data_9ESB
# 
_entry.id   9ESB 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9ESB         pdb_00009esb 10.2210/pdb9esb/pdb 
WWPDB D_1292136146 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-03-05 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9ESB 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-26 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              aengus.mac-sweeney@idorsia.com 
_pdbx_contact_author.name_first         Aengus 
_pdbx_contact_author.name_last          'Mac Sweeney' 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7250-9541 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Wicki, M.'       1 ? 
'Mac Sweeney, A.' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'SAR and cellular potency optimization of novel heme-binding IDO1 inhibitors' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Cren, S.'        1 ? 
primary 'Lotz, C.'        2 ? 
primary 'Mac Sweeney, A.' 3 ? 
primary 'Lange, R.'       4 ? 
primary 'Kimmerlin, T.'   5 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Indoleamine 2,3-dioxygenase 1'                                                        47085.105 2  1.13.11.52 ? 
? ? 
2 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE'                                                      616.487   2  ?          ? 
? ? 
3 non-polymer syn '(~{R})-(6-chloranylimidazo[1,5-a]pyridin-5-yl)-(1-phenyl-1,2,3-triazol-4-yl)methanol' 325.752   2  ?          ? 
? ? 
4 water       nat water                                                                                  18.015    68 ?          ? 
? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'IDO-1,Indoleamine-pyrrole 2,3-dioxygenase' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MGSSHHHHHHSAALEVLFQGPHMWTISKEYHIDEEVGFALPNPQENLPDFYNDWMFIAKHLPDLIESGQLRERVEKLNML
SIDHLTDHKSQRLARLVLGCITMAYVWGKGHGDVRKVLPRNIAVPYCQLSKKLELPPILVYADCVLANWKKKDPNKPLTY
ENMDVLFSFRDGDCSKGFFLVSLLVEIAAASAIKVIPTVFKAMQMQERDTLLKALLEIASCLEKALQVFHQIHDHVNPKA
FFSVLRIYLSGWKGNPQLSDGLVYEGFWEDPKEFAGGSAGQSSVFQCFDVLLGIQQTAGGGHAAQFLQDMRRYMPPAHRN
FLCSLESNPSVREFVLSKGDAGLREAYDACVKALVSLRSYHLQIVTKYILIPASQQPKENKTSEDPSKLEAKGTGGTDLM
NFLKTVRSTTEKSLLKEG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSAALEVLFQGPHMWTISKEYHIDEEVGFALPNPQENLPDFYNDWMFIAKHLPDLIESGQLRERVEKLNML
SIDHLTDHKSQRLARLVLGCITMAYVWGKGHGDVRKVLPRNIAVPYCQLSKKLELPPILVYADCVLANWKKKDPNKPLTY
ENMDVLFSFRDGDCSKGFFLVSLLVEIAAASAIKVIPTVFKAMQMQERDTLLKALLEIASCLEKALQVFHQIHDHVNPKA
FFSVLRIYLSGWKGNPQLSDGLVYEGFWEDPKEFAGGSAGQSSVFQCFDVLLGIQQTAGGGHAAQFLQDMRRYMPPAHRN
FLCSLESNPSVREFVLSKGDAGLREAYDACVKALVSLRSYHLQIVTKYILIPASQQPKENKTSEDPSKLEAKGTGGTDLM
NFLKTVRSTTEKSLLKEG
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'PROTOPORPHYRIN IX CONTAINING FE'                                                      HEM   
3 '(~{R})-(6-chloranylimidazo[1,5-a]pyridin-5-yl)-(1-phenyl-1,2,3-triazol-4-yl)methanol' A1H6T 
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 
A1H6T non-polymer         . '(~{R})-(6-chloranylimidazo[1,5-a]pyridin-5-yl)-(1-phenyl-1,2,3-triazol-4-yl)methanol' ?    
'C16 H12 Cl N5 O'  325.752 
ALA   'L-peptide linking' y ALANINE                                                                                ?    
'C3 H7 N O2'       89.093  
ARG   'L-peptide linking' y ARGININE                                                                               ?    
'C6 H15 N4 O2 1'   175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                             ?    
'C4 H8 N2 O3'      132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                        ?    
'C4 H7 N O4'       133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                               ?    
'C3 H7 N O2 S'     121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                              ?    
'C5 H10 N2 O3'     146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                        ?    
'C5 H9 N O4'       147.129 
GLY   'peptide linking'   y GLYCINE                                                                                ?    
'C2 H5 N O2'       75.067  
HEM   non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE'                                                      HEME 
'C34 H32 Fe N4 O4' 616.487 
HIS   'L-peptide linking' y HISTIDINE                                                                              ?    
'C6 H10 N3 O2 1'   156.162 
HOH   non-polymer         . WATER                                                                                  ?    'H2 O' 
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                             ?    
'C6 H13 N O2'      131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                ?    
'C6 H13 N O2'      131.173 
LYS   'L-peptide linking' y LYSINE                                                                                 ?    
'C6 H15 N2 O2 1'   147.195 
MET   'L-peptide linking' y METHIONINE                                                                             ?    
'C5 H11 N O2 S'    149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                          ?    
'C9 H11 N O2'      165.189 
PRO   'L-peptide linking' y PROLINE                                                                                ?    
'C5 H9 N O2'       115.130 
SER   'L-peptide linking' y SERINE                                                                                 ?    
'C3 H7 N O3'       105.093 
THR   'L-peptide linking' y THREONINE                                                                              ?    
'C4 H9 N O3'       119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                             ?    
'C11 H12 N2 O2'    204.225 
TYR   'L-peptide linking' y TYROSINE                                                                               ?    
'C9 H11 N O3'      181.189 
VAL   'L-peptide linking' y VALINE                                                                                 ?    
'C5 H11 N O2'      117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -14 ?   ?   ?   A . n 
A 1 2   GLY 2   -13 ?   ?   ?   A . n 
A 1 3   SER 3   -12 ?   ?   ?   A . n 
A 1 4   SER 4   -11 ?   ?   ?   A . n 
A 1 5   HIS 5   -10 ?   ?   ?   A . n 
A 1 6   HIS 6   -9  ?   ?   ?   A . n 
A 1 7   HIS 7   -8  ?   ?   ?   A . n 
A 1 8   HIS 8   -7  ?   ?   ?   A . n 
A 1 9   HIS 9   -6  ?   ?   ?   A . n 
A 1 10  HIS 10  -5  ?   ?   ?   A . n 
A 1 11  SER 11  -4  ?   ?   ?   A . n 
A 1 12  ALA 12  -3  ?   ?   ?   A . n 
A 1 13  ALA 13  -2  -2  ALA ALA A . n 
A 1 14  LEU 14  -1  -1  LEU LEU A . n 
A 1 15  GLU 15  0   0   GLU GLU A . n 
A 1 16  VAL 16  1   1   VAL VAL A . n 
A 1 17  LEU 17  2   2   LEU LEU A . n 
A 1 18  PHE 18  3   3   PHE PHE A . n 
A 1 19  GLN 19  4   4   GLN GLN A . n 
A 1 20  GLY 20  5   5   GLY GLY A . n 
A 1 21  PRO 21  6   6   PRO PRO A . n 
A 1 22  HIS 22  7   7   HIS HIS A . n 
A 1 23  MET 23  8   8   MET MET A . n 
A 1 24  TRP 24  9   9   TRP TRP A . n 
A 1 25  THR 25  10  10  THR THR A . n 
A 1 26  ILE 26  11  11  ILE ILE A . n 
A 1 27  SER 27  12  12  SER SER A . n 
A 1 28  LYS 28  13  13  LYS LYS A . n 
A 1 29  GLU 29  14  14  GLU GLU A . n 
A 1 30  TYR 30  15  15  TYR TYR A . n 
A 1 31  HIS 31  16  16  HIS HIS A . n 
A 1 32  ILE 32  17  17  ILE ILE A . n 
A 1 33  ASP 33  18  18  ASP ASP A . n 
A 1 34  GLU 34  19  19  GLU GLU A . n 
A 1 35  GLU 35  20  20  GLU GLU A . n 
A 1 36  VAL 36  21  21  VAL VAL A . n 
A 1 37  GLY 37  22  22  GLY GLY A . n 
A 1 38  PHE 38  23  23  PHE PHE A . n 
A 1 39  ALA 39  24  24  ALA ALA A . n 
A 1 40  LEU 40  25  25  LEU LEU A . n 
A 1 41  PRO 41  26  26  PRO PRO A . n 
A 1 42  ASN 42  27  27  ASN ASN A . n 
A 1 43  PRO 43  28  28  PRO PRO A . n 
A 1 44  GLN 44  29  29  GLN GLN A . n 
A 1 45  GLU 45  30  30  GLU GLU A . n 
A 1 46  ASN 46  31  31  ASN ASN A . n 
A 1 47  LEU 47  32  32  LEU LEU A . n 
A 1 48  PRO 48  33  33  PRO PRO A . n 
A 1 49  ASP 49  34  34  ASP ASP A . n 
A 1 50  PHE 50  35  35  PHE PHE A . n 
A 1 51  TYR 51  36  36  TYR TYR A . n 
A 1 52  ASN 52  37  37  ASN ASN A . n 
A 1 53  ASP 53  38  38  ASP ASP A . n 
A 1 54  TRP 54  39  39  TRP TRP A . n 
A 1 55  MET 55  40  40  MET MET A . n 
A 1 56  PHE 56  41  41  PHE PHE A . n 
A 1 57  ILE 57  42  42  ILE ILE A . n 
A 1 58  ALA 58  43  43  ALA ALA A . n 
A 1 59  LYS 59  44  44  LYS LYS A . n 
A 1 60  HIS 60  45  45  HIS HIS A . n 
A 1 61  LEU 61  46  46  LEU LEU A . n 
A 1 62  PRO 62  47  47  PRO PRO A . n 
A 1 63  ASP 63  48  48  ASP ASP A . n 
A 1 64  LEU 64  49  49  LEU LEU A . n 
A 1 65  ILE 65  50  50  ILE ILE A . n 
A 1 66  GLU 66  51  51  GLU GLU A . n 
A 1 67  SER 67  52  52  SER SER A . n 
A 1 68  GLY 68  53  53  GLY GLY A . n 
A 1 69  GLN 69  54  54  GLN GLN A . n 
A 1 70  LEU 70  55  55  LEU LEU A . n 
A 1 71  ARG 71  56  56  ARG ARG A . n 
A 1 72  GLU 72  57  57  GLU GLU A . n 
A 1 73  ARG 73  58  58  ARG ARG A . n 
A 1 74  VAL 74  59  59  VAL VAL A . n 
A 1 75  GLU 75  60  60  GLU GLU A . n 
A 1 76  LYS 76  61  61  LYS LYS A . n 
A 1 77  LEU 77  62  62  LEU LEU A . n 
A 1 78  ASN 78  63  63  ASN ASN A . n 
A 1 79  MET 79  64  64  MET MET A . n 
A 1 80  LEU 80  65  65  LEU LEU A . n 
A 1 81  SER 81  66  66  SER SER A . n 
A 1 82  ILE 82  67  67  ILE ILE A . n 
A 1 83  ASP 83  68  68  ASP ASP A . n 
A 1 84  HIS 84  69  69  HIS HIS A . n 
A 1 85  LEU 85  70  70  LEU LEU A . n 
A 1 86  THR 86  71  71  THR THR A . n 
A 1 87  ASP 87  72  72  ASP ASP A . n 
A 1 88  HIS 88  73  73  HIS HIS A . n 
A 1 89  LYS 89  74  74  LYS LYS A . n 
A 1 90  SER 90  75  75  SER SER A . n 
A 1 91  GLN 91  76  76  GLN GLN A . n 
A 1 92  ARG 92  77  77  ARG ARG A . n 
A 1 93  LEU 93  78  78  LEU LEU A . n 
A 1 94  ALA 94  79  79  ALA ALA A . n 
A 1 95  ARG 95  80  80  ARG ARG A . n 
A 1 96  LEU 96  81  81  LEU LEU A . n 
A 1 97  VAL 97  82  82  VAL VAL A . n 
A 1 98  LEU 98  83  83  LEU LEU A . n 
A 1 99  GLY 99  84  84  GLY GLY A . n 
A 1 100 CYS 100 85  85  CYS CYS A . n 
A 1 101 ILE 101 86  86  ILE ILE A . n 
A 1 102 THR 102 87  87  THR THR A . n 
A 1 103 MET 103 88  88  MET MET A . n 
A 1 104 ALA 104 89  89  ALA ALA A . n 
A 1 105 TYR 105 90  90  TYR TYR A . n 
A 1 106 VAL 106 91  91  VAL VAL A . n 
A 1 107 TRP 107 92  92  TRP TRP A . n 
A 1 108 GLY 108 93  93  GLY GLY A . n 
A 1 109 LYS 109 94  94  LYS LYS A . n 
A 1 110 GLY 110 95  95  GLY GLY A . n 
A 1 111 HIS 111 96  96  HIS HIS A . n 
A 1 112 GLY 112 97  97  GLY GLY A . n 
A 1 113 ASP 113 98  98  ASP ASP A . n 
A 1 114 VAL 114 99  99  VAL VAL A . n 
A 1 115 ARG 115 100 100 ARG ARG A . n 
A 1 116 LYS 116 101 101 LYS LYS A . n 
A 1 117 VAL 117 102 102 VAL VAL A . n 
A 1 118 LEU 118 103 103 LEU LEU A . n 
A 1 119 PRO 119 104 104 PRO PRO A . n 
A 1 120 ARG 120 105 105 ARG ARG A . n 
A 1 121 ASN 121 106 106 ASN ASN A . n 
A 1 122 ILE 122 107 107 ILE ILE A . n 
A 1 123 ALA 123 108 108 ALA ALA A . n 
A 1 124 VAL 124 109 109 VAL VAL A . n 
A 1 125 PRO 125 110 110 PRO PRO A . n 
A 1 126 TYR 126 111 111 TYR TYR A . n 
A 1 127 CYS 127 112 112 CYS CYS A . n 
A 1 128 GLN 128 113 113 GLN GLN A . n 
A 1 129 LEU 129 114 114 LEU LEU A . n 
A 1 130 SER 130 115 115 SER SER A . n 
A 1 131 LYS 131 116 116 LYS LYS A . n 
A 1 132 LYS 132 117 117 LYS LYS A . n 
A 1 133 LEU 133 118 118 LEU LEU A . n 
A 1 134 GLU 134 119 119 GLU GLU A . n 
A 1 135 LEU 135 120 120 LEU LEU A . n 
A 1 136 PRO 136 121 121 PRO PRO A . n 
A 1 137 PRO 137 122 122 PRO PRO A . n 
A 1 138 ILE 138 123 123 ILE ILE A . n 
A 1 139 LEU 139 124 124 LEU LEU A . n 
A 1 140 VAL 140 125 125 VAL VAL A . n 
A 1 141 TYR 141 126 126 TYR TYR A . n 
A 1 142 ALA 142 127 127 ALA ALA A . n 
A 1 143 ASP 143 128 128 ASP ASP A . n 
A 1 144 CYS 144 129 129 CYS CYS A . n 
A 1 145 VAL 145 130 130 VAL VAL A . n 
A 1 146 LEU 146 131 131 LEU LEU A . n 
A 1 147 ALA 147 132 132 ALA ALA A . n 
A 1 148 ASN 148 133 133 ASN ASN A . n 
A 1 149 TRP 149 134 134 TRP TRP A . n 
A 1 150 LYS 150 135 135 LYS LYS A . n 
A 1 151 LYS 151 136 136 LYS LYS A . n 
A 1 152 LYS 152 137 137 LYS LYS A . n 
A 1 153 ASP 153 138 138 ASP ASP A . n 
A 1 154 PRO 154 139 139 PRO PRO A . n 
A 1 155 ASN 155 140 140 ASN ASN A . n 
A 1 156 LYS 156 141 141 LYS LYS A . n 
A 1 157 PRO 157 142 142 PRO PRO A . n 
A 1 158 LEU 158 143 143 LEU LEU A . n 
A 1 159 THR 159 144 144 THR THR A . n 
A 1 160 TYR 160 145 145 TYR TYR A . n 
A 1 161 GLU 161 146 146 GLU GLU A . n 
A 1 162 ASN 162 147 147 ASN ASN A . n 
A 1 163 MET 163 148 148 MET MET A . n 
A 1 164 ASP 164 149 149 ASP ASP A . n 
A 1 165 VAL 165 150 150 VAL VAL A . n 
A 1 166 LEU 166 151 151 LEU LEU A . n 
A 1 167 PHE 167 152 152 PHE PHE A . n 
A 1 168 SER 168 153 153 SER SER A . n 
A 1 169 PHE 169 154 154 PHE PHE A . n 
A 1 170 ARG 170 155 155 ARG ARG A . n 
A 1 171 ASP 171 156 156 ASP ASP A . n 
A 1 172 GLY 172 157 157 GLY GLY A . n 
A 1 173 ASP 173 158 158 ASP ASP A . n 
A 1 174 CYS 174 159 159 CYS CYS A . n 
A 1 175 SER 175 160 160 SER SER A . n 
A 1 176 LYS 176 161 161 LYS LYS A . n 
A 1 177 GLY 177 162 162 GLY GLY A . n 
A 1 178 PHE 178 163 163 PHE PHE A . n 
A 1 179 PHE 179 164 164 PHE PHE A . n 
A 1 180 LEU 180 165 165 LEU LEU A . n 
A 1 181 VAL 181 166 166 VAL VAL A . n 
A 1 182 SER 182 167 167 SER SER A . n 
A 1 183 LEU 183 168 168 LEU LEU A . n 
A 1 184 LEU 184 169 169 LEU LEU A . n 
A 1 185 VAL 185 170 170 VAL VAL A . n 
A 1 186 GLU 186 171 171 GLU GLU A . n 
A 1 187 ILE 187 172 172 ILE ILE A . n 
A 1 188 ALA 188 173 173 ALA ALA A . n 
A 1 189 ALA 189 174 174 ALA ALA A . n 
A 1 190 ALA 190 175 175 ALA ALA A . n 
A 1 191 SER 191 176 176 SER SER A . n 
A 1 192 ALA 192 177 177 ALA ALA A . n 
A 1 193 ILE 193 178 178 ILE ILE A . n 
A 1 194 LYS 194 179 179 LYS LYS A . n 
A 1 195 VAL 195 180 180 VAL VAL A . n 
A 1 196 ILE 196 181 181 ILE ILE A . n 
A 1 197 PRO 197 182 182 PRO PRO A . n 
A 1 198 THR 198 183 183 THR THR A . n 
A 1 199 VAL 199 184 184 VAL VAL A . n 
A 1 200 PHE 200 185 185 PHE PHE A . n 
A 1 201 LYS 201 186 186 LYS LYS A . n 
A 1 202 ALA 202 187 187 ALA ALA A . n 
A 1 203 MET 203 188 188 MET MET A . n 
A 1 204 GLN 204 189 189 GLN GLN A . n 
A 1 205 MET 205 190 190 MET MET A . n 
A 1 206 GLN 206 191 191 GLN GLN A . n 
A 1 207 GLU 207 192 192 GLU GLU A . n 
A 1 208 ARG 208 193 193 ARG ARG A . n 
A 1 209 ASP 209 194 194 ASP ASP A . n 
A 1 210 THR 210 195 195 THR THR A . n 
A 1 211 LEU 211 196 196 LEU LEU A . n 
A 1 212 LEU 212 197 197 LEU LEU A . n 
A 1 213 LYS 213 198 198 LYS LYS A . n 
A 1 214 ALA 214 199 199 ALA ALA A . n 
A 1 215 LEU 215 200 200 LEU LEU A . n 
A 1 216 LEU 216 201 201 LEU LEU A . n 
A 1 217 GLU 217 202 202 GLU GLU A . n 
A 1 218 ILE 218 203 203 ILE ILE A . n 
A 1 219 ALA 219 204 204 ALA ALA A . n 
A 1 220 SER 220 205 205 SER SER A . n 
A 1 221 CYS 221 206 206 CYS CYS A . n 
A 1 222 LEU 222 207 207 LEU LEU A . n 
A 1 223 GLU 223 208 208 GLU GLU A . n 
A 1 224 LYS 224 209 209 LYS LYS A . n 
A 1 225 ALA 225 210 210 ALA ALA A . n 
A 1 226 LEU 226 211 211 LEU LEU A . n 
A 1 227 GLN 227 212 212 GLN GLN A . n 
A 1 228 VAL 228 213 213 VAL VAL A . n 
A 1 229 PHE 229 214 214 PHE PHE A . n 
A 1 230 HIS 230 215 215 HIS HIS A . n 
A 1 231 GLN 231 216 216 GLN GLN A . n 
A 1 232 ILE 232 217 217 ILE ILE A . n 
A 1 233 HIS 233 218 218 HIS HIS A . n 
A 1 234 ASP 234 219 219 ASP ASP A . n 
A 1 235 HIS 235 220 220 HIS HIS A . n 
A 1 236 VAL 236 221 221 VAL VAL A . n 
A 1 237 ASN 237 222 222 ASN ASN A . n 
A 1 238 PRO 238 223 223 PRO PRO A . n 
A 1 239 LYS 239 224 224 LYS LYS A . n 
A 1 240 ALA 240 225 225 ALA ALA A . n 
A 1 241 PHE 241 226 226 PHE PHE A . n 
A 1 242 PHE 242 227 227 PHE PHE A . n 
A 1 243 SER 243 228 228 SER SER A . n 
A 1 244 VAL 244 229 229 VAL VAL A . n 
A 1 245 LEU 245 230 230 LEU LEU A . n 
A 1 246 ARG 246 231 231 ARG ARG A . n 
A 1 247 ILE 247 232 232 ILE ILE A . n 
A 1 248 TYR 248 233 233 TYR TYR A . n 
A 1 249 LEU 249 234 234 LEU LEU A . n 
A 1 250 SER 250 235 235 SER SER A . n 
A 1 251 GLY 251 236 236 GLY GLY A . n 
A 1 252 TRP 252 237 237 TRP TRP A . n 
A 1 253 LYS 253 238 238 LYS LYS A . n 
A 1 254 GLY 254 239 239 GLY GLY A . n 
A 1 255 ASN 255 240 240 ASN ASN A . n 
A 1 256 PRO 256 241 241 PRO PRO A . n 
A 1 257 GLN 257 242 242 GLN GLN A . n 
A 1 258 LEU 258 243 243 LEU LEU A . n 
A 1 259 SER 259 244 244 SER SER A . n 
A 1 260 ASP 260 245 245 ASP ASP A . n 
A 1 261 GLY 261 246 246 GLY GLY A . n 
A 1 262 LEU 262 247 247 LEU LEU A . n 
A 1 263 VAL 263 248 248 VAL VAL A . n 
A 1 264 TYR 264 249 249 TYR TYR A . n 
A 1 265 GLU 265 250 250 GLU GLU A . n 
A 1 266 GLY 266 251 251 GLY GLY A . n 
A 1 267 PHE 267 252 252 PHE PHE A . n 
A 1 268 TRP 268 253 253 TRP TRP A . n 
A 1 269 GLU 269 254 254 GLU GLU A . n 
A 1 270 ASP 270 255 255 ASP ASP A . n 
A 1 271 PRO 271 256 256 PRO PRO A . n 
A 1 272 LYS 272 257 257 LYS LYS A . n 
A 1 273 GLU 273 258 258 GLU GLU A . n 
A 1 274 PHE 274 259 259 PHE PHE A . n 
A 1 275 ALA 275 260 260 ALA ALA A . n 
A 1 276 GLY 276 261 261 GLY GLY A . n 
A 1 277 GLY 277 262 262 GLY GLY A . n 
A 1 278 SER 278 263 263 SER SER A . n 
A 1 279 ALA 279 264 264 ALA ALA A . n 
A 1 280 GLY 280 265 265 GLY GLY A . n 
A 1 281 GLN 281 266 266 GLN GLN A . n 
A 1 282 SER 282 267 267 SER SER A . n 
A 1 283 SER 283 268 268 SER SER A . n 
A 1 284 VAL 284 269 269 VAL VAL A . n 
A 1 285 PHE 285 270 270 PHE PHE A . n 
A 1 286 GLN 286 271 271 GLN GLN A . n 
A 1 287 CYS 287 272 272 CYS CYS A . n 
A 1 288 PHE 288 273 273 PHE PHE A . n 
A 1 289 ASP 289 274 274 ASP ASP A . n 
A 1 290 VAL 290 275 275 VAL VAL A . n 
A 1 291 LEU 291 276 276 LEU LEU A . n 
A 1 292 LEU 292 277 277 LEU LEU A . n 
A 1 293 GLY 293 278 278 GLY GLY A . n 
A 1 294 ILE 294 279 279 ILE ILE A . n 
A 1 295 GLN 295 280 280 GLN GLN A . n 
A 1 296 GLN 296 281 281 GLN GLN A . n 
A 1 297 THR 297 282 282 THR THR A . n 
A 1 298 ALA 298 283 283 ALA ALA A . n 
A 1 299 GLY 299 284 284 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 ?   ?   ?   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 ?   ?   ?   B . n 
B 1 396 GLY 396 381 ?   ?   ?   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        A1H6T 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1H6T 
_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 A1H6T 1  502 1   A1H6T LIG A . 
E 2 HEM   1  501 501 HEM   HEM B . 
F 3 A1H6T 1  502 2   A1H6T LIG B . 
G 4 HOH   1  601 3   HOH   HOH A . 
G 4 HOH   2  602 26  HOH   HOH A . 
G 4 HOH   3  603 23  HOH   HOH A . 
G 4 HOH   4  604 80  HOH   HOH A . 
G 4 HOH   5  605 17  HOH   HOH A . 
G 4 HOH   6  606 4   HOH   HOH A . 
G 4 HOH   7  607 25  HOH   HOH A . 
G 4 HOH   8  608 9   HOH   HOH A . 
G 4 HOH   9  609 29  HOH   HOH A . 
G 4 HOH   10 610 41  HOH   HOH A . 
G 4 HOH   11 611 69  HOH   HOH A . 
G 4 HOH   12 612 8   HOH   HOH A . 
G 4 HOH   13 613 42  HOH   HOH A . 
G 4 HOH   14 614 36  HOH   HOH A . 
G 4 HOH   15 615 74  HOH   HOH A . 
G 4 HOH   16 616 43  HOH   HOH A . 
G 4 HOH   17 617 1   HOH   HOH A . 
G 4 HOH   18 618 18  HOH   HOH A . 
G 4 HOH   19 619 54  HOH   HOH A . 
G 4 HOH   20 620 86  HOH   HOH A . 
G 4 HOH   21 621 11  HOH   HOH A . 
G 4 HOH   22 622 46  HOH   HOH A . 
G 4 HOH   23 623 38  HOH   HOH A . 
G 4 HOH   24 624 5   HOH   HOH A . 
G 4 HOH   25 625 55  HOH   HOH A . 
G 4 HOH   26 626 24  HOH   HOH A . 
G 4 HOH   27 627 91  HOH   HOH A . 
G 4 HOH   28 628 47  HOH   HOH A . 
G 4 HOH   29 629 7   HOH   HOH A . 
G 4 HOH   30 630 90  HOH   HOH A . 
G 4 HOH   31 631 70  HOH   HOH A . 
G 4 HOH   32 632 68  HOH   HOH A . 
G 4 HOH   33 633 20  HOH   HOH A . 
G 4 HOH   34 634 56  HOH   HOH A . 
G 4 HOH   35 635 53  HOH   HOH A . 
G 4 HOH   36 636 28  HOH   HOH A . 
G 4 HOH   37 637 27  HOH   HOH A . 
G 4 HOH   38 638 76  HOH   HOH A . 
G 4 HOH   39 639 34  HOH   HOH A . 
G 4 HOH   40 640 66  HOH   HOH A . 
G 4 HOH   41 641 60  HOH   HOH A . 
G 4 HOH   42 642 50  HOH   HOH A . 
G 4 HOH   43 643 92  HOH   HOH A . 
H 4 HOH   1  601 75  HOH   HOH B . 
H 4 HOH   2  602 10  HOH   HOH B . 
H 4 HOH   3  603 33  HOH   HOH B . 
H 4 HOH   4  604 21  HOH   HOH B . 
H 4 HOH   5  605 15  HOH   HOH B . 
H 4 HOH   6  606 13  HOH   HOH B . 
H 4 HOH   7  607 82  HOH   HOH B . 
H 4 HOH   8  608 58  HOH   HOH B . 
H 4 HOH   9  609 30  HOH   HOH B . 
H 4 HOH   10 610 89  HOH   HOH B . 
H 4 HOH   11 611 52  HOH   HOH B . 
H 4 HOH   12 612 2   HOH   HOH B . 
H 4 HOH   13 613 48  HOH   HOH B . 
H 4 HOH   14 614 22  HOH   HOH B . 
H 4 HOH   15 615 61  HOH   HOH B . 
H 4 HOH   16 616 71  HOH   HOH B . 
H 4 HOH   17 617 67  HOH   HOH B . 
H 4 HOH   18 618 45  HOH   HOH B . 
H 4 HOH   19 619 14  HOH   HOH B . 
H 4 HOH   20 620 37  HOH   HOH B . 
H 4 HOH   21 621 39  HOH   HOH B . 
H 4 HOH   22 622 62  HOH   HOH B . 
H 4 HOH   23 623 84  HOH   HOH B . 
H 4 HOH   24 624 31  HOH   HOH B . 
H 4 HOH   25 625 63  HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A GLU 0   ? CG  ? A GLU 15  CG  
2   1 Y 1 A GLU 0   ? CD  ? A GLU 15  CD  
3   1 Y 1 A GLU 0   ? OE1 ? A GLU 15  OE1 
4   1 Y 1 A GLU 0   ? OE2 ? A GLU 15  OE2 
5   1 Y 1 A GLN 4   ? CG  ? A GLN 19  CG  
6   1 Y 1 A GLN 4   ? CD  ? A GLN 19  CD  
7   1 Y 1 A GLN 4   ? OE1 ? A GLN 19  OE1 
8   1 Y 1 A GLN 4   ? NE2 ? A GLN 19  NE2 
9   1 Y 1 A HIS 7   ? CG  ? A HIS 22  CG  
10  1 Y 1 A HIS 7   ? ND1 ? A HIS 22  ND1 
11  1 Y 1 A HIS 7   ? CD2 ? A HIS 22  CD2 
12  1 Y 1 A HIS 7   ? CE1 ? A HIS 22  CE1 
13  1 Y 1 A HIS 7   ? NE2 ? A HIS 22  NE2 
14  1 Y 1 A LYS 13  ? CG  ? A LYS 28  CG  
15  1 Y 1 A LYS 13  ? CD  ? A LYS 28  CD  
16  1 Y 1 A LYS 13  ? CE  ? A LYS 28  CE  
17  1 Y 1 A LYS 13  ? NZ  ? A LYS 28  NZ  
18  1 Y 1 A GLU 19  ? CG  ? A GLU 34  CG  
19  1 Y 1 A GLU 19  ? CD  ? A GLU 34  CD  
20  1 Y 1 A GLU 19  ? OE1 ? A GLU 34  OE1 
21  1 Y 1 A GLU 19  ? OE2 ? A GLU 34  OE2 
22  1 Y 1 A LYS 61  ? CG  ? A LYS 76  CG  
23  1 Y 1 A LYS 61  ? CD  ? A LYS 76  CD  
24  1 Y 1 A LYS 61  ? CE  ? A LYS 76  CE  
25  1 Y 1 A LYS 61  ? NZ  ? A LYS 76  NZ  
26  1 Y 1 A SER 66  ? OG  ? A SER 81  OG  
27  1 Y 1 A LYS 101 ? CG  ? A LYS 116 CG  
28  1 Y 1 A LYS 101 ? CD  ? A LYS 116 CD  
29  1 Y 1 A LYS 101 ? CE  ? A LYS 116 CE  
30  1 Y 1 A LYS 101 ? NZ  ? A LYS 116 NZ  
31  1 Y 1 A LYS 186 ? CG  ? A LYS 201 CG  
32  1 Y 1 A LYS 186 ? CD  ? A LYS 201 CD  
33  1 Y 1 A LYS 186 ? CE  ? A LYS 201 CE  
34  1 Y 1 A LYS 186 ? NZ  ? A LYS 201 NZ  
35  1 Y 1 A LYS 198 ? CG  ? A LYS 213 CG  
36  1 Y 1 A LYS 198 ? CD  ? A LYS 213 CD  
37  1 Y 1 A LYS 198 ? CE  ? A LYS 213 CE  
38  1 Y 1 A LYS 198 ? NZ  ? A LYS 213 NZ  
39  1 Y 1 A LYS 209 ? CG  ? A LYS 224 CG  
40  1 Y 1 A LYS 209 ? CD  ? A LYS 224 CD  
41  1 Y 1 A LYS 209 ? CE  ? A LYS 224 CE  
42  1 Y 1 A LYS 209 ? NZ  ? A LYS 224 NZ  
43  1 Y 1 A LYS 224 ? CG  ? A LYS 239 CG  
44  1 Y 1 A LYS 224 ? CD  ? A LYS 239 CD  
45  1 Y 1 A LYS 224 ? CE  ? A LYS 239 CE  
46  1 Y 1 A LYS 224 ? NZ  ? A LYS 239 NZ  
47  1 Y 1 A GLU 318 ? CG  ? A GLU 333 CG  
48  1 Y 1 A GLU 318 ? CD  ? A GLU 333 CD  
49  1 Y 1 A GLU 318 ? OE1 ? A GLU 333 OE1 
50  1 Y 1 A GLU 318 ? OE2 ? A GLU 333 OE2 
51  1 Y 1 A LYS 337 ? CG  ? A LYS 352 CG  
52  1 Y 1 A LYS 337 ? CD  ? A LYS 352 CD  
53  1 Y 1 A LYS 337 ? CE  ? A LYS 352 CE  
54  1 Y 1 A LYS 337 ? NZ  ? A LYS 352 NZ  
55  1 Y 1 A LYS 401 ? CG  ? A LYS 416 CG  
56  1 Y 1 A LYS 401 ? CD  ? A LYS 416 CD  
57  1 Y 1 A LYS 401 ? CE  ? A LYS 416 CE  
58  1 Y 1 A LYS 401 ? NZ  ? A LYS 416 NZ  
59  1 Y 1 B LYS 13  ? CD  ? B LYS 28  CD  
60  1 Y 1 B LYS 13  ? CE  ? B LYS 28  CE  
61  1 Y 1 B LYS 13  ? NZ  ? B LYS 28  NZ  
62  1 Y 1 B GLU 19  ? CG  ? B GLU 34  CG  
63  1 Y 1 B GLU 19  ? CD  ? B GLU 34  CD  
64  1 Y 1 B GLU 19  ? OE1 ? B GLU 34  OE1 
65  1 Y 1 B GLU 19  ? OE2 ? B GLU 34  OE2 
66  1 Y 1 B ASP 34  ? CG  ? B ASP 49  CG  
67  1 Y 1 B ASP 34  ? OD1 ? B ASP 49  OD1 
68  1 Y 1 B ASP 34  ? OD2 ? B ASP 49  OD2 
69  1 Y 1 B LYS 44  ? CG  ? B LYS 59  CG  
70  1 Y 1 B LYS 44  ? CD  ? B LYS 59  CD  
71  1 Y 1 B LYS 44  ? CE  ? B LYS 59  CE  
72  1 Y 1 B LYS 44  ? NZ  ? B LYS 59  NZ  
73  1 Y 1 B ASP 48  ? CG  ? B ASP 63  CG  
74  1 Y 1 B ASP 48  ? OD1 ? B ASP 63  OD1 
75  1 Y 1 B ASP 48  ? OD2 ? B ASP 63  OD2 
76  1 Y 1 B ARG 58  ? CG  ? B ARG 73  CG  
77  1 Y 1 B ARG 58  ? CD  ? B ARG 73  CD  
78  1 Y 1 B ARG 58  ? NE  ? B ARG 73  NE  
79  1 Y 1 B ARG 58  ? CZ  ? B ARG 73  CZ  
80  1 Y 1 B ARG 58  ? NH1 ? B ARG 73  NH1 
81  1 Y 1 B ARG 58  ? NH2 ? B ARG 73  NH2 
82  1 Y 1 B LYS 61  ? CG  ? B LYS 76  CG  
83  1 Y 1 B LYS 61  ? CD  ? B LYS 76  CD  
84  1 Y 1 B LYS 61  ? CE  ? B LYS 76  CE  
85  1 Y 1 B LYS 61  ? NZ  ? B LYS 76  NZ  
86  1 Y 1 B SER 66  ? OG  ? B SER 81  OG  
87  1 Y 1 B HIS 69  ? CG  ? B HIS 84  CG  
88  1 Y 1 B HIS 69  ? ND1 ? B HIS 84  ND1 
89  1 Y 1 B HIS 69  ? CD2 ? B HIS 84  CD2 
90  1 Y 1 B HIS 69  ? CE1 ? B HIS 84  CE1 
91  1 Y 1 B HIS 69  ? NE2 ? B HIS 84  NE2 
92  1 Y 1 B THR 71  ? OG1 ? B THR 86  OG1 
93  1 Y 1 B THR 71  ? CG2 ? B THR 86  CG2 
94  1 Y 1 B SER 75  ? OG  ? B SER 90  OG  
95  1 Y 1 B LYS 101 ? CG  ? B LYS 116 CG  
96  1 Y 1 B LYS 101 ? CD  ? B LYS 116 CD  
97  1 Y 1 B LYS 101 ? CE  ? B LYS 116 CE  
98  1 Y 1 B LYS 101 ? NZ  ? B LYS 116 NZ  
99  1 Y 1 B ARG 105 ? CG  ? B ARG 120 CG  
100 1 Y 1 B ARG 105 ? CD  ? B ARG 120 CD  
101 1 Y 1 B ARG 105 ? NE  ? B ARG 120 NE  
102 1 Y 1 B ARG 105 ? CZ  ? B ARG 120 CZ  
103 1 Y 1 B ARG 105 ? NH1 ? B ARG 120 NH1 
104 1 Y 1 B ARG 105 ? NH2 ? B ARG 120 NH2 
105 1 Y 1 B GLN 113 ? CG  ? B GLN 128 CG  
106 1 Y 1 B GLN 113 ? CD  ? B GLN 128 CD  
107 1 Y 1 B GLN 113 ? OE1 ? B GLN 128 OE1 
108 1 Y 1 B GLN 113 ? NE2 ? B GLN 128 NE2 
109 1 Y 1 B LYS 116 ? CE  ? B LYS 131 CE  
110 1 Y 1 B LYS 116 ? NZ  ? B LYS 131 NZ  
111 1 Y 1 B LYS 117 ? CG  ? B LYS 132 CG  
112 1 Y 1 B LYS 117 ? CD  ? B LYS 132 CD  
113 1 Y 1 B LYS 117 ? CE  ? B LYS 132 CE  
114 1 Y 1 B LYS 117 ? NZ  ? B LYS 132 NZ  
115 1 Y 1 B LYS 141 ? CG  ? B LYS 156 CG  
116 1 Y 1 B LYS 141 ? CD  ? B LYS 156 CD  
117 1 Y 1 B LYS 141 ? CE  ? B LYS 156 CE  
118 1 Y 1 B LYS 141 ? NZ  ? B LYS 156 NZ  
119 1 Y 1 B GLU 146 ? CG  ? B GLU 161 CG  
120 1 Y 1 B GLU 146 ? CD  ? B GLU 161 CD  
121 1 Y 1 B GLU 146 ? OE1 ? B GLU 161 OE1 
122 1 Y 1 B GLU 146 ? OE2 ? B GLU 161 OE2 
123 1 Y 1 B LYS 186 ? CG  ? B LYS 201 CG  
124 1 Y 1 B LYS 186 ? CD  ? B LYS 201 CD  
125 1 Y 1 B LYS 186 ? CE  ? B LYS 201 CE  
126 1 Y 1 B LYS 186 ? NZ  ? B LYS 201 NZ  
127 1 Y 1 B GLN 189 ? CG  ? B GLN 204 CG  
128 1 Y 1 B GLN 189 ? CD  ? B GLN 204 CD  
129 1 Y 1 B GLN 189 ? OE1 ? B GLN 204 OE1 
130 1 Y 1 B GLN 189 ? NE2 ? B GLN 204 NE2 
131 1 Y 1 B LYS 198 ? CG  ? B LYS 213 CG  
132 1 Y 1 B LYS 198 ? CD  ? B LYS 213 CD  
133 1 Y 1 B LYS 198 ? CE  ? B LYS 213 CE  
134 1 Y 1 B LYS 198 ? NZ  ? B LYS 213 NZ  
135 1 Y 1 B LYS 209 ? CG  ? B LYS 224 CG  
136 1 Y 1 B LYS 209 ? CD  ? B LYS 224 CD  
137 1 Y 1 B LYS 209 ? CE  ? B LYS 224 CE  
138 1 Y 1 B LYS 209 ? NZ  ? B LYS 224 NZ  
139 1 Y 1 B LYS 224 ? CG  ? B LYS 239 CG  
140 1 Y 1 B LYS 224 ? CD  ? B LYS 239 CD  
141 1 Y 1 B LYS 224 ? CE  ? B LYS 239 CE  
142 1 Y 1 B LYS 224 ? NZ  ? B LYS 239 NZ  
143 1 Y 1 B GLU 254 ? CG  ? B GLU 269 CG  
144 1 Y 1 B GLU 254 ? CD  ? B GLU 269 CD  
145 1 Y 1 B GLU 254 ? OE1 ? B GLU 269 OE1 
146 1 Y 1 B GLU 254 ? OE2 ? B GLU 269 OE2 
147 1 Y 1 B ASP 255 ? CG  ? B ASP 270 CG  
148 1 Y 1 B ASP 255 ? OD1 ? B ASP 270 OD1 
149 1 Y 1 B ASP 255 ? OD2 ? B ASP 270 OD2 
150 1 Y 1 B LYS 257 ? CG  ? B LYS 272 CG  
151 1 Y 1 B LYS 257 ? CD  ? B LYS 272 CD  
152 1 Y 1 B LYS 257 ? CE  ? B LYS 272 CE  
153 1 Y 1 B LYS 257 ? NZ  ? B LYS 272 NZ  
154 1 Y 1 B ARG 297 ? CG  ? B ARG 312 CG  
155 1 Y 1 B ARG 297 ? CD  ? B ARG 312 CD  
156 1 Y 1 B ARG 297 ? NE  ? B ARG 312 NE  
157 1 Y 1 B ARG 297 ? CZ  ? B ARG 312 CZ  
158 1 Y 1 B ARG 297 ? NH1 ? B ARG 312 NH1 
159 1 Y 1 B ARG 297 ? NH2 ? B ARG 312 NH2 
160 1 Y 1 B GLU 330 ? CG  ? B GLU 345 CG  
161 1 Y 1 B GLU 330 ? CD  ? B GLU 345 CD  
162 1 Y 1 B GLU 330 ? OE1 ? B GLU 345 OE1 
163 1 Y 1 B GLU 330 ? OE2 ? B GLU 345 OE2 
164 1 Y 1 B LYS 337 ? CG  ? B LYS 352 CG  
165 1 Y 1 B LYS 337 ? CD  ? B LYS 352 CD  
166 1 Y 1 B LYS 337 ? CE  ? B LYS 352 CE  
167 1 Y 1 B LYS 337 ? NZ  ? B LYS 352 NZ  
168 1 Y 1 B GLN 361 ? CG  ? B GLN 376 CG  
169 1 Y 1 B GLN 361 ? CD  ? B GLN 376 CD  
170 1 Y 1 B GLN 361 ? OE1 ? B GLN 376 OE1 
171 1 Y 1 B GLN 361 ? NE2 ? B GLN 376 NE2 
172 1 Y 1 B THR 382 ? OG1 ? B THR 397 OG1 
173 1 Y 1 B THR 382 ? CG2 ? B THR 397 CG2 
174 1 Y 1 B ASP 383 ? CG  ? B ASP 398 CG  
175 1 Y 1 B ASP 383 ? OD1 ? B ASP 398 OD1 
176 1 Y 1 B ASP 383 ? OD2 ? B ASP 398 OD2 
177 1 Y 1 B LYS 401 ? CG  ? B LYS 416 CG  
178 1 Y 1 B LYS 401 ? CD  ? B LYS 416 CD  
179 1 Y 1 B LYS 401 ? CE  ? B LYS 416 CE  
180 1 Y 1 B LYS 401 ? NZ  ? B LYS 416 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? BUSTER   ? ? ? 2.11.8 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .      2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE   ? ? ? .      3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .      4 
# 
_cell.angle_alpha                  90 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9ESB 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     84.245 
_cell.length_a_esd                 ? 
_cell.length_b                     92.135 
_cell.length_b_esd                 ? 
_cell.length_c                     132.329 
_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                         9ESB 
_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                   9ESB 
_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             2.73 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.89 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '10% w/v PEG 4000, 20% v/v glycerol, 0.1 M MOPS/HEPES-Na pH 7.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 2M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2017-10-20 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.00 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SLS BEAMLINE X06DA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.00 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06DA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9ESB 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.25 
_reflns.d_resolution_low                               46.1 
_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                                     94264 
_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                           99.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.3 
_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                                .134 
_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                                   .997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.25 
_reflns_shell.d_res_low                                     2.39 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.84 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             15079 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               1.60 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.4 
_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]                            -0.2288 
_refine.aniso_B[1][2]                            0 
_refine.aniso_B[1][3]                            0 
_refine.aniso_B[2][2]                            0.6309 
_refine.aniso_B[2][3]                            0 
_refine.aniso_B[3][3]                            -0.402 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               50.77 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.936 
_refine.correlation_coeff_Fo_to_Fc_free          0.917 
_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                                 9ESB 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.249 
_refine.ls_d_res_low                             46.07 
_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                     49586 
_refine.ls_number_reflns_R_free                  2478 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.9 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2405 
_refine.ls_R_factor_R_free                       0.2715 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2390 
_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   0.213 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.208 
_refine.pdbx_overall_SU_R_Blow_DPI               0.255 
_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             0.262 
_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                        9ESB 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.36 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.249 
_refine_hist.d_res_low                        46.07 
_refine_hist.number_atoms_solvent             68 
_refine_hist.number_atoms_total               6049 
_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        5849 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         132 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.007 ? 6141 ? t_bond_d                  2  HARMONIC     
'X-RAY DIFFRACTION' ? 0.87  ? 8361 ? t_angle_deg               2  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 2053 ? t_dihedral_angle_d        2  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? 1110 ? t_gen_planes              5  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 6141 ? t_it                      10 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 774  ? t_chiral_improper_torsion 5  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? 4819 ? t_ideal_dist_contact      4  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? 2.76  ? ?    ? t_omega_torsion           ?  ?            
'X-RAY DIFFRACTION' ? 16.81 ? ?    ? t_other_torsion           ?  ?            
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.25 
_refine_ls_shell.d_res_low                        2.27 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                992 
_refine_ls_shell.number_reflns_R_free             50 
_refine_ls_shell.number_reflns_R_work             ? 
_refine_ls_shell.percent_reflns_obs               94.32 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     0.3849 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.3854 
_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                  0.3743 
# 
_struct.entry_id                     9ESB 
_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        9ESB 
_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 9ESB A 24 ? 418 ? P14902 9 ? 403 ? 9 403 
2 1 9ESB 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 9ESB MET A 1  ? UNP P14902 ? ? 'initiating methionine' -14 1  
1 9ESB GLY A 2  ? UNP P14902 ? ? 'expression tag'        -13 2  
1 9ESB SER A 3  ? UNP P14902 ? ? 'expression tag'        -12 3  
1 9ESB SER A 4  ? UNP P14902 ? ? 'expression tag'        -11 4  
1 9ESB HIS A 5  ? UNP P14902 ? ? 'expression tag'        -10 5  
1 9ESB HIS A 6  ? UNP P14902 ? ? 'expression tag'        -9  6  
1 9ESB HIS A 7  ? UNP P14902 ? ? 'expression tag'        -8  7  
1 9ESB HIS A 8  ? UNP P14902 ? ? 'expression tag'        -7  8  
1 9ESB HIS A 9  ? UNP P14902 ? ? 'expression tag'        -6  9  
1 9ESB HIS A 10 ? UNP P14902 ? ? 'expression tag'        -5  10 
1 9ESB SER A 11 ? UNP P14902 ? ? 'expression tag'        -4  11 
1 9ESB ALA A 12 ? UNP P14902 ? ? 'expression tag'        -3  12 
1 9ESB ALA A 13 ? UNP P14902 ? ? 'expression tag'        -2  13 
1 9ESB LEU A 14 ? UNP P14902 ? ? 'expression tag'        -1  14 
1 9ESB GLU A 15 ? UNP P14902 ? ? 'expression tag'        0   15 
1 9ESB VAL A 16 ? UNP P14902 ? ? 'expression tag'        1   16 
1 9ESB LEU A 17 ? UNP P14902 ? ? 'expression tag'        2   17 
1 9ESB PHE A 18 ? UNP P14902 ? ? 'expression tag'        3   18 
1 9ESB GLN A 19 ? UNP P14902 ? ? 'expression tag'        4   19 
1 9ESB GLY A 20 ? UNP P14902 ? ? 'expression tag'        5   20 
1 9ESB PRO A 21 ? UNP P14902 ? ? 'expression tag'        6   21 
1 9ESB HIS A 22 ? UNP P14902 ? ? 'expression tag'        7   22 
1 9ESB MET A 23 ? UNP P14902 ? ? 'expression tag'        8   23 
2 9ESB MET B 1  ? UNP P14902 ? ? 'initiating methionine' -14 24 
2 9ESB GLY B 2  ? UNP P14902 ? ? 'expression tag'        -13 25 
2 9ESB SER B 3  ? UNP P14902 ? ? 'expression tag'        -12 26 
2 9ESB SER B 4  ? UNP P14902 ? ? 'expression tag'        -11 27 
2 9ESB HIS B 5  ? UNP P14902 ? ? 'expression tag'        -10 28 
2 9ESB HIS B 6  ? UNP P14902 ? ? 'expression tag'        -9  29 
2 9ESB HIS B 7  ? UNP P14902 ? ? 'expression tag'        -8  30 
2 9ESB HIS B 8  ? UNP P14902 ? ? 'expression tag'        -7  31 
2 9ESB HIS B 9  ? UNP P14902 ? ? 'expression tag'        -6  32 
2 9ESB HIS B 10 ? UNP P14902 ? ? 'expression tag'        -5  33 
2 9ESB SER B 11 ? UNP P14902 ? ? 'expression tag'        -4  34 
2 9ESB ALA B 12 ? UNP P14902 ? ? 'expression tag'        -3  35 
2 9ESB ALA B 13 ? UNP P14902 ? ? 'expression tag'        -2  36 
2 9ESB LEU B 14 ? UNP P14902 ? ? 'expression tag'        -1  37 
2 9ESB GLU B 15 ? UNP P14902 ? ? 'expression tag'        0   38 
2 9ESB VAL B 16 ? UNP P14902 ? ? 'expression tag'        1   39 
2 9ESB LEU B 17 ? UNP P14902 ? ? 'expression tag'        2   40 
2 9ESB PHE B 18 ? UNP P14902 ? ? 'expression tag'        3   41 
2 9ESB GLN B 19 ? UNP P14902 ? ? 'expression tag'        4   42 
2 9ESB GLY B 20 ? UNP P14902 ? ? 'expression tag'        5   43 
2 9ESB PRO B 21 ? UNP P14902 ? ? 'expression tag'        6   44 
2 9ESB HIS B 22 ? UNP P14902 ? ? 'expression tag'        7   45 
2 9ESB MET B 23 ? UNP P14902 ? ? 'expression tag'        8   46 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 4470  ? 
1 MORE         -53   ? 
1 'SSA (A^2)'  29860 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ALA A 13  ? GLY A 20  ? ALA A -2  GLY A 5   1 ? 8  
HELX_P HELX_P2  AA2 SER A 27  ? HIS A 31  ? SER A 12  HIS A 16  5 ? 5  
HELX_P HELX_P3  AA3 PRO A 48  ? PHE A 50  ? PRO A 33  PHE A 35  5 ? 3  
HELX_P HELX_P4  AA4 TYR A 51  ? HIS A 60  ? TYR A 36  HIS A 45  1 ? 10 
HELX_P HELX_P5  AA5 HIS A 60  ? SER A 67  ? HIS A 45  SER A 52  1 ? 8  
HELX_P HELX_P6  AA6 GLN A 69  ? LYS A 76  ? GLN A 54  LYS A 61  1 ? 8  
HELX_P HELX_P7  AA7 SER A 81  ? LEU A 85  ? SER A 66  LEU A 70  5 ? 5  
HELX_P HELX_P8  AA8 ASP A 87  ? GLY A 108 ? ASP A 72  GLY A 93  1 ? 22 
HELX_P HELX_P9  AA9 PRO A 119 ? GLU A 134 ? PRO A 104 GLU A 119 1 ? 16 
HELX_P HELX_P10 AB1 VAL A 140 ? VAL A 145 ? VAL A 125 VAL A 130 1 ? 6  
HELX_P HELX_P11 AB2 THR A 159 ? GLU A 161 ? THR A 144 GLU A 146 5 ? 3  
HELX_P HELX_P12 AB3 CYS A 174 ? SER A 191 ? CYS A 159 SER A 176 1 ? 18 
HELX_P HELX_P13 AB4 ALA A 192 ? LYS A 194 ? ALA A 177 LYS A 179 5 ? 3  
HELX_P HELX_P14 AB5 VAL A 195 ? MET A 205 ? VAL A 180 MET A 190 1 ? 11 
HELX_P HELX_P15 AB6 GLU A 207 ? HIS A 230 ? GLU A 192 HIS A 215 1 ? 24 
HELX_P HELX_P16 AB7 GLN A 231 ? VAL A 236 ? GLN A 216 VAL A 221 1 ? 6  
HELX_P HELX_P17 AB8 ASN A 237 ? VAL A 244 ? ASN A 222 VAL A 229 1 ? 8  
HELX_P HELX_P18 AB9 VAL A 244 ? SER A 250 ? VAL A 229 SER A 235 1 ? 7  
HELX_P HELX_P19 AC1 ASN A 255 ? SER A 259 ? ASN A 240 SER A 244 5 ? 5  
HELX_P HELX_P20 AC2 SER A 278 ? GLN A 281 ? SER A 263 GLN A 266 5 ? 4  
HELX_P HELX_P21 AC3 SER A 282 ? LEU A 292 ? SER A 267 LEU A 277 1 ? 11 
HELX_P HELX_P22 AC4 GLY A 301 ? MET A 310 ? GLY A 286 MET A 295 1 ? 10 
HELX_P HELX_P23 AC5 ARG A 311 ? MET A 314 ? ARG A 296 MET A 299 5 ? 4  
HELX_P HELX_P24 AC6 PRO A 315 ? ASN A 328 ? PRO A 300 ASN A 313 1 ? 14 
HELX_P HELX_P25 AC7 SER A 330 ? SER A 337 ? SER A 315 SER A 322 1 ? 8  
HELX_P HELX_P26 AC8 ASP A 340 ? ILE A 369 ? ASP A 325 ILE A 354 1 ? 30 
HELX_P HELX_P27 AC9 ILE A 369 ? GLN A 375 ? ILE A 354 GLN A 360 1 ? 7  
HELX_P HELX_P28 AD1 THR A 397 ? LYS A 412 ? THR A 382 LYS A 397 1 ? 16 
HELX_P HELX_P29 AD2 SER B 27  ? HIS B 31  ? SER B 12  HIS B 16  5 ? 5  
HELX_P HELX_P30 AD3 PRO B 48  ? PHE B 50  ? PRO B 33  PHE B 35  5 ? 3  
HELX_P HELX_P31 AD4 TYR B 51  ? HIS B 60  ? TYR B 36  HIS B 45  1 ? 10 
HELX_P HELX_P32 AD5 HIS B 60  ? SER B 67  ? HIS B 45  SER B 52  1 ? 8  
HELX_P HELX_P33 AD6 GLN B 69  ? LYS B 76  ? GLN B 54  LYS B 61  1 ? 8  
HELX_P HELX_P34 AD7 SER B 81  ? LEU B 85  ? SER B 66  LEU B 70  5 ? 5  
HELX_P HELX_P35 AD8 ASP B 87  ? GLY B 108 ? ASP B 72  GLY B 93  1 ? 22 
HELX_P HELX_P36 AD9 PRO B 119 ? GLU B 134 ? PRO B 104 GLU B 119 1 ? 16 
HELX_P HELX_P37 AE1 VAL B 140 ? VAL B 145 ? VAL B 125 VAL B 130 1 ? 6  
HELX_P HELX_P38 AE2 THR B 159 ? GLU B 161 ? THR B 144 GLU B 146 5 ? 3  
HELX_P HELX_P39 AE3 CYS B 174 ? SER B 191 ? CYS B 159 SER B 176 1 ? 18 
HELX_P HELX_P40 AE4 ALA B 192 ? LYS B 194 ? ALA B 177 LYS B 179 5 ? 3  
HELX_P HELX_P41 AE5 VAL B 195 ? MET B 205 ? VAL B 180 MET B 190 1 ? 11 
HELX_P HELX_P42 AE6 GLU B 207 ? HIS B 230 ? GLU B 192 HIS B 215 1 ? 24 
HELX_P HELX_P43 AE7 GLN B 231 ? VAL B 236 ? GLN B 216 VAL B 221 1 ? 6  
HELX_P HELX_P44 AE8 ASN B 237 ? VAL B 244 ? ASN B 222 VAL B 229 1 ? 8  
HELX_P HELX_P45 AE9 VAL B 244 ? SER B 250 ? VAL B 229 SER B 235 1 ? 7  
HELX_P HELX_P46 AF1 ASN B 255 ? SER B 259 ? ASN B 240 SER B 244 5 ? 5  
HELX_P HELX_P47 AF2 SER B 278 ? GLN B 281 ? SER B 263 GLN B 266 5 ? 4  
HELX_P HELX_P48 AF3 SER B 282 ? LEU B 292 ? SER B 267 LEU B 277 1 ? 11 
HELX_P HELX_P49 AF4 GLY B 301 ? MET B 310 ? GLY B 286 MET B 295 1 ? 10 
HELX_P HELX_P50 AF5 ARG B 311 ? MET B 314 ? ARG B 296 MET B 299 5 ? 4  
HELX_P HELX_P51 AF6 PRO B 315 ? ASN B 328 ? PRO B 300 ASN B 313 1 ? 14 
HELX_P HELX_P52 AF7 SER B 330 ? SER B 337 ? SER B 315 SER B 322 1 ? 8  
HELX_P HELX_P53 AF8 ASP B 340 ? ILE B 369 ? ASP B 325 ILE B 354 1 ? 30 
HELX_P HELX_P54 AF9 ILE B 369 ? GLN B 375 ? ILE B 354 GLN B 360 1 ? 7  
HELX_P HELX_P55 AG1 ASP B 398 ? LYS B 412 ? ASP B 383 LYS B 397 1 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 323 SG  ? ? ? 1_555 B CYS   323 SG ? ? A CYS 308 B CYS   308 1_555 ? ? ? ? ? ? ? 2.040 ? ? 
metalc1 metalc ? ? A HIS 361 NE2 ? ? ? 1_555 C HEM   .   FE ? ? A HIS 346 A HEM   501 1_555 ? ? ? ? ? ? ? 1.988 ? ? 
metalc2 metalc ? ? C HEM .   FE  ? ? ? 1_555 D A1H6T .   N4 ? ? A HEM 501 A A1H6T 502 1_555 ? ? ? ? ? ? ? 1.969 ? ? 
metalc3 metalc ? ? B HIS 361 NE2 ? ? ? 1_555 E HEM   .   FE ? ? B HIS 346 B HEM   501 1_555 ? ? ? ? ? ? ? 2.057 ? ? 
metalc4 metalc ? ? E HEM .   FE  ? ? ? 1_555 F A1H6T .   N4 ? ? B HEM 501 B A1H6T 502 1_555 ? ? ? ? ? ? ? 1.961 ? ? 
# 
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 90.9  ? 
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 90.8  ? 
3  NA  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NB ? C HEM   . ? A HEM   501 ? 1_555 90.8  ? 
4  NE2 ? A HIS 361 ? A HIS 346 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NC ? C HEM   . ? A HEM   501 ? 1_555 91.4  ? 
5  NA  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NC ? C HEM   . ? A HEM   501 ? 1_555 177.7 ? 
6  NB  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NC ? C HEM   . ? A HEM   501 ? 1_555 89.1  ? 
7  NE2 ? A HIS 361 ? A HIS 346 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM   . ? A HEM   501 ? 1_555 89.3  ? 
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 89.6  ? 
9  NB  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM   . ? A HEM   501 ? 1_555 179.6 ? 
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 90.5  ? 
11 NE2 ? A HIS 361 ? A HIS 346 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 N4 ? D A1H6T . ? A A1H6T 502 ? 1_555 168.5 ? 
12 NA  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 N4 ? D A1H6T . ? A A1H6T 502 ? 1_555 96.4  ? 
13 NB  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 N4 ? D A1H6T . ? A A1H6T 502 ? 1_555 80.1  ? 
14 NC  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 N4 ? D A1H6T . ? A A1H6T 502 ? 1_555 81.4  ? 
15 ND  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 N4 ? D A1H6T . ? A A1H6T 502 ? 1_555 99.7  ? 
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 89.5  ? 
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 88.1  ? 
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 91.0  ? 
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 89.7  ? 
20 NA  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 NC ? E HEM   . ? B HEM   501 ? 1_555 179.3 ? 
21 NB  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 NC ? E HEM   . ? B HEM   501 ? 1_555 89.0  ? 
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 87.2  ? 
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 89.4  ? 
24 NB  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 ND ? E HEM   . ? B HEM   501 ? 1_555 175.3 ? 
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 90.5  ? 
26 NE2 ? B HIS 361 ? B HIS 346 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 N4 ? F A1H6T . ? B A1H6T 502 ? 1_555 170.9 ? 
27 NA  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 N4 ? F A1H6T . ? B A1H6T 502 ? 1_555 97.8  ? 
28 NB  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 N4 ? F A1H6T . ? B A1H6T 502 ? 1_555 86.6  ? 
29 NC  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 N4 ? F A1H6T . ? B A1H6T 502 ? 1_555 82.9  ? 
30 ND  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 N4 ? F A1H6T . ? B A1H6T 502 ? 1_555 98.0  ? 
# 
_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                   9ESB 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 PRO A 6   ? ? -63.21  94.96  
2  1 ASN A 27  ? ? 33.17   71.41  
3  1 ASN A 133 ? ? -95.09  52.13  
4  1 LEU A 243 ? ? -143.34 57.35  
5  1 ILE A 354 ? ? -123.23 -60.42 
6  1 GLN A 360 ? ? -95.00  53.06  
7  1 THR A 382 ? ? -68.96  7.42   
8  1 ASN B 27  ? ? 32.72   71.41  
9  1 ASN B 133 ? ? -97.41  53.04  
10 1 LEU B 243 ? ? -143.54 57.25  
11 1 ILE B 354 ? ? -122.74 -60.05 
12 1 GLN B 360 ? ? -106.39 41.95  
# 
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 PRO 362 ? A PRO 377 
14 1 Y 1 A LYS 363 ? A LYS 378 
15 1 Y 1 A GLU 364 ? A GLU 379 
16 1 Y 1 A ASN 365 ? A ASN 380 
17 1 Y 1 A LYS 366 ? A LYS 381 
18 1 Y 1 A THR 367 ? A THR 382 
19 1 Y 1 A SER 368 ? A SER 383 
20 1 Y 1 A GLU 369 ? A GLU 384 
21 1 Y 1 A ASP 370 ? A ASP 385 
22 1 Y 1 A PRO 371 ? A PRO 386 
23 1 Y 1 A SER 372 ? A SER 387 
24 1 Y 1 A LYS 373 ? A LYS 388 
25 1 Y 1 A LEU 374 ? A LEU 389 
26 1 Y 1 A GLU 375 ? A GLU 390 
27 1 Y 1 A ALA 376 ? A ALA 391 
28 1 Y 1 A LYS 377 ? A LYS 392 
29 1 Y 1 A GLY 378 ? A GLY 393 
30 1 Y 1 A THR 379 ? A THR 394 
31 1 Y 1 A GLY 380 ? A GLY 395 
32 1 Y 1 A GLY 403 ? A GLY 418 
33 1 Y 1 B MET -14 ? B MET 1   
34 1 Y 1 B GLY -13 ? B GLY 2   
35 1 Y 1 B SER -12 ? B SER 3   
36 1 Y 1 B SER -11 ? B SER 4   
37 1 Y 1 B HIS -10 ? B HIS 5   
38 1 Y 1 B HIS -9  ? B HIS 6   
39 1 Y 1 B HIS -8  ? B HIS 7   
40 1 Y 1 B HIS -7  ? B HIS 8   
41 1 Y 1 B HIS -6  ? B HIS 9   
42 1 Y 1 B HIS -5  ? B HIS 10  
43 1 Y 1 B SER -4  ? B SER 11  
44 1 Y 1 B ALA -3  ? B ALA 12  
45 1 Y 1 B ALA -2  ? B ALA 13  
46 1 Y 1 B LEU -1  ? B LEU 14  
47 1 Y 1 B GLU 0   ? B GLU 15  
48 1 Y 1 B VAL 1   ? B VAL 16  
49 1 Y 1 B LEU 2   ? B LEU 17  
50 1 Y 1 B PHE 3   ? B PHE 18  
51 1 Y 1 B GLN 4   ? B GLN 19  
52 1 Y 1 B GLY 5   ? B GLY 20  
53 1 Y 1 B PRO 6   ? B PRO 21  
54 1 Y 1 B HIS 7   ? B HIS 22  
55 1 Y 1 B MET 8   ? B MET 23  
56 1 Y 1 B TRP 9   ? B TRP 24  
57 1 Y 1 B PRO 362 ? B PRO 377 
58 1 Y 1 B LYS 363 ? B LYS 378 
59 1 Y 1 B GLU 364 ? B GLU 379 
60 1 Y 1 B ASN 365 ? B ASN 380 
61 1 Y 1 B LYS 366 ? B LYS 381 
62 1 Y 1 B THR 367 ? B THR 382 
63 1 Y 1 B SER 368 ? B SER 383 
64 1 Y 1 B GLU 369 ? B GLU 384 
65 1 Y 1 B ASP 370 ? B ASP 385 
66 1 Y 1 B PRO 371 ? B PRO 386 
67 1 Y 1 B SER 372 ? B SER 387 
68 1 Y 1 B LYS 373 ? B LYS 388 
69 1 Y 1 B LEU 374 ? B LEU 389 
70 1 Y 1 B GLU 375 ? B GLU 390 
71 1 Y 1 B ALA 376 ? B ALA 391 
72 1 Y 1 B LYS 377 ? B LYS 392 
73 1 Y 1 B GLY 378 ? B GLY 393 
74 1 Y 1 B THR 379 ? B THR 394 
75 1 Y 1 B GLY 380 ? B GLY 395 
76 1 Y 1 B GLY 381 ? B GLY 396 
77 1 Y 1 B GLU 402 ? B GLU 417 
78 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 
A1H6T N1   N  Y N 1   
A1H6T N3   N  Y N 2   
A1H6T C4   C  N R 3   
A1H6T C5   C  Y N 4   
A1H6T C6   C  Y N 5   
A1H6T C7   C  Y N 6   
A1H6T C8   C  Y N 7   
A1H6T C10  C  Y N 8   
A1H6T C13  C  Y N 9   
A1H6T C15  C  Y N 10  
A1H6T CL   CL N N 11  
A1H6T C    C  Y N 12  
A1H6T C3   C  Y N 13  
A1H6T N4   N  Y N 14  
A1H6T C14  C  Y N 15  
A1H6T C2   C  Y N 16  
A1H6T C1   C  Y N 17  
A1H6T O    O  N N 18  
A1H6T N2   N  Y N 19  
A1H6T N    N  Y N 20  
A1H6T C12  C  Y N 21  
A1H6T C11  C  Y N 22  
A1H6T C9   C  Y N 23  
A1H6T H    H  N N 24  
A1H6T H3   H  N N 25  
A1H6T H4   H  N N 26  
A1H6T H6   H  N N 27  
A1H6T H11  H  N N 28  
A1H6T H10  H  N N 29  
A1H6T H2   H  N N 30  
A1H6T H1   H  N N 31  
A1H6T H9   H  N N 32  
A1H6T H8   H  N N 33  
A1H6T H7   H  N N 34  
A1H6T H5   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 
A1H6T C   CL   sing N N 1   
A1H6T C   C1   sing Y N 2   
A1H6T C1  C2   doub Y N 3   
A1H6T C3  C    doub Y N 4   
A1H6T C4  C3   sing N N 5   
A1H6T C5  C4   sing N N 6   
A1H6T C5  N    sing Y N 7   
A1H6T N   N1   doub Y N 8   
A1H6T C6  C5   doub Y N 9   
A1H6T N2  C6   sing Y N 10  
A1H6T N1  N2   sing Y N 11  
A1H6T C7  N2   sing N N 12  
A1H6T C7  C8   doub Y N 13  
A1H6T C8  C9   sing Y N 14  
A1H6T C9  C10  doub Y N 15  
A1H6T C10 C11  sing Y N 16  
A1H6T C11 C12  doub Y N 17  
A1H6T C12 C7   sing Y N 18  
A1H6T O   C4   sing N N 19  
A1H6T N3  C3   sing Y N 20  
A1H6T N3  C13  sing Y N 21  
A1H6T C2  C13  sing Y N 22  
A1H6T C13 C14  doub Y N 23  
A1H6T C14 N4   sing Y N 24  
A1H6T N4  C15  doub Y N 25  
A1H6T C15 N3   sing Y N 26  
A1H6T C4  H    sing N N 27  
A1H6T C6  H3   sing N N 28  
A1H6T C8  H4   sing N N 29  
A1H6T C10 H6   sing N N 30  
A1H6T C15 H11  sing N N 31  
A1H6T C14 H10  sing N N 32  
A1H6T C2  H2   sing N N 33  
A1H6T C1  H1   sing N N 34  
A1H6T O   H9   sing N N 35  
A1H6T C12 H8   sing N N 36  
A1H6T C11 H7   sing N N 37  
A1H6T C9  H5   sing N N 38  
ALA   N   CA   sing N N 39  
ALA   N   H    sing N N 40  
ALA   N   H2   sing N N 41  
ALA   CA  C    sing N N 42  
ALA   CA  CB   sing N N 43  
ALA   CA  HA   sing N N 44  
ALA   C   O    doub N N 45  
ALA   C   OXT  sing N N 46  
ALA   CB  HB1  sing N N 47  
ALA   CB  HB2  sing N N 48  
ALA   CB  HB3  sing N N 49  
ALA   OXT HXT  sing N N 50  
ARG   N   CA   sing N N 51  
ARG   N   H    sing N N 52  
ARG   N   H2   sing N N 53  
ARG   CA  C    sing N N 54  
ARG   CA  CB   sing N N 55  
ARG   CA  HA   sing N N 56  
ARG   C   O    doub N N 57  
ARG   C   OXT  sing N N 58  
ARG   CB  CG   sing N N 59  
ARG   CB  HB2  sing N N 60  
ARG   CB  HB3  sing N N 61  
ARG   CG  CD   sing N N 62  
ARG   CG  HG2  sing N N 63  
ARG   CG  HG3  sing N N 64  
ARG   CD  NE   sing N N 65  
ARG   CD  HD2  sing N N 66  
ARG   CD  HD3  sing N N 67  
ARG   NE  CZ   sing N N 68  
ARG   NE  HE   sing N N 69  
ARG   CZ  NH1  sing N N 70  
ARG   CZ  NH2  doub N N 71  
ARG   NH1 HH11 sing N N 72  
ARG   NH1 HH12 sing N N 73  
ARG   NH2 HH21 sing N N 74  
ARG   NH2 HH22 sing N N 75  
ARG   OXT HXT  sing N N 76  
ASN   N   CA   sing N N 77  
ASN   N   H    sing N N 78  
ASN   N   H2   sing N N 79  
ASN   CA  C    sing N N 80  
ASN   CA  CB   sing N N 81  
ASN   CA  HA   sing N N 82  
ASN   C   O    doub N N 83  
ASN   C   OXT  sing N N 84  
ASN   CB  CG   sing N N 85  
ASN   CB  HB2  sing N N 86  
ASN   CB  HB3  sing N N 87  
ASN   CG  OD1  doub N N 88  
ASN   CG  ND2  sing N N 89  
ASN   ND2 HD21 sing N N 90  
ASN   ND2 HD22 sing N N 91  
ASN   OXT HXT  sing N N 92  
ASP   N   CA   sing N N 93  
ASP   N   H    sing N N 94  
ASP   N   H2   sing N N 95  
ASP   CA  C    sing N N 96  
ASP   CA  CB   sing N N 97  
ASP   CA  HA   sing N N 98  
ASP   C   O    doub N N 99  
ASP   C   OXT  sing N N 100 
ASP   CB  CG   sing N N 101 
ASP   CB  HB2  sing N N 102 
ASP   CB  HB3  sing N N 103 
ASP   CG  OD1  doub N N 104 
ASP   CG  OD2  sing N N 105 
ASP   OD2 HD2  sing N N 106 
ASP   OXT HXT  sing N N 107 
CYS   N   CA   sing N N 108 
CYS   N   H    sing N N 109 
CYS   N   H2   sing N N 110 
CYS   CA  C    sing N N 111 
CYS   CA  CB   sing N N 112 
CYS   CA  HA   sing N N 113 
CYS   C   O    doub N N 114 
CYS   C   OXT  sing N N 115 
CYS   CB  SG   sing N N 116 
CYS   CB  HB2  sing N N 117 
CYS   CB  HB3  sing N N 118 
CYS   SG  HG   sing N N 119 
CYS   OXT HXT  sing N N 120 
GLN   N   CA   sing N N 121 
GLN   N   H    sing N N 122 
GLN   N   H2   sing N N 123 
GLN   CA  C    sing N N 124 
GLN   CA  CB   sing N N 125 
GLN   CA  HA   sing N N 126 
GLN   C   O    doub N N 127 
GLN   C   OXT  sing N N 128 
GLN   CB  CG   sing N N 129 
GLN   CB  HB2  sing N N 130 
GLN   CB  HB3  sing N N 131 
GLN   CG  CD   sing N N 132 
GLN   CG  HG2  sing N N 133 
GLN   CG  HG3  sing N N 134 
GLN   CD  OE1  doub N N 135 
GLN   CD  NE2  sing N N 136 
GLN   NE2 HE21 sing N N 137 
GLN   NE2 HE22 sing N N 138 
GLN   OXT HXT  sing N N 139 
GLU   N   CA   sing N N 140 
GLU   N   H    sing N N 141 
GLU   N   H2   sing N N 142 
GLU   CA  C    sing N N 143 
GLU   CA  CB   sing N N 144 
GLU   CA  HA   sing N N 145 
GLU   C   O    doub N N 146 
GLU   C   OXT  sing N N 147 
GLU   CB  CG   sing N N 148 
GLU   CB  HB2  sing N N 149 
GLU   CB  HB3  sing N N 150 
GLU   CG  CD   sing N N 151 
GLU   CG  HG2  sing N N 152 
GLU   CG  HG3  sing N N 153 
GLU   CD  OE1  doub N N 154 
GLU   CD  OE2  sing N N 155 
GLU   OE2 HE2  sing N N 156 
GLU   OXT HXT  sing N N 157 
GLY   N   CA   sing N N 158 
GLY   N   H    sing N N 159 
GLY   N   H2   sing N N 160 
GLY   CA  C    sing N N 161 
GLY   CA  HA2  sing N N 162 
GLY   CA  HA3  sing N N 163 
GLY   C   O    doub N N 164 
GLY   C   OXT  sing N N 165 
GLY   OXT HXT  sing N N 166 
HEM   CHA C1A  sing N N 167 
HEM   CHA C4D  doub N N 168 
HEM   CHA HHA  sing N N 169 
HEM   CHB C4A  sing N N 170 
HEM   CHB C1B  doub N N 171 
HEM   CHB HHB  sing N N 172 
HEM   CHC C4B  sing N N 173 
HEM   CHC C1C  doub N N 174 
HEM   CHC HHC  sing N N 175 
HEM   CHD C4C  doub N N 176 
HEM   CHD C1D  sing N N 177 
HEM   CHD HHD  sing N N 178 
HEM   C1A C2A  doub Y N 179 
HEM   C1A NA   sing Y N 180 
HEM   C2A C3A  sing Y N 181 
HEM   C2A CAA  sing N N 182 
HEM   C3A C4A  doub Y N 183 
HEM   C3A CMA  sing N N 184 
HEM   C4A NA   sing Y N 185 
HEM   CMA HMA  sing N N 186 
HEM   CMA HMAA sing N N 187 
HEM   CMA HMAB sing N N 188 
HEM   CAA CBA  sing N N 189 
HEM   CAA HAA  sing N N 190 
HEM   CAA HAAA sing N N 191 
HEM   CBA CGA  sing N N 192 
HEM   CBA HBA  sing N N 193 
HEM   CBA HBAA sing N N 194 
HEM   CGA O1A  doub N N 195 
HEM   CGA O2A  sing N N 196 
HEM   C1B C2B  sing N N 197 
HEM   C1B NB   sing N N 198 
HEM   C2B C3B  doub N N 199 
HEM   C2B CMB  sing N N 200 
HEM   C3B C4B  sing N N 201 
HEM   C3B CAB  sing N N 202 
HEM   C4B NB   doub N N 203 
HEM   CMB HMB  sing N N 204 
HEM   CMB HMBA sing N N 205 
HEM   CMB HMBB sing N N 206 
HEM   CAB CBB  doub N N 207 
HEM   CAB HAB  sing N N 208 
HEM   CBB HBB  sing N N 209 
HEM   CBB HBBA sing N N 210 
HEM   C1C C2C  sing Y N 211 
HEM   C1C NC   sing Y N 212 
HEM   C2C C3C  doub Y N 213 
HEM   C2C CMC  sing N N 214 
HEM   C3C C4C  sing Y N 215 
HEM   C3C CAC  sing N N 216 
HEM   C4C NC   sing Y N 217 
HEM   CMC HMC  sing N N 218 
HEM   CMC HMCA sing N N 219 
HEM   CMC HMCB sing N N 220 
HEM   CAC CBC  doub N N 221 
HEM   CAC HAC  sing N N 222 
HEM   CBC HBC  sing N N 223 
HEM   CBC HBCA sing N N 224 
HEM   C1D C2D  sing N N 225 
HEM   C1D ND   doub N N 226 
HEM   C2D C3D  doub N N 227 
HEM   C2D CMD  sing N N 228 
HEM   C3D C4D  sing N N 229 
HEM   C3D CAD  sing N N 230 
HEM   C4D ND   sing N N 231 
HEM   CMD HMD  sing N N 232 
HEM   CMD HMDA sing N N 233 
HEM   CMD HMDB sing N N 234 
HEM   CAD CBD  sing N N 235 
HEM   CAD HAD  sing N N 236 
HEM   CAD HADA sing N N 237 
HEM   CBD CGD  sing N N 238 
HEM   CBD HBD  sing N N 239 
HEM   CBD HBDA sing N N 240 
HEM   CGD O1D  doub N N 241 
HEM   CGD O2D  sing N N 242 
HEM   O2A H2A  sing N N 243 
HEM   O2D H2D  sing N N 244 
HEM   FE  NA   sing N N 245 
HEM   FE  NB   sing N N 246 
HEM   FE  NC   sing N N 247 
HEM   FE  ND   sing N N 248 
HIS   N   CA   sing N N 249 
HIS   N   H    sing N N 250 
HIS   N   H2   sing N N 251 
HIS   CA  C    sing N N 252 
HIS   CA  CB   sing N N 253 
HIS   CA  HA   sing N N 254 
HIS   C   O    doub N N 255 
HIS   C   OXT  sing N N 256 
HIS   CB  CG   sing N N 257 
HIS   CB  HB2  sing N N 258 
HIS   CB  HB3  sing N N 259 
HIS   CG  ND1  sing Y N 260 
HIS   CG  CD2  doub Y N 261 
HIS   ND1 CE1  doub Y N 262 
HIS   ND1 HD1  sing N N 263 
HIS   CD2 NE2  sing Y N 264 
HIS   CD2 HD2  sing N N 265 
HIS   CE1 NE2  sing Y N 266 
HIS   CE1 HE1  sing N N 267 
HIS   NE2 HE2  sing N N 268 
HIS   OXT HXT  sing N N 269 
HOH   O   H1   sing N N 270 
HOH   O   H2   sing N N 271 
ILE   N   CA   sing N N 272 
ILE   N   H    sing N N 273 
ILE   N   H2   sing N N 274 
ILE   CA  C    sing N N 275 
ILE   CA  CB   sing N N 276 
ILE   CA  HA   sing N N 277 
ILE   C   O    doub N N 278 
ILE   C   OXT  sing N N 279 
ILE   CB  CG1  sing N N 280 
ILE   CB  CG2  sing N N 281 
ILE   CB  HB   sing N N 282 
ILE   CG1 CD1  sing N N 283 
ILE   CG1 HG12 sing N N 284 
ILE   CG1 HG13 sing N N 285 
ILE   CG2 HG21 sing N N 286 
ILE   CG2 HG22 sing N N 287 
ILE   CG2 HG23 sing N N 288 
ILE   CD1 HD11 sing N N 289 
ILE   CD1 HD12 sing N N 290 
ILE   CD1 HD13 sing N N 291 
ILE   OXT HXT  sing N N 292 
LEU   N   CA   sing N N 293 
LEU   N   H    sing N N 294 
LEU   N   H2   sing N N 295 
LEU   CA  C    sing N N 296 
LEU   CA  CB   sing N N 297 
LEU   CA  HA   sing N N 298 
LEU   C   O    doub N N 299 
LEU   C   OXT  sing N N 300 
LEU   CB  CG   sing N N 301 
LEU   CB  HB2  sing N N 302 
LEU   CB  HB3  sing N N 303 
LEU   CG  CD1  sing N N 304 
LEU   CG  CD2  sing N N 305 
LEU   CG  HG   sing N N 306 
LEU   CD1 HD11 sing N N 307 
LEU   CD1 HD12 sing N N 308 
LEU   CD1 HD13 sing N N 309 
LEU   CD2 HD21 sing N N 310 
LEU   CD2 HD22 sing N N 311 
LEU   CD2 HD23 sing N N 312 
LEU   OXT HXT  sing N N 313 
LYS   N   CA   sing N N 314 
LYS   N   H    sing N N 315 
LYS   N   H2   sing N N 316 
LYS   CA  C    sing N N 317 
LYS   CA  CB   sing N N 318 
LYS   CA  HA   sing N N 319 
LYS   C   O    doub N N 320 
LYS   C   OXT  sing N N 321 
LYS   CB  CG   sing N N 322 
LYS   CB  HB2  sing N N 323 
LYS   CB  HB3  sing N N 324 
LYS   CG  CD   sing N N 325 
LYS   CG  HG2  sing N N 326 
LYS   CG  HG3  sing N N 327 
LYS   CD  CE   sing N N 328 
LYS   CD  HD2  sing N N 329 
LYS   CD  HD3  sing N N 330 
LYS   CE  NZ   sing N N 331 
LYS   CE  HE2  sing N N 332 
LYS   CE  HE3  sing N N 333 
LYS   NZ  HZ1  sing N N 334 
LYS   NZ  HZ2  sing N N 335 
LYS   NZ  HZ3  sing N N 336 
LYS   OXT HXT  sing N N 337 
MET   N   CA   sing N N 338 
MET   N   H    sing N N 339 
MET   N   H2   sing N N 340 
MET   CA  C    sing N N 341 
MET   CA  CB   sing N N 342 
MET   CA  HA   sing N N 343 
MET   C   O    doub N N 344 
MET   C   OXT  sing N N 345 
MET   CB  CG   sing N N 346 
MET   CB  HB2  sing N N 347 
MET   CB  HB3  sing N N 348 
MET   CG  SD   sing N N 349 
MET   CG  HG2  sing N N 350 
MET   CG  HG3  sing N N 351 
MET   SD  CE   sing N N 352 
MET   CE  HE1  sing N N 353 
MET   CE  HE2  sing N N 354 
MET   CE  HE3  sing N N 355 
MET   OXT HXT  sing N N 356 
PHE   N   CA   sing N N 357 
PHE   N   H    sing N N 358 
PHE   N   H2   sing N N 359 
PHE   CA  C    sing N N 360 
PHE   CA  CB   sing N N 361 
PHE   CA  HA   sing N N 362 
PHE   C   O    doub N N 363 
PHE   C   OXT  sing N N 364 
PHE   CB  CG   sing N N 365 
PHE   CB  HB2  sing N N 366 
PHE   CB  HB3  sing N N 367 
PHE   CG  CD1  doub Y N 368 
PHE   CG  CD2  sing Y N 369 
PHE   CD1 CE1  sing Y N 370 
PHE   CD1 HD1  sing N N 371 
PHE   CD2 CE2  doub Y N 372 
PHE   CD2 HD2  sing N N 373 
PHE   CE1 CZ   doub Y N 374 
PHE   CE1 HE1  sing N N 375 
PHE   CE2 CZ   sing Y N 376 
PHE   CE2 HE2  sing N N 377 
PHE   CZ  HZ   sing N N 378 
PHE   OXT HXT  sing N N 379 
PRO   N   CA   sing N N 380 
PRO   N   CD   sing N N 381 
PRO   N   H    sing N N 382 
PRO   CA  C    sing N N 383 
PRO   CA  CB   sing N N 384 
PRO   CA  HA   sing N N 385 
PRO   C   O    doub N N 386 
PRO   C   OXT  sing N N 387 
PRO   CB  CG   sing N N 388 
PRO   CB  HB2  sing N N 389 
PRO   CB  HB3  sing N N 390 
PRO   CG  CD   sing N N 391 
PRO   CG  HG2  sing N N 392 
PRO   CG  HG3  sing N N 393 
PRO   CD  HD2  sing N N 394 
PRO   CD  HD3  sing N N 395 
PRO   OXT HXT  sing N N 396 
SER   N   CA   sing N N 397 
SER   N   H    sing N N 398 
SER   N   H2   sing N N 399 
SER   CA  C    sing N N 400 
SER   CA  CB   sing N N 401 
SER   CA  HA   sing N N 402 
SER   C   O    doub N N 403 
SER   C   OXT  sing N N 404 
SER   CB  OG   sing N N 405 
SER   CB  HB2  sing N N 406 
SER   CB  HB3  sing N N 407 
SER   OG  HG   sing N N 408 
SER   OXT HXT  sing N N 409 
THR   N   CA   sing N N 410 
THR   N   H    sing N N 411 
THR   N   H2   sing N N 412 
THR   CA  C    sing N N 413 
THR   CA  CB   sing N N 414 
THR   CA  HA   sing N N 415 
THR   C   O    doub N N 416 
THR   C   OXT  sing N N 417 
THR   CB  OG1  sing N N 418 
THR   CB  CG2  sing N N 419 
THR   CB  HB   sing N N 420 
THR   OG1 HG1  sing N N 421 
THR   CG2 HG21 sing N N 422 
THR   CG2 HG22 sing N N 423 
THR   CG2 HG23 sing N N 424 
THR   OXT HXT  sing N N 425 
TRP   N   CA   sing N N 426 
TRP   N   H    sing N N 427 
TRP   N   H2   sing N N 428 
TRP   CA  C    sing N N 429 
TRP   CA  CB   sing N N 430 
TRP   CA  HA   sing N N 431 
TRP   C   O    doub N N 432 
TRP   C   OXT  sing N N 433 
TRP   CB  CG   sing N N 434 
TRP   CB  HB2  sing N N 435 
TRP   CB  HB3  sing N N 436 
TRP   CG  CD1  doub Y N 437 
TRP   CG  CD2  sing Y N 438 
TRP   CD1 NE1  sing Y N 439 
TRP   CD1 HD1  sing N N 440 
TRP   CD2 CE2  doub Y N 441 
TRP   CD2 CE3  sing Y N 442 
TRP   NE1 CE2  sing Y N 443 
TRP   NE1 HE1  sing N N 444 
TRP   CE2 CZ2  sing Y N 445 
TRP   CE3 CZ3  doub Y N 446 
TRP   CE3 HE3  sing N N 447 
TRP   CZ2 CH2  doub Y N 448 
TRP   CZ2 HZ2  sing N N 449 
TRP   CZ3 CH2  sing Y N 450 
TRP   CZ3 HZ3  sing N N 451 
TRP   CH2 HH2  sing N N 452 
TRP   OXT HXT  sing N N 453 
TYR   N   CA   sing N N 454 
TYR   N   H    sing N N 455 
TYR   N   H2   sing N N 456 
TYR   CA  C    sing N N 457 
TYR   CA  CB   sing N N 458 
TYR   CA  HA   sing N N 459 
TYR   C   O    doub N N 460 
TYR   C   OXT  sing N N 461 
TYR   CB  CG   sing N N 462 
TYR   CB  HB2  sing N N 463 
TYR   CB  HB3  sing N N 464 
TYR   CG  CD1  doub Y N 465 
TYR   CG  CD2  sing Y N 466 
TYR   CD1 CE1  sing Y N 467 
TYR   CD1 HD1  sing N N 468 
TYR   CD2 CE2  doub Y N 469 
TYR   CD2 HD2  sing N N 470 
TYR   CE1 CZ   doub Y N 471 
TYR   CE1 HE1  sing N N 472 
TYR   CE2 CZ   sing Y N 473 
TYR   CE2 HE2  sing N N 474 
TYR   CZ  OH   sing N N 475 
TYR   OH  HH   sing N N 476 
TYR   OXT HXT  sing N N 477 
VAL   N   CA   sing N N 478 
VAL   N   H    sing N N 479 
VAL   N   H2   sing N N 480 
VAL   CA  C    sing N N 481 
VAL   CA  CB   sing N N 482 
VAL   CA  HA   sing N N 483 
VAL   C   O    doub N N 484 
VAL   C   OXT  sing N N 485 
VAL   CB  CG1  sing N N 486 
VAL   CB  CG2  sing N N 487 
VAL   CB  HB   sing N N 488 
VAL   CG1 HG11 sing N N 489 
VAL   CG1 HG12 sing N N 490 
VAL   CG1 HG13 sing N N 491 
VAL   CG2 HG21 sing N N 492 
VAL   CG2 HG22 sing N N 493 
VAL   CG2 HG23 sing N N 494 
VAL   OXT HXT  sing N N 495 
# 
_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                    9ESB 
_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]   0.011870 
_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]   0.010854 
_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]   0.007557 
_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  
CL 
FE 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ALA   A 1 13  ? 14.395  -21.177 -1.749  1 64.66 ? -2  ALA   A N   1 
ATOM   2    C  CA  . ALA   A 1 13  ? 14.639  -19.922 -2.47   1 65    ? -2  ALA   A CA  1 
ATOM   3    C  C   . ALA   A 1 13  ? 14.989  -18.782 -1.519  1 65.57 ? -2  ALA   A C   1 
ATOM   4    O  O   . ALA   A 1 13  ? 15.774  -17.905 -1.881  1 65.81 ? -2  ALA   A O   1 
ATOM   5    C  CB  . ALA   A 1 13  ? 13.441  -19.546 -3.325  1 64.86 ? -2  ALA   A CB  1 
ATOM   6    N  N   . LEU   A 1 14  ? 14.434  -18.794 -0.302  1 65.52 ? -1  LEU   A N   1 
ATOM   7    C  CA  . LEU   A 1 14  ? 14.755  -17.766 0.686   1 66.24 ? -1  LEU   A CA  1 
ATOM   8    C  C   . LEU   A 1 14  ? 16.153  -18.046 1.295   1 66.68 ? -1  LEU   A C   1 
ATOM   9    O  O   . LEU   A 1 14  ? 16.935  -17.114 1.502   1 66.82 ? -1  LEU   A O   1 
ATOM   10   C  CB  . LEU   A 1 14  ? 13.657  -17.711 1.768   1 66.62 ? -1  LEU   A CB  1 
ATOM   11   C  CG  . LEU   A 1 14  ? 13.701  -16.584 2.819   1 68.2  ? -1  LEU   A CG  1 
ATOM   12   C  CD1 . LEU   A 1 14  ? 13.979  -15.227 2.193   1 68.73 ? -1  LEU   A CD1 1 
ATOM   13   C  CD2 . LEU   A 1 14  ? 12.389  -16.523 3.59    1 68.82 ? -1  LEU   A CD2 1 
ATOM   14   N  N   . GLU   A 1 15  ? 16.477  -19.34  1.526   1 66.28 ? 0   GLU   A N   1 
ATOM   15   C  CA  . GLU   A 1 15  ? 17.77   -19.764 2.071   1 65.88 ? 0   GLU   A CA  1 
ATOM   16   C  C   . GLU   A 1 15  ? 18.906  -19.619 1.044   1 64.49 ? 0   GLU   A C   1 
ATOM   17   O  O   . GLU   A 1 15  ? 20.056  -19.455 1.436   1 64.25 ? 0   GLU   A O   1 
ATOM   18   C  CB  . GLU   A 1 15  ? 17.697  -21.207 2.613   1 68.51 ? 0   GLU   A CB  1 
ATOM   19   N  N   . VAL   A 1 16  ? 18.592  -19.675 -0.257  1 63.37 ? 1   VAL   A N   1 
ATOM   20   C  CA  . VAL   A 1 16  ? 19.598  -19.479 -1.299  1 63.09 ? 1   VAL   A CA  1 
ATOM   21   C  C   . VAL   A 1 16  ? 20.076  -17.988 -1.306  1 63.3  ? 1   VAL   A C   1 
ATOM   22   O  O   . VAL   A 1 16  ? 21.231  -17.712 -1.617  1 63.27 ? 1   VAL   A O   1 
ATOM   23   C  CB  . VAL   A 1 16  ? 19.087  -19.995 -2.676  1 63.4  ? 1   VAL   A CB  1 
ATOM   24   C  CG1 . VAL   A 1 16  ? 19.953  -19.506 -3.829  1 63.91 ? 1   VAL   A CG1 1 
ATOM   25   C  CG2 . VAL   A 1 16  ? 18.995  -21.518 -2.688  1 63.46 ? 1   VAL   A CG2 1 
ATOM   26   N  N   . LEU   A 1 17  ? 19.218  -17.044 -0.87   1 63.4  ? 2   LEU   A N   1 
ATOM   27   C  CA  . LEU   A 1 17  ? 19.587  -15.637 -0.777  1 64.04 ? 2   LEU   A CA  1 
ATOM   28   C  C   . LEU   A 1 17  ? 20.646  -15.429 0.307   1 64.93 ? 2   LEU   A C   1 
ATOM   29   O  O   . LEU   A 1 17  ? 21.65   -14.767 0.048   1 65.07 ? 2   LEU   A O   1 
ATOM   30   C  CB  . LEU   A 1 17  ? 18.356  -14.765 -0.471  1 63.9  ? 2   LEU   A CB  1 
ATOM   31   C  CG  . LEU   A 1 17  ? 17.57   -14.27  -1.667  1 64.61 ? 2   LEU   A CG  1 
ATOM   32   C  CD1 . LEU   A 1 17  ? 16.33   -13.57  -1.219  1 65.17 ? 2   LEU   A CD1 1 
ATOM   33   C  CD2 . LEU   A 1 17  ? 18.421  -13.368 -2.561  1 64.59 ? 2   LEU   A CD2 1 
ATOM   34   N  N   . PHE   A 1 18  ? 20.442  -16.028 1.499   1 65.21 ? 3   PHE   A N   1 
ATOM   35   C  CA  . PHE   A 1 18  ? 21.346  -15.899 2.652   1 66.01 ? 3   PHE   A CA  1 
ATOM   36   C  C   . PHE   A 1 18  ? 22.582  -16.81  2.633   1 66.33 ? 3   PHE   A C   1 
ATOM   37   O  O   . PHE   A 1 18  ? 23.661  -16.38  3.034   1 66.71 ? 3   PHE   A O   1 
ATOM   38   C  CB  . PHE   A 1 18  ? 20.581  -16.173 3.961   1 66.27 ? 3   PHE   A CB  1 
ATOM   39   C  CG  . PHE   A 1 18  ? 19.287  -15.425 4.112   1 67.23 ? 3   PHE   A CG  1 
ATOM   40   C  CD1 . PHE   A 1 18  ? 19.27   -14.05  4.169   1 68    ? 3   PHE   A CD1 1 
ATOM   41   C  CD2 . PHE   A 1 18  ? 18.093  -16.101 4.253   1 68.38 ? 3   PHE   A CD2 1 
ATOM   42   C  CE1 . PHE   A 1 18  ? 18.083  -13.365 4.337   1 68.75 ? 3   PHE   A CE1 1 
ATOM   43   C  CE2 . PHE   A 1 18  ? 16.9    -15.408 4.4     1 69.11 ? 3   PHE   A CE2 1 
ATOM   44   C  CZ  . PHE   A 1 18  ? 16.903  -14.043 4.432   1 68.66 ? 3   PHE   A CZ  1 
ATOM   45   N  N   . GLN   A 1 19  ? 22.409  -18.089 2.293   1 66.15 ? 4   GLN   A N   1 
ATOM   46   C  CA  . GLN   A 1 19  ? 23.506  -19.056 2.321   1 66.61 ? 4   GLN   A CA  1 
ATOM   47   C  C   . GLN   A 1 19  ? 24.261  -19.163 0.999   1 67.17 ? 4   GLN   A C   1 
ATOM   48   O  O   . GLN   A 1 19  ? 25.45   -19.49  0.99    1 67.29 ? 4   GLN   A O   1 
ATOM   49   C  CB  . GLN   A 1 19  ? 23.002  -20.437 2.78    1 67.8  ? 4   GLN   A CB  1 
ATOM   50   N  N   . GLY   A 1 20  ? 23.576  -18.872 -0.1    1 67.26 ? 5   GLY   A N   1 
ATOM   51   C  CA  . GLY   A 1 20  ? 24.169  -18.913 -1.426  1 67.77 ? 5   GLY   A CA  1 
ATOM   52   C  C   . GLY   A 1 20  ? 23.617  -20.037 -2.272  1 68.35 ? 5   GLY   A C   1 
ATOM   53   O  O   . GLY   A 1 20  ? 22.907  -20.918 -1.768  1 68.38 ? 5   GLY   A O   1 
ATOM   54   N  N   . PRO   A 1 21  ? 23.953  -20.008 -3.578  1 68.52 ? 6   PRO   A N   1 
ATOM   55   C  CA  . PRO   A 1 21  ? 23.475  -21.066 -4.491  1 68.79 ? 6   PRO   A CA  1 
ATOM   56   C  C   . PRO   A 1 21  ? 23.993  -22.464 -4.15   1 69.53 ? 6   PRO   A C   1 
ATOM   57   O  O   . PRO   A 1 21  ? 25.087  -22.843 -4.567  1 70.07 ? 6   PRO   A O   1 
ATOM   58   C  CB  . PRO   A 1 21  ? 23.973  -20.61  -5.866  1 69.36 ? 6   PRO   A CB  1 
ATOM   59   C  CG  . PRO   A 1 21  ? 25.033  -19.601 -5.61   1 69.67 ? 6   PRO   A CG  1 
ATOM   60   C  CD  . PRO   A 1 21  ? 24.773  -18.994 -4.271  1 68.01 ? 6   PRO   A CD  1 
ATOM   61   N  N   . HIS   A 1 22  ? 23.204  -23.237 -3.394  1 69.37 ? 7   HIS   A N   1 
ATOM   62   C  CA  . HIS   A 1 22  ? 23.6    -24.571 -2.974  1 69.78 ? 7   HIS   A CA  1 
ATOM   63   C  C   . HIS   A 1 22  ? 22.436  -25.516 -3.173  1 70.01 ? 7   HIS   A C   1 
ATOM   64   O  O   . HIS   A 1 22  ? 21.584  -25.657 -2.3    1 70.53 ? 7   HIS   A O   1 
ATOM   65   C  CB  . HIS   A 1 22  ? 24.064  -24.555 -1.507  1 70.73 ? 7   HIS   A CB  1 
ATOM   66   N  N   . MET   A 1 23  ? 22.385  -26.153 -4.333  1 69.85 ? 8   MET   A N   1 
ATOM   67   C  CA  . MET   A 1 23  ? 21.296  -27.064 -4.667  1 70.04 ? 8   MET   A CA  1 
ATOM   68   C  C   . MET   A 1 23  ? 21.516  -28.509 -4.199  1 70.09 ? 8   MET   A C   1 
ATOM   69   O  O   . MET   A 1 23  ? 21.624  -29.431 -5.018  1 69.95 ? 8   MET   A O   1 
ATOM   70   C  CB  . MET   A 1 23  ? 20.986  -27.017 -6.164  1 70.54 ? 8   MET   A CB  1 
ATOM   71   C  CG  . MET   A 1 23  ? 19.582  -27.417 -6.469  1 73.08 ? 8   MET   A CG  1 
ATOM   72   S  SD  . MET   A 1 23  ? 19.428  -27.732 -8.216  1 78.2  ? 8   MET   A SD  1 
ATOM   73   C  CE  . MET   A 1 23  ? 19.154  -26.098 -8.783  1 76.6  ? 8   MET   A CE  1 
ATOM   74   N  N   . TRP   A 1 24  ? 21.531  -28.71  -2.87   1 70.03 ? 9   TRP   A N   1 
ATOM   75   C  CA  . TRP   A 1 24  ? 21.662  -30.048 -2.271  1 69.99 ? 9   TRP   A CA  1 
ATOM   76   C  C   . TRP   A 1 24  ? 20.315  -30.825 -2.25   1 67.77 ? 9   TRP   A C   1 
ATOM   77   O  O   . TRP   A 1 24  ? 20.279  -31.982 -1.839  1 67.53 ? 9   TRP   A O   1 
ATOM   78   C  CB  . TRP   A 1 24  ? 22.31   -29.982 -0.87   1 71.04 ? 9   TRP   A CB  1 
ATOM   79   C  CG  . TRP   A 1 24  ? 23.543  -29.118 -0.788  1 72.99 ? 9   TRP   A CG  1 
ATOM   80   C  CD1 . TRP   A 1 24  ? 24.413  -28.815 -1.798  1 74.15 ? 9   TRP   A CD1 1 
ATOM   81   C  CD2 . TRP   A 1 24  ? 24.057  -28.476 0.39    1 74.02 ? 9   TRP   A CD2 1 
ATOM   82   N  NE1 . TRP   A 1 24  ? 25.412  -27.988 -1.332  1 74.76 ? 9   TRP   A NE1 1 
ATOM   83   C  CE2 . TRP   A 1 24  ? 25.221  -27.77  0.01    1 74.87 ? 9   TRP   A CE2 1 
ATOM   84   C  CE3 . TRP   A 1 24  ? 23.643  -28.424 1.731   1 74.81 ? 9   TRP   A CE3 1 
ATOM   85   C  CZ2 . TRP   A 1 24  ? 25.972  -27.024 0.922   1 75.7  ? 9   TRP   A CZ2 1 
ATOM   86   C  CZ3 . TRP   A 1 24  ? 24.387  -27.683 2.632   1 75.68 ? 9   TRP   A CZ3 1 
ATOM   87   C  CH2 . TRP   A 1 24  ? 25.531  -26.989 2.226   1 75.83 ? 9   TRP   A CH2 1 
ATOM   88   N  N   . THR   A 1 25  ? 19.223  -30.192 -2.736  1 65.91 ? 10  THR   A N   1 
ATOM   89   C  CA  . THR   A 1 25  ? 17.902  -30.786 -2.863  1 64.36 ? 10  THR   A CA  1 
ATOM   90   C  C   . THR   A 1 25  ? 17.119  -30.156 -4.045  1 62.14 ? 10  THR   A C   1 
ATOM   91   O  O   . THR   A 1 25  ? 17.292  -28.966 -4.348  1 62.11 ? 10  THR   A O   1 
ATOM   92   C  CB  . THR   A 1 25  ? 17.136  -30.636 -1.535  1 65.8  ? 10  THR   A CB  1 
ATOM   93   O  OG1 . THR   A 1 25  ? 15.832  -31.195 -1.682  1 67.29 ? 10  THR   A OG1 1 
ATOM   94   C  CG2 . THR   A 1 25  ? 17.013  -29.184 -1.092  1 66.05 ? 10  THR   A CG2 1 
ATOM   95   N  N   . ILE   A 1 26  ? 16.266  -30.957 -4.722  1 60.07 ? 11  ILE   A N   1 
ATOM   96   C  CA  . ILE   A 1 26  ? 15.398  -30.397 -5.759  1 58.35 ? 11  ILE   A CA  1 
ATOM   97   C  C   . ILE   A 1 26  ? 14.062  -29.97  -5.148  1 56.04 ? 11  ILE   A C   1 
ATOM   98   O  O   . ILE   A 1 26  ? 13.158  -30.782 -4.895  1 55.36 ? 11  ILE   A O   1 
ATOM   99   C  CB  . ILE   A 1 26  ? 15.196  -31.197 -7.063  1 58.47 ? 11  ILE   A CB  1 
ATOM   100  C  CG1 . ILE   A 1 26  ? 16.555  -31.545 -7.68   1 59.28 ? 11  ILE   A CG1 1 
ATOM   101  C  CG2 . ILE   A 1 26  ? 14.315  -30.344 -8.02   1 58.38 ? 11  ILE   A CG2 1 
ATOM   102  C  CD1 . ILE   A 1 26  ? 16.497  -32.265 -8.898  1 60.22 ? 11  ILE   A CD1 1 
ATOM   103  N  N   . SER   A 1 27  ? 13.967  -28.675 -4.912  1 54.6  ? 12  SER   A N   1 
ATOM   104  C  CA  . SER   A 1 27  ? 12.807  -28.014 -4.355  1 53.71 ? 12  SER   A CA  1 
ATOM   105  C  C   . SER   A 1 27  ? 11.554  -28.254 -5.202  1 52.84 ? 12  SER   A C   1 
ATOM   106  O  O   . SER   A 1 27  ? 11.612  -28.225 -6.441  1 51.85 ? 12  SER   A O   1 
ATOM   107  C  CB  . SER   A 1 27  ? 13.079  -26.521 -4.269  1 54.62 ? 12  SER   A CB  1 
ATOM   108  O  OG  . SER   A 1 27  ? 11.957  -25.847 -3.733  1 57.31 ? 12  SER   A OG  1 
ATOM   109  N  N   . LYS   A 1 28  ? 10.416  -28.467 -4.522  1 52.51 ? 13  LYS   A N   1 
ATOM   110  C  CA  . LYS   A 1 28  ? 9.131   -28.659 -5.182  1 52.74 ? 13  LYS   A CA  1 
ATOM   111  C  C   . LYS   A 1 28  ? 8.696   -27.41  -5.983  1 52.33 ? 13  LYS   A C   1 
ATOM   112  O  O   . LYS   A 1 28  ? 7.889   -27.532 -6.901  1 52.39 ? 13  LYS   A O   1 
ATOM   113  C  CB  . LYS   A 1 28  ? 8.059   -29.075 -4.169  1 55.17 ? 13  LYS   A CB  1 
ATOM   114  N  N   . GLU   A 1 29  ? 9.271   -26.232 -5.671  1 51.71 ? 14  GLU   A N   1 
ATOM   115  C  CA  . GLU   A 1 29  ? 9.039   -24.971 -6.37   1 52.03 ? 14  GLU   A CA  1 
ATOM   116  C  C   . GLU   A 1 29  ? 9.592   -24.974 -7.805  1 50.81 ? 14  GLU   A C   1 
ATOM   117  O  O   . GLU   A 1 29  ? 9.257   -24.086 -8.578  1 50.75 ? 14  GLU   A O   1 
ATOM   118  C  CB  . GLU   A 1 29  ? 9.67    -23.812 -5.585  1 56.51 ? 14  GLU   A CB  1 
ATOM   119  C  CG  . GLU   A 1 29  ? 9.223   -23.737 -4.135  1 65.54 ? 14  GLU   A CG  1 
ATOM   120  C  CD  . GLU   A 1 29  ? 9.82    -22.554 -3.4    1 78.43 ? 14  GLU   A CD  1 
ATOM   121  O  OE1 . GLU   A 1 29  ? 9.831   -21.444 -3.983  1 81.9  ? 14  GLU   A OE1 1 
ATOM   122  O  OE2 . GLU   A 1 29  ? 10.288  -22.736 -2.25   1 82.19 ? 14  GLU   A OE2 1 
ATOM   123  N  N   . TYR   A 1 30  ? 10.46   -25.929 -8.154  1 49.83 ? 15  TYR   A N   1 
ATOM   124  C  CA  . TYR   A 1 30  ? 10.975  -26.047 -9.514  1 49.27 ? 15  TYR   A CA  1 
ATOM   125  C  C   . TYR   A 1 30  ? 10.002  -26.823 -10.438 1 50.47 ? 15  TYR   A C   1 
ATOM   126  O  O   . TYR   A 1 30  ? 10.213  -26.839 -11.646 1 51.36 ? 15  TYR   A O   1 
ATOM   127  C  CB  . TYR   A 1 30  ? 12.38   -26.671 -9.536  1 47.75 ? 15  TYR   A CB  1 
ATOM   128  C  CG  . TYR   A 1 30  ? 13.453  -25.773 -8.955  1 46.79 ? 15  TYR   A CG  1 
ATOM   129  C  CD1 . TYR   A 1 30  ? 13.685  -24.507 -9.473  1 46.67 ? 15  TYR   A CD1 1 
ATOM   130  C  CD2 . TYR   A 1 30  ? 14.252  -26.202 -7.906  1 47.08 ? 15  TYR   A CD2 1 
ATOM   131  C  CE1 . TYR   A 1 30  ? 14.674  -23.684 -8.952  1 47.08 ? 15  TYR   A CE1 1 
ATOM   132  C  CE2 . TYR   A 1 30  ? 15.246  -25.385 -7.372  1 47.54 ? 15  TYR   A CE2 1 
ATOM   133  C  CZ  . TYR   A 1 30  ? 15.463  -24.131 -7.907  1 48.25 ? 15  TYR   A CZ  1 
ATOM   134  O  OH  . TYR   A 1 30  ? 16.461  -23.335 -7.391  1 49.44 ? 15  TYR   A OH  1 
ATOM   135  N  N   . HIS   A 1 31  ? 8.966   -27.471 -9.88   1 50.47 ? 16  HIS   A N   1 
ATOM   136  C  CA  . HIS   A 1 31  ? 7.938   -28.206 -10.617 1 51.2  ? 16  HIS   A CA  1 
ATOM   137  C  C   . HIS   A 1 31  ? 8.519   -29.278 -11.528 1 50.95 ? 16  HIS   A C   1 
ATOM   138  O  O   . HIS   A 1 31  ? 8.155   -29.412 -12.7   1 50.61 ? 16  HIS   A O   1 
ATOM   139  C  CB  . HIS   A 1 31  ? 6.977   -27.253 -11.352 1 53.06 ? 16  HIS   A CB  1 
ATOM   140  C  CG  . HIS   A 1 31  ? 6.188   -26.434 -10.377 1 57.48 ? 16  HIS   A CG  1 
ATOM   141  N  ND1 . HIS   A 1 31  ? 6.33    -25.059 -10.299 1 60.24 ? 16  HIS   A ND1 1 
ATOM   142  C  CD2 . HIS   A 1 31  ? 5.353   -26.843 -9.389  1 59.22 ? 16  HIS   A CD2 1 
ATOM   143  C  CE1 . HIS   A 1 31  ? 5.554   -24.673 -9.296  1 61.04 ? 16  HIS   A CE1 1 
ATOM   144  N  NE2 . HIS   A 1 31  ? 4.936   -25.712 -8.723  1 60.86 ? 16  HIS   A NE2 1 
ATOM   145  N  N   . ILE   A 1 32  ? 9.426   -30.051 -10.96  1 50.68 ? 17  ILE   A N   1 
ATOM   146  C  CA  . ILE   A 1 32  ? 10.011  -31.199 -11.622 1 50.75 ? 17  ILE   A CA  1 
ATOM   147  C  C   . ILE   A 1 32  ? 9.388   -32.395 -10.926 1 51.61 ? 17  ILE   A C   1 
ATOM   148  O  O   . ILE   A 1 32  ? 9.429   -32.499 -9.698  1 52.22 ? 17  ILE   A O   1 
ATOM   149  C  CB  . ILE   A 1 32  ? 11.55   -31.205 -11.511 1 50.45 ? 17  ILE   A CB  1 
ATOM   150  C  CG1 . ILE   A 1 32  ? 12.147  -29.882 -12.056 1 50.87 ? 17  ILE   A CG1 1 
ATOM   151  C  CG2 . ILE   A 1 32  ? 12.126  -32.432 -12.213 1 50.55 ? 17  ILE   A CG2 1 
ATOM   152  C  CD1 . ILE   A 1 32  ? 13.637  -29.728 -11.835 1 51.5  ? 17  ILE   A CD1 1 
ATOM   153  N  N   . ASP   A 1 33  ? 8.737   -33.252 -11.69  1 51.63 ? 18  ASP   A N   1 
ATOM   154  C  CA  . ASP   A 1 33  ? 8.07    -34.421 -11.162 1 51.88 ? 18  ASP   A CA  1 
ATOM   155  C  C   . ASP   A 1 33  ? 9.051   -35.585 -11.037 1 52.02 ? 18  ASP   A C   1 
ATOM   156  O  O   . ASP   A 1 33  ? 9.919   -35.763 -11.89  1 51.95 ? 18  ASP   A O   1 
ATOM   157  C  CB  . ASP   A 1 33  ? 6.882   -34.794 -12.059 1 53.21 ? 18  ASP   A CB  1 
ATOM   158  C  CG  . ASP   A 1 33  ? 6.006   -35.869 -11.453 1 57.65 ? 18  ASP   A CG  1 
ATOM   159  O  OD1 . ASP   A 1 33  ? 5.247   -35.552 -10.506 1 58.97 ? 18  ASP   A OD1 1 
ATOM   160  O  OD2 . ASP   A 1 33  ? 6.095   -37.035 -11.907 1 59.09 ? 18  ASP   A OD2 1 
ATOM   161  N  N   . GLU   A 1 34  ? 8.906   -36.385 -9.98   1 52.02 ? 19  GLU   A N   1 
ATOM   162  C  CA  . GLU   A 1 34  ? 9.777   -37.532 -9.746  1 52.27 ? 19  GLU   A CA  1 
ATOM   163  C  C   . GLU   A 1 34  ? 9.669   -38.571 -10.865 1 51.96 ? 19  GLU   A C   1 
ATOM   164  O  O   . GLU   A 1 34  ? 10.654  -39.229 -11.184 1 52.1  ? 19  GLU   A O   1 
ATOM   165  C  CB  . GLU   A 1 34  ? 9.457   -38.166 -8.382  1 54.54 ? 19  GLU   A CB  1 
ATOM   166  N  N   . GLU   A 1 35  ? 8.488   -38.704 -11.476 1 51.35 ? 20  GLU   A N   1 
ATOM   167  C  CA  . GLU   A 1 35  ? 8.283   -39.683 -12.536 1 51.04 ? 20  GLU   A CA  1 
ATOM   168  C  C   . GLU   A 1 35  ? 8.462   -39.128 -13.954 1 49.6  ? 20  GLU   A C   1 
ATOM   169  O  O   . GLU   A 1 35  ? 9.118   -39.773 -14.769 1 50.1  ? 20  GLU   A O   1 
ATOM   170  C  CB  . GLU   A 1 35  ? 6.894   -40.333 -12.392 1 54.17 ? 20  GLU   A CB  1 
ATOM   171  C  CG  . GLU   A 1 35  ? 6.64    -41.458 -13.382 1 60.92 ? 20  GLU   A CG  1 
ATOM   172  C  CD  . GLU   A 1 35  ? 5.231   -42.021 -13.354 1 69.5  ? 20  GLU   A CD  1 
ATOM   173  O  OE1 . GLU   A 1 35  ? 5.06    -43.209 -13.717 1 72.74 ? 20  GLU   A OE1 1 
ATOM   174  O  OE2 . GLU   A 1 35  ? 4.299   -41.273 -12.974 1 69.96 ? 20  GLU   A OE2 1 
ATOM   175  N  N   . VAL   A 1 36  ? 7.849   -37.971 -14.271 1 47.9  ? 21  VAL   A N   1 
ATOM   176  C  CA  . VAL   A 1 36  ? 7.89    -37.445 -15.64  1 46.52 ? 21  VAL   A CA  1 
ATOM   177  C  C   . VAL   A 1 36  ? 8.823   -36.244 -15.858 1 46.17 ? 21  VAL   A C   1 
ATOM   178  O  O   . VAL   A 1 36  ? 8.875   -35.733 -16.973 1 46.36 ? 21  VAL   A O   1 
ATOM   179  C  CB  . VAL   A 1 36  ? 6.476   -37.133 -16.173 1 45.96 ? 21  VAL   A CB  1 
ATOM   180  C  CG1 . VAL   A 1 36  ? 5.613   -38.375 -16.175 1 46.33 ? 21  VAL   A CG1 1 
ATOM   181  C  CG2 . VAL   A 1 36  ? 5.817   -36.024 -15.38  1 45.79 ? 21  VAL   A CG2 1 
ATOM   182  N  N   . GLY   A 1 37  ? 9.563   -35.836 -14.829 1 45.5  ? 22  GLY   A N   1 
ATOM   183  C  CA  . GLY   A 1 37  ? 10.523  -34.738 -14.908 1 44.8  ? 22  GLY   A CA  1 
ATOM   184  C  C   . GLY   A 1 37  ? 9.921   -33.392 -15.211 1 43.97 ? 22  GLY   A C   1 
ATOM   185  O  O   . GLY   A 1 37  ? 9.058   -32.919 -14.478 1 43.47 ? 22  GLY   A O   1 
ATOM   186  N  N   . PHE   A 1 38  ? 10.371  -32.763 -16.306 1 43.55 ? 23  PHE   A N   1 
ATOM   187  C  CA  . PHE   A 1 38  ? 9.867   -31.461 -16.722 1 42.82 ? 23  PHE   A CA  1 
ATOM   188  C  C   . PHE   A 1 38  ? 8.474   -31.527 -17.356 1 42.12 ? 23  PHE   A C   1 
ATOM   189  O  O   . PHE   A 1 38  ? 7.837   -30.493 -17.5   1 42.43 ? 23  PHE   A O   1 
ATOM   190  C  CB  . PHE   A 1 38  ? 10.866  -30.749 -17.643 1 42.84 ? 23  PHE   A CB  1 
ATOM   191  C  CG  . PHE   A 1 38  ? 12.127  -30.326 -16.936 1 43.72 ? 23  PHE   A CG  1 
ATOM   192  C  CD1 . PHE   A 1 38  ? 12.103  -29.321 -15.988 1 44.58 ? 23  PHE   A CD1 1 
ATOM   193  C  CD2 . PHE   A 1 38  ? 13.333  -30.941 -17.209 1 44.67 ? 23  PHE   A CD2 1 
ATOM   194  C  CE1 . PHE   A 1 38  ? 13.273  -28.908 -15.353 1 45.24 ? 23  PHE   A CE1 1 
ATOM   195  C  CE2 . PHE   A 1 38  ? 14.494  -30.548 -16.55  1 45.52 ? 23  PHE   A CE2 1 
ATOM   196  C  CZ  . PHE   A 1 38  ? 14.454  -29.536 -15.622 1 45.15 ? 23  PHE   A CZ  1 
ATOM   197  N  N   . ALA   A 1 39  ? 7.994   -32.721 -17.725 1 41.26 ? 24  ALA   A N   1 
ATOM   198  C  CA  . ALA   A 1 39  ? 6.658   -32.876 -18.266 1 41.17 ? 24  ALA   A CA  1 
ATOM   199  C  C   . ALA   A 1 39  ? 5.603   -32.555 -17.184 1 42.07 ? 24  ALA   A C   1 
ATOM   200  O  O   . ALA   A 1 39  ? 5.875   -32.622 -15.969 1 41.81 ? 24  ALA   A O   1 
ATOM   201  C  CB  . ALA   A 1 39  ? 6.462   -34.293 -18.779 1 40.85 ? 24  ALA   A CB  1 
ATOM   202  N  N   . LEU   A 1 40  ? 4.409   -32.163 -17.634 1 42.08 ? 25  LEU   A N   1 
ATOM   203  C  CA  . LEU   A 1 40  ? 3.322   -31.862 -16.728 1 42.57 ? 25  LEU   A CA  1 
ATOM   204  C  C   . LEU   A 1 40  ? 2.739   -33.213 -16.335 1 43.89 ? 25  LEU   A C   1 
ATOM   205  O  O   . LEU   A 1 40  ? 2.325   -33.981 -17.21  1 43.84 ? 25  LEU   A O   1 
ATOM   206  C  CB  . LEU   A 1 40  ? 2.279   -31.024 -17.468 1 42.69 ? 25  LEU   A CB  1 
ATOM   207  C  CG  . LEU   A 1 40  ? 1.033   -30.639 -16.696 1 44.19 ? 25  LEU   A CG  1 
ATOM   208  C  CD1 . LEU   A 1 40  ? 1.368   -29.695 -15.545 1 45    ? 25  LEU   A CD1 1 
ATOM   209  C  CD2 . LEU   A 1 40  ? 0.045   -29.983 -17.611 1 44.29 ? 25  LEU   A CD2 1 
ATOM   210  N  N   . PRO   A 1 41  ? 2.787   -33.579 -15.041 1 44.43 ? 26  PRO   A N   1 
ATOM   211  C  CA  . PRO   A 1 41  ? 2.238   -34.88  -14.644 1 45.2  ? 26  PRO   A CA  1 
ATOM   212  C  C   . PRO   A 1 41  ? 0.727   -34.913 -14.846 1 45.96 ? 26  PRO   A C   1 
ATOM   213  O  O   . PRO   A 1 41  ? 0.069   -33.901 -14.64  1 45.71 ? 26  PRO   A O   1 
ATOM   214  C  CB  . PRO   A 1 41  ? 2.628   -34.994 -13.172 1 45.62 ? 26  PRO   A CB  1 
ATOM   215  C  CG  . PRO   A 1 41  ? 2.813   -33.604 -12.715 1 45.51 ? 26  PRO   A CG  1 
ATOM   216  C  CD  . PRO   A 1 41  ? 3.28    -32.812 -13.884 1 43.78 ? 26  PRO   A CD  1 
ATOM   217  N  N   . ASN   A 1 42  ? 0.184   -36.05  -15.338 1 46.84 ? 27  ASN   A N   1 
ATOM   218  C  CA  . ASN   A 1 42  ? -1.249  -36.279 -15.597 1 47.97 ? 27  ASN   A CA  1 
ATOM   219  C  C   . ASN   A 1 42  ? -2.005  -35.004 -16.046 1 47.57 ? 27  ASN   A C   1 
ATOM   220  O  O   . ASN   A 1 42  ? -2.699  -34.374 -15.248 1 47.57 ? 27  ASN   A O   1 
ATOM   221  C  CB  . ASN   A 1 42  ? -1.909  -36.932 -14.368 1 50.99 ? 27  ASN   A CB  1 
ATOM   222  C  CG  . ASN   A 1 42  ? -3.396  -37.198 -14.506 1 58.06 ? 27  ASN   A CG  1 
ATOM   223  O  OD1 . ASN   A 1 42  ? -3.89   -37.597 -15.574 1 60.34 ? 27  ASN   A OD1 1 
ATOM   224  N  ND2 . ASN   A 1 42  ? -4.149  -36.972 -13.42  1 59.69 ? 27  ASN   A ND2 1 
ATOM   225  N  N   . PRO   A 1 43  ? -1.753  -34.534 -17.279 1 46.79 ? 28  PRO   A N   1 
ATOM   226  C  CA  . PRO   A 1 43  ? -2.397  -33.294 -17.727 1 46.38 ? 28  PRO   A CA  1 
ATOM   227  C  C   . PRO   A 1 43  ? -3.915  -33.424 -17.813 1 46.34 ? 28  PRO   A C   1 
ATOM   228  O  O   . PRO   A 1 43  ? -4.446  -34.521 -18.015 1 45.94 ? 28  PRO   A O   1 
ATOM   229  C  CB  . PRO   A 1 43  ? -1.762  -33.043 -19.111 1 46.6  ? 28  PRO   A CB  1 
ATOM   230  C  CG  . PRO   A 1 43  ? -0.595  -33.947 -19.192 1 46.79 ? 28  PRO   A CG  1 
ATOM   231  C  CD  . PRO   A 1 43  ? -0.93   -35.122 -18.35  1 45.58 ? 28  PRO   A CD  1 
ATOM   232  N  N   . GLN   A 1 44  ? -4.606  -32.297 -17.678 1 46.56 ? 29  GLN   A N   1 
ATOM   233  C  CA  . GLN   A 1 44  ? -6.06   -32.225 -17.788 1 47.19 ? 29  GLN   A CA  1 
ATOM   234  C  C   . GLN   A 1 44  ? -6.467  -32.408 -19.258 1 48.3  ? 29  GLN   A C   1 
ATOM   235  O  O   . GLN   A 1 44  ? -5.826  -31.835 -20.139 1 48.13 ? 29  GLN   A O   1 
ATOM   236  C  CB  . GLN   A 1 44  ? -6.539  -30.861 -17.271 1 47.93 ? 29  GLN   A CB  1 
ATOM   237  C  CG  . GLN   A 1 44  ? -7.99   -30.848 -16.794 1 50.81 ? 29  GLN   A CG  1 
ATOM   238  C  CD  . GLN   A 1 44  ? -8.307  -29.529 -16.134 1 54.31 ? 29  GLN   A CD  1 
ATOM   239  O  OE1 . GLN   A 1 44  ? -7.615  -29.099 -15.192 1 55.78 ? 29  GLN   A OE1 1 
ATOM   240  N  NE2 . GLN   A 1 44  ? -9.349  -28.85  -16.625 1 52.81 ? 29  GLN   A NE2 1 
ATOM   241  N  N   . GLU   A 1 45  ? -7.512  -33.212 -19.529 1 49.18 ? 30  GLU   A N   1 
ATOM   242  C  CA  . GLU   A 1 45  ? -7.968  -33.452 -20.902 1 50.35 ? 30  GLU   A CA  1 
ATOM   243  C  C   . GLU   A 1 45  ? -9.156  -32.585 -21.283 1 51.68 ? 30  GLU   A C   1 
ATOM   244  O  O   . GLU   A 1 45  ? -9.3    -32.206 -22.446 1 51.71 ? 30  GLU   A O   1 
ATOM   245  C  CB  . GLU   A 1 45  ? -8.372  -34.908 -21.096 1 53.62 ? 30  GLU   A CB  1 
ATOM   246  C  CG  . GLU   A 1 45  ? -7.372  -35.894 -20.531 1 61.7  ? 30  GLU   A CG  1 
ATOM   247  C  CD  . GLU   A 1 45  ? -7.786  -37.345 -20.655 1 70.35 ? 30  GLU   A CD  1 
ATOM   248  O  OE1 . GLU   A 1 45  ? -8.708  -37.642 -21.454 1 71.67 ? 30  GLU   A OE1 1 
ATOM   249  O  OE2 . GLU   A 1 45  ? -7.176  -38.186 -19.954 1 72.9  ? 30  GLU   A OE2 1 
ATOM   250  N  N   . ASN   A 1 46  ? -10.029 -32.295 -20.314 1 52.31 ? 31  ASN   A N   1 
ATOM   251  C  CA  . ASN   A 1 46  ? -11.221 -31.512 -20.582 1 53.13 ? 31  ASN   A CA  1 
ATOM   252  C  C   . ASN   A 1 46  ? -11.228 -30.221 -19.787 1 53.28 ? 31  ASN   A C   1 
ATOM   253  O  O   . ASN   A 1 46  ? -10.786 -30.192 -18.65  1 53.76 ? 31  ASN   A O   1 
ATOM   254  C  CB  . ASN   A 1 46  ? -12.484 -32.332 -20.269 1 54.75 ? 31  ASN   A CB  1 
ATOM   255  C  CG  . ASN   A 1 46  ? -12.454 -33.741 -20.799 1 58.66 ? 31  ASN   A CG  1 
ATOM   256  O  OD1 . ASN   A 1 46  ? -12.583 -33.993 -22.009 1 59.95 ? 31  ASN   A OD1 1 
ATOM   257  N  ND2 . ASN   A 1 46  ? -12.267 -34.689 -19.893 1 60    ? 31  ASN   A ND2 1 
ATOM   258  N  N   . LEU   A 1 47  ? -11.708 -29.15  -20.397 1 52.99 ? 32  LEU   A N   1 
ATOM   259  C  CA  . LEU   A 1 47  ? -11.845 -27.856 -19.745 1 53.51 ? 32  LEU   A CA  1 
ATOM   260  C  C   . LEU   A 1 47  ? -13.279 -27.755 -19.134 1 55.02 ? 32  LEU   A C   1 
ATOM   261  O  O   . LEU   A 1 47  ? -14.181 -28.489 -19.567 1 55.53 ? 32  LEU   A O   1 
ATOM   262  C  CB  . LEU   A 1 47  ? -11.696 -26.755 -20.816 1 53    ? 32  LEU   A CB  1 
ATOM   263  C  CG  . LEU   A 1 47  ? -10.283 -26.371 -21.254 1 53.98 ? 32  LEU   A CG  1 
ATOM   264  C  CD1 . LEU   A 1 47  ? -10.316 -25.239 -22.278 1 53.69 ? 32  LEU   A CD1 1 
ATOM   265  C  CD2 . LEU   A 1 47  ? -9.421  -25.98  -20.064 1 54.72 ? 32  LEU   A CD2 1 
ATOM   266  N  N   . PRO   A 1 48  ? -13.556 -26.801 -18.204 1 55.21 ? 33  PRO   A N   1 
ATOM   267  C  CA  . PRO   A 1 48  ? -14.952 -26.614 -17.743 1 55.29 ? 33  PRO   A CA  1 
ATOM   268  C  C   . PRO   A 1 48  ? -15.887 -26.334 -18.936 1 55.52 ? 33  PRO   A C   1 
ATOM   269  O  O   . PRO   A 1 48  ? -15.442 -25.743 -19.933 1 56.08 ? 33  PRO   A O   1 
ATOM   270  C  CB  . PRO   A 1 48  ? -14.86  -25.389 -16.829 1 55.99 ? 33  PRO   A CB  1 
ATOM   271  C  CG  . PRO   A 1 48  ? -13.416 -25.311 -16.418 1 56.59 ? 33  PRO   A CG  1 
ATOM   272  C  CD  . PRO   A 1 48  ? -12.645 -25.807 -17.597 1 54.89 ? 33  PRO   A CD  1 
ATOM   273  N  N   . ASP   A 1 49  ? -17.15  -26.812 -18.869 1 54.71 ? 34  ASP   A N   1 
ATOM   274  C  CA  . ASP   A 1 49  ? -18.16  -26.691 -19.932 1 54.5  ? 34  ASP   A CA  1 
ATOM   275  C  C   . ASP   A 1 49  ? -18.281 -25.297 -20.545 1 52.69 ? 34  ASP   A C   1 
ATOM   276  O  O   . ASP   A 1 49  ? -18.704 -25.166 -21.686 1 52.65 ? 34  ASP   A O   1 
ATOM   277  C  CB  . ASP   A 1 49  ? -19.535 -27.184 -19.442 1 57.99 ? 34  ASP   A CB  1 
ATOM   278  C  CG  . ASP   A 1 49  ? -19.644 -28.696 -19.426 1 66.11 ? 34  ASP   A CG  1 
ATOM   279  O  OD1 . ASP   A 1 49  ? -19.152 -29.338 -20.388 1 67.43 ? 34  ASP   A OD1 1 
ATOM   280  O  OD2 . ASP   A 1 49  ? -20.209 -29.243 -18.446 1 69.49 ? 34  ASP   A OD2 1 
ATOM   281  N  N   . PHE   A 1 50  ? -17.908 -24.266 -19.794 1 51.41 ? 35  PHE   A N   1 
ATOM   282  C  CA  . PHE   A 1 50  ? -17.923 -22.875 -20.244 1 50.98 ? 35  PHE   A CA  1 
ATOM   283  C  C   . PHE   A 1 50  ? -17.057 -22.682 -21.513 1 50.72 ? 35  PHE   A C   1 
ATOM   284  O  O   . PHE   A 1 50  ? -17.349 -21.808 -22.34  1 50.87 ? 35  PHE   A O   1 
ATOM   285  C  CB  . PHE   A 1 50  ? -17.412 -21.986 -19.099 1 50.66 ? 35  PHE   A CB  1 
ATOM   286  C  CG  . PHE   A 1 50  ? -17.361 -20.503 -19.364 1 51.82 ? 35  PHE   A CG  1 
ATOM   287  C  CD1 . PHE   A 1 50  ? -18.471 -19.706 -19.146 1 53.23 ? 35  PHE   A CD1 1 
ATOM   288  C  CD2 . PHE   A 1 50  ? -16.182 -19.892 -19.746 1 52.37 ? 35  PHE   A CD2 1 
ATOM   289  C  CE1 . PHE   A 1 50  ? -18.415 -18.335 -19.366 1 54.02 ? 35  PHE   A CE1 1 
ATOM   290  C  CE2 . PHE   A 1 50  ? -16.125 -18.526 -19.952 1 53.3  ? 35  PHE   A CE2 1 
ATOM   291  C  CZ  . PHE   A 1 50  ? -17.239 -17.753 -19.755 1 53.63 ? 35  PHE   A CZ  1 
ATOM   292  N  N   . TYR   A 1 51  ? -16.002 -23.51  -21.673 1 49.75 ? 36  TYR   A N   1 
ATOM   293  C  CA  . TYR   A 1 51  ? -15.076 -23.4   -22.787 1 49.03 ? 36  TYR   A CA  1 
ATOM   294  C  C   . TYR   A 1 51  ? -15.293 -24.432 -23.88  1 49.87 ? 36  TYR   A C   1 
ATOM   295  O  O   . TYR   A 1 51  ? -14.385 -24.646 -24.683 1 49.89 ? 36  TYR   A O   1 
ATOM   296  C  CB  . TYR   A 1 51  ? -13.647 -23.499 -22.257 1 47.93 ? 36  TYR   A CB  1 
ATOM   297  C  CG  . TYR   A 1 51  ? -13.308 -22.417 -21.255 1 47.63 ? 36  TYR   A CG  1 
ATOM   298  C  CD1 . TYR   A 1 51  ? -13.026 -21.125 -21.669 1 47.65 ? 36  TYR   A CD1 1 
ATOM   299  C  CD2 . TYR   A 1 51  ? -13.269 -22.687 -19.891 1 48.33 ? 36  TYR   A CD2 1 
ATOM   300  C  CE1 . TYR   A 1 51  ? -12.686 -20.135 -20.76  1 48.11 ? 36  TYR   A CE1 1 
ATOM   301  C  CE2 . TYR   A 1 51  ? -12.952 -21.695 -18.967 1 48.88 ? 36  TYR   A CE2 1 
ATOM   302  C  CZ  . TYR   A 1 51  ? -12.642 -20.424 -19.409 1 49.39 ? 36  TYR   A CZ  1 
ATOM   303  O  OH  . TYR   A 1 51  ? -12.342 -19.427 -18.507 1 51.08 ? 36  TYR   A OH  1 
ATOM   304  N  N   . ASN   A 1 52  ? -16.486 -25.068 -23.93  1 50.29 ? 37  ASN   A N   1 
ATOM   305  C  CA  . ASN   A 1 52  ? -16.829 -26.079 -24.938 1 50.87 ? 37  ASN   A CA  1 
ATOM   306  C  C   . ASN   A 1 52  ? -16.604 -25.613 -26.387 1 50.19 ? 37  ASN   A C   1 
ATOM   307  O  O   . ASN   A 1 52  ? -16.287 -26.432 -27.251 1 50.5  ? 37  ASN   A O   1 
ATOM   308  C  CB  . ASN   A 1 52  ? -18.274 -26.551 -24.761 1 53.35 ? 37  ASN   A CB  1 
ATOM   309  C  CG  . ASN   A 1 52  ? -18.468 -27.568 -23.664 1 59.48 ? 37  ASN   A CG  1 
ATOM   310  O  OD1 . ASN   A 1 52  ? -17.545 -28.29  -23.254 1 61.19 ? 37  ASN   A OD1 1 
ATOM   311  N  ND2 . ASN   A 1 52  ? -19.687 -27.636 -23.154 1 61.71 ? 37  ASN   A ND2 1 
ATOM   312  N  N   . ASP   A 1 53  ? -16.776 -24.311 -26.654 1 49.26 ? 38  ASP   A N   1 
ATOM   313  C  CA  . ASP   A 1 53  ? -16.595 -23.769 -28     1 49.21 ? 38  ASP   A CA  1 
ATOM   314  C  C   . ASP   A 1 53  ? -15.116 -23.749 -28.407 1 48.28 ? 38  ASP   A C   1 
ATOM   315  O  O   . ASP   A 1 53  ? -14.816 -23.879 -29.59  1 48.44 ? 38  ASP   A O   1 
ATOM   316  C  CB  . ASP   A 1 53  ? -17.198 -22.361 -28.118 1 52.09 ? 38  ASP   A CB  1 
ATOM   317  C  CG  . ASP   A 1 53  ? -18.712 -22.3   -28.013 1 58.37 ? 38  ASP   A CG  1 
ATOM   318  O  OD1 . ASP   A 1 53  ? -19.365 -23.344 -28.219 1 59.32 ? 38  ASP   A OD1 1 
ATOM   319  O  OD2 . ASP   A 1 53  ? -19.238 -21.209 -27.71  1 61.42 ? 38  ASP   A OD2 1 
ATOM   320  N  N   . TRP   A 1 54  ? -14.197 -23.566 -27.438 1 46.76 ? 39  TRP   A N   1 
ATOM   321  C  CA  . TRP   A 1 54  ? -12.758 -23.607 -27.705 1 45.28 ? 39  TRP   A CA  1 
ATOM   322  C  C   . TRP   A 1 54  ? -12.384 -25.062 -27.966 1 44.39 ? 39  TRP   A C   1 
ATOM   323  O  O   . TRP   A 1 54  ? -11.702 -25.36  -28.935 1 43.82 ? 39  TRP   A O   1 
ATOM   324  C  CB  . TRP   A 1 54  ? -11.966 -23.125 -26.469 1 44.74 ? 39  TRP   A CB  1 
ATOM   325  C  CG  . TRP   A 1 54  ? -11.942 -21.653 -26.211 1 44.54 ? 39  TRP   A CG  1 
ATOM   326  C  CD1 . TRP   A 1 54  ? -12.564 -20.672 -26.924 1 45.45 ? 39  TRP   A CD1 1 
ATOM   327  C  CD2 . TRP   A 1 54  ? -11.258 -21     -25.138 1 44.4  ? 39  TRP   A CD2 1 
ATOM   328  N  NE1 . TRP   A 1 54  ? -12.302 -19.446 -26.364 1 45.7  ? 39  TRP   A NE1 1 
ATOM   329  C  CE2 . TRP   A 1 54  ? -11.509 -19.62  -25.26  1 45.33 ? 39  TRP   A CE2 1 
ATOM   330  C  CE3 . TRP   A 1 54  ? -10.456 -21.449 -24.081 1 44.75 ? 39  TRP   A CE3 1 
ATOM   331  C  CZ2 . TRP   A 1 54  ? -10.95  -18.682 -24.39  1 46.09 ? 39  TRP   A CZ2 1 
ATOM   332  C  CZ3 . TRP   A 1 54  ? -9.928  -20.522 -23.206 1 45.76 ? 39  TRP   A CZ3 1 
ATOM   333  C  CH2 . TRP   A 1 54  ? -10.186 -19.158 -23.356 1 46.08 ? 39  TRP   A CH2 1 
ATOM   334  N  N   . MET   A 1 55  ? -12.839 -25.971 -27.09  1 44.64 ? 40  MET   A N   1 
ATOM   335  C  CA  . MET   A 1 55  ? -12.556 -27.394 -27.165 1 45.21 ? 40  MET   A CA  1 
ATOM   336  C  C   . MET   A 1 55  ? -13.045 -28.046 -28.439 1 44.68 ? 40  MET   A C   1 
ATOM   337  O  O   . MET   A 1 55  ? -12.346 -28.912 -28.965 1 45.16 ? 40  MET   A O   1 
ATOM   338  C  CB  . MET   A 1 55  ? -13.079 -28.127 -25.93  1 46.96 ? 40  MET   A CB  1 
ATOM   339  C  CG  . MET   A 1 55  ? -12.029 -28.212 -24.83  1 52.23 ? 40  MET   A CG  1 
ATOM   340  S  SD  . MET   A 1 55  ? -10.615 -29.231 -25.318 1 60.43 ? 40  MET   A SD  1 
ATOM   341  C  CE  . MET   A 1 55  ? -11.112 -30.754 -24.677 1 61.49 ? 40  MET   A CE  1 
ATOM   342  N  N   . PHE   A 1 56  ? -14.203 -27.617 -28.968 1 43.28 ? 41  PHE   A N   1 
ATOM   343  C  CA  . PHE   A 1 56  ? -14.708 -28.185 -30.21  1 42.6  ? 41  PHE   A CA  1 
ATOM   344  C  C   . PHE   A 1 56  ? -13.745 -27.882 -31.373 1 43.46 ? 41  PHE   A C   1 
ATOM   345  O  O   . PHE   A 1 56  ? -13.43  -28.777 -32.164 1 44.34 ? 41  PHE   A O   1 
ATOM   346  C  CB  . PHE   A 1 56  ? -16.148 -27.712 -30.514 1 41.56 ? 41  PHE   A CB  1 
ATOM   347  C  CG  . PHE   A 1 56  ? -16.573 -28.083 -31.916 1 41.5  ? 41  PHE   A CG  1 
ATOM   348  C  CD1 . PHE   A 1 56  ? -16.899 -29.394 -32.234 1 41.86 ? 41  PHE   A CD1 1 
ATOM   349  C  CD2 . PHE   A 1 56  ? -16.523 -27.149 -32.944 1 41.45 ? 41  PHE   A CD2 1 
ATOM   350  C  CE1 . PHE   A 1 56  ? -17.218 -29.748 -33.535 1 42.28 ? 41  PHE   A CE1 1 
ATOM   351  C  CE2 . PHE   A 1 56  ? -16.838 -27.508 -34.246 1 41.79 ? 41  PHE   A CE2 1 
ATOM   352  C  CZ  . PHE   A 1 56  ? -17.192 -28.801 -34.531 1 42.01 ? 41  PHE   A CZ  1 
ATOM   353  N  N   . ILE   A 1 57  ? -13.306 -26.624 -31.49  1 42.79 ? 42  ILE   A N   1 
ATOM   354  C  CA  . ILE   A 1 57  ? -12.384 -26.232 -32.549 1 42.68 ? 42  ILE   A CA  1 
ATOM   355  C  C   . ILE   A 1 57  ? -11.049 -26.985 -32.435 1 42.72 ? 42  ILE   A C   1 
ATOM   356  O  O   . ILE   A 1 57  ? -10.645 -27.635 -33.395 1 43.09 ? 42  ILE   A O   1 
ATOM   357  C  CB  . ILE   A 1 57  ? -12.187 -24.699 -32.552 1 43    ? 42  ILE   A CB  1 
ATOM   358  C  CG1 . ILE   A 1 57  ? -13.543 -23.979 -32.72  1 43.15 ? 42  ILE   A CG1 1 
ATOM   359  C  CG2 . ILE   A 1 57  ? -11.185 -24.29  -33.646 1 43.6  ? 42  ILE   A CG2 1 
ATOM   360  C  CD1 . ILE   A 1 57  ? -13.483 -22.431 -32.793 1 44.18 ? 42  ILE   A CD1 1 
ATOM   361  N  N   . ALA   A 1 58  ? -10.415 -26.963 -31.241 1 42.08 ? 43  ALA   A N   1 
ATOM   362  C  CA  . ALA   A 1 58  ? -9.161  -27.655 -30.946 1 42.14 ? 43  ALA   A CA  1 
ATOM   363  C  C   . ALA   A 1 58  ? -9.218  -29.169 -31.224 1 43.08 ? 43  ALA   A C   1 
ATOM   364  O  O   . ALA   A 1 58  ? -8.281  -29.72  -31.812 1 44.19 ? 43  ALA   A O   1 
ATOM   365  C  CB  . ALA   A 1 58  ? -8.764  -27.411 -29.507 1 41.87 ? 43  ALA   A CB  1 
ATOM   366  N  N   . LYS   A 1 59  ? -10.309 -29.83  -30.834 1 42.28 ? 44  LYS   A N   1 
ATOM   367  C  CA  . LYS   A 1 59  ? -10.457 -31.259 -31.059 1 42.76 ? 44  LYS   A CA  1 
ATOM   368  C  C   . LYS   A 1 59  ? -10.712 -31.628 -32.529 1 42.75 ? 44  LYS   A C   1 
ATOM   369  O  O   . LYS   A 1 59  ? -10.539 -32.789 -32.909 1 42.99 ? 44  LYS   A O   1 
ATOM   370  C  CB  . LYS   A 1 59  ? -11.576 -31.833 -30.173 1 44.79 ? 44  LYS   A CB  1 
ATOM   371  C  CG  . LYS   A 1 59  ? -11.2   -31.995 -28.708 1 51.04 ? 44  LYS   A CG  1 
ATOM   372  C  CD  . LYS   A 1 59  ? -12.474 -32.127 -27.847 1 57.15 ? 44  LYS   A CD  1 
ATOM   373  C  CE  . LYS   A 1 59  ? -12.52  -33.363 -26.974 1 61.35 ? 44  LYS   A CE  1 
ATOM   374  N  NZ  . LYS   A 1 59  ? -13.332 -33.14  -25.735 1 64.03 ? 44  LYS   A NZ  1 
ATOM   375  N  N   . HIS   A 1 60  ? -11.151 -30.668 -33.342 1 42.34 ? 45  HIS   A N   1 
ATOM   376  C  CA  . HIS   A 1 60  ? -11.486 -30.926 -34.735 1 42.11 ? 45  HIS   A CA  1 
ATOM   377  C  C   . HIS   A 1 60  ? -10.679 -30.089 -35.7   1 42.15 ? 45  HIS   A C   1 
ATOM   378  O  O   . HIS   A 1 60  ? -11.176 -29.757 -36.78  1 42.86 ? 45  HIS   A O   1 
ATOM   379  C  CB  . HIS   A 1 60  ? -12.996 -30.757 -34.984 1 41.99 ? 45  HIS   A CB  1 
ATOM   380  C  CG  . HIS   A 1 60  ? -13.82  -31.684 -34.146 1 43.73 ? 45  HIS   A CG  1 
ATOM   381  N  ND1 . HIS   A 1 60  ? -14.227 -31.333 -32.867 1 45.53 ? 45  HIS   A ND1 1 
ATOM   382  C  CD2 . HIS   A 1 60  ? -14.219 -32.956 -34.396 1 44.12 ? 45  HIS   A CD2 1 
ATOM   383  C  CE1 . HIS   A 1 60  ? -14.897 -32.377 -32.405 1 45.37 ? 45  HIS   A CE1 1 
ATOM   384  N  NE2 . HIS   A 1 60  ? -14.902 -33.384 -33.282 1 44.93 ? 45  HIS   A NE2 1 
ATOM   385  N  N   . LEU   A 1 61  ? -9.42   -29.777 -35.35  1 41.32 ? 46  LEU   A N   1 
ATOM   386  C  CA  . LEU   A 1 61  ? -8.548  -29.026 -36.257 1 41.04 ? 46  LEU   A CA  1 
ATOM   387  C  C   . LEU   A 1 61  ? -8.378  -29.743 -37.618 1 40.76 ? 46  LEU   A C   1 
ATOM   388  O  O   . LEU   A 1 61  ? -8.579  -29.099 -38.643 1 40.89 ? 46  LEU   A O   1 
ATOM   389  C  CB  . LEU   A 1 61  ? -7.174  -28.713 -35.637 1 41.48 ? 46  LEU   A CB  1 
ATOM   390  C  CG  . LEU   A 1 61  ? -7.114  -27.679 -34.518 1 44.23 ? 46  LEU   A CG  1 
ATOM   391  C  CD1 . LEU   A 1 61  ? -5.691  -27.381 -34.155 1 44.53 ? 46  LEU   A CD1 1 
ATOM   392  C  CD2 . LEU   A 1 61  ? -7.773  -26.373 -34.929 1 45.15 ? 46  LEU   A CD2 1 
ATOM   393  N  N   . PRO   A 1 62  ? -8.066  -31.067 -37.672 1 39.81 ? 47  PRO   A N   1 
ATOM   394  C  CA  . PRO   A 1 62  ? -7.935  -31.723 -38.98  1 40    ? 47  PRO   A CA  1 
ATOM   395  C  C   . PRO   A 1 62  ? -9.134  -31.498 -39.913 1 41.24 ? 47  PRO   A C   1 
ATOM   396  O  O   . PRO   A 1 62  ? -8.941  -31.065 -41.046 1 42.24 ? 47  PRO   A O   1 
ATOM   397  C  CB  . PRO   A 1 62  ? -7.746  -33.198 -38.606 1 40.02 ? 47  PRO   A CB  1 
ATOM   398  C  CG  . PRO   A 1 62  ? -7.119  -33.155 -37.253 1 39.95 ? 47  PRO   A CG  1 
ATOM   399  C  CD  . PRO   A 1 62  ? -7.773  -32.012 -36.572 1 38.38 ? 47  PRO   A CD  1 
ATOM   400  N  N   . ASP   A 1 63  ? -10.36  -31.699 -39.412 1 40.82 ? 48  ASP   A N   1 
ATOM   401  C  CA  . ASP   A 1 63  ? -11.588 -31.535 -40.178 1 40.97 ? 48  ASP   A CA  1 
ATOM   402  C  C   . ASP   A 1 63  ? -11.929 -30.121 -40.532 1 41.33 ? 48  ASP   A C   1 
ATOM   403  O  O   . ASP   A 1 63  ? -12.301 -29.877 -41.674 1 41.82 ? 48  ASP   A O   1 
ATOM   404  C  CB  . ASP   A 1 63  ? -12.754 -32.193 -39.447 1 41.58 ? 48  ASP   A CB  1 
ATOM   405  C  CG  . ASP   A 1 63  ? -12.483 -33.661 -39.307 1 45.08 ? 48  ASP   A CG  1 
ATOM   406  O  OD1 . ASP   A 1 63  ? -11.976 -34.267 -40.29  1 44.86 ? 48  ASP   A OD1 1 
ATOM   407  O  OD2 . ASP   A 1 63  ? -12.766 -34.208 -38.23  1 47.92 ? 48  ASP   A OD2 1 
ATOM   408  N  N   . LEU   A 1 64  ? -11.812 -29.186 -39.58  1 41.07 ? 49  LEU   A N   1 
ATOM   409  C  CA  . LEU   A 1 64  ? -12.126 -27.789 -39.85  1 41.08 ? 49  LEU   A CA  1 
ATOM   410  C  C   . LEU   A 1 64  ? -11.134 -27.16  -40.812 1 41.95 ? 49  LEU   A C   1 
ATOM   411  O  O   . LEU   A 1 64  ? -11.522 -26.297 -41.598 1 42.47 ? 49  LEU   A O   1 
ATOM   412  C  CB  . LEU   A 1 64  ? -12.171 -26.997 -38.548 1 40.52 ? 49  LEU   A CB  1 
ATOM   413  C  CG  . LEU   A 1 64  ? -13.275 -27.394 -37.586 1 40.41 ? 49  LEU   A CG  1 
ATOM   414  C  CD1 . LEU   A 1 64  ? -13.036 -26.81  -36.203 1 40.15 ? 49  LEU   A CD1 1 
ATOM   415  C  CD2 . LEU   A 1 64  ? -14.627 -27.024 -38.14  1 40.67 ? 49  LEU   A CD2 1 
ATOM   416  N  N   . ILE   A 1 65  ? -9.858  -27.553 -40.737 1 42.43 ? 50  ILE   A N   1 
ATOM   417  C  CA  . ILE   A 1 65  ? -8.839  -26.995 -41.615 1 43.58 ? 50  ILE   A CA  1 
ATOM   418  C  C   . ILE   A 1 65  ? -9.091  -27.478 -43.04  1 44.9  ? 50  ILE   A C   1 
ATOM   419  O  O   . ILE   A 1 65  ? -9.18   -26.665 -43.964 1 45.49 ? 50  ILE   A O   1 
ATOM   420  C  CB  . ILE   A 1 65  ? -7.383  -27.333 -41.149 1 43.76 ? 50  ILE   A CB  1 
ATOM   421  C  CG1 . ILE   A 1 65  ? -7.013  -26.634 -39.825 1 44.58 ? 50  ILE   A CG1 1 
ATOM   422  C  CG2 . ILE   A 1 65  ? -6.368  -26.996 -42.248 1 43.76 ? 50  ILE   A CG2 1 
ATOM   423  C  CD1 . ILE   A 1 65  ? -5.738  -27.216 -39.2   1 45.55 ? 50  ILE   A CD1 1 
ATOM   424  N  N   . GLU   A 1 66  ? -9.199  -28.802 -43.21  1 44.9  ? 51  GLU   A N   1 
ATOM   425  C  CA  . GLU   A 1 66  ? -9.385  -29.433 -44.5   1 45.38 ? 51  GLU   A CA  1 
ATOM   426  C  C   . GLU   A 1 66  ? -10.619 -28.91  -45.24  1 46.17 ? 51  GLU   A C   1 
ATOM   427  O  O   . GLU   A 1 66  ? -10.566 -28.691 -46.453 1 46.54 ? 51  GLU   A O   1 
ATOM   428  C  CB  . GLU   A 1 66  ? -9.462  -30.945 -44.317 1 46.22 ? 51  GLU   A CB  1 
ATOM   429  C  CG  . GLU   A 1 66  ? -9.341  -31.653 -45.637 1 50.93 ? 51  GLU   A CG  1 
ATOM   430  C  CD  . GLU   A 1 66  ? -9.642  -33.124 -45.556 1 55.79 ? 51  GLU   A CD  1 
ATOM   431  O  OE1 . GLU   A 1 66  ? -9.293  -33.743 -44.526 1 55.69 ? 51  GLU   A OE1 1 
ATOM   432  O  OE2 . GLU   A 1 66  ? -10.219 -33.66  -46.531 1 57.77 ? 51  GLU   A OE2 1 
ATOM   433  N  N   . SER   A 1 67  ? -11.719 -28.691 -44.503 1 46.04 ? 52  SER   A N   1 
ATOM   434  C  CA  . SER   A 1 67  ? -12.967 -28.207 -45.081 1 46.44 ? 52  SER   A CA  1 
ATOM   435  C  C   . SER   A 1 67  ? -13.056 -26.694 -45.287 1 46.79 ? 52  SER   A C   1 
ATOM   436  O  O   . SER   A 1 67  ? -14.059 -26.233 -45.807 1 47.33 ? 52  SER   A O   1 
ATOM   437  C  CB  . SER   A 1 67  ? -14.151 -28.669 -44.245 1 47.21 ? 52  SER   A CB  1 
ATOM   438  O  OG  . SER   A 1 67  ? -14.193 -27.959 -43.023 1 49.54 ? 52  SER   A OG  1 
ATOM   439  N  N   . GLY   A 1 68  ? -12.045 -25.939 -44.869 1 46.46 ? 53  GLY   A N   1 
ATOM   440  C  CA  . GLY   A 1 68  ? -12.043 -24.484 -44.986 1 46.29 ? 53  GLY   A CA  1 
ATOM   441  C  C   . GLY   A 1 68  ? -12.993 -23.796 -44.02  1 46.53 ? 53  GLY   A C   1 
ATOM   442  O  O   . GLY   A 1 68  ? -13.349 -22.632 -44.219 1 47.05 ? 53  GLY   A O   1 
ATOM   443  N  N   . GLN   A 1 69  ? -13.388 -24.489 -42.949 1 46.12 ? 54  GLN   A N   1 
ATOM   444  C  CA  . GLN   A 1 69  ? -14.345 -23.968 -41.968 1 46.68 ? 54  GLN   A CA  1 
ATOM   445  C  C   . GLN   A 1 69  ? -13.712 -23.42  -40.695 1 46.54 ? 54  GLN   A C   1 
ATOM   446  O  O   . GLN   A 1 69  ? -14.43  -22.882 -39.852 1 46.41 ? 54  GLN   A O   1 
ATOM   447  C  CB  . GLN   A 1 69  ? -15.334 -25.091 -41.552 1 48.62 ? 54  GLN   A CB  1 
ATOM   448  C  CG  . GLN   A 1 69  ? -16.305 -25.564 -42.638 1 52.11 ? 54  GLN   A CG  1 
ATOM   449  C  CD  . GLN   A 1 69  ? -17.586 -24.784 -42.693 1 59.32 ? 54  GLN   A CD  1 
ATOM   450  O  OE1 . GLN   A 1 69  ? -17.606 -23.547 -42.563 1 62.03 ? 54  GLN   A OE1 1 
ATOM   451  N  NE2 . GLN   A 1 69  ? -18.687 -25.492 -42.891 1 60.3  ? 54  GLN   A NE2 1 
ATOM   452  N  N   . LEU   A 1 70  ? -12.398 -23.641 -40.499 1 46.22 ? 55  LEU   A N   1 
ATOM   453  C  CA  . LEU   A 1 70  ? -11.737 -23.278 -39.252 1 45.11 ? 55  LEU   A CA  1 
ATOM   454  C  C   . LEU   A 1 70  ? -11.732 -21.782 -38.955 1 44.52 ? 55  LEU   A C   1 
ATOM   455  O  O   . LEU   A 1 70  ? -12.094 -21.398 -37.843 1 44.22 ? 55  LEU   A O   1 
ATOM   456  C  CB  . LEU   A 1 70  ? -10.314 -23.853 -39.171 1 44.55 ? 55  LEU   A CB  1 
ATOM   457  C  CG  . LEU   A 1 70  ? -9.608  -23.479 -37.871 1 44.52 ? 55  LEU   A CG  1 
ATOM   458  C  CD1 . LEU   A 1 70  ? -9.581  -24.583 -36.92  1 45.06 ? 55  LEU   A CD1 1 
ATOM   459  C  CD2 . LEU   A 1 70  ? -8.376  -22.739 -38.11  1 44.14 ? 55  LEU   A CD2 1 
ATOM   460  N  N   . ARG   A 1 71  ? -11.241 -20.957 -39.891 1 44.27 ? 56  ARG   A N   1 
ATOM   461  C  CA  . ARG   A 1 71  ? -11.183 -19.515 -39.681 1 44.69 ? 56  ARG   A CA  1 
ATOM   462  C  C   . ARG   A 1 71  ? -12.547 -18.899 -39.336 1 46    ? 56  ARG   A C   1 
ATOM   463  O  O   . ARG   A 1 71  ? -12.617 -18.048 -38.453 1 46.93 ? 56  ARG   A O   1 
ATOM   464  C  CB  . ARG   A 1 71  ? -10.538 -18.843 -40.879 1 45    ? 56  ARG   A CB  1 
ATOM   465  C  CG  . ARG   A 1 71  ? -9.063  -19.157 -40.892 1 46.46 ? 56  ARG   A CG  1 
ATOM   466  C  CD  . ARG   A 1 71  ? -8.38   -18.741 -42.148 1 47.21 ? 56  ARG   A CD  1 
ATOM   467  N  NE  . ARG   A 1 71  ? -6.929  -18.783 -41.996 1 47.56 ? 56  ARG   A NE  1 
ATOM   468  C  CZ  . ARG   A 1 71  ? -6.079  -18.922 -43.005 1 49.22 ? 56  ARG   A CZ  1 
ATOM   469  N  NH1 . ARG   A 1 71  ? -6.529  -19.087 -44.246 1 48.57 ? 56  ARG   A NH1 1 
ATOM   470  N  NH2 . ARG   A 1 71  ? -4.771  -18.913 -42.782 1 48.25 ? 56  ARG   A NH2 1 
ATOM   471  N  N   . GLU   A 1 72  ? -13.632 -19.416 -39.941 1 45.54 ? 57  GLU   A N   1 
ATOM   472  C  CA  . GLU   A 1 72  ? -14.991 -18.976 -39.672 1 45.56 ? 57  GLU   A CA  1 
ATOM   473  C  C   . GLU   A 1 72  ? -15.438 -19.343 -38.248 1 45.13 ? 57  GLU   A C   1 
ATOM   474  O  O   . GLU   A 1 72  ? -16.025 -18.506 -37.574 1 45.34 ? 57  GLU   A O   1 
ATOM   475  C  CB  . GLU   A 1 72  ? -15.949 -19.555 -40.72  1 48.41 ? 57  GLU   A CB  1 
ATOM   476  C  CG  . GLU   A 1 72  ? -17.365 -19.037 -40.586 1 56.89 ? 57  GLU   A CG  1 
ATOM   477  C  CD  . GLU   A 1 72  ? -18.424 -19.986 -41.113 1 69.74 ? 57  GLU   A CD  1 
ATOM   478  O  OE1 . GLU   A 1 72  ? -18.221 -20.566 -42.207 1 72.74 ? 57  GLU   A OE1 1 
ATOM   479  O  OE2 . GLU   A 1 72  ? -19.459 -20.155 -40.427 1 74.08 ? 57  GLU   A OE2 1 
ATOM   480  N  N   . ARG   A 1 73  ? -15.143 -20.566 -37.769 1 44.81 ? 58  ARG   A N   1 
ATOM   481  C  CA  . ARG   A 1 73  ? -15.496 -20.981 -36.403 1 45.09 ? 58  ARG   A CA  1 
ATOM   482  C  C   . ARG   A 1 73  ? -14.77  -20.127 -35.362 1 45.2  ? 58  ARG   A C   1 
ATOM   483  O  O   . ARG   A 1 73  ? -15.33  -19.825 -34.309 1 45.38 ? 58  ARG   A O   1 
ATOM   484  C  CB  . ARG   A 1 73  ? -15.16  -22.468 -36.166 1 46.76 ? 58  ARG   A CB  1 
ATOM   485  C  CG  . ARG   A 1 73  ? -16.009 -23.475 -36.948 1 50.78 ? 58  ARG   A CG  1 
ATOM   486  C  CD  . ARG   A 1 73  ? -17.46  -23.544 -36.473 1 54.57 ? 58  ARG   A CD  1 
ATOM   487  N  NE  . ARG   A 1 73  ? -18.313 -22.586 -37.18  1 58.74 ? 58  ARG   A NE  1 
ATOM   488  C  CZ  . ARG   A 1 73  ? -19.486 -22.146 -36.728 1 61.71 ? 58  ARG   A CZ  1 
ATOM   489  N  NH1 . ARG   A 1 73  ? -19.967 -22.584 -35.569 1 59.67 ? 58  ARG   A NH1 1 
ATOM   490  N  NH2 . ARG   A 1 73  ? -20.188 -21.268 -37.434 1 62.99 ? 58  ARG   A NH2 1 
ATOM   491  N  N   . VAL   A 1 74  ? -13.52  -19.742 -35.657 1 44.8  ? 59  VAL   A N   1 
ATOM   492  C  CA  . VAL   A 1 74  ? -12.735 -18.908 -34.765 1 44.93 ? 59  VAL   A CA  1 
ATOM   493  C  C   . VAL   A 1 74  ? -13.328 -17.51  -34.764 1 45.31 ? 59  VAL   A C   1 
ATOM   494  O  O   . VAL   A 1 74  ? -13.56  -16.948 -33.692 1 45.36 ? 59  VAL   A O   1 
ATOM   495  C  CB  . VAL   A 1 74  ? -11.225 -18.916 -35.141 1 44.61 ? 59  VAL   A CB  1 
ATOM   496  C  CG1 . VAL   A 1 74  ? -10.441 -17.882 -34.345 1 44.26 ? 59  VAL   A CG1 1 
ATOM   497  C  CG2 . VAL   A 1 74  ? -10.626 -20.303 -34.951 1 44.6  ? 59  VAL   A CG2 1 
ATOM   498  N  N   . GLU   A 1 75  ? -13.626 -16.964 -35.961 1 45.05 ? 60  GLU   A N   1 
ATOM   499  C  CA  . GLU   A 1 75  ? -14.208 -15.628 -36.071 1 45.27 ? 60  GLU   A CA  1 
ATOM   500  C  C   . GLU   A 1 75  ? -15.628 -15.517 -35.474 1 45.87 ? 60  GLU   A C   1 
ATOM   501  O  O   . GLU   A 1 75  ? -16.034 -14.437 -35.076 1 45.7  ? 60  GLU   A O   1 
ATOM   502  C  CB  . GLU   A 1 75  ? -14.164 -15.126 -37.515 1 45.83 ? 60  GLU   A CB  1 
ATOM   503  C  CG  . GLU   A 1 75  ? -12.755 -14.869 -38.019 1 47.33 ? 60  GLU   A CG  1 
ATOM   504  C  CD  . GLU   A 1 75  ? -12.575 -15.033 -39.521 1 52.98 ? 60  GLU   A CD  1 
ATOM   505  O  OE1 . GLU   A 1 75  ? -13.58  -15.318 -40.216 1 55.38 ? 60  GLU   A OE1 1 
ATOM   506  O  OE2 . GLU   A 1 75  ? -11.428 -14.89  -40.005 1 53.33 ? 60  GLU   A OE2 1 
ATOM   507  N  N   . LYS   A 1 76  ? -16.359 -16.633 -35.37  1 46.72 ? 61  LYS   A N   1 
ATOM   508  C  CA  . LYS   A 1 76  ? -17.702 -16.652 -34.793 1 47.58 ? 61  LYS   A CA  1 
ATOM   509  C  C   . LYS   A 1 76  ? -17.714 -16.777 -33.251 1 48.59 ? 61  LYS   A C   1 
ATOM   510  O  O   . LYS   A 1 76  ? -18.77  -16.599 -32.637 1 48.86 ? 61  LYS   A O   1 
ATOM   511  C  CB  . LYS   A 1 76  ? -18.553 -17.768 -35.428 1 49.43 ? 61  LYS   A CB  1 
ATOM   512  N  N   . LEU   A 1 77  ? -16.559 -17.105 -32.63  1 48.46 ? 62  LEU   A N   1 
ATOM   513  C  CA  . LEU   A 1 77  ? -16.455 -17.247 -31.176 1 48.42 ? 62  LEU   A CA  1 
ATOM   514  C  C   . LEU   A 1 77  ? -16.743 -15.952 -30.422 1 48.64 ? 62  LEU   A C   1 
ATOM   515  O  O   . LEU   A 1 77  ? -16.447 -14.858 -30.892 1 48.14 ? 62  LEU   A O   1 
ATOM   516  C  CB  . LEU   A 1 77  ? -15.022 -17.676 -30.779 1 47.95 ? 62  LEU   A CB  1 
ATOM   517  C  CG  . LEU   A 1 77  ? -14.586 -19.107 -31.016 1 47.95 ? 62  LEU   A CG  1 
ATOM   518  C  CD1 . LEU   A 1 77  ? -13.081 -19.243 -30.784 1 48.12 ? 62  LEU   A CD1 1 
ATOM   519  C  CD2 . LEU   A 1 77  ? -15.347 -20.052 -30.146 1 47.74 ? 62  LEU   A CD2 1 
ATOM   520  N  N   . ASN   A 1 78  ? -17.226 -16.098 -29.199 1 49.69 ? 63  ASN   A N   1 
ATOM   521  C  CA  . ASN   A 1 78  ? -17.401 -14.98  -28.274 1 50.68 ? 63  ASN   A CA  1 
ATOM   522  C  C   . ASN   A 1 78  ? -16.15  -14.916 -27.37  1 51.63 ? 63  ASN   A C   1 
ATOM   523  O  O   . ASN   A 1 78  ? -15.52  -15.959 -27.106 1 51.8  ? 63  ASN   A O   1 
ATOM   524  C  CB  . ASN   A 1 78  ? -18.63  -15.204 -27.408 1 51.5  ? 63  ASN   A CB  1 
ATOM   525  C  CG  . ASN   A 1 78  ? -19.909 -15.074 -28.177 1 53.45 ? 63  ASN   A CG  1 
ATOM   526  O  OD1 . ASN   A 1 78  ? -20.041 -14.225 -29.077 1 53.48 ? 63  ASN   A OD1 1 
ATOM   527  N  ND2 . ASN   A 1 78  ? -20.867 -15.927 -27.834 1 53.82 ? 63  ASN   A ND2 1 
ATOM   528  N  N   . MET   A 1 79  ? -15.802 -13.709 -26.874 1 51.68 ? 64  MET   A N   1 
ATOM   529  C  CA  . MET   A 1 79  ? -14.635 -13.573 -26.018 1 52.09 ? 64  MET   A CA  1 
ATOM   530  C  C   . MET   A 1 79  ? -14.943 -14.201 -24.692 1 53.55 ? 64  MET   A C   1 
ATOM   531  O  O   . MET   A 1 79  ? -15.848 -13.751 -24     1 54.42 ? 64  MET   A O   1 
ATOM   532  C  CB  . MET   A 1 79  ? -14.199 -12.122 -25.848 1 51.75 ? 64  MET   A CB  1 
ATOM   533  C  CG  . MET   A 1 79  ? -12.764 -12.005 -25.394 1 52.96 ? 64  MET   A CG  1 
ATOM   534  S  SD  . MET   A 1 79  ? -12.29  -10.296 -25.054 1 56.09 ? 64  MET   A SD  1 
ATOM   535  C  CE  . MET   A 1 79  ? -12.144 -9.618  -26.694 1 49.44 ? 64  MET   A CE  1 
ATOM   536  N  N   . LEU   A 1 80  ? -14.267 -15.304 -24.38  1 53.86 ? 65  LEU   A N   1 
ATOM   537  C  CA  . LEU   A 1 80  ? -14.474 -15.991 -23.119 1 54.51 ? 65  LEU   A CA  1 
ATOM   538  C  C   . LEU   A 1 80  ? -13.469 -15.481 -22.088 1 55.37 ? 65  LEU   A C   1 
ATOM   539  O  O   . LEU   A 1 80  ? -12.306 -15.211 -22.427 1 55.93 ? 65  LEU   A O   1 
ATOM   540  C  CB  . LEU   A 1 80  ? -14.372 -17.521 -23.288 1 54.43 ? 65  LEU   A CB  1 
ATOM   541  C  CG  . LEU   A 1 80  ? -15.46  -18.172 -24.143 1 55.56 ? 65  LEU   A CG  1 
ATOM   542  C  CD1 . LEU   A 1 80  ? -15.281 -19.666 -24.204 1 55.67 ? 65  LEU   A CD1 1 
ATOM   543  C  CD2 . LEU   A 1 80  ? -16.877 -17.821 -23.63  1 56.07 ? 65  LEU   A CD2 1 
ATOM   544  N  N   . SER   A 1 81  ? -13.927 -15.308 -20.836 1 55.05 ? 66  SER   A N   1 
ATOM   545  C  CA  . SER   A 1 81  ? -13.074 -14.839 -19.747 1 55.13 ? 66  SER   A CA  1 
ATOM   546  C  C   . SER   A 1 81  ? -12.176 -15.978 -19.283 1 55.17 ? 66  SER   A C   1 
ATOM   547  O  O   . SER   A 1 81  ? -12.628 -17.117 -19.22  1 55.29 ? 66  SER   A O   1 
ATOM   548  C  CB  . SER   A 1 81  ? -13.927 -14.36  -18.573 1 55.71 ? 66  SER   A CB  1 
ATOM   549  N  N   . ILE   A 1 82  ? -10.932 -15.674 -18.912 1 54.94 ? 67  ILE   A N   1 
ATOM   550  C  CA  . ILE   A 1 82  ? -10.03  -16.71  -18.403 1 55.04 ? 67  ILE   A CA  1 
ATOM   551  C  C   . ILE   A 1 82  ? -10.26  -17.027 -16.905 1 56.07 ? 67  ILE   A C   1 
ATOM   552  O  O   . ILE   A 1 82  ? -9.703  -18.014 -16.399 1 56.07 ? 67  ILE   A O   1 
ATOM   553  C  CB  . ILE   A 1 82  ? -8.549  -16.406 -18.713 1 54.41 ? 67  ILE   A CB  1 
ATOM   554  C  CG1 . ILE   A 1 82  ? -7.981  -15.3   -17.827 1 54.77 ? 67  ILE   A CG1 1 
ATOM   555  C  CG2 . ILE   A 1 82  ? -8.37   -16.099 -20.186 1 54.48 ? 67  ILE   A CG2 1 
ATOM   556  C  CD1 . ILE   A 1 82  ? -6.485  -15.31  -17.794 1 55.84 ? 67  ILE   A CD1 1 
ATOM   557  N  N   . ASP   A 1 83  ? -11.109 -16.232 -16.213 1 56.34 ? 68  ASP   A N   1 
ATOM   558  C  CA  . ASP   A 1 83  ? -11.387 -16.38  -14.788 1 57.48 ? 68  ASP   A CA  1 
ATOM   559  C  C   . ASP   A 1 83  ? -11.843 -17.769 -14.358 1 57.79 ? 68  ASP   A C   1 
ATOM   560  O  O   . ASP   A 1 83  ? -11.567 -18.158 -13.226 1 58.35 ? 68  ASP   A O   1 
ATOM   561  C  CB  . ASP   A 1 83  ? -12.401 -15.322 -14.328 1 60.22 ? 68  ASP   A CB  1 
ATOM   562  C  CG  . ASP   A 1 83  ? -11.933 -13.883 -14.48  1 66.9  ? 68  ASP   A CG  1 
ATOM   563  O  OD1 . ASP   A 1 83  ? -10.809 -13.668 -15     1 67.71 ? 68  ASP   A OD1 1 
ATOM   564  O  OD2 . ASP   A 1 83  ? -12.684 -12.969 -14.071 1 70.43 ? 68  ASP   A OD2 1 
ATOM   565  N  N   . HIS   A 1 84  ? -12.499 -18.53  -15.248 1 57.56 ? 69  HIS   A N   1 
ATOM   566  C  CA  . HIS   A 1 84  ? -13.003 -19.868 -14.92  1 58.01 ? 69  HIS   A CA  1 
ATOM   567  C  C   . HIS   A 1 84  ? -11.923 -20.982 -14.996 1 57.31 ? 69  HIS   A C   1 
ATOM   568  O  O   . HIS   A 1 84  ? -12.221 -22.134 -14.685 1 57.69 ? 69  HIS   A O   1 
ATOM   569  C  CB  . HIS   A 1 84  ? -14.252 -20.206 -15.76  1 59.78 ? 69  HIS   A CB  1 
ATOM   570  C  CG  . HIS   A 1 84  ? -15.287 -19.119 -15.683 1 63.72 ? 69  HIS   A CG  1 
ATOM   571  N  ND1 . HIS   A 1 84  ? -16.25  -19.107 -14.689 1 65.95 ? 69  HIS   A ND1 1 
ATOM   572  C  CD2 . HIS   A 1 84  ? -15.406 -17.985 -16.417 1 65.32 ? 69  HIS   A CD2 1 
ATOM   573  C  CE1 . HIS   A 1 84  ? -16.94  -17.992 -14.872 1 66.66 ? 69  HIS   A CE1 1 
ATOM   574  N  NE2 . HIS   A 1 84  ? -16.464 -17.282 -15.895 1 66.55 ? 69  HIS   A NE2 1 
ATOM   575  N  N   . LEU   A 1 85  ? -10.673 -20.632 -15.354 1 56.24 ? 70  LEU   A N   1 
ATOM   576  C  CA  . LEU   A 1 85  ? -9.543  -21.573 -15.375 1 55.73 ? 70  LEU   A CA  1 
ATOM   577  C  C   . LEU   A 1 85  ? -8.825  -21.374 -14.024 1 56.72 ? 70  LEU   A C   1 
ATOM   578  O  O   . LEU   A 1 85  ? -7.923  -20.552 -13.905 1 56.85 ? 70  LEU   A O   1 
ATOM   579  C  CB  . LEU   A 1 85  ? -8.606  -21.267 -16.558 1 54.36 ? 70  LEU   A CB  1 
ATOM   580  C  CG  . LEU   A 1 85  ? -9.273  -21.269 -17.941 1 53.94 ? 70  LEU   A CG  1 
ATOM   581  C  CD1 . LEU   A 1 85  ? -8.45   -20.538 -18.937 1 54.06 ? 70  LEU   A CD1 1 
ATOM   582  C  CD2 . LEU   A 1 85  ? -9.571  -22.663 -18.414 1 53.97 ? 70  LEU   A CD2 1 
ATOM   583  N  N   . THR   A 1 86  ? -9.297  -22.078 -12.998 1 57.4  ? 71  THR   A N   1 
ATOM   584  C  CA  . THR   A 1 86  ? -8.89   -21.915 -11.598 1 58.41 ? 71  THR   A CA  1 
ATOM   585  C  C   . THR   A 1 86  ? -7.526  -22.485 -11.177 1 58.51 ? 71  THR   A C   1 
ATOM   586  O  O   . THR   A 1 86  ? -6.936  -21.959 -10.23  1 59.18 ? 71  THR   A O   1 
ATOM   587  C  CB  . THR   A 1 86  ? -9.97   -22.513 -10.693 1 60.2  ? 71  THR   A CB  1 
ATOM   588  O  OG1 . THR   A 1 86  ? -10.007 -23.938 -10.869 1 61.64 ? 71  THR   A OG1 1 
ATOM   589  C  CG2 . THR   A 1 86  ? -11.341 -21.908 -10.958 1 60.61 ? 71  THR   A CG2 1 
ATOM   590  N  N   . ASP   A 1 87  ? -7.061  -23.583 -11.796 1 57.27 ? 72  ASP   A N   1 
ATOM   591  C  CA  . ASP   A 1 87  ? -5.777  -24.172 -11.413 1 56.48 ? 72  ASP   A CA  1 
ATOM   592  C  C   . ASP   A 1 87  ? -4.744  -24.155 -12.562 1 54.67 ? 72  ASP   A C   1 
ATOM   593  O  O   . ASP   A 1 87  ? -5.092  -23.821 -13.698 1 55    ? 72  ASP   A O   1 
ATOM   594  C  CB  . ASP   A 1 87  ? -5.986  -25.592 -10.838 1 58.7  ? 72  ASP   A CB  1 
ATOM   595  C  CG  . ASP   A 1 87  ? -6.741  -26.535 -11.75  1 63.8  ? 72  ASP   A CG  1 
ATOM   596  O  OD1 . ASP   A 1 87  ? -6.883  -26.218 -12.941 1 64.34 ? 72  ASP   A OD1 1 
ATOM   597  O  OD2 . ASP   A 1 87  ? -7.187  -27.594 -11.268 1 67.08 ? 72  ASP   A OD2 1 
ATOM   598  N  N   . HIS   A 1 88  ? -3.482  -24.519 -12.262 1 52.16 ? 73  HIS   A N   1 
ATOM   599  C  CA  . HIS   A 1 88  ? -2.404  -24.546 -13.237 1 49.96 ? 73  HIS   A CA  1 
ATOM   600  C  C   . HIS   A 1 88  ? -2.706  -25.532 -14.369 1 48.31 ? 73  HIS   A C   1 
ATOM   601  O  O   . HIS   A 1 88  ? -2.514  -25.181 -15.521 1 48.47 ? 73  HIS   A O   1 
ATOM   602  C  CB  . HIS   A 1 88  ? -1.07   -24.891 -12.545 1 49.59 ? 73  HIS   A CB  1 
ATOM   603  C  CG  . HIS   A 1 88  ? 0.12    -24.87  -13.453 1 50.08 ? 73  HIS   A CG  1 
ATOM   604  N  ND1 . HIS   A 1 88  ? 0.659   -23.681 -13.911 1 51.43 ? 73  HIS   A ND1 1 
ATOM   605  C  CD2 . HIS   A 1 88  ? 0.865   -25.893 -13.925 1 50.81 ? 73  HIS   A CD2 1 
ATOM   606  C  CE1 . HIS   A 1 88  ? 1.673   -24.02  -14.688 1 51.56 ? 73  HIS   A CE1 1 
ATOM   607  N  NE2 . HIS   A 1 88  ? 1.849   -25.336 -14.712 1 51.72 ? 73  HIS   A NE2 1 
ATOM   608  N  N   . LYS   A 1 89  ? -3.207  -26.727 -14.054 1 46.74 ? 74  LYS   A N   1 
ATOM   609  C  CA  . LYS   A 1 89  ? -3.512  -27.733 -15.072 1 46.24 ? 74  LYS   A CA  1 
ATOM   610  C  C   . LYS   A 1 89  ? -4.586  -27.3   -16.081 1 46.23 ? 74  LYS   A C   1 
ATOM   611  O  O   . LYS   A 1 89  ? -4.431  -27.577 -17.274 1 46.51 ? 74  LYS   A O   1 
ATOM   612  C  CB  . LYS   A 1 89  ? -3.862  -29.082 -14.444 1 46.73 ? 74  LYS   A CB  1 
ATOM   613  C  CG  . LYS   A 1 89  ? -2.647  -29.743 -13.825 1 49.59 ? 74  LYS   A CG  1 
ATOM   614  C  CD  . LYS   A 1 89  ? -2.849  -31.221 -13.686 1 52.12 ? 74  LYS   A CD  1 
ATOM   615  C  CE  . LYS   A 1 89  ? -1.738  -31.871 -12.932 1 54.13 ? 74  LYS   A CE  1 
ATOM   616  N  NZ  . LYS   A 1 89  ? -2.022  -33.324 -12.76  1 56.36 ? 74  LYS   A NZ  1 
ATOM   617  N  N   . SER   A 1 90  ? -5.645  -26.608 -15.634 1 45.66 ? 75  SER   A N   1 
ATOM   618  C  CA  . SER   A 1 90  ? -6.662  -26.115 -16.573 1 45.5  ? 75  SER   A CA  1 
ATOM   619  C  C   . SER   A 1 90  ? -6.124  -24.927 -17.392 1 44.81 ? 75  SER   A C   1 
ATOM   620  O  O   . SER   A 1 90  ? -6.499  -24.766 -18.557 1 44.83 ? 75  SER   A O   1 
ATOM   621  C  CB  . SER   A 1 90  ? -7.977  -25.777 -15.87  1 46.83 ? 75  SER   A CB  1 
ATOM   622  O  OG  . SER   A 1 90  ? -7.881  -24.631 -15.044 1 49.64 ? 75  SER   A OG  1 
ATOM   623  N  N   . GLN   A 1 91  ? -5.223  -24.125 -16.802 1 43.84 ? 76  GLN   A N   1 
ATOM   624  C  CA  . GLN   A 1 91  ? -4.589  -23.018 -17.506 1 43.89 ? 76  GLN   A CA  1 
ATOM   625  C  C   . GLN   A 1 91  ? -3.613  -23.548 -18.572 1 43.03 ? 76  GLN   A C   1 
ATOM   626  O  O   . GLN   A 1 91  ? -3.461  -22.932 -19.629 1 43.47 ? 76  GLN   A O   1 
ATOM   627  C  CB  . GLN   A 1 91  ? -3.818  -22.136 -16.522 1 45.76 ? 76  GLN   A CB  1 
ATOM   628  C  CG  . GLN   A 1 91  ? -4.708  -21.243 -15.673 1 49.19 ? 76  GLN   A CG  1 
ATOM   629  C  CD  . GLN   A 1 91  ? -4.001  -20.682 -14.456 1 54.4  ? 76  GLN   A CD  1 
ATOM   630  O  OE1 . GLN   A 1 91  ? -2.797  -20.869 -14.244 1 57.11 ? 76  GLN   A OE1 1 
ATOM   631  N  NE2 . GLN   A 1 91  ? -4.741  -19.98  -13.615 1 55.17 ? 76  GLN   A NE2 1 
ATOM   632  N  N   . ARG   A 1 92  ? -2.938  -24.668 -18.283 1 41.44 ? 77  ARG   A N   1 
ATOM   633  C  CA  . ARG   A 1 92  ? -1.989  -25.275 -19.209 1 40.57 ? 77  ARG   A CA  1 
ATOM   634  C  C   . ARG   A 1 92  ? -2.73   -25.904 -20.388 1 39.72 ? 77  ARG   A C   1 
ATOM   635  O  O   . ARG   A 1 92  ? -2.247  -25.807 -21.506 1 39.62 ? 77  ARG   A O   1 
ATOM   636  C  CB  . ARG   A 1 92  ? -1.092  -26.321 -18.505 1 40.4  ? 77  ARG   A CB  1 
ATOM   637  C  CG  . ARG   A 1 92  ? 0.004   -25.71  -17.65  1 40.69 ? 77  ARG   A CG  1 
ATOM   638  C  CD  . ARG   A 1 92  ? 1.124   -25.053 -18.452 1 41.01 ? 77  ARG   A CD  1 
ATOM   639  N  NE  . ARG   A 1 92  ? 1.918   -26.018 -19.218 1 41.07 ? 77  ARG   A NE  1 
ATOM   640  C  CZ  . ARG   A 1 92  ? 2.908   -26.749 -18.713 1 40.52 ? 77  ARG   A CZ  1 
ATOM   641  N  NH1 . ARG   A 1 92  ? 3.243   -26.634 -17.434 1 41.48 ? 77  ARG   A NH1 1 
ATOM   642  N  NH2 . ARG   A 1 92  ? 3.564   -27.608 -19.48  1 37.34 ? 77  ARG   A NH2 1 
ATOM   643  N  N   . LEU   A 1 93  ? -3.887  -26.54  -20.136 1 39.41 ? 78  LEU   A N   1 
ATOM   644  C  CA  . LEU   A 1 93  ? -4.715  -27.159 -21.169 1 39.47 ? 78  LEU   A CA  1 
ATOM   645  C  C   . LEU   A 1 93  ? -5.269  -26.087 -22.076 1 40.53 ? 78  LEU   A C   1 
ATOM   646  O  O   . LEU   A 1 93  ? -5.196  -26.232 -23.298 1 41.34 ? 78  LEU   A O   1 
ATOM   647  C  CB  . LEU   A 1 93  ? -5.868  -27.977 -20.557 1 38.8  ? 78  LEU   A CB  1 
ATOM   648  C  CG  . LEU   A 1 93  ? -6.896  -28.557 -21.561 1 39.03 ? 78  LEU   A CG  1 
ATOM   649  C  CD1 . LEU   A 1 93  ? -6.246  -29.452 -22.598 1 38.85 ? 78  LEU   A CD1 1 
ATOM   650  C  CD2 . LEU   A 1 93  ? -7.952  -29.309 -20.864 1 39.2  ? 78  LEU   A CD2 1 
ATOM   651  N  N   . ALA   A 1 94  ? -5.767  -24.986 -21.493 1 40.09 ? 79  ALA   A N   1 
ATOM   652  C  CA  . ALA   A 1 94  ? -6.309  -23.888 -22.269 1 39.93 ? 79  ALA   A CA  1 
ATOM   653  C  C   . ALA   A 1 94  ? -5.253  -23.262 -23.165 1 39.05 ? 79  ALA   A C   1 
ATOM   654  O  O   . ALA   A 1 94  ? -5.571  -22.893 -24.295 1 39.85 ? 79  ALA   A O   1 
ATOM   655  C  CB  . ALA   A 1 94  ? -6.934  -22.851 -21.356 1 40.38 ? 79  ALA   A CB  1 
ATOM   656  N  N   . ARG   A 1 95  ? -3.999  -23.198 -22.701 1 37.49 ? 80  ARG   A N   1 
ATOM   657  C  CA  . ARG   A 1 95  ? -2.865  -22.676 -23.466 1 36.71 ? 80  ARG   A CA  1 
ATOM   658  C  C   . ARG   A 1 95  ? -2.544  -23.601 -24.662 1 36.68 ? 80  ARG   A C   1 
ATOM   659  O  O   . ARG   A 1 95  ? -2.152  -23.13  -25.733 1 36.44 ? 80  ARG   A O   1 
ATOM   660  C  CB  . ARG   A 1 95  ? -1.635  -22.616 -22.562 1 37.34 ? 80  ARG   A CB  1 
ATOM   661  C  CG  . ARG   A 1 95  ? -1.072  -21.235 -22.39  1 37.78 ? 80  ARG   A CG  1 
ATOM   662  C  CD  . ARG   A 1 95  ? 0.377   -21.314 -21.925 1 37.92 ? 80  ARG   A CD  1 
ATOM   663  N  NE  . ARG   A 1 95  ? 1.334   -21.513 -23.021 1 37.12 ? 80  ARG   A NE  1 
ATOM   664  C  CZ  . ARG   A 1 95  ? 1.798   -20.542 -23.8   1 37.25 ? 80  ARG   A CZ  1 
ATOM   665  N  NH1 . ARG   A 1 95  ? 1.371   -19.3   -23.646 1 37.29 ? 80  ARG   A NH1 1 
ATOM   666  N  NH2 . ARG   A 1 95  ? 2.681   -20.81  -24.75  1 36.31 ? 80  ARG   A NH2 1 
ATOM   667  N  N   . LEU   A 1 96  ? -2.675  -24.914 -24.462 1 36.4  ? 81  LEU   A N   1 
ATOM   668  C  CA  . LEU   A 1 96  ? -2.436  -25.889 -25.511 1 37.32 ? 81  LEU   A CA  1 
ATOM   669  C  C   . LEU   A 1 96  ? -3.575  -25.8   -26.546 1 37.88 ? 81  LEU   A C   1 
ATOM   670  O  O   . LEU   A 1 96  ? -3.305  -25.751 -27.75  1 38.27 ? 81  LEU   A O   1 
ATOM   671  C  CB  . LEU   A 1 96  ? -2.339  -27.277 -24.869 1 37.5  ? 81  LEU   A CB  1 
ATOM   672  C  CG  . LEU   A 1 96  ? -2.4    -28.466 -25.779 1 38.47 ? 81  LEU   A CG  1 
ATOM   673  C  CD1 . LEU   A 1 96  ? -1.26   -28.469 -26.772 1 38.53 ? 81  LEU   A CD1 1 
ATOM   674  C  CD2 . LEU   A 1 96  ? -2.428  -29.722 -24.971 1 39.24 ? 81  LEU   A CD2 1 
ATOM   675  N  N   . VAL   A 1 97  ? -4.832  -25.695 -26.064 1 37.78 ? 82  VAL   A N   1 
ATOM   676  C  CA  . VAL   A 1 97  ? -6.038  -25.524 -26.878 1 38.27 ? 82  VAL   A CA  1 
ATOM   677  C  C   . VAL   A 1 97  ? -5.929  -24.27  -27.754 1 38.93 ? 82  VAL   A C   1 
ATOM   678  O  O   . VAL   A 1 97  ? -5.995  -24.383 -28.976 1 39.81 ? 82  VAL   A O   1 
ATOM   679  C  CB  . VAL   A 1 97  ? -7.34   -25.536 -26.004 1 38.28 ? 82  VAL   A CB  1 
ATOM   680  C  CG1 . VAL   A 1 97  ? -8.538  -24.936 -26.735 1 38.34 ? 82  VAL   A CG1 1 
ATOM   681  C  CG2 . VAL   A 1 97  ? -7.668  -26.943 -25.536 1 38.31 ? 82  VAL   A CG2 1 
ATOM   682  N  N   . LEU   A 1 98  ? -5.716  -23.094 -27.142 1 38.43 ? 83  LEU   A N   1 
ATOM   683  C  CA  . LEU   A 1 98  ? -5.621  -21.821 -27.857 1 38.59 ? 83  LEU   A CA  1 
ATOM   684  C  C   . LEU   A 1 98  ? -4.414  -21.712 -28.783 1 37.72 ? 83  LEU   A C   1 
ATOM   685  O  O   . LEU   A 1 98  ? -4.474  -21.021 -29.806 1 37.03 ? 83  LEU   A O   1 
ATOM   686  C  CB  . LEU   A 1 98  ? -5.594  -20.664 -26.852 1 39.54 ? 83  LEU   A CB  1 
ATOM   687  C  CG  . LEU   A 1 98  ? -6.866  -20.45  -26.037 1 41.51 ? 83  LEU   A CG  1 
ATOM   688  C  CD1 . LEU   A 1 98  ? -6.682  -19.336 -25.042 1 41.58 ? 83  LEU   A CD1 1 
ATOM   689  C  CD2 . LEU   A 1 98  ? -8.052  -20.153 -26.951 1 42.6  ? 83  LEU   A CD2 1 
ATOM   690  N  N   . GLY   A 1 99  ? -3.314  -22.349 -28.394 1 37.15 ? 84  GLY   A N   1 
ATOM   691  C  CA  . GLY   A 1 99  ? -2.086  -22.325 -29.183 1 36.59 ? 84  GLY   A CA  1 
ATOM   692  C  C   . GLY   A 1 99  ? -2.216  -23.154 -30.431 1 36.17 ? 84  GLY   A C   1 
ATOM   693  O  O   . GLY   A 1 99  ? -1.755  -22.745 -31.486 1 36.1  ? 84  GLY   A O   1 
ATOM   694  N  N   . CYS   A 1 100 ? -2.872  -24.315 -30.326 1 36.32 ? 85  CYS   A N   1 
ATOM   695  C  CA  . CYS   A 1 100 ? -3.138  -25.169 -31.489 1 36.78 ? 85  CYS   A CA  1 
ATOM   696  C  C   . CYS   A 1 100 ? -4.098  -24.445 -32.431 1 36.86 ? 85  CYS   A C   1 
ATOM   697  O  O   . CYS   A 1 100 ? -3.894  -24.438 -33.638 1 36.91 ? 85  CYS   A O   1 
ATOM   698  C  CB  . CYS   A 1 100 ? -3.707  -26.516 -31.05  1 37.12 ? 85  CYS   A CB  1 
ATOM   699  S  SG  . CYS   A 1 100 ? -2.484  -27.619 -30.303 1 39.88 ? 85  CYS   A SG  1 
ATOM   700  N  N   . ILE   A 1 101 ? -5.13   -23.803 -31.872 1 37.22 ? 86  ILE   A N   1 
ATOM   701  C  CA  . ILE   A 1 101 ? -6.085  -23.048 -32.669 1 38.07 ? 86  ILE   A CA  1 
ATOM   702  C  C   . ILE   A 1 101 ? -5.389  -21.884 -33.38  1 38.66 ? 86  ILE   A C   1 
ATOM   703  O  O   . ILE   A 1 101 ? -5.633  -21.68  -34.571 1 40    ? 86  ILE   A O   1 
ATOM   704  C  CB  . ILE   A 1 101 ? -7.304  -22.607 -31.826 1 38.48 ? 86  ILE   A CB  1 
ATOM   705  C  CG1 . ILE   A 1 101 ? -8.091  -23.838 -31.347 1 38.75 ? 86  ILE   A CG1 1 
ATOM   706  C  CG2 . ILE   A 1 101 ? -8.197  -21.675 -32.627 1 39    ? 86  ILE   A CG2 1 
ATOM   707  C  CD1 . ILE   A 1 101 ? -9.131  -23.518 -30.302 1 39.32 ? 86  ILE   A CD1 1 
ATOM   708  N  N   . THR   A 1 102 ? -4.47   -21.179 -32.688 1 37.01 ? 87  THR   A N   1 
ATOM   709  C  CA  . THR   A 1 102 ? -3.725  -20.065 -33.278 1 36.49 ? 87  THR   A CA  1 
ATOM   710  C  C   . THR   A 1 102 ? -2.864  -20.513 -34.456 1 37.61 ? 87  THR   A C   1 
ATOM   711  O  O   . THR   A 1 102 ? -2.899  -19.864 -35.495 1 37.75 ? 87  THR   A O   1 
ATOM   712  C  CB  . THR   A 1 102 ? -2.929  -19.333 -32.194 1 36.31 ? 87  THR   A CB  1 
ATOM   713  O  OG1 . THR   A 1 102 ? -3.854  -18.862 -31.22  1 37.4  ? 87  THR   A OG1 1 
ATOM   714  C  CG2 . THR   A 1 102 ? -2.144  -18.165 -32.725 1 35.69 ? 87  THR   A CG2 1 
ATOM   715  N  N   . MET   A 1 103 ? -2.127  -21.647 -34.327 1 38.1  ? 88  MET   A N   1 
ATOM   716  C  CA  . MET   A 1 103 ? -1.325  -22.169 -35.433 1 39.17 ? 88  MET   A CA  1 
ATOM   717  C  C   . MET   A 1 103 ? -2.219  -22.478 -36.658 1 40.43 ? 88  MET   A C   1 
ATOM   718  O  O   . MET   A 1 103 ? -1.871  -22.11  -37.776 1 40.78 ? 88  MET   A O   1 
ATOM   719  C  CB  . MET   A 1 103 ? -0.541  -23.44  -35.038 1 40.26 ? 88  MET   A CB  1 
ATOM   720  C  CG  . MET   A 1 103 ? 0.496   -23.26  -33.905 1 43.6  ? 88  MET   A CG  1 
ATOM   721  S  SD  . MET   A 1 103 ? 1.45    -21.705 -33.802 1 51.21 ? 88  MET   A SD  1 
ATOM   722  C  CE  . MET   A 1 103 ? 2.498   -21.863 -35.038 1 43.11 ? 88  MET   A CE  1 
ATOM   723  N  N   . ALA   A 1 104 ? -3.373  -23.113 -36.438 1 40.92 ? 89  ALA   A N   1 
ATOM   724  C  CA  . ALA   A 1 104 ? -4.289  -23.446 -37.52  1 42.32 ? 89  ALA   A CA  1 
ATOM   725  C  C   . ALA   A 1 104 ? -4.913  -22.215 -38.148 1 43.22 ? 89  ALA   A C   1 
ATOM   726  O  O   . ALA   A 1 104 ? -5.116  -22.178 -39.359 1 43.64 ? 89  ALA   A O   1 
ATOM   727  C  CB  . ALA   A 1 104 ? -5.378  -24.363 -37.004 1 42.77 ? 89  ALA   A CB  1 
ATOM   728  N  N   . TYR   A 1 105 ? -5.216  -21.204 -37.338 1 43.39 ? 90  TYR   A N   1 
ATOM   729  C  CA  . TYR   A 1 105 ? -5.817  -19.973 -37.829 1 43.57 ? 90  TYR   A CA  1 
ATOM   730  C  C   . TYR   A 1 105 ? -4.82   -19.205 -38.679 1 43.24 ? 90  TYR   A C   1 
ATOM   731  O  O   . TYR   A 1 105 ? -5.158  -18.772 -39.774 1 43.21 ? 90  TYR   A O   1 
ATOM   732  C  CB  . TYR   A 1 105 ? -6.363  -19.106 -36.659 1 43.89 ? 90  TYR   A CB  1 
ATOM   733  C  CG  . TYR   A 1 105 ? -7.135  -17.9   -37.152 1 44.89 ? 90  TYR   A CG  1 
ATOM   734  C  CD1 . TYR   A 1 105 ? -8.491  -17.991 -37.453 1 45.76 ? 90  TYR   A CD1 1 
ATOM   735  C  CD2 . TYR   A 1 105 ? -6.493  -16.694 -37.4   1 45.6  ? 90  TYR   A CD2 1 
ATOM   736  C  CE1 . TYR   A 1 105 ? -9.193  -16.901 -37.953 1 46.36 ? 90  TYR   A CE1 1 
ATOM   737  C  CE2 . TYR   A 1 105 ? -7.175  -15.612 -37.933 1 46.58 ? 90  TYR   A CE2 1 
ATOM   738  C  CZ  . TYR   A 1 105 ? -8.527  -15.717 -38.208 1 47.5  ? 90  TYR   A CZ  1 
ATOM   739  O  OH  . TYR   A 1 105 ? -9.195  -14.621 -38.696 1 49.13 ? 90  TYR   A OH  1 
ATOM   740  N  N   . VAL   A 1 106 ? -3.597  -19.04  -38.184 1 42.83 ? 91  VAL   A N   1 
ATOM   741  C  CA  . VAL   A 1 106 ? -2.567  -18.323 -38.913 1 43.16 ? 91  VAL   A CA  1 
ATOM   742  C  C   . VAL   A 1 106 ? -2.2    -19.044 -40.222 1 44.44 ? 91  VAL   A C   1 
ATOM   743  O  O   . VAL   A 1 106 ? -2.195  -18.419 -41.278 1 45.46 ? 91  VAL   A O   1 
ATOM   744  C  CB  . VAL   A 1 106 ? -1.309  -18.098 -38.017 1 43.24 ? 91  VAL   A CB  1 
ATOM   745  C  CG1 . VAL   A 1 106 ? -0.127  -17.585 -38.827 1 43.17 ? 91  VAL   A CG1 1 
ATOM   746  C  CG2 . VAL   A 1 106 ? -1.616  -17.162 -36.86  1 43.47 ? 91  VAL   A CG2 1 
ATOM   747  N  N   . TRP   A 1 107 ? -1.918  -20.35  -40.16  1 43.89 ? 92  TRP   A N   1 
ATOM   748  C  CA  . TRP   A 1 107 ? -1.426  -21.083 -41.31  1 43.98 ? 92  TRP   A CA  1 
ATOM   749  C  C   . TRP   A 1 107 ? -2.48   -21.662 -42.24  1 44.9  ? 92  TRP   A C   1 
ATOM   750  O  O   . TRP   A 1 107 ? -2.15   -21.962 -43.377 1 45.16 ? 92  TRP   A O   1 
ATOM   751  C  CB  . TRP   A 1 107 ? -0.442  -22.188 -40.857 1 43.39 ? 92  TRP   A CB  1 
ATOM   752  C  CG  . TRP   A 1 107 ? 0.73    -21.675 -40.054 1 43.28 ? 92  TRP   A CG  1 
ATOM   753  C  CD1 . TRP   A 1 107 ? 1.099   -22.065 -38.797 1 43.42 ? 92  TRP   A CD1 1 
ATOM   754  C  CD2 . TRP   A 1 107 ? 1.666   -20.66  -40.449 1 42.96 ? 92  TRP   A CD2 1 
ATOM   755  N  NE1 . TRP   A 1 107 ? 2.198   -21.358 -38.388 1 43.16 ? 92  TRP   A NE1 1 
ATOM   756  C  CE2 . TRP   A 1 107 ? 2.571   -20.491 -39.383 1 43.18 ? 92  TRP   A CE2 1 
ATOM   757  C  CE3 . TRP   A 1 107 ? 1.82    -19.865 -41.6   1 43.75 ? 92  TRP   A CE3 1 
ATOM   758  C  CZ2 . TRP   A 1 107 ? 3.635   -19.592 -39.447 1 43.95 ? 92  TRP   A CZ2 1 
ATOM   759  C  CZ3 . TRP   A 1 107 ? 2.865   -18.957 -41.649 1 44.34 ? 92  TRP   A CZ3 1 
ATOM   760  C  CH2 . TRP   A 1 107 ? 3.756   -18.83  -40.583 1 44.14 ? 92  TRP   A CH2 1 
ATOM   761  N  N   . GLY   A 1 108 ? -3.705  -21.839 -41.766 1 45.66 ? 93  GLY   A N   1 
ATOM   762  C  CA  . GLY   A 1 108 ? -4.787  -22.402 -42.566 1 46.85 ? 93  GLY   A CA  1 
ATOM   763  C  C   . GLY   A 1 108 ? -4.465  -23.783 -43.095 1 48.13 ? 93  GLY   A C   1 
ATOM   764  O  O   . GLY   A 1 108 ? -4.04   -24.646 -42.331 1 47.44 ? 93  GLY   A O   1 
ATOM   765  N  N   . LYS   A 1 109 ? -4.62   -23.994 -44.414 1 49.64 ? 94  LYS   A N   1 
ATOM   766  C  CA  . LYS   A 1 109 ? -4.262  -25.286 -45.019 1 51.66 ? 94  LYS   A CA  1 
ATOM   767  C  C   . LYS   A 1 109 ? -2.741  -25.456 -45.24  1 53.56 ? 94  LYS   A C   1 
ATOM   768  O  O   . LYS   A 1 109 ? -2.307  -26.533 -45.632 1 53.74 ? 94  LYS   A O   1 
ATOM   769  C  CB  . LYS   A 1 109 ? -5.035  -25.541 -46.323 1 53.15 ? 94  LYS   A CB  1 
ATOM   770  C  CG  . LYS   A 1 109 ? -6.541  -25.714 -46.117 1 56.55 ? 94  LYS   A CG  1 
ATOM   771  C  CD  . LYS   A 1 109 ? -7.276  -25.991 -47.425 1 59.63 ? 94  LYS   A CD  1 
ATOM   772  C  CE  . LYS   A 1 109 ? -8.772  -25.893 -47.244 1 63.79 ? 94  LYS   A CE  1 
ATOM   773  N  NZ  . LYS   A 1 109 ? -9.523  -26.39  -48.427 1 66.84 ? 94  LYS   A NZ  1 
ATOM   774  N  N   . GLY   A 1 110 ? -1.964  -24.408 -44.97  1 55.07 ? 95  GLY   A N   1 
ATOM   775  C  CA  . GLY   A 1 110 ? -0.517  -24.408 -45.096 1 57.71 ? 95  GLY   A CA  1 
ATOM   776  C  C   . GLY   A 1 110 ? -0.009  -24.227 -46.508 1 60.41 ? 95  GLY   A C   1 
ATOM   777  O  O   . GLY   A 1 110 ? 1.04    -24.778 -46.851 1 60.87 ? 95  GLY   A O   1 
ATOM   778  N  N   . HIS   A 1 111 ? -0.723  -23.439 -47.336 1 61.95 ? 96  HIS   A N   1 
ATOM   779  C  CA  . HIS   A 1 111 ? -0.305  -23.264 -48.727 1 63.99 ? 96  HIS   A CA  1 
ATOM   780  C  C   . HIS   A 1 111 ? -0.164  -21.819 -49.175 1 64.44 ? 96  HIS   A C   1 
ATOM   781  O  O   . HIS   A 1 111 ? -0.345  -21.525 -50.355 1 64.89 ? 96  HIS   A O   1 
ATOM   782  C  CB  . HIS   A 1 111 ? -1.23   -24.035 -49.677 1 65.87 ? 96  HIS   A CB  1 
ATOM   783  C  CG  . HIS   A 1 111 ? -1.166  -25.512 -49.459 1 69.83 ? 96  HIS   A CG  1 
ATOM   784  N  ND1 . HIS   A 1 111 ? 0.051   -26.182 -49.425 1 71.88 ? 96  HIS   A ND1 1 
ATOM   785  C  CD2 . HIS   A 1 111 ? -2.165  -26.401 -49.248 1 71.44 ? 96  HIS   A CD2 1 
ATOM   786  C  CE1 . HIS   A 1 111 ? -0.247  -27.449 -49.19  1 72.62 ? 96  HIS   A CE1 1 
ATOM   787  N  NE2 . HIS   A 1 111 ? -1.567  -27.632 -49.078 1 72.77 ? 96  HIS   A NE2 1 
ATOM   788  N  N   . GLY   A 1 112 ? 0.215   -20.941 -48.259 1 63.97 ? 97  GLY   A N   1 
ATOM   789  C  CA  . GLY   A 1 112 ? 0.447   -19.546 -48.607 1 63.8  ? 97  GLY   A CA  1 
ATOM   790  C  C   . GLY   A 1 112 ? -0.613  -18.569 -48.157 1 63.4  ? 97  GLY   A C   1 
ATOM   791  O  O   . GLY   A 1 112 ? -0.318  -17.382 -48.022 1 64.02 ? 97  GLY   A O   1 
ATOM   792  N  N   . ASP   A 1 113 ? -1.847  -19.034 -47.933 1 62.59 ? 98  ASP   A N   1 
ATOM   793  C  CA  . ASP   A 1 113 ? -2.903  -18.139 -47.466 1 62.3  ? 98  ASP   A CA  1 
ATOM   794  C  C   . ASP   A 1 113 ? -2.784  -18.013 -45.953 1 61.33 ? 98  ASP   A C   1 
ATOM   795  O  O   . ASP   A 1 113 ? -3.329  -18.83  -45.213 1 61.61 ? 98  ASP   A O   1 
ATOM   796  C  CB  . ASP   A 1 113 ? -4.301  -18.619 -47.877 1 64.26 ? 98  ASP   A CB  1 
ATOM   797  C  CG  . ASP   A 1 113 ? -5.391  -17.645 -47.464 1 69.86 ? 98  ASP   A CG  1 
ATOM   798  O  OD1 . ASP   A 1 113 ? -5.11   -16.413 -47.413 1 70.59 ? 98  ASP   A OD1 1 
ATOM   799  O  OD2 . ASP   A 1 113 ? -6.52   -18.104 -47.189 1 72.5  ? 98  ASP   A OD2 1 
ATOM   800  N  N   . VAL   A 1 114 ? -2.031  -17.016 -45.504 1 60.08 ? 99  VAL   A N   1 
ATOM   801  C  CA  . VAL   A 1 114 ? -1.778  -16.771 -44.086 1 59.29 ? 99  VAL   A CA  1 
ATOM   802  C  C   . VAL   A 1 114 ? -2.783  -15.733 -43.542 1 58.4  ? 99  VAL   A C   1 
ATOM   803  O  O   . VAL   A 1 114 ? -3.458  -15.051 -44.317 1 59.22 ? 99  VAL   A O   1 
ATOM   804  C  CB  . VAL   A 1 114 ? -0.296  -16.31  -43.882 1 59.97 ? 99  VAL   A CB  1 
ATOM   805  C  CG1 . VAL   A 1 114 ? 0.083   -16.179 -42.413 1 60.73 ? 99  VAL   A CG1 1 
ATOM   806  C  CG2 . VAL   A 1 114 ? 0.677   -17.252 -44.575 1 60.62 ? 99  VAL   A CG2 1 
ATOM   807  N  N   . ARG   A 1 115 ? -2.913  -15.651 -42.212 1 56.36 ? 100 ARG   A N   1 
ATOM   808  C  CA  . ARG   A 1 115 ? -3.71   -14.635 -41.536 1 54.66 ? 100 ARG   A CA  1 
ATOM   809  C  C   . ARG   A 1 115 ? -2.717  -13.817 -40.702 1 53.48 ? 100 ARG   A C   1 
ATOM   810  O  O   . ARG   A 1 115 ? -1.946  -14.396 -39.942 1 53.51 ? 100 ARG   A O   1 
ATOM   811  C  CB  . ARG   A 1 115 ? -4.786  -15.258 -40.627 1 54.75 ? 100 ARG   A CB  1 
ATOM   812  C  CG  . ARG   A 1 115 ? -6.037  -15.721 -41.357 1 55.93 ? 100 ARG   A CG  1 
ATOM   813  C  CD  . ARG   A 1 115 ? -6.754  -14.585 -42.085 1 58.52 ? 100 ARG   A CD  1 
ATOM   814  N  NE  . ARG   A 1 115 ? -7.841  -15.057 -42.959 1 60.6  ? 100 ARG   A NE  1 
ATOM   815  C  CZ  . ARG   A 1 115 ? -7.668  -15.473 -44.213 1 61.75 ? 100 ARG   A CZ  1 
ATOM   816  N  NH1 . ARG   A 1 115 ? -6.458  -15.474 -44.761 1 61.4  ? 100 ARG   A NH1 1 
ATOM   817  N  NH2 . ARG   A 1 115 ? -8.702  -15.888 -44.928 1 61.13 ? 100 ARG   A NH2 1 
ATOM   818  N  N   . LYS   A 1 116 ? -2.695  -12.492 -40.865 1 52.32 ? 101 LYS   A N   1 
ATOM   819  C  CA  . LYS   A 1 116 ? -1.745  -11.647 -40.124 1 51.28 ? 101 LYS   A CA  1 
ATOM   820  C  C   . LYS   A 1 116 ? -2.332  -11.012 -38.852 1 50.23 ? 101 LYS   A C   1 
ATOM   821  O  O   . LYS   A 1 116 ? -1.621  -10.315 -38.122 1 50.97 ? 101 LYS   A O   1 
ATOM   822  C  CB  . LYS   A 1 116 ? -1.127  -10.581 -41.041 1 52.57 ? 101 LYS   A CB  1 
ATOM   823  N  N   . VAL   A 1 117 ? -3.624  -11.246 -38.579 1 48.45 ? 102 VAL   A N   1 
ATOM   824  C  CA  . VAL   A 1 117 ? -4.295  -10.701 -37.412 1 47.62 ? 102 VAL   A CA  1 
ATOM   825  C  C   . VAL   A 1 117 ? -5.031  -11.843 -36.729 1 47.71 ? 102 VAL   A C   1 
ATOM   826  O  O   . VAL   A 1 117 ? -5.78   -12.562 -37.386 1 48.23 ? 102 VAL   A O   1 
ATOM   827  C  CB  . VAL   A 1 117 ? -5.3    -9.567  -37.797 1 47.38 ? 102 VAL   A CB  1 
ATOM   828  C  CG1 . VAL   A 1 117 ? -6.076  -9.072  -36.579 1 47.35 ? 102 VAL   A CG1 1 
ATOM   829  C  CG2 . VAL   A 1 117 ? -4.607  -8.406  -38.509 1 47.38 ? 102 VAL   A CG2 1 
ATOM   830  N  N   . LEU   A 1 118 ? -4.838  -12.008 -35.422 1 46.98 ? 103 LEU   A N   1 
ATOM   831  C  CA  . LEU   A 1 118 ? -5.543  -13.027 -34.665 1 46.85 ? 103 LEU   A CA  1 
ATOM   832  C  C   . LEU   A 1 118 ? -6.766  -12.342 -34.031 1 47.6  ? 103 LEU   A C   1 
ATOM   833  O  O   . LEU   A 1 118 ? -6.605  -11.345 -33.34  1 47.98 ? 103 LEU   A O   1 
ATOM   834  C  CB  . LEU   A 1 118 ? -4.615  -13.612 -33.595 1 46.4  ? 103 LEU   A CB  1 
ATOM   835  C  CG  . LEU   A 1 118 ? -5.16   -14.774 -32.798 1 47.73 ? 103 LEU   A CG  1 
ATOM   836  C  CD1 . LEU   A 1 118 ? -5.368  -15.992 -33.679 1 48.4  ? 103 LEU   A CD1 1 
ATOM   837  C  CD2 . LEU   A 1 118 ? -4.245  -15.109 -31.633 1 47.84 ? 103 LEU   A CD2 1 
ATOM   838  N  N   . PRO   A 1 119 ? -7.995  -12.838 -34.284 1 47.58 ? 104 PRO   A N   1 
ATOM   839  C  CA  . PRO   A 1 119 ? -9.191  -12.178 -33.729 1 47.47 ? 104 PRO   A CA  1 
ATOM   840  C  C   . PRO   A 1 119 ? -9.174  -11.974 -32.219 1 47.12 ? 104 PRO   A C   1 
ATOM   841  O  O   . PRO   A 1 119 ? -8.817  -12.882 -31.48  1 46.75 ? 104 PRO   A O   1 
ATOM   842  C  CB  . PRO   A 1 119 ? -10.355 -13.088 -34.17  1 48.36 ? 104 PRO   A CB  1 
ATOM   843  C  CG  . PRO   A 1 119 ? -9.834  -13.848 -35.341 1 48.84 ? 104 PRO   A CG  1 
ATOM   844  C  CD  . PRO   A 1 119 ? -8.347  -14.01  -35.104 1 47.08 ? 104 PRO   A CD  1 
ATOM   845  N  N   . ARG   A 1 120 ? -9.614  -10.785 -31.768 1 46.63 ? 105 ARG   A N   1 
ATOM   846  C  CA  . ARG   A 1 120 ? -9.66   -10.39  -30.369 1 46.57 ? 105 ARG   A CA  1 
ATOM   847  C  C   . ARG   A 1 120 ? -10.317 -11.399 -29.46  1 47.04 ? 105 ARG   A C   1 
ATOM   848  O  O   . ARG   A 1 120 ? -9.88   -11.551 -28.327 1 47.28 ? 105 ARG   A O   1 
ATOM   849  C  CB  . ARG   A 1 120 ? -10.34  -9.019  -30.205 1 47.14 ? 105 ARG   A CB  1 
ATOM   850  C  CG  . ARG   A 1 120 ? -11.85  -9.046  -30.41  1 47.79 ? 105 ARG   A CG  1 
ATOM   851  C  CD  . ARG   A 1 120 ? -12.488 -7.696  -30.303 1 47.35 ? 105 ARG   A CD  1 
ATOM   852  N  NE  . ARG   A 1 120 ? -12.017 -6.828  -31.376 1 46.28 ? 105 ARG   A NE  1 
ATOM   853  C  CZ  . ARG   A 1 120 ? -11.167 -5.823  -31.212 1 44.2  ? 105 ARG   A CZ  1 
ATOM   854  N  NH1 . ARG   A 1 120 ? -10.794 -5.092  -32.249 1 41.51 ? 105 ARG   A NH1 1 
ATOM   855  N  NH2 . ARG   A 1 120 ? -10.688 -5.537  -30.005 1 42.76 ? 105 ARG   A NH2 1 
ATOM   856  N  N   . ASN   A 1 121 ? -11.361 -12.086 -29.93  1 47.54 ? 106 ASN   A N   1 
ATOM   857  C  CA  . ASN   A 1 121 ? -12.078 -13.059 -29.1   1 48.68 ? 106 ASN   A CA  1 
ATOM   858  C  C   . ASN   A 1 121 ? -11.229 -14.294 -28.741 1 47.96 ? 106 ASN   A C   1 
ATOM   859  O  O   . ASN   A 1 121 ? -11.577 -15.008 -27.805 1 47.84 ? 106 ASN   A O   1 
ATOM   860  C  CB  . ASN   A 1 121 ? -13.427 -13.448 -29.718 1 51.61 ? 106 ASN   A CB  1 
ATOM   861  C  CG  . ASN   A 1 121 ? -14.443 -12.311 -29.859 1 58.32 ? 106 ASN   A CG  1 
ATOM   862  O  OD1 . ASN   A 1 121 ? -15.455 -12.435 -30.58  1 60.96 ? 106 ASN   A OD1 1 
ATOM   863  N  ND2 . ASN   A 1 121 ? -14.245 -11.195 -29.146 1 59.17 ? 106 ASN   A ND2 1 
ATOM   864  N  N   . ILE   A 1 122 ? -10.094 -14.509 -29.445 1 47.36 ? 107 ILE   A N   1 
ATOM   865  C  CA  . ILE   A 1 122 ? -9.174  -15.586 -29.145 1 47.43 ? 107 ILE   A CA  1 
ATOM   866  C  C   . ILE   A 1 122 ? -7.825  -15.003 -28.654 1 46.17 ? 107 ILE   A C   1 
ATOM   867  O  O   . ILE   A 1 122 ? -7.31   -15.474 -27.64  1 46.62 ? 107 ILE   A O   1 
ATOM   868  C  CB  . ILE   A 1 122 ? -9.049  -16.646 -30.284 1 48.97 ? 107 ILE   A CB  1 
ATOM   869  C  CG1 . ILE   A 1 122 ? -8.311  -17.875 -29.788 1 51.1  ? 107 ILE   A CG1 1 
ATOM   870  C  CG2 . ILE   A 1 122 ? -8.406  -16.104 -31.554 1 49.61 ? 107 ILE   A CG2 1 
ATOM   871  C  CD1 . ILE   A 1 122 ? -8.398  -19.006 -30.682 1 53.04 ? 107 ILE   A CD1 1 
ATOM   872  N  N   . ALA   A 1 123 ? -7.323  -13.926 -29.287 1 44.48 ? 108 ALA   A N   1 
ATOM   873  C  CA  . ALA   A 1 123 ? -6.074  -13.254 -28.911 1 43.85 ? 108 ALA   A CA  1 
ATOM   874  C  C   . ALA   A 1 123 ? -6.085  -12.647 -27.509 1 44.48 ? 108 ALA   A C   1 
ATOM   875  O  O   . ALA   A 1 123 ? -5.076  -12.758 -26.804 1 44.99 ? 108 ALA   A O   1 
ATOM   876  C  CB  . ALA   A 1 123 ? -5.709  -12.184 -29.925 1 43.43 ? 108 ALA   A CB  1 
ATOM   877  N  N   . VAL   A 1 124 ? -7.2    -11.999 -27.093 1 43.71 ? 109 VAL   A N   1 
ATOM   878  C  CA  . VAL   A 1 124 ? -7.256  -11.408 -25.757 1 43.51 ? 109 VAL   A CA  1 
ATOM   879  C  C   . VAL   A 1 124 ? -7.13   -12.507 -24.677 1 43.14 ? 109 VAL   A C   1 
ATOM   880  O  O   . VAL   A 1 124 ? -6.153  -12.464 -23.932 1 43.52 ? 109 VAL   A O   1 
ATOM   881  C  CB  . VAL   A 1 124 ? -8.465  -10.433 -25.53  1 43.99 ? 109 VAL   A CB  1 
ATOM   882  C  CG1 . VAL   A 1 124 ? -8.694  -10.151 -24.044 1 44.13 ? 109 VAL   A CG1 1 
ATOM   883  C  CG2 . VAL   A 1 124 ? -8.274  -9.13   -26.305 1 44.07 ? 109 VAL   A CG2 1 
ATOM   884  N  N   . PRO   A 1 125 ? -7.995  -13.552 -24.638 1 42.5  ? 110 PRO   A N   1 
ATOM   885  C  CA  . PRO   A 1 125 ? -7.82   -14.586 -23.598 1 42.41 ? 110 PRO   A CA  1 
ATOM   886  C  C   . PRO   A 1 125 ? -6.529  -15.4   -23.729 1 42.64 ? 110 PRO   A C   1 
ATOM   887  O  O   . PRO   A 1 125 ? -6.053  -15.939 -22.738 1 42.41 ? 110 PRO   A O   1 
ATOM   888  C  CB  . PRO   A 1 125 ? -9.076  -15.456 -23.731 1 42.98 ? 110 PRO   A CB  1 
ATOM   889  C  CG  . PRO   A 1 125 ? -9.608  -15.178 -25.078 1 43.43 ? 110 PRO   A CG  1 
ATOM   890  C  CD  . PRO   A 1 125 ? -9.217  -13.789 -25.436 1 41.6  ? 110 PRO   A CD  1 
ATOM   891  N  N   . TYR   A 1 126 ? -5.952  -15.476 -24.942 1 42.51 ? 111 TYR   A N   1 
ATOM   892  C  CA  . TYR   A 1 126 ? -4.714  -16.219 -25.147 1 42.11 ? 111 TYR   A CA  1 
ATOM   893  C  C   . TYR   A 1 126 ? -3.572  -15.445 -24.519 1 42.65 ? 111 TYR   A C   1 
ATOM   894  O  O   . TYR   A 1 126 ? -2.801  -16.017 -23.749 1 42.61 ? 111 TYR   A O   1 
ATOM   895  C  CB  . TYR   A 1 126 ? -4.461  -16.466 -26.639 1 41.03 ? 111 TYR   A CB  1 
ATOM   896  C  CG  . TYR   A 1 126 ? -3.306  -17.395 -26.941 1 39.94 ? 111 TYR   A CG  1 
ATOM   897  C  CD1 . TYR   A 1 126 ? -2.952  -18.401 -26.061 1 40.17 ? 111 TYR   A CD1 1 
ATOM   898  C  CD2 . TYR   A 1 126 ? -2.628  -17.323 -28.151 1 39.8  ? 111 TYR   A CD2 1 
ATOM   899  C  CE1 . TYR   A 1 126 ? -1.914  -19.275 -26.346 1 40.55 ? 111 TYR   A CE1 1 
ATOM   900  C  CE2 . TYR   A 1 126 ? -1.628  -18.226 -28.472 1 40.27 ? 111 TYR   A CE2 1 
ATOM   901  C  CZ  . TYR   A 1 126 ? -1.266  -19.197 -27.561 1 41.15 ? 111 TYR   A CZ  1 
ATOM   902  O  OH  . TYR   A 1 126 ? -0.269  -20.088 -27.864 1 42.25 ? 111 TYR   A OH  1 
ATOM   903  N  N   . CYS   A 1 127 ? -3.494  -14.14  -24.798 1 43.03 ? 112 CYS   A N   1 
ATOM   904  C  CA  . CYS   A 1 127 ? -2.443  -13.311 -24.24  1 43.76 ? 112 CYS   A CA  1 
ATOM   905  C  C   . CYS   A 1 127 ? -2.596  -13.123 -22.735 1 45.01 ? 112 CYS   A C   1 
ATOM   906  O  O   . CYS   A 1 127 ? -1.581  -13.036 -22.049 1 45.71 ? 112 CYS   A O   1 
ATOM   907  C  CB  . CYS   A 1 127 ? -2.371  -11.974 -24.948 1 43.71 ? 112 CYS   A CB  1 
ATOM   908  S  SG  . CYS   A 1 127 ? -1.956  -12.079 -26.693 1 44.84 ? 112 CYS   A SG  1 
ATOM   909  N  N   . GLN   A 1 128 ? -3.835  -13.069 -22.22  1 45.05 ? 113 GLN   A N   1 
ATOM   910  C  CA  . GLN   A 1 128 ? -4.039  -12.923 -20.776 1 46.02 ? 113 GLN   A CA  1 
ATOM   911  C  C   . GLN   A 1 128 ? -3.566  -14.181 -20.027 1 46.19 ? 113 GLN   A C   1 
ATOM   912  O  O   . GLN   A 1 128 ? -2.895  -14.09  -19.005 1 45.88 ? 113 GLN   A O   1 
ATOM   913  C  CB  . GLN   A 1 128 ? -5.509  -12.634 -20.442 1 47.43 ? 113 GLN   A CB  1 
ATOM   914  C  CG  . GLN   A 1 128 ? -6.016  -11.29  -20.927 1 51.58 ? 113 GLN   A CG  1 
ATOM   915  C  CD  . GLN   A 1 128 ? -7.512  -11.168 -20.696 1 57.58 ? 113 GLN   A CD  1 
ATOM   916  O  OE1 . GLN   A 1 128 ? -8.262  -12.165 -20.597 1 58.48 ? 113 GLN   A OE1 1 
ATOM   917  N  NE2 . GLN   A 1 128 ? -7.979  -9.93   -20.598 1 58.87 ? 113 GLN   A NE2 1 
ATOM   918  N  N   . LEU   A 1 129 ? -3.917  -15.349 -20.552 1 46.3  ? 114 LEU   A N   1 
ATOM   919  C  CA  . LEU   A 1 129 ? -3.526  -16.626 -19.989 1 46.94 ? 114 LEU   A CA  1 
ATOM   920  C  C   . LEU   A 1 129 ? -2.002  -16.833 -20.125 1 46.96 ? 114 LEU   A C   1 
ATOM   921  O  O   . LEU   A 1 129 ? -1.388  -17.401 -19.233 1 47.39 ? 114 LEU   A O   1 
ATOM   922  C  CB  . LEU   A 1 129 ? -4.282  -17.692 -20.757 1 48.12 ? 114 LEU   A CB  1 
ATOM   923  C  CG  . LEU   A 1 129 ? -4.079  -19.105 -20.355 1 51.16 ? 114 LEU   A CG  1 
ATOM   924  C  CD1 . LEU   A 1 129 ? -4.613  -19.346 -18.965 1 52.5  ? 114 LEU   A CD1 1 
ATOM   925  C  CD2 . LEU   A 1 129 ? -4.755  -20.012 -21.343 1 52.05 ? 114 LEU   A CD2 1 
ATOM   926  N  N   . SER   A 1 130 ? -1.396  -16.334 -21.211 1 46.48 ? 115 SER   A N   1 
ATOM   927  C  CA  . SER   A 1 130 ? 0.033   -16.42  -21.467 1 47.2  ? 115 SER   A CA  1 
ATOM   928  C  C   . SER   A 1 130 ? 0.8     -15.566 -20.473 1 48.99 ? 115 SER   A C   1 
ATOM   929  O  O   . SER   A 1 130 ? 1.826   -16.004 -19.969 1 49.3  ? 115 SER   A O   1 
ATOM   930  C  CB  . SER   A 1 130 ? 0.355   -15.994 -22.899 1 46.89 ? 115 SER   A CB  1 
ATOM   931  O  OG  . SER   A 1 130 ? -0.213  -16.885 -23.846 1 47.41 ? 115 SER   A OG  1 
ATOM   932  N  N   . LYS   A 1 131 ? 0.302   -14.349 -20.19  1 49.92 ? 116 LYS   A N   1 
ATOM   933  C  CA  . LYS   A 1 131 ? 0.878   -13.41  -19.223 1 51.06 ? 116 LYS   A CA  1 
ATOM   934  C  C   . LYS   A 1 131 ? 0.835   -14.028 -17.811 1 51.46 ? 116 LYS   A C   1 
ATOM   935  O  O   . LYS   A 1 131 ? 1.8     -13.91  -17.052 1 52.6  ? 116 LYS   A O   1 
ATOM   936  C  CB  . LYS   A 1 131 ? 0.072   -12.098 -19.255 1 54.05 ? 116 LYS   A CB  1 
ATOM   937  C  CG  . LYS   A 1 131 ? 0.498   -11.046 -18.238 1 59.22 ? 116 LYS   A CG  1 
ATOM   938  C  CD  . LYS   A 1 131 ? -0.434  -9.829  -18.261 1 64.22 ? 116 LYS   A CD  1 
ATOM   939  C  CE  . LYS   A 1 131 ? -0.008  -8.792  -17.257 1 68.22 ? 116 LYS   A CE  1 
ATOM   940  N  NZ  . LYS   A 1 131 ? 1.467   -8.605  -17.292 1 71.41 ? 116 LYS   A NZ  1 
ATOM   941  N  N   . LYS   A 1 132 ? -0.265  -14.722 -17.488 1 50.44 ? 117 LYS   A N   1 
ATOM   942  C  CA  . LYS   A 1 132 ? -0.475  -15.399 -16.217 1 50.61 ? 117 LYS   A CA  1 
ATOM   943  C  C   . LYS   A 1 132 ? 0.562   -16.528 -16.015 1 50.56 ? 117 LYS   A C   1 
ATOM   944  O  O   . LYS   A 1 132 ? 1.136   -16.662 -14.933 1 50.88 ? 117 LYS   A O   1 
ATOM   945  C  CB  . LYS   A 1 132 ? -1.91   -15.947 -16.169 1 52.35 ? 117 LYS   A CB  1 
ATOM   946  C  CG  . LYS   A 1 132 ? -2.495  -16.139 -14.776 1 57.4  ? 117 LYS   A CG  1 
ATOM   947  C  CD  . LYS   A 1 132 ? -4.031  -16.18  -14.814 1 62.42 ? 117 LYS   A CD  1 
ATOM   948  C  CE  . LYS   A 1 132 ? -4.674  -16.02  -13.444 1 66.45 ? 117 LYS   A CE  1 
ATOM   949  N  NZ  . LYS   A 1 132 ? -6.146  -15.759 -13.543 1 67.76 ? 117 LYS   A NZ  1 
ATOM   950  N  N   . LEU   A 1 133 ? 0.815   -17.321 -17.063 1 49.64 ? 118 LEU   A N   1 
ATOM   951  C  CA  . LEU   A 1 133 ? 1.763   -18.428 -16.986 1 48.83 ? 118 LEU   A CA  1 
ATOM   952  C  C   . LEU   A 1 133 ? 3.2     -18.064 -17.359 1 48.81 ? 118 LEU   A C   1 
ATOM   953  O  O   . LEU   A 1 133 ? 4.058   -18.949 -17.351 1 49.24 ? 118 LEU   A O   1 
ATOM   954  C  CB  . LEU   A 1 133 ? 1.274   -19.595 -17.851 1 48.21 ? 118 LEU   A CB  1 
ATOM   955  C  CG  . LEU   A 1 133 ? 0.001   -20.269 -17.38  1 48.19 ? 118 LEU   A CG  1 
ATOM   956  C  CD1 . LEU   A 1 133 ? -0.604  -21.07  -18.473 1 48.49 ? 118 LEU   A CD1 1 
ATOM   957  C  CD2 . LEU   A 1 133 ? 0.269   -21.171 -16.229 1 48.41 ? 118 LEU   A CD2 1 
ATOM   958  N  N   . GLU   A 1 134 ? 3.467   -16.777 -17.665 1 48.32 ? 119 GLU   A N   1 
ATOM   959  C  CA  . GLU   A 1 134 ? 4.777   -16.262 -18.058 1 48.34 ? 119 GLU   A CA  1 
ATOM   960  C  C   . GLU   A 1 134 ? 5.35    -16.982 -19.265 1 48.04 ? 119 GLU   A C   1 
ATOM   961  O  O   . GLU   A 1 134 ? 6.531   -17.329 -19.31  1 48.48 ? 119 GLU   A O   1 
ATOM   962  C  CB  . GLU   A 1 134 ? 5.767   -16.259 -16.901 1 50.54 ? 119 GLU   A CB  1 
ATOM   963  C  CG  . GLU   A 1 134 ? 5.341   -15.396 -15.743 1 54.6  ? 119 GLU   A CG  1 
ATOM   964  C  CD  . GLU   A 1 134 ? 6.431   -15.281 -14.702 1 60.21 ? 119 GLU   A CD  1 
ATOM   965  O  OE1 . GLU   A 1 134 ? 7.528   -14.774 -15.035 1 58.32 ? 119 GLU   A OE1 1 
ATOM   966  O  OE2 . GLU   A 1 134 ? 6.19    -15.716 -13.553 1 64.93 ? 119 GLU   A OE2 1 
ATOM   967  N  N   . LEU   A 1 135 ? 4.499   -17.21  -20.249 1 46.9  ? 120 LEU   A N   1 
ATOM   968  C  CA  . LEU   A 1 135 ? 4.886   -17.86  -21.489 1 46.35 ? 120 LEU   A CA  1 
ATOM   969  C  C   . LEU   A 1 135 ? 4.416   -16.976 -22.653 1 45.62 ? 120 LEU   A C   1 
ATOM   970  O  O   . LEU   A 1 135 ? 3.416   -16.27  -22.526 1 46.79 ? 120 LEU   A O   1 
ATOM   971  C  CB  . LEU   A 1 135 ? 4.239   -19.258 -21.556 1 46.08 ? 120 LEU   A CB  1 
ATOM   972  C  CG  . LEU   A 1 135 ? 4.878   -20.317 -20.677 1 46.8  ? 120 LEU   A CG  1 
ATOM   973  C  CD1 . LEU   A 1 135 ? 3.987   -21.551 -20.574 1 47.52 ? 120 LEU   A CD1 1 
ATOM   974  C  CD2 . LEU   A 1 135 ? 6.244   -20.669 -21.189 1 46.82 ? 120 LEU   A CD2 1 
ATOM   975  N  N   . PRO   A 1 136 ? 5.128   -16.981 -23.783 1 43.8  ? 121 PRO   A N   1 
ATOM   976  C  CA  . PRO   A 1 136 ? 4.688   -16.169 -24.925 1 43.16 ? 121 PRO   A CA  1 
ATOM   977  C  C   . PRO   A 1 136 ? 3.398   -16.689 -25.574 1 42.59 ? 121 PRO   A C   1 
ATOM   978  O  O   . PRO   A 1 136 ? 3.082   -17.879 -25.468 1 42.88 ? 121 PRO   A O   1 
ATOM   979  C  CB  . PRO   A 1 136 ? 5.871   -16.26  -25.887 1 44.05 ? 121 PRO   A CB  1 
ATOM   980  C  CG  . PRO   A 1 136 ? 6.537   -17.531 -25.557 1 44.39 ? 121 PRO   A CG  1 
ATOM   981  C  CD  . PRO   A 1 136 ? 6.346   -17.751 -24.093 1 43    ? 121 PRO   A CD  1 
ATOM   982  N  N   . PRO   A 1 137 ? 2.613   -15.812 -26.221 1 41.55 ? 122 PRO   A N   1 
ATOM   983  C  CA  . PRO   A 1 137 ? 1.357   -16.273 -26.844 1 41.12 ? 122 PRO   A CA  1 
ATOM   984  C  C   . PRO   A 1 137 ? 1.585   -16.936 -28.214 1 40.67 ? 122 PRO   A C   1 
ATOM   985  O  O   . PRO   A 1 137 ? 1.195   -16.424 -29.263 1 41.1  ? 122 PRO   A O   1 
ATOM   986  C  CB  . PRO   A 1 137 ? 0.516   -14.993 -26.942 1 41.63 ? 122 PRO   A CB  1 
ATOM   987  C  CG  . PRO   A 1 137 ? 1.537   -13.912 -27.106 1 42.39 ? 122 PRO   A CG  1 
ATOM   988  C  CD  . PRO   A 1 137 ? 2.788   -14.355 -26.364 1 40.92 ? 122 PRO   A CD  1 
ATOM   989  N  N   . ILE   A 1 138 ? 2.217   -18.101 -28.18  1 38.87 ? 123 ILE   A N   1 
ATOM   990  C  CA  . ILE   A 1 138 ? 2.53    -18.977 -29.303 1 37.08 ? 123 ILE   A CA  1 
ATOM   991  C  C   . ILE   A 1 138 ? 2.704   -20.37  -28.706 1 36    ? 123 ILE   A C   1 
ATOM   992  O  O   . ILE   A 1 138 ? 3.054   -20.518 -27.519 1 36.5  ? 123 ILE   A O   1 
ATOM   993  C  CB  . ILE   A 1 138 ? 3.759   -18.527 -30.15  1 37.07 ? 123 ILE   A CB  1 
ATOM   994  C  CG1 . ILE   A 1 138 ? 3.817   -19.276 -31.498 1 37.34 ? 123 ILE   A CG1 1 
ATOM   995  C  CG2 . ILE   A 1 138 ? 5.078   -18.65  -29.377 1 37.74 ? 123 ILE   A CG2 1 
ATOM   996  C  CD1 . ILE   A 1 138 ? 4.842   -18.791 -32.473 1 38.16 ? 123 ILE   A CD1 1 
ATOM   997  N  N   . LEU   A 1 139 ? 2.424   -21.398 -29.499 1 34.2  ? 124 LEU   A N   1 
ATOM   998  C  CA  . LEU   A 1 139 ? 2.572   -22.772 -29.063 1 33.61 ? 124 LEU   A CA  1 
ATOM   999  C  C   . LEU   A 1 139 ? 4.055   -23.059 -28.766 1 32.92 ? 124 LEU   A C   1 
ATOM   1000 O  O   . LEU   A 1 139 ? 4.914   -22.786 -29.594 1 32.83 ? 124 LEU   A O   1 
ATOM   1001 C  CB  . LEU   A 1 139 ? 2.073   -23.71  -30.173 1 33.74 ? 124 LEU   A CB  1 
ATOM   1002 C  CG  . LEU   A 1 139 ? 1.896   -25.158 -29.782 1 34.37 ? 124 LEU   A CG  1 
ATOM   1003 C  CD1 . LEU   A 1 139 ? 0.714   -25.311 -28.802 1 34.22 ? 124 LEU   A CD1 1 
ATOM   1004 C  CD2 . LEU   A 1 139 ? 1.658   -26.003 -31.015 1 35    ? 124 LEU   A CD2 1 
ATOM   1005 N  N   . VAL   A 1 140 ? 4.348   -23.512 -27.557 1 32.48 ? 125 VAL   A N   1 
ATOM   1006 C  CA  . VAL   A 1 140 ? 5.718   -23.84  -27.156 1 32.8  ? 125 VAL   A CA  1 
ATOM   1007 C  C   . VAL   A 1 140 ? 5.844   -25.348 -26.902 1 33.37 ? 125 VAL   A C   1 
ATOM   1008 O  O   . VAL   A 1 140 ? 4.839   -26.059 -26.885 1 33.95 ? 125 VAL   A O   1 
ATOM   1009 C  CB  . VAL   A 1 140 ? 6.196   -22.994 -25.932 1 32.97 ? 125 VAL   A CB  1 
ATOM   1010 C  CG1 . VAL   A 1 140 ? 6.179   -21.496 -26.237 1 33.21 ? 125 VAL   A CG1 1 
ATOM   1011 C  CG2 . VAL   A 1 140 ? 5.405   -23.312 -24.666 1 32.8  ? 125 VAL   A CG2 1 
ATOM   1012 N  N   . TYR   A 1 141 ? 7.068   -25.846 -26.729 1 33.32 ? 126 TYR   A N   1 
ATOM   1013 C  CA  . TYR   A 1 141 ? 7.36    -27.241 -26.41  1 33.36 ? 126 TYR   A CA  1 
ATOM   1014 C  C   . TYR   A 1 141 ? 6.614   -27.721 -25.126 1 32.71 ? 126 TYR   A C   1 
ATOM   1015 O  O   . TYR   A 1 141 ? 6.083   -28.841 -25.097 1 33.1  ? 126 TYR   A O   1 
ATOM   1016 C  CB  . TYR   A 1 141 ? 8.878   -27.352 -26.225 1 33.81 ? 126 TYR   A CB  1 
ATOM   1017 C  CG  . TYR   A 1 141 ? 9.387   -28.746 -25.971 1 34.16 ? 126 TYR   A CG  1 
ATOM   1018 C  CD1 . TYR   A 1 141 ? 9.68    -29.601 -27.025 1 34.72 ? 126 TYR   A CD1 1 
ATOM   1019 C  CD2 . TYR   A 1 141 ? 9.649   -29.184 -24.68  1 34.56 ? 126 TYR   A CD2 1 
ATOM   1020 C  CE1 . TYR   A 1 141 ? 10.199  -30.866 -26.798 1 35.57 ? 126 TYR   A CE1 1 
ATOM   1021 C  CE2 . TYR   A 1 141 ? 10.149  -30.451 -24.44  1 35.23 ? 126 TYR   A CE2 1 
ATOM   1022 C  CZ  . TYR   A 1 141 ? 10.43   -31.287 -25.502 1 36.25 ? 126 TYR   A CZ  1 
ATOM   1023 O  OH  . TYR   A 1 141 ? 10.938  -32.533 -25.274 1 37.93 ? 126 TYR   A OH  1 
ATOM   1024 N  N   . ALA   A 1 142 ? 6.549   -26.88  -24.084 1 31.42 ? 127 ALA   A N   1 
ATOM   1025 C  CA  . ALA   A 1 142 ? 5.815   -27.22  -22.859 1 31.57 ? 127 ALA   A CA  1 
ATOM   1026 C  C   . ALA   A 1 142 ? 4.299   -27.394 -23.092 1 32.05 ? 127 ALA   A C   1 
ATOM   1027 O  O   . ALA   A 1 142 ? 3.629   -28.014 -22.271 1 32.71 ? 127 ALA   A O   1 
ATOM   1028 C  CB  . ALA   A 1 142 ? 6.053   -26.171 -21.781 1 31.98 ? 127 ALA   A CB  1 
ATOM   1029 N  N   . ASP   A 1 143 ? 3.763   -26.865 -24.201 1 31.33 ? 128 ASP   A N   1 
ATOM   1030 C  CA  . ASP   A 1 143 ? 2.371   -27.063 -24.563 1 31.33 ? 128 ASP   A CA  1 
ATOM   1031 C  C   . ASP   A 1 143 ? 2.243   -28.334 -25.41  1 32.08 ? 128 ASP   A C   1 
ATOM   1032 O  O   . ASP   A 1 143 ? 1.623   -29.297 -24.958 1 32.32 ? 128 ASP   A O   1 
ATOM   1033 C  CB  . ASP   A 1 143 ? 1.804   -25.882 -25.373 1 32.1  ? 128 ASP   A CB  1 
ATOM   1034 C  CG  . ASP   A 1 143 ? 1.849   -24.531 -24.719 1 34.73 ? 128 ASP   A CG  1 
ATOM   1035 O  OD1 . ASP   A 1 143 ? 1.527   -24.442 -23.511 1 34.79 ? 128 ASP   A OD1 1 
ATOM   1036 O  OD2 . ASP   A 1 143 ? 2.157   -23.559 -25.419 1 36.31 ? 128 ASP   A OD2 1 
ATOM   1037 N  N   . CYS   A 1 144 ? 2.852   -28.364 -26.623 1 32.26 ? 129 CYS   A N   1 
ATOM   1038 C  CA  . CYS   A 1 144 ? 2.655   -29.471 -27.559 1 32.38 ? 129 CYS   A CA  1 
ATOM   1039 C  C   . CYS   A 1 144 ? 3.335   -30.768 -27.165 1 32.79 ? 129 CYS   A C   1 
ATOM   1040 O  O   . CYS   A 1 144 ? 2.975   -31.79  -27.735 1 33.92 ? 129 CYS   A O   1 
ATOM   1041 C  CB  . CYS   A 1 144 ? 2.997   -29.072 -28.995 1 32.54 ? 129 CYS   A CB  1 
ATOM   1042 S  SG  . CYS   A 1 144 ? 4.718   -28.553 -29.256 1 35.72 ? 129 CYS   A SG  1 
ATOM   1043 N  N   . VAL   A 1 145 ? 4.267   -30.774 -26.215 1 32.52 ? 130 VAL   A N   1 
ATOM   1044 C  CA  . VAL   A 1 145 ? 4.908   -32.022 -25.8   1 33.37 ? 130 VAL   A CA  1 
ATOM   1045 C  C   . VAL   A 1 145 ? 4.62    -32.336 -24.332 1 34.24 ? 130 VAL   A C   1 
ATOM   1046 O  O   . VAL   A 1 145 ? 4.011   -33.356 -24.027 1 34.54 ? 130 VAL   A O   1 
ATOM   1047 C  CB  . VAL   A 1 145 ? 6.439   -32.096 -26.136 1 33.75 ? 130 VAL   A CB  1 
ATOM   1048 C  CG1 . VAL   A 1 145 ? 7.077   -33.345 -25.528 1 33.8  ? 130 VAL   A CG1 1 
ATOM   1049 C  CG2 . VAL   A 1 145 ? 6.686   -32.044 -27.65  1 33.37 ? 130 VAL   A CG2 1 
ATOM   1050 N  N   . LEU   A 1 146 ? 4.994   -31.43  -23.435 1 34.22 ? 131 LEU   A N   1 
ATOM   1051 C  CA  . LEU   A 1 146 ? 4.888   -31.652 -21.994 1 33.9  ? 131 LEU   A CA  1 
ATOM   1052 C  C   . LEU   A 1 146 ? 3.475   -31.7   -21.449 1 34.41 ? 131 LEU   A C   1 
ATOM   1053 O  O   . LEU   A 1 146 ? 3.246   -32.411 -20.482 1 35.1  ? 131 LEU   A O   1 
ATOM   1054 C  CB  . LEU   A 1 146 ? 5.717   -30.618 -21.228 1 32.93 ? 131 LEU   A CB  1 
ATOM   1055 C  CG  . LEU   A 1 146 ? 7.166   -30.421 -21.704 1 33.08 ? 131 LEU   A CG  1 
ATOM   1056 C  CD1 . LEU   A 1 146 ? 7.863   -29.365 -20.878 1 32.58 ? 131 LEU   A CD1 1 
ATOM   1057 C  CD2 . LEU   A 1 146 ? 7.957   -31.742 -21.664 1 33.67 ? 131 LEU   A CD2 1 
ATOM   1058 N  N   . ALA   A 1 147 ? 2.529   -30.973 -22.049 1 34.28 ? 132 ALA   A N   1 
ATOM   1059 C  CA  . ALA   A 1 147 ? 1.132   -30.99  -21.58  1 34.42 ? 132 ALA   A CA  1 
ATOM   1060 C  C   . ALA   A 1 147 ? 0.141   -31.626 -22.584 1 34.67 ? 132 ALA   A C   1 
ATOM   1061 O  O   . ALA   A 1 147 ? -1.052  -31.695 -22.295 1 34.81 ? 132 ALA   A O   1 
ATOM   1062 C  CB  . ALA   A 1 147 ? 0.679   -29.58  -21.234 1 34.2  ? 132 ALA   A CB  1 
ATOM   1063 N  N   . ASN   A 1 148 ? 0.63    -32.071 -23.76  1 34.22 ? 133 ASN   A N   1 
ATOM   1064 C  CA  . ASN   A 1 148 ? -0.189  -32.649 -24.82  1 34.51 ? 133 ASN   A CA  1 
ATOM   1065 C  C   . ASN   A 1 148 ? -0.227  -34.179 -24.745 1 34.95 ? 133 ASN   A C   1 
ATOM   1066 O  O   . ASN   A 1 148 ? -0.002  -34.855 -25.746 1 34.33 ? 133 ASN   A O   1 
ATOM   1067 C  CB  . ASN   A 1 148 ? 0.351   -32.181 -26.165 1 34.94 ? 133 ASN   A CB  1 
ATOM   1068 C  CG  . ASN   A 1 148 ? -0.555  -32.363 -27.343 1 37.12 ? 133 ASN   A CG  1 
ATOM   1069 O  OD1 . ASN   A 1 148 ? -1.757  -32.582 -27.209 1 38.44 ? 133 ASN   A OD1 1 
ATOM   1070 N  ND2 . ASN   A 1 148 ? 0.018   -32.282 -28.529 1 36.93 ? 133 ASN   A ND2 1 
ATOM   1071 N  N   . TRP   A 1 149 ? -0.563  -34.725 -23.566 1 35.53 ? 134 TRP   A N   1 
ATOM   1072 C  CA  . TRP   A 1 149 ? -0.584  -36.167 -23.422 1 36.91 ? 134 TRP   A CA  1 
ATOM   1073 C  C   . TRP   A 1 149 ? -1.557  -36.683 -22.369 1 38.47 ? 134 TRP   A C   1 
ATOM   1074 O  O   . TRP   A 1 149 ? -1.984  -35.944 -21.512 1 38.39 ? 134 TRP   A O   1 
ATOM   1075 C  CB  . TRP   A 1 149 ? 0.849   -36.669 -23.161 1 36.3  ? 134 TRP   A CB  1 
ATOM   1076 C  CG  . TRP   A 1 149 ? 1.389   -36.296 -21.82  1 36.28 ? 134 TRP   A CG  1 
ATOM   1077 C  CD1 . TRP   A 1 149 ? 1.987   -35.122 -21.462 1 36.91 ? 134 TRP   A CD1 1 
ATOM   1078 C  CD2 . TRP   A 1 149 ? 1.403   -37.13  -20.657 1 36.87 ? 134 TRP   A CD2 1 
ATOM   1079 N  NE1 . TRP   A 1 149 ? 2.343   -35.162 -20.128 1 37.31 ? 134 TRP   A NE1 1 
ATOM   1080 C  CE2 . TRP   A 1 149 ? 2.011   -36.396 -19.618 1 37.37 ? 134 TRP   A CE2 1 
ATOM   1081 C  CE3 . TRP   A 1 149 ? 0.983   -38.444 -20.401 1 37.89 ? 134 TRP   A CE3 1 
ATOM   1082 C  CZ2 . TRP   A 1 149 ? 2.201   -36.932 -18.35  1 38.36 ? 134 TRP   A CZ2 1 
ATOM   1083 C  CZ3 . TRP   A 1 149 ? 1.136   -38.956 -19.128 1 38.66 ? 134 TRP   A CZ3 1 
ATOM   1084 C  CH2 . TRP   A 1 149 ? 1.732   -38.202 -18.119 1 38.76 ? 134 TRP   A CH2 1 
ATOM   1085 N  N   . LYS   A 1 150 ? -1.869  -37.971 -22.434 1 40.05 ? 135 LYS   A N   1 
ATOM   1086 C  CA  . LYS   A 1 150 ? -2.728  -38.659 -21.49  1 42.52 ? 135 LYS   A CA  1 
ATOM   1087 C  C   . LYS   A 1 150 ? -2.367  -40.133 -21.447 1 45.09 ? 135 LYS   A C   1 
ATOM   1088 O  O   . LYS   A 1 150 ? -1.799  -40.687 -22.402 1 45.57 ? 135 LYS   A O   1 
ATOM   1089 C  CB  . LYS   A 1 150 ? -4.22   -38.531 -21.896 1 44.45 ? 135 LYS   A CB  1 
ATOM   1090 C  CG  . LYS   A 1 150 ? -4.561  -39.185 -23.245 1 49.3  ? 135 LYS   A CG  1 
ATOM   1091 C  CD  . LYS   A 1 150 ? -6.067  -39.178 -23.56  1 54.47 ? 135 LYS   A CD  1 
ATOM   1092 C  CE  . LYS   A 1 150 ? -6.841  -40.184 -22.739 1 59.2  ? 135 LYS   A CE  1 
ATOM   1093 N  NZ  . LYS   A 1 150 ? -8.231  -40.378 -23.246 1 62.5  ? 135 LYS   A NZ  1 
ATOM   1094 N  N   . LYS   A 1 151 ? -2.721  -40.783 -20.339 1 46.22 ? 136 LYS   A N   1 
ATOM   1095 C  CA  . LYS   A 1 151 ? -2.603  -42.23  -20.23  1 47.27 ? 136 LYS   A CA  1 
ATOM   1096 C  C   . LYS   A 1 151 ? -3.987  -42.75  -20.642 1 48.89 ? 136 LYS   A C   1 
ATOM   1097 O  O   . LYS   A 1 151 ? -5.008  -42.206 -20.194 1 49.02 ? 136 LYS   A O   1 
ATOM   1098 C  CB  . LYS   A 1 151 ? -2.345  -42.656 -18.776 1 47.82 ? 136 LYS   A CB  1 
ATOM   1099 C  CG  . LYS   A 1 151 ? -0.927  -43.079 -18.492 1 50.7  ? 136 LYS   A CG  1 
ATOM   1100 C  CD  . LYS   A 1 151 ? -0.824  -43.636 -17.089 1 53.96 ? 136 LYS   A CD  1 
ATOM   1101 C  CE  . LYS   A 1 151 ? 0.587   -43.915 -16.67  1 55.8  ? 136 LYS   A CE  1 
ATOM   1102 N  NZ  . LYS   A 1 151 ? 0.609   -44.634 -15.373 1 57.53 ? 136 LYS   A NZ  1 
ATOM   1103 N  N   . LYS   A 1 152 ? -4.029  -43.783 -21.489 1 49.87 ? 137 LYS   A N   1 
ATOM   1104 C  CA  . LYS   A 1 152 ? -5.287  -44.417 -21.887 1 51.04 ? 137 LYS   A CA  1 
ATOM   1105 C  C   . LYS   A 1 152 ? -5.864  -45.13  -20.647 1 53.1  ? 137 LYS   A C   1 
ATOM   1106 O  O   . LYS   A 1 152 ? -7.034  -44.933 -20.301 1 53.43 ? 137 LYS   A O   1 
ATOM   1107 C  CB  . LYS   A 1 152 ? -5.056  -45.408 -23.054 1 51.1  ? 137 LYS   A CB  1 
ATOM   1108 C  CG  . LYS   A 1 152 ? -4.705  -44.724 -24.372 1 51.53 ? 137 LYS   A CG  1 
ATOM   1109 C  CD  . LYS   A 1 152 ? -4.289  -45.722 -25.413 1 54.84 ? 137 LYS   A CD  1 
ATOM   1110 C  CE  . LYS   A 1 152 ? -4.09   -45.096 -26.769 1 58.5  ? 137 LYS   A CE  1 
ATOM   1111 N  NZ  . LYS   A 1 152 ? -3.498  -46.054 -27.745 1 61.57 ? 137 LYS   A NZ  1 
ATOM   1112 N  N   . ASP   A 1 153 ? -5.014  -45.888 -19.935 1 54.35 ? 138 ASP   A N   1 
ATOM   1113 C  CA  . ASP   A 1 153 ? -5.38   -46.578 -18.706 1 56.06 ? 138 ASP   A CA  1 
ATOM   1114 C  C   . ASP   A 1 153 ? -4.465  -46.077 -17.594 1 57.29 ? 138 ASP   A C   1 
ATOM   1115 O  O   . ASP   A 1 153 ? -3.277  -46.393 -17.581 1 57.38 ? 138 ASP   A O   1 
ATOM   1116 C  CB  . ASP   A 1 153 ? -5.242  -48.104 -18.874 1 58.54 ? 138 ASP   A CB  1 
ATOM   1117 C  CG  . ASP   A 1 153 ? -5.721  -48.939 -17.688 1 64.01 ? 138 ASP   A CG  1 
ATOM   1118 O  OD1 . ASP   A 1 153 ? -6.23   -48.35  -16.704 1 64.59 ? 138 ASP   A OD1 1 
ATOM   1119 O  OD2 . ASP   A 1 153 ? -5.594  -50.179 -17.745 1 66.88 ? 138 ASP   A OD2 1 
ATOM   1120 N  N   . PRO   A 1 154 ? -5.022  -45.339 -16.613 1 58.15 ? 139 PRO   A N   1 
ATOM   1121 C  CA  . PRO   A 1 154 ? -4.19   -44.828 -15.501 1 58.39 ? 139 PRO   A CA  1 
ATOM   1122 C  C   . PRO   A 1 154 ? -3.465  -45.892 -14.672 1 59    ? 139 PRO   A C   1 
ATOM   1123 O  O   . PRO   A 1 154 ? -2.52   -45.573 -13.95  1 59    ? 139 PRO   A O   1 
ATOM   1124 C  CB  . PRO   A 1 154 ? -5.187  -44.044 -14.637 1 59.04 ? 139 PRO   A CB  1 
ATOM   1125 C  CG  . PRO   A 1 154 ? -6.353  -43.752 -15.539 1 59.64 ? 139 PRO   A CG  1 
ATOM   1126 C  CD  . PRO   A 1 154 ? -6.429  -44.901 -16.497 1 57.89 ? 139 PRO   A CD  1 
ATOM   1127 N  N   . ASN   A 1 155 ? -3.904  -47.152 -14.761 1 59.43 ? 140 ASN   A N   1 
ATOM   1128 C  CA  . ASN   A 1 155 ? -3.275  -48.241 -14.003 1 60.24 ? 140 ASN   A CA  1 
ATOM   1129 C  C   . ASN   A 1 155 ? -2.187  -48.987 -14.781 1 59.58 ? 140 ASN   A C   1 
ATOM   1130 O  O   . ASN   A 1 155 ? -1.583  -49.909 -14.244 1 59.77 ? 140 ASN   A O   1 
ATOM   1131 C  CB  . ASN   A 1 155 ? -4.326  -49.21  -13.454 1 62.73 ? 140 ASN   A CB  1 
ATOM   1132 C  CG  . ASN   A 1 155 ? -5.484  -48.511 -12.764 1 67.82 ? 140 ASN   A CG  1 
ATOM   1133 O  OD1 . ASN   A 1 155 ? -5.308  -47.744 -11.8   1 69.34 ? 140 ASN   A OD1 1 
ATOM   1134 N  ND2 . ASN   A 1 155 ? -6.691  -48.736 -13.27  1 69.16 ? 140 ASN   A ND2 1 
ATOM   1135 N  N   . LYS   A 1 156 ? -1.934  -48.6   -16.036 1 58.67 ? 141 LYS   A N   1 
ATOM   1136 C  CA  . LYS   A 1 156 ? -0.875  -49.188 -16.854 1 58.34 ? 141 LYS   A CA  1 
ATOM   1137 C  C   . LYS   A 1 156 ? 0.316   -48.189 -16.953 1 57.31 ? 141 LYS   A C   1 
ATOM   1138 O  O   . LYS   A 1 156 ? 0.115   -46.99  -16.743 1 57.16 ? 141 LYS   A O   1 
ATOM   1139 C  CB  . LYS   A 1 156 ? -1.434  -49.629 -18.216 1 60.19 ? 141 LYS   A CB  1 
ATOM   1140 C  CG  . LYS   A 1 156 ? -2.27   -50.897 -18.09  1 64.42 ? 141 LYS   A CG  1 
ATOM   1141 C  CD  . LYS   A 1 156 ? -2.946  -51.276 -19.392 1 68.77 ? 141 LYS   A CD  1 
ATOM   1142 C  CE  . LYS   A 1 156 ? -3.76   -52.541 -19.275 1 72.07 ? 141 LYS   A CE  1 
ATOM   1143 N  NZ  . LYS   A 1 156 ? -4.992  -52.48  -20.113 1 74.64 ? 141 LYS   A NZ  1 
ATOM   1144 N  N   . PRO   A 1 157 ? 1.562   -48.645 -17.21  1 56.3  ? 142 PRO   A N   1 
ATOM   1145 C  CA  . PRO   A 1 157 ? 2.708   -47.707 -17.192 1 55.46 ? 142 PRO   A CA  1 
ATOM   1146 C  C   . PRO   A 1 157 ? 2.822   -46.73  -18.386 1 54.12 ? 142 PRO   A C   1 
ATOM   1147 O  O   . PRO   A 1 157 ? 1.994   -46.727 -19.301 1 54.29 ? 142 PRO   A O   1 
ATOM   1148 C  CB  . PRO   A 1 157 ? 3.926   -48.636 -17.076 1 56.17 ? 142 PRO   A CB  1 
ATOM   1149 C  CG  . PRO   A 1 157 ? 3.489   -49.92  -17.656 1 56.89 ? 142 PRO   A CG  1 
ATOM   1150 C  CD  . PRO   A 1 157 ? 2.002   -50.038 -17.431 1 55.87 ? 142 PRO   A CD  1 
ATOM   1151 N  N   . LEU   A 1 158 ? 3.812   -45.833 -18.316 1 52.76 ? 143 LEU   A N   1 
ATOM   1152 C  CA  . LEU   A 1 158 ? 4.073   -44.82  -19.334 1 51.44 ? 143 LEU   A CA  1 
ATOM   1153 C  C   . LEU   A 1 158 ? 4.792   -45.422 -20.535 1 50.58 ? 143 LEU   A C   1 
ATOM   1154 O  O   . LEU   A 1 158 ? 6.002   -45.248 -20.699 1 50.93 ? 143 LEU   A O   1 
ATOM   1155 C  CB  . LEU   A 1 158 ? 4.896   -43.671 -18.757 1 50.73 ? 143 LEU   A CB  1 
ATOM   1156 C  CG  . LEU   A 1 158 ? 4.187   -42.776 -17.789 1 51.66 ? 143 LEU   A CG  1 
ATOM   1157 C  CD1 . LEU   A 1 158 ? 5.192   -41.928 -17.019 1 52.23 ? 143 LEU   A CD1 1 
ATOM   1158 C  CD2 . LEU   A 1 158 ? 3.17    -41.919 -18.499 1 51.66 ? 143 LEU   A CD2 1 
ATOM   1159 N  N   . THR   A 1 159 ? 4.039   -46.144 -21.364 1 49.51 ? 144 THR   A N   1 
ATOM   1160 C  CA  . THR   A 1 159 ? 4.518   -46.739 -22.602 1 49.65 ? 144 THR   A CA  1 
ATOM   1161 C  C   . THR   A 1 159 ? 3.711   -46.156 -23.773 1 49.46 ? 144 THR   A C   1 
ATOM   1162 O  O   . THR   A 1 159 ? 2.586   -45.703 -23.575 1 49.76 ? 144 THR   A O   1 
ATOM   1163 C  CB  . THR   A 1 159 ? 4.404   -48.262 -22.549 1 51.77 ? 144 THR   A CB  1 
ATOM   1164 O  OG1 . THR   A 1 159 ? 3.028   -48.638 -22.421 1 53.77 ? 144 THR   A OG1 1 
ATOM   1165 C  CG2 . THR   A 1 159 ? 5.255   -48.882 -21.444 1 52.01 ? 144 THR   A CG2 1 
ATOM   1166 N  N   . TYR   A 1 160 ? 4.266   -46.177 -24.998 1 48.75 ? 145 TYR   A N   1 
ATOM   1167 C  CA  . TYR   A 1 160 ? 3.585   -45.625 -26.169 1 48.51 ? 145 TYR   A CA  1 
ATOM   1168 C  C   . TYR   A 1 160 ? 2.167   -46.188 -26.358 1 49.38 ? 145 TYR   A C   1 
ATOM   1169 O  O   . TYR   A 1 160 ? 1.228   -45.431 -26.614 1 49.52 ? 145 TYR   A O   1 
ATOM   1170 C  CB  . TYR   A 1 160 ? 4.441   -45.813 -27.437 1 47.9  ? 145 TYR   A CB  1 
ATOM   1171 C  CG  . TYR   A 1 160 ? 3.937   -45.008 -28.616 1 47.97 ? 145 TYR   A CG  1 
ATOM   1172 C  CD1 . TYR   A 1 160 ? 2.968   -45.519 -29.47  1 48.26 ? 145 TYR   A CD1 1 
ATOM   1173 C  CD2 . TYR   A 1 160 ? 4.421   -43.726 -28.872 1 48.47 ? 145 TYR   A CD2 1 
ATOM   1174 C  CE1 . TYR   A 1 160 ? 2.453   -44.761 -30.515 1 49.13 ? 145 TYR   A CE1 1 
ATOM   1175 C  CE2 . TYR   A 1 160 ? 3.939   -42.972 -29.94  1 49.2  ? 145 TYR   A CE2 1 
ATOM   1176 C  CZ  . TYR   A 1 160 ? 2.959   -43.497 -30.764 1 50.04 ? 145 TYR   A CZ  1 
ATOM   1177 O  OH  . TYR   A 1 160 ? 2.479   -42.781 -31.834 1 51.39 ? 145 TYR   A OH  1 
ATOM   1178 N  N   . GLU   A 1 161 ? 2.006   -47.505 -26.164 1 49.77 ? 146 GLU   A N   1 
ATOM   1179 C  CA  . GLU   A 1 161 ? 0.717   -48.193 -26.32  1 50.11 ? 146 GLU   A CA  1 
ATOM   1180 C  C   . GLU   A 1 161 ? -0.342  -47.699 -25.35  1 49.17 ? 146 GLU   A C   1 
ATOM   1181 O  O   . GLU   A 1 161 ? -1.519  -47.67  -25.691 1 49.84 ? 146 GLU   A O   1 
ATOM   1182 C  CB  . GLU   A 1 161 ? 0.891   -49.711 -26.186 1 53.05 ? 146 GLU   A CB  1 
ATOM   1183 C  CG  . GLU   A 1 161 ? 1.47    -50.341 -27.437 1 58.69 ? 146 GLU   A CG  1 
ATOM   1184 C  CD  . GLU   A 1 161 ? 2.898   -49.925 -27.722 1 65.34 ? 146 GLU   A CD  1 
ATOM   1185 O  OE1 . GLU   A 1 161 ? 3.724   -49.957 -26.779 1 66.22 ? 146 GLU   A OE1 1 
ATOM   1186 O  OE2 . GLU   A 1 161 ? 3.183   -49.537 -28.88  1 66.91 ? 146 GLU   A OE2 1 
ATOM   1187 N  N   . ASN   A 1 162 ? 0.071   -47.277 -24.16  1 47.71 ? 147 ASN   A N   1 
ATOM   1188 C  CA  . ASN   A 1 162 ? -0.851  -46.767 -23.155 1 46.62 ? 147 ASN   A CA  1 
ATOM   1189 C  C   . ASN   A 1 162 ? -0.941  -45.225 -23.148 1 45.55 ? 147 ASN   A C   1 
ATOM   1190 O  O   . ASN   A 1 162 ? -1.377  -44.642 -22.158 1 45.33 ? 147 ASN   A O   1 
ATOM   1191 C  CB  . ASN   A 1 162 ? -0.429  -47.269 -21.771 1 47.19 ? 147 ASN   A CB  1 
ATOM   1192 C  CG  . ASN   A 1 162 ? -1.483  -47.032 -20.733 1 50.33 ? 147 ASN   A CG  1 
ATOM   1193 O  OD1 . ASN   A 1 162 ? -2.67   -47.273 -20.958 1 51.09 ? 147 ASN   A OD1 1 
ATOM   1194 N  ND2 . ASN   A 1 162 ? -1.084  -46.489 -19.601 1 52.21 ? 147 ASN   A ND2 1 
ATOM   1195 N  N   . MET   A 1 163 ? -0.518  -44.562 -24.228 1 44.73 ? 148 MET   A N   1 
ATOM   1196 C  CA  . MET   A 1 163 ? -0.528  -43.105 -24.274 1 44.01 ? 148 MET   A CA  1 
ATOM   1197 C  C   . MET   A 1 163 ? -1.095  -42.565 -25.558 1 43.55 ? 148 MET   A C   1 
ATOM   1198 O  O   . MET   A 1 163 ? -1.109  -43.235 -26.58  1 43.84 ? 148 MET   A O   1 
ATOM   1199 C  CB  . MET   A 1 163 ? 0.891   -42.547 -24.04  1 44.36 ? 148 MET   A CB  1 
ATOM   1200 C  CG  . MET   A 1 163 ? 1.409   -42.75  -22.622 1 45.9  ? 148 MET   A CG  1 
ATOM   1201 S  SD  . MET   A 1 163 ? 3.218   -42.622 -22.553 1 46.68 ? 148 MET   A SD  1 
ATOM   1202 C  CE  . MET   A 1 163 ? 3.377   -40.891 -22.078 1 42.05 ? 148 MET   A CE  1 
ATOM   1203 N  N   . ASP   A 1 164 ? -1.521  -41.32  -25.511 1 43.12 ? 149 ASP   A N   1 
ATOM   1204 C  CA  . ASP   A 1 164 ? -2.048  -40.602 -26.65  1 43.32 ? 149 ASP   A CA  1 
ATOM   1205 C  C   . ASP   A 1 164 ? -1.819  -39.103 -26.441 1 42.26 ? 149 ASP   A C   1 
ATOM   1206 O  O   . ASP   A 1 164 ? -1.634  -38.649 -25.309 1 42.31 ? 149 ASP   A O   1 
ATOM   1207 C  CB  . ASP   A 1 164 ? -3.554  -40.878 -26.783 1 46.65 ? 149 ASP   A CB  1 
ATOM   1208 C  CG  . ASP   A 1 164 ? -4.101  -40.767 -28.195 1 53.79 ? 149 ASP   A CG  1 
ATOM   1209 O  OD1 . ASP   A 1 164 ? -3.385  -40.244 -29.074 1 53.92 ? 149 ASP   A OD1 1 
ATOM   1210 O  OD2 . ASP   A 1 164 ? -5.249  -41.195 -28.417 1 58.82 ? 149 ASP   A OD2 1 
ATOM   1211 N  N   . VAL   A 1 165 ? -1.8    -38.346 -27.532 1 41.25 ? 150 VAL   A N   1 
ATOM   1212 C  CA  . VAL   A 1 165 ? -1.706  -36.895 -27.472 1 41.32 ? 150 VAL   A CA  1 
ATOM   1213 C  C   . VAL   A 1 165 ? -3.116  -36.36  -27.348 1 42.21 ? 150 VAL   A C   1 
ATOM   1214 O  O   . VAL   A 1 165 ? -4.073  -37.059 -27.704 1 43.81 ? 150 VAL   A O   1 
ATOM   1215 C  CB  . VAL   A 1 165 ? -0.995  -36.252 -28.69  1 41.3  ? 150 VAL   A CB  1 
ATOM   1216 C  CG1 . VAL   A 1 165 ? 0.48    -36.627 -28.742 1 41.32 ? 150 VAL   A CG1 1 
ATOM   1217 C  CG2 . VAL   A 1 165 ? -1.716  -36.576 -30.001 1 41.57 ? 150 VAL   A CG2 1 
ATOM   1218 N  N   . LEU   A 1 166 ? -3.272  -35.128 -26.866 1 41.5  ? 151 LEU   A N   1 
ATOM   1219 C  CA  . LEU   A 1 166 ? -4.594  -34.549 -26.746 1 41.28 ? 151 LEU   A CA  1 
ATOM   1220 C  C   . LEU   A 1 166 ? -5.017  -33.884 -28.068 1 41.22 ? 151 LEU   A C   1 
ATOM   1221 O  O   . LEU   A 1 166 ? -6.184  -33.964 -28.434 1 41.75 ? 151 LEU   A O   1 
ATOM   1222 C  CB  . LEU   A 1 166 ? -4.645  -33.566 -25.57  1 41.13 ? 151 LEU   A CB  1 
ATOM   1223 C  CG  . LEU   A 1 166 ? -4.249  -34.129 -24.211 1 42.71 ? 151 LEU   A CG  1 
ATOM   1224 C  CD1 . LEU   A 1 166 ? -4.343  -33.074 -23.15  1 43.07 ? 151 LEU   A CD1 1 
ATOM   1225 C  CD2 . LEU   A 1 166 ? -5.108  -35.333 -23.824 1 43.48 ? 151 LEU   A CD2 1 
ATOM   1226 N  N   . PHE   A 1 167 ? -4.077  -33.221 -28.78  1 40.73 ? 152 PHE   A N   1 
ATOM   1227 C  CA  . PHE   A 1 167 ? -4.396  -32.467 -29.997 1 40.36 ? 152 PHE   A CA  1 
ATOM   1228 C  C   . PHE   A 1 167 ? -3.467  -32.724 -31.168 1 40.01 ? 152 PHE   A C   1 
ATOM   1229 O  O   . PHE   A 1 167 ? -2.267  -32.884 -30.989 1 39.77 ? 152 PHE   A O   1 
ATOM   1230 C  CB  . PHE   A 1 167 ? -4.457  -30.961 -29.704 1 40.31 ? 152 PHE   A CB  1 
ATOM   1231 C  CG  . PHE   A 1 167 ? -5.456  -30.624 -28.618 1 41.6  ? 152 PHE   A CG  1 
ATOM   1232 C  CD1 . PHE   A 1 167 ? -6.817  -30.691 -28.86  1 42.31 ? 152 PHE   A CD1 1 
ATOM   1233 C  CD2 . PHE   A 1 167 ? -5.036  -30.331 -27.335 1 42.59 ? 152 PHE   A CD2 1 
ATOM   1234 C  CE1 . PHE   A 1 167 ? -7.739  -30.456 -27.843 1 43.14 ? 152 PHE   A CE1 1 
ATOM   1235 C  CE2 . PHE   A 1 167 ? -5.957  -30.09  -26.317 1 43.59 ? 152 PHE   A CE2 1 
ATOM   1236 C  CZ  . PHE   A 1 167 ? -7.31   -30.163 -26.579 1 43.26 ? 152 PHE   A CZ  1 
ATOM   1237 N  N   . SER   A 1 168 ? -4.043  -32.696 -32.378 1 39.6  ? 153 SER   A N   1 
ATOM   1238 C  CA  . SER   A 1 168 ? -3.399  -32.873 -33.67  1 39.88 ? 153 SER   A CA  1 
ATOM   1239 C  C   . SER   A 1 168 ? -3.754  -31.715 -34.608 1 39.46 ? 153 SER   A C   1 
ATOM   1240 O  O   . SER   A 1 168 ? -4.725  -31.006 -34.368 1 39.74 ? 153 SER   A O   1 
ATOM   1241 C  CB  . SER   A 1 168 ? -3.868  -34.179 -34.295 1 42.27 ? 153 SER   A CB  1 
ATOM   1242 O  OG  . SER   A 1 168 ? -2.907  -35.185 -34.046 1 47.08 ? 153 SER   A OG  1 
ATOM   1243 N  N   . PHE   A 1 169 ? -3      -31.543 -35.7   1 39.19 ? 154 PHE   A N   1 
ATOM   1244 C  CA  . PHE   A 1 169 ? -3.276  -30.471 -36.66  1 39.61 ? 154 PHE   A CA  1 
ATOM   1245 C  C   . PHE   A 1 169 ? -4.006  -30.957 -37.907 1 39.84 ? 154 PHE   A C   1 
ATOM   1246 O  O   . PHE   A 1 169 ? -4.998  -30.369 -38.295 1 39.9  ? 154 PHE   A O   1 
ATOM   1247 C  CB  . PHE   A 1 169 ? -1.986  -29.735 -37.042 1 39.6  ? 154 PHE   A CB  1 
ATOM   1248 C  CG  . PHE   A 1 169 ? -1.396  -28.981 -35.884 1 40.47 ? 154 PHE   A CG  1 
ATOM   1249 C  CD1 . PHE   A 1 169 ? -1.975  -27.807 -35.435 1 41.01 ? 154 PHE   A CD1 1 
ATOM   1250 C  CD2 . PHE   A 1 169 ? -0.262  -29.447 -35.239 1 41.4  ? 154 PHE   A CD2 1 
ATOM   1251 C  CE1 . PHE   A 1 169 ? -1.438  -27.118 -34.361 1 41.65 ? 154 PHE   A CE1 1 
ATOM   1252 C  CE2 . PHE   A 1 169 ? 0.275   -28.751 -34.167 1 42.12 ? 154 PHE   A CE2 1 
ATOM   1253 C  CZ  . PHE   A 1 169 ? -0.318  -27.591 -33.736 1 41.51 ? 154 PHE   A CZ  1 
ATOM   1254 N  N   . ARG   A 1 170 ? -3.495  -31.998 -38.55  1 40.36 ? 155 ARG   A N   1 
ATOM   1255 C  CA  . ARG   A 1 170 ? -4.061  -32.57  -39.766 1 41.1  ? 155 ARG   A CA  1 
ATOM   1256 C  C   . ARG   A 1 170 ? -4.134  -34.082 -39.66  1 42.74 ? 155 ARG   A C   1 
ATOM   1257 O  O   . ARG   A 1 170 ? -3.469  -34.694 -38.83  1 43.45 ? 155 ARG   A O   1 
ATOM   1258 C  CB  . ARG   A 1 170 ? -3.239  -32.203 -41.015 1 40.83 ? 155 ARG   A CB  1 
ATOM   1259 C  CG  . ARG   A 1 170 ? -3.123  -30.72  -41.276 1 42.54 ? 155 ARG   A CG  1 
ATOM   1260 C  CD  . ARG   A 1 170 ? -4.464  -30.051 -41.518 1 43.73 ? 155 ARG   A CD  1 
ATOM   1261 N  NE  . ARG   A 1 170 ? -5.093  -30.532 -42.74  1 45.95 ? 155 ARG   A NE  1 
ATOM   1262 C  CZ  . ARG   A 1 170 ? -4.875  -30.03  -43.952 1 47.34 ? 155 ARG   A CZ  1 
ATOM   1263 N  NH1 . ARG   A 1 170 ? -4.025  -29.02  -44.12  1 46.38 ? 155 ARG   A NH1 1 
ATOM   1264 N  NH2 . ARG   A 1 170 ? -5.495  -30.536 -45.004 1 47.7  ? 155 ARG   A NH2 1 
ATOM   1265 N  N   . ASP   A 1 171 ? -4.977  -34.683 -40.495 1 43.08 ? 156 ASP   A N   1 
ATOM   1266 C  CA  . ASP   A 1 171 ? -5.153  -36.118 -40.574 1 43.57 ? 156 ASP   A CA  1 
ATOM   1267 C  C   . ASP   A 1 171 ? -3.849  -36.684 -41.168 1 42.69 ? 156 ASP   A C   1 
ATOM   1268 O  O   . ASP   A 1 171 ? -3.376  -36.2   -42.199 1 42.72 ? 156 ASP   A O   1 
ATOM   1269 C  CB  . ASP   A 1 171 ? -6.357  -36.38  -41.498 1 46.4  ? 156 ASP   A CB  1 
ATOM   1270 C  CG  . ASP   A 1 171 ? -6.684  -37.828 -41.715 1 53.56 ? 156 ASP   A CG  1 
ATOM   1271 O  OD1 . ASP   A 1 171 ? -6.6    -38.607 -40.737 1 55.24 ? 156 ASP   A OD1 1 
ATOM   1272 O  OD2 . ASP   A 1 171 ? -7.037  -38.187 -42.859 1 56.73 ? 156 ASP   A OD2 1 
ATOM   1273 N  N   . GLY   A 1 172 ? -3.23   -37.623 -40.467 1 41.81 ? 157 GLY   A N   1 
ATOM   1274 C  CA  . GLY   A 1 172 ? -1.984  -38.222 -40.934 1 41.14 ? 157 GLY   A CA  1 
ATOM   1275 C  C   . GLY   A 1 172 ? -0.745  -37.366 -40.769 1 40.43 ? 157 GLY   A C   1 
ATOM   1276 O  O   . GLY   A 1 172 ? 0.253   -37.609 -41.445 1 40.23 ? 157 GLY   A O   1 
ATOM   1277 N  N   . ASP   A 1 173 ? -0.774  -36.35  -39.879 1 39.66 ? 158 ASP   A N   1 
ATOM   1278 C  CA  . ASP   A 1 173 ? 0.4     -35.481 -39.682 1 38.88 ? 158 ASP   A CA  1 
ATOM   1279 C  C   . ASP   A 1 173 ? 1.514   -36.103 -38.841 1 39.91 ? 158 ASP   A C   1 
ATOM   1280 O  O   . ASP   A 1 173 ? 2.585   -35.497 -38.723 1 40.24 ? 158 ASP   A O   1 
ATOM   1281 C  CB  . ASP   A 1 173 ? 0.014   -34.103 -39.104 1 37.96 ? 158 ASP   A CB  1 
ATOM   1282 C  CG  . ASP   A 1 173 ? -0.656  -34.131 -37.747 1 38.88 ? 158 ASP   A CG  1 
ATOM   1283 O  OD1 . ASP   A 1 173 ? -0.809  -35.234 -37.176 1 38.58 ? 158 ASP   A OD1 1 
ATOM   1284 O  OD2 . ASP   A 1 173 ? -1.076  -33.058 -37.272 1 40.01 ? 158 ASP   A OD2 1 
ATOM   1285 N  N   . CYS   A 1 174 ? 1.251   -37.278 -38.22  1 39.79 ? 159 CYS   A N   1 
ATOM   1286 C  CA  . CYS   A 1 174 ? 2.188   -37.977 -37.343 1 40.6  ? 159 CYS   A CA  1 
ATOM   1287 C  C   . CYS   A 1 174 ? 2.535   -37.177 -36.085 1 40.66 ? 159 CYS   A C   1 
ATOM   1288 O  O   . CYS   A 1 174 ? 3.589   -37.388 -35.504 1 41.48 ? 159 CYS   A O   1 
ATOM   1289 C  CB  . CYS   A 1 174 ? 3.442   -38.408 -38.102 1 41.75 ? 159 CYS   A CB  1 
ATOM   1290 S  SG  . CYS   A 1 174 ? 3.132   -39.659 -39.366 1 45.1  ? 159 CYS   A SG  1 
ATOM   1291 N  N   . SER   A 1 175 ? 1.666   -36.248 -35.679 1 39.93 ? 160 SER   A N   1 
ATOM   1292 C  CA  . SER   A 1 175 ? 1.897   -35.433 -34.5   1 39.06 ? 160 SER   A CA  1 
ATOM   1293 C  C   . SER   A 1 175 ? 1.858   -36.276 -33.235 1 38.49 ? 160 SER   A C   1 
ATOM   1294 O  O   . SER   A 1 175 ? 2.595   -35.971 -32.307 1 38.82 ? 160 SER   A O   1 
ATOM   1295 C  CB  . SER   A 1 175 ? 0.912   -34.268 -34.437 1 39.44 ? 160 SER   A CB  1 
ATOM   1296 O  OG  . SER   A 1 175 ? -0.426  -34.724 -34.379 1 39.92 ? 160 SER   A OG  1 
ATOM   1297 N  N   . LYS   A 1 176 ? 1.076   -37.372 -33.207 1 37.51 ? 161 LYS   A N   1 
ATOM   1298 C  CA  . LYS   A 1 176 ? 1.061   -38.259 -32.044 1 37.33 ? 161 LYS   A CA  1 
ATOM   1299 C  C   . LYS   A 1 176 ? 2.453   -38.902 -31.864 1 36.97 ? 161 LYS   A C   1 
ATOM   1300 O  O   . LYS   A 1 176 ? 3.059   -38.75  -30.811 1 38.21 ? 161 LYS   A O   1 
ATOM   1301 C  CB  . LYS   A 1 176 ? -0.043  -39.333 -32.162 1 39.13 ? 161 LYS   A CB  1 
ATOM   1302 C  CG  . LYS   A 1 176 ? -0.065  -40.286 -30.971 1 42.69 ? 161 LYS   A CG  1 
ATOM   1303 C  CD  . LYS   A 1 176 ? -0.995  -41.467 -31.157 1 46.81 ? 161 LYS   A CD  1 
ATOM   1304 C  CE  . LYS   A 1 176 ? -0.886  -42.436 -29.997 1 50.52 ? 161 LYS   A CE  1 
ATOM   1305 N  NZ  . LYS   A 1 176 ? -1.728  -43.647 -30.191 1 53    ? 161 LYS   A NZ  1 
ATOM   1306 N  N   . GLY   A 1 177 ? 2.986   -39.512 -32.914 1 35.43 ? 162 GLY   A N   1 
ATOM   1307 C  CA  . GLY   A 1 177 ? 4.308   -40.104 -32.867 1 35.24 ? 162 GLY   A CA  1 
ATOM   1308 C  C   . GLY   A 1 177 ? 5.402   -39.107 -32.562 1 35.63 ? 162 GLY   A C   1 
ATOM   1309 O  O   . GLY   A 1 177 ? 6.277   -39.384 -31.739 1 36.55 ? 162 GLY   A O   1 
ATOM   1310 N  N   . PHE   A 1 178 ? 5.374   -37.942 -33.219 1 34.46 ? 163 PHE   A N   1 
ATOM   1311 C  CA  . PHE   A 1 178 ? 6.403   -36.928 -33.01  1 33.76 ? 163 PHE   A CA  1 
ATOM   1312 C  C   . PHE   A 1 178 ? 6.386   -36.396 -31.57  1 34.07 ? 163 PHE   A C   1 
ATOM   1313 O  O   . PHE   A 1 178 ? 7.405   -36.455 -30.885 1 34.35 ? 163 PHE   A O   1 
ATOM   1314 C  CB  . PHE   A 1 178 ? 6.225   -35.783 -34.019 1 32.68 ? 163 PHE   A CB  1 
ATOM   1315 C  CG  . PHE   A 1 178 ? 7.251   -34.683 -33.948 1 32.26 ? 163 PHE   A CG  1 
ATOM   1316 C  CD1 . PHE   A 1 178 ? 8.592   -34.949 -34.175 1 31.95 ? 163 PHE   A CD1 1 
ATOM   1317 C  CD2 . PHE   A 1 178 ? 6.865   -33.371 -33.759 1 32.65 ? 163 PHE   A CD2 1 
ATOM   1318 C  CE1 . PHE   A 1 178 ? 9.525   -33.939 -34.145 1 32.33 ? 163 PHE   A CE1 1 
ATOM   1319 C  CE2 . PHE   A 1 178 ? 7.8     -32.352 -33.785 1 32.83 ? 163 PHE   A CE2 1 
ATOM   1320 C  CZ  . PHE   A 1 178 ? 9.117   -32.639 -34.006 1 32.33 ? 163 PHE   A CZ  1 
ATOM   1321 N  N   . PHE   A 1 179 ? 5.227   -35.913 -31.101 1 33.7  ? 164 PHE   A N   1 
ATOM   1322 C  CA  . PHE   A 1 179 ? 5.12    -35.372 -29.755 1 33.82 ? 164 PHE   A CA  1 
ATOM   1323 C  C   . PHE   A 1 179 ? 5.3     -36.425 -28.664 1 34.49 ? 164 PHE   A C   1 
ATOM   1324 O  O   . PHE   A 1 179 ? 5.934   -36.121 -27.657 1 34.3  ? 164 PHE   A O   1 
ATOM   1325 C  CB  . PHE   A 1 179 ? 3.8     -34.611 -29.567 1 33.45 ? 164 PHE   A CB  1 
ATOM   1326 C  CG  . PHE   A 1 179 ? 3.622   -33.4   -30.461 1 33.36 ? 164 PHE   A CG  1 
ATOM   1327 C  CD1 . PHE   A 1 179 ? 4.695   -32.591 -30.781 1 33.15 ? 164 PHE   A CD1 1 
ATOM   1328 C  CD2 . PHE   A 1 179 ? 2.365   -33.049 -30.938 1 34.41 ? 164 PHE   A CD2 1 
ATOM   1329 C  CE1 . PHE   A 1 179 ? 4.523   -31.46  -31.575 1 33.91 ? 164 PHE   A CE1 1 
ATOM   1330 C  CE2 . PHE   A 1 179 ? 2.196   -31.92  -31.742 1 34.8  ? 164 PHE   A CE2 1 
ATOM   1331 C  CZ  . PHE   A 1 179 ? 3.279   -31.139 -32.063 1 34.14 ? 164 PHE   A CZ  1 
ATOM   1332 N  N   . LEU   A 1 180 ? 4.748   -37.652 -28.844 1 34.88 ? 165 LEU   A N   1 
ATOM   1333 C  CA  . LEU   A 1 180 ? 4.849   -38.7   -27.828 1 35.84 ? 165 LEU   A CA  1 
ATOM   1334 C  C   . LEU   A 1 180 ? 6.236   -39.274 -27.677 1 35.46 ? 165 LEU   A C   1 
ATOM   1335 O  O   . LEU   A 1 180 ? 6.639   -39.566 -26.548 1 35.51 ? 165 LEU   A O   1 
ATOM   1336 C  CB  . LEU   A 1 180 ? 3.85    -39.85  -28.042 1 37.45 ? 165 LEU   A CB  1 
ATOM   1337 C  CG  . LEU   A 1 180 ? 2.397   -39.659 -27.64  1 41.06 ? 165 LEU   A CG  1 
ATOM   1338 C  CD1 . LEU   A 1 180 ? 1.662   -40.992 -27.659 1 42.3  ? 165 LEU   A CD1 1 
ATOM   1339 C  CD2 . LEU   A 1 180 ? 2.262   -39.057 -26.231 1 42    ? 165 LEU   A CD2 1 
ATOM   1340 N  N   . VAL   A 1 181 ? 6.965   -39.471 -28.787 1 35.16 ? 166 VAL   A N   1 
ATOM   1341 C  CA  . VAL   A 1 181 ? 8.326   -39.989 -28.69  1 35.03 ? 166 VAL   A CA  1 
ATOM   1342 C  C   . VAL   A 1 181 ? 9.258   -38.94  -28.044 1 35.05 ? 166 VAL   A C   1 
ATOM   1343 O  O   . VAL   A 1 181 ? 10.082  -39.313 -27.207 1 35.19 ? 166 VAL   A O   1 
ATOM   1344 C  CB  . VAL   A 1 181 ? 8.854   -40.561 -30.017 1 35.36 ? 166 VAL   A CB  1 
ATOM   1345 C  CG1 . VAL   A 1 181 ? 10.331  -40.911 -29.908 1 35.4  ? 166 VAL   A CG1 1 
ATOM   1346 C  CG2 . VAL   A 1 181 ? 8.038   -41.785 -30.424 1 35.8  ? 166 VAL   A CG2 1 
ATOM   1347 N  N   . SER   A 1 182 ? 9.044   -37.625 -28.311 1 33.96 ? 167 SER   A N   1 
ATOM   1348 C  CA  . SER   A 1 182 ? 9.821   -36.568 -27.639 1 33.92 ? 167 SER   A CA  1 
ATOM   1349 C  C   . SER   A 1 182 ? 9.533   -36.638 -26.124 1 35.12 ? 167 SER   A C   1 
ATOM   1350 O  O   . SER   A 1 182 ? 10.454  -36.611 -25.322 1 35.52 ? 167 SER   A O   1 
ATOM   1351 C  CB  . SER   A 1 182 ? 9.441   -35.185 -28.163 1 33.96 ? 167 SER   A CB  1 
ATOM   1352 O  OG  . SER   A 1 182 ? 9.684   -35.018 -29.55  1 34.83 ? 167 SER   A OG  1 
ATOM   1353 N  N   . LEU   A 1 183 ? 8.259   -36.814 -25.755 1 35.37 ? 168 LEU   A N   1 
ATOM   1354 C  CA  . LEU   A 1 183 ? 7.826   -36.924 -24.373 1 36.76 ? 168 LEU   A CA  1 
ATOM   1355 C  C   . LEU   A 1 183 ? 8.441   -38.14  -23.69  1 37.13 ? 168 LEU   A C   1 
ATOM   1356 O  O   . LEU   A 1 183 ? 8.902   -38.032 -22.563 1 37.67 ? 168 LEU   A O   1 
ATOM   1357 C  CB  . LEU   A 1 183 ? 6.299   -37.011 -24.325 1 37.33 ? 168 LEU   A CB  1 
ATOM   1358 C  CG  . LEU   A 1 183 ? 5.705   -37.197 -22.95  1 39.31 ? 168 LEU   A CG  1 
ATOM   1359 C  CD1 . LEU   A 1 183 ? 5.947   -35.971 -22.092 1 39.96 ? 168 LEU   A CD1 1 
ATOM   1360 C  CD2 . LEU   A 1 183 ? 4.24    -37.527 -23.048 1 40.21 ? 168 LEU   A CD2 1 
ATOM   1361 N  N   . LEU   A 1 184 ? 8.477   -39.282 -24.371 1 36.52 ? 169 LEU   A N   1 
ATOM   1362 C  CA  . LEU   A 1 184 ? 9.07    -40.495 -23.814 1 36.31 ? 169 LEU   A CA  1 
ATOM   1363 C  C   . LEU   A 1 184 ? 10.578  -40.324 -23.594 1 36.64 ? 169 LEU   A C   1 
ATOM   1364 O  O   . LEU   A 1 184 ? 11.102  -40.862 -22.645 1 37.13 ? 169 LEU   A O   1 
ATOM   1365 C  CB  . LEU   A 1 184 ? 8.746   -41.707 -24.706 1 35.92 ? 169 LEU   A CB  1 
ATOM   1366 C  CG  . LEU   A 1 184 ? 7.273   -42.163 -24.664 1 36.92 ? 169 LEU   A CG  1 
ATOM   1367 C  CD1 . LEU   A 1 184 ? 6.945   -43.101 -25.813 1 36.78 ? 169 LEU   A CD1 1 
ATOM   1368 C  CD2 . LEU   A 1 184 ? 6.941   -42.816 -23.336 1 37.08 ? 169 LEU   A CD2 1 
ATOM   1369 N  N   . VAL   A 1 185 ? 11.267  -39.563 -24.449 1 36.78 ? 170 VAL   A N   1 
ATOM   1370 C  CA  . VAL   A 1 185 ? 12.688  -39.286 -24.299 1 36.87 ? 170 VAL   A CA  1 
ATOM   1371 C  C   . VAL   A 1 185 ? 12.883  -38.342 -23.103 1 38.3  ? 170 VAL   A C   1 
ATOM   1372 O  O   . VAL   A 1 185 ? 13.762  -38.602 -22.272 1 39.02 ? 170 VAL   A O   1 
ATOM   1373 C  CB  . VAL   A 1 185 ? 13.303  -38.729 -25.603 1 36.15 ? 170 VAL   A CB  1 
ATOM   1374 C  CG1 . VAL   A 1 185 ? 14.694  -38.148 -25.351 1 36.25 ? 170 VAL   A CG1 1 
ATOM   1375 C  CG2 . VAL   A 1 185 ? 13.349  -39.797 -26.685 1 35.32 ? 170 VAL   A CG2 1 
ATOM   1376 N  N   . GLU   A 1 186 ? 12.038  -37.278 -22.989 1 38.28 ? 171 GLU   A N   1 
ATOM   1377 C  CA  . GLU   A 1 186 ? 12.009  -36.342 -21.848 1 38.82 ? 171 GLU   A CA  1 
ATOM   1378 C  C   . GLU   A 1 186 ? 11.87   -37.113 -20.531 1 40.17 ? 171 GLU   A C   1 
ATOM   1379 O  O   . GLU   A 1 186 ? 12.532  -36.778 -19.546 1 41.07 ? 171 GLU   A O   1 
ATOM   1380 C  CB  . GLU   A 1 186 ? 10.747  -35.45  -21.907 1 39.08 ? 171 GLU   A CB  1 
ATOM   1381 C  CG  . GLU   A 1 186 ? 10.894  -34.156 -22.647 1 41.38 ? 171 GLU   A CG  1 
ATOM   1382 C  CD  . GLU   A 1 186 ? 11.64   -33.052 -21.939 1 42.74 ? 171 GLU   A CD  1 
ATOM   1383 O  OE1 . GLU   A 1 186 ? 12.285  -32.275 -22.664 1 46.98 ? 171 GLU   A OE1 1 
ATOM   1384 O  OE2 . GLU   A 1 186 ? 11.588  -32.942 -20.695 1 40.52 ? 171 GLU   A OE2 1 
ATOM   1385 N  N   . ILE   A 1 187 ? 10.919  -38.064 -20.488 1 40.26 ? 172 ILE   A N   1 
ATOM   1386 C  CA  . ILE   A 1 187 ? 10.651  -38.86  -19.301 1 41.56 ? 172 ILE   A CA  1 
ATOM   1387 C  C   . ILE   A 1 187 ? 11.844  -39.757 -18.963 1 42.74 ? 172 ILE   A C   1 
ATOM   1388 O  O   . ILE   A 1 187 ? 12.244  -39.812 -17.8   1 43.53 ? 172 ILE   A O   1 
ATOM   1389 C  CB  . ILE   A 1 187 ? 9.317   -39.628 -19.461 1 41.76 ? 172 ILE   A CB  1 
ATOM   1390 C  CG1 . ILE   A 1 187 ? 8.119   -38.653 -19.387 1 41.97 ? 172 ILE   A CG1 1 
ATOM   1391 C  CG2 . ILE   A 1 187 ? 9.186   -40.762 -18.44  1 42.48 ? 172 ILE   A CG2 1 
ATOM   1392 C  CD1 . ILE   A 1 187 ? 6.765   -39.291 -19.74  1 42.92 ? 172 ILE   A CD1 1 
ATOM   1393 N  N   . ALA   A 1 188 ? 12.458  -40.396 -19.979 1 42.53 ? 173 ALA   A N   1 
ATOM   1394 C  CA  . ALA   A 1 188 ? 13.614  -41.267 -19.78  1 42.74 ? 173 ALA   A CA  1 
ATOM   1395 C  C   . ALA   A 1 188 ? 14.783  -40.469 -19.197 1 44.46 ? 173 ALA   A C   1 
ATOM   1396 O  O   . ALA   A 1 188 ? 15.435  -40.926 -18.248 1 44.29 ? 173 ALA   A O   1 
ATOM   1397 C  CB  . ALA   A 1 188 ? 14.013  -41.931 -21.099 1 41.87 ? 173 ALA   A CB  1 
ATOM   1398 N  N   . ALA   A 1 189 ? 15.023  -39.257 -19.742 1 45.52 ? 174 ALA   A N   1 
ATOM   1399 C  CA  . ALA   A 1 189 ? 16.09   -38.374 -19.276 1 46.64 ? 174 ALA   A CA  1 
ATOM   1400 C  C   . ALA   A 1 189 ? 15.844  -37.819 -17.864 1 47.9  ? 174 ALA   A C   1 
ATOM   1401 O  O   . ALA   A 1 189 ? 16.8    -37.47  -17.162 1 48.47 ? 174 ALA   A O   1 
ATOM   1402 C  CB  . ALA   A 1 189 ? 16.294  -37.231 -20.265 1 46.78 ? 174 ALA   A CB  1 
ATOM   1403 N  N   . ALA   A 1 190 ? 14.582  -37.764 -17.443 1 48.22 ? 175 ALA   A N   1 
ATOM   1404 C  CA  . ALA   A 1 190 ? 14.156  -37.256 -16.141 1 49.36 ? 175 ALA   A CA  1 
ATOM   1405 C  C   . ALA   A 1 190 ? 14.619  -38.085 -14.968 1 49.46 ? 175 ALA   A C   1 
ATOM   1406 O  O   . ALA   A 1 190 ? 14.759  -37.545 -13.865 1 50.53 ? 175 ALA   A O   1 
ATOM   1407 C  CB  . ALA   A 1 190 ? 12.645  -37.125 -16.102 1 49.99 ? 175 ALA   A CB  1 
ATOM   1408 N  N   . SER   A 1 191 ? 14.845  -39.387 -15.176 1 48.51 ? 176 SER   A N   1 
ATOM   1409 C  CA  . SER   A 1 191 ? 15.347  -40.237 -14.096 1 48.4  ? 176 SER   A CA  1 
ATOM   1410 C  C   . SER   A 1 191 ? 16.796  -39.847 -13.689 1 48.06 ? 176 SER   A C   1 
ATOM   1411 O  O   . SER   A 1 191 ? 17.231  -40.194 -12.599 1 48.08 ? 176 SER   A O   1 
ATOM   1412 C  CB  . SER   A 1 191 ? 15.242  -41.713 -14.466 1 49.27 ? 176 SER   A CB  1 
ATOM   1413 O  OG  . SER   A 1 191 ? 15.98   -41.995 -15.64  1 51.86 ? 176 SER   A OG  1 
ATOM   1414 N  N   . ALA   A 1 192 ? 17.518  -39.095 -14.537 1 47.51 ? 177 ALA   A N   1 
ATOM   1415 C  CA  . ALA   A 1 192 ? 18.852  -38.614 -14.202 1 47.7  ? 177 ALA   A CA  1 
ATOM   1416 C  C   . ALA   A 1 192 ? 18.819  -37.288 -13.408 1 48.05 ? 177 ALA   A C   1 
ATOM   1417 O  O   . ALA   A 1 192 ? 19.802  -36.956 -12.758 1 47.33 ? 177 ALA   A O   1 
ATOM   1418 C  CB  . ALA   A 1 192 ? 19.681  -38.455 -15.461 1 47.6  ? 177 ALA   A CB  1 
ATOM   1419 N  N   . ILE   A 1 193 ? 17.692  -36.546 -13.444 1 48.74 ? 178 ILE   A N   1 
ATOM   1420 C  CA  . ILE   A 1 193 ? 17.52   -35.266 -12.743 1 49.85 ? 178 ILE   A CA  1 
ATOM   1421 C  C   . ILE   A 1 193 ? 17.565  -35.458 -11.241 1 50.07 ? 178 ILE   A C   1 
ATOM   1422 O  O   . ILE   A 1 193 ? 18.129  -34.623 -10.535 1 49.81 ? 178 ILE   A O   1 
ATOM   1423 C  CB  . ILE   A 1 193 ? 16.201  -34.558 -13.172 1 51.08 ? 178 ILE   A CB  1 
ATOM   1424 C  CG1 . ILE   A 1 193 ? 16.222  -34.191 -14.667 1 52.8  ? 178 ILE   A CG1 1 
ATOM   1425 C  CG2 . ILE   A 1 193 ? 15.904  -33.329 -12.311 1 51.38 ? 178 ILE   A CG2 1 
ATOM   1426 C  CD1 . ILE   A 1 193 ? 14.873  -33.744 -15.173 1 54.4  ? 178 ILE   A CD1 1 
ATOM   1427 N  N   . LYS   A 1 194 ? 16.981  -36.556 -10.743 1 50.27 ? 179 LYS   A N   1 
ATOM   1428 C  CA  . LYS   A 1 194 ? 16.992  -36.842 -9.308  1 50.54 ? 179 LYS   A CA  1 
ATOM   1429 C  C   . LYS   A 1 194 ? 18.428  -37.042 -8.755  1 50.38 ? 179 LYS   A C   1 
ATOM   1430 O  O   . LYS   A 1 194 ? 18.661  -36.88  -7.554  1 51.45 ? 179 LYS   A O   1 
ATOM   1431 C  CB  . LYS   A 1 194 ? 16.092  -38.053 -8.996  1 52.7  ? 179 LYS   A CB  1 
ATOM   1432 C  CG  . LYS   A 1 194 ? 16.67   -39.391 -9.432  1 56.72 ? 179 LYS   A CG  1 
ATOM   1433 C  CD  . LYS   A 1 194 ? 15.782  -40.562 -9.019  1 60.52 ? 179 LYS   A CD  1 
ATOM   1434 C  CE  . LYS   A 1 194 ? 14.751  -40.906 -10.064 1 64.25 ? 179 LYS   A CE  1 
ATOM   1435 N  NZ  . LYS   A 1 194 ? 15.063  -42.206 -10.728 1 66.58 ? 179 LYS   A NZ  1 
ATOM   1436 N  N   . VAL   A 1 195 ? 19.391  -37.361 -9.636  1 48.79 ? 180 VAL   A N   1 
ATOM   1437 C  CA  . VAL   A 1 195 ? 20.789  -37.555 -9.275  1 47.57 ? 180 VAL   A CA  1 
ATOM   1438 C  C   . VAL   A 1 195 ? 21.547  -36.204 -9.138  1 47.46 ? 180 VAL   A C   1 
ATOM   1439 O  O   . VAL   A 1 195 ? 22.586  -36.151 -8.476  1 47.65 ? 180 VAL   A O   1 
ATOM   1440 C  CB  . VAL   A 1 195 ? 21.479  -38.53  -10.256 1 47.19 ? 180 VAL   A CB  1 
ATOM   1441 C  CG1 . VAL   A 1 195 ? 22.88   -38.866 -9.796  1 47.54 ? 180 VAL   A CG1 1 
ATOM   1442 C  CG2 . VAL   A 1 195 ? 20.66   -39.808 -10.443 1 47.22 ? 180 VAL   A CG2 1 
ATOM   1443 N  N   . ILE   A 1 196 ? 21.02   -35.111 -9.724  1 46.77 ? 181 ILE   A N   1 
ATOM   1444 C  CA  . ILE   A 1 196 ? 21.646  -33.788 -9.657  1 46.74 ? 181 ILE   A CA  1 
ATOM   1445 C  C   . ILE   A 1 196 ? 21.982  -33.356 -8.2    1 47.09 ? 181 ILE   A C   1 
ATOM   1446 O  O   . ILE   A 1 196 ? 23.133  -32.994 -7.957  1 46.93 ? 181 ILE   A O   1 
ATOM   1447 C  CB  . ILE   A 1 196 ? 20.824  -32.717 -10.434 1 46.97 ? 181 ILE   A CB  1 
ATOM   1448 C  CG1 . ILE   A 1 196 ? 20.952  -32.916 -11.957 1 47.03 ? 181 ILE   A CG1 1 
ATOM   1449 C  CG2 . ILE   A 1 196 ? 21.204  -31.274 -10.028 1 47.56 ? 181 ILE   A CG2 1 
ATOM   1450 C  CD1 . ILE   A 1 196 ? 20.09   -31.961 -12.795 1 47.62 ? 181 ILE   A CD1 1 
ATOM   1451 N  N   . PRO   A 1 197 ? 21.057  -33.419 -7.213  1 47.36 ? 182 PRO   A N   1 
ATOM   1452 C  CA  . PRO   A 1 197 ? 21.439  -33.028 -5.841  1 47.5  ? 182 PRO   A CA  1 
ATOM   1453 C  C   . PRO   A 1 197 ? 22.51   -33.935 -5.225  1 47.46 ? 182 PRO   A C   1 
ATOM   1454 O  O   . PRO   A 1 197 ? 23.293  -33.481 -4.389  1 47.31 ? 182 PRO   A O   1 
ATOM   1455 C  CB  . PRO   A 1 197 ? 20.112  -33.049 -5.071  1 48.25 ? 182 PRO   A CB  1 
ATOM   1456 C  CG  . PRO   A 1 197 ? 19.216  -33.918 -5.872  1 48.71 ? 182 PRO   A CG  1 
ATOM   1457 C  CD  . PRO   A 1 197 ? 19.63   -33.796 -7.293  1 46.9  ? 182 PRO   A CD  1 
ATOM   1458 N  N   . THR   A 1 198 ? 22.561  -35.216 -5.64   1 47.14 ? 183 THR   A N   1 
ATOM   1459 C  CA  . THR   A 1 198 ? 23.588  -36.158 -5.171  1 46.55 ? 183 THR   A CA  1 
ATOM   1460 C  C   . THR   A 1 198 ? 24.97   -35.689 -5.657  1 45.57 ? 183 THR   A C   1 
ATOM   1461 O  O   . THR   A 1 198 ? 25.928  -35.742 -4.895  1 45.58 ? 183 THR   A O   1 
ATOM   1462 C  CB  . THR   A 1 198 ? 23.286  -37.572 -5.674  1 47.88 ? 183 THR   A CB  1 
ATOM   1463 O  OG1 . THR   A 1 198 ? 21.925  -37.895 -5.41   1 49.12 ? 183 THR   A OG1 1 
ATOM   1464 C  CG2 . THR   A 1 198 ? 24.182  -38.615 -5.043  1 48.07 ? 183 THR   A CG2 1 
ATOM   1465 N  N   . VAL   A 1 199 ? 25.053  -35.184 -6.907  1 44.53 ? 184 VAL   A N   1 
ATOM   1466 C  CA  . VAL   A 1 199 ? 26.284  -34.658 -7.507  1 44.52 ? 184 VAL   A CA  1 
ATOM   1467 C  C   . VAL   A 1 199 ? 26.808  -33.411 -6.774  1 45.68 ? 184 VAL   A C   1 
ATOM   1468 O  O   . VAL   A 1 199 ? 27.987  -33.357 -6.43   1 45.63 ? 184 VAL   A O   1 
ATOM   1469 C  CB  . VAL   A 1 199 ? 26.098  -34.406 -9.022  1 44.09 ? 184 VAL   A CB  1 
ATOM   1470 C  CG1 . VAL   A 1 199 ? 27.288  -33.677 -9.616  1 44.14 ? 184 VAL   A CG1 1 
ATOM   1471 C  CG2 . VAL   A 1 199 ? 25.832  -35.715 -9.761  1 44.05 ? 184 VAL   A CG2 1 
ATOM   1472 N  N   . PHE   A 1 200 ? 25.937  -32.428 -6.509  1 46.47 ? 185 PHE   A N   1 
ATOM   1473 C  CA  . PHE   A 1 200 ? 26.348  -31.218 -5.804  1 47.81 ? 185 PHE   A CA  1 
ATOM   1474 C  C   . PHE   A 1 200 ? 26.694  -31.474 -4.338  1 48.11 ? 185 PHE   A C   1 
ATOM   1475 O  O   . PHE   A 1 200 ? 27.589  -30.819 -3.806  1 47.99 ? 185 PHE   A O   1 
ATOM   1476 C  CB  . PHE   A 1 200 ? 25.297  -30.1   -5.961  1 48.59 ? 185 PHE   A CB  1 
ATOM   1477 C  CG  . PHE   A 1 200 ? 25.271  -29.553 -7.37   1 50.15 ? 185 PHE   A CG  1 
ATOM   1478 C  CD1 . PHE   A 1 200 ? 26.389  -28.951 -7.916  1 51.01 ? 185 PHE   A CD1 1 
ATOM   1479 C  CD2 . PHE   A 1 200 ? 24.145  -29.673 -8.159  1 51.47 ? 185 PHE   A CD2 1 
ATOM   1480 C  CE1 . PHE   A 1 200 ? 26.389  -28.495 -9.23   1 51.88 ? 185 PHE   A CE1 1 
ATOM   1481 C  CE2 . PHE   A 1 200 ? 24.136  -29.175 -9.463  1 52.56 ? 185 PHE   A CE2 1 
ATOM   1482 C  CZ  . PHE   A 1 200 ? 25.26   -28.582 -9.987  1 52.04 ? 185 PHE   A CZ  1 
ATOM   1483 N  N   . LYS   A 1 201 ? 26.002  -32.423 -3.687  1 48.18 ? 186 LYS   A N   1 
ATOM   1484 C  CA  . LYS   A 1 201 ? 26.303  -32.752 -2.295  1 48.96 ? 186 LYS   A CA  1 
ATOM   1485 C  C   . LYS   A 1 201 ? 27.65   -33.481 -2.232  1 49.85 ? 186 LYS   A C   1 
ATOM   1486 O  O   . LYS   A 1 201 ? 28.476  -33.153 -1.38   1 50.31 ? 186 LYS   A O   1 
ATOM   1487 C  CB  . LYS   A 1 201 ? 25.182  -33.59  -1.64   1 49.8  ? 186 LYS   A CB  1 
ATOM   1488 N  N   . ALA   A 1 202 ? 27.897  -34.414 -3.17   1 49.71 ? 187 ALA   A N   1 
ATOM   1489 C  CA  . ALA   A 1 202 ? 29.16   -35.156 -3.228  1 50.24 ? 187 ALA   A CA  1 
ATOM   1490 C  C   . ALA   A 1 202 ? 30.334  -34.231 -3.458  1 51.16 ? 187 ALA   A C   1 
ATOM   1491 O  O   . ALA   A 1 202 ? 31.373  -34.423 -2.836  1 51.67 ? 187 ALA   A O   1 
ATOM   1492 C  CB  . ALA   A 1 202 ? 29.116  -36.215 -4.317  1 49.9  ? 187 ALA   A CB  1 
ATOM   1493 N  N   . MET   A 1 203 ? 30.178  -33.206 -4.308  1 51.28 ? 188 MET   A N   1 
ATOM   1494 C  CA  . MET   A 1 203 ? 31.264  -32.25  -4.551  1 51.8  ? 188 MET   A CA  1 
ATOM   1495 C  C   . MET   A 1 203 ? 31.578  -31.425 -3.297  1 53.32 ? 188 MET   A C   1 
ATOM   1496 O  O   . MET   A 1 203 ? 32.749  -31.274 -2.939  1 53.46 ? 188 MET   A O   1 
ATOM   1497 C  CB  . MET   A 1 203 ? 30.915  -31.305 -5.699  1 51.43 ? 188 MET   A CB  1 
ATOM   1498 C  CG  . MET   A 1 203 ? 30.942  -31.942 -7.059  1 52.65 ? 188 MET   A CG  1 
ATOM   1499 S  SD  . MET   A 1 203 ? 31.074  -30.636 -8.318  1 53.69 ? 188 MET   A SD  1 
ATOM   1500 C  CE  . MET   A 1 203 ? 29.564  -29.896 -8.171  1 46.71 ? 188 MET   A CE  1 
ATOM   1501 N  N   . GLN   A 1 204 ? 30.531  -30.9   -2.628  1 54.34 ? 189 GLN   A N   1 
ATOM   1502 C  CA  . GLN   A 1 204 ? 30.633  -30.065 -1.427  1 55.76 ? 189 GLN   A CA  1 
ATOM   1503 C  C   . GLN   A 1 204 ? 31.292  -30.839 -0.284  1 56.31 ? 189 GLN   A C   1 
ATOM   1504 O  O   . GLN   A 1 204 ? 32.281  -30.383 0.294   1 56.61 ? 189 GLN   A O   1 
ATOM   1505 C  CB  . GLN   A 1 204 ? 29.226  -29.544 -1.044  1 58.46 ? 189 GLN   A CB  1 
ATOM   1506 C  CG  . GLN   A 1 204 ? 29.053  -29.052 0.382   1 64.16 ? 189 GLN   A CG  1 
ATOM   1507 C  CD  . GLN   A 1 204 ? 29.817  -27.78  0.621   1 71.16 ? 189 GLN   A CD  1 
ATOM   1508 O  OE1 . GLN   A 1 204 ? 30.007  -26.95  -0.291  1 72.82 ? 189 GLN   A OE1 1 
ATOM   1509 N  NE2 . GLN   A 1 204 ? 30.265  -27.598 1.866   1 72.77 ? 189 GLN   A NE2 1 
ATOM   1510 N  N   . MET   A 1 205 ? 30.765  -32.033 0.007   1 56.22 ? 190 MET   A N   1 
ATOM   1511 C  CA  . MET   A 1 205 ? 31.284  -32.898 1.051   1 56.44 ? 190 MET   A CA  1 
ATOM   1512 C  C   . MET   A 1 205 ? 32.546  -33.663 0.65    1 56.01 ? 190 MET   A C   1 
ATOM   1513 O  O   . MET   A 1 205 ? 33.017  -34.47  1.448   1 57.22 ? 190 MET   A O   1 
ATOM   1514 C  CB  . MET   A 1 205 ? 30.204  -33.886 1.48    1 57.96 ? 190 MET   A CB  1 
ATOM   1515 C  CG  . MET   A 1 205 ? 29.005  -33.22  2.087   1 63.37 ? 190 MET   A CG  1 
ATOM   1516 S  SD  . MET   A 1 205 ? 27.63   -34.368 2.38    1 79.23 ? 190 MET   A SD  1 
ATOM   1517 C  CE  . MET   A 1 205 ? 28.504  -35.781 3.217   1 79.45 ? 190 MET   A CE  1 
ATOM   1518 N  N   . GLN   A 1 206 ? 33.067  -33.462 -0.577  1 54.29 ? 191 GLN   A N   1 
ATOM   1519 C  CA  . GLN   A 1 206 ? 34.252  -34.141 -1.088  1 53.26 ? 191 GLN   A CA  1 
ATOM   1520 C  C   . GLN   A 1 206 ? 34.119  -35.661 -0.973  1 52.11 ? 191 GLN   A C   1 
ATOM   1521 O  O   . GLN   A 1 206 ? 34.983  -36.318 -0.415  1 52.74 ? 191 GLN   A O   1 
ATOM   1522 C  CB  . GLN   A 1 206 ? 35.526  -33.628 -0.399  1 54.85 ? 191 GLN   A CB  1 
ATOM   1523 C  CG  . GLN   A 1 206 ? 35.889  -32.185 -0.735  1 59.02 ? 191 GLN   A CG  1 
ATOM   1524 C  CD  . GLN   A 1 206 ? 36.603  -32.077 -2.068  1 64.88 ? 191 GLN   A CD  1 
ATOM   1525 O  OE1 . GLN   A 1 206 ? 37.29   -33.01  -2.531  1 67.12 ? 191 GLN   A OE1 1 
ATOM   1526 N  NE2 . GLN   A 1 206 ? 36.468  -30.928 -2.714  1 65.64 ? 191 GLN   A NE2 1 
ATOM   1527 N  N   . GLU   A 1 207 ? 33.003  -36.203 -1.442  1 50.46 ? 192 GLU   A N   1 
ATOM   1528 C  CA  . GLU   A 1 207 ? 32.716  -37.631 -1.426  1 49.14 ? 192 GLU   A CA  1 
ATOM   1529 C  C   . GLU   A 1 207 ? 32.97   -38.166 -2.832  1 47.73 ? 192 GLU   A C   1 
ATOM   1530 O  O   . GLU   A 1 207 ? 32.049  -38.266 -3.648  1 47.53 ? 192 GLU   A O   1 
ATOM   1531 C  CB  . GLU   A 1 207 ? 31.261  -37.873 -0.997  1 50.69 ? 192 GLU   A CB  1 
ATOM   1532 C  CG  . GLU   A 1 207 ? 30.956  -37.383 0.406   1 56.22 ? 192 GLU   A CG  1 
ATOM   1533 C  CD  . GLU   A 1 207 ? 31.493  -38.269 1.513   1 66.03 ? 192 GLU   A CD  1 
ATOM   1534 O  OE1 . GLU   A 1 207 ? 31.603  -39.496 1.287   1 67.99 ? 192 GLU   A OE1 1 
ATOM   1535 O  OE2 . GLU   A 1 207 ? 31.794  -37.741 2.611   1 69.47 ? 192 GLU   A OE2 1 
ATOM   1536 N  N   . ARG   A 1 208 ? 34.234  -38.461 -3.123  1 46.55 ? 193 ARG   A N   1 
ATOM   1537 C  CA  . ARG   A 1 208 ? 34.682  -38.939 -4.43   1 46.1  ? 193 ARG   A CA  1 
ATOM   1538 C  C   . ARG   A 1 208 ? 33.906  -40.166 -4.961  1 46.41 ? 193 ARG   A C   1 
ATOM   1539 O  O   . ARG   A 1 208 ? 33.489  -40.163 -6.121  1 46.74 ? 193 ARG   A O   1 
ATOM   1540 C  CB  . ARG   A 1 208 ? 36.196  -39.217 -4.402  1 45.53 ? 193 ARG   A CB  1 
ATOM   1541 C  CG  . ARG   A 1 208 ? 36.777  -39.693 -5.724  1 44.92 ? 193 ARG   A CG  1 
ATOM   1542 C  CD  . ARG   A 1 208 ? 36.856  -41.198 -5.801  1 44.52 ? 193 ARG   A CD  1 
ATOM   1543 N  NE  . ARG   A 1 208 ? 37.528  -41.657 -7.009  1 43.46 ? 193 ARG   A NE  1 
ATOM   1544 C  CZ  . ARG   A 1 208 ? 37.498  -42.907 -7.456  1 44.37 ? 193 ARG   A CZ  1 
ATOM   1545 N  NH1 . ARG   A 1 208 ? 36.785  -43.831 -6.821  1 43.91 ? 193 ARG   A NH1 1 
ATOM   1546 N  NH2 . ARG   A 1 208 ? 38.158  -43.239 -8.558  1 43.47 ? 193 ARG   A NH2 1 
ATOM   1547 N  N   . ASP   A 1 209 ? 33.766  -41.218 -4.142  1 45.83 ? 194 ASP   A N   1 
ATOM   1548 C  CA  . ASP   A 1 209 ? 33.093  -42.428 -4.58   1 45.97 ? 194 ASP   A CA  1 
ATOM   1549 C  C   . ASP   A 1 209 ? 31.624  -42.184 -4.861  1 46.4  ? 194 ASP   A C   1 
ATOM   1550 O  O   . ASP   A 1 209 ? 31.095  -42.731 -5.83   1 46.7  ? 194 ASP   A O   1 
ATOM   1551 C  CB  . ASP   A 1 209 ? 33.278  -43.561 -3.571  1 47.45 ? 194 ASP   A CB  1 
ATOM   1552 C  CG  . ASP   A 1 209 ? 34.725  -43.991 -3.346  1 51.4  ? 194 ASP   A CG  1 
ATOM   1553 O  OD1 . ASP   A 1 209 ? 35.526  -43.948 -4.314  1 51.91 ? 194 ASP   A OD1 1 
ATOM   1554 O  OD2 . ASP   A 1 209 ? 35.05   -44.386 -2.218  1 52.99 ? 194 ASP   A OD2 1 
ATOM   1555 N  N   . THR   A 1 210 ? 30.976  -41.333 -4.044  1 46.09 ? 195 THR   A N   1 
ATOM   1556 C  CA  . THR   A 1 210 ? 29.569  -40.968 -4.226  1 46.1  ? 195 THR   A CA  1 
ATOM   1557 C  C   . THR   A 1 210 ? 29.399  -40.254 -5.576  1 45.6  ? 195 THR   A C   1 
ATOM   1558 O  O   . THR   A 1 210 ? 28.527  -40.633 -6.348  1 46.22 ? 195 THR   A O   1 
ATOM   1559 C  CB  . THR   A 1 210 ? 29.075  -40.103 -3.049  1 46.94 ? 195 THR   A CB  1 
ATOM   1560 O  OG1 . THR   A 1 210 ? 29.162  -40.863 -1.85   1 47.28 ? 195 THR   A OG1 1 
ATOM   1561 C  CG2 . THR   A 1 210 ? 27.626  -39.639 -3.233  1 47.28 ? 195 THR   A CG2 1 
ATOM   1562 N  N   . LEU   A 1 211 ? 30.278  -39.278 -5.875  1 44.47 ? 196 LEU   A N   1 
ATOM   1563 C  CA  . LEU   A 1 211 ? 30.281  -38.51  -7.116  1 44.03 ? 196 LEU   A CA  1 
ATOM   1564 C  C   . LEU   A 1 211 ? 30.437  -39.408 -8.33   1 44.89 ? 196 LEU   A C   1 
ATOM   1565 O  O   . LEU   A 1 211 ? 29.717  -39.243 -9.31   1 45.4  ? 196 LEU   A O   1 
ATOM   1566 C  CB  . LEU   A 1 211 ? 31.394  -37.453 -7.096  1 43.36 ? 196 LEU   A CB  1 
ATOM   1567 C  CG  . LEU   A 1 211 ? 31.492  -36.539 -8.322  1 44.15 ? 196 LEU   A CG  1 
ATOM   1568 C  CD1 . LEU   A 1 211 ? 30.192  -35.761 -8.537  1 44.85 ? 196 LEU   A CD1 1 
ATOM   1569 C  CD2 . LEU   A 1 211 ? 32.651  -35.592 -8.198  1 43.56 ? 196 LEU   A CD2 1 
ATOM   1570 N  N   . LEU   A 1 212 ? 31.347  -40.375 -8.258  1 44.81 ? 197 LEU   A N   1 
ATOM   1571 C  CA  . LEU   A 1 212 ? 31.59   -41.285 -9.362  1 45.01 ? 197 LEU   A CA  1 
ATOM   1572 C  C   . LEU   A 1 212 ? 30.362  -42.144 -9.647  1 44.44 ? 197 LEU   A C   1 
ATOM   1573 O  O   . LEU   A 1 212 ? 29.999  -42.333 -10.817 1 44.82 ? 197 LEU   A O   1 
ATOM   1574 C  CB  . LEU   A 1 212 ? 32.819  -42.153 -9.038  1 45.63 ? 197 LEU   A CB  1 
ATOM   1575 C  CG  . LEU   A 1 212 ? 33.508  -42.822 -10.213 1 47.28 ? 197 LEU   A CG  1 
ATOM   1576 C  CD1 . LEU   A 1 212 ? 34.924  -43.151 -9.867  1 47.98 ? 197 LEU   A CD1 1 
ATOM   1577 C  CD2 . LEU   A 1 212 ? 32.85   -44.112 -10.553 1 48.17 ? 197 LEU   A CD2 1 
ATOM   1578 N  N   . LYS   A 1 213 ? 29.731  -42.674 -8.593  1 43.57 ? 198 LYS   A N   1 
ATOM   1579 C  CA  . LYS   A 1 213 ? 28.535  -43.502 -8.74   1 43.13 ? 198 LYS   A CA  1 
ATOM   1580 C  C   . LYS   A 1 213 ? 27.39   -42.676 -9.35   1 42.29 ? 198 LYS   A C   1 
ATOM   1581 O  O   . LYS   A 1 213 ? 26.691  -43.154 -10.239 1 42.45 ? 198 LYS   A O   1 
ATOM   1582 C  CB  . LYS   A 1 213 ? 28.112  -44.093 -7.387  1 44.45 ? 198 LYS   A CB  1 
ATOM   1583 N  N   . ALA   A 1 214 ? 27.236  -41.435 -8.888  1 41.41 ? 199 ALA   A N   1 
ATOM   1584 C  CA  . ALA   A 1 214 ? 26.232  -40.486 -9.355  1 41.09 ? 199 ALA   A CA  1 
ATOM   1585 C  C   . ALA   A 1 214 ? 26.425  -40.154 -10.851 1 41.32 ? 199 ALA   A C   1 
ATOM   1586 O  O   . ALA   A 1 214 ? 25.462  -40.212 -11.617 1 41.46 ? 199 ALA   A O   1 
ATOM   1587 C  CB  . ALA   A 1 214 ? 26.284  -39.21  -8.511  1 40.77 ? 199 ALA   A CB  1 
ATOM   1588 N  N   . LEU   A 1 215 ? 27.672  -39.873 -11.278 1 40.72 ? 200 LEU   A N   1 
ATOM   1589 C  CA  . LEU   A 1 215 ? 27.953  -39.591 -12.676 1 40.42 ? 200 LEU   A CA  1 
ATOM   1590 C  C   . LEU   A 1 215 ? 27.675  -40.799 -13.561 1 41.28 ? 200 LEU   A C   1 
ATOM   1591 O  O   . LEU   A 1 215 ? 27.124  -40.64  -14.651 1 41.81 ? 200 LEU   A O   1 
ATOM   1592 C  CB  . LEU   A 1 215 ? 29.377  -39.098 -12.865 1 39.77 ? 200 LEU   A CB  1 
ATOM   1593 C  CG  . LEU   A 1 215 ? 29.697  -37.734 -12.271 1 40.18 ? 200 LEU   A CG  1 
ATOM   1594 C  CD1 . LEU   A 1 215 ? 31.186  -37.428 -12.377 1 39.84 ? 200 LEU   A CD1 1 
ATOM   1595 C  CD2 . LEU   A 1 215 ? 28.869  -36.637 -12.947 1 40.74 ? 200 LEU   A CD2 1 
ATOM   1596 N  N   . LEU   A 1 216 ? 28.012  -42.01  -13.092 1 41.12 ? 201 LEU   A N   1 
ATOM   1597 C  CA  . LEU   A 1 216 ? 27.734  -43.225 -13.86  1 41.01 ? 201 LEU   A CA  1 
ATOM   1598 C  C   . LEU   A 1 216 ? 26.228  -43.52  -13.937 1 40.76 ? 201 LEU   A C   1 
ATOM   1599 O  O   . LEU   A 1 216 ? 25.776  -44.138 -14.898 1 40.63 ? 201 LEU   A O   1 
ATOM   1600 C  CB  . LEU   A 1 216 ? 28.473  -44.432 -13.286 1 41.62 ? 201 LEU   A CB  1 
ATOM   1601 C  CG  . LEU   A 1 216 ? 29.977  -44.459 -13.538 1 43.53 ? 201 LEU   A CG  1 
ATOM   1602 C  CD1 . LEU   A 1 216 ? 30.625  -45.605 -12.777 1 44.28 ? 201 LEU   A CD1 1 
ATOM   1603 C  CD2 . LEU   A 1 216 ? 30.274  -44.583 -15.012 1 43.62 ? 201 LEU   A CD2 1 
ATOM   1604 N  N   . GLU   A 1 217 ? 25.458  -43.101 -12.929 1 40.42 ? 202 GLU   A N   1 
ATOM   1605 C  CA  . GLU   A 1 217 ? 24.017  -43.292 -12.923 1 40.74 ? 202 GLU   A CA  1 
ATOM   1606 C  C   . GLU   A 1 217 ? 23.337  -42.327 -13.916 1 40.57 ? 202 GLU   A C   1 
ATOM   1607 O  O   . GLU   A 1 217 ? 22.381  -42.715 -14.605 1 40.57 ? 202 GLU   A O   1 
ATOM   1608 C  CB  . GLU   A 1 217 ? 23.457  -43.123 -11.508 1 43.52 ? 202 GLU   A CB  1 
ATOM   1609 C  CG  . GLU   A 1 217 ? 21.954  -43.314 -11.416 1 50.66 ? 202 GLU   A CG  1 
ATOM   1610 C  CD  . GLU   A 1 217 ? 21.421  -44.647 -11.92  1 61.85 ? 202 GLU   A CD  1 
ATOM   1611 O  OE1 . GLU   A 1 217 ? 22.168  -45.653 -11.872 1 64.89 ? 202 GLU   A OE1 1 
ATOM   1612 O  OE2 . GLU   A 1 217 ? 20.246  -44.685 -12.356 1 65.14 ? 202 GLU   A OE2 1 
ATOM   1613 N  N   . ILE   A 1 218 ? 23.865  -41.096 -14.029 1 39.83 ? 203 ILE   A N   1 
ATOM   1614 C  CA  . ILE   A 1 218 ? 23.369  -40.109 -14.99  1 39.4  ? 203 ILE   A CA  1 
ATOM   1615 C  C   . ILE   A 1 218 ? 23.65   -40.634 -16.402 1 39.43 ? 203 ILE   A C   1 
ATOM   1616 O  O   . ILE   A 1 218 ? 22.762  -40.608 -17.242 1 39.69 ? 203 ILE   A O   1 
ATOM   1617 C  CB  . ILE   A 1 218 ? 24.035  -38.729 -14.746 1 39.07 ? 203 ILE   A CB  1 
ATOM   1618 C  CG1 . ILE   A 1 218 ? 23.48   -38.063 -13.466 1 39.09 ? 203 ILE   A CG1 1 
ATOM   1619 C  CG2 . ILE   A 1 218 ? 23.901  -37.806 -15.971 1 39.57 ? 203 ILE   A CG2 1 
ATOM   1620 C  CD1 . ILE   A 1 218 ? 24.234  -36.786 -13.087 1 39.93 ? 203 ILE   A CD1 1 
ATOM   1621 N  N   . ALA   A 1 219 ? 24.859  -41.162 -16.64  1 39.03 ? 204 ALA   A N   1 
ATOM   1622 C  CA  . ALA   A 1 219 ? 25.231  -41.712 -17.932 1 39.53 ? 204 ALA   A CA  1 
ATOM   1623 C  C   . ALA   A 1 219 ? 24.314  -42.872 -18.298 1 41.06 ? 204 ALA   A C   1 
ATOM   1624 O  O   . ALA   A 1 219 ? 23.806  -42.915 -19.404 1 40.95 ? 204 ALA   A O   1 
ATOM   1625 C  CB  . ALA   A 1 219 ? 26.683  -42.166 -17.926 1 38.99 ? 204 ALA   A CB  1 
ATOM   1626 N  N   . SER   A 1 220 ? 24.028  -43.758 -17.344 1 42.21 ? 205 SER   A N   1 
ATOM   1627 C  CA  . SER   A 1 220 ? 23.136  -44.888 -17.535 1 43.22 ? 205 SER   A CA  1 
ATOM   1628 C  C   . SER   A 1 220 ? 21.745  -44.428 -18.002 1 43.26 ? 205 SER   A C   1 
ATOM   1629 O  O   . SER   A 1 220 ? 21.19   -45.014 -18.919 1 43.39 ? 205 SER   A O   1 
ATOM   1630 C  CB  . SER   A 1 220 ? 23.035  -45.678 -16.238 1 46.05 ? 205 SER   A CB  1 
ATOM   1631 O  OG  . SER   A 1 220 ? 22.121  -46.753 -16.38  1 51.36 ? 205 SER   A OG  1 
ATOM   1632 N  N   . CYS   A 1 221 ? 21.216  -43.355 -17.41  1 43.38 ? 206 CYS   A N   1 
ATOM   1633 C  CA  . CYS   A 1 221 ? 19.912  -42.793 -17.774 1 43.96 ? 206 CYS   A CA  1 
ATOM   1634 C  C   . CYS   A 1 221 ? 19.905  -42.202 -19.173 1 43.5  ? 206 CYS   A C   1 
ATOM   1635 O  O   . CYS   A 1 221 ? 18.959  -42.427 -19.924 1 44.47 ? 206 CYS   A O   1 
ATOM   1636 C  CB  . CYS   A 1 221 ? 19.459  -41.767 -16.745 1 45.21 ? 206 CYS   A CB  1 
ATOM   1637 S  SG  . CYS   A 1 221 ? 19.181  -42.453 -15.095 1 51.99 ? 206 CYS   A SG  1 
ATOM   1638 N  N   . LEU   A 1 222 ? 20.947  -41.45  -19.523 1 42.1  ? 207 LEU   A N   1 
ATOM   1639 C  CA  . LEU   A 1 222 ? 21.069  -40.857 -20.85  1 41.26 ? 207 LEU   A CA  1 
ATOM   1640 C  C   . LEU   A 1 222 ? 21.278  -41.897 -21.938 1 41.23 ? 207 LEU   A C   1 
ATOM   1641 O  O   . LEU   A 1 222 ? 20.83   -41.684 -23.066 1 41.48 ? 207 LEU   A O   1 
ATOM   1642 C  CB  . LEU   A 1 222 ? 22.192  -39.822 -20.877 1 40.6  ? 207 LEU   A CB  1 
ATOM   1643 C  CG  . LEU   A 1 222 ? 22.014  -38.647 -19.938 1 41.09 ? 207 LEU   A CG  1 
ATOM   1644 C  CD1 . LEU   A 1 222 ? 23.252  -37.796 -19.934 1 41.47 ? 207 LEU   A CD1 1 
ATOM   1645 C  CD2 . LEU   A 1 222 ? 20.795  -37.822 -20.317 1 41.23 ? 207 LEU   A CD2 1 
ATOM   1646 N  N   . GLU   A 1 223 ? 21.958  -43.009 -21.614 1 40.89 ? 208 GLU   A N   1 
ATOM   1647 C  CA  . GLU   A 1 223 ? 22.185  -44.109 -22.557 1 41.43 ? 208 GLU   A CA  1 
ATOM   1648 C  C   . GLU   A 1 223 ? 20.861  -44.81  -22.852 1 42.06 ? 208 GLU   A C   1 
ATOM   1649 O  O   . GLU   A 1 223 ? 20.579  -45.125 -24.013 1 42.25 ? 208 GLU   A O   1 
ATOM   1650 C  CB  . GLU   A 1 223 ? 23.198  -45.111 -22.002 1 42.72 ? 208 GLU   A CB  1 
ATOM   1651 C  CG  . GLU   A 1 223 ? 24.642  -44.641 -22.009 1 46.34 ? 208 GLU   A CG  1 
ATOM   1652 C  CD  . GLU   A 1 223 ? 25.551  -45.383 -21.038 1 54    ? 208 GLU   A CD  1 
ATOM   1653 O  OE1 . GLU   A 1 223 ? 25.081  -46.337 -20.369 1 57.47 ? 208 GLU   A OE1 1 
ATOM   1654 O  OE2 . GLU   A 1 223 ? 26.738  -44.997 -20.936 1 53.4  ? 208 GLU   A OE2 1 
ATOM   1655 N  N   . LYS   A 1 224 ? 20.038  -45.016 -21.803 1 42.16 ? 209 LYS   A N   1 
ATOM   1656 C  CA  . LYS   A 1 224 ? 18.716  -45.637 -21.89  1 43.07 ? 209 LYS   A CA  1 
ATOM   1657 C  C   . LYS   A 1 224 ? 17.771  -44.778 -22.717 1 43.91 ? 209 LYS   A C   1 
ATOM   1658 O  O   . LYS   A 1 224 ? 16.98   -45.323 -23.495 1 45.3  ? 209 LYS   A O   1 
ATOM   1659 C  CB  . LYS   A 1 224 ? 18.127  -45.887 -20.485 1 45.04 ? 209 LYS   A CB  1 
ATOM   1660 N  N   . ALA   A 1 225 ? 17.879  -43.439 -22.592 1 42.79 ? 210 ALA   A N   1 
ATOM   1661 C  CA  . ALA   A 1 225 ? 17.083  -42.478 -23.35  1 42.26 ? 210 ALA   A CA  1 
ATOM   1662 C  C   . ALA   A 1 225 ? 17.322  -42.571 -24.876 1 42.6  ? 210 ALA   A C   1 
ATOM   1663 O  O   . ALA   A 1 225 ? 16.432  -42.221 -25.667 1 42.15 ? 210 ALA   A O   1 
ATOM   1664 C  CB  . ALA   A 1 225 ? 17.358  -41.067 -22.857 1 41.78 ? 210 ALA   A CB  1 
ATOM   1665 N  N   . LEU   A 1 226 ? 18.508  -43.038 -25.291 1 42.86 ? 211 LEU   A N   1 
ATOM   1666 C  CA  . LEU   A 1 226 ? 18.819  -43.223 -26.709 1 43.38 ? 211 LEU   A CA  1 
ATOM   1667 C  C   . LEU   A 1 226 ? 17.998  -44.375 -27.288 1 44.75 ? 211 LEU   A C   1 
ATOM   1668 O  O   . LEU   A 1 226 ? 17.539  -44.298 -28.422 1 45.5  ? 211 LEU   A O   1 
ATOM   1669 C  CB  . LEU   A 1 226 ? 20.319  -43.474 -26.898 1 43.17 ? 211 LEU   A CB  1 
ATOM   1670 C  CG  . LEU   A 1 226 ? 20.789  -43.759 -28.326 1 44.12 ? 211 LEU   A CG  1 
ATOM   1671 C  CD1 . LEU   A 1 226 ? 20.441  -42.611 -29.264 1 43.91 ? 211 LEU   A CD1 1 
ATOM   1672 C  CD2 . LEU   A 1 226 ? 22.277  -44.013 -28.356 1 44.75 ? 211 LEU   A CD2 1 
ATOM   1673 N  N   . GLN   A 1 227 ? 17.797  -45.437 -26.512 1 45.37 ? 212 GLN   A N   1 
ATOM   1674 C  CA  . GLN   A 1 227 ? 16.988  -46.571 -26.946 1 46.41 ? 212 GLN   A CA  1 
ATOM   1675 C  C   . GLN   A 1 227 ? 15.531  -46.154 -27.148 1 46.44 ? 212 GLN   A C   1 
ATOM   1676 O  O   . GLN   A 1 227 ? 14.891  -46.601 -28.099 1 47.23 ? 212 GLN   A O   1 
ATOM   1677 C  CB  . GLN   A 1 227 ? 17.124  -47.732 -25.942 1 49.08 ? 212 GLN   A CB  1 
ATOM   1678 C  CG  . GLN   A 1 227 ? 18.578  -48.203 -25.785 1 54.05 ? 212 GLN   A CG  1 
ATOM   1679 C  CD  . GLN   A 1 227 ? 19.164  -48.686 -27.106 1 59.26 ? 212 GLN   A CD  1 
ATOM   1680 O  OE1 . GLN   A 1 227 ? 18.574  -49.516 -27.813 1 61.75 ? 212 GLN   A OE1 1 
ATOM   1681 N  NE2 . GLN   A 1 227 ? 20.323  -48.161 -27.478 1 58.58 ? 212 GLN   A NE2 1 
ATOM   1682 N  N   . VAL   A 1 228 ? 15.025  -45.264 -26.276 1 45.42 ? 213 VAL   A N   1 
ATOM   1683 C  CA  . VAL   A 1 228 ? 13.677  -44.691 -26.34  1 44.72 ? 213 VAL   A CA  1 
ATOM   1684 C  C   . VAL   A 1 228 ? 13.478  -43.909 -27.642 1 44.99 ? 213 VAL   A C   1 
ATOM   1685 O  O   . VAL   A 1 228 ? 12.433  -44.02  -28.249 1 45.75 ? 213 VAL   A O   1 
ATOM   1686 C  CB  . VAL   A 1 228 ? 13.407  -43.818 -25.092 1 44.25 ? 213 VAL   A CB  1 
ATOM   1687 C  CG1 . VAL   A 1 228 ? 12.138  -43.002 -25.252 1 44.65 ? 213 VAL   A CG1 1 
ATOM   1688 C  CG2 . VAL   A 1 228 ? 13.337  -44.67  -23.839 1 43.92 ? 213 VAL   A CG2 1 
ATOM   1689 N  N   . PHE   A 1 229 ? 14.503  -43.183 -28.094 1 45.23 ? 214 PHE   A N   1 
ATOM   1690 C  CA  . PHE   A 1 229 ? 14.54   -42.41  -29.331 1 46.03 ? 214 PHE   A CA  1 
ATOM   1691 C  C   . PHE   A 1 229 ? 14.315  -43.287 -30.57  1 46.37 ? 214 PHE   A C   1 
ATOM   1692 O  O   . PHE   A 1 229 ? 13.781  -42.792 -31.56  1 46.97 ? 214 PHE   A O   1 
ATOM   1693 C  CB  . PHE   A 1 229 ? 15.921  -41.781 -29.467 1 46.85 ? 214 PHE   A CB  1 
ATOM   1694 C  CG  . PHE   A 1 229 ? 16.001  -40.325 -29.842 1 48.75 ? 214 PHE   A CG  1 
ATOM   1695 C  CD1 . PHE   A 1 229 ? 15.767  -39.911 -31.143 1 49.72 ? 214 PHE   A CD1 1 
ATOM   1696 C  CD2 . PHE   A 1 229 ? 16.408  -39.382 -28.918 1 50.02 ? 214 PHE   A CD2 1 
ATOM   1697 C  CE1 . PHE   A 1 229 ? 15.905  -38.574 -31.499 1 50.29 ? 214 PHE   A CE1 1 
ATOM   1698 C  CE2 . PHE   A 1 229 ? 16.524  -38.049 -29.272 1 50.79 ? 214 PHE   A CE2 1 
ATOM   1699 C  CZ  . PHE   A 1 229 ? 16.297  -37.659 -30.566 1 50.26 ? 214 PHE   A CZ  1 
ATOM   1700 N  N   . HIS   A 1 230 ? 14.759  -44.567 -30.55  1 45.57 ? 215 HIS   A N   1 
ATOM   1701 C  CA  . HIS   A 1 230 ? 14.606  -45.484 -31.693 1 45.29 ? 215 HIS   A CA  1 
ATOM   1702 C  C   . HIS   A 1 230 ? 13.149  -45.676 -32.126 1 43.54 ? 215 HIS   A C   1 
ATOM   1703 O  O   . HIS   A 1 230 ? 12.901  -45.986 -33.29  1 43.46 ? 215 HIS   A O   1 
ATOM   1704 C  CB  . HIS   A 1 230 ? 15.26   -46.858 -31.424 1 47.49 ? 215 HIS   A CB  1 
ATOM   1705 C  CG  . HIS   A 1 230 ? 16.74   -46.828 -31.164 1 53    ? 215 HIS   A CG  1 
ATOM   1706 N  ND1 . HIS   A 1 230 ? 17.505  -45.677 -31.376 1 55.92 ? 215 HIS   A ND1 1 
ATOM   1707 C  CD2 . HIS   A 1 230 ? 17.556  -47.814 -30.715 1 54.75 ? 215 HIS   A CD2 1 
ATOM   1708 C  CE1 . HIS   A 1 230 ? 18.747  -46.004 -31.042 1 56.51 ? 215 HIS   A CE1 1 
ATOM   1709 N  NE2 . HIS   A 1 230 ? 18.83   -47.276 -30.637 1 56.28 ? 215 HIS   A NE2 1 
ATOM   1710 N  N   . GLN   A 1 231 ? 12.191  -45.477 -31.2   1 42.46 ? 216 GLN   A N   1 
ATOM   1711 C  CA  . GLN   A 1 231 ? 10.759  -45.607 -31.478 1 42.04 ? 216 GLN   A CA  1 
ATOM   1712 C  C   . GLN   A 1 231 ? 10.253  -44.619 -32.526 1 40.84 ? 216 GLN   A C   1 
ATOM   1713 O  O   . GLN   A 1 231 ? 9.174   -44.817 -33.038 1 41.66 ? 216 GLN   A O   1 
ATOM   1714 C  CB  . GLN   A 1 231 ? 9.937   -45.396 -30.193 1 43.75 ? 216 GLN   A CB  1 
ATOM   1715 C  CG  . GLN   A 1 231 ? 10.165  -46.435 -29.125 1 48.16 ? 216 GLN   A CG  1 
ATOM   1716 C  CD  . GLN   A 1 231 ? 9.34    -46.124 -27.901 1 53.96 ? 216 GLN   A CD  1 
ATOM   1717 O  OE1 . GLN   A 1 231 ? 8.146   -46.456 -27.811 1 57.25 ? 216 GLN   A OE1 1 
ATOM   1718 N  NE2 . GLN   A 1 231 ? 9.954   -45.469 -26.932 1 53.87 ? 216 GLN   A NE2 1 
ATOM   1719 N  N   . ILE   A 1 232 ? 10.995  -43.552 -32.825 1 39.52 ? 217 ILE   A N   1 
ATOM   1720 C  CA  . ILE   A 1 232 ? 10.567  -42.534 -33.774 1 39.11 ? 217 ILE   A CA  1 
ATOM   1721 C  C   . ILE   A 1 232 ? 10.2    -43.112 -35.14  1 39.1  ? 217 ILE   A C   1 
ATOM   1722 O  O   . ILE   A 1 232 ? 9.221   -42.681 -35.747 1 39.08 ? 217 ILE   A O   1 
ATOM   1723 C  CB  . ILE   A 1 232 ? 11.622  -41.379 -33.878 1 38.81 ? 217 ILE   A CB  1 
ATOM   1724 C  CG1 . ILE   A 1 232 ? 11.013  -40.09  -34.47  1 38.21 ? 217 ILE   A CG1 1 
ATOM   1725 C  CG2 . ILE   A 1 232 ? 12.878  -41.813 -34.63  1 39.21 ? 217 ILE   A CG2 1 
ATOM   1726 C  CD1 . ILE   A 1 232 ? 9.989   -39.387 -33.501 1 38.5  ? 217 ILE   A CD1 1 
ATOM   1727 N  N   . HIS   A 1 233 ? 10.946  -44.125 -35.593 1 39.03 ? 218 HIS   A N   1 
ATOM   1728 C  CA  . HIS   A 1 233 ? 10.745  -44.725 -36.912 1 38.95 ? 218 HIS   A CA  1 
ATOM   1729 C  C   . HIS   A 1 233 ? 9.431   -45.483 -37.067 1 39.6  ? 218 HIS   A C   1 
ATOM   1730 O  O   . HIS   A 1 233 ? 8.904   -45.559 -38.181 1 40.76 ? 218 HIS   A O   1 
ATOM   1731 C  CB  . HIS   A 1 233 ? 11.93   -45.617 -37.28  1 38.5  ? 218 HIS   A CB  1 
ATOM   1732 C  CG  . HIS   A 1 233 ? 13.257  -44.937 -37.153 1 39.23 ? 218 HIS   A CG  1 
ATOM   1733 N  ND1 . HIS   A 1 233 ? 13.78   -44.17  -38.185 1 40.8  ? 218 HIS   A ND1 1 
ATOM   1734 C  CD2 . HIS   A 1 233 ? 14.139  -44.953 -36.126 1 40.02 ? 218 HIS   A CD2 1 
ATOM   1735 C  CE1 . HIS   A 1 233 ? 14.958  -43.742 -37.755 1 41.37 ? 218 HIS   A CE1 1 
ATOM   1736 N  NE2 . HIS   A 1 233 ? 15.223  -44.194 -36.523 1 41.49 ? 218 HIS   A NE2 1 
ATOM   1737 N  N   . ASP   A 1 234 ? 8.896   -46.032 -35.973 1 38.82 ? 219 ASP   A N   1 
ATOM   1738 C  CA  . ASP   A 1 234 ? 7.634   -46.778 -36.039 1 38.95 ? 219 ASP   A CA  1 
ATOM   1739 C  C   . ASP   A 1 234 ? 6.399   -45.888 -35.958 1 39.12 ? 219 ASP   A C   1 
ATOM   1740 O  O   . ASP   A 1 234 ? 5.299   -46.409 -36.141 1 39.5  ? 219 ASP   A O   1 
ATOM   1741 C  CB  . ASP   A 1 234 ? 7.535   -47.778 -34.874 1 40.16 ? 219 ASP   A CB  1 
ATOM   1742 C  CG  . ASP   A 1 234 ? 8.642   -48.798 -34.833 1 43.77 ? 219 ASP   A CG  1 
ATOM   1743 O  OD1 . ASP   A 1 234 ? 8.902   -49.429 -35.879 1 43.61 ? 219 ASP   A OD1 1 
ATOM   1744 O  OD2 . ASP   A 1 234 ? 9.247   -48.974 -33.748 1 45.99 ? 219 ASP   A OD2 1 
ATOM   1745 N  N   . HIS   A 1 235 ? 6.547   -44.589 -35.593 1 38.28 ? 220 HIS   A N   1 
ATOM   1746 C  CA  . HIS   A 1 235 ? 5.384   -43.742 -35.402 1 37.92 ? 220 HIS   A CA  1 
ATOM   1747 C  C   . HIS   A 1 235 ? 5.398   -42.439 -36.206 1 37.89 ? 220 HIS   A C   1 
ATOM   1748 O  O   . HIS   A 1 235 ? 4.456   -41.66  -36.107 1 38.49 ? 220 HIS   A O   1 
ATOM   1749 C  CB  . HIS   A 1 235 ? 5.176   -43.47  -33.899 1 38.57 ? 220 HIS   A CB  1 
ATOM   1750 C  CG  . HIS   A 1 235 ? 5.246   -44.707 -33.045 1 40.81 ? 220 HIS   A CG  1 
ATOM   1751 N  ND1 . HIS   A 1 235 ? 4.302   -45.716 -33.159 1 42.27 ? 220 HIS   A ND1 1 
ATOM   1752 C  CD2 . HIS   A 1 235 ? 6.173   -45.077 -32.126 1 41.78 ? 220 HIS   A CD2 1 
ATOM   1753 C  CE1 . HIS   A 1 235 ? 4.677   -46.654 -32.301 1 42.91 ? 220 HIS   A CE1 1 
ATOM   1754 N  NE2 . HIS   A 1 235 ? 5.79    -46.307 -31.647 1 43.06 ? 220 HIS   A NE2 1 
ATOM   1755 N  N   . VAL   A 1 236 ? 6.433   -42.19  -37.004 1 37.36 ? 221 VAL   A N   1 
ATOM   1756 C  CA  . VAL   A 1 236 ? 6.521   -40.982 -37.823 1 37.4  ? 221 VAL   A CA  1 
ATOM   1757 C  C   . VAL   A 1 236 ? 7.02    -41.373 -39.209 1 38.55 ? 221 VAL   A C   1 
ATOM   1758 O  O   . VAL   A 1 236 ? 7.975   -42.14  -39.304 1 38.6  ? 221 VAL   A O   1 
ATOM   1759 C  CB  . VAL   A 1 236 ? 7.455   -39.883 -37.201 1 37.02 ? 221 VAL   A CB  1 
ATOM   1760 C  CG1 . VAL   A 1 236 ? 7.413   -38.599 -38.018 1 37.23 ? 221 VAL   A CG1 1 
ATOM   1761 C  CG2 . VAL   A 1 236 ? 7.099   -39.581 -35.749 1 36.85 ? 221 VAL   A CG2 1 
ATOM   1762 N  N   . ASN   A 1 237 ? 6.404   -40.851 -40.279 1 39.51 ? 222 ASN   A N   1 
ATOM   1763 C  CA  . ASN   A 1 237 ? 6.903   -41.08  -41.634 1 41.47 ? 222 ASN   A CA  1 
ATOM   1764 C  C   . ASN   A 1 237 ? 7.379   -39.753 -42.229 1 42.23 ? 222 ASN   A C   1 
ATOM   1765 O  O   . ASN   A 1 237 ? 6.746   -38.715 -42.019 1 42.67 ? 222 ASN   A O   1 
ATOM   1766 C  CB  . ASN   A 1 237 ? 5.895   -41.812 -42.535 1 44.43 ? 222 ASN   A CB  1 
ATOM   1767 C  CG  . ASN   A 1 237 ? 4.797   -40.977 -43.117 1 50.25 ? 222 ASN   A CG  1 
ATOM   1768 O  OD1 . ASN   A 1 237 ? 3.67    -41.001 -42.614 1 53.88 ? 222 ASN   A OD1 1 
ATOM   1769 N  ND2 . ASN   A 1 237 ? 5.08    -40.259 -44.202 1 50.7  ? 222 ASN   A ND2 1 
ATOM   1770 N  N   . PRO   A 1 238 ? 8.499   -39.776 -42.964 1 42.27 ? 223 PRO   A N   1 
ATOM   1771 C  CA  . PRO   A 1 238 ? 9.087   -38.524 -43.474 1 43.11 ? 223 PRO   A CA  1 
ATOM   1772 C  C   . PRO   A 1 238 ? 8.224   -37.613 -44.347 1 44.46 ? 223 PRO   A C   1 
ATOM   1773 O  O   . PRO   A 1 238 ? 8.342   -36.391 -44.217 1 44.34 ? 223 PRO   A O   1 
ATOM   1774 C  CB  . PRO   A 1 238 ? 10.306  -39.008 -44.253 1 43.09 ? 223 PRO   A CB  1 
ATOM   1775 C  CG  . PRO   A 1 238 ? 10.688  -40.257 -43.563 1 43.13 ? 223 PRO   A CG  1 
ATOM   1776 C  CD  . PRO   A 1 238 ? 9.387   -40.921 -43.224 1 41.57 ? 223 PRO   A CD  1 
ATOM   1777 N  N   . LYS   A 1 239 ? 7.395   -38.179 -45.243 1 45.46 ? 224 LYS   A N   1 
ATOM   1778 C  CA  . LYS   A 1 239 ? 6.566   -37.356 -46.123 1 46.41 ? 224 LYS   A CA  1 
ATOM   1779 C  C   . LYS   A 1 239 ? 5.539   -36.585 -45.323 1 47.45 ? 224 LYS   A C   1 
ATOM   1780 O  O   . LYS   A 1 239 ? 5.463   -35.366 -45.464 1 48.45 ? 224 LYS   A O   1 
ATOM   1781 C  CB  . LYS   A 1 239 ? 5.887   -38.184 -47.229 1 47.9  ? 224 LYS   A CB  1 
ATOM   1782 N  N   . ALA   A 1 240 ? 4.788   -37.271 -44.45  1 46.93 ? 225 ALA   A N   1 
ATOM   1783 C  CA  . ALA   A 1 240 ? 3.791   -36.629 -43.615 1 47.43 ? 225 ALA   A CA  1 
ATOM   1784 C  C   . ALA   A 1 240 ? 4.404   -35.632 -42.656 1 48.1  ? 225 ALA   A C   1 
ATOM   1785 O  O   . ALA   A 1 240 ? 3.808   -34.581 -42.428 1 48.79 ? 225 ALA   A O   1 
ATOM   1786 C  CB  . ALA   A 1 240 ? 3.036   -37.673 -42.838 1 47.9  ? 225 ALA   A CB  1 
ATOM   1787 N  N   . PHE   A 1 241 ? 5.58    -35.953 -42.071 1 47.68 ? 226 PHE   A N   1 
ATOM   1788 C  CA  . PHE   A 1 241 ? 6.22    -35.023 -41.147 1 47.92 ? 226 PHE   A CA  1 
ATOM   1789 C  C   . PHE   A 1 241 ? 6.622   -33.723 -41.862 1 48.85 ? 226 PHE   A C   1 
ATOM   1790 O  O   . PHE   A 1 241 ? 6.277   -32.628 -41.408 1 49.16 ? 226 PHE   A O   1 
ATOM   1791 C  CB  . PHE   A 1 241 ? 7.44    -35.665 -40.424 1 47.28 ? 226 PHE   A CB  1 
ATOM   1792 C  CG  . PHE   A 1 241 ? 8.147   -34.676 -39.524 1 46.96 ? 226 PHE   A CG  1 
ATOM   1793 C  CD1 . PHE   A 1 241 ? 7.644   -34.371 -38.271 1 47.38 ? 226 PHE   A CD1 1 
ATOM   1794 C  CD2 . PHE   A 1 241 ? 9.25    -33.972 -39.972 1 47.4  ? 226 PHE   A CD2 1 
ATOM   1795 C  CE1 . PHE   A 1 241 ? 8.248   -33.405 -37.475 1 47.56 ? 226 PHE   A CE1 1 
ATOM   1796 C  CE2 . PHE   A 1 241 ? 9.836   -32.989 -39.185 1 47.98 ? 226 PHE   A CE2 1 
ATOM   1797 C  CZ  . PHE   A 1 241 ? 9.343   -32.727 -37.932 1 47.46 ? 226 PHE   A CZ  1 
ATOM   1798 N  N   . PHE   A 1 242 ? 7.382   -33.843 -42.954 1 49.05 ? 227 PHE   A N   1 
ATOM   1799 C  CA  . PHE   A 1 242 ? 7.886   -32.682 -43.654 1 49.8  ? 227 PHE   A CA  1 
ATOM   1800 C  C   . PHE   A 1 242 ? 6.814   -31.872 -44.386 1 50.97 ? 227 PHE   A C   1 
ATOM   1801 O  O   . PHE   A 1 242 ? 6.799   -30.644 -44.284 1 51.28 ? 227 PHE   A O   1 
ATOM   1802 C  CB  . PHE   A 1 242 ? 9.017   -33.095 -44.602 1 49.75 ? 227 PHE   A CB  1 
ATOM   1803 C  CG  . PHE   A 1 242 ? 9.618   -31.935 -45.354 1 50.41 ? 227 PHE   A CG  1 
ATOM   1804 C  CD1 . PHE   A 1 242 ? 10.583  -31.139 -44.77  1 51.05 ? 227 PHE   A CD1 1 
ATOM   1805 C  CD2 . PHE   A 1 242 ? 9.202   -31.631 -46.642 1 51.4  ? 227 PHE   A CD2 1 
ATOM   1806 C  CE1 . PHE   A 1 242 ? 11.136  -30.069 -45.462 1 51.73 ? 227 PHE   A CE1 1 
ATOM   1807 C  CE2 . PHE   A 1 242 ? 9.734   -30.54  -47.321 1 52.1  ? 227 PHE   A CE2 1 
ATOM   1808 C  CZ  . PHE   A 1 242 ? 10.69   -29.761 -46.721 1 51.77 ? 227 PHE   A CZ  1 
ATOM   1809 N  N   . SER   A 1 243 ? 5.965   -32.533 -45.173 1 51.35 ? 228 SER   A N   1 
ATOM   1810 C  CA  . SER   A 1 243 ? 4.961   -31.821 -45.961 1 52.6  ? 228 SER   A CA  1 
ATOM   1811 C  C   . SER   A 1 243 ? 3.748   -31.354 -45.165 1 53.01 ? 228 SER   A C   1 
ATOM   1812 O  O   . SER   A 1 243 ? 3.038   -30.467 -45.63  1 54.02 ? 228 SER   A O   1 
ATOM   1813 C  CB  . SER   A 1 243 ? 4.511   -32.665 -47.149 1 53.83 ? 228 SER   A CB  1 
ATOM   1814 O  OG  . SER   A 1 243 ? 3.777   -33.782 -46.684 1 55.81 ? 228 SER   A OG  1 
ATOM   1815 N  N   . VAL   A 1 244 ? 3.49    -31.95  -43.993 1 51.87 ? 229 VAL   A N   1 
ATOM   1816 C  CA  . VAL   A 1 244 ? 2.306   -31.586 -43.225 1 50.99 ? 229 VAL   A CA  1 
ATOM   1817 C  C   . VAL   A 1 244 ? 2.643   -31.001 -41.846 1 50.25 ? 229 VAL   A C   1 
ATOM   1818 O  O   . VAL   A 1 244 ? 2.369   -29.822 -41.625 1 50.66 ? 229 VAL   A O   1 
ATOM   1819 C  CB  . VAL   A 1 244 ? 1.303   -32.77  -43.143 1 51.18 ? 229 VAL   A CB  1 
ATOM   1820 C  CG1 . VAL   A 1 244 ? 0.071   -32.387 -42.355 1 51.76 ? 229 VAL   A CG1 1 
ATOM   1821 C  CG2 . VAL   A 1 244 ? 0.932   -33.287 -44.525 1 50.91 ? 229 VAL   A CG2 1 
ATOM   1822 N  N   . LEU   A 1 245 ? 3.267   -31.781 -40.938 1 49.16 ? 230 LEU   A N   1 
ATOM   1823 C  CA  . LEU   A 1 245 ? 3.528   -31.297 -39.581 1 48.71 ? 230 LEU   A CA  1 
ATOM   1824 C  C   . LEU   A 1 245 ? 4.385   -30.029 -39.508 1 49.54 ? 230 LEU   A C   1 
ATOM   1825 O  O   . LEU   A 1 245 ? 4.084   -29.138 -38.725 1 49.97 ? 230 LEU   A O   1 
ATOM   1826 C  CB  . LEU   A 1 245 ? 4.114   -32.409 -38.689 1 47.84 ? 230 LEU   A CB  1 
ATOM   1827 C  CG  . LEU   A 1 245 ? 4.048   -32.183 -37.169 1 48.09 ? 230 LEU   A CG  1 
ATOM   1828 C  CD1 . LEU   A 1 245 ? 2.657   -31.798 -36.714 1 48.52 ? 230 LEU   A CD1 1 
ATOM   1829 C  CD2 . LEU   A 1 245 ? 4.495   -33.404 -36.423 1 48.22 ? 230 LEU   A CD2 1 
ATOM   1830 N  N   . ARG   A 1 246 ? 5.428   -29.943 -40.323 1 49.97 ? 231 ARG   A N   1 
ATOM   1831 C  CA  . ARG   A 1 246 ? 6.358   -28.814 -40.359 1 50.77 ? 231 ARG   A CA  1 
ATOM   1832 C  C   . ARG   A 1 246 ? 5.66    -27.436 -40.417 1 50.68 ? 231 ARG   A C   1 
ATOM   1833 O  O   . ARG   A 1 246 ? 6.072   -26.504 -39.721 1 51.53 ? 231 ARG   A O   1 
ATOM   1834 C  CB  . ARG   A 1 246 ? 7.339   -29.027 -41.527 1 53.14 ? 231 ARG   A CB  1 
ATOM   1835 C  CG  . ARG   A 1 246 ? 7.889   -27.786 -42.21  1 58.77 ? 231 ARG   A CG  1 
ATOM   1836 C  CD  . ARG   A 1 246 ? 8.802   -28.176 -43.352 1 64.72 ? 231 ARG   A CD  1 
ATOM   1837 N  NE  . ARG   A 1 246 ? 8.118   -28.092 -44.649 1 69.57 ? 231 ARG   A NE  1 
ATOM   1838 C  CZ  . ARG   A 1 246 ? 8.438   -27.231 -45.61  1 73.26 ? 231 ARG   A CZ  1 
ATOM   1839 N  NH1 . ARG   A 1 246 ? 7.767   -27.228 -46.755 1 73.28 ? 231 ARG   A NH1 1 
ATOM   1840 N  NH2 . ARG   A 1 246 ? 9.441   -26.374 -45.438 1 74.01 ? 231 ARG   A NH2 1 
ATOM   1841 N  N   . ILE   A 1 247 ? 4.615   -27.326 -41.241 1 49.27 ? 232 ILE   A N   1 
ATOM   1842 C  CA  . ILE   A 1 247 ? 3.848   -26.107 -41.438 1 48.81 ? 232 ILE   A CA  1 
ATOM   1843 C  C   . ILE   A 1 247 ? 3.298   -25.521 -40.138 1 46.81 ? 232 ILE   A C   1 
ATOM   1844 O  O   . ILE   A 1 247 ? 3.453   -24.338 -39.88  1 46.36 ? 232 ILE   A O   1 
ATOM   1845 C  CB  . ILE   A 1 247 ? 2.712   -26.392 -42.47  1 50.36 ? 232 ILE   A CB  1 
ATOM   1846 C  CG1 . ILE   A 1 247 ? 3.282   -26.738 -43.866 1 52.09 ? 232 ILE   A CG1 1 
ATOM   1847 C  CG2 . ILE   A 1 247 ? 1.71    -25.239 -42.533 1 50.89 ? 232 ILE   A CG2 1 
ATOM   1848 C  CD1 . ILE   A 1 247 ? 2.266   -27.358 -44.776 1 53.86 ? 232 ILE   A CD1 1 
ATOM   1849 N  N   . TYR   A 1 248 ? 2.654   -26.351 -39.328 1 45.71 ? 233 TYR   A N   1 
ATOM   1850 C  CA  . TYR   A 1 248 ? 2.01    -25.902 -38.095 1 44.95 ? 233 TYR   A CA  1 
ATOM   1851 C  C   . TYR   A 1 248 ? 2.976   -25.676 -36.935 1 44.93 ? 233 TYR   A C   1 
ATOM   1852 O  O   . TYR   A 1 248 ? 2.586   -25.069 -35.933 1 44.4  ? 233 TYR   A O   1 
ATOM   1853 C  CB  . TYR   A 1 248 ? 0.873   -26.852 -37.712 1 44.35 ? 233 TYR   A CB  1 
ATOM   1854 C  CG  . TYR   A 1 248 ? -0.145  -26.943 -38.827 1 44.6  ? 233 TYR   A CG  1 
ATOM   1855 C  CD1 . TYR   A 1 248 ? -1.117  -25.962 -38.99  1 45.12 ? 233 TYR   A CD1 1 
ATOM   1856 C  CD2 . TYR   A 1 248 ? -0.058  -27.937 -39.794 1 45.23 ? 233 TYR   A CD2 1 
ATOM   1857 C  CE1 . TYR   A 1 248 ? -2.003  -25.992 -40.064 1 45.74 ? 233 TYR   A CE1 1 
ATOM   1858 C  CE2 . TYR   A 1 248 ? -0.918  -27.96  -40.886 1 46.07 ? 233 TYR   A CE2 1 
ATOM   1859 C  CZ  . TYR   A 1 248 ? -1.893  -26.986 -41.018 1 46.93 ? 233 TYR   A CZ  1 
ATOM   1860 O  OH  . TYR   A 1 248 ? -2.759  -27.028 -42.089 1 48.64 ? 233 TYR   A OH  1 
ATOM   1861 N  N   . LEU   A 1 249 ? 4.222   -26.179 -37.051 1 44.93 ? 234 LEU   A N   1 
ATOM   1862 C  CA  . LEU   A 1 249 ? 5.243   -25.956 -36.039 1 45.35 ? 234 LEU   A CA  1 
ATOM   1863 C  C   . LEU   A 1 249 ? 5.932   -24.587 -36.212 1 45.29 ? 234 LEU   A C   1 
ATOM   1864 O  O   . LEU   A 1 249 ? 6.625   -24.158 -35.299 1 45.67 ? 234 LEU   A O   1 
ATOM   1865 C  CB  . LEU   A 1 249 ? 6.299   -27.065 -36.076 1 45.88 ? 234 LEU   A CB  1 
ATOM   1866 C  CG  . LEU   A 1 249 ? 5.828   -28.475 -35.77  1 47.96 ? 234 LEU   A CG  1 
ATOM   1867 C  CD1 . LEU   A 1 249 ? 6.996   -29.437 -35.838 1 48.91 ? 234 LEU   A CD1 1 
ATOM   1868 C  CD2 . LEU   A 1 249 ? 5.122   -28.564 -34.403 1 48.25 ? 234 LEU   A CD2 1 
ATOM   1869 N  N   . SER   A 1 250 ? 5.756   -23.916 -37.374 1 44.97 ? 235 SER   A N   1 
ATOM   1870 C  CA  . SER   A 1 250 ? 6.35    -22.613 -37.694 1 44.88 ? 235 SER   A CA  1 
ATOM   1871 C  C   . SER   A 1 250 ? 5.824   -21.459 -36.866 1 44.6  ? 235 SER   A C   1 
ATOM   1872 O  O   . SER   A 1 250 ? 4.627   -21.373 -36.59  1 44.43 ? 235 SER   A O   1 
ATOM   1873 C  CB  . SER   A 1 250 ? 6.14    -22.28  -39.165 1 46.17 ? 235 SER   A CB  1 
ATOM   1874 O  OG  . SER   A 1 250 ? 6.745   -23.297 -39.943 1 49.94 ? 235 SER   A OG  1 
ATOM   1875 N  N   . GLY   A 1 251 ? 6.723   -20.531 -36.557 1 43.74 ? 236 GLY   A N   1 
ATOM   1876 C  CA  . GLY   A 1 251 ? 6.386   -19.331 -35.816 1 43.39 ? 236 GLY   A CA  1 
ATOM   1877 C  C   . GLY   A 1 251 ? 6.462   -18.093 -36.67  1 42.92 ? 236 GLY   A C   1 
ATOM   1878 O  O   . GLY   A 1 251 ? 6.409   -18.166 -37.901 1 42.42 ? 236 GLY   A O   1 
ATOM   1879 N  N   . TRP   A 1 252 ? 6.567   -16.941 -36.02  1 42.92 ? 237 TRP   A N   1 
ATOM   1880 C  CA  . TRP   A 1 252 ? 6.6     -15.664 -36.726 1 43.22 ? 237 TRP   A CA  1 
ATOM   1881 C  C   . TRP   A 1 252 ? 7.708   -14.768 -36.222 1 45    ? 237 TRP   A C   1 
ATOM   1882 O  O   . TRP   A 1 252 ? 7.458   -13.643 -35.825 1 45.83 ? 237 TRP   A O   1 
ATOM   1883 C  CB  . TRP   A 1 252 ? 5.223   -14.941 -36.734 1 41.96 ? 237 TRP   A CB  1 
ATOM   1884 C  CG  . TRP   A 1 252 ? 4.324   -15.23  -35.559 1 40.93 ? 237 TRP   A CG  1 
ATOM   1885 C  CD1 . TRP   A 1 252 ? 4.199   -14.502 -34.413 1 40.91 ? 237 TRP   A CD1 1 
ATOM   1886 C  CD2 . TRP   A 1 252 ? 3.405   -16.329 -35.442 1 40.7  ? 237 TRP   A CD2 1 
ATOM   1887 N  NE1 . TRP   A 1 252 ? 3.287   -15.1   -33.57  1 40.94 ? 237 TRP   A NE1 1 
ATOM   1888 C  CE2 . TRP   A 1 252 ? 2.773   -16.214 -34.188 1 40.87 ? 237 TRP   A CE2 1 
ATOM   1889 C  CE3 . TRP   A 1 252 ? 3.065   -17.407 -36.278 1 40.8  ? 237 TRP   A CE3 1 
ATOM   1890 C  CZ2 . TRP   A 1 252 ? 1.828   -17.138 -33.747 1 41.17 ? 237 TRP   A CZ2 1 
ATOM   1891 C  CZ3 . TRP   A 1 252 ? 2.122   -18.311 -35.841 1 41.33 ? 237 TRP   A CZ3 1 
ATOM   1892 C  CH2 . TRP   A 1 252 ? 1.503   -18.165 -34.598 1 41.12 ? 237 TRP   A CH2 1 
ATOM   1893 N  N   . LYS   A 1 253 ? 8.936   -15.273 -36.229 1 45.41 ? 238 LYS   A N   1 
ATOM   1894 C  CA  . LYS   A 1 253 ? 10.112  -14.505 -35.871 1 46.19 ? 238 LYS   A CA  1 
ATOM   1895 C  C   . LYS   A 1 253 ? 11.089  -14.777 -37.001 1 47.3  ? 238 LYS   A C   1 
ATOM   1896 O  O   . LYS   A 1 253 ? 11.466  -15.933 -37.217 1 47.21 ? 238 LYS   A O   1 
ATOM   1897 C  CB  . LYS   A 1 253 ? 10.703  -14.943 -34.536 1 47.93 ? 238 LYS   A CB  1 
ATOM   1898 C  CG  . LYS   A 1 253 ? 11.851  -14.048 -34.113 1 52.71 ? 238 LYS   A CG  1 
ATOM   1899 C  CD  . LYS   A 1 253 ? 12.271  -14.335 -32.696 1 59.68 ? 238 LYS   A CD  1 
ATOM   1900 C  CE  . LYS   A 1 253 ? 13.469  -13.507 -32.295 1 65.06 ? 238 LYS   A CE  1 
ATOM   1901 N  NZ  . LYS   A 1 253 ? 13.143  -12.056 -32.314 1 68.29 ? 238 LYS   A NZ  1 
ATOM   1902 N  N   . GLY   A 1 254 ? 11.398  -13.74  -37.781 1 47.88 ? 239 GLY   A N   1 
ATOM   1903 C  CA  . GLY   A 1 254 ? 12.24   -13.888 -38.959 1 48.71 ? 239 GLY   A CA  1 
ATOM   1904 C  C   . GLY   A 1 254 ? 11.575  -14.739 -40.027 1 49.83 ? 239 GLY   A C   1 
ATOM   1905 O  O   . GLY   A 1 254 ? 12.258  -15.389 -40.823 1 50.19 ? 239 GLY   A O   1 
ATOM   1906 N  N   . ASN   A 1 255 ? 10.23   -14.768 -40.04  1 50.07 ? 240 ASN   A N   1 
ATOM   1907 C  CA  . ASN   A 1 255 ? 9.505   -15.563 -41.014 1 51.04 ? 240 ASN   A CA  1 
ATOM   1908 C  C   . ASN   A 1 255 ? 9.069   -14.675 -42.163 1 52.25 ? 240 ASN   A C   1 
ATOM   1909 O  O   . ASN   A 1 255 ? 8.249   -13.786 -41.971 1 52.11 ? 240 ASN   A O   1 
ATOM   1910 C  CB  . ASN   A 1 255 ? 8.293   -16.264 -40.38  1 51.28 ? 240 ASN   A CB  1 
ATOM   1911 C  CG  . ASN   A 1 255 ? 7.698   -17.343 -41.26  1 53.44 ? 240 ASN   A CG  1 
ATOM   1912 O  OD1 . ASN   A 1 255 ? 7.726   -17.286 -42.496 1 53.89 ? 240 ASN   A OD1 1 
ATOM   1913 N  ND2 . ASN   A 1 255 ? 7.163   -18.372 -40.642 1 54.14 ? 240 ASN   A ND2 1 
ATOM   1914 N  N   . PRO   A 1 256 ? 9.547   -14.952 -43.383 1 53.15 ? 241 PRO   A N   1 
ATOM   1915 C  CA  . PRO   A 1 256 ? 9.13    -14.134 -44.535 1 54.07 ? 241 PRO   A CA  1 
ATOM   1916 C  C   . PRO   A 1 256 ? 7.61    -14.05  -44.752 1 55.48 ? 241 PRO   A C   1 
ATOM   1917 O  O   . PRO   A 1 256 ? 7.13    -13     -45.155 1 56.31 ? 241 PRO   A O   1 
ATOM   1918 C  CB  . PRO   A 1 256 ? 9.86    -14.785 -45.712 1 54.42 ? 241 PRO   A CB  1 
ATOM   1919 C  CG  . PRO   A 1 256 ? 11.052  -15.459 -45.081 1 54.69 ? 241 PRO   A CG  1 
ATOM   1920 C  CD  . PRO   A 1 256 ? 10.538  -15.974 -43.768 1 52.73 ? 241 PRO   A CD  1 
ATOM   1921 N  N   . GLN   A 1 257 ? 6.847   -15.113 -44.422 1 55.54 ? 242 GLN   A N   1 
ATOM   1922 C  CA  . GLN   A 1 257 ? 5.387   -15.131 -44.565 1 56.16 ? 242 GLN   A CA  1 
ATOM   1923 C  C   . GLN   A 1 257 ? 4.657   -14.193 -43.598 1 56.67 ? 242 GLN   A C   1 
ATOM   1924 O  O   . GLN   A 1 257 ? 3.52    -13.822 -43.867 1 56.95 ? 242 GLN   A O   1 
ATOM   1925 C  CB  . GLN   A 1 257 ? 4.84    -16.552 -44.393 1 57.88 ? 242 GLN   A CB  1 
ATOM   1926 C  CG  . GLN   A 1 257 ? 5.407   -17.552 -45.391 1 61.9  ? 242 GLN   A CG  1 
ATOM   1927 C  CD  . GLN   A 1 257 ? 4.607   -18.828 -45.36  1 66.63 ? 242 GLN   A CD  1 
ATOM   1928 O  OE1 . GLN   A 1 257 ? 3.48    -18.895 -45.866 1 67.66 ? 242 GLN   A OE1 1 
ATOM   1929 N  NE2 . GLN   A 1 257 ? 5.172   -19.868 -44.758 1 67.62 ? 242 GLN   A NE2 1 
ATOM   1930 N  N   . LEU   A 1 258 ? 5.3     -13.833 -42.464 1 56.44 ? 243 LEU   A N   1 
ATOM   1931 C  CA  . LEU   A 1 258 ? 4.769   -12.928 -41.439 1 56.31 ? 243 LEU   A CA  1 
ATOM   1932 C  C   . LEU   A 1 258 ? 5.958   -12.1   -40.92  1 56.4  ? 243 LEU   A C   1 
ATOM   1933 O  O   . LEU   A 1 258 ? 6.274   -12.14  -39.731 1 56.74 ? 243 LEU   A O   1 
ATOM   1934 C  CB  . LEU   A 1 258 ? 4.144   -13.737 -40.292 1 56.59 ? 243 LEU   A CB  1 
ATOM   1935 C  CG  . LEU   A 1 258 ? 2.739   -14.267 -40.479 1 58.76 ? 243 LEU   A CG  1 
ATOM   1936 C  CD1 . LEU   A 1 258 ? 2.303   -15.01  -39.258 1 59.49 ? 243 LEU   A CD1 1 
ATOM   1937 C  CD2 . LEU   A 1 258 ? 1.759   -13.143 -40.708 1 60.15 ? 243 LEU   A CD2 1 
ATOM   1938 N  N   . SER   A 1 259 ? 6.648   -11.383 -41.841 1 56.03 ? 244 SER   A N   1 
ATOM   1939 C  CA  . SER   A 1 259 ? 7.863   -10.591 -41.603 1 56.09 ? 244 SER   A CA  1 
ATOM   1940 C  C   . SER   A 1 259 ? 7.798   -9.617  -40.439 1 55.7  ? 244 SER   A C   1 
ATOM   1941 O  O   . SER   A 1 259 ? 8.837   -9.323  -39.844 1 56.32 ? 244 SER   A O   1 
ATOM   1942 C  CB  . SER   A 1 259 ? 8.292   -9.853  -42.866 1 58.16 ? 244 SER   A CB  1 
ATOM   1943 O  OG  . SER   A 1 259 ? 7.319   -8.905  -43.271 1 61.65 ? 244 SER   A OG  1 
ATOM   1944 N  N   . ASP   A 1 260 ? 6.605   -9.134  -40.087 1 54.77 ? 245 ASP   A N   1 
ATOM   1945 C  CA  . ASP   A 1 260 ? 6.463   -8.219  -38.945 1 54.48 ? 245 ASP   A CA  1 
ATOM   1946 C  C   . ASP   A 1 260 ? 5.872   -8.872  -37.678 1 52.66 ? 245 ASP   A C   1 
ATOM   1947 O  O   . ASP   A 1 260 ? 5.806   -8.226  -36.63  1 52.6  ? 245 ASP   A O   1 
ATOM   1948 C  CB  . ASP   A 1 260 ? 5.662   -6.968  -39.345 1 57.15 ? 245 ASP   A CB  1 
ATOM   1949 C  CG  . ASP   A 1 260 ? 6.316   -6.223  -40.493 1 63.7  ? 245 ASP   A CG  1 
ATOM   1950 O  OD1 . ASP   A 1 260 ? 7.483   -5.782  -40.331 1 64.72 ? 245 ASP   A OD1 1 
ATOM   1951 O  OD2 . ASP   A 1 260 ? 5.679   -6.11   -41.565 1 66.21 ? 245 ASP   A OD2 1 
ATOM   1952 N  N   . GLY   A 1 261 ? 5.48    -10.138 -37.773 1 50.69 ? 246 GLY   A N   1 
ATOM   1953 C  CA  . GLY   A 1 261 ? 4.879   -10.855 -36.666 1 49.59 ? 246 GLY   A CA  1 
ATOM   1954 C  C   . GLY   A 1 261 ? 3.372   -10.936 -36.774 1 48.88 ? 246 GLY   A C   1 
ATOM   1955 O  O   . GLY   A 1 261 ? 2.784   -10.608 -37.808 1 49.01 ? 246 GLY   A O   1 
ATOM   1956 N  N   . LEU   A 1 262 ? 2.732   -11.367 -35.699 1 47.99 ? 247 LEU   A N   1 
ATOM   1957 C  CA  . LEU   A 1 262 ? 1.291   -11.527 -35.671 1 47.35 ? 247 LEU   A CA  1 
ATOM   1958 C  C   . LEU   A 1 262 ? 0.648   -10.401 -34.858 1 46.95 ? 247 LEU   A C   1 
ATOM   1959 O  O   . LEU   A 1 262 ? 1.199   -9.997  -33.834 1 47.36 ? 247 LEU   A O   1 
ATOM   1960 C  CB  . LEU   A 1 262 ? 0.97    -12.89  -35.045 1 47.03 ? 247 LEU   A CB  1 
ATOM   1961 C  CG  . LEU   A 1 262 ? -0.494  -13.296 -35.009 1 48.04 ? 247 LEU   A CG  1 
ATOM   1962 C  CD1 . LEU   A 1 262 ? -1.051  -13.487 -36.405 1 48.4  ? 247 LEU   A CD1 1 
ATOM   1963 C  CD2 . LEU   A 1 262 ? -0.677  -14.546 -34.196 1 48.41 ? 247 LEU   A CD2 1 
ATOM   1964 N  N   . VAL   A 1 263 ? -0.52   -9.908  -35.296 1 45.64 ? 248 VAL   A N   1 
ATOM   1965 C  CA  . VAL   A 1 263 ? -1.23   -8.894  -34.533 1 45.19 ? 248 VAL   A CA  1 
ATOM   1966 C  C   . VAL   A 1 263 ? -2.151  -9.619  -33.557 1 44.23 ? 248 VAL   A C   1 
ATOM   1967 O  O   . VAL   A 1 263 ? -2.95   -10.459 -33.962 1 44.23 ? 248 VAL   A O   1 
ATOM   1968 C  CB  . VAL   A 1 263 ? -2      -7.882  -35.429 1 46    ? 248 VAL   A CB  1 
ATOM   1969 C  CG1 . VAL   A 1 263 ? -2.886  -6.969  -34.593 1 46.41 ? 248 VAL   A CG1 1 
ATOM   1970 C  CG2 . VAL   A 1 263 ? -1.038  -7.065  -36.283 1 46.16 ? 248 VAL   A CG2 1 
ATOM   1971 N  N   . TYR   A 1 264 ? -1.997  -9.338  -32.267 1 43.5  ? 249 TYR   A N   1 
ATOM   1972 C  CA  . TYR   A 1 264 ? -2.81   -9.932  -31.212 1 43.47 ? 249 TYR   A CA  1 
ATOM   1973 C  C   . TYR   A 1 264 ? -3.902  -8.918  -30.859 1 44.9  ? 249 TYR   A C   1 
ATOM   1974 O  O   . TYR   A 1 264 ? -3.802  -8.219  -29.848 1 44.87 ? 249 TYR   A O   1 
ATOM   1975 C  CB  . TYR   A 1 264 ? -1.933  -10.28  -29.986 1 42.34 ? 249 TYR   A CB  1 
ATOM   1976 C  CG  . TYR   A 1 264 ? -0.942  -11.394 -30.267 1 41.63 ? 249 TYR   A CG  1 
ATOM   1977 C  CD1 . TYR   A 1 264 ? 0.292   -11.127 -30.839 1 41.73 ? 249 TYR   A CD1 1 
ATOM   1978 C  CD2 . TYR   A 1 264 ? -1.271  -12.717 -30.028 1 42    ? 249 TYR   A CD2 1 
ATOM   1979 C  CE1 . TYR   A 1 264 ? 1.19    -12.144 -31.128 1 42.57 ? 249 TYR   A CE1 1 
ATOM   1980 C  CE2 . TYR   A 1 264 ? -0.39   -13.745 -30.331 1 42.74 ? 249 TYR   A CE2 1 
ATOM   1981 C  CZ  . TYR   A 1 264 ? 0.847   -13.455 -30.866 1 43.73 ? 249 TYR   A CZ  1 
ATOM   1982 O  OH  . TYR   A 1 264 ? 1.72    -14.478 -31.162 1 45.43 ? 249 TYR   A OH  1 
ATOM   1983 N  N   . GLU   A 1 265 ? -4.922  -8.819  -31.738 1 45.38 ? 250 GLU   A N   1 
ATOM   1984 C  CA  . GLU   A 1 265 ? -6.038  -7.876  -31.676 1 45.54 ? 250 GLU   A CA  1 
ATOM   1985 C  C   . GLU   A 1 265 ? -6.647  -7.721  -30.304 1 45.93 ? 250 GLU   A C   1 
ATOM   1986 O  O   . GLU   A 1 265 ? -6.993  -8.708  -29.655 1 46.16 ? 250 GLU   A O   1 
ATOM   1987 C  CB  . GLU   A 1 265 ? -7.103  -8.277  -32.693 1 48    ? 250 GLU   A CB  1 
ATOM   1988 C  CG  . GLU   A 1 265 ? -8.222  -7.273  -32.862 1 51.48 ? 250 GLU   A CG  1 
ATOM   1989 C  CD  . GLU   A 1 265 ? -9.227  -7.703  -33.905 1 54.93 ? 250 GLU   A CD  1 
ATOM   1990 O  OE1 . GLU   A 1 265 ? -10.077 -8.562  -33.583 1 56.61 ? 250 GLU   A OE1 1 
ATOM   1991 O  OE2 . GLU   A 1 265 ? -9.162  -7.187  -35.044 1 55.53 ? 250 GLU   A OE2 1 
ATOM   1992 N  N   . GLY   A 1 266 ? -6.74   -6.474  -29.851 1 45.87 ? 251 GLY   A N   1 
ATOM   1993 C  CA  . GLY   A 1 266 ? -7.294  -6.153  -28.542 1 45.98 ? 251 GLY   A CA  1 
ATOM   1994 C  C   . GLY   A 1 266 ? -6.299  -6.24   -27.402 1 47.02 ? 251 GLY   A C   1 
ATOM   1995 O  O   . GLY   A 1 266 ? -6.621  -5.854  -26.27  1 47.38 ? 251 GLY   A O   1 
ATOM   1996 N  N   . PHE   A 1 267 ? -5.078  -6.77   -27.67  1 47.07 ? 252 PHE   A N   1 
ATOM   1997 C  CA  . PHE   A 1 267 ? -4.062  -6.921  -26.641 1 47.28 ? 252 PHE   A CA  1 
ATOM   1998 C  C   . PHE   A 1 267 ? -2.858  -6.011  -26.875 1 48.41 ? 252 PHE   A C   1 
ATOM   1999 O  O   . PHE   A 1 267 ? -2.441  -5.342  -25.95  1 48.02 ? 252 PHE   A O   1 
ATOM   2000 C  CB  . PHE   A 1 267 ? -3.655  -8.392  -26.463 1 46.15 ? 252 PHE   A CB  1 
ATOM   2001 C  CG  . PHE   A 1 267 ? -3.135  -8.655  -25.075 1 45.41 ? 252 PHE   A CG  1 
ATOM   2002 C  CD1 . PHE   A 1 267 ? -4.001  -8.981  -24.047 1 45.42 ? 252 PHE   A CD1 1 
ATOM   2003 C  CD2 . PHE   A 1 267 ? -1.781  -8.531  -24.787 1 45.79 ? 252 PHE   A CD2 1 
ATOM   2004 C  CE1 . PHE   A 1 267 ? -3.524  -9.188  -22.757 1 45.84 ? 252 PHE   A CE1 1 
ATOM   2005 C  CE2 . PHE   A 1 267 ? -1.307  -8.741  -23.498 1 46.03 ? 252 PHE   A CE2 1 
ATOM   2006 C  CZ  . PHE   A 1 267 ? -2.183  -9.068  -22.492 1 45.63 ? 252 PHE   A CZ  1 
ATOM   2007 N  N   . TRP   A 1 268 ? -2.311  -5.982  -28.1   1 49.78 ? 253 TRP   A N   1 
ATOM   2008 C  CA  . TRP   A 1 268 ? -1.18   -5.114  -28.462 1 51.91 ? 253 TRP   A CA  1 
ATOM   2009 C  C   . TRP   A 1 268 ? -1.498  -4.459  -29.784 1 53.9  ? 253 TRP   A C   1 
ATOM   2010 O  O   . TRP   A 1 268 ? -2.121  -5.084  -30.648 1 54.33 ? 253 TRP   A O   1 
ATOM   2011 C  CB  . TRP   A 1 268 ? 0.136   -5.89   -28.64  1 52.25 ? 253 TRP   A CB  1 
ATOM   2012 C  CG  . TRP   A 1 268 ? 0.71    -6.496  -27.398 1 53.51 ? 253 TRP   A CG  1 
ATOM   2013 C  CD1 . TRP   A 1 268 ? 1.12    -5.841  -26.27  1 54.48 ? 253 TRP   A CD1 1 
ATOM   2014 C  CD2 . TRP   A 1 268 ? 1.033   -7.879  -27.201 1 53.82 ? 253 TRP   A CD2 1 
ATOM   2015 N  NE1 . TRP   A 1 268 ? 1.619   -6.741  -25.357 1 54.77 ? 253 TRP   A NE1 1 
ATOM   2016 C  CE2 . TRP   A 1 268 ? 1.587   -8      -25.907 1 54.62 ? 253 TRP   A CE2 1 
ATOM   2017 C  CE3 . TRP   A 1 268 ? 0.864   -9.034  -27.974 1 54.13 ? 253 TRP   A CE3 1 
ATOM   2018 C  CZ2 . TRP   A 1 268 ? 2.015   -9.225  -25.393 1 55.07 ? 253 TRP   A CZ2 1 
ATOM   2019 C  CZ3 . TRP   A 1 268 ? 1.275   -10.243 -27.457 1 54.92 ? 253 TRP   A CZ3 1 
ATOM   2020 C  CH2 . TRP   A 1 268 ? 1.846   -10.332 -26.183 1 55.04 ? 253 TRP   A CH2 1 
ATOM   2021 N  N   . GLU   A 1 269 ? -1.048  -3.211  -29.969 1 54.88 ? 254 GLU   A N   1 
ATOM   2022 C  CA  . GLU   A 1 269 ? -1.324  -2.474  -31.197 1 56.04 ? 254 GLU   A CA  1 
ATOM   2023 C  C   . GLU   A 1 269 ? -0.514  -2.976  -32.38  1 56.46 ? 254 GLU   A C   1 
ATOM   2024 O  O   . GLU   A 1 269 ? -1.055  -3.107  -33.487 1 57.28 ? 254 GLU   A O   1 
ATOM   2025 C  CB  . GLU   A 1 269 ? -1.011  -0.987  -30.998 1 58.86 ? 254 GLU   A CB  1 
ATOM   2026 C  CG  . GLU   A 1 269 ? -1.93   -0.267  -30.047 1 63.5  ? 254 GLU   A CG  1 
ATOM   2027 C  CD  . GLU   A 1 269 ? -1.932  1.21    -30.357 1 67.93 ? 254 GLU   A CD  1 
ATOM   2028 O  OE1 . GLU   A 1 269 ? -1.98   1.559   -31.562 1 66.39 ? 254 GLU   A OE1 1 
ATOM   2029 O  OE2 . GLU   A 1 269 ? -1.88   2.017   -29.398 1 71.01 ? 254 GLU   A OE2 1 
ATOM   2030 N  N   . ASP   A 1 270 ? 0.796   -3.2    -32.16  1 55.64 ? 255 ASP   A N   1 
ATOM   2031 C  CA  . ASP   A 1 270 ? 1.746   -3.621  -33.189 1 55.19 ? 255 ASP   A CA  1 
ATOM   2032 C  C   . ASP   A 1 270 ? 1.842   -5.148  -33.296 1 53.54 ? 255 ASP   A C   1 
ATOM   2033 O  O   . ASP   A 1 270 ? 1.621   -5.862  -32.307 1 52.65 ? 255 ASP   A O   1 
ATOM   2034 C  CB  . ASP   A 1 270 ? 3.149   -3.059  -32.866 1 57.59 ? 255 ASP   A CB  1 
ATOM   2035 C  CG  . ASP   A 1 270 ? 3.232   -1.552  -32.757 1 64.5  ? 255 ASP   A CG  1 
ATOM   2036 O  OD1 . ASP   A 1 270 ? 2.485   -0.979  -31.937 1 65.99 ? 255 ASP   A OD1 1 
ATOM   2037 O  OD2 . ASP   A 1 270 ? 4.072   -0.944  -33.477 1 66.96 ? 255 ASP   A OD2 1 
ATOM   2038 N  N   . PRO   A 1 271 ? 2.221   -5.668  -34.483 1 52.6  ? 256 PRO   A N   1 
ATOM   2039 C  CA  . PRO   A 1 271 ? 2.436   -7.114  -34.592 1 51.64 ? 256 PRO   A CA  1 
ATOM   2040 C  C   . PRO   A 1 271 ? 3.679   -7.532  -33.8   1 50.38 ? 256 PRO   A C   1 
ATOM   2041 O  O   . PRO   A 1 271 ? 4.716   -6.874  -33.87  1 50.66 ? 256 PRO   A O   1 
ATOM   2042 C  CB  . PRO   A 1 271 ? 2.604   -7.346  -36.097 1 52.28 ? 256 PRO   A CB  1 
ATOM   2043 C  CG  . PRO   A 1 271 ? 3.046   -6.059  -36.64  1 52.94 ? 256 PRO   A CG  1 
ATOM   2044 C  CD  . PRO   A 1 271 ? 2.52    -4.971  -35.75  1 51.82 ? 256 PRO   A CD  1 
ATOM   2045 N  N   . LYS   A 1 272 ? 3.561   -8.613  -33.02  1 48.93 ? 257 LYS   A N   1 
ATOM   2046 C  CA  . LYS   A 1 272 ? 4.659   -9.13   -32.207 1 47.65 ? 257 LYS   A CA  1 
ATOM   2047 C  C   . LYS   A 1 272 ? 5.275   -10.382 -32.829 1 46.66 ? 257 LYS   A C   1 
ATOM   2048 O  O   . LYS   A 1 272 ? 4.562   -11.238 -33.362 1 47.04 ? 257 LYS   A O   1 
ATOM   2049 C  CB  . LYS   A 1 272 ? 4.156   -9.451  -30.799 1 48.58 ? 257 LYS   A CB  1 
ATOM   2050 C  CG  . LYS   A 1 272 ? 3.516   -8.278  -30.1   1 51.02 ? 257 LYS   A CG  1 
ATOM   2051 C  CD  . LYS   A 1 272 ? 4.532   -7.211  -29.729 1 53.59 ? 257 LYS   A CD  1 
ATOM   2052 C  CE  . LYS   A 1 272 ? 3.88    -6.023  -29.056 1 55.71 ? 257 LYS   A CE  1 
ATOM   2053 N  NZ  . LYS   A 1 272 ? 4.276   -4.75   -29.704 1 57.89 ? 257 LYS   A NZ  1 
ATOM   2054 N  N   . GLU   A 1 273 ? 6.597   -10.499 -32.746 1 45.37 ? 258 GLU   A N   1 
ATOM   2055 C  CA  . GLU   A 1 273 ? 7.326   -11.649 -33.267 1 44.6  ? 258 GLU   A CA  1 
ATOM   2056 C  C   . GLU   A 1 273 ? 7.652   -12.659 -32.172 1 43.98 ? 258 GLU   A C   1 
ATOM   2057 O  O   . GLU   A 1 273 ? 8.249   -12.3   -31.167 1 44.69 ? 258 GLU   A O   1 
ATOM   2058 C  CB  . GLU   A 1 273 ? 8.635   -11.198 -33.917 1 46.72 ? 258 GLU   A CB  1 
ATOM   2059 C  CG  . GLU   A 1 273 ? 8.48    -10.704 -35.343 1 51.76 ? 258 GLU   A CG  1 
ATOM   2060 C  CD  . GLU   A 1 273 ? 9.806   -10.633 -36.067 1 59.66 ? 258 GLU   A CD  1 
ATOM   2061 O  OE1 . GLU   A 1 273 ? 10.74   -10.006 -35.517 1 64.16 ? 258 GLU   A OE1 1 
ATOM   2062 O  OE2 . GLU   A 1 273 ? 9.927   -11.227 -37.161 1 61.03 ? 258 GLU   A OE2 1 
ATOM   2063 N  N   . PHE   A 1 274 ? 7.279   -13.918 -32.368 1 43.02 ? 259 PHE   A N   1 
ATOM   2064 C  CA  . PHE   A 1 274 ? 7.577   -15.003 -31.433 1 42.52 ? 259 PHE   A CA  1 
ATOM   2065 C  C   . PHE   A 1 274 ? 8.031   -16.226 -32.248 1 41.06 ? 259 PHE   A C   1 
ATOM   2066 O  O   . PHE   A 1 274 ? 7.418   -16.548 -33.264 1 40.73 ? 259 PHE   A O   1 
ATOM   2067 C  CB  . PHE   A 1 274 ? 6.342   -15.361 -30.585 1 42.79 ? 259 PHE   A CB  1 
ATOM   2068 C  CG  . PHE   A 1 274 ? 5.912   -14.274 -29.631 1 43.39 ? 259 PHE   A CG  1 
ATOM   2069 C  CD1 . PHE   A 1 274 ? 6.685   -13.95  -28.527 1 44.45 ? 259 PHE   A CD1 1 
ATOM   2070 C  CD2 . PHE   A 1 274 ? 4.741   -13.571 -29.838 1 43.56 ? 259 PHE   A CD2 1 
ATOM   2071 C  CE1 . PHE   A 1 274 ? 6.287   -12.943 -27.649 1 44.73 ? 259 PHE   A CE1 1 
ATOM   2072 C  CE2 . PHE   A 1 274 ? 4.363   -12.55  -28.977 1 44.18 ? 259 PHE   A CE2 1 
ATOM   2073 C  CZ  . PHE   A 1 274 ? 5.145   -12.231 -27.898 1 43.92 ? 259 PHE   A CZ  1 
ATOM   2074 N  N   . ALA   A 1 275 ? 9.102   -16.89  -31.809 1 39.68 ? 260 ALA   A N   1 
ATOM   2075 C  CA  . ALA   A 1 275 ? 9.641   -18.075 -32.481 1 38.59 ? 260 ALA   A CA  1 
ATOM   2076 C  C   . ALA   A 1 275 ? 8.718   -19.264 -32.281 1 37.87 ? 260 ALA   A C   1 
ATOM   2077 O  O   . ALA   A 1 275 ? 8.027   -19.359 -31.257 1 37.9  ? 260 ALA   A O   1 
ATOM   2078 C  CB  . ALA   A 1 275 ? 11.031  -18.397 -31.941 1 38.39 ? 260 ALA   A CB  1 
ATOM   2079 N  N   . GLY   A 1 276 ? 8.705   -20.168 -33.26  1 37.08 ? 261 GLY   A N   1 
ATOM   2080 C  CA  . GLY   A 1 276 ? 7.861   -21.354 -33.198 1 36.83 ? 261 GLY   A CA  1 
ATOM   2081 C  C   . GLY   A 1 276 ? 8.343   -22.383 -32.197 1 36.7  ? 261 GLY   A C   1 
ATOM   2082 O  O   . GLY   A 1 276 ? 9.446   -22.262 -31.656 1 36.67 ? 261 GLY   A O   1 
ATOM   2083 N  N   . GLY   A 1 277 ? 7.503   -23.389 -31.92  1 36.4  ? 262 GLY   A N   1 
ATOM   2084 C  CA  . GLY   A 1 277 ? 7.819   -24.468 -30.992 1 36.36 ? 262 GLY   A CA  1 
ATOM   2085 C  C   . GLY   A 1 277 ? 9.138   -25.149 -31.34  1 36.64 ? 262 GLY   A C   1 
ATOM   2086 O  O   . GLY   A 1 277 ? 9.455   -25.359 -32.519 1 37.32 ? 262 GLY   A O   1 
ATOM   2087 N  N   . SER   A 1 278 ? 9.942   -25.41  -30.325 1 35.85 ? 263 SER   A N   1 
ATOM   2088 C  CA  . SER   A 1 278 ? 11.236  -25.993 -30.527 1 35.83 ? 263 SER   A CA  1 
ATOM   2089 C  C   . SER   A 1 278 ? 11.647  -26.906 -29.4   1 35.46 ? 263 SER   A C   1 
ATOM   2090 O  O   . SER   A 1 278 ? 11.443  -26.563 -28.242 1 35.99 ? 263 SER   A O   1 
ATOM   2091 C  CB  . SER   A 1 278 ? 12.268  -24.891 -30.695 1 36.99 ? 263 SER   A CB  1 
ATOM   2092 O  OG  . SER   A 1 278 ? 13.543  -25.44  -30.957 1 40.26 ? 263 SER   A OG  1 
ATOM   2093 N  N   . ALA   A 1 279 ? 12.275  -28.046 -29.728 1 33.95 ? 264 ALA   A N   1 
ATOM   2094 C  CA  . ALA   A 1 279 ? 12.866  -28.892 -28.708 1 33.14 ? 264 ALA   A CA  1 
ATOM   2095 C  C   . ALA   A 1 279 ? 14.106  -28.199 -28.07  1 33.94 ? 264 ALA   A C   1 
ATOM   2096 O  O   . ALA   A 1 279 ? 14.55   -28.638 -27.025 1 34.34 ? 264 ALA   A O   1 
ATOM   2097 C  CB  . ALA   A 1 279 ? 13.213  -30.238 -29.271 1 32.27 ? 264 ALA   A CB  1 
ATOM   2098 N  N   . GLY   A 1 280 ? 14.568  -27.062 -28.634 1 33.88 ? 265 GLY   A N   1 
ATOM   2099 C  CA  . GLY   A 1 280 ? 15.557  -26.183 -28.024 1 33.88 ? 265 GLY   A CA  1 
ATOM   2100 C  C   . GLY   A 1 280 ? 14.996  -25.534 -26.757 1 34.46 ? 265 GLY   A C   1 
ATOM   2101 O  O   . GLY   A 1 280 ? 15.75   -25.011 -25.945 1 35.37 ? 265 GLY   A O   1 
ATOM   2102 N  N   . GLN   A 1 281 ? 13.659  -25.579 -26.561 1 34.34 ? 266 GLN   A N   1 
ATOM   2103 C  CA  . GLN   A 1 281 ? 12.934  -25.147 -25.363 1 34.5  ? 266 GLN   A CA  1 
ATOM   2104 C  C   . GLN   A 1 281 ? 12.841  -26.301 -24.32  1 35.41 ? 266 GLN   A C   1 
ATOM   2105 O  O   . GLN   A 1 281 ? 12.25   -26.098 -23.264 1 36.7  ? 266 GLN   A O   1 
ATOM   2106 C  CB  . GLN   A 1 281 ? 11.511  -24.651 -25.73  1 34.14 ? 266 GLN   A CB  1 
ATOM   2107 C  CG  . GLN   A 1 281 ? 11.5    -23.499 -26.716 1 34.46 ? 266 GLN   A CG  1 
ATOM   2108 C  CD  . GLN   A 1 281 ? 10.194  -23.328 -27.463 1 35.22 ? 266 GLN   A CD  1 
ATOM   2109 O  OE1 . GLN   A 1 281 ? 9.293   -24.172 -27.422 1 37.24 ? 266 GLN   A OE1 1 
ATOM   2110 N  NE2 . GLN   A 1 281 ? 10.077  -22.258 -28.229 1 33.62 ? 266 GLN   A NE2 1 
ATOM   2111 N  N   . SER   A 1 282 ? 13.353  -27.508 -24.626 1 35.16 ? 267 SER   A N   1 
ATOM   2112 C  CA  . SER   A 1 282 ? 13.349  -28.614 -23.666 1 35.76 ? 267 SER   A CA  1 
ATOM   2113 C  C   . SER   A 1 282 ? 14.324  -28.263 -22.539 1 36.3  ? 267 SER   A C   1 
ATOM   2114 O  O   . SER   A 1 282 ? 15.464  -27.893 -22.796 1 34.97 ? 267 SER   A O   1 
ATOM   2115 C  CB  . SER   A 1 282 ? 13.784  -29.921 -24.323 1 36.24 ? 267 SER   A CB  1 
ATOM   2116 O  OG  . SER   A 1 282 ? 14.234  -30.856 -23.349 1 37.81 ? 267 SER   A OG  1 
ATOM   2117 N  N   . SER   A 1 283 ? 13.866  -28.39  -21.299 1 37.68 ? 268 SER   A N   1 
ATOM   2118 C  CA  . SER   A 1 283 ? 14.697  -28.076 -20.148 1 39.1  ? 268 SER   A CA  1 
ATOM   2119 C  C   . SER   A 1 283 ? 15.617  -29.232 -19.777 1 41.02 ? 268 SER   A C   1 
ATOM   2120 O  O   . SER   A 1 283 ? 16.647  -28.993 -19.168 1 41.29 ? 268 SER   A O   1 
ATOM   2121 C  CB  . SER   A 1 283 ? 13.829  -27.709 -18.955 1 39.8  ? 268 SER   A CB  1 
ATOM   2122 O  OG  . SER   A 1 283 ? 13.192  -26.455 -19.118 1 42.29 ? 268 SER   A OG  1 
ATOM   2123 N  N   . VAL   A 1 284 ? 15.25   -30.482 -20.122 1 41.97 ? 269 VAL   A N   1 
ATOM   2124 C  CA  . VAL   A 1 284 ? 16.012  -31.637 -19.688 1 42.88 ? 269 VAL   A CA  1 
ATOM   2125 C  C   . VAL   A 1 284 ? 17.354  -31.719 -20.39  1 44.04 ? 269 VAL   A C   1 
ATOM   2126 O  O   . VAL   A 1 284 ? 18.349  -32.011 -19.729 1 44.93 ? 269 VAL   A O   1 
ATOM   2127 C  CB  . VAL   A 1 284 ? 15.208  -32.961 -19.733 1 43.76 ? 269 VAL   A CB  1 
ATOM   2128 C  CG1 . VAL   A 1 284 ? 15.183  -33.592 -21.132 1 43.59 ? 269 VAL   A CG1 1 
ATOM   2129 C  CG2 . VAL   A 1 284 ? 15.734  -33.942 -18.685 1 44.37 ? 269 VAL   A CG2 1 
ATOM   2130 N  N   . PHE   A 1 285 ? 17.421  -31.353 -21.664 1 43.9  ? 270 PHE   A N   1 
ATOM   2131 C  CA  . PHE   A 1 285 ? 18.679  -31.379 -22.395 1 44.44 ? 270 PHE   A CA  1 
ATOM   2132 C  C   . PHE   A 1 285 ? 19.567  -30.212 -22.021 1 44.01 ? 270 PHE   A C   1 
ATOM   2133 O  O   . PHE   A 1 285 ? 20.779  -30.377 -21.913 1 44.03 ? 270 PHE   A O   1 
ATOM   2134 C  CB  . PHE   A 1 285 ? 18.426  -31.431 -23.892 1 45.38 ? 270 PHE   A CB  1 
ATOM   2135 C  CG  . PHE   A 1 285 ? 18.129  -32.841 -24.309 1 47.03 ? 270 PHE   A CG  1 
ATOM   2136 C  CD1 . PHE   A 1 285 ? 16.833  -33.338 -24.264 1 48.22 ? 270 PHE   A CD1 1 
ATOM   2137 C  CD2 . PHE   A 1 285 ? 19.148  -33.686 -24.714 1 48.19 ? 270 PHE   A CD2 1 
ATOM   2138 C  CE1 . PHE   A 1 285 ? 16.562  -34.655 -24.614 1 49.32 ? 270 PHE   A CE1 1 
ATOM   2139 C  CE2 . PHE   A 1 285 ? 18.875  -35     -25.07  1 49.26 ? 270 PHE   A CE2 1 
ATOM   2140 C  CZ  . PHE   A 1 285 ? 17.586  -35.478 -25.015 1 49.33 ? 270 PHE   A CZ  1 
ATOM   2141 N  N   . GLN   A 1 286 ? 18.965  -29.034 -21.801 1 43.17 ? 271 GLN   A N   1 
ATOM   2142 C  CA  . GLN   A 1 286 ? 19.709  -27.859 -21.395 1 42.32 ? 271 GLN   A CA  1 
ATOM   2143 C  C   . GLN   A 1 286 ? 20.276  -28.058 -19.979 1 43.13 ? 271 GLN   A C   1 
ATOM   2144 O  O   . GLN   A 1 286 ? 21.363  -27.568 -19.698 1 43.45 ? 271 GLN   A O   1 
ATOM   2145 C  CB  . GLN   A 1 286 ? 18.814  -26.607 -21.441 1 41.22 ? 271 GLN   A CB  1 
ATOM   2146 C  CG  . GLN   A 1 286 ? 18.433  -26.178 -22.848 1 41.04 ? 271 GLN   A CG  1 
ATOM   2147 C  CD  . GLN   A 1 286 ? 18.466  -24.681 -23.033 1 41.38 ? 271 GLN   A CD  1 
ATOM   2148 O  OE1 . GLN   A 1 286 ? 19.253  -23.981 -22.41  1 41.21 ? 271 GLN   A OE1 1 
ATOM   2149 N  NE2 . GLN   A 1 286 ? 17.621  -24.149 -23.914 1 41.18 ? 271 GLN   A NE2 1 
ATOM   2150 N  N   . CYS   A 1 287 ? 19.566  -28.789 -19.097 1 43.23 ? 272 CYS   A N   1 
ATOM   2151 C  CA  . CYS   A 1 287 ? 20.03   -28.952 -17.728 1 43.86 ? 272 CYS   A CA  1 
ATOM   2152 C  C   . CYS   A 1 287 ? 21.252  -29.89  -17.626 1 42.84 ? 272 CYS   A C   1 
ATOM   2153 O  O   . CYS   A 1 287 ? 22.075  -29.681 -16.753 1 43.35 ? 272 CYS   A O   1 
ATOM   2154 C  CB  . CYS   A 1 287 ? 18.891  -29.338 -16.785 1 46.43 ? 272 CYS   A CB  1 
ATOM   2155 S  SG  . CYS   A 1 287 ? 18.725  -31.107 -16.469 1 57.05 ? 272 CYS   A SG  1 
ATOM   2156 N  N   . PHE   A 1 288 ? 21.412  -30.845 -18.553 1 41.45 ? 273 PHE   A N   1 
ATOM   2157 C  CA  . PHE   A 1 288 ? 22.591  -31.704 -18.557 1 40.74 ? 273 PHE   A CA  1 
ATOM   2158 C  C   . PHE   A 1 288 ? 23.774  -31.007 -19.203 1 40.14 ? 273 PHE   A C   1 
ATOM   2159 O  O   . PHE   A 1 288 ? 24.897  -31.214 -18.77  1 40.11 ? 273 PHE   A O   1 
ATOM   2160 C  CB  . PHE   A 1 288 ? 22.305  -33.09  -19.141 1 40.98 ? 273 PHE   A CB  1 
ATOM   2161 C  CG  . PHE   A 1 288 ? 21.502  -33.848 -18.121 1 41.97 ? 273 PHE   A CG  1 
ATOM   2162 C  CD1 . PHE   A 1 288 ? 22.019  -34.11  -16.874 1 42.54 ? 273 PHE   A CD1 1 
ATOM   2163 C  CD2 . PHE   A 1 288 ? 20.195  -34.222 -18.382 1 43.55 ? 273 PHE   A CD2 1 
ATOM   2164 C  CE1 . PHE   A 1 288 ? 21.259  -34.757 -15.911 1 43.9  ? 273 PHE   A CE1 1 
ATOM   2165 C  CE2 . PHE   A 1 288 ? 19.431  -34.87  -17.416 1 44.46 ? 273 PHE   A CE2 1 
ATOM   2166 C  CZ  . PHE   A 1 288 ? 19.965  -35.119 -16.182 1 44.03 ? 273 PHE   A CZ  1 
ATOM   2167 N  N   . ASP   A 1 289 ? 23.533  -30.115 -20.172 1 39.75 ? 274 ASP   A N   1 
ATOM   2168 C  CA  . ASP   A 1 289 ? 24.591  -29.314 -20.753 1 40.19 ? 274 ASP   A CA  1 
ATOM   2169 C  C   . ASP   A 1 289 ? 25.115  -28.346 -19.68  1 40.85 ? 274 ASP   A C   1 
ATOM   2170 O  O   . ASP   A 1 289 ? 26.324  -28.199 -19.544 1 41.07 ? 274 ASP   A O   1 
ATOM   2171 C  CB  . ASP   A 1 289 ? 24.079  -28.54  -21.965 1 41.53 ? 274 ASP   A CB  1 
ATOM   2172 C  CG  . ASP   A 1 289 ? 23.922  -29.399 -23.209 1 45.62 ? 274 ASP   A CG  1 
ATOM   2173 O  OD1 . ASP   A 1 289 ? 24.714  -30.343 -23.381 1 44.68 ? 274 ASP   A OD1 1 
ATOM   2174 O  OD2 . ASP   A 1 289 ? 23.005  -29.117 -24.014 1 49.13 ? 274 ASP   A OD2 1 
ATOM   2175 N  N   . VAL   A 1 290 ? 24.215  -27.727 -18.892 1 40.78 ? 275 VAL   A N   1 
ATOM   2176 C  CA  . VAL   A 1 290 ? 24.642  -26.847 -17.813 1 41.58 ? 275 VAL   A CA  1 
ATOM   2177 C  C   . VAL   A 1 290 ? 25.395  -27.666 -16.737 1 41.81 ? 275 VAL   A C   1 
ATOM   2178 O  O   . VAL   A 1 290 ? 26.512  -27.31  -16.373 1 42.19 ? 275 VAL   A O   1 
ATOM   2179 C  CB  . VAL   A 1 290 ? 23.464  -26.053 -17.2   1 43.02 ? 275 VAL   A CB  1 
ATOM   2180 C  CG1 . VAL   A 1 290 ? 23.914  -25.31  -15.946 1 43.75 ? 275 VAL   A CG1 1 
ATOM   2181 C  CG2 . VAL   A 1 290 ? 22.87   -25.081 -18.211 1 43.89 ? 275 VAL   A CG2 1 
ATOM   2182 N  N   . LEU   A 1 291 ? 24.801  -28.771 -16.262 1 41.79 ? 276 LEU   A N   1 
ATOM   2183 C  CA  . LEU   A 1 291 ? 25.409  -29.657 -15.259 1 42.05 ? 276 LEU   A CA  1 
ATOM   2184 C  C   . LEU   A 1 291 ? 26.838  -30.076 -15.623 1 42.17 ? 276 LEU   A C   1 
ATOM   2185 O  O   . LEU   A 1 291 ? 27.726  -29.98  -14.789 1 42.9  ? 276 LEU   A O   1 
ATOM   2186 C  CB  . LEU   A 1 291 ? 24.538  -30.905 -15.041 1 42.23 ? 276 LEU   A CB  1 
ATOM   2187 C  CG  . LEU   A 1 291 ? 25.079  -31.95  -14.059 1 44.21 ? 276 LEU   A CG  1 
ATOM   2188 C  CD1 . LEU   A 1 291 ? 24.969  -31.46  -12.605 1 44.99 ? 276 LEU   A CD1 1 
ATOM   2189 C  CD2 . LEU   A 1 291 ? 24.343  -33.269 -14.208 1 45.01 ? 276 LEU   A CD2 1 
ATOM   2190 N  N   . LEU   A 1 292 ? 27.065  -30.502 -16.864 1 41.72 ? 277 LEU   A N   1 
ATOM   2191 C  CA  . LEU   A 1 292 ? 28.372  -30.969 -17.32  1 41.84 ? 277 LEU   A CA  1 
ATOM   2192 C  C   . LEU   A 1 292 ? 29.321  -29.866 -17.822 1 43.32 ? 277 LEU   A C   1 
ATOM   2193 O  O   . LEU   A 1 292 ? 30.443  -30.167 -18.251 1 44.23 ? 277 LEU   A O   1 
ATOM   2194 C  CB  . LEU   A 1 292 ? 28.185  -32.053 -18.386 1 40.82 ? 277 LEU   A CB  1 
ATOM   2195 C  CG  . LEU   A 1 292 ? 27.361  -33.254 -17.91  1 40.35 ? 277 LEU   A CG  1 
ATOM   2196 C  CD1 . LEU   A 1 292 ? 26.965  -34.142 -19.062 1 40.29 ? 277 LEU   A CD1 1 
ATOM   2197 C  CD2 . LEU   A 1 292 ? 28.072  -34.019 -16.809 1 39.48 ? 277 LEU   A CD2 1 
ATOM   2198 N  N   . GLY   A 1 293 ? 28.899  -28.609 -17.743 1 42.86 ? 278 GLY   A N   1 
ATOM   2199 C  CA  . GLY   A 1 293 ? 29.73   -27.499 -18.17  1 43.52 ? 278 GLY   A CA  1 
ATOM   2200 C  C   . GLY   A 1 293 ? 29.971  -27.447 -19.662 1 44.72 ? 278 GLY   A C   1 
ATOM   2201 O  O   . GLY   A 1 293 ? 31.012  -26.981 -20.111 1 44.24 ? 278 GLY   A O   1 
ATOM   2202 N  N   . ILE   A 1 294 ? 29.009  -27.937 -20.446 1 46.21 ? 279 ILE   A N   1 
ATOM   2203 C  CA  . ILE   A 1 294 ? 29.064  -27.867 -21.896 1 47.89 ? 279 ILE   A CA  1 
ATOM   2204 C  C   . ILE   A 1 294 ? 28.452  -26.52  -22.149 1 51.32 ? 279 ILE   A C   1 
ATOM   2205 O  O   . ILE   A 1 294 ? 27.238  -26.374 -21.989 1 52.68 ? 279 ILE   A O   1 
ATOM   2206 C  CB  . ILE   A 1 294 ? 28.203  -29.008 -22.478 1 47.45 ? 279 ILE   A CB  1 
ATOM   2207 C  CG1 . ILE   A 1 294 ? 28.757  -30.379 -22.041 1 47.71 ? 279 ILE   A CG1 1 
ATOM   2208 C  CG2 . ILE   A 1 294 ? 28.123  -28.9   -23.988 1 47.61 ? 279 ILE   A CG2 1 
ATOM   2209 C  CD1 . ILE   A 1 294 ? 27.82   -31.432 -22.161 1 48.31 ? 279 ILE   A CD1 1 
ATOM   2210 N  N   . GLN   A 1 295 ? 29.27   -25.502 -22.415 1 52.9  ? 280 GLN   A N   1 
ATOM   2211 C  CA  . GLN   A 1 295 ? 28.752  -24.135 -22.524 1 54.53 ? 280 GLN   A CA  1 
ATOM   2212 C  C   . GLN   A 1 295 ? 28.077  -23.856 -23.841 1 55.09 ? 280 GLN   A C   1 
ATOM   2213 O  O   . GLN   A 1 295 ? 28.615  -23.161 -24.698 1 55.56 ? 280 GLN   A O   1 
ATOM   2214 C  CB  . GLN   A 1 295 ? 29.842  -23.118 -22.206 1 57.18 ? 280 GLN   A CB  1 
ATOM   2215 C  CG  . GLN   A 1 295 ? 30.328  -23.295 -20.77  1 62.55 ? 280 GLN   A CG  1 
ATOM   2216 C  CD  . GLN   A 1 295 ? 31.251  -22.204 -20.345 1 70.45 ? 280 GLN   A CD  1 
ATOM   2217 O  OE1 . GLN   A 1 295 ? 31.047  -21.565 -19.302 1 73.58 ? 280 GLN   A OE1 1 
ATOM   2218 N  NE2 . GLN   A 1 295 ? 32.29   -21.965 -21.147 1 71.53 ? 280 GLN   A NE2 1 
ATOM   2219 N  N   . GLN   A 1 296 ? 26.871  -24.392 -23.986 1 55.21 ? 281 GLN   A N   1 
ATOM   2220 C  CA  . GLN   A 1 296 ? 26.063  -24.239 -25.192 1 55.81 ? 281 GLN   A CA  1 
ATOM   2221 C  C   . GLN   A 1 296 ? 25.65   -22.799 -25.414 1 57.48 ? 281 GLN   A C   1 
ATOM   2222 O  O   . GLN   A 1 296 ? 25.549  -22.384 -26.555 1 57.35 ? 281 GLN   A O   1 
ATOM   2223 C  CB  . GLN   A 1 296 ? 24.802  -25.131 -25.127 1 54.9  ? 281 GLN   A CB  1 
ATOM   2224 C  CG  . GLN   A 1 296 ? 25.084  -26.621 -25.085 1 54.12 ? 281 GLN   A CG  1 
ATOM   2225 C  CD  . GLN   A 1 296 ? 25.571  -27.197 -26.389 1 54.01 ? 281 GLN   A CD  1 
ATOM   2226 O  OE1 . GLN   A 1 296 ? 25.743  -26.504 -27.393 1 55.91 ? 281 GLN   A OE1 1 
ATOM   2227 N  NE2 . GLN   A 1 296 ? 25.8    -28.489 -26.403 1 52.32 ? 281 GLN   A NE2 1 
ATOM   2228 N  N   . THR   A 1 297 ? 25.42   -22.046 -24.326 1 59.01 ? 282 THR   A N   1 
ATOM   2229 C  CA  . THR   A 1 297 ? 24.974  -20.656 -24.338 1 61.11 ? 282 THR   A CA  1 
ATOM   2230 C  C   . THR   A 1 297 ? 26.114  -19.605 -24.314 1 63.05 ? 282 THR   A C   1 
ATOM   2231 O  O   . THR   A 1 297 ? 25.851  -18.416 -24.128 1 63.32 ? 282 THR   A O   1 
ATOM   2232 C  CB  . THR   A 1 297 ? 23.999  -20.452 -23.181 1 62.01 ? 282 THR   A CB  1 
ATOM   2233 O  OG1 . THR   A 1 297 ? 24.635  -20.848 -21.963 1 62.6  ? 282 THR   A OG1 1 
ATOM   2234 C  CG2 . THR   A 1 297 ? 22.712  -21.237 -23.374 1 62.35 ? 282 THR   A CG2 1 
ATOM   2235 N  N   . ALA   A 1 298 ? 27.358  -20.032 -24.536 1 64.07 ? 283 ALA   A N   1 
ATOM   2236 C  CA  . ALA   A 1 298 ? 28.503  -19.127 -24.503 1 65.32 ? 283 ALA   A CA  1 
ATOM   2237 C  C   . ALA   A 1 298 ? 29.101  -18.866 -25.899 1 66.61 ? 283 ALA   A C   1 
ATOM   2238 O  O   . ALA   A 1 298 ? 28.891  -19.657 -26.82  1 67.05 ? 283 ALA   A O   1 
ATOM   2239 C  CB  . ALA   A 1 298 ? 29.568  -19.701 -23.573 1 65.39 ? 283 ALA   A CB  1 
ATOM   2240 N  N   . GLY   A 1 299 ? 29.825  -17.753 -26.046 1 67.04 ? 284 GLY   A N   1 
ATOM   2241 C  CA  . GLY   A 1 299 ? 30.53   -17.427 -27.285 1 67.54 ? 284 GLY   A CA  1 
ATOM   2242 C  C   . GLY   A 1 299 ? 29.921  -16.378 -28.198 1 67.53 ? 284 GLY   A C   1 
ATOM   2243 O  O   . GLY   A 1 299 ? 30.599  -15.867 -29.099 1 67.92 ? 284 GLY   A O   1 
ATOM   2244 N  N   . GLY   A 1 300 ? 28.642  -16.077 -28.004 1 66.47 ? 285 GLY   A N   1 
ATOM   2245 C  CA  . GLY   A 1 300 ? 27.959  -15.106 -28.85  1 65.71 ? 285 GLY   A CA  1 
ATOM   2246 C  C   . GLY   A 1 300 ? 27.586  -15.591 -30.246 1 64.49 ? 285 GLY   A C   1 
ATOM   2247 O  O   . GLY   A 1 300 ? 27.139  -14.796 -31.078 1 64.97 ? 285 GLY   A O   1 
ATOM   2248 N  N   . GLY   A 1 301 ? 27.746  -16.887 -30.51  1 62.71 ? 286 GLY   A N   1 
ATOM   2249 C  CA  . GLY   A 1 301 ? 27.368  -17.475 -31.793 1 61.25 ? 286 GLY   A CA  1 
ATOM   2250 C  C   . GLY   A 1 301 ? 25.867  -17.652 -31.94  1 59.59 ? 286 GLY   A C   1 
ATOM   2251 O  O   . GLY   A 1 301 ? 25.119  -17.425 -30.987 1 59.39 ? 286 GLY   A O   1 
ATOM   2252 N  N   . HIS   A 1 302 ? 25.405  -18.057 -33.122 1 58.51 ? 287 HIS   A N   1 
ATOM   2253 C  CA  . HIS   A 1 302 ? 23.98   -18.251 -33.362 1 58.17 ? 287 HIS   A CA  1 
ATOM   2254 C  C   . HIS   A 1 302 ? 23.329  -19.366 -32.523 1 55.91 ? 287 HIS   A C   1 
ATOM   2255 O  O   . HIS   A 1 302 ? 22.236  -19.15  -32.02  1 55.67 ? 287 HIS   A O   1 
ATOM   2256 C  CB  . HIS   A 1 302 ? 23.717  -18.455 -34.849 1 60.9  ? 287 HIS   A CB  1 
ATOM   2257 C  CG  . HIS   A 1 302 ? 23.734  -17.161 -35.591 1 67.04 ? 287 HIS   A CG  1 
ATOM   2258 N  ND1 . HIS   A 1 302 ? 24.922  -16.601 -36.046 1 70.1  ? 287 HIS   A ND1 1 
ATOM   2259 C  CD2 . HIS   A 1 302 ? 22.713  -16.318 -35.874 1 69.08 ? 287 HIS   A CD2 1 
ATOM   2260 C  CE1 . HIS   A 1 302 ? 24.58   -15.459 -36.621 1 70.96 ? 287 HIS   A CE1 1 
ATOM   2261 N  NE2 . HIS   A 1 302 ? 23.26   -15.245 -36.541 1 70.9  ? 287 HIS   A NE2 1 
ATOM   2262 N  N   . ALA   A 1 303 ? 24      -20.526 -32.342 1 53.97 ? 288 ALA   A N   1 
ATOM   2263 C  CA  . ALA   A 1 303 ? 23.466  -21.646 -31.564 1 52.42 ? 288 ALA   A CA  1 
ATOM   2264 C  C   . ALA   A 1 303 ? 23.271  -21.256 -30.096 1 51.26 ? 288 ALA   A C   1 
ATOM   2265 O  O   . ALA   A 1 303 ? 22.236  -21.566 -29.483 1 51.77 ? 288 ALA   A O   1 
ATOM   2266 C  CB  . ALA   A 1 303 ? 24.392  -22.857 -31.683 1 52.14 ? 288 ALA   A CB  1 
ATOM   2267 N  N   . ALA   A 1 304 ? 24.253  -20.532 -29.553 1 49.43 ? 289 ALA   A N   1 
ATOM   2268 C  CA  . ALA   A 1 304 ? 24.246  -20.047 -28.185 1 48.01 ? 289 ALA   A CA  1 
ATOM   2269 C  C   . ALA   A 1 304 ? 23.098  -19.081 -27.959 1 46.66 ? 289 ALA   A C   1 
ATOM   2270 O  O   . ALA   A 1 304 ? 22.359  -19.232 -26.983 1 47.62 ? 289 ALA   A O   1 
ATOM   2271 C  CB  . ALA   A 1 304 ? 25.59   -19.387 -27.864 1 47.63 ? 289 ALA   A CB  1 
ATOM   2272 N  N   . GLN   A 1 305 ? 22.918  -18.115 -28.88  1 44.74 ? 290 GLN   A N   1 
ATOM   2273 C  CA  . GLN   A 1 305 ? 21.864  -17.124 -28.808 1 43.37 ? 290 GLN   A CA  1 
ATOM   2274 C  C   . GLN   A 1 305 ? 20.504  -17.807 -28.858 1 42.38 ? 290 GLN   A C   1 
ATOM   2275 O  O   . GLN   A 1 305 ? 19.666  -17.521 -28.02  1 42.61 ? 290 GLN   A O   1 
ATOM   2276 C  CB  . GLN   A 1 305 ? 21.998  -16.109 -29.948 1 44.23 ? 290 GLN   A CB  1 
ATOM   2277 C  CG  . GLN   A 1 305 ? 21.045  -14.937 -29.797 1 47.36 ? 290 GLN   A CG  1 
ATOM   2278 C  CD  . GLN   A 1 305 ? 21.403  -14.089 -28.593 1 52.29 ? 290 GLN   A CD  1 
ATOM   2279 O  OE1 . GLN   A 1 305 ? 22.519  -13.55  -28.507 1 56.11 ? 290 GLN   A OE1 1 
ATOM   2280 N  NE2 . GLN   A 1 305 ? 20.475  -13.942 -27.64  1 49.67 ? 290 GLN   A NE2 1 
ATOM   2281 N  N   . PHE   A 1 306 ? 20.319  -18.768 -29.778 1 41.12 ? 291 PHE   A N   1 
ATOM   2282 C  CA  . PHE   A 1 306 ? 19.068  -19.494 -29.919 1 40.17 ? 291 PHE   A CA  1 
ATOM   2283 C  C   . PHE   A 1 306 ? 18.68   -20.219 -28.634 1 39.96 ? 291 PHE   A C   1 
ATOM   2284 O  O   . PHE   A 1 306 ? 17.57   -20.034 -28.147 1 40.34 ? 291 PHE   A O   1 
ATOM   2285 C  CB  . PHE   A 1 306 ? 19.116  -20.457 -31.129 1 39.73 ? 291 PHE   A CB  1 
ATOM   2286 C  CG  . PHE   A 1 306 ? 17.8    -21.158 -31.349 1 40.72 ? 291 PHE   A CG  1 
ATOM   2287 C  CD1 . PHE   A 1 306 ? 16.69   -20.46  -31.814 1 41.03 ? 291 PHE   A CD1 1 
ATOM   2288 C  CD2 . PHE   A 1 306 ? 17.647  -22.504 -31.032 1 41.34 ? 291 PHE   A CD2 1 
ATOM   2289 C  CE1 . PHE   A 1 306 ? 15.469  -21.103 -31.984 1 41.25 ? 291 PHE   A CE1 1 
ATOM   2290 C  CE2 . PHE   A 1 306 ? 16.425  -23.143 -31.209 1 41.39 ? 291 PHE   A CE2 1 
ATOM   2291 C  CZ  . PHE   A 1 306 ? 15.344  -22.44  -31.679 1 41.08 ? 291 PHE   A CZ  1 
ATOM   2292 N  N   . LEU   A 1 307 ? 19.592  -21.016 -28.064 1 39.46 ? 292 LEU   A N   1 
ATOM   2293 C  CA  . LEU   A 1 307 ? 19.318  -21.774 -26.848 1 38.83 ? 292 LEU   A CA  1 
ATOM   2294 C  C   . LEU   A 1 307 ? 19.069  -20.882 -25.638 1 40.06 ? 292 LEU   A C   1 
ATOM   2295 O  O   . LEU   A 1 307 ? 18.205  -21.193 -24.81  1 40.63 ? 292 LEU   A O   1 
ATOM   2296 C  CB  . LEU   A 1 307 ? 20.426  -22.804 -26.59  1 38.12 ? 292 LEU   A CB  1 
ATOM   2297 C  CG  . LEU   A 1 307 ? 20.45   -23.966 -27.604 1 38.47 ? 292 LEU   A CG  1 
ATOM   2298 C  CD1 . LEU   A 1 307 ? 21.716  -24.815 -27.475 1 38.37 ? 292 LEU   A CD1 1 
ATOM   2299 C  CD2 . LEU   A 1 307 ? 19.204  -24.805 -27.488 1 38.56 ? 292 LEU   A CD2 1 
ATOM   2300 N  N   . GLN   A 1 308 ? 19.769  -19.746 -25.552 1 40.56 ? 293 GLN   A N   1 
ATOM   2301 C  CA  . GLN   A 1 308 ? 19.532  -18.798 -24.476 1 41.35 ? 293 GLN   A CA  1 
ATOM   2302 C  C   . GLN   A 1 308 ? 18.124  -18.207 -24.625 1 41.15 ? 293 GLN   A C   1 
ATOM   2303 O  O   . GLN   A 1 308 ? 17.342  -18.225 -23.667 1 41.93 ? 293 GLN   A O   1 
ATOM   2304 C  CB  . GLN   A 1 308 ? 20.595  -17.694 -24.469 1 44.36 ? 293 GLN   A CB  1 
ATOM   2305 C  CG  . GLN   A 1 308 ? 20.4    -16.702 -23.32  1 49.4  ? 293 GLN   A CG  1 
ATOM   2306 C  CD  . GLN   A 1 308 ? 20.661  -17.339 -21.974 1 56.29 ? 293 GLN   A CD  1 
ATOM   2307 O  OE1 . GLN   A 1 308 ? 19.875  -17.188 -21.014 1 58.8  ? 293 GLN   A OE1 1 
ATOM   2308 N  NE2 . GLN   A 1 308 ? 21.778  -18.062 -21.866 1 56.17 ? 293 GLN   A NE2 1 
ATOM   2309 N  N   . ASP   A 1 309 ? 17.774  -17.753 -25.842 1 40.17 ? 294 ASP   A N   1 
ATOM   2310 C  CA  . ASP   A 1 309 ? 16.46   -17.181 -26.129 1 40.11 ? 294 ASP   A CA  1 
ATOM   2311 C  C   . ASP   A 1 309 ? 15.335  -18.15  -25.838 1 39.42 ? 294 ASP   A C   1 
ATOM   2312 O  O   . ASP   A 1 309 ? 14.283  -17.737 -25.382 1 39.2  ? 294 ASP   A O   1 
ATOM   2313 C  CB  . ASP   A 1 309 ? 16.37   -16.715 -27.597 1 42.56 ? 294 ASP   A CB  1 
ATOM   2314 C  CG  . ASP   A 1 309 ? 17.187  -15.485 -27.919 1 48.13 ? 294 ASP   A CG  1 
ATOM   2315 O  OD1 . ASP   A 1 309 ? 17.662  -14.817 -26.963 1 49.41 ? 294 ASP   A OD1 1 
ATOM   2316 O  OD2 . ASP   A 1 309 ? 17.372  -15.197 -29.126 1 50.51 ? 294 ASP   A OD2 1 
ATOM   2317 N  N   . MET   A 1 310 ? 15.552  -19.446 -26.114 1 39.31 ? 295 MET   A N   1 
ATOM   2318 C  CA  . MET   A 1 310 ? 14.54   -20.471 -25.884 1 39.06 ? 295 MET   A CA  1 
ATOM   2319 C  C   . MET   A 1 310 ? 14.212  -20.701 -24.431 1 39.58 ? 295 MET   A C   1 
ATOM   2320 O  O   . MET   A 1 310 ? 13.182  -21.306 -24.151 1 39.8  ? 295 MET   A O   1 
ATOM   2321 C  CB  . MET   A 1 310 ? 14.913  -21.784 -26.578 1 39.36 ? 295 MET   A CB  1 
ATOM   2322 C  CG  . MET   A 1 310 ? 14.837  -21.698 -28.108 1 40.15 ? 295 MET   A CG  1 
ATOM   2323 S  SD  . MET   A 1 310 ? 13.26   -21.053 -28.766 1 41.48 ? 295 MET   A SD  1 
ATOM   2324 C  CE  . MET   A 1 310 ? 13.722  -19.378 -29.188 1 35.78 ? 295 MET   A CE  1 
ATOM   2325 N  N   . ARG   A 1 311 ? 15.018  -20.165 -23.492 1 39.74 ? 296 ARG   A N   1 
ATOM   2326 C  CA  . ARG   A 1 311 ? 14.718  -20.277 -22.07  1 39.83 ? 296 ARG   A CA  1 
ATOM   2327 C  C   . ARG   A 1 311 ? 13.519  -19.431 -21.673 1 40.07 ? 296 ARG   A C   1 
ATOM   2328 O  O   . ARG   A 1 311 ? 12.805  -19.797 -20.752 1 39.73 ? 296 ARG   A O   1 
ATOM   2329 C  CB  . ARG   A 1 311 ? 15.943  -19.921 -21.235 1 41.22 ? 296 ARG   A CB  1 
ATOM   2330 C  CG  . ARG   A 1 311 ? 17.1    -20.838 -21.534 1 42.72 ? 296 ARG   A CG  1 
ATOM   2331 C  CD  . ARG   A 1 311 ? 18.134  -20.733 -20.467 1 44.72 ? 296 ARG   A CD  1 
ATOM   2332 N  NE  . ARG   A 1 311 ? 19.228  -21.673 -20.684 1 47.05 ? 296 ARG   A NE  1 
ATOM   2333 C  CZ  . ARG   A 1 311 ? 20.313  -21.748 -19.923 1 48.73 ? 296 ARG   A CZ  1 
ATOM   2334 N  NH1 . ARG   A 1 311 ? 20.465  -20.931 -18.885 1 47.84 ? 296 ARG   A NH1 1 
ATOM   2335 N  NH2 . ARG   A 1 311 ? 21.254  -22.634 -20.192 1 48.87 ? 296 ARG   A NH2 1 
ATOM   2336 N  N   . ARG   A 1 312 ? 13.274  -18.313 -22.372 1 40.79 ? 297 ARG   A N   1 
ATOM   2337 C  CA  . ARG   A 1 312 ? 12.093  -17.486 -22.092 1 41.93 ? 297 ARG   A CA  1 
ATOM   2338 C  C   . ARG   A 1 312 ? 10.782  -18.115 -22.626 1 41.36 ? 297 ARG   A C   1 
ATOM   2339 O  O   . ARG   A 1 312 ? 9.693   -17.616 -22.336 1 42.15 ? 297 ARG   A O   1 
ATOM   2340 C  CB  . ARG   A 1 312 ? 12.299  -16.05  -22.588 1 45.33 ? 297 ARG   A CB  1 
ATOM   2341 C  CG  . ARG   A 1 312 ? 13.364  -15.288 -21.768 1 51.52 ? 297 ARG   A CG  1 
ATOM   2342 C  CD  . ARG   A 1 312 ? 12.811  -14.765 -20.443 1 57.01 ? 297 ARG   A CD  1 
ATOM   2343 N  NE  . ARG   A 1 312 ? 13.874  -14.385 -19.504 1 61.77 ? 297 ARG   A NE  1 
ATOM   2344 C  CZ  . ARG   A 1 312 ? 13.657  -13.936 -18.267 1 65.36 ? 297 ARG   A CZ  1 
ATOM   2345 N  NH1 . ARG   A 1 312 ? 12.416  -13.764 -17.823 1 65.51 ? 297 ARG   A NH1 1 
ATOM   2346 N  NH2 . ARG   A 1 312 ? 14.681  -13.614 -17.479 1 64.89 ? 297 ARG   A NH2 1 
ATOM   2347 N  N   . TYR   A 1 313 ? 10.889  -19.209 -23.399 1 39.61 ? 298 TYR   A N   1 
ATOM   2348 C  CA  . TYR   A 1 313 ? 9.757   -19.983 -23.918 1 37.89 ? 298 TYR   A CA  1 
ATOM   2349 C  C   . TYR   A 1 313 ? 9.492   -21.239 -23.041 1 37.97 ? 298 TYR   A C   1 
ATOM   2350 O  O   . TYR   A 1 313 ? 8.623   -22.044 -23.378 1 37.54 ? 298 TYR   A O   1 
ATOM   2351 C  CB  . TYR   A 1 313 ? 10.018  -20.409 -25.365 1 36.66 ? 298 TYR   A CB  1 
ATOM   2352 C  CG  . TYR   A 1 313 ? 10.054  -19.27  -26.356 1 36.36 ? 298 TYR   A CG  1 
ATOM   2353 C  CD1 . TYR   A 1 313 ? 11.086  -18.344 -26.344 1 36.67 ? 298 TYR   A CD1 1 
ATOM   2354 C  CD2 . TYR   A 1 313 ? 9.085   -19.151 -27.341 1 36.75 ? 298 TYR   A CD2 1 
ATOM   2355 C  CE1 . TYR   A 1 313 ? 11.123  -17.299 -27.251 1 37.77 ? 298 TYR   A CE1 1 
ATOM   2356 C  CE2 . TYR   A 1 313 ? 9.108   -18.109 -28.25  1 37.73 ? 298 TYR   A CE2 1 
ATOM   2357 C  CZ  . TYR   A 1 313 ? 10.124  -17.179 -28.199 1 39    ? 298 TYR   A CZ  1 
ATOM   2358 O  OH  . TYR   A 1 313 ? 10.17   -16.163 -29.12  1 41.08 ? 298 TYR   A OH  1 
ATOM   2359 N  N   . MET   A 1 314 ? 10.239  -21.397 -21.92  1 37.91 ? 299 MET   A N   1 
ATOM   2360 C  CA  . MET   A 1 314 ? 10.106  -22.478 -20.956 1 38.51 ? 299 MET   A CA  1 
ATOM   2361 C  C   . MET   A 1 314 ? 9.227   -22.02  -19.797 1 39.29 ? 299 MET   A C   1 
ATOM   2362 O  O   . MET   A 1 314 ? 9.261   -20.84  -19.441 1 39.43 ? 299 MET   A O   1 
ATOM   2363 C  CB  . MET   A 1 314 ? 11.487  -22.782 -20.362 1 38.56 ? 299 MET   A CB  1 
ATOM   2364 C  CG  . MET   A 1 314 ? 12.407  -23.457 -21.303 1 40    ? 299 MET   A CG  1 
ATOM   2365 S  SD  . MET   A 1 314 ? 13.962  -23.825 -20.435 1 38.1  ? 299 MET   A SD  1 
ATOM   2366 C  CE  . MET   A 1 314 ? 14.969  -24.278 -21.8   1 33.17 ? 299 MET   A CE  1 
ATOM   2367 N  N   . PRO   A 1 315 ? 8.56    -22.947 -19.078 1 39.77 ? 300 PRO   A N   1 
ATOM   2368 C  CA  . PRO   A 1 315 ? 7.81    -22.537 -17.875 1 40.34 ? 300 PRO   A CA  1 
ATOM   2369 C  C   . PRO   A 1 315 ? 8.741   -21.849 -16.873 1 41.5  ? 300 PRO   A C   1 
ATOM   2370 O  O   . PRO   A 1 315 ? 9.915   -22.204 -16.786 1 41.69 ? 300 PRO   A O   1 
ATOM   2371 C  CB  . PRO   A 1 315 ? 7.246   -23.859 -17.345 1 40.72 ? 300 PRO   A CB  1 
ATOM   2372 C  CG  . PRO   A 1 315 ? 7.228   -24.774 -18.535 1 40.88 ? 300 PRO   A CG  1 
ATOM   2373 C  CD  . PRO   A 1 315 ? 8.442   -24.401 -19.323 1 39.17 ? 300 PRO   A CD  1 
ATOM   2374 N  N   . PRO   A 1 316 ? 8.273   -20.771 -16.222 1 42.04 ? 301 PRO   A N   1 
ATOM   2375 C  CA  . PRO   A 1 316 ? 9.16    -19.993 -15.341 1 42.28 ? 301 PRO   A CA  1 
ATOM   2376 C  C   . PRO   A 1 316 ? 9.919   -20.797 -14.291 1 43.08 ? 301 PRO   A C   1 
ATOM   2377 O  O   . PRO   A 1 316 ? 11.093  -20.531 -14.095 1 43.8  ? 301 PRO   A O   1 
ATOM   2378 C  CB  . PRO   A 1 316 ? 8.226   -18.952 -14.707 1 42.89 ? 301 PRO   A CB  1 
ATOM   2379 C  CG  . PRO   A 1 316 ? 6.839   -19.456 -14.961 1 43.21 ? 301 PRO   A CG  1 
ATOM   2380 C  CD  . PRO   A 1 316 ? 6.928   -20.183 -16.28  1 41.57 ? 301 PRO   A CD  1 
ATOM   2381 N  N   . ALA   A 1 317 ? 9.286   -21.783 -13.653 1 43    ? 302 ALA   A N   1 
ATOM   2382 C  CA  . ALA   A 1 317 ? 9.956   -22.604 -12.649 1 43.29 ? 302 ALA   A CA  1 
ATOM   2383 C  C   . ALA   A 1 317 ? 11.121  -23.401 -13.265 1 44.08 ? 302 ALA   A C   1 
ATOM   2384 O  O   . ALA   A 1 317 ? 12.142  -23.602 -12.612 1 45.05 ? 302 ALA   A O   1 
ATOM   2385 C  CB  . ALA   A 1 317 ? 8.96    -23.554 -12.012 1 43.04 ? 302 ALA   A CB  1 
ATOM   2386 N  N   . HIS   A 1 318 ? 10.982  -23.831 -14.531 1 43.41 ? 303 HIS   A N   1 
ATOM   2387 C  CA  . HIS   A 1 318 ? 12.016  -24.601 -15.242 1 42.52 ? 303 HIS   A CA  1 
ATOM   2388 C  C   . HIS   A 1 318 ? 13.166  -23.723 -15.722 1 42.37 ? 303 HIS   A C   1 
ATOM   2389 O  O   . HIS   A 1 318 ? 14.314  -24.152 -15.729 1 41.48 ? 303 HIS   A O   1 
ATOM   2390 C  CB  . HIS   A 1 318 ? 11.386  -25.375 -16.405 1 41.85 ? 303 HIS   A CB  1 
ATOM   2391 C  CG  . HIS   A 1 318 ? 10.328  -26.346 -15.986 1 42.99 ? 303 HIS   A CG  1 
ATOM   2392 N  ND1 . HIS   A 1 318 ? 9.509   -26.948 -16.915 1 44.62 ? 303 HIS   A ND1 1 
ATOM   2393 C  CD2 . HIS   A 1 318 ? 10.009  -26.822 -14.755 1 43.96 ? 303 HIS   A CD2 1 
ATOM   2394 C  CE1 . HIS   A 1 318 ? 8.716   -27.756 -16.23  1 45.03 ? 303 HIS   A CE1 1 
ATOM   2395 N  NE2 . HIS   A 1 318 ? 8.982   -27.712 -14.925 1 45.12 ? 303 HIS   A NE2 1 
ATOM   2396 N  N   . ARG   A 1 319 ? 12.848  -22.492 -16.108 1 43.05 ? 304 ARG   A N   1 
ATOM   2397 C  CA  . ARG   A 1 319 ? 13.808  -21.476 -16.495 1 44.65 ? 304 ARG   A CA  1 
ATOM   2398 C  C   . ARG   A 1 319 ? 14.668  -21.121 -15.258 1 46.31 ? 304 ARG   A C   1 
ATOM   2399 O  O   . ARG   A 1 319 ? 15.884  -20.951 -15.384 1 46.67 ? 304 ARG   A O   1 
ATOM   2400 C  CB  . ARG   A 1 319 ? 13.007  -20.258 -16.942 1 45.99 ? 304 ARG   A CB  1 
ATOM   2401 C  CG  . ARG   A 1 319 ? 13.791  -19.104 -17.562 1 48.49 ? 304 ARG   A CG  1 
ATOM   2402 C  CD  . ARG   A 1 319 ? 12.862  -17.913 -17.84  1 51.15 ? 304 ARG   A CD  1 
ATOM   2403 N  NE  . ARG   A 1 319 ? 11.577  -18.33  -18.415 1 53.21 ? 304 ARG   A NE  1 
ATOM   2404 C  CZ  . ARG   A 1 319 ? 10.446  -17.633 -18.318 1 54.46 ? 304 ARG   A CZ  1 
ATOM   2405 N  NH1 . ARG   A 1 319 ? 10.43   -16.462 -17.689 1 53.89 ? 304 ARG   A NH1 1 
ATOM   2406 N  NH2 . ARG   A 1 319 ? 9.32    -18.105 -18.846 1 52.78 ? 304 ARG   A NH2 1 
ATOM   2407 N  N   . ASN   A 1 320 ? 14.024  -21.036 -14.064 1 47.04 ? 305 ASN   A N   1 
ATOM   2408 C  CA  . ASN   A 1 320 ? 14.65   -20.758 -12.772 1 48.51 ? 305 ASN   A CA  1 
ATOM   2409 C  C   . ASN   A 1 320 ? 15.598  -21.893 -12.4   1 48.66 ? 305 ASN   A C   1 
ATOM   2410 O  O   . ASN   A 1 320 ? 16.675  -21.639 -11.866 1 49.15 ? 305 ASN   A O   1 
ATOM   2411 C  CB  . ASN   A 1 320 ? 13.587  -20.639 -11.664 1 50.7  ? 305 ASN   A CB  1 
ATOM   2412 C  CG  . ASN   A 1 320 ? 12.682  -19.437 -11.764 1 55.78 ? 305 ASN   A CG  1 
ATOM   2413 O  OD1 . ASN   A 1 320 ? 12.915  -18.515 -12.56  1 57.97 ? 305 ASN   A OD1 1 
ATOM   2414 N  ND2 . ASN   A 1 320 ? 11.601  -19.436 -10.971 1 56.46 ? 305 ASN   A ND2 1 
ATOM   2415 N  N   . PHE   A 1 321 ? 15.182  -23.14  -12.643 1 47.78 ? 306 PHE   A N   1 
ATOM   2416 C  CA  . PHE   A 1 321 ? 15.991  -24.312 -12.347 1 47.45 ? 306 PHE   A CA  1 
ATOM   2417 C  C   . PHE   A 1 321 ? 17.308  -24.277 -13.118 1 47.9  ? 306 PHE   A C   1 
ATOM   2418 O  O   . PHE   A 1 321 ? 18.358  -24.538 -12.531 1 48.78 ? 306 PHE   A O   1 
ATOM   2419 C  CB  . PHE   A 1 321 ? 15.209  -25.589 -12.658 1 46.6  ? 306 PHE   A CB  1 
ATOM   2420 C  CG  . PHE   A 1 321 ? 15.978  -26.846 -12.353 1 46.88 ? 306 PHE   A CG  1 
ATOM   2421 C  CD1 . PHE   A 1 321 ? 16.203  -27.239 -11.046 1 47.32 ? 306 PHE   A CD1 1 
ATOM   2422 C  CD2 . PHE   A 1 321 ? 16.495  -27.624 -13.37  1 47.27 ? 306 PHE   A CD2 1 
ATOM   2423 C  CE1 . PHE   A 1 321 ? 16.915  -28.396 -10.764 1 47.75 ? 306 PHE   A CE1 1 
ATOM   2424 C  CE2 . PHE   A 1 321 ? 17.212  -28.779 -13.084 1 47.72 ? 306 PHE   A CE2 1 
ATOM   2425 C  CZ  . PHE   A 1 321 ? 17.41   -29.161 -11.785 1 47.4  ? 306 PHE   A CZ  1 
ATOM   2426 N  N   . LEU   A 1 322 ? 17.261  -23.913 -14.408 1 47.24 ? 307 LEU   A N   1 
ATOM   2427 C  CA  . LEU   A 1 322 ? 18.451  -23.835 -15.236 1 47.42 ? 307 LEU   A CA  1 
ATOM   2428 C  C   . LEU   A 1 322 ? 19.437  -22.792 -14.733 1 47.99 ? 307 LEU   A C   1 
ATOM   2429 O  O   . LEU   A 1 322 ? 20.634  -23.081 -14.635 1 47.67 ? 307 LEU   A O   1 
ATOM   2430 C  CB  . LEU   A 1 322 ? 18.104  -23.567 -16.705 1 47.26 ? 307 LEU   A CB  1 
ATOM   2431 C  CG  . LEU   A 1 322 ? 17.379  -24.67  -17.453 1 49.08 ? 307 LEU   A CG  1 
ATOM   2432 C  CD1 . LEU   A 1 322 ? 17.195  -24.301 -18.904 1 48.96 ? 307 LEU   A CD1 1 
ATOM   2433 C  CD2 . LEU   A 1 322 ? 18.146  -25.944 -17.403 1 49.76 ? 307 LEU   A CD2 1 
ATOM   2434 N  N   . CYS   A 1 323 ? 18.944  -21.593 -14.401 1 48.76 ? 308 CYS   A N   1 
ATOM   2435 C  CA  . CYS   A 1 323 ? 19.843  -20.558 -13.918 1 49.91 ? 308 CYS   A CA  1 
ATOM   2436 C  C   . CYS   A 1 323 ? 20.406  -20.914 -12.515 1 49.34 ? 308 CYS   A C   1 
ATOM   2437 O  O   . CYS   A 1 323 ? 21.558  -20.598 -12.238 1 49.92 ? 308 CYS   A O   1 
ATOM   2438 C  CB  . CYS   A 1 323 ? 19.239  -19.157 -14.001 1 52.25 ? 308 CYS   A CB  1 
ATOM   2439 S  SG  . CYS   A 1 323 ? 18.022  -18.784 -12.718 1 60.16 ? 308 CYS   A SG  1 
ATOM   2440 N  N   . SER   A 1 324 ? 19.657  -21.664 -11.697 1 48.17 ? 309 SER   A N   1 
ATOM   2441 C  CA  . SER   A 1 324 ? 20.142  -22.139 -10.415 1 48.1  ? 309 SER   A CA  1 
ATOM   2442 C  C   . SER   A 1 324 ? 21.268  -23.169 -10.616 1 47.9  ? 309 SER   A C   1 
ATOM   2443 O  O   . SER   A 1 324 ? 22.212  -23.19  -9.831  1 48.19 ? 309 SER   A O   1 
ATOM   2444 C  CB  . SER   A 1 324 ? 19.02   -22.788 -9.623  1 49.63 ? 309 SER   A CB  1 
ATOM   2445 O  OG  . SER   A 1 324 ? 18.202  -21.821 -8.993  1 53.19 ? 309 SER   A OG  1 
ATOM   2446 N  N   . LEU   A 1 325 ? 21.171  -24.02  -11.655 1 46.95 ? 310 LEU   A N   1 
ATOM   2447 C  CA  . LEU   A 1 325 ? 22.23   -24.987 -11.958 1 46.06 ? 310 LEU   A CA  1 
ATOM   2448 C  C   . LEU   A 1 325 ? 23.495  -24.237 -12.365 1 46.23 ? 310 LEU   A C   1 
ATOM   2449 O  O   . LEU   A 1 325 ? 24.576  -24.614 -11.925 1 46.4  ? 310 LEU   A O   1 
ATOM   2450 C  CB  . LEU   A 1 325 ? 21.828  -25.944 -13.084 1 45.09 ? 310 LEU   A CB  1 
ATOM   2451 C  CG  . LEU   A 1 325 ? 20.902  -27.105 -12.754 1 44.49 ? 310 LEU   A CG  1 
ATOM   2452 C  CD1 . LEU   A 1 325 ? 20.696  -27.94  -13.968 1 44.34 ? 310 LEU   A CD1 1 
ATOM   2453 C  CD2 . LEU   A 1 325 ? 21.451  -27.956 -11.646 1 44.28 ? 310 LEU   A CD2 1 
ATOM   2454 N  N   . GLU   A 1 326 ? 23.361  -23.149 -13.15  1 46.02 ? 311 GLU   A N   1 
ATOM   2455 C  CA  . GLU   A 1 326 ? 24.501  -22.321 -13.578 1 46.92 ? 311 GLU   A CA  1 
ATOM   2456 C  C   . GLU   A 1 326 ? 25.19   -21.61  -12.408 1 47.44 ? 311 GLU   A C   1 
ATOM   2457 O  O   . GLU   A 1 326 ? 26.399  -21.375 -12.446 1 47.81 ? 311 GLU   A O   1 
ATOM   2458 C  CB  . GLU   A 1 326 ? 24.052  -21.273 -14.604 1 48.73 ? 311 GLU   A CB  1 
ATOM   2459 C  CG  . GLU   A 1 326 ? 24.23   -21.704 -16.042 1 52.11 ? 311 GLU   A CG  1 
ATOM   2460 C  CD  . GLU   A 1 326 ? 23.298  -21.035 -17.034 1 56.52 ? 311 GLU   A CD  1 
ATOM   2461 O  OE1 . GLU   A 1 326 ? 22.398  -20.281 -16.602 1 56.93 ? 311 GLU   A OE1 1 
ATOM   2462 O  OE2 . GLU   A 1 326 ? 23.465  -21.27  -18.251 1 58.22 ? 311 GLU   A OE2 1 
ATOM   2463 N  N   . SER   A 1 327 ? 24.408  -21.252 -11.379 1 47.23 ? 312 SER   A N   1 
ATOM   2464 C  CA  . SER   A 1 327 ? 24.872  -20.587 -10.154 1 46.89 ? 312 SER   A CA  1 
ATOM   2465 C  C   . SER   A 1 327 ? 25.683  -21.524 -9.228  1 45.74 ? 312 SER   A C   1 
ATOM   2466 O  O   . SER   A 1 327 ? 26.456  -21.06  -8.375  1 45.14 ? 312 SER   A O   1 
ATOM   2467 C  CB  . SER   A 1 327 ? 23.678  -19.997 -9.406  1 48.64 ? 312 SER   A CB  1 
ATOM   2468 O  OG  . SER   A 1 327 ? 22.966  -19.072 -10.212 1 51.86 ? 312 SER   A OG  1 
ATOM   2469 N  N   . ASN   A 1 328 ? 25.491  -22.844 -9.395  1 45.13 ? 313 ASN   A N   1 
ATOM   2470 C  CA  . ASN   A 1 328 ? 26.162  -23.873 -8.619  1 44.66 ? 313 ASN   A CA  1 
ATOM   2471 C  C   . ASN   A 1 328 ? 27.58   -24.13  -9.138  1 44.39 ? 313 ASN   A C   1 
ATOM   2472 O  O   . ASN   A 1 328 ? 27.895  -23.789 -10.286 1 44.5  ? 313 ASN   A O   1 
ATOM   2473 C  CB  . ASN   A 1 328 ? 25.328  -25.151 -8.614  1 45.03 ? 313 ASN   A CB  1 
ATOM   2474 C  CG  . ASN   A 1 328 ? 24.247  -25.136 -7.575  1 46.76 ? 313 ASN   A CG  1 
ATOM   2475 O  OD1 . ASN   A 1 328 ? 23.215  -24.498 -7.762  1 49.18 ? 313 ASN   A OD1 1 
ATOM   2476 N  ND2 . ASN   A 1 328 ? 24.438  -25.839 -6.477  1 44.84 ? 313 ASN   A ND2 1 
ATOM   2477 N  N   . PRO   A 1 329 ? 28.465  -24.694 -8.287  1 43.79 ? 314 PRO   A N   1 
ATOM   2478 C  CA  . PRO   A 1 329 ? 29.836  -24.97  -8.741  1 43.84 ? 314 PRO   A CA  1 
ATOM   2479 C  C   . PRO   A 1 329 ? 29.896  -25.893 -9.954  1 43.48 ? 314 PRO   A C   1 
ATOM   2480 O  O   . PRO   A 1 329 ? 29.026  -26.733 -10.164 1 42.68 ? 314 PRO   A O   1 
ATOM   2481 C  CB  . PRO   A 1 329 ? 30.508  -25.617 -7.515  1 44.46 ? 314 PRO   A CB  1 
ATOM   2482 C  CG  . PRO   A 1 329 ? 29.667  -25.225 -6.357  1 44.74 ? 314 PRO   A CG  1 
ATOM   2483 C  CD  . PRO   A 1 329 ? 28.26   -25.125 -6.889  1 43.22 ? 314 PRO   A CD  1 
ATOM   2484 N  N   . SER   A 1 330 ? 30.943  -25.724 -10.751 1 43.6  ? 315 SER   A N   1 
ATOM   2485 C  CA  . SER   A 1 330 ? 31.152  -26.504 -11.952 1 43.91 ? 315 SER   A CA  1 
ATOM   2486 C  C   . SER   A 1 330 ? 31.611  -27.942 -11.673 1 43.97 ? 315 SER   A C   1 
ATOM   2487 O  O   . SER   A 1 330 ? 32.655  -28.158 -11.059 1 44.77 ? 315 SER   A O   1 
ATOM   2488 C  CB  . SER   A 1 330 ? 32.141  -25.79  -12.868 1 45.67 ? 315 SER   A CB  1 
ATOM   2489 O  OG  . SER   A 1 330 ? 32.456  -26.549 -14.025 1 49.11 ? 315 SER   A OG  1 
ATOM   2490 N  N   . VAL   A 1 331 ? 30.828  -28.92  -12.147 1 43.17 ? 316 VAL   A N   1 
ATOM   2491 C  CA  . VAL   A 1 331 ? 31.145  -30.349 -12.083 1 42.83 ? 316 VAL   A CA  1 
ATOM   2492 C  C   . VAL   A 1 331 ? 32.356  -30.609 -12.986 1 42.82 ? 316 VAL   A C   1 
ATOM   2493 O  O   . VAL   A 1 331 ? 33.266  -31.329 -12.599 1 42.69 ? 316 VAL   A O   1 
ATOM   2494 C  CB  . VAL   A 1 331 ? 29.922  -31.183 -12.541 1 43.24 ? 316 VAL   A CB  1 
ATOM   2495 C  CG1 . VAL   A 1 331 ? 30.242  -32.667 -12.593 1 43.45 ? 316 VAL   A CG1 1 
ATOM   2496 C  CG2 . VAL   A 1 331 ? 28.73   -30.918 -11.636 1 43.9  ? 316 VAL   A CG2 1 
ATOM   2497 N  N   . ARG   A 1 332 ? 32.398  -29.965 -14.173 1 42.67 ? 317 ARG   A N   1 
ATOM   2498 C  CA  . ARG   A 1 332 ? 33.52   -30.093 -15.085 1 42.49 ? 317 ARG   A CA  1 
ATOM   2499 C  C   . ARG   A 1 332 ? 34.812  -29.608 -14.439 1 43.77 ? 317 ARG   A C   1 
ATOM   2500 O  O   . ARG   A 1 332 ? 35.798  -30.327 -14.497 1 44.16 ? 317 ARG   A O   1 
ATOM   2501 C  CB  . ARG   A 1 332 ? 33.276  -29.31  -16.382 1 41.9  ? 317 ARG   A CB  1 
ATOM   2502 C  CG  . ARG   A 1 332 ? 34.42   -29.486 -17.376 1 41.59 ? 317 ARG   A CG  1 
ATOM   2503 C  CD  . ARG   A 1 332 ? 34.205  -28.654 -18.609 1 40.92 ? 317 ARG   A CD  1 
ATOM   2504 N  NE  . ARG   A 1 332 ? 35.367  -28.674 -19.488 1 41.35 ? 317 ARG   A NE  1 
ATOM   2505 C  CZ  . ARG   A 1 332 ? 35.609  -29.623 -20.381 1 42.03 ? 317 ARG   A CZ  1 
ATOM   2506 N  NH1 . ARG   A 1 332 ? 36.696  -29.571 -21.132 1 41.49 ? 317 ARG   A NH1 1 
ATOM   2507 N  NH2 . ARG   A 1 332 ? 34.778  -30.645 -20.512 1 41.77 ? 317 ARG   A NH2 1 
ATOM   2508 N  N   . GLU   A 1 333 ? 34.823  -28.391 -13.842 1 44.05 ? 318 GLU   A N   1 
ATOM   2509 C  CA  . GLU   A 1 333 ? 36.029  -27.855 -13.216 1 44.44 ? 318 GLU   A CA  1 
ATOM   2510 C  C   . GLU   A 1 333 ? 36.458  -28.737 -12.062 1 45.19 ? 318 GLU   A C   1 
ATOM   2511 O  O   . GLU   A 1 333 ? 37.658  -28.948 -11.883 1 45.91 ? 318 GLU   A O   1 
ATOM   2512 C  CB  . GLU   A 1 333 ? 35.838  -26.399 -12.746 1 46.31 ? 318 GLU   A CB  1 
ATOM   2513 N  N   . PHE   A 1 334 ? 35.49   -29.294 -11.306 1 44.75 ? 319 PHE   A N   1 
ATOM   2514 C  CA  . PHE   A 1 334 ? 35.804  -30.181 -10.204 1 45.03 ? 319 PHE   A CA  1 
ATOM   2515 C  C   . PHE   A 1 334 ? 36.502  -31.437 -10.705 1 46.42 ? 319 PHE   A C   1 
ATOM   2516 O  O   . PHE   A 1 334 ? 37.535  -31.788 -10.158 1 47.13 ? 319 PHE   A O   1 
ATOM   2517 C  CB  . PHE   A 1 334 ? 34.543  -30.544 -9.416  1 44.33 ? 319 PHE   A CB  1 
ATOM   2518 C  CG  . PHE   A 1 334 ? 34.772  -31.332 -8.147  1 44.84 ? 319 PHE   A CG  1 
ATOM   2519 C  CD1 . PHE   A 1 334 ? 34.937  -32.707 -8.182  1 45.59 ? 319 PHE   A CD1 1 
ATOM   2520 C  CD2 . PHE   A 1 334 ? 34.746  -30.711 -6.916  1 45.77 ? 319 PHE   A CD2 1 
ATOM   2521 C  CE1 . PHE   A 1 334 ? 35.123  -33.431 -7.013  1 46.17 ? 319 PHE   A CE1 1 
ATOM   2522 C  CE2 . PHE   A 1 334 ? 34.908  -31.446 -5.744  1 46.57 ? 319 PHE   A CE2 1 
ATOM   2523 C  CZ  . PHE   A 1 334 ? 35.082  -32.803 -5.801  1 46.12 ? 319 PHE   A CZ  1 
ATOM   2524 N  N   . VAL   A 1 335 ? 35.961  -32.098 -11.738 1 46.6  ? 320 VAL   A N   1 
ATOM   2525 C  CA  . VAL   A 1 335 ? 36.521  -33.338 -12.275 1 47.41 ? 320 VAL   A CA  1 
ATOM   2526 C  C   . VAL   A 1 335 ? 37.882  -33.123 -12.961 1 48.68 ? 320 VAL   A C   1 
ATOM   2527 O  O   . VAL   A 1 335 ? 38.798  -33.949 -12.846 1 48.4  ? 320 VAL   A O   1 
ATOM   2528 C  CB  . VAL   A 1 335 ? 35.483  -34.022 -13.194 1 48.2  ? 320 VAL   A CB  1 
ATOM   2529 C  CG1 . VAL   A 1 335 ? 36.109  -35.16  -13.991 1 48.8  ? 320 VAL   A CG1 1 
ATOM   2530 C  CG2 . VAL   A 1 335 ? 34.291  -34.528 -12.378 1 48.56 ? 320 VAL   A CG2 1 
ATOM   2531 N  N   . LEU   A 1 336 ? 38.02   -31.991 -13.652 1 49.66 ? 321 LEU   A N   1 
ATOM   2532 C  CA  . LEU   A 1 336 ? 39.255  -31.624 -14.335 1 50.86 ? 321 LEU   A CA  1 
ATOM   2533 C  C   . LEU   A 1 336 ? 40.404  -31.408 -13.342 1 51.7  ? 321 LEU   A C   1 
ATOM   2534 O  O   . LEU   A 1 336 ? 41.565  -31.664 -13.672 1 52.16 ? 321 LEU   A O   1 
ATOM   2535 C  CB  . LEU   A 1 336 ? 39.034  -30.317 -15.104 1 51.38 ? 321 LEU   A CB  1 
ATOM   2536 C  CG  . LEU   A 1 336 ? 38.938  -30.417 -16.622 1 53.34 ? 321 LEU   A CG  1 
ATOM   2537 C  CD1 . LEU   A 1 336 ? 38.521  -29.093 -17.222 1 53.97 ? 321 LEU   A CD1 1 
ATOM   2538 C  CD2 . LEU   A 1 336 ? 40.222  -30.887 -17.224 1 54.16 ? 321 LEU   A CD2 1 
ATOM   2539 N  N   . SER   A 1 337 ? 40.092  -30.912 -12.141 1 51.71 ? 322 SER   A N   1 
ATOM   2540 C  CA  . SER   A 1 337 ? 41.12   -30.58  -11.161 1 52.31 ? 322 SER   A CA  1 
ATOM   2541 C  C   . SER   A 1 337 ? 41.579  -31.722 -10.262 1 53.25 ? 322 SER   A C   1 
ATOM   2542 O  O   . SER   A 1 337 ? 42.482  -31.499 -9.456  1 53.85 ? 322 SER   A O   1 
ATOM   2543 C  CB  . SER   A 1 337 ? 40.638  -29.432 -10.282 1 52.75 ? 322 SER   A CB  1 
ATOM   2544 O  OG  . SER   A 1 337 ? 39.614  -29.871 -9.402  1 55.09 ? 322 SER   A OG  1 
ATOM   2545 N  N   . LYS   A 1 338 ? 40.945  -32.902 -10.336 1 53.17 ? 323 LYS   A N   1 
ATOM   2546 C  CA  . LYS   A 1 338 ? 41.235  -33.963 -9.38   1 53.41 ? 323 LYS   A CA  1 
ATOM   2547 C  C   . LYS   A 1 338 ? 42.304  -34.986 -9.769  1 53.15 ? 323 LYS   A C   1 
ATOM   2548 O  O   . LYS   A 1 338 ? 42.769  -35.699 -8.858  1 54.36 ? 323 LYS   A O   1 
ATOM   2549 C  CB  . LYS   A 1 338 ? 39.962  -34.714 -8.969  1 54.98 ? 323 LYS   A CB  1 
ATOM   2550 C  CG  . LYS   A 1 338 ? 38.911  -33.86  -8.261  1 59.07 ? 323 LYS   A CG  1 
ATOM   2551 C  CD  . LYS   A 1 338 ? 39.387  -33.139 -7.016  1 63.74 ? 323 LYS   A CD  1 
ATOM   2552 C  CE  . LYS   A 1 338 ? 38.553  -31.91  -6.785  1 68.19 ? 323 LYS   A CE  1 
ATOM   2553 N  NZ  . LYS   A 1 338 ? 39.178  -30.98  -5.813  1 72.09 ? 323 LYS   A NZ  1 
ATOM   2554 N  N   . GLY   A 1 339 ? 42.701  -35.078 -11.043 1 51.01 ? 324 GLY   A N   1 
ATOM   2555 C  CA  . GLY   A 1 339 ? 43.723  -36.058 -11.447 1 49.43 ? 324 GLY   A CA  1 
ATOM   2556 C  C   . GLY   A 1 339 ? 43.332  -37.49  -11.102 1 47.71 ? 324 GLY   A C   1 
ATOM   2557 O  O   . GLY   A 1 339 ? 44.12   -38.256 -10.53  1 47.63 ? 324 GLY   A O   1 
ATOM   2558 N  N   . ASP   A 1 340 ? 42.049  -37.806 -11.358 1 45.79 ? 325 ASP   A N   1 
ATOM   2559 C  CA  . ASP   A 1 340 ? 41.395  -39.058 -11.026 1 44.47 ? 325 ASP   A CA  1 
ATOM   2560 C  C   . ASP   A 1 340 ? 40.788  -39.607 -12.301 1 44.27 ? 325 ASP   A C   1 
ATOM   2561 O  O   . ASP   A 1 340 ? 39.8    -39.051 -12.776 1 44.71 ? 325 ASP   A O   1 
ATOM   2562 C  CB  . ASP   A 1 340 ? 40.282  -38.748 -10.008 1 44.44 ? 325 ASP   A CB  1 
ATOM   2563 C  CG  . ASP   A 1 340 ? 39.573  -39.927 -9.385  1 46.66 ? 325 ASP   A CG  1 
ATOM   2564 O  OD1 . ASP   A 1 340 ? 39.396  -40.946 -10.072 1 47.16 ? 325 ASP   A OD1 1 
ATOM   2565 O  OD2 . ASP   A 1 340 ? 39.162  -39.815 -8.219  1 48.96 ? 325 ASP   A OD2 1 
ATOM   2566 N  N   . ALA   A 1 341 ? 41.364  -40.701 -12.837 1 43.11 ? 326 ALA   A N   1 
ATOM   2567 C  CA  . ALA   A 1 341 ? 40.938  -41.347 -14.063 1 42.87 ? 326 ALA   A CA  1 
ATOM   2568 C  C   . ALA   A 1 341 ? 39.507  -41.89  -13.987 1 42.87 ? 326 ALA   A C   1 
ATOM   2569 O  O   . ALA   A 1 341 ? 38.736  -41.673 -14.905 1 43.26 ? 326 ALA   A O   1 
ATOM   2570 C  CB  . ALA   A 1 341 ? 41.91   -42.457 -14.432 1 42.48 ? 326 ALA   A CB  1 
ATOM   2571 N  N   . GLY   A 1 342 ? 39.155  -42.555 -12.889 1 42.35 ? 327 GLY   A N   1 
ATOM   2572 C  CA  . GLY   A 1 342 ? 37.819  -43.098 -12.701 1 42.34 ? 327 GLY   A CA  1 
ATOM   2573 C  C   . GLY   A 1 342 ? 36.722  -42.042 -12.747 1 42.32 ? 327 GLY   A C   1 
ATOM   2574 O  O   . GLY   A 1 342 ? 35.67   -42.267 -13.336 1 42.03 ? 327 GLY   A O   1 
ATOM   2575 N  N   . LEU   A 1 343 ? 36.97   -40.881 -12.134 1 42.25 ? 328 LEU   A N   1 
ATOM   2576 C  CA  . LEU   A 1 343 ? 36.048  -39.751 -12.104 1 42.59 ? 328 LEU   A CA  1 
ATOM   2577 C  C   . LEU   A 1 343 ? 35.937  -39.094 -13.481 1 42.87 ? 328 LEU   A C   1 
ATOM   2578 O  O   . LEU   A 1 343 ? 34.829  -38.771 -13.917 1 43.17 ? 328 LEU   A O   1 
ATOM   2579 C  CB  . LEU   A 1 343 ? 36.565  -38.741 -11.089 1 43.05 ? 328 LEU   A CB  1 
ATOM   2580 C  CG  . LEU   A 1 343 ? 35.566  -37.891 -10.344 1 44.59 ? 328 LEU   A CG  1 
ATOM   2581 C  CD1 . LEU   A 1 343 ? 34.438  -38.742 -9.74   1 44.86 ? 328 LEU   A CD1 1 
ATOM   2582 C  CD2 . LEU   A 1 343 ? 36.296  -37.086 -9.271  1 45.08 ? 328 LEU   A CD2 1 
ATOM   2583 N  N   . ARG   A 1 344 ? 37.075  -38.925 -14.179 1 42.47 ? 329 ARG   A N   1 
ATOM   2584 C  CA  . ARG   A 1 344 ? 37.106  -38.373 -15.526 1 42.83 ? 329 ARG   A CA  1 
ATOM   2585 C  C   . ARG   A 1 344 ? 36.341  -39.27  -16.487 1 42.95 ? 329 ARG   A C   1 
ATOM   2586 O  O   . ARG   A 1 344 ? 35.664  -38.77  -17.377 1 43.48 ? 329 ARG   A O   1 
ATOM   2587 C  CB  . ARG   A 1 344 ? 38.556  -38.191 -16.018 1 44.21 ? 329 ARG   A CB  1 
ATOM   2588 C  CG  . ARG   A 1 344 ? 39.262  -36.992 -15.402 1 49.27 ? 329 ARG   A CG  1 
ATOM   2589 C  CD  . ARG   A 1 344 ? 40.46   -36.482 -16.192 1 55.76 ? 329 ARG   A CD  1 
ATOM   2590 N  NE  . ARG   A 1 344 ? 41.416  -37.542 -16.521 1 62.63 ? 329 ARG   A NE  1 
ATOM   2591 C  CZ  . ARG   A 1 344 ? 42.408  -37.936 -15.726 1 68.02 ? 329 ARG   A CZ  1 
ATOM   2592 N  NH1 . ARG   A 1 344 ? 42.586  -37.363 -14.543 1 69.13 ? 329 ARG   A NH1 1 
ATOM   2593 N  NH2 . ARG   A 1 344 ? 43.229  -38.907 -16.109 1 68.54 ? 329 ARG   A NH2 1 
ATOM   2594 N  N   . GLU   A 1 345 ? 36.451  -40.588 -16.314 1 42.55 ? 330 GLU   A N   1 
ATOM   2595 C  CA  . GLU   A 1 345 ? 35.763  -41.534 -17.171 1 42.74 ? 330 GLU   A CA  1 
ATOM   2596 C  C   . GLU   A 1 345 ? 34.262  -41.563 -16.928 1 41.59 ? 330 GLU   A C   1 
ATOM   2597 O  O   . GLU   A 1 345 ? 33.509  -41.742 -17.88  1 41.82 ? 330 GLU   A O   1 
ATOM   2598 C  CB  . GLU   A 1 345 ? 36.395  -42.93  -17.105 1 46.5  ? 330 GLU   A CB  1 
ATOM   2599 C  CG  . GLU   A 1 345 ? 37.697  -43.017 -17.908 1 56.47 ? 330 GLU   A CG  1 
ATOM   2600 C  CD  . GLU   A 1 345 ? 37.744  -42.27  -19.239 1 68.4  ? 330 GLU   A CD  1 
ATOM   2601 O  OE1 . GLU   A 1 345 ? 37.144  -42.767 -20.222 1 69.94 ? 330 GLU   A OE1 1 
ATOM   2602 O  OE2 . GLU   A 1 345 ? 38.34   -41.164 -19.284 1 72.71 ? 330 GLU   A OE2 1 
ATOM   2603 N  N   . ALA   A 1 346 ? 33.828  -41.333 -15.685 1 40.07 ? 331 ALA   A N   1 
ATOM   2604 C  CA  . ALA   A 1 346 ? 32.418  -41.266 -15.351 1 39.53 ? 331 ALA   A CA  1 
ATOM   2605 C  C   . ALA   A 1 346 ? 31.818  -39.98  -15.954 1 39.57 ? 331 ALA   A C   1 
ATOM   2606 O  O   . ALA   A 1 346 ? 30.716  -40.028 -16.475 1 40.33 ? 331 ALA   A O   1 
ATOM   2607 C  CB  . ALA   A 1 346 ? 32.24   -41.281 -13.845 1 39.05 ? 331 ALA   A CB  1 
ATOM   2608 N  N   . TYR   A 1 347 ? 32.554  -38.854 -15.913 1 38.67 ? 332 TYR   A N   1 
ATOM   2609 C  CA  . TYR   A 1 347 ? 32.134  -37.576 -16.492 1 38.19 ? 332 TYR   A CA  1 
ATOM   2610 C  C   . TYR   A 1 347 ? 32.021  -37.746 -18.009 1 38.87 ? 332 TYR   A C   1 
ATOM   2611 O  O   . TYR   A 1 347 ? 31.06   -37.277 -18.603 1 38.72 ? 332 TYR   A O   1 
ATOM   2612 C  CB  . TYR   A 1 347 ? 33.177  -36.485 -16.172 1 37.31 ? 332 TYR   A CB  1 
ATOM   2613 C  CG  . TYR   A 1 347 ? 32.957  -35.184 -16.908 1 37.31 ? 332 TYR   A CG  1 
ATOM   2614 C  CD1 . TYR   A 1 347 ? 32.097  -34.218 -16.407 1 38.2  ? 332 TYR   A CD1 1 
ATOM   2615 C  CD2 . TYR   A 1 347 ? 33.577  -34.936 -18.128 1 37.54 ? 332 TYR   A CD2 1 
ATOM   2616 C  CE1 . TYR   A 1 347 ? 31.861  -33.039 -17.097 1 39.03 ? 332 TYR   A CE1 1 
ATOM   2617 C  CE2 . TYR   A 1 347 ? 33.36   -33.753 -18.819 1 38.2  ? 332 TYR   A CE2 1 
ATOM   2618 C  CZ  . TYR   A 1 347 ? 32.488  -32.813 -18.308 1 39.66 ? 332 TYR   A CZ  1 
ATOM   2619 O  OH  . TYR   A 1 347 ? 32.263  -31.629 -18.976 1 41.61 ? 332 TYR   A OH  1 
ATOM   2620 N  N   . ASP   A 1 348 ? 33.032  -38.385 -18.636 1 39.14 ? 333 ASP   A N   1 
ATOM   2621 C  CA  . ASP   A 1 348 ? 33.058  -38.618 -20.079 1 39.3  ? 333 ASP   A CA  1 
ATOM   2622 C  C   . ASP   A 1 348 ? 31.944  -39.526 -20.548 1 39.78 ? 333 ASP   A C   1 
ATOM   2623 O  O   . ASP   A 1 348 ? 31.483  -39.373 -21.674 1 41.1  ? 333 ASP   A O   1 
ATOM   2624 C  CB  . ASP   A 1 348 ? 34.405  -39.178 -20.534 1 39.71 ? 333 ASP   A CB  1 
ATOM   2625 C  CG  . ASP   A 1 348 ? 35.441  -38.132 -20.861 1 43.2  ? 333 ASP   A CG  1 
ATOM   2626 O  OD1 . ASP   A 1 348 ? 35.163  -36.931 -20.656 1 43.34 ? 333 ASP   A OD1 1 
ATOM   2627 O  OD2 . ASP   A 1 348 ? 36.538  -38.511 -21.317 1 45.37 ? 333 ASP   A OD2 1 
ATOM   2628 N  N   . ALA   A 1 349 ? 31.502  -40.456 -19.71  1 38.56 ? 334 ALA   A N   1 
ATOM   2629 C  CA  . ALA   A 1 349 ? 30.394  -41.336 -20.053 1 38.09 ? 334 ALA   A CA  1 
ATOM   2630 C  C   . ALA   A 1 349 ? 29.098  -40.501 -20.192 1 38.38 ? 334 ALA   A C   1 
ATOM   2631 O  O   . ALA   A 1 349 ? 28.307  -40.753 -21.1   1 38.38 ? 334 ALA   A O   1 
ATOM   2632 C  CB  . ALA   A 1 349 ? 30.232  -42.403 -18.991 1 37.37 ? 334 ALA   A CB  1 
ATOM   2633 N  N   . CYS   A 1 350 ? 28.924  -39.469 -19.336 1 37.89 ? 335 CYS   A N   1 
ATOM   2634 C  CA  . CYS   A 1 350 ? 27.784  -38.566 -19.396 1 37.7  ? 335 CYS   A CA  1 
ATOM   2635 C  C   . CYS   A 1 350 ? 27.814  -37.744 -20.691 1 37.18 ? 335 CYS   A C   1 
ATOM   2636 O  O   . CYS   A 1 350 ? 26.804  -37.653 -21.371 1 36.64 ? 335 CYS   A O   1 
ATOM   2637 C  CB  . CYS   A 1 350 ? 27.767  -37.656 -18.174 1 38.09 ? 335 CYS   A CB  1 
ATOM   2638 S  SG  . CYS   A 1 350 ? 27.402  -38.508 -16.63  1 39.41 ? 335 CYS   A SG  1 
ATOM   2639 N  N   . VAL   A 1 351 ? 28.971  -37.147 -21.018 1 37.16 ? 336 VAL   A N   1 
ATOM   2640 C  CA  . VAL   A 1 351 ? 29.155  -36.328 -22.208 1 37.75 ? 336 VAL   A CA  1 
ATOM   2641 C  C   . VAL   A 1 351 ? 29.001  -37.19  -23.474 1 39.32 ? 336 VAL   A C   1 
ATOM   2642 O  O   . VAL   A 1 351 ? 28.253  -36.8   -24.373 1 40.57 ? 336 VAL   A O   1 
ATOM   2643 C  CB  . VAL   A 1 351 ? 30.511  -35.583 -22.156 1 38.06 ? 336 VAL   A CB  1 
ATOM   2644 C  CG1 . VAL   A 1 351 ? 30.756  -34.774 -23.421 1 38.51 ? 336 VAL   A CG1 1 
ATOM   2645 C  CG2 . VAL   A 1 351 ? 30.601  -34.685 -20.934 1 38.01 ? 336 VAL   A CG2 1 
ATOM   2646 N  N   . LYS   A 1 352 ? 29.608  -38.394 -23.501 1 38.91 ? 337 LYS   A N   1 
ATOM   2647 C  CA  . LYS   A 1 352 ? 29.499  -39.329 -24.619 1 39.5  ? 337 LYS   A CA  1 
ATOM   2648 C  C   . LYS   A 1 352 ? 28.058  -39.757 -24.846 1 39.87 ? 337 LYS   A C   1 
ATOM   2649 O  O   . LYS   A 1 352 ? 27.659  -39.928 -25.993 1 40.59 ? 337 LYS   A O   1 
ATOM   2650 C  CB  . LYS   A 1 352 ? 30.387  -40.574 -24.432 1 41.27 ? 337 LYS   A CB  1 
ATOM   2651 N  N   . ALA   A 1 353 ? 27.262  -39.894 -23.78  1 39.23 ? 338 ALA   A N   1 
ATOM   2652 C  CA  . ALA   A 1 353 ? 25.85   -40.256 -23.913 1 38.63 ? 338 ALA   A CA  1 
ATOM   2653 C  C   . ALA   A 1 353 ? 25.056  -39.143 -24.614 1 38.35 ? 338 ALA   A C   1 
ATOM   2654 O  O   . ALA   A 1 353 ? 24.182  -39.443 -25.42  1 38.81 ? 338 ALA   A O   1 
ATOM   2655 C  CB  . ALA   A 1 353 ? 25.251  -40.573 -22.554 1 37.88 ? 338 ALA   A CB  1 
ATOM   2656 N  N   . LEU   A 1 354 ? 25.381  -37.878 -24.334 1 37.58 ? 339 LEU   A N   1 
ATOM   2657 C  CA  . LEU   A 1 354 ? 24.757  -36.716 -24.977 1 37.78 ? 339 LEU   A CA  1 
ATOM   2658 C  C   . LEU   A 1 354 ? 25.219  -36.614 -26.445 1 37.19 ? 339 LEU   A C   1 
ATOM   2659 O  O   . LEU   A 1 354 ? 24.423  -36.284 -27.322 1 37.51 ? 339 LEU   A O   1 
ATOM   2660 C  CB  . LEU   A 1 354 ? 25.139  -35.436 -24.231 1 38.51 ? 339 LEU   A CB  1 
ATOM   2661 C  CG  . LEU   A 1 354 ? 24.318  -35.038 -23.01  1 40.33 ? 339 LEU   A CG  1 
ATOM   2662 C  CD1 . LEU   A 1 354 ? 24.909  -33.815 -22.348 1 40.89 ? 339 LEU   A CD1 1 
ATOM   2663 C  CD2 . LEU   A 1 354 ? 22.852  -34.784 -23.367 1 41.11 ? 339 LEU   A CD2 1 
ATOM   2664 N  N   . VAL   A 1 355 ? 26.502  -36.896 -26.719 1 36.65 ? 340 VAL   A N   1 
ATOM   2665 C  CA  . VAL   A 1 355 ? 27.025  -36.917 -28.101 1 36.32 ? 340 VAL   A CA  1 
ATOM   2666 C  C   . VAL   A 1 355 ? 26.309  -38.009 -28.917 1 37.1  ? 340 VAL   A C   1 
ATOM   2667 O  O   . VAL   A 1 355 ? 25.931  -37.762 -30.052 1 37.47 ? 340 VAL   A O   1 
ATOM   2668 C  CB  . VAL   A 1 355 ? 28.55   -37.14  -28.134 1 35.74 ? 340 VAL   A CB  1 
ATOM   2669 C  CG1 . VAL   A 1 355 ? 29.06   -37.298 -29.563 1 35.01 ? 340 VAL   A CG1 1 
ATOM   2670 C  CG2 . VAL   A 1 355 ? 29.272  -36.004 -27.423 1 36.41 ? 340 VAL   A CG2 1 
ATOM   2671 N  N   . SER   A 1 356 ? 26.087  -39.192 -28.329 1 37.19 ? 341 SER   A N   1 
ATOM   2672 C  CA  . SER   A 1 356 ? 25.401  -40.272 -29.032 1 38.2  ? 341 SER   A CA  1 
ATOM   2673 C  C   . SER   A 1 356 ? 23.943  -39.905 -29.345 1 39.38 ? 341 SER   A C   1 
ATOM   2674 O  O   . SER   A 1 356 ? 23.475  -40.177 -30.461 1 39.92 ? 341 SER   A O   1 
ATOM   2675 C  CB  . SER   A 1 356 ? 25.48   -41.561 -28.229 1 39.73 ? 341 SER   A CB  1 
ATOM   2676 O  OG  . SER   A 1 356 ? 26.848  -41.919 -28.11  1 43.52 ? 341 SER   A OG  1 
ATOM   2677 N  N   . LEU   A 1 357 ? 23.242  -39.25  -28.38  1 38.71 ? 342 LEU   A N   1 
ATOM   2678 C  CA  . LEU   A 1 357 ? 21.875  -38.792 -28.569 1 38.91 ? 342 LEU   A CA  1 
ATOM   2679 C  C   . LEU   A 1 357 ? 21.823  -37.795 -29.735 1 37.97 ? 342 LEU   A C   1 
ATOM   2680 O  O   . LEU   A 1 357 ? 20.994  -37.957 -30.621 1 38.27 ? 342 LEU   A O   1 
ATOM   2681 C  CB  . LEU   A 1 357 ? 21.33   -38.116 -27.292 1 40.35 ? 342 LEU   A CB  1 
ATOM   2682 C  CG  . LEU   A 1 357 ? 20.961  -39.047 -26.13  1 43.65 ? 342 LEU   A CG  1 
ATOM   2683 C  CD1 . LEU   A 1 357 ? 20.76   -38.272 -24.825 1 44.8  ? 342 LEU   A CD1 1 
ATOM   2684 C  CD2 . LEU   A 1 357 ? 19.706  -39.798 -26.425 1 44.81 ? 342 LEU   A CD2 1 
ATOM   2685 N  N   . ARG   A 1 358 ? 22.736  -36.807 -29.763 1 36.63 ? 343 ARG   A N   1 
ATOM   2686 C  CA  . ARG   A 1 358 ? 22.755  -35.778 -30.805 1 36.46 ? 343 ARG   A CA  1 
ATOM   2687 C  C   . ARG   A 1 358 ? 23.167  -36.297 -32.158 1 37.11 ? 343 ARG   A C   1 
ATOM   2688 O  O   . ARG   A 1 358 ? 22.678  -35.792 -33.17  1 38.21 ? 343 ARG   A O   1 
ATOM   2689 C  CB  . ARG   A 1 358 ? 23.609  -34.576 -30.385 1 36.62 ? 343 ARG   A CB  1 
ATOM   2690 C  CG  . ARG   A 1 358 ? 22.967  -33.896 -29.182 1 37.73 ? 343 ARG   A CG  1 
ATOM   2691 C  CD  . ARG   A 1 358 ? 23.759  -32.756 -28.608 1 37.69 ? 343 ARG   A CD  1 
ATOM   2692 N  NE  . ARG   A 1 358 ? 22.851  -31.91  -27.85  1 38.8  ? 343 ARG   A NE  1 
ATOM   2693 C  CZ  . ARG   A 1 358 ? 23.06   -31.475 -26.617 1 39.99 ? 343 ARG   A CZ  1 
ATOM   2694 N  NH1 . ARG   A 1 358 ? 24.189  -31.769 -25.986 1 38.68 ? 343 ARG   A NH1 1 
ATOM   2695 N  NH2 . ARG   A 1 358 ? 22.15   -30.723 -26.01  1 38.96 ? 343 ARG   A NH2 1 
ATOM   2696 N  N   . SER   A 1 359 ? 24.042  -37.303 -32.191 1 36.27 ? 344 SER   A N   1 
ATOM   2697 C  CA  . SER   A 1 359 ? 24.5    -37.914 -33.439 1 36.03 ? 344 SER   A CA  1 
ATOM   2698 C  C   . SER   A 1 359 ? 23.348  -38.721 -34.027 1 35.78 ? 344 SER   A C   1 
ATOM   2699 O  O   . SER   A 1 359 ? 23.103  -38.638 -35.222 1 35.88 ? 344 SER   A O   1 
ATOM   2700 C  CB  . SER   A 1 359 ? 25.694  -38.838 -33.183 1 37.05 ? 344 SER   A CB  1 
ATOM   2701 O  OG  . SER   A 1 359 ? 26.846  -38.116 -32.785 1 39.43 ? 344 SER   A OG  1 
ATOM   2702 N  N   . TYR   A 1 360 ? 22.613  -39.467 -33.186 1 35.57 ? 345 TYR   A N   1 
ATOM   2703 C  CA  . TYR   A 1 360 ? 21.455  -40.217 -33.648 1 36.62 ? 345 TYR   A CA  1 
ATOM   2704 C  C   . TYR   A 1 360 ? 20.371  -39.236 -34.146 1 36.5  ? 345 TYR   A C   1 
ATOM   2705 O  O   . TYR   A 1 360 ? 19.808  -39.429 -35.221 1 36.88 ? 345 TYR   A O   1 
ATOM   2706 C  CB  . TYR   A 1 360 ? 20.902  -41.076 -32.519 1 37.51 ? 345 TYR   A CB  1 
ATOM   2707 C  CG  . TYR   A 1 360 ? 19.856  -42.046 -33.009 1 39.94 ? 345 TYR   A CG  1 
ATOM   2708 C  CD1 . TYR   A 1 360 ? 20.212  -43.171 -33.739 1 41.29 ? 345 TYR   A CD1 1 
ATOM   2709 C  CD2 . TYR   A 1 360 ? 18.505  -41.822 -32.775 1 41.09 ? 345 TYR   A CD2 1 
ATOM   2710 C  CE1 . TYR   A 1 360 ? 19.252  -44.068 -34.197 1 42.21 ? 345 TYR   A CE1 1 
ATOM   2711 C  CE2 . TYR   A 1 360 ? 17.536  -42.706 -33.239 1 41.9  ? 345 TYR   A CE2 1 
ATOM   2712 C  CZ  . TYR   A 1 360 ? 17.911  -43.82  -33.966 1 42.89 ? 345 TYR   A CZ  1 
ATOM   2713 O  OH  . TYR   A 1 360 ? 16.957  -44.721 -34.407 1 44.38 ? 345 TYR   A OH  1 
ATOM   2714 N  N   . HIS   A 1 361 ? 20.129  -38.155 -33.387 1 35.21 ? 346 HIS   A N   1 
ATOM   2715 C  CA  . HIS   A 1 361 ? 19.178  -37.126 -33.741 1 35.19 ? 346 HIS   A CA  1 
ATOM   2716 C  C   . HIS   A 1 361 ? 19.547  -36.436 -35.087 1 36.15 ? 346 HIS   A C   1 
ATOM   2717 O  O   . HIS   A 1 361 ? 18.658  -36.089 -35.851 1 35.7  ? 346 HIS   A O   1 
ATOM   2718 C  CB  . HIS   A 1 361 ? 19.059  -36.128 -32.586 1 34.67 ? 346 HIS   A CB  1 
ATOM   2719 C  CG  . HIS   A 1 361 ? 18.094  -35.014 -32.827 1 34.92 ? 346 HIS   A CG  1 
ATOM   2720 N  ND1 . HIS   A 1 361 ? 18.527  -33.767 -33.269 1 36.57 ? 346 HIS   A ND1 1 
ATOM   2721 C  CD2 . HIS   A 1 361 ? 16.767  -34.958 -32.605 1 34.93 ? 346 HIS   A CD2 1 
ATOM   2722 C  CE1 . HIS   A 1 361 ? 17.453  -33.006 -33.305 1 36.31 ? 346 HIS   A CE1 1 
ATOM   2723 N  NE2 . HIS   A 1 361 ? 16.366  -33.682 -32.934 1 36.06 ? 346 HIS   A NE2 1 
ATOM   2724 N  N   . LEU   A 1 362 ? 20.847  -36.305 -35.408 1 37.28 ? 347 LEU   A N   1 
ATOM   2725 C  CA  . LEU   A 1 362 ? 21.273  -35.757 -36.703 1 38.59 ? 347 LEU   A CA  1 
ATOM   2726 C  C   . LEU   A 1 362 ? 20.869  -36.698 -37.837 1 39.2  ? 347 LEU   A C   1 
ATOM   2727 O  O   . LEU   A 1 362 ? 20.4    -36.244 -38.874 1 39    ? 347 LEU   A O   1 
ATOM   2728 C  CB  . LEU   A 1 362 ? 22.768  -35.521 -36.732 1 39.24 ? 347 LEU   A CB  1 
ATOM   2729 C  CG  . LEU   A 1 362 ? 23.213  -34.146 -36.246 1 41.25 ? 347 LEU   A CG  1 
ATOM   2730 C  CD1 . LEU   A 1 362 ? 24.688  -34.139 -35.955 1 41.66 ? 347 LEU   A CD1 1 
ATOM   2731 C  CD2 . LEU   A 1 362 ? 22.85   -33.057 -37.251 1 41.93 ? 347 LEU   A CD2 1 
ATOM   2732 N  N   . GLN   A 1 363 ? 20.998  -38.011 -37.626 1 39.52 ? 348 GLN   A N   1 
ATOM   2733 C  CA  . GLN   A 1 363 ? 20.564  -38.997 -38.623 1 39.44 ? 348 GLN   A CA  1 
ATOM   2734 C  C   . GLN   A 1 363 ? 19.047  -38.932 -38.82  1 38.55 ? 348 GLN   A C   1 
ATOM   2735 O  O   . GLN   A 1 363 ? 18.577  -39.028 -39.941 1 39.09 ? 348 GLN   A O   1 
ATOM   2736 C  CB  . GLN   A 1 363 ? 21.009  -40.405 -38.23  1 41.54 ? 348 GLN   A CB  1 
ATOM   2737 C  CG  . GLN   A 1 363 ? 22.524  -40.549 -38.229 1 48.45 ? 348 GLN   A CG  1 
ATOM   2738 C  CD  . GLN   A 1 363 ? 22.985  -41.892 -37.678 1 57.38 ? 348 GLN   A CD  1 
ATOM   2739 O  OE1 . GLN   A 1 363 ? 22.275  -42.597 -36.929 1 58.88 ? 348 GLN   A OE1 1 
ATOM   2740 N  NE2 . GLN   A 1 363 ? 24.198  -42.287 -38.052 1 59.74 ? 348 GLN   A NE2 1 
ATOM   2741 N  N   . ILE   A 1 364 ? 18.293  -38.717 -37.752 1 37.73 ? 349 ILE   A N   1 
ATOM   2742 C  CA  . ILE   A 1 364 ? 16.84   -38.554 -37.795 1 37.53 ? 349 ILE   A CA  1 
ATOM   2743 C  C   . ILE   A 1 364 ? 16.425  -37.298 -38.589 1 36.55 ? 349 ILE   A C   1 
ATOM   2744 O  O   . ILE   A 1 364 ? 15.513  -37.366 -39.416 1 36.57 ? 349 ILE   A O   1 
ATOM   2745 C  CB  . ILE   A 1 364 ? 16.29   -38.522 -36.354 1 38.72 ? 349 ILE   A CB  1 
ATOM   2746 C  CG1 . ILE   A 1 364 ? 16.402  -39.892 -35.698 1 40.2  ? 349 ILE   A CG1 1 
ATOM   2747 C  CG2 . ILE   A 1 364 ? 14.853  -38.004 -36.286 1 39.41 ? 349 ILE   A CG2 1 
ATOM   2748 C  CD1 . ILE   A 1 364 ? 15.74   -40.984 -36.428 1 42.29 ? 349 ILE   A CD1 1 
ATOM   2749 N  N   . VAL   A 1 365 ? 17.098  -36.177 -38.35  1 35.55 ? 350 VAL   A N   1 
ATOM   2750 C  CA  . VAL   A 1 365 ? 16.805  -34.947 -39.062 1 35.87 ? 350 VAL   A CA  1 
ATOM   2751 C  C   . VAL   A 1 365 ? 17.115  -35.113 -40.561 1 37    ? 350 VAL   A C   1 
ATOM   2752 O  O   . VAL   A 1 365 ? 16.362  -34.62  -41.39  1 36.4  ? 350 VAL   A O   1 
ATOM   2753 C  CB  . VAL   A 1 365 ? 17.481  -33.718 -38.398 1 36.13 ? 350 VAL   A CB  1 
ATOM   2754 C  CG1 . VAL   A 1 365 ? 17.344  -32.481 -39.272 1 36.42 ? 350 VAL   A CG1 1 
ATOM   2755 C  CG2 . VAL   A 1 365 ? 16.876  -33.459 -37.018 1 36.19 ? 350 VAL   A CG2 1 
ATOM   2756 N  N   . THR   A 1 366 ? 18.146  -35.901 -40.912 1 38.17 ? 351 THR   A N   1 
ATOM   2757 C  CA  . THR   A 1 366 ? 18.466  -36.18  -42.309 1 39.31 ? 351 THR   A CA  1 
ATOM   2758 C  C   . THR   A 1 366 ? 17.307  -36.963 -42.964 1 39.49 ? 351 THR   A C   1 
ATOM   2759 O  O   . THR   A 1 366 ? 16.85   -36.621 -44.056 1 40.3  ? 351 THR   A O   1 
ATOM   2760 C  CB  . THR   A 1 366 ? 19.792  -36.945 -42.392 1 40.99 ? 351 THR   A CB  1 
ATOM   2761 O  OG1 . THR   A 1 366 ? 20.823  -36.129 -41.824 1 42.44 ? 351 THR   A OG1 1 
ATOM   2762 C  CG2 . THR   A 1 366 ? 20.167  -37.305 -43.83  1 41.04 ? 351 THR   A CG2 1 
ATOM   2763 N  N   . LYS   A 1 367 ? 16.8    -37.976 -42.266 1 38.4  ? 352 LYS   A N   1 
ATOM   2764 C  CA  . LYS   A 1 367 ? 15.712  -38.806 -42.755 1 37.66 ? 352 LYS   A CA  1 
ATOM   2765 C  C   . LYS   A 1 367 ? 14.369  -38.045 -42.896 1 38.59 ? 352 LYS   A C   1 
ATOM   2766 O  O   . LYS   A 1 367 ? 13.679  -38.186 -43.906 1 39.05 ? 352 LYS   A O   1 
ATOM   2767 C  CB  . LYS   A 1 367 ? 15.544  -40.044 -41.833 1 36.82 ? 352 LYS   A CB  1 
ATOM   2768 C  CG  . LYS   A 1 367 ? 14.324  -40.899 -42.166 1 37.15 ? 352 LYS   A CG  1 
ATOM   2769 C  CD  . LYS   A 1 367 ? 14.184  -42.156 -41.324 1 37.18 ? 352 LYS   A CD  1 
ATOM   2770 C  CE  . LYS   A 1 367 ? 12.824  -42.761 -41.547 1 38.32 ? 352 LYS   A CE  1 
ATOM   2771 N  NZ  . LYS   A 1 367 ? 12.655  -44.072 -40.863 1 39.75 ? 352 LYS   A NZ  1 
ATOM   2772 N  N   . TYR   A 1 368 ? 13.999  -37.262 -41.878 1 38.33 ? 353 TYR   A N   1 
ATOM   2773 C  CA  . TYR   A 1 368 ? 12.7    -36.619 -41.804 1 38.66 ? 353 TYR   A CA  1 
ATOM   2774 C  C   . TYR   A 1 368 ? 12.625  -35.215 -42.379 1 39.96 ? 353 TYR   A C   1 
ATOM   2775 O  O   . TYR   A 1 368 ? 11.518  -34.744 -42.629 1 39.5  ? 353 TYR   A O   1 
ATOM   2776 C  CB  . TYR   A 1 368 ? 12.198  -36.629 -40.344 1 38.05 ? 353 TYR   A CB  1 
ATOM   2777 C  CG  . TYR   A 1 368 ? 11.771  -38.009 -39.895 1 38.21 ? 353 TYR   A CG  1 
ATOM   2778 C  CD1 . TYR   A 1 368 ? 12.68   -38.893 -39.337 1 39.2  ? 353 TYR   A CD1 1 
ATOM   2779 C  CD2 . TYR   A 1 368 ? 10.479  -38.454 -40.095 1 39.18 ? 353 TYR   A CD2 1 
ATOM   2780 C  CE1 . TYR   A 1 368 ? 12.297  -40.163 -38.93  1 39.85 ? 353 TYR   A CE1 1 
ATOM   2781 C  CE2 . TYR   A 1 368 ? 10.1    -39.74  -39.749 1 40.17 ? 353 TYR   A CE2 1 
ATOM   2782 C  CZ  . TYR   A 1 368 ? 11.009  -40.592 -39.156 1 40.87 ? 353 TYR   A CZ  1 
ATOM   2783 O  OH  . TYR   A 1 368 ? 10.628  -41.861 -38.805 1 42.75 ? 353 TYR   A OH  1 
ATOM   2784 N  N   . ILE   A 1 369 ? 13.759  -34.534 -42.557 1 41.06 ? 354 ILE   A N   1 
ATOM   2785 C  CA  . ILE   A 1 369 ? 13.745  -33.172 -43.083 1 42.87 ? 354 ILE   A CA  1 
ATOM   2786 C  C   . ILE   A 1 369 ? 14.591  -33.045 -44.334 1 44.89 ? 354 ILE   A C   1 
ATOM   2787 O  O   . ILE   A 1 369 ? 14.056  -32.7   -45.377 1 45.65 ? 354 ILE   A O   1 
ATOM   2788 C  CB  . ILE   A 1 369 ? 14.11   -32.087 -42.009 1 43.22 ? 354 ILE   A CB  1 
ATOM   2789 C  CG1 . ILE   A 1 369 ? 13.061  -32.013 -40.884 1 43.7  ? 354 ILE   A CG1 1 
ATOM   2790 C  CG2 . ILE   A 1 369 ? 14.292  -30.709 -42.657 1 43.57 ? 354 ILE   A CG2 1 
ATOM   2791 C  CD1 . ILE   A 1 369 ? 13.528  -31.21  -39.697 1 44.19 ? 354 ILE   A CD1 1 
ATOM   2792 N  N   . LEU   A 1 370 ? 15.888  -33.326 -44.241 1 46.08 ? 355 LEU   A N   1 
ATOM   2793 C  CA  . LEU   A 1 370 ? 16.846  -33.167 -45.328 1 48.37 ? 355 LEU   A CA  1 
ATOM   2794 C  C   . LEU   A 1 370 ? 16.474  -33.871 -46.624 1 49.7  ? 355 LEU   A C   1 
ATOM   2795 O  O   . LEU   A 1 370 ? 16.441  -33.228 -47.67  1 49.74 ? 355 LEU   A O   1 
ATOM   2796 C  CB  . LEU   A 1 370 ? 18.259  -33.598 -44.881 1 49.12 ? 355 LEU   A CB  1 
ATOM   2797 C  CG  . LEU   A 1 370 ? 19.125  -32.595 -44.101 1 51.49 ? 355 LEU   A CG  1 
ATOM   2798 C  CD1 . LEU   A 1 370 ? 20.571  -33.028 -44.153 1 52.06 ? 355 LEU   A CD1 1 
ATOM   2799 C  CD2 . LEU   A 1 370 ? 19      -31.16  -44.644 1 52.32 ? 355 LEU   A CD2 1 
ATOM   2800 N  N   . ILE   A 1 371 ? 16.226  -35.178 -46.561 1 50.5  ? 356 ILE   A N   1 
ATOM   2801 C  CA  . ILE   A 1 371 ? 15.863  -35.967 -47.723 1 51.87 ? 356 ILE   A CA  1 
ATOM   2802 C  C   . ILE   A 1 371 ? 14.482  -35.543 -48.277 1 53.83 ? 356 ILE   A C   1 
ATOM   2803 O  O   . ILE   A 1 371 ? 14.456  -35.15  -49.444 1 54.11 ? 356 ILE   A O   1 
ATOM   2804 C  CB  . ILE   A 1 371 ? 16.013  -37.467 -47.424 1 51.89 ? 356 ILE   A CB  1 
ATOM   2805 C  CG1 . ILE   A 1 371 ? 17.509  -37.809 -47.293 1 52.42 ? 356 ILE   A CG1 1 
ATOM   2806 C  CG2 . ILE   A 1 371 ? 15.323  -38.321 -48.476 1 52.14 ? 356 ILE   A CG2 1 
ATOM   2807 C  CD1 . ILE   A 1 371 ? 17.793  -39.191 -46.789 1 53.54 ? 356 ILE   A CD1 1 
ATOM   2808 N  N   . PRO   A 1 372 ? 13.376  -35.452 -47.491 1 54.96 ? 357 PRO   A N   1 
ATOM   2809 C  CA  . PRO   A 1 372 ? 12.118  -34.945 -48.062 1 56.26 ? 357 PRO   A CA  1 
ATOM   2810 C  C   . PRO   A 1 372 ? 12.222  -33.534 -48.669 1 58.71 ? 357 PRO   A C   1 
ATOM   2811 O  O   . PRO   A 1 372 ? 11.595  -33.274 -49.694 1 59.26 ? 357 PRO   A O   1 
ATOM   2812 C  CB  . PRO   A 1 372 ? 11.145  -35.01  -46.873 1 56.25 ? 357 PRO   A CB  1 
ATOM   2813 C  CG  . PRO   A 1 372 ? 11.705  -36.061 -45.989 1 56.08 ? 357 PRO   A CG  1 
ATOM   2814 C  CD  . PRO   A 1 372 ? 13.181  -35.848 -46.082 1 54.42 ? 357 PRO   A CD  1 
ATOM   2815 N  N   . ALA   A 1 373 ? 13.032  -32.641 -48.087 1 60.3  ? 358 ALA   A N   1 
ATOM   2816 C  CA  . ALA   A 1 373 ? 13.229  -31.296 -48.654 1 62.56 ? 358 ALA   A CA  1 
ATOM   2817 C  C   . ALA   A 1 373 ? 13.882  -31.352 -50.038 1 65.61 ? 358 ALA   A C   1 
ATOM   2818 O  O   . ALA   A 1 373 ? 13.616  -30.497 -50.887 1 65.98 ? 358 ALA   A O   1 
ATOM   2819 C  CB  . ALA   A 1 373 ? 14.084  -30.443 -47.727 1 62.31 ? 358 ALA   A CB  1 
ATOM   2820 N  N   . SER   A 1 374 ? 14.768  -32.347 -50.247 1 67.46 ? 359 SER   A N   1 
ATOM   2821 C  CA  . SER   A 1 374 ? 15.485  -32.555 -51.506 1 69.44 ? 359 SER   A CA  1 
ATOM   2822 C  C   . SER   A 1 374 ? 14.595  -33.127 -52.612 1 71.54 ? 359 SER   A C   1 
ATOM   2823 O  O   . SER   A 1 374 ? 14.954  -33.028 -53.787 1 71.87 ? 359 SER   A O   1 
ATOM   2824 C  CB  . SER   A 1 374 ? 16.698  -33.46  -51.296 1 70.41 ? 359 SER   A CB  1 
ATOM   2825 O  OG  . SER   A 1 374 ? 16.335  -34.83  -51.2   1 72.51 ? 359 SER   A OG  1 
ATOM   2826 N  N   . GLN   A 1 375 ? 13.452  -33.735 -52.247 1 72.72 ? 360 GLN   A N   1 
ATOM   2827 C  CA  . GLN   A 1 375 ? 12.535  -34.328 -53.207 1 74.47 ? 360 GLN   A CA  1 
ATOM   2828 C  C   . GLN   A 1 375 ? 11.41   -33.365 -53.597 1 76.45 ? 360 GLN   A C   1 
ATOM   2829 O  O   . GLN   A 1 375 ? 10.222  -33.704 -53.523 1 76.91 ? 360 GLN   A O   1 
ATOM   2830 C  CB  . GLN   A 1 375 ? 12.021  -35.679 -52.704 1 75.58 ? 360 GLN   A CB  1 
ATOM   2831 C  CG  . GLN   A 1 375 ? 13.167  -36.653 -52.45  1 78.51 ? 360 GLN   A CG  1 
ATOM   2832 C  CD  . GLN   A 1 375 ? 12.744  -37.84  -51.627 1 82.8  ? 360 GLN   A CD  1 
ATOM   2833 O  OE1 . GLN   A 1 375 ? 11.859  -37.745 -50.769 1 84.6  ? 360 GLN   A OE1 1 
ATOM   2834 N  NE2 . GLN   A 1 375 ? 13.378  -38.983 -51.857 1 83.16 ? 360 GLN   A NE2 1 
ATOM   2835 N  N   . GLN   A 1 376 ? 11.827  -32.152 -54.029 1 77.4  ? 361 GLN   A N   1 
ATOM   2836 C  CA  . GLN   A 1 376 ? 11      -31.059 -54.539 1 78.63 ? 361 GLN   A CA  1 
ATOM   2837 C  C   . GLN   A 1 376 ? 11.749  -30.309 -55.652 1 79.37 ? 361 GLN   A C   1 
ATOM   2838 O  O   . GLN   A 1 376 ? 11.242  -30.165 -56.768 1 79.78 ? 361 GLN   A O   1 
ATOM   2839 C  CB  . GLN   A 1 376 ? 10.6    -30.093 -53.421 1 80.26 ? 361 GLN   A CB  1 
ATOM   2840 C  CG  . GLN   A 1 376 ? 9.34    -30.546 -52.712 1 83.17 ? 361 GLN   A CG  1 
ATOM   2841 C  CD  . GLN   A 1 376 ? 9.585   -30.678 -51.244 1 86.24 ? 361 GLN   A CD  1 
ATOM   2842 O  OE1 . GLN   A 1 376 ? 10.178  -29.794 -50.615 1 86.83 ? 361 GLN   A OE1 1 
ATOM   2843 N  NE2 . GLN   A 1 376 ? 9.133   -31.787 -50.673 1 86.86 ? 361 GLN   A NE2 1 
ATOM   2844 N  N   . GLY   A 1 396 ? 17.356  -23.966 -45.279 1 73.8  ? 381 GLY   A N   1 
ATOM   2845 C  CA  . GLY   A 1 396 ? 17.449  -25.413 -45.438 1 74.39 ? 381 GLY   A CA  1 
ATOM   2846 C  C   . GLY   A 1 396 ? 18.426  -26.064 -44.474 1 74.5  ? 381 GLY   A C   1 
ATOM   2847 O  O   . GLY   A 1 396 ? 18.057  -26.389 -43.343 1 75.09 ? 381 GLY   A O   1 
ATOM   2848 N  N   . THR   A 1 397 ? 19.699  -26.236 -44.905 1 73.46 ? 382 THR   A N   1 
ATOM   2849 C  CA  . THR   A 1 397 ? 20.771  -26.822 -44.085 1 72.68 ? 382 THR   A CA  1 
ATOM   2850 C  C   . THR   A 1 397 ? 21.21   -25.927 -42.908 1 70.77 ? 382 THR   A C   1 
ATOM   2851 O  O   . THR   A 1 397 ? 22.191  -26.247 -42.246 1 70.68 ? 382 THR   A O   1 
ATOM   2852 C  CB  . THR   A 1 397 ? 21.995  -27.162 -44.954 1 74.58 ? 382 THR   A CB  1 
ATOM   2853 O  OG1 . THR   A 1 397 ? 22.359  -26.019 -45.736 1 76.14 ? 382 THR   A OG1 1 
ATOM   2854 C  CG2 . THR   A 1 397 ? 21.772  -28.376 -45.848 1 74.92 ? 382 THR   A CG2 1 
ATOM   2855 N  N   . ASP   A 1 398 ? 20.503  -24.819 -42.654 1 68.93 ? 383 ASP   A N   1 
ATOM   2856 C  CA  . ASP   A 1 398 ? 20.781  -23.918 -41.537 1 67.4  ? 383 ASP   A CA  1 
ATOM   2857 C  C   . ASP   A 1 398 ? 20.473  -24.627 -40.212 1 64.64 ? 383 ASP   A C   1 
ATOM   2858 O  O   . ASP   A 1 398 ? 21.169  -24.383 -39.223 1 64.71 ? 383 ASP   A O   1 
ATOM   2859 C  CB  . ASP   A 1 398 ? 19.918  -22.649 -41.659 1 70.28 ? 383 ASP   A CB  1 
ATOM   2860 C  CG  . ASP   A 1 398 ? 20.628  -21.383 -41.242 1 77.28 ? 383 ASP   A CG  1 
ATOM   2861 O  OD1 . ASP   A 1 398 ? 21.425  -20.851 -42.061 1 78.68 ? 383 ASP   A OD1 1 
ATOM   2862 O  OD2 . ASP   A 1 398 ? 20.39   -20.914 -40.094 1 79.63 ? 383 ASP   A OD2 1 
ATOM   2863 N  N   . LEU   A 1 399 ? 19.42   -25.489 -40.183 1 61.98 ? 384 LEU   A N   1 
ATOM   2864 C  CA  . LEU   A 1 399 ? 19.095  -26.257 -38.986 1 60.03 ? 384 LEU   A CA  1 
ATOM   2865 C  C   . LEU   A 1 399 ? 20.126  -27.356 -38.753 1 58.95 ? 384 LEU   A C   1 
ATOM   2866 O  O   . LEU   A 1 399 ? 20.45   -27.637 -37.602 1 59.11 ? 384 LEU   A O   1 
ATOM   2867 C  CB  . LEU   A 1 399 ? 17.653  -26.79  -38.932 1 59.1  ? 384 LEU   A CB  1 
ATOM   2868 C  CG  . LEU   A 1 399 ? 17.12   -27.59  -40.093 1 58.96 ? 384 LEU   A CG  1 
ATOM   2869 C  CD1 . LEU   A 1 399 ? 17.297  -29.064 -39.859 1 58.89 ? 384 LEU   A CD1 1 
ATOM   2870 C  CD2 . LEU   A 1 399 ? 15.637  -27.324 -40.269 1 58.86 ? 384 LEU   A CD2 1 
ATOM   2871 N  N   . MET   A 1 400 ? 20.679  -27.946 -39.831 1 57.55 ? 385 MET   A N   1 
ATOM   2872 C  CA  . MET   A 1 400 ? 21.726  -28.953 -39.71  1 56.63 ? 385 MET   A CA  1 
ATOM   2873 C  C   . MET   A 1 400 ? 22.964  -28.337 -39.093 1 54.44 ? 385 MET   A C   1 
ATOM   2874 O  O   . MET   A 1 400 ? 23.556  -28.94  -38.209 1 54.54 ? 385 MET   A O   1 
ATOM   2875 C  CB  . MET   A 1 400 ? 22.071  -29.573 -41.07  1 57.98 ? 385 MET   A CB  1 
ATOM   2876 C  CG  . MET   A 1 400 ? 21.031  -30.525 -41.566 1 61.49 ? 385 MET   A CG  1 
ATOM   2877 S  SD  . MET   A 1 400 ? 20.708  -31.939 -40.453 1 72.88 ? 385 MET   A SD  1 
ATOM   2878 C  CE  . MET   A 1 400 ? 22.022  -32.975 -40.797 1 70.37 ? 385 MET   A CE  1 
ATOM   2879 N  N   . ASN   A 1 401 ? 23.327  -27.123 -39.518 1 52.54 ? 386 ASN   A N   1 
ATOM   2880 C  CA  . ASN   A 1 401 ? 24.482  -26.404 -38.984 1 51.31 ? 386 ASN   A CA  1 
ATOM   2881 C  C   . ASN   A 1 401 ? 24.31   -26.102 -37.509 1 47.93 ? 386 ASN   A C   1 
ATOM   2882 O  O   . ASN   A 1 401 ? 25.283  -26.171 -36.758 1 48.3  ? 386 ASN   A O   1 
ATOM   2883 C  CB  . ASN   A 1 401 ? 24.718  -25.108 -39.751 1 54.56 ? 386 ASN   A CB  1 
ATOM   2884 C  CG  . ASN   A 1 401 ? 25.264  -25.332 -41.136 1 61    ? 386 ASN   A CG  1 
ATOM   2885 O  OD1 . ASN   A 1 401 ? 25.867  -26.377 -41.439 1 63.39 ? 386 ASN   A OD1 1 
ATOM   2886 N  ND2 . ASN   A 1 401 ? 25.049  -24.352 -42.008 1 62.26 ? 386 ASN   A ND2 1 
ATOM   2887 N  N   . PHE   A 1 402 ? 23.082  -25.763 -37.086 1 44.71 ? 387 PHE   A N   1 
ATOM   2888 C  CA  . PHE   A 1 402 ? 22.768  -25.491 -35.689 1 42.5  ? 387 PHE   A CA  1 
ATOM   2889 C  C   . PHE   A 1 402 ? 22.977  -26.78  -34.897 1 41.64 ? 387 PHE   A C   1 
ATOM   2890 O  O   . PHE   A 1 402 ? 23.72   -26.769 -33.93  1 42.27 ? 387 PHE   A O   1 
ATOM   2891 C  CB  . PHE   A 1 402 ? 21.316  -24.968 -35.533 1 41.36 ? 387 PHE   A CB  1 
ATOM   2892 C  CG  . PHE   A 1 402 ? 20.793  -25.04  -34.109 1 41.14 ? 387 PHE   A CG  1 
ATOM   2893 C  CD1 . PHE   A 1 402 ? 21.263  -24.171 -33.136 1 41.25 ? 387 PHE   A CD1 1 
ATOM   2894 C  CD2 . PHE   A 1 402 ? 19.886  -26.022 -33.732 1 40.99 ? 387 PHE   A CD2 1 
ATOM   2895 C  CE1 . PHE   A 1 402 ? 20.823  -24.264 -31.826 1 41.35 ? 387 PHE   A CE1 1 
ATOM   2896 C  CE2 . PHE   A 1 402 ? 19.466  -26.129 -32.412 1 41.32 ? 387 PHE   A CE2 1 
ATOM   2897 C  CZ  . PHE   A 1 402 ? 19.928  -25.24  -31.471 1 41.18 ? 387 PHE   A CZ  1 
ATOM   2898 N  N   . LEU   A 1 403 ? 22.403  -27.889 -35.358 1 40.36 ? 388 LEU   A N   1 
ATOM   2899 C  CA  . LEU   A 1 403 ? 22.512  -29.174 -34.695 1 40.7  ? 388 LEU   A CA  1 
ATOM   2900 C  C   . LEU   A 1 403 ? 23.951  -29.705 -34.642 1 41.06 ? 388 LEU   A C   1 
ATOM   2901 O  O   . LEU   A 1 403 ? 24.343  -30.303 -33.634 1 41.38 ? 388 LEU   A O   1 
ATOM   2902 C  CB  . LEU   A 1 403 ? 21.56   -30.188 -35.338 1 40.79 ? 388 LEU   A CB  1 
ATOM   2903 C  CG  . LEU   A 1 403 ? 20.074  -29.888 -35.154 1 42.21 ? 388 LEU   A CG  1 
ATOM   2904 C  CD1 . LEU   A 1 403 ? 19.228  -30.833 -35.981 1 43.19 ? 388 LEU   A CD1 1 
ATOM   2905 C  CD2 . LEU   A 1 403 ? 19.666  -29.958 -33.678 1 42.3  ? 388 LEU   A CD2 1 
ATOM   2906 N  N   . LYS   A 1 404 ? 24.734  -29.456 -35.7   1 40.8  ? 389 LYS   A N   1 
ATOM   2907 C  CA  . LYS   A 1 404 ? 26.137  -29.849 -35.788 1 41.4  ? 389 LYS   A CA  1 
ATOM   2908 C  C   . LYS   A 1 404 ? 26.984  -29.035 -34.841 1 40.94 ? 389 LYS   A C   1 
ATOM   2909 O  O   . LYS   A 1 404 ? 27.906  -29.593 -34.274 1 41.28 ? 389 LYS   A O   1 
ATOM   2910 C  CB  . LYS   A 1 404 ? 26.678  -29.723 -37.216 1 43.84 ? 389 LYS   A CB  1 
ATOM   2911 C  CG  . LYS   A 1 404 ? 26.209  -30.842 -38.142 1 48.36 ? 389 LYS   A CG  1 
ATOM   2912 C  CD  . LYS   A 1 404 ? 26.414  -30.482 -39.596 1 53.34 ? 389 LYS   A CD  1 
ATOM   2913 C  CE  . LYS   A 1 404 ? 27.867  -30.455 -39.961 1 59.86 ? 389 LYS   A CE  1 
ATOM   2914 N  NZ  . LYS   A 1 404 ? 28.079  -29.845 -41.303 1 63.99 ? 389 LYS   A NZ  1 
ATOM   2915 N  N   . THR   A 1 405 ? 26.659  -27.739 -34.63  1 40.24 ? 390 THR   A N   1 
ATOM   2916 C  CA  . THR   A 1 405 ? 27.383  -26.893 -33.686 1 40.41 ? 390 THR   A CA  1 
ATOM   2917 C  C   . THR   A 1 405 ? 27.137  -27.382 -32.255 1 40.7  ? 390 THR   A C   1 
ATOM   2918 O  O   . THR   A 1 405 ? 28.087  -27.561 -31.493 1 40.98 ? 390 THR   A O   1 
ATOM   2919 C  CB  . THR   A 1 405 ? 26.973  -25.428 -33.839 1 41.98 ? 390 THR   A CB  1 
ATOM   2920 O  OG1 . THR   A 1 405 ? 27.347  -24.959 -35.134 1 43.99 ? 390 THR   A OG1 1 
ATOM   2921 C  CG2 . THR   A 1 405 ? 27.594  -24.54  -32.783 1 41.56 ? 390 THR   A CG2 1 
ATOM   2922 N  N   . VAL   A 1 406 ? 25.872  -27.651 -31.907 1 40.22 ? 391 VAL   A N   1 
ATOM   2923 C  CA  . VAL   A 1 406 ? 25.522  -28.145 -30.576 1 40.07 ? 391 VAL   A CA  1 
ATOM   2924 C  C   . VAL   A 1 406 ? 26.2    -29.494 -30.3   1 39.75 ? 391 VAL   A C   1 
ATOM   2925 O  O   . VAL   A 1 406 ? 26.719  -29.711 -29.205 1 39.69 ? 391 VAL   A O   1 
ATOM   2926 C  CB  . VAL   A 1 406 ? 23.977  -28.234 -30.402 1 39.74 ? 391 VAL   A CB  1 
ATOM   2927 C  CG1 . VAL   A 1 406 ? 23.611  -28.807 -29.036 1 39.74 ? 391 VAL   A CG1 1 
ATOM   2928 C  CG2 . VAL   A 1 406 ? 23.324  -26.874 -30.616 1 38.84 ? 391 VAL   A CG2 1 
ATOM   2929 N  N   . ARG   A 1 407 ? 26.225  -30.379 -31.305 1 39.11 ? 392 ARG   A N   1 
ATOM   2930 C  CA  . ARG   A 1 407 ? 26.856  -31.677 -31.165 1 38.92 ? 392 ARG   A CA  1 
ATOM   2931 C  C   . ARG   A 1 407 ? 28.365  -31.546 -30.994 1 39.98 ? 392 ARG   A C   1 
ATOM   2932 O  O   . ARG   A 1 407 ? 28.959  -32.213 -30.139 1 39.81 ? 392 ARG   A O   1 
ATOM   2933 C  CB  . ARG   A 1 407 ? 26.531  -32.592 -32.354 1 38.97 ? 392 ARG   A CB  1 
ATOM   2934 C  CG  . ARG   A 1 407 ? 27.077  -33.972 -32.109 1 41.14 ? 392 ARG   A CG  1 
ATOM   2935 C  CD  . ARG   A 1 407 ? 27.324  -34.815 -33.351 1 45.36 ? 392 ARG   A CD  1 
ATOM   2936 N  NE  . ARG   A 1 407 ? 28.327  -35.838 -33.052 1 48.62 ? 392 ARG   A NE  1 
ATOM   2937 C  CZ  . ARG   A 1 407 ? 29.645  -35.646 -33.111 1 50.47 ? 392 ARG   A CZ  1 
ATOM   2938 N  NH1 . ARG   A 1 407 ? 30.136  -34.491 -33.548 1 49.88 ? 392 ARG   A NH1 1 
ATOM   2939 N  NH2 . ARG   A 1 407 ? 30.479  -36.614 -32.75  1 49.99 ? 392 ARG   A NH2 1 
ATOM   2940 N  N   . SER   A 1 408 ? 28.974  -30.671 -31.79  1 40.47 ? 393 SER   A N   1 
ATOM   2941 C  CA  . SER   A 1 408 ? 30.403  -30.403 -31.788 1 41.29 ? 393 SER   A CA  1 
ATOM   2942 C  C   . SER   A 1 408 ? 30.857  -29.874 -30.427 1 41.52 ? 393 SER   A C   1 
ATOM   2943 O  O   . SER   A 1 408 ? 31.861  -30.331 -29.906 1 41.22 ? 393 SER   A O   1 
ATOM   2944 C  CB  . SER   A 1 408 ? 30.743  -29.406 -32.894 1 43.18 ? 393 SER   A CB  1 
ATOM   2945 O  OG  . SER   A 1 408 ? 32.127  -29.116 -32.871 1 47.41 ? 393 SER   A OG  1 
ATOM   2946 N  N   . THR   A 1 409 ? 30.083  -28.947 -29.837 1 41.81 ? 394 THR   A N   1 
ATOM   2947 C  CA  . THR   A 1 409 ? 30.33   -28.373 -28.517 1 42.05 ? 394 THR   A CA  1 
ATOM   2948 C  C   . THR   A 1 409 ? 30.294  -29.486 -27.464 1 41.84 ? 394 THR   A C   1 
ATOM   2949 O  O   . THR   A 1 409 ? 31.11   -29.493 -26.533 1 42.4  ? 394 THR   A O   1 
ATOM   2950 C  CB  . THR   A 1 409 ? 29.246  -27.307 -28.241 1 43.94 ? 394 THR   A CB  1 
ATOM   2951 O  OG1 . THR   A 1 409 ? 29.351  -26.289 -29.24  1 45.46 ? 394 THR   A OG1 1 
ATOM   2952 C  CG2 . THR   A 1 409 ? 29.363  -26.676 -26.86  1 44.05 ? 394 THR   A CG2 1 
ATOM   2953 N  N   . THR   A 1 410 ? 29.355  -30.439 -27.61  1 40.4  ? 395 THR   A N   1 
ATOM   2954 C  CA  . THR   A 1 410 ? 29.261  -31.556 -26.673 1 39.07 ? 395 THR   A CA  1 
ATOM   2955 C  C   . THR   A 1 410 ? 30.491  -32.432 -26.8   1 38.65 ? 395 THR   A C   1 
ATOM   2956 O  O   . THR   A 1 410 ? 31.083  -32.763 -25.795 1 37.47 ? 395 THR   A O   1 
ATOM   2957 C  CB  . THR   A 1 410 ? 27.984  -32.376 -26.886 1 38.16 ? 395 THR   A CB  1 
ATOM   2958 O  OG1 . THR   A 1 410 ? 26.885  -31.503 -27.12  1 38.22 ? 395 THR   A OG1 1 
ATOM   2959 C  CG2 . THR   A 1 410 ? 27.696  -33.274 -25.711 1 37.62 ? 395 THR   A CG2 1 
ATOM   2960 N  N   . GLU   A 1 411 ? 30.878  -32.794 -28.04  1 39.39 ? 396 GLU   A N   1 
ATOM   2961 C  CA  . GLU   A 1 411 ? 32.019  -33.655 -28.338 1 40.45 ? 396 GLU   A CA  1 
ATOM   2962 C  C   . GLU   A 1 411 ? 33.339  -33.05  -27.826 1 40.95 ? 396 GLU   A C   1 
ATOM   2963 O  O   . GLU   A 1 411 ? 34.168  -33.757 -27.25  1 40.52 ? 396 GLU   A O   1 
ATOM   2964 C  CB  . GLU   A 1 411 ? 32.091  -33.896 -29.85  1 43.27 ? 396 GLU   A CB  1 
ATOM   2965 C  CG  . GLU   A 1 411 ? 32.924  -35.111 -30.209 1 49.28 ? 396 GLU   A CG  1 
ATOM   2966 C  CD  . GLU   A 1 411 ? 34.4    -34.821 -30.42  1 56.78 ? 396 GLU   A CD  1 
ATOM   2967 O  OE1 . GLU   A 1 411 ? 34.728  -33.676 -30.815 1 57.3  ? 396 GLU   A OE1 1 
ATOM   2968 O  OE2 . GLU   A 1 411 ? 35.228  -35.734 -30.177 1 59.07 ? 396 GLU   A OE2 1 
ATOM   2969 N  N   . LYS   A 1 412 ? 33.506  -31.736 -27.997 1 41.1  ? 397 LYS   A N   1 
ATOM   2970 C  CA  . LYS   A 1 412 ? 34.71   -31.052 -27.547 1 42.14 ? 397 LYS   A CA  1 
ATOM   2971 C  C   . LYS   A 1 412 ? 34.799  -30.871 -26.028 1 43.16 ? 397 LYS   A C   1 
ATOM   2972 O  O   . LYS   A 1 412 ? 35.795  -30.35  -25.544 1 43.7  ? 397 LYS   A O   1 
ATOM   2973 C  CB  . LYS   A 1 412 ? 34.882  -29.724 -28.289 1 43.8  ? 397 LYS   A CB  1 
ATOM   2974 C  CG  . LYS   A 1 412 ? 35.191  -30     -29.751 1 47.49 ? 397 LYS   A CG  1 
ATOM   2975 C  CD  . LYS   A 1 412 ? 35.511  -28.77  -30.554 1 54.17 ? 397 LYS   A CD  1 
ATOM   2976 C  CE  . LYS   A 1 412 ? 35.513  -29.136 -32.015 1 59.21 ? 397 LYS   A CE  1 
ATOM   2977 N  NZ  . LYS   A 1 412 ? 34.7    -28.18  -32.811 1 62.29 ? 397 LYS   A NZ  1 
ATOM   2978 N  N   . SER   A 1 413 ? 33.777  -31.304 -25.279 1 43.39 ? 398 SER   A N   1 
ATOM   2979 C  CA  . SER   A 1 413 ? 33.772  -31.285 -23.818 1 43.44 ? 398 SER   A CA  1 
ATOM   2980 C  C   . SER   A 1 413 ? 34.332  -32.572 -23.224 1 43.55 ? 398 SER   A C   1 
ATOM   2981 O  O   . SER   A 1 413 ? 34.519  -32.643 -22.013 1 43.85 ? 398 SER   A O   1 
ATOM   2982 C  CB  . SER   A 1 413 ? 32.372  -31.041 -23.275 1 44.05 ? 398 SER   A CB  1 
ATOM   2983 O  OG  . SER   A 1 413 ? 32.043  -29.677 -23.453 1 47.2  ? 398 SER   A OG  1 
ATOM   2984 N  N   . LEU   A 1 414 ? 34.596  -33.599 -24.042 1 43.84 ? 399 LEU   A N   1 
ATOM   2985 C  CA  . LEU   A 1 414 ? 35.201  -34.83  -23.566 1 45.17 ? 399 LEU   A CA  1 
ATOM   2986 C  C   . LEU   A 1 414 ? 36.607  -34.516 -23.07  1 47.53 ? 399 LEU   A C   1 
ATOM   2987 O  O   . LEU   A 1 414 ? 37.309  -33.706 -23.663 1 47.33 ? 399 LEU   A O   1 
ATOM   2988 C  CB  . LEU   A 1 414 ? 35.238  -35.888 -24.677 1 44.78 ? 399 LEU   A CB  1 
ATOM   2989 C  CG  . LEU   A 1 414 ? 33.88   -36.459 -25.054 1 45.83 ? 399 LEU   A CG  1 
ATOM   2990 C  CD1 . LEU   A 1 414 ? 33.94   -37.168 -26.387 1 46.14 ? 399 LEU   A CD1 1 
ATOM   2991 C  CD2 . LEU   A 1 414 ? 33.352  -37.368 -23.972 1 46.2  ? 399 LEU   A CD2 1 
ATOM   2992 N  N   . LEU   A 1 415 ? 36.94   -35.031 -21.899 1 49.97 ? 400 LEU   A N   1 
ATOM   2993 C  CA  . LEU   A 1 415 ? 38.257  -34.837 -21.305 1 52.46 ? 400 LEU   A CA  1 
ATOM   2994 C  C   . LEU   A 1 415 ? 39.288  -35.73  -22.033 1 55.48 ? 400 LEU   A C   1 
ATOM   2995 O  O   . LEU   A 1 415 ? 40.425  -35.305 -22.232 1 56.3  ? 400 LEU   A O   1 
ATOM   2996 C  CB  . LEU   A 1 415 ? 38.205  -35.1   -19.788 1 52.1  ? 400 LEU   A CB  1 
ATOM   2997 C  CG  . LEU   A 1 415 ? 37.127  -34.334 -19.015 1 52.38 ? 400 LEU   A CG  1 
ATOM   2998 C  CD1 . LEU   A 1 415 ? 37.149  -34.684 -17.547 1 52.83 ? 400 LEU   A CD1 1 
ATOM   2999 C  CD2 . LEU   A 1 415 ? 37.28   -32.828 -19.182 1 52.5  ? 400 LEU   A CD2 1 
ATOM   3000 N  N   . LYS   A 1 416 ? 38.866  -36.928 -22.476 1 57.24 ? 401 LYS   A N   1 
ATOM   3001 C  CA  . LYS   A 1 416 ? 39.643  -37.864 -23.295 1 59.75 ? 401 LYS   A CA  1 
ATOM   3002 C  C   . LYS   A 1 416 ? 38.763  -38.19  -24.524 1 62.67 ? 401 LYS   A C   1 
ATOM   3003 O  O   . LYS   A 1 416 ? 37.549  -38.381 -24.366 1 62.85 ? 401 LYS   A O   1 
ATOM   3004 C  CB  . LYS   A 1 416 ? 39.994  -39.145 -22.512 1 61.04 ? 401 LYS   A CB  1 
ATOM   3005 N  N   . GLU   A 1 417 ? 39.351  -38.229 -25.749 1 64.41 ? 402 GLU   A N   1 
ATOM   3006 C  CA  . GLU   A 1 417 ? 38.584  -38.501 -26.988 1 66.01 ? 402 GLU   A CA  1 
ATOM   3007 C  C   . GLU   A 1 417 ? 37.576  -39.678 -26.896 1 66.5  ? 402 GLU   A C   1 
ATOM   3008 O  O   . GLU   A 1 417 ? 37.942  -40.794 -26.51  1 66.63 ? 402 GLU   A O   1 
ATOM   3009 C  CB  . GLU   A 1 417 ? 39.512  -38.713 -28.196 1 68.79 ? 402 GLU   A CB  1 
ATOM   3010 C  CG  . GLU   A 1 417 ? 40.465  -37.573 -28.5   1 75.23 ? 402 GLU   A CG  1 
ATOM   3011 C  CD  . GLU   A 1 417 ? 41.383  -37.896 -29.667 1 83.41 ? 402 GLU   A CD  1 
ATOM   3012 O  OE1 . GLU   A 1 417 ? 40.945  -38.631 -30.584 1 83.37 ? 402 GLU   A OE1 1 
ATOM   3013 O  OE2 . GLU   A 1 417 ? 42.542  -37.419 -29.666 1 86.96 ? 402 GLU   A OE2 1 
ATOM   3014 N  N   . THR   B 1 25  ? 20.853  -11.808 6.196   1 71.47 ? 10  THR   B N   1 
ATOM   3015 C  CA  . THR   B 1 25  ? 21.489  -10.999 5.151   1 71.79 ? 10  THR   B CA  1 
ATOM   3016 C  C   . THR   B 1 25  ? 22.001  -11.837 3.956   1 70.6  ? 10  THR   B C   1 
ATOM   3017 O  O   . THR   B 1 25  ? 22.361  -13.003 4.128   1 70.65 ? 10  THR   B O   1 
ATOM   3018 C  CB  . THR   B 1 25  ? 22.615  -10.116 5.733   1 74.14 ? 10  THR   B CB  1 
ATOM   3019 O  OG1 . THR   B 1 25  ? 23.779  -10.912 5.977   1 75.66 ? 10  THR   B OG1 1 
ATOM   3020 C  CG2 . THR   B 1 25  ? 22.195  -9.378  7.004   1 74.79 ? 10  THR   B CG2 1 
ATOM   3021 N  N   . ILE   B 1 26  ? 22.083  -11.194 2.773   1 69.13 ? 11  ILE   B N   1 
ATOM   3022 C  CA  . ILE   B 1 26  ? 22.552  -11.691 1.464   1 67.84 ? 11  ILE   B CA  1 
ATOM   3023 C  C   . ILE   B 1 26  ? 23.949  -12.352 1.497   1 66.14 ? 11  ILE   B C   1 
ATOM   3024 O  O   . ILE   B 1 26  ? 24.905  -11.75  1.997   1 66.19 ? 11  ILE   B O   1 
ATOM   3025 C  CB  . ILE   B 1 26  ? 22.512  -10.474 0.503   1 68.36 ? 11  ILE   B CB  1 
ATOM   3026 C  CG1 . ILE   B 1 26  ? 21.061  -10.037 0.215   1 68.99 ? 11  ILE   B CG1 1 
ATOM   3027 C  CG2 . ILE   B 1 26  ? 23.324  -10.683 -0.784  1 68.83 ? 11  ILE   B CG2 1 
ATOM   3028 C  CD1 . ILE   B 1 26  ? 20.967  -8.707  -0.392  1 70.11 ? 11  ILE   B CD1 1 
ATOM   3029 N  N   . SER   B 1 27  ? 24.038  -13.593 0.977   1 64.48 ? 12  SER   B N   1 
ATOM   3030 C  CA  . SER   B 1 27  ? 25.243  -14.418 0.905   1 63.38 ? 12  SER   B CA  1 
ATOM   3031 C  C   . SER   B 1 27  ? 26.435  -13.716 0.312   1 62.56 ? 12  SER   B C   1 
ATOM   3032 O  O   . SER   B 1 27  ? 26.321  -13.027 -0.708  1 62.82 ? 12  SER   B O   1 
ATOM   3033 C  CB  . SER   B 1 27  ? 24.983  -15.684 0.1     1 64.06 ? 12  SER   B CB  1 
ATOM   3034 O  OG  . SER   B 1 27  ? 26.131  -16.518 0.074   1 65.9  ? 12  SER   B OG  1 
ATOM   3035 N  N   . LYS   B 1 28  ? 27.6    -13.944 0.938   1 61.48 ? 13  LYS   B N   1 
ATOM   3036 C  CA  . LYS   B 1 28  ? 28.891  -13.407 0.517   1 60.9  ? 13  LYS   B CA  1 
ATOM   3037 C  C   . LYS   B 1 28  ? 29.286  -13.895 -0.893  1 59.87 ? 13  LYS   B C   1 
ATOM   3038 O  O   . LYS   B 1 28  ? 30.06   -13.219 -1.572  1 59.82 ? 13  LYS   B O   1 
ATOM   3039 C  CB  . LYS   B 1 28  ? 29.978  -13.766 1.549   1 62.74 ? 13  LYS   B CB  1 
ATOM   3040 C  CG  . LYS   B 1 28  ? 29.739  -13.16  2.926   1 66.64 ? 13  LYS   B CG  1 
ATOM   3041 N  N   . GLU   B 1 29  ? 28.732  -15.049 -1.337  1 58.72 ? 14  GLU   B N   1 
ATOM   3042 C  CA  . GLU   B 1 29  ? 28.973  -15.617 -2.663  1 58.27 ? 14  GLU   B CA  1 
ATOM   3043 C  C   . GLU   B 1 29  ? 28.42   -14.745 -3.805  1 57.02 ? 14  GLU   B C   1 
ATOM   3044 O  O   . GLU   B 1 29  ? 28.775  -14.96  -4.959  1 56.78 ? 14  GLU   B O   1 
ATOM   3045 C  CB  . GLU   B 1 29  ? 28.359  -17.015 -2.759  1 61.24 ? 14  GLU   B CB  1 
ATOM   3046 C  CG  . GLU   B 1 29  ? 28.773  -17.974 -1.665  1 67.73 ? 14  GLU   B CG  1 
ATOM   3047 C  CD  . GLU   B 1 29  ? 28.23   -19.372 -1.893  1 77.21 ? 14  GLU   B CD  1 
ATOM   3048 O  OE1 . GLU   B 1 29  ? 28.208  -19.81  -3.067  1 79.04 ? 14  GLU   B OE1 1 
ATOM   3049 O  OE2 . GLU   B 1 29  ? 27.822  -20.029 -0.908  1 80.54 ? 14  GLU   B OE2 1 
ATOM   3050 N  N   . TYR   B 1 30  ? 27.505  -13.819 -3.501  1 56.16 ? 15  TYR   B N   1 
ATOM   3051 C  CA  . TYR   B 1 30  ? 26.935  -12.916 -4.5    1 55.56 ? 15  TYR   B CA  1 
ATOM   3052 C  C   . TYR   B 1 30  ? 27.802  -11.682 -4.758  1 55.43 ? 15  TYR   B C   1 
ATOM   3053 O  O   . TYR   B 1 30  ? 27.511  -10.935 -5.692  1 56.11 ? 15  TYR   B O   1 
ATOM   3054 C  CB  . TYR   B 1 30  ? 25.507  -12.489 -4.122  1 55.07 ? 15  TYR   B CB  1 
ATOM   3055 C  CG  . TYR   B 1 30  ? 24.513  -13.623 -4.199  1 55.28 ? 15  TYR   B CG  1 
ATOM   3056 C  CD1 . TYR   B 1 30  ? 24.349  -14.347 -5.369  1 55.68 ? 15  TYR   B CD1 1 
ATOM   3057 C  CD2 . TYR   B 1 30  ? 23.743  -13.977 -3.1    1 55.98 ? 15  TYR   B CD2 1 
ATOM   3058 C  CE1 . TYR   B 1 30  ? 23.452  -15.399 -5.445  1 56.69 ? 15  TYR   B CE1 1 
ATOM   3059 C  CE2 . TYR   B 1 30  ? 22.842  -15.03  -3.162  1 56.79 ? 15  TYR   B CE2 1 
ATOM   3060 C  CZ  . TYR   B 1 30  ? 22.698  -15.738 -4.339  1 57.88 ? 15  TYR   B CZ  1 
ATOM   3061 O  OH  . TYR   B 1 30  ? 21.804  -16.778 -4.428  1 59.71 ? 15  TYR   B OH  1 
ATOM   3062 N  N   . HIS   B 1 31  ? 28.834  -11.453 -3.935  1 54.63 ? 16  HIS   B N   1 
ATOM   3063 C  CA  . HIS   B 1 31  ? 29.772  -10.35  -4.068  1 54.92 ? 16  HIS   B CA  1 
ATOM   3064 C  C   . HIS   B 1 31  ? 29.082  -8.99   -4.128  1 54.46 ? 16  HIS   B C   1 
ATOM   3065 O  O   . HIS   B 1 31  ? 29.372  -8.151  -4.978  1 54.7  ? 16  HIS   B O   1 
ATOM   3066 C  CB  . HIS   B 1 31  ? 30.749  -10.563 -5.244  1 56.21 ? 16  HIS   B CB  1 
ATOM   3067 C  CG  . HIS   B 1 31  ? 31.569  -11.82  -5.139  1 59.48 ? 16  HIS   B CG  1 
ATOM   3068 N  ND1 . HIS   B 1 31  ? 31.882  -12.391 -3.911  1 61.33 ? 16  HIS   B ND1 1 
ATOM   3069 C  CD2 . HIS   B 1 31  ? 32.123  -12.572 -6.12   1 60.95 ? 16  HIS   B CD2 1 
ATOM   3070 C  CE1 . HIS   B 1 31  ? 32.595  -13.473 -4.185  1 62.09 ? 16  HIS   B CE1 1 
ATOM   3071 N  NE2 . HIS   B 1 31  ? 32.772  -13.62  -5.499  1 62.36 ? 16  HIS   B NE2 1 
ATOM   3072 N  N   . ILE   B 1 32  ? 28.158  -8.789  -3.215  1 53.86 ? 17  ILE   B N   1 
ATOM   3073 C  CA  . ILE   B 1 32  ? 27.48   -7.517  -3.047  1 53.78 ? 17  ILE   B CA  1 
ATOM   3074 C  C   . ILE   B 1 32  ? 28.068  -6.95   -1.766  1 54.47 ? 17  ILE   B C   1 
ATOM   3075 O  O   . ILE   B 1 32  ? 28.116  -7.645  -0.744  1 55.13 ? 17  ILE   B O   1 
ATOM   3076 C  CB  . ILE   B 1 32  ? 25.944  -7.674  -2.954  1 53.47 ? 17  ILE   B CB  1 
ATOM   3077 C  CG1 . ILE   B 1 32  ? 25.405  -8.424  -4.175  1 53.85 ? 17  ILE   B CG1 1 
ATOM   3078 C  CG2 . ILE   B 1 32  ? 25.267  -6.307  -2.785  1 53.8  ? 17  ILE   B CG2 1 
ATOM   3079 C  CD1 . ILE   B 1 32  ? 23.936  -8.751  -4.12   1 54.61 ? 17  ILE   B CD1 1 
ATOM   3080 N  N   . ASP   B 1 33  ? 28.597  -5.734  -1.837  1 53.84 ? 18  ASP   B N   1 
ATOM   3081 C  CA  . ASP   B 1 33  ? 29.201  -5.089  -0.695  1 53.61 ? 18  ASP   B CA  1 
ATOM   3082 C  C   . ASP   B 1 33  ? 28.15   -4.312  0.085   1 54.23 ? 18  ASP   B C   1 
ATOM   3083 O  O   . ASP   B 1 33  ? 27.249  -3.719  -0.501  1 53.82 ? 18  ASP   B O   1 
ATOM   3084 C  CB  . ASP   B 1 33  ? 30.334  -4.17   -1.155  1 54.41 ? 18  ASP   B CB  1 
ATOM   3085 C  CG  . ASP   B 1 33  ? 31.15   -3.616  -0.009  1 56.14 ? 18  ASP   B CG  1 
ATOM   3086 O  OD1 . ASP   B 1 33  ? 31.967  -4.376  0.556   1 55.49 ? 18  ASP   B OD1 1 
ATOM   3087 O  OD2 . ASP   B 1 33  ? 30.95   -2.432  0.344   1 57.4  ? 18  ASP   B OD2 1 
ATOM   3088 N  N   . GLU   B 1 34  ? 28.263  -4.305  1.421   1 55.14 ? 19  GLU   B N   1 
ATOM   3089 C  CA  . GLU   B 1 34  ? 27.314  -3.587  2.276   1 55.8  ? 19  GLU   B CA  1 
ATOM   3090 C  C   . GLU   B 1 34  ? 27.314  -2.07   2.004   1 56.01 ? 19  GLU   B C   1 
ATOM   3091 O  O   . GLU   B 1 34  ? 26.274  -1.415  2.126   1 56.54 ? 19  GLU   B O   1 
ATOM   3092 C  CB  . GLU   B 1 34  ? 27.621  -3.86   3.759   1 57.8  ? 19  GLU   B CB  1 
ATOM   3093 N  N   . GLU   B 1 35  ? 28.47   -1.519  1.629   1 55.37 ? 20  GLU   B N   1 
ATOM   3094 C  CA  . GLU   B 1 35  ? 28.578  -0.089  1.371   1 55.27 ? 20  GLU   B CA  1 
ATOM   3095 C  C   . GLU   B 1 35  ? 28.415  0.313   -0.1    1 54.71 ? 20  GLU   B C   1 
ATOM   3096 O  O   . GLU   B 1 35  ? 27.711  1.277   -0.382  1 54.63 ? 20  GLU   B O   1 
ATOM   3097 C  CB  . GLU   B 1 35  ? 29.908  0.444   1.923   1 57.67 ? 20  GLU   B CB  1 
ATOM   3098 C  CG  . GLU   B 1 35  ? 30.044  1.953   1.847   1 62.8  ? 20  GLU   B CG  1 
ATOM   3099 C  CD  . GLU   B 1 35  ? 31.405  2.467   2.273   1 69.43 ? 20  GLU   B CD  1 
ATOM   3100 O  OE1 . GLU   B 1 35  ? 31.486  3.645   2.693   1 70.23 ? 20  GLU   B OE1 1 
ATOM   3101 O  OE2 . GLU   B 1 35  ? 32.39   1.694   2.19    1 71.26 ? 20  GLU   B OE2 1 
ATOM   3102 N  N   . VAL   B 1 36  ? 29.097  -0.375  -1.027  1 54.32 ? 21  VAL   B N   1 
ATOM   3103 C  CA  . VAL   B 1 36  ? 29.077  0.02    -2.435  1 54.41 ? 21  VAL   B CA  1 
ATOM   3104 C  C   . VAL   B 1 36  ? 28.226  -0.877  -3.35   1 54.49 ? 21  VAL   B C   1 
ATOM   3105 O  O   . VAL   B 1 36  ? 28.188  -0.619  -4.549  1 55.14 ? 21  VAL   B O   1 
ATOM   3106 C  CB  . VAL   B 1 36  ? 30.509  0.187   -3.007  1 54.82 ? 21  VAL   B CB  1 
ATOM   3107 C  CG1 . VAL   B 1 36  ? 31.293  1.221   -2.215  1 55.25 ? 21  VAL   B CG1 1 
ATOM   3108 C  CG2 . VAL   B 1 36  ? 31.253  -1.135  -3.041  1 54.92 ? 21  VAL   B CG2 1 
ATOM   3109 N  N   . GLY   B 1 37  ? 27.528  -1.865  -2.789  1 53.45 ? 22  GLY   B N   1 
ATOM   3110 C  CA  . GLY   B 1 37  ? 26.647  -2.764  -3.532  1 52.4  ? 22  GLY   B CA  1 
ATOM   3111 C  C   . GLY   B 1 37  ? 27.324  -3.601  -4.588  1 51.28 ? 22  GLY   B C   1 
ATOM   3112 O  O   . GLY   B 1 37  ? 28.219  -4.375  -4.283  1 50.97 ? 22  GLY   B O   1 
ATOM   3113 N  N   . PHE   B 1 38  ? 26.898  -3.46   -5.842  1 51.06 ? 23  PHE   B N   1 
ATOM   3114 C  CA  . PHE   B 1 38  ? 27.475  -4.211  -6.952  1 51.16 ? 23  PHE   B CA  1 
ATOM   3115 C  C   . PHE   B 1 38  ? 28.845  -3.68   -7.407  1 51.16 ? 23  PHE   B C   1 
ATOM   3116 O  O   . PHE   B 1 38  ? 29.546  -4.38   -8.143  1 51.07 ? 23  PHE   B O   1 
ATOM   3117 C  CB  . PHE   B 1 38  ? 26.503  -4.297  -8.128  1 51    ? 23  PHE   B CB  1 
ATOM   3118 C  CG  . PHE   B 1 38  ? 25.293  -5.141  -7.829  1 51.47 ? 23  PHE   B CG  1 
ATOM   3119 C  CD1 . PHE   B 1 38  ? 25.402  -6.509  -7.684  1 52.11 ? 23  PHE   B CD1 1 
ATOM   3120 C  CD2 . PHE   B 1 38  ? 24.043  -4.566  -7.7    1 52.45 ? 23  PHE   B CD2 1 
ATOM   3121 C  CE1 . PHE   B 1 38  ? 24.283  -7.29   -7.435  1 52.58 ? 23  PHE   B CE1 1 
ATOM   3122 C  CE2 . PHE   B 1 38  ? 22.925  -5.352  -7.439  1 52.96 ? 23  PHE   B CE2 1 
ATOM   3123 C  CZ  . PHE   B 1 38  ? 23.058  -6.702  -7.287  1 52.37 ? 23  PHE   B CZ  1 
ATOM   3124 N  N   . ALA   B 1 39  ? 29.236  -2.466  -6.964  1 50.51 ? 24  ALA   B N   1 
ATOM   3125 C  CA  . ALA   B 1 39  ? 30.55   -1.931  -7.277  1 50.71 ? 24  ALA   B CA  1 
ATOM   3126 C  C   . ALA   B 1 39  ? 31.641  -2.771  -6.601  1 51.35 ? 24  ALA   B C   1 
ATOM   3127 O  O   . ALA   B 1 39  ? 31.383  -3.467  -5.605  1 51.78 ? 24  ALA   B O   1 
ATOM   3128 C  CB  . ALA   B 1 39  ? 30.649  -0.486  -6.82   1 50.45 ? 24  ALA   B CB  1 
ATOM   3129 N  N   . LEU   B 1 40  ? 32.846  -2.745  -7.167  1 51.2  ? 25  LEU   B N   1 
ATOM   3130 C  CA  . LEU   B 1 40  ? 33.969  -3.469  -6.599  1 52.05 ? 25  LEU   B CA  1 
ATOM   3131 C  C   . LEU   B 1 40  ? 34.475  -2.612  -5.456  1 53.14 ? 25  LEU   B C   1 
ATOM   3132 O  O   . LEU   B 1 40  ? 34.83   -1.456  -5.685  1 53.59 ? 25  LEU   B O   1 
ATOM   3133 C  CB  . LEU   B 1 40  ? 35.058  -3.636  -7.663  1 52.48 ? 25  LEU   B CB  1 
ATOM   3134 C  CG  . LEU   B 1 40  ? 36.333  -4.337  -7.246  1 54.04 ? 25  LEU   B CG  1 
ATOM   3135 C  CD1 . LEU   B 1 40  ? 36.071  -5.8    -6.919  1 54.6  ? 25  LEU   B CD1 1 
ATOM   3136 C  CD2 . LEU   B 1 40  ? 37.352  -4.241  -8.336  1 54.65 ? 25  LEU   B CD2 1 
ATOM   3137 N  N   . PRO   B 1 41  ? 34.413  -3.102  -4.204  1 53.63 ? 26  PRO   B N   1 
ATOM   3138 C  CA  . PRO   B 1 41  ? 34.896  -2.274  -3.084  1 54.11 ? 26  PRO   B CA  1 
ATOM   3139 C  C   . PRO   B 1 41  ? 36.397  -2.035  -3.193  1 54.73 ? 26  PRO   B C   1 
ATOM   3140 O  O   . PRO   B 1 41  ? 37.123  -2.928  -3.618  1 54.13 ? 26  PRO   B O   1 
ATOM   3141 C  CB  . PRO   B 1 41  ? 34.538  -3.1    -1.844  1 54.51 ? 26  PRO   B CB  1 
ATOM   3142 C  CG  . PRO   B 1 41  ? 34.434  -4.508  -2.335  1 54.8  ? 26  PRO   B CG  1 
ATOM   3143 C  CD  . PRO   B 1 41  ? 33.989  -4.448  -3.76   1 53.03 ? 26  PRO   B CD  1 
ATOM   3144 N  N   . ASN   B 1 42  ? 36.855  -0.802  -2.874  1 55.82 ? 27  ASN   B N   1 
ATOM   3145 C  CA  . ASN   B 1 42  ? 38.268  -0.374  -2.909  1 57.27 ? 27  ASN   B CA  1 
ATOM   3146 C  C   . ASN   B 1 42  ? 39.103  -1.058  -4.015  1 57.34 ? 27  ASN   B C   1 
ATOM   3147 O  O   . ASN   B 1 42  ? 39.851  -1.997  -3.74   1 57.46 ? 27  ASN   B O   1 
ATOM   3148 C  CB  . ASN   B 1 42  ? 38.909  -0.562  -1.52   1 60.04 ? 27  ASN   B CB  1 
ATOM   3149 C  CG  . ASN   B 1 42  ? 40.352  -0.109  -1.445  1 66.34 ? 27  ASN   B CG  1 
ATOM   3150 O  OD1 . ASN   B 1 42  ? 40.748  0.908   -2.047  1 68.85 ? 27  ASN   B OD1 1 
ATOM   3151 N  ND2 . ASN   B 1 42  ? 41.177  -0.872  -0.73   1 67.65 ? 27  ASN   B ND2 1 
ATOM   3152 N  N   . PRO   B 1 43  ? 38.862  -0.697  -5.287  1 57.2  ? 28  PRO   B N   1 
ATOM   3153 C  CA  . PRO   B 1 43  ? 39.567  -1.373  -6.38   1 57.26 ? 28  PRO   B CA  1 
ATOM   3154 C  C   . PRO   B 1 43  ? 41.073  -1.134  -6.35   1 58.11 ? 28  PRO   B C   1 
ATOM   3155 O  O   . PRO   B 1 43  ? 41.525  -0.077  -5.888  1 57.28 ? 28  PRO   B O   1 
ATOM   3156 C  CB  . PRO   B 1 43  ? 38.924  -0.777  -7.64   1 57.37 ? 28  PRO   B CB  1 
ATOM   3157 C  CG  . PRO   B 1 43  ? 37.702  -0.076  -7.184  1 57.54 ? 28  PRO   B CG  1 
ATOM   3158 C  CD  . PRO   B 1 43  ? 37.971  0.361   -5.797  1 56.22 ? 28  PRO   B CD  1 
ATOM   3159 N  N   . GLN   B 1 44  ? 41.838  -2.115  -6.866  1 59.22 ? 29  GLN   B N   1 
ATOM   3160 C  CA  . GLN   B 1 44  ? 43.295  -2.051  -6.962  1 61.22 ? 29  GLN   B CA  1 
ATOM   3161 C  C   . GLN   B 1 44  ? 43.689  -0.988  -8      1 62.76 ? 29  GLN   B C   1 
ATOM   3162 O  O   . GLN   B 1 44  ? 43.071  -0.926  -9.065  1 63.15 ? 29  GLN   B O   1 
ATOM   3163 C  CB  . GLN   B 1 44  ? 43.838  -3.427  -7.385  1 63.52 ? 29  GLN   B CB  1 
ATOM   3164 C  CG  . GLN   B 1 44  ? 45.292  -3.684  -6.982  1 68.2  ? 29  GLN   B CG  1 
ATOM   3165 C  CD  . GLN   B 1 44  ? 45.684  -5.114  -7.269  1 72.89 ? 29  GLN   B CD  1 
ATOM   3166 O  OE1 . GLN   B 1 44  ? 45.018  -6.062  -6.846  1 74.34 ? 29  GLN   B OE1 1 
ATOM   3167 N  NE2 . GLN   B 1 44  ? 46.769  -5.308  -8.004  1 73.54 ? 29  GLN   B NE2 1 
ATOM   3168 N  N   . GLU   B 1 45  ? 44.688  -0.137  -7.689  1 63.45 ? 30  GLU   B N   1 
ATOM   3169 C  CA  . GLU   B 1 45  ? 45.126  0.905   -8.625  1 64.5  ? 30  GLU   B CA  1 
ATOM   3170 C  C   . GLU   B 1 45  ? 46.344  0.472   -9.431  1 65.32 ? 30  GLU   B C   1 
ATOM   3171 O  O   . GLU   B 1 45  ? 46.479  0.846   -10.596 1 65.8  ? 30  GLU   B O   1 
ATOM   3172 C  CB  . GLU   B 1 45  ? 45.457  2.213   -7.886  1 66.98 ? 30  GLU   B CB  1 
ATOM   3173 C  CG  . GLU   B 1 45  ? 44.389  2.653   -6.906  1 73.49 ? 30  GLU   B CG  1 
ATOM   3174 C  CD  . GLU   B 1 45  ? 44.685  3.958   -6.192  1 82.64 ? 30  GLU   B CD  1 
ATOM   3175 O  OE1 . GLU   B 1 45  ? 45.541  4.729   -6.69   1 84.66 ? 30  GLU   B OE1 1 
ATOM   3176 O  OE2 . GLU   B 1 45  ? 44.053  4.214   -5.139  1 85.14 ? 30  GLU   B OE2 1 
ATOM   3177 N  N   . ASN   B 1 46  ? 47.243  -0.301  -8.812  1 65.54 ? 31  ASN   B N   1 
ATOM   3178 C  CA  . ASN   B 1 46  ? 48.471  -0.723  -9.482  1 66.1  ? 31  ASN   B CA  1 
ATOM   3179 C  C   . ASN   B 1 46  ? 48.556  -2.229  -9.641  1 66.24 ? 31  ASN   B C   1 
ATOM   3180 O  O   . ASN   B 1 46  ? 48.128  -2.964  -8.765  1 66.21 ? 31  ASN   B O   1 
ATOM   3181 C  CB  . ASN   B 1 46  ? 49.698  -0.192  -8.728  1 67.35 ? 31  ASN   B CB  1 
ATOM   3182 C  CG  . ASN   B 1 46  ? 49.59   1.268   -8.345  1 71.29 ? 31  ASN   B CG  1 
ATOM   3183 O  OD1 . ASN   B 1 46  ? 49.677  2.172   -9.184  1 72.92 ? 31  ASN   B OD1 1 
ATOM   3184 N  ND2 . ASN   B 1 46  ? 49.37   1.538   -7.067  1 72.46 ? 31  ASN   B ND2 1 
ATOM   3185 N  N   . LEU   B 1 47  ? 49.083  -2.687  -10.772 1 66.42 ? 32  LEU   B N   1 
ATOM   3186 C  CA  . LEU   B 1 47  ? 49.274  -4.11   -11.056 1 67.21 ? 32  LEU   B CA  1 
ATOM   3187 C  C   . LEU   B 1 47  ? 50.702  -4.526  -10.609 1 68.11 ? 32  LEU   B C   1 
ATOM   3188 O  O   . LEU   B 1 47  ? 51.566  -3.655  -10.451 1 68.46 ? 32  LEU   B O   1 
ATOM   3189 C  CB  . LEU   B 1 47  ? 49.156  -4.338  -12.587 1 67.3  ? 32  LEU   B CB  1 
ATOM   3190 C  CG  . LEU   B 1 47  ? 47.77   -4.44   -13.205 1 68.71 ? 32  LEU   B CG  1 
ATOM   3191 C  CD1 . LEU   B 1 47  ? 47.866  -4.753  -14.701 1 68.89 ? 32  LEU   B CD1 1 
ATOM   3192 C  CD2 . LEU   B 1 47  ? 46.934  -5.496  -12.515 1 69.6  ? 32  LEU   B CD2 1 
ATOM   3193 N  N   . PRO   B 1 48  ? 51.02   -5.843  -10.492 1 68.24 ? 33  PRO   B N   1 
ATOM   3194 C  CA  . PRO   B 1 48  ? 52.419  -6.231  -10.217 1 68.64 ? 33  PRO   B CA  1 
ATOM   3195 C  C   . PRO   B 1 48  ? 53.363  -5.68   -11.305 1 68.74 ? 33  PRO   B C   1 
ATOM   3196 O  O   . PRO   B 1 48  ? 52.948  -5.568  -12.461 1 69.04 ? 33  PRO   B O   1 
ATOM   3197 C  CB  . PRO   B 1 48  ? 52.377  -7.77   -10.261 1 69.33 ? 33  PRO   B CB  1 
ATOM   3198 C  CG  . PRO   B 1 48  ? 50.95   -8.128  -10.026 1 69.5  ? 33  PRO   B CG  1 
ATOM   3199 C  CD  . PRO   B 1 48  ? 50.157  -7.029  -10.667 1 67.71 ? 33  PRO   B CD  1 
ATOM   3200 N  N   . ASP   B 1 49  ? 54.601  -5.3    -10.927 1 68.19 ? 34  ASP   B N   1 
ATOM   3201 C  CA  . ASP   B 1 49  ? 55.622  -4.72   -11.809 1 68.22 ? 34  ASP   B CA  1 
ATOM   3202 C  C   . ASP   B 1 49  ? 55.813  -5.464  -13.139 1 67.8  ? 34  ASP   B C   1 
ATOM   3203 O  O   . ASP   B 1 49  ? 56.227  -4.856  -14.122 1 67.86 ? 34  ASP   B O   1 
ATOM   3204 C  CB  . ASP   B 1 49  ? 56.966  -4.575  -11.069 1 69.92 ? 34  ASP   B CB  1 
ATOM   3205 N  N   . PHE   B 1 50  ? 55.49   -6.761  -13.178 1 67.38 ? 35  PHE   B N   1 
ATOM   3206 C  CA  . PHE   B 1 50  ? 55.569  -7.578  -14.391 1 67.74 ? 35  PHE   B CA  1 
ATOM   3207 C  C   . PHE   B 1 50  ? 54.702  -6.998  -15.529 1 68.16 ? 35  PHE   B C   1 
ATOM   3208 O  O   . PHE   B 1 50  ? 55.02   -7.179  -16.706 1 68.74 ? 35  PHE   B O   1 
ATOM   3209 C  CB  . PHE   B 1 50  ? 55.104  -9.008  -14.056 1 67.71 ? 35  PHE   B CB  1 
ATOM   3210 C  CG  . PHE   B 1 50  ? 55.126  -10.022 -15.177 1 68.47 ? 35  PHE   B CG  1 
ATOM   3211 C  CD1 . PHE   B 1 50  ? 56.258  -10.774 -15.429 1 69.36 ? 35  PHE   B CD1 1 
ATOM   3212 C  CD2 . PHE   B 1 50  ? 53.984  -10.297 -15.908 1 69.46 ? 35  PHE   B CD2 1 
ATOM   3213 C  CE1 . PHE   B 1 50  ? 56.266  -11.734 -16.439 1 70.1  ? 35  PHE   B CE1 1 
ATOM   3214 C  CE2 . PHE   B 1 50  ? 53.997  -11.249 -16.923 1 70.32 ? 35  PHE   B CE2 1 
ATOM   3215 C  CZ  . PHE   B 1 50  ? 55.139  -11.959 -17.184 1 70.02 ? 35  PHE   B CZ  1 
ATOM   3216 N  N   . TYR   B 1 51  ? 53.61   -6.301  -15.178 1 67.7  ? 36  TYR   B N   1 
ATOM   3217 C  CA  . TYR   B 1 51  ? 52.678  -5.733  -16.146 1 67.72 ? 36  TYR   B CA  1 
ATOM   3218 C  C   . TYR   B 1 51  ? 52.844  -4.24   -16.375 1 67.28 ? 36  TYR   B C   1 
ATOM   3219 O  O   . TYR   B 1 51  ? 51.915  -3.615  -16.885 1 67.31 ? 36  TYR   B O   1 
ATOM   3220 C  CB  . TYR   B 1 51  ? 51.24   -6.015  -15.698 1 67.76 ? 36  TYR   B CB  1 
ATOM   3221 C  CG  . TYR   B 1 51  ? 50.946  -7.491  -15.592 1 68.04 ? 36  TYR   B CG  1 
ATOM   3222 C  CD1 . TYR   B 1 51  ? 50.743  -8.261  -16.727 1 68.64 ? 36  TYR   B CD1 1 
ATOM   3223 C  CD2 . TYR   B 1 51  ? 50.914  -8.126  -14.36  1 68.67 ? 36  TYR   B CD2 1 
ATOM   3224 C  CE1 . TYR   B 1 51  ? 50.458  -9.614  -16.64  1 69.55 ? 36  TYR   B CE1 1 
ATOM   3225 C  CE2 . TYR   B 1 51  ? 50.668  -9.488  -14.262 1 69.46 ? 36  TYR   B CE2 1 
ATOM   3226 C  CZ  . TYR   B 1 51  ? 50.419  -10.226 -15.405 1 70.46 ? 36  TYR   B CZ  1 
ATOM   3227 O  OH  . TYR   B 1 51  ? 50.16   -11.578 -15.348 1 72.2  ? 36  TYR   B OH  1 
ATOM   3228 N  N   . ASN   B 1 52  ? 54.014  -3.669  -16.023 1 66.5  ? 37  ASN   B N   1 
ATOM   3229 C  CA  . ASN   B 1 52  ? 54.304  -2.242  -16.19  1 66.01 ? 37  ASN   B CA  1 
ATOM   3230 C  C   . ASN   B 1 52  ? 54.085  -1.746  -17.622 1 64.85 ? 37  ASN   B C   1 
ATOM   3231 O  O   . ASN   B 1 52  ? 53.716  -0.587  -17.811 1 64.59 ? 37  ASN   B O   1 
ATOM   3232 C  CB  . ASN   B 1 52  ? 55.732  -1.921  -15.738 1 67.48 ? 37  ASN   B CB  1 
ATOM   3233 C  CG  . ASN   B 1 52  ? 55.899  -1.777  -14.247 1 71.29 ? 37  ASN   B CG  1 
ATOM   3234 O  OD1 . ASN   B 1 52  ? 54.955  -1.471  -13.504 1 72.64 ? 37  ASN   B OD1 1 
ATOM   3235 N  ND2 . ASN   B 1 52  ? 57.114  -1.999  -13.774 1 72.02 ? 37  ASN   B ND2 1 
ATOM   3236 N  N   . ASP   B 1 53  ? 54.31   -2.615  -18.622 1 64.12 ? 38  ASP   B N   1 
ATOM   3237 C  CA  . ASP   B 1 53  ? 54.137  -2.268  -20.029 1 64.07 ? 38  ASP   B CA  1 
ATOM   3238 C  C   . ASP   B 1 53  ? 52.659  -2.074  -20.397 1 64.08 ? 38  ASP   B C   1 
ATOM   3239 O  O   . ASP   B 1 53  ? 52.345  -1.251  -21.258 1 64.63 ? 38  ASP   B O   1 
ATOM   3240 C  CB  . ASP   B 1 53  ? 54.806  -3.313  -20.934 1 65.14 ? 38  ASP   B CB  1 
ATOM   3241 C  CG  . ASP   B 1 53  ? 56.326  -3.272  -20.908 1 68.55 ? 38  ASP   B CG  1 
ATOM   3242 O  OD1 . ASP   B 1 53  ? 56.889  -2.244  -20.451 1 68.55 ? 38  ASP   B OD1 1 
ATOM   3243 O  OD2 . ASP   B 1 53  ? 56.953  -4.263  -21.355 1 69.98 ? 38  ASP   B OD2 1 
ATOM   3244 N  N   . TRP   B 1 54  ? 51.757  -2.825  -19.747 1 63.03 ? 39  TRP   B N   1 
ATOM   3245 C  CA  . TRP   B 1 54  ? 50.321  -2.662  -19.956 1 62.49 ? 39  TRP   B CA  1 
ATOM   3246 C  C   . TRP   B 1 54  ? 49.893  -1.363  -19.273 1 62.49 ? 39  TRP   B C   1 
ATOM   3247 O  O   . TRP   B 1 54  ? 49.202  -0.545  -19.874 1 62.68 ? 39  TRP   B O   1 
ATOM   3248 C  CB  . TRP   B 1 54  ? 49.544  -3.831  -19.317 1 61.89 ? 39  TRP   B CB  1 
ATOM   3249 C  CG  . TRP   B 1 54  ? 49.615  -5.151  -20.019 1 61.75 ? 39  TRP   B CG  1 
ATOM   3250 C  CD1 . TRP   B 1 54  ? 50.278  -5.45   -21.175 1 62.49 ? 39  TRP   B CD1 1 
ATOM   3251 C  CD2 . TRP   B 1 54  ? 48.977  -6.357  -19.6   1 61.72 ? 39  TRP   B CD2 1 
ATOM   3252 N  NE1 . TRP   B 1 54  ? 50.088  -6.772  -21.501 1 62.73 ? 39  TRP   B NE1 1 
ATOM   3253 C  CE2 . TRP   B 1 54  ? 49.292  -7.353  -20.548 1 62.44 ? 39  TRP   B CE2 1 
ATOM   3254 C  CE3 . TRP   B 1 54  ? 48.147  -6.688  -18.523 1 62.2  ? 39  TRP   B CE3 1 
ATOM   3255 C  CZ2 . TRP   B 1 54  ? 48.792  -8.65   -20.459 1 63.06 ? 39  TRP   B CZ2 1 
ATOM   3256 C  CZ3 . TRP   B 1 54  ? 47.676  -7.981  -18.422 1 62.93 ? 39  TRP   B CZ3 1 
ATOM   3257 C  CH2 . TRP   B 1 54  ? 47.998  -8.944  -19.383 1 63.13 ? 39  TRP   B CH2 1 
ATOM   3258 N  N   . MET   B 1 55  ? 50.322  -1.174  -18.013 1 62.21 ? 40  MET   B N   1 
ATOM   3259 C  CA  . MET   B 1 55  ? 49.978  -0.017  -17.201 1 62.68 ? 40  MET   B CA  1 
ATOM   3260 C  C   . MET   B 1 55  ? 50.44   1.302   -17.798 1 62.73 ? 40  MET   B C   1 
ATOM   3261 O  O   . MET   B 1 55  ? 49.729  2.302   -17.672 1 62.66 ? 40  MET   B O   1 
ATOM   3262 C  CB  . MET   B 1 55  ? 50.485  -0.189  -15.757 1 63.43 ? 40  MET   B CB  1 
ATOM   3263 C  CG  . MET   B 1 55  ? 49.741  0.66    -14.746 1 66.41 ? 40  MET   B CG  1 
ATOM   3264 S  SD  . MET   B 1 55  ? 47.938  0.354   -14.695 1 72.6  ? 40  MET   B SD  1 
ATOM   3265 C  CE  . MET   B 1 55  ? 47.826  -0.713  -13.39  1 72.38 ? 40  MET   B CE  1 
ATOM   3266 N  N   . PHE   B 1 56  ? 51.616  1.315   -18.458 1 62.62 ? 41  PHE   B N   1 
ATOM   3267 C  CA  . PHE   B 1 56  ? 52.109  2.54    -19.079 1 62.56 ? 41  PHE   B CA  1 
ATOM   3268 C  C   . PHE   B 1 56  ? 51.148  3       -20.193 1 61.54 ? 41  PHE   B C   1 
ATOM   3269 O  O   . PHE   B 1 56  ? 50.807  4.18    -20.267 1 61.4  ? 41  PHE   B O   1 
ATOM   3270 C  CB  . PHE   B 1 56  ? 53.561  2.375   -19.599 1 62.97 ? 41  PHE   B CB  1 
ATOM   3271 C  CG  . PHE   B 1 56  ? 53.985  3.537   -20.466 1 64.19 ? 41  PHE   B CG  1 
ATOM   3272 C  CD1 . PHE   B 1 56  ? 54.294  4.765   -19.902 1 65.04 ? 41  PHE   B CD1 1 
ATOM   3273 C  CD2 . PHE   B 1 56  ? 53.934  3.444   -21.851 1 65.3  ? 41  PHE   B CD2 1 
ATOM   3274 C  CE1 . PHE   B 1 56  ? 54.597  5.858   -20.702 1 65.98 ? 41  PHE   B CE1 1 
ATOM   3275 C  CE2 . PHE   B 1 56  ? 54.223  4.544   -22.649 1 66.2  ? 41  PHE   B CE2 1 
ATOM   3276 C  CZ  . PHE   B 1 56  ? 54.561  5.741   -22.07  1 66.05 ? 41  PHE   B CZ  1 
ATOM   3277 N  N   . ILE   B 1 57  ? 50.732  2.071   -21.058 1 60.86 ? 42  ILE   B N   1 
ATOM   3278 C  CA  . ILE   B 1 57  ? 49.818  2.389   -22.15  1 60.53 ? 42  ILE   B CA  1 
ATOM   3279 C  C   . ILE   B 1 57  ? 48.466  2.887   -21.615 1 60.53 ? 42  ILE   B C   1 
ATOM   3280 O  O   . ILE   B 1 57  ? 48.035  3.983   -21.981 1 61.04 ? 42  ILE   B O   1 
ATOM   3281 C  CB  . ILE   B 1 57  ? 49.675  1.184   -23.108 1 60.34 ? 42  ILE   B CB  1 
ATOM   3282 C  CG1 . ILE   B 1 57  ? 51.054  0.765   -23.67  1 60.47 ? 42  ILE   B CG1 1 
ATOM   3283 C  CG2 . ILE   B 1 57  ? 48.669  1.498   -24.214 1 60.7  ? 42  ILE   B CG2 1 
ATOM   3284 C  CD1 . ILE   B 1 57  ? 51.048  -0.417  -24.655 1 61.24 ? 42  ILE   B CD1 1 
ATOM   3285 N  N   . ALA   B 1 58  ? 47.848  2.121   -20.691 1 59.68 ? 43  ALA   B N   1 
ATOM   3286 C  CA  . ALA   B 1 58  ? 46.566  2.456   -20.059 1 59.28 ? 43  ALA   B CA  1 
ATOM   3287 C  C   . ALA   B 1 58  ? 46.574  3.82    -19.345 1 58.74 ? 43  ALA   B C   1 
ATOM   3288 O  O   . ALA   B 1 58  ? 45.629  4.603   -19.483 1 58.64 ? 43  ALA   B O   1 
ATOM   3289 C  CB  . ALA   B 1 58  ? 46.168  1.359   -19.089 1 59.38 ? 43  ALA   B CB  1 
ATOM   3290 N  N   . LYS   B 1 59  ? 47.65   4.117   -18.611 1 58.25 ? 44  LYS   B N   1 
ATOM   3291 C  CA  . LYS   B 1 59  ? 47.771  5.389   -17.905 1 58.38 ? 44  LYS   B CA  1 
ATOM   3292 C  C   . LYS   B 1 59  ? 48.031  6.579   -18.83  1 58.31 ? 44  LYS   B C   1 
ATOM   3293 O  O   . LYS   B 1 59  ? 47.855  7.719   -18.407 1 58.51 ? 44  LYS   B O   1 
ATOM   3294 C  CB  . LYS   B 1 59  ? 48.876  5.311   -16.842 1 60.37 ? 44  LYS   B CB  1 
ATOM   3295 N  N   . HIS   B 1 60  ? 48.465  6.333   -20.075 1 58.25 ? 45  HIS   B N   1 
ATOM   3296 C  CA  . HIS   B 1 60  ? 48.768  7.418   -21.002 1 58.47 ? 45  HIS   B CA  1 
ATOM   3297 C  C   . HIS   B 1 60  ? 47.93   7.379   -22.27  1 57.68 ? 45  HIS   B C   1 
ATOM   3298 O  O   . HIS   B 1 60  ? 48.403  7.836   -23.313 1 58.22 ? 45  HIS   B O   1 
ATOM   3299 C  CB  . HIS   B 1 60  ? 50.282  7.45    -21.32  1 59.5  ? 45  HIS   B CB  1 
ATOM   3300 C  CG  . HIS   B 1 60  ? 51.119  7.696   -20.105 1 62.15 ? 45  HIS   B CG  1 
ATOM   3301 N  ND1 . HIS   B 1 60  ? 51.548  6.653   -19.298 1 64.18 ? 45  HIS   B ND1 1 
ATOM   3302 C  CD2 . HIS   B 1 60  ? 51.512  8.867   -19.552 1 63.33 ? 45  HIS   B CD2 1 
ATOM   3303 C  CE1 . HIS   B 1 60  ? 52.21   7.219   -18.302 1 64.71 ? 45  HIS   B CE1 1 
ATOM   3304 N  NE2 . HIS   B 1 60  ? 52.225  8.549   -18.417 1 64.57 ? 45  HIS   B NE2 1 
ATOM   3305 N  N   . LEU   B 1 61  ? 46.683  6.862   -22.191 1 55.93 ? 46  LEU   B N   1 
ATOM   3306 C  CA  . LEU   B 1 61  ? 45.816  6.817   -23.368 1 54.64 ? 46  LEU   B CA  1 
ATOM   3307 C  C   . LEU   B 1 61  ? 45.602  8.205   -24.003 1 53.59 ? 46  LEU   B C   1 
ATOM   3308 O  O   . LEU   B 1 61  ? 45.819  8.33    -25.21  1 53.03 ? 46  LEU   B O   1 
ATOM   3309 C  CB  . LEU   B 1 61  ? 44.467  6.113   -23.122 1 54.45 ? 46  LEU   B CB  1 
ATOM   3310 C  CG  . LEU   B 1 61  ? 44.472  4.6     -22.888 1 55.81 ? 46  LEU   B CG  1 
ATOM   3311 C  CD1 . LEU   B 1 61  ? 43.053  4.065   -22.813 1 56.35 ? 46  LEU   B CD1 1 
ATOM   3312 C  CD2 . LEU   B 1 61  ? 45.167  3.87    -23.991 1 56.24 ? 46  LEU   B CD2 1 
ATOM   3313 N  N   . PRO   B 1 62  ? 45.237  9.269   -23.239 1 52.86 ? 47  PRO   B N   1 
ATOM   3314 C  CA  . PRO   B 1 62  ? 45.033  10.58   -23.877 1 52.65 ? 47  PRO   B CA  1 
ATOM   3315 C  C   . PRO   B 1 62  ? 46.216  11.047  -24.739 1 53.36 ? 47  PRO   B C   1 
ATOM   3316 O  O   . PRO   B 1 62  ? 46.008  11.404  -25.897 1 53.89 ? 47  PRO   B O   1 
ATOM   3317 C  CB  . PRO   B 1 62  ? 44.748  11.504  -22.689 1 52.9  ? 47  PRO   B CB  1 
ATOM   3318 C  CG  . PRO   B 1 62  ? 44.137  10.606  -21.669 1 53.19 ? 47  PRO   B CG  1 
ATOM   3319 C  CD  . PRO   B 1 62  ? 44.922  9.329   -21.794 1 51.99 ? 47  PRO   B CD  1 
ATOM   3320 N  N   . ASP   B 1 63  ? 47.454  10.942  -24.215 1 53.08 ? 48  ASP   B N   1 
ATOM   3321 C  CA  . ASP   B 1 63  ? 48.675  11.345  -24.919 1 53.21 ? 48  ASP   B CA  1 
ATOM   3322 C  C   . ASP   B 1 63  ? 49.03   10.443  -26.077 1 53.38 ? 48  ASP   B C   1 
ATOM   3323 O  O   . ASP   B 1 63  ? 49.343  10.955  -27.142 1 53.86 ? 48  ASP   B O   1 
ATOM   3324 C  CB  . ASP   B 1 63  ? 49.87   11.464  -23.954 1 54.41 ? 48  ASP   B CB  1 
ATOM   3325 N  N   . LEU   B 1 64  ? 49      9.117   -25.885 1 53.19 ? 49  LEU   B N   1 
ATOM   3326 C  CA  . LEU   B 1 64  ? 49.355  8.171   -26.947 1 53.51 ? 49  LEU   B CA  1 
ATOM   3327 C  C   . LEU   B 1 64  ? 48.363  8.198   -28.094 1 54.04 ? 49  LEU   B C   1 
ATOM   3328 O  O   . LEU   B 1 64  ? 48.757  7.979   -29.238 1 54.28 ? 49  LEU   B O   1 
ATOM   3329 C  CB  . LEU   B 1 64  ? 49.461  6.74    -26.395 1 53.55 ? 49  LEU   B CB  1 
ATOM   3330 C  CG  . LEU   B 1 64  ? 50.56   6.501   -25.37  1 54.6  ? 49  LEU   B CG  1 
ATOM   3331 C  CD1 . LEU   B 1 64  ? 50.398  5.141   -24.696 1 54.69 ? 49  LEU   B CD1 1 
ATOM   3332 C  CD2 . LEU   B 1 64  ? 51.937  6.628   -26.004 1 55.19 ? 49  LEU   B CD2 1 
ATOM   3333 N  N   . ILE   B 1 65  ? 47.074  8.425   -27.799 1 54.09 ? 50  ILE   B N   1 
ATOM   3334 C  CA  . ILE   B 1 65  ? 46.057  8.457   -28.839 1 54.45 ? 50  ILE   B CA  1 
ATOM   3335 C  C   . ILE   B 1 65  ? 46.253  9.701   -29.687 1 55.16 ? 50  ILE   B C   1 
ATOM   3336 O  O   . ILE   B 1 65  ? 46.356  9.594   -30.911 1 55.59 ? 50  ILE   B O   1 
ATOM   3337 C  CB  . ILE   B 1 65  ? 44.598  8.369   -28.286 1 54.57 ? 50  ILE   B CB  1 
ATOM   3338 C  CG1 . ILE   B 1 65  ? 44.292  7.005   -27.66  1 55.16 ? 50  ILE   B CG1 1 
ATOM   3339 C  CG2 . ILE   B 1 65  ? 43.577  8.695   -29.381 1 54.73 ? 50  ILE   B CG2 1 
ATOM   3340 C  CD1 . ILE   B 1 65  ? 43.007  7.034   -26.828 1 56.03 ? 50  ILE   B CD1 1 
ATOM   3341 N  N   . GLU   B 1 66  ? 46.298  10.876  -29.035 1 55.08 ? 51  GLU   B N   1 
ATOM   3342 C  CA  . GLU   B 1 66  ? 46.448  12.165  -29.699 1 55.8  ? 51  GLU   B CA  1 
ATOM   3343 C  C   . GLU   B 1 66  ? 47.681  12.213  -30.61  1 56.22 ? 51  GLU   B C   1 
ATOM   3344 O  O   . GLU   B 1 66  ? 47.608  12.744  -31.719 1 56.43 ? 51  GLU   B O   1 
ATOM   3345 C  CB  . GLU   B 1 66  ? 46.511  13.293  -28.658 1 58.13 ? 51  GLU   B CB  1 
ATOM   3346 C  CG  . GLU   B 1 66  ? 46.401  14.688  -29.25  1 63.15 ? 51  GLU   B CG  1 
ATOM   3347 C  CD  . GLU   B 1 66  ? 47.709  15.299  -29.729 1 70.81 ? 51  GLU   B CD  1 
ATOM   3348 O  OE1 . GLU   B 1 66  ? 48.787  14.864  -29.257 1 71.63 ? 51  GLU   B OE1 1 
ATOM   3349 O  OE2 . GLU   B 1 66  ? 47.653  16.201  -30.595 1 73.87 ? 51  GLU   B OE2 1 
ATOM   3350 N  N   . SER   B 1 67  ? 48.808  11.663  -30.135 1 55.92 ? 52  SER   B N   1 
ATOM   3351 C  CA  . SER   B 1 67  ? 50.061  11.666  -30.87  1 55.85 ? 52  SER   B CA  1 
ATOM   3352 C  C   . SER   B 1 67  ? 50.205  10.567  -31.921 1 56.54 ? 52  SER   B C   1 
ATOM   3353 O  O   . SER   B 1 67  ? 51.217  10.533  -32.603 1 57.39 ? 52  SER   B O   1 
ATOM   3354 C  CB  . SER   B 1 67  ? 51.234  11.61   -29.904 1 56.26 ? 52  SER   B CB  1 
ATOM   3355 O  OG  . SER   B 1 67  ? 51.351  10.315  -29.345 1 58.23 ? 52  SER   B OG  1 
ATOM   3356 N  N   . GLY   B 1 68  ? 49.233  9.674   -32.037 1 56.03 ? 53  GLY   B N   1 
ATOM   3357 C  CA  . GLY   B 1 68  ? 49.295  8.586   -33.003 1 56.19 ? 53  GLY   B CA  1 
ATOM   3358 C  C   . GLY   B 1 68  ? 50.298  7.506   -32.651 1 56.67 ? 53  GLY   B C   1 
ATOM   3359 O  O   . GLY   B 1 68  ? 50.654  6.687   -33.502 1 56.39 ? 53  GLY   B O   1 
ATOM   3360 N  N   . GLN   B 1 69  ? 50.734  7.466   -31.381 1 57.15 ? 54  GLN   B N   1 
ATOM   3361 C  CA  . GLN   B 1 69  ? 51.717  6.503   -30.886 1 58.06 ? 54  GLN   B CA  1 
ATOM   3362 C  C   . GLN   B 1 69  ? 51.114  5.268   -30.242 1 58.27 ? 54  GLN   B C   1 
ATOM   3363 O  O   . GLN   B 1 69  ? 51.853  4.331   -29.958 1 58.7  ? 54  GLN   B O   1 
ATOM   3364 C  CB  . GLN   B 1 69  ? 52.609  7.172   -29.839 1 60.25 ? 54  GLN   B CB  1 
ATOM   3365 C  CG  . GLN   B 1 69  ? 53.624  8.145   -30.404 1 65.41 ? 54  GLN   B CG  1 
ATOM   3366 C  CD  . GLN   B 1 69  ? 54.916  8.042   -29.634 1 72.28 ? 54  GLN   B CD  1 
ATOM   3367 O  OE1 . GLN   B 1 69  ? 54.939  8.135   -28.399 1 74.88 ? 54  GLN   B OE1 1 
ATOM   3368 N  NE2 . GLN   B 1 69  ? 56.031  7.857   -30.335 1 73.26 ? 54  GLN   B NE2 1 
ATOM   3369 N  N   . LEU   B 1 70  ? 49.804  5.277   -29.948 1 57.48 ? 55  LEU   B N   1 
ATOM   3370 C  CA  . LEU   B 1 70  ? 49.163  4.183   -29.24  1 56.81 ? 55  LEU   B CA  1 
ATOM   3371 C  C   . LEU   B 1 70  ? 49.205  2.842   -29.971 1 56.16 ? 55  LEU   B C   1 
ATOM   3372 O  O   . LEU   B 1 70  ? 49.573  1.84    -29.355 1 56.15 ? 55  LEU   B O   1 
ATOM   3373 C  CB  . LEU   B 1 70  ? 47.723  4.538   -28.844 1 56.91 ? 55  LEU   B CB  1 
ATOM   3374 C  CG  . LEU   B 1 70  ? 47.056  3.425   -28.066 1 58.01 ? 55  LEU   B CG  1 
ATOM   3375 C  CD1 . LEU   B 1 70  ? 46.994  3.719   -26.622 1 58.43 ? 55  LEU   B CD1 1 
ATOM   3376 C  CD2 . LEU   B 1 70  ? 45.847  2.94    -28.738 1 58.3  ? 55  LEU   B CD2 1 
ATOM   3377 N  N   . ARG   B 1 71  ? 48.762  2.793   -31.233 1 55.57 ? 56  ARG   B N   1 
ATOM   3378 C  CA  . ARG   B 1 71  ? 48.751  1.539   -31.983 1 55.62 ? 56  ARG   B CA  1 
ATOM   3379 C  C   . ARG   B 1 71  ? 50.138  0.88    -32.059 1 56.61 ? 56  ARG   B C   1 
ATOM   3380 O  O   . ARG   B 1 71  ? 50.236  -0.333  -31.888 1 56.47 ? 56  ARG   B O   1 
ATOM   3381 C  CB  . ARG   B 1 71  ? 48.116  1.743   -33.36  1 55.27 ? 56  ARG   B CB  1 
ATOM   3382 C  CG  . ARG   B 1 71  ? 46.614  1.934   -33.221 1 55.59 ? 56  ARG   B CG  1 
ATOM   3383 C  CD  . ARG   B 1 71  ? 45.928  2.317   -34.507 1 56.23 ? 56  ARG   B CD  1 
ATOM   3384 N  NE  . ARG   B 1 71  ? 44.479  2.175   -34.393 1 57.43 ? 56  ARG   B NE  1 
ATOM   3385 C  CZ  . ARG   B 1 71  ? 43.592  2.854   -35.114 1 58.19 ? 56  ARG   B CZ  1 
ATOM   3386 N  NH1 . ARG   B 1 71  ? 43.995  3.74    -36.017 1 58.14 ? 56  ARG   B NH1 1 
ATOM   3387 N  NH2 . ARG   B 1 71  ? 42.295  2.649   -34.94  1 56.94 ? 56  ARG   B NH2 1 
ATOM   3388 N  N   . GLU   B 1 72  ? 51.201  1.696   -32.179 1 57.55 ? 57  GLU   B N   1 
ATOM   3389 C  CA  . GLU   B 1 72  ? 52.581  1.226   -32.201 1 59.39 ? 57  GLU   B CA  1 
ATOM   3390 C  C   . GLU   B 1 72  ? 53.009  0.627   -30.857 1 60.13 ? 57  GLU   B C   1 
ATOM   3391 O  O   . GLU   B 1 72  ? 53.618  -0.44   -30.852 1 60.49 ? 57  GLU   B O   1 
ATOM   3392 C  CB  . GLU   B 1 72  ? 53.555  2.347   -32.64  1 63.23 ? 57  GLU   B CB  1 
ATOM   3393 C  CG  . GLU   B 1 72  ? 53.692  2.482   -34.149 1 71.34 ? 57  GLU   B CG  1 
ATOM   3394 C  CD  . GLU   B 1 72  ? 55.111  2.612   -34.672 1 82.7  ? 57  GLU   B CD  1 
ATOM   3395 O  OE1 . GLU   B 1 72  ? 55.92   3.32    -34.027 1 85.67 ? 57  GLU   B OE1 1 
ATOM   3396 O  OE2 . GLU   B 1 72  ? 55.411  2.013   -35.733 1 85.55 ? 57  GLU   B OE2 1 
ATOM   3397 N  N   . ARG   B 1 73  ? 52.666  1.28    -29.723 1 60.09 ? 58  ARG   B N   1 
ATOM   3398 C  CA  . ARG   B 1 73  ? 52.997  0.773   -28.386 1 60.65 ? 58  ARG   B CA  1 
ATOM   3399 C  C   . ARG   B 1 73  ? 52.309  -0.572  -28.114 1 61.67 ? 58  ARG   B C   1 
ATOM   3400 O  O   . ARG   B 1 73  ? 52.888  -1.455  -27.475 1 61.9  ? 58  ARG   B O   1 
ATOM   3401 C  CB  . ARG   B 1 73  ? 52.616  1.789   -27.307 1 61.37 ? 58  ARG   B CB  1 
ATOM   3402 N  N   . VAL   B 1 74  ? 51.086  -0.733  -28.615 1 61.98 ? 59  VAL   B N   1 
ATOM   3403 C  CA  . VAL   B 1 74  ? 50.349  -1.976  -28.454 1 62.99 ? 59  VAL   B CA  1 
ATOM   3404 C  C   . VAL   B 1 74  ? 51      -3.058  -29.325 1 64.23 ? 59  VAL   B C   1 
ATOM   3405 O  O   . VAL   B 1 74  ? 51.252  -4.164  -28.845 1 64.5  ? 59  VAL   B O   1 
ATOM   3406 C  CB  . VAL   B 1 74  ? 48.847  -1.779  -28.78  1 63.27 ? 59  VAL   B CB  1 
ATOM   3407 C  CG1 . VAL   B 1 74  ? 48.109  -3.112  -28.822 1 63.81 ? 59  VAL   B CG1 1 
ATOM   3408 C  CG2 . VAL   B 1 74  ? 48.202  -0.84   -27.774 1 63.45 ? 59  VAL   B CG2 1 
ATOM   3409 N  N   . GLU   B 1 75  ? 51.319  -2.722  -30.591 1 64.71 ? 60  GLU   B N   1 
ATOM   3410 C  CA  . GLU   B 1 75  ? 51.959  -3.665  -31.513 1 65.34 ? 60  GLU   B CA  1 
ATOM   3411 C  C   . GLU   B 1 75  ? 53.373  -4.085  -31.07  1 66    ? 60  GLU   B C   1 
ATOM   3412 O  O   . GLU   B 1 75  ? 53.801  -5.188  -31.395 1 66.46 ? 60  GLU   B O   1 
ATOM   3413 C  CB  . GLU   B 1 75  ? 51.951  -3.124  -32.954 1 66.39 ? 60  GLU   B CB  1 
ATOM   3414 C  CG  . GLU   B 1 75  ? 50.564  -3.059  -33.569 1 68.12 ? 60  GLU   B CG  1 
ATOM   3415 C  CD  . GLU   B 1 75  ? 50.366  -1.994  -34.634 1 72.59 ? 60  GLU   B CD  1 
ATOM   3416 O  OE1 . GLU   B 1 75  ? 51.346  -1.292  -34.974 1 73.84 ? 60  GLU   B OE1 1 
ATOM   3417 O  OE2 . GLU   B 1 75  ? 49.221  -1.85   -35.12  1 73.59 ? 60  GLU   B OE2 1 
ATOM   3418 N  N   . LYS   B 1 76  ? 54.064  -3.242  -30.289 1 66.03 ? 61  LYS   B N   1 
ATOM   3419 C  CA  . LYS   B 1 76  ? 55.407  -3.538  -29.786 1 66.93 ? 61  LYS   B CA  1 
ATOM   3420 C  C   . LYS   B 1 76  ? 55.429  -4.385  -28.497 1 68    ? 61  LYS   B C   1 
ATOM   3421 O  O   . LYS   B 1 76  ? 56.499  -4.823  -28.075 1 68.13 ? 61  LYS   B O   1 
ATOM   3422 C  CB  . LYS   B 1 76  ? 56.202  -2.236  -29.566 1 68.32 ? 61  LYS   B CB  1 
ATOM   3423 N  N   . LEU   B 1 77  ? 54.268  -4.592  -27.855 1 68.46 ? 62  LEU   B N   1 
ATOM   3424 C  CA  . LEU   B 1 77  ? 54.181  -5.36   -26.61  1 68.93 ? 62  LEU   B CA  1 
ATOM   3425 C  C   . LEU   B 1 77  ? 54.557  -6.826  -26.789 1 69.62 ? 62  LEU   B C   1 
ATOM   3426 O  O   . LEU   B 1 77  ? 54.323  -7.409  -27.849 1 69.55 ? 62  LEU   B O   1 
ATOM   3427 C  CB  . LEU   B 1 77  ? 52.738  -5.331  -26.063 1 68.85 ? 62  LEU   B CB  1 
ATOM   3428 C  CG  . LEU   B 1 77  ? 52.254  -4.07   -25.364 1 69.84 ? 62  LEU   B CG  1 
ATOM   3429 C  CD1 . LEU   B 1 77  ? 50.761  -4.156  -25.094 1 70.36 ? 62  LEU   B CD1 1 
ATOM   3430 C  CD2 . LEU   B 1 77  ? 53.015  -3.829  -24.082 1 69.99 ? 62  LEU   B CD2 1 
ATOM   3431 N  N   . ASN   B 1 78  ? 55.073  -7.439  -25.718 1 70.85 ? 63  ASN   B N   1 
ATOM   3432 C  CA  . ASN   B 1 78  ? 55.333  -8.88   -25.685 1 72.19 ? 63  ASN   B CA  1 
ATOM   3433 C  C   . ASN   B 1 78  ? 54.119  -9.55   -25.029 1 72.99 ? 63  ASN   B C   1 
ATOM   3434 O  O   . ASN   B 1 78  ? 53.469  -8.934  -24.177 1 72.99 ? 63  ASN   B O   1 
ATOM   3435 C  CB  . ASN   B 1 78  ? 56.584  -9.194  -24.871 1 73.59 ? 63  ASN   B CB  1 
ATOM   3436 C  CG  . ASN   B 1 78  ? 57.842  -8.723  -25.544 1 76.56 ? 63  ASN   B CG  1 
ATOM   3437 O  OD1 . ASN   B 1 78  ? 57.985  -8.812  -26.775 1 77.38 ? 63  ASN   B OD1 1 
ATOM   3438 N  ND2 . ASN   B 1 78  ? 58.772  -8.206  -24.749 1 77.07 ? 63  ASN   B ND2 1 
ATOM   3439 N  N   . MET   B 1 79  ? 53.818  -10.805 -25.404 1 73.6  ? 64  MET   B N   1 
ATOM   3440 C  CA  . MET   B 1 79  ? 52.671  -11.495 -24.829 1 74.61 ? 64  MET   B CA  1 
ATOM   3441 C  C   . MET   B 1 79  ? 52.96   -11.813 -23.382 1 75.53 ? 64  MET   B C   1 
ATOM   3442 O  O   . MET   B 1 79  ? 53.866  -12.594 -23.097 1 75.93 ? 64  MET   B O   1 
ATOM   3443 C  CB  . MET   B 1 79  ? 52.338  -12.769 -25.598 1 75.18 ? 64  MET   B CB  1 
ATOM   3444 C  CG  . MET   B 1 79  ? 50.938  -13.239 -25.361 1 77.04 ? 64  MET   B CG  1 
ATOM   3445 S  SD  . MET   B 1 79  ? 50.549  -14.703 -26.35  1 81.72 ? 64  MET   B SD  1 
ATOM   3446 C  CE  . MET   B 1 79  ? 51.407  -15.95  -25.403 1 82.65 ? 64  MET   B CE  1 
ATOM   3447 N  N   . LEU   B 1 80  ? 52.254  -11.146 -22.465 1 75.66 ? 65  LEU   B N   1 
ATOM   3448 C  CA  . LEU   B 1 80  ? 52.444  -11.377 -21.04  1 76.24 ? 65  LEU   B CA  1 
ATOM   3449 C  C   . LEU   B 1 80  ? 51.472  -12.449 -20.548 1 76.93 ? 65  LEU   B C   1 
ATOM   3450 O  O   . LEU   B 1 80  ? 50.329  -12.516 -21.013 1 77.44 ? 65  LEU   B O   1 
ATOM   3451 C  CB  . LEU   B 1 80  ? 52.284  -10.081 -20.231 1 76.34 ? 65  LEU   B CB  1 
ATOM   3452 C  CG  . LEU   B 1 80  ? 53.329  -8.995  -20.471 1 77.66 ? 65  LEU   B CG  1 
ATOM   3453 C  CD1 . LEU   B 1 80  ? 53.071  -7.799  -19.573 1 78.05 ? 65  LEU   B CD1 1 
ATOM   3454 C  CD2 . LEU   B 1 80  ? 54.745  -9.522  -20.242 1 78.27 ? 65  LEU   B CD2 1 
ATOM   3455 N  N   . SER   B 1 81  ? 51.941  -13.321 -19.646 1 76.64 ? 66  SER   B N   1 
ATOM   3456 C  CA  . SER   B 1 81  ? 51.114  -14.392 -19.104 1 76.79 ? 66  SER   B CA  1 
ATOM   3457 C  C   . SER   B 1 81  ? 50.18   -13.835 -18.037 1 76.67 ? 66  SER   B C   1 
ATOM   3458 O  O   . SER   B 1 81  ? 50.557  -12.941 -17.288 1 76.54 ? 66  SER   B O   1 
ATOM   3459 C  CB  . SER   B 1 81  ? 51.985  -15.492 -18.502 1 77.8  ? 66  SER   B CB  1 
ATOM   3460 N  N   . ILE   B 1 82  ? 48.969  -14.375 -17.956 1 76.47 ? 67  ILE   B N   1 
ATOM   3461 C  CA  . ILE   B 1 82  ? 47.97   -13.962 -16.961 1 76.68 ? 67  ILE   B CA  1 
ATOM   3462 C  C   . ILE   B 1 82  ? 48.233  -14.544 -15.55  1 76.18 ? 67  ILE   B C   1 
ATOM   3463 O  O   . ILE   B 1 82  ? 47.689  -14.039 -14.565 1 76.03 ? 67  ILE   B O   1 
ATOM   3464 C  CB  . ILE   B 1 82  ? 46.568  -14.354 -17.527 1 77.42 ? 67  ILE   B CB  1 
ATOM   3465 C  CG1 . ILE   B 1 82  ? 46.134  -13.419 -18.667 1 78.41 ? 67  ILE   B CG1 1 
ATOM   3466 C  CG2 . ILE   B 1 82  ? 45.478  -14.495 -16.475 1 78.07 ? 67  ILE   B CG2 1 
ATOM   3467 C  CD1 . ILE   B 1 82  ? 46.233  -11.97  -18.337 1 79.81 ? 67  ILE   B CD1 1 
ATOM   3468 N  N   . ASP   B 1 83  ? 49.102  -15.571 -15.459 1 75.61 ? 68  ASP   B N   1 
ATOM   3469 C  CA  . ASP   B 1 83  ? 49.433  -16.3   -14.234 1 75.56 ? 68  ASP   B CA  1 
ATOM   3470 C  C   . ASP   B 1 83  ? 49.855  -15.43  -13.043 1 74.73 ? 68  ASP   B C   1 
ATOM   3471 O  O   . ASP   B 1 83  ? 49.611  -15.816 -11.9   1 74.6  ? 68  ASP   B O   1 
ATOM   3472 C  CB  . ASP   B 1 83  ? 50.504  -17.364 -14.517 1 77.91 ? 68  ASP   B CB  1 
ATOM   3473 C  CG  . ASP   B 1 83  ? 50.137  -18.373 -15.597 1 83.74 ? 68  ASP   B CG  1 
ATOM   3474 O  OD1 . ASP   B 1 83  ? 48.988  -18.31  -16.111 1 84.3  ? 68  ASP   B OD1 1 
ATOM   3475 O  OD2 . ASP   B 1 83  ? 51.002  -19.226 -15.934 1 86.42 ? 68  ASP   B OD2 1 
ATOM   3476 N  N   . HIS   B 1 84  ? 50.458  -14.261 -13.293 1 74    ? 69  HIS   B N   1 
ATOM   3477 C  CA  . HIS   B 1 84  ? 50.903  -13.389 -12.205 1 74.03 ? 69  HIS   B CA  1 
ATOM   3478 C  C   . HIS   B 1 84  ? 49.793  -12.506 -11.61  1 73.84 ? 69  HIS   B C   1 
ATOM   3479 O  O   . HIS   B 1 84  ? 50.069  -11.736 -10.69  1 74.02 ? 69  HIS   B O   1 
ATOM   3480 C  CB  . HIS   B 1 84  ? 52.113  -12.543 -12.626 1 74.98 ? 69  HIS   B CB  1 
ATOM   3481 N  N   . LEU   B 1 85  ? 48.543  -12.619 -12.113 1 73.29 ? 70  LEU   B N   1 
ATOM   3482 C  CA  . LEU   B 1 85  ? 47.392  -11.888 -11.564 1 73.2  ? 70  LEU   B CA  1 
ATOM   3483 C  C   . LEU   B 1 85  ? 46.727  -12.882 -10.6   1 73.06 ? 70  LEU   B C   1 
ATOM   3484 O  O   . LEU   B 1 85  ? 45.886  -13.688 -10.999 1 72.76 ? 70  LEU   B O   1 
ATOM   3485 C  CB  . LEU   B 1 85  ? 46.434  -11.457 -12.692 1 73.07 ? 70  LEU   B CB  1 
ATOM   3486 C  CG  . LEU   B 1 85  ? 47.053  -10.566 -13.772 1 73.57 ? 70  LEU   B CG  1 
ATOM   3487 C  CD1 . LEU   B 1 85  ? 46.24   -10.592 -15.033 1 73.72 ? 70  LEU   B CD1 1 
ATOM   3488 C  CD2 . LEU   B 1 85  ? 47.253  -9.153  -13.274 1 73.8  ? 70  LEU   B CD2 1 
ATOM   3489 N  N   . THR   B 1 86  ? 47.195  -12.871 -9.347  1 73.1  ? 71  THR   B N   1 
ATOM   3490 C  CA  . THR   B 1 86  ? 46.866  -13.832 -8.293  1 73.56 ? 71  THR   B CA  1 
ATOM   3491 C  C   . THR   B 1 86  ? 45.466  -13.73  -7.659  1 73.37 ? 71  THR   B C   1 
ATOM   3492 O  O   . THR   B 1 86  ? 44.914  -14.765 -7.261  1 73.94 ? 71  THR   B O   1 
ATOM   3493 C  CB  . THR   B 1 86  ? 47.934  -13.746 -7.193  1 74.78 ? 71  THR   B CB  1 
ATOM   3494 N  N   . ASP   B 1 87  ? 44.924  -12.512 -7.495  1 72.02 ? 72  ASP   B N   1 
ATOM   3495 C  CA  . ASP   B 1 87  ? 43.618  -12.351 -6.86   1 71.25 ? 72  ASP   B CA  1 
ATOM   3496 C  C   . ASP   B 1 87  ? 42.562  -11.726 -7.792  1 70.05 ? 72  ASP   B C   1 
ATOM   3497 O  O   . ASP   B 1 87  ? 42.903  -11.278 -8.893  1 70.49 ? 72  ASP   B O   1 
ATOM   3498 C  CB  . ASP   B 1 87  ? 43.761  -11.571 -5.537  1 73.38 ? 72  ASP   B CB  1 
ATOM   3499 C  CG  . ASP   B 1 87  ? 44.454  -10.23  -5.662  1 78.84 ? 72  ASP   B CG  1 
ATOM   3500 O  OD1 . ASP   B 1 87  ? 44.598  -9.744  -6.797  1 80.14 ? 72  ASP   B OD1 1 
ATOM   3501 O  OD2 . ASP   B 1 87  ? 44.849  -9.665  -4.617  1 80.92 ? 72  ASP   B OD2 1 
ATOM   3502 N  N   . HIS   B 1 88  ? 41.285  -11.699 -7.354  1 68.12 ? 73  HIS   B N   1 
ATOM   3503 C  CA  . HIS   B 1 88  ? 40.182  -11.132 -8.128  1 66.65 ? 73  HIS   B CA  1 
ATOM   3504 C  C   . HIS   B 1 88  ? 40.396  -9.647  -8.41   1 65.14 ? 73  HIS   B C   1 
ATOM   3505 O  O   . HIS   B 1 88  ? 40.191  -9.224  -9.543  1 65.48 ? 73  HIS   B O   1 
ATOM   3506 C  CB  . HIS   B 1 88  ? 38.838  -11.355 -7.406  1 66.91 ? 73  HIS   B CB  1 
ATOM   3507 C  CG  . HIS   B 1 88  ? 37.636  -10.868 -8.163  1 67.54 ? 73  HIS   B CG  1 
ATOM   3508 N  ND1 . HIS   B 1 88  ? 37.172  -11.531 -9.289  1 68.85 ? 73  HIS   B ND1 1 
ATOM   3509 C  CD2 . HIS   B 1 88  ? 36.822  -9.817  -7.91   1 68.17 ? 73  HIS   B CD2 1 
ATOM   3510 C  CE1 . HIS   B 1 88  ? 36.111  -10.855 -9.693  1 69.03 ? 73  HIS   B CE1 1 
ATOM   3511 N  NE2 . HIS   B 1 88  ? 35.856  -9.82   -8.891  1 69.01 ? 73  HIS   B NE2 1 
ATOM   3512 N  N   . LYS   B 1 89  ? 40.838  -8.866  -7.412  1 63.28 ? 74  LYS   B N   1 
ATOM   3513 C  CA  . LYS   B 1 89  ? 41.054  -7.437  -7.604  1 62.2  ? 74  LYS   B CA  1 
ATOM   3514 C  C   . LYS   B 1 89  ? 42.114  -7.106  -8.668  1 61.62 ? 74  LYS   B C   1 
ATOM   3515 O  O   . LYS   B 1 89  ? 41.915  -6.161  -9.437  1 61.59 ? 74  LYS   B O   1 
ATOM   3516 C  CB  . LYS   B 1 89  ? 41.351  -6.728  -6.277  1 62.85 ? 74  LYS   B CB  1 
ATOM   3517 C  CG  . LYS   B 1 89  ? 40.112  -6.59   -5.415  1 65.67 ? 74  LYS   B CG  1 
ATOM   3518 C  CD  . LYS   B 1 89  ? 40.234  -5.456  -4.427  1 68.83 ? 74  LYS   B CD  1 
ATOM   3519 C  CE  . LYS   B 1 89  ? 39.093  -5.454  -3.448  1 71.81 ? 74  LYS   B CE  1 
ATOM   3520 N  NZ  . LYS   B 1 89  ? 39.247  -4.381  -2.437  1 73.95 ? 74  LYS   B NZ  1 
ATOM   3521 N  N   . SER   B 1 90  ? 43.22   -7.875  -8.729  1 60.91 ? 75  SER   B N   1 
ATOM   3522 C  CA  . SER   B 1 90  ? 44.25   -7.644  -9.75   1 60.76 ? 75  SER   B CA  1 
ATOM   3523 C  C   . SER   B 1 90  ? 43.758  -8.109  -11.13  1 59.98 ? 75  SER   B C   1 
ATOM   3524 O  O   . SER   B 1 90  ? 44.104  -7.499  -12.136 1 60.34 ? 75  SER   B O   1 
ATOM   3525 C  CB  . SER   B 1 90  ? 45.577  -8.311  -9.385  1 61.75 ? 75  SER   B CB  1 
ATOM   3526 N  N   . GLN   B 1 91  ? 42.923  -9.157  -11.176 1 58.72 ? 76  GLN   B N   1 
ATOM   3527 C  CA  . GLN   B 1 91  ? 42.336  -9.635  -12.428 1 57.93 ? 76  GLN   B CA  1 
ATOM   3528 C  C   . GLN   B 1 91  ? 41.32   -8.623  -12.976 1 56.69 ? 76  GLN   B C   1 
ATOM   3529 O  O   . GLN   B 1 91  ? 41.19   -8.474  -14.198 1 57.02 ? 76  GLN   B O   1 
ATOM   3530 C  CB  . GLN   B 1 91  ? 41.639  -10.972 -12.198 1 59.49 ? 76  GLN   B CB  1 
ATOM   3531 C  CG  . GLN   B 1 91  ? 42.601  -12.138 -12.035 1 63.16 ? 76  GLN   B CG  1 
ATOM   3532 C  CD  . GLN   B 1 91  ? 41.959  -13.366 -11.442 1 68.61 ? 76  GLN   B CD  1 
ATOM   3533 O  OE1 . GLN   B 1 91  ? 40.752  -13.413 -11.159 1 71.08 ? 76  GLN   B OE1 1 
ATOM   3534 N  NE2 . GLN   B 1 91  ? 42.763  -14.394 -11.231 1 69.1  ? 76  GLN   B NE2 1 
ATOM   3535 N  N   . ARG   B 1 92  ? 40.591  -7.942  -12.071 1 54.99 ? 77  ARG   B N   1 
ATOM   3536 C  CA  . ARG   B 1 92  ? 39.593  -6.946  -12.453 1 53.89 ? 77  ARG   B CA  1 
ATOM   3537 C  C   . ARG   B 1 92  ? 40.275  -5.692  -12.997 1 53.18 ? 77  ARG   B C   1 
ATOM   3538 O  O   . ARG   B 1 92  ? 39.792  -5.12   -13.972 1 52.76 ? 77  ARG   B O   1 
ATOM   3539 C  CB  . ARG   B 1 92  ? 38.666  -6.594  -11.273 1 53.62 ? 77  ARG   B CB  1 
ATOM   3540 C  CG  . ARG   B 1 92  ? 37.622  -7.659  -10.975 1 53.32 ? 77  ARG   B CG  1 
ATOM   3541 C  CD  . ARG   B 1 92  ? 36.515  -7.764  -12.02  1 53.36 ? 77  ARG   B CD  1 
ATOM   3542 N  NE  . ARG   B 1 92  ? 35.678  -6.561  -12.058 1 53.31 ? 77  ARG   B NE  1 
ATOM   3543 C  CZ  . ARG   B 1 92  ? 34.664  -6.322  -11.23  1 53.12 ? 77  ARG   B CZ  1 
ATOM   3544 N  NH1 . ARG   B 1 92  ? 34.35   -7.197  -10.284 1 53.22 ? 77  ARG   B NH1 1 
ATOM   3545 N  NH2 . ARG   B 1 92  ? 33.968  -5.197  -11.332 1 50.68 ? 77  ARG   B NH2 1 
ATOM   3546 N  N   . LEU   B 1 93  ? 41.388  -5.268  -12.363 1 52.83 ? 78  LEU   B N   1 
ATOM   3547 C  CA  . LEU   B 1 93  ? 42.164  -4.102  -12.788 1 53.08 ? 78  LEU   B CA  1 
ATOM   3548 C  C   . LEU   B 1 93  ? 42.791  -4.387  -14.159 1 52.92 ? 78  LEU   B C   1 
ATOM   3549 O  O   . LEU   B 1 93  ? 42.71   -3.54   -15.046 1 53.46 ? 78  LEU   B O   1 
ATOM   3550 C  CB  . LEU   B 1 93  ? 43.264  -3.754  -11.768 1 53.61 ? 78  LEU   B CB  1 
ATOM   3551 C  CG  . LEU   B 1 93  ? 44.252  -2.655  -12.18  1 55.29 ? 78  LEU   B CG  1 
ATOM   3552 C  CD1 . LEU   B 1 93  ? 43.536  -1.334  -12.466 1 55.56 ? 78  LEU   B CD1 1 
ATOM   3553 C  CD2 . LEU   B 1 93  ? 45.306  -2.462  -11.128 1 56.06 ? 78  LEU   B CD2 1 
ATOM   3554 N  N   . ALA   B 1 94  ? 43.354  -5.592  -14.354 1 51.47 ? 79  ALA   B N   1 
ATOM   3555 C  CA  . ALA   B 1 94  ? 43.942  -5.953  -15.637 1 50.64 ? 79  ALA   B CA  1 
ATOM   3556 C  C   . ALA   B 1 94  ? 42.903  -5.945  -16.753 1 49.27 ? 79  ALA   B C   1 
ATOM   3557 O  O   . ALA   B 1 94  ? 43.22   -5.549  -17.869 1 49.55 ? 79  ALA   B O   1 
ATOM   3558 C  CB  . ALA   B 1 94  ? 44.625  -7.312  -15.55  1 51.07 ? 79  ALA   B CB  1 
ATOM   3559 N  N   . ARG   B 1 95  ? 41.665  -6.351  -16.449 1 47.88 ? 80  ARG   B N   1 
ATOM   3560 C  CA  . ARG   B 1 95  ? 40.544  -6.352  -17.397 1 46.66 ? 80  ARG   B CA  1 
ATOM   3561 C  C   . ARG   B 1 95  ? 40.162  -4.914  -17.785 1 45.5  ? 80  ARG   B C   1 
ATOM   3562 O  O   . ARG   B 1 95  ? 39.799  -4.656  -18.937 1 46.06 ? 80  ARG   B O   1 
ATOM   3563 C  CB  . ARG   B 1 95  ? 39.339  -7.03   -16.754 1 47.08 ? 80  ARG   B CB  1 
ATOM   3564 C  CG  . ARG   B 1 95  ? 38.88   -8.27   -17.475 1 48.16 ? 80  ARG   B CG  1 
ATOM   3565 C  CD  . ARG   B 1 95  ? 37.445  -8.599  -17.104 1 48.32 ? 80  ARG   B CD  1 
ATOM   3566 N  NE  . ARG   B 1 95  ? 36.462  -7.824  -17.863 1 49.9  ? 80  ARG   B NE  1 
ATOM   3567 C  CZ  . ARG   B 1 95  ? 36.057  -8.129  -19.096 1 50.96 ? 80  ARG   B CZ  1 
ATOM   3568 N  NH1 . ARG   B 1 95  ? 36.58   -9.167  -19.737 1 48.67 ? 80  ARG   B NH1 1 
ATOM   3569 N  NH2 . ARG   B 1 95  ? 35.147  -7.383  -19.705 1 50.84 ? 80  ARG   B NH2 1 
ATOM   3570 N  N   . LEU   B 1 96  ? 40.229  -3.989  -16.825 1 43.82 ? 81  LEU   B N   1 
ATOM   3571 C  CA  . LEU   B 1 96  ? 39.938  -2.584  -17.05  1 43.64 ? 81  LEU   B CA  1 
ATOM   3572 C  C   . LEU   B 1 96  ? 41.065  -1.975  -17.916 1 45.02 ? 81  LEU   B C   1 
ATOM   3573 O  O   . LEU   B 1 96  ? 40.777  -1.294  -18.904 1 45.42 ? 81  LEU   B O   1 
ATOM   3574 C  CB  . LEU   B 1 96  ? 39.807  -1.876  -15.688 1 42.95 ? 81  LEU   B CB  1 
ATOM   3575 C  CG  . LEU   B 1 96  ? 39.787  -0.365  -15.689 1 43.82 ? 81  LEU   B CG  1 
ATOM   3576 C  CD1 . LEU   B 1 96  ? 38.635  0.19    -16.521 1 44.58 ? 81  LEU   B CD1 1 
ATOM   3577 C  CD2 . LEU   B 1 96  ? 39.729  0.15    -14.3   1 43.98 ? 81  LEU   B CD2 1 
ATOM   3578 N  N   . VAL   B 1 97  ? 42.339  -2.271  -17.568 1 45.28 ? 82  VAL   B N   1 
ATOM   3579 C  CA  . VAL   B 1 97  ? 43.543  -1.846  -18.285 1 45.81 ? 82  VAL   B CA  1 
ATOM   3580 C  C   . VAL   B 1 97  ? 43.488  -2.322  -19.745 1 46.27 ? 82  VAL   B C   1 
ATOM   3581 O  O   . VAL   B 1 97  ? 43.519  -1.483  -20.634 1 46.91 ? 82  VAL   B O   1 
ATOM   3582 C  CB  . VAL   B 1 97  ? 44.837  -2.325  -17.547 1 46.45 ? 82  VAL   B CB  1 
ATOM   3583 C  CG1 . VAL   B 1 97  ? 46.061  -2.312  -18.463 1 46.89 ? 82  VAL   B CG1 1 
ATOM   3584 C  CG2 . VAL   B 1 97  ? 45.094  -1.491  -16.297 1 46.71 ? 82  VAL   B CG2 1 
ATOM   3585 N  N   . LEU   B 1 98  ? 43.345  -3.637  -19.99  1 45.89 ? 83  LEU   B N   1 
ATOM   3586 C  CA  . LEU   B 1 98  ? 43.295  -4.225  -21.33  1 46.34 ? 83  LEU   B CA  1 
ATOM   3587 C  C   . LEU   B 1 98  ? 42.09   -3.798  -22.155 1 47.03 ? 83  LEU   B C   1 
ATOM   3588 O  O   . LEU   B 1 98  ? 42.174  -3.699  -23.388 1 47.75 ? 83  LEU   B O   1 
ATOM   3589 C  CB  . LEU   B 1 98  ? 43.328  -5.761  -21.247 1 46.61 ? 83  LEU   B CB  1 
ATOM   3590 C  CG  . LEU   B 1 98  ? 44.619  -6.395  -20.739 1 48.45 ? 83  LEU   B CG  1 
ATOM   3591 C  CD1 . LEU   B 1 98  ? 44.492  -7.893  -20.696 1 48.83 ? 83  LEU   B CD1 1 
ATOM   3592 C  CD2 . LEU   B 1 98  ? 45.798  -6.014  -21.614 1 49.44 ? 83  LEU   B CD2 1 
ATOM   3593 N  N   . GLY   B 1 99  ? 40.968  -3.595  -21.486 1 46.56 ? 84  GLY   B N   1 
ATOM   3594 C  CA  . GLY   B 1 99  ? 39.749  -3.182  -22.159 1 46.4  ? 84  GLY   B CA  1 
ATOM   3595 C  C   . GLY   B 1 99  ? 39.828  -1.759  -22.643 1 45.88 ? 84  GLY   B C   1 
ATOM   3596 O  O   . GLY   B 1 99  ? 39.373  -1.462  -23.741 1 45.85 ? 84  GLY   B O   1 
ATOM   3597 N  N   . CYS   B 1 100 ? 40.413  -0.87   -21.831 1 45.83 ? 85  CYS   B N   1 
ATOM   3598 C  CA  . CYS   B 1 100 ? 40.606  0.534   -22.213 1 46.39 ? 85  CYS   B CA  1 
ATOM   3599 C  C   . CYS   B 1 100 ? 41.593  0.607   -23.383 1 46.98 ? 85  CYS   B C   1 
ATOM   3600 O  O   . CYS   B 1 100 ? 41.389  1.362   -24.331 1 46.88 ? 85  CYS   B O   1 
ATOM   3601 C  CB  . CYS   B 1 100 ? 41.1    1.357   -21.029 1 46.71 ? 85  CYS   B CB  1 
ATOM   3602 S  SG  . CYS   B 1 100 ? 39.834  1.707   -19.795 1 51.39 ? 85  CYS   B SG  1 
ATOM   3603 N  N   . ILE   B 1 101 ? 42.658  -0.2    -23.318 1 47.45 ? 86  ILE   B N   1 
ATOM   3604 C  CA  . ILE   B 1 101 ? 43.65   -0.259  -24.376 1 48    ? 86  ILE   B CA  1 
ATOM   3605 C  C   . ILE   B 1 101 ? 43.025  -0.755  -25.668 1 47.29 ? 86  ILE   B C   1 
ATOM   3606 O  O   . ILE   B 1 101 ? 43.235  -0.142  -26.705 1 47.56 ? 86  ILE   B O   1 
ATOM   3607 C  CB  . ILE   B 1 101 ? 44.898  -1.064  -23.926 1 48.9  ? 86  ILE   B CB  1 
ATOM   3608 C  CG1 . ILE   B 1 101 ? 45.619  -0.337  -22.781 1 49.62 ? 86  ILE   B CG1 1 
ATOM   3609 C  CG2 . ILE   B 1 101 ? 45.845  -1.274  -25.094 1 49.77 ? 86  ILE   B CG2 1 
ATOM   3610 C  CD1 . ILE   B 1 101 ? 46.668  -1.188  -22.105 1 51.59 ? 86  ILE   B CD1 1 
ATOM   3611 N  N   . THR   B 1 102 ? 42.183  -1.8    -25.591 1 46.8  ? 87  THR   B N   1 
ATOM   3612 C  CA  . THR   B 1 102 ? 41.472  -2.351  -26.75  1 46.3  ? 87  THR   B CA  1 
ATOM   3613 C  C   . THR   B 1 102 ? 40.555  -1.327  -27.417 1 46.37 ? 87  THR   B C   1 
ATOM   3614 O  O   . THR   B 1 102 ? 40.578  -1.225  -28.635 1 46.34 ? 87  THR   B O   1 
ATOM   3615 C  CB  . THR   B 1 102 ? 40.732  -3.624  -26.368 1 46.84 ? 87  THR   B CB  1 
ATOM   3616 O  OG1 . THR   B 1 102 ? 41.673  -4.537  -25.824 1 47.65 ? 87  THR   B OG1 1 
ATOM   3617 C  CG2 . THR   B 1 102 ? 40.01   -4.258  -27.547 1 46.73 ? 87  THR   B CG2 1 
ATOM   3618 N  N   . MET   B 1 103 ? 39.787  -0.533  -26.636 1 46.3  ? 88  MET   B N   1 
ATOM   3619 C  CA  . MET   B 1 103 ? 38.915  0.502   -27.207 1 46.49 ? 88  MET   B CA  1 
ATOM   3620 C  C   . MET   B 1 103 ? 39.755  1.54    -27.958 1 46.48 ? 88  MET   B C   1 
ATOM   3621 O  O   . MET   B 1 103 ? 39.404  1.922   -29.059 1 46.05 ? 88  MET   B O   1 
ATOM   3622 C  CB  . MET   B 1 103 ? 38.074  1.214   -26.115 1 47.57 ? 88  MET   B CB  1 
ATOM   3623 C  CG  . MET   B 1 103 ? 37.075  0.321   -25.364 1 50.82 ? 88  MET   B CG  1 
ATOM   3624 S  SD  . MET   B 1 103 ? 36.145  -0.932  -26.311 1 56.5  ? 88  MET   B SD  1 
ATOM   3625 C  CE  . MET   B 1 103 ? 36.941  -2.433  -25.651 1 54.36 ? 88  MET   B CE  1 
ATOM   3626 N  N   . ALA   B 1 104 ? 40.872  1.983   -27.367 1 47.04 ? 89  ALA   B N   1 
ATOM   3627 C  CA  . ALA   B 1 104 ? 41.747  2.977   -27.982 1 48.17 ? 89  ALA   B CA  1 
ATOM   3628 C  C   . ALA   B 1 104 ? 42.435  2.419   -29.23  1 49.24 ? 89  ALA   B C   1 
ATOM   3629 O  O   . ALA   B 1 104 ? 42.632  3.147   -30.194 1 49.08 ? 89  ALA   B O   1 
ATOM   3630 C  CB  . ALA   B 1 104 ? 42.782  3.447   -26.982 1 48.43 ? 89  ALA   B CB  1 
ATOM   3631 N  N   . TYR   B 1 105 ? 42.789  1.133   -29.218 1 49.88 ? 90  TYR   B N   1 
ATOM   3632 C  CA  . TYR   B 1 105 ? 43.431  0.504   -30.36  1 50.48 ? 90  TYR   B CA  1 
ATOM   3633 C  C   . TYR   B 1 105 ? 42.444  0.378   -31.511 1 50.4  ? 90  TYR   B C   1 
ATOM   3634 O  O   . TYR   B 1 105 ? 42.771  0.732   -32.638 1 50.91 ? 90  TYR   B O   1 
ATOM   3635 C  CB  . TYR   B 1 105 ? 44.03   -0.864  -29.978 1 51    ? 90  TYR   B CB  1 
ATOM   3636 C  CG  . TYR   B 1 105 ? 44.843  -1.464  -31.107 1 52.28 ? 90  TYR   B CG  1 
ATOM   3637 C  CD1 . TYR   B 1 105 ? 46.18   -1.131  -31.282 1 53.23 ? 90  TYR   B CD1 1 
ATOM   3638 C  CD2 . TYR   B 1 105 ? 44.259  -2.317  -32.034 1 52.99 ? 90  TYR   B CD2 1 
ATOM   3639 C  CE1 . TYR   B 1 105 ? 46.921  -1.651  -32.337 1 54.01 ? 90  TYR   B CE1 1 
ATOM   3640 C  CE2 . TYR   B 1 105 ? 44.976  -2.804  -33.115 1 53.89 ? 90  TYR   B CE2 1 
ATOM   3641 C  CZ  . TYR   B 1 105 ? 46.31   -2.478  -33.258 1 55.25 ? 90  TYR   B CZ  1 
ATOM   3642 O  OH  . TYR   B 1 105 ? 47.024  -3.004  -34.306 1 57.82 ? 90  TYR   B OH  1 
ATOM   3643 N  N   . VAL   B 1 106 ? 41.243  -0.131  -31.239 1 49.72 ? 91  VAL   B N   1 
ATOM   3644 C  CA  . VAL   B 1 106 ? 40.226  -0.298  -32.263 1 49.58 ? 91  VAL   B CA  1 
ATOM   3645 C  C   . VAL   B 1 106 ? 39.778  1.051   -32.854 1 49.46 ? 91  VAL   B C   1 
ATOM   3646 O  O   . VAL   B 1 106 ? 39.744  1.2     -34.066 1 49.43 ? 91  VAL   B O   1 
ATOM   3647 C  CB  . VAL   B 1 106 ? 39.026  -1.111  -31.722 1 50.12 ? 91  VAL   B CB  1 
ATOM   3648 C  CG1 . VAL   B 1 106 ? 37.86   -1.097  -32.701 1 50.5  ? 91  VAL   B CG1 1 
ATOM   3649 C  CG2 . VAL   B 1 106 ? 39.43   -2.54   -31.402 1 50.67 ? 91  VAL   B CG2 1 
ATOM   3650 N  N   . TRP   B 1 107 ? 39.461  2.029   -32.011 1 49.27 ? 92  TRP   B N   1 
ATOM   3651 C  CA  . TRP   B 1 107 ? 38.907  3.292   -32.474 1 49.75 ? 92  TRP   B CA  1 
ATOM   3652 C  C   . TRP   B 1 107 ? 39.911  4.374   -32.822 1 50.56 ? 92  TRP   B C   1 
ATOM   3653 O  O   . TRP   B 1 107 ? 39.551  5.314   -33.526 1 50.99 ? 92  TRP   B O   1 
ATOM   3654 C  CB  . TRP   B 1 107 ? 37.872  3.828   -31.465 1 49.71 ? 92  TRP   B CB  1 
ATOM   3655 C  CG  . TRP   B 1 107 ? 36.758  2.851   -31.166 1 50.38 ? 92  TRP   B CG  1 
ATOM   3656 C  CD1 . TRP   B 1 107 ? 36.418  2.349   -29.946 1 51.1  ? 92  TRP   B CD1 1 
ATOM   3657 C  CD2 . TRP   B 1 107 ? 35.857  2.247   -32.111 1 50.75 ? 92  TRP   B CD2 1 
ATOM   3658 N  NE1 . TRP   B 1 107 ? 35.389  1.45    -30.074 1 51.43 ? 92  TRP   B NE1 1 
ATOM   3659 C  CE2 . TRP   B 1 107 ? 35.018  1.376   -31.393 1 51.36 ? 92  TRP   B CE2 1 
ATOM   3660 C  CE3 . TRP   B 1 107 ? 35.7    2.335   -33.5   1 51.69 ? 92  TRP   B CE3 1 
ATOM   3661 C  CZ2 . TRP   B 1 107 ? 34.021  0.618   -32.012 1 51.97 ? 92  TRP   B CZ2 1 
ATOM   3662 C  CZ3 . TRP   B 1 107 ? 34.721  1.571   -34.109 1 52.73 ? 92  TRP   B CZ3 1 
ATOM   3663 C  CH2 . TRP   B 1 107 ? 33.897  0.725   -33.367 1 52.5  ? 92  TRP   B CH2 1 
ATOM   3664 N  N   . GLY   B 1 108 ? 41.137  4.259   -32.341 1 50.71 ? 93  GLY   B N   1 
ATOM   3665 C  CA  . GLY   B 1 108 ? 42.174  5.242   -32.61  1 51.67 ? 93  GLY   B CA  1 
ATOM   3666 C  C   . GLY   B 1 108 ? 41.811  6.62    -32.12  1 53.05 ? 93  GLY   B C   1 
ATOM   3667 O  O   . GLY   B 1 108 ? 41.37   6.781   -30.979 1 53.4  ? 93  GLY   B O   1 
ATOM   3668 N  N   . LYS   B 1 109 ? 41.945  7.617   -32.994 1 53.83 ? 94  LYS   B N   1 
ATOM   3669 C  CA  . LYS   B 1 109 ? 41.55   8.987   -32.64  1 55.31 ? 94  LYS   B CA  1 
ATOM   3670 C  C   . LYS   B 1 109 ? 40.026  9.226   -32.708 1 56.28 ? 94  LYS   B C   1 
ATOM   3671 O  O   . LYS   B 1 109 ? 39.57   10.304  -32.344 1 56.1  ? 94  LYS   B O   1 
ATOM   3672 C  CB  . LYS   B 1 109 ? 42.301  10.028  -33.482 1 57.5  ? 94  LYS   B CB  1 
ATOM   3673 C  CG  . LYS   B 1 109 ? 43.802  10.03   -33.25  1 61.41 ? 94  LYS   B CG  1 
ATOM   3674 C  CD  . LYS   B 1 109 ? 44.493  11.051  -34.129 1 65.94 ? 94  LYS   B CD  1 
ATOM   3675 C  CE  . LYS   B 1 109 ? 45.991  10.931  -34.065 1 69.75 ? 94  LYS   B CE  1 
ATOM   3676 N  NZ  . LYS   B 1 109 ? 46.659  12.124  -34.648 1 72.39 ? 94  LYS   B NZ  1 
ATOM   3677 N  N   . GLY   B 1 110 ? 39.272  8.224   -33.161 1 57.46 ? 95  GLY   B N   1 
ATOM   3678 C  CA  . GLY   B 1 110 ? 37.823  8.269   -33.272 1 59.24 ? 95  GLY   B CA  1 
ATOM   3679 C  C   . GLY   B 1 110 ? 37.312  9.027   -34.473 1 60.84 ? 95  GLY   B C   1 
ATOM   3680 O  O   . GLY   B 1 110 ? 36.278  9.697   -34.385 1 61.06 ? 95  GLY   B O   1 
ATOM   3681 N  N   . HIS   B 1 111 ? 38.013  8.91    -35.61  1 61.51 ? 96  HIS   B N   1 
ATOM   3682 C  CA  . HIS   B 1 111 ? 37.606  9.621   -36.809 1 62.48 ? 96  HIS   B CA  1 
ATOM   3683 C  C   . HIS   B 1 111 ? 37.457  8.736   -38.032 1 63.16 ? 96  HIS   B C   1 
ATOM   3684 O  O   . HIS   B 1 111 ? 37.66   9.21    -39.149 1 63.65 ? 96  HIS   B O   1 
ATOM   3685 C  CB  . HIS   B 1 111 ? 38.548  10.799  -37.083 1 63.84 ? 96  HIS   B CB  1 
ATOM   3686 C  CG  . HIS   B 1 111 ? 38.483  11.836  -36.007 1 67.65 ? 96  HIS   B CG  1 
ATOM   3687 N  ND1 . HIS   B 1 111 ? 37.262  12.348  -35.568 1 70.19 ? 96  HIS   B ND1 1 
ATOM   3688 C  CD2 . HIS   B 1 111 ? 39.48   12.409  -35.293 1 68.99 ? 96  HIS   B CD2 1 
ATOM   3689 C  CE1 . HIS   B 1 111 ? 37.561  13.204  -34.601 1 70.83 ? 96  HIS   B CE1 1 
ATOM   3690 N  NE2 . HIS   B 1 111 ? 38.884  13.278  -34.401 1 70.45 ? 96  HIS   B NE2 1 
ATOM   3691 N  N   . GLY   B 1 112 ? 37.089  7.475   -37.826 1 62.89 ? 97  GLY   B N   1 
ATOM   3692 C  CA  . GLY   B 1 112 ? 36.844  6.562   -38.928 1 63.08 ? 97  GLY   B CA  1 
ATOM   3693 C  C   . GLY   B 1 112 ? 37.918  5.545   -39.213 1 63.67 ? 97  GLY   B C   1 
ATOM   3694 O  O   . GLY   B 1 112 ? 37.62   4.525   -39.842 1 64.44 ? 97  GLY   B O   1 
ATOM   3695 N  N   . ASP   B 1 113 ? 39.18   5.817   -38.818 1 63.35 ? 98  ASP   B N   1 
ATOM   3696 C  CA  . ASP   B 1 113 ? 40.25   4.848   -39.073 1 63.57 ? 98  ASP   B CA  1 
ATOM   3697 C  C   . ASP   B 1 113 ? 40.207  3.809   -37.972 1 63.2  ? 98  ASP   B C   1 
ATOM   3698 O  O   . ASP   B 1 113 ? 40.779  4.009   -36.897 1 63.45 ? 98  ASP   B O   1 
ATOM   3699 C  CB  . ASP   B 1 113 ? 41.65   5.491   -39.181 1 65.55 ? 98  ASP   B CB  1 
ATOM   3700 C  CG  . ASP   B 1 113 ? 42.734  4.462   -39.49  1 70.94 ? 98  ASP   B CG  1 
ATOM   3701 O  OD1 . ASP   B 1 113 ? 42.446  3.5     -40.226 1 72.06 ? 98  ASP   B OD1 1 
ATOM   3702 O  OD2 . ASP   B 1 113 ? 43.856  4.607   -38.978 1 73.77 ? 98  ASP   B OD2 1 
ATOM   3703 N  N   . VAL   B 1 114 ? 39.5    2.716   -38.236 1 62.43 ? 99  VAL   B N   1 
ATOM   3704 C  CA  . VAL   B 1 114 ? 39.334  1.638   -37.277 1 62.43 ? 99  VAL   B CA  1 
ATOM   3705 C  C   . VAL   B 1 114 ? 40.385  0.533   -37.497 1 62.69 ? 99  VAL   B C   1 
ATOM   3706 O  O   . VAL   B 1 114 ? 41.022  0.47    -38.551 1 63.61 ? 99  VAL   B O   1 
ATOM   3707 C  CB  . VAL   B 1 114 ? 37.89   1.066   -37.337 1 62.88 ? 99  VAL   B CB  1 
ATOM   3708 C  CG1 . VAL   B 1 114 ? 36.841  2.173   -37.335 1 63.37 ? 99  VAL   B CG1 1 
ATOM   3709 C  CG2 . VAL   B 1 114 ? 37.71   0.159   -38.541 1 63.51 ? 99  VAL   B CG2 1 
ATOM   3710 N  N   . ARG   B 1 115 ? 40.573  -0.329  -36.496 1 61.55 ? 100 ARG   B N   1 
ATOM   3711 C  CA  . ARG   B 1 115 ? 41.433  -1.488  -36.608 1 60.95 ? 100 ARG   B CA  1 
ATOM   3712 C  C   . ARG   B 1 115 ? 40.504  -2.69   -36.502 1 60.35 ? 100 ARG   B C   1 
ATOM   3713 O  O   . ARG   B 1 115 ? 39.713  -2.76   -35.567 1 60.21 ? 100 ARG   B O   1 
ATOM   3714 C  CB  . ARG   B 1 115 ? 42.492  -1.518  -35.495 1 62.18 ? 100 ARG   B CB  1 
ATOM   3715 C  CG  . ARG   B 1 115 ? 43.717  -0.666  -35.774 1 65.09 ? 100 ARG   B CG  1 
ATOM   3716 C  CD  . ARG   B 1 115 ? 44.462  -1.133  -37.002 1 68.19 ? 100 ARG   B CD  1 
ATOM   3717 N  NE  . ARG   B 1 115 ? 45.866  -0.752  -36.937 1 71.09 ? 100 ARG   B NE  1 
ATOM   3718 C  CZ  . ARG   B 1 115 ? 46.396  0.294   -37.561 1 72.86 ? 100 ARG   B CZ  1 
ATOM   3719 N  NH1 . ARG   B 1 115 ? 47.692  0.554   -37.445 1 72.46 ? 100 ARG   B NH1 1 
ATOM   3720 N  NH2 . ARG   B 1 115 ? 45.636  1.082   -38.32  1 72.49 ? 100 ARG   B NH2 1 
ATOM   3721 N  N   . LYS   B 1 116 ? 40.55   -3.604  -37.473 1 60.08 ? 101 LYS   B N   1 
ATOM   3722 C  CA  . LYS   B 1 116 ? 39.698  -4.791  -37.457 1 60.22 ? 101 LYS   B CA  1 
ATOM   3723 C  C   . LYS   B 1 116 ? 40.37   -6.036  -36.852 1 60.77 ? 101 LYS   B C   1 
ATOM   3724 O  O   . LYS   B 1 116 ? 39.732  -7.084  -36.765 1 61.51 ? 101 LYS   B O   1 
ATOM   3725 C  CB  . LYS   B 1 116 ? 39.156  -5.081  -38.862 1 61.56 ? 101 LYS   B CB  1 
ATOM   3726 N  N   . VAL   B 1 117 ? 41.642  -5.937  -36.437 1 60.53 ? 102 VAL   B N   1 
ATOM   3727 C  CA  . VAL   B 1 117 ? 42.381  -7.051  -35.851 1 61.22 ? 102 VAL   B CA  1 
ATOM   3728 C  C   . VAL   B 1 117 ? 43.068  -6.561  -34.573 1 61.87 ? 102 VAL   B C   1 
ATOM   3729 O  O   . VAL   B 1 117 ? 43.754  -5.541  -34.607 1 62.13 ? 102 VAL   B O   1 
ATOM   3730 C  CB  . VAL   B 1 117 ? 43.449  -7.612  -36.843 1 61.94 ? 102 VAL   B CB  1 
ATOM   3731 C  CG1 . VAL   B 1 117 ? 44.296  -8.712  -36.194 1 62.31 ? 102 VAL   B CG1 1 
ATOM   3732 C  CG2 . VAL   B 1 117 ? 42.817  -8.094  -38.152 1 62.08 ? 102 VAL   B CG2 1 
ATOM   3733 N  N   . LEU   B 1 118 ? 42.912  -7.285  -33.46  1 61.69 ? 103 LEU   B N   1 
ATOM   3734 C  CA  . LEU   B 1 118 ? 43.579  -6.934  -32.21  1 61.93 ? 103 LEU   B CA  1 
ATOM   3735 C  C   . LEU   B 1 118 ? 44.85   -7.801  -32.12  1 62.98 ? 103 LEU   B C   1 
ATOM   3736 O  O   . LEU   B 1 118 ? 44.76   -9.021  -32.222 1 63.17 ? 103 LEU   B O   1 
ATOM   3737 C  CB  . LEU   B 1 118 ? 42.638  -7.201  -31.017 1 61.25 ? 103 LEU   B CB  1 
ATOM   3738 C  CG  . LEU   B 1 118 ? 43.156  -6.755  -29.651 1 61.75 ? 103 LEU   B CG  1 
ATOM   3739 C  CD1 . LEU   B 1 118 ? 43.288  -5.252  -29.574 1 61.48 ? 103 LEU   B CD1 1 
ATOM   3740 C  CD2 . LEU   B 1 118 ? 42.264  -7.251  -28.539 1 62.52 ? 103 LEU   B CD2 1 
ATOM   3741 N  N   . PRO   B 1 119 ? 46.037  -7.194  -31.975 1 63.63 ? 104 PRO   B N   1 
ATOM   3742 C  CA  . PRO   B 1 119 ? 47.282  -7.992  -31.934 1 64.61 ? 104 PRO   B CA  1 
ATOM   3743 C  C   . PRO   B 1 119 ? 47.327  -9.103  -30.883 1 65.88 ? 104 PRO   B C   1 
ATOM   3744 O  O   . PRO   B 1 119 ? 46.933  -8.878  -29.743 1 66.67 ? 104 PRO   B O   1 
ATOM   3745 C  CB  . PRO   B 1 119 ? 48.369  -6.948  -31.679 1 64.91 ? 104 PRO   B CB  1 
ATOM   3746 C  CG  . PRO   B 1 119 ? 47.775  -5.652  -32.139 1 65.14 ? 104 PRO   B CG  1 
ATOM   3747 C  CD  . PRO   B 1 119 ? 46.31   -5.753  -31.853 1 63.32 ? 104 PRO   B CD  1 
ATOM   3748 N  N   . ARG   B 1 120 ? 47.836  -10.294 -31.271 1 65.46 ? 105 ARG   B N   1 
ATOM   3749 C  CA  . ARG   B 1 120 ? 47.927  -11.49  -30.436 1 65.41 ? 105 ARG   B CA  1 
ATOM   3750 C  C   . ARG   B 1 120 ? 48.53   -11.268 -29.074 1 65.36 ? 105 ARG   B C   1 
ATOM   3751 O  O   . ARG   B 1 120 ? 48.082  -11.88  -28.108 1 65.51 ? 105 ARG   B O   1 
ATOM   3752 C  CB  . ARG   B 1 120 ? 48.685  -12.604 -31.166 1 66.56 ? 105 ARG   B CB  1 
ATOM   3753 N  N   . ASN   B 1 121 ? 49.532  -10.394 -28.976 1 65.28 ? 106 ASN   B N   1 
ATOM   3754 C  CA  . ASN   B 1 121 ? 50.193  -10.133 -27.699 1 65.88 ? 106 ASN   B CA  1 
ATOM   3755 C  C   . ASN   B 1 121 ? 49.287  -9.429  -26.662 1 65.67 ? 106 ASN   B C   1 
ATOM   3756 O  O   . ASN   B 1 121 ? 49.612  -9.428  -25.468 1 65.62 ? 106 ASN   B O   1 
ATOM   3757 C  CB  . ASN   B 1 121 ? 51.507  -9.384  -27.906 1 67.89 ? 106 ASN   B CB  1 
ATOM   3758 C  CG  . ASN   B 1 121 ? 52.584  -10.147 -28.687 1 72.65 ? 106 ASN   B CG  1 
ATOM   3759 O  OD1 . ASN   B 1 121 ? 53.576  -9.556  -29.15  1 74.23 ? 106 ASN   B OD1 1 
ATOM   3760 N  ND2 . ASN   B 1 121 ? 52.454  -11.468 -28.824 1 73.14 ? 106 ASN   B ND2 1 
ATOM   3761 N  N   . ILE   B 1 122 ? 48.146  -8.853  -27.113 1 65.27 ? 107 ILE   B N   1 
ATOM   3762 C  CA  . ILE   B 1 122 ? 47.179  -8.231  -26.217 1 65.08 ? 107 ILE   B CA  1 
ATOM   3763 C  C   . ILE   B 1 122 ? 45.88   -9.051  -26.222 1 64.42 ? 107 ILE   B C   1 
ATOM   3764 O  O   . ILE   B 1 122 ? 45.353  -9.338  -25.149 1 64.37 ? 107 ILE   B O   1 
ATOM   3765 C  CB  . ILE   B 1 122 ? 46.975  -6.702  -26.432 1 65.68 ? 107 ILE   B CB  1 
ATOM   3766 C  CG1 . ILE   B 1 122 ? 46.163  -6.087  -25.28  1 66.79 ? 107 ILE   B CG1 1 
ATOM   3767 C  CG2 . ILE   B 1 122 ? 46.363  -6.367  -27.784 1 66.18 ? 107 ILE   B CG2 1 
ATOM   3768 C  CD1 . ILE   B 1 122 ? 46.127  -4.63   -25.266 1 68.16 ? 107 ILE   B CD1 1 
ATOM   3769 N  N   . ALA   B 1 123 ? 45.437  -9.522  -27.403 1 63.72 ? 108 ALA   B N   1 
ATOM   3770 C  CA  . ALA   B 1 123 ? 44.224  -10.329 -27.561 1 63.78 ? 108 ALA   B CA  1 
ATOM   3771 C  C   . ALA   B 1 123 ? 44.263  -11.666 -26.828 1 63.84 ? 108 ALA   B C   1 
ATOM   3772 O  O   . ALA   B 1 123 ? 43.258  -12.044 -26.222 1 64.68 ? 108 ALA   B O   1 
ATOM   3773 C  CB  . ALA   B 1 123 ? 43.915  -10.551 -29.036 1 63.8  ? 108 ALA   B CB  1 
ATOM   3774 N  N   . VAL   B 1 124 ? 45.402  -12.388 -26.876 1 62.67 ? 109 VAL   B N   1 
ATOM   3775 C  CA  . VAL   B 1 124 ? 45.494  -13.676 -26.194 1 61.75 ? 109 VAL   B CA  1 
ATOM   3776 C  C   . VAL   B 1 124 ? 45.322  -13.493 -24.663 1 60.51 ? 109 VAL   B C   1 
ATOM   3777 O  O   . VAL   B 1 124 ? 44.347  -14.029 -24.129 1 60.35 ? 109 VAL   B O   1 
ATOM   3778 C  CB  . VAL   B 1 124 ? 46.738  -14.528 -26.596 1 62.32 ? 109 VAL   B CB  1 
ATOM   3779 C  CG1 . VAL   B 1 124 ? 46.97   -15.679 -25.618 1 62.52 ? 109 VAL   B CG1 1 
ATOM   3780 C  CG2 . VAL   B 1 124 ? 46.597  -15.058 -28.022 1 62.58 ? 109 VAL   B CG2 1 
ATOM   3781 N  N   . PRO   B 1 125 ? 46.145  -12.675 -23.958 1 59.27 ? 110 PRO   B N   1 
ATOM   3782 C  CA  . PRO   B 1 125 ? 45.931  -12.515 -22.51  1 58.47 ? 110 PRO   B CA  1 
ATOM   3783 C  C   . PRO   B 1 125 ? 44.608  -11.84  -22.132 1 57.99 ? 110 PRO   B C   1 
ATOM   3784 O  O   . PRO   B 1 125 ? 44.125  -12.039 -21.021 1 57.67 ? 110 PRO   B O   1 
ATOM   3785 C  CB  . PRO   B 1 125 ? 47.143  -11.703 -22.046 1 59.35 ? 110 PRO   B CB  1 
ATOM   3786 C  CG  . PRO   B 1 125 ? 47.656  -11.038 -23.254 1 59.98 ? 110 PRO   B CG  1 
ATOM   3787 C  CD  . PRO   B 1 125 ? 47.344  -11.939 -24.409 1 58.6  ? 110 PRO   B CD  1 
ATOM   3788 N  N   . TYR   B 1 126 ? 44.017  -11.055 -23.048 1 57.39 ? 111 TYR   B N   1 
ATOM   3789 C  CA  . TYR   B 1 126 ? 42.747  -10.394 -22.775 1 56.79 ? 111 TYR   B CA  1 
ATOM   3790 C  C   . TYR   B 1 126 ? 41.655  -11.441 -22.778 1 56.62 ? 111 TYR   B C   1 
ATOM   3791 O  O   . TYR   B 1 126 ? 40.885  -11.502 -21.824 1 56.76 ? 111 TYR   B O   1 
ATOM   3792 C  CB  . TYR   B 1 126 ? 42.462  -9.279  -23.803 1 56.2  ? 111 TYR   B CB  1 
ATOM   3793 C  CG  . TYR   B 1 126 ? 41.274  -8.4    -23.468 1 56.35 ? 111 TYR   B CG  1 
ATOM   3794 C  CD1 . TYR   B 1 126 ? 40.879  -8.197  -22.149 1 56.87 ? 111 TYR   B CD1 1 
ATOM   3795 C  CD2 . TYR   B 1 126 ? 40.582  -7.728  -24.462 1 56.83 ? 111 TYR   B CD2 1 
ATOM   3796 C  CE1 . TYR   B 1 126 ? 39.805  -7.381  -21.836 1 57.52 ? 111 TYR   B CE1 1 
ATOM   3797 C  CE2 . TYR   B 1 126 ? 39.524  -6.883  -24.158 1 57.54 ? 111 TYR   B CE2 1 
ATOM   3798 C  CZ  . TYR   B 1 126 ? 39.131  -6.724  -22.844 1 58.02 ? 111 TYR   B CZ  1 
ATOM   3799 O  OH  . TYR   B 1 126 ? 38.082  -5.917  -22.525 1 58.14 ? 111 TYR   B OH  1 
ATOM   3800 N  N   . CYS   B 1 127 ? 41.624  -12.3   -23.81  1 56.16 ? 112 CYS   B N   1 
ATOM   3801 C  CA  . CYS   B 1 127 ? 40.63   -13.354 -23.909 1 56.47 ? 112 CYS   B CA  1 
ATOM   3802 C  C   . CYS   B 1 127 ? 40.786  -14.42  -22.84  1 57.53 ? 112 CYS   B C   1 
ATOM   3803 O  O   . CYS   B 1 127 ? 39.781  -14.973 -22.397 1 57.98 ? 112 CYS   B O   1 
ATOM   3804 C  CB  . CYS   B 1 127 ? 40.63   -13.969 -25.296 1 56.37 ? 112 CYS   B CB  1 
ATOM   3805 S  SG  . CYS   B 1 127 ? 40.217  -12.817 -26.618 1 59.62 ? 112 CYS   B SG  1 
ATOM   3806 N  N   . GLN   B 1 128 ? 42.029  -14.722 -22.431 1 57.66 ? 113 GLN   B N   1 
ATOM   3807 C  CA  . GLN   B 1 128 ? 42.27   -15.721 -21.395 1 58.02 ? 113 GLN   B CA  1 
ATOM   3808 C  C   . GLN   B 1 128 ? 41.774  -15.208 -20.033 1 58.14 ? 113 GLN   B C   1 
ATOM   3809 O  O   . GLN   B 1 128 ? 41.118  -15.941 -19.301 1 58.54 ? 113 GLN   B O   1 
ATOM   3810 C  CB  . GLN   B 1 128 ? 43.765  -16.089 -21.333 1 59.46 ? 113 GLN   B CB  1 
ATOM   3811 N  N   . LEU   B 1 129 ? 42.088  -13.954 -19.702 1 57.78 ? 114 LEU   B N   1 
ATOM   3812 C  CA  . LEU   B 1 129 ? 41.651  -13.304 -18.469 1 58.32 ? 114 LEU   B CA  1 
ATOM   3813 C  C   . LEU   B 1 129 ? 40.118  -13.14  -18.452 1 59    ? 114 LEU   B C   1 
ATOM   3814 O  O   . LEU   B 1 129 ? 39.501  -13.268 -17.398 1 59.43 ? 114 LEU   B O   1 
ATOM   3815 C  CB  . LEU   B 1 129 ? 42.326  -11.938 -18.381 1 58.46 ? 114 LEU   B CB  1 
ATOM   3816 C  CG  . LEU   B 1 129 ? 41.999  -11.06  -17.19  1 60.21 ? 114 LEU   B CG  1 
ATOM   3817 C  CD1 . LEU   B 1 129 ? 42.487  -11.686 -15.894 1 60.94 ? 114 LEU   B CD1 1 
ATOM   3818 C  CD2 . LEU   B 1 129 ? 42.604  -9.688  -17.373 1 60.55 ? 114 LEU   B CD2 1 
ATOM   3819 N  N   . SER   B 1 130 ? 39.513  -12.893 -19.626 1 58.81 ? 115 SER   B N   1 
ATOM   3820 C  CA  . SER   B 1 130 ? 38.077  -12.721 -19.793 1 59.23 ? 115 SER   B CA  1 
ATOM   3821 C  C   . SER   B 1 130 ? 37.362  -14.043 -19.552 1 60.14 ? 115 SER   B C   1 
ATOM   3822 O  O   . SER   B 1 130 ? 36.339  -14.058 -18.878 1 60.66 ? 115 SER   B O   1 
ATOM   3823 C  CB  . SER   B 1 130 ? 37.763  -12.184 -21.188 1 59.37 ? 115 SER   B CB  1 
ATOM   3824 O  OG  . SER   B 1 130 ? 38.269  -10.871 -21.372 1 59.78 ? 115 SER   B OG  1 
ATOM   3825 N  N   . LYS   B 1 131 ? 37.914  -15.15  -20.074 1 59.95 ? 116 LYS   B N   1 
ATOM   3826 C  CA  . LYS   B 1 131 ? 37.394  -16.508 -19.886 1 60.23 ? 116 LYS   B CA  1 
ATOM   3827 C  C   . LYS   B 1 131 ? 37.444  -16.886 -18.39  1 59.93 ? 116 LYS   B C   1 
ATOM   3828 O  O   . LYS   B 1 131 ? 36.505  -17.5   -17.876 1 60.28 ? 116 LYS   B O   1 
ATOM   3829 C  CB  . LYS   B 1 131 ? 38.248  -17.498 -20.697 1 62.72 ? 116 LYS   B CB  1 
ATOM   3830 C  CG  . LYS   B 1 131 ? 37.8    -18.952 -20.6   1 67.55 ? 116 LYS   B CG  1 
ATOM   3831 C  CD  . LYS   B 1 131 ? 38.692  -19.867 -21.443 1 72.14 ? 116 LYS   B CD  1 
ATOM   3832 N  N   . LYS   B 1 132 ? 38.526  -16.483 -17.699 1 58.94 ? 117 LYS   B N   1 
ATOM   3833 C  CA  . LYS   B 1 132 ? 38.733  -16.713 -16.277 1 59.17 ? 117 LYS   B CA  1 
ATOM   3834 C  C   . LYS   B 1 132 ? 37.654  -16.011 -15.439 1 59.59 ? 117 LYS   B C   1 
ATOM   3835 O  O   . LYS   B 1 132 ? 37.092  -16.622 -14.529 1 59.74 ? 117 LYS   B O   1 
ATOM   3836 C  CB  . LYS   B 1 132 ? 40.135  -16.239 -15.851 1 60.4  ? 117 LYS   B CB  1 
ATOM   3837 N  N   . LEU   B 1 133 ? 37.344  -14.74  -15.766 1 59.04 ? 118 LEU   B N   1 
ATOM   3838 C  CA  . LEU   B 1 133 ? 36.339  -13.976 -15.029 1 58.43 ? 118 LEU   B CA  1 
ATOM   3839 C  C   . LEU   B 1 133 ? 34.91   -14.112 -15.559 1 57.56 ? 118 LEU   B C   1 
ATOM   3840 O  O   . LEU   B 1 133 ? 34.01   -13.476 -15.011 1 57.2  ? 118 LEU   B O   1 
ATOM   3841 C  CB  . LEU   B 1 133 ? 36.735  -12.501 -14.976 1 58.71 ? 118 LEU   B CB  1 
ATOM   3842 C  CG  . LEU   B 1 133 ? 37.947  -12.179 -14.128 1 60.21 ? 118 LEU   B CG  1 
ATOM   3843 C  CD1 . LEU   B 1 133 ? 38.495  -10.839 -14.492 1 61.08 ? 118 LEU   B CD1 1 
ATOM   3844 C  CD2 . LEU   B 1 133 ? 37.605  -12.196 -12.649 1 60.64 ? 118 LEU   B CD2 1 
ATOM   3845 N  N   . GLU   B 1 134 ? 34.703  -14.942 -16.603 1 56.83 ? 119 GLU   B N   1 
ATOM   3846 C  CA  . GLU   B 1 134 ? 33.418  -15.19  -17.244 1 56.81 ? 119 GLU   B CA  1 
ATOM   3847 C  C   . GLU   B 1 134 ? 32.785  -13.909 -17.764 1 56.59 ? 119 GLU   B C   1 
ATOM   3848 O  O   . GLU   B 1 134 ? 31.584  -13.684 -17.61  1 57.42 ? 119 GLU   B O   1 
ATOM   3849 C  CB  . GLU   B 1 134 ? 32.459  -15.963 -16.339 1 59.26 ? 119 GLU   B CB  1 
ATOM   3850 C  CG  . GLU   B 1 134 ? 32.984  -17.32  -15.915 1 63.89 ? 119 GLU   B CG  1 
ATOM   3851 C  CD  . GLU   B 1 134 ? 31.97   -18.107 -15.111 1 70.65 ? 119 GLU   B CD  1 
ATOM   3852 O  OE1 . GLU   B 1 134 ? 30.872  -18.383 -15.647 1 71.73 ? 119 GLU   B OE1 1 
ATOM   3853 O  OE2 . GLU   B 1 134 ? 32.264  -18.426 -13.935 1 72.75 ? 119 GLU   B OE2 1 
ATOM   3854 N  N   . LEU   B 1 135 ? 33.6    -13.069 -18.385 1 55.04 ? 120 LEU   B N   1 
ATOM   3855 C  CA  . LEU   B 1 135 ? 33.172  -11.815 -18.979 1 54.18 ? 120 LEU   B CA  1 
ATOM   3856 C  C   . LEU   B 1 135 ? 33.68   -11.766 -20.429 1 54    ? 120 LEU   B C   1 
ATOM   3857 O  O   . LEU   B 1 135 ? 34.731  -12.337 -20.735 1 54.51 ? 120 LEU   B O   1 
ATOM   3858 C  CB  . LEU   B 1 135 ? 33.74   -10.643 -18.163 1 53.8  ? 120 LEU   B CB  1 
ATOM   3859 C  CG  . LEU   B 1 135 ? 33.056  -10.389 -16.825 1 54.63 ? 120 LEU   B CG  1 
ATOM   3860 C  CD1 . LEU   B 1 135 ? 33.864  -9.44   -15.961 1 54.9  ? 120 LEU   B CD1 1 
ATOM   3861 C  CD2 . LEU   B 1 135 ? 31.659  -9.862  -17.033 1 54.86 ? 120 LEU   B CD2 1 
ATOM   3862 N  N   . PRO   B 1 136 ? 32.943  -11.128 -21.353 1 52.86 ? 121 PRO   B N   1 
ATOM   3863 C  CA  . PRO   B 1 136 ? 33.415  -11.067 -22.753 1 51.94 ? 121 PRO   B CA  1 
ATOM   3864 C  C   . PRO   B 1 136 ? 34.671  -10.203 -22.925 1 50.79 ? 121 PRO   B C   1 
ATOM   3865 O  O   . PRO   B 1 136 ? 34.915  -9.302  -22.116 1 50.88 ? 121 PRO   B O   1 
ATOM   3866 C  CB  . PRO   B 1 136 ? 32.208  -10.483 -23.505 1 52.71 ? 121 PRO   B CB  1 
ATOM   3867 C  CG  . PRO   B 1 136 ? 31.461  -9.731  -22.478 1 53.25 ? 121 PRO   B CG  1 
ATOM   3868 C  CD  . PRO   B 1 136 ? 31.662  -10.424 -21.17  1 51.99 ? 121 PRO   B CD  1 
ATOM   3869 N  N   . PRO   B 1 137 ? 35.504  -10.469 -23.957 1 49.72 ? 122 PRO   B N   1 
ATOM   3870 C  CA  . PRO   B 1 137 ? 36.7    -9.641  -24.16  1 49.02 ? 122 PRO   B CA  1 
ATOM   3871 C  C   . PRO   B 1 137 ? 36.402  -8.289  -24.825 1 47.89 ? 122 PRO   B C   1 
ATOM   3872 O  O   . PRO   B 1 137 ? 36.806  -8.017  -25.958 1 48.02 ? 122 PRO   B O   1 
ATOM   3873 C  CB  . PRO   B 1 137 ? 37.591  -10.524 -25.033 1 49.78 ? 122 PRO   B CB  1 
ATOM   3874 C  CG  . PRO   B 1 137 ? 36.632  -11.315 -25.843 1 50.38 ? 122 PRO   B CG  1 
ATOM   3875 C  CD  . PRO   B 1 137 ? 35.403  -11.52  -24.987 1 49.02 ? 122 PRO   B CD  1 
ATOM   3876 N  N   . ILE   B 1 138 ? 35.704  -7.433  -24.083 1 46.23 ? 123 ILE   B N   1 
ATOM   3877 C  CA  . ILE   B 1 138 ? 35.336  -6.061  -24.432 1 44.5  ? 123 ILE   B CA  1 
ATOM   3878 C  C   . ILE   B 1 138 ? 35.106  -5.331  -23.112 1 43.39 ? 123 ILE   B C   1 
ATOM   3879 O  O   . ILE   B 1 138 ? 34.774  -5.962  -22.091 1 43.62 ? 123 ILE   B O   1 
ATOM   3880 C  CB  . ILE   B 1 138 ? 34.12   -5.97   -25.402 1 44.22 ? 123 ILE   B CB  1 
ATOM   3881 C  CG1 . ILE   B 1 138 ? 33.997  -4.534  -26.003 1 44.8  ? 123 ILE   B CG1 1 
ATOM   3882 C  CG2 . ILE   B 1 138 ? 32.819  -6.422  -24.736 1 44    ? 123 ILE   B CG2 1 
ATOM   3883 C  CD1 . ILE   B 1 138 ? 32.976  -4.342  -27.075 1 44.97 ? 123 ILE   B CD1 1 
ATOM   3884 N  N   . LEU   B 1 139 ? 35.345  -4.02   -23.099 1 42.04 ? 124 LEU   B N   1 
ATOM   3885 C  CA  . LEU   B 1 139 ? 35.124  -3.194  -21.915 1 41.49 ? 124 LEU   B CA  1 
ATOM   3886 C  C   . LEU   B 1 139 ? 33.627  -3.23   -21.54  1 40.69 ? 124 LEU   B C   1 
ATOM   3887 O  O   . LEU   B 1 139 ? 32.769  -2.981  -22.39  1 40.33 ? 124 LEU   B O   1 
ATOM   3888 C  CB  . LEU   B 1 139 ? 35.544  -1.748  -22.214 1 41.32 ? 124 LEU   B CB  1 
ATOM   3889 C  CG  . LEU   B 1 139 ? 35.637  -0.82   -21.009 1 42.68 ? 124 LEU   B CG  1 
ATOM   3890 C  CD1 . LEU   B 1 139 ? 36.809  -1.205  -20.126 1 43.21 ? 124 LEU   B CD1 1 
ATOM   3891 C  CD2 . LEU   B 1 139 ? 35.772  0.649   -21.449 1 43.14 ? 124 LEU   B CD2 1 
ATOM   3892 N  N   . VAL   B 1 140 ? 33.325  -3.624  -20.301 1 40.1  ? 125 VAL   B N   1 
ATOM   3893 C  CA  . VAL   B 1 140 ? 31.944  -3.685  -19.812 1 39.76 ? 125 VAL   B CA  1 
ATOM   3894 C  C   . VAL   B 1 140 ? 31.736  -2.638  -18.699 1 38.89 ? 125 VAL   B C   1 
ATOM   3895 O  O   . VAL   B 1 140 ? 32.699  -2.045  -18.23  1 39.06 ? 125 VAL   B O   1 
ATOM   3896 C  CB  . VAL   B 1 140 ? 31.51   -5.132  -19.369 1 40.13 ? 125 VAL   B CB  1 
ATOM   3897 C  CG1 . VAL   B 1 140 ? 31.61   -6.139  -20.51  1 40.45 ? 125 VAL   B CG1 1 
ATOM   3898 C  CG2 . VAL   B 1 140 ? 32.288  -5.597  -18.144 1 40.25 ? 125 VAL   B CG2 1 
ATOM   3899 N  N   . TYR   B 1 141 ? 30.485  -2.417  -18.278 1 38.2  ? 126 TYR   B N   1 
ATOM   3900 C  CA  . TYR   B 1 141 ? 30.098  -1.53   -17.184 1 38.03 ? 126 TYR   B CA  1 
ATOM   3901 C  C   . TYR   B 1 141 ? 30.84   -1.871  -15.867 1 38.87 ? 126 TYR   B C   1 
ATOM   3902 O  O   . TYR   B 1 141 ? 31.309  -0.973  -15.16  1 39.36 ? 126 TYR   B O   1 
ATOM   3903 C  CB  . TYR   B 1 141 ? 28.58   -1.67   -17.001 1 37.48 ? 126 TYR   B CB  1 
ATOM   3904 C  CG  . TYR   B 1 141 ? 27.98   -0.762  -15.962 1 37.13 ? 126 TYR   B CG  1 
ATOM   3905 C  CD1 . TYR   B 1 141 ? 27.623  0.544   -16.274 1 37.38 ? 126 TYR   B CD1 1 
ATOM   3906 C  CD2 . TYR   B 1 141 ? 27.725  -1.219  -14.678 1 37.47 ? 126 TYR   B CD2 1 
ATOM   3907 C  CE1 . TYR   B 1 141 ? 27.057  1.378   -15.327 1 37.67 ? 126 TYR   B CE1 1 
ATOM   3908 C  CE2 . TYR   B 1 141 ? 27.167  -0.389  -13.719 1 38.38 ? 126 TYR   B CE2 1 
ATOM   3909 C  CZ  . TYR   B 1 141 ? 26.826  0.904   -14.053 1 38.89 ? 126 TYR   B CZ  1 
ATOM   3910 O  OH  . TYR   B 1 141 ? 26.263  1.709   -13.111 1 41.23 ? 126 TYR   B OH  1 
ATOM   3911 N  N   . ALA   B 1 142 ? 30.971  -3.165  -15.546 1 39.23 ? 127 ALA   B N   1 
ATOM   3912 C  CA  . ALA   B 1 142 ? 31.708  -3.603  -14.352 1 39.95 ? 127 ALA   B CA  1 
ATOM   3913 C  C   . ALA   B 1 142 ? 33.206  -3.232  -14.395 1 40.75 ? 127 ALA   B C   1 
ATOM   3914 O  O   . ALA   B 1 142 ? 33.862  -3.207  -13.351 1 41.56 ? 127 ALA   B O   1 
ATOM   3915 C  CB  . ALA   B 1 142 ? 31.532  -5.107  -14.122 1 39.74 ? 127 ALA   B CB  1 
ATOM   3916 N  N   . ASP   B 1 143 ? 33.741  -2.932  -15.587 1 39.95 ? 128 ASP   B N   1 
ATOM   3917 C  CA  . ASP   B 1 143 ? 35.126  -2.483  -15.723 1 39.45 ? 128 ASP   B CA  1 
ATOM   3918 C  C   . ASP   B 1 143 ? 35.181  -0.956  -15.617 1 39.42 ? 128 ASP   B C   1 
ATOM   3919 O  O   . ASP   B 1 143 ? 35.758  -0.439  -14.656 1 39.8  ? 128 ASP   B O   1 
ATOM   3920 C  CB  . ASP   B 1 143 ? 35.759  -2.917  -17.069 1 39.47 ? 128 ASP   B CB  1 
ATOM   3921 C  CG  . ASP   B 1 143 ? 35.758  -4.397  -17.376 1 41.57 ? 128 ASP   B CG  1 
ATOM   3922 O  OD1 . ASP   B 1 143 ? 36.056  -5.195  -16.462 1 42.77 ? 128 ASP   B OD1 1 
ATOM   3923 O  OD2 . ASP   B 1 143 ? 35.502  -4.757  -18.543 1 40.94 ? 128 ASP   B OD2 1 
ATOM   3924 N  N   . CYS   B 1 144 ? 34.556  -0.229  -16.569 1 38.91 ? 129 CYS   B N   1 
ATOM   3925 C  CA  . CYS   B 1 144 ? 34.675  1.234   -16.625 1 38.91 ? 129 CYS   B CA  1 
ATOM   3926 C  C   . CYS   B 1 144 ? 33.938  1.979   -15.533 1 39.17 ? 129 CYS   B C   1 
ATOM   3927 O  O   . CYS   B 1 144 ? 34.227  3.162   -15.345 1 39.18 ? 129 CYS   B O   1 
ATOM   3928 C  CB  . CYS   B 1 144 ? 34.323  1.788   -18.009 1 39.14 ? 129 CYS   B CB  1 
ATOM   3929 S  SG  . CYS   B 1 144 ? 32.636  1.427   -18.572 1 40.94 ? 129 CYS   B SG  1 
ATOM   3930 N  N   . VAL   B 1 145 ? 32.992  1.345   -14.824 1 39.71 ? 130 VAL   B N   1 
ATOM   3931 C  CA  . VAL   B 1 145 ? 32.271  2.047   -13.757 1 40.58 ? 130 VAL   B CA  1 
ATOM   3932 C  C   . VAL   B 1 145 ? 32.556  1.419   -12.391 1 42.12 ? 130 VAL   B C   1 
ATOM   3933 O  O   . VAL   B 1 145 ? 33.09   2.087   -11.508 1 43.04 ? 130 VAL   B O   1 
ATOM   3934 C  CB  . VAL   B 1 145 ? 30.746  2.226   -14.022 1 40.99 ? 130 VAL   B CB  1 
ATOM   3935 C  CG1 . VAL   B 1 145 ? 30.034  2.807   -12.799 1 41.15 ? 130 VAL   B CG1 1 
ATOM   3936 C  CG2 . VAL   B 1 145 ? 30.487  3.093   -15.248 1 41.35 ? 130 VAL   B CG2 1 
ATOM   3937 N  N   . LEU   B 1 146 ? 32.258  0.133   -12.237 1 42.48 ? 131 LEU   B N   1 
ATOM   3938 C  CA  . LEU   B 1 146 ? 32.367  -0.546  -10.957 1 43.55 ? 131 LEU   B CA  1 
ATOM   3939 C  C   . LEU   B 1 146 ? 33.789  -0.744  -10.443 1 44.84 ? 131 LEU   B C   1 
ATOM   3940 O  O   . LEU   B 1 146 ? 33.986  -0.757  -9.227  1 44.97 ? 131 LEU   B O   1 
ATOM   3941 C  CB  . LEU   B 1 146 ? 31.621  -1.888  -10.986 1 43.11 ? 131 LEU   B CB  1 
ATOM   3942 C  CG  . LEU   B 1 146 ? 30.19   -1.857  -11.508 1 44.07 ? 131 LEU   B CG  1 
ATOM   3943 C  CD1 . LEU   B 1 146 ? 29.599  -3.255  -11.499 1 44.3  ? 131 LEU   B CD1 1 
ATOM   3944 C  CD2 . LEU   B 1 146 ? 29.314  -0.881  -10.704 1 44.89 ? 131 LEU   B CD2 1 
ATOM   3945 N  N   . ALA   B 1 147 ? 34.766  -0.907  -11.339 1 45.22 ? 132 ALA   B N   1 
ATOM   3946 C  CA  . ALA   B 1 147 ? 36.153  -1.103  -10.911 1 46.03 ? 132 ALA   B CA  1 
ATOM   3947 C  C   . ALA   B 1 147 ? 37.09   0.064   -11.29  1 46.59 ? 132 ALA   B C   1 
ATOM   3948 O  O   . ALA   B 1 147 ? 38.276  0       -10.983 1 46.75 ? 132 ALA   B O   1 
ATOM   3949 C  CB  . ALA   B 1 147 ? 36.689  -2.411  -11.476 1 46.1  ? 132 ALA   B CB  1 
ATOM   3950 N  N   . ASN   B 1 148 ? 36.565  1.115   -11.951 1 46.62 ? 133 ASN   B N   1 
ATOM   3951 C  CA  . ASN   B 1 148 ? 37.342  2.262   -12.421 1 47.37 ? 133 ASN   B CA  1 
ATOM   3952 C  C   . ASN   B 1 148 ? 37.269  3.447   -11.451 1 48.46 ? 133 ASN   B C   1 
ATOM   3953 O  O   . ASN   B 1 148 ? 36.944  4.576   -11.858 1 47.98 ? 133 ASN   B O   1 
ATOM   3954 C  CB  . ASN   B 1 148 ? 36.831  2.655   -13.808 1 47.95 ? 133 ASN   B CB  1 
ATOM   3955 C  CG  . ASN   B 1 148 ? 37.701  3.597   -14.591 1 49.23 ? 133 ASN   B CG  1 
ATOM   3956 O  OD1 . ASN   B 1 148 ? 38.879  3.771   -14.296 1 49.87 ? 133 ASN   B OD1 1 
ATOM   3957 N  ND2 . ASN   B 1 148 ? 37.121  4.221   -15.607 1 49.15 ? 133 ASN   B ND2 1 
ATOM   3958 N  N   . TRP   B 1 149 ? 37.583  3.197   -10.171 1 49.61 ? 134 TRP   B N   1 
ATOM   3959 C  CA  . TRP   B 1 149 ? 37.485  4.267   -9.183  1 51.56 ? 134 TRP   B CA  1 
ATOM   3960 C  C   . TRP   B 1 149 ? 38.426  4.109   -7.991  1 52.7  ? 134 TRP   B C   1 
ATOM   3961 O  O   . TRP   B 1 149 ? 38.932  3.022   -7.733  1 52.07 ? 134 TRP   B O   1 
ATOM   3962 C  CB  . TRP   B 1 149 ? 36.024  4.421   -8.72   1 51.77 ? 134 TRP   B CB  1 
ATOM   3963 C  CG  . TRP   B 1 149 ? 35.53   3.276   -7.885  1 53.36 ? 134 TRP   B CG  1 
ATOM   3964 C  CD1 . TRP   B 1 149 ? 35.032  2.084   -8.325  1 54.59 ? 134 TRP   B CD1 1 
ATOM   3965 C  CD2 . TRP   B 1 149 ? 35.477  3.229   -6.453  1 54.12 ? 134 TRP   B CD2 1 
ATOM   3966 N  NE1 . TRP   B 1 149 ? 34.695  1.284   -7.252  1 55.08 ? 134 TRP   B NE1 1 
ATOM   3967 C  CE2 . TRP   B 1 149 ? 34.94   1.974   -6.091  1 55.09 ? 134 TRP   B CE2 1 
ATOM   3968 C  CE3 . TRP   B 1 149 ? 35.846  4.125   -5.439  1 54.82 ? 134 TRP   B CE3 1 
ATOM   3969 C  CZ2 . TRP   B 1 149 ? 34.768  1.598   -4.76   1 55.82 ? 134 TRP   B CZ2 1 
ATOM   3970 C  CZ3 . TRP   B 1 149 ? 35.688  3.742   -4.124  1 55.82 ? 134 TRP   B CZ3 1 
ATOM   3971 C  CH2 . TRP   B 1 149 ? 35.155  2.494   -3.796  1 55.96 ? 134 TRP   B CH2 1 
ATOM   3972 N  N   . LYS   B 1 150 ? 38.638  5.217   -7.263  1 54.1  ? 135 LYS   B N   1 
ATOM   3973 C  CA  . LYS   B 1 150 ? 39.466  5.281   -6.066  1 56.27 ? 135 LYS   B CA  1 
ATOM   3974 C  C   . LYS   B 1 150 ? 39.01   6.423   -5.167  1 57.83 ? 135 LYS   B C   1 
ATOM   3975 O  O   . LYS   B 1 150 ? 38.388  7.384   -5.623  1 57.97 ? 135 LYS   B O   1 
ATOM   3976 C  CB  . LYS   B 1 150 ? 40.959  5.477   -6.432  1 58.64 ? 135 LYS   B CB  1 
ATOM   3977 C  CG  . LYS   B 1 150 ? 41.251  6.82    -7.104  1 63.55 ? 135 LYS   B CG  1 
ATOM   3978 C  CD  . LYS   B 1 150 ? 42.744  7.072   -7.31   1 68.36 ? 135 LYS   B CD  1 
ATOM   3979 C  CE  . LYS   B 1 150 ? 43.452  7.467   -6.03   1 72.51 ? 135 LYS   B CE  1 
ATOM   3980 N  NZ  . LYS   B 1 150 ? 44.842  7.935   -6.285  1 74.89 ? 135 LYS   B NZ  1 
ATOM   3981 N  N   . LYS   B 1 151 ? 39.328  6.321   -3.882  1 59.08 ? 136 LYS   B N   1 
ATOM   3982 C  CA  . LYS   B 1 151 ? 39.094  7.418   -2.944  1 60.47 ? 136 LYS   B CA  1 
ATOM   3983 C  C   . LYS   B 1 151 ? 40.403  8.227   -2.931  1 61.58 ? 136 LYS   B C   1 
ATOM   3984 O  O   . LYS   B 1 151 ? 41.485  7.643   -2.893  1 61.71 ? 136 LYS   B O   1 
ATOM   3985 C  CB  . LYS   B 1 151 ? 38.834  6.885   -1.526  1 62.09 ? 136 LYS   B CB  1 
ATOM   3986 C  CG  . LYS   B 1 151 ? 37.384  6.928   -1.079  1 65.92 ? 136 LYS   B CG  1 
ATOM   3987 C  CD  . LYS   B 1 151 ? 37.286  6.529   0.387   1 70.51 ? 136 LYS   B CD  1 
ATOM   3988 C  CE  . LYS   B 1 151 ? 35.868  6.35    0.868   1 74.12 ? 136 LYS   B CE  1 
ATOM   3989 N  NZ  . LYS   B 1 151 ? 35.812  6.154   2.341   1 76.27 ? 136 LYS   B NZ  1 
ATOM   3990 N  N   . LYS   B 1 152 ? 40.311  9.554   -2.967  1 62.55 ? 137 LYS   B N   1 
ATOM   3991 C  CA  . LYS   B 1 152 ? 41.49   10.42   -2.877  1 63.95 ? 137 LYS   B CA  1 
ATOM   3992 C  C   . LYS   B 1 152 ? 42.047  10.294  -1.452  1 65.79 ? 137 LYS   B C   1 
ATOM   3993 O  O   . LYS   B 1 152 ? 43.232  10.028  -1.28   1 66.39 ? 137 LYS   B O   1 
ATOM   3994 C  CB  . LYS   B 1 152 ? 41.121  11.886  -3.183  1 64.4  ? 137 LYS   B CB  1 
ATOM   3995 C  CG  . LYS   B 1 152 ? 40.793  12.129  -4.639  1 66.21 ? 137 LYS   B CG  1 
ATOM   3996 C  CD  . LYS   B 1 152 ? 40.256  13.53   -4.859  1 69.4  ? 137 LYS   B CD  1 
ATOM   3997 C  CE  . LYS   B 1 152 ? 40.104  13.826  -6.331  1 72.3  ? 137 LYS   B CE  1 
ATOM   3998 N  NZ  . LYS   B 1 152 ? 39.411  15.113  -6.547  1 74.08 ? 137 LYS   B NZ  1 
ATOM   3999 N  N   . ASP   B 1 153 ? 41.171  10.401  -0.444  1 66.73 ? 138 ASP   B N   1 
ATOM   4000 C  CA  . ASP   B 1 153 ? 41.52   10.252  0.965   1 68.36 ? 138 ASP   B CA  1 
ATOM   4001 C  C   . ASP   B 1 153 ? 40.687  9.108   1.541   1 69.66 ? 138 ASP   B C   1 
ATOM   4002 O  O   . ASP   B 1 153 ? 39.476  9.249   1.709   1 69.78 ? 138 ASP   B O   1 
ATOM   4003 C  CB  . ASP   B 1 153 ? 41.233  11.56   1.734   1 70.32 ? 138 ASP   B CB  1 
ATOM   4004 C  CG  . ASP   B 1 153 ? 41.672  11.573  3.192   1 74.84 ? 138 ASP   B CG  1 
ATOM   4005 O  OD1 . ASP   B 1 153 ? 42.294  10.578  3.639   1 75.7  ? 138 ASP   B OD1 1 
ATOM   4006 O  OD2 . ASP   B 1 153 ? 41.394  12.576  3.883   1 76.75 ? 138 ASP   B OD2 1 
ATOM   4007 N  N   . PRO   B 1 154 ? 41.331  7.981   1.89    1 70.51 ? 139 PRO   B N   1 
ATOM   4008 C  CA  . PRO   B 1 154 ? 40.577  6.839   2.447   1 71.13 ? 139 PRO   B CA  1 
ATOM   4009 C  C   . PRO   B 1 154 ? 39.807  7.123   3.743   1 71.95 ? 139 PRO   B C   1 
ATOM   4010 O  O   . PRO   B 1 154 ? 38.91   6.355   4.108   1 72.32 ? 139 PRO   B O   1 
ATOM   4011 C  CB  . PRO   B 1 154 ? 41.652  5.763   2.659   1 71.76 ? 139 PRO   B CB  1 
ATOM   4012 C  CG  . PRO   B 1 154 ? 42.797  6.172   1.787   1 72.2  ? 139 PRO   B CG  1 
ATOM   4013 C  CD  . PRO   B 1 154 ? 42.767  7.674   1.747   1 70.34 ? 139 PRO   B CD  1 
ATOM   4014 N  N   . ASN   B 1 155 ? 40.139  8.218   4.433   1 71.92 ? 140 ASN   B N   1 
ATOM   4015 C  CA  . ASN   B 1 155 ? 39.451  8.578   5.678   1 72.31 ? 140 ASN   B CA  1 
ATOM   4016 C  C   . ASN   B 1 155 ? 38.265  9.532   5.476   1 72.1  ? 140 ASN   B C   1 
ATOM   4017 O  O   . ASN   B 1 155 ? 37.591  9.871   6.448   1 72.52 ? 140 ASN   B O   1 
ATOM   4018 C  CB  . ASN   B 1 155 ? 40.433  9.132   6.714   1 73.88 ? 140 ASN   B CB  1 
ATOM   4019 C  CG  . ASN   B 1 155 ? 41.675  8.285   6.863   1 77.63 ? 140 ASN   B CG  1 
ATOM   4020 O  OD1 . ASN   B 1 155 ? 41.608  7.08    7.169   1 79.06 ? 140 ASN   B OD1 1 
ATOM   4021 N  ND2 . ASN   B 1 155 ? 42.834  8.898   6.618   1 77.86 ? 140 ASN   B ND2 1 
ATOM   4022 N  N   . LYS   B 1 156 ? 38.005  9.963   4.229   1 71.14 ? 141 LYS   B N   1 
ATOM   4023 C  CA  . LYS   B 1 156 ? 36.873  10.825  3.899   1 70.51 ? 141 LYS   B CA  1 
ATOM   4024 C  C   . LYS   B 1 156 ? 35.765  9.978   3.195   1 69.41 ? 141 LYS   B C   1 
ATOM   4025 O  O   . LYS   B 1 156 ? 36.065  8.904   2.672   1 69.35 ? 141 LYS   B O   1 
ATOM   4026 C  CB  . LYS   B 1 156 ? 37.347  12.034  3.069   1 72.19 ? 141 LYS   B CB  1 
ATOM   4027 N  N   . PRO   B 1 157 ? 34.483  10.398  3.215   1 68.37 ? 142 PRO   B N   1 
ATOM   4028 C  CA  . PRO   B 1 157 ? 33.417  9.542   2.647   1 68.02 ? 142 PRO   B CA  1 
ATOM   4029 C  C   . PRO   B 1 157 ? 33.362  9.414   1.104   1 67.44 ? 142 PRO   B C   1 
ATOM   4030 O  O   . PRO   B 1 157 ? 34.142  10.043  0.387   1 67.66 ? 142 PRO   B O   1 
ATOM   4031 C  CB  . PRO   B 1 157 ? 32.131  10.163  3.214   1 68.71 ? 142 PRO   B CB  1 
ATOM   4032 C  CG  . PRO   B 1 157 ? 32.476  11.574  3.484   1 69.13 ? 142 PRO   B CG  1 
ATOM   4033 C  CD  . PRO   B 1 157 ? 33.93   11.613  3.845   1 67.62 ? 142 PRO   B CD  1 
ATOM   4034 N  N   . LEU   B 1 158 ? 32.444  8.565   0.595   1 66.28 ? 143 LEU   B N   1 
ATOM   4035 C  CA  . LEU   B 1 158 ? 32.263  8.328   -0.834  1 65.32 ? 143 LEU   B CA  1 
ATOM   4036 C  C   . LEU   B 1 158 ? 31.464  9.445   -1.474  1 64.76 ? 143 LEU   B C   1 
ATOM   4037 O  O   . LEU   B 1 158 ? 30.269  9.307   -1.737  1 64.38 ? 143 LEU   B O   1 
ATOM   4038 C  CB  . LEU   B 1 158 ? 31.566  6.992   -1.069  1 65.15 ? 143 LEU   B CB  1 
ATOM   4039 C  CG  . LEU   B 1 158 ? 32.399  5.758   -0.819  1 66.25 ? 143 LEU   B CG  1 
ATOM   4040 C  CD1 . LEU   B 1 158 ? 31.515  4.537   -0.738  1 66.9  ? 143 LEU   B CD1 1 
ATOM   4041 C  CD2 . LEU   B 1 158 ? 33.455  5.591   -1.885  1 66.35 ? 143 LEU   B CD2 1 
ATOM   4042 N  N   . THR   B 1 159 ? 32.131  10.563  -1.712  1 64.29 ? 144 THR   B N   1 
ATOM   4043 C  CA  . THR   B 1 159 ? 31.546  11.743  -2.337  1 64.13 ? 144 THR   B CA  1 
ATOM   4044 C  C   . THR   B 1 159 ? 32.359  12.082  -3.588  1 63.12 ? 144 THR   B C   1 
ATOM   4045 O  O   . THR   B 1 159 ? 33.523  11.692  -3.68   1 63.44 ? 144 THR   B O   1 
ATOM   4046 C  CB  . THR   B 1 159 ? 31.504  12.894  -1.326  1 66.24 ? 144 THR   B CB  1 
ATOM   4047 O  OG1 . THR   B 1 159 ? 31.031  14.075  -1.967  1 68.33 ? 144 THR   B OG1 1 
ATOM   4048 C  CG2 . THR   B 1 159 ? 32.86   13.158  -0.683  1 66.71 ? 144 THR   B CG2 1 
ATOM   4049 N  N   . TYR   B 1 160 ? 31.766  12.8    -4.558  1 61.86 ? 145 TYR   B N   1 
ATOM   4050 C  CA  . TYR   B 1 160 ? 32.464  13.153  -5.804  1 61.21 ? 145 TYR   B CA  1 
ATOM   4051 C  C   . TYR   B 1 160 ? 33.807  13.85   -5.559  1 60.5  ? 145 TYR   B C   1 
ATOM   4052 O  O   . TYR   B 1 160 ? 34.81   13.499  -6.19   1 60.47 ? 145 TYR   B O   1 
ATOM   4053 C  CB  . TYR   B 1 160 ? 31.58   14.023  -6.72   1 61.08 ? 145 TYR   B CB  1 
ATOM   4054 C  CG  . TYR   B 1 160 ? 32.136  14.16   -8.121  1 61.35 ? 145 TYR   B CG  1 
ATOM   4055 C  CD1 . TYR   B 1 160 ? 33.031  15.173  -8.44   1 61.99 ? 145 TYR   B CD1 1 
ATOM   4056 C  CD2 . TYR   B 1 160 ? 31.788  13.261  -9.119  1 61.92 ? 145 TYR   B CD2 1 
ATOM   4057 C  CE1 . TYR   B 1 160 ? 33.592  15.267  -9.704  1 62.82 ? 145 TYR   B CE1 1 
ATOM   4058 C  CE2 . TYR   B 1 160 ? 32.31   13.369  -10.4   1 62.67 ? 145 TYR   B CE2 1 
ATOM   4059 C  CZ  . TYR   B 1 160 ? 33.211  14.379  -10.691 1 63.56 ? 145 TYR   B CZ  1 
ATOM   4060 O  OH  . TYR   B 1 160 ? 33.745  14.514  -11.948 1 64.52 ? 145 TYR   B OH  1 
ATOM   4061 N  N   . GLU   B 1 161 ? 33.824  14.807  -4.612  1 59.65 ? 146 GLU   B N   1 
ATOM   4062 C  CA  . GLU   B 1 161 ? 35.017  15.566  -4.241  1 59.07 ? 146 GLU   B CA  1 
ATOM   4063 C  C   . GLU   B 1 161 ? 36.15   14.667  -3.754  1 58.2  ? 146 GLU   B C   1 
ATOM   4064 O  O   . GLU   B 1 161 ? 37.315  14.967  -3.997  1 58.69 ? 146 GLU   B O   1 
ATOM   4065 C  CB  . GLU   B 1 161 ? 34.668  16.622  -3.184  1 60.99 ? 146 GLU   B CB  1 
ATOM   4066 N  N   . ASN   B 1 162 ? 35.817  13.56   -3.097  1 57.14 ? 147 ASN   B N   1 
ATOM   4067 C  CA  . ASN   B 1 162 ? 36.821  12.636  -2.576  1 57.07 ? 147 ASN   B CA  1 
ATOM   4068 C  C   . ASN   B 1 162 ? 37.064  11.421  -3.488  1 56.81 ? 147 ASN   B C   1 
ATOM   4069 O  O   . ASN   B 1 162 ? 37.605  10.407  -3.033  1 57.17 ? 147 ASN   B O   1 
ATOM   4070 C  CB  . ASN   B 1 162 ? 36.419  12.169  -1.177  1 57.98 ? 147 ASN   B CB  1 
ATOM   4071 C  CG  . ASN   B 1 162 ? 37.525  11.451  -0.473  1 61.21 ? 147 ASN   B CG  1 
ATOM   4072 O  OD1 . ASN   B 1 162 ? 38.666  11.905  -0.468  1 62.86 ? 147 ASN   B OD1 1 
ATOM   4073 N  ND2 . ASN   B 1 162 ? 37.233  10.277  0.07    1 61.85 ? 147 ASN   B ND2 1 
ATOM   4074 N  N   . MET   B 1 163 ? 36.672  11.502  -4.763  1 55.94 ? 148 MET   B N   1 
ATOM   4075 C  CA  . MET   B 1 163 ? 36.841  10.369  -5.669  1 55.51 ? 148 MET   B CA  1 
ATOM   4076 C  C   . MET   B 1 163 ? 37.427  10.758  -6.993  1 54.75 ? 148 MET   B C   1 
ATOM   4077 O  O   . MET   B 1 163 ? 37.347  11.918  -7.399  1 54.61 ? 148 MET   B O   1 
ATOM   4078 C  CB  . MET   B 1 163 ? 35.5    9.639   -5.874  1 56.16 ? 148 MET   B CB  1 
ATOM   4079 C  CG  . MET   B 1 163 ? 35.016  8.905   -4.644  1 58.07 ? 148 MET   B CG  1 
ATOM   4080 S  SD  . MET   B 1 163 ? 33.263  8.554   -4.748  1 58.83 ? 148 MET   B SD  1 
ATOM   4081 C  CE  . MET   B 1 163 ? 33.342  6.924   -5.38   1 55.71 ? 148 MET   B CE  1 
ATOM   4082 N  N   . ASP   B 1 164 ? 37.974  9.755   -7.687  1 54.06 ? 149 ASP   B N   1 
ATOM   4083 C  CA  . ASP   B 1 164 ? 38.533  9.887   -9.012  1 53.99 ? 149 ASP   B CA  1 
ATOM   4084 C  C   . ASP   B 1 164 ? 38.44   8.539   -9.754  1 52.29 ? 149 ASP   B C   1 
ATOM   4085 O  O   . ASP   B 1 164 ? 38.353  7.478   -9.132  1 52    ? 149 ASP   B O   1 
ATOM   4086 C  CB  . ASP   B 1 164 ? 40.005  10.318  -8.899  1 57.56 ? 149 ASP   B CB  1 
ATOM   4087 C  CG  . ASP   B 1 164 ? 40.51   11.139  -10.071 1 65.38 ? 149 ASP   B CG  1 
ATOM   4088 O  OD1 . ASP   B 1 164 ? 39.812  11.182  -11.122 1 66.49 ? 149 ASP   B OD1 1 
ATOM   4089 O  OD2 . ASP   B 1 164 ? 41.603  11.741  -9.944  1 68.74 ? 149 ASP   B OD2 1 
ATOM   4090 N  N   . VAL   B 1 165 ? 38.468  8.584   -11.086 1 50.92 ? 150 VAL   B N   1 
ATOM   4091 C  CA  . VAL   B 1 165 ? 38.508  7.374   -11.909 1 49.8  ? 150 VAL   B CA  1 
ATOM   4092 C  C   . VAL   B 1 165 ? 39.972  6.951   -12.061 1 49.23 ? 150 VAL   B C   1 
ATOM   4093 O  O   . VAL   B 1 165 ? 40.873  7.761   -11.82  1 49.48 ? 150 VAL   B O   1 
ATOM   4094 C  CB  . VAL   B 1 165 ? 37.831  7.558   -13.297 1 50    ? 150 VAL   B CB  1 
ATOM   4095 C  CG1 . VAL   B 1 165 ? 36.333  7.81    -13.153 1 50.2  ? 150 VAL   B CG1 1 
ATOM   4096 C  CG2 . VAL   B 1 165 ? 38.505  8.669   -14.106 1 50.28 ? 150 VAL   B CG2 1 
ATOM   4097 N  N   . LEU   B 1 166 ? 40.218  5.697   -12.449 1 48.55 ? 151 LEU   B N   1 
ATOM   4098 C  CA  . LEU   B 1 166 ? 41.578  5.233   -12.655 1 48.81 ? 151 LEU   B CA  1 
ATOM   4099 C  C   . LEU   B 1 166 ? 42.04   5.513   -14.089 1 50.43 ? 151 LEU   B C   1 
ATOM   4100 O  O   . LEU   B 1 166 ? 43.206  5.84    -14.3   1 51.08 ? 151 LEU   B O   1 
ATOM   4101 C  CB  . LEU   B 1 166 ? 41.715  3.737   -12.326 1 48.3  ? 151 LEU   B CB  1 
ATOM   4102 C  CG  . LEU   B 1 166 ? 41.282  3.307   -10.92  1 48.95 ? 151 LEU   B CG  1 
ATOM   4103 C  CD1 . LEU   B 1 166 ? 41.479  1.82    -10.734 1 48.93 ? 151 LEU   B CD1 1 
ATOM   4104 C  CD2 . LEU   B 1 166 ? 42.043  4.06    -9.847  1 49.62 ? 151 LEU   B CD2 1 
ATOM   4105 N  N   . PHE   B 1 167 ? 41.145  5.363   -15.082 1 50.76 ? 152 PHE   B N   1 
ATOM   4106 C  CA  . PHE   B 1 167 ? 41.502  5.528   -16.491 1 51.28 ? 152 PHE   B CA  1 
ATOM   4107 C  C   . PHE   B 1 167 ? 40.544  6.387   -17.287 1 50.94 ? 152 PHE   B C   1 
ATOM   4108 O  O   . PHE   B 1 167 ? 39.332  6.353   -17.078 1 51.1  ? 152 PHE   B O   1 
ATOM   4109 C  CB  . PHE   B 1 167 ? 41.658  4.161   -17.183 1 52.12 ? 152 PHE   B CB  1 
ATOM   4110 C  CG  . PHE   B 1 167 ? 42.675  3.277   -16.503 1 54.04 ? 152 PHE   B CG  1 
ATOM   4111 C  CD1 . PHE   B 1 167 ? 44.034  3.538   -16.615 1 55.46 ? 152 PHE   B CD1 1 
ATOM   4112 C  CD2 . PHE   B 1 167 ? 42.272  2.225   -15.699 1 55.06 ? 152 PHE   B CD2 1 
ATOM   4113 C  CE1 . PHE   B 1 167 ? 44.965  2.751   -15.943 1 56.44 ? 152 PHE   B CE1 1 
ATOM   4114 C  CE2 . PHE   B 1 167 ? 43.204  1.43    -15.046 1 56.09 ? 152 PHE   B CE2 1 
ATOM   4115 C  CZ  . PHE   B 1 167 ? 44.544  1.699   -15.167 1 56.11 ? 152 PHE   B CZ  1 
ATOM   4116 N  N   . SER   B 1 168 ? 41.107  7.143   -18.228 1 50.23 ? 153 SER   B N   1 
ATOM   4117 C  CA  . SER   B 1 168 ? 40.417  8.035   -19.152 1 49.48 ? 153 SER   B CA  1 
ATOM   4118 C  C   . SER   B 1 168 ? 40.857  7.711   -20.588 1 48.88 ? 153 SER   B C   1 
ATOM   4119 O  O   . SER   B 1 168 ? 41.853  7.007   -20.791 1 49    ? 153 SER   B O   1 
ATOM   4120 C  CB  . SER   B 1 168 ? 40.755  9.483   -18.825 1 50.74 ? 153 SER   B CB  1 
ATOM   4121 O  OG  . SER   B 1 168 ? 39.729  10.065  -18.039 1 53.39 ? 153 SER   B OG  1 
ATOM   4122 N  N   . PHE   B 1 169 ? 40.112  8.204   -21.583 1 48.24 ? 154 PHE   B N   1 
ATOM   4123 C  CA  . PHE   B 1 169 ? 40.448  7.941   -22.979 1 48.53 ? 154 PHE   B CA  1 
ATOM   4124 C  C   . PHE   B 1 169 ? 41.144  9.145   -23.623 1 49.48 ? 154 PHE   B C   1 
ATOM   4125 O  O   . PHE   B 1 169 ? 42.209  8.996   -24.201 1 49.93 ? 154 PHE   B O   1 
ATOM   4126 C  CB  . PHE   B 1 169 ? 39.204  7.519   -23.776 1 47.93 ? 154 PHE   B CB  1 
ATOM   4127 C  CG  . PHE   B 1 169 ? 38.661  6.178   -23.353 1 47.6  ? 154 PHE   B CG  1 
ATOM   4128 C  CD1 . PHE   B 1 169 ? 39.305  5.009   -23.715 1 47.9  ? 154 PHE   B CD1 1 
ATOM   4129 C  CD2 . PHE   B 1 169 ? 37.52   6.089   -22.574 1 47.86 ? 154 PHE   B CD2 1 
ATOM   4130 C  CE1 . PHE   B 1 169 ? 38.817  3.777   -23.308 1 48.79 ? 154 PHE   B CE1 1 
ATOM   4131 C  CE2 . PHE   B 1 169 ? 37.027  4.857   -22.177 1 48.43 ? 154 PHE   B CE2 1 
ATOM   4132 C  CZ  . PHE   B 1 169 ? 37.671  3.706   -22.553 1 48.48 ? 154 PHE   B CZ  1 
ATOM   4133 N  N   . ARG   B 1 170 ? 40.546  10.33   -23.522 1 49.38 ? 155 ARG   B N   1 
ATOM   4134 C  CA  . ARG   B 1 170 ? 41.068  11.566  -24.09  1 49.6  ? 155 ARG   B CA  1 
ATOM   4135 C  C   . ARG   B 1 170 ? 41.025  12.68   -23.061 1 50.64 ? 155 ARG   B C   1 
ATOM   4136 O  O   . ARG   B 1 170 ? 40.267  12.622  -22.091 1 50.84 ? 155 ARG   B O   1 
ATOM   4137 C  CB  . ARG   B 1 170 ? 40.246  12.003  -25.325 1 49.59 ? 155 ARG   B CB  1 
ATOM   4138 C  CG  . ARG   B 1 170 ? 40.202  10.972  -26.445 1 51.97 ? 155 ARG   B CG  1 
ATOM   4139 C  CD  . ARG   B 1 170 ? 41.584  10.64   -26.988 1 54.15 ? 155 ARG   B CD  1 
ATOM   4140 N  NE  . ARG   B 1 170 ? 42.192  11.8    -27.639 1 56.09 ? 155 ARG   B NE  1 
ATOM   4141 C  CZ  . ARG   B 1 170 ? 41.999  12.132  -28.913 1 57.27 ? 155 ARG   B CZ  1 
ATOM   4142 N  NH1 . ARG   B 1 170 ? 41.225  11.385  -29.692 1 56    ? 155 ARG   B NH1 1 
ATOM   4143 N  NH2 . ARG   B 1 170 ? 42.582  13.209  -29.418 1 57.68 ? 155 ARG   B NH2 1 
ATOM   4144 N  N   . ASP   B 1 171 ? 41.83   13.716  -23.282 1 51    ? 156 ASP   B N   1 
ATOM   4145 C  CA  . ASP   B 1 171 ? 41.835  14.875  -22.402 1 51.79 ? 156 ASP   B CA  1 
ATOM   4146 C  C   . ASP   B 1 171 ? 40.515  15.621  -22.643 1 50.5  ? 156 ASP   B C   1 
ATOM   4147 O  O   . ASP   B 1 171 ? 40.129  15.847  -23.793 1 50.47 ? 156 ASP   B O   1 
ATOM   4148 C  CB  . ASP   B 1 171 ? 43.05   15.778  -22.705 1 55.3  ? 156 ASP   B CB  1 
ATOM   4149 C  CG  . ASP   B 1 171 ? 44.387  15.203  -22.253 1 63.16 ? 156 ASP   B CG  1 
ATOM   4150 O  OD1 . ASP   B 1 171 ? 44.433  14.576  -21.16  1 63.67 ? 156 ASP   B OD1 1 
ATOM   4151 O  OD2 . ASP   B 1 171 ? 45.39   15.391  -22.983 1 67.46 ? 156 ASP   B OD2 1 
ATOM   4152 N  N   . GLY   B 1 172 ? 39.788  15.895  -21.573 1 49.49 ? 157 GLY   B N   1 
ATOM   4153 C  CA  . GLY   B 1 172 ? 38.506  16.589  -21.686 1 48.82 ? 157 GLY   B CA  1 
ATOM   4154 C  C   . GLY   B 1 172 ? 37.339  15.732  -22.141 1 47.62 ? 157 GLY   B C   1 
ATOM   4155 O  O   . GLY   B 1 172 ? 36.316  16.272  -22.549 1 47.61 ? 157 GLY   B O   1 
ATOM   4156 N  N   . ASP   B 1 173 ? 37.451  14.395  -22.049 1 46.72 ? 158 ASP   B N   1 
ATOM   4157 C  CA  . ASP   B 1 173 ? 36.348  13.507  -22.464 1 45.96 ? 158 ASP   B CA  1 
ATOM   4158 C  C   . ASP   B 1 173 ? 35.194  13.406  -21.452 1 46.41 ? 158 ASP   B C   1 
ATOM   4159 O  O   . ASP   B 1 173 ? 34.193  12.765  -21.749 1 46.8  ? 158 ASP   B O   1 
ATOM   4160 C  CB  . ASP   B 1 173 ? 36.855  12.097  -22.832 1 44.86 ? 158 ASP   B CB  1 
ATOM   4161 C  CG  . ASP   B 1 173 ? 37.525  11.326  -21.714 1 44.56 ? 158 ASP   B CG  1 
ATOM   4162 O  OD1 . ASP   B 1 173 ? 37.59   11.848  -20.588 1 43.94 ? 158 ASP   B OD1 1 
ATOM   4163 O  OD2 . ASP   B 1 173 ? 38.03   10.216  -21.98  1 45.59 ? 158 ASP   B OD2 1 
ATOM   4164 N  N   . CYS   B 1 174 ? 35.35   14.003  -20.259 1 46.51 ? 159 CYS   B N   1 
ATOM   4165 C  CA  . CYS   B 1 174 ? 34.371  13.971  -19.171 1 46.93 ? 159 CYS   B CA  1 
ATOM   4166 C  C   . CYS   B 1 174 ? 34.089  12.553  -18.665 1 47.23 ? 159 CYS   B C   1 
ATOM   4167 O  O   . CYS   B 1 174 ? 33.023  12.311  -18.105 1 47.02 ? 159 CYS   B O   1 
ATOM   4168 C  CB  . CYS   B 1 174 ? 33.087  14.705  -19.547 1 47.32 ? 159 CYS   B CB  1 
ATOM   4169 S  SG  . CYS   B 1 174 ? 33.291  16.492  -19.705 1 49.97 ? 159 CYS   B SG  1 
ATOM   4170 N  N   . SER   B 1 175 ? 35.043  11.626  -18.865 1 47.4  ? 160 SER   B N   1 
ATOM   4171 C  CA  . SER   B 1 175 ? 34.9    10.253  -18.413 1 48.12 ? 160 SER   B CA  1 
ATOM   4172 C  C   . SER   B 1 175 ? 34.867  10.175  -16.893 1 48.43 ? 160 SER   B C   1 
ATOM   4173 O  O   . SER   B 1 175 ? 34.155  9.334   -16.36  1 48.99 ? 160 SER   B O   1 
ATOM   4174 C  CB  . SER   B 1 175 ? 35.985  9.354   -18.997 1 49.21 ? 160 SER   B CB  1 
ATOM   4175 O  OG  . SER   B 1 175 ? 37.284  9.775   -18.627 1 51.38 ? 160 SER   B OG  1 
ATOM   4176 N  N   . LYS   B 1 176 ? 35.544  11.101  -16.189 1 47.48 ? 161 LYS   B N   1 
ATOM   4177 C  CA  . LYS   B 1 176 ? 35.503  11.127  -14.737 1 46.79 ? 161 LYS   B CA  1 
ATOM   4178 C  C   . LYS   B 1 176 ? 34.075  11.402  -14.255 1 46    ? 161 LYS   B C   1 
ATOM   4179 O  O   . LYS   B 1 176 ? 33.521  10.595  -13.537 1 45.91 ? 161 LYS   B O   1 
ATOM   4180 C  CB  . LYS   B 1 176 ? 36.501  12.142  -14.158 1 47.89 ? 161 LYS   B CB  1 
ATOM   4181 C  CG  . LYS   B 1 176 ? 36.502  12.137  -12.64  1 51.74 ? 161 LYS   B CG  1 
ATOM   4182 C  CD  . LYS   B 1 176 ? 37.301  13.283  -12.038 1 55.25 ? 161 LYS   B CD  1 
ATOM   4183 C  CE  . LYS   B 1 176 ? 37.124  13.323  -10.542 1 58.31 ? 161 LYS   B CE  1 
ATOM   4184 N  NZ  . LYS   B 1 176 ? 37.839  14.468  -9.935  1 60.85 ? 161 LYS   B NZ  1 
ATOM   4185 N  N   . GLY   B 1 177 ? 33.471  12.478  -14.728 1 45.55 ? 162 GLY   B N   1 
ATOM   4186 C  CA  . GLY   B 1 177 ? 32.105  12.828  -14.378 1 45.01 ? 162 GLY   B CA  1 
ATOM   4187 C  C   . GLY   B 1 177 ? 31.104  11.771  -14.782 1 45.05 ? 162 GLY   B C   1 
ATOM   4188 O  O   . GLY   B 1 177 ? 30.216  11.437  -14     1 45.39 ? 162 GLY   B O   1 
ATOM   4189 N  N   . PHE   B 1 178 ? 31.236  11.225  -16.007 1 43.87 ? 163 PHE   B N   1 
ATOM   4190 C  CA  . PHE   B 1 178 ? 30.285  10.226  -16.492 1 42.91 ? 163 PHE   B CA  1 
ATOM   4191 C  C   . PHE   B 1 178 ? 30.366  8.929   -15.674 1 42.04 ? 163 PHE   B C   1 
ATOM   4192 O  O   . PHE   B 1 178 ? 29.365  8.492   -15.123 1 41.38 ? 163 PHE   B O   1 
ATOM   4193 C  CB  . PHE   B 1 178 ? 30.511  9.963   -17.991 1 42.29 ? 163 PHE   B CB  1 
ATOM   4194 C  CG  . PHE   B 1 178 ? 29.572  8.963   -18.628 1 41.71 ? 163 PHE   B CG  1 
ATOM   4195 C  CD1 . PHE   B 1 178 ? 28.208  9.2     -18.67  1 41.84 ? 163 PHE   B CD1 1 
ATOM   4196 C  CD2 . PHE   B 1 178 ? 30.062  7.822   -19.244 1 41.51 ? 163 PHE   B CD2 1 
ATOM   4197 C  CE1 . PHE   B 1 178 ? 27.353  8.312   -19.302 1 42    ? 163 PHE   B CE1 1 
ATOM   4198 C  CE2 . PHE   B 1 178 ? 29.204  6.933   -19.876 1 42.07 ? 163 PHE   B CE2 1 
ATOM   4199 C  CZ  . PHE   B 1 178 ? 27.856  7.193   -19.914 1 41.99 ? 163 PHE   B CZ  1 
ATOM   4200 N  N   . PHE   B 1 179 ? 31.561  8.344   -15.563 1 41.95 ? 164 PHE   B N   1 
ATOM   4201 C  CA  . PHE   B 1 179 ? 31.75   7.109   -14.816 1 42.23 ? 164 PHE   B CA  1 
ATOM   4202 C  C   . PHE   B 1 179 ? 31.509  7.267   -13.319 1 43.14 ? 164 PHE   B C   1 
ATOM   4203 O  O   . PHE   B 1 179 ? 30.916  6.381   -12.721 1 43.35 ? 164 PHE   B O   1 
ATOM   4204 C  CB  . PHE   B 1 179 ? 33.129  6.491   -15.089 1 41.91 ? 164 PHE   B CB  1 
ATOM   4205 C  CG  . PHE   B 1 179 ? 33.394  6.086   -16.521 1 42.54 ? 164 PHE   B CG  1 
ATOM   4206 C  CD1 . PHE   B 1 179 ? 32.382  5.576   -17.312 1 43.43 ? 164 PHE   B CD1 1 
ATOM   4207 C  CD2 . PHE   B 1 179 ? 34.665  6.178   -17.061 1 43.49 ? 164 PHE   B CD2 1 
ATOM   4208 C  CE1 . PHE   B 1 179 ? 32.635  5.176   -18.619 1 44.03 ? 164 PHE   B CE1 1 
ATOM   4209 C  CE2 . PHE   B 1 179 ? 34.914  5.781   -18.374 1 44.18 ? 164 PHE   B CE2 1 
ATOM   4210 C  CZ  . PHE   B 1 179 ? 33.897  5.283   -19.142 1 43.67 ? 164 PHE   B CZ  1 
ATOM   4211 N  N   . LEU   B 1 180 ? 31.952  8.382   -12.707 1 43.78 ? 165 LEU   B N   1 
ATOM   4212 C  CA  . LEU   B 1 180 ? 31.784  8.601   -11.26  1 44.48 ? 165 LEU   B CA  1 
ATOM   4213 C  C   . LEU   B 1 180 ? 30.354  8.851   -10.836 1 44.83 ? 165 LEU   B C   1 
ATOM   4214 O  O   . LEU   B 1 180 ? 29.954  8.355   -9.785  1 45.78 ? 165 LEU   B O   1 
ATOM   4215 C  CB  . LEU   B 1 180 ? 32.672  9.717   -10.706 1 44.77 ? 165 LEU   B CB  1 
ATOM   4216 C  CG  . LEU   B 1 180 ? 34.162  9.429   -10.49  1 46.5  ? 165 LEU   B CG  1 
ATOM   4217 C  CD1 . LEU   B 1 180 ? 34.782  10.545  -9.674  1 47.25 ? 165 LEU   B CD1 1 
ATOM   4218 C  CD2 . LEU   B 1 180 ? 34.404  8.076   -9.786  1 46.69 ? 165 LEU   B CD2 1 
ATOM   4219 N  N   . VAL   B 1 181 ? 29.583  9.621   -11.62  1 43.58 ? 166 VAL   B N   1 
ATOM   4220 C  CA  . VAL   B 1 181 ? 28.193  9.869   -11.277 1 43.08 ? 166 VAL   B CA  1 
ATOM   4221 C  C   . VAL   B 1 181 ? 27.365  8.573   -11.415 1 42.66 ? 166 VAL   B C   1 
ATOM   4222 O  O   . VAL   B 1 181 ? 26.536  8.307   -10.551 1 42.7  ? 166 VAL   B O   1 
ATOM   4223 C  CB  . VAL   B 1 181 ? 27.603  11.077  -12.019 1 43.58 ? 166 VAL   B CB  1 
ATOM   4224 C  CG1 . VAL   B 1 181 ? 26.107  11.191  -11.774 1 44.04 ? 166 VAL   B CG1 1 
ATOM   4225 C  CG2 . VAL   B 1 181 ? 28.311  12.361  -11.588 1 44.02 ? 166 VAL   B CG2 1 
ATOM   4226 N  N   . SER   B 1 182 ? 27.674  7.703   -12.409 1 41.7  ? 167 SER   B N   1 
ATOM   4227 C  CA  . SER   B 1 182 ? 27.001  6.409   -12.547 1 41.14 ? 167 SER   B CA  1 
ATOM   4228 C  C   . SER   B 1 182 ? 27.293  5.565   -11.301 1 41.23 ? 167 SER   B C   1 
ATOM   4229 O  O   . SER   B 1 182 ? 26.375  4.994   -10.706 1 40.98 ? 167 SER   B O   1 
ATOM   4230 C  CB  . SER   B 1 182 ? 27.481  5.668   -13.797 1 41.72 ? 167 SER   B CB  1 
ATOM   4231 O  OG  . SER   B 1 182 ? 27.184  6.356   -15     1 42.74 ? 167 SER   B OG  1 
ATOM   4232 N  N   . LEU   B 1 183 ? 28.573  5.543   -10.88  1 40.71 ? 168 LEU   B N   1 
ATOM   4233 C  CA  . LEU   B 1 183 ? 29.024  4.836   -9.702  1 40.85 ? 168 LEU   B CA  1 
ATOM   4234 C  C   . LEU   B 1 183 ? 28.327  5.354   -8.44   1 42.03 ? 168 LEU   B C   1 
ATOM   4235 O  O   . LEU   B 1 183 ? 27.879  4.553   -7.627  1 42.67 ? 168 LEU   B O   1 
ATOM   4236 C  CB  . LEU   B 1 183 ? 30.537  4.991   -9.575  1 40.6  ? 168 LEU   B CB  1 
ATOM   4237 C  CG  . LEU   B 1 183 ? 31.155  4.367   -8.352  1 40.99 ? 168 LEU   B CG  1 
ATOM   4238 C  CD1 . LEU   B 1 183 ? 31.021  2.86    -8.397  1 41.59 ? 168 LEU   B CD1 1 
ATOM   4239 C  CD2 . LEU   B 1 183 ? 32.582  4.778   -8.227  1 40.84 ? 168 LEU   B CD2 1 
ATOM   4240 N  N   . LEU   B 1 184 ? 28.186  6.667   -8.299  1 42.38 ? 169 LEU   B N   1 
ATOM   4241 C  CA  . LEU   B 1 184 ? 27.524  7.254   -7.143  1 43.36 ? 169 LEU   B CA  1 
ATOM   4242 C  C   . LEU   B 1 184 ? 26.039  6.89    -7.098  1 44    ? 169 LEU   B C   1 
ATOM   4243 O  O   . LEU   B 1 184 ? 25.492  6.724   -6.015  1 44.75 ? 169 LEU   B O   1 
ATOM   4244 C  CB  . LEU   B 1 184 ? 27.745  8.771   -7.112  1 43.73 ? 169 LEU   B CB  1 
ATOM   4245 C  CG  . LEU   B 1 184 ? 29.173  9.205   -6.741  1 44.94 ? 169 LEU   B CG  1 
ATOM   4246 C  CD1 . LEU   B 1 184 ? 29.416  10.675  -7.073  1 45    ? 169 LEU   B CD1 1 
ATOM   4247 C  CD2 . LEU   B 1 184 ? 29.449  8.941   -5.281  1 45.25 ? 169 LEU   B CD2 1 
ATOM   4248 N  N   . VAL   B 1 185 ? 25.39   6.743   -8.256  1 43.46 ? 170 VAL   B N   1 
ATOM   4249 C  CA  . VAL   B 1 185 ? 23.994  6.339   -8.317  1 43.29 ? 170 VAL   B CA  1 
ATOM   4250 C  C   . VAL   B 1 185 ? 23.899  4.844   -7.947  1 44.15 ? 170 VAL   B C   1 
ATOM   4251 O  O   . VAL   B 1 185 ? 23.024  4.477   -7.179  1 44.63 ? 170 VAL   B O   1 
ATOM   4252 C  CB  . VAL   B 1 185 ? 23.379  6.654   -9.696  1 43.31 ? 170 VAL   B CB  1 
ATOM   4253 C  CG1 . VAL   B 1 185 ? 22.042  5.933   -9.881  1 43.27 ? 170 VAL   B CG1 1 
ATOM   4254 C  CG2 . VAL   B 1 185 ? 23.232  8.168   -9.901  1 43.29 ? 170 VAL   B CG2 1 
ATOM   4255 N  N   . GLU   B 1 186 ? 24.832  3.996   -8.448  1 44.08 ? 171 GLU   B N   1 
ATOM   4256 C  CA  . GLU   B 1 186 ? 24.951  2.572   -8.106  1 44.57 ? 171 GLU   B CA  1 
ATOM   4257 C  C   . GLU   B 1 186 ? 25.057  2.408   -6.588  1 46.2  ? 171 GLU   B C   1 
ATOM   4258 O  O   . GLU   B 1 186 ? 24.436  1.512   -6.017  1 46.95 ? 171 GLU   B O   1 
ATOM   4259 C  CB  . GLU   B 1 186 ? 26.263  1.982   -8.662  1 44.78 ? 171 GLU   B CB  1 
ATOM   4260 C  CG  . GLU   B 1 186 ? 26.197  1.397   -10.037 1 45.51 ? 171 GLU   B CG  1 
ATOM   4261 C  CD  . GLU   B 1 186 ? 25.516  0.052   -10.174 1 44.57 ? 171 GLU   B CD  1 
ATOM   4262 O  OE1 . GLU   B 1 186 ? 24.919  -0.162  -11.247 1 45.55 ? 171 GLU   B OE1 1 
ATOM   4263 O  OE2 . GLU   B 1 186 ? 25.594  -0.793  -9.256  1 41.78 ? 171 GLU   B OE2 1 
ATOM   4264 N  N   . ILE   B 1 187 ? 25.916  3.218   -5.955  1 46.51 ? 172 ILE   B N   1 
ATOM   4265 C  CA  . ILE   B 1 187 ? 26.157  3.166   -4.524  1 47.6  ? 172 ILE   B CA  1 
ATOM   4266 C  C   . ILE   B 1 187 ? 24.91   3.608   -3.752  1 48.18 ? 172 ILE   B C   1 
ATOM   4267 O  O   . ILE   B 1 187 ? 24.53   2.932   -2.796  1 48.91 ? 172 ILE   B O   1 
ATOM   4268 C  CB  . ILE   B 1 187 ? 27.448  3.963   -4.167  1 48.21 ? 172 ILE   B CB  1 
ATOM   4269 C  CG1 . ILE   B 1 187 ? 28.705  3.226   -4.679  1 49.54 ? 172 ILE   B CG1 1 
ATOM   4270 C  CG2 . ILE   B 1 187 ? 27.552  4.237   -2.68   1 48.27 ? 172 ILE   B CG2 1 
ATOM   4271 C  CD1 . ILE   B 1 187 ? 30.036  4.031   -4.541  1 51.03 ? 172 ILE   B CD1 1 
ATOM   4272 N  N   . ALA   B 1 188 ? 24.239  4.693   -4.195  1 47.54 ? 173 ALA   B N   1 
ATOM   4273 C  CA  . ALA   B 1 188 ? 23.008  5.174   -3.563  1 47.87 ? 173 ALA   B CA  1 
ATOM   4274 C  C   . ALA   B 1 188 ? 21.897  4.111   -3.641  1 48.98 ? 173 ALA   B C   1 
ATOM   4275 O  O   . ALA   B 1 188 ? 21.185  3.879   -2.661  1 49.43 ? 173 ALA   B O   1 
ATOM   4276 C  CB  . ALA   B 1 188 ? 22.534  6.463   -4.223  1 47.55 ? 173 ALA   B CB  1 
ATOM   4277 N  N   . ALA   B 1 189 ? 21.765  3.454   -4.797  1 49    ? 174 ALA   B N   1 
ATOM   4278 C  CA  . ALA   B 1 189 ? 20.764  2.409   -4.988  1 49.7  ? 174 ALA   B CA  1 
ATOM   4279 C  C   . ALA   B 1 189 ? 21.067  1.144   -4.184  1 50.69 ? 174 ALA   B C   1 
ATOM   4280 O  O   . ALA   B 1 189 ? 20.146  0.392   -3.869  1 50.7  ? 174 ALA   B O   1 
ATOM   4281 C  CB  . ALA   B 1 189 ? 20.633  2.071   -6.463  1 49.6  ? 174 ALA   B CB  1 
ATOM   4282 N  N   . ALA   B 1 190 ? 22.343  0.93    -3.823  1 51.61 ? 175 ALA   B N   1 
ATOM   4283 C  CA  . ALA   B 1 190 ? 22.827  -0.225  -3.065  1 52.95 ? 175 ALA   B CA  1 
ATOM   4284 C  C   . ALA   B 1 190 ? 22.316  -0.279  -1.636  1 53.52 ? 175 ALA   B C   1 
ATOM   4285 O  O   . ALA   B 1 190 ? 22.226  -1.37   -1.075  1 53.79 ? 175 ALA   B O   1 
ATOM   4286 C  CB  . ALA   B 1 190 ? 24.342  -0.26   -3.068  1 53.46 ? 175 ALA   B CB  1 
ATOM   4287 N  N   . SER   B 1 191 ? 21.982  0.878   -1.043  1 53.43 ? 176 SER   B N   1 
ATOM   4288 C  CA  . SER   B 1 191 ? 21.426  0.887   0.3     1 54.33 ? 176 SER   B CA  1 
ATOM   4289 C  C   . SER   B 1 191 ? 20.022  0.231   0.342   1 55.07 ? 176 SER   B C   1 
ATOM   4290 O  O   . SER   B 1 191 ? 19.582  -0.187  1.411   1 55.69 ? 176 SER   B O   1 
ATOM   4291 C  CB  . SER   B 1 191 ? 21.397  2.3     0.865   1 56.3  ? 176 SER   B CB  1 
ATOM   4292 O  OG  . SER   B 1 191 ? 20.606  3.161   0.065   1 59.6  ? 176 SER   B OG  1 
ATOM   4293 N  N   . ALA   B 1 192 ? 19.339  0.095   -0.813  1 54.7  ? 177 ALA   B N   1 
ATOM   4294 C  CA  . ALA   B 1 192 ? 18.047  -0.578  -0.864  1 54.82 ? 177 ALA   B CA  1 
ATOM   4295 C  C   . ALA   B 1 192 ? 18.197  -2.112  -1.029  1 55.02 ? 177 ALA   B C   1 
ATOM   4296 O  O   . ALA   B 1 192 ? 17.251  -2.834  -0.733  1 55.2  ? 177 ALA   B O   1 
ATOM   4297 C  CB  . ALA   B 1 192 ? 17.188  0.01    -1.97   1 54.58 ? 177 ALA   B CB  1 
ATOM   4298 N  N   . ILE   B 1 193 ? 19.382  -2.608  -1.449  1 54.9  ? 178 ILE   B N   1 
ATOM   4299 C  CA  . ILE   B 1 193 ? 19.659  -4.038  -1.647  1 55.53 ? 178 ILE   B CA  1 
ATOM   4300 C  C   . ILE   B 1 193 ? 19.646  -4.792  -0.327  1 55.93 ? 178 ILE   B C   1 
ATOM   4301 O  O   . ILE   B 1 193 ? 19.178  -5.932  -0.275  1 56.5  ? 178 ILE   B O   1 
ATOM   4302 C  CB  . ILE   B 1 193 ? 21.005  -4.261  -2.388  1 56.36 ? 178 ILE   B CB  1 
ATOM   4303 C  CG1 . ILE   B 1 193 ? 20.99   -3.651  -3.793  1 57.54 ? 178 ILE   B CG1 1 
ATOM   4304 C  CG2 . ILE   B 1 193 ? 21.404  -5.747  -2.434  1 56.66 ? 178 ILE   B CG2 1 
ATOM   4305 C  CD1 . ILE   B 1 193 ? 22.369  -3.627  -4.419  1 59.08 ? 178 ILE   B CD1 1 
ATOM   4306 N  N   . LYS   B 1 194 ? 20.141  -4.164  0.745   1 55.18 ? 179 LYS   B N   1 
ATOM   4307 C  CA  . LYS   B 1 194 ? 20.13   -4.797  2.067   1 54.91 ? 179 LYS   B CA  1 
ATOM   4308 C  C   . LYS   B 1 194 ? 18.701  -5.065  2.589   1 54.14 ? 179 LYS   B C   1 
ATOM   4309 O  O   . LYS   B 1 194 ? 18.51   -5.926  3.451   1 54.23 ? 179 LYS   B O   1 
ATOM   4310 C  CB  . LYS   B 1 194 ? 20.931  -3.963  3.079   1 57.08 ? 179 LYS   B CB  1 
ATOM   4311 C  CG  . LYS   B 1 194 ? 20.261  -2.658  3.491   1 61.6  ? 179 LYS   B CG  1 
ATOM   4312 C  CD  . LYS   B 1 194 ? 21.065  -1.903  4.54    1 66.47 ? 179 LYS   B CD  1 
ATOM   4313 C  CE  . LYS   B 1 194 ? 22.072  -0.961  3.924   1 71.16 ? 179 LYS   B CE  1 
ATOM   4314 N  NZ  . LYS   B 1 194 ? 21.691  0.461   4.136   1 74.07 ? 179 LYS   B NZ  1 
ATOM   4315 N  N   . VAL   B 1 195 ? 17.703  -4.341  2.056   1 53.17 ? 180 VAL   B N   1 
ATOM   4316 C  CA  . VAL   B 1 195 ? 16.302  -4.499  2.433   1 52.62 ? 180 VAL   B CA  1 
ATOM   4317 C  C   . VAL   B 1 195 ? 15.66   -5.712  1.712   1 51.84 ? 180 VAL   B C   1 
ATOM   4318 O  O   . VAL   B 1 195 ? 14.652  -6.226  2.182   1 51.99 ? 180 VAL   B O   1 
ATOM   4319 C  CB  . VAL   B 1 195 ? 15.513  -3.179  2.186   1 53.33 ? 180 VAL   B CB  1 
ATOM   4320 C  CG1 . VAL   B 1 195 ? 14.087  -3.274  2.706   1 53.87 ? 180 VAL   B CG1 1 
ATOM   4321 C  CG2 . VAL   B 1 195 ? 16.224  -1.981  2.801   1 53.58 ? 180 VAL   B CG2 1 
ATOM   4322 N  N   . ILE   B 1 196 ? 16.246  -6.185  0.59    1 50.99 ? 181 ILE   B N   1 
ATOM   4323 C  CA  . ILE   B 1 196 ? 15.708  -7.311  -0.181  1 50.74 ? 181 ILE   B CA  1 
ATOM   4324 C  C   . ILE   B 1 196 ? 15.42   -8.554  0.701   1 50.25 ? 181 ILE   B C   1 
ATOM   4325 O  O   . ILE   B 1 196 ? 14.295  -9.051  0.654   1 49.97 ? 181 ILE   B O   1 
ATOM   4326 C  CB  . ILE   B 1 196 ? 16.584  -7.637  -1.43   1 51.09 ? 181 ILE   B CB  1 
ATOM   4327 C  CG1 . ILE   B 1 196 ? 16.414  -6.547  -2.52   1 51.73 ? 181 ILE   B CG1 1 
ATOM   4328 C  CG2 . ILE   B 1 196 ? 16.302  -9.041  -1.988  1 51.04 ? 181 ILE   B CG2 1 
ATOM   4329 C  CD1 . ILE   B 1 196 ? 17.306  -6.746  -3.765  1 52.65 ? 181 ILE   B CD1 1 
ATOM   4330 N  N   . PRO   B 1 197 ? 16.361  -9.044  1.537   1 49.95 ? 182 PRO   B N   1 
ATOM   4331 C  CA  . PRO   B 1 197 ? 16.042  -10.216 2.371   1 49.53 ? 182 PRO   B CA  1 
ATOM   4332 C  C   . PRO   B 1 197 ? 14.934  -9.952  3.402   1 49.02 ? 182 PRO   B C   1 
ATOM   4333 O  O   . PRO   B 1 197 ? 14.205  -10.874 3.76    1 49.04 ? 182 PRO   B O   1 
ATOM   4334 C  CB  . PRO   B 1 197 ? 17.391  -10.585 2.991   1 50.33 ? 182 PRO   B CB  1 
ATOM   4335 C  CG  . PRO   B 1 197 ? 18.196  -9.342  2.952   1 50.75 ? 182 PRO   B CG  1 
ATOM   4336 C  CD  . PRO   B 1 197 ? 17.765  -8.613  1.727   1 49.36 ? 182 PRO   B CD  1 
ATOM   4337 N  N   . THR   B 1 198 ? 14.773  -8.687  3.843   1 48.41 ? 183 THR   B N   1 
ATOM   4338 C  CA  . THR   B 1 198 ? 13.693  -8.297  4.764   1 48.42 ? 183 THR   B CA  1 
ATOM   4339 C  C   . THR   B 1 198 ? 12.335  -8.462  4.051   1 48.69 ? 183 THR   B C   1 
ATOM   4340 O  O   . THR   B 1 198 ? 11.378  -8.934  4.66    1 49.36 ? 183 THR   B O   1 
ATOM   4341 C  CB  . THR   B 1 198 ? 13.881  -6.837  5.218   1 48.7  ? 183 THR   B CB  1 
ATOM   4342 O  OG1 . THR   B 1 198 ? 15.201  -6.676  5.716   1 49.51 ? 183 THR   B OG1 1 
ATOM   4343 C  CG2 . THR   B 1 198 ? 12.876  -6.404  6.257   1 48.62 ? 183 THR   B CG2 1 
ATOM   4344 N  N   . VAL   B 1 199 ? 12.266  -8.099  2.757   1 48.12 ? 184 VAL   B N   1 
ATOM   4345 C  CA  . VAL   B 1 199 ? 11.057  -8.211  1.942   1 48.59 ? 184 VAL   B CA  1 
ATOM   4346 C  C   . VAL   B 1 199 ? 10.606  -9.67   1.777   1 49.76 ? 184 VAL   B C   1 
ATOM   4347 O  O   . VAL   B 1 199 ? 9.438   -9.988  2.033   1 50.46 ? 184 VAL   B O   1 
ATOM   4348 C  CB  . VAL   B 1 199 ? 11.22   -7.483  0.58    1 48.32 ? 184 VAL   B CB  1 
ATOM   4349 C  CG1 . VAL   B 1 199 ? 10.048  -7.769  -0.355  1 48.44 ? 184 VAL   B CG1 1 
ATOM   4350 C  CG2 . VAL   B 1 199 ? 11.393  -5.982  0.781   1 48.29 ? 184 VAL   B CG2 1 
ATOM   4351 N  N   . PHE   B 1 200 ? 11.519  -10.55  1.385   1 49.78 ? 185 PHE   B N   1 
ATOM   4352 C  CA  . PHE   B 1 200 ? 11.19   -11.951 1.202   1 51.12 ? 185 PHE   B CA  1 
ATOM   4353 C  C   . PHE   B 1 200 ? 10.898  -12.681 2.51    1 51.89 ? 185 PHE   B C   1 
ATOM   4354 O  O   . PHE   B 1 200 ? 10.07   -13.599 2.509   1 52.76 ? 185 PHE   B O   1 
ATOM   4355 C  CB  . PHE   B 1 200 ? 12.267  -12.656 0.393   1 51.76 ? 185 PHE   B CB  1 
ATOM   4356 C  CG  . PHE   B 1 200 ? 12.281  -12.199 -1.041  1 52.75 ? 185 PHE   B CG  1 
ATOM   4357 C  CD1 . PHE   B 1 200 ? 11.181  -12.399 -1.86   1 53.43 ? 185 PHE   B CD1 1 
ATOM   4358 C  CD2 . PHE   B 1 200 ? 13.401  -11.583 -1.576  1 53.69 ? 185 PHE   B CD2 1 
ATOM   4359 C  CE1 . PHE   B 1 200 ? 11.198  -11.979 -3.185  1 54.38 ? 185 PHE   B CE1 1 
ATOM   4360 C  CE2 . PHE   B 1 200 ? 13.424  -11.187 -2.91   1 54.45 ? 185 PHE   B CE2 1 
ATOM   4361 C  CZ  . PHE   B 1 200 ? 12.327  -11.394 -3.708  1 54.17 ? 185 PHE   B CZ  1 
ATOM   4362 N  N   . LYS   B 1 201 ? 11.554  -12.287 3.62    1 51.28 ? 186 LYS   B N   1 
ATOM   4363 C  CA  . LYS   B 1 201 ? 11.277  -12.914 4.909   1 51.4  ? 186 LYS   B CA  1 
ATOM   4364 C  C   . LYS   B 1 201 ? 9.894   -12.481 5.381   1 51.51 ? 186 LYS   B C   1 
ATOM   4365 O  O   . LYS   B 1 201 ? 9.127   -13.32  5.839   1 51.74 ? 186 LYS   B O   1 
ATOM   4366 C  CB  . LYS   B 1 201 ? 12.348  -12.583 5.965   1 52.81 ? 186 LYS   B CB  1 
ATOM   4367 N  N   . ALA   B 1 202 ? 9.553   -11.18  5.224   1 51.38 ? 187 ALA   B N   1 
ATOM   4368 C  CA  . ALA   B 1 202 ? 8.24    -10.645 5.605   1 51.18 ? 187 ALA   B CA  1 
ATOM   4369 C  C   . ALA   B 1 202 ? 7.124   -11.333 4.829   1 51.22 ? 187 ALA   B C   1 
ATOM   4370 O  O   . ALA   B 1 202 ? 6.101   -11.632 5.411   1 51.12 ? 187 ALA   B O   1 
ATOM   4371 C  CB  . ALA   B 1 202 ? 8.184   -9.149  5.374   1 51.05 ? 187 ALA   B CB  1 
ATOM   4372 N  N   . MET   B 1 203 ? 7.323   -11.614 3.536   1 51.24 ? 188 MET   B N   1 
ATOM   4373 C  CA  . MET   B 1 203 ? 6.313   -12.307 2.743   1 51.91 ? 188 MET   B CA  1 
ATOM   4374 C  C   . MET   B 1 203 ? 6.098   -13.753 3.239   1 53.89 ? 188 MET   B C   1 
ATOM   4375 O  O   . MET   B 1 203 ? 4.952   -14.165 3.414   1 54.26 ? 188 MET   B O   1 
ATOM   4376 C  CB  . MET   B 1 203 ? 6.701   -12.327 1.274   1 51.75 ? 188 MET   B CB  1 
ATOM   4377 C  CG  . MET   B 1 203 ? 6.595   -10.996 0.584   1 53.62 ? 188 MET   B CG  1 
ATOM   4378 S  SD  . MET   B 1 203 ? 7.47    -11.019 -1.005  1 58.53 ? 188 MET   B SD  1 
ATOM   4379 C  CE  . MET   B 1 203 ? 6.554   -12.235 -1.852  1 55.58 ? 188 MET   B CE  1 
ATOM   4380 N  N   . GLN   B 1 204 ? 7.192   -14.509 3.477   1 54.82 ? 189 GLN   B N   1 
ATOM   4381 C  CA  . GLN   B 1 204 ? 7.163   -15.899 3.942   1 56.18 ? 189 GLN   B CA  1 
ATOM   4382 C  C   . GLN   B 1 204 ? 6.506   -16.004 5.322   1 57.69 ? 189 GLN   B C   1 
ATOM   4383 O  O   . GLN   B 1 204 ? 5.593   -16.807 5.504   1 58.28 ? 189 GLN   B O   1 
ATOM   4384 C  CB  . GLN   B 1 204 ? 8.593   -16.487 3.98    1 57.48 ? 189 GLN   B CB  1 
ATOM   4385 N  N   . MET   B 1 205 ? 6.951   -15.172 6.283   1 58.01 ? 190 MET   B N   1 
ATOM   4386 C  CA  . MET   B 1 205 ? 6.398   -15.142 7.636   1 58.51 ? 190 MET   B CA  1 
ATOM   4387 C  C   . MET   B 1 205 ? 5.065   -14.381 7.738   1 57.98 ? 190 MET   B C   1 
ATOM   4388 O  O   . MET   B 1 205 ? 4.546   -14.231 8.846   1 58.58 ? 190 MET   B O   1 
ATOM   4389 C  CB  . MET   B 1 205 ? 7.401   -14.518 8.621   1 60.28 ? 190 MET   B CB  1 
ATOM   4390 C  CG  . MET   B 1 205 ? 8.771   -15.182 8.651   1 65.57 ? 190 MET   B CG  1 
ATOM   4391 S  SD  . MET   B 1 205 ? 8.83    -16.996 8.665   1 80.24 ? 190 MET   B SD  1 
ATOM   4392 C  CE  . MET   B 1 205 ? 10.343  -17.291 7.638   1 79.35 ? 190 MET   B CE  1 
ATOM   4393 N  N   . GLN   B 1 206 ? 4.535   -13.861 6.61    1 56.3  ? 191 GLN   B N   1 
ATOM   4394 C  CA  . GLN   B 1 206 ? 3.295   -13.106 6.566   1 55.58 ? 191 GLN   B CA  1 
ATOM   4395 C  C   . GLN   B 1 206 ? 3.311   -11.941 7.553   1 55.24 ? 191 GLN   B C   1 
ATOM   4396 O  O   . GLN   B 1 206 ? 2.384   -11.787 8.335   1 56.48 ? 191 GLN   B O   1 
ATOM   4397 C  CB  . GLN   B 1 206 ? 2.079   -14.021 6.772   1 56.74 ? 191 GLN   B CB  1 
ATOM   4398 C  CG  . GLN   B 1 206 ? 1.848   -15.019 5.645   1 59.84 ? 191 GLN   B CG  1 
ATOM   4399 C  CD  . GLN   B 1 206 ? 1.106   -14.4   4.489   1 65.35 ? 191 GLN   B CD  1 
ATOM   4400 O  OE1 . GLN   B 1 206 ? 0.305   -13.466 4.657   1 67.69 ? 191 GLN   B OE1 1 
ATOM   4401 N  NE2 . GLN   B 1 206 ? 1.347   -14.912 3.285   1 65.53 ? 191 GLN   B NE2 1 
ATOM   4402 N  N   . GLU   B 1 207 ? 4.39    -11.16  7.556   1 53.26 ? 192 GLU   B N   1 
ATOM   4403 C  CA  . GLU   B 1 207 ? 4.563   -10.012 8.422   1 52.23 ? 192 GLU   B CA  1 
ATOM   4404 C  C   . GLU   B 1 207 ? 4.259   -8.765  7.618   1 51.62 ? 192 GLU   B C   1 
ATOM   4405 O  O   . GLU   B 1 207 ? 5.168   -8.129  7.086   1 51.87 ? 192 GLU   B O   1 
ATOM   4406 C  CB  . GLU   B 1 207 ? 5.998   -9.969  8.964   1 54.08 ? 192 GLU   B CB  1 
ATOM   4407 C  CG  . GLU   B 1 207 ? 6.341   -11.153 9.848   1 58.41 ? 192 GLU   B CG  1 
ATOM   4408 C  CD  . GLU   B 1 207 ? 5.712   -11.119 11.233  1 65.64 ? 192 GLU   B CD  1 
ATOM   4409 O  OE1 . GLU   B 1 207 ? 5.46    -10.002 11.749  1 65.12 ? 192 GLU   B OE1 1 
ATOM   4410 O  OE2 . GLU   B 1 207 ? 5.48    -12.211 11.807  1 68.3  ? 192 GLU   B OE2 1 
ATOM   4411 N  N   . ARG   B 1 208 ? 2.968   -8.439  7.507   1 50.26 ? 193 ARG   B N   1 
ATOM   4412 C  CA  . ARG   B 1 208 ? 2.454   -7.309  6.755   1 49.07 ? 193 ARG   B CA  1 
ATOM   4413 C  C   . ARG   B 1 208 ? 3.114   -5.981  7.104   1 49.4  ? 193 ARG   B C   1 
ATOM   4414 O  O   . ARG   B 1 208 ? 3.485   -5.24   6.197   1 49.92 ? 193 ARG   B O   1 
ATOM   4415 C  CB  . ARG   B 1 208 ? 0.927   -7.217  6.932   1 48.48 ? 193 ARG   B CB  1 
ATOM   4416 C  CG  . ARG   B 1 208 ? 0.265   -6.087  6.165   1 47.96 ? 193 ARG   B CG  1 
ATOM   4417 C  CD  . ARG   B 1 208 ? 0.03    -4.875  7.027   1 48.2  ? 193 ARG   B CD  1 
ATOM   4418 N  NE  . ARG   B 1 208 ? -0.695  -3.829  6.315   1 48.74 ? 193 ARG   B NE  1 
ATOM   4419 C  CZ  . ARG   B 1 208 ? -0.769  -2.563  6.711   1 50.09 ? 193 ARG   B CZ  1 
ATOM   4420 N  NH1 . ARG   B 1 208 ? -0.123  -2.161  7.797   1 50.68 ? 193 ARG   B NH1 1 
ATOM   4421 N  NH2 . ARG   B 1 208 ? -1.472  -1.682  6.01    1 49.32 ? 193 ARG   B NH2 1 
ATOM   4422 N  N   . ASP   B 1 209 ? 3.209   -5.643  8.401   1 48.84 ? 194 ASP   B N   1 
ATOM   4423 C  CA  . ASP   B 1 209 ? 3.765   -4.356  8.801   1 48.43 ? 194 ASP   B CA  1 
ATOM   4424 C  C   . ASP   B 1 209 ? 5.249   -4.265  8.453   1 47.97 ? 194 ASP   B C   1 
ATOM   4425 O  O   . ASP   B 1 209 ? 5.705   -3.204  8.031   1 48.39 ? 194 ASP   B O   1 
ATOM   4426 C  CB  . ASP   B 1 209 ? 3.526   -4.106  10.291  1 49.7  ? 194 ASP   B CB  1 
ATOM   4427 C  CG  . ASP   B 1 209 ? 2.06    -4.036  10.68   1 53.79 ? 194 ASP   B CG  1 
ATOM   4428 O  OD1 . ASP   B 1 209 ? 1.254   -3.489  9.885   1 54.08 ? 194 ASP   B OD1 1 
ATOM   4429 O  OD2 . ASP   B 1 209 ? 1.722   -4.507  11.778  1 55.75 ? 194 ASP   B OD2 1 
ATOM   4430 N  N   . THR   B 1 210 ? 5.989   -5.38   8.608   1 46.98 ? 195 THR   B N   1 
ATOM   4431 C  CA  . THR   B 1 210 ? 7.409   -5.456  8.265   1 46.74 ? 195 THR   B CA  1 
ATOM   4432 C  C   . THR   B 1 210 ? 7.586   -5.205  6.758   1 45.96 ? 195 THR   B C   1 
ATOM   4433 O  O   . THR   B 1 210 ? 8.41    -4.389  6.377   1 45.92 ? 195 THR   B O   1 
ATOM   4434 C  CB  . THR   B 1 210 ? 7.998   -6.808  8.712   1 47.78 ? 195 THR   B CB  1 
ATOM   4435 O  OG1 . THR   B 1 210 ? 7.897   -6.899  10.129  1 49.1  ? 195 THR   B OG1 1 
ATOM   4436 C  CG2 . THR   B 1 210 ? 9.464   -6.981  8.304   1 47.47 ? 195 THR   B CG2 1 
ATOM   4437 N  N   . LEU   B 1 211 ? 6.762   -5.854  5.924   1 45.65 ? 196 LEU   B N   1 
ATOM   4438 C  CA  . LEU   B 1 211 ? 6.783   -5.714  4.467   1 45.93 ? 196 LEU   B CA  1 
ATOM   4439 C  C   . LEU   B 1 211 ? 6.509   -4.289  4.035   1 46.44 ? 196 LEU   B C   1 
ATOM   4440 O  O   . LEU   B 1 211 ? 7.204   -3.772  3.165   1 47.38 ? 196 LEU   B O   1 
ATOM   4441 C  CB  . LEU   B 1 211 ? 5.762   -6.654  3.817   1 45.65 ? 196 LEU   B CB  1 
ATOM   4442 C  CG  . LEU   B 1 211 ? 5.708   -6.65   2.29    1 46.19 ? 196 LEU   B CG  1 
ATOM   4443 C  CD1 . LEU   B 1 211 ? 7.055   -7.013  1.682   1 46.37 ? 196 LEU   B CD1 1 
ATOM   4444 C  CD2 . LEU   B 1 211 ? 4.655   -7.611  1.791   1 45.99 ? 196 LEU   B CD2 1 
ATOM   4445 N  N   . LEU   B 1 212 ? 5.541   -3.638  4.657   1 46.09 ? 197 LEU   B N   1 
ATOM   4446 C  CA  . LEU   B 1 212 ? 5.197   -2.257  4.327   1 46.61 ? 197 LEU   B CA  1 
ATOM   4447 C  C   . LEU   B 1 212 ? 6.361   -1.318  4.645   1 46.89 ? 197 LEU   B C   1 
ATOM   4448 O  O   . LEU   B 1 212 ? 6.689   -0.456  3.833   1 47.8  ? 197 LEU   B O   1 
ATOM   4449 C  CB  . LEU   B 1 212 ? 3.929   -1.851  5.088   1 47.03 ? 197 LEU   B CB  1 
ATOM   4450 C  CG  . LEU   B 1 212 ? 3.162   -0.672  4.536   1 48.89 ? 197 LEU   B CG  1 
ATOM   4451 C  CD1 . LEU   B 1 212 ? 1.717   -0.733  4.964   1 49.32 ? 197 LEU   B CD1 1 
ATOM   4452 C  CD2 . LEU   B 1 212 ? 3.719   0.609   5.06    1 49.68 ? 197 LEU   B CD2 1 
ATOM   4453 N  N   . LYS   B 1 213 ? 6.994   -1.49   5.812   1 46.34 ? 198 LYS   B N   1 
ATOM   4454 C  CA  . LYS   B 1 213 ? 8.129   -0.661  6.212   1 46.17 ? 198 LYS   B CA  1 
ATOM   4455 C  C   . LYS   B 1 213 ? 9.305   -0.876  5.251   1 45.11 ? 198 LYS   B C   1 
ATOM   4456 O  O   . LYS   B 1 213 ? 9.955   0.078   4.853   1 45.38 ? 198 LYS   B O   1 
ATOM   4457 C  CB  . LYS   B 1 213 ? 8.548   -0.982  7.663   1 48.07 ? 198 LYS   B CB  1 
ATOM   4458 N  N   . ALA   B 1 214 ? 9.556   -2.132  4.875   1 44.16 ? 199 ALA   B N   1 
ATOM   4459 C  CA  . ALA   B 1 214 ? 10.61   -2.513  3.944   1 43.74 ? 199 ALA   B CA  1 
ATOM   4460 C  C   . ALA   B 1 214 ? 10.402  -1.882  2.561   1 43.42 ? 199 ALA   B C   1 
ATOM   4461 O  O   . ALA   B 1 214 ? 11.332  -1.281  2.029   1 43.38 ? 199 ALA   B O   1 
ATOM   4462 C  CB  . ALA   B 1 214 ? 10.693  -4.029  3.841   1 43.53 ? 199 ALA   B CB  1 
ATOM   4463 N  N   . LEU   B 1 215 ? 9.178   -1.949  2.018   1 43.26 ? 200 LEU   B N   1 
ATOM   4464 C  CA  . LEU   B 1 215 ? 8.864   -1.343  0.731   1 43.7  ? 200 LEU   B CA  1 
ATOM   4465 C  C   . LEU   B 1 215 ? 9.03    0.172   0.764   1 45.67 ? 200 LEU   B C   1 
ATOM   4466 O  O   . LEU   B 1 215 ? 9.546   0.745   -0.197  1 46.44 ? 200 LEU   B O   1 
ATOM   4467 C  CB  . LEU   B 1 215 ? 7.451   -1.708  0.279   1 42.81 ? 200 LEU   B CB  1 
ATOM   4468 C  CG  . LEU   B 1 215 ? 7.246   -3.166  -0.101  1 43.18 ? 200 LEU   B CG  1 
ATOM   4469 C  CD1 . LEU   B 1 215 ? 5.77    -3.451  -0.372  1 43.22 ? 200 LEU   B CD1 1 
ATOM   4470 C  CD2 . LEU   B 1 215 ? 8.094   -3.55   -1.287  1 43.06 ? 200 LEU   B CD2 1 
ATOM   4471 N  N   . LEU   B 1 216 ? 8.622   0.824   1.874   1 45.99 ? 201 LEU   B N   1 
ATOM   4472 C  CA  . LEU   B 1 216 ? 8.781   2.273   2.001   1 46.39 ? 201 LEU   B CA  1 
ATOM   4473 C  C   . LEU   B 1 216 ? 10.254  2.668   2.132   1 46.38 ? 201 LEU   B C   1 
ATOM   4474 O  O   . LEU   B 1 216 ? 10.617  3.762   1.721   1 46.76 ? 201 LEU   B O   1 
ATOM   4475 C  CB  . LEU   B 1 216 ? 7.98    2.822   3.186   1 46.56 ? 201 LEU   B CB  1 
ATOM   4476 C  CG  . LEU   B 1 216 ? 6.475   2.896   2.984   1 48.31 ? 201 LEU   B CG  1 
ATOM   4477 C  CD1 . LEU   B 1 216 ? 5.784   3.316   4.273   1 48.79 ? 201 LEU   B CD1 1 
ATOM   4478 C  CD2 . LEU   B 1 216 ? 6.117   3.847   1.843   1 48.77 ? 201 LEU   B CD2 1 
ATOM   4479 N  N   . GLU   B 1 217 ? 11.089  1.801   2.72    1 45.99 ? 202 GLU   B N   1 
ATOM   4480 C  CA  . GLU   B 1 217 ? 12.512  2.056   2.859   1 46.33 ? 202 GLU   B CA  1 
ATOM   4481 C  C   . GLU   B 1 217 ? 13.221  1.914   1.489   1 46.76 ? 202 GLU   B C   1 
ATOM   4482 O  O   . GLU   B 1 217 ? 14.127  2.686   1.185   1 47.63 ? 202 GLU   B O   1 
ATOM   4483 C  CB  . GLU   B 1 217 ? 13.117  1.119   3.897   1 49.03 ? 202 GLU   B CB  1 
ATOM   4484 C  CG  . GLU   B 1 217 ? 14.61   1.309   4.103   1 56.09 ? 202 GLU   B CG  1 
ATOM   4485 C  CD  . GLU   B 1 217 ? 15.059  2.708   4.5     1 64.05 ? 202 GLU   B CD  1 
ATOM   4486 O  OE1 . GLU   B 1 217 ? 14.266  3.454   5.125   1 66.5  ? 202 GLU   B OE1 1 
ATOM   4487 O  OE2 . GLU   B 1 217 ? 16.225  3.048   4.2     1 65.55 ? 202 GLU   B OE2 1 
ATOM   4488 N  N   . ILE   B 1 218 ? 12.775  0.977   0.645   1 46.03 ? 203 ILE   B N   1 
ATOM   4489 C  CA  . ILE   B 1 218 ? 13.327  0.81    -0.696  1 46.25 ? 203 ILE   B CA  1 
ATOM   4490 C  C   . ILE   B 1 218 ? 12.963  2.056   -1.519  1 47.16 ? 203 ILE   B C   1 
ATOM   4491 O  O   . ILE   B 1 218 ? 13.828  2.617   -2.187  1 47.68 ? 203 ILE   B O   1 
ATOM   4492 C  CB  . ILE   B 1 218 ? 12.814  -0.495  -1.353  1 46.11 ? 203 ILE   B CB  1 
ATOM   4493 C  CG1 . ILE   B 1 218 ? 13.456  -1.736  -0.706  1 46.39 ? 203 ILE   B CG1 1 
ATOM   4494 C  CG2 . ILE   B 1 218 ? 13.024  -0.485  -2.875  1 46.37 ? 203 ILE   B CG2 1 
ATOM   4495 C  CD1 . ILE   B 1 218 ? 12.83   -3.028  -1.169  1 47.34 ? 203 ILE   B CD1 1 
ATOM   4496 N  N   . ALA   B 1 219 ? 11.711  2.531   -1.41   1 47.22 ? 204 ALA   B N   1 
ATOM   4497 C  CA  . ALA   B 1 219 ? 11.269  3.731   -2.113  1 48.25 ? 204 ALA   B CA  1 
ATOM   4498 C  C   . ALA   B 1 219 ? 12.103  4.937   -1.682  1 49.9  ? 204 ALA   B C   1 
ATOM   4499 O  O   . ALA   B 1 219 ? 12.586  5.679   -2.531  1 50.8  ? 204 ALA   B O   1 
ATOM   4500 C  CB  . ALA   B 1 219 ? 9.787   3.987   -1.868  1 47.6  ? 204 ALA   B CB  1 
ATOM   4501 N  N   . SER   B 1 220 ? 12.356  5.066   -0.38   1 50.03 ? 205 SER   B N   1 
ATOM   4502 C  CA  . SER   B 1 220 ? 13.178  6.129   0.177   1 50.67 ? 205 SER   B CA  1 
ATOM   4503 C  C   . SER   B 1 220 ? 14.583  6.14    -0.437  1 50.53 ? 205 SER   B C   1 
ATOM   4504 O  O   . SER   B 1 220 ? 15.076  7.207   -0.795  1 50.9  ? 205 SER   B O   1 
ATOM   4505 C  CB  . SER   B 1 220 ? 13.257  5.984   1.694   1 52.5  ? 205 SER   B CB  1 
ATOM   4506 O  OG  . SER   B 1 220 ? 14.072  6.994   2.263   1 55.57 ? 205 SER   B OG  1 
ATOM   4507 N  N   . CYS   B 1 221 ? 15.211  4.959   -0.589  1 50.19 ? 206 CYS   B N   1 
ATOM   4508 C  CA  . CYS   B 1 221 ? 16.541  4.824   -1.191  1 50.76 ? 206 CYS   B CA  1 
ATOM   4509 C  C   . CYS   B 1 221 ? 16.561  5.218   -2.664  1 51.03 ? 206 CYS   B C   1 
ATOM   4510 O  O   . CYS   B 1 221 ? 17.499  5.888   -3.106  1 51.69 ? 206 CYS   B O   1 
ATOM   4511 C  CB  . CYS   B 1 221 ? 17.092  3.418   -1      1 51.95 ? 206 CYS   B CB  1 
ATOM   4512 S  SG  . CYS   B 1 221 ? 17.359  2.963   0.729   1 58.34 ? 206 CYS   B SG  1 
ATOM   4513 N  N   . LEU   B 1 222 ? 15.542  4.786   -3.427  1 50.24 ? 207 LEU   B N   1 
ATOM   4514 C  CA  . LEU   B 1 222 ? 15.448  5.114   -4.84   1 50.24 ? 207 LEU   B CA  1 
ATOM   4515 C  C   . LEU   B 1 222 ? 15.16   6.588   -5.067  1 51.59 ? 207 LEU   B C   1 
ATOM   4516 O  O   . LEU   B 1 222 ? 15.6    7.134   -6.073  1 51.98 ? 207 LEU   B O   1 
ATOM   4517 C  CB  . LEU   B 1 222 ? 14.406  4.242   -5.54   1 49.54 ? 207 LEU   B CB  1 
ATOM   4518 C  CG  . LEU   B 1 222 ? 14.686  2.753   -5.509  1 49.81 ? 207 LEU   B CG  1 
ATOM   4519 C  CD1 . LEU   B 1 222 ? 13.505  1.975   -6.037  1 49.86 ? 207 LEU   B CD1 1 
ATOM   4520 C  CD2 . LEU   B 1 222 ? 15.992  2.413   -6.238  1 49.97 ? 207 LEU   B CD2 1 
ATOM   4521 N  N   . GLU   B 1 223 ? 14.42   7.234   -4.152  1 52.24 ? 208 GLU   B N   1 
ATOM   4522 C  CA  . GLU   B 1 223 ? 14.127  8.67    -4.231  1 53.37 ? 208 GLU   B CA  1 
ATOM   4523 C  C   . GLU   B 1 223 ? 15.421  9.466   -3.992  1 54.65 ? 208 GLU   B C   1 
ATOM   4524 O  O   . GLU   B 1 223 ? 15.685  10.442  -4.696  1 55.06 ? 208 GLU   B O   1 
ATOM   4525 C  CB  . GLU   B 1 223 ? 13.067  9.066   -3.194  1 55.18 ? 208 GLU   B CB  1 
ATOM   4526 C  CG  . GLU   B 1 223 ? 11.654  8.613   -3.534  1 58.99 ? 208 GLU   B CG  1 
ATOM   4527 C  CD  . GLU   B 1 223 ? 10.69   8.524   -2.36   1 62.46 ? 208 GLU   B CD  1 
ATOM   4528 O  OE1 . GLU   B 1 223 ? 11.097  8.86    -1.221  1 62.51 ? 208 GLU   B OE1 1 
ATOM   4529 O  OE2 . GLU   B 1 223 ? 9.531   8.095   -2.579  1 61.88 ? 208 GLU   B OE2 1 
ATOM   4530 N  N   . LYS   B 1 224 ? 16.245  9.015   -3.029  1 55.12 ? 209 LYS   B N   1 
ATOM   4531 C  CA  . LYS   B 1 224 ? 17.531  9.627   -2.696  1 56.08 ? 209 LYS   B CA  1 
ATOM   4532 C  C   . LYS   B 1 224 ? 18.531  9.488   -3.87   1 56.94 ? 209 LYS   B C   1 
ATOM   4533 O  O   . LYS   B 1 224 ? 19.311  10.414  -4.14   1 57.57 ? 209 LYS   B O   1 
ATOM   4534 C  CB  . LYS   B 1 224 ? 18.109  8.996   -1.416  1 57.81 ? 209 LYS   B CB  1 
ATOM   4535 N  N   . ALA   B 1 225 ? 18.481  8.343   -4.581  1 56.13 ? 210 ALA   B N   1 
ATOM   4536 C  CA  . ALA   B 1 225 ? 19.331  8.081   -5.743  1 55.76 ? 210 ALA   B CA  1 
ATOM   4537 C  C   . ALA   B 1 225 ? 19.063  9.057   -6.909  1 55.22 ? 210 ALA   B C   1 
ATOM   4538 O  O   . ALA   B 1 225 ? 19.953  9.285   -7.73   1 55.39 ? 210 ALA   B O   1 
ATOM   4539 C  CB  . ALA   B 1 225 ? 19.162  6.644   -6.205  1 55.68 ? 210 ALA   B CB  1 
ATOM   4540 N  N   . LEU   B 1 226 ? 17.859  9.639   -6.97   1 54.6  ? 211 LEU   B N   1 
ATOM   4541 C  CA  . LEU   B 1 226 ? 17.514  10.624  -7.99   1 54.9  ? 211 LEU   B CA  1 
ATOM   4542 C  C   . LEU   B 1 226 ? 18.275  11.926  -7.742  1 55.89 ? 211 LEU   B C   1 
ATOM   4543 O  O   . LEU   B 1 226 ? 18.715  12.571  -8.688  1 56.21 ? 211 LEU   B O   1 
ATOM   4544 C  CB  . LEU   B 1 226 ? 16.002  10.88   -7.996  1 54.62 ? 211 LEU   B CB  1 
ATOM   4545 C  CG  . LEU   B 1 226 ? 15.481  11.923  -8.978  1 55.82 ? 211 LEU   B CG  1 
ATOM   4546 C  CD1 . LEU   B 1 226 ? 15.853  11.571  -10.411 1 56.45 ? 211 LEU   B CD1 1 
ATOM   4547 C  CD2 . LEU   B 1 226 ? 13.986  12.048  -8.878  1 56    ? 211 LEU   B CD2 1 
ATOM   4548 N  N   . GLN   B 1 227 ? 18.447  12.309  -6.474  1 56.18 ? 212 GLN   B N   1 
ATOM   4549 C  CA  . GLN   B 1 227 ? 19.192  13.52   -6.128  1 56.52 ? 212 GLN   B CA  1 
ATOM   4550 C  C   . GLN   B 1 227 ? 20.663  13.382  -6.529  1 55.89 ? 212 GLN   B C   1 
ATOM   4551 O  O   . GLN   B 1 227 ? 21.255  14.335  -7.024  1 56.19 ? 212 GLN   B O   1 
ATOM   4552 C  CB  . GLN   B 1 227 ? 19.026  13.828  -4.628  1 58.85 ? 212 GLN   B CB  1 
ATOM   4553 C  CG  . GLN   B 1 227 ? 17.562  14.028  -4.231  1 63.9  ? 212 GLN   B CG  1 
ATOM   4554 C  CD  . GLN   B 1 227 ? 16.949  15.203  -4.969  1 70.06 ? 212 GLN   B CD  1 
ATOM   4555 O  OE1 . GLN   B 1 227 ? 17.51   16.319  -4.989  1 72.61 ? 212 GLN   B OE1 1 
ATOM   4556 N  NE2 . GLN   B 1 227 ? 15.802  14.971  -5.608  1 69.82 ? 212 GLN   B NE2 1 
ATOM   4557 N  N   . VAL   B 1 228 ? 21.229  12.176  -6.359  1 55.08 ? 213 VAL   B N   1 
ATOM   4558 C  CA  . VAL   B 1 228 ? 22.592  11.83   -6.734  1 55.04 ? 213 VAL   B CA  1 
ATOM   4559 C  C   . VAL   B 1 228 ? 22.805  12.011  -8.25   1 55.59 ? 213 VAL   B C   1 
ATOM   4560 O  O   . VAL   B 1 228 ? 23.848  12.5    -8.675  1 55.98 ? 213 VAL   B O   1 
ATOM   4561 C  CB  . VAL   B 1 228 ? 22.926  10.395  -6.265  1 55.15 ? 213 VAL   B CB  1 
ATOM   4562 C  CG1 . VAL   B 1 228 ? 24.246  9.923   -6.853  1 55.81 ? 213 VAL   B CG1 1 
ATOM   4563 C  CG2 . VAL   B 1 228 ? 22.963  10.314  -4.743  1 55.01 ? 213 VAL   B CG2 1 
ATOM   4564 N  N   . PHE   B 1 229 ? 21.796  11.666  -9.047  1 55.59 ? 214 PHE   B N   1 
ATOM   4565 C  CA  . PHE   B 1 229 ? 21.775  11.781  -10.501 1 56.2  ? 214 PHE   B CA  1 
ATOM   4566 C  C   . PHE   B 1 229 ? 21.949  13.232  -10.976 1 56.71 ? 214 PHE   B C   1 
ATOM   4567 O  O   . PHE   B 1 229 ? 22.515  13.453  -12.049 1 56.45 ? 214 PHE   B O   1 
ATOM   4568 C  CB  . PHE   B 1 229 ? 20.429  11.268  -11.003 1 56.23 ? 214 PHE   B CB  1 
ATOM   4569 C  CG  . PHE   B 1 229 ? 20.468  10.313  -12.163 1 57.39 ? 214 PHE   B CG  1 
ATOM   4570 C  CD1 . PHE   B 1 229 ? 20.721  10.768  -13.441 1 58.49 ? 214 PHE   B CD1 1 
ATOM   4571 C  CD2 . PHE   B 1 229 ? 20.166  8.97    -11.988 1 58.38 ? 214 PHE   B CD2 1 
ATOM   4572 C  CE1 . PHE   B 1 229 ? 20.714  9.898   -14.518 1 59.38 ? 214 PHE   B CE1 1 
ATOM   4573 C  CE2 . PHE   B 1 229 ? 20.167  8.098   -13.066 1 59.07 ? 214 PHE   B CE2 1 
ATOM   4574 C  CZ  . PHE   B 1 229 ? 20.42   8.572   -14.326 1 59.09 ? 214 PHE   B CZ  1 
ATOM   4575 N  N   . HIS   B 1 230 ? 21.442  14.218  -10.195 1 56.92 ? 215 HIS   B N   1 
ATOM   4576 C  CA  . HIS   B 1 230 ? 21.521  15.643  -10.556 1 57.35 ? 215 HIS   B CA  1 
ATOM   4577 C  C   . HIS   B 1 230 ? 22.958  16.136  -10.778 1 56.36 ? 215 HIS   B C   1 
ATOM   4578 O  O   . HIS   B 1 230 ? 23.171  17.086  -11.532 1 56.13 ? 215 HIS   B O   1 
ATOM   4579 C  CB  . HIS   B 1 230 ? 20.816  16.534  -9.507  1 59.33 ? 215 HIS   B CB  1 
ATOM   4580 C  CG  . HIS   B 1 230 ? 19.35   16.279  -9.322  1 63.9  ? 215 HIS   B CG  1 
ATOM   4581 N  ND1 . HIS   B 1 230 ? 18.628  15.474  -10.194 1 66.45 ? 215 HIS   B ND1 1 
ATOM   4582 C  CD2 . HIS   B 1 230 ? 18.508  16.753  -8.371  1 65.87 ? 215 HIS   B CD2 1 
ATOM   4583 C  CE1 . HIS   B 1 230 ? 17.383  15.471  -9.738  1 67.28 ? 215 HIS   B CE1 1 
ATOM   4584 N  NE2 . HIS   B 1 230 ? 17.261  16.225  -8.642  1 67.36 ? 215 HIS   B NE2 1 
ATOM   4585 N  N   . GLN   B 1 231 ? 23.939  15.48   -10.137 1 55.58 ? 216 GLN   B N   1 
ATOM   4586 C  CA  . GLN   B 1 231 ? 25.355  15.826  -10.254 1 55.02 ? 216 GLN   B CA  1 
ATOM   4587 C  C   . GLN   B 1 231 ? 25.909  15.715  -11.673 1 54.75 ? 216 GLN   B C   1 
ATOM   4588 O  O   . GLN   B 1 231 ? 26.963  16.262  -11.942 1 54.57 ? 216 GLN   B O   1 
ATOM   4589 C  CB  . GLN   B 1 231 ? 26.203  14.944  -9.329  1 55.73 ? 216 GLN   B CB  1 
ATOM   4590 C  CG  . GLN   B 1 231 ? 25.915  15.123  -7.864  1 58.28 ? 216 GLN   B CG  1 
ATOM   4591 C  CD  . GLN   B 1 231 ? 26.784  14.206  -7.057  1 62.17 ? 216 GLN   B CD  1 
ATOM   4592 O  OE1 . GLN   B 1 231 ? 27.928  14.517  -6.743  1 62.28 ? 216 GLN   B OE1 1 
ATOM   4593 N  NE2 . GLN   B 1 231 ? 26.257  13.045  -6.71   1 64.54 ? 216 GLN   B NE2 1 
ATOM   4594 N  N   . ILE   B 1 232 ? 25.232  15.003  -12.569 1 54.71 ? 217 ILE   B N   1 
ATOM   4595 C  CA  . ILE   B 1 232 ? 25.706  14.811  -13.934 1 54.77 ? 217 ILE   B CA  1 
ATOM   4596 C  C   . ILE   B 1 232 ? 25.979  16.134  -14.668 1 54.64 ? 217 ILE   B C   1 
ATOM   4597 O  O   . ILE   B 1 232 ? 26.977  16.242  -15.374 1 54.25 ? 217 ILE   B O   1 
ATOM   4598 C  CB  . ILE   B 1 232 ? 24.746  13.885  -14.726 1 55.15 ? 217 ILE   B CB  1 
ATOM   4599 C  CG1 . ILE   B 1 232 ? 25.445  13.267  -15.945 1 56.17 ? 217 ILE   B CG1 1 
ATOM   4600 C  CG2 . ILE   B 1 232 ? 23.448  14.586  -15.099 1 55.68 ? 217 ILE   B CG2 1 
ATOM   4601 C  CD1 . ILE   B 1 232 ? 26.495  12.203  -15.559 1 57.3  ? 217 ILE   B CD1 1 
ATOM   4602 N  N   . HIS   B 1 233 ? 25.13   17.151  -14.449 1 54.58 ? 218 HIS   B N   1 
ATOM   4603 C  CA  . HIS   B 1 233 ? 25.236  18.445  -15.116 1 54.73 ? 218 HIS   B CA  1 
ATOM   4604 C  C   . HIS   B 1 233 ? 26.47   19.259  -14.743 1 55.51 ? 218 HIS   B C   1 
ATOM   4605 O  O   . HIS   B 1 233 ? 26.948  20.049  -15.555 1 55.36 ? 218 HIS   B O   1 
ATOM   4606 C  CB  . HIS   B 1 233 ? 23.971  19.261  -14.887 1 54.91 ? 218 HIS   B CB  1 
ATOM   4607 C  CG  . HIS   B 1 233 ? 22.711  18.533  -15.237 1 56.23 ? 218 HIS   B CG  1 
ATOM   4608 N  ND1 . HIS   B 1 233 ? 22.208  18.536  -16.526 1 57.57 ? 218 HIS   B ND1 1 
ATOM   4609 C  CD2 . HIS   B 1 233 ? 21.865  17.84   -14.44  1 57.34 ? 218 HIS   B CD2 1 
ATOM   4610 C  CE1 . HIS   B 1 233 ? 21.084  17.841  -16.476 1 57.9  ? 218 HIS   B CE1 1 
ATOM   4611 N  NE2 . HIS   B 1 233 ? 20.829  17.409  -15.242 1 57.98 ? 218 HIS   B NE2 1 
ATOM   4612 N  N   . ASP   B 1 234 ? 26.992  19.062  -13.527 1 55.96 ? 219 ASP   B N   1 
ATOM   4613 C  CA  . ASP   B 1 234 ? 28.166  19.792  -13.066 1 56.58 ? 219 ASP   B CA  1 
ATOM   4614 C  C   . ASP   B 1 234 ? 29.484  19.16   -13.488 1 57.11 ? 219 ASP   B C   1 
ATOM   4615 O  O   . ASP   B 1 234 ? 30.532  19.792  -13.307 1 58.3  ? 219 ASP   B O   1 
ATOM   4616 C  CB  . ASP   B 1 234 ? 28.167  19.9    -11.537 1 58.18 ? 219 ASP   B CB  1 
ATOM   4617 C  CG  . ASP   B 1 234 ? 26.93   20.546  -10.954 1 63.26 ? 219 ASP   B CG  1 
ATOM   4618 O  OD1 . ASP   B 1 234 ? 26.54   21.639  -11.441 1 63.57 ? 219 ASP   B OD1 1 
ATOM   4619 O  OD2 . ASP   B 1 234 ? 26.351  19.966  -10.008 1 65.56 ? 219 ASP   B OD2 1 
ATOM   4620 N  N   . HIS   B 1 235 ? 29.472  17.911  -13.971 1 55.88 ? 220 HIS   B N   1 
ATOM   4621 C  CA  . HIS   B 1 235 ? 30.726  17.223  -14.283 1 55.09 ? 220 HIS   B CA  1 
ATOM   4622 C  C   . HIS   B 1 235 ? 30.821  16.669  -15.705 1 53.89 ? 220 HIS   B C   1 
ATOM   4623 O  O   . HIS   B 1 235 ? 31.848  16.095  -16.061 1 54.21 ? 220 HIS   B O   1 
ATOM   4624 C  CB  . HIS   B 1 235 ? 30.987  16.121  -13.243 1 56.04 ? 220 HIS   B CB  1 
ATOM   4625 C  CG  . HIS   B 1 235 ? 30.821  16.592  -11.825 1 59.24 ? 220 HIS   B CG  1 
ATOM   4626 N  ND1 . HIS   B 1 235 ? 31.655  17.558  -11.278 1 60.96 ? 220 HIS   B ND1 1 
ATOM   4627 C  CD2 . HIS   B 1 235 ? 29.894  16.244  -10.899 1 60.59 ? 220 HIS   B CD2 1 
ATOM   4628 C  CE1 . HIS   B 1 235 ? 31.225  17.744  -10.037 1 61.39 ? 220 HIS   B CE1 1 
ATOM   4629 N  NE2 . HIS   B 1 235 ? 30.172  16.974  -9.761  1 61.51 ? 220 HIS   B NE2 1 
ATOM   4630 N  N   . VAL   B 1 236 ? 29.774  16.832  -16.518 1 52.58 ? 221 VAL   B N   1 
ATOM   4631 C  CA  . VAL   B 1 236 ? 29.783  16.351  -17.897 1 52.13 ? 221 VAL   B CA  1 
ATOM   4632 C  C   . VAL   B 1 236 ? 29.232  17.455  -18.791 1 52.09 ? 221 VAL   B C   1 
ATOM   4633 O  O   . VAL   B 1 236 ? 28.219  18.071  -18.44  1 52.59 ? 221 VAL   B O   1 
ATOM   4634 C  CB  . VAL   B 1 236 ? 28.948  15.043  -18.08  1 52.11 ? 221 VAL   B CB  1 
ATOM   4635 C  CG1 . VAL   B 1 236 ? 29.068  14.498  -19.498 1 52.52 ? 221 VAL   B CG1 1 
ATOM   4636 C  CG2 . VAL   B 1 236 ? 29.355  13.975  -17.082 1 52.05 ? 221 VAL   B CG2 1 
ATOM   4637 N  N   . ASN   B 1 237 ? 29.892  17.73   -19.928 1 51.25 ? 222 ASN   B N   1 
ATOM   4638 C  CA  . ASN   B 1 237 ? 29.356  18.696  -20.88  1 51.34 ? 222 ASN   B CA  1 
ATOM   4639 C  C   . ASN   B 1 237 ? 28.953  17.965  -22.155 1 50.8  ? 222 ASN   B C   1 
ATOM   4640 O  O   . ASN   B 1 237 ? 29.658  17.043  -22.589 1 50.76 ? 222 ASN   B O   1 
ATOM   4641 C  CB  . ASN   B 1 237 ? 30.285  19.884  -21.13  1 53.18 ? 222 ASN   B CB  1 
ATOM   4642 C  CG  . ASN   B 1 237 ? 31.443  19.633  -22.048 1 57.09 ? 222 ASN   B CG  1 
ATOM   4643 O  OD1 . ASN   B 1 237 ? 32.578  19.416  -21.599 1 58.91 ? 222 ASN   B OD1 1 
ATOM   4644 N  ND2 . ASN   B 1 237 ? 31.195  19.699  -23.354 1 57.5  ? 222 ASN   B ND2 1 
ATOM   4645 N  N   . PRO   B 1 238 ? 27.807  18.351  -22.751 1 50.13 ? 223 PRO   B N   1 
ATOM   4646 C  CA  . PRO   B 1 238 ? 27.295  17.625  -23.924 1 50.04 ? 223 PRO   B CA  1 
ATOM   4647 C  C   . PRO   B 1 238 ? 28.217  17.477  -25.13  1 50.92 ? 223 PRO   B C   1 
ATOM   4648 O  O   . PRO   B 1 238 ? 28.186  16.419  -25.757 1 51.04 ? 223 PRO   B O   1 
ATOM   4649 C  CB  . PRO   B 1 238 ? 26.037  18.408  -24.296 1 50.28 ? 223 PRO   B CB  1 
ATOM   4650 C  CG  . PRO   B 1 238 ? 25.577  18.99   -23.013 1 50.83 ? 223 PRO   B CG  1 
ATOM   4651 C  CD  . PRO   B 1 238 ? 26.843  19.371  -22.294 1 49.41 ? 223 PRO   B CD  1 
ATOM   4652 N  N   . LYS   B 1 239 ? 28.998  18.521  -25.481 1 51.36 ? 224 LYS   B N   1 
ATOM   4653 C  CA  . LYS   B 1 239 ? 29.878  18.459  -26.65  1 51.69 ? 224 LYS   B CA  1 
ATOM   4654 C  C   . LYS   B 1 239 ? 30.966  17.422  -26.447 1 51.33 ? 224 LYS   B C   1 
ATOM   4655 O  O   . LYS   B 1 239 ? 31.121  16.536  -27.287 1 51.56 ? 224 LYS   B O   1 
ATOM   4656 C  CB  . LYS   B 1 239 ? 30.477  19.845  -26.988 1 53.77 ? 224 LYS   B CB  1 
ATOM   4657 N  N   . ALA   B 1 240 ? 31.677  17.491  -25.318 1 50.86 ? 225 ALA   B N   1 
ATOM   4658 C  CA  . ALA   B 1 240 ? 32.746  16.541  -24.996 1 50.91 ? 225 ALA   B CA  1 
ATOM   4659 C  C   . ALA   B 1 240 ? 32.227  15.135  -24.826 1 51.3  ? 225 ALA   B C   1 
ATOM   4660 O  O   . ALA   B 1 240 ? 32.898  14.2    -25.255 1 52.27 ? 225 ALA   B O   1 
ATOM   4661 C  CB  . ALA   B 1 240 ? 33.47   16.966  -23.743 1 50.66 ? 225 ALA   B CB  1 
ATOM   4662 N  N   . PHE   B 1 241 ? 31.034  14.965  -24.212 1 50.37 ? 226 PHE   B N   1 
ATOM   4663 C  CA  . PHE   B 1 241 ? 30.475  13.627  -24.049 1 49.49 ? 226 PHE   B CA  1 
ATOM   4664 C  C   . PHE   B 1 241 ? 30.156  13.01   -25.413 1 49.5  ? 226 PHE   B C   1 
ATOM   4665 O  O   . PHE   B 1 241 ? 30.6    11.899  -25.701 1 50.05 ? 226 PHE   B O   1 
ATOM   4666 C  CB  . PHE   B 1 241 ? 29.214  13.621  -23.143 1 48.81 ? 226 PHE   B CB  1 
ATOM   4667 C  CG  . PHE   B 1 241 ? 28.591  12.238  -23.063 1 48.59 ? 226 PHE   B CG  1 
ATOM   4668 C  CD1 . PHE   B 1 241 ? 29.149  11.254  -22.262 1 48.69 ? 226 PHE   B CD1 1 
ATOM   4669 C  CD2 . PHE   B 1 241 ? 27.519  11.894  -23.869 1 48.63 ? 226 PHE   B CD2 1 
ATOM   4670 C  CE1 . PHE   B 1 241 ? 28.619  9.965   -22.237 1 48.92 ? 226 PHE   B CE1 1 
ATOM   4671 C  CE2 . PHE   B 1 241 ? 27.013  10.598  -23.861 1 49.23 ? 226 PHE   B CE2 1 
ATOM   4672 C  CZ  . PHE   B 1 241 ? 27.557  9.647   -23.032 1 48.79 ? 226 PHE   B CZ  1 
ATOM   4673 N  N   . PHE   B 1 242 ? 29.356  13.708  -26.228 1 48.7  ? 227 PHE   B N   1 
ATOM   4674 C  CA  . PHE   B 1 242 ? 28.922  13.176  -27.502 1 48.78 ? 227 PHE   B CA  1 
ATOM   4675 C  C   . PHE   B 1 242 ? 30.042  13.017  -28.541 1 49.88 ? 227 PHE   B C   1 
ATOM   4676 O  O   . PHE   B 1 242 ? 30.141  11.966  -29.175 1 50.07 ? 227 PHE   B O   1 
ATOM   4677 C  CB  . PHE   B 1 242 ? 27.77   14.019  -28.058 1 47.89 ? 227 PHE   B CB  1 
ATOM   4678 C  CG  . PHE   B 1 242 ? 27.235  13.498  -29.362 1 47.86 ? 227 PHE   B CG  1 
ATOM   4679 C  CD1 . PHE   B 1 242 ? 26.309  12.471  -29.388 1 48.1  ? 227 PHE   B CD1 1 
ATOM   4680 C  CD2 . PHE   B 1 242 ? 27.661  14.03   -30.566 1 48.28 ? 227 PHE   B CD2 1 
ATOM   4681 C  CE1 . PHE   B 1 242 ? 25.826  11.988  -30.593 1 48.87 ? 227 PHE   B CE1 1 
ATOM   4682 C  CE2 . PHE   B 1 242 ? 27.211  13.515  -31.771 1 48.75 ? 227 PHE   B CE2 1 
ATOM   4683 C  CZ  . PHE   B 1 242 ? 26.297  12.501  -31.78  1 48.61 ? 227 PHE   B CZ  1 
ATOM   4684 N  N   . SER   B 1 243 ? 30.836  14.062  -28.758 1 50.42 ? 228 SER   B N   1 
ATOM   4685 C  CA  . SER   B 1 243 ? 31.871  14.025  -29.789 1 51.56 ? 228 SER   B CA  1 
ATOM   4686 C  C   . SER   B 1 243 ? 33.118  13.27   -29.383 1 52.32 ? 228 SER   B C   1 
ATOM   4687 O  O   . SER   B 1 243 ? 33.868  12.878  -30.264 1 53.21 ? 228 SER   B O   1 
ATOM   4688 C  CB  . SER   B 1 243 ? 32.24   15.437  -30.232 1 53.28 ? 228 SER   B CB  1 
ATOM   4689 O  OG  . SER   B 1 243 ? 32.869  16.12   -29.161 1 56.24 ? 228 SER   B OG  1 
ATOM   4690 N  N   . VAL   B 1 244 ? 33.372  13.084  -28.078 1 51.95 ? 229 VAL   B N   1 
ATOM   4691 C  CA  . VAL   B 1 244 ? 34.592  12.414  -27.648 1 52.08 ? 229 VAL   B CA  1 
ATOM   4692 C  C   . VAL   B 1 244 ? 34.323  11.085  -26.904 1 51.61 ? 229 VAL   B C   1 
ATOM   4693 O  O   . VAL   B 1 244 ? 34.67   10.024  -27.423 1 51.23 ? 229 VAL   B O   1 
ATOM   4694 C  CB  . VAL   B 1 244 ? 35.522  13.372  -26.847 1 53.01 ? 229 VAL   B CB  1 
ATOM   4695 C  CG1 . VAL   B 1 244 ? 36.814  12.675  -26.434 1 53.27 ? 229 VAL   B CG1 1 
ATOM   4696 C  CG2 . VAL   B 1 244 ? 35.808  14.651  -27.631 1 53.55 ? 229 VAL   B CG2 1 
ATOM   4697 N  N   . LEU   B 1 245 ? 33.688  11.126  -25.723 1 51.23 ? 230 LEU   B N   1 
ATOM   4698 C  CA  . LEU   B 1 245 ? 33.475  9.911   -24.935 1 50.92 ? 230 LEU   B CA  1 
ATOM   4699 C  C   . LEU   B 1 245 ? 32.684  8.807   -25.659 1 51.46 ? 230 LEU   B C   1 
ATOM   4700 O  O   . LEU   B 1 245 ? 33.073  7.649   -25.578 1 52.01 ? 230 LEU   B O   1 
ATOM   4701 C  CB  . LEU   B 1 245 ? 32.845  10.229  -23.565 1 49.93 ? 230 LEU   B CB  1 
ATOM   4702 C  CG  . LEU   B 1 245 ? 32.949  9.126   -22.51  1 50.19 ? 230 LEU   B CG  1 
ATOM   4703 C  CD1 . LEU   B 1 245 ? 34.403  8.625   -22.345 1 50.35 ? 230 LEU   B CD1 1 
ATOM   4704 C  CD2 . LEU   B 1 245 ? 32.404  9.601   -21.196 1 50.21 ? 230 LEU   B CD2 1 
ATOM   4705 N  N   . ARG   B 1 246 ? 31.615  9.16    -26.365 1 51.26 ? 231 ARG   B N   1 
ATOM   4706 C  CA  . ARG   B 1 246 ? 30.753  8.225   -27.081 1 51.98 ? 231 ARG   B CA  1 
ATOM   4707 C  C   . ARG   B 1 246 ? 31.522  7.226   -27.964 1 51.92 ? 231 ARG   B C   1 
ATOM   4708 O  O   . ARG   B 1 246 ? 31.181  6.039   -27.987 1 52.11 ? 231 ARG   B O   1 
ATOM   4709 C  CB  . ARG   B 1 246 ? 29.702  9.018   -27.883 1 54.12 ? 231 ARG   B CB  1 
ATOM   4710 C  CG  . ARG   B 1 246 ? 29.199  8.398   -29.179 1 58.42 ? 231 ARG   B CG  1 
ATOM   4711 C  CD  . ARG   B 1 246 ? 28.242  9.336   -29.882 1 62.33 ? 231 ARG   B CD  1 
ATOM   4712 N  NE  . ARG   B 1 246 ? 28.887  10.025  -31     1 65.31 ? 231 ARG   B NE  1 
ATOM   4713 C  CZ  . ARG   B 1 246 ? 28.57   9.829   -32.276 1 68.12 ? 231 ARG   B CZ  1 
ATOM   4714 N  NH1 . ARG   B 1 246 ? 29.206  10.494  -33.232 1 68.35 ? 231 ARG   B NH1 1 
ATOM   4715 N  NH2 . ARG   B 1 246 ? 27.604  8.979   -32.606 1 68.34 ? 231 ARG   B NH2 1 
ATOM   4716 N  N   . ILE   B 1 247 ? 32.542  7.714   -28.68  1 51.2  ? 232 ILE   B N   1 
ATOM   4717 C  CA  . ILE   B 1 247 ? 33.378  6.929   -29.577 1 50.95 ? 232 ILE   B CA  1 
ATOM   4718 C  C   . ILE   B 1 247 ? 34.017  5.731   -28.894 1 48.82 ? 232 ILE   B C   1 
ATOM   4719 O  O   . ILE   B 1 247 ? 33.954  4.629   -29.424 1 48.92 ? 232 ILE   B O   1 
ATOM   4720 C  CB  . ILE   B 1 247 ? 34.451  7.861   -30.206 1 52.96 ? 232 ILE   B CB  1 
ATOM   4721 C  CG1 . ILE   B 1 247 ? 33.811  8.888   -31.139 1 55    ? 232 ILE   B CG1 1 
ATOM   4722 C  CG2 . ILE   B 1 247 ? 35.563  7.09    -30.913 1 53.59 ? 232 ILE   B CG2 1 
ATOM   4723 C  CD1 . ILE   B 1 247 ? 34.769  10.039  -31.421 1 57.41 ? 232 ILE   B CD1 1 
ATOM   4724 N  N   . TYR   B 1 248 ? 34.632  5.936   -27.739 1 47.13 ? 233 TYR   B N   1 
ATOM   4725 C  CA  . TYR   B 1 248 ? 35.339  4.87    -27.038 1 46.63 ? 233 TYR   B CA  1 
ATOM   4726 C  C   . TYR   B 1 248 ? 34.423  3.919   -26.281 1 46.97 ? 233 TYR   B C   1 
ATOM   4727 O  O   . TYR   B 1 248 ? 34.878  2.853   -25.872 1 47.19 ? 233 TYR   B O   1 
ATOM   4728 C  CB  . TYR   B 1 248 ? 36.428  5.453   -26.132 1 45.86 ? 233 TYR   B CB  1 
ATOM   4729 C  CG  . TYR   B 1 248 ? 37.409  6.274   -26.938 1 45.56 ? 233 TYR   B CG  1 
ATOM   4730 C  CD1 . TYR   B 1 248 ? 38.428  5.665   -27.658 1 45.45 ? 233 TYR   B CD1 1 
ATOM   4731 C  CD2 . TYR   B 1 248 ? 37.265  7.652   -27.052 1 45.82 ? 233 TYR   B CD2 1 
ATOM   4732 C  CE1 . TYR   B 1 248 ? 39.288  6.406   -28.451 1 46    ? 233 TYR   B CE1 1 
ATOM   4733 C  CE2 . TYR   B 1 248 ? 38.118  8.403   -27.846 1 46.4  ? 233 TYR   B CE2 1 
ATOM   4734 C  CZ  . TYR   B 1 248 ? 39.131  7.777   -28.543 1 47.05 ? 233 TYR   B CZ  1 
ATOM   4735 O  OH  . TYR   B 1 248 ? 39.984  8.527   -29.316 1 48.47 ? 233 TYR   B OH  1 
ATOM   4736 N  N   . LEU   B 1 249 ? 33.147  4.294   -26.081 1 46.57 ? 234 LEU   B N   1 
ATOM   4737 C  CA  . LEU   B 1 249 ? 32.177  3.419   -25.431 1 46.66 ? 234 LEU   B CA  1 
ATOM   4738 C  C   . LEU   B 1 249 ? 31.572  2.405   -26.42  1 46.92 ? 234 LEU   B C   1 
ATOM   4739 O  O   . LEU   B 1 249 ? 30.95   1.448   -25.982 1 46.88 ? 234 LEU   B O   1 
ATOM   4740 C  CB  . LEU   B 1 249 ? 31.049  4.237   -24.779 1 46.51 ? 234 LEU   B CB  1 
ATOM   4741 C  CG  . LEU   B 1 249 ? 31.45   5.211   -23.697 1 47.41 ? 234 LEU   B CG  1 
ATOM   4742 C  CD1 . LEU   B 1 249 ? 30.251  5.921   -23.169 1 48.23 ? 234 LEU   B CD1 1 
ATOM   4743 C  CD2 . LEU   B 1 249 ? 32.172  4.518   -22.568 1 47.91 ? 234 LEU   B CD2 1 
ATOM   4744 N  N   . SER   B 1 250 ? 31.745  2.619   -27.747 1 46.98 ? 235 SER   B N   1 
ATOM   4745 C  CA  . SER   B 1 250 ? 31.21   1.766   -28.801 1 47.11 ? 235 SER   B CA  1 
ATOM   4746 C  C   . SER   B 1 250 ? 31.824  0.39    -28.874 1 47.01 ? 235 SER   B C   1 
ATOM   4747 O  O   . SER   B 1 250 ? 33.034  0.231   -28.702 1 47.18 ? 235 SER   B O   1 
ATOM   4748 C  CB  . SER   B 1 250 ? 31.375  2.43    -30.156 1 48.59 ? 235 SER   B CB  1 
ATOM   4749 O  OG  . SER   B 1 250 ? 30.743  3.694   -30.139 1 52.22 ? 235 SER   B OG  1 
ATOM   4750 N  N   . GLY   B 1 251 ? 30.984  -0.58   -29.204 1 46.28 ? 236 GLY   B N   1 
ATOM   4751 C  CA  . GLY   B 1 251 ? 31.393  -1.958  -29.373 1 46.6  ? 236 GLY   B CA  1 
ATOM   4752 C  C   . GLY   B 1 251 ? 31.328  -2.392  -30.82  1 47.11 ? 236 GLY   B C   1 
ATOM   4753 O  O   . GLY   B 1 251 ? 31.296  -1.56   -31.725 1 46.9  ? 236 GLY   B O   1 
ATOM   4754 N  N   . TRP   B 1 252 ? 31.308  -3.701  -31.048 1 47.26 ? 237 TRP   B N   1 
ATOM   4755 C  CA  . TRP   B 1 252 ? 31.313  -4.243  -32.403 1 47.51 ? 237 TRP   B CA  1 
ATOM   4756 C  C   . TRP   B 1 252 ? 30.264  -5.321  -32.595 1 48.99 ? 237 TRP   B C   1 
ATOM   4757 O  O   . TRP   B 1 252 ? 30.588  -6.426  -32.992 1 48.87 ? 237 TRP   B O   1 
ATOM   4758 C  CB  . TRP   B 1 252 ? 32.73   -4.719  -32.839 1 46.41 ? 237 TRP   B CB  1 
ATOM   4759 C  CG  . TRP   B 1 252 ? 33.641  -5.173  -31.726 1 45.4  ? 237 TRP   B CG  1 
ATOM   4760 C  CD1 . TRP   B 1 252 ? 33.823  -6.447  -31.278 1 45.68 ? 237 TRP   B CD1 1 
ATOM   4761 C  CD2 . TRP   B 1 252 ? 34.492  -4.341  -30.92  1 44.9  ? 237 TRP   B CD2 1 
ATOM   4762 N  NE1 . TRP   B 1 252 ? 34.717  -6.459  -30.23  1 45.49 ? 237 TRP   B NE1 1 
ATOM   4763 C  CE2 . TRP   B 1 252 ? 35.145  -5.18   -29.993 1 45.24 ? 237 TRP   B CE2 1 
ATOM   4764 C  CE3 . TRP   B 1 252 ? 34.77   -2.967  -30.898 1 44.79 ? 237 TRP   B CE3 1 
ATOM   4765 C  CZ2 . TRP   B 1 252 ? 36.044  -4.685  -29.045 1 45.67 ? 237 TRP   B CZ2 1 
ATOM   4766 C  CZ3 . TRP   B 1 252 ? 35.661  -2.483  -29.962 1 45.37 ? 237 TRP   B CZ3 1 
ATOM   4767 C  CH2 . TRP   B 1 252 ? 36.291  -3.334  -29.054 1 45.52 ? 237 TRP   B CH2 1 
ATOM   4768 N  N   . LYS   B 1 253 ? 29.008  -4.994  -32.307 1 50.31 ? 238 LYS   B N   1 
ATOM   4769 C  CA  . LYS   B 1 253 ? 27.888  -5.895  -32.526 1 52.41 ? 238 LYS   B CA  1 
ATOM   4770 C  C   . LYS   B 1 253 ? 26.865  -5.058  -33.261 1 54.72 ? 238 LYS   B C   1 
ATOM   4771 O  O   . LYS   B 1 253 ? 26.396  -4.061  -32.715 1 55.3  ? 238 LYS   B O   1 
ATOM   4772 C  CB  . LYS   B 1 253 ? 27.305  -6.414  -31.214 1 54.5  ? 238 LYS   B CB  1 
ATOM   4773 C  CG  . LYS   B 1 253 ? 26.208  -7.434  -31.453 1 58.75 ? 238 LYS   B CG  1 
ATOM   4774 C  CD  . LYS   B 1 253 ? 25.823  -8.188  -30.201 1 63.63 ? 238 LYS   B CD  1 
ATOM   4775 C  CE  . LYS   B 1 253 ? 24.576  -9.016  -30.422 1 68.11 ? 238 LYS   B CE  1 
ATOM   4776 N  NZ  . LYS   B 1 253 ? 24.681  -9.888  -31.628 1 70.93 ? 238 LYS   B NZ  1 
ATOM   4777 N  N   . GLY   B 1 254 ? 26.588  -5.407  -34.515 1 55.72 ? 239 GLY   B N   1 
ATOM   4778 C  CA  . GLY   B 1 254 ? 25.698  -4.607  -35.343 1 57.38 ? 239 GLY   B CA  1 
ATOM   4779 C  C   . GLY   B 1 254 ? 26.266  -3.223  -35.626 1 59.19 ? 239 GLY   B C   1 
ATOM   4780 O  O   . GLY   B 1 254 ? 25.513  -2.275  -35.866 1 59.68 ? 239 GLY   B O   1 
ATOM   4781 N  N   . ASN   B 1 255 ? 27.606  -3.087  -35.582 1 59.85 ? 240 ASN   B N   1 
ATOM   4782 C  CA  . ASN   B 1 255 ? 28.256  -1.81   -35.821 1 60.96 ? 240 ASN   B CA  1 
ATOM   4783 C  C   . ASN   B 1 255 ? 28.702  -1.743  -37.262 1 62.68 ? 240 ASN   B C   1 
ATOM   4784 O  O   . ASN   B 1 255 ? 29.573  -2.508  -37.676 1 63.55 ? 240 ASN   B O   1 
ATOM   4785 C  CB  . ASN   B 1 255 ? 29.456  -1.606  -34.883 1 61.02 ? 240 ASN   B CB  1 
ATOM   4786 C  CG  . ASN   B 1 255 ? 29.96   -0.179  -34.857 1 62.86 ? 240 ASN   B CG  1 
ATOM   4787 O  OD1 . ASN   B 1 255 ? 29.88   0.557   -35.842 1 63.97 ? 240 ASN   B OD1 1 
ATOM   4788 N  ND2 . ASN   B 1 255 ? 30.482  0.26    -33.73  1 62.4  ? 240 ASN   B ND2 1 
ATOM   4789 N  N   . PRO   B 1 256 ? 28.165  -0.788  -38.032 1 63    ? 241 PRO   B N   1 
ATOM   4790 C  CA  . PRO   B 1 256 ? 28.583  -0.662  -39.434 1 63.31 ? 241 PRO   B CA  1 
ATOM   4791 C  C   . PRO   B 1 256 ? 30.093  -0.489  -39.644 1 63.78 ? 241 PRO   B C   1 
ATOM   4792 O  O   . PRO   B 1 256 ? 30.608  -0.981  -40.643 1 64.27 ? 241 PRO   B O   1 
ATOM   4793 C  CB  . PRO   B 1 256 ? 27.77   0.539   -39.928 1 64.08 ? 241 PRO   B CB  1 
ATOM   4794 C  CG  . PRO   B 1 256 ? 26.568  0.587   -39.022 1 64.23 ? 241 PRO   B CG  1 
ATOM   4795 C  CD  . PRO   B 1 256 ? 27.11   0.188   -37.688 1 62.64 ? 241 PRO   B CD  1 
ATOM   4796 N  N   . GLN   B 1 257 ? 30.81   0.146   -38.69  1 63.74 ? 242 GLN   B N   1 
ATOM   4797 C  CA  . GLN   B 1 257 ? 32.264  0.345   -38.772 1 64.55 ? 242 GLN   B CA  1 
ATOM   4798 C  C   . GLN   B 1 257 ? 33.079  -0.956  -38.627 1 65.13 ? 242 GLN   B C   1 
ATOM   4799 O  O   . GLN   B 1 257 ? 34.236  -1.006  -39.053 1 64.77 ? 242 GLN   B O   1 
ATOM   4800 C  CB  . GLN   B 1 257 ? 32.74   1.365   -37.73  1 66.05 ? 242 GLN   B CB  1 
ATOM   4801 C  CG  . GLN   B 1 257 ? 32.095  2.733   -37.859 1 69.62 ? 242 GLN   B CG  1 
ATOM   4802 C  CD  . GLN   B 1 257 ? 32.816  3.742   -36.995 1 74.63 ? 242 GLN   B CD  1 
ATOM   4803 O  OE1 . GLN   B 1 257 ? 33.913  4.195   -37.314 1 76.15 ? 242 GLN   B OE1 1 
ATOM   4804 N  NE2 . GLN   B 1 257 ? 32.223  4.116   -35.874 1 75.81 ? 242 GLN   B NE2 1 
ATOM   4805 N  N   . LEU   B 1 258 ? 32.49   -1.982  -37.993 1 65.62 ? 243 LEU   B N   1 
ATOM   4806 C  CA  . LEU   B 1 258 ? 33.103  -3.294  -37.772 1 66.65 ? 243 LEU   B CA  1 
ATOM   4807 C  C   . LEU   B 1 258 ? 31.985  -4.342  -37.907 1 67.58 ? 243 LEU   B C   1 
ATOM   4808 O  O   . LEU   B 1 258 ? 31.715  -5.097  -36.97  1 67.97 ? 243 LEU   B O   1 
ATOM   4809 C  CB  . LEU   B 1 258 ? 33.722  -3.36   -36.364 1 66.96 ? 243 LEU   B CB  1 
ATOM   4810 C  CG  . LEU   B 1 258 ? 35.097  -2.772  -36.171 1 68.81 ? 243 LEU   B CG  1 
ATOM   4811 C  CD1 . LEU   B 1 258 ? 35.531  -2.936  -34.748 1 69.68 ? 243 LEU   B CD1 1 
ATOM   4812 C  CD2 . LEU   B 1 258 ? 36.11   -3.445  -37.067 1 69.61 ? 243 LEU   B CD2 1 
ATOM   4813 N  N   . SER   B 1 259 ? 31.312  -4.35   -39.076 1 67.89 ? 244 SER   B N   1 
ATOM   4814 C  CA  . SER   B 1 259 ? 30.155  -5.187  -39.418 1 68.42 ? 244 SER   B CA  1 
ATOM   4815 C  C   . SER   B 1 259 ? 30.302  -6.685  -39.111 1 68.34 ? 244 SER   B C   1 
ATOM   4816 O  O   . SER   B 1 259 ? 29.296  -7.343  -38.86  1 68.66 ? 244 SER   B O   1 
ATOM   4817 C  CB  . SER   B 1 259 ? 29.766  -4.99   -40.88  1 70.21 ? 244 SER   B CB  1 
ATOM   4818 O  OG  . SER   B 1 259 ? 30.801  -5.409  -41.758 1 72.93 ? 244 SER   B OG  1 
ATOM   4819 N  N   . ASP   B 1 260 ? 31.526  -7.222  -39.122 1 67.92 ? 245 ASP   B N   1 
ATOM   4820 C  CA  . ASP   B 1 260 ? 31.74   -8.644  -38.806 1 68.05 ? 245 ASP   B CA  1 
ATOM   4821 C  C   . ASP   B 1 260 ? 32.347  -8.903  -37.404 1 67.13 ? 245 ASP   B C   1 
ATOM   4822 O  O   . ASP   B 1 260 ? 32.487  -10.062 -37     1 67.17 ? 245 ASP   B O   1 
ATOM   4823 C  CB  . ASP   B 1 260 ? 32.58   -9.322  -39.897 1 70.48 ? 245 ASP   B CB  1 
ATOM   4824 C  CG  . ASP   B 1 260 ? 31.914  -9.239  -41.254 1 76.93 ? 245 ASP   B CG  1 
ATOM   4825 O  OD1 . ASP   B 1 260 ? 30.776  -9.757  -41.392 1 77.46 ? 245 ASP   B OD1 1 
ATOM   4826 O  OD2 . ASP   B 1 260 ? 32.515  -8.637  -42.175 1 80.18 ? 245 ASP   B OD2 1 
ATOM   4827 N  N   . GLY   B 1 261 ? 32.678  -7.83   -36.682 1 65.86 ? 246 GLY   B N   1 
ATOM   4828 C  CA  . GLY   B 1 261 ? 33.268  -7.918  -35.359 1 65.08 ? 246 GLY   B CA  1 
ATOM   4829 C  C   . GLY   B 1 261 ? 34.762  -7.7    -35.377 1 64.07 ? 246 GLY   B C   1 
ATOM   4830 O  O   . GLY   B 1 261 ? 35.33   -7.291  -36.386 1 64.01 ? 246 GLY   B O   1 
ATOM   4831 N  N   . LEU   B 1 262 ? 35.411  -7.986  -34.259 1 63.16 ? 247 LEU   B N   1 
ATOM   4832 C  CA  . LEU   B 1 262 ? 36.844  -7.799  -34.105 1 62.38 ? 247 LEU   B CA  1 
ATOM   4833 C  C   . LEU   B 1 262 ? 37.555  -9.144  -34.152 1 62.52 ? 247 LEU   B C   1 
ATOM   4834 O  O   . LEU   B 1 262 ? 37.043  -10.116 -33.609 1 62.74 ? 247 LEU   B O   1 
ATOM   4835 C  CB  . LEU   B 1 262 ? 37.101  -7.125  -32.744 1 61.8  ? 247 LEU   B CB  1 
ATOM   4836 C  CG  . LEU   B 1 262 ? 38.533  -6.758  -32.427 1 61.99 ? 247 LEU   B CG  1 
ATOM   4837 C  CD1 . LEU   B 1 262 ? 39.044  -5.705  -33.397 1 62.52 ? 247 LEU   B CD1 1 
ATOM   4838 C  CD2 . LEU   B 1 262 ? 38.675  -6.306  -30.984 1 61.78 ? 247 LEU   B CD2 1 
ATOM   4839 N  N   . VAL   B 1 263 ? 38.739  -9.204  -34.779 1 62.24 ? 248 VAL   B N   1 
ATOM   4840 C  CA  . VAL   B 1 263 ? 39.517  -10.436 -34.812 1 62.22 ? 248 VAL   B CA  1 
ATOM   4841 C  C   . VAL   B 1 263 ? 40.411  -10.447 -33.576 1 62.76 ? 248 VAL   B C   1 
ATOM   4842 O  O   . VAL   B 1 263 ? 41.156  -9.496  -33.346 1 62.31 ? 248 VAL   B O   1 
ATOM   4843 C  CB  . VAL   B 1 263 ? 40.325  -10.613 -36.127 1 62.25 ? 248 VAL   B CB  1 
ATOM   4844 C  CG1 . VAL   B 1 263 ? 41.284  -11.797 -36.031 1 62.53 ? 248 VAL   B CG1 1 
ATOM   4845 C  CG2 . VAL   B 1 263 ? 39.394  -10.775 -37.321 1 62.33 ? 248 VAL   B CG2 1 
ATOM   4846 N  N   . TYR   B 1 264 ? 40.298  -11.499 -32.75  1 63.5  ? 249 TYR   B N   1 
ATOM   4847 C  CA  . TYR   B 1 264 ? 41.106  -11.636 -31.54  1 64.69 ? 249 TYR   B CA  1 
ATOM   4848 C  C   . TYR   B 1 264 ? 42.259  -12.581 -31.873 1 67.49 ? 249 TYR   B C   1 
ATOM   4849 O  O   . TYR   B 1 264 ? 42.215  -13.764 -31.543 1 67.97 ? 249 TYR   B O   1 
ATOM   4850 C  CB  . TYR   B 1 264 ? 40.248  -12.155 -30.368 1 63.52 ? 249 TYR   B CB  1 
ATOM   4851 C  CG  . TYR   B 1 264 ? 39.205  -11.157 -29.906 1 62.79 ? 249 TYR   B CG  1 
ATOM   4852 C  CD1 . TYR   B 1 264 ? 37.975  -11.063 -30.537 1 63.14 ? 249 TYR   B CD1 1 
ATOM   4853 C  CD2 . TYR   B 1 264 ? 39.465  -10.283 -28.86  1 63.09 ? 249 TYR   B CD2 1 
ATOM   4854 C  CE1 . TYR   B 1 264 ? 37.025  -10.133 -30.133 1 63.64 ? 249 TYR   B CE1 1 
ATOM   4855 C  CE2 . TYR   B 1 264 ? 38.529  -9.342  -28.455 1 63.48 ? 249 TYR   B CE2 1 
ATOM   4856 C  CZ  . TYR   B 1 264 ? 37.306  -9.273  -29.091 1 64.08 ? 249 TYR   B CZ  1 
ATOM   4857 O  OH  . TYR   B 1 264 ? 36.377  -8.342  -28.685 1 64.83 ? 249 TYR   B OH  1 
ATOM   4858 N  N   . GLU   B 1 265 ? 43.262  -12.048 -32.588 1 69.09 ? 250 GLU   B N   1 
ATOM   4859 C  CA  . GLU   B 1 265 ? 44.427  -12.764 -33.101 1 70.81 ? 250 GLU   B CA  1 
ATOM   4860 C  C   . GLU   B 1 265 ? 45.059  -13.728 -32.112 1 72.1  ? 250 GLU   B C   1 
ATOM   4861 O  O   . GLU   B 1 265 ? 45.362  -13.35  -30.982 1 72.52 ? 250 GLU   B O   1 
ATOM   4862 C  CB  . GLU   B 1 265 ? 45.46   -11.761 -33.624 1 73.56 ? 250 GLU   B CB  1 
ATOM   4863 C  CG  . GLU   B 1 265 ? 46.634  -12.372 -34.367 1 78    ? 250 GLU   B CG  1 
ATOM   4864 C  CD  . GLU   B 1 265 ? 47.606  -11.324 -34.874 1 83.43 ? 250 GLU   B CD  1 
ATOM   4865 O  OE1 . GLU   B 1 265 ? 48.421  -10.823 -34.064 1 82.1  ? 250 GLU   B OE1 1 
ATOM   4866 O  OE2 . GLU   B 1 265 ? 47.537  -10.987 -36.078 1 86.93 ? 250 GLU   B OE2 1 
ATOM   4867 N  N   . GLY   B 1 266 ? 45.218  -14.978 -32.533 1 72.58 ? 251 GLY   B N   1 
ATOM   4868 C  CA  . GLY   B 1 266 ? 45.805  -16.011 -31.685 1 73.47 ? 251 GLY   B CA  1 
ATOM   4869 C  C   . GLY   B 1 266 ? 44.836  -16.702 -30.743 1 74.19 ? 251 GLY   B C   1 
ATOM   4870 O  O   . GLY   B 1 266 ? 45.196  -17.691 -30.097 1 74.28 ? 251 GLY   B O   1 
ATOM   4871 N  N   . PHE   B 1 267 ? 43.598  -16.188 -30.641 1 74.5  ? 252 PHE   B N   1 
ATOM   4872 C  CA  . PHE   B 1 267 ? 42.594  -16.776 -29.765 1 74.84 ? 252 PHE   B CA  1 
ATOM   4873 C  C   . PHE   B 1 267 ? 41.448  -17.405 -30.553 1 75.2  ? 252 PHE   B C   1 
ATOM   4874 O  O   . PHE   B 1 267 ? 41.071  -18.535 -30.256 1 75.27 ? 252 PHE   B O   1 
ATOM   4875 C  CB  . PHE   B 1 267 ? 42.095  -15.766 -28.724 1 74.57 ? 252 PHE   B CB  1 
ATOM   4876 C  CG  . PHE   B 1 267 ? 41.572  -16.455 -27.489 1 75.04 ? 252 PHE   B CG  1 
ATOM   4877 C  CD1 . PHE   B 1 267 ? 42.42   -16.788 -26.451 1 75.74 ? 252 PHE   B CD1 1 
ATOM   4878 C  CD2 . PHE   B 1 267 ? 40.237  -16.805 -27.384 1 75.91 ? 252 PHE   B CD2 1 
ATOM   4879 C  CE1 . PHE   B 1 267 ? 41.937  -17.435 -25.322 1 76.7  ? 252 PHE   B CE1 1 
ATOM   4880 C  CE2 . PHE   B 1 267 ? 39.757  -17.455 -26.256 1 76.53 ? 252 PHE   B CE2 1 
ATOM   4881 C  CZ  . PHE   B 1 267 ? 40.606  -17.763 -25.23  1 76.51 ? 252 PHE   B CZ  1 
ATOM   4882 N  N   . TRP   B 1 268 ? 40.909  -16.691 -31.558 1 75.36 ? 253 TRP   B N   1 
ATOM   4883 C  CA  . TRP   B 1 268 ? 39.836  -17.183 -32.436 1 76.07 ? 253 TRP   B CA  1 
ATOM   4884 C  C   . TRP   B 1 268 ? 40.208  -16.862 -33.881 1 76.91 ? 253 TRP   B C   1 
ATOM   4885 O  O   . TRP   B 1 268 ? 40.791  -15.811 -34.147 1 77.18 ? 253 TRP   B O   1 
ATOM   4886 C  CB  . TRP   B 1 268 ? 38.482  -16.516 -32.13  1 75.98 ? 253 TRP   B CB  1 
ATOM   4887 C  CG  . TRP   B 1 268 ? 37.881  -16.85  -30.798 1 76.61 ? 253 TRP   B CG  1 
ATOM   4888 C  CD1 . TRP   B 1 268 ? 37.499  -18.081 -30.354 1 77.45 ? 253 TRP   B CD1 1 
ATOM   4889 C  CD2 . TRP   B 1 268 ? 37.486  -15.917 -29.784 1 76.8  ? 253 TRP   B CD2 1 
ATOM   4890 N  NE1 . TRP   B 1 268 ? 36.95   -17.981 -29.098 1 77.79 ? 253 TRP   B NE1 1 
ATOM   4891 C  CE2 . TRP   B 1 268 ? 36.924  -16.66  -28.727 1 77.67 ? 253 TRP   B CE2 1 
ATOM   4892 C  CE3 . TRP   B 1 268 ? 37.578  -14.527 -29.653 1 77.24 ? 253 TRP   B CE3 1 
ATOM   4893 C  CZ2 . TRP   B 1 268 ? 36.455  -16.056 -27.558 1 78.36 ? 253 TRP   B CZ2 1 
ATOM   4894 C  CZ3 . TRP   B 1 268 ? 37.128  -13.933 -28.49  1 78.1  ? 253 TRP   B CZ3 1 
ATOM   4895 C  CH2 . TRP   B 1 268 ? 36.573  -14.693 -27.46  1 78.28 ? 253 TRP   B CH2 1 
ATOM   4896 N  N   . GLU   B 1 269 ? 39.834  -17.735 -34.822 1 77.01 ? 254 GLU   B N   1 
ATOM   4897 C  CA  . GLU   B 1 269 ? 40.139  -17.511 -36.234 1 77.2  ? 254 GLU   B CA  1 
ATOM   4898 C  C   . GLU   B 1 269 ? 39.248  -16.447 -36.869 1 76.7  ? 254 GLU   B C   1 
ATOM   4899 O  O   . GLU   B 1 269 ? 39.737  -15.614 -37.63  1 77    ? 254 GLU   B O   1 
ATOM   4900 C  CB  . GLU   B 1 269 ? 40.034  -18.821 -37.026 1 79.74 ? 254 GLU   B CB  1 
ATOM   4901 N  N   . ASP   B 1 270 ? 37.942  -16.488 -36.58  1 75.84 ? 255 ASP   B N   1 
ATOM   4902 C  CA  . ASP   B 1 270 ? 36.964  -15.552 -37.143 1 75.31 ? 255 ASP   B CA  1 
ATOM   4903 C  C   . ASP   B 1 270 ? 36.735  -14.304 -36.265 1 74.34 ? 255 ASP   B C   1 
ATOM   4904 O  O   . ASP   B 1 270 ? 36.946  -14.351 -35.047 1 74.54 ? 255 ASP   B O   1 
ATOM   4905 C  CB  . ASP   B 1 270 ? 35.629  -16.288 -37.364 1 76.85 ? 255 ASP   B CB  1 
ATOM   4906 N  N   . PRO   B 1 271 ? 36.279  -13.18  -36.861 1 72.94 ? 256 PRO   B N   1 
ATOM   4907 C  CA  . PRO   B 1 271 ? 35.975  -12.001 -36.037 1 71.85 ? 256 PRO   B CA  1 
ATOM   4908 C  C   . PRO   B 1 271 ? 34.737  -12.239 -35.17  1 70.38 ? 256 PRO   B C   1 
ATOM   4909 O  O   . PRO   B 1 271 ? 33.734  -12.769 -35.648 1 70.61 ? 256 PRO   B O   1 
ATOM   4910 C  CB  . PRO   B 1 271 ? 35.744  -10.885 -37.067 1 72.72 ? 256 PRO   B CB  1 
ATOM   4911 C  CG  . PRO   B 1 271 ? 35.352  -11.574 -38.311 1 73.34 ? 256 PRO   B CG  1 
ATOM   4912 C  CD  . PRO   B 1 271 ? 35.97   -12.949 -38.288 1 72.16 ? 256 PRO   B CD  1 
ATOM   4913 N  N   . LYS   B 1 272 ? 34.82   -11.874 -33.882 1 68.59 ? 257 LYS   B N   1 
ATOM   4914 C  CA  . LYS   B 1 272 ? 33.722  -12.041 -32.931 1 66.76 ? 257 LYS   B CA  1 
ATOM   4915 C  C   . LYS   B 1 272 ? 33.021  -10.706 -32.637 1 64.59 ? 257 LYS   B C   1 
ATOM   4916 O  O   . LYS   B 1 272 ? 33.671  -9.669  -32.492 1 63.93 ? 257 LYS   B O   1 
ATOM   4917 C  CB  . LYS   B 1 272 ? 34.239  -12.662 -31.629 1 68.27 ? 257 LYS   B CB  1 
ATOM   4918 N  N   . GLU   B 1 273 ? 31.689  -10.745 -32.526 1 62.92 ? 258 GLU   B N   1 
ATOM   4919 C  CA  . GLU   B 1 273 ? 30.88   -9.567  -32.222 1 61.32 ? 258 GLU   B CA  1 
ATOM   4920 C  C   . GLU   B 1 273 ? 30.531  -9.486  -30.735 1 59.37 ? 258 GLU   B C   1 
ATOM   4921 O  O   . GLU   B 1 273 ? 29.983  -10.439 -30.173 1 59.84 ? 258 GLU   B O   1 
ATOM   4922 C  CB  . GLU   B 1 273 ? 29.577  -9.588  -33.027 1 63.29 ? 258 GLU   B CB  1 
ATOM   4923 C  CG  . GLU   B 1 273 ? 29.72   -9.113  -34.46  1 67.98 ? 258 GLU   B CG  1 
ATOM   4924 C  CD  . GLU   B 1 273 ? 28.384  -8.773  -35.085 1 73.95 ? 258 GLU   B CD  1 
ATOM   4925 O  OE1 . GLU   B 1 273 ? 27.485  -9.644  -35.065 1 76.44 ? 258 GLU   B OE1 1 
ATOM   4926 O  OE2 . GLU   B 1 273 ? 28.224  -7.631  -35.571 1 75.36 ? 258 GLU   B OE2 1 
ATOM   4927 N  N   . PHE   B 1 274 ? 30.832  -8.345  -30.099 1 56.93 ? 259 PHE   B N   1 
ATOM   4928 C  CA  . PHE   B 1 274 ? 30.499  -8.096  -28.696 1 54.8  ? 259 PHE   B CA  1 
ATOM   4929 C  C   . PHE   B 1 274 ? 29.942  -6.685  -28.575 1 52.2  ? 259 PHE   B C   1 
ATOM   4930 O  O   . PHE   B 1 274 ? 30.484  -5.758  -29.173 1 52.15 ? 259 PHE   B O   1 
ATOM   4931 C  CB  . PHE   B 1 274 ? 31.719  -8.274  -27.781 1 54.82 ? 259 PHE   B CB  1 
ATOM   4932 C  CG  . PHE   B 1 274 ? 32.236  -9.689  -27.705 1 55.82 ? 259 PHE   B CG  1 
ATOM   4933 C  CD1 . PHE   B 1 274 ? 31.517  -10.672 -27.048 1 56.62 ? 259 PHE   B CD1 1 
ATOM   4934 C  CD2 . PHE   B 1 274 ? 33.442  -10.038 -28.294 1 56.39 ? 259 PHE   B CD2 1 
ATOM   4935 C  CE1 . PHE   B 1 274 ? 31.991  -11.972 -26.982 1 57.17 ? 259 PHE   B CE1 1 
ATOM   4936 C  CE2 . PHE   B 1 274 ? 33.906  -11.341 -28.238 1 57.06 ? 259 PHE   B CE2 1 
ATOM   4937 C  CZ  . PHE   B 1 274 ? 33.178  -12.3   -27.583 1 56.93 ? 259 PHE   B CZ  1 
ATOM   4938 N  N   . ALA   B 1 275 ? 28.857  -6.518  -27.821 1 50.07 ? 260 ALA   B N   1 
ATOM   4939 C  CA  . ALA   B 1 275 ? 28.243  -5.208  -27.631 1 48.48 ? 260 ALA   B CA  1 
ATOM   4940 C  C   . ALA   B 1 275 ? 29.109  -4.341  -26.711 1 47.31 ? 260 ALA   B C   1 
ATOM   4941 O  O   . ALA   B 1 275 ? 29.794  -4.857  -25.822 1 47.2  ? 260 ALA   B O   1 
ATOM   4942 C  CB  . ALA   B 1 275 ? 26.85   -5.366  -27.04  1 48.03 ? 260 ALA   B CB  1 
ATOM   4943 N  N   . GLY   B 1 276 ? 29.077  -3.035  -26.933 1 46.06 ? 261 GLY   B N   1 
ATOM   4944 C  CA  . GLY   B 1 276 ? 29.852  -2.105  -26.126 1 45.69 ? 261 GLY   B CA  1 
ATOM   4945 C  C   . GLY   B 1 276 ? 29.312  -1.939  -24.719 1 45.44 ? 261 GLY   B C   1 
ATOM   4946 O  O   . GLY   B 1 276 ? 28.216  -2.412  -24.399 1 45.54 ? 261 GLY   B O   1 
ATOM   4947 N  N   . GLY   B 1 277 ? 30.089  -1.279  -23.867 1 44.38 ? 262 GLY   B N   1 
ATOM   4948 C  CA  . GLY   B 1 277 ? 29.717  -1.015  -22.482 1 43.52 ? 262 GLY   B CA  1 
ATOM   4949 C  C   . GLY   B 1 277 ? 28.37   -0.326  -22.376 1 42.71 ? 262 GLY   B C   1 
ATOM   4950 O  O   . GLY   B 1 277 ? 28.025  0.543   -23.196 1 42.44 ? 262 GLY   B O   1 
ATOM   4951 N  N   . SER   B 1 278 ? 27.567  -0.801  -21.434 1 41.66 ? 263 SER   B N   1 
ATOM   4952 C  CA  . SER   B 1 278 ? 26.23   -0.306  -21.277 1 41.1  ? 263 SER   B CA  1 
ATOM   4953 C  C   . SER   B 1 278 ? 25.789  -0.308  -19.846 1 39.86 ? 263 SER   B C   1 
ATOM   4954 O  O   . SER   B 1 278 ? 26.066  -1.257  -19.119 1 39.51 ? 263 SER   B O   1 
ATOM   4955 C  CB  . SER   B 1 278 ? 25.268  -1.148  -22.107 1 42.39 ? 263 SER   B CB  1 
ATOM   4956 O  OG  . SER   B 1 278 ? 23.945  -0.649  -22.026 1 45.17 ? 263 SER   B OG  1 
ATOM   4957 N  N   . ALA   B 1 279 ? 25.048  0.737   -19.448 1 38.78 ? 264 ALA   B N   1 
ATOM   4958 C  CA  . ALA   B 1 279 ? 24.439  0.732   -18.129 1 37.81 ? 264 ALA   B CA  1 
ATOM   4959 C  C   . ALA   B 1 279 ? 23.28   -0.29   -18.065 1 37.97 ? 264 ALA   B C   1 
ATOM   4960 O  O   . ALA   B 1 279 ? 22.83   -0.612  -16.979 1 38.21 ? 264 ALA   B O   1 
ATOM   4961 C  CB  . ALA   B 1 279 ? 24.002  2.112   -17.731 1 37.21 ? 264 ALA   B CB  1 
ATOM   4962 N  N   . GLY   B 1 280 ? 22.88   -0.862  -19.208 1 38.22 ? 265 GLY   B N   1 
ATOM   4963 C  CA  . GLY   B 1 280 ? 21.965  -1.99   -19.298 1 38.99 ? 265 GLY   B CA  1 
ATOM   4964 C  C   . GLY   B 1 280 ? 22.572  -3.233  -18.651 1 39.56 ? 265 GLY   B C   1 
ATOM   4965 O  O   . GLY   B 1 280 ? 21.848  -4.174  -18.338 1 40.6  ? 265 GLY   B O   1 
ATOM   4966 N  N   . GLN   B 1 281 ? 23.906  -3.232  -18.415 1 38.74 ? 266 GLN   B N   1 
ATOM   4967 C  CA  . GLN   B 1 281 ? 24.708  -4.25   -17.715 1 38.08 ? 266 GLN   B CA  1 
ATOM   4968 C  C   . GLN   B 1 281 ? 24.761  -3.974  -16.182 1 39.17 ? 266 GLN   B C   1 
ATOM   4969 O  O   . GLN   B 1 281 ? 25.349  -4.761  -15.445 1 38.69 ? 266 GLN   B O   1 
ATOM   4970 C  CB  . GLN   B 1 281 ? 26.141  -4.312  -18.293 1 36.69 ? 266 GLN   B CB  1 
ATOM   4971 C  CG  . GLN   B 1 281 ? 26.186  -4.599  -19.784 1 36.22 ? 266 GLN   B CG  1 
ATOM   4972 C  CD  . GLN   B 1 281 ? 27.483  -4.222  -20.45  1 39.43 ? 266 GLN   B CD  1 
ATOM   4973 O  OE1 . GLN   B 1 281 ? 28.354  -3.548  -19.884 1 40.62 ? 266 GLN   B OE1 1 
ATOM   4974 N  NE2 . GLN   B 1 281 ? 27.623  -4.586  -21.709 1 39.93 ? 266 GLN   B NE2 1 
ATOM   4975 N  N   . SER   B 1 282 ? 24.18   -2.854  -15.703 1 40.36 ? 267 SER   B N   1 
ATOM   4976 C  CA  . SER   B 1 282 ? 24.12   -2.552  -14.278 1 41.95 ? 267 SER   B CA  1 
ATOM   4977 C  C   . SER   B 1 282 ? 23.175  -3.574  -13.624 1 43.86 ? 267 SER   B C   1 
ATOM   4978 O  O   . SER   B 1 282 ? 22.047  -3.758  -14.076 1 43.97 ? 267 SER   B O   1 
ATOM   4979 C  CB  . SER   B 1 282 ? 23.578  -1.145  -14.037 1 42.67 ? 267 SER   B CB  1 
ATOM   4980 O  OG  . SER   B 1 282 ? 23.099  -1.009  -12.708 1 44.79 ? 267 SER   B OG  1 
ATOM   4981 N  N   . SER   B 1 283 ? 23.64   -4.21   -12.549 1 44.98 ? 268 SER   B N   1 
ATOM   4982 C  CA  . SER   B 1 283 ? 22.839  -5.188  -11.837 1 45.97 ? 268 SER   B CA  1 
ATOM   4983 C  C   . SER   B 1 283 ? 21.859  -4.538  -10.866 1 46.97 ? 268 SER   B C   1 
ATOM   4984 O  O   . SER   B 1 283 ? 20.837  -5.149  -10.559 1 47.15 ? 268 SER   B O   1 
ATOM   4985 C  CB  . SER   B 1 283 ? 23.738  -6.153  -11.081 1 47.33 ? 268 SER   B CB  1 
ATOM   4986 O  OG  . SER   B 1 283 ? 24.501  -6.944  -11.979 1 49.8  ? 268 SER   B OG  1 
ATOM   4987 N  N   . VAL   B 1 284 ? 22.151  -3.316  -10.383 1 47.36 ? 269 VAL   B N   1 
ATOM   4988 C  CA  . VAL   B 1 284 ? 21.315  -2.686  -9.377  1 48.12 ? 269 VAL   B CA  1 
ATOM   4989 C  C   . VAL   B 1 284 ? 19.957  -2.271  -9.943  1 47.84 ? 269 VAL   B C   1 
ATOM   4990 O  O   . VAL   B 1 284 ? 18.952  -2.475  -9.267  1 47.95 ? 269 VAL   B O   1 
ATOM   4991 C  CB  . VAL   B 1 284 ? 22.023  -1.554  -8.589  1 49.26 ? 269 VAL   B CB  1 
ATOM   4992 C  CG1 . VAL   B 1 284 ? 21.95   -0.207  -9.307  1 49.43 ? 269 VAL   B CG1 1 
ATOM   4993 C  CG2 . VAL   B 1 284 ? 21.455  -1.448  -7.175  1 50.32 ? 269 VAL   B CG2 1 
ATOM   4994 N  N   . PHE   B 1 285 ? 19.904  -1.805  -11.186 1 47.41 ? 270 PHE   B N   1 
ATOM   4995 C  CA  . PHE   B 1 285 ? 18.637  -1.424  -11.787 1 47.9  ? 270 PHE   B CA  1 
ATOM   4996 C  C   . PHE   B 1 285 ? 17.82   -2.619  -12.21  1 47.2  ? 270 PHE   B C   1 
ATOM   4997 O  O   . PHE   B 1 285 ? 16.597  -2.608  -12.064 1 47.74 ? 270 PHE   B O   1 
ATOM   4998 C  CB  . PHE   B 1 285 ? 18.857  -0.458  -12.929 1 48.95 ? 270 PHE   B CB  1 
ATOM   4999 C  CG  . PHE   B 1 285 ? 19.035  0.931   -12.388 1 50.81 ? 270 PHE   B CG  1 
ATOM   5000 C  CD1 . PHE   B 1 285 ? 20.288  1.387   -12.003 1 52.08 ? 270 PHE   B CD1 1 
ATOM   5001 C  CD2 . PHE   B 1 285 ? 17.944  1.779   -12.239 1 52.09 ? 270 PHE   B CD2 1 
ATOM   5002 C  CE1 . PHE   B 1 285 ? 20.444  2.657   -11.463 1 53.12 ? 270 PHE   B CE1 1 
ATOM   5003 C  CE2 . PHE   B 1 285 ? 18.104  3.06    -11.719 1 53.13 ? 270 PHE   B CE2 1 
ATOM   5004 C  CZ  . PHE   B 1 285 ? 19.348  3.485   -11.32  1 53.05 ? 270 PHE   B CZ  1 
ATOM   5005 N  N   . GLN   B 1 286 ? 18.492  -3.661  -12.717 1 46.2  ? 271 GLN   B N   1 
ATOM   5006 C  CA  . GLN   B 1 286 ? 17.837  -4.9    -13.103 1 45.57 ? 271 GLN   B CA  1 
ATOM   5007 C  C   . GLN   B 1 286 ? 17.284  -5.604  -11.863 1 45.63 ? 271 GLN   B C   1 
ATOM   5008 O  O   . GLN   B 1 286 ? 16.227  -6.202  -11.954 1 45.95 ? 271 GLN   B O   1 
ATOM   5009 C  CB  . GLN   B 1 286 ? 18.802  -5.84   -13.864 1 45.52 ? 271 GLN   B CB  1 
ATOM   5010 C  CG  . GLN   B 1 286 ? 19.223  -5.325  -15.23  1 46.39 ? 271 GLN   B CG  1 
ATOM   5011 C  CD  . GLN   B 1 286 ? 19.243  -6.394  -16.297 1 48.64 ? 271 GLN   B CD  1 
ATOM   5012 O  OE1 . GLN   B 1 286 ? 18.497  -7.371  -16.254 1 48.07 ? 271 GLN   B OE1 1 
ATOM   5013 N  NE2 . GLN   B 1 286 ? 20.085  -6.217  -17.308 1 49.56 ? 271 GLN   B NE2 1 
ATOM   5014 N  N   . CYS   B 1 287 ? 17.968  -5.519  -10.71  1 45.46 ? 272 CYS   B N   1 
ATOM   5015 C  CA  . CYS   B 1 287 ? 17.51   -6.213  -9.507  1 46.18 ? 272 CYS   B CA  1 
ATOM   5016 C  C   . CYS   B 1 287 ? 16.249  -5.572  -8.9    1 45.42 ? 272 CYS   B C   1 
ATOM   5017 O  O   . CYS   B 1 287 ? 15.457  -6.3    -8.333  1 45.51 ? 272 CYS   B O   1 
ATOM   5018 C  CB  . CYS   B 1 287 ? 18.633  -6.413  -8.484  1 48.58 ? 272 CYS   B CB  1 
ATOM   5019 S  SG  . CYS   B 1 287 ? 18.722  -5.159  -7.183  1 58.83 ? 272 CYS   B SG  1 
ATOM   5020 N  N   . PHE   B 1 288 ? 16.018  -4.263  -9.097  1 44.82 ? 273 PHE   B N   1 
ATOM   5021 C  CA  . PHE   B 1 288 ? 14.783  -3.636  -8.62   1 45.15 ? 273 PHE   B CA  1 
ATOM   5022 C  C   . PHE   B 1 288 ? 13.617  -3.91   -9.574  1 43.29 ? 273 PHE   B C   1 
ATOM   5023 O  O   . PHE   B 1 288 ? 12.493  -4.07   -9.119  1 43.2  ? 273 PHE   B O   1 
ATOM   5024 C  CB  . PHE   B 1 288 ? 14.963  -2.148  -8.282  1 46.31 ? 273 PHE   B CB  1 
ATOM   5025 C  CG  . PHE   B 1 288 ? 15.709  -2.083  -6.972  1 48.66 ? 273 PHE   B CG  1 
ATOM   5026 C  CD1 . PHE   B 1 288 ? 15.177  -2.655  -5.825  1 50.19 ? 273 PHE   B CD1 1 
ATOM   5027 C  CD2 . PHE   B 1 288 ? 16.986  -1.554  -6.909  1 50.08 ? 273 PHE   B CD2 1 
ATOM   5028 C  CE1 . PHE   B 1 288 ? 15.895  -2.666  -4.632  1 51.53 ? 273 PHE   B CE1 1 
ATOM   5029 C  CE2 . PHE   B 1 288 ? 17.708  -1.579  -5.721  1 51.24 ? 273 PHE   B CE2 1 
ATOM   5030 C  CZ  . PHE   B 1 288 ? 17.169  -2.158  -4.596  1 51.43 ? 273 PHE   B CZ  1 
ATOM   5031 N  N   . ASP   B 1 289 ? 13.89   -4.057  -10.873 1 41.8  ? 274 ASP   B N   1 
ATOM   5032 C  CA  . ASP   B 1 289 ? 12.871  -4.445  -11.836 1 41.07 ? 274 ASP   B CA  1 
ATOM   5033 C  C   . ASP   B 1 289 ? 12.447  -5.883  -11.538 1 40.39 ? 274 ASP   B C   1 
ATOM   5034 O  O   . ASP   B 1 289 ? 11.257  -6.166  -11.521 1 39.89 ? 274 ASP   B O   1 
ATOM   5035 C  CB  . ASP   B 1 289 ? 13.406  -4.336  -13.266 1 42.83 ? 274 ASP   B CB  1 
ATOM   5036 C  CG  . ASP   B 1 289 ? 13.479  -2.903  -13.762 1 47.92 ? 274 ASP   B CG  1 
ATOM   5037 O  OD1 . ASP   B 1 289 ? 12.622  -2.09   -13.35  1 48.97 ? 274 ASP   B OD1 1 
ATOM   5038 O  OD2 . ASP   B 1 289 ? 14.395  -2.595  -14.569 1 49.39 ? 274 ASP   B OD2 1 
ATOM   5039 N  N   . VAL   B 1 290 ? 13.411  -6.783  -11.243 1 40.36 ? 275 VAL   B N   1 
ATOM   5040 C  CA  . VAL   B 1 290 ? 13.077  -8.161  -10.892 1 40.77 ? 275 VAL   B CA  1 
ATOM   5041 C  C   . VAL   B 1 290 ? 12.3    -8.19   -9.552  1 42.63 ? 275 VAL   B C   1 
ATOM   5042 O  O   . VAL   B 1 290 ? 11.221  -8.784  -9.473  1 43.05 ? 275 VAL   B O   1 
ATOM   5043 C  CB  . VAL   B 1 290 ? 14.322  -9.068  -10.854 1 40.72 ? 275 VAL   B CB  1 
ATOM   5044 C  CG1 . VAL   B 1 290 ? 13.98   -10.429 -10.262 1 41.08 ? 275 VAL   B CG1 1 
ATOM   5045 C  CG2 . VAL   B 1 290 ? 14.935  -9.226  -12.244 1 40.56 ? 275 VAL   B CG2 1 
ATOM   5046 N  N   . LEU   B 1 291 ? 12.816  -7.507  -8.523  1 43.33 ? 276 LEU   B N   1 
ATOM   5047 C  CA  . LEU   B 1 291 ? 12.172  -7.44   -7.211  1 44.28 ? 276 LEU   B CA  1 
ATOM   5048 C  C   . LEU   B 1 291 ? 10.705  -6.986  -7.284  1 45.05 ? 276 LEU   B C   1 
ATOM   5049 O  O   . LEU   B 1 291 ? 9.833   -7.61   -6.682  1 45.95 ? 276 LEU   B O   1 
ATOM   5050 C  CB  . LEU   B 1 291 ? 12.969  -6.501  -6.282  1 44.41 ? 276 LEU   B CB  1 
ATOM   5051 C  CG  . LEU   B 1 291 ? 12.375  -6.276  -4.89   1 46.39 ? 276 LEU   B CG  1 
ATOM   5052 C  CD1 . LEU   B 1 291 ? 12.511  -7.522  -4.021  1 46.7  ? 276 LEU   B CD1 1 
ATOM   5053 C  CD2 . LEU   B 1 291 ? 13.024  -5.099  -4.22   1 47.2  ? 276 LEU   B CD2 1 
ATOM   5054 N  N   . LEU   B 1 292 ? 10.432  -5.928  -8.04   1 44.53 ? 277 LEU   B N   1 
ATOM   5055 C  CA  . LEU   B 1 292 ? 9.089   -5.377  -8.147  1 44.53 ? 277 LEU   B CA  1 
ATOM   5056 C  C   . LEU   B 1 292 ? 8.199   -6.031  -9.214  1 45.19 ? 277 LEU   B C   1 
ATOM   5057 O  O   . LEU   B 1 292 ? 7.057   -5.595  -9.416  1 45.48 ? 277 LEU   B O   1 
ATOM   5058 C  CB  . LEU   B 1 292 ? 9.183   -3.862  -8.363  1 44.28 ? 277 LEU   B CB  1 
ATOM   5059 C  CG  . LEU   B 1 292 ? 9.934   -3.114  -7.247  1 44.87 ? 277 LEU   B CG  1 
ATOM   5060 C  CD1 . LEU   B 1 292 ? 10.198  -1.681  -7.632  1 44.86 ? 277 LEU   B CD1 1 
ATOM   5061 C  CD2 . LEU   B 1 292 ? 9.177   -3.199  -5.92   1 45.49 ? 277 LEU   B CD2 1 
ATOM   5062 N  N   . GLY   B 1 293 ? 8.701   -7.072  -9.876  1 44.83 ? 278 GLY   B N   1 
ATOM   5063 C  CA  . GLY   B 1 293 ? 7.929   -7.783  -10.884 1 44.97 ? 278 GLY   B CA  1 
ATOM   5064 C  C   . GLY   B 1 293 ? 7.673   -6.997  -12.145 1 45.46 ? 278 GLY   B C   1 
ATOM   5065 O  O   . GLY   B 1 293 ? 6.661   -7.207  -12.809 1 45.69 ? 278 GLY   B O   1 
ATOM   5066 N  N   . ILE   B 1 294 ? 8.569   -6.061  -12.469 1 45.73 ? 279 ILE   B N   1 
ATOM   5067 C  CA  . ILE   B 1 294 ? 8.488   -5.269  -13.677 1 46.59 ? 279 ILE   B CA  1 
ATOM   5068 C  C   . ILE   B 1 294 ? 9.193   -6.178  -14.677 1 49.03 ? 279 ILE   B C   1 
ATOM   5069 O  O   . ILE   B 1 294 ? 10.419  -6.311  -14.627 1 50.25 ? 279 ILE   B O   1 
ATOM   5070 C  CB  . ILE   B 1 294 ? 9.245   -3.939  -13.461 1 46.18 ? 279 ILE   B CB  1 
ATOM   5071 C  CG1 . ILE   B 1 294 ? 8.623   -3.139  -12.317 1 46.29 ? 279 ILE   B CG1 1 
ATOM   5072 C  CG2 . ILE   B 1 294 ? 9.288   -3.126  -14.739 1 46.57 ? 279 ILE   B CG2 1 
ATOM   5073 C  CD1 . ILE   B 1 294 ? 9.48    -2.134  -11.761 1 47.14 ? 279 ILE   B CD1 1 
ATOM   5074 N  N   . GLN   B 1 295 ? 8.435   -6.879  -15.51  1 49.83 ? 280 GLN   B N   1 
ATOM   5075 C  CA  . GLN   B 1 295 ? 9.01    -7.861  -16.427 1 51.28 ? 280 GLN   B CA  1 
ATOM   5076 C  C   . GLN   B 1 295 ? 9.671   -7.214  -17.633 1 51.5  ? 280 GLN   B C   1 
ATOM   5077 O  O   . GLN   B 1 295 ? 9.116   -7.223  -18.742 1 51.84 ? 280 GLN   B O   1 
ATOM   5078 C  CB  . GLN   B 1 295 ? 7.96    -8.887  -16.85  1 54.26 ? 280 GLN   B CB  1 
ATOM   5079 C  CG  . GLN   B 1 295 ? 7.221   -9.526  -15.68  1 60.62 ? 280 GLN   B CG  1 
ATOM   5080 C  CD  . GLN   B 1 295 ? 6.177   -10.514 -16.167 1 68.87 ? 280 GLN   B CD  1 
ATOM   5081 O  OE1 . GLN   B 1 295 ? 6.187   -11.696 -15.799 1 71.83 ? 280 GLN   B OE1 1 
ATOM   5082 N  NE2 . GLN   B 1 295 ? 5.262   -10.065 -17.025 1 69.92 ? 280 GLN   B NE2 1 
ATOM   5083 N  N   . GLN   B 1 296 ? 10.862  -6.64   -17.406 1 50.54 ? 281 GLN   B N   1 
ATOM   5084 C  CA  . GLN   B 1 296 ? 11.624  -5.966  -18.442 1 50.31 ? 281 GLN   B CA  1 
ATOM   5085 C  C   . GLN   B 1 296 ? 12.1    -6.922  -19.525 1 51.2  ? 281 GLN   B C   1 
ATOM   5086 O  O   . GLN   B 1 296 ? 12.185  -6.532  -20.687 1 50.85 ? 281 GLN   B O   1 
ATOM   5087 C  CB  . GLN   B 1 296 ? 12.829  -5.226  -17.833 1 49.84 ? 281 GLN   B CB  1 
ATOM   5088 C  CG  . GLN   B 1 296 ? 12.456  -4.069  -16.919 1 49.89 ? 281 GLN   B CG  1 
ATOM   5089 C  CD  . GLN   B 1 296 ? 11.898  -2.858  -17.631 1 52.18 ? 281 GLN   B CD  1 
ATOM   5090 O  OE1 . GLN   B 1 296 ? 11.746  -2.821  -18.854 1 53.13 ? 281 GLN   B OE1 1 
ATOM   5091 N  NE2 . GLN   B 1 296 ? 11.58   -1.826  -16.872 1 53.13 ? 281 GLN   B NE2 1 
ATOM   5092 N  N   . THR   B 1 297 ? 12.404  -8.172  -19.137 1 51.91 ? 282 THR   B N   1 
ATOM   5093 C  CA  . THR   B 1 297 ? 12.921  -9.221  -20.01  1 53.08 ? 282 THR   B CA  1 
ATOM   5094 C  C   . THR   B 1 297 ? 11.831  -10.103 -20.662 1 54.51 ? 282 THR   B C   1 
ATOM   5095 O  O   . THR   B 1 297 ? 12.156  -11.117 -21.276 1 55.59 ? 282 THR   B O   1 
ATOM   5096 C  CB  . THR   B 1 297 ? 13.928  -10.045 -19.215 1 54.21 ? 282 THR   B CB  1 
ATOM   5097 O  OG1 . THR   B 1 297 ? 13.277  -10.549 -18.031 1 55.61 ? 282 THR   B OG1 1 
ATOM   5098 C  CG2 . THR   B 1 297 ? 15.182  -9.218  -18.823 1 53.82 ? 282 THR   B CG2 1 
ATOM   5099 N  N   . ALA   B 1 298 ? 10.557  -9.698  -20.575 1 54.43 ? 283 ALA   B N   1 
ATOM   5100 C  CA  . ALA   B 1 298 ? 9.436   -10.447 -21.129 1 55.06 ? 283 ALA   B CA  1 
ATOM   5101 C  C   . ALA   B 1 298 ? 8.814   -9.775  -22.364 1 55.31 ? 283 ALA   B C   1 
ATOM   5102 O  O   . ALA   B 1 298 ? 8.993   -8.568  -22.572 1 54.84 ? 283 ALA   B O   1 
ATOM   5103 C  CB  . ALA   B 1 298 ? 8.367   -10.622 -20.047 1 55.31 ? 283 ALA   B CB  1 
ATOM   5104 N  N   . GLY   B 1 299 ? 8.091   -10.566 -23.169 1 55.54 ? 284 GLY   B N   1 
ATOM   5105 C  CA  . GLY   B 1 299 ? 7.331   -10.063 -24.309 1 56.19 ? 284 GLY   B CA  1 
ATOM   5106 C  C   . GLY   B 1 299 ? 7.943   -10.183 -25.689 1 56.65 ? 284 GLY   B C   1 
ATOM   5107 O  O   . GLY   B 1 299 ? 7.282   -9.835  -26.68  1 56.89 ? 284 GLY   B O   1 
ATOM   5108 N  N   . GLY   B 1 300 ? 9.217   -10.597 -25.742 1 56.14 ? 285 GLY   B N   1 
ATOM   5109 C  CA  . GLY   B 1 300 ? 9.958   -10.789 -26.987 1 56.09 ? 285 GLY   B CA  1 
ATOM   5110 C  C   . GLY   B 1 300 ? 10.334  -9.539  -27.763 1 55.56 ? 285 GLY   B C   1 
ATOM   5111 O  O   . GLY   B 1 300 ? 10.806  -9.636  -28.898 1 55.73 ? 285 GLY   B O   1 
ATOM   5112 N  N   . GLY   B 1 301 ? 10.147  -8.37   -27.159 1 54.66 ? 286 GLY   B N   1 
ATOM   5113 C  CA  . GLY   B 1 301 ? 10.5    -7.11   -27.799 1 54.06 ? 286 GLY   B CA  1 
ATOM   5114 C  C   . GLY   B 1 301 ? 11.994  -6.845  -27.815 1 53.1  ? 286 GLY   B C   1 
ATOM   5115 O  O   . GLY   B 1 301 ? 12.782  -7.598  -27.227 1 53.12 ? 286 GLY   B O   1 
ATOM   5116 N  N   . HIS   B 1 302 ? 12.398  -5.759  -28.48  1 52.11 ? 287 HIS   B N   1 
ATOM   5117 C  CA  . HIS   B 1 302 ? 13.817  -5.408  -28.593 1 51.58 ? 287 HIS   B CA  1 
ATOM   5118 C  C   . HIS   B 1 302 ? 14.472  -4.992  -27.256 1 49.34 ? 287 HIS   B C   1 
ATOM   5119 O  O   . HIS   B 1 302 ? 15.61   -5.374  -27.005 1 49.33 ? 287 HIS   B O   1 
ATOM   5120 C  CB  . HIS   B 1 302 ? 14.028  -4.352  -29.681 1 53.73 ? 287 HIS   B CB  1 
ATOM   5121 C  CG  . HIS   B 1 302 ? 13.807  -4.901  -31.057 1 58.82 ? 287 HIS   B CG  1 
ATOM   5122 N  ND1 . HIS   B 1 302 ? 12.549  -4.894  -31.644 1 61.54 ? 287 HIS   B ND1 1 
ATOM   5123 C  CD2 . HIS   B 1 302 ? 14.674  -5.521  -31.896 1 60.69 ? 287 HIS   B CD2 1 
ATOM   5124 C  CE1 . HIS   B 1 302 ? 12.697  -5.483  -32.823 1 62.2  ? 287 HIS   B CE1 1 
ATOM   5125 N  NE2 . HIS   B 1 302 ? 13.957  -5.876  -33.022 1 62    ? 287 HIS   B NE2 1 
ATOM   5126 N  N   . ALA   B 1 303 ? 13.75   -4.259  -26.39  1 47.48 ? 288 ALA   B N   1 
ATOM   5127 C  CA  . ALA   B 1 303 ? 14.269  -3.827  -25.092 1 46.25 ? 288 ALA   B CA  1 
ATOM   5128 C  C   . ALA   B 1 303 ? 14.517  -5.02   -24.167 1 45.22 ? 288 ALA   B C   1 
ATOM   5129 O  O   . ALA   B 1 303 ? 15.542  -5.067  -23.48  1 44.85 ? 288 ALA   B O   1 
ATOM   5130 C  CB  . ALA   B 1 303 ? 13.297  -2.851  -24.439 1 45.98 ? 288 ALA   B CB  1 
ATOM   5131 N  N   . ALA   B 1 304 ? 13.575  -5.988  -24.168 1 44.54 ? 289 ALA   B N   1 
ATOM   5132 C  CA  . ALA   B 1 304 ? 13.631  -7.223  -23.387 1 43.78 ? 289 ALA   B CA  1 
ATOM   5133 C  C   . ALA   B 1 304 ? 14.834  -8.047  -23.809 1 43.41 ? 289 ALA   B C   1 
ATOM   5134 O  O   . ALA   B 1 304 ? 15.583  -8.509  -22.947 1 43.76 ? 289 ALA   B O   1 
ATOM   5135 C  CB  . ALA   B 1 304 ? 12.339  -8.024  -23.582 1 43.79 ? 289 ALA   B CB  1 
ATOM   5136 N  N   . GLN   B 1 305 ? 15.058  -8.181  -25.144 1 42.57 ? 290 GLN   B N   1 
ATOM   5137 C  CA  . GLN   B 1 305 ? 16.179  -8.926  -25.694 1 42.5  ? 290 GLN   B CA  1 
ATOM   5138 C  C   . GLN   B 1 305 ? 17.491  -8.296  -25.246 1 41.87 ? 290 GLN   B C   1 
ATOM   5139 O  O   . GLN   B 1 305 ? 18.367  -8.997  -24.737 1 42.04 ? 290 GLN   B O   1 
ATOM   5140 C  CB  . GLN   B 1 305 ? 16.103  -8.956  -27.238 1 44.41 ? 290 GLN   B CB  1 
ATOM   5141 C  CG  . GLN   B 1 305 ? 17.176  -9.848  -27.861 1 47.91 ? 290 GLN   B CG  1 
ATOM   5142 C  CD  . GLN   B 1 305 ? 16.871  -11.29  -27.542 1 53.14 ? 290 GLN   B CD  1 
ATOM   5143 O  OE1 . GLN   B 1 305 ? 15.796  -11.791 -27.867 1 56.18 ? 290 GLN   B OE1 1 
ATOM   5144 N  NE2 . GLN   B 1 305 ? 17.788  -11.986 -26.875 1 53.91 ? 290 GLN   B NE2 1 
ATOM   5145 N  N   . PHE   B 1 306 ? 17.599  -6.961  -25.371 1 40.8  ? 291 PHE   B N   1 
ATOM   5146 C  CA  . PHE   B 1 306 ? 18.806  -6.246  -24.994 1 40.3  ? 291 PHE   B CA  1 
ATOM   5147 C  C   . PHE   B 1 306 ? 19.162  -6.434  -23.525 1 39.97 ? 291 PHE   B C   1 
ATOM   5148 O  O   . PHE   B 1 306 ? 20.286  -6.804  -23.226 1 40.19 ? 291 PHE   B O   1 
ATOM   5149 C  CB  . PHE   B 1 306 ? 18.693  -4.749  -25.365 1 40.17 ? 291 PHE   B CB  1 
ATOM   5150 C  CG  . PHE   B 1 306 ? 19.966  -3.99   -25.056 1 40.75 ? 291 PHE   B CG  1 
ATOM   5151 C  CD1 . PHE   B 1 306 ? 21.108  -4.178  -25.821 1 41.2  ? 291 PHE   B CD1 1 
ATOM   5152 C  CD2 . PHE   B 1 306 ? 20.037  -3.129  -23.967 1 41.16 ? 291 PHE   B CD2 1 
ATOM   5153 C  CE1 . PHE   B 1 306 ? 22.282  -3.491  -25.524 1 41.44 ? 291 PHE   B CE1 1 
ATOM   5154 C  CE2 . PHE   B 1 306 ? 21.214  -2.45   -23.672 1 41.35 ? 291 PHE   B CE2 1 
ATOM   5155 C  CZ  . PHE   B 1 306 ? 22.328  -2.639  -24.454 1 40.95 ? 291 PHE   B CZ  1 
ATOM   5156 N  N   . LEU   B 1 307 ? 18.202  -6.218  -22.611 1 39.77 ? 292 LEU   B N   1 
ATOM   5157 C  CA  . LEU   B 1 307 ? 18.447  -6.357  -21.173 1 39.87 ? 292 LEU   B CA  1 
ATOM   5158 C  C   . LEU   B 1 307 ? 18.777  -7.786  -20.752 1 40.73 ? 292 LEU   B C   1 
ATOM   5159 O  O   . LEU   B 1 307 ? 19.626  -7.989  -19.879 1 40.49 ? 292 LEU   B O   1 
ATOM   5160 C  CB  . LEU   B 1 307 ? 17.283  -5.784  -20.368 1 39.19 ? 292 LEU   B CB  1 
ATOM   5161 C  CG  . LEU   B 1 307 ? 17.17   -4.252  -20.435 1 39.35 ? 292 LEU   B CG  1 
ATOM   5162 C  CD1 . LEU   B 1 307 ? 15.871  -3.762  -19.821 1 39    ? 292 LEU   B CD1 1 
ATOM   5163 C  CD2 . LEU   B 1 307 ? 18.367  -3.588  -19.783 1 39.19 ? 292 LEU   B CD2 1 
ATOM   5164 N  N   . GLN   B 1 308 ? 18.158  -8.775  -21.406 1 41.75 ? 293 GLN   B N   1 
ATOM   5165 C  CA  . GLN   B 1 308 ? 18.471  -10.175 -21.116 1 43.28 ? 293 GLN   B CA  1 
ATOM   5166 C  C   . GLN   B 1 308 ? 19.91   -10.459 -21.571 1 44.24 ? 293 GLN   B C   1 
ATOM   5167 O  O   . GLN   B 1 308 ? 20.713  -10.97  -20.788 1 44.69 ? 293 GLN   B O   1 
ATOM   5168 C  CB  . GLN   B 1 308 ? 17.481  -11.121 -21.821 1 45.81 ? 293 GLN   B CB  1 
ATOM   5169 C  CG  . GLN   B 1 308 ? 17.752  -12.6   -21.517 1 50.57 ? 293 GLN   B CG  1 
ATOM   5170 C  CD  . GLN   B 1 308 ? 17.542  -12.933 -20.058 1 58.05 ? 293 GLN   B CD  1 
ATOM   5171 O  OE1 . GLN   B 1 308 ? 18.378  -13.572 -19.4   1 60.42 ? 293 GLN   B OE1 1 
ATOM   5172 N  NE2 . GLN   B 1 308 ? 16.413  -12.506 -19.51  1 60.11 ? 293 GLN   B NE2 1 
ATOM   5173 N  N   . ASP   B 1 309 ? 20.259  -10.044 -22.808 1 44.32 ? 294 ASP   B N   1 
ATOM   5174 C  CA  . ASP   B 1 309 ? 21.608  -10.25  -23.352 1 44.84 ? 294 ASP   B CA  1 
ATOM   5175 C  C   . ASP   B 1 309 ? 22.673  -9.589  -22.496 1 44.4  ? 294 ASP   B C   1 
ATOM   5176 O  O   . ASP   B 1 309 ? 23.769  -10.139 -22.344 1 44.85 ? 294 ASP   B O   1 
ATOM   5177 C  CB  . ASP   B 1 309 ? 21.714  -9.735  -24.804 1 46.87 ? 294 ASP   B CB  1 
ATOM   5178 C  CG  . ASP   B 1 309 ? 20.932  -10.539 -25.827 1 51.74 ? 294 ASP   B CG  1 
ATOM   5179 O  OD1 . ASP   B 1 309 ? 20.49   -11.668 -25.491 1 52.61 ? 294 ASP   B OD1 1 
ATOM   5180 O  OD2 . ASP   B 1 309 ? 20.75   -10.037 -26.967 1 54.25 ? 294 ASP   B OD2 1 
ATOM   5181 N  N   . MET   B 1 310 ? 22.361  -8.417  -21.924 1 43.44 ? 295 MET   B N   1 
ATOM   5182 C  CA  . MET   B 1 310 ? 23.316  -7.698  -21.078 1 42.69 ? 295 MET   B CA  1 
ATOM   5183 C  C   . MET   B 1 310 ? 23.642  -8.391  -19.775 1 42.14 ? 295 MET   B C   1 
ATOM   5184 O  O   . MET   B 1 310 ? 24.621  -8.018  -19.154 1 42.31 ? 295 MET   B O   1 
ATOM   5185 C  CB  . MET   B 1 310 ? 22.88   -6.256  -20.829 1 42.99 ? 295 MET   B CB  1 
ATOM   5186 C  CG  . MET   B 1 310 ? 22.911  -5.397  -22.08  1 44.69 ? 295 MET   B CG  1 
ATOM   5187 S  SD  . MET   B 1 310 ? 24.506  -5.361  -22.932 1 47.11 ? 295 MET   B SD  1 
ATOM   5188 C  CE  . MET   B 1 310 ? 24.163  -6.471  -24.361 1 42.05 ? 295 MET   B CE  1 
ATOM   5189 N  N   . ARG   B 1 311 ? 22.899  -9.433  -19.394 1 42.35 ? 296 ARG   B N   1 
ATOM   5190 C  CA  . ARG   B 1 311 ? 23.21   -10.2   -18.186 1 43.37 ? 296 ARG   B CA  1 
ATOM   5191 C  C   . ARG   B 1 311 ? 24.467  -11.045 -18.329 1 43.97 ? 296 ARG   B C   1 
ATOM   5192 O  O   . ARG   B 1 311 ? 25.163  -11.284 -17.343 1 44.02 ? 296 ARG   B O   1 
ATOM   5193 C  CB  . ARG   B 1 311 ? 22.036  -11.066 -17.771 1 44.33 ? 296 ARG   B CB  1 
ATOM   5194 C  CG  . ARG   B 1 311 ? 20.827  -10.229 -17.465 1 46.71 ? 296 ARG   B CG  1 
ATOM   5195 C  CD  . ARG   B 1 311 ? 19.837  -11.039 -16.687 1 48.77 ? 296 ARG   B CD  1 
ATOM   5196 N  NE  . ARG   B 1 311 ? 18.688  -10.238 -16.289 1 50.61 ? 296 ARG   B NE  1 
ATOM   5197 C  CZ  . ARG   B 1 311 ? 17.63   -10.714 -15.642 1 51.93 ? 296 ARG   B CZ  1 
ATOM   5198 N  NH1 . ARG   B 1 311 ? 17.574  -11.999 -15.299 1 50.35 ? 296 ARG   B NH1 1 
ATOM   5199 N  NH2 . ARG   B 1 311 ? 16.622  -9.91   -15.329 1 52.1  ? 296 ARG   B NH2 1 
ATOM   5200 N  N   . ARG   B 1 312 ? 24.772  -11.481 -19.561 1 44.32 ? 297 ARG   B N   1 
ATOM   5201 C  CA  . ARG   B 1 312 ? 25.996  -12.223 -19.826 1 45.39 ? 297 ARG   B CA  1 
ATOM   5202 C  C   . ARG   B 1 312 ? 27.247  -11.322 -19.839 1 45.09 ? 297 ARG   B C   1 
ATOM   5203 O  O   . ARG   B 1 312 ? 28.365  -11.832 -19.88  1 45.48 ? 297 ARG   B O   1 
ATOM   5204 C  CB  . ARG   B 1 312 ? 25.867  -13.034 -21.123 1 48.37 ? 297 ARG   B CB  1 
ATOM   5205 N  N   . TYR   B 1 313 ? 27.065  -9.987  -19.785 1 44.74 ? 298 TYR   B N   1 
ATOM   5206 C  CA  . TYR   B 1 313 ? 28.138  -8.996  -19.688 1 44.47 ? 298 TYR   B CA  1 
ATOM   5207 C  C   . TYR   B 1 313 ? 28.34   -8.536  -18.225 1 44.26 ? 298 TYR   B C   1 
ATOM   5208 O  O   . TYR   B 1 313 ? 29.147  -7.638  -17.979 1 45.02 ? 298 TYR   B O   1 
ATOM   5209 C  CB  . TYR   B 1 313 ? 27.842  -7.791  -20.586 1 44.81 ? 298 TYR   B CB  1 
ATOM   5210 C  CG  . TYR   B 1 313 ? 27.86   -8.084  -22.075 1 46    ? 298 TYR   B CG  1 
ATOM   5211 C  CD1 . TYR   B 1 313 ? 26.877  -8.863  -22.662 1 46.99 ? 298 TYR   B CD1 1 
ATOM   5212 C  CD2 . TYR   B 1 313 ? 28.817  -7.517  -22.905 1 46.87 ? 298 TYR   B CD2 1 
ATOM   5213 C  CE1 . TYR   B 1 313 ? 26.888  -9.131  -24.026 1 48.04 ? 298 TYR   B CE1 1 
ATOM   5214 C  CE2 . TYR   B 1 313 ? 28.833  -7.768  -24.271 1 47.54 ? 298 TYR   B CE2 1 
ATOM   5215 C  CZ  . TYR   B 1 313 ? 27.869  -8.58   -24.829 1 48.99 ? 298 TYR   B CZ  1 
ATOM   5216 O  OH  . TYR   B 1 313 ? 27.861  -8.825  -26.187 1 51.06 ? 298 TYR   B OH  1 
ATOM   5217 N  N   . MET   B 1 314 ? 27.621  -9.153  -17.255 1 43.58 ? 299 MET   B N   1 
ATOM   5218 C  CA  . MET   B 1 314 ? 27.701  -8.876  -15.818 1 43.32 ? 299 MET   B CA  1 
ATOM   5219 C  C   . MET   B 1 314 ? 28.623  -9.863  -15.145 1 43.27 ? 299 MET   B C   1 
ATOM   5220 O  O   . MET   B 1 314 ? 28.666  -11.012 -15.574 1 43.57 ? 299 MET   B O   1 
ATOM   5221 C  CB  . MET   B 1 314 ? 26.322  -9.085  -15.175 1 43.28 ? 299 MET   B CB  1 
ATOM   5222 C  CG  . MET   B 1 314 ? 25.341  -8.045  -15.516 1 44.87 ? 299 MET   B CG  1 
ATOM   5223 S  SD  . MET   B 1 314 ? 23.806  -8.345  -14.623 1 43.53 ? 299 MET   B SD  1 
ATOM   5224 C  CE  . MET   B 1 314 ? 22.774  -7.22   -15.468 1 37.29 ? 299 MET   B CE  1 
ATOM   5225 N  N   . PRO   B 1 315 ? 29.264  -9.514  -14.005 1 43.04 ? 300 PRO   B N   1 
ATOM   5226 C  CA  . PRO   B 1 315 ? 30.068  -10.522 -13.283 1 43.48 ? 300 PRO   B CA  1 
ATOM   5227 C  C   . PRO   B 1 315 ? 29.208  -11.742 -12.915 1 44.82 ? 300 PRO   B C   1 
ATOM   5228 O  O   . PRO   B 1 315 ? 28.024  -11.591 -12.618 1 45.73 ? 300 PRO   B O   1 
ATOM   5229 C  CB  . PRO   B 1 315 ? 30.571  -9.767  -12.05  1 44.14 ? 300 PRO   B CB  1 
ATOM   5230 C  CG  . PRO   B 1 315 ? 30.515  -8.297  -12.459 1 44.66 ? 300 PRO   B CG  1 
ATOM   5231 C  CD  . PRO   B 1 315 ? 29.291  -8.203  -13.328 1 42.58 ? 300 PRO   B CD  1 
ATOM   5232 N  N   . PRO   B 1 316 ? 29.746  -12.964 -13.058 1 44.98 ? 301 PRO   B N   1 
ATOM   5233 C  CA  . PRO   B 1 316 ? 28.939  -14.165 -12.81  1 45.11 ? 301 PRO   B CA  1 
ATOM   5234 C  C   . PRO   B 1 316 ? 28.19   -14.198 -11.482 1 45.66 ? 301 PRO   B C   1 
ATOM   5235 O  O   . PRO   B 1 316 ? 27.029  -14.59  -11.489 1 45.99 ? 301 PRO   B O   1 
ATOM   5236 C  CB  . PRO   B 1 316 ? 29.948  -15.311 -12.933 1 45.86 ? 301 PRO   B CB  1 
ATOM   5237 C  CG  . PRO   B 1 316 ? 31.302  -14.664 -12.819 1 46.02 ? 301 PRO   B CG  1 
ATOM   5238 C  CD  . PRO   B 1 316 ? 31.125  -13.316 -13.441 1 44.54 ? 301 PRO   B CD  1 
ATOM   5239 N  N   . ALA   B 1 317 ? 28.8    -13.738 -10.376 1 45.58 ? 302 ALA   B N   1 
ATOM   5240 C  CA  . ALA   B 1 317 ? 28.133  -13.696 -9.068  1 46.23 ? 302 ALA   B CA  1 
ATOM   5241 C  C   . ALA   B 1 317 ? 26.895  -12.779 -9.084  1 47.21 ? 302 ALA   B C   1 
ATOM   5242 O  O   . ALA   B 1 317 ? 25.898  -13.067 -8.416  1 47.3  ? 302 ALA   B O   1 
ATOM   5243 C  CB  . ALA   B 1 317 ? 29.104  -13.229 -7.998  1 45.9  ? 302 ALA   B CB  1 
ATOM   5244 N  N   . HIS   B 1 318 ? 26.959  -11.678 -9.862  1 47.25 ? 303 HIS   B N   1 
ATOM   5245 C  CA  . HIS   B 1 318 ? 25.851  -10.723 -9.977  1 46.96 ? 303 HIS   B CA  1 
ATOM   5246 C  C   . HIS   B 1 318 ? 24.743  -11.222 -10.881 1 46.79 ? 303 HIS   B C   1 
ATOM   5247 O  O   . HIS   B 1 318 ? 23.575  -10.966 -10.622 1 47.3  ? 303 HIS   B O   1 
ATOM   5248 C  CB  . HIS   B 1 318 ? 26.371  -9.359  -10.428 1 46.93 ? 303 HIS   B CB  1 
ATOM   5249 C  CG  . HIS   B 1 318 ? 27.364  -8.749  -9.49   1 48.73 ? 303 HIS   B CG  1 
ATOM   5250 N  ND1 . HIS   B 1 318 ? 28.125  -7.659  -9.87   1 50.93 ? 303 HIS   B ND1 1 
ATOM   5251 C  CD2 . HIS   B 1 318 ? 27.676  -9.075  -8.211  1 49.79 ? 303 HIS   B CD2 1 
ATOM   5252 C  CE1 . HIS   B 1 318 ? 28.876  -7.369  -8.82   1 51.5  ? 303 HIS   B CE1 1 
ATOM   5253 N  NE2 . HIS   B 1 318 ? 28.634  -8.193  -7.797  1 51.02 ? 303 HIS   B NE2 1 
ATOM   5254 N  N   . ARG   B 1 319 ? 25.108  -11.947 -11.926 1 46.46 ? 304 ARG   B N   1 
ATOM   5255 C  CA  . ARG   B 1 319 ? 24.194  -12.609 -12.849 1 46.98 ? 304 ARG   B CA  1 
ATOM   5256 C  C   . ARG   B 1 319 ? 23.413  -13.696 -12.059 1 47.27 ? 304 ARG   B C   1 
ATOM   5257 O  O   . ARG   B 1 319 ? 22.215  -13.858 -12.267 1 47.45 ? 304 ARG   B O   1 
ATOM   5258 C  CB  . ARG   B 1 319 ? 25.045  -13.257 -13.938 1 48.52 ? 304 ARG   B CB  1 
ATOM   5259 C  CG  . ARG   B 1 319 ? 24.317  -13.779 -15.153 1 52.36 ? 304 ARG   B CG  1 
ATOM   5260 C  CD  . ARG   B 1 319 ? 25.297  -14.498 -16.097 1 55.48 ? 304 ARG   B CD  1 
ATOM   5261 N  NE  . ARG   B 1 319 ? 26.538  -13.744 -16.299 1 57.66 ? 304 ARG   B NE  1 
ATOM   5262 C  CZ  . ARG   B 1 319 ? 27.704  -14.283 -16.647 1 58.75 ? 304 ARG   B CZ  1 
ATOM   5263 N  NH1 . ARG   B 1 319 ? 27.8    -15.586 -16.877 1 57.91 ? 304 ARG   B NH1 1 
ATOM   5264 N  NH2 . ARG   B 1 319 ? 28.783  -13.52  -16.769 1 57.77 ? 304 ARG   B NH2 1 
ATOM   5265 N  N   . ASN   B 1 320 ? 24.098  -14.408 -11.134 1 47.31 ? 305 ASN   B N   1 
ATOM   5266 C  CA  . ASN   B 1 320 ? 23.545  -15.434 -10.25  1 47.75 ? 305 ASN   B CA  1 
ATOM   5267 C  C   . ASN   B 1 320 ? 22.55   -14.807 -9.268  1 47.37 ? 305 ASN   B C   1 
ATOM   5268 O  O   . ASN   B 1 320 ? 21.522  -15.407 -8.956  1 47.51 ? 305 ASN   B O   1 
ATOM   5269 C  CB  . ASN   B 1 320 ? 24.672  -16.09  -9.422  1 49.33 ? 305 ASN   B CB  1 
ATOM   5270 C  CG  . ASN   B 1 320 ? 25.636  -16.939 -10.189 1 53.04 ? 305 ASN   B CG  1 
ATOM   5271 O  OD1 . ASN   B 1 320 ? 25.444  -17.226 -11.377 1 54.48 ? 305 ASN   B OD1 1 
ATOM   5272 N  ND2 . ASN   B 1 320 ? 26.706  -17.348 -9.512  1 53.87 ? 305 ASN   B ND2 1 
ATOM   5273 N  N   . PHE   B 1 321 ? 22.883  -13.63  -8.737  1 46.85 ? 306 PHE   B N   1 
ATOM   5274 C  CA  . PHE   B 1 321 ? 22.009  -12.929 -7.811  1 47.39 ? 306 PHE   B CA  1 
ATOM   5275 C  C   . PHE   B 1 321 ? 20.668  -12.584 -8.47   1 48.21 ? 306 PHE   B C   1 
ATOM   5276 O  O   . PHE   B 1 321 ? 19.629  -12.782 -7.844  1 47.82 ? 306 PHE   B O   1 
ATOM   5277 C  CB  . PHE   B 1 321 ? 22.681  -11.664 -7.292  1 46.93 ? 306 PHE   B CB  1 
ATOM   5278 C  CG  . PHE   B 1 321 ? 21.821  -10.903 -6.315  1 47.25 ? 306 PHE   B CG  1 
ATOM   5279 C  CD1 . PHE   B 1 321 ? 21.581  -11.402 -5.042  1 48.17 ? 306 PHE   B CD1 1 
ATOM   5280 C  CD2 . PHE   B 1 321 ? 21.219  -9.709  -6.679  1 47.43 ? 306 PHE   B CD2 1 
ATOM   5281 C  CE1 . PHE   B 1 321 ? 20.781  -10.696 -4.143  1 48.44 ? 306 PHE   B CE1 1 
ATOM   5282 C  CE2 . PHE   B 1 321 ? 20.426  -9.004  -5.776  1 47.86 ? 306 PHE   B CE2 1 
ATOM   5283 C  CZ  . PHE   B 1 321 ? 20.218  -9.498  -4.514  1 47.78 ? 306 PHE   B CZ  1 
ATOM   5284 N  N   . LEU   B 1 322 ? 20.698  -12.099 -9.739  1 48.64 ? 307 LEU   B N   1 
ATOM   5285 C  CA  . LEU   B 1 322 ? 19.491  -11.768 -10.487 1 49.33 ? 307 LEU   B CA  1 
ATOM   5286 C  C   . LEU   B 1 322 ? 18.608  -12.997 -10.681 1 50.15 ? 307 LEU   B C   1 
ATOM   5287 O  O   . LEU   B 1 322 ? 17.402  -12.903 -10.463 1 50.32 ? 307 LEU   B O   1 
ATOM   5288 C  CB  . LEU   B 1 322 ? 19.807  -11.109 -11.834 1 49.64 ? 307 LEU   B CB  1 
ATOM   5289 C  CG  . LEU   B 1 322 ? 20.436  -9.717  -11.781 1 51.44 ? 307 LEU   B CG  1 
ATOM   5290 C  CD1 . LEU   B 1 322 ? 20.595  -9.139  -13.172 1 51.84 ? 307 LEU   B CD1 1 
ATOM   5291 C  CD2 . LEU   B 1 322 ? 19.589  -8.766  -10.979 1 52.42 ? 307 LEU   B CD2 1 
ATOM   5292 N  N   . CYS   B 1 323 ? 19.202  -14.144 -11.046 1 50.29 ? 308 CYS   B N   1 
ATOM   5293 C  CA  . CYS   B 1 323 ? 18.525  -15.439 -11.206 1 51.62 ? 308 CYS   B CA  1 
ATOM   5294 C  C   . CYS   B 1 323 ? 17.803  -15.813 -9.897  1 52.04 ? 308 CYS   B C   1 
ATOM   5295 O  O   . CYS   B 1 323 ? 16.67   -16.271 -9.923  1 51.98 ? 308 CYS   B O   1 
ATOM   5296 C  CB  . CYS   B 1 323 ? 19.569  -16.499 -11.587 1 53.36 ? 308 CYS   B CB  1 
ATOM   5297 S  SG  . CYS   B 1 323 ? 19.153  -18.211 -11.12  1 58.76 ? 308 CYS   B SG  1 
ATOM   5298 N  N   . SER   B 1 324 ? 18.501  -15.676 -8.771  1 52.69 ? 309 SER   B N   1 
ATOM   5299 C  CA  . SER   B 1 324 ? 17.99   -16.009 -7.453  1 53.66 ? 309 SER   B CA  1 
ATOM   5300 C  C   . SER   B 1 324 ? 16.804  -15.132 -7.082  1 54.27 ? 309 SER   B C   1 
ATOM   5301 O  O   . SER   B 1 324 ? 15.856  -15.625 -6.468  1 55.33 ? 309 SER   B O   1 
ATOM   5302 C  CB  . SER   B 1 324 ? 19.09   -15.873 -6.409  1 55.54 ? 309 SER   B CB  1 
ATOM   5303 O  OG  . SER   B 1 324 ? 20.006  -16.949 -6.5    1 59.03 ? 309 SER   B OG  1 
ATOM   5304 N  N   . LEU   B 1 325 ? 16.838  -13.847 -7.46   1 53.27 ? 310 LEU   B N   1 
ATOM   5305 C  CA  . LEU   B 1 325 ? 15.725  -12.953 -7.198  1 53.26 ? 310 LEU   B CA  1 
ATOM   5306 C  C   . LEU   B 1 325 ? 14.511  -13.391 -8.001  1 53.58 ? 310 LEU   B C   1 
ATOM   5307 O  O   . LEU   B 1 325 ? 13.412  -13.392 -7.46   1 54.17 ? 310 LEU   B O   1 
ATOM   5308 C  CB  . LEU   B 1 325 ? 16.074  -11.505 -7.567  1 53.3  ? 310 LEU   B CB  1 
ATOM   5309 C  CG  . LEU   B 1 325 ? 16.899  -10.7   -6.599  1 54.34 ? 310 LEU   B CG  1 
ATOM   5310 C  CD1 . LEU   B 1 325 ? 17.009  -9.298  -7.092  1 54.62 ? 310 LEU   B CD1 1 
ATOM   5311 C  CD2 . LEU   B 1 325 ? 16.279  -10.69  -5.223  1 55.14 ? 310 LEU   B CD2 1 
ATOM   5312 N  N   . GLU   B 1 326 ? 14.707  -13.787 -9.276  1 53.49 ? 311 GLU   B N   1 
ATOM   5313 C  CA  . GLU   B 1 326 ? 13.633  -14.259 -10.156 1 54.26 ? 311 GLU   B CA  1 
ATOM   5314 C  C   . GLU   B 1 326 ? 12.992  -15.559 -9.653  1 54.8  ? 311 GLU   B C   1 
ATOM   5315 O  O   . GLU   B 1 326 ? 11.798  -15.783 -9.868  1 55.6  ? 311 GLU   B O   1 
ATOM   5316 C  CB  . GLU   B 1 326 ? 14.165  -14.482 -11.57  1 56.51 ? 311 GLU   B CB  1 
ATOM   5317 C  CG  . GLU   B 1 326 ? 13.911  -13.313 -12.5   1 61.63 ? 311 GLU   B CG  1 
ATOM   5318 C  CD  . GLU   B 1 326 ? 14.859  -13.206 -13.678 1 67.24 ? 311 GLU   B CD  1 
ATOM   5319 O  OE1 . GLU   B 1 326 ? 15.814  -14.014 -13.754 1 67.8  ? 311 GLU   B OE1 1 
ATOM   5320 O  OE2 . GLU   B 1 326 ? 14.642  -12.314 -14.53  1 70.42 ? 311 GLU   B OE2 1 
ATOM   5321 N  N   . SER   B 1 327 ? 13.797  -16.412 -9.007  1 54.4  ? 312 SER   B N   1 
ATOM   5322 C  CA  . SER   B 1 327 ? 13.405  -17.701 -8.44   1 54.65 ? 312 SER   B CA  1 
ATOM   5323 C  C   . SER   B 1 327 ? 12.545  -17.553 -7.157  1 54.28 ? 312 SER   B C   1 
ATOM   5324 O  O   . SER   B 1 327 ? 11.85   -18.491 -6.749  1 54.62 ? 312 SER   B O   1 
ATOM   5325 C  CB  . SER   B 1 327 ? 14.653  -18.57  -8.235  1 56.48 ? 312 SER   B CB  1 
ATOM   5326 O  OG  . SER   B 1 327 ? 14.81   -19.22  -6.984  1 59.28 ? 312 SER   B OG  1 
ATOM   5327 N  N   . ASN   B 1 328 ? 12.593  -16.372 -6.532  1 53.22 ? 313 ASN   B N   1 
ATOM   5328 C  CA  . ASN   B 1 328 ? 11.823  -16.062 -5.341  1 52.24 ? 313 ASN   B CA  1 
ATOM   5329 C  C   . ASN   B 1 328 ? 10.396  -15.637 -5.71   1 51.67 ? 313 ASN   B C   1 
ATOM   5330 O  O   . ASN   B 1 328 ? 10.138  -15.227 -6.851  1 52.24 ? 313 ASN   B O   1 
ATOM   5331 C  CB  . ASN   B 1 328 ? 12.535  -14.989 -4.538  1 52.52 ? 313 ASN   B CB  1 
ATOM   5332 C  CG  . ASN   B 1 328 ? 13.601  -15.552 -3.647  1 54.79 ? 313 ASN   B CG  1 
ATOM   5333 O  OD1 . ASN   B 1 328 ? 14.711  -15.871 -4.097  1 56.27 ? 313 ASN   B OD1 1 
ATOM   5334 N  ND2 . ASN   B 1 328 ? 13.287  -15.672 -2.362  1 54.41 ? 313 ASN   B ND2 1 
ATOM   5335 N  N   . PRO   B 1 329 ? 9.443   -15.757 -4.769  1 50.46 ? 314 PRO   B N   1 
ATOM   5336 C  CA  . PRO   B 1 329 ? 8.058   -15.388 -5.088  1 49.73 ? 314 PRO   B CA  1 
ATOM   5337 C  C   . PRO   B 1 329 ? 7.908   -13.93  -5.49   1 49.2  ? 314 PRO   B C   1 
ATOM   5338 O  O   . PRO   B 1 329 ? 8.704   -13.078 -5.099  1 49.9  ? 314 PRO   B O   1 
ATOM   5339 C  CB  . PRO   B 1 329 ? 7.298   -15.684 -3.788  1 50.6  ? 314 PRO   B CB  1 
ATOM   5340 C  CG  . PRO   B 1 329 ? 8.171   -16.603 -3.009  1 51.28 ? 314 PRO   B CG  1 
ATOM   5341 C  CD  . PRO   B 1 329 ? 9.574   -16.229 -3.375  1 49.97 ? 314 PRO   B CD  1 
ATOM   5342 N  N   . SER   B 1 330 ? 6.888   -13.644 -6.276  1 48.07 ? 315 SER   B N   1 
ATOM   5343 C  CA  . SER   B 1 330 ? 6.626   -12.296 -6.749  1 47.69 ? 315 SER   B CA  1 
ATOM   5344 C  C   . SER   B 1 330 ? 6.086   -11.364 -5.641  1 47.2  ? 315 SER   B C   1 
ATOM   5345 O  O   . SER   B 1 330 ? 5.035   -11.643 -5.05   1 47.26 ? 315 SER   B O   1 
ATOM   5346 C  CB  . SER   B 1 330 ? 5.657   -12.339 -7.927  1 48.39 ? 315 SER   B CB  1 
ATOM   5347 O  OG  . SER   B 1 330 ? 5.268   -11.049 -8.374  1 50.14 ? 315 SER   B OG  1 
ATOM   5348 N  N   . VAL   B 1 331 ? 6.808   -10.254 -5.384  1 45.94 ? 316 VAL   B N   1 
ATOM   5349 C  CA  . VAL   B 1 331 ? 6.406   -9.197  -4.461  1 45.16 ? 316 VAL   B CA  1 
ATOM   5350 C  C   . VAL   B 1 331 ? 5.145   -8.538  -5.029  1 44.97 ? 316 VAL   B C   1 
ATOM   5351 O  O   . VAL   B 1 331 ? 4.195   -8.299  -4.29   1 44.88 ? 316 VAL   B O   1 
ATOM   5352 C  CB  . VAL   B 1 331 ? 7.543   -8.161  -4.28   1 45.6  ? 316 VAL   B CB  1 
ATOM   5353 C  CG1 . VAL   B 1 331 ? 7.097   -6.993  -3.416  1 45.92 ? 316 VAL   B CG1 1 
ATOM   5354 C  CG2 . VAL   B 1 331 ? 8.778   -8.808  -3.691  1 46.17 ? 316 VAL   B CG2 1 
ATOM   5355 N  N   . ARG   B 1 332 ? 5.113   -8.29   -6.353  1 44.89 ? 317 ARG   B N   1 
ATOM   5356 C  CA  . ARG   B 1 332 ? 3.953   -7.709  -7.019  1 45.1  ? 317 ARG   B CA  1 
ATOM   5357 C  C   . ARG   B 1 332 ? 2.71    -8.575  -6.844  1 46.35 ? 317 ARG   B C   1 
ATOM   5358 O  O   . ARG   B 1 332 ? 1.668   -8.06   -6.462  1 46.38 ? 317 ARG   B O   1 
ATOM   5359 C  CB  . ARG   B 1 332 ? 4.226   -7.495  -8.517  1 45.05 ? 317 ARG   B CB  1 
ATOM   5360 C  CG  . ARG   B 1 332 ? 3.075   -6.791  -9.208  1 44.13 ? 317 ARG   B CG  1 
ATOM   5361 C  CD  . ARG   B 1 332 ? 3.35    -6.514  -10.661 1 45.07 ? 317 ARG   B CD  1 
ATOM   5362 N  NE  . ARG   B 1 332 ? 2.651   -5.299  -11.104 1 45.23 ? 317 ARG   B NE  1 
ATOM   5363 C  CZ  . ARG   B 1 332 ? 1.468   -5.308  -11.711 1 48.05 ? 317 ARG   B CZ  1 
ATOM   5364 N  NH1 . ARG   B 1 332 ? 0.846   -6.457  -11.953 1 48.09 ? 317 ARG   B NH1 1 
ATOM   5365 N  NH2 . ARG   B 1 332 ? 0.885   -4.169  -12.062 1 48.22 ? 317 ARG   B NH2 1 
ATOM   5366 N  N   . GLU   B 1 333 ? 2.811   -9.889  -7.123  1 47.24 ? 318 GLU   B N   1 
ATOM   5367 C  CA  . GLU   B 1 333 ? 1.658   -10.777 -6.988  1 47.99 ? 318 GLU   B CA  1 
ATOM   5368 C  C   . GLU   B 1 333 ? 1.208   -10.871 -5.538  1 47.29 ? 318 GLU   B C   1 
ATOM   5369 O  O   . GLU   B 1 333 ? 0.008   -10.907 -5.284  1 47.2  ? 318 GLU   B O   1 
ATOM   5370 C  CB  . GLU   B 1 333 ? 1.915   -12.162 -7.612  1 51.35 ? 318 GLU   B CB  1 
ATOM   5371 C  CG  . GLU   B 1 333 ? 1.08    -12.405 -8.861  1 58.97 ? 318 GLU   B CG  1 
ATOM   5372 C  CD  . GLU   B 1 333 ? 1.472   -11.583 -10.079 1 69.17 ? 318 GLU   B CD  1 
ATOM   5373 O  OE1 . GLU   B 1 333 ? 0.915   -10.474 -10.266 1 69.97 ? 318 GLU   B OE1 1 
ATOM   5374 O  OE2 . GLU   B 1 333 ? 2.335   -12.058 -10.856 1 72.59 ? 318 GLU   B OE2 1 
ATOM   5375 N  N   . PHE   B 1 334 ? 2.162   -10.856 -4.585  1 46.42 ? 319 PHE   B N   1 
ATOM   5376 C  CA  . PHE   B 1 334 ? 1.823   -10.886 -3.164  1 45.75 ? 319 PHE   B CA  1 
ATOM   5377 C  C   . PHE   B 1 334 ? 1.016   -9.645  -2.78   1 45.53 ? 319 PHE   B C   1 
ATOM   5378 O  O   . PHE   B 1 334 ? 0.004   -9.777  -2.113  1 45.83 ? 319 PHE   B O   1 
ATOM   5379 C  CB  . PHE   B 1 334 ? 3.088   -10.979 -2.294  1 45.21 ? 319 PHE   B CB  1 
ATOM   5380 C  CG  . PHE   B 1 334 ? 2.85    -11.151 -0.806  1 45.34 ? 319 PHE   B CG  1 
ATOM   5381 C  CD1 . PHE   B 1 334 ? 2.578   -10.061 0.003   1 45.43 ? 319 PHE   B CD1 1 
ATOM   5382 C  CD2 . PHE   B 1 334 ? 2.954   -12.396 -0.209  1 45.78 ? 319 PHE   B CD2 1 
ATOM   5383 C  CE1 . PHE   B 1 334 ? 2.364   -10.222 1.362   1 45.98 ? 319 PHE   B CE1 1 
ATOM   5384 C  CE2 . PHE   B 1 334 ? 2.755   -12.548 1.158   1 46.21 ? 319 PHE   B CE2 1 
ATOM   5385 C  CZ  . PHE   B 1 334 ? 2.472   -11.46  1.934   1 45.81 ? 319 PHE   B CZ  1 
ATOM   5386 N  N   . VAL   B 1 335 ? 1.46    -8.455  -3.189  1 45.04 ? 320 VAL   B N   1 
ATOM   5387 C  CA  . VAL   B 1 335 ? 0.802   -7.195  -2.849  1 45.36 ? 320 VAL   B CA  1 
ATOM   5388 C  C   . VAL   B 1 335 ? -0.574  -7.068  -3.524  1 47.44 ? 320 VAL   B C   1 
ATOM   5389 O  O   . VAL   B 1 335 ? -1.532  -6.553  -2.94   1 47.71 ? 320 VAL   B O   1 
ATOM   5390 C  CB  . VAL   B 1 335 ? 1.756   -6.008  -3.15   1 44.53 ? 320 VAL   B CB  1 
ATOM   5391 C  CG1 . VAL   B 1 335 ? 1.036   -4.68   -3.099  1 44.85 ? 320 VAL   B CG1 1 
ATOM   5392 C  CG2 . VAL   B 1 335 ? 2.938   -6.009  -2.191  1 44.38 ? 320 VAL   B CG2 1 
ATOM   5393 N  N   . LEU   B 1 336 ? -0.672  -7.558  -4.75   1 48.36 ? 321 LEU   B N   1 
ATOM   5394 C  CA  . LEU   B 1 336 ? -1.906  -7.52   -5.51   1 49.34 ? 321 LEU   B CA  1 
ATOM   5395 C  C   . LEU   B 1 336 ? -2.982  -8.425  -4.875  1 49.77 ? 321 LEU   B C   1 
ATOM   5396 O  O   . LEU   B 1 336 ? -4.172  -8.132  -4.98   1 50.21 ? 321 LEU   B O   1 
ATOM   5397 C  CB  . LEU   B 1 336 ? -1.583  -8.018  -6.923  1 50.06 ? 321 LEU   B CB  1 
ATOM   5398 C  CG  . LEU   B 1 336 ? -2.164  -7.34   -8.169  1 52.81 ? 321 LEU   B CG  1 
ATOM   5399 C  CD1 . LEU   B 1 336 ? -2.717  -5.934  -7.911  1 53.6  ? 321 LEU   B CD1 1 
ATOM   5400 C  CD2 . LEU   B 1 336 ? -1.14   -7.344  -9.288  1 53.69 ? 321 LEU   B CD2 1 
ATOM   5401 N  N   . SER   B 1 337 ? -2.57   -9.512  -4.222  1 49.56 ? 322 SER   B N   1 
ATOM   5402 C  CA  . SER   B 1 337 ? -3.508  -10.47  -3.658  1 50.09 ? 322 SER   B CA  1 
ATOM   5403 C  C   . SER   B 1 337 ? -4.019  -10.152 -2.249  1 51.09 ? 322 SER   B C   1 
ATOM   5404 O  O   . SER   B 1 337 ? -4.856  -10.902 -1.747  1 51.76 ? 322 SER   B O   1 
ATOM   5405 C  CB  . SER   B 1 337 ? -2.877  -11.855 -3.656  1 50.14 ? 322 SER   B CB  1 
ATOM   5406 O  OG  . SER   B 1 337 ? -1.896  -11.957 -2.635  1 51.42 ? 322 SER   B OG  1 
ATOM   5407 N  N   . LYS   B 1 338 ? -3.486  -9.115  -1.583  1 50.71 ? 323 LYS   B N   1 
ATOM   5408 C  CA  . LYS   B 1 338 ? -3.835  -8.853  -0.191  1 50.46 ? 323 LYS   B CA  1 
ATOM   5409 C  C   . LYS   B 1 338 ? -5      -7.876  0.062   1 50.9  ? 323 LYS   B C   1 
ATOM   5410 O  O   . LYS   B 1 338 ? -5.506  -7.859  1.191   1 51.79 ? 323 LYS   B O   1 
ATOM   5411 C  CB  . LYS   B 1 338 ? -2.61   -8.386  0.603   1 51.54 ? 323 LYS   B CB  1 
ATOM   5412 C  CG  . LYS   B 1 338 ? -1.457  -9.381  0.68    1 54.72 ? 323 LYS   B CG  1 
ATOM   5413 C  CD  . LYS   B 1 338 ? -1.838  -10.741 1.251   1 58.59 ? 323 LYS   B CD  1 
ATOM   5414 C  CE  . LYS   B 1 338 ? -0.931  -11.811 0.679   1 62.9  ? 323 LYS   B CE  1 
ATOM   5415 N  NZ  . LYS   B 1 338 ? -1.471  -13.193 0.862   1 65.19 ? 323 LYS   B NZ  1 
ATOM   5416 N  N   . GLY   B 1 339 ? -5.425  -7.091  -0.939  1 49.79 ? 324 GLY   B N   1 
ATOM   5417 C  CA  . GLY   B 1 339 ? -6.513  -6.123  -0.768  1 49.17 ? 324 GLY   B CA  1 
ATOM   5418 C  C   . GLY   B 1 339 ? -6.229  -5.133  0.351   1 48.23 ? 324 GLY   B C   1 
ATOM   5419 O  O   . GLY   B 1 339 ? -7.093  -4.843  1.181   1 48.42 ? 324 GLY   B O   1 
ATOM   5420 N  N   . ASP   B 1 340 ? -4.976  -4.66   0.396   1 47.01 ? 325 ASP   B N   1 
ATOM   5421 C  CA  . ASP   B 1 340 ? -4.418  -3.791  1.417   1 46.26 ? 325 ASP   B CA  1 
ATOM   5422 C  C   . ASP   B 1 340 ? -3.9    -2.543  0.733   1 46.26 ? 325 ASP   B C   1 
ATOM   5423 O  O   . ASP   B 1 340 ? -2.893  -2.612  0.038   1 46.78 ? 325 ASP   B O   1 
ATOM   5424 C  CB  . ASP   B 1 340 ? -3.255  -4.552  2.073   1 46.75 ? 325 ASP   B CB  1 
ATOM   5425 C  CG  . ASP   B 1 340 ? -2.625  -3.93   3.296   1 48.12 ? 325 ASP   B CG  1 
ATOM   5426 O  OD1 . ASP   B 1 340 ? -2.542  -2.684  3.357   1 47.54 ? 325 ASP   B OD1 1 
ATOM   5427 O  OD2 . ASP   B 1 340 ? -2.187  -4.69   4.178   1 49.5  ? 325 ASP   B OD2 1 
ATOM   5428 N  N   . ALA   B 1 341 ? -4.575  -1.415  0.934   1 45.85 ? 326 ALA   B N   1 
ATOM   5429 C  CA  . ALA   B 1 341 ? -4.242  -0.134  0.339   1 46.28 ? 326 ALA   B CA  1 
ATOM   5430 C  C   . ALA   B 1 341 ? -2.878  0.382   0.766   1 46.75 ? 326 ALA   B C   1 
ATOM   5431 O  O   . ALA   B 1 341 ? -2.133  0.839   -0.087  1 47.16 ? 326 ALA   B O   1 
ATOM   5432 C  CB  . ALA   B 1 341 ? -5.323  0.898   0.643   1 46.19 ? 326 ALA   B CB  1 
ATOM   5433 N  N   . GLY   B 1 342 ? -2.551  0.289   2.05    1 46.71 ? 327 GLY   B N   1 
ATOM   5434 C  CA  . GLY   B 1 342 ? -1.257  0.729   2.559   1 47.16 ? 327 GLY   B CA  1 
ATOM   5435 C  C   . GLY   B 1 342 ? -0.076  0.003   1.934   1 47.44 ? 327 GLY   B C   1 
ATOM   5436 O  O   . GLY   B 1 342 ? 0.95    0.616   1.638   1 47.77 ? 327 GLY   B O   1 
ATOM   5437 N  N   . LEU   B 1 343 ? -0.22   -1.308  1.717   1 47.09 ? 328 LEU   B N   1 
ATOM   5438 C  CA  . LEU   B 1 343 ? 0.794   -2.155  1.099   1 47.17 ? 328 LEU   B CA  1 
ATOM   5439 C  C   . LEU   B 1 343 ? 0.919   -1.832  -0.395  1 47.4  ? 328 LEU   B C   1 
ATOM   5440 O  O   . LEU   B 1 343 ? 2.032   -1.755  -0.907  1 47.86 ? 328 LEU   B O   1 
ATOM   5441 C  CB  . LEU   B 1 343 ? 0.385   -3.617  1.29    1 47.2  ? 328 LEU   B CB  1 
ATOM   5442 C  CG  . LEU   B 1 343 ? 1.486   -4.661  1.425   1 48.95 ? 328 LEU   B CG  1 
ATOM   5443 C  CD1 . LEU   B 1 343 ? 2.545   -4.256  2.449   1 49.24 ? 328 LEU   B CD1 1 
ATOM   5444 C  CD2 . LEU   B 1 343 ? 0.895   -5.987  1.824   1 49.62 ? 328 LEU   B CD2 1 
ATOM   5445 N  N   . ARG   B 1 344 ? -0.214  -1.633  -1.083  1 46.9  ? 329 ARG   B N   1 
ATOM   5446 C  CA  . ARG   B 1 344 ? -0.237  -1.258  -2.491  1 47.6  ? 329 ARG   B CA  1 
ATOM   5447 C  C   . ARG   B 1 344 ? 0.416   0.104   -2.696  1 47.44 ? 329 ARG   B C   1 
ATOM   5448 O  O   . ARG   B 1 344 ? 1.097   0.301   -3.696  1 47.48 ? 329 ARG   B O   1 
ATOM   5449 C  CB  . ARG   B 1 344 ? -1.674  -1.225  -3.055  1 49.13 ? 329 ARG   B CB  1 
ATOM   5450 C  CG  . ARG   B 1 344 ? -2.26   -2.607  -3.296  1 52.93 ? 329 ARG   B CG  1 
ATOM   5451 C  CD  . ARG   B 1 344 ? -3.428  -2.617  -4.274  1 56.49 ? 329 ARG   B CD  1 
ATOM   5452 N  NE  . ARG   B 1 344 ? -4.485  -1.674  -3.904  1 59.67 ? 329 ARG   B NE  1 
ATOM   5453 C  CZ  . ARG   B 1 344 ? -5.481  -1.952  -3.067  1 60.9  ? 329 ARG   B CZ  1 
ATOM   5454 N  NH1 . ARG   B 1 344 ? -5.568  -3.149  -2.499  1 59.2  ? 329 ARG   B NH1 1 
ATOM   5455 N  NH2 . ARG   B 1 344 ? -6.396  -1.032  -2.787  1 61.19 ? 329 ARG   B NH2 1 
ATOM   5456 N  N   . GLU   B 1 345 ? 0.208   1.041   -1.763  1 46.8  ? 330 GLU   B N   1 
ATOM   5457 C  CA  . GLU   B 1 345 ? 0.776   2.376   -1.862  1 46.35 ? 330 GLU   B CA  1 
ATOM   5458 C  C   . GLU   B 1 345 ? 2.287   2.366   -1.623  1 45.96 ? 330 GLU   B C   1 
ATOM   5459 O  O   . GLU   B 1 345 ? 2.994   3.154   -2.238  1 46.68 ? 330 GLU   B O   1 
ATOM   5460 C  CB  . GLU   B 1 345 ? 0.049   3.367   -0.939  1 47.37 ? 330 GLU   B CB  1 
ATOM   5461 N  N   . ALA   B 1 346 ? 2.776   1.485   -0.75   1 44.66 ? 331 ALA   B N   1 
ATOM   5462 C  CA  . ALA   B 1 346 ? 4.206   1.33    -0.491  1 43.85 ? 331 ALA   B CA  1 
ATOM   5463 C  C   . ALA   B 1 346 ? 4.883   0.711   -1.739  1 42.94 ? 331 ALA   B C   1 
ATOM   5464 O  O   . ALA   B 1 346 ? 5.982   1.109   -2.11   1 43    ? 331 ALA   B O   1 
ATOM   5465 C  CB  . ALA   B 1 346 ? 4.431   0.44    0.73    1 43.48 ? 331 ALA   B CB  1 
ATOM   5466 N  N   . TYR   B 1 347 ? 4.224   -0.25   -2.383  1 42.16 ? 332 TYR   B N   1 
ATOM   5467 C  CA  . TYR   B 1 347 ? 4.732   -0.889  -3.598  1 41.57 ? 332 TYR   B CA  1 
ATOM   5468 C  C   . TYR   B 1 347 ? 4.787   0.165   -4.721  1 42.64 ? 332 TYR   B C   1 
ATOM   5469 O  O   . TYR   B 1 347 ? 5.763   0.24    -5.466  1 42.96 ? 332 TYR   B O   1 
ATOM   5470 C  CB  . TYR   B 1 347 ? 3.799   -2.055  -4.013  1 40.17 ? 332 TYR   B CB  1 
ATOM   5471 C  CG  . TYR   B 1 347 ? 4.138   -2.634  -5.369  1 39.23 ? 332 TYR   B CG  1 
ATOM   5472 C  CD1 . TYR   B 1 347 ? 5.123   -3.606  -5.506  1 39.23 ? 332 TYR   B CD1 1 
ATOM   5473 C  CD2 . TYR   B 1 347 ? 3.547   -2.141  -6.523  1 38.85 ? 332 TYR   B CD2 1 
ATOM   5474 C  CE1 . TYR   B 1 347 ? 5.483   -4.09   -6.753  1 39.42 ? 332 TYR   B CE1 1 
ATOM   5475 C  CE2 . TYR   B 1 347 ? 3.886   -2.632  -7.772  1 38.84 ? 332 TYR   B CE2 1 
ATOM   5476 C  CZ  . TYR   B 1 347 ? 4.875   -3.582  -7.886  1 39.82 ? 332 TYR   B CZ  1 
ATOM   5477 O  OH  . TYR   B 1 347 ? 5.215   -4.083  -9.122  1 41.4  ? 332 TYR   B OH  1 
ATOM   5478 N  N   . ASP   B 1 348 ? 3.71    0.952   -4.861  1 42.68 ? 333 ASP   B N   1 
ATOM   5479 C  CA  . ASP   B 1 348 ? 3.618   1.98    -5.892  1 43.04 ? 333 ASP   B CA  1 
ATOM   5480 C  C   . ASP   B 1 348 ? 4.634   3.086   -5.712  1 43.68 ? 333 ASP   B C   1 
ATOM   5481 O  O   . ASP   B 1 348 ? 5.059   3.67    -6.705  1 43.83 ? 333 ASP   B O   1 
ATOM   5482 C  CB  . ASP   B 1 348 ? 2.202   2.558   -5.975  1 43.92 ? 333 ASP   B CB  1 
ATOM   5483 C  CG  . ASP   B 1 348 ? 1.248   1.782   -6.848  1 46.58 ? 333 ASP   B CG  1 
ATOM   5484 O  OD1 . ASP   B 1 348 ? 1.65    0.732   -7.383  1 46.16 ? 333 ASP   B OD1 1 
ATOM   5485 O  OD2 . ASP   B 1 348 ? 0.094   2.225   -7.002  1 49.6  ? 333 ASP   B OD2 1 
ATOM   5486 N  N   . ALA   B 1 349 ? 5.034   3.368   -4.46   1 43.54 ? 334 ALA   B N   1 
ATOM   5487 C  CA  . ALA   B 1 349 ? 6.052   4.37    -4.173  1 43.46 ? 334 ALA   B CA  1 
ATOM   5488 C  C   . ALA   B 1 349 ? 7.394   3.894   -4.76   1 43.56 ? 334 ALA   B C   1 
ATOM   5489 O  O   . ALA   B 1 349 ? 8.131   4.72    -5.292  1 44.54 ? 334 ALA   B O   1 
ATOM   5490 C  CB  . ALA   B 1 349 ? 6.169   4.575   -2.671  1 43.14 ? 334 ALA   B CB  1 
ATOM   5491 N  N   . CYS   B 1 350 ? 7.693   2.571   -4.687  1 42.36 ? 335 CYS   B N   1 
ATOM   5492 C  CA  . CYS   B 1 350 ? 8.907   1.97    -5.229  1 42.07 ? 335 CYS   B CA  1 
ATOM   5493 C  C   . CYS   B 1 350 ? 8.917   2.112   -6.752  1 42.99 ? 335 CYS   B C   1 
ATOM   5494 O  O   . CYS   B 1 350 ? 9.914   2.538   -7.318  1 43.06 ? 335 CYS   B O   1 
ATOM   5495 C  CB  . CYS   B 1 350 ? 9.024   0.503   -4.824  1 41.66 ? 335 CYS   B CB  1 
ATOM   5496 S  SG  . CYS   B 1 350 ? 9.389   0.222   -3.081  1 43.2  ? 335 CYS   B SG  1 
ATOM   5497 N  N   . VAL   B 1 351 ? 7.819   1.733   -7.408  1 43.61 ? 336 VAL   B N   1 
ATOM   5498 C  CA  . VAL   B 1 351 ? 7.67    1.808   -8.855  1 44.55 ? 336 VAL   B CA  1 
ATOM   5499 C  C   . VAL   B 1 351 ? 7.726   3.268   -9.34   1 45.45 ? 336 VAL   B C   1 
ATOM   5500 O  O   . VAL   B 1 351 ? 8.47    3.565   -10.281 1 46.34 ? 336 VAL   B O   1 
ATOM   5501 C  CB  . VAL   B 1 351 ? 6.386   1.068   -9.311  1 45.09 ? 336 VAL   B CB  1 
ATOM   5502 C  CG1 . VAL   B 1 351 ? 6.201   1.162   -10.822 1 45.69 ? 336 VAL   B CG1 1 
ATOM   5503 C  CG2 . VAL   B 1 351 ? 6.414   -0.39   -8.865  1 45.14 ? 336 VAL   B CG2 1 
ATOM   5504 N  N   . LYS   B 1 352 ? 7.031   4.187   -8.646  1 44.72 ? 337 LYS   B N   1 
ATOM   5505 C  CA  . LYS   B 1 352 ? 7.036   5.612   -8.99   1 44.41 ? 337 LYS   B CA  1 
ATOM   5506 C  C   . LYS   B 1 352 ? 8.427   6.203   -8.893  1 44.25 ? 337 LYS   B C   1 
ATOM   5507 O  O   . LYS   B 1 352 ? 8.79    7.03    -9.736  1 44.93 ? 337 LYS   B O   1 
ATOM   5508 C  CB  . LYS   B 1 352 ? 6.034   6.414   -8.142  1 45.13 ? 337 LYS   B CB  1 
ATOM   5509 N  N   . ALA   B 1 353 ? 9.224   5.758   -7.901  1 43.26 ? 338 ALA   B N   1 
ATOM   5510 C  CA  . ALA   B 1 353 ? 10.612  6.211   -7.74   1 42.86 ? 338 ALA   B CA  1 
ATOM   5511 C  C   . ALA   B 1 353 ? 11.497  5.774   -8.929  1 42.85 ? 338 ALA   B C   1 
ATOM   5512 O  O   . ALA   B 1 353 ? 12.357  6.536   -9.346  1 43.7  ? 338 ALA   B O   1 
ATOM   5513 C  CB  . ALA   B 1 353 ? 11.192  5.701   -6.441  1 42.57 ? 338 ALA   B CB  1 
ATOM   5514 N  N   . LEU   B 1 354 ? 11.268  4.574   -9.481  1 41.82 ? 339 LEU   B N   1 
ATOM   5515 C  CA  . LEU   B 1 354 ? 11.997  4.05    -10.641 1 41.59 ? 339 LEU   B CA  1 
ATOM   5516 C  C   . LEU   B 1 354 ? 11.561  4.802   -11.903 1 41.05 ? 339 LEU   B C   1 
ATOM   5517 O  O   . LEU   B 1 354 ? 12.394  5.091   -12.76  1 41.01 ? 339 LEU   B O   1 
ATOM   5518 C  CB  . LEU   B 1 354 ? 11.681  2.559   -10.797 1 41.88 ? 339 LEU   B CB  1 
ATOM   5519 C  CG  . LEU   B 1 354 ? 12.805  1.587   -11.004 1 44.86 ? 339 LEU   B CG  1 
ATOM   5520 C  CD1 . LEU   B 1 354 ? 14      1.824   -10.055 1 46.08 ? 339 LEU   B CD1 1 
ATOM   5521 C  CD2 . LEU   B 1 354 ? 12.293  0.169   -10.851 1 45.95 ? 339 LEU   B CD2 1 
ATOM   5522 N  N   . VAL   B 1 355 ? 10.257  5.115   -12.024 1 40.13 ? 340 VAL   B N   1 
ATOM   5523 C  CA  . VAL   B 1 355 ? 9.739   5.887   -13.147 1 39.72 ? 340 VAL   B CA  1 
ATOM   5524 C  C   . VAL   B 1 355 ? 10.377  7.289   -13.135 1 40.51 ? 340 VAL   B C   1 
ATOM   5525 O  O   . VAL   B 1 355 ? 10.788  7.775   -14.185 1 40.8  ? 340 VAL   B O   1 
ATOM   5526 C  CB  . VAL   B 1 355 ? 8.189   5.97    -13.156 1 38.6  ? 340 VAL   B CB  1 
ATOM   5527 C  CG1 . VAL   B 1 355 ? 7.693   6.887   -14.262 1 37.86 ? 340 VAL   B CG1 1 
ATOM   5528 C  CG2 . VAL   B 1 355 ? 7.549   4.59    -13.288 1 38.89 ? 340 VAL   B CG2 1 
ATOM   5529 N  N   . SER   B 1 356 ? 10.491  7.916   -11.96  1 40.77 ? 341 SER   B N   1 
ATOM   5530 C  CA  . SER   B 1 356 ? 11.098  9.244   -11.86  1 41.87 ? 341 SER   B CA  1 
ATOM   5531 C  C   . SER   B 1 356 ? 12.586  9.211   -12.242 1 42.43 ? 341 SER   B C   1 
ATOM   5532 O  O   . SER   B 1 356 ? 13.045  10.112  -12.945 1 42.79 ? 341 SER   B O   1 
ATOM   5533 C  CB  . SER   B 1 356 ? 10.921  9.816   -10.461 1 44.17 ? 341 SER   B CB  1 
ATOM   5534 O  OG  . SER   B 1 356 ? 9.534   9.974   -10.223 1 48.29 ? 341 SER   B OG  1 
ATOM   5535 N  N   . LEU   B 1 357 ? 13.325  8.154   -11.827 1 42.08 ? 342 LEU   B N   1 
ATOM   5536 C  CA  . LEU   B 1 357 ? 14.735  7.994   -12.19  1 42.35 ? 342 LEU   B CA  1 
ATOM   5537 C  C   . LEU   B 1 357 ? 14.88   7.923   -13.72  1 41.47 ? 342 LEU   B C   1 
ATOM   5538 O  O   . LEU   B 1 357 ? 15.68   8.665   -14.291 1 41.41 ? 342 LEU   B O   1 
ATOM   5539 C  CB  . LEU   B 1 357 ? 15.337  6.726   -11.557 1 43.38 ? 342 LEU   B CB  1 
ATOM   5540 C  CG  . LEU   B 1 357 ? 15.637  6.781   -10.067 1 46.65 ? 342 LEU   B CG  1 
ATOM   5541 C  CD1 . LEU   B 1 357 ? 15.901  5.399   -9.529  1 47.22 ? 342 LEU   B CD1 1 
ATOM   5542 C  CD2 . LEU   B 1 357 ? 16.842  7.625   -9.802  1 48.03 ? 342 LEU   B CD2 1 
ATOM   5543 N  N   . ARG   B 1 358 ? 14.069  7.072   -14.375 1 40.32 ? 343 ARG   B N   1 
ATOM   5544 C  CA  . ARG   B 1 358 ? 14.118  6.865   -15.81  1 39.71 ? 343 ARG   B CA  1 
ATOM   5545 C  C   . ARG   B 1 358 ? 13.654  8.069   -16.606 1 39.9  ? 343 ARG   B C   1 
ATOM   5546 O  O   . ARG   B 1 358 ? 14.184  8.327   -17.686 1 39.98 ? 343 ARG   B O   1 
ATOM   5547 C  CB  . ARG   B 1 358 ? 13.35   5.598   -16.189 1 39.91 ? 343 ARG   B CB  1 
ATOM   5548 C  CG  . ARG   B 1 358 ? 14.021  4.373   -15.604 1 40.31 ? 343 ARG   B CG  1 
ATOM   5549 C  CD  . ARG   B 1 358 ? 13.311  3.092   -15.927 1 41.59 ? 343 ARG   B CD  1 
ATOM   5550 N  NE  . ARG   B 1 358 ? 14.278  2.01    -15.832 1 43.62 ? 343 ARG   B NE  1 
ATOM   5551 C  CZ  . ARG   B 1 358 ? 14.103  0.89    -15.148 1 44.26 ? 343 ARG   B CZ  1 
ATOM   5552 N  NH1 . ARG   B 1 358 ? 12.957  0.66    -14.519 1 44.1  ? 343 ARG   B NH1 1 
ATOM   5553 N  NH2 . ARG   B 1 358 ? 15.066  -0.019  -15.101 1 43.04 ? 343 ARG   B NH2 1 
ATOM   5554 N  N   . SER   B 1 359 ? 12.688  8.813   -16.072 1 39.66 ? 344 SER   B N   1 
ATOM   5555 C  CA  . SER   B 1 359 ? 12.178  10.016  -16.719 1 39.99 ? 344 SER   B CA  1 
ATOM   5556 C  C   . SER   B 1 359 ? 13.261  11.091  -16.671 1 39.56 ? 344 SER   B C   1 
ATOM   5557 O  O   . SER   B 1 359 ? 13.486  11.76   -17.664 1 39.45 ? 344 SER   B O   1 
ATOM   5558 C  CB  . SER   B 1 359 ? 10.922  10.516  -16.003 1 41.47 ? 344 SER   B CB  1 
ATOM   5559 O  OG  . SER   B 1 359 ? 9.821   9.651   -16.232 1 44.46 ? 344 SER   B OG  1 
ATOM   5560 N  N   . TYR   B 1 360 ? 13.953  11.232  -15.532 1 39    ? 345 TYR   B N   1 
ATOM   5561 C  CA  . TYR   B 1 360 ? 15.017  12.2    -15.403 1 39.67 ? 345 TYR   B CA  1 
ATOM   5562 C  C   . TYR   B 1 360 ? 16.174  11.824  -16.351 1 40.12 ? 345 TYR   B C   1 
ATOM   5563 O  O   . TYR   B 1 360 ? 16.7    12.679  -17.074 1 41.12 ? 345 TYR   B O   1 
ATOM   5564 C  CB  . TYR   B 1 360 ? 15.483  12.254  -13.95  1 40.45 ? 345 TYR   B CB  1 
ATOM   5565 C  CG  . TYR   B 1 360 ? 16.445  13.383  -13.709 1 42.95 ? 345 TYR   B CG  1 
ATOM   5566 C  CD1 . TYR   B 1 360 ? 15.997  14.692  -13.606 1 44.36 ? 345 TYR   B CD1 1 
ATOM   5567 C  CD2 . TYR   B 1 360 ? 17.813  13.154  -13.636 1 44.74 ? 345 TYR   B CD2 1 
ATOM   5568 C  CE1 . TYR   B 1 360 ? 16.884  15.743  -13.405 1 46.12 ? 345 TYR   B CE1 1 
ATOM   5569 C  CE2 . TYR   B 1 360 ? 18.709  14.196  -13.433 1 46.19 ? 345 TYR   B CE2 1 
ATOM   5570 C  CZ  . TYR   B 1 360 ? 18.243  15.493  -13.354 1 47.66 ? 345 TYR   B CZ  1 
ATOM   5571 O  OH  . TYR   B 1 360 ? 19.128  16.528  -13.187 1 50.73 ? 345 TYR   B OH  1 
ATOM   5572 N  N   . HIS   B 1 361 ? 16.529  10.529  -16.382 1 38.73 ? 346 HIS   B N   1 
ATOM   5573 C  CA  . HIS   B 1 361 ? 17.569  9.991   -17.237 1 37.4  ? 346 HIS   B CA  1 
ATOM   5574 C  C   . HIS   B 1 361 ? 17.236  10.225  -18.725 1 37.77 ? 346 HIS   B C   1 
ATOM   5575 O  O   . HIS   B 1 361 ? 18.153  10.465  -19.505 1 38.26 ? 346 HIS   B O   1 
ATOM   5576 C  CB  . HIS   B 1 361 ? 17.778  8.495   -16.904 1 36.58 ? 346 HIS   B CB  1 
ATOM   5577 C  CG  . HIS   B 1 361 ? 18.792  7.788   -17.751 1 35.96 ? 346 HIS   B CG  1 
ATOM   5578 N  ND1 . HIS   B 1 361 ? 18.411  7.009   -18.831 1 37.08 ? 346 HIS   B ND1 1 
ATOM   5579 C  CD2 . HIS   B 1 361 ? 20.135  7.723   -17.617 1 36.31 ? 346 HIS   B CD2 1 
ATOM   5580 C  CE1 . HIS   B 1 361 ? 19.526  6.515   -19.328 1 37.49 ? 346 HIS   B CE1 1 
ATOM   5581 N  NE2 . HIS   B 1 361 ? 20.591  6.905   -18.621 1 37.52 ? 346 HIS   B NE2 1 
ATOM   5582 N  N   . LEU   B 1 362 ? 15.941  10.202  -19.114 1 37.59 ? 347 LEU   B N   1 
ATOM   5583 C  CA  . LEU   B 1 362 ? 15.533  10.497  -20.494 1 38.03 ? 347 LEU   B CA  1 
ATOM   5584 C  C   . LEU   B 1 362 ? 15.838  11.96   -20.835 1 38.64 ? 347 LEU   B C   1 
ATOM   5585 O  O   . LEU   B 1 362 ? 16.3    12.247  -21.927 1 38.68 ? 347 LEU   B O   1 
ATOM   5586 C  CB  . LEU   B 1 362 ? 14.044  10.228  -20.698 1 37.92 ? 347 LEU   B CB  1 
ATOM   5587 C  CG  . LEU   B 1 362 ? 13.716  8.812   -21.157 1 38.61 ? 347 LEU   B CG  1 
ATOM   5588 C  CD1 . LEU   B 1 362 ? 12.261  8.471   -20.932 1 38.1  ? 347 LEU   B CD1 1 
ATOM   5589 C  CD2 . LEU   B 1 362 ? 14.119  8.61    -22.586 1 38.69 ? 347 LEU   B CD2 1 
ATOM   5590 N  N   . GLN   B 1 363 ? 15.588  12.879  -19.896 1 39.02 ? 348 GLN   B N   1 
ATOM   5591 C  CA  . GLN   B 1 363 ? 15.879  14.291  -20.1   1 40.22 ? 348 GLN   B CA  1 
ATOM   5592 C  C   . GLN   B 1 363 ? 17.384  14.508  -20.284 1 41.28 ? 348 GLN   B C   1 
ATOM   5593 O  O   . GLN   B 1 363 ? 17.783  15.3    -21.131 1 41.52 ? 348 GLN   B O   1 
ATOM   5594 C  CB  . GLN   B 1 363 ? 15.325  15.118  -18.948 1 41.96 ? 348 GLN   B CB  1 
ATOM   5595 C  CG  . GLN   B 1 363 ? 13.808  15.144  -18.969 1 46.47 ? 348 GLN   B CG  1 
ATOM   5596 C  CD  . GLN   B 1 363 ? 13.239  15.714  -17.701 1 52.9  ? 348 GLN   B CD  1 
ATOM   5597 O  OE1 . GLN   B 1 363 ? 12.492  15.036  -16.987 1 55.89 ? 348 GLN   B OE1 1 
ATOM   5598 N  NE2 . GLN   B 1 363 ? 13.603  16.944  -17.379 1 53.36 ? 348 GLN   B NE2 1 
ATOM   5599 N  N   . ILE   B 1 364 ? 18.209  13.758  -19.532 1 41.11 ? 349 ILE   B N   1 
ATOM   5600 C  CA  . ILE   B 1 364 ? 19.661  13.773  -19.634 1 41.66 ? 349 ILE   B CA  1 
ATOM   5601 C  C   . ILE   B 1 364 ? 20.126  13.268  -21.01  1 42.06 ? 349 ILE   B C   1 
ATOM   5602 O  O   . ILE   B 1 364 ? 20.977  13.89   -21.624 1 42.88 ? 349 ILE   B O   1 
ATOM   5603 C  CB  . ILE   B 1 364 ? 20.245  12.924  -18.482 1 41.83 ? 349 ILE   B CB  1 
ATOM   5604 C  CG1 . ILE   B 1 364 ? 20.016  13.66   -17.163 1 43.3  ? 349 ILE   B CG1 1 
ATOM   5605 C  CG2 . ILE   B 1 364 ? 21.724  12.541  -18.724 1 41.71 ? 349 ILE   B CG2 1 
ATOM   5606 C  CD1 . ILE   B 1 364 ? 20.382  12.961  -16.08  1 45.45 ? 349 ILE   B CD1 1 
ATOM   5607 N  N   . VAL   B 1 365 ? 19.559  12.164  -21.495 1 41.44 ? 350 VAL   B N   1 
ATOM   5608 C  CA  . VAL   B 1 365 ? 19.922  11.63   -22.796 1 41.31 ? 350 VAL   B CA  1 
ATOM   5609 C  C   . VAL   B 1 365 ? 19.543  12.634  -23.916 1 41.45 ? 350 VAL   B C   1 
ATOM   5610 O  O   . VAL   B 1 365 ? 20.289  12.776  -24.88  1 42.42 ? 350 VAL   B O   1 
ATOM   5611 C  CB  . VAL   B 1 365 ? 19.378  10.199  -23     1 41.6  ? 350 VAL   B CB  1 
ATOM   5612 C  CG1 . VAL   B 1 365 ? 19.631  9.721   -24.415 1 41.92 ? 350 VAL   B CG1 1 
ATOM   5613 C  CG2 . VAL   B 1 365 ? 20.011  9.235   -22.005 1 41.71 ? 350 VAL   B CG2 1 
ATOM   5614 N  N   . THR   B 1 366 ? 18.461  13.392  -23.75  1 40.84 ? 351 THR   B N   1 
ATOM   5615 C  CA  . THR   B 1 366 ? 18.081  14.435  -24.722 1 40.95 ? 351 THR   B CA  1 
ATOM   5616 C  C   . THR   B 1 366 ? 19.158  15.54   -24.757 1 41.42 ? 351 THR   B C   1 
ATOM   5617 O  O   . THR   B 1 366 ? 19.613  15.944  -25.832 1 42.1  ? 351 THR   B O   1 
ATOM   5618 C  CB  . THR   B 1 366 ? 16.697  15.014  -24.354 1 41.34 ? 351 THR   B CB  1 
ATOM   5619 O  OG1 . THR   B 1 366 ? 15.733  13.961  -24.409 1 41.74 ? 351 THR   B OG1 1 
ATOM   5620 C  CG2 . THR   B 1 366 ? 16.261  16.121  -25.301 1 41.49 ? 351 THR   B CG2 1 
ATOM   5621 N  N   . LYS   B 1 367 ? 19.605  15.98   -23.576 1 40.74 ? 352 LYS   B N   1 
ATOM   5622 C  CA  . LYS   B 1 367 ? 20.636  17.007  -23.448 1 40.82 ? 352 LYS   B CA  1 
ATOM   5623 C  C   . LYS   B 1 367 ? 22.03   16.57   -23.954 1 41.49 ? 352 LYS   B C   1 
ATOM   5624 O  O   . LYS   B 1 367 ? 22.691  17.339  -24.654 1 42.04 ? 352 LYS   B O   1 
ATOM   5625 C  CB  . LYS   B 1 367 ? 20.736  17.471  -21.973 1 41.67 ? 352 LYS   B CB  1 
ATOM   5626 C  CG  . LYS   B 1 367 ? 21.898  18.418  -21.679 1 43.84 ? 352 LYS   B CG  1 
ATOM   5627 C  CD  . LYS   B 1 367 ? 21.917  18.943  -20.257 1 47.21 ? 352 LYS   B CD  1 
ATOM   5628 C  CE  . LYS   B 1 367 ? 23.239  19.625  -19.979 1 51.04 ? 352 LYS   B CE  1 
ATOM   5629 N  NZ  . LYS   B 1 367 ? 23.289  20.243  -18.63  1 52.62 ? 352 LYS   B NZ  1 
ATOM   5630 N  N   . TYR   B 1 368 ? 22.475  15.345  -23.594 1 41.04 ? 353 TYR   B N   1 
ATOM   5631 C  CA  . TYR   B 1 368 ? 23.817  14.861  -23.878 1 40.54 ? 353 TYR   B CA  1 
ATOM   5632 C  C   . TYR   B 1 368 ? 23.987  14.095  -25.162 1 40.13 ? 353 TYR   B C   1 
ATOM   5633 O  O   . TYR   B 1 368 ? 25.127  13.923  -25.597 1 40.06 ? 353 TYR   B O   1 
ATOM   5634 C  CB  . TYR   B 1 368 ? 24.333  14.03   -22.701 1 40.67 ? 353 TYR   B CB  1 
ATOM   5635 C  CG  . TYR   B 1 368 ? 24.675  14.896  -21.509 1 41.83 ? 353 TYR   B CG  1 
ATOM   5636 C  CD1 . TYR   B 1 368 ? 23.715  15.227  -20.567 1 42.39 ? 353 TYR   B CD1 1 
ATOM   5637 C  CD2 . TYR   B 1 368 ? 25.945  15.432  -21.358 1 42.79 ? 353 TYR   B CD2 1 
ATOM   5638 C  CE1 . TYR   B 1 368 ? 24.014  16.05   -19.494 1 43.59 ? 353 TYR   B CE1 1 
ATOM   5639 C  CE2 . TYR   B 1 368 ? 26.25   16.269  -20.298 1 43.7  ? 353 TYR   B CE2 1 
ATOM   5640 C  CZ  . TYR   B 1 368 ? 25.284  16.578  -19.367 1 44.44 ? 353 TYR   B CZ  1 
ATOM   5641 O  OH  . TYR   B 1 368 ? 25.598  17.408  -18.317 1 45.05 ? 353 TYR   B OH  1 
ATOM   5642 N  N   . ILE   B 1 369 ? 22.898  13.589  -25.754 1 39.93 ? 354 ILE   B N   1 
ATOM   5643 C  CA  . ILE   B 1 369 ? 23.004  12.824  -26.993 1 40.41 ? 354 ILE   B CA  1 
ATOM   5644 C  C   . ILE   B 1 369 ? 22.16   13.436  -28.109 1 41.97 ? 354 ILE   B C   1 
ATOM   5645 O  O   . ILE   B 1 369 ? 22.719  13.83   -29.12  1 42.47 ? 354 ILE   B O   1 
ATOM   5646 C  CB  . ILE   B 1 369 ? 22.726  11.296  -26.814 1 40.48 ? 354 ILE   B CB  1 
ATOM   5647 C  CG1 . ILE   B 1 369 ? 23.791  10.613  -25.924 1 42.08 ? 354 ILE   B CG1 1 
ATOM   5648 C  CG2 . ILE   B 1 369 ? 22.679  10.597  -28.164 1 40.22 ? 354 ILE   B CG2 1 
ATOM   5649 C  CD1 . ILE   B 1 369 ? 23.4    9.255   -25.473 1 43.33 ? 354 ILE   B CD1 1 
ATOM   5650 N  N   . LEU   B 1 370 ? 20.841  13.541  -27.918 1 42.4  ? 355 LEU   B N   1 
ATOM   5651 C  CA  . LEU   B 1 370 ? 19.904  14.018  -28.928 1 43.82 ? 355 LEU   B CA  1 
ATOM   5652 C  C   . LEU   B 1 370 ? 20.233  15.387  -29.529 1 44.99 ? 355 LEU   B C   1 
ATOM   5653 O  O   . LEU   B 1 370 ? 20.346  15.522  -30.752 1 44.94 ? 355 LEU   B O   1 
ATOM   5654 C  CB  . LEU   B 1 370 ? 18.484  14.014  -28.349 1 44.18 ? 355 LEU   B CB  1 
ATOM   5655 C  CG  . LEU   B 1 370 ? 17.402  13.505  -29.251 1 46.21 ? 355 LEU   B CG  1 
ATOM   5656 C  CD1 . LEU   B 1 370 ? 17.65   12.04   -29.657 1 46.84 ? 355 LEU   B CD1 1 
ATOM   5657 C  CD2 . LEU   B 1 370 ? 16.041  13.671  -28.584 1 46.85 ? 355 LEU   B CD2 1 
ATOM   5658 N  N   . ILE   B 1 371 ? 20.365  16.396  -28.673 1 45.8  ? 356 ILE   B N   1 
ATOM   5659 C  CA  . ILE   B 1 371 ? 20.667  17.747  -29.105 1 46.99 ? 356 ILE   B CA  1 
ATOM   5660 C  C   . ILE   B 1 371 ? 22.09   17.842  -29.708 1 48.89 ? 356 ILE   B C   1 
ATOM   5661 O  O   . ILE   B 1 371 ? 22.17   18.245  -30.87  1 49.46 ? 356 ILE   B O   1 
ATOM   5662 C  CB  . ILE   B 1 371 ? 20.371  18.737  -27.963 1 46.57 ? 356 ILE   B CB  1 
ATOM   5663 C  CG1 . ILE   B 1 371 ? 18.83   18.794  -27.733 1 46.47 ? 356 ILE   B CG1 1 
ATOM   5664 C  CG2 . ILE   B 1 371 ? 20.97   20.107  -28.264 1 46.7  ? 356 ILE   B CG2 1 
ATOM   5665 C  CD1 . ILE   B 1 371 ? 18.371  19.575  -26.575 1 46.39 ? 356 ILE   B CD1 1 
ATOM   5666 N  N   . PRO   B 1 372 ? 23.194  17.365  -29.065 1 49.62 ? 357 PRO   B N   1 
ATOM   5667 C  CA  . PRO   B 1 372 ? 24.502  17.389  -29.746 1 50.35 ? 357 PRO   B CA  1 
ATOM   5668 C  C   . PRO   B 1 372 ? 24.533  16.626  -31.074 1 51.8  ? 357 PRO   B C   1 
ATOM   5669 O  O   . PRO   B 1 372 ? 25.227  17.068  -31.983 1 52.66 ? 357 PRO   B O   1 
ATOM   5670 C  CB  . PRO   B 1 372 ? 25.444  16.75   -28.723 1 50.68 ? 357 PRO   B CB  1 
ATOM   5671 C  CG  . PRO   B 1 372 ? 24.804  16.994  -27.432 1 50.73 ? 357 PRO   B CG  1 
ATOM   5672 C  CD  . PRO   B 1 372 ? 23.34   16.821  -27.704 1 49.14 ? 357 PRO   B CD  1 
ATOM   5673 N  N   . ALA   B 1 373 ? 23.774  15.518  -31.216 1 52.2  ? 358 ALA   B N   1 
ATOM   5674 C  CA  . ALA   B 1 373 ? 23.706  14.793  -32.489 1 53.32 ? 358 ALA   B CA  1 
ATOM   5675 C  C   . ALA   B 1 373 ? 23.104  15.662  -33.601 1 54.86 ? 358 ALA   B C   1 
ATOM   5676 O  O   . ALA   B 1 373 ? 23.493  15.534  -34.763 1 55.35 ? 358 ALA   B O   1 
ATOM   5677 C  CB  . ALA   B 1 373 ? 22.895  13.516  -32.34  1 53.05 ? 358 ALA   B CB  1 
ATOM   5678 N  N   . SER   B 1 374 ? 22.178  16.553  -33.239 1 55.44 ? 359 SER   B N   1 
ATOM   5679 C  CA  . SER   B 1 374 ? 21.533  17.461  -34.175 1 56.7  ? 359 SER   B CA  1 
ATOM   5680 C  C   . SER   B 1 374 ? 22.453  18.625  -34.623 1 59.21 ? 359 SER   B C   1 
ATOM   5681 O  O   . SER   B 1 374 ? 22.18   19.247  -35.644 1 59.75 ? 359 SER   B O   1 
ATOM   5682 C  CB  . SER   B 1 374 ? 20.236  18.004  -33.577 1 55.8  ? 359 SER   B CB  1 
ATOM   5683 O  OG  . SER   B 1 374 ? 20.45   19.011  -32.604 1 55.34 ? 359 SER   B OG  1 
ATOM   5684 N  N   . GLN   B 1 375 ? 23.51   18.928  -33.857 1 60.49 ? 360 GLN   B N   1 
ATOM   5685 C  CA  . GLN   B 1 375 ? 24.437  20.015  -34.163 1 62.21 ? 360 GLN   B CA  1 
ATOM   5686 C  C   . GLN   B 1 375 ? 25.798  19.478  -34.683 1 63.67 ? 360 GLN   B C   1 
ATOM   5687 O  O   . GLN   B 1 375 ? 26.838  19.998  -34.299 1 63.82 ? 360 GLN   B O   1 
ATOM   5688 C  CB  . GLN   B 1 375 ? 24.659  20.888  -32.902 1 64.04 ? 360 GLN   B CB  1 
ATOM   5689 C  CG  . GLN   B 1 375 ? 23.4    21.38   -32.211 1 67.24 ? 360 GLN   B CG  1 
ATOM   5690 C  CD  . GLN   B 1 375 ? 23.679  21.824  -30.79  1 72.45 ? 360 GLN   B CD  1 
ATOM   5691 O  OE1 . GLN   B 1 375 ? 24.519  21.259  -30.075 1 74.07 ? 360 GLN   B OE1 1 
ATOM   5692 N  NE2 . GLN   B 1 375 ? 22.971  22.845  -30.339 1 73.58 ? 360 GLN   B NE2 1 
ATOM   5693 N  N   . GLN   B 1 376 ? 25.805  18.46   -35.555 1 64.75 ? 361 GLN   B N   1 
ATOM   5694 C  CA  . GLN   B 1 376 ? 27.06   17.876  -36.046 1 65.89 ? 361 GLN   B CA  1 
ATOM   5695 C  C   . GLN   B 1 376 ? 27.223  17.933  -37.576 1 67.21 ? 361 GLN   B C   1 
ATOM   5696 O  O   . GLN   B 1 376 ? 28.307  18.262  -38.086 1 67.71 ? 361 GLN   B O   1 
ATOM   5697 C  CB  . GLN   B 1 376 ? 27.205  16.44   -35.523 1 67.01 ? 361 GLN   B CB  1 
ATOM   5698 N  N   . THR   B 1 397 ? 18.027  8.323   -31.685 1 50.71 ? 382 THR   B N   1 
ATOM   5699 C  CA  . THR   B 1 397 ? 16.587  8.169   -31.581 1 51.06 ? 382 THR   B CA  1 
ATOM   5700 C  C   . THR   B 1 397 ? 16.2    6.701   -31.268 1 51.65 ? 382 THR   B C   1 
ATOM   5701 O  O   . THR   B 1 397 ? 15.198  6.466   -30.584 1 52.15 ? 382 THR   B O   1 
ATOM   5702 C  CB  . THR   B 1 397 ? 15.891  8.76    -32.812 1 52.2  ? 382 THR   B CB  1 
ATOM   5703 N  N   . ASP   B 1 398 ? 17.005  5.725   -31.721 1 51.21 ? 383 ASP   B N   1 
ATOM   5704 C  CA  . ASP   B 1 398 ? 16.757  4.317   -31.414 1 51.36 ? 383 ASP   B CA  1 
ATOM   5705 C  C   . ASP   B 1 398 ? 17.032  4.052   -29.922 1 51.51 ? 383 ASP   B C   1 
ATOM   5706 O  O   . ASP   B 1 398 ? 16.353  3.201   -29.327 1 52.43 ? 383 ASP   B O   1 
ATOM   5707 C  CB  . ASP   B 1 398 ? 17.601  3.397   -32.304 1 52.63 ? 383 ASP   B CB  1 
ATOM   5708 N  N   . LEU   B 1 399 ? 18.02   4.785   -29.319 1 50.14 ? 384 LEU   B N   1 
ATOM   5709 C  CA  . LEU   B 1 399 ? 18.354  4.703   -27.898 1 49.47 ? 384 LEU   B CA  1 
ATOM   5710 C  C   . LEU   B 1 399 ? 17.209  5.302   -27.078 1 49.02 ? 384 LEU   B C   1 
ATOM   5711 O  O   . LEU   B 1 399 ? 16.882  4.781   -26.019 1 49.44 ? 384 LEU   B O   1 
ATOM   5712 C  CB  . LEU   B 1 399 ? 19.657  5.467   -27.564 1 49.28 ? 384 LEU   B CB  1 
ATOM   5713 C  CG  . LEU   B 1 399 ? 20.924  5.153   -28.36  1 50.36 ? 384 LEU   B CG  1 
ATOM   5714 C  CD1 . LEU   B 1 399 ? 21.965  6.249   -28.18  1 50    ? 384 LEU   B CD1 1 
ATOM   5715 C  CD2 . LEU   B 1 399 ? 21.515  3.8     -27.961 1 50.94 ? 384 LEU   B CD2 1 
ATOM   5716 N  N   . MET   B 1 400 ? 16.603  6.399   -27.56  1 48.36 ? 385 MET   B N   1 
ATOM   5717 C  CA  . MET   B 1 400 ? 15.476  7.044   -26.885 1 47.66 ? 385 MET   B CA  1 
ATOM   5718 C  C   . MET   B 1 400 ? 14.293  6.09    -26.817 1 46.62 ? 385 MET   B C   1 
ATOM   5719 O  O   . MET   B 1 400 ? 13.669  5.969   -25.773 1 46.08 ? 385 MET   B O   1 
ATOM   5720 C  CB  . MET   B 1 400 ? 15.05   8.336   -27.61  1 47.98 ? 385 MET   B CB  1 
ATOM   5721 C  CG  . MET   B 1 400 ? 16.074  9.423   -27.57  1 49.79 ? 385 MET   B CG  1 
ATOM   5722 S  SD  . MET   B 1 400 ? 16.501  9.947   -25.923 1 52.71 ? 385 MET   B SD  1 
ATOM   5723 C  CE  . MET   B 1 400 ? 15.04   10.717  -25.424 1 51.43 ? 385 MET   B CE  1 
ATOM   5724 N  N   . ASN   B 1 401 ? 14.02   5.386   -27.922 1 45.67 ? 386 ASN   B N   1 
ATOM   5725 C  CA  . ASN   B 1 401 ? 12.93   4.424   -27.993 1 45.34 ? 386 ASN   B CA  1 
ATOM   5726 C  C   . ASN   B 1 401 ? 13.139  3.278   -27.025 1 43.52 ? 386 ASN   B C   1 
ATOM   5727 O  O   . ASN   B 1 401 ? 12.18   2.79    -26.429 1 43.98 ? 386 ASN   B O   1 
ATOM   5728 C  CB  . ASN   B 1 401 ? 12.776  3.888   -29.42  1 47.8  ? 386 ASN   B CB  1 
ATOM   5729 C  CG  . ASN   B 1 401 ? 12.2    4.912   -30.359 1 52.81 ? 386 ASN   B CG  1 
ATOM   5730 O  OD1 . ASN   B 1 401 ? 11.504  5.855   -29.948 1 53.47 ? 386 ASN   B OD1 1 
ATOM   5731 N  ND2 . ASN   B 1 401 ? 12.502  4.76    -31.639 1 55.19 ? 386 ASN   B ND2 1 
ATOM   5732 N  N   . PHE   B 1 402 ? 14.388  2.844   -26.859 1 41.82 ? 387 PHE   B N   1 
ATOM   5733 C  CA  . PHE   B 1 402 ? 14.734  1.779   -25.931 1 40.2  ? 387 PHE   B CA  1 
ATOM   5734 C  C   . PHE   B 1 402 ? 14.43   2.274   -24.508 1 39.63 ? 387 PHE   B C   1 
ATOM   5735 O  O   . PHE   B 1 402 ? 13.701  1.615   -23.774 1 39.76 ? 387 PHE   B O   1 
ATOM   5736 C  CB  . PHE   B 1 402 ? 16.233  1.383   -26.079 1 38.9  ? 387 PHE   B CB  1 
ATOM   5737 C  CG  . PHE   B 1 402 ? 16.745  0.574   -24.911 1 38.31 ? 387 PHE   B CG  1 
ATOM   5738 C  CD1 . PHE   B 1 402 ? 16.318  -0.737  -24.71  1 38.43 ? 387 PHE   B CD1 1 
ATOM   5739 C  CD2 . PHE   B 1 402 ? 17.581  1.147   -23.965 1 37.96 ? 387 PHE   B CD2 1 
ATOM   5740 C  CE1 . PHE   B 1 402 ? 16.745  -1.459  -23.593 1 38.57 ? 387 PHE   B CE1 1 
ATOM   5741 C  CE2 . PHE   B 1 402 ? 17.995  0.426   -22.851 1 38.28 ? 387 PHE   B CE2 1 
ATOM   5742 C  CZ  . PHE   B 1 402 ? 17.571  -0.868  -22.669 1 38    ? 387 PHE   B CZ  1 
ATOM   5743 N  N   . LEU   B 1 403 ? 14.921  3.467   -24.163 1 38.78 ? 388 LEU   B N   1 
ATOM   5744 C  CA  . LEU   B 1 403 ? 14.716  4.02    -22.836 1 38.89 ? 388 LEU   B CA  1 
ATOM   5745 C  C   . LEU   B 1 403 ? 13.238  4.297   -22.527 1 39.18 ? 388 LEU   B C   1 
ATOM   5746 O  O   . LEU   B 1 403 ? 12.804  4.095   -21.395 1 39.46 ? 388 LEU   B O   1 
ATOM   5747 C  CB  . LEU   B 1 403 ? 15.579  5.27    -22.661 1 39.02 ? 388 LEU   B CB  1 
ATOM   5748 C  CG  . LEU   B 1 403 ? 17.089  5.031   -22.703 1 39.99 ? 388 LEU   B CG  1 
ATOM   5749 C  CD1 . LEU   B 1 403 ? 17.852  6.355   -22.761 1 39.98 ? 388 LEU   B CD1 1 
ATOM   5750 C  CD2 . LEU   B 1 403 ? 17.541  4.167   -21.517 1 39.81 ? 388 LEU   B CD2 1 
ATOM   5751 N  N   . LYS   B 1 404 ? 12.466  4.734   -23.533 1 38.95 ? 389 LYS   B N   1 
ATOM   5752 C  CA  . LYS   B 1 404 ? 11.039  4.999   -23.389 1 39.32 ? 389 LYS   B CA  1 
ATOM   5753 C  C   . LYS   B 1 404 ? 10.254  3.694   -23.193 1 40.06 ? 389 LYS   B C   1 
ATOM   5754 O  O   . LYS   B 1 404 ? 9.26    3.695   -22.478 1 40.16 ? 389 LYS   B O   1 
ATOM   5755 C  CB  . LYS   B 1 404 ? 10.495  5.752   -24.601 1 40.1  ? 389 LYS   B CB  1 
ATOM   5756 C  CG  . LYS   B 1 404 ? 10.852  7.227   -24.639 1 42.63 ? 389 LYS   B CG  1 
ATOM   5757 C  CD  . LYS   B 1 404 ? 10.512  7.694   -26.038 1 45.1  ? 389 LYS   B CD  1 
ATOM   5758 C  CE  . LYS   B 1 404 ? 10.645  9.14    -26.319 1 44.81 ? 389 LYS   B CE  1 
ATOM   5759 N  NZ  . LYS   B 1 404 ? 10.977  9.33    -27.736 1 44.9  ? 389 LYS   B NZ  1 
ATOM   5760 N  N   . THR   B 1 405 ? 10.705  2.585   -23.806 1 40.04 ? 390 THR   B N   1 
ATOM   5761 C  CA  . THR   B 1 405 ? 10.058  1.292   -23.632 1 40.4  ? 390 THR   B CA  1 
ATOM   5762 C  C   . THR   B 1 405 ? 10.269  0.806   -22.202 1 41.2  ? 390 THR   B C   1 
ATOM   5763 O  O   . THR   B 1 405 ? 9.303   0.411   -21.543 1 42.67 ? 390 THR   B O   1 
ATOM   5764 C  CB  . THR   B 1 405 ? 10.608  0.278   -24.648 1 41.51 ? 390 THR   B CB  1 
ATOM   5765 O  OG1 . THR   B 1 405 ? 10.281  0.702   -25.974 1 42.26 ? 390 THR   B OG1 1 
ATOM   5766 C  CG2 . THR   B 1 405 ? 10.08   -1.125  -24.4   1 41.77 ? 390 THR   B CG2 1 
ATOM   5767 N  N   . VAL   B 1 406 ? 11.516  0.876   -21.7   1 40.28 ? 391 VAL   B N   1 
ATOM   5768 C  CA  . VAL   B 1 406 ? 11.851  0.475   -20.338 1 40.44 ? 391 VAL   B CA  1 
ATOM   5769 C  C   . VAL   B 1 406 ? 11.071  1.312   -19.332 1 40.76 ? 391 VAL   B C   1 
ATOM   5770 O  O   . VAL   B 1 406 ? 10.548  0.773   -18.365 1 41.89 ? 391 VAL   B O   1 
ATOM   5771 C  CB  . VAL   B 1 406 ? 13.381  0.566   -20.091 1 40.96 ? 391 VAL   B CB  1 
ATOM   5772 C  CG1 . VAL   B 1 406 ? 13.73   0.211   -18.654 1 41.31 ? 391 VAL   B CG1 1 
ATOM   5773 C  CG2 . VAL   B 1 406 ? 14.141  -0.334  -21.064 1 41.53 ? 391 VAL   B CG2 1 
ATOM   5774 N  N   . ARG   B 1 407 ? 10.965  2.613   -19.573 1 40.24 ? 392 ARG   B N   1 
ATOM   5775 C  CA  . ARG   B 1 407 ? 10.233  3.505   -18.688 1 40.85 ? 392 ARG   B CA  1 
ATOM   5776 C  C   . ARG   B 1 407 ? 8.724   3.184   -18.703 1 41.4  ? 392 ARG   B C   1 
ATOM   5777 O  O   . ARG   B 1 407 ? 8.096   3.163   -17.65  1 41.53 ? 392 ARG   B O   1 
ATOM   5778 C  CB  . ARG   B 1 407 ? 10.486  4.991   -19.047 1 41.5  ? 392 ARG   B CB  1 
ATOM   5779 C  CG  . ARG   B 1 407 ? 9.688   5.876   -18.124 1 44.49 ? 392 ARG   B CG  1 
ATOM   5780 C  CD  . ARG   B 1 407 ? 9.639   7.317   -18.443 1 47.72 ? 392 ARG   B CD  1 
ATOM   5781 N  NE  . ARG   B 1 407 ? 9.097   7.73    -19.737 1 48.7  ? 392 ARG   B NE  1 
ATOM   5782 C  CZ  . ARG   B 1 407 ? 8.922   9.01    -20.068 1 49.82 ? 392 ARG   B CZ  1 
ATOM   5783 N  NH1 . ARG   B 1 407 ? 9.178   9.973   -19.187 1 49.33 ? 392 ARG   B NH1 1 
ATOM   5784 N  NH2 . ARG   B 1 407 ? 8.472   9.335   -21.272 1 48.63 ? 392 ARG   B NH2 1 
ATOM   5785 N  N   . SER   B 1 408 ? 8.165   2.947   -19.892 1 41.83 ? 393 SER   B N   1 
ATOM   5786 C  CA  . SER   B 1 408 ? 6.753   2.624   -20.104 1 42.89 ? 393 SER   B CA  1 
ATOM   5787 C  C   . SER   B 1 408 ? 6.374   1.337   -19.368 1 42.69 ? 393 SER   B C   1 
ATOM   5788 O  O   . SER   B 1 408 ? 5.334   1.296   -18.717 1 42.49 ? 393 SER   B O   1 
ATOM   5789 C  CB  . SER   B 1 408 ? 6.46    2.494   -21.596 1 44.9  ? 393 SER   B CB  1 
ATOM   5790 O  OG  . SER   B 1 408 ? 5.097   2.171   -21.801 1 49.26 ? 393 SER   B OG  1 
ATOM   5791 N  N   . THR   B 1 409 ? 7.248   0.316   -19.429 1 42.46 ? 394 THR   B N   1 
ATOM   5792 C  CA  . THR   B 1 409 ? 7.09    -0.951  -18.73  1 42.75 ? 394 THR   B CA  1 
ATOM   5793 C  C   . THR   B 1 409 ? 7.054   -0.708  -17.201 1 44.4  ? 394 THR   B C   1 
ATOM   5794 O  O   . THR   B 1 409 ? 6.262   -1.326  -16.484 1 45.07 ? 394 THR   B O   1 
ATOM   5795 C  CB  . THR   B 1 409 ? 8.223   -1.887  -19.14  1 42.65 ? 394 THR   B CB  1 
ATOM   5796 O  OG1 . THR   B 1 409 ? 8.182   -2.091  -20.552 1 42.71 ? 394 THR   B OG1 1 
ATOM   5797 C  CG2 . THR   B 1 409 ? 8.186   -3.225  -18.411 1 42.39 ? 394 THR   B CG2 1 
ATOM   5798 N  N   . THR   B 1 410 ? 7.892   0.209   -16.711 1 44.65 ? 395 THR   B N   1 
ATOM   5799 C  CA  . THR   B 1 410 ? 7.912   0.549   -15.292 1 45.19 ? 395 THR   B CA  1 
ATOM   5800 C  C   . THR   B 1 410 ? 6.591   1.217   -14.907 1 47.58 ? 395 THR   B C   1 
ATOM   5801 O  O   . THR   B 1 410 ? 5.997   0.854   -13.906 1 48.16 ? 395 THR   B O   1 
ATOM   5802 C  CB  . THR   B 1 410 ? 9.125   1.435   -14.939 1 44.04 ? 395 THR   B CB  1 
ATOM   5803 O  OG1 . THR   B 1 410 ? 10.295  0.943   -15.602 1 44.66 ? 395 THR   B OG1 1 
ATOM   5804 C  CG2 . THR   B 1 410 ? 9.372   1.501   -13.457 1 42.64 ? 395 THR   B CG2 1 
ATOM   5805 N  N   . GLU   B 1 411 ? 6.133   2.186   -15.703 1 48.72 ? 396 GLU   B N   1 
ATOM   5806 C  CA  . GLU   B 1 411 ? 4.89    2.937   -15.472 1 50.26 ? 396 GLU   B CA  1 
ATOM   5807 C  C   . GLU   B 1 411 ? 3.675   1.986   -15.442 1 50.39 ? 396 GLU   B C   1 
ATOM   5808 O  O   . GLU   B 1 411 ? 2.826   2.104   -14.563 1 50.33 ? 396 GLU   B O   1 
ATOM   5809 C  CB  . GLU   B 1 411 ? 4.703   3.988   -16.591 1 53.89 ? 396 GLU   B CB  1 
ATOM   5810 C  CG  . GLU   B 1 411 ? 4.786   5.456   -16.186 1 61.69 ? 396 GLU   B CG  1 
ATOM   5811 C  CD  . GLU   B 1 411 ? 5.123   6.409   -17.331 1 70.78 ? 396 GLU   B CD  1 
ATOM   5812 O  OE1 . GLU   B 1 411 ? 5.382   5.933   -18.463 1 70.19 ? 396 GLU   B OE1 1 
ATOM   5813 O  OE2 . GLU   B 1 411 ? 5.146   7.64    -17.085 1 74.42 ? 396 GLU   B OE2 1 
ATOM   5814 N  N   . LYS   B 1 412 ? 3.62    1.025   -16.38  1 50.25 ? 397 LYS   B N   1 
ATOM   5815 C  CA  . LYS   B 1 412 ? 2.531   0.05    -16.461 1 50.6  ? 397 LYS   B CA  1 
ATOM   5816 C  C   . LYS   B 1 412 ? 2.497   -0.975  -15.309 1 51.45 ? 397 LYS   B C   1 
ATOM   5817 O  O   . LYS   B 1 412 ? 1.601   -1.823  -15.26  1 52.14 ? 397 LYS   B O   1 
ATOM   5818 C  CB  . LYS   B 1 412 ? 2.546   -0.663  -17.813 1 51.93 ? 397 LYS   B CB  1 
ATOM   5819 C  CG  . LYS   B 1 412 ? 2.188   0.252   -18.966 1 56.28 ? 397 LYS   B CG  1 
ATOM   5820 C  CD  . LYS   B 1 412 ? 2.022   -0.515  -20.283 1 60.43 ? 397 LYS   B CD  1 
ATOM   5821 C  CE  . LYS   B 1 412 ? 3.299   -0.861  -21.016 1 64.01 ? 397 LYS   B CE  1 
ATOM   5822 N  NZ  . LYS   B 1 412 ? 3.275   -0.344  -22.415 1 66.14 ? 397 LYS   B NZ  1 
ATOM   5823 N  N   . SER   B 1 413 ? 3.468   -0.924  -14.406 1 51.02 ? 398 SER   B N   1 
ATOM   5824 C  CA  . SER   B 1 413 ? 3.507   -1.803  -13.245 1 51.15 ? 398 SER   B CA  1 
ATOM   5825 C  C   . SER   B 1 413 ? 2.826   -1.187  -12.025 1 52.23 ? 398 SER   B C   1 
ATOM   5826 O  O   . SER   B 1 413 ? 2.649   -1.88   -11.024 1 52.18 ? 398 SER   B O   1 
ATOM   5827 C  CB  . SER   B 1 413 ? 4.941   -2.168  -12.902 1 51.46 ? 398 SER   B CB  1 
ATOM   5828 O  OG  . SER   B 1 413 ? 5.375   -3.106  -13.866 1 54.8  ? 398 SER   B OG  1 
ATOM   5829 N  N   . LEU   B 1 414 ? 2.444   0.109   -12.083 1 52.86 ? 399 LEU   B N   1 
ATOM   5830 C  CA  . LEU   B 1 414 ? 1.745   0.743   -10.984 1 54.49 ? 399 LEU   B CA  1 
ATOM   5831 C  C   . LEU   B 1 414 ? 0.383   0.053   -10.816 1 56.56 ? 399 LEU   B C   1 
ATOM   5832 O  O   . LEU   B 1 414 ? -0.272  -0.285  -11.804 1 56.63 ? 399 LEU   B O   1 
ATOM   5833 C  CB  . LEU   B 1 414 ? 1.56    2.238   -11.259 1 54.59 ? 399 LEU   B CB  1 
ATOM   5834 C  CG  . LEU   B 1 414 ? 2.826   3.084   -11.182 1 56.03 ? 399 LEU   B CG  1 
ATOM   5835 C  CD1 . LEU   B 1 414 ? 2.62    4.434   -11.832 1 56.44 ? 399 LEU   B CD1 1 
ATOM   5836 C  CD2 . LEU   B 1 414 ? 3.299   3.243   -9.75   1 56.38 ? 399 LEU   B CD2 1 
ATOM   5837 N  N   . LEU   B 1 415 ? 0.043   -0.281  -9.58   1 57.76 ? 400 LEU   B N   1 
ATOM   5838 C  CA  . LEU   B 1 415 ? -1.215  -0.946  -9.274  1 59.21 ? 400 LEU   B CA  1 
ATOM   5839 C  C   . LEU   B 1 415 ? -2.375  0.067   -9.313  1 61.38 ? 400 LEU   B C   1 
ATOM   5840 O  O   . LEU   B 1 415 ? -3.487  -0.31   -9.691  1 61.93 ? 400 LEU   B O   1 
ATOM   5841 C  CB  . LEU   B 1 415 ? -1.132  -1.614  -7.893  1 58.86 ? 400 LEU   B CB  1 
ATOM   5842 C  CG  . LEU   B 1 415 ? 0.058   -2.536  -7.662  1 59.43 ? 400 LEU   B CG  1 
ATOM   5843 C  CD1 . LEU   B 1 415 ? 0.042   -3.076  -6.265  1 59.66 ? 400 LEU   B CD1 1 
ATOM   5844 C  CD2 . LEU   B 1 415 ? 0.085   -3.658  -8.659  1 59.73 ? 400 LEU   B CD2 1 
ATOM   5845 N  N   . LYS   B 1 416 ? -2.097  1.357   -8.925  1 62.45 ? 401 LYS   B N   1 
ATOM   5846 C  CA  . LYS   B 1 416 ? -2.993  2.531   -8.861  1 63.54 ? 401 LYS   B CA  1 
ATOM   5847 C  C   . LYS   B 1 416 ? -4.168  2.332   -7.891  1 64.76 ? 401 LYS   B C   1 
ATOM   5848 O  O   . LYS   B 1 416 ? -4.045  1.617   -6.888  1 65.43 ? 401 LYS   B O   1 
ATOM   5849 C  CB  . LYS   B 1 416 ? -3.477  2.986   -10.255 1 65.04 ? 401 LYS   B CB  1 
HETATM 5850 C  CHA . HEM   C 2 .   ? 16.297  -29.842 -32.064 1 35.05 ? 501 HEM   A CHA 1 
HETATM 5851 C  CHB . HEM   C 2 .   ? 13.934  -32.073 -35.646 1 34.77 ? 501 HEM   A CHB 1 
HETATM 5852 C  CHC . HEM   C 2 .   ? 13.001  -35.838 -32.789 1 33.02 ? 501 HEM   A CHC 1 
HETATM 5853 C  CHD . HEM   C 2 .   ? 15.121  -33.501 -29.094 1 33.46 ? 501 HEM   A CHD 1 
HETATM 5854 C  C1A . HEM   C 2 .   ? 15.697  -30.103 -33.312 1 35.83 ? 501 HEM   A C1A 1 
HETATM 5855 C  C2A . HEM   C 2 .   ? 15.726  -29.196 -34.446 1 36.1  ? 501 HEM   A C2A 1 
HETATM 5856 C  C3A . HEM   C 2 .   ? 15.019  -29.816 -35.461 1 35.32 ? 501 HEM   A C3A 1 
HETATM 5857 C  C4A . HEM   C 2 .   ? 14.592  -31.103 -34.934 1 35.27 ? 501 HEM   A C4A 1 
HETATM 5858 C  CMA . HEM   C 2 .   ? 14.704  -29.297 -36.831 1 34.42 ? 501 HEM   A CMA 1 
HETATM 5859 C  CAA . HEM   C 2 .   ? 16.438  -27.873 -34.502 1 37.41 ? 501 HEM   A CAA 1 
HETATM 5860 C  CBA . HEM   C 2 .   ? 15.762  -26.783 -33.665 1 38.37 ? 501 HEM   A CBA 1 
HETATM 5861 C  CGA . HEM   C 2 .   ? 14.462  -26.284 -34.226 1 39.32 ? 501 HEM   A CGA 1 
HETATM 5862 O  O1A . HEM   C 2 .   ? 13.532  -25.949 -33.526 1 40.13 ? 501 HEM   A O1A 1 
HETATM 5863 O  O2A . HEM   C 2 .   ? 14.416  -26.231 -35.524 1 39.72 ? 501 HEM   A O2A 1 
HETATM 5864 C  C1B . HEM   C 2 .   ? 13.55   -33.354 -35.216 1 34.48 ? 501 HEM   A C1B 1 
HETATM 5865 C  C2B . HEM   C 2 .   ? 12.915  -34.341 -36.069 1 34.29 ? 501 HEM   A C2B 1 
HETATM 5866 C  C3B . HEM   C 2 .   ? 12.621  -35.403 -35.229 1 34    ? 501 HEM   A C3B 1 
HETATM 5867 C  C4B . HEM   C 2 .   ? 13.108  -35.07  -33.919 1 33.54 ? 501 HEM   A C4B 1 
HETATM 5868 C  CMB . HEM   C 2 .   ? 12.719  -34.206 -37.55  1 33.94 ? 501 HEM   A CMB 1 
HETATM 5869 C  CAB . HEM   C 2 .   ? 11.896  -36.63  -35.579 1 33.95 ? 501 HEM   A CAB 1 
HETATM 5870 C  CBB . HEM   C 2 .   ? 10.801  -36.772 -36.296 1 33.64 ? 501 HEM   A CBB 1 
HETATM 5871 C  C1C . HEM   C 2 .   ? 13.449  -35.514 -31.484 1 32.8  ? 501 HEM   A C1C 1 
HETATM 5872 C  C2C . HEM   C 2 .   ? 13.113  -36.268 -30.291 1 31.72 ? 501 HEM   A C2C 1 
HETATM 5873 C  C3C . HEM   C 2 .   ? 13.668  -35.564 -29.246 1 32.21 ? 501 HEM   A C3C 1 
HETATM 5874 C  C4C . HEM   C 2 .   ? 14.354  -34.427 -29.795 1 33.3  ? 501 HEM   A C4C 1 
HETATM 5875 C  CMC . HEM   C 2 .   ? 12.35   -37.558 -30.267 1 31.01 ? 501 HEM   A CMC 1 
HETATM 5876 C  CAC . HEM   C 2 .   ? 13.546  -35.894 -27.824 1 32.36 ? 501 HEM   A CAC 1 
HETATM 5877 C  CBC . HEM   C 2 .   ? 13.121  -35.147 -26.813 1 32.52 ? 501 HEM   A CBC 1 
HETATM 5878 C  C1D . HEM   C 2 .   ? 15.753  -32.341 -29.613 1 33.65 ? 501 HEM   A C1D 1 
HETATM 5879 C  C2D . HEM   C 2 .   ? 16.563  -31.424 -28.835 1 33.58 ? 501 HEM   A C2D 1 
HETATM 5880 C  C3D . HEM   C 2 .   ? 16.888  -30.382 -29.681 1 34.1  ? 501 HEM   A C3D 1 
HETATM 5881 C  C4D . HEM   C 2 .   ? 16.268  -30.68  -30.957 1 34.55 ? 501 HEM   A C4D 1 
HETATM 5882 C  CMD . HEM   C 2 .   ? 16.9    -31.577 -27.383 1 33.33 ? 501 HEM   A CMD 1 
HETATM 5883 C  CAD . HEM   C 2 .   ? 17.673  -29.141 -29.352 1 34.13 ? 501 HEM   A CAD 1 
HETATM 5884 C  CBD . HEM   C 2 .   ? 19.111  -29.184 -29.864 1 34.77 ? 501 HEM   A CBD 1 
HETATM 5885 C  CGD . HEM   C 2 .   ? 20.02   -30.109 -29.1   1 36.01 ? 501 HEM   A CGD 1 
HETATM 5886 O  O1D . HEM   C 2 .   ? 20.706  -30.971 -29.639 1 36.64 ? 501 HEM   A O1D 1 
HETATM 5887 O  O2D . HEM   C 2 .   ? 20.034  -29.895 -27.813 1 36.26 ? 501 HEM   A O2D 1 
HETATM 5888 N  NA  . HEM   C 2 .   ? 15.015  -31.241 -33.628 1 35.43 ? 501 HEM   A NA  1 
HETATM 5889 N  NB  . HEM   C 2 .   ? 13.675  -33.813 -33.942 1 34.47 ? 501 HEM   A NB  1 
HETATM 5890 N  NC  . HEM   C 2 .   ? 14.192  -34.42  -31.175 1 34.02 ? 501 HEM   A NC  1 
HETATM 5891 N  ND  . HEM   C 2 .   ? 15.594  -31.889 -30.88  1 34.61 ? 501 HEM   A ND  1 
HETATM 5892 FE FE  . HEM   C 2 .   ? 14.64   -32.845 -32.413 1 35.74 ? 501 HEM   A FE  1 
HETATM 5893 N  N1  . A1H6T D 3 .   ? 10.821  -29.834 -36.322 1 42.06 ? 502 A1H6T A N1  1 
HETATM 5894 N  N3  . A1H6T D 3 .   ? 11.139  -30.86  -31.913 1 35.02 ? 502 A1H6T A N3  1 
HETATM 5895 C  C4  . A1H6T D 3 .   ? 10.853  -28.589 -32.928 1 36.66 ? 502 A1H6T A C4  1 
HETATM 5896 C  C5  . A1H6T D 3 .   ? 10.86   -28.77  -34.418 1 39.75 ? 502 A1H6T A C5  1 
HETATM 5897 C  C6  . A1H6T D 3 .   ? 10.884  -27.816 -35.392 1 41.68 ? 502 A1H6T A C6  1 
HETATM 5898 C  C7  . A1H6T D 3 .   ? 10.762  -27.992 -37.887 1 46.54 ? 502 A1H6T A C7  1 
HETATM 5899 C  C8  . A1H6T D 3 .   ? 11.065  -28.811 -38.962 1 47.25 ? 502 A1H6T A C8  1 
HETATM 5900 C  C10 . A1H6T D 3 .   ? 10.865  -26.93  -40.448 1 48.99 ? 502 A1H6T A C10 1 
HETATM 5901 C  C13 . A1H6T D 3 .   ? 10.731  -31.928 -31.106 1 34.67 ? 502 A1H6T A C13 1 
HETATM 5902 C  C15 . A1H6T D 3 .   ? 12.371  -31.188 -32.408 1 34.64 ? 502 A1H6T A C15 1 
HETATM 5903 CL CL  . A1H6T D 3 .   ? 7.936   -28.463 -31.773 1 36.54 ? 502 A1H6T A CL  1 
HETATM 5904 C  C   . A1H6T D 3 .   ? 9.081   -29.738 -31.515 1 35.9  ? 502 A1H6T A C   1 
HETATM 5905 C  C3  . A1H6T D 3 .   ? 10.308  -29.746 -32.125 1 35.88 ? 502 A1H6T A C3  1 
HETATM 5906 N  N4  . A1H6T D 3 .   ? 12.777  -32.368 -31.991 1 34.54 ? 502 A1H6T A N4  1 
HETATM 5907 C  C14 . A1H6T D 3 .   ? 11.765  -32.833 -31.182 1 34.5  ? 502 A1H6T A C14 1 
HETATM 5908 C  C2  . A1H6T D 3 .   ? 9.452   -31.865 -30.493 1 34.8  ? 502 A1H6T A C2  1 
HETATM 5909 C  C1  . A1H6T D 3 .   ? 8.652   -30.803 -30.69  1 35.23 ? 502 A1H6T A C1  1 
HETATM 5910 O  O   . A1H6T D 3 .   ? 12.15   -28.26  -32.541 1 34.83 ? 502 A1H6T A O   1 
HETATM 5911 N  N2  . A1H6T D 3 .   ? 10.854  -28.5   -36.555 1 43.42 ? 502 A1H6T A N2  1 
HETATM 5912 N  N   . A1H6T D 3 .   ? 10.823  -29.996 -35.019 1 40.81 ? 502 A1H6T A N   1 
HETATM 5913 C  C12 . A1H6T D 3 .   ? 10.497  -26.634 -38.092 1 48.42 ? 502 A1H6T A C12 1 
HETATM 5914 C  C11 . A1H6T D 3 .   ? 10.553  -26.113 -39.376 1 49.11 ? 502 A1H6T A C11 1 
HETATM 5915 C  C9  . A1H6T D 3 .   ? 11.119  -28.274 -40.24  1 48.16 ? 502 A1H6T A C9  1 
HETATM 5916 C  CHA . HEM   E 2 .   ? 20.934  3.337   -20.277 1 37.29 ? 501 HEM   B CHA 1 
HETATM 5917 C  CHB . HEM   E 2 .   ? 23.014  7.463   -21.735 1 38.11 ? 501 HEM   B CHB 1 
HETATM 5918 C  CHC . HEM   E 2 .   ? 23.809  8.779   -17.149 1 36.55 ? 501 HEM   B CHC 1 
HETATM 5919 C  CHD . HEM   E 2 .   ? 21.963  4.519   -15.705 1 36.26 ? 501 HEM   B CHD 1 
HETATM 5920 C  C1A . HEM   E 2 .   ? 21.462  4.358   -21.11  1 37.9  ? 501 HEM   B C1A 1 
HETATM 5921 C  C2A . HEM   E 2 .   ? 21.434  4.343   -22.564 1 38.32 ? 501 HEM   B C2A 1 
HETATM 5922 C  C3A . HEM   E 2 .   ? 22.05   5.507   -22.98  1 38.15 ? 501 HEM   B C3A 1 
HETATM 5923 C  C4A . HEM   E 2 .   ? 22.423  6.223   -21.775 1 38.11 ? 501 HEM   B C4A 1 
HETATM 5924 C  CMA . HEM   E 2 .   ? 22.383  5.936   -24.376 1 37.96 ? 501 HEM   B CMA 1 
HETATM 5925 C  CAA . HEM   E 2 .   ? 20.86   3.262   -23.441 1 38.96 ? 501 HEM   B CAA 1 
HETATM 5926 C  CBA . HEM   E 2 .   ? 21.651  1.949   -23.398 1 40.03 ? 501 HEM   B CBA 1 
HETATM 5927 C  CGA . HEM   E 2 .   ? 22.947  2.003   -24.157 1 41.19 ? 501 HEM   B CGA 1 
HETATM 5928 O  O1A . HEM   E 2 .   ? 23.072  2.603   -25.21  1 42.23 ? 501 HEM   B O1A 1 
HETATM 5929 O  O2A . HEM   E 2 .   ? 23.931  1.369   -23.578 1 41.06 ? 501 HEM   B O2A 1 
HETATM 5930 C  C1B . HEM   E 2 .   ? 23.33   8.243   -20.618 1 37.95 ? 501 HEM   B C1B 1 
HETATM 5931 C  C2B . HEM   E 2 .   ? 23.901  9.575   -20.691 1 38.17 ? 501 HEM   B C2B 1 
HETATM 5932 C  C3B . HEM   E 2 .   ? 24.152  9.93    -19.378 1 38.23 ? 501 HEM   B C3B 1 
HETATM 5933 C  C4B . HEM   E 2 .   ? 23.711  8.85    -18.532 1 37.51 ? 501 HEM   B C4B 1 
HETATM 5934 C  CMB . HEM   E 2 .   ? 24.075  10.373  -21.95  1 38.1  ? 501 HEM   B CMB 1 
HETATM 5935 C  CAB . HEM   E 2 .   ? 24.776  11.169  -18.906 1 38.46 ? 501 HEM   B CAB 1 
HETATM 5936 C  CBB . HEM   E 2 .   ? 25.82   11.805  -19.391 1 38.5  ? 501 HEM   B CBB 1 
HETATM 5937 C  C1C . HEM   E 2 .   ? 23.429  7.679   -16.324 1 36.05 ? 501 HEM   B C1C 1 
HETATM 5938 C  C2C . HEM   E 2 .   ? 23.695  7.585   -14.898 1 35.91 ? 501 HEM   B C2C 1 
HETATM 5939 C  C3C . HEM   E 2 .   ? 23.217  6.351   -14.515 1 36.06 ? 501 HEM   B C3C 1 
HETATM 5940 C  C4C . HEM   E 2 .   ? 22.648  5.73    -15.681 1 36.27 ? 501 HEM   B C4C 1 
HETATM 5941 C  CMC . HEM   E 2 .   ? 24.347  8.645   -14.06  1 35.51 ? 501 HEM   B CMC 1 
HETATM 5942 C  CAC . HEM   E 2 .   ? 23.313  5.753   -13.178 1 35.88 ? 501 HEM   B CAC 1 
HETATM 5943 C  CBC . HEM   E 2 .   ? 23.827  4.557   -12.81  1 35.63 ? 501 HEM   B CBC 1 
HETATM 5944 C  C1D . HEM   E 2 .   ? 21.393  3.872   -16.82  1 36.2  ? 501 HEM   B C1D 1 
HETATM 5945 C  C2D . HEM   E 2 .   ? 20.66   2.619   -16.762 1 36.17 ? 501 HEM   B C2D 1 
HETATM 5946 C  C3D . HEM   E 2 .   ? 20.374  2.278   -18.068 1 36.67 ? 501 HEM   B C3D 1 
HETATM 5947 C  C4D . HEM   E 2 .   ? 20.944  3.325   -18.899 1 36.87 ? 501 HEM   B C4D 1 
HETATM 5948 C  CMD . HEM   E 2 .   ? 20.328  1.861   -15.513 1 35.79 ? 501 HEM   B CMD 1 
HETATM 5949 C  CAD . HEM   E 2 .   ? 19.651  1.044   -18.533 1 36.97 ? 501 HEM   B CAD 1 
HETATM 5950 C  CBD . HEM   E 2 .   ? 18.199  1.304   -18.933 1 37.33 ? 501 HEM   B CBD 1 
HETATM 5951 C  CGD . HEM   E 2 .   ? 17.269  1.556   -17.778 1 37.68 ? 501 HEM   B CGD 1 
HETATM 5952 O  O1D . HEM   E 2 .   ? 16.499  2.502   -17.734 1 37.85 ? 501 HEM   B O1D 1 
HETATM 5953 O  O2D . HEM   E 2 .   ? 17.31   0.629   -16.855 1 37.76 ? 501 HEM   B O2D 1 
HETATM 5954 N  NA  . HEM   E 2 .   ? 22.063  5.493   -20.663 1 37.87 ? 501 HEM   B NA  1 
HETATM 5955 N  NB  . HEM   E 2 .   ? 23.198  7.834   -19.332 1 37.7  ? 501 HEM   B NB  1 
HETATM 5956 N  NC  . HEM   E 2 .   ? 22.805  6.561   -16.776 1 36.26 ? 501 HEM   B NC  1 
HETATM 5957 N  ND  . HEM   E 2 .   ? 21.545  4.287   -18.1   1 36.85 ? 501 HEM   B ND  1 
HETATM 5958 FE FE  . HEM   E 2 .   ? 22.445  6.021   -18.728 1 37.33 ? 501 HEM   B FE  1 
HETATM 5959 N  N1  . A1H6T F 3 .   ? 26.062  6.333   -23.421 1 45.74 ? 502 A1H6T B N1  1 
HETATM 5960 N  N3  . A1H6T F 3 .   ? 26.03   4.263   -19.47  1 39.86 ? 502 A1H6T B N3  1 
HETATM 5961 C  C4  . A1H6T F 3 .   ? 26.521  3.193   -21.706 1 42.81 ? 502 A1H6T B C4  1 
HETATM 5962 C  C5  . A1H6T F 3 .   ? 26.508  4.32    -22.706 1 44.48 ? 502 A1H6T B C5  1 
HETATM 5963 C  C6  . A1H6T F 3 .   ? 26.706  4.301   -24.058 1 45.05 ? 502 A1H6T B C6  1 
HETATM 5964 C  C7  . A1H6T F 3 .   ? 26.323  6.075   -25.799 1 48.51 ? 502 A1H6T B C7  1 
HETATM 5965 C  C8  . A1H6T F 3 .   ? 25.998  5.229   -26.849 1 49.68 ? 502 A1H6T B C8  1 
HETATM 5966 C  C10 . A1H6T F 3 .   ? 25.854  7.114   -28.324 1 50.42 ? 502 A1H6T B C10 1 
HETATM 5967 C  C13 . A1H6T F 3 .   ? 26.374  4.61    -18.157 1 39.33 ? 502 A1H6T B C13 1 
HETATM 5968 C  C15 . A1H6T F 3 .   ? 24.781  4.774   -19.693 1 39.73 ? 502 A1H6T B C15 1 
HETATM 5969 CL CL  . A1H6T F 3 .   ? 29.391  2.498   -20.729 1 40.29 ? 502 A1H6T B CL  1 
HETATM 5970 C  C   . A1H6T F 3 .   ? 28.182  3.294   -19.796 1 40.33 ? 502 A1H6T B C   1 
HETATM 5971 C  C3  . A1H6T F 3 .   ? 26.949  3.588   -20.312 1 40.86 ? 502 A1H6T B C3  1 
HETATM 5972 N  N4  . A1H6T F 3 .   ? 24.306  5.409   -18.646 1 39.17 ? 502 A1H6T B N4  1 
HETATM 5973 C  C14 . A1H6T F 3 .   ? 25.288  5.31    -17.689 1 38.73 ? 502 A1H6T B C14 1 
HETATM 5974 C  C2  . A1H6T F 3 .   ? 27.674  4.271   -17.679 1 39.62 ? 502 A1H6T B C2  1 
HETATM 5975 C  C1  . A1H6T F 3 .   ? 28.55   3.634   -18.472 1 39.81 ? 502 A1H6T B C1  1 
HETATM 5976 O  O   . A1H6T F 3 .   ? 25.234  2.602   -21.687 1 42.69 ? 502 A1H6T B O   1 
HETATM 5977 N  N2  . A1H6T F 3 .   ? 26.419  5.557   -24.472 1 46.24 ? 502 A1H6T B N2  1 
HETATM 5978 N  N   . A1H6T F 3 .   ? 26.117  5.58    -22.349 1 45.44 ? 502 A1H6T B N   1 
HETATM 5979 C  C12 . A1H6T F 3 .   ? 26.42   7.444   -26.013 1 49.5  ? 502 A1H6T B C12 1 
HETATM 5980 C  C11 . A1H6T F 3 .   ? 26.181  7.956   -27.279 1 50.31 ? 502 A1H6T B C11 1 
HETATM 5981 C  C9  . A1H6T F 3 .   ? 25.762  5.757   -28.109 1 50.12 ? 502 A1H6T B C9  1 
HETATM 5982 O  O   . HOH   G 4 .   ? -0.002  -22.301 -26.533 1 30.04 ? 601 HOH   A O   1 
HETATM 5983 O  O   . HOH   G 4 .   ? 21.781  -27.02  -24.487 1 35.96 ? 602 HOH   A O   1 
HETATM 5984 O  O   . HOH   G 4 .   ? -0.342  -7.196  -31.554 1 48.12 ? 603 HOH   A O   1 
HETATM 5985 O  O   . HOH   G 4 .   ? 6.521   -30.951 -13.853 1 45.62 ? 604 HOH   A O   1 
HETATM 5986 O  O   . HOH   G 4 .   ? -12.944 -16.704 -26.52  1 44    ? 605 HOH   A O   1 
HETATM 5987 O  O   . HOH   G 4 .   ? 10.148  -26.291 -21.823 1 33.23 ? 606 HOH   A O   1 
HETATM 5988 O  O   . HOH   G 4 .   ? -17.866 -22.229 -24.841 1 37.43 ? 607 HOH   A O   1 
HETATM 5989 O  O   . HOH   G 4 .   ? 0.387   -26.037 -21.789 1 34.01 ? 608 HOH   A O   1 
HETATM 5990 O  O   . HOH   G 4 .   ? 39.519  -37.609 -6.768  1 41.99 ? 609 HOH   A O   1 
HETATM 5991 O  O   . HOH   G 4 .   ? 28.526  -28.504 -4.735  1 37.48 ? 610 HOH   A O   1 
HETATM 5992 O  O   . HOH   G 4 .   ? -13.353 -20.348 -42.838 1 42.23 ? 611 HOH   A O   1 
HETATM 5993 O  O   . HOH   G 4 .   ? 11.955  -34.162 -18.346 1 38.46 ? 612 HOH   A O   1 
HETATM 5994 O  O   . HOH   G 4 .   ? -12.96  -14.809 -32.155 1 61.49 ? 613 HOH   A O   1 
HETATM 5995 O  O   . HOH   G 4 .   ? 19.41   -28.066 -25.925 1 37.55 ? 614 HOH   A O   1 
HETATM 5996 O  O   . HOH   G 4 .   ? 26.745  -24.412 -28.797 1 52.55 ? 615 HOH   A O   1 
HETATM 5997 O  O   . HOH   G 4 .   ? 21.402  -33.399 -33.32  1 35.86 ? 616 HOH   A O   1 
HETATM 5998 O  O   . HOH   G 4 .   ? 7.447   -21.296 -29.443 1 33.14 ? 617 HOH   A O   1 
HETATM 5999 O  O   . HOH   G 4 .   ? -3.202  -29.799 -18.291 1 35.27 ? 618 HOH   A O   1 
HETATM 6000 O  O   . HOH   G 4 .   ? 16.918  -28.498 -25.039 1 38.37 ? 619 HOH   A O   1 
HETATM 6001 O  O   . HOH   G 4 .   ? -8.685  -23.974 -43.539 1 40.22 ? 620 HOH   A O   1 
HETATM 6002 O  O   . HOH   G 4 .   ? 8.527   -24.779 -23.842 1 34.07 ? 621 HOH   A O   1 
HETATM 6003 O  O   . HOH   G 4 .   ? 22.508  -31.484 -31.691 1 39.37 ? 622 HOH   A O   1 
HETATM 6004 O  O   . HOH   G 4 .   ? 10.342  -27.425 -19.533 1 37.73 ? 623 HOH   A O   1 
HETATM 6005 O  O   . HOH   G 4 .   ? 11.435  -29.675 -20.799 1 36.64 ? 624 HOH   A O   1 
HETATM 6006 O  O   . HOH   G 4 .   ? -0.051  -21.285 -12.652 1 67.39 ? 625 HOH   A O   1 
HETATM 6007 O  O   . HOH   G 4 .   ? 46.87   -38.74  -10.764 1 39.03 ? 626 HOH   A O   1 
HETATM 6008 O  O   . HOH   G 4 .   ? 5.705   -28.665 -17.78  1 39.26 ? 627 HOH   A O   1 
HETATM 6009 O  O   . HOH   G 4 .   ? 0.769   -12.125 -23.352 1 48.9  ? 628 HOH   A O   1 
HETATM 6010 O  O   . HOH   G 4 .   ? -3.195  -30.383 -20.942 1 38.74 ? 629 HOH   A O   1 
HETATM 6011 O  O   . HOH   G 4 .   ? 10.373  -30.101 -8.202  1 40.33 ? 630 HOH   A O   1 
HETATM 6012 O  O   . HOH   G 4 .   ? 36.499  -40.941 -22.83  1 54.13 ? 631 HOH   A O   1 
HETATM 6013 O  O   . HOH   G 4 .   ? -13.686 -29.725 -22.451 1 58.48 ? 632 HOH   A O   1 
HETATM 6014 O  O   . HOH   G 4 .   ? -10.468 -22.093 -42.492 1 34.19 ? 633 HOH   A O   1 
HETATM 6015 O  O   . HOH   G 4 .   ? -16.875 -23.452 -31.801 1 36.78 ? 634 HOH   A O   1 
HETATM 6016 O  O   . HOH   G 4 .   ? 19.33   -33.716 -29.948 1 41.65 ? 635 HOH   A O   1 
HETATM 6017 O  O   . HOH   G 4 .   ? -3.31   -27.841 -11.026 1 42.64 ? 636 HOH   A O   1 
HETATM 6018 O  O   . HOH   G 4 .   ? -9.41   -34.087 -17.03  1 46.24 ? 637 HOH   A O   1 
HETATM 6019 O  O   . HOH   G 4 .   ? -12.993 -11.368 -32.671 1 47.57 ? 638 HOH   A O   1 
HETATM 6020 O  O   . HOH   G 4 .   ? 10.331  -18.939 -36.572 1 55.84 ? 639 HOH   A O   1 
HETATM 6021 O  O   . HOH   G 4 .   ? 38.316  -34.39  -26.768 1 61.7  ? 640 HOH   A O   1 
HETATM 6022 O  O   . HOH   G 4 .   ? 6.221   -23.304 -14.088 1 46.51 ? 641 HOH   A O   1 
HETATM 6023 O  O   . HOH   G 4 .   ? 5.244   -25.821 -14.337 1 47.12 ? 642 HOH   A O   1 
HETATM 6024 O  O   . HOH   G 4 .   ? 4.98    -28.554 -15.037 1 49.33 ? 643 HOH   A O   1 
HETATM 6025 O  O   . HOH   H 4 .   ? 40.877  2.155   -5.541  1 52.11 ? 601 HOH   B O   1 
HETATM 6026 O  O   . HOH   H 4 .   ? 37.744  -5.248  -20.055 1 41.18 ? 602 HOH   B O   1 
HETATM 6027 O  O   . HOH   H 4 .   ? 9.085   -7.149  -24.762 1 49.56 ? 603 HOH   B O   1 
HETATM 6028 O  O   . HOH   H 4 .   ? 37.008  -4.903  -14.028 1 44.59 ? 604 HOH   B O   1 
HETATM 6029 O  O   . HOH   H 4 .   ? 40.666  -3.902  -8.862  1 37.9  ? 605 HOH   B O   1 
HETATM 6030 O  O   . HOH   H 4 .   ? 29.109  -5.337  -16.622 1 40.48 ? 606 HOH   B O   1 
HETATM 6031 O  O   . HOH   H 4 .   ? 18.047  -1.921  -16.517 1 33.53 ? 607 HOH   B O   1 
HETATM 6032 O  O   . HOH   H 4 .   ? 16.185  -3.9    -16.07  1 47.93 ? 608 HOH   B O   1 
HETATM 6033 O  O   . HOH   H 4 .   ? -2.106  -7.374  4.141   1 51.2  ? 609 HOH   B O   1 
HETATM 6034 O  O   . HOH   H 4 .   ? 20.565  -2.056  -15.536 1 42.99 ? 610 HOH   B O   1 
HETATM 6035 O  O   . HOH   H 4 .   ? 15.62   6.571   -19.229 1 36.66 ? 611 HOH   B O   1 
HETATM 6036 O  O   . HOH   H 4 .   ? 25.363  -1.208  -6.521  1 37.58 ? 612 HOH   B O   1 
HETATM 6037 O  O   . HOH   H 4 .   ? 14.453  4.084   -19.117 1 37.97 ? 613 HOH   B O   1 
HETATM 6038 O  O   . HOH   H 4 .   ? 30.45   -4.497  -23.001 1 40.99 ? 614 HOH   B O   1 
HETATM 6039 O  O   . HOH   H 4 .   ? 33.151  4.474   -32.15  1 60.7  ? 615 HOH   B O   1 
HETATM 6040 O  O   . HOH   H 4 .   ? 45.7    6.995   -31.901 1 41.99 ? 616 HOH   B O   1 
HETATM 6041 O  O   . HOH   H 4 .   ? 27.957  1.232   -26.01  1 56.8  ? 617 HOH   B O   1 
HETATM 6042 O  O   . HOH   H 4 .   ? 24.84   2.201   -27.499 1 59.88 ? 618 HOH   B O   1 
HETATM 6043 O  O   . HOH   H 4 .   ? 27.079  -5.583  -11.785 1 54.89 ? 619 HOH   B O   1 
HETATM 6044 O  O   . HOH   H 4 .   ? 26.059  -3.096  -11.347 1 37.46 ? 620 HOH   B O   1 
HETATM 6045 O  O   . HOH   H 4 .   ? 40.477  -1.865  -10.459 1 38.35 ? 621 HOH   B O   1 
HETATM 6046 O  O   . HOH   H 4 .   ? 27.9    -1.832  -31.509 1 53.24 ? 622 HOH   B O   1 
HETATM 6047 O  O   . HOH   H 4 .   ? 37.246  15.882  -18.601 1 47.13 ? 623 HOH   B O   1 
HETATM 6048 O  O   . HOH   H 4 .   ? 10.663  -5.116  -25.043 1 54.29 ? 624 HOH   B O   1 
HETATM 6049 O  O   . HOH   H 4 .   ? 46.943  -0.726  -5.196  1 54.31 ? 625 HOH   B O   1 
# 
