data_9EW0
# 
_entry.id   9EW0 
# 
_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   9EW0         pdb_00009ew0 10.2210/pdb9ew0/pdb 
WWPDB D_1292136140 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-02 
_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                        9EW0 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-03 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              aengus.mac-sweeney@idorsia.com 
_pdbx_contact_author.name_first         Aengus 
_pdbx_contact_author.name_last          'Mac Sweeney' 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7250-9541 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Wicki, M.'       1 ? 
'Mac Sweeney, A.' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'SAR and cellular potency optimization of novel heme-binding IDO1 inhibitors' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Cren, S.'        1 ? 
primary 'Lotz, C.'        2 ? 
primary 'Mac Sweeney, A.' 3 ? 
primary 'Lange, R.'       4 ? 
primary 'Kimmerlin, T.'   5 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Indoleamine 2,3-dioxygenase 1'                         47085.105 2   1.13.11.52 ? ? ? 
2 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE'                       616.487   2   ?          ? ? ? 
3 non-polymer syn '(~{S})-cyclohexyl(imidazo[1,5-a]pyridin-5-yl)methanol' 230.306   2   ?          ? ? ? 
4 water       nat water                                                   18.015    189 ?          ? ? ? 
# 
_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 '(~{S})-cyclohexyl(imidazo[1,5-a]pyridin-5-yl)methanol' A1H6U 
4 water                                                   HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  ALA n 
1 13  ALA n 
1 14  LEU n 
1 15  GLU n 
1 16  VAL n 
1 17  LEU n 
1 18  PHE n 
1 19  GLN n 
1 20  GLY n 
1 21  PRO n 
1 22  HIS n 
1 23  MET n 
1 24  TRP n 
1 25  THR n 
1 26  ILE n 
1 27  SER n 
1 28  LYS n 
1 29  GLU n 
1 30  TYR n 
1 31  HIS n 
1 32  ILE n 
1 33  ASP n 
1 34  GLU n 
1 35  GLU n 
1 36  VAL n 
1 37  GLY n 
1 38  PHE n 
1 39  ALA n 
1 40  LEU n 
1 41  PRO n 
1 42  ASN n 
1 43  PRO n 
1 44  GLN n 
1 45  GLU n 
1 46  ASN n 
1 47  LEU n 
1 48  PRO n 
1 49  ASP n 
1 50  PHE n 
1 51  TYR n 
1 52  ASN n 
1 53  ASP n 
1 54  TRP n 
1 55  MET n 
1 56  PHE n 
1 57  ILE n 
1 58  ALA n 
1 59  LYS n 
1 60  HIS n 
1 61  LEU n 
1 62  PRO n 
1 63  ASP n 
1 64  LEU n 
1 65  ILE n 
1 66  GLU n 
1 67  SER n 
1 68  GLY n 
1 69  GLN n 
1 70  LEU n 
1 71  ARG n 
1 72  GLU n 
1 73  ARG n 
1 74  VAL n 
1 75  GLU n 
1 76  LYS n 
1 77  LEU n 
1 78  ASN n 
1 79  MET n 
1 80  LEU n 
1 81  SER n 
1 82  ILE n 
1 83  ASP n 
1 84  HIS n 
1 85  LEU n 
1 86  THR n 
1 87  ASP n 
1 88  HIS n 
1 89  LYS n 
1 90  SER n 
1 91  GLN n 
1 92  ARG n 
1 93  LEU n 
1 94  ALA n 
1 95  ARG n 
1 96  LEU n 
1 97  VAL n 
1 98  LEU n 
1 99  GLY n 
1 100 CYS n 
1 101 ILE n 
1 102 THR n 
1 103 MET n 
1 104 ALA n 
1 105 TYR n 
1 106 VAL n 
1 107 TRP n 
1 108 GLY n 
1 109 LYS n 
1 110 GLY n 
1 111 HIS n 
1 112 GLY n 
1 113 ASP n 
1 114 VAL n 
1 115 ARG n 
1 116 LYS n 
1 117 VAL n 
1 118 LEU n 
1 119 PRO n 
1 120 ARG n 
1 121 ASN n 
1 122 ILE n 
1 123 ALA n 
1 124 VAL n 
1 125 PRO n 
1 126 TYR n 
1 127 CYS n 
1 128 GLN n 
1 129 LEU n 
1 130 SER n 
1 131 LYS n 
1 132 LYS n 
1 133 LEU n 
1 134 GLU n 
1 135 LEU n 
1 136 PRO n 
1 137 PRO n 
1 138 ILE n 
1 139 LEU n 
1 140 VAL n 
1 141 TYR n 
1 142 ALA n 
1 143 ASP n 
1 144 CYS n 
1 145 VAL n 
1 146 LEU n 
1 147 ALA n 
1 148 ASN n 
1 149 TRP n 
1 150 LYS n 
1 151 LYS n 
1 152 LYS n 
1 153 ASP n 
1 154 PRO n 
1 155 ASN n 
1 156 LYS n 
1 157 PRO n 
1 158 LEU n 
1 159 THR n 
1 160 TYR n 
1 161 GLU n 
1 162 ASN n 
1 163 MET n 
1 164 ASP n 
1 165 VAL n 
1 166 LEU n 
1 167 PHE n 
1 168 SER n 
1 169 PHE n 
1 170 ARG n 
1 171 ASP n 
1 172 GLY n 
1 173 ASP n 
1 174 CYS n 
1 175 SER n 
1 176 LYS n 
1 177 GLY n 
1 178 PHE n 
1 179 PHE n 
1 180 LEU n 
1 181 VAL n 
1 182 SER n 
1 183 LEU n 
1 184 LEU n 
1 185 VAL n 
1 186 GLU n 
1 187 ILE n 
1 188 ALA n 
1 189 ALA n 
1 190 ALA n 
1 191 SER n 
1 192 ALA n 
1 193 ILE n 
1 194 LYS n 
1 195 VAL n 
1 196 ILE n 
1 197 PRO n 
1 198 THR n 
1 199 VAL n 
1 200 PHE n 
1 201 LYS n 
1 202 ALA n 
1 203 MET n 
1 204 GLN n 
1 205 MET n 
1 206 GLN n 
1 207 GLU n 
1 208 ARG n 
1 209 ASP n 
1 210 THR n 
1 211 LEU n 
1 212 LEU n 
1 213 LYS n 
1 214 ALA n 
1 215 LEU n 
1 216 LEU n 
1 217 GLU n 
1 218 ILE n 
1 219 ALA n 
1 220 SER n 
1 221 CYS n 
1 222 LEU n 
1 223 GLU n 
1 224 LYS n 
1 225 ALA n 
1 226 LEU n 
1 227 GLN n 
1 228 VAL n 
1 229 PHE n 
1 230 HIS n 
1 231 GLN n 
1 232 ILE n 
1 233 HIS n 
1 234 ASP n 
1 235 HIS n 
1 236 VAL n 
1 237 ASN n 
1 238 PRO n 
1 239 LYS n 
1 240 ALA n 
1 241 PHE n 
1 242 PHE n 
1 243 SER n 
1 244 VAL n 
1 245 LEU n 
1 246 ARG n 
1 247 ILE n 
1 248 TYR n 
1 249 LEU n 
1 250 SER n 
1 251 GLY n 
1 252 TRP n 
1 253 LYS n 
1 254 GLY n 
1 255 ASN n 
1 256 PRO n 
1 257 GLN n 
1 258 LEU n 
1 259 SER n 
1 260 ASP n 
1 261 GLY n 
1 262 LEU n 
1 263 VAL n 
1 264 TYR n 
1 265 GLU n 
1 266 GLY n 
1 267 PHE n 
1 268 TRP n 
1 269 GLU n 
1 270 ASP n 
1 271 PRO n 
1 272 LYS n 
1 273 GLU n 
1 274 PHE n 
1 275 ALA n 
1 276 GLY n 
1 277 GLY n 
1 278 SER n 
1 279 ALA n 
1 280 GLY n 
1 281 GLN n 
1 282 SER n 
1 283 SER n 
1 284 VAL n 
1 285 PHE n 
1 286 GLN n 
1 287 CYS n 
1 288 PHE n 
1 289 ASP n 
1 290 VAL n 
1 291 LEU n 
1 292 LEU n 
1 293 GLY n 
1 294 ILE n 
1 295 GLN n 
1 296 GLN n 
1 297 THR n 
1 298 ALA n 
1 299 GLY n 
1 300 GLY n 
1 301 GLY n 
1 302 HIS n 
1 303 ALA n 
1 304 ALA n 
1 305 GLN n 
1 306 PHE n 
1 307 LEU n 
1 308 GLN n 
1 309 ASP n 
1 310 MET n 
1 311 ARG n 
1 312 ARG n 
1 313 TYR n 
1 314 MET n 
1 315 PRO n 
1 316 PRO n 
1 317 ALA n 
1 318 HIS n 
1 319 ARG n 
1 320 ASN n 
1 321 PHE n 
1 322 LEU n 
1 323 CYS n 
1 324 SER n 
1 325 LEU n 
1 326 GLU n 
1 327 SER n 
1 328 ASN n 
1 329 PRO n 
1 330 SER n 
1 331 VAL n 
1 332 ARG n 
1 333 GLU n 
1 334 PHE n 
1 335 VAL n 
1 336 LEU n 
1 337 SER n 
1 338 LYS n 
1 339 GLY n 
1 340 ASP n 
1 341 ALA n 
1 342 GLY n 
1 343 LEU n 
1 344 ARG n 
1 345 GLU n 
1 346 ALA n 
1 347 TYR n 
1 348 ASP n 
1 349 ALA n 
1 350 CYS n 
1 351 VAL n 
1 352 LYS n 
1 353 ALA n 
1 354 LEU n 
1 355 VAL n 
1 356 SER n 
1 357 LEU n 
1 358 ARG n 
1 359 SER n 
1 360 TYR n 
1 361 HIS n 
1 362 LEU n 
1 363 GLN n 
1 364 ILE n 
1 365 VAL n 
1 366 THR n 
1 367 LYS n 
1 368 TYR n 
1 369 ILE n 
1 370 LEU n 
1 371 ILE n 
1 372 PRO n 
1 373 ALA n 
1 374 SER n 
1 375 GLN n 
1 376 GLN n 
1 377 PRO n 
1 378 LYS n 
1 379 GLU n 
1 380 ASN n 
1 381 LYS n 
1 382 THR n 
1 383 SER n 
1 384 GLU n 
1 385 ASP n 
1 386 PRO n 
1 387 SER n 
1 388 LYS n 
1 389 LEU n 
1 390 GLU n 
1 391 ALA n 
1 392 LYS n 
1 393 GLY n 
1 394 THR n 
1 395 GLY n 
1 396 GLY n 
1 397 THR n 
1 398 ASP n 
1 399 LEU n 
1 400 MET n 
1 401 ASN n 
1 402 PHE n 
1 403 LEU n 
1 404 LYS n 
1 405 THR n 
1 406 VAL n 
1 407 ARG n 
1 408 SER n 
1 409 THR n 
1 410 THR n 
1 411 GLU n 
1 412 LYS n 
1 413 SER n 
1 414 LEU n 
1 415 LEU n 
1 416 LYS n 
1 417 GLU n 
1 418 GLY n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   418 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'IDO1, IDO, INDO' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1H6U non-polymer         . '(~{S})-cyclohexyl(imidazo[1,5-a]pyridin-5-yl)methanol' ?    'C14 H18 N2 O'     230.306 
ALA   'L-peptide linking' y ALANINE                                                 ?    'C3 H7 N O2'       89.093  
ARG   'L-peptide linking' y ARGININE                                                ?    'C6 H15 N4 O2 1'   175.209 
ASN   'L-peptide linking' y ASPARAGINE                                              ?    'C4 H8 N2 O3'      132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                         ?    'C4 H7 N O4'       133.103 
CYS   'L-peptide linking' y CYSTEINE                                                ?    'C3 H7 N O2 S'     121.158 
GLN   'L-peptide linking' y GLUTAMINE                                               ?    'C5 H10 N2 O3'     146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                         ?    'C5 H9 N O4'       147.129 
GLY   'peptide linking'   y GLYCINE                                                 ?    'C2 H5 N O2'       75.067  
HEM   non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE'                       HEME 'C34 H32 Fe N4 O4' 616.487 
HIS   'L-peptide linking' y HISTIDINE                                               ?    'C6 H10 N3 O2 1'   156.162 
HOH   non-polymer         . WATER                                                   ?    'H2 O'             18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                              ?    'C6 H13 N O2'      131.173 
LEU   'L-peptide linking' y LEUCINE                                                 ?    'C6 H13 N O2'      131.173 
LYS   'L-peptide linking' y LYSINE                                                  ?    'C6 H15 N2 O2 1'   147.195 
MET   'L-peptide linking' y METHIONINE                                              ?    'C5 H11 N O2 S'    149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                           ?    'C9 H11 N O2'      165.189 
PRO   'L-peptide linking' y PROLINE                                                 ?    'C5 H9 N O2'       115.130 
SER   'L-peptide linking' y SERINE                                                  ?    'C3 H7 N O3'       105.093 
THR   'L-peptide linking' y THREONINE                                               ?    'C4 H9 N O3'       119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                              ?    'C11 H12 N2 O2'    204.225 
TYR   'L-peptide linking' y TYROSINE                                                ?    'C9 H11 N O3'      181.189 
VAL   'L-peptide linking' y VALINE                                                  ?    'C5 H11 N O2'      117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -14 ?   ?   ?   A . n 
A 1 2   GLY 2   -13 ?   ?   ?   A . n 
A 1 3   SER 3   -12 ?   ?   ?   A . n 
A 1 4   SER 4   -11 ?   ?   ?   A . n 
A 1 5   HIS 5   -10 ?   ?   ?   A . n 
A 1 6   HIS 6   -9  ?   ?   ?   A . n 
A 1 7   HIS 7   -8  ?   ?   ?   A . n 
A 1 8   HIS 8   -7  ?   ?   ?   A . n 
A 1 9   HIS 9   -6  ?   ?   ?   A . n 
A 1 10  HIS 10  -5  ?   ?   ?   A . n 
A 1 11  SER 11  -4  ?   ?   ?   A . n 
A 1 12  ALA 12  -3  ?   ?   ?   A . n 
A 1 13  ALA 13  -2  ?   ?   ?   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   ?   ?   ?   A . n 
A 1 20  GLY 20  5   ?   ?   ?   A . n 
A 1 21  PRO 21  6   ?   ?   ?   A . n 
A 1 22  HIS 22  7   ?   ?   ?   A . n 
A 1 23  MET 23  8   ?   ?   ?   A . n 
A 1 24  TRP 24  9   ?   ?   ?   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 ?   ?   ?   A . n 
A 1 392 LYS 392 377 ?   ?   ?   A . n 
A 1 393 GLY 393 378 ?   ?   ?   A . n 
A 1 394 THR 394 379 ?   ?   ?   A . n 
A 1 395 GLY 395 380 ?   ?   ?   A . n 
A 1 396 GLY 396 381 381 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  10  THR THR B . n 
B 1 26  ILE 26  11  11  ILE ILE B . n 
B 1 27  SER 27  12  12  SER SER B . n 
B 1 28  LYS 28  13  13  LYS LYS B . n 
B 1 29  GLU 29  14  14  GLU GLU B . n 
B 1 30  TYR 30  15  15  TYR TYR B . n 
B 1 31  HIS 31  16  16  HIS HIS B . n 
B 1 32  ILE 32  17  17  ILE ILE B . n 
B 1 33  ASP 33  18  18  ASP ASP B . n 
B 1 34  GLU 34  19  19  GLU GLU B . n 
B 1 35  GLU 35  20  20  GLU GLU B . n 
B 1 36  VAL 36  21  21  VAL VAL B . n 
B 1 37  GLY 37  22  22  GLY GLY B . n 
B 1 38  PHE 38  23  23  PHE PHE B . n 
B 1 39  ALA 39  24  24  ALA ALA B . n 
B 1 40  LEU 40  25  25  LEU LEU B . n 
B 1 41  PRO 41  26  26  PRO PRO B . n 
B 1 42  ASN 42  27  27  ASN ASN B . n 
B 1 43  PRO 43  28  28  PRO PRO B . n 
B 1 44  GLN 44  29  29  GLN GLN B . n 
B 1 45  GLU 45  30  30  GLU GLU B . n 
B 1 46  ASN 46  31  31  ASN ASN B . n 
B 1 47  LEU 47  32  32  LEU LEU B . n 
B 1 48  PRO 48  33  33  PRO PRO B . n 
B 1 49  ASP 49  34  34  ASP ASP B . n 
B 1 50  PHE 50  35  35  PHE PHE B . n 
B 1 51  TYR 51  36  36  TYR TYR B . n 
B 1 52  ASN 52  37  37  ASN ASN B . n 
B 1 53  ASP 53  38  38  ASP ASP B . n 
B 1 54  TRP 54  39  39  TRP TRP B . n 
B 1 55  MET 55  40  40  MET MET B . n 
B 1 56  PHE 56  41  41  PHE PHE B . n 
B 1 57  ILE 57  42  42  ILE ILE B . n 
B 1 58  ALA 58  43  43  ALA ALA B . n 
B 1 59  LYS 59  44  44  LYS LYS B . n 
B 1 60  HIS 60  45  45  HIS HIS B . n 
B 1 61  LEU 61  46  46  LEU LEU B . n 
B 1 62  PRO 62  47  47  PRO PRO B . n 
B 1 63  ASP 63  48  48  ASP ASP B . n 
B 1 64  LEU 64  49  49  LEU LEU B . n 
B 1 65  ILE 65  50  50  ILE ILE B . n 
B 1 66  GLU 66  51  51  GLU GLU B . n 
B 1 67  SER 67  52  52  SER SER B . n 
B 1 68  GLY 68  53  53  GLY GLY B . n 
B 1 69  GLN 69  54  54  GLN GLN B . n 
B 1 70  LEU 70  55  55  LEU LEU B . n 
B 1 71  ARG 71  56  56  ARG ARG B . n 
B 1 72  GLU 72  57  57  GLU GLU B . n 
B 1 73  ARG 73  58  58  ARG ARG B . n 
B 1 74  VAL 74  59  59  VAL VAL B . n 
B 1 75  GLU 75  60  60  GLU GLU B . n 
B 1 76  LYS 76  61  61  LYS LYS B . n 
B 1 77  LEU 77  62  62  LEU LEU B . n 
B 1 78  ASN 78  63  63  ASN ASN B . n 
B 1 79  MET 79  64  64  MET MET B . n 
B 1 80  LEU 80  65  65  LEU LEU B . n 
B 1 81  SER 81  66  66  SER SER B . n 
B 1 82  ILE 82  67  67  ILE ILE B . n 
B 1 83  ASP 83  68  68  ASP ASP B . n 
B 1 84  HIS 84  69  69  HIS HIS B . n 
B 1 85  LEU 85  70  70  LEU LEU B . n 
B 1 86  THR 86  71  71  THR THR B . n 
B 1 87  ASP 87  72  72  ASP ASP B . n 
B 1 88  HIS 88  73  73  HIS HIS B . n 
B 1 89  LYS 89  74  74  LYS LYS B . n 
B 1 90  SER 90  75  75  SER SER B . n 
B 1 91  GLN 91  76  76  GLN GLN B . n 
B 1 92  ARG 92  77  77  ARG ARG B . n 
B 1 93  LEU 93  78  78  LEU LEU B . n 
B 1 94  ALA 94  79  79  ALA ALA B . n 
B 1 95  ARG 95  80  80  ARG ARG B . n 
B 1 96  LEU 96  81  81  LEU LEU B . n 
B 1 97  VAL 97  82  82  VAL VAL B . n 
B 1 98  LEU 98  83  83  LEU LEU B . n 
B 1 99  GLY 99  84  84  GLY GLY B . n 
B 1 100 CYS 100 85  85  CYS CYS B . n 
B 1 101 ILE 101 86  86  ILE ILE B . n 
B 1 102 THR 102 87  87  THR THR B . n 
B 1 103 MET 103 88  88  MET MET B . n 
B 1 104 ALA 104 89  89  ALA ALA B . n 
B 1 105 TYR 105 90  90  TYR TYR B . n 
B 1 106 VAL 106 91  91  VAL VAL B . n 
B 1 107 TRP 107 92  92  TRP TRP B . n 
B 1 108 GLY 108 93  93  GLY GLY B . n 
B 1 109 LYS 109 94  94  LYS LYS B . n 
B 1 110 GLY 110 95  95  GLY GLY B . n 
B 1 111 HIS 111 96  96  HIS HIS B . n 
B 1 112 GLY 112 97  97  GLY GLY B . n 
B 1 113 ASP 113 98  98  ASP ASP B . n 
B 1 114 VAL 114 99  99  VAL VAL B . n 
B 1 115 ARG 115 100 100 ARG ARG B . n 
B 1 116 LYS 116 101 101 LYS LYS B . n 
B 1 117 VAL 117 102 102 VAL VAL B . n 
B 1 118 LEU 118 103 103 LEU LEU B . n 
B 1 119 PRO 119 104 104 PRO PRO B . n 
B 1 120 ARG 120 105 105 ARG ARG B . n 
B 1 121 ASN 121 106 106 ASN ASN B . n 
B 1 122 ILE 122 107 107 ILE ILE B . n 
B 1 123 ALA 123 108 108 ALA ALA B . n 
B 1 124 VAL 124 109 109 VAL VAL B . n 
B 1 125 PRO 125 110 110 PRO PRO B . n 
B 1 126 TYR 126 111 111 TYR TYR B . n 
B 1 127 CYS 127 112 112 CYS CYS B . n 
B 1 128 GLN 128 113 113 GLN GLN B . n 
B 1 129 LEU 129 114 114 LEU LEU B . n 
B 1 130 SER 130 115 115 SER SER B . n 
B 1 131 LYS 131 116 116 LYS LYS B . n 
B 1 132 LYS 132 117 117 LYS LYS B . n 
B 1 133 LEU 133 118 118 LEU LEU B . n 
B 1 134 GLU 134 119 119 GLU GLU B . n 
B 1 135 LEU 135 120 120 LEU LEU B . n 
B 1 136 PRO 136 121 121 PRO PRO B . n 
B 1 137 PRO 137 122 122 PRO PRO B . n 
B 1 138 ILE 138 123 123 ILE ILE B . n 
B 1 139 LEU 139 124 124 LEU LEU B . n 
B 1 140 VAL 140 125 125 VAL VAL B . n 
B 1 141 TYR 141 126 126 TYR TYR B . n 
B 1 142 ALA 142 127 127 ALA ALA B . n 
B 1 143 ASP 143 128 128 ASP ASP B . n 
B 1 144 CYS 144 129 129 CYS CYS B . n 
B 1 145 VAL 145 130 130 VAL VAL B . n 
B 1 146 LEU 146 131 131 LEU LEU B . n 
B 1 147 ALA 147 132 132 ALA ALA B . n 
B 1 148 ASN 148 133 133 ASN ASN B . n 
B 1 149 TRP 149 134 134 TRP TRP B . n 
B 1 150 LYS 150 135 135 LYS LYS B . n 
B 1 151 LYS 151 136 136 LYS LYS B . n 
B 1 152 LYS 152 137 137 LYS LYS B . n 
B 1 153 ASP 153 138 138 ASP ASP B . n 
B 1 154 PRO 154 139 139 PRO PRO B . n 
B 1 155 ASN 155 140 140 ASN ASN B . n 
B 1 156 LYS 156 141 141 LYS LYS B . n 
B 1 157 PRO 157 142 142 PRO PRO B . n 
B 1 158 LEU 158 143 143 LEU LEU B . n 
B 1 159 THR 159 144 144 THR THR B . n 
B 1 160 TYR 160 145 145 TYR TYR B . n 
B 1 161 GLU 161 146 146 GLU GLU B . n 
B 1 162 ASN 162 147 147 ASN ASN B . n 
B 1 163 MET 163 148 148 MET MET B . n 
B 1 164 ASP 164 149 149 ASP ASP B . n 
B 1 165 VAL 165 150 150 VAL VAL B . n 
B 1 166 LEU 166 151 151 LEU LEU B . n 
B 1 167 PHE 167 152 152 PHE PHE B . n 
B 1 168 SER 168 153 153 SER SER B . n 
B 1 169 PHE 169 154 154 PHE PHE B . n 
B 1 170 ARG 170 155 155 ARG ARG B . n 
B 1 171 ASP 171 156 156 ASP ASP B . n 
B 1 172 GLY 172 157 157 GLY GLY B . n 
B 1 173 ASP 173 158 158 ASP ASP B . n 
B 1 174 CYS 174 159 159 CYS CYS B . n 
B 1 175 SER 175 160 160 SER SER B . n 
B 1 176 LYS 176 161 161 LYS LYS B . n 
B 1 177 GLY 177 162 162 GLY GLY B . n 
B 1 178 PHE 178 163 163 PHE PHE B . n 
B 1 179 PHE 179 164 164 PHE PHE B . n 
B 1 180 LEU 180 165 165 LEU LEU B . n 
B 1 181 VAL 181 166 166 VAL VAL B . n 
B 1 182 SER 182 167 167 SER SER B . n 
B 1 183 LEU 183 168 168 LEU LEU B . n 
B 1 184 LEU 184 169 169 LEU LEU B . n 
B 1 185 VAL 185 170 170 VAL VAL B . n 
B 1 186 GLU 186 171 171 GLU GLU B . n 
B 1 187 ILE 187 172 172 ILE ILE B . n 
B 1 188 ALA 188 173 173 ALA ALA B . n 
B 1 189 ALA 189 174 174 ALA ALA B . n 
B 1 190 ALA 190 175 175 ALA ALA B . n 
B 1 191 SER 191 176 176 SER SER B . n 
B 1 192 ALA 192 177 177 ALA ALA B . n 
B 1 193 ILE 193 178 178 ILE ILE B . n 
B 1 194 LYS 194 179 179 LYS LYS B . n 
B 1 195 VAL 195 180 180 VAL VAL B . n 
B 1 196 ILE 196 181 181 ILE ILE B . n 
B 1 197 PRO 197 182 182 PRO PRO B . n 
B 1 198 THR 198 183 183 THR THR B . n 
B 1 199 VAL 199 184 184 VAL VAL B . n 
B 1 200 PHE 200 185 185 PHE PHE B . n 
B 1 201 LYS 201 186 186 LYS LYS B . n 
B 1 202 ALA 202 187 187 ALA ALA B . n 
B 1 203 MET 203 188 188 MET MET B . n 
B 1 204 GLN 204 189 189 GLN GLN B . n 
B 1 205 MET 205 190 190 MET MET B . n 
B 1 206 GLN 206 191 191 GLN GLN B . n 
B 1 207 GLU 207 192 192 GLU GLU B . n 
B 1 208 ARG 208 193 193 ARG ARG B . n 
B 1 209 ASP 209 194 194 ASP ASP B . n 
B 1 210 THR 210 195 195 THR THR B . n 
B 1 211 LEU 211 196 196 LEU LEU B . n 
B 1 212 LEU 212 197 197 LEU LEU B . n 
B 1 213 LYS 213 198 198 LYS LYS B . n 
B 1 214 ALA 214 199 199 ALA ALA B . n 
B 1 215 LEU 215 200 200 LEU LEU B . n 
B 1 216 LEU 216 201 201 LEU LEU B . n 
B 1 217 GLU 217 202 202 GLU GLU B . n 
B 1 218 ILE 218 203 203 ILE ILE B . n 
B 1 219 ALA 219 204 204 ALA ALA B . n 
B 1 220 SER 220 205 205 SER SER B . n 
B 1 221 CYS 221 206 206 CYS CYS B . n 
B 1 222 LEU 222 207 207 LEU LEU B . n 
B 1 223 GLU 223 208 208 GLU GLU B . n 
B 1 224 LYS 224 209 209 LYS LYS B . n 
B 1 225 ALA 225 210 210 ALA ALA B . n 
B 1 226 LEU 226 211 211 LEU LEU B . n 
B 1 227 GLN 227 212 212 GLN GLN B . n 
B 1 228 VAL 228 213 213 VAL VAL B . n 
B 1 229 PHE 229 214 214 PHE PHE B . n 
B 1 230 HIS 230 215 215 HIS HIS B . n 
B 1 231 GLN 231 216 216 GLN GLN B . n 
B 1 232 ILE 232 217 217 ILE ILE B . n 
B 1 233 HIS 233 218 218 HIS HIS B . n 
B 1 234 ASP 234 219 219 ASP ASP B . n 
B 1 235 HIS 235 220 220 HIS HIS B . n 
B 1 236 VAL 236 221 221 VAL VAL B . n 
B 1 237 ASN 237 222 222 ASN ASN B . n 
B 1 238 PRO 238 223 223 PRO PRO B . n 
B 1 239 LYS 239 224 224 LYS LYS B . n 
B 1 240 ALA 240 225 225 ALA ALA B . n 
B 1 241 PHE 241 226 226 PHE PHE B . n 
B 1 242 PHE 242 227 227 PHE PHE B . n 
B 1 243 SER 243 228 228 SER SER B . n 
B 1 244 VAL 244 229 229 VAL VAL B . n 
B 1 245 LEU 245 230 230 LEU LEU B . n 
B 1 246 ARG 246 231 231 ARG ARG B . n 
B 1 247 ILE 247 232 232 ILE ILE B . n 
B 1 248 TYR 248 233 233 TYR TYR B . n 
B 1 249 LEU 249 234 234 LEU LEU B . n 
B 1 250 SER 250 235 235 SER SER B . n 
B 1 251 GLY 251 236 236 GLY GLY B . n 
B 1 252 TRP 252 237 237 TRP TRP B . n 
B 1 253 LYS 253 238 238 LYS LYS B . n 
B 1 254 GLY 254 239 239 GLY GLY B . n 
B 1 255 ASN 255 240 240 ASN ASN B . n 
B 1 256 PRO 256 241 241 PRO PRO B . n 
B 1 257 GLN 257 242 242 GLN GLN B . n 
B 1 258 LEU 258 243 243 LEU LEU B . n 
B 1 259 SER 259 244 244 SER SER B . n 
B 1 260 ASP 260 245 245 ASP ASP B . n 
B 1 261 GLY 261 246 246 GLY GLY B . n 
B 1 262 LEU 262 247 247 LEU LEU B . n 
B 1 263 VAL 263 248 248 VAL VAL B . n 
B 1 264 TYR 264 249 249 TYR TYR B . n 
B 1 265 GLU 265 250 250 GLU GLU B . n 
B 1 266 GLY 266 251 251 GLY GLY B . n 
B 1 267 PHE 267 252 252 PHE PHE B . n 
B 1 268 TRP 268 253 253 TRP TRP B . n 
B 1 269 GLU 269 254 254 GLU GLU B . n 
B 1 270 ASP 270 255 255 ASP ASP B . n 
B 1 271 PRO 271 256 256 PRO PRO B . n 
B 1 272 LYS 272 257 257 LYS LYS B . n 
B 1 273 GLU 273 258 258 GLU GLU B . n 
B 1 274 PHE 274 259 259 PHE PHE B . n 
B 1 275 ALA 275 260 260 ALA ALA B . n 
B 1 276 GLY 276 261 261 GLY GLY B . n 
B 1 277 GLY 277 262 262 GLY GLY B . n 
B 1 278 SER 278 263 263 SER SER B . n 
B 1 279 ALA 279 264 264 ALA ALA B . n 
B 1 280 GLY 280 265 265 GLY GLY B . n 
B 1 281 GLN 281 266 266 GLN GLN B . n 
B 1 282 SER 282 267 267 SER SER B . n 
B 1 283 SER 283 268 268 SER SER B . n 
B 1 284 VAL 284 269 269 VAL VAL B . n 
B 1 285 PHE 285 270 270 PHE PHE B . n 
B 1 286 GLN 286 271 271 GLN GLN B . n 
B 1 287 CYS 287 272 272 CYS CYS B . n 
B 1 288 PHE 288 273 273 PHE PHE B . n 
B 1 289 ASP 289 274 274 ASP ASP B . n 
B 1 290 VAL 290 275 275 VAL VAL B . n 
B 1 291 LEU 291 276 276 LEU LEU B . n 
B 1 292 LEU 292 277 277 LEU LEU B . n 
B 1 293 GLY 293 278 278 GLY GLY B . n 
B 1 294 ILE 294 279 279 ILE ILE B . n 
B 1 295 GLN 295 280 280 GLN GLN B . n 
B 1 296 GLN 296 281 281 GLN GLN B . n 
B 1 297 THR 297 282 282 THR THR B . n 
B 1 298 ALA 298 283 283 ALA ALA B . n 
B 1 299 GLY 299 284 284 GLY GLY B . n 
B 1 300 GLY 300 285 285 GLY GLY B . n 
B 1 301 GLY 301 286 286 GLY GLY B . n 
B 1 302 HIS 302 287 287 HIS HIS B . n 
B 1 303 ALA 303 288 288 ALA ALA B . n 
B 1 304 ALA 304 289 289 ALA ALA B . n 
B 1 305 GLN 305 290 290 GLN GLN B . n 
B 1 306 PHE 306 291 291 PHE PHE B . n 
B 1 307 LEU 307 292 292 LEU LEU B . n 
B 1 308 GLN 308 293 293 GLN GLN B . n 
B 1 309 ASP 309 294 294 ASP ASP B . n 
B 1 310 MET 310 295 295 MET MET B . n 
B 1 311 ARG 311 296 296 ARG ARG B . n 
B 1 312 ARG 312 297 297 ARG ARG B . n 
B 1 313 TYR 313 298 298 TYR TYR B . n 
B 1 314 MET 314 299 299 MET MET B . n 
B 1 315 PRO 315 300 300 PRO PRO B . n 
B 1 316 PRO 316 301 301 PRO PRO B . n 
B 1 317 ALA 317 302 302 ALA ALA B . n 
B 1 318 HIS 318 303 303 HIS HIS B . n 
B 1 319 ARG 319 304 304 ARG ARG B . n 
B 1 320 ASN 320 305 305 ASN ASN B . n 
B 1 321 PHE 321 306 306 PHE PHE B . n 
B 1 322 LEU 322 307 307 LEU LEU B . n 
B 1 323 CYS 323 308 308 CYS CYS B . n 
B 1 324 SER 324 309 309 SER SER B . n 
B 1 325 LEU 325 310 310 LEU LEU B . n 
B 1 326 GLU 326 311 311 GLU GLU B . n 
B 1 327 SER 327 312 312 SER SER B . n 
B 1 328 ASN 328 313 313 ASN ASN B . n 
B 1 329 PRO 329 314 314 PRO PRO B . n 
B 1 330 SER 330 315 315 SER SER B . n 
B 1 331 VAL 331 316 316 VAL VAL B . n 
B 1 332 ARG 332 317 317 ARG ARG B . n 
B 1 333 GLU 333 318 318 GLU GLU B . n 
B 1 334 PHE 334 319 319 PHE PHE B . n 
B 1 335 VAL 335 320 320 VAL VAL B . n 
B 1 336 LEU 336 321 321 LEU LEU B . n 
B 1 337 SER 337 322 322 SER SER B . n 
B 1 338 LYS 338 323 323 LYS LYS B . n 
B 1 339 GLY 339 324 324 GLY GLY B . n 
B 1 340 ASP 340 325 325 ASP ASP B . n 
B 1 341 ALA 341 326 326 ALA ALA B . n 
B 1 342 GLY 342 327 327 GLY GLY B . n 
B 1 343 LEU 343 328 328 LEU LEU B . n 
B 1 344 ARG 344 329 329 ARG ARG B . n 
B 1 345 GLU 345 330 330 GLU GLU B . n 
B 1 346 ALA 346 331 331 ALA ALA B . n 
B 1 347 TYR 347 332 332 TYR TYR B . n 
B 1 348 ASP 348 333 333 ASP ASP B . n 
B 1 349 ALA 349 334 334 ALA ALA B . n 
B 1 350 CYS 350 335 335 CYS CYS B . n 
B 1 351 VAL 351 336 336 VAL VAL B . n 
B 1 352 LYS 352 337 337 LYS LYS B . n 
B 1 353 ALA 353 338 338 ALA ALA B . n 
B 1 354 LEU 354 339 339 LEU LEU B . n 
B 1 355 VAL 355 340 340 VAL VAL B . n 
B 1 356 SER 356 341 341 SER SER B . n 
B 1 357 LEU 357 342 342 LEU LEU B . n 
B 1 358 ARG 358 343 343 ARG ARG B . n 
B 1 359 SER 359 344 344 SER SER B . n 
B 1 360 TYR 360 345 345 TYR TYR B . n 
B 1 361 HIS 361 346 346 HIS HIS B . n 
B 1 362 LEU 362 347 347 LEU LEU B . n 
B 1 363 GLN 363 348 348 GLN GLN B . n 
B 1 364 ILE 364 349 349 ILE ILE B . n 
B 1 365 VAL 365 350 350 VAL VAL B . n 
B 1 366 THR 366 351 351 THR THR B . n 
B 1 367 LYS 367 352 352 LYS LYS B . n 
B 1 368 TYR 368 353 353 TYR TYR B . n 
B 1 369 ILE 369 354 354 ILE ILE B . n 
B 1 370 LEU 370 355 355 LEU LEU B . n 
B 1 371 ILE 371 356 356 ILE ILE B . n 
B 1 372 PRO 372 357 357 PRO PRO B . n 
B 1 373 ALA 373 358 358 ALA ALA B . n 
B 1 374 SER 374 359 359 SER SER B . n 
B 1 375 GLN 375 360 360 GLN GLN B . n 
B 1 376 GLN 376 361 361 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 ?   ?   ?   B . n 
B 1 388 LYS 388 373 ?   ?   ?   B . n 
B 1 389 LEU 389 374 ?   ?   ?   B . n 
B 1 390 GLU 390 375 ?   ?   ?   B . n 
B 1 391 ALA 391 376 ?   ?   ?   B . n 
B 1 392 LYS 392 377 ?   ?   ?   B . n 
B 1 393 GLY 393 378 ?   ?   ?   B . n 
B 1 394 THR 394 379 ?   ?   ?   B . n 
B 1 395 GLY 395 380 380 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 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1H6U 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1H6U 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 HEM   1   501 501 HEM   HEM A . 
D 3 A1H6U 1   502 2   A1H6U LIG A . 
E 2 HEM   1   501 501 HEM   HEM B . 
F 3 A1H6U 1   502 1   A1H6U LIG B . 
G 4 HOH   1   601 121 HOH   HOH A . 
G 4 HOH   2   602 177 HOH   HOH A . 
G 4 HOH   3   603 101 HOH   HOH A . 
G 4 HOH   4   604 179 HOH   HOH A . 
G 4 HOH   5   605 183 HOH   HOH A . 
G 4 HOH   6   606 11  HOH   HOH A . 
G 4 HOH   7   607 24  HOH   HOH A . 
G 4 HOH   8   608 92  HOH   HOH A . 
G 4 HOH   9   609 131 HOH   HOH A . 
G 4 HOH   10  610 5   HOH   HOH A . 
G 4 HOH   11  611 87  HOH   HOH A . 
G 4 HOH   12  612 8   HOH   HOH A . 
G 4 HOH   13  613 119 HOH   HOH A . 
G 4 HOH   14  614 26  HOH   HOH A . 
G 4 HOH   15  615 78  HOH   HOH A . 
G 4 HOH   16  616 74  HOH   HOH A . 
G 4 HOH   17  617 39  HOH   HOH A . 
G 4 HOH   18  618 18  HOH   HOH A . 
G 4 HOH   19  619 6   HOH   HOH A . 
G 4 HOH   20  620 12  HOH   HOH A . 
G 4 HOH   21  621 190 HOH   HOH A . 
G 4 HOH   22  622 50  HOH   HOH A . 
G 4 HOH   23  623 90  HOH   HOH A . 
G 4 HOH   24  624 71  HOH   HOH A . 
G 4 HOH   25  625 79  HOH   HOH A . 
G 4 HOH   26  626 86  HOH   HOH A . 
G 4 HOH   27  627 13  HOH   HOH A . 
G 4 HOH   28  628 89  HOH   HOH A . 
G 4 HOH   29  629 100 HOH   HOH A . 
G 4 HOH   30  630 106 HOH   HOH A . 
G 4 HOH   31  631 186 HOH   HOH A . 
G 4 HOH   32  632 47  HOH   HOH A . 
G 4 HOH   33  633 60  HOH   HOH A . 
G 4 HOH   34  634 107 HOH   HOH A . 
G 4 HOH   35  635 97  HOH   HOH A . 
G 4 HOH   36  636 80  HOH   HOH A . 
G 4 HOH   37  637 81  HOH   HOH A . 
G 4 HOH   38  638 117 HOH   HOH A . 
G 4 HOH   39  639 14  HOH   HOH A . 
G 4 HOH   40  640 147 HOH   HOH A . 
G 4 HOH   41  641 168 HOH   HOH A . 
G 4 HOH   42  642 187 HOH   HOH A . 
G 4 HOH   43  643 98  HOH   HOH A . 
G 4 HOH   44  644 27  HOH   HOH A . 
G 4 HOH   45  645 62  HOH   HOH A . 
G 4 HOH   46  646 69  HOH   HOH A . 
G 4 HOH   47  647 173 HOH   HOH A . 
G 4 HOH   48  648 114 HOH   HOH A . 
G 4 HOH   49  649 111 HOH   HOH A . 
G 4 HOH   50  650 165 HOH   HOH A . 
G 4 HOH   51  651 116 HOH   HOH A . 
G 4 HOH   52  652 95  HOH   HOH A . 
G 4 HOH   53  653 166 HOH   HOH A . 
G 4 HOH   54  654 72  HOH   HOH A . 
G 4 HOH   55  655 16  HOH   HOH A . 
G 4 HOH   56  656 104 HOH   HOH A . 
G 4 HOH   57  657 9   HOH   HOH A . 
G 4 HOH   58  658 115 HOH   HOH A . 
G 4 HOH   59  659 52  HOH   HOH A . 
G 4 HOH   60  660 25  HOH   HOH A . 
G 4 HOH   61  661 82  HOH   HOH A . 
G 4 HOH   62  662 126 HOH   HOH A . 
G 4 HOH   63  663 137 HOH   HOH A . 
G 4 HOH   64  664 31  HOH   HOH A . 
G 4 HOH   65  665 112 HOH   HOH A . 
G 4 HOH   66  666 19  HOH   HOH A . 
G 4 HOH   67  667 34  HOH   HOH A . 
G 4 HOH   68  668 99  HOH   HOH A . 
G 4 HOH   69  669 105 HOH   HOH A . 
G 4 HOH   70  670 152 HOH   HOH A . 
G 4 HOH   71  671 36  HOH   HOH A . 
G 4 HOH   72  672 63  HOH   HOH A . 
G 4 HOH   73  673 65  HOH   HOH A . 
G 4 HOH   74  674 139 HOH   HOH A . 
G 4 HOH   75  675 83  HOH   HOH A . 
G 4 HOH   76  676 3   HOH   HOH A . 
G 4 HOH   77  677 75  HOH   HOH A . 
G 4 HOH   78  678 143 HOH   HOH A . 
G 4 HOH   79  679 22  HOH   HOH A . 
G 4 HOH   80  680 56  HOH   HOH A . 
G 4 HOH   81  681 191 HOH   HOH A . 
G 4 HOH   82  682 181 HOH   HOH A . 
G 4 HOH   83  683 61  HOH   HOH A . 
G 4 HOH   84  684 125 HOH   HOH A . 
G 4 HOH   85  685 33  HOH   HOH A . 
G 4 HOH   86  686 64  HOH   HOH A . 
G 4 HOH   87  687 148 HOH   HOH A . 
G 4 HOH   88  688 189 HOH   HOH A . 
G 4 HOH   89  689 185 HOH   HOH A . 
G 4 HOH   90  690 110 HOH   HOH A . 
G 4 HOH   91  691 108 HOH   HOH A . 
G 4 HOH   92  692 123 HOH   HOH A . 
G 4 HOH   93  693 42  HOH   HOH A . 
G 4 HOH   94  694 88  HOH   HOH A . 
G 4 HOH   95  695 178 HOH   HOH A . 
G 4 HOH   96  696 113 HOH   HOH A . 
G 4 HOH   97  697 154 HOH   HOH A . 
G 4 HOH   98  698 124 HOH   HOH A . 
G 4 HOH   99  699 149 HOH   HOH A . 
G 4 HOH   100 700 150 HOH   HOH A . 
G 4 HOH   101 701 1   HOH   HOH A . 
G 4 HOH   102 702 103 HOH   HOH A . 
G 4 HOH   103 703 146 HOH   HOH A . 
G 4 HOH   104 704 44  HOH   HOH A . 
G 4 HOH   105 705 138 HOH   HOH A . 
G 4 HOH   106 706 153 HOH   HOH A . 
G 4 HOH   107 707 76  HOH   HOH A . 
H 4 HOH   1   601 20  HOH   HOH B . 
H 4 HOH   2   602 132 HOH   HOH B . 
H 4 HOH   3   603 160 HOH   HOH B . 
H 4 HOH   4   604 91  HOH   HOH B . 
H 4 HOH   5   605 128 HOH   HOH B . 
H 4 HOH   6   606 170 HOH   HOH B . 
H 4 HOH   7   607 66  HOH   HOH B . 
H 4 HOH   8   608 21  HOH   HOH B . 
H 4 HOH   9   609 120 HOH   HOH B . 
H 4 HOH   10  610 32  HOH   HOH B . 
H 4 HOH   11  611 96  HOH   HOH B . 
H 4 HOH   12  612 164 HOH   HOH B . 
H 4 HOH   13  613 41  HOH   HOH B . 
H 4 HOH   14  614 144 HOH   HOH B . 
H 4 HOH   15  615 59  HOH   HOH B . 
H 4 HOH   16  616 49  HOH   HOH B . 
H 4 HOH   17  617 118 HOH   HOH B . 
H 4 HOH   18  618 28  HOH   HOH B . 
H 4 HOH   19  619 35  HOH   HOH B . 
H 4 HOH   20  620 38  HOH   HOH B . 
H 4 HOH   21  621 102 HOH   HOH B . 
H 4 HOH   22  622 58  HOH   HOH B . 
H 4 HOH   23  623 159 HOH   HOH B . 
H 4 HOH   24  624 169 HOH   HOH B . 
H 4 HOH   25  625 48  HOH   HOH B . 
H 4 HOH   26  626 162 HOH   HOH B . 
H 4 HOH   27  627 155 HOH   HOH B . 
H 4 HOH   28  628 46  HOH   HOH B . 
H 4 HOH   29  629 94  HOH   HOH B . 
H 4 HOH   30  630 174 HOH   HOH B . 
H 4 HOH   31  631 180 HOH   HOH B . 
H 4 HOH   32  632 136 HOH   HOH B . 
H 4 HOH   33  633 171 HOH   HOH B . 
H 4 HOH   34  634 84  HOH   HOH B . 
H 4 HOH   35  635 17  HOH   HOH B . 
H 4 HOH   36  636 158 HOH   HOH B . 
H 4 HOH   37  637 70  HOH   HOH B . 
H 4 HOH   38  638 133 HOH   HOH B . 
H 4 HOH   39  639 129 HOH   HOH B . 
H 4 HOH   40  640 68  HOH   HOH B . 
H 4 HOH   41  641 67  HOH   HOH B . 
H 4 HOH   42  642 10  HOH   HOH B . 
H 4 HOH   43  643 51  HOH   HOH B . 
H 4 HOH   44  644 93  HOH   HOH B . 
H 4 HOH   45  645 135 HOH   HOH B . 
H 4 HOH   46  646 182 HOH   HOH B . 
H 4 HOH   47  647 188 HOH   HOH B . 
H 4 HOH   48  648 122 HOH   HOH B . 
H 4 HOH   49  649 156 HOH   HOH B . 
H 4 HOH   50  650 127 HOH   HOH B . 
H 4 HOH   51  651 172 HOH   HOH B . 
H 4 HOH   52  652 55  HOH   HOH B . 
H 4 HOH   53  653 15  HOH   HOH B . 
H 4 HOH   54  654 161 HOH   HOH B . 
H 4 HOH   55  655 109 HOH   HOH B . 
H 4 HOH   56  656 151 HOH   HOH B . 
H 4 HOH   57  657 130 HOH   HOH B . 
H 4 HOH   58  658 176 HOH   HOH B . 
H 4 HOH   59  659 23  HOH   HOH B . 
H 4 HOH   60  660 163 HOH   HOH B . 
H 4 HOH   61  661 157 HOH   HOH B . 
H 4 HOH   62  662 141 HOH   HOH B . 
H 4 HOH   63  663 73  HOH   HOH B . 
H 4 HOH   64  664 40  HOH   HOH B . 
H 4 HOH   65  665 57  HOH   HOH B . 
H 4 HOH   66  666 145 HOH   HOH B . 
H 4 HOH   67  667 29  HOH   HOH B . 
H 4 HOH   68  668 4   HOH   HOH B . 
H 4 HOH   69  669 7   HOH   HOH B . 
H 4 HOH   70  670 142 HOH   HOH B . 
H 4 HOH   71  671 43  HOH   HOH B . 
H 4 HOH   72  672 30  HOH   HOH B . 
H 4 HOH   73  673 77  HOH   HOH B . 
H 4 HOH   74  674 184 HOH   HOH B . 
H 4 HOH   75  675 140 HOH   HOH B . 
H 4 HOH   76  676 54  HOH   HOH B . 
H 4 HOH   77  677 45  HOH   HOH B . 
H 4 HOH   78  678 175 HOH   HOH B . 
H 4 HOH   79  679 167 HOH   HOH B . 
H 4 HOH   80  680 134 HOH   HOH B . 
H 4 HOH   81  681 53  HOH   HOH B . 
H 4 HOH   82  682 85  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 LYS 13  ? CG  ? A LYS 28  CG  
2  1 Y 1 A LYS 13  ? CD  ? A LYS 28  CD  
3  1 Y 1 A LYS 13  ? CE  ? A LYS 28  CE  
4  1 Y 1 A LYS 13  ? NZ  ? A LYS 28  NZ  
5  1 Y 1 A GLU 14  ? CD  ? A GLU 29  CD  
6  1 Y 1 A GLU 14  ? OE1 ? A GLU 29  OE1 
7  1 Y 1 A GLU 14  ? OE2 ? A GLU 29  OE2 
8  1 Y 1 A GLU 19  ? CG  ? A GLU 34  CG  
9  1 Y 1 A GLU 19  ? CD  ? A GLU 34  CD  
10 1 Y 1 A GLU 19  ? OE1 ? A GLU 34  OE1 
11 1 Y 1 A GLU 19  ? OE2 ? A GLU 34  OE2 
12 1 Y 1 A LYS 116 ? NZ  ? A LYS 131 NZ  
13 1 Y 1 A LYS 186 ? CE  ? A LYS 201 CE  
14 1 Y 1 A LYS 186 ? NZ  ? A LYS 201 NZ  
15 1 Y 1 A LYS 224 ? CD  ? A LYS 239 CD  
16 1 Y 1 A LYS 224 ? CE  ? A LYS 239 CE  
17 1 Y 1 A LYS 224 ? NZ  ? A LYS 239 NZ  
18 1 Y 1 A GLU 318 ? CD  ? A GLU 333 CD  
19 1 Y 1 A GLU 318 ? OE1 ? A GLU 333 OE1 
20 1 Y 1 A GLU 318 ? OE2 ? A GLU 333 OE2 
21 1 Y 1 A LYS 337 ? CD  ? A LYS 352 CD  
22 1 Y 1 A LYS 337 ? CE  ? A LYS 352 CE  
23 1 Y 1 A LYS 337 ? NZ  ? A LYS 352 NZ  
24 1 Y 1 A GLN 361 ? CD  ? A GLN 376 CD  
25 1 Y 1 A GLN 361 ? OE1 ? A GLN 376 OE1 
26 1 Y 1 A GLN 361 ? NE2 ? A GLN 376 NE2 
27 1 Y 1 B THR 10  ? OG1 ? B THR 25  OG1 
28 1 Y 1 B THR 10  ? CG2 ? B THR 25  CG2 
29 1 Y 1 B LYS 13  ? CD  ? B LYS 28  CD  
30 1 Y 1 B LYS 13  ? CE  ? B LYS 28  CE  
31 1 Y 1 B LYS 13  ? NZ  ? B LYS 28  NZ  
32 1 Y 1 B LYS 44  ? CE  ? B LYS 59  CE  
33 1 Y 1 B LYS 44  ? NZ  ? B LYS 59  NZ  
34 1 Y 1 B LYS 61  ? CG  ? B LYS 76  CG  
35 1 Y 1 B LYS 61  ? CD  ? B LYS 76  CD  
36 1 Y 1 B LYS 61  ? CE  ? B LYS 76  CE  
37 1 Y 1 B LYS 61  ? NZ  ? B LYS 76  NZ  
38 1 Y 1 B LYS 116 ? CE  ? B LYS 131 CE  
39 1 Y 1 B LYS 116 ? NZ  ? B LYS 131 NZ  
40 1 Y 1 B LYS 117 ? CE  ? B LYS 132 CE  
41 1 Y 1 B LYS 117 ? NZ  ? B LYS 132 NZ  
42 1 Y 1 B LYS 135 ? CE  ? B LYS 150 CE  
43 1 Y 1 B LYS 135 ? NZ  ? B LYS 150 NZ  
44 1 Y 1 B LYS 137 ? NZ  ? B LYS 152 NZ  
45 1 Y 1 B LYS 141 ? CE  ? B LYS 156 CE  
46 1 Y 1 B LYS 141 ? NZ  ? B LYS 156 NZ  
47 1 Y 1 B LYS 186 ? CG  ? B LYS 201 CG  
48 1 Y 1 B LYS 186 ? CD  ? B LYS 201 CD  
49 1 Y 1 B LYS 186 ? CE  ? B LYS 201 CE  
50 1 Y 1 B LYS 186 ? NZ  ? B LYS 201 NZ  
51 1 Y 1 B GLN 189 ? CD  ? B GLN 204 CD  
52 1 Y 1 B GLN 189 ? OE1 ? B GLN 204 OE1 
53 1 Y 1 B GLN 189 ? NE2 ? B GLN 204 NE2 
54 1 Y 1 B LYS 198 ? CE  ? B LYS 213 CE  
55 1 Y 1 B LYS 198 ? NZ  ? B LYS 213 NZ  
56 1 Y 1 B LYS 224 ? CG  ? B LYS 239 CG  
57 1 Y 1 B LYS 224 ? CD  ? B LYS 239 CD  
58 1 Y 1 B LYS 224 ? CE  ? B LYS 239 CE  
59 1 Y 1 B LYS 224 ? NZ  ? B LYS 239 NZ  
60 1 Y 1 B LYS 238 ? NZ  ? B LYS 253 NZ  
61 1 Y 1 B GLU 254 ? CG  ? B GLU 269 CG  
62 1 Y 1 B GLU 254 ? CD  ? B GLU 269 CD  
63 1 Y 1 B GLU 254 ? OE1 ? B GLU 269 OE1 
64 1 Y 1 B GLU 254 ? OE2 ? B GLU 269 OE2 
65 1 Y 1 B LYS 257 ? CD  ? B LYS 272 CD  
66 1 Y 1 B LYS 257 ? CE  ? B LYS 272 CE  
67 1 Y 1 B LYS 257 ? NZ  ? B LYS 272 NZ  
68 1 Y 1 B ARG 297 ? NE  ? B ARG 312 NE  
69 1 Y 1 B ARG 297 ? CZ  ? B ARG 312 CZ  
70 1 Y 1 B ARG 297 ? NH1 ? B ARG 312 NH1 
71 1 Y 1 B ARG 297 ? NH2 ? B ARG 312 NH2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? BUSTER   ? ? ? 2.11.8 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .      2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE   ? ? ? .      3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .      4 
# 
_cell.angle_alpha                  90 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EW0 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     85.05 
_cell.length_a_esd                 ? 
_cell.length_b                     92.891 
_cell.length_b_esd                 ? 
_cell.length_c                     129.357 
_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                         9EW0 
_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                   9EW0 
_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             2.71 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.66 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '10% w/v PEG 4000, 20% v/v glycerol, 0.1 M MOPS/HEPES-Na pH 7.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 2M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2016-04-15 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.00 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SLS BEAMLINE X06DA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.00 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06DA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9EW0 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.80 
_reflns.d_resolution_low                               46.5 
_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                                     95350 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                .20 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   .99 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.80 
_reflns_shell.d_res_low                                     1.91 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.39 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             14907 
_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                               6.1 
_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                                  .134 
_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]                            -0.8427 
_refine.aniso_B[1][2]                            0 
_refine.aniso_B[1][3]                            0 
_refine.aniso_B[2][2]                            0.5771 
_refine.aniso_B[2][3]                            0 
_refine.aniso_B[3][3]                            0.2657 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               39.02 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.951 
_refine.correlation_coeff_Fo_to_Fc_free          0.938 
_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                                 9EW0 
_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                            1.8 
_refine.ls_d_res_low                             46.45 
_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                     95155 
_refine.ls_number_reflns_R_free                  4901 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.7 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2509 
_refine.ls_R_factor_R_free                       0.2783 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2494 
_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   0.128 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.126 
_refine.pdbx_overall_SU_R_Blow_DPI               0.131 
_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             0.133 
_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                        9EW0 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.35 
_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                       1.8 
_refine_hist.d_res_low                        46.45 
_refine_hist.number_atoms_solvent             189 
_refine_hist.number_atoms_total               6180 
_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        5871 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         120 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.009 ? 6191 ? t_bond_d                  2  HARMONIC     
'X-RAY DIFFRACTION' ? 0.95  ? 8410 ? t_angle_deg               2  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 2153 ? t_dihedral_angle_d        2  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? 1105 ? t_gen_planes              5  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 6191 ? t_it                      10 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 768  ? t_chiral_improper_torsion 5  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? 5318 ? t_ideal_dist_contact      4  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? 2.96  ? ?    ? t_omega_torsion           ?  ?            
'X-RAY DIFFRACTION' ? 17.23 ? ?    ? t_other_torsion           ?  ?            
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.8 
_refine_ls_shell.d_res_low                        1.81 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                1904 
_refine_ls_shell.number_reflns_R_free             105 
_refine_ls_shell.number_reflns_R_work             ? 
_refine_ls_shell.percent_reflns_obs               91.2 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     0.4955 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.4938 
_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                  0.5219 
# 
_struct.entry_id                     9EW0 
_struct.title                        'Holo IDO with a bound inhibitor' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9EW0 
_struct_keywords.text            'Inhibitor, heme, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    I23O1_HUMAN 
_struct_ref.pdbx_db_accession          P14902 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;WTISKEYHIDEEVGFALPNPQENLPDFYNDWMFIAKHLPDLIESGQLRERVEKLNMLSIDHLTDHKSQRLARLVLGCITM
AYVWGKGHGDVRKVLPRNIAVPYCQLSKKLELPPILVYADCVLANWKKKDPNKPLTYENMDVLFSFRDGDCSKGFFLVSL
LVEIAAASAIKVIPTVFKAMQMQERDTLLKALLEIASCLEKALQVFHQIHDHVNPKAFFSVLRIYLSGWKGNPQLSDGLV
YEGFWEDPKEFAGGSAGQSSVFQCFDVLLGIQQTAGGGHAAQFLQDMRRYMPPAHRNFLCSLESNPSVREFVLSKGDAGL
REAYDACVKALVSLRSYHLQIVTKYILIPASQQPKENKTSEDPSKLEAKGTGGTDLMNFLKTVRSTTEKSLLKEG
;
_struct_ref.pdbx_align_begin           9 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9EW0 A 24 ? 418 ? P14902 9 ? 403 ? 9 403 
2 1 9EW0 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 9EW0 MET A 1  ? UNP P14902 ? ? 'initiating methionine' -14 1  
1 9EW0 GLY A 2  ? UNP P14902 ? ? 'expression tag'        -13 2  
1 9EW0 SER A 3  ? UNP P14902 ? ? 'expression tag'        -12 3  
1 9EW0 SER A 4  ? UNP P14902 ? ? 'expression tag'        -11 4  
1 9EW0 HIS A 5  ? UNP P14902 ? ? 'expression tag'        -10 5  
1 9EW0 HIS A 6  ? UNP P14902 ? ? 'expression tag'        -9  6  
1 9EW0 HIS A 7  ? UNP P14902 ? ? 'expression tag'        -8  7  
1 9EW0 HIS A 8  ? UNP P14902 ? ? 'expression tag'        -7  8  
1 9EW0 HIS A 9  ? UNP P14902 ? ? 'expression tag'        -6  9  
1 9EW0 HIS A 10 ? UNP P14902 ? ? 'expression tag'        -5  10 
1 9EW0 SER A 11 ? UNP P14902 ? ? 'expression tag'        -4  11 
1 9EW0 ALA A 12 ? UNP P14902 ? ? 'expression tag'        -3  12 
1 9EW0 ALA A 13 ? UNP P14902 ? ? 'expression tag'        -2  13 
1 9EW0 LEU A 14 ? UNP P14902 ? ? 'expression tag'        -1  14 
1 9EW0 GLU A 15 ? UNP P14902 ? ? 'expression tag'        0   15 
1 9EW0 VAL A 16 ? UNP P14902 ? ? 'expression tag'        1   16 
1 9EW0 LEU A 17 ? UNP P14902 ? ? 'expression tag'        2   17 
1 9EW0 PHE A 18 ? UNP P14902 ? ? 'expression tag'        3   18 
1 9EW0 GLN A 19 ? UNP P14902 ? ? 'expression tag'        4   19 
1 9EW0 GLY A 20 ? UNP P14902 ? ? 'expression tag'        5   20 
1 9EW0 PRO A 21 ? UNP P14902 ? ? 'expression tag'        6   21 
1 9EW0 HIS A 22 ? UNP P14902 ? ? 'expression tag'        7   22 
1 9EW0 MET A 23 ? UNP P14902 ? ? 'expression tag'        8   23 
2 9EW0 MET B 1  ? UNP P14902 ? ? 'initiating methionine' -14 24 
2 9EW0 GLY B 2  ? UNP P14902 ? ? 'expression tag'        -13 25 
2 9EW0 SER B 3  ? UNP P14902 ? ? 'expression tag'        -12 26 
2 9EW0 SER B 4  ? UNP P14902 ? ? 'expression tag'        -11 27 
2 9EW0 HIS B 5  ? UNP P14902 ? ? 'expression tag'        -10 28 
2 9EW0 HIS B 6  ? UNP P14902 ? ? 'expression tag'        -9  29 
2 9EW0 HIS B 7  ? UNP P14902 ? ? 'expression tag'        -8  30 
2 9EW0 HIS B 8  ? UNP P14902 ? ? 'expression tag'        -7  31 
2 9EW0 HIS B 9  ? UNP P14902 ? ? 'expression tag'        -6  32 
2 9EW0 HIS B 10 ? UNP P14902 ? ? 'expression tag'        -5  33 
2 9EW0 SER B 11 ? UNP P14902 ? ? 'expression tag'        -4  34 
2 9EW0 ALA B 12 ? UNP P14902 ? ? 'expression tag'        -3  35 
2 9EW0 ALA B 13 ? UNP P14902 ? ? 'expression tag'        -2  36 
2 9EW0 LEU B 14 ? UNP P14902 ? ? 'expression tag'        -1  37 
2 9EW0 GLU B 15 ? UNP P14902 ? ? 'expression tag'        0   38 
2 9EW0 VAL B 16 ? UNP P14902 ? ? 'expression tag'        1   39 
2 9EW0 LEU B 17 ? UNP P14902 ? ? 'expression tag'        2   40 
2 9EW0 PHE B 18 ? UNP P14902 ? ? 'expression tag'        3   41 
2 9EW0 GLN B 19 ? UNP P14902 ? ? 'expression tag'        4   42 
2 9EW0 GLY B 20 ? UNP P14902 ? ? 'expression tag'        5   43 
2 9EW0 PRO B 21 ? UNP P14902 ? ? 'expression tag'        6   44 
2 9EW0 HIS B 22 ? UNP P14902 ? ? 'expression tag'        7   45 
2 9EW0 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,G 
2 1 B,E,F,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 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  ? LYS A 76  ? GLN A 54  LYS A 61  1 ? 8  
HELX_P HELX_P6  AA6 ASP A 87  ? GLY A 108 ? ASP A 72  GLY A 93  1 ? 22 
HELX_P HELX_P7  AA7 PRO A 119 ? GLU A 134 ? PRO A 104 GLU A 119 1 ? 16 
HELX_P HELX_P8  AA8 VAL A 140 ? VAL A 145 ? VAL A 125 VAL A 130 1 ? 6  
HELX_P HELX_P9  AA9 THR A 159 ? GLU A 161 ? THR A 144 GLU A 146 5 ? 3  
HELX_P HELX_P10 AB1 CYS A 174 ? LYS A 194 ? CYS A 159 LYS A 179 1 ? 21 
HELX_P HELX_P11 AB2 VAL A 195 ? MET A 205 ? VAL A 180 MET A 190 1 ? 11 
HELX_P HELX_P12 AB3 GLU A 207 ? HIS A 230 ? GLU A 192 HIS A 215 1 ? 24 
HELX_P HELX_P13 AB4 GLN A 231 ? VAL A 236 ? GLN A 216 VAL A 221 1 ? 6  
HELX_P HELX_P14 AB5 ASN A 237 ? VAL A 244 ? ASN A 222 VAL A 229 1 ? 8  
HELX_P HELX_P15 AB6 VAL A 244 ? SER A 250 ? VAL A 229 SER A 235 1 ? 7  
HELX_P HELX_P16 AB7 ASN A 255 ? SER A 259 ? ASN A 240 SER A 244 5 ? 5  
HELX_P HELX_P17 AB8 SER A 278 ? SER A 282 ? SER A 263 SER A 267 5 ? 5  
HELX_P HELX_P18 AB9 PHE A 285 ? LEU A 292 ? PHE A 270 LEU A 277 1 ? 8  
HELX_P HELX_P19 AC1 GLY A 301 ? ARG A 311 ? GLY A 286 ARG A 296 1 ? 11 
HELX_P HELX_P20 AC2 ARG A 312 ? MET A 314 ? ARG A 297 MET A 299 5 ? 3  
HELX_P HELX_P21 AC3 PRO A 315 ? ASN A 328 ? PRO A 300 ASN A 313 1 ? 14 
HELX_P HELX_P22 AC4 SER A 330 ? SER A 337 ? SER A 315 SER A 322 1 ? 8  
HELX_P HELX_P23 AC5 ASP A 340 ? ILE A 369 ? ASP A 325 ILE A 354 1 ? 30 
HELX_P HELX_P24 AC6 ILE A 369 ? GLN A 375 ? ILE A 354 GLN A 360 1 ? 7  
HELX_P HELX_P25 AC7 THR A 397 ? LYS A 412 ? THR A 382 LYS A 397 1 ? 16 
HELX_P HELX_P26 AC8 SER B 27  ? HIS B 31  ? SER B 12  HIS B 16  5 ? 5  
HELX_P HELX_P27 AC9 PRO B 48  ? PHE B 50  ? PRO B 33  PHE B 35  5 ? 3  
HELX_P HELX_P28 AD1 TYR B 51  ? HIS B 60  ? TYR B 36  HIS B 45  1 ? 10 
HELX_P HELX_P29 AD2 HIS B 60  ? SER B 67  ? HIS B 45  SER B 52  1 ? 8  
HELX_P HELX_P30 AD3 GLN B 69  ? LYS B 76  ? GLN B 54  LYS B 61  1 ? 8  
HELX_P HELX_P31 AD4 ASP B 87  ? GLY B 108 ? ASP B 72  GLY B 93  1 ? 22 
HELX_P HELX_P32 AD5 PRO B 119 ? GLU B 134 ? PRO B 104 GLU B 119 1 ? 16 
HELX_P HELX_P33 AD6 VAL B 140 ? VAL B 145 ? VAL B 125 VAL B 130 1 ? 6  
HELX_P HELX_P34 AD7 THR B 159 ? GLU B 161 ? THR B 144 GLU B 146 5 ? 3  
HELX_P HELX_P35 AD8 CYS B 174 ? LYS B 194 ? CYS B 159 LYS B 179 1 ? 21 
HELX_P HELX_P36 AD9 VAL B 195 ? MET B 205 ? VAL B 180 MET B 190 1 ? 11 
HELX_P HELX_P37 AE1 GLU B 207 ? HIS B 230 ? GLU B 192 HIS B 215 1 ? 24 
HELX_P HELX_P38 AE2 GLN B 231 ? VAL B 236 ? GLN B 216 VAL B 221 1 ? 6  
HELX_P HELX_P39 AE3 ASN B 237 ? VAL B 244 ? ASN B 222 VAL B 229 1 ? 8  
HELX_P HELX_P40 AE4 VAL B 244 ? SER B 250 ? VAL B 229 SER B 235 1 ? 7  
HELX_P HELX_P41 AE5 ASN B 255 ? SER B 259 ? ASN B 240 SER B 244 5 ? 5  
HELX_P HELX_P42 AE6 SER B 278 ? SER B 282 ? SER B 263 SER B 267 5 ? 5  
HELX_P HELX_P43 AE7 PHE B 285 ? LEU B 292 ? PHE B 270 LEU B 277 1 ? 8  
HELX_P HELX_P44 AE8 GLY B 301 ? ARG B 311 ? GLY B 286 ARG B 296 1 ? 11 
HELX_P HELX_P45 AE9 ARG B 312 ? MET B 314 ? ARG B 297 MET B 299 5 ? 3  
HELX_P HELX_P46 AF1 PRO B 315 ? ASN B 328 ? PRO B 300 ASN B 313 1 ? 14 
HELX_P HELX_P47 AF2 SER B 330 ? SER B 337 ? SER B 315 SER B 322 1 ? 8  
HELX_P HELX_P48 AF3 ASP B 340 ? ILE B 369 ? ASP B 325 ILE B 354 1 ? 30 
HELX_P HELX_P49 AF4 ILE B 369 ? GLN B 375 ? ILE B 354 GLN B 360 1 ? 7  
HELX_P HELX_P50 AF5 GLY B 396 ? LYS B 412 ? GLY B 381 LYS B 397 1 ? 17 
# 
_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 ? ? ? ? ? ? ? 2.043 ? ? 
metalc1 metalc ? ? A HIS 361 NE2 ? ? ? 1_555 C HEM   .   FE ? ? A HIS 346 A HEM   501 1_555 ? ? ? ? ? ? ? 2.048 ? ? 
metalc2 metalc ? ? C HEM .   FE  ? ? ? 1_555 D A1H6U .   N2 ? ? A HEM 501 A A1H6U 502 1_555 ? ? ? ? ? ? ? 2.122 ? ? 
metalc3 metalc ? ? B HIS 361 NE2 ? ? ? 1_555 E HEM   .   FE ? ? B HIS 346 B HEM   501 1_555 ? ? ? ? ? ? ? 2.074 ? ? 
metalc4 metalc ? ? E HEM .   FE  ? ? ? 1_555 F A1H6U .   N2 ? ? B HEM 501 B A1H6U 502 1_555 ? ? ? ? ? ? ? 2.076 ? ? 
# 
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 91.5  ? 
2  NE2 ? A HIS 361 ? A HIS 346 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NB ? C HEM   . ? A HEM   501 ? 1_555 86.6  ? 
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 88.7  ? 
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 87.7  ? 
5  NA  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NC ? C HEM   . ? A HEM   501 ? 1_555 178.4 ? 
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 92.7  ? 
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 88.3  ? 
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 90.9  ? 
9  NB  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM   . ? A HEM   501 ? 1_555 174.9 ? 
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 87.7  ? 
11 NE2 ? A HIS 361 ? A HIS 346 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 N2 ? D A1H6U . ? A A1H6U 502 ? 1_555 169.8 ? 
12 NA  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 N2 ? D A1H6U . ? A A1H6U 502 ? 1_555 97.3  ? 
13 NB  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 N2 ? D A1H6U . ? A A1H6U 502 ? 1_555 88.3  ? 
14 NC  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 N2 ? D A1H6U . ? A A1H6U 502 ? 1_555 83.7  ? 
15 ND  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 N2 ? D A1H6U . ? A A1H6U 502 ? 1_555 96.8  ? 
16 NE2 ? B HIS 361 ? B HIS 346 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 NA ? E HEM   . ? B HEM   501 ? 1_555 91.0  ? 
17 NE2 ? B HIS 361 ? B HIS 346 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 NB ? E HEM   . ? B HEM   501 ? 1_555 86.7  ? 
18 NA  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 NB ? E HEM   . ? B HEM   501 ? 1_555 87.5  ? 
19 NE2 ? B HIS 361 ? B HIS 346 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 NC ? E HEM   . ? B HEM   501 ? 1_555 86.8  ? 
20 NA  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 NC ? E HEM   . ? B HEM   501 ? 1_555 177.8 ? 
21 NB  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 NC ? E HEM   . ? B HEM   501 ? 1_555 92.3  ? 
22 NE2 ? B HIS 361 ? B HIS 346 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 ND ? E HEM   . ? B HEM   501 ? 1_555 88.8  ? 
23 NA  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 ND ? E HEM   . ? B HEM   501 ? 1_555 90.3  ? 
24 NB  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 ND ? E HEM   . ? B HEM   501 ? 1_555 174.9 ? 
25 NC  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 ND ? E HEM   . ? B HEM   501 ? 1_555 89.8  ? 
26 NE2 ? B HIS 361 ? B HIS 346 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 N2 ? F A1H6U . ? B A1H6U 502 ? 1_555 171.4 ? 
27 NA  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 N2 ? F A1H6U . ? B A1H6U 502 ? 1_555 96.7  ? 
28 NB  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 N2 ? F A1H6U . ? B A1H6U 502 ? 1_555 90.1  ? 
29 NC  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 N2 ? F A1H6U . ? B A1H6U 502 ? 1_555 85.4  ? 
30 ND  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 N2 ? F A1H6U . ? B A1H6U 502 ? 1_555 94.7  ? 
# 
_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                   9EW0 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   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 35.07   69.37  
2  1 ASN A 27  ? B 31.80   72.66  
3  1 ASN A 133 ? ? -96.79  56.81  
4  1 LEU A 243 ? ? -142.41 59.83  
5  1 ILE A 354 ? ? -124.60 -57.36 
6  1 LYS A 401 ? ? -122.11 -71.79 
7  1 GLU A 402 ? ? -40.55  98.85  
8  1 ASN B 27  ? ? 33.15   69.28  
9  1 ASN B 133 ? ? -97.99  53.95  
10 1 ILE B 354 ? ? -122.70 -56.36 
# 
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 GLN 4   ? A GLN 19  
20 1 Y 1 A GLY 5   ? A GLY 20  
21 1 Y 1 A PRO 6   ? A PRO 21  
22 1 Y 1 A HIS 7   ? A HIS 22  
23 1 Y 1 A MET 8   ? A MET 23  
24 1 Y 1 A TRP 9   ? A TRP 24  
25 1 Y 1 A PRO 362 ? A PRO 377 
26 1 Y 1 A LYS 363 ? A LYS 378 
27 1 Y 1 A GLU 364 ? A GLU 379 
28 1 Y 1 A ASN 365 ? A ASN 380 
29 1 Y 1 A LYS 366 ? A LYS 381 
30 1 Y 1 A THR 367 ? A THR 382 
31 1 Y 1 A SER 368 ? A SER 383 
32 1 Y 1 A GLU 369 ? A GLU 384 
33 1 Y 1 A ASP 370 ? A ASP 385 
34 1 Y 1 A PRO 371 ? A PRO 386 
35 1 Y 1 A SER 372 ? A SER 387 
36 1 Y 1 A LYS 373 ? A LYS 388 
37 1 Y 1 A LEU 374 ? A LEU 389 
38 1 Y 1 A GLU 375 ? A GLU 390 
39 1 Y 1 A ALA 376 ? A ALA 391 
40 1 Y 1 A LYS 377 ? A LYS 392 
41 1 Y 1 A GLY 378 ? A GLY 393 
42 1 Y 1 A THR 379 ? A THR 394 
43 1 Y 1 A GLY 380 ? A GLY 395 
44 1 Y 1 B MET -14 ? B MET 1   
45 1 Y 1 B GLY -13 ? B GLY 2   
46 1 Y 1 B SER -12 ? B SER 3   
47 1 Y 1 B SER -11 ? B SER 4   
48 1 Y 1 B HIS -10 ? B HIS 5   
49 1 Y 1 B HIS -9  ? B HIS 6   
50 1 Y 1 B HIS -8  ? B HIS 7   
51 1 Y 1 B HIS -7  ? B HIS 8   
52 1 Y 1 B HIS -6  ? B HIS 9   
53 1 Y 1 B HIS -5  ? B HIS 10  
54 1 Y 1 B SER -4  ? B SER 11  
55 1 Y 1 B ALA -3  ? B ALA 12  
56 1 Y 1 B ALA -2  ? B ALA 13  
57 1 Y 1 B LEU -1  ? B LEU 14  
58 1 Y 1 B GLU 0   ? B GLU 15  
59 1 Y 1 B VAL 1   ? B VAL 16  
60 1 Y 1 B LEU 2   ? B LEU 17  
61 1 Y 1 B PHE 3   ? B PHE 18  
62 1 Y 1 B GLN 4   ? B GLN 19  
63 1 Y 1 B GLY 5   ? B GLY 20  
64 1 Y 1 B PRO 6   ? B PRO 21  
65 1 Y 1 B HIS 7   ? B HIS 22  
66 1 Y 1 B MET 8   ? B MET 23  
67 1 Y 1 B TRP 9   ? B TRP 24  
68 1 Y 1 B PRO 362 ? B PRO 377 
69 1 Y 1 B LYS 363 ? B LYS 378 
70 1 Y 1 B GLU 364 ? B GLU 379 
71 1 Y 1 B ASN 365 ? B ASN 380 
72 1 Y 1 B LYS 366 ? B LYS 381 
73 1 Y 1 B THR 367 ? B THR 382 
74 1 Y 1 B SER 368 ? B SER 383 
75 1 Y 1 B GLU 369 ? B GLU 384 
76 1 Y 1 B ASP 370 ? B ASP 385 
77 1 Y 1 B PRO 371 ? B PRO 386 
78 1 Y 1 B SER 372 ? B SER 387 
79 1 Y 1 B LYS 373 ? B LYS 388 
80 1 Y 1 B LEU 374 ? B LEU 389 
81 1 Y 1 B GLU 375 ? B GLU 390 
82 1 Y 1 B ALA 376 ? B ALA 391 
83 1 Y 1 B LYS 377 ? B LYS 392 
84 1 Y 1 B GLY 378 ? B GLY 393 
85 1 Y 1 B THR 379 ? B THR 394 
86 1 Y 1 B GLU 402 ? B GLU 417 
87 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 
A1H6U C5   C  Y N 1   
A1H6U C6   C  Y N 2   
A1H6U C7   C  Y N 3   
A1H6U C8   C  Y N 4   
A1H6U C13  C  N N 5   
A1H6U O    O  N N 6   
A1H6U C1   C  N S 7   
A1H6U CA   C  Y N 8   
A1H6U N    N  Y N 9   
A1H6U C3   C  Y N 10  
A1H6U CG2  C  Y N 11  
A1H6U N2   N  Y N 12  
A1H6U C9   C  N N 13  
A1H6U CD1  C  N N 14  
A1H6U CG1  C  N N 15  
A1H6U C12  C  N N 16  
A1H6U C14  C  N N 17  
A1H6U H4   H  N N 18  
A1H6U H5   H  N N 19  
A1H6U H6   H  N N 20  
A1H6U H7   H  N N 21  
A1H6U H16  H  N N 22  
A1H6U H15  H  N N 23  
A1H6U H1   H  N N 24  
A1H6U H2   H  N N 25  
A1H6U H3   H  N N 26  
A1H6U H8   H  N N 27  
A1H6U H10  H  N N 28  
A1H6U H9   H  N N 29  
A1H6U H12  H  N N 30  
A1H6U H11  H  N N 31  
A1H6U H13  H  N N 32  
A1H6U H14  H  N N 33  
A1H6U H18  H  N N 34  
A1H6U H17  H  N N 35  
ALA   N    N  N N 36  
ALA   CA   C  N S 37  
ALA   C    C  N N 38  
ALA   O    O  N N 39  
ALA   CB   C  N N 40  
ALA   OXT  O  N N 41  
ALA   H    H  N N 42  
ALA   H2   H  N N 43  
ALA   HA   H  N N 44  
ALA   HB1  H  N N 45  
ALA   HB2  H  N N 46  
ALA   HB3  H  N N 47  
ALA   HXT  H  N N 48  
ARG   N    N  N N 49  
ARG   CA   C  N S 50  
ARG   C    C  N N 51  
ARG   O    O  N N 52  
ARG   CB   C  N N 53  
ARG   CG   C  N N 54  
ARG   CD   C  N N 55  
ARG   NE   N  N N 56  
ARG   CZ   C  N N 57  
ARG   NH1  N  N N 58  
ARG   NH2  N  N N 59  
ARG   OXT  O  N N 60  
ARG   H    H  N N 61  
ARG   H2   H  N N 62  
ARG   HA   H  N N 63  
ARG   HB2  H  N N 64  
ARG   HB3  H  N N 65  
ARG   HG2  H  N N 66  
ARG   HG3  H  N N 67  
ARG   HD2  H  N N 68  
ARG   HD3  H  N N 69  
ARG   HE   H  N N 70  
ARG   HH11 H  N N 71  
ARG   HH12 H  N N 72  
ARG   HH21 H  N N 73  
ARG   HH22 H  N N 74  
ARG   HXT  H  N N 75  
ASN   N    N  N N 76  
ASN   CA   C  N S 77  
ASN   C    C  N N 78  
ASN   O    O  N N 79  
ASN   CB   C  N N 80  
ASN   CG   C  N N 81  
ASN   OD1  O  N N 82  
ASN   ND2  N  N N 83  
ASN   OXT  O  N N 84  
ASN   H    H  N N 85  
ASN   H2   H  N N 86  
ASN   HA   H  N N 87  
ASN   HB2  H  N N 88  
ASN   HB3  H  N N 89  
ASN   HD21 H  N N 90  
ASN   HD22 H  N N 91  
ASN   HXT  H  N N 92  
ASP   N    N  N N 93  
ASP   CA   C  N S 94  
ASP   C    C  N N 95  
ASP   O    O  N N 96  
ASP   CB   C  N N 97  
ASP   CG   C  N N 98  
ASP   OD1  O  N N 99  
ASP   OD2  O  N N 100 
ASP   OXT  O  N N 101 
ASP   H    H  N N 102 
ASP   H2   H  N N 103 
ASP   HA   H  N N 104 
ASP   HB2  H  N N 105 
ASP   HB3  H  N N 106 
ASP   HD2  H  N N 107 
ASP   HXT  H  N N 108 
CYS   N    N  N N 109 
CYS   CA   C  N R 110 
CYS   C    C  N N 111 
CYS   O    O  N N 112 
CYS   CB   C  N N 113 
CYS   SG   S  N N 114 
CYS   OXT  O  N N 115 
CYS   H    H  N N 116 
CYS   H2   H  N N 117 
CYS   HA   H  N N 118 
CYS   HB2  H  N N 119 
CYS   HB3  H  N N 120 
CYS   HG   H  N N 121 
CYS   HXT  H  N N 122 
GLN   N    N  N N 123 
GLN   CA   C  N S 124 
GLN   C    C  N N 125 
GLN   O    O  N N 126 
GLN   CB   C  N N 127 
GLN   CG   C  N N 128 
GLN   CD   C  N N 129 
GLN   OE1  O  N N 130 
GLN   NE2  N  N N 131 
GLN   OXT  O  N N 132 
GLN   H    H  N N 133 
GLN   H2   H  N N 134 
GLN   HA   H  N N 135 
GLN   HB2  H  N N 136 
GLN   HB3  H  N N 137 
GLN   HG2  H  N N 138 
GLN   HG3  H  N N 139 
GLN   HE21 H  N N 140 
GLN   HE22 H  N N 141 
GLN   HXT  H  N N 142 
GLU   N    N  N N 143 
GLU   CA   C  N S 144 
GLU   C    C  N N 145 
GLU   O    O  N N 146 
GLU   CB   C  N N 147 
GLU   CG   C  N N 148 
GLU   CD   C  N N 149 
GLU   OE1  O  N N 150 
GLU   OE2  O  N N 151 
GLU   OXT  O  N N 152 
GLU   H    H  N N 153 
GLU   H2   H  N N 154 
GLU   HA   H  N N 155 
GLU   HB2  H  N N 156 
GLU   HB3  H  N N 157 
GLU   HG2  H  N N 158 
GLU   HG3  H  N N 159 
GLU   HE2  H  N N 160 
GLU   HXT  H  N N 161 
GLY   N    N  N N 162 
GLY   CA   C  N N 163 
GLY   C    C  N N 164 
GLY   O    O  N N 165 
GLY   OXT  O  N N 166 
GLY   H    H  N N 167 
GLY   H2   H  N N 168 
GLY   HA2  H  N N 169 
GLY   HA3  H  N N 170 
GLY   HXT  H  N N 171 
HEM   CHA  C  N N 172 
HEM   CHB  C  N N 173 
HEM   CHC  C  N N 174 
HEM   CHD  C  N N 175 
HEM   C1A  C  Y N 176 
HEM   C2A  C  Y N 177 
HEM   C3A  C  Y N 178 
HEM   C4A  C  Y N 179 
HEM   CMA  C  N N 180 
HEM   CAA  C  N N 181 
HEM   CBA  C  N N 182 
HEM   CGA  C  N N 183 
HEM   O1A  O  N N 184 
HEM   O2A  O  N N 185 
HEM   C1B  C  N N 186 
HEM   C2B  C  N N 187 
HEM   C3B  C  N N 188 
HEM   C4B  C  N N 189 
HEM   CMB  C  N N 190 
HEM   CAB  C  N N 191 
HEM   CBB  C  N N 192 
HEM   C1C  C  Y N 193 
HEM   C2C  C  Y N 194 
HEM   C3C  C  Y N 195 
HEM   C4C  C  Y N 196 
HEM   CMC  C  N N 197 
HEM   CAC  C  N N 198 
HEM   CBC  C  N N 199 
HEM   C1D  C  N N 200 
HEM   C2D  C  N N 201 
HEM   C3D  C  N N 202 
HEM   C4D  C  N N 203 
HEM   CMD  C  N N 204 
HEM   CAD  C  N N 205 
HEM   CBD  C  N N 206 
HEM   CGD  C  N N 207 
HEM   O1D  O  N N 208 
HEM   O2D  O  N N 209 
HEM   NA   N  Y N 210 
HEM   NB   N  N N 211 
HEM   NC   N  Y N 212 
HEM   ND   N  N N 213 
HEM   FE   FE N N 214 
HEM   HHB  H  N N 215 
HEM   HHC  H  N N 216 
HEM   HHD  H  N N 217 
HEM   HMA  H  N N 218 
HEM   HMAA H  N N 219 
HEM   HMAB H  N N 220 
HEM   HAA  H  N N 221 
HEM   HAAA H  N N 222 
HEM   HBA  H  N N 223 
HEM   HBAA H  N N 224 
HEM   HMB  H  N N 225 
HEM   HMBA H  N N 226 
HEM   HMBB H  N N 227 
HEM   HAB  H  N N 228 
HEM   HBB  H  N N 229 
HEM   HBBA H  N N 230 
HEM   HMC  H  N N 231 
HEM   HMCA H  N N 232 
HEM   HMCB H  N N 233 
HEM   HAC  H  N N 234 
HEM   HBC  H  N N 235 
HEM   HBCA H  N N 236 
HEM   HMD  H  N N 237 
HEM   HMDA H  N N 238 
HEM   HMDB H  N N 239 
HEM   HAD  H  N N 240 
HEM   HADA H  N N 241 
HEM   HBD  H  N N 242 
HEM   HBDA H  N N 243 
HEM   H2A  H  N N 244 
HEM   H2D  H  N N 245 
HEM   HHA  H  N N 246 
HIS   N    N  N N 247 
HIS   CA   C  N S 248 
HIS   C    C  N N 249 
HIS   O    O  N N 250 
HIS   CB   C  N N 251 
HIS   CG   C  Y N 252 
HIS   ND1  N  Y N 253 
HIS   CD2  C  Y N 254 
HIS   CE1  C  Y N 255 
HIS   NE2  N  Y N 256 
HIS   OXT  O  N N 257 
HIS   H    H  N N 258 
HIS   H2   H  N N 259 
HIS   HA   H  N N 260 
HIS   HB2  H  N N 261 
HIS   HB3  H  N N 262 
HIS   HD1  H  N N 263 
HIS   HD2  H  N N 264 
HIS   HE1  H  N N 265 
HIS   HE2  H  N N 266 
HIS   HXT  H  N N 267 
HOH   O    O  N N 268 
HOH   H1   H  N N 269 
HOH   H2   H  N N 270 
ILE   N    N  N N 271 
ILE   CA   C  N S 272 
ILE   C    C  N N 273 
ILE   O    O  N N 274 
ILE   CB   C  N S 275 
ILE   CG1  C  N N 276 
ILE   CG2  C  N N 277 
ILE   CD1  C  N N 278 
ILE   OXT  O  N N 279 
ILE   H    H  N N 280 
ILE   H2   H  N N 281 
ILE   HA   H  N N 282 
ILE   HB   H  N N 283 
ILE   HG12 H  N N 284 
ILE   HG13 H  N N 285 
ILE   HG21 H  N N 286 
ILE   HG22 H  N N 287 
ILE   HG23 H  N N 288 
ILE   HD11 H  N N 289 
ILE   HD12 H  N N 290 
ILE   HD13 H  N N 291 
ILE   HXT  H  N N 292 
LEU   N    N  N N 293 
LEU   CA   C  N S 294 
LEU   C    C  N N 295 
LEU   O    O  N N 296 
LEU   CB   C  N N 297 
LEU   CG   C  N N 298 
LEU   CD1  C  N N 299 
LEU   CD2  C  N N 300 
LEU   OXT  O  N N 301 
LEU   H    H  N N 302 
LEU   H2   H  N N 303 
LEU   HA   H  N N 304 
LEU   HB2  H  N N 305 
LEU   HB3  H  N N 306 
LEU   HG   H  N N 307 
LEU   HD11 H  N N 308 
LEU   HD12 H  N N 309 
LEU   HD13 H  N N 310 
LEU   HD21 H  N N 311 
LEU   HD22 H  N N 312 
LEU   HD23 H  N N 313 
LEU   HXT  H  N N 314 
LYS   N    N  N N 315 
LYS   CA   C  N S 316 
LYS   C    C  N N 317 
LYS   O    O  N N 318 
LYS   CB   C  N N 319 
LYS   CG   C  N N 320 
LYS   CD   C  N N 321 
LYS   CE   C  N N 322 
LYS   NZ   N  N N 323 
LYS   OXT  O  N N 324 
LYS   H    H  N N 325 
LYS   H2   H  N N 326 
LYS   HA   H  N N 327 
LYS   HB2  H  N N 328 
LYS   HB3  H  N N 329 
LYS   HG2  H  N N 330 
LYS   HG3  H  N N 331 
LYS   HD2  H  N N 332 
LYS   HD3  H  N N 333 
LYS   HE2  H  N N 334 
LYS   HE3  H  N N 335 
LYS   HZ1  H  N N 336 
LYS   HZ2  H  N N 337 
LYS   HZ3  H  N N 338 
LYS   HXT  H  N N 339 
MET   N    N  N N 340 
MET   CA   C  N S 341 
MET   C    C  N N 342 
MET   O    O  N N 343 
MET   CB   C  N N 344 
MET   CG   C  N N 345 
MET   SD   S  N N 346 
MET   CE   C  N N 347 
MET   OXT  O  N N 348 
MET   H    H  N N 349 
MET   H2   H  N N 350 
MET   HA   H  N N 351 
MET   HB2  H  N N 352 
MET   HB3  H  N N 353 
MET   HG2  H  N N 354 
MET   HG3  H  N N 355 
MET   HE1  H  N N 356 
MET   HE2  H  N N 357 
MET   HE3  H  N N 358 
MET   HXT  H  N N 359 
PHE   N    N  N N 360 
PHE   CA   C  N S 361 
PHE   C    C  N N 362 
PHE   O    O  N N 363 
PHE   CB   C  N N 364 
PHE   CG   C  Y N 365 
PHE   CD1  C  Y N 366 
PHE   CD2  C  Y N 367 
PHE   CE1  C  Y N 368 
PHE   CE2  C  Y N 369 
PHE   CZ   C  Y N 370 
PHE   OXT  O  N N 371 
PHE   H    H  N N 372 
PHE   H2   H  N N 373 
PHE   HA   H  N N 374 
PHE   HB2  H  N N 375 
PHE   HB3  H  N N 376 
PHE   HD1  H  N N 377 
PHE   HD2  H  N N 378 
PHE   HE1  H  N N 379 
PHE   HE2  H  N N 380 
PHE   HZ   H  N N 381 
PHE   HXT  H  N N 382 
PRO   N    N  N N 383 
PRO   CA   C  N S 384 
PRO   C    C  N N 385 
PRO   O    O  N N 386 
PRO   CB   C  N N 387 
PRO   CG   C  N N 388 
PRO   CD   C  N N 389 
PRO   OXT  O  N N 390 
PRO   H    H  N N 391 
PRO   HA   H  N N 392 
PRO   HB2  H  N N 393 
PRO   HB3  H  N N 394 
PRO   HG2  H  N N 395 
PRO   HG3  H  N N 396 
PRO   HD2  H  N N 397 
PRO   HD3  H  N N 398 
PRO   HXT  H  N N 399 
SER   N    N  N N 400 
SER   CA   C  N S 401 
SER   C    C  N N 402 
SER   O    O  N N 403 
SER   CB   C  N N 404 
SER   OG   O  N N 405 
SER   OXT  O  N N 406 
SER   H    H  N N 407 
SER   H2   H  N N 408 
SER   HA   H  N N 409 
SER   HB2  H  N N 410 
SER   HB3  H  N N 411 
SER   HG   H  N N 412 
SER   HXT  H  N N 413 
THR   N    N  N N 414 
THR   CA   C  N S 415 
THR   C    C  N N 416 
THR   O    O  N N 417 
THR   CB   C  N R 418 
THR   OG1  O  N N 419 
THR   CG2  C  N N 420 
THR   OXT  O  N N 421 
THR   H    H  N N 422 
THR   H2   H  N N 423 
THR   HA   H  N N 424 
THR   HB   H  N N 425 
THR   HG1  H  N N 426 
THR   HG21 H  N N 427 
THR   HG22 H  N N 428 
THR   HG23 H  N N 429 
THR   HXT  H  N N 430 
TRP   N    N  N N 431 
TRP   CA   C  N S 432 
TRP   C    C  N N 433 
TRP   O    O  N N 434 
TRP   CB   C  N N 435 
TRP   CG   C  Y N 436 
TRP   CD1  C  Y N 437 
TRP   CD2  C  Y N 438 
TRP   NE1  N  Y N 439 
TRP   CE2  C  Y N 440 
TRP   CE3  C  Y N 441 
TRP   CZ2  C  Y N 442 
TRP   CZ3  C  Y N 443 
TRP   CH2  C  Y N 444 
TRP   OXT  O  N N 445 
TRP   H    H  N N 446 
TRP   H2   H  N N 447 
TRP   HA   H  N N 448 
TRP   HB2  H  N N 449 
TRP   HB3  H  N N 450 
TRP   HD1  H  N N 451 
TRP   HE1  H  N N 452 
TRP   HE3  H  N N 453 
TRP   HZ2  H  N N 454 
TRP   HZ3  H  N N 455 
TRP   HH2  H  N N 456 
TRP   HXT  H  N N 457 
TYR   N    N  N N 458 
TYR   CA   C  N S 459 
TYR   C    C  N N 460 
TYR   O    O  N N 461 
TYR   CB   C  N N 462 
TYR   CG   C  Y N 463 
TYR   CD1  C  Y N 464 
TYR   CD2  C  Y N 465 
TYR   CE1  C  Y N 466 
TYR   CE2  C  Y N 467 
TYR   CZ   C  Y N 468 
TYR   OH   O  N N 469 
TYR   OXT  O  N N 470 
TYR   H    H  N N 471 
TYR   H2   H  N N 472 
TYR   HA   H  N N 473 
TYR   HB2  H  N N 474 
TYR   HB3  H  N N 475 
TYR   HD1  H  N N 476 
TYR   HD2  H  N N 477 
TYR   HE1  H  N N 478 
TYR   HE2  H  N N 479 
TYR   HH   H  N N 480 
TYR   HXT  H  N N 481 
VAL   N    N  N N 482 
VAL   CA   C  N S 483 
VAL   C    C  N N 484 
VAL   O    O  N N 485 
VAL   CB   C  N N 486 
VAL   CG1  C  N N 487 
VAL   CG2  C  N N 488 
VAL   OXT  O  N N 489 
VAL   H    H  N N 490 
VAL   H2   H  N N 491 
VAL   HA   H  N N 492 
VAL   HB   H  N N 493 
VAL   HG11 H  N N 494 
VAL   HG12 H  N N 495 
VAL   HG13 H  N N 496 
VAL   HG21 H  N N 497 
VAL   HG22 H  N N 498 
VAL   HG23 H  N N 499 
VAL   HXT  H  N N 500 
# 
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 
A1H6U O   C1   sing N N 1   
A1H6U C1  CA   sing N N 2   
A1H6U CA  N    sing Y N 3   
A1H6U N   C3   sing Y N 4   
A1H6U C3  CG2  sing Y N 5   
A1H6U CG2 C5   doub Y N 6   
A1H6U C5  C6   sing Y N 7   
A1H6U C3  C7   doub Y N 8   
A1H6U C7  N2   sing Y N 9   
A1H6U N2  C8   doub Y N 10  
A1H6U C1  C9   sing N N 11  
A1H6U C9  CD1  sing N N 12  
A1H6U CD1 CG1  sing N N 13  
A1H6U CG1 C12  sing N N 14  
A1H6U C12 C13  sing N N 15  
A1H6U C13 C14  sing N N 16  
A1H6U CA  C6   doub Y N 17  
A1H6U C8  N    sing Y N 18  
A1H6U C14 C9   sing N N 19  
A1H6U C5  H4   sing N N 20  
A1H6U C6  H5   sing N N 21  
A1H6U C7  H6   sing N N 22  
A1H6U C8  H7   sing N N 23  
A1H6U C13 H16  sing N N 24  
A1H6U C13 H15  sing N N 25  
A1H6U O   H1   sing N N 26  
A1H6U C1  H2   sing N N 27  
A1H6U CG2 H3   sing N N 28  
A1H6U C9  H8   sing N N 29  
A1H6U CD1 H10  sing N N 30  
A1H6U CD1 H9   sing N N 31  
A1H6U CG1 H12  sing N N 32  
A1H6U CG1 H11  sing N N 33  
A1H6U C12 H13  sing N N 34  
A1H6U C12 H14  sing N N 35  
A1H6U C14 H18  sing N N 36  
A1H6U C14 H17  sing N N 37  
ALA   N   CA   sing N N 38  
ALA   N   H    sing N N 39  
ALA   N   H2   sing N N 40  
ALA   CA  C    sing N N 41  
ALA   CA  CB   sing N N 42  
ALA   CA  HA   sing N N 43  
ALA   C   O    doub N N 44  
ALA   C   OXT  sing N N 45  
ALA   CB  HB1  sing N N 46  
ALA   CB  HB2  sing N N 47  
ALA   CB  HB3  sing N N 48  
ALA   OXT HXT  sing N N 49  
ARG   N   CA   sing N N 50  
ARG   N   H    sing N N 51  
ARG   N   H2   sing N N 52  
ARG   CA  C    sing N N 53  
ARG   CA  CB   sing N N 54  
ARG   CA  HA   sing N N 55  
ARG   C   O    doub N N 56  
ARG   C   OXT  sing N N 57  
ARG   CB  CG   sing N N 58  
ARG   CB  HB2  sing N N 59  
ARG   CB  HB3  sing N N 60  
ARG   CG  CD   sing N N 61  
ARG   CG  HG2  sing N N 62  
ARG   CG  HG3  sing N N 63  
ARG   CD  NE   sing N N 64  
ARG   CD  HD2  sing N N 65  
ARG   CD  HD3  sing N N 66  
ARG   NE  CZ   sing N N 67  
ARG   NE  HE   sing N N 68  
ARG   CZ  NH1  sing N N 69  
ARG   CZ  NH2  doub N N 70  
ARG   NH1 HH11 sing N N 71  
ARG   NH1 HH12 sing N N 72  
ARG   NH2 HH21 sing N N 73  
ARG   NH2 HH22 sing N N 74  
ARG   OXT HXT  sing N N 75  
ASN   N   CA   sing N N 76  
ASN   N   H    sing N N 77  
ASN   N   H2   sing N N 78  
ASN   CA  C    sing N N 79  
ASN   CA  CB   sing N N 80  
ASN   CA  HA   sing N N 81  
ASN   C   O    doub N N 82  
ASN   C   OXT  sing N N 83  
ASN   CB  CG   sing N N 84  
ASN   CB  HB2  sing N N 85  
ASN   CB  HB3  sing N N 86  
ASN   CG  OD1  doub N N 87  
ASN   CG  ND2  sing N N 88  
ASN   ND2 HD21 sing N N 89  
ASN   ND2 HD22 sing N N 90  
ASN   OXT HXT  sing N N 91  
ASP   N   CA   sing N N 92  
ASP   N   H    sing N N 93  
ASP   N   H2   sing N N 94  
ASP   CA  C    sing N N 95  
ASP   CA  CB   sing N N 96  
ASP   CA  HA   sing N N 97  
ASP   C   O    doub N N 98  
ASP   C   OXT  sing N N 99  
ASP   CB  CG   sing N N 100 
ASP   CB  HB2  sing N N 101 
ASP   CB  HB3  sing N N 102 
ASP   CG  OD1  doub N N 103 
ASP   CG  OD2  sing N N 104 
ASP   OD2 HD2  sing N N 105 
ASP   OXT HXT  sing N N 106 
CYS   N   CA   sing N N 107 
CYS   N   H    sing N N 108 
CYS   N   H2   sing N N 109 
CYS   CA  C    sing N N 110 
CYS   CA  CB   sing N N 111 
CYS   CA  HA   sing N N 112 
CYS   C   O    doub N N 113 
CYS   C   OXT  sing N N 114 
CYS   CB  SG   sing N N 115 
CYS   CB  HB2  sing N N 116 
CYS   CB  HB3  sing N N 117 
CYS   SG  HG   sing N N 118 
CYS   OXT HXT  sing N N 119 
GLN   N   CA   sing N N 120 
GLN   N   H    sing N N 121 
GLN   N   H2   sing N N 122 
GLN   CA  C    sing N N 123 
GLN   CA  CB   sing N N 124 
GLN   CA  HA   sing N N 125 
GLN   C   O    doub N N 126 
GLN   C   OXT  sing N N 127 
GLN   CB  CG   sing N N 128 
GLN   CB  HB2  sing N N 129 
GLN   CB  HB3  sing N N 130 
GLN   CG  CD   sing N N 131 
GLN   CG  HG2  sing N N 132 
GLN   CG  HG3  sing N N 133 
GLN   CD  OE1  doub N N 134 
GLN   CD  NE2  sing N N 135 
GLN   NE2 HE21 sing N N 136 
GLN   NE2 HE22 sing N N 137 
GLN   OXT HXT  sing N N 138 
GLU   N   CA   sing N N 139 
GLU   N   H    sing N N 140 
GLU   N   H2   sing N N 141 
GLU   CA  C    sing N N 142 
GLU   CA  CB   sing N N 143 
GLU   CA  HA   sing N N 144 
GLU   C   O    doub N N 145 
GLU   C   OXT  sing N N 146 
GLU   CB  CG   sing N N 147 
GLU   CB  HB2  sing N N 148 
GLU   CB  HB3  sing N N 149 
GLU   CG  CD   sing N N 150 
GLU   CG  HG2  sing N N 151 
GLU   CG  HG3  sing N N 152 
GLU   CD  OE1  doub N N 153 
GLU   CD  OE2  sing N N 154 
GLU   OE2 HE2  sing N N 155 
GLU   OXT HXT  sing N N 156 
GLY   N   CA   sing N N 157 
GLY   N   H    sing N N 158 
GLY   N   H2   sing N N 159 
GLY   CA  C    sing N N 160 
GLY   CA  HA2  sing N N 161 
GLY   CA  HA3  sing N N 162 
GLY   C   O    doub N N 163 
GLY   C   OXT  sing N N 164 
GLY   OXT HXT  sing N N 165 
HEM   CHA C1A  sing N N 166 
HEM   CHA C4D  doub N N 167 
HEM   CHA HHA  sing N N 168 
HEM   CHB C4A  sing N N 169 
HEM   CHB C1B  doub N N 170 
HEM   CHB HHB  sing N N 171 
HEM   CHC C4B  sing N N 172 
HEM   CHC C1C  doub N N 173 
HEM   CHC HHC  sing N N 174 
HEM   CHD C4C  doub N N 175 
HEM   CHD C1D  sing N N 176 
HEM   CHD HHD  sing N N 177 
HEM   C1A C2A  doub Y N 178 
HEM   C1A NA   sing Y N 179 
HEM   C2A C3A  sing Y N 180 
HEM   C2A CAA  sing N N 181 
HEM   C3A C4A  doub Y N 182 
HEM   C3A CMA  sing N N 183 
HEM   C4A NA   sing Y N 184 
HEM   CMA HMA  sing N N 185 
HEM   CMA HMAA sing N N 186 
HEM   CMA HMAB sing N N 187 
HEM   CAA CBA  sing N N 188 
HEM   CAA HAA  sing N N 189 
HEM   CAA HAAA sing N N 190 
HEM   CBA CGA  sing N N 191 
HEM   CBA HBA  sing N N 192 
HEM   CBA HBAA sing N N 193 
HEM   CGA O1A  doub N N 194 
HEM   CGA O2A  sing N N 195 
HEM   C1B C2B  sing N N 196 
HEM   C1B NB   sing N N 197 
HEM   C2B C3B  doub N N 198 
HEM   C2B CMB  sing N N 199 
HEM   C3B C4B  sing N N 200 
HEM   C3B CAB  sing N N 201 
HEM   C4B NB   doub N N 202 
HEM   CMB HMB  sing N N 203 
HEM   CMB HMBA sing N N 204 
HEM   CMB HMBB sing N N 205 
HEM   CAB CBB  doub N N 206 
HEM   CAB HAB  sing N N 207 
HEM   CBB HBB  sing N N 208 
HEM   CBB HBBA sing N N 209 
HEM   C1C C2C  sing Y N 210 
HEM   C1C NC   sing Y N 211 
HEM   C2C C3C  doub Y N 212 
HEM   C2C CMC  sing N N 213 
HEM   C3C C4C  sing Y N 214 
HEM   C3C CAC  sing N N 215 
HEM   C4C NC   sing Y N 216 
HEM   CMC HMC  sing N N 217 
HEM   CMC HMCA sing N N 218 
HEM   CMC HMCB sing N N 219 
HEM   CAC CBC  doub N N 220 
HEM   CAC HAC  sing N N 221 
HEM   CBC HBC  sing N N 222 
HEM   CBC HBCA sing N N 223 
HEM   C1D C2D  sing N N 224 
HEM   C1D ND   doub N N 225 
HEM   C2D C3D  doub N N 226 
HEM   C2D CMD  sing N N 227 
HEM   C3D C4D  sing N N 228 
HEM   C3D CAD  sing N N 229 
HEM   C4D ND   sing N N 230 
HEM   CMD HMD  sing N N 231 
HEM   CMD HMDA sing N N 232 
HEM   CMD HMDB sing N N 233 
HEM   CAD CBD  sing N N 234 
HEM   CAD HAD  sing N N 235 
HEM   CAD HADA sing N N 236 
HEM   CBD CGD  sing N N 237 
HEM   CBD HBD  sing N N 238 
HEM   CBD HBDA sing N N 239 
HEM   CGD O1D  doub N N 240 
HEM   CGD O2D  sing N N 241 
HEM   O2A H2A  sing N N 242 
HEM   O2D H2D  sing N N 243 
HEM   FE  NA   sing N N 244 
HEM   FE  NB   sing N N 245 
HEM   FE  NC   sing N N 246 
HEM   FE  ND   sing N N 247 
HIS   N   CA   sing N N 248 
HIS   N   H    sing N N 249 
HIS   N   H2   sing N N 250 
HIS   CA  C    sing N N 251 
HIS   CA  CB   sing N N 252 
HIS   CA  HA   sing N N 253 
HIS   C   O    doub N N 254 
HIS   C   OXT  sing N N 255 
HIS   CB  CG   sing N N 256 
HIS   CB  HB2  sing N N 257 
HIS   CB  HB3  sing N N 258 
HIS   CG  ND1  sing Y N 259 
HIS   CG  CD2  doub Y N 260 
HIS   ND1 CE1  doub Y N 261 
HIS   ND1 HD1  sing N N 262 
HIS   CD2 NE2  sing Y N 263 
HIS   CD2 HD2  sing N N 264 
HIS   CE1 NE2  sing Y N 265 
HIS   CE1 HE1  sing N N 266 
HIS   NE2 HE2  sing N N 267 
HIS   OXT HXT  sing N N 268 
HOH   O   H1   sing N N 269 
HOH   O   H2   sing N N 270 
ILE   N   CA   sing N N 271 
ILE   N   H    sing N N 272 
ILE   N   H2   sing N N 273 
ILE   CA  C    sing N N 274 
ILE   CA  CB   sing N N 275 
ILE   CA  HA   sing N N 276 
ILE   C   O    doub N N 277 
ILE   C   OXT  sing N N 278 
ILE   CB  CG1  sing N N 279 
ILE   CB  CG2  sing N N 280 
ILE   CB  HB   sing N N 281 
ILE   CG1 CD1  sing N N 282 
ILE   CG1 HG12 sing N N 283 
ILE   CG1 HG13 sing N N 284 
ILE   CG2 HG21 sing N N 285 
ILE   CG2 HG22 sing N N 286 
ILE   CG2 HG23 sing N N 287 
ILE   CD1 HD11 sing N N 288 
ILE   CD1 HD12 sing N N 289 
ILE   CD1 HD13 sing N N 290 
ILE   OXT HXT  sing N N 291 
LEU   N   CA   sing N N 292 
LEU   N   H    sing N N 293 
LEU   N   H2   sing N N 294 
LEU   CA  C    sing N N 295 
LEU   CA  CB   sing N N 296 
LEU   CA  HA   sing N N 297 
LEU   C   O    doub N N 298 
LEU   C   OXT  sing N N 299 
LEU   CB  CG   sing N N 300 
LEU   CB  HB2  sing N N 301 
LEU   CB  HB3  sing N N 302 
LEU   CG  CD1  sing N N 303 
LEU   CG  CD2  sing N N 304 
LEU   CG  HG   sing N N 305 
LEU   CD1 HD11 sing N N 306 
LEU   CD1 HD12 sing N N 307 
LEU   CD1 HD13 sing N N 308 
LEU   CD2 HD21 sing N N 309 
LEU   CD2 HD22 sing N N 310 
LEU   CD2 HD23 sing N N 311 
LEU   OXT HXT  sing N N 312 
LYS   N   CA   sing N N 313 
LYS   N   H    sing N N 314 
LYS   N   H2   sing N N 315 
LYS   CA  C    sing N N 316 
LYS   CA  CB   sing N N 317 
LYS   CA  HA   sing N N 318 
LYS   C   O    doub N N 319 
LYS   C   OXT  sing N N 320 
LYS   CB  CG   sing N N 321 
LYS   CB  HB2  sing N N 322 
LYS   CB  HB3  sing N N 323 
LYS   CG  CD   sing N N 324 
LYS   CG  HG2  sing N N 325 
LYS   CG  HG3  sing N N 326 
LYS   CD  CE   sing N N 327 
LYS   CD  HD2  sing N N 328 
LYS   CD  HD3  sing N N 329 
LYS   CE  NZ   sing N N 330 
LYS   CE  HE2  sing N N 331 
LYS   CE  HE3  sing N N 332 
LYS   NZ  HZ1  sing N N 333 
LYS   NZ  HZ2  sing N N 334 
LYS   NZ  HZ3  sing N N 335 
LYS   OXT HXT  sing N N 336 
MET   N   CA   sing N N 337 
MET   N   H    sing N N 338 
MET   N   H2   sing N N 339 
MET   CA  C    sing N N 340 
MET   CA  CB   sing N N 341 
MET   CA  HA   sing N N 342 
MET   C   O    doub N N 343 
MET   C   OXT  sing N N 344 
MET   CB  CG   sing N N 345 
MET   CB  HB2  sing N N 346 
MET   CB  HB3  sing N N 347 
MET   CG  SD   sing N N 348 
MET   CG  HG2  sing N N 349 
MET   CG  HG3  sing N N 350 
MET   SD  CE   sing N N 351 
MET   CE  HE1  sing N N 352 
MET   CE  HE2  sing N N 353 
MET   CE  HE3  sing N N 354 
MET   OXT HXT  sing N N 355 
PHE   N   CA   sing N N 356 
PHE   N   H    sing N N 357 
PHE   N   H2   sing N N 358 
PHE   CA  C    sing N N 359 
PHE   CA  CB   sing N N 360 
PHE   CA  HA   sing N N 361 
PHE   C   O    doub N N 362 
PHE   C   OXT  sing N N 363 
PHE   CB  CG   sing N N 364 
PHE   CB  HB2  sing N N 365 
PHE   CB  HB3  sing N N 366 
PHE   CG  CD1  doub Y N 367 
PHE   CG  CD2  sing Y N 368 
PHE   CD1 CE1  sing Y N 369 
PHE   CD1 HD1  sing N N 370 
PHE   CD2 CE2  doub Y N 371 
PHE   CD2 HD2  sing N N 372 
PHE   CE1 CZ   doub Y N 373 
PHE   CE1 HE1  sing N N 374 
PHE   CE2 CZ   sing Y N 375 
PHE   CE2 HE2  sing N N 376 
PHE   CZ  HZ   sing N N 377 
PHE   OXT HXT  sing N N 378 
PRO   N   CA   sing N N 379 
PRO   N   CD   sing N N 380 
PRO   N   H    sing N N 381 
PRO   CA  C    sing N N 382 
PRO   CA  CB   sing N N 383 
PRO   CA  HA   sing N N 384 
PRO   C   O    doub N N 385 
PRO   C   OXT  sing N N 386 
PRO   CB  CG   sing N N 387 
PRO   CB  HB2  sing N N 388 
PRO   CB  HB3  sing N N 389 
PRO   CG  CD   sing N N 390 
PRO   CG  HG2  sing N N 391 
PRO   CG  HG3  sing N N 392 
PRO   CD  HD2  sing N N 393 
PRO   CD  HD3  sing N N 394 
PRO   OXT HXT  sing N N 395 
SER   N   CA   sing N N 396 
SER   N   H    sing N N 397 
SER   N   H2   sing N N 398 
SER   CA  C    sing N N 399 
SER   CA  CB   sing N N 400 
SER   CA  HA   sing N N 401 
SER   C   O    doub N N 402 
SER   C   OXT  sing N N 403 
SER   CB  OG   sing N N 404 
SER   CB  HB2  sing N N 405 
SER   CB  HB3  sing N N 406 
SER   OG  HG   sing N N 407 
SER   OXT HXT  sing N N 408 
THR   N   CA   sing N N 409 
THR   N   H    sing N N 410 
THR   N   H2   sing N N 411 
THR   CA  C    sing N N 412 
THR   CA  CB   sing N N 413 
THR   CA  HA   sing N N 414 
THR   C   O    doub N N 415 
THR   C   OXT  sing N N 416 
THR   CB  OG1  sing N N 417 
THR   CB  CG2  sing N N 418 
THR   CB  HB   sing N N 419 
THR   OG1 HG1  sing N N 420 
THR   CG2 HG21 sing N N 421 
THR   CG2 HG22 sing N N 422 
THR   CG2 HG23 sing N N 423 
THR   OXT HXT  sing N N 424 
TRP   N   CA   sing N N 425 
TRP   N   H    sing N N 426 
TRP   N   H2   sing N N 427 
TRP   CA  C    sing N N 428 
TRP   CA  CB   sing N N 429 
TRP   CA  HA   sing N N 430 
TRP   C   O    doub N N 431 
TRP   C   OXT  sing N N 432 
TRP   CB  CG   sing N N 433 
TRP   CB  HB2  sing N N 434 
TRP   CB  HB3  sing N N 435 
TRP   CG  CD1  doub Y N 436 
TRP   CG  CD2  sing Y N 437 
TRP   CD1 NE1  sing Y N 438 
TRP   CD1 HD1  sing N N 439 
TRP   CD2 CE2  doub Y N 440 
TRP   CD2 CE3  sing Y N 441 
TRP   NE1 CE2  sing Y N 442 
TRP   NE1 HE1  sing N N 443 
TRP   CE2 CZ2  sing Y N 444 
TRP   CE3 CZ3  doub Y N 445 
TRP   CE3 HE3  sing N N 446 
TRP   CZ2 CH2  doub Y N 447 
TRP   CZ2 HZ2  sing N N 448 
TRP   CZ3 CH2  sing Y N 449 
TRP   CZ3 HZ3  sing N N 450 
TRP   CH2 HH2  sing N N 451 
TRP   OXT HXT  sing N N 452 
TYR   N   CA   sing N N 453 
TYR   N   H    sing N N 454 
TYR   N   H2   sing N N 455 
TYR   CA  C    sing N N 456 
TYR   CA  CB   sing N N 457 
TYR   CA  HA   sing N N 458 
TYR   C   O    doub N N 459 
TYR   C   OXT  sing N N 460 
TYR   CB  CG   sing N N 461 
TYR   CB  HB2  sing N N 462 
TYR   CB  HB3  sing N N 463 
TYR   CG  CD1  doub Y N 464 
TYR   CG  CD2  sing Y N 465 
TYR   CD1 CE1  sing Y N 466 
TYR   CD1 HD1  sing N N 467 
TYR   CD2 CE2  doub Y N 468 
TYR   CD2 HD2  sing N N 469 
TYR   CE1 CZ   doub Y N 470 
TYR   CE1 HE1  sing N N 471 
TYR   CE2 CZ   sing Y N 472 
TYR   CE2 HE2  sing N N 473 
TYR   CZ  OH   sing N N 474 
TYR   OH  HH   sing N N 475 
TYR   OXT HXT  sing N N 476 
VAL   N   CA   sing N N 477 
VAL   N   H    sing N N 478 
VAL   N   H2   sing N N 479 
VAL   CA  C    sing N N 480 
VAL   CA  CB   sing N N 481 
VAL   CA  HA   sing N N 482 
VAL   C   O    doub N N 483 
VAL   C   OXT  sing N N 484 
VAL   CB  CG1  sing N N 485 
VAL   CB  CG2  sing N N 486 
VAL   CB  HB   sing N N 487 
VAL   CG1 HG11 sing N N 488 
VAL   CG1 HG12 sing N N 489 
VAL   CG1 HG13 sing N N 490 
VAL   CG2 HG21 sing N N 491 
VAL   CG2 HG22 sing N N 492 
VAL   CG2 HG23 sing N N 493 
VAL   OXT HXT  sing N N 494 
# 
_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                    9EW0 
_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]   0.011758 
_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]   0.010765 
_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]   0.007731 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
FE 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . THR   A 1 25  ? 17.376  33.774  2.19    1   59.18 ? 10  THR   A N   1 
ATOM   2    C  CA  . THR   A 1 25  ? 16.155  33.639  2.99    1   59.4  ? 10  THR   A CA  1 
ATOM   3    C  C   . THR   A 1 25  ? 16.07   32.258  3.684   1   58.69 ? 10  THR   A C   1 
ATOM   4    O  O   . THR   A 1 25  ? 16.469  31.248  3.094   1   59.53 ? 10  THR   A O   1 
ATOM   5    C  CB  . THR   A 1 25  ? 14.912  33.98   2.125   1   61.31 ? 10  THR   A CB  1 
ATOM   6    O  OG1 . THR   A 1 25  ? 13.971  34.735  2.895   1   62.85 ? 10  THR   A OG1 1 
ATOM   7    C  CG2 . THR   A 1 25  ? 14.241  32.748  1.498   1   61.61 ? 10  THR   A CG2 1 
ATOM   8    N  N   . ILE   A 1 26  ? 15.571  32.215  4.94    1   56.92 ? 11  ILE   A N   1 
ATOM   9    C  CA  . ILE   A 1 26  ? 15.409  30.948  5.67    1   55.69 ? 11  ILE   A CA  1 
ATOM   10   C  C   . ILE   A 1 26  ? 14.216  30.181  5.06    1   54.64 ? 11  ILE   A C   1 
ATOM   11   O  O   . ILE   A 1 26  ? 13.182  30.783  4.763   1   53.97 ? 11  ILE   A O   1 
ATOM   12   C  CB  . ILE   A 1 26  ? 15.214  31.189  7.201   1   55.48 ? 11  ILE   A CB  1 
ATOM   13   C  CG1 . ILE   A 1 26  ? 16.512  31.679  7.859   1   55.49 ? 11  ILE   A CG1 1 
ATOM   14   C  CG2 . ILE   A 1 26  ? 14.661  29.939  7.918   1   55.8  ? 11  ILE   A CG2 1 
ATOM   15   C  CD1 . ILE   A 1 26  ? 16.35   32.149  9.294   1   56.25 ? 11  ILE   A CD1 1 
ATOM   16   N  N   . SER   A 1 27  ? 14.368  28.866  4.865   1   53.96 ? 12  SER   A N   1 
ATOM   17   C  CA  . SER   A 1 27  ? 13.317  28.042  4.29    1   53.91 ? 12  SER   A CA  1 
ATOM   18   C  C   . SER   A 1 27  ? 12.027  28.099  5.1     1   52.94 ? 12  SER   A C   1 
ATOM   19   O  O   . SER   A 1 27  ? 12.063  28.141  6.335   1   53.3  ? 12  SER   A O   1 
ATOM   20   C  CB  . SER   A 1 27  ? 13.791  26.602  4.14    1   56.15 ? 12  SER   A CB  1 
ATOM   21   O  OG  . SER   A 1 27  ? 12.779  25.808  3.542   1   59.87 ? 12  SER   A OG  1 
ATOM   22   N  N   . LYS   A 1 28  ? 10.885  28.142  4.398   1   51.45 ? 13  LYS   A N   1 
ATOM   23   C  CA  . LYS   A 1 28  ? 9.569   28.213  5.023   1   50.1  ? 13  LYS   A CA  1 
ATOM   24   C  C   . LYS   A 1 28  ? 9.297   27.032  5.943   1   48.57 ? 13  LYS   A C   1 
ATOM   25   O  O   . LYS   A 1 28  ? 8.602   27.204  6.943   1   49.24 ? 13  LYS   A O   1 
ATOM   26   C  CB  . LYS   A 1 28  ? 8.461   28.332  3.965   1   51.52 ? 13  LYS   A CB  1 
ATOM   27   N  N   . GLU   A 1 29  ? 9.879   25.856  5.646   1   46.55 ? 14  GLU   A N   1 
ATOM   28   C  CA  . GLU   A 1 29  ? 9.687   24.653  6.445   1   45.8  ? 14  GLU   A CA  1 
ATOM   29   C  C   . GLU   A 1 29  ? 10.267  24.725  7.869   1   44.61 ? 14  GLU   A C   1 
ATOM   30   O  O   . GLU   A 1 29  ? 10.052  23.795  8.655   1   45.28 ? 14  GLU   A O   1 
ATOM   31   C  CB  . GLU   A 1 29  ? 10.229  23.424  5.706   1   48.27 ? 14  GLU   A CB  1 
ATOM   32   C  CG  . GLU   A 1 29  ? 11.738  23.405  5.599   1   53.8  ? 14  GLU   A CG  1 
ATOM   33   N  N   . TYR   A 1 30  ? 10.999  25.799  8.203   1   42.27 ? 15  TYR   A N   1 
ATOM   34   C  CA  . TYR   A 1 30  ? 11.536  25.947  9.551   1   40.61 ? 15  TYR   A CA  1 
ATOM   35   C  C   . TYR   A 1 30  ? 10.594  26.743  10.476  1   40.04 ? 15  TYR   A C   1 
ATOM   36   O  O   . TYR   A 1 30  ? 10.832  26.782  11.674  1   39.75 ? 15  TYR   A O   1 
ATOM   37   C  CB  . TYR   A 1 30  ? 12.974  26.498  9.548   1   39.96 ? 15  TYR   A CB  1 
ATOM   38   C  CG  . TYR   A 1 30  ? 13.964  25.509  8.958   1   40.29 ? 15  TYR   A CG  1 
ATOM   39   C  CD1 . TYR   A 1 30  ? 14.051  24.207  9.44    1   40.66 ? 15  TYR   A CD1 1 
ATOM   40   C  CD2 . TYR   A 1 30  ? 14.78   25.862  7.888   1   40.96 ? 15  TYR   A CD2 1 
ATOM   41   C  CE1 . TYR   A 1 30  ? 14.923  23.283  8.877   1   41.32 ? 15  TYR   A CE1 1 
ATOM   42   C  CE2 . TYR   A 1 30  ? 15.657  24.946  7.317   1   41.57 ? 15  TYR   A CE2 1 
ATOM   43   C  CZ  . TYR   A 1 30  ? 15.73   23.659  7.818   1   42.5  ? 15  TYR   A CZ  1 
ATOM   44   O  OH  . TYR   A 1 30  ? 16.607  22.759  7.267   1   43.7  ? 15  TYR   A OH  1 
ATOM   45   N  N   . HIS   A 1 31  ? 9.51    27.336  9.934   1   39.72 ? 16  HIS   A N   1 
ATOM   46   C  CA  . HIS   A 1 31  ? 8.511   28.066  10.692  1   40.11 ? 16  HIS   A CA  1 
ATOM   47   C  C   . HIS   A 1 31  ? 9.112   29.213  11.473  1   39.01 ? 16  HIS   A C   1 
ATOM   48   O  O   . HIS   A 1 31  ? 8.804   29.412  12.653  1   39.38 ? 16  HIS   A O   1 
ATOM   49   C  CB  . HIS   A 1 31  ? 7.671   27.139  11.596  1   42.61 ? 16  HIS   A CB  1 
ATOM   50   C  CG  . HIS   A 1 31  ? 6.866   26.088  10.877  1   48.3  ? 16  HIS   A CG  1 
ATOM   51   N  ND1 . HIS   A 1 31  ? 6.837   26      9.484   1   51.01 ? 16  HIS   A ND1 1 
ATOM   52   C  CD2 . HIS   A 1 31  ? 6.072   25.118  11.39   1   50.23 ? 16  HIS   A CD2 1 
ATOM   53   C  CE1 . HIS   A 1 31  ? 6.063   24.963  9.209   1   51.69 ? 16  HIS   A CE1 1 
ATOM   54   N  NE2 . HIS   A 1 31  ? 5.568   24.409  10.321  1   51.66 ? 16  HIS   A NE2 1 
ATOM   55   N  N   . ILE   A 1 32  ? 9.967   29.97   10.812  1   38.02 ? 17  ILE   A N   1 
ATOM   56   C  CA  . ILE   A 1 32  ? 10.574  31.141  11.41   1   38.33 ? 17  ILE   A CA  1 
ATOM   57   C  C   . ILE   A 1 32  ? 10.032  32.342  10.643  1   38.66 ? 17  ILE   A C   1 
ATOM   58   O  O   . ILE   A 1 32  ? 10.11   32.394  9.412   1   39.19 ? 17  ILE   A O   1 
ATOM   59   C  CB  . ILE   A 1 32  ? 12.11   31.046  11.4    1   38.18 ? 17  ILE   A CB  1 
ATOM   60   C  CG1 . ILE   A 1 32  ? 12.557  29.862  12.245  1   38.86 ? 17  ILE   A CG1 1 
ATOM   61   C  CG2 . ILE   A 1 32  ? 12.719  32.34   11.921  1   38.5  ? 17  ILE   A CG2 1 
ATOM   62   C  CD1 . ILE   A 1 32  ? 13.9    29.463  11.97   1   41.44 ? 17  ILE   A CD1 1 
ATOM   63   N  N   . ASP   A 1 33  ? 9.42    33.257  11.359  1   37.91 ? 18  ASP   A N   1 
ATOM   64   C  CA  . ASP   A 1 33  ? 8.776   34.405  10.751  1   37.77 ? 18  ASP   A CA  1 
ATOM   65   C  C   . ASP   A 1 33  ? 9.723   35.571  10.684  1   36.61 ? 18  ASP   A C   1 
ATOM   66   O  O   . ASP   A 1 33  ? 10.489  35.797  11.617  1   35.46 ? 18  ASP   A O   1 
ATOM   67   C  CB  . ASP   A 1 33  ? 7.504   34.752  11.541  1   39.04 ? 18  ASP   A CB  1 
ATOM   68   C  CG  . ASP   A 1 33  ? 6.665   35.801  10.865  1   42.12 ? 18  ASP   A CG  1 
ATOM   69   O  OD1 . ASP   A 1 33  ? 6.038   35.477  9.837   1   42.68 ? 18  ASP   A OD1 1 
ATOM   70   O  OD2 . ASP   A 1 33  ? 6.653   36.954  11.355  1   42.62 ? 18  ASP   A OD2 1 
ATOM   71   N  N   . GLU   A 1 34  ? 9.672   36.33   9.591   1   36.65 ? 19  GLU   A N   1 
ATOM   72   C  CA  . GLU   A 1 34  ? 10.57   37.473  9.429   1   37.01 ? 19  GLU   A CA  1 
ATOM   73   C  C   . GLU   A 1 34  ? 10.347  38.531  10.49   1   36.9  ? 19  GLU   A C   1 
ATOM   74   O  O   . GLU   A 1 34  ? 11.303  39.199  10.894  1   38.24 ? 19  GLU   A O   1 
ATOM   75   C  CB  . GLU   A 1 34  ? 10.441  38.074  8.019   1   39.26 ? 19  GLU   A CB  1 
ATOM   76   N  N   . GLU   A 1 35  ? 9.102   38.685  10.955  1   35.7  ? 20  GLU   A N   1 
ATOM   77   C  CA  . GLU   A 1 35  ? 8.801   39.716  11.94   1   34.35 ? 20  GLU   A CA  1 
ATOM   78   C  C   . GLU   A 1 35  ? 8.902   39.236  13.377  1   32.97 ? 20  GLU   A C   1 
ATOM   79   O  O   . GLU   A 1 35  ? 9.413   39.971  14.235  1   34.46 ? 20  GLU   A O   1 
ATOM   80   C  CB  . GLU   A 1 35  ? 7.415   40.323  11.665  1   35.91 ? 20  GLU   A CB  1 
ATOM   81   C  CG  . GLU   A 1 35  ? 7.097   41.515  12.55   1   40.34 ? 20  GLU   A CG  1 
ATOM   82   C  CD  . GLU   A 1 35  ? 5.697   42.063  12.38   1   45.32 ? 20  GLU   A CD  1 
ATOM   83   O  OE1 . GLU   A 1 35  ? 4.793   41.289  11.985  1   46.95 ? 20  GLU   A OE1 1 
ATOM   84   O  OE2 . GLU   A 1 35  ? 5.509   43.273  12.638  1   45.75 ? 20  GLU   A OE2 1 
ATOM   85   N  N   . VAL   A 1 36  ? 8.384   38.047  13.663  1   30.99 ? 21  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 36  ? 8.323   37.581  15.049  1   30.31 ? 21  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 36  ? 9.235   36.4    15.365  1   31.41 ? 21  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 36  ? 9.265   35.993  16.52   1   32.6  ? 21  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 36  ? 6.863   37.293  15.505  1   28.63 ? 21  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 36  ? 6.015   38.557  15.444  1   29.31 ? 21  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 36  ? 6.238   36.18   14.675  1   26.72 ? 21  VAL   A CG2 1 
ATOM   92   N  N   . GLY   A 1 37  ? 9.953   35.87   14.382  1   31.33 ? 22  GLY   A N   1 
ATOM   93   C  CA  . GLY   A 1 37  ? 10.948  34.817  14.581  1   32.04 ? 22  GLY   A CA  1 
ATOM   94   C  C   . GLY   A 1 37  ? 10.395  33.455  14.931  1   32.49 ? 22  GLY   A C   1 
ATOM   95   O  O   . GLY   A 1 37  ? 9.614   32.881  14.165  1   33.25 ? 22  GLY   A O   1 
ATOM   96   N  N   . PHE   A 1 38  ? 10.828  32.904  16.077  1   32.07 ? 23  PHE   A N   1 
ATOM   97   C  CA  . PHE   A 1 38  ? 10.3    31.623  16.526  1   32.12 ? 23  PHE   A CA  1 
ATOM   98   C  C   . PHE   A 1 38  ? 8.847   31.75   17.05   1   32.57 ? 23  PHE   A C   1 
ATOM   99   O  O   . PHE   A 1 38  ? 8.182   30.735  17.208  1   33.17 ? 23  PHE   A O   1 
ATOM   100  C  CB  . PHE   A 1 38  ? 11.216  30.976  17.572  1   31.98 ? 23  PHE   A CB  1 
ATOM   101  C  CG  . PHE   A 1 38  ? 12.565  30.598  16.997  1   32.23 ? 23  PHE   A CG  1 
ATOM   102  C  CD1 . PHE   A 1 38  ? 12.693  29.519  16.133  1   32.22 ? 23  PHE   A CD1 1 
ATOM   103  C  CD2 . PHE   A 1 38  ? 13.692  31.362  17.269  1   32.85 ? 23  PHE   A CD2 1 
ATOM   104  C  CE1 . PHE   A 1 38  ? 13.941  29.169  15.612  1   33.2  ? 23  PHE   A CE1 1 
ATOM   105  C  CE2 . PHE   A 1 38  ? 14.937  31.028  16.722  1   33.41 ? 23  PHE   A CE2 1 
ATOM   106  C  CZ  . PHE   A 1 38  ? 15.05   29.941  15.888  1   33.11 ? 23  PHE   A CZ  1 
ATOM   107  N  N   . ALA   A 1 39  ? 8.368   32.969  17.353  1   31.61 ? 24  ALA   A N   1 
ATOM   108  C  CA  . ALA   A 1 39  ? 6.996   33.147  17.81   1   31.61 ? 24  ALA   A CA  1 
ATOM   109  C  C   . ALA   A 1 39  ? 5.997   32.745  16.725  1   31.88 ? 24  ALA   A C   1 
ATOM   110  O  O   . ALA   A 1 39  ? 6.298   32.844  15.524  1   30.51 ? 24  ALA   A O   1 
ATOM   111  C  CB  . ALA   A 1 39  ? 6.756   34.587  18.222  1   31.49 ? 24  ALA   A CB  1 
ATOM   112  N  N   . LEU   A 1 40  ? 4.824   32.243  17.145  1   32.97 ? 25  LEU   A N   1 
ATOM   113  C  CA  . LEU   A 1 40  ? 3.76    31.89   16.206  1   33.02 ? 25  LEU   A CA  1 
ATOM   114  C  C   . LEU   A 1 40  ? 3.144   33.205  15.704  1   32.08 ? 25  LEU   A C   1 
ATOM   115  O  O   . LEU   A 1 40  ? 2.693   34.031  16.51   1   31.59 ? 25  LEU   A O   1 
ATOM   116  C  CB  . LEU   A 1 40  ? 2.724   31.018  16.904  1   33.55 ? 25  LEU   A CB  1 
ATOM   117  C  CG  . LEU   A 1 40  ? 1.571   30.495  16.059  1   35.28 ? 25  LEU   A CG  1 
ATOM   118  C  CD1 . LEU   A 1 40  ? 2.069   29.542  14.968  1   36.08 ? 25  LEU   A CD1 1 
ATOM   119  C  CD2 . LEU   A 1 40  ? 0.571   29.806  16.935  1   35.57 ? 25  LEU   A CD2 1 
ATOM   120  N  N   . PRO   A 1 41  ? 3.232   33.493  14.39   1   32.08 ? 26  PRO   A N   1 
ATOM   121  C  CA  . PRO   A 1 41  ? 2.693   34.77   13.902  1   32.95 ? 26  PRO   A CA  1 
ATOM   122  C  C   . PRO   A 1 41  ? 1.179   34.787  14.053  1   34.01 ? 26  PRO   A C   1 
ATOM   123  O  O   . PRO   A 1 41  ? 0.541   33.757  13.82   1   34.07 ? 26  PRO   A O   1 
ATOM   124  C  CB  . PRO   A 1 41  ? 3.095   34.8    12.428  1   33.81 ? 26  PRO   A CB  1 
ATOM   125  C  CG  . PRO   A 1 41  ? 3.409   33.403  12.072  1   33.97 ? 26  PRO   A CG  1 
ATOM   126  C  CD  . PRO   A 1 41  ? 3.793   32.673  13.304  1   31.69 ? 26  PRO   A CD  1 
ATOM   127  N  N   A ASN   A 1 42  ? 0.59    35.926  14.48   0.5 34.01 ? 27  ASN   A N   1 
ATOM   128  N  N   B ASN   A 1 42  ? 0.619   35.919  14.531  0.5 34.24 ? 27  ASN   A N   1 
ATOM   129  C  CA  A ASN   A 1 42  ? -0.869  36.09   14.668  0.5 34.46 ? 27  ASN   A CA  1 
ATOM   130  C  CA  B ASN   A 1 42  ? -0.819  36.135  14.774  0.5 34.96 ? 27  ASN   A CA  1 
ATOM   131  C  C   A ASN   A 1 42  ? -1.581  34.819  15.173  0.5 34.32 ? 27  ASN   A C   1 
ATOM   132  C  C   B ASN   A 1 42  ? -1.579  34.854  15.191  0.5 34.56 ? 27  ASN   A C   1 
ATOM   133  O  O   A ASN   A 1 42  ? -2.24   34.139  14.38   0.5 34.74 ? 27  ASN   A O   1 
ATOM   134  O  O   B ASN   A 1 42  ? -2.231  34.208  14.371  0.5 35.02 ? 27  ASN   A O   1 
ATOM   135  C  CB  A ASN   A 1 42  ? -1.524  36.586  13.356  0.5 35.76 ? 27  ASN   A CB  1 
ATOM   136  C  CB  B ASN   A 1 42  ? -1.469  36.819  13.569  0.5 37.01 ? 27  ASN   A CB  1 
ATOM   137  C  CG  A ASN   A 1 42  ? -2.973  37.038  13.468  0.5 38.59 ? 27  ASN   A CG  1 
ATOM   138  C  CG  B ASN   A 1 42  ? -0.968  38.236  13.368  0.5 41.14 ? 27  ASN   A CG  1 
ATOM   139  O  OD1 A ASN   A 1 42  ? -3.715  37.059  12.479  0.5 39.24 ? 27  ASN   A OD1 1 
ATOM   140  O  OD1 B ASN   A 1 42  ? -1.133  39.117  14.234  0.5 42.92 ? 27  ASN   A OD1 1 
ATOM   141  N  ND2 A ASN   A 1 42  ? -3.415  37.419  14.666  0.5 39.6  ? 27  ASN   A ND2 1 
ATOM   142  N  ND2 B ASN   A 1 42  ? -0.326  38.485  12.229  0.5 41.28 ? 27  ASN   A ND2 1 
ATOM   143  N  N   . PRO   A 1 43  ? -1.349  34.398  16.432  1   33.46 ? 28  PRO   A N   1 
ATOM   144  C  CA  . PRO   A 1 43  ? -1.993  33.164  16.899  1   33.29 ? 28  PRO   A CA  1 
ATOM   145  C  C   . PRO   A 1 43  ? -3.52   33.273  16.883  1   32.8  ? 28  PRO   A C   1 
ATOM   146  O  O   . PRO   A 1 43  ? -4.073  34.363  16.985  1   32.43 ? 28  PRO   A O   1 
ATOM   147  C  CB  . PRO   A 1 43  ? -1.491  33.027  18.341  1   33.34 ? 28  PRO   A CB  1 
ATOM   148  C  CG  . PRO   A 1 43  ? -0.235  33.868  18.399  1   33.62 ? 28  PRO   A CG  1 
ATOM   149  C  CD  . PRO   A 1 43  ? -0.559  35.028  17.51   1   32.63 ? 28  PRO   A CD  1 
ATOM   150  N  N   . GLN   A 1 44  ? -4.182  32.144  16.743  1   32.91 ? 29  GLN   A N   1 
ATOM   151  C  CA  . GLN   A 1 44  ? -5.645  32.049  16.765  1   33.8  ? 29  GLN   A CA  1 
ATOM   152  C  C   . GLN   A 1 44  ? -6.127  32.286  18.204  1   34.3  ? 29  GLN   A C   1 
ATOM   153  O  O   . GLN   A 1 44  ? -5.537  31.731  19.119  1   33.66 ? 29  GLN   A O   1 
ATOM   154  C  CB  . GLN   A 1 44  ? -6.057  30.65   16.299  1   35.64 ? 29  GLN   A CB  1 
ATOM   155  C  CG  . GLN   A 1 44  ? -7.532  30.522  15.971  1   41.92 ? 29  GLN   A CG  1 
ATOM   156  C  CD  . GLN   A 1 44  ? -7.776  29.349  15.061  1   49.56 ? 29  GLN   A CD  1 
ATOM   157  O  OE1 . GLN   A 1 44  ? -7.066  29.155  14.052  1   51.99 ? 29  GLN   A OE1 1 
ATOM   158  N  NE2 . GLN   A 1 44  ? -8.804  28.55   15.398  1   49.85 ? 29  GLN   A NE2 1 
ATOM   159  N  N   . GLU   A 1 45  ? -7.176  33.108  18.412  1   34.64 ? 30  GLU   A N   1 
ATOM   160  C  CA  A GLU   A 1 45  ? -7.701  33.4    19.743  0.5 34.71 ? 30  GLU   A CA  1 
ATOM   161  C  CA  B GLU   A 1 45  ? -7.682  33.364  19.767  0.5 34.98 ? 30  GLU   A CA  1 
ATOM   162  C  C   . GLU   A 1 45  ? -8.918  32.529  20.1    1   35.7  ? 30  GLU   A C   1 
ATOM   163  O  O   . GLU   A 1 45  ? -9.182  32.274  21.276  1   36.82 ? 30  GLU   A O   1 
ATOM   164  C  CB  A GLU   A 1 45  ? -8.089  34.886  19.816  0.5 35.35 ? 30  GLU   A CB  1 
ATOM   165  C  CB  B GLU   A 1 45  ? -7.974  34.864  20.023  0.5 36.56 ? 30  GLU   A CB  1 
ATOM   166  C  CG  A GLU   A 1 45  ? -6.946  35.817  19.459  0.5 35.84 ? 30  GLU   A CG  1 
ATOM   167  C  CG  B GLU   A 1 45  ? -8.384  35.131  21.473  0.5 38.87 ? 30  GLU   A CG  1 
ATOM   168  C  CD  A GLU   A 1 45  ? -7.349  37.249  19.17   0.5 38.35 ? 30  GLU   A CD  1 
ATOM   169  C  CD  B GLU   A 1 45  ? -8.942  36.489  21.858  0.5 40.42 ? 30  GLU   A CD  1 
ATOM   170  O  OE1 A GLU   A 1 45  ? -6.729  37.866  18.275  0.5 36.66 ? 30  GLU   A OE1 1 
ATOM   171  O  OE1 B GLU   A 1 45  ? -9.478  37.192  20.974  0.5 41.19 ? 30  GLU   A OE1 1 
ATOM   172  O  OE2 A GLU   A 1 45  ? -8.274  37.759  19.844  0.5 39.18 ? 30  GLU   A OE2 1 
ATOM   173  O  OE2 B GLU   A 1 45  ? -8.863  36.84   23.057  0.5 40.11 ? 30  GLU   A OE2 1 
ATOM   174  N  N   . ASN   A 1 46  ? -9.68   32.093  19.09   1   35.72 ? 31  ASN   A N   1 
ATOM   175  C  CA  . ASN   A 1 46  ? -10.892 31.316  19.33   1   36.08 ? 31  ASN   A CA  1 
ATOM   176  C  C   . ASN   A 1 46  ? -10.849 29.994  18.621  1   35.95 ? 31  ASN   A C   1 
ATOM   177  O  O   . ASN   A 1 46  ? -10.345 29.893  17.509  1   34.7  ? 31  ASN   A O   1 
ATOM   178  C  CB  . ASN   A 1 46  ? -12.129 32.102  18.848  1   37.71 ? 31  ASN   A CB  1 
ATOM   179  C  CG  . ASN   A 1 46  ? -12.227 33.502  19.385  1   41.69 ? 31  ASN   A CG  1 
ATOM   180  O  OD1 . ASN   A 1 46  ? -12.415 33.712  20.594  1   43.79 ? 31  ASN   A OD1 1 
ATOM   181  N  ND2 . ASN   A 1 46  ? -12.076 34.499  18.495  1   42.18 ? 31  ASN   A ND2 1 
ATOM   182  N  N   . LEU   A 1 47  ? -11.355 28.969  19.277  1   37.57 ? 32  LEU   A N   1 
ATOM   183  C  CA  . LEU   A 1 47  ? -11.452 27.644  18.67   1   39.91 ? 32  LEU   A CA  1 
ATOM   184  C  C   . LEU   A 1 47  ? -12.874 27.523  18.033  1   42.24 ? 32  LEU   A C   1 
ATOM   185  O  O   . LEU   A 1 47  ? -13.794 28.263  18.419  1   42.58 ? 32  LEU   A O   1 
ATOM   186  C  CB  . LEU   A 1 47  ? -11.321 26.583  19.78   1   40.03 ? 32  LEU   A CB  1 
ATOM   187  C  CG  . LEU   A 1 47  ? -9.911  26.227  20.268  1   41.65 ? 32  LEU   A CG  1 
ATOM   188  C  CD1 . LEU   A 1 47  ? -9.971  25.169  21.375  1   41.67 ? 32  LEU   A CD1 1 
ATOM   189  C  CD2 . LEU   A 1 47  ? -9.005  25.792  19.114  1   42.27 ? 32  LEU   A CD2 1 
ATOM   190  N  N   . PRO   A 1 48  ? -13.115 26.549  17.123  1   43.6  ? 33  PRO   A N   1 
ATOM   191  C  CA  . PRO   A 1 48  ? -14.494 26.336  16.629  1   44.09 ? 33  PRO   A CA  1 
ATOM   192  C  C   . PRO   A 1 48  ? -15.483 26.095  17.795  1   44.82 ? 33  PRO   A C   1 
ATOM   193  O  O   . PRO   A 1 48  ? -15.083 25.553  18.835  1   45.29 ? 33  PRO   A O   1 
ATOM   194  C  CB  . PRO   A 1 48  ? -14.361 25.075  15.763  1   44.8  ? 33  PRO   A CB  1 
ATOM   195  C  CG  . PRO   A 1 48  ? -12.903 25.073  15.322  1   45.34 ? 33  PRO   A CG  1 
ATOM   196  C  CD  . PRO   A 1 48  ? -12.173 25.561  16.554  1   43.54 ? 33  PRO   A CD  1 
ATOM   197  N  N   . ASP   A 1 49  ? -16.757 26.52   17.638  1   44.45 ? 34  ASP   A N   1 
ATOM   198  C  CA  . ASP   A 1 49  ? -17.816 26.396  18.649  1   44.45 ? 34  ASP   A CA  1 
ATOM   199  C  C   . ASP   A 1 49  ? -17.896 25.024  19.306  1   42.3  ? 34  ASP   A C   1 
ATOM   200  O  O   . ASP   A 1 49  ? -18.287 24.927  20.465  1   42.39 ? 34  ASP   A O   1 
ATOM   201  C  CB  . ASP   A 1 49  ? -19.196 26.772  18.054  1   48.37 ? 34  ASP   A CB  1 
ATOM   202  C  CG  . ASP   A 1 49  ? -19.264 28.195  17.533  1   58.46 ? 34  ASP   A CG  1 
ATOM   203  O  OD1 . ASP   A 1 49  ? -19.107 29.146  18.357  1   60.22 ? 34  ASP   A OD1 1 
ATOM   204  O  OD2 . ASP   A 1 49  ? -19.476 28.368  16.305  1   62.29 ? 34  ASP   A OD2 1 
ATOM   205  N  N   . PHE   A 1 50  ? -17.503 23.976  18.59   1   40.9  ? 35  PHE   A N   1 
ATOM   206  C  CA  . PHE   A 1 50  ? -17.507 22.607  19.091  1   40.87 ? 35  PHE   A CA  1 
ATOM   207  C  C   . PHE   A 1 50  ? -16.707 22.483  20.401  1   41.19 ? 35  PHE   A C   1 
ATOM   208  O  O   . PHE   A 1 50  ? -17.095 21.721  21.284  1   42.06 ? 35  PHE   A O   1 
ATOM   209  C  CB  . PHE   A 1 50  ? -16.909 21.691  18.008  1   40.87 ? 35  PHE   A CB  1 
ATOM   210  C  CG  . PHE   A 1 50  ? -16.854 20.218  18.325  1   42.35 ? 35  PHE   A CG  1 
ATOM   211  C  CD1 . PHE   A 1 50  ? -17.98  19.423  18.197  1   44.16 ? 35  PHE   A CD1 1 
ATOM   212  C  CD2 . PHE   A 1 50  ? -15.658 19.607  18.641  1   43.05 ? 35  PHE   A CD2 1 
ATOM   213  C  CE1 . PHE   A 1 50  ? -17.917 18.053  18.449  1   44.81 ? 35  PHE   A CE1 1 
ATOM   214  C  CE2 . PHE   A 1 50  ? -15.597 18.246  18.893  1   44.11 ? 35  PHE   A CE2 1 
ATOM   215  C  CZ  . PHE   A 1 50  ? -16.725 17.476  18.787  1   44.44 ? 35  PHE   A CZ  1 
ATOM   216  N  N   . TYR   A 1 51  ? -15.631 23.294  20.554  1   39.96 ? 36  TYR   A N   1 
ATOM   217  C  CA  . TYR   A 1 51  ? -14.751 23.24   21.716  1   39.17 ? 36  TYR   A CA  1 
ATOM   218  C  C   . TYR   A 1 51  ? -15.056 24.285  22.787  1   39.26 ? 36  TYR   A C   1 
ATOM   219  O  O   . TYR   A 1 51  ? -14.198 24.53   23.643  1   39.44 ? 36  TYR   A O   1 
ATOM   220  C  CB  . TYR   A 1 51  ? -13.294 23.387  21.254  1   38.11 ? 36  TYR   A CB  1 
ATOM   221  C  CG  . TYR   A 1 51  ? -12.879 22.325  20.257  1   36.88 ? 36  TYR   A CG  1 
ATOM   222  C  CD1 . TYR   A 1 51  ? -12.702 21.01   20.649  1   36.57 ? 36  TYR   A CD1 1 
ATOM   223  C  CD2 . TYR   A 1 51  ? -12.748 22.622  18.905  1   36.73 ? 36  TYR   A CD2 1 
ATOM   224  C  CE1 . TYR   A 1 51  ? -12.31  20.031  19.741  1   36.67 ? 36  TYR   A CE1 1 
ATOM   225  C  CE2 . TYR   A 1 51  ? -12.413 21.637  17.977  1   36.63 ? 36  TYR   A CE2 1 
ATOM   226  C  CZ  . TYR   A 1 51  ? -12.183 20.345  18.402  1   36.7  ? 36  TYR   A CZ  1 
ATOM   227  O  OH  . TYR   A 1 51  ? -11.845 19.358  17.504  1   36.94 ? 36  TYR   A OH  1 
ATOM   228  N  N   . ASN   A 1 52  ? -16.258 24.893  22.764  1   38.67 ? 37  ASN   A N   1 
ATOM   229  C  CA  . ASN   A 1 52  ? -16.656 25.934  23.724  1   38.33 ? 37  ASN   A CA  1 
ATOM   230  C  C   . ASN   A 1 52  ? -16.453 25.504  25.195  1   36.03 ? 37  ASN   A C   1 
ATOM   231  O  O   . ASN   A 1 52  ? -16.16  26.353  26.046  1   35.84 ? 37  ASN   A O   1 
ATOM   232  C  CB  . ASN   A 1 52  ? -18.128 26.362  23.507  1   41.79 ? 37  ASN   A CB  1 
ATOM   233  C  CG  . ASN   A 1 52  ? -18.334 27.458  22.472  1   47.62 ? 37  ASN   A CG  1 
ATOM   234  O  OD1 . ASN   A 1 52  ? -17.381 28.018  21.896  1   48.61 ? 37  ASN   A OD1 1 
ATOM   235  N  ND2 . ASN   A 1 52  ? -19.602 27.789  22.209  1   49.13 ? 37  ASN   A ND2 1 
ATOM   236  N  N   . ASP   A 1 53  ? -16.645 24.219  25.497  1   33.86 ? 38  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 53  ? -16.484 23.725  26.87   1   33.31 ? 38  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 53  ? -15.008 23.771  27.313  1   33.13 ? 38  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 53  ? -14.726 23.942  28.502  1   33.02 ? 38  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 53  ? -17.011 22.278  26.999  1   35.28 ? 38  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 53  ? -18.533 22.146  26.859  1   39.1  ? 38  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 53  ? -19.242 23.119  27.161  1   37.28 ? 38  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 53  ? -18.997 21.068  26.445  1   42.32 ? 38  ASP   A OD2 1 
ATOM   244  N  N   . TRP   A 1 54  ? -14.078 23.558  26.373  1   32.25 ? 39  TRP   A N   1 
ATOM   245  C  CA  . TRP   A 1 54  ? -12.642 23.651  26.676  1   32.04 ? 39  TRP   A CA  1 
ATOM   246  C  C   . TRP   A 1 54  ? -12.325 25.098  26.916  1   32.41 ? 39  TRP   A C   1 
ATOM   247  O  O   . TRP   A 1 54  ? -11.759 25.423  27.949  1   33.2  ? 39  TRP   A O   1 
ATOM   248  C  CB  . TRP   A 1 54  ? -11.799 23.175  25.486  1   31.39 ? 39  TRP   A CB  1 
ATOM   249  C  CG  . TRP   A 1 54  ? -11.717 21.701  25.26   1   31.71 ? 39  TRP   A CG  1 
ATOM   250  C  CD1 . TRP   A 1 54  ? -12.263 20.709  26.021  1   32.68 ? 39  TRP   A CD1 1 
ATOM   251  C  CD2 . TRP   A 1 54  ? -11.005 21.053  24.2    1   32.15 ? 39  TRP   A CD2 1 
ATOM   252  N  NE1 . TRP   A 1 54  ? -11.969 19.478  25.473  1   33.34 ? 39  TRP   A NE1 1 
ATOM   253  C  CE2 . TRP   A 1 54  ? -11.207 19.663  24.345  1   33.11 ? 39  TRP   A CE2 1 
ATOM   254  C  CE3 . TRP   A 1 54  ? -10.249 21.515  23.113  1   32.45 ? 39  TRP   A CE3 1 
ATOM   255  C  CZ2 . TRP   A 1 54  ? -10.646 18.728  23.46   1   33.48 ? 39  TRP   A CZ2 1 
ATOM   256  C  CZ3 . TRP   A 1 54  ? -9.682  20.587  22.256  1   33.39 ? 39  TRP   A CZ3 1 
ATOM   257  C  CH2 . TRP   A 1 54  ? -9.911  19.215  22.413  1   33.37 ? 39  TRP   A CH2 1 
ATOM   258  N  N   . MET   A 1 55  ? -12.729 25.978  25.98   1   32.5  ? 40  MET   A N   1 
ATOM   259  C  CA  . MET   A 1 55  ? -12.45  27.414  26.062  1   33.58 ? 40  MET   A CA  1 
ATOM   260  C  C   . MET   A 1 55  ? -12.978 28.049  27.31   1   33.55 ? 40  MET   A C   1 
ATOM   261  O  O   . MET   A 1 55  ? -12.28  28.879  27.908  1   34.58 ? 40  MET   A O   1 
ATOM   262  C  CB  . MET   A 1 55  ? -12.985 28.169  24.841  1   35.48 ? 40  MET   A CB  1 
ATOM   263  C  CG  . MET   A 1 55  ? -12.199 27.935  23.571  1   39.57 ? 40  MET   A CG  1 
ATOM   264  S  SD  . MET   A 1 55  ? -10.544 28.715  23.406  1   46.39 ? 40  MET   A SD  1 
ATOM   265  C  CE  . MET   A 1 55  ? -10.638 30.06   24.54   1   28.03 ? 40  MET   A CE  1 
ATOM   266  N  N   . PHE   A 1 56  ? -14.196 27.668  27.742  1   31.96 ? 41  PHE   A N   1 
ATOM   267  C  CA  . PHE   A 1 56  ? -14.745 28.244  28.975  1   31.18 ? 41  PHE   A CA  1 
ATOM   268  C  C   . PHE   A 1 56  ? -13.82  27.965  30.175  1   30.27 ? 41  PHE   A C   1 
ATOM   269  O  O   . PHE   A 1 56  ? -13.533 28.872  30.956  1   30.4  ? 41  PHE   A O   1 
ATOM   270  C  CB  . PHE   A 1 56  ? -16.207 27.776  29.258  1   30.59 ? 41  PHE   A CB  1 
ATOM   271  C  CG  . PHE   A 1 56  ? -16.638 28.167  30.663  1   29.74 ? 41  PHE   A CG  1 
ATOM   272  C  CD1 . PHE   A 1 56  ? -16.888 29.482  30.983  1   30.43 ? 41  PHE   A CD1 1 
ATOM   273  C  CD2 . PHE   A 1 56  ? -16.657 27.233  31.685  1   30.36 ? 41  PHE   A CD2 1 
ATOM   274  C  CE1 . PHE   A 1 56  ? -17.213 29.846  32.295  1   31.04 ? 41  PHE   A CE1 1 
ATOM   275  C  CE2 . PHE   A 1 56  ? -16.981 27.596  32.987  1   30.47 ? 41  PHE   A CE2 1 
ATOM   276  C  CZ  . PHE   A 1 56  ? -17.22  28.901  33.294  1   30.05 ? 41  PHE   A CZ  1 
ATOM   277  N  N   . ILE   A 1 57  ? -13.401 26.714  30.337  1   30.11 ? 42  ILE   A N   1 
ATOM   278  C  CA  . ILE   A 1 57  ? -12.539 26.343  31.467  1   30.41 ? 42  ILE   A CA  1 
ATOM   279  C  C   . ILE   A 1 57  ? -11.187 27.095  31.427  1   29.48 ? 42  ILE   A C   1 
ATOM   280  O  O   . ILE   A 1 57  ? -10.805 27.738  32.402  1   29.22 ? 42  ILE   A O   1 
ATOM   281  C  CB  . ILE   A 1 57  ? -12.341 24.808  31.496  1   31.94 ? 42  ILE   A CB  1 
ATOM   282  C  CG1 . ILE   A 1 57  ? -13.681 24.083  31.705  1   33.17 ? 42  ILE   A CG1 1 
ATOM   283  C  CG2 . ILE   A 1 57  ? -11.312 24.431  32.558  1   32.84 ? 42  ILE   A CG2 1 
ATOM   284  C  CD1 . ILE   A 1 57  ? -13.562 22.547  31.651  1   36.12 ? 42  ILE   A CD1 1 
ATOM   285  N  N   . ALA   A 1 58  ? -10.524 27.077  30.266  1   29.05 ? 43  ALA   A N   1 
ATOM   286  C  CA  . ALA   A 1 58  ? -9.225  27.713  30.05   1   29.89 ? 43  ALA   A CA  1 
ATOM   287  C  C   . ALA   A 1 58  ? -9.287  29.221  30.281  1   30.67 ? 43  ALA   A C   1 
ATOM   288  O  O   . ALA   A 1 58  ? -8.372  29.782  30.883  1   30.92 ? 43  ALA   A O   1 
ATOM   289  C  CB  . ALA   A 1 58  ? -8.741  27.429  28.636  1   29.59 ? 43  ALA   A CB  1 
ATOM   290  N  N   . LYS   A 1 59  ? -10.344 29.874  29.804  1   30.57 ? 44  LYS   A N   1 
ATOM   291  C  CA  . LYS   A 1 59  ? -10.485 31.317  29.969  1   30.51 ? 44  LYS   A CA  1 
ATOM   292  C  C   . LYS   A 1 59  ? -10.79  31.729  31.417  1   29.93 ? 44  LYS   A C   1 
ATOM   293  O  O   . LYS   A 1 59  ? -10.641 32.911  31.755  1   29.73 ? 44  LYS   A O   1 
ATOM   294  C  CB  . LYS   A 1 59  ? -11.547 31.877  29.016  1   32.78 ? 44  LYS   A CB  1 
ATOM   295  C  CG  . LYS   A 1 59  ? -11.07  31.996  27.573  1   40.25 ? 44  LYS   A CG  1 
ATOM   296  C  CD  . LYS   A 1 59  ? -12.126 32.61   26.629  1   48.8  ? 44  LYS   A CD  1 
ATOM   297  C  CE  . LYS   A 1 59  ? -12.556 34.034  26.981  1   55.19 ? 44  LYS   A CE  1 
ATOM   298  N  NZ  . LYS   A 1 59  ? -12.495 34.972  25.809  1   57.86 ? 44  LYS   A NZ  1 
ATOM   299  N  N   . HIS   A 1 60  ? -11.181 30.781  32.274  1   28.64 ? 45  HIS   A N   1 
ATOM   300  C  CA  . HIS   A 1 60  ? -11.603 31.106  33.645  1   29.09 ? 45  HIS   A CA  1 
ATOM   301  C  C   . HIS   A 1 60  ? -10.872 30.335  34.692  1   28.94 ? 45  HIS   A C   1 
ATOM   302  O  O   . HIS   A 1 60  ? -11.401 30.149  35.8    1   28.46 ? 45  HIS   A O   1 
ATOM   303  C  CB  . HIS   A 1 60  ? -13.126 30.933  33.807  1   30.81 ? 45  HIS   A CB  1 
ATOM   304  C  CG  . HIS   A 1 60  ? -13.906 31.852  32.915  1   34.17 ? 45  HIS   A CG  1 
ATOM   305  N  ND1 . HIS   A 1 60  ? -14.374 31.43   31.68   1   36.11 ? 45  HIS   A ND1 1 
ATOM   306  C  CD2 . HIS   A 1 60  ? -14.195 33.169  33.067  1   35.65 ? 45  HIS   A CD2 1 
ATOM   307  C  CE1 . HIS   A 1 60  ? -14.963 32.484  31.131  1   36.67 ? 45  HIS   A CE1 1 
ATOM   308  N  NE2 . HIS   A 1 60  ? -14.879 33.559  31.927  1   36.93 ? 45  HIS   A NE2 1 
ATOM   309  N  N   . LEU   A 1 61  ? -9.599  29.938  34.397  1   28.69 ? 46  LEU   A N   1 
ATOM   310  C  CA  . LEU   A 1 61  ? -8.78   29.233  35.378  1   28.76 ? 46  LEU   A CA  1 
ATOM   311  C  C   . LEU   A 1 61  ? -8.639  29.992  36.687  1   29.4  ? 46  LEU   A C   1 
ATOM   312  O  O   . LEU   A 1 61  ? -8.838  29.381  37.73   1   30.86 ? 46  LEU   A O   1 
ATOM   313  C  CB  . LEU   A 1 61  ? -7.388  28.849  34.826  1   29.3  ? 46  LEU   A CB  1 
ATOM   314  C  CG  . LEU   A 1 61  ? -7.397  27.796  33.723  1   30.05 ? 46  LEU   A CG  1 
ATOM   315  C  CD1 . LEU   A 1 61  ? -5.983  27.593  33.152  1   30.32 ? 46  LEU   A CD1 1 
ATOM   316  C  CD2 . LEU   A 1 61  ? -8.074  26.506  34.19   1   29.7  ? 46  LEU   A CD2 1 
ATOM   317  N  N   . PRO   A 1 62  ? -8.36   31.314  36.691  1   28.68 ? 47  PRO   A N   1 
ATOM   318  C  CA  . PRO   A 1 62  ? -8.25   32.022  37.97   1   28.83 ? 47  PRO   A CA  1 
ATOM   319  C  C   . PRO   A 1 62  ? -9.477  31.852  38.86   1   30.15 ? 47  PRO   A C   1 
ATOM   320  O  O   . PRO   A 1 62  ? -9.343  31.438  40.014  1   31.64 ? 47  PRO   A O   1 
ATOM   321  C  CB  . PRO   A 1 62  ? -8.031  33.481  37.554  1   29.89 ? 47  PRO   A CB  1 
ATOM   322  C  CG  . PRO   A 1 62  ? -7.468  33.413  36.163  1   30.6  ? 47  PRO   A CG  1 
ATOM   323  C  CD  . PRO   A 1 62  ? -8.129  32.223  35.547  1   28.61 ? 47  PRO   A CD  1 
ATOM   324  N  N   . ASP   A 1 63  ? -10.665 32.043  38.3    1   30.38 ? 48  ASP   A N   1 
ATOM   325  C  CA  . ASP   A 1 63  ? -11.94  31.93   38.998  1   30.71 ? 48  ASP   A CA  1 
ATOM   326  C  C   . ASP   A 1 63  ? -12.288 30.503  39.385  1   30.18 ? 48  ASP   A C   1 
ATOM   327  O  O   . ASP   A 1 63  ? -12.638 30.263  40.53   1   30.46 ? 48  ASP   A O   1 
ATOM   328  C  CB  . ASP   A 1 63  ? -13.048 32.535  38.118  1   33    ? 48  ASP   A CB  1 
ATOM   329  C  CG  . ASP   A 1 63  ? -12.823 34.001  37.877  1   38.89 ? 48  ASP   A CG  1 
ATOM   330  O  OD1 . ASP   A 1 63  ? -12.255 34.673  38.777  1   38.91 ? 48  ASP   A OD1 1 
ATOM   331  O  OD2 . ASP   A 1 63  ? -13.206 34.486  36.796  1   41.47 ? 48  ASP   A OD2 1 
ATOM   332  N  N   . LEU   A 1 64  ? -12.159 29.559  38.457  1   29.05 ? 49  LEU   A N   1 
ATOM   333  C  CA  . LEU   A 1 64  ? -12.484 28.148  38.749  1   29.06 ? 49  LEU   A CA  1 
ATOM   334  C  C   . LEU   A 1 64  ? -11.589 27.514  39.777  1   30.55 ? 49  LEU   A C   1 
ATOM   335  O  O   . LEU   A 1 64  ? -12.066 26.745  40.606  1   31.23 ? 49  LEU   A O   1 
ATOM   336  C  CB  . LEU   A 1 64  ? -12.492 27.322  37.48   1   28.67 ? 49  LEU   A CB  1 
ATOM   337  C  CG  . LEU   A 1 64  ? -13.598 27.679  36.513  1   30.1  ? 49  LEU   A CG  1 
ATOM   338  C  CD1 . LEU   A 1 64  ? -13.379 26.995  35.164  1   30.03 ? 49  LEU   A CD1 1 
ATOM   339  C  CD2 . LEU   A 1 64  ? -14.988 27.312  37.125  1   32.05 ? 49  LEU   A CD2 1 
ATOM   340  N  N   . ILE   A 1 65  ? -10.289 27.835  39.744  1   30.47 ? 50  ILE   A N   1 
ATOM   341  C  CA  . ILE   A 1 65  ? -9.348  27.277  40.702  1   30.63 ? 50  ILE   A CA  1 
ATOM   342  C  C   . ILE   A 1 65  ? -9.659  27.819  42.088  1   30.6  ? 50  ILE   A C   1 
ATOM   343  O  O   . ILE   A 1 65  ? -9.691  27.054  43.06   1   30.19 ? 50  ILE   A O   1 
ATOM   344  C  CB  . ILE   A 1 65  ? -7.882  27.634  40.282  1   30.98 ? 50  ILE   A CB  1 
ATOM   345  C  CG1 . ILE   A 1 65  ? -7.451  26.914  38.992  1   31.73 ? 50  ILE   A CG1 1 
ATOM   346  C  CG2 . ILE   A 1 65  ? -6.902  27.373  41.417  1   30.38 ? 50  ILE   A CG2 1 
ATOM   347  C  CD1 . ILE   A 1 65  ? -6.036  27.46   38.457  1   32.93 ? 50  ILE   A CD1 1 
ATOM   348  N  N   . GLU   A 1 66  ? -9.859  29.138  42.185  1   30.21 ? 51  GLU   A N   1 
ATOM   349  C  CA  . GLU   A 1 66  ? -10.061 29.799  43.469  1   31.26 ? 51  GLU   A CA  1 
ATOM   350  C  C   . GLU   A 1 66  ? -11.343 29.331  44.162  1   32.12 ? 51  GLU   A C   1 
ATOM   351  O  O   . GLU   A 1 66  ? -11.369 29.16   45.377  1   33.13 ? 51  GLU   A O   1 
ATOM   352  C  CB  . GLU   A 1 66  ? -10.028 31.322  43.27   1   33.72 ? 51  GLU   A CB  1 
ATOM   353  C  CG  . GLU   A 1 66  ? -9.942  32.093  44.562  1   39.73 ? 51  GLU   A CG  1 
ATOM   354  C  CD  . GLU   A 1 66  ? -9.915  33.608  44.456  1   44.85 ? 51  GLU   A CD  1 
ATOM   355  O  OE1 . GLU   A 1 66  ? -9.645  34.148  43.358  1   43.58 ? 51  GLU   A OE1 1 
ATOM   356  O  OE2 . GLU   A 1 66  ? -10.16  34.257  45.498  1   48.37 ? 51  GLU   A OE2 1 
ATOM   357  N  N   . SER   A 1 67  ? -12.39  29.101  43.387  1   32.1  ? 52  SER   A N   1 
ATOM   358  C  CA  . SER   A 1 67  ? -13.672 28.631  43.909  1   32.7  ? 52  SER   A CA  1 
ATOM   359  C  C   . SER   A 1 67  ? -13.738 27.102  44.133  1   34.05 ? 52  SER   A C   1 
ATOM   360  O  O   . SER   A 1 67  ? -14.769 26.619  44.567  1   34.77 ? 52  SER   A O   1 
ATOM   361  C  CB  . SER   A 1 67  ? -14.794 29.046  42.971  1   33.59 ? 52  SER   A CB  1 
ATOM   362  O  OG  . SER   A 1 67  ? -14.738 28.308  41.76   1   36.97 ? 52  SER   A OG  1 
ATOM   363  N  N   . GLY   A 1 68  ? -12.681 26.361  43.792  1   33.79 ? 53  GLY   A N   1 
ATOM   364  C  CA  . GLY   A 1 68  ? -12.66  24.909  43.955  1   33.85 ? 53  GLY   A CA  1 
ATOM   365  C  C   . GLY   A 1 68  ? -13.54  24.175  42.955  1   34.34 ? 53  GLY   A C   1 
ATOM   366  O  O   . GLY   A 1 68  ? -13.906 23.015  43.176  1   35.45 ? 53  GLY   A O   1 
ATOM   367  N  N   . GLN   A 1 69  ? -13.87  24.822  41.832  1   33.69 ? 54  GLN   A N   1 
ATOM   368  C  CA  . GLN   A 1 69  ? -14.755 24.248  40.803  1   33.67 ? 54  GLN   A CA  1 
ATOM   369  C  C   . GLN   A 1 69  ? -14.007 23.705  39.589  1   32.79 ? 54  GLN   A C   1 
ATOM   370  O  O   . GLN   A 1 69  ? -14.623 23.071  38.731  1   32.67 ? 54  GLN   A O   1 
ATOM   371  C  CB  . GLN   A 1 69  ? -15.756 25.312  40.302  1   35.35 ? 54  GLN   A CB  1 
ATOM   372  C  CG  . GLN   A 1 69  ? -16.728 25.854  41.35   1   39.52 ? 54  GLN   A CG  1 
ATOM   373  C  CD  . GLN   A 1 69  ? -18.054 25.132  41.381  1   46.35 ? 54  GLN   A CD  1 
ATOM   374  O  OE1 . GLN   A 1 69  ? -18.359 24.276  40.543  1   49.52 ? 54  GLN   A OE1 1 
ATOM   375  N  NE2 . GLN   A 1 69  ? -18.859 25.449  42.369  1   46.92 ? 54  GLN   A NE2 1 
ATOM   376  N  N   . LEU   A 1 70  ? -12.701 23.975  39.487  1   31.63 ? 55  LEU   A N   1 
ATOM   377  C  CA  . LEU   A 1 70  ? -11.926 23.564  38.326  1   30.22 ? 55  LEU   A CA  1 
ATOM   378  C  C   . LEU   A 1 70  ? -11.985 22.055  38.047  1   29.78 ? 55  LEU   A C   1 
ATOM   379  O  O   . LEU   A 1 70  ? -12.256 21.667  36.915  1   29.65 ? 55  LEU   A O   1 
ATOM   380  C  CB  . LEU   A 1 70  ? -10.466 24.069  38.457  1   29.63 ? 55  LEU   A CB  1 
ATOM   381  C  CG  . LEU   A 1 70  ? -9.486  23.828  37.273  1   31.1  ? 55  LEU   A CG  1 
ATOM   382  C  CD1 . LEU   A 1 70  ? -8.881  22.458  37.303  1   31.56 ? 55  LEU   A CD1 1 
ATOM   383  C  CD2 . LEU   A 1 70  ? -10.11  24.099  35.926  1   32.09 ? 55  LEU   A CD2 1 
ATOM   384  N  N   . ARG   A 1 71  ? -11.64  21.222  39.031  1   29.71 ? 56  ARG   A N   1 
ATOM   385  C  CA  . ARG   A 1 71  ? -11.541 19.782  38.803  1   31.37 ? 56  ARG   A CA  1 
ATOM   386  C  C   . ARG   A 1 71  ? -12.891 19.161  38.435  1   33.84 ? 56  ARG   A C   1 
ATOM   387  O  O   . ARG   A 1 71  ? -12.954 18.362  37.496  1   34.76 ? 56  ARG   A O   1 
ATOM   388  C  CB  . ARG   A 1 71  ? -10.863 19.105  40.002  1   31.52 ? 56  ARG   A CB  1 
ATOM   389  C  CG  . ARG   A 1 71  ? -9.35   19.427  40.012  1   33    ? 56  ARG   A CG  1 
ATOM   390  C  CD  . ARG   A 1 71  ? -8.705  19.165  41.345  1   34.68 ? 56  ARG   A CD  1 
ATOM   391  N  NE  . ARG   A 1 71  ? -7.239  19.261  41.312  1   34.44 ? 56  ARG   A NE  1 
ATOM   392  C  CZ  . ARG   A 1 71  ? -6.477  19.314  42.396  1   34.8  ? 56  ARG   A CZ  1 
ATOM   393  N  NH1 . ARG   A 1 71  ? -7.03   19.36   43.605  1   34.8  ? 56  ARG   A NH1 1 
ATOM   394  N  NH2 . ARG   A 1 71  ? -5.153  19.335  42.283  1   34.35 ? 56  ARG   A NH2 1 
ATOM   395  N  N   . GLU   A 1 72  ? -13.979 19.62   39.078  1   34.15 ? 57  GLU   A N   1 
ATOM   396  C  CA  . GLU   A 1 72  ? -15.339 19.165  38.766  1   34.71 ? 57  GLU   A CA  1 
ATOM   397  C  C   . GLU   A 1 72  ? -15.694 19.505  37.306  1   33.89 ? 57  GLU   A C   1 
ATOM   398  O  O   . GLU   A 1 72  ? -16.082 18.603  36.568  1   33.9  ? 57  GLU   A O   1 
ATOM   399  C  CB  . GLU   A 1 72  ? -16.338 19.8    39.739  1   39.05 ? 57  GLU   A CB  1 
ATOM   400  C  CG  . GLU   A 1 72  ? -17.747 19.234  39.647  1   50.27 ? 57  GLU   A CG  1 
ATOM   401  C  CD  . GLU   A 1 72  ? -18.752 20.1    40.385  1   64.15 ? 57  GLU   A CD  1 
ATOM   402  O  OE1 . GLU   A 1 72  ? -19.084 21.189  39.859  1   67.64 ? 57  GLU   A OE1 1 
ATOM   403  O  OE2 . GLU   A 1 72  ? -19.174 19.714  41.502  1   68.33 ? 57  GLU   A OE2 1 
ATOM   404  N  N   . ARG   A 1 73  ? -15.486 20.769  36.862  1   33.32 ? 58  ARG   A N   1 
ATOM   405  C  CA  . ARG   A 1 73  ? -15.745 21.19   35.479  1   33.68 ? 58  ARG   A CA  1 
ATOM   406  C  C   . ARG   A 1 73  ? -14.98  20.319  34.486  1   34.17 ? 58  ARG   A C   1 
ATOM   407  O  O   . ARG   A 1 73  ? -15.516 19.987  33.421  1   34.15 ? 58  ARG   A O   1 
ATOM   408  C  CB  . ARG   A 1 73  ? -15.316 22.644  35.24   1   35.93 ? 58  ARG   A CB  1 
ATOM   409  C  CG  . ARG   A 1 73  ? -16.068 23.692  36.043  1   41.67 ? 58  ARG   A CG  1 
ATOM   410  C  CD  . ARG   A 1 73  ? -17.525 23.776  35.639  1   48    ? 58  ARG   A CD  1 
ATOM   411  N  NE  . ARG   A 1 73  ? -18.373 23.155  36.653  1   53.33 ? 58  ARG   A NE  1 
ATOM   412  C  CZ  . ARG   A 1 73  ? -19.527 22.545  36.4    1   56.66 ? 58  ARG   A CZ  1 
ATOM   413  N  NH1 . ARG   A 1 73  ? -19.98  22.451  35.151  1   55.01 ? 58  ARG   A NH1 1 
ATOM   414  N  NH2 . ARG   A 1 73  ? -20.237 22.022  37.392  1   57.13 ? 58  ARG   A NH2 1 
ATOM   415  N  N   . VAL   A 1 74  ? -13.716 19.967  34.819  1   33.51 ? 59  VAL   A N   1 
ATOM   416  C  CA  . VAL   A 1 74  ? -12.892 19.139  33.946  1   33.16 ? 59  VAL   A CA  1 
ATOM   417  C  C   . VAL   A 1 74  ? -13.477 17.753  33.887  1   33.53 ? 59  VAL   A C   1 
ATOM   418  O  O   . VAL   A 1 74  ? -13.698 17.242  32.8    1   34.24 ? 59  VAL   A O   1 
ATOM   419  C  CB  . VAL   A 1 74  ? -11.391 19.146  34.355  1   32.8  ? 59  VAL   A CB  1 
ATOM   420  C  CG1 . VAL   A 1 74  ? -10.603 18.035  33.644  1   33.14 ? 59  VAL   A CG1 1 
ATOM   421  C  CG2 . VAL   A 1 74  ? -10.765 20.513  34.078  1   32.27 ? 59  VAL   A CG2 1 
ATOM   422  N  N   . GLU   A 1 75  ? -13.768 17.162  35.04   1   33.39 ? 60  GLU   A N   1 
ATOM   423  C  CA  . GLU   A 1 75  ? -14.356 15.814  35.121  1   34.58 ? 60  GLU   A CA  1 
ATOM   424  C  C   . GLU   A 1 75  ? -15.767 15.718  34.451  1   36.22 ? 60  GLU   A C   1 
ATOM   425  O  O   . GLU   A 1 75  ? -16.154 14.66   33.967  1   36.41 ? 60  GLU   A O   1 
ATOM   426  C  CB  . GLU   A 1 75  ? -14.364 15.331  36.576  1   34.64 ? 60  GLU   A CB  1 
ATOM   427  C  CG  . GLU   A 1 75  ? -12.958 15.159  37.13   1   35.5  ? 60  GLU   A CG  1 
ATOM   428  C  CD  . GLU   A 1 75  ? -12.827 15.313  38.64   1   42.26 ? 60  GLU   A CD  1 
ATOM   429  O  OE1 . GLU   A 1 75  ? -13.87  15.515  39.306  1   45.97 ? 60  GLU   A OE1 1 
ATOM   430  O  OE2 . GLU   A 1 75  ? -11.688 15.242  39.16   1   39.02 ? 60  GLU   A OE2 1 
ATOM   431  N  N   . LYS   A 1 76  ? -16.459 16.847  34.314  1   36.05 ? 61  LYS   A N   1 
ATOM   432  C  CA  . LYS   A 1 76  ? -17.767 16.886  33.661  1   37.42 ? 61  LYS   A CA  1 
ATOM   433  C  C   . LYS   A 1 76  ? -17.677 16.958  32.118  1   37.42 ? 61  LYS   A C   1 
ATOM   434  O  O   . LYS   A 1 76  ? -18.694 16.805  31.442  1   37.57 ? 61  LYS   A O   1 
ATOM   435  C  CB  . LYS   A 1 76  ? -18.597 18.062  34.199  1   39.93 ? 61  LYS   A CB  1 
ATOM   436  C  CG  . LYS   A 1 76  ? -19.693 17.621  35.157  1   46.84 ? 61  LYS   A CG  1 
ATOM   437  C  CD  . LYS   A 1 76  ? -19.985 18.689  36.212  1   53.45 ? 61  LYS   A CD  1 
ATOM   438  C  CE  . LYS   A 1 76  ? -20.779 18.125  37.371  1   57.2  ? 61  LYS   A CE  1 
ATOM   439  N  NZ  . LYS   A 1 76  ? -20.083 16.976  38.007  1   59.18 ? 61  LYS   A NZ  1 
ATOM   440  N  N   . LEU   A 1 77  ? -16.469 17.189  31.558  1   36.16 ? 62  LEU   A N   1 
ATOM   441  C  CA  . LEU   A 1 77  ? -16.322 17.289  30.102  1   35.2  ? 62  LEU   A CA  1 
ATOM   442  C  C   . LEU   A 1 77  ? -16.63  15.988  29.402  1   35.36 ? 62  LEU   A C   1 
ATOM   443  O  O   . LEU   A 1 77  ? -16.359 14.919  29.943  1   33.83 ? 62  LEU   A O   1 
ATOM   444  C  CB  . LEU   A 1 77  ? -14.866 17.659  29.75   1   34.76 ? 62  LEU   A CB  1 
ATOM   445  C  CG  . LEU   A 1 77  ? -14.409 19.056  30.082  1   34.99 ? 62  LEU   A CG  1 
ATOM   446  C  CD1 . LEU   A 1 77  ? -12.901 19.17   29.963  1   35.28 ? 62  LEU   A CD1 1 
ATOM   447  C  CD2 . LEU   A 1 77  ? -15.064 20.055  29.165  1   35.74 ? 62  LEU   A CD2 1 
ATOM   448  N  N   . ASN   A 1 78  ? -17.127 16.081  28.162  1   36.27 ? 63  ASN   A N   1 
ATOM   449  C  CA  . ASN   A 1 78  ? -17.256 14.904  27.304  1   37.8  ? 63  ASN   A CA  1 
ATOM   450  C  C   . ASN   A 1 78  ? -15.983 14.84   26.441  1   38.8  ? 63  ASN   A C   1 
ATOM   451  O  O   . ASN   A 1 78  ? -15.407 15.9    26.119  1   39    ? 63  ASN   A O   1 
ATOM   452  C  CB  . ASN   A 1 78  ? -18.464 15.006  26.38   1   38.88 ? 63  ASN   A CB  1 
ATOM   453  C  CG  . ASN   A 1 78  ? -19.775 14.979  27.125  1   43.18 ? 63  ASN   A CG  1 
ATOM   454  O  OD1 . ASN   A 1 78  ? -19.953 14.264  28.128  1   44.58 ? 63  ASN   A OD1 1 
ATOM   455  N  ND2 . ASN   A 1 78  ? -20.702 15.781  26.661  1   43.65 ? 63  ASN   A ND2 1 
ATOM   456  N  N   . MET   A 1 79  ? -15.549 13.623  26.047  1   38.86 ? 64  MET   A N   1 
ATOM   457  C  CA  . MET   A 1 79  ? -14.36  13.507  25.219  1   39.28 ? 64  MET   A CA  1 
ATOM   458  C  C   . MET   A 1 79  ? -14.6   14.104  23.853  1   40.62 ? 64  MET   A C   1 
ATOM   459  O  O   . MET   A 1 79  ? -15.378 13.544  23.089  1   41.52 ? 64  MET   A O   1 
ATOM   460  C  CB  . MET   A 1 79  ? -13.926 12.063  25.046  1   39.07 ? 64  MET   A CB  1 
ATOM   461  C  CG  . MET   A 1 79  ? -12.492 11.973  24.562  1   40.02 ? 64  MET   A CG  1 
ATOM   462  S  SD  . MET   A 1 79  ? -12.006 10.266  24.298  1   49.06 ? 64  MET   A SD  1 
ATOM   463  C  CE  . MET   A 1 79  ? -11.946 9.658   25.979  1   36.13 ? 64  MET   A CE  1 
ATOM   464  N  N   . LEU   A 1 80  ? -13.958 15.243  23.544  1   40.65 ? 65  LEU   A N   1 
ATOM   465  C  CA  . LEU   A 1 80  ? -14.134 15.873  22.245  1   41.44 ? 65  LEU   A CA  1 
ATOM   466  C  C   . LEU   A 1 80  ? -13.083 15.391  21.262  1   42.98 ? 65  LEU   A C   1 
ATOM   467  O  O   . LEU   A 1 80  ? -11.908 15.267  21.605  1   43.51 ? 65  LEU   A O   1 
ATOM   468  C  CB  . LEU   A 1 80  ? -14.087 17.403  22.339  1   41.27 ? 65  LEU   A CB  1 
ATOM   469  C  CG  . LEU   A 1 80  ? -15.094 18.076  23.271  1   42.63 ? 65  LEU   A CG  1 
ATOM   470  C  CD1 . LEU   A 1 80  ? -14.976 19.593  23.195  1   42.4  ? 65  LEU   A CD1 1 
ATOM   471  C  CD2 . LEU   A 1 80  ? -16.543 17.632  22.964  1   43.33 ? 65  LEU   A CD2 1 
ATOM   472  N  N   . SER   A 1 81  ? -13.501 15.145  20.02   1   42.94 ? 66  SER   A N   1 
ATOM   473  C  CA  . SER   A 1 81  ? -12.594 14.717  18.968  1   43.28 ? 66  SER   A CA  1 
ATOM   474  C  C   . SER   A 1 81  ? -11.709 15.883  18.544  1   43.27 ? 66  SER   A C   1 
ATOM   475  O  O   . SER   A 1 81  ? -12.173 17.023  18.521  1   43.29 ? 66  SER   A O   1 
ATOM   476  C  CB  . SER   A 1 81  ? -13.399 14.246  17.757  1   44.2  ? 66  SER   A CB  1 
ATOM   477  O  OG  . SER   A 1 81  ? -12.557 13.827  16.696  1   45.8  ? 66  SER   A OG  1 
ATOM   478  N  N   . ILE   A 1 82  ? -10.458 15.602  18.151  1   42.97 ? 67  ILE   A N   1 
ATOM   479  C  CA  . ILE   A 1 82  ? -9.567  16.672  17.674  1   43.19 ? 67  ILE   A CA  1 
ATOM   480  C  C   . ILE   A 1 82  ? -9.666  16.905  16.158  1   44.5  ? 67  ILE   A C   1 
ATOM   481  O  O   . ILE   A 1 82  ? -9.01   17.803  15.646  1   44.4  ? 67  ILE   A O   1 
ATOM   482  C  CB  . ILE   A 1 82  ? -8.091  16.397  18.087  1   42.51 ? 67  ILE   A CB  1 
ATOM   483  C  CG1 . ILE   A 1 82  ? -7.571  15.103  17.441  1   42.7  ? 67  ILE   A CG1 1 
ATOM   484  C  CG2 . ILE   A 1 82  ? -7.935  16.381  19.588  1   42.61 ? 67  ILE   A CG2 1 
ATOM   485  C  CD1 . ILE   A 1 82  ? -6.07   15.037  17.327  1   43.98 ? 67  ILE   A CD1 1 
ATOM   486  N  N   . ASP   A 1 83  ? -10.492 16.13   15.44   1   45.87 ? 68  ASP   A N   1 
ATOM   487  C  CA  . ASP   A 1 83  ? -10.601 16.23   13.982  1   47.42 ? 68  ASP   A CA  1 
ATOM   488  C  C   . ASP   A 1 83  ? -11.147 17.551  13.457  1   47.95 ? 68  ASP   A C   1 
ATOM   489  O  O   . ASP   A 1 83  ? -11.023 17.822  12.264  1   48.45 ? 68  ASP   A O   1 
ATOM   490  C  CB  . ASP   A 1 83  ? -11.417 15.053  13.431  1   50.01 ? 68  ASP   A CB  1 
ATOM   491  C  CG  . ASP   A 1 83  ? -10.744 13.739  13.745  1   56.79 ? 68  ASP   A CG  1 
ATOM   492  O  OD1 . ASP   A 1 83  ? -9.492  13.687  13.695  1   57.77 ? 68  ASP   A OD1 1 
ATOM   493  O  OD2 . ASP   A 1 83  ? -11.461 12.768  14.064  1   60.09 ? 68  ASP   A OD2 1 
ATOM   494  N  N   . HIS   A 1 84  ? -11.722 18.385  14.327  1   47.69 ? 69  HIS   A N   1 
ATOM   495  C  CA  . HIS   A 1 84  ? -12.25  19.683  13.895  1   47.86 ? 69  HIS   A CA  1 
ATOM   496  C  C   . HIS   A 1 84  ? -11.214 20.834  14.035  1   47.34 ? 69  HIS   A C   1 
ATOM   497  O  O   . HIS   A 1 84  ? -11.555 21.997  13.821  1   47.47 ? 69  HIS   A O   1 
ATOM   498  C  CB  . HIS   A 1 84  ? -13.584 19.992  14.596  1   49.17 ? 69  HIS   A CB  1 
ATOM   499  C  CG  . HIS   A 1 84  ? -14.515 18.811  14.61   1   53.07 ? 69  HIS   A CG  1 
ATOM   500  N  ND1 . HIS   A 1 84  ? -15.242 18.443  13.486  1   55.47 ? 69  HIS   A ND1 1 
ATOM   501  C  CD2 . HIS   A 1 84  ? -14.724 17.891  15.58   1   54.7  ? 69  HIS   A CD2 1 
ATOM   502  C  CE1 . HIS   A 1 84  ? -15.908 17.352  13.83   1   56.17 ? 69  HIS   A CE1 1 
ATOM   503  N  NE2 . HIS   A 1 84  ? -15.626 16.979  15.078  1   56.12 ? 69  HIS   A NE2 1 
ATOM   504  N  N   . LEU   A 1 85  ? -9.951  20.494  14.376  1   46.33 ? 70  LEU   A N   1 
ATOM   505  C  CA  . LEU   A 1 85  ? -8.808  21.407  14.49   1   45.28 ? 70  LEU   A CA  1 
ATOM   506  C  C   . LEU   A 1 85  ? -8.022  21.068  13.241  1   45.95 ? 70  LEU   A C   1 
ATOM   507  O  O   . LEU   A 1 85  ? -7.229  20.131  13.253  1   46.28 ? 70  LEU   A O   1 
ATOM   508  C  CB  . LEU   A 1 85  ? -7.982  21.054  15.736  1   43.84 ? 70  LEU   A CB  1 
ATOM   509  C  CG  . LEU   A 1 85  ? -8.75   21.087  17.04   1   43.21 ? 70  LEU   A CG  1 
ATOM   510  C  CD1 . LEU   A 1 85  ? -8.045  20.3    18.112  1   42.29 ? 70  LEU   A CD1 1 
ATOM   511  C  CD2 . LEU   A 1 85  ? -9.033  22.496  17.459  1   43.98 ? 70  LEU   A CD2 1 
ATOM   512  N  N   . THR   A 1 86  ? -8.317  21.763  12.148  1   46.43 ? 71  THR   A N   1 
ATOM   513  C  CA  . THR   A 1 86  ? -7.822  21.433  10.81   1   47.66 ? 71  THR   A CA  1 
ATOM   514  C  C   . THR   A 1 86  ? -6.574  22.154  10.285  1   48.13 ? 71  THR   A C   1 
ATOM   515  O  O   . THR   A 1 86  ? -6.188  21.933  9.131   1   49.04 ? 71  THR   A O   1 
ATOM   516  C  CB  . THR   A 1 86  ? -8.957  21.688  9.829   1   49.24 ? 71  THR   A CB  1 
ATOM   517  O  OG1 . THR   A 1 86  ? -9.288  23.082  9.916   1   51.32 ? 71  THR   A OG1 1 
ATOM   518  C  CG2 . THR   A 1 86  ? -10.193 20.853  10.153  1   48.92 ? 71  THR   A CG2 1 
ATOM   519  N  N   . ASP   A 1 87  ? -5.963  23.014  11.089  1   46.83 ? 72  ASP   A N   1 
ATOM   520  C  CA  . ASP   A 1 87  ? -4.762  23.728  10.667  1   45.71 ? 72  ASP   A CA  1 
ATOM   521  C  C   . ASP   A 1 87  ? -3.831  23.933  11.871  1   43.78 ? 72  ASP   A C   1 
ATOM   522  O  O   . ASP   A 1 87  ? -4.257  23.763  13.016  1   43.98 ? 72  ASP   A O   1 
ATOM   523  C  CB  . ASP   A 1 87  ? -5.113  25.052  9.961   1   47.26 ? 72  ASP   A CB  1 
ATOM   524  C  CG  . ASP   A 1 87  ? -5.855  26.056  10.815  1   53.36 ? 72  ASP   A CG  1 
ATOM   525  O  OD1 . ASP   A 1 87  ? -6.026  25.799  12.026  1   54.47 ? 72  ASP   A OD1 1 
ATOM   526  O  OD2 . ASP   A 1 87  ? -6.257  27.111  10.276  1   56.2  ? 72  ASP   A OD2 1 
ATOM   527  N  N   . HIS   A 1 88  ? -2.572  24.3    11.615  1   41.45 ? 73  HIS   A N   1 
ATOM   528  C  CA  . HIS   A 1 88  ? -1.572  24.477  12.649  1   39.4  ? 73  HIS   A CA  1 
ATOM   529  C  C   . HIS   A 1 88  ? -2.009  25.425  13.75   1   37.33 ? 73  HIS   A C   1 
ATOM   530  O  O   . HIS   A 1 88  ? -1.937  25.04   14.906  1   37.26 ? 73  HIS   A O   1 
ATOM   531  C  CB  . HIS   A 1 88  ? -0.215  24.9    12.052  1   39.78 ? 73  HIS   A CB  1 
ATOM   532  C  CG  . HIS   A 1 88  ? 0.932   24.759  13.012  1   41.52 ? 73  HIS   A CG  1 
ATOM   533  N  ND1 . HIS   A 1 88  ? 1.398   23.521  13.396  1   42.53 ? 73  HIS   A ND1 1 
ATOM   534  C  CD2 . HIS   A 1 88  ? 1.672   25.712  13.624  1   42.99 ? 73  HIS   A CD2 1 
ATOM   535  C  CE1 . HIS   A 1 88  ? 2.389   23.756  14.236  1   43.32 ? 73  HIS   A CE1 1 
ATOM   536  N  NE2 . HIS   A 1 88  ? 2.605   25.06   14.388  1   43.69 ? 73  HIS   A NE2 1 
ATOM   537  N  N   . LYS   A 1 89  ? -2.497  26.624  13.406  1   35.64 ? 74  LYS   A N   1 
ATOM   538  C  CA  . LYS   A 1 89  ? -2.913  27.598  14.395  1   35.77 ? 74  LYS   A CA  1 
ATOM   539  C  C   . LYS   A 1 89  ? -4.005  27.117  15.337  1   37.09 ? 74  LYS   A C   1 
ATOM   540  O  O   . LYS   A 1 89  ? -3.883  27.327  16.554  1   37.73 ? 74  LYS   A O   1 
ATOM   541  C  CB  . LYS   A 1 89  ? -3.313  28.912  13.738  1   36.53 ? 74  LYS   A CB  1 
ATOM   542  C  CG  . LYS   A 1 89  ? -2.117  29.573  13.057  1   36.56 ? 74  LYS   A CG  1 
ATOM   543  C  CD  . LYS   A 1 89  ? -2.363  31.034  12.869  1   38.15 ? 74  LYS   A CD  1 
ATOM   544  C  CE  . LYS   A 1 89  ? -1.264  31.683  12.087  1   39.14 ? 74  LYS   A CE  1 
ATOM   545  N  NZ  . LYS   A 1 89  ? -1.569  33.113  11.898  1   39.75 ? 74  LYS   A NZ  1 
ATOM   546  N  N   . SER   A 1 90  ? -5.067  26.483  14.809  1   37.05 ? 75  SER   A N   1 
ATOM   547  C  CA  . SER   A 1 90  ? -6.133  25.982  15.688  1   36.7  ? 75  SER   A CA  1 
ATOM   548  C  C   . SER   A 1 90  ? -5.595  24.847  16.569  1   35.55 ? 75  SER   A C   1 
ATOM   549  O  O   . SER   A 1 90  ? -5.953  24.776  17.748  1   35.53 ? 75  SER   A O   1 
ATOM   550  C  CB  . SER   A 1 90  ? -7.354  25.533  14.885  1   38.43 ? 75  SER   A CB  1 
ATOM   551  O  OG  . SER   A 1 90  ? -7.044  24.4    14.088  1   40.87 ? 75  SER   A OG  1 
ATOM   552  N  N   . GLN   A 1 91  ? -4.686  24.009  16.032  1   34.63 ? 76  GLN   A N   1 
ATOM   553  C  CA  . GLN   A 1 91  ? -4.068  22.932  16.808  1   34.81 ? 76  GLN   A CA  1 
ATOM   554  C  C   . GLN   A 1 91  ? -3.14   23.486  17.923  1   34.32 ? 76  GLN   A C   1 
ATOM   555  O  O   . GLN   A 1 91  ? -3.115  22.975  19.042  1   33.95 ? 76  GLN   A O   1 
ATOM   556  C  CB  . GLN   A 1 91  ? -3.306  21.989  15.878  1   36.16 ? 76  GLN   A CB  1 
ATOM   557  C  CG  . GLN   A 1 91  ? -4.222  21.106  15.036  1   38.05 ? 76  GLN   A CG  1 
ATOM   558  C  CD  . GLN   A 1 91  ? -3.512  20.562  13.826  1   43.5  ? 76  GLN   A CD  1 
ATOM   559  O  OE1 . GLN   A 1 91  ? -2.295  20.318  13.828  1   44.99 ? 76  GLN   A OE1 1 
ATOM   560  N  NE2 . GLN   A 1 91  ? -4.252  20.368  12.758  1   45.38 ? 76  GLN   A NE2 1 
ATOM   561  N  N   . ARG   A 1 92  ? -2.418  24.558  17.617  1   33.77 ? 77  ARG   A N   1 
ATOM   562  C  CA  . ARG   A 1 92  ? -1.528  25.214  18.577  1   33.37 ? 77  ARG   A CA  1 
ATOM   563  C  C   . ARG   A 1 92  ? -2.365  25.856  19.678  1   32.84 ? 77  ARG   A C   1 
ATOM   564  O  O   . ARG   A 1 92  ? -2.036  25.702  20.865  1   32.8  ? 77  ARG   A O   1 
ATOM   565  C  CB  . ARG   A 1 92  ? -0.635  26.259  17.873  1   33.32 ? 77  ARG   A CB  1 
ATOM   566  C  CG  . ARG   A 1 92  ? 0.533   25.62   17.1    1   33.59 ? 77  ARG   A CG  1 
ATOM   567  C  CD  . ARG   A 1 92  ? 1.612   24.974  17.984  1   33.81 ? 77  ARG   A CD  1 
ATOM   568  N  NE  . ARG   A 1 92  ? 2.364   25.959  18.781  1   31.08 ? 77  ARG   A NE  1 
ATOM   569  C  CZ  . ARG   A 1 92  ? 3.345   26.718  18.304  1   31.02 ? 77  ARG   A CZ  1 
ATOM   570  N  NH1 . ARG   A 1 92  ? 3.677   26.655  17.016  1   30.18 ? 77  ARG   A NH1 1 
ATOM   571  N  NH2 . ARG   A 1 92  ? 3.955   27.598  19.092  1   28.19 ? 77  ARG   A NH2 1 
ATOM   572  N  N   . LEU   A 1 93  ? -3.481  26.51   19.306  1   32.54 ? 78  LEU   A N   1 
ATOM   573  C  CA  . LEU   A 1 93  ? -4.389  27.12   20.304  1   32.52 ? 78  LEU   A CA  1 
ATOM   574  C  C   . LEU   A 1 93  ? -4.954  26.053  21.219  1   32.36 ? 78  LEU   A C   1 
ATOM   575  O  O   . LEU   A 1 93  ? -4.922  26.211  22.451  1   32.01 ? 78  LEU   A O   1 
ATOM   576  C  CB  . LEU   A 1 93  ? -5.53   27.923  19.657  1   32.3  ? 78  LEU   A CB  1 
ATOM   577  C  CG  . LEU   A 1 93  ? -6.566  28.496  20.628  1   32.91 ? 78  LEU   A CG  1 
ATOM   578  C  CD1 . LEU   A 1 93  ? -5.926  29.468  21.6    1   32.69 ? 78  LEU   A CD1 1 
ATOM   579  C  CD2 . LEU   A 1 93  ? -7.689  29.191  19.891  1   33.79 ? 78  LEU   A CD2 1 
ATOM   580  N  N   . ALA   A 1 94  ? -5.373  24.935  20.629  1   32.75 ? 79  ALA   A N   1 
ATOM   581  C  CA  . ALA   A 1 94  ? -5.923  23.814  21.381  1   32.97 ? 79  ALA   A CA  1 
ATOM   582  C  C   . ALA   A 1 94  ? -4.888  23.235  22.341  1   31.66 ? 79  ALA   A C   1 
ATOM   583  O  O   . ALA   A 1 94  ? -5.213  23.02   23.515  1   32.19 ? 79  ALA   A O   1 
ATOM   584  C  CB  . ALA   A 1 94  ? -6.43   22.75   20.431  1   33.41 ? 79  ALA   A CB  1 
ATOM   585  N  N   . ARG   A 1 95  ? -3.618  23.095  21.894  1   30.05 ? 80  ARG   A N   1 
ATOM   586  C  CA  . ARG   A 1 95  ? -2.493  22.621  22.737  1   29.56 ? 80  ARG   A CA  1 
ATOM   587  C  C   . ARG   A 1 95  ? -2.351  23.549  23.94   1   28.25 ? 80  ARG   A C   1 
ATOM   588  O  O   . ARG   A 1 95  ? -2.309  23.076  25.058  1   27.69 ? 80  ARG   A O   1 
ATOM   589  C  CB  . ARG   A 1 95  ? -1.179  22.631  21.948  1   30.08 ? 80  ARG   A CB  1 
ATOM   590  C  CG  . ARG   A 1 95  ? -0.639  21.257  21.66   1   31.46 ? 80  ARG   A CG  1 
ATOM   591  C  CD  . ARG   A 1 95  ? 0.854   21.311  21.365  1   31.31 ? 80  ARG   A CD  1 
ATOM   592  N  NE  . ARG   A 1 95  ? 1.68    21.546  22.557  1   33.47 ? 80  ARG   A NE  1 
ATOM   593  C  CZ  . ARG   A 1 95  ? 2.096   20.588  23.382  1   30.23 ? 80  ARG   A CZ  1 
ATOM   594  N  NH1 . ARG   A 1 95  ? 1.737   19.327  23.181  1   25.83 ? 80  ARG   A NH1 1 
ATOM   595  N  NH2 . ARG   A 1 95  ? 2.864   20.888  24.426  1   27.45 ? 80  ARG   A NH2 1 
ATOM   596  N  N   . LEU   A 1 96  ? -2.435  24.865  23.71   1   27.72 ? 81  LEU   A N   1 
ATOM   597  C  CA  . LEU   A 1 96  ? -2.327  25.863  24.775  1   28.06 ? 81  LEU   A CA  1 
ATOM   598  C  C   . LEU   A 1 96  ? -3.502  25.757  25.779  1   28.19 ? 81  LEU   A C   1 
ATOM   599  O  O   . LEU   A 1 96  ? -3.286  25.793  27.001  1   28.89 ? 81  LEU   A O   1 
ATOM   600  C  CB  . LEU   A 1 96  ? -2.256  27.248  24.116  1   28.52 ? 81  LEU   A CB  1 
ATOM   601  C  CG  . LEU   A 1 96  ? -2.246  28.438  25.023  1   31.08 ? 81  LEU   A CG  1 
ATOM   602  C  CD1 . LEU   A 1 96  ? -1.099  28.39   26.009  1   31.44 ? 81  LEU   A CD1 1 
ATOM   603  C  CD2 . LEU   A 1 96  ? -2.136  29.698  24.215  1   33.13 ? 81  LEU   A CD2 1 
ATOM   604  N  N   . VAL   A 1 97  ? -4.74   25.648  25.265  1   28.17 ? 82  VAL   A N   1 
ATOM   605  C  CA  . VAL   A 1 97  ? -5.945  25.493  26.083  1   27.78 ? 82  VAL   A CA  1 
ATOM   606  C  C   . VAL   A 1 97  ? -5.836  24.242  26.97   1   27.28 ? 82  VAL   A C   1 
ATOM   607  O  O   . VAL   A 1 97  ? -5.928  24.341  28.201  1   27.87 ? 82  VAL   A O   1 
ATOM   608  C  CB  . VAL   A 1 97  ? -7.214  25.465  25.176  1   28.41 ? 82  VAL   A CB  1 
ATOM   609  C  CG1 . VAL   A 1 97  ? -8.438  24.956  25.934  1   28.83 ? 82  VAL   A CG1 1 
ATOM   610  C  CG2 . VAL   A 1 97  ? -7.469  26.84   24.587  1   28.6  ? 82  VAL   A CG2 1 
ATOM   611  N  N   . LEU   A 1 98  ? -5.574  23.087  26.362  1   26.11 ? 83  LEU   A N   1 
ATOM   612  C  CA  . LEU   A 1 98  ? -5.479  21.833  27.13   1   26.28 ? 83  LEU   A CA  1 
ATOM   613  C  C   . LEU   A 1 98  ? -4.272  21.781  28.091  1   25.76 ? 83  LEU   A C   1 
ATOM   614  O  O   . LEU   A 1 98  ? -4.342  21.161  29.173  1   25.79 ? 83  LEU   A O   1 
ATOM   615  C  CB  . LEU   A 1 98  ? -5.446  20.652  26.152  1   27.42 ? 83  LEU   A CB  1 
ATOM   616  C  CG  . LEU   A 1 98  ? -6.733  20.49   25.323  1   29.7  ? 83  LEU   A CG  1 
ATOM   617  C  CD1 . LEU   A 1 98  ? -6.58   19.39   24.318  1   31.31 ? 83  LEU   A CD1 1 
ATOM   618  C  CD2 . LEU   A 1 98  ? -7.92   20.188  26.207  1   28.53 ? 83  LEU   A CD2 1 
ATOM   619  N  N   . GLY   A 1 99  ? -3.165  22.433  27.709  1   25.42 ? 84  GLY   A N   1 
ATOM   620  C  CA  . GLY   A 1 99  ? -1.984  22.463  28.544  1   24.75 ? 84  GLY   A CA  1 
ATOM   621  C  C   . GLY   A 1 99  ? -2.258  23.312  29.757  1   24.84 ? 84  GLY   A C   1 
ATOM   622  O  O   . GLY   A 1 99  ? -1.976  22.868  30.865  1   24.76 ? 84  GLY   A O   1 
ATOM   623  N  N   . CYS   A 1 100 ? -2.897  24.496  29.577  1   25.97 ? 85  CYS   A N   1 
ATOM   624  C  CA  . CYS   A 1 100 ? -3.222  25.324  30.749  1   27.43 ? 85  CYS   A CA  1 
ATOM   625  C  C   . CYS   A 1 100 ? -4.204  24.619  31.661  1   27.85 ? 85  CYS   A C   1 
ATOM   626  O  O   . CYS   A 1 100 ? -4.017  24.631  32.873  1   29.04 ? 85  CYS   A O   1 
ATOM   627  C  CB  . CYS   A 1 100 ? -3.705  26.708  30.348  1   29.25 ? 85  CYS   A CB  1 
ATOM   628  S  SG  . CYS   A 1 100 ? -2.445  27.704  29.501  1   31.83 ? 85  CYS   A SG  1 
ATOM   629  N  N   . ILE   A 1 101 ? -5.194  23.923  31.078  1   27.41 ? 86  ILE   A N   1 
ATOM   630  C  CA  . ILE   A 1 101 ? -6.175  23.173  31.879  1   27.33 ? 86  ILE   A CA  1 
ATOM   631  C  C   . ILE   A 1 101 ? -5.472  22.053  32.648  1   26.67 ? 86  ILE   A C   1 
ATOM   632  O  O   . ILE   A 1 101 ? -5.735  21.88   33.836  1   27.05 ? 86  ILE   A O   1 
ATOM   633  C  CB  . ILE   A 1 101 ? -7.35   22.616  30.994  1   27.14 ? 86  ILE   A CB  1 
ATOM   634  C  CG1 . ILE   A 1 101 ? -8.238  23.762  30.443  1   28.01 ? 86  ILE   A CG1 1 
ATOM   635  C  CG2 . ILE   A 1 101 ? -8.204  21.633  31.802  1   26.41 ? 86  ILE   A CG2 1 
ATOM   636  C  CD1 . ILE   A 1 101 ? -9.243  23.267  29.389  1   29.37 ? 86  ILE   A CD1 1 
ATOM   637  N  N   . THR   A 1 102 ? -4.534  21.321  31.992  1   26.9  ? 87  THR   A N   1 
ATOM   638  C  CA  . THR   A 1 102 ? -3.806  20.24   32.65   1   26.78 ? 87  THR   A CA  1 
ATOM   639  C  C   . THR   A 1 102 ? -2.989  20.719  33.849  1   27.52 ? 87  THR   A C   1 
ATOM   640  O  O   . THR   A 1 102 ? -3.056  20.088  34.914  1   27.6  ? 87  THR   A O   1 
ATOM   641  C  CB  . THR   A 1 102 ? -2.983  19.466  31.643  1   27.65 ? 87  THR   A CB  1 
ATOM   642  O  OG1 . THR   A 1 102 ? -3.914  18.998  30.649  1   26.88 ? 87  THR   A OG1 1 
ATOM   643  C  CG2 . THR   A 1 102 ? -2.218  18.306  32.287  1   27.19 ? 87  THR   A CG2 1 
ATOM   644  N  N   . MET   A 1 103 ? -2.278  21.87   33.72   1   26.99 ? 88  MET   A N   1 
ATOM   645  C  CA  . MET   A 1 103 ? -1.515  22.428  34.85   1   26.25 ? 88  MET   A CA  1 
ATOM   646  C  C   . MET   A 1 103 ? -2.452  22.783  35.985  1   26.81 ? 88  MET   A C   1 
ATOM   647  O  O   . MET   A 1 103 ? -2.138  22.481  37.124  1   28.09 ? 88  MET   A O   1 
ATOM   648  C  CB  . MET   A 1 103 ? -0.734  23.699  34.46   1   25.99 ? 88  MET   A CB  1 
ATOM   649  C  CG  . MET   A 1 103 ? 0.373   23.517  33.401  1   27.37 ? 88  MET   A CG  1 
ATOM   650  S  SD  . MET   A 1 103 ? 1.359   22.021  33.592  1   33.94 ? 88  MET   A SD  1 
ATOM   651  C  CE  . MET   A 1 103 ? 0.773   21.166  31.998  1   29.9  ? 88  MET   A CE  1 
ATOM   652  N  N   . ALA   A 1 104 ? -3.586  23.427  35.678  1   27.44 ? 89  ALA   A N   1 
ATOM   653  C  CA  . ALA   A 1 104 ? -4.571  23.814  36.701  1   28.41 ? 89  ALA   A CA  1 
ATOM   654  C  C   . ALA   A 1 104 ? -5.144  22.568  37.371  1   28.4  ? 89  ALA   A C   1 
ATOM   655  O  O   . ALA   A 1 104 ? -5.236  22.514  38.581  1   28.14 ? 89  ALA   A O   1 
ATOM   656  C  CB  . ALA   A 1 104 ? -5.692  24.621  36.066  1   28.52 ? 89  ALA   A CB  1 
ATOM   657  N  N   . TYR   A 1 105 ? -5.434  21.525  36.59   1   28.76 ? 90  TYR   A N   1 
ATOM   658  C  CA  . TYR   A 1 105 ? -5.98   20.283  37.139  1   30.11 ? 90  TYR   A CA  1 
ATOM   659  C  C   . TYR   A 1 105 ? -4.983  19.581  38.069  1   29.87 ? 90  TYR   A C   1 
ATOM   660  O  O   . TYR   A 1 105 ? -5.347  19.182  39.187  1   29.28 ? 90  TYR   A O   1 
ATOM   661  C  CB  . TYR   A 1 105 ? -6.433  19.345  36.001  1   30.45 ? 90  TYR   A CB  1 
ATOM   662  C  CG  . TYR   A 1 105 ? -7.213  18.15   36.514  1   32.02 ? 90  TYR   A CG  1 
ATOM   663  C  CD1 . TYR   A 1 105 ? -8.586  18.235  36.758  1   33.33 ? 90  TYR   A CD1 1 
ATOM   664  C  CD2 . TYR   A 1 105 ? -6.575  16.942  36.788  1   33.17 ? 90  TYR   A CD2 1 
ATOM   665  C  CE1 . TYR   A 1 105 ? -9.299  17.147  37.256  1   34.71 ? 90  TYR   A CE1 1 
ATOM   666  C  CE2 . TYR   A 1 105 ? -7.275  15.855  37.297  1   34.58 ? 90  TYR   A CE2 1 
ATOM   667  C  CZ  . TYR   A 1 105 ? -8.636  15.957  37.524  1   35.8  ? 90  TYR   A CZ  1 
ATOM   668  O  OH  . TYR   A 1 105 ? -9.303  14.874  38.04   1   38.45 ? 90  TYR   A OH  1 
ATOM   669  N  N   . VAL   A 1 106 ? -3.733  19.411  37.607  1   29.39 ? 91  VAL   A N   1 
ATOM   670  C  CA  . VAL   A 1 106 ? -2.72   18.72   38.388  1   29.53 ? 91  VAL   A CA  1 
ATOM   671  C  C   . VAL   A 1 106 ? -2.394  19.477  39.657  1   30.9  ? 91  VAL   A C   1 
ATOM   672  O  O   . VAL   A 1 106 ? -2.421  18.886  40.736  1   32.37 ? 91  VAL   A O   1 
ATOM   673  C  CB  . VAL   A 1 106 ? -1.447  18.431  37.543  1   30.55 ? 91  VAL   A CB  1 
ATOM   674  C  CG1 . VAL   A 1 106 ? -0.3    17.917  38.4    1   30.96 ? 91  VAL   A CG1 1 
ATOM   675  C  CG2 . VAL   A 1 106 ? -1.739  17.468  36.404  1   31.4  ? 91  VAL   A CG2 1 
ATOM   676  N  N   . TRP   A 1 107 ? -2.157  20.801  39.549  1   29.64 ? 92  TRP   A N   1 
ATOM   677  C  CA  . TRP   A 1 107 ? -1.709  21.571  40.698  1   28.93 ? 92  TRP   A CA  1 
ATOM   678  C  C   . TRP   A 1 107 ? -2.814  22.177  41.551  1   28.55 ? 92  TRP   A C   1 
ATOM   679  O  O   . TRP   A 1 107 ? -2.521  22.614  42.66   1   28.7  ? 92  TRP   A O   1 
ATOM   680  C  CB  . TRP   A 1 107 ? -0.681  22.675  40.256  1   28.49 ? 92  TRP   A CB  1 
ATOM   681  C  CG  . TRP   A 1 107 ? 0.509   22.17   39.474  1   29.1  ? 92  TRP   A CG  1 
ATOM   682  C  CD1 . TRP   A 1 107 ? 0.854   22.51   38.197  1   29.62 ? 92  TRP   A CD1 1 
ATOM   683  C  CD2 . TRP   A 1 107 ? 1.403   21.113  39.866  1   29.13 ? 92  TRP   A CD2 1 
ATOM   684  N  NE1 . TRP   A 1 107 ? 1.925   21.749  37.781  1   30.31 ? 92  TRP   A NE1 1 
ATOM   685  C  CE2 . TRP   A 1 107 ? 2.279   20.883  38.789  1   29.97 ? 92  TRP   A CE2 1 
ATOM   686  C  CE3 . TRP   A 1 107 ? 1.573   20.372  41.045  1   30.61 ? 92  TRP   A CE3 1 
ATOM   687  C  CZ2 . TRP   A 1 107 ? 3.332   19.973  38.867  1   30.9  ? 92  TRP   A CZ2 1 
ATOM   688  C  CZ3 . TRP   A 1 107 ? 2.589   19.429  41.099  1   31.64 ? 92  TRP   A CZ3 1 
ATOM   689  C  CH2 . TRP   A 1 107 ? 3.477   19.266  40.032  1   31.64 ? 92  TRP   A CH2 1 
ATOM   690  N  N   . GLY   A 1 108 ? -4.042  22.261  41.04   1   28.03 ? 93  GLY   A N   1 
ATOM   691  C  CA  . GLY   A 1 108 ? -5.163  22.798  41.809  1   28.67 ? 93  GLY   A CA  1 
ATOM   692  C  C   . GLY   A 1 108 ? -4.93   24.222  42.266  1   28.16 ? 93  GLY   A C   1 
ATOM   693  O  O   . GLY   A 1 108 ? -4.562  25.052  41.45   1   26.79 ? 93  GLY   A O   1 
ATOM   694  N  N   . LYS   A 1 109 ? -5.029  24.484  43.573  1   28.73 ? 94  LYS   A N   1 
ATOM   695  C  CA  . LYS   A 1 109 ? -4.774  25.816  44.098  1   31.95 ? 94  LYS   A CA  1 
ATOM   696  C  C   . LYS   A 1 109 ? -3.267  26.137  44.268  1   35.83 ? 94  LYS   A C   1 
ATOM   697  O  O   . LYS   A 1 109 ? -2.932  27.243  44.681  1   36.83 ? 94  LYS   A O   1 
ATOM   698  C  CB  . LYS   A 1 109 ? -5.541  26.032  45.426  1   33.2  ? 94  LYS   A CB  1 
ATOM   699  C  CG  . LYS   A 1 109 ? -7.056  26.074  45.253  1   35.48 ? 94  LYS   A CG  1 
ATOM   700  C  CD  . LYS   A 1 109 ? -7.811  26.264  46.556  1   37.74 ? 94  LYS   A CD  1 
ATOM   701  C  CE  . LYS   A 1 109 ? -9.313  26.236  46.325  1   41.29 ? 94  LYS   A CE  1 
ATOM   702  N  NZ  . LYS   A 1 109 ? -10.087 26.622  47.538  1   44.29 ? 94  LYS   A NZ  1 
ATOM   703  N  N   . GLY   A 1 110 ? -2.385  25.192  43.938  1   38.01 ? 95  GLY   A N   1 
ATOM   704  C  CA  . GLY   A 1 110 ? -0.948  25.371  44.057  1   40.23 ? 95  GLY   A CA  1 
ATOM   705  C  C   . GLY   A 1 110 ? -0.452  25.28   45.483  1   42.87 ? 95  GLY   A C   1 
ATOM   706  O  O   . GLY   A 1 110 ? 0.512   25.952  45.842  1   43.45 ? 95  GLY   A O   1 
ATOM   707  N  N   . HIS   A 1 111 ? -1.111  24.474  46.315  1   44.83 ? 96  HIS   A N   1 
ATOM   708  C  CA  . HIS   A 1 111 ? -0.705  24.347  47.721  1   47.05 ? 96  HIS   A CA  1 
ATOM   709  C  C   . HIS   A 1 111 ? -0.375  22.927  48.161  1   47.79 ? 96  HIS   A C   1 
ATOM   710  O  O   . HIS   A 1 111 ? -0.203  22.715  49.353  1   48.77 ? 96  HIS   A O   1 
ATOM   711  C  CB  . HIS   A 1 111 ? -1.741  24.962  48.677  1   49.33 ? 96  HIS   A CB  1 
ATOM   712  C  CG  . HIS   A 1 111 ? -1.953  26.417  48.435  1   54.4  ? 96  HIS   A CG  1 
ATOM   713  N  ND1 . HIS   A 1 111 ? -0.88   27.3    48.368  1   57.05 ? 96  HIS   A ND1 1 
ATOM   714  C  CD2 . HIS   A 1 111 ? -3.1    27.1    48.202  1   56.23 ? 96  HIS   A CD2 1 
ATOM   715  C  CE1 . HIS   A 1 111 ? -1.408  28.489  48.115  1   57.83 ? 96  HIS   A CE1 1 
ATOM   716  N  NE2 . HIS   A 1 111 ? -2.741  28.42   48.005  1   57.86 ? 96  HIS   A NE2 1 
ATOM   717  N  N   . GLY   A 1 112 ? -0.285  21.979  47.236  1   47.26 ? 97  GLY   A N   1 
ATOM   718  C  CA  . GLY   A 1 112 ? 0.098   20.616  47.587  1   47.86 ? 97  GLY   A CA  1 
ATOM   719  C  C   . GLY   A 1 112 ? -0.948  19.548  47.361  1   48.38 ? 97  GLY   A C   1 
ATOM   720  O  O   . GLY   A 1 112 ? -0.612  18.365  47.352  1   48.47 ? 97  GLY   A O   1 
ATOM   721  N  N   . ASP   A 1 113 ? -2.234  19.934  47.209  1   48.31 ? 98  ASP   A N   1 
ATOM   722  C  CA  . ASP   A 1 113 ? -3.281  18.947  46.942  1   48.18 ? 98  ASP   A CA  1 
ATOM   723  C  C   . ASP   A 1 113 ? -3.186  18.717  45.438  1   46.44 ? 98  ASP   A C   1 
ATOM   724  O  O   . ASP   A 1 113 ? -3.656  19.548  44.66   1   46.79 ? 98  ASP   A O   1 
ATOM   725  C  CB  . ASP   A 1 113 ? -4.669  19.497  47.337  1   51.38 ? 98  ASP   A CB  1 
ATOM   726  C  CG  . ASP   A 1 113 ? -5.844  18.589  46.984  1   58.33 ? 98  ASP   A CG  1 
ATOM   727  O  OD1 . ASP   A 1 113 ? -5.608  17.41   46.649  1   60.27 ? 98  ASP   A OD1 1 
ATOM   728  O  OD2 . ASP   A 1 113 ? -6.995  19.053  47.062  1   60.79 ? 98  ASP   A OD2 1 
ATOM   729  N  N   . VAL   A 1 114 ? -2.576  17.609  45.03   1   44.17 ? 99  VAL   A N   1 
ATOM   730  C  CA  . VAL   A 1 114 ? -2.336  17.348  43.618  1   43.43 ? 99  VAL   A CA  1 
ATOM   731  C  C   . VAL   A 1 114 ? -3.211  16.203  43.049  1   42.05 ? 99  VAL   A C   1 
ATOM   732  O  O   . VAL   A 1 114 ? -3.81   15.423  43.794  1   41.52 ? 99  VAL   A O   1 
ATOM   733  C  CB  . VAL   A 1 114 ? -0.82   17.029  43.519  1   44.56 ? 99  VAL   A CB  1 
ATOM   734  C  CG1 . VAL   A 1 114 ? -0.529  15.616  44.009  1   44.44 ? 99  VAL   A CG1 1 
ATOM   735  C  CG2 . VAL   A 1 114 ? -0.263  17.266  42.136  1   45.64 ? 99  VAL   A CG2 1 
ATOM   736  N  N   . ARG   A 1 115 ? -3.292  16.12   41.723  1   41.09 ? 100 ARG   A N   1 
ATOM   737  C  CA  . ARG   A 1 115 ? -3.984  15.043  41.037  1   40.59 ? 100 ARG   A CA  1 
ATOM   738  C  C   . ARG   A 1 115 ? -2.923  14.258  40.267  1   39.92 ? 100 ARG   A C   1 
ATOM   739  O  O   . ARG   A 1 115 ? -2.129  14.85   39.547  1   39.71 ? 100 ARG   A O   1 
ATOM   740  C  CB  . ARG   A 1 115 ? -5.007  15.597  40.045  1   42.3  ? 100 ARG   A CB  1 
ATOM   741  C  CG  . ARG   A 1 115 ? -6.264  16.117  40.701  1   45.79 ? 100 ARG   A CG  1 
ATOM   742  C  CD  . ARG   A 1 115 ? -7.105  14.979  41.22   1   50.43 ? 100 ARG   A CD  1 
ATOM   743  N  NE  . ARG   A 1 115 ? -7.519  15.274  42.587  1   54.17 ? 100 ARG   A NE  1 
ATOM   744  C  CZ  . ARG   A 1 115 ? -8.732  15.681  42.932  1   58.58 ? 100 ARG   A CZ  1 
ATOM   745  N  NH1 . ARG   A 1 115 ? -9.704  15.748  42.022  1   60.16 ? 100 ARG   A NH1 1 
ATOM   746  N  NH2 . ARG   A 1 115 ? -9      15.984  44.199  1   59.19 ? 100 ARG   A NH2 1 
ATOM   747  N  N   . LYS   A 1 116 ? -2.908  12.937  40.408  1   39.31 ? 101 LYS   A N   1 
ATOM   748  C  CA  . LYS   A 1 116 ? -1.924  12.091  39.721  1   39.03 ? 101 LYS   A CA  1 
ATOM   749  C  C   . LYS   A 1 116 ? -2.474  11.379  38.489  1   37.89 ? 101 LYS   A C   1 
ATOM   750  O  O   . LYS   A 1 116 ? -1.749  10.624  37.866  1   39.31 ? 101 LYS   A O   1 
ATOM   751  C  CB  . LYS   A 1 116 ? -1.32   11.08   40.696  1   41.22 ? 101 LYS   A CB  1 
ATOM   752  C  CG  . LYS   A 1 116 ? -0.608  11.77   41.839  1   46.37 ? 101 LYS   A CG  1 
ATOM   753  C  CD  . LYS   A 1 116 ? -0.529  10.907  43.076  1   52.22 ? 101 LYS   A CD  1 
ATOM   754  C  CE  . LYS   A 1 116 ? 0.09    11.653  44.24   1   56.57 ? 101 LYS   A CE  1 
ATOM   755  N  NZ  . LYS   A 1 116 ? 1.579   11.615  44.202  1   57.47 ? 101 LYS   A NZ  1 
ATOM   756  N  N   . VAL   A 1 117 ? -3.752  11.576  38.156  1   36.04 ? 102 VAL   A N   1 
ATOM   757  C  CA  . VAL   A 1 117 ? -4.366  10.973  36.987  1   34.94 ? 102 VAL   A CA  1 
ATOM   758  C  C   . VAL   A 1 117 ? -5.099  12.078  36.277  1   33.59 ? 102 VAL   A C   1 
ATOM   759  O  O   . VAL   A 1 117 ? -5.911  12.764  36.892  1   33.24 ? 102 VAL   A O   1 
ATOM   760  C  CB  . VAL   A 1 117 ? -5.365  9.819   37.335  1   35.82 ? 102 VAL   A CB  1 
ATOM   761  C  CG1 . VAL   A 1 117 ? -5.907  9.168   36.068  1   36    ? 102 VAL   A CG1 1 
ATOM   762  C  CG2 . VAL   A 1 117 ? -4.741  8.77    38.249  1   35.93 ? 102 VAL   A CG2 1 
ATOM   763  N  N   . LEU   A 1 118 ? -4.837  12.242  34.985  1   32.85 ? 103 LEU   A N   1 
ATOM   764  C  CA  . LEU   A 1 118 ? -5.511  13.227  34.152  1   32.36 ? 103 LEU   A CA  1 
ATOM   765  C  C   . LEU   A 1 118 ? -6.663  12.454  33.5    1   33.18 ? 103 LEU   A C   1 
ATOM   766  O  O   . LEU   A 1 118 ? -6.424  11.407  32.892  1   32.4  ? 103 LEU   A O   1 
ATOM   767  C  CB  . LEU   A 1 118 ? -4.549  13.781  33.101  1   31.15 ? 103 LEU   A CB  1 
ATOM   768  C  CG  . LEU   A 1 118 ? -5.067  14.916  32.266  1   31.8  ? 103 LEU   A CG  1 
ATOM   769  C  CD1 . LEU   A 1 118 ? -5.203  16.171  33.083  1   31.62 ? 103 LEU   A CD1 1 
ATOM   770  C  CD2 . LEU   A 1 118 ? -4.169  15.158  31.08   1   32.36 ? 103 LEU   A CD2 1 
ATOM   771  N  N   . PRO   A 1 119 ? -7.911  12.936  33.681  1   33.94 ? 104 PRO   A N   1 
ATOM   772  C  CA  . PRO   A 1 119 ? -9.083  12.201  33.168  1   33.54 ? 104 PRO   A CA  1 
ATOM   773  C  C   . PRO   A 1 119 ? -9.05   11.989  31.674  1   33.12 ? 104 PRO   A C   1 
ATOM   774  O  O   . PRO   A 1 119 ? -8.591  12.861  30.941  1   33.27 ? 104 PRO   A O   1 
ATOM   775  C  CB  . PRO   A 1 119 ? -10.274 13.084  33.576  1   34.89 ? 104 PRO   A CB  1 
ATOM   776  C  CG  . PRO   A 1 119 ? -9.763  13.948  34.693  1   35.53 ? 104 PRO   A CG  1 
ATOM   777  C  CD  . PRO   A 1 119 ? -8.313  14.17   34.394  1   33.8  ? 104 PRO   A CD  1 
ATOM   778  N  N   . ARG   A 1 120 ? -9.541  10.838  31.222  1   32.33 ? 105 ARG   A N   1 
ATOM   779  C  CA  . ARG   A 1 120 ? -9.536  10.498  29.81   1   33.09 ? 105 ARG   A CA  1 
ATOM   780  C  C   . ARG   A 1 120 ? -10.18  11.526  28.901  1   33.76 ? 105 ARG   A C   1 
ATOM   781  O  O   . ARG   A 1 120 ? -9.716  11.674  27.762  1   34.96 ? 105 ARG   A O   1 
ATOM   782  C  CB  . ARG   A 1 120 ? -10.177 9.132   29.579  1   35.27 ? 105 ARG   A CB  1 
ATOM   783  C  CG  . ARG   A 1 120 ? -11.727 9.081   29.807  1   37.89 ? 105 ARG   A CG  1 
ATOM   784  C  CD  . ARG   A 1 120 ? -12.249 7.699   30.261  1   40.37 ? 105 ARG   A CD  1 
ATOM   785  N  NE  . ARG   A 1 120 ? -11.53  6.652   29.558  1   43.34 ? 105 ARG   A NE  1 
ATOM   786  C  CZ  . ARG   A 1 120 ? -10.838 5.682   30.133  1   42.94 ? 105 ARG   A CZ  1 
ATOM   787  N  NH1 . ARG   A 1 120 ? -10.891 5.506   31.449  1   41.54 ? 105 ARG   A NH1 1 
ATOM   788  N  NH2 . ARG   A 1 120 ? -10.171 4.824   29.396  1   44.55 ? 105 ARG   A NH2 1 
ATOM   789  N  N   . ASN   A 1 121 ? -11.246 12.217  29.376  1   32.96 ? 106 ASN   A N   1 
ATOM   790  C  CA  . ASN   A 1 121 ? -11.966 13.212  28.574  1   34.17 ? 106 ASN   A CA  1 
ATOM   791  C  C   . ASN   A 1 121 ? -11.054 14.299  28.058  1   34.3  ? 106 ASN   A C   1 
ATOM   792  O  O   . ASN   A 1 121 ? -11.309 14.818  26.975  1   34.88 ? 106 ASN   A O   1 
ATOM   793  C  CB  . ASN   A 1 121 ? -13.197 13.805  29.307  1   35.11 ? 106 ASN   A CB  1 
ATOM   794  C  CG  . ASN   A 1 121 ? -12.896 14.361  30.698  1   38.96 ? 106 ASN   A CG  1 
ATOM   795  O  OD1 . ASN   A 1 121 ? -11.74  14.49   31.11   1   40.27 ? 106 ASN   A OD1 1 
ATOM   796  N  ND2 . ASN   A 1 121 ? -13.921 14.696  31.473  1   38.88 ? 106 ASN   A ND2 1 
ATOM   797  N  N   . ILE   A 1 122 ? -9.983  14.637  28.808  1   34.38 ? 107 ILE   A N   1 
ATOM   798  C  CA  . ILE   A 1 122 ? -8.999  15.617  28.343  1   34.52 ? 107 ILE   A CA  1 
ATOM   799  C  C   . ILE   A 1 122 ? -7.675  14.965  27.967  1   33.87 ? 107 ILE   A C   1 
ATOM   800  O  O   . ILE   A 1 122 ? -7.075  15.391  26.996  1   34.4  ? 107 ILE   A O   1 
ATOM   801  C  CB  . ILE   A 1 122 ? -8.774  16.831  29.283  1   35.58 ? 107 ILE   A CB  1 
ATOM   802  C  CG1 . ILE   A 1 122 ? -8.452  16.418  30.702  1   37.15 ? 107 ILE   A CG1 1 
ATOM   803  C  CG2 . ILE   A 1 122 ? -9.923  17.805  29.239  1   35.91 ? 107 ILE   A CG2 1 
ATOM   804  C  CD1 . ILE   A 1 122 ? -7.799  17.523  31.41   1   39.23 ? 107 ILE   A CD1 1 
ATOM   805  N  N   . ALA   A 1 123 ? -7.216  13.94   28.702  1   32.79 ? 108 ALA   A N   1 
ATOM   806  C  CA  . ALA   A 1 123 ? -5.94   13.289  28.402  1   32.76 ? 108 ALA   A CA  1 
ATOM   807  C  C   . ALA   A 1 123 ? -5.877  12.692  27.011  1   33.52 ? 108 ALA   A C   1 
ATOM   808  O  O   . ALA   A 1 123 ? -4.833  12.806  26.351  1   34.44 ? 108 ALA   A O   1 
ATOM   809  C  CB  . ALA   A 1 123 ? -5.625  12.215  29.431  1   32.31 ? 108 ALA   A CB  1 
ATOM   810  N  N   . VAL   A 1 124 ? -6.988  12.097  26.535  1   32.9  ? 109 VAL   A N   1 
ATOM   811  C  CA  . VAL   A 1 124 ? -6.987  11.488  25.217  1   32.96 ? 109 VAL   A CA  1 
ATOM   812  C  C   . VAL   A 1 124 ? -6.868  12.544  24.12   1   33.01 ? 109 VAL   A C   1 
ATOM   813  O  O   . VAL   A 1 124 ? -5.889  12.465  23.368  1   33.78 ? 109 VAL   A O   1 
ATOM   814  C  CB  . VAL   A 1 124 ? -8.158  10.485  24.999  1   33.74 ? 109 VAL   A CB  1 
ATOM   815  C  CG1 . VAL   A 1 124 ? -8.335  10.146  23.52   1   34.42 ? 109 VAL   A CG1 1 
ATOM   816  C  CG2 . VAL   A 1 124 ? -7.941  9.224   25.823  1   33.1  ? 109 VAL   A CG2 1 
ATOM   817  N  N   . PRO   A 1 125 ? -7.744  13.562  24.011  1   32.75 ? 110 PRO   A N   1 
ATOM   818  C  CA  . PRO   A 1 125 ? -7.551  14.565  22.943  1   32.69 ? 110 PRO   A CA  1 
ATOM   819  C  C   . PRO   A 1 125 ? -6.217  15.338  23.068  1   32.56 ? 110 PRO   A C   1 
ATOM   820  O  O   . PRO   A 1 125 ? -5.618  15.745  22.063  1   32.12 ? 110 PRO   A O   1 
ATOM   821  C  CB  . PRO   A 1 125 ? -8.785  15.484  23.073  1   33.31 ? 110 PRO   A CB  1 
ATOM   822  C  CG  . PRO   A 1 125 ? -9.28   15.285  24.439  1   33.95 ? 110 PRO   A CG  1 
ATOM   823  C  CD  . PRO   A 1 125 ? -8.953  13.859  24.808  1   32.35 ? 110 PRO   A CD  1 
ATOM   824  N  N   . TYR   A 1 126 ? -5.754  15.544  24.305  1   32.1  ? 111 TYR   A N   1 
ATOM   825  C  CA  . TYR   A 1 126 ? -4.501  16.261  24.546  1   31.27 ? 111 TYR   A CA  1 
ATOM   826  C  C   . TYR   A 1 126 ? -3.335  15.461  24.002  1   32.1  ? 111 TYR   A C   1 
ATOM   827  O  O   . TYR   A 1 126 ? -2.557  16.011  23.227  1   32.09 ? 111 TYR   A O   1 
ATOM   828  C  CB  . TYR   A 1 126 ? -4.346  16.587  26.043  1   29.91 ? 111 TYR   A CB  1 
ATOM   829  C  CG  . TYR   A 1 126 ? -3.198  17.506  26.397  1   28.86 ? 111 TYR   A CG  1 
ATOM   830  C  CD1 . TYR   A 1 126 ? -2.736  18.456  25.496  1   28.59 ? 111 TYR   A CD1 1 
ATOM   831  C  CD2 . TYR   A 1 126 ? -2.594  17.442  27.64   1   28.66 ? 111 TYR   A CD2 1 
ATOM   832  C  CE1 . TYR   A 1 126 ? -1.662  19.288  25.811  1   28.53 ? 111 TYR   A CE1 1 
ATOM   833  C  CE2 . TYR   A 1 126 ? -1.539  18.287  27.978  1   28.3  ? 111 TYR   A CE2 1 
ATOM   834  C  CZ  . TYR   A 1 126 ? -1.076  19.211  27.061  1   28    ? 111 TYR   A CZ  1 
ATOM   835  O  OH  . TYR   A 1 126 ? -0.046  20.063  27.411  1   25.57 ? 111 TYR   A OH  1 
ATOM   836  N  N   . CYS   A 1 127 ? -3.247  14.154  24.32   1   32.17 ? 112 CYS   A N   1 
ATOM   837  C  CA  . CYS   A 1 127 ? -2.169  13.309  23.797  1   32.7  ? 112 CYS   A CA  1 
ATOM   838  C  C   . CYS   A 1 127 ? -2.25   13.104  22.291  1   34.2  ? 112 CYS   A C   1 
ATOM   839  O  O   . CYS   A 1 127 ? -1.215  12.948  21.636  1   34.91 ? 112 CYS   A O   1 
ATOM   840  C  CB  . CYS   A 1 127 ? -2.106  11.971  24.516  1   32.41 ? 112 CYS   A CB  1 
ATOM   841  S  SG  . CYS   A 1 127 ? -1.667  12.07   26.264  1   35.58 ? 112 CYS   A SG  1 
ATOM   842  N  N   . GLN   A 1 128 ? -3.462  13.064  21.738  1   34.47 ? 113 GLN   A N   1 
ATOM   843  C  CA  . GLN   A 1 128 ? -3.619  12.882  20.293  1   34.55 ? 113 GLN   A CA  1 
ATOM   844  C  C   . GLN   A 1 128 ? -3.105  14.122  19.555  1   35.21 ? 113 GLN   A C   1 
ATOM   845  O  O   . GLN   A 1 128 ? -2.409  14.014  18.547  1   36.14 ? 113 GLN   A O   1 
ATOM   846  C  CB  . GLN   A 1 128 ? -5.1    12.619  19.944  1   35.17 ? 113 GLN   A CB  1 
ATOM   847  C  CG  . GLN   A 1 128 ? -5.599  11.263  20.43   1   37    ? 113 GLN   A CG  1 
ATOM   848  C  CD  . GLN   A 1 128 ? -7.067  11.061  20.123  1   41.48 ? 113 GLN   A CD  1 
ATOM   849  O  OE1 . GLN   A 1 128 ? -7.856  12.016  19.951  1   40.67 ? 113 GLN   A OE1 1 
ATOM   850  N  NE2 . GLN   A 1 128 ? -7.463  9.803   20.045  1   42.43 ? 113 GLN   A NE2 1 
ATOM   851  N  N   . LEU   A 1 129 ? -3.452  15.293  20.061  1   34.51 ? 114 LEU   A N   1 
ATOM   852  C  CA  . LEU   A 1 129 ? -3.036  16.541  19.463  1   34.63 ? 114 LEU   A CA  1 
ATOM   853  C  C   . LEU   A 1 129 ? -1.524  16.742  19.628  1   34.75 ? 114 LEU   A C   1 
ATOM   854  O  O   . LEU   A 1 129 ? -0.86   17.176  18.696  1   35.16 ? 114 LEU   A O   1 
ATOM   855  C  CB  . LEU   A 1 129 ? -3.809  17.649  20.148  1   35.04 ? 114 LEU   A CB  1 
ATOM   856  C  CG  . LEU   A 1 129 ? -3.528  19.016  19.668  1   37.43 ? 114 LEU   A CG  1 
ATOM   857  C  CD1 . LEU   A 1 129 ? -3.933  19.163  18.205  1   38.08 ? 114 LEU   A CD1 1 
ATOM   858  C  CD2 . LEU   A 1 129 ? -4.282  19.991  20.498  1   38.24 ? 114 LEU   A CD2 1 
ATOM   859  N  N   . SER   A 1 130 ? -0.97   16.345  20.778  1   34.73 ? 115 SER   A N   1 
ATOM   860  C  CA  . SER   A 1 130 ? 0.459   16.412  21.052  1   35.49 ? 115 SER   A CA  1 
ATOM   861  C  C   . SER   A 1 130 ? 1.22    15.494  20.094  1   37.17 ? 115 SER   A C   1 
ATOM   862  O  O   . SER   A 1 130 ? 2.239   15.915  19.547  1   37.27 ? 115 SER   A O   1 
ATOM   863  C  CB  . SER   A 1 130 ? 0.757   16.015  22.494  1   35.36 ? 115 SER   A CB  1 
ATOM   864  O  OG  . SER   A 1 130 ? 0.191   16.953  23.393  1   36.2  ? 115 SER   A OG  1 
ATOM   865  N  N   . LYS   A 1 131 ? 0.718   14.274  19.849  1   37.58 ? 116 LYS   A N   1 
ATOM   866  C  CA  . LYS   A 1 131 ? 1.376   13.358  18.919  1   38.71 ? 116 LYS   A CA  1 
ATOM   867  C  C   . LYS   A 1 131 ? 1.401   13.919  17.503  1   39.79 ? 116 LYS   A C   1 
ATOM   868  O  O   . LYS   A 1 131 ? 2.398   13.783  16.798  1   41.22 ? 116 LYS   A O   1 
ATOM   869  C  CB  . LYS   A 1 131 ? 0.709   11.974  18.913  1   40.75 ? 116 LYS   A CB  1 
ATOM   870  C  CG  . LYS   A 1 131 ? 1.532   10.963  18.119  1   45.23 ? 116 LYS   A CG  1 
ATOM   871  C  CD  . LYS   A 1 131 ? 0.946   9.557   18.108  1   51.14 ? 116 LYS   A CD  1 
ATOM   872  C  CE  . LYS   A 1 131 ? 2.052   8.519   17.997  1   55.45 ? 116 LYS   A CE  1 
ATOM   873  N  N   . LYS   A 1 132 ? 0.326   14.569  17.099  1   39.84 ? 117 LYS   A N   1 
ATOM   874  C  CA  . LYS   A 1 132 ? 0.185   15.177  15.789  1   40.69 ? 117 LYS   A CA  1 
ATOM   875  C  C   . LYS   A 1 132 ? 1.174   16.345  15.629  1   40.88 ? 117 LYS   A C   1 
ATOM   876  O  O   . LYS   A 1 132 ? 1.772   16.503  14.567  1   41.63 ? 117 LYS   A O   1 
ATOM   877  C  CB  . LYS   A 1 132 ? -1.27   15.663  15.628  1   43.95 ? 117 LYS   A CB  1 
ATOM   878  C  CG  . LYS   A 1 132 ? -1.669  16.014  14.207  1   49.9  ? 117 LYS   A CG  1 
ATOM   879  C  CD  . LYS   A 1 132 ? -3.182  16.141  14.074  1   56.41 ? 117 LYS   A CD  1 
ATOM   880  C  CE  . LYS   A 1 132 ? -3.569  16.796  12.765  1   62.29 ? 117 LYS   A CE  1 
ATOM   881  N  NZ  . LYS   A 1 132 ? -3.938  15.805  11.708  1   65.37 ? 117 LYS   A NZ  1 
ATOM   882  N  N   . LEU   A 1 133 ? 1.337   17.169  16.669  1   40.06 ? 118 LEU   A N   1 
ATOM   883  C  CA  . LEU   A 1 133 ? 2.262   18.305  16.608  1   40.15 ? 118 LEU   A CA  1 
ATOM   884  C  C   . LEU   A 1 133 ? 3.702   17.956  17.003  1   39.8  ? 118 LEU   A C   1 
ATOM   885  O  O   . LEU   A 1 133 ? 4.543   18.843  16.998  1   40.39 ? 118 LEU   A O   1 
ATOM   886  C  CB  . LEU   A 1 133 ? 1.727   19.465  17.476  1   40.47 ? 118 LEU   A CB  1 
ATOM   887  C  CG  . LEU   A 1 133 ? 0.429   20.116  16.968  1   41.58 ? 118 LEU   A CG  1 
ATOM   888  C  CD1 . LEU   A 1 133 ? -0.081  21.131  17.938  1   41.94 ? 118 LEU   A CD1 1 
ATOM   889  C  CD2 . LEU   A 1 133 ? 0.633   20.767  15.629  1   42.25 ? 118 LEU   A CD2 1 
ATOM   890  N  N   . GLU   A 1 134 ? 3.98    16.682  17.347  1   39.24 ? 119 GLU   A N   1 
ATOM   891  C  CA  . GLU   A 1 134 ? 5.263   16.132  17.79   1   39.2  ? 119 GLU   A CA  1 
ATOM   892  C  C   . GLU   A 1 134 ? 5.807   16.855  19.006  1   38.33 ? 119 GLU   A C   1 
ATOM   893  O  O   . GLU   A 1 134 ? 6.968   17.264  19.045  1   38.87 ? 119 GLU   A O   1 
ATOM   894  C  CB  . GLU   A 1 134 ? 6.295   16.08   16.672  1   42.76 ? 119 GLU   A CB  1 
ATOM   895  C  CG  . GLU   A 1 134 ? 5.89    15.219  15.5    1   48.59 ? 119 GLU   A CG  1 
ATOM   896  C  CD  . GLU   A 1 134 ? 6.971   15.269  14.447  1   56.99 ? 119 GLU   A CD  1 
ATOM   897  O  OE1 . GLU   A 1 134 ? 8.095   14.803  14.739  1   57.28 ? 119 GLU   A OE1 1 
ATOM   898  O  OE2 . GLU   A 1 134 ? 6.71    15.824  13.354  1   61.94 ? 119 GLU   A OE2 1 
ATOM   899  N  N   . LEU   A 1 135 ? 4.96    17.004  20.006  1   36.4  ? 120 LEU   A N   1 
ATOM   900  C  CA  . LEU   A 1 135 ? 5.325   17.654  21.255  1   34.69 ? 120 LEU   A CA  1 
ATOM   901  C  C   . LEU   A 1 135 ? 4.814   16.79   22.392  1   34.03 ? 120 LEU   A C   1 
ATOM   902  O  O   . LEU   A 1 135 ? 3.856   16.039  22.217  1   34.46 ? 120 LEU   A O   1 
ATOM   903  C  CB  . LEU   A 1 135 ? 4.695   19.056  21.312  1   34.3  ? 120 LEU   A CB  1 
ATOM   904  C  CG  . LEU   A 1 135 ? 5.344   20.086  20.416  1   34.65 ? 120 LEU   A CG  1 
ATOM   905  C  CD1 . LEU   A 1 135 ? 4.469   21.309  20.259  1   35.16 ? 120 LEU   A CD1 1 
ATOM   906  C  CD2 . LEU   A 1 135 ? 6.719   20.454  20.946  1   35.27 ? 120 LEU   A CD2 1 
ATOM   907  N  N   . PRO   A 1 136 ? 5.425   16.884  23.58   1   33    ? 121 PRO   A N   1 
ATOM   908  C  CA  . PRO   A 1 136 ? 4.917   16.113  24.711  1   32.55 ? 121 PRO   A CA  1 
ATOM   909  C  C   . PRO   A 1 136 ? 3.596   16.675  25.259  1   32.43 ? 121 PRO   A C   1 
ATOM   910  O  O   . PRO   A 1 136 ? 3.278   17.862  25.087  1   33.14 ? 121 PRO   A O   1 
ATOM   911  C  CB  . PRO   A 1 136 ? 6.041   16.237  25.735  1   33.91 ? 121 PRO   A CB  1 
ATOM   912  C  CG  . PRO   A 1 136 ? 6.649   17.555  25.459  1   34.41 ? 121 PRO   A CG  1 
ATOM   913  C  CD  . PRO   A 1 136 ? 6.6     17.697  23.96   1   32.62 ? 121 PRO   A CD  1 
ATOM   914  N  N   . PRO   A 1 137 ? 2.804   15.834  25.941  1   31.23 ? 122 PRO   A N   1 
ATOM   915  C  CA  . PRO   A 1 137 ? 1.52    16.314  26.479  1   30.65 ? 122 PRO   A CA  1 
ATOM   916  C  C   . PRO   A 1 137 ? 1.685   17.058  27.806  1   29.62 ? 122 PRO   A C   1 
ATOM   917  O  O   . PRO   A 1 137 ? 1.226   16.61   28.864  1   29.82 ? 122 PRO   A O   1 
ATOM   918  C  CB  . PRO   A 1 137 ? 0.685   15.027  26.599  1   31.49 ? 122 PRO   A CB  1 
ATOM   919  C  CG  . PRO   A 1 137 ? 1.706   13.952  26.868  1   31.37 ? 122 PRO   A CG  1 
ATOM   920  C  CD  . PRO   A 1 137 ? 2.989   14.38   26.153  1   30.5  ? 122 PRO   A CD  1 
ATOM   921  N  N   . ILE   A 1 138 ? 2.38    18.193  27.742  1   27.33 ? 123 ILE   A N   1 
ATOM   922  C  CA  . ILE   A 1 138 ? 2.623   19.089  28.867  1   26.25 ? 123 ILE   A CA  1 
ATOM   923  C  C   . ILE   A 1 138 ? 2.82    20.479  28.263  1   24.69 ? 123 ILE   A C   1 
ATOM   924  O  O   . ILE   A 1 138 ? 3.189   20.622  27.079  1   24.21 ? 123 ILE   A O   1 
ATOM   925  C  CB  . ILE   A 1 138 ? 3.801   18.651  29.792  1   27.83 ? 123 ILE   A CB  1 
ATOM   926  C  CG1 . ILE   A 1 138 ? 3.792   19.456  31.143  1   29.18 ? 123 ILE   A CG1 1 
ATOM   927  C  CG2 . ILE   A 1 138 ? 5.166   18.745  29.085  1   27.86 ? 123 ILE   A CG2 1 
ATOM   928  C  CD1 . ILE   A 1 138 ? 4.73    18.947  32.185  1   31.2  ? 123 ILE   A CD1 1 
ATOM   929  N  N   . LEU   A 1 139 ? 2.488   21.515  29.032  1   23.13 ? 124 LEU   A N   1 
ATOM   930  C  CA  . LEU   A 1 139 ? 2.644   22.886  28.576  1   23.43 ? 124 LEU   A CA  1 
ATOM   931  C  C   . LEU   A 1 139 ? 4.159   23.169  28.395  1   23.56 ? 124 LEU   A C   1 
ATOM   932  O  O   . LEU   A 1 139 ? 4.944   22.937  29.318  1   23.18 ? 124 LEU   A O   1 
ATOM   933  C  CB  . LEU   A 1 139 ? 2.088   23.803  29.653  1   24.16 ? 124 LEU   A CB  1 
ATOM   934  C  CG  . LEU   A 1 139 ? 1.933   25.258  29.262  1   26.55 ? 124 LEU   A CG  1 
ATOM   935  C  CD1 . LEU   A 1 139 ? 0.829   25.437  28.181  1   26.45 ? 124 LEU   A CD1 1 
ATOM   936  C  CD2 . LEU   A 1 139 ? 1.643   26.105  30.469  1   27.74 ? 124 LEU   A CD2 1 
ATOM   937  N  N   . VAL   A 1 140 ? 4.556   23.632  27.2    1   23.01 ? 125 VAL   A N   1 
ATOM   938  C  CA  . VAL   A 1 140 ? 5.935   23.959  26.876  1   23.86 ? 125 VAL   A CA  1 
ATOM   939  C  C   . VAL   A 1 140 ? 5.996   25.456  26.577  1   23.16 ? 125 VAL   A C   1 
ATOM   940  O  O   . VAL   A 1 140 ? 4.961   26.104  26.372  1   23.22 ? 125 VAL   A O   1 
ATOM   941  C  CB  . VAL   A 1 140 ? 6.477   23.104  25.687  1   25.08 ? 125 VAL   A CB  1 
ATOM   942  C  CG1 . VAL   A 1 140 ? 6.382   21.604  25.976  1   24.94 ? 125 VAL   A CG1 1 
ATOM   943  C  CG2 . VAL   A 1 140 ? 5.774   23.438  24.396  1   25.54 ? 125 VAL   A CG2 1 
ATOM   944  N  N   . TYR   A 1 141 ? 7.192   25.998  26.548  1   23.61 ? 126 TYR   A N   1 
ATOM   945  C  CA  . TYR   A 1 141 ? 7.476   27.401  26.244  1   22.76 ? 126 TYR   A CA  1 
ATOM   946  C  C   . TYR   A 1 141 ? 6.818   27.814  24.904  1   22.26 ? 126 TYR   A C   1 
ATOM   947  O  O   . TYR   A 1 141 ? 6.335   28.93   24.796  1   22.84 ? 126 TYR   A O   1 
ATOM   948  C  CB  . TYR   A 1 141 ? 9.018   27.56   26.176  1   22.53 ? 126 TYR   A CB  1 
ATOM   949  C  CG  . TYR   A 1 141 ? 9.497   28.927  25.77   1   24.15 ? 126 TYR   A CG  1 
ATOM   950  C  CD1 . TYR   A 1 141 ? 9.722   29.239  24.435  1   25.42 ? 126 TYR   A CD1 1 
ATOM   951  C  CD2 . TYR   A 1 141 ? 9.852   29.865  26.724  1   26.05 ? 126 TYR   A CD2 1 
ATOM   952  C  CE1 . TYR   A 1 141 ? 10.231  30.478  24.063  1   26.85 ? 126 TYR   A CE1 1 
ATOM   953  C  CE2 . TYR   A 1 141 ? 10.358  31.103  26.366  1   27.14 ? 126 TYR   A CE2 1 
ATOM   954  C  CZ  . TYR   A 1 141 ? 10.522  31.417  25.036  1   28.48 ? 126 TYR   A CZ  1 
ATOM   955  O  OH  . TYR   A 1 141 ? 11.029  32.656  24.714  1   29.09 ? 126 TYR   A OH  1 
ATOM   956  N  N   . ALA   A 1 142 ? 6.824   26.939  23.891  1   22.56 ? 127 ALA   A N   1 
ATOM   957  C  CA  . ALA   A 1 142 ? 6.201   27.263  22.595  1   23.08 ? 127 ALA   A CA  1 
ATOM   958  C  C   . ALA   A 1 142 ? 4.654   27.468  22.727  1   23.75 ? 127 ALA   A C   1 
ATOM   959  O  O   . ALA   A 1 142 ? 4.038   28.14   21.9    1   26.03 ? 127 ALA   A O   1 
ATOM   960  C  CB  . ALA   A 1 142 ? 6.49    26.175  21.574  1   23.4  ? 127 ALA   A CB  1 
ATOM   961  N  N   . ASP   A 1 143 ? 4.033   26.881  23.768  1   22.77 ? 128 ASP   A N   1 
ATOM   962  C  CA  . ASP   A 1 143 ? 2.603   27.082  24.01   1   23.87 ? 128 ASP   A CA  1 
ATOM   963  C  C   . ASP   A 1 143 ? 2.414   28.354  24.846  1   25.53 ? 128 ASP   A C   1 
ATOM   964  O  O   . ASP   A 1 143 ? 1.73    29.26   24.383  1   28.24 ? 128 ASP   A O   1 
ATOM   965  C  CB  . ASP   A 1 143 ? 1.984   25.924  24.795  1   23.48 ? 128 ASP   A CB  1 
ATOM   966  C  CG  . ASP   A 1 143 ? 2.147   24.559  24.19   1   26.1  ? 128 ASP   A CG  1 
ATOM   967  O  OD1 . ASP   A 1 143 ? 1.879   24.411  22.961  1   26.31 ? 128 ASP   A OD1 1 
ATOM   968  O  OD2 . ASP   A 1 143 ? 2.461   23.623  24.945  1   27.17 ? 128 ASP   A OD2 1 
ATOM   969  N  N   . CYS   A 1 144 ? 2.968   28.406  26.086  1   24.77 ? 129 CYS   A N   1 
ATOM   970  C  CA  . CYS   A 1 144 ? 2.718   29.51   27.012  1   24.57 ? 129 CYS   A CA  1 
ATOM   971  C  C   . CYS   A 1 144 ? 3.368   30.837  26.61   1   24.72 ? 129 CYS   A C   1 
ATOM   972  O  O   . CYS   A 1 144 ? 2.921   31.88   27.116  1   24.49 ? 129 CYS   A O   1 
ATOM   973  C  CB  . CYS   A 1 144 ? 3.045   29.14   28.463  1   25.32 ? 129 CYS   A CB  1 
ATOM   974  S  SG  . CYS   A 1 144 ? 4.81    28.824  28.795  1   32.73 ? 129 CYS   A SG  1 
ATOM   975  N  N   . VAL   A 1 145 ? 4.397   30.84   25.728  1   24.86 ? 130 VAL   A N   1 
ATOM   976  C  CA  . VAL   A 1 145 ? 4.986   32.106  25.299  1   25.58 ? 130 VAL   A CA  1 
ATOM   977  C  C   . VAL   A 1 145 ? 4.721   32.319  23.788  1   26.6  ? 130 VAL   A C   1 
ATOM   978  O  O   . VAL   A 1 145 ? 4.117   33.318  23.416  1   27.09 ? 130 VAL   A O   1 
ATOM   979  C  CB  . VAL   A 1 145 ? 6.499   32.186  25.639  1   26.43 ? 130 VAL   A CB  1 
ATOM   980  C  CG1 . VAL   A 1 145 ? 7.198   33.337  24.905  1   26.5  ? 130 VAL   A CG1 1 
ATOM   981  C  CG2 . VAL   A 1 145 ? 6.747   32.259  27.142  1   26.56 ? 130 VAL   A CG2 1 
ATOM   982  N  N   . LEU   A 1 146 ? 5.153   31.387  22.942  1   26.14 ? 131 LEU   A N   1 
ATOM   983  C  CA  . LEU   A 1 146 ? 5.154   31.576  21.493  1   26.9  ? 131 LEU   A CA  1 
ATOM   984  C  C   . LEU   A 1 146 ? 3.77    31.657  20.83   1   28.52 ? 131 LEU   A C   1 
ATOM   985  O  O   . LEU   A 1 146 ? 3.619   32.367  19.834  1   29.66 ? 131 LEU   A O   1 
ATOM   986  C  CB  . LEU   A 1 146 ? 6.039   30.509  20.81   1   26.75 ? 131 LEU   A CB  1 
ATOM   987  C  CG  . LEU   A 1 146 ? 7.552   30.506  21.268  1   27.47 ? 131 LEU   A CG  1 
ATOM   988  C  CD1 . LEU   A 1 146 ? 8.385   29.546  20.48   1   27.99 ? 131 LEU   A CD1 1 
ATOM   989  C  CD2 . LEU   A 1 146 ? 8.168   31.891  21.2    1   28.83 ? 131 LEU   A CD2 1 
ATOM   990  N  N   . ALA   A 1 147 ? 2.775   30.957  21.36   1   28.49 ? 132 ALA   A N   1 
ATOM   991  C  CA  . ALA   A 1 147 ? 1.399   30.934  20.832  1   28.84 ? 132 ALA   A CA  1 
ATOM   992  C  C   . ALA   A 1 147 ? 0.367   31.644  21.754  1   28.97 ? 132 ALA   A C   1 
ATOM   993  O  O   . ALA   A 1 147 ? -0.82   31.703  21.445  1   29.76 ? 132 ALA   A O   1 
ATOM   994  C  CB  . ALA   A 1 147 ? 0.979   29.484  20.628  1   28.2  ? 132 ALA   A CB  1 
ATOM   995  N  N   . ASN   A 1 148 ? 0.801   32.11   22.923  1   28.06 ? 133 ASN   A N   1 
ATOM   996  C  CA  . ASN   A 1 148 ? -0.082  32.691  23.927  1   26.76 ? 133 ASN   A CA  1 
ATOM   997  C  C   . ASN   A 1 148 ? -0.122  34.207  23.857  1   27.93 ? 133 ASN   A C   1 
ATOM   998  O  O   . ASN   A 1 148 ? 0.078   34.885  24.865  1   27.12 ? 133 ASN   A O   1 
ATOM   999  C  CB  . ASN   A 1 148 ? 0.381   32.215  25.286  1   25.28 ? 133 ASN   A CB  1 
ATOM   1000 C  CG  . ASN   A 1 148 ? -0.535  32.488  26.434  1   23.29 ? 133 ASN   A CG  1 
ATOM   1001 O  OD1 . ASN   A 1 148 ? -1.749  32.793  26.264  1   21.23 ? 133 ASN   A OD1 1 
ATOM   1002 N  ND2 . ASN   A 1 148 ? 0.016   32.359  27.661  1   21.89 ? 133 ASN   A ND2 1 
ATOM   1003 N  N   . TRP   A 1 149 ? -0.484  34.746  22.674  1   28.35 ? 134 TRP   A N   1 
ATOM   1004 C  CA  . TRP   A 1 149 ? -0.482  36.192  22.535  1   28.9  ? 134 TRP   A CA  1 
ATOM   1005 C  C   . TRP   A 1 149 ? -1.421  36.723  21.464  1   30.63 ? 134 TRP   A C   1 
ATOM   1006 O  O   . TRP   A 1 149 ? -1.827  35.993  20.576  1   31.29 ? 134 TRP   A O   1 
ATOM   1007 C  CB  . TRP   A 1 149 ? 0.967   36.674  22.277  1   28.06 ? 134 TRP   A CB  1 
ATOM   1008 C  CG  . TRP   A 1 149 ? 1.524   36.34   20.919  1   28.43 ? 134 TRP   A CG  1 
ATOM   1009 C  CD1 . TRP   A 1 149 ? 2.153   35.191  20.54   1   28.56 ? 134 TRP   A CD1 1 
ATOM   1010 C  CD2 . TRP   A 1 149 ? 1.561   37.212  19.781  1   29.07 ? 134 TRP   A CD2 1 
ATOM   1011 N  NE1 . TRP   A 1 149 ? 2.544   35.277  19.217  1   28.2  ? 134 TRP   A NE1 1 
ATOM   1012 C  CE2 . TRP   A 1 149 ? 2.247   36.533  18.751  1   29.02 ? 134 TRP   A CE2 1 
ATOM   1013 C  CE3 . TRP   A 1 149 ? 1.162   38.541  19.564  1   30.39 ? 134 TRP   A CE3 1 
ATOM   1014 C  CZ2 . TRP   A 1 149 ? 2.45    37.102  17.5    1   30.16 ? 134 TRP   A CZ2 1 
ATOM   1015 C  CZ3 . TRP   A 1 149 ? 1.386   39.109  18.325  1   31.19 ? 134 TRP   A CZ3 1 
ATOM   1016 C  CH2 . TRP   A 1 149 ? 2.024   38.39   17.311  1   31.13 ? 134 TRP   A CH2 1 
ATOM   1017 N  N   . LYS   A 1 150 ? -1.688  38.018  21.511  1   31.23 ? 135 LYS   A N   1 
ATOM   1018 C  CA  . LYS   A 1 150 ? -2.468  38.707  20.504  1   33.02 ? 135 LYS   A CA  1 
ATOM   1019 C  C   . LYS   A 1 150 ? -2.099  40.175  20.525  1   34.82 ? 135 LYS   A C   1 
ATOM   1020 O  O   . LYS   A 1 150 ? -1.64   40.709  21.551  1   35.11 ? 135 LYS   A O   1 
ATOM   1021 C  CB  . LYS   A 1 150 ? -3.986  38.56   20.782  1   35.42 ? 135 LYS   A CB  1 
ATOM   1022 C  CG  . LYS   A 1 150 ? -4.455  39.185  22.106  1   41.54 ? 135 LYS   A CG  1 
ATOM   1023 C  CD  . LYS   A 1 150 ? -5.968  39.091  22.295  1   47.67 ? 135 LYS   A CD  1 
ATOM   1024 C  CE  . LYS   A 1 150 ? -6.415  39.665  23.616  1   54.67 ? 135 LYS   A CE  1 
ATOM   1025 N  NZ  . LYS   A 1 150 ? -7.911  39.758  23.719  1   58.78 ? 135 LYS   A NZ  1 
ATOM   1026 N  N   . LYS   A 1 151 ? -2.332  40.833  19.398  1   35.65 ? 136 LYS   A N   1 
ATOM   1027 C  CA  . LYS   A 1 151 ? -2.255  42.281  19.294  1   36.54 ? 136 LYS   A CA  1 
ATOM   1028 C  C   . LYS   A 1 151 ? -3.671  42.781  19.705  1   37.46 ? 136 LYS   A C   1 
ATOM   1029 O  O   . LYS   A 1 151 ? -4.67   42.201  19.268  1   37.25 ? 136 LYS   A O   1 
ATOM   1030 C  CB  . LYS   A 1 151 ? -2.036  42.691  17.824  1   37.83 ? 136 LYS   A CB  1 
ATOM   1031 C  CG  . LYS   A 1 151 ? -0.591  42.898  17.402  1   41.08 ? 136 LYS   A CG  1 
ATOM   1032 C  CD  . LYS   A 1 151 ? -0.566  43.399  15.955  1   44.31 ? 136 LYS   A CD  1 
ATOM   1033 C  CE  . LYS   A 1 151 ? 0.82    43.661  15.44   1   47.39 ? 136 LYS   A CE  1 
ATOM   1034 N  NZ  . LYS   A 1 151 ? 0.819   44.59   14.281  1   48.79 ? 136 LYS   A NZ  1 
ATOM   1035 N  N   . LYS   A 1 152 ? -3.77   43.845  20.496  1   38.7  ? 137 LYS   A N   1 
ATOM   1036 C  CA  . LYS   A 1 152 ? -5.06   44.428  20.853  1   40.69 ? 137 LYS   A CA  1 
ATOM   1037 C  C   . LYS   A 1 152 ? -5.651  45.061  19.58   1   43.21 ? 137 LYS   A C   1 
ATOM   1038 O  O   . LYS   A 1 152 ? -6.734  44.678  19.16   1   44.36 ? 137 LYS   A O   1 
ATOM   1039 C  CB  . LYS   A 1 152 ? -4.907  45.457  21.986  1   40.9  ? 137 LYS   A CB  1 
ATOM   1040 C  CG  . LYS   A 1 152 ? -4.729  44.819  23.358  1   41.42 ? 137 LYS   A CG  1 
ATOM   1041 C  CD  . LYS   A 1 152 ? -4.292  45.855  24.35   1   41.15 ? 137 LYS   A CD  1 
ATOM   1042 C  CE  . LYS   A 1 152 ? -4.121  45.327  25.74   1   43.15 ? 137 LYS   A CE  1 
ATOM   1043 N  NZ  . LYS   A 1 152 ? -3.425  46.348  26.565  1   45.54 ? 137 LYS   A NZ  1 
ATOM   1044 N  N   . ASP   A 1 153 ? -4.886  45.918  18.908  1   44.24 ? 138 ASP   A N   1 
ATOM   1045 C  CA  . ASP   A 1 153 ? -5.269  46.553  17.645  1   45.49 ? 138 ASP   A CA  1 
ATOM   1046 C  C   . ASP   A 1 153 ? -4.319  46.019  16.579  1   46.63 ? 138 ASP   A C   1 
ATOM   1047 O  O   . ASP   A 1 153 ? -3.114  46.268  16.655  1   46.83 ? 138 ASP   A O   1 
ATOM   1048 C  CB  . ASP   A 1 153 ? -5.108  48.093  17.768  1   46.96 ? 138 ASP   A CB  1 
ATOM   1049 C  CG  . ASP   A 1 153 ? -5.543  48.929  16.562  1   52.28 ? 138 ASP   A CG  1 
ATOM   1050 O  OD1 . ASP   A 1 153 ? -5.723  48.354  15.465  1   52.13 ? 138 ASP   A OD1 1 
ATOM   1051 O  OD2 . ASP   A 1 153 ? -5.68   50.161  16.714  1   55.99 ? 138 ASP   A OD2 1 
ATOM   1052 N  N   . PRO   A 1 154 ? -4.839  45.331  15.549  1   47.69 ? 139 PRO   A N   1 
ATOM   1053 C  CA  . PRO   A 1 154 ? -3.965  44.809  14.482  1   48.53 ? 139 PRO   A CA  1 
ATOM   1054 C  C   . PRO   A 1 154 ? -3.266  45.875  13.641  1   49.92 ? 139 PRO   A C   1 
ATOM   1055 O  O   . PRO   A 1 154 ? -2.284  45.574  12.961  1   49.86 ? 139 PRO   A O   1 
ATOM   1056 C  CB  . PRO   A 1 154 ? -4.916  43.968  13.62   1   48.88 ? 139 PRO   A CB  1 
ATOM   1057 C  CG  . PRO   A 1 154 ? -6.092  43.702  14.496  1   49.62 ? 139 PRO   A CG  1 
ATOM   1058 C  CD  . PRO   A 1 154 ? -6.238  44.953  15.316  1   47.87 ? 139 PRO   A CD  1 
ATOM   1059 N  N   . ASN   A 1 155 ? -3.76   47.121  13.681  1   50.62 ? 140 ASN   A N   1 
ATOM   1060 C  CA  . ASN   A 1 155 ? -3.134  48.217  12.936  1   51.29 ? 140 ASN   A CA  1 
ATOM   1061 C  C   . ASN   A 1 155 ? -2.037  48.943  13.716  1   50.84 ? 140 ASN   A C   1 
ATOM   1062 O  O   . ASN   A 1 155 ? -1.456  49.895  13.197  1   51.24 ? 140 ASN   A O   1 
ATOM   1063 C  CB  . ASN   A 1 155 ? -4.193  49.206  12.45   1   53.25 ? 140 ASN   A CB  1 
ATOM   1064 C  CG  . ASN   A 1 155 ? -5.232  48.525  11.605  1   57.48 ? 140 ASN   A CG  1 
ATOM   1065 O  OD1 . ASN   A 1 155 ? -4.927  47.995  10.528  1   59.16 ? 140 ASN   A OD1 1 
ATOM   1066 N  ND2 . ASN   A 1 155 ? -6.466  48.482  12.093  1   58.29 ? 140 ASN   A ND2 1 
ATOM   1067 N  N   . LYS   A 1 156 ? -1.744  48.506  14.951  1   49.64 ? 141 LYS   A N   1 
ATOM   1068 C  CA  . LYS   A 1 156 ? -0.699  49.121  15.753  1   48.92 ? 141 LYS   A CA  1 
ATOM   1069 C  C   . LYS   A 1 156 ? 0.519   48.162  15.914  1   47.6  ? 141 LYS   A C   1 
ATOM   1070 O  O   . LYS   A 1 156 ? 0.384   46.953  15.721  1   47.71 ? 141 LYS   A O   1 
ATOM   1071 C  CB  . LYS   A 1 156 ? -1.277  49.592  17.09   1   50.79 ? 141 LYS   A CB  1 
ATOM   1072 C  CG  . LYS   A 1 156 ? -2.346  50.666  16.919  1   54.48 ? 141 LYS   A CG  1 
ATOM   1073 C  CD  . LYS   A 1 156 ? -2.68   51.305  18.244  1   58.26 ? 141 LYS   A CD  1 
ATOM   1074 C  CE  . LYS   A 1 156 ? -3.379  52.626  18.104  1   61.49 ? 141 LYS   A CE  1 
ATOM   1075 N  NZ  . LYS   A 1 156 ? -3.413  53.338  19.408  1   63.28 ? 141 LYS   A NZ  1 
ATOM   1076 N  N   . PRO   A 1 157 ? 1.723   48.692  16.198  1   46.22 ? 142 PRO   A N   1 
ATOM   1077 C  CA  . PRO   A 1 157 ? 2.913   47.822  16.27   1   45.05 ? 142 PRO   A CA  1 
ATOM   1078 C  C   . PRO   A 1 157 ? 2.975   46.845  17.457  1   43.71 ? 142 PRO   A C   1 
ATOM   1079 O  O   . PRO   A 1 157 ? 2.146   46.879  18.364  1   43.93 ? 142 PRO   A O   1 
ATOM   1080 C  CB  . PRO   A 1 157 ? 4.072   48.826  16.296  1   45.98 ? 142 PRO   A CB  1 
ATOM   1081 C  CG  . PRO   A 1 157 ? 3.491   50.038  16.913  1   46.89 ? 142 PRO   A CG  1 
ATOM   1082 C  CD  . PRO   A 1 157 ? 2.087   50.111  16.393  1   45.61 ? 142 PRO   A CD  1 
ATOM   1083 N  N   . LEU   A 1 158 ? 3.95    45.941  17.421  1   41.87 ? 143 LEU   A N   1 
ATOM   1084 C  CA  . LEU   A 1 158 ? 4.154   44.954  18.459  1   40.31 ? 143 LEU   A CA  1 
ATOM   1085 C  C   . LEU   A 1 158 ? 4.794   45.57   19.694  1   39.27 ? 143 LEU   A C   1 
ATOM   1086 O  O   . LEU   A 1 158 ? 5.965   45.367  19.947  1   39.43 ? 143 LEU   A O   1 
ATOM   1087 C  CB  . LEU   A 1 158 ? 5.02    43.811  17.922  1   40.07 ? 143 LEU   A CB  1 
ATOM   1088 C  CG  . LEU   A 1 158 ? 4.354   42.975  16.877  1   40.89 ? 143 LEU   A CG  1 
ATOM   1089 C  CD1 . LEU   A 1 158 ? 5.381   42.243  16.044  1   41.28 ? 143 LEU   A CD1 1 
ATOM   1090 C  CD2 . LEU   A 1 158 ? 3.379   42.025  17.518  1   41.64 ? 143 LEU   A CD2 1 
ATOM   1091 N  N   . THR   A 1 159 ? 4.015   46.304  20.48   1   38.18 ? 144 THR   A N   1 
ATOM   1092 C  CA  . THR   A 1 159 ? 4.485   46.897  21.721  1   37.98 ? 144 THR   A CA  1 
ATOM   1093 C  C   . THR   A 1 159 ? 3.664   46.322  22.879  1   36.91 ? 144 THR   A C   1 
ATOM   1094 O  O   . THR   A 1 159 ? 2.525   45.884  22.671  1   36.97 ? 144 THR   A O   1 
ATOM   1095 C  CB  . THR   A 1 159 ? 4.362   48.416  21.656  1   40.98 ? 144 THR   A CB  1 
ATOM   1096 O  OG1 . THR   A 1 159 ? 2.988   48.777  21.535  1   43.18 ? 144 THR   A OG1 1 
ATOM   1097 C  CG2 . THR   A 1 159 ? 5.168   49.023  20.525  1   41.73 ? 144 THR   A CG2 1 
ATOM   1098 N  N   . TYR   A 1 160 ? 4.21    46.341  24.107  1   35.89 ? 145 TYR   A N   1 
ATOM   1099 C  CA  . TYR   A 1 160 ? 3.517   45.813  25.278  1   35.47 ? 145 TYR   A CA  1 
ATOM   1100 C  C   . TYR   A 1 160 ? 2.081   46.381  25.432  1   36.79 ? 145 TYR   A C   1 
ATOM   1101 O  O   . TYR   A 1 160 ? 1.131   45.627  25.646  1   36.64 ? 145 TYR   A O   1 
ATOM   1102 C  CB  . TYR   A 1 160 ? 4.35    46.045  26.547  1   34.53 ? 145 TYR   A CB  1 
ATOM   1103 C  CG  . TYR   A 1 160 ? 3.848   45.271  27.748  1   34.27 ? 145 TYR   A CG  1 
ATOM   1104 C  CD1 . TYR   A 1 160 ? 2.872   45.797  28.58   1   34.85 ? 145 TYR   A CD1 1 
ATOM   1105 C  CD2 . TYR   A 1 160 ? 4.369   44.016  28.064  1   34.48 ? 145 TYR   A CD2 1 
ATOM   1106 C  CE1 . TYR   A 1 160 ? 2.382   45.074  29.667  1   35.92 ? 145 TYR   A CE1 1 
ATOM   1107 C  CE2 . TYR   A 1 160 ? 3.915   43.301  29.171  1   35.34 ? 145 TYR   A CE2 1 
ATOM   1108 C  CZ  . TYR   A 1 160 ? 2.909   43.828  29.959  1   36.73 ? 145 TYR   A CZ  1 
ATOM   1109 O  OH  . TYR   A 1 160 ? 2.461   43.141  31.06   1   39.41 ? 145 TYR   A OH  1 
ATOM   1110 N  N   . GLU   A 1 161 ? 1.922   47.707  25.264  1   37.16 ? 146 GLU   A N   1 
ATOM   1111 C  CA  . GLU   A 1 161 ? 0.614   48.353  25.398  1   36.95 ? 146 GLU   A CA  1 
ATOM   1112 C  C   . GLU   A 1 161 ? -0.399  47.873  24.375  1   35.7  ? 146 GLU   A C   1 
ATOM   1113 O  O   . GLU   A 1 161 ? -1.585  47.832  24.677  1   36.45 ? 146 GLU   A O   1 
ATOM   1114 C  CB  . GLU   A 1 161 ? 0.721   49.885  25.394  1   39.68 ? 146 GLU   A CB  1 
ATOM   1115 C  CG  . GLU   A 1 161 ? 1.372   50.41   26.662  1   46.18 ? 146 GLU   A CG  1 
ATOM   1116 C  CD  . GLU   A 1 161 ? 2.867   50.156  26.719  1   52.53 ? 146 GLU   A CD  1 
ATOM   1117 O  OE1 . GLU   A 1 161 ? 3.518   50.225  25.647  1   52.58 ? 146 GLU   A OE1 1 
ATOM   1118 O  OE2 . GLU   A 1 161 ? 3.377   49.857  27.827  1   54    ? 146 GLU   A OE2 1 
ATOM   1119 N  N   . ASN   A 1 162 ? 0.062   47.47   23.197  1   34.23 ? 147 ASN   A N   1 
ATOM   1120 C  CA  . ASN   A 1 162 ? -0.822  46.959  22.171  1   33.52 ? 147 ASN   A CA  1 
ATOM   1121 C  C   . ASN   A 1 162 ? -0.88   45.431  22.159  1   32.17 ? 147 ASN   A C   1 
ATOM   1122 O  O   . ASN   A 1 162 ? -1.239  44.867  21.127  1   31.88 ? 147 ASN   A O   1 
ATOM   1123 C  CB  . ASN   A 1 162 ? -0.393  47.462  20.79   1   35.89 ? 147 ASN   A CB  1 
ATOM   1124 C  CG  . ASN   A 1 162 ? -1.44   47.166  19.755  1   41.05 ? 147 ASN   A CG  1 
ATOM   1125 O  OD1 . ASN   A 1 162 ? -2.631  47.428  19.968  1   42.22 ? 147 ASN   A OD1 1 
ATOM   1126 N  ND2 . ASN   A 1 162 ? -1.038  46.527  18.662  1   43.05 ? 147 ASN   A ND2 1 
ATOM   1127 N  N   . MET   A 1 163 ? -0.588  44.752  23.281  1   30.74 ? 148 MET   A N   1 
ATOM   1128 C  CA  . MET   A 1 163 ? -0.555  43.281  23.27   1   30.21 ? 148 MET   A CA  1 
ATOM   1129 C  C   . MET   A 1 163 ? -1.123  42.669  24.529  1   29.91 ? 148 MET   A C   1 
ATOM   1130 O  O   . MET   A 1 163 ? -1.194  43.315  25.574  1   29.81 ? 148 MET   A O   1 
ATOM   1131 C  CB  . MET   A 1 163 ? 0.922   42.787  23.088  1   30.42 ? 148 MET   A CB  1 
ATOM   1132 C  CG  . MET   A 1 163 ? 1.488   43.002  21.693  1   32.62 ? 148 MET   A CG  1 
ATOM   1133 S  SD  . MET   A 1 163 ? 3.314   42.813  21.652  1   39.54 ? 148 MET   A SD  1 
ATOM   1134 C  CE  . MET   A 1 163 ? 3.425   41.085  21.257  1   34.53 ? 148 MET   A CE  1 
ATOM   1135 N  N   . ASP   A 1 164 ? -1.492  41.397  24.435  1   30    ? 149 ASP   A N   1 
ATOM   1136 C  CA  . ASP   A 1 164 ? -1.971  40.67   25.601  1   30.66 ? 149 ASP   A CA  1 
ATOM   1137 C  C   . ASP   A 1 164 ? -1.703  39.181  25.445  1   29.9  ? 149 ASP   A C   1 
ATOM   1138 O  O   . ASP   A 1 164 ? -1.54   38.701  24.325  1   29.57 ? 149 ASP   A O   1 
ATOM   1139 C  CB  . ASP   A 1 164 ? -3.49   40.892  25.782  1   33.36 ? 149 ASP   A CB  1 
ATOM   1140 C  CG  . ASP   A 1 164 ? -3.928  41      27.232  1   41.23 ? 149 ASP   A CG  1 
ATOM   1141 O  OD1 . ASP   A 1 164 ? -3.392  40.245  28.081  1   40.07 ? 149 ASP   A OD1 1 
ATOM   1142 O  OD2 . ASP   A 1 164 ? -4.814  41.822  27.516  1   48.01 ? 149 ASP   A OD2 1 
ATOM   1143 N  N   . VAL   A 1 165 ? -1.726  38.444  26.565  1   29.42 ? 150 VAL   A N   1 
ATOM   1144 C  CA  . VAL   A 1 165 ? -1.67   36.994  26.547  1   30.42 ? 150 VAL   A CA  1 
ATOM   1145 C  C   . VAL   A 1 165 ? -3.094  36.461  26.35   1   32.83 ? 150 VAL   A C   1 
ATOM   1146 O  O   . VAL   A 1 165 ? -4.076  37.211  26.49   1   33.9  ? 150 VAL   A O   1 
ATOM   1147 C  CB  . VAL   A 1 165 ? -1.059  36.396  27.833  1   30.32 ? 150 VAL   A CB  1 
ATOM   1148 C  CG1 . VAL   A 1 165 ? 0.441   36.623  27.915  1   30.1  ? 150 VAL   A CG1 1 
ATOM   1149 C  CG2 . VAL   A 1 165 ? -1.8    36.88   29.07   1   30.93 ? 150 VAL   A CG2 1 
ATOM   1150 N  N   . LEU   A 1 166 ? -3.229  35.171  26.033  1   32.59 ? 151 LEU   A N   1 
ATOM   1151 C  CA  . LEU   A 1 166 ? -4.54   34.582  25.871  1   32.62 ? 151 LEU   A CA  1 
ATOM   1152 C  C   . LEU   A 1 166 ? -5.022  33.92   27.159  1   33.42 ? 151 LEU   A C   1 
ATOM   1153 O  O   . LEU   A 1 166 ? -6.223  33.938  27.429  1   34.27 ? 151 LEU   A O   1 
ATOM   1154 C  CB  . LEU   A 1 166 ? -4.56   33.604  24.694  1   31.86 ? 151 LEU   A CB  1 
ATOM   1155 C  CG  . LEU   A 1 166 ? -4.108  34.187  23.354  1   32.22 ? 151 LEU   A CG  1 
ATOM   1156 C  CD1 . LEU   A 1 166 ? -4.242  33.17   22.285  1   32    ? 151 LEU   A CD1 1 
ATOM   1157 C  CD2 . LEU   A 1 166 ? -4.877  35.481  22.998  1   32.38 ? 151 LEU   A CD2 1 
ATOM   1158 N  N   . PHE   A 1 167 ? -4.101  33.354  27.953  1   32.56 ? 152 PHE   A N   1 
ATOM   1159 C  CA  . PHE   A 1 167 ? -4.462  32.634  29.161  1   31.17 ? 152 PHE   A CA  1 
ATOM   1160 C  C   . PHE   A 1 167 ? -3.504  32.901  30.302  1   30.95 ? 152 PHE   A C   1 
ATOM   1161 O  O   . PHE   A 1 167 ? -2.292  33.064  30.105  1   30.83 ? 152 PHE   A O   1 
ATOM   1162 C  CB  . PHE   A 1 167 ? -4.475  31.12   28.872  1   30.98 ? 152 PHE   A CB  1 
ATOM   1163 C  CG  . PHE   A 1 167 ? -5.369  30.724  27.711  1   32.24 ? 152 PHE   A CG  1 
ATOM   1164 C  CD1 . PHE   A 1 167 ? -6.745  30.657  27.865  1   33.35 ? 152 PHE   A CD1 1 
ATOM   1165 C  CD2 . PHE   A 1 167 ? -4.836  30.48   26.458  1   32.94 ? 152 PHE   A CD2 1 
ATOM   1166 C  CE1 . PHE   A 1 167 ? -7.574  30.335  26.795  1   34.47 ? 152 PHE   A CE1 1 
ATOM   1167 C  CE2 . PHE   A 1 167 ? -5.657  30.137  25.39   1   34.16 ? 152 PHE   A CE2 1 
ATOM   1168 C  CZ  . PHE   A 1 167 ? -7.031  30.076  25.562  1   34.37 ? 152 PHE   A CZ  1 
ATOM   1169 N  N   . SER   A 1 168 ? -4.048  32.908  31.51   1   30.46 ? 153 SER   A N   1 
ATOM   1170 C  CA  . SER   A 1 168 ? -3.325  33.088  32.78   1   30.56 ? 153 SER   A CA  1 
ATOM   1171 C  C   . SER   A 1 168 ? -3.767  31.953  33.714  1   29.84 ? 153 SER   A C   1 
ATOM   1172 O  O   . SER   A 1 168 ? -4.771  31.303  33.431  1   30.9  ? 153 SER   A O   1 
ATOM   1173 C  CB  . SER   A 1 168 ? -3.74   34.415  33.418  1   32.62 ? 153 SER   A CB  1 
ATOM   1174 O  OG  . SER   A 1 168 ? -3.16   35.511  32.73   1   36.68 ? 153 SER   A OG  1 
ATOM   1175 N  N   . PHE   A 1 169 ? -3.089  31.77   34.866  1   28.85 ? 154 PHE   A N   1 
ATOM   1176 C  CA  . PHE   A 1 169 ? -3.476  30.722  35.821  1   28.86 ? 154 PHE   A CA  1 
ATOM   1177 C  C   . PHE   A 1 169 ? -4.25   31.265  37.028  1   29.02 ? 154 PHE   A C   1 
ATOM   1178 O  O   . PHE   A 1 169 ? -5.299  30.713  37.416  1   28.96 ? 154 PHE   A O   1 
ATOM   1179 C  CB  . PHE   A 1 169 ? -2.259  29.95   36.323  1   27.88 ? 154 PHE   A CB  1 
ATOM   1180 C  CG  . PHE   A 1 169 ? -1.581  29.18   35.231  1   29.14 ? 154 PHE   A CG  1 
ATOM   1181 C  CD1 . PHE   A 1 169 ? -2.071  27.952  34.822  1   30.23 ? 154 PHE   A CD1 1 
ATOM   1182 C  CD2 . PHE   A 1 169 ? -0.441  29.678  34.618  1   30.9  ? 154 PHE   A CD2 1 
ATOM   1183 C  CE1 . PHE   A 1 169 ? -1.431  27.229  33.827  1   31.29 ? 154 PHE   A CE1 1 
ATOM   1184 C  CE2 . PHE   A 1 169 ? 0.193   28.956  33.608  1   32.55 ? 154 PHE   A CE2 1 
ATOM   1185 C  CZ  . PHE   A 1 169 ? -0.321  27.743  33.213  1   31.54 ? 154 PHE   A CZ  1 
ATOM   1186 N  N   . ARG   A 1 170 ? -3.719  32.325  37.637  1   27.99 ? 155 ARG   A N   1 
ATOM   1187 C  CA  . ARG   A 1 170 ? -4.337  32.91   38.803  1   28.84 ? 155 ARG   A CA  1 
ATOM   1188 C  C   . ARG   A 1 170 ? -4.329  34.423  38.721  1   30.36 ? 155 ARG   A C   1 
ATOM   1189 O  O   . ARG   A 1 170 ? -3.486  35.02   38.049  1   28.67 ? 155 ARG   A O   1 
ATOM   1190 C  CB  . ARG   A 1 170 ? -3.614  32.498  40.082  1   29.53 ? 155 ARG   A CB  1 
ATOM   1191 C  CG  . ARG   A 1 170 ? -3.505  30.989  40.287  1   33.45 ? 155 ARG   A CG  1 
ATOM   1192 C  CD  . ARG   A 1 170 ? -4.847  30.324  40.604  1   34.15 ? 155 ARG   A CD  1 
ATOM   1193 N  NE  . ARG   A 1 170 ? -5.467  30.935  41.771  1   33.59 ? 155 ARG   A NE  1 
ATOM   1194 C  CZ  . ARG   A 1 170 ? -5.337  30.486  43.014  1   36.08 ? 155 ARG   A CZ  1 
ATOM   1195 N  NH1 . ARG   A 1 170 ? -4.657  29.375  43.259  1   33.08 ? 155 ARG   A NH1 1 
ATOM   1196 N  NH2 . ARG   A 1 170 ? -5.921  31.123  44.017  1   38.71 ? 155 ARG   A NH2 1 
ATOM   1197 N  N   . ASP   A 1 171 ? -5.266  35.056  39.432  1   31.54 ? 156 ASP   A N   1 
ATOM   1198 C  CA  A ASP   A 1 171 ? -5.314  36.513  39.467  0.5 32.58 ? 156 ASP   A CA  1 
ATOM   1199 C  CA  B ASP   A 1 171 ? -5.364  36.507  39.516  0.5 32.34 ? 156 ASP   A CA  1 
ATOM   1200 C  C   . ASP   A 1 171 ? -4.076  37.003  40.203  1   32.53 ? 156 ASP   A C   1 
ATOM   1201 O  O   . ASP   A 1 171 ? -3.692  36.447  41.24   1   32.25 ? 156 ASP   A O   1 
ATOM   1202 C  CB  A ASP   A 1 171 ? -6.607  37.005  40.112  0.5 34.61 ? 156 ASP   A CB  1 
ATOM   1203 C  CB  B ASP   A 1 171 ? -6.592  36.859  40.374  0.5 33.66 ? 156 ASP   A CB  1 
ATOM   1204 C  CG  A ASP   A 1 171 ? -7.792  36.62   39.267  0.5 39.39 ? 156 ASP   A CG  1 
ATOM   1205 C  CG  B ASP   A 1 171 ? -7.009  38.305  40.322  0.5 36.81 ? 156 ASP   A CG  1 
ATOM   1206 O  OD1 A ASP   A 1 171 ? -7.766  36.91   38.041  0.5 38.65 ? 156 ASP   A OD1 1 
ATOM   1207 O  OD1 B ASP   A 1 171 ? -6.859  38.925  39.25   0.5 38.14 ? 156 ASP   A OD1 1 
ATOM   1208 O  OD2 A ASP   A 1 171 ? -8.741  36.002  39.818  0.5 43.23 ? 156 ASP   A OD2 1 
ATOM   1209 O  OD2 B ASP   A 1 171 ? -7.508  38.81   41.342  0.5 37.97 ? 156 ASP   A OD2 1 
ATOM   1210 N  N   . GLY   A 1 172 ? -3.413  37.973  39.604  1   32.41 ? 157 GLY   A N   1 
ATOM   1211 C  CA  . GLY   A 1 172 ? -2.176  38.53   40.149  1   32.85 ? 157 GLY   A CA  1 
ATOM   1212 C  C   . GLY   A 1 172 ? -0.95   37.652  39.956  1   32.56 ? 157 GLY   A C   1 
ATOM   1213 O  O   . GLY   A 1 172 ? 0.055   37.883  40.615  1   34.3  ? 157 GLY   A O   1 
ATOM   1214 N  N   . ASP   A 1 173 ? -0.988  36.655  39.035  1   30.48 ? 158 ASP   A N   1 
ATOM   1215 C  CA  . ASP   A 1 173 ? 0.158   35.765  38.842  1   29.46 ? 158 ASP   A CA  1 
ATOM   1216 C  C   . ASP   A 1 173 ? 1.279   36.36   37.958  1   30.12 ? 158 ASP   A C   1 
ATOM   1217 O  O   . ASP   A 1 173 ? 2.321   35.726  37.812  1   30.72 ? 158 ASP   A O   1 
ATOM   1218 C  CB  . ASP   A 1 173 ? -0.291  34.376  38.316  1   28.13 ? 158 ASP   A CB  1 
ATOM   1219 C  CG  . ASP   A 1 173 ? -0.797  34.378  36.877  1   29.35 ? 158 ASP   A CG  1 
ATOM   1220 O  OD1 . ASP   A 1 173 ? -0.825  35.461  36.26   1   28.42 ? 158 ASP   A OD1 1 
ATOM   1221 O  OD2 . ASP   A 1 173 ? -1.203  33.306  36.387  1   28.71 ? 158 ASP   A OD2 1 
ATOM   1222 N  N   . CYS   A 1 174 ? 1.039   37.501  37.307  1   29.62 ? 159 CYS   A N   1 
ATOM   1223 C  CA  . CYS   A 1 174 ? 2.052   38.157  36.448  1   30.67 ? 159 CYS   A CA  1 
ATOM   1224 C  C   . CYS   A 1 174 ? 2.389   37.379  35.176  1   29.73 ? 159 CYS   A C   1 
ATOM   1225 O  O   . CYS   A 1 174 ? 3.411   37.658  34.545  1   28.92 ? 159 CYS   A O   1 
ATOM   1226 C  CB  . CYS   A 1 174 ? 3.308   38.508  37.233  1   32.3  ? 159 CYS   A CB  1 
ATOM   1227 S  SG  . CYS   A 1 174 ? 3.022   39.718  38.558  1   37.29 ? 159 CYS   A SG  1 
ATOM   1228 N  N   . SER   A 1 175 ? 1.509   36.454  34.773  1   29.17 ? 160 SER   A N   1 
ATOM   1229 C  CA  . SER   A 1 175 ? 1.753   35.677  33.569  1   29.13 ? 160 SER   A CA  1 
ATOM   1230 C  C   . SER   A 1 175 ? 1.737   36.568  32.336  1   29.03 ? 160 SER   A C   1 
ATOM   1231 O  O   . SER   A 1 175 ? 2.488   36.287  31.418  1   30.06 ? 160 SER   A O   1 
ATOM   1232 C  CB  . SER   A 1 175 ? 0.749   34.539  33.431  1   29.48 ? 160 SER   A CB  1 
ATOM   1233 O  OG  . SER   A 1 175 ? -0.57   34.952  33.749  1   30    ? 160 SER   A OG  1 
ATOM   1234 N  N   . LYS   A 1 176 ? 0.955   37.672  32.321  1   27.3  ? 161 LYS   A N   1 
ATOM   1235 C  CA  . LYS   A 1 176 ? 0.965   38.573  31.166  1   26.54 ? 161 LYS   A CA  1 
ATOM   1236 C  C   . LYS   A 1 176 ? 2.369   39.21   31.041  1   25.93 ? 161 LYS   A C   1 
ATOM   1237 O  O   . LYS   A 1 176 ? 2.961   39.176  29.977  1   26.21 ? 161 LYS   A O   1 
ATOM   1238 C  CB  . LYS   A 1 176 ? -0.094  39.7    31.29   1   28.07 ? 161 LYS   A CB  1 
ATOM   1239 C  CG  . LYS   A 1 176 ? -0.092  40.626  30.061  1   30.69 ? 161 LYS   A CG  1 
ATOM   1240 C  CD  . LYS   A 1 176 ? -1.021  41.817  30.199  1   35.25 ? 161 LYS   A CD  1 
ATOM   1241 C  CE  . LYS   A 1 176 ? -0.938  42.741  29.008  1   39.56 ? 161 LYS   A CE  1 
ATOM   1242 N  NZ  . LYS   A 1 176 ? -1.793  43.948  29.207  1   41.35 ? 161 LYS   A NZ  1 
ATOM   1243 N  N   . GLY   A 1 177 ? 2.907   39.713  32.148  1   24.87 ? 162 GLY   A N   1 
ATOM   1244 C  CA  . GLY   A 1 177 ? 4.205   40.356  32.139  1   25.76 ? 162 GLY   A CA  1 
ATOM   1245 C  C   . GLY   A 1 177 ? 5.32    39.401  31.776  1   27.63 ? 162 GLY   A C   1 
ATOM   1246 O  O   . GLY   A 1 177 ? 6.117   39.676  30.887  1   28.38 ? 162 GLY   A O   1 
ATOM   1247 N  N   . PHE   A 1 178 ? 5.321   38.237  32.398  1   27.38 ? 163 PHE   A N   1 
ATOM   1248 C  CA  . PHE   A 1 178 ? 6.35    37.236  32.165  1   27.03 ? 163 PHE   A CA  1 
ATOM   1249 C  C   . PHE   A 1 178 ? 6.34    36.677  30.741  1   26.01 ? 163 PHE   A C   1 
ATOM   1250 O  O   . PHE   A 1 178 ? 7.396   36.649  30.089  1   25.39 ? 163 PHE   A O   1 
ATOM   1251 C  CB  . PHE   A 1 178 ? 6.228   36.123  33.204  1   26.46 ? 163 PHE   A CB  1 
ATOM   1252 C  CG  . PHE   A 1 178 ? 7.269   35.035  33.138  1   26.11 ? 163 PHE   A CG  1 
ATOM   1253 C  CD1 . PHE   A 1 178 ? 8.607   35.312  33.404  1   26.65 ? 163 PHE   A CD1 1 
ATOM   1254 C  CD2 . PHE   A 1 178 ? 6.903   33.72   32.911  1   26.22 ? 163 PHE   A CD2 1 
ATOM   1255 C  CE1 . PHE   A 1 178 ? 9.568   34.302  33.383  1   27.06 ? 163 PHE   A CE1 1 
ATOM   1256 C  CE2 . PHE   A 1 178 ? 7.847   32.702  32.959  1   26.34 ? 163 PHE   A CE2 1 
ATOM   1257 C  CZ  . PHE   A 1 178 ? 9.177   32.997  33.182  1   25.71 ? 163 PHE   A CZ  1 
ATOM   1258 N  N   . PHE   A 1 179 ? 5.172   36.237  30.262  1   25.07 ? 164 PHE   A N   1 
ATOM   1259 C  CA  . PHE   A 1 179 ? 5.088   35.639  28.943  1   25.08 ? 164 PHE   A CA  1 
ATOM   1260 C  C   . PHE   A 1 179 ? 5.295   36.676  27.88   1   26.57 ? 164 PHE   A C   1 
ATOM   1261 O  O   . PHE   A 1 179 ? 5.97    36.39   26.892  1   27.57 ? 164 PHE   A O   1 
ATOM   1262 C  CB  . PHE   A 1 179 ? 3.757   34.903  28.747  1   25.51 ? 164 PHE   A CB  1 
ATOM   1263 C  CG  . PHE   A 1 179 ? 3.543   33.726  29.686  1   25.8  ? 164 PHE   A CG  1 
ATOM   1264 C  CD1 . PHE   A 1 179 ? 4.601   32.93   30.071  1   26.03 ? 164 PHE   A CD1 1 
ATOM   1265 C  CD2 . PHE   A 1 179 ? 2.269   33.37   30.099  1   26.87 ? 164 PHE   A CD2 1 
ATOM   1266 C  CE1 . PHE   A 1 179 ? 4.386   31.812  30.894  1   27.15 ? 164 PHE   A CE1 1 
ATOM   1267 C  CE2 . PHE   A 1 179 ? 2.067   32.267  30.929  1   27.14 ? 164 PHE   A CE2 1 
ATOM   1268 C  CZ  . PHE   A 1 179 ? 3.128   31.526  31.345  1   26.67 ? 164 PHE   A CZ  1 
ATOM   1269 N  N   . LEU   A 1 180 ? 4.738   37.888  28.059  1   27.23 ? 165 LEU   A N   1 
ATOM   1270 C  CA  . LEU   A 1 180 ? 4.875   38.931  27.029  1   28.31 ? 165 LEU   A CA  1 
ATOM   1271 C  C   . LEU   A 1 180 ? 6.29    39.496  26.931  1   27.32 ? 165 LEU   A C   1 
ATOM   1272 O  O   . LEU   A 1 180 ? 6.712   39.819  25.833  1   27.25 ? 165 LEU   A O   1 
ATOM   1273 C  CB  . LEU   A 1 180 ? 3.86    40.056  27.253  1   30.73 ? 165 LEU   A CB  1 
ATOM   1274 C  CG  . LEU   A 1 180 ? 2.616   40.15   26.344  1   34.19 ? 165 LEU   A CG  1 
ATOM   1275 C  CD1 . LEU   A 1 180 ? 2.137   38.846  25.755  1   34.95 ? 165 LEU   A CD1 1 
ATOM   1276 C  CD2 . LEU   A 1 180 ? 1.569   41.095  26.874  1   35.24 ? 165 LEU   A CD2 1 
ATOM   1277 N  N   . VAL   A 1 181 ? 6.999   39.652  28.058  1   26.36 ? 166 VAL   A N   1 
ATOM   1278 C  CA  . VAL   A 1 181 ? 8.371   40.165  27.988  1   26.61 ? 166 VAL   A CA  1 
ATOM   1279 C  C   . VAL   A 1 181 ? 9.281   39.102  27.332  1   26.07 ? 166 VAL   A C   1 
ATOM   1280 O  O   . VAL   A 1 181 ? 10.086  39.441  26.469  1   27.4  ? 166 VAL   A O   1 
ATOM   1281 C  CB  . VAL   A 1 181 ? 8.895   40.74   29.314  1   27.91 ? 166 VAL   A CB  1 
ATOM   1282 C  CG1 . VAL   A 1 181 ? 10.376  41.1    29.191  1   28.91 ? 166 VAL   A CG1 1 
ATOM   1283 C  CG2 . VAL   A 1 181 ? 8.082   41.966  29.705  1   28.54 ? 166 VAL   A CG2 1 
ATOM   1284 N  N   . SER   A 1 182 ? 9.038   37.795  27.587  1   24.57 ? 167 SER   A N   1 
ATOM   1285 C  CA  . SER   A 1 182 ? 9.778   36.73   26.912  1   25.42 ? 167 SER   A CA  1 
ATOM   1286 C  C   . SER   A 1 182 ? 9.507   36.806  25.402  1   25.91 ? 167 SER   A C   1 
ATOM   1287 O  O   . SER   A 1 182 ? 10.449  36.725  24.604  1   26.27 ? 167 SER   A O   1 
ATOM   1288 C  CB  . SER   A 1 182 ? 9.352   35.363  27.446  1   26.78 ? 167 SER   A CB  1 
ATOM   1289 O  OG  . SER   A 1 182 ? 9.781   35.194  28.786  1   28.2  ? 167 SER   A OG  1 
ATOM   1290 N  N   . LEU   A 1 183 ? 8.234   37.01   25.029  1   26.64 ? 168 LEU   A N   1 
ATOM   1291 C  CA  . LEU   A 1 183 ? 7.819   37.113  23.645  1   27.54 ? 168 LEU   A CA  1 
ATOM   1292 C  C   . LEU   A 1 183 ? 8.458   38.323  22.969  1   27.27 ? 168 LEU   A C   1 
ATOM   1293 O  O   . LEU   A 1 183 ? 8.885   38.224  21.824  1   27.27 ? 168 LEU   A O   1 
ATOM   1294 C  CB  . LEU   A 1 183 ? 6.286   37.221  23.576  1   28.35 ? 168 LEU   A CB  1 
ATOM   1295 C  CG  . LEU   A 1 183 ? 5.716   37.389  22.195  1   30.21 ? 168 LEU   A CG  1 
ATOM   1296 C  CD1 . LEU   A 1 183 ? 5.93    36.131  21.374  1   30.45 ? 168 LEU   A CD1 1 
ATOM   1297 C  CD2 . LEU   A 1 183 ? 4.261   37.822  22.27   1   30.79 ? 168 LEU   A CD2 1 
ATOM   1298 N  N   . LEU   A 1 184 ? 8.488   39.475  23.643  1   26.74 ? 169 LEU   A N   1 
ATOM   1299 C  CA  . LEU   A 1 184 ? 9.066   40.688  23.082  1   26.67 ? 169 LEU   A CA  1 
ATOM   1300 C  C   . LEU   A 1 184 ? 10.584  40.546  22.847  1   26.7  ? 169 LEU   A C   1 
ATOM   1301 O  O   . LEU   A 1 184 ? 11.114  41.171  21.934  1   27.41 ? 169 LEU   A O   1 
ATOM   1302 C  CB  . LEU   A 1 184 ? 8.735   41.896  23.988  1   26.96 ? 169 LEU   A CB  1 
ATOM   1303 C  CG  . LEU   A 1 184 ? 7.257   42.39   23.854  1   28.31 ? 169 LEU   A CG  1 
ATOM   1304 C  CD1 . LEU   A 1 184 ? 6.857   43.286  25.014  1   29.56 ? 169 LEU   A CD1 1 
ATOM   1305 C  CD2 . LEU   A 1 184 ? 7.022   43.097  22.52   1   28.77 ? 169 LEU   A CD2 1 
ATOM   1306 N  N   . VAL   A 1 185 ? 11.278  39.727  23.648  1   26.23 ? 170 VAL   A N   1 
ATOM   1307 C  CA  . VAL   A 1 185 ? 12.705  39.429  23.438  1   27.24 ? 170 VAL   A CA  1 
ATOM   1308 C  C   . VAL   A 1 185 ? 12.835  38.508  22.201  1   29.32 ? 170 VAL   A C   1 
ATOM   1309 O  O   . VAL   A 1 185 ? 13.669  38.702  21.335  1   30    ? 170 VAL   A O   1 
ATOM   1310 C  CB  . VAL   A 1 185 ? 13.314  38.773  24.679  1   27.08 ? 170 VAL   A CB  1 
ATOM   1311 C  CG1 . VAL   A 1 185 ? 14.728  38.263  24.381  1   28.51 ? 170 VAL   A CG1 1 
ATOM   1312 C  CG2 . VAL   A 1 185 ? 13.337  39.775  25.836  1   26.17 ? 170 VAL   A CG2 1 
ATOM   1313 N  N   . GLU   A 1 186 ? 11.938  37.56   22.096  1   29.73 ? 171 GLU   A N   1 
ATOM   1314 C  CA  . GLU   A 1 186 ? 11.832  36.616  20.997  1   30.45 ? 171 GLU   A CA  1 
ATOM   1315 C  C   . GLU   A 1 186 ? 11.631  37.422  19.662  1   32.14 ? 171 GLU   A C   1 
ATOM   1316 O  O   . GLU   A 1 186 ? 12.305  37.155  18.655  1   32.89 ? 171 GLU   A O   1 
ATOM   1317 C  CB  . GLU   A 1 186 ? 10.624  35.756  21.358  1   30.84 ? 171 GLU   A CB  1 
ATOM   1318 C  CG  . GLU   A 1 186 ? 10.532  34.381  20.782  1   34.55 ? 171 GLU   A CG  1 
ATOM   1319 C  CD  . GLU   A 1 186 ? 11.577  33.334  21.081  1   34.95 ? 171 GLU   A CD  1 
ATOM   1320 O  OE1 . GLU   A 1 186 ? 11.757  32.931  22.255  1   32.88 ? 171 GLU   A OE1 1 
ATOM   1321 O  OE2 . GLU   A 1 186 ? 12.142  32.828  20.09   1   36.4  ? 171 GLU   A OE2 1 
ATOM   1322 N  N   . ILE   A 1 187 ? 10.815  38.486  19.712  1   32.25 ? 172 ILE   A N   1 
ATOM   1323 C  CA  . ILE   A 1 187 ? 10.537  39.35   18.559  1   33.36 ? 172 ILE   A CA  1 
ATOM   1324 C  C   . ILE   A 1 187 ? 11.759  40.247  18.231  1   33.14 ? 172 ILE   A C   1 
ATOM   1325 O  O   . ILE   A 1 187 ? 12.11   40.423  17.06   1   33.92 ? 172 ILE   A O   1 
ATOM   1326 C  CB  . ILE   A 1 187 ? 9.268   40.172  18.817  1   33.96 ? 172 ILE   A CB  1 
ATOM   1327 C  CG1 . ILE   A 1 187 ? 8.027   39.264  18.806  1   34.38 ? 172 ILE   A CG1 1 
ATOM   1328 C  CG2 . ILE   A 1 187 ? 9.117   41.297  17.788  1   34.84 ? 172 ILE   A CG2 1 
ATOM   1329 C  CD1 . ILE   A 1 187 ? 6.807   39.948  19.399  1   35.62 ? 172 ILE   A CD1 1 
ATOM   1330 N  N   . ALA   A 1 188 ? 12.408  40.798  19.265  1   31.67 ? 173 ALA   A N   1 
ATOM   1331 C  CA  . ALA   A 1 188 ? 13.628  41.6    19.082  1   31.82 ? 173 ALA   A CA  1 
ATOM   1332 C  C   . ALA   A 1 188 ? 14.726  40.731  18.426  1   31.99 ? 173 ALA   A C   1 
ATOM   1333 O  O   . ALA   A 1 188 ? 15.44   41.212  17.54   1   32.55 ? 173 ALA   A O   1 
ATOM   1334 C  CB  . ALA   A 1 188 ? 14.102  42.11   20.427  1   32.14 ? 173 ALA   A CB  1 
ATOM   1335 N  N   . ALA   A 1 189 ? 14.796  39.436  18.781  1   31.43 ? 174 ALA   A N   1 
ATOM   1336 C  CA  . ALA   A 1 189 ? 15.766  38.537  18.176  1   32.21 ? 174 ALA   A CA  1 
ATOM   1337 C  C   . ALA   A 1 189 ? 15.502  38.225  16.714  1   33.34 ? 174 ALA   A C   1 
ATOM   1338 O  O   . ALA   A 1 189 ? 16.434  37.823  16.021  1   34.23 ? 174 ALA   A O   1 
ATOM   1339 C  CB  . ALA   A 1 189 ? 15.861  37.251  18.955  1   31.77 ? 174 ALA   A CB  1 
ATOM   1340 N  N   . ALA   A 1 190 ? 14.269  38.407  16.239  1   33.35 ? 175 ALA   A N   1 
ATOM   1341 C  CA  . ALA   A 1 190 ? 13.896  38.105  14.849  1   33.45 ? 175 ALA   A CA  1 
ATOM   1342 C  C   . ALA   A 1 190 ? 14.703  38.87   13.846  1   33.71 ? 175 ALA   A C   1 
ATOM   1343 O  O   . ALA   A 1 190 ? 14.977  38.343  12.766  1   35.52 ? 175 ALA   A O   1 
ATOM   1344 C  CB  . ALA   A 1 190 ? 12.429  38.397  14.622  1   33.15 ? 175 ALA   A CB  1 
ATOM   1345 N  N   . SER   A 1 191 ? 15.043  40.132  14.155  1   32.48 ? 176 SER   A N   1 
ATOM   1346 C  CA  . SER   A 1 191 ? 15.845  40.926  13.22   1   33.14 ? 176 SER   A CA  1 
ATOM   1347 C  C   . SER   A 1 191 ? 17.288  40.378  13.084  1   33.87 ? 176 SER   A C   1 
ATOM   1348 O  O   . SER   A 1 191 ? 17.936  40.607  12.073  1   33.9  ? 176 SER   A O   1 
ATOM   1349 C  CB  . SER   A 1 191 ? 15.832  42.403  13.598  1   34.36 ? 176 SER   A CB  1 
ATOM   1350 O  OG  . SER   A 1 191 ? 16.144  42.57   14.973  1   37.63 ? 176 SER   A OG  1 
ATOM   1351 N  N   . ALA   A 1 192 ? 17.758  39.604  14.081  1   33.38 ? 177 ALA   A N   1 
ATOM   1352 C  CA  . ALA   A 1 192 ? 19.07   38.978  14.038  1   33.65 ? 177 ALA   A CA  1 
ATOM   1353 C  C   . ALA   A 1 192 ? 18.974  37.61   13.35   1   34.37 ? 177 ALA   A C   1 
ATOM   1354 O  O   . ALA   A 1 192 ? 19.839  37.272  12.544  1   34.44 ? 177 ALA   A O   1 
ATOM   1355 C  CB  . ALA   A 1 192 ? 19.628  38.826  15.448  1   32.82 ? 177 ALA   A CB  1 
ATOM   1356 N  N   . ILE   A 1 193 ? 17.897  36.847  13.611  1   34.81 ? 178 ILE   A N   1 
ATOM   1357 C  CA  . ILE   A 1 193 ? 17.701  35.513  13.002  1   36.8  ? 178 ILE   A CA  1 
ATOM   1358 C  C   . ILE   A 1 193 ? 17.704  35.604  11.491  1   37.11 ? 178 ILE   A C   1 
ATOM   1359 O  O   . ILE   A 1 193 ? 18.248  34.732  10.815  1   37.16 ? 178 ILE   A O   1 
ATOM   1360 C  CB  . ILE   A 1 193 ? 16.338  34.858  13.432  1   38.76 ? 178 ILE   A CB  1 
ATOM   1361 C  CG1 . ILE   A 1 193 ? 16.02   35.076  14.943  1   41.93 ? 178 ILE   A CG1 1 
ATOM   1362 C  CG2 . ILE   A 1 193 ? 16.247  33.383  13.01   1   38.66 ? 178 ILE   A CG2 1 
ATOM   1363 C  CD1 . ILE   A 1 193 ? 16.599  34.232  15.873  1   44.55 ? 178 ILE   A CD1 1 
ATOM   1364 N  N   . LYS   A 1 194 ? 17.043  36.642  10.948  1   37.79 ? 179 LYS   A N   1 
ATOM   1365 C  CA  . LYS   A 1 194 ? 16.913  36.765  9.497   1   38.17 ? 179 LYS   A CA  1 
ATOM   1366 C  C   . LYS   A 1 194 ? 18.254  36.989  8.772   1   37.86 ? 179 LYS   A C   1 
ATOM   1367 O  O   . LYS   A 1 194 ? 18.333  36.772  7.566   1   38.19 ? 179 LYS   A O   1 
ATOM   1368 C  CB  . LYS   A 1 194 ? 15.873  37.831  9.119   1   39.78 ? 179 LYS   A CB  1 
ATOM   1369 C  CG  . LYS   A 1 194 ? 16.29   39.252  9.4     1   43.91 ? 179 LYS   A CG  1 
ATOM   1370 C  CD  . LYS   A 1 194 ? 15.153  40.197  9.05    1   48.33 ? 179 LYS   A CD  1 
ATOM   1371 C  CE  . LYS   A 1 194 ? 15.445  41.624  9.443   1   52.34 ? 179 LYS   A CE  1 
ATOM   1372 N  NZ  . LYS   A 1 194 ? 14.199  42.44   9.525   1   53.57 ? 179 LYS   A NZ  1 
ATOM   1373 N  N   . VAL   A 1 195 ? 19.313  37.374  9.507   1   36.82 ? 180 VAL   A N   1 
ATOM   1374 C  CA  . VAL   A 1 195 ? 20.634  37.577  8.924   1   36.58 ? 180 VAL   A CA  1 
ATOM   1375 C  C   . VAL   A 1 195 ? 21.42   36.249  8.837   1   37.87 ? 180 VAL   A C   1 
ATOM   1376 O  O   . VAL   A 1 195 ? 22.357  36.163  8.053   1   38.96 ? 180 VAL   A O   1 
ATOM   1377 C  CB  . VAL   A 1 195 ? 21.394  38.687  9.704   1   36.27 ? 180 VAL   A CB  1 
ATOM   1378 C  CG1 . VAL   A 1 195 ? 22.797  38.931  9.158   1   36.54 ? 180 VAL   A CG1 1 
ATOM   1379 C  CG2 . VAL   A 1 195 ? 20.588  39.981  9.743   1   36.58 ? 180 VAL   A CG2 1 
ATOM   1380 N  N   . ILE   A 1 196 ? 20.992  35.171  9.556   1   37.73 ? 181 ILE   A N   1 
ATOM   1381 C  CA  . ILE   A 1 196 ? 21.686  33.885  9.54    1   38    ? 181 ILE   A CA  1 
ATOM   1382 C  C   . ILE   A 1 196 ? 22.008  33.398  8.107   1   39.41 ? 181 ILE   A C   1 
ATOM   1383 O  O   . ILE   A 1 196 ? 23.189  33.18   7.855   1   39.89 ? 181 ILE   A O   1 
ATOM   1384 C  CB  . ILE   A 1 196 ? 20.968  32.818  10.401  1   37.69 ? 181 ILE   A CB  1 
ATOM   1385 C  CG1 . ILE   A 1 196 ? 21.098  33.171  11.899  1   38.55 ? 181 ILE   A CG1 1 
ATOM   1386 C  CG2 . ILE   A 1 196 ? 21.475  31.398  10.116  1   37.24 ? 181 ILE   A CG2 1 
ATOM   1387 C  CD1 . ILE   A 1 196 ? 20.355  32.231  12.854  1   38.58 ? 181 ILE   A CD1 1 
ATOM   1388 N  N   . PRO   A 1 197 ? 21.068  33.366  7.135   1   40.58 ? 182 PRO   A N   1 
ATOM   1389 C  CA  . PRO   A 1 197 ? 21.447  32.908  5.78    1   41.21 ? 182 PRO   A CA  1 
ATOM   1390 C  C   . PRO   A 1 197 ? 22.531  33.752  5.098   1   41.21 ? 182 PRO   A C   1 
ATOM   1391 O  O   . PRO   A 1 197 ? 23.291  33.215  4.305   1   41.14 ? 182 PRO   A O   1 
ATOM   1392 C  CB  . PRO   A 1 197 ? 20.126  32.939  4.996   1   42.3  ? 182 PRO   A CB  1 
ATOM   1393 C  CG  . PRO   A 1 197 ? 19.172  33.741  5.822   1   42.65 ? 182 PRO   A CG  1 
ATOM   1394 C  CD  . PRO   A 1 197 ? 19.609  33.604  7.235   1   40.73 ? 182 PRO   A CD  1 
ATOM   1395 N  N   . THR   A 1 198 ? 22.57   35.065  5.368   1   41.23 ? 183 THR   A N   1 
ATOM   1396 C  CA  . THR   A 1 198 ? 23.591  35.963  4.814   1   41.03 ? 183 THR   A CA  1 
ATOM   1397 C  C   . THR   A 1 198 ? 24.979  35.548  5.318   1   39.87 ? 183 THR   A C   1 
ATOM   1398 O  O   . THR   A 1 198 ? 25.941  35.577  4.558   1   40.22 ? 183 THR   A O   1 
ATOM   1399 C  CB  . THR   A 1 198 ? 23.274  37.424  5.191   1   42.76 ? 183 THR   A CB  1 
ATOM   1400 O  OG1 . THR   A 1 198 ? 22.001  37.771  4.662   1   43.45 ? 183 THR   A OG1 1 
ATOM   1401 C  CG2 . THR   A 1 198 ? 24.322  38.406  4.675   1   43.13 ? 183 THR   A CG2 1 
ATOM   1402 N  N   . VAL   A 1 199 ? 25.079  35.142  6.585   1   38.25 ? 184 VAL   A N   1 
ATOM   1403 C  CA  . VAL   A 1 199 ? 26.326  34.675  7.177   1   37.82 ? 184 VAL   A CA  1 
ATOM   1404 C  C   . VAL   A 1 199 ? 26.836  33.434  6.445   1   38.22 ? 184 VAL   A C   1 
ATOM   1405 O  O   . VAL   A 1 199 ? 27.995  33.415  6.037   1   37.87 ? 184 VAL   A O   1 
ATOM   1406 C  CB  . VAL   A 1 199 ? 26.13   34.412  8.694   1   37.48 ? 184 VAL   A CB  1 
ATOM   1407 C  CG1 . VAL   A 1 199 ? 27.265  33.577  9.278   1   37.57 ? 184 VAL   A CG1 1 
ATOM   1408 C  CG2 . VAL   A 1 199 ? 25.946  35.718  9.453   1   37.6  ? 184 VAL   A CG2 1 
ATOM   1409 N  N   . PHE   A 1 200 ? 25.987  32.412  6.265   1   38.63 ? 185 PHE   A N   1 
ATOM   1410 C  CA  . PHE   A 1 200 ? 26.392  31.181  5.587   1   39.7  ? 185 PHE   A CA  1 
ATOM   1411 C  C   . PHE   A 1 200 ? 26.691  31.387  4.122   1   40.78 ? 185 PHE   A C   1 
ATOM   1412 O  O   . PHE   A 1 200 ? 27.599  30.743  3.606   1   41.44 ? 185 PHE   A O   1 
ATOM   1413 C  CB  . PHE   A 1 200 ? 25.367  30.035  5.798   1   39.83 ? 185 PHE   A CB  1 
ATOM   1414 C  CG  . PHE   A 1 200 ? 25.419  29.511  7.213   1   40.26 ? 185 PHE   A CG  1 
ATOM   1415 C  CD1 . PHE   A 1 200 ? 26.519  28.814  7.668   1   41.01 ? 185 PHE   A CD1 1 
ATOM   1416 C  CD2 . PHE   A 1 200 ? 24.415  29.797  8.108   1   40.86 ? 185 PHE   A CD2 1 
ATOM   1417 C  CE1 . PHE   A 1 200 ? 26.605  28.4    8.994   1   41.74 ? 185 PHE   A CE1 1 
ATOM   1418 C  CE2 . PHE   A 1 200 ? 24.489  29.355  9.423   1   41.51 ? 185 PHE   A CE2 1 
ATOM   1419 C  CZ  . PHE   A 1 200 ? 25.581  28.659  9.858   1   41.49 ? 185 PHE   A CZ  1 
ATOM   1420 N  N   . LYS   A 1 201 ? 25.957  32.275  3.457   1   41.34 ? 186 LYS   A N   1 
ATOM   1421 C  CA  . LYS   A 1 201 ? 26.211  32.521  2.044   1   42.97 ? 186 LYS   A CA  1 
ATOM   1422 C  C   . LYS   A 1 201 ? 27.538  33.253  1.853   1   43.34 ? 186 LYS   A C   1 
ATOM   1423 O  O   . LYS   A 1 201 ? 28.293  32.891  0.949   1   43.59 ? 186 LYS   A O   1 
ATOM   1424 C  CB  . LYS   A 1 201 ? 25.053  33.226  1.339   1   45.83 ? 186 LYS   A CB  1 
ATOM   1425 C  CG  . LYS   A 1 201 ? 24.837  32.695  -0.084  1   51.39 ? 186 LYS   A CG  1 
ATOM   1426 C  CD  . LYS   A 1 201 ? 24.507  31.179  -0.144  1   55.77 ? 186 LYS   A CD  1 
ATOM   1427 N  N   . ALA   A 1 202 ? 27.867  34.207  2.745   1   42.94 ? 187 ALA   A N   1 
ATOM   1428 C  CA  . ALA   A 1 202 ? 29.152  34.928  2.679   1   43.4  ? 187 ALA   A CA  1 
ATOM   1429 C  C   . ALA   A 1 202 ? 30.332  33.983  2.883   1   43.84 ? 187 ALA   A C   1 
ATOM   1430 O  O   . ALA   A 1 202 ? 31.358  34.12   2.209   1   44.13 ? 187 ALA   A O   1 
ATOM   1431 C  CB  . ALA   A 1 202 ? 29.201  36.035  3.712   1   43.36 ? 187 ALA   A CB  1 
ATOM   1432 N  N   . MET   A 1 203 ? 30.186  33.01   3.777   1   43.57 ? 188 MET   A N   1 
ATOM   1433 C  CA  . MET   A 1 203 ? 31.236  32.033  4.014   1   44.6  ? 188 MET   A CA  1 
ATOM   1434 C  C   . MET   A 1 203 ? 31.44   31.112  2.814   1   46.36 ? 188 MET   A C   1 
ATOM   1435 O  O   . MET   A 1 203 ? 32.582  30.813  2.457   1   46.34 ? 188 MET   A O   1 
ATOM   1436 C  CB  . MET   A 1 203 ? 30.923  31.197  5.229   1   44.64 ? 188 MET   A CB  1 
ATOM   1437 C  CG  . MET   A 1 203 ? 31.254  31.86   6.503   1   47.55 ? 188 MET   A CG  1 
ATOM   1438 S  SD  . MET   A 1 203 ? 30.743  30.779  7.848   1   57.63 ? 188 MET   A SD  1 
ATOM   1439 C  CE  . MET   A 1 203 ? 31.657  29.275  7.48    1   53.66 ? 188 MET   A CE  1 
ATOM   1440 N  N   . GLN   A 1 204 ? 30.346  30.651  2.208   1   47.68 ? 189 GLN   A N   1 
ATOM   1441 C  CA  . GLN   A 1 204 ? 30.428  29.754  1.058   1   49.36 ? 189 GLN   A CA  1 
ATOM   1442 C  C   . GLN   A 1 204 ? 31.012  30.488  -0.148  1   49.52 ? 189 GLN   A C   1 
ATOM   1443 O  O   . GLN   A 1 204 ? 31.824  29.929  -0.866  1   50.13 ? 189 GLN   A O   1 
ATOM   1444 C  CB  . GLN   A 1 204 ? 29.038  29.188  0.709   1   52.7  ? 189 GLN   A CB  1 
ATOM   1445 C  CG  . GLN   A 1 204 ? 29.117  28.07   -0.326  1   59.74 ? 189 GLN   A CG  1 
ATOM   1446 C  CD  . GLN   A 1 204 ? 27.767  27.516  -0.703  1   68.87 ? 189 GLN   A CD  1 
ATOM   1447 O  OE1 . GLN   A 1 204 ? 26.724  28.181  -0.554  1   71.08 ? 189 GLN   A OE1 1 
ATOM   1448 N  NE2 . GLN   A 1 204 ? 27.762  26.273  -1.209  1   70.99 ? 189 GLN   A NE2 1 
ATOM   1449 N  N   . MET   A 1 205 ? 30.599  31.741  -0.353  1   49.31 ? 190 MET   A N   1 
ATOM   1450 C  CA  . MET   A 1 205 ? 31.056  32.588  -1.454  1   49.61 ? 190 MET   A CA  1 
ATOM   1451 C  C   . MET   A 1 205 ? 32.413  33.259  -1.196  1   48.77 ? 190 MET   A C   1 
ATOM   1452 O  O   . MET   A 1 205 ? 32.876  33.987  -2.064  1   49.32 ? 190 MET   A O   1 
ATOM   1453 C  CB  . MET   A 1 205 ? 30.025  33.705  -1.749  1   51.22 ? 190 MET   A CB  1 
ATOM   1454 C  CG  . MET   A 1 205 ? 28.625  33.223  -2.082  1   55.99 ? 190 MET   A CG  1 
ATOM   1455 S  SD  . MET   A 1 205 ? 28.583  32.084  -3.469  1   69.93 ? 190 MET   A SD  1 
ATOM   1456 C  CE  . MET   A 1 205 ? 27.852  30.638  -2.683  1   69.61 ? 190 MET   A CE  1 
ATOM   1457 N  N   . GLN   A 1 206 ? 32.998  33.091  0.002   1   47.58 ? 191 GLN   A N   1 
ATOM   1458 C  CA  . GLN   A 1 206 ? 34.25   33.708  0.411   1   47.23 ? 191 GLN   A CA  1 
ATOM   1459 C  C   . GLN   A 1 206 ? 34.177  35.229  0.258   1   45.97 ? 191 GLN   A C   1 
ATOM   1460 O  O   . GLN   A 1 206 ? 34.931  35.832  -0.505  1   46.21 ? 191 GLN   A O   1 
ATOM   1461 C  CB  . GLN   A 1 206 ? 35.431  33.103  -0.348  1   49    ? 191 GLN   A CB  1 
ATOM   1462 C  CG  . GLN   A 1 206 ? 35.817  31.717  0.158   1   52.75 ? 191 GLN   A CG  1 
ATOM   1463 C  CD  . GLN   A 1 206 ? 36.675  31.784  1.41    1   59.77 ? 191 GLN   A CD  1 
ATOM   1464 O  OE1 . GLN   A 1 206 ? 37.148  32.853  1.847   1   61.14 ? 191 GLN   A OE1 1 
ATOM   1465 N  NE2 . GLN   A 1 206 ? 36.912  30.63   2.02    1   61.85 ? 191 GLN   A NE2 1 
ATOM   1466 N  N   . GLU   A 1 207 ? 33.204  35.823  0.93    1   43.31 ? 192 GLU   A N   1 
ATOM   1467 C  CA  . GLU   A 1 207 ? 32.939  37.245  0.887   1   41.61 ? 192 GLU   A CA  1 
ATOM   1468 C  C   . GLU   A 1 207 ? 33.131  37.816  2.289   1   39.74 ? 192 GLU   A C   1 
ATOM   1469 O  O   . GLU   A 1 207 ? 32.153  38.023  3.009   1   39.52 ? 192 GLU   A O   1 
ATOM   1470 C  CB  . GLU   A 1 207 ? 31.501  37.499  0.392   1   43.65 ? 192 GLU   A CB  1 
ATOM   1471 C  CG  . GLU   A 1 207 ? 31.273  37.069  -1.047  1   48    ? 192 GLU   A CG  1 
ATOM   1472 C  CD  . GLU   A 1 207 ? 31.865  38.002  -2.085  1   56.41 ? 192 GLU   A CD  1 
ATOM   1473 O  OE1 . GLU   A 1 207 ? 31.932  39.224  -1.812  1   55.77 ? 192 GLU   A OE1 1 
ATOM   1474 O  OE2 . GLU   A 1 207 ? 32.264  37.513  -3.171  1   60.31 ? 192 GLU   A OE2 1 
ATOM   1475 N  N   . ARG   A 1 208 ? 34.404  38.058  2.671   1   37.47 ? 193 ARG   A N   1 
ATOM   1476 C  CA  . ARG   A 1 208 ? 34.793  38.566  3.981   1   36.08 ? 193 ARG   A CA  1 
ATOM   1477 C  C   . ARG   A 1 208 ? 34.049  39.824  4.396   1   35.87 ? 193 ARG   A C   1 
ATOM   1478 O  O   . ARG   A 1 208 ? 33.585  39.886  5.538   1   36.26 ? 193 ARG   A O   1 
ATOM   1479 C  CB  . ARG   A 1 208 ? 36.33   38.775  4.048   1   36.32 ? 193 ARG   A CB  1 
ATOM   1480 C  CG  . ARG   A 1 208 ? 36.881  39.279  5.38    1   34.47 ? 193 ARG   A CG  1 
ATOM   1481 C  CD  . ARG   A 1 208 ? 36.959  40.783  5.392   1   34.66 ? 193 ARG   A CD  1 
ATOM   1482 N  NE  . ARG   A 1 208 ? 37.597  41.312  6.597   1   32.67 ? 193 ARG   A NE  1 
ATOM   1483 C  CZ  . ARG   A 1 208 ? 37.614  42.603  6.92    1   32    ? 193 ARG   A CZ  1 
ATOM   1484 N  NH1 . ARG   A 1 208 ? 36.998  43.493  6.157   1   28.22 ? 193 ARG   A NH1 1 
ATOM   1485 N  NH2 . ARG   A 1 208 ? 38.23   43.011  8.022   1   33.45 ? 193 ARG   A NH2 1 
ATOM   1486 N  N   . ASP   A 1 209 ? 33.968  40.843  3.521   1   34.94 ? 194 ASP   A N   1 
ATOM   1487 C  CA  . ASP   A 1 209 ? 33.308  42.097  3.916   1   35.05 ? 194 ASP   A CA  1 
ATOM   1488 C  C   . ASP   A 1 209 ? 31.808  41.888  4.21    1   34.77 ? 194 ASP   A C   1 
ATOM   1489 O  O   . ASP   A 1 209 ? 31.274  42.513  5.135   1   35.17 ? 194 ASP   A O   1 
ATOM   1490 C  CB  . ASP   A 1 209 ? 33.493  43.199  2.857   1   35.88 ? 194 ASP   A CB  1 
ATOM   1491 C  CG  . ASP   A 1 209 ? 34.936  43.677  2.721   1   39.3  ? 194 ASP   A CG  1 
ATOM   1492 O  OD1 . ASP   A 1 209 ? 35.719  43.485  3.676   1   40.95 ? 194 ASP   A OD1 1 
ATOM   1493 O  OD2 . ASP   A 1 209 ? 35.272  44.245  1.668   1   39.52 ? 194 ASP   A OD2 1 
ATOM   1494 N  N   . THR   A 1 210 ? 31.144  41.035  3.41    1   33.81 ? 195 THR   A N   1 
ATOM   1495 C  CA  . THR   A 1 210 ? 29.724  40.735  3.592   1   34.66 ? 195 THR   A CA  1 
ATOM   1496 C  C   . THR   A 1 210 ? 29.549  40.002  4.928   1   34.2  ? 195 THR   A C   1 
ATOM   1497 O  O   . THR   A 1 210 ? 28.664  40.375  5.695   1   35.08 ? 195 THR   A O   1 
ATOM   1498 C  CB  . THR   A 1 210 ? 29.172  39.958  2.386   1   36.69 ? 195 THR   A CB  1 
ATOM   1499 O  OG1 . THR   A 1 210 ? 29.435  40.715  1.191   1   37.97 ? 195 THR   A OG1 1 
ATOM   1500 C  CG2 . THR   A 1 210 ? 27.649  39.695  2.509   1   36.4  ? 195 THR   A CG2 1 
ATOM   1501 N  N   . LEU   A 1 211 ? 30.443  39.038  5.245   1   32.46 ? 196 LEU   A N   1 
ATOM   1502 C  CA  . LEU   A 1 211 ? 30.367  38.314  6.518   1   33.31 ? 196 LEU   A CA  1 
ATOM   1503 C  C   . LEU   A 1 211 ? 30.536  39.252  7.702   1   34.9  ? 196 LEU   A C   1 
ATOM   1504 O  O   . LEU   A 1 211 ? 29.745  39.195  8.636   1   34.92 ? 196 LEU   A O   1 
ATOM   1505 C  CB  . LEU   A 1 211 ? 31.392  37.177  6.576   1   32.96 ? 196 LEU   A CB  1 
ATOM   1506 C  CG  . LEU   A 1 211 ? 31.445  36.385  7.877   1   33.61 ? 196 LEU   A CG  1 
ATOM   1507 C  CD1 . LEU   A 1 211 ? 30.096  35.704  8.165   1   33.35 ? 196 LEU   A CD1 1 
ATOM   1508 C  CD2 . LEU   A 1 211 ? 32.567  35.383  7.851   1   34.05 ? 196 LEU   A CD2 1 
ATOM   1509 N  N   . LEU   A 1 212 ? 31.522  40.148  7.648   1   35.34 ? 197 LEU   A N   1 
ATOM   1510 C  CA  . LEU   A 1 212 ? 31.757  41.099  8.736   1   36.08 ? 197 LEU   A CA  1 
ATOM   1511 C  C   . LEU   A 1 212 ? 30.526  42.011  8.968   1   35.53 ? 197 LEU   A C   1 
ATOM   1512 O  O   . LEU   A 1 212 ? 30.153  42.27   10.117  1   35.31 ? 197 LEU   A O   1 
ATOM   1513 C  CB  . LEU   A 1 212 ? 32.993  41.96   8.403   1   37.24 ? 197 LEU   A CB  1 
ATOM   1514 C  CG  . LEU   A 1 212 ? 33.56   42.769  9.554   1   40.04 ? 197 LEU   A CG  1 
ATOM   1515 C  CD1 . LEU   A 1 212 ? 35.06   42.829  9.461   1   41.54 ? 197 LEU   A CD1 1 
ATOM   1516 C  CD2 . LEU   A 1 212 ? 33.056  44.176  9.54    1   40.82 ? 197 LEU   A CD2 1 
ATOM   1517 N  N   . LYS   A 1 213 ? 29.937  42.536  7.885   1   35.12 ? 198 LYS   A N   1 
ATOM   1518 C  CA  . LYS   A 1 213 ? 28.761  43.406  7.983   1   36    ? 198 LYS   A CA  1 
ATOM   1519 C  C   . LYS   A 1 213 ? 27.579  42.651  8.649   1   35.26 ? 198 LYS   A C   1 
ATOM   1520 O  O   . LYS   A 1 213 ? 26.946  43.183  9.558   1   34.77 ? 198 LYS   A O   1 
ATOM   1521 C  CB  . LYS   A 1 213 ? 28.382  43.9    6.58    1   39.07 ? 198 LYS   A CB  1 
ATOM   1522 C  CG  . LYS   A 1 213 ? 27.406  45.059  6.538   1   45.85 ? 198 LYS   A CG  1 
ATOM   1523 C  CD  . LYS   A 1 213 ? 26.864  45.251  5.107   1   51.6  ? 198 LYS   A CD  1 
ATOM   1524 C  CE  . LYS   A 1 213 ? 25.531  45.956  5.044   1   56.44 ? 198 LYS   A CE  1 
ATOM   1525 N  NZ  . LYS   A 1 213 ? 24.849  45.732  3.73    1   60.5  ? 198 LYS   A NZ  1 
ATOM   1526 N  N   . ALA   A 1 214 ? 27.333  41.391  8.226   1   34.41 ? 199 ALA   A N   1 
ATOM   1527 C  CA  . ALA   A 1 214 ? 26.287  40.517  8.764   1   33.45 ? 199 ALA   A CA  1 
ATOM   1528 C  C   . ALA   A 1 214 ? 26.53   40.226  10.257  1   33.56 ? 199 ALA   A C   1 
ATOM   1529 O  O   . ALA   A 1 214 ? 25.589  40.321  11.061  1   33.38 ? 199 ALA   A O   1 
ATOM   1530 C  CB  . ALA   A 1 214 ? 26.251  39.207  7.982   1   32.43 ? 199 ALA   A CB  1 
ATOM   1531 N  N   . LEU   A 1 215 ? 27.8    39.914  10.649  1   32.4  ? 200 LEU   A N   1 
ATOM   1532 C  CA  . LEU   A 1 215 ? 28.087  39.658  12.051  1   31.81 ? 200 LEU   A CA  1 
ATOM   1533 C  C   . LEU   A 1 215 ? 27.82   40.898  12.907  1   32.42 ? 200 LEU   A C   1 
ATOM   1534 O  O   . LEU   A 1 215 ? 27.269  40.778  14.002  1   32.2  ? 200 LEU   A O   1 
ATOM   1535 C  CB  . LEU   A 1 215 ? 29.484  39.119  12.257  1   31.88 ? 200 LEU   A CB  1 
ATOM   1536 C  CG  . LEU   A 1 215 ? 29.771  37.717  11.713  1   32.28 ? 200 LEU   A CG  1 
ATOM   1537 C  CD1 . LEU   A 1 215 ? 31.184  37.33   11.992  1   32.91 ? 200 LEU   A CD1 1 
ATOM   1538 C  CD2 . LEU   A 1 215 ? 28.883  36.695  12.348  1   32.77 ? 200 LEU   A CD2 1 
ATOM   1539 N  N   . LEU   A 1 216 ? 28.14   42.087  12.398  1   32.6  ? 201 LEU   A N   1 
ATOM   1540 C  CA  . LEU   A 1 216 ? 27.887  43.33   13.136  1   33.61 ? 201 LEU   A CA  1 
ATOM   1541 C  C   . LEU   A 1 216 ? 26.389  43.67   13.235  1   33.66 ? 201 LEU   A C   1 
ATOM   1542 O  O   . LEU   A 1 216 ? 25.972  44.28   14.212  1   33.68 ? 201 LEU   A O   1 
ATOM   1543 C  CB  . LEU   A 1 216 ? 28.626  44.502  12.474  1   34.7  ? 201 LEU   A CB  1 
ATOM   1544 C  CG  . LEU   A 1 216 ? 30.154  44.498  12.621  1   36.89 ? 201 LEU   A CG  1 
ATOM   1545 C  CD1 . LEU   A 1 216 ? 30.764  45.703  11.887  1   37.67 ? 201 LEU   A CD1 1 
ATOM   1546 C  CD2 . LEU   A 1 216 ? 30.573  44.5    14.099  1   36.96 ? 201 LEU   A CD2 1 
ATOM   1547 N  N   . GLU   A 1 217 ? 25.599  43.315  12.214  1   33.01 ? 202 GLU   A N   1 
ATOM   1548 C  CA  . GLU   A 1 217 ? 24.158  43.53   12.215  1   32.8  ? 202 GLU   A CA  1 
ATOM   1549 C  C   . GLU   A 1 217 ? 23.504  42.577  13.229  1   32.91 ? 202 GLU   A C   1 
ATOM   1550 O  O   . GLU   A 1 217 ? 22.655  42.997  14.003  1   33.32 ? 202 GLU   A O   1 
ATOM   1551 C  CB  . GLU   A 1 217 ? 23.585  43.338  10.802  1   34.7  ? 202 GLU   A CB  1 
ATOM   1552 C  CG  . GLU   A 1 217 ? 22.077  43.53   10.696  1   38.04 ? 202 GLU   A CG  1 
ATOM   1553 C  CD  . GLU   A 1 217 ? 21.479  44.858  11.149  1   47.17 ? 202 GLU   A CD  1 
ATOM   1554 O  OE1 . GLU   A 1 217 ? 22.221  45.863  11.265  1   49.01 ? 202 GLU   A OE1 1 
ATOM   1555 O  OE2 . GLU   A 1 217 ? 20.247  44.892  11.373  1   49.54 ? 202 GLU   A OE2 1 
ATOM   1556 N  N   . ILE   A 1 218 ? 23.988  41.322  13.318  1   31.62 ? 203 ILE   A N   1 
ATOM   1557 C  CA  . ILE   A 1 218 ? 23.495  40.379  14.314  1   31.4  ? 203 ILE   A CA  1 
ATOM   1558 C  C   . ILE   A 1 218 ? 23.805  40.914  15.708  1   32.17 ? 203 ILE   A C   1 
ATOM   1559 O  O   . ILE   A 1 218 ? 22.888  41.007  16.54   1   33.56 ? 203 ILE   A O   1 
ATOM   1560 C  CB  . ILE   A 1 218 ? 24.075  38.969  14.068  1   30.43 ? 203 ILE   A CB  1 
ATOM   1561 C  CG1 . ILE   A 1 218 ? 23.434  38.33   12.835  1   30.39 ? 203 ILE   A CG1 1 
ATOM   1562 C  CG2 . ILE   A 1 218 ? 23.983  38.066  15.309  1   30.77 ? 203 ILE   A CG2 1 
ATOM   1563 C  CD1 . ILE   A 1 218 ? 23.991  36.996  12.454  1   30.33 ? 203 ILE   A CD1 1 
ATOM   1564 N  N   . ALA   A 1 219 ? 25.051  41.364  15.934  1   31.05 ? 204 ALA   A N   1 
ATOM   1565 C  CA  . ALA   A 1 219 ? 25.463  41.884  17.231  1   31.6  ? 204 ALA   A CA  1 
ATOM   1566 C  C   . ALA   A 1 219 ? 24.602  43.103  17.612  1   33.15 ? 204 ALA   A C   1 
ATOM   1567 O  O   . ALA   A 1 219 ? 24.064  43.15   18.714  1   33.66 ? 204 ALA   A O   1 
ATOM   1568 C  CB  . ALA   A 1 219 ? 26.944  42.258  17.205  1   31.56 ? 204 ALA   A CB  1 
ATOM   1569 N  N   . SER   A 1 220 ? 24.377  44.015  16.657  1   32.8  ? 205 SER   A N   1 
ATOM   1570 C  CA  . SER   A 1 220 ? 23.565  45.198  16.865  1   33.83 ? 205 SER   A CA  1 
ATOM   1571 C  C   . SER   A 1 220 ? 22.117  44.812  17.309  1   34.74 ? 205 SER   A C   1 
ATOM   1572 O  O   . SER   A 1 220 ? 21.6    45.341  18.287  1   34.98 ? 205 SER   A O   1 
ATOM   1573 C  CB  . SER   A 1 220 ? 23.554  46.021  15.577  1   35.04 ? 205 SER   A CB  1 
ATOM   1574 O  OG  . SER   A 1 220 ? 22.449  46.894  15.479  1   38.2  ? 205 SER   A OG  1 
ATOM   1575 N  N   . CYS   A 1 221 ? 21.517  43.83   16.636  1   34.65 ? 206 CYS   A N   1 
ATOM   1576 C  CA  . CYS   A 1 221 ? 20.176  43.362  16.948  1   34.95 ? 206 CYS   A CA  1 
ATOM   1577 C  C   . CYS   A 1 221 ? 20.086  42.707  18.331  1   35.03 ? 206 CYS   A C   1 
ATOM   1578 O  O   . CYS   A 1 221 ? 19.188  43.046  19.109  1   35.36 ? 206 CYS   A O   1 
ATOM   1579 C  CB  . CYS   A 1 221 ? 19.682  42.44   15.845  1   35.81 ? 206 CYS   A CB  1 
ATOM   1580 S  SG  . CYS   A 1 221 ? 19.334  43.295  14.286  1   42.09 ? 206 CYS   A SG  1 
ATOM   1581 N  N   . LEU   A 1 222 ? 21.073  41.873  18.684  1   33.57 ? 207 LEU   A N   1 
ATOM   1582 C  CA  . LEU   A 1 222 ? 21.111  41.248  20.011  1   32.6  ? 207 LEU   A CA  1 
ATOM   1583 C  C   . LEU   A 1 222 ? 21.367  42.256  21.122  1   32.25 ? 207 LEU   A C   1 
ATOM   1584 O  O   . LEU   A 1 222 ? 20.862  42.072  22.225  1   31.67 ? 207 LEU   A O   1 
ATOM   1585 C  CB  . LEU   A 1 222 ? 22.141  40.119  20.062  1   32.2  ? 207 LEU   A CB  1 
ATOM   1586 C  CG  . LEU   A 1 222 ? 21.876  38.967  19.101  1   32.07 ? 207 LEU   A CG  1 
ATOM   1587 C  CD1 . LEU   A 1 222 ? 22.962  37.942  19.185  1   31.83 ? 207 LEU   A CD1 1 
ATOM   1588 C  CD2 . LEU   A 1 222 ? 20.537  38.302  19.395  1   32.08 ? 207 LEU   A CD2 1 
ATOM   1589 N  N   . GLU   A 1 223 ? 22.101  43.345  20.818  1   32.74 ? 208 GLU   A N   1 
ATOM   1590 C  CA  . GLU   A 1 223 ? 22.359  44.436  21.761  1   33.87 ? 208 GLU   A CA  1 
ATOM   1591 C  C   . GLU   A 1 223 ? 21.044  45.187  22.019  1   35.81 ? 208 GLU   A C   1 
ATOM   1592 O  O   . GLU   A 1 223 ? 20.777  45.566  23.161  1   36.91 ? 208 GLU   A O   1 
ATOM   1593 C  CB  . GLU   A 1 223 ? 23.404  45.414  21.201  1   35.39 ? 208 GLU   A CB  1 
ATOM   1594 C  CG  . GLU   A 1 223 ? 24.842  44.936  21.329  1   39.08 ? 208 GLU   A CG  1 
ATOM   1595 C  CD  . GLU   A 1 223 ? 25.823  45.603  20.375  1   45.91 ? 208 GLU   A CD  1 
ATOM   1596 O  OE1 . GLU   A 1 223 ? 25.488  46.68   19.828  1   46.48 ? 208 GLU   A OE1 1 
ATOM   1597 O  OE2 . GLU   A 1 223 ? 26.929  45.047  20.176  1   47.3  ? 208 GLU   A OE2 1 
ATOM   1598 N  N   . LYS   A 1 224 ? 20.212  45.384  20.976  1   35.4  ? 209 LYS   A N   1 
ATOM   1599 C  CA  . LYS   A 1 224 ? 18.914  46.05   21.134  1   36.25 ? 209 LYS   A CA  1 
ATOM   1600 C  C   . LYS   A 1 224 ? 17.945  45.206  21.951  1   36.49 ? 209 LYS   A C   1 
ATOM   1601 O  O   . LYS   A 1 224 ? 17.188  45.758  22.732  1   38.13 ? 209 LYS   A O   1 
ATOM   1602 C  CB  . LYS   A 1 224 ? 18.306  46.399  19.774  1   38.23 ? 209 LYS   A CB  1 
ATOM   1603 C  CG  . LYS   A 1 224 ? 19.023  47.563  19.087  1   43.75 ? 209 LYS   A CG  1 
ATOM   1604 C  CD  . LYS   A 1 224 ? 18.601  47.649  17.619  1   50.07 ? 209 LYS   A CD  1 
ATOM   1605 C  CE  . LYS   A 1 224 ? 18.717  49.044  17.065  1   55.93 ? 209 LYS   A CE  1 
ATOM   1606 N  NZ  . LYS   A 1 224 ? 20.081  49.606  17.244  1   60.42 ? 209 LYS   A NZ  1 
ATOM   1607 N  N   . ALA   A 1 225 ? 18.035  43.878  21.848  1   35.31 ? 210 ALA   A N   1 
ATOM   1608 C  CA  . ALA   A 1 225 ? 17.21   42.946  22.606  1   35.6  ? 210 ALA   A CA  1 
ATOM   1609 C  C   . ALA   A 1 225 ? 17.415  43.065  24.125  1   35.71 ? 210 ALA   A C   1 
ATOM   1610 O  O   . ALA   A 1 225 ? 16.511  42.724  24.89   1   35.09 ? 210 ALA   A O   1 
ATOM   1611 C  CB  . ALA   A 1 225 ? 17.5    41.522  22.158  1   35.36 ? 210 ALA   A CB  1 
ATOM   1612 N  N   . LEU   A 1 226 ? 18.594  43.534  24.564  1   35.14 ? 211 LEU   A N   1 
ATOM   1613 C  CA  . LEU   A 1 226 ? 18.874  43.698  25.984  1   35.03 ? 211 LEU   A CA  1 
ATOM   1614 C  C   . LEU   A 1 226 ? 17.941  44.725  26.607  1   35.94 ? 211 LEU   A C   1 
ATOM   1615 O  O   . LEU   A 1 226 ? 17.479  44.53   27.739  1   35.41 ? 211 LEU   A O   1 
ATOM   1616 C  CB  . LEU   A 1 226 ? 20.338  44.121  26.201  1   34.17 ? 211 LEU   A CB  1 
ATOM   1617 C  CG  . LEU   A 1 226 ? 20.752  44.401  27.647  1   34.41 ? 211 LEU   A CG  1 
ATOM   1618 C  CD1 . LEU   A 1 226 ? 20.61   43.165  28.492  1   34.88 ? 211 LEU   A CD1 1 
ATOM   1619 C  CD2 . LEU   A 1 226 ? 22.206  44.883  27.713  1   35.04 ? 211 LEU   A CD2 1 
ATOM   1620 N  N   . GLN   A 1 227 ? 17.669  45.821  25.889  1   37.29 ? 212 GLN   A N   1 
ATOM   1621 C  CA  . GLN   A 1 227 ? 16.787  46.863  26.422  1   39.58 ? 212 GLN   A CA  1 
ATOM   1622 C  C   . GLN   A 1 227 ? 15.357  46.338  26.629  1   39.42 ? 212 GLN   A C   1 
ATOM   1623 O  O   . GLN   A 1 227 ? 14.687  46.751  27.574  1   40.05 ? 212 GLN   A O   1 
ATOM   1624 C  CB  . GLN   A 1 227 ? 16.802  48.147  25.559  1   43.92 ? 212 GLN   A CB  1 
ATOM   1625 C  CG  . GLN   A 1 227 ? 18.104  48.427  24.759  1   51.32 ? 212 GLN   A CG  1 
ATOM   1626 C  CD  . GLN   A 1 227 ? 19.413  48.36   25.551  1   60.07 ? 212 GLN   A CD  1 
ATOM   1627 O  OE1 . GLN   A 1 227 ? 19.524  48.805  26.71   1   62.89 ? 212 GLN   A OE1 1 
ATOM   1628 N  NE2 . GLN   A 1 227 ? 20.447  47.798  24.931  1   61.43 ? 212 GLN   A NE2 1 
ATOM   1629 N  N   . VAL   A 1 228 ? 14.932  45.378  25.795  1   38.07 ? 213 VAL   A N   1 
ATOM   1630 C  CA  . VAL   A 1 228 ? 13.631  44.729  25.891  1   37.66 ? 213 VAL   A CA  1 
ATOM   1631 C  C   . VAL   A 1 228 ? 13.483  44.016  27.223  1   37.66 ? 213 VAL   A C   1 
ATOM   1632 O  O   . VAL   A 1 228 ? 12.425  44.113  27.823  1   38.61 ? 213 VAL   A O   1 
ATOM   1633 C  CB  . VAL   A 1 228 ? 13.413  43.788  24.69   1   37.84 ? 213 VAL   A CB  1 
ATOM   1634 C  CG1 . VAL   A 1 228 ? 12.071  43.087  24.781  1   38.52 ? 213 VAL   A CG1 1 
ATOM   1635 C  CG2 . VAL   A 1 228 ? 13.514  44.57   23.39   1   37.63 ? 213 VAL   A CG2 1 
ATOM   1636 N  N   . PHE   A 1 229 ? 14.553  43.399  27.736  1   36.48 ? 214 PHE   A N   1 
ATOM   1637 C  CA  . PHE   A 1 229 ? 14.578  42.718  29.031  1   36.9  ? 214 PHE   A CA  1 
ATOM   1638 C  C   . PHE   A 1 229 ? 14.284  43.641  30.189  1   38.41 ? 214 PHE   A C   1 
ATOM   1639 O  O   . PHE   A 1 229 ? 13.791  43.173  31.223  1   39.21 ? 214 PHE   A O   1 
ATOM   1640 C  CB  . PHE   A 1 229 ? 15.954  42.094  29.297  1   36.6  ? 214 PHE   A CB  1 
ATOM   1641 C  CG  . PHE   A 1 229 ? 16.114  40.642  28.933  1   37.1  ? 214 PHE   A CG  1 
ATOM   1642 C  CD1 . PHE   A 1 229 ? 15.857  39.647  29.857  1   37.81 ? 214 PHE   A CD1 1 
ATOM   1643 C  CD2 . PHE   A 1 229 ? 16.569  40.277  27.685  1   37.8  ? 214 PHE   A CD2 1 
ATOM   1644 C  CE1 . PHE   A 1 229 ? 16.04   38.309  29.531  1   38.89 ? 214 PHE   A CE1 1 
ATOM   1645 C  CE2 . PHE   A 1 229 ? 16.739  38.941  27.357  1   38.72 ? 214 PHE   A CE2 1 
ATOM   1646 C  CZ  . PHE   A 1 229 ? 16.48   37.964  28.284  1   38.82 ? 214 PHE   A CZ  1 
ATOM   1647 N  N   . HIS   A 1 230 ? 14.626  44.937  30.068  1   38.81 ? 215 HIS   A N   1 
ATOM   1648 C  CA  . HIS   A 1 230 ? 14.377  45.873  31.172  1   39.61 ? 215 HIS   A CA  1 
ATOM   1649 C  C   . HIS   A 1 230 ? 12.885  46.011  31.513  1   37.92 ? 215 HIS   A C   1 
ATOM   1650 O  O   . HIS   A 1 230 ? 12.562  46.312  32.652  1   38.79 ? 215 HIS   A O   1 
ATOM   1651 C  CB  . HIS   A 1 230 ? 14.981  47.255  30.887  1   42.1  ? 215 HIS   A CB  1 
ATOM   1652 C  CG  . HIS   A 1 230 ? 16.454  47.243  30.63   1   46.96 ? 215 HIS   A CG  1 
ATOM   1653 N  ND1 . HIS   A 1 230 ? 17.073  48.284  29.963  1   49.67 ? 215 HIS   A ND1 1 
ATOM   1654 C  CD2 . HIS   A 1 230 ? 17.389  46.322  30.963  1   48.47 ? 215 HIS   A CD2 1 
ATOM   1655 C  CE1 . HIS   A 1 230 ? 18.356  47.964  29.913  1   50.25 ? 215 HIS   A CE1 1 
ATOM   1656 N  NE2 . HIS   A 1 230 ? 18.591  46.79   30.5    1   49.75 ? 215 HIS   A NE2 1 
ATOM   1657 N  N   . GLN   A 1 231 ? 11.983  45.742  30.554  1   36.53 ? 216 GLN   A N   1 
ATOM   1658 C  CA  . GLN   A 1 231 ? 10.511  45.803  30.771  1   35.48 ? 216 GLN   A CA  1 
ATOM   1659 C  C   . GLN   A 1 231 ? 9.994   44.854  31.821  1   34.36 ? 216 GLN   A C   1 
ATOM   1660 O  O   . GLN   A 1 231 ? 8.876   45.048  32.289  1   35.06 ? 216 GLN   A O   1 
ATOM   1661 C  CB  . GLN   A 1 231 ? 9.75    45.496  29.483  1   37.19 ? 216 GLN   A CB  1 
ATOM   1662 C  CG  . GLN   A 1 231 ? 10.023  46.51   28.391  1   42.2  ? 216 GLN   A CG  1 
ATOM   1663 C  CD  . GLN   A 1 231 ? 9.292   46.122  27.141  1   48.3  ? 216 GLN   A CD  1 
ATOM   1664 O  OE1 . GLN   A 1 231 ? 8.155   46.541  26.892  1   50.66 ? 216 GLN   A OE1 1 
ATOM   1665 N  NE2 . GLN   A 1 231 ? 9.928   45.295  26.336  1   48.61 ? 216 GLN   A NE2 1 
ATOM   1666 N  N   . ILE   A 1 232 ? 10.771  43.814  32.171  1   32.56 ? 217 ILE   A N   1 
ATOM   1667 C  CA  . ILE   A 1 232 ? 10.373  42.803  33.145  1   30.8  ? 217 ILE   A CA  1 
ATOM   1668 C  C   . ILE   A 1 232 ? 10.04   43.422  34.481  1   30.71 ? 217 ILE   A C   1 
ATOM   1669 O  O   . ILE   A 1 232 ? 9.069   43.008  35.115  1   30.96 ? 217 ILE   A O   1 
ATOM   1670 C  CB  . ILE   A 1 232 ? 11.42   41.654  33.293  1   30.44 ? 217 ILE   A CB  1 
ATOM   1671 C  CG1 . ILE   A 1 232 ? 10.778  40.401  33.895  1   30.73 ? 217 ILE   A CG1 1 
ATOM   1672 C  CG2 . ILE   A 1 232 ? 12.666  42.071  34.077  1   30.93 ? 217 ILE   A CG2 1 
ATOM   1673 C  CD1 . ILE   A 1 232 ? 10.018  39.587  32.833  1   30.4  ? 217 ILE   A CD1 1 
ATOM   1674 N  N   . HIS   A 1 233 ? 10.804  44.437  34.898  1   30.28 ? 218 HIS   A N   1 
ATOM   1675 C  CA  . HIS   A 1 233 ? 10.575  45.06   36.206  1   30.88 ? 218 HIS   A CA  1 
ATOM   1676 C  C   . HIS   A 1 233 ? 9.233   45.791  36.332  1   31.59 ? 218 HIS   A C   1 
ATOM   1677 O  O   . HIS   A 1 233 ? 8.671   45.879  37.428  1   32.07 ? 218 HIS   A O   1 
ATOM   1678 C  CB  . HIS   A 1 233 ? 11.736  45.994  36.56   1   30.95 ? 218 HIS   A CB  1 
ATOM   1679 C  CG  . HIS   A 1 233 ? 13.069  45.306  36.5    1   33.44 ? 218 HIS   A CG  1 
ATOM   1680 N  ND1 . HIS   A 1 233 ? 13.457  44.401  37.481  1   35.12 ? 218 HIS   A ND1 1 
ATOM   1681 C  CD2 . HIS   A 1 233 ? 14.021  45.35   35.542  1   33.1  ? 218 HIS   A CD2 1 
ATOM   1682 C  CE1 . HIS   A 1 233 ? 14.653  43.971  37.117  1   34.75 ? 218 HIS   A CE1 1 
ATOM   1683 N  NE2 . HIS   A 1 233 ? 15.032  44.506  35.952  1   34.02 ? 218 HIS   A NE2 1 
ATOM   1684 N  N   . ASP   A 1 234 ? 8.722   46.313  35.222  1   31.36 ? 219 ASP   A N   1 
ATOM   1685 C  CA  . ASP   A 1 234 ? 7.454   47.035  35.232  1   32.17 ? 219 ASP   A CA  1 
ATOM   1686 C  C   . ASP   A 1 234 ? 6.223   46.132  35.251  1   32.55 ? 219 ASP   A C   1 
ATOM   1687 O  O   . ASP   A 1 234 ? 5.129   46.603  35.561  1   33.9  ? 219 ASP   A O   1 
ATOM   1688 C  CB  . ASP   A 1 234 ? 7.385   47.91   33.977  1   33.68 ? 219 ASP   A CB  1 
ATOM   1689 C  CG  . ASP   A 1 234 ? 8.387   49.038  34.013  1   38.8  ? 219 ASP   A CG  1 
ATOM   1690 O  OD1 . ASP   A 1 234 ? 8.718   49.501  35.125  1   39.66 ? 219 ASP   A OD1 1 
ATOM   1691 O  OD2 . ASP   A 1 234 ? 8.845   49.458  32.935  1   41.44 ? 219 ASP   A OD2 1 
ATOM   1692 N  N   . HIS   A 1 235 ? 6.368   44.869  34.852  1   31.22 ? 220 HIS   A N   1 
ATOM   1693 C  CA  . HIS   A 1 235 ? 5.224   44.009  34.664  1   30.82 ? 220 HIS   A CA  1 
ATOM   1694 C  C   . HIS   A 1 235 ? 5.224   42.74   35.489  1   31.04 ? 220 HIS   A C   1 
ATOM   1695 O  O   . HIS   A 1 235 ? 4.261   41.977  35.387  1   30.97 ? 220 HIS   A O   1 
ATOM   1696 C  CB  . HIS   A 1 235 ? 5.086   43.693  33.161  1   32.25 ? 220 HIS   A CB  1 
ATOM   1697 C  CG  . HIS   A 1 235 ? 5.056   44.936  32.321  1   35.24 ? 220 HIS   A CG  1 
ATOM   1698 N  ND1 . HIS   A 1 235 ? 4.169   45.957  32.592  1   37.63 ? 220 HIS   A ND1 1 
ATOM   1699 C  CD2 . HIS   A 1 235 ? 5.833   45.302  31.273  1   35.98 ? 220 HIS   A CD2 1 
ATOM   1700 C  CE1 . HIS   A 1 235 ? 4.429   46.91   31.704  1   37.06 ? 220 HIS   A CE1 1 
ATOM   1701 N  NE2 . HIS   A 1 235 ? 5.409   46.553  30.878  1   36.38 ? 220 HIS   A NE2 1 
ATOM   1702 N  N   . VAL   A 1 236 ? 6.283   42.471  36.273  1   30.68 ? 221 VAL   A N   1 
ATOM   1703 C  CA  . VAL   A 1 236 ? 6.335   41.262  37.09   1   31    ? 221 VAL   A CA  1 
ATOM   1704 C  C   . VAL   A 1 236 ? 6.774   41.617  38.499  1   31.64 ? 221 VAL   A C   1 
ATOM   1705 O  O   . VAL   A 1 236 ? 7.709   42.403  38.641  1   31.24 ? 221 VAL   A O   1 
ATOM   1706 C  CB  . VAL   A 1 236 ? 7.279   40.187  36.496  1   31.5  ? 221 VAL   A CB  1 
ATOM   1707 C  CG1 . VAL   A 1 236 ? 7.182   38.877  37.298  1   32.7  ? 221 VAL   A CG1 1 
ATOM   1708 C  CG2 . VAL   A 1 236 ? 6.989   39.922  35.025  1   30.88 ? 221 VAL   A CG2 1 
ATOM   1709 N  N   . ASN   A 1 237 ? 6.147   41.032  39.538  1   32.43 ? 222 ASN   A N   1 
ATOM   1710 C  CA  . ASN   A 1 237 ? 6.627   41.259  40.899  1   34.41 ? 222 ASN   A CA  1 
ATOM   1711 C  C   . ASN   A 1 237 ? 7.128   39.944  41.484  1   35.95 ? 222 ASN   A C   1 
ATOM   1712 O  O   . ASN   A 1 237 ? 6.537   38.896  41.24   1   37.29 ? 222 ASN   A O   1 
ATOM   1713 C  CB  . ASN   A 1 237 ? 5.625   41.988  41.798  1   36.53 ? 222 ASN   A CB  1 
ATOM   1714 C  CG  . ASN   A 1 237 ? 4.572   41.116  42.406  1   40.67 ? 222 ASN   A CG  1 
ATOM   1715 O  OD1 . ASN   A 1 237 ? 3.539   40.909  41.801  1   44.51 ? 222 ASN   A OD1 1 
ATOM   1716 N  ND2 . ASN   A 1 237 ? 4.813   40.591  43.614  1   39.72 ? 222 ASN   A ND2 1 
ATOM   1717 N  N   . PRO   A 1 238 ? 8.251   39.984  42.216  1   36.28 ? 223 PRO   A N   1 
ATOM   1718 C  CA  . PRO   A 1 238 ? 8.858   38.736  42.716  1   36.34 ? 223 PRO   A CA  1 
ATOM   1719 C  C   . PRO   A 1 238 ? 7.968   37.807  43.547  1   37.29 ? 223 PRO   A C   1 
ATOM   1720 O  O   . PRO   A 1 238 ? 8.013   36.596  43.328  1   37.94 ? 223 PRO   A O   1 
ATOM   1721 C  CB  . PRO   A 1 238 ? 10.06   39.226  43.53   1   36.32 ? 223 PRO   A CB  1 
ATOM   1722 C  CG  . PRO   A 1 238 ? 10.4    40.546  42.939  1   37.09 ? 223 PRO   A CG  1 
ATOM   1723 C  CD  . PRO   A 1 238 ? 9.098   41.158  42.515  1   35.76 ? 223 PRO   A CD  1 
ATOM   1724 N  N   . LYS   A 1 239 ? 7.206   38.339  44.511  1   37.36 ? 224 LYS   A N   1 
ATOM   1725 C  CA  . LYS   A 1 239 ? 6.371   37.493  45.369  1   38.66 ? 224 LYS   A CA  1 
ATOM   1726 C  C   . LYS   A 1 239 ? 5.388   36.611  44.593  1   38.23 ? 224 LYS   A C   1 
ATOM   1727 O  O   . LYS   A 1 239 ? 5.365   35.391  44.782  1   38.82 ? 224 LYS   A O   1 
ATOM   1728 C  CB  . LYS   A 1 239 ? 5.637   38.317  46.439  1   41.5  ? 224 LYS   A CB  1 
ATOM   1729 C  CG  . LYS   A 1 239 ? 4.855   37.454  47.421  1   45.8  ? 224 LYS   A CG  1 
ATOM   1730 N  N   . ALA   A 1 240 ? 4.635   37.22   43.691  1   37.17 ? 225 ALA   A N   1 
ATOM   1731 C  CA  . ALA   A 1 240 ? 3.631   36.559  42.883  1   37.44 ? 225 ALA   A CA  1 
ATOM   1732 C  C   . ALA   A 1 240 ? 4.269   35.597  41.898  1   37.67 ? 225 ALA   A C   1 
ATOM   1733 O  O   . ALA   A 1 240 ? 3.804   34.464  41.733  1   38.1  ? 225 ALA   A O   1 
ATOM   1734 C  CB  . ALA   A 1 240 ? 2.828   37.618  42.134  1   37.29 ? 225 ALA   A CB  1 
ATOM   1735 N  N   . PHE   A 1 241 ? 5.362   36.018  41.259  1   37.58 ? 226 PHE   A N   1 
ATOM   1736 C  CA  . PHE   A 1 241 ? 6.068   35.183  40.303  1   37.23 ? 226 PHE   A CA  1 
ATOM   1737 C  C   . PHE   A 1 241 ? 6.581   33.906  40.987  1   37.57 ? 226 PHE   A C   1 
ATOM   1738 O  O   . PHE   A 1 241 ? 6.425   32.802  40.465  1   37.17 ? 226 PHE   A O   1 
ATOM   1739 C  CB  . PHE   A 1 241 ? 7.248   35.978  39.698  1   36.35 ? 226 PHE   A CB  1 
ATOM   1740 C  CG  . PHE   A 1 241 ? 8.152   35.109  38.863  1   36.15 ? 226 PHE   A CG  1 
ATOM   1741 C  CD1 . PHE   A 1 241 ? 7.85    34.84   37.539  1   36.99 ? 226 PHE   A CD1 1 
ATOM   1742 C  CD2 . PHE   A 1 241 ? 9.25    34.48   39.428  1   36.72 ? 226 PHE   A CD2 1 
ATOM   1743 C  CE1 . PHE   A 1 241 ? 8.639   33.979  36.797  1   37.8  ? 226 PHE   A CE1 1 
ATOM   1744 C  CE2 . PHE   A 1 241 ? 10.039  33.62   38.68   1   37.58 ? 226 PHE   A CE2 1 
ATOM   1745 C  CZ  . PHE   A 1 241 ? 9.729   33.379  37.365  1   37.81 ? 226 PHE   A CZ  1 
ATOM   1746 N  N   . PHE   A 1 242 ? 7.197   34.084  42.161  1   38.1  ? 227 PHE   A N   1 
ATOM   1747 C  CA  . PHE   A 1 242 ? 7.816   32.981  42.856  1   38.35 ? 227 PHE   A CA  1 
ATOM   1748 C  C   . PHE   A 1 242 ? 6.819   32.049  43.478  1   38.72 ? 227 PHE   A C   1 
ATOM   1749 O  O   . PHE   A 1 242 ? 6.935   30.841  43.295  1   38.55 ? 227 PHE   A O   1 
ATOM   1750 C  CB  . PHE   A 1 242 ? 8.851   33.472  43.882  1   38.42 ? 227 PHE   A CB  1 
ATOM   1751 C  CG  . PHE   A 1 242 ? 9.577   32.347  44.579  1   39.15 ? 227 PHE   A CG  1 
ATOM   1752 C  CD1 . PHE   A 1 242 ? 10.637  31.701  43.967  1   40.18 ? 227 PHE   A CD1 1 
ATOM   1753 C  CD2 . PHE   A 1 242 ? 9.168   31.902  45.829  1   40.6  ? 227 PHE   A CD2 1 
ATOM   1754 C  CE1 . PHE   A 1 242 ? 11.284  30.641  44.591  1   41.24 ? 227 PHE   A CE1 1 
ATOM   1755 C  CE2 . PHE   A 1 242 ? 9.818   30.847  46.457  1   41.49 ? 227 PHE   A CE2 1 
ATOM   1756 C  CZ  . PHE   A 1 242 ? 10.884  30.234  45.845  1   41.25 ? 227 PHE   A CZ  1 
ATOM   1757 N  N   . SER   A 1 243 ? 5.867   32.583  44.242  1   39.22 ? 228 SER   A N   1 
ATOM   1758 C  CA  . SER   A 1 243 ? 4.911   31.738  44.948  1   39.9  ? 228 SER   A CA  1 
ATOM   1759 C  C   . SER   A 1 243 ? 3.777   31.205  44.076  1   39.76 ? 228 SER   A C   1 
ATOM   1760 O  O   . SER   A 1 243 ? 3.23    30.146  44.399  1   40.84 ? 228 SER   A O   1 
ATOM   1761 C  CB  . SER   A 1 243 ? 4.359   32.463  46.168  1   42.05 ? 228 SER   A CB  1 
ATOM   1762 O  OG  . SER   A 1 243 ? 3.577   33.575  45.758  1   46.05 ? 228 SER   A OG  1 
ATOM   1763 N  N   . VAL   A 1 244 ? 3.448   31.881  42.955  1   37.86 ? 229 VAL   A N   1 
ATOM   1764 C  CA  . VAL   A 1 244 ? 2.332   31.439  42.129  1   37.11 ? 229 VAL   A CA  1 
ATOM   1765 C  C   . VAL   A 1 244 ? 2.73    30.916  40.727  1   36.42 ? 229 VAL   A C   1 
ATOM   1766 O  O   . VAL   A 1 244 ? 2.532   29.733  40.452  1   36.78 ? 229 VAL   A O   1 
ATOM   1767 C  CB  . VAL   A 1 244 ? 1.227   32.526  42.037  1   37.51 ? 229 VAL   A CB  1 
ATOM   1768 C  CG1 . VAL   A 1 244 ? 0.04    32.013  41.24   1   38.09 ? 229 VAL   A CG1 1 
ATOM   1769 C  CG2 . VAL   A 1 244 ? 0.789   32.997  43.428  1   37.7  ? 229 VAL   A CG2 1 
ATOM   1770 N  N   . LEU   A 1 245 ? 3.221   31.777  39.827  1   35.48 ? 230 LEU   A N   1 
ATOM   1771 C  CA  . LEU   A 1 245 ? 3.494   31.37   38.446  1   34.78 ? 230 LEU   A CA  1 
ATOM   1772 C  C   . LEU   A 1 245 ? 4.463   30.183  38.331  1   34.4  ? 230 LEU   A C   1 
ATOM   1773 O  O   . LEU   A 1 245 ? 4.26    29.28   37.516  1   34.35 ? 230 LEU   A O   1 
ATOM   1774 C  CB  . LEU   A 1 245 ? 3.968   32.586  37.65   1   33.92 ? 230 LEU   A CB  1 
ATOM   1775 C  CG  . LEU   A 1 245 ? 4.068   32.432  36.147  1   35.22 ? 230 LEU   A CG  1 
ATOM   1776 C  CD1 . LEU   A 1 245 ? 2.772   31.937  35.56   1   35.57 ? 230 LEU   A CD1 1 
ATOM   1777 C  CD2 . LEU   A 1 245 ? 4.434   33.771  35.515  1   35.6  ? 230 LEU   A CD2 1 
ATOM   1778 N  N   . ARG   A 1 246 ? 5.496   30.171  39.166  1   34.34 ? 231 ARG   A N   1 
ATOM   1779 C  CA  . ARG   A 1 246 ? 6.485   29.102  39.198  1   34.09 ? 231 ARG   A CA  1 
ATOM   1780 C  C   . ARG   A 1 246 ? 5.821   27.732  39.5    1   33.4  ? 231 ARG   A C   1 
ATOM   1781 O  O   . ARG   A 1 246 ? 6.16    26.723  38.877  1   33.54 ? 231 ARG   A O   1 
ATOM   1782 C  CB  . ARG   A 1 246 ? 7.553   29.466  40.252  1   36.01 ? 231 ARG   A CB  1 
ATOM   1783 C  CG  . ARG   A 1 246 ? 8.674   28.476  40.439  1   40.66 ? 231 ARG   A CG  1 
ATOM   1784 C  CD  . ARG   A 1 246 ? 9.553   28.975  41.56   1   46.13 ? 231 ARG   A CD  1 
ATOM   1785 N  NE  . ARG   A 1 246 ? 9.803   27.93   42.54   1   51.34 ? 231 ARG   A NE  1 
ATOM   1786 C  CZ  . ARG   A 1 246 ? 9.172   27.804  43.702  1   54.54 ? 231 ARG   A CZ  1 
ATOM   1787 N  NH1 . ARG   A 1 246 ? 9.475   26.808  44.52   1   54.24 ? 231 ARG   A NH1 1 
ATOM   1788 N  NH2 . ARG   A 1 246 ? 8.252   28.685  44.066  1   54.74 ? 231 ARG   A NH2 1 
ATOM   1789 N  N   . ILE   A 1 247 ? 4.861   27.712  40.437  1   32.53 ? 232 ILE   A N   1 
ATOM   1790 C  CA  . ILE   A 1 247 ? 4.134   26.491  40.814  1   32.99 ? 232 ILE   A CA  1 
ATOM   1791 C  C   . ILE   A 1 247 ? 3.382   25.876  39.608  1   30.53 ? 232 ILE   A C   1 
ATOM   1792 O  O   . ILE   A 1 247 ? 3.436   24.658  39.392  1   29.94 ? 232 ILE   A O   1 
ATOM   1793 C  CB  . ILE   A 1 247 ? 3.137   26.816  41.966  1   35.34 ? 232 ILE   A CB  1 
ATOM   1794 C  CG1 . ILE   A 1 247 ? 3.844   27.291  43.249  1   36.87 ? 232 ILE   A CG1 1 
ATOM   1795 C  CG2 . ILE   A 1 247 ? 2.164   25.661  42.259  1   37.04 ? 232 ILE   A CG2 1 
ATOM   1796 C  CD1 . ILE   A 1 247 ? 5.091   26.583  43.708  1   39.05 ? 232 ILE   A CD1 1 
ATOM   1797 N  N   . TYR   A 1 248 ? 2.685   26.723  38.833  1   29.02 ? 233 TYR   A N   1 
ATOM   1798 C  CA  . TYR   A 1 248 ? 1.842   26.26   37.718  1   29.73 ? 233 TYR   A CA  1 
ATOM   1799 C  C   . TYR   A 1 248 ? 2.616   25.815  36.507  1   31.08 ? 233 TYR   A C   1 
ATOM   1800 O  O   . TYR   A 1 248 ? 2.114   24.995  35.725  1   31.8  ? 233 TYR   A O   1 
ATOM   1801 C  CB  . TYR   A 1 248 ? 0.782   27.308  37.324  1   29.62 ? 233 TYR   A CB  1 
ATOM   1802 C  CG  . TYR   A 1 248 ? -0.339  27.371  38.337  1   29.6  ? 233 TYR   A CG  1 
ATOM   1803 C  CD1 . TYR   A 1 248 ? -1.347  26.416  38.345  1   29.52 ? 233 TYR   A CD1 1 
ATOM   1804 C  CD2 . TYR   A 1 248 ? -0.317  28.3    39.372  1   29.79 ? 233 TYR   A CD2 1 
ATOM   1805 C  CE1 . TYR   A 1 248 ? -2.33   26.407  39.326  1   29.65 ? 233 TYR   A CE1 1 
ATOM   1806 C  CE2 . TYR   A 1 248 ? -1.288  28.288  40.371  1   29.7  ? 233 TYR   A CE2 1 
ATOM   1807 C  CZ  . TYR   A 1 248 ? -2.317  27.363  40.321  1   29.88 ? 233 TYR   A CZ  1 
ATOM   1808 O  OH  . TYR   A 1 248 ? -3.27   27.32   41.309  1   29.33 ? 233 TYR   A OH  1 
ATOM   1809 N  N   . LEU   A 1 249 ? 3.841   26.318  36.35   1   30.48 ? 234 LEU   A N   1 
ATOM   1810 C  CA  . LEU   A 1 249 ? 4.687   25.892  35.248  1   30.12 ? 234 LEU   A CA  1 
ATOM   1811 C  C   . LEU   A 1 249 ? 5.498   24.613  35.594  1   29.91 ? 234 LEU   A C   1 
ATOM   1812 O  O   . LEU   A 1 249 ? 6.154   24.077  34.716  1   29.6  ? 234 LEU   A O   1 
ATOM   1813 C  CB  . LEU   A 1 249 ? 5.591   27.039  34.78   1   29.32 ? 234 LEU   A CB  1 
ATOM   1814 C  CG  . LEU   A 1 249 ? 4.831   28.265  34.231  1   30.26 ? 234 LEU   A CG  1 
ATOM   1815 C  CD1 . LEU   A 1 249 ? 5.766   29.424  33.908  1   30.02 ? 234 LEU   A CD1 1 
ATOM   1816 C  CD2 . LEU   A 1 249 ? 4.002   27.912  32.995  1   31.43 ? 234 LEU   A CD2 1 
ATOM   1817 N  N   . SER   A 1 250 ? 5.476   24.138  36.861  1   30.32 ? 235 SER   A N   1 
ATOM   1818 C  CA  . SER   A 1 250 ? 6.214   22.931  37.226  1   31.12 ? 235 SER   A CA  1 
ATOM   1819 C  C   . SER   A 1 250 ? 5.696   21.719  36.489  1   31.47 ? 235 SER   A C   1 
ATOM   1820 O  O   . SER   A 1 250 ? 4.483   21.621  36.235  1   31.68 ? 235 SER   A O   1 
ATOM   1821 C  CB  . SER   A 1 250 ? 6.108   22.64   38.715  1   33.15 ? 235 SER   A CB  1 
ATOM   1822 O  OG  . SER   A 1 250 ? 6.444   23.806  39.438  1   37.17 ? 235 SER   A OG  1 
ATOM   1823 N  N   . GLY   A 1 251 ? 6.604   20.767  36.255  1   30.81 ? 236 GLY   A N   1 
ATOM   1824 C  CA  . GLY   A 1 251 ? 6.297   19.518  35.591  1   30.98 ? 236 GLY   A CA  1 
ATOM   1825 C  C   . GLY   A 1 251 ? 6.309   18.334  36.523  1   30.89 ? 236 GLY   A C   1 
ATOM   1826 O  O   . GLY   A 1 251 ? 6.224   18.477  37.744  1   30.62 ? 236 GLY   A O   1 
ATOM   1827 N  N   . TRP   A 1 252 ? 6.367   17.149  35.946  1   31.1  ? 237 TRP   A N   1 
ATOM   1828 C  CA  . TRP   A 1 252 ? 6.344   15.913  36.73   1   31.03 ? 237 TRP   A CA  1 
ATOM   1829 C  C   . TRP   A 1 252 ? 7.484   15.032  36.283  1   32.84 ? 237 TRP   A C   1 
ATOM   1830 O  O   . TRP   A 1 252 ? 7.271   13.9    35.886  1   33.73 ? 237 TRP   A O   1 
ATOM   1831 C  CB  . TRP   A 1 252 ? 4.971   15.173  36.667  1   29.06 ? 237 TRP   A CB  1 
ATOM   1832 C  CG  . TRP   A 1 252 ? 4.164   15.396  35.426  1   27.15 ? 237 TRP   A CG  1 
ATOM   1833 C  CD1 . TRP   A 1 252 ? 4.101   14.605  34.312  1   26.92 ? 237 TRP   A CD1 1 
ATOM   1834 C  CD2 . TRP   A 1 252 ? 3.278   16.494  35.193  1   25.96 ? 237 TRP   A CD2 1 
ATOM   1835 N  NE1 . TRP   A 1 252 ? 3.241   15.159  33.391  1   26.66 ? 237 TRP   A NE1 1 
ATOM   1836 C  CE2 . TRP   A 1 252 ? 2.747   16.338  33.897  1   26.27 ? 237 TRP   A CE2 1 
ATOM   1837 C  CE3 . TRP   A 1 252 ? 2.932   17.628  35.933  1   26.43 ? 237 TRP   A CE3 1 
ATOM   1838 C  CZ2 . TRP   A 1 252 ? 1.852   17.255  33.349  1   26.51 ? 237 TRP   A CZ2 1 
ATOM   1839 C  CZ3 . TRP   A 1 252 ? 2.031   18.523  35.39   1   27.32 ? 237 TRP   A CZ3 1 
ATOM   1840 C  CH2 . TRP   A 1 252 ? 1.531   18.354  34.103  1   26.58 ? 237 TRP   A CH2 1 
ATOM   1841 N  N   . LYS   A 1 253 ? 8.694   15.562  36.327  1   33.22 ? 238 LYS   A N   1 
ATOM   1842 C  CA  . LYS   A 1 253 ? 9.907   14.813  35.976  1   33.78 ? 238 LYS   A CA  1 
ATOM   1843 C  C   . LYS   A 1 253 ? 10.859  15.078  37.115  1   34.95 ? 238 LYS   A C   1 
ATOM   1844 O  O   . LYS   A 1 253 ? 11.179  16.236  37.388  1   35.3  ? 238 LYS   A O   1 
ATOM   1845 C  CB  . LYS   A 1 253 ? 10.51   15.266  34.647  1   34.42 ? 238 LYS   A CB  1 
ATOM   1846 C  CG  . LYS   A 1 253 ? 11.731  14.423  34.259  1   37.7  ? 238 LYS   A CG  1 
ATOM   1847 C  CD  . LYS   A 1 253 ? 11.969  14.416  32.773  1   43.73 ? 238 LYS   A CD  1 
ATOM   1848 C  CE  . LYS   A 1 253 ? 13.264  13.739  32.377  1   47.06 ? 238 LYS   A CE  1 
ATOM   1849 N  NZ  . LYS   A 1 253 ? 13.347  12.369  32.928  1   51.47 ? 238 LYS   A NZ  1 
ATOM   1850 N  N   . GLY   A 1 254 ? 11.211  14.039  37.857  1   35.42 ? 239 GLY   A N   1 
ATOM   1851 C  CA  . GLY   A 1 254 ? 12.05   14.199  39.036  1   36.63 ? 239 GLY   A CA  1 
ATOM   1852 C  C   . GLY   A 1 254 ? 11.366  15.057  40.091  1   37.85 ? 239 GLY   A C   1 
ATOM   1853 O  O   . GLY   A 1 254 ? 12.035  15.752  40.849  1   38.36 ? 239 GLY   A O   1 
ATOM   1854 N  N   . ASN   A 1 255 ? 10.013  15.048  40.124  1   38.01 ? 240 ASN   A N   1 
ATOM   1855 C  CA  . ASN   A 1 255 ? 9.258   15.865  41.074  1   38.26 ? 240 ASN   A CA  1 
ATOM   1856 C  C   . ASN   A 1 255 ? 8.748   14.973  42.168  1   39.73 ? 240 ASN   A C   1 
ATOM   1857 O  O   . ASN   A 1 255 ? 7.973   14.062  41.887  1   40.03 ? 240 ASN   A O   1 
ATOM   1858 C  CB  . ASN   A 1 255 ? 8.075   16.552  40.384  1   38.48 ? 240 ASN   A CB  1 
ATOM   1859 C  CG  . ASN   A 1 255 ? 7.42    17.624  41.236  1   40.69 ? 240 ASN   A CG  1 
ATOM   1860 O  OD1 . ASN   A 1 255 ? 7.375   17.533  42.476  1   42.76 ? 240 ASN   A OD1 1 
ATOM   1861 N  ND2 . ASN   A 1 255 ? 6.921   18.685  40.592  1   38.87 ? 240 ASN   A ND2 1 
ATOM   1862 N  N   . PRO   A 1 256 ? 9.131   15.23   43.425  1   40.32 ? 241 PRO   A N   1 
ATOM   1863 C  CA  . PRO   A 1 256 ? 8.651   14.377  44.53   1   40.67 ? 241 PRO   A CA  1 
ATOM   1864 C  C   . PRO   A 1 256 ? 7.132   14.367  44.697  1   41.07 ? 241 PRO   A C   1 
ATOM   1865 O  O   . PRO   A 1 256 ? 6.604   13.413  45.258  1   41.43 ? 241 PRO   A O   1 
ATOM   1866 C  CB  . PRO   A 1 256 ? 9.326   14.973  45.773  1   41.26 ? 241 PRO   A CB  1 
ATOM   1867 C  CG  . PRO   A 1 256 ? 10.476  15.782  45.237  1   42    ? 241 PRO   A CG  1 
ATOM   1868 C  CD  . PRO   A 1 256 ? 10.035  16.293  43.904  1   40.14 ? 241 PRO   A CD  1 
ATOM   1869 N  N   . GLN   A 1 257 ? 6.426   15.42   44.237  1   40.37 ? 242 GLN   A N   1 
ATOM   1870 C  CA  . GLN   A 1 257 ? 4.964   15.465  44.346  1   40.42 ? 242 GLN   A CA  1 
ATOM   1871 C  C   . GLN   A 1 257 ? 4.254   14.516  43.386  1   40.84 ? 242 GLN   A C   1 
ATOM   1872 O  O   . GLN   A 1 257 ? 3.093   14.215  43.611  1   41.8  ? 242 GLN   A O   1 
ATOM   1873 C  CB  . GLN   A 1 257 ? 4.433   16.884  44.152  1   40.84 ? 242 GLN   A CB  1 
ATOM   1874 C  CG  . GLN   A 1 257 ? 4.845   17.839  45.251  1   43.49 ? 242 GLN   A CG  1 
ATOM   1875 C  CD  . GLN   A 1 257 ? 4.247   19.195  44.976  1   47.18 ? 242 GLN   A CD  1 
ATOM   1876 O  OE1 . GLN   A 1 257 ? 4.488   19.795  43.924  1   50.32 ? 242 GLN   A OE1 1 
ATOM   1877 N  NE2 . GLN   A 1 257 ? 3.439   19.685  45.888  1   45.55 ? 242 GLN   A NE2 1 
ATOM   1878 N  N   . LEU   A 1 258 ? 4.919   14.093  42.3    1   40.19 ? 243 LEU   A N   1 
ATOM   1879 C  CA  . LEU   A 1 258 ? 4.373   13.147  41.314  1   40.77 ? 243 LEU   A CA  1 
ATOM   1880 C  C   . LEU   A 1 258 ? 5.544   12.264  40.902  1   40.3  ? 243 LEU   A C   1 
ATOM   1881 O  O   . LEU   A 1 258 ? 5.936   12.247  39.733  1   40.3  ? 243 LEU   A O   1 
ATOM   1882 C  CB  . LEU   A 1 258 ? 3.766   13.862  40.074  1   41.13 ? 243 LEU   A CB  1 
ATOM   1883 C  CG  . LEU   A 1 258 ? 2.375   14.439  40.229  1   42.79 ? 243 LEU   A CG  1 
ATOM   1884 C  CD1 . LEU   A 1 258 ? 2.459   15.893  40.505  1   43.15 ? 243 LEU   A CD1 1 
ATOM   1885 C  CD2 . LEU   A 1 258 ? 1.565   14.249  38.947  1   43.76 ? 243 LEU   A CD2 1 
ATOM   1886 N  N   . SER   A 1 259 ? 6.128   11.562  41.891  1   39.66 ? 244 SER   A N   1 
ATOM   1887 C  CA  . SER   A 1 259 ? 7.343   10.746  41.75   1   40.3  ? 244 SER   A CA  1 
ATOM   1888 C  C   . SER   A 1 259 ? 7.362   9.783   40.566  1   39.98 ? 244 SER   A C   1 
ATOM   1889 O  O   . SER   A 1 259 ? 8.443   9.462   40.09   1   40.3  ? 244 SER   A O   1 
ATOM   1890 C  CB  . SER   A 1 259 ? 7.648   9.987   43.039  1   42.46 ? 244 SER   A CB  1 
ATOM   1891 O  OG  . SER   A 1 259 ? 6.686   8.984   43.312  1   45.93 ? 244 SER   A OG  1 
ATOM   1892 N  N   . ASP   A 1 260 ? 6.202   9.34    40.07   1   39.55 ? 245 ASP   A N   1 
ATOM   1893 C  CA  . ASP   A 1 260 ? 6.182   8.419   38.919  1   39.52 ? 245 ASP   A CA  1 
ATOM   1894 C  C   . ASP   A 1 260 ? 5.683   9.04    37.616  1   38.15 ? 245 ASP   A C   1 
ATOM   1895 O  O   . ASP   A 1 260 ? 5.683   8.374   36.575  1   39.05 ? 245 ASP   A O   1 
ATOM   1896 C  CB  . ASP   A 1 260 ? 5.373   7.153   39.258  1   42.62 ? 245 ASP   A CB  1 
ATOM   1897 C  CG  . ASP   A 1 260 ? 5.849   6.501   40.547  1   49.34 ? 245 ASP   A CG  1 
ATOM   1898 O  OD1 . ASP   A 1 260 ? 6.959   5.918   40.542  1   51.01 ? 245 ASP   A OD1 1 
ATOM   1899 O  OD2 . ASP   A 1 260 ? 5.128   6.607   41.574  1   51.11 ? 245 ASP   A OD2 1 
ATOM   1900 N  N   . GLY   A 1 261 ? 5.298   10.305  37.661  1   35.98 ? 246 GLY   A N   1 
ATOM   1901 C  CA  . GLY   A 1 261 ? 4.746   10.971  36.502  1   35.09 ? 246 GLY   A CA  1 
ATOM   1902 C  C   . GLY   A 1 261 ? 3.237   11.113  36.629  1   34.34 ? 246 GLY   A C   1 
ATOM   1903 O  O   . GLY   A 1 261 ? 2.674   10.951  37.71   1   34.57 ? 246 GLY   A O   1 
ATOM   1904 N  N   . LEU   A 1 262 ? 2.582   11.424  35.532  1   33.12 ? 247 LEU   A N   1 
ATOM   1905 C  CA  . LEU   A 1 262 ? 1.153   11.636  35.484  1   32.56 ? 247 LEU   A CA  1 
ATOM   1906 C  C   . LEU   A 1 262 ? 0.535   10.522  34.662  1   32.93 ? 247 LEU   A C   1 
ATOM   1907 O  O   . LEU   A 1 262 ? 1.115   10.118  33.645  1   33.24 ? 247 LEU   A O   1 
ATOM   1908 C  CB  . LEU   A 1 262 ? 0.89    12.988  34.79   1   32.05 ? 247 LEU   A CB  1 
ATOM   1909 C  CG  . LEU   A 1 262 ? -0.549  13.484  34.755  1   32.09 ? 247 LEU   A CG  1 
ATOM   1910 C  CD1 . LEU   A 1 262 ? -1.021  13.828  36.131  1   32.28 ? 247 LEU   A CD1 1 
ATOM   1911 C  CD2 . LEU   A 1 262 ? -0.693  14.705  33.842  1   31.7  ? 247 LEU   A CD2 1 
ATOM   1912 N  N   . VAL   A 1 263 ? -0.635  10.027  35.088  1   32.97 ? 248 VAL   A N   1 
ATOM   1913 C  CA  . VAL   A 1 263 ? -1.344  9.035   34.308  1   32.66 ? 248 VAL   A CA  1 
ATOM   1914 C  C   . VAL   A 1 263 ? -2.174  9.774   33.288  1   31.94 ? 248 VAL   A C   1 
ATOM   1915 O  O   . VAL   A 1 263 ? -2.984  10.633  33.636  1   31.71 ? 248 VAL   A O   1 
ATOM   1916 C  CB  . VAL   A 1 263 ? -2.203  8.065   35.166  1   34    ? 248 VAL   A CB  1 
ATOM   1917 C  CG1 . VAL   A 1 263 ? -2.922  7.058   34.28   1   34.59 ? 248 VAL   A CG1 1 
ATOM   1918 C  CG2 . VAL   A 1 263 ? -1.344  7.351   36.205  1   34.06 ? 248 VAL   A CG2 1 
ATOM   1919 N  N   . TYR   A 1 264 ? -1.937  9.495   32.019  1   31.47 ? 249 TYR   A N   1 
ATOM   1920 C  CA  . TYR   A 1 264 ? -2.71   10.077  30.94   1   31.41 ? 249 TYR   A CA  1 
ATOM   1921 C  C   . TYR   A 1 264 ? -3.766  9.01    30.61   1   32.83 ? 249 TYR   A C   1 
ATOM   1922 O  O   . TYR   A 1 264 ? -3.583  8.199   29.701  1   33.07 ? 249 TYR   A O   1 
ATOM   1923 C  CB  . TYR   A 1 264 ? -1.807  10.371  29.738  1   30.65 ? 249 TYR   A CB  1 
ATOM   1924 C  CG  . TYR   A 1 264 ? -0.851  11.524  29.987  1   30.15 ? 249 TYR   A CG  1 
ATOM   1925 C  CD1 . TYR   A 1 264 ? 0.345   11.329  30.666  1   30.34 ? 249 TYR   A CD1 1 
ATOM   1926 C  CD2 . TYR   A 1 264 ? -1.183  12.816  29.621  1   30.66 ? 249 TYR   A CD2 1 
ATOM   1927 C  CE1 . TYR   A 1 264 ? 1.212   12.388  30.923  1   31.55 ? 249 TYR   A CE1 1 
ATOM   1928 C  CE2 . TYR   A 1 264 ? -0.329  13.882  29.878  1   31.63 ? 249 TYR   A CE2 1 
ATOM   1929 C  CZ  . TYR   A 1 264 ? 0.893   13.658  30.49   1   32.37 ? 249 TYR   A CZ  1 
ATOM   1930 O  OH  . TYR   A 1 264 ? 1.752   14.717  30.731  1   33.52 ? 249 TYR   A OH  1 
ATOM   1931 N  N   . GLU   A 1 265 ? -4.851  9.002   31.399  1   32.31 ? 250 GLU   A N   1 
ATOM   1932 C  CA  . GLU   A 1 265 ? -5.922  7.999   31.327  1   31.63 ? 250 GLU   A CA  1 
ATOM   1933 C  C   . GLU   A 1 265 ? -6.492  7.817   29.955  1   31.26 ? 250 GLU   A C   1 
ATOM   1934 O  O   . GLU   A 1 265 ? -6.866  8.783   29.296  1   30.61 ? 250 GLU   A O   1 
ATOM   1935 C  CB  . GLU   A 1 265 ? -7.013  8.365   32.316  1   34.13 ? 250 GLU   A CB  1 
ATOM   1936 C  CG  . GLU   A 1 265 ? -8.122  7.338   32.423  1   36.49 ? 250 GLU   A CG  1 
ATOM   1937 C  CD  . GLU   A 1 265 ? -9.128  7.804   33.433  1   38.61 ? 250 GLU   A CD  1 
ATOM   1938 O  OE1 . GLU   A 1 265 ? -9.887  8.741   33.103  1   37    ? 250 GLU   A OE1 1 
ATOM   1939 O  OE2 . GLU   A 1 265 ? -9.111  7.284   34.571  1   42.05 ? 250 GLU   A OE2 1 
ATOM   1940 N  N   . GLY   A 1 266 ? -6.513  6.573   29.507  1   32.61 ? 251 GLY   A N   1 
ATOM   1941 C  CA  . GLY   A 1 266 ? -7.044  6.205   28.205  1   33.86 ? 251 GLY   A CA  1 
ATOM   1942 C  C   . GLY   A 1 266 ? -6.063  6.316   27.057  1   35.56 ? 251 GLY   A C   1 
ATOM   1943 O  O   . GLY   A 1 266 ? -6.417  5.985   25.918  1   35.82 ? 251 GLY   A O   1 
ATOM   1944 N  N   . PHE   A 1 267 ? -4.819  6.791   27.331  1   36.03 ? 252 PHE   A N   1 
ATOM   1945 C  CA  . PHE   A 1 267 ? -3.805  6.943   26.276  1   36.52 ? 252 PHE   A CA  1 
ATOM   1946 C  C   . PHE   A 1 267 ? -2.614  6.04    26.533  1   38.01 ? 252 PHE   A C   1 
ATOM   1947 O  O   . PHE   A 1 267 ? -2.202  5.328   25.627  1   39.2  ? 252 PHE   A O   1 
ATOM   1948 C  CB  . PHE   A 1 267 ? -3.368  8.414   26.079  1   35.03 ? 252 PHE   A CB  1 
ATOM   1949 C  CG  . PHE   A 1 267 ? -2.77   8.636   24.711  1   34.66 ? 252 PHE   A CG  1 
ATOM   1950 C  CD1 . PHE   A 1 267 ? -3.576  8.923   23.626  1   34.96 ? 252 PHE   A CD1 1 
ATOM   1951 C  CD2 . PHE   A 1 267 ? -1.401  8.528   24.506  1   35.26 ? 252 PHE   A CD2 1 
ATOM   1952 C  CE1 . PHE   A 1 267 ? -3.029  9.104   22.362  1   35.66 ? 252 PHE   A CE1 1 
ATOM   1953 C  CE2 . PHE   A 1 267 ? -0.854  8.73    23.245  1   35.84 ? 252 PHE   A CE2 1 
ATOM   1954 C  CZ  . PHE   A 1 267 ? -1.672  9.006   22.182  1   35.49 ? 252 PHE   A CZ  1 
ATOM   1955 N  N   . TRP   A 1 268 ? -2.067  6.071   27.746  1   37.93 ? 253 TRP   A N   1 
ATOM   1956 C  CA  . TRP   A 1 268 ? -0.957  5.219   28.169  1   39.28 ? 253 TRP   A CA  1 
ATOM   1957 C  C   . TRP   A 1 268 ? -1.359  4.581   29.489  1   39.65 ? 253 TRP   A C   1 
ATOM   1958 O  O   . TRP   A 1 268 ? -2.032  5.22    30.308  1   39.28 ? 253 TRP   A O   1 
ATOM   1959 C  CB  . TRP   A 1 268 ? 0.36    6.009   28.395  1   39.78 ? 253 TRP   A CB  1 
ATOM   1960 C  CG  . TRP   A 1 268 ? 0.987   6.561   27.156  1   41.05 ? 253 TRP   A CG  1 
ATOM   1961 C  CD1 . TRP   A 1 268 ? 1.383   5.864   26.05   1   42.59 ? 253 TRP   A CD1 1 
ATOM   1962 C  CD2 . TRP   A 1 268 ? 1.354   7.926   26.923  1   41.12 ? 253 TRP   A CD2 1 
ATOM   1963 N  NE1 . TRP   A 1 268 ? 1.915   6.726   25.114  1   43.09 ? 253 TRP   A NE1 1 
ATOM   1964 C  CE2 . TRP   A 1 268 ? 1.923   7.997   25.634  1   42.37 ? 253 TRP   A CE2 1 
ATOM   1965 C  CE3 . TRP   A 1 268 ? 1.237   9.098   27.671  1   41.23 ? 253 TRP   A CE3 1 
ATOM   1966 C  CZ2 . TRP   A 1 268 ? 2.353   9.199   25.072  1   42.78 ? 253 TRP   A CZ2 1 
ATOM   1967 C  CZ3 . TRP   A 1 268 ? 1.674   10.282  27.12   1   42.61 ? 253 TRP   A CZ3 1 
ATOM   1968 C  CH2 . TRP   A 1 268 ? 2.232   10.326  25.839  1   42.8  ? 253 TRP   A CH2 1 
ATOM   1969 N  N   . GLU   A 1 269 ? -0.915  3.344   29.716  1   39.97 ? 254 GLU   A N   1 
ATOM   1970 C  CA  . GLU   A 1 269 ? -1.288  2.627   30.932  1   40.99 ? 254 GLU   A CA  1 
ATOM   1971 C  C   . GLU   A 1 269 ? -0.513  3.086   32.132  1   40.42 ? 254 GLU   A C   1 
ATOM   1972 O  O   . GLU   A 1 269 ? -1.089  3.252   33.217  1   40.72 ? 254 GLU   A O   1 
ATOM   1973 C  CB  . GLU   A 1 269 ? -1.077  1.116   30.741  1   44.34 ? 254 GLU   A CB  1 
ATOM   1974 C  CG  . GLU   A 1 269 ? -1.77   0.526   29.529  1   48.81 ? 254 GLU   A CG  1 
ATOM   1975 C  CD  . GLU   A 1 269 ? -1.758  -0.99   29.568  1   51.88 ? 254 GLU   A CD  1 
ATOM   1976 O  OE1 . GLU   A 1 269 ? -1.641  -1.611  28.483  1   53.65 ? 254 GLU   A OE1 1 
ATOM   1977 O  OE2 . GLU   A 1 269 ? -1.84   -1.551  30.688  1   50.64 ? 254 GLU   A OE2 1 
ATOM   1978 N  N   . ASP   A 1 270 ? 0.809   3.252   31.948  1   39.42 ? 255 ASP   A N   1 
ATOM   1979 C  CA  . ASP   A 1 270 ? 1.74    3.64    33.011  1   39.19 ? 255 ASP   A CA  1 
ATOM   1980 C  C   . ASP   A 1 270 ? 1.888   5.154   33.102  1   36.91 ? 255 ASP   A C   1 
ATOM   1981 O  O   . ASP   A 1 270 ? 1.798   5.838   32.083  1   36.48 ? 255 ASP   A O   1 
ATOM   1982 C  CB  . ASP   A 1 270 ? 3.116   3.005   32.723  1   43.3  ? 255 ASP   A CB  1 
ATOM   1983 C  CG  . ASP   A 1 270 ? 3.072   1.5     32.503  1   53.01 ? 255 ASP   A CG  1 
ATOM   1984 O  OD1 . ASP   A 1 270 ? 2.569   0.782   33.4    1   55.12 ? 255 ASP   A OD1 1 
ATOM   1985 O  OD2 . ASP   A 1 270 ? 3.541   1.04    31.432  1   56.2  ? 255 ASP   A OD2 1 
ATOM   1986 N  N   . PRO   A 1 271 ? 2.154   5.7     34.297  1   35.51 ? 256 PRO   A N   1 
ATOM   1987 C  CA  . PRO   A 1 271 ? 2.379   7.156   34.393  1   34.9  ? 256 PRO   A CA  1 
ATOM   1988 C  C   . PRO   A 1 271 ? 3.674   7.577   33.67   1   34.05 ? 256 PRO   A C   1 
ATOM   1989 O  O   . PRO   A 1 271 ? 4.633   6.802   33.616  1   34.58 ? 256 PRO   A O   1 
ATOM   1990 C  CB  . PRO   A 1 271 ? 2.442   7.422   35.899  1   35.79 ? 256 PRO   A CB  1 
ATOM   1991 C  CG  . PRO   A 1 271 ? 2.815   6.126   36.509  1   36.65 ? 256 PRO   A CG  1 
ATOM   1992 C  CD  . PRO   A 1 271 ? 2.296   5.031   35.603  1   34.99 ? 256 PRO   A CD  1 
ATOM   1993 N  N   . LYS   A 1 272 ? 3.677   8.773   33.056  1   31.94 ? 257 LYS   A N   1 
ATOM   1994 C  CA  . LYS   A 1 272 ? 4.804   9.28    32.288  1   31.49 ? 257 LYS   A CA  1 
ATOM   1995 C  C   . LYS   A 1 272 ? 5.314   10.584  32.866  1   31.91 ? 257 LYS   A C   1 
ATOM   1996 O  O   . LYS   A 1 272 ? 4.523   11.454  33.223  1   31.37 ? 257 LYS   A O   1 
ATOM   1997 C  CB  . LYS   A 1 272 ? 4.381   9.526   30.832  1   32.31 ? 257 LYS   A CB  1 
ATOM   1998 C  CG  . LYS   A 1 272 ? 3.705   8.35    30.159  1   37.21 ? 257 LYS   A CG  1 
ATOM   1999 C  CD  . LYS   A 1 272 ? 4.635   7.157   30.036  1   42.83 ? 257 LYS   A CD  1 
ATOM   2000 C  CE  . LYS   A 1 272 ? 4.037   6.104   29.148  1   47.8  ? 257 LYS   A CE  1 
ATOM   2001 N  NZ  . LYS   A 1 272 ? 4.957   4.952   28.948  1   52.43 ? 257 LYS   A NZ  1 
ATOM   2002 N  N   . GLU   A 1 273 ? 6.645   10.738  32.904  1   31.88 ? 258 GLU   A N   1 
ATOM   2003 C  CA  . GLU   A 1 273 ? 7.31    11.936  33.404  1   32.36 ? 258 GLU   A CA  1 
ATOM   2004 C  C   . GLU   A 1 273 ? 7.624   12.901  32.287  1   32.61 ? 258 GLU   A C   1 
ATOM   2005 O  O   . GLU   A 1 273 ? 8.211   12.498  31.283  1   33.36 ? 258 GLU   A O   1 
ATOM   2006 C  CB  . GLU   A 1 273 ? 8.611   11.533  34.093  1   35    ? 258 GLU   A CB  1 
ATOM   2007 C  CG  . GLU   A 1 273 ? 8.43    11.007  35.503  1   39.19 ? 258 GLU   A CG  1 
ATOM   2008 C  CD  . GLU   A 1 273 ? 9.753   10.792  36.219  1   41.01 ? 258 GLU   A CD  1 
ATOM   2009 O  OE1 . GLU   A 1 273 ? 10.492  9.863   35.824  1   43.28 ? 258 GLU   A OE1 1 
ATOM   2010 O  OE2 . GLU   A 1 273 ? 10.047  11.535  37.182  1   39.31 ? 258 GLU   A OE2 1 
ATOM   2011 N  N   . PHE   A 1 274 ? 7.252   14.185  32.447  1   32.2  ? 259 PHE   A N   1 
ATOM   2012 C  CA  . PHE   A 1 274 ? 7.6     15.246  31.487  1   31.76 ? 259 PHE   A CA  1 
ATOM   2013 C  C   . PHE   A 1 274 ? 8.052   16.495  32.271  1   32.05 ? 259 PHE   A C   1 
ATOM   2014 O  O   . PHE   A 1 274 ? 7.459   16.817  33.299  1   33.3  ? 259 PHE   A O   1 
ATOM   2015 C  CB  . PHE   A 1 274 ? 6.424   15.592  30.556  1   31.79 ? 259 PHE   A CB  1 
ATOM   2016 C  CG  . PHE   A 1 274 ? 6.043   14.478  29.608  1   31.89 ? 259 PHE   A CG  1 
ATOM   2017 C  CD1 . PHE   A 1 274 ? 6.867   14.138  28.547  1   32.24 ? 259 PHE   A CD1 1 
ATOM   2018 C  CD2 . PHE   A 1 274 ? 4.897   13.729  29.817  1   31.86 ? 259 PHE   A CD2 1 
ATOM   2019 C  CE1 . PHE   A 1 274 ? 6.505   13.122  27.662  1   32.26 ? 259 PHE   A CE1 1 
ATOM   2020 C  CE2 . PHE   A 1 274 ? 4.56    12.683  28.958  1   32.21 ? 259 PHE   A CE2 1 
ATOM   2021 C  CZ  . PHE   A 1 274 ? 5.371   12.377  27.896  1   31.85 ? 259 PHE   A CZ  1 
ATOM   2022 N  N   . ALA   A 1 275 ? 9.12    17.167  31.822  1   31.19 ? 260 ALA   A N   1 
ATOM   2023 C  CA  . ALA   A 1 275 ? 9.646   18.375  32.484  1   29.67 ? 260 ALA   A CA  1 
ATOM   2024 C  C   . ALA   A 1 275 ? 8.672   19.542  32.275  1   28.36 ? 260 ALA   A C   1 
ATOM   2025 O  O   . ALA   A 1 275 ? 7.985   19.605  31.256  1   27.62 ? 260 ALA   A O   1 
ATOM   2026 C  CB  . ALA   A 1 275 ? 11.034  18.736  31.91   1   29.59 ? 260 ALA   A CB  1 
ATOM   2027 N  N   . GLY   A 1 276 ? 8.652   20.469  33.218  1   27.68 ? 261 GLY   A N   1 
ATOM   2028 C  CA  . GLY   A 1 276 ? 7.758   21.618  33.123  1   27.96 ? 261 GLY   A CA  1 
ATOM   2029 C  C   . GLY   A 1 276 ? 8.212   22.655  32.111  1   28.62 ? 261 GLY   A C   1 
ATOM   2030 O  O   . GLY   A 1 276 ? 9.353   22.604  31.644  1   28.68 ? 261 GLY   A O   1 
ATOM   2031 N  N   . GLY   A 1 277 ? 7.331   23.598  31.778  1   27.96 ? 262 GLY   A N   1 
ATOM   2032 C  CA  . GLY   A 1 277 ? 7.597   24.671  30.821  1   28.23 ? 262 GLY   A CA  1 
ATOM   2033 C  C   . GLY   A 1 277 ? 8.853   25.433  31.19   1   29.42 ? 262 GLY   A C   1 
ATOM   2034 O  O   . GLY   A 1 277 ? 9.105   25.706  32.384  1   30.77 ? 262 GLY   A O   1 
ATOM   2035 N  N   . SER   A 1 278 ? 9.731   25.605  30.206  1   28.26 ? 263 SER   A N   1 
ATOM   2036 C  CA  . SER   A 1 278 ? 11.035  26.191  30.473  1   27.48 ? 263 SER   A CA  1 
ATOM   2037 C  C   . SER   A 1 278 ? 11.607  26.933  29.306  1   26.73 ? 263 SER   A C   1 
ATOM   2038 O  O   . SER   A 1 278 ? 11.585  26.418  28.187  1   25.73 ? 263 SER   A O   1 
ATOM   2039 C  CB  . SER   A 1 278 ? 12.013  25.09   30.899  1   29.22 ? 263 SER   A CB  1 
ATOM   2040 O  OG  . SER   A 1 278 ? 13.372  25.5    31.028  1   31.39 ? 263 SER   A OG  1 
ATOM   2041 N  N   . ALA   A 1 279 ? 12.26   28.078  29.567  1   26.78 ? 264 ALA   A N   1 
ATOM   2042 C  CA  . ALA   A 1 279 ? 12.966  28.768  28.467  1   27.21 ? 264 ALA   A CA  1 
ATOM   2043 C  C   . ALA   A 1 279 ? 14.221  27.979  27.975  1   28.44 ? 264 ALA   A C   1 
ATOM   2044 O  O   . ALA   A 1 279 ? 14.796  28.309  26.938  1   28.17 ? 264 ALA   A O   1 
ATOM   2045 C  CB  . ALA   A 1 279 ? 13.319  30.18   28.848  1   26.6  ? 264 ALA   A CB  1 
ATOM   2046 N  N   . GLY   A 1 280 ? 14.583  26.889  28.662  1   29.22 ? 265 GLY   A N   1 
ATOM   2047 C  CA  . GLY   A 1 280 ? 15.579  25.949  28.164  1   29.27 ? 265 GLY   A CA  1 
ATOM   2048 C  C   . GLY   A 1 280 ? 15.064  25.261  26.886  1   28.94 ? 265 GLY   A C   1 
ATOM   2049 O  O   . GLY   A 1 280 ? 15.855  24.738  26.097  1   29.12 ? 265 GLY   A O   1 
ATOM   2050 N  N   . GLN   A 1 281 ? 13.728  25.272  26.67   1   28.1  ? 266 GLN   A N   1 
ATOM   2051 C  CA  . GLN   A 1 281 ? 13.028  24.778  25.478  1   28.18 ? 266 GLN   A CA  1 
ATOM   2052 C  C   . GLN   A 1 281 ? 13.033  25.816  24.338  1   29.23 ? 266 GLN   A C   1 
ATOM   2053 O  O   . GLN   A 1 281 ? 12.624  25.497  23.219  1   30.19 ? 266 GLN   A O   1 
ATOM   2054 C  CB  . GLN   A 1 281 ? 11.57   24.408  25.828  1   26.59 ? 266 GLN   A CB  1 
ATOM   2055 C  CG  . GLN   A 1 281 ? 11.519  23.36   26.927  1   26.35 ? 266 GLN   A CG  1 
ATOM   2056 C  CD  . GLN   A 1 281 ? 10.189  23.233  27.607  1   26.21 ? 266 GLN   A CD  1 
ATOM   2057 O  OE1 . GLN   A 1 281 ? 9.323   24.113  27.519  1   24.3  ? 266 GLN   A OE1 1 
ATOM   2058 N  NE2 . GLN   A 1 281 ? 10.027  22.159  28.385  1   26.65 ? 266 GLN   A NE2 1 
ATOM   2059 N  N   . SER   A 1 282 ? 13.42   27.062  24.62   1   28.92 ? 267 SER   A N   1 
ATOM   2060 C  CA  . SER   A 1 282 ? 13.456  28.115  23.636  1   29.58 ? 267 SER   A CA  1 
ATOM   2061 C  C   . SER   A 1 282 ? 14.561  27.93   22.615  1   29.03 ? 267 SER   A C   1 
ATOM   2062 O  O   . SER   A 1 282 ? 15.565  27.304  22.886  1   28.47 ? 267 SER   A O   1 
ATOM   2063 C  CB  . SER   A 1 282 ? 13.628  29.453  24.336  1   33.47 ? 267 SER   A CB  1 
ATOM   2064 O  OG  . SER   A 1 282 ? 13.674  30.506  23.391  1   39.78 ? 267 SER   A OG  1 
ATOM   2065 N  N   . SER   A 1 283 ? 14.35   28.441  21.414  1   29.37 ? 268 SER   A N   1 
ATOM   2066 C  CA  . SER   A 1 283 ? 15.33   28.396  20.335  1   30.54 ? 268 SER   A CA  1 
ATOM   2067 C  C   . SER   A 1 283 ? 16.06   29.752  20.148  1   31.49 ? 268 SER   A C   1 
ATOM   2068 O  O   . SER   A 1 283 ? 17.034  29.807  19.415  1   31.7  ? 268 SER   A O   1 
ATOM   2069 C  CB  . SER   A 1 283 ? 14.618  28.114  19.021  1   31.64 ? 268 SER   A CB  1 
ATOM   2070 O  OG  . SER   A 1 283 ? 13.942  26.873  19.016  1   35.96 ? 268 SER   A OG  1 
ATOM   2071 N  N   . VAL   A 1 284 ? 15.55   30.829  20.76   1   31.77 ? 269 VAL   A N   1 
ATOM   2072 C  CA  . VAL   A 1 284 ? 15.981  32.201  20.573  1   33.25 ? 269 VAL   A CA  1 
ATOM   2073 C  C   . VAL   A 1 284 ? 17.473  32.424  20.777  1   35.16 ? 269 VAL   A C   1 
ATOM   2074 O  O   . VAL   A 1 284 ? 18.085  32.963  19.865  1   37.65 ? 269 VAL   A O   1 
ATOM   2075 C  CB  . VAL   A 1 284 ? 15.146  33.19   21.399  1   33.25 ? 269 VAL   A CB  1 
ATOM   2076 C  CG1 . VAL   A 1 284 ? 15.425  33.084  22.907  1   33.52 ? 269 VAL   A CG1 1 
ATOM   2077 C  CG2 . VAL   A 1 284 ? 15.354  34.591  20.908  1   33.97 ? 269 VAL   A CG2 1 
ATOM   2078 N  N   . PHE   A 1 285 ? 18.065  32.07   21.941  1   34.05 ? 270 PHE   A N   1 
ATOM   2079 C  CA  . PHE   A 1 285 ? 19.512  32.263  22.132  1   33.04 ? 270 PHE   A CA  1 
ATOM   2080 C  C   . PHE   A 1 285 ? 20.273  31.024  21.604  1   32.88 ? 270 PHE   A C   1 
ATOM   2081 O  O   . PHE   A 1 285 ? 21.404  31.154  21.125  1   33.34 ? 270 PHE   A O   1 
ATOM   2082 C  CB  . PHE   A 1 285 ? 19.857  32.482  23.621  1   33    ? 270 PHE   A CB  1 
ATOM   2083 C  CG  . PHE   A 1 285 ? 19.374  33.751  24.29   1   33.83 ? 270 PHE   A CG  1 
ATOM   2084 C  CD1 . PHE   A 1 285 ? 18.784  34.761  23.551  1   34.76 ? 270 PHE   A CD1 1 
ATOM   2085 C  CD2 . PHE   A 1 285 ? 19.536  33.936  25.654  1   34.53 ? 270 PHE   A CD2 1 
ATOM   2086 C  CE1 . PHE   A 1 285 ? 18.319  35.908  24.166  1   35.76 ? 270 PHE   A CE1 1 
ATOM   2087 C  CE2 . PHE   A 1 285 ? 19.069  35.076  26.274  1   35.64 ? 270 PHE   A CE2 1 
ATOM   2088 C  CZ  . PHE   A 1 285 ? 18.471  36.067  25.521  1   35.65 ? 270 PHE   A CZ  1 
ATOM   2089 N  N   . GLN   A 1 286 ? 19.656  29.836  21.681  1   31.62 ? 271 GLN   A N   1 
ATOM   2090 C  CA  . GLN   A 1 286 ? 20.22   28.579  21.239  1   32.19 ? 271 GLN   A CA  1 
ATOM   2091 C  C   . GLN   A 1 286 ? 20.652  28.585  19.772  1   32.86 ? 271 GLN   A C   1 
ATOM   2092 O  O   . GLN   A 1 286 ? 21.737  28.095  19.485  1   32.33 ? 271 GLN   A O   1 
ATOM   2093 C  CB  . GLN   A 1 286 ? 19.257  27.437  21.544  1   34.68 ? 271 GLN   A CB  1 
ATOM   2094 C  CG  . GLN   A 1 286 ? 19.83   26.083  21.251  1   37.46 ? 271 GLN   A CG  1 
ATOM   2095 C  CD  . GLN   A 1 286 ? 19.189  24.93   22.01   1   39.05 ? 271 GLN   A CD  1 
ATOM   2096 O  OE1 . GLN   A 1 286 ? 19.717  23.817  21.993  1   38.81 ? 271 GLN   A OE1 1 
ATOM   2097 N  NE2 . GLN   A 1 286 ? 18.076  25.14   22.682  1   38.16 ? 271 GLN   A NE2 1 
ATOM   2098 N  N   . CYS   A 1 287 ? 19.889  29.23   18.859  1   32.76 ? 272 CYS   A N   1 
ATOM   2099 C  CA  . CYS   A 1 287 ? 20.327  29.287  17.455  1   32.38 ? 272 CYS   A CA  1 
ATOM   2100 C  C   . CYS   A 1 287 ? 21.587  30.151  17.28   1   31.8  ? 272 CYS   A C   1 
ATOM   2101 O  O   . CYS   A 1 287 ? 22.346  29.912  16.349  1   31.24 ? 272 CYS   A O   1 
ATOM   2102 C  CB  . CYS   A 1 287 ? 19.207  29.712  16.516  1   33.65 ? 272 CYS   A CB  1 
ATOM   2103 S  SG  . CYS   A 1 287 ? 18.772  31.46   16.635  1   41.07 ? 272 CYS   A SG  1 
ATOM   2104 N  N   . PHE   A 1 288 ? 21.816  31.128  18.184  1   30.78 ? 273 PHE   A N   1 
ATOM   2105 C  CA  . PHE   A 1 288 ? 23.022  31.939  18.153  1   30.98 ? 273 PHE   A CA  1 
ATOM   2106 C  C   . PHE   A 1 288 ? 24.187  31.185  18.788  1   31.86 ? 273 PHE   A C   1 
ATOM   2107 O  O   . PHE   A 1 288 ? 25.302  31.289  18.296  1   32.68 ? 273 PHE   A O   1 
ATOM   2108 C  CB  . PHE   A 1 288 ? 22.797  33.328  18.762  1   31.13 ? 273 PHE   A CB  1 
ATOM   2109 C  CG  . PHE   A 1 288 ? 21.857  34.102  17.884  1   32.06 ? 273 PHE   A CG  1 
ATOM   2110 C  CD1 . PHE   A 1 288 ? 22.236  34.487  16.611  1   33.06 ? 273 PHE   A CD1 1 
ATOM   2111 C  CD2 . PHE   A 1 288 ? 20.555  34.335  18.277  1   33.01 ? 273 PHE   A CD2 1 
ATOM   2112 C  CE1 . PHE   A 1 288 ? 21.338  35.133  15.764  1   33.31 ? 273 PHE   A CE1 1 
ATOM   2113 C  CE2 . PHE   A 1 288 ? 19.673  35.014  17.452  1   34.1  ? 273 PHE   A CE2 1 
ATOM   2114 C  CZ  . PHE   A 1 288 ? 20.064  35.387  16.182  1   33.66 ? 273 PHE   A CZ  1 
ATOM   2115 N  N   . ASP   A 1 289 ? 23.935  30.341  19.804  1   31.46 ? 274 ASP   A N   1 
ATOM   2116 C  CA  . ASP   A 1 289 ? 24.96   29.458  20.343  1   31.84 ? 274 ASP   A CA  1 
ATOM   2117 C  C   . ASP   A 1 289 ? 25.419  28.474  19.246  1   32.19 ? 274 ASP   A C   1 
ATOM   2118 O  O   . ASP   A 1 289 ? 26.616  28.243  19.079  1   32.48 ? 274 ASP   A O   1 
ATOM   2119 C  CB  . ASP   A 1 289 ? 24.417  28.667  21.521  1   33.66 ? 274 ASP   A CB  1 
ATOM   2120 C  CG  . ASP   A 1 289 ? 24.196  29.487  22.781  1   40.47 ? 274 ASP   A CG  1 
ATOM   2121 O  OD1 . ASP   A 1 289 ? 25.133  30.209  23.2    1   42    ? 274 ASP   A OD1 1 
ATOM   2122 O  OD2 . ASP   A 1 289 ? 23.113  29.362  23.382  1   43.18 ? 274 ASP   A OD2 1 
ATOM   2123 N  N   . VAL   A 1 290 ? 24.467  27.939  18.469  1   31.64 ? 275 VAL   A N   1 
ATOM   2124 C  CA  . VAL   A 1 290 ? 24.81   27.019  17.389  1   31.16 ? 275 VAL   A CA  1 
ATOM   2125 C  C   . VAL   A 1 290 ? 25.545  27.759  16.276  1   30.64 ? 275 VAL   A C   1 
ATOM   2126 O  O   . VAL   A 1 290 ? 26.619  27.327  15.875  1   29.96 ? 275 VAL   A O   1 
ATOM   2127 C  CB  . VAL   A 1 290 ? 23.593  26.193  16.893  1   32.12 ? 275 VAL   A CB  1 
ATOM   2128 C  CG1 . VAL   A 1 290 ? 23.993  25.314  15.727  1   33.08 ? 275 VAL   A CG1 1 
ATOM   2129 C  CG2 . VAL   A 1 290 ? 23.024  25.342  18.032  1   31.66 ? 275 VAL   A CG2 1 
ATOM   2130 N  N   . LEU   A 1 291 ? 25.024  28.916  15.845  1   31.48 ? 276 LEU   A N   1 
ATOM   2131 C  CA  . LEU   A 1 291 ? 25.636  29.726  14.791  1   31.74 ? 276 LEU   A CA  1 
ATOM   2132 C  C   . LEU   A 1 291 ? 27.094  30.091  15.132  1   31    ? 276 LEU   A C   1 
ATOM   2133 O  O   . LEU   A 1 291 ? 27.968  29.948  14.292  1   31    ? 276 LEU   A O   1 
ATOM   2134 C  CB  . LEU   A 1 291 ? 24.818  31.01   14.553  1   31.95 ? 276 LEU   A CB  1 
ATOM   2135 C  CG  . LEU   A 1 291 ? 25.387  31.999  13.536  1   34.01 ? 276 LEU   A CG  1 
ATOM   2136 C  CD1 . LEU   A 1 291 ? 25.096  31.533  12.145  1   35.52 ? 276 LEU   A CD1 1 
ATOM   2137 C  CD2 . LEU   A 1 291 ? 24.79   33.388  13.712  1   34.74 ? 276 LEU   A CD2 1 
ATOM   2138 N  N   . LEU   A 1 292 ? 27.367  30.518  16.377  1   30.29 ? 277 LEU   A N   1 
ATOM   2139 C  CA  . LEU   A 1 292 ? 28.697  30.973  16.784  1   29.39 ? 277 LEU   A CA  1 
ATOM   2140 C  C   . LEU   A 1 292 ? 29.649  29.873  17.318  1   30.48 ? 277 LEU   A C   1 
ATOM   2141 O  O   . LEU   A 1 292 ? 30.74   30.183  17.786  1   31.9  ? 277 LEU   A O   1 
ATOM   2142 C  CB  . LEU   A 1 292 ? 28.53   32.069  17.859  1   28.27 ? 277 LEU   A CB  1 
ATOM   2143 C  CG  . LEU   A 1 292 ? 27.669  33.271  17.443  1   28.73 ? 277 LEU   A CG  1 
ATOM   2144 C  CD1 . LEU   A 1 292 ? 27.488  34.219  18.574  1   28.76 ? 277 LEU   A CD1 1 
ATOM   2145 C  CD2 . LEU   A 1 292 ? 28.248  33.991  16.223  1   29.27 ? 277 LEU   A CD2 1 
ATOM   2146 N  N   . GLY   A 1 293 ? 29.218  28.626  17.293  1   29.91 ? 278 GLY   A N   1 
ATOM   2147 C  CA  . GLY   A 1 293 ? 30.027  27.521  17.771  1   30.5  ? 278 GLY   A CA  1 
ATOM   2148 C  C   . GLY   A 1 293 ? 30.216  27.487  19.27   1   31    ? 278 GLY   A C   1 
ATOM   2149 O  O   . GLY   A 1 293 ? 31.216  26.969  19.744  1   31.07 ? 278 GLY   A O   1 
ATOM   2150 N  N   . ILE   A 1 294 ? 29.286  28.075  20.034  1   32.01 ? 279 ILE   A N   1 
ATOM   2151 C  CA  . ILE   A 1 294 ? 29.348  28.013  21.494  1   33.37 ? 279 ILE   A CA  1 
ATOM   2152 C  C   . ILE   A 1 294 ? 28.717  26.671  21.792  1   36.71 ? 279 ILE   A C   1 
ATOM   2153 O  O   . ILE   A 1 294 ? 27.51   26.5    21.581  1   39.34 ? 279 ILE   A O   1 
ATOM   2154 C  CB  . ILE   A 1 294 ? 28.558  29.179  22.097  1   32.85 ? 279 ILE   A CB  1 
ATOM   2155 C  CG1 . ILE   A 1 294 ? 29.162  30.504  21.616  1   34.4  ? 279 ILE   A CG1 1 
ATOM   2156 C  CG2 . ILE   A 1 294 ? 28.577  29.093  23.613  1   31.81 ? 279 ILE   A CG2 1 
ATOM   2157 C  CD1 . ILE   A 1 294 ? 28.269  31.64   21.74   1   35.76 ? 279 ILE   A CD1 1 
ATOM   2158 N  N   . GLN   A 1 295 ? 29.511  25.701  22.194  1   36.93 ? 280 GLN   A N   1 
ATOM   2159 C  CA  . GLN   A 1 295 ? 29.033  24.325  22.33   1   37.72 ? 280 GLN   A CA  1 
ATOM   2160 C  C   . GLN   A 1 295 ? 28.321  24.059  23.629  1   37.34 ? 280 GLN   A C   1 
ATOM   2161 O  O   . GLN   A 1 295 ? 28.81   23.298  24.467  1   37.3  ? 280 GLN   A O   1 
ATOM   2162 C  CB  . GLN   A 1 295 ? 30.214  23.359  22.112  1   40.55 ? 280 GLN   A CB  1 
ATOM   2163 C  CG  . GLN   A 1 295 ? 30.857  23.564  20.75   1   46.53 ? 280 GLN   A CG  1 
ATOM   2164 C  CD  . GLN   A 1 295 ? 31.571  22.342  20.254  1   57    ? 280 GLN   A CD  1 
ATOM   2165 O  OE1 . GLN   A 1 295 ? 31.451  21.96   19.08   1   61.08 ? 280 GLN   A OE1 1 
ATOM   2166 N  NE2 . GLN   A 1 295 ? 32.322  21.673  21.134  1   58    ? 280 GLN   A NE2 1 
ATOM   2167 N  N   . GLN   A 1 296 ? 27.133  24.662  23.785  1   36.6  ? 281 GLN   A N   1 
ATOM   2168 C  CA  . GLN   A 1 296 ? 26.323  24.522  24.992  1   36.13 ? 281 GLN   A CA  1 
ATOM   2169 C  C   . GLN   A 1 296 ? 25.893  23.072  25.254  1   37.47 ? 281 GLN   A C   1 
ATOM   2170 O  O   . GLN   A 1 296 ? 25.784  22.667  26.413  1   37.88 ? 281 GLN   A O   1 
ATOM   2171 C  CB  . GLN   A 1 296 ? 25.086  25.435  24.915  1   34.58 ? 281 GLN   A CB  1 
ATOM   2172 C  CG  . GLN   A 1 296 ? 25.39   26.918  24.756  1   32.35 ? 281 GLN   A CG  1 
ATOM   2173 C  CD  . GLN   A 1 296 ? 25.983  27.553  26.002  1   32.65 ? 281 GLN   A CD  1 
ATOM   2174 O  OE1 . GLN   A 1 296 ? 26.238  26.903  27.019  1   32.55 ? 281 GLN   A OE1 1 
ATOM   2175 N  NE2 . GLN   A 1 296 ? 26.132  28.857  25.975  1   32.56 ? 281 GLN   A NE2 1 
ATOM   2176 N  N   . THR   A 1 297 ? 25.686  22.3    24.182  1   37.8  ? 282 THR   A N   1 
ATOM   2177 C  CA  . THR   A 1 297 ? 25.23   20.914  24.249  1   40.12 ? 282 THR   A CA  1 
ATOM   2178 C  C   . THR   A 1 297 ? 26.347  19.86   24.18   1   42.53 ? 282 THR   A C   1 
ATOM   2179 O  O   . THR   A 1 297 ? 26.045  18.662  24.189  1   44.09 ? 282 THR   A O   1 
ATOM   2180 C  CB  . THR   A 1 297 ? 24.175  20.664  23.187  1   41.23 ? 282 THR   A CB  1 
ATOM   2181 O  OG1 . THR   A 1 297 ? 24.616  21.187  21.925  1   42.75 ? 282 THR   A OG1 1 
ATOM   2182 C  CG2 . THR   A 1 297 ? 22.839  21.277  23.564  1   41.73 ? 282 THR   A CG2 1 
ATOM   2183 N  N   . ALA   A 1 298 ? 27.621  20.283  24.16   1   42.84 ? 283 ALA   A N   1 
ATOM   2184 C  CA  . ALA   A 1 298 ? 28.731  19.336  24.125  1   43.48 ? 283 ALA   A CA  1 
ATOM   2185 C  C   . ALA   A 1 298 ? 29.058  18.801  25.512  1   44.13 ? 283 ALA   A C   1 
ATOM   2186 O  O   . ALA   A 1 298 ? 28.969  19.521  26.511  1   43.26 ? 283 ALA   A O   1 
ATOM   2187 C  CB  . ALA   A 1 298 ? 29.965  19.982  23.51   1   43.47 ? 283 ALA   A CB  1 
ATOM   2188 N  N   . GLY   A 1 299 ? 29.416  17.521  25.558  1   45.29 ? 284 GLY   A N   1 
ATOM   2189 C  CA  . GLY   A 1 299 ? 29.8    16.88   26.807  1   46.3  ? 284 GLY   A CA  1 
ATOM   2190 C  C   . GLY   A 1 299 ? 28.675  16.209  27.57   1   47.22 ? 284 GLY   A C   1 
ATOM   2191 O  O   . GLY   A 1 299 ? 27.508  16.202  27.144  1   47.43 ? 284 GLY   A O   1 
ATOM   2192 N  N   . GLY   A 1 300 ? 29.042  15.66   28.709  1   46.93 ? 285 GLY   A N   1 
ATOM   2193 C  CA  . GLY   A 1 300 ? 28.082  14.956  29.533  1   46.98 ? 285 GLY   A CA  1 
ATOM   2194 C  C   . GLY   A 1 300 ? 27.627  15.709  30.757  1   46.34 ? 285 GLY   A C   1 
ATOM   2195 O  O   . GLY   A 1 300 ? 27.031  15.092  31.645  1   47.12 ? 285 GLY   A O   1 
ATOM   2196 N  N   . GLY   A 1 301 ? 27.867  17.032  30.803  1   44.16 ? 286 GLY   A N   1 
ATOM   2197 C  CA  . GLY   A 1 301 ? 27.464  17.849  31.947  1   42.12 ? 286 GLY   A CA  1 
ATOM   2198 C  C   . GLY   A 1 301 ? 25.96   18.018  32.088  1   39.59 ? 286 GLY   A C   1 
ATOM   2199 O  O   . GLY   A 1 301 ? 25.203  17.728  31.158  1   37.75 ? 286 GLY   A O   1 
ATOM   2200 N  N   . HIS   A 1 302 ? 25.515  18.479  33.246  1   39.01 ? 287 HIS   A N   1 
ATOM   2201 C  CA  . HIS   A 1 302 ? 24.095  18.676  33.498  1   38.91 ? 287 HIS   A CA  1 
ATOM   2202 C  C   . HIS   A 1 302 ? 23.495  19.711  32.564  1   36.29 ? 287 HIS   A C   1 
ATOM   2203 O  O   . HIS   A 1 302 ? 22.46   19.444  31.962  1   35.75 ? 287 HIS   A O   1 
ATOM   2204 C  CB  . HIS   A 1 302 ? 23.872  19.089  34.947  1   42.38 ? 287 HIS   A CB  1 
ATOM   2205 C  CG  . HIS   A 1 302 ? 24.403  18.087  35.91   1   49.45 ? 287 HIS   A CG  1 
ATOM   2206 N  ND1 . HIS   A 1 302 ? 25.548  18.338  36.653  1   53.13 ? 287 HIS   A ND1 1 
ATOM   2207 C  CD2 . HIS   A 1 302 ? 23.952  16.842  36.199  1   51.54 ? 287 HIS   A CD2 1 
ATOM   2208 C  CE1 . HIS   A 1 302 ? 25.741  17.251  37.389  1   53.88 ? 287 HIS   A CE1 1 
ATOM   2209 N  NE2 . HIS   A 1 302 ? 24.811  16.319  37.141  1   53.4  ? 287 HIS   A NE2 1 
ATOM   2210 N  N   . ALA   A 1 303 ? 24.19   20.858  32.371  1   34.43 ? 288 ALA   A N   1 
ATOM   2211 C  CA  . ALA   A 1 303 ? 23.672  21.941  31.541  1   32.8  ? 288 ALA   A CA  1 
ATOM   2212 C  C   . ALA   A 1 303 ? 23.468  21.462  30.11   1   31.25 ? 288 ALA   A C   1 
ATOM   2213 O  O   . ALA   A 1 303 ? 22.384  21.628  29.552  1   30.75 ? 288 ALA   A O   1 
ATOM   2214 C  CB  . ALA   A 1 303 ? 24.615  23.157  31.6    1   32.71 ? 288 ALA   A CB  1 
ATOM   2215 N  N   . ALA   A 1 304 ? 24.458  20.756  29.572  1   30.12 ? 289 ALA   A N   1 
ATOM   2216 C  CA  . ALA   A 1 304 ? 24.429  20.239  28.214  1   28.8  ? 289 ALA   A CA  1 
ATOM   2217 C  C   . ALA   A 1 304 ? 23.341  19.2    28.078  1   28.08 ? 289 ALA   A C   1 
ATOM   2218 O  O   . ALA   A 1 304 ? 22.615  19.224  27.096  1   27.95 ? 289 ALA   A O   1 
ATOM   2219 C  CB  . ALA   A 1 304 ? 25.786  19.614  27.862  1   28.88 ? 289 ALA   A CB  1 
ATOM   2220 N  N   . GLN   A 1 305 ? 23.196  18.287  29.062  1   27.47 ? 290 GLN   A N   1 
ATOM   2221 C  CA  . GLN   A 1 305 ? 22.168  17.252  28.955  1   27.11 ? 290 GLN   A CA  1 
ATOM   2222 C  C   . GLN   A 1 305 ? 20.758  17.904  28.955  1   28.41 ? 290 GLN   A C   1 
ATOM   2223 O  O   . GLN   A 1 305 ? 19.894  17.521  28.166  1   28.57 ? 290 GLN   A O   1 
ATOM   2224 C  CB  . GLN   A 1 305 ? 22.311  16.253  30.118  1   27.8  ? 290 GLN   A CB  1 
ATOM   2225 C  CG  . GLN   A 1 305 ? 21.297  15.097  30.032  1   30.46 ? 290 GLN   A CG  1 
ATOM   2226 C  CD  . GLN   A 1 305 ? 21.659  14.123  28.938  1   34.52 ? 290 GLN   A CD  1 
ATOM   2227 O  OE1 . GLN   A 1 305 ? 22.804  13.719  28.803  1   34.33 ? 290 GLN   A OE1 1 
ATOM   2228 N  NE2 . GLN   A 1 305 ? 20.693  13.738  28.116  1   37.35 ? 290 GLN   A NE2 1 
ATOM   2229 N  N   . PHE   A 1 306 ? 20.548  18.906  29.82   1   28.39 ? 291 PHE   A N   1 
ATOM   2230 C  CA  . PHE   A 1 306 ? 19.275  19.592  29.942  1   28.12 ? 291 PHE   A CA  1 
ATOM   2231 C  C   . PHE   A 1 306 ? 18.932  20.328  28.668  1   28.09 ? 291 PHE   A C   1 
ATOM   2232 O  O   . PHE   A 1 306 ? 17.815  20.174  28.196  1   28.02 ? 291 PHE   A O   1 
ATOM   2233 C  CB  . PHE   A 1 306 ? 19.238  20.506  31.175  1   28.32 ? 291 PHE   A CB  1 
ATOM   2234 C  CG  . PHE   A 1 306 ? 17.919  21.225  31.354  1   29.47 ? 291 PHE   A CG  1 
ATOM   2235 C  CD1 . PHE   A 1 306 ? 16.802  20.554  31.845  1   30.39 ? 291 PHE   A CD1 1 
ATOM   2236 C  CD2 . PHE   A 1 306 ? 17.801  22.585  31.074  1   30.48 ? 291 PHE   A CD2 1 
ATOM   2237 C  CE1 . PHE   A 1 306 ? 15.597  21.216  32.037  1   31.1  ? 291 PHE   A CE1 1 
ATOM   2238 C  CE2 . PHE   A 1 306 ? 16.583  23.244  31.254  1   31.25 ? 291 PHE   A CE2 1 
ATOM   2239 C  CZ  . PHE   A 1 306 ? 15.491  22.555  31.731  1   31.32 ? 291 PHE   A CZ  1 
ATOM   2240 N  N   . LEU   A 1 307 ? 19.887  21.039  28.047  1   28.64 ? 292 LEU   A N   1 
ATOM   2241 C  CA  . LEU   A 1 307 ? 19.591  21.729  26.788  1   29.27 ? 292 LEU   A CA  1 
ATOM   2242 C  C   . LEU   A 1 307 ? 19.281  20.752  25.65   1   30.6  ? 292 LEU   A C   1 
ATOM   2243 O  O   . LEU   A 1 307 ? 18.367  21.01   24.857  1   31.05 ? 292 LEU   A O   1 
ATOM   2244 C  CB  . LEU   A 1 307 ? 20.662  22.736  26.398  1   30.14 ? 292 LEU   A CB  1 
ATOM   2245 C  CG  . LEU   A 1 307 ? 20.689  23.987  27.28   1   31.67 ? 292 LEU   A CG  1 
ATOM   2246 C  CD1 . LEU   A 1 307 ? 21.996  24.743  27.126  1   33.1  ? 292 LEU   A CD1 1 
ATOM   2247 C  CD2 . LEU   A 1 307 ? 19.471  24.865  27.016  1   31.55 ? 292 LEU   A CD2 1 
ATOM   2248 N  N   . GLN   A 1 308 ? 19.964  19.598  25.617  1   31.09 ? 293 GLN   A N   1 
ATOM   2249 C  CA  . GLN   A 1 308 ? 19.668  18.611  24.577  1   31.31 ? 293 GLN   A CA  1 
ATOM   2250 C  C   . GLN   A 1 308 ? 18.276  17.994  24.794  1   30.13 ? 293 GLN   A C   1 
ATOM   2251 O  O   . GLN   A 1 308 ? 17.484  17.938  23.872  1   31.04 ? 293 GLN   A O   1 
ATOM   2252 C  CB  . GLN   A 1 308 ? 20.746  17.536  24.451  1   33.91 ? 293 GLN   A CB  1 
ATOM   2253 C  CG  . GLN   A 1 308 ? 20.481  16.614  23.24   1   41.03 ? 293 GLN   A CG  1 
ATOM   2254 C  CD  . GLN   A 1 308 ? 20.737  17.243  21.868  1   48.53 ? 293 GLN   A CD  1 
ATOM   2255 O  OE1 . GLN   A 1 308 ? 19.967  17.045  20.907  1   50.13 ? 293 GLN   A OE1 1 
ATOM   2256 N  NE2 . GLN   A 1 308 ? 21.845  18.002  21.734  1   49.56 ? 293 GLN   A NE2 1 
ATOM   2257 N  N   . ASP   A 1 309 ? 17.958  17.593  26.025  1   28.48 ? 294 ASP   A N   1 
ATOM   2258 C  CA  . ASP   A 1 309 ? 16.653  17.034  26.355  1   28.91 ? 294 ASP   A CA  1 
ATOM   2259 C  C   . ASP   A 1 309 ? 15.51   17.997  26.018  1   28.42 ? 294 ASP   A C   1 
ATOM   2260 O  O   . ASP   A 1 309 ? 14.486  17.564  25.482  1   28.03 ? 294 ASP   A O   1 
ATOM   2261 C  CB  . ASP   A 1 309 ? 16.612  16.658  27.843  1   30.05 ? 294 ASP   A CB  1 
ATOM   2262 C  CG  . ASP   A 1 309 ? 17.469  15.459  28.202  1   35.25 ? 294 ASP   A CG  1 
ATOM   2263 O  OD1 . ASP   A 1 309 ? 17.998  14.788  27.263  1   36.73 ? 294 ASP   A OD1 1 
ATOM   2264 O  OD2 . ASP   A 1 309 ? 17.642  15.204  29.407  1   37    ? 294 ASP   A OD2 1 
ATOM   2265 N  N   . MET   A 1 310 ? 15.7    19.303  26.296  1   28.24 ? 295 MET   A N   1 
ATOM   2266 C  CA  . MET   A 1 310 ? 14.694  20.315  26.04   1   28.6  ? 295 MET   A CA  1 
ATOM   2267 C  C   . MET   A 1 310 ? 14.395  20.53   24.574  1   29.91 ? 295 MET   A C   1 
ATOM   2268 O  O   . MET   A 1 310 ? 13.33   21.082  24.272  1   30.41 ? 295 MET   A O   1 
ATOM   2269 C  CB  . MET   A 1 310 ? 15      21.632  26.749  1   28.57 ? 295 MET   A CB  1 
ATOM   2270 C  CG  . MET   A 1 310 ? 14.835  21.546  28.275  1   30.85 ? 295 MET   A CG  1 
ATOM   2271 S  SD  . MET   A 1 310 ? 13.224  20.823  28.847  1   30.95 ? 295 MET   A SD  1 
ATOM   2272 C  CE  . MET   A 1 310 ? 13.756  19.145  29.306  1   27.05 ? 295 MET   A CE  1 
ATOM   2273 N  N   . ARG   A 1 311 ? 15.246  20.021  23.667  1   29.75 ? 296 ARG   A N   1 
ATOM   2274 C  CA  . ARG   A 1 311 ? 14.946  20.092  22.231  1   30.25 ? 296 ARG   A CA  1 
ATOM   2275 C  C   . ARG   A 1 311 ? 13.714  19.243  21.858  1   31.04 ? 296 ARG   A C   1 
ATOM   2276 O  O   . ARG   A 1 311 ? 13.021  19.553  20.889  1   30.72 ? 296 ARG   A O   1 
ATOM   2277 C  CB  . ARG   A 1 311 ? 16.151  19.68   21.393  1   30.25 ? 296 ARG   A CB  1 
ATOM   2278 C  CG  . ARG   A 1 311 ? 17.156  20.802  21.291  1   31.77 ? 296 ARG   A CG  1 
ATOM   2279 C  CD  . ARG   A 1 311 ? 18.336  20.437  20.449  1   34.57 ? 296 ARG   A CD  1 
ATOM   2280 N  NE  . ARG   A 1 311 ? 19.339  21.5    20.48   1   35.53 ? 296 ARG   A NE  1 
ATOM   2281 C  CZ  . ARG   A 1 311 ? 20.341  21.61   19.613  1   36.32 ? 296 ARG   A CZ  1 
ATOM   2282 N  NH1 . ARG   A 1 311 ? 20.479  20.726  18.635  1   34.43 ? 296 ARG   A NH1 1 
ATOM   2283 N  NH2 . ARG   A 1 311 ? 21.202  22.619  19.709  1   34.13 ? 296 ARG   A NH2 1 
ATOM   2284 N  N   . ARG   A 1 312 ? 13.441  18.18   22.638  1   31.11 ? 297 ARG   A N   1 
ATOM   2285 C  CA  . ARG   A 1 312 ? 12.251  17.36   22.436  1   32.07 ? 297 ARG   A CA  1 
ATOM   2286 C  C   . ARG   A 1 312 ? 10.949  18.121  22.763  1   30.4  ? 297 ARG   A C   1 
ATOM   2287 O  O   . ARG   A 1 312 ? 9.869   17.697  22.355  1   29.64 ? 297 ARG   A O   1 
ATOM   2288 C  CB  . ARG   A 1 312 ? 12.336  16.085  23.28   1   35.42 ? 297 ARG   A CB  1 
ATOM   2289 C  CG  . ARG   A 1 312 ? 13.276  15.064  22.671  1   43.35 ? 297 ARG   A CG  1 
ATOM   2290 C  CD  . ARG   A 1 312 ? 12.735  14.562  21.329  1   49.74 ? 297 ARG   A CD  1 
ATOM   2291 N  NE  . ARG   A 1 312 ? 13.8    14.268  20.364  1   54.82 ? 297 ARG   A NE  1 
ATOM   2292 C  CZ  . ARG   A 1 312 ? 13.591  14.014  19.074  1   57.84 ? 297 ARG   A CZ  1 
ATOM   2293 N  NH1 . ARG   A 1 312 ? 12.357  14.017  18.58   1   58.02 ? 297 ARG   A NH1 1 
ATOM   2294 N  NH2 . ARG   A 1 312 ? 14.614  13.742  18.271  1   57.66 ? 297 ARG   A NH2 1 
ATOM   2295 N  N   . TYR   A 1 313 ? 11.051  19.175  23.602  1   28.81 ? 298 TYR   A N   1 
ATOM   2296 C  CA  . TYR   A 1 313 ? 9.928   20.026  24.009  1   27.87 ? 298 TYR   A CA  1 
ATOM   2297 C  C   . TYR   A 1 313 ? 9.801   21.291  23.175  1   28.72 ? 298 TYR   A C   1 
ATOM   2298 O  O   . TYR   A 1 313 ? 9.018   22.182  23.508  1   29.07 ? 298 TYR   A O   1 
ATOM   2299 C  CB  . TYR   A 1 313 ? 10.129  20.444  25.431  1   26.99 ? 298 TYR   A CB  1 
ATOM   2300 C  CG  . TYR   A 1 313 ? 10.142  19.3    26.401  1   27.64 ? 298 TYR   A CG  1 
ATOM   2301 C  CD1 . TYR   A 1 313 ? 11.2    18.4    26.432  1   27.56 ? 298 TYR   A CD1 1 
ATOM   2302 C  CD2 . TYR   A 1 313 ? 9.151   19.175  27.363  1   28.37 ? 298 TYR   A CD2 1 
ATOM   2303 C  CE1 . TYR   A 1 313 ? 11.237  17.364  27.365  1   28.48 ? 298 TYR   A CE1 1 
ATOM   2304 C  CE2 . TYR   A 1 313 ? 9.196   18.166  28.315  1   28.97 ? 298 TYR   A CE2 1 
ATOM   2305 C  CZ  . TYR   A 1 313 ? 10.22   17.247  28.295  1   29.24 ? 298 TYR   A CZ  1 
ATOM   2306 O  OH  . TYR   A 1 313 ? 10.218  16.261  29.244  1   30.3  ? 298 TYR   A OH  1 
ATOM   2307 N  N   . MET   A 1 314 ? 10.522  21.34   22.067  1   29.12 ? 299 MET   A N   1 
ATOM   2308 C  CA  . MET   A 1 314 ? 10.593  22.426  21.111  1   30.1  ? 299 MET   A CA  1 
ATOM   2309 C  C   . MET   A 1 314 ? 9.83    21.965  19.868  1   29.85 ? 299 MET   A C   1 
ATOM   2310 O  O   . MET   A 1 314 ? 9.889   20.786  19.536  1   30.61 ? 299 MET   A O   1 
ATOM   2311 C  CB  . MET   A 1 314 ? 12.084  22.587  20.778  1   31.23 ? 299 MET   A CB  1 
ATOM   2312 C  CG  . MET   A 1 314 ? 12.436  23.793  20.024  1   35.62 ? 299 MET   A CG  1 
ATOM   2313 S  SD  . MET   A 1 314 ? 14.23   23.869  19.712  1   31.06 ? 299 MET   A SD  1 
ATOM   2314 C  CE  . MET   A 1 314 ? 14.931  24.152  21.395  1   23.49 ? 299 MET   A CE  1 
ATOM   2315 N  N   . PRO   A 1 315 ? 9.133   22.856  19.14   1   29.16 ? 300 PRO   A N   1 
ATOM   2316 C  CA  . PRO   A 1 315 ? 8.434   22.42   17.924  1   29.77 ? 300 PRO   A CA  1 
ATOM   2317 C  C   . PRO   A 1 315 ? 9.374   21.742  16.935  1   32.05 ? 300 PRO   A C   1 
ATOM   2318 O  O   . PRO   A 1 315 ? 10.494  22.198  16.748  1   32.36 ? 300 PRO   A O   1 
ATOM   2319 C  CB  . PRO   A 1 315 ? 7.885   23.727  17.336  1   30.16 ? 300 PRO   A CB  1 
ATOM   2320 C  CG  . PRO   A 1 315 ? 7.815   24.651  18.475  1   30.46 ? 300 PRO   A CG  1 
ATOM   2321 C  CD  . PRO   A 1 315 ? 8.935   24.296  19.394  1   28.53 ? 300 PRO   A CD  1 
ATOM   2322 N  N   . PRO   A 1 316 ? 8.923   20.643  16.31   1   32.85 ? 301 PRO   A N   1 
ATOM   2323 C  CA  . PRO   A 1 316 ? 9.776   19.938  15.344  1   32.1  ? 301 PRO   A CA  1 
ATOM   2324 C  C   . PRO   A 1 316 ? 10.473  20.83   14.314  1   32.02 ? 301 PRO   A C   1 
ATOM   2325 O  O   . PRO   A 1 316 ? 11.665  20.658  14.117  1   33.03 ? 301 PRO   A O   1 
ATOM   2326 C  CB  . PRO   A 1 316 ? 8.821   18.918  14.688  1   32.6  ? 301 PRO   A CB  1 
ATOM   2327 C  CG  . PRO   A 1 316 ? 7.407   19.37   15.063  1   33.5  ? 301 PRO   A CG  1 
ATOM   2328 C  CD  . PRO   A 1 316 ? 7.59    20.006  16.427  1   31.97 ? 301 PRO   A CD  1 
ATOM   2329 N  N   . ALA   A 1 317 ? 9.785   21.809  13.72   1   31.51 ? 302 ALA   A N   1 
ATOM   2330 C  CA  . ALA   A 1 317 ? 10.41   22.687  12.725  1   31.68 ? 302 ALA   A CA  1 
ATOM   2331 C  C   . ALA   A 1 317 ? 11.641  23.452  13.271  1   32.35 ? 302 ALA   A C   1 
ATOM   2332 O  O   . ALA   A 1 317 ? 12.618  23.689  12.549  1   31.57 ? 302 ALA   A O   1 
ATOM   2333 C  CB  . ALA   A 1 317 ? 9.382   23.664  12.194  1   31.49 ? 302 ALA   A CB  1 
ATOM   2334 N  N   . HIS   A 1 318 ? 11.566  23.84   14.555  1   31.8  ? 303 HIS   A N   1 
ATOM   2335 C  CA  . HIS   A 1 318 ? 12.567  24.612  15.262  1   31.59 ? 303 HIS   A CA  1 
ATOM   2336 C  C   . HIS   A 1 318 ? 13.71   23.738  15.708  1   31.97 ? 303 HIS   A C   1 
ATOM   2337 O  O   . HIS   A 1 318 ? 14.865  24.148  15.588  1   32.26 ? 303 HIS   A O   1 
ATOM   2338 C  CB  . HIS   A 1 318 ? 11.905  25.342  16.434  1   31.62 ? 303 HIS   A CB  1 
ATOM   2339 C  CG  . HIS   A 1 318 ? 10.886  26.375  16.024  1   32.68 ? 303 HIS   A CG  1 
ATOM   2340 N  ND1 . HIS   A 1 318 ? 10.12   27.037  16.973  1   34.2  ? 303 HIS   A ND1 1 
ATOM   2341 C  CD2 . HIS   A 1 318 ? 10.604  26.887  14.798  1   33.31 ? 303 HIS   A CD2 1 
ATOM   2342 C  CE1 . HIS   A 1 318 ? 9.385   27.91   16.296  1   35.18 ? 303 HIS   A CE1 1 
ATOM   2343 N  NE2 . HIS   A 1 318 ? 9.646   27.859  14.982  1   34.85 ? 303 HIS   A NE2 1 
ATOM   2344 N  N   . ARG   A 1 319 ? 13.411  22.502  16.136  1   31.75 ? 304 ARG   A N   1 
ATOM   2345 C  CA  . ARG   A 1 319 ? 14.408  21.484  16.46   1   33.45 ? 304 ARG   A CA  1 
ATOM   2346 C  C   . ARG   A 1 319 ? 15.234  21.202  15.171  1   34.21 ? 304 ARG   A C   1 
ATOM   2347 O  O   . ARG   A 1 319 ? 16.463  21.165  15.221  1   34.48 ? 304 ARG   A O   1 
ATOM   2348 C  CB  . ARG   A 1 319 ? 13.633  20.233  16.879  1   36.49 ? 304 ARG   A CB  1 
ATOM   2349 C  CG  . ARG   A 1 319 ? 14.405  19.064  17.462  1   42.26 ? 304 ARG   A CG  1 
ATOM   2350 C  CD  . ARG   A 1 319 ? 13.463  17.856  17.656  1   47.52 ? 304 ARG   A CD  1 
ATOM   2351 N  NE  . ARG   A 1 319 ? 12.207  18.221  18.328  1   52.09 ? 304 ARG   A NE  1 
ATOM   2352 C  CZ  . ARG   A 1 319 ? 11.034  17.64   18.097  1   56.04 ? 304 ARG   A CZ  1 
ATOM   2353 N  NH1 . ARG   A 1 319 ? 10.935  16.664  17.204  1   57.1  ? 304 ARG   A NH1 1 
ATOM   2354 N  NH2 . ARG   A 1 319 ? 9.944   18.049  18.739  1   55.77 ? 304 ARG   A NH2 1 
ATOM   2355 N  N   . ASN   A 1 320 ? 14.542  21.1    14.021  1   34.94 ? 305 ASN   A N   1 
ATOM   2356 C  CA  . ASN   A 1 320 ? 15.136  20.859  12.715  1   36.18 ? 305 ASN   A CA  1 
ATOM   2357 C  C   . ASN   A 1 320 ? 15.981  22.008  12.264  1   37.16 ? 305 ASN   A C   1 
ATOM   2358 O  O   . ASN   A 1 320 ? 17.015  21.77   11.649  1   38.42 ? 305 ASN   A O   1 
ATOM   2359 C  CB  . ASN   A 1 320 ? 14.072  20.582  11.668  1   37.59 ? 305 ASN   A CB  1 
ATOM   2360 C  CG  . ASN   A 1 320 ? 13.319  19.303  11.901  1   42.12 ? 305 ASN   A CG  1 
ATOM   2361 O  OD1 . ASN   A 1 320 ? 13.692  18.468  12.747  1   43.72 ? 305 ASN   A OD1 1 
ATOM   2362 N  ND2 . ASN   A 1 320 ? 12.205  19.139  11.18   1   42.7  ? 305 ASN   A ND2 1 
ATOM   2363 N  N   . PHE   A 1 321 ? 15.577  23.25   12.564  1   35.95 ? 306 PHE   A N   1 
ATOM   2364 C  CA  . PHE   A 1 321 ? 16.381  24.409  12.206  1   34.99 ? 306 PHE   A CA  1 
ATOM   2365 C  C   . PHE   A 1 321 ? 17.732  24.36   12.92   1   34.29 ? 306 PHE   A C   1 
ATOM   2366 O  O   . PHE   A 1 321 ? 18.755  24.51   12.262  1   34.43 ? 306 PHE   A O   1 
ATOM   2367 C  CB  . PHE   A 1 321 ? 15.633  25.694  12.523  1   35    ? 306 PHE   A CB  1 
ATOM   2368 C  CG  . PHE   A 1 321 ? 16.417  26.931  12.189  1   35.7  ? 306 PHE   A CG  1 
ATOM   2369 C  CD1 . PHE   A 1 321 ? 16.67   27.274  10.875  1   36.14 ? 306 PHE   A CD1 1 
ATOM   2370 C  CD2 . PHE   A 1 321 ? 16.859  27.779  13.187  1   36.8  ? 306 PHE   A CD2 1 
ATOM   2371 C  CE1 . PHE   A 1 321 ? 17.353  28.44   10.568  1   37.07 ? 306 PHE   A CE1 1 
ATOM   2372 C  CE2 . PHE   A 1 321 ? 17.525  28.95   12.876  1   37.34 ? 306 PHE   A CE2 1 
ATOM   2373 C  CZ  . PHE   A 1 321 ? 17.766  29.275  11.568  1   37.21 ? 306 PHE   A CZ  1 
ATOM   2374 N  N   . LEU   A 1 322 ? 17.735  24.047  14.232  1   33.19 ? 307 LEU   A N   1 
ATOM   2375 C  CA  . LEU   A 1 322 ? 18.952  23.945  15.03   1   33.69 ? 307 LEU   A CA  1 
ATOM   2376 C  C   . LEU   A 1 322 ? 19.885  22.849  14.53   1   34.73 ? 307 LEU   A C   1 
ATOM   2377 O  O   . LEU   A 1 322 ? 21.075  23.105  14.338  1   34.71 ? 307 LEU   A O   1 
ATOM   2378 C  CB  . LEU   A 1 322 ? 18.637  23.697  16.524  1   33.14 ? 307 LEU   A CB  1 
ATOM   2379 C  CG  . LEU   A 1 322 ? 17.89   24.787  17.27   1   34.39 ? 307 LEU   A CG  1 
ATOM   2380 C  CD1 . LEU   A 1 322 ? 17.702  24.396  18.727  1   34.49 ? 307 LEU   A CD1 1 
ATOM   2381 C  CD2 . LEU   A 1 322 ? 18.632  26.112  17.176  1   35.11 ? 307 LEU   A CD2 1 
ATOM   2382 N  N   . CYS   A 1 323 ? 19.361  21.639  14.325  1   35.59 ? 308 CYS   A N   1 
ATOM   2383 C  CA  . CYS   A 1 323 ? 20.218  20.553  13.87   1   36.58 ? 308 CYS   A CA  1 
ATOM   2384 C  C   . CYS   A 1 323 ? 20.775  20.84   12.453  1   35.71 ? 308 CYS   A C   1 
ATOM   2385 O  O   . CYS   A 1 323 ? 21.957  20.564  12.197  1   34.83 ? 308 CYS   A O   1 
ATOM   2386 C  CB  . CYS   A 1 323 ? 19.547  19.19   13.996  1   38.31 ? 308 CYS   A CB  1 
ATOM   2387 S  SG  . CYS   A 1 323 ? 18.345  18.831  12.701  1   46.88 ? 308 CYS   A SG  1 
ATOM   2388 N  N   . SER   A 1 324 ? 19.98   21.507  11.592  1   35.72 ? 309 SER   A N   1 
ATOM   2389 C  CA  . SER   A 1 324 ? 20.489  21.889  10.268  1   37.18 ? 309 SER   A CA  1 
ATOM   2390 C  C   . SER   A 1 324 ? 21.59   22.993  10.375  1   37.84 ? 309 SER   A C   1 
ATOM   2391 O  O   . SER   A 1 324 ? 22.529  22.973  9.58    1   38.81 ? 309 SER   A O   1 
ATOM   2392 C  CB  . SER   A 1 324 ? 19.359  22.297  9.334   1   39.5  ? 309 SER   A CB  1 
ATOM   2393 O  OG  . SER   A 1 324 ? 18.928  23.603  9.675   1   45.42 ? 309 SER   A OG  1 
ATOM   2394 N  N   . LEU   A 1 325 ? 21.507  23.917  11.378  1   36.68 ? 310 LEU   A N   1 
ATOM   2395 C  CA  . LEU   A 1 325 ? 22.573  24.903  11.601  1   35.92 ? 310 LEU   A CA  1 
ATOM   2396 C  C   . LEU   A 1 325 ? 23.842  24.158  12.015  1   36.05 ? 310 LEU   A C   1 
ATOM   2397 O  O   . LEU   A 1 325 ? 24.926  24.52   11.567  1   35.8  ? 310 LEU   A O   1 
ATOM   2398 C  CB  . LEU   A 1 325 ? 22.225  25.912  12.708  1   35.15 ? 310 LEU   A CB  1 
ATOM   2399 C  CG  . LEU   A 1 325 ? 21.232  27.022  12.411  1   34.93 ? 310 LEU   A CG  1 
ATOM   2400 C  CD1 . LEU   A 1 325 ? 21.118  27.935  13.595  1   34.59 ? 310 LEU   A CD1 1 
ATOM   2401 C  CD2 . LEU   A 1 325 ? 21.637  27.828  11.21   1   34.62 ? 310 LEU   A CD2 1 
ATOM   2402 N  N   . GLU   A 1 326 ? 23.711  23.108  12.854  1   36.37 ? 311 GLU   A N   1 
ATOM   2403 C  CA  . GLU   A 1 326 ? 24.816  22.254  13.31   1   37.31 ? 311 GLU   A CA  1 
ATOM   2404 C  C   . GLU   A 1 326 ? 25.481  21.518  12.16   1   38.56 ? 311 GLU   A C   1 
ATOM   2405 O  O   . GLU   A 1 326 ? 26.673  21.267  12.231  1   39.68 ? 311 GLU   A O   1 
ATOM   2406 C  CB  . GLU   A 1 326 ? 24.338  21.25   14.366  1   39.07 ? 311 GLU   A CB  1 
ATOM   2407 C  CG  . GLU   A 1 326 ? 24.481  21.764  15.787  1   42.95 ? 311 GLU   A CG  1 
ATOM   2408 C  CD  . GLU   A 1 326 ? 23.556  21.165  16.835  1   47.26 ? 311 GLU   A CD  1 
ATOM   2409 O  OE1 . GLU   A 1 326 ? 22.739  20.28   16.486  1   48.88 ? 311 GLU   A OE1 1 
ATOM   2410 O  OE2 . GLU   A 1 326 ? 23.655  21.579  18.015  1   46.65 ? 311 GLU   A OE2 1 
ATOM   2411 N  N   . SER   A 1 327 ? 24.729  21.188  11.097  1   38.82 ? 312 SER   A N   1 
ATOM   2412 C  CA  . SER   A 1 327 ? 25.237  20.495  9.898   1   40.36 ? 312 SER   A CA  1 
ATOM   2413 C  C   . SER   A 1 327 ? 26.055  21.421  8.968   1   41.12 ? 312 SER   A C   1 
ATOM   2414 O  O   . SER   A 1 327 ? 26.799  20.946  8.111   1   40.6  ? 312 SER   A O   1 
ATOM   2415 C  CB  . SER   A 1 327 ? 24.075  19.922  9.088   1   42.09 ? 312 SER   A CB  1 
ATOM   2416 O  OG  . SER   A 1 327 ? 23.287  19.008  9.839   1   47.26 ? 312 SER   A OG  1 
ATOM   2417 N  N   . ASN   A 1 328 ? 25.823  22.73   9.063   1   42.02 ? 313 ASN   A N   1 
ATOM   2418 C  CA  . ASN   A 1 328 ? 26.472  23.733  8.236   1   43.16 ? 313 ASN   A CA  1 
ATOM   2419 C  C   . ASN   A 1 328 ? 27.92   23.982  8.718   1   44.2  ? 313 ASN   A C   1 
ATOM   2420 O  O   . ASN   A 1 328 ? 28.254  23.706  9.878   1   44.26 ? 313 ASN   A O   1 
ATOM   2421 C  CB  . ASN   A 1 328 ? 25.646  25.027  8.263   1   44.74 ? 313 ASN   A CB  1 
ATOM   2422 C  CG  . ASN   A 1 328 ? 24.516  25.056  7.264   1   48.95 ? 313 ASN   A CG  1 
ATOM   2423 O  OD1 . ASN   A 1 328 ? 24.312  26.046  6.553   1   51.89 ? 313 ASN   A OD1 1 
ATOM   2424 N  ND2 . ASN   A 1 328 ? 23.76   23.975  7.159   1   48.78 ? 313 ASN   A ND2 1 
ATOM   2425 N  N   . PRO   A 1 329 ? 28.81   24.477  7.833   1   44.9  ? 314 PRO   A N   1 
ATOM   2426 C  CA  . PRO   A 1 329 ? 30.195  24.751  8.259   1   45.02 ? 314 PRO   A CA  1 
ATOM   2427 C  C   . PRO   A 1 329 ? 30.27   25.734  9.424   1   44.71 ? 314 PRO   A C   1 
ATOM   2428 O  O   . PRO   A 1 329 ? 29.38   26.57   9.585   1   45.27 ? 314 PRO   A O   1 
ATOM   2429 C  CB  . PRO   A 1 329 ? 30.845  25.338  7.004   1   46.32 ? 314 PRO   A CB  1 
ATOM   2430 C  CG  . PRO   A 1 329 ? 29.99   24.869  5.865   1   46.82 ? 314 PRO   A CG  1 
ATOM   2431 C  CD  . PRO   A 1 329 ? 28.597  24.851  6.42    1   44.92 ? 314 PRO   A CD  1 
ATOM   2432 N  N   . SER   A 1 330 ? 31.308  25.61   10.252  1   43.75 ? 315 SER   A N   1 
ATOM   2433 C  CA  . SER   A 1 330 ? 31.464  26.447  11.443  1   43.43 ? 315 SER   A CA  1 
ATOM   2434 C  C   . SER   A 1 330 ? 31.87   27.901  11.162  1   43.03 ? 315 SER   A C   1 
ATOM   2435 O  O   . SER   A 1 330 ? 32.873  28.148  10.491  1   44.03 ? 315 SER   A O   1 
ATOM   2436 C  CB  . SER   A 1 330 ? 32.441  25.798  12.424  1   44.22 ? 315 SER   A CB  1 
ATOM   2437 O  OG  . SER   A 1 330 ? 32.753  26.636  13.528  1   46.77 ? 315 SER   A OG  1 
ATOM   2438 N  N   . VAL   A 1 331 ? 31.129  28.852  11.739  1   41.51 ? 316 VAL   A N   1 
ATOM   2439 C  CA  . VAL   A 1 331 ? 31.416  30.278  11.636  1   40.41 ? 316 VAL   A CA  1 
ATOM   2440 C  C   . VAL   A 1 331 ? 32.66   30.586  12.49   1   39.99 ? 316 VAL   A C   1 
ATOM   2441 O  O   . VAL   A 1 331 ? 33.556  31.285  12.025  1   39.56 ? 316 VAL   A O   1 
ATOM   2442 C  CB  . VAL   A 1 331 ? 30.19   31.122  12.063  1   40.21 ? 316 VAL   A CB  1 
ATOM   2443 C  CG1 . VAL   A 1 331 ? 30.519  32.613  12.096  1   40.68 ? 316 VAL   A CG1 1 
ATOM   2444 C  CG2 . VAL   A 1 331 ? 28.996  30.842  11.148  1   40.56 ? 316 VAL   A CG2 1 
ATOM   2445 N  N   . ARG   A 1 332 ? 32.76   30.006  13.703  1   39.15 ? 317 ARG   A N   1 
ATOM   2446 C  CA  . ARG   A 1 332 ? 33.925  30.206  14.56   1   38.93 ? 317 ARG   A CA  1 
ATOM   2447 C  C   . ARG   A 1 332 ? 35.203  29.71   13.862  1   39.59 ? 317 ARG   A C   1 
ATOM   2448 O  O   . ARG   A 1 332 ? 36.194  30.423  13.856  1   39.39 ? 317 ARG   A O   1 
ATOM   2449 C  CB  . ARG   A 1 332 ? 33.74   29.531  15.934  1   39.46 ? 317 ARG   A CB  1 
ATOM   2450 C  CG  . ARG   A 1 332 ? 35.019  28.97   16.563  1   41.28 ? 317 ARG   A CG  1 
ATOM   2451 C  CD  . ARG   A 1 332 ? 34.849  28.471  17.97   1   42.63 ? 317 ARG   A CD  1 
ATOM   2452 N  NE  . ARG   A 1 332 ? 34.584  29.626  18.791  1   43.26 ? 317 ARG   A NE  1 
ATOM   2453 C  CZ  . ARG   A 1 332 ? 35.356  30.061  19.772  1   40.8  ? 317 ARG   A CZ  1 
ATOM   2454 N  NH1 . ARG   A 1 332 ? 36.43   29.375  20.138  1   40.58 ? 317 ARG   A NH1 1 
ATOM   2455 N  NH2 . ARG   A 1 332 ? 35.038  31.156  20.423  1   37.61 ? 317 ARG   A NH2 1 
ATOM   2456 N  N   . GLU   A 1 333 ? 35.174  28.501  13.285  1   40.33 ? 318 GLU   A N   1 
ATOM   2457 C  CA  . GLU   A 1 333 ? 36.343  27.947  12.6    1   41.76 ? 318 GLU   A CA  1 
ATOM   2458 C  C   . GLU   A 1 333 ? 36.759  28.84   11.427  1   41.46 ? 318 GLU   A C   1 
ATOM   2459 O  O   . GLU   A 1 333 ? 37.948  29.059  11.219  1   42.31 ? 318 GLU   A O   1 
ATOM   2460 C  CB  . GLU   A 1 333 ? 36.061  26.517  12.096  1   45.15 ? 318 GLU   A CB  1 
ATOM   2461 C  CG  . GLU   A 1 333 ? 36.934  25.457  12.738  1   51.9  ? 318 GLU   A CG  1 
ATOM   2462 N  N   . PHE   A 1 334 ? 35.79   29.377  10.693  1   40.07 ? 319 PHE   A N   1 
ATOM   2463 C  CA  . PHE   A 1 334 ? 36.077  30.249  9.565   1   39.64 ? 319 PHE   A CA  1 
ATOM   2464 C  C   . PHE   A 1 334 ? 36.752  31.534  10.06   1   40.16 ? 319 PHE   A C   1 
ATOM   2465 O  O   . PHE   A 1 334 ? 37.773  31.93   9.511   1   41.38 ? 319 PHE   A O   1 
ATOM   2466 C  CB  . PHE   A 1 334 ? 34.791  30.575  8.817   1   38.63 ? 319 PHE   A CB  1 
ATOM   2467 C  CG  . PHE   A 1 334 ? 34.978  31.371  7.555   1   38.63 ? 319 PHE   A CG  1 
ATOM   2468 C  CD1 . PHE   A 1 334 ? 35.003  32.75   7.585   1   39.07 ? 319 PHE   A CD1 1 
ATOM   2469 C  CD2 . PHE   A 1 334 ? 35.055  30.742  6.33    1   39.66 ? 319 PHE   A CD2 1 
ATOM   2470 C  CE1 . PHE   A 1 334 ? 35.149  33.48   6.42    1   39.83 ? 319 PHE   A CE1 1 
ATOM   2471 C  CE2 . PHE   A 1 334 ? 35.187  31.478  5.164   1   40.42 ? 319 PHE   A CE2 1 
ATOM   2472 C  CZ  . PHE   A 1 334 ? 35.236  32.841  5.216   1   39.82 ? 319 PHE   A CZ  1 
ATOM   2473 N  N   . VAL   A 1 335 ? 36.214  32.146  11.112  1   38.89 ? 320 VAL   A N   1 
ATOM   2474 C  CA  . VAL   A 1 335 ? 36.772  33.371  11.66   1   38.9  ? 320 VAL   A CA  1 
ATOM   2475 C  C   . VAL   A 1 335 ? 38.194  33.144  12.234  1   39.62 ? 320 VAL   A C   1 
ATOM   2476 O  O   . VAL   A 1 335 ? 39.091  33.96   12.011  1   39.54 ? 320 VAL   A O   1 
ATOM   2477 C  CB  . VAL   A 1 335 ? 35.78   33.988  12.659  1   38.61 ? 320 VAL   A CB  1 
ATOM   2478 C  CG1 . VAL   A 1 335 ? 36.44   35.033  13.535  1   39.06 ? 320 VAL   A CG1 1 
ATOM   2479 C  CG2 . VAL   A 1 335 ? 34.585  34.583  11.917  1   39.15 ? 320 VAL   A CG2 1 
ATOM   2480 N  N   . LEU   A 1 336 ? 38.415  32.005  12.894  1   40    ? 321 LEU   A N   1 
ATOM   2481 C  CA  . LEU   A 1 336 ? 39.719  31.674  13.461  1   41.31 ? 321 LEU   A CA  1 
ATOM   2482 C  C   . LEU   A 1 336 ? 40.791  31.343  12.403  1   42.76 ? 321 LEU   A C   1 
ATOM   2483 O  O   . LEU   A 1 336 ? 41.984  31.479  12.666  1   43.58 ? 321 LEU   A O   1 
ATOM   2484 C  CB  . LEU   A 1 336 ? 39.58   30.474  14.409  1   41.23 ? 321 LEU   A CB  1 
ATOM   2485 C  CG  . LEU   A 1 336 ? 39.009  30.784  15.78   1   41.99 ? 321 LEU   A CG  1 
ATOM   2486 C  CD1 . LEU   A 1 336 ? 38.87   29.511  16.599  1   41.5  ? 321 LEU   A CD1 1 
ATOM   2487 C  CD2 . LEU   A 1 336 ? 39.873  31.812  16.537  1   42.51 ? 321 LEU   A CD2 1 
ATOM   2488 N  N   . SER   A 1 337 ? 40.373  30.893  11.229  1   42.96 ? 322 SER   A N   1 
ATOM   2489 C  CA  . SER   A 1 337 ? 41.312  30.473  10.196  1   43.27 ? 322 SER   A CA  1 
ATOM   2490 C  C   . SER   A 1 337 ? 41.815  31.611  9.305   1   44.35 ? 322 SER   A C   1 
ATOM   2491 O  O   . SER   A 1 337 ? 42.575  31.328  8.374   1   45.37 ? 322 SER   A O   1 
ATOM   2492 C  CB  . SER   A 1 337 ? 40.667  29.4    9.324   1   43.22 ? 322 SER   A CB  1 
ATOM   2493 O  OG  . SER   A 1 337 ? 39.778  29.964  8.369   1   44.71 ? 322 SER   A OG  1 
ATOM   2494 N  N   . LYS   A 1 338 ? 41.397  32.866  9.551   1   43.18 ? 323 LYS   A N   1 
ATOM   2495 C  CA  . LYS   A 1 338 ? 41.711  33.935  8.621   1   42.3  ? 323 LYS   A CA  1 
ATOM   2496 C  C   . LYS   A 1 338 ? 42.751  34.972  9.064   1   40.97 ? 323 LYS   A C   1 
ATOM   2497 O  O   . LYS   A 1 338 ? 43.208  35.748  8.216   1   40.66 ? 323 LYS   A O   1 
ATOM   2498 C  CB  . LYS   A 1 338 ? 40.414  34.651  8.212   1   43.63 ? 323 LYS   A CB  1 
ATOM   2499 C  CG  . LYS   A 1 338 ? 39.393  33.744  7.549   1   48.09 ? 323 LYS   A CG  1 
ATOM   2500 C  CD  . LYS   A 1 338 ? 39.835  33.304  6.168   1   54.44 ? 323 LYS   A CD  1 
ATOM   2501 C  CE  . LYS   A 1 338 ? 38.963  32.231  5.564   1   60.19 ? 323 LYS   A CE  1 
ATOM   2502 N  NZ  . LYS   A 1 338 ? 39.645  30.901  5.56    1   63.72 ? 323 LYS   A NZ  1 
ATOM   2503 N  N   . GLY   A 1 339 ? 43.105  35.022  10.348  1   39.1  ? 324 GLY   A N   1 
ATOM   2504 C  CA  . GLY   A 1 339 ? 44.063  36.013  10.843  1   37.91 ? 324 GLY   A CA  1 
ATOM   2505 C  C   . GLY   A 1 339 ? 43.592  37.434  10.551  1   36.92 ? 324 GLY   A C   1 
ATOM   2506 O  O   . GLY   A 1 339 ? 44.316  38.243  9.964   1   36.84 ? 324 GLY   A O   1 
ATOM   2507 N  N   . ASP   A 1 340 ? 42.321  37.701  10.862  1   35.32 ? 325 ASP   A N   1 
ATOM   2508 C  CA  . ASP   A 1 340 ? 41.676  38.971  10.549  1   34.04 ? 325 ASP   A CA  1 
ATOM   2509 C  C   . ASP   A 1 340 ? 41.053  39.57   11.805  1   35.19 ? 325 ASP   A C   1 
ATOM   2510 O  O   . ASP   A 1 340 ? 39.982  39.121  12.196  1   35.75 ? 325 ASP   A O   1 
ATOM   2511 C  CB  . ASP   A 1 340 ? 40.577  38.646  9.544   1   32.53 ? 325 ASP   A CB  1 
ATOM   2512 C  CG  . ASP   A 1 340 ? 39.846  39.803  8.922   1   33.77 ? 325 ASP   A CG  1 
ATOM   2513 O  OD1 . ASP   A 1 340 ? 39.584  40.79   9.63    1   33.99 ? 325 ASP   A OD1 1 
ATOM   2514 O  OD2 . ASP   A 1 340 ? 39.515  39.71   7.728   1   35.33 ? 325 ASP   A OD2 1 
ATOM   2515 N  N   . ALA   A 1 341 ? 41.66   40.605  12.39   1   34.35 ? 326 ALA   A N   1 
ATOM   2516 C  CA  . ALA   A 1 341 ? 41.152  41.232  13.6    1   34.59 ? 326 ALA   A CA  1 
ATOM   2517 C  C   . ALA   A 1 341 ? 39.741  41.797  13.49   1   34.78 ? 326 ALA   A C   1 
ATOM   2518 O  O   . ALA   A 1 341 ? 38.992  41.699  14.455  1   34.91 ? 326 ALA   A O   1 
ATOM   2519 C  CB  . ALA   A 1 341 ? 42.102  42.308  14.09   1   34.67 ? 326 ALA   A CB  1 
ATOM   2520 N  N   . GLY   A 1 342 ? 39.394  42.402  12.358  1   33.8  ? 327 GLY   A N   1 
ATOM   2521 C  CA  . GLY   A 1 342 ? 38.064  42.974  12.172  1   34.14 ? 327 GLY   A CA  1 
ATOM   2522 C  C   . GLY   A 1 342 ? 36.984  41.907  12.196  1   33.85 ? 327 GLY   A C   1 
ATOM   2523 O  O   . GLY   A 1 342 ? 35.917  42.102  12.778  1   32.92 ? 327 GLY   A O   1 
ATOM   2524 N  N   . LEU   A 1 343 ? 37.258  40.76   11.556  1   34.24 ? 328 LEU   A N   1 
ATOM   2525 C  CA  . LEU   A 1 343 ? 36.34   39.634  11.529  1   35.19 ? 328 LEU   A CA  1 
ATOM   2526 C  C   . LEU   A 1 343 ? 36.18   39.039  12.934  1   35.36 ? 328 LEU   A C   1 
ATOM   2527 O  O   . LEU   A 1 343 ? 35.053  38.781  13.36   1   35.76 ? 328 LEU   A O   1 
ATOM   2528 C  CB  . LEU   A 1 343 ? 36.884  38.583  10.563  1   36.08 ? 328 LEU   A CB  1 
ATOM   2529 C  CG  . LEU   A 1 343 ? 35.884  37.803  9.739   1   38.56 ? 328 LEU   A CG  1 
ATOM   2530 C  CD1 . LEU   A 1 343 ? 34.776  38.716  9.134   1   39.39 ? 328 LEU   A CD1 1 
ATOM   2531 C  CD2 . LEU   A 1 343 ? 36.602  37.012  8.645   1   39.15 ? 328 LEU   A CD2 1 
ATOM   2532 N  N   . ARG   A 1 344 ? 37.294  38.873  13.666  1   34.16 ? 329 ARG   A N   1 
ATOM   2533 C  CA  . ARG   A 1 344 ? 37.277  38.364  15.034  1   33.84 ? 329 ARG   A CA  1 
ATOM   2534 C  C   . ARG   A 1 344 ? 36.509  39.316  15.95   1   33.9  ? 329 ARG   A C   1 
ATOM   2535 O  O   . ARG   A 1 344 ? 35.802  38.846  16.837  1   33.63 ? 329 ARG   A O   1 
ATOM   2536 C  CB  . ARG   A 1 344 ? 38.702  38.159  15.579  1   34.73 ? 329 ARG   A CB  1 
ATOM   2537 C  CG  . ARG   A 1 344 ? 39.463  37      14.931  1   36.41 ? 329 ARG   A CG  1 
ATOM   2538 C  CD  . ARG   A 1 344 ? 40.655  36.562  15.776  1   38.1  ? 329 ARG   A CD  1 
ATOM   2539 N  NE  . ARG   A 1 344 ? 41.593  37.661  16.054  1   38.86 ? 329 ARG   A NE  1 
ATOM   2540 C  CZ  . ARG   A 1 344 ? 42.586  38.023  15.245  1   40.9  ? 329 ARG   A CZ  1 
ATOM   2541 N  NH1 . ARG   A 1 344 ? 42.801  37.366  14.115  1   41.64 ? 329 ARG   A NH1 1 
ATOM   2542 N  NH2 . ARG   A 1 344 ? 43.379  39.04   15.567  1   39.35 ? 329 ARG   A NH2 1 
ATOM   2543 N  N   . GLU   A 1 345 ? 36.666  40.637  15.763  1   33.29 ? 330 GLU   A N   1 
ATOM   2544 C  CA  . GLU   A 1 345 ? 35.952  41.623  16.58   1   33.49 ? 330 GLU   A CA  1 
ATOM   2545 C  C   . GLU   A 1 345 ? 34.428  41.576  16.299  1   31.43 ? 330 GLU   A C   1 
ATOM   2546 O  O   . GLU   A 1 345 ? 33.643  41.778  17.209  1   31.18 ? 330 GLU   A O   1 
ATOM   2547 C  CB  . GLU   A 1 345 ? 36.465  43.043  16.3    1   37.1  ? 330 GLU   A CB  1 
ATOM   2548 C  CG  . GLU   A 1 345 ? 37.778  43.393  16.99   1   46.52 ? 330 GLU   A CG  1 
ATOM   2549 C  CD  . GLU   A 1 345 ? 38.51   44.559  16.338  1   58.86 ? 330 GLU   A CD  1 
ATOM   2550 O  OE1 . GLU   A 1 345 ? 37.841  45.383  15.667  1   61.65 ? 330 GLU   A OE1 1 
ATOM   2551 O  OE2 . GLU   A 1 345 ? 39.753  44.643  16.489  1   61.73 ? 330 GLU   A OE2 1 
ATOM   2552 N  N   . ALA   A 1 346 ? 34.025  41.362  15.041  1   29.24 ? 331 ALA   A N   1 
ATOM   2553 C  CA  . ALA   A 1 346 ? 32.616  41.27   14.665  1   29.54 ? 331 ALA   A CA  1 
ATOM   2554 C  C   . ALA   A 1 346 ? 31.992  39.987  15.272  1   30.15 ? 331 ALA   A C   1 
ATOM   2555 O  O   . ALA   A 1 346 ? 30.872  40.025  15.782  1   31.4  ? 331 ALA   A O   1 
ATOM   2556 C  CB  . ALA   A 1 346 ? 32.491  41.235  13.156  1   28.87 ? 331 ALA   A CB  1 
ATOM   2557 N  N   . TYR   A 1 347 ? 32.743  38.884  15.256  1   29.01 ? 332 TYR   A N   1 
ATOM   2558 C  CA  . TYR   A 1 347 ? 32.333  37.611  15.83   1   29.73 ? 332 TYR   A CA  1 
ATOM   2559 C  C   . TYR   A 1 347 ? 32.182  37.787  17.338  1   30.83 ? 332 TYR   A C   1 
ATOM   2560 O  O   . TYR   A 1 347 ? 31.137  37.404  17.898  1   31.05 ? 332 TYR   A O   1 
ATOM   2561 C  CB  . TYR   A 1 347 ? 33.363  36.52   15.51   1   29.48 ? 332 TYR   A CB  1 
ATOM   2562 C  CG  . TYR   A 1 347 ? 33.151  35.247  16.297  1   29.88 ? 332 TYR   A CG  1 
ATOM   2563 C  CD1 . TYR   A 1 347 ? 33.704  35.089  17.562  1   30.28 ? 332 TYR   A CD1 1 
ATOM   2564 C  CD2 . TYR   A 1 347 ? 32.342  34.23   15.809  1   29.61 ? 332 TYR   A CD2 1 
ATOM   2565 C  CE1 . TYR   A 1 347 ? 33.471  33.949  18.313  1   30.31 ? 332 TYR   A CE1 1 
ATOM   2566 C  CE2 . TYR   A 1 347 ? 32.114  33.077  16.545  1   29.79 ? 332 TYR   A CE2 1 
ATOM   2567 C  CZ  . TYR   A 1 347 ? 32.687  32.939  17.795  1   29.76 ? 332 TYR   A CZ  1 
ATOM   2568 O  OH  . TYR   A 1 347 ? 32.474  31.804  18.538  1   27.64 ? 332 TYR   A OH  1 
ATOM   2569 N  N   . ASP   A 1 348 ? 33.184  38.401  17.98   1   30.19 ? 333 ASP   A N   1 
ATOM   2570 C  CA  . ASP   A 1 348 ? 33.14   38.659  19.422  1   30.59 ? 333 ASP   A CA  1 
ATOM   2571 C  C   . ASP   A 1 348 ? 32.049  39.625  19.822  1   30.09 ? 333 ASP   A C   1 
ATOM   2572 O  O   . ASP   A 1 348 ? 31.615  39.58   20.967  1   30.26 ? 333 ASP   A O   1 
ATOM   2573 C  CB  . ASP   A 1 348 ? 34.471  39.202  19.92   1   32.24 ? 333 ASP   A CB  1 
ATOM   2574 C  CG  . ASP   A 1 348 ? 35.47   38.164  20.323  1   36.36 ? 333 ASP   A CG  1 
ATOM   2575 O  OD1 . ASP   A 1 348 ? 35.196  36.953  20.121  1   36.93 ? 333 ASP   A OD1 1 
ATOM   2576 O  OD2 . ASP   A 1 348 ? 36.538  38.546  20.854  1   37.98 ? 333 ASP   A OD2 1 
ATOM   2577 N  N   . ALA   A 1 349 ? 31.613  40.521  18.917  1   29.06 ? 334 ALA   A N   1 
ATOM   2578 C  CA  . ALA   A 1 349 ? 30.524  41.423  19.255  1   29.04 ? 334 ALA   A CA  1 
ATOM   2579 C  C   . ALA   A 1 349 ? 29.208  40.61   19.428  1   28.99 ? 334 ALA   A C   1 
ATOM   2580 O  O   . ALA   A 1 349 ? 28.392  40.942  20.291  1   29.8  ? 334 ALA   A O   1 
ATOM   2581 C  CB  . ALA   A 1 349 ? 30.38   42.496  18.188  1   29.6  ? 334 ALA   A CB  1 
ATOM   2582 N  N   . CYS   A 1 350 ? 29.025  39.525  18.644  1   27.12 ? 335 CYS   A N   1 
ATOM   2583 C  CA  . CYS   A 1 350 ? 27.844  38.686  18.749  1   26.76 ? 335 CYS   A CA  1 
ATOM   2584 C  C   . CYS   A 1 350 ? 27.914  37.894  20.056  1   27    ? 335 CYS   A C   1 
ATOM   2585 O  O   . CYS   A 1 350 ? 26.919  37.853  20.799  1   26.84 ? 335 CYS   A O   1 
ATOM   2586 C  CB  . CYS   A 1 350 ? 27.753  37.754  17.553  1   26.9  ? 335 CYS   A CB  1 
ATOM   2587 S  SG  . CYS   A 1 350 ? 27.45   38.606  15.997  1   30.26 ? 335 CYS   A SG  1 
ATOM   2588 N  N   . VAL   A 1 351 ? 29.102  37.321  20.369  1   26.01 ? 336 VAL   A N   1 
ATOM   2589 C  CA  . VAL   A 1 351 ? 29.292  36.55   21.601  1   25.86 ? 336 VAL   A CA  1 
ATOM   2590 C  C   . VAL   A 1 351 ? 29.092  37.434  22.799  1   26.49 ? 336 VAL   A C   1 
ATOM   2591 O  O   . VAL   A 1 351 ? 28.412  37.039  23.748  1   27.25 ? 336 VAL   A O   1 
ATOM   2592 C  CB  . VAL   A 1 351 ? 30.678  35.879  21.641  1   26.53 ? 336 VAL   A CB  1 
ATOM   2593 C  CG1 . VAL   A 1 351 ? 30.894  35.157  22.971  1   27.03 ? 336 VAL   A CG1 1 
ATOM   2594 C  CG2 . VAL   A 1 351 ? 30.842  34.903  20.479  1   25.97 ? 336 VAL   A CG2 1 
ATOM   2595 N  N   . LYS   A 1 352 ? 29.649  38.65   22.759  1   25.91 ? 337 LYS   A N   1 
ATOM   2596 C  CA  . LYS   A 1 352 ? 29.499  39.584  23.881  1   26.65 ? 337 LYS   A CA  1 
ATOM   2597 C  C   . LYS   A 1 352 ? 28.04   39.967  24.083  1   27.33 ? 337 LYS   A C   1 
ATOM   2598 O  O   . LYS   A 1 352 ? 27.626  40.163  25.22   1   28.06 ? 337 LYS   A O   1 
ATOM   2599 C  CB  . LYS   A 1 352 ? 30.338  40.848  23.698  1   27.91 ? 337 LYS   A CB  1 
ATOM   2600 C  CG  . LYS   A 1 352 ? 30.797  41.447  25.046  1   32.31 ? 337 LYS   A CG  1 
ATOM   2601 N  N   . ALA   A 1 353 ? 27.258  40.121  22.998  1   27.72 ? 338 ALA   A N   1 
ATOM   2602 C  CA  . ALA   A 1 353 ? 25.843  40.48   23.14   1   27.79 ? 338 ALA   A CA  1 
ATOM   2603 C  C   . ALA   A 1 353 ? 25.097  39.354  23.872  1   28.82 ? 338 ALA   A C   1 
ATOM   2604 O  O   . ALA   A 1 353 ? 24.276  39.647  24.742  1   30.3  ? 338 ALA   A O   1 
ATOM   2605 C  CB  . ALA   A 1 353 ? 25.215  40.778  21.791  1   27.59 ? 338 ALA   A CB  1 
ATOM   2606 N  N   . LEU   A 1 354 ? 25.469  38.079  23.619  1   26.85 ? 339 LEU   A N   1 
ATOM   2607 C  CA  . LEU   A 1 354 ? 24.881  36.957  24.317  1   26.76 ? 339 LEU   A CA  1 
ATOM   2608 C  C   . LEU   A 1 354 ? 25.288  36.929  25.773  1   27.03 ? 339 LEU   A C   1 
ATOM   2609 O  O   . LEU   A 1 354 ? 24.457  36.673  26.615  1   28.84 ? 339 LEU   A O   1 
ATOM   2610 C  CB  . LEU   A 1 354 ? 25.251  35.643  23.663  1   26.52 ? 339 LEU   A CB  1 
ATOM   2611 C  CG  . LEU   A 1 354 ? 24.442  35.238  22.467  1   29.35 ? 339 LEU   A CG  1 
ATOM   2612 C  CD1 . LEU   A 1 354 ? 25.053  34.012  21.821  1   28.96 ? 339 LEU   A CD1 1 
ATOM   2613 C  CD2 . LEU   A 1 354 ? 22.919  35.091  22.8    1   31.1  ? 339 LEU   A CD2 1 
ATOM   2614 N  N   . VAL   A 1 355 ? 26.549  37.221  26.082  1   26.88 ? 340 VAL   A N   1 
ATOM   2615 C  CA  . VAL   A 1 355 ? 27.052  37.287  27.458  1   25.58 ? 340 VAL   A CA  1 
ATOM   2616 C  C   . VAL   A 1 355 ? 26.294  38.387  28.205  1   25.46 ? 340 VAL   A C   1 
ATOM   2617 O  O   . VAL   A 1 355 ? 25.947  38.185  29.349  1   24.83 ? 340 VAL   A O   1 
ATOM   2618 C  CB  . VAL   A 1 355 ? 28.589  37.552  27.498  1   26.33 ? 340 VAL   A CB  1 
ATOM   2619 C  CG1 . VAL   A 1 355 ? 29.061  37.873  28.923  1   27.5  ? 340 VAL   A CG1 1 
ATOM   2620 C  CG2 . VAL   A 1 355 ? 29.366  36.376  26.908  1   24.97 ? 340 VAL   A CG2 1 
ATOM   2621 N  N   . SER   A 1 356 ? 26.074  39.555  27.585  1   25.88 ? 341 SER   A N   1 
ATOM   2622 C  CA  . SER   A 1 356 ? 25.347  40.65   28.23   1   28.01 ? 341 SER   A CA  1 
ATOM   2623 C  C   . SER   A 1 356 ? 23.875  40.288  28.548  1   28.98 ? 341 SER   A C   1 
ATOM   2624 O  O   . SER   A 1 356 ? 23.352  40.654  29.616  1   29.03 ? 341 SER   A O   1 
ATOM   2625 C  CB  . SER   A 1 356 ? 25.394  41.911  27.358  1   30.53 ? 341 SER   A CB  1 
ATOM   2626 O  OG  . SER   A 1 356 ? 26.747  42.244  27.074  1   33.64 ? 341 SER   A OG  1 
ATOM   2627 N  N   . LEU   A 1 357 ? 23.201  39.586  27.61   1   28.15 ? 342 LEU   A N   1 
ATOM   2628 C  CA  . LEU   A 1 357 ? 21.84   39.122  27.781  1   28.12 ? 342 LEU   A CA  1 
ATOM   2629 C  C   . LEU   A 1 357 ? 21.828  38.126  28.953  1   27.68 ? 342 LEU   A C   1 
ATOM   2630 O  O   . LEU   A 1 357 ? 21.061  38.335  29.878  1   28.27 ? 342 LEU   A O   1 
ATOM   2631 C  CB  . LEU   A 1 357 ? 21.335  38.443  26.496  1   28.41 ? 342 LEU   A CB  1 
ATOM   2632 C  CG  . LEU   A 1 357 ? 20.986  39.41   25.363  1   30.22 ? 342 LEU   A CG  1 
ATOM   2633 C  CD1 . LEU   A 1 357 ? 20.818  38.671  24.025  1   30.41 ? 342 LEU   A CD1 1 
ATOM   2634 C  CD2 . LEU   A 1 357 ? 19.703  40.146  25.68   1   32.52 ? 342 LEU   A CD2 1 
ATOM   2635 N  N   . ARG   A 1 358 ? 22.751  37.147  28.978  1   26.65 ? 343 ARG   A N   1 
ATOM   2636 C  CA  . ARG   A 1 358 ? 22.747  36.166  30.052  1   25.97 ? 343 ARG   A CA  1 
ATOM   2637 C  C   . ARG   A 1 358 ? 23.148  36.768  31.388  1   27.45 ? 343 ARG   A C   1 
ATOM   2638 O  O   . ARG   A 1 358 ? 22.638  36.338  32.414  1   28.33 ? 343 ARG   A O   1 
ATOM   2639 C  CB  . ARG   A 1 358 ? 23.559  34.93   29.691  1   25.91 ? 343 ARG   A CB  1 
ATOM   2640 C  CG  . ARG   A 1 358 ? 22.921  34.198  28.515  1   25.11 ? 343 ARG   A CG  1 
ATOM   2641 C  CD  . ARG   A 1 358 ? 23.75   33.044  27.937  1   26.92 ? 343 ARG   A CD  1 
ATOM   2642 N  NE  . ARG   A 1 358 ? 22.851  32.17   27.176  1   29.93 ? 343 ARG   A NE  1 
ATOM   2643 C  CZ  . ARG   A 1 358 ? 23.128  31.645  25.99   1   31.81 ? 343 ARG   A CZ  1 
ATOM   2644 N  NH1 . ARG   A 1 358 ? 24.291  31.888  25.405  1   29.96 ? 343 ARG   A NH1 1 
ATOM   2645 N  NH2 . ARG   A 1 358 ? 22.244  30.869  25.381  1   31.28 ? 343 ARG   A NH2 1 
ATOM   2646 N  N   . SER   A 1 359 ? 24.01   37.783  31.393  1   28    ? 344 SER   A N   1 
ATOM   2647 C  CA  . SER   A 1 359 ? 24.422  38.432  32.659  1   27.81 ? 344 SER   A CA  1 
ATOM   2648 C  C   . SER   A 1 359 ? 23.231  39.244  33.232  1   28.19 ? 344 SER   A C   1 
ATOM   2649 O  O   . SER   A 1 359 ? 22.95   39.172  34.428  1   28.17 ? 344 SER   A O   1 
ATOM   2650 C  CB  . SER   A 1 359 ? 25.665  39.308  32.444  1   27.05 ? 344 SER   A CB  1 
ATOM   2651 O  OG  . SER   A 1 359 ? 26.799  38.543  32.044  1   27.43 ? 344 SER   A OG  1 
ATOM   2652 N  N   . TYR   A 1 360 ? 22.508  39.983  32.377  1   28.37 ? 345 TYR   A N   1 
ATOM   2653 C  CA  . TYR   A 1 360 ? 21.306  40.697  32.818  1   29.82 ? 345 TYR   A CA  1 
ATOM   2654 C  C   . TYR   A 1 360 ? 20.256  39.708  33.315  1   29.72 ? 345 TYR   A C   1 
ATOM   2655 O  O   . TYR   A 1 360 ? 19.682  39.891  34.394  1   30.65 ? 345 TYR   A O   1 
ATOM   2656 C  CB  . TYR   A 1 360 ? 20.707  41.539  31.7    1   30.52 ? 345 TYR   A CB  1 
ATOM   2657 C  CG  . TYR   A 1 360 ? 19.69   42.506  32.256  1   31.71 ? 345 TYR   A CG  1 
ATOM   2658 C  CD1 . TYR   A 1 360 ? 20.08   43.559  33.067  1   32.67 ? 345 TYR   A CD1 1 
ATOM   2659 C  CD2 . TYR   A 1 360 ? 18.33   42.3    32.067  1   32.38 ? 345 TYR   A CD2 1 
ATOM   2660 C  CE1 . TYR   A 1 360 ? 19.145  44.423  33.627  1   34.11 ? 345 TYR   A CE1 1 
ATOM   2661 C  CE2 . TYR   A 1 360 ? 17.386  43.175  32.595  1   33.06 ? 345 TYR   A CE2 1 
ATOM   2662 C  CZ  . TYR   A 1 360 ? 17.796  44.23   33.385  1   34.32 ? 345 TYR   A CZ  1 
ATOM   2663 O  OH  . TYR   A 1 360 ? 16.869  45.086  33.922  1   36.31 ? 345 TYR   A OH  1 
ATOM   2664 N  N   . HIS   A 1 361 ? 20.085  38.594  32.589  1   28.45 ? 346 HIS   A N   1 
ATOM   2665 C  CA  . HIS   A 1 361 ? 19.152  37.545  32.961  1   27.79 ? 346 HIS   A CA  1 
ATOM   2666 C  C   . HIS   A 1 361 ? 19.484  36.962  34.332  1   28.27 ? 346 HIS   A C   1 
ATOM   2667 O  O   . HIS   A 1 361 ? 18.579  36.764  35.123  1   29.42 ? 346 HIS   A O   1 
ATOM   2668 C  CB  . HIS   A 1 361 ? 19.119  36.454  31.866  1   26.54 ? 346 HIS   A CB  1 
ATOM   2669 C  CG  . HIS   A 1 361 ? 18.128  35.37   32.088  1   26.36 ? 346 HIS   A CG  1 
ATOM   2670 N  ND1 . HIS   A 1 361 ? 18.504  34.158  32.628  1   28.13 ? 346 HIS   A ND1 1 
ATOM   2671 C  CD2 . HIS   A 1 361 ? 16.81   35.318  31.769  1   26.63 ? 346 HIS   A CD2 1 
ATOM   2672 C  CE1 . HIS   A 1 361 ? 17.422  33.404  32.619  1   27.8  ? 346 HIS   A CE1 1 
ATOM   2673 N  NE2 . HIS   A 1 361 ? 16.367  34.071  32.151  1   28.58 ? 346 HIS   A NE2 1 
ATOM   2674 N  N   . LEU   A 1 362 ? 20.771  36.759  34.652  1   28.79 ? 347 LEU   A N   1 
ATOM   2675 C  CA  . LEU   A 1 362 ? 21.173  36.262  35.981  1   28.64 ? 347 LEU   A CA  1 
ATOM   2676 C  C   . LEU   A 1 362 ? 20.809  37.251  37.08   1   28.38 ? 347 LEU   A C   1 
ATOM   2677 O  O   . LEU   A 1 362 ? 20.486  36.825  38.189  1   28.82 ? 347 LEU   A O   1 
ATOM   2678 C  CB  . LEU   A 1 362 ? 22.676  35.926  36.042  1   29.67 ? 347 LEU   A CB  1 
ATOM   2679 C  CG  . LEU   A 1 362 ? 23.051  34.504  35.568  1   31.77 ? 347 LEU   A CG  1 
ATOM   2680 C  CD1 . LEU   A 1 362 ? 24.503  34.458  35.091  1   32.77 ? 347 LEU   A CD1 1 
ATOM   2681 C  CD2 . LEU   A 1 362 ? 22.849  33.493  36.682  1   31.74 ? 347 LEU   A CD2 1 
ATOM   2682 N  N   . GLN   A 1 363 ? 20.829  38.562  36.792  1   28.12 ? 348 GLN   A N   1 
ATOM   2683 C  CA  . GLN   A 1 363 ? 20.438  39.561  37.793  1   29.18 ? 348 GLN   A CA  1 
ATOM   2684 C  C   . GLN   A 1 363 ? 18.932  39.482  38.021  1   29.03 ? 348 GLN   A C   1 
ATOM   2685 O  O   . GLN   A 1 363 ? 18.471  39.642  39.149  1   29.61 ? 348 GLN   A O   1 
ATOM   2686 C  CB  . GLN   A 1 363 ? 20.781  40.992  37.354  1   32.17 ? 348 GLN   A CB  1 
ATOM   2687 C  CG  . GLN   A 1 363 ? 22.247  41.254  37.064  1   39.47 ? 348 GLN   A CG  1 
ATOM   2688 C  CD  . GLN   A 1 363 ? 22.388  42.682  36.563  1   48.46 ? 348 GLN   A CD  1 
ATOM   2689 O  OE1 . GLN   A 1 363 ? 21.801  43.616  37.12   1   51.56 ? 348 GLN   A OE1 1 
ATOM   2690 N  NE2 . GLN   A 1 363 ? 23.153  42.882  35.491  1   50.26 ? 348 GLN   A NE2 1 
ATOM   2691 N  N   . ILE   A 1 364 ? 18.148  39.255  36.953  1   28.51 ? 349 ILE   A N   1 
ATOM   2692 C  CA  . ILE   A 1 364 ? 16.696  39.077  37.057  1   29.25 ? 349 ILE   A CA  1 
ATOM   2693 C  C   . ILE   A 1 364 ? 16.396  37.879  37.93   1   30.46 ? 349 ILE   A C   1 
ATOM   2694 O  O   . ILE   A 1 364 ? 15.54   37.965  38.805  1   31.58 ? 349 ILE   A O   1 
ATOM   2695 C  CB  . ILE   A 1 364 ? 16.098  38.911  35.642  1   30.43 ? 349 ILE   A CB  1 
ATOM   2696 C  CG1 . ILE   A 1 364 ? 16.065  40.262  34.921  1   31.91 ? 349 ILE   A CG1 1 
ATOM   2697 C  CG2 . ILE   A 1 364 ? 14.709  38.276  35.659  1   30.87 ? 349 ILE   A CG2 1 
ATOM   2698 C  CD1 . ILE   A 1 364 ? 15.77   40.095  33.426  1   34.48 ? 349 ILE   A CD1 1 
ATOM   2699 N  N   . VAL   A 1 365 ? 17.093  36.764  37.712  1   30.54 ? 350 VAL   A N   1 
ATOM   2700 C  CA  . VAL   A 1 365 ? 16.849  35.535  38.471  1   30.93 ? 350 VAL   A CA  1 
ATOM   2701 C  C   . VAL   A 1 365 ? 17.154  35.705  39.956  1   32.04 ? 350 VAL   A C   1 
ATOM   2702 O  O   . VAL   A 1 365 ? 16.444  35.151  40.8    1   32.13 ? 350 VAL   A O   1 
ATOM   2703 C  CB  . VAL   A 1 365 ? 17.57   34.341  37.844  1   31.38 ? 350 VAL   A CB  1 
ATOM   2704 C  CG1 . VAL   A 1 365 ? 17.468  33.101  38.727  1   32.4  ? 350 VAL   A CG1 1 
ATOM   2705 C  CG2 . VAL   A 1 365 ? 16.997  34.053  36.459  1   32.1  ? 350 VAL   A CG2 1 
ATOM   2706 N  N   . THR   A 1 366 ? 18.159  36.507  40.292  1   32.62 ? 351 THR   A N   1 
ATOM   2707 C  CA  . THR   A 1 366 ? 18.472  36.797  41.7    1   33.43 ? 351 THR   A CA  1 
ATOM   2708 C  C   . THR   A 1 366 ? 17.271  37.526  42.36   1   33.97 ? 351 THR   A C   1 
ATOM   2709 O  O   . THR   A 1 366 ? 16.807  37.145  43.441  1   34.65 ? 351 THR   A O   1 
ATOM   2710 C  CB  . THR   A 1 366 ? 19.749  37.646  41.766  1   34.8  ? 351 THR   A CB  1 
ATOM   2711 O  OG1 . THR   A 1 366 ? 20.825  36.892  41.175  1   35.94 ? 351 THR   A OG1 1 
ATOM   2712 C  CG2 . THR   A 1 366 ? 20.074  38.075  43.177  1   34.74 ? 351 THR   A CG2 1 
ATOM   2713 N  N   . LYS   A 1 367 ? 16.721  38.523  41.669  1   33.34 ? 352 LYS   A N   1 
ATOM   2714 C  CA  . LYS   A 1 367 ? 15.58   39.275  42.169  1   33.01 ? 352 LYS   A CA  1 
ATOM   2715 C  C   . LYS   A 1 367 ? 14.282  38.453  42.21   1   32.95 ? 352 LYS   A C   1 
ATOM   2716 O  O   . LYS   A 1 367 ? 13.534  38.542  43.168  1   32.97 ? 352 LYS   A O   1 
ATOM   2717 C  CB  . LYS   A 1 367 ? 15.369  40.556  41.308  1   32.89 ? 352 LYS   A CB  1 
ATOM   2718 C  CG  . LYS   A 1 367 ? 14.098  41.327  41.628  1   32.74 ? 352 LYS   A CG  1 
ATOM   2719 C  CD  . LYS   A 1 367 ? 14.001  42.65   40.848  1   33.74 ? 352 LYS   A CD  1 
ATOM   2720 C  CE  . LYS   A 1 367 ? 12.609  43.266  40.978  1   37.37 ? 352 LYS   A CE  1 
ATOM   2721 N  NZ  . LYS   A 1 367 ? 12.454  44.497  40.138  1   35.54 ? 352 LYS   A NZ  1 
ATOM   2722 N  N   . TYR   A 1 368 ? 13.986  37.7    41.153  1   33.23 ? 353 TYR   A N   1 
ATOM   2723 C  CA  . TYR   A 1 368 ? 12.711  37.002  41.038  1   33.17 ? 353 TYR   A CA  1 
ATOM   2724 C  C   . TYR   A 1 368 ? 12.677  35.606  41.656  1   33.98 ? 353 TYR   A C   1 
ATOM   2725 O  O   . TYR   A 1 368 ? 11.584  35.116  41.93   1   34.43 ? 353 TYR   A O   1 
ATOM   2726 C  CB  . TYR   A 1 368 ? 12.246  36.967  39.57   1   31.99 ? 353 TYR   A CB  1 
ATOM   2727 C  CG  . TYR   A 1 368 ? 11.745  38.327  39.147  1   31.43 ? 353 TYR   A CG  1 
ATOM   2728 C  CD1 . TYR   A 1 368 ? 12.616  39.29   38.652  1   32.04 ? 353 TYR   A CD1 1 
ATOM   2729 C  CD2 . TYR   A 1 368 ? 10.431  38.697  39.361  1   31.23 ? 353 TYR   A CD2 1 
ATOM   2730 C  CE1 . TYR   A 1 368 ? 12.168  40.561  38.306  1   32.67 ? 353 TYR   A CE1 1 
ATOM   2731 C  CE2 . TYR   A 1 368 ? 9.986   39.978  39.072  1   32.16 ? 353 TYR   A CE2 1 
ATOM   2732 C  CZ  . TYR   A 1 368 ? 10.852  40.904  38.522  1   33.06 ? 353 TYR   A CZ  1 
ATOM   2733 O  OH  . TYR   A 1 368 ? 10.405  42.156  38.196  1   35.37 ? 353 TYR   A OH  1 
ATOM   2734 N  N   . ILE   A 1 369 ? 13.833  34.965  41.868  1   34.16 ? 354 ILE   A N   1 
ATOM   2735 C  CA  . ILE   A 1 369 ? 13.859  33.618  42.421  1   34.99 ? 354 ILE   A CA  1 
ATOM   2736 C  C   . ILE   A 1 369 ? 14.721  33.531  43.68   1   36.92 ? 354 ILE   A C   1 
ATOM   2737 O  O   . ILE   A 1 369 ? 14.213  33.134  44.723  1   37.47 ? 354 ILE   A O   1 
ATOM   2738 C  CB  . ILE   A 1 369 ? 14.236  32.542  41.364  1   34.9  ? 354 ILE   A CB  1 
ATOM   2739 C  CG1 . ILE   A 1 369 ? 13.135  32.414  40.297  1   35.51 ? 354 ILE   A CG1 1 
ATOM   2740 C  CG2 . ILE   A 1 369 ? 14.514  31.17   42.042  1   35.35 ? 354 ILE   A CG2 1 
ATOM   2741 C  CD1 . ILE   A 1 369 ? 13.417  31.461  39.192  1   36.73 ? 354 ILE   A CD1 1 
ATOM   2742 N  N   . LEU   A 1 370 ? 16.001  33.901  43.593  1   37.99 ? 355 LEU   A N   1 
ATOM   2743 C  CA  . LEU   A 1 370 ? 16.93   33.774  44.714  1   39.41 ? 355 LEU   A CA  1 
ATOM   2744 C  C   . LEU   A 1 370 ? 16.51   34.473  45.984  1   40.06 ? 355 LEU   A C   1 
ATOM   2745 O  O   . LEU   A 1 370 ? 16.5    33.835  47.043  1   39.23 ? 355 LEU   A O   1 
ATOM   2746 C  CB  . LEU   A 1 370 ? 18.337  34.218  44.315  1   39.76 ? 355 LEU   A CB  1 
ATOM   2747 C  CG  . LEU   A 1 370 ? 19.148  33.303  43.403  1   41.87 ? 355 LEU   A CG  1 
ATOM   2748 C  CD1 . LEU   A 1 370 ? 20.618  33.675  43.503  1   42.95 ? 355 LEU   A CD1 1 
ATOM   2749 C  CD2 . LEU   A 1 370 ? 18.949  31.792  43.753  1   42.82 ? 355 LEU   A CD2 1 
ATOM   2750 N  N   . ILE   A 1 371 ? 16.179  35.763  45.893  1   41.39 ? 356 ILE   A N   1 
ATOM   2751 C  CA  . ILE   A 1 371 ? 15.766  36.526  47.054  1   44.19 ? 356 ILE   A CA  1 
ATOM   2752 C  C   . ILE   A 1 371 ? 14.441  35.989  47.634  1   46.48 ? 356 ILE   A C   1 
ATOM   2753 O  O   . ILE   A 1 371 ? 14.457  35.577  48.802  1   47.89 ? 356 ILE   A O   1 
ATOM   2754 C  CB  . ILE   A 1 371 ? 15.765  38.043  46.764  1   45.11 ? 356 ILE   A CB  1 
ATOM   2755 C  CG1 . ILE   A 1 371 ? 17.204  38.54   46.524  1   46.1  ? 356 ILE   A CG1 1 
ATOM   2756 C  CG2 . ILE   A 1 371 ? 15.111  38.806  47.912  1   46.03 ? 356 ILE   A CG2 1 
ATOM   2757 C  CD1 . ILE   A 1 371 ? 17.296  40.011  46.094  1   47.51 ? 356 ILE   A CD1 1 
ATOM   2758 N  N   . PRO   A 1 372 ? 13.342  35.827  46.849  1   46.4  ? 357 PRO   A N   1 
ATOM   2759 C  CA  . PRO   A 1 372 ? 12.123  35.242  47.432  1   46.63 ? 357 PRO   A CA  1 
ATOM   2760 C  C   . PRO   A 1 372 ? 12.33   33.867  48.076  1   47.47 ? 357 PRO   A C   1 
ATOM   2761 O  O   . PRO   A 1 372 ? 11.786  33.634  49.146  1   47.63 ? 357 PRO   A O   1 
ATOM   2762 C  CB  . PRO   A 1 372 ? 11.14   35.208  46.249  1   47.24 ? 357 PRO   A CB  1 
ATOM   2763 C  CG  . PRO   A 1 372 ? 11.62   36.296  45.317  1   47.73 ? 357 PRO   A CG  1 
ATOM   2764 C  CD  . PRO   A 1 372 ? 13.123  36.238  45.442  1   45.9  ? 357 PRO   A CD  1 
ATOM   2765 N  N   . ALA   A 1 373 ? 13.159  32.996  47.492  1   47.9  ? 358 ALA   A N   1 
ATOM   2766 C  CA  . ALA   A 1 373 ? 13.43   31.68   48.084  1   49.31 ? 358 ALA   A CA  1 
ATOM   2767 C  C   . ALA   A 1 373 ? 14.112  31.792  49.452  1   52.53 ? 358 ALA   A C   1 
ATOM   2768 O  O   . ALA   A 1 373 ? 13.93   30.919  50.308  1   52.64 ? 358 ALA   A O   1 
ATOM   2769 C  CB  . ALA   A 1 373 ? 14.296  30.854  47.16   1   48.41 ? 358 ALA   A CB  1 
ATOM   2770 N  N   . SER   A 1 374 ? 14.931  32.843  49.642  1   54.39 ? 359 SER   A N   1 
ATOM   2771 C  CA  . SER   A 1 374 ? 15.642  33.087  50.894  1   56.85 ? 359 SER   A CA  1 
ATOM   2772 C  C   . SER   A 1 374 ? 14.711  33.577  52.001  1   59.95 ? 359 SER   A C   1 
ATOM   2773 O  O   . SER   A 1 374 ? 15.028  33.397  53.179  1   60.56 ? 359 SER   A O   1 
ATOM   2774 C  CB  . SER   A 1 374 ? 16.772  34.095  50.689  1   57.48 ? 359 SER   A CB  1 
ATOM   2775 O  OG  . SER   A 1 374 ? 16.292  35.43   50.604  1   58.73 ? 359 SER   A OG  1 
ATOM   2776 N  N   . GLN   A 1 375 ? 13.582  34.215  51.639  1   61.71 ? 360 GLN   A N   1 
ATOM   2777 C  CA  . GLN   A 1 375 ? 12.622  34.725  52.613  1   63.89 ? 360 GLN   A CA  1 
ATOM   2778 C  C   . GLN   A 1 375 ? 11.53   33.707  52.978  1   66.22 ? 360 GLN   A C   1 
ATOM   2779 O  O   . GLN   A 1 375 ? 10.477  34.111  53.468  1   67.08 ? 360 GLN   A O   1 
ATOM   2780 C  CB  . GLN   A 1 375 ? 11.991  36.023  52.105  1   65.15 ? 360 GLN   A CB  1 
ATOM   2781 C  CG  . GLN   A 1 375 ? 13.014  37.125  51.853  1   68.02 ? 360 GLN   A CG  1 
ATOM   2782 C  CD  . GLN   A 1 375 ? 12.535  38.142  50.846  1   71.9  ? 360 GLN   A CD  1 
ATOM   2783 O  OE1 . GLN   A 1 375 ? 11.648  37.873  50.021  1   73.8  ? 360 GLN   A OE1 1 
ATOM   2784 N  NE2 . GLN   A 1 375 ? 13.123  39.335  50.878  1   71.79 ? 360 GLN   A NE2 1 
ATOM   2785 N  N   . GLN   A 1 376 ? 11.788  32.394  52.77   1   66.99 ? 361 GLN   A N   1 
ATOM   2786 C  CA  . GLN   A 1 376 ? 10.861  31.298  53.089  1   68.28 ? 361 GLN   A CA  1 
ATOM   2787 C  C   . GLN   A 1 376 ? 10.841  30.968  54.599  1   69.3  ? 361 GLN   A C   1 
ATOM   2788 O  O   . GLN   A 1 376 ? 11.883  30.696  55.207  1   69.67 ? 361 GLN   A O   1 
ATOM   2789 C  CB  . GLN   A 1 376 ? 11.241  30.031  52.298  1   69.75 ? 361 GLN   A CB  1 
ATOM   2790 C  CG  . GLN   A 1 376 ? 10.72   29.989  50.869  1   72.59 ? 361 GLN   A CG  1 
ATOM   2791 N  N   . GLY   A 1 396 ? 16.879  26.853  43.866  1   57    ? 381 GLY   A N   1 
ATOM   2792 C  CA  . GLY   A 1 396 ? 17.467  28.106  43.403  1   57.65 ? 381 GLY   A CA  1 
ATOM   2793 C  C   . GLY   A 1 396 ? 18.925  27.939  43.02   1   58.48 ? 381 GLY   A C   1 
ATOM   2794 O  O   . GLY   A 1 396 ? 19.361  28.407  41.963  1   58.67 ? 381 GLY   A O   1 
ATOM   2795 N  N   . THR   A 1 397 ? 19.677  27.238  43.875  1   58.7  ? 382 THR   A N   1 
ATOM   2796 C  CA  . THR   A 1 397 ? 21.105  26.942  43.7    1   58.96 ? 382 THR   A CA  1 
ATOM   2797 C  C   . THR   A 1 397 ? 21.37   26.239  42.354  1   57.21 ? 382 THR   A C   1 
ATOM   2798 O  O   . THR   A 1 397 ? 22.254  26.655  41.605  1   57.23 ? 382 THR   A O   1 
ATOM   2799 C  CB  . THR   A 1 397 ? 21.711  26.173  44.95   1   61.9  ? 382 THR   A CB  1 
ATOM   2800 O  OG1 . THR   A 1 397 ? 22.647  25.149  44.546  1   63.41 ? 382 THR   A OG1 1 
ATOM   2801 C  CG2 . THR   A 1 397 ? 20.644  25.552  45.906  1   62.72 ? 382 THR   A CG2 1 
ATOM   2802 N  N   . ASP   A 1 398 ? 20.599  25.194  42.054  1   55.56 ? 383 ASP   A N   1 
ATOM   2803 C  CA  . ASP   A 1 398 ? 20.778  24.447  40.812  1   54.37 ? 383 ASP   A CA  1 
ATOM   2804 C  C   . ASP   A 1 398 ? 20.384  25.247  39.589  1   51.59 ? 383 ASP   A C   1 
ATOM   2805 O  O   . ASP   A 1 398 ? 21.004  25.081  38.544  1   51.05 ? 383 ASP   A O   1 
ATOM   2806 C  CB  . ASP   A 1 398 ? 20.042  23.107  40.846  1   58.06 ? 383 ASP   A CB  1 
ATOM   2807 C  CG  . ASP   A 1 398 ? 20.556  22.191  41.939  1   67.24 ? 383 ASP   A CG  1 
ATOM   2808 O  OD1 . ASP   A 1 398 ? 20.276  22.475  43.134  1   69.04 ? 383 ASP   A OD1 1 
ATOM   2809 O  OD2 . ASP   A 1 398 ? 21.254  21.197  41.605  1   71.07 ? 383 ASP   A OD2 1 
ATOM   2810 N  N   . LEU   A 1 399 ? 19.379  26.131  39.72   1   49.57 ? 384 LEU   A N   1 
ATOM   2811 C  CA  . LEU   A 1 399 ? 18.938  27.016  38.631  1   47.95 ? 384 LEU   A CA  1 
ATOM   2812 C  C   . LEU   A 1 399 ? 20.055  27.99   38.327  1   45.1  ? 384 LEU   A C   1 
ATOM   2813 O  O   . LEU   A 1 399 ? 20.376  28.185  37.158  1   44.12 ? 384 LEU   A O   1 
ATOM   2814 C  CB  . LEU   A 1 399 ? 17.657  27.833  38.997  1   48.17 ? 384 LEU   A CB  1 
ATOM   2815 C  CG  . LEU   A 1 399 ? 16.429  27.051  39.455  1   50.46 ? 384 LEU   A CG  1 
ATOM   2816 C  CD1 . LEU   A 1 399 ? 15.224  27.952  39.556  1   50.95 ? 384 LEU   A CD1 1 
ATOM   2817 C  CD2 . LEU   A 1 399 ? 16.126  25.876  38.53   1   51.69 ? 384 LEU   A CD2 1 
ATOM   2818 N  N   . MET   A 1 400 ? 20.64   28.601  39.386  1   43.67 ? 385 MET   A N   1 
ATOM   2819 C  CA  . MET   A 1 400 ? 21.729  29.554  39.251  1   43.22 ? 385 MET   A CA  1 
ATOM   2820 C  C   . MET   A 1 400 ? 22.937  28.889  38.641  1   41.06 ? 385 MET   A C   1 
ATOM   2821 O  O   . MET   A 1 400 ? 23.565  29.482  37.777  1   41.74 ? 385 MET   A O   1 
ATOM   2822 C  CB  . MET   A 1 400 ? 22.089  30.177  40.599  1   45.26 ? 385 MET   A CB  1 
ATOM   2823 C  CG  . MET   A 1 400 ? 21.053  31.134  41.078  1   50    ? 385 MET   A CG  1 
ATOM   2824 S  SD  . MET   A 1 400 ? 20.8    32.587  39.973  1   61.16 ? 385 MET   A SD  1 
ATOM   2825 C  CE  . MET   A 1 400 ? 22.186  33.605  40.347  1   58.35 ? 385 MET   A CE  1 
ATOM   2826 N  N   . ASN   A 1 401 ? 23.251  27.662  39.06   1   38.8  ? 386 ASN   A N   1 
ATOM   2827 C  CA  . ASN   A 1 401 ? 24.408  26.958  38.534  1   38.09 ? 386 ASN   A CA  1 
ATOM   2828 C  C   . ASN   A 1 401 ? 24.228  26.624  37.067  1   35.74 ? 386 ASN   A C   1 
ATOM   2829 O  O   . ASN   A 1 401 ? 25.173  26.784  36.293  1   36.66 ? 386 ASN   A O   1 
ATOM   2830 C  CB  . ASN   A 1 401 ? 24.737  25.718  39.365  1   41.38 ? 386 ASN   A CB  1 
ATOM   2831 C  CG  . ASN   A 1 401 ? 25.311  26.055  40.743  1   47.53 ? 386 ASN   A CG  1 
ATOM   2832 O  OD1 . ASN   A 1 401 ? 25.743  27.197  41.024  1   47.68 ? 386 ASN   A OD1 1 
ATOM   2833 N  ND2 . ASN   A 1 401 ? 25.293  25.066  41.641  1   49.5  ? 386 ASN   A ND2 1 
ATOM   2834 N  N   . PHE   A 1 402 ? 22.995  26.254  36.646  1   32.4  ? 387 PHE   A N   1 
ATOM   2835 C  CA  . PHE   A 1 402 ? 22.754  25.955  35.235  1   30.56 ? 387 PHE   A CA  1 
ATOM   2836 C  C   . PHE   A 1 402 ? 22.981  27.235  34.407  1   29.64 ? 387 PHE   A C   1 
ATOM   2837 O  O   . PHE   A 1 402 ? 23.744  27.196  33.455  1   29.53 ? 387 PHE   A O   1 
ATOM   2838 C  CB  . PHE   A 1 402 ? 21.328  25.409  35.017  1   29.65 ? 387 PHE   A CB  1 
ATOM   2839 C  CG  . PHE   A 1 402 ? 20.876  25.434  33.578  1   29.17 ? 387 PHE   A CG  1 
ATOM   2840 C  CD1 . PHE   A 1 402 ? 21.365  24.515  32.672  1   28.76 ? 387 PHE   A CD1 1 
ATOM   2841 C  CD2 . PHE   A 1 402 ? 19.954  26.384  33.136  1   30.01 ? 387 PHE   A CD2 1 
ATOM   2842 C  CE1 . PHE   A 1 402 ? 20.943  24.531  31.351  1   29.51 ? 387 PHE   A CE1 1 
ATOM   2843 C  CE2 . PHE   A 1 402 ? 19.548  26.414  31.813  1   29.61 ? 387 PHE   A CE2 1 
ATOM   2844 C  CZ  . PHE   A 1 402 ? 20.052  25.494  30.925  1   29.29 ? 387 PHE   A CZ  1 
ATOM   2845 N  N   . LEU   A 1 403 ? 22.367  28.36   34.82   1   28.34 ? 388 LEU   A N   1 
ATOM   2846 C  CA  . LEU   A 1 403 ? 22.51   29.644  34.147  1   27.39 ? 388 LEU   A CA  1 
ATOM   2847 C  C   . LEU   A 1 403 ? 23.971  30.133  34.134  1   27.28 ? 388 LEU   A C   1 
ATOM   2848 O  O   . LEU   A 1 403 ? 24.428  30.695  33.142  1   26.41 ? 388 LEU   A O   1 
ATOM   2849 C  CB  . LEU   A 1 403 ? 21.628  30.679  34.841  1   27.08 ? 388 LEU   A CB  1 
ATOM   2850 C  CG  . LEU   A 1 403 ? 20.119  30.421  34.745  1   28.07 ? 388 LEU   A CG  1 
ATOM   2851 C  CD1 . LEU   A 1 403 ? 19.359  31.515  35.493  1   29.36 ? 388 LEU   A CD1 1 
ATOM   2852 C  CD2 . LEU   A 1 403 ? 19.649  30.351  33.262  1   27.17 ? 388 LEU   A CD2 1 
ATOM   2853 N  N   . LYS   A 1 404 ? 24.68   29.924  35.221  1   27.83 ? 389 LYS   A N   1 
ATOM   2854 C  CA  . LYS   A 1 404 ? 26.081  30.322  35.326  1   28.94 ? 389 LYS   A CA  1 
ATOM   2855 C  C   . LYS   A 1 404 ? 26.947  29.536  34.398  1   29.02 ? 389 LYS   A C   1 
ATOM   2856 O  O   . LYS   A 1 404 ? 27.828  30.119  33.795  1   30.39 ? 389 LYS   A O   1 
ATOM   2857 C  CB  . LYS   A 1 404 ? 26.57   30.226  36.767  1   31.91 ? 389 LYS   A CB  1 
ATOM   2858 C  CG  . LYS   A 1 404 ? 26.101  31.415  37.581  1   37.4  ? 389 LYS   A CG  1 
ATOM   2859 C  CD  . LYS   A 1 404 ? 26.855  31.526  38.87   1   44.23 ? 389 LYS   A CD  1 
ATOM   2860 C  CE  . LYS   A 1 404 ? 26.063  31.077  40.071  1   51.08 ? 389 LYS   A CE  1 
ATOM   2861 N  NZ  . LYS   A 1 404 ? 26.519  31.792  41.313  1   55.18 ? 389 LYS   A NZ  1 
ATOM   2862 N  N   . THR   A 1 405 ? 26.674  28.233  34.226  1   27.99 ? 390 THR   A N   1 
ATOM   2863 C  CA  . THR   A 1 405 ? 27.417  27.386  33.312  1   26.88 ? 390 THR   A CA  1 
ATOM   2864 C  C   . THR   A 1 405 ? 27.194  27.831  31.865  1   26.92 ? 390 THR   A C   1 
ATOM   2865 O  O   . THR   A 1 405 ? 28.167  27.959  31.111  1   27.91 ? 390 THR   A O   1 
ATOM   2866 C  CB  . THR   A 1 405 ? 27.034  25.918  33.519  1   27.55 ? 390 THR   A CB  1 
ATOM   2867 O  OG1 . THR   A 1 405 ? 27.463  25.522  34.822  1   28.46 ? 390 THR   A OG1 1 
ATOM   2868 C  CG2 . THR   A 1 405 ? 27.664  25.013  32.503  1   27.48 ? 390 THR   A CG2 1 
ATOM   2869 N  N   . VAL   A 1 406 ? 25.945  28.098  31.493  1   26.56 ? 391 VAL   A N   1 
ATOM   2870 C  CA  . VAL   A 1 406 ? 25.6    28.535  30.139  1   26.14 ? 391 VAL   A CA  1 
ATOM   2871 C  C   . VAL   A 1 406 ? 26.264  29.906  29.847  1   25.29 ? 391 VAL   A C   1 
ATOM   2872 O  O   . VAL   A 1 406 ? 26.787  30.147  28.739  1   23.6  ? 391 VAL   A O   1 
ATOM   2873 C  CB  . VAL   A 1 406 ? 24.059  28.542  29.936  1   26.49 ? 391 VAL   A CB  1 
ATOM   2874 C  CG1 . VAL   A 1 406 ? 23.682  29.1    28.56   1   26.33 ? 391 VAL   A CG1 1 
ATOM   2875 C  CG2 . VAL   A 1 406 ? 23.484  27.134  30.112  1   26.83 ? 391 VAL   A CG2 1 
ATOM   2876 N  N   . ARG   A 1 407 ? 26.216  30.801  30.829  1   25.35 ? 392 ARG   A N   1 
ATOM   2877 C  CA  . ARG   A 1 407 ? 26.867  32.102  30.693  1   25.69 ? 392 ARG   A CA  1 
ATOM   2878 C  C   . ARG   A 1 407 ? 28.409  31.923  30.6    1   27.31 ? 392 ARG   A C   1 
ATOM   2879 O  O   . ARG   A 1 407 ? 29.037  32.512  29.744  1   26.92 ? 392 ARG   A O   1 
ATOM   2880 C  CB  . ARG   A 1 407 ? 26.526  32.994  31.875  1   26.19 ? 392 ARG   A CB  1 
ATOM   2881 C  CG  . ARG   A 1 407 ? 26.902  34.451  31.604  1   28.35 ? 392 ARG   A CG  1 
ATOM   2882 C  CD  . ARG   A 1 407 ? 27.451  35.021  32.887  1   32.57 ? 392 ARG   A CD  1 
ATOM   2883 N  NE  . ARG   A 1 407 ? 28.33   36.158  32.636  1   36.84 ? 392 ARG   A NE  1 
ATOM   2884 C  CZ  . ARG   A 1 407 ? 29.661  36.098  32.658  1   37.63 ? 392 ARG   A CZ  1 
ATOM   2885 N  NH1 . ARG   A 1 407 ? 30.279  34.959  32.972  1   34.11 ? 392 ARG   A NH1 1 
ATOM   2886 N  NH2 . ARG   A 1 407 ? 30.383  37.175  32.382  1   37.35 ? 392 ARG   A NH2 1 
ATOM   2887 N  N   . SER   A 1 408 ? 28.996  31.084  31.45   1   27.93 ? 393 SER   A N   1 
ATOM   2888 C  CA  . SER   A 1 408 ? 30.43   30.78   31.463  1   29.98 ? 393 SER   A CA  1 
ATOM   2889 C  C   . SER   A 1 408 ? 30.883  30.257  30.103  1   30.72 ? 393 SER   A C   1 
ATOM   2890 O  O   . SER   A 1 408 ? 31.816  30.814  29.532  1   31.24 ? 393 SER   A O   1 
ATOM   2891 C  CB  . SER   A 1 408 ? 30.747  29.734  32.537  1   32.06 ? 393 SER   A CB  1 
ATOM   2892 O  OG  . SER   A 1 408 ? 32.114  29.356  32.457  1   36.65 ? 393 SER   A OG  1 
ATOM   2893 N  N   . THR   A 1 409 ? 30.174  29.249  29.552  1   30.47 ? 394 THR   A N   1 
ATOM   2894 C  CA  . THR   A 1 409 ? 30.485  28.658  28.256  1   30.72 ? 394 THR   A CA  1 
ATOM   2895 C  C   . THR   A 1 409 ? 30.461  29.73   27.158  1   30.59 ? 394 THR   A C   1 
ATOM   2896 O  O   . THR   A 1 409 ? 31.322  29.73   26.278  1   30.09 ? 394 THR   A O   1 
ATOM   2897 C  CB  . THR   A 1 409 ? 29.517  27.473  28.005  1   32.76 ? 394 THR   A CB  1 
ATOM   2898 O  OG1 . THR   A 1 409 ? 29.663  26.519  29.065  1   34.54 ? 394 THR   A OG1 1 
ATOM   2899 C  CG2 . THR   A 1 409 ? 29.751  26.786  26.681  1   32.07 ? 394 THR   A CG2 1 
ATOM   2900 N  N   . THR   A 1 410 ? 29.507  30.673  27.24   1   29.91 ? 395 THR   A N   1 
ATOM   2901 C  CA  . THR   A 1 410 ? 29.397  31.786  26.291  1   28.84 ? 395 THR   A CA  1 
ATOM   2902 C  C   . THR   A 1 410 ? 30.613  32.703  26.442  1   29.56 ? 395 THR   A C   1 
ATOM   2903 O  O   . THR   A 1 410 ? 31.248  33.029  25.445  1   28.68 ? 395 THR   A O   1 
ATOM   2904 C  CB  . THR   A 1 410 ? 28.077  32.574  26.534  1   28.27 ? 395 THR   A CB  1 
ATOM   2905 O  OG1 . THR   A 1 410 ? 26.989  31.668  26.641  1   27.99 ? 395 THR   A OG1 1 
ATOM   2906 C  CG2 . THR   A 1 410 ? 27.777  33.561  25.438  1   27.94 ? 395 THR   A CG2 1 
ATOM   2907 N  N   . GLU   A 1 411 ? 30.925  33.144  27.674  1   29.36 ? 396 GLU   A N   1 
ATOM   2908 C  CA  . GLU   A 1 411 ? 32.076  34.017  27.906  1   31.27 ? 396 GLU   A CA  1 
ATOM   2909 C  C   . GLU   A 1 411 ? 33.428  33.395  27.438  1   30.57 ? 396 GLU   A C   1 
ATOM   2910 O  O   . GLU   A 1 411 ? 34.194  34.057  26.764  1   31.09 ? 396 GLU   A O   1 
ATOM   2911 C  CB  . GLU   A 1 411 ? 32.113  34.459  29.38   1   34.62 ? 396 GLU   A CB  1 
ATOM   2912 C  CG  . GLU   A 1 411 ? 33.032  35.64   29.613  1   40.36 ? 396 GLU   A CG  1 
ATOM   2913 C  CD  . GLU   A 1 411 ? 34.46   35.241  29.943  1   47.02 ? 396 GLU   A CD  1 
ATOM   2914 O  OE1 . GLU   A 1 411 ? 34.696  34.085  30.376  1   47.62 ? 396 GLU   A OE1 1 
ATOM   2915 O  OE2 . GLU   A 1 411 ? 35.346  36.106  29.766  1   50.21 ? 396 GLU   A OE2 1 
ATOM   2916 N  N   . LYS   A 1 412 ? 33.654  32.124  27.712  1   30.19 ? 397 LYS   A N   1 
ATOM   2917 C  CA  . LYS   A 1 412 ? 34.855  31.426  27.289  1   31.17 ? 397 LYS   A CA  1 
ATOM   2918 C  C   . LYS   A 1 412 ? 34.982  31.272  25.778  1   31.9  ? 397 LYS   A C   1 
ATOM   2919 O  O   . LYS   A 1 412 ? 36.07   30.935  25.304  1   33.66 ? 397 LYS   A O   1 
ATOM   2920 C  CB  . LYS   A 1 412 ? 34.993  30.094  27.995  1   32.7  ? 397 LYS   A CB  1 
ATOM   2921 C  CG  . LYS   A 1 412 ? 35.253  30.338  29.459  1   36.54 ? 397 LYS   A CG  1 
ATOM   2922 C  CD  . LYS   A 1 412 ? 35.494  29.095  30.244  1   40.9  ? 397 LYS   A CD  1 
ATOM   2923 C  CE  . LYS   A 1 412 ? 35.393  29.471  31.708  1   46.19 ? 397 LYS   A CE  1 
ATOM   2924 N  NZ  . LYS   A 1 412 ? 35.237  28.274  32.558  1   50.83 ? 397 LYS   A NZ  1 
ATOM   2925 N  N   . SER   A 1 413 ? 33.924  31.585  25.021  1   30.57 ? 398 SER   A N   1 
ATOM   2926 C  CA  . SER   A 1 413 ? 33.974  31.548  23.565  1   30.57 ? 398 SER   A CA  1 
ATOM   2927 C  C   . SER   A 1 413 ? 34.496  32.837  22.984  1   29.82 ? 398 SER   A C   1 
ATOM   2928 O  O   . SER   A 1 413 ? 34.678  32.904  21.778  1   29.56 ? 398 SER   A O   1 
ATOM   2929 C  CB  . SER   A 1 413 ? 32.586  31.299  22.977  1   31.59 ? 398 SER   A CB  1 
ATOM   2930 O  OG  . SER   A 1 413 ? 32.11   30.002  23.291  1   34.81 ? 398 SER   A OG  1 
ATOM   2931 N  N   . LEU   A 1 414 ? 34.695  33.891  23.783  1   29.84 ? 399 LEU   A N   1 
ATOM   2932 C  CA  . LEU   A 1 414 ? 35.244  35.145  23.26   1   31.8  ? 399 LEU   A CA  1 
ATOM   2933 C  C   . LEU   A 1 414 ? 36.681  34.868  22.73   1   34.17 ? 399 LEU   A C   1 
ATOM   2934 O  O   . LEU   A 1 414 ? 37.397  34.033  23.282  1   33.14 ? 399 LEU   A O   1 
ATOM   2935 C  CB  . LEU   A 1 414 ? 35.235  36.213  24.362  1   31.59 ? 399 LEU   A CB  1 
ATOM   2936 C  CG  . LEU   A 1 414 ? 33.877  36.849  24.603  1   31.26 ? 399 LEU   A CG  1 
ATOM   2937 C  CD1 . LEU   A 1 414 ? 33.851  37.635  25.879  1   30.99 ? 399 LEU   A CD1 1 
ATOM   2938 C  CD2 . LEU   A 1 414 ? 33.472  37.697  23.433  1   31.44 ? 399 LEU   A CD2 1 
ATOM   2939 N  N   . LEU   A 1 415 ? 36.98   35.369  21.541  1   36.61 ? 400 LEU   A N   1 
ATOM   2940 C  CA  . LEU   A 1 415 ? 38.287  35.189  20.929  1   39.35 ? 400 LEU   A CA  1 
ATOM   2941 C  C   . LEU   A 1 415 ? 39.32   36.146  21.59   1   43.14 ? 400 LEU   A C   1 
ATOM   2942 O  O   . LEU   A 1 415 ? 40.479  35.789  21.717  1   43.43 ? 400 LEU   A O   1 
ATOM   2943 C  CB  . LEU   A 1 415 ? 38.193  35.409  19.406  1   38.35 ? 400 LEU   A CB  1 
ATOM   2944 C  CG  . LEU   A 1 415 ? 37.242  34.466  18.667  1   38.15 ? 400 LEU   A CG  1 
ATOM   2945 C  CD1 . LEU   A 1 415 ? 37.307  34.693  17.171  1   38.49 ? 400 LEU   A CD1 1 
ATOM   2946 C  CD2 . LEU   A 1 415 ? 37.561  32.975  18.966  1   37.98 ? 400 LEU   A CD2 1 
ATOM   2947 N  N   . LYS   A 1 416 ? 38.87   37.322  22.068  1   46.22 ? 401 LYS   A N   1 
ATOM   2948 C  CA  . LYS   A 1 416 ? 39.724  38.3    22.718  1   49.53 ? 401 LYS   A CA  1 
ATOM   2949 C  C   . LYS   A 1 416 ? 39.269  38.648  24.152  1   53.95 ? 401 LYS   A C   1 
ATOM   2950 O  O   . LYS   A 1 416 ? 39.966  38.24   25.062  1   55.05 ? 401 LYS   A O   1 
ATOM   2951 C  CB  . LYS   A 1 416 ? 39.912  39.56   21.846  1   50.55 ? 401 LYS   A CB  1 
ATOM   2952 C  CG  . LYS   A 1 416 ? 40.707  40.667  22.51   1   54.42 ? 401 LYS   A CG  1 
ATOM   2953 C  CD  . LYS   A 1 416 ? 40.881  41.859  21.589  1   59.53 ? 401 LYS   A CD  1 
ATOM   2954 C  CE  . LYS   A 1 416 ? 41.894  42.86   22.093  1   63.75 ? 401 LYS   A CE  1 
ATOM   2955 N  NZ  . LYS   A 1 416 ? 41.329  43.804  23.097  1   65.43 ? 401 LYS   A NZ  1 
ATOM   2956 N  N   . GLU   A 1 417 ? 38.152  39.391  24.38   1   56.65 ? 402 GLU   A N   1 
ATOM   2957 C  CA  . GLU   A 1 417 ? 37.748  39.868  25.731  1   59.33 ? 402 GLU   A CA  1 
ATOM   2958 C  C   . GLU   A 1 417 ? 37.954  38.827  26.853  1   61.34 ? 402 GLU   A C   1 
ATOM   2959 O  O   . GLU   A 1 417 ? 37.153  37.904  27.02   1   62.51 ? 402 GLU   A O   1 
ATOM   2960 C  CB  . GLU   A 1 417 ? 36.305  40.421  25.739  1   62.26 ? 402 GLU   A CB  1 
ATOM   2961 C  CG  . GLU   A 1 417 ? 35.725  40.792  27.099  1   66.5  ? 402 GLU   A CG  1 
ATOM   2962 C  CD  . GLU   A 1 417 ? 36.083  42.152  27.673  1   72.9  ? 402 GLU   A CD  1 
ATOM   2963 O  OE1 . GLU   A 1 417 ? 35.188  43.026  27.721  1   73.08 ? 402 GLU   A OE1 1 
ATOM   2964 O  OE2 . GLU   A 1 417 ? 37.248  42.339  28.095  1   75.13 ? 402 GLU   A OE2 1 
ATOM   2965 N  N   . GLY   A 1 418 ? 39.063  38.978  27.573  1   61.45 ? 403 GLY   A N   1 
ATOM   2966 C  CA  . GLY   A 1 418 ? 39.443  38.098  28.661  1   61.97 ? 403 GLY   A CA  1 
ATOM   2967 C  C   . GLY   A 1 418 ? 40.2    38.889  29.723  1   61.8  ? 403 GLY   A C   1 
ATOM   2968 O  O   . GLY   A 1 418 ? 41.444  38.749  29.779  1   61.4  ? 403 GLY   A O   1 
ATOM   2969 O  OXT . GLY   A 1 418 ? 39.546  39.621  30.512  1   60.87 ? 403 GLY   A OXT 1 
ATOM   2970 N  N   . THR   B 1 25  ? 20.545  10.457  -5.704  1   55.49 ? 10  THR   B N   1 
ATOM   2971 C  CA  . THR   B 1 25  ? 21.726  10.025  -4.959  1   56.1  ? 10  THR   B CA  1 
ATOM   2972 C  C   . THR   B 1 25  ? 21.973  10.883  -3.697  1   56.8  ? 10  THR   B C   1 
ATOM   2973 O  O   . THR   B 1 25  ? 21.762  12.099  -3.715  1   57.44 ? 10  THR   B O   1 
ATOM   2974 C  CB  . THR   B 1 25  ? 22.956  9.947   -5.875  1   57.13 ? 10  THR   B CB  1 
ATOM   2975 N  N   . ILE   B 1 26  ? 22.407  10.237  -2.594  1   56.24 ? 11  ILE   B N   1 
ATOM   2976 C  CA  . ILE   B 1 26  ? 22.686  10.913  -1.323  1   55.88 ? 11  ILE   B CA  1 
ATOM   2977 C  C   . ILE   B 1 26  ? 23.949  11.757  -1.429  1   55.61 ? 11  ILE   B C   1 
ATOM   2978 O  O   . ILE   B 1 26  ? 24.933  11.314  -2.022  1   55.7  ? 11  ILE   B O   1 
ATOM   2979 C  CB  . ILE   B 1 26  ? 22.771  9.875   -0.173  1   56.23 ? 11  ILE   B CB  1 
ATOM   2980 C  CG1 . ILE   B 1 26  ? 21.384  9.281   0.135   1   56.7  ? 11  ILE   B CG1 1 
ATOM   2981 C  CG2 . ILE   B 1 26  ? 23.411  10.46   1.095   1   56.6  ? 11  ILE   B CG2 1 
ATOM   2982 C  CD1 . ILE   B 1 26  ? 21.412  8.076   1.06    1   57.69 ? 11  ILE   B CD1 1 
ATOM   2983 N  N   . SER   B 1 27  ? 23.916  12.98   -0.868  1   55.07 ? 12  SER   B N   1 
ATOM   2984 C  CA  . SER   B 1 27  ? 25.052  13.891  -0.899  1   55.25 ? 12  SER   B CA  1 
ATOM   2985 C  C   . SER   B 1 27  ? 26.304  13.279  -0.278  1   54.76 ? 12  SER   B C   1 
ATOM   2986 O  O   . SER   B 1 27  ? 26.229  12.554  0.717   1   54.89 ? 12  SER   B O   1 
ATOM   2987 C  CB  . SER   B 1 27  ? 24.707  15.202  -0.203  1   56.99 ? 12  SER   B CB  1 
ATOM   2988 O  OG  . SER   B 1 27  ? 25.802  16.1    -0.264  1   60.05 ? 12  SER   B OG  1 
ATOM   2989 N  N   . LYS   B 1 28  ? 27.458  13.569  -0.885  1   54.02 ? 13  LYS   B N   1 
ATOM   2990 C  CA  . LYS   B 1 28  ? 28.752  13.048  -0.446  1   53.33 ? 13  LYS   B CA  1 
ATOM   2991 C  C   . LYS   B 1 28  ? 29.091  13.46   0.98    1   52.07 ? 13  LYS   B C   1 
ATOM   2992 O  O   . LYS   B 1 28  ? 29.716  12.683  1.696   1   52.59 ? 13  LYS   B O   1 
ATOM   2993 C  CB  . LYS   B 1 28  ? 29.863  13.485  -1.419  1   55.21 ? 13  LYS   B CB  1 
ATOM   2994 C  CG  . LYS   B 1 28  ? 29.607  13.025  -2.855  1   59.13 ? 13  LYS   B CG  1 
ATOM   2995 N  N   . GLU   B 1 29  ? 28.637  14.643  1.413   1   50.26 ? 14  GLU   B N   1 
ATOM   2996 C  CA  . GLU   B 1 29  ? 28.913  15.154  2.757   1   49.41 ? 14  GLU   B CA  1 
ATOM   2997 C  C   . GLU   B 1 29  ? 28.289  14.332  3.909   1   46.6  ? 14  GLU   B C   1 
ATOM   2998 O  O   . GLU   B 1 29  ? 28.587  14.591  5.078   1   46.23 ? 14  GLU   B O   1 
ATOM   2999 C  CB  . GLU   B 1 29  ? 28.498  16.623  2.861   1   53.86 ? 14  GLU   B CB  1 
ATOM   3000 C  CG  . GLU   B 1 29  ? 26.991  16.818  2.795   1   63.26 ? 14  GLU   B CG  1 
ATOM   3001 C  CD  . GLU   B 1 29  ? 26.541  18.241  2.527   1   74.7  ? 14  GLU   B CD  1 
ATOM   3002 O  OE1 . GLU   B 1 29  ? 25.345  18.54   2.763   1   76.11 ? 14  GLU   B OE1 1 
ATOM   3003 O  OE2 . GLU   B 1 29  ? 27.383  19.057  2.078   1   78.77 ? 14  GLU   B OE2 1 
ATOM   3004 N  N   . TYR   B 1 30  ? 27.444  13.351  3.59    1   44.79 ? 15  TYR   B N   1 
ATOM   3005 C  CA  . TYR   B 1 30  ? 26.846  12.496  4.626   1   43.09 ? 15  TYR   B CA  1 
ATOM   3006 C  C   . TYR   B 1 30  ? 27.652  11.23   4.905   1   41.74 ? 15  TYR   B C   1 
ATOM   3007 O  O   . TYR   B 1 30  ? 27.335  10.523  5.867   1   41.24 ? 15  TYR   B O   1 
ATOM   3008 C  CB  . TYR   B 1 30  ? 25.373  12.162  4.329   1   42.32 ? 15  TYR   B CB  1 
ATOM   3009 C  CG  . TYR   B 1 30  ? 24.493  13.384  4.399   1   41.97 ? 15  TYR   B CG  1 
ATOM   3010 C  CD1 . TYR   B 1 30  ? 24.503  14.207  5.515   1   41.95 ? 15  TYR   B CD1 1 
ATOM   3011 C  CD2 . TYR   B 1 30  ? 23.681  13.74   3.332   1   42.7  ? 15  TYR   B CD2 1 
ATOM   3012 C  CE1 . TYR   B 1 30  ? 23.721  15.354  5.57    1   43.1  ? 15  TYR   B CE1 1 
ATOM   3013 C  CE2 . TYR   B 1 30  ? 22.896  14.884  3.375   1   43.55 ? 15  TYR   B CE2 1 
ATOM   3014 C  CZ  . TYR   B 1 30  ? 22.918  15.689  4.495   1   44.59 ? 15  TYR   B CZ  1 
ATOM   3015 O  OH  . TYR   B 1 30  ? 22.142  16.822  4.527   1   47.15 ? 15  TYR   B OH  1 
ATOM   3016 N  N   . HIS   B 1 31  ? 28.693  10.955  4.091   1   40.99 ? 16  HIS   B N   1 
ATOM   3017 C  CA  . HIS   B 1 31  ? 29.581  9.82    4.254   1   40.98 ? 16  HIS   B CA  1 
ATOM   3018 C  C   . HIS   B 1 31  ? 28.829  8.503   4.26    1   39.04 ? 16  HIS   B C   1 
ATOM   3019 O  O   . HIS   B 1 31  ? 29.041  7.664   5.133   1   38.45 ? 16  HIS   B O   1 
ATOM   3020 C  CB  . HIS   B 1 31  ? 30.47   9.979   5.509   1   43.4  ? 16  HIS   B CB  1 
ATOM   3021 C  CG  . HIS   B 1 31  ? 31.397  11.168  5.493   1   48.42 ? 16  HIS   B CG  1 
ATOM   3022 N  ND1 . HIS   B 1 31  ? 31.501  12.015  4.384   1   51.09 ? 16  HIS   B ND1 1 
ATOM   3023 C  CD2 . HIS   B 1 31  ? 32.248  11.606  6.451   1   49.95 ? 16  HIS   B CD2 1 
ATOM   3024 C  CE1 . HIS   B 1 31  ? 32.394  12.935  4.717   1   51.62 ? 16  HIS   B CE1 1 
ATOM   3025 N  NE2 . HIS   B 1 31  ? 32.876  12.728  5.946   1   51.37 ? 16  HIS   B NE2 1 
ATOM   3026 N  N   . ILE   B 1 32  ? 27.936  8.338   3.292   1   38.12 ? 17  ILE   B N   1 
ATOM   3027 C  CA  . ILE   B 1 32  ? 27.183  7.11    3.116   1   38.51 ? 17  ILE   B CA  1 
ATOM   3028 C  C   . ILE   B 1 32  ? 27.598  6.562   1.773   1   40.35 ? 17  ILE   B C   1 
ATOM   3029 O  O   . ILE   B 1 32  ? 27.491  7.252   0.762   1   41.52 ? 17  ILE   B O   1 
ATOM   3030 C  CB  . ILE   B 1 32  ? 25.652  7.327   3.218   1   38.32 ? 17  ILE   B CB  1 
ATOM   3031 C  CG1 . ILE   B 1 32  ? 25.293  7.818   4.62    1   39.1  ? 17  ILE   B CG1 1 
ATOM   3032 C  CG2 . ILE   B 1 32  ? 24.888  6.044   2.891   1   38.59 ? 17  ILE   B CG2 1 
ATOM   3033 C  CD1 . ILE   B 1 32  ? 24.034  8.408   4.675   1   40.39 ? 17  ILE   B CD1 1 
ATOM   3034 N  N   . ASP   B 1 33  ? 28.134  5.346   1.767   1   39.88 ? 18  ASP   B N   1 
ATOM   3035 C  CA  . ASP   B 1 33  ? 28.638  4.735   0.56    1   39.77 ? 18  ASP   B CA  1 
ATOM   3036 C  C   . ASP   B 1 33  ? 27.562  3.925   -0.122  1   40.36 ? 18  ASP   B C   1 
ATOM   3037 O  O   . ASP   B 1 33  ? 26.782  3.257   0.547   1   40.1  ? 18  ASP   B O   1 
ATOM   3038 C  CB  . ASP   B 1 33  ? 29.837  3.852   0.919   1   40.84 ? 18  ASP   B CB  1 
ATOM   3039 C  CG  . ASP   B 1 33  ? 30.567  3.325   -0.282  1   44.13 ? 18  ASP   B CG  1 
ATOM   3040 O  OD1 . ASP   B 1 33  ? 31.23   4.13    -0.968  1   46.4  ? 18  ASP   B OD1 1 
ATOM   3041 O  OD2 . ASP   B 1 33  ? 30.448  2.116   -0.559  1   43.77 ? 18  ASP   B OD2 1 
ATOM   3042 N  N   . GLU   B 1 34  ? 27.528  3.944   -1.457  1   40.83 ? 19  GLU   B N   1 
ATOM   3043 C  CA  . GLU   B 1 34  ? 26.521  3.211   -2.207  1   41.51 ? 19  GLU   B CA  1 
ATOM   3044 C  C   . GLU   B 1 34  ? 26.603  1.71    -1.953  1   41.4  ? 19  GLU   B C   1 
ATOM   3045 O  O   . GLU   B 1 34  ? 25.567  1.032   -1.913  1   41.49 ? 19  GLU   B O   1 
ATOM   3046 C  CB  . GLU   B 1 34  ? 26.616  3.522   -3.715  1   44.83 ? 19  GLU   B CB  1 
ATOM   3047 C  CG  . GLU   B 1 34  ? 25.608  2.747   -4.557  1   53.2  ? 19  GLU   B CG  1 
ATOM   3048 C  CD  . GLU   B 1 34  ? 25.618  2.989   -6.058  1   64.18 ? 19  GLU   B CD  1 
ATOM   3049 O  OE1 . GLU   B 1 34  ? 25.246  2.056   -6.809  1   65.83 ? 19  GLU   B OE1 1 
ATOM   3050 O  OE2 . GLU   B 1 34  ? 25.989  4.11    -6.484  1   67.2  ? 19  GLU   B OE2 1 
ATOM   3051 N  N   . GLU   B 1 35  ? 27.824  1.186   -1.759  1   40.57 ? 20  GLU   B N   1 
ATOM   3052 C  CA  . GLU   B 1 35  ? 27.994  -0.246  -1.55   1   39.98 ? 20  GLU   B CA  1 
ATOM   3053 C  C   . GLU   B 1 35  ? 27.941  -0.676  -0.093  1   38.88 ? 20  GLU   B C   1 
ATOM   3054 O  O   . GLU   B 1 35  ? 27.351  -1.718  0.215   1   39.46 ? 20  GLU   B O   1 
ATOM   3055 C  CB  . GLU   B 1 35  ? 29.308  -0.709  -2.181  1   42.43 ? 20  GLU   B CB  1 
ATOM   3056 C  CG  . GLU   B 1 35  ? 29.46   -2.224  -2.221  1   48.8  ? 20  GLU   B CG  1 
ATOM   3057 C  CD  . GLU   B 1 35  ? 30.801  -2.704  -2.745  1   54.64 ? 20  GLU   B CD  1 
ATOM   3058 O  OE1 . GLU   B 1 35  ? 31.77   -1.909  -2.732  1   54.29 ? 20  GLU   B OE1 1 
ATOM   3059 O  OE2 . GLU   B 1 35  ? 30.878  -3.878  -3.175  1   57.3  ? 20  GLU   B OE2 1 
ATOM   3060 N  N   . VAL   B 1 36  ? 28.595  0.073   0.797   1   37.55 ? 21  VAL   B N   1 
ATOM   3061 C  CA  . VAL   B 1 36  ? 28.704  -0.354  2.194   1   36.25 ? 21  VAL   B CA  1 
ATOM   3062 C  C   . VAL   B 1 36  ? 27.922  0.5     3.19    1   35.22 ? 21  VAL   B C   1 
ATOM   3063 O  O   . VAL   B 1 36  ? 27.9    0.157   4.361   1   35.56 ? 21  VAL   B O   1 
ATOM   3064 C  CB  . VAL   B 1 36  ? 30.177  -0.529  2.647   1   35.64 ? 21  VAL   B CB  1 
ATOM   3065 C  CG1 . VAL   B 1 36  ? 30.875  -1.569  1.791   1   35.73 ? 21  VAL   B CG1 1 
ATOM   3066 C  CG2 . VAL   B 1 36  ? 30.931  0.791   2.624   1   35.77 ? 21  VAL   B CG2 1 
ATOM   3067 N  N   . GLY   B 1 37  ? 27.281  1.572   2.738   1   34.07 ? 22  GLY   B N   1 
ATOM   3068 C  CA  . GLY   B 1 37  ? 26.39   2.368   3.572   1   33.38 ? 22  GLY   B CA  1 
ATOM   3069 C  C   . GLY   B 1 37  ? 27.047  3.216   4.616   1   32.07 ? 22  GLY   B C   1 
ATOM   3070 O  O   . GLY   B 1 37  ? 27.882  4.052   4.289   1   31.73 ? 22  GLY   B O   1 
ATOM   3071 N  N   . PHE   B 1 38  ? 26.641  3.041   5.891   1   31.76 ? 23  PHE   B N   1 
ATOM   3072 C  CA  . PHE   B 1 38  ? 27.273  3.783   6.976   1   31.28 ? 23  PHE   B CA  1 
ATOM   3073 C  C   . PHE   B 1 38  ? 28.7    3.263   7.273   1   31.43 ? 23  PHE   B C   1 
ATOM   3074 O  O   . PHE   B 1 38  ? 29.461  3.941   7.957   1   30.75 ? 23  PHE   B O   1 
ATOM   3075 C  CB  . PHE   B 1 38  ? 26.399  3.77    8.247   1   31.11 ? 23  PHE   B CB  1 
ATOM   3076 C  CG  . PHE   B 1 38  ? 25.104  4.519   8.06    1   31.42 ? 23  PHE   B CG  1 
ATOM   3077 C  CD1 . PHE   B 1 38  ? 25.092  5.902   7.975   1   32.35 ? 23  PHE   B CD1 1 
ATOM   3078 C  CD2 . PHE   B 1 38  ? 23.91   3.839   7.905   1   32.15 ? 23  PHE   B CD2 1 
ATOM   3079 C  CE1 . PHE   B 1 38  ? 23.9    6.594   7.802   1   33.51 ? 23  PHE   B CE1 1 
ATOM   3080 C  CE2 . PHE   B 1 38  ? 22.72   4.533   7.697   1   33.55 ? 23  PHE   B CE2 1 
ATOM   3081 C  CZ  . PHE   B 1 38  ? 22.727  5.909   7.645   1   33.36 ? 23  PHE   B CZ  1 
ATOM   3082 N  N   . ALA   B 1 39  ? 29.064  2.059   6.777   1   30.99 ? 24  ALA   B N   1 
ATOM   3083 C  CA  . ALA   B 1 39  ? 30.402  1.514   7.002   1   31.42 ? 24  ALA   B CA  1 
ATOM   3084 C  C   . ALA   B 1 39  ? 31.441  2.369   6.303   1   33.11 ? 24  ALA   B C   1 
ATOM   3085 O  O   . ALA   B 1 39  ? 31.143  3.013   5.29    1   32.65 ? 24  ALA   B O   1 
ATOM   3086 C  CB  . ALA   B 1 39  ? 30.482  0.081   6.495   1   30.56 ? 24  ALA   B CB  1 
ATOM   3087 N  N   . LEU   B 1 40  ? 32.643  2.427   6.867   1   34.15 ? 25  LEU   B N   1 
ATOM   3088 C  CA  . LEU   B 1 40  ? 33.734  3.188   6.256   1   35.75 ? 25  LEU   B CA  1 
ATOM   3089 C  C   . LEU   B 1 40  ? 34.231  2.384   5.07    1   36.53 ? 25  LEU   B C   1 
ATOM   3090 O  O   . LEU   B 1 40  ? 34.587  1.212   5.232   1   36.89 ? 25  LEU   B O   1 
ATOM   3091 C  CB  . LEU   B 1 40  ? 34.855  3.399   7.286   1   36.56 ? 25  LEU   B CB  1 
ATOM   3092 C  CG  . LEU   B 1 40  ? 36.038  4.269   6.875   1   39.07 ? 25  LEU   B CG  1 
ATOM   3093 C  CD1 . LEU   B 1 40  ? 35.598  5.708   6.586   1   39.33 ? 25  LEU   B CD1 1 
ATOM   3094 C  CD2 . LEU   B 1 40  ? 37.093  4.257   7.971   1   39.72 ? 25  LEU   B CD2 1 
ATOM   3095 N  N   . PRO   B 1 41  ? 34.142  2.927   3.845   1   37.07 ? 26  PRO   B N   1 
ATOM   3096 C  CA  . PRO   B 1 41  ? 34.601  2.146   2.68    1   37.18 ? 26  PRO   B CA  1 
ATOM   3097 C  C   . PRO   B 1 41  ? 36.111  1.949   2.727   1   37.95 ? 26  PRO   B C   1 
ATOM   3098 O  O   . PRO   B 1 41  ? 36.831  2.873   3.134   1   37.11 ? 26  PRO   B O   1 
ATOM   3099 C  CB  . PRO   B 1 41  ? 34.176  2.989   1.475   1   37.48 ? 26  PRO   B CB  1 
ATOM   3100 C  CG  . PRO   B 1 41  ? 34.006  4.357   2.007   1   38.09 ? 26  PRO   B CG  1 
ATOM   3101 C  CD  . PRO   B 1 41  ? 33.684  4.277   3.465   1   36.71 ? 26  PRO   B CD  1 
ATOM   3102 N  N   . ASN   B 1 42  ? 36.584  0.721   2.389   1   39.31 ? 27  ASN   B N   1 
ATOM   3103 C  CA  . ASN   B 1 42  ? 38.011  0.304   2.387   1   40.89 ? 27  ASN   B CA  1 
ATOM   3104 C  C   . ASN   B 1 42  ? 38.842  0.978   3.473   1   40.41 ? 27  ASN   B C   1 
ATOM   3105 O  O   . ASN   B 1 42  ? 39.584  1.919   3.162   1   40.14 ? 27  ASN   B O   1 
ATOM   3106 C  CB  . ASN   B 1 42  ? 38.644  0.532   0.998   1   44.26 ? 27  ASN   B CB  1 
ATOM   3107 C  CG  . ASN   B 1 42  ? 38.038  -0.342  -0.087  1   52.23 ? 27  ASN   B CG  1 
ATOM   3108 O  OD1 . ASN   B 1 42  ? 38.23   -1.58   -0.124  1   55.65 ? 27  ASN   B OD1 1 
ATOM   3109 N  ND2 . ASN   B 1 42  ? 37.271  0.273   -0.99   1   53.25 ? 27  ASN   B ND2 1 
ATOM   3110 N  N   . PRO   B 1 43  ? 38.602  0.634   4.762   1   40.16 ? 28  PRO   B N   1 
ATOM   3111 C  CA  . PRO   B 1 43  ? 39.326  1.314   5.845   1   40.63 ? 28  PRO   B CA  1 
ATOM   3112 C  C   . PRO   B 1 43  ? 40.838  1.134   5.729   1   41.76 ? 28  PRO   B C   1 
ATOM   3113 O  O   . PRO   B 1 43  ? 41.298  0.089   5.25    1   41.21 ? 28  PRO   B O   1 
ATOM   3114 C  CB  . PRO   B 1 43  ? 38.809  0.602   7.115   1   40.91 ? 28  PRO   B CB  1 
ATOM   3115 C  CG  . PRO   B 1 43  ? 37.511  -0.005  6.733   1   40.87 ? 28  PRO   B CG  1 
ATOM   3116 C  CD  . PRO   B 1 43  ? 37.727  -0.427  5.3     1   39.47 ? 28  PRO   B CD  1 
ATOM   3117 N  N   . GLN   B 1 44  ? 41.591  2.136   6.202   1   42.89 ? 29  GLN   B N   1 
ATOM   3118 C  CA  . GLN   B 1 44  ? 43.058  2.126   6.241   1   44.55 ? 29  GLN   B CA  1 
ATOM   3119 C  C   . GLN   B 1 44  ? 43.503  1.083   7.284   1   46.12 ? 29  GLN   B C   1 
ATOM   3120 O  O   . GLN   B 1 44  ? 42.965  1.07    8.393   1   46.38 ? 29  GLN   B O   1 
ATOM   3121 C  CB  . GLN   B 1 44  ? 43.562  3.515   6.658   1   45.83 ? 29  GLN   B CB  1 
ATOM   3122 C  CG  . GLN   B 1 44  ? 45.044  3.752   6.392   1   49.42 ? 29  GLN   B CG  1 
ATOM   3123 C  CD  . GLN   B 1 44  ? 45.38   5.225   6.424   1   53.13 ? 29  GLN   B CD  1 
ATOM   3124 O  OE1 . GLN   B 1 44  ? 44.707  6.054   5.799   1   54    ? 29  GLN   B OE1 1 
ATOM   3125 N  NE2 . GLN   B 1 44  ? 46.441  5.584   7.146   1   53.83 ? 29  GLN   B NE2 1 
ATOM   3126 N  N   . GLU   B 1 45  ? 44.484  0.23    6.944   1   46.34 ? 30  GLU   B N   1 
ATOM   3127 C  CA  . GLU   B 1 45  ? 44.978  -0.786  7.867   1   47.48 ? 30  GLU   B CA  1 
ATOM   3128 C  C   . GLU   B 1 45  ? 46.248  -0.356  8.598   1   48.27 ? 30  GLU   B C   1 
ATOM   3129 O  O   . GLU   B 1 45  ? 46.51   -0.844  9.696   1   48.72 ? 30  GLU   B O   1 
ATOM   3130 C  CB  . GLU   B 1 45  ? 45.274  -2.094  7.12    1   50.93 ? 30  GLU   B CB  1 
ATOM   3131 C  CG  . GLU   B 1 45  ? 44.119  -2.583  6.275   1   57.3  ? 30  GLU   B CG  1 
ATOM   3132 C  CD  . GLU   B 1 45  ? 44.476  -3.75   5.379   1   64.97 ? 30  GLU   B CD  1 
ATOM   3133 O  OE1 . GLU   B 1 45  ? 45.345  -4.565  5.771   1   65.08 ? 30  GLU   B OE1 1 
ATOM   3134 O  OE2 . GLU   B 1 45  ? 43.869  -3.858  4.287   1   67.98 ? 30  GLU   B OE2 1 
ATOM   3135 N  N   . ASN   B 1 46  ? 47.058  0.52    7.985   1   48.01 ? 31  ASN   B N   1 
ATOM   3136 C  CA  . ASN   B 1 46  ? 48.308  0.948   8.591   1   48.36 ? 31  ASN   B CA  1 
ATOM   3137 C  C   . ASN   B 1 46  ? 48.382  2.444   8.774   1   47.45 ? 31  ASN   B C   1 
ATOM   3138 O  O   . ASN   B 1 46  ? 47.886  3.19    7.944   1   47.18 ? 31  ASN   B O   1 
ATOM   3139 C  CB  . ASN   B 1 46  ? 49.483  0.457   7.745   1   50.62 ? 31  ASN   B CB  1 
ATOM   3140 C  CG  . ASN   B 1 46  ? 49.457  -1.038  7.484   1   55.04 ? 31  ASN   B CG  1 
ATOM   3141 O  OD1 . ASN   B 1 46  ? 49.601  -1.862  8.408   1   56.39 ? 31  ASN   B OD1 1 
ATOM   3142 N  ND2 . ASN   B 1 46  ? 49.256  -1.426  6.213   1   56.22 ? 31  ASN   B ND2 1 
ATOM   3143 N  N   . LEU   B 1 47  ? 48.929  2.88    9.896   1   47.4  ? 32  LEU   B N   1 
ATOM   3144 C  CA  . LEU   B 1 47  ? 49.136  4.295   10.196  1   48.37 ? 32  LEU   B CA  1 
ATOM   3145 C  C   . LEU   B 1 47  ? 50.562  4.697   9.709   1   49.87 ? 32  LEU   B C   1 
ATOM   3146 O  O   . LEU   B 1 47  ? 51.417  3.828   9.535   1   49.79 ? 32  LEU   B O   1 
ATOM   3147 C  CB  . LEU   B 1 47  ? 49.086  4.488   11.732  1   48.54 ? 32  LEU   B CB  1 
ATOM   3148 C  CG  . LEU   B 1 47  ? 47.702  4.55    12.408  1   50.03 ? 32  LEU   B CG  1 
ATOM   3149 C  CD1 . LEU   B 1 47  ? 47.833  4.756   13.924  1   50.17 ? 32  LEU   B CD1 1 
ATOM   3150 C  CD2 . LEU   B 1 47  ? 46.84   5.628   11.793  1   50.3  ? 32  LEU   B CD2 1 
ATOM   3151 N  N   . PRO   B 1 48  ? 50.88   6.004   9.583   1   51.13 ? 33  PRO   B N   1 
ATOM   3152 C  CA  . PRO   B 1 48  ? 52.267  6.396   9.262   1   51.62 ? 33  PRO   B CA  1 
ATOM   3153 C  C   . PRO   B 1 48  ? 53.266  5.848   10.301  1   52.55 ? 33  PRO   B C   1 
ATOM   3154 O  O   . PRO   B 1 48  ? 52.913  5.682   11.48   1   52.53 ? 33  PRO   B O   1 
ATOM   3155 C  CB  . PRO   B 1 48  ? 52.216  7.925   9.312   1   52.11 ? 33  PRO   B CB  1 
ATOM   3156 C  CG  . PRO   B 1 48  ? 50.773  8.268   9.063   1   52.74 ? 33  PRO   B CG  1 
ATOM   3157 C  CD  . PRO   B 1 48  ? 50.016  7.188   9.769   1   51    ? 33  PRO   B CD  1 
ATOM   3158 N  N   . ASP   B 1 49  ? 54.515  5.551   9.859   1   52.73 ? 34  ASP   B N   1 
ATOM   3159 C  CA  . ASP   B 1 49  ? 55.582  4.983   10.689  1   52.9  ? 34  ASP   B CA  1 
ATOM   3160 C  C   . ASP   B 1 49  ? 55.77   5.692   12.033  1   51.56 ? 34  ASP   B C   1 
ATOM   3161 O  O   . ASP   B 1 49  ? 56.158  5.057   13.014  1   51.49 ? 34  ASP   B O   1 
ATOM   3162 C  CB  . ASP   B 1 49  ? 56.904  4.922   9.903   1   56.51 ? 34  ASP   B CB  1 
ATOM   3163 C  CG  . ASP   B 1 49  ? 56.818  4.048   8.661   1   65.63 ? 34  ASP   B CG  1 
ATOM   3164 O  OD1 . ASP   B 1 49  ? 56.582  2.819   8.808   1   67.52 ? 34  ASP   B OD1 1 
ATOM   3165 O  OD2 . ASP   B 1 49  ? 56.983  4.588   7.537   1   69.09 ? 34  ASP   B OD2 1 
ATOM   3166 N  N   . PHE   B 1 50  ? 55.448  6.985   12.095  1   50.15 ? 35  PHE   B N   1 
ATOM   3167 C  CA  . PHE   B 1 50  ? 55.555  7.767   13.319  1   50.35 ? 35  PHE   B CA  1 
ATOM   3168 C  C   . PHE   B 1 50  ? 54.769  7.132   14.486  1   50.36 ? 35  PHE   B C   1 
ATOM   3169 O  O   . PHE   B 1 50  ? 55.199  7.219   15.632  1   51.05 ? 35  PHE   B O   1 
ATOM   3170 C  CB  . PHE   B 1 50  ? 55.043  9.187   13.046  1   50.72 ? 35  PHE   B CB  1 
ATOM   3171 C  CG  . PHE   B 1 50  ? 55.106  10.166  14.198  1   52.06 ? 35  PHE   B CG  1 
ATOM   3172 C  CD1 . PHE   B 1 50  ? 56.288  10.819  14.511  1   53.31 ? 35  PHE   B CD1 1 
ATOM   3173 C  CD2 . PHE   B 1 50  ? 53.962  10.525  14.885  1   53.22 ? 35  PHE   B CD2 1 
ATOM   3174 C  CE1 . PHE   B 1 50  ? 56.333  11.764  15.533  1   54.17 ? 35  PHE   B CE1 1 
ATOM   3175 C  CE2 . PHE   B 1 50  ? 54.012  11.451  15.923  1   54.35 ? 35  PHE   B CE2 1 
ATOM   3176 C  CZ  . PHE   B 1 50  ? 55.195  12.077  16.232  1   54.31 ? 35  PHE   B CZ  1 
ATOM   3177 N  N   . TYR   B 1 51  ? 53.643  6.454   14.178  1   49.2  ? 36  TYR   B N   1 
ATOM   3178 C  CA  . TYR   B 1 51  ? 52.759  5.835   15.175  1   48.42 ? 36  TYR   B CA  1 
ATOM   3179 C  C   . TYR   B 1 51  ? 52.99   4.348   15.387  1   49.17 ? 36  TYR   B C   1 
ATOM   3180 O  O   . TYR   B 1 51  ? 52.101  3.677   15.924  1   49.5  ? 36  TYR   B O   1 
ATOM   3181 C  CB  . TYR   B 1 51  ? 51.285  6.06    14.774  1   46.58 ? 36  TYR   B CB  1 
ATOM   3182 C  CG  . TYR   B 1 51  ? 50.957  7.525   14.645  1   45.32 ? 36  TYR   B CG  1 
ATOM   3183 C  CD1 . TYR   B 1 51  ? 50.893  8.342   15.766  1   45.48 ? 36  TYR   B CD1 1 
ATOM   3184 C  CD2 . TYR   B 1 51  ? 50.824  8.118   13.398  1   45.22 ? 36  TYR   B CD2 1 
ATOM   3185 C  CE1 . TYR   B 1 51  ? 50.594  9.689   15.658  1   46.1  ? 36  TYR   B CE1 1 
ATOM   3186 C  CE2 . TYR   B 1 51  ? 50.583  9.478   13.272  1   45.82 ? 36  TYR   B CE2 1 
ATOM   3187 C  CZ  . TYR   B 1 51  ? 50.446  10.256  14.407  1   47.17 ? 36  TYR   B CZ  1 
ATOM   3188 O  OH  . TYR   B 1 51  ? 50.187  11.6    14.311  1   49.59 ? 36  TYR   B OH  1 
ATOM   3189 N  N   . ASN   B 1 52  ? 54.165  3.826   14.984  1   48.91 ? 37  ASN   B N   1 
ATOM   3190 C  CA  . ASN   B 1 52  ? 54.485  2.401   15.117  1   48.89 ? 37  ASN   B CA  1 
ATOM   3191 C  C   . ASN   B 1 52  ? 54.305  1.879   16.549  1   47.42 ? 37  ASN   B C   1 
ATOM   3192 O  O   . ASN   B 1 52  ? 53.954  0.715   16.726  1   47.62 ? 37  ASN   B O   1 
ATOM   3193 C  CB  . ASN   B 1 52  ? 55.917  2.102   14.626  1   51.09 ? 37  ASN   B CB  1 
ATOM   3194 C  CG  . ASN   B 1 52  ? 56.047  1.829   13.142  1   56.26 ? 37  ASN   B CG  1 
ATOM   3195 O  OD1 . ASN   B 1 52  ? 55.066  1.782   12.387  1   57.71 ? 37  ASN   B OD1 1 
ATOM   3196 N  ND2 . ASN   B 1 52  ? 57.278  1.641   12.682  1   57.71 ? 37  ASN   B ND2 1 
ATOM   3197 N  N   . ASP   B 1 53  ? 54.56   2.719   17.562  1   45.55 ? 38  ASP   B N   1 
ATOM   3198 C  CA  . ASP   B 1 53  ? 54.423  2.291   18.953  1   45.11 ? 38  ASP   B CA  1 
ATOM   3199 C  C   . ASP   B 1 53  ? 52.94   2.059   19.329  1   45.04 ? 38  ASP   B C   1 
ATOM   3200 O  O   . ASP   B 1 53  ? 52.643  1.218   20.184  1   45.14 ? 38  ASP   B O   1 
ATOM   3201 C  CB  . ASP   B 1 53  ? 55.059  3.307   19.909  1   45.68 ? 38  ASP   B CB  1 
ATOM   3202 C  CG  . ASP   B 1 53  ? 56.575  3.468   19.776  1   48.69 ? 38  ASP   B CG  1 
ATOM   3203 O  OD1 . ASP   B 1 53  ? 57.241  2.528   19.245  1   47.84 ? 38  ASP   B OD1 1 
ATOM   3204 O  OD2 . ASP   B 1 53  ? 57.092  4.518   20.203  1   50.06 ? 38  ASP   B OD2 1 
ATOM   3205 N  N   . TRP   B 1 54  ? 52.018  2.816   18.709  1   44.1  ? 39  TRP   B N   1 
ATOM   3206 C  CA  . TRP   B 1 54  ? 50.588  2.624   18.946  1   43.31 ? 39  TRP   B CA  1 
ATOM   3207 C  C   . TRP   B 1 54  ? 50.19   1.345   18.259  1   44.68 ? 39  TRP   B C   1 
ATOM   3208 O  O   . TRP   B 1 54  ? 49.597  0.476   18.894  1   46.1  ? 39  TRP   B O   1 
ATOM   3209 C  CB  . TRP   B 1 54  ? 49.776  3.775   18.334  1   42.25 ? 39  TRP   B CB  1 
ATOM   3210 C  CG  . TRP   B 1 54  ? 49.823  5.08    19.057  1   41.63 ? 39  TRP   B CG  1 
ATOM   3211 C  CD1 . TRP   B 1 54  ? 50.466  5.368   20.225  1   42.17 ? 39  TRP   B CD1 1 
ATOM   3212 C  CD2 . TRP   B 1 54  ? 49.202  6.288   18.631  1   41.78 ? 39  TRP   B CD2 1 
ATOM   3213 N  NE1 . TRP   B 1 54  ? 50.27   6.684   20.557  1   42.67 ? 39  TRP   B NE1 1 
ATOM   3214 C  CE2 . TRP   B 1 54  ? 49.519  7.281   19.581  1   42.35 ? 39  TRP   B CE2 1 
ATOM   3215 C  CE3 . TRP   B 1 54  ? 48.392  6.628   17.54   1   42.37 ? 39  TRP   B CE3 1 
ATOM   3216 C  CZ2 . TRP   B 1 54  ? 49.03   8.579   19.491  1   43.18 ? 39  TRP   B CZ2 1 
ATOM   3217 C  CZ3 . TRP   B 1 54  ? 47.916  7.918   17.449  1   43.2  ? 39  TRP   B CZ3 1 
ATOM   3218 C  CH2 . TRP   B 1 54  ? 48.24   8.879   18.412  1   43.32 ? 39  TRP   B CH2 1 
ATOM   3219 N  N   . MET   B 1 55  ? 50.547  1.199   16.97   1   44.27 ? 40  MET   B N   1 
ATOM   3220 C  CA  . MET   B 1 55  ? 50.198  0.026   16.186  1   44.42 ? 40  MET   B CA  1 
ATOM   3221 C  C   . MET   B 1 55  ? 50.712  -1.256  16.767  1   44.92 ? 40  MET   B C   1 
ATOM   3222 O  O   . MET   B 1 55  ? 50.001  -2.261  16.738  1   44.95 ? 40  MET   B O   1 
ATOM   3223 C  CB  . MET   B 1 55  ? 50.66   0.174   14.736  1   45.66 ? 40  MET   B CB  1 
ATOM   3224 C  CG  . MET   B 1 55  ? 49.935  -0.763  13.766  1   48.81 ? 40  MET   B CG  1 
ATOM   3225 S  SD  . MET   B 1 55  ? 48.125  -0.467  13.583  1   53.13 ? 40  MET   B SD  1 
ATOM   3226 C  CE  . MET   B 1 55  ? 48.124  1.25    13.376  1   45.2  ? 40  MET   B CE  1 
ATOM   3227 N  N   . PHE   B 1 56  ? 51.945  -1.254  17.318  1   45.03 ? 41  PHE   B N   1 
ATOM   3228 C  CA  . PHE   B 1 56  ? 52.492  -2.47   17.924  1   45.1  ? 41  PHE   B CA  1 
ATOM   3229 C  C   . PHE   B 1 56  ? 51.584  -2.961  19.064  1   43.14 ? 41  PHE   B C   1 
ATOM   3230 O  O   . PHE   B 1 56  ? 51.258  -4.141  19.099  1   43.65 ? 41  PHE   B O   1 
ATOM   3231 C  CB  . PHE   B 1 56  ? 53.962  -2.296  18.406  1   46.28 ? 41  PHE   B CB  1 
ATOM   3232 C  CG  . PHE   B 1 56  ? 54.407  -3.448  19.286  1   48.57 ? 41  PHE   B CG  1 
ATOM   3233 C  CD1 . PHE   B 1 56  ? 54.65   -4.701  18.743  1   50.08 ? 41  PHE   B CD1 1 
ATOM   3234 C  CD2 . PHE   B 1 56  ? 54.432  -3.317  20.668  1   50.04 ? 41  PHE   B CD2 1 
ATOM   3235 C  CE1 . PHE   B 1 56  ? 54.959  -5.783  19.555  1   51.04 ? 41  PHE   B CE1 1 
ATOM   3236 C  CE2 . PHE   B 1 56  ? 54.741  -4.403  21.478  1   51.34 ? 41  PHE   B CE2 1 
ATOM   3237 C  CZ  . PHE   B 1 56  ? 54.997  -5.631  20.916  1   51.12 ? 41  PHE   B CZ  1 
ATOM   3238 N  N   . ILE   B 1 57  ? 51.181  -2.057  19.968  1   41.2  ? 42  ILE   B N   1 
ATOM   3239 C  CA  . ILE   B 1 57  ? 50.334  -2.418  21.096  1   40.53 ? 42  ILE   B CA  1 
ATOM   3240 C  C   . ILE   B 1 57  ? 48.967  -2.948  20.635  1   41.07 ? 42  ILE   B C   1 
ATOM   3241 O  O   . ILE   B 1 57  ? 48.573  -4.049  21.019  1   41.66 ? 42  ILE   B O   1 
ATOM   3242 C  CB  . ILE   B 1 57  ? 50.197  -1.219  22.054  1   39.84 ? 42  ILE   B CB  1 
ATOM   3243 C  CG1 . ILE   B 1 57  ? 51.563  -0.812  22.654  1   39.73 ? 42  ILE   B CG1 1 
ATOM   3244 C  CG2 . ILE   B 1 57  ? 49.184  -1.527  23.153  1   40.12 ? 42  ILE   B CG2 1 
ATOM   3245 C  CD1 . ILE   B 1 57  ? 51.497  0.44    23.549  1   41.04 ? 42  ILE   B CD1 1 
ATOM   3246 N  N   . ALA   B 1 58  ? 48.285  -2.197  19.754  1   40.81 ? 43  ALA   B N   1 
ATOM   3247 C  CA  . ALA   B 1 58  ? 46.966  -2.544  19.222  1   40.42 ? 43  ALA   B CA  1 
ATOM   3248 C  C   . ALA   B 1 58  ? 46.972  -3.866  18.485  1   40.89 ? 43  ALA   B C   1 
ATOM   3249 O  O   . ALA   B 1 58  ? 46.052  -4.669  18.662  1   40.76 ? 43  ALA   B O   1 
ATOM   3250 C  CB  . ALA   B 1 58  ? 46.471  -1.448  18.315  1   40.48 ? 43  ALA   B CB  1 
ATOM   3251 N  N   . LYS   B 1 59  ? 48.023  -4.129  17.691  1   41.04 ? 44  LYS   B N   1 
ATOM   3252 C  CA  . LYS   B 1 59  ? 48.1    -5.39   16.953  1   41.53 ? 44  LYS   B CA  1 
ATOM   3253 C  C   . LYS   B 1 59  ? 48.41   -6.598  17.829  1   41.47 ? 44  LYS   B C   1 
ATOM   3254 O  O   . LYS   B 1 59  ? 48.242  -7.73   17.374  1   41.93 ? 44  LYS   B O   1 
ATOM   3255 C  CB  . LYS   B 1 59  ? 49.12   -5.281  15.817  1   44.48 ? 44  LYS   B CB  1 
ATOM   3256 C  CG  . LYS   B 1 59  ? 48.598  -4.499  14.617  1   48.98 ? 44  LYS   B CG  1 
ATOM   3257 C  CD  . LYS   B 1 59  ? 49.641  -4.457  13.499  0.5 53.07 ? 44  LYS   B CD  1 
ATOM   3258 N  N   . HIS   B 1 60  ? 48.846  -6.379  19.083  1   41.36 ? 45  HIS   B N   1 
ATOM   3259 C  CA  . HIS   B 1 60  ? 49.216  -7.487  19.959  1   42.03 ? 45  HIS   B CA  1 
ATOM   3260 C  C   . HIS   B 1 60  ? 48.459  -7.5    21.269  1   41.24 ? 45  HIS   B C   1 
ATOM   3261 O  O   . HIS   B 1 60  ? 48.968  -8.044  22.252  1   41.18 ? 45  HIS   B O   1 
ATOM   3262 C  CB  . HIS   B 1 60  ? 50.745  -7.486  20.208  1   44.29 ? 45  HIS   B CB  1 
ATOM   3263 C  CG  . HIS   B 1 60  ? 51.527  -7.696  18.956  1   47.9  ? 45  HIS   B CG  1 
ATOM   3264 N  ND1 . HIS   B 1 60  ? 52.018  -6.631  18.224  1   50.54 ? 45  HIS   B ND1 1 
ATOM   3265 C  CD2 . HIS   B 1 60  ? 51.783  -8.843  18.288  1   49.36 ? 45  HIS   B CD2 1 
ATOM   3266 C  CE1 . HIS   B 1 60  ? 52.576  -7.166  17.153  1   51.23 ? 45  HIS   B CE1 1 
ATOM   3267 N  NE2 . HIS   B 1 60  ? 52.453  -8.493  17.148  1   50.75 ? 45  HIS   B NE2 1 
ATOM   3268 N  N   . LEU   B 1 61  ? 47.226  -6.94   21.288  1   40    ? 46  LEU   B N   1 
ATOM   3269 C  CA  . LEU   B 1 61  ? 46.412  -6.927  22.507  1   39.13 ? 46  LEU   B CA  1 
ATOM   3270 C  C   . LEU   B 1 61  ? 46.205  -8.312  23.095  1   38.33 ? 46  LEU   B C   1 
ATOM   3271 O  O   . LEU   B 1 61  ? 46.408  -8.465  24.297  1   38.57 ? 46  LEU   B O   1 
ATOM   3272 C  CB  . LEU   B 1 61  ? 45.055  -6.213  22.315  1   38.83 ? 46  LEU   B CB  1 
ATOM   3273 C  CG  . LEU   B 1 61  ? 45.116  -4.703  22.114  1   40.36 ? 46  LEU   B CG  1 
ATOM   3274 C  CD1 . LEU   B 1 61  ? 43.712  -4.117  21.899  1   40.49 ? 46  LEU   B CD1 1 
ATOM   3275 C  CD2 . LEU   B 1 61  ? 45.826  -4      23.283  1   40.43 ? 46  LEU   B CD2 1 
ATOM   3276 N  N   . PRO   B 1 62  ? 45.868  -9.361  22.302  1   37.39 ? 47  PRO   B N   1 
ATOM   3277 C  CA  . PRO   B 1 62  ? 45.663  -10.679 22.913  1   36.94 ? 47  PRO   B CA  1 
ATOM   3278 C  C   . PRO   B 1 62  ? 46.884  -11.149 23.709  1   36.96 ? 47  PRO   B C   1 
ATOM   3279 O  O   . PRO   B 1 62  ? 46.743  -11.537 24.858  1   36.8  ? 47  PRO   B O   1 
ATOM   3280 C  CB  . PRO   B 1 62  ? 45.337  -11.586 21.714  1   37.84 ? 47  PRO   B CB  1 
ATOM   3281 C  CG  . PRO   B 1 62  ? 44.779  -10.661 20.682  1   37.96 ? 47  PRO   B CG  1 
ATOM   3282 C  CD  . PRO   B 1 62  ? 45.579  -9.392  20.851  1   36.52 ? 47  PRO   B CD  1 
ATOM   3283 N  N   . ASP   B 1 63  ? 48.08   -11.01  23.138  1   37.31 ? 48  ASP   B N   1 
ATOM   3284 C  CA  . ASP   B 1 63  ? 49.336  -11.42  23.78   1   38    ? 48  ASP   B CA  1 
ATOM   3285 C  C   . ASP   B 1 63  ? 49.699  -10.539 24.946  1   37.09 ? 48  ASP   B C   1 
ATOM   3286 O  O   . ASP   B 1 63  ? 49.978  -11.062 26.014  1   36.65 ? 48  ASP   B O   1 
ATOM   3287 C  CB  . ASP   B 1 63  ? 50.484  -11.42  22.765  1   42.37 ? 48  ASP   B CB  1 
ATOM   3288 C  CG  . ASP   B 1 63  ? 50.262  -12.398 21.637  1   53.84 ? 48  ASP   B CG  1 
ATOM   3289 O  OD1 . ASP   B 1 63  ? 49.617  -13.452 21.882  1   56.63 ? 48  ASP   B OD1 1 
ATOM   3290 O  OD2 . ASP   B 1 63  ? 50.725  -12.114 20.501  1   58.05 ? 48  ASP   B OD2 1 
ATOM   3291 N  N   . LEU   B 1 64  ? 49.66   -9.202  24.764  1   36.63 ? 49  LEU   B N   1 
ATOM   3292 C  CA  . LEU   B 1 64  ? 50.042  -8.271  25.813  1   36.85 ? 49  LEU   B CA  1 
ATOM   3293 C  C   . LEU   B 1 64  ? 49.141  -8.318  27.018  1   37.85 ? 49  LEU   B C   1 
ATOM   3294 O  O   . LEU   B 1 64  ? 49.62   -8.179  28.142  1   39.06 ? 49  LEU   B O   1 
ATOM   3295 C  CB  . LEU   B 1 64  ? 50.131  -6.841  25.275  1   36.64 ? 49  LEU   B CB  1 
ATOM   3296 C  CG  . LEU   B 1 64  ? 51.263  -6.599  24.273  1   38.1  ? 49  LEU   B CG  1 
ATOM   3297 C  CD1 . LEU   B 1 64  ? 51.163  -5.182  23.664  1   38.1  ? 49  LEU   B CD1 1 
ATOM   3298 C  CD2 . LEU   B 1 64  ? 52.67   -6.801  24.948  1   38.36 ? 49  LEU   B CD2 1 
ATOM   3299 N  N   . ILE   B 1 65  ? 47.831  -8.479  26.808  1   36.73 ? 50  ILE   B N   1 
ATOM   3300 C  CA  . ILE   B 1 65  ? 46.893  -8.539  27.923  1   36.07 ? 50  ILE   B CA  1 
ATOM   3301 C  C   . ILE   B 1 65  ? 47.139  -9.813  28.722  1   36.21 ? 50  ILE   B C   1 
ATOM   3302 O  O   . ILE   B 1 65  ? 47.215  -9.757  29.948  1   36.45 ? 50  ILE   B O   1 
ATOM   3303 C  CB  . ILE   B 1 65  ? 45.425  -8.492  27.403  1   35.47 ? 50  ILE   B CB  1 
ATOM   3304 C  CG1 . ILE   B 1 65  ? 45.065  -7.116  26.812  1   35.57 ? 50  ILE   B CG1 1 
ATOM   3305 C  CG2 . ILE   B 1 65  ? 44.46   -8.887  28.51   1   35.79 ? 50  ILE   B CG2 1 
ATOM   3306 C  CD1 . ILE   B 1 65  ? 43.691  -7.114  26.112  1   36.34 ? 50  ILE   B CD1 1 
ATOM   3307 N  N   . GLU   B 1 66  ? 47.242  -10.954 28.027  1   36.6  ? 51  GLU   B N   1 
ATOM   3308 C  CA  . GLU   B 1 66  ? 47.389  -12.251 28.67   1   38.82 ? 51  GLU   B CA  1 
ATOM   3309 C  C   . GLU   B 1 66  ? 48.668  -12.334 29.504  1   40.65 ? 51  GLU   B C   1 
ATOM   3310 O  O   . GLU   B 1 66  ? 48.659  -12.891 30.602  1   41.32 ? 51  GLU   B O   1 
ATOM   3311 C  CB  . GLU   B 1 66  ? 47.354  -13.37  27.625  1   41.25 ? 51  GLU   B CB  1 
ATOM   3312 C  CG  . GLU   B 1 66  ? 47.112  -14.748 28.215  1   47.51 ? 51  GLU   B CG  1 
ATOM   3313 C  CD  . GLU   B 1 66  ? 48.278  -15.445 28.896  1   58.28 ? 51  GLU   B CD  1 
ATOM   3314 O  OE1 . GLU   B 1 66  ? 49.448  -15.103 28.597  1   57.56 ? 51  GLU   B OE1 1 
ATOM   3315 O  OE2 . GLU   B 1 66  ? 48.011  -16.335 29.738  1   64.02 ? 51  GLU   B OE2 1 
ATOM   3316 N  N   . SER   B 1 67  ? 49.755  -11.79  28.977  1   40.67 ? 52  SER   B N   1 
ATOM   3317 C  CA  . SER   B 1 67  ? 51.04   -11.797 29.66   1   41.43 ? 52  SER   B CA  1 
ATOM   3318 C  C   . SER   B 1 67  ? 51.185  -10.699 30.724  1   42.75 ? 52  SER   B C   1 
ATOM   3319 O  O   . SER   B 1 67  ? 52.228  -10.616 31.346  1   43.35 ? 52  SER   B O   1 
ATOM   3320 C  CB  . SER   B 1 67  ? 52.169  -11.674 28.64   1   41.65 ? 52  SER   B CB  1 
ATOM   3321 O  OG  . SER   B 1 67  ? 52.208  -10.367 28.088  1   43.3  ? 52  SER   B OG  1 
ATOM   3322 N  N   . GLY   B 1 68  ? 50.178  -9.852  30.912  1   42.89 ? 53  GLY   B N   1 
ATOM   3323 C  CA  . GLY   B 1 68  ? 50.241  -8.762  31.878  1   43.26 ? 53  GLY   B CA  1 
ATOM   3324 C  C   . GLY   B 1 68  ? 51.202  -7.651  31.487  1   43.67 ? 53  GLY   B C   1 
ATOM   3325 O  O   . GLY   B 1 68  ? 51.582  -6.833  32.333  1   43.88 ? 53  GLY   B O   1 
ATOM   3326 N  N   . GLN   B 1 69  ? 51.573  -7.577  30.193  1   43.61 ? 54  GLN   B N   1 
ATOM   3327 C  CA  . GLN   B 1 69  ? 52.493  -6.558  29.699  1   44.96 ? 54  GLN   B CA  1 
ATOM   3328 C  C   . GLN   B 1 69  ? 51.802  -5.335  29.108  1   45.19 ? 54  GLN   B C   1 
ATOM   3329 O  O   . GLN   B 1 69  ? 52.484  -4.347  28.843  1   46.06 ? 54  GLN   B O   1 
ATOM   3330 C  CB  . GLN   B 1 69  ? 53.409  -7.151  28.622  1   47.95 ? 54  GLN   B CB  1 
ATOM   3331 C  CG  . GLN   B 1 69  ? 54.363  -8.233  29.113  1   53.53 ? 54  GLN   B CG  1 
ATOM   3332 C  CD  . GLN   B 1 69  ? 55.778  -7.722  29.134  1   61.11 ? 54  GLN   B CD  1 
ATOM   3333 O  OE1 . GLN   B 1 69  ? 56.081  -6.645  29.687  1   63.34 ? 54  GLN   B OE1 1 
ATOM   3334 N  NE2 . GLN   B 1 69  ? 56.682  -8.471  28.51   1   62.69 ? 54  GLN   B NE2 1 
ATOM   3335 N  N   . LEU   B 1 70  ? 50.475  -5.403  28.858  1   43.82 ? 55  LEU   B N   1 
ATOM   3336 C  CA  . LEU   B 1 70  ? 49.735  -4.327  28.219  1   42.92 ? 55  LEU   B CA  1 
ATOM   3337 C  C   . LEU   B 1 70  ? 49.89   -2.982  28.903  1   42.57 ? 55  LEU   B C   1 
ATOM   3338 O  O   . LEU   B 1 70  ? 50.251  -2.024  28.239  1   42.83 ? 55  LEU   B O   1 
ATOM   3339 C  CB  . LEU   B 1 70  ? 48.237  -4.715  28.069  1   42.93 ? 55  LEU   B CB  1 
ATOM   3340 C  CG  . LEU   B 1 70  ? 47.308  -3.759  27.295  1   44.4  ? 55  LEU   B CG  1 
ATOM   3341 C  CD1 . LEU   B 1 70  ? 46.81   -2.632  28.161  1   44.87 ? 55  LEU   B CD1 1 
ATOM   3342 C  CD2 . LEU   B 1 70  ? 47.946  -3.217  26.024  1   45.13 ? 55  LEU   B CD2 1 
ATOM   3343 N  N   . ARG   B 1 71  ? 49.565  -2.895  30.193  1   42.27 ? 56  ARG   B N   1 
ATOM   3344 C  CA  . ARG   B 1 71  ? 49.586  -1.643  30.929  1   43.44 ? 56  ARG   B CA  1 
ATOM   3345 C  C   . ARG   B 1 71  ? 50.98   -1.016  30.994  1   45.31 ? 56  ARG   B C   1 
ATOM   3346 O  O   . ARG   B 1 71  ? 51.096  0.184   30.781  1   45.54 ? 56  ARG   B O   1 
ATOM   3347 C  CB  . ARG   B 1 71  ? 48.954  -1.822  32.315  1   43.47 ? 56  ARG   B CB  1 
ATOM   3348 C  CG  . ARG   B 1 71  ? 47.436  -2.054  32.238  1   43.99 ? 56  ARG   B CG  1 
ATOM   3349 C  CD  . ARG   B 1 71  ? 46.828  -2.525  33.535  1   44.9  ? 56  ARG   B CD  1 
ATOM   3350 N  NE  . ARG   B 1 71  ? 45.363  -2.488  33.528  1   45.35 ? 56  ARG   B NE  1 
ATOM   3351 C  CZ  . ARG   B 1 71  ? 44.588  -3.129  34.404  1   46.82 ? 56  ARG   B CZ  1 
ATOM   3352 N  NH1 . ARG   B 1 71  ? 45.127  -3.89   35.347  1   45.66 ? 56  ARG   B NH1 1 
ATOM   3353 N  NH2 . ARG   B 1 71  ? 43.27   -3.003  34.347  1   46.51 ? 56  ARG   B NH2 1 
ATOM   3354 N  N   . GLU   B 1 72  ? 52.029  -1.832  31.168  1   46.48 ? 57  GLU   B N   1 
ATOM   3355 C  CA  . GLU   B 1 72  ? 53.42   -1.355  31.195  1   48.15 ? 57  GLU   B CA  1 
ATOM   3356 C  C   . GLU   B 1 72  ? 53.779  -0.735  29.834  1   47.75 ? 57  GLU   B C   1 
ATOM   3357 O  O   . GLU   B 1 72  ? 54.211  0.41    29.809  1   47.7  ? 57  GLU   B O   1 
ATOM   3358 C  CB  . GLU   B 1 72  ? 54.379  -2.501  31.565  1   52.72 ? 57  GLU   B CB  1 
ATOM   3359 C  CG  . GLU   B 1 72  ? 55.807  -2.064  31.846  1   62.48 ? 57  GLU   B CG  1 
ATOM   3360 C  CD  . GLU   B 1 72  ? 56.816  -3.203  31.886  1   72.5  ? 57  GLU   B CD  1 
ATOM   3361 O  OE1 . GLU   B 1 72  ? 56.983  -3.899  30.853  1   74.47 ? 57  GLU   B OE1 1 
ATOM   3362 O  OE2 . GLU   B 1 72  ? 57.451  -3.391  32.95   1   74.51 ? 57  GLU   B OE2 1 
ATOM   3363 N  N   . ARG   B 1 73  ? 53.514  -1.442  28.709  1   47.44 ? 58  ARG   B N   1 
ATOM   3364 C  CA  . ARG   B 1 73  ? 53.768  -0.932  27.356  1   48.09 ? 58  ARG   B CA  1 
ATOM   3365 C  C   . ARG   B 1 73  ? 53.046  0.394   27.126  1   49.03 ? 58  ARG   B C   1 
ATOM   3366 O  O   . ARG   B 1 73  ? 53.591  1.281   26.476  1   49.91 ? 58  ARG   B O   1 
ATOM   3367 C  CB  . ARG   B 1 73  ? 53.295  -1.917  26.275  1   49.73 ? 58  ARG   B CB  1 
ATOM   3368 C  CG  . ARG   B 1 73  ? 53.926  -3.279  26.309  1   53.3  ? 58  ARG   B CG  1 
ATOM   3369 C  CD  . ARG   B 1 73  ? 55.391  -3.304  25.925  1   57.87 ? 58  ARG   B CD  1 
ATOM   3370 N  NE  . ARG   B 1 73  ? 55.917  -4.657  26.144  1   60.41 ? 58  ARG   B NE  1 
ATOM   3371 C  CZ  . ARG   B 1 73  ? 56.039  -5.581  25.195  1   62.77 ? 58  ARG   B CZ  1 
ATOM   3372 N  NH1 . ARG   B 1 73  ? 55.73   -5.294  23.935  1   62.38 ? 58  ARG   B NH1 1 
ATOM   3373 N  NH2 . ARG   B 1 73  ? 56.483  -6.796  25.497  1   62.74 ? 58  ARG   B NH2 1 
ATOM   3374 N  N   . VAL   B 1 74  ? 51.816  0.533   27.643  1   48.75 ? 59  VAL   B N   1 
ATOM   3375 C  CA  . VAL   B 1 74  ? 51.056  1.773   27.49   1   49.19 ? 59  VAL   B CA  1 
ATOM   3376 C  C   . VAL   B 1 74  ? 51.725  2.883   28.281  1   50.19 ? 59  VAL   B C   1 
ATOM   3377 O  O   . VAL   B 1 74  ? 51.985  3.944   27.732  1   50.19 ? 59  VAL   B O   1 
ATOM   3378 C  CB  . VAL   B 1 74  ? 49.554  1.593   27.857  1   48.86 ? 59  VAL   B CB  1 
ATOM   3379 C  CG1 . VAL   B 1 74  ? 48.844  2.932   28.003  1   48.59 ? 59  VAL   B CG1 1 
ATOM   3380 C  CG2 . VAL   B 1 74  ? 48.861  0.732   26.815  1   49.12 ? 59  VAL   B CG2 1 
ATOM   3381 N  N   . GLU   B 1 75  ? 52.045  2.621   29.554  1   51.06 ? 60  GLU   B N   1 
ATOM   3382 C  CA  . GLU   B 1 75  ? 52.719  3.579   30.435  1   52.18 ? 60  GLU   B CA  1 
ATOM   3383 C  C   . GLU   B 1 75  ? 54.115  3.998   29.92   1   53.1  ? 60  GLU   B C   1 
ATOM   3384 O  O   . GLU   B 1 75  ? 54.57   5.104   30.204  1   53.28 ? 60  GLU   B O   1 
ATOM   3385 C  CB  . GLU   B 1 75  ? 52.784  3.024   31.867  1   53.69 ? 60  GLU   B CB  1 
ATOM   3386 C  CG  . GLU   B 1 75  ? 51.412  2.911   32.505  1   57.23 ? 60  GLU   B CG  1 
ATOM   3387 C  CD  . GLU   B 1 75  ? 51.259  1.861   33.588  1   61.45 ? 60  GLU   B CD  1 
ATOM   3388 O  OE1 . GLU   B 1 75  ? 52.274  1.222   33.945  1   62.48 ? 60  GLU   B OE1 1 
ATOM   3389 O  OE2 . GLU   B 1 75  ? 50.121  1.671   34.077  1   61.77 ? 60  GLU   B OE2 1 
ATOM   3390 N  N   . LYS   B 1 76  ? 54.746  3.153   29.104  1   53.62 ? 61  LYS   B N   1 
ATOM   3391 C  CA  . LYS   B 1 76  ? 56.065  3.442   28.532  1   54.63 ? 61  LYS   B CA  1 
ATOM   3392 C  C   . LYS   B 1 76  ? 56.007  4.339   27.283  1   55.52 ? 61  LYS   B C   1 
ATOM   3393 O  O   . LYS   B 1 76  ? 57.051  4.788   26.815  1   55.5  ? 61  LYS   B O   1 
ATOM   3394 C  CB  . LYS   B 1 76  ? 56.798  2.129   28.197  1   55.76 ? 61  LYS   B CB  1 
ATOM   3395 N  N   . LEU   B 1 77  ? 54.809  4.572   26.718  1   55.57 ? 62  LEU   B N   1 
ATOM   3396 C  CA  . LEU   B 1 77  ? 54.681  5.371   25.497  1   55.44 ? 62  LEU   B CA  1 
ATOM   3397 C  C   . LEU   B 1 77  ? 55.082  6.804   25.702  1   55.64 ? 62  LEU   B C   1 
ATOM   3398 O  O   . LEU   B 1 77  ? 54.889  7.351   26.782  1   55.61 ? 62  LEU   B O   1 
ATOM   3399 C  CB  . LEU   B 1 77  ? 53.224  5.37    24.996  1   55.13 ? 62  LEU   B CB  1 
ATOM   3400 C  CG  . LEU   B 1 77  ? 52.67   4.083   24.437  1   55.91 ? 62  LEU   B CG  1 
ATOM   3401 C  CD1 . LEU   B 1 77  ? 51.168  4.168   24.307  1   56.27 ? 62  LEU   B CD1 1 
ATOM   3402 C  CD2 . LEU   B 1 77  ? 53.269  3.775   23.097  1   56.38 ? 62  LEU   B CD2 1 
ATOM   3403 N  N   . ASN   B 1 78  ? 55.593  7.434   24.646  1   55.89 ? 63  ASN   B N   1 
ATOM   3404 C  CA  . ASN   B 1 78  ? 55.875  8.868   24.644  1   56.52 ? 63  ASN   B CA  1 
ATOM   3405 C  C   . ASN   B 1 78  ? 54.652  9.537   24.018  1   56.5  ? 63  ASN   B C   1 
ATOM   3406 O  O   . ASN   B 1 78  ? 54.033  8.955   23.124  1   56.76 ? 63  ASN   B O   1 
ATOM   3407 C  CB  . ASN   B 1 78  ? 57.115  9.178   23.797  1   58.13 ? 63  ASN   B CB  1 
ATOM   3408 C  CG  . ASN   B 1 78  ? 58.372  8.542   24.352  1   60.84 ? 63  ASN   B CG  1 
ATOM   3409 O  OD1 . ASN   B 1 78  ? 58.645  8.643   25.559  1   61.89 ? 63  ASN   B OD1 1 
ATOM   3410 N  ND2 . ASN   B 1 78  ? 59.132  7.846   23.496  1   60.65 ? 63  ASN   B ND2 1 
ATOM   3411 N  N   . MET   B 1 79  ? 54.305  10.744  24.464  1   56.35 ? 64  MET   B N   1 
ATOM   3412 C  CA  . MET   B 1 79  ? 53.153  11.442  23.911  1   56.72 ? 64  MET   B CA  1 
ATOM   3413 C  C   . MET   B 1 79  ? 53.353  11.782  22.449  1   57.04 ? 64  MET   B C   1 
ATOM   3414 O  O   . MET   B 1 79  ? 54.148  12.658  22.145  1   57.33 ? 64  MET   B O   1 
ATOM   3415 C  CB  . MET   B 1 79  ? 52.845  12.709  24.689  1   57.35 ? 64  MET   B CB  1 
ATOM   3416 C  CG  . MET   B 1 79  ? 51.451  13.2    24.436  1   58.85 ? 64  MET   B CG  1 
ATOM   3417 S  SD  . MET   B 1 79  ? 51.114  14.7    25.368  1   61.33 ? 64  MET   B SD  1 
ATOM   3418 C  CE  . MET   B 1 79  ? 51.925  15.902  24.307  1   62.87 ? 64  MET   B CE  1 
ATOM   3419 N  N   . LEU   B 1 80  ? 52.643  11.097  21.54   1   56.76 ? 65  LEU   B N   1 
ATOM   3420 C  CA  . LEU   B 1 80  ? 52.76   11.377  20.114  1   56.98 ? 65  LEU   B CA  1 
ATOM   3421 C  C   . LEU   B 1 80  ? 51.751  12.419  19.666  1   58.07 ? 65  LEU   B C   1 
ATOM   3422 O  O   . LEU   B 1 80  ? 50.599  12.393  20.097  1   58.71 ? 65  LEU   B O   1 
ATOM   3423 C  CB  . LEU   B 1 80  ? 52.584  10.113  19.268  1   56.79 ? 65  LEU   B CB  1 
ATOM   3424 C  CG  . LEU   B 1 80  ? 53.535  8.96    19.533  1   57.89 ? 65  LEU   B CG  1 
ATOM   3425 C  CD1 . LEU   B 1 80  ? 53.299  7.835   18.534  1   57.88 ? 65  LEU   B CD1 1 
ATOM   3426 C  CD2 . LEU   B 1 80  ? 55.012  9.416   19.492  1   58.59 ? 65  LEU   B CD2 1 
ATOM   3427 N  N   . SER   B 1 81  ? 52.177  13.322  18.778  1   57.88 ? 66  SER   B N   1 
ATOM   3428 C  CA  . SER   B 1 81  ? 51.315  14.354  18.221  1   57.92 ? 66  SER   B CA  1 
ATOM   3429 C  C   . SER   B 1 81  ? 50.353  13.723  17.222  1   57.38 ? 66  SER   B C   1 
ATOM   3430 O  O   . SER   B 1 81  ? 50.733  12.801  16.508  1   56.91 ? 66  SER   B O   1 
ATOM   3431 C  CB  . SER   B 1 81  ? 52.154  15.405  17.498  1   59.35 ? 66  SER   B CB  1 
ATOM   3432 O  OG  . SER   B 1 81  ? 51.351  16.432  16.937  1   62.18 ? 66  SER   B OG  1 
ATOM   3433 N  N   . ILE   B 1 82  ? 49.127  14.239  17.137  1   57.18 ? 67  ILE   B N   1 
ATOM   3434 C  CA  . ILE   B 1 82  ? 48.148  13.736  16.164  1   57.73 ? 67  ILE   B CA  1 
ATOM   3435 C  C   . ILE   B 1 82  ? 48.203  14.458  14.8    1   58.58 ? 67  ILE   B C   1 
ATOM   3436 O  O   . ILE   B 1 82  ? 47.449  14.092  13.885  1   59.01 ? 67  ILE   B O   1 
ATOM   3437 C  CB  . ILE   B 1 82  ? 46.72   13.807  16.741  1   57.72 ? 67  ILE   B CB  1 
ATOM   3438 C  CG1 . ILE   B 1 82  ? 46.33   15.255  17.05   1   57.99 ? 67  ILE   B CG1 1 
ATOM   3439 C  CG2 . ILE   B 1 82  ? 46.585  12.931  17.965  1   58.16 ? 67  ILE   B CG2 1 
ATOM   3440 C  CD1 . ILE   B 1 82  ? 44.872  15.48   17.064  1   58.97 ? 67  ILE   B CD1 1 
ATOM   3441 N  N   . ASP   B 1 83  ? 49.094  15.458  14.649  1   58.36 ? 68  ASP   B N   1 
ATOM   3442 C  CA  . ASP   B 1 83  ? 49.188  16.248  13.419  1   58.67 ? 68  ASP   B CA  1 
ATOM   3443 C  C   . ASP   B 1 83  ? 49.638  15.479  12.185  1   58.3  ? 68  ASP   B C   1 
ATOM   3444 O  O   . ASP   B 1 83  ? 49.486  15.988  11.072  1   59.05 ? 68  ASP   B O   1 
ATOM   3445 C  CB  . ASP   B 1 83  ? 50.067  17.472  13.641  1   60.79 ? 68  ASP   B CB  1 
ATOM   3446 C  CG  . ASP   B 1 83  ? 49.495  18.355  14.725  1   66.67 ? 68  ASP   B CG  1 
ATOM   3447 O  OD1 . ASP   B 1 83  ? 48.249  18.479  14.796  1   67.09 ? 68  ASP   B OD1 1 
ATOM   3448 O  OD2 . ASP   B 1 83  ? 50.286  18.907  15.519  1   70.17 ? 68  ASP   B OD2 1 
ATOM   3449 N  N   . HIS   B 1 84  ? 50.141  14.26   12.354  1   57.21 ? 69  HIS   B N   1 
ATOM   3450 C  CA  . HIS   B 1 84  ? 50.568  13.457  11.208  1   57.31 ? 69  HIS   B CA  1 
ATOM   3451 C  C   . HIS   B 1 84  ? 49.468  12.504  10.691  1   56.12 ? 69  HIS   B C   1 
ATOM   3452 O  O   . HIS   B 1 84  ? 49.734  11.671  9.828   1   55.75 ? 69  HIS   B O   1 
ATOM   3453 C  CB  . HIS   B 1 84  ? 51.882  12.721  11.513  1   59.84 ? 69  HIS   B CB  1 
ATOM   3454 C  CG  . HIS   B 1 84  ? 52.896  13.606  12.179  1   64.36 ? 69  HIS   B CG  1 
ATOM   3455 N  ND1 . HIS   B 1 84  ? 53.661  14.502  11.45   1   67.13 ? 69  HIS   B ND1 1 
ATOM   3456 C  CD2 . HIS   B 1 84  ? 53.168  13.768  13.497  1   65.82 ? 69  HIS   B CD2 1 
ATOM   3457 C  CE1 . HIS   B 1 84  ? 54.399  15.148  12.342  1   67.93 ? 69  HIS   B CE1 1 
ATOM   3458 N  NE2 . HIS   B 1 84  ? 54.13   14.745  13.588  1   67.45 ? 69  HIS   B NE2 1 
ATOM   3459 N  N   . LEU   B 1 85  ? 48.23   12.638  11.213  1   55.36 ? 70  LEU   B N   1 
ATOM   3460 C  CA  . LEU   B 1 85  ? 47.044  11.893  10.784  1   54.96 ? 70  LEU   B CA  1 
ATOM   3461 C  C   . LEU   B 1 85  ? 46.302  12.954  9.988   1   54.78 ? 70  LEU   B C   1 
ATOM   3462 O  O   . LEU   B 1 85  ? 45.574  13.769  10.566  1   54.67 ? 70  LEU   B O   1 
ATOM   3463 C  CB  . LEU   B 1 85  ? 46.225  11.484  12.018  1   54.55 ? 70  LEU   B CB  1 
ATOM   3464 C  CG  . LEU   B 1 85  ? 46.97   10.627  13.015  1   54.44 ? 70  LEU   B CG  1 
ATOM   3465 C  CD1 . LEU   B 1 85  ? 46.324  10.671  14.373  1   54.83 ? 70  LEU   B CD1 1 
ATOM   3466 C  CD2 . LEU   B 1 85  ? 47.13   9.231   12.503  1   53.91 ? 70  LEU   B CD2 1 
ATOM   3467 N  N   . THR   B 1 86  ? 46.58   13.011  8.679   1   54.62 ? 71  THR   B N   1 
ATOM   3468 C  CA  . THR   B 1 86  ? 46.141  14.092  7.795   1   55.05 ? 71  THR   B CA  1 
ATOM   3469 C  C   . THR   B 1 86  ? 44.859  13.896  6.982   1   54.83 ? 71  THR   B C   1 
ATOM   3470 O  O   . THR   B 1 86  ? 44.502  14.784  6.198   1   55.07 ? 71  THR   B O   1 
ATOM   3471 C  CB  . THR   B 1 86  ? 47.274  14.396  6.835   1   56.32 ? 71  THR   B CB  1 
ATOM   3472 O  OG1 . THR   B 1 86  ? 47.521  13.21   6.069   1   56.97 ? 71  THR   B OG1 1 
ATOM   3473 C  CG2 . THR   B 1 86  ? 48.535  14.834  7.57    1   56.96 ? 71  THR   B CG2 1 
ATOM   3474 N  N   . ASP   B 1 87  ? 44.184  12.762  7.139   1   53.96 ? 72  ASP   B N   1 
ATOM   3475 C  CA  . ASP   B 1 87  ? 42.939  12.523  6.421   1   53.39 ? 72  ASP   B CA  1 
ATOM   3476 C  C   . ASP   B 1 87  ? 41.966  11.729  7.29    1   52.15 ? 72  ASP   B C   1 
ATOM   3477 O  O   . ASP   B 1 87  ? 42.374  11.16   8.309   1   52.83 ? 72  ASP   B O   1 
ATOM   3478 C  CB  . ASP   B 1 87  ? 43.207  11.846  5.067   1   55.48 ? 72  ASP   B CB  1 
ATOM   3479 C  CG  . ASP   B 1 87  ? 43.865  10.487  5.149   1   61.52 ? 72  ASP   B CG  1 
ATOM   3480 O  OD1 . ASP   B 1 87  ? 44.027  9.978   6.27    1   62.69 ? 72  ASP   B OD1 1 
ATOM   3481 O  OD2 . ASP   B 1 87  ? 44.211  9.925   4.079   1   63.9  ? 72  ASP   B OD2 1 
ATOM   3482 N  N   . HIS   B 1 88  ? 40.683  11.671  6.885   1   49.73 ? 73  HIS   B N   1 
ATOM   3483 C  CA  . HIS   B 1 88  ? 39.658  10.968  7.646   1   47.35 ? 73  HIS   B CA  1 
ATOM   3484 C  C   . HIS   B 1 88  ? 40.011  9.524   7.954   1   45.3  ? 73  HIS   B C   1 
ATOM   3485 O  O   . HIS   B 1 88  ? 39.948  9.14    9.115   1   45.31 ? 73  HIS   B O   1 
ATOM   3486 C  CB  . HIS   B 1 88  ? 38.28   11.066  6.966   1   47.12 ? 73  HIS   B CB  1 
ATOM   3487 C  CG  . HIS   B 1 88  ? 37.147  10.683  7.868   1   48.07 ? 73  HIS   B CG  1 
ATOM   3488 N  ND1 . HIS   B 1 88  ? 36.784  11.477  8.956   1   49.61 ? 73  HIS   B ND1 1 
ATOM   3489 C  CD2 . HIS   B 1 88  ? 36.335  9.602   7.826   1   48.83 ? 73  HIS   B CD2 1 
ATOM   3490 C  CE1 . HIS   B 1 88  ? 35.77   10.852  9.534   1   50.07 ? 73  HIS   B CE1 1 
ATOM   3491 N  NE2 . HIS   B 1 88  ? 35.454  9.725   8.883   1   50.03 ? 73  HIS   B NE2 1 
ATOM   3492 N  N   . LYS   B 1 89  ? 40.414  8.741   6.948   1   43.79 ? 74  LYS   B N   1 
ATOM   3493 C  CA  . LYS   B 1 89  ? 40.733  7.34    7.148   1   43.34 ? 74  LYS   B CA  1 
ATOM   3494 C  C   . LYS   B 1 89  ? 41.838  7.077   8.169   1   44.32 ? 74  LYS   B C   1 
ATOM   3495 O  O   . LYS   B 1 89  ? 41.676  6.185   9.013   1   45.02 ? 74  LYS   B O   1 
ATOM   3496 C  CB  . LYS   B 1 89  ? 41.048  6.646   5.821   1   43.57 ? 74  LYS   B CB  1 
ATOM   3497 C  CG  . LYS   B 1 89  ? 39.829  6.55    4.923   1   45.98 ? 74  LYS   B CG  1 
ATOM   3498 C  CD  . LYS   B 1 89  ? 39.943  5.423   3.934   1   49.45 ? 74  LYS   B CD  1 
ATOM   3499 C  CE  . LYS   B 1 89  ? 38.825  5.486   2.926   1   53.74 ? 74  LYS   B CE  1 
ATOM   3500 N  NZ  . LYS   B 1 89  ? 38.96   4.446   1.882   1   56.18 ? 74  LYS   B NZ  1 
ATOM   3501 N  N   . SER   B 1 90  ? 42.948  7.833   8.109   1   43.89 ? 75  SER   B N   1 
ATOM   3502 C  CA  . SER   B 1 90  ? 44.031  7.632   9.071   1   43.58 ? 75  SER   B CA  1 
ATOM   3503 C  C   . SER   B 1 90  ? 43.554  8.058   10.47   1   42.68 ? 75  SER   B C   1 
ATOM   3504 O  O   . SER   B 1 90  ? 43.898  7.403   11.449  1   42.45 ? 75  SER   B O   1 
ATOM   3505 C  CB  . SER   B 1 90  ? 45.296  8.387   8.66    1   45.17 ? 75  SER   B CB  1 
ATOM   3506 O  OG  . SER   B 1 90  ? 45.116  9.792   8.734   1   47.33 ? 75  SER   B OG  1 
ATOM   3507 N  N   . GLN   B 1 91  ? 42.737  9.125   10.565  1   42.37 ? 76  GLN   B N   1 
ATOM   3508 C  CA  . GLN   B 1 91  ? 42.19   9.573   11.848  1   42.41 ? 76  GLN   B CA  1 
ATOM   3509 C  C   . GLN   B 1 91  ? 41.226  8.526   12.455  1   41.38 ? 76  GLN   B C   1 
ATOM   3510 O  O   . GLN   B 1 91  ? 41.254  8.283   13.658  1   42.01 ? 76  GLN   B O   1 
ATOM   3511 C  CB  . GLN   B 1 91  ? 41.507  10.927  11.684  1   45.49 ? 76  GLN   B CB  1 
ATOM   3512 C  CG  . GLN   B 1 91  ? 42.5    12.062  11.482  1   51.46 ? 76  GLN   B CG  1 
ATOM   3513 C  CD  . GLN   B 1 91  ? 41.852  13.28   10.881  1   58.44 ? 76  GLN   B CD  1 
ATOM   3514 O  OE1 . GLN   B 1 91  ? 40.669  13.554  11.097  1   60.68 ? 76  GLN   B OE1 1 
ATOM   3515 N  NE2 . GLN   B 1 91  ? 42.614  14.041  10.108  1   59.48 ? 76  GLN   B NE2 1 
ATOM   3516 N  N   . ARG   B 1 92  ? 40.423  7.88    11.606  1   39.88 ? 77  ARG   B N   1 
ATOM   3517 C  CA  . ARG   B 1 92  ? 39.473  6.851   12.009  1   39    ? 77  ARG   B CA  1 
ATOM   3518 C  C   . ARG   B 1 92  ? 40.245  5.617   12.475  1   38.91 ? 77  ARG   B C   1 
ATOM   3519 O  O   . ARG   B 1 92  ? 39.939  5.068   13.54   1   38.04 ? 77  ARG   B O   1 
ATOM   3520 C  CB  . ARG   B 1 92  ? 38.516  6.493   10.849  1   38.13 ? 77  ARG   B CB  1 
ATOM   3521 C  CG  . ARG   B 1 92  ? 37.418  7.545   10.615  1   37.24 ? 77  ARG   B CG  1 
ATOM   3522 C  CD  . ARG   B 1 92  ? 36.36   7.608   11.719  1   37.66 ? 77  ARG   B CD  1 
ATOM   3523 N  NE  . ARG   B 1 92  ? 35.549  6.388   11.787  1   36.74 ? 77  ARG   B NE  1 
ATOM   3524 C  CZ  . ARG   B 1 92  ? 34.542  6.103   10.961  1   37.41 ? 77  ARG   B CZ  1 
ATOM   3525 N  NH1 . ARG   B 1 92  ? 34.237  6.926   9.963   1   36.44 ? 77  ARG   B NH1 1 
ATOM   3526 N  NH2 . ARG   B 1 92  ? 33.863  4.975   11.098  1   34.89 ? 77  ARG   B NH2 1 
ATOM   3527 N  N   . LEU   B 1 93  ? 41.296  5.225   11.732  1   39.3  ? 78  LEU   B N   1 
ATOM   3528 C  CA  . LEU   B 1 93  ? 42.136  4.088   12.131  1   40.21 ? 78  LEU   B CA  1 
ATOM   3529 C  C   . LEU   B 1 93  ? 42.792  4.359   13.477  1   40.03 ? 78  LEU   B C   1 
ATOM   3530 O  O   . LEU   B 1 93  ? 42.761  3.494   14.354  1   40.69 ? 78  LEU   B O   1 
ATOM   3531 C  CB  . LEU   B 1 93  ? 43.216  3.782   11.08   1   42.1  ? 78  LEU   B CB  1 
ATOM   3532 C  CG  . LEU   B 1 93  ? 44.224  2.686   11.464  1   44.6  ? 78  LEU   B CG  1 
ATOM   3533 C  CD1 . LEU   B 1 93  ? 43.533  1.357   11.723  1   45.04 ? 78  LEU   B CD1 1 
ATOM   3534 C  CD2 . LEU   B 1 93  ? 45.264  2.53    10.394  1   45.76 ? 78  LEU   B CD2 1 
ATOM   3535 N  N   . ALA   B 1 94  ? 43.307  5.584   13.671  1   38.85 ? 79  ALA   B N   1 
ATOM   3536 C  CA  . ALA   B 1 94  ? 43.935  5.976   14.925  1   38.39 ? 79  ALA   B CA  1 
ATOM   3537 C  C   . ALA   B 1 94  ? 42.933  5.903   16.069  1   36.87 ? 79  ALA   B C   1 
ATOM   3538 O  O   . ALA   B 1 94  ? 43.259  5.354   17.119  1   36.9  ? 79  ALA   B O   1 
ATOM   3539 C  CB  . ALA   B 1 94  ? 44.524  7.375   14.811  1   38.34 ? 79  ALA   B CB  1 
ATOM   3540 N  N   . ARG   B 1 95  ? 41.686  6.381   15.845  1   35.62 ? 80  ARG   B N   1 
ATOM   3541 C  CA  . ARG   B 1 95  ? 40.613  6.323   16.844  1   34.4  ? 80  ARG   B CA  1 
ATOM   3542 C  C   . ARG   B 1 95  ? 40.375  4.867   17.258  1   33.47 ? 80  ARG   B C   1 
ATOM   3543 O  O   . ARG   B 1 95  ? 40.331  4.567   18.447  1   34.08 ? 80  ARG   B O   1 
ATOM   3544 C  CB  . ARG   B 1 95  ? 39.322  6.924   16.275  1   35.16 ? 80  ARG   B CB  1 
ATOM   3545 C  CG  . ARG   B 1 95  ? 38.954  8.265   16.882  1   34.91 ? 80  ARG   B CG  1 
ATOM   3546 C  CD  . ARG   B 1 95  ? 37.464  8.542   16.663  1   35.1  ? 80  ARG   B CD  1 
ATOM   3547 N  NE  . ARG   B 1 95  ? 36.601  7.715   17.507  1   36.71 ? 80  ARG   B NE  1 
ATOM   3548 C  CZ  . ARG   B 1 95  ? 36.272  8.022   18.761  1   35.7  ? 80  ARG   B CZ  1 
ATOM   3549 N  NH1 . ARG   B 1 95  ? 36.735  9.13    19.325  1   31.46 ? 80  ARG   B NH1 1 
ATOM   3550 N  NH2 . ARG   B 1 95  ? 35.488  7.216   19.465  1   35.04 ? 80  ARG   B NH2 1 
ATOM   3551 N  N   . LEU   B 1 96  ? 40.365  3.955   16.288  1   31.49 ? 81  LEU   B N   1 
ATOM   3552 C  CA  . LEU   B 1 96  ? 40.184  2.523   16.526  1   31.46 ? 81  LEU   B CA  1 
ATOM   3553 C  C   . LEU   B 1 96  ? 41.361  1.901   17.345  1   33.93 ? 81  LEU   B C   1 
ATOM   3554 O  O   . LEU   B 1 96  ? 41.142  1.118   18.29   1   34.35 ? 81  LEU   B O   1 
ATOM   3555 C  CB  . LEU   B 1 96  ? 40.038  1.823   15.157  1   29.8  ? 81  LEU   B CB  1 
ATOM   3556 C  CG  . LEU   B 1 96  ? 39.918  0.303   15.176  1   31.43 ? 81  LEU   B CG  1 
ATOM   3557 C  CD1 . LEU   B 1 96  ? 38.753  -0.175  16.077  1   32.81 ? 81  LEU   B CD1 1 
ATOM   3558 C  CD2 . LEU   B 1 96  ? 39.728  -0.224  13.783  1   31.38 ? 81  LEU   B CD2 1 
ATOM   3559 N  N   . VAL   B 1 97  ? 42.606  2.247   16.968  1   34.02 ? 82  VAL   B N   1 
ATOM   3560 C  CA  . VAL   B 1 97  ? 43.802  1.785   17.649  1   34.38 ? 82  VAL   B CA  1 
ATOM   3561 C  C   . VAL   B 1 97  ? 43.778  2.263   19.114  1   35.32 ? 82  VAL   B C   1 
ATOM   3562 O  O   . VAL   B 1 97  ? 43.836  1.436   20.033  1   35.84 ? 82  VAL   B O   1 
ATOM   3563 C  CB  . VAL   B 1 97  ? 45.059  2.288   16.876  1   35.32 ? 82  VAL   B CB  1 
ATOM   3564 C  CG1 . VAL   B 1 97  ? 46.32   2.175   17.723  1   35.61 ? 82  VAL   B CG1 1 
ATOM   3565 C  CG2 . VAL   B 1 97  ? 45.218  1.528   15.563  1   35.64 ? 82  VAL   B CG2 1 
ATOM   3566 N  N   . LEU   B 1 98  ? 43.596  3.572   19.337  1   35.06 ? 83  LEU   B N   1 
ATOM   3567 C  CA  . LEU   B 1 98  ? 43.599  4.131   20.69   1   35.83 ? 83  LEU   B CA  1 
ATOM   3568 C  C   . LEU   B 1 98  ? 42.413  3.693   21.561  1   36.13 ? 83  LEU   B C   1 
ATOM   3569 O  O   . LEU   B 1 98  ? 42.528  3.564   22.801  1   36.54 ? 83  LEU   B O   1 
ATOM   3570 C  CB  . LEU   B 1 98  ? 43.69   5.663   20.623  1   36.42 ? 83  LEU   B CB  1 
ATOM   3571 C  CG  . LEU   B 1 98  ? 44.974  6.227   20.011  1   38.57 ? 83  LEU   B CG  1 
ATOM   3572 C  CD1 . LEU   B 1 98  ? 44.921  7.737   19.941  1   38.57 ? 83  LEU   B CD1 1 
ATOM   3573 C  CD2 . LEU   B 1 98  ? 46.179  5.839   20.841  1   39.64 ? 83  LEU   B CD2 1 
ATOM   3574 N  N   . GLY   B 1 99  ? 41.272  3.488   20.916  1   35.1  ? 84  GLY   B N   1 
ATOM   3575 C  CA  . GLY   B 1 99  ? 40.082  3.04    21.603  1   34.18 ? 84  GLY   B CA  1 
ATOM   3576 C  C   . GLY   B 1 99  ? 40.259  1.615   22.062  1   32.63 ? 84  GLY   B C   1 
ATOM   3577 O  O   . GLY   B 1 99  ? 39.969  1.316   23.221  1   32.17 ? 84  GLY   B O   1 
ATOM   3578 N  N   . CYS   B 1 100 ? 40.808  0.73    21.189  1   31.69 ? 85  CYS   B N   1 
ATOM   3579 C  CA  . CYS   B 1 100 ? 41.041  -0.661  21.616  1   32.43 ? 85  CYS   B CA  1 
ATOM   3580 C  C   . CYS   B 1 100 ? 42.081  -0.707  22.731  1   32.77 ? 85  CYS   B C   1 
ATOM   3581 O  O   . CYS   B 1 100 ? 41.915  -1.466  23.688  1   33.46 ? 85  CYS   B O   1 
ATOM   3582 C  CB  . CYS   B 1 100 ? 41.454  -1.544  20.447  1   34.2  ? 85  CYS   B CB  1 
ATOM   3583 S  SG  . CYS   B 1 100 ? 40.163  -1.773  19.207  1   39.89 ? 85  CYS   B SG  1 
ATOM   3584 N  N   . ILE   B 1 101 ? 43.131  0.137   22.638  1   31.71 ? 86  ILE   B N   1 
ATOM   3585 C  CA  . ILE   B 1 101 ? 44.154  0.174   23.674  1   32.37 ? 86  ILE   B CA  1 
ATOM   3586 C  C   . ILE   B 1 101 ? 43.537  0.678   24.989  1   31.75 ? 86  ILE   B C   1 
ATOM   3587 O  O   . ILE   B 1 101 ? 43.821  0.112   26.035  1   31.53 ? 86  ILE   B O   1 
ATOM   3588 C  CB  . ILE   B 1 101 ? 45.38   1.034   23.251  1   33.87 ? 86  ILE   B CB  1 
ATOM   3589 C  CG1 . ILE   B 1 101 ? 46.162  0.411   22.071  1   34.88 ? 86  ILE   B CG1 1 
ATOM   3590 C  CG2 . ILE   B 1 101 ? 46.302  1.285   24.434  1   34.61 ? 86  ILE   B CG2 1 
ATOM   3591 C  CD1 . ILE   B 1 101 ? 47.214  1.38    21.481  1   36.36 ? 86  ILE   B CD1 1 
ATOM   3592 N  N   . THR   B 1 102 ? 42.678  1.704   24.94   1   31.86 ? 87  THR   B N   1 
ATOM   3593 C  CA  . THR   B 1 102 ? 42.014  2.22    26.153  1   32.13 ? 87  THR   B CA  1 
ATOM   3594 C  C   . THR   B 1 102 ? 41.142  1.172   26.835  1   32.14 ? 87  THR   B C   1 
ATOM   3595 O  O   . THR   B 1 102 ? 41.21   1.023   28.058  1   32.5  ? 87  THR   B O   1 
ATOM   3596 C  CB  . THR   B 1 102 ? 41.275  3.5     25.862  1   33.06 ? 87  THR   B CB  1 
ATOM   3597 O  OG1 . THR   B 1 102 ? 42.212  4.411   25.311  1   33.84 ? 87  THR   B OG1 1 
ATOM   3598 C  CG2 . THR   B 1 102 ? 40.649  4.103   27.099  1   32.84 ? 87  THR   B CG2 1 
ATOM   3599 N  N   . MET   B 1 103 ? 40.375  0.391   26.061  1   31.55 ? 88  MET   B N   1 
ATOM   3600 C  CA  . MET   B 1 103 ? 39.555  -0.691  26.636  1   31.4  ? 88  MET   B CA  1 
ATOM   3601 C  C   . MET   B 1 103 ? 40.448  -1.731  27.312  1   31.06 ? 88  MET   B C   1 
ATOM   3602 O  O   . MET   B 1 103 ? 40.155  -2.177  28.42   1   30.06 ? 88  MET   B O   1 
ATOM   3603 C  CB  . MET   B 1 103 ? 38.697  -1.401  25.565  1   31.21 ? 88  MET   B CB  1 
ATOM   3604 C  CG  . MET   B 1 103 ? 37.612  -0.521  24.906  1   34.4  ? 88  MET   B CG  1 
ATOM   3605 S  SD  . MET   B 1 103 ? 36.74   0.633   26.006  1   40.98 ? 88  MET   B SD  1 
ATOM   3606 C  CE  . MET   B 1 103 ? 37.429  2.245   25.263  1   33.55 ? 88  MET   B CE  1 
ATOM   3607 N  N   . ALA   B 1 104 ? 41.513  -2.132  26.637  1   31.71 ? 89  ALA   B N   1 
ATOM   3608 C  CA  . ALA   B 1 104 ? 42.465  -3.108  27.161  1   32.38 ? 89  ALA   B CA  1 
ATOM   3609 C  C   . ALA   B 1 104 ? 43.113  -2.582  28.433  1   33.61 ? 89  ALA   B C   1 
ATOM   3610 O  O   . ALA   B 1 104 ? 43.189  -3.305  29.425  1   33.24 ? 89  ALA   B O   1 
ATOM   3611 C  CB  . ALA   B 1 104 ? 43.524  -3.428  26.115  1   32.57 ? 89  ALA   B CB  1 
ATOM   3612 N  N   . TYR   B 1 105 ? 43.477  -1.303  28.449  1   34.56 ? 90  TYR   B N   1 
ATOM   3613 C  CA  . TYR   B 1 105 ? 44.119  -0.707  29.61   1   35.93 ? 90  TYR   B CA  1 
ATOM   3614 C  C   . TYR   B 1 105 ? 43.177  -0.659  30.797  1   36.38 ? 90  TYR   B C   1 
ATOM   3615 O  O   . TYR   B 1 105 ? 43.559  -1.027  31.911  1   36.43 ? 90  TYR   B O   1 
ATOM   3616 C  CB  . TYR   B 1 105 ? 44.664  0.695   29.264  1   36.69 ? 90  TYR   B CB  1 
ATOM   3617 C  CG  . TYR   B 1 105 ? 45.516  1.285   30.37   1   38.39 ? 90  TYR   B CG  1 
ATOM   3618 C  CD1 . TYR   B 1 105 ? 46.864  0.987   30.469  1   39.83 ? 90  TYR   B CD1 1 
ATOM   3619 C  CD2 . TYR   B 1 105 ? 44.966  2.126   31.326  1   40.09 ? 90  TYR   B CD2 1 
ATOM   3620 C  CE1 . TYR   B 1 105 ? 47.642  1.497   31.501  1   40.62 ? 90  TYR   B CE1 1 
ATOM   3621 C  CE2 . TYR   B 1 105 ? 45.729  2.635   32.364  1   41.42 ? 90  TYR   B CE2 1 
ATOM   3622 C  CZ  . TYR   B 1 105 ? 47.071  2.325   32.444  1   42.21 ? 90  TYR   B CZ  1 
ATOM   3623 O  OH  . TYR   B 1 105 ? 47.813  2.831   33.48   1   43.76 ? 90  TYR   B OH  1 
ATOM   3624 N  N   . VAL   B 1 106 ? 41.954  -0.159  30.576  1   35.6  ? 91  VAL   B N   1 
ATOM   3625 C  CA  . VAL   B 1 106 ? 40.999  -0.003  31.653  1   34.95 ? 91  VAL   B CA  1 
ATOM   3626 C  C   . VAL   B 1 106 ? 40.588  -1.366  32.212  1   34.8  ? 91  VAL   B C   1 
ATOM   3627 O  O   . VAL   B 1 106 ? 40.622  -1.55   33.429  1   34.77 ? 91  VAL   B O   1 
ATOM   3628 C  CB  . VAL   B 1 106 ? 39.779  0.853   31.214  1   35.22 ? 91  VAL   B CB  1 
ATOM   3629 C  CG1 . VAL   B 1 106 ? 38.672  0.813   32.252  1   35.97 ? 91  VAL   B CG1 1 
ATOM   3630 C  CG2 . VAL   B 1 106 ? 40.182  2.292   30.912  1   35.64 ? 91  VAL   B CG2 1 
ATOM   3631 N  N   . TRP   B 1 107 ? 40.256  -2.33   31.338  1   33.75 ? 92  TRP   B N   1 
ATOM   3632 C  CA  . TRP   B 1 107 ? 39.723  -3.598  31.808  1   34.1  ? 92  TRP   B CA  1 
ATOM   3633 C  C   . TRP   B 1 107 ? 40.762  -4.69   32.075  1   34.04 ? 92  TRP   B C   1 
ATOM   3634 O  O   . TRP   B 1 107 ? 40.417  -5.702  32.683  1   33.85 ? 92  TRP   B O   1 
ATOM   3635 C  CB  . TRP   B 1 107 ? 38.605  -4.116  30.859  1   34.26 ? 92  TRP   B CB  1 
ATOM   3636 C  CG  . TRP   B 1 107 ? 37.505  -3.111  30.576  1   34.37 ? 92  TRP   B CG  1 
ATOM   3637 C  CD1 . TRP   B 1 107 ? 37.161  -2.585  29.36   1   34.66 ? 92  TRP   B CD1 1 
ATOM   3638 C  CD2 . TRP   B 1 107 ? 36.682  -2.446  31.545  1   34.71 ? 92  TRP   B CD2 1 
ATOM   3639 N  NE1 . TRP   B 1 107 ? 36.181  -1.629  29.516  1   34.85 ? 92  TRP   B NE1 1 
ATOM   3640 C  CE2 . TRP   B 1 107 ? 35.866  -1.53   30.85   1   35.28 ? 92  TRP   B CE2 1 
ATOM   3641 C  CE3 . TRP   B 1 107 ? 36.539  -2.552  32.936  1   35.5  ? 92  TRP   B CE3 1 
ATOM   3642 C  CZ2 . TRP   B 1 107 ? 34.917  -0.742  31.5    1   36.19 ? 92  TRP   B CZ2 1 
ATOM   3643 C  CZ3 . TRP   B 1 107 ? 35.624  -1.749  33.575  1   36.24 ? 92  TRP   B CZ3 1 
ATOM   3644 C  CH2 . TRP   B 1 107 ? 34.793  -0.891  32.858  1   36.47 ? 92  TRP   B CH2 1 
ATOM   3645 N  N   . GLY   B 1 108 ? 42.001  -4.502  31.635  1   33.77 ? 93  GLY   B N   1 
ATOM   3646 C  CA  . GLY   B 1 108 ? 43.061  -5.474  31.854  1   34.29 ? 93  GLY   B CA  1 
ATOM   3647 C  C   . GLY   B 1 108 ? 42.748  -6.837  31.282  1   34.19 ? 93  GLY   B C   1 
ATOM   3648 O  O   . GLY   B 1 108 ? 42.362  -6.942  30.121  1   35.49 ? 93  GLY   B O   1 
ATOM   3649 N  N   . LYS   B 1 109 ? 42.807  -7.867  32.114  1   32.86 ? 94  LYS   B N   1 
ATOM   3650 C  CA  . LYS   B 1 109 ? 42.463  -9.222  31.687  1   32.71 ? 94  LYS   B CA  1 
ATOM   3651 C  C   . LYS   B 1 109 ? 40.941  -9.488  31.674  1   33.75 ? 94  LYS   B C   1 
ATOM   3652 O  O   . LYS   B 1 109 ? 40.547  -10.594 31.36   1   33.42 ? 94  LYS   B O   1 
ATOM   3653 C  CB  . LYS   B 1 109 ? 43.174  -10.28  32.544  1   33.56 ? 94  LYS   B CB  1 
ATOM   3654 C  CG  . LYS   B 1 109 ? 44.697  -10.272 32.357  1   37.2  ? 94  LYS   B CG  1 
ATOM   3655 C  CD  . LYS   B 1 109 ? 45.411  -11.134 33.368  1   40.9  ? 94  LYS   B CD  1 
ATOM   3656 C  CE  . LYS   B 1 109 ? 46.913  -11.018 33.235  1   43.21 ? 94  LYS   B CE  1 
ATOM   3657 N  NZ  . LYS   B 1 109 ? 47.607  -12.159 33.906  1   44.43 ? 94  LYS   B NZ  1 
ATOM   3658 N  N   . GLY   B 1 110 ? 40.123  -8.491  31.996  1   34.92 ? 95  GLY   B N   1 
ATOM   3659 C  CA  . GLY   B 1 110 ? 38.679  -8.629  31.994  1   37.33 ? 95  GLY   B CA  1 
ATOM   3660 C  C   . GLY   B 1 110 ? 38.145  -9.389  33.184  1   40.19 ? 95  GLY   B C   1 
ATOM   3661 O  O   . GLY   B 1 110 ? 37.143  -10.106 33.065  1   40.88 ? 95  GLY   B O   1 
ATOM   3662 N  N   . HIS   B 1 111 ? 38.797  -9.232  34.34   1   41.34 ? 96  HIS   B N   1 
ATOM   3663 C  CA  . HIS   B 1 111 ? 38.362  -9.947  35.532  1   42.92 ? 96  HIS   B CA  1 
ATOM   3664 C  C   . HIS   B 1 111 ? 38.002  -9.068  36.704  1   43.43 ? 96  HIS   B C   1 
ATOM   3665 O  O   . HIS   B 1 111 ? 37.769  -9.605  37.772  1   44.2  ? 96  HIS   B O   1 
ATOM   3666 C  CB  . HIS   B 1 111 ? 39.405  -10.989 35.946  1   45.51 ? 96  HIS   B CB  1 
ATOM   3667 C  CG  . HIS   B 1 111 ? 39.593  -12.05  34.911  1   50.83 ? 96  HIS   B CG  1 
ATOM   3668 N  ND1 . HIS   B 1 111 ? 38.511  -12.732 34.374  1   54.09 ? 96  HIS   B ND1 1 
ATOM   3669 C  CD2 . HIS   B 1 111 ? 40.729  -12.51  34.339  1   52.47 ? 96  HIS   B CD2 1 
ATOM   3670 C  CE1 . HIS   B 1 111 ? 39.022  -13.574 33.487  1   54.69 ? 96  HIS   B CE1 1 
ATOM   3671 N  NE2 . HIS   B 1 111 ? 40.353  -13.475 33.429  1   54.06 ? 96  HIS   B NE2 1 
ATOM   3672 N  N   . GLY   B 1 112 ? 37.914  -7.753  36.518  1   43.71 ? 97  GLY   B N   1 
ATOM   3673 C  CA  . GLY   B 1 112 ? 37.533  -6.86   37.607  1   44.1  ? 97  GLY   B CA  1 
ATOM   3674 C  C   . GLY   B 1 112 ? 38.612  -5.936  38.13   1   44.44 ? 97  GLY   B C   1 
ATOM   3675 O  O   . GLY   B 1 112 ? 38.286  -4.967  38.817  1   45.74 ? 97  GLY   B O   1 
ATOM   3676 N  N   . ASP   B 1 113 ? 39.895  -6.222  37.853  1   43.28 ? 98  ASP   B N   1 
ATOM   3677 C  CA  A ASP   B 1 113 ? 40.982  -5.334  38.295  0.5 43.73 ? 98  ASP   B CA  1 
ATOM   3678 C  CA  B ASP   B 1 113 ? 40.965  -5.35   38.306  0.5 43.07 ? 98  ASP   B CA  1 
ATOM   3679 C  C   . ASP   B 1 113 ? 41.075  -4.274  37.23   1   43.75 ? 98  ASP   B C   1 
ATOM   3680 O  O   . ASP   B 1 113 ? 41.579  -4.531  36.13   1   43.99 ? 98  ASP   B O   1 
ATOM   3681 C  CB  A ASP   B 1 113 ? 42.342  -6.056  38.453  0.5 45.57 ? 98  ASP   B CB  1 
ATOM   3682 C  CB  B ASP   B 1 113 ? 42.253  -6.158  38.53   0.5 42.9  ? 98  ASP   B CB  1 
ATOM   3683 C  CG  A ASP   B 1 113 ? 43.531  -5.097  38.522  0.5 50.25 ? 98  ASP   B CG  1 
ATOM   3684 C  CG  B ASP   B 1 113 ? 42.026  -7.337  39.468  0.5 43.26 ? 98  ASP   B CG  1 
ATOM   3685 O  OD1 A ASP   B 1 113 ? 43.521  -4.205  39.378  0.5 51.06 ? 98  ASP   B OD1 1 
ATOM   3686 O  OD1 B ASP   B 1 113 ? 41.18   -7.214  40.388  0.5 42.38 ? 98  ASP   B OD1 1 
ATOM   3687 O  OD2 A ASP   B 1 113 ? 44.419  -5.194  37.662  0.5 52.8  ? 98  ASP   B OD2 1 
ATOM   3688 O  OD2 B ASP   B 1 113 ? 42.688  -8.383  39.278  0.5 43.89 ? 98  ASP   B OD2 1 
ATOM   3689 N  N   . VAL   B 1 114 ? 40.542  -3.106  37.534  1   43.44 ? 99  VAL   B N   1 
ATOM   3690 C  CA  . VAL   B 1 114 ? 40.487  -2.027  36.577  1   44.09 ? 99  VAL   B CA  1 
ATOM   3691 C  C   . VAL   B 1 114 ? 41.484  -0.853  36.841  1   44.93 ? 99  VAL   B C   1 
ATOM   3692 O  O   . VAL   B 1 114 ? 42.086  -0.737  37.906  1   45.43 ? 99  VAL   B O   1 
ATOM   3693 C  CB  . VAL   B 1 114 ? 39.009  -1.509  36.452  1   44.4  ? 99  VAL   B CB  1 
ATOM   3694 C  CG1 . VAL   B 1 114 ? 37.987  -2.644  36.337  1   45.18 ? 99  VAL   B CG1 1 
ATOM   3695 C  CG2 . VAL   B 1 114 ? 38.648  -0.542  37.57   1   44.29 ? 99  VAL   B CG2 1 
ATOM   3696 N  N   . ARG   B 1 115 ? 41.65   0.007   35.844  1   44.85 ? 100 ARG   B N   1 
ATOM   3697 C  CA  . ARG   B 1 115 ? 42.442  1.218   35.958  1   45.52 ? 100 ARG   B CA  1 
ATOM   3698 C  C   . ARG   B 1 115 ? 41.465  2.384   35.912  1   45.54 ? 100 ARG   B C   1 
ATOM   3699 O  O   . ARG   B 1 115 ? 40.613  2.42    35.024  1   45.62 ? 100 ARG   B O   1 
ATOM   3700 C  CB  . ARG   B 1 115 ? 43.418  1.325   34.784  1   47.05 ? 100 ARG   B CB  1 
ATOM   3701 C  CG  . ARG   B 1 115 ? 44.639  0.446   34.942  1   51.36 ? 100 ARG   B CG  1 
ATOM   3702 C  CD  . ARG   B 1 115 ? 45.567  1.011   35.992  1   55.82 ? 100 ARG   B CD  1 
ATOM   3703 N  NE  . ARG   B 1 115 ? 45.972  -0.046  36.91   1   60.11 ? 100 ARG   B NE  1 
ATOM   3704 C  CZ  . ARG   B 1 115 ? 47.158  -0.645  36.895  1   62.54 ? 100 ARG   B CZ  1 
ATOM   3705 N  NH1 . ARG   B 1 115 ? 48.098  -0.256  36.042  1   62.19 ? 100 ARG   B NH1 1 
ATOM   3706 N  NH2 . ARG   B 1 115 ? 47.422  -1.621  37.75   1   63.31 ? 100 ARG   B NH2 1 
ATOM   3707 N  N   . LYS   B 1 116 ? 41.589  3.337   36.847  1   45.29 ? 101 LYS   B N   1 
ATOM   3708 C  CA  . LYS   B 1 116 ? 40.72   4.517   36.904  1   45.78 ? 101 LYS   B CA  1 
ATOM   3709 C  C   . LYS   B 1 116 ? 41.334  5.796   36.333  1   45.97 ? 101 LYS   B C   1 
ATOM   3710 O  O   . LYS   B 1 116 ? 40.68   6.842   36.343  1   46.24 ? 101 LYS   B O   1 
ATOM   3711 C  CB  . LYS   B 1 116 ? 40.247  4.738   38.34   1   47.66 ? 101 LYS   B CB  1 
ATOM   3712 C  CG  . LYS   B 1 116 ? 39.426  3.561   38.84   1   52.01 ? 101 LYS   B CG  1 
ATOM   3713 C  CD  . LYS   B 1 116 ? 39.406  3.464   40.345  1   57.22 ? 101 LYS   B CD  1 
ATOM   3714 C  CE  . LYS   B 1 116 ? 38.747  2.182   40.808  1   61.58 ? 101 LYS   B CE  1 
ATOM   3715 N  NZ  . LYS   B 1 116 ? 37.259  2.273   40.772  1   64.74 ? 101 LYS   B NZ  1 
ATOM   3716 N  N   . VAL   B 1 117 ? 42.589  5.73    35.867  1   45.75 ? 102 VAL   B N   1 
ATOM   3717 C  CA  . VAL   B 1 117 ? 43.292  6.861   35.28   1   46.09 ? 102 VAL   B CA  1 
ATOM   3718 C  C   . VAL   B 1 117 ? 43.927  6.376   33.994  1   46.17 ? 102 VAL   B C   1 
ATOM   3719 O  O   . VAL   B 1 117 ? 44.635  5.384   34.015  1   46.34 ? 102 VAL   B O   1 
ATOM   3720 C  CB  . VAL   B 1 117 ? 44.396  7.45    36.224  1   46.74 ? 102 VAL   B CB  1 
ATOM   3721 C  CG1 . VAL   B 1 117 ? 45.044  8.681   35.603  1   47.27 ? 102 VAL   B CG1 1 
ATOM   3722 C  CG2 . VAL   B 1 117 ? 43.849  7.784   37.609  1   46.89 ? 102 VAL   B CG2 1 
ATOM   3723 N  N   . LEU   B 1 118 ? 43.685  7.061   32.883  1   46.26 ? 103 LEU   B N   1 
ATOM   3724 C  CA  . LEU   B 1 118 ? 44.296  6.741   31.591  1   47.19 ? 103 LEU   B CA  1 
ATOM   3725 C  C   . LEU   B 1 118 ? 45.518  7.656   31.499  1   48.75 ? 103 LEU   B C   1 
ATOM   3726 O  O   . LEU   B 1 118 ? 45.384  8.868   31.697  1   48.99 ? 103 LEU   B O   1 
ATOM   3727 C  CB  . LEU   B 1 118 ? 43.318  7.029   30.447  1   46.64 ? 103 LEU   B CB  1 
ATOM   3728 C  CG  . LEU   B 1 118 ? 43.784  6.598   29.057  1   47.17 ? 103 LEU   B CG  1 
ATOM   3729 C  CD1 . LEU   B 1 118 ? 43.798  5.092   28.929  1   47.23 ? 103 LEU   B CD1 1 
ATOM   3730 C  CD2 . LEU   B 1 118 ? 42.905  7.182   27.984  1   47.48 ? 103 LEU   B CD2 1 
ATOM   3731 N  N   . PRO   B 1 119 ? 46.717  7.088   31.285  1   49.51 ? 104 PRO   B N   1 
ATOM   3732 C  CA  . PRO   B 1 119 ? 47.946  7.91    31.288  1   50.4  ? 104 PRO   B CA  1 
ATOM   3733 C  C   . PRO   B 1 119 ? 47.969  9       30.237  1   51.89 ? 104 PRO   B C   1 
ATOM   3734 O  O   . PRO   B 1 119 ? 47.499  8.772   29.132  1   52.18 ? 104 PRO   B O   1 
ATOM   3735 C  CB  . PRO   B 1 119 ? 49.055  6.895   31.032  1   51.03 ? 104 PRO   B CB  1 
ATOM   3736 C  CG  . PRO   B 1 119 ? 48.452  5.557   31.374  1   51.45 ? 104 PRO   B CG  1 
ATOM   3737 C  CD  . PRO   B 1 119 ? 47.01   5.667   31.039  1   49.52 ? 104 PRO   B CD  1 
ATOM   3738 N  N   . ARG   B 1 120 ? 48.534  10.169  30.57   1   52.37 ? 105 ARG   B N   1 
ATOM   3739 C  CA  . ARG   B 1 120 ? 48.582  11.323  29.675  1   53.16 ? 105 ARG   B CA  1 
ATOM   3740 C  C   . ARG   B 1 120 ? 49.157  11.061  28.298  1   53.19 ? 105 ARG   B C   1 
ATOM   3741 O  O   . ARG   B 1 120 ? 48.706  11.653  27.324  1   53.13 ? 105 ARG   B O   1 
ATOM   3742 C  CB  . ARG   B 1 120 ? 49.328  12.49   30.336  1   55.42 ? 105 ARG   B CB  1 
ATOM   3743 C  CG  . ARG   B 1 120 ? 50.846  12.314  30.476  1   59.11 ? 105 ARG   B CG  1 
ATOM   3744 C  CD  . ARG   B 1 120 ? 51.453  13.152  31.602  1   62.61 ? 105 ARG   B CD  1 
ATOM   3745 N  NE  . ARG   B 1 120 ? 50.762  14.431  31.787  1   64.7  ? 105 ARG   B NE  1 
ATOM   3746 C  CZ  . ARG   B 1 120 ? 50.209  14.826  32.928  1   66.14 ? 105 ARG   B CZ  1 
ATOM   3747 N  NH1 . ARG   B 1 120 ? 50.333  14.088  34.024  1   65.51 ? 105 ARG   B NH1 1 
ATOM   3748 N  NH2 . ARG   B 1 120 ? 49.574  15.99   32.997  1   66.12 ? 105 ARG   B NH2 1 
ATOM   3749 N  N   . ASN   B 1 121 ? 50.151  10.193  28.21   1   53.29 ? 106 ASN   B N   1 
ATOM   3750 C  CA  . ASN   B 1 121 ? 50.812  9.852   26.954  1   53.65 ? 106 ASN   B CA  1 
ATOM   3751 C  C   . ASN   B 1 121 ? 49.84   9.332   25.9    1   52.36 ? 106 ASN   B C   1 
ATOM   3752 O  O   . ASN   B 1 121 ? 50.075  9.53    24.706  1   52.61 ? 106 ASN   B O   1 
ATOM   3753 C  CB  . ASN   B 1 121 ? 52.004  8.886   27.152  1   56.6  ? 106 ASN   B CB  1 
ATOM   3754 C  CG  . ASN   B 1 121 ? 51.979  7.953   28.373  1   62.4  ? 106 ASN   B CG  1 
ATOM   3755 O  OD1 . ASN   B 1 121 ? 51.654  8.353   29.508  1   63.67 ? 106 ASN   B OD1 1 
ATOM   3756 N  ND2 . ASN   B 1 121 ? 52.428  6.706   28.197  1   63.88 ? 106 ASN   B ND2 1 
ATOM   3757 N  N   . ILE   B 1 122 ? 48.751  8.67    26.334  1   50.77 ? 107 ILE   B N   1 
ATOM   3758 C  CA  . ILE   B 1 122 ? 47.73   8.168   25.413  1   49.34 ? 107 ILE   B CA  1 
ATOM   3759 C  C   . ILE   B 1 122 ? 46.439  8.988   25.527  1   47.78 ? 107 ILE   B C   1 
ATOM   3760 O  O   . ILE   B 1 122 ? 45.86   9.322   24.502  1   47.29 ? 107 ILE   B O   1 
ATOM   3761 C  CB  . ILE   B 1 122 ? 47.513  6.651   25.549  1   49.38 ? 107 ILE   B CB  1 
ATOM   3762 C  CG1 . ILE   B 1 122 ? 46.809  6.081   24.333  1   50.53 ? 107 ILE   B CG1 1 
ATOM   3763 C  CG2 . ILE   B 1 122 ? 46.823  6.262   26.861  1   49.62 ? 107 ILE   B CG2 1 
ATOM   3764 C  CD1 . ILE   B 1 122 ? 46.791  4.618   24.277  1   51.15 ? 107 ILE   B CD1 1 
ATOM   3765 N  N   . ALA   B 1 123 ? 46.045  9.393   26.747  1   46.67 ? 108 ALA   B N   1 
ATOM   3766 C  CA  . ALA   B 1 123 ? 44.837  10.184  26.953  1   46.86 ? 108 ALA   B CA  1 
ATOM   3767 C  C   . ALA   B 1 123 ? 44.838  11.511  26.21   1   47.76 ? 108 ALA   B C   1 
ATOM   3768 O  O   . ALA   B 1 123 ? 43.796  11.906  25.677  1   48.28 ? 108 ALA   B O   1 
ATOM   3769 C  CB  . ALA   B 1 123 ? 44.591  10.422  28.433  1   46.84 ? 108 ALA   B CB  1 
ATOM   3770 N  N   . VAL   B 1 124 ? 45.994  12.202  26.152  1   46.96 ? 109 VAL   B N   1 
ATOM   3771 C  CA  . VAL   B 1 124 ? 46.047  13.497  25.481  1   46.44 ? 109 VAL   B CA  1 
ATOM   3772 C  C   . VAL   B 1 124 ? 45.843  13.353  23.97   1   46.03 ? 109 VAL   B C   1 
ATOM   3773 O  O   . VAL   B 1 124 ? 44.883  13.951  23.473  1   46.93 ? 109 VAL   B O   1 
ATOM   3774 C  CB  . VAL   B 1 124 ? 47.293  14.336  25.864  1   46.79 ? 109 VAL   B CB  1 
ATOM   3775 C  CG1 . VAL   B 1 124 ? 47.488  15.516  24.911  1   47.5  ? 109 VAL   B CG1 1 
ATOM   3776 C  CG2 . VAL   B 1 124 ? 47.171  14.824  27.302  1   46.95 ? 109 VAL   B CG2 1 
ATOM   3777 N  N   . PRO   B 1 125 ? 46.629  12.545  23.223  1   44.93 ? 110 PRO   B N   1 
ATOM   3778 C  CA  . PRO   B 1 125 ? 46.359  12.423  21.782  1   44.55 ? 110 PRO   B CA  1 
ATOM   3779 C  C   . PRO   B 1 125 ? 44.982  11.815  21.48   1   44.59 ? 110 PRO   B C   1 
ATOM   3780 O  O   . PRO   B 1 125 ? 44.386  12.118  20.451  1   45.06 ? 110 PRO   B O   1 
ATOM   3781 C  CB  . PRO   B 1 125 ? 47.498  11.514  21.27   1   45.34 ? 110 PRO   B CB  1 
ATOM   3782 C  CG  . PRO   B 1 125 ? 48.007  10.8    22.466  1   45.71 ? 110 PRO   B CG  1 
ATOM   3783 C  CD  . PRO   B 1 125 ? 47.81   11.748  23.622  1   44.33 ? 110 PRO   B CD  1 
ATOM   3784 N  N   . TYR   B 1 126 ? 44.487  10.936  22.359  1   44.03 ? 111 TYR   B N   1 
ATOM   3785 C  CA  . TYR   B 1 126 ? 43.187  10.298  22.149  1   43.37 ? 111 TYR   B CA  1 
ATOM   3786 C  C   . TYR   B 1 126 ? 42.092  11.344  22.255  1   43.36 ? 111 TYR   B C   1 
ATOM   3787 O  O   . TYR   B 1 126 ? 41.279  11.44   21.345  1   43.77 ? 111 TYR   B O   1 
ATOM   3788 C  CB  . TYR   B 1 126 ? 43.001  9.122   23.115  1   42.44 ? 111 TYR   B CB  1 
ATOM   3789 C  CG  . TYR   B 1 126 ? 41.773  8.267   22.872  1   42.48 ? 111 TYR   B CG  1 
ATOM   3790 C  CD1 . TYR   B 1 126 ? 41.253  8.101   21.59   1   42.72 ? 111 TYR   B CD1 1 
ATOM   3791 C  CD2 . TYR   B 1 126 ? 41.164  7.583   23.913  1   42.6  ? 111 TYR   B CD2 1 
ATOM   3792 C  CE1 . TYR   B 1 126 ? 40.138  7.312   21.364  1   43.08 ? 111 TYR   B CE1 1 
ATOM   3793 C  CE2 . TYR   B 1 126 ? 40.055  6.778   23.696  1   42.84 ? 111 TYR   B CE2 1 
ATOM   3794 C  CZ  . TYR   B 1 126 ? 39.541  6.649   22.421  1   43.24 ? 111 TYR   B CZ  1 
ATOM   3795 O  OH  . TYR   B 1 126 ? 38.452  5.848   22.199  1   42.07 ? 111 TYR   B OH  1 
ATOM   3796 N  N   . CYS   B 1 127 ? 42.106  12.182  23.3    1   43.16 ? 112 CYS   B N   1 
ATOM   3797 C  CA  . CYS   B 1 127 ? 41.109  13.239  23.452  1   43.72 ? 112 CYS   B CA  1 
ATOM   3798 C  C   . CYS   B 1 127 ? 41.206  14.317  22.365  1   44.26 ? 112 CYS   B C   1 
ATOM   3799 O  O   . CYS   B 1 127 ? 40.177  14.911  21.991  1   44.99 ? 112 CYS   B O   1 
ATOM   3800 C  CB  . CYS   B 1 127 ? 41.17   13.864  24.838  1   44.89 ? 112 CYS   B CB  1 
ATOM   3801 S  SG  . CYS   B 1 127 ? 40.739  12.746  26.202  1   49.32 ? 112 CYS   B SG  1 
ATOM   3802 N  N   . GLN   B 1 128 ? 42.429  14.603  21.886  1   43.1  ? 113 GLN   B N   1 
ATOM   3803 C  CA  . GLN   B 1 128 ? 42.606  15.604  20.832  1   42.77 ? 113 GLN   B CA  1 
ATOM   3804 C  C   . GLN   B 1 128 ? 42.043  15.086  19.51   1   42.81 ? 113 GLN   B C   1 
ATOM   3805 O  O   . GLN   B 1 128 ? 41.426  15.839  18.759  1   43.87 ? 113 GLN   B O   1 
ATOM   3806 C  CB  . GLN   B 1 128 ? 44.096  15.943  20.659  1   43.64 ? 113 GLN   B CB  1 
ATOM   3807 C  CG  . GLN   B 1 128 ? 44.717  16.655  21.846  1   46.3  ? 113 GLN   B CG  1 
ATOM   3808 C  CD  . GLN   B 1 128 ? 46.191  16.942  21.641  1   50.42 ? 113 GLN   B CD  1 
ATOM   3809 O  OE1 . GLN   B 1 128 ? 46.921  16.228  20.917  1   50.53 ? 113 GLN   B OE1 1 
ATOM   3810 N  NE2 . GLN   B 1 128 ? 46.659  18.005  22.289  1   51.72 ? 113 GLN   B NE2 1 
ATOM   3811 N  N   . LEU   B 1 129 ? 42.282  13.821  19.206  1   42.32 ? 114 LEU   B N   1 
ATOM   3812 C  CA  . LEU   B 1 129 ? 41.788  13.205  17.98   1   43.31 ? 114 LEU   B CA  1 
ATOM   3813 C  C   . LEU   B 1 129 ? 40.259  13.069  18.034  1   44.34 ? 114 LEU   B C   1 
ATOM   3814 O  O   . LEU   B 1 129 ? 39.577  13.315  17.039  1   45.26 ? 114 LEU   B O   1 
ATOM   3815 C  CB  . LEU   B 1 129 ? 42.421  11.83   17.826  1   43.46 ? 114 LEU   B CB  1 
ATOM   3816 C  CG  . LEU   B 1 129 ? 42.005  11.035  16.619  1   45.24 ? 114 LEU   B CG  1 
ATOM   3817 C  CD1 . LEU   B 1 129 ? 42.373  11.742  15.329  1   45.84 ? 114 LEU   B CD1 1 
ATOM   3818 C  CD2 . LEU   B 1 129 ? 42.637  9.68    16.656  1   46.31 ? 114 LEU   B CD2 1 
ATOM   3819 N  N   . SER   B 1 130 ? 39.721  12.755  19.221  1   43.77 ? 115 SER   B N   1 
ATOM   3820 C  CA  . SER   B 1 130 ? 38.294  12.635  19.427  1   43.72 ? 115 SER   B CA  1 
ATOM   3821 C  C   . SER   B 1 130 ? 37.627  13.99   19.233  1   44.88 ? 115 SER   B C   1 
ATOM   3822 O  O   . SER   B 1 130 ? 36.58   14.06   18.584  1   45.31 ? 115 SER   B O   1 
ATOM   3823 C  CB  . SER   B 1 130 ? 38.011  12.082  20.819  1   42.48 ? 115 SER   B CB  1 
ATOM   3824 O  OG  . SER   B 1 130 ? 38.491  10.746  20.898  1   41.68 ? 115 SER   B OG  1 
ATOM   3825 N  N   . LYS   B 1 131 ? 38.238  15.072  19.747  1   44.9  ? 116 LYS   B N   1 
ATOM   3826 C  CA  . LYS   B 1 131 ? 37.666  16.416  19.574  1   45.58 ? 116 LYS   B CA  1 
ATOM   3827 C  C   . LYS   B 1 131 ? 37.617  16.812  18.101  1   45.85 ? 116 LYS   B C   1 
ATOM   3828 O  O   . LYS   B 1 131 ? 36.631  17.391  17.647  1   46.72 ? 116 LYS   B O   1 
ATOM   3829 C  CB  . LYS   B 1 131 ? 38.442  17.469  20.383  1   48.52 ? 116 LYS   B CB  1 
ATOM   3830 C  CG  . LYS   B 1 131 ? 37.786  18.851  20.361  1   53.54 ? 116 LYS   B CG  1 
ATOM   3831 C  CD  . LYS   B 1 131 ? 38.623  19.928  21.084  1   58.45 ? 116 LYS   B CD  1 
ATOM   3832 N  N   . LYS   B 1 132 ? 38.648  16.438  17.348  1   45.6  ? 117 LYS   B N   1 
ATOM   3833 C  CA  . LYS   B 1 132 ? 38.773  16.702  15.922  1   45.71 ? 117 LYS   B CA  1 
ATOM   3834 C  C   . LYS   B 1 132 ? 37.695  15.95   15.145  1   45.71 ? 117 LYS   B C   1 
ATOM   3835 O  O   . LYS   B 1 132 ? 37.112  16.51   14.212  1   46.48 ? 117 LYS   B O   1 
ATOM   3836 C  CB  . LYS   B 1 132 ? 40.168  16.267  15.447  1   47.73 ? 117 LYS   B CB  1 
ATOM   3837 C  CG  . LYS   B 1 132 ? 40.568  16.811  14.084  1   52.02 ? 117 LYS   B CG  1 
ATOM   3838 C  CD  . LYS   B 1 132 ? 42.063  16.65   13.831  1   55.97 ? 117 LYS   B CD  1 
ATOM   3839 N  N   . LEU   B 1 133 ? 37.439  14.676  15.501  1   44.4  ? 118 LEU   B N   1 
ATOM   3840 C  CA  . LEU   B 1 133 ? 36.435  13.887  14.796  1   43.68 ? 118 LEU   B CA  1 
ATOM   3841 C  C   . LEU   B 1 133 ? 35.006  14.048  15.34   1   42.95 ? 118 LEU   B C   1 
ATOM   3842 O  O   . LEU   B 1 133 ? 34.093  13.422  14.799  1   43.14 ? 118 LEU   B O   1 
ATOM   3843 C  CB  . LEU   B 1 133 ? 36.831  12.403  14.758  1   43.7  ? 118 LEU   B CB  1 
ATOM   3844 C  CG  . LEU   B 1 133 ? 38.017  12.053  13.872  1   45.17 ? 118 LEU   B CG  1 
ATOM   3845 C  CD1 . LEU   B 1 133 ? 38.386  10.609  14.006  1   45.6  ? 118 LEU   B CD1 1 
ATOM   3846 C  CD2 . LEU   B 1 133 ? 37.721  12.299  12.417  1   46.08 ? 118 LEU   B CD2 1 
ATOM   3847 N  N   . GLU   B 1 134 ? 34.823  14.872  16.393  1   41.7  ? 119 GLU   B N   1 
ATOM   3848 C  CA  . GLU   B 1 134 ? 33.56   15.15   17.07   1   42.2  ? 119 GLU   B CA  1 
ATOM   3849 C  C   . GLU   B 1 134 ? 32.937  13.88   17.628  1   41.53 ? 119 GLU   B C   1 
ATOM   3850 O  O   . GLU   B 1 134 ? 31.752  13.618  17.437  1   41.58 ? 119 GLU   B O   1 
ATOM   3851 C  CB  . GLU   B 1 134 ? 32.57   15.912  16.177  1   45.02 ? 119 GLU   B CB  1 
ATOM   3852 C  CG  . GLU   B 1 134 ? 33.065  17.272  15.757  1   52.09 ? 119 GLU   B CG  1 
ATOM   3853 C  CD  . GLU   B 1 134 ? 32.031  17.98   14.914  1   61.24 ? 119 GLU   B CD  1 
ATOM   3854 O  OE1 . GLU   B 1 134 ? 30.944  18.288  15.456  1   63.52 ? 119 GLU   B OE1 1 
ATOM   3855 O  OE2 . GLU   B 1 134 ? 32.292  18.197  13.707  1   63.48 ? 119 GLU   B OE2 1 
ATOM   3856 N  N   . LEU   B 1 135 ? 33.758  13.089  18.312  1   40.25 ? 120 LEU   B N   1 
ATOM   3857 C  CA  . LEU   B 1 135 ? 33.356  11.845  18.942  1   39.53 ? 120 LEU   B CA  1 
ATOM   3858 C  C   . LEU   B 1 135 ? 33.936  11.816  20.352  1   40.73 ? 120 LEU   B C   1 
ATOM   3859 O  O   . LEU   B 1 135 ? 34.944  12.473  20.618  1   42.44 ? 120 LEU   B O   1 
ATOM   3860 C  CB  . LEU   B 1 135 ? 33.891  10.67   18.115  1   38.31 ? 120 LEU   B CB  1 
ATOM   3861 C  CG  . LEU   B 1 135 ? 33.16   10.443  16.802  1   38.42 ? 120 LEU   B CG  1 
ATOM   3862 C  CD1 . LEU   B 1 135 ? 33.905  9.485   15.906  1   38.04 ? 120 LEU   B CD1 1 
ATOM   3863 C  CD2 . LEU   B 1 135 ? 31.718  9.955   17.055  1   38.95 ? 120 LEU   B CD2 1 
ATOM   3864 N  N   . PRO   B 1 136 ? 33.319  11.088  21.28   1   39.54 ? 121 PRO   B N   1 
ATOM   3865 C  CA  . PRO   B 1 136 ? 33.884  11.005  22.642  1   38.33 ? 121 PRO   B CA  1 
ATOM   3866 C  C   . PRO   B 1 136 ? 35.145  10.128  22.697  1   36.17 ? 121 PRO   B C   1 
ATOM   3867 O  O   . PRO   B 1 136 ? 35.37   9.264   21.826  1   35.38 ? 121 PRO   B O   1 
ATOM   3868 C  CB  . PRO   B 1 136 ? 32.737  10.404  23.458  1   39.34 ? 121 PRO   B CB  1 
ATOM   3869 C  CG  . PRO   B 1 136 ? 32.023  9.555   22.474  1   40.75 ? 121 PRO   B CG  1 
ATOM   3870 C  CD  . PRO   B 1 136 ? 32.092  10.277  21.145  1   39.41 ? 121 PRO   B CD  1 
ATOM   3871 N  N   . PRO   B 1 137 ? 36.004  10.343  23.714  1   35.51 ? 122 PRO   B N   1 
ATOM   3872 C  CA  . PRO   B 1 137 ? 37.216  9.523   23.829  1   34.86 ? 122 PRO   B CA  1 
ATOM   3873 C  C   . PRO   B 1 137 ? 36.964  8.144   24.455  1   34.62 ? 122 PRO   B C   1 
ATOM   3874 O  O   . PRO   B 1 137 ? 37.441  7.83    25.554  1   34.12 ? 122 PRO   B O   1 
ATOM   3875 C  CB  . PRO   B 1 137 ? 38.136  10.38   24.699  1   35.39 ? 122 PRO   B CB  1 
ATOM   3876 C  CG  . PRO   B 1 137 ? 37.215  11.132  25.584  1   35.81 ? 122 PRO   B CG  1 
ATOM   3877 C  CD  . PRO   B 1 137 ? 35.937  11.355  24.795  1   34.9  ? 122 PRO   B CD  1 
ATOM   3878 N  N   . ILE   B 1 138 ? 36.211  7.321   23.734  1   33.7  ? 123 ILE   B N   1 
ATOM   3879 C  CA  . ILE   B 1 138 ? 35.867  5.944   24.088  1   32.06 ? 123 ILE   B CA  1 
ATOM   3880 C  C   . ILE   B 1 138 ? 35.573  5.231   22.766  1   30.47 ? 123 ILE   B C   1 
ATOM   3881 O  O   . ILE   B 1 138 ? 35.256  5.882   21.764  1   31.33 ? 123 ILE   B O   1 
ATOM   3882 C  CB  . ILE   B 1 138 ? 34.723  5.83    25.13   1   32.31 ? 123 ILE   B CB  1 
ATOM   3883 C  CG1 . ILE   B 1 138 ? 34.643  4.379   25.718  1   32.24 ? 123 ILE   B CG1 1 
ATOM   3884 C  CG2 . ILE   B 1 138 ? 33.372  6.285   24.557  1   33.08 ? 123 ILE   B CG2 1 
ATOM   3885 C  CD1 . ILE   B 1 138 ? 33.736  4.197   26.881  1   32.91 ? 123 ILE   B CD1 1 
ATOM   3886 N  N   . LEU   B 1 139 ? 35.792  3.924   22.721  1   28.94 ? 124 LEU   B N   1 
ATOM   3887 C  CA  . LEU   B 1 139 ? 35.522  3.122   21.528  1   28.76 ? 124 LEU   B CA  1 
ATOM   3888 C  C   . LEU   B 1 139 ? 34.004  3.139   21.26   1   27.96 ? 124 LEU   B C   1 
ATOM   3889 O  O   . LEU   B 1 139 ? 33.219  2.846   22.153  1   26.09 ? 124 LEU   B O   1 
ATOM   3890 C  CB  . LEU   B 1 139 ? 35.972  1.681   21.806  1   28.79 ? 124 LEU   B CB  1 
ATOM   3891 C  CG  . LEU   B 1 139 ? 35.992  0.742   20.628  1   30.17 ? 124 LEU   B CG  1 
ATOM   3892 C  CD1 . LEU   B 1 139 ? 37.042  1.132   19.644  1   30.07 ? 124 LEU   B CD1 1 
ATOM   3893 C  CD2 . LEU   B 1 139 ? 36.192  -0.707  21.092  1   30.26 ? 124 LEU   B CD2 1 
ATOM   3894 N  N   . VAL   B 1 140 ? 33.598  3.502   20.035  1   27.43 ? 125 VAL   B N   1 
ATOM   3895 C  CA  . VAL   B 1 140 ? 32.193  3.558   19.665  1   27.54 ? 125 VAL   B CA  1 
ATOM   3896 C  C   . VAL   B 1 140 ? 31.962  2.527   18.543  1   26.78 ? 125 VAL   B C   1 
ATOM   3897 O  O   . VAL   B 1 140 ? 32.918  2.028   17.937  1   25.69 ? 125 VAL   B O   1 
ATOM   3898 C  CB  . VAL   B 1 140 ? 31.737  4.993   19.241  1   28.55 ? 125 VAL   B CB  1 
ATOM   3899 C  CG1 . VAL   B 1 140 ? 31.984  6.025   20.347  1   28.95 ? 125 VAL   B CG1 1 
ATOM   3900 C  CG2 . VAL   B 1 140 ? 32.411  5.422   17.959  1   28.55 ? 125 VAL   B CG2 1 
ATOM   3901 N  N   . TYR   B 1 141 ? 30.693  2.234   18.248  1   26.99 ? 126 TYR   B N   1 
ATOM   3902 C  CA  . TYR   B 1 141 ? 30.293  1.31    17.199  1   26.41 ? 126 TYR   B CA  1 
ATOM   3903 C  C   . TYR   B 1 141 ? 30.949  1.693   15.84   1   26.92 ? 126 TYR   B C   1 
ATOM   3904 O  O   . TYR   B 1 141 ? 31.312  0.817   15.073  1   28.07 ? 126 TYR   B O   1 
ATOM   3905 C  CB  . TYR   B 1 141 ? 28.759  1.379   17.102  1   25.84 ? 126 TYR   B CB  1 
ATOM   3906 C  CG  . TYR   B 1 141 ? 28.164  0.543   16.001  1   27.13 ? 126 TYR   B CG  1 
ATOM   3907 C  CD1 . TYR   B 1 141 ? 27.921  1.083   14.744  1   28.61 ? 126 TYR   B CD1 1 
ATOM   3908 C  CD2 . TYR   B 1 141 ? 27.751  -0.762  16.239  1   27.91 ? 126 TYR   B CD2 1 
ATOM   3909 C  CE1 . TYR   B 1 141 ? 27.344  0.321   13.732  1   29.55 ? 126 TYR   B CE1 1 
ATOM   3910 C  CE2 . TYR   B 1 141 ? 27.129  -1.51   15.253  1   29.22 ? 126 TYR   B CE2 1 
ATOM   3911 C  CZ  . TYR   B 1 141 ? 26.944  -0.973  13.994  1   30.33 ? 126 TYR   B CZ  1 
ATOM   3912 O  OH  . TYR   B 1 141 ? 26.31   -1.741  13.039  1   31.87 ? 126 TYR   B OH  1 
ATOM   3913 N  N   . ALA   B 1 142 ? 31.062  2.997   15.539  1   27.14 ? 127 ALA   B N   1 
ATOM   3914 C  CA  . ALA   B 1 142 ? 31.672  3.438   14.271  1   28.12 ? 127 ALA   B CA  1 
ATOM   3915 C  C   . ALA   B 1 142 ? 33.189  3.06    14.187  1   30.19 ? 127 ALA   B C   1 
ATOM   3916 O  O   . ALA   B 1 142 ? 33.745  2.928   13.096  1   30.38 ? 127 ALA   B O   1 
ATOM   3917 C  CB  . ALA   B 1 142 ? 31.499  4.933   14.096  1   28.09 ? 127 ALA   B CB  1 
ATOM   3918 N  N   . ASP   B 1 143 ? 33.834  2.851   15.344  1   30.41 ? 128 ASP   B N   1 
ATOM   3919 C  CA  . ASP   B 1 143 ? 35.226  2.431   15.377  1   30.47 ? 128 ASP   B CA  1 
ATOM   3920 C  C   . ASP   B 1 143 ? 35.294  0.92    15.296  1   31.49 ? 128 ASP   B C   1 
ATOM   3921 O  O   . ASP   B 1 143 ? 35.91   0.406   14.363  1   32.86 ? 128 ASP   B O   1 
ATOM   3922 C  CB  . ASP   B 1 143 ? 35.932  2.891   16.674  1   29.22 ? 128 ASP   B CB  1 
ATOM   3923 C  CG  . ASP   B 1 143 ? 35.864  4.364   17.009  1   31.57 ? 128 ASP   B CG  1 
ATOM   3924 O  OD1 . ASP   B 1 143 ? 36.079  5.201   16.095  1   30.91 ? 128 ASP   B OD1 1 
ATOM   3925 O  OD2 . ASP   B 1 143 ? 35.673  4.689   18.204  1   32.36 ? 128 ASP   B OD2 1 
ATOM   3926 N  N   . CYS   B 1 144 ? 34.701  0.197   16.284  1   31.06 ? 129 CYS   B N   1 
ATOM   3927 C  CA  . CYS   B 1 144 ? 34.835  -1.277  16.369  1   30.88 ? 129 CYS   B CA  1 
ATOM   3928 C  C   . CYS   B 1 144 ? 34.078  -2.048  15.301  1   30.89 ? 129 CYS   B C   1 
ATOM   3929 O  O   . CYS   B 1 144 ? 34.399  -3.221  15.089  1   30.09 ? 129 CYS   B O   1 
ATOM   3930 C  CB  . CYS   B 1 144 ? 34.503  -1.799  17.768  1   30.56 ? 129 CYS   B CB  1 
ATOM   3931 S  SG  . CYS   B 1 144 ? 32.778  -1.554  18.269  1   31.58 ? 129 CYS   B SG  1 
ATOM   3932 N  N   . VAL   B 1 145 ? 33.073  -1.438  14.632  1   30.78 ? 130 VAL   B N   1 
ATOM   3933 C  CA  . VAL   B 1 145 ? 32.367  -2.145  13.574  1   29.97 ? 130 VAL   B CA  1 
ATOM   3934 C  C   . VAL   B 1 145 ? 32.651  -1.491  12.23   1   29.92 ? 130 VAL   B C   1 
ATOM   3935 O  O   . VAL   B 1 145 ? 33.177  -2.147  11.329  1   30.63 ? 130 VAL   B O   1 
ATOM   3936 C  CB  . VAL   B 1 145 ? 30.837  -2.297  13.851  1   30.91 ? 130 VAL   B CB  1 
ATOM   3937 C  CG1 . VAL   B 1 145 ? 30.091  -2.759  12.599  1   31.12 ? 130 VAL   B CG1 1 
ATOM   3938 C  CG2 . VAL   B 1 145 ? 30.559  -3.231  15.03   1   31.6  ? 130 VAL   B CG2 1 
ATOM   3939 N  N   . LEU   B 1 146 ? 32.297  -0.206  12.085  1   29.15 ? 131 LEU   B N   1 
ATOM   3940 C  CA  . LEU   B 1 146 ? 32.302  0.479   10.801  1   30.04 ? 131 LEU   B CA  1 
ATOM   3941 C  C   . LEU   B 1 146 ? 33.685  0.696   10.164  1   31.74 ? 131 LEU   B C   1 
ATOM   3942 O  O   . LEU   B 1 146 ? 33.795  0.669   8.925   1   32.83 ? 131 LEU   B O   1 
ATOM   3943 C  CB  . LEU   B 1 146 ? 31.531  1.809   10.921  1   29.42 ? 131 LEU   B CB  1 
ATOM   3944 C  CG  . LEU   B 1 146 ? 30.028  1.685   11.369  1   29.29 ? 131 LEU   B CG  1 
ATOM   3945 C  CD1 . LEU   B 1 146 ? 29.334  3.002   11.298  1   30.89 ? 131 LEU   B CD1 1 
ATOM   3946 C  CD2 . LEU   B 1 146 ? 29.276  0.678   10.533  1   29.19 ? 131 LEU   B CD2 1 
ATOM   3947 N  N   . ALA   B 1 147 ? 34.718  0.89    10.984  1   30.74 ? 132 ALA   B N   1 
ATOM   3948 C  CA  . ALA   B 1 147 ? 36.092  1.106   10.509  1   31.43 ? 132 ALA   B CA  1 
ATOM   3949 C  C   . ALA   B 1 147 ? 37.045  -0.069  10.799  1   32.1  ? 132 ALA   B C   1 
ATOM   3950 O  O   . ALA   B 1 147 ? 38.216  -0.007  10.432  1   33.29 ? 132 ALA   B O   1 
ATOM   3951 C  CB  . ALA   B 1 147 ? 36.642  2.376   11.125  1   31.18 ? 132 ALA   B CB  1 
ATOM   3952 N  N   . ASN   B 1 148 ? 36.56   -1.12   11.463  1   31.21 ? 133 ASN   B N   1 
ATOM   3953 C  CA  . ASN   B 1 148 ? 37.362  -2.263  11.89   1   30.24 ? 133 ASN   B CA  1 
ATOM   3954 C  C   . ASN   B 1 148 ? 37.269  -3.447  10.948  1   30.24 ? 133 ASN   B C   1 
ATOM   3955 O  O   . ASN   B 1 148 ? 36.991  -4.566  11.387  1   30.35 ? 133 ASN   B O   1 
ATOM   3956 C  CB  . ASN   B 1 148 ? 36.932  -2.637  13.305  1   30.17 ? 133 ASN   B CB  1 
ATOM   3957 C  CG  . ASN   B 1 148 ? 37.8    -3.629  14.012  1   31.42 ? 133 ASN   B CG  1 
ATOM   3958 O  OD1 . ASN   B 1 148 ? 38.95   -3.879  13.621  1   32.04 ? 133 ASN   B OD1 1 
ATOM   3959 N  ND2 . ASN   B 1 148 ? 37.266  -4.188  15.112  1   29.7  ? 133 ASN   B ND2 1 
ATOM   3960 N  N   . TRP   B 1 149 ? 37.545  -3.224  9.647   1   30.47 ? 134 TRP   B N   1 
ATOM   3961 C  CA  . TRP   B 1 149 ? 37.405  -4.328  8.701   1   31.46 ? 134 TRP   B CA  1 
ATOM   3962 C  C   . TRP   B 1 149 ? 38.294  -4.241  7.476   1   32.56 ? 134 TRP   B C   1 
ATOM   3963 O  O   . TRP   B 1 149 ? 38.806  -3.175  7.154   1   31.72 ? 134 TRP   B O   1 
ATOM   3964 C  CB  . TRP   B 1 149 ? 35.932  -4.443  8.285   1   32.07 ? 134 TRP   B CB  1 
ATOM   3965 C  CG  . TRP   B 1 149 ? 35.444  -3.331  7.392   1   33.54 ? 134 TRP   B CG  1 
ATOM   3966 C  CD1 . TRP   B 1 149 ? 34.971  -2.109  7.775   1   34.71 ? 134 TRP   B CD1 1 
ATOM   3967 C  CD2 . TRP   B 1 149 ? 35.355  -3.366  5.959   1   34.29 ? 134 TRP   B CD2 1 
ATOM   3968 N  NE1 . TRP   B 1 149 ? 34.594  -1.373  6.662   1   34.88 ? 134 TRP   B NE1 1 
ATOM   3969 C  CE2 . TRP   B 1 149 ? 34.785  -2.142  5.54    1   35.03 ? 134 TRP   B CE2 1 
ATOM   3970 C  CE3 . TRP   B 1 149 ? 35.632  -4.347  4.994   1   35.23 ? 134 TRP   B CE3 1 
ATOM   3971 C  CZ2 . TRP   B 1 149 ? 34.568  -1.848  4.194   1   36.07 ? 134 TRP   B CZ2 1 
ATOM   3972 C  CZ3 . TRP   B 1 149 ? 35.414  -4.052  3.662   1   36    ? 134 TRP   B CZ3 1 
ATOM   3973 C  CH2 . TRP   B 1 149 ? 34.881  -2.823  3.276   1   36.28 ? 134 TRP   B CH2 1 
ATOM   3974 N  N   . LYS   B 1 150 ? 38.433  -5.379  6.774   1   34.42 ? 135 LYS   B N   1 
ATOM   3975 C  CA  . LYS   B 1 150 ? 39.161  -5.465  5.523   1   36.4  ? 135 LYS   B CA  1 
ATOM   3976 C  C   . LYS   B 1 150 ? 38.671  -6.627  4.715   1   38.61 ? 135 LYS   B C   1 
ATOM   3977 O  O   . LYS   B 1 150 ? 38.141  -7.607  5.25    1   38.75 ? 135 LYS   B O   1 
ATOM   3978 C  CB  . LYS   B 1 150 ? 40.685  -5.608  5.775   1   38.38 ? 135 LYS   B CB  1 
ATOM   3979 C  CG  . LYS   B 1 150 ? 41.103  -6.92   6.459   1   41.41 ? 135 LYS   B CG  1 
ATOM   3980 C  CD  . LYS   B 1 150 ? 42.618  -6.999  6.637   1   44.6  ? 135 LYS   B CD  1 
ATOM   3981 N  N   . LYS   B 1 151 ? 38.868  -6.539  3.409   1   40.28 ? 136 LYS   B N   1 
ATOM   3982 C  CA  . LYS   B 1 151 ? 38.622  -7.665  2.512   1   41.72 ? 136 LYS   B CA  1 
ATOM   3983 C  C   . LYS   B 1 151 ? 39.97   -8.457  2.498   1   43.83 ? 136 LYS   B C   1 
ATOM   3984 O  O   . LYS   B 1 151 ? 41.041  -7.841  2.46    1   44.26 ? 136 LYS   B O   1 
ATOM   3985 C  CB  . LYS   B 1 151 ? 38.375  -7.142  1.083   1   42.08 ? 136 LYS   B CB  1 
ATOM   3986 C  CG  . LYS   B 1 151 ? 36.918  -6.893  0.704   1   44.33 ? 136 LYS   B CG  1 
ATOM   3987 C  CD  . LYS   B 1 151 ? 36.843  -6.48   -0.767  1   46.41 ? 136 LYS   B CD  1 
ATOM   3988 C  CE  . LYS   B 1 151 ? 35.442  -6.251  -1.272  1   48.71 ? 136 LYS   B CE  1 
ATOM   3989 N  NZ  . LYS   B 1 151 ? 35.367  -6.331  -2.757  1   50.81 ? 136 LYS   B NZ  1 
ATOM   3990 N  N   . LYS   B 1 152 ? 39.928  -9.796  2.501   1   45    ? 137 LYS   B N   1 
ATOM   3991 C  CA  . LYS   B 1 152 ? 41.144  -10.607 2.398   1   46.29 ? 137 LYS   B CA  1 
ATOM   3992 C  C   . LYS   B 1 152 ? 41.68   -10.418 0.966   1   48.46 ? 137 LYS   B C   1 
ATOM   3993 O  O   . LYS   B 1 152 ? 42.791  -9.934  0.789   1   48.81 ? 137 LYS   B O   1 
ATOM   3994 C  CB  . LYS   B 1 152 ? 40.861  -12.091 2.707   1   46.93 ? 137 LYS   B CB  1 
ATOM   3995 C  CG  . LYS   B 1 152 ? 40.718  -12.389 4.195   1   48.55 ? 137 LYS   B CG  1 
ATOM   3996 C  CD  . LYS   B 1 152 ? 40.1    -13.77  4.407   1   51.36 ? 137 LYS   B CD  1 
ATOM   3997 C  CE  . LYS   B 1 152 ? 39.965  -14.151 5.858   1   54.29 ? 137 LYS   B CE  1 
ATOM   3998 N  N   . ASP   B 1 153 ? 40.839  -10.667 -0.039  1   50.01 ? 138 ASP   B N   1 
ATOM   3999 C  CA  . ASP   B 1 153 ? 41.173  -10.475 -1.451  1   51.98 ? 138 ASP   B CA  1 
ATOM   4000 C  C   . ASP   B 1 153 ? 40.301  -9.327  -1.962  1   53.74 ? 138 ASP   B C   1 
ATOM   4001 O  O   . ASP   B 1 153 ? 39.08   -9.459  -1.992  1   53.65 ? 138 ASP   B O   1 
ATOM   4002 C  CB  . ASP   B 1 153 ? 40.851  -11.769 -2.243  1   53.91 ? 138 ASP   B CB  1 
ATOM   4003 C  CG  . ASP   B 1 153 ? 41.202  -11.768 -3.731  1   57.99 ? 138 ASP   B CG  1 
ATOM   4004 O  OD1 . ASP   B 1 153 ? 41.463  -10.673 -4.285  1   58.52 ? 138 ASP   B OD1 1 
ATOM   4005 O  OD2 . ASP   B 1 153 ? 41.2    -12.864 -4.345  1   59.84 ? 138 ASP   B OD2 1 
ATOM   4006 N  N   . PRO   B 1 154 ? 40.909  -8.219  -2.409  1   55.17 ? 139 PRO   B N   1 
ATOM   4007 C  CA  . PRO   B 1 154 ? 40.109  -7.09   -2.921  1   56.07 ? 139 PRO   B CA  1 
ATOM   4008 C  C   . PRO   B 1 154 ? 39.324  -7.383  -4.204  1   56.83 ? 139 PRO   B C   1 
ATOM   4009 O  O   . PRO   B 1 154 ? 38.38   -6.654  -4.528  1   57.19 ? 139 PRO   B O   1 
ATOM   4010 C  CB  . PRO   B 1 154 ? 41.148  -5.976  -3.129  1   56.67 ? 139 PRO   B CB  1 
ATOM   4011 C  CG  . PRO   B 1 154 ? 42.358  -6.417  -2.378  1   57.06 ? 139 PRO   B CG  1 
ATOM   4012 C  CD  . PRO   B 1 154 ? 42.346  -7.911  -2.441  1   55.18 ? 139 PRO   B CD  1 
ATOM   4013 N  N   . ASN   B 1 155 ? 39.687  -8.452  -4.922  1   56.75 ? 140 ASN   B N   1 
ATOM   4014 C  CA  . ASN   B 1 155 ? 38.965  -8.836  -6.134  1   57.43 ? 140 ASN   B CA  1 
ATOM   4015 C  C   . ASN   B 1 155 ? 37.776  -9.772  -5.871  1   57.06 ? 140 ASN   B C   1 
ATOM   4016 O  O   . ASN   B 1 155 ? 37.101  -10.175 -6.816  1   57.73 ? 140 ASN   B O   1 
ATOM   4017 C  CB  . ASN   B 1 155 ? 39.917  -9.451  -7.154  1   59.76 ? 140 ASN   B CB  1 
ATOM   4018 C  CG  . ASN   B 1 155 ? 41.059  -8.533  -7.474  1   64.87 ? 140 ASN   B CG  1 
ATOM   4019 O  OD1 . ASN   B 1 155 ? 40.86   -7.428  -7.992  1   67.13 ? 140 ASN   B OD1 1 
ATOM   4020 N  ND2 . ASN   B 1 155 ? 42.273  -8.956  -7.133  1   65.67 ? 140 ASN   B ND2 1 
ATOM   4021 N  N   . LYS   B 1 156 ? 37.511  -10.12  -4.602  1   55.78 ? 141 LYS   B N   1 
ATOM   4022 C  CA  . LYS   B 1 156 ? 36.391  -10.985 -4.253  1   54.92 ? 141 LYS   B CA  1 
ATOM   4023 C  C   . LYS   B 1 156 ? 35.276  -10.188 -3.522  1   53.21 ? 141 LYS   B C   1 
ATOM   4024 O  O   . LYS   B 1 156 ? 35.536  -9.105  -2.984  1   53.07 ? 141 LYS   B O   1 
ATOM   4025 C  CB  . LYS   B 1 156 ? 36.894  -12.201 -3.462  1   57.15 ? 141 LYS   B CB  1 
ATOM   4026 C  CG  . LYS   B 1 156 ? 37.835  -13.075 -4.278  1   60.69 ? 141 LYS   B CG  1 
ATOM   4027 C  CD  . LYS   B 1 156 ? 38.102  -14.392 -3.585  1   64.8  ? 141 LYS   B CD  1 
ATOM   4028 N  N   . PRO   B 1 157 ? 34.023  -10.678 -3.536  1   51.87 ? 142 PRO   B N   1 
ATOM   4029 C  CA  . PRO   B 1 157 ? 32.922  -9.913  -2.931  1   50.88 ? 142 PRO   B CA  1 
ATOM   4030 C  C   . PRO   B 1 157 ? 32.951  -9.743  -1.405  1   49.61 ? 142 PRO   B C   1 
ATOM   4031 O  O   . PRO   B 1 157 ? 33.775  -10.337 -0.705  1   49.71 ? 142 PRO   B O   1 
ATOM   4032 C  CB  . PRO   B 1 157 ? 31.683  -10.69  -3.383  1   51.94 ? 142 PRO   B CB  1 
ATOM   4033 C  CG  . PRO   B 1 157 ? 32.163  -12.081 -3.57   1   52.66 ? 142 PRO   B CG  1 
ATOM   4034 C  CD  . PRO   B 1 157 ? 33.524  -11.914 -4.169  1   51.34 ? 142 PRO   B CD  1 
ATOM   4035 N  N   . LEU   B 1 158 ? 32.041  -8.899  -0.884  1   47.9  ? 143 LEU   B N   1 
ATOM   4036 C  CA  . LEU   B 1 158 ? 31.942  -8.653  0.544   1   46.48 ? 143 LEU   B CA  1 
ATOM   4037 C  C   . LEU   B 1 158 ? 31.224  -9.8    1.229   1   45.72 ? 143 LEU   B C   1 
ATOM   4038 O  O   . LEU   B 1 158 ? 30.057  -9.694  1.577   1   45.96 ? 143 LEU   B O   1 
ATOM   4039 C  CB  . LEU   B 1 158 ? 31.218  -7.337  0.804   1   45.89 ? 143 LEU   B CB  1 
ATOM   4040 C  CG  . LEU   B 1 158 ? 32.002  -6.107  0.411   1   46.85 ? 143 LEU   B CG  1 
ATOM   4041 C  CD1 . LEU   B 1 158 ? 31.076  -4.941  0.176   1   47.36 ? 143 LEU   B CD1 1 
ATOM   4042 C  CD2 . LEU   B 1 158 ? 33.067  -5.773  1.458   1   46.91 ? 143 LEU   B CD2 1 
ATOM   4043 N  N   . THR   B 1 159 ? 31.924  -10.897 1.427   1   44.75 ? 144 THR   B N   1 
ATOM   4044 C  CA  . THR   B 1 159 ? 31.371  -12.064 2.094   1   44.55 ? 144 THR   B CA  1 
ATOM   4045 C  C   . THR   B 1 159 ? 32.218  -12.357 3.336   1   43.6  ? 144 THR   B C   1 
ATOM   4046 O  O   . THR   B 1 159 ? 33.396  -11.994 3.389   1   43.72 ? 144 THR   B O   1 
ATOM   4047 C  CB  . THR   B 1 159 ? 31.324  -13.22  1.104   1   47.13 ? 144 THR   B CB  1 
ATOM   4048 O  OG1 . THR   B 1 159 ? 30.747  -14.365 1.722   1   49.93 ? 144 THR   B OG1 1 
ATOM   4049 C  CG2 . THR   B 1 159 ? 32.686  -13.554 0.562   1   47.48 ? 144 THR   B CG2 1 
ATOM   4050 N  N   . TYR   B 1 160 ? 31.639  -13.02  4.34    1   42.72 ? 145 TYR   B N   1 
ATOM   4051 C  CA  . TYR   B 1 160 ? 32.342  -13.356 5.584   1   42.4  ? 145 TYR   B CA  1 
ATOM   4052 C  C   . TYR   B 1 160 ? 33.673  -14.086 5.317   1   43.16 ? 145 TYR   B C   1 
ATOM   4053 O  O   . TYR   B 1 160 ? 34.7    -13.718 5.889   1   42.82 ? 145 TYR   B O   1 
ATOM   4054 C  CB  . TYR   B 1 160 ? 31.446  -14.206 6.505   1   41.4  ? 145 TYR   B CB  1 
ATOM   4055 C  CG  . TYR   B 1 160 ? 32.022  -14.388 7.892   1   41.05 ? 145 TYR   B CG  1 
ATOM   4056 C  CD1 . TYR   B 1 160 ? 32.882  -15.445 8.18    1   41.04 ? 145 TYR   B CD1 1 
ATOM   4057 C  CD2 . TYR   B 1 160 ? 31.714  -13.503 8.913   1   41.44 ? 145 TYR   B CD2 1 
ATOM   4058 C  CE1 . TYR   B 1 160 ? 33.464  -15.582 9.435   1   41.14 ? 145 TYR   B CE1 1 
ATOM   4059 C  CE2 . TYR   B 1 160 ? 32.255  -13.651 10.183  1   41.82 ? 145 TYR   B CE2 1 
ATOM   4060 C  CZ  . TYR   B 1 160 ? 33.133  -14.694 10.444  1   41.86 ? 145 TYR   B CZ  1 
ATOM   4061 O  OH  . TYR   B 1 160 ? 33.665  -14.841 11.705  1   41.44 ? 145 TYR   B OH  1 
ATOM   4062 N  N   . GLU   B 1 161 ? 33.656  -15.07  4.395   1   43.39 ? 146 GLU   B N   1 
ATOM   4063 C  CA  . GLU   B 1 161 ? 34.865  -15.832 4.044   1   43.94 ? 146 GLU   B CA  1 
ATOM   4064 C  C   . GLU   B 1 161 ? 35.97   -14.96  3.482   1   42.91 ? 146 GLU   B C   1 
ATOM   4065 O  O   . GLU   B 1 161 ? 37.143  -15.256 3.698   1   43.9  ? 146 GLU   B O   1 
ATOM   4066 C  CB  . GLU   B 1 161 ? 34.542  -17.002 3.108   1   48.24 ? 146 GLU   B CB  1 
ATOM   4067 C  CG  . GLU   B 1 161 ? 33.713  -18.083 3.787   1   58.84 ? 146 GLU   B CG  1 
ATOM   4068 C  CD  . GLU   B 1 161 ? 32.271  -17.69  4.081   1   71.84 ? 146 GLU   B CD  1 
ATOM   4069 O  OE1 . GLU   B 1 161 ? 31.658  -17.012 3.223   1   74.08 ? 146 GLU   B OE1 1 
ATOM   4070 O  OE2 . GLU   B 1 161 ? 31.759  -18.043 5.172   1   75.19 ? 146 GLU   B OE2 1 
ATOM   4071 N  N   . ASN   B 1 162 ? 35.618  -13.871 2.803   1   41.16 ? 147 ASN   B N   1 
ATOM   4072 C  CA  . ASN   B 1 162 ? 36.598  -12.963 2.23    1   40.15 ? 147 ASN   B CA  1 
ATOM   4073 C  C   . ASN   B 1 162 ? 36.839  -11.737 3.089   1   38.82 ? 147 ASN   B C   1 
ATOM   4074 O  O   . ASN   B 1 162 ? 37.274  -10.715 2.558   1   38.34 ? 147 ASN   B O   1 
ATOM   4075 C  CB  . ASN   B 1 162 ? 36.171  -12.532 0.822   1   41.42 ? 147 ASN   B CB  1 
ATOM   4076 C  CG  . ASN   B 1 162 ? 37.264  -11.808 0.104   1   44.31 ? 147 ASN   B CG  1 
ATOM   4077 O  OD1 . ASN   B 1 162 ? 38.407  -12.259 0.087   1   46.13 ? 147 ASN   B OD1 1 
ATOM   4078 N  ND2 . ASN   B 1 162 ? 36.961  -10.625 -0.407  1   44.33 ? 147 ASN   B ND2 1 
ATOM   4079 N  N   . MET   B 1 163 ? 36.583  -11.807 4.407   1   38.17 ? 148 MET   B N   1 
ATOM   4080 C  CA  . MET   B 1 163 ? 36.739  -10.62  5.249   1   37.69 ? 148 MET   B CA  1 
ATOM   4081 C  C   . MET   B 1 163 ? 37.388  -10.891 6.567   1   37.24 ? 148 MET   B C   1 
ATOM   4082 O  O   . MET   B 1 163 ? 37.358  -12.02  7.048   1   37.3  ? 148 MET   B O   1 
ATOM   4083 C  CB  . MET   B 1 163 ? 35.348  -9.95   5.47    1   38.52 ? 148 MET   B CB  1 
ATOM   4084 C  CG  . MET   B 1 163 ? 34.804  -9.238  4.219   1   40.7  ? 148 MET   B CG  1 
ATOM   4085 S  SD  . MET   B 1 163 ? 33.047  -8.835  4.348   1   42.59 ? 148 MET   B SD  1 
ATOM   4086 C  CE  . MET   B 1 163 ? 33.181  -7.233  5.001   1   37.65 ? 148 MET   B CE  1 
ATOM   4087 N  N   . ASP   B 1 164 ? 37.918  -9.84   7.193   1   36.67 ? 149 ASP   B N   1 
ATOM   4088 C  CA  . ASP   B 1 164 ? 38.465  -9.953  8.528   1   37.29 ? 149 ASP   B CA  1 
ATOM   4089 C  C   . ASP   B 1 164 ? 38.357  -8.614  9.278   1   36.86 ? 149 ASP   B C   1 
ATOM   4090 O  O   . ASP   B 1 164 ? 38.239  -7.548  8.659   1   36.9  ? 149 ASP   B O   1 
ATOM   4091 C  CB  . ASP   B 1 164 ? 39.939  -10.411 8.468   1   40.47 ? 149 ASP   B CB  1 
ATOM   4092 C  CG  . ASP   B 1 164 ? 40.28   -11.412 9.569   1   48.88 ? 149 ASP   B CG  1 
ATOM   4093 O  OD1 . ASP   B 1 164 ? 39.885  -11.168 10.754  1   49.21 ? 149 ASP   B OD1 1 
ATOM   4094 O  OD2 . ASP   B 1 164 ? 40.92   -12.451 9.254   1   53.12 ? 149 ASP   B OD2 1 
ATOM   4095 N  N   . VAL   B 1 165 ? 38.452  -8.658  10.606  1   36.09 ? 150 VAL   B N   1 
ATOM   4096 C  CA  . VAL   B 1 165 ? 38.51   -7.435  11.412  1   35.96 ? 150 VAL   B CA  1 
ATOM   4097 C  C   . VAL   B 1 165 ? 39.988  -6.981  11.473  1   35.99 ? 150 VAL   B C   1 
ATOM   4098 O  O   . VAL   B 1 165 ? 40.889  -7.74   11.089  1   36.59 ? 150 VAL   B O   1 
ATOM   4099 C  CB  . VAL   B 1 165 ? 37.964  -7.659  12.846  1   36.43 ? 150 VAL   B CB  1 
ATOM   4100 C  CG1 . VAL   B 1 165 ? 36.452  -7.785  12.848  1   37.22 ? 150 VAL   B CG1 1 
ATOM   4101 C  CG2 . VAL   B 1 165 ? 38.629  -8.869  13.499  1   36.63 ? 150 VAL   B CG2 1 
ATOM   4102 N  N   . LEU   B 1 166 ? 40.24   -5.76   11.951  1   35.01 ? 151 LEU   B N   1 
ATOM   4103 C  CA  . LEU   B 1 166 ? 41.606  -5.282  12.101  1   35.17 ? 151 LEU   B CA  1 
ATOM   4104 C  C   . LEU   B 1 166 ? 42.141  -5.537  13.498  1   36.14 ? 151 LEU   B C   1 
ATOM   4105 O  O   . LEU   B 1 166 ? 43.326  -5.842  13.649  1   35.62 ? 151 LEU   B O   1 
ATOM   4106 C  CB  . LEU   B 1 166 ? 41.736  -3.81   11.735  1   35.2  ? 151 LEU   B CB  1 
ATOM   4107 C  CG  . LEU   B 1 166 ? 41.228  -3.441  10.335  1   37.13 ? 151 LEU   B CG  1 
ATOM   4108 C  CD1 . LEU   B 1 166 ? 41.442  -1.952  10.062  1   37.4  ? 151 LEU   B CD1 1 
ATOM   4109 C  CD2 . LEU   B 1 166 ? 41.875  -4.334  9.244   1   37.29 ? 151 LEU   B CD2 1 
ATOM   4110 N  N   . PHE   B 1 167 ? 41.278  -5.444  14.517  1   36.74 ? 152 PHE   B N   1 
ATOM   4111 C  CA  . PHE   B 1 167 ? 41.715  -5.642  15.886  1   37.61 ? 152 PHE   B CA  1 
ATOM   4112 C  C   . PHE   B 1 167 ? 40.742  -6.495  16.686  1   38.06 ? 152 PHE   B C   1 
ATOM   4113 O  O   . PHE   B 1 167 ? 39.52   -6.406  16.524  1   38.47 ? 152 PHE   B O   1 
ATOM   4114 C  CB  . PHE   B 1 167 ? 41.917  -4.291  16.579  1   38.66 ? 152 PHE   B CB  1 
ATOM   4115 C  CG  . PHE   B 1 167 ? 42.835  -3.348  15.835  1   41.06 ? 152 PHE   B CG  1 
ATOM   4116 C  CD1 . PHE   B 1 167 ? 44.221  -3.486  15.917  1   42.87 ? 152 PHE   B CD1 1 
ATOM   4117 C  CD2 . PHE   B 1 167 ? 42.321  -2.366  15.004  1   42.02 ? 152 PHE   B CD2 1 
ATOM   4118 C  CE1 . PHE   B 1 167 ? 45.066  -2.651  15.182  1   43.79 ? 152 PHE   B CE1 1 
ATOM   4119 C  CE2 . PHE   B 1 167 ? 43.168  -1.513  14.293  1   43.28 ? 152 PHE   B CE2 1 
ATOM   4120 C  CZ  . PHE   B 1 167 ? 44.534  -1.656  14.389  1   43.49 ? 152 PHE   B CZ  1 
ATOM   4121 N  N   . SER   B 1 168 ? 41.297  -7.32   17.557  1   36.78 ? 153 SER   B N   1 
ATOM   4122 C  CA  . SER   B 1 168 ? 40.576  -8.151  18.5    1   36.39 ? 153 SER   B CA  1 
ATOM   4123 C  C   . SER   B 1 168 ? 41.127  -7.807  19.898  1   35.97 ? 153 SER   B C   1 
ATOM   4124 O  O   . SER   B 1 168 ? 42.166  -7.127  20      1   36.61 ? 153 SER   B O   1 
ATOM   4125 C  CB  . SER   B 1 168 ? 40.837  -9.623  18.197  1   38.2  ? 153 SER   B CB  1 
ATOM   4126 O  OG  . SER   B 1 168 ? 40.057  -10.039 17.085  1   40.16 ? 153 SER   B OG  1 
ATOM   4127 N  N   . PHE   B 1 169 ? 40.477  -8.294  20.967  1   34.63 ? 154 PHE   B N   1 
ATOM   4128 C  CA  . PHE   B 1 169 ? 40.972  -8.026  22.312  1   34.55 ? 154 PHE   B CA  1 
ATOM   4129 C  C   . PHE   B 1 169 ? 41.724  -9.256  22.858  1   35.4  ? 154 PHE   B C   1 
ATOM   4130 O  O   . PHE   B 1 169 ? 42.824  -9.131  23.4    1   35.34 ? 154 PHE   B O   1 
ATOM   4131 C  CB  . PHE   B 1 169 ? 39.827  -7.636  23.252  1   33.65 ? 154 PHE   B CB  1 
ATOM   4132 C  CG  . PHE   B 1 169 ? 39.189  -6.32   22.898  1   34.21 ? 154 PHE   B CG  1 
ATOM   4133 C  CD1 . PHE   B 1 169 ? 39.753  -5.13   23.307  1   34.51 ? 154 PHE   B CD1 1 
ATOM   4134 C  CD2 . PHE   B 1 169 ? 38.015  -6.276  22.168  1   35.06 ? 154 PHE   B CD2 1 
ATOM   4135 C  CE1 . PHE   B 1 169 ? 39.172  -3.92   22.972  1   35.61 ? 154 PHE   B CE1 1 
ATOM   4136 C  CE2 . PHE   B 1 169 ? 37.436  -5.056  21.828  1   35.94 ? 154 PHE   B CE2 1 
ATOM   4137 C  CZ  . PHE   B 1 169 ? 38.009  -3.889  22.244  1   35.55 ? 154 PHE   B CZ  1 
ATOM   4138 N  N   . ARG   B 1 170 ? 41.111  -10.43  22.73   1   34.75 ? 155 ARG   B N   1 
ATOM   4139 C  CA  . ARG   B 1 170 ? 41.651  -11.65  23.27   1   35.38 ? 155 ARG   B CA  1 
ATOM   4140 C  C   . ARG   B 1 170 ? 41.439  -12.789 22.301  1   37.07 ? 155 ARG   B C   1 
ATOM   4141 O  O   . ARG   B 1 170 ? 40.486  -12.788 21.503  1   37.22 ? 155 ARG   B O   1 
ATOM   4142 C  CB  . ARG   B 1 170 ? 40.928  -12.017 24.588  1   34.74 ? 155 ARG   B CB  1 
ATOM   4143 C  CG  . ARG   B 1 170 ? 40.937  -10.927 25.654  1   36.81 ? 155 ARG   B CG  1 
ATOM   4144 C  CD  . ARG   B 1 170 ? 42.331  -10.688 26.211  1   38.11 ? 155 ARG   B CD  1 
ATOM   4145 N  NE  . ARG   B 1 170 ? 42.892  -11.932 26.751  1   36.93 ? 155 ARG   B NE  1 
ATOM   4146 C  CZ  . ARG   B 1 170 ? 42.778  -12.316 28.014  1   36.55 ? 155 ARG   B CZ  1 
ATOM   4147 N  NH1 . ARG   B 1 170 ? 42.212  -11.515 28.91   1   36.19 ? 155 ARG   B NH1 1 
ATOM   4148 N  NH2 . ARG   B 1 170 ? 43.285  -13.477 28.407  1   34.96 ? 155 ARG   B NH2 1 
ATOM   4149 N  N   . ASP   B 1 171 ? 42.281  -13.825 22.421  1   37.59 ? 156 ASP   B N   1 
ATOM   4150 C  CA  . ASP   B 1 171 ? 42.108  -15.025 21.601  1   38.48 ? 156 ASP   B CA  1 
ATOM   4151 C  C   . ASP   B 1 171 ? 40.829  -15.718 22.044  1   37.33 ? 156 ASP   B C   1 
ATOM   4152 O  O   . ASP   B 1 171 ? 40.576  -15.85  23.24   1   37.41 ? 156 ASP   B O   1 
ATOM   4153 C  CB  . ASP   B 1 171 ? 43.332  -15.959 21.735  1   42.23 ? 156 ASP   B CB  1 
ATOM   4154 C  CG  . ASP   B 1 171 ? 44.569  -15.371 21.076  1   50.26 ? 156 ASP   B CG  1 
ATOM   4155 O  OD1 . ASP   B 1 171 ? 44.419  -14.671 20.041  1   51.38 ? 156 ASP   B OD1 1 
ATOM   4156 O  OD2 . ASP   B 1 171 ? 45.686  -15.595 21.597  1   54.15 ? 156 ASP   B OD2 1 
ATOM   4157 N  N   . GLY   B 1 172 ? 40.002  -16.088 21.085  1   36.47 ? 157 GLY   B N   1 
ATOM   4158 C  CA  . GLY   B 1 172 ? 38.729  -16.733 21.384  1   36.3  ? 157 GLY   B CA  1 
ATOM   4159 C  C   . GLY   B 1 172 ? 37.617  -15.795 21.841  1   35.63 ? 157 GLY   B C   1 
ATOM   4160 O  O   . GLY   B 1 172 ? 36.592  -16.265 22.327  1   36.23 ? 157 GLY   B O   1 
ATOM   4161 N  N   . ASP   B 1 173 ? 37.784  -14.467 21.668  1   33.48 ? 158 ASP   B N   1 
ATOM   4162 C  CA  . ASP   B 1 173 ? 36.749  -13.522 22.072  1   32.05 ? 158 ASP   B CA  1 
ATOM   4163 C  C   . ASP   B 1 173 ? 35.572  -13.413 21.06   1   32.84 ? 158 ASP   B C   1 
ATOM   4164 O  O   . ASP   B 1 173 ? 34.586  -12.768 21.378  1   33.5  ? 158 ASP   B O   1 
ATOM   4165 C  CB  . ASP   B 1 173 ? 37.359  -12.131 22.393  1   30.71 ? 158 ASP   B CB  1 
ATOM   4166 C  CG  . ASP   B 1 173 ? 37.885  -11.356 21.207  1   31.3  ? 158 ASP   B CG  1 
ATOM   4167 O  OD1 . ASP   B 1 173 ? 37.796  -11.871 20.076  1   31.52 ? 158 ASP   B OD1 1 
ATOM   4168 O  OD2 . ASP   B 1 173 ? 38.409  -10.228 21.413  1   32.16 ? 158 ASP   B OD2 1 
ATOM   4169 N  N   . CYS   B 1 174 ? 35.699  -13.97  19.84   1   32.63 ? 159 CYS   B N   1 
ATOM   4170 C  CA  . CYS   B 1 174 ? 34.648  -13.929 18.813  1   33.44 ? 159 CYS   B CA  1 
ATOM   4171 C  C   . CYS   B 1 174 ? 34.37   -12.537 18.257  1   33.86 ? 159 CYS   B C   1 
ATOM   4172 O  O   . CYS   B 1 174 ? 33.31   -12.328 17.653  1   32.71 ? 159 CYS   B O   1 
ATOM   4173 C  CB  . CYS   B 1 174 ? 33.361  -14.586 19.298  1   33.83 ? 159 CYS   B CB  1 
ATOM   4174 S  SG  . CYS   B 1 174 ? 33.521  -16.354 19.622  1   38.22 ? 159 CYS   B SG  1 
ATOM   4175 N  N   . SER   B 1 175 ? 35.305  -11.596 18.447  1   34.5  ? 160 SER   B N   1 
ATOM   4176 C  CA  . SER   B 1 175 ? 35.176  -10.247 17.924  1   35.33 ? 160 SER   B CA  1 
ATOM   4177 C  C   . SER   B 1 175 ? 35.092  -10.244 16.418  1   34.99 ? 160 SER   B C   1 
ATOM   4178 O  O   . SER   B 1 175 ? 34.369  -9.418  15.882  1   35.4  ? 160 SER   B O   1 
ATOM   4179 C  CB  . SER   B 1 175 ? 36.308  -9.341  18.402  1   37.89 ? 160 SER   B CB  1 
ATOM   4180 O  OG  . SER   B 1 175 ? 37.572  -9.973  18.281  1   40.98 ? 160 SER   B OG  1 
ATOM   4181 N  N   . LYS   B 1 176 ? 35.727  -11.208 15.726  1   33.95 ? 161 LYS   B N   1 
ATOM   4182 C  CA  . LYS   B 1 176 ? 35.621  -11.268 14.269  1   34.54 ? 161 LYS   B CA  1 
ATOM   4183 C  C   . LYS   B 1 176 ? 34.176  -11.563 13.876  1   34.54 ? 161 LYS   B C   1 
ATOM   4184 O  O   . LYS   B 1 176 ? 33.615  -10.847 13.062  1   35.2  ? 161 LYS   B O   1 
ATOM   4185 C  CB  . LYS   B 1 176 ? 36.553  -12.33  13.657  1   37.17 ? 161 LYS   B CB  1 
ATOM   4186 C  CG  . LYS   B 1 176 ? 36.481  -12.336 12.135  1   41.18 ? 161 LYS   B CG  1 
ATOM   4187 C  CD  . LYS   B 1 176 ? 37.234  -13.508 11.517  1   46.54 ? 161 LYS   B CD  1 
ATOM   4188 C  CE  . LYS   B 1 176 ? 37.047  -13.536 10.018  1   50.75 ? 161 LYS   B CE  1 
ATOM   4189 N  NZ  . LYS   B 1 176 ? 37.666  -14.742 9.391   1   53.67 ? 161 LYS   B NZ  1 
ATOM   4190 N  N   . GLY   B 1 177 ? 33.577  -12.577 14.497  1   33.86 ? 162 GLY   B N   1 
ATOM   4191 C  CA  . GLY   B 1 177 ? 32.209  -12.977 14.199  1   33.62 ? 162 GLY   B CA  1 
ATOM   4192 C  C   . GLY   B 1 177 ? 31.225  -11.873 14.525  1   33.15 ? 162 GLY   B C   1 
ATOM   4193 O  O   . GLY   B 1 177 ? 30.414  -11.504 13.695  1   33.55 ? 162 GLY   B O   1 
ATOM   4194 N  N   . PHE   B 1 178 ? 31.34   -11.288 15.71   1   32.07 ? 163 PHE   B N   1 
ATOM   4195 C  CA  . PHE   B 1 178 ? 30.437  -10.243 16.154  1   31.32 ? 163 PHE   B CA  1 
ATOM   4196 C  C   . PHE   B 1 178 ? 30.532  -8.949  15.339  1   29.66 ? 163 PHE   B C   1 
ATOM   4197 O  O   . PHE   B 1 178 ? 29.502  -8.435  14.877  1   28.62 ? 163 PHE   B O   1 
ATOM   4198 C  CB  . PHE   B 1 178 ? 30.659  -9.997  17.639  1   31.17 ? 163 PHE   B CB  1 
ATOM   4199 C  CG  . PHE   B 1 178 ? 29.755  -8.992  18.283  1   31.7  ? 163 PHE   B CG  1 
ATOM   4200 C  CD1 . PHE   B 1 178 ? 28.399  -9.239  18.406  1   32.13 ? 163 PHE   B CD1 1 
ATOM   4201 C  CD2 . PHE   B 1 178 ? 30.271  -7.84   18.852  1   31.8  ? 163 PHE   B CD2 1 
ATOM   4202 C  CE1 . PHE   B 1 178 ? 27.564  -8.322  19.021  1   32.61 ? 163 PHE   B CE1 1 
ATOM   4203 C  CE2 . PHE   B 1 178 ? 29.443  -6.939  19.497  1   32.18 ? 163 PHE   B CE2 1 
ATOM   4204 C  CZ  . PHE   B 1 178 ? 28.094  -7.186  19.573  1   32.14 ? 163 PHE   B CZ  1 
ATOM   4205 N  N   . PHE   B 1 179 ? 31.739  -8.427  15.158  1   28.63 ? 164 PHE   B N   1 
ATOM   4206 C  CA  . PHE   B 1 179 ? 31.921  -7.175  14.43   1   28.73 ? 164 PHE   B CA  1 
ATOM   4207 C  C   . PHE   B 1 179 ? 31.614  -7.362  12.968  1   28.74 ? 164 PHE   B C   1 
ATOM   4208 O  O   . PHE   B 1 179 ? 30.989  -6.48   12.368  1   28.97 ? 164 PHE   B O   1 
ATOM   4209 C  CB  . PHE   B 1 179 ? 33.329  -6.588  14.623  1   29.12 ? 164 PHE   B CB  1 
ATOM   4210 C  CG  . PHE   B 1 179 ? 33.662  -6.194  16.047  1   29.64 ? 164 PHE   B CG  1 
ATOM   4211 C  CD1 . PHE   B 1 179 ? 32.687  -5.693  16.894  1   29.36 ? 164 PHE   B CD1 1 
ATOM   4212 C  CD2 . PHE   B 1 179 ? 34.956  -6.309  16.532  1   30.28 ? 164 PHE   B CD2 1 
ATOM   4213 C  CE1 . PHE   B 1 179 ? 33      -5.317  18.203  1   29.88 ? 164 PHE   B CE1 1 
ATOM   4214 C  CE2 . PHE   B 1 179 ? 35.268  -5.923  17.842  1   30.81 ? 164 PHE   B CE2 1 
ATOM   4215 C  CZ  . PHE   B 1 179 ? 34.284  -5.443  18.668  1   30.23 ? 164 PHE   B CZ  1 
ATOM   4216 N  N   . LEU   B 1 180 ? 32.013  -8.512  12.385  1   28.27 ? 165 LEU   B N   1 
ATOM   4217 C  CA  . LEU   B 1 180 ? 31.785  -8.723  10.95   1   29.37 ? 165 LEU   B CA  1 
ATOM   4218 C  C   . LEU   B 1 180 ? 30.327  -8.98   10.609  1   30.84 ? 165 LEU   B C   1 
ATOM   4219 O  O   . LEU   B 1 180 ? 29.9    -8.581  9.521   1   31.92 ? 165 LEU   B O   1 
ATOM   4220 C  CB  . LEU   B 1 180 ? 32.64   -9.865  10.369  1   29.61 ? 165 LEU   B CB  1 
ATOM   4221 C  CG  . LEU   B 1 180 ? 34.125  -9.61   10.033  1   30.9  ? 165 LEU   B CG  1 
ATOM   4222 C  CD1 . LEU   B 1 180 ? 34.612  -10.625 9.016   1   31.94 ? 165 LEU   B CD1 1 
ATOM   4223 C  CD2 . LEU   B 1 180 ? 34.396  -8.18   9.491   1   31.56 ? 165 LEU   B CD2 1 
ATOM   4224 N  N   . VAL   B 1 181 ? 29.593  -9.725  11.451  1   29.73 ? 166 VAL   B N   1 
ATOM   4225 C  CA  . VAL   B 1 181 ? 28.183  -9.979  11.163  1   29.95 ? 166 VAL   B CA  1 
ATOM   4226 C  C   . VAL   B 1 181 ? 27.392  -8.649  11.288  1   30.83 ? 166 VAL   B C   1 
ATOM   4227 O  O   . VAL   B 1 181 ? 26.554  -8.369  10.433  1   32.21 ? 166 VAL   B O   1 
ATOM   4228 C  CB  . VAL   B 1 181 ? 27.579  -11.168 11.944  1   29.73 ? 166 VAL   B CB  1 
ATOM   4229 C  CG1 . VAL   B 1 181 ? 26.075  -11.254 11.711  1   29.6  ? 166 VAL   B CG1 1 
ATOM   4230 C  CG2 . VAL   B 1 181 ? 28.268  -12.492 11.55   1   29.19 ? 166 VAL   B CG2 1 
ATOM   4231 N  N   . SER   B 1 182 ? 27.764  -7.769  12.231  1   30.37 ? 167 SER   B N   1 
ATOM   4232 C  CA  . SER   B 1 182 ? 27.149  -6.441  12.343  1   30.93 ? 167 SER   B CA  1 
ATOM   4233 C  C   . SER   B 1 182 ? 27.421  -5.636  11.08   1   30.73 ? 167 SER   B C   1 
ATOM   4234 O  O   . SER   B 1 182 ? 26.512  -5.017  10.524  1   30.27 ? 167 SER   B O   1 
ATOM   4235 C  CB  . SER   B 1 182 ? 27.694  -5.689  13.553  1   33.43 ? 167 SER   B CB  1 
ATOM   4236 O  OG  . SER   B 1 182 ? 27.265  -6.279  14.77   1   37.63 ? 167 SER   B OG  1 
ATOM   4237 N  N   . LEU   B 1 183 ? 28.673  -5.678  10.611  1   29.6  ? 168 LEU   B N   1 
ATOM   4238 C  CA  . LEU   B 1 183 ? 29.09   -5.001  9.398   1   29.99 ? 168 LEU   B CA  1 
ATOM   4239 C  C   . LEU   B 1 183 ? 28.342  -5.542  8.173   1   29.68 ? 168 LEU   B C   1 
ATOM   4240 O  O   . LEU   B 1 183 ? 27.928  -4.762  7.325   1   30.03 ? 168 LEU   B O   1 
ATOM   4241 C  CB  . LEU   B 1 183 ? 30.595  -5.197  9.216   1   30.7  ? 168 LEU   B CB  1 
ATOM   4242 C  CG  . LEU   B 1 183 ? 31.177  -4.561  7.978   1   33.34 ? 168 LEU   B CG  1 
ATOM   4243 C  CD1 . LEU   B 1 183 ? 31.115  -3.044  8.07    1   33.33 ? 168 LEU   B CD1 1 
ATOM   4244 C  CD2 . LEU   B 1 183 ? 32.585  -5.069  7.75    1   33.93 ? 168 LEU   B CD2 1 
ATOM   4245 N  N   . LEU   B 1 184 ? 28.172  -6.851  8.073   1   28.8  ? 169 LEU   B N   1 
ATOM   4246 C  CA  . LEU   B 1 184 ? 27.471  -7.461  6.94    1   30.37 ? 169 LEU   B CA  1 
ATOM   4247 C  C   . LEU   B 1 184 ? 25.987  -7.058  6.878   1   30.3  ? 169 LEU   B C   1 
ATOM   4248 O  O   . LEU   B 1 184 ? 25.427  -6.97   5.798   1   30.34 ? 169 LEU   B O   1 
ATOM   4249 C  CB  . LEU   B 1 184 ? 27.651  -8.98   6.959   1   31.27 ? 169 LEU   B CB  1 
ATOM   4250 C  CG  . LEU   B 1 184 ? 29.077  -9.422  6.507   1   34.19 ? 169 LEU   B CG  1 
ATOM   4251 C  CD1 . LEU   B 1 184 ? 29.345  -10.852 6.899   1   35.68 ? 169 LEU   B CD1 1 
ATOM   4252 C  CD2 . LEU   B 1 184 ? 29.274  -9.217  4.996   1   34    ? 169 LEU   B CD2 1 
ATOM   4253 N  N   . VAL   B 1 185 ? 25.363  -6.803  8.027   1   30.04 ? 170 VAL   B N   1 
ATOM   4254 C  CA  . VAL   B 1 185 ? 23.984  -6.311  8.075   1   31.16 ? 170 VAL   B CA  1 
ATOM   4255 C  C   . VAL   B 1 185 ? 23.977  -4.835  7.645   1   32.39 ? 170 VAL   B C   1 
ATOM   4256 O  O   . VAL   B 1 185 ? 23.126  -4.392  6.887   1   33.71 ? 170 VAL   B O   1 
ATOM   4257 C  CB  . VAL   B 1 185 ? 23.407  -6.478  9.489   1   31.22 ? 170 VAL   B CB  1 
ATOM   4258 C  CG1 . VAL   B 1 185 ? 22.066  -5.735  9.632   1   32.09 ? 170 VAL   B CG1 1 
ATOM   4259 C  CG2 . VAL   B 1 185 ? 23.256  -7.959  9.812   1   30.88 ? 170 VAL   B CG2 1 
ATOM   4260 N  N   . GLU   B 1 186 ? 24.953  -4.083  8.091   1   32.34 ? 171 GLU   B N   1 
ATOM   4261 C  CA  . GLU   B 1 186 ? 25.175  -2.694  7.743   1   33.15 ? 171 GLU   B CA  1 
ATOM   4262 C  C   . GLU   B 1 186 ? 25.315  -2.586  6.177   1   35.08 ? 171 GLU   B C   1 
ATOM   4263 O  O   . GLU   B 1 186 ? 24.685  -1.72   5.549   1   35.71 ? 171 GLU   B O   1 
ATOM   4264 C  CB  . GLU   B 1 186 ? 26.461  -2.314  8.464   1   34.81 ? 171 GLU   B CB  1 
ATOM   4265 C  CG  . GLU   B 1 186 ? 26.688  -0.871  8.801   1   39.18 ? 171 GLU   B CG  1 
ATOM   4266 C  CD  . GLU   B 1 186 ? 25.742  -0.122  9.715   1   41.01 ? 171 GLU   B CD  1 
ATOM   4267 O  OE1 . GLU   B 1 186 ? 25.577  -0.481  10.904  1   35    ? 171 GLU   B OE1 1 
ATOM   4268 O  OE2 . GLU   B 1 186 ? 25.232  0.913   9.238   1   46.42 ? 171 GLU   B OE2 1 
ATOM   4269 N  N   . ILE   B 1 187 ? 26.01   -3.55   5.558   1   35.04 ? 172 ILE   B N   1 
ATOM   4270 C  CA  . ILE   B 1 187 ? 26.206  -3.609  4.105   1   35.65 ? 172 ILE   B CA  1 
ATOM   4271 C  C   . ILE   B 1 187 ? 24.913  -4.005  3.382   1   35.97 ? 172 ILE   B C   1 
ATOM   4272 O  O   . ILE   B 1 187 ? 24.572  -3.403  2.36    1   36.55 ? 172 ILE   B O   1 
ATOM   4273 C  CB  . ILE   B 1 187 ? 27.396  -4.541  3.767   1   36.24 ? 172 ILE   B CB  1 
ATOM   4274 C  CG1 . ILE   B 1 187 ? 28.72   -3.915  4.239   1   36.9  ? 172 ILE   B CG1 1 
ATOM   4275 C  CG2 . ILE   B 1 187 ? 27.448  -4.86   2.278   1   36.74 ? 172 ILE   B CG2 1 
ATOM   4276 C  CD1 . ILE   B 1 187 ? 29.887  -4.935  4.279   1   38.16 ? 172 ILE   B CD1 1 
ATOM   4277 N  N   . ALA   B 1 188 ? 24.19   -4.996  3.908   1   35.55 ? 173 ALA   B N   1 
ATOM   4278 C  CA  . ALA   B 1 188 ? 22.884  -5.407  3.371   1   36.02 ? 173 ALA   B CA  1 
ATOM   4279 C  C   . ALA   B 1 188 ? 21.902  -4.22   3.406   1   35.61 ? 173 ALA   B C   1 
ATOM   4280 O  O   . ALA   B 1 188 ? 21.16   -4.018  2.443   1   35.78 ? 173 ALA   B O   1 
ATOM   4281 C  CB  . ALA   B 1 188 ? 22.316  -6.565  4.17    1   35.8  ? 173 ALA   B CB  1 
ATOM   4282 N  N   . ALA   B 1 189 ? 21.973  -3.376  4.452   1   34.49 ? 174 ALA   B N   1 
ATOM   4283 C  CA  . ALA   B 1 189 ? 21.109  -2.199  4.534   1   34.52 ? 174 ALA   B CA  1 
ATOM   4284 C  C   . ALA   B 1 189 ? 21.416  -1.134  3.498   1   34.92 ? 174 ALA   B C   1 
ATOM   4285 O  O   . ALA   B 1 189 ? 20.544  -0.315  3.204   1   34.52 ? 174 ALA   B O   1 
ATOM   4286 C  CB  . ALA   B 1 189 ? 21.175  -1.572  5.908   1   33.93 ? 174 ALA   B CB  1 
ATOM   4287 N  N   . ALA   B 1 190 ? 22.642  -1.114  2.966   1   34.73 ? 175 ALA   B N   1 
ATOM   4288 C  CA  . ALA   B 1 190 ? 23.07   -0.094  2.008   1   35.01 ? 175 ALA   B CA  1 
ATOM   4289 C  C   . ALA   B 1 190 ? 22.198  -0.065  0.765   1   35.45 ? 175 ALA   B C   1 
ATOM   4290 O  O   . ALA   B 1 190 ? 22.007  1.007   0.201   1   35.11 ? 175 ALA   B O   1 
ATOM   4291 C  CB  . ALA   B 1 190 ? 24.508  -0.326  1.613   1   35.04 ? 175 ALA   B CB  1 
ATOM   4292 N  N   . SER   B 1 191 ? 21.709  -1.232  0.308   1   36.02 ? 176 SER   B N   1 
ATOM   4293 C  CA  . SER   B 1 191 ? 20.859  -1.259  -0.884  1   37.52 ? 176 SER   B CA  1 
ATOM   4294 C  C   . SER   B 1 191 ? 19.489  -0.605  -0.612  1   38.68 ? 176 SER   B C   1 
ATOM   4295 O  O   . SER   B 1 191 ? 18.849  -0.129  -1.55   1   39.58 ? 176 SER   B O   1 
ATOM   4296 C  CB  . SER   B 1 191 ? 20.715  -2.678  -1.423  1   39.38 ? 176 SER   B CB  1 
ATOM   4297 O  OG  . SER   B 1 191 ? 20.32   -3.575  -0.396  1   43.27 ? 176 SER   B OG  1 
ATOM   4298 N  N   . ALA   B 1 192 ? 19.061  -0.525  0.671   1   38.37 ? 177 ALA   B N   1 
ATOM   4299 C  CA  . ALA   B 1 192 ? 17.812  0.13    1.038   1   38.66 ? 177 ALA   B CA  1 
ATOM   4300 C  C   . ALA   B 1 192 ? 18.075  1.629   1.257   1   39.36 ? 177 ALA   B C   1 
ATOM   4301 O  O   . ALA   B 1 192 ? 17.27   2.456   0.829   1   38.99 ? 177 ALA   B O   1 
ATOM   4302 C  CB  . ALA   B 1 192 ? 17.233  -0.506  2.298   1   38.57 ? 177 ALA   B CB  1 
ATOM   4303 N  N   . ILE   B 1 193 ? 19.216  1.988   1.893   1   39.72 ? 178 ILE   B N   1 
ATOM   4304 C  CA  . ILE   B 1 193 ? 19.58   3.387   2.171   1   41.01 ? 178 ILE   B CA  1 
ATOM   4305 C  C   . ILE   B 1 193 ? 19.633  4.187   0.877   1   41.56 ? 178 ILE   B C   1 
ATOM   4306 O  O   . ILE   B 1 193 ? 19.196  5.338   0.85    1   42.28 ? 178 ILE   B O   1 
ATOM   4307 C  CB  . ILE   B 1 193 ? 20.977  3.53    2.849   1   42.22 ? 178 ILE   B CB  1 
ATOM   4308 C  CG1 . ILE   B 1 193 ? 21.235  2.467   3.942   1   44.53 ? 178 ILE   B CG1 1 
ATOM   4309 C  CG2 . ILE   B 1 193 ? 21.224  4.949   3.35    1   42.6  ? 178 ILE   B CG2 1 
ATOM   4310 C  CD1 . ILE   B 1 193 ? 20.714  2.654   5.218   1   46.86 ? 178 ILE   B CD1 1 
ATOM   4311 N  N   . LYS   B 1 194 ? 20.218  3.603   -0.182  1   41.02 ? 179 LYS   B N   1 
ATOM   4312 C  CA  . LYS   B 1 194 ? 20.391  4.33    -1.433  1   41.4  ? 179 LYS   B CA  1 
ATOM   4313 C  C   . LYS   B 1 194 ? 19.071  4.727   -2.113  1   41.29 ? 179 LYS   B C   1 
ATOM   4314 O  O   . LYS   B 1 194 ? 19.084  5.601   -2.987  1   41.72 ? 179 LYS   B O   1 
ATOM   4315 C  CB  . LYS   B 1 194 ? 21.311  3.569   -2.403  1   43.2  ? 179 LYS   B CB  1 
ATOM   4316 C  CG  . LYS   B 1 194 ? 20.722  2.304   -2.98   1   46.1  ? 179 LYS   B CG  1 
ATOM   4317 C  CD  . LYS   B 1 194 ? 21.722  1.618   -3.894  1   50.24 ? 179 LYS   B CD  1 
ATOM   4318 C  CE  . LYS   B 1 194 ? 21.217  0.29    -4.402  1   53.87 ? 179 LYS   B CE  1 
ATOM   4319 N  NZ  . LYS   B 1 194 ? 22.325  -0.556  -4.916  1   55.46 ? 179 LYS   B NZ  1 
ATOM   4320 N  N   . VAL   B 1 195 ? 17.953  4.098   -1.722  1   40.7  ? 180 VAL   B N   1 
ATOM   4321 C  CA  . VAL   B 1 195 ? 16.677  4.425   -2.33   1   40.63 ? 180 VAL   B CA  1 
ATOM   4322 C  C   . VAL   B 1 195 ? 15.989  5.592   -1.548  1   40.61 ? 180 VAL   B C   1 
ATOM   4323 O  O   . VAL   B 1 195 ? 15.088  6.219   -2.099  1   41.01 ? 180 VAL   B O   1 
ATOM   4324 C  CB  . VAL   B 1 195 ? 15.747  3.211   -2.657  1   41.59 ? 180 VAL   B CB  1 
ATOM   4325 C  CG1 . VAL   B 1 195 ? 16.221  1.869   -2.126  1   42.07 ? 180 VAL   B CG1 1 
ATOM   4326 C  CG2 . VAL   B 1 195 ? 14.258  3.46    -2.422  1   41.9  ? 180 VAL   B CG2 1 
ATOM   4327 N  N   . ILE   B 1 196 ? 16.494  5.983   -0.352  1   39.84 ? 181 ILE   B N   1 
ATOM   4328 C  CA  . ILE   B 1 196 ? 15.929  7.087   0.42    1   40.15 ? 181 ILE   B CA  1 
ATOM   4329 C  C   . ILE   B 1 196 ? 15.718  8.371   -0.433  1   41.6  ? 181 ILE   B C   1 
ATOM   4330 O  O   . ILE   B 1 196 ? 14.589  8.848   -0.466  1   42.19 ? 181 ILE   B O   1 
ATOM   4331 C  CB  . ILE   B 1 196 ? 16.711  7.349   1.729   1   39.48 ? 181 ILE   B CB  1 
ATOM   4332 C  CG1 . ILE   B 1 196 ? 16.457  6.203   2.734   1   39.82 ? 181 ILE   B CG1 1 
ATOM   4333 C  CG2 . ILE   B 1 196 ? 16.364  8.706   2.332   1   39.93 ? 181 ILE   B CG2 1 
ATOM   4334 C  CD1 . ILE   B 1 196 ? 17.25   6.296   4.023   1   40.16 ? 181 ILE   B CD1 1 
ATOM   4335 N  N   . PRO   B 1 197 ? 16.699  8.869   -1.221  1   41.93 ? 182 PRO   B N   1 
ATOM   4336 C  CA  . PRO   B 1 197 ? 16.426  10.068  -2.047  1   41.93 ? 182 PRO   B CA  1 
ATOM   4337 C  C   . PRO   B 1 197 ? 15.287  9.899   -3.071  1   41.62 ? 182 PRO   B C   1 
ATOM   4338 O  O   . PRO   B 1 197 ? 14.623  10.877  -3.391  1   41.65 ? 182 PRO   B O   1 
ATOM   4339 C  CB  . PRO   B 1 197 ? 17.767  10.351  -2.731  1   42.45 ? 182 PRO   B CB  1 
ATOM   4340 C  CG  . PRO   B 1 197 ? 18.571  9.109   -2.561  1   42.73 ? 182 PRO   B CG  1 
ATOM   4341 C  CD  . PRO   B 1 197 ? 18.112  8.454   -1.322  1   40.88 ? 182 PRO   B CD  1 
ATOM   4342 N  N   . THR   B 1 198 ? 15.08   8.678   -3.6    1   41.14 ? 183 THR   B N   1 
ATOM   4343 C  CA  . THR   B 1 198 ? 13.995  8.397   -4.544  1   41.35 ? 183 THR   B CA  1 
ATOM   4344 C  C   . THR   B 1 198 ? 12.64   8.589   -3.833  1   40.34 ? 183 THR   B C   1 
ATOM   4345 O  O   . THR   B 1 198 ? 11.71   9.109   -4.424  1   40.82 ? 183 THR   B O   1 
ATOM   4346 C  CB  . THR   B 1 198 ? 14.142  6.98    -5.113  1   43.56 ? 183 THR   B CB  1 
ATOM   4347 O  OG1 . THR   B 1 198 ? 15.373  6.901   -5.82   1   45.75 ? 183 THR   B OG1 1 
ATOM   4348 C  CG2 . THR   B 1 198 ? 12.996  6.587   -6.04   1   43.95 ? 183 THR   B CG2 1 
ATOM   4349 N  N   . VAL   B 1 199 ? 12.539  8.193   -2.565  1   38.81 ? 184 VAL   B N   1 
ATOM   4350 C  CA  . VAL   B 1 199 ? 11.334  8.361   -1.783  1   38.57 ? 184 VAL   B CA  1 
ATOM   4351 C  C   . VAL   B 1 199 ? 10.976  9.855   -1.65   1   40.4  ? 184 VAL   B C   1 
ATOM   4352 O  O   . VAL   B 1 199 ? 9.83    10.238  -1.912  1   40.92 ? 184 VAL   B O   1 
ATOM   4353 C  CB  . VAL   B 1 199 ? 11.499  7.673   -0.407  1   37.76 ? 184 VAL   B CB  1 
ATOM   4354 C  CG1 . VAL   B 1 199 ? 10.424  8.11    0.573   1   38.1  ? 184 VAL   B CG1 1 
ATOM   4355 C  CG2 . VAL   B 1 199 ? 11.512  6.16    -0.552  1   37.3  ? 184 VAL   B CG2 1 
ATOM   4356 N  N   . PHE   B 1 200 ? 11.94   10.69   -1.271  1   40.91 ? 185 PHE   B N   1 
ATOM   4357 C  CA  . PHE   B 1 200 ? 11.685  12.116  -1.1    1   41.94 ? 185 PHE   B CA  1 
ATOM   4358 C  C   . PHE   B 1 200 ? 11.44   12.841  -2.406  1   41.7  ? 185 PHE   B C   1 
ATOM   4359 O  O   . PHE   B 1 200 ? 10.609  13.753  -2.44   1   41.66 ? 185 PHE   B O   1 
ATOM   4360 C  CB  . PHE   B 1 200 ? 12.792  12.789  -0.296  1   43.23 ? 185 PHE   B CB  1 
ATOM   4361 C  CG  . PHE   B 1 200 ? 12.737  12.363  1.147   1   45.21 ? 185 PHE   B CG  1 
ATOM   4362 C  CD1 . PHE   B 1 200 ? 11.671  12.721  1.95    1   46.13 ? 185 PHE   B CD1 1 
ATOM   4363 C  CD2 . PHE   B 1 200 ? 13.734  11.572  1.693   1   47.15 ? 185 PHE   B CD2 1 
ATOM   4364 C  CE1 . PHE   B 1 200 ? 11.608  12.308  3.276   1   47.53 ? 185 PHE   B CE1 1 
ATOM   4365 C  CE2 . PHE   B 1 200 ? 13.673  11.17   3.027   1   48.37 ? 185 PHE   B CE2 1 
ATOM   4366 C  CZ  . PHE   B 1 200 ? 12.608  11.539  3.809   1   47.81 ? 185 PHE   B CZ  1 
ATOM   4367 N  N   . LYS   B 1 201 ? 12.117  12.429  -3.481  1   41.34 ? 186 LYS   B N   1 
ATOM   4368 C  CA  . LYS   B 1 201 ? 11.901  13.062  -4.776  1   41.48 ? 186 LYS   B CA  1 
ATOM   4369 C  C   . LYS   B 1 201 ? 10.486  12.735  -5.288  1   41.81 ? 186 LYS   B C   1 
ATOM   4370 O  O   . LYS   B 1 201 ? 9.83    13.628  -5.808  1   41.14 ? 186 LYS   B O   1 
ATOM   4371 C  CB  . LYS   B 1 201 ? 12.974  12.683  -5.809  1   42.78 ? 186 LYS   B CB  1 
ATOM   4372 N  N   . ALA   B 1 202 ? 10.009  11.482  -5.102  1   42.11 ? 187 ALA   B N   1 
ATOM   4373 C  CA  . ALA   B 1 202 ? 8.664   11.066  -5.524  1   43.17 ? 187 ALA   B CA  1 
ATOM   4374 C  C   . ALA   B 1 202 ? 7.588   11.855  -4.778  1   44.82 ? 187 ALA   B C   1 
ATOM   4375 O  O   . ALA   B 1 202 ? 6.6     12.263  -5.381  1   45.08 ? 187 ALA   B O   1 
ATOM   4376 C  CB  . ALA   B 1 202 ? 8.461   9.582   -5.294  1   42.57 ? 187 ALA   B CB  1 
ATOM   4377 N  N   . MET   B 1 203 ? 7.789   12.1    -3.49   1   45.72 ? 188 MET   B N   1 
ATOM   4378 C  CA  . MET   B 1 203 ? 6.844   12.893  -2.713  1   47.15 ? 188 MET   B CA  1 
ATOM   4379 C  C   . MET   B 1 203 ? 6.808   14.366  -3.154  1   48.55 ? 188 MET   B C   1 
ATOM   4380 O  O   . MET   B 1 203 ? 5.73    14.945  -3.243  1   49.25 ? 188 MET   B O   1 
ATOM   4381 C  CB  . MET   B 1 203 ? 7.187   12.814  -1.247  1   47.73 ? 188 MET   B CB  1 
ATOM   4382 C  CG  . MET   B 1 203 ? 6.76    11.546  -0.612  1   50.69 ? 188 MET   B CG  1 
ATOM   4383 S  SD  . MET   B 1 203 ? 7.317   11.506  1.106   1   60.73 ? 188 MET   B SD  1 
ATOM   4384 C  CE  . MET   B 1 203 ? 6.604   12.996  1.706   1   57.18 ? 188 MET   B CE  1 
ATOM   4385 N  N   . GLN   B 1 204 ? 7.97    14.965  -3.432  1   48.82 ? 189 GLN   B N   1 
ATOM   4386 C  CA  . GLN   B 1 204 ? 8.055   16.363  -3.859  1   49.54 ? 189 GLN   B CA  1 
ATOM   4387 C  C   . GLN   B 1 204 ? 7.451   16.533  -5.246  1   49.9  ? 189 GLN   B C   1 
ATOM   4388 O  O   . GLN   B 1 204 ? 6.736   17.501  -5.477  1   49.85 ? 189 GLN   B O   1 
ATOM   4389 C  CB  . GLN   B 1 204 ? 9.517   16.843  -3.867  1   51.02 ? 189 GLN   B CB  1 
ATOM   4390 C  CG  . GLN   B 1 204 ? 9.677   18.333  -4.138  1   54.26 ? 189 GLN   B CG  1 
ATOM   4391 N  N   . MET   B 1 205 ? 7.728   15.575  -6.156  1   49.68 ? 190 MET   B N   1 
ATOM   4392 C  CA  . MET   B 1 205 ? 7.237   15.559  -7.533  1   50.02 ? 190 MET   B CA  1 
ATOM   4393 C  C   . MET   B 1 205 ? 5.809   15.024  -7.675  1   49.71 ? 190 MET   B C   1 
ATOM   4394 O  O   . MET   B 1 205 ? 5.308   14.972  -8.801  1   50.14 ? 190 MET   B O   1 
ATOM   4395 C  CB  . MET   B 1 205 ? 8.149   14.701  -8.427  1   51.71 ? 190 MET   B CB  1 
ATOM   4396 C  CG  . MET   B 1 205 ? 9.601   15.151  -8.468  1   57.1  ? 190 MET   B CG  1 
ATOM   4397 S  SD  . MET   B 1 205 ? 9.818   16.878  -8.966  1   71.21 ? 190 MET   B SD  1 
ATOM   4398 C  CE  . MET   B 1 205 ? 10.688  17.516  -7.529  1   73.27 ? 190 MET   B CE  1 
ATOM   4399 N  N   . GLN   B 1 206 ? 5.186   14.564  -6.568  1   48.63 ? 191 GLN   B N   1 
ATOM   4400 C  CA  . GLN   B 1 206 ? 3.858   13.977  -6.555  1   48.36 ? 191 GLN   B CA  1 
ATOM   4401 C  C   . GLN   B 1 206 ? 3.768   12.811  -7.534  1   47.76 ? 191 GLN   B C   1 
ATOM   4402 O  O   . GLN   B 1 206 ? 2.988   12.845  -8.484  1   48.55 ? 191 GLN   B O   1 
ATOM   4403 C  CB  . GLN   B 1 206 ? 2.797   15.044  -6.804  1   49.57 ? 191 GLN   B CB  1 
ATOM   4404 C  CG  . GLN   B 1 206 ? 2.527   15.905  -5.568  1   52.93 ? 191 GLN   B CG  1 
ATOM   4405 C  CD  . GLN   B 1 206 ? 1.639   15.216  -4.548  1   58.62 ? 191 GLN   B CD  1 
ATOM   4406 O  OE1 . GLN   B 1 206 ? 1.038   14.164  -4.794  1   59.57 ? 191 GLN   B OE1 1 
ATOM   4407 N  NE2 . GLN   B 1 206 ? 1.52    15.807  -3.372  1   60.83 ? 191 GLN   B NE2 1 
ATOM   4408 N  N   . GLU   B 1 207 ? 4.643   11.823  -7.335  1   45.82 ? 192 GLU   B N   1 
ATOM   4409 C  CA  . GLU   B 1 207 ? 4.747   10.644  -8.162  1   44.85 ? 192 GLU   B CA  1 
ATOM   4410 C  C   . GLU   B 1 207 ? 4.437   9.405   -7.321  1   43.04 ? 192 GLU   B C   1 
ATOM   4411 O  O   . GLU   B 1 207 ? 5.351   8.713   -6.867  1   42.33 ? 192 GLU   B O   1 
ATOM   4412 C  CB  . GLU   B 1 207 ? 6.151   10.561  -8.764  1   48.65 ? 192 GLU   B CB  1 
ATOM   4413 C  CG  . GLU   B 1 207 ? 6.457   11.674  -9.75   1   56.16 ? 192 GLU   B CG  1 
ATOM   4414 C  CD  . GLU   B 1 207 ? 5.773   11.538  -11.1   1   65.69 ? 192 GLU   B CD  1 
ATOM   4415 O  OE1 . GLU   B 1 207 ? 5.521   10.391  -11.535 1   65.97 ? 192 GLU   B OE1 1 
ATOM   4416 O  OE2 . GLU   B 1 207 ? 5.496   12.585  -11.729 1   70.99 ? 192 GLU   B OE2 1 
ATOM   4417 N  N   . ARG   B 1 208 ? 3.137   9.121   -7.133  1   41.01 ? 193 ARG   B N   1 
ATOM   4418 C  CA  . ARG   B 1 208 ? 2.649   7.992   -6.339  1   38.86 ? 193 ARG   B CA  1 
ATOM   4419 C  C   . ARG   B 1 208 ? 3.233   6.655   -6.768  1   37.5  ? 193 ARG   B C   1 
ATOM   4420 O  O   . ARG   B 1 208 ? 3.595   5.855   -5.898  1   37.57 ? 193 ARG   B O   1 
ATOM   4421 C  CB  . ARG   B 1 208 ? 1.096   7.94    -6.349  1   38.02 ? 193 ARG   B CB  1 
ATOM   4422 C  CG  . ARG   B 1 208 ? 0.451   6.801   -5.541  1   37.1  ? 193 ARG   B CG  1 
ATOM   4423 C  CD  . ARG   B 1 208 ? 0.18    5.591   -6.406  1   37.23 ? 193 ARG   B CD  1 
ATOM   4424 N  NE  . ARG   B 1 208 ? -0.546  4.534   -5.703  1   38.39 ? 193 ARG   B NE  1 
ATOM   4425 C  CZ  . ARG   B 1 208 ? -0.693  3.292   -6.157  1   38.68 ? 193 ARG   B CZ  1 
ATOM   4426 N  NH1 . ARG   B 1 208 ? -0.13   2.924   -7.301  1   36.53 ? 193 ARG   B NH1 1 
ATOM   4427 N  NH2 . ARG   B 1 208 ? -1.384  2.401   -5.457  1   39.15 ? 193 ARG   B NH2 1 
ATOM   4428 N  N   . ASP   B 1 209 ? 3.255   6.364   -8.074  1   35.92 ? 194 ASP   B N   1 
ATOM   4429 C  CA  . ASP   B 1 209 ? 3.74    5.052   -8.522  1   35.58 ? 194 ASP   B CA  1 
ATOM   4430 C  C   . ASP   B 1 209 ? 5.241   4.868   -8.223  1   35.99 ? 194 ASP   B C   1 
ATOM   4431 O  O   . ASP   B 1 209 ? 5.661   3.778   -7.833  1   35.99 ? 194 ASP   B O   1 
ATOM   4432 C  CB  . ASP   B 1 209 ? 3.435   4.826   -10.005 1   35.44 ? 194 ASP   B CB  1 
ATOM   4433 C  CG  . ASP   B 1 209 ? 1.944   4.682   -10.331 1   36.53 ? 194 ASP   B CG  1 
ATOM   4434 O  OD1 . ASP   B 1 209 ? 1.145   4.461   -9.402  1   36.88 ? 194 ASP   B OD1 1 
ATOM   4435 O  OD2 . ASP   B 1 209 ? 1.593   4.771   -11.508 1   36.51 ? 194 ASP   B OD2 1 
ATOM   4436 N  N   . THR   B 1 210 ? 6.026   5.944   -8.39   1   36.12 ? 195 THR   B N   1 
ATOM   4437 C  CA  . THR   B 1 210 ? 7.459   5.934   -8.084  1   37.09 ? 195 THR   B CA  1 
ATOM   4438 C  C   . THR   B 1 210 ? 7.65    5.715   -6.578  1   38.15 ? 195 THR   B C   1 
ATOM   4439 O  O   . THR   B 1 210 ? 8.461   4.873   -6.193  1   38.67 ? 195 THR   B O   1 
ATOM   4440 C  CB  . THR   B 1 210 ? 8.145   7.198   -8.623  1   38.18 ? 195 THR   B CB  1 
ATOM   4441 O  OG1 . THR   B 1 210 ? 7.89    7.3     -10.032 1   38.89 ? 195 THR   B OG1 1 
ATOM   4442 C  CG2 . THR   B 1 210 ? 9.67    7.19    -8.389  1   38.41 ? 195 THR   B CG2 1 
ATOM   4443 N  N   . LEU   B 1 211 ? 6.859   6.4     -5.736  1   38.11 ? 196 LEU   B N   1 
ATOM   4444 C  CA  . LEU   B 1 211 ? 6.955   6.227   -4.29   1   39.02 ? 196 LEU   B CA  1 
ATOM   4445 C  C   . LEU   B 1 211 ? 6.637   4.8     -3.87   1   40.27 ? 196 LEU   B C   1 
ATOM   4446 O  O   . LEU   B 1 211 ? 7.375   4.226   -3.069  1   40.76 ? 196 LEU   B O   1 
ATOM   4447 C  CB  . LEU   B 1 211 ? 6.051   7.217   -3.541  1   38.88 ? 196 LEU   B CB  1 
ATOM   4448 C  CG  . LEU   B 1 211 ? 6.038   7.097   -2.025  1   39.89 ? 196 LEU   B CG  1 
ATOM   4449 C  CD1 . LEU   B 1 211 ? 7.425   7.346   -1.431  1   40.35 ? 196 LEU   B CD1 1 
ATOM   4450 C  CD2 . LEU   B 1 211 ? 5.027   8.041   -1.425  1   40.03 ? 196 LEU   B CD2 1 
ATOM   4451 N  N   . LEU   B 1 212 ? 5.577   4.212   -4.425  1   40.6  ? 197 LEU   B N   1 
ATOM   4452 C  CA  . LEU   B 1 212 ? 5.2     2.839   -4.083  1   41.08 ? 197 LEU   B CA  1 
ATOM   4453 C  C   . LEU   B 1 212 ? 6.316   1.843   -4.44   1   40.35 ? 197 LEU   B C   1 
ATOM   4454 O  O   . LEU   B 1 212 ? 6.597   0.944   -3.659  1   40.73 ? 197 LEU   B O   1 
ATOM   4455 C  CB  . LEU   B 1 212 ? 3.888   2.464   -4.793  1   41.87 ? 197 LEU   B CB  1 
ATOM   4456 C  CG  . LEU   B 1 212 ? 3.225   1.177   -4.321  1   43.98 ? 197 LEU   B CG  1 
ATOM   4457 C  CD1 . LEU   B 1 212 ? 1.726   1.319   -4.306  1   45.09 ? 197 LEU   B CD1 1 
ATOM   4458 C  CD2 . LEU   B 1 212 ? 3.582   0.046   -5.23   1   44.87 ? 197 LEU   B CD2 1 
ATOM   4459 N  N   . LYS   B 1 213 ? 6.915   1.982   -5.628  1   39.3  ? 198 LYS   B N   1 
ATOM   4460 C  CA  . LYS   B 1 213 ? 7.993   1.112   -6.084  1   38.91 ? 198 LYS   B CA  1 
ATOM   4461 C  C   . LYS   B 1 213 ? 9.21    1.246   -5.148  1   38.11 ? 198 LYS   B C   1 
ATOM   4462 O  O   . LYS   B 1 213 ? 9.777   0.242   -4.746  1   38.23 ? 198 LYS   B O   1 
ATOM   4463 C  CB  . LYS   B 1 213 ? 8.362   1.485   -7.532  1   41.13 ? 198 LYS   B CB  1 
ATOM   4464 C  CG  . LYS   B 1 213 ? 9.342   0.533   -8.223  1   46.31 ? 198 LYS   B CG  1 
ATOM   4465 C  CD  . LYS   B 1 213 ? 9.939   1.162   -9.498  1   51.35 ? 198 LYS   B CD  1 
ATOM   4466 N  N   . ALA   B 1 214 ? 9.552   2.484   -4.742  1   37.18 ? 199 ALA   B N   1 
ATOM   4467 C  CA  . ALA   B 1 214 ? 10.654  2.762   -3.824  1   36.73 ? 199 ALA   B CA  1 
ATOM   4468 C  C   . ALA   B 1 214 ? 10.408  2.153   -2.436  1   36.62 ? 199 ALA   B C   1 
ATOM   4469 O  O   . ALA   B 1 214 ? 11.313  1.507   -1.883  1   36.89 ? 199 ALA   B O   1 
ATOM   4470 C  CB  . ALA   B 1 214 ? 10.876  4.261   -3.712  1   36.44 ? 199 ALA   B CB  1 
ATOM   4471 N  N   . LEU   B 1 215 ? 9.18    2.279   -1.908  1   36.17 ? 200 LEU   B N   1 
ATOM   4472 C  CA  . LEU   B 1 215 ? 8.855   1.685   -0.614  1   35.8  ? 200 LEU   B CA  1 
ATOM   4473 C  C   . LEU   B 1 215 ? 8.956   0.161   -0.661  1   36.38 ? 200 LEU   B C   1 
ATOM   4474 O  O   . LEU   B 1 215 ? 9.451   -0.455  0.294   1   37.16 ? 200 LEU   B O   1 
ATOM   4475 C  CB  . LEU   B 1 215 ? 7.485   2.13    -0.123  1   35.81 ? 200 LEU   B CB  1 
ATOM   4476 C  CG  . LEU   B 1 215 ? 7.377   3.597   0.293   1   37.36 ? 200 LEU   B CG  1 
ATOM   4477 C  CD1 . LEU   B 1 215 ? 5.984   3.906   0.779   1   37.41 ? 200 LEU   B CD1 1 
ATOM   4478 C  CD2 . LEU   B 1 215 ? 8.378   3.945   1.396   1   38.03 ? 200 LEU   B CD2 1 
ATOM   4479 N  N   . LEU   B 1 216 ? 8.538   -0.452  -1.772  1   35.61 ? 201 LEU   B N   1 
ATOM   4480 C  CA  . LEU   B 1 216 ? 8.622   -1.905  -1.915  1   36.31 ? 201 LEU   B CA  1 
ATOM   4481 C  C   . LEU   B 1 216 ? 10.066  -2.396  -2.068  1   36.63 ? 201 LEU   B C   1 
ATOM   4482 O  O   . LEU   B 1 216 ? 10.374  -3.508  -1.663  1   36.52 ? 201 LEU   B O   1 
ATOM   4483 C  CB  . LEU   B 1 216 ? 7.802   -2.381  -3.118  1   36.51 ? 201 LEU   B CB  1 
ATOM   4484 C  CG  . LEU   B 1 216 ? 6.283   -2.333  -2.95   1   38.08 ? 201 LEU   B CG  1 
ATOM   4485 C  CD1 . LEU   B 1 216 ? 5.598   -2.806  -4.222  1   38.44 ? 201 LEU   B CD1 1 
ATOM   4486 C  CD2 . LEU   B 1 216 ? 5.812   -3.142  -1.731  1   37.88 ? 201 LEU   B CD2 1 
ATOM   4487 N  N   . GLU   B 1 217 ? 10.919  -1.595  -2.697  1   36.6  ? 202 GLU   B N   1 
ATOM   4488 C  CA  . GLU   B 1 217 ? 12.322  -1.925  -2.873  1   36.59 ? 202 GLU   B CA  1 
ATOM   4489 C  C   . GLU   B 1 217 ? 13.033  -1.835  -1.508  1   36.26 ? 202 GLU   B C   1 
ATOM   4490 O  O   . GLU   B 1 217 ? 13.782  -2.743  -1.155  1   37.73 ? 202 GLU   B O   1 
ATOM   4491 C  CB  . GLU   B 1 217 ? 12.963  -1.014  -3.932  1   37.91 ? 202 GLU   B CB  1 
ATOM   4492 C  CG  . GLU   B 1 217 ? 14.454  -1.249  -4.128  1   41.32 ? 202 GLU   B CG  1 
ATOM   4493 C  CD  . GLU   B 1 217 ? 14.917  -2.633  -4.559  1   46.5  ? 202 GLU   B CD  1 
ATOM   4494 O  OE1 . GLU   B 1 217 ? 14.082  -3.446  -5.021  1   46.8  ? 202 GLU   B OE1 1 
ATOM   4495 O  OE2 . GLU   B 1 217 ? 16.137  -2.895  -4.444  1   47.08 ? 202 GLU   B OE2 1 
ATOM   4496 N  N   . ILE   B 1 218 ? 12.697  -0.836  -0.688  1   34.29 ? 203 ILE   B N   1 
ATOM   4497 C  CA  . ILE   B 1 218 ? 13.245  -0.725  0.658   1   33.77 ? 203 ILE   B CA  1 
ATOM   4498 C  C   . ILE   B 1 218 ? 12.819  -1.943  1.491   1   34.61 ? 203 ILE   B C   1 
ATOM   4499 O  O   . ILE   B 1 218 ? 13.656  -2.6    2.103   1   35.42 ? 203 ILE   B O   1 
ATOM   4500 C  CB  . ILE   B 1 218 ? 12.83   0.625   1.291   1   33.13 ? 203 ILE   B CB  1 
ATOM   4501 C  CG1 . ILE   B 1 218 ? 13.602  1.773   0.625   1   33.39 ? 203 ILE   B CG1 1 
ATOM   4502 C  CG2 . ILE   B 1 218 ? 13.02   0.625   2.821   1   32.99 ? 203 ILE   B CG2 1 
ATOM   4503 C  CD1 . ILE   B 1 218 ? 13.214  3.152   1.101   1   33.97 ? 203 ILE   B CD1 1 
ATOM   4504 N  N   . ALA   B 1 219 ? 11.534  -2.307  1.435   1   34.77 ? 204 ALA   B N   1 
ATOM   4505 C  CA  . ALA   B 1 219 ? 11.029  -3.462  2.173   1   35.43 ? 204 ALA   B CA  1 
ATOM   4506 C  C   . ALA   B 1 219 ? 11.736  -4.743  1.717   1   36.99 ? 204 ALA   B C   1 
ATOM   4507 O  O   . ALA   B 1 219 ? 12.23   -5.509  2.55    1   37.83 ? 204 ALA   B O   1 
ATOM   4508 C  CB  . ALA   B 1 219 ? 9.525   -3.584  2.001   1   35.5  ? 204 ALA   B CB  1 
ATOM   4509 N  N   . SER   B 1 220 ? 11.893  -4.913  0.394   1   36.74 ? 205 SER   B N   1 
ATOM   4510 C  CA  . SER   B 1 220 ? 12.579  -6.065  -0.166  1   37.12 ? 205 SER   B CA  1 
ATOM   4511 C  C   . SER   B 1 220 ? 14.025  -6.181  0.376   1   37.42 ? 205 SER   B C   1 
ATOM   4512 O  O   . SER   B 1 220 ? 14.434  -7.265  0.798   1   38.3  ? 205 SER   B O   1 
ATOM   4513 C  CB  . SER   B 1 220 ? 12.572  -5.973  -1.691  1   38.18 ? 205 SER   B CB  1 
ATOM   4514 O  OG  . SER   B 1 220 ? 13.578  -6.758  -2.312  1   40.54 ? 205 SER   B OG  1 
ATOM   4515 N  N   . CYS   B 1 221 ? 14.757  -5.056  0.412   1   36.48 ? 206 CYS   B N   1 
ATOM   4516 C  CA  . CYS   B 1 221 ? 16.137  -4.998  0.878   1   35.96 ? 206 CYS   B CA  1 
ATOM   4517 C  C   . CYS   B 1 221 ? 16.272  -5.332  2.357   1   35.43 ? 206 CYS   B C   1 
ATOM   4518 O  O   . CYS   B 1 221 ? 17.116  -6.158  2.722   1   34.4  ? 206 CYS   B O   1 
ATOM   4519 C  CB  . CYS   B 1 221 ? 16.753  -3.65   0.537   1   36.44 ? 206 CYS   B CB  1 
ATOM   4520 S  SG  . CYS   B 1 221 ? 17.078  -3.438  -1.234  1   40.93 ? 206 CYS   B SG  1 
ATOM   4521 N  N   . LEU   B 1 222 ? 15.368  -4.78   3.188   1   35.08 ? 207 LEU   B N   1 
ATOM   4522 C  CA  . LEU   B 1 222 ? 15.349  -5.071  4.626   1   35.25 ? 207 LEU   B CA  1 
ATOM   4523 C  C   . LEU   B 1 222 ? 14.946  -6.52   4.912   1   35.42 ? 207 LEU   B C   1 
ATOM   4524 O  O   . LEU   B 1 222 ? 15.386  -7.091  5.912   1   34.96 ? 207 LEU   B O   1 
ATOM   4525 C  CB  . LEU   B 1 222 ? 14.446  -4.079  5.379   1   35.48 ? 207 LEU   B CB  1 
ATOM   4526 C  CG  . LEU   B 1 222 ? 14.864  -2.614  5.28    1   37.12 ? 207 LEU   B CG  1 
ATOM   4527 C  CD1 . LEU   B 1 222 ? 13.892  -1.715  6       1   37.31 ? 207 LEU   B CD1 1 
ATOM   4528 C  CD2 . LEU   B 1 222 ? 16.287  -2.397  5.838   1   37.87 ? 207 LEU   B CD2 1 
ATOM   4529 N  N   . GLU   B 1 223 ? 14.119  -7.118  4.045   1   35.98 ? 208 GLU   B N   1 
ATOM   4530 C  CA  . GLU   B 1 223 ? 13.72   -8.522  4.177   1   37.85 ? 208 GLU   B CA  1 
ATOM   4531 C  C   . GLU   B 1 223 ? 14.936  -9.429  3.905   1   38.95 ? 208 GLU   B C   1 
ATOM   4532 O  O   . GLU   B 1 223 ? 15.126  -10.434 4.591   1   38.79 ? 208 GLU   B O   1 
ATOM   4533 C  CB  . GLU   B 1 223 ? 12.589  -8.871  3.183   1   40.21 ? 208 GLU   B CB  1 
ATOM   4534 C  CG  . GLU   B 1 223 ? 11.207  -8.395  3.614   1   44.11 ? 208 GLU   B CG  1 
ATOM   4535 C  CD  . GLU   B 1 223 ? 10.187  -8.248  2.499   1   48.74 ? 208 GLU   B CD  1 
ATOM   4536 O  OE1 . GLU   B 1 223 ? 10.416  -8.797  1.396   1   49.25 ? 208 GLU   B OE1 1 
ATOM   4537 O  OE2 . GLU   B 1 223 ? 9.16    -7.569  2.731   1   50.07 ? 208 GLU   B OE2 1 
ATOM   4538 N  N   . LYS   B 1 224 ? 15.772  -9.052  2.919   1   39.88 ? 209 LYS   B N   1 
ATOM   4539 C  CA  . LYS   B 1 224 ? 16.981  -9.816  2.593   1   40.9  ? 209 LYS   B CA  1 
ATOM   4540 C  C   . LYS   B 1 224 ? 18.03   -9.717  3.714   1   41.45 ? 209 LYS   B C   1 
ATOM   4541 O  O   . LYS   B 1 224 ? 18.754  -10.674 3.975   1   42.04 ? 209 LYS   B O   1 
ATOM   4542 C  CB  . LYS   B 1 224 ? 17.559  -9.356  1.245   1   42.35 ? 209 LYS   B CB  1 
ATOM   4543 C  CG  . LYS   B 1 224 ? 16.708  -9.769  0.053   1   46.51 ? 209 LYS   B CG  1 
ATOM   4544 C  CD  . LYS   B 1 224 ? 17.213  -9.057  -1.201  1   50.42 ? 209 LYS   B CD  1 
ATOM   4545 C  CE  . LYS   B 1 224 ? 16.181  -8.941  -2.299  1   54.23 ? 209 LYS   B CE  1 
ATOM   4546 N  NZ  . LYS   B 1 224 ? 15.563  -10.252 -2.637  1   55.81 ? 209 LYS   B NZ  1 
ATOM   4547 N  N   . ALA   B 1 225 ? 18.085  -8.565  4.4     1   41.32 ? 210 ALA   B N   1 
ATOM   4548 C  CA  . ALA   B 1 225 ? 19.008  -8.346  5.5     1   41.54 ? 210 ALA   B CA  1 
ATOM   4549 C  C   . ALA   B 1 225 ? 18.789  -9.319  6.68    1   42.16 ? 210 ALA   B C   1 
ATOM   4550 O  O   . ALA   B 1 225 ? 19.709  -9.545  7.469   1   43.03 ? 210 ALA   B O   1 
ATOM   4551 C  CB  . ALA   B 1 225 ? 18.903  -6.906  5.98    1   41.23 ? 210 ALA   B CB  1 
ATOM   4552 N  N   . LEU   B 1 226 ? 17.583  -9.867  6.821   1   41.96 ? 211 LEU   B N   1 
ATOM   4553 C  CA  . LEU   B 1 226 ? 17.277  -10.795 7.905   1   42.2  ? 211 LEU   B CA  1 
ATOM   4554 C  C   . LEU   B 1 226 ? 18.128  -12.057 7.805   1   42.84 ? 211 LEU   B C   1 
ATOM   4555 O  O   . LEU   B 1 226 ? 18.593  -12.573 8.824   1   43.51 ? 211 LEU   B O   1 
ATOM   4556 C  CB  . LEU   B 1 226 ? 15.782  -11.169 7.876   1   42.04 ? 211 LEU   B CB  1 
ATOM   4557 C  CG  . LEU   B 1 226 ? 15.325  -12.18  8.919   1   43.16 ? 211 LEU   B CG  1 
ATOM   4558 C  CD1 . LEU   B 1 226 ? 15.548  -11.66  10.308  1   43.34 ? 211 LEU   B CD1 1 
ATOM   4559 C  CD2 . LEU   B 1 226 ? 13.856  -12.525 8.75    1   44.29 ? 211 LEU   B CD2 1 
ATOM   4560 N  N   . GLN   B 1 227 ? 18.327  -12.555 6.584   1   42.93 ? 212 GLN   B N   1 
ATOM   4561 C  CA  . GLN   B 1 227 ? 19.111  -13.776 6.379   1   43.66 ? 212 GLN   B CA  1 
ATOM   4562 C  C   . GLN   B 1 227 ? 20.571  -13.578 6.802   1   43.14 ? 212 GLN   B C   1 
ATOM   4563 O  O   . GLN   B 1 227 ? 21.21   -14.514 7.293   1   43.25 ? 212 GLN   B O   1 
ATOM   4564 C  CB  . GLN   B 1 227 ? 19.008  -14.285 4.915   1   47.14 ? 212 GLN   B CB  1 
ATOM   4565 C  CG  . GLN   B 1 227 ? 17.696  -13.919 4.145   1   54.5  ? 212 GLN   B CG  1 
ATOM   4566 C  CD  . GLN   B 1 227 ? 16.381  -14.235 4.851   1   60.73 ? 212 GLN   B CD  1 
ATOM   4567 O  OE1 . GLN   B 1 227 ? 16.216  -15.271 5.52    1   62.91 ? 212 GLN   B OE1 1 
ATOM   4568 N  NE2 . GLN   B 1 227 ? 15.41   -13.336 4.702   1   61.12 ? 212 GLN   B NE2 1 
ATOM   4569 N  N   . VAL   B 1 228 ? 21.083  -12.339 6.66    1   42.15 ? 213 VAL   B N   1 
ATOM   4570 C  CA  . VAL   B 1 228 ? 22.432  -11.973 7.051   1   41.29 ? 213 VAL   B CA  1 
ATOM   4571 C  C   . VAL   B 1 228 ? 22.647  -12.213 8.542   1   41.11 ? 213 VAL   B C   1 
ATOM   4572 O  O   . VAL   B 1 228 ? 23.696  -12.707 8.935   1   41.7  ? 213 VAL   B O   1 
ATOM   4573 C  CB  . VAL   B 1 228 ? 22.736  -10.52  6.628   1   41.21 ? 213 VAL   B CB  1 
ATOM   4574 C  CG1 . VAL   B 1 228 ? 24.152  -10.116 7.035   1   41.26 ? 213 VAL   B CG1 1 
ATOM   4575 C  CG2 . VAL   B 1 228 ? 22.522  -10.347 5.125   1   40.93 ? 213 VAL   B CG2 1 
ATOM   4576 N  N   . PHE   B 1 229 ? 21.627  -11.952 9.359   1   40.38 ? 214 PHE   B N   1 
ATOM   4577 C  CA  . PHE   B 1 229 ? 21.68   -12.146 10.806  1   40.07 ? 214 PHE   B CA  1 
ATOM   4578 C  C   . PHE   B 1 229 ? 21.887  -13.603 11.205  1   40.83 ? 214 PHE   B C   1 
ATOM   4579 O  O   . PHE   B 1 229 ? 22.414  -13.866 12.292  1   40.74 ? 214 PHE   B O   1 
ATOM   4580 C  CB  . PHE   B 1 229 ? 20.371  -11.656 11.443  1   39.11 ? 214 PHE   B CB  1 
ATOM   4581 C  CG  . PHE   B 1 229 ? 20.398  -10.238 11.958  1   38.06 ? 214 PHE   B CG  1 
ATOM   4582 C  CD1 . PHE   B 1 229 ? 20.793  -9.964  13.254  1   37.75 ? 214 PHE   B CD1 1 
ATOM   4583 C  CD2 . PHE   B 1 229 ? 19.984  -9.184  11.159  1   38.19 ? 214 PHE   B CD2 1 
ATOM   4584 C  CE1 . PHE   B 1 229 ? 20.784  -8.67   13.743  1   37.89 ? 214 PHE   B CE1 1 
ATOM   4585 C  CE2 . PHE   B 1 229 ? 19.982  -7.882  11.652  1   38.05 ? 214 PHE   B CE2 1 
ATOM   4586 C  CZ  . PHE   B 1 229 ? 20.381  -7.638  12.944  1   37.56 ? 214 PHE   B CZ  1 
ATOM   4587 N  N   . HIS   B 1 230 ? 21.445  -14.552 10.363  1   40.76 ? 215 HIS   B N   1 
ATOM   4588 C  CA  . HIS   B 1 230 ? 21.59   -15.974 10.686  1   41.66 ? 215 HIS   B CA  1 
ATOM   4589 C  C   . HIS   B 1 230 ? 23.045  -16.4   10.866  1   40.96 ? 215 HIS   B C   1 
ATOM   4590 O  O   . HIS   B 1 230 ? 23.299  -17.328 11.633  1   40.86 ? 215 HIS   B O   1 
ATOM   4591 C  CB  . HIS   B 1 230 ? 20.892  -16.875 9.65    1   43.76 ? 215 HIS   B CB  1 
ATOM   4592 C  CG  . HIS   B 1 230 ? 19.42   -16.617 9.496   1   47.89 ? 215 HIS   B CG  1 
ATOM   4593 N  ND1 . HIS   B 1 230 ? 18.733  -17.023 8.365   1   50.58 ? 215 HIS   B ND1 1 
ATOM   4594 C  CD2 . HIS   B 1 230 ? 18.558  -15.975 10.322  1   49.46 ? 215 HIS   B CD2 1 
ATOM   4595 C  CE1 . HIS   B 1 230 ? 17.48   -16.634 8.549   1   51.32 ? 215 HIS   B CE1 1 
ATOM   4596 N  NE2 . HIS   B 1 230 ? 17.329  -15.996 9.709   1   50.89 ? 215 HIS   B NE2 1 
ATOM   4597 N  N   . GLN   B 1 231 ? 23.996  -15.69  10.217  1   39.99 ? 216 GLN   B N   1 
ATOM   4598 C  CA  . GLN   B 1 231 ? 25.436  -15.956 10.3    1   39.96 ? 216 GLN   B CA  1 
ATOM   4599 C  C   . GLN   B 1 231 ? 26.011  -15.846 11.692  1   40.7  ? 216 GLN   B C   1 
ATOM   4600 O  O   . GLN   B 1 231 ? 27.084  -16.391 11.935  1   41.08 ? 216 GLN   B O   1 
ATOM   4601 C  CB  . GLN   B 1 231 ? 26.226  -15.021 9.387   1   40.28 ? 216 GLN   B CB  1 
ATOM   4602 C  CG  . GLN   B 1 231 ? 25.884  -15.213 7.936   1   42.34 ? 216 GLN   B CG  1 
ATOM   4603 C  CD  . GLN   B 1 231 ? 26.624  -14.197 7.138   1   44.48 ? 216 GLN   B CD  1 
ATOM   4604 O  OE1 . GLN   B 1 231 ? 27.713  -14.463 6.632   1   45.31 ? 216 GLN   B OE1 1 
ATOM   4605 N  NE2 . GLN   B 1 231 ? 26.065  -12.998 7.04    1   43.14 ? 216 GLN   B NE2 1 
ATOM   4606 N  N   . ILE   B 1 232 ? 25.331  -15.129 12.61   1   40.37 ? 217 ILE   B N   1 
ATOM   4607 C  CA  . ILE   B 1 232 ? 25.819  -14.946 13.967  1   39.96 ? 217 ILE   B CA  1 
ATOM   4608 C  C   . ILE   B 1 232 ? 26.028  -16.276 14.68   1   39.31 ? 217 ILE   B C   1 
ATOM   4609 O  O   . ILE   B 1 232 ? 27.012  -16.425 15.391  1   38.92 ? 217 ILE   B O   1 
ATOM   4610 C  CB  . ILE   B 1 232 ? 24.904  -14.004 14.785  1   40.65 ? 217 ILE   B CB  1 
ATOM   4611 C  CG1 . ILE   B 1 232 ? 25.652  -13.401 15.961  1   41.31 ? 217 ILE   B CG1 1 
ATOM   4612 C  CG2 . ILE   B 1 232 ? 23.624  -14.69  15.252  1   41.79 ? 217 ILE   B CG2 1 
ATOM   4613 C  CD1 . ILE   B 1 232 ? 26.573  -12.196 15.51   1   41.62 ? 217 ILE   B CD1 1 
ATOM   4614 N  N   . HIS   B 1 233 ? 25.137  -17.254 14.457  1   39.41 ? 218 HIS   B N   1 
ATOM   4615 C  CA  . HIS   B 1 233 ? 25.243  -18.558 15.125  1   39.64 ? 218 HIS   B CA  1 
ATOM   4616 C  C   . HIS   B 1 233 ? 26.464  -19.373 14.718  1   40.21 ? 218 HIS   B C   1 
ATOM   4617 O  O   . HIS   B 1 233 ? 26.957  -20.186 15.508  1   39.94 ? 218 HIS   B O   1 
ATOM   4618 C  CB  . HIS   B 1 233 ? 23.965  -19.375 14.918  1   39.52 ? 218 HIS   B CB  1 
ATOM   4619 C  CG  . HIS   B 1 233 ? 22.735  -18.633 15.331  1   39.89 ? 218 HIS   B CG  1 
ATOM   4620 N  ND1 . HIS   B 1 233 ? 22.408  -18.471 16.66   1   41.03 ? 218 HIS   B ND1 1 
ATOM   4621 C  CD2 . HIS   B 1 233 ? 21.813  -18.004 14.569  1   40.86 ? 218 HIS   B CD2 1 
ATOM   4622 C  CE1 . HIS   B 1 233 ? 21.282  -17.776 16.665  1   42.06 ? 218 HIS   B CE1 1 
ATOM   4623 N  NE2 . HIS   B 1 233 ? 20.888  -17.469 15.425  1   41.84 ? 218 HIS   B NE2 1 
ATOM   4624 N  N   . ASP   B 1 234 ? 26.945  -19.161 13.494  1   40.64 ? 219 ASP   B N   1 
ATOM   4625 C  CA  . ASP   B 1 234 ? 28.103  -19.888 12.989  1   41.45 ? 219 ASP   B CA  1 
ATOM   4626 C  C   . ASP   B 1 234 ? 29.437  -19.34  13.464  1   41.2  ? 219 ASP   B C   1 
ATOM   4627 O  O   . ASP   B 1 234 ? 30.437  -20.057 13.423  1   42.19 ? 219 ASP   B O   1 
ATOM   4628 C  CB  . ASP   B 1 234 ? 28.086  -19.869 11.454  1   43.5  ? 219 ASP   B CB  1 
ATOM   4629 C  CG  . ASP   B 1 234 ? 26.91   -20.631 10.887  1   49.25 ? 219 ASP   B CG  1 
ATOM   4630 O  OD1 . ASP   B 1 234 ? 26.509  -21.634 11.5    1   50.31 ? 219 ASP   B OD1 1 
ATOM   4631 O  OD2 . ASP   B 1 234 ? 26.39   -20.221 9.833   1   52.45 ? 219 ASP   B OD2 1 
ATOM   4632 N  N   . HIS   B 1 235 ? 29.478  -18.066 13.871  1   39.28 ? 220 HIS   B N   1 
ATOM   4633 C  CA  . HIS   B 1 235 ? 30.746  -17.422 14.165  1   37.6  ? 220 HIS   B CA  1 
ATOM   4634 C  C   . HIS   B 1 235 ? 30.907  -16.867 15.554  1   36.26 ? 220 HIS   B C   1 
ATOM   4635 O  O   . HIS   B 1 235 ? 31.975  -16.329 15.856  1   37.61 ? 220 HIS   B O   1 
ATOM   4636 C  CB  . HIS   B 1 235 ? 30.974  -16.316 13.134  1   38.23 ? 220 HIS   B CB  1 
ATOM   4637 C  CG  . HIS   B 1 235 ? 30.848  -16.809 11.728  1   40.58 ? 220 HIS   B CG  1 
ATOM   4638 N  ND1 . HIS   B 1 235 ? 31.548  -17.917 11.291  1   42.7  ? 220 HIS   B ND1 1 
ATOM   4639 C  CD2 . HIS   B 1 235 ? 30.068  -16.363 10.72   1   42.15 ? 220 HIS   B CD2 1 
ATOM   4640 C  CE1 . HIS   B 1 235 ? 31.203  -18.089 10.028  1   43.01 ? 220 HIS   B CE1 1 
ATOM   4641 N  NE2 . HIS   B 1 235 ? 30.315  -17.178 9.64    1   43.28 ? 220 HIS   B NE2 1 
ATOM   4642 N  N   . VAL   B 1 236 ? 29.873  -16.95  16.395  1   34.1  ? 221 VAL   B N   1 
ATOM   4643 C  CA  . VAL   B 1 236 ? 29.978  -16.42  17.76   1   33.7  ? 221 VAL   B CA  1 
ATOM   4644 C  C   . VAL   B 1 236 ? 29.477  -17.469 18.708  1   34.55 ? 221 VAL   B C   1 
ATOM   4645 O  O   . VAL   B 1 236 ? 28.452  -18.088 18.416  1   36.12 ? 221 VAL   B O   1 
ATOM   4646 C  CB  . VAL   B 1 236 ? 29.169  -15.103 17.942  1   32.28 ? 221 VAL   B CB  1 
ATOM   4647 C  CG1 . VAL   B 1 236 ? 29.368  -14.507 19.338  1   31.56 ? 221 VAL   B CG1 1 
ATOM   4648 C  CG2 . VAL   B 1 236 ? 29.541  -14.082 16.887  1   32.1  ? 221 VAL   B CG2 1 
ATOM   4649 N  N   . ASN   B 1 237 ? 30.159  -17.671 19.846  1   33.85 ? 222 ASN   B N   1 
ATOM   4650 C  CA  . ASN   B 1 237 ? 29.648  -18.606 20.823  1   34.03 ? 222 ASN   B CA  1 
ATOM   4651 C  C   . ASN   B 1 237 ? 29.275  -17.86  22.077  1   33.17 ? 222 ASN   B C   1 
ATOM   4652 O  O   . ASN   B 1 237 ? 29.986  -16.925 22.466  1   32.09 ? 222 ASN   B O   1 
ATOM   4653 C  CB  . ASN   B 1 237 ? 30.557  -19.815 21.069  1   37.98 ? 222 ASN   B CB  1 
ATOM   4654 C  CG  . ASN   B 1 237 ? 31.694  -19.568 22.008  1   43.72 ? 222 ASN   B CG  1 
ATOM   4655 O  OD1 . ASN   B 1 237 ? 32.772  -19.141 21.581  1   48.32 ? 222 ASN   B OD1 1 
ATOM   4656 N  ND2 . ASN   B 1 237 ? 31.488  -19.827 23.293  1   42.94 ? 222 ASN   B ND2 1 
ATOM   4657 N  N   . PRO   B 1 238 ? 28.108  -18.218 22.674  1   33.81 ? 223 PRO   B N   1 
ATOM   4658 C  CA  . PRO   B 1 238 ? 27.602  -17.454 23.823  1   34.35 ? 223 PRO   B CA  1 
ATOM   4659 C  C   . PRO   B 1 238 ? 28.558  -17.272 24.99   1   35.4  ? 223 PRO   B C   1 
ATOM   4660 O  O   . PRO   B 1 238 ? 28.676  -16.145 25.476  1   36.31 ? 223 PRO   B O   1 
ATOM   4661 C  CB  . PRO   B 1 238 ? 26.339  -18.222 24.241  1   34.73 ? 223 PRO   B CB  1 
ATOM   4662 C  CG  . PRO   B 1 238 ? 25.893  -18.932 23.02   1   34.52 ? 223 PRO   B CG  1 
ATOM   4663 C  CD  . PRO   B 1 238 ? 27.144  -19.26  22.245  1   32.89 ? 223 PRO   B CD  1 
ATOM   4664 N  N   . LYS   B 1 239 ? 29.225  -18.339 25.455  1   35.59 ? 224 LYS   B N   1 
ATOM   4665 C  CA  . LYS   B 1 239 ? 30.126  -18.235 26.607  1   36.11 ? 224 LYS   B CA  1 
ATOM   4666 C  C   . LYS   B 1 239 ? 31.221  -17.172 26.443  1   36.09 ? 224 LYS   B C   1 
ATOM   4667 O  O   . LYS   B 1 239 ? 31.361  -16.303 27.299  1   36.57 ? 224 LYS   B O   1 
ATOM   4668 C  CB  . LYS   B 1 239 ? 30.738  -19.615 26.964  1   38.68 ? 224 LYS   B CB  1 
ATOM   4669 N  N   . ALA   B 1 240 ? 31.969  -17.226 25.347  1   35.5  ? 225 ALA   B N   1 
ATOM   4670 C  CA  . ALA   B 1 240 ? 33.069  -16.312 25.051  1   35.51 ? 225 ALA   B CA  1 
ATOM   4671 C  C   . ALA   B 1 240 ? 32.564  -14.895 24.818  1   35.05 ? 225 ALA   B C   1 
ATOM   4672 O  O   . ALA   B 1 240 ? 33.147  -13.933 25.332  1   35.41 ? 225 ALA   B O   1 
ATOM   4673 C  CB  . ALA   B 1 240 ? 33.82   -16.805 23.826  1   35.43 ? 225 ALA   B CB  1 
ATOM   4674 N  N   . PHE   B 1 241 ? 31.452  -14.757 24.101  1   34.08 ? 226 PHE   B N   1 
ATOM   4675 C  CA  . PHE   B 1 241 ? 30.848  -13.462 23.828  1   33.51 ? 226 PHE   B CA  1 
ATOM   4676 C  C   . PHE   B 1 241 ? 30.445  -12.797 25.143  1   33.31 ? 226 PHE   B C   1 
ATOM   4677 O  O   . PHE   B 1 241 ? 30.748  -11.633 25.373  1   33.61 ? 226 PHE   B O   1 
ATOM   4678 C  CB  . PHE   B 1 241 ? 29.609  -13.635 22.917  1   32.92 ? 226 PHE   B CB  1 
ATOM   4679 C  CG  . PHE   B 1 241 ? 28.791  -12.362 22.802  1   33.1  ? 226 PHE   B CG  1 
ATOM   4680 C  CD1 . PHE   B 1 241 ? 29.173  -11.353 21.934  1   33.97 ? 226 PHE   B CD1 1 
ATOM   4681 C  CD2 . PHE   B 1 241 ? 27.725  -12.123 23.66   1   33.27 ? 226 PHE   B CD2 1 
ATOM   4682 C  CE1 . PHE   B 1 241 ? 28.482  -10.148 21.901  1   34.46 ? 226 PHE   B CE1 1 
ATOM   4683 C  CE2 . PHE   B 1 241 ? 27.045  -10.913 23.63   1   33.92 ? 226 PHE   B CE2 1 
ATOM   4684 C  CZ  . PHE   B 1 241 ? 27.417  -9.941  22.738  1   33.86 ? 226 PHE   B CZ  1 
ATOM   4685 N  N   . PHE   B 1 242 ? 29.787  -13.563 26.011  1   33.51 ? 227 PHE   B N   1 
ATOM   4686 C  CA  . PHE   B 1 242 ? 29.26   -13.031 27.247  1   33.01 ? 227 PHE   B CA  1 
ATOM   4687 C  C   . PHE   B 1 242 ? 30.338  -12.74  28.254  1   34.1  ? 227 PHE   B C   1 
ATOM   4688 O  O   . PHE   B 1 242 ? 30.379  -11.638 28.789  1   34.55 ? 227 PHE   B O   1 
ATOM   4689 C  CB  . PHE   B 1 242 ? 28.153  -13.937 27.822  1   31.31 ? 227 PHE   B CB  1 
ATOM   4690 C  CG  . PHE   B 1 242 ? 27.535  -13.373 29.078  1   30.62 ? 227 PHE   B CG  1 
ATOM   4691 C  CD1 . PHE   B 1 242 ? 26.566  -12.385 29.01   1   31.08 ? 227 PHE   B CD1 1 
ATOM   4692 C  CD2 . PHE   B 1 242 ? 27.949  -13.803 30.326  1   30.55 ? 227 PHE   B CD2 1 
ATOM   4693 C  CE1 . PHE   B 1 242 ? 26.029  -11.833 30.175  1   32.16 ? 227 PHE   B CE1 1 
ATOM   4694 C  CE2 . PHE   B 1 242 ? 27.425  -13.244 31.484  1   31.18 ? 227 PHE   B CE2 1 
ATOM   4695 C  CZ  . PHE   B 1 242 ? 26.461  -12.273 31.412  1   31.42 ? 227 PHE   B CZ  1 
ATOM   4696 N  N   . SER   B 1 243 ? 31.21   -13.711 28.539  1   34.37 ? 228 SER   B N   1 
ATOM   4697 C  CA  . SER   B 1 243 ? 32.226  -13.536 29.562  1   35.1  ? 228 SER   B CA  1 
ATOM   4698 C  C   . SER   B 1 243 ? 33.438  -12.713 29.117  1   35.31 ? 228 SER   B C   1 
ATOM   4699 O  O   . SER   B 1 243 ? 34.075  -12.105 29.975  1   37.19 ? 228 SER   B O   1 
ATOM   4700 C  CB  . SER   B 1 243 ? 32.659  -14.887 30.122  1   36.79 ? 228 SER   B CB  1 
ATOM   4701 O  OG  . SER   B 1 243 ? 33.234  -15.666 29.091  1   39.26 ? 228 SER   B OG  1 
ATOM   4702 N  N   . VAL   B 1 244 ? 33.729  -12.627 27.811  1   33.84 ? 229 VAL   B N   1 
ATOM   4703 C  CA  . VAL   B 1 244 ? 34.911  -11.887 27.356  1   33.8  ? 229 VAL   B CA  1 
ATOM   4704 C  C   . VAL   B 1 244 ? 34.591  -10.602 26.534  1   32.68 ? 229 VAL   B C   1 
ATOM   4705 O  O   . VAL   B 1 244 ? 34.899  -9.505  27.007  1   32.09 ? 229 VAL   B O   1 
ATOM   4706 C  CB  . VAL   B 1 244 ? 35.922  -12.813 26.609  1   34.43 ? 229 VAL   B CB  1 
ATOM   4707 C  CG1 . VAL   B 1 244 ? 37.174  -12.036 26.166  1   34.84 ? 229 VAL   B CG1 1 
ATOM   4708 C  CG2 . VAL   B 1 244 ? 36.29   -14.027 27.477  1   34.76 ? 229 VAL   B CG2 1 
ATOM   4709 N  N   . LEU   B 1 245 ? 34.051  -10.721 25.318  1   31.51 ? 230 LEU   B N   1 
ATOM   4710 C  CA  . LEU   B 1 245 ? 33.841  -9.555  24.464  1   32.14 ? 230 LEU   B CA  1 
ATOM   4711 C  C   . LEU   B 1 245 ? 32.985  -8.463  25.099  1   32.76 ? 230 LEU   B C   1 
ATOM   4712 O  O   . LEU   B 1 245 ? 33.302  -7.276  24.963  1   34.57 ? 230 LEU   B O   1 
ATOM   4713 C  CB  . LEU   B 1 245 ? 33.251  -10.008 23.119  1   32.21 ? 230 LEU   B CB  1 
ATOM   4714 C  CG  . LEU   B 1 245 ? 33.24   -8.99   21.997  1   32.91 ? 230 LEU   B CG  1 
ATOM   4715 C  CD1 . LEU   B 1 245 ? 34.608  -8.377  21.78   1   33.27 ? 230 LEU   B CD1 1 
ATOM   4716 C  CD2 . LEU   B 1 245 ? 32.732  -9.645  20.722  1   33.38 ? 230 LEU   B CD2 1 
ATOM   4717 N  N   . ARG   B 1 246 ? 31.917  -8.848  25.807  1   31.07 ? 231 ARG   B N   1 
ATOM   4718 C  CA  . ARG   B 1 246 ? 31.01   -7.915  26.476  1   30.29 ? 231 ARG   B CA  1 
ATOM   4719 C  C   . ARG   B 1 246 ? 31.775  -7.046  27.491  1   30.11 ? 231 ARG   B C   1 
ATOM   4720 O  O   . ARG   B 1 246 ? 31.515  -5.84   27.606  1   28.52 ? 231 ARG   B O   1 
ATOM   4721 C  CB  . ARG   B 1 246 ? 29.9    -8.711  27.17   1   30.42 ? 231 ARG   B CB  1 
ATOM   4722 C  CG  . ARG   B 1 246 ? 28.917  -7.906  28.014  1   32.85 ? 231 ARG   B CG  1 
ATOM   4723 C  CD  . ARG   B 1 246 ? 27.945  -8.851  28.705  1   36.7  ? 231 ARG   B CD  1 
ATOM   4724 N  NE  . ARG   B 1 246 ? 28.636  -9.646  29.722  1   40.2  ? 231 ARG   B NE  1 
ATOM   4725 C  CZ  . ARG   B 1 246 ? 28.628  -9.377  31.022  1   43.07 ? 231 ARG   B CZ  1 
ATOM   4726 N  NH1 . ARG   B 1 246 ? 27.925  -8.355  31.49   1   44.06 ? 231 ARG   B NH1 1 
ATOM   4727 N  NH2 . ARG   B 1 246 ? 29.314  -10.14  31.867  1   42.67 ? 231 ARG   B NH2 1 
ATOM   4728 N  N   . ILE   B 1 247 ? 32.721  -7.66   28.214  1   31.14 ? 232 ILE   B N   1 
ATOM   4729 C  CA  . ILE   B 1 247 ? 33.551  -6.985  29.212  1   32.54 ? 232 ILE   B CA  1 
ATOM   4730 C  C   . ILE   B 1 247 ? 34.391  -5.875  28.576  1   31.97 ? 232 ILE   B C   1 
ATOM   4731 O  O   . ILE   B 1 247 ? 34.423  -4.764  29.103  1   32.46 ? 232 ILE   B O   1 
ATOM   4732 C  CB  . ILE   B 1 247 ? 34.465  -8.025  29.911  1   34.52 ? 232 ILE   B CB  1 
ATOM   4733 C  CG1 . ILE   B 1 247 ? 33.667  -9.071  30.698  1   36.68 ? 232 ILE   B CG1 1 
ATOM   4734 C  CG2 . ILE   B 1 247 ? 35.54   -7.366  30.777  1   35.38 ? 232 ILE   B CG2 1 
ATOM   4735 C  CD1 . ILE   B 1 247 ? 32.593  -8.592  31.605  1   38.22 ? 232 ILE   B CD1 1 
ATOM   4736 N  N   . TYR   B 1 248 ? 35.031  -6.159  27.435  1   30.83 ? 233 TYR   B N   1 
ATOM   4737 C  CA  . TYR   B 1 248 ? 35.926  -5.199  26.773  1   31.58 ? 233 TYR   B CA  1 
ATOM   4738 C  C   . TYR   B 1 248 ? 35.194  -4.04   26.12   1   32.17 ? 233 TYR   B C   1 
ATOM   4739 O  O   . TYR   B 1 248 ? 35.767  -2.958  25.982  1   33.02 ? 233 TYR   B O   1 
ATOM   4740 C  CB  . TYR   B 1 248 ? 36.864  -5.903  25.777  1   31.34 ? 233 TYR   B CB  1 
ATOM   4741 C  CG  . TYR   B 1 248 ? 37.981  -6.63   26.487  1   31.84 ? 233 TYR   B CG  1 
ATOM   4742 C  CD1 . TYR   B 1 248 ? 39.054  -5.936  27.026  1   32.61 ? 233 TYR   B CD1 1 
ATOM   4743 C  CD2 . TYR   B 1 248 ? 37.905  -7.995  26.724  1   32.27 ? 233 TYR   B CD2 1 
ATOM   4744 C  CE1 . TYR   B 1 248 ? 40.06   -6.594  27.721  1   33.21 ? 233 TYR   B CE1 1 
ATOM   4745 C  CE2 . TYR   B 1 248 ? 38.9    -8.663  27.422  1   33.03 ? 233 TYR   B CE2 1 
ATOM   4746 C  CZ  . TYR   B 1 248 ? 39.993  -7.962  27.893  1   34.18 ? 233 TYR   B CZ  1 
ATOM   4747 O  OH  . TYR   B 1 248 ? 40.968  -8.599  28.62   1   36.25 ? 233 TYR   B OH  1 
ATOM   4748 N  N   . LEU   B 1 249 ? 33.923  -4.255  25.725  1   30.93 ? 234 LEU   B N   1 
ATOM   4749 C  CA  . LEU   B 1 249 ? 33.147  -3.18   25.125  1   30.49 ? 234 LEU   B CA  1 
ATOM   4750 C  C   . LEU   B 1 249 ? 32.39   -2.328  26.183  1   30.65 ? 234 LEU   B C   1 
ATOM   4751 O  O   . LEU   B 1 249 ? 31.766  -1.325  25.821  1   29.98 ? 234 LEU   B O   1 
ATOM   4752 C  CB  . LEU   B 1 249 ? 32.209  -3.75   24.079  1   29.66 ? 234 LEU   B CB  1 
ATOM   4753 C  CG  . LEU   B 1 249 ? 32.894  -4.487  22.949  1   30.25 ? 234 LEU   B CG  1 
ATOM   4754 C  CD1 . LEU   B 1 249 ? 31.88   -5.182  22.076  1   30.35 ? 234 LEU   B CD1 1 
ATOM   4755 C  CD2 . LEU   B 1 249 ? 33.762  -3.522  22.123  1   30.74 ? 234 LEU   B CD2 1 
ATOM   4756 N  N   . SER   B 1 250 ? 32.465  -2.698  27.489  1   30.79 ? 235 SER   B N   1 
ATOM   4757 C  CA  . SER   B 1 250 ? 31.804  -1.896  28.525  1   31.89 ? 235 SER   B CA  1 
ATOM   4758 C  C   . SER   B 1 250 ? 32.437  -0.521  28.639  1   33.44 ? 235 SER   B C   1 
ATOM   4759 O  O   . SER   B 1 250 ? 33.641  -0.377  28.435  1   34.48 ? 235 SER   B O   1 
ATOM   4760 C  CB  . SER   B 1 250 ? 31.924  -2.551  29.893  1   33.92 ? 235 SER   B CB  1 
ATOM   4761 O  OG  . SER   B 1 250 ? 31.516  -3.9    29.838  1   37.42 ? 235 SER   B OG  1 
ATOM   4762 N  N   . GLY   B 1 251 ? 31.648  0.449   29.074  1   33.76 ? 236 GLY   B N   1 
ATOM   4763 C  CA  . GLY   B 1 251 ? 32.107  1.812   29.288  1   34.47 ? 236 GLY   B CA  1 
ATOM   4764 C  C   . GLY   B 1 251 ? 32.136  2.186   30.754  1   34.46 ? 236 GLY   B C   1 
ATOM   4765 O  O   . GLY   B 1 251 ? 32.156  1.317   31.634  1   33.4  ? 236 GLY   B O   1 
ATOM   4766 N  N   . TRP   B 1 252 ? 32.177  3.477   31.023  1   34.56 ? 237 TRP   B N   1 
ATOM   4767 C  CA  . TRP   B 1 252 ? 32.26   3.978   32.399  1   36.3  ? 237 TRP   B CA  1 
ATOM   4768 C  C   . TRP   B 1 252 ? 31.201  5.044   32.635  1   38.91 ? 237 TRP   B C   1 
ATOM   4769 O  O   . TRP   B 1 252 ? 31.514  6.161   33.025  1   39.39 ? 237 TRP   B O   1 
ATOM   4770 C  CB  . TRP   B 1 252 ? 33.682  4.485   32.774  1   35.57 ? 237 TRP   B CB  1 
ATOM   4771 C  CG  . TRP   B 1 252 ? 34.513  4.99    31.622  1   34.85 ? 237 TRP   B CG  1 
ATOM   4772 C  CD1 . TRP   B 1 252 ? 34.652  6.287   31.201  1   35.71 ? 237 TRP   B CD1 1 
ATOM   4773 C  CD2 . TRP   B 1 252 ? 35.301  4.19    30.732  1   33.69 ? 237 TRP   B CD2 1 
ATOM   4774 N  NE1 . TRP   B 1 252 ? 35.486  6.338   30.099  1   35.25 ? 237 TRP   B NE1 1 
ATOM   4775 C  CE2 . TRP   B 1 252 ? 35.881  5.061   29.781  1   34.49 ? 237 TRP   B CE2 1 
ATOM   4776 C  CE3 . TRP   B 1 252 ? 35.559  2.815   30.635  1   33.77 ? 237 TRP   B CE3 1 
ATOM   4777 C  CZ2 . TRP   B 1 252 ? 36.695  4.597   28.751  1   34.92 ? 237 TRP   B CZ2 1 
ATOM   4778 C  CZ3 . TRP   B 1 252 ? 36.362  2.361   29.605  1   34.88 ? 237 TRP   B CZ3 1 
ATOM   4779 C  CH2 . TRP   B 1 252 ? 36.903  3.242   28.668  1   35    ? 237 TRP   B CH2 1 
ATOM   4780 N  N   . LYS   B 1 253 ? 29.945  4.706   32.363  1   40.01 ? 238 LYS   B N   1 
ATOM   4781 C  CA  . LYS   B 1 253 ? 28.824  5.61    32.611  1   41.38 ? 238 LYS   B CA  1 
ATOM   4782 C  C   . LYS   B 1 253 ? 27.829  4.797   33.406  1   43.12 ? 238 LYS   B C   1 
ATOM   4783 O  O   . LYS   B 1 253 ? 27.397  3.746   32.938  1   43.28 ? 238 LYS   B O   1 
ATOM   4784 C  CB  . LYS   B 1 253 ? 28.195  6.107   31.312  1   42.21 ? 238 LYS   B CB  1 
ATOM   4785 C  CG  . LYS   B 1 253 ? 27.057  7.083   31.567  1   45.62 ? 238 LYS   B CG  1 
ATOM   4786 C  CD  . LYS   B 1 253 ? 26.851  8.031   30.41   1   50.48 ? 238 LYS   B CD  1 
ATOM   4787 C  CE  . LYS   B 1 253 ? 25.744  9.028   30.693  1   54.59 ? 238 LYS   B CE  1 
ATOM   4788 N  N   . GLY   B 1 254 ? 27.566  5.206   34.644  1   43.96 ? 239 GLY   B N   1 
ATOM   4789 C  CA  . GLY   B 1 254 ? 26.695  4.433   35.521  1   45.17 ? 239 GLY   B CA  1 
ATOM   4790 C  C   . GLY   B 1 254 ? 27.244  3.043   35.804  1   46.27 ? 239 GLY   B C   1 
ATOM   4791 O  O   . GLY   B 1 254 ? 26.474  2.114   36.071  1   46.42 ? 239 GLY   B O   1 
ATOM   4792 N  N   . ASN   B 1 255 ? 28.585  2.882   35.732  1   46.43 ? 240 ASN   B N   1 
ATOM   4793 C  CA  . ASN   B 1 255 ? 29.244  1.606   35.971  1   47.75 ? 240 ASN   B CA  1 
ATOM   4794 C  C   . ASN   B 1 255 ? 29.814  1.614   37.38   1   50.01 ? 240 ASN   B C   1 
ATOM   4795 O  O   . ASN   B 1 255 ? 30.652  2.459   37.705  1   50.4  ? 240 ASN   B O   1 
ATOM   4796 C  CB  . ASN   B 1 255 ? 30.359  1.395   34.959  1   48.1  ? 240 ASN   B CB  1 
ATOM   4797 C  CG  . ASN   B 1 255 ? 30.937  0.004   34.965  1   50.12 ? 240 ASN   B CG  1 
ATOM   4798 O  OD1 . ASN   B 1 255 ? 30.98   -0.668  35.997  1   51.66 ? 240 ASN   B OD1 1 
ATOM   4799 N  ND2 . ASN   B 1 255 ? 31.401  -0.467  33.807  1   49.35 ? 240 ASN   B ND2 1 
ATOM   4800 N  N   . PRO   B 1 256 ? 29.402  0.652   38.222  1   51.03 ? 241 PRO   B N   1 
ATOM   4801 C  CA  . PRO   B 1 256 ? 29.924  0.609   39.599  1   51.46 ? 241 PRO   B CA  1 
ATOM   4802 C  C   . PRO   B 1 256 ? 31.433  0.409   39.683  1   52.39 ? 241 PRO   B C   1 
ATOM   4803 O  O   . PRO   B 1 256 ? 32.027  0.786   40.693  1   52.98 ? 241 PRO   B O   1 
ATOM   4804 C  CB  . PRO   B 1 256 ? 29.188  -0.578  40.229  1   51.98 ? 241 PRO   B CB  1 
ATOM   4805 C  CG  . PRO   B 1 256 ? 27.998  -0.804  39.37   1   52.54 ? 241 PRO   B CG  1 
ATOM   4806 C  CD  . PRO   B 1 256 ? 28.41   -0.412  37.981  1   50.83 ? 241 PRO   B CD  1 
ATOM   4807 N  N   . GLN   B 1 257 ? 32.055  -0.189  38.648  1   52.26 ? 242 GLN   B N   1 
ATOM   4808 C  CA  . GLN   B 1 257 ? 33.5    -0.426  38.642  1   52.64 ? 242 GLN   B CA  1 
ATOM   4809 C  C   . GLN   B 1 257 ? 34.314  0.852   38.453  1   52.93 ? 242 GLN   B C   1 
ATOM   4810 O  O   . GLN   B 1 257 ? 35.491  0.862   38.794  1   52.9  ? 242 GLN   B O   1 
ATOM   4811 C  CB  . GLN   B 1 257 ? 33.887  -1.469  37.592  1   54.51 ? 242 GLN   B CB  1 
ATOM   4812 C  CG  . GLN   B 1 257 ? 33.351  -2.854  37.881  1   58.74 ? 242 GLN   B CG  1 
ATOM   4813 C  CD  . GLN   B 1 257 ? 33.705  -3.813  36.773  1   63.96 ? 242 GLN   B CD  1 
ATOM   4814 O  OE1 . GLN   B 1 257 ? 33.545  -3.523  35.591  1   66.16 ? 242 GLN   B OE1 1 
ATOM   4815 N  NE2 . GLN   B 1 257 ? 34.188  -4.985  37.128  1   64.53 ? 242 GLN   B NE2 1 
ATOM   4816 N  N   . LEU   B 1 258 ? 33.713  1.913   37.877  1   52.88 ? 243 LEU   B N   1 
ATOM   4817 C  CA  . LEU   B 1 258 ? 34.361  3.213   37.677  1   53.55 ? 243 LEU   B CA  1 
ATOM   4818 C  C   . LEU   B 1 258 ? 33.277  4.257   37.932  1   53.92 ? 243 LEU   B C   1 
ATOM   4819 O  O   . LEU   B 1 258 ? 32.891  5.009   37.031  1   53.84 ? 243 LEU   B O   1 
ATOM   4820 C  CB  . LEU   B 1 258 ? 34.919  3.354   36.245  1   54.26 ? 243 LEU   B CB  1 
ATOM   4821 C  CG  . LEU   B 1 258 ? 36.261  2.703   35.967  1   56.57 ? 243 LEU   B CG  1 
ATOM   4822 C  CD1 . LEU   B 1 258 ? 36.064  1.377   35.292  1   57.46 ? 243 LEU   B CD1 1 
ATOM   4823 C  CD2 . LEU   B 1 258 ? 37.104  3.576   35.048  1   57.52 ? 243 LEU   B CD2 1 
ATOM   4824 N  N   . SER   B 1 259 ? 32.752  4.259   39.164  1   54.14 ? 244 SER   B N   1 
ATOM   4825 C  CA  . SER   B 1 259 ? 31.621  5.078   39.609  1   55.08 ? 244 SER   B CA  1 
ATOM   4826 C  C   . SER   B 1 259 ? 31.683  6.572   39.235  1   54.83 ? 244 SER   B C   1 
ATOM   4827 O  O   . SER   B 1 259 ? 30.633  7.188   39.071  1   54.96 ? 244 SER   B O   1 
ATOM   4828 C  CB  . SER   B 1 259 ? 31.391  4.918   41.112  1   57.23 ? 244 SER   B CB  1 
ATOM   4829 O  OG  . SER   B 1 259 ? 32.453  5.473   41.875  1   60.21 ? 244 SER   B OG  1 
ATOM   4830 N  N   . ASP   B 1 260 ? 32.878  7.145   39.085  1   54.54 ? 245 ASP   B N   1 
ATOM   4831 C  CA  . ASP   B 1 260 ? 32.994  8.564   38.719  1   54.47 ? 245 ASP   B CA  1 
ATOM   4832 C  C   . ASP   B 1 260 ? 33.475  8.821   37.284  1   52.86 ? 245 ASP   B C   1 
ATOM   4833 O  O   . ASP   B 1 260 ? 33.568  9.974   36.855  1   52.53 ? 245 ASP   B O   1 
ATOM   4834 C  CB  . ASP   B 1 260 ? 33.883  9.295   39.73   1   57.61 ? 245 ASP   B CB  1 
ATOM   4835 C  CG  . ASP   B 1 260 ? 33.356  9.136   41.141  1   65.67 ? 245 ASP   B CG  1 
ATOM   4836 O  OD1 . ASP   B 1 260 ? 32.278  9.709   41.44   1   66.68 ? 245 ASP   B OD1 1 
ATOM   4837 O  OD2 . ASP   B 1 260 ? 34.002  8.406   41.942  1   69.48 ? 245 ASP   B OD2 1 
ATOM   4838 N  N   . GLY   B 1 261 ? 33.745  7.756   36.547  1   51.26 ? 246 GLY   B N   1 
ATOM   4839 C  CA  . GLY   B 1 261 ? 34.256  7.876   35.197  1   50.11 ? 246 GLY   B CA  1 
ATOM   4840 C  C   . GLY   B 1 261 ? 35.734  7.571   35.158  1   48.67 ? 246 GLY   B C   1 
ATOM   4841 O  O   . GLY   B 1 261 ? 36.295  7.012   36.105  1   48.68 ? 246 GLY   B O   1 
ATOM   4842 N  N   . LEU   B 1 262 ? 36.371  7.933   34.058  1   47.3  ? 247 LEU   B N   1 
ATOM   4843 C  CA  . LEU   B 1 262 ? 37.782  7.684   33.85   1   47.12 ? 247 LEU   B CA  1 
ATOM   4844 C  C   . LEU   B 1 262 ? 38.505  9.006   33.872  1   47.24 ? 247 LEU   B C   1 
ATOM   4845 O  O   . LEU   B 1 262 ? 37.984  9.991   33.342  1   46.99 ? 247 LEU   B O   1 
ATOM   4846 C  CB  . LEU   B 1 262 ? 37.963  7.033   32.466  1   46.87 ? 247 LEU   B CB  1 
ATOM   4847 C  CG  . LEU   B 1 262 ? 39.356  6.538   32.105  1   47.65 ? 247 LEU   B CG  1 
ATOM   4848 C  CD1 . LEU   B 1 262 ? 39.761  5.377   32.998  1   47.88 ? 247 LEU   B CD1 1 
ATOM   4849 C  CD2 . LEU   B 1 262 ? 39.425  6.127   30.629  1   47.75 ? 247 LEU   B CD2 1 
ATOM   4850 N  N   . VAL   B 1 263 ? 39.701  9.04    34.479  1   47.24 ? 248 VAL   B N   1 
ATOM   4851 C  CA  . VAL   B 1 263 ? 40.494  10.259  34.457  1   47.52 ? 248 VAL   B CA  1 
ATOM   4852 C  C   . VAL   B 1 263 ? 41.282  10.242  33.166  1   47.61 ? 248 VAL   B C   1 
ATOM   4853 O  O   . VAL   B 1 263 ? 42.003  9.293   32.904  1   47.7  ? 248 VAL   B O   1 
ATOM   4854 C  CB  . VAL   B 1 263 ? 41.409  10.419  35.692  1   48.25 ? 248 VAL   B CB  1 
ATOM   4855 C  CG1 . VAL   B 1 263 ? 42.264  11.676  35.578  1   48.67 ? 248 VAL   B CG1 1 
ATOM   4856 C  CG2 . VAL   B 1 263 ? 40.592  10.436  36.979  1   48.6  ? 248 VAL   B CG2 1 
ATOM   4857 N  N   . TYR   B 1 264 ? 41.094  11.244  32.323  1   47.75 ? 249 TYR   B N   1 
ATOM   4858 C  CA  . TYR   B 1 264 ? 41.844  11.37   31.08   1   48.63 ? 249 TYR   B CA  1 
ATOM   4859 C  C   . TYR   B 1 264 ? 42.977  12.337  31.424  1   50.33 ? 249 TYR   B C   1 
ATOM   4860 O  O   . TYR   B 1 264 ? 42.851  13.553  31.242  1   49.66 ? 249 TYR   B O   1 
ATOM   4861 C  CB  . TYR   B 1 264 ? 40.95   11.944  29.976  1   48.22 ? 249 TYR   B CB  1 
ATOM   4862 C  CG  . TYR   B 1 264 ? 39.909  10.957  29.496  1   47.83 ? 249 TYR   B CG  1 
ATOM   4863 C  CD1 . TYR   B 1 264 ? 38.717  10.785  30.183  1   48.24 ? 249 TYR   B CD1 1 
ATOM   4864 C  CD2 . TYR   B 1 264 ? 40.137  10.163  28.383  1   48.3  ? 249 TYR   B CD2 1 
ATOM   4865 C  CE1 . TYR   B 1 264 ? 37.773  9.855   29.77   1   49.01 ? 249 TYR   B CE1 1 
ATOM   4866 C  CE2 . TYR   B 1 264 ? 39.201  9.231   27.959  1   49.04 ? 249 TYR   B CE2 1 
ATOM   4867 C  CZ  . TYR   B 1 264 ? 38.007  9.097   28.639  1   50.09 ? 249 TYR   B CZ  1 
ATOM   4868 O  OH  . TYR   B 1 264 ? 37.068  8.185   28.2    1   51.88 ? 249 TYR   B OH  1 
ATOM   4869 N  N   . GLU   B 1 265 ? 44.035  11.782  32.037  1   51.8  ? 250 GLU   B N   1 
ATOM   4870 C  CA  . GLU   B 1 265 ? 45.182  12.524  32.546  1   53.27 ? 250 GLU   B CA  1 
ATOM   4871 C  C   . GLU   B 1 265 ? 45.784  13.481  31.538  1   54.01 ? 250 GLU   B C   1 
ATOM   4872 O  O   . GLU   B 1 265 ? 46.061  13.089  30.409  1   54.02 ? 250 GLU   B O   1 
ATOM   4873 C  CB  . GLU   B 1 265 ? 46.234  11.551  33.05   1   56.34 ? 250 GLU   B CB  1 
ATOM   4874 C  CG  . GLU   B 1 265 ? 47.403  12.208  33.757  1   62.15 ? 250 GLU   B CG  1 
ATOM   4875 C  CD  . GLU   B 1 265 ? 48.395  11.161  34.211  1   67.45 ? 250 GLU   B CD  1 
ATOM   4876 O  OE1 . GLU   B 1 265 ? 49.077  10.576  33.338  1   67.53 ? 250 GLU   B OE1 1 
ATOM   4877 O  OE2 . GLU   B 1 265 ? 48.465  10.898  35.433  1   70.2  ? 250 GLU   B OE2 1 
ATOM   4878 N  N   . GLY   B 1 266 ? 45.93   14.74   31.935  1   54.45 ? 251 GLY   B N   1 
ATOM   4879 C  CA  . GLY   B 1 266 ? 46.513  15.755  31.07   1   55.28 ? 251 GLY   B CA  1 
ATOM   4880 C  C   . GLY   B 1 266 ? 45.542  16.454  30.14   1   56.32 ? 251 GLY   B C   1 
ATOM   4881 O  O   . GLY   B 1 266 ? 45.927  17.407  29.453  1   56.48 ? 251 GLY   B O   1 
ATOM   4882 N  N   . PHE   B 1 267 ? 44.272  15.988  30.085  1   56.39 ? 252 PHE   B N   1 
ATOM   4883 C  CA  . PHE   B 1 267 ? 43.274  16.617  29.222  1   56.51 ? 252 PHE   B CA  1 
ATOM   4884 C  C   . PHE   B 1 267 ? 42.172  17.273  30.047  1   57.01 ? 252 PHE   B C   1 
ATOM   4885 O  O   . PHE   B 1 267 ? 41.844  18.43   29.805  1   57.57 ? 252 PHE   B O   1 
ATOM   4886 C  CB  . PHE   B 1 267 ? 42.707  15.633  28.199  1   55.98 ? 252 PHE   B CB  1 
ATOM   4887 C  CG  . PHE   B 1 267 ? 42.116  16.342  27.004  1   55.99 ? 252 PHE   B CG  1 
ATOM   4888 C  CD1 . PHE   B 1 267 ? 42.909  16.707  25.93   1   56.26 ? 252 PHE   B CD1 1 
ATOM   4889 C  CD2 . PHE   B 1 267 ? 40.771  16.656  26.962  1   56.24 ? 252 PHE   B CD2 1 
ATOM   4890 C  CE1 . PHE   B 1 267 ? 42.364  17.356  24.833  1   56.64 ? 252 PHE   B CE1 1 
ATOM   4891 C  CE2 . PHE   B 1 267 ? 40.229  17.305  25.861  1   56.65 ? 252 PHE   B CE2 1 
ATOM   4892 C  CZ  . PHE   B 1 267 ? 41.029  17.651  24.804  1   56.4  ? 252 PHE   B CZ  1 
ATOM   4893 N  N   . TRP   B 1 268 ? 41.609  16.545  31.019  1   56.84 ? 253 TRP   B N   1 
ATOM   4894 C  CA  . TRP   B 1 268 ? 40.59   17.068  31.932  1   57.46 ? 253 TRP   B CA  1 
ATOM   4895 C  C   . TRP   B 1 268 ? 41.048  16.705  33.344  1   58.32 ? 253 TRP   B C   1 
ATOM   4896 O  O   . TRP   B 1 268 ? 41.618  15.626  33.548  1   58.4  ? 253 TRP   B O   1 
ATOM   4897 C  CB  . TRP   B 1 268 ? 39.186  16.455  31.677  1   57.29 ? 253 TRP   B CB  1 
ATOM   4898 C  CG  . TRP   B 1 268 ? 38.557  16.795  30.359  1   57.68 ? 253 TRP   B CG  1 
ATOM   4899 C  CD1 . TRP   B 1 268 ? 38.232  18.04   29.903  1   58.56 ? 253 TRP   B CD1 1 
ATOM   4900 C  CD2 . TRP   B 1 268 ? 38.089  15.867  29.364  1   57.74 ? 253 TRP   B CD2 1 
ATOM   4901 N  NE1 . TRP   B 1 268 ? 37.641  17.951  28.659  1   58.74 ? 253 TRP   B NE1 1 
ATOM   4902 C  CE2 . TRP   B 1 268 ? 37.535  16.628  28.308  1   58.57 ? 253 TRP   B CE2 1 
ATOM   4903 C  CE3 . TRP   B 1 268 ? 38.103  14.47   29.25   1   57.76 ? 253 TRP   B CE3 1 
ATOM   4904 C  CZ2 . TRP   B 1 268 ? 37.031  16.036  27.148  1   59.08 ? 253 TRP   B CZ2 1 
ATOM   4905 C  CZ3 . TRP   B 1 268 ? 37.594  13.889  28.105  1   58.65 ? 253 TRP   B CZ3 1 
ATOM   4906 C  CH2 . TRP   B 1 268 ? 37.072  14.666  27.068  1   58.97 ? 253 TRP   B CH2 1 
ATOM   4907 N  N   . GLU   B 1 269 ? 40.782  17.571  34.323  1   58.84 ? 254 GLU   B N   1 
ATOM   4908 C  CA  . GLU   B 1 269 ? 41.192  17.294  35.703  1   59.99 ? 254 GLU   B CA  1 
ATOM   4909 C  C   . GLU   B 1 269 ? 40.273  16.289  36.377  1   60.54 ? 254 GLU   B C   1 
ATOM   4910 O  O   . GLU   B 1 269 ? 40.739  15.411  37.102  1   60.8  ? 254 GLU   B O   1 
ATOM   4911 C  CB  . GLU   B 1 269 ? 41.257  18.586  36.535  1   62.47 ? 254 GLU   B CB  1 
ATOM   4912 N  N   . ASP   B 1 270 ? 38.961  16.436  36.157  1   60.33 ? 255 ASP   B N   1 
ATOM   4913 C  CA  . ASP   B 1 270 ? 37.929  15.594  36.764  1   60.22 ? 255 ASP   B CA  1 
ATOM   4914 C  C   . ASP   B 1 270 ? 37.635  14.354  35.915  1   58.42 ? 255 ASP   B C   1 
ATOM   4915 O  O   . ASP   B 1 270 ? 37.714  14.419  34.686  1   58.36 ? 255 ASP   B O   1 
ATOM   4916 C  CB  . ASP   B 1 270 ? 36.641  16.419  36.948  1   63.52 ? 255 ASP   B CB  1 
ATOM   4917 C  CG  . ASP   B 1 270 ? 36.87   17.782  37.602  1   71.05 ? 255 ASP   B CG  1 
ATOM   4918 O  OD1 . ASP   B 1 270 ? 37.383  17.812  38.752  1   71.82 ? 255 ASP   B OD1 1 
ATOM   4919 O  OD2 . ASP   B 1 270 ? 36.54   18.823  36.957  1   74.24 ? 255 ASP   B OD2 1 
ATOM   4920 N  N   . PRO   B 1 271 ? 37.285  13.217  36.542  1   56.74 ? 256 PRO   B N   1 
ATOM   4921 C  CA  . PRO   B 1 271 ? 36.96   12.021  35.743  1   55.79 ? 256 PRO   B CA  1 
ATOM   4922 C  C   . PRO   B 1 271 ? 35.673  12.218  34.935  1   54.41 ? 256 PRO   B C   1 
ATOM   4923 O  O   . PRO   B 1 271 ? 34.763  12.923  35.372  1   54.86 ? 256 PRO   B O   1 
ATOM   4924 C  CB  . PRO   B 1 271 ? 36.839  10.907  36.788  1   56.52 ? 256 PRO   B CB  1 
ATOM   4925 C  CG  . PRO   B 1 271 ? 36.507  11.614  38.063  1   57.05 ? 256 PRO   B CG  1 
ATOM   4926 C  CD  . PRO   B 1 271 ? 37.14   12.973  37.991  1   55.87 ? 256 PRO   B CD  1 
ATOM   4927 N  N   . LYS   B 1 272 ? 35.622  11.653  33.727  1   52.64 ? 257 LYS   B N   1 
ATOM   4928 C  CA  . LYS   B 1 272 ? 34.455  11.804  32.854  1   50.9  ? 257 LYS   B CA  1 
ATOM   4929 C  C   . LYS   B 1 272 ? 33.819  10.454  32.539  1   48.78 ? 257 LYS   B C   1 
ATOM   4930 O  O   . LYS   B 1 272 ? 34.529  9.486   32.261  1   48.61 ? 257 LYS   B O   1 
ATOM   4931 C  CB  . LYS   B 1 272 ? 34.86   12.492  31.544  1   52.35 ? 257 LYS   B CB  1 
ATOM   4932 C  CG  . LYS   B 1 272 ? 35.521  13.847  31.738  1   55.95 ? 257 LYS   B CG  1 
ATOM   4933 N  N   . GLU   B 1 273 ? 32.485  10.409  32.544  1   46.76 ? 258 GLU   B N   1 
ATOM   4934 C  CA  . GLU   B 1 273 ? 31.711  9.213   32.246  1   45.21 ? 258 GLU   B CA  1 
ATOM   4935 C  C   . GLU   B 1 273 ? 31.316  9.15    30.778  1   42.9  ? 258 GLU   B C   1 
ATOM   4936 O  O   . GLU   B 1 273 ? 30.776  10.122  30.258  1   43.09 ? 258 GLU   B O   1 
ATOM   4937 C  CB  . GLU   B 1 273 ? 30.43   9.204   33.082  1   48.1  ? 258 GLU   B CB  1 
ATOM   4938 C  CG  . GLU   B 1 273 ? 30.627  8.781   34.523  1   53.18 ? 258 GLU   B CG  1 
ATOM   4939 C  CD  . GLU   B 1 273 ? 29.316  8.627   35.266  1   60.56 ? 258 GLU   B CD  1 
ATOM   4940 O  OE1 . GLU   B 1 273 ? 28.643  9.658   35.493  1   61.72 ? 258 GLU   B OE1 1 
ATOM   4941 O  OE2 . GLU   B 1 273 ? 28.955  7.478   35.609  1   63.1  ? 258 GLU   B OE2 1 
ATOM   4942 N  N   . PHE   B 1 274 ? 31.578  8.011   30.11   1   40.6  ? 259 PHE   B N   1 
ATOM   4943 C  CA  . PHE   B 1 274 ? 31.182  7.787   28.716  1   38.87 ? 259 PHE   B CA  1 
ATOM   4944 C  C   . PHE   B 1 274 ? 30.622  6.374   28.586  1   37.66 ? 259 PHE   B C   1 
ATOM   4945 O  O   . PHE   B 1 274 ? 31.173  5.443   29.177  1   38.05 ? 259 PHE   B O   1 
ATOM   4946 C  CB  . PHE   B 1 274 ? 32.341  7.991   27.733  1   38.8  ? 259 PHE   B CB  1 
ATOM   4947 C  CG  . PHE   B 1 274 ? 32.833  9.412   27.647  1   39.88 ? 259 PHE   B CG  1 
ATOM   4948 C  CD1 . PHE   B 1 274 ? 32.068  10.391  27.042  1   40.61 ? 259 PHE   B CD1 1 
ATOM   4949 C  CD2 . PHE   B 1 274 ? 34.053  9.775   28.197  1   40.66 ? 259 PHE   B CD2 1 
ATOM   4950 C  CE1 . PHE   B 1 274 ? 32.524  11.701  26.964  1   41.4  ? 259 PHE   B CE1 1 
ATOM   4951 C  CE2 . PHE   B 1 274 ? 34.504  11.086  28.122  1   41.21 ? 259 PHE   B CE2 1 
ATOM   4952 C  CZ  . PHE   B 1 274 ? 33.73   12.045  27.519  1   41.1  ? 259 PHE   B CZ  1 
ATOM   4953 N  N   . ALA   B 1 275 ? 29.499  6.215   27.866  1   35.97 ? 260 ALA   B N   1 
ATOM   4954 C  CA  . ALA   B 1 275 ? 28.886  4.905   27.677  1   34.89 ? 260 ALA   B CA  1 
ATOM   4955 C  C   . ALA   B 1 275 ? 29.765  4.039   26.761  1   33.7  ? 260 ALA   B C   1 
ATOM   4956 O  O   . ALA   B 1 275 ? 30.444  4.57    25.868  1   34.2  ? 260 ALA   B O   1 
ATOM   4957 C  CB  . ALA   B 1 275 ? 27.506  5.072   27.064  1   34.59 ? 260 ALA   B CB  1 
ATOM   4958 N  N   . GLY   B 1 276 ? 29.72   2.722   26.948  1   31.64 ? 261 GLY   B N   1 
ATOM   4959 C  CA  . GLY   B 1 276 ? 30.525  1.825   26.128  1   30.54 ? 261 GLY   B CA  1 
ATOM   4960 C  C   . GLY   B 1 276 ? 29.99   1.655   24.728  1   29.96 ? 261 GLY   B C   1 
ATOM   4961 O  O   . GLY   B 1 276 ? 28.862  2.081   24.436  1   30.81 ? 261 GLY   B O   1 
ATOM   4962 N  N   . GLY   B 1 277 ? 30.787  1.014   23.856  1   27.59 ? 262 GLY   B N   1 
ATOM   4963 C  CA  . GLY   B 1 277 ? 30.432  0.761   22.454  1   27.18 ? 262 GLY   B CA  1 
ATOM   4964 C  C   . GLY   B 1 277 ? 29.087  0.066   22.357  1   27.87 ? 262 GLY   B C   1 
ATOM   4965 O  O   . GLY   B 1 277 ? 28.837  -0.869  23.117  1   29.17 ? 262 GLY   B O   1 
ATOM   4966 N  N   . SER   B 1 278 ? 28.184  0.584   21.52   1   26.29 ? 263 SER   B N   1 
ATOM   4967 C  CA  . SER   B 1 278 ? 26.835  0.06    21.447  1   26.14 ? 263 SER   B CA  1 
ATOM   4968 C  C   . SER   B 1 278 ? 26.208  0.246   20.1    1   26.98 ? 263 SER   B C   1 
ATOM   4969 O  O   . SER   B 1 278 ? 26.295  1.341   19.533  1   26.77 ? 263 SER   B O   1 
ATOM   4970 C  CB  . SER   B 1 278 ? 25.968  0.77    22.48   1   26.92 ? 263 SER   B CB  1 
ATOM   4971 O  OG  . SER   B 1 278 ? 24.585  0.442   22.408  1   29.24 ? 263 SER   B OG  1 
ATOM   4972 N  N   . ALA   B 1 279 ? 25.427  -0.749  19.645  1   27.6  ? 264 ALA   B N   1 
ATOM   4973 C  CA  . ALA   B 1 279 ? 24.68   -0.596  18.402  1   28.04 ? 264 ALA   B CA  1 
ATOM   4974 C  C   . ALA   B 1 279 ? 23.525  0.428   18.521  1   27.96 ? 264 ALA   B C   1 
ATOM   4975 O  O   . ALA   B 1 279 ? 22.957  0.826   17.503  1   26.73 ? 264 ALA   B O   1 
ATOM   4976 C  CB  . ALA   B 1 279 ? 24.197  -1.931  17.897  1   27.95 ? 264 ALA   B CB  1 
ATOM   4977 N  N   . GLY   B 1 280 ? 23.251  0.914   19.739  1   27.94 ? 265 GLY   B N   1 
ATOM   4978 C  CA  . GLY   B 1 280 ? 22.35   2.023   19.971  1   29.24 ? 265 GLY   B CA  1 
ATOM   4979 C  C   . GLY   B 1 280 ? 22.939  3.309   19.387  1   30.08 ? 265 GLY   B C   1 
ATOM   4980 O  O   . GLY   B 1 280 ? 22.208  4.264   19.171  1   29.48 ? 265 GLY   B O   1 
ATOM   4981 N  N   . GLN   B 1 281 ? 24.273  3.335   19.124  1   30.39 ? 266 GLN   B N   1 
ATOM   4982 C  CA  . GLN   B 1 281 ? 25.033  4.383   18.447  1   29.89 ? 266 GLN   B CA  1 
ATOM   4983 C  C   . GLN   B 1 281 ? 24.947  4.234   16.919  1   30.12 ? 266 GLN   B C   1 
ATOM   4984 O  O   . GLN   B 1 281 ? 25.337  5.153   16.224  1   30.45 ? 266 GLN   B O   1 
ATOM   4985 C  CB  . GLN   B 1 281 ? 26.506  4.332   18.885  1   30.2  ? 266 GLN   B CB  1 
ATOM   4986 C  CG  . GLN   B 1 281 ? 26.643  4.47    20.398  1   29.67 ? 266 GLN   B CG  1 
ATOM   4987 C  CD  . GLN   B 1 281 ? 27.996  4.074   20.915  1   31.7  ? 266 GLN   B CD  1 
ATOM   4988 O  OE1 . GLN   B 1 281 ? 28.763  3.356   20.257  1   31.75 ? 266 GLN   B OE1 1 
ATOM   4989 N  NE2 . GLN   B 1 281 ? 28.275  4.452   22.157  1   31.09 ? 266 GLN   B NE2 1 
ATOM   4990 N  N   . SER   B 1 282 ? 24.486  3.088   16.399  1   29.49 ? 267 SER   B N   1 
ATOM   4991 C  CA  . SER   B 1 282 ? 24.393  2.845   14.957  1   30.14 ? 267 SER   B CA  1 
ATOM   4992 C  C   . SER   B 1 282 ? 23.281  3.664   14.296  1   31.35 ? 267 SER   B C   1 
ATOM   4993 O  O   . SER   B 1 282 ? 22.352  4.158   14.96   1   31.04 ? 267 SER   B O   1 
ATOM   4994 C  CB  . SER   B 1 282 ? 24.18   1.36    14.673  1   30.5  ? 267 SER   B CB  1 
ATOM   4995 O  OG  . SER   B 1 282 ? 22.916  0.885   15.117  1   32.14 ? 267 SER   B OG  1 
ATOM   4996 N  N   . SER   B 1 283 ? 23.442  3.915   13.002  1   32.33 ? 268 SER   B N   1 
ATOM   4997 C  CA  . SER   B 1 283 ? 22.497  4.669   12.185  1   33.72 ? 268 SER   B CA  1 
ATOM   4998 C  C   . SER   B 1 283 ? 21.66   3.739   11.283  1   34.67 ? 268 SER   B C   1 
ATOM   4999 O  O   . SER   B 1 283 ? 20.686  4.203   10.7    1   35.3  ? 268 SER   B O   1 
ATOM   5000 C  CB  . SER   B 1 283 ? 23.263  5.613   11.254  1   36.36 ? 268 SER   B CB  1 
ATOM   5001 O  OG  . SER   B 1 283 ? 24.09   6.539   11.942  1   39.83 ? 268 SER   B OG  1 
ATOM   5002 N  N   . VAL   B 1 284 ? 22.058  2.462   11.129  1   33.83 ? 269 VAL   B N   1 
ATOM   5003 C  CA  . VAL   B 1 284 ? 21.496  1.493   10.21   1   33.56 ? 269 VAL   B CA  1 
ATOM   5004 C  C   . VAL   B 1 284 ? 19.983  1.331   10.303  1   33.18 ? 269 VAL   B C   1 
ATOM   5005 O  O   . VAL   B 1 284 ? 19.341  1.477   9.273   1   33.76 ? 269 VAL   B O   1 
ATOM   5006 C  CB  . VAL   B 1 284 ? 22.215  0.131   10.272  1   34.68 ? 269 VAL   B CB  1 
ATOM   5007 C  CG1 . VAL   B 1 284 ? 21.952  -0.615  11.581  1   35.26 ? 269 VAL   B CG1 1 
ATOM   5008 C  CG2 . VAL   B 1 284 ? 21.856  -0.731  9.07    1   35.64 ? 269 VAL   B CG2 1 
ATOM   5009 N  N   . PHE   B 1 285 ? 19.412  1.019   11.468  1   32.59 ? 270 PHE   B N   1 
ATOM   5010 C  CA  . PHE   B 1 285 ? 17.95   0.874   11.589  1   33.04 ? 270 PHE   B CA  1 
ATOM   5011 C  C   . PHE   B 1 285 ? 17.309  2.251   11.912  1   32.3  ? 270 PHE   B C   1 
ATOM   5012 O  O   . PHE   B 1 285 ? 16.179  2.513   11.504  1   32.51 ? 270 PHE   B O   1 
ATOM   5013 C  CB  . PHE   B 1 285 ? 17.574  -0.153  12.676  1   33.27 ? 270 PHE   B CB  1 
ATOM   5014 C  CG  . PHE   B 1 285 ? 17.88   -1.623  12.405  1   34.71 ? 270 PHE   B CG  1 
ATOM   5015 C  CD1 . PHE   B 1 285 ? 18.347  -2.041  11.169  1   35.98 ? 270 PHE   B CD1 1 
ATOM   5016 C  CD2 . PHE   B 1 285 ? 17.699  -2.578  13.391  1   35.35 ? 270 PHE   B CD2 1 
ATOM   5017 C  CE1 . PHE   B 1 285 ? 18.661  -3.38   10.941  1   36.76 ? 270 PHE   B CE1 1 
ATOM   5018 C  CE2 . PHE   B 1 285 ? 18.046  -3.908  13.174  1   35.79 ? 270 PHE   B CE2 1 
ATOM   5019 C  CZ  . PHE   B 1 285 ? 18.496  -4.308  11.942  1   36.08 ? 270 PHE   B CZ  1 
ATOM   5020 N  N   . GLN   B 1 286 ? 18.031  3.105   12.656  1   31.36 ? 271 GLN   B N   1 
ATOM   5021 C  CA  . GLN   B 1 286 ? 17.613  4.444   13.038  1   31.05 ? 271 GLN   B CA  1 
ATOM   5022 C  C   . GLN   B 1 286 ? 17.208  5.335   11.841  1   31.72 ? 271 GLN   B C   1 
ATOM   5023 O  O   . GLN   B 1 286 ? 16.184  6.017   11.938  1   31.53 ? 271 GLN   B O   1 
ATOM   5024 C  CB  . GLN   B 1 286 ? 18.678  5.105   13.901  1   32.11 ? 271 GLN   B CB  1 
ATOM   5025 C  CG  . GLN   B 1 286 ? 18.269  6.466   14.447  1   35.41 ? 271 GLN   B CG  1 
ATOM   5026 C  CD  . GLN   B 1 286 ? 18.962  6.867   15.74   1   37.52 ? 271 GLN   B CD  1 
ATOM   5027 O  OE1 . GLN   B 1 286 ? 18.557  7.825   16.393  1   38.96 ? 271 GLN   B OE1 1 
ATOM   5028 N  NE2 . GLN   B 1 286 ? 20.021  6.166   16.144  1   36.64 ? 271 GLN   B NE2 1 
ATOM   5029 N  N   . CYS   B 1 287 ? 17.926  5.258   10.696  1   31.64 ? 272 CYS   B N   1 
ATOM   5030 C  CA  . CYS   B 1 287 ? 17.529  6.054   9.541   1   32.46 ? 272 CYS   B CA  1 
ATOM   5031 C  C   . CYS   B 1 287 ? 16.197  5.591   8.938   1   32.4  ? 272 CYS   B C   1 
ATOM   5032 O  O   . CYS   B 1 287 ? 15.516  6.405   8.314   1   32.29 ? 272 CYS   B O   1 
ATOM   5033 C  CB  . CYS   B 1 287 ? 18.634  6.141   8.496   1   34.44 ? 272 CYS   B CB  1 
ATOM   5034 S  SG  . CYS   B 1 287 ? 18.862  4.629   7.548   1   40.23 ? 272 CYS   B SG  1 
ATOM   5035 N  N   . PHE   B 1 288 ? 15.832  4.309   9.119   1   32.34 ? 273 PHE   B N   1 
ATOM   5036 C  CA  . PHE   B 1 288 ? 14.55   3.776   8.688   1   32.63 ? 273 PHE   B CA  1 
ATOM   5037 C  C   . PHE   B 1 288 ? 13.451  4.162   9.676   1   33.61 ? 273 PHE   B C   1 
ATOM   5038 O  O   . PHE   B 1 288 ? 12.356  4.495   9.253   1   34.33 ? 273 PHE   B O   1 
ATOM   5039 C  CB  . PHE   B 1 288 ? 14.617  2.277   8.39    1   32.43 ? 273 PHE   B CB  1 
ATOM   5040 C  CG  . PHE   B 1 288 ? 15.5    2.061   7.177   1   32.52 ? 273 PHE   B CG  1 
ATOM   5041 C  CD1 . PHE   B 1 288 ? 15.11   2.512   5.93    1   33.51 ? 273 PHE   B CD1 1 
ATOM   5042 C  CD2 . PHE   B 1 288 ? 16.748  1.476   7.304   1   32.91 ? 273 PHE   B CD2 1 
ATOM   5043 C  CE1 . PHE   B 1 288 ? 15.939  2.353   4.823   1   34.25 ? 273 PHE   B CE1 1 
ATOM   5044 C  CE2 . PHE   B 1 288 ? 17.585  1.33    6.202   1   33.84 ? 273 PHE   B CE2 1 
ATOM   5045 C  CZ  . PHE   B 1 288 ? 17.179  1.785   4.966   1   33.75 ? 273 PHE   B CZ  1 
ATOM   5046 N  N   . ASP   B 1 289 ? 13.76   4.255   10.976  1   33.73 ? 274 ASP   B N   1 
ATOM   5047 C  CA  . ASP   B 1 289 ? 12.823  4.764   11.956  1   34.13 ? 274 ASP   B CA  1 
ATOM   5048 C  C   . ASP   B 1 289 ? 12.511  6.249   11.625  1   34.71 ? 274 ASP   B C   1 
ATOM   5049 O  O   . ASP   B 1 289 ? 11.351  6.66    11.669  1   34.65 ? 274 ASP   B O   1 
ATOM   5050 C  CB  . ASP   B 1 289 ? 13.416  4.668   13.364  1   36.31 ? 274 ASP   B CB  1 
ATOM   5051 C  CG  . ASP   B 1 289 ? 13.51   3.256   13.913  1   41.35 ? 274 ASP   B CG  1 
ATOM   5052 O  OD1 . ASP   B 1 289 ? 12.492  2.541   13.882  1   42.73 ? 274 ASP   B OD1 1 
ATOM   5053 O  OD2 . ASP   B 1 289 ? 14.593  2.886   14.428  1   44.27 ? 274 ASP   B OD2 1 
ATOM   5054 N  N   . VAL   B 1 290 ? 13.541  7.032   11.253  1   34    ? 275 VAL   B N   1 
ATOM   5055 C  CA  . VAL   B 1 290 ? 13.335  8.431   10.917  1   33.91 ? 275 VAL   B CA  1 
ATOM   5056 C  C   . VAL   B 1 290 ? 12.585  8.534   9.593   1   34.81 ? 275 VAL   B C   1 
ATOM   5057 O  O   . VAL   B 1 290 ? 11.57   9.216   9.535   1   35.26 ? 275 VAL   B O   1 
ATOM   5058 C  CB  . VAL   B 1 290 ? 14.631  9.256   10.953  1   34.47 ? 275 VAL   B CB  1 
ATOM   5059 C  CG1 . VAL   B 1 290 ? 14.372  10.681  10.497  1   35.57 ? 275 VAL   B CG1 1 
ATOM   5060 C  CG2 . VAL   B 1 290 ? 15.239  9.249   12.352  1   34.16 ? 275 VAL   B CG2 1 
ATOM   5061 N  N   . LEU   B 1 291 ? 13.004  7.775   8.562   1   34.87 ? 276 LEU   B N   1 
ATOM   5062 C  CA  . LEU   B 1 291 ? 12.322  7.775   7.256   1   35.42 ? 276 LEU   B CA  1 
ATOM   5063 C  C   . LEU   B 1 291 ? 10.83   7.444   7.381   1   36.04 ? 276 LEU   B C   1 
ATOM   5064 O  O   . LEU   B 1 291 ? 10.01   8.139   6.799   1   37.16 ? 276 LEU   B O   1 
ATOM   5065 C  CB  . LEU   B 1 291 ? 12.984  6.773   6.299   1   35.22 ? 276 LEU   B CB  1 
ATOM   5066 C  CG  . LEU   B 1 291 ? 12.35   6.651   4.912   1   36.3  ? 276 LEU   B CG  1 
ATOM   5067 C  CD1 . LEU   B 1 291 ? 12.733  7.839   4.044   1   36.37 ? 276 LEU   B CD1 1 
ATOM   5068 C  CD2 . LEU   B 1 291 ? 12.779  5.368   4.227   1   37.24 ? 276 LEU   B CD2 1 
ATOM   5069 N  N   . LEU   B 1 292 ? 10.478  6.389   8.141   1   35.52 ? 277 LEU   B N   1 
ATOM   5070 C  CA  . LEU   B 1 292 ? 9.096   5.926   8.285   1   35.66 ? 277 LEU   B CA  1 
ATOM   5071 C  C   . LEU   B 1 292 ? 8.258   6.621   9.382   1   36.78 ? 277 LEU   B C   1 
ATOM   5072 O  O   . LEU   B 1 292 ? 7.113   6.236   9.61    1   38.02 ? 277 LEU   B O   1 
ATOM   5073 C  CB  . LEU   B 1 292 ? 9.081   4.417   8.509   1   35.21 ? 277 LEU   B CB  1 
ATOM   5074 C  CG  . LEU   B 1 292 ? 9.815   3.57    7.463   1   37.55 ? 277 LEU   B CG  1 
ATOM   5075 C  CD1 . LEU   B 1 292 ? 9.839   2.089   7.873   1   37.48 ? 277 LEU   B CD1 1 
ATOM   5076 C  CD2 . LEU   B 1 292 ? 9.215   3.745   6.074   1   39.31 ? 277 LEU   B CD2 1 
ATOM   5077 N  N   . GLY   B 1 293 ? 8.821   7.615   10.053  1   36.51 ? 278 GLY   B N   1 
ATOM   5078 C  CA  . GLY   B 1 293 ? 8.112   8.333   11.1    1   36.88 ? 278 GLY   B CA  1 
ATOM   5079 C  C   . GLY   B 1 293 ? 7.852   7.53    12.355  1   37.48 ? 278 GLY   B C   1 
ATOM   5080 O  O   . GLY   B 1 293 ? 6.893   7.812   13.078  1   38.49 ? 278 GLY   B O   1 
ATOM   5081 N  N   . ILE   B 1 294 ? 8.676   6.507   12.623  1   37.13 ? 279 ILE   B N   1 
ATOM   5082 C  CA  . ILE   B 1 294 ? 8.583   5.727   13.854  1   37.32 ? 279 ILE   B CA  1 
ATOM   5083 C  C   . ILE   B 1 294 ? 9.338   6.575   14.852  1   38.39 ? 279 ILE   B C   1 
ATOM   5084 O  O   . ILE   B 1 294 ? 10.56   6.682   14.761  1   40.33 ? 279 ILE   B O   1 
ATOM   5085 C  CB  . ILE   B 1 294 ? 9.231   4.338   13.645  1   36.77 ? 279 ILE   B CB  1 
ATOM   5086 C  CG1 . ILE   B 1 294 ? 8.518   3.608   12.483  1   36.14 ? 279 ILE   B CG1 1 
ATOM   5087 C  CG2 . ILE   B 1 294 ? 9.165   3.525   14.939  1   37.17 ? 279 ILE   B CG2 1 
ATOM   5088 C  CD1 . ILE   B 1 294 ? 9.259   2.527   11.895  1   36.73 ? 279 ILE   B CD1 1 
ATOM   5089 N  N   . GLN   B 1 295 ? 8.631   7.253   15.745  1   37.31 ? 280 GLN   B N   1 
ATOM   5090 C  CA  . GLN   B 1 295 ? 9.269   8.199   16.657  1   36.04 ? 280 GLN   B CA  1 
ATOM   5091 C  C   . GLN   B 1 295 ? 9.896   7.504   17.855  1   34.31 ? 280 GLN   B C   1 
ATOM   5092 O  O   . GLN   B 1 295 ? 9.365   7.586   18.971  1   34.43 ? 280 GLN   B O   1 
ATOM   5093 C  CB  . GLN   B 1 295 ? 8.265   9.267   17.088  1   38.36 ? 280 GLN   B CB  1 
ATOM   5094 C  CG  . GLN   B 1 295 ? 7.598   9.983   15.913  1   44.44 ? 280 GLN   B CG  1 
ATOM   5095 C  CD  . GLN   B 1 295 ? 6.311   10.666  16.376  1   54.35 ? 280 GLN   B CD  1 
ATOM   5096 O  OE1 . GLN   B 1 295 ? 6.123   11.877  16.218  1   57.16 ? 280 GLN   B OE1 1 
ATOM   5097 N  NE2 . GLN   B 1 295 ? 5.381   9.894   16.954  1   56.61 ? 280 GLN   B NE2 1 
ATOM   5098 N  N   . GLN   B 1 296 ? 11.023  6.811   17.619  1   32.4  ? 281 GLN   B N   1 
ATOM   5099 C  CA  . GLN   B 1 296 ? 11.764  6.105   18.661  1   31.99 ? 281 GLN   B CA  1 
ATOM   5100 C  C   . GLN   B 1 296 ? 12.289  7.028   19.772  1   31.43 ? 281 GLN   B C   1 
ATOM   5101 O  O   . GLN   B 1 296 ? 12.419  6.602   20.913  1   30.64 ? 281 GLN   B O   1 
ATOM   5102 C  CB  . GLN   B 1 296 ? 12.929  5.306   18.046  1   31.77 ? 281 GLN   B CB  1 
ATOM   5103 C  CG  . GLN   B 1 296 ? 12.485  4.234   17.039  1   30.42 ? 281 GLN   B CG  1 
ATOM   5104 C  CD  . GLN   B 1 296 ? 11.839  3.036   17.693  1   30.84 ? 281 GLN   B CD  1 
ATOM   5105 O  OE1 . GLN   B 1 296 ? 11.66   2.963   18.912  1   31.7  ? 281 GLN   B OE1 1 
ATOM   5106 N  NE2 . GLN   B 1 296 ? 11.54   2.016   16.909  1   30.75 ? 281 GLN   B NE2 1 
ATOM   5107 N  N   . THR   B 1 297 ? 12.552  8.288   19.44   1   32.14 ? 282 THR   B N   1 
ATOM   5108 C  CA  . THR   B 1 297 ? 13.084  9.286   20.365  1   34.69 ? 282 THR   B CA  1 
ATOM   5109 C  C   . THR   B 1 297 ? 11.998  10.167  21.035  1   36.64 ? 282 THR   B C   1 
ATOM   5110 O  O   . THR   B 1 297 ? 12.337  11.053  21.814  1   37.2  ? 282 THR   B O   1 
ATOM   5111 C  CB  . THR   B 1 297 ? 14.168  10.119  19.64   1   36.54 ? 282 THR   B CB  1 
ATOM   5112 O  OG1 . THR   B 1 297 ? 13.662  10.56   18.36   1   37.9  ? 282 THR   B OG1 1 
ATOM   5113 C  CG2 . THR   B 1 297 ? 15.484  9.298   19.415  1   36.64 ? 282 THR   B CG2 1 
ATOM   5114 N  N   . ALA   B 1 298 ? 10.714  9.869   20.833  1   37.15 ? 283 ALA   B N   1 
ATOM   5115 C  CA  . ALA   B 1 298 ? 9.623   10.619  21.476  1   37.9  ? 283 ALA   B CA  1 
ATOM   5116 C  C   . ALA   B 1 298 ? 9.124   9.907   22.766  1   39.14 ? 283 ALA   B C   1 
ATOM   5117 O  O   . ALA   B 1 298 ? 9.415   8.726   22.974  1   39.31 ? 283 ALA   B O   1 
ATOM   5118 C  CB  . ALA   B 1 298 ? 8.466   10.753  20.479  1   38.2  ? 283 ALA   B CB  1 
ATOM   5119 N  N   . GLY   B 1 299 ? 8.357   10.606  23.611  1   39.55 ? 284 GLY   B N   1 
ATOM   5120 C  CA  . GLY   B 1 299 ? 7.69    9.986   24.759  1   40.1  ? 284 GLY   B CA  1 
ATOM   5121 C  C   . GLY   B 1 299 ? 8.291   10.06   26.152  1   40.62 ? 284 GLY   B C   1 
ATOM   5122 O  O   . GLY   B 1 299 ? 7.636   9.658   27.127  1   40.39 ? 284 GLY   B O   1 
ATOM   5123 N  N   . GLY   B 1 300 ? 9.545   10.494  26.257  1   40.79 ? 285 GLY   B N   1 
ATOM   5124 C  CA  . GLY   B 1 300 ? 10.23   10.655  27.537  1   41.16 ? 285 GLY   B CA  1 
ATOM   5125 C  C   . GLY   B 1 300 ? 10.764  9.425   28.25   1   41.48 ? 285 GLY   B C   1 
ATOM   5126 O  O   . GLY   B 1 300 ? 11.333  9.552   29.341  1   42.46 ? 285 GLY   B O   1 
ATOM   5127 N  N   . GLY   B 1 301 ? 10.583  8.245   27.667  1   40.1  ? 286 GLY   B N   1 
ATOM   5128 C  CA  . GLY   B 1 301 ? 11.078  7.02    28.285  1   39.82 ? 286 GLY   B CA  1 
ATOM   5129 C  C   . GLY   B 1 301 ? 12.58   6.799   28.222  1   39.79 ? 286 GLY   B C   1 
ATOM   5130 O  O   . GLY   B 1 301 ? 13.324  7.577   27.621  1   39.49 ? 286 GLY   B O   1 
ATOM   5131 N  N   . HIS   B 1 302 ? 13.023  5.701   28.833  1   39.86 ? 287 HIS   B N   1 
ATOM   5132 C  CA  . HIS   B 1 302 ? 14.416  5.327   28.875  1   41    ? 287 HIS   B CA  1 
ATOM   5133 C  C   . HIS   B 1 302 ? 14.948  4.956   27.514  1   39.03 ? 287 HIS   B C   1 
ATOM   5134 O  O   . HIS   B 1 302 ? 16.05   5.383   27.156  1   39.08 ? 287 HIS   B O   1 
ATOM   5135 C  CB  . HIS   B 1 302 ? 14.629  4.198   29.865  1   45.2  ? 287 HIS   B CB  1 
ATOM   5136 C  CG  . HIS   B 1 302 ? 14.329  4.623   31.267  1   53.07 ? 287 HIS   B CG  1 
ATOM   5137 N  ND1 . HIS   B 1 302 ? 13.141  4.27    31.895  1   56.76 ? 287 HIS   B ND1 1 
ATOM   5138 C  CD2 . HIS   B 1 302 ? 15.054  5.401   32.104  1   55.53 ? 287 HIS   B CD2 1 
ATOM   5139 C  CE1 . HIS   B 1 302 ? 13.195  4.827   33.097  1   57.89 ? 287 HIS   B CE1 1 
ATOM   5140 N  NE2 . HIS   B 1 302 ? 14.326  5.52    33.266  1   57.5  ? 287 HIS   B NE2 1 
ATOM   5141 N  N   . ALA   B 1 303 ? 14.171  4.212   26.715  1   37.17 ? 288 ALA   B N   1 
ATOM   5142 C  CA  . ALA   B 1 303 ? 14.626  3.812   25.388  1   36.65 ? 288 ALA   B CA  1 
ATOM   5143 C  C   . ALA   B 1 303 ? 14.883  5.028   24.511  1   35.6  ? 288 ALA   B C   1 
ATOM   5144 O  O   . ALA   B 1 303 ? 15.963  5.144   23.931  1   35.03 ? 288 ALA   B O   1 
ATOM   5145 C  CB  . ALA   B 1 303 ? 13.613  2.882   24.726  1   36.95 ? 288 ALA   B CB  1 
ATOM   5146 N  N   . ALA   B 1 304 ? 13.946  5.991   24.541  1   34.6  ? 289 ALA   B N   1 
ATOM   5147 C  CA  . ALA   B 1 304 ? 14.024  7.223   23.77   1   33.89 ? 289 ALA   B CA  1 
ATOM   5148 C  C   . ALA   B 1 304 ? 15.22   8.048   24.238  1   32.31 ? 289 ALA   B C   1 
ATOM   5149 O  O   . ALA   B 1 304 ? 15.968  8.562   23.411  1   32.01 ? 289 ALA   B O   1 
ATOM   5150 C  CB  . ALA   B 1 304 ? 12.727  8.01    23.934  1   33.8  ? 289 ALA   B CB  1 
ATOM   5151 N  N   . GLN   B 1 305 ? 15.426  8.143   25.558  1   31.27 ? 290 GLN   B N   1 
ATOM   5152 C  CA  . GLN   B 1 305 ? 16.552  8.916   26.096  1   30.68 ? 290 GLN   B CA  1 
ATOM   5153 C  C   . GLN   B 1 305 ? 17.889  8.295   25.656  1   31.97 ? 290 GLN   B C   1 
ATOM   5154 O  O   . GLN   B 1 305 ? 18.793  9.018   25.227  1   32.61 ? 290 GLN   B O   1 
ATOM   5155 C  CB  . GLN   B 1 305 ? 16.481  8.965   27.631  1   30.35 ? 290 GLN   B CB  1 
ATOM   5156 C  CG  . GLN   B 1 305 ? 17.537  9.849   28.257  1   33.62 ? 290 GLN   B CG  1 
ATOM   5157 C  CD  . GLN   B 1 305 ? 17.23   11.322  28.006  1   36.86 ? 290 GLN   B CD  1 
ATOM   5158 O  OE1 . GLN   B 1 305 ? 16.098  11.789  28.218  1   37.12 ? 290 GLN   B OE1 1 
ATOM   5159 N  NE2 . GLN   B 1 305 ? 18.228  12.068  27.54   1   36.14 ? 290 GLN   B NE2 1 
ATOM   5160 N  N   . PHE   B 1 306 ? 18.005  6.961   25.737  1   31.37 ? 291 PHE   B N   1 
ATOM   5161 C  CA  . PHE   B 1 306 ? 19.224  6.28    25.357  1   31.52 ? 291 PHE   B CA  1 
ATOM   5162 C  C   . PHE   B 1 306 ? 19.527  6.456   23.883  1   31.33 ? 291 PHE   B C   1 
ATOM   5163 O  O   . PHE   B 1 306 ? 20.653  6.752   23.568  1   31.17 ? 291 PHE   B O   1 
ATOM   5164 C  CB  . PHE   B 1 306 ? 19.169  4.796   25.739  1   32.16 ? 291 PHE   B CB  1 
ATOM   5165 C  CG  . PHE   B 1 306 ? 20.436  4.021   25.412  1   33.36 ? 291 PHE   B CG  1 
ATOM   5166 C  CD1 . PHE   B 1 306 ? 21.566  4.139   26.21   1   34.09 ? 291 PHE   B CD1 1 
ATOM   5167 C  CD2 . PHE   B 1 306 ? 20.471  3.135   24.343  1   33.81 ? 291 PHE   B CD2 1 
ATOM   5168 C  CE1 . PHE   B 1 306 ? 22.723  3.395   25.929  1   35.61 ? 291 PHE   B CE1 1 
ATOM   5169 C  CE2 . PHE   B 1 306 ? 21.608  2.38    24.076  1   34.96 ? 291 PHE   B CE2 1 
ATOM   5170 C  CZ  . PHE   B 1 306 ? 22.738  2.523   24.857  1   35.56 ? 291 PHE   B CZ  1 
ATOM   5171 N  N   . LEU   B 1 307 ? 18.518  6.364   22.985  1   31.45 ? 292 LEU   B N   1 
ATOM   5172 C  CA  . LEU   B 1 307 ? 18.783  6.544   21.554  1   31.5  ? 292 LEU   B CA  1 
ATOM   5173 C  C   . LEU   B 1 307 ? 19.21   7.978   21.232  1   31.14 ? 292 LEU   B C   1 
ATOM   5174 O  O   . LEU   B 1 307 ? 20.076  8.178   20.367  1   31.62 ? 292 LEU   B O   1 
ATOM   5175 C  CB  . LEU   B 1 307 ? 17.602  6.108   20.688  1   32.57 ? 292 LEU   B CB  1 
ATOM   5176 C  CG  . LEU   B 1 307 ? 17.434  4.586   20.596  1   34.73 ? 292 LEU   B CG  1 
ATOM   5177 C  CD1 . LEU   B 1 307 ? 16.092  4.22    20.017  1   35.75 ? 292 LEU   B CD1 1 
ATOM   5178 C  CD2 . LEU   B 1 307 ? 18.579  3.948   19.854  1   34.6  ? 292 LEU   B CD2 1 
ATOM   5179 N  N   . GLN   B 1 308 ? 18.644  8.979   21.948  1   29.6  ? 293 GLN   B N   1 
ATOM   5180 C  CA  A GLN   B 1 308 ? 19.034  10.362  21.695  0.5 29.75 ? 293 GLN   B CA  1 
ATOM   5181 C  CA  B GLN   B 1 308 ? 19.031  10.364  21.704  0.5 29.78 ? 293 GLN   B CA  1 
ATOM   5182 C  C   . GLN   B 1 308 ? 20.461  10.583  22.191  1   30.05 ? 293 GLN   B C   1 
ATOM   5183 O  O   . GLN   B 1 308 ? 21.291  11.076  21.438  1   29.84 ? 293 GLN   B O   1 
ATOM   5184 C  CB  A GLN   B 1 308 ? 18.033  11.353  22.318  0.5 29.87 ? 293 GLN   B CB  1 
ATOM   5185 C  CB  B GLN   B 1 308 ? 18.007  11.384  22.282  0.5 30.02 ? 293 GLN   B CB  1 
ATOM   5186 C  CG  A GLN   B 1 308 ? 18.227  12.821  21.896  0.5 30.44 ? 293 GLN   B CG  1 
ATOM   5187 C  CG  B GLN   B 1 308 ? 18.208  11.813  23.743  0.5 30.75 ? 293 GLN   B CG  1 
ATOM   5188 C  CD  A GLN   B 1 308 ? 18.128  13.066  20.397  0.5 33.97 ? 293 GLN   B CD  1 
ATOM   5189 C  CD  B GLN   B 1 308 ? 17.433  13.055  24.16   0.5 29.79 ? 293 GLN   B CD  1 
ATOM   5190 O  OE1 A GLN   B 1 308 ? 18.923  13.817  19.814  0.5 35.73 ? 293 GLN   B OE1 1 
ATOM   5191 O  OE1 B GLN   B 1 308 ? 16.186  13.111  24.09   0.5 29.71 ? 293 GLN   B OE1 1 
ATOM   5192 N  NE2 A GLN   B 1 308 ? 17.153  12.466  19.736  0.5 33.45 ? 293 GLN   B NE2 1 
ATOM   5193 N  NE2 B GLN   B 1 308 ? 18.16   14.053  24.656  0.5 27.25 ? 293 GLN   B NE2 1 
ATOM   5194 N  N   . ASP   B 1 309 ? 20.776  10.145  23.435  1   30.25 ? 294 ASP   B N   1 
ATOM   5195 C  CA  . ASP   B 1 309 ? 22.118  10.279  23.988  1   31.94 ? 294 ASP   B CA  1 
ATOM   5196 C  C   . ASP   B 1 309 ? 23.184  9.615   23.08   1   33.33 ? 294 ASP   B C   1 
ATOM   5197 O  O   . ASP   B 1 309 ? 24.263  10.18   22.866  1   35.03 ? 294 ASP   B O   1 
ATOM   5198 C  CB  . ASP   B 1 309 ? 22.154  9.675   25.401  1   34    ? 294 ASP   B CB  1 
ATOM   5199 C  CG  . ASP   B 1 309 ? 21.344  10.452  26.443  1   40.04 ? 294 ASP   B CG  1 
ATOM   5200 O  OD1 . ASP   B 1 309 ? 20.89   11.579  26.132  1   40.55 ? 294 ASP   B OD1 1 
ATOM   5201 O  OD2 . ASP   B 1 309 ? 21.153  9.922   27.573  1   42.13 ? 294 ASP   B OD2 1 
ATOM   5202 N  N   . MET   B 1 310 ? 22.872  8.426   22.528  1   32.5  ? 295 MET   B N   1 
ATOM   5203 C  CA  . MET   B 1 310 ? 23.818  7.707   21.682  1   32.48 ? 295 MET   B CA  1 
ATOM   5204 C  C   . MET   B 1 310 ? 24.116  8.393   20.345  1   33.08 ? 295 MET   B C   1 
ATOM   5205 O  O   . MET   B 1 310 ? 25.115  8.042   19.713  1   31.91 ? 295 MET   B O   1 
ATOM   5206 C  CB  . MET   B 1 310 ? 23.404  6.254   21.477  1   32.88 ? 295 MET   B CB  1 
ATOM   5207 C  CG  . MET   B 1 310 ? 23.528  5.403   22.733  1   35.46 ? 295 MET   B CG  1 
ATOM   5208 S  SD  . MET   B 1 310 ? 25.139  5.441   23.586  1   36.29 ? 295 MET   B SD  1 
ATOM   5209 C  CE  . MET   B 1 310 ? 24.804  6.579   24.973  1   30.49 ? 295 MET   B CE  1 
ATOM   5210 N  N   . ARG   B 1 311 ? 23.333  9.411   19.956  1   33.41 ? 296 ARG   B N   1 
ATOM   5211 C  CA  . ARG   B 1 311 ? 23.626  10.189  18.738  1   34.76 ? 296 ARG   B CA  1 
ATOM   5212 C  C   . ARG   B 1 311 ? 24.938  10.971  18.873  1   35.06 ? 296 ARG   B C   1 
ATOM   5213 O  O   . ARG   B 1 311 ? 25.599  11.243  17.875  1   35.05 ? 296 ARG   B O   1 
ATOM   5214 C  CB  . ARG   B 1 311 ? 22.469  11.131  18.371  1   36.1  ? 296 ARG   B CB  1 
ATOM   5215 C  CG  . ARG   B 1 311 ? 21.342  10.394  17.634  1   39.64 ? 296 ARG   B CG  1 
ATOM   5216 C  CD  . ARG   B 1 311 ? 20.249  11.315  17.134  1   43.06 ? 296 ARG   B CD  1 
ATOM   5217 N  NE  . ARG   B 1 311 ? 19.145  10.555  16.546  1   46.03 ? 296 ARG   B NE  1 
ATOM   5218 C  CZ  . ARG   B 1 311 ? 18.212  11.073  15.744  1   48.04 ? 296 ARG   B CZ  1 
ATOM   5219 N  NH1 . ARG   B 1 311 ? 18.26   12.359  15.397  1   47.53 ? 296 ARG   B NH1 1 
ATOM   5220 N  NH2 . ARG   B 1 311 ? 17.248  10.303  15.255  1   46.44 ? 296 ARG   B NH2 1 
ATOM   5221 N  N   . ARG   B 1 312 ? 25.324  11.324  20.106  1   35.86 ? 297 ARG   B N   1 
ATOM   5222 C  CA  . ARG   B 1 312 ? 26.584  12.017  20.362  1   37.55 ? 297 ARG   B CA  1 
ATOM   5223 C  C   . ARG   B 1 312 ? 27.797  11.093  20.099  1   37.01 ? 297 ARG   B C   1 
ATOM   5224 O  O   . ARG   B 1 312 ? 28.911  11.58   19.949  1   37.47 ? 297 ARG   B O   1 
ATOM   5225 C  CB  . ARG   B 1 312 ? 26.644  12.468  21.829  1   40.26 ? 297 ARG   B CB  1 
ATOM   5226 C  CG  . ARG   B 1 312 ? 25.776  13.658  22.203  1   44.23 ? 297 ARG   B CG  1 
ATOM   5227 C  CD  . ARG   B 1 312 ? 25.93   13.905  23.704  1   46.32 ? 297 ARG   B CD  1 
ATOM   5228 N  N   . TYR   B 1 313 ? 27.594  9.758   20.155  1   34.87 ? 298 TYR   B N   1 
ATOM   5229 C  CA  . TYR   B 1 313 ? 28.625  8.757   19.912  1   32.52 ? 298 TYR   B CA  1 
ATOM   5230 C  C   . TYR   B 1 313 ? 28.608  8.242   18.47   1   31.5  ? 298 TYR   B C   1 
ATOM   5231 O  O   . TYR   B 1 313 ? 29.263  7.246   18.169  1   30.02 ? 298 TYR   B O   1 
ATOM   5232 C  CB  . TYR   B 1 313 ? 28.38   7.574   20.832  1   31.26 ? 298 TYR   B CB  1 
ATOM   5233 C  CG  . TYR   B 1 313 ? 28.444  7.897   22.312  1   30.91 ? 298 TYR   B CG  1 
ATOM   5234 C  CD1 . TYR   B 1 313 ? 27.476  8.682   22.915  1   31.42 ? 298 TYR   B CD1 1 
ATOM   5235 C  CD2 . TYR   B 1 313 ? 29.416  7.335   23.12   1   31.65 ? 298 TYR   B CD2 1 
ATOM   5236 C  CE1 . TYR   B 1 313 ? 27.508  8.951   24.28   1   31.78 ? 298 TYR   B CE1 1 
ATOM   5237 C  CE2 . TYR   B 1 313 ? 29.445  7.572   24.487  1   31.98 ? 298 TYR   B CE2 1 
ATOM   5238 C  CZ  . TYR   B 1 313 ? 28.507  8.407   25.062  1   33.33 ? 298 TYR   B CZ  1 
ATOM   5239 O  OH  . TYR   B 1 313 ? 28.508  8.611   26.431  1   35.13 ? 298 TYR   B OH  1 
ATOM   5240 N  N   . MET   B 1 314 ? 27.887  8.935   17.584  1   31.06 ? 299 MET   B N   1 
ATOM   5241 C  CA  . MET   B 1 314 ? 27.707  8.635   16.172  1   30.98 ? 299 MET   B CA  1 
ATOM   5242 C  C   . MET   B 1 314 ? 28.529  9.654   15.377  1   30.81 ? 299 MET   B C   1 
ATOM   5243 O  O   . MET   B 1 314 ? 28.587  10.808  15.786  1   30.75 ? 299 MET   B O   1 
ATOM   5244 C  CB  . MET   B 1 314 ? 26.212  8.841   15.865  1   30.85 ? 299 MET   B CB  1 
ATOM   5245 C  CG  . MET   B 1 314 ? 25.773  8.394   14.505  1   32.49 ? 299 MET   B CG  1 
ATOM   5246 S  SD  . MET   B 1 314 ? 24.001  8.715   14.259  1   34.49 ? 299 MET   B SD  1 
ATOM   5247 C  CE  . MET   B 1 314 ? 23.268  7.517   15.48   1   26.88 ? 299 MET   B CE  1 
ATOM   5248 N  N   . PRO   B 1 315 ? 29.144  9.289   14.236  1   30.78 ? 300 PRO   B N   1 
ATOM   5249 C  CA  . PRO   B 1 315 ? 29.917  10.286  13.476  1   32.06 ? 300 PRO   B CA  1 
ATOM   5250 C  C   . PRO   B 1 315 ? 29.071  11.509  13.104  1   34    ? 300 PRO   B C   1 
ATOM   5251 O  O   . PRO   B 1 315 ? 27.9    11.371  12.723  1   34.12 ? 300 PRO   B O   1 
ATOM   5252 C  CB  . PRO   B 1 315 ? 30.358  9.516   12.22   1   32.65 ? 300 PRO   B CB  1 
ATOM   5253 C  CG  . PRO   B 1 315 ? 30.273  8.073   12.592  1   32.4  ? 300 PRO   B CG  1 
ATOM   5254 C  CD  . PRO   B 1 315 ? 29.191  7.955   13.604  1   30.57 ? 300 PRO   B CD  1 
ATOM   5255 N  N   . PRO   B 1 316 ? 29.641  12.725  13.221  1   34.51 ? 301 PRO   B N   1 
ATOM   5256 C  CA  . PRO   B 1 316 ? 28.878  13.93   12.869  1   33.81 ? 301 PRO   B CA  1 
ATOM   5257 C  C   . PRO   B 1 316 ? 28.178  13.868  11.51   1   33.91 ? 301 PRO   B C   1 
ATOM   5258 O  O   . PRO   B 1 316 ? 27.024  14.271  11.465  1   34.58 ? 301 PRO   B O   1 
ATOM   5259 C  CB  . PRO   B 1 316 ? 29.913  15.064  12.943  1   34.85 ? 301 PRO   B CB  1 
ATOM   5260 C  CG  . PRO   B 1 316 ? 31.25   14.383  12.978  1   35.57 ? 301 PRO   B CG  1 
ATOM   5261 C  CD  . PRO   B 1 316 ? 31.01   13.063  13.659  1   34.18 ? 301 PRO   B CD  1 
ATOM   5262 N  N   . ALA   B 1 317 ? 28.813  13.335  10.436  1   32.95 ? 302 ALA   B N   1 
ATOM   5263 C  CA  . ALA   B 1 317 ? 28.171  13.247  9.11    1   32.63 ? 302 ALA   B CA  1 
ATOM   5264 C  C   . ALA   B 1 317 ? 26.862  12.436  9.134   1   33.46 ? 302 ALA   B C   1 
ATOM   5265 O  O   . ALA   B 1 317 ? 25.912  12.727  8.398   1   33.18 ? 302 ALA   B O   1 
ATOM   5266 C  CB  . ALA   B 1 317 ? 29.124  12.628  8.103   1   31.38 ? 302 ALA   B CB  1 
ATOM   5267 N  N   . HIS   B 1 318 ? 26.841  11.391  9.97    1   33.8  ? 303 HIS   B N   1 
ATOM   5268 C  CA  . HIS   B 1 318 ? 25.727  10.465  10.12   1   33.33 ? 303 HIS   B CA  1 
ATOM   5269 C  C   . HIS   B 1 318 ? 24.645  11.063  10.997  1   33.69 ? 303 HIS   B C   1 
ATOM   5270 O  O   . HIS   B 1 318 ? 23.466  10.95   10.68   1   33.64 ? 303 HIS   B O   1 
ATOM   5271 C  CB  . HIS   B 1 318 ? 26.242  9.117   10.635  1   33.45 ? 303 HIS   B CB  1 
ATOM   5272 C  CG  . HIS   B 1 318 ? 27.15   8.403   9.674   1   35.74 ? 303 HIS   B CG  1 
ATOM   5273 N  ND1 . HIS   B 1 318 ? 27.829  7.25    10.049  1   37.49 ? 303 HIS   B ND1 1 
ATOM   5274 C  CD2 . HIS   B 1 318 ? 27.395  8.643   8.356   1   36.54 ? 303 HIS   B CD2 1 
ATOM   5275 C  CE1 . HIS   B 1 318 ? 28.487  6.853   8.968   1   37.94 ? 303 HIS   B CE1 1 
ATOM   5276 N  NE2 . HIS   B 1 318 ? 28.261  7.663   7.928   1   37.58 ? 303 HIS   B NE2 1 
ATOM   5277 N  N   . ARG   B 1 319 ? 25.028  11.796  12.037  1   33.59 ? 304 ARG   B N   1 
ATOM   5278 C  CA  . ARG   B 1 319 ? 24.115  12.574  12.864  1   34.55 ? 304 ARG   B CA  1 
ATOM   5279 C  C   . ARG   B 1 319 ? 23.401  13.621  11.948  1   34.6  ? 304 ARG   B C   1 
ATOM   5280 O  O   . ARG   B 1 319 ? 22.179  13.785  12.005  1   34.63 ? 304 ARG   B O   1 
ATOM   5281 C  CB  . ARG   B 1 319 ? 24.956  13.31   13.909  1   37.47 ? 304 ARG   B CB  1 
ATOM   5282 C  CG  . ARG   B 1 319 ? 24.27   13.699  15.19   1   43.71 ? 304 ARG   B CG  1 
ATOM   5283 C  CD  . ARG   B 1 319 ? 25.262  14.431  16.103  1   49.31 ? 304 ARG   B CD  1 
ATOM   5284 N  NE  . ARG   B 1 319 ? 26.487  13.662  16.378  1   53.5  ? 304 ARG   B NE  1 
ATOM   5285 C  CZ  . ARG   B 1 319 ? 27.696  14.205  16.521  1   57.25 ? 304 ARG   B CZ  1 
ATOM   5286 N  NH1 . ARG   B 1 319 ? 27.862  15.517  16.405  1   58.27 ? 304 ARG   B NH1 1 
ATOM   5287 N  NH2 . ARG   B 1 319 ? 28.75   13.438  16.769  1   57.19 ? 304 ARG   B NH2 1 
ATOM   5288 N  N   . ASN   B 1 320 ? 24.165  14.244  11.031  1   34.08 ? 305 ASN   B N   1 
ATOM   5289 C  CA  . ASN   B 1 320 ? 23.656  15.217  10.068  1   33.65 ? 305 ASN   B CA  1 
ATOM   5290 C  C   . ASN   B 1 320 ? 22.72   14.606  9.065   1   33.32 ? 305 ASN   B C   1 
ATOM   5291 O  O   . ASN   B 1 320 ? 21.735  15.246  8.676   1   33.54 ? 305 ASN   B O   1 
ATOM   5292 C  CB  . ASN   B 1 320 ? 24.8    15.903  9.352   1   34.83 ? 305 ASN   B CB  1 
ATOM   5293 C  CG  . ASN   B 1 320 ? 25.624  16.776  10.245  1   36.61 ? 305 ASN   B CG  1 
ATOM   5294 O  OD1 . ASN   B 1 320 ? 25.269  17.056  11.395  1   36.79 ? 305 ASN   B OD1 1 
ATOM   5295 N  ND2 . ASN   B 1 320 ? 26.758  17.205  9.737   1   38.31 ? 305 ASN   B ND2 1 
ATOM   5296 N  N   . PHE   B 1 321 ? 23      13.373  8.64    1   32.55 ? 306 PHE   B N   1 
ATOM   5297 C  CA  . PHE   B 1 321 ? 22.113  12.68   7.718   1   32.8  ? 306 PHE   B CA  1 
ATOM   5298 C  C   . PHE   B 1 321 ? 20.74   12.453  8.355   1   32.42 ? 306 PHE   B C   1 
ATOM   5299 O  O   . PHE   B 1 321 ? 19.731  12.772  7.714   1   31.83 ? 306 PHE   B O   1 
ATOM   5300 C  CB  . PHE   B 1 321 ? 22.721  11.357  7.274   1   32.77 ? 306 PHE   B CB  1 
ATOM   5301 C  CG  . PHE   B 1 321 ? 21.826  10.59   6.334   1   33.55 ? 306 PHE   B CG  1 
ATOM   5302 C  CD1 . PHE   B 1 321 ? 21.573  11.059  5.056   1   35.1  ? 306 PHE   B CD1 1 
ATOM   5303 C  CD2 . PHE   B 1 321 ? 21.268  9.383   6.712   1   34.21 ? 306 PHE   B CD2 1 
ATOM   5304 C  CE1 . PHE   B 1 321 ? 20.779  10.331  4.171   1   35.67 ? 306 PHE   B CE1 1 
ATOM   5305 C  CE2 . PHE   B 1 321 ? 20.473  8.659   5.833   1   35.22 ? 306 PHE   B CE2 1 
ATOM   5306 C  CZ  . PHE   B 1 321 ? 20.237  9.133   4.565   1   35.27 ? 306 PHE   B CZ  1 
ATOM   5307 N  N   . LEU   B 1 322 ? 20.716  11.976  9.637   1   31.7  ? 307 LEU   B N   1 
ATOM   5308 C  CA  . LEU   B 1 322 ? 19.487  11.745  10.4    1   31.84 ? 307 LEU   B CA  1 
ATOM   5309 C  C   . LEU   B 1 322 ? 18.698  13.035  10.558  1   33.36 ? 307 LEU   B C   1 
ATOM   5310 O  O   . LEU   B 1 322 ? 17.492  13.042  10.314  1   33.51 ? 307 LEU   B O   1 
ATOM   5311 C  CB  . LEU   B 1 322 ? 19.738  11.107  11.793  1   31.34 ? 307 LEU   B CB  1 
ATOM   5312 C  CG  . LEU   B 1 322 ? 20.355  9.695   11.831  1   32.55 ? 307 LEU   B CG  1 
ATOM   5313 C  CD1 . LEU   B 1 322 ? 20.482  9.206   13.271  1   32.26 ? 307 LEU   B CD1 1 
ATOM   5314 C  CD2 . LEU   B 1 322 ? 19.549  8.71    11.042  1   32.66 ? 307 LEU   B CD2 1 
ATOM   5315 N  N   . CYS   B 1 323 ? 19.354  14.132  10.94   1   34.2  ? 308 CYS   B N   1 
ATOM   5316 C  CA  . CYS   B 1 323 ? 18.716  15.433  11.096  1   35.88 ? 308 CYS   B CA  1 
ATOM   5317 C  C   . CYS   B 1 323 ? 18.061  15.857  9.777   1   36.47 ? 308 CYS   B C   1 
ATOM   5318 O  O   . CYS   B 1 323 ? 16.907  16.299  9.775   1   35.88 ? 308 CYS   B O   1 
ATOM   5319 C  CB  . CYS   B 1 323 ? 19.739  16.467  11.575  1   38.13 ? 308 CYS   B CB  1 
ATOM   5320 S  SG  . CYS   B 1 323 ? 19.387  18.178  11.069  1   45.47 ? 308 CYS   B SG  1 
ATOM   5321 N  N   . SER   B 1 324 ? 18.787  15.716  8.668   1   37.17 ? 309 SER   B N   1 
ATOM   5322 C  CA  . SER   B 1 324 ? 18.236  16.093  7.368   1   38.27 ? 309 SER   B CA  1 
ATOM   5323 C  C   . SER   B 1 324 ? 17.033  15.221  6.978   1   38.29 ? 309 SER   B C   1 
ATOM   5324 O  O   . SER   B 1 324 ? 16.102  15.743  6.375   1   38.19 ? 309 SER   B O   1 
ATOM   5325 C  CB  . SER   B 1 324 ? 19.302  16.103  6.288   1   40.26 ? 309 SER   B CB  1 
ATOM   5326 O  OG  . SER   B 1 324 ? 19.605  14.774  5.912   1   44.32 ? 309 SER   B OG  1 
ATOM   5327 N  N   . LEU   B 1 325 ? 17.007  13.929  7.358   1   37.59 ? 310 LEU   B N   1 
ATOM   5328 C  CA  . LEU   B 1 325 ? 15.833  13.091  7.089   1   38.23 ? 310 LEU   B CA  1 
ATOM   5329 C  C   . LEU   B 1 325 ? 14.646  13.626  7.911   1   40.81 ? 310 LEU   B C   1 
ATOM   5330 O  O   . LEU   B 1 325 ? 13.538  13.742  7.389   1   41.58 ? 310 LEU   B O   1 
ATOM   5331 C  CB  . LEU   B 1 325 ? 16.103  11.629  7.49    1   37.5  ? 310 LEU   B CB  1 
ATOM   5332 C  CG  . LEU   B 1 325 ? 17.021  10.803  6.646   1   38    ? 310 LEU   B CG  1 
ATOM   5333 C  CD1 . LEU   B 1 325 ? 17.042  9.398   7.144   1   38.32 ? 310 LEU   B CD1 1 
ATOM   5334 C  CD2 . LEU   B 1 325 ? 16.604  10.822  5.216   1   38.86 ? 310 LEU   B CD2 1 
ATOM   5335 N  N   . GLU   B 1 326 ? 14.898  14.007  9.184   1   42.06 ? 311 GLU   B N   1 
ATOM   5336 C  CA  . GLU   B 1 326 ? 13.904  14.582  10.094  1   43.96 ? 311 GLU   B CA  1 
ATOM   5337 C  C   . GLU   B 1 326 ? 13.35   15.906  9.562   1   45.13 ? 311 GLU   B C   1 
ATOM   5338 O  O   . GLU   B 1 326 ? 12.177  16.197  9.783   1   45.91 ? 311 GLU   B O   1 
ATOM   5339 C  CB  . GLU   B 1 326 ? 14.505  14.802  11.501  1   47.32 ? 311 GLU   B CB  1 
ATOM   5340 C  CG  . GLU   B 1 326 ? 14.264  13.654  12.474  1   54.43 ? 311 GLU   B CG  1 
ATOM   5341 C  CD  . GLU   B 1 326 ? 15.272  13.475  13.604  1   63.05 ? 311 GLU   B CD  1 
ATOM   5342 O  OE1 . GLU   B 1 326 ? 16.22   14.29   13.706  1   65.89 ? 311 GLU   B OE1 1 
ATOM   5343 O  OE2 . GLU   B 1 326 ? 15.111  12.513  14.392  1   64.45 ? 311 GLU   B OE2 1 
ATOM   5344 N  N   . SER   B 1 327 ? 14.191  16.708  8.884   1   45.22 ? 312 SER   B N   1 
ATOM   5345 C  CA  . SER   B 1 327 ? 13.821  18.012  8.323   1   46.6  ? 312 SER   B CA  1 
ATOM   5346 C  C   . SER   B 1 327 ? 12.934  17.913  7.077   1   48.04 ? 312 SER   B C   1 
ATOM   5347 O  O   . SER   B 1 327 ? 12.24   18.872  6.728   1   48.34 ? 312 SER   B O   1 
ATOM   5348 C  CB  . SER   B 1 327 ? 15.071  18.813  7.978   1   48.19 ? 312 SER   B CB  1 
ATOM   5349 O  OG  . SER   B 1 327 ? 15.851  19.081  9.134   1   50.95 ? 312 SER   B OG  1 
ATOM   5350 N  N   . ASN   B 1 328 ? 12.999  16.784  6.379   1   48.48 ? 313 ASN   B N   1 
ATOM   5351 C  CA  . ASN   B 1 328 ? 12.231  16.57   5.163   1   49.4  ? 313 ASN   B CA  1 
ATOM   5352 C  C   . ASN   B 1 328 ? 10.758  16.251  5.487   1   48.89 ? 313 ASN   B C   1 
ATOM   5353 O  O   . ASN   B 1 328 ? 10.451  15.854  6.61    1   49.26 ? 313 ASN   B O   1 
ATOM   5354 C  CB  . ASN   B 1 328 ? 12.878  15.433  4.38    1   51.87 ? 313 ASN   B CB  1 
ATOM   5355 C  CG  . ASN   B 1 328 ? 14.01   15.878  3.49    1   57.58 ? 313 ASN   B CG  1 
ATOM   5356 O  OD1 . ASN   B 1 328 ? 14.113  15.469  2.338   1   60.33 ? 313 ASN   B OD1 1 
ATOM   5357 N  ND2 . ASN   B 1 328 ? 14.891  16.724  3.982   1   58.47 ? 313 ASN   B ND2 1 
ATOM   5358 N  N   . PRO   B 1 329 ? 9.82    16.435  4.536   1   48.1  ? 314 PRO   B N   1 
ATOM   5359 C  CA  . PRO   B 1 329 ? 8.409   16.105  4.826   1   46.8  ? 314 PRO   B CA  1 
ATOM   5360 C  C   . PRO   B 1 329 ? 8.236   14.634  5.201   1   45.54 ? 314 PRO   B C   1 
ATOM   5361 O  O   . PRO   B 1 329 ? 9.002   13.787  4.752   1   45.47 ? 314 PRO   B O   1 
ATOM   5362 C  CB  . PRO   B 1 329 ? 7.685   16.424  3.511   1   47.8  ? 314 PRO   B CB  1 
ATOM   5363 C  CG  . PRO   B 1 329 ? 8.607   17.349  2.769   1   48.9  ? 314 PRO   B CG  1 
ATOM   5364 C  CD  . PRO   B 1 329 ? 9.992   16.911  3.149   1   47.7  ? 314 PRO   B CD  1 
ATOM   5365 N  N   . SER   B 1 330 ? 7.254   14.34   6.046   1   44.03 ? 315 SER   B N   1 
ATOM   5366 C  CA  . SER   B 1 330 ? 6.982   13.003  6.538   1   43.18 ? 315 SER   B CA  1 
ATOM   5367 C  C   . SER   B 1 330 ? 6.435   12.031  5.483   1   43.51 ? 315 SER   B C   1 
ATOM   5368 O  O   . SER   B 1 330 ? 5.422   12.314  4.826   1   43.3  ? 315 SER   B O   1 
ATOM   5369 C  CB  . SER   B 1 330 ? 6.03    13.079  7.726   1   43.05 ? 315 SER   B CB  1 
ATOM   5370 O  OG  . SER   B 1 330 ? 5.586   11.801  8.158   1   44.87 ? 315 SER   B OG  1 
ATOM   5371 N  N   . VAL   B 1 331 ? 7.082   10.858  5.369   1   42.86 ? 316 VAL   B N   1 
ATOM   5372 C  CA  . VAL   B 1 331 ? 6.645   9.779   4.486   1   42.67 ? 316 VAL   B CA  1 
ATOM   5373 C  C   . VAL   B 1 331 ? 5.337   9.167   5.036   1   42.07 ? 316 VAL   B C   1 
ATOM   5374 O  O   . VAL   B 1 331 ? 4.4     8.934   4.269   1   41.53 ? 316 VAL   B O   1 
ATOM   5375 C  CB  . VAL   B 1 331 ? 7.75    8.705   4.342   1   42.86 ? 316 VAL   B CB  1 
ATOM   5376 C  CG1 . VAL   B 1 331 ? 7.251   7.501   3.551   1   43.07 ? 316 VAL   B CG1 1 
ATOM   5377 C  CG2 . VAL   B 1 331 ? 8.987   9.299   3.696   1   43.47 ? 316 VAL   B CG2 1 
ATOM   5378 N  N   . ARG   B 1 332 ? 5.25    8.969   6.371   1   41.9  ? 317 ARG   B N   1 
ATOM   5379 C  CA  . ARG   B 1 332 ? 4.053   8.408   6.993   1   41.97 ? 317 ARG   B CA  1 
ATOM   5380 C  C   . ARG   B 1 332 ? 2.857   9.341   6.748   1   42.62 ? 317 ARG   B C   1 
ATOM   5381 O  O   . ARG   B 1 332 ? 1.793   8.874   6.367   1   42.23 ? 317 ARG   B O   1 
ATOM   5382 C  CB  . ARG   B 1 332 ? 4.271   8.148   8.508   1   42.42 ? 317 ARG   B CB  1 
ATOM   5383 C  CG  . ARG   B 1 332 ? 3.059   8.426   9.402   1   45.99 ? 317 ARG   B CG  1 
ATOM   5384 C  CD  . ARG   B 1 332 ? 3.224   7.985   10.822  1   49.16 ? 317 ARG   B CD  1 
ATOM   5385 N  NE  . ARG   B 1 332 ? 3.315   6.538   10.817  1   51.64 ? 317 ARG   B NE  1 
ATOM   5386 C  CZ  . ARG   B 1 332 ? 2.49    5.722   11.445  1   51.28 ? 317 ARG   B CZ  1 
ATOM   5387 N  NH1 . ARG   B 1 332 ? 1.51    6.205   12.2    1   51.6  ? 317 ARG   B NH1 1 
ATOM   5388 N  NH2 . ARG   B 1 332 ? 2.646   4.423   11.343  1   48.48 ? 317 ARG   B NH2 1 
ATOM   5389 N  N   . GLU   B 1 333 ? 3.043   10.648  6.971   1   43.33 ? 318 GLU   B N   1 
ATOM   5390 C  CA  . GLU   B 1 333 ? 1.955   11.609  6.788   1   44.28 ? 318 GLU   B CA  1 
ATOM   5391 C  C   . GLU   B 1 333 ? 1.479   11.634  5.34    1   43.53 ? 318 GLU   B C   1 
ATOM   5392 O  O   . GLU   B 1 333 ? 0.282   11.712  5.096   1   44.11 ? 318 GLU   B O   1 
ATOM   5393 C  CB  . GLU   B 1 333 ? 2.376   13.004  7.277   1   48.25 ? 318 GLU   B CB  1 
ATOM   5394 C  CG  . GLU   B 1 333 ? 1.587   13.541  8.472   1   57.52 ? 318 GLU   B CG  1 
ATOM   5395 C  CD  . GLU   B 1 333 ? 1.014   12.574  9.504   1   68.43 ? 318 GLU   B CD  1 
ATOM   5396 O  OE1 . GLU   B 1 333 ? -0.232  12.537  9.648   1   70.44 ? 318 GLU   B OE1 1 
ATOM   5397 O  OE2 . GLU   B 1 333 ? 1.802   11.859  10.171  1   71.45 ? 318 GLU   B OE2 1 
ATOM   5398 N  N   . PHE   B 1 334 ? 2.404   11.504  4.388   1   42.07 ? 319 PHE   B N   1 
ATOM   5399 C  CA  . PHE   B 1 334 ? 2.053   11.492  2.982   1   41.55 ? 319 PHE   B CA  1 
ATOM   5400 C  C   . PHE   B 1 334 ? 1.23    10.261  2.659   1   41.67 ? 319 PHE   B C   1 
ATOM   5401 O  O   . PHE   B 1 334 ? 0.205   10.371  1.997   1   42.35 ? 319 PHE   B O   1 
ATOM   5402 C  CB  . PHE   B 1 334 ? 3.31    11.533  2.132   1   41.15 ? 319 PHE   B CB  1 
ATOM   5403 C  CG  . PHE   B 1 334 ? 3.077   11.682  0.651   1   41.13 ? 319 PHE   B CG  1 
ATOM   5404 C  CD1 . PHE   B 1 334 ? 2.878   10.571  -0.15   1   41.43 ? 319 PHE   B CD1 1 
ATOM   5405 C  CD2 . PHE   B 1 334 ? 3.125   12.928  0.047   1   41.44 ? 319 PHE   B CD2 1 
ATOM   5406 C  CE1 . PHE   B 1 334 ? 2.692   10.705  -1.517  1   41.83 ? 319 PHE   B CE1 1 
ATOM   5407 C  CE2 . PHE   B 1 334 ? 2.943   13.059  -1.324  1   42.01 ? 319 PHE   B CE2 1 
ATOM   5408 C  CZ  . PHE   B 1 334 ? 2.738   11.945  -2.098  1   41.8  ? 319 PHE   B CZ  1 
ATOM   5409 N  N   . VAL   B 1 335 ? 1.644   9.107   3.151   1   40.22 ? 320 VAL   B N   1 
ATOM   5410 C  CA  . VAL   B 1 335 ? 0.938   7.861   2.91    1   39.74 ? 320 VAL   B CA  1 
ATOM   5411 C  C   . VAL   B 1 335 ? -0.462  7.871   3.553   1   40.53 ? 320 VAL   B C   1 
ATOM   5412 O  O   . VAL   B 1 335 ? -1.423  7.424   2.933   1   40.53 ? 320 VAL   B O   1 
ATOM   5413 C  CB  . VAL   B 1 335 ? 1.827   6.67    3.344   1   39.06 ? 320 VAL   B CB  1 
ATOM   5414 C  CG1 . VAL   B 1 335 ? 1.029   5.39    3.508   1   39.07 ? 320 VAL   B CG1 1 
ATOM   5415 C  CG2 . VAL   B 1 335 ? 2.969   6.479   2.356   1   39.28 ? 320 VAL   B CG2 1 
ATOM   5416 N  N   . LEU   B 1 336 ? -0.586  8.436   4.746   1   41.04 ? 321 LEU   B N   1 
ATOM   5417 C  CA  . LEU   B 1 336 ? -1.859  8.529   5.46    1   42.17 ? 321 LEU   B CA  1 
ATOM   5418 C  C   . LEU   B 1 336 ? -2.843  9.531   4.846   1   42.13 ? 321 LEU   B C   1 
ATOM   5419 O  O   . LEU   B 1 336 ? -4.05   9.424   5.069   1   42.84 ? 321 LEU   B O   1 
ATOM   5420 C  CB  . LEU   B 1 336 ? -1.611  8.928   6.924   1   42.84 ? 321 LEU   B CB  1 
ATOM   5421 C  CG  . LEU   B 1 336 ? -1.11   7.81    7.835   1   44.95 ? 321 LEU   B CG  1 
ATOM   5422 C  CD1 . LEU   B 1 336 ? -0.826  8.331   9.226   1   45.78 ? 321 LEU   B CD1 1 
ATOM   5423 C  CD2 . LEU   B 1 336 ? -2.128  6.687   7.906   1   45.8  ? 321 LEU   B CD2 1 
ATOM   5424 N  N   . SER   B 1 337 ? -2.337  10.513  4.115   1   41.6  ? 322 SER   B N   1 
ATOM   5425 C  CA  . SER   B 1 337 ? -3.173  11.555  3.538   1   41.4  ? 322 SER   B CA  1 
ATOM   5426 C  C   . SER   B 1 337 ? -3.733  11.23   2.156   1   41.16 ? 322 SER   B C   1 
ATOM   5427 O  O   . SER   B 1 337 ? -4.416  12.087  1.592   1   42.39 ? 322 SER   B O   1 
ATOM   5428 C  CB  . SER   B 1 337 ? -2.373  12.855  3.434   1   41.99 ? 322 SER   B CB  1 
ATOM   5429 O  OG  . SER   B 1 337 ? -1.517  12.866  2.299   1   43.51 ? 322 SER   B OG  1 
ATOM   5430 N  N   A LYS   B 1 338 ? -3.426  10.05   1.588   0.5 39.91 ? 323 LYS   B N   1 
ATOM   5431 N  N   B LYS   B 1 338 ? -3.433  10.046  1.593   0.5 40    ? 323 LYS   B N   1 
ATOM   5432 C  CA  A LYS   B 1 338 ? -3.847  9.745   0.226   0.5 39.18 ? 323 LYS   B CA  1 
ATOM   5433 C  CA  B LYS   B 1 338 ? -3.852  9.734   0.233   0.5 39.36 ? 323 LYS   B CA  1 
ATOM   5434 C  C   A LYS   B 1 338 ? -5.016  8.771   0.079   0.5 39.07 ? 323 LYS   B C   1 
ATOM   5435 C  C   B LYS   B 1 338 ? -5.028  8.779   0.085   0.5 39.15 ? 323 LYS   B C   1 
ATOM   5436 O  O   A LYS   B 1 338 ? -5.564  8.678   -1.021  0.5 39.26 ? 323 LYS   B O   1 
ATOM   5437 O  O   B LYS   B 1 338 ? -5.587  8.699   -1.011  0.5 39.36 ? 323 LYS   B O   1 
ATOM   5438 C  CB  A LYS   B 1 338 ? -2.656  9.241   -0.605  0.5 39.6  ? 323 LYS   B CB  1 
ATOM   5439 C  CB  B LYS   B 1 338 ? -2.668  9.199   -0.582  0.5 40.04 ? 323 LYS   B CB  1 
ATOM   5440 C  CG  A LYS   B 1 338 ? -1.523  10.266  -0.746  0.5 41.1  ? 323 LYS   B CG  1 
ATOM   5441 C  CG  B LYS   B 1 338 ? -1.535  10.212  -0.737  0.5 42.17 ? 323 LYS   B CG  1 
ATOM   5442 C  CD  A LYS   B 1 338 ? -1.924  11.496  -1.547  0.5 43.4  ? 323 LYS   B CD  1 
ATOM   5443 C  CD  B LYS   B 1 338 ? -0.811  10.04   -2.052  0.5 45.05 ? 323 LYS   B CD  1 
ATOM   5444 C  CE  A LYS   B 1 338 ? -0.852  12.561  -1.537  0.5 45.69 ? 323 LYS   B CE  1 
ATOM   5445 C  CE  B LYS   B 1 338 ? -1.618  10.652  -3.164  0.5 47.64 ? 323 LYS   B CE  1 
ATOM   5446 N  NZ  A LYS   B 1 338 ? -0.802  13.317  -2.818  0.5 47.08 ? 323 LYS   B NZ  1 
ATOM   5447 N  NZ  B LYS   B 1 338 ? -1.031  10.368  -4.49   0.5 48.99 ? 323 LYS   B NZ  1 
ATOM   5448 N  N   . GLY   B 1 339 ? -5.383  8.043   1.14    1   38.38 ? 324 GLY   B N   1 
ATOM   5449 C  CA  . GLY   B 1 339 ? -6.484  7.074   1.083   1   37.88 ? 324 GLY   B CA  1 
ATOM   5450 C  C   . GLY   B 1 339 ? -6.215  6.004   0.036   1   38.12 ? 324 GLY   B C   1 
ATOM   5451 O  O   . GLY   B 1 339 ? -7.03   5.764   -0.861  1   38.17 ? 324 GLY   B O   1 
ATOM   5452 N  N   . ASP   B 1 340 ? -4.993  5.462   0.071   1   37.16 ? 325 ASP   B N   1 
ATOM   5453 C  CA  . ASP   B 1 340 ? -4.491  4.543   -0.943  1   36.64 ? 325 ASP   B CA  1 
ATOM   5454 C  C   . ASP   B 1 340 ? -3.987  3.268   -0.281  1   36.93 ? 325 ASP   B C   1 
ATOM   5455 O  O   . ASP   B 1 340 ? -2.882  3.273   0.249   1   36.49 ? 325 ASP   B O   1 
ATOM   5456 C  CB  . ASP   B 1 340 ? -3.312  5.266   -1.61   1   37.5  ? 325 ASP   B CB  1 
ATOM   5457 C  CG  . ASP   B 1 340 ? -2.668  4.622   -2.807  1   40.16 ? 325 ASP   B CG  1 
ATOM   5458 O  OD1 . ASP   B 1 340 ? -2.566  3.38    -2.831  1   41.24 ? 325 ASP   B OD1 1 
ATOM   5459 O  OD2 . ASP   B 1 340 ? -2.231  5.358   -3.701  1   41.62 ? 325 ASP   B OD2 1 
ATOM   5460 N  N   . ALA   B 1 341 ? -4.748  2.176   -0.355  1   36.87 ? 326 ALA   B N   1 
ATOM   5461 C  CA  . ALA   B 1 341 ? -4.36   0.897   0.236   1   37.39 ? 326 ALA   B CA  1 
ATOM   5462 C  C   . ALA   B 1 341 ? -3.006  0.337   -0.251  1   38.36 ? 326 ALA   B C   1 
ATOM   5463 O  O   . ALA   B 1 341 ? -2.275  -0.232  0.552   1   38.29 ? 326 ALA   B O   1 
ATOM   5464 C  CB  . ALA   B 1 341 ? -5.456  -0.129  0.028   1   36.98 ? 326 ALA   B CB  1 
ATOM   5465 N  N   . GLY   B 1 342 ? -2.698  0.479   -1.539  1   38.51 ? 327 GLY   B N   1 
ATOM   5466 C  CA  . GLY   B 1 342 ? -1.439  -0.006  -2.091  1   38.88 ? 327 GLY   B CA  1 
ATOM   5467 C  C   . GLY   B 1 342 ? -0.24   0.703   -1.489  1   39.03 ? 327 GLY   B C   1 
ATOM   5468 O  O   . GLY   B 1 342 ? 0.774   0.078   -1.18   1   39.25 ? 327 GLY   B O   1 
ATOM   5469 N  N   . LEU   B 1 343 ? -0.359  2.018   -1.301  1   38.38 ? 328 LEU   B N   1 
ATOM   5470 C  CA  . LEU   B 1 343 ? 0.694   2.831   -0.72   1   38.21 ? 328 LEU   B CA  1 
ATOM   5471 C  C   . LEU   B 1 343 ? 0.859   2.476   0.756   1   38.77 ? 328 LEU   B C   1 
ATOM   5472 O  O   . LEU   B 1 343 ? 1.988   2.34    1.229   1   38.4  ? 328 LEU   B O   1 
ATOM   5473 C  CB  . LEU   B 1 343 ? 0.326   4.305   -0.884  1   38.04 ? 328 LEU   B CB  1 
ATOM   5474 C  CG  . LEU   B 1 343 ? 1.427   5.306   -1.183  1   39.26 ? 328 LEU   B CG  1 
ATOM   5475 C  CD1 . LEU   B 1 343 ? 2.42    4.799   -2.252  1   39.26 ? 328 LEU   B CD1 1 
ATOM   5476 C  CD2 . LEU   B 1 343 ? 0.837   6.649   -1.598  1   39.38 ? 328 LEU   B CD2 1 
ATOM   5477 N  N   . ARG   B 1 344 ? -0.257  2.3     1.483   1   39.3  ? 329 ARG   B N   1 
ATOM   5478 C  CA  . ARG   B 1 344 ? -0.222  1.916   2.894   1   39.85 ? 329 ARG   B CA  1 
ATOM   5479 C  C   . ARG   B 1 344 ? 0.399   0.533   3.049   1   40.91 ? 329 ARG   B C   1 
ATOM   5480 O  O   . ARG   B 1 344 ? 1.131   0.315   4.009   1   41.56 ? 329 ARG   B O   1 
ATOM   5481 C  CB  . ARG   B 1 344 ? -1.62   1.927   3.521   1   40.9  ? 329 ARG   B CB  1 
ATOM   5482 C  CG  . ARG   B 1 344 ? -2.218  3.325   3.679   1   43.85 ? 329 ARG   B CG  1 
ATOM   5483 C  CD  . ARG   B 1 344 ? -3.38   3.348   4.67    1   46.07 ? 329 ARG   B CD  1 
ATOM   5484 N  NE  . ARG   B 1 344 ? -4.433  2.388   4.313   1   46.61 ? 329 ARG   B NE  1 
ATOM   5485 C  CZ  . ARG   B 1 344 ? -5.45   2.662   3.493   1   46.23 ? 329 ARG   B CZ  1 
ATOM   5486 N  NH1 . ARG   B 1 344 ? -5.558  3.866   2.934   1   45.41 ? 329 ARG   B NH1 1 
ATOM   5487 N  NH2 . ARG   B 1 344 ? -6.357  1.73    3.216   1   43.05 ? 329 ARG   B NH2 1 
ATOM   5488 N  N   . GLU   B 1 345 ? 0.11    -0.404  2.125   1   41.04 ? 330 GLU   B N   1 
ATOM   5489 C  CA  . GLU   B 1 345 ? 0.681   -1.749  2.18    1   41.9  ? 330 GLU   B CA  1 
ATOM   5490 C  C   . GLU   B 1 345 ? 2.198   -1.707  1.93    1   41.08 ? 330 GLU   B C   1 
ATOM   5491 O  O   . GLU   B 1 345 ? 2.925   -2.495  2.513   1   41.92 ? 330 GLU   B O   1 
ATOM   5492 C  CB  . GLU   B 1 345 ? 0.019   -2.674  1.152   1   46.11 ? 330 GLU   B CB  1 
ATOM   5493 C  CG  . GLU   B 1 345 ? -1.34   -3.226  1.557   1   56.58 ? 330 GLU   B CG  1 
ATOM   5494 C  CD  . GLU   B 1 345 ? -2.176  -3.694  0.37    1   71.05 ? 330 GLU   B CD  1 
ATOM   5495 O  OE1 . GLU   B 1 345 ? -1.583  -4.007  -0.693  1   74.22 ? 330 GLU   B OE1 1 
ATOM   5496 O  OE2 . GLU   B 1 345 ? -3.424  -3.732  0.495   1   75.12 ? 330 GLU   B OE2 1 
ATOM   5497 N  N   . ALA   B 1 346 ? 2.664   -0.834  1.038   1   39.64 ? 331 ALA   B N   1 
ATOM   5498 C  CA  . ALA   B 1 346 ? 4.087   -0.698  0.725   1   38.78 ? 331 ALA   B CA  1 
ATOM   5499 C  C   . ALA   B 1 346 ? 4.832   -0.117  1.947   1   38.06 ? 331 ALA   B C   1 
ATOM   5500 O  O   . ALA   B 1 346 ? 5.938   -0.562  2.294   1   37.86 ? 331 ALA   B O   1 
ATOM   5501 C  CB  . ALA   B 1 346 ? 4.274   0.214   -0.489  1   38.39 ? 331 ALA   B CB  1 
ATOM   5502 N  N   . TYR   B 1 347 ? 4.207   0.858   2.61    1   37.07 ? 332 TYR   B N   1 
ATOM   5503 C  CA  . TYR   B 1 347 ? 4.749   1.489   3.798   1   35.69 ? 332 TYR   B CA  1 
ATOM   5504 C  C   . TYR   B 1 347 ? 4.818   0.438   4.922   1   36.23 ? 332 TYR   B C   1 
ATOM   5505 O  O   . TYR   B 1 347 ? 5.861   0.278   5.567   1   35.6  ? 332 TYR   B O   1 
ATOM   5506 C  CB  . TYR   B 1 347 ? 3.879   2.681   4.199   1   33.61 ? 332 TYR   B CB  1 
ATOM   5507 C  CG  . TYR   B 1 347 ? 4.221   3.234   5.562   1   32.05 ? 332 TYR   B CG  1 
ATOM   5508 C  CD1 . TYR   B 1 347 ? 3.661   2.698   6.71    1   31.98 ? 332 TYR   B CD1 1 
ATOM   5509 C  CD2 . TYR   B 1 347 ? 5.144   4.255   5.708   1   32.11 ? 332 TYR   B CD2 1 
ATOM   5510 C  CE1 . TYR   B 1 347 ? 3.999   3.17    7.965   1   31.81 ? 332 TYR   B CE1 1 
ATOM   5511 C  CE2 . TYR   B 1 347 ? 5.474   4.753   6.962   1   32.38 ? 332 TYR   B CE2 1 
ATOM   5512 C  CZ  . TYR   B 1 347 ? 4.91    4.192   8.09    1   32.86 ? 332 TYR   B CZ  1 
ATOM   5513 O  OH  . TYR   B 1 347 ? 5.251   4.663   9.341   1   34.06 ? 332 TYR   B OH  1 
ATOM   5514 N  N   . ASP   B 1 348 ? 3.731   -0.314  5.108   1   36.34 ? 333 ASP   B N   1 
ATOM   5515 C  CA  . ASP   B 1 348 ? 3.67    -1.373  6.121   1   36.55 ? 333 ASP   B CA  1 
ATOM   5516 C  C   . ASP   B 1 348 ? 4.643   -2.507  5.856   1   36.36 ? 333 ASP   B C   1 
ATOM   5517 O  O   . ASP   B 1 348 ? 5.038   -3.188  6.804   1   36.4  ? 333 ASP   B O   1 
ATOM   5518 C  CB  . ASP   B 1 348 ? 2.246   -1.936  6.269   1   38.63 ? 333 ASP   B CB  1 
ATOM   5519 C  CG  . ASP   B 1 348 ? 1.35    -1.154  7.206   1   43.61 ? 333 ASP   B CG  1 
ATOM   5520 O  OD1 . ASP   B 1 348 ? 1.787   -0.1    7.709   1   44.49 ? 333 ASP   B OD1 1 
ATOM   5521 O  OD2 . ASP   B 1 348 ? 0.216   -1.609  7.464   1   47.04 ? 333 ASP   B OD2 1 
ATOM   5522 N  N   . ALA   B 1 349 ? 5.016   -2.733  4.591   1   35.83 ? 334 ALA   B N   1 
ATOM   5523 C  CA  . ALA   B 1 349 ? 5.979   -3.777  4.271   1   35.98 ? 334 ALA   B CA  1 
ATOM   5524 C  C   . ALA   B 1 349 ? 7.371   -3.375  4.825   1   36.11 ? 334 ALA   B C   1 
ATOM   5525 O  O   . ALA   B 1 349 ? 8.116   -4.241  5.278   1   37.38 ? 334 ALA   B O   1 
ATOM   5526 C  CB  . ALA   B 1 349 ? 6.035   -4.001  2.769   1   35.84 ? 334 ALA   B CB  1 
ATOM   5527 N  N   . CYS   B 1 350 ? 7.706   -2.067  4.826   1   34.45 ? 335 CYS   B N   1 
ATOM   5528 C  CA  . CYS   B 1 350 ? 8.966   -1.591  5.369   1   33.93 ? 335 CYS   B CA  1 
ATOM   5529 C  C   . CYS   B 1 350 ? 8.942   -1.739  6.885   1   34.39 ? 335 CYS   B C   1 
ATOM   5530 O  O   . CYS   B 1 350 ? 9.908   -2.226  7.471   1   34.9  ? 335 CYS   B O   1 
ATOM   5531 C  CB  . CYS   B 1 350 ? 9.232   -0.148  4.95    1   33.51 ? 335 CYS   B CB  1 
ATOM   5532 S  SG  . CYS   B 1 350 ? 9.46    0.063   3.168   1   35.52 ? 335 CYS   B SG  1 
ATOM   5533 N  N   . VAL   B 1 351 ? 7.84    -1.343  7.52    1   33.82 ? 336 VAL   B N   1 
ATOM   5534 C  CA  . VAL   B 1 351 ? 7.697   -1.418  8.976   1   33.74 ? 336 VAL   B CA  1 
ATOM   5535 C  C   . VAL   B 1 351 ? 7.77    -2.87   9.426   1   34.21 ? 336 VAL   B C   1 
ATOM   5536 O  O   . VAL   B 1 351 ? 8.495   -3.183  10.382  1   34.93 ? 336 VAL   B O   1 
ATOM   5537 C  CB  . VAL   B 1 351 ? 6.381   -0.736  9.443   1   34.36 ? 336 VAL   B CB  1 
ATOM   5538 C  CG1 . VAL   B 1 351 ? 6.186   -0.907  10.942  1   34.86 ? 336 VAL   B CG1 1 
ATOM   5539 C  CG2 . VAL   B 1 351 ? 6.363   0.747   9.061   1   34.36 ? 336 VAL   B CG2 1 
ATOM   5540 N  N   . LYS   B 1 352 ? 7.088   -3.771  8.695   1   33.41 ? 337 LYS   B N   1 
ATOM   5541 C  CA  . LYS   B 1 352 ? 7.119   -5.205  9.023   1   33.55 ? 337 LYS   B CA  1 
ATOM   5542 C  C   . LYS   B 1 352 ? 8.543   -5.773  8.929   1   32.36 ? 337 LYS   B C   1 
ATOM   5543 O  O   . LYS   B 1 352 ? 8.92    -6.618  9.747   1   31.26 ? 337 LYS   B O   1 
ATOM   5544 C  CB  . LYS   B 1 352 ? 6.2     -6.021  8.103   1   37    ? 337 LYS   B CB  1 
ATOM   5545 C  CG  . LYS   B 1 352 ? 4.741   -6.009  8.528   1   43.83 ? 337 LYS   B CG  1 
ATOM   5546 C  CD  . LYS   B 1 352 ? 3.756   -6.577  7.483   1   48.08 ? 337 LYS   B CD  1 
ATOM   5547 C  CE  . LYS   B 1 352 ? 2.377   -6.656  8.102   1   51.83 ? 337 LYS   B CE  1 
ATOM   5548 N  NZ  . LYS   B 1 352 ? 2.427   -7.156  9.524   1   54.69 ? 337 LYS   B NZ  1 
ATOM   5549 N  N   . ALA   B 1 353 ? 9.303   -5.362  7.911   1   31.59 ? 338 ALA   B N   1 
ATOM   5550 C  CA  . ALA   B 1 353 ? 10.676  -5.84   7.749   1   31.84 ? 338 ALA   B CA  1 
ATOM   5551 C  C   . ALA   B 1 353 ? 11.544  -5.436  8.933   1   32.51 ? 338 ALA   B C   1 
ATOM   5552 O  O   . ALA   B 1 353 ? 12.349  -6.239  9.39    1   34.09 ? 338 ALA   B O   1 
ATOM   5553 C  CB  . ALA   B 1 353 ? 11.262  -5.316  6.462   1   32.18 ? 338 ALA   B CB  1 
ATOM   5554 N  N   . LEU   B 1 354 ? 11.33   -4.221  9.483   1   31.25 ? 339 LEU   B N   1 
ATOM   5555 C  CA  . LEU   B 1 354 ? 12.072  -3.731  10.633  1   31.66 ? 339 LEU   B CA  1 
ATOM   5556 C  C   . LEU   B 1 354 ? 11.685  -4.528  11.854  1   30.84 ? 339 LEU   B C   1 
ATOM   5557 O  O   . LEU   B 1 354 ? 12.568  -4.889  12.619  1   31.06 ? 339 LEU   B O   1 
ATOM   5558 C  CB  . LEU   B 1 354 ? 11.749  -2.258  10.872  1   32.52 ? 339 LEU   B CB  1 
ATOM   5559 C  CG  . LEU   B 1 354 ? 12.777  -1.158  10.752  1   35.38 ? 339 LEU   B CG  1 
ATOM   5560 C  CD1 . LEU   B 1 354 ? 14.106  -1.546  10.029  1   36.04 ? 339 LEU   B CD1 1 
ATOM   5561 C  CD2 . LEU   B 1 354 ? 12.12   0.139   10.335  1   36.13 ? 339 LEU   B CD2 1 
ATOM   5562 N  N   . VAL   B 1 355 ? 10.372  -4.828  12.029  1   29.45 ? 340 VAL   B N   1 
ATOM   5563 C  CA  . VAL   B 1 355 ? 9.885   -5.616  13.156  1   28.18 ? 340 VAL   B CA  1 
ATOM   5564 C  C   . VAL   B 1 355 ? 10.516  -7.024  13.083  1   27.24 ? 340 VAL   B C   1 
ATOM   5565 O  O   . VAL   B 1 355 ? 10.907  -7.563  14.109  1   27.33 ? 340 VAL   B O   1 
ATOM   5566 C  CB  . VAL   B 1 355 ? 8.343   -5.703  13.2    1   27.57 ? 340 VAL   B CB  1 
ATOM   5567 C  CG1 . VAL   B 1 355 ? 7.897   -6.677  14.283  1   26.9  ? 340 VAL   B CG1 1 
ATOM   5568 C  CG2 . VAL   B 1 355 ? 7.691   -4.331  13.431  1   27.45 ? 340 VAL   B CG2 1 
ATOM   5569 N  N   . SER   B 1 356 ? 10.597  -7.613  11.891  1   26.99 ? 341 SER   B N   1 
ATOM   5570 C  CA  . SER   B 1 356 ? 11.2    -8.955  11.735  1   29.68 ? 341 SER   B CA  1 
ATOM   5571 C  C   . SER   B 1 356 ? 12.711  -8.982  12.104  1   30.36 ? 341 SER   B C   1 
ATOM   5572 O  O   . SER   B 1 356 ? 13.209  -9.939  12.726  1   31.28 ? 341 SER   B O   1 
ATOM   5573 C  CB  . SER   B 1 356 ? 10.988  -9.477  10.314  1   32.13 ? 341 SER   B CB  1 
ATOM   5574 O  OG  . SER   B 1 356 ? 9.592   -9.473  10.05   1   37.81 ? 341 SER   B OG  1 
ATOM   5575 N  N   . LEU   B 1 357 ? 13.429  -7.924  11.738  1   29.7  ? 342 LEU   B N   1 
ATOM   5576 C  CA  . LEU   B 1 357 ? 14.839  -7.802  12.065  1   29.93 ? 342 LEU   B CA  1 
ATOM   5577 C  C   . LEU   B 1 357 ? 14.981  -7.684  13.589  1   29.95 ? 342 LEU   B C   1 
ATOM   5578 O  O   . LEU   B 1 357 ? 15.731  -8.467  14.177  1   30.81 ? 342 LEU   B O   1 
ATOM   5579 C  CB  . LEU   B 1 357 ? 15.437  -6.576  11.388  1   30.55 ? 342 LEU   B CB  1 
ATOM   5580 C  CG  . LEU   B 1 357 ? 15.667  -6.715  9.899   1   32.18 ? 342 LEU   B CG  1 
ATOM   5581 C  CD1 . LEU   B 1 357 ? 15.918  -5.341  9.28    1   31.64 ? 342 LEU   B CD1 1 
ATOM   5582 C  CD2 . LEU   B 1 357 ? 16.846  -7.616  9.656   1   34.2  ? 342 LEU   B CD2 1 
ATOM   5583 N  N   . ARG   B 1 358 ? 14.197  -6.795  14.223  1   28.22 ? 343 ARG   B N   1 
ATOM   5584 C  CA  . ARG   B 1 358 ? 14.284  -6.622  15.653  1   28.1  ? 343 ARG   B CA  1 
ATOM   5585 C  C   . ARG   B 1 358 ? 13.824  -7.864  16.423  1   28.64 ? 343 ARG   B C   1 
ATOM   5586 O  O   . ARG   B 1 358 ? 14.376  -8.146  17.484  1   28.48 ? 343 ARG   B O   1 
ATOM   5587 C  CB  . ARG   B 1 358 ? 13.568  -5.336  16.108  1   29.14 ? 343 ARG   B CB  1 
ATOM   5588 C  CG  . ARG   B 1 358 ? 14.258  -4.091  15.545  1   28.35 ? 343 ARG   B CG  1 
ATOM   5589 C  CD  . ARG   B 1 358 ? 13.521  -2.768  15.814  1   29.42 ? 343 ARG   B CD  1 
ATOM   5590 N  NE  . ARG   B 1 358 ? 14.486  -1.683  15.732  1   32.88 ? 343 ARG   B NE  1 
ATOM   5591 C  CZ  . ARG   B 1 358 ? 14.296  -0.536  15.091  1   34.42 ? 343 ARG   B CZ  1 
ATOM   5592 N  NH1 . ARG   B 1 358 ? 13.125  -0.274  14.514  1   30.93 ? 343 ARG   B NH1 1 
ATOM   5593 N  NH2 . ARG   B 1 358 ? 15.249  0.384   15.076  1   33.84 ? 343 ARG   B NH2 1 
ATOM   5594 N  N   . SER   B 1 359 ? 12.834  -8.611  15.906  1   29.19 ? 344 SER   B N   1 
ATOM   5595 C  CA  . SER   B 1 359 ? 12.369  -9.834  16.566  1   30.15 ? 344 SER   B CA  1 
ATOM   5596 C  C   . SER   B 1 359 ? 13.467  -10.919 16.512  1   30.12 ? 344 SER   B C   1 
ATOM   5597 O  O   . SER   B 1 359 ? 13.728  -11.582 17.522  1   29.73 ? 344 SER   B O   1 
ATOM   5598 C  CB  . SER   B 1 359 ? 11.083  -10.354 15.921  1   31.45 ? 344 SER   B CB  1 
ATOM   5599 O  OG  . SER   B 1 359 ? 10.021  -9.453  16.179  1   35.61 ? 344 SER   B OG  1 
ATOM   5600 N  N   . TYR   B 1 360 ? 14.11   -11.093 15.352  1   30.38 ? 345 TYR   B N   1 
ATOM   5601 C  CA  . TYR   B 1 360 ? 15.19   -12.059 15.244  1   32.05 ? 345 TYR   B CA  1 
ATOM   5602 C  C   . TYR   B 1 360 ? 16.36   -11.66  16.167  1   31.98 ? 345 TYR   B C   1 
ATOM   5603 O  O   . TYR   B 1 360 ? 16.89   -12.502 16.91   1   33.13 ? 345 TYR   B O   1 
ATOM   5604 C  CB  . TYR   B 1 360 ? 15.677  -12.171 13.812  1   33.21 ? 345 TYR   B CB  1 
ATOM   5605 C  CG  . TYR   B 1 360 ? 16.566  -13.379 13.659  1   34.49 ? 345 TYR   B CG  1 
ATOM   5606 C  CD1 . TYR   B 1 360 ? 16.04   -14.664 13.723  1   35.74 ? 345 TYR   B CD1 1 
ATOM   5607 C  CD2 . TYR   B 1 360 ? 17.946  -13.246 13.576  1   34.67 ? 345 TYR   B CD2 1 
ATOM   5608 C  CE1 . TYR   B 1 360 ? 16.856  -15.782 13.611  1   36.77 ? 345 TYR   B CE1 1 
ATOM   5609 C  CE2 . TYR   B 1 360 ? 18.773  -14.355 13.451  1   35.92 ? 345 TYR   B CE2 1 
ATOM   5610 C  CZ  . TYR   B 1 360 ? 18.227  -15.625 13.485  1   37.54 ? 345 TYR   B CZ  1 
ATOM   5611 O  OH  . TYR   B 1 360 ? 19.029  -16.743 13.372  1   39.02 ? 345 TYR   B OH  1 
ATOM   5612 N  N   . HIS   B 1 361 ? 16.677  -10.361 16.207  1   30.21 ? 346 HIS   B N   1 
ATOM   5613 C  CA  . HIS   B 1 361 ? 17.72   -9.818  17.054  1   29.4  ? 346 HIS   B CA  1 
ATOM   5614 C  C   . HIS   B 1 361 ? 17.432  -10.1   18.528  1   29.22 ? 346 HIS   B C   1 
ATOM   5615 O  O   . HIS   B 1 361 ? 18.35   -10.494 19.267  1   29.94 ? 346 HIS   B O   1 
ATOM   5616 C  CB  . HIS   B 1 361 ? 17.892  -8.304  16.776  1   28.56 ? 346 HIS   B CB  1 
ATOM   5617 C  CG  . HIS   B 1 361 ? 18.954  -7.634  17.583  1   27.25 ? 346 HIS   B CG  1 
ATOM   5618 N  ND1 . HIS   B 1 361 ? 18.642  -6.902  18.708  1   28.75 ? 346 HIS   B ND1 1 
ATOM   5619 C  CD2 . HIS   B 1 361 ? 20.281  -7.53   17.348  1   26.48 ? 346 HIS   B CD2 1 
ATOM   5620 C  CE1 . HIS   B 1 361 ? 19.786  -6.395  19.14   1   28.07 ? 346 HIS   B CE1 1 
ATOM   5621 N  NE2 . HIS   B 1 361 ? 20.806  -6.776  18.369  1   28.87 ? 346 HIS   B NE2 1 
ATOM   5622 N  N   . LEU   B 1 362 ? 16.178  -9.989  18.952  1   28.14 ? 347 LEU   B N   1 
ATOM   5623 C  CA  . LEU   B 1 362 ? 15.808  -10.293 20.345  1   28.09 ? 347 LEU   B CA  1 
ATOM   5624 C  C   . LEU   B 1 362 ? 16.042  -11.781 20.658  1   27.72 ? 347 LEU   B C   1 
ATOM   5625 O  O   . LEU   B 1 362 ? 16.459  -12.099 21.777  1   28.32 ? 347 LEU   B O   1 
ATOM   5626 C  CB  . LEU   B 1 362 ? 14.362  -9.925  20.63   1   28.31 ? 347 LEU   B CB  1 
ATOM   5627 C  CG  . LEU   B 1 362 ? 14.134  -8.505  21.089  1   30.62 ? 347 LEU   B CG  1 
ATOM   5628 C  CD1 . LEU   B 1 362 ? 12.68   -8.055  20.78   1   32.27 ? 347 LEU   B CD1 1 
ATOM   5629 C  CD2 . LEU   B 1 362 ? 14.384  -8.406  22.583  1   31.17 ? 347 LEU   B CD2 1 
ATOM   5630 N  N   . GLN   B 1 363 ? 15.851  -12.669 19.685  1   26.8  ? 348 GLN   B N   1 
ATOM   5631 C  CA  . GLN   B 1 363 ? 16.108  -14.102 19.908  1   28.61 ? 348 GLN   B CA  1 
ATOM   5632 C  C   . GLN   B 1 363 ? 17.598  -14.341 20.068  1   29.43 ? 348 GLN   B C   1 
ATOM   5633 O  O   . GLN   B 1 363 ? 17.999  -15.213 20.835  1   29.58 ? 348 GLN   B O   1 
ATOM   5634 C  CB  . GLN   B 1 363 ? 15.616  -14.956 18.733  1   30.11 ? 348 GLN   B CB  1 
ATOM   5635 C  CG  . GLN   B 1 363 ? 14.127  -14.845 18.444  1   33.44 ? 348 GLN   B CG  1 
ATOM   5636 C  CD  . GLN   B 1 363 ? 13.811  -15.722 17.265  1   39.14 ? 348 GLN   B CD  1 
ATOM   5637 O  OE1 . GLN   B 1 363 ? 14.275  -16.868 17.171  1   42.3  ? 348 GLN   B OE1 1 
ATOM   5638 N  NE2 . GLN   B 1 363 ? 13.044  -15.202 16.341  1   40.2  ? 348 GLN   B NE2 1 
ATOM   5639 N  N   . ILE   B 1 364 ? 18.436  -13.6   19.3    1   28.85 ? 349 ILE   B N   1 
ATOM   5640 C  CA  . ILE   B 1 364 ? 19.89   -13.685 19.425  1   28.58 ? 349 ILE   B CA  1 
ATOM   5641 C  C   . ILE   B 1 364 ? 20.285  -13.255 20.834  1   27.8  ? 349 ILE   B C   1 
ATOM   5642 O  O   . ILE   B 1 364 ? 21.085  -13.926 21.462  1   28.76 ? 349 ILE   B O   1 
ATOM   5643 C  CB  . ILE   B 1 364 ? 20.536  -12.788 18.358  1   29.32 ? 349 ILE   B CB  1 
ATOM   5644 C  CG1 . ILE   B 1 364 ? 20.389  -13.44  16.98   1   30.26 ? 349 ILE   B CG1 1 
ATOM   5645 C  CG2 . ILE   B 1 364 ? 22.02   -12.413 18.701  1   30.07 ? 349 ILE   B CG2 1 
ATOM   5646 C  CD1 . ILE   B 1 364 ? 20.754  -12.497 15.864  1   33.35 ? 349 ILE   B CD1 1 
ATOM   5647 N  N   . VAL   B 1 365 ? 19.73   -12.159 21.325  1   26.1  ? 350 VAL   B N   1 
ATOM   5648 C  CA  . VAL   B 1 365 ? 20.072  -11.639 22.65   1   25.1  ? 350 VAL   B CA  1 
ATOM   5649 C  C   . VAL   B 1 365 ? 19.683  -12.597 23.782  1   26.54 ? 350 VAL   B C   1 
ATOM   5650 O  O   . VAL   B 1 365 ? 20.421  -12.709 24.78   1   28.08 ? 350 VAL   B O   1 
ATOM   5651 C  CB  . VAL   B 1 365 ? 19.517  -10.213 22.856  1   25.36 ? 350 VAL   B CB  1 
ATOM   5652 C  CG1 . VAL   B 1 365 ? 19.821  -9.715  24.259  1   26.07 ? 350 VAL   B CG1 1 
ATOM   5653 C  CG2 . VAL   B 1 365 ? 20.127  -9.25   21.845  1   24.43 ? 350 VAL   B CG2 1 
ATOM   5654 N  N   . THR   B 1 366 ? 18.566  -13.317 23.646  1   26.12 ? 351 THR   B N   1 
ATOM   5655 C  CA  . THR   B 1 366 ? 18.185  -14.331 24.644  1   27.4  ? 351 THR   B CA  1 
ATOM   5656 C  C   . THR   B 1 366 ? 19.28   -15.446 24.691  1   29.15 ? 351 THR   B C   1 
ATOM   5657 O  O   . THR   B 1 366 ? 19.742  -15.83  25.775  1   30.58 ? 351 THR   B O   1 
ATOM   5658 C  CB  . THR   B 1 366 ? 16.844  -14.959 24.194  1   28.79 ? 351 THR   B CB  1 
ATOM   5659 O  OG1 . THR   B 1 366 ? 15.847  -13.948 24.099  1   30.22 ? 351 THR   B OG1 1 
ATOM   5660 C  CG2 . THR   B 1 366 ? 16.421  -16.118 25.05   1   27.64 ? 351 THR   B CG2 1 
ATOM   5661 N  N   . LYS   B 1 367 ? 19.73   -15.917 23.514  1   28.53 ? 352 LYS   B N   1 
ATOM   5662 C  CA  . LYS   B 1 367 ? 20.783  -16.931 23.453  1   29.53 ? 352 LYS   B CA  1 
ATOM   5663 C  C   . LYS   B 1 367 ? 22.185  -16.407 23.891  1   29.94 ? 352 LYS   B C   1 
ATOM   5664 O  O   . LYS   B 1 367 ? 22.914  -17.13  24.551  1   30.37 ? 352 LYS   B O   1 
ATOM   5665 C  CB  . LYS   B 1 367 ? 20.876  -17.497 22.017  1   30.62 ? 352 LYS   B CB  1 
ATOM   5666 C  CG  . LYS   B 1 367 ? 22.076  -18.428 21.761  1   32.03 ? 352 LYS   B CG  1 
ATOM   5667 C  CD  . LYS   B 1 367 ? 22.032  -19.038 20.381  1   34.93 ? 352 LYS   B CD  1 
ATOM   5668 C  CE  . LYS   B 1 367 ? 23.311  -19.781 20.056  1   37.66 ? 352 LYS   B CE  1 
ATOM   5669 N  NZ  . LYS   B 1 367 ? 23.276  -20.317 18.672  1   38.99 ? 352 LYS   B NZ  1 
ATOM   5670 N  N   . TYR   B 1 368 ? 22.589  -15.193 23.464  1   29.13 ? 353 TYR   B N   1 
ATOM   5671 C  CA  . TYR   B 1 368 ? 23.932  -14.688 23.702  1   28.01 ? 353 TYR   B CA  1 
ATOM   5672 C  C   . TYR   B 1 368 ? 24.109  -13.928 25.001  1   28.54 ? 353 TYR   B C   1 
ATOM   5673 O  O   . TYR   B 1 368 ? 25.24   -13.778 25.433  1   29.74 ? 353 TYR   B O   1 
ATOM   5674 C  CB  . TYR   B 1 368 ? 24.428  -13.855 22.512  1   27.41 ? 353 TYR   B CB  1 
ATOM   5675 C  CG  . TYR   B 1 368 ? 24.803  -14.761 21.36   1   28.24 ? 353 TYR   B CG  1 
ATOM   5676 C  CD1 . TYR   B 1 368 ? 23.84   -15.228 20.476  1   29.64 ? 353 TYR   B CD1 1 
ATOM   5677 C  CD2 . TYR   B 1 368 ? 26.09   -15.268 21.241  1   29.22 ? 353 TYR   B CD2 1 
ATOM   5678 C  CE1 . TYR   B 1 368 ? 24.168  -16.105 19.45   1   30.94 ? 353 TYR   B CE1 1 
ATOM   5679 C  CE2 . TYR   B 1 368 ? 26.412  -16.202 20.264  1   30.44 ? 353 TYR   B CE2 1 
ATOM   5680 C  CZ  . TYR   B 1 368 ? 25.459  -16.599 19.357  1   31.83 ? 353 TYR   B CZ  1 
ATOM   5681 O  OH  . TYR   B 1 368 ? 25.804  -17.501 18.38   1   34.05 ? 353 TYR   B OH  1 
ATOM   5682 N  N   . ILE   B 1 369 ? 23.026  -13.418 25.61   1   28.18 ? 354 ILE   B N   1 
ATOM   5683 C  CA  . ILE   B 1 369 ? 23.14   -12.681 26.853  1   28.68 ? 354 ILE   B CA  1 
ATOM   5684 C  C   . ILE   B 1 369 ? 22.295  -13.293 27.977  1   29.28 ? 354 ILE   B C   1 
ATOM   5685 O  O   . ILE   B 1 369 ? 22.835  -13.603 29.05   1   28.43 ? 354 ILE   B O   1 
ATOM   5686 C  CB  . ILE   B 1 369 ? 22.872  -11.16  26.657  1   30.61 ? 354 ILE   B CB  1 
ATOM   5687 C  CG1 . ILE   B 1 369 ? 24.015  -10.513 25.83   1   33.35 ? 354 ILE   B CG1 1 
ATOM   5688 C  CG2 . ILE   B 1 369 ? 22.703  -10.439 28.027  1   30.91 ? 354 ILE   B CG2 1 
ATOM   5689 C  CD1 . ILE   B 1 369 ? 23.85   -9.094  25.51   1   35.73 ? 354 ILE   B CD1 1 
ATOM   5690 N  N   . LEU   B 1 370 ? 20.975  -13.446 27.756  1   29.34 ? 355 LEU   B N   1 
ATOM   5691 C  CA  . LEU   B 1 370 ? 20.08   -13.921 28.801  1   30.73 ? 355 LEU   B CA  1 
ATOM   5692 C  C   . LEU   B 1 370 ? 20.442  -15.292 29.396  1   29.37 ? 355 LEU   B C   1 
ATOM   5693 O  O   . LEU   B 1 370 ? 20.562  -15.442 30.624  1   28.93 ? 355 LEU   B O   1 
ATOM   5694 C  CB  . LEU   B 1 370 ? 18.638  -13.922 28.263  1   31.78 ? 355 LEU   B CB  1 
ATOM   5695 C  CG  . LEU   B 1 370 ? 17.581  -13.47  29.22   1   35.02 ? 355 LEU   B CG  1 
ATOM   5696 C  CD1 . LEU   B 1 370 ? 17.803  -12.011 29.643  1   35.66 ? 355 LEU   B CD1 1 
ATOM   5697 C  CD2 . LEU   B 1 370 ? 16.208  -13.656 28.587  1   36.73 ? 355 LEU   B CD2 1 
ATOM   5698 N  N   . ILE   B 1 371 ? 20.61   -16.284 28.528  1   28.22 ? 356 ILE   B N   1 
ATOM   5699 C  CA  . ILE   B 1 371 ? 20.909  -17.631 28.984  1   29.27 ? 356 ILE   B CA  1 
ATOM   5700 C  C   . ILE   B 1 371 ? 22.325  -17.69  29.635  1   31.2  ? 356 ILE   B C   1 
ATOM   5701 O  O   . ILE   B 1 371 ? 22.396  -18.055 30.822  1   31.48 ? 356 ILE   B O   1 
ATOM   5702 C  CB  . ILE   B 1 371 ? 20.651  -18.645 27.852  1   29.58 ? 356 ILE   B CB  1 
ATOM   5703 C  CG1 . ILE   B 1 371 ? 19.121  -18.695 27.516  1   30.05 ? 356 ILE   B CG1 1 
ATOM   5704 C  CG2 . ILE   B 1 371 ? 21.23   -20.027 28.226  1   31.11 ? 356 ILE   B CG2 1 
ATOM   5705 C  CD1 . ILE   B 1 371 ? 18.747  -19.554 26.385  1   30.94 ? 356 ILE   B CD1 1 
ATOM   5706 N  N   . PRO   B 1 372 ? 23.407  -17.162 29.019  1   32.11 ? 357 PRO   B N   1 
ATOM   5707 C  CA  . PRO   B 1 372 ? 24.713  -17.163 29.715  1   32.96 ? 357 PRO   B CA  1 
ATOM   5708 C  C   . PRO   B 1 372 ? 24.707  -16.427 31.048  1   35.13 ? 357 PRO   B C   1 
ATOM   5709 O  O   . PRO   B 1 372 ? 25.339  -16.911 31.972  1   35.23 ? 357 PRO   B O   1 
ATOM   5710 C  CB  . PRO   B 1 372 ? 25.655  -16.49  28.721  1   33.38 ? 357 PRO   B CB  1 
ATOM   5711 C  CG  . PRO   B 1 372 ? 25.042  -16.76  27.39   1   32.83 ? 357 PRO   B CG  1 
ATOM   5712 C  CD  . PRO   B 1 372 ? 23.549  -16.668 27.634  1   31.41 ? 357 PRO   B CD  1 
ATOM   5713 N  N   . ALA   B 1 373 ? 23.958  -15.315 31.187  1   36.4  ? 358 ALA   B N   1 
ATOM   5714 C  CA  . ALA   B 1 373 ? 23.864  -14.62  32.474  1   38.59 ? 358 ALA   B CA  1 
ATOM   5715 C  C   . ALA   B 1 373 ? 23.253  -15.521 33.559  1   41.38 ? 358 ALA   B C   1 
ATOM   5716 O  O   . ALA   B 1 373 ? 23.558  -15.358 34.741  1   41.88 ? 358 ALA   B O   1 
ATOM   5717 C  CB  . ALA   B 1 373 ? 23.028  -13.356 32.333  1   38.54 ? 358 ALA   B CB  1 
ATOM   5718 N  N   . SER   B 1 374 ? 22.336  -16.421 33.165  1   42.89 ? 359 SER   B N   1 
ATOM   5719 C  CA  . SER   B 1 374 ? 21.682  -17.335 34.101  1   44.68 ? 359 SER   B CA  1 
ATOM   5720 C  C   . SER   B 1 374 ? 22.635  -18.459 34.564  1   47.78 ? 359 SER   B C   1 
ATOM   5721 O  O   . SER   B 1 374 ? 22.472  -18.984 35.662  1   48.13 ? 359 SER   B O   1 
ATOM   5722 C  CB  . SER   B 1 374 ? 20.411  -17.918 33.476  1   44.01 ? 359 SER   B CB  1 
ATOM   5723 O  OG  . SER   B 1 374 ? 20.669  -18.934 32.518  1   43.96 ? 359 SER   B OG  1 
ATOM   5724 N  N   . GLN   B 1 375 ? 23.625  -18.819 33.735  1   49.99 ? 360 GLN   B N   1 
ATOM   5725 C  CA  . GLN   B 1 375 ? 24.573  -19.881 34.056  1   52.41 ? 360 GLN   B CA  1 
ATOM   5726 C  C   . GLN   B 1 375 ? 25.88   -19.371 34.665  1   55.23 ? 360 GLN   B C   1 
ATOM   5727 O  O   . GLN   B 1 375 ? 26.837  -20.142 34.699  1   55.8  ? 360 GLN   B O   1 
ATOM   5728 C  CB  . GLN   B 1 375 ? 24.922  -20.683 32.798  1   53.72 ? 360 GLN   B CB  1 
ATOM   5729 C  CG  . GLN   B 1 375 ? 23.742  -21.287 32.064  1   57.63 ? 360 GLN   B CG  1 
ATOM   5730 C  CD  . GLN   B 1 375 ? 24.056  -21.516 30.595  1   62.87 ? 360 GLN   B CD  1 
ATOM   5731 O  OE1 . GLN   B 1 375 ? 24.937  -20.875 29.999  1   64.31 ? 360 GLN   B OE1 1 
ATOM   5732 N  NE2 . GLN   B 1 375 ? 23.325  -22.423 29.963  1   63.36 ? 360 GLN   B NE2 1 
ATOM   5733 N  N   . GLN   B 1 376 ? 25.96   -18.098 35.094  1   56.83 ? 361 GLN   B N   1 
ATOM   5734 C  CA  . GLN   B 1 376 ? 27.22   -17.585 35.633  1   58.9  ? 361 GLN   B CA  1 
ATOM   5735 C  C   . GLN   B 1 376 ? 27.293  -17.667 37.156  1   60.5  ? 361 GLN   B C   1 
ATOM   5736 O  O   . GLN   B 1 376 ? 28.389  -17.857 37.705  1   61.26 ? 361 GLN   B O   1 
ATOM   5737 C  CB  . GLN   B 1 376 ? 27.542  -16.17  35.121  1   61.01 ? 361 GLN   B CB  1 
ATOM   5738 C  CG  . GLN   B 1 376 ? 26.648  -15.067 35.681  1   65.58 ? 361 GLN   B CG  1 
ATOM   5739 C  CD  . GLN   B 1 376 ? 27.134  -13.665 35.343  1   71.23 ? 361 GLN   B CD  1 
ATOM   5740 O  OE1 . GLN   B 1 376 ? 28.177  -13.465 34.694  1   73.37 ? 361 GLN   B OE1 1 
ATOM   5741 N  NE2 . GLN   B 1 376 ? 26.389  -12.657 35.784  1   71.65 ? 361 GLN   B NE2 1 
ATOM   5742 N  N   . GLY   B 1 395 ? 19.727  -9.942  35.096  1   51.37 ? 380 GLY   B N   1 
ATOM   5743 C  CA  . GLY   B 1 395 ? 20.828  -10.343 34.229  1   51.64 ? 380 GLY   B CA  1 
ATOM   5744 C  C   . GLY   B 1 395 ? 20.485  -10.214 32.756  1   51.49 ? 380 GLY   B C   1 
ATOM   5745 O  O   . GLY   B 1 395 ? 20.237  -11.225 32.083  1   51.4  ? 380 GLY   B O   1 
ATOM   5746 N  N   . GLY   B 1 396 ? 20.466  -8.968  32.258  1   50.64 ? 381 GLY   B N   1 
ATOM   5747 C  CA  . GLY   B 1 396 ? 20.109  -8.675  30.871  1   50.31 ? 381 GLY   B CA  1 
ATOM   5748 C  C   . GLY   B 1 396 ? 18.649  -8.279  30.667  1   49.86 ? 381 GLY   B C   1 
ATOM   5749 O  O   . GLY   B 1 396 ? 18.256  -7.904  29.561  1   49.93 ? 381 GLY   B O   1 
ATOM   5750 N  N   . THR   B 1 397 ? 17.833  -8.334  31.731  1   48.93 ? 382 THR   B N   1 
ATOM   5751 C  CA  . THR   B 1 397 ? 16.425  -7.947  31.706  1   49.17 ? 382 THR   B CA  1 
ATOM   5752 C  C   . THR   B 1 397 ? 16.24   -6.484  31.24   1   48.41 ? 382 THR   B C   1 
ATOM   5753 O  O   . THR   B 1 397 ? 15.363  -6.218  30.422  1   48.77 ? 382 THR   B O   1 
ATOM   5754 C  CB  . THR   B 1 397 ? 15.776  -8.253  33.064  1   51.58 ? 382 THR   B CB  1 
ATOM   5755 O  OG1 . THR   B 1 397 ? 15.795  -9.673  33.256  1   53.14 ? 382 THR   B OG1 1 
ATOM   5756 C  CG2 . THR   B 1 397 ? 14.347  -7.726  33.172  1   52.12 ? 382 THR   B CG2 1 
ATOM   5757 N  N   . ASP   B 1 398 ? 17.104  -5.561  31.677  1   47.12 ? 383 ASP   B N   1 
ATOM   5758 C  CA  . ASP   B 1 398 ? 17.011  -4.161  31.261  1   46.34 ? 383 ASP   B CA  1 
ATOM   5759 C  C   . ASP   B 1 398 ? 17.354  -3.979  29.772  1   43.99 ? 383 ASP   B C   1 
ATOM   5760 O  O   . ASP   B 1 398 ? 16.742  -3.143  29.087  1   43.78 ? 383 ASP   B O   1 
ATOM   5761 C  CB  . ASP   B 1 398 ? 17.883  -3.299  32.168  1   50.51 ? 383 ASP   B CB  1 
ATOM   5762 C  CG  . ASP   B 1 398 ? 17.362  -3.275  33.607  1   61.92 ? 383 ASP   B CG  1 
ATOM   5763 O  OD1 . ASP   B 1 398 ? 17.438  -4.337  34.298  1   63.93 ? 383 ASP   B OD1 1 
ATOM   5764 O  OD2 . ASP   B 1 398 ? 16.869  -2.199  34.048  1   65.95 ? 383 ASP   B OD2 1 
ATOM   5765 N  N   . LEU   B 1 399 ? 18.298  -4.799  29.262  1   41.76 ? 384 LEU   B N   1 
ATOM   5766 C  CA  . LEU   B 1 399 ? 18.714  -4.795  27.849  1   39.79 ? 384 LEU   B CA  1 
ATOM   5767 C  C   . LEU   B 1 399 ? 17.564  -5.311  26.996  1   37.92 ? 384 LEU   B C   1 
ATOM   5768 O  O   . LEU   B 1 399 ? 17.265  -4.742  25.949  1   37.56 ? 384 LEU   B O   1 
ATOM   5769 C  CB  . LEU   B 1 399 ? 19.96   -5.693  27.622  1   39.3  ? 384 LEU   B CB  1 
ATOM   5770 C  CG  . LEU   B 1 399 ? 21.232  -5.379  28.41   1   40.25 ? 384 LEU   B CG  1 
ATOM   5771 C  CD1 . LEU   B 1 399 ? 22.412  -6.205  27.883  1   39.83 ? 384 LEU   B CD1 1 
ATOM   5772 C  CD2 . LEU   B 1 399 ? 21.578  -3.908  28.322  1   40.84 ? 384 LEU   B CD2 1 
ATOM   5773 N  N   . MET   B 1 400 ? 16.922  -6.393  27.449  1   37.14 ? 385 MET   B N   1 
ATOM   5774 C  CA  . MET   B 1 400 ? 15.789  -6.988  26.755  1   37.02 ? 385 MET   B CA  1 
ATOM   5775 C  C   . MET   B 1 400 ? 14.616  -6.001  26.743  1   36.34 ? 385 MET   B C   1 
ATOM   5776 O  O   . MET   B 1 400 ? 13.94   -5.882  25.729  1   35.74 ? 385 MET   B O   1 
ATOM   5777 C  CB  . MET   B 1 400 ? 15.357  -8.295  27.438  1   37.73 ? 385 MET   B CB  1 
ATOM   5778 C  CG  . MET   B 1 400 ? 16.394  -9.377  27.379  1   40.21 ? 385 MET   B CG  1 
ATOM   5779 S  SD  . MET   B 1 400 ? 16.716  -9.986  25.718  1   40.6  ? 385 MET   B SD  1 
ATOM   5780 C  CE  . MET   B 1 400 ? 15.224  -10.763 25.339  1   39.52 ? 385 MET   B CE  1 
ATOM   5781 N  N   . ASN   B 1 401 ? 14.388  -5.281  27.851  1   35.63 ? 386 ASN   B N   1 
ATOM   5782 C  CA  . ASN   B 1 401 ? 13.291  -4.327  27.924  1   36.05 ? 386 ASN   B CA  1 
ATOM   5783 C  C   . ASN   B 1 401 ? 13.533  -3.16   26.968  1   35.38 ? 386 ASN   B C   1 
ATOM   5784 O  O   . ASN   B 1 401 ? 12.591  -2.719  26.298  1   35.37 ? 386 ASN   B O   1 
ATOM   5785 C  CB  . ASN   B 1 401 ? 13.028  -3.865  29.369  1   37.67 ? 386 ASN   B CB  1 
ATOM   5786 C  CG  . ASN   B 1 401 ? 12.405  -4.961  30.233  1   42.1  ? 386 ASN   B CG  1 
ATOM   5787 O  OD1 . ASN   B 1 401 ? 11.879  -5.959  29.735  1   42.3  ? 386 ASN   B OD1 1 
ATOM   5788 N  ND2 . ASN   B 1 401 ? 12.487  -4.82   31.553  1   43.2  ? 386 ASN   B ND2 1 
ATOM   5789 N  N   . PHE   B 1 402 ? 14.798  -2.721  26.822  1   33.72 ? 387 PHE   B N   1 
ATOM   5790 C  CA  . PHE   B 1 402 ? 15.117  -1.641  25.875  1   32.77 ? 387 PHE   B CA  1 
ATOM   5791 C  C   . PHE   B 1 402 ? 14.769  -2.087  24.446  1   31.95 ? 387 PHE   B C   1 
ATOM   5792 O  O   . PHE   B 1 402 ? 14.051  -1.379  23.737  1   32.72 ? 387 PHE   B O   1 
ATOM   5793 C  CB  . PHE   B 1 402 ? 16.604  -1.202  25.978  1   32.11 ? 387 PHE   B CB  1 
ATOM   5794 C  CG  . PHE   B 1 402 ? 17.083  -0.377  24.801  1   32.08 ? 387 PHE   B CG  1 
ATOM   5795 C  CD1 . PHE   B 1 402 ? 16.679  0.935   24.643  1   32.73 ? 387 PHE   B CD1 1 
ATOM   5796 C  CD2 . PHE   B 1 402 ? 17.886  -0.941  23.816  1   31.99 ? 387 PHE   B CD2 1 
ATOM   5797 C  CE1 . PHE   B 1 402 ? 17.114  1.685   23.551  1   33.81 ? 387 PHE   B CE1 1 
ATOM   5798 C  CE2 . PHE   B 1 402 ? 18.288  -0.204  22.718  1   32.76 ? 387 PHE   B CE2 1 
ATOM   5799 C  CZ  . PHE   B 1 402 ? 17.9    1.103   22.587  1   33.05 ? 387 PHE   B CZ  1 
ATOM   5800 N  N   . LEU   B 1 403 ? 15.25   -3.266  24.051  1   29.87 ? 388 LEU   B N   1 
ATOM   5801 C  CA  . LEU   B 1 403 ? 15.002  -3.83   22.732  1   28.92 ? 388 LEU   B CA  1 
ATOM   5802 C  C   . LEU   B 1 403 ? 13.519  -4.08   22.479  1   27.52 ? 388 LEU   B C   1 
ATOM   5803 O  O   . LEU   B 1 403 ? 13.026  -3.876  21.369  1   27.38 ? 388 LEU   B O   1 
ATOM   5804 C  CB  . LEU   B 1 403 ? 15.779  -5.138  22.605  1   29.27 ? 388 LEU   B CB  1 
ATOM   5805 C  CG  . LEU   B 1 403 ? 17.322  -5.02   22.649  1   29.88 ? 388 LEU   B CG  1 
ATOM   5806 C  CD1 . LEU   B 1 403 ? 17.944  -6.383  22.577  1   30.63 ? 388 LEU   B CD1 1 
ATOM   5807 C  CD2 . LEU   B 1 403 ? 17.838  -4.129  21.522  1   29.56 ? 388 LEU   B CD2 1 
ATOM   5808 N  N   . LYS   B 1 404 ? 12.804  -4.49   23.515  1   26.09 ? 389 LYS   B N   1 
ATOM   5809 C  CA  . LYS   B 1 404 ? 11.383  -4.756  23.423  1   27.04 ? 389 LYS   B CA  1 
ATOM   5810 C  C   . LYS   B 1 404 ? 10.592  -3.487  23.214  1   27.36 ? 389 LYS   B C   1 
ATOM   5811 O  O   . LYS   B 1 404 ? 9.66    -3.5    22.428  1   28.46 ? 389 LYS   B O   1 
ATOM   5812 C  CB  . LYS   B 1 404 ? 10.91   -5.547  24.633  1   28.18 ? 389 LYS   B CB  1 
ATOM   5813 C  CG  . LYS   B 1 404 ? 11.246  -7.032  24.455  1   30.26 ? 389 LYS   B CG  1 
ATOM   5814 C  CD  . LYS   B 1 404 ? 10.519  -7.873  25.471  1   32.07 ? 389 LYS   B CD  1 
ATOM   5815 C  CE  . LYS   B 1 404 ? 11.378  -8.396  26.58   1   31.17 ? 389 LYS   B CE  1 
ATOM   5816 N  NZ  . LYS   B 1 404 ? 10.882  -9.73   27.007  1   30.41 ? 389 LYS   B NZ  1 
ATOM   5817 N  N   . THR   B 1 405 ? 10.99   -2.381  23.868  1   26.25 ? 390 THR   B N   1 
ATOM   5818 C  CA  . THR   B 1 405 ? 10.334  -1.104  23.692  1   27.08 ? 390 THR   B CA  1 
ATOM   5819 C  C   . THR   B 1 405 ? 10.516  -0.589  22.249  1   28.42 ? 390 THR   B C   1 
ATOM   5820 O  O   . THR   B 1 405 ? 9.537   -0.162  21.619  1   28.17 ? 390 THR   B O   1 
ATOM   5821 C  CB  . THR   B 1 405 ? 10.873  -0.117  24.693  1   28.64 ? 390 THR   B CB  1 
ATOM   5822 O  OG1 . THR   B 1 405 ? 10.493  -0.551  26.002  1   28.22 ? 390 THR   B OG1 1 
ATOM   5823 C  CG2 . THR   B 1 405 ? 10.346  1.285   24.46   1   30.03 ? 390 THR   B CG2 1 
ATOM   5824 N  N   . VAL   B 1 406 ? 11.745  -0.714  21.717  1   28.73 ? 391 VAL   B N   1 
ATOM   5825 C  CA  . VAL   B 1 406 ? 12.064  -0.279  20.361  1   29.18 ? 391 VAL   B CA  1 
ATOM   5826 C  C   . VAL   B 1 406 ? 11.263  -1.125  19.354  1   29.52 ? 391 VAL   B C   1 
ATOM   5827 O  O   . VAL   B 1 406 ? 10.742  -0.603  18.358  1   29.57 ? 391 VAL   B O   1 
ATOM   5828 C  CB  . VAL   B 1 406 ? 13.616  -0.31   20.131  1   29.34 ? 391 VAL   B CB  1 
ATOM   5829 C  CG1 . VAL   B 1 406 ? 13.985  0.018   18.686  1   29.56 ? 391 VAL   B CG1 1 
ATOM   5830 C  CG2 . VAL   B 1 406 ? 14.35   0.639   21.094  1   29.59 ? 391 VAL   B CG2 1 
ATOM   5831 N  N   . ARG   B 1 407 ? 11.196  -2.441  19.589  1   29.08 ? 392 ARG   B N   1 
ATOM   5832 C  CA  . ARG   B 1 407 ? 10.432  -3.34   18.726  1   29.75 ? 392 ARG   B CA  1 
ATOM   5833 C  C   . ARG   B 1 407 ? 8.906   -3.002  18.804  1   31.59 ? 392 ARG   B C   1 
ATOM   5834 O  O   . ARG   B 1 407 ? 8.241   -2.863  17.783  1   31.01 ? 392 ARG   B O   1 
ATOM   5835 C  CB  . ARG   B 1 407 ? 10.666  -4.79   19.161  1   29.13 ? 392 ARG   B CB  1 
ATOM   5836 C  CG  . ARG   B 1 407 ? 10.359  -5.766  18.052  1   32.05 ? 392 ARG   B CG  1 
ATOM   5837 C  CD  . ARG   B 1 407 ? 9.273   -6.739  18.33   1   34.21 ? 392 ARG   B CD  1 
ATOM   5838 N  NE  . ARG   B 1 407 ? 9.333   -7.397  19.634  1   34.19 ? 392 ARG   B NE  1 
ATOM   5839 C  CZ  . ARG   B 1 407 ? 9.437   -8.712  19.791  1   34.06 ? 392 ARG   B CZ  1 
ATOM   5840 N  NH1 . ARG   B 1 407 ? 9.642   -9.499  18.741  1   34.44 ? 392 ARG   B NH1 1 
ATOM   5841 N  NH2 . ARG   B 1 407 ? 9.387   -9.245  21.001  1   32.23 ? 392 ARG   B NH2 1 
ATOM   5842 N  N   . SER   B 1 408 ? 8.379   -2.838  20.023  1   33.04 ? 393 SER   B N   1 
ATOM   5843 C  CA  . SER   B 1 408 ? 6.989   -2.46   20.278  1   34.43 ? 393 SER   B CA  1 
ATOM   5844 C  C   . SER   B 1 408 ? 6.625   -1.164  19.529  1   34.49 ? 393 SER   B C   1 
ATOM   5845 O  O   . SER   B 1 408 ? 5.633   -1.147  18.799  1   34.39 ? 393 SER   B O   1 
ATOM   5846 C  CB  . SER   B 1 408 ? 6.782   -2.288  21.777  1   36.81 ? 393 SER   B CB  1 
ATOM   5847 O  OG  . SER   B 1 408 ? 5.502   -1.757  22.059  1   43.54 ? 393 SER   B OG  1 
ATOM   5848 N  N   . THR   B 1 409 ? 7.465   -0.097  19.661  1   33.97 ? 394 THR   B N   1 
ATOM   5849 C  CA  . THR   B 1 409 ? 7.249   1.183   18.991  1   33.99 ? 394 THR   B CA  1 
ATOM   5850 C  C   . THR   B 1 409 ? 7.185   1.011   17.471  1   34.5  ? 394 THR   B C   1 
ATOM   5851 O  O   . THR   B 1 409 ? 6.374   1.665   16.788  1   35.2  ? 394 THR   B O   1 
ATOM   5852 C  CB  . THR   B 1 409 ? 8.302   2.201   19.46   1   35.3  ? 394 THR   B CB  1 
ATOM   5853 O  OG1 . THR   B 1 409 ? 8.181   2.33    20.878  1   36.5  ? 394 THR   B OG1 1 
ATOM   5854 C  CG2 . THR   B 1 409 ? 8.139   3.573   18.801  1   35.28 ? 394 THR   B CG2 1 
ATOM   5855 N  N   . THR   B 1 410 ? 8.02    0.12    16.94   1   33.45 ? 395 THR   B N   1 
ATOM   5856 C  CA  . THR   B 1 410 ? 8.036   -0.199  15.515  1   33.13 ? 395 THR   B CA  1 
ATOM   5857 C  C   . THR   B 1 410 ? 6.706   -0.86   15.128  1   34.98 ? 395 THR   B C   1 
ATOM   5858 O  O   . THR   B 1 410 ? 6.071   -0.436  14.166  1   35.7  ? 395 THR   B O   1 
ATOM   5859 C  CB  . THR   B 1 410 ? 9.26    -1.096  15.18   1   33.38 ? 395 THR   B CB  1 
ATOM   5860 O  OG1 . THR   B 1 410 ? 10.441  -0.534  15.76   1   33.38 ? 395 THR   B OG1 1 
ATOM   5861 C  CG2 . THR   B 1 410 ? 9.472   -1.273  13.681  1   32.84 ? 395 THR   B CG2 1 
ATOM   5862 N  N   . GLU   B 1 411 ? 6.286   -1.903  15.86   1   35.09 ? 396 GLU   B N   1 
ATOM   5863 C  CA  . GLU   B 1 411 ? 5.031   -2.589  15.547  1   35.96 ? 396 GLU   B CA  1 
ATOM   5864 C  C   . GLU   B 1 411 ? 3.799   -1.642  15.613  1   34.91 ? 396 GLU   B C   1 
ATOM   5865 O  O   . GLU   B 1 411 ? 2.964   -1.658  14.725  1   33.9  ? 396 GLU   B O   1 
ATOM   5866 C  CB  . GLU   B 1 411 ? 4.85    -3.806  16.453  1   40.44 ? 396 GLU   B CB  1 
ATOM   5867 C  CG  . GLU   B 1 411 ? 3.884   -4.811  15.856  1   50.76 ? 396 GLU   B CG  1 
ATOM   5868 C  CD  . GLU   B 1 411 ? 4.409   -6.235  15.829  1   64.01 ? 396 GLU   B CD  1 
ATOM   5869 O  OE1 . GLU   B 1 411 ? 5.006   -6.665  16.848  1   68.12 ? 396 GLU   B OE1 1 
ATOM   5870 O  OE2 . GLU   B 1 411 ? 4.233   -6.918  14.79   1   66.05 ? 396 GLU   B OE2 1 
ATOM   5871 N  N   . LYS   B 1 412 ? 3.735   -0.775  16.626  1   35.14 ? 397 LYS   B N   1 
ATOM   5872 C  CA  . LYS   B 1 412 ? 2.643   0.178   16.77   1   36.26 ? 397 LYS   B CA  1 
ATOM   5873 C  C   . LYS   B 1 412 ? 2.552   1.193   15.63   1   37.22 ? 397 LYS   B C   1 
ATOM   5874 O  O   . LYS   B 1 412 ? 1.541   1.879   15.526  1   38.45 ? 397 LYS   B O   1 
ATOM   5875 C  CB  . LYS   B 1 412 ? 2.685   0.863   18.134  1   38.02 ? 397 LYS   B CB  1 
ATOM   5876 C  CG  . LYS   B 1 412 ? 2.454   -0.162  19.228  1   45.44 ? 397 LYS   B CG  1 
ATOM   5877 C  CD  . LYS   B 1 412 ? 2.104   0.445   20.572  1   52.31 ? 397 LYS   B CD  1 
ATOM   5878 C  CE  . LYS   B 1 412 ? 3.247   0.665   21.523  1   56.92 ? 397 LYS   B CE  1 
ATOM   5879 N  NZ  . LYS   B 1 412 ? 2.916   0.197   22.899  1   59.65 ? 397 LYS   B NZ  1 
ATOM   5880 N  N   . SER   B 1 413 ? 3.568   1.266   14.766  1   36.41 ? 398 SER   B N   1 
ATOM   5881 C  CA  . SER   B 1 413 ? 3.57    2.147   13.599  1   35.79 ? 398 SER   B CA  1 
ATOM   5882 C  C   . SER   B 1 413 ? 2.889   1.502   12.392  1   34.94 ? 398 SER   B C   1 
ATOM   5883 O  O   . SER   B 1 413 ? 2.752   2.171   11.378  1   32.96 ? 398 SER   B O   1 
ATOM   5884 C  CB  . SER   B 1 413 ? 4.992   2.541   13.207  1   37.02 ? 398 SER   B CB  1 
ATOM   5885 O  OG  . SER   B 1 413 ? 5.582   3.341   14.219  1   40.72 ? 398 SER   B OG  1 
ATOM   5886 N  N   . LEU   B 1 414 ? 2.481   0.226   12.461  1   35.9  ? 399 LEU   B N   1 
ATOM   5887 C  CA  . LEU   B 1 414 ? 1.775   -0.394  11.341  1   37.96 ? 399 LEU   B CA  1 
ATOM   5888 C  C   . LEU   B 1 414 ? 0.426   0.352   11.113  1   40.19 ? 399 LEU   B C   1 
ATOM   5889 O  O   . LEU   B 1 414 ? -0.208  0.821   12.064  1   39.16 ? 399 LEU   B O   1 
ATOM   5890 C  CB  . LEU   B 1 414 ? 1.575   -1.896  11.578  1   37.99 ? 399 LEU   B CB  1 
ATOM   5891 C  CG  . LEU   B 1 414 ? 2.826   -2.744  11.378  1   39.61 ? 399 LEU   B CG  1 
ATOM   5892 C  CD1 . LEU   B 1 414 ? 2.617   -4.14   11.911  1   40.61 ? 399 LEU   B CD1 1 
ATOM   5893 C  CD2 . LEU   B 1 414 ? 3.23    -2.786  9.921   1   39.15 ? 399 LEU   B CD2 1 
ATOM   5894 N  N   . LEU   B 1 415 ? 0.121   0.631   9.854   1   42.71 ? 400 LEU   B N   1 
ATOM   5895 C  CA  . LEU   B 1 415 ? -1.098  1.35    9.5     1   45.78 ? 400 LEU   B CA  1 
ATOM   5896 C  C   . LEU   B 1 415 ? -2.309  0.431   9.503   1   50.01 ? 400 LEU   B C   1 
ATOM   5897 O  O   . LEU   B 1 415 ? -3.414  0.876   9.812   1   50.56 ? 400 LEU   B O   1 
ATOM   5898 C  CB  . LEU   B 1 415 ? -0.937  2.039   8.144   1   44.96 ? 400 LEU   B CB  1 
ATOM   5899 C  CG  . LEU   B 1 415 ? 0.175   3.062   8.049   1   45.43 ? 400 LEU   B CG  1 
ATOM   5900 C  CD1 . LEU   B 1 415 ? 0.156   3.718   6.711   1   46.12 ? 400 LEU   B CD1 1 
ATOM   5901 C  CD2 . LEU   B 1 415 ? 0.062   4.125   9.138   1   45.3  ? 400 LEU   B CD2 1 
ATOM   5902 N  N   . LYS   B 1 416 ? -2.11   -0.852  9.164   1   52.85 ? 401 LYS   B N   1 
ATOM   5903 C  CA  . LYS   B 1 416 ? -3.192  -1.834  9.143   1   55.7  ? 401 LYS   B CA  1 
ATOM   5904 C  C   . LYS   B 1 416 ? -2.883  -3.025  10.059  1   57.26 ? 401 LYS   B C   1 
ATOM   5905 O  O   . LYS   B 1 416 ? -3.431  -3.119  11.162  1   58.04 ? 401 LYS   B O   1 
ATOM   5906 C  CB  . LYS   B 1 416 ? -3.469  -2.303  7.699   1   58.89 ? 401 LYS   B CB  1 
ATOM   5907 C  CG  . LYS   B 1 416 ? -3.805  -1.15   6.728   1   64.62 ? 401 LYS   B CG  1 
ATOM   5908 C  CD  . LYS   B 1 416 ? -5.066  -0.392  7.156   1   70.11 ? 401 LYS   B CD  1 
ATOM   5909 C  CE  . LYS   B 1 416 ? -4.949  1.087   6.904   1   74.38 ? 401 LYS   B CE  1 
ATOM   5910 N  NZ  . LYS   B 1 416 ? -5.947  1.862   7.684   1   76.73 ? 401 LYS   B NZ  1 
HETATM 5911 C  CHA . HEM   C 2 .   ? 16.279  30.187  31.435  1   25.09 ? 501 HEM   A CHA 1 
HETATM 5912 C  CHB . HEM   C 2 .   ? 14.21   32.55   35.094  1   26.57 ? 501 HEM   A CHB 1 
HETATM 5913 C  CHC . HEM   C 2 .   ? 12.989  36.034  32.025  1   25.68 ? 501 HEM   A CHC 1 
HETATM 5914 C  CHD . HEM   C 2 .   ? 15.037  33.676  28.356  1   25.78 ? 501 HEM   A CHD 1 
HETATM 5915 C  C1A . HEM   C 2 .   ? 15.698  30.467  32.68   1   25.3  ? 501 HEM   A C1A 1 
HETATM 5916 C  C2A . HEM   C 2 .   ? 15.861  29.622  33.853  1   25.73 ? 501 HEM   A C2A 1 
HETATM 5917 C  C3A . HEM   C 2 .   ? 15.307  30.308  34.908  1   25.58 ? 501 HEM   A C3A 1 
HETATM 5918 C  C4A . HEM   C 2 .   ? 14.803  31.556  34.363  1   25.83 ? 501 HEM   A C4A 1 
HETATM 5919 C  CMA . HEM   C 2 .   ? 15.26   29.916  36.355  1   25.62 ? 501 HEM   A CMA 1 
HETATM 5920 C  CAA . HEM   C 2 .   ? 16.579  28.302  33.899  1   27.89 ? 501 HEM   A CAA 1 
HETATM 5921 C  CBA . HEM   C 2 .   ? 15.793  27.17   33.23   1   29.92 ? 501 HEM   A CBA 1 
HETATM 5922 C  CGA . HEM   C 2 .   ? 14.65   26.636  34.046  1   31.93 ? 501 HEM   A CGA 1 
HETATM 5923 O  O1A . HEM   C 2 .   ? 13.624  26.259  33.517  1   31.97 ? 501 HEM   A O1A 1 
HETATM 5924 O  O2A . HEM   C 2 .   ? 14.831  26.641  35.361  1   33.43 ? 501 HEM   A O2A 1 
HETATM 5925 C  C1B . HEM   C 2 .   ? 13.749  33.756  34.6    1   27.1  ? 501 HEM   A C1B 1 
HETATM 5926 C  C2B . HEM   C 2 .   ? 13.061  34.742  35.404  1   27.16 ? 501 HEM   A C2B 1 
HETATM 5927 C  C3B . HEM   C 2 .   ? 12.685  35.718  34.5    1   26.81 ? 501 HEM   A C3B 1 
HETATM 5928 C  C4B . HEM   C 2 .   ? 13.169  35.341  33.2    1   26.2  ? 501 HEM   A C4B 1 
HETATM 5929 C  CMB . HEM   C 2 .   ? 12.905  34.677  36.894  1   27.88 ? 501 HEM   A CMB 1 
HETATM 5930 C  CAB . HEM   C 2 .   ? 11.947  36.958  34.754  1   27.71 ? 501 HEM   A CAB 1 
HETATM 5931 C  CBB . HEM   C 2 .   ? 10.966  37.172  35.583  1   27.73 ? 501 HEM   A CBB 1 
HETATM 5932 C  C1C . HEM   C 2 .   ? 13.411  35.694  30.729  1   25.25 ? 501 HEM   A C1C 1 
HETATM 5933 C  C2C . HEM   C 2 .   ? 13.033  36.42   29.528  1   25.25 ? 501 HEM   A C2C 1 
HETATM 5934 C  C3C . HEM   C 2 .   ? 13.607  35.733  28.483  1   25.42 ? 501 HEM   A C3C 1 
HETATM 5935 C  C4C . HEM   C 2 .   ? 14.333  34.62   29.048  1   25.26 ? 501 HEM   A C4C 1 
HETATM 5936 C  CMC . HEM   C 2 .   ? 12.212  37.673  29.491  1   24.69 ? 501 HEM   A CMC 1 
HETATM 5937 C  CAC . HEM   C 2 .   ? 13.434  36.054  27.061  1   26.3  ? 501 HEM   A CAC 1 
HETATM 5938 C  CBC . HEM   C 2 .   ? 13.233  35.241  26.024  1   25.66 ? 501 HEM   A CBC 1 
HETATM 5939 C  C1D . HEM   C 2 .   ? 15.704  32.557  28.912  1   25.68 ? 501 HEM   A C1D 1 
HETATM 5940 C  C2D . HEM   C 2 .   ? 16.521  31.614  28.165  1   25.43 ? 501 HEM   A C2D 1 
HETATM 5941 C  C3D . HEM   C 2 .   ? 16.848  30.608  29.041  1   25.57 ? 501 HEM   A C3D 1 
HETATM 5942 C  C4D . HEM   C 2 .   ? 16.236  30.957  30.313  1   25.15 ? 501 HEM   A C4D 1 
HETATM 5943 C  CMD . HEM   C 2 .   ? 16.911  31.742  26.72   1   25.79 ? 501 HEM   A CMD 1 
HETATM 5944 C  CAD . HEM   C 2 .   ? 17.7    29.401  28.753  1   26.06 ? 501 HEM   A CAD 1 
HETATM 5945 C  CBD . HEM   C 2 .   ? 19.148  29.517  29.28   1   26.19 ? 501 HEM   A CBD 1 
HETATM 5946 C  CGD . HEM   C 2 .   ? 20.054  30.421  28.484  1   26.77 ? 501 HEM   A CGD 1 
HETATM 5947 O  O1D . HEM   C 2 .   ? 20.817  31.212  28.996  1   26.57 ? 501 HEM   A O1D 1 
HETATM 5948 O  O2D . HEM   C 2 .   ? 19.975  30.269  27.187  1   26.88 ? 501 HEM   A O2D 1 
HETATM 5949 N  NA  . HEM   C 2 .   ? 15.049  31.612  33.004  1   25.04 ? 501 HEM   A NA  1 
HETATM 5950 N  NB  . HEM   C 2 .   ? 13.821  34.144  33.299  1   26.49 ? 501 HEM   A NB  1 
HETATM 5951 N  NC  . HEM   C 2 .   ? 14.196  34.63   30.428  1   25.05 ? 501 HEM   A NC  1 
HETATM 5952 N  ND  . HEM   C 2 .   ? 15.55   32.159  30.198  1   25.12 ? 501 HEM   A ND  1 
HETATM 5953 FE FE  . HEM   C 2 .   ? 14.6    33.123  31.734  1   26.22 ? 501 HEM   A FE  1 
HETATM 5954 C  C5  . A1H6U D 3 .   ? 8.74    30.515  30.183  1   31.65 ? 502 A1H6U A C5  1 
HETATM 5955 C  C6  . A1H6U D 3 .   ? 9.233   29.593  31.106  1   32.41 ? 502 A1H6U A C6  1 
HETATM 5956 C  C7  . A1H6U D 3 .   ? 11.612  32.824  30.445  1   32.86 ? 502 A1H6U A C7  1 
HETATM 5957 C  C8  . A1H6U D 3 .   ? 12.363  31.323  31.869  1   33.36 ? 502 A1H6U A C8  1 
HETATM 5958 C  C13 . A1H6U D 3 .   ? 11.46   29.066  36.615  1   33.67 ? 502 A1H6U A C13 1 
HETATM 5959 O  O   . A1H6U D 3 .   ? 12.329  28.397  32.462  1   33.44 ? 502 A1H6U A O   1 
HETATM 5960 C  C1  . A1H6U D 3 .   ? 10.988  28.805  32.722  1   33.15 ? 502 A1H6U A C1  1 
HETATM 5961 C  CA  . A1H6U D 3 .   ? 10.457  29.809  31.753  1   33.22 ? 502 A1H6U A CA  1 
HETATM 5962 N  N   . A1H6U D 3 .   ? 11.188  30.868  31.398  1   33.5  ? 502 A1H6U A N   1 
HETATM 5963 C  C3  . A1H6U D 3 .   ? 10.701  31.786  30.542  1   33    ? 502 A1H6U A C3  1 
HETATM 5964 C  CG2 . A1H6U D 3 .   ? 9.473   31.665  29.919  1   32.31 ? 502 A1H6U A CG2 1 
HETATM 5965 N  N2  . A1H6U D 3 .   ? 12.634  32.49   31.249  1   33.69 ? 502 A1H6U A N2  1 
HETATM 5966 C  C9  . A1H6U D 3 .   ? 10.652  28.857  34.218  1   33.55 ? 502 A1H6U A C9  1 
HETATM 5967 C  CD1 . A1H6U D 3 .   ? 9.442   29.723  34.549  1   34.21 ? 502 A1H6U A CD1 1 
HETATM 5968 C  CG1 . A1H6U D 3 .   ? 9.036   29.584  36.021  1   34.1  ? 502 A1H6U A CG1 1 
HETATM 5969 C  C12 . A1H6U D 3 .   ? 10.201  29.867  36.972  1   34.1  ? 502 A1H6U A C12 1 
HETATM 5970 C  C14 . A1H6U D 3 .   ? 11.829  29.195  35.136  1   33.75 ? 502 A1H6U A C14 1 
HETATM 5971 C  CHA . HEM   E 2 .   ? 21.2    -3.227  20.09   1   26.86 ? 501 HEM   B CHA 1 
HETATM 5972 C  CHB . HEM   E 2 .   ? 23.034  -7.432  21.594  1   26.91 ? 501 HEM   B CHB 1 
HETATM 5973 C  CHC . HEM   E 2 .   ? 24.009  -8.574  17.039  1   28.63 ? 501 HEM   B CHC 1 
HETATM 5974 C  CHD . HEM   E 2 .   ? 22.183  -4.363  15.497  1   28.21 ? 501 HEM   B CHD 1 
HETATM 5975 C  C1A . HEM   E 2 .   ? 21.727  -4.239  20.906  1   27.53 ? 501 HEM   B C1A 1 
HETATM 5976 C  C2A . HEM   E 2 .   ? 21.614  -4.234  22.35   1   27.95 ? 501 HEM   B C2A 1 
HETATM 5977 C  C3A . HEM   E 2 .   ? 22.1    -5.44   22.785  1   26.92 ? 501 HEM   B C3A 1 
HETATM 5978 C  C4A . HEM   E 2 .   ? 22.524  -6.161  21.6    1   26.74 ? 501 HEM   B C4A 1 
HETATM 5979 C  CMA . HEM   E 2 .   ? 22.117  -5.978  24.183  1   26.96 ? 501 HEM   B CMA 1 
HETATM 5980 C  CAA . HEM   E 2 .   ? 21.066  -3.111  23.186  1   29.85 ? 501 HEM   B CAA 1 
HETATM 5981 C  CBA . HEM   E 2 .   ? 22.02   -1.921  23.278  1   30.4  ? 501 HEM   B CBA 1 
HETATM 5982 C  CGA . HEM   E 2 .   ? 23.111  -2.1    24.298  1   31.22 ? 501 HEM   B CGA 1 
HETATM 5983 O  O1A . HEM   E 2 .   ? 22.935  -2.634  25.375  1   30.82 ? 501 HEM   B O1A 1 
HETATM 5984 O  O2A . HEM   E 2 .   ? 24.271  -1.603  23.927  1   31.06 ? 501 HEM   B O2A 1 
HETATM 5985 C  C1B . HEM   E 2 .   ? 23.419  -8.151  20.487  1   27.35 ? 501 HEM   B C1B 1 
HETATM 5986 C  C2B . HEM   E 2 .   ? 24.008  -9.484  20.534  1   27.79 ? 501 HEM   B C2B 1 
HETATM 5987 C  C3B . HEM   E 2 .   ? 24.306  -9.786  19.221  1   28.24 ? 501 HEM   B C3B 1 
HETATM 5988 C  C4B . HEM   E 2 .   ? 23.891  -8.666  18.409  1   28.25 ? 501 HEM   B C4B 1 
HETATM 5989 C  CMB . HEM   E 2 .   ? 24.113  -10.342 21.762  1   26.82 ? 501 HEM   B CMB 1 
HETATM 5990 C  CAB . HEM   E 2 .   ? 24.861  -11.02  18.667  1   28.47 ? 501 HEM   B CAB 1 
HETATM 5991 C  CBB . HEM   E 2 .   ? 25.832  -11.784 19.134  1   28.95 ? 501 HEM   B CBB 1 
HETATM 5992 C  C1C . HEM   E 2 .   ? 23.626  -7.517  16.199  1   28.09 ? 501 HEM   B C1C 1 
HETATM 5993 C  C2C . HEM   E 2 .   ? 23.923  -7.454  14.776  1   28.45 ? 501 HEM   B C2C 1 
HETATM 5994 C  C3C . HEM   E 2 .   ? 23.441  -6.238  14.353  1   27.86 ? 501 HEM   B C3C 1 
HETATM 5995 C  C4C . HEM   E 2 .   ? 22.839  -5.593  15.492  1   27.63 ? 501 HEM   B C4C 1 
HETATM 5996 C  CMC . HEM   E 2 .   ? 24.586  -8.535  13.98   1   28.48 ? 501 HEM   B CMC 1 
HETATM 5997 C  CAC . HEM   E 2 .   ? 23.572  -5.694  12.997  1   28.24 ? 501 HEM   B CAC 1 
HETATM 5998 C  CBC . HEM   E 2 .   ? 23.887  -4.44   12.626  1   27.98 ? 501 HEM   B CBC 1 
HETATM 5999 C  C1D . HEM   E 2 .   ? 21.656  -3.697  16.643  1   27.23 ? 501 HEM   B C1D 1 
HETATM 6000 C  C2D . HEM   E 2 .   ? 20.922  -2.443  16.609  1   26.8  ? 501 HEM   B C2D 1 
HETATM 6001 C  C3D . HEM   E 2 .   ? 20.654  -2.118  17.918  1   26.65 ? 501 HEM   B C3D 1 
HETATM 6002 C  C4D . HEM   E 2 .   ? 21.226  -3.181  18.729  1   26.72 ? 501 HEM   B C4D 1 
HETATM 6003 C  CMD . HEM   E 2 .   ? 20.549  -1.687  15.368  1   26.87 ? 501 HEM   B CMD 1 
HETATM 6004 C  CAD . HEM   E 2 .   ? 19.92   -0.9    18.415  1   25.79 ? 501 HEM   B CAD 1 
HETATM 6005 C  CBD . HEM   E 2 .   ? 18.459  -1.159  18.829  1   25.43 ? 501 HEM   B CBD 1 
HETATM 6006 C  CGD . HEM   E 2 .   ? 17.485  -1.336  17.692  1   26.53 ? 501 HEM   B CGD 1 
HETATM 6007 O  O1D . HEM   E 2 .   ? 16.626  -2.208  17.666  1   27.16 ? 501 HEM   B O1D 1 
HETATM 6008 O  O2D . HEM   E 2 .   ? 17.635  -0.484  16.719  1   25.57 ? 501 HEM   B O2D 1 
HETATM 6009 N  NA  . HEM   E 2 .   ? 22.301  -5.397  20.481  1   26.21 ? 501 HEM   B NA  1 
HETATM 6010 N  NB  . HEM   E 2 .   ? 23.341  -7.692  19.216  1   27.58 ? 501 HEM   B NB  1 
HETATM 6011 N  NC  . HEM   E 2 .   ? 22.971  -6.409  16.604  1   26.5  ? 501 HEM   B NC  1 
HETATM 6012 N  ND  . HEM   E 2 .   ? 21.836  -4.121  17.925  1   26.7  ? 501 HEM   B ND  1 
HETATM 6013 FE FE  . HEM   E 2 .   ? 22.671  -5.886  18.54   1   26.87 ? 501 HEM   B FE  1 
HETATM 6014 C  C5  . A1H6U F 3 .   ? 28.81   -3.443  18.63   1   29.76 ? 502 A1H6U B C5  1 
HETATM 6015 C  C6  . A1H6U F 3 .   ? 28.367  -3.175  19.924  1   30.25 ? 502 A1H6U B C6  1 
HETATM 6016 C  C7  . A1H6U F 3 .   ? 25.621  -5.073  17.58   1   30.85 ? 502 A1H6U B C7  1 
HETATM 6017 C  C8  . A1H6U F 3 .   ? 25.026  -4.644  19.646  1   31.13 ? 502 A1H6U B C8  1 
HETATM 6018 C  C13 . A1H6U F 3 .   ? 26.12   -5.785  24.77   1   35.91 ? 502 A1H6U B C13 1 
HETATM 6019 O  O   . A1H6U F 3 .   ? 25.348  -2.727  21.83   1   34.13 ? 502 A1H6U B O   1 
HETATM 6020 C  C1  . A1H6U F 3 .   ? 26.657  -3.307  21.756  1   33.27 ? 502 A1H6U B C1  1 
HETATM 6021 C  CA  . A1H6U F 3 .   ? 27.098  -3.585  20.36   1   31.7  ? 502 A1H6U B CA  1 
HETATM 6022 N  N   . A1H6U F 3 .   ? 26.273  -4.189  19.494  1   31.45 ? 502 A1H6U B N   1 
HETATM 6023 C  C3  . A1H6U F 3 .   ? 26.649  -4.402  18.23   1   30.67 ? 502 A1H6U B C3  1 
HETATM 6024 C  CG2 . A1H6U F 3 .   ? 27.929  -4.095  17.762  1   30.44 ? 502 A1H6U B CG2 1 
HETATM 6025 N  N2  . A1H6U F 3 .   ? 24.623  -5.182  18.479  1   31.76 ? 502 A1H6U B N2  1 
HETATM 6026 C  C9  . A1H6U F 3 .   ? 26.955  -4.324  22.88   1   35.02 ? 502 A1H6U B C9  1 
HETATM 6027 C  CD1 . A1H6U F 3 .   ? 27.982  -5.394  22.49   1   35.98 ? 502 A1H6U B CD1 1 
HETATM 6028 C  CG1 . A1H6U F 3 .   ? 28.391  -6.271  23.685  1   35.81 ? 502 A1H6U B CG1 1 
HETATM 6029 C  C12 . A1H6U F 3 .   ? 27.187  -6.853  24.44   1   35.88 ? 502 A1H6U B C12 1 
HETATM 6030 C  C14 . A1H6U F 3 .   ? 25.724  -4.972  23.532  1   35.54 ? 502 A1H6U B C14 1 
HETATM 6031 O  O   . HOH   G 4 .   ? 35.218  38.362  29.144  1   42.59 ? 601 HOH   A O   1 
HETATM 6032 O  O   . HOH   G 4 .   ? -17.798 22.155  23.517  1   40.42 ? 602 HOH   A O   1 
HETATM 6033 O  O   . HOH   G 4 .   ? 16.626  43.31   17.69   1   33.34 ? 603 HOH   A O   1 
HETATM 6034 O  O   . HOH   G 4 .   ? 28.951  22.276  26.701  1   47.05 ? 604 HOH   A O   1 
HETATM 6035 O  O   . HOH   G 4 .   ? -13.809 35.92   34.877  1   34    ? 605 HOH   A O   1 
HETATM 6036 O  O   . HOH   G 4 .   ? 18.483  43.214  10.868  1   37.31 ? 606 HOH   A O   1 
HETATM 6037 O  O   . HOH   G 4 .   ? 12.48   34.751  17.98   1   35.25 ? 607 HOH   A O   1 
HETATM 6038 O  O   . HOH   G 4 .   ? 7.07    31.428  13.602  1   40.51 ? 608 HOH   A O   1 
HETATM 6039 O  O   . HOH   G 4 .   ? -9.835  12.664  18.52   1   35.42 ? 609 HOH   A O   1 
HETATM 6040 O  O   . HOH   G 4 .   ? -7.221  31.827  31.846  1   27.58 ? 610 HOH   A O   1 
HETATM 6041 O  O   . HOH   G 4 .   ? -8.36   40.597  42.933  1   39.68 ? 611 HOH   A O   1 
HETATM 6042 O  O   . HOH   G 4 .   ? 28.128  43.131  21.555  1   31.16 ? 612 HOH   A O   1 
HETATM 6043 O  O   . HOH   G 4 .   ? 34.227  42.832  19.461  1   37.71 ? 613 HOH   A O   1 
HETATM 6044 O  O   . HOH   G 4 .   ? 0.282   22.12   25.928  1   24.16 ? 614 HOH   A O   1 
HETATM 6045 O  O   . HOH   G 4 .   ? 26.375  45.692  9.581   1   34.9  ? 615 HOH   A O   1 
HETATM 6046 O  O   . HOH   G 4 .   ? 17.523  16.794  31.427  1   44.32 ? 616 HOH   A O   1 
HETATM 6047 O  O   . HOH   G 4 .   ? 36.9    35.283  2.679   1   42.73 ? 617 HOH   A O   1 
HETATM 6048 O  O   . HOH   G 4 .   ? 0.825   25.946  21.172  1   30.49 ? 618 HOH   A O   1 
HETATM 6049 O  O   . HOH   G 4 .   ? 9.577   45.164  39.742  1   40.87 ? 619 HOH   A O   1 
HETATM 6050 O  O   . HOH   G 4 .   ? 8.773   24.759  23.551  1   18.71 ? 620 HOH   A O   1 
HETATM 6051 O  O   . HOH   G 4 .   ? 0.796   40.281  41.255  1   43.18 ? 621 HOH   A O   1 
HETATM 6052 O  O   . HOH   G 4 .   ? 21.823  27.293  24.26   1   31.05 ? 622 HOH   A O   1 
HETATM 6053 O  O   . HOH   G 4 .   ? -12.261 34.624  41.37   1   31.92 ? 623 HOH   A O   1 
HETATM 6054 O  O   . HOH   G 4 .   ? -13.78  20.872  41.709  1   30.54 ? 624 HOH   A O   1 
HETATM 6055 O  O   . HOH   G 4 .   ? 37.618  31.436  23.154  1   31.59 ? 625 HOH   A O   1 
HETATM 6056 O  O   . HOH   G 4 .   ? 3.867   22.842  41.216  1   35.58 ? 626 HOH   A O   1 
HETATM 6057 O  O   . HOH   G 4 .   ? 1.037   12.18   22.713  1   34.01 ? 627 HOH   A O   1 
HETATM 6058 O  O   . HOH   G 4 .   ? -12.698 16.718  25.828  1   38.23 ? 628 HOH   A O   1 
HETATM 6059 O  O   . HOH   G 4 .   ? -1.009  45.73   27.373  1   44.19 ? 629 HOH   A O   1 
HETATM 6060 O  O   . HOH   G 4 .   ? -9.333  24.455  42.92   1   36    ? 630 HOH   A O   1 
HETATM 6061 O  O   . HOH   G 4 .   ? 9.129   49.328  37.72   1   39.4  ? 631 HOH   A O   1 
HETATM 6062 O  O   . HOH   G 4 .   ? 36.529  40.718  22.345  1   43.85 ? 632 HOH   A O   1 
HETATM 6063 O  O   . HOH   G 4 .   ? 16.855  23.02   24.031  1   37.52 ? 633 HOH   A O   1 
HETATM 6064 O  O   . HOH   G 4 .   ? 4.308   38.683  11.848  1   37.76 ? 634 HOH   A O   1 
HETATM 6065 O  O   . HOH   G 4 .   ? 13.119  36.224  11.679  1   40.94 ? 635 HOH   A O   1 
HETATM 6066 O  O   . HOH   G 4 .   ? 19.405  28.404  25.37   1   33.55 ? 636 HOH   A O   1 
HETATM 6067 O  O   . HOH   G 4 .   ? 9.028   25.142  34.989  1   31.11 ? 637 HOH   A O   1 
HETATM 6068 O  O   . HOH   G 4 .   ? 3.439   13.405  22.116  1   35.21 ? 638 HOH   A O   1 
HETATM 6069 O  O   . HOH   G 4 .   ? -6.967  33.035  41.022  1   32.98 ? 639 HOH   A O   1 
HETATM 6070 O  O   . HOH   G 4 .   ? 26.477  24.738  28.631  1   51.2  ? 640 HOH   A O   1 
HETATM 6071 O  O   . HOH   G 4 .   ? -7.99   12.465  38.606  1   40.64 ? 641 HOH   A O   1 
HETATM 6072 O  O   . HOH   G 4 .   ? -12.799 26.896  47.472  1   43.12 ? 642 HOH   A O   1 
HETATM 6073 O  O   . HOH   G 4 .   ? 35.036  35.512  -3.225  1   39.28 ? 643 HOH   A O   1 
HETATM 6074 O  O   . HOH   G 4 .   ? -0.433  7.329   31.269  1   34.05 ? 644 HOH   A O   1 
HETATM 6075 O  O   . HOH   G 4 .   ? 28.97   19.207  29.235  1   41.95 ? 645 HOH   A O   1 
HETATM 6076 O  O   . HOH   G 4 .   ? -2.812  29.723  17.352  1   33.54 ? 646 HOH   A O   1 
HETATM 6077 O  O   . HOH   G 4 .   ? 37.884  45.169  3.583   1   36.83 ? 647 HOH   A O   1 
HETATM 6078 O  O   . HOH   G 4 .   ? 6.953   47.149  24.498  1   39.2  ? 648 HOH   A O   1 
HETATM 6079 O  O   . HOH   G 4 .   ? 8.378   13.099  38.79   1   45.09 ? 649 HOH   A O   1 
HETATM 6080 O  O   . HOH   G 4 .   ? -4.697  4.557   30.541  1   42.28 ? 650 HOH   A O   1 
HETATM 6081 O  O   . HOH   G 4 .   ? 10.758  29.979  7.929   1   44.36 ? 651 HOH   A O   1 
HETATM 6082 O  O   . HOH   G 4 .   ? 6.064   28.983  17.513  1   38.77 ? 652 HOH   A O   1 
HETATM 6083 O  O   . HOH   G 4 .   ? -17.29  21.548  31.983  1   43.2  ? 653 HOH   A O   1 
HETATM 6084 O  O   . HOH   G 4 .   ? -0.399  22      44.332  1   33.57 ? 654 HOH   A O   1 
HETATM 6085 O  O   . HOH   G 4 .   ? 7.461   21.52   29.226  1   29.84 ? 655 HOH   A O   1 
HETATM 6086 O  O   . HOH   G 4 .   ? 4.365   21.102  15.391  1   36.54 ? 656 HOH   A O   1 
HETATM 6087 O  O   . HOH   G 4 .   ? 28.887  32.536  34.669  1   31.32 ? 657 HOH   A O   1 
HETATM 6088 O  O   . HOH   G 4 .   ? 6.935   47.94   29.011  1   40.47 ? 658 HOH   A O   1 
HETATM 6089 O  O   . HOH   G 4 .   ? 10.854  12.147  30.479  1   37.96 ? 659 HOH   A O   1 
HETATM 6090 O  O   . HOH   G 4 .   ? -2.819  30.257  20.133  1   26.61 ? 660 HOH   A O   1 
HETATM 6091 O  O   . HOH   G 4 .   ? 8.5     26.059  37.499  1   34.78 ? 661 HOH   A O   1 
HETATM 6092 O  O   . HOH   G 4 .   ? 24.293  42.931  30.961  1   39.53 ? 662 HOH   A O   1 
HETATM 6093 O  O   . HOH   G 4 .   ? -3.89   39.397  37.232  1   39.05 ? 663 HOH   A O   1 
HETATM 6094 O  O   . HOH   G 4 .   ? 10.382  26.422  21.802  1   28.21 ? 664 HOH   A O   1 
HETATM 6095 O  O   . HOH   G 4 .   ? 10.48   43.736  20.943  1   31.86 ? 665 HOH   A O   1 
HETATM 6096 O  O   . HOH   G 4 .   ? 21.325  33.843  32.649  1   29.36 ? 666 HOH   A O   1 
HETATM 6097 O  O   . HOH   G 4 .   ? 12.085  30.015  20.751  1   32.82 ? 667 HOH   A O   1 
HETATM 6098 O  O   . HOH   G 4 .   ? 30.549  28.116  14.534  1   46.3  ? 668 HOH   A O   1 
HETATM 6099 O  O   . HOH   G 4 .   ? 5.413   25.473  14.219  1   45.47 ? 669 HOH   A O   1 
HETATM 6100 O  O   . HOH   G 4 .   ? 41.751  35.024  12.886  1   50.02 ? 670 HOH   A O   1 
HETATM 6101 O  O   . HOH   G 4 .   ? 11.205  27.585  19.555  1   31.07 ? 671 HOH   A O   1 
HETATM 6102 O  O   . HOH   G 4 .   ? 27.094  43.554  24.53   1   39.63 ? 672 HOH   A O   1 
HETATM 6103 O  O   . HOH   G 4 .   ? 22.044  24.758  23.412  1   34.74 ? 673 HOH   A O   1 
HETATM 6104 O  O   . HOH   G 4 .   ? 7.233   41.096  45.363  1   41.59 ? 674 HOH   A O   1 
HETATM 6105 O  O   . HOH   G 4 .   ? 12.948  25.856  37.407  1   44.58 ? 675 HOH   A O   1 
HETATM 6106 O  O   . HOH   G 4 .   ? 32.537  40.767  0.567   1   36.62 ? 676 HOH   A O   1 
HETATM 6107 O  O   . HOH   G 4 .   ? -5.819  22.337  45.369  1   42.93 ? 677 HOH   A O   1 
HETATM 6108 O  O   . HOH   G 4 .   ? -3.289  22.529  46.38   1   49.97 ? 678 HOH   A O   1 
HETATM 6109 O  O   . HOH   G 4 .   ? 22.558  31.959  31.272  1   25.95 ? 679 HOH   A O   1 
HETATM 6110 O  O   . HOH   G 4 .   ? -0.957  39.63   36.963  1   34.94 ? 680 HOH   A O   1 
HETATM 6111 O  O   . HOH   G 4 .   ? -17.671 27.004  44.837  1   42.49 ? 681 HOH   A O   1 
HETATM 6112 O  O   . HOH   G 4 .   ? -8.611  34.27   25.735  1   45.16 ? 682 HOH   A O   1 
HETATM 6113 O  O   . HOH   G 4 .   ? -10.765 34.202  35.165  1   57.44 ? 683 HOH   A O   1 
HETATM 6114 O  O   . HOH   G 4 .   ? -14.592 27.371  21.142  1   38.95 ? 684 HOH   A O   1 
HETATM 6115 O  O   . HOH   G 4 .   ? 3.014   35.398  25.225  1   29.5  ? 685 HOH   A O   1 
HETATM 6116 O  O   . HOH   G 4 .   ? 17.395  29.833  23.793  1   29.64 ? 686 HOH   A O   1 
HETATM 6117 O  O   . HOH   G 4 .   ? 25.159  24.715  20.986  1   54.53 ? 687 HOH   A O   1 
HETATM 6118 O  O   . HOH   G 4 .   ? -1.11   38.552  34.329  1   42.41 ? 688 HOH   A O   1 
HETATM 6119 O  O   . HOH   G 4 .   ? 8.385   8.489   31.819  1   32.03 ? 689 HOH   A O   1 
HETATM 6120 O  O   . HOH   G 4 .   ? 36.526  40.377  30.557  1   35.43 ? 690 HOH   A O   1 
HETATM 6121 O  O   . HOH   G 4 .   ? 2.435   38.317  13.683  1   47.5  ? 691 HOH   A O   1 
HETATM 6122 O  O   . HOH   G 4 .   ? -11.745 17.49   43.93   1   47.75 ? 692 HOH   A O   1 
HETATM 6123 O  O   . HOH   G 4 .   ? 27.428  20.958  30.61   1   40.11 ? 693 HOH   A O   1 
HETATM 6124 O  O   . HOH   G 4 .   ? -13.09  11.61   31.892  1   36.82 ? 694 HOH   A O   1 
HETATM 6125 O  O   . HOH   G 4 .   ? 9.548   21.968  36.264  1   47.43 ? 695 HOH   A O   1 
HETATM 6126 O  O   . HOH   G 4 .   ? 9.614   45.808  23.189  1   38.84 ? 696 HOH   A O   1 
HETATM 6127 O  O   . HOH   G 4 .   ? 28.798  18.905  11.806  1   48.6  ? 697 HOH   A O   1 
HETATM 6128 O  O   . HOH   G 4 .   ? -10.075 20.213  44.264  1   54.08 ? 698 HOH   A O   1 
HETATM 6129 O  O   . HOH   G 4 .   ? 25.528  22.966  35.285  1   47.52 ? 699 HOH   A O   1 
HETATM 6130 O  O   . HOH   G 4 .   ? 27.236  21.225  33.619  1   55.89 ? 700 HOH   A O   1 
HETATM 6131 O  O   . HOH   G 4 .   ? -10.849 22.521  41.917  1   26.35 ? 701 HOH   A O   1 
HETATM 6132 O  O   . HOH   G 4 .   ? 6.635   22.613  14.031  1   42.93 ? 702 HOH   A O   1 
HETATM 6133 O  O   . HOH   G 4 .   ? -7.585  34.264  32.009  1   44.66 ? 703 HOH   A O   1 
HETATM 6134 O  O   . HOH   G 4 .   ? 2.477   2.65    28.673  1   31.48 ? 704 HOH   A O   1 
HETATM 6135 O  O   . HOH   G 4 .   ? 30.381  44.649  21.894  1   39.83 ? 705 HOH   A O   1 
HETATM 6136 O  O   . HOH   G 4 .   ? 36.802  42.721  20.281  1   44.15 ? 706 HOH   A O   1 
HETATM 6137 O  O   . HOH   G 4 .   ? 2.325   9.665   21.489  1   38.6  ? 707 HOH   A O   1 
HETATM 6138 O  O   . HOH   H 4 .   ? 24.816  0.596   6.27    1   34.65 ? 601 HOH   B O   1 
HETATM 6139 O  O   . HOH   H 4 .   ? 51.679  -4.371  32.485  1   45.68 ? 602 HOH   B O   1 
HETATM 6140 O  O   . HOH   H 4 .   ? 25.727  -8.297  3.647   1   43.21 ? 603 HOH   B O   1 
HETATM 6141 O  O   . HOH   H 4 .   ? 40.506  -2.288  4.756   1   44.61 ? 604 HOH   B O   1 
HETATM 6142 O  O   . HOH   H 4 .   ? 28.9    -1.531  25.585  1   38.65 ? 605 HOH   B O   1 
HETATM 6143 O  O   . HOH   H 4 .   ? 44.403  -1.28   38.839  1   47.35 ? 606 HOH   B O   1 
HETATM 6144 O  O   . HOH   H 4 .   ? 18.321  1.969   16.48   1   26.25 ? 607 HOH   B O   1 
HETATM 6145 O  O   . HOH   H 4 .   ? 29.236  5.129   16.729  1   28.04 ? 608 HOH   B O   1 
HETATM 6146 O  O   . HOH   H 4 .   ? 20.99   13.747  24.761  1   43.61 ? 609 HOH   B O   1 
HETATM 6147 O  O   . HOH   H 4 .   ? 37.063  4.956   13.726  1   31.25 ? 610 HOH   B O   1 
HETATM 6148 O  O   . HOH   H 4 .   ? 7.818   -6.799  4.893   1   44.61 ? 611 HOH   B O   1 
HETATM 6149 O  O   . HOH   H 4 .   ? 10.98   13.233  7.455   1   39.66 ? 612 HOH   B O   1 
HETATM 6150 O  O   . HOH   H 4 .   ? 39.671  13.536  33.198  1   43.48 ? 613 HOH   B O   1 
HETATM 6151 O  O   . HOH   H 4 .   ? 1.462   -2.224  -2.206  1   35.44 ? 614 HOH   B O   1 
HETATM 6152 O  O   . HOH   H 4 .   ? 23.099  -19.688 25.077  1   37.75 ? 615 HOH   B O   1 
HETATM 6153 O  O   . HOH   H 4 .   ? 16.212  3.784   16.29   1   34.09 ? 616 HOH   B O   1 
HETATM 6154 O  O   . HOH   H 4 .   ? 18.015  -1.108  -4.011  1   38.9  ? 617 HOH   B O   1 
HETATM 6155 O  O   . HOH   H 4 .   ? 37.935  5.251   19.684  1   30.64 ? 618 HOH   B O   1 
HETATM 6156 O  O   . HOH   H 4 .   ? 21.486  6.868   18.528  1   34.22 ? 619 HOH   B O   1 
HETATM 6157 O  O   . HOH   H 4 .   ? 1.084   11.529  -5.621  1   50.97 ? 620 HOH   B O   1 
HETATM 6158 O  O   . HOH   H 4 .   ? 21.474  17.842  8.101   1   44.96 ? 621 HOH   B O   1 
HETATM 6159 O  O   . HOH   H 4 .   ? 33.262  -12.297 32.517  1   40.62 ? 622 HOH   B O   1 
HETATM 6160 O  O   . HOH   H 4 .   ? 23.568  -4.113  -0.023  1   52.22 ? 623 HOH   B O   1 
HETATM 6161 O  O   . HOH   H 4 .   ? 51.18   8.61    22.435  1   43.75 ? 624 HOH   B O   1 
HETATM 6162 O  O   . HOH   H 4 .   ? 9.364   7.145   25.149  1   42.89 ? 625 HOH   B O   1 
HETATM 6163 O  O   . HOH   H 4 .   ? 19.742  -6.086  1.47    1   44.42 ? 626 HOH   B O   1 
HETATM 6164 O  O   . HOH   H 4 .   ? 27.521  16.396  7.278   1   49.93 ? 627 HOH   B O   1 
HETATM 6165 O  O   . HOH   H 4 .   ? 40.498  3.92    8.136   1   36.2  ? 628 HOH   B O   1 
HETATM 6166 O  O   . HOH   H 4 .   ? 22.89   17.822  12.451  1   39.02 ? 629 HOH   B O   1 
HETATM 6167 O  O   . HOH   H 4 .   ? 13.711  -14.116 22.412  1   42.47 ? 630 HOH   B O   1 
HETATM 6168 O  O   . HOH   H 4 .   ? 5.134   -6.707  12.22   1   37.09 ? 631 HOH   B O   1 
HETATM 6169 O  O   . HOH   H 4 .   ? 12.032  3.948   21.463  1   38.84 ? 632 HOH   B O   1 
HETATM 6170 O  O   . HOH   H 4 .   ? 28.788  2.236   31.114  1   40.29 ? 633 HOH   B O   1 
HETATM 6171 O  O   . HOH   H 4 .   ? 12.06   -12.437 12.63   1   40.74 ? 634 HOH   B O   1 
HETATM 6172 O  O   . HOH   H 4 .   ? 25.781  -21.235 17.981  1   47.11 ? 635 HOH   B O   1 
HETATM 6173 O  O   . HOH   H 4 .   ? 24.039  -1.099  -2.826  1   38.73 ? 636 HOH   B O   1 
HETATM 6174 O  O   . HOH   H 4 .   ? -2.574  8.284   -5.430  1   46.36 ? 637 HOH   B O   1 
HETATM 6175 O  O   . HOH   H 4 .   ? 37.98   -6.012  33.947  1   39.43 ? 638 HOH   B O   1 
HETATM 6176 O  O   . HOH   H 4 .   ? 26.235  -1.04   25.789  1   43.23 ? 639 HOH   B O   1 
HETATM 6177 O  O   . HOH   H 4 .   ? 26.72   5.652   12.045  1   34.71 ? 640 HOH   B O   1 
HETATM 6178 O  O   . HOH   H 4 .   ? 20.57   3.502   17.059  1   31.55 ? 641 HOH   B O   1 
HETATM 6179 O  O   . HOH   H 4 .   ? 30.953  4.176   23.164  1   27.79 ? 642 HOH   B O   1 
HETATM 6180 O  O   . HOH   H 4 .   ? 4.638   8.005   -10.413 1   34.4  ? 643 HOH   B O   1 
HETATM 6181 O  O   . HOH   H 4 .   ? 46.647  -7.271  31.072  1   38.06 ? 644 HOH   B O   1 
HETATM 6182 O  O   . HOH   H 4 .   ? 34.031  -4.426  31.846  1   42.42 ? 645 HOH   B O   1 
HETATM 6183 O  O   . HOH   H 4 .   ? 0.1     3.414   13.055  1   37    ? 646 HOH   B O   1 
HETATM 6184 O  O   . HOH   H 4 .   ? 52.471  2.999   12.129  1   47.41 ? 647 HOH   B O   1 
HETATM 6185 O  O   . HOH   H 4 .   ? 44.317  -13.306 24.767  1   36.17 ? 648 HOH   B O   1 
HETATM 6186 O  O   . HOH   H 4 .   ? 27.132  17.001  -2.561  1   46.1  ? 649 HOH   B O   1 
HETATM 6187 O  O   . HOH   H 4 .   ? 29.178  -4.312  27.356  1   35.64 ? 650 HOH   B O   1 
HETATM 6188 O  O   . HOH   H 4 .   ? -3.972  6.257   3.034   1   54.86 ? 651 HOH   B O   1 
HETATM 6189 O  O   . HOH   H 4 .   ? 18.839  -17.183 19.022  1   31.06 ? 652 HOH   B O   1 
HETATM 6190 O  O   . HOH   H 4 .   ? 14.892  -3.999  18.969  1   30.15 ? 653 HOH   B O   1 
HETATM 6191 O  O   . HOH   H 4 .   ? 27.627  -8.275  1.613   1   43.33 ? 654 HOH   B O   1 
HETATM 6192 O  O   . HOH   H 4 .   ? 28.81   -13.614 4.182   1   40.6  ? 655 HOH   B O   1 
HETATM 6193 O  O   . HOH   H 4 .   ? 52.086  -15.251 29.606  1   50.29 ? 656 HOH   B O   1 
HETATM 6194 O  O   . HOH   H 4 .   ? 31.762  5.121   9.113   1   32.32 ? 657 HOH   B O   1 
HETATM 6195 O  O   . HOH   H 4 .   ? 38.881  -11.969 29.525  1   35.69 ? 658 HOH   B O   1 
HETATM 6196 O  O   . HOH   H 4 .   ? 15.842  -6.24   18.986  1   22.28 ? 659 HOH   B O   1 
HETATM 6197 O  O   . HOH   H 4 .   ? -1.534  12.801  6.986   1   42.92 ? 660 HOH   B O   1 
HETATM 6198 O  O   . HOH   H 4 .   ? 23.932  3.19    0.55    1   37.42 ? 661 HOH   B O   1 
HETATM 6199 O  O   . HOH   H 4 .   ? 39.89   -12.928 18.452  1   35.87 ? 662 HOH   B O   1 
HETATM 6200 O  O   . HOH   H 4 .   ? 40.748  -7.215  35.298  1   37.36 ? 663 HOH   B O   1 
HETATM 6201 O  O   . HOH   H 4 .   ? 25.584  2.781   11.447  1   34.6  ? 664 HOH   B O   1 
HETATM 6202 O  O   . HOH   H 4 .   ? 48.855  -5.206  31.768  1   36.57 ? 665 HOH   B O   1 
HETATM 6203 O  O   . HOH   H 4 .   ? 11.842  11.23   24.662  1   36.45 ? 666 HOH   B O   1 
HETATM 6204 O  O   . HOH   H 4 .   ? 27.575  5.002   14.399  1   27.89 ? 667 HOH   B O   1 
HETATM 6205 O  O   . HOH   H 4 .   ? 8.034   13.482  23.687  1   37.45 ? 668 HOH   B O   1 
HETATM 6206 O  O   . HOH   H 4 .   ? 20.215  1.731   14.175  1   30.96 ? 669 HOH   B O   1 
HETATM 6207 O  O   . HOH   H 4 .   ? 37.739  -15.456 18.373  1   45.81 ? 670 HOH   B O   1 
HETATM 6208 O  O   . HOH   H 4 .   ? 34.099  -4.995  11.487  1   32.88 ? 671 HOH   B O   1 
HETATM 6209 O  O   . HOH   H 4 .   ? 40.426  1.868   10.017  1   31.61 ? 672 HOH   B O   1 
HETATM 6210 O  O   . HOH   H 4 .   ? 14.438  -16.068 10.211  1   45.82 ? 673 HOH   B O   1 
HETATM 6211 O  O   . HOH   H 4 .   ? 34.539  -0.646  0.688   1   45.58 ? 674 HOH   B O   1 
HETATM 6212 O  O   . HOH   H 4 .   ? 26.681  17.263  14.064  1   48.46 ? 675 HOH   B O   1 
HETATM 6213 O  O   . HOH   H 4 .   ? 11.106  5.255   25.346  1   29.35 ? 676 HOH   B O   1 
HETATM 6214 O  O   . HOH   H 4 .   ? 31.744  12.261  10.262  1   42.4  ? 677 HOH   B O   1 
HETATM 6215 O  O   . HOH   H 4 .   ? 25.203  11.256  25.699  1   50.16 ? 678 HOH   B O   1 
HETATM 6216 O  O   . HOH   H 4 .   ? 26.162  1.92    26.168  1   46.35 ? 679 HOH   B O   1 
HETATM 6217 O  O   . HOH   H 4 .   ? 35.33   -5.754  33.985  1   38.07 ? 680 HOH   B O   1 
HETATM 6218 O  O   . HOH   H 4 .   ? 18.809  13.459  2.896   1   54.21 ? 681 HOH   B O   1 
HETATM 6219 O  O   . HOH   H 4 .   ? 11.324  -10.058 6.993   1   41.05 ? 682 HOH   B O   1 
# 
