1   27.37 ? 317 ARG   B O   1 
ATOM   5492 C  CB  . ARG   B 1 332 ? -4.542  7.288   -8.184  1   27.94 ? 317 ARG   B CB  1 
ATOM   5493 C  CG  . ARG   B 1 332 ? -3.378  6.681   -8.918  1   29.83 ? 317 ARG   B CG  1 
ATOM   5494 C  CD  . ARG   B 1 332 ? -3.661  6.376   -10.374 1   32.15 ? 317 ARG   B CD  1 
ATOM   5495 N  NE  . ARG   B 1 332 ? -2.847  5.22    -10.8   1   32.85 ? 317 ARG   B NE  1 
ATOM   5496 C  CZ  . ARG   B 1 332 ? -1.68   5.335   -11.417 1   36.39 ? 317 ARG   B CZ  1 
ATOM   5497 N  NH1 . ARG   B 1 332 ? -1.197  6.534   -11.725 1   39.42 ? 317 ARG   B NH1 1 
ATOM   5498 N  NH2 . ARG   B 1 332 ? -0.978  4.26    -11.724 1   34.82 ? 317 ARG   B NH2 1 
ATOM   5499 N  N   . GLU   B 1 333 ? -3.1    9.643   -6.804  1   27.57 ? 318 GLU   B N   1 
ATOM   5500 C  CA  . GLU   B 1 333 ? -1.958  10.545  -6.677  1   29    ? 318 GLU   B CA  1 
ATOM   5501 C  C   . GLU   B 1 333 ? -1.495  10.661  -5.235  1   29.59 ? 318 GLU   B C   1 
ATOM   5502 O  O   . GLU   B 1 333 ? -0.283  10.692  -4.995  1   30.9  ? 318 GLU   B O   1 
ATOM   5503 C  CB  . GLU   B 1 333 ? -2.278  11.918  -7.279  1   32.48 ? 318 GLU   B CB  1 
ATOM   5504 C  CG  . GLU   B 1 333 ? -2.357  11.882  -8.802  1   38.79 ? 318 GLU   B CG  1 
ATOM   5505 C  CD  . GLU   B 1 333 ? -1.086  11.424  -9.498  1   45.73 ? 318 GLU   B CD  1 
ATOM   5506 O  OE1 . GLU   B 1 333 ? 0.01    11.88   -9.093  1   47.43 ? 318 GLU   B OE1 1 
ATOM   5507 O  OE2 . GLU   B 1 333 ? -1.183  10.605  -10.445 1   45.42 ? 318 GLU   B OE2 1 
ATOM   5508 N  N   . PHE   B 1 334 ? -2.432  10.667  -4.272  1   28.38 ? 319 PHE   B N   1 
ATOM   5509 C  CA  . PHE   B 1 334 ? -2.096  10.726  -2.856  1   29.36 ? 319 PHE   B CA  1 
ATOM   5510 C  C   . PHE   B 1 334 ? -1.263  9.488   -2.458  1   29.37 ? 319 PHE   B C   1 
ATOM   5511 O  O   . PHE   B 1 334 ? -0.222  9.63    -1.814  1   29.17 ? 319 PHE   B O   1 
ATOM   5512 C  CB  . PHE   B 1 334 ? -3.372  10.805  -2.003  1   29.87 ? 319 PHE   B CB  1 
ATOM   5513 C  CG  . PHE   B 1 334 ? -3.142  11.012  -0.521  1   31.51 ? 319 PHE   B CG  1 
ATOM   5514 C  CD1 . PHE   B 1 334 ? -2.907  9.931   0.321   1   32.53 ? 319 PHE   B CD1 1 
ATOM   5515 C  CD2 . PHE   B 1 334 ? -3.215  12.28   0.04    1   32.2  ? 319 PHE   B CD2 1 
ATOM   5516 C  CE1 . PHE   B 1 334 ? -2.692  10.122  1.682   1   33.35 ? 319 PHE   B CE1 1 
ATOM   5517 C  CE2 . PHE   B 1 334 ? -3.033  12.464  1.411   1   33.26 ? 319 PHE   B CE2 1 
ATOM   5518 C  CZ  . PHE   B 1 334 ? -2.774  11.384  2.222   1   33.21 ? 319 PHE   B CZ  1 
ATOM   5519 N  N   . VAL   B 1 335 ? -1.719  8.278   -2.843  1   28.22 ? 320 VAL   B N   1 
ATOM   5520 C  CA  . VAL   B 1 335 ? -1.033  7.036   -2.515  1   28.33 ? 320 VAL   B CA  1 
ATOM   5521 C  C   . VAL   B 1 335 ? 0.326   6.951   -3.213  1   30.08 ? 320 VAL   B C   1 
ATOM   5522 O  O   . VAL   B 1 335 ? 1.316   6.581   -2.585  1   30.77 ? 320 VAL   B O   1 
ATOM   5523 C  CB  . VAL   B 1 335 ? -1.935  5.816   -2.844  1   27.76 ? 320 VAL   B CB  1 
ATOM   5524 C  CG1 . VAL   B 1 335 ? -1.154  4.525   -2.743  1   28.87 ? 320 VAL   B CG1 1 
ATOM   5525 C  CG2 . VAL   B 1 335 ? -3.145  5.786   -1.923  1   27.64 ? 320 VAL   B CG2 1 
ATOM   5526 N  N   . LEU   B 1 336 ? 0.376   7.309   -4.489  1   30.75 ? 321 LEU   B N   1 
ATOM   5527 C  CA  . LEU   B 1 336 ? 1.611   7.284   -5.267  1   33.13 ? 321 LEU   B CA  1 
ATOM   5528 C  C   . LEU   B 1 336 ? 2.707   8.18    -4.672  1   34.5  ? 321 LEU   B C   1 
ATOM   5529 O  O   . LEU   B 1 336 ? 3.89    7.862   -4.8    1   35.96 ? 321 LEU   B O   1 
ATOM   5530 C  CB  . LEU   B 1 336 ? 1.332   7.782   -6.688  1   34.49 ? 321 LEU   B CB  1 
ATOM   5531 C  CG  . LEU   B 1 336 ? 1.244   6.736   -7.772  1   37.81 ? 321 LEU   B CG  1 
ATOM   5532 C  CD1 . LEU   B 1 336 ? 0.946   7.384   -9.112  1   39.38 ? 321 LEU   B CD1 1 
ATOM   5533 C  CD2 . LEU   B 1 336 ? 2.525   5.91    -7.848  1   38.56 ? 321 LEU   B CD2 1 
ATOM   5534 N  N   . SER   B 1 337 ? 2.321   9.28    -4.037  1   33.61 ? 322 SER   B N   1 
ATOM   5535 C  CA  . SER   B 1 337 ? 3.284   10.233  -3.513  1   34.46 ? 322 SER   B CA  1 
ATOM   5536 C  C   . SER   B 1 337 ? 3.759   9.979   -2.077  1   34.74 ? 322 SER   B C   1 
ATOM   5537 O  O   . SER   B 1 337 ? 4.547   10.774  -1.565  1   34.7  ? 322 SER   B O   1 
ATOM   5538 C  CB  . SER   B 1 337 ? 2.705   11.632  -3.599  1   34.94 ? 322 SER   B CB  1 
ATOM   5539 O  OG  . SER   B 1 337 ? 1.682   11.794  -2.633  1   36.98 ? 322 SER   B OG  1 
ATOM   5540 N  N   . LYS   B 1 338 ? 3.3     8.9     -1.428  1   34.18 ? 323 LYS   B N   1 
ATOM   5541 C  CA  . LYS   B 1 338 ? 3.638   8.658   -0.02   1   33.74 ? 323 LYS   B CA  1 
ATOM   5542 C  C   . LYS   B 1 338 ? 4.81    7.715   0.294   1   32.65 ? 323 LYS   B C   1 
ATOM   5543 O  O   . LYS   B 1 338 ? 5.216   7.672   1.461   1   33.22 ? 323 LYS   B O   1 
ATOM   5544 C  CB  . LYS   B 1 338 ? 2.412   8.15    0.748   1   35.16 ? 323 LYS   B CB  1 
ATOM   5545 C  CG  . LYS   B 1 338 ? 1.291   9.156   0.878   1   39.17 ? 323 LYS   B CG  1 
ATOM   5546 C  CD  . LYS   B 1 338 ? 1.696   10.411  1.605   1   44.4  ? 323 LYS   B CD  1 
ATOM   5547 C  CE  . LYS   B 1 338 ? 0.747   11.551  1.34    1   50.09 ? 323 LYS   B CE  1 
ATOM   5548 N  NZ  . LYS   B 1 338 ? 0.69    11.937  -0.102  1   54.03 ? 323 LYS   B NZ  1 
ATOM   5549 N  N   . GLY   B 1 339 ? 5.335   6.968   -0.682  1   31.04 ? 324 GLY   B N   1 
ATOM   5550 C  CA  . GLY   B 1 339 ? 6.417   6.008   -0.457  1   30.62 ? 324 GLY   B CA  1 
ATOM   5551 C  C   . GLY   B 1 339 ? 6.068   4.997   0.622   1   30.74 ? 324 GLY   B C   1 
ATOM   5552 O  O   . GLY   B 1 339 ? 6.891   4.674   1.496   1   31.51 ? 324 GLY   B O   1 
ATOM   5553 N  N   . ASP   B 1 340 ? 4.816   4.517   0.584   1   28.82 ? 325 ASP   B N   1 
ATOM   5554 C  CA  . ASP   B 1 340 ? 4.271   3.651   1.614   1   27.46 ? 325 ASP   B CA  1 
ATOM   5555 C  C   . ASP   B 1 340 ? 3.741   2.377   0.982   1   26.78 ? 325 ASP   B C   1 
ATOM   5556 O  O   . ASP   B 1 340 ? 2.697   2.403   0.332   1   25.97 ? 325 ASP   B O   1 
ATOM   5557 C  CB  . ASP   B 1 340 ? 3.174   4.457   2.324   1   27.55 ? 325 ASP   B CB  1 
ATOM   5558 C  CG  . ASP   B 1 340 ? 2.473   3.824   3.499   1   30.29 ? 325 ASP   B CG  1 
ATOM   5559 O  OD1 . ASP   B 1 340 ? 2.365   2.578   3.531   1   30.61 ? 325 ASP   B OD1 1 
ATOM   5560 O  OD2 . ASP   B 1 340 ? 2.013   4.574   4.38    1   32.03 ? 325 ASP   B OD2 1 
ATOM   5561 N  N   . ALA   B 1 341 ? 4.481   1.283   1.122   1   26.68 ? 326 ALA   B N   1 
ATOM   5562 C  CA  . ALA   B 1 341 ? 4.142   -0.014  0.544   1   27.26 ? 326 ALA   B CA  1 
ATOM   5563 C  C   . ALA   B 1 341 ? 2.797   -0.56   1.049   1   27.59 ? 326 ALA   B C   1 
ATOM   5564 O  O   . ALA   B 1 341 ? 2.039   -1.099  0.248   1   27.41 ? 326 ALA   B O   1 
ATOM   5565 C  CB  . ALA   B 1 341 ? 5.257   -1.026  0.789   1   27.59 ? 326 ALA   B CB  1 
ATOM   5566 N  N   . GLY   B 1 342 ? 2.496   -0.406  2.34    1   26.88 ? 327 GLY   B N   1 
ATOM   5567 C  CA  . GLY   B 1 342 ? 1.211   -0.851  2.876   1   27.42 ? 327 GLY   B CA  1 
ATOM   5568 C  C   . GLY   B 1 342 ? 0.027   -0.134  2.222   1   27.82 ? 327 GLY   B C   1 
ATOM   5569 O  O   . GLY   B 1 342 ? -0.987  -0.753  1.892   1   28.17 ? 327 GLY   B O   1 
ATOM   5570 N  N   . LEU   B 1 343 ? 0.148   1.185   2.029   1   27.09 ? 328 LEU   B N   1 
ATOM   5571 C  CA  . LEU   B 1 343 ? -0.886  2       1.413   1   27.01 ? 328 LEU   B CA  1 
ATOM   5572 C  C   . LEU   B 1 343 ? -1.041  1.678   -0.08   1   27.15 ? 328 LEU   B C   1 
ATOM   5573 O  O   . LEU   B 1 343 ? -2.176  1.628   -0.579  1   26.77 ? 328 LEU   B O   1 
ATOM   5574 C  CB  . LEU   B 1 343 ? -0.541  3.472   1.607   1   27.33 ? 328 LEU   B CB  1 
ATOM   5575 C  CG  . LEU   B 1 343 ? -1.662  4.483   1.707   1   28.81 ? 328 LEU   B CG  1 
ATOM   5576 C  CD1 . LEU   B 1 343 ? -2.742  4.056   2.726   1   28.56 ? 328 LEU   B CD1 1 
ATOM   5577 C  CD2 . LEU   B 1 343 ? -1.091  5.88    2.055   1   28.96 ? 328 LEU   B CD2 1 
ATOM   5578 N  N   . ARG   B 1 344 ? 0.089   1.44    -0.792  1   27    ? 329 ARG   B N   1 
ATOM   5579 C  CA  . ARG   B 1 344 ? 0.046   1.061   -2.198  1   27.11 ? 329 ARG   B CA  1 
ATOM   5580 C  C   . ARG   B 1 344 ? -0.62   -0.309  -2.351  1   28.16 ? 329 ARG   B C   1 
ATOM   5581 O  O   . ARG   B 1 344 ? -1.388  -0.511  -3.295  1   27.57 ? 329 ARG   B O   1 
ATOM   5582 C  CB  . ARG   B 1 344 ? 1.448   1.016   -2.824  1   28.26 ? 329 ARG   B CB  1 
ATOM   5583 C  CG  . ARG   B 1 344 ? 2.102   2.389   -3.024  1   30.43 ? 329 ARG   B CG  1 
ATOM   5584 C  CD  . ARG   B 1 344 ? 3.299   2.332   -3.997  1   32.76 ? 329 ARG   B CD  1 
ATOM   5585 N  NE  . ARG   B 1 344 ? 4.338   1.362   -3.611  1   35.09 ? 329 ARG   B NE  1 
ATOM   5586 C  CZ  . ARG   B 1 344 ? 5.308   1.618   -2.728  1   34.39 ? 329 ARG   B CZ  1 
ATOM   5587 N  NH1 . ARG   B 1 344 ? 5.378   2.802   -2.135  1   31.63 ? 329 ARG   B NH1 1 
ATOM   5588 N  NH2 . ARG   B 1 344 ? 6.205   0.686   -2.428  1   32.65 ? 329 ARG   B NH2 1 
ATOM   5589 N  N   . GLU   B 1 345 ? -0.336  -1.247  -1.44   1   28.34 ? 330 GLU   B N   1 
ATOM   5590 C  CA  . GLU   B 1 345 ? -0.926  -2.586  -1.527  1   29.28 ? 330 GLU   B CA  1 
ATOM   5591 C  C   . GLU   B 1 345 ? -2.427  -2.558  -1.344  1   29.02 ? 330 GLU   B C   1 
ATOM   5592 O  O   . GLU   B 1 345 ? -3.143  -3.301  -2.035  1   29.43 ? 330 GLU   B O   1 
ATOM   5593 C  CB  . GLU   B 1 345 ? -0.29   -3.531  -0.508  1   32.35 ? 330 GLU   B CB  1 
ATOM   5594 C  CG  . GLU   B 1 345 ? 1.063   -4.054  -0.941  1   42.63 ? 330 GLU   B CG  1 
ATOM   5595 C  CD  . GLU   B 1 345 ? 1.761   -4.805  0.175   1   54.95 ? 330 GLU   B CD  1 
ATOM   5596 O  OE1 . GLU   B 1 345 ? 1.108   -5.668  0.816   1   58.15 ? 330 GLU   B OE1 1 
ATOM   5597 O  OE2 . GLU   B 1 345 ? 2.955   -4.513  0.423   1   57.6  ? 330 GLU   B OE2 1 
ATOM   5598 N  N   . ALA   B 1 346 ? -2.912  -1.739  -0.405  1   28.4  ? 331 ALA   B N   1 
ATOM   5599 C  CA  . ALA   B 1 346 ? -4.342  -1.593  -0.147  1   28.24 ? 331 ALA   B CA  1 
ATOM   5600 C  C   . ALA   B 1 346 ? -5.048  -0.96   -1.374  1   28.18 ? 331 ALA   B C   1 
ATOM   5601 O  O   . ALA   B 1 346 ? -6.133  -1.391  -1.751  1   28.05 ? 331 ALA   B O   1 
ATOM   5602 C  CB  . ALA   B 1 346 ? -4.56   -0.736  1.081   1   28.15 ? 331 ALA   B CB  1 
ATOM   5603 N  N   . TYR   B 1 347 ? -4.392  0.024   -2.024  1   27.4  ? 332 TYR   B N   1 
ATOM   5604 C  CA  . TYR   B 1 347 ? -4.932  0.662   -3.219  1   26.9  ? 332 TYR   B CA  1 
ATOM   5605 C  C   . TYR   B 1 347 ? -4.975  -0.385  -4.358  1   28.11 ? 332 TYR   B C   1 
ATOM   5606 O  O   . TYR   B 1 347 ? -5.969  -0.486  -5.084  1   28.48 ? 332 TYR   B O   1 
ATOM   5607 C  CB  . TYR   B 1 347 ? -4.064  1.879   -3.613  1   25.66 ? 332 TYR   B CB  1 
ATOM   5608 C  CG  . TYR   B 1 347 ? -4.402  2.405   -4.985  1   24.77 ? 332 TYR   B CG  1 
ATOM   5609 C  CD1 . TYR   B 1 347 ? -5.399  3.353   -5.161  1   25.36 ? 332 TYR   B CD1 1 
ATOM   5610 C  CD2 . TYR   B 1 347 ? -3.75   1.924   -6.112  1   24.7  ? 332 TYR   B CD2 1 
ATOM   5611 C  CE1 . TYR   B 1 347 ? -5.73   3.819   -6.425  1   25.81 ? 332 TYR   B CE1 1 
ATOM   5612 C  CE2 . TYR   B 1 347 ? -4.069  2.381   -7.375  1   25.66 ? 332 TYR   B CE2 1 
ATOM   5613 C  CZ  . TYR   B 1 347 ? -5.069  3.317   -7.532  1   25.97 ? 332 TYR   B CZ  1 
ATOM   5614 O  OH  . TYR   B 1 347 ? -5.386  3.748   -8.797  1   26.52 ? 332 TYR   B OH  1 
ATOM   5615 N  N   . ASP   B 1 348 ? -3.9    -1.161  -4.51   1   28.13 ? 333 ASP   B N   1 
ATOM   5616 C  CA  . ASP   B 1 348 ? -3.834  -2.191  -5.534  1   27.88 ? 333 ASP   B CA  1 
ATOM   5617 C  C   . ASP   B 1 348 ? -4.844  -3.311  -5.301  1   28.38 ? 333 ASP   B C   1 
ATOM   5618 O  O   . ASP   B 1 348 ? -5.292  -3.926  -6.268  1   27.9  ? 333 ASP   B O   1 
ATOM   5619 C  CB  . ASP   B 1 348 ? -2.414  -2.753  -5.676  1   27.78 ? 333 ASP   B CB  1 
ATOM   5620 C  CG  . ASP   B 1 348 ? -1.492  -1.921  -6.552  1   30.38 ? 333 ASP   B CG  1 
ATOM   5621 O  OD1 . ASP   B 1 348 ? -1.928  -0.841  -7.029  1   28.94 ? 333 ASP   B OD1 1 
ATOM   5622 O  OD2 . ASP   B 1 348 ? -0.346  -2.354  -6.784  1   32.29 ? 333 ASP   B OD2 1 
ATOM   5623 N  N   . ALA   B 1 349 ? -5.223  -3.568  -4.042  1   28.26 ? 334 ALA   B N   1 
ATOM   5624 C  CA  . ALA   B 1 349 ? -6.228  -4.595  -3.756  1   28.35 ? 334 ALA   B CA  1 
ATOM   5625 C  C   . ALA   B 1 349 ? -7.59   -4.149  -4.356  1   28.21 ? 334 ALA   B C   1 
ATOM   5626 O  O   . ALA   B 1 349 ? -8.353  -4.99   -4.834  1   27.86 ? 334 ALA   B O   1 
ATOM   5627 C  CB  . ALA   B 1 349 ? -6.35   -4.814  -2.256  1   28.12 ? 334 ALA   B CB  1 
ATOM   5628 N  N   . CYS   B 1 350 ? -7.871  -2.829  -4.344  1   26.84 ? 335 CYS   B N   1 
ATOM   5629 C  CA  . CYS   B 1 350 ? -9.086  -2.248  -4.902  1   25.77 ? 335 CYS   B CA  1 
ATOM   5630 C  C   . CYS   B 1 350 ? -9.072  -2.408  -6.415  1   25.31 ? 335 CYS   B C   1 
ATOM   5631 O  O   . CYS   B 1 350 ? -10.049 -2.893  -6.989  1   26.15 ? 335 CYS   B O   1 
ATOM   5632 C  CB  . CYS   B 1 350 ? -9.209  -0.777  -4.501  1   25.58 ? 335 CYS   B CB  1 
ATOM   5633 S  SG  . CYS   B 1 350 ? -9.626  -0.506  -2.766  1   26.01 ? 335 CYS   B SG  1 
ATOM   5634 N  N   . VAL   B 1 351 ? -7.982  -1.985  -7.064  1   24.71 ? 336 VAL   B N   1 
ATOM   5635 C  CA  . VAL   B 1 351 ? -7.804  -2.09   -8.501  1   24.43 ? 336 VAL   B CA  1 
ATOM   5636 C  C   . VAL   B 1 351 ? -7.878  -3.549  -8.961  1   25.53 ? 336 VAL   B C   1 
ATOM   5637 O  O   . VAL   B 1 351 ? -8.603  -3.864  -9.924  1   25.85 ? 336 VAL   B O   1 
ATOM   5638 C  CB  . VAL   B 1 351 ? -6.494  -1.418  -8.946  1   23.69 ? 336 VAL   B CB  1 
ATOM   5639 C  CG1 . VAL   B 1 351 ? -6.224  -1.677  -10.425 1   24.27 ? 336 VAL   B CG1 1 
ATOM   5640 C  CG2 . VAL   B 1 351 ? -6.495  0.08    -8.619  1   23.18 ? 336 VAL   B CG2 1 
ATOM   5641 N  N   . LYS   B 1 352 ? -7.181  -4.454  -8.244  1   24.79 ? 337 LYS   B N   1 
ATOM   5642 C  CA  . LYS   B 1 352 ? -7.219  -5.88   -8.549  1   25.19 ? 337 LYS   B CA  1 
ATOM   5643 C  C   . LYS   B 1 352 ? -8.654  -6.434  -8.504  1   24.87 ? 337 LYS   B C   1 
ATOM   5644 O  O   . LYS   B 1 352 ? -9.028  -7.202  -9.398  1   25.09 ? 337 LYS   B O   1 
ATOM   5645 C  CB  . LYS   B 1 352 ? -6.335  -6.678  -7.574  1   26.99 ? 337 LYS   B CB  1 
ATOM   5646 C  CG  . LYS   B 1 352 ? -4.877  -6.765  -7.987  1   32.13 ? 337 LYS   B CG  1 
ATOM   5647 N  N   . ALA   B 1 353 ? -9.442  -6.059  -7.47   1   24.3  ? 338 ALA   B N   1 
ATOM   5648 C  CA  . ALA   B 1 353 ? -10.827 -6.497  -7.345  1   24.47 ? 338 ALA   B CA  1 
ATOM   5649 C  C   . ALA   B 1 353 ? -11.672 -6.03   -8.563  1   24.03 ? 338 ALA   B C   1 
ATOM   5650 O  O   . ALA   B 1 353 ? -12.495 -6.808  -9.044  1   23.81 ? 338 ALA   B O   1 
ATOM   5651 C  CB  . ALA   B 1 353 ? -11.437 -5.995  -6.053  1   24.76 ? 338 ALA   B CB  1 
ATOM   5652 N  N   . LEU   B 1 354 ? -11.433 -4.809  -9.086  1   23.42 ? 339 LEU   B N   1 
ATOM   5653 C  CA  . LEU   B 1 354 ? -12.141 -4.314  -10.282 1   23.53 ? 339 LEU   B CA  1 
ATOM   5654 C  C   . LEU   B 1 354 ? -11.703 -5.07   -11.514 1   22.36 ? 339 LEU   B C   1 
ATOM   5655 O  O   . LEU   B 1 354 ? -12.534 -5.342  -12.383 1   22.18 ? 339 LEU   B O   1 
ATOM   5656 C  CB  . LEU   B 1 354 ? -11.932 -2.806  -10.549 1   24.02 ? 339 LEU   B CB  1 
ATOM   5657 C  CG  . LEU   B 1 354 ? -12.722 -1.867  -9.693  1   26.96 ? 339 LEU   B CG  1 
ATOM   5658 C  CD1 . LEU   B 1 354 ? -12.326 -0.406  -10.011 1   26.97 ? 339 LEU   B CD1 1 
ATOM   5659 C  CD2 . LEU   B 1 354 ? -14.236 -2.056  -9.922  1   28.25 ? 339 LEU   B CD2 1 
ATOM   5660 N  N   . VAL   B 1 355 ? -10.409 -5.402  -11.621 1   21.34 ? 340 VAL   B N   1 
ATOM   5661 C  CA  . VAL   B 1 355 ? -9.911  -6.181  -12.749 1   21.28 ? 340 VAL   B CA  1 
ATOM   5662 C  C   . VAL   B 1 355 ? -10.574 -7.584  -12.698 1   21.32 ? 340 VAL   B C   1 
ATOM   5663 O  O   . VAL   B 1 355 ? -11.065 -8.057  -13.715 1   20.71 ? 340 VAL   B O   1 
ATOM   5664 C  CB  . VAL   B 1 355 ? -8.366  -6.311  -12.76  1   22.65 ? 340 VAL   B CB  1 
ATOM   5665 C  CG1 . VAL   B 1 355 ? -7.915  -7.323  -13.819 1   23.39 ? 340 VAL   B CG1 1 
ATOM   5666 C  CG2 . VAL   B 1 355 ? -7.682  -4.946  -12.963 1   22.64 ? 340 VAL   B CG2 1 
ATOM   5667 N  N   . SER   B 1 356 ? -10.643 -8.195  -11.515 1   21.41 ? 341 SER   B N   1 
ATOM   5668 C  CA  . SER   B 1 356 ? -11.289 -9.523  -11.377 1   22.85 ? 341 SER   B CA  1 
ATOM   5669 C  C   . SER   B 1 356 ? -12.767 -9.484  -11.835 1   22.45 ? 341 SER   B C   1 
ATOM   5670 O  O   . SER   B 1 356 ? -13.226 -10.419 -12.48  1   23.23 ? 341 SER   B O   1 
ATOM   5671 C  CB  . SER   B 1 356 ? -11.206 -10.016 -9.94   1   25.63 ? 341 SER   B CB  1 
ATOM   5672 O  OG  . SER   B 1 356 ? -9.843  -10.207 -9.598  1   30.13 ? 341 SER   B OG  1 
ATOM   5673 N  N   . LEU   B 1 357 ? -13.515 -8.427  -11.455 1   21.51 ? 342 LEU   B N   1 
ATOM   5674 C  CA  . LEU   B 1 357 ? -14.914 -8.259  -11.852 1   22.16 ? 342 LEU   B CA  1 
ATOM   5675 C  C   . LEU   B 1 357 ? -15.021 -8.17   -13.364 1   21.85 ? 342 LEU   B C   1 
ATOM   5676 O  O   . LEU   B 1 357 ? -15.857 -8.86   -13.974 1   21.65 ? 342 LEU   B O   1 
ATOM   5677 C  CB  . LEU   B 1 357 ? -15.485 -6.973  -11.218 1   22.66 ? 342 LEU   B CB  1 
ATOM   5678 C  CG  . LEU   B 1 357 ? -16.046 -7.17   -9.847  1   26.01 ? 342 LEU   B CG  1 
ATOM   5679 C  CD1 . LEU   B 1 357 ? -16.133 -5.867  -9.104  1   26.71 ? 342 LEU   B CD1 1 
ATOM   5680 C  CD2 . LEU   B 1 357 ? -17.427 -7.853  -9.939  1   28.48 ? 342 LEU   B CD2 1 
ATOM   5681 N  N   . ARG   B 1 358 ? -14.179 -7.303  -13.98  1   20.28 ? 343 ARG   B N   1 
ATOM   5682 C  CA  . ARG   B 1 358 ? -14.198 -7.083  -15.417 1   19.92 ? 343 ARG   B CA  1 
ATOM   5683 C  C   . ARG   B 1 358 ? -13.776 -8.323  -16.206 1   19.91 ? 343 ARG   B C   1 
ATOM   5684 O  O   . ARG   B 1 358 ? -14.352 -8.614  -17.261 1   18.72 ? 343 ARG   B O   1 
ATOM   5685 C  CB  . ARG   B 1 358 ? -13.361 -5.839  -15.766 1   20.12 ? 343 ARG   B CB  1 
ATOM   5686 C  CG  . ARG   B 1 358 ? -14.07  -4.603  -15.186 1   18.78 ? 343 ARG   B CG  1 
ATOM   5687 C  CD  . ARG   B 1 358 ? -13.453 -3.261  -15.533 1   22.04 ? 343 ARG   B CD  1 
ATOM   5688 N  NE  . ARG   B 1 358 ? -14.477 -2.238  -15.361 1   22.5  ? 343 ARG   B NE  1 
ATOM   5689 C  CZ  . ARG   B 1 358 ? -14.321 -1.105  -14.688 1   24.86 ? 343 ARG   B CZ  1 
ATOM   5690 N  NH1 . ARG   B 1 358 ? -13.139 -0.798  -14.147 1   21.75 ? 343 ARG   B NH1 1 
ATOM   5691 N  NH2 . ARG   B 1 358 ? -15.321 -0.235  -14.608 1   24.88 ? 343 ARG   B NH2 1 
ATOM   5692 N  N   . SER   B 1 359 ? -12.822 -9.086  -15.662 1   19.57 ? 344 SER   B N   1 
ATOM   5693 C  CA  . SER   B 1 359 ? -12.358 -10.301 -16.328 1   21.53 ? 344 SER   B CA  1 
ATOM   5694 C  C   . SER   B 1 359 ? -13.497 -11.363 -16.282 1   22.02 ? 344 SER   B C   1 
ATOM   5695 O  O   . SER   B 1 359 ? -13.726 -12.038 -17.28  1   22.24 ? 344 SER   B O   1 
ATOM   5696 C  CB  . SER   B 1 359 ? -11.115 -10.872 -15.632 1   22.16 ? 344 SER   B CB  1 
ATOM   5697 O  OG  . SER   B 1 359 ? -10.006 -10.001 -15.8   1   23.29 ? 344 SER   B OG  1 
ATOM   5698 N  N   . TYR   B 1 360 ? -14.202 -11.484 -15.158 1   21.43 ? 345 TYR   B N   1 
ATOM   5699 C  CA  . TYR   B 1 360 ? -15.29  -12.464 -15.047 1   22.12 ? 345 TYR   B CA  1 
ATOM   5700 C  C   . TYR   B 1 360 ? -16.448 -12.054 -16.001 1   22.47 ? 345 TYR   B C   1 
ATOM   5701 O  O   . TYR   B 1 360 ? -16.997 -12.886 -16.747 1   22.48 ? 345 TYR   B O   1 
ATOM   5702 C  CB  . TYR   B 1 360 ? -15.777 -12.508 -13.606 1   22.95 ? 345 TYR   B CB  1 
ATOM   5703 C  CG  . TYR   B 1 360 ? -16.789 -13.599 -13.373 1   25.3  ? 345 TYR   B CG  1 
ATOM   5704 C  CD1 . TYR   B 1 360 ? -16.401 -14.934 -13.322 1   26.99 ? 345 TYR   B CD1 1 
ATOM   5705 C  CD2 . TYR   B 1 360 ? -18.138 -13.303 -13.224 1   26.8  ? 345 TYR   B CD2 1 
ATOM   5706 C  CE1 . TYR   B 1 360 ? -17.337 -15.95  -13.157 1   28.79 ? 345 TYR   B CE1 1 
ATOM   5707 C  CE2 . TYR   B 1 360 ? -19.082 -14.309 -13.045 1   28.32 ? 345 TYR   B CE2 1 
ATOM   5708 C  CZ  . TYR   B 1 360 ? -18.679 -15.636 -13.033 1   30.3  ? 345 TYR   B CZ  1 
ATOM   5709 O  OH  . TYR   B 1 360 ? -19.606 -16.657 -12.896 1   32.42 ? 345 TYR   B OH  1 
ATOM   5710 N  N   . HIS   B 1 361 ? -16.748 -10.745 -16.038 1   20.82 ? 346 HIS   B N   1 
ATOM   5711 C  CA  . HIS   B 1 361 ? -17.76  -10.185 -16.918 1   20.21 ? 346 HIS   B CA  1 
ATOM   5712 C  C   . HIS   B 1 361 ? -17.396 -10.476 -18.383 1   20.85 ? 346 HIS   B C   1 
ATOM   5713 O  O   . HIS   B 1 361 ? -18.287 -10.872 -19.131 1   20.3  ? 346 HIS   B O   1 
ATOM   5714 C  CB  . HIS   B 1 361 ? -17.915 -8.677  -16.622 1   20.27 ? 346 HIS   B CB  1 
ATOM   5715 C  CG  . HIS   B 1 361 ? -18.92  -7.97   -17.473 1   20.92 ? 346 HIS   B CG  1 
ATOM   5716 N  ND1 . HIS   B 1 361 ? -18.534 -7.239  -18.573 1   21.5  ? 346 HIS   B ND1 1 
ATOM   5717 C  CD2 . HIS   B 1 361 ? -20.263 -7.88   -17.332 1   21.45 ? 346 HIS   B CD2 1 
ATOM   5718 C  CE1 . HIS   B 1 361 ? -19.644 -6.731  -19.077 1   21.64 ? 346 HIS   B CE1 1 
ATOM   5719 N  NE2 . HIS   B 1 361 ? -20.715 -7.115  -18.372 1   23.09 ? 346 HIS   B NE2 1 
ATOM   5720 N  N   . LEU   B 1 362 ? -16.101 -10.38  -18.782 1   21.33 ? 347 LEU   B N   1 
ATOM   5721 C  CA  . LEU   B 1 362 ? -15.684 -10.742 -20.16  1   21.91 ? 347 LEU   B CA  1 
ATOM   5722 C  C   . LEU   B 1 362 ? -15.999 -12.216 -20.5   1   22.3  ? 347 LEU   B C   1 
ATOM   5723 O  O   . LEU   B 1 362 ? -16.475 -12.511 -21.611 1   20.68 ? 347 LEU   B O   1 
ATOM   5724 C  CB  . LEU   B 1 362 ? -14.203 -10.474 -20.417 1   22.73 ? 347 LEU   B CB  1 
ATOM   5725 C  CG  . LEU   B 1 362 ? -13.929 -9.076  -20.864 1   25.29 ? 347 LEU   B CG  1 
ATOM   5726 C  CD1 . LEU   B 1 362 ? -12.472 -8.671  -20.589 1   25.66 ? 347 LEU   B CD1 1 
ATOM   5727 C  CD2 . LEU   B 1 362 ? -14.376 -8.883  -22.296 1   25.79 ? 347 LEU   B CD2 1 
ATOM   5728 N  N   . GLN   B 1 363 ? -15.75  -13.139 -19.541 1   23.2  ? 348 GLN   B N   1 
ATOM   5729 C  CA  . GLN   B 1 363 ? -16.084 -14.551 -19.763 1   25.02 ? 348 GLN   B CA  1 
ATOM   5730 C  C   . GLN   B 1 363 ? -17.604 -14.722 -19.938 1   24.48 ? 348 GLN   B C   1 
ATOM   5731 O  O   . GLN   B 1 363 ? -18.032 -15.525 -20.766 1   24.37 ? 348 GLN   B O   1 
ATOM   5732 C  CB  . GLN   B 1 363 ? -15.617 -15.414 -18.586 1   28.91 ? 348 GLN   B CB  1 
ATOM   5733 C  CG  . GLN   B 1 363 ? -14.106 -15.477 -18.48  1   36.13 ? 348 GLN   B CG  1 
ATOM   5734 C  CD  . GLN   B 1 363 ? -13.626 -16.097 -17.177 1   45.28 ? 348 GLN   B CD  1 
ATOM   5735 O  OE1 . GLN   B 1 363 ? -14.411 -16.571 -16.318 1   50.58 ? 348 GLN   B OE1 1 
ATOM   5736 N  NE2 . GLN   B 1 363 ? -12.319 -16.091 -16.998 1   44.55 ? 348 GLN   B NE2 1 
ATOM   5737 N  N   . ILE   B 1 364 ? -18.413 -13.989 -19.136 1   23.85 ? 349 ILE   B N   1 
ATOM   5738 C  CA  . ILE   B 1 364 ? -19.86  -14.025 -19.231 1   24.39 ? 349 ILE   B CA  1 
ATOM   5739 C  C   . ILE   B 1 364 ? -20.322 -13.543 -20.609 1   23.1  ? 349 ILE   B C   1 
ATOM   5740 O  O   . ILE   B 1 364 ? -21.197 -14.168 -21.237 1   22.11 ? 349 ILE   B O   1 
ATOM   5741 C  CB  . ILE   B 1 364 ? -20.442 -13.156 -18.088 1   26.49 ? 349 ILE   B CB  1 
ATOM   5742 C  CG1 . ILE   B 1 364 ? -20.3   -13.933 -16.789 1   28.66 ? 349 ILE   B CG1 1 
ATOM   5743 C  CG2 . ILE   B 1 364 ? -21.908 -12.667 -18.376 1   26.99 ? 349 ILE   B CG2 1 
ATOM   5744 C  CD1 . ILE   B 1 364 ? -20.672 -13.201 -15.704 1   31.97 ? 349 ILE   B CD1 1 
ATOM   5745 N  N   . VAL   B 1 365 ? -19.738 -12.44  -21.087 1   21.44 ? 350 VAL   B N   1 
ATOM   5746 C  CA  . VAL   B 1 365 ? -20.12  -11.91  -22.394 1   21.93 ? 350 VAL   B CA  1 
ATOM   5747 C  C   . VAL   B 1 365 ? -19.727 -12.889 -23.519 1   21.53 ? 350 VAL   B C   1 
ATOM   5748 O  O   . VAL   B 1 365 ? -20.451 -13.01  -24.504 1   21.32 ? 350 VAL   B O   1 
ATOM   5749 C  CB  . VAL   B 1 365 ? -19.542 -10.496 -22.596 1   23.39 ? 350 VAL   B CB  1 
ATOM   5750 C  CG1 . VAL   B 1 365 ? -19.76  -10.024 -24.011 1   23.67 ? 350 VAL   B CG1 1 
ATOM   5751 C  CG2 . VAL   B 1 365 ? -20.175 -9.517  -21.609 1   24.09 ? 350 VAL   B CG2 1 
ATOM   5752 N  N   . THR   B 1 366 ? -18.626 -13.652 -23.343 1   20.74 ? 351 THR   B N   1 
ATOM   5753 C  CA  . THR   B 1 366 ? -18.257 -14.673 -24.348 1   21.69 ? 351 THR   B CA  1 
ATOM   5754 C  C   . THR   B 1 366 ? -19.353 -15.76  -24.387 1   22.76 ? 351 THR   B C   1 
ATOM   5755 O  O   . THR   B 1 366 ? -19.809 -16.155 -25.47  1   23.66 ? 351 THR   B O   1 
ATOM   5756 C  CB  . THR   B 1 366 ? -16.863 -15.268 -24.058 1   22.81 ? 351 THR   B CB  1 
ATOM   5757 O  OG1 . THR   B 1 366 ? -15.882 -14.216 -24.191 1   22.84 ? 351 THR   B OG1 1 
ATOM   5758 C  CG2 . THR   B 1 366 ? -16.507 -16.399 -25.038 1   22.83 ? 351 THR   B CG2 1 
ATOM   5759 N  N   . LYS   B 1 367 ? -19.819 -16.18  -23.215 1   22.41 ? 352 LYS   B N   1 
ATOM   5760 C  CA  . LYS   B 1 367 ? -20.889 -17.191 -23.132 1   23.19 ? 352 LYS   B CA  1 
ATOM   5761 C  C   . LYS   B 1 367 ? -22.254 -16.7   -23.658 1   23.83 ? 352 LYS   B C   1 
ATOM   5762 O  O   . LYS   B 1 367 ? -22.928 -17.459 -24.366 1   24.28 ? 352 LYS   B O   1 
ATOM   5763 C  CB  . LYS   B 1 367 ? -21.059 -17.66  -21.677 1   24.21 ? 352 LYS   B CB  1 
ATOM   5764 C  CG  . LYS   B 1 367 ? -22.238 -18.609 -21.42  1   25.81 ? 352 LYS   B CG  1 
ATOM   5765 C  CD  . LYS   B 1 367 ? -22.266 -19.108 -19.971 1   28.77 ? 352 LYS   B CD  1 
ATOM   5766 C  CE  . LYS   B 1 367 ? -23.515 -19.928 -19.698 1   31.65 ? 352 LYS   B CE  1 
ATOM   5767 N  NZ  . LYS   B 1 367 ? -23.668 -20.241 -18.256 1   32.06 ? 352 LYS   B NZ  1 
ATOM   5768 N  N   . TYR   B 1 368 ? -22.691 -15.473 -23.263 1   22.57 ? 353 TYR   B N   1 
ATOM   5769 C  CA  . TYR   B 1 368 ? -24.038 -14.982 -23.55  1   22.21 ? 353 TYR   B CA  1 
ATOM   5770 C  C   . TYR   B 1 368 ? -24.192 -14.241 -24.837 1   21.36 ? 353 TYR   B C   1 
ATOM   5771 O  O   . TYR   B 1 368 ? -25.314 -14.152 -25.35  1   21.74 ? 353 TYR   B O   1 
ATOM   5772 C  CB  . TYR   B 1 368 ? -24.558 -14.121 -22.384 1   22.9  ? 353 TYR   B CB  1 
ATOM   5773 C  CG  . TYR   B 1 368 ? -24.941 -14.974 -21.196 1   24.79 ? 353 TYR   B CG  1 
ATOM   5774 C  CD1 . TYR   B 1 368 ? -24.01  -15.306 -20.226 1   26.39 ? 353 TYR   B CD1 1 
ATOM   5775 C  CD2 . TYR   B 1 368 ? -26.194 -15.558 -21.115 1   25.89 ? 353 TYR   B CD2 1 
ATOM   5776 C  CE1 . TYR   B 1 368 ? -24.337 -16.137 -19.162 1   27.71 ? 353 TYR   B CE1 1 
ATOM   5777 C  CE2 . TYR   B 1 368 ? -26.532 -16.397 -20.062 1   27.55 ? 353 TYR   B CE2 1 
ATOM   5778 C  CZ  . TYR   B 1 368 ? -25.595 -16.699 -19.094 1   28.73 ? 353 TYR   B CZ  1 
ATOM   5779 O  OH  . TYR   B 1 368 ? -25.938 -17.533 -18.055 1   30.8  ? 353 TYR   B OH  1 
ATOM   5780 N  N   . ILE   B 1 369 ? -23.092 -13.679 -25.374 1   19.77 ? 354 ILE   B N   1 
ATOM   5781 C  CA  . ILE   B 1 369 ? -23.179 -12.955 -26.624 1   19.63 ? 354 ILE   B CA  1 
ATOM   5782 C  C   . ILE   B 1 369 ? -22.292 -13.534 -27.749 1   21.37 ? 354 ILE   B C   1 
ATOM   5783 O  O   . ILE   B 1 369 ? -22.818 -13.794 -28.827 1   22.01 ? 354 ILE   B O   1 
ATOM   5784 C  CB  . ILE   B 1 369 ? -22.917 -11.44  -26.439 1   18.92 ? 354 ILE   B CB  1 
ATOM   5785 C  CG1 . ILE   B 1 369 ? -23.995 -10.768 -25.52  1   18.9  ? 354 ILE   B CG1 1 
ATOM   5786 C  CG2 . ILE   B 1 369 ? -22.84  -10.728 -27.803 1   18.83 ? 354 ILE   B CG2 1 
ATOM   5787 C  CD1 . ILE   B 1 369 ? -23.663 -9.289  -25.2   1   19.43 ? 354 ILE   B CD1 1 
ATOM   5788 N  N   . LEU   B 1 370 ? -20.966 -13.626 -27.552 1   21.16 ? 355 LEU   B N   1 
ATOM   5789 C  CA  . LEU   B 1 370 ? -20.065 -14.037 -28.65  1   22.62 ? 355 LEU   B CA  1 
ATOM   5790 C  C   . LEU   B 1 370 ? -20.41  -15.418 -29.269 1   23.09 ? 355 LEU   B C   1 
ATOM   5791 O  O   . LEU   B 1 370 ? -20.588 -15.519 -30.48  1   24.4  ? 355 LEU   B O   1 
ATOM   5792 C  CB  . LEU   B 1 370 ? -18.593 -13.98  -28.2   1   23.59 ? 355 LEU   B CB  1 
ATOM   5793 C  CG  . LEU   B 1 370 ? -17.563 -14.221 -29.319 1   26.72 ? 355 LEU   B CG  1 
ATOM   5794 C  CD1 . LEU   B 1 370 ? -17.354 -12.951 -30.155 1   27.41 ? 355 LEU   B CD1 1 
ATOM   5795 C  CD2 . LEU   B 1 370 ? -16.189 -14.682 -28.726 1   28.77 ? 355 LEU   B CD2 1 
ATOM   5796 N  N   . ILE   B 1 371 ? -20.56  -16.429 -28.442 1   23.05 ? 356 ILE   B N   1 
ATOM   5797 C  CA  . ILE   B 1 371 ? -20.833 -17.783 -28.929 1   24.24 ? 356 ILE   B CA  1 
ATOM   5798 C  C   . ILE   B 1 371 ? -22.241 -17.871 -29.562 1   24.87 ? 356 ILE   B C   1 
ATOM   5799 O  O   . ILE   B 1 371 ? -22.318 -18.221 -30.745 1   24.67 ? 356 ILE   B O   1 
ATOM   5800 C  CB  . ILE   B 1 371 ? -20.53  -18.831 -27.839 1   25.28 ? 356 ILE   B CB  1 
ATOM   5801 C  CG1 . ILE   B 1 371 ? -18.989 -18.887 -27.628 1   26.22 ? 356 ILE   B CG1 1 
ATOM   5802 C  CG2 . ILE   B 1 371 ? -21.084 -20.215 -28.249 1   25.32 ? 356 ILE   B CG2 1 
ATOM   5803 C  CD1 . ILE   B 1 371 ? -18.538 -19.721 -26.54  1   28.04 ? 356 ILE   B CD1 1 
ATOM   5804 N  N   . PRO   B 1 372 ? -23.328 -17.404 -28.896 1   24.54 ? 357 PRO   B N   1 
ATOM   5805 C  CA  . PRO   B 1 372 ? -24.637 -17.378 -29.584 1   24.67 ? 357 PRO   B CA  1 
ATOM   5806 C  C   . PRO   B 1 372 ? -24.618 -16.544 -30.884 1   25.51 ? 357 PRO   B C   1 
ATOM   5807 O  O   . PRO   B 1 372 ? -25.222 -16.969 -31.871 1   26.06 ? 357 PRO   B O   1 
ATOM   5808 C  CB  . PRO   B 1 372 ? -25.586 -16.774 -28.533 1   24.9  ? 357 PRO   B CB  1 
ATOM   5809 C  CG  . PRO   B 1 372 ? -24.933 -17.032 -27.219 1   24.92 ? 357 PRO   B CG  1 
ATOM   5810 C  CD  . PRO   B 1 372 ? -23.444 -16.943 -27.496 1   23.82 ? 357 PRO   B CD  1 
ATOM   5811 N  N   . ALA   B 1 373 ? -23.882 -15.406 -30.935 1   24.88 ? 358 ALA   B N   1 
ATOM   5812 C  CA  . ALA   B 1 373 ? -23.789 -14.625 -32.184 1   25.6  ? 358 ALA   B CA  1 
ATOM   5813 C  C   . ALA   B 1 373 ? -23.116 -15.432 -33.304 1   27.44 ? 358 ALA   B C   1 
ATOM   5814 O  O   . ALA   B 1 373 ? -23.496 -15.309 -34.482 1   28.14 ? 358 ALA   B O   1 
ATOM   5815 C  CB  . ALA   B 1 373 ? -23.017 -13.337 -31.974 1   25.61 ? 358 ALA   B CB  1 
ATOM   5816 N  N   . SER   B 1 374 ? -22.134 -16.245 -32.941 1   27.68 ? 359 SER   B N   1 
ATOM   5817 C  CA  . SER   B 1 374 ? -21.434 -17.07  -33.928 1   29.6  ? 359 SER   B CA  1 
ATOM   5818 C  C   . SER   B 1 374 ? -22.357 -18.144 -34.53  1   32.96 ? 359 SER   B C   1 
ATOM   5819 O  O   . SER   B 1 374 ? -22.101 -18.588 -35.64  1   34.11 ? 359 SER   B O   1 
ATOM   5820 C  CB  . SER   B 1 374 ? -20.217 -17.733 -33.314 1   28.27 ? 359 SER   B CB  1 
ATOM   5821 O  OG  . SER   B 1 374 ? -20.572 -18.779 -32.431 1   26.95 ? 359 SER   B OG  1 
ATOM   5822 N  N   . GLN   B 1 375 ? -23.394 -18.572 -33.78  1   33.89 ? 360 GLN   B N   1 
ATOM   5823 C  CA  . GLN   B 1 375 ? -24.37  -19.584 -34.197 1   35.95 ? 360 GLN   B CA  1 
ATOM   5824 C  C   . GLN   B 1 375 ? -25.638 -18.96  -34.823 1   38.3  ? 360 GLN   B C   1 
ATOM   5825 O  O   . GLN   B 1 375 ? -26.545 -19.703 -35.158 1   38.78 ? 360 GLN   B O   1 
ATOM   5826 C  CB  . GLN   B 1 375 ? -24.764 -20.454 -32.985 1   37.82 ? 360 GLN   B CB  1 
ATOM   5827 C  CG  . GLN   B 1 375 ? -23.6   -21.197 -32.331 1   42.89 ? 360 GLN   B CG  1 
ATOM   5828 C  CD  . GLN   B 1 375 ? -23.892 -21.654 -30.908 1   51.51 ? 360 GLN   B CD  1 
ATOM   5829 O  OE1 . GLN   B 1 375 ? -24.901 -21.29  -30.294 1   54.13 ? 360 GLN   B OE1 1 
ATOM   5830 N  NE2 . GLN   B 1 375 ? -22.994 -22.446 -30.326 1   53.42 ? 360 GLN   B NE2 1 
ATOM   5831 N  N   . GLN   B 1 376 ? -25.72  -17.608 -34.951 1   39.49 ? 361 GLN   B N   1 
ATOM   5832 C  CA  . GLN   B 1 376 ? -26.892 -16.908 -35.501 1   41.34 ? 361 GLN   B CA  1 
ATOM   5833 C  C   . GLN   B 1 376 ? -27.038 -17.176 -36.984 1   42.73 ? 361 GLN   B C   1 
ATOM   5834 O  O   . GLN   B 1 376 ? -26.149 -16.806 -37.749 1   43.79 ? 361 GLN   B O   1 
ATOM   5835 C  CB  . GLN   B 1 376 ? -26.79  -15.386 -35.268 1   42.92 ? 361 GLN   B CB  1 
ATOM   5836 C  CG  . GLN   B 1 376 ? -28.134 -14.655 -35.48  1   45.5  ? 361 GLN   B CG  1 
ATOM   5837 C  CD  . GLN   B 1 376 ? -28.024 -13.148 -35.585 1   48.75 ? 361 GLN   B CD  1 
ATOM   5838 O  OE1 . GLN   B 1 376 ? -27.057 -12.532 -35.148 1   49.99 ? 361 GLN   B OE1 1 
ATOM   5839 N  NE2 . GLN   B 1 376 ? -29.021 -12.51  -36.174 1   49.41 ? 361 GLN   B NE2 1 
ATOM   5840 N  N   . SER   B 1 387 ? -22.218 -15.203 -37.531 1   48.99 ? 372 SER   B N   1 
ATOM   5841 C  CA  . SER   B 1 387 ? -22.311 -14.024 -38.391 1   49.2  ? 372 SER   B CA  1 
ATOM   5842 C  C   . SER   B 1 387 ? -20.922 -13.439 -38.632 1   49.62 ? 372 SER   B C   1 
ATOM   5843 O  O   . SER   B 1 387 ? -20.042 -13.497 -37.762 1   49.94 ? 372 SER   B O   1 
ATOM   5844 C  CB  . SER   B 1 387 ? -23.265 -12.993 -37.799 1   49.75 ? 372 SER   B CB  1 
ATOM   5845 O  OG  . SER   B 1 387 ? -23.274 -11.729 -38.443 1   51.08 ? 372 SER   B OG  1 
ATOM   5846 N  N   . LYS   B 1 388 ? -20.718 -12.899 -39.829 1   49.41 ? 373 LYS   B N   1 
ATOM   5847 C  CA  . LYS   B 1 388 ? -19.425 -12.363 -40.238 1   49.39 ? 373 LYS   B CA  1 
ATOM   5848 C  C   . LYS   B 1 388 ? -19.102 -10.989 -39.629 1   48.75 ? 373 LYS   B C   1 
ATOM   5849 O  O   . LYS   B 1 388 ? -17.945 -10.56  -39.674 1   49.74 ? 373 LYS   B O   1 
ATOM   5850 C  CB  . LYS   B 1 388 ? -19.336 -12.352 -41.77  1   51.84 ? 373 LYS   B CB  1 
ATOM   5851 C  CG  . LYS   B 1 388 ? -19.612 -13.74  -42.368 1   57.04 ? 373 LYS   B CG  1 
ATOM   5852 C  CD  . LYS   B 1 388 ? -19.58  -13.762 -43.898 1   61.88 ? 373 LYS   B CD  1 
ATOM   5853 C  CE  . LYS   B 1 388 ? -18.253 -14.215 -44.463 1   65.53 ? 373 LYS   B CE  1 
ATOM   5854 N  NZ  . LYS   B 1 388 ? -17.968 -15.642 -44.156 1   67.76 ? 373 LYS   B NZ  1 
ATOM   5855 N  N   . LEU   B 1 389 ? -20.105 -10.304 -39.042 1   46.72 ? 374 LEU   B N   1 
ATOM   5856 C  CA  . LEU   B 1 389 ? -19.905 -9.007  -38.402 1   44.58 ? 374 LEU   B CA  1 
ATOM   5857 C  C   . LEU   B 1 389 ? -19.765 -9.197  -36.881 1   42.5  ? 374 LEU   B C   1 
ATOM   5858 O  O   . LEU   B 1 389 ? -20.48  -10.015 -36.288 1   42.5  ? 374 LEU   B O   1 
ATOM   5859 C  CB  . LEU   B 1 389 ? -21.069 -8.058  -38.73  1   45.22 ? 374 LEU   B CB  1 
ATOM   5860 N  N   . GLU   B 1 390 ? -18.816 -8.478  -36.255 1   40.08 ? 375 GLU   B N   1 
ATOM   5861 C  CA  . GLU   B 1 390 ? -18.601 -8.607  -34.817 1   38.16 ? 375 GLU   B CA  1 
ATOM   5862 C  C   . GLU   B 1 390 ? -19.769 -8.026  -34.01  1   36.32 ? 375 GLU   B C   1 
ATOM   5863 O  O   . GLU   B 1 390 ? -20.467 -7.123  -34.478 1   36.77 ? 375 GLU   B O   1 
ATOM   5864 C  CB  . GLU   B 1 390 ? -17.276 -7.947  -34.395 1   39.33 ? 375 GLU   B CB  1 
ATOM   5865 C  CG  . GLU   B 1 390 ? -16.035 -8.609  -34.971 1   41.48 ? 375 GLU   B CG  1 
ATOM   5866 C  CD  . GLU   B 1 390 ? -15.881 -10.09  -34.677 1   41.93 ? 375 GLU   B CD  1 
ATOM   5867 O  OE1 . GLU   B 1 390 ? -16.035 -10.494 -33.499 1   35.79 ? 375 GLU   B OE1 1 
ATOM   5868 O  OE2 . GLU   B 1 390 ? -15.587 -10.846 -35.634 1   45.91 ? 375 GLU   B OE2 1 
ATOM   5869 N  N   . ALA   B 1 391 ? -19.982 -8.554  -32.806 1   33.85 ? 376 ALA   B N   1 
ATOM   5870 C  CA  . ALA   B 1 391 ? -21.056 -8.136  -31.915 1   32.55 ? 376 ALA   B CA  1 
ATOM   5871 C  C   . ALA   B 1 391 ? -20.944 -6.652  -31.596 1   31.71 ? 376 ALA   B C   1 
ATOM   5872 O  O   . ALA   B 1 391 ? -19.935 -6.213  -31.04  1   29.62 ? 376 ALA   B O   1 
ATOM   5873 C  CB  . ALA   B 1 391 ? -20.998 -8.94   -30.626 1   32.08 ? 376 ALA   B CB  1 
ATOM   5874 N  N   . LYS   B 1 392 ? -21.985 -5.878  -31.963 1   31.8  ? 377 LYS   B N   1 
ATOM   5875 C  CA  . LYS   B 1 392 ? -21.957 -4.445  -31.712 1   32.21 ? 377 LYS   B CA  1 
ATOM   5876 C  C   . LYS   B 1 392 ? -22.697 -4.088  -30.441 1   31.86 ? 377 LYS   B C   1 
ATOM   5877 O  O   . LYS   B 1 392 ? -23.796 -4.59   -30.199 1   32.06 ? 377 LYS   B O   1 
ATOM   5878 C  CB  . LYS   B 1 392 ? -22.47  -3.649  -32.931 1   35.18 ? 377 LYS   B CB  1 
ATOM   5879 C  CG  . LYS   B 1 392 ? -21.316 -3.238  -33.858 1   41.19 ? 377 LYS   B CG  1 
ATOM   5880 C  CD  . LYS   B 1 392 ? -21.352 -4.014  -35.17  1   45.69 ? 377 LYS   B CD  1 
ATOM   5881 C  CE  . LYS   B 1 392 ? -20.007 -4.164  -35.839 1   48.89 ? 377 LYS   B CE  1 
ATOM   5882 N  NZ  . LYS   B 1 392 ? -19.112 -3.017  -35.572 1   51.64 ? 377 LYS   B NZ  1 
ATOM   5883 N  N   . GLY   B 1 393 ? -22.092 -3.232  -29.625 1   31.17 ? 378 GLY   B N   1 
ATOM   5884 C  CA  . GLY   B 1 393 ? -22.717 -2.818  -28.379 1   30.83 ? 378 GLY   B CA  1 
ATOM   5885 C  C   . GLY   B 1 393 ? -23.565 -1.571  -28.544 1   30.79 ? 378 GLY   B C   1 
ATOM   5886 O  O   . GLY   B 1 393 ? -23.77  -1.102  -29.662 1   29.83 ? 378 GLY   B O   1 
ATOM   5887 N  N   . THR   B 1 394 ? -24.03  -1.011  -27.407 1   30.92 ? 379 THR   B N   1 
ATOM   5888 C  CA  . THR   B 1 394 ? -24.867 0.183   -27.32  1   31.72 ? 379 THR   B CA  1 
ATOM   5889 C  C   . THR   B 1 394 ? -24.291 1.423   -28.025 1   33.95 ? 379 THR   B C   1 
ATOM   5890 O  O   . THR   B 1 394 ? -25.037 2.275   -28.524 1   35.03 ? 379 THR   B O   1 
ATOM   5891 C  CB  . THR   B 1 394 ? -25.164 0.46    -25.851 1   31.43 ? 379 THR   B CB  1 
ATOM   5892 O  OG1 . THR   B 1 394 ? -25.805 -0.691  -25.284 1   31.47 ? 379 THR   B OG1 1 
ATOM   5893 C  CG2 . THR   B 1 394 ? -26.004 1.723   -25.65  1   31.43 ? 379 THR   B CG2 1 
ATOM   5894 N  N   . GLY   B 1 395 ? -22.976 1.504   -28.081 1   34.06 ? 380 GLY   B N   1 
ATOM   5895 C  CA  . GLY   B 1 395 ? -22.284 2.62    -28.709 1   34.94 ? 380 GLY   B CA  1 
ATOM   5896 C  C   . GLY   B 1 395 ? -22.032 2.467   -30.192 1   36.28 ? 380 GLY   B C   1 
ATOM   5897 O  O   . GLY   B 1 395 ? -21.368 3.318   -30.786 1   37.42 ? 380 GLY   B O   1 
ATOM   5898 N  N   . GLY   B 1 396 ? -22.561 1.401   -30.794 1   36.63 ? 381 GLY   B N   1 
ATOM   5899 C  CA  . GLY   B 1 396 ? -22.429 1.153   -32.226 1   37.25 ? 381 GLY   B CA  1 
ATOM   5900 C  C   . GLY   B 1 396 ? -21.11  0.549   -32.668 1   37.21 ? 381 GLY   B C   1 
ATOM   5901 O  O   . GLY   B 1 396 ? -20.91  0.324   -33.864 1   37.45 ? 381 GLY   B O   1 
ATOM   5902 N  N   . THR   B 1 397 ? -20.184 0.303   -31.711 1   36.14 ? 382 THR   B N   1 
ATOM   5903 C  CA  . THR   B 1 397 ? -18.874 -0.292  -31.989 1   35.36 ? 382 THR   B CA  1 
ATOM   5904 C  C   . THR   B 1 397 ? -18.723 -1.649  -31.243 1   33.72 ? 382 THR   B C   1 
ATOM   5905 O  O   . THR   B 1 397 ? -19.498 -1.936  -30.317 1   33.38 ? 382 THR   B O   1 
ATOM   5906 C  CB  . THR   B 1 397 ? -17.737 0.689   -31.653 1   37.14 ? 382 THR   B CB  1 
ATOM   5907 O  OG1 . THR   B 1 397 ? -17.622 0.803   -30.235 1   37.86 ? 382 THR   B OG1 1 
ATOM   5908 C  CG2 . THR   B 1 397 ? -17.941 2.084   -32.272 1   37.53 ? 382 THR   B CG2 1 
ATOM   5909 N  N   . ASP   B 1 398 ? -17.741 -2.485  -31.665 1   31.7  ? 383 ASP   B N   1 
ATOM   5910 C  CA  . ASP   B 1 398 ? -17.499 -3.819  -31.082 1   30.31 ? 383 ASP   B CA  1 
ATOM   5911 C  C   . ASP   B 1 398 ? -17.472 -3.831  -29.566 1   26.99 ? 383 ASP   B C   1 
ATOM   5912 O  O   . ASP   B 1 398 ? -16.651 -3.139  -28.943 1   26.12 ? 383 ASP   B O   1 
ATOM   5913 C  CB  . ASP   B 1 398 ? -16.232 -4.461  -31.651 1   32.72 ? 383 ASP   B CB  1 
ATOM   5914 C  CG  . ASP   B 1 398 ? -16.301 -4.736  -33.148 1   38.79 ? 383 ASP   B CG  1 
ATOM   5915 O  OD1 . ASP   B 1 398 ? -17.367 -4.434  -33.771 1   39.69 ? 383 ASP   B OD1 1 
ATOM   5916 O  OD2 . ASP   B 1 398 ? -15.287 -5.232  -33.711 1   39.97 ? 383 ASP   B OD2 1 
ATOM   5917 N  N   . LEU   B 1 399 ? -18.416 -4.575  -28.97  1   24.57 ? 384 LEU   B N   1 
ATOM   5918 C  CA  . LEU   B 1 399 ? -18.53  -4.594  -27.522 1   22.98 ? 384 LEU   B CA  1 
ATOM   5919 C  C   . LEU   B 1 399 ? -17.381 -5.316  -26.838 1   22    ? 384 LEU   B C   1 
ATOM   5920 O  O   . LEU   B 1 399 ? -17.038 -4.912  -25.74  1   21.9  ? 384 LEU   B O   1 
ATOM   5921 C  CB  . LEU   B 1 399 ? -19.886 -5.136  -27.064 1   23.39 ? 384 LEU   B CB  1 
ATOM   5922 C  CG  . LEU   B 1 399 ? -20.266 -6.532  -27.494 1   25.43 ? 384 LEU   B CG  1 
ATOM   5923 C  CD1 . LEU   B 1 399 ? -19.926 -7.532  -26.41  1   26.79 ? 384 LEU   B CD1 1 
ATOM   5924 C  CD2 . LEU   B 1 399 ? -21.79  -6.625  -27.718 1   25.76 ? 384 LEU   B CD2 1 
ATOM   5925 N  N   . MET   B 1 400 ? -16.768 -6.364  -27.471 1   21.19 ? 385 MET   B N   1 
ATOM   5926 C  CA  . MET   B 1 400 ? -15.655 -7.069  -26.801 1   21.72 ? 385 MET   B CA  1 
ATOM   5927 C  C   . MET   B 1 400 ? -14.441 -6.149  -26.692 1   21.54 ? 385 MET   B C   1 
ATOM   5928 O  O   . MET   B 1 400 ? -13.75  -6.164  -25.674 1   21.04 ? 385 MET   B O   1 
ATOM   5929 C  CB  . MET   B 1 400 ? -15.241 -8.374  -27.539 1   22.52 ? 385 MET   B CB  1 
ATOM   5930 C  CG  . MET   B 1 400 ? -16.315 -9.411  -27.628 1   25.48 ? 385 MET   B CG  1 
ATOM   5931 S  SD  . MET   B 1 400 ? -16.883 -10.09  -26.056 1   30.45 ? 385 MET   B SD  1 
ATOM   5932 C  CE  . MET   B 1 400 ? -15.447 -10.94  -25.447 1   27.31 ? 385 MET   B CE  1 
ATOM   5933 N  N   . ASN   B 1 401 ? -14.196 -5.336  -27.735 1   22.79 ? 386 ASN   B N   1 
ATOM   5934 C  CA  . ASN   B 1 401 ? -13.103 -4.361  -27.794 1   24.3  ? 386 ASN   B CA  1 
ATOM   5935 C  C   . ASN   B 1 401 ? -13.324 -3.3    -26.744 1   23.22 ? 386 ASN   B C   1 
ATOM   5936 O  O   . ASN   B 1 401 ? -12.391 -2.963  -25.996 1   23.31 ? 386 ASN   B O   1 
ATOM   5937 C  CB  . ASN   B 1 401 ? -12.998 -3.74   -29.195 1   28.32 ? 386 ASN   B CB  1 
ATOM   5938 C  CG  . ASN   B 1 401 ? -12.367 -4.66   -30.219 1   38.45 ? 386 ASN   B CG  1 
ATOM   5939 O  OD1 . ASN   B 1 401 ? -11.898 -5.777  -29.909 1   42.39 ? 386 ASN   B OD1 1 
ATOM   5940 N  ND2 . ASN   B 1 401 ? -12.313 -4.201  -31.468 1   41.18 ? 386 ASN   B ND2 1 
ATOM   5941 N  N   . PHE   B 1 402 ? -14.575 -2.794  -26.623 1   22.06 ? 387 PHE   B N   1 
ATOM   5942 C  CA  . PHE   B 1 402 ? -14.921 -1.834  -25.563 1   20.93 ? 387 PHE   B CA  1 
ATOM   5943 C  C   . PHE   B 1 402 ? -14.591 -2.419  -24.181 1   19.78 ? 387 PHE   B C   1 
ATOM   5944 O  O   . PHE   B 1 402 ? -13.869 -1.794  -23.405 1   19.02 ? 387 PHE   B O   1 
ATOM   5945 C  CB  . PHE   B 1 402 ? -16.412 -1.422  -25.621 1   20.96 ? 387 PHE   B CB  1 
ATOM   5946 C  CG  . PHE   B 1 402 ? -16.922 -0.691  -24.395 1   22.01 ? 387 PHE   B CG  1 
ATOM   5947 C  CD1 . PHE   B 1 402 ? -16.551 0.622   -24.143 1   22.24 ? 387 PHE   B CD1 1 
ATOM   5948 C  CD2 . PHE   B 1 402 ? -17.726 -1.331  -23.464 1   22.69 ? 387 PHE   B CD2 1 
ATOM   5949 C  CE1 . PHE   B 1 402 ? -17.005 1.288   -22.999 1   21.85 ? 387 PHE   B CE1 1 
ATOM   5950 C  CE2 . PHE   B 1 402 ? -18.207 -0.647  -22.342 1   22.8  ? 387 PHE   B CE2 1 
ATOM   5951 C  CZ  . PHE   B 1 402 ? -17.832 0.66    -22.117 1   21.87 ? 387 PHE   B CZ  1 
ATOM   5952 N  N   . LEU   B 1 403 ? -15.118 -3.633  -23.883 1   18.42 ? 388 LEU   B N   1 
ATOM   5953 C  CA  . LEU   B 1 403 ? -14.894 -4.228  -22.57  1   18.76 ? 388 LEU   B CA  1 
ATOM   5954 C  C   . LEU   B 1 403 ? -13.412 -4.476  -22.25  1   18.76 ? 388 LEU   B C   1 
ATOM   5955 O  O   . LEU   B 1 403 ? -12.97  -4.239  -21.122 1   19.84 ? 388 LEU   B O   1 
ATOM   5956 C  CB  . LEU   B 1 403 ? -15.719 -5.525  -22.447 1   18.75 ? 388 LEU   B CB  1 
ATOM   5957 C  CG  . LEU   B 1 403 ? -17.232 -5.339  -22.455 1   19.68 ? 388 LEU   B CG  1 
ATOM   5958 C  CD1 . LEU   B 1 403 ? -17.951 -6.719  -22.503 1   18.97 ? 388 LEU   B CD1 1 
ATOM   5959 C  CD2 . LEU   B 1 403 ? -17.681 -4.505  -21.264 1   20.24 ? 388 LEU   B CD2 1 
ATOM   5960 N  N   . LYS   B 1 404 ? -12.645 -4.953  -23.238 1   18.66 ? 389 LYS   B N   1 
ATOM   5961 C  CA  . LYS   B 1 404 ? -11.213 -5.192  -23.064 1   19.46 ? 389 LYS   B CA  1 
ATOM   5962 C  C   . LYS   B 1 404 ? -10.44  -3.877  -22.873 1   20.27 ? 389 LYS   B C   1 
ATOM   5963 O  O   . LYS   B 1 404 ? -9.504  -3.841  -22.083 1   21.18 ? 389 LYS   B O   1 
ATOM   5964 C  CB  . LYS   B 1 404 ? -10.656 -6.013  -24.22  1   20.36 ? 389 LYS   B CB  1 
ATOM   5965 C  CG  . LYS   B 1 404 ? -11.255 -7.42   -24.11  1   24.19 ? 389 LYS   B CG  1 
ATOM   5966 C  CD  . LYS   B 1 404 ? -10.623 -8.424  -25.024 1   30.33 ? 389 LYS   B CD  1 
ATOM   5967 C  CE  . LYS   B 1 404 ? -11.144 -8.341  -26.42  1   32.22 ? 389 LYS   B CE  1 
ATOM   5968 N  NZ  . LYS   B 1 404 ? -10.885 -9.601  -27.175 1   31.24 ? 389 LYS   B NZ  1 
ATOM   5969 N  N   . THR   B 1 405 ? -10.864 -2.806  -23.529 1   19.58 ? 390 THR   B N   1 
ATOM   5970 C  CA  . THR   B 1 405 ? -10.265 -1.483  -23.331 1   20.44 ? 390 THR   B CA  1 
ATOM   5971 C  C   . THR   B 1 405 ? -10.482 -1.015  -21.901 1   20.66 ? 390 THR   B C   1 
ATOM   5972 O  O   . THR   B 1 405 ? -9.53   -0.6    -21.239 1   22.27 ? 390 THR   B O   1 
ATOM   5973 C  CB  . THR   B 1 405 ? -10.814 -0.476  -24.338 1   21.75 ? 390 THR   B CB  1 
ATOM   5974 O  OG1 . THR   B 1 405 ? -10.402 -0.893  -25.634 1   21.4  ? 390 THR   B OG1 1 
ATOM   5975 C  CG2 . THR   B 1 405 ? -10.292 0.956   -24.07  1   22.74 ? 390 THR   B CG2 1 
ATOM   5976 N  N   . VAL   B 1 406 ? -11.719 -1.142  -21.397 1   19.36 ? 391 VAL   B N   1 
ATOM   5977 C  CA  . VAL   B 1 406 ? -12.043 -0.745  -20.032 1   20.26 ? 391 VAL   B CA  1 
ATOM   5978 C  C   . VAL   B 1 406 ? -11.246 -1.597  -19.03  1   21.88 ? 391 VAL   B C   1 
ATOM   5979 O  O   . VAL   B 1 406 ? -10.693 -1.056  -18.063 1   23.71 ? 391 VAL   B O   1 
ATOM   5980 C  CB  . VAL   B 1 406 ? -13.581 -0.819  -19.787 1   20.97 ? 391 VAL   B CB  1 
ATOM   5981 C  CG1 . VAL   B 1 406 ? -13.93  -0.536  -18.333 1   22.02 ? 391 VAL   B CG1 1 
ATOM   5982 C  CG2 . VAL   B 1 406 ? -14.316 0.174   -20.696 1   20.55 ? 391 VAL   B CG2 1 
ATOM   5983 N  N   . ARG   B 1 407 ? -11.185 -2.918  -19.249 1   21.05 ? 392 ARG   B N   1 
ATOM   5984 C  CA  . ARG   B 1 407 ? -10.42  -3.781  -18.35  1   21.94 ? 392 ARG   B CA  1 
ATOM   5985 C  C   . ARG   B 1 407 ? -8.906  -3.435  -18.374 1   23.32 ? 392 ARG   B C   1 
ATOM   5986 O  O   . ARG   B 1 407 ? -8.251  -3.388  -17.323 1   23.37 ? 392 ARG   B O   1 
ATOM   5987 C  CB  . ARG   B 1 407 ? -10.654 -5.261  -18.682 1   23.46 ? 392 ARG   B CB  1 
ATOM   5988 C  CG  . ARG   B 1 407 ? -9.947  -6.118  -17.651 1   26.84 ? 392 ARG   B CG  1 
ATOM   5989 C  CD  . ARG   B 1 407 ? -9.761  -7.545  -18.024 1   29.63 ? 392 ARG   B CD  1 
ATOM   5990 N  NE  . ARG   B 1 407 ? -9.235  -7.833  -19.363 1   30.43 ? 392 ARG   B NE  1 
ATOM   5991 C  CZ  . ARG   B 1 407 ? -9.18   -9.069  -19.859 1   30.23 ? 392 ARG   B CZ  1 
ATOM   5992 N  NH1 . ARG   B 1 407 ? -9.567  -10.101 -19.126 1   29.32 ? 392 ARG   B NH1 1 
ATOM   5993 N  NH2 . ARG   B 1 407 ? -8.756  -9.276  -21.097 1   30.85 ? 392 ARG   B NH2 1 
ATOM   5994 N  N   . SER   B 1 408 ? -8.347  -3.201  -19.579 1   23.91 ? 393 SER   B N   1 
ATOM   5995 C  CA  . SER   B 1 408 ? -6.927  -2.872  -19.749 1   25.66 ? 393 SER   B CA  1 
ATOM   5996 C  C   . SER   B 1 408 ? -6.57   -1.55   -19.036 1   25.38 ? 393 SER   B C   1 
ATOM   5997 O  O   . SER   B 1 408 ? -5.553  -1.484  -18.34  1   25.45 ? 393 SER   B O   1 
ATOM   5998 C  CB  . SER   B 1 408 ? -6.578  -2.8    -21.233 1   28.37 ? 393 SER   B CB  1 
ATOM   5999 O  OG  . SER   B 1 408 ? -5.223  -2.446  -21.429 1   34.45 ? 393 SER   B OG  1 
ATOM   6000 N  N   . THR   B 1 409 ? -7.432  -0.526  -19.149 1   24.16 ? 394 THR   B N   1 
ATOM   6001 C  CA  . THR   B 1 409 ? -7.212  0.756   -18.469 1   23.76 ? 394 THR   B CA  1 
ATOM   6002 C  C   . THR   B 1 409 ? -7.199  0.553   -16.93  1   23.65 ? 394 THR   B C   1 
ATOM   6003 O  O   . THR   B 1 409 ? -6.397  1.177   -16.214 1   23.02 ? 394 THR   B O   1 
ATOM   6004 C  CB  . THR   B 1 409 ? -8.272  1.741   -18.933 1   24.51 ? 394 THR   B CB  1 
ATOM   6005 O  OG1 . THR   B 1 409 ? -8.132  1.868   -20.348 1   24.94 ? 394 THR   B OG1 1 
ATOM   6006 C  CG2 . THR   B 1 409 ? -8.175  3.103   -18.246 1   25.3  ? 394 THR   B CG2 1 
ATOM   6007 N  N   . THR   B 1 410 ? -8.061  -0.366  -16.429 1   22.65 ? 395 THR   B N   1 
ATOM   6008 C  CA  . THR   B 1 410 ? -8.077  -0.697  -15.011 1   23.05 ? 395 THR   B CA  1 
ATOM   6009 C  C   . THR   B 1 410 ? -6.777  -1.416  -14.61  1   24.96 ? 395 THR   B C   1 
ATOM   6010 O  O   . THR   B 1 410 ? -6.148  -1.016  -13.625 1   25.41 ? 395 THR   B O   1 
ATOM   6011 C  CB  . THR   B 1 410 ? -9.291  -1.605  -14.67  1   22.2  ? 395 THR   B CB  1 
ATOM   6012 O  OG1 . THR   B 1 410 ? -10.469 -1.077  -15.298 1   22.09 ? 395 THR   B OG1 1 
ATOM   6013 C  CG2 . THR   B 1 410 ? -9.474  -1.773  -13.179 1   21.48 ? 395 THR   B CG2 1 
ATOM   6014 N  N   . GLU   B 1 411 ? -6.368  -2.47   -15.353 1   25.93 ? 396 GLU   B N   1 
ATOM   6015 C  CA  . GLU   B 1 411 ? -5.127  -3.217  -15.037 1   28.06 ? 396 GLU   B CA  1 
ATOM   6016 C  C   . GLU   B 1 411 ? -3.901  -2.257  -15.039 1   28.49 ? 396 GLU   B C   1 
ATOM   6017 O  O   . GLU   B 1 411 ? -3.016  -2.368  -14.183 1   27.15 ? 396 GLU   B O   1 
ATOM   6018 C  CB  . GLU   B 1 411 ? -4.862  -4.322  -16.084 1   31.95 ? 396 GLU   B CB  1 
ATOM   6019 C  CG  . GLU   B 1 411 ? -5.743  -5.546  -15.988 1   40.33 ? 396 GLU   B CG  1 
ATOM   6020 C  CD  . GLU   B 1 411 ? -5.535  -6.559  -17.101 1   50.24 ? 396 GLU   B CD  1 
ATOM   6021 O  OE1 . GLU   B 1 411 ? -5.424  -6.139  -18.28  1   50.72 ? 396 GLU   B OE1 1 
ATOM   6022 O  OE2 . GLU   B 1 411 ? -5.5    -7.775  -16.794 1   53.59 ? 396 GLU   B OE2 1 
ATOM   6023 N  N   . LYS   B 1 412 ? -3.867  -1.315  -15.995 1   28.8  ? 397 LYS   B N   1 
ATOM   6024 C  CA  . LYS   B 1 412 ? -2.744  -0.368  -16.09  1   30.57 ? 397 LYS   B CA  1 
ATOM   6025 C  C   . LYS   B 1 412 ? -2.672  0.642   -14.931 1   31.23 ? 397 LYS   B C   1 
ATOM   6026 O  O   . LYS   B 1 412 ? -1.677  1.361   -14.799 1   31.86 ? 397 LYS   B O   1 
ATOM   6027 C  CB  . LYS   B 1 412 ? -2.75   0.353   -17.445 1   33.23 ? 397 LYS   B CB  1 
ATOM   6028 C  CG  . LYS   B 1 412 ? -2.294  -0.534  -18.585 1   39.55 ? 397 LYS   B CG  1 
ATOM   6029 C  CD  . LYS   B 1 412 ? -2.703  0.085   -19.919 1   46.91 ? 397 LYS   B CD  1 
ATOM   6030 C  CE  . LYS   B 1 412 ? -2.333  -0.769  -21.108 1   52.49 ? 397 LYS   B CE  1 
ATOM   6031 N  NZ  . LYS   B 1 412 ? -3.152  -0.412  -22.309 1   56.28 ? 397 LYS   B NZ  1 
ATOM   6032 N  N   . SER   B 1 413 ? -3.71   0.692   -14.08  1   30.2  ? 398 SER   B N   1 
ATOM   6033 C  CA  . SER   B 1 413 ? -3.703  1.563   -12.921 1   30.11 ? 398 SER   B CA  1 
ATOM   6034 C  C   . SER   B 1 413 ? -2.998  0.939   -11.71  1   29.96 ? 398 SER   B C   1 
ATOM   6035 O  O   . SER   B 1 413 ? -2.82   1.625   -10.699 1   30.12 ? 398 SER   B O   1 
ATOM   6036 C  CB  . SER   B 1 413 ? -5.116  1.983   -12.561 1   31.61 ? 398 SER   B CB  1 
ATOM   6037 O  OG  . SER   B 1 413 ? -5.619  2.671   -13.692 1   37.23 ? 398 SER   B OG  1 
ATOM   6038 N  N   . LEU   B 1 414 ? -2.6    -0.342  -11.786 1   29.82 ? 399 LEU   B N   1 
ATOM   6039 C  CA  . LEU   B 1 414 ? -1.9    -0.984  -10.687 1   31.11 ? 399 LEU   B CA  1 
ATOM   6040 C  C   . LEU   B 1 414 ? -0.552  -0.248  -10.437 1   33.67 ? 399 LEU   B C   1 
ATOM   6041 O  O   . LEU   B 1 414 ? 0.106   0.192   -11.38  1   33.08 ? 399 LEU   B O   1 
ATOM   6042 C  CB  . LEU   B 1 414 ? -1.646  -2.456  -10.994 1   30.65 ? 399 LEU   B CB  1 
ATOM   6043 C  CG  . LEU   B 1 414 ? -2.855  -3.39   -10.883 1   31.43 ? 399 LEU   B CG  1 
ATOM   6044 C  CD1 . LEU   B 1 414 ? -2.515  -4.761  -11.453 1   32.21 ? 399 LEU   B CD1 1 
ATOM   6045 C  CD2 . LEU   B 1 414 ? -3.361  -3.495  -9.438  1   30.79 ? 399 LEU   B CD2 1 
ATOM   6046 N  N   . LEU   B 1 415 ? -0.241  -0.008  -9.179  1   35.88 ? 400 LEU   B N   1 
ATOM   6047 C  CA  . LEU   B 1 415 ? 1.005   0.66    -8.808  1   38.8  ? 400 LEU   B CA  1 
ATOM   6048 C  C   . LEU   B 1 415 ? 2.191   -0.303  -8.891  1   42.77 ? 400 LEU   B C   1 
ATOM   6049 O  O   . LEU   B 1 415 ? 3.301   0.151   -9.165  1   43.84 ? 400 LEU   B O   1 
ATOM   6050 C  CB  . LEU   B 1 415 ? 0.901   1.296   -7.42   1   38.25 ? 400 LEU   B CB  1 
ATOM   6051 C  CG  . LEU   B 1 415 ? -0.269  2.256   -7.246  1   39.48 ? 400 LEU   B CG  1 
ATOM   6052 C  CD1 . LEU   B 1 415 ? -0.328  2.777   -5.845  1   40.25 ? 400 LEU   B CD1 1 
ATOM   6053 C  CD2 . LEU   B 1 415 ? -0.221  3.391   -8.244  1   40.2  ? 400 LEU   B CD2 1 
ATOM   6054 N  N   . LYS   B 1 416 ? 1.965   -1.628  -8.695  1   44.46 ? 401 LYS   B N   1 
ATOM   6055 C  CA  . LYS   B 1 416 ? 3.044   -2.612  -8.813  1   46.32 ? 401 LYS   B CA  1 
ATOM   6056 C  C   . LYS   B 1 416 ? 2.702   -3.717  -9.812  1   47.93 ? 401 LYS   B C   1 
ATOM   6057 O  O   . LYS   B 1 416 ? 3.163   -3.681  -10.956 1   49.05 ? 401 LYS   B O   1 
ATOM   6058 C  CB  . LYS   B 1 416 ? 3.386   -3.221  -7.456  1   48.42 ? 401 LYS   B CB  1 
HETATM 6059 C  CHA . HEM   C 2 .   ? -16.658 29.659  -31.887 1   15.73 ? 501 HEM   A CHA 1 
HETATM 6060 C  CHB . HEM   C 2 .   ? -14.238 31.761  -35.536 1   16.22 ? 501 HEM   A CHB 1 
HETATM 6061 C  CHC . HEM   C 2 .   ? -13.298 35.57   -32.714 1   16.73 ? 501 HEM   A CHC 1 
HETATM 6062 C  CHD . HEM   C 2 .   ? -15.395 33.324  -28.961 1   16.42 ? 501 HEM   A CHD 1 
HETATM 6063 C  C1A . HEM   C 2 .   ? -16.036 29.874  -33.143 1   16.59 ? 501 HEM   A C1A 1 
HETATM 6064 C  C2A . HEM   C 2 .   ? -16.068 28.927  -34.247 1   17.45 ? 501 HEM   A C2A 1 
HETATM 6065 C  C3A . HEM   C 2 .   ? -15.377 29.513  -35.286 1   18.03 ? 501 HEM   A C3A 1 
HETATM 6066 C  C4A . HEM   C 2 .   ? -14.93  30.816  -34.8   1   17.05 ? 501 HEM   A C4A 1 
HETATM 6067 C  CMA . HEM   C 2 .   ? -15.071 28.94   -36.64  1   18.98 ? 501 HEM   A CMA 1 
HETATM 6068 C  CAA . HEM   C 2 .   ? -16.724 27.572  -34.227 1   19.38 ? 501 HEM   A CAA 1 
HETATM 6069 C  CBA . HEM   C 2 .   ? -16.005 26.569  -33.308 1   20.49 ? 501 HEM   A CBA 1 
HETATM 6070 C  CGA . HEM   C 2 .   ? -14.803 25.903  -33.916 1   20.85 ? 501 HEM   A CGA 1 
HETATM 6071 O  O1A . HEM   C 2 .   ? -13.74  25.774  -33.333 1   21.04 ? 501 HEM   A O1A 1 
HETATM 6072 O  O2A . HEM   C 2 .   ? -15.019 25.405  -35.09  1   21.13 ? 501 HEM   A O2A 1 
HETATM 6073 C  C1B . HEM   C 2 .   ? -13.854 33.051  -35.12  1   15.99 ? 501 HEM   A C1B 1 
HETATM 6074 C  C2B . HEM   C 2 .   ? -13.193 34.017  -35.974 1   16.38 ? 501 HEM   A C2B 1 
HETATM 6075 C  C3B . HEM   C 2 .   ? -12.92  35.102  -35.152 1   17.17 ? 501 HEM   A C3B 1 
HETATM 6076 C  C4B . HEM   C 2 .   ? -13.442 34.796  -33.846 1   17.18 ? 501 HEM   A C4B 1 
HETATM 6077 C  CMB . HEM   C 2 .   ? -12.931 33.83   -37.438 1   15.42 ? 501 HEM   A CMB 1 
HETATM 6078 C  CAB . HEM   C 2 .   ? -12.209 36.347  -35.476 1   17.44 ? 501 HEM   A CAB 1 
HETATM 6079 C  CBB . HEM   C 2 .   ? -11.198 36.503  -36.368 1   17.76 ? 501 HEM   A CBB 1 
HETATM 6080 C  C1C . HEM   C 2 .   ? -13.717 35.272  -31.39  1   17.26 ? 501 HEM   A C1C 1 
HETATM 6081 C  C2C . HEM   C 2 .   ? -13.391 36.073  -30.219 1   17.53 ? 501 HEM   A C2C 1 
HETATM 6082 C  C3C . HEM   C 2 .   ? -13.987 35.422  -29.174 1   18.17 ? 501 HEM   A C3C 1 
HETATM 6083 C  C4C . HEM   C 2 .   ? -14.671 34.265  -29.693 1   16.77 ? 501 HEM   A C4C 1 
HETATM 6084 C  CMC . HEM   C 2 .   ? -12.563 37.321  -30.216 1   17.77 ? 501 HEM   A CMC 1 
HETATM 6085 C  CAC . HEM   C 2 .   ? -13.824 35.751  -27.754 1   18.67 ? 501 HEM   A CAC 1 
HETATM 6086 C  CBC . HEM   C 2 .   ? -13.4   34.959  -26.799 1   19.18 ? 501 HEM   A CBC 1 
HETATM 6087 C  C1D . HEM   C 2 .   ? -16.026 32.15   -29.464 1   15.74 ? 501 HEM   A C1D 1 
HETATM 6088 C  C2D . HEM   C 2 .   ? -16.823 31.24   -28.663 1   16.21 ? 501 HEM   A C2D 1 
HETATM 6089 C  C3D . HEM   C 2 .   ? -17.206 30.221  -29.501 1   17.12 ? 501 HEM   A C3D 1 
HETATM 6090 C  C4D . HEM   C 2 .   ? -16.601 30.503  -30.795 1   16.35 ? 501 HEM   A C4D 1 
HETATM 6091 C  CMD . HEM   C 2 .   ? -17.055 31.354  -27.188 1   16.74 ? 501 HEM   A CMD 1 
HETATM 6092 C  CAD . HEM   C 2 .   ? -18.053 29.026  -29.156 1   17.15 ? 501 HEM   A CAD 1 
HETATM 6093 C  CBD . HEM   C 2 .   ? -19.49  29.135  -29.699 1   17.79 ? 501 HEM   A CBD 1 
HETATM 6094 C  CGD . HEM   C 2 .   ? -20.36  30.151  -28.999 1   18.78 ? 501 HEM   A CGD 1 
HETATM 6095 O  O1D . HEM   C 2 .   ? -21.121 30.911  -29.596 1   18.03 ? 501 HEM   A O1D 1 
HETATM 6096 O  O2D . HEM   C 2 .   ? -20.273 30.121  -27.687 1   19.45 ? 501 HEM   A O2D 1 
HETATM 6097 N  NA  . HEM   C 2 .   ? -15.35  31.002  -33.494 1   16.74 ? 501 HEM   A NA  1 
HETATM 6098 N  NB  . HEM   C 2 .   ? -14.016 33.534  -33.868 1   16.61 ? 501 HEM   A NB  1 
HETATM 6099 N  NC  . HEM   C 2 .   ? -14.472 34.192  -31.051 1   17.06 ? 501 HEM   A NC  1 
HETATM 6100 N  ND  . HEM   C 2 .   ? -15.907 31.696  -30.74  1   15.91 ? 501 HEM   A ND  1 
HETATM 6101 FE FE  . HEM   C 2 .   ? -14.947 32.621  -32.297 1   17.25 ? 501 HEM   A FE  1 
HETATM 6102 N  N1  . A1H93 D 3 .   ? -11.227 28.545  -36.532 1   22.96 ? 502 A1H93 A N1  1 
HETATM 6103 N  N3  . A1H93 D 3 .   ? -11.179 29.864  -34.811 1   22.97 ? 502 A1H93 A N3  1 
HETATM 6104 C  C4  . A1H93 D 3 .   ? -12.202 27.25   -38.369 1   24.03 ? 502 A1H93 A C4  1 
HETATM 6105 C  C5  . A1H93 D 3 .   ? -11.349 28.245  -37.902 1   23.06 ? 502 A1H93 A C5  1 
HETATM 6106 C  C6  . A1H93 D 3 .   ? -11.113 28.58   -34.343 1   21.59 ? 502 A1H93 A C6  1 
HETATM 6107 C  C7  . A1H93 D 3 .   ? -11.095 28.313  -32.879 1   18.81 ? 502 A1H93 A C7  1 
HETATM 6108 C  C8  . A1H93 D 3 .   ? -10.559 29.44   -32.014 1   17.89 ? 502 A1H93 A C8  1 
HETATM 6109 C  C10 . A1H93 D 3 .   ? -8.408  28.366  -31.381 1   17.53 ? 502 A1H93 A C10 1 
HETATM 6110 C  C13 . A1H93 D 3 .   ? -9.846  31.56   -30.352 1   15.75 ? 502 A1H93 A C13 1 
HETATM 6111 C  C15 . A1H93 D 3 .   ? -12.157 32.405  -30.991 1   16.36 ? 502 A1H93 A C15 1 
HETATM 6112 C  C17 . A1H93 D 3 .   ? -11.179 27.729  -35.431 1   22.63 ? 502 A1H93 A C17 1 
HETATM 6113 C  C1  . A1H93 D 3 .   ? -12.636 26.749  -42.496 1   24.76 ? 502 A1H93 A C1  1 
HETATM 6114 O  O1  . A1H93 D 3 .   ? -11.811 27.81   -42.003 1   25.14 ? 502 A1H93 A O1  1 
HETATM 6115 C  C2  . A1H93 D 3 .   ? -11.671 27.84   -40.623 1   24.47 ? 502 A1H93 A C2  1 
HETATM 6116 C  C3  . A1H93 D 3 .   ? -12.347 27.026  -39.726 1   24.29 ? 502 A1H93 A C3  1 
HETATM 6117 N  N2  . A1H93 D 3 .   ? -11.244 29.83   -36.128 1   23.23 ? 502 A1H93 A N2  1 
HETATM 6118 C  C9  . A1H93 D 3 .   ? -9.401  29.474  -31.309 1   16.82 ? 502 A1H93 A C9  1 
HETATM 6119 C  C11 . A1H93 D 3 .   ? -6.91   28.537  -31.261 1   17.39 ? 502 A1H93 A C11 1 
HETATM 6120 C  C12 . A1H93 D 3 .   ? -7.661  27.878  -30.147 1   17.67 ? 502 A1H93 A C12 1 
HETATM 6121 N  N4  . A1H93 D 3 .   ? -9.044  30.547  -30.473 1   15.32 ? 502 A1H93 A N4  1 
HETATM 6122 C  C14 . A1H93 D 3 .   ? -11.096 31.532  -30.993 1   16.58 ? 502 A1H93 A C14 1 
HETATM 6123 N  N5  . A1H93 D 3 .   ? -13.16  31.865  -31.752 1   18.03 ? 502 A1H93 A N5  1 
HETATM 6124 C  C16 . A1H93 D 3 .   ? -12.688 30.744  -32.283 1   17.18 ? 502 A1H93 A C16 1 
HETATM 6125 N  N6  . A1H93 D 3 .   ? -11.443 30.474  -31.785 1   17.57 ? 502 A1H93 A N6  1 
HETATM 6126 O  O2  . A1H93 D 3 .   ? -12.412 27.934  -32.474 1   18.64 ? 502 A1H93 A O2  1 
HETATM 6127 C  C18 . A1H93 D 3 .   ? -10.7   29.063  -38.799 1   23.54 ? 502 A1H93 A C18 1 
HETATM 6128 F  F1  . A1H93 D 3 .   ? -12.786 26.378  -37.529 1   24.06 ? 502 A1H93 A F1  1 
HETATM 6129 C  C19 . A1H93 D 3 .   ? -10.889 28.877  -40.157 1   24.36 ? 502 A1H93 A C19 1 
HETATM 6130 F  F2  . A1H93 D 3 .   ? -10.339 29.745  -41.036 1   24.04 ? 502 A1H93 A F2  1 
HETATM 6131 S  S   . DMS   E 4 .   ? -19.346 33.85   -29.28  1   47.34 ? 503 DMS   A S   1 
HETATM 6132 O  O   . DMS   E 4 .   ? -20.322 33.496  -30.365 1   45.28 ? 503 DMS   A O   1 
HETATM 6133 C  C1  . DMS   E 4 .   ? -20.089 33.476  -27.666 1   47.46 ? 503 DMS   A C1  1 
HETATM 6134 C  C2  . DMS   E 4 .   ? -19.339 35.617  -28.878 1   46.43 ? 503 DMS   A C2  1 
HETATM 6135 C  CHA . HEM   F 2 .   ? -21.04  -3.531  -19.928 1   18.91 ? 501 HEM   B CHA 1 
HETATM 6136 C  CHB . HEM   F 2 .   ? -23.202 -7.598  -21.498 1   20.44 ? 501 HEM   B CHB 1 
HETATM 6137 C  CHC . HEM   F 2 .   ? -24.014 -8.946  -16.934 1   20.33 ? 501 HEM   B CHC 1 
HETATM 6138 C  CHD . HEM   F 2 .   ? -22.213 -4.701  -15.378 1   20.18 ? 501 HEM   B CHD 1 
HETATM 6139 C  C1A . HEM   F 2 .   ? -21.615 -4.515  -20.78  1   19.92 ? 501 HEM   B C1A 1 
HETATM 6140 C  C2A . HEM   F 2 .   ? -21.623 -4.433  -22.23  1   20.57 ? 501 HEM   B C2A 1 
HETATM 6141 C  C3A . HEM   F 2 .   ? -22.245 -5.58   -22.686 1   21.3  ? 501 HEM   B C3A 1 
HETATM 6142 C  C4A . HEM   F 2 .   ? -22.595 -6.354  -21.505 1   20.96 ? 501 HEM   B C4A 1 
HETATM 6143 C  CMA . HEM   F 2 .   ? -22.594 -5.944  -24.097 1   21.58 ? 501 HEM   B CMA 1 
HETATM 6144 C  CAA . HEM   F 2 .   ? -21.045 -3.311  -23.053 1   20.8  ? 501 HEM   B CAA 1 
HETATM 6145 C  CBA . HEM   F 2 .   ? -21.84  -1.991  -22.92  1   20.22 ? 501 HEM   B CBA 1 
HETATM 6146 C  CGA . HEM   F 2 .   ? -23.061 -1.901  -23.796 1   20.8  ? 501 HEM   B CGA 1 
HETATM 6147 O  O1A . HEM   F 2 .   ? -24.147 -1.505  -23.402 1   20.75 ? 501 HEM   B O1A 1 
HETATM 6148 O  O2A . HEM   F 2 .   ? -22.851 -2.253  -25.03  1   20.93 ? 501 HEM   B O2A 1 
HETATM 6149 C  C1B . HEM   F 2 .   ? -23.499 -8.404  -20.378 1   20.29 ? 501 HEM   B C1B 1 
HETATM 6150 C  C2B . HEM   F 2 .   ? -24.069 -9.744  -20.46  1   20.87 ? 501 HEM   B C2B 1 
HETATM 6151 C  C3B . HEM   F 2 .   ? -24.294 -10.12  -19.149 1   21.67 ? 501 HEM   B C3B 1 
HETATM 6152 C  C4B . HEM   F 2 .   ? -23.852 -9.034  -18.303 1   20.92 ? 501 HEM   B C4B 1 
HETATM 6153 C  CMB . HEM   F 2 .   ? -24.317 -10.498 -21.73  1   20.72 ? 501 HEM   B CMB 1 
HETATM 6154 C  CAB . HEM   F 2 .   ? -24.934 -11.356 -18.67  1   22.08 ? 501 HEM   B CAB 1 
HETATM 6155 C  CBB . HEM   F 2 .   ? -25.914 -12.057 -19.289 1   21.92 ? 501 HEM   B CBB 1 
HETATM 6156 C  C1C . HEM   F 2 .   ? -23.626 -7.872  -16.083 1   20.76 ? 501 HEM   B C1C 1 
HETATM 6157 C  C2C . HEM   F 2 .   ? -23.946 -7.789  -14.666 1   20.97 ? 501 HEM   B C2C 1 
HETATM 6158 C  C3C . HEM   F 2 .   ? -23.458 -6.573  -14.253 1   21.42 ? 501 HEM   B C3C 1 
HETATM 6159 C  C4C . HEM   F 2 .   ? -22.836 -5.942  -15.382 1   20.71 ? 501 HEM   B C4C 1 
HETATM 6160 C  CMC . HEM   F 2 .   ? -24.685 -8.832  -13.878 1   21.02 ? 501 HEM   B CMC 1 
HETATM 6161 C  CAC . HEM   F 2 .   ? -23.625 -5.967  -12.928 1   21.78 ? 501 HEM   B CAC 1 
HETATM 6162 C  CBC . HEM   F 2 .   ? -24.114 -4.761  -12.649 1   22.22 ? 501 HEM   B CBC 1 
HETATM 6163 C  C1D . HEM   F 2 .   ? -21.629 -4.046  -16.497 1   19.39 ? 501 HEM   B C1D 1 
HETATM 6164 C  C2D . HEM   F 2 .   ? -20.935 -2.777  -16.419 1   19.72 ? 501 HEM   B C2D 1 
HETATM 6165 C  C3D . HEM   F 2 .   ? -20.564 -2.461  -17.705 1   19.33 ? 501 HEM   B C3D 1 
HETATM 6166 C  C4D . HEM   F 2 .   ? -21.079 -3.526  -18.554 1   19.17 ? 501 HEM   B C4D 1 
HETATM 6167 C  CMD . HEM   F 2 .   ? -20.763 -1.963  -15.174 1   21.58 ? 501 HEM   B CMD 1 
HETATM 6168 C  CAD . HEM   F 2 .   ? -19.76  -1.266  -18.148 1   19.03 ? 501 HEM   B CAD 1 
HETATM 6169 C  CBD . HEM   F 2 .   ? -18.317 -1.613  -18.521 1   19.5  ? 501 HEM   B CBD 1 
HETATM 6170 C  CGD . HEM   F 2 .   ? -17.405 -1.905  -17.353 1   20.59 ? 501 HEM   B CGD 1 
HETATM 6171 O  O1D . HEM   F 2 .   ? -16.574 -2.798  -17.371 1   21.35 ? 501 HEM   B O1D 1 
HETATM 6172 O  O2D . HEM   F 2 .   ? -17.53  -1.086  -16.339 1   20.04 ? 501 HEM   B O2D 1 
HETATM 6173 N  NA  . HEM   F 2 .   ? -22.191 -5.678  -20.361 1   19.99 ? 501 HEM   B NA  1 
HETATM 6174 N  NB  . HEM   F 2 .   ? -23.347 -8.019  -19.095 1   20.19 ? 501 HEM   B NB  1 
HETATM 6175 N  NC  . HEM   F 2 .   ? -22.958 -6.752  -16.5   1   19.78 ? 501 HEM   B NC  1 
HETATM 6176 N  ND  . HEM   F 2 .   ? -21.692 -4.49   -17.776 1   18.78 ? 501 HEM   B ND  1 
HETATM 6177 FE FE  . HEM   F 2 .   ? -22.564 -6.235  -18.438 1   19.72 ? 501 HEM   B FE  1 
HETATM 6178 N  N1  . A1H93 G 3 .   ? -26.429 -5.812  -24.199 1   21.91 ? 502 A1H93 B N1  1 
HETATM 6179 N  N3  . A1H93 G 3 .   ? -26.377 -5.822  -22.036 1   22.36 ? 502 A1H93 B N3  1 
HETATM 6180 C  C4  . A1H93 G 3 .   ? -25.543 -5.807  -26.468 1   22.62 ? 502 A1H93 B C4  1 
HETATM 6181 C  C5  . A1H93 G 3 .   ? -26.304 -6.398  -25.473 1   21.87 ? 502 A1H93 B C5  1 
HETATM 6182 C  C6  . A1H93 G 3 .   ? -26.579 -4.528  -22.452 1   21.41 ? 502 A1H93 B C6  1 
HETATM 6183 C  C7  . A1H93 G 3 .   ? -26.65  -3.415  -21.464 1   19.95 ? 502 A1H93 B C7  1 
HETATM 6184 C  C8  . A1H93 G 3 .   ? -27.121 -3.82   -20.084 1   19.86 ? 502 A1H93 B C8  1 
HETATM 6185 C  C10 . A1H93 G 3 .   ? -29.344 -2.713  -20.196 1   19.97 ? 502 A1H93 B C10 1 
HETATM 6186 C  C13 . A1H93 G 3 .   ? -27.781 -4.564  -17.501 1   19.4  ? 502 A1H93 B C13 1 
HETATM 6187 C  C15 . A1H93 G 3 .   ? -25.39  -5.475  -17.502 1   20    ? 502 A1H93 B C15 1 
HETATM 6188 C  C17 . A1H93 G 3 .   ? -26.556 -4.502  -23.831 1   21.09 ? 502 A1H93 B C17 1 
HETATM 6189 C  C1  . A1H93 G 3 .   ? -25.1   -7.83   -30.076 1   23.85 ? 502 A1H93 B C1  1 
HETATM 6190 O  O1  . A1H93 G 3 .   ? -25.72  -8.507  -28.981 1   23.87 ? 502 A1H93 B O1  1 
HETATM 6191 C  C2  . A1H93 G 3 .   ? -25.899 -7.704  -27.866 1   23.26 ? 502 A1H93 B C2  1 
HETATM 6192 C  C3  . A1H93 G 3 .   ? -25.36  -6.442  -27.68  1   22.99 ? 502 A1H93 B C3  1 
HETATM 6193 N  N2  . A1H93 G 3 .   ? -26.285 -6.595  -23.108 1   22.42 ? 502 A1H93 B N2  1 
HETATM 6194 C  C9  . A1H93 G 3 .   ? -28.305 -3.499  -19.501 1   19.63 ? 502 A1H93 B C9  1 
HETATM 6195 C  C11 . A1H93 G 3 .   ? -30.84  -2.879  -20.036 1   19.75 ? 502 A1H93 B C11 1 
HETATM 6196 C  C12 . A1H93 G 3 .   ? -30.178 -1.615  -19.553 1   19.36 ? 502 A1H93 B C12 1 
HETATM 6197 N  N4  . A1H93 G 3 .   ? -28.637 -3.906  -18.214 1   19.15 ? 502 A1H93 B N4  1 
HETATM 6198 C  C14 . A1H93 G 3 .   ? -26.496 -4.843  -18.028 1   19.87 ? 502 A1H93 B C14 1 
HETATM 6199 N  N5  . A1H93 G 3 .   ? -24.391 -5.452  -18.452 1   21.03 ? 502 A1H93 B N5  1 
HETATM 6200 C  C16 . A1H93 G 3 .   ? -24.918 -4.892  -19.523 1   19.82 ? 502 A1H93 B C16 1 
HETATM 6201 N  N6  . A1H93 G 3 .   ? -26.191 -4.463  -19.293 1   19.52 ? 502 A1H93 B N6  1 
HETATM 6202 O  O2  . A1H93 G 3 .   ? -25.365 -2.781  -21.4   1   19.23 ? 502 A1H93 B O2  1 
HETATM 6203 C  C18 . A1H93 G 3 .   ? -26.809 -7.673  -25.643 1   22.41 ? 502 A1H93 B C18 1 
HETATM 6204 F  F1  . A1H93 G 3 .   ? -25.014 -4.573  -26.331 1   22.52 ? 502 A1H93 B F1  1 
HETATM 6205 C  C19 . A1H93 G 3 .   ? -26.599 -8.311  -26.847 1   23.03 ? 502 A1H93 B C19 1 
HETATM 6206 F  F2  . A1H93 G 3 .   ? -27.032 -9.567  -27.033 1   23.07 ? 502 A1H93 B F2  1 
HETATM 6207 S  S   . DMS   H 4 .   ? -19.861 -0.679  -26.288 1   53.29 ? 503 DMS   B S   1 
HETATM 6208 O  O   . DMS   H 4 .   ? -20.444 -2.004  -26.568 1   53.05 ? 503 DMS   B O   1 
HETATM 6209 C  C1  . DMS   H 4 .   ? -21.174 0.318   -25.777 1   53.54 ? 503 DMS   B C1  1 
HETATM 6210 C  C2  . DMS   H 4 .   ? -19.656 0.267   -27.809 1   52.62 ? 503 DMS   B C2  1 
HETATM 6211 S  S   . DMS   I 4 .   ? -18.222 -4.961  -15.13  1   50.8  ? 504 DMS   B S   1 
HETATM 6212 O  O   . DMS   I 4 .   ? -17.409 -5.359  -16.371 1   49.67 ? 504 DMS   B O   1 
HETATM 6213 C  C1  . DMS   I 4 .   ? -17.312 -3.71   -14.2   1   50.55 ? 504 DMS   B C1  1 
HETATM 6214 C  C2  . DMS   I 4 .   ? -18.01  -6.17   -13.811 1   50.58 ? 504 DMS   B C2  1 
HETATM 6215 O  O   . HOH   J 5 .   ? -5.423  33.354  -9.023  1   37.99 ? 601 HOH   A O   1 
HETATM 6216 O  O   . HOH   J 5 .   ? 7.33    31.188  -32.82  1   26.43 ? 602 HOH   A O   1 
HETATM 6217 O  O   . HOH   J 5 .   ? -15.159 17.149  -13.522 1   33.64 ? 603 HOH   A O   1 
HETATM 6218 O  O   . HOH   J 5 .   ? 3.56    36.374  -18.815 1   29.41 ? 604 HOH   A O   1 
HETATM 6219 O  O   . HOH   J 5 .   ? 9.201   34.372  -41.832 1   30.76 ? 605 HOH   A O   1 
HETATM 6220 O  O   . HOH   J 5 .   ? -21.805 27.067  -24.307 1   28.03 ? 606 HOH   A O   1 
HETATM 6221 O  O   . HOH   J 5 .   ? -8.595  15.755  -20.958 1   32.9  ? 607 HOH   A O   1 
HETATM 6222 O  O   . HOH   J 5 .   ? 13.768  35.581  -35.873 1   29.09 ? 608 HOH   A O   1 
HETATM 6223 O  O   . HOH   J 5 .   ? -8.51   12.769  -38.5   1   30.23 ? 609 HOH   A O   1 
HETATM 6224 O  O   . HOH   J 5 .   ? -37.724 31.069  -23.255 1   32.89 ? 610 HOH   A O   1 
HETATM 6225 O  O   . HOH   J 5 .   ? -26.432 45.542  -10.6   1   33.88 ? 611 HOH   A O   1 
HETATM 6226 O  O   . HOH   J 5 .   ? 6.979   17.873  -14.692 1   35.84 ? 612 HOH   A O   1 
HETATM 6227 O  O   . HOH   J 5 .   ? 20.847  15.421  -32.9   1   48.03 ? 613 HOH   A O   1 
HETATM 6228 O  O   . HOH   J 5 .   ? 13.355  20.428  -42.502 1   25.63 ? 614 HOH   A O   1 
HETATM 6229 O  O   . HOH   J 5 .   ? -34.443 26.862  -9.145  1   40.78 ? 615 HOH   A O   1 
HETATM 6230 O  O   . HOH   J 5 .   ? 10.021  12.657  -18.945 1   26.48 ? 616 HOH   A O   1 
HETATM 6231 O  O   . HOH   J 5 .   ? -29.04  28.568  -4.631  1   29.77 ? 617 HOH   A O   1 
HETATM 6232 O  O   . HOH   J 5 .   ? -17.02  26.489  -4.358  1   36.63 ? 618 HOH   A O   1 
HETATM 6233 O  O   . HOH   J 5 .   ? -16.488 43.128  -18.209 1   32.54 ? 619 HOH   A O   1 
HETATM 6234 O  O   . HOH   J 5 .   ? -11.553 13.823  -28.292 1   31.63 ? 620 HOH   A O   1 
HETATM 6235 O  O   . HOH   J 5 .   ? -6.881  30.95   -13.488 1   25.45 ? 621 HOH   A O   1 
HETATM 6236 O  O   . HOH   J 5 .   ? -39.625 46.474  -14.834 1   48.56 ? 622 HOH   A O   1 
HETATM 6237 O  O   . HOH   J 5 .   ? -22.181 46.232  -25.46  1   40.3  ? 623 HOH   A O   1 
HETATM 6238 O  O   . HOH   J 5 .   ? -6.825  25.576  -33.019 1   34.65 ? 624 HOH   A O   1 
HETATM 6239 O  O   . HOH   J 5 .   ? -11.882 47.696  -34.486 1   45.38 ? 625 HOH   A O   1 
HETATM 6240 O  O   . HOH   J 5 .   ? 18.008  22.111  -24.362 1   24.49 ? 626 HOH   A O   1 
HETATM 6241 O  O   . HOH   J 5 .   ? 14.87   27.35   -21.931 1   40.2  ? 627 HOH   A O   1 
HETATM 6242 O  O   . HOH   J 5 .   ? -0.27   21.852  -26.125 1   17.52 ? 628 HOH   A O   1 
HETATM 6243 O  O   . HOH   J 5 .   ? -0.682  25.789  -21.416 1   15.37 ? 629 HOH   A O   1 
HETATM 6244 O  O   . HOH   J 5 .   ? 10.944  33.351  -36.495 1   22.6  ? 630 HOH   A O   1 
HETATM 6245 O  O   . HOH   J 5 .   ? -18.469 12.768  -29.913 1   30.7  ? 631 HOH   A O   1 
HETATM 6246 O  O   . HOH   J 5 .   ? 0.462   20.846  -44.756 1   35.56 ? 632 HOH   A O   1 
HETATM 6247 O  O   . HOH   J 5 .   ? -10.072 44.697  -40.416 1   30.73 ? 633 HOH   A O   1 
HETATM 6248 O  O   . HOH   J 5 .   ? 12.27   9.536   -34.025 1   36.24 ? 634 HOH   A O   1 
HETATM 6249 O  O   . HOH   J 5 .   ? -29.05  18.818  -28.839 1   40.39 ? 635 HOH   A O   1 
HETATM 6250 O  O   . HOH   J 5 .   ? 12.894  16.573  -26.296 1   22.98 ? 636 HOH   A O   1 
HETATM 6251 O  O   . HOH   J 5 .   ? -25.27  38.255  -37.043 1   29.22 ? 637 HOH   A O   1 
HETATM 6252 O  O   . HOH   J 5 .   ? 2.763   36.867  -36.514 1   33.61 ? 638 HOH   A O   1 
HETATM 6253 O  O   . HOH   J 5 .   ? -32.877 41.154  -1.133  1   29.58 ? 639 HOH   A O   1 
HETATM 6254 O  O   . HOH   J 5 .   ? 18.821  18.513  -28.523 1   44.04 ? 640 HOH   A O   1 
HETATM 6255 O  O   . HOH   J 5 .   ? 8.154   34.031  -29.777 1   31.02 ? 641 HOH   A O   1 
HETATM 6256 O  O   . HOH   J 5 .   ? 3.297   49.261  -21.98  1   35.02 ? 642 HOH   A O   1 
HETATM 6257 O  O   . HOH   J 5 .   ? -39.994 37.56   -6.944  1   32.54 ? 643 HOH   A O   1 
HETATM 6258 O  O   . HOH   J 5 .   ? 0.474   6.887   -31.531 1   21.55 ? 644 HOH   A O   1 
HETATM 6259 O  O   . HOH   J 5 .   ? -23.117 41.519  -25.097 1   26.02 ? 645 HOH   A O   1 
HETATM 6260 O  O   . HOH   J 5 .   ? -28.225 42.977  -22.452 1   25.85 ? 646 HOH   A O   1 
HETATM 6261 O  O   . HOH   J 5 .   ? -3.55   44.879  -14.134 1   44.82 ? 647 HOH   A O   1 
HETATM 6262 O  O   . HOH   J 5 .   ? -7.02   47.636  -29.598 1   22.59 ? 648 HOH   A O   1 
HETATM 6263 O  O   . HOH   J 5 .   ? -10.605 42.788  -21.137 1   26.49 ? 649 HOH   A O   1 
HETATM 6264 O  O   . HOH   J 5 .   ? 8.007   12.191  -38.751 1   32.63 ? 650 HOH   A O   1 
HETATM 6265 O  O   . HOH   J 5 .   ? -21.887 40.385  -5.975  1   42.68 ? 651 HOH   A O   1 
HETATM 6266 O  O   . HOH   J 5 .   ? -13.687 39.636  -45.715 1   26.8  ? 652 HOH   A O   1 
HETATM 6267 O  O   . HOH   J 5 .   ? 9.051   4.922   -25.757 1   28.21 ? 653 HOH   A O   1 
HETATM 6268 O  O   . HOH   J 5 .   ? -6.088  28.493  -17.821 1   22.69 ? 654 HOH   A O   1 
HETATM 6269 O  O   . HOH   J 5 .   ? 4.667   36.787  -31.569 1   29.29 ? 655 HOH   A O   1 
HETATM 6270 O  O   . HOH   J 5 .   ? -28.511 45.343  -18.806 1   50.36 ? 656 HOH   A O   1 
HETATM 6271 O  O   . HOH   J 5 .   ? -32.895 25.303  -18.457 1   34.13 ? 657 HOH   A O   1 
HETATM 6272 O  O   . HOH   J 5 .   ? -14.815 37.726  -11.442 1   33.63 ? 658 HOH   A O   1 
HETATM 6273 O  O   . HOH   J 5 .   ? -18.59  42.571  -11.595 1   40.49 ? 659 HOH   A O   1 
HETATM 6274 O  O   . HOH   J 5 .   ? -8.99   48.848  -38.638 1   30.58 ? 660 HOH   A O   1 
HETATM 6275 O  O   . HOH   J 5 .   ? -7.359  46.898  -25.344 1   29.09 ? 661 HOH   A O   1 
HETATM 6276 O  O   . HOH   J 5 .   ? -34.459 42.868  -20.248 1   30.57 ? 662 HOH   A O   1 
HETATM 6277 O  O   . HOH   J 5 .   ? -34.847 44.603  -13.915 1   35.09 ? 663 HOH   A O   1 
HETATM 6278 O  O   . HOH   J 5 .   ? -2.601  14.096  -46.225 1   40.84 ? 664 HOH   A O   1 
HETATM 6279 O  O   . HOH   J 5 .   ? -32.487 32.505  -33.389 1   41.73 ? 665 HOH   A O   1 
HETATM 6280 O  O   . HOH   J 5 .   ? -27.281 45.79   -16.549 1   28.66 ? 666 HOH   A O   1 
HETATM 6281 O  O   . HOH   J 5 .   ? 3.007   29.598  -17.836 1   21.75 ? 667 HOH   A O   1 
HETATM 6282 O  O   . HOH   J 5 .   ? -10.117 26.038  -21.616 1   16.39 ? 668 HOH   A O   1 
HETATM 6283 O  O   . HOH   J 5 .   ? -23.306 35.247  -43.222 1   38.67 ? 669 HOH   A O   1 
HETATM 6284 O  O   . HOH   J 5 .   ? -17.137 28.253  -24.945 1   17.23 ? 670 HOH   A O   1 
HETATM 6285 O  O   . HOH   J 5 .   ? 0.429   45.514  -28.166 1   25.91 ? 671 HOH   A O   1 
HETATM 6286 O  O   . HOH   J 5 .   ? -23.136 17.839  -12.433 1   36.9  ? 672 HOH   A O   1 
HETATM 6287 O  O   . HOH   J 5 .   ? -17.944 30.75   -48.019 1   29.97 ? 673 HOH   A O   1 
HETATM 6288 O  O   . HOH   J 5 .   ? 12.146  34.047  -42.446 1   34.38 ? 674 HOH   A O   1 
HETATM 6289 O  O   . HOH   J 5 .   ? -8.608  24.608  -23.48  1   14.54 ? 675 HOH   A O   1 
HETATM 6290 O  O   . HOH   J 5 .   ? -27.112 24.307  -28.828 1   47.43 ? 676 HOH   A O   1 
HETATM 6291 O  O   . HOH   J 5 .   ? -29.247 31.771  -34.984 1   27.58 ? 677 HOH   A O   1 
HETATM 6292 O  O   . HOH   J 5 .   ? -11.371 20.767  -8.736  1   56.21 ? 678 HOH   A O   1 
HETATM 6293 O  O   . HOH   J 5 .   ? -25.966 47.523  -17.991 1   39.28 ? 679 HOH   A O   1 
HETATM 6294 O  O   . HOH   J 5 .   ? -25.381 24.641  -21.45  1   41.42 ? 680 HOH   A O   1 
HETATM 6295 O  O   . HOH   J 5 .   ? 16.319  14.7    -40.196 1   35.3  ? 681 HOH   A O   1 
HETATM 6296 O  O   . HOH   J 5 .   ? -29.695 21.386  -10.631 1   46.53 ? 682 HOH   A O   1 
HETATM 6297 O  O   . HOH   J 5 .   ? 8.166   39.910  -44.352 1   29.33 ? 683 HOH   A O   1 
HETATM 6298 O  O   . HOH   J 5 .   ? -10.744 29.669  -7.91   1   28.71 ? 684 HOH   A O   1 
HETATM 6299 O  O   . HOH   J 5 .   ? -11.722 29.498  -20.576 1   18.44 ? 685 HOH   A O   1 
HETATM 6300 O  O   . HOH   J 5 .   ? -13.979 14.916  -25.286 1   43.58 ? 686 HOH   A O   1 
HETATM 6301 O  O   . HOH   J 5 .   ? -4.732  48.631  -37.033 1   37.82 ? 687 HOH   A O   1 
HETATM 6302 O  O   . HOH   J 5 .   ? -12.038 33.786  -18.109 1   23.43 ? 688 HOH   A O   1 
HETATM 6303 O  O   . HOH   J 5 .   ? 19.353  19.834  -21.88  1   32.44 ? 689 HOH   A O   1 
HETATM 6304 O  O   . HOH   J 5 .   ? -21.718 33.235  -33.306 1   17.28 ? 690 HOH   A O   1 
HETATM 6305 O  O   . HOH   J 5 .   ? -7.76   21.725  -8.17   1   34.74 ? 691 HOH   A O   1 
HETATM 6306 O  O   . HOH   J 5 .   ? 2.961   30.243  -20.531 1   18.93 ? 692 HOH   A O   1 
HETATM 6307 O  O   . HOH   J 5 .   ? 0.261   34.658  -10.632 1   43.81 ? 693 HOH   A O   1 
HETATM 6308 O  O   . HOH   J 5 .   ? -3.951  20.886  -15.661 1   28.14 ? 694 HOH   A O   1 
HETATM 6309 O  O   . HOH   J 5 .   ? 12.196  26.227  -48.285 1   41.11 ? 695 HOH   A O   1 
HETATM 6310 O  O   . HOH   J 5 .   ? -36.754 40.451  -23.012 1   42.89 ? 696 HOH   A O   1 
HETATM 6311 O  O   . HOH   J 5 .   ? -10.61  27.231  -19.179 1   20.95 ? 697 HOH   A O   1 
HETATM 6312 O  O   . HOH   J 5 .   ? -4.916  22.772  -32.066 1   27.12 ? 698 HOH   A O   1 
HETATM 6313 O  O   . HOH   J 5 .   ? -19.764 28.088  -25.861 1   20.94 ? 699 HOH   A O   1 
HETATM 6314 O  O   . HOH   J 5 .   ? -0.823  8.882   -38.435 1   27.91 ? 700 HOH   A O   1 
HETATM 6315 O  O   . HOH   J 5 .   ? -22.856 31.301  -31.741 1   19.07 ? 701 HOH   A O   1 
HETATM 6316 O  O   . HOH   J 5 .   ? -26.74  26.696  -4.372  1   37.16 ? 702 HOH   A O   1 
HETATM 6317 O  O   . HOH   J 5 .   ? 3.191   11.757  -16.951 1   28.37 ? 703 HOH   A O   1 
HETATM 6318 O  O   . HOH   J 5 .   ? 8.317   34.319  -26.322 1   38.53 ? 704 HOH   A O   1 
HETATM 6319 O  O   . HOH   J 5 .   ? -24.87  42.204  -31.819 1   29.91 ? 705 HOH   A O   1 
HETATM 6320 O  O   . HOH   J 5 .   ? 8.706   23.96   -43.206 1   28.91 ? 706 HOH   A O   1 
HETATM 6321 O  O   . HOH   J 5 .   ? 3.88    39.172  -37.935 1   37.79 ? 707 HOH   A O   1 
HETATM 6322 O  O   . HOH   J 5 .   ? -3.98   22.488  -41.609 1   26.33 ? 708 HOH   A O   1 
HETATM 6323 O  O   . HOH   J 5 .   ? -26.351 41.745  -5.851  1   32.36 ? 709 HOH   A O   1 
HETATM 6324 O  O   . HOH   J 5 .   ? -1.156  40.343  -41.831 1   36.67 ? 710 HOH   A O   1 
HETATM 6325 O  O   . HOH   J 5 .   ? -6.553  29.355  -7.333  1   48.52 ? 711 HOH   A O   1 
HETATM 6326 O  O   . HOH   J 5 .   ? 18.349  12.384  -24.083 1   55.72 ? 712 HOH   A O   1 
HETATM 6327 O  O   . HOH   J 5 .   ? 4.149   33.286  -11.089 1   48.68 ? 713 HOH   A O   1 
HETATM 6328 O  O   . HOH   J 5 .   ? -20.498 17.25   -32.741 1   41.35 ? 714 HOH   A O   1 
HETATM 6329 O  O   . HOH   J 5 .   ? -21.461 18.236  -8.079  1   42.36 ? 715 HOH   A O   1 
HETATM 6330 O  O   . HOH   J 5 .   ? -10.889 11.9    -30.055 1   29.51 ? 716 HOH   A O   1 
HETATM 6331 O  O   . HOH   J 5 .   ? 8.773   29.3    -48.121 1   35.24 ? 717 HOH   A O   1 
HETATM 6332 O  O   . HOH   J 5 .   ? 16.867  23.541  -31.159 1   29.62 ? 718 HOH   A O   1 
HETATM 6333 O  O   . HOH   J 5 .   ? 5.389   21.79   -45.627 1   37.68 ? 719 HOH   A O   1 
HETATM 6334 O  O   . HOH   J 5 .   ? -9.753  45.781  -24.044 1   38.33 ? 720 HOH   A O   1 
HETATM 6335 O  O   . HOH   J 5 .   ? -3.303  13.125  -22.149 1   23.7  ? 721 HOH   A O   1 
HETATM 6336 O  O   . HOH   J 5 .   ? -28.85  21.549  -6.154  1   49.4  ? 722 HOH   A O   1 
HETATM 6337 O  O   . HOH   J 5 .   ? -38.551 39.695  -19.489 1   39.62 ? 723 HOH   A O   1 
HETATM 6338 O  O   . HOH   J 5 .   ? 5.395   34.015  -14.38  1   40.23 ? 724 HOH   A O   1 
HETATM 6339 O  O   . HOH   J 5 .   ? -7.601  9.86    -29.327 1   33.05 ? 725 HOH   A O   1 
HETATM 6340 O  O   . HOH   J 5 .   ? -30.507 28.177  -14.933 1   30.6  ? 726 HOH   A O   1 
HETATM 6341 O  O   . HOH   J 5 .   ? 6.691   32.764  -41.699 1   24.27 ? 727 HOH   A O   1 
HETATM 6342 O  O   . HOH   J 5 .   ? -1.058  11.904  -22.9   1   22.53 ? 728 HOH   A O   1 
HETATM 6343 O  O   . HOH   J 5 .   ? 17.774  11.497  -27.132 1   40.86 ? 729 HOH   A O   1 
HETATM 6344 O  O   . HOH   J 5 .   ? 4.836   4.393   -31.071 1   33.64 ? 730 HOH   A O   1 
HETATM 6345 O  O   . HOH   J 5 .   ? -3.731  9.661   -40.331 1   30.28 ? 731 HOH   A O   1 
HETATM 6346 O  O   . HOH   J 5 .   ? -1.886  40.57   -35.085 1   24.39 ? 732 HOH   A O   1 
HETATM 6347 O  O   . HOH   J 5 .   ? -7.643  21.185  -29.011 1   14.33 ? 733 HOH   A O   1 
HETATM 6348 O  O   . HOH   J 5 .   ? 3.048   39.159  -17.699 1   34.44 ? 734 HOH   A O   1 
HETATM 6349 O  O   . HOH   J 5 .   ? -3.121  35.114  -25.763 1   27.96 ? 735 HOH   A O   1 
HETATM 6350 O  O   . HOH   J 5 .   ? 18.112  24.131  -16.364 1   40.65 ? 736 HOH   A O   1 
HETATM 6351 O  O   . HOH   J 5 .   ? 13.504  29.582  -21.963 1   33.41 ? 737 HOH   A O   1 
HETATM 6352 O  O   . HOH   J 5 .   ? 17.424  21.295  -32.665 1   37.29 ? 738 HOH   A O   1 
HETATM 6353 O  O   . HOH   J 5 .   ? 10.919  6.284   -27.138 1   32.29 ? 739 HOH   A O   1 
HETATM 6354 O  O   . HOH   J 5 .   ? -3.252  12.514  -14.562 1   34.25 ? 740 HOH   A O   1 
HETATM 6355 O  O   . HOH   J 5 .   ? 4.826   11.237  -42.074 1   47.86 ? 741 HOH   A O   1 
HETATM 6356 O  O   . HOH   J 5 .   ? -5.149  11.042  -44.341 1   41.02 ? 742 HOH   A O   1 
HETATM 6357 O  O   . HOH   J 5 .   ? -18.247 14.332  -23.906 1   31.55 ? 743 HOH   A O   1 
HETATM 6358 O  O   . HOH   J 5 .   ? -6.573  44.854  -39.674 1   43.33 ? 744 HOH   A O   1 
HETATM 6359 O  O   . HOH   J 5 .   ? -8.034  40.843  -46.042 1   34.44 ? 745 HOH   A O   1 
HETATM 6360 O  O   . HOH   J 5 .   ? -8.4    43.03   -19.675 1   37.46 ? 746 HOH   A O   1 
HETATM 6361 O  O   . HOH   J 5 .   ? 9.568   33.409  -17.051 1   48.22 ? 747 HOH   A O   1 
HETATM 6362 O  O   . HOH   J 5 .   ? 1.05    38.155  -34.822 1   23.64 ? 748 HOH   A O   1 
HETATM 6363 O  O   . HOH   J 5 .   ? -27.582 18.054  -35.063 1   51    ? 749 HOH   A O   1 
HETATM 6364 O  O   . HOH   J 5 .   ? -8.285  8.246   -31.355 1   29.29 ? 750 HOH   A O   1 
HETATM 6365 O  O   . HOH   J 5 .   ? 10.818  12.729  -21.926 1   36.51 ? 751 HOH   A O   1 
HETATM 6366 O  O   . HOH   J 5 .   ? 17.87   26.981  -15.477 1   44.16 ? 752 HOH   A O   1 
HETATM 6367 O  O   . HOH   J 5 .   ? -7.266  35.635  -7.432  1   43.18 ? 753 HOH   A O   1 
HETATM 6368 O  O   . HOH   J 5 .   ? 0.833   39.26   -37.563 1   27.03 ? 754 HOH   A O   1 
HETATM 6369 O  O   . HOH   J 5 .   ? -27.42  20.248  -30.374 1   37.13 ? 755 HOH   A O   1 
HETATM 6370 O  O   . HOH   J 5 .   ? -36.984 40.125  -31.032 1   42.45 ? 756 HOH   A O   1 
HETATM 6371 O  O   . HOH   J 5 .   ? -2.28   38.062  -14.282 1   30.24 ? 757 HOH   A O   1 
HETATM 6372 O  O   . HOH   J 5 .   ? -6.216  45.449  -15.867 1   46.2  ? 758 HOH   A O   1 
HETATM 6373 O  O   . HOH   J 5 .   ? 10.427  21.993  -42.304 1   31.01 ? 759 HOH   A O   1 
HETATM 6374 O  O   . HOH   J 5 .   ? -11.466 28.223  -56.956 1   57.97 ? 760 HOH   A O   1 
HETATM 6375 O  O   . HOH   J 5 .   ? 12.928  11.49   -32.212 1   22.88 ? 761 HOH   A O   1 
HETATM 6376 O  O   . HOH   J 5 .   ? -26.216 37.069  -2.127  1   36.64 ? 762 HOH   A O   1 
HETATM 6377 O  O   . HOH   J 5 .   ? -6.856  22.689  -13.759 1   32.08 ? 763 HOH   A O   1 
HETATM 6378 O  O   . HOH   J 5 .   ? 2.731   24.953  -8.924  1   48.32 ? 764 HOH   A O   1 
HETATM 6379 O  O   . HOH   J 5 .   ? -18.097 16.569  -31.589 1   36.32 ? 765 HOH   A O   1 
HETATM 6380 O  O   . HOH   J 5 .   ? 10.272  24.452  -13.398 1   41.19 ? 766 HOH   A O   1 
HETATM 6381 O  O   . HOH   J 5 .   ? 5.433   36.466  -36.047 1   31.53 ? 767 HOH   A O   1 
HETATM 6382 O  O   . HOH   J 5 .   ? -27.001 20.602  -33.511 1   35.45 ? 768 HOH   A O   1 
HETATM 6383 O  O   . HOH   J 5 .   ? 13.247  16.271  -42.747 1   55.49 ? 769 HOH   A O   1 
HETATM 6384 O  O   . HOH   J 5 .   ? -2.204  6.32    -22.111 1   49.31 ? 770 HOH   A O   1 
HETATM 6385 O  O   . HOH   J 5 .   ? 3.371   27.636  -10.784 1   33.78 ? 771 HOH   A O   1 
HETATM 6386 O  O   . HOH   J 5 .   ? -19.515 45.788  -15.05  1   50.52 ? 772 HOH   A O   1 
HETATM 6387 O  O   . HOH   J 5 .   ? -22.443 25.063  -22.141 1   38.02 ? 773 HOH   A O   1 
HETATM 6388 O  O   . HOH   J 5 .   ? -37.593 34.128  -27.44  1   59.32 ? 774 HOH   A O   1 
HETATM 6389 O  O   . HOH   J 5 .   ? -4.127  23.45   -15.975 1   42.99 ? 775 HOH   A O   1 
HETATM 6390 O  O   . HOH   J 5 .   ? -7.516  5.722   -27.784 1   33.41 ? 776 HOH   A O   1 
HETATM 6391 O  O   . HOH   J 5 .   ? -27.384 43.305  -24.958 1   42.19 ? 777 HOH   A O   1 
HETATM 6392 O  O   . HOH   J 5 .   ? -0.185  1.383   -35.907 1   38.03 ? 778 HOH   A O   1 
HETATM 6393 O  O   . HOH   J 5 .   ? -15.998 26.988  -47.584 1   61.39 ? 779 HOH   A O   1 
HETATM 6394 O  O   . HOH   J 5 .   ? -6.001  30.955  -10.692 1   37.39 ? 780 HOH   A O   1 
HETATM 6395 O  O   . HOH   J 5 .   ? 7.323   33.663  -32.397 1   30.06 ? 781 HOH   A O   1 
HETATM 6396 O  O   . HOH   J 5 .   ? 5.954   11.904  -44.685 1   58.52 ? 782 HOH   A O   1 
HETATM 6397 O  O   . HOH   J 5 .   ? -31.555 27.78   -4.077  1   42.36 ? 783 HOH   A O   1 
HETATM 6398 O  O   . HOH   J 5 .   ? 13.588  7.055   -33.593 1   49.19 ? 784 HOH   A O   1 
HETATM 6399 O  O   . HOH   J 5 .   ? 13.534  2.880   -29.776 1   55.23 ? 785 HOH   A O   1 
HETATM 6400 O  O   . HOH   J 5 .   ? -28.059 36.952  -0.308  1   34.83 ? 786 HOH   A O   1 
HETATM 6401 O  O   . HOH   J 5 .   ? -34.054 45.707  -16.147 1   47.43 ? 787 HOH   A O   1 
HETATM 6402 O  O   . HOH   J 5 .   ? -4.25   43.55   -39.213 1   34.68 ? 788 HOH   A O   1 
HETATM 6403 O  O   . HOH   J 5 .   ? -24.825 43.784  -25.486 1   29.75 ? 789 HOH   A O   1 
HETATM 6404 O  O   . HOH   J 5 .   ? -8.296  5.881   -30.334 1   34.25 ? 790 HOH   A O   1 
HETATM 6405 O  O   . HOH   J 5 .   ? -12.031 43.713  -18.974 1   34.39 ? 791 HOH   A O   1 
HETATM 6406 O  O   . HOH   J 5 .   ? -5.805  25.026  -14.324 1   37.59 ? 792 HOH   A O   1 
HETATM 6407 O  O   . HOH   J 5 .   ? -24.112 41.995  -7.29   1   40.34 ? 793 HOH   A O   1 
HETATM 6408 O  O   . HOH   J 5 .   ? -5.709  50.045  -32.341 1   38.02 ? 794 HOH   A O   1 
HETATM 6409 O  O   . HOH   J 5 .   ? 8.239   22.262  -45.304 1   40.91 ? 795 HOH   A O   1 
HETATM 6410 O  O   . HOH   J 5 .   ? 17.243  23.848  -33.548 1   41.51 ? 796 HOH   A O   1 
HETATM 6411 O  O   . HOH   J 5 .   ? -30.626 44.392  -22.502 1   29.04 ? 797 HOH   A O   1 
HETATM 6412 O  O   . HOH   J 5 .   ? 19.555  20.508  -31.583 1   44.51 ? 798 HOH   A O   1 
HETATM 6413 O  O   . HOH   J 5 .   ? -8.593  43.73   -17.026 1   35.44 ? 799 HOH   A O   1 
HETATM 6414 O  O   . HOH   J 5 .   ? -6.168  6.488   -24.751 1   47.33 ? 800 HOH   A O   1 
HETATM 6415 O  O   . HOH   J 5 .   ? -2.066  9.501   -21.543 1   27.8  ? 801 HOH   A O   1 
HETATM 6416 O  O   . HOH   J 5 .   ? -15.654 41.844  -45.482 1   43.12 ? 802 HOH   A O   1 
HETATM 6417 O  O   . HOH   J 5 .   ? 2.947   39.906  -33.669 1   27.41 ? 803 HOH   A O   1 
HETATM 6418 O  O   . HOH   J 5 .   ? -0.825  6.69    -40.014 1   39.69 ? 804 HOH   A O   1 
HETATM 6419 O  O   . HOH   J 5 .   ? -10.434 42.087  -46.615 1   49.61 ? 805 HOH   A O   1 
HETATM 6420 O  O   . HOH   J 5 .   ? -33.652 27.347  -6.013  1   39.59 ? 806 HOH   A O   1 
HETATM 6421 O  O   . HOH   K 5 .   ? -41.302 -2.228  -5.36   1   45.95 ? 601 HOH   B O   1 
HETATM 6422 O  O   . HOH   K 5 .   ? -11.801 -13.321 -18.059 1   52.35 ? 602 HOH   B O   1 
HETATM 6423 O  O   . HOH   K 5 .   ? -11.974 3.615   -20.71  1   35.3  ? 603 HOH   B O   1 
HETATM 6424 O  O   . HOH   K 5 .   ? -50.32  -14.354 -26.816 1   45.24 ? 604 HOH   B O   1 
HETATM 6425 O  O   . HOH   K 5 .   ? -24.564 -12.835 -35.147 1   42.18 ? 605 HOH   B O   1 
HETATM 6426 O  O   . HOH   K 5 .   ? -15.844 -0.75   -29.118 1   39.21 ? 606 HOH   B O   1 
HETATM 6427 O  O   . HOH   K 5 .   ? -14.036 10.86   -29.163 1   41.2  ? 607 HOH   B O   1 
HETATM 6428 O  O   . HOH   K 5 .   ? -16.238 3.544   -15.637 1   26.1  ? 608 HOH   B O   1 
HETATM 6429 O  O   . HOH   K 5 .   ? -12.738 7.304   -14.646 1   31.92 ? 609 HOH   B O   1 
HETATM 6430 O  O   . HOH   K 5 .   ? -29.666 5.252   -35.406 1   44.78 ? 610 HOH   B O   1 
HETATM 6431 O  O   . HOH   K 5 .   ? -51.201 8.63    -23.337 1   36.12 ? 611 HOH   B O   1 
HETATM 6432 O  O   . HOH   K 5 .   ? -26.371 -10.089 -34.877 1   37.83 ? 612 HOH   B O   1 
HETATM 6433 O  O   . HOH   K 5 .   ? -31.558 11.033  -0.537  1   48.11 ? 613 HOH   B O   1 
HETATM 6434 O  O   . HOH   K 5 .   ? -37.385 5.092   -13.849 1   26.72 ? 614 HOH   B O   1 
HETATM 6435 O  O   . HOH   K 5 .   ? 1.614   11.467  -7.109  1   35.84 ? 615 HOH   B O   1 
HETATM 6436 O  O   . HOH   K 5 .   ? -12.008 -8.34   -29.499 1   43.1  ? 616 HOH   B O   1 
HETATM 6437 O  O   . HOH   K 5 .   ? -5.104  3.439   -16.311 1   42.1  ? 617 HOH   B O   1 
HETATM 6438 O  O   . HOH   K 5 .   ? -20.731 7.245   -27.482 1   32.69 ? 618 HOH   B O   1 
HETATM 6439 O  O   . HOH   K 5 .   ? -17.681 -18.111 -20.601 1   35.67 ? 619 HOH   B O   1 
HETATM 6440 O  O   . HOH   K 5 .   ? -46.317 4.966   -35.702 1   38.19 ? 620 HOH   B O   1 
HETATM 6441 O  O   . HOH   K 5 .   ? -13.734 -8.414  -7.378  1   33.4  ? 621 HOH   B O   1 
HETATM 6442 O  O   . HOH   K 5 .   ? -27.656 2.166   -28.743 1   31.02 ? 622 HOH   B O   1 
HETATM 6443 O  O   . HOH   K 5 .   ? -23.031 -20.036 -24.934 1   26.9  ? 623 HOH   B O   1 
HETATM 6444 O  O   . HOH   K 5 .   ? -9.491  14.761  0.658   1   38.64 ? 624 HOH   B O   1 
HETATM 6445 O  O   . HOH   K 5 .   ? -28.35  -1.272  -25.696 1   41.83 ? 625 HOH   B O   1 
HETATM 6446 O  O   . HOH   K 5 .   ? -20.584 13.428  -23.617 1   40.53 ? 626 HOH   B O   1 
HETATM 6447 O  O   . HOH   K 5 .   ? -22.327 -10.897 -34.605 1   37.94 ? 627 HOH   B O   1 
HETATM 6448 O  O   . HOH   K 5 .   ? -38.03  5.425   -19.781 1   25.24 ? 628 HOH   B O   1 
HETATM 6449 O  O   . HOH   K 5 .   ? -2.438  -5.562  -3.269  1   32.55 ? 629 HOH   B O   1 
HETATM 6450 O  O   . HOH   K 5 .   ? -20.28  10.713  -29.114 1   27.76 ? 630 HOH   B O   1 
HETATM 6451 O  O   . HOH   K 5 .   ? -18.103 1.509   -16.015 1   21.58 ? 631 HOH   B O   1 
HETATM 6452 O  O   . HOH   K 5 .   ? -11.544 16.272  -0.211  1   38.46 ? 632 HOH   B O   1 
HETATM 6453 O  O   . HOH   K 5 .   ? -13.606 -14.212 -22.779 1   26.45 ? 633 HOH   B O   1 
HETATM 6454 O  O   . HOH   K 5 .   ? 0.996   2.343   11.052  1   26.27 ? 634 HOH   B O   1 
HETATM 6455 O  O   . HOH   K 5 .   ? -5.319  9.169   -11.824 1   31.38 ? 635 HOH   B O   1 
HETATM 6456 O  O   . HOH   K 5 .   ? -20.885 1.914   -15.395 1   22.54 ? 636 HOH   B O   1 
HETATM 6457 O  O   . HOH   K 5 .   ? -0.154  -4.99   -7.25   1   42.08 ? 637 HOH   B O   1 
HETATM 6458 O  O   . HOH   K 5 .   ? -27.542 10.518  -0.749  1   36.88 ? 638 HOH   B O   1 
HETATM 6459 O  O   . HOH   K 5 .   ? -39.938 -12.987 -18.808 1   37.97 ? 639 HOH   B O   1 
HETATM 6460 O  O   . HOH   K 5 .   ? -18.668 -19.042 -12.084 1   44.38 ? 640 HOH   B O   1 
HETATM 6461 O  O   . HOH   K 5 .   ? -1.806  -3.059  3.008   1   36.41 ? 641 HOH   B O   1 
HETATM 6462 O  O   . HOH   K 5 .   ? -3.795  15.902  2.632   1   54.13 ? 642 HOH   B O   1 
HETATM 6463 O  O   . HOH   K 5 .   ? -35.571 14.532  -22.093 1   46.82 ? 643 HOH   B O   1 
HETATM 6464 O  O   . HOH   K 5 .   ? -8.833  6.37    -20.762 1   37.97 ? 644 HOH   B O   1 
HETATM 6465 O  O   . HOH   K 5 .   ? -9.711  10.084  -6.593  1   35.42 ? 645 HOH   B O   1 
HETATM 6466 O  O   . HOH   K 5 .   ? -26.261 -21.281 -17.549 1   41.46 ? 646 HOH   B O   1 
HETATM 6467 O  O   . HOH   K 5 .   ? -27.536 5.842   -11.392 1   25.72 ? 647 HOH   B O   1 
HETATM 6468 O  O   . HOH   K 5 .   ? -8.365  -7.66   -4.366  1   31.99 ? 648 HOH   B O   1 
HETATM 6469 O  O   . HOH   K 5 .   ? -29.547 5.184   -16.223 1   18.51 ? 649 HOH   B O   1 
HETATM 6470 O  O   . HOH   K 5 .   ? -29.208 -5.38   -27.907 1   38.72 ? 650 HOH   B O   1 
HETATM 6471 O  O   . HOH   K 5 .   ? -31.251 5.857   -4.434  1   35.2  ? 651 HOH   B O   1 
HETATM 6472 O  O   . HOH   K 5 .   ? -34.373 -4.798  -11.667 1   32.02 ? 652 HOH   B O   1 
HETATM 6473 O  O   . HOH   K 5 .   ? 1.86    7.302   4.279   1   34.86 ? 653 HOH   B O   1 
HETATM 6474 O  O   . HOH   K 5 .   ? -4.614  12.055  -17.751 1   33.13 ? 654 HOH   B O   1 
HETATM 6475 O  O   . HOH   K 5 .   ? -40.958 3.8     -8.567  1   29.59 ? 655 HOH   B O   1 
HETATM 6476 O  O   . HOH   K 5 .   ? -14.321 -10.394 1.57    1   57.11 ? 656 HOH   B O   1 
HETATM 6477 O  O   . HOH   K 5 .   ? 3.665   5.188   -2.247  1   45.15 ? 657 HOH   B O   1 
HETATM 6478 O  O   . HOH   K 5 .   ? -28.061 5.139   -14.018 1   23.84 ? 658 HOH   B O   1 
HETATM 6479 O  O   . HOH   K 5 .   ? -33.663 0.739   1.246   1   44.09 ? 659 HOH   B O   1 
HETATM 6480 O  O   . HOH   K 5 .   ? -26.676 -7.965  -3.39   1   35.75 ? 660 HOH   B O   1 
HETATM 6481 O  O   . HOH   K 5 .   ? -26.268 3.22    -11.042 1   24.35 ? 661 HOH   B O   1 
HETATM 6482 O  O   . HOH   K 5 .   ? -10.563 -2.678  6.544   1   34.22 ? 662 HOH   B O   1 
HETATM 6483 O  O   . HOH   K 5 .   ? -37.118 -15.171 -7.152  1   37.73 ? 663 HOH   B O   1 
HETATM 6484 O  O   . HOH   K 5 .   ? -15.798 -6.815  -18.885 1   18.83 ? 664 HOH   B O   1 
HETATM 6485 O  O   . HOH   K 5 .   ? -12.252 -13.031 -12.323 1   32.76 ? 665 HOH   B O   1 
HETATM 6486 O  O   . HOH   K 5 .   ? -26.824 11.098  -26.592 1   55.62 ? 666 HOH   B O   1 
HETATM 6487 O  O   . HOH   K 5 .   ? -9.217  7.229   -24.575 1   24.41 ? 667 HOH   B O   1 
HETATM 6488 O  O   . HOH   K 5 .   ? -14.427 13.979  -27.562 1   29.74 ? 668 HOH   B O   1 
HETATM 6489 O  O   . HOH   K 5 .   ? -32.083 5.306   -9.298  1   31.83 ? 669 HOH   B O   1 
HETATM 6490 O  O   . HOH   K 5 .   ? -18.533 -1.345  3.796   1   41.89 ? 670 HOH   B O   1 
HETATM 6491 O  O   . HOH   K 5 .   ? -13.029 10.386  -25.694 1   39.16 ? 671 HOH   B O   1 
HETATM 6492 O  O   . HOH   K 5 .   ? -28.829 -7.33   -1.873  1   38.52 ? 672 HOH   B O   1 
HETATM 6493 O  O   . HOH   K 5 .   ? -30.672 4.471   -22.782 1   22.75 ? 673 HOH   B O   1 
HETATM 6494 O  O   . HOH   K 5 .   ? -44.042 -13.259 -25.575 1   39.57 ? 674 HOH   B O   1 
HETATM 6495 O  O   . HOH   K 5 .   ? 1.422   -2.37   -4.574  1   32.53 ? 675 HOH   B O   1 
HETATM 6496 O  O   . HOH   K 5 .   ? -17.625 -7.573  -30.119 1   28.06 ? 676 HOH   B O   1 
HETATM 6497 O  O   . HOH   K 5 .   ? -27.966 -17.689 -31.971 1   40.85 ? 677 HOH   B O   1 
HETATM 6498 O  O   . HOH   K 5 .   ? -22.918 -7.068  -35.91  1   40.68 ? 678 HOH   B O   1 
HETATM 6499 O  O   . HOH   K 5 .   ? -11.069 3.4     7.902   1   37.72 ? 679 HOH   B O   1 
HETATM 6500 O  O   . HOH   K 5 .   ? -14.644 -4.364  -18.759 1   18.96 ? 680 HOH   B O   1 
HETATM 6501 O  O   . HOH   K 5 .   ? -4.837  6.988   10.993  1   32.17 ? 681 HOH   B O   1 
HETATM 6502 O  O   . HOH   K 5 .   ? -46.015 -7.156  -31.704 1   34.15 ? 682 HOH   B O   1 
HETATM 6503 O  O   . HOH   K 5 .   ? -7.738  13.317  -21.705 1   36.61 ? 683 HOH   B O   1 
HETATM 6504 O  O   . HOH   K 5 .   ? -40.345 -7.058  -35.916 1   44.69 ? 684 HOH   B O   1 
HETATM 6505 O  O   . HOH   K 5 .   ? -19.555 -18.762 -36.925 1   31.99 ? 685 HOH   B O   1 
HETATM 6506 O  O   . HOH   K 5 .   ? -37.493 19.267  -13.153 1   48.72 ? 686 HOH   B O   1 
HETATM 6507 O  O   . HOH   K 5 .   ? -34.834 -15.125 -15.601 1   29.25 ? 687 HOH   B O   1 
HETATM 6508 O  O   . HOH   K 5 .   ? -31.758 -3.21   -33.257 1   39.79 ? 688 HOH   B O   1 
HETATM 6509 O  O   . HOH   K 5 .   ? -37.716 15.155  -23.67  1   39.2  ? 689 HOH   B O   1 
HETATM 6510 O  O   . HOH   K 5 .   ? -7.104  -9.03   -10.489 1   35.8  ? 690 HOH   B O   1 
HETATM 6511 O  O   . HOH   K 5 .   ? -7.663  8.905   -7.663  1   39.19 ? 691 HOH   B O   1 
HETATM 6512 O  O   . HOH   K 5 .   ? 3.439   -0.962  -5.062  1   55.53 ? 692 HOH   B O   1 
HETATM 6513 O  O   . HOH   K 5 .   ? -17.338 -6.522  -37.773 1   52.38 ? 693 HOH   B O   1 
HETATM 6514 O  O   . HOH   K 5 .   ? -21.567 13.658  -20.311 1   39.87 ? 694 HOH   B O   1 
HETATM 6515 O  O   . HOH   K 5 .   ? -28.499 -0.144  -28.851 1   34.7  ? 695 HOH   B O   1 
HETATM 6516 O  O   . HOH   K 5 .   ? -51.613 -15.417 -30.403 1   43.94 ? 696 HOH   B O   1 
HETATM 6517 O  O   . HOH   K 5 .   ? -47.724 15.881  -35.842 1   57.14 ? 697 HOH   B O   1 
HETATM 6518 O  O   . HOH   K 5 .   ? -18.863 14.48   -15.196 1   52.94 ? 698 HOH   B O   1 
HETATM 6519 O  O   . HOH   K 5 .   ? -25.624 1.083   -6.359  1   31.49 ? 699 HOH   B O   1 
HETATM 6520 O  O   . HOH   K 5 .   ? -48.108 -5.388  -32.17  1   38.82 ? 700 HOH   B O   1 
HETATM 6521 O  O   . HOH   K 5 .   ? -30.323 9.111   0.717   1   47.96 ? 701 HOH   B O   1 
HETATM 6522 O  O   . HOH   K 5 .   ? -24.117 -7.042  -33.573 1   30.86 ? 702 HOH   B O   1 
HETATM 6523 O  O   . HOH   K 5 .   ? -40.903 1.776   -10.35  1   28.57 ? 703 HOH   B O   1 
HETATM 6524 O  O   . HOH   K 5 .   ? -15.587 3.741   6.949   1   43.66 ? 704 HOH   B O   1 
HETATM 6525 O  O   . HOH   K 5 .   ? 4.360   0.209   4.529   1   30.06 ? 705 HOH   B O   1 
HETATM 6526 O  O   . HOH   K 5 .   ? 7.825   2.366   -0.557  1   39.36 ? 706 HOH   B O   1 
HETATM 6527 O  O   . HOH   K 5 .   ? -34.564 6.32    -38.827 1   61.35 ? 707 HOH   B O   1 
HETATM 6528 O  O   . HOH   K 5 .   ? -10.861 5.034   -24.551 1   24.08 ? 708 HOH   B O   1 
HETATM 6529 O  O   . HOH   K 5 .   ? -26.998 17.322  -13.741 1   37.43 ? 709 HOH   B O   1 
HETATM 6530 O  O   . HOH   K 5 .   ? -9.078  -9.565  -6.738  1   36.65 ? 710 HOH   B O   1 
HETATM 6531 O  O   . HOH   K 5 .   ? -37.807 -15.779 -18.469 1   32.32 ? 711 HOH   B O   1 
HETATM 6532 O  O   . HOH   K 5 .   ? -12.875 17.802  7.141   1   80.52 ? 712 HOH   B O   1 
HETATM 6533 O  O   . HOH   K 5 .   ? -31.855 12.409  -9.776  1   34.88 ? 713 HOH   B O   1 
HETATM 6534 O  O   . HOH   K 5 .   ? -15.742 -1.384  -33.73  1   41.92 ? 714 HOH   B O   1 
HETATM 6535 O  O   . HOH   K 5 .   ? -40.887 -3.607  -2.818  1   50.89 ? 715 HOH   B O   1 
HETATM 6536 O  O   . HOH   K 5 .   ? -47.135 0.988   -5.236  1   49.87 ? 716 HOH   B O   1 
HETATM 6537 O  O   . HOH   K 5 .   ? -38.523 20.051  -33.417 1   54.3  ? 717 HOH   B O   1 
HETATM 6538 O  O   . HOH   K 5 .   ? -42.876 -12.749 -18.723 1   44.12 ? 718 HOH   B O   1 
HETATM 6539 O  O   . HOH   K 5 .   ? -38.028 -13.428 -16.989 1   30.47 ? 719 HOH   B O   1 
HETATM 6540 O  O   . HOH   K 5 .   ? -9.865  3.934   -21.938 1   40.6  ? 720 HOH   B O   1 
HETATM 6541 O  O   . HOH   K 5 .   ? -28.781 -21.723 -24.164 1   56.44 ? 721 HOH   B O   1 
HETATM 6542 O  O   . HOH   K 5 .   ? 5.192   1.223   -6.881  1   48.78 ? 722 HOH   B O   1 
HETATM 6543 O  O   . HOH   K 5 .   ? -35.251 -0.638  -0.677  1   39.51 ? 723 HOH   B O   1 
HETATM 6544 O  O   . HOH   K 5 .   ? -41.313 9.74    -4.025  1   49.46 ? 724 HOH   B O   1 
HETATM 6545 O  O   . HOH   K 5 .   ? -13.695 -1.18   -31.58  1   50.11 ? 725 HOH   B O   1 
HETATM 6546 O  O   . HOH   K 5 .   ? -6.766  15.788  0.737   1   44.97 ? 726 HOH   B O   1 
HETATM 6547 O  O   . HOH   K 5 .   ? -31.61  21.514  -12.347 1   58.93 ? 727 HOH   B O   1 
HETATM 6548 O  O   . HOH   K 5 .   ? -36.242 -17.765 -7.22   1   44.47 ? 728 HOH   B O   1 
HETATM 6549 O  O   . HOH   K 5 .   ? -32.298 7.745   -2.241  1   47.24 ? 729 HOH   B O   1 
HETATM 6550 O  O   . HOH   K 5 .   ? -11.783 -10.47  -6.457  1   32.14 ? 730 HOH   B O   1 
HETATM 6551 O  O   . HOH   K 5 .   ? -27.877 -3.383  -26.872 1   38    ? 731 HOH   B O   1 
HETATM 6552 O  O   . HOH   K 5 .   ? -13.197 2.027   6.689   1   39.54 ? 732 HOH   B O   1 
HETATM 6553 O  O   . HOH   K 5 .   ? -32.548 10.158  -8.697  1   45.74 ? 733 HOH   B O   1 
HETATM 6554 O  O   . HOH   K 5 .   ? -37.489 -18.242 -9.736  1   55.01 ? 734 HOH   B O   1 
HETATM 6555 O  O   . HOH   K 5 .   ? -26.382 -5.657  -33.636 1   59.56 ? 735 HOH   B O   1 
HETATM 6556 O  O   . HOH   K 5 .   ? -5.211  12.295  -23.994 1   38.46 ? 736 HOH   B O   1 
HETATM 6557 O  O   . HOH   K 5 .   ? -36.246 -16.993 -15.716 1   44.17 ? 737 HOH   B O   1 
HETATM 6558 O  O   . HOH   K 5 .   ? -15.294 12.996  -23.524 1   48.89 ? 738 HOH   B O   1 
HETATM 6559 O  O   . HOH   K 5 .   ? -24.331 -9.733  -33.099 1   40.41 ? 739 HOH   B O   1 
HETATM 6560 O  O   . HOH   K 5 .   ? -12.461 -12.54  -4.846  1   59.12 ? 740 HOH   B O   1 
HETATM 6561 O  O   . HOH   K 5 .   ? -19.564 8.822   -30.741 1   49.12 ? 741 HOH   B O   1 
HETATM 6562 O  O   . HOH   K 5 .   ? -30.145 -15.872 -32.602 1   44.33 ? 742 HOH   B O   1 
HETATM 6563 O  O   . HOH   K 5 .   ? -39.963 -13.983 -14.658 1   42.32 ? 743 HOH   B O   1 
HETATM 6564 O  O   . HOH   K 5 .   ? -4.619  15.219  -1.398  1   36.2  ? 744 HOH   B O   1 
# 
