data_9ESC
# 
_entry.id   9ESC 
# 
_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   9ESC         pdb_00009esc 10.2210/pdb9esc/pdb 
WWPDB D_1292136164 ?            ?                   
# 
_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                        9ESC 
_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 '(~{S})-[(7~{a}~{R})-2-cyclopentyl-5,6,7,7~{a}-tetrahydroimidazo[5,1-b][1,3]thiazol-3-yl]-cyclohexyl-methanol' 
308.482   2   ?          ? ? ? 
4 water       nat water                                                                                                          
18.015    197 ?          ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'IDO-1,Indoleamine-pyrrole 2,3-dioxygenase' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MGSSHHHHHHSAALEVLFQGPHMWTISKEYHIDEEVGFALPNPQENLPDFYNDWMFIAKHLPDLIESGQLRERVEKLNML
SIDHLTDHKSQRLARLVLGCITMAYVWGKGHGDVRKVLPRNIAVPYCQLSKKLELPPILVYADCVLANWKKKDPNKPLTY
ENMDVLFSFRDGDCSKGFFLVSLLVEIAAASAIKVIPTVFKAMQMQERDTLLKALLEIASCLEKALQVFHQIHDHVNPKA
FFSVLRIYLSGWKGNPQLSDGLVYEGFWEDPKEFAGGSAGQSSVFQCFDVLLGIQQTAGGGHAAQFLQDMRRYMPPAHRN
FLCSLESNPSVREFVLSKGDAGLREAYDACVKALVSLRSYHLQIVTKYILIPASQQPKENKTSEDPSKLEAKGTGGTDLM
NFLKTVRSTTEKSLLKEG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSAALEVLFQGPHMWTISKEYHIDEEVGFALPNPQENLPDFYNDWMFIAKHLPDLIESGQLRERVEKLNML
SIDHLTDHKSQRLARLVLGCITMAYVWGKGHGDVRKVLPRNIAVPYCQLSKKLELPPILVYADCVLANWKKKDPNKPLTY
ENMDVLFSFRDGDCSKGFFLVSLLVEIAAASAIKVIPTVFKAMQMQERDTLLKALLEIASCLEKALQVFHQIHDHVNPKA
FFSVLRIYLSGWKGNPQLSDGLVYEGFWEDPKEFAGGSAGQSSVFQCFDVLLGIQQTAGGGHAAQFLQDMRRYMPPAHRN
FLCSLESNPSVREFVLSKGDAGLREAYDACVKALVSLRSYHLQIVTKYILIPASQQPKENKTSEDPSKLEAKGTGGTDLM
NFLKTVRSTTEKSLLKEG
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'PROTOPORPHYRIN IX CONTAINING FE'                                                                              HEM   
3 '(~{S})-[(7~{a}~{R})-2-cyclopentyl-5,6,7,7~{a}-tetrahydroimidazo[5,1-b][1,3]thiazol-3-yl]-cyclohexyl-methanol' A1H6R 
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 
A1H6R non-polymer         . 
'(~{S})-[(7~{a}~{R})-2-cyclopentyl-5,6,7,7~{a}-tetrahydroimidazo[5,1-b][1,3]thiazol-3-yl]-cyclohexyl-methanol' ?    
'C17 H28 N2 O S'   308.482 
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  -3  ALA ALA 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 ?   ?   ?   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 ?   ?   ?   B . n 
B 1 377 PRO 377 362 ?   ?   ?   B . n 
B 1 378 LYS 378 363 ?   ?   ?   B . n 
B 1 379 GLU 379 364 ?   ?   ?   B . n 
B 1 380 ASN 380 365 ?   ?   ?   B . n 
B 1 381 LYS 381 366 ?   ?   ?   B . n 
B 1 382 THR 382 367 ?   ?   ?   B . n 
B 1 383 SER 383 368 ?   ?   ?   B . n 
B 1 384 GLU 384 369 ?   ?   ?   B . n 
B 1 385 ASP 385 370 ?   ?   ?   B . n 
B 1 386 PRO 386 371 ?   ?   ?   B . n 
B 1 387 SER 387 372 ?   ?   ?   B . n 
B 1 388 LYS 388 373 ?   ?   ?   B . n 
B 1 389 LEU 389 374 ?   ?   ?   B . n 
B 1 390 GLU 390 375 ?   ?   ?   B . n 
B 1 391 ALA 391 376 ?   ?   ?   B . n 
B 1 392 LYS 392 377 ?   ?   ?   B . n 
B 1 393 GLY 393 378 ?   ?   ?   B . n 
B 1 394 THR 394 379 ?   ?   ?   B . n 
B 1 395 GLY 395 380 380 GLY GLY B . n 
B 1 396 GLY 396 381 381 GLY GLY B . n 
B 1 397 THR 397 382 382 THR THR B . n 
B 1 398 ASP 398 383 383 ASP ASP B . n 
B 1 399 LEU 399 384 384 LEU LEU B . n 
B 1 400 MET 400 385 385 MET MET B . n 
B 1 401 ASN 401 386 386 ASN ASN B . n 
B 1 402 PHE 402 387 387 PHE PHE B . n 
B 1 403 LEU 403 388 388 LEU LEU B . n 
B 1 404 LYS 404 389 389 LYS LYS B . n 
B 1 405 THR 405 390 390 THR THR B . n 
B 1 406 VAL 406 391 391 VAL VAL B . n 
B 1 407 ARG 407 392 392 ARG ARG B . n 
B 1 408 SER 408 393 393 SER SER B . n 
B 1 409 THR 409 394 394 THR THR B . n 
B 1 410 THR 410 395 395 THR THR B . n 
B 1 411 GLU 411 396 396 GLU GLU B . n 
B 1 412 LYS 412 397 397 LYS LYS B . n 
B 1 413 SER 413 398 398 SER SER B . n 
B 1 414 LEU 414 399 399 LEU LEU B . n 
B 1 415 LEU 415 400 400 LEU LEU B . n 
B 1 416 LYS 416 401 401 LYS LYS B . n 
B 1 417 GLU 417 402 ?   ?   ?   B . n 
B 1 418 GLY 418 403 ?   ?   ?   B . n 
# 
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 A1H6R 1   502 1   A1H6R LIG A . 
E 2 HEM   1   501 501 HEM   HEM B . 
F 3 A1H6R 1   502 2   A1H6R LIG B . 
G 4 HOH   1   601 72  HOH   HOH A . 
G 4 HOH   2   602 50  HOH   HOH A . 
G 4 HOH   3   603 79  HOH   HOH A . 
G 4 HOH   4   604 109 HOH   HOH A . 
G 4 HOH   5   605 70  HOH   HOH A . 
G 4 HOH   6   606 255 HOH   HOH A . 
G 4 HOH   7   607 101 HOH   HOH A . 
G 4 HOH   8   608 124 HOH   HOH A . 
G 4 HOH   9   609 37  HOH   HOH A . 
G 4 HOH   10  610 178 HOH   HOH A . 
G 4 HOH   11  611 244 HOH   HOH A . 
G 4 HOH   12  612 20  HOH   HOH A . 
G 4 HOH   13  613 248 HOH   HOH A . 
G 4 HOH   14  614 41  HOH   HOH A . 
G 4 HOH   15  615 133 HOH   HOH A . 
G 4 HOH   16  616 150 HOH   HOH A . 
G 4 HOH   17  617 221 HOH   HOH A . 
G 4 HOH   18  618 74  HOH   HOH A . 
G 4 HOH   19  619 170 HOH   HOH A . 
G 4 HOH   20  620 195 HOH   HOH A . 
G 4 HOH   21  621 47  HOH   HOH A . 
G 4 HOH   22  622 211 HOH   HOH A . 
G 4 HOH   23  623 187 HOH   HOH A . 
G 4 HOH   24  624 200 HOH   HOH A . 
G 4 HOH   25  625 84  HOH   HOH A . 
G 4 HOH   26  626 173 HOH   HOH A . 
G 4 HOH   27  627 151 HOH   HOH A . 
G 4 HOH   28  628 1   HOH   HOH A . 
G 4 HOH   29  629 33  HOH   HOH A . 
G 4 HOH   30  630 2   HOH   HOH A . 
G 4 HOH   31  631 246 HOH   HOH A . 
G 4 HOH   32  632 142 HOH   HOH A . 
G 4 HOH   33  633 162 HOH   HOH A . 
G 4 HOH   34  634 166 HOH   HOH A . 
G 4 HOH   35  635 208 HOH   HOH A . 
G 4 HOH   36  636 181 HOH   HOH A . 
G 4 HOH   37  637 190 HOH   HOH A . 
G 4 HOH   38  638 34  HOH   HOH A . 
G 4 HOH   39  639 122 HOH   HOH A . 
G 4 HOH   40  640 67  HOH   HOH A . 
G 4 HOH   41  641 230 HOH   HOH A . 
G 4 HOH   42  642 148 HOH   HOH A . 
G 4 HOH   43  643 31  HOH   HOH A . 
G 4 HOH   44  644 176 HOH   HOH A . 
G 4 HOH   45  645 105 HOH   HOH A . 
G 4 HOH   46  646 155 HOH   HOH A . 
G 4 HOH   47  647 83  HOH   HOH A . 
G 4 HOH   48  648 199 HOH   HOH A . 
G 4 HOH   49  649 205 HOH   HOH A . 
G 4 HOH   50  650 168 HOH   HOH A . 
G 4 HOH   51  651 25  HOH   HOH A . 
G 4 HOH   52  652 158 HOH   HOH A . 
G 4 HOH   53  653 9   HOH   HOH A . 
G 4 HOH   54  654 156 HOH   HOH A . 
G 4 HOH   55  655 53  HOH   HOH A . 
G 4 HOH   56  656 40  HOH   HOH A . 
G 4 HOH   57  657 98  HOH   HOH A . 
G 4 HOH   58  658 7   HOH   HOH A . 
G 4 HOH   59  659 233 HOH   HOH A . 
G 4 HOH   60  660 64  HOH   HOH A . 
G 4 HOH   61  661 103 HOH   HOH A . 
G 4 HOH   62  662 65  HOH   HOH A . 
G 4 HOH   63  663 48  HOH   HOH A . 
G 4 HOH   64  664 217 HOH   HOH A . 
G 4 HOH   65  665 8   HOH   HOH A . 
G 4 HOH   66  666 135 HOH   HOH A . 
G 4 HOH   67  667 6   HOH   HOH A . 
G 4 HOH   68  668 258 HOH   HOH A . 
G 4 HOH   69  669 5   HOH   HOH A . 
G 4 HOH   70  670 38  HOH   HOH A . 
G 4 HOH   71  671 90  HOH   HOH A . 
G 4 HOH   72  672 49  HOH   HOH A . 
G 4 HOH   73  673 42  HOH   HOH A . 
G 4 HOH   74  674 225 HOH   HOH A . 
G 4 HOH   75  675 144 HOH   HOH A . 
G 4 HOH   76  676 127 HOH   HOH A . 
G 4 HOH   77  677 92  HOH   HOH A . 
G 4 HOH   78  678 179 HOH   HOH A . 
G 4 HOH   79  679 82  HOH   HOH A . 
G 4 HOH   80  680 128 HOH   HOH A . 
G 4 HOH   81  681 58  HOH   HOH A . 
G 4 HOH   82  682 167 HOH   HOH A . 
G 4 HOH   83  683 60  HOH   HOH A . 
G 4 HOH   84  684 249 HOH   HOH A . 
G 4 HOH   85  685 171 HOH   HOH A . 
G 4 HOH   86  686 100 HOH   HOH A . 
G 4 HOH   87  687 204 HOH   HOH A . 
G 4 HOH   88  688 87  HOH   HOH A . 
G 4 HOH   89  689 28  HOH   HOH A . 
G 4 HOH   90  690 80  HOH   HOH A . 
G 4 HOH   91  691 223 HOH   HOH A . 
G 4 HOH   92  692 239 HOH   HOH A . 
G 4 HOH   93  693 97  HOH   HOH A . 
G 4 HOH   94  694 203 HOH   HOH A . 
G 4 HOH   95  695 214 HOH   HOH A . 
G 4 HOH   96  696 147 HOH   HOH A . 
G 4 HOH   97  697 261 HOH   HOH A . 
G 4 HOH   98  698 247 HOH   HOH A . 
G 4 HOH   99  699 132 HOH   HOH A . 
G 4 HOH   100 700 71  HOH   HOH A . 
G 4 HOH   101 701 196 HOH   HOH A . 
G 4 HOH   102 702 23  HOH   HOH A . 
G 4 HOH   103 703 85  HOH   HOH A . 
G 4 HOH   104 704 29  HOH   HOH A . 
G 4 HOH   105 705 27  HOH   HOH A . 
G 4 HOH   106 706 185 HOH   HOH A . 
G 4 HOH   107 707 102 HOH   HOH A . 
G 4 HOH   108 708 163 HOH   HOH A . 
G 4 HOH   109 709 198 HOH   HOH A . 
G 4 HOH   110 710 55  HOH   HOH A . 
G 4 HOH   111 711 257 HOH   HOH A . 
G 4 HOH   112 712 138 HOH   HOH A . 
G 4 HOH   113 713 218 HOH   HOH A . 
G 4 HOH   114 714 89  HOH   HOH A . 
G 4 HOH   115 715 91  HOH   HOH A . 
G 4 HOH   116 716 228 HOH   HOH A . 
G 4 HOH   117 717 107 HOH   HOH A . 
G 4 HOH   118 718 250 HOH   HOH A . 
G 4 HOH   119 719 93  HOH   HOH A . 
G 4 HOH   120 720 152 HOH   HOH A . 
G 4 HOH   121 721 115 HOH   HOH A . 
G 4 HOH   122 722 123 HOH   HOH A . 
G 4 HOH   123 723 140 HOH   HOH A . 
G 4 HOH   124 724 192 HOH   HOH A . 
G 4 HOH   125 725 94  HOH   HOH A . 
H 4 HOH   1   601 52  HOH   HOH B . 
H 4 HOH   2   602 104 HOH   HOH B . 
H 4 HOH   3   603 26  HOH   HOH B . 
H 4 HOH   4   604 238 HOH   HOH B . 
H 4 HOH   5   605 243 HOH   HOH B . 
H 4 HOH   6   606 86  HOH   HOH B . 
H 4 HOH   7   607 17  HOH   HOH B . 
H 4 HOH   8   608 252 HOH   HOH B . 
H 4 HOH   9   609 14  HOH   HOH B . 
H 4 HOH   10  610 30  HOH   HOH B . 
H 4 HOH   11  611 260 HOH   HOH B . 
H 4 HOH   12  612 145 HOH   HOH B . 
H 4 HOH   13  613 57  HOH   HOH B . 
H 4 HOH   14  614 46  HOH   HOH B . 
H 4 HOH   15  615 254 HOH   HOH B . 
H 4 HOH   16  616 226 HOH   HOH B . 
H 4 HOH   17  617 45  HOH   HOH B . 
H 4 HOH   18  618 13  HOH   HOH B . 
H 4 HOH   19  619 164 HOH   HOH B . 
H 4 HOH   20  620 10  HOH   HOH B . 
H 4 HOH   21  621 215 HOH   HOH B . 
H 4 HOH   22  622 153 HOH   HOH B . 
H 4 HOH   23  623 22  HOH   HOH B . 
H 4 HOH   24  624 207 HOH   HOH B . 
H 4 HOH   25  625 216 HOH   HOH B . 
H 4 HOH   26  626 251 HOH   HOH B . 
H 4 HOH   27  627 59  HOH   HOH B . 
H 4 HOH   28  628 35  HOH   HOH B . 
H 4 HOH   29  629 39  HOH   HOH B . 
H 4 HOH   30  630 88  HOH   HOH B . 
H 4 HOH   31  631 237 HOH   HOH B . 
H 4 HOH   32  632 3   HOH   HOH B . 
H 4 HOH   33  633 111 HOH   HOH B . 
H 4 HOH   34  634 130 HOH   HOH B . 
H 4 HOH   35  635 36  HOH   HOH B . 
H 4 HOH   36  636 66  HOH   HOH B . 
H 4 HOH   37  637 11  HOH   HOH B . 
H 4 HOH   38  638 76  HOH   HOH B . 
H 4 HOH   39  639 141 HOH   HOH B . 
H 4 HOH   40  640 177 HOH   HOH B . 
H 4 HOH   41  641 126 HOH   HOH B . 
H 4 HOH   42  642 96  HOH   HOH B . 
H 4 HOH   43  643 4   HOH   HOH B . 
H 4 HOH   44  644 99  HOH   HOH B . 
H 4 HOH   45  645 16  HOH   HOH B . 
H 4 HOH   46  646 18  HOH   HOH B . 
H 4 HOH   47  647 165 HOH   HOH B . 
H 4 HOH   48  648 68  HOH   HOH B . 
H 4 HOH   49  649 12  HOH   HOH B . 
H 4 HOH   50  650 63  HOH   HOH B . 
H 4 HOH   51  651 186 HOH   HOH B . 
H 4 HOH   52  652 134 HOH   HOH B . 
H 4 HOH   53  653 220 HOH   HOH B . 
H 4 HOH   54  654 120 HOH   HOH B . 
H 4 HOH   55  655 182 HOH   HOH B . 
H 4 HOH   56  656 19  HOH   HOH B . 
H 4 HOH   57  657 236 HOH   HOH B . 
H 4 HOH   58  658 78  HOH   HOH B . 
H 4 HOH   59  659 212 HOH   HOH B . 
H 4 HOH   60  660 61  HOH   HOH B . 
H 4 HOH   61  661 95  HOH   HOH B . 
H 4 HOH   62  662 253 HOH   HOH B . 
H 4 HOH   63  663 117 HOH   HOH B . 
H 4 HOH   64  664 202 HOH   HOH B . 
H 4 HOH   65  665 232 HOH   HOH B . 
H 4 HOH   66  666 149 HOH   HOH B . 
H 4 HOH   67  667 116 HOH   HOH B . 
H 4 HOH   68  668 77  HOH   HOH B . 
H 4 HOH   69  669 159 HOH   HOH B . 
H 4 HOH   70  670 231 HOH   HOH B . 
H 4 HOH   71  671 213 HOH   HOH B . 
H 4 HOH   72  672 234 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 TRP 9   ? CG  ? A TRP 24  CG  
10 1 Y 1 A TRP 9   ? CD1 ? A TRP 24  CD1 
11 1 Y 1 A TRP 9   ? CD2 ? A TRP 24  CD2 
12 1 Y 1 A TRP 9   ? NE1 ? A TRP 24  NE1 
13 1 Y 1 A TRP 9   ? CE2 ? A TRP 24  CE2 
14 1 Y 1 A TRP 9   ? CE3 ? A TRP 24  CE3 
15 1 Y 1 A TRP 9   ? CZ2 ? A TRP 24  CZ2 
16 1 Y 1 A TRP 9   ? CZ3 ? A TRP 24  CZ3 
17 1 Y 1 A TRP 9   ? CH2 ? A TRP 24  CH2 
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 LYS 224 ? CD  ? A LYS 239 CD  
27 1 Y 1 A LYS 224 ? CE  ? A LYS 239 CE  
28 1 Y 1 A LYS 224 ? NZ  ? A LYS 239 NZ  
29 1 Y 1 A GLU 254 ? CG  ? A GLU 269 CG  
30 1 Y 1 A GLU 254 ? CD  ? A GLU 269 CD  
31 1 Y 1 A GLU 254 ? OE1 ? A GLU 269 OE1 
32 1 Y 1 A GLU 254 ? OE2 ? A GLU 269 OE2 
33 1 Y 1 A GLU 318 ? CG  ? A GLU 333 CG  
34 1 Y 1 A GLU 318 ? CD  ? A GLU 333 CD  
35 1 Y 1 A GLU 318 ? OE1 ? A GLU 333 OE1 
36 1 Y 1 A GLU 318 ? OE2 ? A GLU 333 OE2 
37 1 Y 1 B LYS 13  ? CD  ? B LYS 28  CD  
38 1 Y 1 B LYS 13  ? CE  ? B LYS 28  CE  
39 1 Y 1 B LYS 13  ? NZ  ? B LYS 28  NZ  
40 1 Y 1 B LYS 44  ? CG  ? B LYS 59  CG  
41 1 Y 1 B LYS 44  ? CD  ? B LYS 59  CD  
42 1 Y 1 B LYS 44  ? CE  ? B LYS 59  CE  
43 1 Y 1 B LYS 44  ? NZ  ? B LYS 59  NZ  
44 1 Y 1 B LYS 61  ? CG  ? B LYS 76  CG  
45 1 Y 1 B LYS 61  ? CD  ? B LYS 76  CD  
46 1 Y 1 B LYS 61  ? CE  ? B LYS 76  CE  
47 1 Y 1 B LYS 61  ? NZ  ? B LYS 76  NZ  
48 1 Y 1 B ILE 67  ? CG1 ? B ILE 82  CG1 
49 1 Y 1 B ILE 67  ? CG2 ? B ILE 82  CG2 
50 1 Y 1 B ILE 67  ? CD1 ? B ILE 82  CD1 
51 1 Y 1 B ARG 105 ? CG  ? B ARG 120 CG  
52 1 Y 1 B ARG 105 ? CD  ? B ARG 120 CD  
53 1 Y 1 B ARG 105 ? NE  ? B ARG 120 NE  
54 1 Y 1 B ARG 105 ? CZ  ? B ARG 120 CZ  
55 1 Y 1 B ARG 105 ? NH1 ? B ARG 120 NH1 
56 1 Y 1 B ARG 105 ? NH2 ? B ARG 120 NH2 
57 1 Y 1 B ASN 106 ? CG  ? B ASN 121 CG  
58 1 Y 1 B ASN 106 ? OD1 ? B ASN 121 OD1 
59 1 Y 1 B ASN 106 ? ND2 ? B ASN 121 ND2 
60 1 Y 1 B LYS 116 ? CE  ? B LYS 131 CE  
61 1 Y 1 B LYS 116 ? NZ  ? B LYS 131 NZ  
62 1 Y 1 B LYS 117 ? CE  ? B LYS 132 CE  
63 1 Y 1 B LYS 117 ? NZ  ? B LYS 132 NZ  
64 1 Y 1 B LYS 141 ? CG  ? B LYS 156 CG  
65 1 Y 1 B LYS 141 ? CD  ? B LYS 156 CD  
66 1 Y 1 B LYS 141 ? CE  ? B LYS 156 CE  
67 1 Y 1 B LYS 141 ? NZ  ? B LYS 156 NZ  
68 1 Y 1 B GLU 146 ? CG  ? B GLU 161 CG  
69 1 Y 1 B GLU 146 ? CD  ? B GLU 161 CD  
70 1 Y 1 B GLU 146 ? OE1 ? B GLU 161 OE1 
71 1 Y 1 B GLU 146 ? OE2 ? B GLU 161 OE2 
72 1 Y 1 B LYS 186 ? CG  ? B LYS 201 CG  
73 1 Y 1 B LYS 186 ? CD  ? B LYS 201 CD  
74 1 Y 1 B LYS 186 ? CE  ? B LYS 201 CE  
75 1 Y 1 B LYS 186 ? NZ  ? B LYS 201 NZ  
76 1 Y 1 B LYS 224 ? CG  ? B LYS 239 CG  
77 1 Y 1 B LYS 224 ? CD  ? B LYS 239 CD  
78 1 Y 1 B LYS 224 ? CE  ? B LYS 239 CE  
79 1 Y 1 B LYS 224 ? NZ  ? B LYS 239 NZ  
80 1 Y 1 B GLU 254 ? CG  ? B GLU 269 CG  
81 1 Y 1 B GLU 254 ? CD  ? B GLU 269 CD  
82 1 Y 1 B GLU 254 ? OE1 ? B GLU 269 OE1 
83 1 Y 1 B GLU 254 ? OE2 ? B GLU 269 OE2 
84 1 Y 1 B ASP 255 ? CG  ? B ASP 270 CG  
85 1 Y 1 B ASP 255 ? OD1 ? B ASP 270 OD1 
86 1 Y 1 B ASP 255 ? OD2 ? B ASP 270 OD2 
87 1 Y 1 B LYS 401 ? CG  ? B LYS 416 CG  
88 1 Y 1 B LYS 401 ? CD  ? B LYS 416 CD  
89 1 Y 1 B LYS 401 ? CE  ? B LYS 416 CE  
90 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' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .      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                     9ESC 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     84.623 
_cell.length_a_esd                 ? 
_cell.length_b                     92.049 
_cell.length_b_esd                 ? 
_cell.length_c                     132.253 
_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                         9ESC 
_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                   9ESC 
_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          55.03 
_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         2017-04-10 
_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                                       9ESC 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.76 
_reflns.d_resolution_low                               46.02 
_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                                     102271 
_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                           99.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.8 
_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                                .108 
_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                                   .999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.76 
_reflns_shell.d_res_low                                     1.87 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             16009 
_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                               4.87 
_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                                  .178 
_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]                            -0.1744 
_refine.aniso_B[1][2]                            0 
_refine.aniso_B[1][3]                            0 
_refine.aniso_B[2][2]                            0.6747 
_refine.aniso_B[2][3]                            0 
_refine.aniso_B[3][3]                            -0.5003 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               43.5 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.945 
_refine.correlation_coeff_Fo_to_Fc_free          0.93 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9ESC 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.95 
_refine.ls_d_res_low                             46.02 
_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                     75682 
_refine.ls_number_reflns_R_free                  3785 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.7 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2352 
_refine.ls_R_factor_R_free                       0.2602 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2338 
_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   0.147 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.145 
_refine.pdbx_overall_SU_R_Blow_DPI               0.16 
_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             0.162 
_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                        9ESC 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.3 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.95 
_refine_hist.d_res_low                        46.02 
_refine_hist.number_atoms_solvent             197 
_refine_hist.number_atoms_total               6259 
_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        5934 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         128 
_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' ? 0.008 ? 6322 ? t_bond_d                  2  HARMONIC     
'X-RAY DIFFRACTION' ? 0.79  ? 8593 ? t_angle_deg               2  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 2201 ? t_dihedral_angle_d        2  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? 1125 ? t_gen_planes              5  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 6322 ? t_it                      10 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 785  ? t_chiral_improper_torsion 5  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? 5364 ? t_ideal_dist_contact      4  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? 2.95  ? ?    ? t_omega_torsion           ?  ?            
'X-RAY DIFFRACTION' ? 16.5  ? ?    ? t_other_torsion           ?  ?            
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.95 
_refine_ls_shell.d_res_low                        1.96 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                1514 
_refine_ls_shell.number_reflns_R_free             76 
_refine_ls_shell.number_reflns_R_work             ? 
_refine_ls_shell.percent_reflns_obs               99.73 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     0.3885 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.3883 
_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                  0.3918 
# 
_struct.entry_id                     9ESC 
_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        9ESC 
_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 9ESC A 24 ? 418 ? P14902 9 ? 403 ? 9 403 
2 1 9ESC 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 9ESC MET A 1  ? UNP P14902 ? ? 'initiating methionine' -14 1  
1 9ESC GLY A 2  ? UNP P14902 ? ? 'expression tag'        -13 2  
1 9ESC SER A 3  ? UNP P14902 ? ? 'expression tag'        -12 3  
1 9ESC SER A 4  ? UNP P14902 ? ? 'expression tag'        -11 4  
1 9ESC HIS A 5  ? UNP P14902 ? ? 'expression tag'        -10 5  
1 9ESC HIS A 6  ? UNP P14902 ? ? 'expression tag'        -9  6  
1 9ESC HIS A 7  ? UNP P14902 ? ? 'expression tag'        -8  7  
1 9ESC HIS A 8  ? UNP P14902 ? ? 'expression tag'        -7  8  
1 9ESC HIS A 9  ? UNP P14902 ? ? 'expression tag'        -6  9  
1 9ESC HIS A 10 ? UNP P14902 ? ? 'expression tag'        -5  10 
1 9ESC SER A 11 ? UNP P14902 ? ? 'expression tag'        -4  11 
1 9ESC ALA A 12 ? UNP P14902 ? ? 'expression tag'        -3  12 
1 9ESC ALA A 13 ? UNP P14902 ? ? 'expression tag'        -2  13 
1 9ESC LEU A 14 ? UNP P14902 ? ? 'expression tag'        -1  14 
1 9ESC GLU A 15 ? UNP P14902 ? ? 'expression tag'        0   15 
1 9ESC VAL A 16 ? UNP P14902 ? ? 'expression tag'        1   16 
1 9ESC LEU A 17 ? UNP P14902 ? ? 'expression tag'        2   17 
1 9ESC PHE A 18 ? UNP P14902 ? ? 'expression tag'        3   18 
1 9ESC GLN A 19 ? UNP P14902 ? ? 'expression tag'        4   19 
1 9ESC GLY A 20 ? UNP P14902 ? ? 'expression tag'        5   20 
1 9ESC PRO A 21 ? UNP P14902 ? ? 'expression tag'        6   21 
1 9ESC HIS A 22 ? UNP P14902 ? ? 'expression tag'        7   22 
1 9ESC MET A 23 ? UNP P14902 ? ? 'expression tag'        8   23 
2 9ESC MET B 1  ? UNP P14902 ? ? 'initiating methionine' -14 24 
2 9ESC GLY B 2  ? UNP P14902 ? ? 'expression tag'        -13 25 
2 9ESC SER B 3  ? UNP P14902 ? ? 'expression tag'        -12 26 
2 9ESC SER B 4  ? UNP P14902 ? ? 'expression tag'        -11 27 
2 9ESC HIS B 5  ? UNP P14902 ? ? 'expression tag'        -10 28 
2 9ESC HIS B 6  ? UNP P14902 ? ? 'expression tag'        -9  29 
2 9ESC HIS B 7  ? UNP P14902 ? ? 'expression tag'        -8  30 
2 9ESC HIS B 8  ? UNP P14902 ? ? 'expression tag'        -7  31 
2 9ESC HIS B 9  ? UNP P14902 ? ? 'expression tag'        -6  32 
2 9ESC HIS B 10 ? UNP P14902 ? ? 'expression tag'        -5  33 
2 9ESC SER B 11 ? UNP P14902 ? ? 'expression tag'        -4  34 
2 9ESC ALA B 12 ? UNP P14902 ? ? 'expression tag'        -3  35 
2 9ESC ALA B 13 ? UNP P14902 ? ? 'expression tag'        -2  36 
2 9ESC LEU B 14 ? UNP P14902 ? ? 'expression tag'        -1  37 
2 9ESC GLU B 15 ? UNP P14902 ? ? 'expression tag'        0   38 
2 9ESC VAL B 16 ? UNP P14902 ? ? 'expression tag'        1   39 
2 9ESC LEU B 17 ? UNP P14902 ? ? 'expression tag'        2   40 
2 9ESC PHE B 18 ? UNP P14902 ? ? 'expression tag'        3   41 
2 9ESC GLN B 19 ? UNP P14902 ? ? 'expression tag'        4   42 
2 9ESC GLY B 20 ? UNP P14902 ? ? 'expression tag'        5   43 
2 9ESC PRO B 21 ? UNP P14902 ? ? 'expression tag'        6   44 
2 9ESC HIS B 22 ? UNP P14902 ? ? 'expression tag'        7   45 
2 9ESC 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)' 4620  ? 
1 MORE         -51   ? 
1 'SSA (A^2)'  30250 ? 
# 
_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 12  ? GLY A 20  ? ALA A -3  GLY A 5   1 ? 9  
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 ? LEU A 249 ? VAL A 229 LEU A 234 1 ? 6  
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 ? ARG A 311 ? GLY A 286 ARG A 296 1 ? 11 
HELX_P HELX_P23 AC5 ARG A 312 ? MET A 314 ? ARG A 297 MET A 299 5 ? 3  
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 ? LEU B 249 ? VAL B 229 LEU B 234 1 ? 6  
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 ? ARG B 311 ? GLY B 286 ARG B 296 1 ? 11 
HELX_P HELX_P50 AF5 ARG B 312 ? MET B 314 ? ARG B 297 MET B 299 5 ? 3  
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 GLY B 396 ? LYS B 412 ? GLY B 381 LYS B 397 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 323 SG  ? ? ? 1_555 B CYS   323 SG ? ? A CYS 308 B CYS   308 1_555 ? ? ? ? ? ? ? 2.046 ? ? 
metalc1 metalc ? ? A HIS 361 NE2 ? ? ? 1_555 C HEM   .   FE ? ? A HIS 346 A HEM   501 1_555 ? ? ? ? ? ? ? 2.028 ? ? 
metalc2 metalc ? ? C HEM .   FE  ? ? ? 1_555 D A1H6R .   N  ? ? A HEM 501 A A1H6R 502 1_555 ? ? ? ? ? ? ? 2.045 ? ? 
metalc3 metalc ? ? B HIS 361 NE2 ? ? ? 1_555 E HEM   .   FE ? ? B HIS 346 B HEM   501 1_555 ? ? ? ? ? ? ? 2.055 ? ? 
metalc4 metalc ? ? E HEM .   FE  ? ? ? 1_555 F A1H6R .   N  ? ? B HEM 501 B A1H6R 502 1_555 ? ? ? ? ? ? ? 2.117 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 361 ? A HIS 346 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NA ? C HEM   . ? A HEM   501 ? 1_555 91.4  ? 
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 92.3  ? 
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 91.9  ? 
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 90.8  ? 
5  NA  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 NC ? C HEM   . ? A HEM   501 ? 1_555 177.7 ? 
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 88.7  ? 
7  NE2 ? A HIS 361 ? A HIS 346 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM   . ? A HEM   501 ? 1_555 87.6  ? 
8  NA  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM   . ? A HEM   501 ? 1_555 88.1  ? 
9  NB  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM   . ? A HEM   501 ? 1_555 179.9 ? 
10 NC  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 ND ? C HEM   . ? A HEM   501 ? 1_555 91.4  ? 
11 NE2 ? A HIS 361 ? A HIS 346 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 N  ? D A1H6R . ? A A1H6R 502 ? 1_555 168.5 ? 
12 NA  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 N  ? D A1H6R . ? A A1H6R 502 ? 1_555 99.4  ? 
13 NB  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 N  ? D A1H6R . ? A A1H6R 502 ? 1_555 83.5  ? 
14 NC  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 N  ? D A1H6R . ? A A1H6R 502 ? 1_555 78.4  ? 
15 ND  ? C HEM .   ? A HEM 501 ? 1_555 FE ? C HEM . ? A HEM 501 ? 1_555 N  ? D A1H6R . ? A A1H6R 502 ? 1_555 96.7  ? 
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 91.9  ? 
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 91.3  ? 
18 NA  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 NB ? E HEM   . ? B HEM   501 ? 1_555 91.2  ? 
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 89.4  ? 
20 NA  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 NC ? E HEM   . ? B HEM   501 ? 1_555 178.6 ? 
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 88.2  ? 
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 86.8  ? 
23 NA  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 ND ? E HEM   . ? B HEM   501 ? 1_555 89.0  ? 
24 NB  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 ND ? E HEM   . ? B HEM   501 ? 1_555 178.1 ? 
25 NC  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 ND ? E HEM   . ? B HEM   501 ? 1_555 91.7  ? 
26 NE2 ? B HIS 361 ? B HIS 346 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 N  ? F A1H6R . ? B A1H6R 502 ? 1_555 164.7 ? 
27 NA  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 N  ? F A1H6R . ? B A1H6R 502 ? 1_555 103.3 ? 
28 NB  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 N  ? F A1H6R . ? B A1H6R 502 ? 1_555 87.2  ? 
29 NC  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 N  ? F A1H6R . ? B A1H6R 502 ? 1_555 75.4  ? 
30 ND  ? E HEM .   ? B HEM 501 ? 1_555 FE ? E HEM . ? B HEM 501 ? 1_555 N  ? F A1H6R . ? B A1H6R 502 ? 1_555 94.5  ? 
# 
_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                   9ESC 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 27  ? ? 33.06   67.48  
2 1 ASN A 133 ? ? -100.01 54.52  
3 1 LEU A 243 ? ? -140.24 59.83  
4 1 ILE A 354 ? ? -120.98 -56.30 
5 1 ASN B 27  ? ? 34.10   66.66  
6 1 ASN B 133 ? ? -99.60  54.90  
7 1 LEU B 243 ? ? -140.57 59.78  
8 1 ILE B 354 ? ? -120.75 -56.55 
# 
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 GLN 361 ? A GLN 376 
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 GLN 361 ? B GLN 376 
58 1 Y 1 B PRO 362 ? B PRO 377 
59 1 Y 1 B LYS 363 ? B LYS 378 
60 1 Y 1 B GLU 364 ? B GLU 379 
61 1 Y 1 B ASN 365 ? B ASN 380 
62 1 Y 1 B LYS 366 ? B LYS 381 
63 1 Y 1 B THR 367 ? B THR 382 
64 1 Y 1 B SER 368 ? B SER 383 
65 1 Y 1 B GLU 369 ? B GLU 384 
66 1 Y 1 B ASP 370 ? B ASP 385 
67 1 Y 1 B PRO 371 ? B PRO 386 
68 1 Y 1 B SER 372 ? B SER 387 
69 1 Y 1 B LYS 373 ? B LYS 388 
70 1 Y 1 B LEU 374 ? B LEU 389 
71 1 Y 1 B GLU 375 ? B GLU 390 
72 1 Y 1 B ALA 376 ? B ALA 391 
73 1 Y 1 B LYS 377 ? B LYS 392 
74 1 Y 1 B GLY 378 ? B GLY 393 
75 1 Y 1 B THR 379 ? B THR 394 
76 1 Y 1 B GLU 402 ? B GLU 417 
77 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 
A1H6R N1   N  N N 1   
A1H6R C4   C  N N 2   
A1H6R C5   C  N N 3   
A1H6R C6   C  N N 4   
A1H6R C7   C  N N 5   
A1H6R C8   C  N N 6   
A1H6R C10  C  N N 7   
A1H6R C13  C  N N 8   
A1H6R C15  C  N N 9   
A1H6R O    O  N N 10  
A1H6R C    C  N S 11  
A1H6R C1   C  N N 12  
A1H6R C3   C  N N 13  
A1H6R C2   C  N N 14  
A1H6R C16  C  N N 15  
A1H6R N    N  N N 16  
A1H6R C14  C  N R 17  
A1H6R S    S  N N 18  
A1H6R C9   C  N N 19  
A1H6R C12  C  N N 20  
A1H6R C11  C  N N 21  
A1H6R H2   H  N N 22  
A1H6R H3   H  N N 23  
A1H6R H4   H  N N 24  
A1H6R H5   H  N N 25  
A1H6R H6   H  N N 26  
A1H6R H7   H  N N 27  
A1H6R H10  H  N N 28  
A1H6R H11  H  N N 29  
A1H6R H12  H  N N 30  
A1H6R H13  H  N N 31  
A1H6R H14  H  N N 32  
A1H6R H15  H  N N 33  
A1H6R H16  H  N N 34  
A1H6R H17  H  N N 35  
A1H6R H18  H  N N 36  
A1H6R H19  H  N N 37  
A1H6R H20  H  N N 38  
A1H6R H21  H  N N 39  
A1H6R H22  H  N N 40  
A1H6R H23  H  N N 41  
A1H6R H24  H  N N 42  
A1H6R H25  H  N N 43  
A1H6R H27  H  N N 44  
A1H6R H28  H  N N 45  
A1H6R H29  H  N N 46  
A1H6R H30  H  N N 47  
A1H6R H31  H  N N 48  
A1H6R H32  H  N N 49  
ALA   N    N  N N 50  
ALA   CA   C  N S 51  
ALA   C    C  N N 52  
ALA   O    O  N N 53  
ALA   CB   C  N N 54  
ALA   OXT  O  N N 55  
ALA   H    H  N N 56  
ALA   H2   H  N N 57  
ALA   HA   H  N N 58  
ALA   HB1  H  N N 59  
ALA   HB2  H  N N 60  
ALA   HB3  H  N N 61  
ALA   HXT  H  N N 62  
ARG   N    N  N N 63  
ARG   CA   C  N S 64  
ARG   C    C  N N 65  
ARG   O    O  N N 66  
ARG   CB   C  N N 67  
ARG   CG   C  N N 68  
ARG   CD   C  N N 69  
ARG   NE   N  N N 70  
ARG   CZ   C  N N 71  
ARG   NH1  N  N N 72  
ARG   NH2  N  N N 73  
ARG   OXT  O  N N 74  
ARG   H    H  N N 75  
ARG   H2   H  N N 76  
ARG   HA   H  N N 77  
ARG   HB2  H  N N 78  
ARG   HB3  H  N N 79  
ARG   HG2  H  N N 80  
ARG   HG3  H  N N 81  
ARG   HD2  H  N N 82  
ARG   HD3  H  N N 83  
ARG   HE   H  N N 84  
ARG   HH11 H  N N 85  
ARG   HH12 H  N N 86  
ARG   HH21 H  N N 87  
ARG   HH22 H  N N 88  
ARG   HXT  H  N N 89  
ASN   N    N  N N 90  
ASN   CA   C  N S 91  
ASN   C    C  N N 92  
ASN   O    O  N N 93  
ASN   CB   C  N N 94  
ASN   CG   C  N N 95  
ASN   OD1  O  N N 96  
ASN   ND2  N  N N 97  
ASN   OXT  O  N N 98  
ASN   H    H  N N 99  
ASN   H2   H  N N 100 
ASN   HA   H  N N 101 
ASN   HB2  H  N N 102 
ASN   HB3  H  N N 103 
ASN   HD21 H  N N 104 
ASN   HD22 H  N N 105 
ASN   HXT  H  N N 106 
ASP   N    N  N N 107 
ASP   CA   C  N S 108 
ASP   C    C  N N 109 
ASP   O    O  N N 110 
ASP   CB   C  N N 111 
ASP   CG   C  N N 112 
ASP   OD1  O  N N 113 
ASP   OD2  O  N N 114 
ASP   OXT  O  N N 115 
ASP   H    H  N N 116 
ASP   H2   H  N N 117 
ASP   HA   H  N N 118 
ASP   HB2  H  N N 119 
ASP   HB3  H  N N 120 
ASP   HD2  H  N N 121 
ASP   HXT  H  N N 122 
CYS   N    N  N N 123 
CYS   CA   C  N R 124 
CYS   C    C  N N 125 
CYS   O    O  N N 126 
CYS   CB   C  N N 127 
CYS   SG   S  N N 128 
CYS   OXT  O  N N 129 
CYS   H    H  N N 130 
CYS   H2   H  N N 131 
CYS   HA   H  N N 132 
CYS   HB2  H  N N 133 
CYS   HB3  H  N N 134 
CYS   HG   H  N N 135 
CYS   HXT  H  N N 136 
GLN   N    N  N N 137 
GLN   CA   C  N S 138 
GLN   C    C  N N 139 
GLN   O    O  N N 140 
GLN   CB   C  N N 141 
GLN   CG   C  N N 142 
GLN   CD   C  N N 143 
GLN   OE1  O  N N 144 
GLN   NE2  N  N N 145 
GLN   OXT  O  N N 146 
GLN   H    H  N N 147 
GLN   H2   H  N N 148 
GLN   HA   H  N N 149 
GLN   HB2  H  N N 150 
GLN   HB3  H  N N 151 
GLN   HG2  H  N N 152 
GLN   HG3  H  N N 153 
GLN   HE21 H  N N 154 
GLN   HE22 H  N N 155 
GLN   HXT  H  N N 156 
GLU   N    N  N N 157 
GLU   CA   C  N S 158 
GLU   C    C  N N 159 
GLU   O    O  N N 160 
GLU   CB   C  N N 161 
GLU   CG   C  N N 162 
GLU   CD   C  N N 163 
GLU   OE1  O  N N 164 
GLU   OE2  O  N N 165 
GLU   OXT  O  N N 166 
GLU   H    H  N N 167 
GLU   H2   H  N N 168 
GLU   HA   H  N N 169 
GLU   HB2  H  N N 170 
GLU   HB3  H  N N 171 
GLU   HG2  H  N N 172 
GLU   HG3  H  N N 173 
GLU   HE2  H  N N 174 
GLU   HXT  H  N N 175 
GLY   N    N  N N 176 
GLY   CA   C  N N 177 
GLY   C    C  N N 178 
GLY   O    O  N N 179 
GLY   OXT  O  N N 180 
GLY   H    H  N N 181 
GLY   H2   H  N N 182 
GLY   HA2  H  N N 183 
GLY   HA3  H  N N 184 
GLY   HXT  H  N N 185 
HEM   CHA  C  N N 186 
HEM   CHB  C  N N 187 
HEM   CHC  C  N N 188 
HEM   CHD  C  N N 189 
HEM   C1A  C  Y N 190 
HEM   C2A  C  Y N 191 
HEM   C3A  C  Y N 192 
HEM   C4A  C  Y N 193 
HEM   CMA  C  N N 194 
HEM   CAA  C  N N 195 
HEM   CBA  C  N N 196 
HEM   CGA  C  N N 197 
HEM   O1A  O  N N 198 
HEM   O2A  O  N N 199 
HEM   C1B  C  N N 200 
HEM   C2B  C  N N 201 
HEM   C3B  C  N N 202 
HEM   C4B  C  N N 203 
HEM   CMB  C  N N 204 
HEM   CAB  C  N N 205 
HEM   CBB  C  N N 206 
HEM   C1C  C  Y N 207 
HEM   C2C  C  Y N 208 
HEM   C3C  C  Y N 209 
HEM   C4C  C  Y N 210 
HEM   CMC  C  N N 211 
HEM   CAC  C  N N 212 
HEM   CBC  C  N N 213 
HEM   C1D  C  N N 214 
HEM   C2D  C  N N 215 
HEM   C3D  C  N N 216 
HEM   C4D  C  N N 217 
HEM   CMD  C  N N 218 
HEM   CAD  C  N N 219 
HEM   CBD  C  N N 220 
HEM   CGD  C  N N 221 
HEM   O1D  O  N N 222 
HEM   O2D  O  N N 223 
HEM   NA   N  Y N 224 
HEM   NB   N  N N 225 
HEM   NC   N  Y N 226 
HEM   ND   N  N N 227 
HEM   FE   FE N N 228 
HEM   HHB  H  N N 229 
HEM   HHC  H  N N 230 
HEM   HHD  H  N N 231 
HEM   HMA  H  N N 232 
HEM   HMAA H  N N 233 
HEM   HMAB H  N N 234 
HEM   HAA  H  N N 235 
HEM   HAAA H  N N 236 
HEM   HBA  H  N N 237 
HEM   HBAA H  N N 238 
HEM   HMB  H  N N 239 
HEM   HMBA H  N N 240 
HEM   HMBB H  N N 241 
HEM   HAB  H  N N 242 
HEM   HBB  H  N N 243 
HEM   HBBA H  N N 244 
HEM   HMC  H  N N 245 
HEM   HMCA H  N N 246 
HEM   HMCB H  N N 247 
HEM   HAC  H  N N 248 
HEM   HBC  H  N N 249 
HEM   HBCA H  N N 250 
HEM   HMD  H  N N 251 
HEM   HMDA H  N N 252 
HEM   HMDB H  N N 253 
HEM   HAD  H  N N 254 
HEM   HADA H  N N 255 
HEM   HBD  H  N N 256 
HEM   HBDA H  N N 257 
HEM   H2A  H  N N 258 
HEM   H2D  H  N N 259 
HEM   HHA  H  N N 260 
HIS   N    N  N N 261 
HIS   CA   C  N S 262 
HIS   C    C  N N 263 
HIS   O    O  N N 264 
HIS   CB   C  N N 265 
HIS   CG   C  Y N 266 
HIS   ND1  N  Y N 267 
HIS   CD2  C  Y N 268 
HIS   CE1  C  Y N 269 
HIS   NE2  N  Y N 270 
HIS   OXT  O  N N 271 
HIS   H    H  N N 272 
HIS   H2   H  N N 273 
HIS   HA   H  N N 274 
HIS   HB2  H  N N 275 
HIS   HB3  H  N N 276 
HIS   HD1  H  N N 277 
HIS   HD2  H  N N 278 
HIS   HE1  H  N N 279 
HIS   HE2  H  N N 280 
HIS   HXT  H  N N 281 
HOH   O    O  N N 282 
HOH   H1   H  N N 283 
HOH   H2   H  N N 284 
ILE   N    N  N N 285 
ILE   CA   C  N S 286 
ILE   C    C  N N 287 
ILE   O    O  N N 288 
ILE   CB   C  N S 289 
ILE   CG1  C  N N 290 
ILE   CG2  C  N N 291 
ILE   CD1  C  N N 292 
ILE   OXT  O  N N 293 
ILE   H    H  N N 294 
ILE   H2   H  N N 295 
ILE   HA   H  N N 296 
ILE   HB   H  N N 297 
ILE   HG12 H  N N 298 
ILE   HG13 H  N N 299 
ILE   HG21 H  N N 300 
ILE   HG22 H  N N 301 
ILE   HG23 H  N N 302 
ILE   HD11 H  N N 303 
ILE   HD12 H  N N 304 
ILE   HD13 H  N N 305 
ILE   HXT  H  N N 306 
LEU   N    N  N N 307 
LEU   CA   C  N S 308 
LEU   C    C  N N 309 
LEU   O    O  N N 310 
LEU   CB   C  N N 311 
LEU   CG   C  N N 312 
LEU   CD1  C  N N 313 
LEU   CD2  C  N N 314 
LEU   OXT  O  N N 315 
LEU   H    H  N N 316 
LEU   H2   H  N N 317 
LEU   HA   H  N N 318 
LEU   HB2  H  N N 319 
LEU   HB3  H  N N 320 
LEU   HG   H  N N 321 
LEU   HD11 H  N N 322 
LEU   HD12 H  N N 323 
LEU   HD13 H  N N 324 
LEU   HD21 H  N N 325 
LEU   HD22 H  N N 326 
LEU   HD23 H  N N 327 
LEU   HXT  H  N N 328 
LYS   N    N  N N 329 
LYS   CA   C  N S 330 
LYS   C    C  N N 331 
LYS   O    O  N N 332 
LYS   CB   C  N N 333 
LYS   CG   C  N N 334 
LYS   CD   C  N N 335 
LYS   CE   C  N N 336 
LYS   NZ   N  N N 337 
LYS   OXT  O  N N 338 
LYS   H    H  N N 339 
LYS   H2   H  N N 340 
LYS   HA   H  N N 341 
LYS   HB2  H  N N 342 
LYS   HB3  H  N N 343 
LYS   HG2  H  N N 344 
LYS   HG3  H  N N 345 
LYS   HD2  H  N N 346 
LYS   HD3  H  N N 347 
LYS   HE2  H  N N 348 
LYS   HE3  H  N N 349 
LYS   HZ1  H  N N 350 
LYS   HZ2  H  N N 351 
LYS   HZ3  H  N N 352 
LYS   HXT  H  N N 353 
MET   N    N  N N 354 
MET   CA   C  N S 355 
MET   C    C  N N 356 
MET   O    O  N N 357 
MET   CB   C  N N 358 
MET   CG   C  N N 359 
MET   SD   S  N N 360 
MET   CE   C  N N 361 
MET   OXT  O  N N 362 
MET   H    H  N N 363 
MET   H2   H  N N 364 
MET   HA   H  N N 365 
MET   HB2  H  N N 366 
MET   HB3  H  N N 367 
MET   HG2  H  N N 368 
MET   HG3  H  N N 369 
MET   HE1  H  N N 370 
MET   HE2  H  N N 371 
MET   HE3  H  N N 372 
MET   HXT  H  N N 373 
PHE   N    N  N N 374 
PHE   CA   C  N S 375 
PHE   C    C  N N 376 
PHE   O    O  N N 377 
PHE   CB   C  N N 378 
PHE   CG   C  Y N 379 
PHE   CD1  C  Y N 380 
PHE   CD2  C  Y N 381 
PHE   CE1  C  Y N 382 
PHE   CE2  C  Y N 383 
PHE   CZ   C  Y N 384 
PHE   OXT  O  N N 385 
PHE   H    H  N N 386 
PHE   H2   H  N N 387 
PHE   HA   H  N N 388 
PHE   HB2  H  N N 389 
PHE   HB3  H  N N 390 
PHE   HD1  H  N N 391 
PHE   HD2  H  N N 392 
PHE   HE1  H  N N 393 
PHE   HE2  H  N N 394 
PHE   HZ   H  N N 395 
PHE   HXT  H  N N 396 
PRO   N    N  N N 397 
PRO   CA   C  N S 398 
PRO   C    C  N N 399 
PRO   O    O  N N 400 
PRO   CB   C  N N 401 
PRO   CG   C  N N 402 
PRO   CD   C  N N 403 
PRO   OXT  O  N N 404 
PRO   H    H  N N 405 
PRO   HA   H  N N 406 
PRO   HB2  H  N N 407 
PRO   HB3  H  N N 408 
PRO   HG2  H  N N 409 
PRO   HG3  H  N N 410 
PRO   HD2  H  N N 411 
PRO   HD3  H  N N 412 
PRO   HXT  H  N N 413 
SER   N    N  N N 414 
SER   CA   C  N S 415 
SER   C    C  N N 416 
SER   O    O  N N 417 
SER   CB   C  N N 418 
SER   OG   O  N N 419 
SER   OXT  O  N N 420 
SER   H    H  N N 421 
SER   H2   H  N N 422 
SER   HA   H  N N 423 
SER   HB2  H  N N 424 
SER   HB3  H  N N 425 
SER   HG   H  N N 426 
SER   HXT  H  N N 427 
THR   N    N  N N 428 
THR   CA   C  N S 429 
THR   C    C  N N 430 
THR   O    O  N N 431 
THR   CB   C  N R 432 
THR   OG1  O  N N 433 
THR   CG2  C  N N 434 
THR   OXT  O  N N 435 
THR   H    H  N N 436 
THR   H2   H  N N 437 
THR   HA   H  N N 438 
THR   HB   H  N N 439 
THR   HG1  H  N N 440 
THR   HG21 H  N N 441 
THR   HG22 H  N N 442 
THR   HG23 H  N N 443 
THR   HXT  H  N N 444 
TRP   N    N  N N 445 
TRP   CA   C  N S 446 
TRP   C    C  N N 447 
TRP   O    O  N N 448 
TRP   CB   C  N N 449 
TRP   CG   C  Y N 450 
TRP   CD1  C  Y N 451 
TRP   CD2  C  Y N 452 
TRP   NE1  N  Y N 453 
TRP   CE2  C  Y N 454 
TRP   CE3  C  Y N 455 
TRP   CZ2  C  Y N 456 
TRP   CZ3  C  Y N 457 
TRP   CH2  C  Y N 458 
TRP   OXT  O  N N 459 
TRP   H    H  N N 460 
TRP   H2   H  N N 461 
TRP   HA   H  N N 462 
TRP   HB2  H  N N 463 
TRP   HB3  H  N N 464 
TRP   HD1  H  N N 465 
TRP   HE1  H  N N 466 
TRP   HE3  H  N N 467 
TRP   HZ2  H  N N 468 
TRP   HZ3  H  N N 469 
TRP   HH2  H  N N 470 
TRP   HXT  H  N N 471 
TYR   N    N  N N 472 
TYR   CA   C  N S 473 
TYR   C    C  N N 474 
TYR   O    O  N N 475 
TYR   CB   C  N N 476 
TYR   CG   C  Y N 477 
TYR   CD1  C  Y N 478 
TYR   CD2  C  Y N 479 
TYR   CE1  C  Y N 480 
TYR   CE2  C  Y N 481 
TYR   CZ   C  Y N 482 
TYR   OH   O  N N 483 
TYR   OXT  O  N N 484 
TYR   H    H  N N 485 
TYR   H2   H  N N 486 
TYR   HA   H  N N 487 
TYR   HB2  H  N N 488 
TYR   HB3  H  N N 489 
TYR   HD1  H  N N 490 
TYR   HD2  H  N N 491 
TYR   HE1  H  N N 492 
TYR   HE2  H  N N 493 
TYR   HH   H  N N 494 
TYR   HXT  H  N N 495 
VAL   N    N  N N 496 
VAL   CA   C  N S 497 
VAL   C    C  N N 498 
VAL   O    O  N N 499 
VAL   CB   C  N N 500 
VAL   CG1  C  N N 501 
VAL   CG2  C  N N 502 
VAL   OXT  O  N N 503 
VAL   H    H  N N 504 
VAL   H2   H  N N 505 
VAL   HA   H  N N 506 
VAL   HB   H  N N 507 
VAL   HG11 H  N N 508 
VAL   HG12 H  N N 509 
VAL   HG13 H  N N 510 
VAL   HG21 H  N N 511 
VAL   HG22 H  N N 512 
VAL   HG23 H  N N 513 
VAL   HXT  H  N N 514 
# 
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 
A1H6R C4  C5   sing N N 1   
A1H6R C4  C3   sing N N 2   
A1H6R C5  C6   sing N N 3   
A1H6R C3  C2   sing N N 4   
A1H6R C6  C1   sing N N 5   
A1H6R C2  C1   sing N N 6   
A1H6R C1  C    sing N N 7   
A1H6R C   O    sing N N 8   
A1H6R C   C7   sing N N 9   
A1H6R C16 N    sing N N 10  
A1H6R C16 N1   sing N N 11  
A1H6R C7  N1   sing N N 12  
A1H6R C7  C8   doub N N 13  
A1H6R N   C15  sing N N 14  
A1H6R N1  C14  sing N N 15  
A1H6R C10 C9   sing N N 16  
A1H6R C10 C11  sing N N 17  
A1H6R C8  C9   sing N N 18  
A1H6R C8  S    sing N N 19  
A1H6R C14 C15  sing N N 20  
A1H6R C14 S    sing N N 21  
A1H6R C9  C13  sing N N 22  
A1H6R C11 C12  sing N N 23  
A1H6R C12 C13  sing N N 24  
A1H6R C4  H2   sing N N 25  
A1H6R C4  H3   sing N N 26  
A1H6R C5  H4   sing N N 27  
A1H6R C5  H5   sing N N 28  
A1H6R C6  H6   sing N N 29  
A1H6R C6  H7   sing N N 30  
A1H6R C10 H10  sing N N 31  
A1H6R C10 H11  sing N N 32  
A1H6R C13 H12  sing N N 33  
A1H6R C13 H13  sing N N 34  
A1H6R C15 H14  sing N N 35  
A1H6R C15 H15  sing N N 36  
A1H6R O   H16  sing N N 37  
A1H6R C   H17  sing N N 38  
A1H6R C1  H18  sing N N 39  
A1H6R C3  H19  sing N N 40  
A1H6R C3  H20  sing N N 41  
A1H6R C2  H21  sing N N 42  
A1H6R C2  H22  sing N N 43  
A1H6R C16 H23  sing N N 44  
A1H6R C16 H24  sing N N 45  
A1H6R N   H25  sing N N 46  
A1H6R C14 H27  sing N N 47  
A1H6R C9  H28  sing N N 48  
A1H6R C12 H29  sing N N 49  
A1H6R C12 H30  sing N N 50  
A1H6R C11 H31  sing N N 51  
A1H6R C11 H32  sing N N 52  
ALA   N   CA   sing N N 53  
ALA   N   H    sing N N 54  
ALA   N   H2   sing N N 55  
ALA   CA  C    sing N N 56  
ALA   CA  CB   sing N N 57  
ALA   CA  HA   sing N N 58  
ALA   C   O    doub N N 59  
ALA   C   OXT  sing N N 60  
ALA   CB  HB1  sing N N 61  
ALA   CB  HB2  sing N N 62  
ALA   CB  HB3  sing N N 63  
ALA   OXT HXT  sing N N 64  
ARG   N   CA   sing N N 65  
ARG   N   H    sing N N 66  
ARG   N   H2   sing N N 67  
ARG   CA  C    sing N N 68  
ARG   CA  CB   sing N N 69  
ARG   CA  HA   sing N N 70  
ARG   C   O    doub N N 71  
ARG   C   OXT  sing N N 72  
ARG   CB  CG   sing N N 73  
ARG   CB  HB2  sing N N 74  
ARG   CB  HB3  sing N N 75  
ARG   CG  CD   sing N N 76  
ARG   CG  HG2  sing N N 77  
ARG   CG  HG3  sing N N 78  
ARG   CD  NE   sing N N 79  
ARG   CD  HD2  sing N N 80  
ARG   CD  HD3  sing N N 81  
ARG   NE  CZ   sing N N 82  
ARG   NE  HE   sing N N 83  
ARG   CZ  NH1  sing N N 84  
ARG   CZ  NH2  doub N N 85  
ARG   NH1 HH11 sing N N 86  
ARG   NH1 HH12 sing N N 87  
ARG   NH2 HH21 sing N N 88  
ARG   NH2 HH22 sing N N 89  
ARG   OXT HXT  sing N N 90  
ASN   N   CA   sing N N 91  
ASN   N   H    sing N N 92  
ASN   N   H2   sing N N 93  
ASN   CA  C    sing N N 94  
ASN   CA  CB   sing N N 95  
ASN   CA  HA   sing N N 96  
ASN   C   O    doub N N 97  
ASN   C   OXT  sing N N 98  
ASN   CB  CG   sing N N 99  
ASN   CB  HB2  sing N N 100 
ASN   CB  HB3  sing N N 101 
ASN   CG  OD1  doub N N 102 
ASN   CG  ND2  sing N N 103 
ASN   ND2 HD21 sing N N 104 
ASN   ND2 HD22 sing N N 105 
ASN   OXT HXT  sing N N 106 
ASP   N   CA   sing N N 107 
ASP   N   H    sing N N 108 
ASP   N   H2   sing N N 109 
ASP   CA  C    sing N N 110 
ASP   CA  CB   sing N N 111 
ASP   CA  HA   sing N N 112 
ASP   C   O    doub N N 113 
ASP   C   OXT  sing N N 114 
ASP   CB  CG   sing N N 115 
ASP   CB  HB2  sing N N 116 
ASP   CB  HB3  sing N N 117 
ASP   CG  OD1  doub N N 118 
ASP   CG  OD2  sing N N 119 
ASP   OD2 HD2  sing N N 120 
ASP   OXT HXT  sing N N 121 
CYS   N   CA   sing N N 122 
CYS   N   H    sing N N 123 
CYS   N   H2   sing N N 124 
CYS   CA  C    sing N N 125 
CYS   CA  CB   sing N N 126 
CYS   CA  HA   sing N N 127 
CYS   C   O    doub N N 128 
CYS   C   OXT  sing N N 129 
CYS   CB  SG   sing N N 130 
CYS   CB  HB2  sing N N 131 
CYS   CB  HB3  sing N N 132 
CYS   SG  HG   sing N N 133 
CYS   OXT HXT  sing N N 134 
GLN   N   CA   sing N N 135 
GLN   N   H    sing N N 136 
GLN   N   H2   sing N N 137 
GLN   CA  C    sing N N 138 
GLN   CA  CB   sing N N 139 
GLN   CA  HA   sing N N 140 
GLN   C   O    doub N N 141 
GLN   C   OXT  sing N N 142 
GLN   CB  CG   sing N N 143 
GLN   CB  HB2  sing N N 144 
GLN   CB  HB3  sing N N 145 
GLN   CG  CD   sing N N 146 
GLN   CG  HG2  sing N N 147 
GLN   CG  HG3  sing N N 148 
GLN   CD  OE1  doub N N 149 
GLN   CD  NE2  sing N N 150 
GLN   NE2 HE21 sing N N 151 
GLN   NE2 HE22 sing N N 152 
GLN   OXT HXT  sing N N 153 
GLU   N   CA   sing N N 154 
GLU   N   H    sing N N 155 
GLU   N   H2   sing N N 156 
GLU   CA  C    sing N N 157 
GLU   CA  CB   sing N N 158 
GLU   CA  HA   sing N N 159 
GLU   C   O    doub N N 160 
GLU   C   OXT  sing N N 161 
GLU   CB  CG   sing N N 162 
GLU   CB  HB2  sing N N 163 
GLU   CB  HB3  sing N N 164 
GLU   CG  CD   sing N N 165 
GLU   CG  HG2  sing N N 166 
GLU   CG  HG3  sing N N 167 
GLU   CD  OE1  doub N N 168 
GLU   CD  OE2  sing N N 169 
GLU   OE2 HE2  sing N N 170 
GLU   OXT HXT  sing N N 171 
GLY   N   CA   sing N N 172 
GLY   N   H    sing N N 173 
GLY   N   H2   sing N N 174 
GLY   CA  C    sing N N 175 
GLY   CA  HA2  sing N N 176 
GLY   CA  HA3  sing N N 177 
GLY   C   O    doub N N 178 
GLY   C   OXT  sing N N 179 
GLY   OXT HXT  sing N N 180 
HEM   CHA C1A  sing N N 181 
HEM   CHA C4D  doub N N 182 
HEM   CHA HHA  sing N N 183 
HEM   CHB C4A  sing N N 184 
HEM   CHB C1B  doub N N 185 
HEM   CHB HHB  sing N N 186 
HEM   CHC C4B  sing N N 187 
HEM   CHC C1C  doub N N 188 
HEM   CHC HHC  sing N N 189 
HEM   CHD C4C  doub N N 190 
HEM   CHD C1D  sing N N 191 
HEM   CHD HHD  sing N N 192 
HEM   C1A C2A  doub Y N 193 
HEM   C1A NA   sing Y N 194 
HEM   C2A C3A  sing Y N 195 
HEM   C2A CAA  sing N N 196 
HEM   C3A C4A  doub Y N 197 
HEM   C3A CMA  sing N N 198 
HEM   C4A NA   sing Y N 199 
HEM   CMA HMA  sing N N 200 
HEM   CMA HMAA sing N N 201 
HEM   CMA HMAB sing N N 202 
HEM   CAA CBA  sing N N 203 
HEM   CAA HAA  sing N N 204 
HEM   CAA HAAA sing N N 205 
HEM   CBA CGA  sing N N 206 
HEM   CBA HBA  sing N N 207 
HEM   CBA HBAA sing N N 208 
HEM   CGA O1A  doub N N 209 
HEM   CGA O2A  sing N N 210 
HEM   C1B C2B  sing N N 211 
HEM   C1B NB   sing N N 212 
HEM   C2B C3B  doub N N 213 
HEM   C2B CMB  sing N N 214 
HEM   C3B C4B  sing N N 215 
HEM   C3B CAB  sing N N 216 
HEM   C4B NB   doub N N 217 
HEM   CMB HMB  sing N N 218 
HEM   CMB HMBA sing N N 219 
HEM   CMB HMBB sing N N 220 
HEM   CAB CBB  doub N N 221 
HEM   CAB HAB  sing N N 222 
HEM   CBB HBB  sing N N 223 
HEM   CBB HBBA sing N N 224 
HEM   C1C C2C  sing Y N 225 
HEM   C1C NC   sing Y N 226 
HEM   C2C C3C  doub Y N 227 
HEM   C2C CMC  sing N N 228 
HEM   C3C C4C  sing Y N 229 
HEM   C3C CAC  sing N N 230 
HEM   C4C NC   sing Y N 231 
HEM   CMC HMC  sing N N 232 
HEM   CMC HMCA sing N N 233 
HEM   CMC HMCB sing N N 234 
HEM   CAC CBC  doub N N 235 
HEM   CAC HAC  sing N N 236 
HEM   CBC HBC  sing N N 237 
HEM   CBC HBCA sing N N 238 
HEM   C1D C2D  sing N N 239 
HEM   C1D ND   doub N N 240 
HEM   C2D C3D  doub N N 241 
HEM   C2D CMD  sing N N 242 
HEM   C3D C4D  sing N N 243 
HEM   C3D CAD  sing N N 244 
HEM   C4D ND   sing N N 245 
HEM   CMD HMD  sing N N 246 
HEM   CMD HMDA sing N N 247 
HEM   CMD HMDB sing N N 248 
HEM   CAD CBD  sing N N 249 
HEM   CAD HAD  sing N N 250 
HEM   CAD HADA sing N N 251 
HEM   CBD CGD  sing N N 252 
HEM   CBD HBD  sing N N 253 
HEM   CBD HBDA sing N N 254 
HEM   CGD O1D  doub N N 255 
HEM   CGD O2D  sing N N 256 
HEM   O2A H2A  sing N N 257 
HEM   O2D H2D  sing N N 258 
HEM   FE  NA   sing N N 259 
HEM   FE  NB   sing N N 260 
HEM   FE  NC   sing N N 261 
HEM   FE  ND   sing N N 262 
HIS   N   CA   sing N N 263 
HIS   N   H    sing N N 264 
HIS   N   H2   sing N N 265 
HIS   CA  C    sing N N 266 
HIS   CA  CB   sing N N 267 
HIS   CA  HA   sing N N 268 
HIS   C   O    doub N N 269 
HIS   C   OXT  sing N N 270 
HIS   CB  CG   sing N N 271 
HIS   CB  HB2  sing N N 272 
HIS   CB  HB3  sing N N 273 
HIS   CG  ND1  sing Y N 274 
HIS   CG  CD2  doub Y N 275 
HIS   ND1 CE1  doub Y N 276 
HIS   ND1 HD1  sing N N 277 
HIS   CD2 NE2  sing Y N 278 
HIS   CD2 HD2  sing N N 279 
HIS   CE1 NE2  sing Y N 280 
HIS   CE1 HE1  sing N N 281 
HIS   NE2 HE2  sing N N 282 
HIS   OXT HXT  sing N N 283 
HOH   O   H1   sing N N 284 
HOH   O   H2   sing N N 285 
ILE   N   CA   sing N N 286 
ILE   N   H    sing N N 287 
ILE   N   H2   sing N N 288 
ILE   CA  C    sing N N 289 
ILE   CA  CB   sing N N 290 
ILE   CA  HA   sing N N 291 
ILE   C   O    doub N N 292 
ILE   C   OXT  sing N N 293 
ILE   CB  CG1  sing N N 294 
ILE   CB  CG2  sing N N 295 
ILE   CB  HB   sing N N 296 
ILE   CG1 CD1  sing N N 297 
ILE   CG1 HG12 sing N N 298 
ILE   CG1 HG13 sing N N 299 
ILE   CG2 HG21 sing N N 300 
ILE   CG2 HG22 sing N N 301 
ILE   CG2 HG23 sing N N 302 
ILE   CD1 HD11 sing N N 303 
ILE   CD1 HD12 sing N N 304 
ILE   CD1 HD13 sing N N 305 
ILE   OXT HXT  sing N N 306 
LEU   N   CA   sing N N 307 
LEU   N   H    sing N N 308 
LEU   N   H2   sing N N 309 
LEU   CA  C    sing N N 310 
LEU   CA  CB   sing N N 311 
LEU   CA  HA   sing N N 312 
LEU   C   O    doub N N 313 
LEU   C   OXT  sing N N 314 
LEU   CB  CG   sing N N 315 
LEU   CB  HB2  sing N N 316 
LEU   CB  HB3  sing N N 317 
LEU   CG  CD1  sing N N 318 
LEU   CG  CD2  sing N N 319 
LEU   CG  HG   sing N N 320 
LEU   CD1 HD11 sing N N 321 
LEU   CD1 HD12 sing N N 322 
LEU   CD1 HD13 sing N N 323 
LEU   CD2 HD21 sing N N 324 
LEU   CD2 HD22 sing N N 325 
LEU   CD2 HD23 sing N N 326 
LEU   OXT HXT  sing N N 327 
LYS   N   CA   sing N N 328 
LYS   N   H    sing N N 329 
LYS   N   H2   sing N N 330 
LYS   CA  C    sing N N 331 
LYS   CA  CB   sing N N 332 
LYS   CA  HA   sing N N 333 
LYS   C   O    doub N N 334 
LYS   C   OXT  sing N N 335 
LYS   CB  CG   sing N N 336 
LYS   CB  HB2  sing N N 337 
LYS   CB  HB3  sing N N 338 
LYS   CG  CD   sing N N 339 
LYS   CG  HG2  sing N N 340 
LYS   CG  HG3  sing N N 341 
LYS   CD  CE   sing N N 342 
LYS   CD  HD2  sing N N 343 
LYS   CD  HD3  sing N N 344 
LYS   CE  NZ   sing N N 345 
LYS   CE  HE2  sing N N 346 
LYS   CE  HE3  sing N N 347 
LYS   NZ  HZ1  sing N N 348 
LYS   NZ  HZ2  sing N N 349 
LYS   NZ  HZ3  sing N N 350 
LYS   OXT HXT  sing N N 351 
MET   N   CA   sing N N 352 
MET   N   H    sing N N 353 
MET   N   H2   sing N N 354 
MET   CA  C    sing N N 355 
MET   CA  CB   sing N N 356 
MET   CA  HA   sing N N 357 
MET   C   O    doub N N 358 
MET   C   OXT  sing N N 359 
MET   CB  CG   sing N N 360 
MET   CB  HB2  sing N N 361 
MET   CB  HB3  sing N N 362 
MET   CG  SD   sing N N 363 
MET   CG  HG2  sing N N 364 
MET   CG  HG3  sing N N 365 
MET   SD  CE   sing N N 366 
MET   CE  HE1  sing N N 367 
MET   CE  HE2  sing N N 368 
MET   CE  HE3  sing N N 369 
MET   OXT HXT  sing N N 370 
PHE   N   CA   sing N N 371 
PHE   N   H    sing N N 372 
PHE   N   H2   sing N N 373 
PHE   CA  C    sing N N 374 
PHE   CA  CB   sing N N 375 
PHE   CA  HA   sing N N 376 
PHE   C   O    doub N N 377 
PHE   C   OXT  sing N N 378 
PHE   CB  CG   sing N N 379 
PHE   CB  HB2  sing N N 380 
PHE   CB  HB3  sing N N 381 
PHE   CG  CD1  doub Y N 382 
PHE   CG  CD2  sing Y N 383 
PHE   CD1 CE1  sing Y N 384 
PHE   CD1 HD1  sing N N 385 
PHE   CD2 CE2  doub Y N 386 
PHE   CD2 HD2  sing N N 387 
PHE   CE1 CZ   doub Y N 388 
PHE   CE1 HE1  sing N N 389 
PHE   CE2 CZ   sing Y N 390 
PHE   CE2 HE2  sing N N 391 
PHE   CZ  HZ   sing N N 392 
PHE   OXT HXT  sing N N 393 
PRO   N   CA   sing N N 394 
PRO   N   CD   sing N N 395 
PRO   N   H    sing N N 396 
PRO   CA  C    sing N N 397 
PRO   CA  CB   sing N N 398 
PRO   CA  HA   sing N N 399 
PRO   C   O    doub N N 400 
PRO   C   OXT  sing N N 401 
PRO   CB  CG   sing N N 402 
PRO   CB  HB2  sing N N 403 
PRO   CB  HB3  sing N N 404 
PRO   CG  CD   sing N N 405 
PRO   CG  HG2  sing N N 406 
PRO   CG  HG3  sing N N 407 
PRO   CD  HD2  sing N N 408 
PRO   CD  HD3  sing N N 409 
PRO   OXT HXT  sing N N 410 
SER   N   CA   sing N N 411 
SER   N   H    sing N N 412 
SER   N   H2   sing N N 413 
SER   CA  C    sing N N 414 
SER   CA  CB   sing N N 415 
SER   CA  HA   sing N N 416 
SER   C   O    doub N N 417 
SER   C   OXT  sing N N 418 
SER   CB  OG   sing N N 419 
SER   CB  HB2  sing N N 420 
SER   CB  HB3  sing N N 421 
SER   OG  HG   sing N N 422 
SER   OXT HXT  sing N N 423 
THR   N   CA   sing N N 424 
THR   N   H    sing N N 425 
THR   N   H2   sing N N 426 
THR   CA  C    sing N N 427 
THR   CA  CB   sing N N 428 
THR   CA  HA   sing N N 429 
THR   C   O    doub N N 430 
THR   C   OXT  sing N N 431 
THR   CB  OG1  sing N N 432 
THR   CB  CG2  sing N N 433 
THR   CB  HB   sing N N 434 
THR   OG1 HG1  sing N N 435 
THR   CG2 HG21 sing N N 436 
THR   CG2 HG22 sing N N 437 
THR   CG2 HG23 sing N N 438 
THR   OXT HXT  sing N N 439 
TRP   N   CA   sing N N 440 
TRP   N   H    sing N N 441 
TRP   N   H2   sing N N 442 
TRP   CA  C    sing N N 443 
TRP   CA  CB   sing N N 444 
TRP   CA  HA   sing N N 445 
TRP   C   O    doub N N 446 
TRP   C   OXT  sing N N 447 
TRP   CB  CG   sing N N 448 
TRP   CB  HB2  sing N N 449 
TRP   CB  HB3  sing N N 450 
TRP   CG  CD1  doub Y N 451 
TRP   CG  CD2  sing Y N 452 
TRP   CD1 NE1  sing Y N 453 
TRP   CD1 HD1  sing N N 454 
TRP   CD2 CE2  doub Y N 455 
TRP   CD2 CE3  sing Y N 456 
TRP   NE1 CE2  sing Y N 457 
TRP   NE1 HE1  sing N N 458 
TRP   CE2 CZ2  sing Y N 459 
TRP   CE3 CZ3  doub Y N 460 
TRP   CE3 HE3  sing N N 461 
TRP   CZ2 CH2  doub Y N 462 
TRP   CZ2 HZ2  sing N N 463 
TRP   CZ3 CH2  sing Y N 464 
TRP   CZ3 HZ3  sing N N 465 
TRP   CH2 HH2  sing N N 466 
TRP   OXT HXT  sing N N 467 
TYR   N   CA   sing N N 468 
TYR   N   H    sing N N 469 
TYR   N   H2   sing N N 470 
TYR   CA  C    sing N N 471 
TYR   CA  CB   sing N N 472 
TYR   CA  HA   sing N N 473 
TYR   C   O    doub N N 474 
TYR   C   OXT  sing N N 475 
TYR   CB  CG   sing N N 476 
TYR   CB  HB2  sing N N 477 
TYR   CB  HB3  sing N N 478 
TYR   CG  CD1  doub Y N 479 
TYR   CG  CD2  sing Y N 480 
TYR   CD1 CE1  sing Y N 481 
TYR   CD1 HD1  sing N N 482 
TYR   CD2 CE2  doub Y N 483 
TYR   CD2 HD2  sing N N 484 
TYR   CE1 CZ   doub Y N 485 
TYR   CE1 HE1  sing N N 486 
TYR   CE2 CZ   sing Y N 487 
TYR   CE2 HE2  sing N N 488 
TYR   CZ  OH   sing N N 489 
TYR   OH  HH   sing N N 490 
TYR   OXT HXT  sing N N 491 
VAL   N   CA   sing N N 492 
VAL   N   H    sing N N 493 
VAL   N   H2   sing N N 494 
VAL   CA  C    sing N N 495 
VAL   CA  CB   sing N N 496 
VAL   CA  HA   sing N N 497 
VAL   C   O    doub N N 498 
VAL   C   OXT  sing N N 499 
VAL   CB  CG1  sing N N 500 
VAL   CB  CG2  sing N N 501 
VAL   CB  HB   sing N N 502 
VAL   CG1 HG11 sing N N 503 
VAL   CG1 HG12 sing N N 504 
VAL   CG1 HG13 sing N N 505 
VAL   CG2 HG21 sing N N 506 
VAL   CG2 HG22 sing N N 507 
VAL   CG2 HG23 sing N N 508 
VAL   OXT HXT  sing N N 509 
# 
_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                    9ESC 
_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]   0.011817 
_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]   0.010864 
_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]   0.007561 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
FE 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ALA   A 1 12  ? 13.108  -22.691 -0.25   1   63.16 ? -3  ALA   A N   1 
ATOM   2    C  CA  . ALA   A 1 12  ? 14.457  -22.983 -0.741  1   63.36 ? -3  ALA   A CA  1 
ATOM   3    C  C   . ALA   A 1 12  ? 15.104  -21.715 -1.295  1   63.05 ? -3  ALA   A C   1 
ATOM   4    O  O   . ALA   A 1 12  ? 16.285  -21.469 -1.038  1   63.31 ? -3  ALA   A O   1 
ATOM   5    C  CB  . ALA   A 1 12  ? 14.407  -24.058 -1.819  1   63.64 ? -3  ALA   A CB  1 
ATOM   6    N  N   . ALA   A 1 13  ? 14.317  -20.899 -2.032  1   62.11 ? -2  ALA   A N   1 
ATOM   7    C  CA  . ALA   A 1 13  ? 14.767  -19.638 -2.625  1   61.17 ? -2  ALA   A CA  1 
ATOM   8    C  C   . ALA   A 1 13  ? 15.207  -18.641 -1.543  1   60.61 ? -2  ALA   A C   1 
ATOM   9    O  O   . ALA   A 1 13  ? 16.242  -17.986 -1.692  1   60.27 ? -2  ALA   A O   1 
ATOM   10   C  CB  . ALA   A 1 13  ? 13.658  -19.045 -3.475  1   60.91 ? -2  ALA   A CB  1 
ATOM   11   N  N   . LEU   A 1 14  ? 14.457  -18.57  -0.433  1   60.28 ? -1  LEU   A N   1 
ATOM   12   C  CA  . LEU   A 1 14  ? 14.784  -17.684 0.685   1   60.71 ? -1  LEU   A CA  1 
ATOM   13   C  C   . LEU   A 1 14  ? 16.182  -18.005 1.26    1   60.74 ? -1  LEU   A C   1 
ATOM   14   O  O   . LEU   A 1 14  ? 16.995  -17.098 1.477   1   61.64 ? -1  LEU   A O   1 
ATOM   15   C  CB  . LEU   A 1 14  ? 13.721  -17.837 1.787   1   61.21 ? -1  LEU   A CB  1 
ATOM   16   C  CG  . LEU   A 1 14  ? 12.994  -16.57  2.238   1   62.94 ? -1  LEU   A CG  1 
ATOM   17   C  CD1 . LEU   A 1 14  ? 12.015  -16.885 3.323   1   63.27 ? -1  LEU   A CD1 1 
ATOM   18   C  CD2 . LEU   A 1 14  ? 13.956  -15.533 2.754   1   63.53 ? -1  LEU   A CD2 1 
ATOM   19   N  N   . GLU   A 1 15  ? 16.457  -19.299 1.48    1   59.63 ? 0   GLU   A N   1 
ATOM   20   C  CA  . GLU   A 1 15  ? 17.72   -19.799 2.014   1   59.13 ? 0   GLU   A CA  1 
ATOM   21   C  C   . GLU   A 1 15  ? 18.871  -19.667 1.002   1   57.73 ? 0   GLU   A C   1 
ATOM   22   O  O   . GLU   A 1 15  ? 20.023  -19.546 1.414   1   57.66 ? 0   GLU   A O   1 
ATOM   23   C  CB  . GLU   A 1 15  ? 17.565  -21.265 2.47    1   61.25 ? 0   GLU   A CB  1 
ATOM   24   N  N   . VAL   A 1 16  ? 18.572  -19.715 -0.309  1   56.48 ? 1   VAL   A N   1 
ATOM   25   C  CA  . VAL   A 1 16  ? 19.606  -19.557 -1.337  1   56.13 ? 1   VAL   A CA  1 
ATOM   26   C  C   . VAL   A 1 16  ? 20.145  -18.097 -1.316  1   56.13 ? 1   VAL   A C   1 
ATOM   27   O  O   . VAL   A 1 16  ? 21.346  -17.88  -1.494  1   55.6  ? 1   VAL   A O   1 
ATOM   28   C  CB  . VAL   A 1 16  ? 19.145  -20.064 -2.741  1   56.56 ? 1   VAL   A CB  1 
ATOM   29   C  CG1 . VAL   A 1 16  ? 19.979  -19.462 -3.866  1   56.77 ? 1   VAL   A CG1 1 
ATOM   30   C  CG2 . VAL   A 1 16  ? 19.191  -21.589 -2.814  1   56.78 ? 1   VAL   A CG2 1 
ATOM   31   N  N   . LEU   A 1 17  ? 19.273  -17.115 -0.975  1   56.3  ? 2   LEU   A N   1 
ATOM   32   C  CA  . LEU   A 1 17  ? 19.688  -15.72  -0.841  1   56.74 ? 2   LEU   A CA  1 
ATOM   33   C  C   . LEU   A 1 17  ? 20.686  -15.557 0.311   1   56.96 ? 2   LEU   A C   1 
ATOM   34   O  O   . LEU   A 1 17  ? 21.659  -14.829 0.163   1   57    ? 2   LEU   A O   1 
ATOM   35   C  CB  . LEU   A 1 17  ? 18.476  -14.784 -0.609  1   56.58 ? 2   LEU   A CB  1 
ATOM   36   C  CG  . LEU   A 1 17  ? 17.743  -14.227 -1.838  1   57.53 ? 2   LEU   A CG  1 
ATOM   37   C  CD1 . LEU   A 1 17  ? 16.773  -13.159 -1.426  1   57.82 ? 2   LEU   A CD1 1 
ATOM   38   C  CD2 . LEU   A 1 17  ? 18.719  -13.655 -2.892  1   57.62 ? 2   LEU   A CD2 1 
ATOM   39   N  N   . PHE   A 1 18  ? 20.462  -16.26  1.438   1   56.95 ? 3   PHE   A N   1 
ATOM   40   C  CA  . PHE   A 1 18  ? 21.312  -16.156 2.631   1   57.5  ? 3   PHE   A CA  1 
ATOM   41   C  C   . PHE   A 1 18  ? 22.545  -17.06  2.654   1   57.29 ? 3   PHE   A C   1 
ATOM   42   O  O   . PHE   A 1 18  ? 23.591  -16.65  3.157   1   57.03 ? 3   PHE   A O   1 
ATOM   43   C  CB  . PHE   A 1 18  ? 20.497  -16.447 3.905   1   57.99 ? 3   PHE   A CB  1 
ATOM   44   C  CG  . PHE   A 1 18  ? 19.198  -15.694 4.055   1   59.14 ? 3   PHE   A CG  1 
ATOM   45   C  CD1 . PHE   A 1 18  ? 19.129  -14.34  3.784   1   59.66 ? 3   PHE   A CD1 1 
ATOM   46   C  CD2 . PHE   A 1 18  ? 18.068  -16.324 4.535   1   60.3  ? 3   PHE   A CD2 1 
ATOM   47   C  CE1 . PHE   A 1 18  ? 17.951  -13.642 3.96    1   60.45 ? 3   PHE   A CE1 1 
ATOM   48   C  CE2 . PHE   A 1 18  ? 16.882  -15.622 4.697   1   61.17 ? 3   PHE   A CE2 1 
ATOM   49   C  CZ  . PHE   A 1 18  ? 16.836  -14.28  4.418   1   60.69 ? 3   PHE   A CZ  1 
ATOM   50   N  N   . GLN   A 1 19  ? 22.399  -18.32  2.22    1   57.08 ? 4   GLN   A N   1 
ATOM   51   C  CA  . GLN   A 1 19  ? 23.495  -19.292 2.287   1   57.29 ? 4   GLN   A CA  1 
ATOM   52   C  C   . GLN   A 1 19  ? 24.254  -19.493 0.975   1   57.99 ? 4   GLN   A C   1 
ATOM   53   O  O   . GLN   A 1 19  ? 25.29   -20.151 0.967   1   58.71 ? 4   GLN   A O   1 
ATOM   54   C  CB  . GLN   A 1 19  ? 22.987  -20.639 2.827   1   58.08 ? 4   GLN   A CB  1 
ATOM   55   N  N   . GLY   A 1 20  ? 23.747  -18.938 -0.116  1   57.87 ? 5   GLY   A N   1 
ATOM   56   C  CA  . GLY   A 1 20  ? 24.395  -19.06  -1.41   1   58.23 ? 5   GLY   A CA  1 
ATOM   57   C  C   . GLY   A 1 20  ? 23.736  -20.097 -2.294  1   58.38 ? 5   GLY   A C   1 
ATOM   58   O  O   . GLY   A 1 20  ? 22.938  -20.925 -1.83   1   58.24 ? 5   GLY   A O   1 
ATOM   59   N  N   . PRO   A 1 21  ? 24.073  -20.051 -3.591  1   58.12 ? 6   PRO   A N   1 
ATOM   60   C  CA  . PRO   A 1 21  ? 23.464  -20.996 -4.536  1   58.23 ? 6   PRO   A CA  1 
ATOM   61   C  C   . PRO   A 1 21  ? 23.949  -22.437 -4.386  1   58.6  ? 6   PRO   A C   1 
ATOM   62   O  O   . PRO   A 1 21  ? 24.932  -22.819 -5.024  1   59.42 ? 6   PRO   A O   1 
ATOM   63   C  CB  . PRO   A 1 21  ? 23.835  -20.41  -5.901  1   58.96 ? 6   PRO   A CB  1 
ATOM   64   C  CG  . PRO   A 1 21  ? 25.072  -19.608 -5.665  1   59.29 ? 6   PRO   A CG  1 
ATOM   65   C  CD  . PRO   A 1 21  ? 25.004  -19.11  -4.253  1   57.58 ? 6   PRO   A CD  1 
ATOM   66   N  N   . HIS   A 1 22  ? 23.267  -23.249 -3.559  1   58.21 ? 7   HIS   A N   1 
ATOM   67   C  CA  . HIS   A 1 22  ? 23.676  -24.641 -3.372  1   58.69 ? 7   HIS   A CA  1 
ATOM   68   C  C   . HIS   A 1 22  ? 22.523  -25.595 -3.486  1   57.86 ? 7   HIS   A C   1 
ATOM   69   O  O   . HIS   A 1 22  ? 21.63   -25.625 -2.646  1   58.38 ? 7   HIS   A O   1 
ATOM   70   C  CB  . HIS   A 1 22  ? 24.475  -24.843 -2.087  1   61.17 ? 7   HIS   A CB  1 
ATOM   71   C  CG  . HIS   A 1 22  ? 25.788  -24.131 -2.147  1   65.91 ? 7   HIS   A CG  1 
ATOM   72   N  ND1 . HIS   A 1 22  ? 26.826  -24.594 -2.954  1   68.54 ? 7   HIS   A ND1 1 
ATOM   73   C  CD2 . HIS   A 1 22  ? 26.154  -22.95  -1.595  1   67.89 ? 7   HIS   A CD2 1 
ATOM   74   C  CE1 . HIS   A 1 22  ? 27.8    -23.707 -2.83   1   69.48 ? 7   HIS   A CE1 1 
ATOM   75   N  NE2 . HIS   A 1 22  ? 27.446  -22.701 -2.018  1   69.63 ? 7   HIS   A NE2 1 
ATOM   76   N  N   . MET   A 1 23  ? 22.536  -26.375 -4.556  1   56.64 ? 8   MET   A N   1 
ATOM   77   C  CA  . MET   A 1 23  ? 21.472  -27.318 -4.833  1   55.92 ? 8   MET   A CA  1 
ATOM   78   C  C   . MET   A 1 23  ? 21.667  -28.676 -4.163  1   55.55 ? 8   MET   A C   1 
ATOM   79   O  O   . MET   A 1 23  ? 21.815  -29.704 -4.835  1   55.47 ? 8   MET   A O   1 
ATOM   80   C  CB  . MET   A 1 23  ? 21.25   -27.467 -6.335  1   55.74 ? 8   MET   A CB  1 
ATOM   81   C  CG  . MET   A 1 23  ? 19.834  -27.803 -6.68   1   57.46 ? 8   MET   A CG  1 
ATOM   82   S  SD  . MET   A 1 23  ? 19.718  -28.029 -8.45   1   61.6  ? 8   MET   A SD  1 
ATOM   83   C  CE  . MET   A 1 23  ? 19.644  -26.321 -8.975  1   60.04 ? 8   MET   A CE  1 
ATOM   84   N  N   . TRP   A 1 24  ? 21.613  -28.674 -2.823  1   54.84 ? 9   TRP   A N   1 
ATOM   85   C  CA  . TRP   A 1 24  ? 21.663  -29.895 -2.015  1   53.98 ? 9   TRP   A CA  1 
ATOM   86   C  C   . TRP   A 1 24  ? 20.354  -30.721 -2.176  1   52.34 ? 9   TRP   A C   1 
ATOM   87   O  O   . TRP   A 1 24  ? 20.325  -31.906 -1.85   1   52.21 ? 9   TRP   A O   1 
ATOM   88   C  CB  . TRP   A 1 24  ? 21.911  -29.542 -0.535  1   54.04 ? 9   TRP   A CB  1 
ATOM   89   N  N   . THR   A 1 25  ? 19.279  -30.099 -2.692  1   50.98 ? 10  THR   A N   1 
ATOM   90   C  CA  . THR   A 1 25  ? 18.015  -30.771 -2.925  1   50.61 ? 10  THR   A CA  1 
ATOM   91   C  C   . THR   A 1 25  ? 17.244  -30.167 -4.114  1   49.22 ? 10  THR   A C   1 
ATOM   92   O  O   . THR   A 1 25  ? 17.457  -28.998 -4.481  1   49.6  ? 10  THR   A O   1 
ATOM   93   C  CB  . THR   A 1 25  ? 17.148  -30.676 -1.661  1   52.55 ? 10  THR   A CB  1 
ATOM   94   O  OG1 . THR   A 1 25  ? 15.972  -31.447 -1.874  1   54.72 ? 10  THR   A OG1 1 
ATOM   95   C  CG2 . THR   A 1 25  ? 16.772  -29.253 -1.333  1   52.52 ? 10  THR   A CG2 1 
ATOM   96   N  N   . ILE   A 1 26  ? 16.329  -30.968 -4.708  1   46.95 ? 11  ILE   A N   1 
ATOM   97   C  CA  . ILE   A 1 26  ? 15.47   -30.419 -5.746  1   45.21 ? 11  ILE   A CA  1 
ATOM   98   C  C   . ILE   A 1 26  ? 14.136  -30.023 -5.121  1   43.41 ? 11  ILE   A C   1 
ATOM   99   O  O   . ILE   A 1 26  ? 13.221  -30.834 -4.91   1   42.62 ? 11  ILE   A O   1 
ATOM   100  C  CB  . ILE   A 1 26  ? 15.318  -31.181 -7.065  1   44.76 ? 11  ILE   A CB  1 
ATOM   101  C  CG1 . ILE   A 1 26  ? 16.708  -31.363 -7.682  1   45.23 ? 11  ILE   A CG1 1 
ATOM   102  C  CG2 . ILE   A 1 26  ? 14.41   -30.342 -8      1   44.58 ? 11  ILE   A CG2 1 
ATOM   103  C  CD1 . ILE   A 1 26  ? 16.75   -32.256 -8.687  1   45.91 ? 11  ILE   A CD1 1 
ATOM   104  N  N   . SER   A 1 27  ? 14.069  -28.737 -4.809  1   42.26 ? 12  SER   A N   1 
ATOM   105  C  CA  . SER   A 1 27  ? 12.916  -28.067 -4.243  1   42.02 ? 12  SER   A CA  1 
ATOM   106  C  C   . SER   A 1 27  ? 11.686  -28.267 -5.113  1   40.98 ? 12  SER   A C   1 
ATOM   107  O  O   . SER   A 1 27  ? 11.776  -28.254 -6.343  1   40.14 ? 12  SER   A O   1 
ATOM   108  C  CB  . SER   A 1 27  ? 13.209  -26.577 -4.145  1   44.25 ? 12  SER   A CB  1 
ATOM   109  O  OG  . SER   A 1 27  ? 12.064  -25.859 -3.721  1   47.3  ? 12  SER   A OG  1 
ATOM   110  N  N   . LYS   A 1 28  ? 10.539  -28.449 -4.465  1   40.6  ? 13  LYS   A N   1 
ATOM   111  C  CA  . LYS   A 1 28  ? 9.253   -28.587 -5.131  1   40.86 ? 13  LYS   A CA  1 
ATOM   112  C  C   . LYS   A 1 28  ? 8.88    -27.332 -5.938  1   39.76 ? 13  LYS   A C   1 
ATOM   113  O  O   . LYS   A 1 28  ? 8.082   -27.431 -6.865  1   39.74 ? 13  LYS   A O   1 
ATOM   114  C  CB  . LYS   A 1 28  ? 8.158   -28.92  -4.106  1   44.11 ? 13  LYS   A CB  1 
ATOM   115  C  CG  . LYS   A 1 28  ? 8.251   -30.354 -3.594  1   50    ? 13  LYS   A CG  1 
ATOM   116  C  CD  . LYS   A 1 28  ? 7.635   -31.336 -4.585  1   55.88 ? 13  LYS   A CD  1 
ATOM   117  C  CE  . LYS   A 1 28  ? 8.192   -32.732 -4.415  1   60.68 ? 13  LYS   A CE  1 
ATOM   118  N  NZ  . LYS   A 1 28  ? 7.781   -33.627 -5.528  1   63.51 ? 13  LYS   A NZ  1 
ATOM   119  N  N   . GLU   A 1 29  ? 9.476   -26.172 -5.606  1   38.91 ? 14  GLU   A N   1 
ATOM   120  C  CA  . GLU   A 1 29  ? 9.286   -24.914 -6.308  1   39.27 ? 14  GLU   A CA  1 
ATOM   121  C  C   . GLU   A 1 29  ? 9.779   -24.961 -7.764  1   37.88 ? 14  GLU   A C   1 
ATOM   122  O  O   . GLU   A 1 29  ? 9.451   -24.069 -8.537  1   37.14 ? 14  GLU   A O   1 
ATOM   123  C  CB  . GLU   A 1 29  ? 10.019  -23.795 -5.565  1   43.71 ? 14  GLU   A CB  1 
ATOM   124  C  CG  . GLU   A 1 29  ? 9.268   -23.317 -4.333  1   53.89 ? 14  GLU   A CG  1 
ATOM   125  C  CD  . GLU   A 1 29  ? 10.14   -23.157 -3.106  1   65.58 ? 14  GLU   A CD  1 
ATOM   126  O  OE1 . GLU   A 1 29  ? 10.208  -24.131 -2.322  1   68.33 ? 14  GLU   A OE1 1 
ATOM   127  O  OE2 . GLU   A 1 29  ? 10.767  -22.082 -2.935  1   69.19 ? 14  GLU   A OE2 1 
ATOM   128  N  N   . TYR   A 1 30  ? 10.611  -25.948 -8.124  1   36.94 ? 15  TYR   A N   1 
ATOM   129  C  CA  . TYR   A 1 30  ? 11.096  -26.077 -9.496  1   36.46 ? 15  TYR   A CA  1 
ATOM   130  C  C   . TYR   A 1 30  ? 10.098  -26.844 -10.39  1   37.27 ? 15  TYR   A C   1 
ATOM   131  O  O   . TYR   A 1 30  ? 10.287  -26.874 -11.602 1   37.89 ? 15  TYR   A O   1 
ATOM   132  C  CB  . TYR   A 1 30  ? 12.49   -26.724 -9.526  1   35.45 ? 15  TYR   A CB  1 
ATOM   133  C  CG  . TYR   A 1 30  ? 13.571  -25.829 -8.952  1   35.8  ? 15  TYR   A CG  1 
ATOM   134  C  CD1 . TYR   A 1 30  ? 13.787  -24.554 -9.456  1   36    ? 15  TYR   A CD1 1 
ATOM   135  C  CD2 . TYR   A 1 30  ? 14.359  -26.25  -7.888  1   36.84 ? 15  TYR   A CD2 1 
ATOM   136  C  CE1 . TYR   A 1 30  ? 14.785  -23.733 -8.944  1   37.08 ? 15  TYR   A CE1 1 
ATOM   137  C  CE2 . TYR   A 1 30  ? 15.38   -25.446 -7.381  1   37.56 ? 15  TYR   A CE2 1 
ATOM   138  C  CZ  . TYR   A 1 30  ? 15.586  -24.184 -7.909  1   38.97 ? 15  TYR   A CZ  1 
ATOM   139  O  OH  . TYR   A 1 30  ? 16.604  -23.386 -7.437  1   41.82 ? 15  TYR   A OH  1 
ATOM   140  N  N   . HIS   A 1 31  ? 9.08    -27.497 -9.799  1   36.96 ? 16  HIS   A N   1 
ATOM   141  C  CA  . HIS   A 1 31  ? 8.03    -28.231 -10.492 1   37.79 ? 16  HIS   A CA  1 
ATOM   142  C  C   . HIS   A 1 31  ? 8.57    -29.282 -11.431 1   37.25 ? 16  HIS   A C   1 
ATOM   143  O  O   . HIS   A 1 31  ? 8.193   -29.385 -12.603 1   36.91 ? 16  HIS   A O   1 
ATOM   144  C  CB  . HIS   A 1 31  ? 7.044   -27.276 -11.178 1   40.08 ? 16  HIS   A CB  1 
ATOM   145  C  CG  . HIS   A 1 31  ? 6.356   -26.415 -10.175 1   43.99 ? 16  HIS   A CG  1 
ATOM   146  N  ND1 . HIS   A 1 31  ? 5.395   -26.935 -9.316  1   46.4  ? 16  HIS   A ND1 1 
ATOM   147  C  CD2 . HIS   A 1 31  ? 6.567   -25.118 -9.864  1   45.39 ? 16  HIS   A CD2 1 
ATOM   148  C  CE1 . HIS   A 1 31  ? 5.039   -25.931 -8.536  1   47.07 ? 16  HIS   A CE1 1 
ATOM   149  N  NE2 . HIS   A 1 31  ? 5.714   -24.816 -8.836  1   46.87 ? 16  HIS   A NE2 1 
ATOM   150  N  N   . ILE   A 1 32  ? 9.467   -30.083 -10.876 1   36.48 ? 17  ILE   A N   1 
ATOM   151  C  CA  . ILE   A 1 32  ? 10.065  -31.22  -11.53  1   35.47 ? 17  ILE   A CA  1 
ATOM   152  C  C   . ILE   A 1 32  ? 9.421   -32.4   -10.839 1   36.33 ? 17  ILE   A C   1 
ATOM   153  O  O   . ILE   A 1 32  ? 9.482   -32.516 -9.611  1   37.36 ? 17  ILE   A O   1 
ATOM   154  C  CB  . ILE   A 1 32  ? 11.608  -31.22  -11.41  1   34.49 ? 17  ILE   A CB  1 
ATOM   155  C  CG1 . ILE   A 1 32  ? 12.202  -29.923 -12.032 1   34.74 ? 17  ILE   A CG1 1 
ATOM   156  C  CG2 . ILE   A 1 32  ? 12.178  -32.482 -12.045 1   34.24 ? 17  ILE   A CG2 1 
ATOM   157  C  CD1 . ILE   A 1 32  ? 13.727  -29.711 -11.833 1   35.94 ? 17  ILE   A CD1 1 
ATOM   158  N  N   . ASP   A 1 33  ? 8.708   -33.202 -11.604 1   35.92 ? 18  ASP   A N   1 
ATOM   159  C  CA  . ASP   A 1 33  ? 8.005   -34.362 -11.105 1   36.72 ? 18  ASP   A CA  1 
ATOM   160  C  C   . ASP   A 1 33  ? 8.979   -35.532 -10.976 1   37.79 ? 18  ASP   A C   1 
ATOM   161  O  O   . ASP   A 1 33  ? 9.892   -35.67  -11.774 1   37.52 ? 18  ASP   A O   1 
ATOM   162  C  CB  . ASP   A 1 33  ? 6.838   -34.721 -12.048 1   37.04 ? 18  ASP   A CB  1 
ATOM   163  C  CG  . ASP   A 1 33  ? 5.955   -35.826 -11.484 1   39.98 ? 18  ASP   A CG  1 
ATOM   164  O  OD1 . ASP   A 1 33  ? 5.282   -35.581 -10.462 1   41.32 ? 18  ASP   A OD1 1 
ATOM   165  O  OD2 . ASP   A 1 33  ? 5.965   -36.941 -12.048 1   39.95 ? 18  ASP   A OD2 1 
ATOM   166  N  N   . GLU   A 1 34  ? 8.761   -36.399 -9.983  1   38.49 ? 19  GLU   A N   1 
ATOM   167  C  CA  . GLU   A 1 34  ? 9.635   -37.555 -9.746  1   39.15 ? 19  GLU   A CA  1 
ATOM   168  C  C   . GLU   A 1 34  ? 9.579   -38.556 -10.878 1   39.05 ? 19  GLU   A C   1 
ATOM   169  O  O   . GLU   A 1 34  ? 10.582  -39.188 -11.191 1   39.36 ? 19  GLU   A O   1 
ATOM   170  C  CB  . GLU   A 1 34  ? 9.273   -38.246 -8.408  1   41.37 ? 19  GLU   A CB  1 
ATOM   171  N  N   . GLU   A 1 35  ? 8.409   -38.696 -11.507 1   38.3  ? 20  GLU   A N   1 
ATOM   172  C  CA  . GLU   A 1 35  ? 8.238   -39.638 -12.58  1   38.1  ? 20  GLU   A CA  1 
ATOM   173  C  C   . GLU   A 1 35  ? 8.456   -39.034 -13.971 1   37.79 ? 20  GLU   A C   1 
ATOM   174  O  O   . GLU   A 1 35  ? 9.112   -39.668 -14.798 1   38.35 ? 20  GLU   A O   1 
ATOM   175  C  CB  . GLU   A 1 35  ? 6.843   -40.264 -12.475 1   40.84 ? 20  GLU   A CB  1 
ATOM   176  C  CG  . GLU   A 1 35  ? 6.533   -41.302 -13.538 1   46.9  ? 20  GLU   A CG  1 
ATOM   177  C  CD  . GLU   A 1 35  ? 5.097   -41.795 -13.512 1   54.52 ? 20  GLU   A CD  1 
ATOM   178  O  OE1 . GLU   A 1 35  ? 4.227   -41.095 -12.943 1   54.63 ? 20  GLU   A OE1 1 
ATOM   179  O  OE2 . GLU   A 1 35  ? 4.842   -42.89  -14.063 1   59.08 ? 20  GLU   A OE2 1 
ATOM   180  N  N   . VAL   A 1 36  ? 7.84    -37.872 -14.27  1   36.65 ? 21  VAL   A N   1 
ATOM   181  C  CA  . VAL   A 1 36  ? 7.899   -37.324 -15.63  1   35.88 ? 21  VAL   A CA  1 
ATOM   182  C  C   . VAL   A 1 36  ? 8.827   -36.129 -15.818 1   35.31 ? 21  VAL   A C   1 
ATOM   183  O  O   . VAL   A 1 36  ? 8.906   -35.61  -16.935 1   35.33 ? 21  VAL   A O   1 
ATOM   184  C  CB  . VAL   A 1 36  ? 6.498   -37.016 -16.176 1   36.43 ? 21  VAL   A CB  1 
ATOM   185  C  CG1 . VAL   A 1 36  ? 5.651   -38.281 -16.193 1   37.6  ? 21  VAL   A CG1 1 
ATOM   186  C  CG2 . VAL   A 1 36  ? 5.816   -35.941 -15.37  1   36.68 ? 21  VAL   A CG2 1 
ATOM   187  N  N   . GLY   A 1 37  ? 9.556   -35.745 -14.771 1   33.77 ? 22  GLY   A N   1 
ATOM   188  C  CA  . GLY   A 1 37  ? 10.532  -34.671 -14.827 1   33.17 ? 22  GLY   A CA  1 
ATOM   189  C  C   . GLY   A 1 37  ? 9.934   -33.323 -15.127 1   33.01 ? 22  GLY   A C   1 
ATOM   190  O  O   . GLY   A 1 37  ? 9.062   -32.851 -14.396 1   32.63 ? 22  GLY   A O   1 
ATOM   191  N  N   . PHE   A 1 38  ? 10.387  -32.704 -16.234 1   32.55 ? 23  PHE   A N   1 
ATOM   192  C  CA  . PHE   A 1 38  ? 9.886   -31.405 -16.668 1   31.54 ? 23  PHE   A CA  1 
ATOM   193  C  C   . PHE   A 1 38  ? 8.495   -31.467 -17.323 1   31.34 ? 23  PHE   A C   1 
ATOM   194  O  O   . PHE   A 1 38  ? 7.867   -30.424 -17.501 1   31.55 ? 23  PHE   A O   1 
ATOM   195  C  CB  . PHE   A 1 38  ? 10.894  -30.731 -17.606 1   30.97 ? 23  PHE   A CB  1 
ATOM   196  C  CG  . PHE   A 1 38  ? 12.142  -30.279 -16.888 1   30.97 ? 23  PHE   A CG  1 
ATOM   197  C  CD1 . PHE   A 1 38  ? 12.112  -29.193 -16.03  1   31.66 ? 23  PHE   A CD1 1 
ATOM   198  C  CD2 . PHE   A 1 38  ? 13.348  -30.945 -17.065 1   31.31 ? 23  PHE   A CD2 1 
ATOM   199  C  CE1 . PHE   A 1 38  ? 13.265  -28.768 -15.375 1   32.26 ? 23  PHE   A CE1 1 
ATOM   200  C  CE2 . PHE   A 1 38  ? 14.497  -30.527 -16.394 1   32.06 ? 23  PHE   A CE2 1 
ATOM   201  C  CZ  . PHE   A 1 38  ? 14.455  -29.436 -15.566 1   31.96 ? 23  PHE   A CZ  1 
ATOM   202  N  N   . ALA   A 1 39  ? 8.014   -32.655 -17.677 1   30.35 ? 24  ALA   A N   1 
ATOM   203  C  CA  . ALA   A 1 39  ? 6.687   -32.808 -18.245 1   30.52 ? 24  ALA   A CA  1 
ATOM   204  C  C   . ALA   A 1 39  ? 5.621   -32.483 -17.17  1   32.21 ? 24  ALA   A C   1 
ATOM   205  O  O   . ALA   A 1 39  ? 5.892   -32.507 -15.955 1   32.33 ? 24  ALA   A O   1 
ATOM   206  C  CB  . ALA   A 1 39  ? 6.503   -34.224 -18.758 1   29.86 ? 24  ALA   A CB  1 
ATOM   207  N  N   . LEU   A 1 40  ? 4.436   -32.104 -17.628 1   32.59 ? 25  LEU   A N   1 
ATOM   208  C  CA  . LEU   A 1 40  ? 3.34    -31.791 -16.729 1   33.37 ? 25  LEU   A CA  1 
ATOM   209  C  C   . LEU   A 1 40  ? 2.743   -33.118 -16.328 1   34.01 ? 25  LEU   A C   1 
ATOM   210  O  O   . LEU   A 1 40  ? 2.308   -33.882 -17.206 1   33.68 ? 25  LEU   A O   1 
ATOM   211  C  CB  . LEU   A 1 40  ? 2.291   -30.96  -17.476 1   34.08 ? 25  LEU   A CB  1 
ATOM   212  C  CG  . LEU   A 1 40  ? 1.075   -30.581 -16.656 1   35.61 ? 25  LEU   A CG  1 
ATOM   213  C  CD1 . LEU   A 1 40  ? 1.467   -29.649 -15.486 1   35.31 ? 25  LEU   A CD1 1 
ATOM   214  C  CD2 . LEU   A 1 40  ? 0.048   -29.961 -17.525 1   36.66 ? 25  LEU   A CD2 1 
ATOM   215  N  N   . PRO   A 1 41  ? 2.737   -33.456 -15.026 1   34.58 ? 26  PRO   A N   1 
ATOM   216  C  CA  . PRO   A 1 41  ? 2.175   -34.756 -14.636 1   35.48 ? 26  PRO   A CA  1 
ATOM   217  C  C   . PRO   A 1 41  ? 0.669   -34.803 -14.876 1   36.34 ? 26  PRO   A C   1 
ATOM   218  O  O   . PRO   A 1 41  ? 0.009   -33.788 -14.703 1   36.76 ? 26  PRO   A O   1 
ATOM   219  C  CB  . PRO   A 1 41  ? 2.559   -34.9   -13.154 1   36.13 ? 26  PRO   A CB  1 
ATOM   220  C  CG  . PRO   A 1 41  ? 2.885   -33.543 -12.695 1   36.34 ? 26  PRO   A CG  1 
ATOM   221  C  CD  . PRO   A 1 41  ? 3.271   -32.704 -13.875 1   34.05 ? 26  PRO   A CD  1 
ATOM   222  N  N   . ASN   A 1 42  ? 0.128   -35.946 -15.353 1   37.01 ? 27  ASN   A N   1 
ATOM   223  C  CA  . ASN   A 1 42  ? -1.309  -36.152 -15.638 1   38.61 ? 27  ASN   A CA  1 
ATOM   224  C  C   . ASN   A 1 42  ? -2.042  -34.905 -16.124 1   38.13 ? 27  ASN   A C   1 
ATOM   225  O  O   . ASN   A 1 42  ? -2.802  -34.301 -15.37  1   38.12 ? 27  ASN   A O   1 
ATOM   226  C  CB  . ASN   A 1 42  ? -2.024  -36.756 -14.431 1   41.67 ? 27  ASN   A CB  1 
ATOM   227  C  CG  . ASN   A 1 42  ? -1.386  -38.05  -14.038 1   48.03 ? 27  ASN   A CG  1 
ATOM   228  O  OD1 . ASN   A 1 42  ? -1.361  -39.008 -14.837 1   50.86 ? 27  ASN   A OD1 1 
ATOM   229  N  ND2 . ASN   A 1 42  ? -0.785  -38.078 -12.841 1   48.25 ? 27  ASN   A ND2 1 
ATOM   230  N  N   . PRO   A 1 43  ? -1.704  -34.424 -17.335 1   37.06 ? 28  PRO   A N   1 
ATOM   231  C  CA  . PRO   A 1 43  ? -2.313  -33.18  -17.811 1   36.46 ? 28  PRO   A CA  1 
ATOM   232  C  C   . PRO   A 1 43  ? -3.843  -33.233 -17.844 1   36.37 ? 28  PRO   A C   1 
ATOM   233  O  O   . PRO   A 1 43  ? -4.419  -34.3   -18.04  1   36.09 ? 28  PRO   A O   1 
ATOM   234  C  CB  . PRO   A 1 43  ? -1.717  -33.011 -19.217 1   36.64 ? 28  PRO   A CB  1 
ATOM   235  C  CG  . PRO   A 1 43  ? -0.456  -33.83  -19.215 1   37.09 ? 28  PRO   A CG  1 
ATOM   236  C  CD  . PRO   A 1 43  ? -0.784  -35     -18.337 1   35.92 ? 28  PRO   A CD  1 
ATOM   237  N  N   . GLN   A 1 44  ? -4.491  -32.089 -17.642 1   36.91 ? 29  GLN   A N   1 
ATOM   238  C  CA  . GLN   A 1 44  ? -5.957  -32.014 -17.714 1   37.62 ? 29  GLN   A CA  1 
ATOM   239  C  C   . GLN   A 1 44  ? -6.396  -32.236 -19.158 1   37.96 ? 29  GLN   A C   1 
ATOM   240  O  O   . GLN   A 1 44  ? -5.756  -31.721 -20.071 1   37.77 ? 29  GLN   A O   1 
ATOM   241  C  CB  . GLN   A 1 44  ? -6.441  -30.636 -17.227 1   39.63 ? 29  GLN   A CB  1 
ATOM   242  C  CG  . GLN   A 1 44  ? -7.935  -30.599 -16.87  1   43.25 ? 29  GLN   A CG  1 
ATOM   243  C  CD  . GLN   A 1 44  ? -8.251  -29.387 -16.04  1   47.09 ? 29  GLN   A CD  1 
ATOM   244  O  OE1 . GLN   A 1 44  ? -7.575  -29.103 -15.043 1   49.1  ? 29  GLN   A OE1 1 
ATOM   245  N  NE2 . GLN   A 1 44  ? -9.284  -28.642 -16.439 1   46.9  ? 29  GLN   A NE2 1 
ATOM   246  N  N   A GLU   A 1 45  ? -7.476  -33.007 -19.362 0.5 37.99 ? 30  GLU   A N   1 
ATOM   247  N  N   B GLU   A 1 45  ? -7.472  -33.014 -19.384 0.5 38.24 ? 30  GLU   A N   1 
ATOM   248  C  CA  A GLU   A 1 45  ? -7.98   -33.353 -20.69  0.5 38.28 ? 30  GLU   A CA  1 
ATOM   249  C  CA  B GLU   A 1 45  ? -7.947  -33.261 -20.748 0.5 38.78 ? 30  GLU   A CA  1 
ATOM   250  C  C   A GLU   A 1 45  ? -9.214  -32.539 -21.108 0.5 39.68 ? 30  GLU   A C   1 
ATOM   251  C  C   B GLU   A 1 45  ? -9.157  -32.393 -21.12  0.5 39.87 ? 30  GLU   A C   1 
ATOM   252  O  O   A GLU   A 1 45  ? -9.452  -32.34  -22.299 0.5 40.14 ? 30  GLU   A O   1 
ATOM   253  O  O   B GLU   A 1 45  ? -9.306  -31.991 -22.278 0.5 40.22 ? 30  GLU   A O   1 
ATOM   254  C  CB  A GLU   A 1 45  ? -8.282  -34.855 -20.743 0.5 38.99 ? 30  GLU   A CB  1 
ATOM   255  C  CB  B GLU   A 1 45  ? -8.265  -34.743 -20.973 0.5 40.44 ? 30  GLU   A CB  1 
ATOM   256  C  CG  A GLU   A 1 45  ? -7.095  -35.7   -20.328 0.5 40.81 ? 30  GLU   A CG  1 
ATOM   257  C  CG  B GLU   A 1 45  ? -8.541  -35.049 -22.438 0.5 43.8  ? 30  GLU   A CG  1 
ATOM   258  C  CD  A GLU   A 1 45  ? -7.393  -37.167 -20.119 0.5 44.23 ? 30  GLU   A CD  1 
ATOM   259  C  CD  B GLU   A 1 45  ? -9.055  -36.441 -22.741 0.5 47.27 ? 30  GLU   A CD  1 
ATOM   260  O  OE1 A GLU   A 1 45  ? -6.683  -37.807 -19.309 0.5 45.19 ? 30  GLU   A OE1 1 
ATOM   261  O  OE1 B GLU   A 1 45  ? -9.124  -37.267 -21.804 0.5 47.88 ? 30  GLU   A OE1 1 
ATOM   262  O  OE2 A GLU   A 1 45  ? -8.335  -37.679 -20.763 0.5 45.57 ? 30  GLU   A OE2 1 
ATOM   263  O  OE2 B GLU   A 1 45  ? -9.38   -36.708 -23.92  0.5 49.04 ? 30  GLU   A OE2 1 
ATOM   264  N  N   . ASN   A 1 46  ? -9.994  -32.062 -20.133 1   40.04 ? 31  ASN   A N   1 
ATOM   265  C  CA  . ASN   A 1 46  ? -11.191 -31.289 -20.39  1   41.01 ? 31  ASN   A CA  1 
ATOM   266  C  C   . ASN   A 1 46  ? -11.191 -29.971 -19.677 1   41.7  ? 31  ASN   A C   1 
ATOM   267  O  O   . ASN   A 1 46  ? -10.724 -29.872 -18.542 1   42.08 ? 31  ASN   A O   1 
ATOM   268  C  CB  . ASN   A 1 46  ? -12.43  -32.093 -19.973 1   42.49 ? 31  ASN   A CB  1 
ATOM   269  C  CG  . ASN   A 1 46  ? -12.498 -33.432 -20.643 1   46.15 ? 31  ASN   A CG  1 
ATOM   270  O  OD1 . ASN   A 1 46  ? -12.677 -33.526 -21.858 1   46.91 ? 31  ASN   A OD1 1 
ATOM   271  N  ND2 . ASN   A 1 46  ? -12.311 -34.49  -19.868 1   47.97 ? 31  ASN   A ND2 1 
ATOM   272  N  N   . LEU   A 1 47  ? -11.701 -28.951 -20.34  1   41.84 ? 32  LEU   A N   1 
ATOM   273  C  CA  . LEU   A 1 47  ? -11.841 -27.639 -19.733 1   43.09 ? 32  LEU   A CA  1 
ATOM   274  C  C   . LEU   A 1 47  ? -13.271 -27.567 -19.118 1   45.17 ? 32  LEU   A C   1 
ATOM   275  O  O   . LEU   A 1 47  ? -14.144 -28.359 -19.496 1   45.27 ? 32  LEU   A O   1 
ATOM   276  C  CB  . LEU   A 1 47  ? -11.7   -26.57  -20.821 1   42.76 ? 32  LEU   A CB  1 
ATOM   277  C  CG  . LEU   A 1 47  ? -10.282 -26.187 -21.269 1   43.86 ? 32  LEU   A CG  1 
ATOM   278  C  CD1 . LEU   A 1 47  ? -10.321 -25.074 -22.308 1   43.35 ? 32  LEU   A CD1 1 
ATOM   279  C  CD2 . LEU   A 1 47  ? -9.395  -25.771 -20.088 1   44.5  ? 32  LEU   A CD2 1 
ATOM   280  N  N   . PRO   A 1 48  ? -13.576 -26.605 -18.217 1   46.26 ? 33  PRO   A N   1 
ATOM   281  C  CA  . PRO   A 1 48  ? -14.969 -26.47  -17.745 1   47.13 ? 33  PRO   A CA  1 
ATOM   282  C  C   . PRO   A 1 48  ? -15.911 -26.221 -18.941 1   47.89 ? 33  PRO   A C   1 
ATOM   283  O  O   . PRO   A 1 48  ? -15.474 -25.69  -19.98  1   47.59 ? 33  PRO   A O   1 
ATOM   284  C  CB  . PRO   A 1 48  ? -14.901 -25.259 -16.815 1   47.85 ? 33  PRO   A CB  1 
ATOM   285  C  CG  . PRO   A 1 48  ? -13.451 -25.204 -16.383 1   48.14 ? 33  PRO   A CG  1 
ATOM   286  C  CD  . PRO   A 1 48  ? -12.712 -25.566 -17.633 1   46.15 ? 33  PRO   A CD  1 
ATOM   287  N  N   . ASP   A 1 49  ? -17.179 -26.658 -18.821 1   47.99 ? 34  ASP   A N   1 
ATOM   288  C  CA  . ASP   A 1 49  ? -18.206 -26.549 -19.86  1   48.34 ? 34  ASP   A CA  1 
ATOM   289  C  C   . ASP   A 1 49  ? -18.317 -25.165 -20.485 1   46.34 ? 34  ASP   A C   1 
ATOM   290  O  O   . ASP   A 1 49  ? -18.693 -25.04  -21.645 1   46.59 ? 34  ASP   A O   1 
ATOM   291  C  CB  . ASP   A 1 49  ? -19.565 -27.008 -19.314 1   52.49 ? 34  ASP   A CB  1 
ATOM   292  C  CG  . ASP   A 1 49  ? -19.711 -28.517 -19.249 1   61.75 ? 34  ASP   A CG  1 
ATOM   293  O  OD1 . ASP   A 1 49  ? -19.025 -29.218 -20.03  1   62.94 ? 34  ASP   A OD1 1 
ATOM   294  O  OD2 . ASP   A 1 49  ? -20.528 -28.998 -18.439 1   66.43 ? 34  ASP   A OD2 1 
ATOM   295  N  N   . PHE   A 1 50  ? -17.966 -24.133 -19.73  1   44.6  ? 35  PHE   A N   1 
ATOM   296  C  CA  . PHE   A 1 50  ? -17.971 -22.753 -20.189 1   44.2  ? 35  PHE   A CA  1 
ATOM   297  C  C   . PHE   A 1 50  ? -17.124 -22.574 -21.466 1   44.1  ? 35  PHE   A C   1 
ATOM   298  O  O   . PHE   A 1 50  ? -17.488 -21.791 -22.352 1   44.36 ? 35  PHE   A O   1 
ATOM   299  C  CB  . PHE   A 1 50  ? -17.42  -21.874 -19.061 1   44.26 ? 35  PHE   A CB  1 
ATOM   300  C  CG  . PHE   A 1 50  ? -17.37  -20.389 -19.333 1   45.18 ? 35  PHE   A CG  1 
ATOM   301  C  CD1 . PHE   A 1 50  ? -18.494 -19.6   -19.166 1   46.47 ? 35  PHE   A CD1 1 
ATOM   302  C  CD2 . PHE   A 1 50  ? -16.185 -19.772 -19.683 1   45.77 ? 35  PHE   A CD2 1 
ATOM   303  C  CE1 . PHE   A 1 50  ? -18.43  -18.226 -19.364 1   47.05 ? 35  PHE   A CE1 1 
ATOM   304  C  CE2 . PHE   A 1 50  ? -16.129 -18.405 -19.894 1   46.48 ? 35  PHE   A CE2 1 
ATOM   305  C  CZ  . PHE   A 1 50  ? -17.25  -17.641 -19.731 1   46.61 ? 35  PHE   A CZ  1 
ATOM   306  N  N   . TYR   A 1 51  ? -16.039 -23.369 -21.589 1   42.94 ? 36  TYR   A N   1 
ATOM   307  C  CA  . TYR   A 1 51  ? -15.091 -23.293 -22.683 1   41.89 ? 36  TYR   A CA  1 
ATOM   308  C  C   . TYR   A 1 51  ? -15.337 -24.289 -23.808 1   41.91 ? 36  TYR   A C   1 
ATOM   309  O  O   . TYR   A 1 51  ? -14.44  -24.494 -24.634 1   41.86 ? 36  TYR   A O   1 
ATOM   310  C  CB  . TYR   A 1 51  ? -13.674 -23.458 -22.107 1   40.94 ? 36  TYR   A CB  1 
ATOM   311  C  CG  . TYR   A 1 51  ? -13.317 -22.378 -21.103 1   40.16 ? 36  TYR   A CG  1 
ATOM   312  C  CD1 . TYR   A 1 51  ? -13.017 -21.094 -21.518 1   39.83 ? 36  TYR   A CD1 1 
ATOM   313  C  CD2 . TYR   A 1 51  ? -13.326 -22.635 -19.735 1   40.55 ? 36  TYR   A CD2 1 
ATOM   314  C  CE1 . TYR   A 1 51  ? -12.67  -20.105 -20.607 1   40.69 ? 36  TYR   A CE1 1 
ATOM   315  C  CE2 . TYR   A 1 51  ? -13.011 -21.642 -18.808 1   40.93 ? 36  TYR   A CE2 1 
ATOM   316  C  CZ  . TYR   A 1 51  ? -12.665 -20.383 -19.25  1   41.69 ? 36  TYR   A CZ  1 
ATOM   317  O  OH  . TYR   A 1 51  ? -12.332 -19.39  -18.355 1   43.07 ? 36  TYR   A OH  1 
ATOM   318  N  N   . ASN   A 1 52  ? -16.546 -24.898 -23.872 1   41.43 ? 37  ASN   A N   1 
ATOM   319  C  CA  . ASN   A 1 52  ? -16.883 -25.879 -24.92  1   41.84 ? 37  ASN   A CA  1 
ATOM   320  C  C   . ASN   A 1 52  ? -16.619 -25.394 -26.362 1   41.25 ? 37  ASN   A C   1 
ATOM   321  O  O   . ASN   A 1 52  ? -16.262 -26.209 -27.208 1   41.37 ? 37  ASN   A O   1 
ATOM   322  C  CB  . ASN   A 1 52  ? -18.347 -26.362 -24.791 1   44.41 ? 37  ASN   A CB  1 
ATOM   323  C  CG  . ASN   A 1 52  ? -18.55  -27.509 -23.825 1   49.53 ? 37  ASN   A CG  1 
ATOM   324  O  OD1 . ASN   A 1 52  ? -17.605 -28.162 -23.367 1   50.44 ? 37  ASN   A OD1 1 
ATOM   325  N  ND2 . ASN   A 1 52  ? -19.803 -27.773 -23.483 1   51.51 ? 37  ASN   A ND2 1 
ATOM   326  N  N   . ASP   A 1 53  ? -16.809 -24.089 -26.641 1   40.44 ? 38  ASP   A N   1 
ATOM   327  C  CA  . ASP   A 1 53  ? -16.603 -23.537 -27.982 1   40.64 ? 38  ASP   A CA  1 
ATOM   328  C  C   . ASP   A 1 53  ? -15.114 -23.542 -28.37  1   39.93 ? 38  ASP   A C   1 
ATOM   329  O  O   . ASP   A 1 53  ? -14.795 -23.683 -29.551 1   39.65 ? 38  ASP   A O   1 
ATOM   330  C  CB  . ASP   A 1 53  ? -17.166 -22.109 -28.097 1   43.27 ? 38  ASP   A CB  1 
ATOM   331  C  CG  . ASP   A 1 53  ? -18.681 -22.002 -27.956 1   50.58 ? 38  ASP   A CG  1 
ATOM   332  O  OD1 . ASP   A 1 53  ? -19.364 -23.051 -28.046 1   51.15 ? 38  ASP   A OD1 1 
ATOM   333  O  OD2 . ASP   A 1 53  ? -19.178 -20.874 -27.73  1   53.2  ? 38  ASP   A OD2 1 
ATOM   334  N  N   . TRP   A 1 54  ? -14.212 -23.37  -27.388 1   38.97 ? 39  TRP   A N   1 
ATOM   335  C  CA  . TRP   A 1 54  ? -12.777 -23.456 -27.657 1   38.19 ? 39  TRP   A CA  1 
ATOM   336  C  C   . TRP   A 1 54  ? -12.44  -24.912 -27.909 1   37.43 ? 39  TRP   A C   1 
ATOM   337  O  O   . TRP   A 1 54  ? -11.754 -25.208 -28.877 1   37.09 ? 39  TRP   A O   1 
ATOM   338  C  CB  . TRP   A 1 54  ? -11.952 -23.009 -26.435 1   37.8  ? 39  TRP   A CB  1 
ATOM   339  C  CG  . TRP   A 1 54  ? -11.925 -21.544 -26.141 1   37.8  ? 39  TRP   A CG  1 
ATOM   340  C  CD1 . TRP   A 1 54  ? -12.515 -20.538 -26.85  1   38.84 ? 39  TRP   A CD1 1 
ATOM   341  C  CD2 . TRP   A 1 54  ? -11.248 -20.926 -25.048 1   37.93 ? 39  TRP   A CD2 1 
ATOM   342  N  NE1 . TRP   A 1 54  ? -12.226 -19.325 -26.27  1   39.38 ? 39  TRP   A NE1 1 
ATOM   343  C  CE2 . TRP   A 1 54  ? -11.468 -19.539 -25.146 1   38.96 ? 39  TRP   A CE2 1 
ATOM   344  C  CE3 . TRP   A 1 54  ? -10.488 -21.414 -23.98  1   38.51 ? 39  TRP   A CE3 1 
ATOM   345  C  CZ2 . TRP   A 1 54  ? -10.944 -18.636 -24.224 1   39.5  ? 39  TRP   A CZ2 1 
ATOM   346  C  CZ3 . TRP   A 1 54  ? -9.972  -20.515 -23.064 1   39.46 ? 39  TRP   A CZ3 1 
ATOM   347  C  CH2 . TRP   A 1 54  ? -10.21  -19.148 -23.186 1   39.7  ? 39  TRP   A CH2 1 
ATOM   348  N  N   . MET   A 1 55  ? -12.9   -25.816 -27.021 1   37.01 ? 40  MET   A N   1 
ATOM   349  C  CA  . MET   A 1 55  ? -12.597 -27.235 -27.109 1   37.7  ? 40  MET   A CA  1 
ATOM   350  C  C   . MET   A 1 55  ? -13.063 -27.864 -28.373 1   37.75 ? 40  MET   A C   1 
ATOM   351  O  O   . MET   A 1 55  ? -12.343 -28.702 -28.924 1   37.45 ? 40  MET   A O   1 
ATOM   352  C  CB  . MET   A 1 55  ? -13.108 -28.022 -25.905 1   39.16 ? 40  MET   A CB  1 
ATOM   353  C  CG  . MET   A 1 55  ? -12.26  -27.802 -24.656 1   45.01 ? 40  MET   A CG  1 
ATOM   354  S  SD  . MET   A 1 55  ? -10.707 -28.76  -24.438 1   50.73 ? 40  MET   A SD  1 
ATOM   355  C  CE  . MET   A 1 55  ? -10.746 -29.879 -25.713 1   33.5  ? 40  MET   A CE  1 
ATOM   356  N  N   . PHE   A 1 56  ? -14.263 -27.477 -28.869 1   37.46 ? 41  PHE   A N   1 
ATOM   357  C  CA  . PHE   A 1 56  ? -14.749 -28.041 -30.123 1   37.32 ? 41  PHE   A CA  1 
ATOM   358  C  C   . PHE   A 1 56  ? -13.788 -27.73  -31.274 1   36.81 ? 41  PHE   A C   1 
ATOM   359  O  O   . PHE   A 1 56  ? -13.437 -28.627 -32.037 1   38.32 ? 41  PHE   A O   1 
ATOM   360  C  CB  . PHE   A 1 56  ? -16.19  -27.582 -30.457 1   37.77 ? 41  PHE   A CB  1 
ATOM   361  C  CG  . PHE   A 1 56  ? -16.603 -28.033 -31.845 1   39.03 ? 41  PHE   A CG  1 
ATOM   362  C  CD1 . PHE   A 1 56  ? -16.637 -27.136 -32.9   1   39.39 ? 41  PHE   A CD1 1 
ATOM   363  C  CD2 . PHE   A 1 56  ? -16.811 -29.374 -32.121 1   40.23 ? 41  PHE   A CD2 1 
ATOM   364  C  CE1 . PHE   A 1 56  ? -16.946 -27.561 -34.181 1   40.07 ? 41  PHE   A CE1 1 
ATOM   365  C  CE2 . PHE   A 1 56  ? -17.104 -29.798 -33.411 1   40.61 ? 41  PHE   A CE2 1 
ATOM   366  C  CZ  . PHE   A 1 56  ? -17.172 -28.891 -34.431 1   40.26 ? 41  PHE   A CZ  1 
ATOM   367  N  N   . ILE   A 1 57  ? -13.368 -26.473 -31.394 1   35.53 ? 42  ILE   A N   1 
ATOM   368  C  CA  . ILE   A 1 57  ? -12.45  -26.076 -32.446 1   35.7  ? 42  ILE   A CA  1 
ATOM   369  C  C   . ILE   A 1 57  ? -11.103 -26.821 -32.339 1   35.74 ? 42  ILE   A C   1 
ATOM   370  O  O   . ILE   A 1 57  ? -10.683 -27.452 -33.305 1   35.97 ? 42  ILE   A O   1 
ATOM   371  C  CB  . ILE   A 1 57  ? -12.273 -24.547 -32.449 1   36.04 ? 42  ILE   A CB  1 
ATOM   372  C  CG1 . ILE   A 1 57  ? -13.625 -23.843 -32.702 1   36.65 ? 42  ILE   A CG1 1 
ATOM   373  C  CG2 . ILE   A 1 57  ? -11.24  -24.154 -33.506 1   36.56 ? 42  ILE   A CG2 1 
ATOM   374  C  CD1 . ILE   A 1 57  ? -13.543 -22.304 -32.624 1   37.71 ? 42  ILE   A CD1 1 
ATOM   375  N  N   . ALA   A 1 58  ? -10.482 -26.826 -31.139 1   35.1  ? 43  ALA   A N   1 
ATOM   376  C  CA  . ALA   A 1 58  ? -9.204  -27.497 -30.895 1   35.3  ? 43  ALA   A CA  1 
ATOM   377  C  C   . ALA   A 1 58  ? -9.244  -28.998 -31.168 1   36.12 ? 43  ALA   A C   1 
ATOM   378  O  O   . ALA   A 1 58  ? -8.322  -29.536 -31.794 1   37.64 ? 43  ALA   A O   1 
ATOM   379  C  CB  . ALA   A 1 58  ? -8.754  -27.235 -29.465 1   35.39 ? 43  ALA   A CB  1 
ATOM   380  N  N   . LYS   A 1 59  ? -10.315 -29.668 -30.753 1   35.85 ? 44  LYS   A N   1 
ATOM   381  C  CA  . LYS   A 1 59  ? -10.459 -31.089 -30.983 1   36.73 ? 44  LYS   A CA  1 
ATOM   382  C  C   . LYS   A 1 59  ? -10.775 -31.447 -32.448 1   36.88 ? 44  LYS   A C   1 
ATOM   383  O  O   . LYS   A 1 59  ? -10.612 -32.608 -32.828 1   37.06 ? 44  LYS   A O   1 
ATOM   384  C  CB  . LYS   A 1 59  ? -11.5   -31.701 -30.025 1   38.55 ? 44  LYS   A CB  1 
ATOM   385  C  CG  . LYS   A 1 59  ? -11.013 -31.815 -28.567 1   42.93 ? 44  LYS   A CG  1 
ATOM   386  C  CD  . LYS   A 1 59  ? -9.947  -32.921 -28.377 1   46.82 ? 44  LYS   A CD  1 
ATOM   387  C  CE  . LYS   A 1 59  ? -9.54   -33.172 -26.925 1   48.15 ? 44  LYS   A CE  1 
ATOM   388  N  NZ  . LYS   A 1 59  ? -8.532  -34.274 -26.803 1   45.47 ? 44  LYS   A NZ  1 
ATOM   389  N  N   . HIS   A 1 60  ? -11.212 -30.482 -33.261 1   36.34 ? 45  HIS   A N   1 
ATOM   390  C  CA  . HIS   A 1 60  ? -11.57  -30.771 -34.654 1   36.75 ? 45  HIS   A CA  1 
ATOM   391  C  C   . HIS   A 1 60  ? -10.768 -29.966 -35.66  1   36.75 ? 45  HIS   A C   1 
ATOM   392  O  O   . HIS   A 1 60  ? -11.248 -29.708 -36.773 1   36.67 ? 45  HIS   A O   1 
ATOM   393  C  CB  . HIS   A 1 60  ? -13.083 -30.628 -34.897 1   37.22 ? 45  HIS   A CB  1 
ATOM   394  C  CG  . HIS   A 1 60  ? -13.877 -31.601 -34.077 1   39.37 ? 45  HIS   A CG  1 
ATOM   395  N  ND1 . HIS   A 1 60  ? -14.36  -31.262 -32.826 1   41.25 ? 45  HIS   A ND1 1 
ATOM   396  C  CD2 . HIS   A 1 60  ? -14.168 -32.907 -34.321 1   40.41 ? 45  HIS   A CD2 1 
ATOM   397  C  CE1 . HIS   A 1 60  ? -14.949 -32.356 -32.358 1   41.46 ? 45  HIS   A CE1 1 
ATOM   398  N  NE2 . HIS   A 1 60  ? -14.861 -33.372 -33.223 1   41.6  ? 45  HIS   A NE2 1 
ATOM   399  N  N   . LEU   A 1 61  ? -9.507  -29.622 -35.309 1   36.15 ? 46  LEU   A N   1 
ATOM   400  C  CA  . LEU   A 1 61  ? -8.65   -28.896 -36.24  1   35.86 ? 46  LEU   A CA  1 
ATOM   401  C  C   . LEU   A 1 61  ? -8.468  -29.617 -37.575 1   35.76 ? 46  LEU   A C   1 
ATOM   402  O  O   . LEU   A 1 61  ? -8.597  -28.966 -38.599 1   35.47 ? 46  LEU   A O   1 
ATOM   403  C  CB  . LEU   A 1 61  ? -7.276  -28.554 -35.643 1   36.51 ? 46  LEU   A CB  1 
ATOM   404  C  CG  . LEU   A 1 61  ? -7.239  -27.559 -34.498 1   38.26 ? 46  LEU   A CG  1 
ATOM   405  C  CD1 . LEU   A 1 61  ? -5.8    -27.317 -34.056 1   38.71 ? 46  LEU   A CD1 1 
ATOM   406  C  CD2 . LEU   A 1 61  ? -7.845  -26.233 -34.903 1   38.69 ? 46  LEU   A CD2 1 
ATOM   407  N  N   . PRO   A 1 62  ? -8.184  -30.942 -37.627 1   35.88 ? 47  PRO   A N   1 
ATOM   408  C  CA  . PRO   A 1 62  ? -8.018  -31.585 -38.933 1   36.03 ? 47  PRO   A CA  1 
ATOM   409  C  C   . PRO   A 1 62  ? -9.236  -31.407 -39.853 1   36.25 ? 47  PRO   A C   1 
ATOM   410  O  O   . PRO   A 1 62  ? -9.044  -31.072 -41.021 1   36.39 ? 47  PRO   A O   1 
ATOM   411  C  CB  . PRO   A 1 62  ? -7.771  -33.052 -38.575 1   36.73 ? 47  PRO   A CB  1 
ATOM   412  C  CG  . PRO   A 1 62  ? -7.245  -33.023 -37.183 1   36.81 ? 47  PRO   A CG  1 
ATOM   413  C  CD  . PRO   A 1 62  ? -7.992  -31.917 -36.53  1   35.23 ? 47  PRO   A CD  1 
ATOM   414  N  N   . ASP   A 1 63  ? -10.467 -31.562 -39.326 1   35.31 ? 48  ASP   A N   1 
ATOM   415  C  CA  . ASP   A 1 63  ? -11.673 -31.445 -40.151 1   35.51 ? 48  ASP   A CA  1 
ATOM   416  C  C   . ASP   A 1 63  ? -12.022 -30.026 -40.485 1   34.52 ? 48  ASP   A C   1 
ATOM   417  O  O   . ASP   A 1 63  ? -12.421 -29.767 -41.619 1   34.08 ? 48  ASP   A O   1 
ATOM   418  C  CB  . ASP   A 1 63  ? -12.877 -32.106 -39.49  1   37.96 ? 48  ASP   A CB  1 
ATOM   419  C  CG  . ASP   A 1 63  ? -12.608 -33.519 -39.087 1   43.59 ? 48  ASP   A CG  1 
ATOM   420  O  OD1 . ASP   A 1 63  ? -11.937 -34.235 -39.858 1   42.95 ? 48  ASP   A OD1 1 
ATOM   421  O  OD2 . ASP   A 1 63  ? -13.029 -33.9   -37.975 1   48.03 ? 48  ASP   A OD2 1 
ATOM   422  N  N   . LEU   A 1 64  ? -11.9   -29.107 -39.519 1   33.76 ? 49  LEU   A N   1 
ATOM   423  C  CA  . LEU   A 1 64  ? -12.223 -27.708 -39.755 1   33.8  ? 49  LEU   A CA  1 
ATOM   424  C  C   . LEU   A 1 64  ? -11.242 -27.065 -40.705 1   34.6  ? 49  LEU   A C   1 
ATOM   425  O  O   . LEU   A 1 64  ? -11.638 -26.22  -41.509 1   35.15 ? 49  LEU   A O   1 
ATOM   426  C  CB  . LEU   A 1 64  ? -12.307 -26.915 -38.458 1   33.91 ? 49  LEU   A CB  1 
ATOM   427  C  CG  . LEU   A 1 64  ? -13.392 -27.356 -37.477 1   35.84 ? 49  LEU   A CG  1 
ATOM   428  C  CD1 . LEU   A 1 64  ? -13.21  -26.633 -36.126 1   36.31 ? 49  LEU   A CD1 1 
ATOM   429  C  CD2 . LEU   A 1 64  ? -14.796 -27.108 -38.07  1   36.61 ? 49  LEU   A CD2 1 
ATOM   430  N  N   . ILE   A 1 65  ? -9.953  -27.444 -40.624 1   34.43 ? 50  ILE   A N   1 
ATOM   431  C  CA  . ILE   A 1 65  ? -8.954  -26.899 -41.525 1   34.55 ? 50  ILE   A CA  1 
ATOM   432  C  C   . ILE   A 1 65  ? -9.236  -27.38  -42.949 1   35.61 ? 50  ILE   A C   1 
ATOM   433  O  O   . ILE   A 1 65  ? -9.329  -26.559 -43.859 1   34.77 ? 50  ILE   A O   1 
ATOM   434  C  CB  . ILE   A 1 65  ? -7.491  -27.263 -41.097 1   34.62 ? 50  ILE   A CB  1 
ATOM   435  C  CG1 . ILE   A 1 65  ? -7.094  -26.569 -39.787 1   35.17 ? 50  ILE   A CG1 1 
ATOM   436  C  CG2 . ILE   A 1 65  ? -6.5    -26.915 -42.215 1   35.52 ? 50  ILE   A CG2 1 
ATOM   437  C  CD1 . ILE   A 1 65  ? -5.737  -27.096 -39.196 1   35.66 ? 50  ILE   A CD1 1 
ATOM   438  N  N   . GLU   A 1 66  ? -9.366  -28.716 -43.142 1   36.76 ? 51  GLU   A N   1 
ATOM   439  C  CA  . GLU   A 1 66  ? -9.56   -29.318 -44.459 1   38.44 ? 51  GLU   A CA  1 
ATOM   440  C  C   . GLU   A 1 66  ? -10.824 -28.808 -45.155 1   39.47 ? 51  GLU   A C   1 
ATOM   441  O  O   . GLU   A 1 66  ? -10.828 -28.61  -46.371 1   39.55 ? 51  GLU   A O   1 
ATOM   442  C  CB  . GLU   A 1 66  ? -9.592  -30.846 -44.337 1   40.44 ? 51  GLU   A CB  1 
ATOM   443  C  CG  . GLU   A 1 66  ? -9.277  -31.517 -45.656 1   47.72 ? 51  GLU   A CG  1 
ATOM   444  C  CD  . GLU   A 1 66  ? -9.523  -33.013 -45.717 1   53.69 ? 51  GLU   A CD  1 
ATOM   445  O  OE1 . GLU   A 1 66  ? -9.364  -33.692 -44.676 1   51.33 ? 51  GLU   A OE1 1 
ATOM   446  O  OE2 . GLU   A 1 66  ? -9.848  -33.509 -46.823 1   56.79 ? 51  GLU   A OE2 1 
ATOM   447  N  N   . SER   A 1 67  ? -11.9   -28.6   -44.378 1   39.63 ? 52  SER   A N   1 
ATOM   448  C  CA  . SER   A 1 67  ? -13.176 -28.125 -44.919 1   40.91 ? 52  SER   A CA  1 
ATOM   449  C  C   . SER   A 1 67  ? -13.237 -26.61  -45.158 1   41.43 ? 52  SER   A C   1 
ATOM   450  O  O   . SER   A 1 67  ? -14.239 -26.143 -45.684 1   42.07 ? 52  SER   A O   1 
ATOM   451  C  CB  . SER   A 1 67  ? -14.326 -28.533 -44.008 1   42.5  ? 52  SER   A CB  1 
ATOM   452  O  OG  . SER   A 1 67  ? -14.303 -27.766 -42.816 1   44.98 ? 52  SER   A OG  1 
ATOM   453  N  N   . GLY   A 1 68  ? -12.193 -25.867 -44.782 1   40.59 ? 53  GLY   A N   1 
ATOM   454  C  CA  . GLY   A 1 68  ? -12.158 -24.411 -44.927 1   40.37 ? 53  GLY   A CA  1 
ATOM   455  C  C   . GLY   A 1 68  ? -13.098 -23.685 -43.972 1   41.04 ? 53  GLY   A C   1 
ATOM   456  O  O   . GLY   A 1 68  ? -13.476 -22.536 -44.219 1   41.85 ? 53  GLY   A O   1 
ATOM   457  N  N   . GLN   A 1 69  ? -13.488 -24.344 -42.875 1   40.73 ? 54  GLN   A N   1 
ATOM   458  C  CA  . GLN   A 1 69  ? -14.427 -23.784 -41.9   1   41.67 ? 54  GLN   A CA  1 
ATOM   459  C  C   . GLN   A 1 69  ? -13.781 -23.292 -40.616 1   41.15 ? 54  GLN   A C   1 
ATOM   460  O  O   . GLN   A 1 69  ? -14.479 -22.723 -39.779 1   41.32 ? 54  GLN   A O   1 
ATOM   461  C  CB  . GLN   A 1 69  ? -15.484 -24.84  -41.519 1   44.74 ? 54  GLN   A CB  1 
ATOM   462  C  CG  . GLN   A 1 69  ? -16.444 -25.178 -42.651 1   50.46 ? 54  GLN   A CG  1 
ATOM   463  C  CD  . GLN   A 1 69  ? -17.826 -24.587 -42.493 1   57.52 ? 54  GLN   A CD  1 
ATOM   464  O  OE1 . GLN   A 1 69  ? -18.828 -25.279 -42.679 1   60.54 ? 54  GLN   A OE1 1 
ATOM   465  N  NE2 . GLN   A 1 69  ? -17.911 -23.3   -42.152 1   57.71 ? 54  GLN   A NE2 1 
ATOM   466  N  N   . LEU   A 1 70  ? -12.477 -23.545 -40.426 1   40.45 ? 55  LEU   A N   1 
ATOM   467  C  CA  . LEU   A 1 70  ? -11.801 -23.169 -39.19  1   39.64 ? 55  LEU   A CA  1 
ATOM   468  C  C   . LEU   A 1 70  ? -11.802 -21.664 -38.897 1   39.23 ? 55  LEU   A C   1 
ATOM   469  O  O   . LEU   A 1 70  ? -12.082 -21.275 -37.756 1   39.42 ? 55  LEU   A O   1 
ATOM   470  C  CB  . LEU   A 1 70  ? -10.368 -23.732 -39.136 1   39.39 ? 55  LEU   A CB  1 
ATOM   471  C  CG  . LEU   A 1 70  ? -9.581  -23.226 -37.919 1   40.22 ? 55  LEU   A CG  1 
ATOM   472  C  CD1 . LEU   A 1 70  ? -9.689  -24.084 -36.753 1   40.13 ? 55  LEU   A CD1 1 
ATOM   473  C  CD2 . LEU   A 1 70  ? -8.338  -22.605 -38.276 1   41.12 ? 55  LEU   A CD2 1 
ATOM   474  N  N   . ARG   A 1 71  ? -11.364 -20.845 -39.854 1   38.43 ? 56  ARG   A N   1 
ATOM   475  C  CA  . ARG   A 1 71  ? -11.276 -19.406 -39.624 1   38.88 ? 56  ARG   A CA  1 
ATOM   476  C  C   . ARG   A 1 71  ? -12.628 -18.779 -39.283 1   40.91 ? 56  ARG   A C   1 
ATOM   477  O  O   . ARG   A 1 71  ? -12.701 -17.914 -38.408 1   41.64 ? 56  ARG   A O   1 
ATOM   478  C  CB  . ARG   A 1 71  ? -10.606 -18.727 -40.798 1   39.33 ? 56  ARG   A CB  1 
ATOM   479  C  CG  . ARG   A 1 71  ? -9.122  -19     -40.753 1   41.65 ? 56  ARG   A CG  1 
ATOM   480  C  CD  . ARG   A 1 71  ? -8.447  -18.818 -42.061 1   42.94 ? 56  ARG   A CD  1 
ATOM   481  N  NE  . ARG   A 1 71  ? -6.992  -18.788 -41.938 1   41.91 ? 56  ARG   A NE  1 
ATOM   482  C  CZ  . ARG   A 1 71  ? -6.165  -18.844 -42.976 1   42.95 ? 56  ARG   A CZ  1 
ATOM   483  N  NH1 . ARG   A 1 71  ? -6.642  -19.004 -44.209 1   42.51 ? 56  ARG   A NH1 1 
ATOM   484  N  NH2 . ARG   A 1 71  ? -4.855  -18.748 -42.793 1   41.02 ? 56  ARG   A NH2 1 
ATOM   485  N  N   . GLU   A 1 72  ? -13.706 -19.279 -39.906 1   40.79 ? 57  GLU   A N   1 
ATOM   486  C  CA  . GLU   A 1 72  ? -15.057 -18.811 -39.616 1   41.26 ? 57  GLU   A CA  1 
ATOM   487  C  C   . GLU   A 1 72  ? -15.476 -19.199 -38.195 1   41.3  ? 57  GLU   A C   1 
ATOM   488  O  O   . GLU   A 1 72  ? -16.016 -18.369 -37.48  1   41.29 ? 57  GLU   A O   1 
ATOM   489  C  CB  . GLU   A 1 72  ? -16.056 -19.386 -40.635 1   44.13 ? 57  GLU   A CB  1 
ATOM   490  C  CG  . GLU   A 1 72  ? -17.435 -18.762 -40.52  1   52.75 ? 57  GLU   A CG  1 
ATOM   491  C  CD  . GLU   A 1 72  ? -18.573 -19.759 -40.579 1   65.4  ? 57  GLU   A CD  1 
ATOM   492  O  OE1 . GLU   A 1 72  ? -18.683 -20.462 -41.609 1   68.19 ? 57  GLU   A OE1 1 
ATOM   493  O  OE2 . GLU   A 1 72  ? -19.337 -19.856 -39.589 1   69.98 ? 57  GLU   A OE2 1 
ATOM   494  N  N   . ARG   A 1 73  ? -15.224 -20.453 -37.769 1   41.63 ? 58  ARG   A N   1 
ATOM   495  C  CA  . ARG   A 1 73  ? -15.551 -20.883 -36.407 1   42.46 ? 58  ARG   A CA  1 
ATOM   496  C  C   . ARG   A 1 73  ? -14.802 -20.03  -35.368 1   42.86 ? 58  ARG   A C   1 
ATOM   497  O  O   . ARG   A 1 73  ? -15.359 -19.712 -34.315 1   42.87 ? 58  ARG   A O   1 
ATOM   498  C  CB  . ARG   A 1 73  ? -15.213 -22.362 -36.194 1   44.4  ? 58  ARG   A CB  1 
ATOM   499  C  CG  . ARG   A 1 73  ? -16.121 -23.365 -36.916 1   49.43 ? 58  ARG   A CG  1 
ATOM   500  C  CD  . ARG   A 1 73  ? -17.529 -23.439 -36.356 1   52.91 ? 58  ARG   A CD  1 
ATOM   501  N  NE  . ARG   A 1 73  ? -18.382 -22.491 -37.054 1   56.47 ? 58  ARG   A NE  1 
ATOM   502  C  CZ  . ARG   A 1 73  ? -19.557 -22.063 -36.613 1   59.55 ? 58  ARG   A CZ  1 
ATOM   503  N  NH1 . ARG   A 1 73  ? -20.061 -22.533 -35.476 1   58.53 ? 58  ARG   A NH1 1 
ATOM   504  N  NH2 . ARG   A 1 73  ? -20.242 -21.164 -37.305 1   60.57 ? 58  ARG   A NH2 1 
ATOM   505  N  N   . VAL   A 1 74  ? -13.533 -19.659 -35.668 1   42.24 ? 59  VAL   A N   1 
ATOM   506  C  CA  . VAL   A 1 74  ? -12.745 -18.832 -34.755 1   41.94 ? 59  VAL   A CA  1 
ATOM   507  C  C   . VAL   A 1 74  ? -13.323 -17.424 -34.715 1   42.55 ? 59  VAL   A C   1 
ATOM   508  O  O   . VAL   A 1 74  ? -13.485 -16.85  -33.634 1   42.94 ? 59  VAL   A O   1 
ATOM   509  C  CB  . VAL   A 1 74  ? -11.237 -18.836 -35.107 1   41.08 ? 59  VAL   A CB  1 
ATOM   510  C  CG1 . VAL   A 1 74  ? -10.466 -17.773 -34.321 1   40.35 ? 59  VAL   A CG1 1 
ATOM   511  C  CG2 . VAL   A 1 74  ? -10.639 -20.224 -34.875 1   40.44 ? 59  VAL   A CG2 1 
ATOM   512  N  N   . GLU   A 1 75  ? -13.64  -16.872 -35.888 1   42.1  ? 60  GLU   A N   1 
ATOM   513  C  CA  . GLU   A 1 75  ? -14.217 -15.529 -35.973 1   42.35 ? 60  GLU   A CA  1 
ATOM   514  C  C   . GLU   A 1 75  ? -15.632 -15.433 -35.339 1   42.52 ? 60  GLU   A C   1 
ATOM   515  O  O   . GLU   A 1 75  ? -15.998 -14.38  -34.85  1   42.01 ? 60  GLU   A O   1 
ATOM   516  C  CB  . GLU   A 1 75  ? -14.195 -15.011 -37.412 1   42.76 ? 60  GLU   A CB  1 
ATOM   517  C  CG  . GLU   A 1 75  ? -12.798 -14.704 -37.924 1   43.88 ? 60  GLU   A CG  1 
ATOM   518  C  CD  . GLU   A 1 75  ? -12.632 -14.846 -39.433 1   47.41 ? 60  GLU   A CD  1 
ATOM   519  O  OE1 . GLU   A 1 75  ? -13.651 -15.076 -40.126 1   49.15 ? 60  GLU   A OE1 1 
ATOM   520  O  OE2 . GLU   A 1 75  ? -11.486 -14.728 -39.927 1   46.13 ? 60  GLU   A OE2 1 
ATOM   521  N  N   . LYS   A 1 76  ? -16.384 -16.553 -35.286 1   42.87 ? 61  LYS   A N   1 
ATOM   522  C  CA  . LYS   A 1 76  ? -17.714 -16.605 -34.674 1   43.88 ? 61  LYS   A CA  1 
ATOM   523  C  C   . LYS   A 1 76  ? -17.676 -16.736 -33.136 1   44.83 ? 61  LYS   A C   1 
ATOM   524  O  O   . LYS   A 1 76  ? -18.725 -16.663 -32.502 1   45.26 ? 61  LYS   A O   1 
ATOM   525  C  CB  . LYS   A 1 76  ? -18.535 -17.772 -35.258 1   45.54 ? 61  LYS   A CB  1 
ATOM   526  N  N   . LEU   A 1 77  ? -16.492 -16.964 -32.534 1   44.36 ? 62  LEU   A N   1 
ATOM   527  C  CA  . LEU   A 1 77  ? -16.389 -17.108 -31.079 1   44.32 ? 62  LEU   A CA  1 
ATOM   528  C  C   . LEU   A 1 77  ? -16.714 -15.833 -30.331 1   44.12 ? 62  LEU   A C   1 
ATOM   529  O  O   . LEU   A 1 77  ? -16.38  -14.746 -30.783 1   43.59 ? 62  LEU   A O   1 
ATOM   530  C  CB  . LEU   A 1 77  ? -14.948 -17.493 -30.672 1   44.37 ? 62  LEU   A CB  1 
ATOM   531  C  CG  . LEU   A 1 77  ? -14.472 -18.898 -30.958 1   45.3  ? 62  LEU   A CG  1 
ATOM   532  C  CD1 . LEU   A 1 77  ? -12.967 -19.021 -30.656 1   45.21 ? 62  LEU   A CD1 1 
ATOM   533  C  CD2 . LEU   A 1 77  ? -15.254 -19.887 -30.167 1   45.88 ? 62  LEU   A CD2 1 
ATOM   534  N  N   . ASN   A 1 78  ? -17.278 -15.982 -29.14  1   44.79 ? 63  ASN   A N   1 
ATOM   535  C  CA  . ASN   A 1 78  ? -17.455 -14.874 -28.211 1   45.81 ? 63  ASN   A CA  1 
ATOM   536  C  C   . ASN   A 1 78  ? -16.163 -14.822 -27.343 1   47.48 ? 63  ASN   A C   1 
ATOM   537  O  O   . ASN   A 1 78  ? -15.485 -15.856 -27.175 1   47.28 ? 63  ASN   A O   1 
ATOM   538  C  CB  . ASN   A 1 78  ? -18.65  -15.134 -27.315 1   46.24 ? 63  ASN   A CB  1 
ATOM   539  C  CG  . ASN   A 1 78  ? -19.957 -15.007 -28.051 1   47.72 ? 63  ASN   A CG  1 
ATOM   540  O  OD1 . ASN   A 1 78  ? -20.138 -14.12  -28.9   1   47.71 ? 63  ASN   A OD1 1 
ATOM   541  N  ND2 . ASN   A 1 78  ? -20.866 -15.918 -27.759 1   47.4  ? 63  ASN   A ND2 1 
ATOM   542  N  N   . MET   A 1 79  ? -15.826 -13.639 -26.788 1   47.97 ? 64  MET   A N   1 
ATOM   543  C  CA  . MET   A 1 79  ? -14.623 -13.527 -25.971 1   48.43 ? 64  MET   A CA  1 
ATOM   544  C  C   . MET   A 1 79  ? -14.901 -14.153 -24.643 1   49.12 ? 64  MET   A C   1 
ATOM   545  O  O   . MET   A 1 79  ? -15.689 -13.607 -23.882 1   50.31 ? 64  MET   A O   1 
ATOM   546  C  CB  . MET   A 1 79  ? -14.161 -12.082 -25.782 1   48.87 ? 64  MET   A CB  1 
ATOM   547  C  CG  . MET   A 1 79  ? -12.744 -12.001 -25.205 1   50.75 ? 64  MET   A CG  1 
ATOM   548  S  SD  . MET   A 1 79  ? -12.139 -10.312 -24.949 1   57.26 ? 64  MET   A SD  1 
ATOM   549  C  CE  . MET   A 1 79  ? -12.066 -9.691  -26.624 1   50.27 ? 64  MET   A CE  1 
ATOM   550  N  N   . LEU   A 1 80  ? -14.299 -15.319 -24.367 1   48.03 ? 65  LEU   A N   1 
ATOM   551  C  CA  . LEU   A 1 80  ? -14.514 -15.983 -23.096 1   47.44 ? 65  LEU   A CA  1 
ATOM   552  C  C   . LEU   A 1 80  ? -13.491 -15.515 -22.069 1   47.86 ? 65  LEU   A C   1 
ATOM   553  O  O   . LEU   A 1 80  ? -12.306 -15.385 -22.382 1   48.22 ? 65  LEU   A O   1 
ATOM   554  C  CB  . LEU   A 1 80  ? -14.483 -17.508 -23.255 1   47.17 ? 65  LEU   A CB  1 
ATOM   555  C  CG  . LEU   A 1 80  ? -15.564 -18.093 -24.171 1   47.9  ? 65  LEU   A CG  1 
ATOM   556  C  CD1 . LEU   A 1 80  ? -15.416 -19.597 -24.291 1   47.98 ? 65  LEU   A CD1 1 
ATOM   557  C  CD2 . LEU   A 1 80  ? -16.991 -17.714 -23.684 1   48.15 ? 65  LEU   A CD2 1 
ATOM   558  N  N   . SER   A 1 81  ? -13.956 -15.228 -20.845 1   47.32 ? 66  SER   A N   1 
ATOM   559  C  CA  . SER   A 1 81  ? -13.086 -14.77  -19.771 1   47.28 ? 66  SER   A CA  1 
ATOM   560  C  C   . SER   A 1 81  ? -12.202 -15.919 -19.266 1   45.89 ? 66  SER   A C   1 
ATOM   561  O  O   . SER   A 1 81  ? -12.679 -17.046 -19.154 1   45.58 ? 66  SER   A O   1 
ATOM   562  C  CB  . SER   A 1 81  ? -13.934 -14.239 -18.613 1   49.21 ? 66  SER   A CB  1 
ATOM   563  O  OG  . SER   A 1 81  ? -13.123 -13.848 -17.517 1   52.3  ? 66  SER   A OG  1 
ATOM   564  N  N   . ILE   A 1 82  ? -10.944 -15.636 -18.913 1   45.32 ? 67  ILE   A N   1 
ATOM   565  C  CA  . ILE   A 1 82  ? -10.06  -16.679 -18.369 1   45.22 ? 67  ILE   A CA  1 
ATOM   566  C  C   . ILE   A 1 82  ? -10.227 -16.915 -16.863 1   46.2  ? 67  ILE   A C   1 
ATOM   567  O  O   . ILE   A 1 82  ? -9.557  -17.793 -16.313 1   45.77 ? 67  ILE   A O   1 
ATOM   568  C  CB  . ILE   A 1 82  ? -8.58   -16.431 -18.713 1   44.49 ? 67  ILE   A CB  1 
ATOM   569  C  CG1 . ILE   A 1 82  ? -8.055  -15.158 -18.024 1   44.46 ? 67  ILE   A CG1 1 
ATOM   570  C  CG2 . ILE   A 1 82  ? -8.39   -16.401 -20.2   1   44.18 ? 67  ILE   A CG2 1 
ATOM   571  C  CD1 . ILE   A 1 82  ? -6.624  -15.102 -17.938 1   45.53 ? 67  ILE   A CD1 1 
ATOM   572  N  N   . ASP   A 1 83  ? -11.135 -16.183 -16.191 1   46.78 ? 68  ASP   A N   1 
ATOM   573  C  CA  . ASP   A 1 83  ? -11.321 -16.309 -14.742 1   47.46 ? 68  ASP   A CA  1 
ATOM   574  C  C   . ASP   A 1 83  ? -11.833 -17.668 -14.275 1   47.69 ? 68  ASP   A C   1 
ATOM   575  O  O   . ASP   A 1 83  ? -11.642 -18.008 -13.11  1   47.94 ? 68  ASP   A O   1 
ATOM   576  C  CB  . ASP   A 1 83  ? -12.213 -15.179 -14.217 1   50.25 ? 68  ASP   A CB  1 
ATOM   577  C  CG  . ASP   A 1 83  ? -11.66  -13.785 -14.47  1   57.31 ? 68  ASP   A CG  1 
ATOM   578  O  OD1 . ASP   A 1 83  ? -10.502 -13.675 -14.921 1   58.53 ? 68  ASP   A OD1 1 
ATOM   579  O  OD2 . ASP   A 1 83  ? -12.392 -12.801 -14.222 1   61.94 ? 68  ASP   A OD2 1 
ATOM   580  N  N   . HIS   A 1 84  ? -12.437 -18.458 -15.168 1   47.47 ? 69  HIS   A N   1 
ATOM   581  C  CA  . HIS   A 1 84  ? -12.92  -19.791 -14.807 1   48.3  ? 69  HIS   A CA  1 
ATOM   582  C  C   . HIS   A 1 84  ? -11.825 -20.896 -14.935 1   48.03 ? 69  HIS   A C   1 
ATOM   583  O  O   . HIS   A 1 84  ? -12.127 -22.078 -14.764 1   48.94 ? 69  HIS   A O   1 
ATOM   584  C  CB  . HIS   A 1 84  ? -14.207 -20.144 -15.582 1   50.15 ? 69  HIS   A CB  1 
ATOM   585  C  CG  . HIS   A 1 84  ? -15.218 -19.034 -15.541 1   54.29 ? 69  HIS   A CG  1 
ATOM   586  N  ND1 . HIS   A 1 84  ? -16.005 -18.816 -14.425 1   56.88 ? 69  HIS   A ND1 1 
ATOM   587  C  CD2 . HIS   A 1 84  ? -15.445 -18.041 -16.433 1   56.08 ? 69  HIS   A CD2 1 
ATOM   588  C  CE1 . HIS   A 1 84  ? -16.717 -17.734 -14.691 1   57.77 ? 69  HIS   A CE1 1 
ATOM   589  N  NE2 . HIS   A 1 84  ? -16.407 -17.226 -15.885 1   57.67 ? 69  HIS   A NE2 1 
ATOM   590  N  N   . LEU   A 1 85  ? -10.566 -20.508 -15.213 1   46.71 ? 70  LEU   A N   1 
ATOM   591  C  CA  . LEU   A 1 85  ? -9.418  -21.427 -15.289 1   46.39 ? 70  LEU   A CA  1 
ATOM   592  C  C   . LEU   A 1 85  ? -8.69   -21.169 -13.968 1   47.37 ? 70  LEU   A C   1 
ATOM   593  O  O   . LEU   A 1 85  ? -7.855  -20.273 -13.87  1   46.8  ? 70  LEU   A O   1 
ATOM   594  C  CB  . LEU   A 1 85  ? -8.528  -21.071 -16.488 1   45.25 ? 70  LEU   A CB  1 
ATOM   595  C  CG  . LEU   A 1 85  ? -9.223  -21.085 -17.843 1   44.86 ? 70  LEU   A CG  1 
ATOM   596  C  CD1 . LEU   A 1 85  ? -8.41   -20.385 -18.864 1   44.97 ? 70  LEU   A CD1 1 
ATOM   597  C  CD2 . LEU   A 1 85  ? -9.564  -22.483 -18.266 1   44.79 ? 70  LEU   A CD2 1 
ATOM   598  N  N   . THR   A 1 86  ? -9.103  -21.897 -12.928 1   48.7  ? 71  THR   A N   1 
ATOM   599  C  CA  . THR   A 1 86  ? -8.693  -21.657 -11.544 1   50    ? 71  THR   A CA  1 
ATOM   600  C  C   . THR   A 1 86  ? -7.392  -22.311 -11.085 1   49.95 ? 71  THR   A C   1 
ATOM   601  O  O   . THR   A 1 86  ? -6.868  -21.9   -10.048 1   50.75 ? 71  THR   A O   1 
ATOM   602  C  CB  . THR   A 1 86  ? -9.84   -22.063 -10.607 1   51.78 ? 71  THR   A CB  1 
ATOM   603  O  OG1 . THR   A 1 86  ? -10.075 -23.474 -10.729 1   52.72 ? 71  THR   A OG1 1 
ATOM   604  C  CG2 . THR   A 1 86  ? -11.129 -21.322 -10.937 1   52.68 ? 71  THR   A CG2 1 
ATOM   605  N  N   . ASP   A 1 87  ? -6.88   -23.315 -11.806 1   48.65 ? 72  ASP   A N   1 
ATOM   606  C  CA  . ASP   A 1 87  ? -5.629  -23.962 -11.402 1   47.35 ? 72  ASP   A CA  1 
ATOM   607  C  C   . ASP   A 1 87  ? -4.622  -24.06  -12.562 1   45.73 ? 72  ASP   A C   1 
ATOM   608  O  O   . ASP   A 1 87  ? -5      -23.902 -13.726 1   46.48 ? 72  ASP   A O   1 
ATOM   609  C  CB  . ASP   A 1 87  ? -5.901  -25.324 -10.755 1   48.62 ? 72  ASP   A CB  1 
ATOM   610  C  CG  . ASP   A 1 87  ? -6.656  -26.289 -11.636 1   54.06 ? 72  ASP   A CG  1 
ATOM   611  O  OD1 . ASP   A 1 87  ? -6.609  -26.127 -12.873 1   54.52 ? 72  ASP   A OD1 1 
ATOM   612  O  OD2 . ASP   A 1 87  ? -7.28   -27.224 -11.09  1   56.7  ? 72  ASP   A OD2 1 
ATOM   613  N  N   . HIS   A 1 88  ? -3.35   -24.334 -12.248 1   42.71 ? 73  HIS   A N   1 
ATOM   614  C  CA  . HIS   A 1 88  ? -2.293  -24.425 -13.242 1   39.88 ? 73  HIS   A CA  1 
ATOM   615  C  C   . HIS   A 1 88  ? -2.624  -25.389 -14.394 1   37.8  ? 73  HIS   A C   1 
ATOM   616  O  O   . HIS   A 1 88  ? -2.438  -25.013 -15.538 1   36.94 ? 73  HIS   A O   1 
ATOM   617  C  CB  . HIS   A 1 88  ? -0.963  -24.805 -12.567 1   39.22 ? 73  HIS   A CB  1 
ATOM   618  C  CG  . HIS   A 1 88  ? 0.205   -24.777 -13.499 1   38.76 ? 73  HIS   A CG  1 
ATOM   619  N  ND1 . HIS   A 1 88  ? 0.809   -23.589 -13.857 1   39.77 ? 73  HIS   A ND1 1 
ATOM   620  C  CD2 . HIS   A 1 88  ? 0.847   -25.795 -14.11  1   39.19 ? 73  HIS   A CD2 1 
ATOM   621  C  CE1 . HIS   A 1 88  ? 1.793   -23.916 -14.674 1   39.82 ? 73  HIS   A CE1 1 
ATOM   622  N  NE2 . HIS   A 1 88  ? 1.863   -25.233 -14.848 1   39.94 ? 73  HIS   A NE2 1 
ATOM   623  N  N   . LYS   A 1 89  ? -3.136  -26.591 -14.1   1   37.19 ? 74  LYS   A N   1 
ATOM   624  C  CA  . LYS   A 1 89  ? -3.459  -27.585 -15.117 1   37.2  ? 74  LYS   A CA  1 
ATOM   625  C  C   . LYS   A 1 89  ? -4.548  -27.136 -16.103 1   38.15 ? 74  LYS   A C   1 
ATOM   626  O  O   . LYS   A 1 89  ? -4.386  -27.364 -17.311 1   38.19 ? 74  LYS   A O   1 
ATOM   627  C  CB  . LYS   A 1 89  ? -3.802  -28.938 -14.503 1   38.02 ? 74  LYS   A CB  1 
ATOM   628  C  CG  . LYS   A 1 89  ? -2.6    -29.605 -13.852 1   39.43 ? 74  LYS   A CG  1 
ATOM   629  C  CD  . LYS   A 1 89  ? -2.829  -31.075 -13.699 1   40.39 ? 74  LYS   A CD  1 
ATOM   630  C  CE  . LYS   A 1 89  ? -1.725  -31.736 -12.922 1   41.53 ? 74  LYS   A CE  1 
ATOM   631  N  NZ  . LYS   A 1 89  ? -1.955  -33.208 -12.845 1   42.08 ? 74  LYS   A NZ  1 
ATOM   632  N  N   . SER   A 1 90  ? -5.636  -26.483 -15.617 1   37.4  ? 75  SER   A N   1 
ATOM   633  C  CA  . SER   A 1 90  ? -6.643  -25.972 -16.538 1   37.77 ? 75  SER   A CA  1 
ATOM   634  C  C   . SER   A 1 90  ? -6.072  -24.81  -17.368 1   36.65 ? 75  SER   A C   1 
ATOM   635  O  O   . SER   A 1 90  ? -6.412  -24.686 -18.545 1   36.36 ? 75  SER   A O   1 
ATOM   636  C  CB  . SER   A 1 90  ? -7.937  -25.586 -15.817 1   40.12 ? 75  SER   A CB  1 
ATOM   637  O  OG  . SER   A 1 90  ? -7.72   -24.509 -14.925 1   43.74 ? 75  SER   A OG  1 
ATOM   638  N  N   . GLN   A 1 91  ? -5.177  -23.993 -16.786 1   36.03 ? 76  GLN   A N   1 
ATOM   639  C  CA  . GLN   A 1 91  ? -4.544  -22.9   -17.533 1   35.78 ? 76  GLN   A CA  1 
ATOM   640  C  C   . GLN   A 1 91  ? -3.566  -23.444 -18.613 1   35.18 ? 76  GLN   A C   1 
ATOM   641  O  O   . GLN   A 1 91  ? -3.432  -22.854 -19.696 1   34.93 ? 76  GLN   A O   1 
ATOM   642  C  CB  . GLN   A 1 91  ? -3.8    -21.965 -16.581 1   37.25 ? 76  GLN   A CB  1 
ATOM   643  C  CG  . GLN   A 1 91  ? -4.735  -21.123 -15.696 1   41.1  ? 76  GLN   A CG  1 
ATOM   644  C  CD  . GLN   A 1 91  ? -4.02   -20.566 -14.485 1   44.99 ? 76  GLN   A CD  1 
ATOM   645  O  OE1 . GLN   A 1 91  ? -2.787  -20.507 -14.417 1   45.07 ? 76  GLN   A OE1 1 
ATOM   646  N  NE2 . GLN   A 1 91  ? -4.788  -20.147 -13.49  1   45.78 ? 76  GLN   A NE2 1 
ATOM   647  N  N   . ARG   A 1 92  ? -2.884  -24.561 -18.306 1   33.88 ? 77  ARG   A N   1 
ATOM   648  C  CA  . ARG   A 1 92  ? -1.947  -25.204 -19.222 1   33.32 ? 77  ARG   A CA  1 
ATOM   649  C  C   . ARG   A 1 92  ? -2.73   -25.831 -20.375 1   32.65 ? 77  ARG   A C   1 
ATOM   650  O  O   . ARG   A 1 92  ? -2.307  -25.701 -21.514 1   32.68 ? 77  ARG   A O   1 
ATOM   651  C  CB  . ARG   A 1 92  ? -1.078  -26.273 -18.512 1   32.47 ? 77  ARG   A CB  1 
ATOM   652  C  CG  . ARG   A 1 92  ? 0.039   -25.674 -17.659 1   34.23 ? 77  ARG   A CG  1 
ATOM   653  C  CD  . ARG   A 1 92  ? 1.214   -25.048 -18.432 1   34.4  ? 77  ARG   A CD  1 
ATOM   654  N  NE  . ARG   A 1 92  ? 1.996   -26.048 -19.164 1   34.34 ? 77  ARG   A NE  1 
ATOM   655  C  CZ  . ARG   A 1 92  ? 2.972   -26.775 -18.633 1   35.12 ? 77  ARG   A CZ  1 
ATOM   656  N  NH1 . ARG   A 1 92  ? 3.312   -26.615 -17.353 1   34.92 ? 77  ARG   A NH1 1 
ATOM   657  N  NH2 . ARG   A 1 92  ? 3.604   -27.68  -19.364 1   32.77 ? 77  ARG   A NH2 1 
ATOM   658  N  N   . LEU   A 1 93  ? -3.88   -26.473 -20.086 1   32.53 ? 78  LEU   A N   1 
ATOM   659  C  CA  . LEU   A 1 93  ? -4.716  -27.068 -21.124 1   32.66 ? 78  LEU   A CA  1 
ATOM   660  C  C   . LEU   A 1 93  ? -5.271  -25.967 -22.013 1   33.06 ? 78  LEU   A C   1 
ATOM   661  O  O   . LEU   A 1 93  ? -5.229  -26.101 -23.24  1   32.64 ? 78  LEU   A O   1 
ATOM   662  C  CB  . LEU   A 1 93  ? -5.857  -27.889 -20.515 1   32.83 ? 78  LEU   A CB  1 
ATOM   663  C  CG  . LEU   A 1 93  ? -6.894  -28.433 -21.498 1   33.34 ? 78  LEU   A CG  1 
ATOM   664  C  CD1 . LEU   A 1 93  ? -6.277  -29.365 -22.53  1   33.38 ? 78  LEU   A CD1 1 
ATOM   665  C  CD2 . LEU   A 1 93  ? -7.987  -29.122 -20.773 1   33.17 ? 78  LEU   A CD2 1 
ATOM   666  N  N   . ALA   A 1 94  ? -5.729  -24.855 -21.407 1   32.91 ? 79  ALA   A N   1 
ATOM   667  C  CA  . ALA   A 1 94  ? -6.269  -23.732 -22.153 1   32.85 ? 79  ALA   A CA  1 
ATOM   668  C  C   . ALA   A 1 94  ? -5.207  -23.128 -23.068 1   32.92 ? 79  ALA   A C   1 
ATOM   669  O  O   . ALA   A 1 94  ? -5.532  -22.72  -24.187 1   33.58 ? 79  ALA   A O   1 
ATOM   670  C  CB  . ALA   A 1 94  ? -6.792  -22.689 -21.201 1   33.3  ? 79  ALA   A CB  1 
ATOM   671  N  N   . ARG   A 1 95  ? -3.946  -23.072 -22.611 1   31.56 ? 80  ARG   A N   1 
ATOM   672  C  CA  . ARG   A 1 95  ? -2.818  -22.566 -23.398 1   31.58 ? 80  ARG   A CA  1 
ATOM   673  C  C   . ARG   A 1 95  ? -2.581  -23.481 -24.598 1   31.24 ? 80  ARG   A C   1 
ATOM   674  O  O   . ARG   A 1 95  ? -2.33   -22.997 -25.698 1   32.19 ? 80  ARG   A O   1 
ATOM   675  C  CB  . ARG   A 1 95  ? -1.54   -22.558 -22.534 1   32.84 ? 80  ARG   A CB  1 
ATOM   676  C  CG  . ARG   A 1 95  ? -1.026  -21.187 -22.244 1   33.15 ? 80  ARG   A CG  1 
ATOM   677  C  CD  . ARG   A 1 95  ? 0.424   -21.266 -21.807 1   31.74 ? 80  ARG   A CD  1 
ATOM   678  N  NE  . ARG   A 1 95  ? 1.353   -21.534 -22.905 1   31.68 ? 80  ARG   A NE  1 
ATOM   679  C  CZ  . ARG   A 1 95  ? 1.874   -20.602 -23.694 1   31.09 ? 80  ARG   A CZ  1 
ATOM   680  N  NH1 . ARG   A 1 95  ? 1.482   -19.338 -23.587 1   27.58 ? 80  ARG   A NH1 1 
ATOM   681  N  NH2 . ARG   A 1 95  ? 2.764   -20.933 -24.628 1   31.18 ? 80  ARG   A NH2 1 
ATOM   682  N  N   . LEU   A 1 96  ? -2.654  -24.797 -24.387 1   30.73 ? 81  LEU   A N   1 
ATOM   683  C  CA  . LEU   A 1 96  ? -2.476  -25.756 -25.467 1   31.97 ? 81  LEU   A CA  1 
ATOM   684  C  C   . LEU   A 1 96  ? -3.627  -25.604 -26.502 1   32.42 ? 81  LEU   A C   1 
ATOM   685  O  O   . LEU   A 1 96  ? -3.364  -25.514 -27.703 1   32.06 ? 81  LEU   A O   1 
ATOM   686  C  CB  . LEU   A 1 96  ? -2.433  -27.14  -24.854 1   32.04 ? 81  LEU   A CB  1 
ATOM   687  C  CG  . LEU   A 1 96  ? -2.349  -28.335 -25.752 1   33.29 ? 81  LEU   A CG  1 
ATOM   688  C  CD1 . LEU   A 1 96  ? -1.143  -28.258 -26.74  1   33.36 ? 81  LEU   A CD1 1 
ATOM   689  C  CD2 . LEU   A 1 96  ? -2.333  -29.575 -24.899 1   33.54 ? 81  LEU   A CD2 1 
ATOM   690  N  N   . VAL   A 1 97  ? -4.875  -25.5   -26.01  1   32.21 ? 82  VAL   A N   1 
ATOM   691  C  CA  . VAL   A 1 97  ? -6.089  -25.304 -26.806 1   32.54 ? 82  VAL   A CA  1 
ATOM   692  C  C   . VAL   A 1 97  ? -5.968  -24.043 -27.654 1   32.42 ? 82  VAL   A C   1 
ATOM   693  O  O   . VAL   A 1 97  ? -6.044  -24.131 -28.873 1   32.18 ? 82  VAL   A O   1 
ATOM   694  C  CB  . VAL   A 1 97  ? -7.38   -25.304 -25.922 1   32.79 ? 82  VAL   A CB  1 
ATOM   695  C  CG1 . VAL   A 1 97  ? -8.593  -24.759 -26.677 1   32.94 ? 82  VAL   A CG1 1 
ATOM   696  C  CG2 . VAL   A 1 97  ? -7.682  -26.696 -25.408 1   32.9  ? 82  VAL   A CG2 1 
ATOM   697  N  N   . LEU   A 1 98  ? -5.712  -22.887 -27.029 1   32.54 ? 83  LEU   A N   1 
ATOM   698  C  CA  . LEU   A 1 98  ? -5.633  -21.621 -27.749 1   32.83 ? 83  LEU   A CA  1 
ATOM   699  C  C   . LEU   A 1 98  ? -4.446  -21.537 -28.7   1   31.84 ? 83  LEU   A C   1 
ATOM   700  O  O   . LEU   A 1 98  ? -4.545  -20.89  -29.752 1   31.81 ? 83  LEU   A O   1 
ATOM   701  C  CB  . LEU   A 1 98  ? -5.6    -20.445 -26.769 1   33.5  ? 83  LEU   A CB  1 
ATOM   702  C  CG  . LEU   A 1 98  ? -6.858  -20.273 -25.896 1   35.26 ? 83  LEU   A CG  1 
ATOM   703  C  CD1 . LEU   A 1 98  ? -6.668  -19.165 -24.898 1   35.05 ? 83  LEU   A CD1 1 
ATOM   704  C  CD2 . LEU   A 1 98  ? -8.073  -19.992 -26.738 1   36.25 ? 83  LEU   A CD2 1 
ATOM   705  N  N   . GLY   A 1 99  ? -3.338  -22.176 -28.321 1   30.72 ? 84  GLY   A N   1 
ATOM   706  C  CA  . GLY   A 1 99  ? -2.123  -22.199 -29.123 1   29.87 ? 84  GLY   A CA  1 
ATOM   707  C  C   . GLY   A 1 99  ? -2.313  -22.998 -30.385 1   28.93 ? 84  GLY   A C   1 
ATOM   708  O  O   . GLY   A 1 99  ? -1.866  -22.577 -31.439 1   28.4  ? 84  GLY   A O   1 
ATOM   709  N  N   . CYS   A 1 100 ? -2.957  -24.166 -30.281 1   29.8  ? 85  CYS   A N   1 
ATOM   710  C  CA  . CYS   A 1 100 ? -3.239  -25.003 -31.449 1   30.73 ? 85  CYS   A CA  1 
ATOM   711  C  C   . CYS   A 1 100 ? -4.205  -24.288 -32.393 1   31.55 ? 85  CYS   A C   1 
ATOM   712  O  O   . CYS   A 1 100 ? -3.996  -24.303 -33.608 1   31.81 ? 85  CYS   A O   1 
ATOM   713  C  CB  . CYS   A 1 100 ? -3.776  -26.365 -31.023 1   31.48 ? 85  CYS   A CB  1 
ATOM   714  S  SG  . CYS   A 1 100 ? -2.525  -27.456 -30.299 1   34.84 ? 85  CYS   A SG  1 
ATOM   715  N  N   . ILE   A 1 101 ? -5.217  -23.613 -31.828 1   31.72 ? 86  ILE   A N   1 
ATOM   716  C  CA  . ILE   A 1 101 ? -6.183  -22.837 -32.601 1   33.01 ? 86  ILE   A CA  1 
ATOM   717  C  C   . ILE   A 1 101 ? -5.464  -21.676 -33.306 1   33.53 ? 86  ILE   A C   1 
ATOM   718  O  O   . ILE   A 1 101 ? -5.677  -21.471 -34.507 1   33.37 ? 86  ILE   A O   1 
ATOM   719  C  CB  . ILE   A 1 101 ? -7.353  -22.352 -31.712 1   33.71 ? 86  ILE   A CB  1 
ATOM   720  C  CG1 . ILE   A 1 101 ? -8.201  -23.541 -31.243 1   34.28 ? 86  ILE   A CG1 1 
ATOM   721  C  CG2 . ILE   A 1 101 ? -8.232  -21.35  -32.476 1   34.48 ? 86  ILE   A CG2 1 
ATOM   722  C  CD1 . ILE   A 1 101 ? -9.229  -23.145 -30.134 1   35.3  ? 86  ILE   A CD1 1 
ATOM   723  N  N   . THR   A 1 102 ? -4.563  -20.968 -32.588 1   33.09 ? 87  THR   A N   1 
ATOM   724  C  CA  . THR   A 1 102 ? -3.794  -19.869 -33.173 1   33.16 ? 87  THR   A CA  1 
ATOM   725  C  C   . THR   A 1 102 ? -2.963  -20.345 -34.363 1   34.29 ? 87  THR   A C   1 
ATOM   726  O  O   . THR   A 1 102 ? -3.039  -19.742 -35.429 1   34.22 ? 87  THR   A O   1 
ATOM   727  C  CB  . THR   A 1 102 ? -2.974  -19.168 -32.108 1   33.66 ? 87  THR   A CB  1 
ATOM   728  O  OG1 . THR   A 1 102 ? -3.877  -18.644 -31.131 1   35.31 ? 87  THR   A OG1 1 
ATOM   729  C  CG2 . THR   A 1 102 ? -2.106  -18.069 -32.656 1   33.37 ? 87  THR   A CG2 1 
ATOM   730  N  N   . MET   A 1 103 ? -2.228  -21.471 -34.219 1   34.57 ? 88  MET   A N   1 
ATOM   731  C  CA  . MET   A 1 103 ? -1.438  -22.003 -35.327 1   35.42 ? 88  MET   A CA  1 
ATOM   732  C  C   . MET   A 1 103 ? -2.317  -22.336 -36.54  1   35.12 ? 88  MET   A C   1 
ATOM   733  O  O   . MET   A 1 103 ? -1.952  -22.003 -37.661 1   36.07 ? 88  MET   A O   1 
ATOM   734  C  CB  . MET   A 1 103 ? -0.657  -23.254 -34.893 1   37.3  ? 88  MET   A CB  1 
ATOM   735  C  CG  . MET   A 1 103 ? 0.482   -22.956 -33.946 1   43.29 ? 88  MET   A CG  1 
ATOM   736  S  SD  . MET   A 1 103 ? 1.693   -21.786 -34.617 1   56.06 ? 88  MET   A SD  1 
ATOM   737  C  CE  . MET   A 1 103 ? 3.131   -22.197 -33.638 1   55.68 ? 88  MET   A CE  1 
ATOM   738  N  N   . ALA   A 1 104 ? -3.452  -22.997 -36.315 1   34.48 ? 89  ALA   A N   1 
ATOM   739  C  CA  . ALA   A 1 104 ? -4.353  -23.372 -37.387 1   35.18 ? 89  ALA   A CA  1 
ATOM   740  C  C   . ALA   A 1 104 ? -4.947  -22.128 -38.063 1   35.22 ? 89  ALA   A C   1 
ATOM   741  O  O   . ALA   A 1 104 ? -5.065  -22.087 -39.283 1   35.9  ? 89  ALA   A O   1 
ATOM   742  C  CB  . ALA   A 1 104 ? -5.467  -24.253 -36.841 1   35.16 ? 89  ALA   A CB  1 
ATOM   743  N  N   . TYR   A 1 105 ? -5.289  -21.115 -37.274 1   34.96 ? 90  TYR   A N   1 
ATOM   744  C  CA  . TYR   A 1 105 ? -5.876  -19.886 -37.775 1   35.32 ? 90  TYR   A CA  1 
ATOM   745  C  C   . TYR   A 1 105 ? -4.858  -19.137 -38.626 1   35.76 ? 90  TYR   A C   1 
ATOM   746  O  O   . TYR   A 1 105 ? -5.184  -18.698 -39.727 1   35.79 ? 90  TYR   A O   1 
ATOM   747  C  CB  . TYR   A 1 105 ? -6.414  -19.008 -36.617 1   35.26 ? 90  TYR   A CB  1 
ATOM   748  C  CG  . TYR   A 1 105 ? -7.167  -17.797 -37.124 1   36.51 ? 90  TYR   A CG  1 
ATOM   749  C  CD1 . TYR   A 1 105 ? -8.523  -17.872 -37.428 1   37.58 ? 90  TYR   A CD1 1 
ATOM   750  C  CD2 . TYR   A 1 105 ? -6.509  -16.596 -37.37  1   37.27 ? 90  TYR   A CD2 1 
ATOM   751  C  CE1 . TYR   A 1 105 ? -9.208  -16.782 -37.951 1   38.54 ? 90  TYR   A CE1 1 
ATOM   752  C  CE2 . TYR   A 1 105 ? -7.179  -15.507 -37.914 1   38.26 ? 90  TYR   A CE2 1 
ATOM   753  C  CZ  . TYR   A 1 105 ? -8.525  -15.609 -38.214 1   39.7  ? 90  TYR   A CZ  1 
ATOM   754  O  OH  . TYR   A 1 105 ? -9.183  -14.533 -38.746 1   42.38 ? 90  TYR   A OH  1 
ATOM   755  N  N   . VAL   A 1 106 ? -3.624  -19.003 -38.134 1   35.73 ? 91  VAL   A N   1 
ATOM   756  C  CA  . VAL   A 1 106 ? -2.586  -18.283 -38.864 1   36.16 ? 91  VAL   A CA  1 
ATOM   757  C  C   . VAL   A 1 106 ? -2.208  -18.972 -40.171 1   36.72 ? 91  VAL   A C   1 
ATOM   758  O  O   . VAL   A 1 106 ? -2.14   -18.308 -41.213 1   37.46 ? 91  VAL   A O   1 
ATOM   759  C  CB  . VAL   A 1 106 ? -1.334  -18.015 -37.964 1   37.37 ? 91  VAL   A CB  1 
ATOM   760  C  CG1 . VAL   A 1 106 ? -0.142  -17.513 -38.772 1   37.57 ? 91  VAL   A CG1 1 
ATOM   761  C  CG2 . VAL   A 1 106 ? -1.673  -17.043 -36.843 1   38.71 ? 91  VAL   A CG2 1 
ATOM   762  N  N   . TRP   A 1 107 ? -1.945  -20.294 -40.128 1   35.54 ? 92  TRP   A N   1 
ATOM   763  C  CA  . TRP   A 1 107 ? -1.451  -20.983 -41.299 1   35.48 ? 92  TRP   A CA  1 
ATOM   764  C  C   . TRP   A 1 107 ? -2.517  -21.537 -42.232 1   35.76 ? 92  TRP   A C   1 
ATOM   765  O  O   . TRP   A 1 107 ? -2.192  -21.839 -43.367 1   35.29 ? 92  TRP   A O   1 
ATOM   766  C  CB  . TRP   A 1 107 ? -0.44   -22.089 -40.896 1   34.88 ? 92  TRP   A CB  1 
ATOM   767  C  CG  . TRP   A 1 107 ? 0.691   -21.591 -40.028 1   34.48 ? 92  TRP   A CG  1 
ATOM   768  C  CD1 . TRP   A 1 107 ? 0.992   -21.995 -38.757 1   34.48 ? 92  TRP   A CD1 1 
ATOM   769  C  CD2 . TRP   A 1 107 ? 1.612   -20.548 -40.341 1   34.6  ? 92  TRP   A CD2 1 
ATOM   770  N  NE1 . TRP   A 1 107 ? 2.056   -21.292 -38.282 1   34.42 ? 92  TRP   A NE1 1 
ATOM   771  C  CE2 . TRP   A 1 107 ? 2.464   -20.399 -39.233 1   34.75 ? 92  TRP   A CE2 1 
ATOM   772  C  CE3 . TRP   A 1 107 ? 1.826   -19.745 -41.473 1   35.98 ? 92  TRP   A CE3 1 
ATOM   773  C  CZ2 . TRP   A 1 107 ? 3.504   -19.477 -39.215 1   36.07 ? 92  TRP   A CZ2 1 
ATOM   774  C  CZ3 . TRP   A 1 107 ? 2.866   -18.841 -41.453 1   36.88 ? 92  TRP   A CZ3 1 
ATOM   775  C  CH2 . TRP   A 1 107 ? 3.69    -18.712 -40.331 1   36.43 ? 92  TRP   A CH2 1 
ATOM   776  N  N   . GLY   A 1 108 ? -3.734  -21.697 -41.754 1   36.99 ? 93  GLY   A N   1 
ATOM   777  C  CA  . GLY   A 1 108 ? -4.839  -22.23  -42.548 1   38.21 ? 93  GLY   A CA  1 
ATOM   778  C  C   . GLY   A 1 108 ? -4.556  -23.625 -43.068 1   39.35 ? 93  GLY   A C   1 
ATOM   779  O  O   . GLY   A 1 108 ? -4.15   -24.498 -42.302 1   38.22 ? 93  GLY   A O   1 
ATOM   780  N  N   . LYS   A 1 109 ? -4.735  -23.843 -44.378 1   40.67 ? 94  LYS   A N   1 
ATOM   781  C  CA  . LYS   A 1 109 ? -4.446  -25.149 -44.994 1   42.83 ? 94  LYS   A CA  1 
ATOM   782  C  C   . LYS   A 1 109 ? -2.947  -25.414 -45.22  1   45.16 ? 94  LYS   A C   1 
ATOM   783  O  O   . LYS   A 1 109 ? -2.574  -26.506 -45.64  1   45.82 ? 94  LYS   A O   1 
ATOM   784  C  CB  . LYS   A 1 109 ? -5.231  -25.356 -46.301 1   43.94 ? 94  LYS   A CB  1 
ATOM   785  C  CG  . LYS   A 1 109 ? -6.743  -25.469 -46.091 1   46.16 ? 94  LYS   A CG  1 
ATOM   786  C  CD  . LYS   A 1 109 ? -7.429  -26.001 -47.34  1   48.09 ? 94  LYS   A CD  1 
ATOM   787  C  CE  . LYS   A 1 109 ? -8.918  -25.81  -47.312 1   51.24 ? 94  LYS   A CE  1 
ATOM   788  N  NZ  . LYS   A 1 109 ? -9.549  -26.25  -48.578 1   54.62 ? 94  LYS   A NZ  1 
ATOM   789  N  N   . GLY   A 1 110 ? -2.107  -24.437 -44.92  1   46.85 ? 95  GLY   A N   1 
ATOM   790  C  CA  . GLY   A 1 110 ? -0.672  -24.588 -45.052 1   50.21 ? 95  GLY   A CA  1 
ATOM   791  C  C   . GLY   A 1 110 ? -0.152  -24.473 -46.461 1   53.46 ? 95  GLY   A C   1 
ATOM   792  O  O   . GLY   A 1 110 ? 0.911   -25.018 -46.768 1   54.32 ? 95  GLY   A O   1 
ATOM   793  N  N   . HIS   A 1 111 ? -0.877  -23.757 -47.318 1   55.26 ? 96  HIS   A N   1 
ATOM   794  C  CA  . HIS   A 1 111 ? -0.445  -23.584 -48.702 1   57.39 ? 96  HIS   A CA  1 
ATOM   795  C  C   . HIS   A 1 111 ? 0.006   -22.15  -49.044 1   57.65 ? 96  HIS   A C   1 
ATOM   796  O  O   . HIS   A 1 111 ? 0.372   -21.897 -50.188 1   58.29 ? 96  HIS   A O   1 
ATOM   797  C  CB  . HIS   A 1 111 ? -1.498  -24.097 -49.711 1   59.79 ? 96  HIS   A CB  1 
ATOM   798  C  CG  . HIS   A 1 111 ? -2.887  -23.563 -49.528 1   64.89 ? 96  HIS   A CG  1 
ATOM   799  N  ND1 . HIS   A 1 111 ? -3.123  -22.206 -49.353 1   67.75 ? 96  HIS   A ND1 1 
ATOM   800  C  CD2 . HIS   A 1 111 ? -4.079  -24.204 -49.615 1   66.68 ? 96  HIS   A CD2 1 
ATOM   801  C  CE1 . HIS   A 1 111 ? -4.44   -22.068 -49.306 1   68.41 ? 96  HIS   A CE1 1 
ATOM   802  N  NE2 . HIS   A 1 111 ? -5.06   -23.241 -49.459 1   68.18 ? 96  HIS   A NE2 1 
ATOM   803  N  N   . GLY   A 1 112 ? 0.012   -21.246 -48.069 1   56.88 ? 97  GLY   A N   1 
ATOM   804  C  CA  . GLY   A 1 112 ? 0.46    -19.882 -48.312 1   56.6  ? 97  GLY   A CA  1 
ATOM   805  C  C   . GLY   A 1 112 ? -0.551  -18.796 -48.022 1   56.02 ? 97  GLY   A C   1 
ATOM   806  O  O   . GLY   A 1 112 ? -0.186  -17.623 -47.991 1   56.22 ? 97  GLY   A O   1 
ATOM   807  N  N   . ASP   A 1 113 ? -1.822  -19.158 -47.803 1   55.46 ? 98  ASP   A N   1 
ATOM   808  C  CA  . ASP   A 1 113 ? -2.832  -18.159 -47.452 1   55.24 ? 98  ASP   A CA  1 
ATOM   809  C  C   . ASP   A 1 113 ? -2.789  -18.005 -45.938 1   54.7  ? 98  ASP   A C   1 
ATOM   810  O  O   . ASP   A 1 113 ? -3.313  -18.841 -45.197 1   55.21 ? 98  ASP   A O   1 
ATOM   811  C  CB  . ASP   A 1 113 ? -4.235  -18.542 -47.924 1   56.72 ? 98  ASP   A CB  1 
ATOM   812  C  CG  . ASP   A 1 113 ? -5.248  -17.469 -47.582 1   61.55 ? 98  ASP   A CG  1 
ATOM   813  O  OD1 . ASP   A 1 113 ? -4.89   -16.271 -47.64  1   61.97 ? 98  ASP   A OD1 1 
ATOM   814  O  OD2 . ASP   A 1 113 ? -6.385  -17.825 -47.231 1   64.5  ? 98  ASP   A OD2 1 
ATOM   815  N  N   . VAL   A 1 114 ? -2.123  -16.958 -45.488 1   53.47 ? 99  VAL   A N   1 
ATOM   816  C  CA  . VAL   A 1 114 ? -1.877  -16.703 -44.079 1   52.98 ? 99  VAL   A CA  1 
ATOM   817  C  C   . VAL   A 1 114 ? -2.803  -15.635 -43.508 1   51.59 ? 99  VAL   A C   1 
ATOM   818  O  O   . VAL   A 1 114 ? -3.351  -14.832 -44.251 1   52.41 ? 99  VAL   A O   1 
ATOM   819  C  CB  . VAL   A 1 114 ? -0.37   -16.324 -43.968 1   54.01 ? 99  VAL   A CB  1 
ATOM   820  C  CG1 . VAL   A 1 114 ? -0.057  -15.298 -42.894 1   54.96 ? 99  VAL   A CG1 1 
ATOM   821  C  CG2 . VAL   A 1 114 ? 0.5     -17.553 -43.849 1   54.53 ? 99  VAL   A CG2 1 
ATOM   822  N  N   . ARG   A 1 115 ? -2.981  -15.639 -42.184 1   49.39 ? 100 ARG   A N   1 
ATOM   823  C  CA  . ARG   A 1 115 ? -3.722  -14.595 -41.481 1   47.76 ? 100 ARG   A CA  1 
ATOM   824  C  C   . ARG   A 1 115 ? -2.709  -13.872 -40.606 1   46.4  ? 100 ARG   A C   1 
ATOM   825  O  O   . ARG   A 1 115 ? -1.945  -14.507 -39.865 1   45.92 ? 100 ARG   A O   1 
ATOM   826  C  CB  . ARG   A 1 115 ? -4.86   -15.155 -40.621 1   47.9  ? 100 ARG   A CB  1 
ATOM   827  C  CG  . ARG   A 1 115 ? -6.082  -15.624 -41.411 1   49.47 ? 100 ARG   A CG  1 
ATOM   828  C  CD  . ARG   A 1 115 ? -6.77   -14.489 -42.167 1   51.63 ? 100 ARG   A CD  1 
ATOM   829  N  NE  . ARG   A 1 115 ? -7.852  -14.973 -43.033 1   53.64 ? 100 ARG   A NE  1 
ATOM   830  C  CZ  . ARG   A 1 115 ? -7.678  -15.465 -44.259 1   55.25 ? 100 ARG   A CZ  1 
ATOM   831  N  NH1 . ARG   A 1 115 ? -6.463  -15.537 -44.788 1   55.67 ? 100 ARG   A NH1 1 
ATOM   832  N  NH2 . ARG   A 1 115 ? -8.713  -15.901 -44.957 1   55.12 ? 100 ARG   A NH2 1 
ATOM   833  N  N   . LYS   A 1 116 ? -2.683  -12.548 -40.7   1   45.22 ? 101 LYS   A N   1 
ATOM   834  C  CA  . LYS   A 1 116 ? -1.735  -11.724 -39.94  1   44.27 ? 101 LYS   A CA  1 
ATOM   835  C  C   . LYS   A 1 116 ? -2.344  -11.042 -38.712 1   42.82 ? 101 LYS   A C   1 
ATOM   836  O  O   . LYS   A 1 116 ? -1.643  -10.333 -37.989 1   43.13 ? 101 LYS   A O   1 
ATOM   837  C  CB  . LYS   A 1 116 ? -1.057  -10.704 -40.864 1   45.52 ? 101 LYS   A CB  1 
ATOM   838  C  CG  . LYS   A 1 116 ? -0.352  -11.4   -42.017 1   50.45 ? 101 LYS   A CG  1 
ATOM   839  C  CD  . LYS   A 1 116 ? 0.711   -10.545 -42.709 1   56.25 ? 101 LYS   A CD  1 
ATOM   840  C  CE  . LYS   A 1 116 ? 1.327   -11.301 -43.869 1   60.76 ? 101 LYS   A CE  1 
ATOM   841  N  NZ  . LYS   A 1 116 ? 2.268   -10.462 -44.66  1   64.14 ? 101 LYS   A NZ  1 
ATOM   842  N  N   . VAL   A 1 117 ? -3.639  -11.245 -38.466 1   41.32 ? 102 VAL   A N   1 
ATOM   843  C  CA  . VAL   A 1 117 ? -4.305  -10.663 -37.314 1   40.5  ? 102 VAL   A CA  1 
ATOM   844  C  C   . VAL   A 1 117 ? -5.042  -11.773 -36.622 1   41.01 ? 102 VAL   A C   1 
ATOM   845  O  O   . VAL   A 1 117 ? -5.833  -12.475 -37.253 1   41.49 ? 102 VAL   A O   1 
ATOM   846  C  CB  . VAL   A 1 117 ? -5.265  -9.494  -37.684 1   40.32 ? 102 VAL   A CB  1 
ATOM   847  C  CG1 . VAL   A 1 117 ? -5.878  -8.88   -36.432 1   40.72 ? 102 VAL   A CG1 1 
ATOM   848  C  CG2 . VAL   A 1 117 ? -4.553  -8.419  -38.506 1   40.44 ? 102 VAL   A CG2 1 
ATOM   849  N  N   . LEU   A 1 118 ? -4.768  -11.975 -35.333 1   40.69 ? 103 LEU   A N   1 
ATOM   850  C  CA  . LEU   A 1 118 ? -5.452  -13.005 -34.571 1   40.16 ? 103 LEU   A CA  1 
ATOM   851  C  C   . LEU   A 1 118 ? -6.647  -12.301 -33.937 1   40.64 ? 103 LEU   A C   1 
ATOM   852  O  O   . LEU   A 1 118 ? -6.446  -11.321 -33.225 1   41.14 ? 103 LEU   A O   1 
ATOM   853  C  CB  . LEU   A 1 118 ? -4.505  -13.58  -33.501 1   39.51 ? 103 LEU   A CB  1 
ATOM   854  C  CG  . LEU   A 1 118 ? -5.063  -14.722 -32.684 1   40.05 ? 103 LEU   A CG  1 
ATOM   855  C  CD1 . LEU   A 1 118 ? -5.344  -15.937 -33.553 1   39.76 ? 103 LEU   A CD1 1 
ATOM   856  C  CD2 . LEU   A 1 118 ? -4.135  -15.062 -31.522 1   40.94 ? 103 LEU   A CD2 1 
ATOM   857  N  N   . PRO   A 1 119 ? -7.894  -12.744 -34.23  1   40.38 ? 104 PRO   A N   1 
ATOM   858  C  CA  . PRO   A 1 119 ? -9.077  -12.061 -33.687 1   40.27 ? 104 PRO   A CA  1 
ATOM   859  C  C   . PRO   A 1 119 ? -9.057  -11.874 -32.175 1   39.62 ? 104 PRO   A C   1 
ATOM   860  O  O   . PRO   A 1 119 ? -8.619  -12.765 -31.449 1   39.08 ? 104 PRO   A O   1 
ATOM   861  C  CB  . PRO   A 1 119 ? -10.255 -12.95  -34.142 1   41.22 ? 104 PRO   A CB  1 
ATOM   862  C  CG  . PRO   A 1 119 ? -9.755  -13.687 -35.302 1   41.67 ? 104 PRO   A CG  1 
ATOM   863  C  CD  . PRO   A 1 119 ? -8.28   -13.896 -35.06  1   40.08 ? 104 PRO   A CD  1 
ATOM   864  N  N   . ARG   A 1 120 ? -9.553  -10.724 -31.704 1   38.91 ? 105 ARG   A N   1 
ATOM   865  C  CA  . ARG   A 1 120 ? -9.585  -10.376 -30.288 1   39.55 ? 105 ARG   A CA  1 
ATOM   866  C  C   . ARG   A 1 120 ? -10.245 -11.397 -29.393 1   39.97 ? 105 ARG   A C   1 
ATOM   867  O  O   . ARG   A 1 120 ? -9.815  -11.558 -28.256 1   40.23 ? 105 ARG   A O   1 
ATOM   868  C  CB  . ARG   A 1 120 ? -10.258 -9.017  -30.083 1   41.45 ? 105 ARG   A CB  1 
ATOM   869  C  CG  . ARG   A 1 120 ? -11.791 -9.025  -30.38  1   44.05 ? 105 ARG   A CG  1 
ATOM   870  C  CD  . ARG   A 1 120 ? -12.325 -7.721  -30.971 1   45.65 ? 105 ARG   A CD  1 
ATOM   871  N  NE  . ARG   A 1 120 ? -11.688 -6.638  -30.261 1   46.4  ? 105 ARG   A NE  1 
ATOM   872  C  CZ  . ARG   A 1 120 ? -10.99  -5.665  -30.808 1   46.21 ? 105 ARG   A CZ  1 
ATOM   873  N  NH1 . ARG   A 1 120 ? -11.003 -5.485  -32.123 1   45.48 ? 105 ARG   A NH1 1 
ATOM   874  N  NH2 . ARG   A 1 120 ? -10.358 -4.801  -30.044 1   46.63 ? 105 ARG   A NH2 1 
ATOM   875  N  N   . ASN   A 1 121 ? -11.273 -12.095 -29.879 1   40.1  ? 106 ASN   A N   1 
ATOM   876  C  CA  . ASN   A 1 121 ? -11.978 -13.076 -29.047 1   41.21 ? 106 ASN   A CA  1 
ATOM   877  C  C   . ASN   A 1 121 ? -11.084 -14.263 -28.648 1   40.77 ? 106 ASN   A C   1 
ATOM   878  O  O   . ASN   A 1 121 ? -11.35  -14.889 -27.621 1   40.55 ? 106 ASN   A O   1 
ATOM   879  C  CB  . ASN   A 1 121 ? -13.301 -13.521 -29.682 1   43.51 ? 106 ASN   A CB  1 
ATOM   880  C  CG  . ASN   A 1 121 ? -14.391 -12.433 -29.65  1   50.77 ? 106 ASN   A CG  1 
ATOM   881  O  OD1 . ASN   A 1 121 ? -15.517 -12.631 -30.148 1   53.17 ? 106 ASN   A OD1 1 
ATOM   882  N  ND2 . ASN   A 1 121 ? -14.126 -11.271 -29.028 1   51.41 ? 106 ASN   A ND2 1 
ATOM   883  N  N   . ILE   A 1 122 ? -10.011 -14.536 -29.426 1   40.56 ? 107 ILE   A N   1 
ATOM   884  C  CA  . ILE   A 1 122 ? -9.051  -15.569 -29.066 1   41.29 ? 107 ILE   A CA  1 
ATOM   885  C  C   . ILE   A 1 122 ? -7.747  -14.926 -28.536 1   40.18 ? 107 ILE   A C   1 
ATOM   886  O  O   . ILE   A 1 122 ? -7.251  -15.347 -27.485 1   40.36 ? 107 ILE   A O   1 
ATOM   887  C  CB  . ILE   A 1 122 ? -8.834  -16.628 -30.177 1   43.66 ? 107 ILE   A CB  1 
ATOM   888  C  CG1 . ILE   A 1 122 ? -7.765  -17.628 -29.773 1   46.66 ? 107 ILE   A CG1 1 
ATOM   889  C  CG2 . ILE   A 1 122 ? -8.48   -16.021 -31.525 1   44.57 ? 107 ILE   A CG2 1 
ATOM   890  C  CD1 . ILE   A 1 122 ? -8.111  -18.92  -30.216 1   49.19 ? 107 ILE   A CD1 1 
ATOM   891  N  N   . ALA   A 1 123 ? -7.239  -13.877 -29.212 1   38.61 ? 108 ALA   A N   1 
ATOM   892  C  CA  . ALA   A 1 123 ? -6.013  -13.179 -28.832 1   38.61 ? 108 ALA   A CA  1 
ATOM   893  C  C   . ALA   A 1 123 ? -6      -12.602 -27.426 1   38.53 ? 108 ALA   A C   1 
ATOM   894  O  O   . ALA   A 1 123 ? -4.965  -12.708 -26.747 1   38.78 ? 108 ALA   A O   1 
ATOM   895  C  CB  . ALA   A 1 123 ? -5.683  -12.09  -29.83  1   38.68 ? 108 ALA   A CB  1 
ATOM   896  N  N   . VAL   A 1 124 ? -7.129  -11.996 -26.969 1   36.38 ? 109 VAL   A N   1 
ATOM   897  C  CA  . VAL   A 1 124 ? -7.163  -11.441 -25.621 1   36.4  ? 109 VAL   A CA  1 
ATOM   898  C  C   . VAL   A 1 124 ? -7.07   -12.544 -24.543 1   35.9  ? 109 VAL   A C   1 
ATOM   899  O  O   . VAL   A 1 124 ? -6.142  -12.464 -23.744 1   36.55 ? 109 VAL   A O   1 
ATOM   900  C  CB  . VAL   A 1 124 ? -8.35   -10.451 -25.389 1   37.14 ? 109 VAL   A CB  1 
ATOM   901  C  CG1 . VAL   A 1 124 ? -8.521  -10.123 -23.904 1   37.83 ? 109 VAL   A CG1 1 
ATOM   902  C  CG2 . VAL   A 1 124 ? -8.14   -9.177  -26.202 1   37.05 ? 109 VAL   A CG2 1 
ATOM   903  N  N   . PRO   A 1 125 ? -7.943  -13.584 -24.49  1   35.37 ? 110 PRO   A N   1 
ATOM   904  C  CA  . PRO   A 1 125 ? -7.766  -14.612 -23.443 1   35.6  ? 110 PRO   A CA  1 
ATOM   905  C  C   . PRO   A 1 125 ? -6.434  -15.369 -23.576 1   35.82 ? 110 PRO   A C   1 
ATOM   906  O  O   . PRO   A 1 125 ? -5.882  -15.804 -22.566 1   35.15 ? 110 PRO   A O   1 
ATOM   907  C  CB  . PRO   A 1 125 ? -8.981  -15.536 -23.612 1   36.18 ? 110 PRO   A CB  1 
ATOM   908  C  CG  . PRO   A 1 125 ? -9.502  -15.269 -24.971 1   36.24 ? 110 PRO   A CG  1 
ATOM   909  C  CD  . PRO   A 1 125 ? -9.115  -13.875 -25.35  1   34.5  ? 110 PRO   A CD  1 
ATOM   910  N  N   . TYR   A 1 126 ? -5.915  -15.514 -24.818 1   35.92 ? 111 TYR   A N   1 
ATOM   911  C  CA  . TYR   A 1 126 ? -4.639  -16.199 -25.04  1   36.21 ? 111 TYR   A CA  1 
ATOM   912  C  C   . TYR   A 1 126 ? -3.511  -15.413 -24.402 1   37.11 ? 111 TYR   A C   1 
ATOM   913  O  O   . TYR   A 1 126 ? -2.744  -15.979 -23.626 1   36.99 ? 111 TYR   A O   1 
ATOM   914  C  CB  . TYR   A 1 126 ? -4.375  -16.413 -26.544 1   35.25 ? 111 TYR   A CB  1 
ATOM   915  C  CG  . TYR   A 1 126 ? -3.212  -17.326 -26.875 1   34.24 ? 111 TYR   A CG  1 
ATOM   916  C  CD1 . TYR   A 1 126 ? -2.766  -18.281 -25.969 1   34.38 ? 111 TYR   A CD1 1 
ATOM   917  C  CD2 . TYR   A 1 126 ? -2.631  -17.308 -28.131 1   34.32 ? 111 TYR   A CD2 1 
ATOM   918  C  CE1 . TYR   A 1 126 ? -1.716  -19.142 -26.283 1   34.11 ? 111 TYR   A CE1 1 
ATOM   919  C  CE2 . TYR   A 1 126 ? -1.61   -18.187 -28.471 1   34.7  ? 111 TYR   A CE2 1 
ATOM   920  C  CZ  . TYR   A 1 126 ? -1.14   -19.093 -27.54  1   34.78 ? 111 TYR   A CZ  1 
ATOM   921  O  OH  . TYR   A 1 126 ? -0.135  -19.969 -27.91  1   34.38 ? 111 TYR   A OH  1 
ATOM   922  N  N   . CYS   A 1 127 ? -3.429  -14.12  -24.69  1   37.67 ? 112 CYS   A N   1 
ATOM   923  C  CA  . CYS   A 1 127 ? -2.372  -13.293 -24.116 1   38.4  ? 112 CYS   A CA  1 
ATOM   924  C  C   . CYS   A 1 127 ? -2.509  -13.134 -22.626 1   39.42 ? 112 CYS   A C   1 
ATOM   925  O  O   . CYS   A 1 127 ? -1.49   -13.082 -21.931 1   40.46 ? 112 CYS   A O   1 
ATOM   926  C  CB  . CYS   A 1 127 ? -2.274  -11.946 -24.802 1   38.28 ? 112 CYS   A CB  1 
ATOM   927  S  SG  . CYS   A 1 127 ? -1.794  -12.031 -26.53  1   41.6  ? 112 CYS   A SG  1 
ATOM   928  N  N   . GLN   A 1 128 ? -3.747  -13.072 -22.112 1   39.11 ? 113 GLN   A N   1 
ATOM   929  C  CA  . GLN   A 1 128 ? -3.953  -12.928 -20.669 1   39.15 ? 113 GLN   A CA  1 
ATOM   930  C  C   . GLN   A 1 128 ? -3.436  -14.162 -19.925 1   39.18 ? 113 GLN   A C   1 
ATOM   931  O  O   . GLN   A 1 128 ? -2.776  -14.06  -18.893 1   39.27 ? 113 GLN   A O   1 
ATOM   932  C  CB  . GLN   A 1 128 ? -5.443  -12.722 -20.353 1   40.81 ? 113 GLN   A CB  1 
ATOM   933  C  CG  . GLN   A 1 128 ? -5.979  -11.373 -20.766 1   44.67 ? 113 GLN   A CG  1 
ATOM   934  C  CD  . GLN   A 1 128 ? -7.489  -11.323 -20.619 1   50.41 ? 113 GLN   A CD  1 
ATOM   935  O  OE1 . GLN   A 1 128 ? -8.202  -12.33  -20.755 1   52.19 ? 113 GLN   A OE1 1 
ATOM   936  N  NE2 . GLN   A 1 128 ? -8.005  -10.139 -20.342 1   51.07 ? 113 GLN   A NE2 1 
ATOM   937  N  N   . LEU   A 1 129 ? -3.757  -15.325 -20.455 1   38.65 ? 114 LEU   A N   1 
ATOM   938  C  CA  . LEU   A 1 129 ? -3.365  -16.586 -19.873 1   38.77 ? 114 LEU   A CA  1 
ATOM   939  C  C   . LEU   A 1 129 ? -1.842  -16.789 -20.004 1   37.64 ? 114 LEU   A C   1 
ATOM   940  O  O   . LEU   A 1 129 ? -1.218  -17.287 -19.078 1   37.37 ? 114 LEU   A O   1 
ATOM   941  C  CB  . LEU   A 1 129 ? -4.127  -17.656 -20.621 1   40.15 ? 114 LEU   A CB  1 
ATOM   942  C  CG  . LEU   A 1 129 ? -4.049  -19.01  -20.068 1   44.62 ? 114 LEU   A CG  1 
ATOM   943  C  CD1 . LEU   A 1 129 ? -4.844  -19.095 -18.771 1   46.17 ? 114 LEU   A CD1 1 
ATOM   944  C  CD2 . LEU   A 1 129 ? -4.616  -19.969 -21.054 1   45.87 ? 114 LEU   A CD2 1 
ATOM   945  N  N   . SER   A 1 130 ? -1.249  -16.324 -21.112 1   36.75 ? 115 SER   A N   1 
ATOM   946  C  CA  . SER   A 1 130 ? 0.185   -16.389 -21.37  1   37.38 ? 115 SER   A CA  1 
ATOM   947  C  C   . SER   A 1 130 ? 0.947   -15.497 -20.391 1   39.09 ? 115 SER   A C   1 
ATOM   948  O  O   . SER   A 1 130 ? 2.003   -15.901 -19.907 1   38.77 ? 115 SER   A O   1 
ATOM   949  C  CB  . SER   A 1 130 ? 0.501   -16.006 -22.815 1   36.16 ? 115 SER   A CB  1 
ATOM   950  O  OG  . SER   A 1 130 ? -0.038  -16.981 -23.696 1   36.45 ? 115 SER   A OG  1 
ATOM   951  N  N   . LYS   A 1 131 ? 0.402   -14.307 -20.084 1   40.31 ? 116 LYS   A N   1 
ATOM   952  C  CA  . LYS   A 1 131 ? 1.001   -13.376 -19.123 1   42.19 ? 116 LYS   A CA  1 
ATOM   953  C  C   . LYS   A 1 131 ? 0.994   -14.016 -17.738 1   43.42 ? 116 LYS   A C   1 
ATOM   954  O  O   . LYS   A 1 131 ? 2.007   -13.975 -17.042 1   44.99 ? 116 LYS   A O   1 
ATOM   955  C  CB  . LYS   A 1 131 ? 0.23    -12.037 -19.09  1   45.21 ? 116 LYS   A CB  1 
ATOM   956  C  CG  . LYS   A 1 131 ? 0.758   -11.049 -18.039 1   51.21 ? 116 LYS   A CG  1 
ATOM   957  C  CD  . LYS   A 1 131 ? -0.292  -10.014 -17.614 1   57.36 ? 116 LYS   A CD  1 
ATOM   958  C  CE  . LYS   A 1 131 ? -0.071  -8.679  -18.285 1   61.89 ? 116 LYS   A CE  1 
ATOM   959  N  NZ  . LYS   A 1 131 ? 1.262   -8.114  -17.94  1   64.62 ? 116 LYS   A NZ  1 
ATOM   960  N  N   . LYS   A 1 132 ? -0.116  -14.67  -17.38  1   42.9  ? 117 LYS   A N   1 
ATOM   961  C  CA  . LYS   A 1 132 ? -0.314  -15.373 -16.124 1   43.27 ? 117 LYS   A CA  1 
ATOM   962  C  C   . LYS   A 1 132 ? 0.678   -16.55  -15.953 1   43.22 ? 117 LYS   A C   1 
ATOM   963  O  O   . LYS   A 1 132 ? 1.201   -16.764 -14.848 1   43.51 ? 117 LYS   A O   1 
ATOM   964  C  CB  . LYS   A 1 132 ? -1.766  -15.863 -16.055 1   45.72 ? 117 LYS   A CB  1 
ATOM   965  C  CG  . LYS   A 1 132 ? -2.159  -16.51  -14.748 1   51.41 ? 117 LYS   A CG  1 
ATOM   966  C  CD  . LYS   A 1 132 ? -3.654  -16.837 -14.693 1   57.06 ? 117 LYS   A CD  1 
ATOM   967  C  CE  . LYS   A 1 132 ? -4.521  -15.605 -14.567 1   61.31 ? 117 LYS   A CE  1 
ATOM   968  N  NZ  . LYS   A 1 132 ? -5.887  -15.922 -14.044 1   63.47 ? 117 LYS   A NZ  1 
ATOM   969  N  N   . LEU   A 1 133 ? 0.908   -17.336 -17.026 1   41.78 ? 118 LEU   A N   1 
ATOM   970  C  CA  . LEU   A 1 133 ? 1.845   -18.463 -16.929 1   40.98 ? 118 LEU   A CA  1 
ATOM   971  C  C   . LEU   A 1 133 ? 3.287   -18.093 -17.266 1   41.06 ? 118 LEU   A C   1 
ATOM   972  O  O   . LEU   A 1 133 ? 4.141   -18.985 -17.255 1   42.31 ? 118 LEU   A O   1 
ATOM   973  C  CB  . LEU   A 1 133 ? 1.391   -19.651 -17.787 1   39.82 ? 118 LEU   A CB  1 
ATOM   974  C  CG  . LEU   A 1 133 ? 0.097   -20.322 -17.362 1   40.34 ? 118 LEU   A CG  1 
ATOM   975  C  CD1 . LEU   A 1 133 ? -0.345  -21.314 -18.398 1   40.32 ? 118 LEU   A CD1 1 
ATOM   976  C  CD2 . LEU   A 1 133 ? 0.257   -21.037 -16.049 1   40.86 ? 118 LEU   A CD2 1 
ATOM   977  N  N   . GLU   A 1 134 ? 3.56    -16.8   -17.559 1   40.38 ? 119 GLU   A N   1 
ATOM   978  C  CA  . GLU   A 1 134 ? 4.857   -16.25  -17.953 1   40.67 ? 119 GLU   A CA  1 
ATOM   979  C  C   . GLU   A 1 134 ? 5.432   -17.002 -19.147 1   40.41 ? 119 GLU   A C   1 
ATOM   980  O  O   . GLU   A 1 134 ? 6.599   -17.415 -19.152 1   40.64 ? 119 GLU   A O   1 
ATOM   981  C  CB  . GLU   A 1 134 ? 5.858   -16.234 -16.797 1   43.81 ? 119 GLU   A CB  1 
ATOM   982  C  CG  . GLU   A 1 134 ? 5.463   -15.358 -15.634 1   48.79 ? 119 GLU   A CG  1 
ATOM   983  C  CD  . GLU   A 1 134 ? 6.584   -15.34  -14.612 1   54.15 ? 119 GLU   A CD  1 
ATOM   984  O  OE1 . GLU   A 1 134 ? 7.695   -14.873 -14.957 1   53.01 ? 119 GLU   A OE1 1 
ATOM   985  O  OE2 . GLU   A 1 134 ? 6.36    -15.836 -13.483 1   57.71 ? 119 GLU   A OE2 1 
ATOM   986  N  N   . LEU   A 1 135 ? 4.584   -17.224 -20.144 1   39.12 ? 120 LEU   A N   1 
ATOM   987  C  CA  . LEU   A 1 135 ? 4.969   -17.897 -21.377 1   37.95 ? 120 LEU   A CA  1 
ATOM   988  C  C   . LEU   A 1 135 ? 4.515   -17     -22.527 1   37.6  ? 120 LEU   A C   1 
ATOM   989  O  O   . LEU   A 1 135 ? 3.519   -16.269 -22.397 1   38.58 ? 120 LEU   A O   1 
ATOM   990  C  CB  . LEU   A 1 135 ? 4.28    -19.272 -21.447 1   37.52 ? 120 LEU   A CB  1 
ATOM   991  C  CG  . LEU   A 1 135 ? 4.936   -20.375 -20.637 1   37.01 ? 120 LEU   A CG  1 
ATOM   992  C  CD1 . LEU   A 1 135 ? 4.084   -21.609 -20.612 1   36.69 ? 120 LEU   A CD1 1 
ATOM   993  C  CD2 . LEU   A 1 135 ? 6.342   -20.666 -21.154 1   37.05 ? 120 LEU   A CD2 1 
ATOM   994  N  N   . PRO   A 1 136 ? 5.235   -17.006 -23.649 1   35.8  ? 121 PRO   A N   1 
ATOM   995  C  CA  . PRO   A 1 136 ? 4.805   -16.182 -24.781 1   34.5  ? 121 PRO   A CA  1 
ATOM   996  C  C   . PRO   A 1 136 ? 3.509   -16.707 -25.426 1   33.44 ? 121 PRO   A C   1 
ATOM   997  O  O   . PRO   A 1 136 ? 3.191   -17.886 -25.299 1   33.02 ? 121 PRO   A O   1 
ATOM   998  C  CB  . PRO   A 1 136 ? 6.003   -16.257 -25.73  1   35.32 ? 121 PRO   A CB  1 
ATOM   999  C  CG  . PRO   A 1 136 ? 6.638   -17.554 -25.435 1   36.03 ? 121 PRO   A CG  1 
ATOM   1000 C  CD  . PRO   A 1 136 ? 6.443   -17.801 -23.973 1   34.92 ? 121 PRO   A CD  1 
ATOM   1001 N  N   . PRO   A 1 137 ? 2.738   -15.84  -26.106 1   33.03 ? 122 PRO   A N   1 
ATOM   1002 C  CA  . PRO   A 1 137 ? 1.478   -16.296 -26.723 1   33.33 ? 122 PRO   A CA  1 
ATOM   1003 C  C   . PRO   A 1 137 ? 1.663   -17.003 -28.081 1   33.27 ? 122 PRO   A C   1 
ATOM   1004 O  O   . PRO   A 1 137 ? 1.221   -16.528 -29.145 1   32.96 ? 122 PRO   A O   1 
ATOM   1005 C  CB  . PRO   A 1 137 ? 0.647   -15.009 -26.824 1   33.66 ? 122 PRO   A CB  1 
ATOM   1006 C  CG  . PRO   A 1 137 ? 1.703   -13.939 -27.044 1   34.02 ? 122 PRO   A CG  1 
ATOM   1007 C  CD  . PRO   A 1 137 ? 2.935   -14.382 -26.266 1   32.84 ? 122 PRO   A CD  1 
ATOM   1008 N  N   . ILE   A 1 138 ? 2.346   -18.153 -28.042 1   31.66 ? 123 ILE   A N   1 
ATOM   1009 C  CA  . ILE   A 1 138 ? 2.634   -19.011 -29.195 1   30.03 ? 123 ILE   A CA  1 
ATOM   1010 C  C   . ILE   A 1 138 ? 2.84    -20.405 -28.592 1   29.14 ? 123 ILE   A C   1 
ATOM   1011 O  O   . ILE   A 1 138 ? 3.215   -20.527 -27.414 1   27.85 ? 123 ILE   A O   1 
ATOM   1012 C  CB  . ILE   A 1 138 ? 3.888   -18.538 -30.016 1   30.36 ? 123 ILE   A CB  1 
ATOM   1013 C  CG1 . ILE   A 1 138 ? 4.032   -19.328 -31.339 1   31.44 ? 123 ILE   A CG1 1 
ATOM   1014 C  CG2 . ILE   A 1 138 ? 5.197   -18.608 -29.185 1   30.47 ? 123 ILE   A CG2 1 
ATOM   1015 C  CD1 . ILE   A 1 138 ? 4.991   -18.723 -32.377 1   32.63 ? 123 ILE   A CD1 1 
ATOM   1016 N  N   . LEU   A 1 139 ? 2.517   -21.468 -29.351 1   29.06 ? 124 LEU   A N   1 
ATOM   1017 C  CA  . LEU   A 1 139 ? 2.748   -22.828 -28.872 1   29.4  ? 124 LEU   A CA  1 
ATOM   1018 C  C   . LEU   A 1 139 ? 4.243   -23.043 -28.594 1   28.36 ? 124 LEU   A C   1 
ATOM   1019 O  O   . LEU   A 1 139 ? 5.096   -22.686 -29.415 1   27.82 ? 124 LEU   A O   1 
ATOM   1020 C  CB  . LEU   A 1 139 ? 2.323   -23.867 -29.911 1   30.49 ? 124 LEU   A CB  1 
ATOM   1021 C  CG  . LEU   A 1 139 ? 0.911   -24.384 -29.836 1   33.13 ? 124 LEU   A CG  1 
ATOM   1022 C  CD1 . LEU   A 1 139 ? 0.619   -25.278 -31.05  1   34.89 ? 124 LEU   A CD1 1 
ATOM   1023 C  CD2 . LEU   A 1 139 ? 0.594   -25.107 -28.52  1   32.67 ? 124 LEU   A CD2 1 
ATOM   1024 N  N   . VAL   A 1 140 ? 4.556   -23.53  -27.394 1   27.8  ? 125 VAL   A N   1 
ATOM   1025 C  CA  . VAL   A 1 140 ? 5.934   -23.852 -27.016 1   27.6  ? 125 VAL   A CA  1 
ATOM   1026 C  C   . VAL   A 1 140 ? 6.033   -25.372 -26.786 1   27.37 ? 125 VAL   A C   1 
ATOM   1027 O  O   . VAL   A 1 140 ? 5.015   -26.066 -26.737 1   27.67 ? 125 VAL   A O   1 
ATOM   1028 C  CB  . VAL   A 1 140 ? 6.39    -23.052 -25.762 1   28.19 ? 125 VAL   A CB  1 
ATOM   1029 C  CG1 . VAL   A 1 140 ? 6.372   -21.54  -26.028 1   29.41 ? 125 VAL   A CG1 1 
ATOM   1030 C  CG2 . VAL   A 1 140 ? 5.553   -23.407 -24.527 1   27.56 ? 125 VAL   A CG2 1 
ATOM   1031 N  N   . TYR   A 1 141 ? 7.249   -25.894 -26.634 1   27.09 ? 126 TYR   A N   1 
ATOM   1032 C  CA  . TYR   A 1 141 ? 7.524   -27.3   -26.335 1   27.31 ? 126 TYR   A CA  1 
ATOM   1033 C  C   . TYR   A 1 141 ? 6.738   -27.742 -25.075 1   27.02 ? 126 TYR   A C   1 
ATOM   1034 O  O   . TYR   A 1 141 ? 6.168   -28.826 -25.072 1   28.21 ? 126 TYR   A O   1 
ATOM   1035 C  CB  . TYR   A 1 141 ? 9.044   -27.435 -26.098 1   27.22 ? 126 TYR   A CB  1 
ATOM   1036 C  CG  . TYR   A 1 141 ? 9.551   -28.83  -25.822 1   27.96 ? 126 TYR   A CG  1 
ATOM   1037 C  CD1 . TYR   A 1 141 ? 9.873   -29.689 -26.861 1   28.68 ? 126 TYR   A CD1 1 
ATOM   1038 C  CD2 . TYR   A 1 141 ? 9.823   -29.247 -24.526 1   28.38 ? 126 TYR   A CD2 1 
ATOM   1039 C  CE1 . TYR   A 1 141 ? 10.396  -30.953 -26.616 1   29.64 ? 126 TYR   A CE1 1 
ATOM   1040 C  CE2 . TYR   A 1 141 ? 10.333  -30.51  -24.266 1   29.38 ? 126 TYR   A CE2 1 
ATOM   1041 C  CZ  . TYR   A 1 141 ? 10.651  -31.353 -25.315 1   29.93 ? 126 TYR   A CZ  1 
ATOM   1042 O  OH  . TYR   A 1 141 ? 11.165  -32.6   -25.059 1   29.31 ? 126 TYR   A OH  1 
ATOM   1043 N  N   . ALA   A 1 142 ? 6.652   -26.875 -24.045 1   26.18 ? 127 ALA   A N   1 
ATOM   1044 C  CA  . ALA   A 1 142 ? 5.889   -27.163 -22.82  1   27.23 ? 127 ALA   A CA  1 
ATOM   1045 C  C   . ALA   A 1 142 ? 4.381   -27.333 -23.057 1   27.61 ? 127 ALA   A C   1 
ATOM   1046 O  O   . ALA   A 1 142 ? 3.7     -27.945 -22.23  1   28.38 ? 127 ALA   A O   1 
ATOM   1047 C  CB  . ALA   A 1 142 ? 6.132   -26.095 -21.75  1   27.77 ? 127 ALA   A CB  1 
ATOM   1048 N  N   . ASP   A 1 143 ? 3.849   -26.795 -24.152 1   27.69 ? 128 ASP   A N   1 
ATOM   1049 C  CA  . ASP   A 1 143 ? 2.44    -26.999 -24.462 1   27.42 ? 128 ASP   A CA  1 
ATOM   1050 C  C   . ASP   A 1 143 ? 2.27    -28.303 -25.211 1   28.42 ? 128 ASP   A C   1 
ATOM   1051 O  O   . ASP   A 1 143 ? 1.618   -29.236 -24.742 1   28.76 ? 128 ASP   A O   1 
ATOM   1052 C  CB  . ASP   A 1 143 ? 1.846   -25.854 -25.305 1   28.32 ? 128 ASP   A CB  1 
ATOM   1053 C  CG  . ASP   A 1 143 ? 1.955   -24.468 -24.728 1   28.77 ? 128 ASP   A CG  1 
ATOM   1054 O  OD1 . ASP   A 1 143 ? 1.611   -24.29  -23.551 1   29.27 ? 128 ASP   A OD1 1 
ATOM   1055 O  OD2 . ASP   A 1 143 ? 2.374   -23.572 -25.456 1   30.31 ? 128 ASP   A OD2 1 
ATOM   1056 N  N   . CYS   A 1 144 ? 2.849   -28.35  -26.41  1   29.21 ? 129 CYS   A N   1 
ATOM   1057 C  CA  . CYS   A 1 144 ? 2.663   -29.351 -27.414 1   31.17 ? 129 CYS   A CA  1 
ATOM   1058 C  C   . CYS   A 1 144 ? 3.301   -30.697 -27.107 1   31.38 ? 129 CYS   A C   1 
ATOM   1059 O  O   . CYS   A 1 144 ? 2.831   -31.732 -27.611 1   32.02 ? 129 CYS   A O   1 
ATOM   1060 C  CB  . CYS   A 1 144 ? 3.165   -28.781 -28.73  1   34.93 ? 129 CYS   A CB  1 
ATOM   1061 S  SG  . CYS   A 1 144 ? 2.014   -28.927 -30.078 1   47.05 ? 129 CYS   A SG  1 
ATOM   1062 N  N   . VAL   A 1 145 ? 4.339   -30.709 -26.278 1   30.16 ? 130 VAL   A N   1 
ATOM   1063 C  CA  . VAL   A 1 145 ? 4.958   -31.968 -25.884 1   30.53 ? 130 VAL   A CA  1 
ATOM   1064 C  C   . VAL   A 1 145 ? 4.666   -32.282 -24.39  1   30.72 ? 130 VAL   A C   1 
ATOM   1065 O  O   . VAL   A 1 145 ? 4.075   -33.316 -24.069 1   31.57 ? 130 VAL   A O   1 
ATOM   1066 C  CB  . VAL   A 1 145 ? 6.483   -31.983 -26.214 1   31.06 ? 130 VAL   A CB  1 
ATOM   1067 C  CG1 . VAL   A 1 145 ? 7.149   -33.248 -25.674 1   30.54 ? 130 VAL   A CG1 1 
ATOM   1068 C  CG2 . VAL   A 1 145 ? 6.706   -31.853 -27.73  1   31.03 ? 130 VAL   A CG2 1 
ATOM   1069 N  N   . LEU   A 1 146 ? 5       -31.364 -23.513 1   29.37 ? 131 LEU   A N   1 
ATOM   1070 C  CA  . LEU   A 1 146 ? 4.926   -31.585 -22.073 1   28.99 ? 131 LEU   A CA  1 
ATOM   1071 C  C   . LEU   A 1 146 ? 3.517   -31.649 -21.472 1   29.94 ? 131 LEU   A C   1 
ATOM   1072 O  O   . LEU   A 1 146 ? 3.338   -32.34  -20.477 1   31.26 ? 131 LEU   A O   1 
ATOM   1073 C  CB  . LEU   A 1 146 ? 5.774   -30.539 -21.347 1   28.13 ? 131 LEU   A CB  1 
ATOM   1074 C  CG  . LEU   A 1 146 ? 7.279   -30.472 -21.747 1   29.01 ? 131 LEU   A CG  1 
ATOM   1075 C  CD1 . LEU   A 1 146 ? 8.047   -29.525 -20.859 1   28.61 ? 131 LEU   A CD1 1 
ATOM   1076 C  CD2 . LEU   A 1 146 ? 7.95    -31.847 -21.71  1   30.02 ? 131 LEU   A CD2 1 
ATOM   1077 N  N   . ALA   A 1 147 ? 2.531   -30.96  -22.062 1   29.33 ? 132 ALA   A N   1 
ATOM   1078 C  CA  . ALA   A 1 147 ? 1.145   -30.954 -21.558 1   29.8  ? 132 ALA   A CA  1 
ATOM   1079 C  C   . ALA   A 1 147 ? 0.113   -31.568 -22.51  1   29.88 ? 132 ALA   A C   1 
ATOM   1080 O  O   . ALA   A 1 147 ? -1.088  -31.572 -22.194 1   30.17 ? 132 ALA   A O   1 
ATOM   1081 C  CB  . ALA   A 1 147 ? 0.73    -29.537 -21.229 1   29.02 ? 132 ALA   A CB  1 
ATOM   1082 N  N   . ASN   A 1 148 ? 0.556   -32.04  -23.685 1   29.38 ? 133 ASN   A N   1 
ATOM   1083 C  CA  . ASN   A 1 148 ? -0.328  -32.556 -24.733 1   29.7  ? 133 ASN   A CA  1 
ATOM   1084 C  C   . ASN   A 1 148 ? -0.388  -34.069 -24.742 1   30.34 ? 133 ASN   A C   1 
ATOM   1085 O  O   . ASN   A 1 148 ? -0.174  -34.699 -25.771 1   30.73 ? 133 ASN   A O   1 
ATOM   1086 C  CB  . ASN   A 1 148 ? 0.139   -32.011 -26.096 1   29.9  ? 133 ASN   A CB  1 
ATOM   1087 C  CG  . ASN   A 1 148 ? -0.779  -32.262 -27.269 1   30.76 ? 133 ASN   A CG  1 
ATOM   1088 O  OD1 . ASN   A 1 148 ? -1.973  -32.527 -27.105 1   30.79 ? 133 ASN   A OD1 1 
ATOM   1089 N  ND2 . ASN   A 1 148 ? -0.246  -32.155 -28.485 1   29.29 ? 133 ASN   A ND2 1 
ATOM   1090 N  N   . TRP   A 1 149 ? -0.718  -34.658 -23.599 1   30.77 ? 134 TRP   A N   1 
ATOM   1091 C  CA  . TRP   A 1 149 ? -0.729  -36.099 -23.496 1   30.74 ? 134 TRP   A CA  1 
ATOM   1092 C  C   . TRP   A 1 149 ? -1.647  -36.636 -22.421 1   31.89 ? 134 TRP   A C   1 
ATOM   1093 O  O   . TRP   A 1 149 ? -2.063  -35.911 -21.541 1   31.69 ? 134 TRP   A O   1 
ATOM   1094 C  CB  . TRP   A 1 149 ? 0.732   -36.598 -23.294 1   30.35 ? 134 TRP   A CB  1 
ATOM   1095 C  CG  . TRP   A 1 149 ? 1.332   -36.219 -21.977 1   30.65 ? 134 TRP   A CG  1 
ATOM   1096 C  CD1 . TRP   A 1 149 ? 1.951   -35.047 -21.654 1   31.39 ? 134 TRP   A CD1 1 
ATOM   1097 C  CD2 . TRP   A 1 149 ? 1.353   -37.024 -20.799 1   31.64 ? 134 TRP   A CD2 1 
ATOM   1098 N  NE1 . TRP   A 1 149 ? 2.381   -35.087 -20.347 1   31.8  ? 134 TRP   A NE1 1 
ATOM   1099 C  CE2 . TRP   A 1 149 ? 2.03    -36.298 -19.802 1   32.42 ? 134 TRP   A CE2 1 
ATOM   1100 C  CE3 . TRP   A 1 149 ? 0.904   -38.317 -20.502 1   33.03 ? 134 TRP   A CE3 1 
ATOM   1101 C  CZ2 . TRP   A 1 149 ? 2.267   -36.824 -18.53  1   34.26 ? 134 TRP   A CZ2 1 
ATOM   1102 C  CZ3 . TRP   A 1 149 ? 1.102   -38.814 -19.23  1   34.6  ? 134 TRP   A CZ3 1 
ATOM   1103 C  CH2 . TRP   A 1 149 ? 1.78    -38.076 -18.263 1   34.81 ? 134 TRP   A CH2 1 
ATOM   1104 N  N   . LYS   A 1 150 ? -1.957  -37.929 -22.504 1   32.63 ? 135 LYS   A N   1 
ATOM   1105 C  CA  . LYS   A 1 150 ? -2.776  -38.615 -21.521 1   34.23 ? 135 LYS   A CA  1 
ATOM   1106 C  C   . LYS   A 1 150 ? -2.411  -40.087 -21.511 1   36.4  ? 135 LYS   A C   1 
ATOM   1107 O  O   . LYS   A 1 150 ? -1.88   -40.616 -22.491 1   36.01 ? 135 LYS   A O   1 
ATOM   1108 C  CB  . LYS   A 1 150 ? -4.279  -38.485 -21.877 1   35.84 ? 135 LYS   A CB  1 
ATOM   1109 C  CG  . LYS   A 1 150 ? -4.645  -39.131 -23.224 1   41.05 ? 135 LYS   A CG  1 
ATOM   1110 C  CD  . LYS   A 1 150 ? -6.134  -39.067 -23.538 1   46.65 ? 135 LYS   A CD  1 
ATOM   1111 C  CE  . LYS   A 1 150 ? -6.939  -40.061 -22.741 1   52.81 ? 135 LYS   A CE  1 
ATOM   1112 N  NZ  . LYS   A 1 150 ? -8.395  -39.951 -23.05  1   57.13 ? 135 LYS   A NZ  1 
ATOM   1113 N  N   . LYS   A 1 151 ? -2.707  -40.753 -20.404 1   38.28 ? 136 LYS   A N   1 
ATOM   1114 C  CA  . LYS   A 1 151 ? -2.606  -42.197 -20.321 1   40.19 ? 136 LYS   A CA  1 
ATOM   1115 C  C   . LYS   A 1 151 ? -3.982  -42.704 -20.789 1   42.3  ? 136 LYS   A C   1 
ATOM   1116 O  O   . LYS   A 1 151 ? -5.008  -42.126 -20.418 1   42.96 ? 136 LYS   A O   1 
ATOM   1117 C  CB  . LYS   A 1 151 ? -2.429  -42.641 -18.859 1   41.37 ? 136 LYS   A CB  1 
ATOM   1118 C  CG  . LYS   A 1 151 ? -1.003  -42.795 -18.398 1   43.83 ? 136 LYS   A CG  1 
ATOM   1119 C  CD  . LYS   A 1 151 ? -0.955  -43.278 -16.961 1   46.27 ? 136 LYS   A CD  1 
ATOM   1120 C  CE  . LYS   A 1 151 ? 0.463   -43.573 -16.536 1   49.24 ? 136 LYS   A CE  1 
ATOM   1121 N  NZ  . LYS   A 1 151 ? 0.501   -44.39  -15.298 1   50.43 ? 136 LYS   A NZ  1 
ATOM   1122 N  N   . LYS   A 1 152 ? -4.012  -43.783 -21.569 1   43.59 ? 137 LYS   A N   1 
ATOM   1123 C  CA  . LYS   A 1 152 ? -5.269  -44.415 -22.002 1   45.14 ? 137 LYS   A CA  1 
ATOM   1124 C  C   . LYS   A 1 152 ? -5.877  -45.131 -20.773 1   47.37 ? 137 LYS   A C   1 
ATOM   1125 O  O   . LYS   A 1 152 ? -7.058  -44.966 -20.484 1   48.27 ? 137 LYS   A O   1 
ATOM   1126 C  CB  . LYS   A 1 152 ? -5.002  -45.427 -23.128 1   45.25 ? 137 LYS   A CB  1 
ATOM   1127 C  CG  . LYS   A 1 152 ? -4.62   -44.767 -24.436 1   47.99 ? 137 LYS   A CG  1 
ATOM   1128 C  CD  . LYS   A 1 152 ? -4.281  -45.809 -25.469 1   51.61 ? 137 LYS   A CD  1 
ATOM   1129 C  CE  . LYS   A 1 152 ? -3.968  -45.181 -26.794 1   55.11 ? 137 LYS   A CE  1 
ATOM   1130 N  NZ  . LYS   A 1 152 ? -3.612  -46.202 -27.806 1   58.28 ? 137 LYS   A NZ  1 
ATOM   1131 N  N   . ASP   A 1 153 ? -5.037  -45.859 -20.024 1   48.32 ? 138 ASP   A N   1 
ATOM   1132 C  CA  . ASP   A 1 153 ? -5.399  -46.562 -18.81  1   49.8  ? 138 ASP   A CA  1 
ATOM   1133 C  C   . ASP   A 1 153 ? -4.535  -46.015 -17.684 1   50.53 ? 138 ASP   A C   1 
ATOM   1134 O  O   . ASP   A 1 153 ? -3.338  -46.279 -17.65  1   49.68 ? 138 ASP   A O   1 
ATOM   1135 C  CB  . ASP   A 1 153 ? -5.143  -48.074 -18.979 1   52    ? 138 ASP   A CB  1 
ATOM   1136 C  CG  . ASP   A 1 153 ? -5.58   -48.938 -17.803 1   56.21 ? 138 ASP   A CG  1 
ATOM   1137 O  OD1 . ASP   A 1 153 ? -5.997  -48.375 -16.768 1   56.35 ? 138 ASP   A OD1 1 
ATOM   1138 O  OD2 . ASP   A 1 153 ? -5.511  -50.173 -17.92  1   58.99 ? 138 ASP   A OD2 1 
ATOM   1139 N  N   . PRO   A 1 154 ? -5.147  -45.301 -16.715 1   51.66 ? 139 PRO   A N   1 
ATOM   1140 C  CA  . PRO   A 1 154 ? -4.37   -44.763 -15.579 1   52.15 ? 139 PRO   A CA  1 
ATOM   1141 C  C   . PRO   A 1 154 ? -3.643  -45.814 -14.743 1   52.5  ? 139 PRO   A C   1 
ATOM   1142 O  O   . PRO   A 1 154 ? -2.708  -45.478 -14.018 1   52.59 ? 139 PRO   A O   1 
ATOM   1143 C  CB  . PRO   A 1 154 ? -5.433  -44.045 -14.733 1   52.88 ? 139 PRO   A CB  1 
ATOM   1144 C  CG  . PRO   A 1 154 ? -6.567  -43.78  -15.672 1   53.3  ? 139 PRO   A CG  1 
ATOM   1145 C  CD  . PRO   A 1 154 ? -6.574  -44.939 -16.618 1   51.47 ? 139 PRO   A CD  1 
ATOM   1146 N  N   . ASN   A 1 155 ? -4.062  -47.086 -14.836 1   52.52 ? 140 ASN   A N   1 
ATOM   1147 C  CA  . ASN   A 1 155 ? -3.415  -48.157 -14.073 1   53.03 ? 140 ASN   A CA  1 
ATOM   1148 C  C   . ASN   A 1 155 ? -2.24   -48.811 -14.794 1   52.07 ? 140 ASN   A C   1 
ATOM   1149 O  O   . ASN   A 1 155 ? -1.54   -49.62  -14.191 1   52.18 ? 140 ASN   A O   1 
ATOM   1150 C  CB  . ASN   A 1 155 ? -4.437  -49.2   -13.625 1   55.87 ? 140 ASN   A CB  1 
ATOM   1151 C  CG  . ASN   A 1 155 ? -5.607  -48.581 -12.898 1   61.61 ? 140 ASN   A CG  1 
ATOM   1152 O  OD1 . ASN   A 1 155 ? -5.444  -47.745 -11.996 1   63.64 ? 140 ASN   A OD1 1 
ATOM   1153 N  ND2 . ASN   A 1 155 ? -6.817  -48.947 -13.303 1   63.46 ? 140 ASN   A ND2 1 
ATOM   1154 N  N   . LYS   A 1 156 ? -1.994  -48.456 -16.063 1   51.09 ? 141 LYS   A N   1 
ATOM   1155 C  CA  . LYS   A 1 156 ? -0.868  -49.001 -16.817 1   50.41 ? 141 LYS   A CA  1 
ATOM   1156 C  C   . LYS   A 1 156 ? 0.296   -47.978 -16.899 1   49.45 ? 141 LYS   A C   1 
ATOM   1157 O  O   . LYS   A 1 156 ? 0.068   -46.771 -16.747 1   48.72 ? 141 LYS   A O   1 
ATOM   1158 C  CB  . LYS   A 1 156 ? -1.339  -49.484 -18.193 1   52.07 ? 141 LYS   A CB  1 
ATOM   1159 C  CG  . LYS   A 1 156 ? -2.151  -50.764 -18.101 1   56.46 ? 141 LYS   A CG  1 
ATOM   1160 C  CD  . LYS   A 1 156 ? -2.694  -51.177 -19.46  1   60.99 ? 141 LYS   A CD  1 
ATOM   1161 C  CE  . LYS   A 1 156 ? -3.574  -52.4   -19.381 1   64.16 ? 141 LYS   A CE  1 
ATOM   1162 N  NZ  . LYS   A 1 156 ? -4.698  -52.321 -20.354 1   66.18 ? 141 LYS   A NZ  1 
ATOM   1163 N  N   . PRO   A 1 157 ? 1.551   -48.435 -17.08  1   49.11 ? 142 PRO   A N   1 
ATOM   1164 C  CA  . PRO   A 1 157 ? 2.68    -47.488 -17.079 1   48.55 ? 142 PRO   A CA  1 
ATOM   1165 C  C   . PRO   A 1 157 ? 2.767   -46.555 -18.306 1   47.46 ? 142 PRO   A C   1 
ATOM   1166 O  O   . PRO   A 1 157 ? 1.964   -46.644 -19.233 1   47.4  ? 142 PRO   A O   1 
ATOM   1167 C  CB  . PRO   A 1 157 ? 3.904   -48.409 -16.947 1   49.1  ? 142 PRO   A CB  1 
ATOM   1168 C  CG  . PRO   A 1 157 ? 3.48    -49.676 -17.573 1   49.87 ? 142 PRO   A CG  1 
ATOM   1169 C  CD  . PRO   A 1 157 ? 2.022   -49.831 -17.224 1   48.76 ? 142 PRO   A CD  1 
ATOM   1170 N  N   . LEU   A 1 158 ? 3.735   -45.633 -18.276 1   46.28 ? 143 LEU   A N   1 
ATOM   1171 C  CA  . LEU   A 1 158 ? 3.961   -44.681 -19.343 1   45.73 ? 143 LEU   A CA  1 
ATOM   1172 C  C   . LEU   A 1 158 ? 4.718   -45.297 -20.499 1   44.39 ? 143 LEU   A C   1 
ATOM   1173 O  O   . LEU   A 1 158 ? 5.942   -45.173 -20.592 1   43.82 ? 143 LEU   A O   1 
ATOM   1174 C  CB  . LEU   A 1 158 ? 4.717   -43.467 -18.821 1   46.1  ? 143 LEU   A CB  1 
ATOM   1175 C  CG  . LEU   A 1 158 ? 3.905   -42.526 -17.976 1   48.17 ? 143 LEU   A CG  1 
ATOM   1176 C  CD1 . LEU   A 1 158 ? 4.8     -41.536 -17.294 1   48.99 ? 143 LEU   A CD1 1 
ATOM   1177 C  CD2 . LEU   A 1 158 ? 2.852   -41.838 -18.794 1   48.19 ? 143 LEU   A CD2 1 
ATOM   1178 N  N   . THR   A 1 159 ? 3.978   -45.977 -21.377 1   43.57 ? 144 THR   A N   1 
ATOM   1179 C  CA  . THR   A 1 159 ? 4.491   -46.559 -22.607 1   43.05 ? 144 THR   A CA  1 
ATOM   1180 C  C   . THR   A 1 159 ? 3.718   -45.964 -23.776 1   42.29 ? 144 THR   A C   1 
ATOM   1181 O  O   . THR   A 1 159 ? 2.582   -45.519 -23.598 1   42.18 ? 144 THR   A O   1 
ATOM   1182 C  CB  . THR   A 1 159 ? 4.397   -48.088 -22.586 1   44.63 ? 144 THR   A CB  1 
ATOM   1183 O  OG1 . THR   A 1 159 ? 3.03    -48.487 -22.65  1   45.21 ? 144 THR   A OG1 1 
ATOM   1184 C  CG2 . THR   A 1 159 ? 5.143   -48.723 -21.399 1   45.28 ? 144 THR   A CG2 1 
ATOM   1185 N  N   . TYR   A 1 160 ? 4.285   -46.003 -24.996 1   41.69 ? 145 TYR   A N   1 
ATOM   1186 C  CA  . TYR   A 1 160 ? 3.622   -45.464 -26.181 1   41.11 ? 145 TYR   A CA  1 
ATOM   1187 C  C   . TYR   A 1 160 ? 2.232   -46.063 -26.373 1   41.81 ? 145 TYR   A C   1 
ATOM   1188 O  O   . TYR   A 1 160 ? 1.272   -45.329 -26.642 1   41.58 ? 145 TYR   A O   1 
ATOM   1189 C  CB  . TYR   A 1 160 ? 4.478   -45.677 -27.433 1   40.72 ? 145 TYR   A CB  1 
ATOM   1190 C  CG  . TYR   A 1 160 ? 3.966   -44.908 -28.635 1   40.94 ? 145 TYR   A CG  1 
ATOM   1191 C  CD1 . TYR   A 1 160 ? 4.411   -43.616 -28.904 1   41.07 ? 145 TYR   A CD1 1 
ATOM   1192 C  CD2 . TYR   A 1 160 ? 3.02    -45.46  -29.489 1   41.5  ? 145 TYR   A CD2 1 
ATOM   1193 C  CE1 . TYR   A 1 160 ? 3.931   -42.899 -29.994 1   41.29 ? 145 TYR   A CE1 1 
ATOM   1194 C  CE2 . TYR   A 1 160 ? 2.485   -44.726 -30.54  1   42.05 ? 145 TYR   A CE2 1 
ATOM   1195 C  CZ  . TYR   A 1 160 ? 2.981   -43.464 -30.82  1   42.06 ? 145 TYR   A CZ  1 
ATOM   1196 O  OH  . TYR   A 1 160 ? 2.5     -42.763 -31.893 1   42.97 ? 145 TYR   A OH  1 
ATOM   1197 N  N   . GLU   A 1 161 ? 2.114   -47.389 -26.14  1   41.95 ? 146 GLU   A N   1 
ATOM   1198 C  CA  . GLU   A 1 161 ? 0.847   -48.12  -26.284 1   42.33 ? 146 GLU   A CA  1 
ATOM   1199 C  C   . GLU   A 1 161 ? -0.229  -47.622 -25.349 1   41.73 ? 146 GLU   A C   1 
ATOM   1200 O  O   . GLU   A 1 161 ? -1.392  -47.606 -25.715 1   43.2  ? 146 GLU   A O   1 
ATOM   1201 C  CB  . GLU   A 1 161 ? 1.051   -49.634 -26.081 1   45.06 ? 146 GLU   A CB  1 
ATOM   1202 C  CG  . GLU   A 1 161 ? 1.496   -50.334 -27.344 1   50.48 ? 146 GLU   A CG  1 
ATOM   1203 C  CD  . GLU   A 1 161 ? 2.881   -49.913 -27.775 1   56.4  ? 146 GLU   A CD  1 
ATOM   1204 O  OE1 . GLU   A 1 161 ? 3.778   -49.855 -26.902 1   57.88 ? 146 GLU   A OE1 1 
ATOM   1205 O  OE2 . GLU   A 1 161 ? 3.06    -49.604 -28.976 1   57.57 ? 146 GLU   A OE2 1 
ATOM   1206 N  N   . ASN   A 1 162 ? 0.156   -47.178 -24.167 1   40.54 ? 147 ASN   A N   1 
ATOM   1207 C  CA  . ASN   A 1 162 ? -0.783  -46.678 -23.179 1   40.15 ? 147 ASN   A CA  1 
ATOM   1208 C  C   . ASN   A 1 162 ? -0.915  -45.151 -23.198 1   39.67 ? 147 ASN   A C   1 
ATOM   1209 O  O   . ASN   A 1 162 ? -1.425  -44.587 -22.24  1   39.85 ? 147 ASN   A O   1 
ATOM   1210 C  CB  . ASN   A 1 162 ? -0.363  -47.148 -21.774 1   40.58 ? 147 ASN   A CB  1 
ATOM   1211 C  CG  . ASN   A 1 162 ? -1.445  -46.92  -20.763 1   44.36 ? 147 ASN   A CG  1 
ATOM   1212 O  OD1 . ASN   A 1 162 ? -2.631  -47.127 -21.05  1   45.86 ? 147 ASN   A OD1 1 
ATOM   1213 N  ND2 . ASN   A 1 162 ? -1.076  -46.427 -19.587 1   45.06 ? 147 ASN   A ND2 1 
ATOM   1214 N  N   . MET   A 1 163 ? -0.466  -44.471 -24.268 1   38.97 ? 148 MET   A N   1 
ATOM   1215 C  CA  . MET   A 1 163 ? -0.514  -43.014 -24.305 1   37.79 ? 148 MET   A CA  1 
ATOM   1216 C  C   . MET   A 1 163 ? -1.133  -42.466 -25.569 1   37.16 ? 148 MET   A C   1 
ATOM   1217 O  O   . MET   A 1 163 ? -1.201  -43.136 -26.587 1   36.82 ? 148 MET   A O   1 
ATOM   1218 C  CB  . MET   A 1 163 ? 0.911   -42.453 -24.116 1   37.9  ? 148 MET   A CB  1 
ATOM   1219 C  CG  . MET   A 1 163 ? 1.503   -42.769 -22.755 1   40.05 ? 148 MET   A CG  1 
ATOM   1220 S  SD  . MET   A 1 163 ? 3.295   -42.48  -22.672 1   41.08 ? 148 MET   A SD  1 
ATOM   1221 C  CE  . MET   A 1 163 ? 3.295   -40.741 -22.45  1   36.7  ? 148 MET   A CE  1 
ATOM   1222 N  N   . ASP   A 1 164 ? -1.562  -41.224 -25.504 1   36.76 ? 149 ASP   A N   1 
ATOM   1223 C  CA  . ASP   A 1 164 ? -2.106  -40.521 -26.647 1   36.8  ? 149 ASP   A CA  1 
ATOM   1224 C  C   . ASP   A 1 164 ? -1.895  -39.011 -26.464 1   35.12 ? 149 ASP   A C   1 
ATOM   1225 O  O   . ASP   A 1 164 ? -1.656  -38.548 -25.355 1   35.35 ? 149 ASP   A O   1 
ATOM   1226 C  CB  . ASP   A 1 164 ? -3.598  -40.848 -26.841 1   40.47 ? 149 ASP   A CB  1 
ATOM   1227 C  CG  . ASP   A 1 164 ? -4.045  -40.825 -28.294 1   47.43 ? 149 ASP   A CG  1 
ATOM   1228 O  OD1 . ASP   A 1 164 ? -3.306  -40.242 -29.145 1   47.95 ? 149 ASP   A OD1 1 
ATOM   1229 O  OD2 . ASP   A 1 164 ? -5.134  -41.372 -28.585 1   50.69 ? 149 ASP   A OD2 1 
ATOM   1230 N  N   . VAL   A 1 165 ? -1.933  -38.266 -27.549 1   33.69 ? 150 VAL   A N   1 
ATOM   1231 C  CA  . VAL   A 1 165 ? -1.865  -36.811 -27.497 1   33.49 ? 150 VAL   A CA  1 
ATOM   1232 C  C   . VAL   A 1 165 ? -3.289  -36.267 -27.361 1   34.74 ? 150 VAL   A C   1 
ATOM   1233 O  O   . VAL   A 1 165 ? -4.255  -36.975 -27.664 1   36.36 ? 150 VAL   A O   1 
ATOM   1234 C  CB  . VAL   A 1 165 ? -1.145  -36.203 -28.727 1   32.64 ? 150 VAL   A CB  1 
ATOM   1235 C  CG1 . VAL   A 1 165 ? 0.304   -36.66  -28.778 1   32.77 ? 150 VAL   A CG1 1 
ATOM   1236 C  CG2 . VAL   A 1 165 ? -1.885  -36.53  -30.033 1   32.06 ? 150 VAL   A CG2 1 
ATOM   1237 N  N   . LEU   A 1 166 ? -3.436  -35.019 -26.922 1   33.97 ? 151 LEU   A N   1 
ATOM   1238 C  CA  . LEU   A 1 166 ? -4.755  -34.421 -26.788 1   34.13 ? 151 LEU   A CA  1 
ATOM   1239 C  C   . LEU   A 1 166 ? -5.174  -33.749 -28.089 1   34.98 ? 151 LEU   A C   1 
ATOM   1240 O  O   . LEU   A 1 166 ? -6.344  -33.828 -28.46  1   34.54 ? 151 LEU   A O   1 
ATOM   1241 C  CB  . LEU   A 1 166 ? -4.791  -33.435 -25.612 1   33.45 ? 151 LEU   A CB  1 
ATOM   1242 C  CG  . LEU   A 1 166 ? -4.295  -33.982 -24.265 1   35.15 ? 151 LEU   A CG  1 
ATOM   1243 C  CD1 . LEU   A 1 166 ? -4.469  -32.952 -23.169 1   35.76 ? 151 LEU   A CD1 1 
ATOM   1244 C  CD2 . LEU   A 1 166 ? -5.053  -35.238 -23.861 1   35.72 ? 151 LEU   A CD2 1 
ATOM   1245 N  N   . PHE   A 1 167 ? -4.215  -33.092 -28.793 1   35.38 ? 152 PHE   A N   1 
ATOM   1246 C  CA  . PHE   A 1 167 ? -4.485  -32.348 -30.021 1   35.84 ? 152 PHE   A CA  1 
ATOM   1247 C  C   . PHE   A 1 167 ? -3.499  -32.618 -31.156 1   35.44 ? 152 PHE   A C   1 
ATOM   1248 O  O   . PHE   A 1 167 ? -2.297  -32.833 -30.934 1   34.53 ? 152 PHE   A O   1 
ATOM   1249 C  CB  . PHE   A 1 167 ? -4.576  -30.833 -29.738 1   36.22 ? 152 PHE   A CB  1 
ATOM   1250 C  CG  . PHE   A 1 167 ? -5.479  -30.496 -28.573 1   38.01 ? 152 PHE   A CG  1 
ATOM   1251 C  CD1 . PHE   A 1 167 ? -6.856  -30.47  -28.725 1   39.57 ? 152 PHE   A CD1 1 
ATOM   1252 C  CD2 . PHE   A 1 167 ? -4.953  -30.235 -27.318 1   38.95 ? 152 PHE   A CD2 1 
ATOM   1253 C  CE1 . PHE   A 1 167 ? -7.691  -30.204 -27.636 1   40.73 ? 152 PHE   A CE1 1 
ATOM   1254 C  CE2 . PHE   A 1 167 ? -5.789  -29.974 -26.226 1   39.68 ? 152 PHE   A CE2 1 
ATOM   1255 C  CZ  . PHE   A 1 167 ? -7.153  -29.971 -26.392 1   40.17 ? 152 PHE   A CZ  1 
ATOM   1256 N  N   . SER   A 1 168 ? -4.042  -32.626 -32.386 1   34.66 ? 153 SER   A N   1 
ATOM   1257 C  CA  . SER   A 1 168 ? -3.343  -32.798 -33.656 1   35.34 ? 153 SER   A CA  1 
ATOM   1258 C  C   . SER   A 1 168 ? -3.742  -31.662 -34.608 1   34.57 ? 153 SER   A C   1 
ATOM   1259 O  O   . SER   A 1 168 ? -4.744  -31.011 -34.376 1   34.43 ? 153 SER   A O   1 
ATOM   1260 C  CB  . SER   A 1 168 ? -3.742  -34.125 -34.29  1   39.07 ? 153 SER   A CB  1 
ATOM   1261 O  OG  . SER   A 1 168 ? -3.117  -35.187 -33.599 1   44.83 ? 153 SER   A OG  1 
ATOM   1262 N  N   . PHE   A 1 169 ? -2.995  -31.454 -35.703 1   34.38 ? 154 PHE   A N   1 
ATOM   1263 C  CA  . PHE   A 1 169 ? -3.328  -30.394 -36.654 1   34.29 ? 154 PHE   A CA  1 
ATOM   1264 C  C   . PHE   A 1 169 ? -4.067  -30.898 -37.878 1   34.07 ? 154 PHE   A C   1 
ATOM   1265 O  O   . PHE   A 1 169 ? -5.04   -30.281 -38.28  1   34.55 ? 154 PHE   A O   1 
ATOM   1266 C  CB  . PHE   A 1 169 ? -2.084  -29.611 -37.071 1   33.96 ? 154 PHE   A CB  1 
ATOM   1267 C  CG  . PHE   A 1 169 ? -1.509  -28.823 -35.931 1   35.29 ? 154 PHE   A CG  1 
ATOM   1268 C  CD1 . PHE   A 1 169 ? -2.088  -27.629 -35.532 1   36.31 ? 154 PHE   A CD1 1 
ATOM   1269 C  CD2 . PHE   A 1 169 ? -0.389  -29.272 -35.254 1   36.02 ? 154 PHE   A CD2 1 
ATOM   1270 C  CE1 . PHE   A 1 169 ? -1.557  -26.902 -34.487 1   36.91 ? 154 PHE   A CE1 1 
ATOM   1271 C  CE2 . PHE   A 1 169 ? 0.142   -28.537 -34.208 1   37.3  ? 154 PHE   A CE2 1 
ATOM   1272 C  CZ  . PHE   A 1 169 ? -0.451  -27.363 -33.827 1   36.77 ? 154 PHE   A CZ  1 
ATOM   1273 N  N   . ARG   A 1 170 ? -3.57   -31.954 -38.512 1   33.84 ? 155 ARG   A N   1 
ATOM   1274 C  CA  . ARG   A 1 170 ? -4.161  -32.514 -39.727 1   34.43 ? 155 ARG   A CA  1 
ATOM   1275 C  C   . ARG   A 1 170 ? -4.155  -34.017 -39.641 1   35.66 ? 155 ARG   A C   1 
ATOM   1276 O  O   . ARG   A 1 170 ? -3.336  -34.597 -38.918 1   35.59 ? 155 ARG   A O   1 
ATOM   1277 C  CB  . ARG   A 1 170 ? -3.35   -32.127 -40.987 1   34.05 ? 155 ARG   A CB  1 
ATOM   1278 C  CG  . ARG   A 1 170 ? -3.179  -30.635 -41.215 1   34.63 ? 155 ARG   A CG  1 
ATOM   1279 C  CD  . ARG   A 1 170 ? -4.495  -29.935 -41.474 1   35.76 ? 155 ARG   A CD  1 
ATOM   1280 N  NE  . ARG   A 1 170 ? -5.159  -30.478 -42.655 1   37.46 ? 155 ARG   A NE  1 
ATOM   1281 C  CZ  . ARG   A 1 170 ? -5.02   -29.999 -43.889 1   40.67 ? 155 ARG   A CZ  1 
ATOM   1282 N  NH1 . ARG   A 1 170 ? -4.264  -28.931 -44.116 1   39.19 ? 155 ARG   A NH1 1 
ATOM   1283 N  NH2 . ARG   A 1 170 ? -5.665  -30.562 -44.9   1   41.47 ? 155 ARG   A NH2 1 
ATOM   1284 N  N   A ASP   A 1 171 ? -5.077  -34.679 -40.363 0.5 35.69 ? 156 ASP   A N   1 
ATOM   1285 N  N   B ASP   A 1 171 ? -5.044  -34.656 -40.412 0.5 35.61 ? 156 ASP   A N   1 
ATOM   1286 C  CA  A ASP   A 1 171 ? -5.088  -36.14  -40.359 0.5 36.15 ? 156 ASP   A CA  1 
ATOM   1287 C  CA  B ASP   A 1 171 ? -5.156  -36.105 -40.538 0.5 35.98 ? 156 ASP   A CA  1 
ATOM   1288 C  C   A ASP   A 1 171 ? -3.854  -36.648 -41.074 0.5 36.5  ? 156 ASP   A C   1 
ATOM   1289 C  C   B ASP   A 1 171 ? -3.825  -36.628 -41.106 0.5 36.4  ? 156 ASP   A C   1 
ATOM   1290 O  O   A ASP   A 1 171 ? -3.395  -36.044 -42.05  0.5 36.66 ? 156 ASP   A O   1 
ATOM   1291 O  O   B ASP   A 1 171 ? -3.302  -36.035 -42.056 0.5 36.5  ? 156 ASP   A O   1 
ATOM   1292 C  CB  A ASP   A 1 171 ? -6.385  -36.71  -40.908 0.5 37.04 ? 156 ASP   A CB  1 
ATOM   1293 C  CB  B ASP   A 1 171 ? -6.295  -36.398 -41.528 0.5 36.57 ? 156 ASP   A CB  1 
ATOM   1294 C  CG  A ASP   A 1 171 ? -7.513  -36.407 -39.956 0.5 40.39 ? 156 ASP   A CG  1 
ATOM   1295 C  CG  B ASP   A 1 171 ? -6.702  -37.846 -41.657 0.5 39.64 ? 156 ASP   A CG  1 
ATOM   1296 O  OD1 A ASP   A 1 171 ? -7.51   -36.962 -38.829 0.5 39.85 ? 156 ASP   A OD1 1 
ATOM   1297 O  OD1 B ASP   A 1 171 ? -6.569  -38.587 -40.666 0.5 39.74 ? 156 ASP   A OD1 1 
ATOM   1298 O  OD2 A ASP   A 1 171 ? -8.38   -35.604 -40.316 0.5 43.2  ? 156 ASP   A OD2 1 
ATOM   1299 O  OD2 B ASP   A 1 171 ? -7.183  -38.232 -42.746 0.5 41.57 ? 156 ASP   A OD2 1 
ATOM   1300 N  N   . GLY   A 1 172 ? -3.249  -37.659 -40.485 1   36.22 ? 157 GLY   A N   1 
ATOM   1301 C  CA  . GLY   A 1 172 ? -2.001  -38.226 -40.978 1   36.65 ? 157 GLY   A CA  1 
ATOM   1302 C  C   . GLY   A 1 172 ? -0.778  -37.346 -40.791 1   37.14 ? 157 GLY   A C   1 
ATOM   1303 O  O   . GLY   A 1 172 ? 0.234   -37.599 -41.424 1   37.68 ? 157 GLY   A O   1 
ATOM   1304 N  N   . ASP   A 1 173 ? -0.834  -36.299 -39.918 1   36.41 ? 158 ASP   A N   1 
ATOM   1305 C  CA  . ASP   A 1 173 ? 0.32    -35.417 -39.725 1   35.5  ? 158 ASP   A CA  1 
ATOM   1306 C  C   . ASP   A 1 173 ? 1.415   -36.009 -38.833 1   36.49 ? 158 ASP   A C   1 
ATOM   1307 O  O   . ASP   A 1 173 ? 2.436   -35.36  -38.656 1   36.73 ? 158 ASP   A O   1 
ATOM   1308 C  CB  . ASP   A 1 173 ? -0.096  -34.031 -39.201 1   34.16 ? 158 ASP   A CB  1 
ATOM   1309 C  CG  . ASP   A 1 173 ? -0.687  -34.032 -37.802 1   34.51 ? 158 ASP   A CG  1 
ATOM   1310 O  OD1 . ASP   A 1 173 ? -0.775  -35.122 -37.19  1   35.12 ? 158 ASP   A OD1 1 
ATOM   1311 O  OD2 . ASP   A 1 173 ? -1.11   -32.949 -37.332 1   33.79 ? 158 ASP   A OD2 1 
ATOM   1312 N  N   . CYS   A 1 174 ? 1.179   -37.19  -38.215 1   36.83 ? 159 CYS   A N   1 
ATOM   1313 C  CA  . CYS   A 1 174 ? 2.143   -37.844 -37.336 1   37.51 ? 159 CYS   A CA  1 
ATOM   1314 C  C   . CYS   A 1 174 ? 2.456   -37.028 -36.081 1   37.2  ? 159 CYS   A C   1 
ATOM   1315 O  O   . CYS   A 1 174 ? 3.53    -37.18  -35.511 1   37.1  ? 159 CYS   A O   1 
ATOM   1316 C  CB  . CYS   A 1 174 ? 3.419   -38.196 -38.095 1   39.51 ? 159 CYS   A CB  1 
ATOM   1317 S  SG  . CYS   A 1 174 ? 3.189   -39.416 -39.408 1   44.14 ? 159 CYS   A SG  1 
ATOM   1318 N  N   . SER   A 1 175 ? 1.531   -36.165 -35.648 1   36.62 ? 160 SER   A N   1 
ATOM   1319 C  CA  . SER   A 1 175 ? 1.737   -35.358 -34.462 1   35.54 ? 160 SER   A CA  1 
ATOM   1320 C  C   . SER   A 1 175 ? 1.775   -36.257 -33.239 1   34.28 ? 160 SER   A C   1 
ATOM   1321 O  O   . SER   A 1 175 ? 2.611   -36.03  -32.386 1   33.34 ? 160 SER   A O   1 
ATOM   1322 C  CB  . SER   A 1 175 ? 0.664   -34.281 -34.344 1   36.7  ? 160 SER   A CB  1 
ATOM   1323 O  OG  . SER   A 1 175 ? -0.625  -34.867 -34.377 1   37.76 ? 160 SER   A OG  1 
ATOM   1324 N  N   . LYS   A 1 176 ? 0.966   -37.342 -33.188 1   33.34 ? 161 LYS   A N   1 
ATOM   1325 C  CA  . LYS   A 1 176 ? 1.016   -38.269 -32.053 1   33.36 ? 161 LYS   A CA  1 
ATOM   1326 C  C   . LYS   A 1 176 ? 2.42    -38.877 -31.885 1   32.32 ? 161 LYS   A C   1 
ATOM   1327 O  O   . LYS   A 1 176 ? 2.998   -38.782 -30.802 1   32.28 ? 161 LYS   A O   1 
ATOM   1328 C  CB  . LYS   A 1 176 ? -0.057  -39.376 -32.152 1   35.57 ? 161 LYS   A CB  1 
ATOM   1329 C  CG  . LYS   A 1 176 ? 0.043   -40.39  -30.992 1   39.85 ? 161 LYS   A CG  1 
ATOM   1330 C  CD  . LYS   A 1 176 ? -0.956  -41.542 -31.103 1   43.68 ? 161 LYS   A CD  1 
ATOM   1331 C  CE  . LYS   A 1 176 ? -0.683  -42.622 -30.075 1   46.48 ? 161 LYS   A CE  1 
ATOM   1332 N  NZ  . LYS   A 1 176 ? -1.792  -43.621 -30.003 1   48.36 ? 161 LYS   A NZ  1 
ATOM   1333 N  N   . GLY   A 1 177 ? 2.948   -39.459 -32.957 1   31.22 ? 162 GLY   A N   1 
ATOM   1334 C  CA  . GLY   A 1 177 ? 4.268   -40.062 -32.946 1   31.45 ? 162 GLY   A CA  1 
ATOM   1335 C  C   . GLY   A 1 177 ? 5.375   -39.082 -32.592 1   31.72 ? 162 GLY   A C   1 
ATOM   1336 O  O   . GLY   A 1 177 ? 6.224   -39.392 -31.756 1   32.11 ? 162 GLY   A O   1 
ATOM   1337 N  N   . PHE   A 1 178 ? 5.381   -37.9   -33.229 1   30.86 ? 163 PHE   A N   1 
ATOM   1338 C  CA  . PHE   A 1 178 ? 6.417   -36.897 -33     1   31.18 ? 163 PHE   A CA  1 
ATOM   1339 C  C   . PHE   A 1 178 ? 6.376   -36.366 -31.572 1   31.62 ? 163 PHE   A C   1 
ATOM   1340 O  O   . PHE   A 1 178 ? 7.407   -36.344 -30.911 1   31.8  ? 163 PHE   A O   1 
ATOM   1341 C  CB  . PHE   A 1 178 ? 6.285   -35.731 -33.998 1   30.52 ? 163 PHE   A CB  1 
ATOM   1342 C  CG  . PHE   A 1 178 ? 7.374   -34.685 -33.914 1   31.27 ? 163 PHE   A CG  1 
ATOM   1343 C  CD1 . PHE   A 1 178 ? 8.699   -35.027 -34.1   1   31.77 ? 163 PHE   A CD1 1 
ATOM   1344 C  CD2 . PHE   A 1 178 ? 7.062   -33.35  -33.762 1   31.86 ? 163 PHE   A CD2 1 
ATOM   1345 C  CE1 . PHE   A 1 178 ? 9.692   -34.065 -34.082 1   31.88 ? 163 PHE   A CE1 1 
ATOM   1346 C  CE2 . PHE   A 1 178 ? 8.059   -32.381 -33.786 1   32.37 ? 163 PHE   A CE2 1 
ATOM   1347 C  CZ  . PHE   A 1 178 ? 9.371   -32.751 -33.905 1   31.94 ? 163 PHE   A CZ  1 
ATOM   1348 N  N   . PHE   A 1 179 ? 5.194   -35.939 -31.101 1   31.22 ? 164 PHE   A N   1 
ATOM   1349 C  CA  . PHE   A 1 179 ? 5.065   -35.379 -29.757 1   31.25 ? 164 PHE   A CA  1 
ATOM   1350 C  C   . PHE   A 1 179 ? 5.319   -36.404 -28.676 1   30.25 ? 164 PHE   A C   1 
ATOM   1351 O  O   . PHE   A 1 179 ? 6.024   -36.092 -27.714 1   28.91 ? 164 PHE   A O   1 
ATOM   1352 C  CB  . PHE   A 1 179 ? 3.699   -34.708 -29.539 1   31.61 ? 164 PHE   A CB  1 
ATOM   1353 C  CG  . PHE   A 1 179 ? 3.322   -33.575 -30.48  1   32.84 ? 164 PHE   A CG  1 
ATOM   1354 C  CD1 . PHE   A 1 179 ? 4.294   -32.872 -31.172 1   34.08 ? 164 PHE   A CD1 1 
ATOM   1355 C  CD2 . PHE   A 1 179 ? 1.99    -33.263 -30.718 1   34.15 ? 164 PHE   A CD2 1 
ATOM   1356 C  CE1 . PHE   A 1 179 ? 3.939   -31.868 -32.071 1   35.28 ? 164 PHE   A CE1 1 
ATOM   1357 C  CE2 . PHE   A 1 179 ? 1.641   -32.238 -31.587 1   35.13 ? 164 PHE   A CE2 1 
ATOM   1358 C  CZ  . PHE   A 1 179 ? 2.614   -31.55  -32.26  1   35.39 ? 164 PHE   A CZ  1 
ATOM   1359 N  N   . LEU   A 1 180 ? 4.742   -37.614 -28.813 1   29.73 ? 165 LEU   A N   1 
ATOM   1360 C  CA  . LEU   A 1 180 ? 4.905   -38.641 -27.793 1   31.11 ? 165 LEU   A CA  1 
ATOM   1361 C  C   . LEU   A 1 180 ? 6.297   -39.228 -27.714 1   30.88 ? 165 LEU   A C   1 
ATOM   1362 O  O   . LEU   A 1 180 ? 6.725   -39.562 -26.608 1   30.98 ? 165 LEU   A O   1 
ATOM   1363 C  CB  . LEU   A 1 180 ? 3.877   -39.783 -27.908 1   32.41 ? 165 LEU   A CB  1 
ATOM   1364 C  CG  . LEU   A 1 180 ? 2.422   -39.494 -27.593 1   35    ? 165 LEU   A CG  1 
ATOM   1365 C  CD1 . LEU   A 1 180 ? 1.61    -40.788 -27.623 1   35.68 ? 165 LEU   A CD1 1 
ATOM   1366 C  CD2 . LEU   A 1 180 ? 2.265   -38.841 -26.22  1   35.91 ? 165 LEU   A CD2 1 
ATOM   1367 N  N   . VAL   A 1 181 ? 7.003   -39.398 -28.856 1   29.83 ? 166 VAL   A N   1 
ATOM   1368 C  CA  . VAL   A 1 181 ? 8.371   -39.931 -28.787 1   29.4  ? 166 VAL   A CA  1 
ATOM   1369 C  C   . VAL   A 1 181 ? 9.298   -38.895 -28.148 1   28.77 ? 166 VAL   A C   1 
ATOM   1370 O  O   . VAL   A 1 181 ? 10.122  -39.253 -27.302 1   28.39 ? 166 VAL   A O   1 
ATOM   1371 C  CB  . VAL   A 1 181 ? 8.873   -40.49  -30.134 1   29.97 ? 166 VAL   A CB  1 
ATOM   1372 C  CG1 . VAL   A 1 181 ? 10.37   -40.795 -30.086 1   30.14 ? 166 VAL   A CG1 1 
ATOM   1373 C  CG2 . VAL   A 1 181 ? 8.07    -41.747 -30.506 1   30.66 ? 166 VAL   A CG2 1 
ATOM   1374 N  N   . SER   A 1 182 ? 9.071   -37.587 -28.425 1   27.8  ? 167 SER   A N   1 
ATOM   1375 C  CA  . SER   A 1 182 ? 9.811   -36.509 -27.77  1   28.52 ? 167 SER   A CA  1 
ATOM   1376 C  C   . SER   A 1 182 ? 9.549   -36.569 -26.255 1   29.67 ? 167 SER   A C   1 
ATOM   1377 O  O   . SER   A 1 182 ? 10.482  -36.492 -25.473 1   29.4  ? 167 SER   A O   1 
ATOM   1378 C  CB  . SER   A 1 182 ? 9.357   -35.155 -28.309 1   29.73 ? 167 SER   A CB  1 
ATOM   1379 O  OG  . SER   A 1 182 ? 9.893   -34.965 -29.606 1   32.73 ? 167 SER   A OG  1 
ATOM   1380 N  N   . LEU   A 1 183 ? 8.278   -36.744 -25.867 1   29.76 ? 168 LEU   A N   1 
ATOM   1381 C  CA  . LEU   A 1 183 ? 7.881   -36.813 -24.468 1   30.6  ? 168 LEU   A CA  1 
ATOM   1382 C  C   . LEU   A 1 183 ? 8.513   -38.021 -23.784 1   31.66 ? 168 LEU   A C   1 
ATOM   1383 O  O   . LEU   A 1 183 ? 9.009   -37.9   -22.664 1   31.99 ? 168 LEU   A O   1 
ATOM   1384 C  CB  . LEU   A 1 183 ? 6.354   -36.882 -24.354 1   30.34 ? 168 LEU   A CB  1 
ATOM   1385 C  CG  . LEU   A 1 183 ? 5.813   -37.046 -22.931 1   31.42 ? 168 LEU   A CG  1 
ATOM   1386 C  CD1 . LEU   A 1 183 ? 6.135   -35.829 -22.074 1   31.54 ? 168 LEU   A CD1 1 
ATOM   1387 C  CD2 . LEU   A 1 183 ? 4.33    -37.34  -22.936 1   31.61 ? 168 LEU   A CD2 1 
ATOM   1388 N  N   . LEU   A 1 184 ? 8.503   -39.184 -24.447 1   31.04 ? 169 LEU   A N   1 
ATOM   1389 C  CA  . LEU   A 1 184 ? 9.089   -40.391 -23.856 1   30.75 ? 169 LEU   A CA  1 
ATOM   1390 C  C   . LEU   A 1 184 ? 10.594  -40.244 -23.663 1   30.55 ? 169 LEU   A C   1 
ATOM   1391 O  O   . LEU   A 1 184 ? 11.095  -40.672 -22.637 1   31.32 ? 169 LEU   A O   1 
ATOM   1392 C  CB  . LEU   A 1 184 ? 8.735   -41.631 -24.703 1   30.88 ? 169 LEU   A CB  1 
ATOM   1393 C  CG  . LEU   A 1 184 ? 7.261   -42.053 -24.616 1   32.49 ? 169 LEU   A CG  1 
ATOM   1394 C  CD1 . LEU   A 1 184 ? 6.884   -43.031 -25.748 1   32.89 ? 169 LEU   A CD1 1 
ATOM   1395 C  CD2 . LEU   A 1 184 ? 6.925   -42.598 -23.229 1   32.35 ? 169 LEU   A CD2 1 
ATOM   1396 N  N   . VAL   A 1 185 ? 11.316  -39.637 -24.619 1   30.04 ? 170 VAL   A N   1 
ATOM   1397 C  CA  . VAL   A 1 185 ? 12.756  -39.382 -24.485 1   30.76 ? 170 VAL   A CA  1 
ATOM   1398 C  C   . VAL   A 1 185 ? 12.985  -38.398 -23.329 1   31.76 ? 170 VAL   A C   1 
ATOM   1399 O  O   . VAL   A 1 185 ? 13.834  -38.634 -22.471 1   32.61 ? 170 VAL   A O   1 
ATOM   1400 C  CB  . VAL   A 1 185 ? 13.403  -38.877 -25.805 1   29.88 ? 170 VAL   A CB  1 
ATOM   1401 C  CG1 . VAL   A 1 185 ? 14.822  -38.355 -25.565 1   30.72 ? 170 VAL   A CG1 1 
ATOM   1402 C  CG2 . VAL   A 1 185 ? 13.409  -39.968 -26.847 1   29.48 ? 170 VAL   A CG2 1 
ATOM   1403 N  N   . GLU   A 1 186 ? 12.178  -37.321 -23.292 1   31.72 ? 171 GLU   A N   1 
ATOM   1404 C  CA  . GLU   A 1 186 ? 12.206  -36.275 -22.264 1   31.87 ? 171 GLU   A CA  1 
ATOM   1405 C  C   . GLU   A 1 186 ? 12.034  -36.893 -20.86  1   33.13 ? 171 GLU   A C   1 
ATOM   1406 O  O   . GLU   A 1 186 ? 12.81   -36.577 -19.951 1   33.83 ? 171 GLU   A O   1 
ATOM   1407 C  CB  . GLU   A 1 186 ? 11.086  -35.264 -22.555 1   32.07 ? 171 GLU   A CB  1 
ATOM   1408 C  CG  . GLU   A 1 186 ? 10.873  -34.198 -21.5   1   32.44 ? 171 GLU   A CG  1 
ATOM   1409 C  CD  . GLU   A 1 186 ? 11.779  -32.994 -21.576 1   31.66 ? 171 GLU   A CD  1 
ATOM   1410 O  OE1 . GLU   A 1 186 ? 12.239  -32.666 -22.692 1   30.82 ? 171 GLU   A OE1 1 
ATOM   1411 O  OE2 . GLU   A 1 186 ? 12.036  -32.374 -20.519 1   32.96 ? 171 GLU   A OE2 1 
ATOM   1412 N  N   . ILE   A 1 187 ? 11.09   -37.829 -20.71  1   33    ? 172 ILE   A N   1 
ATOM   1413 C  CA  . ILE   A 1 187 ? 10.839  -38.544 -19.462 1   32.93 ? 172 ILE   A CA  1 
ATOM   1414 C  C   . ILE   A 1 187 ? 11.996  -39.52  -19.1   1   33.27 ? 172 ILE   A C   1 
ATOM   1415 O  O   . ILE   A 1 187 ? 12.365  -39.607 -17.929 1   33.63 ? 172 ILE   A O   1 
ATOM   1416 C  CB  . ILE   A 1 187 ? 9.465   -39.261 -19.5   1   32.91 ? 172 ILE   A CB  1 
ATOM   1417 C  CG1 . ILE   A 1 187 ? 8.301   -38.241 -19.504 1   33.23 ? 172 ILE   A CG1 1 
ATOM   1418 C  CG2 . ILE   A 1 187 ? 9.319   -40.259 -18.325 1   33.57 ? 172 ILE   A CG2 1 
ATOM   1419 C  CD1 . ILE   A 1 187 ? 6.95    -38.887 -19.784 1   34.54 ? 172 ILE   A CD1 1 
ATOM   1420 N  N   . ALA   A 1 188 ? 12.546  -40.245 -20.08  1   32.2  ? 173 ALA   A N   1 
ATOM   1421 C  CA  . ALA   A 1 188 ? 13.656  -41.158 -19.829 1   33.08 ? 173 ALA   A CA  1 
ATOM   1422 C  C   . ALA   A 1 188 ? 14.888  -40.383 -19.352 1   34.83 ? 173 ALA   A C   1 
ATOM   1423 O  O   . ALA   A 1 188 ? 15.532  -40.801 -18.396 1   35.59 ? 173 ALA   A O   1 
ATOM   1424 C  CB  . ALA   A 1 188 ? 13.98   -41.951 -21.076 1   32.21 ? 173 ALA   A CB  1 
ATOM   1425 N  N   . ALA   A 1 189 ? 15.192  -39.235 -19.981 1   35.74 ? 174 ALA   A N   1 
ATOM   1426 C  CA  . ALA   A 1 189 ? 16.321  -38.396 -19.557 1   36.29 ? 174 ALA   A CA  1 
ATOM   1427 C  C   . ALA   A 1 189 ? 16.118  -37.801 -18.164 1   36.86 ? 174 ALA   A C   1 
ATOM   1428 O  O   . ALA   A 1 189 ? 17.086  -37.611 -17.413 1   37.19 ? 174 ALA   A O   1 
ATOM   1429 C  CB  . ALA   A 1 189 ? 16.575  -37.287 -20.577 1   36.45 ? 174 ALA   A CB  1 
ATOM   1430 N  N   . ALA   A 1 190 ? 14.866  -37.517 -17.809 1   37.28 ? 175 ALA   A N   1 
ATOM   1431 C  CA  . ALA   A 1 190 ? 14.514  -36.934 -16.516 1   37.85 ? 175 ALA   A CA  1 
ATOM   1432 C  C   . ALA   A 1 190 ? 14.811  -37.819 -15.323 1   37.33 ? 175 ALA   A C   1 
ATOM   1433 O  O   . ALA   A 1 190 ? 14.896  -37.297 -14.218 1   37.44 ? 175 ALA   A O   1 
ATOM   1434 C  CB  . ALA   A 1 190 ? 13.052  -36.552 -16.493 1   38.55 ? 175 ALA   A CB  1 
ATOM   1435 N  N   . SER   A 1 191 ? 14.947  -39.135 -15.516 1   36.83 ? 176 SER   A N   1 
ATOM   1436 C  CA  . SER   A 1 191 ? 15.283  -40.017 -14.391 1   37.18 ? 176 SER   A CA  1 
ATOM   1437 C  C   . SER   A 1 191 ? 16.707  -39.709 -13.82  1   36.23 ? 176 SER   A C   1 
ATOM   1438 O  O   . SER   A 1 191 ? 16.983  -40.002 -12.65  1   36.06 ? 176 SER   A O   1 
ATOM   1439 C  CB  . SER   A 1 191 ? 15.123  -41.478 -14.773 1   38.44 ? 176 SER   A CB  1 
ATOM   1440 O  OG  . SER   A 1 191 ? 16.127  -41.774 -15.717 1   42.74 ? 176 SER   A OG  1 
ATOM   1441 N  N   . ALA   A 1 192 ? 17.569  -39.036 -14.618 1   34.28 ? 177 ALA   A N   1 
ATOM   1442 C  CA  . ALA   A 1 192 ? 18.873  -38.595 -14.153 1   34.22 ? 177 ALA   A CA  1 
ATOM   1443 C  C   . ALA   A 1 192 ? 18.809  -37.309 -13.294 1   33.64 ? 177 ALA   A C   1 
ATOM   1444 O  O   . ALA   A 1 192 ? 19.771  -36.987 -12.617 1   32.71 ? 177 ALA   A O   1 
ATOM   1445 C  CB  . ALA   A 1 192 ? 19.809  -38.39  -15.333 1   34.57 ? 177 ALA   A CB  1 
ATOM   1446 N  N   . ILE   A 1 193 ? 17.677  -36.574 -13.305 1   33.88 ? 178 ILE   A N   1 
ATOM   1447 C  CA  . ILE   A 1 193 ? 17.552  -35.329 -12.538 1   34.34 ? 178 ILE   A CA  1 
ATOM   1448 C  C   . ILE   A 1 193 ? 17.67   -35.543 -11.054 1   35.14 ? 178 ILE   A C   1 
ATOM   1449 O  O   . ILE   A 1 193 ? 18.323  -34.734 -10.383 1   35.95 ? 178 ILE   A O   1 
ATOM   1450 C  CB  . ILE   A 1 193 ? 16.241  -34.553 -12.901 1   35.34 ? 178 ILE   A CB  1 
ATOM   1451 C  CG1 . ILE   A 1 193 ? 16.252  -34.101 -14.376 1   36.4  ? 178 ILE   A CG1 1 
ATOM   1452 C  CG2 . ILE   A 1 193 ? 16.022  -33.356 -11.973 1   34.95 ? 178 ILE   A CG2 1 
ATOM   1453 C  CD1 . ILE   A 1 193 ? 14.845  -33.632 -14.82  1   39.07 ? 178 ILE   A CD1 1 
ATOM   1454 N  N   . LYS   A 1 194 ? 17.06   -36.626 -10.521 1   35.45 ? 179 LYS   A N   1 
ATOM   1455 C  CA  . LYS   A 1 194 ? 17.137  -36.913 -9.086  1   36.89 ? 179 LYS   A CA  1 
ATOM   1456 C  C   . LYS   A 1 194 ? 18.576  -37.138 -8.602  1   37.01 ? 179 LYS   A C   1 
ATOM   1457 O  O   . LYS   A 1 194 ? 18.848  -37.002 -7.417  1   37.94 ? 179 LYS   A O   1 
ATOM   1458 C  CB  . LYS   A 1 194 ? 16.223  -38.096 -8.697  1   40.24 ? 179 LYS   A CB  1 
ATOM   1459 C  CG  . LYS   A 1 194 ? 16.683  -39.434 -9.268  1   45.67 ? 179 LYS   A CG  1 
ATOM   1460 C  CD  . LYS   A 1 194 ? 15.601  -40.493 -9.123  1   51.05 ? 179 LYS   A CD  1 
ATOM   1461 C  CE  . LYS   A 1 194 ? 16.078  -41.852 -9.585  1   55.24 ? 179 LYS   A CE  1 
ATOM   1462 N  NZ  . LYS   A 1 194 ? 15.784  -42.11  -11.023 1   57.37 ? 179 LYS   A NZ  1 
ATOM   1463 N  N   . VAL   A 1 195 ? 19.514  -37.409 -9.528  1   36.06 ? 180 VAL   A N   1 
ATOM   1464 C  CA  . VAL   A 1 195 ? 20.923  -37.607 -9.204  1   34.73 ? 180 VAL   A CA  1 
ATOM   1465 C  C   . VAL   A 1 195 ? 21.68   -36.264 -9.056  1   34.81 ? 180 VAL   A C   1 
ATOM   1466 O  O   . VAL   A 1 195 ? 22.729  -36.205 -8.407  1   34.7  ? 180 VAL   A O   1 
ATOM   1467 C  CB  . VAL   A 1 195 ? 21.594  -38.573 -10.208 1   34.7  ? 180 VAL   A CB  1 
ATOM   1468 C  CG1 . VAL   A 1 195 ? 22.972  -38.983 -9.719  1   35.18 ? 180 VAL   A CG1 1 
ATOM   1469 C  CG2 . VAL   A 1 195 ? 20.733  -39.826 -10.428 1   34.98 ? 180 VAL   A CG2 1 
ATOM   1470 N  N   . ILE   A 1 196 ? 21.134  -35.173 -9.611  1   34.66 ? 181 ILE   A N   1 
ATOM   1471 C  CA  . ILE   A 1 196 ? 21.782  -33.86  -9.546  1   35.1  ? 181 ILE   A CA  1 
ATOM   1472 C  C   . ILE   A 1 196 ? 22.121  -33.429 -8.108  1   35.85 ? 181 ILE   A C   1 
ATOM   1473 O  O   . ILE   A 1 196 ? 23.28   -33.093 -7.881  1   35.74 ? 181 ILE   A O   1 
ATOM   1474 C  CB  . ILE   A 1 196 ? 20.986  -32.783 -10.329 1   34.67 ? 181 ILE   A CB  1 
ATOM   1475 C  CG1 . ILE   A 1 196 ? 20.989  -33.134 -11.831 1   35.09 ? 181 ILE   A CG1 1 
ATOM   1476 C  CG2 . ILE   A 1 196 ? 21.572  -31.39  -10.114 1   34.89 ? 181 ILE   A CG2 1 
ATOM   1477 C  CD1 . ILE   A 1 196 ? 20.171  -32.164 -12.721 1   35.98 ? 181 ILE   A CD1 1 
ATOM   1478 N  N   . PRO   A 1 197 ? 21.208  -33.513 -7.11   1   36.14 ? 182 PRO   A N   1 
ATOM   1479 C  CA  . PRO   A 1 197 ? 21.598  -33.108 -5.743  1   36.33 ? 182 PRO   A CA  1 
ATOM   1480 C  C   . PRO   A 1 197 ? 22.733  -33.971 -5.186  1   36.1  ? 182 PRO   A C   1 
ATOM   1481 O  O   . PRO   A 1 197 ? 23.565  -33.473 -4.452  1   35.13 ? 182 PRO   A O   1 
ATOM   1482 C  CB  . PRO   A 1 197 ? 20.309  -33.303 -4.921  1   37.42 ? 182 PRO   A CB  1 
ATOM   1483 C  CG  . PRO   A 1 197 ? 19.215  -33.464 -5.906  1   37.34 ? 182 PRO   A CG  1 
ATOM   1484 C  CD  . PRO   A 1 197 ? 19.788  -33.927 -7.179  1   35.59 ? 182 PRO   A CD  1 
ATOM   1485 N  N   . THR   A 1 198 ? 22.748  -35.27  -5.531  1   36.5  ? 183 THR   A N   1 
ATOM   1486 C  CA  . THR   A 1 198 ? 23.8    -36.203 -5.113  1   37    ? 183 THR   A CA  1 
ATOM   1487 C  C   . THR   A 1 198 ? 25.16   -35.751 -5.638  1   36.41 ? 183 THR   A C   1 
ATOM   1488 O  O   . THR   A 1 198 ? 26.132  -35.757 -4.885  1   36.47 ? 183 THR   A O   1 
ATOM   1489 C  CB  . THR   A 1 198 ? 23.452  -37.622 -5.566  1   38.88 ? 183 THR   A CB  1 
ATOM   1490 O  OG1 . THR   A 1 198 ? 22.177  -37.948 -5.035  1   40.58 ? 183 THR   A OG1 1 
ATOM   1491 C  CG2 . THR   A 1 198 ? 24.471  -38.66  -5.085  1   39.5  ? 183 THR   A CG2 1 
ATOM   1492 N  N   . VAL   A 1 199 ? 25.222  -35.314 -6.91   1   35.55 ? 184 VAL   A N   1 
ATOM   1493 C  CA  . VAL   A 1 199 ? 26.437  -34.791 -7.533  1   34.69 ? 184 VAL   A CA  1 
ATOM   1494 C  C   . VAL   A 1 199 ? 26.959  -33.548 -6.788  1   34.95 ? 184 VAL   A C   1 
ATOM   1495 O  O   . VAL   A 1 199 ? 28.15   -33.472 -6.475  1   34.13 ? 184 VAL   A O   1 
ATOM   1496 C  CB  . VAL   A 1 199 ? 26.196  -34.481 -9.038  1   34.79 ? 184 VAL   A CB  1 
ATOM   1497 C  CG1 . VAL   A 1 199 ? 27.353  -33.686 -9.637  1   35.06 ? 184 VAL   A CG1 1 
ATOM   1498 C  CG2 . VAL   A 1 199 ? 25.949  -35.766 -9.824  1   35.51 ? 184 VAL   A CG2 1 
ATOM   1499 N  N   . PHE   A 1 200 ? 26.086  -32.562 -6.526  1   35.36 ? 185 PHE   A N   1 
ATOM   1500 C  CA  . PHE   A 1 200 ? 26.508  -31.342 -5.832  1   36.49 ? 185 PHE   A CA  1 
ATOM   1501 C  C   . PHE   A 1 200 ? 26.88   -31.586 -4.366  1   37.16 ? 185 PHE   A C   1 
ATOM   1502 O  O   . PHE   A 1 200 ? 27.807  -30.954 -3.881  1   38.22 ? 185 PHE   A O   1 
ATOM   1503 C  CB  . PHE   A 1 200 ? 25.437  -30.232 -5.959  1   36.82 ? 185 PHE   A CB  1 
ATOM   1504 C  CG  . PHE   A 1 200 ? 25.398  -29.671 -7.361  1   37.37 ? 185 PHE   A CG  1 
ATOM   1505 C  CD1 . PHE   A 1 200 ? 26.535  -29.161 -7.945  1   37.86 ? 185 PHE   A CD1 1 
ATOM   1506 C  CD2 . PHE   A 1 200 ? 24.224  -29.649 -8.084  1   38.69 ? 185 PHE   A CD2 1 
ATOM   1507 C  CE1 . PHE   A 1 200 ? 26.524  -28.691 -9.243  1   38.78 ? 185 PHE   A CE1 1 
ATOM   1508 C  CE2 . PHE   A 1 200 ? 24.201  -29.115 -9.366  1   39.45 ? 185 PHE   A CE2 1 
ATOM   1509 C  CZ  . PHE   A 1 200 ? 25.357  -28.648 -9.939  1   39.17 ? 185 PHE   A CZ  1 
ATOM   1510 N  N   . LYS   A 1 201 ? 26.164  -32.462 -3.67   1   37.44 ? 186 LYS   A N   1 
ATOM   1511 C  CA  . LYS   A 1 201 ? 26.482  -32.777 -2.269  1   38.63 ? 186 LYS   A CA  1 
ATOM   1512 C  C   . LYS   A 1 201 ? 27.832  -33.511 -2.226  1   38.36 ? 186 LYS   A C   1 
ATOM   1513 O  O   . LYS   A 1 201 ? 28.68   -33.17  -1.398  1   38    ? 186 LYS   A O   1 
ATOM   1514 C  CB  . LYS   A 1 201 ? 25.397  -33.661 -1.618  1   41.08 ? 186 LYS   A CB  1 
ATOM   1515 C  CG  . LYS   A 1 201 ? 24.163  -32.925 -1.123  1   47.73 ? 186 LYS   A CG  1 
ATOM   1516 C  CD  . LYS   A 1 201 ? 23.145  -33.904 -0.472  1   53.95 ? 186 LYS   A CD  1 
ATOM   1517 C  CE  . LYS   A 1 201 ? 22.302  -34.628 -1.501  1   58.42 ? 186 LYS   A CE  1 
ATOM   1518 N  NZ  . LYS   A 1 201 ? 21.773  -35.924 -1.003  1   61.29 ? 186 LYS   A NZ  1 
ATOM   1519 N  N   . ALA   A 1 202 ? 28.051  -34.476 -3.149  1   37.99 ? 187 ALA   A N   1 
ATOM   1520 C  CA  . ALA   A 1 202 ? 29.31   -35.227 -3.207  1   38.45 ? 187 ALA   A CA  1 
ATOM   1521 C  C   . ALA   A 1 202 ? 30.483  -34.328 -3.447  1   39.47 ? 187 ALA   A C   1 
ATOM   1522 O  O   . ALA   A 1 202 ? 31.532  -34.545 -2.84   1   40.13 ? 187 ALA   A O   1 
ATOM   1523 C  CB  . ALA   A 1 202 ? 29.258  -36.329 -4.245  1   38.1  ? 187 ALA   A CB  1 
ATOM   1524 N  N   A MET   A 1 203 ? 30.324  -33.3   -4.291  0.5 39.31 ? 188 MET   A N   1 
ATOM   1525 N  N   B MET   A 1 203 ? 30.311  -33.265 -4.26   0.5 39.25 ? 188 MET   A N   1 
ATOM   1526 C  CA  A MET   A 1 203 ? 31.415  -32.369 -4.542  0.5 39.69 ? 188 MET   A CA  1 
ATOM   1527 C  CA  B MET   A 1 203 ? 31.377  -32.3   -4.523  0.5 39.58 ? 188 MET   A CA  1 
ATOM   1528 C  C   A MET   A 1 203 ? 31.73   -31.551 -3.289  0.5 41.34 ? 188 MET   A C   1 
ATOM   1529 C  C   B MET   A 1 203 ? 31.705  -31.435 -3.292  0.5 41.32 ? 188 MET   A C   1 
ATOM   1530 O  O   A MET   A 1 203 ? 32.887  -31.494 -2.878  0.5 41.83 ? 188 MET   A O   1 
ATOM   1531 O  O   B MET   A 1 203 ? 32.882  -31.219 -3.002  0.5 41.86 ? 188 MET   A O   1 
ATOM   1532 C  CB  A MET   A 1 203 ? 31.097  -31.45  -5.723  0.5 39.05 ? 188 MET   A CB  1 
ATOM   1533 C  CB  B MET   A 1 203 ? 31.027  -31.384 -5.708  0.5 38.75 ? 188 MET   A CB  1 
ATOM   1534 C  CG  A MET   A 1 203 ? 31.167  -32.144 -7.054  0.5 39.57 ? 188 MET   A CG  1 
ATOM   1535 C  CG  B MET   A 1 203 ? 31.308  -31.989 -7.081  0.5 38.92 ? 188 MET   A CG  1 
ATOM   1536 S  SD  A MET   A 1 203 ? 30.081  -31.324 -8.243  0.5 39.68 ? 188 MET   A SD  1 
ATOM   1537 S  SD  B MET   A 1 203 ? 31.344  -30.753 -8.432  0.5 38.21 ? 188 MET   A SD  1 
ATOM   1538 C  CE  A MET   A 1 203 ? 30.936  -29.778 -8.447  0.5 34.65 ? 188 MET   A CE  1 
ATOM   1539 C  CE  B MET   A 1 203 ? 29.83   -29.932 -8.174  0.5 33.8  ? 188 MET   A CE  1 
ATOM   1540 N  N   A GLN   A 1 204 ? 30.711  -30.955 -2.659  0.5 42.07 ? 189 GLN   A N   1 
ATOM   1541 N  N   B GLN   A 1 204 ? 30.683  -30.908 -2.592  0.5 42.06 ? 189 GLN   A N   1 
ATOM   1542 C  CA  A GLN   A 1 204 ? 30.923  -30.134 -1.47   0.5 43.34 ? 189 GLN   A CA  1 
ATOM   1543 C  CA  B GLN   A 1 204 ? 30.93   -30.035 -1.439  0.5 43.34 ? 189 GLN   A CA  1 
ATOM   1544 C  C   A GLN   A 1 204 ? 31.531  -30.961 -0.326  0.5 44.19 ? 189 GLN   A C   1 
ATOM   1545 C  C   B GLN   A 1 204 ? 31.549  -30.801 -0.267  0.5 44.3  ? 189 GLN   A C   1 
ATOM   1546 O  O   A GLN   A 1 204 ? 32.527  -30.557 0.273   0.5 44.66 ? 189 GLN   A O   1 
ATOM   1547 O  O   B GLN   A 1 204 ? 32.468  -30.302 0.38    0.5 44.81 ? 189 GLN   A O   1 
ATOM   1548 C  CB  A GLN   A 1 204 ? 29.61   -29.449 -1.051  0.5 45.28 ? 189 GLN   A CB  1 
ATOM   1549 C  CB  B GLN   A 1 204 ? 29.655  -29.281 -1.014  0.5 45.21 ? 189 GLN   A CB  1 
ATOM   1550 C  CG  A GLN   A 1 204 ? 29.805  -28.313 -0.058  0.5 49.29 ? 189 GLN   A CG  1 
ATOM   1551 C  CG  B GLN   A 1 204 ? 29.924  -28.073 -0.108  0.5 49.01 ? 189 GLN   A CG  1 
ATOM   1552 C  CD  A GLN   A 1 204 ? 29.653  -28.817 1.348   0.5 54.31 ? 189 GLN   A CD  1 
ATOM   1553 C  CD  B GLN   A 1 204 ? 30.231  -26.804 -0.87   0.5 54.16 ? 189 GLN   A CD  1 
ATOM   1554 O  OE1 A GLN   A 1 204 ? 28.787  -29.652 1.637   0.5 56.24 ? 189 GLN   A OE1 1 
ATOM   1555 O  OE1 B GLN   A 1 204 ? 30.917  -26.807 -1.9    0.5 56.72 ? 189 GLN   A OE1 1 
ATOM   1556 N  NE2 A GLN   A 1 204 ? 30.508  -28.342 2.247   0.5 55.2  ? 189 GLN   A NE2 1 
ATOM   1557 N  NE2 B GLN   A 1 204 ? 29.736  -25.679 -0.375  0.5 54.46 ? 189 GLN   A NE2 1 
ATOM   1558 N  N   A MET   A 1 205 ? 30.984  -32.151 -0.084  0.5 44.07 ? 190 MET   A N   1 
ATOM   1559 N  N   B MET   A 1 205 ? 31.09   -32.031 -0.038  0.5 44.22 ? 190 MET   A N   1 
ATOM   1560 C  CA  A MET   A 1 205 ? 31.473  -33.037 0.963   0.5 44.51 ? 190 MET   A CA  1 
ATOM   1561 C  CA  B MET   A 1 205 ? 31.604  -32.882 1.03    0.5 44.73 ? 190 MET   A CA  1 
ATOM   1562 C  C   A MET   A 1 205 ? 32.682  -33.88  0.563   0.5 44.81 ? 190 MET   A C   1 
ATOM   1563 C  C   B MET   A 1 205 ? 32.917  -33.595 0.684   0.5 44.93 ? 190 MET   A C   1 
ATOM   1564 O  O   A MET   A 1 205 ? 33.012  -34.821 1.285   0.5 44.86 ? 190 MET   A O   1 
ATOM   1565 O  O   B MET   A 1 205 ? 33.529  -34.188 1.571   0.5 45.17 ? 190 MET   A O   1 
ATOM   1566 C  CB  A MET   A 1 205 ? 30.337  -33.931 1.492   0.5 45.14 ? 190 MET   A CB  1 
ATOM   1567 C  CB  B MET   A 1 205 ? 30.545  -33.924 1.418   0.5 45.57 ? 190 MET   A CB  1 
ATOM   1568 C  CG  A MET   A 1 205 ? 29.156  -33.141 2.023   0.5 47.75 ? 190 MET   A CG  1 
ATOM   1569 C  CG  B MET   A 1 205 ? 29.278  -33.308 1.937   0.5 48.46 ? 190 MET   A CG  1 
ATOM   1570 S  SD  A MET   A 1 205 ? 29.573  -31.948 3.326   0.5 53.44 ? 190 MET   A SD  1 
ATOM   1571 S  SD  B MET   A 1 205 ? 28.059  -34.556 2.382   0.5 55.39 ? 190 MET   A SD  1 
ATOM   1572 C  CE  A MET   A 1 205 ? 29.414  -32.974 4.753   0.5 50.89 ? 190 MET   A CE  1 
ATOM   1573 C  CE  B MET   A 1 205 ? 28.834  -35.237 3.882   0.5 54.05 ? 190 MET   A CE  1 
ATOM   1574 N  N   . GLN   A 1 206 ? 33.322  -33.577 -0.596  1   44.67 ? 191 GLN   A N   1 
ATOM   1575 C  CA  . GLN   A 1 206 ? 34.514  -34.257 -1.115  1   44.04 ? 191 GLN   A CA  1 
ATOM   1576 C  C   . GLN   A 1 206 ? 34.388  -35.767 -1.047  1   43.29 ? 191 GLN   A C   1 
ATOM   1577 O  O   . GLN   A 1 206 ? 35.3    -36.44  -0.583  1   43.92 ? 191 GLN   A O   1 
ATOM   1578 C  CB  . GLN   A 1 206 ? 35.815  -33.752 -0.442  1   45.31 ? 191 GLN   A CB  1 
ATOM   1579 C  CG  . GLN   A 1 206 ? 36.176  -32.3   -0.77   1   49.55 ? 191 GLN   A CG  1 
ATOM   1580 C  CD  . GLN   A 1 206 ? 36.893  -32.169 -2.102  1   56.08 ? 191 GLN   A CD  1 
ATOM   1581 O  OE1 . GLN   A 1 206 ? 37.582  -33.093 -2.576  1   59.23 ? 191 GLN   A OE1 1 
ATOM   1582 N  NE2 . GLN   A 1 206 ? 36.779  -31.005 -2.732  1   56.48 ? 191 GLN   A NE2 1 
ATOM   1583 N  N   . GLU   A 1 207 ? 33.237  -36.292 -1.456  1   41.57 ? 192 GLU   A N   1 
ATOM   1584 C  CA  . GLU   A 1 207 ? 32.947  -37.718 -1.459  1   40.56 ? 192 GLU   A CA  1 
ATOM   1585 C  C   . GLU   A 1 207 ? 33.211  -38.272 -2.845  1   39.74 ? 192 GLU   A C   1 
ATOM   1586 O  O   . GLU   A 1 207 ? 32.294  -38.404 -3.67   1   39.79 ? 192 GLU   A O   1 
ATOM   1587 C  CB  . GLU   A 1 207 ? 31.488  -37.973 -1.031  1   43.16 ? 192 GLU   A CB  1 
ATOM   1588 C  CG  . GLU   A 1 207 ? 31.194  -37.588 0.41    1   50.5  ? 192 GLU   A CG  1 
ATOM   1589 C  CD  . GLU   A 1 207 ? 31.731  -38.562 1.443   1   61.41 ? 192 GLU   A CD  1 
ATOM   1590 O  OE1 . GLU   A 1 207 ? 31.85   -39.767 1.117   1   63.3  ? 192 GLU   A OE1 1 
ATOM   1591 O  OE2 . GLU   A 1 207 ? 32.032  -38.122 2.578   1   65.64 ? 192 GLU   A OE2 1 
ATOM   1592 N  N   . ARG   A 1 208 ? 34.478  -38.595 -3.109  1   38.47 ? 193 ARG   A N   1 
ATOM   1593 C  CA  . ARG   A 1 208 ? 34.911  -39.099 -4.408  1   37    ? 193 ARG   A CA  1 
ATOM   1594 C  C   . ARG   A 1 208 ? 34.121  -40.319 -4.924  1   35.56 ? 193 ARG   A C   1 
ATOM   1595 O  O   . ARG   A 1 208 ? 33.684  -40.297 -6.073  1   35.24 ? 193 ARG   A O   1 
ATOM   1596 C  CB  . ARG   A 1 208 ? 36.415  -39.385 -4.395  1   37.1  ? 193 ARG   A CB  1 
ATOM   1597 C  CG  . ARG   A 1 208 ? 36.972  -39.774 -5.74   1   37.08 ? 193 ARG   A CG  1 
ATOM   1598 C  CD  . ARG   A 1 208 ? 37.067  -41.265 -5.865  1   37.77 ? 193 ARG   A CD  1 
ATOM   1599 N  NE  . ARG   A 1 208 ? 37.746  -41.657 -7.091  1   36.44 ? 193 ARG   A NE  1 
ATOM   1600 C  CZ  . ARG   A 1 208 ? 37.74   -42.891 -7.583  1   36.79 ? 193 ARG   A CZ  1 
ATOM   1601 N  NH1 . ARG   A 1 208 ? 37.086  -43.857 -6.958  1   35.78 ? 193 ARG   A NH1 1 
ATOM   1602 N  NH2 . ARG   A 1 208 ? 38.391  -43.168 -8.707  1   34.99 ? 193 ARG   A NH2 1 
ATOM   1603 N  N   . ASP   A 1 209 ? 33.957  -41.369 -4.113  1   34.4  ? 194 ASP   A N   1 
ATOM   1604 C  CA  . ASP   A 1 209 ? 33.254  -42.553 -4.581  1   34.72 ? 194 ASP   A CA  1 
ATOM   1605 C  C   . ASP   A 1 209 ? 31.777  -42.272 -4.836  1   35.3  ? 194 ASP   A C   1 
ATOM   1606 O  O   . ASP   A 1 209 ? 31.234  -42.797 -5.797  1   35.51 ? 194 ASP   A O   1 
ATOM   1607 C  CB  . ASP   A 1 209 ? 33.435  -43.755 -3.648  1   36.28 ? 194 ASP   A CB  1 
ATOM   1608 C  CG  . ASP   A 1 209 ? 34.889  -44.118 -3.361  1   39.48 ? 194 ASP   A CG  1 
ATOM   1609 O  OD1 . ASP   A 1 209 ? 35.719  -44.017 -4.28   1   40.79 ? 194 ASP   A OD1 1 
ATOM   1610 O  OD2 . ASP   A 1 209 ? 35.185  -44.496 -2.223  1   40.23 ? 194 ASP   A OD2 1 
ATOM   1611 N  N   . THR   A 1 210 ? 31.143  -41.416 -4.017  1   35.74 ? 195 THR   A N   1 
ATOM   1612 C  CA  . THR   A 1 210 ? 29.733  -41.067 -4.223  1   36.55 ? 195 THR   A CA  1 
ATOM   1613 C  C   . THR   A 1 210 ? 29.578  -40.314 -5.536  1   35.61 ? 195 THR   A C   1 
ATOM   1614 O  O   . THR   A 1 210 ? 28.648  -40.608 -6.281  1   36.77 ? 195 THR   A O   1 
ATOM   1615 C  CB  . THR   A 1 210 ? 29.205  -40.212 -3.056  1   38.86 ? 195 THR   A CB  1 
ATOM   1616 O  OG1 . THR   A 1 210 ? 29.415  -40.934 -1.85   1   40.26 ? 195 THR   A OG1 1 
ATOM   1617 C  CG2 . THR   A 1 210 ? 27.682  -39.877 -3.2    1   39.32 ? 195 THR   A CG2 1 
ATOM   1618 N  N   . LEU   A 1 211 ? 30.483  -39.366 -5.821  1   34.39 ? 196 LEU   A N   1 
ATOM   1619 C  CA  . LEU   A 1 211 ? 30.447  -38.587 -7.054  1   34.31 ? 196 LEU   A CA  1 
ATOM   1620 C  C   . LEU   A 1 211 ? 30.603  -39.478 -8.28   1   35.39 ? 196 LEU   A C   1 
ATOM   1621 O  O   . LEU   A 1 211 ? 29.833  -39.367 -9.239  1   35.85 ? 196 LEU   A O   1 
ATOM   1622 C  CB  . LEU   A 1 211 ? 31.528  -37.503 -7.047  1   34.18 ? 196 LEU   A CB  1 
ATOM   1623 C  CG  . LEU   A 1 211 ? 31.603  -36.623 -8.311  1   34.59 ? 196 LEU   A CG  1 
ATOM   1624 C  CD1 . LEU   A 1 211 ? 30.248  -35.936 -8.604  1   35.01 ? 196 LEU   A CD1 1 
ATOM   1625 C  CD2 . LEU   A 1 211 ? 32.703  -35.589 -8.195  1   34.11 ? 196 LEU   A CD2 1 
ATOM   1626 N  N   . LEU   A 1 212 ? 31.573  -40.403 -8.241  1   34.79 ? 197 LEU   A N   1 
ATOM   1627 C  CA  . LEU   A 1 212 ? 31.8    -41.313 -9.348  1   35.13 ? 197 LEU   A CA  1 
ATOM   1628 C  C   . LEU   A 1 212 ? 30.547  -42.162 -9.628  1   34.69 ? 197 LEU   A C   1 
ATOM   1629 O  O   . LEU   A 1 212 ? 30.132  -42.305 -10.788 1   34.39 ? 197 LEU   A O   1 
ATOM   1630 C  CB  . LEU   A 1 212 ? 33.002  -42.209 -9.019  1   35.74 ? 197 LEU   A CB  1 
ATOM   1631 C  CG  . LEU   A 1 212 ? 33.613  -42.995 -10.174 1   37.51 ? 197 LEU   A CG  1 
ATOM   1632 C  CD1 . LEU   A 1 212 ? 35.052  -43.347 -9.86   1   37.8  ? 197 LEU   A CD1 1 
ATOM   1633 C  CD2 . LEU   A 1 212 ? 32.868  -44.29  -10.421 1   38.37 ? 197 LEU   A CD2 1 
ATOM   1634 N  N   . LYS   A 1 213 ? 29.953  -42.722 -8.57   1   34.39 ? 198 LYS   A N   1 
ATOM   1635 C  CA  . LYS   A 1 213 ? 28.765  -43.551 -8.727  1   34.86 ? 198 LYS   A CA  1 
ATOM   1636 C  C   . LYS   A 1 213 ? 27.585  -42.717 -9.282  1   33.65 ? 198 LYS   A C   1 
ATOM   1637 O  O   . LYS   A 1 213 ? 26.836  -43.199 -10.111 1   33.17 ? 198 LYS   A O   1 
ATOM   1638 C  CB  . LYS   A 1 213 ? 28.405  -44.188 -7.383  1   38.53 ? 198 LYS   A CB  1 
ATOM   1639 C  CG  . LYS   A 1 213 ? 27.147  -45.056 -7.421  1   45.26 ? 198 LYS   A CG  1 
ATOM   1640 C  CD  . LYS   A 1 213 ? 26.676  -45.418 -6.008  1   51.95 ? 198 LYS   A CD  1 
ATOM   1641 C  CE  . LYS   A 1 213 ? 25.377  -46.192 -6.026  1   56.84 ? 198 LYS   A CE  1 
ATOM   1642 N  NZ  . LYS   A 1 213 ? 24.714  -46.176 -4.699  1   59.86 ? 198 LYS   A NZ  1 
ATOM   1643 N  N   . ALA   A 1 214 ? 27.446  -41.475 -8.835  1   33.02 ? 199 ALA   A N   1 
ATOM   1644 C  CA  . ALA   A 1 214 ? 26.386  -40.581 -9.304  1   32.78 ? 199 ALA   A CA  1 
ATOM   1645 C  C   . ALA   A 1 214 ? 26.56   -40.277 -10.816 1   32.58 ? 199 ALA   A C   1 
ATOM   1646 O  O   . ALA   A 1 214 ? 25.586  -40.357 -11.566 1   32.88 ? 199 ALA   A O   1 
ATOM   1647 C  CB  . ALA   A 1 214 ? 26.404  -39.286 -8.496  1   32.62 ? 199 ALA   A CB  1 
ATOM   1648 N  N   . LEU   A 1 215 ? 27.799  -39.976 -11.259 1   31.74 ? 200 LEU   A N   1 
ATOM   1649 C  CA  . LEU   A 1 215 ? 28.084  -39.708 -12.666 1   31.79 ? 200 LEU   A CA  1 
ATOM   1650 C  C   . LEU   A 1 215 ? 27.766  -40.926 -13.545 1   32.81 ? 200 LEU   A C   1 
ATOM   1651 O  O   . LEU   A 1 215 ? 27.178  -40.766 -14.627 1   32.7  ? 200 LEU   A O   1 
ATOM   1652 C  CB  . LEU   A 1 215 ? 29.524  -39.223 -12.857 1   31.26 ? 200 LEU   A CB  1 
ATOM   1653 C  CG  . LEU   A 1 215 ? 29.817  -37.817 -12.329 1   32.12 ? 200 LEU   A CG  1 
ATOM   1654 C  CD1 . LEU   A 1 215 ? 31.313  -37.468 -12.422 1   31.4  ? 200 LEU   A CD1 1 
ATOM   1655 C  CD2 . LEU   A 1 215 ? 28.96   -36.776 -13.046 1   32.59 ? 200 LEU   A CD2 1 
ATOM   1656 N  N   . LEU   A 1 216 ? 28.061  -42.143 -13.052 1   33.14 ? 201 LEU   A N   1 
ATOM   1657 C  CA  . LEU   A 1 216 ? 27.739  -43.379 -13.774 1   34.05 ? 201 LEU   A CA  1 
ATOM   1658 C  C   . LEU   A 1 216 ? 26.238  -43.627 -13.874 1   33.66 ? 201 LEU   A C   1 
ATOM   1659 O  O   . LEU   A 1 216 ? 25.778  -44.16  -14.87  1   34.16 ? 201 LEU   A O   1 
ATOM   1660 C  CB  . LEU   A 1 216 ? 28.455  -44.608 -13.173 1   34.82 ? 201 LEU   A CB  1 
ATOM   1661 C  CG  . LEU   A 1 216 ? 29.998  -44.599 -13.301 1   36.8  ? 201 LEU   A CG  1 
ATOM   1662 C  CD1 . LEU   A 1 216 ? 30.601  -45.888 -12.708 1   37.73 ? 201 LEU   A CD1 1 
ATOM   1663 C  CD2 . LEU   A 1 216 ? 30.431  -44.48  -14.758 1   36.18 ? 201 LEU   A CD2 1 
ATOM   1664 N  N   . GLU   A 1 217 ? 25.48   -43.263 -12.854 1   33.43 ? 202 GLU   A N   1 
ATOM   1665 C  CA  . GLU   A 1 217 ? 24.028  -43.407 -12.858 1   33.81 ? 202 GLU   A CA  1 
ATOM   1666 C  C   . GLU   A 1 217 ? 23.392  -42.421 -13.862 1   33    ? 202 GLU   A C   1 
ATOM   1667 O  O   . GLU   A 1 217 ? 22.428  -42.774 -14.54  1   32.95 ? 202 GLU   A O   1 
ATOM   1668 C  CB  . GLU   A 1 217 ? 23.465  -43.225 -11.429 1   36.66 ? 202 GLU   A CB  1 
ATOM   1669 C  CG  . GLU   A 1 217 ? 21.95   -43.094 -11.297 1   45.93 ? 202 GLU   A CG  1 
ATOM   1670 C  CD  . GLU   A 1 217 ? 21.052  -44.162 -11.911 1   58.6  ? 202 GLU   A CD  1 
ATOM   1671 O  OE1 . GLU   A 1 217 ? 21.578  -45.207 -12.361 1   60.87 ? 202 GLU   A OE1 1 
ATOM   1672 O  OE2 . GLU   A 1 217 ? 19.816  -43.945 -11.954 1   62.85 ? 202 GLU   A OE2 1 
ATOM   1673 N  N   . ILE   A 1 218 ? 23.954  -41.212 -13.985 1   31.98 ? 203 ILE   A N   1 
ATOM   1674 C  CA  . ILE   A 1 218 ? 23.469  -40.223 -14.956 1   32    ? 203 ILE   A CA  1 
ATOM   1675 C  C   . ILE   A 1 218 ? 23.758  -40.716 -16.367 1   33.06 ? 203 ILE   A C   1 
ATOM   1676 O  O   . ILE   A 1 218 ? 22.883  -40.64  -17.242 1   33.74 ? 203 ILE   A O   1 
ATOM   1677 C  CB  . ILE   A 1 218 ? 24.096  -38.828 -14.696 1   30.91 ? 203 ILE   A CB  1 
ATOM   1678 C  CG1 . ILE   A 1 218 ? 23.488  -38.205 -13.434 1   30.38 ? 203 ILE   A CG1 1 
ATOM   1679 C  CG2 . ILE   A 1 218 ? 23.975  -37.872 -15.927 1   30.54 ? 203 ILE   A CG2 1 
ATOM   1680 C  CD1 . ILE   A 1 218 ? 24.273  -36.965 -12.92  1   30.78 ? 203 ILE   A CD1 1 
ATOM   1681 N  N   . ALA   A 1 219 ? 24.953  -41.271 -16.584 1   32.35 ? 204 ALA   A N   1 
ATOM   1682 C  CA  . ALA   A 1 219 ? 25.327  -41.793 -17.891 1   32.67 ? 204 ALA   A CA  1 
ATOM   1683 C  C   . ALA   A 1 219 ? 24.393  -42.936 -18.289 1   33.75 ? 204 ALA   A C   1 
ATOM   1684 O  O   . ALA   A 1 219 ? 23.92   -42.972 -19.411 1   34.23 ? 204 ALA   A O   1 
ATOM   1685 C  CB  . ALA   A 1 219 ? 26.772  -42.269 -17.869 1   31.98 ? 204 ALA   A CB  1 
ATOM   1686 N  N   . SER   A 1 220 ? 24.074  -43.809 -17.345 1   34.25 ? 205 SER   A N   1 
ATOM   1687 C  CA  . SER   A 1 220 ? 23.167  -44.914 -17.55  1   35.17 ? 205 SER   A CA  1 
ATOM   1688 C  C   . SER   A 1 220 ? 21.77   -44.425 -17.955 1   35.19 ? 205 SER   A C   1 
ATOM   1689 O  O   . SER   A 1 220 ? 21.193  -44.984 -18.869 1   35.07 ? 205 SER   A O   1 
ATOM   1690 C  CB  . SER   A 1 220 ? 23.109  -45.773 -16.295 1   37.75 ? 205 SER   A CB  1 
ATOM   1691 O  OG  . SER   A 1 220 ? 22.181  -46.824 -16.475 1   43.07 ? 205 SER   A OG  1 
ATOM   1692 N  N   . CYS   A 1 221 ? 21.257  -43.359 -17.322 1   35.55 ? 206 CYS   A N   1 
ATOM   1693 C  CA  . CYS   A 1 221 ? 19.955  -42.791 -17.652 1   36.45 ? 206 CYS   A CA  1 
ATOM   1694 C  C   . CYS   A 1 221 ? 19.966  -42.22  -19.069 1   36.81 ? 206 CYS   A C   1 
ATOM   1695 O  O   . CYS   A 1 221 ? 19.012  -42.417 -19.821 1   37.93 ? 206 CYS   A O   1 
ATOM   1696 C  CB  . CYS   A 1 221 ? 19.55   -41.725 -16.639 1   37.17 ? 206 CYS   A CB  1 
ATOM   1697 S  SG  . CYS   A 1 221 ? 19.205  -42.355 -14.974 1   42.07 ? 206 CYS   A SG  1 
ATOM   1698 N  N   . LEU   A 1 222 ? 21.013  -41.492 -19.419 1   35.39 ? 207 LEU   A N   1 
ATOM   1699 C  CA  . LEU   A 1 222 ? 21.141  -40.901 -20.748 1   35.04 ? 207 LEU   A CA  1 
ATOM   1700 C  C   . LEU   A 1 222 ? 21.317  -41.947 -21.849 1   34.69 ? 207 LEU   A C   1 
ATOM   1701 O  O   . LEU   A 1 222 ? 20.858  -41.721 -22.976 1   34.24 ? 207 LEU   A O   1 
ATOM   1702 C  CB  . LEU   A 1 222 ? 22.276  -39.865 -20.788 1   34.34 ? 207 LEU   A CB  1 
ATOM   1703 C  CG  . LEU   A 1 222 ? 22.135  -38.702 -19.837 1   34.9  ? 207 LEU   A CG  1 
ATOM   1704 C  CD1 . LEU   A 1 222 ? 23.372  -37.834 -19.876 1   35.16 ? 207 LEU   A CD1 1 
ATOM   1705 C  CD2 . LEU   A 1 222 ? 20.905  -37.896 -20.142 1   35.75 ? 207 LEU   A CD2 1 
ATOM   1706 N  N   . GLU   A 1 223 ? 21.97   -43.087 -21.523 1   34.71 ? 208 GLU   A N   1 
ATOM   1707 C  CA  . GLU   A 1 223 ? 22.143  -44.217 -22.438 1   35.67 ? 208 GLU   A CA  1 
ATOM   1708 C  C   . GLU   A 1 223 ? 20.767  -44.858 -22.701 1   37.16 ? 208 GLU   A C   1 
ATOM   1709 O  O   . GLU   A 1 223 ? 20.434  -45.178 -23.844 1   37.49 ? 208 GLU   A O   1 
ATOM   1710 C  CB  . GLU   A 1 223 ? 23.131  -45.251 -21.852 1   36.66 ? 208 GLU   A CB  1 
ATOM   1711 C  CG  . GLU   A 1 223 ? 24.589  -44.837 -21.958 1   38.71 ? 208 GLU   A CG  1 
ATOM   1712 C  CD  . GLU   A 1 223 ? 25.529  -45.509 -20.968 1   44.14 ? 208 GLU   A CD  1 
ATOM   1713 O  OE1 . GLU   A 1 223 ? 25.099  -46.466 -20.287 1   46.99 ? 208 GLU   A OE1 1 
ATOM   1714 O  OE2 . GLU   A 1 223 ? 26.691  -45.059 -20.852 1   44.37 ? 208 GLU   A OE2 1 
ATOM   1715 N  N   . LYS   A 1 224 ? 19.968  -45.023 -21.642 1   37.64 ? 209 LYS   A N   1 
ATOM   1716 C  CA  . LYS   A 1 224 ? 18.615  -45.58  -21.708 1   38.69 ? 209 LYS   A CA  1 
ATOM   1717 C  C   . LYS   A 1 224 ? 17.723  -44.711 -22.573 1   38.86 ? 209 LYS   A C   1 
ATOM   1718 O  O   . LYS   A 1 224 ? 16.883  -45.241 -23.285 1   39.7  ? 209 LYS   A O   1 
ATOM   1719 C  CB  . LYS   A 1 224 ? 18.003  -45.699 -20.297 1   41.56 ? 209 LYS   A CB  1 
ATOM   1720 C  CG  . LYS   A 1 224 ? 18.343  -47.023 -19.598 1   46.83 ? 209 LYS   A CG  1 
ATOM   1721 C  CD  . LYS   A 1 224 ? 18.237  -46.892 -18.093 1   52.4  ? 209 LYS   A CD  1 
ATOM   1722 C  CE  . LYS   A 1 224 ? 18.726  -48.142 -17.393 1   57.47 ? 209 LYS   A CE  1 
ATOM   1723 N  NZ  . LYS   A 1 224 ? 19.915  -48.751 -18.069 1   60.05 ? 209 LYS   A NZ  1 
ATOM   1724 N  N   . ALA   A 1 225 ? 17.893  -43.378 -22.511 1   37.8  ? 210 ALA   A N   1 
ATOM   1725 C  CA  . ALA   A 1 225 ? 17.104  -42.449 -23.312 1   38.08 ? 210 ALA   A CA  1 
ATOM   1726 C  C   . ALA   A 1 225 ? 17.352  -42.603 -24.825 1   38.99 ? 210 ALA   A C   1 
ATOM   1727 O  O   . ALA   A 1 225 ? 16.458  -42.309 -25.623 1   39.05 ? 210 ALA   A O   1 
ATOM   1728 C  CB  . ALA   A 1 225 ? 17.364  -41.02  -22.876 1   37.19 ? 210 ALA   A CB  1 
ATOM   1729 N  N   . LEU   A 1 226 ? 18.54   -43.068 -25.223 1   38.92 ? 211 LEU   A N   1 
ATOM   1730 C  CA  . LEU   A 1 226 ? 18.846  -43.291 -26.639 1   39.34 ? 211 LEU   A CA  1 
ATOM   1731 C  C   . LEU   A 1 226 ? 18.005  -44.426 -27.209 1   39.89 ? 211 LEU   A C   1 
ATOM   1732 O  O   . LEU   A 1 226 ? 17.502  -44.33  -28.333 1   38.83 ? 211 LEU   A O   1 
ATOM   1733 C  CB  . LEU   A 1 226 ? 20.346  -43.572 -26.839 1   39.66 ? 211 LEU   A CB  1 
ATOM   1734 C  CG  . LEU   A 1 226 ? 20.793  -43.899 -28.26  1   41.35 ? 211 LEU   A CG  1 
ATOM   1735 C  CD1 . LEU   A 1 226 ? 20.437  -42.792 -29.226 1   40.83 ? 211 LEU   A CD1 1 
ATOM   1736 C  CD2 . LEU   A 1 226 ? 22.28   -44.14  -28.312 1   42.82 ? 211 LEU   A CD2 1 
ATOM   1737 N  N   . GLN   A 1 227 ? 17.798  -45.479 -26.422 1   41.18 ? 212 GLN   A N   1 
ATOM   1738 C  CA  . GLN   A 1 227 ? 16.976  -46.601 -26.853 1   43.15 ? 212 GLN   A CA  1 
ATOM   1739 C  C   . GLN   A 1 227 ? 15.536  -46.158 -27.096 1   43.23 ? 212 GLN   A C   1 
ATOM   1740 O  O   . GLN   A 1 227 ? 14.926  -46.537 -28.104 1   44.1  ? 212 GLN   A O   1 
ATOM   1741 C  CB  . GLN   A 1 227 ? 17.049  -47.736 -25.815 1   46.91 ? 212 GLN   A CB  1 
ATOM   1742 C  CG  . GLN   A 1 227 ? 18.016  -48.869 -26.213 1   52.83 ? 212 GLN   A CG  1 
ATOM   1743 C  CD  . GLN   A 1 227 ? 19.401  -48.383 -26.555 1   58.97 ? 212 GLN   A CD  1 
ATOM   1744 O  OE1 . GLN   A 1 227 ? 19.88   -48.538 -27.691 1   60.58 ? 212 GLN   A OE1 1 
ATOM   1745 N  NE2 . GLN   A 1 227 ? 20.058  -47.757 -25.584 1   60.74 ? 212 GLN   A NE2 1 
ATOM   1746 N  N   . VAL   A 1 228 ? 15.022  -45.299 -26.199 1   41.67 ? 213 VAL   A N   1 
ATOM   1747 C  CA  . VAL   A 1 228 ? 13.676  -44.736 -26.285 1   40.65 ? 213 VAL   A CA  1 
ATOM   1748 C  C   . VAL   A 1 228 ? 13.498  -43.946 -27.585 1   40.95 ? 213 VAL   A C   1 
ATOM   1749 O  O   . VAL   A 1 228 ? 12.449  -44.026 -28.196 1   41.18 ? 213 VAL   A O   1 
ATOM   1750 C  CB  . VAL   A 1 228 ? 13.367  -43.887 -25.026 1   39.83 ? 213 VAL   A CB  1 
ATOM   1751 C  CG1 . VAL   A 1 228 ? 12.082  -43.088 -25.204 1   40.37 ? 213 VAL   A CG1 1 
ATOM   1752 C  CG2 . VAL   A 1 228 ? 13.286  -44.765 -23.787 1   39.52 ? 213 VAL   A CG2 1 
ATOM   1753 N  N   . PHE   A 1 229 ? 14.547  -43.252 -28.048 1   41.14 ? 214 PHE   A N   1 
ATOM   1754 C  CA  . PHE   A 1 229 ? 14.566  -42.478 -29.287 1   41.79 ? 214 PHE   A CA  1 
ATOM   1755 C  C   . PHE   A 1 229 ? 14.291  -43.315 -30.532 1   41.57 ? 214 PHE   A C   1 
ATOM   1756 O  O   . PHE   A 1 229 ? 13.724  -42.784 -31.479 1   40.95 ? 214 PHE   A O   1 
ATOM   1757 C  CB  . PHE   A 1 229 ? 15.951  -41.885 -29.467 1   42.71 ? 214 PHE   A CB  1 
ATOM   1758 C  CG  . PHE   A 1 229 ? 16.047  -40.418 -29.764 1   45.15 ? 214 PHE   A CG  1 
ATOM   1759 C  CD1 . PHE   A 1 229 ? 15.693  -39.921 -31     1   46.52 ? 214 PHE   A CD1 1 
ATOM   1760 C  CD2 . PHE   A 1 229 ? 16.566  -39.542 -28.828 1   47.46 ? 214 PHE   A CD2 1 
ATOM   1761 C  CE1 . PHE   A 1 229 ? 15.841  -38.57  -31.29  1   47.73 ? 214 PHE   A CE1 1 
ATOM   1762 C  CE2 . PHE   A 1 229 ? 16.704  -38.191 -29.114 1   48.5  ? 214 PHE   A CE2 1 
ATOM   1763 C  CZ  . PHE   A 1 229 ? 16.366  -37.722 -30.35  1   47.95 ? 214 PHE   A CZ  1 
ATOM   1764 N  N   . HIS   A 1 230 ? 14.743  -44.593 -30.558 1   41.39 ? 215 HIS   A N   1 
ATOM   1765 C  CA  . HIS   A 1 230 ? 14.605  -45.49  -31.715 1   42.02 ? 215 HIS   A CA  1 
ATOM   1766 C  C   . HIS   A 1 230 ? 13.167  -45.639 -32.225 1   40.73 ? 215 HIS   A C   1 
ATOM   1767 O  O   . HIS   A 1 230 ? 12.971  -45.829 -33.416 1   40.76 ? 215 HIS   A O   1 
ATOM   1768 C  CB  . HIS   A 1 230 ? 15.216  -46.886 -31.423 1   44.34 ? 215 HIS   A CB  1 
ATOM   1769 C  CG  . HIS   A 1 230 ? 16.682  -46.881 -31.098 1   49.11 ? 215 HIS   A CG  1 
ATOM   1770 N  ND1 . HIS   A 1 230 ? 17.5    -45.785 -31.389 1   51.51 ? 215 HIS   A ND1 1 
ATOM   1771 C  CD2 . HIS   A 1 230 ? 17.449  -47.861 -30.558 1   50.64 ? 215 HIS   A CD2 1 
ATOM   1772 C  CE1 . HIS   A 1 230 ? 18.718  -46.126 -30.986 1   51.79 ? 215 HIS   A CE1 1 
ATOM   1773 N  NE2 . HIS   A 1 230 ? 18.74   -47.362 -30.478 1   51.77 ? 215 HIS   A NE2 1 
ATOM   1774 N  N   . GLN   A 1 231 ? 12.173  -45.532 -31.328 1   39.99 ? 216 GLN   A N   1 
ATOM   1775 C  CA  . GLN   A 1 231 ? 10.739  -45.629 -31.617 1   39.62 ? 216 GLN   A CA  1 
ATOM   1776 C  C   . GLN   A 1 231 ? 10.236  -44.628 -32.606 1   38.87 ? 216 GLN   A C   1 
ATOM   1777 O  O   . GLN   A 1 231 ? 9.133   -44.812 -33.083 1   39.7  ? 216 GLN   A O   1 
ATOM   1778 C  CB  . GLN   A 1 231 ? 9.911   -45.405 -30.345 1   41.1  ? 216 GLN   A CB  1 
ATOM   1779 C  CG  . GLN   A 1 231 ? 10.21   -46.33  -29.21  1   44.19 ? 216 GLN   A CG  1 
ATOM   1780 C  CD  . GLN   A 1 231 ? 9.364   -45.892 -28.046 1   48.32 ? 216 GLN   A CD  1 
ATOM   1781 O  OE1 . GLN   A 1 231 ? 8.281   -46.435 -27.793 1   47.17 ? 216 GLN   A OE1 1 
ATOM   1782 N  NE2 . GLN   A 1 231 ? 9.808   -44.844 -27.357 1   48.66 ? 216 GLN   A NE2 1 
ATOM   1783 N  N   . ILE   A 1 232 ? 10.976  -43.535 -32.869 1   37.81 ? 217 ILE   A N   1 
ATOM   1784 C  CA  . ILE   A 1 232 ? 10.556  -42.475 -33.796 1   36.8  ? 217 ILE   A CA  1 
ATOM   1785 C  C   . ILE   A 1 232 ? 10.169  -43.026 -35.164 1   36.64 ? 217 ILE   A C   1 
ATOM   1786 O  O   . ILE   A 1 232 ? 9.166   -42.589 -35.738 1   36    ? 217 ILE   A O   1 
ATOM   1787 C  CB  . ILE   A 1 232 ? 11.621  -41.328 -33.906 1   36.45 ? 217 ILE   A CB  1 
ATOM   1788 C  CG1 . ILE   A 1 232 ? 11.049  -40.06  -34.572 1   36.08 ? 217 ILE   A CG1 1 
ATOM   1789 C  CG2 . ILE   A 1 232 ? 12.915  -41.775 -34.588 1   37.15 ? 217 ILE   A CG2 1 
ATOM   1790 C  CD1 . ILE   A 1 232 ? 10.261  -39.153 -33.582 1   35.9  ? 217 ILE   A CD1 1 
ATOM   1791 N  N   . HIS   A 1 233 ? 10.952  -44.009 -35.659 1   36.53 ? 218 HIS   A N   1 
ATOM   1792 C  CA  . HIS   A 1 233 ? 10.767  -44.601 -36.982 1   37.35 ? 218 HIS   A CA  1 
ATOM   1793 C  C   . HIS   A 1 233 ? 9.431   -45.317 -37.127 1   37.57 ? 218 HIS   A C   1 
ATOM   1794 O  O   . HIS   A 1 233 ? 8.84    -45.278 -38.199 1   37.98 ? 218 HIS   A O   1 
ATOM   1795 C  CB  . HIS   A 1 233 ? 11.93   -45.532 -37.336 1   37.73 ? 218 HIS   A CB  1 
ATOM   1796 C  CG  . HIS   A 1 233 ? 13.271  -44.885 -37.187 1   39.3  ? 218 HIS   A CG  1 
ATOM   1797 N  ND1 . HIS   A 1 233 ? 13.797  -44.08  -38.178 1   41.46 ? 218 HIS   A ND1 1 
ATOM   1798 C  CD2 . HIS   A 1 233 ? 14.148  -44.946 -36.157 1   39.62 ? 218 HIS   A CD2 1 
ATOM   1799 C  CE1 . HIS   A 1 233 ? 14.98   -43.679 -37.728 1   41.86 ? 218 HIS   A CE1 1 
ATOM   1800 N  NE2 . HIS   A 1 233 ? 15.228  -44.169 -36.508 1   41.06 ? 218 HIS   A NE2 1 
ATOM   1801 N  N   . ASP   A 1 234 ? 8.933   -45.912 -36.048 1   37.75 ? 219 ASP   A N   1 
ATOM   1802 C  CA  . ASP   A 1 234 ? 7.652   -46.616 -36.091 1   38.5  ? 219 ASP   A CA  1 
ATOM   1803 C  C   . ASP   A 1 234 ? 6.45    -45.69  -36.062 1   39.38 ? 219 ASP   A C   1 
ATOM   1804 O  O   . ASP   A 1 234 ? 5.347   -46.141 -36.405 1   40.54 ? 219 ASP   A O   1 
ATOM   1805 C  CB  . ASP   A 1 234 ? 7.54    -47.57  -34.895 1   40.21 ? 219 ASP   A CB  1 
ATOM   1806 C  CG  . ASP   A 1 234 ? 8.586   -48.661 -34.904 1   44.85 ? 219 ASP   A CG  1 
ATOM   1807 O  OD1 . ASP   A 1 234 ? 8.876   -49.183 -35.987 1   44.53 ? 219 ASP   A OD1 1 
ATOM   1808 O  OD2 . ASP   A 1 234 ? 9.108   -48.993 -33.82  1   47.99 ? 219 ASP   A OD2 1 
ATOM   1809 N  N   . HIS   A 1 235 ? 6.616   -44.423 -35.593 1   38.04 ? 220 HIS   A N   1 
ATOM   1810 C  CA  . HIS   A 1 235 ? 5.454   -43.57  -35.412 1   37.19 ? 220 HIS   A CA  1 
ATOM   1811 C  C   . HIS   A 1 235 ? 5.459   -42.267 -36.211 1   37.14 ? 220 HIS   A C   1 
ATOM   1812 O  O   . HIS   A 1 235 ? 4.479   -41.516 -36.159 1   37.01 ? 220 HIS   A O   1 
ATOM   1813 C  CB  . HIS   A 1 235 ? 5.257   -43.305 -33.91  1   37.7  ? 220 HIS   A CB  1 
ATOM   1814 C  CG  . HIS   A 1 235 ? 5.258   -44.556 -33.084 1   39.44 ? 220 HIS   A CG  1 
ATOM   1815 N  ND1 . HIS   A 1 235 ? 4.279   -45.525 -33.242 1   41.25 ? 220 HIS   A ND1 1 
ATOM   1816 C  CD2 . HIS   A 1 235 ? 6.147   -44.982 -32.151 1   40.53 ? 220 HIS   A CD2 1 
ATOM   1817 C  CE1 . HIS   A 1 235 ? 4.611   -46.506 -32.409 1   41.54 ? 220 HIS   A CE1 1 
ATOM   1818 N  NE2 . HIS   A 1 235 ? 5.724   -46.223 -31.732 1   41.15 ? 220 HIS   A NE2 1 
ATOM   1819 N  N   . VAL   A 1 236 ? 6.515   -41.998 -36.975 1   37.27 ? 221 VAL   A N   1 
ATOM   1820 C  CA  . VAL   A 1 236 ? 6.583   -40.801 -37.809 1   38.35 ? 221 VAL   A CA  1 
ATOM   1821 C  C   . VAL   A 1 236 ? 7.056   -41.189 -39.198 1   40.65 ? 221 VAL   A C   1 
ATOM   1822 O  O   . VAL   A 1 236 ? 7.993   -41.971 -39.308 1   41.35 ? 221 VAL   A O   1 
ATOM   1823 C  CB  . VAL   A 1 236 ? 7.511   -39.693 -37.221 1   38.28 ? 221 VAL   A CB  1 
ATOM   1824 C  CG1 . VAL   A 1 236 ? 7.306   -38.372 -37.953 1   39.04 ? 221 VAL   A CG1 1 
ATOM   1825 C  CG2 . VAL   A 1 236 ? 7.293   -39.506 -35.722 1   37.66 ? 221 VAL   A CG2 1 
ATOM   1826 N  N   . ASN   A 1 237 ? 6.444   -40.633 -40.256 1   42.14 ? 222 ASN   A N   1 
ATOM   1827 C  CA  . ASN   A 1 237 ? 6.922   -40.876 -41.613 1   43.87 ? 222 ASN   A CA  1 
ATOM   1828 C  C   . ASN   A 1 237 ? 7.416   -39.567 -42.217 1   44.04 ? 222 ASN   A C   1 
ATOM   1829 O  O   . ASN   A 1 237 ? 6.783   -38.52  -42.037 1   44.16 ? 222 ASN   A O   1 
ATOM   1830 C  CB  . ASN   A 1 237 ? 5.908   -41.609 -42.491 1   46.89 ? 222 ASN   A CB  1 
ATOM   1831 C  CG  . ASN   A 1 237 ? 4.755   -40.775 -42.958 1   52.77 ? 222 ASN   A CG  1 
ATOM   1832 O  OD1 . ASN   A 1 237 ? 3.694   -40.762 -42.32  1   56.7  ? 222 ASN   A OD1 1 
ATOM   1833 N  ND2 . ASN   A 1 237 ? 4.921   -40.078 -44.079 1   52.64 ? 222 ASN   A ND2 1 
ATOM   1834 N  N   . PRO   A 1 238 ? 8.571   -39.609 -42.9   1   43.66 ? 223 PRO   A N   1 
ATOM   1835 C  CA  . PRO   A 1 238 ? 9.17    -38.375 -43.438 1   43.58 ? 223 PRO   A CA  1 
ATOM   1836 C  C   . PRO   A 1 238 ? 8.28    -37.437 -44.259 1   43.83 ? 223 PRO   A C   1 
ATOM   1837 O  O   . PRO   A 1 238 ? 8.32    -36.223 -44.039 1   43.12 ? 223 PRO   A O   1 
ATOM   1838 C  CB  . PRO   A 1 238 ? 10.327  -38.896 -44.287 1   44.34 ? 223 PRO   A CB  1 
ATOM   1839 C  CG  . PRO   A 1 238 ? 10.705  -40.177 -43.65  1   44.81 ? 223 PRO   A CG  1 
ATOM   1840 C  CD  . PRO   A 1 238 ? 9.444   -40.778 -43.125 1   43.25 ? 223 PRO   A CD  1 
ATOM   1841 N  N   . LYS   A 1 239 ? 7.496   -37.974 -45.217 1   44.33 ? 224 LYS   A N   1 
ATOM   1842 C  CA  . LYS   A 1 239 ? 6.641   -37.146 -46.065 1   44.84 ? 224 LYS   A CA  1 
ATOM   1843 C  C   . LYS   A 1 239 ? 5.626   -36.313 -45.272 1   45.28 ? 224 LYS   A C   1 
ATOM   1844 O  O   . LYS   A 1 239 ? 5.539   -35.088 -45.454 1   45.62 ? 224 LYS   A O   1 
ATOM   1845 C  CB  . LYS   A 1 239 ? 5.922   -38.021 -47.117 1   47.09 ? 224 LYS   A CB  1 
ATOM   1846 C  CG  . LYS   A 1 239 ? 4.905   -37.258 -47.973 1   50.7  ? 224 LYS   A CG  1 
ATOM   1847 N  N   . ALA   A 1 240 ? 4.851   -36.976 -44.397 1   44.91 ? 225 ALA   A N   1 
ATOM   1848 C  CA  . ALA   A 1 240 ? 3.833   -36.295 -43.617 1   44.92 ? 225 ALA   A CA  1 
ATOM   1849 C  C   . ALA   A 1 240 ? 4.453   -35.302 -42.652 1   44.34 ? 225 ALA   A C   1 
ATOM   1850 O  O   . ALA   A 1 240 ? 3.947   -34.188 -42.512 1   44.12 ? 225 ALA   A O   1 
ATOM   1851 C  CB  . ALA   A 1 240 ? 3.009   -37.314 -42.867 1   45.67 ? 225 ALA   A CB  1 
ATOM   1852 N  N   . PHE   A 1 241 ? 5.573   -35.68  -42.01  1   44.02 ? 226 PHE   A N   1 
ATOM   1853 C  CA  . PHE   A 1 241 ? 6.245   -34.78  -41.081 1   43.73 ? 226 PHE   A CA  1 
ATOM   1854 C  C   . PHE   A 1 241 ? 6.734   -33.503 -41.794 1   43.94 ? 226 PHE   A C   1 
ATOM   1855 O  O   . PHE   A 1 241 ? 6.493   -32.38  -41.328 1   43.48 ? 226 PHE   A O   1 
ATOM   1856 C  CB  . PHE   A 1 241 ? 7.423   -35.506 -40.378 1   43.21 ? 226 PHE   A CB  1 
ATOM   1857 C  CG  . PHE   A 1 241 ? 8.243   -34.558 -39.537 1   42.7  ? 226 PHE   A CG  1 
ATOM   1858 C  CD1 . PHE   A 1 241 ? 7.846   -34.225 -38.255 1   43.21 ? 226 PHE   A CD1 1 
ATOM   1859 C  CD2 . PHE   A 1 241 ? 9.362   -33.936 -40.06  1   42.73 ? 226 PHE   A CD2 1 
ATOM   1860 C  CE1 . PHE   A 1 241 ? 8.572   -33.306 -37.503 1   43.64 ? 226 PHE   A CE1 1 
ATOM   1861 C  CE2 . PHE   A 1 241 ? 10.064  -33     -39.321 1   43.14 ? 226 PHE   A CE2 1 
ATOM   1862 C  CZ  . PHE   A 1 241 ? 9.675   -32.705 -38.041 1   43.24 ? 226 PHE   A CZ  1 
ATOM   1863 N  N   . PHE   A 1 242 ? 7.47    -33.688 -42.894 1   44.39 ? 227 PHE   A N   1 
ATOM   1864 C  CA  . PHE   A 1 242 ? 8.051   -32.568 -43.603 1   45.41 ? 227 PHE   A CA  1 
ATOM   1865 C  C   . PHE   A 1 242 ? 7.02    -31.666 -44.283 1   45.86 ? 227 PHE   A C   1 
ATOM   1866 O  O   . PHE   A 1 242 ? 7.11    -30.45  -44.158 1   45.97 ? 227 PHE   A O   1 
ATOM   1867 C  CB  . PHE   A 1 242 ? 9.123   -33.053 -44.609 1   45.8  ? 227 PHE   A CB  1 
ATOM   1868 C  CG  . PHE   A 1 242 ? 9.758   -31.925 -45.383 1   46.27 ? 227 PHE   A CG  1 
ATOM   1869 C  CD1 . PHE   A 1 242 ? 10.768  -31.165 -44.823 1   47.1  ? 227 PHE   A CD1 1 
ATOM   1870 C  CD2 . PHE   A 1 242 ? 9.334   -31.617 -46.666 1   47.3  ? 227 PHE   A CD2 1 
ATOM   1871 C  CE1 . PHE   A 1 242 ? 11.346  -30.114 -45.533 1   48.12 ? 227 PHE   A CE1 1 
ATOM   1872 C  CE2 . PHE   A 1 242 ? 9.89    -30.547 -47.363 1   48.13 ? 227 PHE   A CE2 1 
ATOM   1873 C  CZ  . PHE   A 1 242 ? 10.883  -29.793 -46.786 1   47.92 ? 227 PHE   A CZ  1 
ATOM   1874 N  N   . SER   A 1 243 ? 6.097   -32.245 -45.053 1   46.39 ? 228 SER   A N   1 
ATOM   1875 C  CA  . SER   A 1 243 ? 5.156   -31.442 -45.821 1   48.43 ? 228 SER   A CA  1 
ATOM   1876 C  C   . SER   A 1 243 ? 3.928   -30.967 -45.034 1   49.7  ? 228 SER   A C   1 
ATOM   1877 O  O   . SER   A 1 243 ? 3.29    -29.996 -45.45  1   50.37 ? 228 SER   A O   1 
ATOM   1878 C  CB  . SER   A 1 243 ? 4.732   -32.184 -47.088 1   50.61 ? 228 SER   A CB  1 
ATOM   1879 O  OG  . SER   A 1 243 ? 4.071   -33.402 -46.787 1   53.75 ? 228 SER   A OG  1 
ATOM   1880 N  N   . VAL   A 1 244 ? 3.586   -31.637 -43.911 1   49.51 ? 229 VAL   A N   1 
ATOM   1881 C  CA  . VAL   A 1 244 ? 2.389   -31.26  -43.155 1   49.58 ? 229 VAL   A CA  1 
ATOM   1882 C  C   . VAL   A 1 244 ? 2.689   -30.728 -41.736 1   49.5  ? 229 VAL   A C   1 
ATOM   1883 O  O   . VAL   A 1 244 ? 2.449   -29.547 -41.482 1   50.83 ? 229 VAL   A O   1 
ATOM   1884 C  CB  . VAL   A 1 244 ? 1.361   -32.414 -43.134 1   50.78 ? 229 VAL   A CB  1 
ATOM   1885 C  CG1 . VAL   A 1 244 ? 0.126   -32.02  -42.347 1   51.67 ? 229 VAL   A CG1 1 
ATOM   1886 C  CG2 . VAL   A 1 244 ? 0.996   -32.864 -44.548 1   51.83 ? 229 VAL   A CG2 1 
ATOM   1887 N  N   . LEU   A 1 245 ? 3.228   -31.558 -40.821 1   47.85 ? 230 LEU   A N   1 
ATOM   1888 C  CA  . LEU   A 1 245 ? 3.47    -31.134 -39.444 1   46.42 ? 230 LEU   A CA  1 
ATOM   1889 C  C   . LEU   A 1 245 ? 4.353   -29.915 -39.323 1   46.12 ? 230 LEU   A C   1 
ATOM   1890 O  O   . LEU   A 1 245 ? 4.035   -28.994 -38.566 1   46.56 ? 230 LEU   A O   1 
ATOM   1891 C  CB  . LEU   A 1 245 ? 4.015   -32.299 -38.577 1   45.29 ? 230 LEU   A CB  1 
ATOM   1892 C  CG  . LEU   A 1 245 ? 3.971   -32.081 -37.057 1   45.08 ? 230 LEU   A CG  1 
ATOM   1893 C  CD1 . LEU   A 1 245 ? 2.559   -31.744 -36.583 1   44.7  ? 230 LEU   A CD1 1 
ATOM   1894 C  CD2 . LEU   A 1 245 ? 4.478   -33.292 -36.309 1   45.18 ? 230 LEU   A CD2 1 
ATOM   1895 N  N   . ARG   A 1 246 ? 5.456   -29.902 -40.059 1   45.48 ? 231 ARG   A N   1 
ATOM   1896 C  CA  . ARG   A 1 246 ? 6.429   -28.818 -40.039 1   45.65 ? 231 ARG   A CA  1 
ATOM   1897 C  C   . ARG   A 1 246 ? 5.816   -27.418 -40.326 1   44.63 ? 231 ARG   A C   1 
ATOM   1898 O  O   . ARG   A 1 246 ? 6.214   -26.434 -39.698 1   44.92 ? 231 ARG   A O   1 
ATOM   1899 C  CB  . ARG   A 1 246 ? 7.574   -29.165 -41.008 1   47.85 ? 231 ARG   A CB  1 
ATOM   1900 C  CG  . ARG   A 1 246 ? 8.761   -28.225 -40.987 1   53.63 ? 231 ARG   A CG  1 
ATOM   1901 C  CD  . ARG   A 1 246 ? 9.792   -28.595 -42.057 1   59.63 ? 231 ARG   A CD  1 
ATOM   1902 N  NE  . ARG   A 1 246 ? 9.196   -28.64  -43.401 1   65.57 ? 231 ARG   A NE  1 
ATOM   1903 C  CZ  . ARG   A 1 246 ? 9.12    -27.601 -44.226 1   69.57 ? 231 ARG   A CZ  1 
ATOM   1904 N  NH1 . ARG   A 1 246 ? 9.636   -26.427 -43.878 1   70.26 ? 231 ARG   A NH1 1 
ATOM   1905 N  NH2 . ARG   A 1 246 ? 8.54    -27.73  -45.414 1   70.03 ? 231 ARG   A NH2 1 
ATOM   1906 N  N   . ILE   A 1 247 ? 4.836   -27.336 -41.226 1   43.96 ? 232 ILE   A N   1 
ATOM   1907 C  CA  . ILE   A 1 247 ? 4.205   -26.046 -41.536 1   44.19 ? 232 ILE   A CA  1 
ATOM   1908 C  C   . ILE   A 1 247 ? 3.436   -25.464 -40.304 1   41.23 ? 232 ILE   A C   1 
ATOM   1909 O  O   . ILE   A 1 247 ? 3.515   -24.264 -40.046 1   40.81 ? 232 ILE   A O   1 
ATOM   1910 C  CB  . ILE   A 1 247 ? 3.349   -26.063 -42.863 1   46.49 ? 232 ILE   A CB  1 
ATOM   1911 C  CG1 . ILE   A 1 247 ? 1.887   -26.405 -42.651 1   48.42 ? 232 ILE   A CG1 1 
ATOM   1912 C  CG2 . ILE   A 1 247 ? 3.951   -26.951 -43.956 1   47.47 ? 232 ILE   A CG2 1 
ATOM   1913 C  CD1 . ILE   A 1 247 ? 1.013   -25.127 -42.299 1   50.56 ? 232 ILE   A CD1 1 
ATOM   1914 N  N   . TYR   A 1 248 ? 2.711   -26.296 -39.569 1   39.64 ? 233 TYR   A N   1 
ATOM   1915 C  CA  . TYR   A 1 248 ? 1.926   -25.83  -38.422 1   39.58 ? 233 TYR   A CA  1 
ATOM   1916 C  C   . TYR   A 1 248 ? 2.762   -25.428 -37.223 1   40.57 ? 233 TYR   A C   1 
ATOM   1917 O  O   . TYR   A 1 248 ? 2.288   -24.662 -36.379 1   41.46 ? 233 TYR   A O   1 
ATOM   1918 C  CB  . TYR   A 1 248 ? 0.863   -26.858 -38.02  1   38.85 ? 233 TYR   A CB  1 
ATOM   1919 C  CG  . TYR   A 1 248 ? -0.218  -26.917 -39.069 1   38.59 ? 233 TYR   A CG  1 
ATOM   1920 C  CD1 . TYR   A 1 248 ? -1.206  -25.942 -39.132 1   38.88 ? 233 TYR   A CD1 1 
ATOM   1921 C  CD2 . TYR   A 1 248 ? -0.166  -27.856 -40.094 1   38.91 ? 233 TYR   A CD2 1 
ATOM   1922 C  CE1 . TYR   A 1 248 ? -2.138  -25.926 -40.167 1   38.87 ? 233 TYR   A CE1 1 
ATOM   1923 C  CE2 . TYR   A 1 248 ? -1.074  -27.835 -41.141 1   39.2  ? 233 TYR   A CE2 1 
ATOM   1924 C  CZ  . TYR   A 1 248 ? -2.063  -26.874 -41.174 1   39.7  ? 233 TYR   A CZ  1 
ATOM   1925 O  OH  . TYR   A 1 248 ? -2.963  -26.89  -42.212 1   40.29 ? 233 TYR   A OH  1 
ATOM   1926 N  N   . LEU   A 1 249 ? 4       -25.938 -37.14  1   39.95 ? 234 LEU   A N   1 
ATOM   1927 C  CA  . LEU   A 1 249 ? 4.892   -25.623 -36.04  1   40.44 ? 234 LEU   A CA  1 
ATOM   1928 C  C   . LEU   A 1 249 ? 5.786   -24.396 -36.323 1   40.62 ? 234 LEU   A C   1 
ATOM   1929 O  O   . LEU   A 1 249 ? 6.644   -24.082 -35.503 1   42.14 ? 234 LEU   A O   1 
ATOM   1930 C  CB  . LEU   A 1 249 ? 5.699   -26.877 -35.649 1   41.37 ? 234 LEU   A CB  1 
ATOM   1931 C  CG  . LEU   A 1 249 ? 4.8     -28.067 -35.202 1   43.41 ? 234 LEU   A CG  1 
ATOM   1932 C  CD1 . LEU   A 1 249 ? 5.586   -29.338 -34.991 1   43.93 ? 234 LEU   A CD1 1 
ATOM   1933 C  CD2 . LEU   A 1 249 ? 4.011   -27.736 -33.955 1   44.4  ? 234 LEU   A CD2 1 
ATOM   1934 N  N   . SER   A 1 250 ? 5.577   -23.681 -37.457 1   38.55 ? 235 SER   A N   1 
ATOM   1935 C  CA  . SER   A 1 250 ? 6.332   -22.466 -37.727 1   37.65 ? 235 SER   A CA  1 
ATOM   1936 C  C   . SER   A 1 250 ? 5.873   -21.332 -36.841 1   36.63 ? 235 SER   A C   1 
ATOM   1937 O  O   . SER   A 1 250 ? 4.679   -21.204 -36.547 1   36.83 ? 235 SER   A O   1 
ATOM   1938 C  CB  . SER   A 1 250 ? 6.167   -22.027 -39.176 1   39.17 ? 235 SER   A CB  1 
ATOM   1939 O  OG  . SER   A 1 250 ? 6.753   -23.004 -40.013 1   43.42 ? 235 SER   A OG  1 
ATOM   1940 N  N   . GLY   A 1 251 ? 6.808   -20.464 -36.493 1   35.33 ? 236 GLY   A N   1 
ATOM   1941 C  CA  . GLY   A 1 251 ? 6.493   -19.281 -35.716 1   34.73 ? 236 GLY   A CA  1 
ATOM   1942 C  C   . GLY   A 1 251 ? 6.487   -18.044 -36.586 1   34.54 ? 236 GLY   A C   1 
ATOM   1943 O  O   . GLY   A 1 251 ? 6.375   -18.121 -37.825 1   34.33 ? 236 GLY   A O   1 
ATOM   1944 N  N   . TRP   A 1 252 ? 6.6     -16.902 -35.945 1   33.97 ? 237 TRP   A N   1 
ATOM   1945 C  CA  . TRP   A 1 252 ? 6.599   -15.632 -36.653 1   34.73 ? 237 TRP   A CA  1 
ATOM   1946 C  C   . TRP   A 1 252 ? 7.713   -14.735 -36.153 1   36.58 ? 237 TRP   A C   1 
ATOM   1947 O  O   . TRP   A 1 252 ? 7.446   -13.659 -35.662 1   38.25 ? 237 TRP   A O   1 
ATOM   1948 C  CB  . TRP   A 1 252 ? 5.217   -14.941 -36.618 1   33.67 ? 237 TRP   A CB  1 
ATOM   1949 C  CG  . TRP   A 1 252 ? 4.362   -15.215 -35.404 1   31.96 ? 237 TRP   A CG  1 
ATOM   1950 C  CD1 . TRP   A 1 252 ? 4.282   -14.477 -34.257 1   31.61 ? 237 TRP   A CD1 1 
ATOM   1951 C  CD2 . TRP   A 1 252 ? 3.44    -16.303 -35.25  1   31.75 ? 237 TRP   A CD2 1 
ATOM   1952 N  NE1 . TRP   A 1 252 ? 3.363   -15.036 -33.397 1   31.62 ? 237 TRP   A NE1 1 
ATOM   1953 C  CE2 . TRP   A 1 252 ? 2.847   -16.174 -33.976 1   31.83 ? 237 TRP   A CE2 1 
ATOM   1954 C  CE3 . TRP   A 1 252 ? 3.081   -17.397 -36.06  1   31.68 ? 237 TRP   A CE3 1 
ATOM   1955 C  CZ2 . TRP   A 1 252 ? 1.886   -17.066 -33.514 1   32    ? 237 TRP   A CZ2 1 
ATOM   1956 C  CZ3 . TRP   A 1 252 ? 2.148   -18.291 -35.579 1   32.66 ? 237 TRP   A CZ3 1 
ATOM   1957 C  CH2 . TRP   A 1 252 ? 1.552   -18.112 -34.33  1   32.26 ? 237 TRP   A CH2 1 
ATOM   1958 N  N   . LYS   A 1 253 ? 8.96    -15.195 -36.242 1   36.14 ? 238 LYS   A N   1 
ATOM   1959 C  CA  . LYS   A 1 253 ? 10.116  -14.402 -35.87  1   36.95 ? 238 LYS   A CA  1 
ATOM   1960 C  C   . LYS   A 1 253 ? 11.111  -14.632 -36.977 1   38.3  ? 238 LYS   A C   1 
ATOM   1961 O  O   . LYS   A 1 253 ? 11.557  -15.762 -37.168 1   38.36 ? 238 LYS   A O   1 
ATOM   1962 C  CB  . LYS   A 1 253 ? 10.697  -14.827 -34.521 1   38.29 ? 238 LYS   A CB  1 
ATOM   1963 C  CG  . LYS   A 1 253 ? 11.778  -13.875 -34.024 1   42.36 ? 238 LYS   A CG  1 
ATOM   1964 C  CD  . LYS   A 1 253 ? 12.413  -14.386 -32.739 1   47.4  ? 238 LYS   A CD  1 
ATOM   1965 C  CE  . LYS   A 1 253 ? 13.626  -13.578 -32.321 1   51.73 ? 238 LYS   A CE  1 
ATOM   1966 N  NZ  . LYS   A 1 253 ? 13.246  -12.304 -31.642 1   54.81 ? 238 LYS   A NZ  1 
ATOM   1967 N  N   . GLY   A 1 254 ? 11.402  -13.585 -37.752 1   39.07 ? 239 GLY   A N   1 
ATOM   1968 C  CA  . GLY   A 1 254 ? 12.253  -13.701 -38.935 1   39.51 ? 239 GLY   A CA  1 
ATOM   1969 C  C   . GLY   A 1 254 ? 11.59   -14.564 -40.003 1   40.38 ? 239 GLY   A C   1 
ATOM   1970 O  O   . GLY   A 1 254 ? 12.266  -15.26  -40.771 1   40.55 ? 239 GLY   A O   1 
ATOM   1971 N  N   . ASN   A 1 255 ? 10.247  -14.591 -40.016 1   40.71 ? 240 ASN   A N   1 
ATOM   1972 C  CA  . ASN   A 1 255 ? 9.512   -15.4   -40.976 1   41.79 ? 240 ASN   A CA  1 
ATOM   1973 C  C   . ASN   A 1 255 ? 9.053   -14.514 -42.12  1   43.13 ? 240 ASN   A C   1 
ATOM   1974 O  O   . ASN   A 1 255 ? 8.249   -13.626 -41.895 1   42.79 ? 240 ASN   A O   1 
ATOM   1975 C  CB  . ASN   A 1 255 ? 8.306   -16.093 -40.321 1   41.59 ? 240 ASN   A CB  1 
ATOM   1976 C  CG  . ASN   A 1 255 ? 7.704   -17.152 -41.202 1   43.94 ? 240 ASN   A CG  1 
ATOM   1977 O  OD1 . ASN   A 1 255 ? 7.791   -17.107 -42.44  1   46.46 ? 240 ASN   A OD1 1 
ATOM   1978 N  ND2 . ASN   A 1 255 ? 7.105   -18.151 -40.595 1   42.67 ? 240 ASN   A ND2 1 
ATOM   1979 N  N   . PRO   A 1 256 ? 9.526   -14.776 -43.354 1   44.53 ? 241 PRO   A N   1 
ATOM   1980 C  CA  . PRO   A 1 256 ? 9.105   -13.947 -44.502 1   45.64 ? 241 PRO   A CA  1 
ATOM   1981 C  C   . PRO   A 1 256 ? 7.592   -13.895 -44.735 1   46.89 ? 241 PRO   A C   1 
ATOM   1982 O  O   . PRO   A 1 256 ? 7.096   -12.889 -45.232 1   47.91 ? 241 PRO   A O   1 
ATOM   1983 C  CB  . PRO   A 1 256 ? 9.84    -14.588 -45.691 1   46.25 ? 241 PRO   A CB  1 
ATOM   1984 C  CG  . PRO   A 1 256 ? 11.012  -15.303 -45.081 1   46.42 ? 241 PRO   A CG  1 
ATOM   1985 C  CD  . PRO   A 1 256 ? 10.502  -15.81  -43.757 1   44.24 ? 241 PRO   A CD  1 
ATOM   1986 N  N   . GLN   A 1 257 ? 6.853   -14.954 -44.358 1   46.6  ? 242 GLN   A N   1 
ATOM   1987 C  CA  . GLN   A 1 257 ? 5.4     -14.985 -44.507 1   46.82 ? 242 GLN   A CA  1 
ATOM   1988 C  C   . GLN   A 1 257 ? 4.688   -14.062 -43.524 1   47.56 ? 242 GLN   A C   1 
ATOM   1989 O  O   . GLN   A 1 257 ? 3.558   -13.688 -43.782 1   48.02 ? 242 GLN   A O   1 
ATOM   1990 C  CB  . GLN   A 1 257 ? 4.853   -16.411 -44.399 1   47.87 ? 242 GLN   A CB  1 
ATOM   1991 C  CG  . GLN   A 1 257 ? 5.558   -17.384 -45.337 1   50.05 ? 242 GLN   A CG  1 
ATOM   1992 C  CD  . GLN   A 1 257 ? 4.879   -18.718 -45.363 1   52.77 ? 242 GLN   A CD  1 
ATOM   1993 O  OE1 . GLN   A 1 257 ? 3.692   -18.816 -45.644 1   52.05 ? 242 GLN   A OE1 1 
ATOM   1994 N  NE2 . GLN   A 1 257 ? 5.635   -19.774 -45.071 1   54.21 ? 242 GLN   A NE2 1 
ATOM   1995 N  N   . LEU   A 1 258 ? 5.324   -13.715 -42.387 1   47.75 ? 243 LEU   A N   1 
ATOM   1996 C  CA  . LEU   A 1 258 ? 4.791   -12.802 -41.37  1   47.68 ? 243 LEU   A CA  1 
ATOM   1997 C  C   . LEU   A 1 258 ? 5.973   -11.952 -40.909 1   47.88 ? 243 LEU   A C   1 
ATOM   1998 O  O   . LEU   A 1 258 ? 6.356   -11.986 -39.736 1   47.53 ? 243 LEU   A O   1 
ATOM   1999 C  CB  . LEU   A 1 258 ? 4.199   -13.571 -40.179 1   47.81 ? 243 LEU   A CB  1 
ATOM   2000 C  CG  . LEU   A 1 258 ? 2.75    -13.942 -40.251 1   49.62 ? 243 LEU   A CG  1 
ATOM   2001 C  CD1 . LEU   A 1 258 ? 2.616   -15.317 -40.798 1   50.67 ? 243 LEU   A CD1 1 
ATOM   2002 C  CD2 . LEU   A 1 258 ? 2.12    -13.926 -38.863 1   50.26 ? 243 LEU   A CD2 1 
ATOM   2003 N  N   . SER   A 1 259 ? 6.583   -11.214 -41.86  1   48.22 ? 244 SER   A N   1 
ATOM   2004 C  CA  . SER   A 1 259 ? 7.793   -10.414 -41.645 1   48.97 ? 244 SER   A CA  1 
ATOM   2005 C  C   . SER   A 1 259 ? 7.756   -9.469  -40.44  1   48.71 ? 244 SER   A C   1 
ATOM   2006 O  O   . SER   A 1 259 ? 8.813   -9.221  -39.862 1   49.3  ? 244 SER   A O   1 
ATOM   2007 C  CB  . SER   A 1 259 ? 8.191   -9.654  -42.909 1   51.36 ? 244 SER   A CB  1 
ATOM   2008 O  OG  . SER   A 1 259 ? 7.147   -8.841  -43.415 1   54.99 ? 244 SER   A OG  1 
ATOM   2009 N  N   . ASP   A 1 260 ? 6.579   -8.988  -40.02  1   47.73 ? 245 ASP   A N   1 
ATOM   2010 C  CA  . ASP   A 1 260 ? 6.501   -8.095  -38.845 1   47.52 ? 245 ASP   A CA  1 
ATOM   2011 C  C   . ASP   A 1 260 ? 5.986   -8.753  -37.551 1   45.73 ? 245 ASP   A C   1 
ATOM   2012 O  O   . ASP   A 1 260 ? 5.973   -8.127  -36.49  1   45.71 ? 245 ASP   A O   1 
ATOM   2013 C  CB  . ASP   A 1 260 ? 5.648   -6.858  -39.163 1   50.48 ? 245 ASP   A CB  1 
ATOM   2014 C  CG  . ASP   A 1 260 ? 6.108   -6.139  -40.417 1   57.02 ? 245 ASP   A CG  1 
ATOM   2015 O  OD1 . ASP   A 1 260 ? 7.338   -5.919  -40.56  1   58.2  ? 245 ASP   A OD1 1 
ATOM   2016 O  OD2 . ASP   A 1 260 ? 5.245   -5.827  -41.272 1   59.92 ? 245 ASP   A OD2 1 
ATOM   2017 N  N   . GLY   A 1 261 ? 5.566   -9.999  -37.649 1   44.37 ? 246 GLY   A N   1 
ATOM   2018 C  CA  . GLY   A 1 261 ? 4.995   -10.709 -36.524 1   43.18 ? 246 GLY   A CA  1 
ATOM   2019 C  C   . GLY   A 1 261 ? 3.502   -10.86  -36.681 1   42.44 ? 246 GLY   A C   1 
ATOM   2020 O  O   . GLY   A 1 261 ? 2.96    -10.777 -37.792 1   42.87 ? 246 GLY   A O   1 
ATOM   2021 N  N   . LEU   A 1 262 ? 2.822   -11.096 -35.57  1   40.75 ? 247 LEU   A N   1 
ATOM   2022 C  CA  . LEU   A 1 262 ? 1.395   -11.333 -35.588 1   39.25 ? 247 LEU   A CA  1 
ATOM   2023 C  C   . LEU   A 1 262 ? 0.693   -10.28  -34.753 1   38.08 ? 247 LEU   A C   1 
ATOM   2024 O  O   . LEU   A 1 262 ? 1.178   -9.947  -33.665 1   37.28 ? 247 LEU   A O   1 
ATOM   2025 C  CB  . LEU   A 1 262 ? 1.121   -12.739 -35.007 1   38.65 ? 247 LEU   A CB  1 
ATOM   2026 C  CG  . LEU   A 1 262 ? -0.335  -13.189 -34.958 1   39.19 ? 247 LEU   A CG  1 
ATOM   2027 C  CD1 . LEU   A 1 262 ? -0.888  -13.455 -36.359 1   38.7  ? 247 LEU   A CD1 1 
ATOM   2028 C  CD2 . LEU   A 1 262 ? -0.486  -14.433 -34.081 1   40.22 ? 247 LEU   A CD2 1 
ATOM   2029 N  N   . VAL   A 1 263 ? -0.46   -9.771  -35.239 1   37.6  ? 248 VAL   A N   1 
ATOM   2030 C  CA  . VAL   A 1 263 ? -1.223  -8.813  -34.454 1   38.02 ? 248 VAL   A CA  1 
ATOM   2031 C  C   . VAL   A 1 263 ? -2.1    -9.59   -33.498 1   38.09 ? 248 VAL   A C   1 
ATOM   2032 O  O   . VAL   A 1 263 ? -2.882  -10.431 -33.931 1   39.27 ? 248 VAL   A O   1 
ATOM   2033 C  CB  . VAL   A 1 263 ? -2.052  -7.801  -35.306 1   38.94 ? 248 VAL   A CB  1 
ATOM   2034 C  CG1 . VAL   A 1 263 ? -2.852  -6.86   -34.412 1   39.21 ? 248 VAL   A CG1 1 
ATOM   2035 C  CG2 . VAL   A 1 263 ? -1.155  -7.008  -36.243 1   39.2  ? 248 VAL   A CG2 1 
ATOM   2036 N  N   . TYR   A 1 264 ? -1.946  -9.35   -32.197 1   36.99 ? 249 TYR   A N   1 
ATOM   2037 C  CA  . TYR   A 1 264 ? -2.742  -9.981  -31.162 1   37.16 ? 249 TYR   A CA  1 
ATOM   2038 C  C   . TYR   A 1 264 ? -3.82   -8.93   -30.833 1   39.12 ? 249 TYR   A C   1 
ATOM   2039 O  O   . TYR   A 1 264 ? -3.675  -8.137  -29.892 1   39.22 ? 249 TYR   A O   1 
ATOM   2040 C  CB  . TYR   A 1 264 ? -1.867  -10.319 -29.931 1   36.08 ? 249 TYR   A CB  1 
ATOM   2041 C  CG  . TYR   A 1 264 ? -0.878  -11.445 -30.187 1   35.63 ? 249 TYR   A CG  1 
ATOM   2042 C  CD1 . TYR   A 1 264 ? 0.405   -11.181 -30.641 1   35.86 ? 249 TYR   A CD1 1 
ATOM   2043 C  CD2 . TYR   A 1 264 ? -1.225  -12.769 -29.956 1   36.03 ? 249 TYR   A CD2 1 
ATOM   2044 C  CE1 . TYR   A 1 264 ? 1.319   -12.204 -30.865 1   36.44 ? 249 TYR   A CE1 1 
ATOM   2045 C  CE2 . TYR   A 1 264 ? -0.327  -13.806 -30.201 1   36.04 ? 249 TYR   A CE2 1 
ATOM   2046 C  CZ  . TYR   A 1 264 ? 0.947   -13.515 -30.651 1   37.07 ? 249 TYR   A CZ  1 
ATOM   2047 O  OH  . TYR   A 1 264 ? 1.855   -14.524 -30.872 1   39.28 ? 249 TYR   A OH  1 
ATOM   2048 N  N   . GLU   A 1 265 ? -4.865  -8.889  -31.682 1   38.97 ? 250 GLU   A N   1 
ATOM   2049 C  CA  . GLU   A 1 265 ? -5.942  -7.898  -31.64  1   38.37 ? 250 GLU   A CA  1 
ATOM   2050 C  C   . GLU   A 1 265 ? -6.563  -7.701  -30.285 1   38.01 ? 250 GLU   A C   1 
ATOM   2051 O  O   . GLU   A 1 265 ? -6.98   -8.658  -29.639 1   37.05 ? 250 GLU   A O   1 
ATOM   2052 C  CB  . GLU   A 1 265 ? -7.007  -8.259  -32.671 1   39.97 ? 250 GLU   A CB  1 
ATOM   2053 C  CG  . GLU   A 1 265 ? -8.059  -7.184  -32.875 1   43.54 ? 250 GLU   A CG  1 
ATOM   2054 C  CD  . GLU   A 1 265 ? -9.066  -7.61   -33.918 1   43.57 ? 250 GLU   A CD  1 
ATOM   2055 O  OE1 . GLU   A 1 265 ? -8.998  -7.109  -35.062 1   45.09 ? 250 GLU   A OE1 1 
ATOM   2056 O  OE2 . GLU   A 1 265 ? -9.924  -8.455  -33.587 1   43.7  ? 250 GLU   A OE2 1 
ATOM   2057 N  N   . GLY   A 1 266 ? -6.602  -6.449  -29.836 1   38.79 ? 251 GLY   A N   1 
ATOM   2058 C  CA  . GLY   A 1 266 ? -7.189  -6.128  -28.54  1   39.9  ? 251 GLY   A CA  1 
ATOM   2059 C  C   . GLY   A 1 266 ? -6.234  -6.232  -27.367 1   42.09 ? 251 GLY   A C   1 
ATOM   2060 O  O   . GLY   A 1 266 ? -6.55   -5.75   -26.273 1   42.59 ? 251 GLY   A O   1 
ATOM   2061 N  N   . PHE   A 1 267 ? -5.057  -6.872  -27.564 1   42.9  ? 252 PHE   A N   1 
ATOM   2062 C  CA  . PHE   A 1 267 ? -4.077  -7.009  -26.482 1   43.43 ? 252 PHE   A CA  1 
ATOM   2063 C  C   . PHE   A 1 267 ? -2.878  -6.069  -26.649 1   44.15 ? 252 PHE   A C   1 
ATOM   2064 O  O   . PHE   A 1 267 ? -2.545  -5.357  -25.709 1   44.26 ? 252 PHE   A O   1 
ATOM   2065 C  CB  . PHE   A 1 267 ? -3.636  -8.468  -26.28  1   42.55 ? 252 PHE   A CB  1 
ATOM   2066 C  CG  . PHE   A 1 267 ? -3.048  -8.658  -24.906 1   42.43 ? 252 PHE   A CG  1 
ATOM   2067 C  CD1 . PHE   A 1 267 ? -3.862  -8.936  -23.82  1   42.68 ? 252 PHE   A CD1 1 
ATOM   2068 C  CD2 . PHE   A 1 267 ? -1.684  -8.504  -24.69  1   42.81 ? 252 PHE   A CD2 1 
ATOM   2069 C  CE1 . PHE   A 1 267 ? -3.319  -9.082  -22.552 1   43.17 ? 252 PHE   A CE1 1 
ATOM   2070 C  CE2 . PHE   A 1 267 ? -1.142  -8.674  -23.425 1   42.98 ? 252 PHE   A CE2 1 
ATOM   2071 C  CZ  . PHE   A 1 267 ? -1.962  -8.947  -22.365 1   42.81 ? 252 PHE   A CZ  1 
ATOM   2072 N  N   . TRP   A 1 268 ? -2.223  -6.083  -27.826 1   44.58 ? 253 TRP   A N   1 
ATOM   2073 C  CA  . TRP   A 1 268 ? -1.097  -5.196  -28.154 1   46.05 ? 253 TRP   A CA  1 
ATOM   2074 C  C   . TRP   A 1 268 ? -1.414  -4.495  -29.457 1   47.59 ? 253 TRP   A C   1 
ATOM   2075 O  O   . TRP   A 1 268 ? -2.031  -5.083  -30.345 1   47.76 ? 253 TRP   A O   1 
ATOM   2076 C  CB  . TRP   A 1 268 ? 0.248   -5.937  -28.34  1   46.06 ? 253 TRP   A CB  1 
ATOM   2077 C  CG  . TRP   A 1 268 ? 0.806   -6.559  -27.098 1   46.79 ? 253 TRP   A CG  1 
ATOM   2078 C  CD1 . TRP   A 1 268 ? 1.158   -5.927  -25.94  1   47.38 ? 253 TRP   A CD1 1 
ATOM   2079 C  CD2 . TRP   A 1 268 ? 1.143   -7.939  -26.922 1   46.8  ? 253 TRP   A CD2 1 
ATOM   2080 N  NE1 . TRP   A 1 268 ? 1.638   -6.842  -25.03  1   47.49 ? 253 TRP   A NE1 1 
ATOM   2081 C  CE2 . TRP   A 1 268 ? 1.673   -8.079  -25.621 1   47.42 ? 253 TRP   A CE2 1 
ATOM   2082 C  CE3 . TRP   A 1 268 ? 1.05    -9.07   -27.741 1   47.28 ? 253 TRP   A CE3 1 
ATOM   2083 C  CZ2 . TRP   A 1 268 ? 2.103   -9.31   -25.121 1   47.67 ? 253 TRP   A CZ2 1 
ATOM   2084 C  CZ3 . TRP   A 1 268 ? 1.495   -10.281 -27.25  1   47.87 ? 253 TRP   A CZ3 1 
ATOM   2085 C  CH2 . TRP   A 1 268 ? 1.992   -10.395 -25.948 1   47.74 ? 253 TRP   A CH2 1 
ATOM   2086 N  N   . GLU   A 1 269 ? -0.927  -3.266  -29.593 1   48.51 ? 254 GLU   A N   1 
ATOM   2087 C  CA  . GLU   A 1 269 ? -1.17   -2.44   -30.756 1   49.86 ? 254 GLU   A CA  1 
ATOM   2088 C  C   . GLU   A 1 269 ? -0.402  -2.884  -31.994 1   49.91 ? 254 GLU   A C   1 
ATOM   2089 O  O   . GLU   A 1 269 ? -0.987  -2.965  -33.078 1   51.26 ? 254 GLU   A O   1 
ATOM   2090 C  CB  . GLU   A 1 269 ? -0.853  -0.978  -30.416 1   52.48 ? 254 GLU   A CB  1 
ATOM   2091 N  N   . ASP   A 1 270 ? 0.901   -3.141  -31.842 1   47.99 ? 255 ASP   A N   1 
ATOM   2092 C  CA  . ASP   A 1 270 ? 1.793   -3.536  -32.929 1   46.79 ? 255 ASP   A CA  1 
ATOM   2093 C  C   . ASP   A 1 270 ? 1.95    -5.054  -33.03  1   43.82 ? 255 ASP   A C   1 
ATOM   2094 O  O   . ASP   A 1 270 ? 1.79    -5.756  -32.039 1   42.57 ? 255 ASP   A O   1 
ATOM   2095 C  CB  . ASP   A 1 270 ? 3.175   -2.899  -32.694 1   50    ? 255 ASP   A CB  1 
ATOM   2096 C  CG  . ASP   A 1 270 ? 3.107   -1.397  -32.634 1   58.78 ? 255 ASP   A CG  1 
ATOM   2097 O  OD1 . ASP   A 1 270 ? 2.4     -0.801  -33.487 1   60.23 ? 255 ASP   A OD1 1 
ATOM   2098 O  OD2 . ASP   A 1 270 ? 3.753   -0.81   -31.731 1   62.18 ? 255 ASP   A OD2 1 
ATOM   2099 N  N   . PRO   A 1 271 ? 2.272   -5.577  -34.228 1   42.78 ? 256 PRO   A N   1 
ATOM   2100 C  CA  . PRO   A 1 271 ? 2.486   -7.024  -34.353 1   41.63 ? 256 PRO   A CA  1 
ATOM   2101 C  C   . PRO   A 1 271 ? 3.733   -7.47   -33.583 1   40.47 ? 256 PRO   A C   1 
ATOM   2102 O  O   . PRO   A 1 271 ? 4.711   -6.724  -33.498 1   40.03 ? 256 PRO   A O   1 
ATOM   2103 C  CB  . PRO   A 1 271 ? 2.642   -7.236  -35.86  1   42.24 ? 256 PRO   A CB  1 
ATOM   2104 C  CG  . PRO   A 1 271 ? 3.099   -5.936  -36.375 1   43.16 ? 256 PRO   A CG  1 
ATOM   2105 C  CD  . PRO   A 1 271 ? 2.472   -4.885  -35.517 1   41.8  ? 256 PRO   A CD  1 
ATOM   2106 N  N   . LYS   A 1 272 ? 3.668   -8.654  -32.967 1   39.31 ? 257 LYS   A N   1 
ATOM   2107 C  CA  . LYS   A 1 272 ? 4.785   -9.167  -32.178 1   38.47 ? 257 LYS   A CA  1 
ATOM   2108 C  C   . LYS   A 1 272 ? 5.395   -10.408 -32.801 1   37.89 ? 257 LYS   A C   1 
ATOM   2109 O  O   . LYS   A 1 272 ? 4.691   -11.257 -33.353 1   38.04 ? 257 LYS   A O   1 
ATOM   2110 C  CB  . LYS   A 1 272 ? 4.335   -9.478  -30.756 1   40.12 ? 257 LYS   A CB  1 
ATOM   2111 C  CG  . LYS   A 1 272 ? 3.68    -8.309  -30.032 1   44.91 ? 257 LYS   A CG  1 
ATOM   2112 C  CD  . LYS   A 1 272 ? 4.673   -7.223  -29.717 1   48.41 ? 257 LYS   A CD  1 
ATOM   2113 C  CE  . LYS   A 1 272 ? 4.028   -6.132  -28.9   1   52.58 ? 257 LYS   A CE  1 
ATOM   2114 N  NZ  . LYS   A 1 272 ? 4.741   -4.84   -29.061 1   56.71 ? 257 LYS   A NZ  1 
ATOM   2115 N  N   . GLU   A 1 273 ? 6.701   -10.534 -32.669 1   37.47 ? 258 GLU   A N   1 
ATOM   2116 C  CA  . GLU   A 1 273 ? 7.42    -11.687 -33.183 1   37.1  ? 258 GLU   A CA  1 
ATOM   2117 C  C   . GLU   A 1 273 ? 7.722   -12.674 -32.071 1   36.93 ? 258 GLU   A C   1 
ATOM   2118 O  O   . GLU   A 1 273 ? 8.249   -12.288 -31.026 1   37.49 ? 258 GLU   A O   1 
ATOM   2119 C  CB  . GLU   A 1 273 ? 8.733   -11.254 -33.827 1   37.27 ? 258 GLU   A CB  1 
ATOM   2120 C  CG  . GLU   A 1 273 ? 8.542   -10.602 -35.179 1   40.33 ? 258 GLU   A CG  1 
ATOM   2121 C  CD  . GLU   A 1 273 ? 9.848   -10.44  -35.923 1   45.06 ? 258 GLU   A CD  1 
ATOM   2122 O  OE1 . GLU   A 1 273 ? 10.724  -9.702  -35.422 1   49.38 ? 258 GLU   A OE1 1 
ATOM   2123 O  OE2 . GLU   A 1 273 ? 10.016  -11.082 -36.983 1   46.56 ? 258 GLU   A OE2 1 
ATOM   2124 N  N   . PHE   A 1 274 ? 7.412   -13.944 -32.303 1   35.87 ? 259 PHE   A N   1 
ATOM   2125 C  CA  . PHE   A 1 274 ? 7.732   -15.017 -31.361 1   35.27 ? 259 PHE   A CA  1 
ATOM   2126 C  C   . PHE   A 1 274 ? 8.232   -16.216 -32.164 1   33.9  ? 259 PHE   A C   1 
ATOM   2127 O  O   . PHE   A 1 274 ? 7.692   -16.52  -33.23  1   33.53 ? 259 PHE   A O   1 
ATOM   2128 C  CB  . PHE   A 1 274 ? 6.512   -15.391 -30.498 1   35.41 ? 259 PHE   A CB  1 
ATOM   2129 C  CG  . PHE   A 1 274 ? 6.087   -14.318 -29.522 1   35.65 ? 259 PHE   A CG  1 
ATOM   2130 C  CD1 . PHE   A 1 274 ? 6.891   -13.986 -28.435 1   36.33 ? 259 PHE   A CD1 1 
ATOM   2131 C  CD2 . PHE   A 1 274 ? 4.923   -13.591 -29.727 1   35.73 ? 259 PHE   A CD2 1 
ATOM   2132 C  CE1 . PHE   A 1 274 ? 6.515   -12.966 -27.552 1   36.81 ? 259 PHE   A CE1 1 
ATOM   2133 C  CE2 . PHE   A 1 274 ? 4.566   -12.556 -28.86  1   36.4  ? 259 PHE   A CE2 1 
ATOM   2134 C  CZ  . PHE   A 1 274 ? 5.359   -12.252 -27.779 1   35.9  ? 259 PHE   A CZ  1 
ATOM   2135 N  N   . ALA   A 1 275 ? 9.278   -16.888 -31.681 1   33.02 ? 260 ALA   A N   1 
ATOM   2136 C  CA  . ALA   A 1 275 ? 9.822   -18.068 -32.359 1   31.61 ? 260 ALA   A CA  1 
ATOM   2137 C  C   . ALA   A 1 275 ? 8.871   -19.256 -32.19  1   30.24 ? 260 ALA   A C   1 
ATOM   2138 O  O   . ALA   A 1 275 ? 8.119   -19.327 -31.213 1   30.73 ? 260 ALA   A O   1 
ATOM   2139 C  CB  . ALA   A 1 275 ? 11.208  -18.411 -31.795 1   31.57 ? 260 ALA   A CB  1 
ATOM   2140 N  N   . GLY   A 1 276 ? 8.861   -20.145 -33.172 1   29.57 ? 261 GLY   A N   1 
ATOM   2141 C  CA  . GLY   A 1 276 ? 8.008   -21.325 -33.137 1   29.93 ? 261 GLY   A CA  1 
ATOM   2142 C  C   . GLY   A 1 276 ? 8.496   -22.327 -32.097 1   29.87 ? 261 GLY   A C   1 
ATOM   2143 O  O   . GLY   A 1 276 ? 9.62    -22.211 -31.582 1   28.85 ? 261 GLY   A O   1 
ATOM   2144 N  N   . GLY   A 1 277 ? 7.648   -23.303 -31.788 1   29.65 ? 262 GLY   A N   1 
ATOM   2145 C  CA  . GLY   A 1 277 ? 7.959   -24.359 -30.83  1   30.96 ? 262 GLY   A CA  1 
ATOM   2146 C  C   . GLY   A 1 277 ? 9.221   -25.111 -31.222 1   31.75 ? 262 GLY   A C   1 
ATOM   2147 O  O   . GLY   A 1 277 ? 9.384   -25.502 -32.378 1   32.5  ? 262 GLY   A O   1 
ATOM   2148 N  N   . SER   A 1 278 ? 10.128  -25.278 -30.279 1   31.17 ? 263 SER   A N   1 
ATOM   2149 C  CA  . SER   A 1 278 ? 11.387  -25.932 -30.526 1   31.04 ? 263 SER   A CA  1 
ATOM   2150 C  C   . SER   A 1 278 ? 11.823  -26.885 -29.401 1   29.88 ? 263 SER   A C   1 
ATOM   2151 O  O   . SER   A 1 278 ? 11.652  -26.547 -28.239 1   29.39 ? 263 SER   A O   1 
ATOM   2152 C  CB  . SER   A 1 278 ? 12.462  -24.875 -30.692 1   33.24 ? 263 SER   A CB  1 
ATOM   2153 O  OG  . SER   A 1 278 ? 13.727  -25.468 -30.957 1   36.36 ? 263 SER   A OG  1 
ATOM   2154 N  N   . ALA   A 1 279 ? 12.493  -28.01  -29.743 1   29.2  ? 264 ALA   A N   1 
ATOM   2155 C  CA  . ALA   A 1 279 ? 13.077  -28.857 -28.698 1   29.23 ? 264 ALA   A CA  1 
ATOM   2156 C  C   . ALA   A 1 279 ? 14.322  -28.163 -28.071 1   29.71 ? 264 ALA   A C   1 
ATOM   2157 O  O   . ALA   A 1 279 ? 14.754  -28.574 -27.019 1   30.29 ? 264 ALA   A O   1 
ATOM   2158 C  CB  . ALA   A 1 279 ? 13.383  -30.239 -29.219 1   28.82 ? 264 ALA   A CB  1 
ATOM   2159 N  N   . GLY   A 1 280 ? 14.784  -27.028 -28.626 1   29.24 ? 265 GLY   A N   1 
ATOM   2160 C  CA  . GLY   A 1 280 ? 15.752  -26.162 -27.966 1   29.55 ? 265 GLY   A CA  1 
ATOM   2161 C  C   . GLY   A 1 280 ? 15.141  -25.555 -26.685 1   29.72 ? 265 GLY   A C   1 
ATOM   2162 O  O   . GLY   A 1 280 ? 15.869  -25.046 -25.832 1   30.57 ? 265 GLY   A O   1 
ATOM   2163 N  N   . GLN   A 1 281 ? 13.793  -25.643 -26.512 1   28.86 ? 266 GLN   A N   1 
ATOM   2164 C  CA  . GLN   A 1 281 ? 13.053  -25.248 -25.319 1   28.6  ? 266 GLN   A CA  1 
ATOM   2165 C  C   . GLN   A 1 281 ? 12.991  -26.397 -24.277 1   29.01 ? 266 GLN   A C   1 
ATOM   2166 O  O   . GLN   A 1 281 ? 12.451  -26.193 -23.195 1   29.46 ? 266 GLN   A O   1 
ATOM   2167 C  CB  . GLN   A 1 281 ? 11.623  -24.767 -25.681 1   29    ? 266 GLN   A CB  1 
ATOM   2168 C  CG  . GLN   A 1 281 ? 11.631  -23.574 -26.625 1   29.41 ? 266 GLN   A CG  1 
ATOM   2169 C  CD  . GLN   A 1 281 ? 10.332  -23.349 -27.348 1   30.3  ? 266 GLN   A CD  1 
ATOM   2170 O  OE1 . GLN   A 1 281 ? 9.451   -24.217 -27.387 1   29.66 ? 266 GLN   A OE1 1 
ATOM   2171 N  NE2 . GLN   A 1 281 ? 10.209  -22.184 -28.019 1   28.83 ? 266 GLN   A NE2 1 
ATOM   2172 N  N   . SER   A 1 282 ? 13.497  -27.61  -24.599 1   29.18 ? 267 SER   A N   1 
ATOM   2173 C  CA  . SER   A 1 282 ? 13.533  -28.698 -23.632 1   29.44 ? 267 SER   A CA  1 
ATOM   2174 C  C   . SER   A 1 282 ? 14.499  -28.33  -22.508 1   29.71 ? 267 SER   A C   1 
ATOM   2175 O  O   . SER   A 1 282 ? 15.66   -27.982 -22.748 1   29.93 ? 267 SER   A O   1 
ATOM   2176 C  CB  . SER   A 1 282 ? 13.967  -30.012 -24.269 1   30.77 ? 267 SER   A CB  1 
ATOM   2177 O  OG  . SER   A 1 282 ? 14.231  -30.993 -23.274 1   32.62 ? 267 SER   A OG  1 
ATOM   2178 N  N   . SER   A 1 283 ? 13.998  -28.386 -21.287 1   29.28 ? 268 SER   A N   1 
ATOM   2179 C  CA  . SER   A 1 283 ? 14.786  -28.07  -20.121 1   29.07 ? 268 SER   A CA  1 
ATOM   2180 C  C   . SER   A 1 283 ? 15.714  -29.212 -19.747 1   29.78 ? 268 SER   A C   1 
ATOM   2181 O  O   . SER   A 1 283 ? 16.777  -28.947 -19.219 1   29.57 ? 268 SER   A O   1 
ATOM   2182 C  CB  . SER   A 1 283 ? 13.876  -27.752 -18.943 1   30.12 ? 268 SER   A CB  1 
ATOM   2183 O  OG  . SER   A 1 283 ? 13.124  -26.562 -19.134 1   31.79 ? 268 SER   A OG  1 
ATOM   2184 N  N   . VAL   A 1 284 ? 15.329  -30.474 -20.003 1   30.47 ? 269 VAL   A N   1 
ATOM   2185 C  CA  . VAL   A 1 284 ? 16.149  -31.605 -19.567 1   30.4  ? 269 VAL   A CA  1 
ATOM   2186 C  C   . VAL   A 1 284 ? 17.496  -31.676 -20.326 1   30.99 ? 269 VAL   A C   1 
ATOM   2187 O  O   . VAL   A 1 284 ? 18.532  -31.908 -19.698 1   30.05 ? 269 VAL   A O   1 
ATOM   2188 C  CB  . VAL   A 1 284 ? 15.373  -32.946 -19.558 1   30.73 ? 269 VAL   A CB  1 
ATOM   2189 C  CG1 . VAL   A 1 284 ? 15.234  -33.541 -20.96  1   30.37 ? 269 VAL   A CG1 1 
ATOM   2190 C  CG2 . VAL   A 1 284 ? 16.039  -33.93  -18.595 1   31.77 ? 269 VAL   A CG2 1 
ATOM   2191 N  N   . PHE   A 1 285 ? 17.506  -31.358 -21.626 1   31.68 ? 270 PHE   A N   1 
ATOM   2192 C  CA  . PHE   A 1 285 ? 18.723  -31.354 -22.415 1   32.99 ? 270 PHE   A CA  1 
ATOM   2193 C  C   . PHE   A 1 285 ? 19.596  -30.168 -22.072 1   32.65 ? 270 PHE   A C   1 
ATOM   2194 O  O   . PHE   A 1 285 ? 20.809  -30.347 -21.931 1   33.38 ? 270 PHE   A O   1 
ATOM   2195 C  CB  . PHE   A 1 285 ? 18.394  -31.401 -23.91  1   34.77 ? 270 PHE   A CB  1 
ATOM   2196 C  CG  . PHE   A 1 285 ? 18.042  -32.811 -24.292 1   36.7  ? 270 PHE   A CG  1 
ATOM   2197 C  CD1 . PHE   A 1 285 ? 16.732  -33.256 -24.226 1   38.05 ? 270 PHE   A CD1 1 
ATOM   2198 C  CD2 . PHE   A 1 285 ? 19.03   -33.717 -24.631 1   38.7  ? 270 PHE   A CD2 1 
ATOM   2199 C  CE1 . PHE   A 1 285 ? 16.416  -34.586 -24.495 1   39.44 ? 270 PHE   A CE1 1 
ATOM   2200 C  CE2 . PHE   A 1 285 ? 18.714  -35.036 -24.917 1   39.99 ? 270 PHE   A CE2 1 
ATOM   2201 C  CZ  . PHE   A 1 285 ? 17.412  -35.465 -24.835 1   39.93 ? 270 PHE   A CZ  1 
ATOM   2202 N  N   . GLN   A 1 286 ? 18.995  -28.979 -21.846 1   30.81 ? 271 GLN   A N   1 
ATOM   2203 C  CA  . GLN   A 1 286 ? 19.784  -27.825 -21.417 1   30.3  ? 271 GLN   A CA  1 
ATOM   2204 C  C   . GLN   A 1 286 ? 20.385  -28.08  -20.01  1   30.25 ? 271 GLN   A C   1 
ATOM   2205 O  O   . GLN   A 1 286 ? 21.507  -27.688 -19.753 1   30.04 ? 271 GLN   A O   1 
ATOM   2206 C  CB  . GLN   A 1 286 ? 18.942  -26.543 -21.413 1   30.67 ? 271 GLN   A CB  1 
ATOM   2207 C  CG  . GLN   A 1 286 ? 18.514  -26.107 -22.817 1   31.34 ? 271 GLN   A CG  1 
ATOM   2208 C  CD  . GLN   A 1 286 ? 18.603  -24.608 -23.011 1   30.6  ? 271 GLN   A CD  1 
ATOM   2209 O  OE1 . GLN   A 1 286 ? 19.36   -23.915 -22.326 1   30.2  ? 271 GLN   A OE1 1 
ATOM   2210 N  NE2 . GLN   A 1 286 ? 17.828  -24.079 -23.956 1   28.53 ? 271 GLN   A NE2 1 
ATOM   2211 N  N   . CYS   A 1 287 ? 19.631  -28.75  -19.135 1   30.54 ? 272 CYS   A N   1 
ATOM   2212 C  CA  . CYS   A 1 287 ? 19.995  -29.112 -17.765 1   31.84 ? 272 CYS   A CA  1 
ATOM   2213 C  C   . CYS   A 1 287 ? 21.302  -29.948 -17.732 1   31.52 ? 272 CYS   A C   1 
ATOM   2214 O  O   . CYS   A 1 287 ? 22.19   -29.621 -16.963 1   30.75 ? 272 CYS   A O   1 
ATOM   2215 C  CB  . CYS   A 1 287 ? 18.808  -29.82  -17.096 1   34.58 ? 272 CYS   A CB  1 
ATOM   2216 S  SG  . CYS   A 1 287 ? 19.222  -30.955 -15.741 1   45.51 ? 272 CYS   A SG  1 
ATOM   2217 N  N   . PHE   A 1 288 ? 21.426  -30.993 -18.572 1   31.82 ? 273 PHE   A N   1 
ATOM   2218 C  CA  . PHE   A 1 288 ? 22.637  -31.825 -18.583 1   31.74 ? 273 PHE   A CA  1 
ATOM   2219 C  C   . PHE   A 1 288 ? 23.808  -31.119 -19.241 1   31.14 ? 273 PHE   A C   1 
ATOM   2220 O  O   . PHE   A 1 288 ? 24.935  -31.333 -18.81  1   31.14 ? 273 PHE   A O   1 
ATOM   2221 C  CB  . PHE   A 1 288 ? 22.361  -33.221 -19.158 1   32.18 ? 273 PHE   A CB  1 
ATOM   2222 C  CG  . PHE   A 1 288 ? 21.574  -33.949 -18.098 1   33.76 ? 273 PHE   A CG  1 
ATOM   2223 C  CD1 . PHE   A 1 288 ? 22.145  -34.229 -16.867 1   35.2  ? 273 PHE   A CD1 1 
ATOM   2224 C  CD2 . PHE   A 1 288 ? 20.221  -34.183 -18.256 1   35.07 ? 273 PHE   A CD2 1 
ATOM   2225 C  CE1 . PHE   A 1 288 ? 21.393  -34.8   -15.841 1   36.63 ? 273 PHE   A CE1 1 
ATOM   2226 C  CE2 . PHE   A 1 288 ? 19.472  -34.771 -17.242 1   36.53 ? 273 PHE   A CE2 1 
ATOM   2227 C  CZ  . PHE   A 1 288 ? 20.05   -35.044 -16.027 1   36.59 ? 273 PHE   A CZ  1 
ATOM   2228 N  N   . ASP   A 1 289 ? 23.567  -30.204 -20.191 1   30.77 ? 274 ASP   A N   1 
ATOM   2229 C  CA  . ASP   A 1 289 ? 24.667  -29.418 -20.779 1   31.16 ? 274 ASP   A CA  1 
ATOM   2230 C  C   . ASP   A 1 289 ? 25.199  -28.441 -19.725 1   30.97 ? 274 ASP   A C   1 
ATOM   2231 O  O   . ASP   A 1 289 ? 26.412  -28.211 -19.665 1   30.75 ? 274 ASP   A O   1 
ATOM   2232 C  CB  . ASP   A 1 289 ? 24.207  -28.637 -22.006 1   32.62 ? 274 ASP   A CB  1 
ATOM   2233 C  CG  . ASP   A 1 289 ? 24.053  -29.477 -23.266 1   37.56 ? 274 ASP   A CG  1 
ATOM   2234 O  OD1 . ASP   A 1 289 ? 24.766  -30.475 -23.401 1   37.62 ? 274 ASP   A OD1 1 
ATOM   2235 O  OD2 . ASP   A 1 289 ? 23.229  -29.112 -24.124 1   40.9  ? 274 ASP   A OD2 1 
ATOM   2236 N  N   . VAL   A 1 290 ? 24.301  -27.854 -18.903 1   30.57 ? 275 VAL   A N   1 
ATOM   2237 C  CA  . VAL   A 1 290 ? 24.743  -26.941 -17.848 1   31.26 ? 275 VAL   A CA  1 
ATOM   2238 C  C   . VAL   A 1 290 ? 25.488  -27.756 -16.777 1   31.17 ? 275 VAL   A C   1 
ATOM   2239 O  O   . VAL   A 1 290 ? 26.592  -27.404 -16.399 1   31.77 ? 275 VAL   A O   1 
ATOM   2240 C  CB  . VAL   A 1 290 ? 23.575  -26.135 -17.216 1   32.77 ? 275 VAL   A CB  1 
ATOM   2241 C  CG1 . VAL   A 1 290 ? 24.036  -25.412 -15.946 1   33.93 ? 275 VAL   A CG1 1 
ATOM   2242 C  CG2 . VAL   A 1 290 ? 22.984  -25.154 -18.215 1   33.21 ? 275 VAL   A CG2 1 
ATOM   2243 N  N   . LEU   A 1 291 ? 24.894  -28.855 -16.313 1   31.24 ? 276 LEU   A N   1 
ATOM   2244 C  CA  . LEU   A 1 291 ? 25.498  -29.718 -15.297 1   32.22 ? 276 LEU   A CA  1 
ATOM   2245 C  C   . LEU   A 1 291 ? 26.908  -30.169 -15.678 1   33.33 ? 276 LEU   A C   1 
ATOM   2246 O  O   . LEU   A 1 291 ? 27.821  -30.068 -14.86  1   33.96 ? 276 LEU   A O   1 
ATOM   2247 C  CB  . LEU   A 1 291 ? 24.606  -30.946 -15.035 1   31.84 ? 276 LEU   A CB  1 
ATOM   2248 C  CG  . LEU   A 1 291 ? 25.143  -31.968 -14.02  1   33.8  ? 276 LEU   A CG  1 
ATOM   2249 C  CD1 . LEU   A 1 291 ? 24.964  -31.468 -12.597 1   34.57 ? 276 LEU   A CD1 1 
ATOM   2250 C  CD2 . LEU   A 1 291 ? 24.44   -33.331 -14.179 1   34.55 ? 276 LEU   A CD2 1 
ATOM   2251 N  N   . LEU   A 1 292 ? 27.103  -30.588 -16.936 1   32.84 ? 277 LEU   A N   1 
ATOM   2252 C  CA  . LEU   A 1 292 ? 28.392  -31.097 -17.38  1   32.92 ? 277 LEU   A CA  1 
ATOM   2253 C  C   . LEU   A 1 292 ? 29.36   -30.045 -17.933 1   34.11 ? 277 LEU   A C   1 
ATOM   2254 O  O   . LEU   A 1 292 ? 30.432  -30.402 -18.412 1   34.26 ? 277 LEU   A O   1 
ATOM   2255 C  CB  . LEU   A 1 292 ? 28.177  -32.213 -18.399 1   32.6  ? 277 LEU   A CB  1 
ATOM   2256 C  CG  . LEU   A 1 292 ? 27.365  -33.389 -17.88  1   33.38 ? 277 LEU   A CG  1 
ATOM   2257 C  CD1 . LEU   A 1 292 ? 26.993  -34.315 -18.993 1   34.23 ? 277 LEU   A CD1 1 
ATOM   2258 C  CD2 . LEU   A 1 292 ? 28.085  -34.121 -16.753 1   33.59 ? 277 LEU   A CD2 1 
ATOM   2259 N  N   . GLY   A 1 293 ? 29.014  -28.765 -17.825 1   34.61 ? 278 GLY   A N   1 
ATOM   2260 C  CA  . GLY   A 1 293 ? 29.895  -27.693 -18.276 1   35.84 ? 278 GLY   A CA  1 
ATOM   2261 C  C   . GLY   A 1 293 ? 30.098  -27.627 -19.776 1   37.42 ? 278 GLY   A C   1 
ATOM   2262 O  O   . GLY   A 1 293 ? 31.096  -27.083 -20.25  1   37.6  ? 278 GLY   A O   1 
ATOM   2263 N  N   . ILE   A 1 294 ? 29.16   -28.197 -20.543 1   38.64 ? 279 ILE   A N   1 
ATOM   2264 C  CA  . ILE   A 1 294 ? 29.202  -28.123 -22     1   40.83 ? 279 ILE   A CA  1 
ATOM   2265 C  C   . ILE   A 1 294 ? 28.581  -26.769 -22.244 1   45.48 ? 279 ILE   A C   1 
ATOM   2266 O  O   . ILE   A 1 294 ? 27.367  -26.624 -22.081 1   47.09 ? 279 ILE   A O   1 
ATOM   2267 C  CB  . ILE   A 1 294 ? 28.338  -29.258 -22.591 1   39.53 ? 279 ILE   A CB  1 
ATOM   2268 C  CG1 . ILE   A 1 294 ? 28.923  -30.636 -22.189 1   39.69 ? 279 ILE   A CG1 1 
ATOM   2269 C  CG2 . ILE   A 1 294 ? 28.257  -29.114 -24.101 1   38.94 ? 279 ILE   A CG2 1 
ATOM   2270 C  CD1 . ILE   A 1 294 ? 27.937  -31.671 -22.16  1   41.23 ? 279 ILE   A CD1 1 
ATOM   2271 N  N   . GLN   A 1 295 ? 29.405  -25.75  -22.458 1   47.63 ? 280 GLN   A N   1 
ATOM   2272 C  CA  . GLN   A 1 295 ? 28.907  -24.377 -22.513 1   49.64 ? 280 GLN   A CA  1 
ATOM   2273 C  C   . GLN   A 1 295 ? 28.24   -24.054 -23.817 1   50.02 ? 280 GLN   A C   1 
ATOM   2274 O  O   . GLN   A 1 295 ? 28.767  -23.29  -24.626 1   50.09 ? 280 GLN   A O   1 
ATOM   2275 C  CB  . GLN   A 1 295 ? 30.009  -23.381 -22.159 1   53.07 ? 280 GLN   A CB  1 
ATOM   2276 C  CG  . GLN   A 1 295 ? 30.445  -23.551 -20.705 1   59.63 ? 280 GLN   A CG  1 
ATOM   2277 C  CD  . GLN   A 1 295 ? 31.388  -22.484 -20.21  1   67.39 ? 280 GLN   A CD  1 
ATOM   2278 O  OE1 . GLN   A 1 295 ? 31.402  -22.158 -19.015 1   70.18 ? 280 GLN   A OE1 1 
ATOM   2279 N  NE2 . GLN   A 1 295 ? 32.2    -21.918 -21.101 1   68.41 ? 280 GLN   A NE2 1 
ATOM   2280 N  N   . GLN   A 1 296 ? 27.054  -24.644 -24.012 1   49.97 ? 281 GLN   A N   1 
ATOM   2281 C  CA  . GLN   A 1 296 ? 26.258  -24.448 -25.218 1   50.24 ? 281 GLN   A CA  1 
ATOM   2282 C  C   . GLN   A 1 296 ? 25.849  -23.009 -25.377 1   51.56 ? 281 GLN   A C   1 
ATOM   2283 O  O   . GLN   A 1 296 ? 25.733  -22.578 -26.498 1   51.95 ? 281 GLN   A O   1 
ATOM   2284 C  CB  . GLN   A 1 296 ? 24.988  -25.326 -25.219 1   49.49 ? 281 GLN   A CB  1 
ATOM   2285 C  CG  . GLN   A 1 296 ? 25.229  -26.806 -25.202 1   49.26 ? 281 GLN   A CG  1 
ATOM   2286 C  CD  . GLN   A 1 296 ? 25.784  -27.375 -26.476 1   49.91 ? 281 GLN   A CD  1 
ATOM   2287 O  OE1 . GLN   A 1 296 ? 26.11   -26.667 -27.433 1   50.9  ? 281 GLN   A OE1 1 
ATOM   2288 N  NE2 . GLN   A 1 296 ? 25.913  -28.691 -26.506 1   49.13 ? 281 GLN   A NE2 1 
ATOM   2289 N  N   . THR   A 1 297 ? 25.622  -22.277 -24.28  1   52.77 ? 282 THR   A N   1 
ATOM   2290 C  CA  . THR   A 1 297 ? 25.181  -20.881 -24.295 1   54.78 ? 282 THR   A CA  1 
ATOM   2291 C  C   . THR   A 1 297 ? 26.307  -19.84  -24.217 1   56.56 ? 282 THR   A C   1 
ATOM   2292 O  O   . THR   A 1 297 ? 26.017  -18.643 -24.16  1   56.89 ? 282 THR   A O   1 
ATOM   2293 C  CB  . THR   A 1 297 ? 24.173  -20.661 -23.178 1   55.72 ? 282 THR   A CB  1 
ATOM   2294 O  OG1 . THR   A 1 297 ? 24.767  -21.064 -21.942 1   56.01 ? 282 THR   A OG1 1 
ATOM   2295 C  CG2 . THR   A 1 297 ? 22.889  -21.432 -23.405 1   56.25 ? 282 THR   A CG2 1 
ATOM   2296 N  N   . ALA   A 1 298 ? 27.573  -20.273 -24.219 1   57.58 ? 283 ALA   A N   1 
ATOM   2297 C  CA  . ALA   A 1 298 ? 28.697  -19.338 -24.161 1   58.78 ? 283 ALA   A CA  1 
ATOM   2298 C  C   . ALA   A 1 298 ? 29.125  -18.881 -25.555 1   59.68 ? 283 ALA   A C   1 
ATOM   2299 O  O   . ALA   A 1 298 ? 28.967  -19.618 -26.529 1   59.44 ? 283 ALA   A O   1 
ATOM   2300 C  CB  . ALA   A 1 298 ? 29.874  -19.975 -23.45  1   59    ? 283 ALA   A CB  1 
ATOM   2301 N  N   . GLY   A 1 299 ? 29.684  -17.673 -25.625 1   60.51 ? 284 GLY   A N   1 
ATOM   2302 C  CA  . GLY   A 1 299 ? 30.155  -17.083 -26.873 1   61.47 ? 284 GLY   A CA  1 
ATOM   2303 C  C   . GLY   A 1 299 ? 29.084  -16.284 -27.59  1   61.83 ? 284 GLY   A C   1 
ATOM   2304 O  O   . GLY   A 1 299 ? 27.937  -16.198 -27.13  1   62.22 ? 284 GLY   A O   1 
ATOM   2305 N  N   . GLY   A 1 300 ? 29.46   -15.709 -28.714 1   61.4  ? 285 GLY   A N   1 
ATOM   2306 C  CA  . GLY   A 1 300 ? 28.517  -14.93  -29.5   1   61.16 ? 285 GLY   A CA  1 
ATOM   2307 C  C   . GLY   A 1 300 ? 27.893  -15.673 -30.662 1   60.09 ? 285 GLY   A C   1 
ATOM   2308 O  O   . GLY   A 1 300 ? 27.236  -15.039 -31.492 1   61.22 ? 285 GLY   A O   1 
ATOM   2309 N  N   . GLY   A 1 301 ? 28.1    -16.992 -30.739 1   57.7  ? 286 GLY   A N   1 
ATOM   2310 C  CA  . GLY   A 1 301 ? 27.58   -17.802 -31.834 1   55.86 ? 286 GLY   A CA  1 
ATOM   2311 C  C   . GLY   A 1 301 ? 26.069  -17.86  -31.897 1   53.81 ? 286 GLY   A C   1 
ATOM   2312 O  O   . GLY   A 1 301 ? 25.401  -17.636 -30.888 1   53.56 ? 286 GLY   A O   1 
ATOM   2313 N  N   . HIS   A 1 302 ? 25.518  -18.179 -33.072 1   52.28 ? 287 HIS   A N   1 
ATOM   2314 C  CA  . HIS   A 1 302 ? 24.071  -18.27  -33.236 1   51.39 ? 287 HIS   A CA  1 
ATOM   2315 C  C   . HIS   A 1 302 ? 23.453  -19.396 -32.407 1   48.2  ? 287 HIS   A C   1 
ATOM   2316 O  O   . HIS   A 1 302 ? 22.36   -19.204 -31.89  1   47.58 ? 287 HIS   A O   1 
ATOM   2317 C  CB  . HIS   A 1 302 ? 23.692  -18.463 -34.707 1   53.97 ? 287 HIS   A CB  1 
ATOM   2318 C  CG  . HIS   A 1 302 ? 24.109  -17.332 -35.586 1   60.13 ? 287 HIS   A CG  1 
ATOM   2319 N  ND1 . HIS   A 1 302 ? 25.036  -17.509 -36.602 1   62.86 ? 287 HIS   A ND1 1 
ATOM   2320 C  CD2 . HIS   A 1 302 ? 23.708  -16.04  -35.575 1   62.32 ? 287 HIS   A CD2 1 
ATOM   2321 C  CE1 . HIS   A 1 302 ? 25.165  -16.324 -37.178 1   63.66 ? 287 HIS   A CE1 1 
ATOM   2322 N  NE2 . HIS   A 1 302 ? 24.387  -15.408 -36.595 1   63.78 ? 287 HIS   A NE2 1 
ATOM   2323 N  N   . ALA   A 1 303 ? 24.141  -20.563 -32.295 1   45.75 ? 288 ALA   A N   1 
ATOM   2324 C  CA  . ALA   A 1 303 ? 23.632  -21.726 -31.574 1   44.16 ? 288 ALA   A CA  1 
ATOM   2325 C  C   . ALA   A 1 303 ? 23.45   -21.398 -30.103 1   42.41 ? 288 ALA   A C   1 
ATOM   2326 O  O   . ALA   A 1 303 ? 22.398  -21.687 -29.537 1   42.7  ? 288 ALA   A O   1 
ATOM   2327 C  CB  . ALA   A 1 303 ? 24.563  -22.928 -31.767 1   43.97 ? 288 ALA   A CB  1 
ATOM   2328 N  N   . ALA   A 1 304 ? 24.452  -20.725 -29.514 1   40.71 ? 289 ALA   A N   1 
ATOM   2329 C  CA  . ALA   A 1 304 ? 24.456  -20.26  -28.132 1   39.41 ? 289 ALA   A CA  1 
ATOM   2330 C  C   . ALA   A 1 304 ? 23.326  -19.271 -27.875 1   38.18 ? 289 ALA   A C   1 
ATOM   2331 O  O   . ALA   A 1 304 ? 22.601  -19.39  -26.888 1   37.68 ? 289 ALA   A O   1 
ATOM   2332 C  CB  . ALA   A 1 304 ? 25.813  -19.622 -27.804 1   39.23 ? 289 ALA   A CB  1 
ATOM   2333 N  N   . GLN   A 1 305 ? 23.169  -18.29  -28.765 1   37.7  ? 290 GLN   A N   1 
ATOM   2334 C  CA  . GLN   A 1 305 ? 22.155  -17.266 -28.61  1   36.56 ? 290 GLN   A CA  1 
ATOM   2335 C  C   . GLN   A 1 305 ? 20.761  -17.89  -28.714 1   35.07 ? 290 GLN   A C   1 
ATOM   2336 O  O   . GLN   A 1 305 ? 19.879  -17.522 -27.95  1   35.36 ? 290 GLN   A O   1 
ATOM   2337 C  CB  . GLN   A 1 305 ? 22.357  -16.158 -29.665 1   37.26 ? 290 GLN   A CB  1 
ATOM   2338 C  CG  . GLN   A 1 305 ? 21.35   -15.027 -29.534 1   39.59 ? 290 GLN   A CG  1 
ATOM   2339 C  CD  . GLN   A 1 305 ? 21.613  -14.229 -28.279 1   44.95 ? 290 GLN   A CD  1 
ATOM   2340 O  OE1 . GLN   A 1 305 ? 22.742  -13.807 -28.011 1   47.87 ? 290 GLN   A OE1 1 
ATOM   2341 N  NE2 . GLN   A 1 305 ? 20.588  -14.018 -27.468 1   43.6  ? 290 GLN   A NE2 1 
ATOM   2342 N  N   . PHE   A 1 306 ? 20.574  -18.855 -29.611 1   34.1  ? 291 PHE   A N   1 
ATOM   2343 C  CA  . PHE   A 1 306 ? 19.283  -19.514 -29.78  1   33.4  ? 291 PHE   A CA  1 
ATOM   2344 C  C   . PHE   A 1 306 ? 18.885  -20.288 -28.513 1   32.57 ? 291 PHE   A C   1 
ATOM   2345 O  O   . PHE   A 1 306 ? 17.767  -20.133 -28.032 1   32.11 ? 291 PHE   A O   1 
ATOM   2346 C  CB  . PHE   A 1 306 ? 19.277  -20.429 -31.02  1   33.46 ? 291 PHE   A CB  1 
ATOM   2347 C  CG  . PHE   A 1 306 ? 17.977  -21.18  -31.2   1   34.46 ? 291 PHE   A CG  1 
ATOM   2348 C  CD1 . PHE   A 1 306 ? 16.816  -20.513 -31.596 1   35.14 ? 291 PHE   A CD1 1 
ATOM   2349 C  CD2 . PHE   A 1 306 ? 17.897  -22.541 -30.929 1   35.31 ? 291 PHE   A CD2 1 
ATOM   2350 C  CE1 . PHE   A 1 306 ? 15.612  -21.202 -31.739 1   35.97 ? 291 PHE   A CE1 1 
ATOM   2351 C  CE2 . PHE   A 1 306 ? 16.691  -23.23  -31.077 1   35.55 ? 291 PHE   A CE2 1 
ATOM   2352 C  CZ  . PHE   A 1 306 ? 15.559  -22.559 -31.484 1   35.64 ? 291 PHE   A CZ  1 
ATOM   2353 N  N   . LEU   A 1 307 ? 19.795  -21.113 -27.969 1   32.02 ? 292 LEU   A N   1 
ATOM   2354 C  CA  . LEU   A 1 307 ? 19.492  -21.892 -26.773 1   31.87 ? 292 LEU   A CA  1 
ATOM   2355 C  C   . LEU   A 1 307 ? 19.251  -20.994 -25.569 1   32.57 ? 292 LEU   A C   1 
ATOM   2356 O  O   . LEU   A 1 307 ? 18.388  -21.305 -24.739 1   33.05 ? 292 LEU   A O   1 
ATOM   2357 C  CB  . LEU   A 1 307 ? 20.594  -22.949 -26.51  1   32.73 ? 292 LEU   A CB  1 
ATOM   2358 C  CG  . LEU   A 1 307 ? 20.602  -24.101 -27.512 1   34.85 ? 292 LEU   A CG  1 
ATOM   2359 C  CD1 . LEU   A 1 307 ? 21.915  -24.964 -27.419 1   36.45 ? 292 LEU   A CD1 1 
ATOM   2360 C  CD2 . LEU   A 1 307 ? 19.354  -24.947 -27.394 1   35.9  ? 292 LEU   A CD2 1 
ATOM   2361 N  N   . GLN   A 1 308 ? 19.978  -19.857 -25.479 1   32.41 ? 293 GLN   A N   1 
ATOM   2362 C  CA  . GLN   A 1 308 ? 19.744  -18.925 -24.385 1   33.26 ? 293 GLN   A CA  1 
ATOM   2363 C  C   . GLN   A 1 308 ? 18.359  -18.286 -24.536 1   32.03 ? 293 GLN   A C   1 
ATOM   2364 O  O   . GLN   A 1 308 ? 17.601  -18.248 -23.579 1   32.4  ? 293 GLN   A O   1 
ATOM   2365 C  CB  . GLN   A 1 308 ? 20.833  -17.848 -24.36  1   37.85 ? 293 GLN   A CB  1 
ATOM   2366 C  CG  . GLN   A 1 308 ? 20.689  -16.89  -23.191 1   44.58 ? 293 GLN   A CG  1 
ATOM   2367 C  CD  . GLN   A 1 308 ? 20.815  -17.556 -21.836 1   51.85 ? 293 GLN   A CD  1 
ATOM   2368 O  OE1 . GLN   A 1 308 ? 20.074  -17.247 -20.881 1   54.58 ? 293 GLN   A OE1 1 
ATOM   2369 N  NE2 . GLN   A 1 308 ? 21.764  -18.464 -21.712 1   51.59 ? 293 GLN   A NE2 1 
ATOM   2370 N  N   . ASP   A 1 309 ? 18.004  -17.836 -25.745 1   31.17 ? 294 ASP   A N   1 
ATOM   2371 C  CA  . ASP   A 1 309 ? 16.7    -17.229 -25.993 1   30.56 ? 294 ASP   A CA  1 
ATOM   2372 C  C   . ASP   A 1 309 ? 15.557  -18.2   -25.719 1   29.6  ? 294 ASP   A C   1 
ATOM   2373 O  O   . ASP   A 1 309 ? 14.498  -17.761 -25.276 1   28.35 ? 294 ASP   A O   1 
ATOM   2374 C  CB  . ASP   A 1 309 ? 16.585  -16.738 -27.444 1   33.17 ? 294 ASP   A CB  1 
ATOM   2375 C  CG  . ASP   A 1 309 ? 17.473  -15.565 -27.793 1   38.47 ? 294 ASP   A CG  1 
ATOM   2376 O  OD1 . ASP   A 1 309 ? 18.023  -14.929 -26.849 1   38.58 ? 294 ASP   A OD1 1 
ATOM   2377 O  OD2 . ASP   A 1 309 ? 17.64   -15.294 -29.004 1   40.24 ? 294 ASP   A OD2 1 
ATOM   2378 N  N   . MET   A 1 310 ? 15.757  -19.51  -26.005 1   29.14 ? 295 MET   A N   1 
ATOM   2379 C  CA  . MET   A 1 310 ? 14.704  -20.495 -25.774 1   29.84 ? 295 MET   A CA  1 
ATOM   2380 C  C   . MET   A 1 310 ? 14.346  -20.703 -24.328 1   30.47 ? 295 MET   A C   1 
ATOM   2381 O  O   . MET   A 1 310 ? 13.268  -21.213 -24.081 1   30.58 ? 295 MET   A O   1 
ATOM   2382 C  CB  . MET   A 1 310 ? 15.017  -21.829 -26.457 1   30.35 ? 295 MET   A CB  1 
ATOM   2383 C  CG  . MET   A 1 310 ? 14.946  -21.744 -27.978 1   31.51 ? 295 MET   A CG  1 
ATOM   2384 S  SD  . MET   A 1 310 ? 13.405  -21.035 -28.674 1   34.04 ? 295 MET   A SD  1 
ATOM   2385 C  CE  . MET   A 1 310 ? 13.949  -19.286 -29.048 1   30.39 ? 295 MET   A CE  1 
ATOM   2386 N  N   . ARG   A 1 311 ? 15.183  -20.246 -23.366 1   30.91 ? 296 ARG   A N   1 
ATOM   2387 C  CA  . ARG   A 1 311 ? 14.865  -20.348 -21.941 1   32.12 ? 296 ARG   A CA  1 
ATOM   2388 C  C   . ARG   A 1 311 ? 13.681  -19.501 -21.544 1   33.81 ? 296 ARG   A C   1 
ATOM   2389 O  O   . ARG   A 1 311 ? 12.911  -19.891 -20.663 1   33.97 ? 296 ARG   A O   1 
ATOM   2390 C  CB  . ARG   A 1 311 ? 16.076  -20.002 -21.077 1   33.48 ? 296 ARG   A CB  1 
ATOM   2391 C  CG  . ARG   A 1 311 ? 17.233  -20.935 -21.347 1   35.98 ? 296 ARG   A CG  1 
ATOM   2392 C  CD  . ARG   A 1 311 ? 18.287  -20.767 -20.299 1   38.12 ? 296 ARG   A CD  1 
ATOM   2393 N  NE  . ARG   A 1 311 ? 19.387  -21.715 -20.492 1   39.96 ? 296 ARG   A NE  1 
ATOM   2394 C  CZ  . ARG   A 1 311 ? 20.47   -21.763 -19.727 1   42.05 ? 296 ARG   A CZ  1 
ATOM   2395 N  NH1 . ARG   A 1 311 ? 20.615  -20.916 -18.713 1   41.31 ? 296 ARG   A NH1 1 
ATOM   2396 N  NH2 . ARG   A 1 311 ? 21.426  -22.644 -19.979 1   41.25 ? 296 ARG   A NH2 1 
ATOM   2397 N  N   . ARG   A 1 312 ? 13.483  -18.36  -22.22  1   35.29 ? 297 ARG   A N   1 
ATOM   2398 C  CA  . ARG   A 1 312 ? 12.29   -17.526 -21.957 1   35.82 ? 297 ARG   A CA  1 
ATOM   2399 C  C   . ARG   A 1 312 ? 10.997  -18.153 -22.517 1   34.04 ? 297 ARG   A C   1 
ATOM   2400 O  O   . ARG   A 1 312 ? 9.922   -17.623 -22.321 1   34.12 ? 297 ARG   A O   1 
ATOM   2401 C  CB  . ARG   A 1 312 ? 12.502  -16.092 -22.473 1   39.9  ? 297 ARG   A CB  1 
ATOM   2402 C  CG  . ARG   A 1 312 ? 13.565  -15.323 -21.665 1   45.53 ? 297 ARG   A CG  1 
ATOM   2403 C  CD  . ARG   A 1 312 ? 13.029  -14.823 -20.33  1   49.75 ? 297 ARG   A CD  1 
ATOM   2404 N  NE  . ARG   A 1 312 ? 14.079  -14.229 -19.495 1   53.15 ? 297 ARG   A NE  1 
ATOM   2405 C  CZ  . ARG   A 1 312 ? 13.906  -13.862 -18.226 1   56.72 ? 297 ARG   A CZ  1 
ATOM   2406 N  NH1 . ARG   A 1 312 ? 12.717  -13.987 -17.644 1   57.2  ? 297 ARG   A NH1 1 
ATOM   2407 N  NH2 . ARG   A 1 312 ? 14.914  -13.338 -17.536 1   55.9  ? 297 ARG   A NH2 1 
ATOM   2408 N  N   . TYR   A 1 313 ? 11.099  -19.279 -23.218 1   32.46 ? 298 TYR   A N   1 
ATOM   2409 C  CA  . TYR   A 1 313 ? 9.955   -20.03  -23.733 1   31.43 ? 298 TYR   A CA  1 
ATOM   2410 C  C   . TYR   A 1 313 ? 9.668   -21.282 -22.898 1   30.77 ? 298 TYR   A C   1 
ATOM   2411 O  O   . TYR   A 1 313 ? 8.788   -22.061 -23.258 1   30.88 ? 298 TYR   A O   1 
ATOM   2412 C  CB  . TYR   A 1 313 ? 10.2    -20.453 -25.177 1   30.94 ? 298 TYR   A CB  1 
ATOM   2413 C  CG  . TYR   A 1 313 ? 10.216  -19.308 -26.158 1   31.59 ? 298 TYR   A CG  1 
ATOM   2414 C  CD1 . TYR   A 1 313 ? 11.271  -18.406 -26.188 1   32.36 ? 298 TYR   A CD1 1 
ATOM   2415 C  CD2 . TYR   A 1 313 ? 9.21    -19.165 -27.102 1   32.62 ? 298 TYR   A CD2 1 
ATOM   2416 C  CE1 . TYR   A 1 313 ? 11.289  -17.348 -27.089 1   33.29 ? 298 TYR   A CE1 1 
ATOM   2417 C  CE2 . TYR   A 1 313 ? 9.245   -18.149 -28.046 1   32.74 ? 298 TYR   A CE2 1 
ATOM   2418 C  CZ  . TYR   A 1 313 ? 10.266  -17.223 -28.017 1   33.69 ? 298 TYR   A CZ  1 
ATOM   2419 O  OH  . TYR   A 1 313 ? 10.297  -16.225 -28.966 1   34.29 ? 298 TYR   A OH  1 
ATOM   2420 N  N   . MET   A 1 314 ? 10.394  -21.468 -21.793 1   29.71 ? 299 MET   A N   1 
ATOM   2421 C  CA  . MET   A 1 314 ? 10.205  -22.558 -20.858 1   30.39 ? 299 MET   A CA  1 
ATOM   2422 C  C   . MET   A 1 314 ? 9.344   -22.052 -19.713 1   30.31 ? 299 MET   A C   1 
ATOM   2423 O  O   . MET   A 1 314 ? 9.414   -20.863 -19.38  1   30.73 ? 299 MET   A O   1 
ATOM   2424 C  CB  . MET   A 1 314 ? 11.582  -22.958 -20.269 1   30.44 ? 299 MET   A CB  1 
ATOM   2425 C  CG  . MET   A 1 314 ? 12.584  -23.395 -21.306 1   32.52 ? 299 MET   A CG  1 
ATOM   2426 S  SD  . MET   A 1 314 ? 14.137  -23.925 -20.47  1   31.51 ? 299 MET   A SD  1 
ATOM   2427 C  CE  . MET   A 1 314 ? 15.087  -24.46  -21.847 1   24.49 ? 299 MET   A CE  1 
ATOM   2428 N  N   . PRO   A 1 315 ? 8.632   -22.938 -18.989 1   29.75 ? 300 PRO   A N   1 
ATOM   2429 C  CA  . PRO   A 1 315 ? 7.917   -22.491 -17.784 1   30    ? 300 PRO   A CA  1 
ATOM   2430 C  C   . PRO   A 1 315 ? 8.88    -21.826 -16.801 1   30.66 ? 300 PRO   A C   1 
ATOM   2431 O  O   . PRO   A 1 315 ? 10.066  -22.173 -16.761 1   29.94 ? 300 PRO   A O   1 
ATOM   2432 C  CB  . PRO   A 1 315 ? 7.322   -23.79  -17.224 1   30.54 ? 300 PRO   A CB  1 
ATOM   2433 C  CG  . PRO   A 1 315 ? 7.209   -24.693 -18.403 1   30.79 ? 300 PRO   A CG  1 
ATOM   2434 C  CD  . PRO   A 1 315 ? 8.452   -24.385 -19.203 1   28.97 ? 300 PRO   A CD  1 
ATOM   2435 N  N   . PRO   A 1 316 ? 8.426   -20.76  -16.125 1   32.07 ? 301 PRO   A N   1 
ATOM   2436 C  CA  . PRO   A 1 316 ? 9.342   -19.982 -15.282 1   31.98 ? 301 PRO   A CA  1 
ATOM   2437 C  C   . PRO   A 1 316 ? 10.09   -20.804 -14.234 1   32.81 ? 301 PRO   A C   1 
ATOM   2438 O  O   . PRO   A 1 316 ? 11.266  -20.588 -14.095 1   33.6  ? 301 PRO   A O   1 
ATOM   2439 C  CB  . PRO   A 1 316 ? 8.45    -18.877 -14.67  1   32.55 ? 301 PRO   A CB  1 
ATOM   2440 C  CG  . PRO   A 1 316 ? 7.068   -19.286 -14.924 1   33.71 ? 301 PRO   A CG  1 
ATOM   2441 C  CD  . PRO   A 1 316 ? 7.083   -20.154 -16.169 1   31.73 ? 301 PRO   A CD  1 
ATOM   2442 N  N   . ALA   A 1 317 ? 9.454   -21.776 -13.58  1   33.63 ? 302 ALA   A N   1 
ATOM   2443 C  CA  . ALA   A 1 317 ? 10.129  -22.604 -12.577 1   34.33 ? 302 ALA   A CA  1 
ATOM   2444 C  C   . ALA   A 1 317 ? 11.275  -23.415 -13.211 1   34.57 ? 302 ALA   A C   1 
ATOM   2445 O  O   . ALA   A 1 317 ? 12.297  -23.613 -12.572 1   35.49 ? 302 ALA   A O   1 
ATOM   2446 C  CB  . ALA   A 1 317 ? 9.139   -23.542 -11.918 1   34.17 ? 302 ALA   A CB  1 
ATOM   2447 N  N   . HIS   A 1 318 ? 11.125  -23.83  -14.489 1   33.23 ? 303 HIS   A N   1 
ATOM   2448 C  CA  . HIS   A 1 318 ? 12.137  -24.613 -15.214 1   31.56 ? 303 HIS   A CA  1 
ATOM   2449 C  C   . HIS   A 1 318 ? 13.293  -23.76  -15.699 1   31.37 ? 303 HIS   A C   1 
ATOM   2450 O  O   . HIS   A 1 318 ? 14.449  -24.187 -15.689 1   30.39 ? 303 HIS   A O   1 
ATOM   2451 C  CB  . HIS   A 1 318 ? 11.478  -25.407 -16.352 1   30.47 ? 303 HIS   A CB  1 
ATOM   2452 C  CG  . HIS   A 1 318 ? 10.389  -26.332 -15.9   1   30.1  ? 303 HIS   A CG  1 
ATOM   2453 N  ND1 . HIS   A 1 318 ? 9.563   -26.961 -16.812 1   31.4  ? 303 HIS   A ND1 1 
ATOM   2454 C  CD2 . HIS   A 1 318 ? 10.048  -26.742 -14.648 1   31.17 ? 303 HIS   A CD2 1 
ATOM   2455 C  CE1 . HIS   A 1 318 ? 8.747   -27.719 -16.092 1   32.31 ? 303 HIS   A CE1 1 
ATOM   2456 N  NE2 . HIS   A 1 318 ? 9.007   -27.616 -14.781 1   32.08 ? 303 HIS   A NE2 1 
ATOM   2457 N  N   . ARG   A 1 319 ? 12.992  -22.541 -16.086 1   32.2  ? 304 ARG   A N   1 
ATOM   2458 C  CA  . ARG   A 1 319 ? 13.97   -21.528 -16.452 1   34.4  ? 304 ARG   A CA  1 
ATOM   2459 C  C   . ARG   A 1 319 ? 14.796  -21.188 -15.18  1   35.41 ? 304 ARG   A C   1 
ATOM   2460 O  O   . ARG   A 1 319 ? 16.024  -21.048 -15.262 1   36.07 ? 304 ARG   A O   1 
ATOM   2461 C  CB  . ARG   A 1 319 ? 13.172  -20.297 -16.904 1   37.11 ? 304 ARG   A CB  1 
ATOM   2462 C  CG  . ARG   A 1 319 ? 13.943  -19.079 -17.439 1   42.75 ? 304 ARG   A CG  1 
ATOM   2463 C  CD  . ARG   A 1 319 ? 12.954  -17.925 -17.77  1   47.67 ? 304 ARG   A CD  1 
ATOM   2464 N  NE  . ARG   A 1 319 ? 11.635  -18.411 -18.219 1   51.05 ? 304 ARG   A NE  1 
ATOM   2465 C  CZ  . ARG   A 1 319 ? 10.522  -17.682 -18.231 1   52.16 ? 304 ARG   A CZ  1 
ATOM   2466 N  NH1 . ARG   A 1 319 ? 10.556  -16.403 -17.875 1   51.68 ? 304 ARG   A NH1 1 
ATOM   2467 N  NH2 . ARG   A 1 319 ? 9.365   -18.229 -18.602 1   49.55 ? 304 ARG   A NH2 1 
ATOM   2468 N  N   . ASN   A 1 320 ? 14.121  -21.074 -14.012 1   35.35 ? 305 ASN   A N   1 
ATOM   2469 C  CA  . ASN   A 1 320 ? 14.761  -20.783 -12.722 1   35.62 ? 305 ASN   A CA  1 
ATOM   2470 C  C   . ASN   A 1 320 ? 15.721  -21.923 -12.36  1   35.24 ? 305 ASN   A C   1 
ATOM   2471 O  O   . ASN   A 1 320 ? 16.835  -21.672 -11.894 1   35.43 ? 305 ASN   A O   1 
ATOM   2472 C  CB  . ASN   A 1 320 ? 13.706  -20.649 -11.614 1   38.18 ? 305 ASN   A CB  1 
ATOM   2473 C  CG  . ASN   A 1 320 ? 12.831  -19.427 -11.712 1   43.46 ? 305 ASN   A CG  1 
ATOM   2474 O  OD1 . ASN   A 1 320 ? 13.107  -18.512 -12.495 1   46.1  ? 305 ASN   A OD1 1 
ATOM   2475 N  ND2 . ASN   A 1 320 ? 11.757  -19.38  -10.915 1   43.96 ? 305 ASN   A ND2 1 
ATOM   2476 N  N   . PHE   A 1 321 ? 15.292  -23.168 -12.585 1   33.85 ? 306 PHE   A N   1 
ATOM   2477 C  CA  . PHE   A 1 321 ? 16.095  -24.348 -12.3   1   33.31 ? 306 PHE   A CA  1 
ATOM   2478 C  C   . PHE   A 1 321 ? 17.407  -24.298 -13.071 1   33.87 ? 306 PHE   A C   1 
ATOM   2479 O  O   . PHE   A 1 321 ? 18.46   -24.521 -12.48  1   34.23 ? 306 PHE   A O   1 
ATOM   2480 C  CB  . PHE   A 1 321 ? 15.301  -25.632 -12.619 1   32.92 ? 306 PHE   A CB  1 
ATOM   2481 C  CG  . PHE   A 1 321 ? 16.07   -26.875 -12.283 1   34.15 ? 306 PHE   A CG  1 
ATOM   2482 C  CD1 . PHE   A 1 321 ? 16.266  -27.248 -10.969 1   35.07 ? 306 PHE   A CD1 1 
ATOM   2483 C  CD2 . PHE   A 1 321 ? 16.7    -27.609 -13.275 1   34.99 ? 306 PHE   A CD2 1 
ATOM   2484 C  CE1 . PHE   A 1 321 ? 17.001  -28.389 -10.654 1   35.64 ? 306 PHE   A CE1 1 
ATOM   2485 C  CE2 . PHE   A 1 321 ? 17.451  -28.742 -12.956 1   35.83 ? 306 PHE   A CE2 1 
ATOM   2486 C  CZ  . PHE   A 1 321 ? 17.589  -29.126 -11.646 1   35.6  ? 306 PHE   A CZ  1 
ATOM   2487 N  N   . LEU   A 1 322 ? 17.349  -23.933 -14.361 1   33.9  ? 307 LEU   A N   1 
ATOM   2488 C  CA  . LEU   A 1 322 ? 18.528  -23.824 -15.193 1   35.24 ? 307 LEU   A CA  1 
ATOM   2489 C  C   . LEU   A 1 322 ? 19.533  -22.768 -14.721 1   35.86 ? 307 LEU   A C   1 
ATOM   2490 O  O   . LEU   A 1 322 ? 20.735  -23.061 -14.627 1   35.02 ? 307 LEU   A O   1 
ATOM   2491 C  CB  . LEU   A 1 322 ? 18.146  -23.588 -16.652 1   35.29 ? 307 LEU   A CB  1 
ATOM   2492 C  CG  . LEU   A 1 322 ? 17.597  -24.79  -17.365 1   37.3  ? 307 LEU   A CG  1 
ATOM   2493 C  CD1 . LEU   A 1 322 ? 17.12   -24.402 -18.747 1   37.19 ? 307 LEU   A CD1 1 
ATOM   2494 C  CD2 . LEU   A 1 322 ? 18.648  -25.866 -17.479 1   37.74 ? 307 LEU   A CD2 1 
ATOM   2495 N  N   . CYS   A 1 323 ? 19.049  -21.559 -14.403 1   37.1  ? 308 CYS   A N   1 
ATOM   2496 C  CA  . CYS   A 1 323 ? 19.988  -20.539 -13.939 1   38.3  ? 308 CYS   A CA  1 
ATOM   2497 C  C   . CYS   A 1 323 ? 20.558  -20.908 -12.527 1   37.32 ? 308 CYS   A C   1 
ATOM   2498 O  O   . CYS   A 1 323 ? 21.731  -20.647 -12.275 1   37.28 ? 308 CYS   A O   1 
ATOM   2499 C  CB  . CYS   A 1 323 ? 19.427  -19.122 -14.032 1   41.59 ? 308 CYS   A CB  1 
ATOM   2500 S  SG  . CYS   A 1 323 ? 18.158  -18.757 -12.809 1   49.03 ? 308 CYS   A SG  1 
ATOM   2501 N  N   . SER   A 1 324 ? 19.792  -21.638 -11.696 1   36.35 ? 309 SER   A N   1 
ATOM   2502 C  CA  . SER   A 1 324 ? 20.245  -22.139 -10.405 1   36.36 ? 309 SER   A CA  1 
ATOM   2503 C  C   . SER   A 1 324 ? 21.322  -23.203 -10.615 1   36.16 ? 309 SER   A C   1 
ATOM   2504 O  O   . SER   A 1 324 ? 22.285  -23.248 -9.845  1   36.12 ? 309 SER   A O   1 
ATOM   2505 C  CB  . SER   A 1 324 ? 19.098  -22.758 -9.619  1   37.46 ? 309 SER   A CB  1 
ATOM   2506 O  OG  . SER   A 1 324 ? 18.245  -21.77  -9.068  1   42.76 ? 309 SER   A OG  1 
ATOM   2507 N  N   . LEU   A 1 325 ? 21.173  -24.066 -11.638 1   35.16 ? 310 LEU   A N   1 
ATOM   2508 C  CA  . LEU   A 1 325 ? 22.219  -25.05  -11.963 1   35.12 ? 310 LEU   A CA  1 
ATOM   2509 C  C   . LEU   A 1 325 ? 23.505  -24.343 -12.348 1   34.88 ? 310 LEU   A C   1 
ATOM   2510 O  O   . LEU   A 1 325 ? 24.582  -24.758 -11.94  1   34.95 ? 310 LEU   A O   1 
ATOM   2511 C  CB  . LEU   A 1 325 ? 21.796  -25.974 -13.122 1   35.04 ? 310 LEU   A CB  1 
ATOM   2512 C  CG  . LEU   A 1 325 ? 21.008  -27.219 -12.792 1   36.76 ? 310 LEU   A CG  1 
ATOM   2513 C  CD1 . LEU   A 1 325 ? 20.797  -28.037 -14.069 1   37.32 ? 310 LEU   A CD1 1 
ATOM   2514 C  CD2 . LEU   A 1 325 ? 21.701  -28.054 -11.718 1   37.2  ? 310 LEU   A CD2 1 
ATOM   2515 N  N   . GLU   A 1 326 ? 23.387  -23.24  -13.099 1   34.74 ? 311 GLU   A N   1 
ATOM   2516 C  CA  . GLU   A 1 326 ? 24.504  -22.419 -13.547 1   35.72 ? 311 GLU   A CA  1 
ATOM   2517 C  C   . GLU   A 1 326 ? 25.235  -21.707 -12.419 1   35.56 ? 311 GLU   A C   1 
ATOM   2518 O  O   . GLU   A 1 326 ? 26.414  -21.396 -12.556 1   35.91 ? 311 GLU   A O   1 
ATOM   2519 C  CB  . GLU   A 1 326 ? 24.022  -21.366 -14.559 1   38.54 ? 311 GLU   A CB  1 
ATOM   2520 C  CG  . GLU   A 1 326 ? 24.224  -21.78  -15.994 1   43.24 ? 311 GLU   A CG  1 
ATOM   2521 C  CD  . GLU   A 1 326 ? 23.424  -20.967 -16.997 1   50.85 ? 311 GLU   A CD  1 
ATOM   2522 O  OE1 . GLU   A 1 326 ? 22.592  -20.126 -16.584 1   50.77 ? 311 GLU   A OE1 1 
ATOM   2523 O  OE2 . GLU   A 1 326 ? 23.62   -21.195 -18.211 1   53.47 ? 311 GLU   A OE2 1 
ATOM   2524 N  N   . SER   A 1 327 ? 24.522  -21.395 -11.341 1   35.03 ? 312 SER   A N   1 
ATOM   2525 C  CA  . SER   A 1 327 ? 25.044  -20.716 -10.168 1   35.5  ? 312 SER   A CA  1 
ATOM   2526 C  C   . SER   A 1 327 ? 25.843  -21.667 -9.242  1   35.62 ? 312 SER   A C   1 
ATOM   2527 O  O   . SER   A 1 327 ? 26.591  -21.196 -8.392  1   35.67 ? 312 SER   A O   1 
ATOM   2528 C  CB  . SER   A 1 327 ? 23.894  -20.064 -9.398  1   37.3  ? 312 SER   A CB  1 
ATOM   2529 O  OG  . SER   A 1 327 ? 23.202  -19.074 -10.153 1   39.78 ? 312 SER   A OG  1 
ATOM   2530 N  N   . ASN   A 1 328 ? 25.643  -22.986 -9.374  1   35.85 ? 313 ASN   A N   1 
ATOM   2531 C  CA  . ASN   A 1 328 ? 26.349  -23.993 -8.594  1   36.23 ? 313 ASN   A CA  1 
ATOM   2532 C  C   . ASN   A 1 328 ? 27.746  -24.231 -9.138  1   36.17 ? 313 ASN   A C   1 
ATOM   2533 O  O   . ASN   A 1 328 ? 28.025  -23.914 -10.294 1   36.13 ? 313 ASN   A O   1 
ATOM   2534 C  CB  . ASN   A 1 328 ? 25.558  -25.297 -8.573  1   37.25 ? 313 ASN   A CB  1 
ATOM   2535 C  CG  . ASN   A 1 328 ? 24.454  -25.26  -7.585  1   39.9  ? 313 ASN   A CG  1 
ATOM   2536 O  OD1 . ASN   A 1 328 ? 23.385  -24.692 -7.85   1   41.93 ? 313 ASN   A OD1 1 
ATOM   2537 N  ND2 . ASN   A 1 328 ? 24.68   -25.856 -6.433  1   38.36 ? 313 ASN   A ND2 1 
ATOM   2538 N  N   . PRO   A 1 329 ? 28.66   -24.773 -8.299  1   36.21 ? 314 PRO   A N   1 
ATOM   2539 C  CA  . PRO   A 1 329 ? 30.018  -25.065 -8.778  1   35.96 ? 314 PRO   A CA  1 
ATOM   2540 C  C   . PRO   A 1 329 ? 30.028  -25.997 -9.976  1   34.95 ? 314 PRO   A C   1 
ATOM   2541 O  O   . PRO   A 1 329 ? 29.109  -26.787 -10.182 1   34.35 ? 314 PRO   A O   1 
ATOM   2542 C  CB  . PRO   A 1 329 ? 30.692  -25.733 -7.567  1   37.2  ? 314 PRO   A CB  1 
ATOM   2543 C  CG  . PRO   A 1 329 ? 29.869  -25.32  -6.4    1   37.56 ? 314 PRO   A CG  1 
ATOM   2544 C  CD  . PRO   A 1 329 ? 28.471  -25.198 -6.902  1   35.95 ? 314 PRO   A CD  1 
ATOM   2545 N  N   . SER   A 1 330 ? 31.068  -25.883 -10.77  1   34.95 ? 315 SER   A N   1 
ATOM   2546 C  CA  . SER   A 1 330 ? 31.229  -26.645 -11.98  1   35.31 ? 315 SER   A CA  1 
ATOM   2547 C  C   . SER   A 1 330 ? 31.713  -28.062 -11.701 1   35.26 ? 315 SER   A C   1 
ATOM   2548 O  O   . SER   A 1 330 ? 32.798  -28.247 -11.145 1   35.44 ? 315 SER   A O   1 
ATOM   2549 C  CB  . SER   A 1 330 ? 32.211  -25.925 -12.901 1   36.8  ? 315 SER   A CB  1 
ATOM   2550 O  OG  . SER   A 1 330 ? 32.534  -26.682 -14.057 1   39.83 ? 315 SER   A OG  1 
ATOM   2551 N  N   . VAL   A 1 331 ? 30.928  -29.054 -12.145 1   34.39 ? 316 VAL   A N   1 
ATOM   2552 C  CA  . VAL   A 1 331 ? 31.255  -30.471 -12.082 1   34.64 ? 316 VAL   A CA  1 
ATOM   2553 C  C   . VAL   A 1 331 ? 32.487  -30.752 -12.952 1   33.9  ? 316 VAL   A C   1 
ATOM   2554 O  O   . VAL   A 1 331 ? 33.398  -31.458 -12.529 1   33.55 ? 316 VAL   A O   1 
ATOM   2555 C  CB  . VAL   A 1 331 ? 30.039  -31.294 -12.555 1   36.37 ? 316 VAL   A CB  1 
ATOM   2556 C  CG1 . VAL   A 1 331 ? 30.393  -32.768 -12.693 1   37.62 ? 316 VAL   A CG1 1 
ATOM   2557 C  CG2 . VAL   A 1 331 ? 28.862  -31.091 -11.606 1   37.54 ? 316 VAL   A CG2 1 
ATOM   2558 N  N   . ARG   A 1 332 ? 32.518  -30.175 -14.164 1   33.43 ? 317 ARG   A N   1 
ATOM   2559 C  CA  . ARG   A 1 332 ? 33.642  -30.312 -15.083 1   33.43 ? 317 ARG   A CA  1 
ATOM   2560 C  C   . ARG   A 1 332 ? 34.948  -29.788 -14.459 1   34.38 ? 317 ARG   A C   1 
ATOM   2561 O  O   . ARG   A 1 332 ? 35.978  -30.438 -14.589 1   34.69 ? 317 ARG   A O   1 
ATOM   2562 C  CB  . ARG   A 1 332 ? 33.355  -29.538 -16.385 1   33.26 ? 317 ARG   A CB  1 
ATOM   2563 C  CG  . ARG   A 1 332 ? 34.538  -29.514 -17.339 1   33.26 ? 317 ARG   A CG  1 
ATOM   2564 C  CD  . ARG   A 1 332 ? 34.26   -28.665 -18.556 1   35.15 ? 317 ARG   A CD  1 
ATOM   2565 N  NE  . ARG   A 1 332 ? 35.367  -28.71  -19.509 1   36.22 ? 317 ARG   A NE  1 
ATOM   2566 C  CZ  . ARG   A 1 332 ? 35.601  -29.711 -20.347 1   35.19 ? 317 ARG   A CZ  1 
ATOM   2567 N  NH1 . ARG   A 1 332 ? 36.647  -29.668 -21.165 1   34.26 ? 317 ARG   A NH1 1 
ATOM   2568 N  NH2 . ARG   A 1 332 ? 34.812  -30.778 -20.351 1   32.79 ? 317 ARG   A NH2 1 
ATOM   2569 N  N   . GLU   A 1 333 ? 34.917  -28.585 -13.858 1   34.15 ? 318 GLU   A N   1 
ATOM   2570 C  CA  . GLU   A 1 333 ? 36.11   -28.002 -13.256 1   34.53 ? 318 GLU   A CA  1 
ATOM   2571 C  C   . GLU   A 1 333 ? 36.589  -28.869 -12.088 1   35.43 ? 318 GLU   A C   1 
ATOM   2572 O  O   . GLU   A 1 333 ? 37.79   -29.101 -11.956 1   35.9  ? 318 GLU   A O   1 
ATOM   2573 C  CB  . GLU   A 1 333 ? 35.835  -26.564 -12.787 1   35.83 ? 318 GLU   A CB  1 
ATOM   2574 N  N   . PHE   A 1 334 ? 35.659  -29.387 -11.282 1   35.7  ? 319 PHE   A N   1 
ATOM   2575 C  CA  . PHE   A 1 334 ? 35.978  -30.266 -10.161 1   36.47 ? 319 PHE   A CA  1 
ATOM   2576 C  C   . PHE   A 1 334 ? 36.683  -31.524 -10.658 1   37.4  ? 319 PHE   A C   1 
ATOM   2577 O  O   . PHE   A 1 334 ? 37.752  -31.849 -10.148 1   37.64 ? 319 PHE   A O   1 
ATOM   2578 C  CB  . PHE   A 1 334 ? 34.707  -30.649 -9.391  1   36.14 ? 319 PHE   A CB  1 
ATOM   2579 C  CG  . PHE   A 1 334 ? 34.904  -31.434 -8.113  1   37.08 ? 319 PHE   A CG  1 
ATOM   2580 C  CD1 . PHE   A 1 334 ? 35.05   -32.811 -8.139  1   38.31 ? 319 PHE   A CD1 1 
ATOM   2581 C  CD2 . PHE   A 1 334 ? 34.935  -30.796 -6.884  1   37.75 ? 319 PHE   A CD2 1 
ATOM   2582 C  CE1 . PHE   A 1 334 ? 35.247  -33.53  -6.963  1   38.88 ? 319 PHE   A CE1 1 
ATOM   2583 C  CE2 . PHE   A 1 334 ? 35.087  -31.522 -5.709  1   38.59 ? 319 PHE   A CE2 1 
ATOM   2584 C  CZ  . PHE   A 1 334 ? 35.231  -32.886 -5.753  1   38.67 ? 319 PHE   A CZ  1 
ATOM   2585 N  N   . VAL   A 1 335 ? 36.096  -32.216 -11.661 1   36.61 ? 320 VAL   A N   1 
ATOM   2586 C  CA  . VAL   A 1 335 ? 36.658  -33.442 -12.22  1   36.82 ? 320 VAL   A CA  1 
ATOM   2587 C  C   . VAL   A 1 335 ? 38.025  -33.185 -12.878 1   37.93 ? 320 VAL   A C   1 
ATOM   2588 O  O   . VAL   A 1 335 ? 38.967  -33.968 -12.712 1   37.9  ? 320 VAL   A O   1 
ATOM   2589 C  CB  . VAL   A 1 335 ? 35.638  -34.098 -13.183 1   36.85 ? 320 VAL   A CB  1 
ATOM   2590 C  CG1 . VAL   A 1 335 ? 36.295  -35.173 -14.046 1   36.6  ? 320 VAL   A CG1 1 
ATOM   2591 C  CG2 . VAL   A 1 335 ? 34.447  -34.662 -12.404 1   36.82 ? 320 VAL   A CG2 1 
ATOM   2592 N  N   . LEU   A 1 336 ? 38.142  -32.082 -13.601 1   39.08 ? 321 LEU   A N   1 
ATOM   2593 C  CA  . LEU   A 1 336 ? 39.396  -31.717 -14.259 1   41.55 ? 321 LEU   A CA  1 
ATOM   2594 C  C   . LEU   A 1 336 ? 40.537  -31.441 -13.265 1   43.02 ? 321 LEU   A C   1 
ATOM   2595 O  O   . LEU   A 1 336 ? 41.705  -31.549 -13.631 1   43.79 ? 321 LEU   A O   1 
ATOM   2596 C  CB  . LEU   A 1 336 ? 39.187  -30.482 -15.141 1   42.39 ? 321 LEU   A CB  1 
ATOM   2597 C  CG  . LEU   A 1 336 ? 38.89   -30.766 -16.62  1   45.16 ? 321 LEU   A CG  1 
ATOM   2598 C  CD1 . LEU   A 1 336 ? 38.577  -29.485 -17.359 1   46.13 ? 321 LEU   A CD1 1 
ATOM   2599 C  CD2 . LEU   A 1 336 ? 40.051  -31.48  -17.288 1   46.13 ? 321 LEU   A CD2 1 
ATOM   2600 N  N   . SER   A 1 337 ? 40.211  -31.041 -12.034 1   42.99 ? 322 SER   A N   1 
ATOM   2601 C  CA  . SER   A 1 337 ? 41.241  -30.685 -11.052 1   43.51 ? 322 SER   A CA  1 
ATOM   2602 C  C   . SER   A 1 337 ? 41.697  -31.832 -10.146 1   44.66 ? 322 SER   A C   1 
ATOM   2603 O  O   . SER   A 1 337 ? 42.536  -31.589 -9.262  1   45.07 ? 322 SER   A O   1 
ATOM   2604 C  CB  . SER   A 1 337 ? 40.74   -29.547 -10.173 1   43.49 ? 322 SER   A CB  1 
ATOM   2605 O  OG  . SER   A 1 337 ? 39.738  -29.997 -9.273  1   45.4  ? 322 SER   A OG  1 
ATOM   2606 N  N   . LYS   A 1 338 ? 41.148  -33.045 -10.318 1   44.41 ? 323 LYS   A N   1 
ATOM   2607 C  CA  . LYS   A 1 338 ? 41.427  -34.106 -9.357  1   44.86 ? 323 LYS   A CA  1 
ATOM   2608 C  C   . LYS   A 1 338 ? 42.464  -35.17  -9.715  1   44.53 ? 323 LYS   A C   1 
ATOM   2609 O  O   . LYS   A 1 338 ? 42.794  -35.958 -8.807  1   45.49 ? 323 LYS   A O   1 
ATOM   2610 C  CB  . LYS   A 1 338 ? 40.135  -34.816 -8.946  1   46.19 ? 323 LYS   A CB  1 
ATOM   2611 C  CG  . LYS   A 1 338 ? 39.147  -33.934 -8.184  1   50.85 ? 323 LYS   A CG  1 
ATOM   2612 C  CD  . LYS   A 1 338 ? 39.783  -33.03  -7.116  1   56.84 ? 323 LYS   A CD  1 
ATOM   2613 C  CE  . LYS   A 1 338 ? 38.755  -32.251 -6.34   1   61.6  ? 323 LYS   A CE  1 
ATOM   2614 N  NZ  . LYS   A 1 338 ? 39.29   -30.949 -5.842  1   65    ? 323 LYS   A NZ  1 
ATOM   2615 N  N   . GLY   A 1 339 ? 42.999  -35.194 -10.948 1   42.45 ? 324 GLY   A N   1 
ATOM   2616 C  CA  . GLY   A 1 339 ? 43.984  -36.205 -11.377 1   40.8  ? 324 GLY   A CA  1 
ATOM   2617 C  C   . GLY   A 1 339 ? 43.519  -37.624 -11.082 1   38.6  ? 324 GLY   A C   1 
ATOM   2618 O  O   . GLY   A 1 339 ? 44.244  -38.439 -10.499 1   38.24 ? 324 GLY   A O   1 
ATOM   2619 N  N   . ASP   A 1 340 ? 42.256  -37.887 -11.417 1   36.5  ? 325 ASP   A N   1 
ATOM   2620 C  CA  . ASP   A 1 340 ? 41.586  -39.122 -11.063 1   34.62 ? 325 ASP   A CA  1 
ATOM   2621 C  C   . ASP   A 1 340 ? 40.929  -39.705 -12.298 1   34.59 ? 325 ASP   A C   1 
ATOM   2622 O  O   . ASP   A 1 340 ? 39.879  -39.208 -12.725 1   33.76 ? 325 ASP   A O   1 
ATOM   2623 C  CB  . ASP   A 1 340 ? 40.559  -38.759 -9.992  1   33.31 ? 325 ASP   A CB  1 
ATOM   2624 C  CG  . ASP   A 1 340 ? 39.738  -39.857 -9.373  1   36.13 ? 325 ASP   A CG  1 
ATOM   2625 O  OD1 . ASP   A 1 340 ? 39.467  -40.857 -10.053 1   35.47 ? 325 ASP   A OD1 1 
ATOM   2626 O  OD2 . ASP   A 1 340 ? 39.323  -39.694 -8.221  1   39.61 ? 325 ASP   A OD2 1 
ATOM   2627 N  N   . ALA   A 1 341 ? 41.552  -40.769 -12.857 1   33.89 ? 326 ALA   A N   1 
ATOM   2628 C  CA  . ALA   A 1 341 ? 41.105  -41.453 -14.06  1   33.66 ? 326 ALA   A CA  1 
ATOM   2629 C  C   . ALA   A 1 341 ? 39.679  -41.974 -13.968 1   33.03 ? 326 ALA   A C   1 
ATOM   2630 O  O   . ALA   A 1 341 ? 38.899  -41.726 -14.877 1   32.61 ? 326 ALA   A O   1 
ATOM   2631 C  CB  . ALA   A 1 341 ? 42.073  -42.565 -14.445 1   33.58 ? 326 ALA   A CB  1 
ATOM   2632 N  N   . GLY   A 1 342 ? 39.331  -42.638 -12.873 1   32.45 ? 327 GLY   A N   1 
ATOM   2633 C  CA  . GLY   A 1 342 ? 37.987  -43.152 -12.676 1   33.22 ? 327 GLY   A CA  1 
ATOM   2634 C  C   . GLY   A 1 342 ? 36.912  -42.064 -12.705 1   33.48 ? 327 GLY   A C   1 
ATOM   2635 O  O   . GLY   A 1 342 ? 35.852  -42.25  -13.297 1   32.86 ? 327 GLY   A O   1 
ATOM   2636 N  N   . LEU   A 1 343 ? 37.189  -40.911 -12.091 1   33.17 ? 328 LEU   A N   1 
ATOM   2637 C  CA  . LEU   A 1 343 ? 36.23   -39.801 -12.057 1   33.55 ? 328 LEU   A CA  1 
ATOM   2638 C  C   . LEU   A 1 343 ? 36.114  -39.16  -13.447 1   33    ? 328 LEU   A C   1 
ATOM   2639 O  O   . LEU   A 1 343 ? 35.006  -38.846 -13.892 1   32.41 ? 328 LEU   A O   1 
ATOM   2640 C  CB  . LEU   A 1 343 ? 36.728  -38.786 -11.034 1   34.39 ? 328 LEU   A CB  1 
ATOM   2641 C  CG  . LEU   A 1 343 ? 35.736  -37.86  -10.409 1   36.81 ? 328 LEU   A CG  1 
ATOM   2642 C  CD1 . LEU   A 1 343 ? 34.53   -38.632 -9.779  1   36.39 ? 328 LEU   A CD1 1 
ATOM   2643 C  CD2 . LEU   A 1 343 ? 36.456  -36.975 -9.397  1   38.13 ? 328 LEU   A CD2 1 
ATOM   2644 N  N   . ARG   A 1 344 ? 37.244  -39.029 -14.158 1   32.98 ? 329 ARG   A N   1 
ATOM   2645 C  CA  . ARG   A 1 344 ? 37.238  -38.512 -15.52  1   32.97 ? 329 ARG   A CA  1 
ATOM   2646 C  C   . ARG   A 1 344 ? 36.452  -39.4   -16.439 1   32.93 ? 329 ARG   A C   1 
ATOM   2647 O  O   . ARG   A 1 344 ? 35.698  -38.91  -17.281 1   33.32 ? 329 ARG   A O   1 
ATOM   2648 C  CB  . ARG   A 1 344 ? 38.664  -38.318 -16.054 1   33.57 ? 329 ARG   A CB  1 
ATOM   2649 C  CG  . ARG   A 1 344 ? 39.395  -37.191 -15.335 1   36.98 ? 329 ARG   A CG  1 
ATOM   2650 C  CD  . ARG   A 1 344 ? 40.581  -36.644 -16.114 1   41.68 ? 329 ARG   A CD  1 
ATOM   2651 N  NE  . ARG   A 1 344 ? 41.559  -37.674 -16.471 1   45.57 ? 329 ARG   A NE  1 
ATOM   2652 C  CZ  . ARG   A 1 344 ? 42.545  -38.084 -15.672 1   48.73 ? 329 ARG   A CZ  1 
ATOM   2653 N  NH1 . ARG   A 1 344 ? 42.677  -37.576 -14.456 1   47.53 ? 329 ARG   A NH1 1 
ATOM   2654 N  NH2 . ARG   A 1 344 ? 43.395  -39.017 -16.081 1   48.69 ? 329 ARG   A NH2 1 
ATOM   2655 N  N   . GLU   A 1 345 ? 36.603  -40.717 -16.275 1   32.43 ? 330 GLU   A N   1 
ATOM   2656 C  CA  . GLU   A 1 345 ? 35.903  -41.683 -17.081 1   32.59 ? 330 GLU   A CA  1 
ATOM   2657 C  C   . GLU   A 1 345 ? 34.403  -41.646 -16.863 1   31.37 ? 330 GLU   A C   1 
ATOM   2658 O  O   . GLU   A 1 345 ? 33.652  -41.734 -17.831 1   31.18 ? 330 GLU   A O   1 
ATOM   2659 C  CB  . GLU   A 1 345 ? 36.488  -43.097 -16.888 1   36.69 ? 330 GLU   A CB  1 
ATOM   2660 C  CG  . GLU   A 1 345 ? 37.756  -43.32  -17.709 1   46.99 ? 330 GLU   A CG  1 
ATOM   2661 C  CD  . GLU   A 1 345 ? 37.756  -42.793 -19.142 1   59.49 ? 330 GLU   A CD  1 
ATOM   2662 O  OE1 . GLU   A 1 345 ? 37.014  -43.344 -19.992 1   62.55 ? 330 GLU   A OE1 1 
ATOM   2663 O  OE2 . GLU   A 1 345 ? 38.464  -41.791 -19.4   1   63.8  ? 330 GLU   A OE2 1 
ATOM   2664 N  N   . ALA   A 1 346 ? 33.962  -41.467 -15.615 1   29.9  ? 331 ALA   A N   1 
ATOM   2665 C  CA  . ALA   A 1 346 ? 32.553  -41.369 -15.296 1   29.77 ? 331 ALA   A CA  1 
ATOM   2666 C  C   . ALA   A 1 346 ? 31.972  -40.082 -15.898 1   29.29 ? 331 ALA   A C   1 
ATOM   2667 O  O   . ALA   A 1 346 ? 30.86   -40.102 -16.428 1   29.18 ? 331 ALA   A O   1 
ATOM   2668 C  CB  . ALA   A 1 346 ? 32.356  -41.372 -13.78  1   30.36 ? 331 ALA   A CB  1 
ATOM   2669 N  N   . TYR   A 1 347 ? 32.709  -38.969 -15.816 1   28.93 ? 332 TYR   A N   1 
ATOM   2670 C  CA  . TYR   A 1 347 ? 32.28   -37.692 -16.4   1   29.47 ? 332 TYR   A CA  1 
ATOM   2671 C  C   . TYR   A 1 347 ? 32.137  -37.856 -17.92  1   31.26 ? 332 TYR   A C   1 
ATOM   2672 O  O   . TYR   A 1 347 ? 31.135  -37.425 -18.505 1   31.89 ? 332 TYR   A O   1 
ATOM   2673 C  CB  . TYR   A 1 347 ? 33.285  -36.575 -16.054 1   28.44 ? 332 TYR   A CB  1 
ATOM   2674 C  CG  . TYR   A 1 347 ? 33.072  -35.303 -16.85  1   29.59 ? 332 TYR   A CG  1 
ATOM   2675 C  CD1 . TYR   A 1 347 ? 33.703  -35.108 -18.073 1   30.3  ? 332 TYR   A CD1 1 
ATOM   2676 C  CD2 . TYR   A 1 347 ? 32.174  -34.336 -16.422 1   30.8  ? 332 TYR   A CD2 1 
ATOM   2677 C  CE1 . TYR   A 1 347 ? 33.483  -33.958 -18.82  1   31.19 ? 332 TYR   A CE1 1 
ATOM   2678 C  CE2 . TYR   A 1 347 ? 31.943  -33.185 -17.165 1   30.95 ? 332 TYR   A CE2 1 
ATOM   2679 C  CZ  . TYR   A 1 347 ? 32.578  -33.011 -18.373 1   31.58 ? 332 TYR   A CZ  1 
ATOM   2680 O  OH  . TYR   A 1 347 ? 32.358  -31.853 -19.093 1   31.69 ? 332 TYR   A OH  1 
ATOM   2681 N  N   . ASP   A 1 348 ? 33.125  -38.524 -18.548 1   31.54 ? 333 ASP   A N   1 
ATOM   2682 C  CA  . ASP   A 1 348 ? 33.132  -38.787 -19.989 1   31.3  ? 333 ASP   A CA  1 
ATOM   2683 C  C   . ASP   A 1 348 ? 32.026  -39.695 -20.417 1   31.38 ? 333 ASP   A C   1 
ATOM   2684 O  O   . ASP   A 1 348 ? 31.51   -39.5   -21.496 1   31.66 ? 333 ASP   A O   1 
ATOM   2685 C  CB  . ASP   A 1 348 ? 34.47   -39.326 -20.48  1   31.92 ? 333 ASP   A CB  1 
ATOM   2686 C  CG  . ASP   A 1 348 ? 35.477  -38.266 -20.845 1   35.79 ? 333 ASP   A CG  1 
ATOM   2687 O  OD1 . ASP   A 1 348 ? 35.157  -37.057 -20.705 1   35.13 ? 333 ASP   A OD1 1 
ATOM   2688 O  OD2 . ASP   A 1 348 ? 36.597  -38.638 -21.27  1   37.43 ? 333 ASP   A OD2 1 
ATOM   2689 N  N   . ALA   A 1 349 ? 31.609  -40.64  -19.577 1   30.84 ? 334 ALA   A N   1 
ATOM   2690 C  CA  . ALA   A 1 349 ? 30.467  -41.494 -19.905 1   31    ? 334 ALA   A CA  1 
ATOM   2691 C  C   . ALA   A 1 349 ? 29.171  -40.646 -20.034 1   31.47 ? 334 ALA   A C   1 
ATOM   2692 O  O   . ALA   A 1 349 ? 28.334  -40.95  -20.88  1   31.51 ? 334 ALA   A O   1 
ATOM   2693 C  CB  . ALA   A 1 349 ? 30.301  -42.57  -18.86  1   30.86 ? 334 ALA   A CB  1 
ATOM   2694 N  N   . CYS   A 1 350 ? 29.018  -39.582 -19.217 1   30.67 ? 335 CYS   A N   1 
ATOM   2695 C  CA  . CYS   A 1 350 ? 27.856  -38.691 -19.324 1   30.13 ? 335 CYS   A CA  1 
ATOM   2696 C  C   . CYS   A 1 350 ? 27.908  -37.888 -20.631 1   29.64 ? 335 CYS   A C   1 
ATOM   2697 O  O   . CYS   A 1 350 ? 26.907  -37.794 -21.327 1   29.34 ? 335 CYS   A O   1 
ATOM   2698 C  CB  . CYS   A 1 350 ? 27.779  -37.765 -18.116 1   29.92 ? 335 CYS   A CB  1 
ATOM   2699 S  SG  . CYS   A 1 350 ? 27.445  -38.618 -16.554 1   31.62 ? 335 CYS   A SG  1 
ATOM   2700 N  N   . VAL   A 1 351 ? 29.075  -37.295 -20.942 1   29.37 ? 336 VAL   A N   1 
ATOM   2701 C  CA  . VAL   A 1 351 ? 29.262  -36.511 -22.147 1   30.79 ? 336 VAL   A CA  1 
ATOM   2702 C  C   . VAL   A 1 351 ? 29.083  -37.393 -23.381 1   32.43 ? 336 VAL   A C   1 
ATOM   2703 O  O   . VAL   A 1 351 ? 28.356  -37.003 -24.297 1   32.95 ? 336 VAL   A O   1 
ATOM   2704 C  CB  . VAL   A 1 351 ? 30.631  -35.802 -22.136 1   31.67 ? 336 VAL   A CB  1 
ATOM   2705 C  CG1 . VAL   A 1 351 ? 30.878  -35.074 -23.454 1   32.51 ? 336 VAL   A CG1 1 
ATOM   2706 C  CG2 . VAL   A 1 351 ? 30.733  -34.836 -20.967 1   31.44 ? 336 VAL   A CG2 1 
ATOM   2707 N  N   . LYS   A 1 352 ? 29.682  -38.613 -23.383 1   32.43 ? 337 LYS   A N   1 
ATOM   2708 C  CA  . LYS   A 1 352 ? 29.557  -39.569 -24.476 1   33.5  ? 337 LYS   A CA  1 
ATOM   2709 C  C   . LYS   A 1 352 ? 28.102  -39.963 -24.728 1   32.93 ? 337 LYS   A C   1 
ATOM   2710 O  O   . LYS   A 1 352 ? 27.695  -40.059 -25.885 1   33.07 ? 337 LYS   A O   1 
ATOM   2711 C  CB  . LYS   A 1 352 ? 30.389  -40.829 -24.196 1   37.78 ? 337 LYS   A CB  1 
ATOM   2712 C  CG  . LYS   A 1 352 ? 30.511  -41.785 -25.385 1   44.98 ? 337 LYS   A CG  1 
ATOM   2713 C  CD  . LYS   A 1 352 ? 31.934  -41.824 -25.983 1   53.15 ? 337 LYS   A CD  1 
ATOM   2714 C  CE  . LYS   A 1 352 ? 32.954  -42.583 -25.144 1   58.77 ? 337 LYS   A CE  1 
ATOM   2715 N  NZ  . LYS   A 1 352 ? 33.521  -41.812 -23.985 1   60.11 ? 337 LYS   A NZ  1 
ATOM   2716 N  N   . ALA   A 1 353 ? 27.303  -40.152 -23.667 1   32.3  ? 338 ALA   A N   1 
ATOM   2717 C  CA  . ALA   A 1 353 ? 25.89   -40.478 -23.806 1   32.01 ? 338 ALA   A CA  1 
ATOM   2718 C  C   . ALA   A 1 353 ? 25.137  -39.338 -24.502 1   31.46 ? 338 ALA   A C   1 
ATOM   2719 O  O   . ALA   A 1 353 ? 24.261  -39.615 -25.304 1   31.79 ? 338 ALA   A O   1 
ATOM   2720 C  CB  . ALA   A 1 353 ? 25.273  -40.752 -22.439 1   31.97 ? 338 ALA   A CB  1 
ATOM   2721 N  N   . LEU   A 1 354 ? 25.487  -38.079 -24.215 1   30.48 ? 339 LEU   A N   1 
ATOM   2722 C  CA  . LEU   A 1 354 ? 24.897  -36.909 -24.859 1   30.68 ? 339 LEU   A CA  1 
ATOM   2723 C  C   . LEU   A 1 354 ? 25.356  -36.819 -26.324 1   30.53 ? 339 LEU   A C   1 
ATOM   2724 O  O   . LEU   A 1 354 ? 24.56   -36.489 -27.194 1   29.65 ? 339 LEU   A O   1 
ATOM   2725 C  CB  . LEU   A 1 354 ? 25.288  -35.626 -24.112 1   30.46 ? 339 LEU   A CB  1 
ATOM   2726 C  CG  . LEU   A 1 354 ? 24.413  -35.249 -22.908 1   32.71 ? 339 LEU   A CG  1 
ATOM   2727 C  CD1 . LEU   A 1 354 ? 24.914  -33.96  -22.269 1   32.78 ? 339 LEU   A CD1 1 
ATOM   2728 C  CD2 . LEU   A 1 354 ? 22.898  -35.147 -23.298 1   32.9  ? 339 LEU   A CD2 1 
ATOM   2729 N  N   . VAL   A 1 355 ? 26.633  -37.127 -26.602 1   30.24 ? 340 VAL   A N   1 
ATOM   2730 C  CA  . VAL   A 1 355 ? 27.148  -37.158 -27.987 1   29.87 ? 340 VAL   A CA  1 
ATOM   2731 C  C   . VAL   A 1 355 ? 26.406  -38.254 -28.777 1   30.11 ? 340 VAL   A C   1 
ATOM   2732 O  O   . VAL   A 1 355 ? 26.015  -38.012 -29.906 1   30.41 ? 340 VAL   A O   1 
ATOM   2733 C  CB  . VAL   A 1 355 ? 28.677  -37.394 -28.056 1   30.22 ? 340 VAL   A CB  1 
ATOM   2734 C  CG1 . VAL   A 1 355 ? 29.148  -37.605 -29.498 1   29.95 ? 340 VAL   A CG1 1 
ATOM   2735 C  CG2 . VAL   A 1 355 ? 29.431  -36.247 -27.407 1   30.88 ? 340 VAL   A CG2 1 
ATOM   2736 N  N   . SER   A 1 356 ? 26.19   -39.428 -28.185 1   30.3  ? 341 SER   A N   1 
ATOM   2737 C  CA  . SER   A 1 356 ? 25.492  -40.516 -28.864 1   31.73 ? 341 SER   A CA  1 
ATOM   2738 C  C   . SER   A 1 356 ? 24.042  -40.122 -29.192 1   32.89 ? 341 SER   A C   1 
ATOM   2739 O  O   . SER   A 1 356 ? 23.589  -40.381 -30.303 1   32.99 ? 341 SER   A O   1 
ATOM   2740 C  CB  . SER   A 1 356 ? 25.535  -41.795 -28.034 1   33.69 ? 341 SER   A CB  1 
ATOM   2741 O  OG  . SER   A 1 356 ? 26.902  -42.156 -27.854 1   37.72 ? 341 SER   A OG  1 
ATOM   2742 N  N   . LEU   A 1 357 ? 23.339  -39.447 -28.255 1   32.4  ? 342 LEU   A N   1 
ATOM   2743 C  CA  . LEU   A 1 357 ? 21.977  -38.975 -28.485 1   32.26 ? 342 LEU   A CA  1 
ATOM   2744 C  C   . LEU   A 1 357 ? 21.964  -37.989 -29.635 1   31.23 ? 342 LEU   A C   1 
ATOM   2745 O  O   . LEU   A 1 357 ? 21.141  -38.129 -30.531 1   30.89 ? 342 LEU   A O   1 
ATOM   2746 C  CB  . LEU   A 1 357 ? 21.419  -38.285 -27.218 1   33.49 ? 342 LEU   A CB  1 
ATOM   2747 C  CG  . LEU   A 1 357 ? 20.806  -39.218 -26.177 1   36.39 ? 342 LEU   A CG  1 
ATOM   2748 C  CD1 . LEU   A 1 357 ? 20.785  -38.566 -24.793 1   36.58 ? 342 LEU   A CD1 1 
ATOM   2749 C  CD2 . LEU   A 1 357 ? 19.389  -39.567 -26.572 1   37.86 ? 342 LEU   A CD2 1 
ATOM   2750 N  N   . ARG   A 1 358 ? 22.89   -36.998 -29.631 1   30.24 ? 343 ARG   A N   1 
ATOM   2751 C  CA  . ARG   A 1 358 ? 22.923  -35.981 -30.671 1   30.28 ? 343 ARG   A CA  1 
ATOM   2752 C  C   . ARG   A 1 358 ? 23.366  -36.513 -32.026 1   30.91 ? 343 ARG   A C   1 
ATOM   2753 O  O   . ARG   A 1 358 ? 22.889  -36.02  -33.044 1   31.54 ? 343 ARG   A O   1 
ATOM   2754 C  CB  . ARG   A 1 358 ? 23.764  -34.767 -30.226 1   30.79 ? 343 ARG   A CB  1 
ATOM   2755 C  CG  . ARG   A 1 358 ? 23.076  -34.079 -29.051 1   30.53 ? 343 ARG   A CG  1 
ATOM   2756 C  CD  . ARG   A 1 358 ? 23.809  -32.858 -28.545 1   31.2  ? 343 ARG   A CD  1 
ATOM   2757 N  NE  . ARG   A 1 358 ? 22.872  -32.054 -27.764 1   32    ? 343 ARG   A NE  1 
ATOM   2758 C  CZ  . ARG   A 1 358 ? 23.106  -31.583 -26.546 1   30.89 ? 343 ARG   A CZ  1 
ATOM   2759 N  NH1 . ARG   A 1 358 ? 24.283  -31.774 -25.97  1   27.96 ? 343 ARG   A NH1 1 
ATOM   2760 N  NH2 . ARG   A 1 358 ? 22.191  -30.846 -25.926 1   27.53 ? 343 ARG   A NH2 1 
ATOM   2761 N  N   . SER   A 1 359 ? 24.211  -37.546 -32.057 1   30.5  ? 344 SER   A N   1 
ATOM   2762 C  CA  . SER   A 1 359 ? 24.648  -38.139 -33.329 1   31.16 ? 344 SER   A CA  1 
ATOM   2763 C  C   . SER   A 1 359 ? 23.475  -38.914 -33.958 1   32.05 ? 344 SER   A C   1 
ATOM   2764 O  O   . SER   A 1 359 ? 23.26   -38.829 -35.162 1   31.96 ? 344 SER   A O   1 
ATOM   2765 C  CB  . SER   A 1 359 ? 25.838  -39.079 -33.102 1   31.76 ? 344 SER   A CB  1 
ATOM   2766 O  OG  . SER   A 1 359 ? 26.974  -38.324 -32.715 1   33.3  ? 344 SER   A OG  1 
ATOM   2767 N  N   . TYR   A 1 360 ? 22.723  -39.664 -33.133 1   32.36 ? 345 TYR   A N   1 
ATOM   2768 C  CA  . TYR   A 1 360 ? 21.571  -40.412 -33.606 1   33.66 ? 345 TYR   A CA  1 
ATOM   2769 C  C   . TYR   A 1 360 ? 20.482  -39.447 -34.112 1   34.01 ? 345 TYR   A C   1 
ATOM   2770 O  O   . TYR   A 1 360 ? 19.853  -39.688 -35.154 1   34.54 ? 345 TYR   A O   1 
ATOM   2771 C  CB  . TYR   A 1 360 ? 21.03   -41.283 -32.482 1   34.66 ? 345 TYR   A CB  1 
ATOM   2772 C  CG  . TYR   A 1 360 ? 19.943  -42.212 -32.958 1   38.19 ? 345 TYR   A CG  1 
ATOM   2773 C  CD1 . TYR   A 1 360 ? 20.246  -43.335 -33.716 1   40.14 ? 345 TYR   A CD1 1 
ATOM   2774 C  CD2 . TYR   A 1 360 ? 18.6    -41.918 -32.738 1   39.33 ? 345 TYR   A CD2 1 
ATOM   2775 C  CE1 . TYR   A 1 360 ? 19.247  -44.17  -34.195 1   41.57 ? 345 TYR   A CE1 1 
ATOM   2776 C  CE2 . TYR   A 1 360 ? 17.593  -42.761 -33.195 1   40.81 ? 345 TYR   A CE2 1 
ATOM   2777 C  CZ  . TYR   A 1 360 ? 17.92   -43.878 -33.94  1   42.49 ? 345 TYR   A CZ  1 
ATOM   2778 O  OH  . TYR   A 1 360 ? 16.943  -44.735 -34.396 1   45.1  ? 345 TYR   A OH  1 
ATOM   2779 N  N   . HIS   A 1 361 ? 20.28   -38.339 -33.379 1   32.64 ? 346 HIS   A N   1 
ATOM   2780 C  CA  . HIS   A 1 361 ? 19.328  -37.3   -33.71  1   32.38 ? 346 HIS   A CA  1 
ATOM   2781 C  C   . HIS   A 1 361 ? 19.708  -36.622 -35.036 1   32.9  ? 346 HIS   A C   1 
ATOM   2782 O  O   . HIS   A 1 361 ? 18.826  -36.333 -35.826 1   32.84 ? 346 HIS   A O   1 
ATOM   2783 C  CB  . HIS   A 1 361 ? 19.226  -36.31  -32.528 1   31.08 ? 346 HIS   A CB  1 
ATOM   2784 C  CG  . HIS   A 1 361 ? 18.29   -35.169 -32.741 1   29.31 ? 346 HIS   A CG  1 
ATOM   2785 N  ND1 . HIS   A 1 361 ? 18.743  -33.953 -33.19  1   30.89 ? 346 HIS   A ND1 1 
ATOM   2786 C  CD2 . HIS   A 1 361 ? 16.963  -35.091 -32.509 1   29.7  ? 346 HIS   A CD2 1 
ATOM   2787 C  CE1 . HIS   A 1 361 ? 17.692  -33.158 -33.201 1   31.14 ? 346 HIS   A CE1 1 
ATOM   2788 N  NE2 . HIS   A 1 361 ? 16.593  -33.808 -32.816 1   31.63 ? 346 HIS   A NE2 1 
ATOM   2789 N  N   . LEU   A 1 362 ? 21.003  -36.447 -35.328 1   33.92 ? 347 LEU   A N   1 
ATOM   2790 C  CA  . LEU   A 1 362 ? 21.434  -35.885 -36.613 1   35.47 ? 347 LEU   A CA  1 
ATOM   2791 C  C   . LEU   A 1 362 ? 21.017  -36.818 -37.778 1   35.71 ? 347 LEU   A C   1 
ATOM   2792 O  O   . LEU   A 1 362 ? 20.605  -36.336 -38.82  1   34.95 ? 347 LEU   A O   1 
ATOM   2793 C  CB  . LEU   A 1 362 ? 22.944  -35.646 -36.644 1   36.78 ? 347 LEU   A CB  1 
ATOM   2794 C  CG  . LEU   A 1 362 ? 23.387  -34.249 -36.203 1   39.26 ? 347 LEU   A CG  1 
ATOM   2795 C  CD1 . LEU   A 1 362 ? 24.879  -34.213 -35.933 1   40.01 ? 347 LEU   A CD1 1 
ATOM   2796 C  CD2 . LEU   A 1 362 ? 22.974  -33.176 -37.217 1   39.69 ? 347 LEU   A CD2 1 
ATOM   2797 N  N   . GLN   A 1 363 ? 21.085  -38.142 -37.569 1   35.91 ? 348 GLN   A N   1 
ATOM   2798 C  CA  . GLN   A 1 363 ? 20.645  -39.105 -38.572 1   37.05 ? 348 GLN   A CA  1 
ATOM   2799 C  C   . GLN   A 1 363 ? 19.125  -39.034 -38.751 1   36.93 ? 348 GLN   A C   1 
ATOM   2800 O  O   . GLN   A 1 363 ? 18.65   -39.142 -39.864 1   38.11 ? 348 GLN   A O   1 
ATOM   2801 C  CB  . GLN   A 1 363 ? 21.1    -40.52  -38.201 1   40.24 ? 348 GLN   A CB  1 
ATOM   2802 C  CG  . GLN   A 1 363 ? 22.616  -40.596 -38.114 1   48.3  ? 348 GLN   A CG  1 
ATOM   2803 C  CD  . GLN   A 1 363 ? 23.12   -41.956 -37.694 1   60.08 ? 348 GLN   A CD  1 
ATOM   2804 O  OE1 . GLN   A 1 363 ? 22.801  -42.985 -38.308 1   63.84 ? 348 GLN   A OE1 1 
ATOM   2805 N  NE2 . GLN   A 1 363 ? 23.943  -41.99  -36.644 1   62.69 ? 348 GLN   A NE2 1 
ATOM   2806 N  N   . ILE   A 1 364 ? 18.376  -38.776 -37.689 1   35.68 ? 349 ILE   A N   1 
ATOM   2807 C  CA  . ILE   A 1 364 ? 16.937  -38.595 -37.74  1   35.45 ? 349 ILE   A CA  1 
ATOM   2808 C  C   . ILE   A 1 364 ? 16.576  -37.357 -38.538 1   35.15 ? 349 ILE   A C   1 
ATOM   2809 O  O   . ILE   A 1 364 ? 15.681  -37.414 -39.378 1   35.58 ? 349 ILE   A O   1 
ATOM   2810 C  CB  . ILE   A 1 364 ? 16.371  -38.556 -36.301 1   36.1  ? 349 ILE   A CB  1 
ATOM   2811 C  CG1 . ILE   A 1 364 ? 16.372  -39.95  -35.668 1   37.28 ? 349 ILE   A CG1 1 
ATOM   2812 C  CG2 . ILE   A 1 364 ? 14.961  -37.933 -36.233 1   36.32 ? 349 ILE   A CG2 1 
ATOM   2813 C  CD1 . ILE   A 1 364 ? 15.833  -41.05  -36.515 1   39.73 ? 349 ILE   A CD1 1 
ATOM   2814 N  N   . VAL   A 1 365 ? 17.28   -36.245 -38.301 1   34.65 ? 350 VAL   A N   1 
ATOM   2815 C  CA  . VAL   A 1 365 ? 17.017  -35.02  -39.038 1   35.8  ? 350 VAL   A CA  1 
ATOM   2816 C  C   . VAL   A 1 365 ? 17.334  -35.198 -40.537 1   36.91 ? 350 VAL   A C   1 
ATOM   2817 O  O   . VAL   A 1 365 ? 16.616  -34.662 -41.377 1   36.42 ? 350 VAL   A O   1 
ATOM   2818 C  CB  . VAL   A 1 365 ? 17.71   -33.81  -38.381 1   36.83 ? 350 VAL   A CB  1 
ATOM   2819 C  CG1 . VAL   A 1 365 ? 17.475  -32.532 -39.185 1   37.57 ? 350 VAL   A CG1 1 
ATOM   2820 C  CG2 . VAL   A 1 365 ? 17.177  -33.639 -36.962 1   37.81 ? 350 VAL   A CG2 1 
ATOM   2821 N  N   . THR   A 1 366 ? 18.348  -36.013 -40.881 1   37.73 ? 351 THR   A N   1 
ATOM   2822 C  CA  . THR   A 1 366 ? 18.669  -36.284 -42.285 1   39.19 ? 351 THR   A CA  1 
ATOM   2823 C  C   . THR   A 1 366 ? 17.48   -37.028 -42.941 1   39.29 ? 351 THR   A C   1 
ATOM   2824 O  O   . THR   A 1 366 ? 17.033  -36.674 -44.031 1   39.75 ? 351 THR   A O   1 
ATOM   2825 C  CB  . THR   A 1 366 ? 19.95   -37.127 -42.37  1   41.5  ? 351 THR   A CB  1 
ATOM   2826 O  OG1 . THR   A 1 366 ? 21.043  -36.36  -41.849 1   42.74 ? 351 THR   A OG1 1 
ATOM   2827 C  CG2 . THR   A 1 366 ? 20.249  -37.595 -43.801 1   41.81 ? 351 THR   A CG2 1 
ATOM   2828 N  N   . LYS   A 1 367 ? 16.933  -38.016 -42.237 1   38.57 ? 352 LYS   A N   1 
ATOM   2829 C  CA  . LYS   A 1 367 ? 15.811  -38.792 -42.729 1   38.35 ? 352 LYS   A CA  1 
ATOM   2830 C  C   . LYS   A 1 367 ? 14.516  -37.99  -42.853 1   38.85 ? 352 LYS   A C   1 
ATOM   2831 O  O   . LYS   A 1 367 ? 13.796  -38.13  -43.839 1   39.62 ? 352 LYS   A O   1 
ATOM   2832 C  CB  . LYS   A 1 367 ? 15.599  -40.023 -41.812 1   39.28 ? 352 LYS   A CB  1 
ATOM   2833 C  CG  . LYS   A 1 367 ? 14.337  -40.842 -42.124 1   39.27 ? 352 LYS   A CG  1 
ATOM   2834 C  CD  . LYS   A 1 367 ? 14.219  -42.111 -41.282 1   39.14 ? 352 LYS   A CD  1 
ATOM   2835 C  CE  . LYS   A 1 367 ? 12.841  -42.703 -41.471 1   38.21 ? 352 LYS   A CE  1 
ATOM   2836 N  NZ  . LYS   A 1 367 ? 12.659  -43.97  -40.737 1   37.26 ? 352 LYS   A NZ  1 
ATOM   2837 N  N   . TYR   A 1 368 ? 14.193  -37.174 -41.848 1   38.02 ? 353 TYR   A N   1 
ATOM   2838 C  CA  . TYR   A 1 368 ? 12.91   -36.492 -41.797 1   37.36 ? 353 TYR   A CA  1 
ATOM   2839 C  C   . TYR   A 1 368 ? 12.876  -35.106 -42.392 1   37.92 ? 353 TYR   A C   1 
ATOM   2840 O  O   . TYR   A 1 368 ? 11.79   -34.631 -42.698 1   37.37 ? 353 TYR   A O   1 
ATOM   2841 C  CB  . TYR   A 1 368 ? 12.399  -36.464 -40.346 1   36.59 ? 353 TYR   A CB  1 
ATOM   2842 C  CG  . TYR   A 1 368 ? 11.915  -37.822 -39.892 1   36.03 ? 353 TYR   A CG  1 
ATOM   2843 C  CD1 . TYR   A 1 368 ? 12.785  -38.735 -39.311 1   36.39 ? 353 TYR   A CD1 1 
ATOM   2844 C  CD2 . TYR   A 1 368 ? 10.602  -38.213 -40.093 1   36.78 ? 353 TYR   A CD2 1 
ATOM   2845 C  CE1 . TYR   A 1 368 ? 12.352  -39.995 -38.914 1   37.15 ? 353 TYR   A CE1 1 
ATOM   2846 C  CE2 . TYR   A 1 368 ? 10.168  -39.484 -39.74  1   37.54 ? 353 TYR   A CE2 1 
ATOM   2847 C  CZ  . TYR   A 1 368 ? 11.038  -40.366 -39.124 1   38.24 ? 353 TYR   A CZ  1 
ATOM   2848 O  OH  . TYR   A 1 368 ? 10.603  -41.607 -38.711 1   39.19 ? 353 TYR   A OH  1 
ATOM   2849 N  N   . ILE   A 1 369 ? 14.02   -34.439 -42.525 1   38.95 ? 354 ILE   A N   1 
ATOM   2850 C  CA  . ILE   A 1 369 ? 14.049  -33.082 -43.073 1   40.68 ? 354 ILE   A CA  1 
ATOM   2851 C  C   . ILE   A 1 369 ? 14.916  -32.985 -44.321 1   43.83 ? 354 ILE   A C   1 
ATOM   2852 O  O   . ILE   A 1 369 ? 14.423  -32.528 -45.349 1   44.83 ? 354 ILE   A O   1 
ATOM   2853 C  CB  . ILE   A 1 369 ? 14.421  -32.005 -42.007 1   40.37 ? 354 ILE   A CB  1 
ATOM   2854 C  CG1 . ILE   A 1 369 ? 13.253  -31.805 -40.999 1   40.9  ? 354 ILE   A CG1 1 
ATOM   2855 C  CG2 . ILE   A 1 369 ? 14.797  -30.656 -42.664 1   40.62 ? 354 ILE   A CG2 1 
ATOM   2856 C  CD1 . ILE   A 1 369 ? 13.56   -30.859 -39.879 1   42.04 ? 354 ILE   A CD1 1 
ATOM   2857 N  N   . LEU   A 1 370 ? 16.191  -33.373 -44.237 1   45.28 ? 355 LEU   A N   1 
ATOM   2858 C  CA  . LEU   A 1 370 ? 17.123  -33.226 -45.353 1   47.14 ? 355 LEU   A CA  1 
ATOM   2859 C  C   . LEU   A 1 370 ? 16.713  -33.938 -46.632 1   47.99 ? 355 LEU   A C   1 
ATOM   2860 O  O   . LEU   A 1 370 ? 16.611  -33.294 -47.679 1   47.76 ? 355 LEU   A O   1 
ATOM   2861 C  CB  . LEU   A 1 370 ? 18.543  -33.645 -44.958 1   48.14 ? 355 LEU   A CB  1 
ATOM   2862 C  CG  . LEU   A 1 370 ? 19.283  -32.86  -43.88  1   51.3  ? 355 LEU   A CG  1 
ATOM   2863 C  CD1 . LEU   A 1 370 ? 20.772  -33.141 -44.006 1   52.41 ? 355 LEU   A CD1 1 
ATOM   2864 C  CD2 . LEU   A 1 370 ? 19.009  -31.341 -43.966 1   51.99 ? 355 LEU   A CD2 1 
ATOM   2865 N  N   . ILE   A 1 371 ? 16.474  -35.249 -46.554 1   48.37 ? 356 ILE   A N   1 
ATOM   2866 C  CA  . ILE   A 1 371 ? 16.083  -36.031 -47.704 1   49.25 ? 356 ILE   A CA  1 
ATOM   2867 C  C   . ILE   A 1 371 ? 14.737  -35.545 -48.263 1   50.35 ? 356 ILE   A C   1 
ATOM   2868 O  O   . ILE   A 1 371 ? 14.733  -35.14  -49.424 1   50.96 ? 356 ILE   A O   1 
ATOM   2869 C  CB  . ILE   A 1 371 ? 16.152  -37.538 -47.39  1   49.84 ? 356 ILE   A CB  1 
ATOM   2870 C  CG1 . ILE   A 1 371 ? 17.628  -37.957 -47.23  1   50.67 ? 356 ILE   A CG1 1 
ATOM   2871 C  CG2 . ILE   A 1 371 ? 15.453  -38.359 -48.476 1   50.42 ? 356 ILE   A CG2 1 
ATOM   2872 C  CD1 . ILE   A 1 371 ? 17.838  -39.334 -46.717 1   51.58 ? 356 ILE   A CD1 1 
ATOM   2873 N  N   . PRO   A 1 372 ? 13.643  -35.405 -47.469 1   50.54 ? 357 PRO   A N   1 
ATOM   2874 C  CA  . PRO   A 1 372 ? 12.394  -34.873 -48.043 1   51.22 ? 357 PRO   A CA  1 
ATOM   2875 C  C   . PRO   A 1 372 ? 12.518  -33.48  -48.667 1   52.42 ? 357 PRO   A C   1 
ATOM   2876 O  O   . PRO   A 1 372 ? 11.901  -33.239 -49.701 1   52.7  ? 357 PRO   A O   1 
ATOM   2877 C  CB  . PRO   A 1 372 ? 11.422  -34.889 -46.849 1   51.37 ? 357 PRO   A CB  1 
ATOM   2878 C  CG  . PRO   A 1 372 ? 11.956  -35.96  -45.948 1   51.55 ? 357 PRO   A CG  1 
ATOM   2879 C  CD  . PRO   A 1 372 ? 13.443  -35.802 -46.057 1   50    ? 357 PRO   A CD  1 
ATOM   2880 N  N   . ALA   A 1 373 ? 13.332  -32.581 -48.083 1   53.16 ? 358 ALA   A N   1 
ATOM   2881 C  CA  . ALA   A 1 373 ? 13.533  -31.239 -48.651 1   54.83 ? 358 ALA   A CA  1 
ATOM   2882 C  C   . ALA   A 1 373 ? 14.15   -31.288 -50.044 1   57.38 ? 358 ALA   A C   1 
ATOM   2883 O  O   . ALA   A 1 373 ? 13.881  -30.405 -50.864 1   57.62 ? 358 ALA   A O   1 
ATOM   2884 C  CB  . ALA   A 1 373 ? 14.407  -30.386 -47.742 1   54.37 ? 358 ALA   A CB  1 
ATOM   2885 N  N   . SER   A 1 374 ? 14.997  -32.306 -50.299 1   58.86 ? 359 SER   A N   1 
ATOM   2886 C  CA  . SER   A 1 374 ? 15.672  -32.5   -51.581 1   60.66 ? 359 SER   A CA  1 
ATOM   2887 C  C   . SER   A 1 374 ? 14.748  -33.107 -52.665 1   62.61 ? 359 SER   A C   1 
ATOM   2888 O  O   . SER   A 1 374 ? 15.102  -33.06  -53.844 1   63.41 ? 359 SER   A O   1 
ATOM   2889 C  CB  . SER   A 1 374 ? 16.914  -33.374 -51.398 1   61.19 ? 359 SER   A CB  1 
ATOM   2890 O  OG  . SER   A 1 374 ? 16.581  -34.741 -51.209 1   62.51 ? 359 SER   A OG  1 
ATOM   2891 N  N   . GLN   A 1 375 ? 13.581  -33.665 -52.275 1   63.03 ? 360 GLN   A N   1 
ATOM   2892 C  CA  . GLN   A 1 375 ? 12.631  -34.307 -53.191 1   63.62 ? 360 GLN   A CA  1 
ATOM   2893 C  C   . GLN   A 1 375 ? 11.324  -33.518 -53.416 1   64.4  ? 360 GLN   A C   1 
ATOM   2894 O  O   . GLN   A 1 375 ? 11.253  -32.305 -53.205 1   64.85 ? 360 GLN   A O   1 
ATOM   2895 C  CB  . GLN   A 1 375 ? 12.299  -35.721 -52.684 1   64.39 ? 360 GLN   A CB  1 
ATOM   2896 C  CG  . GLN   A 1 375 ? 13.528  -36.572 -52.386 1   66.44 ? 360 GLN   A CG  1 
ATOM   2897 C  CD  . GLN   A 1 375 ? 13.159  -37.858 -51.682 1   69.83 ? 360 GLN   A CD  1 
ATOM   2898 O  OE1 . GLN   A 1 375 ? 12.185  -37.923 -50.921 1   70.67 ? 360 GLN   A OE1 1 
ATOM   2899 N  NE2 . GLN   A 1 375 ? 13.943  -38.909 -51.906 1   70.19 ? 360 GLN   A NE2 1 
ATOM   2900 N  N   . GLY   A 1 396 ? 17.125  -26.104 -44.131 1   58.23 ? 381 GLY   A N   1 
ATOM   2901 C  CA  . GLY   A 1 396 ? 17.539  -27.496 -43.965 1   58.52 ? 381 GLY   A CA  1 
ATOM   2902 C  C   . GLY   A 1 396 ? 18.991  -27.592 -43.547 1   58.63 ? 381 GLY   A C   1 
ATOM   2903 O  O   . GLY   A 1 396 ? 19.318  -28.172 -42.504 1   59.2  ? 381 GLY   A O   1 
ATOM   2904 N  N   . THR   A 1 397 ? 19.87   -26.982 -44.346 1   57.7  ? 382 THR   A N   1 
ATOM   2905 C  CA  . THR   A 1 397 ? 21.288  -26.963 -44.031 1   57.25 ? 382 THR   A CA  1 
ATOM   2906 C  C   . THR   A 1 397 ? 21.559  -26.068 -42.813 1   55.63 ? 382 THR   A C   1 
ATOM   2907 O  O   . THR   A 1 397 ? 22.46   -26.386 -42.047 1   55.67 ? 382 THR   A O   1 
ATOM   2908 C  CB  . THR   A 1 397 ? 22.141  -26.634 -45.258 1   59.39 ? 382 THR   A CB  1 
ATOM   2909 O  OG1 . THR   A 1 397 ? 21.962  -25.256 -45.586 1   61.2  ? 382 THR   A OG1 1 
ATOM   2910 C  CG2 . THR   A 1 397 ? 21.83   -27.541 -46.442 1   59.49 ? 382 THR   A CG2 1 
ATOM   2911 N  N   A ASP   A 1 398 ? 20.772  -24.988 -42.614 0.5 54.93 ? 383 ASP   A N   1 
ATOM   2912 N  N   B ASP   A 1 398 ? 20.775  -24.983 -42.618 0.5 54.8  ? 383 ASP   A N   1 
ATOM   2913 C  CA  A ASP   A 1 398 ? 20.902  -24.112 -41.44  0.5 54.62 ? 383 ASP   A CA  1 
ATOM   2914 C  CA  B ASP   A 1 398 ? 20.923  -24.106 -41.448 0.5 54.34 ? 383 ASP   A CA  1 
ATOM   2915 C  C   A ASP   A 1 398 ? 20.547  -24.887 -40.157 0.5 53.71 ? 383 ASP   A C   1 
ATOM   2916 C  C   B ASP   A 1 398 ? 20.511  -24.839 -40.151 0.5 53.59 ? 383 ASP   A C   1 
ATOM   2917 O  O   A ASP   A 1 398 ? 21.147  -24.657 -39.104 0.5 53.72 ? 383 ASP   A O   1 
ATOM   2918 O  O   B ASP   A 1 398 ? 21.057  -24.552 -39.083 0.5 53.62 ? 383 ASP   A O   1 
ATOM   2919 C  CB  A ASP   A 1 398 ? 19.98   -22.883 -41.579 0.5 56.61 ? 383 ASP   A CB  1 
ATOM   2920 C  CB  B ASP   A 1 398 ? 20.116  -22.802 -41.616 0.5 55.89 ? 383 ASP   A CB  1 
ATOM   2921 C  CG  A ASP   A 1 398 ? 19.949  -21.975 -40.363 0.5 61.4  ? 383 ASP   A CG  1 
ATOM   2922 C  CG  B ASP   A 1 398 ? 20.787  -21.73  -42.464 0.5 59.58 ? 383 ASP   A CG  1 
ATOM   2923 O  OD1 A ASP   A 1 398 ? 20.985  -21.342 -40.068 0.5 61.95 ? 383 ASP   A OD1 1 
ATOM   2924 O  OD1 B ASP   A 1 398 ? 21.918  -21.969 -42.944 0.5 59.93 ? 383 ASP   A OD1 1 
ATOM   2925 O  OD2 A ASP   A 1 398 ? 18.89   -21.908 -39.698 0.5 64.04 ? 383 ASP   A OD2 1 
ATOM   2926 O  OD2 B ASP   A 1 398 ? 20.181  -20.652 -42.646 0.5 61.2  ? 383 ASP   A OD2 1 
ATOM   2927 N  N   . LEU   A 1 399 ? 19.556  -25.785 -40.251 1   52.63 ? 384 LEU   A N   1 
ATOM   2928 C  CA  . LEU   A 1 399 ? 19.116  -26.607 -39.127 1   51.1  ? 384 LEU   A CA  1 
ATOM   2929 C  C   . LEU   A 1 399 ? 20.246  -27.585 -38.783 1   49.08 ? 384 LEU   A C   1 
ATOM   2930 O  O   . LEU   A 1 399 ? 20.553  -27.756 -37.608 1   47.58 ? 384 LEU   A O   1 
ATOM   2931 C  CB  . LEU   A 1 399 ? 17.849  -27.417 -39.493 1   50.68 ? 384 LEU   A CB  1 
ATOM   2932 C  CG  . LEU   A 1 399 ? 16.587  -26.621 -39.719 1   52.08 ? 384 LEU   A CG  1 
ATOM   2933 C  CD1 . LEU   A 1 399 ? 15.439  -27.534 -40.098 1   52.51 ? 384 LEU   A CD1 1 
ATOM   2934 C  CD2 . LEU   A 1 399 ? 16.217  -25.805 -38.484 1   52.76 ? 384 LEU   A CD2 1 
ATOM   2935 N  N   . MET   A 1 400 ? 20.856  -28.214 -39.819 1   48.37 ? 385 MET   A N   1 
ATOM   2936 C  CA  . MET   A 1 400 ? 21.938  -29.168 -39.637 1   48.33 ? 385 MET   A CA  1 
ATOM   2937 C  C   . MET   A 1 400 ? 23.15   -28.509 -39.048 1   47.1  ? 385 MET   A C   1 
ATOM   2938 O  O   . MET   A 1 400 ? 23.777  -29.101 -38.194 1   47.78 ? 385 MET   A O   1 
ATOM   2939 C  CB  . MET   A 1 400 ? 22.306  -29.869 -40.948 1   49.32 ? 385 MET   A CB  1 
ATOM   2940 C  CG  . MET   A 1 400 ? 21.21   -30.721 -41.474 1   51.75 ? 385 MET   A CG  1 
ATOM   2941 S  SD  . MET   A 1 400 ? 20.791  -32.174 -40.455 1   61.33 ? 385 MET   A SD  1 
ATOM   2942 C  CE  . MET   A 1 400 ? 22.151  -33.209 -40.727 1   61.57 ? 385 MET   A CE  1 
ATOM   2943 N  N   . ASN   A 1 401 ? 23.485  -27.298 -39.483 1   45.14 ? 386 ASN   A N   1 
ATOM   2944 C  CA  . ASN   A 1 401 ? 24.633  -26.578 -38.956 1   44.22 ? 386 ASN   A CA  1 
ATOM   2945 C  C   . ASN   A 1 401 ? 24.448  -26.24  -37.477 1   41.54 ? 386 ASN   A C   1 
ATOM   2946 O  O   . ASN   A 1 401 ? 25.408  -26.315 -36.698 1   41.46 ? 386 ASN   A O   1 
ATOM   2947 C  CB  . ASN   A 1 401 ? 24.908  -25.317 -39.774 1   47.46 ? 386 ASN   A CB  1 
ATOM   2948 C  CG  . ASN   A 1 401 ? 25.533  -25.608 -41.119 1   54.61 ? 386 ASN   A CG  1 
ATOM   2949 O  OD1 . ASN   A 1 401 ? 26.016  -26.725 -41.389 1   57.03 ? 386 ASN   A OD1 1 
ATOM   2950 N  ND2 . ASN   A 1 401 ? 25.503  -24.616 -42.005 1   56.65 ? 386 ASN   A ND2 1 
ATOM   2951 N  N   . PHE   A 1 402 ? 23.206  -25.911 -37.068 1   38.69 ? 387 PHE   A N   1 
ATOM   2952 C  CA  . PHE   A 1 402 ? 22.927  -25.646 -35.659 1   36.59 ? 387 PHE   A CA  1 
ATOM   2953 C  C   . PHE   A 1 402 ? 23.127  -26.941 -34.87  1   35.44 ? 387 PHE   A C   1 
ATOM   2954 O  O   . PHE   A 1 402 ? 23.835  -26.935 -33.868 1   36.4  ? 387 PHE   A O   1 
ATOM   2955 C  CB  . PHE   A 1 402 ? 21.495  -25.094 -35.456 1   35.41 ? 387 PHE   A CB  1 
ATOM   2956 C  CG  . PHE   A 1 402 ? 20.983  -25.204 -34.025 1   34.36 ? 387 PHE   A CG  1 
ATOM   2957 C  CD1 . PHE   A 1 402 ? 21.439  -24.342 -33.04  1   33.77 ? 387 PHE   A CD1 1 
ATOM   2958 C  CD2 . PHE   A 1 402 ? 20.032  -26.153 -33.684 1   34.08 ? 387 PHE   A CD2 1 
ATOM   2959 C  CE1 . PHE   A 1 402 ? 20.978  -24.444 -31.733 1   34.3  ? 387 PHE   A CE1 1 
ATOM   2960 C  CE2 . PHE   A 1 402 ? 19.563  -26.255 -32.385 1   34.38 ? 387 PHE   A CE2 1 
ATOM   2961 C  CZ  . PHE   A 1 402 ? 20.036  -25.402 -31.41  1   34.3  ? 387 PHE   A CZ  1 
ATOM   2962 N  N   . LEU   A 1 403 ? 22.543  -28.039 -35.343 1   33.14 ? 388 LEU   A N   1 
ATOM   2963 C  CA  . LEU   A 1 403 ? 22.635  -29.309 -34.656 1   33.4  ? 388 LEU   A CA  1 
ATOM   2964 C  C   . LEU   A 1 403 ? 24.083  -29.835 -34.579 1   33.63 ? 388 LEU   A C   1 
ATOM   2965 O  O   . LEU   A 1 403 ? 24.475  -30.422 -33.574 1   32.56 ? 388 LEU   A O   1 
ATOM   2966 C  CB  . LEU   A 1 403 ? 21.711  -30.323 -35.332 1   33.11 ? 388 LEU   A CB  1 
ATOM   2967 C  CG  . LEU   A 1 403 ? 20.2    -30.08  -35.126 1   34.52 ? 388 LEU   A CG  1 
ATOM   2968 C  CD1 . LEU   A 1 403 ? 19.415  -31.136 -35.817 1   34.86 ? 388 LEU   A CD1 1 
ATOM   2969 C  CD2 . LEU   A 1 403 ? 19.819  -30.076 -33.625 1   34.85 ? 388 LEU   A CD2 1 
ATOM   2970 N  N   . LYS   A 1 404 ? 24.854  -29.631 -35.652 1   33.97 ? 389 LYS   A N   1 
ATOM   2971 C  CA  . LYS   A 1 404 ? 26.25   -30.035 -35.729 1   34.49 ? 389 LYS   A CA  1 
ATOM   2972 C  C   . LYS   A 1 404 ? 27.12   -29.205 -34.813 1   34.02 ? 389 LYS   A C   1 
ATOM   2973 O  O   . LYS   A 1 404 ? 28.026  -29.762 -34.238 1   34.33 ? 389 LYS   A O   1 
ATOM   2974 C  CB  . LYS   A 1 404 ? 26.756  -30.018 -37.172 1   37.25 ? 389 LYS   A CB  1 
ATOM   2975 C  CG  . LYS   A 1 404 ? 26.254  -31.223 -37.943 1   42.9  ? 389 LYS   A CG  1 
ATOM   2976 C  CD  . LYS   A 1 404 ? 26.198  -31.003 -39.462 1   49.92 ? 389 LYS   A CD  1 
ATOM   2977 C  CE  . LYS   A 1 404 ? 27.448  -30.456 -40.1   1   55.88 ? 389 LYS   A CE  1 
ATOM   2978 N  NZ  . LYS   A 1 404 ? 27.422  -30.67  -41.577 1   59.73 ? 389 LYS   A NZ  1 
ATOM   2979 N  N   . THR   A 1 405 ? 26.805  -27.922 -34.601 1   33.73 ? 390 THR   A N   1 
ATOM   2980 C  CA  . THR   A 1 405 ? 27.529  -27.056 -33.68  1   34.51 ? 390 THR   A CA  1 
ATOM   2981 C  C   . THR   A 1 405 ? 27.28   -27.524 -32.234 1   35.16 ? 390 THR   A C   1 
ATOM   2982 O  O   . THR   A 1 405 ? 28.223  -27.681 -31.462 1   35.41 ? 390 THR   A O   1 
ATOM   2983 C  CB  . THR   A 1 405 ? 27.085  -25.603 -33.887 1   36.8  ? 390 THR   A CB  1 
ATOM   2984 O  OG1 . THR   A 1 405 ? 27.564  -25.17  -35.153 1   39.76 ? 390 THR   A OG1 1 
ATOM   2985 C  CG2 . THR   A 1 405 ? 27.579  -24.663 -32.804 1   35.97 ? 390 THR   A CG2 1 
ATOM   2986 N  N   . VAL   A 1 406 ? 26.021  -27.8   -31.89  1   34.49 ? 391 VAL   A N   1 
ATOM   2987 C  CA  . VAL   A 1 406 ? 25.655  -28.285 -30.562 1   34.35 ? 391 VAL   A CA  1 
ATOM   2988 C  C   . VAL   A 1 406 ? 26.337  -29.642 -30.303 1   33.77 ? 391 VAL   A C   1 
ATOM   2989 O  O   . VAL   A 1 406 ? 26.921  -29.853 -29.232 1   33.45 ? 391 VAL   A O   1 
ATOM   2990 C  CB  . VAL   A 1 406 ? 24.105  -28.381 -30.419 1   33.89 ? 391 VAL   A CB  1 
ATOM   2991 C  CG1 . VAL   A 1 406 ? 23.723  -29.041 -29.088 1   33.85 ? 391 VAL   A CG1 1 
ATOM   2992 C  CG2 . VAL   A 1 406 ? 23.455  -26.992 -30.536 1   33.4  ? 391 VAL   A CG2 1 
ATOM   2993 N  N   . ARG   A 1 407 ? 26.271  -30.541 -31.286 1   32.92 ? 392 ARG   A N   1 
ATOM   2994 C  CA  . ARG   A 1 407 ? 26.901  -31.848 -31.157 1   33.52 ? 392 ARG   A CA  1 
ATOM   2995 C  C   . ARG   A 1 407 ? 28.427  -31.721 -31.011 1   34.39 ? 392 ARG   A C   1 
ATOM   2996 O  O   . ARG   A 1 407 ? 29.013  -32.388 -30.168 1   34.21 ? 392 ARG   A O   1 
ATOM   2997 C  CB  . ARG   A 1 407 ? 26.583  -32.762 -32.345 1   33.83 ? 392 ARG   A CB  1 
ATOM   2998 C  CG  . ARG   A 1 407 ? 27.17   -34.139 -32.108 1   35.7  ? 392 ARG   A CG  1 
ATOM   2999 C  CD  . ARG   A 1 407 ? 27.325  -35.015 -33.334 1   39.79 ? 392 ARG   A CD  1 
ATOM   3000 N  NE  . ARG   A 1 407 ? 28.296  -36.078 -33.058 1   41.14 ? 392 ARG   A NE  1 
ATOM   3001 C  CZ  . ARG   A 1 407 ? 29.615  -35.924 -33.136 1   41.3  ? 392 ARG   A CZ  1 
ATOM   3002 N  NH1 . ARG   A 1 407 ? 30.133  -34.782 -33.578 1   39.34 ? 392 ARG   A NH1 1 
ATOM   3003 N  NH2 . ARG   A 1 407 ? 30.426  -36.911 -32.773 1   41.13 ? 392 ARG   A NH2 1 
ATOM   3004 N  N   . SER   A 1 408 ? 29.047  -30.847 -31.809 1   34.65 ? 393 SER   A N   1 
ATOM   3005 C  CA  . SER   A 1 408 ? 30.492  -30.618 -31.815 1   35.89 ? 393 SER   A CA  1 
ATOM   3006 C  C   . SER   A 1 408 ? 30.981  -30.053 -30.495 1   35.67 ? 393 SER   A C   1 
ATOM   3007 O  O   . SER   A 1 408 ? 32.026  -30.482 -30.01  1   35.84 ? 393 SER   A O   1 
ATOM   3008 C  CB  . SER   A 1 408 ? 30.883  -29.694 -32.977 1   38.62 ? 393 SER   A CB  1 
ATOM   3009 O  OG  . SER   A 1 408 ? 32.157  -29.097 -32.782 1   42.94 ? 393 SER   A OG  1 
ATOM   3010 N  N   . THR   A 1 409 ? 30.246  -29.084 -29.922 1   34.81 ? 394 THR   A N   1 
ATOM   3011 C  CA  . THR   A 1 409 ? 30.548  -28.478 -28.626 1   34.68 ? 394 THR   A CA  1 
ATOM   3012 C  C   . THR   A 1 409 ? 30.498  -29.588 -27.561 1   33.57 ? 394 THR   A C   1 
ATOM   3013 O  O   . THR   A 1 409 ? 31.376  -29.642 -26.701 1   33.3  ? 394 THR   A O   1 
ATOM   3014 C  CB  . THR   A 1 409 ? 29.532  -27.349 -28.339 1   37.61 ? 394 THR   A CB  1 
ATOM   3015 O  OG1 . THR   A 1 409 ? 29.622  -26.388 -29.39  1   40.13 ? 394 THR   A OG1 1 
ATOM   3016 C  CG2 . THR   A 1 409 ? 29.776  -26.651 -27.023 1   37.66 ? 394 THR   A CG2 1 
ATOM   3017 N  N   . THR   A 1 410 ? 29.52   -30.522 -27.678 1   32.22 ? 395 THR   A N   1 
ATOM   3018 C  CA  . THR   A 1 410 ? 29.425  -31.65  -26.763 1   32.06 ? 395 THR   A CA  1 
ATOM   3019 C  C   . THR   A 1 410 ? 30.634  -32.579 -26.91  1   32.32 ? 395 THR   A C   1 
ATOM   3020 O  O   . THR   A 1 410 ? 31.228  -32.937 -25.906 1   31.97 ? 395 THR   A O   1 
ATOM   3021 C  CB  . THR   A 1 410 ? 28.117  -32.445 -26.965 1   31.03 ? 395 THR   A CB  1 
ATOM   3022 O  OG1 . THR   A 1 410 ? 27.011  -31.549 -27.116 1   31.11 ? 395 THR   A OG1 1 
ATOM   3023 C  CG2 . THR   A 1 410 ? 27.857  -33.395 -25.824 1   30.06 ? 395 THR   A CG2 1 
ATOM   3024 N  N   . GLU   A 1 411 ? 30.976  -32.996 -28.144 1   32.56 ? 396 GLU   A N   1 
ATOM   3025 C  CA  . GLU   A 1 411 ? 32.097  -33.916 -28.387 1   33.53 ? 396 GLU   A CA  1 
ATOM   3026 C  C   . GLU   A 1 411 ? 33.413  -33.301 -27.914 1   33.66 ? 396 GLU   A C   1 
ATOM   3027 O  O   . GLU   A 1 411 ? 34.234  -34.001 -27.329 1   33.13 ? 396 GLU   A O   1 
ATOM   3028 C  CB  . GLU   A 1 411 ? 32.179  -34.308 -29.879 1   36.36 ? 396 GLU   A CB  1 
ATOM   3029 C  CG  . GLU   A 1 411 ? 33.044  -35.534 -30.145 1   41.65 ? 396 GLU   A CG  1 
ATOM   3030 C  CD  . GLU   A 1 411 ? 34.531  -35.255 -30.318 1   45.44 ? 396 GLU   A CD  1 
ATOM   3031 O  OE1 . GLU   A 1 411 ? 34.884  -34.085 -30.596 1   44.95 ? 396 GLU   A OE1 1 
ATOM   3032 O  OE2 . GLU   A 1 411 ? 35.343  -36.198 -30.151 1   47.24 ? 396 GLU   A OE2 1 
ATOM   3033 N  N   . LYS   A 1 412 ? 33.606  -31.996 -28.137 1   34.11 ? 397 LYS   A N   1 
ATOM   3034 C  CA  . LYS   A 1 412 ? 34.819  -31.32  -27.706 1   35.47 ? 397 LYS   A CA  1 
ATOM   3035 C  C   . LYS   A 1 412 ? 34.94   -31.158 -26.182 1   36.16 ? 397 LYS   A C   1 
ATOM   3036 O  O   . LYS   A 1 412 ? 35.999  -30.761 -25.71  1   35.98 ? 397 LYS   A O   1 
ATOM   3037 C  CB  . LYS   A 1 412 ? 34.994  -29.978 -28.425 1   38.32 ? 397 LYS   A CB  1 
ATOM   3038 C  CG  . LYS   A 1 412 ? 35.294  -30.152 -29.921 1   42.59 ? 397 LYS   A CG  1 
ATOM   3039 C  CD  . LYS   A 1 412 ? 35.444  -28.808 -30.629 1   47.97 ? 397 LYS   A CD  1 
ATOM   3040 C  CE  . LYS   A 1 412 ? 35.968  -28.945 -32.044 1   51.88 ? 397 LYS   A CE  1 
ATOM   3041 N  NZ  . LYS   A 1 412 ? 34.979  -29.603 -32.942 1   54.2  ? 397 LYS   A NZ  1 
ATOM   3042 N  N   . SER   A 1 413 ? 33.88   -31.482 -25.416 1   36.39 ? 398 SER   A N   1 
ATOM   3043 C  CA  . SER   A 1 413 ? 33.886  -31.447 -23.943 1   35.89 ? 398 SER   A CA  1 
ATOM   3044 C  C   . SER   A 1 413 ? 34.41   -32.741 -23.334 1   35.05 ? 398 SER   A C   1 
ATOM   3045 O  O   . SER   A 1 413 ? 34.627  -32.791 -22.128 1   34.39 ? 398 SER   A O   1 
ATOM   3046 C  CB  . SER   A 1 413 ? 32.488  -31.189 -23.392 1   37.36 ? 398 SER   A CB  1 
ATOM   3047 O  OG  . SER   A 1 413 ? 32.076  -29.884 -23.753 1   40.32 ? 398 SER   A OG  1 
ATOM   3048 N  N   . LEU   A 1 414 ? 34.592  -33.805 -24.139 1   35.36 ? 399 LEU   A N   1 
ATOM   3049 C  CA  . LEU   A 1 414 ? 35.156  -35.058 -23.653 1   36.28 ? 399 LEU   A CA  1 
ATOM   3050 C  C   . LEU   A 1 414 ? 36.584  -34.787 -23.183 1   38.22 ? 399 LEU   A C   1 
ATOM   3051 O  O   . LEU   A 1 414 ? 37.303  -34.014 -23.81  1   38.04 ? 399 LEU   A O   1 
ATOM   3052 C  CB  . LEU   A 1 414 ? 35.178  -36.132 -24.753 1   35.6  ? 399 LEU   A CB  1 
ATOM   3053 C  CG  . LEU   A 1 414 ? 33.839  -36.761 -25.124 1   36.37 ? 399 LEU   A CG  1 
ATOM   3054 C  CD1 . LEU   A 1 414 ? 33.941  -37.541 -26.449 1   36.35 ? 399 LEU   A CD1 1 
ATOM   3055 C  CD2 . LEU   A 1 414 ? 33.331  -37.651 -24.01  1   36.31 ? 399 LEU   A CD2 1 
ATOM   3056 N  N   . LEU   A 1 415 ? 36.941  -35.319 -22.031 1   39.99 ? 400 LEU   A N   1 
ATOM   3057 C  CA  . LEU   A 1 415 ? 38.278  -35.155 -21.483 1   42.15 ? 400 LEU   A CA  1 
ATOM   3058 C  C   . LEU   A 1 415 ? 39.247  -36.048 -22.269 1   44.44 ? 400 LEU   A C   1 
ATOM   3059 O  O   . LEU   A 1 415 ? 40.312  -35.584 -22.648 1   45.37 ? 400 LEU   A O   1 
ATOM   3060 C  CB  . LEU   A 1 415 ? 38.277  -35.442 -19.972 1   42.04 ? 400 LEU   A CB  1 
ATOM   3061 C  CG  . LEU   A 1 415 ? 37.273  -34.604 -19.159 1   42.93 ? 400 LEU   A CG  1 
ATOM   3062 C  CD1 . LEU   A 1 415 ? 37.327  -34.941 -17.679 1   43.4  ? 400 LEU   A CD1 1 
ATOM   3063 C  CD2 . LEU   A 1 415 ? 37.472  -33.104 -19.374 1   43.43 ? 400 LEU   A CD2 1 
ATOM   3064 N  N   . LYS   A 1 416 ? 38.829  -37.266 -22.615 1   45.28 ? 401 LYS   A N   1 
ATOM   3065 C  CA  . LYS   A 1 416 ? 39.589  -38.206 -23.445 1   47.12 ? 401 LYS   A CA  1 
ATOM   3066 C  C   . LYS   A 1 416 ? 38.732  -38.489 -24.7   1   48.54 ? 401 LYS   A C   1 
ATOM   3067 O  O   . LYS   A 1 416 ? 37.503  -38.614 -24.583 1   48.71 ? 401 LYS   A O   1 
ATOM   3068 C  CB  . LYS   A 1 416 ? 39.841  -39.513 -22.657 1   49.86 ? 401 LYS   A CB  1 
ATOM   3069 C  CG  . LYS   A 1 416 ? 40.952  -40.368 -23.212 1   55.67 ? 401 LYS   A CG  1 
ATOM   3070 C  CD  . LYS   A 1 416 ? 41.484  -41.323 -22.152 1   61.77 ? 401 LYS   A CD  1 
ATOM   3071 C  CE  . LYS   A 1 416 ? 40.602  -42.536 -21.971 1   66.24 ? 401 LYS   A CE  1 
ATOM   3072 N  NZ  . LYS   A 1 416 ? 41.208  -43.529 -21.037 1   68.62 ? 401 LYS   A NZ  1 
ATOM   3073 N  N   . GLU   A 1 417 ? 39.341  -38.589 -25.904 1   49.35 ? 402 GLU   A N   1 
ATOM   3074 C  CA  . GLU   A 1 417 ? 38.549  -38.845 -27.124 1   50.09 ? 402 GLU   A CA  1 
ATOM   3075 C  C   . GLU   A 1 417 ? 37.677  -40.107 -27.022 1   50.59 ? 402 GLU   A C   1 
ATOM   3076 O  O   . GLU   A 1 417 ? 38.113  -41.098 -26.43  1   50.79 ? 402 GLU   A O   1 
ATOM   3077 C  CB  . GLU   A 1 417 ? 39.445  -38.928 -28.364 1   51.61 ? 402 GLU   A CB  1 
ATOM   3078 C  CG  . GLU   A 1 417 ? 40.291  -37.692 -28.591 1   54.99 ? 402 GLU   A CG  1 
ATOM   3079 C  CD  . GLU   A 1 417 ? 41.357  -37.875 -29.658 1   58.73 ? 402 GLU   A CD  1 
ATOM   3080 O  OE1 . GLU   A 1 417 ? 41.255  -38.832 -30.465 1   56.37 ? 402 GLU   A OE1 1 
ATOM   3081 O  OE2 . GLU   A 1 417 ? 42.297  -37.048 -29.689 1   61.56 ? 402 GLU   A OE2 1 
ATOM   3082 N  N   . THR   B 1 25  ? 20.697  -11.908 6.172   1   57.18 ? 10  THR   B N   1 
ATOM   3083 C  CA  . THR   B 1 25  ? 21.557  -11.155 5.255   1   57.59 ? 10  THR   B CA  1 
ATOM   3084 C  C   . THR   B 1 25  ? 21.946  -11.967 4.01    1   56.15 ? 10  THR   B C   1 
ATOM   3085 O  O   . THR   B 1 25  ? 22.066  -13.197 4.074   1   56.19 ? 10  THR   B O   1 
ATOM   3086 C  CB  . THR   B 1 25  ? 22.829  -10.651 5.966   1   60.11 ? 10  THR   B CB  1 
ATOM   3087 O  OG1 . THR   B 1 25  ? 23.678  -11.756 6.289   1   61.44 ? 10  THR   B OG1 1 
ATOM   3088 C  CG2 . THR   B 1 25  ? 22.524  -9.83   7.216   1   61.04 ? 10  THR   B CG2 1 
ATOM   3089 N  N   . ILE   B 1 26  ? 22.201  -11.255 2.906   1   54.33 ? 11  ILE   B N   1 
ATOM   3090 C  CA  . ILE   B 1 26  ? 22.62   -11.788 1.595   1   52.48 ? 11  ILE   B CA  1 
ATOM   3091 C  C   . ILE   B 1 26  ? 23.995  -12.486 1.66    1   49.95 ? 11  ILE   B C   1 
ATOM   3092 O  O   . ILE   B 1 26  ? 24.933  -11.934 2.226   1   49.94 ? 11  ILE   B O   1 
ATOM   3093 C  CB  . ILE   B 1 26  ? 22.577  -10.603 0.598   1   52.87 ? 11  ILE   B CB  1 
ATOM   3094 C  CG1 . ILE   B 1 26  ? 21.119  -10.254 0.241   1   53.45 ? 11  ILE   B CG1 1 
ATOM   3095 C  CG2 . ILE   B 1 26  ? 23.448  -10.818 -0.645  1   53.29 ? 11  ILE   B CG2 1 
ATOM   3096 C  CD1 . ILE   B 1 26  ? 20.93   -8.898  -0.057  1   54.68 ? 11  ILE   B CD1 1 
ATOM   3097 N  N   . SER   B 1 27  ? 24.076  -13.719 1.135   1   48.02 ? 12  SER   B N   1 
ATOM   3098 C  CA  . SER   B 1 27  ? 25.28   -14.541 1.105   1   47.33 ? 12  SER   B CA  1 
ATOM   3099 C  C   . SER   B 1 27  ? 26.466  -13.823 0.507   1   46.29 ? 12  SER   B C   1 
ATOM   3100 O  O   . SER   B 1 27  ? 26.335  -13.122 -0.505  1   46.2  ? 12  SER   B O   1 
ATOM   3101 C  CB  . SER   B 1 27  ? 25.034  -15.804 0.294   1   48.16 ? 12  SER   B CB  1 
ATOM   3102 O  OG  . SER   B 1 27  ? 26.21   -16.592 0.187   1   51.36 ? 12  SER   B OG  1 
ATOM   3103 N  N   . LYS   B 1 28  ? 27.628  -14.038 1.11    1   45.2  ? 13  LYS   B N   1 
ATOM   3104 C  CA  . LYS   B 1 28  ? 28.89   -13.477 0.638   1   44.73 ? 13  LYS   B CA  1 
ATOM   3105 C  C   . LYS   B 1 28  ? 29.3    -14.032 -0.733  1   43.3  ? 13  LYS   B C   1 
ATOM   3106 O  O   . LYS   B 1 28  ? 30.085  -13.401 -1.433  1   43.32 ? 13  LYS   B O   1 
ATOM   3107 C  CB  . LYS   B 1 28  ? 29.999  -13.67  1.683   1   47.27 ? 13  LYS   B CB  1 
ATOM   3108 C  CG  . LYS   B 1 28  ? 29.807  -12.791 2.911   1   51.5  ? 13  LYS   B CG  1 
ATOM   3109 N  N   . GLU   B 1 29  ? 28.752  -15.189 -1.135  1   42.51 ? 14  GLU   B N   1 
ATOM   3110 C  CA  . GLU   B 1 29  ? 28.986  -15.778 -2.445  1   42.65 ? 14  GLU   B CA  1 
ATOM   3111 C  C   . GLU   B 1 29  ? 28.459  -14.876 -3.61   1   42.22 ? 14  GLU   B C   1 
ATOM   3112 O  O   . GLU   B 1 29  ? 28.808  -15.102 -4.763  1   41.67 ? 14  GLU   B O   1 
ATOM   3113 C  CB  . GLU   B 1 29  ? 28.293  -17.135 -2.523  1   45.8  ? 14  GLU   B CB  1 
ATOM   3114 C  CG  . GLU   B 1 29  ? 28.972  -18.225 -1.731  1   53.47 ? 14  GLU   B CG  1 
ATOM   3115 C  CD  . GLU   B 1 29  ? 28.399  -19.58  -2.074  1   62.74 ? 14  GLU   B CD  1 
ATOM   3116 O  OE1 . GLU   B 1 29  ? 28.543  -20.008 -3.243  1   65.69 ? 14  GLU   B OE1 1 
ATOM   3117 O  OE2 . GLU   B 1 29  ? 27.79   -20.209 -1.181  1   65.62 ? 14  GLU   B OE2 1 
ATOM   3118 N  N   . TYR   B 1 30  ? 27.586  -13.903 -3.314  1   41.62 ? 15  TYR   B N   1 
ATOM   3119 C  CA  . TYR   B 1 30  ? 27.068  -12.99  -4.34   1   41.24 ? 15  TYR   B CA  1 
ATOM   3120 C  C   . TYR   B 1 30  ? 27.978  -11.777 -4.572  1   40.79 ? 15  TYR   B C   1 
ATOM   3121 O  O   . TYR   B 1 30  ? 27.747  -11.027 -5.517  1   40.85 ? 15  TYR   B O   1 
ATOM   3122 C  CB  . TYR   B 1 30  ? 25.648  -12.532 -3.989  1   40.83 ? 15  TYR   B CB  1 
ATOM   3123 C  CG  . TYR   B 1 30  ? 24.655  -13.664 -4.071  1   41.53 ? 15  TYR   B CG  1 
ATOM   3124 C  CD1 . TYR   B 1 30  ? 24.507  -14.396 -5.237  1   41.63 ? 15  TYR   B CD1 1 
ATOM   3125 C  CD2 . TYR   B 1 30  ? 23.887  -14.023 -2.972  1   42.74 ? 15  TYR   B CD2 1 
ATOM   3126 C  CE1 . TYR   B 1 30  ? 23.602  -15.434 -5.32   1   43.06 ? 15  TYR   B CE1 1 
ATOM   3127 C  CE2 . TYR   B 1 30  ? 22.978  -15.067 -3.042  1   43.68 ? 15  TYR   B CE2 1 
ATOM   3128 C  CZ  . TYR   B 1 30  ? 22.846  -15.776 -4.217  1   44.93 ? 15  TYR   B CZ  1 
ATOM   3129 O  OH  . TYR   B 1 30  ? 21.954  -16.812 -4.306  1   47.77 ? 15  TYR   B OH  1 
ATOM   3130 N  N   . HIS   B 1 31  ? 28.961  -11.551 -3.688  1   40.64 ? 16  HIS   B N   1 
ATOM   3131 C  CA  . HIS   B 1 31  ? 29.937  -10.472 -3.788  1   41.36 ? 16  HIS   B CA  1 
ATOM   3132 C  C   . HIS   B 1 31  ? 29.302  -9.099  -3.901  1   41.12 ? 16  HIS   B C   1 
ATOM   3133 O  O   . HIS   B 1 31  ? 29.659  -8.283  -4.757  1   41.45 ? 16  HIS   B O   1 
ATOM   3134 C  CB  . HIS   B 1 31  ? 30.947  -10.747 -4.912  1   42.76 ? 16  HIS   B CB  1 
ATOM   3135 C  CG  . HIS   B 1 31  ? 31.725  -11.993 -4.632  1   47.83 ? 16  HIS   B CG  1 
ATOM   3136 N  ND1 . HIS   B 1 31  ? 32.663  -12.038 -3.617  1   50.37 ? 16  HIS   B ND1 1 
ATOM   3137 C  CD2 . HIS   B 1 31  ? 31.602  -13.229 -5.169  1   49.88 ? 16  HIS   B CD2 1 
ATOM   3138 C  CE1 . HIS   B 1 31  ? 33.102  -13.288 -3.594  1   51.53 ? 16  HIS   B CE1 1 
ATOM   3139 N  NE2 . HIS   B 1 31  ? 32.493  -14.038 -4.514  1   51.47 ? 16  HIS   B NE2 1 
ATOM   3140 N  N   . ILE   B 1 32  ? 28.346  -8.855  -3.007  1   40.38 ? 17  ILE   B N   1 
ATOM   3141 C  CA  . ILE   B 1 32  ? 27.694  -7.582  -2.856  1   40.65 ? 17  ILE   B CA  1 
ATOM   3142 C  C   . ILE   B 1 32  ? 28.303  -7.001  -1.587  1   42.26 ? 17  ILE   B C   1 
ATOM   3143 O  O   . ILE   B 1 32  ? 28.254  -7.625  -0.526  1   43.04 ? 17  ILE   B O   1 
ATOM   3144 C  CB  . ILE   B 1 32  ? 26.161  -7.75   -2.759  1   41.02 ? 17  ILE   B CB  1 
ATOM   3145 C  CG1 . ILE   B 1 32  ? 25.626  -8.455  -4.022  1   41.76 ? 17  ILE   B CG1 1 
ATOM   3146 C  CG2 . ILE   B 1 32  ? 25.48   -6.398  -2.524  1   41.33 ? 17  ILE   B CG2 1 
ATOM   3147 C  CD1 . ILE   B 1 32  ? 24.119  -8.812  -3.999  1   42.87 ? 17  ILE   B CD1 1 
ATOM   3148 N  N   . ASP   B 1 33  ? 28.97   -5.865  -1.711  1   42.32 ? 18  ASP   B N   1 
ATOM   3149 C  CA  . ASP   B 1 33  ? 29.589  -5.19   -0.589  1   42.75 ? 18  ASP   B CA  1 
ATOM   3150 C  C   . ASP   B 1 33  ? 28.536  -4.403  0.188   1   44.62 ? 18  ASP   B C   1 
ATOM   3151 O  O   . ASP   B 1 33  ? 27.58   -3.897  -0.39   1   45.06 ? 18  ASP   B O   1 
ATOM   3152 C  CB  . ASP   B 1 33  ? 30.679  -4.237  -1.086  1   42.71 ? 18  ASP   B CB  1 
ATOM   3153 C  CG  . ASP   B 1 33  ? 31.506  -3.66   0.045   1   43.41 ? 18  ASP   B CG  1 
ATOM   3154 O  OD1 . ASP   B 1 33  ? 32.241  -4.43   0.685   1   44.11 ? 18  ASP   B OD1 1 
ATOM   3155 O  OD2 . ASP   B 1 33  ? 31.391  -2.442  0.304   1   43.5  ? 18  ASP   B OD2 1 
ATOM   3156 N  N   . GLU   B 1 34  ? 28.713  -4.293  1.504   1   45.59 ? 19  GLU   B N   1 
ATOM   3157 C  CA  . GLU   B 1 34  ? 27.769  -3.582  2.372   1   46.64 ? 19  GLU   B CA  1 
ATOM   3158 C  C   . GLU   B 1 34  ? 27.703  -2.101  2.054   1   46.47 ? 19  GLU   B C   1 
ATOM   3159 O  O   . GLU   B 1 34  ? 26.637  -1.5    2.145   1   47.08 ? 19  GLU   B O   1 
ATOM   3160 C  CB  . GLU   B 1 34  ? 28.089  -3.784  3.878   1   49.74 ? 19  GLU   B CB  1 
ATOM   3161 C  CG  . GLU   B 1 34  ? 29.365  -4.554  4.189   1   57.36 ? 19  GLU   B CG  1 
ATOM   3162 C  CD  . GLU   B 1 34  ? 29.352  -5.998  3.722   1   65.34 ? 19  GLU   B CD  1 
ATOM   3163 O  OE1 . GLU   B 1 34  ? 28.409  -6.728  4.106   1   68.57 ? 19  GLU   B OE1 1 
ATOM   3164 O  OE2 . GLU   B 1 34  ? 30.263  -6.388  2.951   1   65.4  ? 19  GLU   B OE2 1 
ATOM   3165 N  N   . GLU   B 1 35  ? 28.838  -1.517  1.676   1   45.37 ? 20  GLU   B N   1 
ATOM   3166 C  CA  . GLU   B 1 35  ? 28.909  -0.101  1.385   1   44.53 ? 20  GLU   B CA  1 
ATOM   3167 C  C   . GLU   B 1 35  ? 28.72   0.24    -0.089  1   43.41 ? 20  GLU   B C   1 
ATOM   3168 O  O   . GLU   B 1 35  ? 27.994  1.183   -0.398  1   43.9  ? 20  GLU   B O   1 
ATOM   3169 C  CB  . GLU   B 1 35  ? 30.257  0.444   1.887   1   47.14 ? 20  GLU   B CB  1 
ATOM   3170 C  CG  . GLU   B 1 35  ? 30.456  1.931   1.668   1   52.38 ? 20  GLU   B CG  1 
ATOM   3171 C  CD  . GLU   B 1 35  ? 31.833  2.434   2.058   1   60.13 ? 20  GLU   B CD  1 
ATOM   3172 O  OE1 . GLU   B 1 35  ? 32.772  1.608   2.138   1   62.49 ? 20  GLU   B OE1 1 
ATOM   3173 O  OE2 . GLU   B 1 35  ? 31.974  3.658   2.283   1   62.13 ? 20  GLU   B OE2 1 
ATOM   3174 N  N   . VAL   B 1 36  ? 29.412  -0.463  -0.998  1   42.26 ? 21  VAL   B N   1 
ATOM   3175 C  CA  . VAL   B 1 36  ? 29.363  -0.09   -2.416  1   41.26 ? 21  VAL   B CA  1 
ATOM   3176 C  C   . VAL   B 1 36  ? 28.511  -0.997  -3.294  1   40.04 ? 21  VAL   B C   1 
ATOM   3177 O  O   . VAL   B 1 36  ? 28.458  -0.76   -4.501  1   40.34 ? 21  VAL   B O   1 
ATOM   3178 C  CB  . VAL   B 1 36  ? 30.784  0.077   -2.996  1   41.63 ? 21  VAL   B CB  1 
ATOM   3179 C  CG1 . VAL   B 1 36  ? 31.535  1.154   -2.233  1   42.7  ? 21  VAL   B CG1 1 
ATOM   3180 C  CG2 . VAL   B 1 36  ? 31.563  -1.232  -2.964  1   41.18 ? 21  VAL   B CG2 1 
ATOM   3181 N  N   . GLY   B 1 37  ? 27.826  -1.974  -2.701  1   38.45 ? 22  GLY   B N   1 
ATOM   3182 C  CA  . GLY   B 1 37  ? 26.924  -2.876  -3.41   1   37.39 ? 22  GLY   B CA  1 
ATOM   3183 C  C   . GLY   B 1 37  ? 27.598  -3.715  -4.461  1   36.18 ? 22  GLY   B C   1 
ATOM   3184 O  O   . GLY   B 1 37  ? 28.506  -4.479  -4.156  1   36    ? 22  GLY   B O   1 
ATOM   3185 N  N   . PHE   B 1 38  ? 27.16   -3.577  -5.711  1   36.26 ? 23  PHE   B N   1 
ATOM   3186 C  CA  . PHE   B 1 38  ? 27.737  -4.323  -6.828  1   36.42 ? 23  PHE   B CA  1 
ATOM   3187 C  C   . PHE   B 1 38  ? 29.108  -3.783  -7.285  1   37.47 ? 23  PHE   B C   1 
ATOM   3188 O  O   . PHE   B 1 38  ? 29.794  -4.472  -8.035  1   37.88 ? 23  PHE   B O   1 
ATOM   3189 C  CB  . PHE   B 1 38  ? 26.766  -4.377  -8.011  1   35.82 ? 23  PHE   B CB  1 
ATOM   3190 C  CG  . PHE   B 1 38  ? 25.575  -5.256  -7.735  1   35.67 ? 23  PHE   B CG  1 
ATOM   3191 C  CD1 . PHE   B 1 38  ? 25.701  -6.633  -7.711  1   35.91 ? 23  PHE   B CD1 1 
ATOM   3192 C  CD2 . PHE   B 1 38  ? 24.329  -4.706  -7.493  1   36.19 ? 23  PHE   B CD2 1 
ATOM   3193 C  CE1 . PHE   B 1 38  ? 24.606  -7.439  -7.442  1   36.04 ? 23  PHE   B CE1 1 
ATOM   3194 C  CE2 . PHE   B 1 38  ? 23.232  -5.521  -7.242  1   36.27 ? 23  PHE   B CE2 1 
ATOM   3195 C  CZ  . PHE   B 1 38  ? 23.386  -6.875  -7.197  1   35.63 ? 23  PHE   B CZ  1 
ATOM   3196 N  N   . ALA   B 1 39  ? 29.507  -2.575  -6.843  1   37.51 ? 24  ALA   B N   1 
ATOM   3197 C  CA  . ALA   B 1 39  ? 30.826  -2.04   -7.177  1   38.59 ? 24  ALA   B CA  1 
ATOM   3198 C  C   . ALA   B 1 39  ? 31.919  -2.875  -6.506  1   40.08 ? 24  ALA   B C   1 
ATOM   3199 O  O   . ALA   B 1 39  ? 31.663  -3.576  -5.521  1   40.33 ? 24  ALA   B O   1 
ATOM   3200 C  CB  . ALA   B 1 39  ? 30.93   -0.588  -6.737  1   38.43 ? 24  ALA   B CB  1 
ATOM   3201 N  N   . LEU   B 1 40  ? 33.127  -2.848  -7.072  1   40.32 ? 25  LEU   B N   1 
ATOM   3202 C  CA  . LEU   B 1 40  ? 34.255  -3.571  -6.504  1   41.34 ? 25  LEU   B CA  1 
ATOM   3203 C  C   . LEU   B 1 40  ? 34.785  -2.728  -5.368  1   43.22 ? 25  LEU   B C   1 
ATOM   3204 O  O   . LEU   B 1 40  ? 35.168  -1.579  -5.594  1   43.83 ? 25  LEU   B O   1 
ATOM   3205 C  CB  . LEU   B 1 40  ? 35.342  -3.739  -7.562  1   41.33 ? 25  LEU   B CB  1 
ATOM   3206 C  CG  . LEU   B 1 40  ? 36.581  -4.456  -7.11   1   42.95 ? 25  LEU   B CG  1 
ATOM   3207 C  CD1 . LEU   B 1 40  ? 36.268  -5.924  -6.775  1   42.87 ? 25  LEU   B CD1 1 
ATOM   3208 C  CD2 . LEU   B 1 40  ? 37.654  -4.356  -8.175  1   43.73 ? 25  LEU   B CD2 1 
ATOM   3209 N  N   . PRO   B 1 41  ? 34.782  -3.246  -4.127  1   43.97 ? 26  PRO   B N   1 
ATOM   3210 C  CA  . PRO   B 1 41  ? 35.272  -2.423  -3.006  1   44.24 ? 26  PRO   B CA  1 
ATOM   3211 C  C   . PRO   B 1 41  ? 36.772  -2.159  -3.109  1   44.63 ? 26  PRO   B C   1 
ATOM   3212 O  O   . PRO   B 1 41  ? 37.498  -3.036  -3.553  1   44.45 ? 26  PRO   B O   1 
ATOM   3213 C  CB  . PRO   B 1 41  ? 34.904  -3.235  -1.76   1   45    ? 26  PRO   B CB  1 
ATOM   3214 C  CG  . PRO   B 1 41  ? 34.671  -4.645  -2.24   1   45.1  ? 26  PRO   B CG  1 
ATOM   3215 C  CD  . PRO   B 1 41  ? 34.334  -4.593  -3.701  1   43.39 ? 26  PRO   B CD  1 
ATOM   3216 N  N   . ASN   B 1 42  ? 37.23   -0.922  -2.774  1   45.1  ? 27  ASN   B N   1 
ATOM   3217 C  CA  . ASN   B 1 42  ? 38.648  -0.497  -2.833  1   46.49 ? 27  ASN   B CA  1 
ATOM   3218 C  C   . ASN   B 1 42  ? 39.45   -1.128  -3.976  1   45.63 ? 27  ASN   B C   1 
ATOM   3219 O  O   . ASN   B 1 42  ? 40.264  -2.029  -3.739  1   45.63 ? 27  ASN   B O   1 
ATOM   3220 C  CB  . ASN   B 1 42  ? 39.333  -0.771  -1.491  1   49.83 ? 27  ASN   B CB  1 
ATOM   3221 C  CG  . ASN   B 1 42  ? 38.64   -0.069  -0.364  1   56.87 ? 27  ASN   B CG  1 
ATOM   3222 O  OD1 . ASN   B 1 42  ? 38.502  1.169   -0.355  1   59.44 ? 27  ASN   B OD1 1 
ATOM   3223 N  ND2 . ASN   B 1 42  ? 38.153  -0.851  0.593   1   58.6  ? 27  ASN   B ND2 1 
ATOM   3224 N  N   . PRO   B 1 43  ? 39.118  -0.791  -5.236  1   44.84 ? 28  PRO   B N   1 
ATOM   3225 C  CA  . PRO   B 1 43  ? 39.782  -1.454  -6.364  1   44.9  ? 28  PRO   B CA  1 
ATOM   3226 C  C   . PRO   B 1 43  ? 41.304  -1.324  -6.335  1   46.18 ? 28  PRO   B C   1 
ATOM   3227 O  O   . PRO   B 1 43  ? 41.811  -0.304  -5.853  1   45.86 ? 28  PRO   B O   1 
ATOM   3228 C  CB  . PRO   B 1 43  ? 39.189  -0.748  -7.586  1   45.2  ? 28  PRO   B CB  1 
ATOM   3229 C  CG  . PRO   B 1 43  ? 37.899  -0.177  -7.121  1   45.61 ? 28  PRO   B CG  1 
ATOM   3230 C  CD  . PRO   B 1 43  ? 38.148  0.216   -5.699  1   44.01 ? 28  PRO   B CD  1 
ATOM   3231 N  N   . GLN   B 1 44  ? 42.023  -2.364  -6.819  1   47.34 ? 29  GLN   B N   1 
ATOM   3232 C  CA  . GLN   B 1 44  ? 43.487  -2.332  -6.901  1   49.03 ? 29  GLN   B CA  1 
ATOM   3233 C  C   . GLN   B 1 44  ? 43.901  -1.25   -7.918  1   50.83 ? 29  GLN   B C   1 
ATOM   3234 O  O   . GLN   B 1 44  ? 43.275  -1.137  -8.977  1   51    ? 29  GLN   B O   1 
ATOM   3235 C  CB  . GLN   B 1 44  ? 44.031  -3.697  -7.343  1   50.41 ? 29  GLN   B CB  1 
ATOM   3236 C  CG  . GLN   B 1 44  ? 45.52   -3.886  -7.028  1   53.87 ? 29  GLN   B CG  1 
ATOM   3237 C  CD  . GLN   B 1 44  ? 45.904  -5.341  -7.132  1   57.18 ? 29  GLN   B CD  1 
ATOM   3238 O  OE1 . GLN   B 1 44  ? 45.244  -6.215  -6.564  1   58.5  ? 29  GLN   B OE1 1 
ATOM   3239 N  NE2 . GLN   B 1 44  ? 46.976  -5.64   -7.858  1   56.73 ? 29  GLN   B NE2 1 
ATOM   3240 N  N   A GLU   B 1 45  ? 44.938  -0.463  -7.592  0.5 51.36 ? 30  GLU   B N   1 
ATOM   3241 N  N   B GLU   B 1 45  ? 44.936  -0.46   -7.607  0.5 51.45 ? 30  GLU   B N   1 
ATOM   3242 C  CA  A GLU   B 1 45  ? 45.413  0.63    -8.44   0.5 52.43 ? 30  GLU   B CA  1 
ATOM   3243 C  CA  B GLU   B 1 45  ? 45.383  0.587   -8.523  0.5 52.61 ? 30  GLU   B CA  1 
ATOM   3244 C  C   A GLU   B 1 45  ? 46.675  0.277   -9.235  0.5 53.57 ? 30  GLU   B C   1 
ATOM   3245 C  C   B GLU   B 1 45  ? 46.622  0.177   -9.318  0.5 53.68 ? 30  GLU   B C   1 
ATOM   3246 O  O   A GLU   B 1 45  ? 46.894  0.824   -10.317 0.5 54    ? 30  GLU   B O   1 
ATOM   3247 O  O   B GLU   B 1 45  ? 46.761  0.56    -10.484 0.5 54.1  ? 30  GLU   B O   1 
ATOM   3248 C  CB  A GLU   B 1 45  ? 45.627  1.901   -7.598  0.5 54.18 ? 30  GLU   B CB  1 
ATOM   3249 C  CB  B GLU   B 1 45  ? 45.619  1.911   -7.781  0.5 54.66 ? 30  GLU   B CB  1 
ATOM   3250 C  CG  A GLU   B 1 45  ? 44.392  2.292   -6.807  0.5 57.77 ? 30  GLU   B CG  1 
ATOM   3251 C  CG  B GLU   B 1 45  ? 45.841  3.074   -8.727  0.5 58.74 ? 30  GLU   B CG  1 
ATOM   3252 C  CD  A GLU   B 1 45  ? 44.606  3.368   -5.763  0.5 63.25 ? 30  GLU   B CD  1 
ATOM   3253 C  CD  B GLU   B 1 45  ? 46.232  4.382   -8.077  0.5 63.28 ? 30  GLU   B CD  1 
ATOM   3254 O  OE1 A GLU   B 1 45  ? 45.472  4.245   -5.983  0.5 64.08 ? 30  GLU   B OE1 1 
ATOM   3255 O  OE1 B GLU   B 1 45  ? 46.249  4.449   -6.827  0.5 64.73 ? 30  GLU   B OE1 1 
ATOM   3256 O  OE2 A GLU   B 1 45  ? 43.9    3.342   -4.729  0.5 65.07 ? 30  GLU   B OE2 1 
ATOM   3257 O  OE2 B GLU   B 1 45  ? 46.511  5.348   -8.822  0.5 64.43 ? 30  GLU   B OE2 1 
ATOM   3258 N  N   . ASN   B 1 46  ? 47.496  -0.643  -8.718  1   53.93 ? 31  ASN   B N   1 
ATOM   3259 C  CA  . ASN   B 1 46  ? 48.721  -1.06   -9.403  1   54.95 ? 31  ASN   B CA  1 
ATOM   3260 C  C   . ASN   B 1 46  ? 48.799  -2.551  -9.634  1   55.46 ? 31  ASN   B C   1 
ATOM   3261 O  O   . ASN   B 1 46  ? 48.333  -3.332  -8.811  1   55.48 ? 31  ASN   B O   1 
ATOM   3262 C  CB  . ASN   B 1 46  ? 49.947  -0.593  -8.613  1   56.84 ? 31  ASN   B CB  1 
ATOM   3263 C  CG  . ASN   B 1 46  ? 49.92   0.881   -8.32   1   61.36 ? 31  ASN   B CG  1 
ATOM   3264 O  OD1 . ASN   B 1 46  ? 50.052  1.719   -9.216  1   63.33 ? 31  ASN   B OD1 1 
ATOM   3265 N  ND2 . ASN   B 1 46  ? 49.704  1.237   -7.062  1   62.78 ? 31  ASN   B ND2 1 
ATOM   3266 N  N   . LEU   B 1 47  ? 49.368  -2.951  -10.762 1   55.89 ? 32  LEU   B N   1 
ATOM   3267 C  CA  . LEU   B 1 47  ? 49.561  -4.369  -11.076 1   57.27 ? 32  LEU   B CA  1 
ATOM   3268 C  C   . LEU   B 1 47  ? 50.984  -4.781  -10.623 1   59.24 ? 32  LEU   B C   1 
ATOM   3269 O  O   . LEU   B 1 47  ? 51.832  -3.903  -10.429 1   59.63 ? 32  LEU   B O   1 
ATOM   3270 C  CB  . LEU   B 1 47  ? 49.435  -4.594  -12.607 1   57.29 ? 32  LEU   B CB  1 
ATOM   3271 C  CG  . LEU   B 1 47  ? 48.035  -4.672  -13.217 1   58.65 ? 32  LEU   B CG  1 
ATOM   3272 C  CD1 . LEU   B 1 47  ? 48.11   -4.933  -14.72  1   59.14 ? 32  LEU   B CD1 1 
ATOM   3273 C  CD2 . LEU   B 1 47  ? 47.201  -5.742  -12.556 1   59.42 ? 32  LEU   B CD2 1 
ATOM   3274 N  N   . PRO   B 1 48  ? 51.313  -6.092  -10.511 1   60.21 ? 33  PRO   B N   1 
ATOM   3275 C  CA  . PRO   B 1 48  ? 52.707  -6.468  -10.206 1   61.19 ? 33  PRO   B CA  1 
ATOM   3276 C  C   . PRO   B 1 48  ? 53.669  -5.924  -11.274 1   62.22 ? 33  PRO   B C   1 
ATOM   3277 O  O   . PRO   B 1 48  ? 53.259  -5.723  -12.424 1   62.47 ? 33  PRO   B O   1 
ATOM   3278 C  CB  . PRO   B 1 48  ? 52.671  -8.005  -10.223 1   61.82 ? 33  PRO   B CB  1 
ATOM   3279 C  CG  . PRO   B 1 48  ? 51.236  -8.351  -9.964  1   62.01 ? 33  PRO   B CG  1 
ATOM   3280 C  CD  . PRO   B 1 48  ? 50.478  -7.291  -10.715 1   60.07 ? 33  PRO   B CD  1 
ATOM   3281 N  N   . ASP   B 1 49  ? 54.931  -5.651  -10.885 1   62.4  ? 34  ASP   B N   1 
ATOM   3282 C  CA  . ASP   B 1 49  ? 55.976  -5.091  -11.751 1   62.75 ? 34  ASP   B CA  1 
ATOM   3283 C  C   . ASP   B 1 49  ? 56.122  -5.791  -13.087 1   61.49 ? 34  ASP   B C   1 
ATOM   3284 O  O   . ASP   B 1 49  ? 56.476  -5.16   -14.077 1   61.68 ? 34  ASP   B O   1 
ATOM   3285 C  CB  . ASP   B 1 49  ? 57.328  -5.046  -11.02  1   65.96 ? 34  ASP   B CB  1 
ATOM   3286 C  CG  . ASP   B 1 49  ? 57.427  -3.9    -10.038 1   72.94 ? 34  ASP   B CG  1 
ATOM   3287 O  OD1 . ASP   B 1 49  ? 56.772  -2.854  -10.276 1   74.05 ? 34  ASP   B OD1 1 
ATOM   3288 O  OD2 . ASP   B 1 49  ? 58.158  -4.044  -9.031  1   76.21 ? 34  ASP   B OD2 1 
ATOM   3289 N  N   . PHE   B 1 50  ? 55.807  -7.078  -13.13  1   60.42 ? 35  PHE   B N   1 
ATOM   3290 C  CA  . PHE   B 1 50  ? 55.852  -7.875  -14.348 1   60.23 ? 35  PHE   B CA  1 
ATOM   3291 C  C   . PHE   B 1 50  ? 55      -7.261  -15.475 1   59.97 ? 35  PHE   B C   1 
ATOM   3292 O  O   . PHE   B 1 50  ? 55.363  -7.338  -16.649 1   60.83 ? 35  PHE   B O   1 
ATOM   3293 C  CB  . PHE   B 1 50  ? 55.34   -9.278  -14.018 1   60.4  ? 35  PHE   B CB  1 
ATOM   3294 C  CG  . PHE   B 1 50  ? 55.363  -10.274 -15.147 1   61.66 ? 35  PHE   B CG  1 
ATOM   3295 C  CD1 . PHE   B 1 50  ? 56.514  -10.979 -15.446 1   62.75 ? 35  PHE   B CD1 1 
ATOM   3296 C  CD2 . PHE   B 1 50  ? 54.209  -10.581 -15.843 1   62.88 ? 35  PHE   B CD2 1 
ATOM   3297 C  CE1 . PHE   B 1 50  ? 56.525  -11.923 -16.467 1   63.69 ? 35  PHE   B CE1 1 
ATOM   3298 C  CE2 . PHE   B 1 50  ? 54.221  -11.527 -16.86  1   63.78 ? 35  PHE   B CE2 1 
ATOM   3299 C  CZ  . PHE   B 1 50  ? 55.38   -12.188 -17.17  1   63.65 ? 35  PHE   B CZ  1 
ATOM   3300 N  N   . TYR   B 1 51  ? 53.894  -6.61   -15.101 1   58.4  ? 36  TYR   B N   1 
ATOM   3301 C  CA  . TYR   B 1 51  ? 52.938  -6.019  -16.023 1   57.16 ? 36  TYR   B CA  1 
ATOM   3302 C  C   . TYR   B 1 51  ? 53.144  -4.532  -16.303 1   56.61 ? 36  TYR   B C   1 
ATOM   3303 O  O   . TYR   B 1 51  ? 52.234  -3.897  -16.839 1   56.49 ? 36  TYR   B O   1 
ATOM   3304 C  CB  . TYR   B 1 51  ? 51.518  -6.271  -15.495 1   56.09 ? 36  TYR   B CB  1 
ATOM   3305 C  CG  . TYR   B 1 51  ? 51.205  -7.746  -15.388 1   55.17 ? 36  TYR   B CG  1 
ATOM   3306 C  CD1 . TYR   B 1 51  ? 50.983  -8.512  -16.522 1   55.27 ? 36  TYR   B CD1 1 
ATOM   3307 C  CD2 . TYR   B 1 51  ? 51.197  -8.388  -14.158 1   55.38 ? 36  TYR   B CD2 1 
ATOM   3308 C  CE1 . TYR   B 1 51  ? 50.694  -9.867  -16.434 1   56.15 ? 36  TYR   B CE1 1 
ATOM   3309 C  CE2 . TYR   B 1 51  ? 50.951  -9.751  -14.059 1   55.94 ? 36  TYR   B CE2 1 
ATOM   3310 C  CZ  . TYR   B 1 51  ? 50.672  -10.484 -15.199 1   57.14 ? 36  TYR   B CZ  1 
ATOM   3311 O  OH  . TYR   B 1 51  ? 50.401  -11.835 -15.141 1   58.68 ? 36  TYR   B OH  1 
ATOM   3312 N  N   . ASN   B 1 52  ? 54.329  -3.983  -15.972 1   55.77 ? 37  ASN   B N   1 
ATOM   3313 C  CA  . ASN   B 1 52  ? 54.652  -2.568  -16.197 1   55.38 ? 37  ASN   B CA  1 
ATOM   3314 C  C   . ASN   B 1 52  ? 54.407  -2.09   -17.636 1   53.46 ? 37  ASN   B C   1 
ATOM   3315 O  O   . ASN   B 1 52  ? 54.023  -0.94   -17.814 1   53.41 ? 37  ASN   B O   1 
ATOM   3316 C  CB  . ASN   B 1 52  ? 56.102  -2.253  -15.781 1   57.7  ? 37  ASN   B CB  1 
ATOM   3317 C  CG  . ASN   B 1 52  ? 56.275  -1.914  -14.316 1   63.05 ? 37  ASN   B CG  1 
ATOM   3318 O  OD1 . ASN   B 1 52  ? 55.309  -1.671  -13.573 1   64.72 ? 37  ASN   B OD1 1 
ATOM   3319 N  ND2 . ASN   B 1 52  ? 57.522  -1.886  -13.864 1   64.42 ? 37  ASN   B ND2 1 
ATOM   3320 N  N   . ASP   B 1 53  ? 54.625  -2.957  -18.651 1   51.6  ? 38  ASP   B N   1 
ATOM   3321 C  CA  . ASP   B 1 53  ? 54.431  -2.595  -20.056 1   50.79 ? 38  ASP   B CA  1 
ATOM   3322 C  C   . ASP   B 1 53  ? 52.947  -2.365  -20.383 1   50.31 ? 38  ASP   B C   1 
ATOM   3323 O  O   . ASP   B 1 53  ? 52.632  -1.532  -21.226 1   49.92 ? 38  ASP   B O   1 
ATOM   3324 C  CB  . ASP   B 1 53  ? 55.018  -3.659  -20.999 1   51.21 ? 38  ASP   B CB  1 
ATOM   3325 C  CG  . ASP   B 1 53  ? 56.533  -3.806  -20.939 1   53.63 ? 38  ASP   B CG  1 
ATOM   3326 O  OD1 . ASP   B 1 53  ? 57.196  -2.918  -20.337 1   53.27 ? 38  ASP   B OD1 1 
ATOM   3327 O  OD2 . ASP   B 1 53  ? 57.051  -4.811  -21.485 1   53.61 ? 38  ASP   B OD2 1 
ATOM   3328 N  N   . TRP   B 1 54  ? 52.046  -3.107  -19.721 1   50.16 ? 39  TRP   B N   1 
ATOM   3329 C  CA  . TRP   B 1 54  ? 50.609  -2.912  -19.891 1   49.92 ? 39  TRP   B CA  1 
ATOM   3330 C  C   . TRP   B 1 54  ? 50.232  -1.619  -19.198 1   50.76 ? 39  TRP   B C   1 
ATOM   3331 O  O   . TRP   B 1 54  ? 49.563  -0.775  -19.793 1   51.77 ? 39  TRP   B O   1 
ATOM   3332 C  CB  . TRP   B 1 54  ? 49.813  -4.056  -19.233 1   49.18 ? 39  TRP   B CB  1 
ATOM   3333 C  CG  . TRP   B 1 54  ? 49.867  -5.388  -19.911 1   48.88 ? 39  TRP   B CG  1 
ATOM   3334 C  CD1 . TRP   B 1 54  ? 50.489  -5.707  -21.087 1   49.52 ? 39  TRP   B CD1 1 
ATOM   3335 C  CD2 . TRP   B 1 54  ? 49.242  -6.585  -19.449 1   48.84 ? 39  TRP   B CD2 1 
ATOM   3336 N  NE1 . TRP   B 1 54  ? 50.289  -7.035  -21.379 1   49.78 ? 39  TRP   B NE1 1 
ATOM   3337 C  CE2 . TRP   B 1 54  ? 49.527  -7.598  -20.385 1   49.51 ? 39  TRP   B CE2 1 
ATOM   3338 C  CE3 . TRP   B 1 54  ? 48.436  -6.893  -18.341 1   49.29 ? 39  TRP   B CE3 1 
ATOM   3339 C  CZ2 . TRP   B 1 54  ? 49.041  -8.895  -20.245 1   50.26 ? 39  TRP   B CZ2 1 
ATOM   3340 C  CZ3 . TRP   B 1 54  ? 47.972  -8.183  -18.2   1   49.94 ? 39  TRP   B CZ3 1 
ATOM   3341 C  CH2 . TRP   B 1 54  ? 48.275  -9.166  -19.142 1   50.35 ? 39  TRP   B CH2 1 
ATOM   3342 N  N   . MET   B 1 55  ? 50.67   -1.453  -17.936 1   50.56 ? 40  MET   B N   1 
ATOM   3343 C  CA  . MET   B 1 55  ? 50.332  -0.285  -17.137 1   50.91 ? 40  MET   B CA  1 
ATOM   3344 C  C   . MET   B 1 55  ? 50.791  1.008   -17.738 1   51.14 ? 40  MET   B C   1 
ATOM   3345 O  O   . MET   B 1 55  ? 50.063  2.003   -17.661 1   51.13 ? 40  MET   B O   1 
ATOM   3346 C  CB  . MET   B 1 55  ? 50.829  -0.416  -15.689 1   51.47 ? 40  MET   B CB  1 
ATOM   3347 C  CG  . MET   B 1 55  ? 50.211  0.599   -14.745 1   53.34 ? 40  MET   B CG  1 
ATOM   3348 S  SD  . MET   B 1 55  ? 48.415  0.366   -14.424 1   61.52 ? 40  MET   B SD  1 
ATOM   3349 C  CE  . MET   B 1 55  ? 48.37   -1.317  -14.039 1   58.72 ? 40  MET   B CE  1 
ATOM   3350 N  N   . PHE   B 1 56  ? 51.998  1.028   -18.347 1   51.2  ? 41  PHE   B N   1 
ATOM   3351 C  CA  . PHE   B 1 56  ? 52.49   2.267   -18.959 1   51.23 ? 41  PHE   B CA  1 
ATOM   3352 C  C   . PHE   B 1 56  ? 51.544  2.728   -20.071 1   49.27 ? 41  PHE   B C   1 
ATOM   3353 O  O   . PHE   B 1 56  ? 51.152  3.893   -20.097 1   49.78 ? 41  PHE   B O   1 
ATOM   3354 C  CB  . PHE   B 1 56  ? 53.946  2.135   -19.473 1   52.32 ? 41  PHE   B CB  1 
ATOM   3355 C  CG  . PHE   B 1 56  ? 54.366  3.359   -20.251 1   54.31 ? 41  PHE   B CG  1 
ATOM   3356 C  CD1 . PHE   B 1 56  ? 54.373  3.349   -21.638 1   55.8  ? 41  PHE   B CD1 1 
ATOM   3357 C  CD2 . PHE   B 1 56  ? 54.588  4.564   -19.607 1   55.65 ? 41  PHE   B CD2 1 
ATOM   3358 C  CE1 . PHE   B 1 56  ? 54.661  4.506   -22.362 1   56.82 ? 41  PHE   B CE1 1 
ATOM   3359 C  CE2 . PHE   B 1 56  ? 54.898  5.714   -20.332 1   56.67 ? 41  PHE   B CE2 1 
ATOM   3360 C  CZ  . PHE   B 1 56  ? 54.933  5.677   -21.706 1   56.55 ? 41  PHE   B CZ  1 
ATOM   3361 N  N   . ILE   B 1 57  ? 51.163  1.809   -20.961 1   47.63 ? 42  ILE   B N   1 
ATOM   3362 C  CA  . ILE   B 1 57  ? 50.247  2.136   -22.054 1   46.51 ? 42  ILE   B CA  1 
ATOM   3363 C  C   . ILE   B 1 57  ? 48.885  2.63    -21.528 1   45.82 ? 42  ILE   B C   1 
ATOM   3364 O  O   . ILE   B 1 57  ? 48.459  3.717   -21.899 1   45.83 ? 42  ILE   B O   1 
ATOM   3365 C  CB  . ILE   B 1 57  ? 50.095  0.934   -23.001 1   46.38 ? 42  ILE   B CB  1 
ATOM   3366 C  CG1 . ILE   B 1 57  ? 51.462  0.537   -23.612 1   46.54 ? 42  ILE   B CG1 1 
ATOM   3367 C  CG2 . ILE   B 1 57  ? 49.059  1.251   -24.086 1   46.58 ? 42  ILE   B CG2 1 
ATOM   3368 C  CD1 . ILE   B 1 57  ? 51.406  -0.729  -24.49  1   47.25 ? 42  ILE   B CD1 1 
ATOM   3369 N  N   . ALA   B 1 58  ? 48.254  1.874   -20.599 1   45.15 ? 43  ALA   B N   1 
ATOM   3370 C  CA  . ALA   B 1 58  ? 46.949  2.223   -20.013 1   44.43 ? 43  ALA   B CA  1 
ATOM   3371 C  C   . ALA   B 1 58  ? 46.956  3.568   -19.3   1   44.1  ? 43  ALA   B C   1 
ATOM   3372 O  O   . ALA   B 1 58  ? 46.044  4.37    -19.487 1   43.86 ? 43  ALA   B O   1 
ATOM   3373 C  CB  . ALA   B 1 58  ? 46.489  1.125   -19.069 1   44.2  ? 43  ALA   B CB  1 
ATOM   3374 N  N   . LYS   B 1 59  ? 48.014  3.852   -18.542 1   44.71 ? 44  LYS   B N   1 
ATOM   3375 C  CA  . LYS   B 1 59  ? 48.126  5.128   -17.833 1   45.66 ? 44  LYS   B CA  1 
ATOM   3376 C  C   . LYS   B 1 59  ? 48.443  6.312   -18.752 1   46.2  ? 44  LYS   B C   1 
ATOM   3377 O  O   . LYS   B 1 59  ? 48.218  7.449   -18.352 1   46.58 ? 44  LYS   B O   1 
ATOM   3378 C  CB  . LYS   B 1 59  ? 49.144  5.032   -16.689 1   48.45 ? 44  LYS   B CB  1 
ATOM   3379 N  N   . HIS   B 1 60  ? 48.904  6.068   -19.99  1   46.65 ? 45  HIS   B N   1 
ATOM   3380 C  CA  . HIS   B 1 60  ? 49.222  7.173   -20.9   1   47.56 ? 45  HIS   B CA  1 
ATOM   3381 C  C   . HIS   B 1 60  ? 48.386  7.167   -22.181 1   47.58 ? 45  HIS   B C   1 
ATOM   3382 O  O   . HIS   B 1 60  ? 48.837  7.69    -23.201 1   47.08 ? 45  HIS   B O   1 
ATOM   3383 C  CB  . HIS   B 1 60  ? 50.734  7.205   -21.197 1   49.16 ? 45  HIS   B CB  1 
ATOM   3384 C  CG  . HIS   B 1 60  ? 51.536  7.503   -19.971 1   53.31 ? 45  HIS   B CG  1 
ATOM   3385 N  ND1 . HIS   B 1 60  ? 52.039  6.489   -19.17  1   55.62 ? 45  HIS   B ND1 1 
ATOM   3386 C  CD2 . HIS   B 1 60  ? 51.809  8.696   -19.39  1   55.05 ? 45  HIS   B CD2 1 
ATOM   3387 C  CE1 . HIS   B 1 60  ? 52.614  7.098   -18.145 1   56.58 ? 45  HIS   B CE1 1 
ATOM   3388 N  NE2 . HIS   B 1 60  ? 52.511  8.425   -18.238 1   56.61 ? 45  HIS   B NE2 1 
ATOM   3389 N  N   . LEU   B 1 61  ? 47.143  6.618   -22.127 1   47.04 ? 46  LEU   B N   1 
ATOM   3390 C  CA  . LEU   B 1 61  ? 46.273  6.614   -23.302 1   46.48 ? 46  LEU   B CA  1 
ATOM   3391 C  C   . LEU   B 1 61  ? 46.055  7.998   -23.905 1   46.54 ? 46  LEU   B C   1 
ATOM   3392 O  O   . LEU   B 1 61  ? 46.201  8.116   -25.114 1   46.23 ? 46  LEU   B O   1 
ATOM   3393 C  CB  . LEU   B 1 61  ? 44.913  5.935   -23.061 1   46.02 ? 46  LEU   B CB  1 
ATOM   3394 C  CG  . LEU   B 1 61  ? 44.914  4.428   -22.796 1   46.23 ? 46  LEU   B CG  1 
ATOM   3395 C  CD1 . LEU   B 1 61  ? 43.481  3.915   -22.66  1   45.46 ? 46  LEU   B CD1 1 
ATOM   3396 C  CD2 . LEU   B 1 61  ? 45.585  3.665   -23.918 1   46.42 ? 46  LEU   B CD2 1 
ATOM   3397 N  N   . PRO   B 1 62  ? 45.731  9.064   -23.136 1   46.78 ? 47  PRO   B N   1 
ATOM   3398 C  CA  . PRO   B 1 62  ? 45.505  10.364  -23.776 1   47.16 ? 47  PRO   B CA  1 
ATOM   3399 C  C   . PRO   B 1 62  ? 46.703  10.848  -24.614 1   48.56 ? 47  PRO   B C   1 
ATOM   3400 O  O   . PRO   B 1 62  ? 46.508  11.316  -25.735 1   48.56 ? 47  PRO   B O   1 
ATOM   3401 C  CB  . PRO   B 1 62  ? 45.172  11.282  -22.6   1   47.68 ? 47  PRO   B CB  1 
ATOM   3402 C  CG  . PRO   B 1 62  ? 44.618  10.354  -21.548 1   48.07 ? 47  PRO   B CG  1 
ATOM   3403 C  CD  . PRO   B 1 62  ? 45.477  9.136   -21.684 1   46.6  ? 47  PRO   B CD  1 
ATOM   3404 N  N   . ASP   B 1 63  ? 47.931  10.684  -24.104 1   49.14 ? 48  ASP   B N   1 
ATOM   3405 C  CA  . ASP   B 1 63  ? 49.127  11.135  -24.822 1   50.41 ? 48  ASP   B CA  1 
ATOM   3406 C  C   . ASP   B 1 63  ? 49.496  10.231  -25.964 1   49.69 ? 48  ASP   B C   1 
ATOM   3407 O  O   . ASP   B 1 63  ? 49.806  10.733  -27.039 1   50.75 ? 48  ASP   B O   1 
ATOM   3408 C  CB  . ASP   B 1 63  ? 50.33   11.302  -23.87  1   54.5  ? 48  ASP   B CB  1 
ATOM   3409 C  CG  . ASP   B 1 63  ? 50.013  12.176  -22.669 1   64.18 ? 48  ASP   B CG  1 
ATOM   3410 O  OD1 . ASP   B 1 63  ? 49.316  11.687  -21.735 1   66.89 ? 48  ASP   B OD1 1 
ATOM   3411 O  OD2 . ASP   B 1 63  ? 50.439  13.354  -22.662 1   67.32 ? 48  ASP   B OD2 1 
ATOM   3412 N  N   . LEU   B 1 64  ? 49.477  8.903   -25.748 1   47.89 ? 49  LEU   B N   1 
ATOM   3413 C  CA  . LEU   B 1 64  ? 49.833  7.951   -26.787 1   47.2  ? 49  LEU   B CA  1 
ATOM   3414 C  C   . LEU   B 1 64  ? 48.839  7.977   -27.938 1   46.86 ? 49  LEU   B C   1 
ATOM   3415 O  O   . LEU   B 1 64  ? 49.238  7.804   -29.095 1   47    ? 49  LEU   B O   1 
ATOM   3416 C  CB  . LEU   B 1 64  ? 49.944  6.525   -26.231 1   47.3  ? 49  LEU   B CB  1 
ATOM   3417 C  CG  . LEU   B 1 64  ? 51.038  6.291   -25.186 1   49.02 ? 49  LEU   B CG  1 
ATOM   3418 C  CD1 . LEU   B 1 64  ? 50.939  4.888   -24.609 1   49.03 ? 49  LEU   B CD1 1 
ATOM   3419 C  CD2 . LEU   B 1 64  ? 52.443  6.497   -25.788 1   50.11 ? 49  LEU   B CD2 1 
ATOM   3420 N  N   . ILE   B 1 65  ? 47.541  8.18    -27.638 1   45.42 ? 50  ILE   B N   1 
ATOM   3421 C  CA  . ILE   B 1 65  ? 46.538  8.249   -28.681 1   44.7  ? 50  ILE   B CA  1 
ATOM   3422 C  C   . ILE   B 1 65  ? 46.765  9.483   -29.537 1   44.98 ? 50  ILE   B C   1 
ATOM   3423 O  O   . ILE   B 1 65  ? 46.841  9.347   -30.76  1   45.79 ? 50  ILE   B O   1 
ATOM   3424 C  CB  . ILE   B 1 65  ? 45.074  8.204   -28.14  1   44.14 ? 50  ILE   B CB  1 
ATOM   3425 C  CG1 . ILE   B 1 65  ? 44.734  6.842   -27.523 1   44.16 ? 50  ILE   B CG1 1 
ATOM   3426 C  CG2 . ILE   B 1 65  ? 44.085  8.55    -29.25  1   44.12 ? 50  ILE   B CG2 1 
ATOM   3427 C  CD1 . ILE   B 1 65  ? 43.372  6.853   -26.757 1   44.78 ? 50  ILE   B CD1 1 
ATOM   3428 N  N   . GLU   B 1 66  ? 46.84   10.672  -28.906 1   45.11 ? 51  GLU   B N   1 
ATOM   3429 C  CA  . GLU   B 1 66  ? 46.974  11.951  -29.608 1   46.38 ? 51  GLU   B CA  1 
ATOM   3430 C  C   . GLU   B 1 66  ? 48.205  11.992  -30.497 1   48.07 ? 51  GLU   B C   1 
ATOM   3431 O  O   . GLU   B 1 66  ? 48.137  12.492  -31.618 1   48.66 ? 51  GLU   B O   1 
ATOM   3432 C  CB  . GLU   B 1 66  ? 46.976  13.136  -28.628 1   47.78 ? 51  GLU   B CB  1 
ATOM   3433 C  CG  . GLU   B 1 66  ? 46.665  14.483  -29.277 1   52.71 ? 51  GLU   B CG  1 
ATOM   3434 C  CD  . GLU   B 1 66  ? 47.833  15.244  -29.901 1   60    ? 51  GLU   B CD  1 
ATOM   3435 O  OE1 . GLU   B 1 66  ? 48.977  14.736  -29.847 1   58.27 ? 51  GLU   B OE1 1 
ATOM   3436 O  OE2 . GLU   B 1 66  ? 47.601  16.348  -30.45  1   63.77 ? 51  GLU   B OE2 1 
ATOM   3437 N  N   . SER   B 1 67  ? 49.327  11.476  -29.994 1   48.65 ? 52  SER   B N   1 
ATOM   3438 C  CA  . SER   B 1 67  ? 50.6    11.458  -30.709 1   49.3  ? 52  SER   B CA  1 
ATOM   3439 C  C   . SER   B 1 67  ? 50.701  10.384  -31.797 1   50.24 ? 52  SER   B C   1 
ATOM   3440 O  O   . SER   B 1 67  ? 51.703  10.35   -32.497 1   51.19 ? 52  SER   B O   1 
ATOM   3441 C  CB  . SER   B 1 67  ? 51.752  11.29   -29.723 1   50.26 ? 52  SER   B CB  1 
ATOM   3442 O  OG  . SER   B 1 67  ? 51.777  9.967   -29.207 1   52.99 ? 52  SER   B OG  1 
ATOM   3443 N  N   . GLY   B 1 68  ? 49.713  9.506   -31.917 1   49.77 ? 53  GLY   B N   1 
ATOM   3444 C  CA  . GLY   B 1 68  ? 49.755  8.432   -32.898 1   50.2  ? 53  GLY   B CA  1 
ATOM   3445 C  C   . GLY   B 1 68  ? 50.737  7.324   -32.559 1   50.73 ? 53  GLY   B C   1 
ATOM   3446 O  O   . GLY   B 1 68  ? 51.079  6.502   -33.421 1   50.48 ? 53  GLY   B O   1 
ATOM   3447 N  N   . GLN   B 1 69  ? 51.153  7.245   -31.281 1   50.9  ? 54  GLN   B N   1 
ATOM   3448 C  CA  . GLN   B 1 69  ? 52.113  6.242   -30.816 1   51.56 ? 54  GLN   B CA  1 
ATOM   3449 C  C   . GLN   B 1 69  ? 51.494  5.043   -30.135 1   51.69 ? 54  GLN   B C   1 
ATOM   3450 O  O   . GLN   B 1 69  ? 52.217  4.097   -29.833 1   52.25 ? 54  GLN   B O   1 
ATOM   3451 C  CB  . GLN   B 1 69  ? 53.078  6.883   -29.828 1   53.76 ? 54  GLN   B CB  1 
ATOM   3452 C  CG  . GLN   B 1 69  ? 54.05   7.819   -30.477 1   58.86 ? 54  GLN   B CG  1 
ATOM   3453 C  CD  . GLN   B 1 69  ? 55.132  8.176   -29.514 1   66.71 ? 54  GLN   B CD  1 
ATOM   3454 O  OE1 . GLN   B 1 69  ? 56.307  7.779   -29.667 1   69.63 ? 54  GLN   B OE1 1 
ATOM   3455 N  NE2 . GLN   B 1 69  ? 54.757  8.944   -28.497 1   68.27 ? 54  GLN   B NE2 1 
ATOM   3456 N  N   . LEU   B 1 70  ? 50.182  5.078   -29.84  1   50.8  ? 55  LEU   B N   1 
ATOM   3457 C  CA  . LEU   B 1 70  ? 49.534  3.987   -29.133 1   50.02 ? 55  LEU   B CA  1 
ATOM   3458 C  C   . LEU   B 1 70  ? 49.582  2.644   -29.861 1   49.79 ? 55  LEU   B C   1 
ATOM   3459 O  O   . LEU   B 1 70  ? 49.885  1.63    -29.221 1   49.54 ? 55  LEU   B O   1 
ATOM   3460 C  CB  . LEU   B 1 70  ? 48.082  4.35    -28.761 1   49.86 ? 55  LEU   B CB  1 
ATOM   3461 C  CG  . LEU   B 1 70  ? 47.334  3.178   -28.152 1   50.66 ? 55  LEU   B CG  1 
ATOM   3462 C  CD1 . LEU   B 1 70  ? 47.433  3.12    -26.679 1   51.21 ? 55  LEU   B CD1 1 
ATOM   3463 C  CD2 . LEU   B 1 70  ? 46.128  2.847   -28.866 1   50.79 ? 55  LEU   B CD2 1 
ATOM   3464 N  N   . ARG   B 1 71  ? 49.173  2.604   -31.134 1   49.6  ? 56  ARG   B N   1 
ATOM   3465 C  CA  . ARG   B 1 71  ? 49.132  1.343   -31.866 1   50.76 ? 56  ARG   B CA  1 
ATOM   3466 C  C   . ARG   B 1 71  ? 50.497  0.68    -31.974 1   52.67 ? 56  ARG   B C   1 
ATOM   3467 O  O   . ARG   B 1 71  ? 50.586  -0.542  -31.852 1   52.97 ? 56  ARG   B O   1 
ATOM   3468 C  CB  . ARG   B 1 71  ? 48.47   1.532   -33.225 1   51.22 ? 56  ARG   B CB  1 
ATOM   3469 C  CG  . ARG   B 1 71  ? 46.969  1.691   -33.07  1   52.34 ? 56  ARG   B CG  1 
ATOM   3470 C  CD  . ARG   B 1 71  ? 46.314  2.256   -34.304 1   53.04 ? 56  ARG   B CD  1 
ATOM   3471 N  NE  . ARG   B 1 71  ? 44.864  2.084   -34.262 1   53.08 ? 56  ARG   B NE  1 
ATOM   3472 C  CZ  . ARG   B 1 71  ? 44.007  2.714   -35.061 1   52.93 ? 56  ARG   B CZ  1 
ATOM   3473 N  NH1 . ARG   B 1 71  ? 44.445  3.574   -35.974 1   52.27 ? 56  ARG   B NH1 1 
ATOM   3474 N  NH2 . ARG   B 1 71  ? 42.707  2.487   -34.956 1   50.86 ? 56  ARG   B NH2 1 
ATOM   3475 N  N   . GLU   B 1 72  ? 51.556  1.49    -32.114 1   53.98 ? 57  GLU   B N   1 
ATOM   3476 C  CA  . GLU   B 1 72  ? 52.928  1.003   -32.176 1   56.03 ? 57  GLU   B CA  1 
ATOM   3477 C  C   . GLU   B 1 72  ? 53.342  0.422   -30.818 1   56.2  ? 57  GLU   B C   1 
ATOM   3478 O  O   . GLU   B 1 72  ? 53.9    -0.667  -30.784 1   56.05 ? 57  GLU   B O   1 
ATOM   3479 C  CB  . GLU   B 1 72  ? 53.887  2.124   -32.61  1   60.9  ? 57  GLU   B CB  1 
ATOM   3480 C  CG  . GLU   B 1 72  ? 55.278  1.607   -32.931 1   70.97 ? 57  GLU   B CG  1 
ATOM   3481 C  CD  . GLU   B 1 72  ? 56.294  2.681   -33.271 1   83.15 ? 57  GLU   B CD  1 
ATOM   3482 O  OE1 . GLU   B 1 72  ? 56.521  3.585   -32.43  1   85.63 ? 57  GLU   B OE1 1 
ATOM   3483 O  OE2 . GLU   B 1 72  ? 56.88   2.605   -34.378 1   86.45 ? 57  GLU   B OE2 1 
ATOM   3484 N  N   . ARG   B 1 73  ? 53.033  1.116   -29.702 1   56.23 ? 58  ARG   B N   1 
ATOM   3485 C  CA  . ARG   B 1 73  ? 53.35   0.612   -28.361 1   57.18 ? 58  ARG   B CA  1 
ATOM   3486 C  C   . ARG   B 1 73  ? 52.642  -0.722  -28.094 1   57.27 ? 58  ARG   B C   1 
ATOM   3487 O  O   . ARG   B 1 73  ? 53.222  -1.613  -27.473 1   57.26 ? 58  ARG   B O   1 
ATOM   3488 C  CB  . ARG   B 1 73  ? 52.959  1.631   -27.284 1   59.67 ? 58  ARG   B CB  1 
ATOM   3489 C  CG  . ARG   B 1 73  ? 53.878  2.857   -27.198 1   65.11 ? 58  ARG   B CG  1 
ATOM   3490 C  CD  . ARG   B 1 73  ? 55.292  2.535   -26.705 1   70.04 ? 58  ARG   B CD  1 
ATOM   3491 N  NE  . ARG   B 1 73  ? 55.297  1.708   -25.491 1   74    ? 58  ARG   B NE  1 
ATOM   3492 C  CZ  . ARG   B 1 73  ? 55.824  2.083   -24.331 1   78    ? 58  ARG   B CZ  1 
ATOM   3493 N  NH1 . ARG   B 1 73  ? 56.379  3.284   -24.201 1   78.47 ? 58  ARG   B NH1 1 
ATOM   3494 N  NH2 . ARG   B 1 73  ? 55.761  1.279   -23.276 1   78.7  ? 58  ARG   B NH2 1 
ATOM   3495 N  N   . VAL   B 1 74  ? 51.395  -0.868  -28.572 1   56.98 ? 59  VAL   B N   1 
ATOM   3496 C  CA  . VAL   B 1 74  ? 50.657  -2.115  -28.396 1   57.52 ? 59  VAL   B CA  1 
ATOM   3497 C  C   . VAL   B 1 74  ? 51.284  -3.219  -29.25  1   58.23 ? 59  VAL   B C   1 
ATOM   3498 O  O   . VAL   B 1 74  ? 51.467  -4.34   -28.772 1   58.56 ? 59  VAL   B O   1 
ATOM   3499 C  CB  . VAL   B 1 74  ? 49.147  -1.936  -28.694 1   57.63 ? 59  VAL   B CB  1 
ATOM   3500 C  CG1 . VAL   B 1 74  ? 48.43   -3.282  -28.748 1   58.21 ? 59  VAL   B CG1 1 
ATOM   3501 C  CG2 . VAL   B 1 74  ? 48.495  -1.02   -27.665 1   57.39 ? 59  VAL   B CG2 1 
ATOM   3502 N  N   . GLU   B 1 75  ? 51.63   -2.899  -30.504 1   58.61 ? 60  GLU   B N   1 
ATOM   3503 C  CA  . GLU   B 1 75  ? 52.268  -3.861  -31.408 1   59.41 ? 60  GLU   B CA  1 
ATOM   3504 C  C   . GLU   B 1 75  ? 53.674  -4.301  -30.93  1   60.33 ? 60  GLU   B C   1 
ATOM   3505 O  O   . GLU   B 1 75  ? 54.079  -5.433  -31.19  1   60.42 ? 60  GLU   B O   1 
ATOM   3506 C  CB  . GLU   B 1 75  ? 52.287  -3.33   -32.85  1   60.78 ? 60  GLU   B CB  1 
ATOM   3507 C  CG  . GLU   B 1 75  ? 50.915  -3.316  -33.503 1   63.86 ? 60  GLU   B CG  1 
ATOM   3508 C  CD  . GLU   B 1 75  ? 50.72   -2.268  -34.585 1   69.44 ? 60  GLU   B CD  1 
ATOM   3509 O  OE1 . GLU   B 1 75  ? 51.709  -1.592  -34.946 1   70.37 ? 60  GLU   B OE1 1 
ATOM   3510 O  OE2 . GLU   B 1 75  ? 49.573  -2.111  -35.065 1   71.04 ? 60  GLU   B OE2 1 
ATOM   3511 N  N   . LYS   B 1 76  ? 54.38   -3.432  -30.186 1   60.9  ? 61  LYS   B N   1 
ATOM   3512 C  CA  . LYS   B 1 76  ? 55.708  -3.714  -29.629 1   62.17 ? 61  LYS   B CA  1 
ATOM   3513 C  C   . LYS   B 1 76  ? 55.678  -4.558  -28.342 1   63.74 ? 61  LYS   B C   1 
ATOM   3514 O  O   . LYS   B 1 76  ? 56.739  -4.906  -27.829 1   64.05 ? 61  LYS   B O   1 
ATOM   3515 C  CB  . LYS   B 1 76  ? 56.453  -2.401  -29.331 1   63.6  ? 61  LYS   B CB  1 
ATOM   3516 N  N   . LEU   B 1 77  ? 54.49   -4.844  -27.786 1   64.26 ? 62  LEU   B N   1 
ATOM   3517 C  CA  . LEU   B 1 77  ? 54.39   -5.617  -26.549 1   64.71 ? 62  LEU   B CA  1 
ATOM   3518 C  C   . LEU   B 1 77  ? 54.793  -7.064  -26.721 1   65.37 ? 62  LEU   B C   1 
ATOM   3519 O  O   . LEU   B 1 77  ? 54.533  -7.667  -27.756 1   65.24 ? 62  LEU   B O   1 
ATOM   3520 C  CB  . LEU   B 1 77  ? 52.943  -5.613  -26.017 1   64.6  ? 62  LEU   B CB  1 
ATOM   3521 C  CG  . LEU   B 1 77  ? 52.437  -4.355  -25.353 1   65.9  ? 62  LEU   B CG  1 
ATOM   3522 C  CD1 . LEU   B 1 77  ? 50.953  -4.476  -25.042 1   66.84 ? 62  LEU   B CD1 1 
ATOM   3523 C  CD2 . LEU   B 1 77  ? 53.195  -4.072  -24.095 1   66.09 ? 62  LEU   B CD2 1 
ATOM   3524 N  N   . ASN   B 1 78  ? 55.36   -7.641  -25.663 1   66.02 ? 63  ASN   B N   1 
ATOM   3525 C  CA  . ASN   B 1 78  ? 55.633  -9.073  -25.588 1   67.08 ? 63  ASN   B CA  1 
ATOM   3526 C  C   . ASN   B 1 78  ? 54.378  -9.718  -24.972 1   67.34 ? 63  ASN   B C   1 
ATOM   3527 O  O   . ASN   B 1 78  ? 53.677  -9.061  -24.192 1   67.18 ? 63  ASN   B O   1 
ATOM   3528 C  CB  . ASN   B 1 78  ? 56.836  -9.348  -24.683 1   68.67 ? 63  ASN   B CB  1 
ATOM   3529 C  CG  . ASN   B 1 78  ? 58.125  -8.83   -25.249 1   71.99 ? 63  ASN   B CG  1 
ATOM   3530 O  OD1 . ASN   B 1 78  ? 58.392  -8.952  -26.453 1   73.13 ? 63  ASN   B OD1 1 
ATOM   3531 N  ND2 . ASN   B 1 78  ? 58.942  -8.23   -24.392 1   72.4  ? 63  ASN   B ND2 1 
ATOM   3532 N  N   . MET   B 1 79  ? 54.087  -10.99  -25.311 1   67.53 ? 64  MET   B N   1 
ATOM   3533 C  CA  . MET   B 1 79  ? 52.912  -11.651 -24.75  1   68.05 ? 64  MET   B CA  1 
ATOM   3534 C  C   . MET   B 1 79  ? 53.163  -11.997 -23.3   1   68.31 ? 64  MET   B C   1 
ATOM   3535 O  O   . MET   B 1 79  ? 53.943  -12.902 -23.026 1   68.67 ? 64  MET   B O   1 
ATOM   3536 C  CB  . MET   B 1 79  ? 52.535  -12.909 -25.529 1   68.6  ? 64  MET   B CB  1 
ATOM   3537 C  CG  . MET   B 1 79  ? 51.157  -13.41  -25.184 1   70.66 ? 64  MET   B CG  1 
ATOM   3538 S  SD  . MET   B 1 79  ? 50.684  -14.858 -26.162 1   76.49 ? 64  MET   B SD  1 
ATOM   3539 C  CE  . MET   B 1 79  ? 51.686  -16.096 -25.37  1   77.28 ? 64  MET   B CE  1 
ATOM   3540 N  N   . LEU   B 1 80  ? 52.536  -11.267 -22.368 1   67.85 ? 65  LEU   B N   1 
ATOM   3541 C  CA  . LEU   B 1 80  ? 52.722  -11.543 -20.944 1   67.75 ? 65  LEU   B CA  1 
ATOM   3542 C  C   . LEU   B 1 80  ? 51.729  -12.59  -20.451 1   67.91 ? 65  LEU   B C   1 
ATOM   3543 O  O   . LEU   B 1 80  ? 50.564  -12.58  -20.85  1   68.31 ? 65  LEU   B O   1 
ATOM   3544 C  CB  . LEU   B 1 80  ? 52.627  -10.263 -20.108 1   67.61 ? 65  LEU   B CB  1 
ATOM   3545 C  CG  . LEU   B 1 80  ? 53.66   -9.192  -20.426 1   68.81 ? 65  LEU   B CG  1 
ATOM   3546 C  CD1 . LEU   B 1 80  ? 53.427  -7.957  -19.576 1   69.28 ? 65  LEU   B CD1 1 
ATOM   3547 C  CD2 . LEU   B 1 80  ? 55.086  -9.715  -20.246 1   69.22 ? 65  LEU   B CD2 1 
ATOM   3548 N  N   . SER   B 1 81  ? 52.196  -13.514 -19.619 1   67.32 ? 66  SER   B N   1 
ATOM   3549 C  CA  . SER   B 1 81  ? 51.351  -14.571 -19.076 1   67.49 ? 66  SER   B CA  1 
ATOM   3550 C  C   . SER   B 1 81  ? 50.429  -14.012 -17.987 1   67.21 ? 66  SER   B C   1 
ATOM   3551 O  O   . SER   B 1 81  ? 50.849  -13.157 -17.212 1   67.17 ? 66  SER   B O   1 
ATOM   3552 C  CB  . SER   B 1 81  ? 52.221  -15.682 -18.494 1   68.72 ? 66  SER   B CB  1 
ATOM   3553 O  OG  . SER   B 1 81  ? 51.446  -16.689 -17.866 1   70.85 ? 66  SER   B OG  1 
ATOM   3554 N  N   . ILE   B 1 82  ? 49.19   -14.515 -17.901 1   66.96 ? 67  ILE   B N   1 
ATOM   3555 C  CA  . ILE   B 1 82  ? 48.246  -14.064 -16.867 1   66.98 ? 67  ILE   B CA  1 
ATOM   3556 C  C   . ILE   B 1 82  ? 48.41   -14.777 -15.507 1   66.67 ? 67  ILE   B C   1 
ATOM   3557 O  O   . ILE   B 1 82  ? 47.709  -14.429 -14.558 1   66.78 ? 67  ILE   B O   1 
ATOM   3558 C  CB  . ILE   B 1 82  ? 46.792  -14.166 -17.371 1   67.28 ? 67  ILE   B CB  1 
ATOM   3559 N  N   . ASP   B 1 83  ? 49.341  -15.743 -15.398 1   66.11 ? 68  ASP   B N   1 
ATOM   3560 C  CA  . ASP   B 1 83  ? 49.546  -16.513 -14.166 1   66.12 ? 68  ASP   B CA  1 
ATOM   3561 C  C   . ASP   B 1 83  ? 49.999  -15.691 -12.946 1   65.5  ? 68  ASP   B C   1 
ATOM   3562 O  O   . ASP   B 1 83  ? 49.822  -16.137 -11.809 1   65.62 ? 68  ASP   B O   1 
ATOM   3563 C  CB  . ASP   B 1 83  ? 50.519  -17.674 -14.411 1   68.62 ? 68  ASP   B CB  1 
ATOM   3564 C  CG  . ASP   B 1 83  ? 50.092  -18.635 -15.504 1   75.61 ? 68  ASP   B CG  1 
ATOM   3565 O  OD1 . ASP   B 1 83  ? 48.933  -18.517 -15.989 1   76.63 ? 68  ASP   B OD1 1 
ATOM   3566 O  OD2 . ASP   B 1 83  ? 50.912  -19.509 -15.88  1   78.63 ? 68  ASP   B OD2 1 
ATOM   3567 N  N   . HIS   B 1 84  ? 50.565  -14.502 -13.17  1   64.63 ? 69  HIS   B N   1 
ATOM   3568 C  CA  . HIS   B 1 84  ? 51.012  -13.654 -12.062 1   64.6  ? 69  HIS   B CA  1 
ATOM   3569 C  C   . HIS   B 1 84  ? 49.908  -12.721 -11.517 1   63.09 ? 69  HIS   B C   1 
ATOM   3570 O  O   . HIS   B 1 84  ? 50.196  -11.855 -10.691 1   63.09 ? 69  HIS   B O   1 
ATOM   3571 C  CB  . HIS   B 1 84  ? 52.286  -12.874 -12.435 1   66.85 ? 69  HIS   B CB  1 
ATOM   3572 C  CG  . HIS   B 1 84  ? 53.324  -13.75  -13.07  1   71.24 ? 69  HIS   B CG  1 
ATOM   3573 N  ND1 . HIS   B 1 84  ? 54.133  -14.578 -12.308 1   73.79 ? 69  HIS   B ND1 1 
ATOM   3574 C  CD2 . HIS   B 1 84  ? 53.578  -13.976 -14.382 1   72.81 ? 69  HIS   B CD2 1 
ATOM   3575 C  CE1 . HIS   B 1 84  ? 54.878  -15.245 -13.176 1   74.55 ? 69  HIS   B CE1 1 
ATOM   3576 N  NE2 . HIS   B 1 84  ? 54.575  -14.919 -14.436 1   74.27 ? 69  HIS   B NE2 1 
ATOM   3577 N  N   . LEU   B 1 85  ? 48.648  -12.894 -11.974 1   61.52 ? 70  LEU   B N   1 
ATOM   3578 C  CA  . LEU   B 1 85  ? 47.49   -12.144 -11.474 1   60.44 ? 70  LEU   B CA  1 
ATOM   3579 C  C   . LEU   B 1 85  ? 46.819  -13.155 -10.548 1   59.4  ? 70  LEU   B C   1 
ATOM   3580 O  O   . LEU   B 1 85  ? 46.044  -14.002 -10.998 1   59.13 ? 70  LEU   B O   1 
ATOM   3581 C  CB  . LEU   B 1 85  ? 46.58   -11.762 -12.647 1   60.07 ? 70  LEU   B CB  1 
ATOM   3582 C  CG  . LEU   B 1 85  ? 47.243  -10.893 -13.701 1   60.38 ? 70  LEU   B CG  1 
ATOM   3583 C  CD1 . LEU   B 1 85  ? 46.438  -10.87  -14.98  1   60.36 ? 70  LEU   B CD1 1 
ATOM   3584 C  CD2 . LEU   B 1 85  ? 47.504  -9.502  -13.167 1   60.73 ? 70  LEU   B CD2 1 
ATOM   3585 N  N   . THR   B 1 86  ? 47.234  -13.144 -9.273  1   58.75 ? 71  THR   B N   1 
ATOM   3586 C  CA  . THR   B 1 86  ? 46.892  -14.173 -8.292  1   58.88 ? 71  THR   B CA  1 
ATOM   3587 C  C   . THR   B 1 86  ? 45.575  -14.002 -7.527  1   58.46 ? 71  THR   B C   1 
ATOM   3588 O  O   . THR   B 1 86  ? 45.105  -14.982 -6.941  1   58.91 ? 71  THR   B O   1 
ATOM   3589 C  CB  . THR   B 1 86  ? 48.051  -14.33  -7.309  1   60.05 ? 71  THR   B CB  1 
ATOM   3590 O  OG1 . THR   B 1 86  ? 48.228  -13.099 -6.588  1   61.2  ? 71  THR   B OG1 1 
ATOM   3591 C  CG2 . THR   B 1 86  ? 49.349  -14.719 -8.021  1   60.23 ? 71  THR   B CG2 1 
ATOM   3592 N  N   . ASP   B 1 87  ? 44.988  -12.8   -7.514  1   57.13 ? 72  ASP   B N   1 
ATOM   3593 C  CA  . ASP   B 1 87  ? 43.72   -12.593 -6.823  1   56.05 ? 72  ASP   B CA  1 
ATOM   3594 C  C   . ASP   B 1 87  ? 42.686  -11.878 -7.712  1   54.76 ? 72  ASP   B C   1 
ATOM   3595 O  O   . ASP   B 1 87  ? 43.05   -11.288 -8.737  1   55.43 ? 72  ASP   B O   1 
ATOM   3596 C  CB  . ASP   B 1 87  ? 43.939  -11.875 -5.482  1   58.02 ? 72  ASP   B CB  1 
ATOM   3597 C  CG  . ASP   B 1 87  ? 44.63   -10.537 -5.599  1   63.9  ? 72  ASP   B CG  1 
ATOM   3598 O  OD1 . ASP   B 1 87  ? 44.578  -9.939  -6.689  1   65.58 ? 72  ASP   B OD1 1 
ATOM   3599 O  OD2 . ASP   B 1 87  ? 45.204  -10.074 -4.59   1   65.72 ? 72  ASP   B OD2 1 
ATOM   3600 N  N   . HIS   B 1 88  ? 41.405  -11.917 -7.314  1   52.15 ? 73  HIS   B N   1 
ATOM   3601 C  CA  . HIS   B 1 88  ? 40.326  -11.301 -8.077  1   50.03 ? 73  HIS   B CA  1 
ATOM   3602 C  C   . HIS   B 1 88  ? 40.577  -9.823  -8.399  1   48.52 ? 73  HIS   B C   1 
ATOM   3603 O  O   . HIS   B 1 88  ? 40.4    -9.433  -9.547  1   48.45 ? 73  HIS   B O   1 
ATOM   3604 C  CB  . HIS   B 1 88  ? 38.978  -11.491 -7.356  1   49.35 ? 73  HIS   B CB  1 
ATOM   3605 C  CG  . HIS   B 1 88  ? 37.799  -11.02  -8.145  1   49.11 ? 73  HIS   B CG  1 
ATOM   3606 N  ND1 . HIS   B 1 88  ? 37.282  -11.77  -9.194  1   50.52 ? 73  HIS   B ND1 1 
ATOM   3607 C  CD2 . HIS   B 1 88  ? 37.075  -9.886  -8.021  1   49.48 ? 73  HIS   B CD2 1 
ATOM   3608 C  CE1 . HIS   B 1 88  ? 36.262  -11.073 -9.665  1   50.5  ? 73  HIS   B CE1 1 
ATOM   3609 N  NE2 . HIS   B 1 88  ? 36.09   -9.94   -8.979  1   50.39 ? 73  HIS   B NE2 1 
ATOM   3610 N  N   . LYS   B 1 89  ? 41.036  -9.024  -7.417  1   47.4  ? 74  LYS   B N   1 
ATOM   3611 C  CA  . LYS   B 1 89  ? 41.28   -7.6    -7.615  1   47.22 ? 74  LYS   B CA  1 
ATOM   3612 C  C   . LYS   B 1 89  ? 42.352  -7.29   -8.666  1   48.02 ? 74  LYS   B C   1 
ATOM   3613 O  O   . LYS   B 1 89  ? 42.152  -6.37   -9.471  1   48.4  ? 74  LYS   B O   1 
ATOM   3614 C  CB  . LYS   B 1 89  ? 41.577  -6.878  -6.296  1   47.79 ? 74  LYS   B CB  1 
ATOM   3615 C  CG  . LYS   B 1 89  ? 40.342  -6.737  -5.423  1   50.54 ? 74  LYS   B CG  1 
ATOM   3616 C  CD  . LYS   B 1 89  ? 40.494  -5.632  -4.42   1   53.94 ? 74  LYS   B CD  1 
ATOM   3617 C  CE  . LYS   B 1 89  ? 39.375  -5.639  -3.416  1   57.53 ? 74  LYS   B CE  1 
ATOM   3618 N  NZ  . LYS   B 1 89  ? 39.518  -4.525  -2.442  1   59.47 ? 74  LYS   B NZ  1 
ATOM   3619 N  N   . SER   B 1 90  ? 43.471  -8.042  -8.677  1   47.52 ? 75  SER   B N   1 
ATOM   3620 C  CA  . SER   B 1 90  ? 44.498  -7.823  -9.689  1   47.24 ? 75  SER   B CA  1 
ATOM   3621 C  C   . SER   B 1 90  ? 43.97   -8.278  -11.066 1   46.46 ? 75  SER   B C   1 
ATOM   3622 O  O   . SER   B 1 90  ? 44.277  -7.635  -12.057 1   46.86 ? 75  SER   B O   1 
ATOM   3623 C  CB  . SER   B 1 90  ? 45.816  -8.512  -9.325  1   48.06 ? 75  SER   B CB  1 
ATOM   3624 O  OG  . SER   B 1 90  ? 45.696  -9.925  -9.296  1   50.64 ? 75  SER   B OG  1 
ATOM   3625 N  N   . GLN   B 1 91  ? 43.139  -9.337  -11.127 1   45.42 ? 76  GLN   B N   1 
ATOM   3626 C  CA  . GLN   B 1 91  ? 42.561  -9.793  -12.392 1   45.35 ? 76  GLN   B CA  1 
ATOM   3627 C  C   . GLN   B 1 91  ? 41.541  -8.768  -12.951 1   44.91 ? 76  GLN   B C   1 
ATOM   3628 O  O   . GLN   B 1 91  ? 41.436  -8.585  -14.178 1   45.41 ? 76  GLN   B O   1 
ATOM   3629 C  CB  . GLN   B 1 91  ? 41.896  -11.154 -12.204 1   47.68 ? 76  GLN   B CB  1 
ATOM   3630 C  CG  . GLN   B 1 91  ? 42.882  -12.302 -11.983 1   53.07 ? 76  GLN   B CG  1 
ATOM   3631 C  CD  . GLN   B 1 91  ? 42.23   -13.531 -11.388 1   58.74 ? 76  GLN   B CD  1 
ATOM   3632 O  OE1 . GLN   B 1 91  ? 41.01   -13.696 -11.411 1   60.46 ? 76  GLN   B OE1 1 
ATOM   3633 N  NE2 . GLN   B 1 91  ? 43.032  -14.427 -10.838 1   59.09 ? 76  GLN   B NE2 1 
ATOM   3634 N  N   . ARG   B 1 92  ? 40.798  -8.096  -12.041 1   43.27 ? 77  ARG   B N   1 
ATOM   3635 C  CA  . ARG   B 1 92  ? 39.811  -7.079  -12.402 1   41.88 ? 77  ARG   B CA  1 
ATOM   3636 C  C   . ARG   B 1 92  ? 40.539  -5.835  -12.919 1   41.56 ? 77  ARG   B C   1 
ATOM   3637 O  O   . ARG   B 1 92  ? 40.106  -5.247  -13.908 1   41.05 ? 77  ARG   B O   1 
ATOM   3638 C  CB  . ARG   B 1 92  ? 38.908  -6.714  -11.197 1   41.02 ? 77  ARG   B CB  1 
ATOM   3639 C  CG  . ARG   B 1 92  ? 37.848  -7.767  -10.883 1   40.6  ? 77  ARG   B CG  1 
ATOM   3640 C  CD  . ARG   B 1 92  ? 36.691  -7.849  -11.886 1   39.99 ? 77  ARG   B CD  1 
ATOM   3641 N  NE  . ARG   B 1 92  ? 35.861  -6.637  -11.855 1   38.98 ? 77  ARG   B NE  1 
ATOM   3642 C  CZ  . ARG   B 1 92  ? 34.877  -6.422  -10.982 1   38.62 ? 77  ARG   B CZ  1 
ATOM   3643 N  NH1 . ARG   B 1 92  ? 34.566  -7.348  -10.077 1   38.6  ? 77  ARG   B NH1 1 
ATOM   3644 N  NH2 . ARG   B 1 92  ? 34.189  -5.293  -11.017 1   35.16 ? 77  ARG   B NH2 1 
ATOM   3645 N  N   . LEU   B 1 93  ? 41.643  -5.437  -12.255 1   41.4  ? 78  LEU   B N   1 
ATOM   3646 C  CA  . LEU   B 1 93  ? 42.432  -4.276  -12.693 1   41.5  ? 78  LEU   B CA  1 
ATOM   3647 C  C   . LEU   B 1 93  ? 43.068  -4.581  -14.056 1   41.31 ? 78  LEU   B C   1 
ATOM   3648 O  O   . LEU   B 1 93  ? 43.039  -3.732  -14.941 1   41.87 ? 78  LEU   B O   1 
ATOM   3649 C  CB  . LEU   B 1 93  ? 43.517  -3.916  -11.66  1   41.91 ? 78  LEU   B CB  1 
ATOM   3650 C  CG  . LEU   B 1 93  ? 44.531  -2.854  -12.086 1   42.89 ? 78  LEU   B CG  1 
ATOM   3651 C  CD1 . LEU   B 1 93  ? 43.846  -1.504  -12.336 1   43.12 ? 78  LEU   B CD1 1 
ATOM   3652 C  CD2 . LEU   B 1 93  ? 45.626  -2.724  -11.057 1   43.63 ? 78  LEU   B CD2 1 
ATOM   3653 N  N   . ALA   B 1 94  ? 43.572  -5.804  -14.247 1   40.69 ? 79  ALA   B N   1 
ATOM   3654 C  CA  . ALA   B 1 94  ? 44.176  -6.201  -15.51  1   40.88 ? 79  ALA   B CA  1 
ATOM   3655 C  C   . ALA   B 1 94  ? 43.148  -6.163  -16.639 1   40.39 ? 79  ALA   B C   1 
ATOM   3656 O  O   . ALA   B 1 94  ? 43.487  -5.785  -17.761 1   40.35 ? 79  ALA   B O   1 
ATOM   3657 C  CB  . ALA   B 1 94  ? 44.779  -7.594  -15.391 1   41.5  ? 79  ALA   B CB  1 
ATOM   3658 N  N   . ARG   B 1 95  ? 41.892  -6.561  -16.342 1   39.38 ? 80  ARG   B N   1 
ATOM   3659 C  CA  . ARG   B 1 95  ? 40.793  -6.528  -17.308 1   38.28 ? 80  ARG   B CA  1 
ATOM   3660 C  C   . ARG   B 1 95  ? 40.508  -5.086  -17.701 1   37.47 ? 80  ARG   B C   1 
ATOM   3661 O  O   . ARG   B 1 95  ? 40.247  -4.81   -18.869 1   38.36 ? 80  ARG   B O   1 
ATOM   3662 C  CB  . ARG   B 1 95  ? 39.524  -7.138  -16.691 1   38.19 ? 80  ARG   B CB  1 
ATOM   3663 C  CG  . ARG   B 1 95  ? 39.133  -8.453  -17.307 1   38.99 ? 80  ARG   B CG  1 
ATOM   3664 C  CD  . ARG   B 1 95  ? 37.703  -8.797  -16.934 1   38.85 ? 80  ARG   B CD  1 
ATOM   3665 N  NE  . ARG   B 1 95  ? 36.722  -7.981  -17.645 1   39.51 ? 80  ARG   B NE  1 
ATOM   3666 C  CZ  . ARG   B 1 95  ? 36.264  -8.248  -18.863 1   39.88 ? 80  ARG   B CZ  1 
ATOM   3667 N  NH1 . ARG   B 1 95  ? 36.741  -9.283  -19.55  1   38.05 ? 80  ARG   B NH1 1 
ATOM   3668 N  NH2 . ARG   B 1 95  ? 35.338  -7.475  -19.413 1   39.34 ? 80  ARG   B NH2 1 
ATOM   3669 N  N   . LEU   B 1 96  ? 40.531  -4.168  -16.731 1   35.94 ? 81  LEU   B N   1 
ATOM   3670 C  CA  . LEU   B 1 96  ? 40.29   -2.758  -16.995 1   35.7  ? 81  LEU   B CA  1 
ATOM   3671 C  C   . LEU   B 1 96  ? 41.436  -2.195  -17.886 1   37.52 ? 81  LEU   B C   1 
ATOM   3672 O  O   . LEU   B 1 96  ? 41.174  -1.537  -18.898 1   37.99 ? 81  LEU   B O   1 
ATOM   3673 C  CB  . LEU   B 1 96  ? 40.209  -2.041  -15.649 1   34.85 ? 81  LEU   B CB  1 
ATOM   3674 C  CG  . LEU   B 1 96  ? 40.045  -0.532  -15.623 1   35.06 ? 81  LEU   B CG  1 
ATOM   3675 C  CD1 . LEU   B 1 96  ? 38.866  -0.055  -16.476 1   34.41 ? 81  LEU   B CD1 1 
ATOM   3676 C  CD2 . LEU   B 1 96  ? 39.947  -0.067  -14.216 1   35.99 ? 81  LEU   B CD2 1 
ATOM   3677 N  N   . VAL   B 1 97  ? 42.696  -2.486  -17.511 1   38.05 ? 82  VAL   B N   1 
ATOM   3678 C  CA  . VAL   B 1 97  ? 43.9    -2.102  -18.248 1   39.07 ? 82  VAL   B CA  1 
ATOM   3679 C  C   . VAL   B 1 97  ? 43.823  -2.599  -19.697 1   39.28 ? 82  VAL   B C   1 
ATOM   3680 O  O   . VAL   B 1 97  ? 43.874  -1.779  -20.593 1   39.99 ? 82  VAL   B O   1 
ATOM   3681 C  CB  . VAL   B 1 97  ? 45.186  -2.602  -17.518 1   40.05 ? 82  VAL   B CB  1 
ATOM   3682 C  CG1 . VAL   B 1 97  ? 46.417  -2.563  -18.435 1   40.16 ? 82  VAL   B CG1 1 
ATOM   3683 C  CG2 . VAL   B 1 97  ? 45.432  -1.807  -16.245 1   40.54 ? 82  VAL   B CG2 1 
ATOM   3684 N  N   . LEU   B 1 98  ? 43.655  -3.916  -19.926 1   39.25 ? 83  LEU   B N   1 
ATOM   3685 C  CA  . LEU   B 1 98  ? 43.601  -4.497  -21.266 1   40.16 ? 83  LEU   B CA  1 
ATOM   3686 C  C   . LEU   B 1 98  ? 42.41   -4.027  -22.083 1   40.54 ? 83  LEU   B C   1 
ATOM   3687 O  O   . LEU   B 1 98  ? 42.509  -3.887  -23.31  1   41.37 ? 83  LEU   B O   1 
ATOM   3688 C  CB  . LEU   B 1 98  ? 43.617  -6.029  -21.21  1   40.81 ? 83  LEU   B CB  1 
ATOM   3689 C  CG  . LEU   B 1 98  ? 44.88   -6.665  -20.611 1   42.72 ? 83  LEU   B CG  1 
ATOM   3690 C  CD1 . LEU   B 1 98  ? 44.75   -8.165  -20.565 1   43.33 ? 83  LEU   B CD1 1 
ATOM   3691 C  CD2 . LEU   B 1 98  ? 46.106  -6.315  -21.423 1   43.71 ? 83  LEU   B CD2 1 
ATOM   3692 N  N   . GLY   B 1 99  ? 41.285  -3.809  -21.408 1   39.05 ? 84  GLY   B N   1 
ATOM   3693 C  CA  . GLY   B 1 99  ? 40.08   -3.359  -22.078 1   38.45 ? 84  GLY   B CA  1 
ATOM   3694 C  C   . GLY   B 1 99  ? 40.196  -1.943  -22.581 1   36.55 ? 84  GLY   B C   1 
ATOM   3695 O  O   . GLY   B 1 99  ? 39.753  -1.661  -23.686 1   35.82 ? 84  GLY   B O   1 
ATOM   3696 N  N   . CYS   B 1 100 ? 40.789  -1.049  -21.782 1   36.35 ? 85  CYS   B N   1 
ATOM   3697 C  CA  . CYS   B 1 100 ? 40.995  0.35    -22.178 1   37.53 ? 85  CYS   B CA  1 
ATOM   3698 C  C   . CYS   B 1 100 ? 41.991  0.425   -23.337 1   39.27 ? 85  CYS   B C   1 
ATOM   3699 O  O   . CYS   B 1 100 ? 41.786  1.196   -24.281 1   39.58 ? 85  CYS   B O   1 
ATOM   3700 C  CB  . CYS   B 1 100 ? 41.449  1.197   -20.995 1   37.54 ? 85  CYS   B CB  1 
ATOM   3701 S  SG  . CYS   B 1 100 ? 40.147  1.521   -19.778 1   41.14 ? 85  CYS   B SG  1 
ATOM   3702 N  N   . ILE   B 1 101 ? 43.042  -0.415  -23.285 1   39.98 ? 86  ILE   B N   1 
ATOM   3703 C  CA  . ILE   B 1 101 ? 44.034  -0.51   -24.346 1   40.76 ? 86  ILE   B CA  1 
ATOM   3704 C  C   . ILE   B 1 101 ? 43.371  -1.017  -25.625 1   41.37 ? 86  ILE   B C   1 
ATOM   3705 O  O   . ILE   B 1 101 ? 43.571  -0.431  -26.684 1   41.25 ? 86  ILE   B O   1 
ATOM   3706 C  CB  . ILE   B 1 101 ? 45.239  -1.379  -23.906 1   41.37 ? 86  ILE   B CB  1 
ATOM   3707 C  CG1 . ILE   B 1 101 ? 46.029  -0.684  -22.775 1   42.72 ? 86  ILE   B CG1 1 
ATOM   3708 C  CG2 . ILE   B 1 101 ? 46.16   -1.669  -25.086 1   41.83 ? 86  ILE   B CG2 1 
ATOM   3709 C  CD1 . ILE   B 1 101 ? 47.077  -1.636  -22.11  1   44.36 ? 86  ILE   B CD1 1 
ATOM   3710 N  N   . THR   B 1 102 ? 42.543  -2.067  -25.524 1   42.01 ? 87  THR   B N   1 
ATOM   3711 C  CA  . THR   B 1 102 ? 41.803  -2.608  -26.67  1   42.5  ? 87  THR   B CA  1 
ATOM   3712 C  C   . THR   B 1 102 ? 40.929  -1.537  -27.339 1   43.43 ? 87  THR   B C   1 
ATOM   3713 O  O   . THR   B 1 102 ? 40.992  -1.379  -28.552 1   43.3  ? 87  THR   B O   1 
ATOM   3714 C  CB  . THR   B 1 102 ? 41.028  -3.853  -26.274 1   42.91 ? 87  THR   B CB  1 
ATOM   3715 O  OG1 . THR   B 1 102 ? 41.955  -4.823  -25.791 1   43.68 ? 87  THR   B OG1 1 
ATOM   3716 C  CG2 . THR   B 1 102 ? 40.239  -4.442  -27.424 1   42.88 ? 87  THR   B CG2 1 
ATOM   3717 N  N   . MET   B 1 103 ? 40.166  -0.761  -26.555 1   43.57 ? 88  MET   B N   1 
ATOM   3718 C  CA  . MET   B 1 103 ? 39.332  0.303   -27.113 1   43.67 ? 88  MET   B CA  1 
ATOM   3719 C  C   . MET   B 1 103 ? 40.175  1.351   -27.842 1   43.34 ? 88  MET   B C   1 
ATOM   3720 O  O   . MET   B 1 103 ? 39.816  1.776   -28.937 1   43.18 ? 88  MET   B O   1 
ATOM   3721 C  CB  . MET   B 1 103 ? 38.487  0.991   -26.015 1   44.69 ? 88  MET   B CB  1 
ATOM   3722 C  CG  . MET   B 1 103 ? 37.39   0.118   -25.447 1   48.32 ? 88  MET   B CG  1 
ATOM   3723 S  SD  . MET   B 1 103 ? 36.276  -0.571  -26.707 1   57.46 ? 88  MET   B SD  1 
ATOM   3724 C  CE  . MET   B 1 103 ? 34.856  -0.93   -25.715 1   58.31 ? 88  MET   B CE  1 
ATOM   3725 N  N   . ALA   B 1 104 ? 41.275  1.782   -27.229 1   43.21 ? 89  ALA   B N   1 
ATOM   3726 C  CA  . ALA   B 1 104 ? 42.143  2.79    -27.823 1   43.84 ? 89  ALA   B CA  1 
ATOM   3727 C  C   . ALA   B 1 104 ? 42.792  2.245   -29.114 1   44.28 ? 89  ALA   B C   1 
ATOM   3728 O  O   . ALA   B 1 104 ? 42.913  2.975   -30.087 1   44.22 ? 89  ALA   B O   1 
ATOM   3729 C  CB  . ALA   B 1 104 ? 43.206  3.205   -26.825 1   44.26 ? 89  ALA   B CB  1 
ATOM   3730 N  N   . TYR   B 1 105 ? 43.165  0.965   -29.124 1   44.16 ? 90  TYR   B N   1 
ATOM   3731 C  CA  . TYR   B 1 105 ? 43.782  0.344   -30.27  1   45.33 ? 90  TYR   B CA  1 
ATOM   3732 C  C   . TYR   B 1 105 ? 42.783  0.238   -31.421 1   45.01 ? 90  TYR   B C   1 
ATOM   3733 O  O   . TYR   B 1 105 ? 43.11   0.592   -32.553 1   45.39 ? 90  TYR   B O   1 
ATOM   3734 C  CB  . TYR   B 1 105 ? 44.359  -1.04   -29.901 1   46.36 ? 90  TYR   B CB  1 
ATOM   3735 C  CG  . TYR   B 1 105 ? 45.164  -1.634  -31.037 1   48.56 ? 90  TYR   B CG  1 
ATOM   3736 C  CD1 . TYR   B 1 105 ? 46.503  -1.312  -31.209 1   49.98 ? 90  TYR   B CD1 1 
ATOM   3737 C  CD2 . TYR   B 1 105 ? 44.57   -2.46   -31.977 1   50.08 ? 90  TYR   B CD2 1 
ATOM   3738 C  CE1 . TYR   B 1 105 ? 47.233  -1.81   -32.281 1   50.96 ? 90  TYR   B CE1 1 
ATOM   3739 C  CE2 . TYR   B 1 105 ? 45.28   -2.934  -33.071 1   51.5  ? 90  TYR   B CE2 1 
ATOM   3740 C  CZ  . TYR   B 1 105 ? 46.615  -2.613  -33.215 1   52.52 ? 90  TYR   B CZ  1 
ATOM   3741 O  OH  . TYR   B 1 105 ? 47.321  -3.11   -34.277 1   54.71 ? 90  TYR   B OH  1 
ATOM   3742 N  N   . VAL   B 1 106 ? 41.57   -0.245  -31.139 1   43.71 ? 91  VAL   B N   1 
ATOM   3743 C  CA  . VAL   B 1 106 ? 40.557  -0.405  -32.161 1   43.44 ? 91  VAL   B CA  1 
ATOM   3744 C  C   . VAL   B 1 106 ? 40.118  0.929   -32.761 1   42.85 ? 91  VAL   B C   1 
ATOM   3745 O  O   . VAL   B 1 106 ? 40.061  1.049   -33.981 1   42.77 ? 91  VAL   B O   1 
ATOM   3746 C  CB  . VAL   B 1 106 ? 39.36   -1.243  -31.647 1   44.42 ? 91  VAL   B CB  1 
ATOM   3747 C  CG1 . VAL   B 1 106 ? 38.185  -1.205  -32.619 1   45.41 ? 91  VAL   B CG1 1 
ATOM   3748 C  CG2 . VAL   B 1 106 ? 39.779  -2.677  -31.383 1   44.91 ? 91  VAL   B CG2 1 
ATOM   3749 N  N   . TRP   B 1 107 ? 39.822  1.929   -31.927 1   41.98 ? 92  TRP   B N   1 
ATOM   3750 C  CA  . TRP   B 1 107 ? 39.278  3.188   -32.419 1   41.91 ? 92  TRP   B CA  1 
ATOM   3751 C  C   . TRP   B 1 107 ? 40.308  4.26    -32.77  1   42.27 ? 92  TRP   B C   1 
ATOM   3752 O  O   . TRP   B 1 107 ? 39.946  5.24    -33.428 1   42.73 ? 92  TRP   B O   1 
ATOM   3753 C  CB  . TRP   B 1 107 ? 38.221  3.748   -31.435 1   41.43 ? 92  TRP   B CB  1 
ATOM   3754 C  CG  . TRP   B 1 107 ? 37.142  2.742   -31.086 1   41.74 ? 92  TRP   B CG  1 
ATOM   3755 C  CD1 . TRP   B 1 107 ? 36.845  2.261   -29.842 1   42.38 ? 92  TRP   B CD1 1 
ATOM   3756 C  CD2 . TRP   B 1 107 ? 36.26   2.063   -31.995 1   42.03 ? 92  TRP   B CD2 1 
ATOM   3757 N  NE1 . TRP   B 1 107 ? 35.835  1.334   -29.92  1   42.37 ? 92  TRP   B NE1 1 
ATOM   3758 C  CE2 . TRP   B 1 107 ? 35.444  1.206   -31.228 1   42.61 ? 92  TRP   B CE2 1 
ATOM   3759 C  CE3 . TRP   B 1 107 ? 36.053  2.123   -33.38  1   42.66 ? 92  TRP   B CE3 1 
ATOM   3760 C  CZ2 . TRP   B 1 107 ? 34.468  0.392   -31.805 1   43.16 ? 92  TRP   B CZ2 1 
ATOM   3761 C  CZ3 . TRP   B 1 107 ? 35.087  1.312   -33.942 1   43.52 ? 92  TRP   B CZ3 1 
ATOM   3762 C  CH2 . TRP   B 1 107 ? 34.297  0.475   -33.156 1   43.43 ? 92  TRP   B CH2 1 
ATOM   3763 N  N   . GLY   B 1 108 ? 41.539  4.099   -32.317 1   41.31 ? 93  GLY   B N   1 
ATOM   3764 C  CA  . GLY   B 1 108 ? 42.602  5.053   -32.595 1   41.57 ? 93  GLY   B CA  1 
ATOM   3765 C  C   . GLY   B 1 108 ? 42.304  6.438   -32.076 1   41.64 ? 93  GLY   B C   1 
ATOM   3766 O  O   . GLY   B 1 108 ? 41.895  6.586   -30.921 1   42.64 ? 93  GLY   B O   1 
ATOM   3767 N  N   . LYS   B 1 109 ? 42.441  7.454   -32.935 1   40.72 ? 94  LYS   B N   1 
ATOM   3768 C  CA  . LYS   B 1 109 ? 42.151  8.824   -32.518 1   41.88 ? 94  LYS   B CA  1 
ATOM   3769 C  C   . LYS   B 1 109 ? 40.656  9.172   -32.466 1   43.05 ? 94  LYS   B C   1 
ATOM   3770 O  O   . LYS   B 1 109 ? 40.325  10.31   -32.148 1   42.8  ? 94  LYS   B O   1 
ATOM   3771 C  CB  . LYS   B 1 109 ? 42.881  9.857   -33.39  1   44.03 ? 94  LYS   B CB  1 
ATOM   3772 C  CG  . LYS   B 1 109 ? 44.39   9.796   -33.29  1   46.17 ? 94  LYS   B CG  1 
ATOM   3773 C  CD  . LYS   B 1 109 ? 44.994  11.015  -33.948 1   49.26 ? 94  LYS   B CD  1 
ATOM   3774 C  CE  . LYS   B 1 109 ? 46.483  10.869  -34.138 1   52.07 ? 94  LYS   B CE  1 
ATOM   3775 N  NZ  . LYS   B 1 109 ? 47.04   12.07   -34.808 1   53.14 ? 94  LYS   B NZ  1 
ATOM   3776 N  N   . GLY   B 1 110 ? 39.785  8.217   -32.77  1   44.03 ? 95  GLY   B N   1 
ATOM   3777 C  CA  . GLY   B 1 110 ? 38.349  8.453   -32.737 1   46.38 ? 95  GLY   B CA  1 
ATOM   3778 C  C   . GLY   B 1 110 ? 37.814  9.264   -33.899 1   47.88 ? 95  GLY   B C   1 
ATOM   3779 O  O   . GLY   B 1 110 ? 36.776  9.932   -33.774 1   48.15 ? 95  GLY   B O   1 
ATOM   3780 N  N   . HIS   B 1 111 ? 38.526  9.215   -35.033 1   48.19 ? 96  HIS   B N   1 
ATOM   3781 C  CA  . HIS   B 1 111 ? 38.128  9.925   -36.244 1   49.66 ? 96  HIS   B CA  1 
ATOM   3782 C  C   . HIS   B 1 111 ? 37.619  8.994   -37.355 1   50.14 ? 96  HIS   B C   1 
ATOM   3783 O  O   . HIS   B 1 111 ? 37.307  9.491   -38.429 1   50.69 ? 96  HIS   B O   1 
ATOM   3784 C  CB  . HIS   B 1 111 ? 39.267  10.793  -36.807 1   50.8  ? 96  HIS   B CB  1 
ATOM   3785 C  CG  . HIS   B 1 111 ? 39.894  11.754  -35.846 1   53.95 ? 96  HIS   B CG  1 
ATOM   3786 N  ND1 . HIS   B 1 111 ? 39.131  12.521  -34.968 1   56.38 ? 96  HIS   B ND1 1 
ATOM   3787 C  CD2 . HIS   B 1 111 ? 41.197  12.102  -35.712 1   55.26 ? 96  HIS   B CD2 1 
ATOM   3788 C  CE1 . HIS   B 1 111 ? 39.999  13.269  -34.299 1   57.06 ? 96  HIS   B CE1 1 
ATOM   3789 N  NE2 . HIS   B 1 111 ? 41.257  13.05   -34.709 1   56.86 ? 96  HIS   B NE2 1 
ATOM   3790 N  N   . GLY   B 1 112 ? 37.561  7.681   -37.116 1   49.9  ? 97  GLY   B N   1 
ATOM   3791 C  CA  . GLY   B 1 112 ? 37.054  6.738   -38.099 1   50.33 ? 97  GLY   B CA  1 
ATOM   3792 C  C   . GLY   B 1 112 ? 38.036  5.714   -38.619 1   51.15 ? 97  GLY   B C   1 
ATOM   3793 O  O   . GLY   B 1 112 ? 37.612  4.763   -39.282 1   51.3  ? 97  GLY   B O   1 
ATOM   3794 N  N   . ASP   B 1 113 ? 39.354  5.894   -38.352 1   51.17 ? 98  ASP   B N   1 
ATOM   3795 C  CA  . ASP   B 1 113 ? 40.351  4.924   -38.808 1   52.07 ? 98  ASP   B CA  1 
ATOM   3796 C  C   . ASP   B 1 113 ? 40.431  3.836   -37.775 1   52.07 ? 98  ASP   B C   1 
ATOM   3797 O  O   . ASP   B 1 113 ? 41.048  4.017   -36.716 1   51.75 ? 98  ASP   B O   1 
ATOM   3798 C  CB  . ASP   B 1 113 ? 41.745  5.545   -39.031 1   54.68 ? 98  ASP   B CB  1 
ATOM   3799 C  CG  . ASP   B 1 113 ? 42.731  4.494   -39.538 1   60.33 ? 98  ASP   B CG  1 
ATOM   3800 O  OD1 . ASP   B 1 113 ? 42.333  3.677   -40.395 1   62.19 ? 98  ASP   B OD1 1 
ATOM   3801 O  OD2 . ASP   B 1 113 ? 43.875  4.454   -39.036 1   61.7  ? 98  ASP   B OD2 1 
ATOM   3802 N  N   . VAL   B 1 114 ? 39.839  2.702   -38.096 1   52.04 ? 99  VAL   B N   1 
ATOM   3803 C  CA  . VAL   B 1 114 ? 39.737  1.589   -37.177 1   52.84 ? 99  VAL   B CA  1 
ATOM   3804 C  C   . VAL   B 1 114 ? 40.715  0.446   -37.457 1   53.29 ? 99  VAL   B C   1 
ATOM   3805 O  O   . VAL   B 1 114 ? 41.22   0.314   -38.568 1   53.94 ? 99  VAL   B O   1 
ATOM   3806 C  CB  . VAL   B 1 114 ? 38.269  1.083   -37.139 1   53.62 ? 99  VAL   B CB  1 
ATOM   3807 C  CG1 . VAL   B 1 114 ? 37.31   2.219   -36.809 1   54.21 ? 99  VAL   B CG1 1 
ATOM   3808 C  CG2 . VAL   B 1 114 ? 37.878  0.422   -38.442 1   54.17 ? 99  VAL   B CG2 1 
ATOM   3809 N  N   . ARG   B 1 115 ? 40.986  -0.369  -36.428 1   52.43 ? 100 ARG   B N   1 
ATOM   3810 C  CA  . ARG   B 1 115 ? 41.782  -1.574  -36.526 1   52.28 ? 100 ARG   B CA  1 
ATOM   3811 C  C   . ARG   B 1 115 ? 40.822  -2.725  -36.329 1   51.85 ? 100 ARG   B C   1 
ATOM   3812 O  O   . ARG   B 1 115 ? 40.027  -2.723  -35.389 1   51.58 ? 100 ARG   B O   1 
ATOM   3813 C  CB  . ARG   B 1 115 ? 42.892  -1.627  -35.461 1   53.79 ? 100 ARG   B CB  1 
ATOM   3814 C  CG  . ARG   B 1 115 ? 44.098  -0.769  -35.777 1   57.38 ? 100 ARG   B CG  1 
ATOM   3815 C  CD  . ARG   B 1 115 ? 44.842  -1.267  -36.996 1   61.68 ? 100 ARG   B CD  1 
ATOM   3816 N  NE  . ARG   B 1 115 ? 46.28   -1.05   -36.844 1   64.86 ? 100 ARG   B NE  1 
ATOM   3817 C  CZ  . ARG   B 1 115 ? 46.948  -0.029  -37.374 1   66.06 ? 100 ARG   B CZ  1 
ATOM   3818 N  NH1 . ARG   B 1 115 ? 48.254  0.089   -37.176 1   65.54 ? 100 ARG   B NH1 1 
ATOM   3819 N  NH2 . ARG   B 1 115 ? 46.316  0.875   -38.117 1   65.09 ? 100 ARG   B NH2 1 
ATOM   3820 N  N   . LYS   B 1 116 ? 40.874  -3.702  -37.224 1   51.88 ? 101 LYS   B N   1 
ATOM   3821 C  CA  . LYS   B 1 116 ? 40.007  -4.87   -37.175 1   52.29 ? 101 LYS   B CA  1 
ATOM   3822 C  C   . LYS   B 1 116 ? 40.681  -6.129  -36.626 1   52.27 ? 101 LYS   B C   1 
ATOM   3823 O  O   . LYS   B 1 116 ? 40.041  -7.173  -36.557 1   52.67 ? 101 LYS   B O   1 
ATOM   3824 C  CB  . LYS   B 1 116 ? 39.398  -5.122  -38.559 1   55.08 ? 101 LYS   B CB  1 
ATOM   3825 C  CG  . LYS   B 1 116 ? 38.631  -3.907  -39.082 1   60.75 ? 101 LYS   B CG  1 
ATOM   3826 C  CD  . LYS   B 1 116 ? 37.679  -4.265  -40.211 1   66.54 ? 101 LYS   B CD  1 
ATOM   3827 C  CE  . LYS   B 1 116 ? 36.777  -3.123  -40.61  1   71.08 ? 101 LYS   B CE  1 
ATOM   3828 N  NZ  . LYS   B 1 116 ? 37.529  -1.887  -40.96  1   73.82 ? 101 LYS   B NZ  1 
ATOM   3829 N  N   . VAL   B 1 117 ? 41.96   -6.05   -36.249 1   52.23 ? 102 VAL   B N   1 
ATOM   3830 C  CA  . VAL   B 1 117 ? 42.674  -7.191  -35.692 1   53.27 ? 102 VAL   B CA  1 
ATOM   3831 C  C   . VAL   B 1 117 ? 43.356  -6.724  -34.416 1   54.07 ? 102 VAL   B C   1 
ATOM   3832 O  O   . VAL   B 1 117 ? 44.081  -5.734  -34.439 1   54.27 ? 102 VAL   B O   1 
ATOM   3833 C  CB  . VAL   B 1 117 ? 43.717  -7.793  -36.684 1   54.12 ? 102 VAL   B CB  1 
ATOM   3834 C  CG1 . VAL   B 1 117 ? 44.388  -9.026  -36.081 1   54.79 ? 102 VAL   B CG1 1 
ATOM   3835 C  CG2 . VAL   B 1 117 ? 43.077  -8.135  -38.029 1   54.52 ? 102 VAL   B CG2 1 
ATOM   3836 N  N   . LEU   B 1 118 ? 43.106  -7.4    -33.298 1   54.43 ? 103 LEU   B N   1 
ATOM   3837 C  CA  . LEU   B 1 118 ? 43.75   -7.058  -32.033 1   54.85 ? 103 LEU   B CA  1 
ATOM   3838 C  C   . LEU   B 1 118 ? 44.996  -7.949  -31.965 1   55.9  ? 103 LEU   B C   1 
ATOM   3839 O  O   . LEU   B 1 118 ? 44.873  -9.17   -32.054 1   56.08 ? 103 LEU   B O   1 
ATOM   3840 C  CB  . LEU   B 1 118 ? 42.802  -7.341  -30.851 1   54.12 ? 103 LEU   B CB  1 
ATOM   3841 C  CG  . LEU   B 1 118 ? 43.323  -6.914  -29.477 1   54.39 ? 103 LEU   B CG  1 
ATOM   3842 C  CD1 . LEU   B 1 118 ? 43.509  -5.415  -29.4   1   54.07 ? 103 LEU   B CD1 1 
ATOM   3843 C  CD2 . LEU   B 1 118 ? 42.407  -7.394  -28.368 1   55.1  ? 103 LEU   B CD2 1 
ATOM   3844 N  N   . PRO   B 1 119 ? 46.2    -7.361  -31.877 1   56.49 ? 104 PRO   B N   1 
ATOM   3845 C  CA  . PRO   B 1 119 ? 47.429  -8.182  -31.879 1   57.4  ? 104 PRO   B CA  1 
ATOM   3846 C  C   . PRO   B 1 119 ? 47.455  -9.271  -30.818 1   58.67 ? 104 PRO   B C   1 
ATOM   3847 O  O   . PRO   B 1 119 ? 46.97   -9.051  -29.71  1   59.13 ? 104 PRO   B O   1 
ATOM   3848 C  CB  . PRO   B 1 119 ? 48.546  -7.161  -31.659 1   57.68 ? 104 PRO   B CB  1 
ATOM   3849 C  CG  . PRO   B 1 119 ? 47.965  -5.858  -32.089 1   57.89 ? 104 PRO   B CG  1 
ATOM   3850 C  CD  . PRO   B 1 119 ? 46.505  -5.926  -31.772 1   56.01 ? 104 PRO   B CD  1 
ATOM   3851 N  N   . ARG   B 1 120 ? 48.02   -10.443 -31.164 1   58.52 ? 105 ARG   B N   1 
ATOM   3852 C  CA  . ARG   B 1 120 ? 48.091  -11.609 -30.289 1   58.82 ? 105 ARG   B CA  1 
ATOM   3853 C  C   . ARG   B 1 120 ? 48.693  -11.353 -28.927 1   59.03 ? 105 ARG   B C   1 
ATOM   3854 O  O   . ARG   B 1 120 ? 48.252  -11.962 -27.953 1   59.36 ? 105 ARG   B O   1 
ATOM   3855 C  CB  . ARG   B 1 120 ? 48.832  -12.765 -30.975 1   59.98 ? 105 ARG   B CB  1 
ATOM   3856 N  N   . ASN   B 1 121 ? 49.695  -10.474 -28.84  1   58.84 ? 106 ASN   B N   1 
ATOM   3857 C  CA  . ASN   B 1 121 ? 50.331  -10.184 -27.551 1   59.18 ? 106 ASN   B CA  1 
ATOM   3858 C  C   . ASN   B 1 121 ? 49.378  -9.561  -26.519 1   59.32 ? 106 ASN   B C   1 
ATOM   3859 O  O   . ASN   B 1 121 ? 49.636  -9.67   -25.316 1   59.45 ? 106 ASN   B O   1 
ATOM   3860 C  CB  . ASN   B 1 121 ? 51.58   -9.342  -27.72  1   59.98 ? 106 ASN   B CB  1 
ATOM   3861 N  N   . ILE   B 1 122 ? 48.28   -8.912  -26.981 1   58.91 ? 107 ILE   B N   1 
ATOM   3862 C  CA  . ILE   B 1 122 ? 47.288  -8.355  -26.066 1   58.93 ? 107 ILE   B CA  1 
ATOM   3863 C  C   . ILE   B 1 122 ? 46.031  -9.228  -26.079 1   58.43 ? 107 ILE   B C   1 
ATOM   3864 O  O   . ILE   B 1 122 ? 45.524  -9.575  -25.012 1   58.63 ? 107 ILE   B O   1 
ATOM   3865 C  CB  . ILE   B 1 122 ? 47.01   -6.837  -26.262 1   59.78 ? 107 ILE   B CB  1 
ATOM   3866 C  CG1 . ILE   B 1 122 ? 45.914  -6.341  -25.313 1   61.17 ? 107 ILE   B CG1 1 
ATOM   3867 C  CG2 . ILE   B 1 122 ? 46.682  -6.48   -27.698 1   60.2  ? 107 ILE   B CG2 1 
ATOM   3868 C  CD1 . ILE   B 1 122 ? 46.14   -5.024  -24.862 1   62.74 ? 107 ILE   B CD1 1 
ATOM   3869 N  N   . ALA   B 1 123 ? 45.586  -9.654  -27.272 1   57.46 ? 108 ALA   B N   1 
ATOM   3870 C  CA  . ALA   B 1 123 ? 44.405  -10.49  -27.451 1   57.05 ? 108 ALA   B CA  1 
ATOM   3871 C  C   . ALA   B 1 123 ? 44.431  -11.813 -26.701 1   56.33 ? 108 ALA   B C   1 
ATOM   3872 O  O   . ALA   B 1 123 ? 43.408  -12.192 -26.126 1   56.39 ? 108 ALA   B O   1 
ATOM   3873 C  CB  . ALA   B 1 123 ? 44.139  -10.734 -28.932 1   57.11 ? 108 ALA   B CB  1 
ATOM   3874 N  N   . VAL   B 1 124 ? 45.576  -12.524 -26.705 1   55.17 ? 109 VAL   B N   1 
ATOM   3875 C  CA  . VAL   B 1 124 ? 45.65   -13.808 -26.01  1   54.32 ? 109 VAL   B CA  1 
ATOM   3876 C  C   . VAL   B 1 124 ? 45.511  -13.632 -24.476 1   53.45 ? 109 VAL   B C   1 
ATOM   3877 O  O   . VAL   B 1 124 ? 44.585  -14.232 -23.929 1   53.68 ? 109 VAL   B O   1 
ATOM   3878 C  CB  . VAL   B 1 124 ? 46.871  -14.689 -26.42  1   54.68 ? 109 VAL   B CB  1 
ATOM   3879 C  CG1 . VAL   B 1 124 ? 47.043  -15.883 -25.479 1   54.7  ? 109 VAL   B CG1 1 
ATOM   3880 C  CG2 . VAL   B 1 124 ? 46.739  -15.159 -27.868 1   54.92 ? 109 VAL   B CG2 1 
ATOM   3881 N  N   . PRO   B 1 125 ? 46.332  -12.814 -23.764 1   52.08 ? 110 PRO   B N   1 
ATOM   3882 C  CA  . PRO   B 1 125 ? 46.125  -12.683 -22.313 1   51.5  ? 110 PRO   B CA  1 
ATOM   3883 C  C   . PRO   B 1 125 ? 44.773  -12.053 -21.959 1   50.71 ? 110 PRO   B C   1 
ATOM   3884 O  O   . PRO   B 1 125 ? 44.235  -12.357 -20.907 1   50.52 ? 110 PRO   B O   1 
ATOM   3885 C  CB  . PRO   B 1 125 ? 47.303  -11.817 -21.841 1   52.1  ? 110 PRO   B CB  1 
ATOM   3886 C  CG  . PRO   B 1 125 ? 47.776  -11.114 -23.036 1   52.65 ? 110 PRO   B CG  1 
ATOM   3887 C  CD  . PRO   B 1 125 ? 47.475  -12.001 -24.221 1   51.27 ? 110 PRO   B CD  1 
ATOM   3888 N  N   . TYR   B 1 126 ? 44.226  -11.197 -22.837 1   50.06 ? 111 TYR   B N   1 
ATOM   3889 C  CA  . TYR   B 1 126 ? 42.929  -10.57  -22.603 1   49.47 ? 111 TYR   B CA  1 
ATOM   3890 C  C   . TYR   B 1 126 ? 41.85   -11.633 -22.627 1   49.71 ? 111 TYR   B C   1 
ATOM   3891 O  O   . TYR   B 1 126 ? 41.077  -11.714 -21.674 1   49.69 ? 111 TYR   B O   1 
ATOM   3892 C  CB  . TYR   B 1 126 ? 42.651  -9.466  -23.638 1   48.64 ? 111 TYR   B CB  1 
ATOM   3893 C  CG  . TYR   B 1 126 ? 41.446  -8.593  -23.343 1   48.04 ? 111 TYR   B CG  1 
ATOM   3894 C  CD1 . TYR   B 1 126 ? 40.97   -8.442  -22.045 1   48.1  ? 111 TYR   B CD1 1 
ATOM   3895 C  CD2 . TYR   B 1 126 ? 40.85   -7.842  -24.342 1   48.01 ? 111 TYR   B CD2 1 
ATOM   3896 C  CE1 . TYR   B 1 126 ? 39.886  -7.63   -21.768 1   48.5  ? 111 TYR   B CE1 1 
ATOM   3897 C  CE2 . TYR   B 1 126 ? 39.791  -6.992  -24.069 1   48.43 ? 111 TYR   B CE2 1 
ATOM   3898 C  CZ  . TYR   B 1 126 ? 39.299  -6.905  -22.783 1   48.92 ? 111 TYR   B CZ  1 
ATOM   3899 O  OH  . TYR   B 1 126 ? 38.26   -6.064  -22.494 1   48.89 ? 111 TYR   B OH  1 
ATOM   3900 N  N   . CYS   B 1 127 ? 41.812  -12.473 -23.676 1   49.82 ? 112 CYS   B N   1 
ATOM   3901 C  CA  . CYS   B 1 127 ? 40.814  -13.528 -23.76  1   50.6  ? 112 CYS   B CA  1 
ATOM   3902 C  C   . CYS   B 1 127 ? 40.963  -14.578 -22.672 1   50.74 ? 112 CYS   B C   1 
ATOM   3903 O  O   . CYS   B 1 127 ? 39.96   -15.096 -22.187 1   50.99 ? 112 CYS   B O   1 
ATOM   3904 C  CB  . CYS   B 1 127 ? 40.797  -14.165 -25.14  1   51.84 ? 112 CYS   B CB  1 
ATOM   3905 S  SG  . CYS   B 1 127 ? 40.314  -13.048 -26.477 1   57.19 ? 112 CYS   B SG  1 
ATOM   3906 N  N   . GLN   B 1 128 ? 42.198  -14.888 -22.28  1   50.72 ? 113 GLN   B N   1 
ATOM   3907 C  CA  . GLN   B 1 128 ? 42.446  -15.877 -21.232 1   51.07 ? 113 GLN   B CA  1 
ATOM   3908 C  C   . GLN   B 1 128 ? 41.921  -15.38  -19.883 1   50.65 ? 113 GLN   B C   1 
ATOM   3909 O  O   . GLN   B 1 128 ? 41.308  -16.14  -19.133 1   51.1  ? 113 GLN   B O   1 
ATOM   3910 C  CB  . GLN   B 1 128 ? 43.954  -16.152 -21.111 1   52.96 ? 113 GLN   B CB  1 
ATOM   3911 C  CG  . GLN   B 1 128 ? 44.537  -16.929 -22.275 1   57.04 ? 113 GLN   B CG  1 
ATOM   3912 C  CD  . GLN   B 1 128 ? 46.038  -17.015 -22.159 1   61.79 ? 113 GLN   B CD  1 
ATOM   3913 O  OE1 . GLN   B 1 128 ? 46.713  -16.106 -21.635 1   62.92 ? 113 GLN   B OE1 1 
ATOM   3914 N  NE2 . GLN   B 1 128 ? 46.592  -18.119 -22.647 1   62.78 ? 113 GLN   B NE2 1 
ATOM   3915 N  N   . LEU   B 1 129 ? 42.203  -14.116 -19.566 1   49.9  ? 114 LEU   B N   1 
ATOM   3916 C  CA  . LEU   B 1 129 ? 41.775  -13.48  -18.331 1   50.05 ? 114 LEU   B CA  1 
ATOM   3917 C  C   . LEU   B 1 129 ? 40.239  -13.336 -18.3   1   49.42 ? 114 LEU   B C   1 
ATOM   3918 O  O   . LEU   B 1 129 ? 39.624  -13.526 -17.255 1   49.46 ? 114 LEU   B O   1 
ATOM   3919 C  CB  . LEU   B 1 129 ? 42.445  -12.113 -18.235 1   50.36 ? 114 LEU   B CB  1 
ATOM   3920 C  CG  . LEU   B 1 129 ? 42.25   -11.356 -16.933 1   52.42 ? 114 LEU   B CG  1 
ATOM   3921 C  CD1 . LEU   B 1 129 ? 42.979  -12.042 -15.777 1   53.35 ? 114 LEU   B CD1 1 
ATOM   3922 C  CD2 . LEU   B 1 129 ? 42.736  -9.949  -17.081 1   52.83 ? 114 LEU   B CD2 1 
ATOM   3923 N  N   . SER   B 1 130 ? 39.637  -13.065 -19.458 1   48.76 ? 115 SER   B N   1 
ATOM   3924 C  CA  . SER   B 1 130 ? 38.206  -12.919 -19.628 1   48.76 ? 115 SER   B CA  1 
ATOM   3925 C  C   . SER   B 1 130 ? 37.505  -14.26  -19.412 1   49.86 ? 115 SER   B C   1 
ATOM   3926 O  O   . SER   B 1 130 ? 36.455  -14.3   -18.762 1   49.79 ? 115 SER   B O   1 
ATOM   3927 C  CB  . SER   B 1 130 ? 37.899  -12.337 -21.006 1   48.28 ? 115 SER   B CB  1 
ATOM   3928 O  OG  . SER   B 1 130 ? 38.366  -10.998 -21.093 1   48.25 ? 115 SER   B OG  1 
ATOM   3929 N  N   . LYS   B 1 131 ? 38.101  -15.362 -19.908 1   50.01 ? 116 LYS   B N   1 
ATOM   3930 C  CA  . LYS   B 1 131 ? 37.572  -16.707 -19.692 1   50.37 ? 116 LYS   B CA  1 
ATOM   3931 C  C   . LYS   B 1 131 ? 37.604  -17.042 -18.188 1   50.12 ? 116 LYS   B C   1 
ATOM   3932 O  O   . LYS   B 1 131 ? 36.617  -17.556 -17.65  1   50.63 ? 116 LYS   B O   1 
ATOM   3933 C  CB  . LYS   B 1 131 ? 38.385  -17.75  -20.473 1   53.22 ? 116 LYS   B CB  1 
ATOM   3934 C  CG  . LYS   B 1 131 ? 37.859  -19.172 -20.286 1   57.65 ? 116 LYS   B CG  1 
ATOM   3935 C  CD  . LYS   B 1 131 ? 38.857  -20.217 -20.75  1   62.45 ? 116 LYS   B CD  1 
ATOM   3936 N  N   . LYS   B 1 132 ? 38.701  -16.673 -17.513 1   49.16 ? 117 LYS   B N   1 
ATOM   3937 C  CA  . LYS   B 1 132 ? 38.915  -16.847 -16.081 1   49.51 ? 117 LYS   B CA  1 
ATOM   3938 C  C   . LYS   B 1 132 ? 37.863  -16.099 -15.236 1   49.53 ? 117 LYS   B C   1 
ATOM   3939 O  O   . LYS   B 1 132 ? 37.348  -16.661 -14.27  1   49.28 ? 117 LYS   B O   1 
ATOM   3940 C  CB  . LYS   B 1 132 ? 40.326  -16.372 -15.696 1   51.38 ? 117 LYS   B CB  1 
ATOM   3941 C  CG  . LYS   B 1 132 ? 40.706  -16.675 -14.249 1   56.38 ? 117 LYS   B CG  1 
ATOM   3942 C  CD  . LYS   B 1 132 ? 42.17   -16.359 -13.942 1   60.88 ? 117 LYS   B CD  1 
ATOM   3943 N  N   . LEU   B 1 133 ? 37.558  -14.832 -15.584 1   49.15 ? 118 LEU   B N   1 
ATOM   3944 C  CA  . LEU   B 1 133 ? 36.566  -14.068 -14.826 1   48.4  ? 118 LEU   B CA  1 
ATOM   3945 C  C   . LEU   B 1 133 ? 35.13   -14.231 -15.341 1   47.9  ? 118 LEU   B C   1 
ATOM   3946 O  O   . LEU   B 1 133 ? 34.226  -13.578 -14.797 1   47.64 ? 118 LEU   B O   1 
ATOM   3947 C  CB  . LEU   B 1 133 ? 36.933  -12.585 -14.78  1   48.61 ? 118 LEU   B CB  1 
ATOM   3948 C  CG  . LEU   B 1 133 ? 38.157  -12.221 -13.967 1   50.19 ? 118 LEU   B CG  1 
ATOM   3949 C  CD1 . LEU   B 1 133 ? 38.512  -10.782 -14.167 1   50.7  ? 118 LEU   B CD1 1 
ATOM   3950 C  CD2 . LEU   B 1 133 ? 37.937  -12.48  -12.488 1   50.93 ? 118 LEU   B CD2 1 
ATOM   3951 N  N   . GLU   B 1 134 ? 34.92   -15.086 -16.376 1   47.31 ? 119 GLU   B N   1 
ATOM   3952 C  CA  . GLU   B 1 134 ? 33.642  -15.359 -17.024 1   47.5  ? 119 GLU   B CA  1 
ATOM   3953 C  C   . GLU   B 1 134 ? 33.007  -14.074 -17.536 1   47.78 ? 119 GLU   B C   1 
ATOM   3954 O  O   . GLU   B 1 134 ? 31.812  -13.831 -17.337 1   48.86 ? 119 GLU   B O   1 
ATOM   3955 C  CB  . GLU   B 1 134 ? 32.678  -16.121 -16.11  1   50.17 ? 119 GLU   B CB  1 
ATOM   3956 C  CG  . GLU   B 1 134 ? 33.155  -17.503 -15.707 1   54.69 ? 119 GLU   B CG  1 
ATOM   3957 C  CD  . GLU   B 1 134 ? 32.121  -18.184 -14.839 1   60.36 ? 119 GLU   B CD  1 
ATOM   3958 O  OE1 . GLU   B 1 134 ? 31.007  -18.447 -15.348 1   61.68 ? 119 GLU   B OE1 1 
ATOM   3959 O  OE2 . GLU   B 1 134 ? 32.403  -18.406 -13.639 1   62.67 ? 119 GLU   B OE2 1 
ATOM   3960 N  N   . LEU   B 1 135 ? 33.822  -13.235 -18.172 1   46.12 ? 120 LEU   B N   1 
ATOM   3961 C  CA  . LEU   B 1 135 ? 33.392  -11.976 -18.761 1   45.32 ? 120 LEU   B CA  1 
ATOM   3962 C  C   . LEU   B 1 135 ? 33.875  -11.953 -20.21  1   46.15 ? 120 LEU   B C   1 
ATOM   3963 O  O   . LEU   B 1 135 ? 34.926  -12.531 -20.521 1   46.71 ? 120 LEU   B O   1 
ATOM   3964 C  CB  . LEU   B 1 135 ? 33.999  -10.806 -17.972 1   44.19 ? 120 LEU   B CB  1 
ATOM   3965 C  CG  . LEU   B 1 135 ? 33.315  -10.499 -16.644 1   44.27 ? 120 LEU   B CG  1 
ATOM   3966 C  CD1 . LEU   B 1 135 ? 34.107  -9.486  -15.833 1   43.49 ? 120 LEU   B CD1 1 
ATOM   3967 C  CD2 . LEU   B 1 135 ? 31.881  -10.021 -16.876 1   44.44 ? 120 LEU   B CD2 1 
ATOM   3968 N  N   . PRO   B 1 136 ? 33.137  -11.311 -21.123 1   45.42 ? 121 PRO   B N   1 
ATOM   3969 C  CA  . PRO   B 1 136 ? 33.598  -11.261 -22.529 1   45.06 ? 121 PRO   B CA  1 
ATOM   3970 C  C   . PRO   B 1 136 ? 34.839  -10.382 -22.701 1   44.55 ? 121 PRO   B C   1 
ATOM   3971 O  O   . PRO   B 1 136 ? 35.083  -9.497  -21.881 1   45.55 ? 121 PRO   B O   1 
ATOM   3972 C  CB  . PRO   B 1 136 ? 32.38   -10.694 -23.278 1   45.64 ? 121 PRO   B CB  1 
ATOM   3973 C  CG  . PRO   B 1 136 ? 31.674  -9.892  -22.25  1   46.12 ? 121 PRO   B CG  1 
ATOM   3974 C  CD  . PRO   B 1 136 ? 31.87   -10.582 -20.931 1   44.44 ? 121 PRO   B CD  1 
ATOM   3975 N  N   . PRO   B 1 137 ? 35.658  -10.617 -23.752 1   43.55 ? 122 PRO   B N   1 
ATOM   3976 C  CA  . PRO   B 1 137 ? 36.863  -9.789  -23.949 1   42.63 ? 122 PRO   B CA  1 
ATOM   3977 C  C   . PRO   B 1 137 ? 36.599  -8.399  -24.568 1   40.93 ? 122 PRO   B C   1 
ATOM   3978 O  O   . PRO   B 1 137 ? 37.065  -8.071  -25.678 1   41.09 ? 122 PRO   B O   1 
ATOM   3979 C  CB  . PRO   B 1 137 ? 37.732  -10.662 -24.857 1   43.26 ? 122 PRO   B CB  1 
ATOM   3980 C  CG  . PRO   B 1 137 ? 36.752  -11.396 -25.697 1   43.86 ? 122 PRO   B CG  1 
ATOM   3981 C  CD  . PRO   B 1 137 ? 35.546  -11.66  -24.796 1   42.78 ? 122 PRO   B CD  1 
ATOM   3982 N  N   . ILE   B 1 138 ? 35.869  -7.576  -23.83  1   38.52 ? 123 ILE   B N   1 
ATOM   3983 C  CA  . ILE   B 1 138 ? 35.528  -6.198  -24.197 1   37.61 ? 123 ILE   B CA  1 
ATOM   3984 C  C   . ILE   B 1 138 ? 35.272  -5.475  -22.86  1   36.45 ? 123 ILE   B C   1 
ATOM   3985 O  O   . ILE   B 1 138 ? 34.904  -6.113  -21.869 1   35.94 ? 123 ILE   B O   1 
ATOM   3986 C  CB  . ILE   B 1 138 ? 34.322  -6.115  -25.183 1   37.95 ? 123 ILE   B CB  1 
ATOM   3987 C  CG1 . ILE   B 1 138 ? 34.136  -4.662  -25.742 1   38.62 ? 123 ILE   B CG1 1 
ATOM   3988 C  CG2 . ILE   B 1 138 ? 33.036  -6.628  -24.534 1   38.44 ? 123 ILE   B CG2 1 
ATOM   3989 C  CD1 . ILE   B 1 138 ? 33.195  -4.534  -26.958 1   38.55 ? 123 ILE   B CD1 1 
ATOM   3990 N  N   . LEU   B 1 139 ? 35.54   -4.17   -22.798 1   35.36 ? 124 LEU   B N   1 
ATOM   3991 C  CA  . LEU   B 1 139 ? 35.277  -3.37   -21.598 1   35.48 ? 124 LEU   B CA  1 
ATOM   3992 C  C   . LEU   B 1 139 ? 33.769  -3.449  -21.264 1   33.45 ? 124 LEU   B C   1 
ATOM   3993 O  O   . LEU   B 1 139 ? 32.923  -3.285  -22.151 1   32.68 ? 124 LEU   B O   1 
ATOM   3994 C  CB  . LEU   B 1 139 ? 35.616  -1.909  -21.935 1   36.14 ? 124 LEU   B CB  1 
ATOM   3995 C  CG  . LEU   B 1 139 ? 36.385  -1.012  -20.978 1   38.06 ? 124 LEU   B CG  1 
ATOM   3996 C  CD1 . LEU   B 1 139 ? 37.441  -1.745  -20.149 1   38.19 ? 124 LEU   B CD1 1 
ATOM   3997 C  CD2 . LEU   B 1 139 ? 36.875  0.224   -21.703 1   38.77 ? 124 LEU   B CD2 1 
ATOM   3998 N  N   . VAL   B 1 140 ? 33.457  -3.804  -20.021 1   32.82 ? 125 VAL   B N   1 
ATOM   3999 C  CA  . VAL   B 1 140 ? 32.073  -3.869  -19.548 1   32.02 ? 125 VAL   B CA  1 
ATOM   4000 C  C   . VAL   B 1 140 ? 31.891  -2.8    -18.445 1   31.31 ? 125 VAL   B C   1 
ATOM   4001 O  O   . VAL   B 1 140 ? 32.866  -2.236  -17.961 1   31.68 ? 125 VAL   B O   1 
ATOM   4002 C  CB  . VAL   B 1 140 ? 31.678  -5.3    -19.054 1   31.66 ? 125 VAL   B CB  1 
ATOM   4003 C  CG1 . VAL   B 1 140 ? 31.759  -6.329  -20.183 1   31.74 ? 125 VAL   B CG1 1 
ATOM   4004 C  CG2 . VAL   B 1 140 ? 32.512  -5.726  -17.845 1   31.67 ? 125 VAL   B CG2 1 
ATOM   4005 N  N   . TYR   B 1 141 ? 30.648  -2.539  -18.042 1   30.38 ? 126 TYR   B N   1 
ATOM   4006 C  CA  . TYR   B 1 141 ? 30.278  -1.644  -16.948 1   30.43 ? 126 TYR   B CA  1 
ATOM   4007 C  C   . TYR   B 1 141 ? 31.053  -1.99   -15.665 1   30.86 ? 126 TYR   B C   1 
ATOM   4008 O  O   . TYR   B 1 141 ? 31.568  -1.096  -14.987 1   31.15 ? 126 TYR   B O   1 
ATOM   4009 C  CB  . TYR   B 1 141 ? 28.751  -1.772  -16.735 1   30.28 ? 126 TYR   B CB  1 
ATOM   4010 C  CG  . TYR   B 1 141 ? 28.148  -0.858  -15.687 1   31.58 ? 126 TYR   B CG  1 
ATOM   4011 C  CD1 . TYR   B 1 141 ? 27.767  0.442   -16.004 1   32.95 ? 126 TYR   B CD1 1 
ATOM   4012 C  CD2 . TYR   B 1 141 ? 27.876  -1.321  -14.406 1   32.21 ? 126 TYR   B CD2 1 
ATOM   4013 C  CE1 . TYR   B 1 141 ? 27.172  1.269   -15.061 1   33.95 ? 126 TYR   B CE1 1 
ATOM   4014 C  CE2 . TYR   B 1 141 ? 27.277  -0.504  -13.455 1   32.88 ? 126 TYR   B CE2 1 
ATOM   4015 C  CZ  . TYR   B 1 141 ? 26.911  0.784   -13.792 1   34.23 ? 126 TYR   B CZ  1 
ATOM   4016 O  OH  . TYR   B 1 141 ? 26.298  1.596   -12.873 1   35.79 ? 126 TYR   B OH  1 
ATOM   4017 N  N   . ALA   B 1 142 ? 31.22   -3.295  -15.375 1   31.27 ? 127 ALA   B N   1 
ATOM   4018 C  CA  . ALA   B 1 142 ? 31.97   -3.751  -14.189 1   32.18 ? 127 ALA   B CA  1 
ATOM   4019 C  C   . ALA   B 1 142 ? 33.459  -3.399  -14.232 1   33.82 ? 127 ALA   B C   1 
ATOM   4020 O  O   . ALA   B 1 142 ? 34.109  -3.347  -13.173 1   34.27 ? 127 ALA   B O   1 
ATOM   4021 C  CB  . ALA   B 1 142 ? 31.779  -5.245  -13.954 1   31.37 ? 127 ALA   B CB  1 
ATOM   4022 N  N   . ASP   B 1 143 ? 34.012  -3.16   -15.434 1   33.78 ? 128 ASP   B N   1 
ATOM   4023 C  CA  . ASP   B 1 143 ? 35.412  -2.738  -15.519 1   34.28 ? 128 ASP   B CA  1 
ATOM   4024 C  C   . ASP   B 1 143 ? 35.493  -1.217  -15.342 1   35.01 ? 128 ASP   B C   1 
ATOM   4025 O  O   . ASP   B 1 143 ? 36.069  -0.717  -14.386 1   35.41 ? 128 ASP   B O   1 
ATOM   4026 C  CB  . ASP   B 1 143 ? 36.061  -3.114  -16.882 1   34.28 ? 128 ASP   B CB  1 
ATOM   4027 C  CG  . ASP   B 1 143 ? 35.995  -4.56   -17.27  1   35.6  ? 128 ASP   B CG  1 
ATOM   4028 O  OD1 . ASP   B 1 143 ? 36.306  -5.409  -16.421 1   36.74 ? 128 ASP   B OD1 1 
ATOM   4029 O  OD2 . ASP   B 1 143 ? 35.664  -4.844  -18.444 1   34.69 ? 128 ASP   B OD2 1 
ATOM   4030 N  N   . CYS   B 1 144 ? 34.896  -0.504  -16.282 1   35.54 ? 129 CYS   B N   1 
ATOM   4031 C  CA  . CYS   B 1 144 ? 35.01   0.919   -16.472 1   36.65 ? 129 CYS   B CA  1 
ATOM   4032 C  C   . CYS   B 1 144 ? 34.271  1.782   -15.457 1   36.5  ? 129 CYS   B C   1 
ATOM   4033 O  O   . CYS   B 1 144 ? 34.633  2.946   -15.266 1   36.58 ? 129 CYS   B O   1 
ATOM   4034 C  CB  . CYS   B 1 144 ? 34.595  1.242   -17.903 1   38.4  ? 129 CYS   B CB  1 
ATOM   4035 S  SG  . CYS   B 1 144 ? 35.621  2.489   -18.685 1   44.08 ? 129 CYS   B SG  1 
ATOM   4036 N  N   . VAL   B 1 145 ? 33.25   1.227   -14.799 1   36.23 ? 130 VAL   B N   1 
ATOM   4037 C  CA  . VAL   B 1 145 ? 32.531  1.959   -13.767 1   36.06 ? 130 VAL   B CA  1 
ATOM   4038 C  C   . VAL   B 1 145 ? 32.809  1.35    -12.372 1   36.9  ? 130 VAL   B C   1 
ATOM   4039 O  O   . VAL   B 1 145 ? 33.345  2.028   -11.495 1   38.11 ? 130 VAL   B O   1 
ATOM   4040 C  CB  . VAL   B 1 145 ? 31.018  2.094   -14.07  1   35.42 ? 130 VAL   B CB  1 
ATOM   4041 C  CG1 . VAL   B 1 145 ? 30.271  2.74    -12.899 1   36.17 ? 130 VAL   B CG1 1 
ATOM   4042 C  CG2 . VAL   B 1 145 ? 30.795  2.879   -15.366 1   34.79 ? 130 VAL   B CG2 1 
ATOM   4043 N  N   . LEU   B 1 146 ? 32.532  0.059   -12.206 1   35.57 ? 131 LEU   B N   1 
ATOM   4044 C  CA  . LEU   B 1 146 ? 32.625  -0.606  -10.918 1   35.06 ? 131 LEU   B CA  1 
ATOM   4045 C  C   . LEU   B 1 146 ? 34.044  -0.818  -10.358 1   35.54 ? 131 LEU   B C   1 
ATOM   4046 O  O   . LEU   B 1 146 ? 34.207  -0.883  -9.139  1   35.53 ? 131 LEU   B O   1 
ATOM   4047 C  CB  . LEU   B 1 146 ? 31.867  -1.944  -10.986 1   34.15 ? 131 LEU   B CB  1 
ATOM   4048 C  CG  . LEU   B 1 146 ? 30.381  -1.869  -11.39  1   34.85 ? 131 LEU   B CG  1 
ATOM   4049 C  CD1 . LEU   B 1 146 ? 29.727  -3.235  -11.271 1   35.23 ? 131 LEU   B CD1 1 
ATOM   4050 C  CD2 . LEU   B 1 146 ? 29.609  -0.832  -10.589 1   35.41 ? 131 LEU   B CD2 1 
ATOM   4051 N  N   . ALA   B 1 147 ? 35.049  -0.958  -11.218 1   35.43 ? 132 ALA   B N   1 
ATOM   4052 C  CA  . ALA   B 1 147 ? 36.424  -1.177  -10.762 1   35.75 ? 132 ALA   B CA  1 
ATOM   4053 C  C   . ALA   B 1 147 ? 37.392  -0.045  -11.137 1   36.85 ? 132 ALA   B C   1 
ATOM   4054 O  O   . ALA   B 1 147 ? 38.579  -0.155  -10.843 1   37.81 ? 132 ALA   B O   1 
ATOM   4055 C  CB  . ALA   B 1 147 ? 36.94   -2.488  -11.315 1   35.83 ? 132 ALA   B CB  1 
ATOM   4056 N  N   . ASN   B 1 148 ? 36.915  1.007   -11.814 1   36.56 ? 133 ASN   B N   1 
ATOM   4057 C  CA  . ASN   B 1 148 ? 37.765  2.106   -12.306 1   37.03 ? 133 ASN   B CA  1 
ATOM   4058 C  C   . ASN   B 1 148 ? 37.723  3.33    -11.398 1   38.09 ? 133 ASN   B C   1 
ATOM   4059 O  O   . ASN   B 1 148 ? 37.398  4.447   -11.845 1   37.97 ? 133 ASN   B O   1 
ATOM   4060 C  CB  . ASN   B 1 148 ? 37.299  2.473   -13.73  1   37.54 ? 133 ASN   B CB  1 
ATOM   4061 C  CG  . ASN   B 1 148 ? 38.186  3.435   -14.485 1   37.38 ? 133 ASN   B CG  1 
ATOM   4062 O  OD1 . ASN   B 1 148 ? 39.357  3.631   -14.145 1   37.16 ? 133 ASN   B OD1 1 
ATOM   4063 N  ND2 . ASN   B 1 148 ? 37.644  4.04    -15.532 1   36.93 ? 133 ASN   B ND2 1 
ATOM   4064 N  N   . TRP   B 1 149 ? 38.025  3.124   -10.11  1   38.91 ? 134 TRP   B N   1 
ATOM   4065 C  CA  . TRP   B 1 149 ? 37.908  4.218   -9.161  1   40.39 ? 134 TRP   B CA  1 
ATOM   4066 C  C   . TRP   B 1 149 ? 38.808  4.083   -7.935  1   41.3  ? 134 TRP   B C   1 
ATOM   4067 O  O   . TRP   B 1 149 ? 39.312  3.005   -7.642  1   39.7  ? 134 TRP   B O   1 
ATOM   4068 C  CB  . TRP   B 1 149 ? 36.433  4.396   -8.758  1   40.61 ? 134 TRP   B CB  1 
ATOM   4069 C  CG  . TRP   B 1 149 ? 35.879  3.266   -7.942  1   42.25 ? 134 TRP   B CG  1 
ATOM   4070 C  CD1 . TRP   B 1 149 ? 35.338  2.099   -8.401  1   43.41 ? 134 TRP   B CD1 1 
ATOM   4071 C  CD2 . TRP   B 1 149 ? 35.833  3.195   -6.512  1   43.08 ? 134 TRP   B CD2 1 
ATOM   4072 N  NE1 . TRP   B 1 149 ? 34.938  1.313   -7.343  1   43.84 ? 134 TRP   B NE1 1 
ATOM   4073 C  CE2 . TRP   B 1 149 ? 35.215  1.972   -6.171  1   44.13 ? 134 TRP   B CE2 1 
ATOM   4074 C  CE3 . TRP   B 1 149 ? 36.225  4.065   -5.484  1   43.8  ? 134 TRP   B CE3 1 
ATOM   4075 C  CZ2 . TRP   B 1 149 ? 35.008  1.588   -4.843  1   45.14 ? 134 TRP   B CZ2 1 
ATOM   4076 C  CZ3 . TRP   B 1 149 ? 36.038  3.673   -4.173  1   45.16 ? 134 TRP   B CZ3 1 
ATOM   4077 C  CH2 . TRP   B 1 149 ? 35.426  2.454   -3.863  1   45.34 ? 134 TRP   B CH2 1 
ATOM   4078 N  N   . LYS   B 1 150 ? 39.021  5.212   -7.241  1   43.71 ? 135 LYS   B N   1 
ATOM   4079 C  CA  . LYS   B 1 150 ? 39.815  5.267   -6.012  1   46.52 ? 135 LYS   B CA  1 
ATOM   4080 C  C   . LYS   B 1 150 ? 39.36   6.428   -5.156  1   49.52 ? 135 LYS   B C   1 
ATOM   4081 O  O   . LYS   B 1 150 ? 38.778  7.387   -5.653  1   49.96 ? 135 LYS   B O   1 
ATOM   4082 C  CB  . LYS   B 1 150 ? 41.322  5.417   -6.323  1   47.78 ? 135 LYS   B CB  1 
ATOM   4083 C  CG  . LYS   B 1 150 ? 41.671  6.744   -7.004  1   51.73 ? 135 LYS   B CG  1 
ATOM   4084 C  CD  . LYS   B 1 150 ? 43.175  6.895   -7.228  1   56.43 ? 135 LYS   B CD  1 
ATOM   4085 C  CE  . LYS   B 1 150 ? 43.91   7.226   -5.941  1   61.24 ? 135 LYS   B CE  1 
ATOM   4086 N  NZ  . LYS   B 1 150 ? 45.391  7.244   -6.119  1   63.89 ? 135 LYS   B NZ  1 
ATOM   4087 N  N   . LYS   B 1 151 ? 39.634  6.351   -3.861  1   51.71 ? 136 LYS   B N   1 
ATOM   4088 C  CA  . LYS   B 1 151 ? 39.405  7.469   -2.954  1   53.73 ? 136 LYS   B CA  1 
ATOM   4089 C  C   . LYS   B 1 151 ? 40.71   8.28    -2.979  1   55.48 ? 136 LYS   B C   1 
ATOM   4090 O  O   . LYS   B 1 151 ? 41.797  7.703   -3.009  1   55.66 ? 136 LYS   B O   1 
ATOM   4091 C  CB  . LYS   B 1 151 ? 39.204  6.972   -1.515  1   55.9  ? 136 LYS   B CB  1 
ATOM   4092 C  CG  . LYS   B 1 151 ? 37.767  6.683   -1.118  1   60.5  ? 136 LYS   B CG  1 
ATOM   4093 C  CD  . LYS   B 1 151 ? 37.695  6.247   0.349   1   65.64 ? 136 LYS   B CD  1 
ATOM   4094 C  CE  . LYS   B 1 151 ? 36.273  6.084   0.836   1   69.69 ? 136 LYS   B CE  1 
ATOM   4095 N  NZ  . LYS   B 1 151 ? 36.193  6.037   2.323   1   71.8  ? 136 LYS   B NZ  1 
ATOM   4096 N  N   . LYS   B 1 152 ? 40.611  9.607   -2.968  1   56.74 ? 137 LYS   B N   1 
ATOM   4097 C  CA  . LYS   B 1 152 ? 41.783  10.481  -2.894  1   58.44 ? 137 LYS   B CA  1 
ATOM   4098 C  C   . LYS   B 1 152 ? 42.335  10.382  -1.458  1   60.7  ? 137 LYS   B C   1 
ATOM   4099 O  O   . LYS   B 1 152 ? 43.524  10.147  -1.265  1   61.27 ? 137 LYS   B O   1 
ATOM   4100 C  CB  . LYS   B 1 152 ? 41.389  11.934  -3.209  1   58.96 ? 137 LYS   B CB  1 
ATOM   4101 C  CG  . LYS   B 1 152 ? 41.03   12.16   -4.659  1   61.41 ? 137 LYS   B CG  1 
ATOM   4102 C  CD  . LYS   B 1 152 ? 40.558  13.577  -4.872  1   64.47 ? 137 LYS   B CD  1 
ATOM   4103 C  CE  . LYS   B 1 152 ? 40.274  13.846  -6.321  1   67.8  ? 137 LYS   B CE  1 
ATOM   4104 N  NZ  . LYS   B 1 152 ? 39.832  15.241  -6.528  1   70.1  ? 137 LYS   B NZ  1 
ATOM   4105 N  N   . ASP   B 1 153 ? 41.444  10.485  -0.463  1   61.84 ? 138 ASP   B N   1 
ATOM   4106 C  CA  . ASP   B 1 153 ? 41.769  10.38   0.947   1   63.69 ? 138 ASP   B CA  1 
ATOM   4107 C  C   . ASP   B 1 153 ? 40.983  9.205   1.515   1   65.26 ? 138 ASP   B C   1 
ATOM   4108 O  O   . ASP   B 1 153 ? 39.765  9.285   1.648   1   65.44 ? 138 ASP   B O   1 
ATOM   4109 C  CB  . ASP   B 1 153 ? 41.36   11.685  1.662   1   65.88 ? 138 ASP   B CB  1 
ATOM   4110 C  CG  . ASP   B 1 153 ? 41.686  11.766  3.145   1   70.95 ? 138 ASP   B CG  1 
ATOM   4111 O  OD1 . ASP   B 1 153 ? 42.239  10.777  3.692   1   71.18 ? 138 ASP   B OD1 1 
ATOM   4112 O  OD2 . ASP   B 1 153 ? 41.382  12.818  3.761   1   73.36 ? 138 ASP   B OD2 1 
ATOM   4113 N  N   . PRO   B 1 154 ? 41.669  8.123   1.904   1   66.57 ? 139 PRO   B N   1 
ATOM   4114 C  CA  . PRO   B 1 154 ? 40.96   6.965   2.485   1   67.36 ? 139 PRO   B CA  1 
ATOM   4115 C  C   . PRO   B 1 154 ? 40.169  7.27    3.759   1   68.32 ? 139 PRO   B C   1 
ATOM   4116 O  O   . PRO   B 1 154 ? 39.278  6.501   4.122   1   68.96 ? 139 PRO   B O   1 
ATOM   4117 C  CB  . PRO   B 1 154 ? 42.081  5.956   2.766   1   67.91 ? 139 PRO   B CB  1 
ATOM   4118 C  CG  . PRO   B 1 154 ? 43.22   6.381   1.892   1   68.32 ? 139 PRO   B CG  1 
ATOM   4119 C  CD  . PRO   B 1 154 ? 43.12   7.88    1.808   1   66.57 ? 139 PRO   B CD  1 
ATOM   4120 N  N   . ASN   B 1 155 ? 40.474  8.382   4.433   1   68.25 ? 140 ASN   B N   1 
ATOM   4121 C  CA  . ASN   B 1 155 ? 39.756  8.754   5.652   1   68.76 ? 140 ASN   B CA  1 
ATOM   4122 C  C   . ASN   B 1 155 ? 38.496  9.596   5.396   1   68.36 ? 140 ASN   B C   1 
ATOM   4123 O  O   . ASN   B 1 155 ? 37.747  9.864   6.334   1   68.79 ? 140 ASN   B O   1 
ATOM   4124 C  CB  . ASN   B 1 155 ? 40.692  9.441   6.647   1   70.67 ? 140 ASN   B CB  1 
ATOM   4125 C  CG  . ASN   B 1 155 ? 41.944  8.642   6.906   1   74.63 ? 140 ASN   B CG  1 
ATOM   4126 O  OD1 . ASN   B 1 155 ? 41.893  7.429   7.155   1   76.2  ? 140 ASN   B OD1 1 
ATOM   4127 N  ND2 . ASN   B 1 155 ? 43.097  9.299   6.824   1   75.39 ? 140 ASN   B ND2 1 
ATOM   4128 N  N   . LYS   B 1 156 ? 38.246  10.001  4.138   1   67.13 ? 141 LYS   B N   1 
ATOM   4129 C  CA  . LYS   B 1 156 ? 37.059  10.78   3.799   1   66.31 ? 141 LYS   B CA  1 
ATOM   4130 C  C   . LYS   B 1 156 ? 36.001  9.896   3.095   1   65.13 ? 141 LYS   B C   1 
ATOM   4131 O  O   . LYS   B 1 156 ? 36.347  8.862   2.521   1   65.33 ? 141 LYS   B O   1 
ATOM   4132 C  CB  . LYS   B 1 156 ? 37.451  12.011  2.964   1   68.2  ? 141 LYS   B CB  1 
ATOM   4133 N  N   . PRO   B 1 157 ? 34.703  10.258  3.157   1   63.58 ? 142 PRO   B N   1 
ATOM   4134 C  CA  . PRO   B 1 157 ? 33.669  9.396   2.56    1   62.71 ? 142 PRO   B CA  1 
ATOM   4135 C  C   . PRO   B 1 157 ? 33.663  9.295   1.02    1   61.27 ? 142 PRO   B C   1 
ATOM   4136 O  O   . PRO   B 1 157 ? 34.442  9.96    0.334   1   61.3  ? 142 PRO   B O   1 
ATOM   4137 C  CB  . PRO   B 1 157 ? 32.365  10.007  3.097   1   63.67 ? 142 PRO   B CB  1 
ATOM   4138 C  CG  . PRO   B 1 157 ? 32.694  11.435  3.33    1   64.3  ? 142 PRO   B CG  1 
ATOM   4139 C  CD  . PRO   B 1 157 ? 34.105  11.425  3.834   1   62.84 ? 142 PRO   B CD  1 
ATOM   4140 N  N   . LEU   B 1 158 ? 32.77   8.449   0.477   1   59.55 ? 143 LEU   B N   1 
ATOM   4141 C  CA  . LEU   B 1 158 ? 32.621  8.264   -0.955  1   58.19 ? 143 LEU   B CA  1 
ATOM   4142 C  C   . LEU   B 1 158 ? 31.79   9.365   -1.563  1   56.92 ? 143 LEU   B C   1 
ATOM   4143 O  O   . LEU   B 1 158 ? 30.576  9.235   -1.734  1   56.74 ? 143 LEU   B O   1 
ATOM   4144 C  CB  . LEU   B 1 158 ? 32.009  6.907   -1.262  1   58.28 ? 143 LEU   B CB  1 
ATOM   4145 C  CG  . LEU   B 1 158 ? 32.96   5.738   -1.09   1   59.7  ? 143 LEU   B CG  1 
ATOM   4146 C  CD1 . LEU   B 1 158 ? 32.217  4.432   -1.15   1   60.88 ? 143 LEU   B CD1 1 
ATOM   4147 C  CD2 . LEU   B 1 158 ? 34.04   5.77    -2.122  1   59.8  ? 143 LEU   B CD2 1 
ATOM   4148 N  N   . THR   B 1 159 ? 32.46   10.462  -1.886  1   55.89 ? 144 THR   B N   1 
ATOM   4149 C  CA  . THR   B 1 159 ? 31.87   11.648  -2.508  1   55.24 ? 144 THR   B CA  1 
ATOM   4150 C  C   . THR   B 1 159 ? 32.658  11.955  -3.769  1   53.41 ? 144 THR   B C   1 
ATOM   4151 O  O   . THR   B 1 159 ? 33.83   11.595  -3.866  1   53.21 ? 144 THR   B O   1 
ATOM   4152 C  CB  . THR   B 1 159 ? 31.843  12.836  -1.505  1   57.62 ? 144 THR   B CB  1 
ATOM   4153 O  OG1 . THR   B 1 159 ? 31.547  14.054  -2.182  1   59.93 ? 144 THR   B OG1 1 
ATOM   4154 C  CG2 . THR   B 1 159 ? 33.149  12.991  -0.732  1   58.19 ? 144 THR   B CG2 1 
ATOM   4155 N  N   . TYR   B 1 160 ? 32.053  12.674  -4.721  1   52.39 ? 145 TYR   B N   1 
ATOM   4156 C  CA  . TYR   B 1 160 ? 32.734  13.025  -5.974  1   51.92 ? 145 TYR   B CA  1 
ATOM   4157 C  C   . TYR   B 1 160 ? 34.062  13.747  -5.728  1   51.78 ? 145 TYR   B C   1 
ATOM   4158 O  O   . TYR   B 1 160 ? 35.078  13.402  -6.335  1   51.24 ? 145 TYR   B O   1 
ATOM   4159 C  CB  . TYR   B 1 160 ? 31.824  13.882  -6.862  1   51.7  ? 145 TYR   B CB  1 
ATOM   4160 C  CG  . TYR   B 1 160 ? 32.379  14.064  -8.254  1   51.87 ? 145 TYR   B CG  1 
ATOM   4161 C  CD1 . TYR   B 1 160 ? 32.061  13.178  -9.269  1   52.12 ? 145 TYR   B CD1 1 
ATOM   4162 C  CD2 . TYR   B 1 160 ? 33.226  15.126  -8.555  1   52.55 ? 145 TYR   B CD2 1 
ATOM   4163 C  CE1 . TYR   B 1 160 ? 32.572  13.336  -10.546 1   52.47 ? 145 TYR   B CE1 1 
ATOM   4164 C  CE2 . TYR   B 1 160 ? 33.788  15.261  -9.813  1   52.97 ? 145 TYR   B CE2 1 
ATOM   4165 C  CZ  . TYR   B 1 160 ? 33.433  14.383  -10.816 1   53.25 ? 145 TYR   B CZ  1 
ATOM   4166 O  OH  . TYR   B 1 160 ? 33.957  14.54   -12.071 1   53.57 ? 145 TYR   B OH  1 
ATOM   4167 N  N   . GLU   B 1 161 ? 34.055  14.695  -4.776  1   51.88 ? 146 GLU   B N   1 
ATOM   4168 C  CA  . GLU   B 1 161 ? 35.233  15.476  -4.412  1   52.1  ? 146 GLU   B CA  1 
ATOM   4169 C  C   . GLU   B 1 161 ? 36.37   14.612  -3.885  1   52.14 ? 146 GLU   B C   1 
ATOM   4170 O  O   . GLU   B 1 161 ? 37.537  14.935  -4.103  1   52.63 ? 146 GLU   B O   1 
ATOM   4171 C  CB  . GLU   B 1 161 ? 34.861  16.576  -3.406  1   54.23 ? 146 GLU   B CB  1 
ATOM   4172 N  N   . ASN   B 1 162 ? 36.042  13.508  -3.221  1   51.3  ? 147 ASN   B N   1 
ATOM   4173 C  CA  . ASN   B 1 162 ? 37.061  12.618  -2.676  1   51.2  ? 147 ASN   B CA  1 
ATOM   4174 C  C   . ASN   B 1 162 ? 37.355  11.408  -3.589  1   50.69 ? 147 ASN   B C   1 
ATOM   4175 O  O   . ASN   B 1 162 ? 37.956  10.439  -3.132  1   50.72 ? 147 ASN   B O   1 
ATOM   4176 C  CB  . ASN   B 1 162 ? 36.643  12.141  -1.278  1   51.82 ? 147 ASN   B CB  1 
ATOM   4177 C  CG  . ASN   B 1 162 ? 37.749  11.436  -0.568  1   53.85 ? 147 ASN   B CG  1 
ATOM   4178 O  OD1 . ASN   B 1 162 ? 38.897  11.857  -0.632  1   55.87 ? 147 ASN   B OD1 1 
ATOM   4179 N  ND2 . ASN   B 1 162 ? 37.454  10.305  0.044   1   53.62 ? 147 ASN   B ND2 1 
ATOM   4180 N  N   . MET   B 1 163 ? 36.949  11.452  -4.867  1   49.98 ? 148 MET   B N   1 
ATOM   4181 C  CA  . MET   B 1 163 ? 37.155  10.304  -5.744  1   49.4  ? 148 MET   B CA  1 
ATOM   4182 C  C   . MET   B 1 163 ? 37.803  10.66   -7.062  1   49.09 ? 148 MET   B C   1 
ATOM   4183 O  O   . MET   B 1 163 ? 37.751  11.807  -7.504  1   49.54 ? 148 MET   B O   1 
ATOM   4184 C  CB  . MET   B 1 163 ? 35.818  9.574   -5.979  1   49.39 ? 148 MET   B CB  1 
ATOM   4185 C  CG  . MET   B 1 163 ? 35.221  8.976   -4.726  1   51.4  ? 148 MET   B CG  1 
ATOM   4186 S  SD  . MET   B 1 163 ? 33.482  8.565   -4.942  1   53.36 ? 148 MET   B SD  1 
ATOM   4187 C  CE  . MET   B 1 163 ? 33.661  7.015   -5.734  1   50.35 ? 148 MET   B CE  1 
ATOM   4188 N  N   . ASP   B 1 164 ? 38.373  9.652   -7.709  1   48.03 ? 149 ASP   B N   1 
ATOM   4189 C  CA  . ASP   B 1 164 ? 38.931  9.784   -9.03   1   48.08 ? 149 ASP   B CA  1 
ATOM   4190 C  C   . ASP   B 1 164 ? 38.841  8.433   -9.763  1   45.68 ? 149 ASP   B C   1 
ATOM   4191 O  O   . ASP   B 1 164 ? 38.707  7.38    -9.14   1   45.74 ? 149 ASP   B O   1 
ATOM   4192 C  CB  . ASP   B 1 164 ? 40.388  10.284  -8.963  1   52.03 ? 149 ASP   B CB  1 
ATOM   4193 C  CG  . ASP   B 1 164 ? 40.769  11.186  -10.13  1   61.56 ? 149 ASP   B CG  1 
ATOM   4194 O  OD1 . ASP   B 1 164 ? 40.067  11.142  -11.189 1   62.88 ? 149 ASP   B OD1 1 
ATOM   4195 O  OD2 . ASP   B 1 164 ? 41.764  11.93   -10     1   66.14 ? 149 ASP   B OD2 1 
ATOM   4196 N  N   . VAL   B 1 165 ? 38.907  8.473   -11.084 1   43.62 ? 150 VAL   B N   1 
ATOM   4197 C  CA  . VAL   B 1 165 ? 38.951  7.272   -11.909 1   42.19 ? 150 VAL   B CA  1 
ATOM   4198 C  C   . VAL   B 1 165 ? 40.417  6.835   -12.063 1   41.31 ? 150 VAL   B C   1 
ATOM   4199 O  O   . VAL   B 1 165 ? 41.312  7.626   -11.807 1   41.76 ? 150 VAL   B O   1 
ATOM   4200 C  CB  . VAL   B 1 165 ? 38.262  7.503   -13.279 1   42.59 ? 150 VAL   B CB  1 
ATOM   4201 C  CG1 . VAL   B 1 165 ? 36.788  7.829   -13.088 1   42.76 ? 150 VAL   B CG1 1 
ATOM   4202 C  CG2 . VAL   B 1 165 ? 38.966  8.604   -14.085 1   42.51 ? 150 VAL   B CG2 1 
ATOM   4203 N  N   . LEU   B 1 166 ? 40.668  5.583   -12.439 1   40.41 ? 151 LEU   B N   1 
ATOM   4204 C  CA  . LEU   B 1 166 ? 42.028  5.093   -12.645 1   39.73 ? 151 LEU   B CA  1 
ATOM   4205 C  C   . LEU   B 1 166 ? 42.476  5.342   -14.073 1   40.19 ? 151 LEU   B C   1 
ATOM   4206 O  O   . LEU   B 1 166 ? 43.645  5.651   -14.287 1   40.07 ? 151 LEU   B O   1 
ATOM   4207 C  CB  . LEU   B 1 166 ? 42.154  3.597   -12.305 1   39.08 ? 151 LEU   B CB  1 
ATOM   4208 C  CG  . LEU   B 1 166 ? 41.616  3.169   -10.928 1   40.31 ? 151 LEU   B CG  1 
ATOM   4209 C  CD1 . LEU   B 1 166 ? 41.858  1.678   -10.693 1   40.26 ? 151 LEU   B CD1 1 
ATOM   4210 C  CD2 . LEU   B 1 166 ? 42.267  3.964   -9.806  1   40.86 ? 151 LEU   B CD2 1 
ATOM   4211 N  N   . PHE   B 1 167 ? 41.556  5.197   -15.061 1   40.2  ? 152 PHE   B N   1 
ATOM   4212 C  CA  . PHE   B 1 167 ? 41.869  5.369   -16.482 1   40.8  ? 152 PHE   B CA  1 
ATOM   4213 C  C   . PHE   B 1 167 ? 40.852  6.206   -17.245 1   41.42 ? 152 PHE   B C   1 
ATOM   4214 O  O   . PHE   B 1 167 ? 39.626  6.137   -17.008 1   40.75 ? 152 PHE   B O   1 
ATOM   4215 C  CB  . PHE   B 1 167 ? 42.075  4.016   -17.184 1   41.05 ? 152 PHE   B CB  1 
ATOM   4216 C  CG  . PHE   B 1 167 ? 43.007  3.075   -16.454 1   42.98 ? 152 PHE   B CG  1 
ATOM   4217 C  CD1 . PHE   B 1 167 ? 44.386  3.199   -16.577 1   44.04 ? 152 PHE   B CD1 1 
ATOM   4218 C  CD2 . PHE   B 1 167 ? 42.506  2.079   -15.627 1   43.53 ? 152 PHE   B CD2 1 
ATOM   4219 C  CE1 . PHE   B 1 167 ? 45.241  2.349   -15.872 1   44.71 ? 152 PHE   B CE1 1 
ATOM   4220 C  CE2 . PHE   B 1 167 ? 43.36   1.239   -14.922 1   44.04 ? 152 PHE   B CE2 1 
ATOM   4221 C  CZ  . PHE   B 1 167 ? 44.719  1.385   -15.039 1   44.17 ? 152 PHE   B CZ  1 
ATOM   4222 N  N   . SER   B 1 168 ? 41.381  7.024   -18.165 1   41.55 ? 153 SER   B N   1 
ATOM   4223 C  CA  . SER   B 1 168 ? 40.626  7.876   -19.076 1   42.3  ? 153 SER   B CA  1 
ATOM   4224 C  C   . SER   B 1 168 ? 41.134  7.604   -20.508 1   41.52 ? 153 SER   B C   1 
ATOM   4225 O  O   . SER   B 1 168 ? 42.164  6.93    -20.686 1   42.07 ? 153 SER   B O   1 
ATOM   4226 C  CB  . SER   B 1 168 ? 40.8    9.344   -18.709 1   45.65 ? 153 SER   B CB  1 
ATOM   4227 O  OG  . SER   B 1 168 ? 42.1    9.795   -19.043 1   51.48 ? 153 SER   B OG  1 
ATOM   4228 N  N   . PHE   B 1 169 ? 40.409  8.079   -21.524 1   40.13 ? 154 PHE   B N   1 
ATOM   4229 C  CA  . PHE   B 1 169 ? 40.826  7.849   -22.909 1   39.42 ? 154 PHE   B CA  1 
ATOM   4230 C  C   . PHE   B 1 169 ? 41.545  9.064   -23.503 1   40.27 ? 154 PHE   B C   1 
ATOM   4231 O  O   . PHE   B 1 169 ? 42.592  8.909   -24.111 1   40.54 ? 154 PHE   B O   1 
ATOM   4232 C  CB  . PHE   B 1 169 ? 39.636  7.423   -23.784 1   38.29 ? 154 PHE   B CB  1 
ATOM   4233 C  CG  . PHE   B 1 169 ? 39.087  6.073   -23.399 1   38.41 ? 154 PHE   B CG  1 
ATOM   4234 C  CD1 . PHE   B 1 169 ? 39.728  4.91    -23.792 1   38.49 ? 154 PHE   B CD1 1 
ATOM   4235 C  CD2 . PHE   B 1 169 ? 37.942  5.965   -22.62  1   38.96 ? 154 PHE   B CD2 1 
ATOM   4236 C  CE1 . PHE   B 1 169 ? 39.24   3.671   -23.418 1   39.75 ? 154 PHE   B CE1 1 
ATOM   4237 C  CE2 . PHE   B 1 169 ? 37.449  4.721   -22.256 1   39.59 ? 154 PHE   B CE2 1 
ATOM   4238 C  CZ  . PHE   B 1 169 ? 38.106  3.581   -22.644 1   39.73 ? 154 PHE   B CZ  1 
ATOM   4239 N  N   . ARG   B 1 170 ? 40.973  10.255  -23.359 1   40.14 ? 155 ARG   B N   1 
ATOM   4240 C  CA  . ARG   B 1 170 ? 41.517  11.479  -23.937 1   41.26 ? 155 ARG   B CA  1 
ATOM   4241 C  C   . ARG   B 1 170 ? 41.373  12.619  -22.942 1   43.11 ? 155 ARG   B C   1 
ATOM   4242 O  O   . ARG   B 1 170 ? 40.453  12.607  -22.113 1   43.23 ? 155 ARG   B O   1 
ATOM   4243 C  CB  . ARG   B 1 170 ? 40.722  11.895  -25.213 1   41.67 ? 155 ARG   B CB  1 
ATOM   4244 C  CG  . ARG   B 1 170 ? 40.635  10.854  -26.322 1   43.73 ? 155 ARG   B CG  1 
ATOM   4245 C  CD  . ARG   B 1 170 ? 42.005  10.477  -26.871 1   46.44 ? 155 ARG   B CD  1 
ATOM   4246 N  NE  . ARG   B 1 170 ? 42.674  11.649  -27.441 1   48.2  ? 155 ARG   B NE  1 
ATOM   4247 C  CZ  . ARG   B 1 170 ? 42.551  12.039  -28.706 1   48.14 ? 155 ARG   B CZ  1 
ATOM   4248 N  NH1 . ARG   B 1 170 ? 41.839  11.321  -29.563 1   45.4  ? 155 ARG   B NH1 1 
ATOM   4249 N  NH2 . ARG   B 1 170 ? 43.174  13.132  -29.133 1   47.26 ? 155 ARG   B NH2 1 
ATOM   4250 N  N   . ASP   B 1 171 ? 42.23   13.655  -23.062 1   43.26 ? 156 ASP   B N   1 
ATOM   4251 C  CA  . ASP   B 1 171 ? 42.089  14.829  -22.202 1   44.15 ? 156 ASP   B CA  1 
ATOM   4252 C  C   . ASP   B 1 171 ? 40.775  15.556  -22.553 1   43.02 ? 156 ASP   B C   1 
ATOM   4253 O  O   . ASP   B 1 171 ? 40.402  15.638  -23.719 1   42.56 ? 156 ASP   B O   1 
ATOM   4254 C  CB  . ASP   B 1 171 ? 43.308  15.764  -22.357 1   47.76 ? 156 ASP   B CB  1 
ATOM   4255 C  CG  . ASP   B 1 171 ? 44.608  15.092  -21.926 1   54.42 ? 156 ASP   B CG  1 
ATOM   4256 O  OD1 . ASP   B 1 171 ? 44.586  14.345  -20.908 1   54.17 ? 156 ASP   B OD1 1 
ATOM   4257 O  OD2 . ASP   B 1 171 ? 45.645  15.302  -22.611 1   57.98 ? 156 ASP   B OD2 1 
ATOM   4258 N  N   . GLY   B 1 172 ? 40.042  15.985  -21.539 1   42.38 ? 157 GLY   B N   1 
ATOM   4259 C  CA  . GLY   B 1 172 ? 38.758  16.652  -21.743 1   41.97 ? 157 GLY   B CA  1 
ATOM   4260 C  C   . GLY   B 1 172 ? 37.614  15.737  -22.154 1   41.19 ? 157 GLY   B C   1 
ATOM   4261 O  O   . GLY   B 1 172 ? 36.55   16.235  -22.534 1   42.13 ? 157 GLY   B O   1 
ATOM   4262 N  N   . ASP   B 1 173 ? 37.795  14.393  -22.082 1   39.55 ? 158 ASP   B N   1 
ATOM   4263 C  CA  . ASP   B 1 173 ? 36.722  13.472  -22.49  1   38.33 ? 158 ASP   B CA  1 
ATOM   4264 C  C   . ASP   B 1 173 ? 35.582  13.334  -21.463 1   38.57 ? 158 ASP   B C   1 
ATOM   4265 O  O   . ASP   B 1 173 ? 34.615  12.641  -21.742 1   38.81 ? 158 ASP   B O   1 
ATOM   4266 C  CB  . ASP   B 1 173 ? 37.272  12.08   -22.876 1   37.77 ? 158 ASP   B CB  1 
ATOM   4267 C  CG  . ASP   B 1 173 ? 37.872  11.289  -21.721 1   38.28 ? 158 ASP   B CG  1 
ATOM   4268 O  OD1 . ASP   B 1 173 ? 37.859  11.8    -20.576 1   37.3  ? 158 ASP   B OD1 1 
ATOM   4269 O  OD2 . ASP   B 1 173 ? 38.392  10.167  -21.969 1   38.25 ? 158 ASP   B OD2 1 
ATOM   4270 N  N   . CYS   B 1 174 ? 35.714  13.937  -20.269 1   38.75 ? 159 CYS   B N   1 
ATOM   4271 C  CA  . CYS   B 1 174 ? 34.697  13.869  -19.214 1   39.02 ? 159 CYS   B CA  1 
ATOM   4272 C  C   . CYS   B 1 174 ? 34.48   12.443  -18.685 1   38.52 ? 159 CYS   B C   1 
ATOM   4273 O  O   . CYS   B 1 174 ? 33.396  12.145  -18.182 1   38.23 ? 159 CYS   B O   1 
ATOM   4274 C  CB  . CYS   B 1 174 ? 33.379  14.508  -19.657 1   39.79 ? 159 CYS   B CB  1 
ATOM   4275 S  SG  . CYS   B 1 174 ? 33.465  16.296  -19.934 1   45.67 ? 159 CYS   B SG  1 
ATOM   4276 N  N   . SER   B 1 175 ? 35.484  11.572  -18.816 1   38.64 ? 160 SER   B N   1 
ATOM   4277 C  CA  . SER   B 1 175 ? 35.366  10.193  -18.363 1   39.42 ? 160 SER   B CA  1 
ATOM   4278 C  C   . SER   B 1 175 ? 35.241  10.146  -16.857 1   39.23 ? 160 SER   B C   1 
ATOM   4279 O  O   . SER   B 1 175 ? 34.427  9.387   -16.357 1   38.62 ? 160 SER   B O   1 
ATOM   4280 C  CB  . SER   B 1 175 ? 36.518  9.336   -18.87  1   42.22 ? 160 SER   B CB  1 
ATOM   4281 O  OG  . SER   B 1 175 ? 37.757  9.903   -18.495 1   46.42 ? 160 SER   B OG  1 
ATOM   4282 N  N   . LYS   B 1 176 ? 35.933  11.045  -16.129 1   38.98 ? 161 LYS   B N   1 
ATOM   4283 C  CA  . LYS   B 1 176 ? 35.804  11.105  -14.682 1   39.26 ? 161 LYS   B CA  1 
ATOM   4284 C  C   . LYS   B 1 176 ? 34.349  11.373  -14.251 1   38.94 ? 161 LYS   B C   1 
ATOM   4285 O  O   . LYS   B 1 176 ? 33.8    10.596  -13.49  1   39.1  ? 161 LYS   B O   1 
ATOM   4286 C  CB  . LYS   B 1 176 ? 36.772  12.125  -14.065 1   41.09 ? 161 LYS   B CB  1 
ATOM   4287 C  CG  . LYS   B 1 176 ? 36.649  12.192  -12.559 1   44.94 ? 161 LYS   B CG  1 
ATOM   4288 C  CD  . LYS   B 1 176 ? 37.545  13.263  -11.952 1   48.59 ? 161 LYS   B CD  1 
ATOM   4289 C  CE  . LYS   B 1 176 ? 37.192  13.474  -10.504 1   52.07 ? 161 LYS   B CE  1 
ATOM   4290 N  NZ  . LYS   B 1 176 ? 38.212  14.299  -9.818  1   54.44 ? 161 LYS   B NZ  1 
ATOM   4291 N  N   . GLY   B 1 177 ? 33.747  12.437  -14.769 1   38.26 ? 162 GLY   B N   1 
ATOM   4292 C  CA  . GLY   B 1 177 ? 32.37   12.799  -14.481 1   38.12 ? 162 GLY   B CA  1 
ATOM   4293 C  C   . GLY   B 1 177 ? 31.365  11.72   -14.855 1   37.44 ? 162 GLY   B C   1 
ATOM   4294 O  O   . GLY   B 1 177 ? 30.491  11.408  -14.056 1   38.09 ? 162 GLY   B O   1 
ATOM   4295 N  N   . PHE   B 1 178 ? 31.484  11.132  -16.049 1   35.85 ? 163 PHE   B N   1 
ATOM   4296 C  CA  . PHE   B 1 178 ? 30.543  10.122  -16.513 1   35.87 ? 163 PHE   B CA  1 
ATOM   4297 C  C   . PHE   B 1 178 ? 30.652  8.833   -15.721 1   35.92 ? 163 PHE   B C   1 
ATOM   4298 O  O   . PHE   B 1 178 ? 29.622  8.321   -15.267 1   36.34 ? 163 PHE   B O   1 
ATOM   4299 C  CB  . PHE   B 1 178 ? 30.73   9.835   -18.008 1   35.65 ? 163 PHE   B CB  1 
ATOM   4300 C  CG  . PHE   B 1 178 ? 29.713  8.889   -18.615 1   35.92 ? 163 PHE   B CG  1 
ATOM   4301 C  CD1 . PHE   B 1 178 ? 28.357  9.187   -18.586 1   36.19 ? 163 PHE   B CD1 1 
ATOM   4302 C  CD2 . PHE   B 1 178 ? 30.118  7.744   -19.279 1   35.93 ? 163 PHE   B CD2 1 
ATOM   4303 C  CE1 . PHE   B 1 178 ? 27.43   8.358   -19.203 1   36.26 ? 163 PHE   B CE1 1 
ATOM   4304 C  CE2 . PHE   B 1 178 ? 29.188  6.903   -19.875 1   36.33 ? 163 PHE   B CE2 1 
ATOM   4305 C  CZ  . PHE   B 1 178 ? 27.844  7.212   -19.827 1   35.87 ? 163 PHE   B CZ  1 
ATOM   4306 N  N   . PHE   B 1 179 ? 31.882  8.317   -15.536 1   35.2  ? 164 PHE   B N   1 
ATOM   4307 C  CA  . PHE   B 1 179 ? 32.09   7.061   -14.8   1   35.29 ? 164 PHE   B CA  1 
ATOM   4308 C  C   . PHE   B 1 179 ? 31.768  7.221   -13.321 1   36.1  ? 164 PHE   B C   1 
ATOM   4309 O  O   . PHE   B 1 179 ? 31.124  6.352   -12.753 1   36.1  ? 164 PHE   B O   1 
ATOM   4310 C  CB  . PHE   B 1 179 ? 33.515  6.499   -14.969 1   34.6  ? 164 PHE   B CB  1 
ATOM   4311 C  CG  . PHE   B 1 179 ? 33.975  6.211   -16.386 1   35.16 ? 164 PHE   B CG  1 
ATOM   4312 C  CD1 . PHE   B 1 179 ? 33.06   6.02    -17.405 1   35.52 ? 164 PHE   B CD1 1 
ATOM   4313 C  CD2 . PHE   B 1 179 ? 35.324  6.2     -16.703 1   36.13 ? 164 PHE   B CD2 1 
ATOM   4314 C  CE1 . PHE   B 1 179 ? 33.486  5.811   -18.713 1   36.35 ? 164 PHE   B CE1 1 
ATOM   4315 C  CE2 . PHE   B 1 179 ? 35.751  5.969   -18.006 1   36.19 ? 164 PHE   B CE2 1 
ATOM   4316 C  CZ  . PHE   B 1 179 ? 34.83   5.782   -19.003 1   36.4  ? 164 PHE   B CZ  1 
ATOM   4317 N  N   . LEU   B 1 180 ? 32.244  8.301   -12.685 1   36.36 ? 165 LEU   B N   1 
ATOM   4318 C  CA  . LEU   B 1 180 ? 31.996  8.506   -11.253 1   36.89 ? 165 LEU   B CA  1 
ATOM   4319 C  C   . LEU   B 1 180 ? 30.548  8.816   -10.905 1   36.91 ? 165 LEU   B C   1 
ATOM   4320 O  O   . LEU   B 1 180 ? 30.107  8.363   -9.861  1   38.68 ? 165 LEU   B O   1 
ATOM   4321 C  CB  . LEU   B 1 180 ? 32.918  9.563   -10.624 1   37.34 ? 165 LEU   B CB  1 
ATOM   4322 C  CG  . LEU   B 1 180 ? 34.416  9.228   -10.514 1   39.2  ? 165 LEU   B CG  1 
ATOM   4323 C  CD1 . LEU   B 1 180 ? 35.142  10.303  -9.737  1   39.66 ? 165 LEU   B CD1 1 
ATOM   4324 C  CD2 . LEU   B 1 180 ? 34.662  7.876   -9.864  1   39.22 ? 165 LEU   B CD2 1 
ATOM   4325 N  N   . VAL   B 1 181 ? 29.821  9.584   -11.716 1   35.32 ? 166 VAL   B N   1 
ATOM   4326 C  CA  . VAL   B 1 181 ? 28.417  9.867   -11.431 1   35.26 ? 166 VAL   B CA  1 
ATOM   4327 C  C   . VAL   B 1 181 ? 27.59   8.564   -11.565 1   35.37 ? 166 VAL   B C   1 
ATOM   4328 O  O   . VAL   B 1 181 ? 26.753  8.285   -10.703 1   35.35 ? 166 VAL   B O   1 
ATOM   4329 C  CB  . VAL   B 1 181 ? 27.839  11.073  -12.209 1   35.7  ? 166 VAL   B CB  1 
ATOM   4330 C  CG1 . VAL   B 1 181 ? 26.329  11.17   -12.05  1   36.15 ? 166 VAL   B CG1 1 
ATOM   4331 C  CG2 . VAL   B 1 181 ? 28.507  12.372  -11.743 1   36.19 ? 166 VAL   B CG2 1 
ATOM   4332 N  N   . SER   B 1 182 ? 27.933  7.705   -12.548 1   34.25 ? 167 SER   B N   1 
ATOM   4333 C  CA  . SER   B 1 182 ? 27.279  6.402   -12.705 1   34.83 ? 167 SER   B CA  1 
ATOM   4334 C  C   . SER   B 1 182 ? 27.554  5.556   -11.459 1   35.17 ? 167 SER   B C   1 
ATOM   4335 O  O   . SER   B 1 182 ? 26.629  4.963   -10.898 1   35.25 ? 167 SER   B O   1 
ATOM   4336 C  CB  . SER   B 1 182 ? 27.825  5.684   -13.942 1   35.52 ? 167 SER   B CB  1 
ATOM   4337 O  OG  . SER   B 1 182 ? 27.28   6.289   -15.098 1   37.66 ? 167 SER   B OG  1 
ATOM   4338 N  N   . LEU   B 1 183 ? 28.82   5.535   -11.014 1   34.68 ? 168 LEU   B N   1 
ATOM   4339 C  CA  . LEU   B 1 183 ? 29.235  4.797   -9.829  1   35.23 ? 168 LEU   B CA  1 
ATOM   4340 C  C   . LEU   B 1 183 ? 28.514  5.297   -8.576  1   37.28 ? 168 LEU   B C   1 
ATOM   4341 O  O   . LEU   B 1 183 ? 28.05   4.485   -7.773  1   38.06 ? 168 LEU   B O   1 
ATOM   4342 C  CB  . LEU   B 1 183 ? 30.748  4.89    -9.631  1   34.06 ? 168 LEU   B CB  1 
ATOM   4343 C  CG  . LEU   B 1 183 ? 31.297  4.214   -8.365  1   34.75 ? 168 LEU   B CG  1 
ATOM   4344 C  CD1 . LEU   B 1 183 ? 31.094  2.712   -8.429  1   35.11 ? 168 LEU   B CD1 1 
ATOM   4345 C  CD2 . LEU   B 1 183 ? 32.771  4.539   -8.146  1   34.66 ? 168 LEU   B CD2 1 
ATOM   4346 N  N   . LEU   B 1 184 ? 28.395  6.608   -8.416  1   37.8  ? 169 LEU   B N   1 
ATOM   4347 C  CA  . LEU   B 1 184 ? 27.731  7.179   -7.247  1   38.44 ? 169 LEU   B CA  1 
ATOM   4348 C  C   . LEU   B 1 184 ? 26.253  6.835   -7.218  1   38.28 ? 169 LEU   B C   1 
ATOM   4349 O  O   . LEU   B 1 184 ? 25.739  6.554   -6.147  1   38.96 ? 169 LEU   B O   1 
ATOM   4350 C  CB  . LEU   B 1 184 ? 27.968  8.693   -7.171  1   39.63 ? 169 LEU   B CB  1 
ATOM   4351 C  CG  . LEU   B 1 184 ? 29.403  9.09    -6.805  1   41.91 ? 169 LEU   B CG  1 
ATOM   4352 C  CD1 . LEU   B 1 184 ? 29.654  10.587  -7.078  1   42.35 ? 169 LEU   B CD1 1 
ATOM   4353 C  CD2 . LEU   B 1 184 ? 29.742  8.684   -5.36   1   42.61 ? 169 LEU   B CD2 1 
ATOM   4354 N  N   . VAL   B 1 185 ? 25.554  6.866   -8.372  1   37.3  ? 170 VAL   B N   1 
ATOM   4355 C  CA  . VAL   B 1 185 ? 24.144  6.497   -8.432  1   37.7  ? 170 VAL   B CA  1 
ATOM   4356 C  C   . VAL   B 1 185 ? 24.024  4.991   -8.108  1   38.13 ? 170 VAL   B C   1 
ATOM   4357 O  O   . VAL   B 1 185 ? 23.188  4.596   -7.295  1   38.39 ? 170 VAL   B O   1 
ATOM   4358 C  CB  . VAL   B 1 185 ? 23.511  6.848   -9.801  1   38.65 ? 170 VAL   B CB  1 
ATOM   4359 C  CG1 . VAL   B 1 185 ? 22.135  6.207   -9.956  1   39.48 ? 170 VAL   B CG1 1 
ATOM   4360 C  CG2 . VAL   B 1 185 ? 23.419  8.358   -9.992  1   39.3  ? 170 VAL   B CG2 1 
ATOM   4361 N  N   . GLU   B 1 186 ? 24.911  4.167   -8.699  1   37.69 ? 171 GLU   B N   1 
ATOM   4362 C  CA  . GLU   B 1 186 ? 24.994  2.722   -8.493  1   37.69 ? 171 GLU   B CA  1 
ATOM   4363 C  C   . GLU   B 1 186 ? 25.148  2.397   -6.986  1   39.83 ? 171 GLU   B C   1 
ATOM   4364 O  O   . GLU   B 1 186 ? 24.432  1.535   -6.463  1   40.66 ? 171 GLU   B O   1 
ATOM   4365 C  CB  . GLU   B 1 186 ? 26.182  2.178   -9.306  1   37.22 ? 171 GLU   B CB  1 
ATOM   4366 C  CG  . GLU   B 1 186 ? 26.51   0.715   -9.088  1   37.53 ? 171 GLU   B CG  1 
ATOM   4367 C  CD  . GLU   B 1 186 ? 25.669  -0.26   -9.89   1   36.12 ? 171 GLU   B CD  1 
ATOM   4368 O  OE1 . GLU   B 1 186 ? 25.157  0.124   -10.971 1   33.5  ? 171 GLU   B OE1 1 
ATOM   4369 O  OE2 . GLU   B 1 186 ? 25.525  -1.419  -9.436  1   35.3  ? 171 GLU   B OE2 1 
ATOM   4370 N  N   . ILE   B 1 187 ? 26.023  3.146   -6.277  1   39.8  ? 172 ILE   B N   1 
ATOM   4371 C  CA  . ILE   B 1 187 ? 26.252  2.979   -4.845  1   40.57 ? 172 ILE   B CA  1 
ATOM   4372 C  C   . ILE   B 1 187 ? 25.038  3.456   -4      1   41.23 ? 172 ILE   B C   1 
ATOM   4373 O  O   . ILE   B 1 187 ? 24.695  2.793   -3.01   1   42.1  ? 172 ILE   B O   1 
ATOM   4374 C  CB  . ILE   B 1 187 ? 27.576  3.666   -4.415  1   41.17 ? 172 ILE   B CB  1 
ATOM   4375 C  CG1 . ILE   B 1 187 ? 28.799  2.929   -4.988  1   41.76 ? 172 ILE   B CG1 1 
ATOM   4376 C  CG2 . ILE   B 1 187 ? 27.692  3.784   -2.866  1   41.59 ? 172 ILE   B CG2 1 
ATOM   4377 C  CD1 . ILE   B 1 187 ? 30.127  3.711   -4.773  1   42.82 ? 172 ILE   B CD1 1 
ATOM   4378 N  N   . ALA   B 1 188 ? 24.396  4.587   -4.383  1   40.03 ? 173 ALA   B N   1 
ATOM   4379 C  CA  . ALA   B 1 188 ? 23.22   5.081   -3.665  1   40.63 ? 173 ALA   B CA  1 
ATOM   4380 C  C   . ALA   B 1 188 ? 22.054  4.089   -3.781  1   41.32 ? 173 ALA   B C   1 
ATOM   4381 O  O   . ALA   B 1 188 ? 21.366  3.824   -2.792  1   42.03 ? 173 ALA   B O   1 
ATOM   4382 C  CB  . ALA   B 1 188 ? 22.798  6.445   -4.194  1   40.31 ? 173 ALA   B CB  1 
ATOM   4383 N  N   . ALA   B 1 189 ? 21.839  3.527   -4.976  1   40.41 ? 174 ALA   B N   1 
ATOM   4384 C  CA  . ALA   B 1 189 ? 20.764  2.547   -5.183  1   39.95 ? 174 ALA   B CA  1 
ATOM   4385 C  C   . ALA   B 1 189 ? 21.035  1.238   -4.431  1   39.44 ? 174 ALA   B C   1 
ATOM   4386 O  O   . ALA   B 1 189 ? 20.091  0.576   -4.009  1   39.04 ? 174 ALA   B O   1 
ATOM   4387 C  CB  . ALA   B 1 189 ? 20.58   2.259   -6.666  1   39.54 ? 174 ALA   B CB  1 
ATOM   4388 N  N   . ALA   B 1 190 ? 22.316  0.888   -4.235  1   39.17 ? 175 ALA   B N   1 
ATOM   4389 C  CA  . ALA   B 1 190 ? 22.724  -0.332  -3.537  1   39.29 ? 175 ALA   B CA  1 
ATOM   4390 C  C   . ALA   B 1 190 ? 22.309  -0.363  -2.064  1   39.37 ? 175 ALA   B C   1 
ATOM   4391 O  O   . ALA   B 1 190 ? 22.25   -1.451  -1.486  1   38.86 ? 175 ALA   B O   1 
ATOM   4392 C  CB  . ALA   B 1 190 ? 24.224  -0.523  -3.633  1   39.09 ? 175 ALA   B CB  1 
ATOM   4393 N  N   . SER   B 1 191 ? 22.058  0.806   -1.447  1   38.95 ? 176 SER   B N   1 
ATOM   4394 C  CA  . SER   B 1 191 ? 21.636  0.823   -0.054  1   39.34 ? 176 SER   B CA  1 
ATOM   4395 C  C   . SER   B 1 191 ? 20.249  0.123   0.13    1   38.84 ? 176 SER   B C   1 
ATOM   4396 O  O   . SER   B 1 191 ? 19.952  -0.361  1.218   1   38.83 ? 176 SER   B O   1 
ATOM   4397 C  CB  . SER   B 1 191 ? 21.608  2.248   0.474   1   41.31 ? 176 SER   B CB  1 
ATOM   4398 O  OG  . SER   B 1 191 ? 20.557  2.941   -0.169  1   43.92 ? 176 SER   B OG  1 
ATOM   4399 N  N   . ALA   B 1 192 ? 19.444  0.016   -0.944  1   37.99 ? 177 ALA   B N   1 
ATOM   4400 C  CA  . ALA   B 1 192 ? 18.175  -0.692  -0.884  1   37.49 ? 177 ALA   B CA  1 
ATOM   4401 C  C   . ALA   B 1 192 ? 18.354  -2.234  -0.956  1   37.24 ? 177 ALA   B C   1 
ATOM   4402 O  O   . ALA   B 1 192 ? 17.423  -2.954  -0.631  1   36.9  ? 177 ALA   B O   1 
ATOM   4403 C  CB  . ALA   B 1 192 ? 17.248  -0.195  -1.975  1   37.14 ? 177 ALA   B CB  1 
ATOM   4404 N  N   . ILE   B 1 193 ? 19.544  -2.737  -1.345  1   37.32 ? 178 ILE   B N   1 
ATOM   4405 C  CA  . ILE   B 1 193 ? 19.799  -4.18   -1.454  1   38.42 ? 178 ILE   B CA  1 
ATOM   4406 C  C   . ILE   B 1 193 ? 19.683  -4.904  -0.109  1   39.61 ? 178 ILE   B C   1 
ATOM   4407 O  O   . ILE   B 1 193 ? 19.112  -6.003  -0.061  1   39.83 ? 178 ILE   B O   1 
ATOM   4408 C  CB  . ILE   B 1 193 ? 21.159  -4.488  -2.128  1   38.77 ? 178 ILE   B CB  1 
ATOM   4409 C  CG1 . ILE   B 1 193 ? 21.193  -3.979  -3.582  1   39.68 ? 178 ILE   B CG1 1 
ATOM   4410 C  CG2 . ILE   B 1 193 ? 21.515  -5.984  -2.063  1   38.82 ? 178 ILE   B CG2 1 
ATOM   4411 C  CD1 . ILE   B 1 193 ? 22.662  -3.976  -4.126  1   41.41 ? 178 ILE   B CD1 1 
ATOM   4412 N  N   . LYS   B 1 194 ? 20.208  -4.302  0.971   1   39.27 ? 179 LYS   B N   1 
ATOM   4413 C  CA  . LYS   B 1 194 ? 20.116  -4.918  2.291   1   40.51 ? 179 LYS   B CA  1 
ATOM   4414 C  C   . LYS   B 1 194 ? 18.659  -5.102  2.775   1   40.89 ? 179 LYS   B C   1 
ATOM   4415 O  O   . LYS   B 1 194 ? 18.413  -5.902  3.677   1   42.49 ? 179 LYS   B O   1 
ATOM   4416 C  CB  . LYS   B 1 194 ? 20.944  -4.142  3.335   1   42.93 ? 179 LYS   B CB  1 
ATOM   4417 C  CG  . LYS   B 1 194 ? 20.384  -2.768  3.646   1   48.84 ? 179 LYS   B CG  1 
ATOM   4418 C  CD  . LYS   B 1 194 ? 21.378  -1.938  4.462   1   55.21 ? 179 LYS   B CD  1 
ATOM   4419 C  CE  . LYS   B 1 194 ? 20.807  -0.599  4.863   1   60.13 ? 179 LYS   B CE  1 
ATOM   4420 N  NZ  . LYS   B 1 194 ? 21.007  0.451   3.823   1   63.04 ? 179 LYS   B NZ  1 
ATOM   4421 N  N   . VAL   B 1 195 ? 17.708  -4.41   2.166   1   39.8  ? 180 VAL   B N   1 
ATOM   4422 C  CA  . VAL   B 1 195 ? 16.292  -4.527  2.509   1   39.57 ? 180 VAL   B CA  1 
ATOM   4423 C  C   . VAL   B 1 195 ? 15.641  -5.748  1.793   1   40.02 ? 180 VAL   B C   1 
ATOM   4424 O  O   . VAL   B 1 195 ? 14.598  -6.235  2.23    1   40.46 ? 180 VAL   B O   1 
ATOM   4425 C  CB  . VAL   B 1 195 ? 15.529  -3.203  2.229   1   39.7  ? 180 VAL   B CB  1 
ATOM   4426 C  CG1 . VAL   B 1 195 ? 14.124  -3.241  2.807   1   39.8  ? 180 VAL   B CG1 1 
ATOM   4427 C  CG2 . VAL   B 1 195 ? 16.285  -1.996  2.785   1   39.87 ? 180 VAL   B CG2 1 
ATOM   4428 N  N   . ILE   B 1 196 ? 16.268  -6.265  0.726   1   39.43 ? 181 ILE   B N   1 
ATOM   4429 C  CA  . ILE   B 1 196 ? 15.739  -7.397  -0.027  1   40.07 ? 181 ILE   B CA  1 
ATOM   4430 C  C   . ILE   B 1 196 ? 15.473  -8.63   0.862   1   40.68 ? 181 ILE   B C   1 
ATOM   4431 O  O   . ILE   B 1 196 ? 14.36   -9.14   0.791   1   41.23 ? 181 ILE   B O   1 
ATOM   4432 C  CB  . ILE   B 1 196 ? 16.608  -7.72   -1.273  1   40.29 ? 181 ILE   B CB  1 
ATOM   4433 C  CG1 . ILE   B 1 196 ? 16.537  -6.542  -2.264  1   40.34 ? 181 ILE   B CG1 1 
ATOM   4434 C  CG2 . ILE   B 1 196 ? 16.166  -9.027  -1.934  1   40.72 ? 181 ILE   B CG2 1 
ATOM   4435 C  CD1 . ILE   B 1 196 ? 17.426  -6.69   -3.52   1   41.42 ? 181 ILE   B CD1 1 
ATOM   4436 N  N   . PRO   B 1 197 ? 16.399  -9.086  1.744   1   40.64 ? 182 PRO   B N   1 
ATOM   4437 C  CA  . PRO   B 1 197 ? 16.077  -10.243 2.598   1   40.73 ? 182 PRO   B CA  1 
ATOM   4438 C  C   . PRO   B 1 197 ? 14.877  -9.991  3.499   1   41.04 ? 182 PRO   B C   1 
ATOM   4439 O  O   . PRO   B 1 197 ? 14.105  -10.907 3.739   1   41.46 ? 182 PRO   B O   1 
ATOM   4440 C  CB  . PRO   B 1 197 ? 17.353  -10.44  3.438   1   41.53 ? 182 PRO   B CB  1 
ATOM   4441 C  CG  . PRO   B 1 197 ? 18.419  -9.729  2.718   1   41.86 ? 182 PRO   B CG  1 
ATOM   4442 C  CD  . PRO   B 1 197 ? 17.771  -8.595  2.006   1   39.88 ? 182 PRO   B CD  1 
ATOM   4443 N  N   . THR   B 1 198 ? 14.716  -8.743  3.979   1   40.95 ? 183 THR   B N   1 
ATOM   4444 C  CA  . THR   B 1 198 ? 13.591  -8.337  4.825   1   40.71 ? 183 THR   B CA  1 
ATOM   4445 C  C   . THR   B 1 198 ? 12.278  -8.486  4.068   1   39.19 ? 183 THR   B C   1 
ATOM   4446 O  O   . THR   B 1 198 ? 11.301  -8.997  4.617   1   38.45 ? 183 THR   B O   1 
ATOM   4447 C  CB  . THR   B 1 198 ? 13.813  -6.914  5.338   1   42.53 ? 183 THR   B CB  1 
ATOM   4448 O  OG1 . THR   B 1 198 ? 15.055  -6.901  6.038   1   44.84 ? 183 THR   B OG1 1 
ATOM   4449 C  CG2 . THR   B 1 198 ? 12.705  -6.447  6.264   1   42.58 ? 183 THR   B CG2 1 
ATOM   4450 N  N   . VAL   B 1 199 ? 12.256  -8.063  2.798   1   38.02 ? 184 VAL   B N   1 
ATOM   4451 C  CA  . VAL   B 1 199 ? 11.068  -8.176  1.95    1   37.41 ? 184 VAL   B CA  1 
ATOM   4452 C  C   . VAL   B 1 199 ? 10.634  -9.647  1.799   1   37.97 ? 184 VAL   B C   1 
ATOM   4453 O  O   . VAL   B 1 199 ? 9.459   -9.971  2.013   1   37.29 ? 184 VAL   B O   1 
ATOM   4454 C  CB  . VAL   B 1 199 ? 11.285  -7.496  0.569   1   36.99 ? 184 VAL   B CB  1 
ATOM   4455 C  CG1 . VAL   B 1 199 ? 10.14   -7.804  -0.388  1   36.98 ? 184 VAL   B CG1 1 
ATOM   4456 C  CG2 . VAL   B 1 199 ? 11.443  -5.993  0.72    1   36.72 ? 184 VAL   B CG2 1 
ATOM   4457 N  N   . PHE   B 1 200 ? 11.571  -10.526 1.445   1   38.1  ? 185 PHE   B N   1 
ATOM   4458 C  CA  . PHE   B 1 200 ? 11.242  -11.94  1.253   1   39.85 ? 185 PHE   B CA  1 
ATOM   4459 C  C   . PHE   B 1 200 ? 10.913  -12.685 2.544   1   40.12 ? 185 PHE   B C   1 
ATOM   4460 O  O   . PHE   B 1 200 ? 10.057  -13.566 2.522   1   39.9  ? 185 PHE   B O   1 
ATOM   4461 C  CB  . PHE   B 1 200 ? 12.343  -12.663 0.465   1   40.69 ? 185 PHE   B CB  1 
ATOM   4462 C  CG  . PHE   B 1 200 ? 12.355  -12.191 -0.968  1   41.93 ? 185 PHE   B CG  1 
ATOM   4463 C  CD1 . PHE   B 1 200 ? 11.215  -12.277 -1.755  1   42.91 ? 185 PHE   B CD1 1 
ATOM   4464 C  CD2 . PHE   B 1 200 ? 13.51   -11.683 -1.536  1   43.43 ? 185 PHE   B CD2 1 
ATOM   4465 C  CE1 . PHE   B 1 200 ? 11.231  -11.848 -3.083  1   43.98 ? 185 PHE   B CE1 1 
ATOM   4466 C  CE2 . PHE   B 1 200 ? 13.533  -11.289 -2.873  1   44.3  ? 185 PHE   B CE2 1 
ATOM   4467 C  CZ  . PHE   B 1 200 ? 12.394  -11.364 -3.636  1   44    ? 185 PHE   B CZ  1 
ATOM   4468 N  N   . LYS   B 1 201 ? 11.577  -12.345 3.654   1   40.51 ? 186 LYS   B N   1 
ATOM   4469 C  CA  . LYS   B 1 201 ? 11.271  -12.977 4.935   1   41.4  ? 186 LYS   B CA  1 
ATOM   4470 C  C   . LYS   B 1 201 ? 9.875   -12.529 5.379   1   42.17 ? 186 LYS   B C   1 
ATOM   4471 O  O   . LYS   B 1 201 ? 9.087   -13.359 5.82    1   42.33 ? 186 LYS   B O   1 
ATOM   4472 C  CB  . LYS   B 1 201 ? 12.32   -12.634 6.006   1   43.03 ? 186 LYS   B CB  1 
ATOM   4473 N  N   . ALA   B 1 202 ? 9.555   -11.23  5.227   1   42.2  ? 187 ALA   B N   1 
ATOM   4474 C  CA  . ALA   B 1 202 ? 8.24    -10.702 5.599   1   42.42 ? 187 ALA   B CA  1 
ATOM   4475 C  C   . ALA   B 1 202 ? 7.133   -11.358 4.8     1   42.92 ? 187 ALA   B C   1 
ATOM   4476 O  O   . ALA   B 1 202 ? 6.081   -11.635 5.356   1   42.84 ? 187 ALA   B O   1 
ATOM   4477 C  CB  . ALA   B 1 202 ? 8.189   -9.197  5.413   1   42.05 ? 187 ALA   B CB  1 
ATOM   4478 N  N   . MET   B 1 203 ? 7.351   -11.608 3.502   1   43.11 ? 188 MET   B N   1 
ATOM   4479 C  CA  . MET   B 1 203 ? 6.336   -12.262 2.681   1   44.48 ? 188 MET   B CA  1 
ATOM   4480 C  C   . MET   B 1 203 ? 6.097   -13.709 3.139   1   46.09 ? 188 MET   B C   1 
ATOM   4481 O  O   . MET   B 1 203 ? 4.949   -14.103 3.311   1   46.25 ? 188 MET   B O   1 
ATOM   4482 C  CB  . MET   B 1 203 ? 6.736   -12.245 1.208   1   44.57 ? 188 MET   B CB  1 
ATOM   4483 C  CG  . MET   B 1 203 ? 6.474   -10.948 0.524   1   45.89 ? 188 MET   B CG  1 
ATOM   4484 S  SD  . MET   B 1 203 ? 7.35    -10.928 -1.059  1   47.92 ? 188 MET   B SD  1 
ATOM   4485 C  CE  . MET   B 1 203 ? 6.55    -12.25  -1.905  1   49.14 ? 188 MET   B CE  1 
ATOM   4486 N  N   . GLN   B 1 204 ? 7.172   -14.473 3.379   1   47.13 ? 189 GLN   B N   1 
ATOM   4487 C  CA  . GLN   B 1 204 ? 7.105   -15.866 3.818   1   49.21 ? 189 GLN   B CA  1 
ATOM   4488 C  C   . GLN   B 1 204 ? 6.473   -16.017 5.22    1   50.4  ? 189 GLN   B C   1 
ATOM   4489 O  O   . GLN   B 1 204 ? 5.652   -16.917 5.428   1   50.93 ? 189 GLN   B O   1 
ATOM   4490 C  CB  . GLN   B 1 204 ? 8.509   -16.49  3.806   1   52.14 ? 189 GLN   B CB  1 
ATOM   4491 C  CG  . GLN   B 1 204 ? 8.502   -17.98  3.496   1   58.18 ? 189 GLN   B CG  1 
ATOM   4492 C  CD  . GLN   B 1 204 ? 8.904   -18.789 4.698   1   66.1  ? 189 GLN   B CD  1 
ATOM   4493 O  OE1 . GLN   B 1 204 ? 9.721   -18.352 5.529   1   68.22 ? 189 GLN   B OE1 1 
ATOM   4494 N  NE2 . GLN   B 1 204 ? 8.34    -20     4.815   1   67.75 ? 189 GLN   B NE2 1 
ATOM   4495 N  N   . MET   B 1 205 ? 6.86    -15.147 6.167   1   50.22 ? 190 MET   B N   1 
ATOM   4496 C  CA  . MET   B 1 205 ? 6.322   -15.145 7.531   1   50.86 ? 190 MET   B CA  1 
ATOM   4497 C  C   . MET   B 1 205 ? 4.98    -14.407 7.653   1   50.55 ? 190 MET   B C   1 
ATOM   4498 O  O   . MET   B 1 205 ? 4.461   -14.305 8.76    1   51.16 ? 190 MET   B O   1 
ATOM   4499 C  CB  . MET   B 1 205 ? 7.32    -14.521 8.527   1   52.56 ? 190 MET   B CB  1 
ATOM   4500 C  CG  . MET   B 1 205 ? 8.675   -15.197 8.563   1   58.38 ? 190 MET   B CG  1 
ATOM   4501 S  SD  . MET   B 1 205 ? 8.611   -16.993 8.847   1   77.03 ? 190 MET   B SD  1 
ATOM   4502 C  CE  . MET   B 1 205 ? 8.17    -17.03  10.606  1   75.45 ? 190 MET   B CE  1 
ATOM   4503 N  N   . GLN   B 1 206 ? 4.444   -13.866 6.54    1   49.11 ? 191 GLN   B N   1 
ATOM   4504 C  CA  . GLN   B 1 206 ? 3.202   -13.124 6.501   1   48.87 ? 191 GLN   B CA  1 
ATOM   4505 C  C   . GLN   B 1 206 ? 3.218   -11.957 7.473   1   47.97 ? 191 GLN   B C   1 
ATOM   4506 O  O   . GLN   B 1 206 ? 2.255   -11.751 8.201   1   49.16 ? 191 GLN   B O   1 
ATOM   4507 C  CB  . GLN   B 1 206 ? 1.989   -14.047 6.708   1   50.75 ? 191 GLN   B CB  1 
ATOM   4508 C  CG  . GLN   B 1 206 ? 1.735   -15.016 5.543   1   53.9  ? 191 GLN   B CG  1 
ATOM   4509 C  CD  . GLN   B 1 206 ? 0.966   -14.378 4.403   1   60.08 ? 191 GLN   B CD  1 
ATOM   4510 O  OE1 . GLN   B 1 206 ? 0.184   -13.423 4.579   1   62    ? 191 GLN   B OE1 1 
ATOM   4511 N  NE2 . GLN   B 1 206 ? 1.158   -14.901 3.195   1   61.41 ? 191 GLN   B NE2 1 
ATOM   4512 N  N   . GLU   B 1 207 ? 4.323   -11.204 7.499   1   45.47 ? 192 GLU   B N   1 
ATOM   4513 C  CA  . GLU   B 1 207 ? 4.495   -10.045 8.344   1   43.55 ? 192 GLU   B CA  1 
ATOM   4514 C  C   . GLU   B 1 207 ? 4.157   -8.777  7.557   1   42.01 ? 192 GLU   B C   1 
ATOM   4515 O  O   . GLU   B 1 207 ? 5.047   -8.102  7.033   1   41.33 ? 192 GLU   B O   1 
ATOM   4516 C  CB  . GLU   B 1 207 ? 5.926   -9.982  8.884   1   45.59 ? 192 GLU   B CB  1 
ATOM   4517 C  CG  . GLU   B 1 207 ? 6.28    -11.105 9.842   1   51.92 ? 192 GLU   B CG  1 
ATOM   4518 C  CD  . GLU   B 1 207 ? 5.683   -10.991 11.234  1   63.14 ? 192 GLU   B CD  1 
ATOM   4519 O  OE1 . GLU   B 1 207 ? 5.404   -9.853  11.678  1   64.37 ? 192 GLU   B OE1 1 
ATOM   4520 O  OE2 . GLU   B 1 207 ? 5.504   -12.046 11.889  1   67.65 ? 192 GLU   B OE2 1 
ATOM   4521 N  N   . ARG   B 1 208 ? 2.863   -8.46   7.476   1   40.47 ? 193 ARG   B N   1 
ATOM   4522 C  CA  . ARG   B 1 208 ? 2.359   -7.293  6.775   1   39    ? 193 ARG   B CA  1 
ATOM   4523 C  C   . ARG   B 1 208 ? 3.049   -5.976  7.148   1   39.69 ? 193 ARG   B C   1 
ATOM   4524 O  O   . ARG   B 1 208 ? 3.433   -5.231  6.242   1   40.73 ? 193 ARG   B O   1 
ATOM   4525 C  CB  . ARG   B 1 208 ? 0.84    -7.172  6.953   1   37.79 ? 193 ARG   B CB  1 
ATOM   4526 C  CG  . ARG   B 1 208 ? 0.219   -6.045  6.166   1   36.73 ? 193 ARG   B CG  1 
ATOM   4527 C  CD  . ARG   B 1 208 ? 0.019   -4.794  6.989   1   36.17 ? 193 ARG   B CD  1 
ATOM   4528 N  NE  . ARG   B 1 208 ? -0.735  -3.799  6.233   1   35.1  ? 193 ARG   B NE  1 
ATOM   4529 C  CZ  . ARG   B 1 208 ? -0.836  -2.52   6.57    1   35.64 ? 193 ARG   B CZ  1 
ATOM   4530 N  NH1 . ARG   B 1 208 ? -0.224  -2.062  7.656   1   35.44 ? 193 ARG   B NH1 1 
ATOM   4531 N  NH2 . ARG   B 1 208 ? -1.554  -1.688  5.829   1   33.05 ? 193 ARG   B NH2 1 
ATOM   4532 N  N   . ASP   B 1 209 ? 3.17    -5.656  8.448   1   38.59 ? 194 ASP   B N   1 
ATOM   4533 C  CA  . ASP   B 1 209 ? 3.764   -4.383  8.835   1   37.9  ? 194 ASP   B CA  1 
ATOM   4534 C  C   . ASP   B 1 209 ? 5.255   -4.332  8.478   1   37.52 ? 194 ASP   B C   1 
ATOM   4535 O  O   . ASP   B 1 209 ? 5.736   -3.284  8.072   1   37.85 ? 194 ASP   B O   1 
ATOM   4536 C  CB  . ASP   B 1 209 ? 3.528   -4.082  10.318  1   38.69 ? 194 ASP   B CB  1 
ATOM   4537 C  CG  . ASP   B 1 209 ? 2.067   -4.033  10.725  1   41.87 ? 194 ASP   B CG  1 
ATOM   4538 O  OD1 . ASP   B 1 209 ? 1.232   -3.512  9.928   1   42    ? 194 ASP   B OD1 1 
ATOM   4539 O  OD2 . ASP   B 1 209 ? 1.757   -4.495  11.833  1   42.01 ? 194 ASP   B OD2 1 
ATOM   4540 N  N   . THR   B 1 210 ? 5.973   -5.455  8.61    1   36.94 ? 195 THR   B N   1 
ATOM   4541 C  CA  . THR   B 1 210 ? 7.391   -5.494  8.271   1   37.11 ? 195 THR   B CA  1 
ATOM   4542 C  C   . THR   B 1 210 ? 7.567   -5.26   6.759   1   36.61 ? 195 THR   B C   1 
ATOM   4543 O  O   . THR   B 1 210 ? 8.455   -4.502  6.35    1   37.02 ? 195 THR   B O   1 
ATOM   4544 C  CB  . THR   B 1 210 ? 8.001   -6.822  8.702   1   38.61 ? 195 THR   B CB  1 
ATOM   4545 O  OG1 . THR   B 1 210 ? 7.808   -6.969  10.107  1   40.92 ? 195 THR   B OG1 1 
ATOM   4546 C  CG2 . THR   B 1 210 ? 9.505   -6.906  8.394   1   38.41 ? 195 THR   B CG2 1 
ATOM   4547 N  N   . LEU   B 1 211 ? 6.72    -5.895  5.945   1   35.34 ? 196 LEU   B N   1 
ATOM   4548 C  CA  . LEU   B 1 211 ? 6.77    -5.757  4.496   1   35.47 ? 196 LEU   B CA  1 
ATOM   4549 C  C   . LEU   B 1 211 ? 6.489   -4.326  4.06    1   36.1  ? 196 LEU   B C   1 
ATOM   4550 O  O   . LEU   B 1 211 ? 7.215   -3.77   3.226   1   36.14 ? 196 LEU   B O   1 
ATOM   4551 C  CB  . LEU   B 1 211 ? 5.807   -6.724  3.817   1   34.92 ? 196 LEU   B CB  1 
ATOM   4552 C  CG  . LEU   B 1 211 ? 5.747   -6.65   2.289   1   35.67 ? 196 LEU   B CG  1 
ATOM   4553 C  CD1 . LEU   B 1 211 ? 7.123   -6.9    1.661   1   35.79 ? 196 LEU   B CD1 1 
ATOM   4554 C  CD2 . LEU   B 1 211 ? 4.747   -7.651  1.75    1   35.72 ? 196 LEU   B CD2 1 
ATOM   4555 N  N   . LEU   B 1 212 ? 5.482   -3.697  4.653   1   36.13 ? 197 LEU   B N   1 
ATOM   4556 C  CA  . LEU   B 1 212 ? 5.139   -2.316  4.328   1   37.03 ? 197 LEU   B CA  1 
ATOM   4557 C  C   . LEU   B 1 212 ? 6.321   -1.386  4.624   1   37.49 ? 197 LEU   B C   1 
ATOM   4558 O  O   . LEU   B 1 212 ? 6.683   -0.566  3.782   1   38.13 ? 197 LEU   B O   1 
ATOM   4559 C  CB  . LEU   B 1 212 ? 3.892   -1.882  5.121   1   37.91 ? 197 LEU   B CB  1 
ATOM   4560 C  CG  . LEU   B 1 212 ? 3.204   -0.603  4.638   1   40.82 ? 197 LEU   B CG  1 
ATOM   4561 C  CD1 . LEU   B 1 212 ? 1.746   -0.583  5.067   1   41.45 ? 197 LEU   B CD1 1 
ATOM   4562 C  CD2 . LEU   B 1 212 ? 3.862   0.61    5.225   1   41.71 ? 197 LEU   B CD2 1 
ATOM   4563 N  N   . LYS   B 1 213 ? 6.923   -1.537  5.804   1   37.55 ? 198 LYS   B N   1 
ATOM   4564 C  CA  . LYS   B 1 213 ? 8.061   -0.72   6.212   1   38.83 ? 198 LYS   B CA  1 
ATOM   4565 C  C   . LYS   B 1 213 ? 9.256   -0.958  5.275   1   38.71 ? 198 LYS   B C   1 
ATOM   4566 O  O   . LYS   B 1 213 ? 9.931   -0.013  4.898   1   39.22 ? 198 LYS   B O   1 
ATOM   4567 C  CB  . LYS   B 1 213 ? 8.435   -1.028  7.661   1   41.81 ? 198 LYS   B CB  1 
ATOM   4568 C  CG  . LYS   B 1 213 ? 9.623   -0.227  8.166   1   48.6  ? 198 LYS   B CG  1 
ATOM   4569 C  CD  . LYS   B 1 213 ? 10.113  -0.721  9.522   1   55.56 ? 198 LYS   B CD  1 
ATOM   4570 C  CE  . LYS   B 1 213 ? 11.22   0.167   10.067  1   60.79 ? 198 LYS   B CE  1 
ATOM   4571 N  NZ  . LYS   B 1 213 ? 11.397  -0.003  11.538  1   64.03 ? 198 LYS   B NZ  1 
ATOM   4572 N  N   . ALA   B 1 214 ? 9.473   -2.205  4.852   1   37.8  ? 199 ALA   B N   1 
ATOM   4573 C  CA  . ALA   B 1 214 ? 10.571  -2.545  3.945   1   37.49 ? 199 ALA   B CA  1 
ATOM   4574 C  C   . ALA   B 1 214 ? 10.391  -1.888  2.576   1   37.34 ? 199 ALA   B C   1 
ATOM   4575 O  O   . ALA   B 1 214 ? 11.336  -1.273  2.074   1   37.58 ? 199 ALA   B O   1 
ATOM   4576 C  CB  . ALA   B 1 214 ? 10.693  -4.054  3.812   1   37.07 ? 199 ALA   B CB  1 
ATOM   4577 N  N   . LEU   B 1 215 ? 9.17    -1.943  2.013   1   36.88 ? 200 LEU   B N   1 
ATOM   4578 C  CA  . LEU   B 1 215 ? 8.865   -1.31   0.738   1   37.59 ? 200 LEU   B CA  1 
ATOM   4579 C  C   . LEU   B 1 215 ? 9.068   0.213   0.794   1   39.31 ? 200 LEU   B C   1 
ATOM   4580 O  O   . LEU   B 1 215 ? 9.606   0.8     -0.161  1   39.75 ? 200 LEU   B O   1 
ATOM   4581 C  CB  . LEU   B 1 215 ? 7.443   -1.663  0.288   1   37.4  ? 200 LEU   B CB  1 
ATOM   4582 C  CG  . LEU   B 1 215 ? 7.268   -3.123  -0.164  1   38.88 ? 200 LEU   B CG  1 
ATOM   4583 C  CD1 . LEU   B 1 215 ? 5.813   -3.436  -0.447  1   39.49 ? 200 LEU   B CD1 1 
ATOM   4584 C  CD2 . LEU   B 1 215 ? 8.144   -3.44   -1.361  1   39.04 ? 200 LEU   B CD2 1 
ATOM   4585 N  N   . LEU   B 1 216 ? 8.694   0.845   1.933   1   39.34 ? 201 LEU   B N   1 
ATOM   4586 C  CA  . LEU   B 1 216 ? 8.877   2.291   2.101   1   39.84 ? 201 LEU   B CA  1 
ATOM   4587 C  C   . LEU   B 1 216 ? 10.369  2.665   2.174   1   39.14 ? 201 LEU   B C   1 
ATOM   4588 O  O   . LEU   B 1 216 ? 10.742  3.728   1.7     1   39.2  ? 201 LEU   B O   1 
ATOM   4589 C  CB  . LEU   B 1 216 ? 8.11    2.824   3.328   1   40.17 ? 201 LEU   B CB  1 
ATOM   4590 C  CG  . LEU   B 1 216 ? 6.595   2.803   3.231   1   42.47 ? 201 LEU   B CG  1 
ATOM   4591 C  CD1 . LEU   B 1 216 ? 5.957   3.374   4.523   1   43.43 ? 201 LEU   B CD1 1 
ATOM   4592 C  CD2 . LEU   B 1 216 ? 6.111   3.604   2.018   1   43.5  ? 201 LEU   B CD2 1 
ATOM   4593 N  N   A GLU   B 1 217 ? 11.205  1.81    2.773   0.5 38.76 ? 202 GLU   B N   1 
ATOM   4594 N  N   B GLU   B 1 217 ? 11.193  1.793   2.768   0.5 38.87 ? 202 GLU   B N   1 
ATOM   4595 C  CA  A GLU   B 1 217 ? 12.637  2.08    2.841   0.5 39.12 ? 202 GLU   B CA  1 
ATOM   4596 C  CA  B GLU   B 1 217 ? 12.636  1.977   2.889   0.5 39.33 ? 202 GLU   B CA  1 
ATOM   4597 C  C   A GLU   B 1 217 ? 13.279  1.942   1.453   0.5 39.39 ? 202 GLU   B C   1 
ATOM   4598 C  C   B GLU   B 1 217 ? 13.327  1.852   1.516   0.5 39.51 ? 202 GLU   B C   1 
ATOM   4599 O  O   A GLU   B 1 217 ? 14.118  2.767   1.089   0.5 39.83 ? 202 GLU   B O   1 
ATOM   4600 O  O   B GLU   B 1 217 ? 14.298  2.559   1.252   0.5 40.01 ? 202 GLU   B O   1 
ATOM   4601 C  CB  A GLU   B 1 217 ? 13.333  1.204   3.893   0.5 41.01 ? 202 GLU   B CB  1 
ATOM   4602 C  CB  B GLU   B 1 217 ? 13.215  0.965   3.887   0.5 41.56 ? 202 GLU   B CB  1 
ATOM   4603 C  CG  A GLU   B 1 217 ? 14.848  1.358   3.95    0.5 45.71 ? 202 GLU   B CG  1 
ATOM   4604 C  CG  B GLU   B 1 217 ? 14.655  1.252   4.274   0.5 47.1  ? 202 GLU   B CG  1 
ATOM   4605 C  CD  A GLU   B 1 217 ? 15.434  2.748   4.148   0.5 50.85 ? 202 GLU   B CD  1 
ATOM   4606 C  CD  B GLU   B 1 217 ? 15.191  0.402   5.408   0.5 53.6  ? 202 GLU   B CD  1 
ATOM   4607 O  OE1 A GLU   B 1 217 ? 14.699  3.661   4.591   0.5 52.49 ? 202 GLU   B OE1 1 
ATOM   4608 O  OE1 B GLU   B 1 217 ? 14.373  -0.086  6.22    0.5 53.95 ? 202 GLU   B OE1 1 
ATOM   4609 O  OE2 A GLU   B 1 217 ? 16.641  2.919   3.859   0.5 51.09 ? 202 GLU   B OE2 1 
ATOM   4610 O  OE2 B GLU   B 1 217 ? 16.431  0.235   5.493   0.5 56.32 ? 202 GLU   B OE2 1 
ATOM   4611 N  N   . ILE   B 1 218 ? 12.811  0.981   0.641   1   38.74 ? 203 ILE   B N   1 
ATOM   4612 C  CA  . ILE   B 1 218 ? 13.338  0.815   -0.711  1   38.61 ? 203 ILE   B CA  1 
ATOM   4613 C  C   . ILE   B 1 218 ? 12.962  2.043   -1.552  1   39.58 ? 203 ILE   B C   1 
ATOM   4614 O  O   . ILE   B 1 218 ? 13.806  2.577   -2.267  1   40.09 ? 203 ILE   B O   1 
ATOM   4615 C  CB  . ILE   B 1 218 ? 12.846  -0.502  -1.342  1   37.44 ? 203 ILE   B CB  1 
ATOM   4616 C  CG1 . ILE   B 1 218 ? 13.527  -1.693  -0.646  1   38.11 ? 203 ILE   B CG1 1 
ATOM   4617 C  CG2 . ILE   B 1 218 ? 13.079  -0.513  -2.877  1   36.54 ? 203 ILE   B CG2 1 
ATOM   4618 C  CD1 . ILE   B 1 218 ? 12.9    -3.022  -0.976  1   39.51 ? 203 ILE   B CD1 1 
ATOM   4619 N  N   . ALA   B 1 219 ? 11.729  2.536   -1.405  1   39.46 ? 204 ALA   B N   1 
ATOM   4620 C  CA  . ALA   B 1 219 ? 11.288  3.727   -2.12   1   39.98 ? 204 ALA   B CA  1 
ATOM   4621 C  C   . ALA   B 1 219 ? 12.156  4.94    -1.706  1   41.21 ? 204 ALA   B C   1 
ATOM   4622 O  O   . ALA   B 1 219 ? 12.609  5.704   -2.555  1   40.86 ? 204 ALA   B O   1 
ATOM   4623 C  CB  . ALA   B 1 219 ? 9.815   3.992   -1.842  1   39.11 ? 204 ALA   B CB  1 
ATOM   4624 N  N   . SER   B 1 220 ? 12.454  5.042   -0.42   1   41.92 ? 205 SER   B N   1 
ATOM   4625 C  CA  . SER   B 1 220 ? 13.289  6.094   0.119   1   43.79 ? 205 SER   B CA  1 
ATOM   4626 C  C   . SER   B 1 220 ? 14.706  6.034   -0.485  1   44.09 ? 205 SER   B C   1 
ATOM   4627 O  O   . SER   B 1 220 ? 15.231  7.071   -0.851  1   44.56 ? 205 SER   B O   1 
ATOM   4628 C  CB  . SER   B 1 220 ? 13.339  5.98    1.642   1   46.6  ? 205 SER   B CB  1 
ATOM   4629 O  OG  . SER   B 1 220 ? 14.262  6.889   2.217   1   50.59 ? 205 SER   B OG  1 
ATOM   4630 N  N   . CYS   B 1 221 ? 15.301  4.832   -0.622  1   43.73 ? 206 CYS   B N   1 
ATOM   4631 C  CA  . CYS   B 1 221 ? 16.634  4.661   -1.208  1   43.89 ? 206 CYS   B CA  1 
ATOM   4632 C  C   . CYS   B 1 221 ? 16.641  5.08    -2.67   1   44.64 ? 206 CYS   B C   1 
ATOM   4633 O  O   . CYS   B 1 221 ? 17.582  5.749   -3.127  1   44.88 ? 206 CYS   B O   1 
ATOM   4634 C  CB  . CYS   B 1 221 ? 17.118  3.227   -1.048  1   44.76 ? 206 CYS   B CB  1 
ATOM   4635 S  SG  . CYS   B 1 221 ? 17.458  2.739   0.659   1   50.63 ? 206 CYS   B SG  1 
ATOM   4636 N  N   . LEU   B 1 222 ? 15.595  4.684   -3.413  1   44.06 ? 207 LEU   B N   1 
ATOM   4637 C  CA  . LEU   B 1 222 ? 15.482  5.036   -4.821  1   44.92 ? 207 LEU   B CA  1 
ATOM   4638 C  C   . LEU   B 1 222 ? 15.253  6.532   -5.042  1   46.15 ? 207 LEU   B C   1 
ATOM   4639 O  O   . LEU   B 1 222 ? 15.701  7.071   -6.052  1   45.74 ? 207 LEU   B O   1 
ATOM   4640 C  CB  . LEU   B 1 222 ? 14.408  4.194   -5.517  1   44.5  ? 207 LEU   B CB  1 
ATOM   4641 C  CG  . LEU   B 1 222 ? 14.659  2.692   -5.487  1   45.45 ? 207 LEU   B CG  1 
ATOM   4642 C  CD1 . LEU   B 1 222 ? 13.477  1.936   -6.038  1   45.59 ? 207 LEU   B CD1 1 
ATOM   4643 C  CD2 . LEU   B 1 222 ? 15.976  2.323   -6.179  1   46.03 ? 207 LEU   B CD2 1 
ATOM   4644 N  N   . GLU   B 1 223 ? 14.565  7.196   -4.095  1   46.84 ? 208 GLU   B N   1 
ATOM   4645 C  CA  . GLU   B 1 223 ? 14.325  8.643   -4.126  1   48.05 ? 208 GLU   B CA  1 
ATOM   4646 C  C   . GLU   B 1 223 ? 15.671  9.37    -3.904  1   48.66 ? 208 GLU   B C   1 
ATOM   4647 O  O   . GLU   B 1 223 ? 15.997  10.305  -4.632  1   48.84 ? 208 GLU   B O   1 
ATOM   4648 C  CB  . GLU   B 1 223 ? 13.282  9.049   -3.054  1   50.41 ? 208 GLU   B CB  1 
ATOM   4649 C  CG  . GLU   B 1 223 ? 11.842  8.709   -3.427  1   54.18 ? 208 GLU   B CG  1 
ATOM   4650 C  CD  . GLU   B 1 223 ? 10.859  8.52    -2.275  1   60.05 ? 208 GLU   B CD  1 
ATOM   4651 O  OE1 . GLU   B 1 223 ? 11.22   8.842   -1.115  1   60.2  ? 208 GLU   B OE1 1 
ATOM   4652 O  OE2 . GLU   B 1 223 ? 9.734   8.025   -2.536  1   60.11 ? 208 GLU   B OE2 1 
ATOM   4653 N  N   . LYS   B 1 224 ? 16.473  8.885   -2.95   1   49.26 ? 209 LYS   B N   1 
ATOM   4654 C  CA  . LYS   B 1 224 ? 17.796  9.422   -2.639  1   51.13 ? 209 LYS   B CA  1 
ATOM   4655 C  C   . LYS   B 1 224 ? 18.746  9.314   -3.858  1   52.57 ? 209 LYS   B C   1 
ATOM   4656 O  O   . LYS   B 1 224 ? 19.557  10.219  -4.099  1   53.44 ? 209 LYS   B O   1 
ATOM   4657 C  CB  . LYS   B 1 224 ? 18.407  8.638   -1.458  1   53.48 ? 209 LYS   B CB  1 
ATOM   4658 C  CG  . LYS   B 1 224 ? 18.151  9.19    -0.052  1   59.17 ? 209 LYS   B CG  1 
ATOM   4659 C  CD  . LYS   B 1 224 ? 16.729  9.703   0.247   1   65.58 ? 209 LYS   B CD  1 
ATOM   4660 C  CE  . LYS   B 1 224 ? 16.502  9.889   1.731   1   70.01 ? 209 LYS   B CE  1 
ATOM   4661 N  NZ  . LYS   B 1 224 ? 17.011  8.721   2.497   1   72.21 ? 209 LYS   B NZ  1 
ATOM   4662 N  N   . ALA   B 1 225 ? 18.658  8.198   -4.609  1   51.97 ? 210 ALA   B N   1 
ATOM   4663 C  CA  . ALA   B 1 225 ? 19.5    7.978   -5.772  1   52.01 ? 210 ALA   B CA  1 
ATOM   4664 C  C   . ALA   B 1 225 ? 19.224  8.988   -6.904  1   52.18 ? 210 ALA   B C   1 
ATOM   4665 O  O   . ALA   B 1 225 ? 20.126  9.279   -7.685  1   52.5  ? 210 ALA   B O   1 
ATOM   4666 C  CB  . ALA   B 1 225 ? 19.347  6.548   -6.275  1   51.68 ? 210 ALA   B CB  1 
ATOM   4667 N  N   . LEU   B 1 226 ? 18.006  9.534   -6.979  1   51.94 ? 211 LEU   B N   1 
ATOM   4668 C  CA  . LEU   B 1 226 ? 17.659  10.523  -8.003  1   52.78 ? 211 LEU   B CA  1 
ATOM   4669 C  C   . LEU   B 1 226 ? 18.421  11.829  -7.78   1   53.47 ? 211 LEU   B C   1 
ATOM   4670 O  O   . LEU   B 1 226 ? 18.883  12.449  -8.742  1   53.4  ? 211 LEU   B O   1 
ATOM   4671 C  CB  . LEU   B 1 226 ? 16.143  10.78   -8.026  1   52.86 ? 211 LEU   B CB  1 
ATOM   4672 C  CG  . LEU   B 1 226 ? 15.639  11.871  -8.974  1   54.53 ? 211 LEU   B CG  1 
ATOM   4673 C  CD1 . LEU   B 1 226 ? 16.039  11.589  -10.414 1   55.26 ? 211 LEU   B CD1 1 
ATOM   4674 C  CD2 . LEU   B 1 226 ? 14.136  11.993  -8.893  1   55.18 ? 211 LEU   B CD2 1 
ATOM   4675 N  N   . GLN   B 1 227 ? 18.588  12.222  -6.517  1   53.56 ? 212 GLN   B N   1 
ATOM   4676 C  CA  . GLN   B 1 227 ? 19.32   13.436  -6.19   1   54.64 ? 212 GLN   B CA  1 
ATOM   4677 C  C   . GLN   B 1 227 ? 20.784  13.316  -6.629  1   53.79 ? 212 GLN   B C   1 
ATOM   4678 O  O   . GLN   B 1 227 ? 21.321  14.242  -7.24   1   53.66 ? 212 GLN   B O   1 
ATOM   4679 C  CB  . GLN   B 1 227 ? 19.198  13.734  -4.684  1   57.74 ? 212 GLN   B CB  1 
ATOM   4680 C  CG  . GLN   B 1 227 ? 18.154  14.813  -4.353  1   63.51 ? 212 GLN   B CG  1 
ATOM   4681 C  CD  . GLN   B 1 227 ? 16.787  14.519  -4.926  1   70.4  ? 212 GLN   B CD  1 
ATOM   4682 O  OE1 . GLN   B 1 227 ? 16.246  15.268  -5.757  1   72.2  ? 212 GLN   B OE1 1 
ATOM   4683 N  NE2 . GLN   B 1 227 ? 16.208  13.404  -4.509  1   71.81 ? 212 GLN   B NE2 1 
ATOM   4684 N  N   . VAL   B 1 228 ? 21.383  12.135  -6.393  1   52.94 ? 213 VAL   B N   1 
ATOM   4685 C  CA  . VAL   B 1 228 ? 22.754  11.808  -6.771  1   52.76 ? 213 VAL   B CA  1 
ATOM   4686 C  C   . VAL   B 1 228 ? 22.959  11.965  -8.288  1   52.77 ? 213 VAL   B C   1 
ATOM   4687 O  O   . VAL   B 1 228 ? 23.996  12.451  -8.723  1   53.21 ? 213 VAL   B O   1 
ATOM   4688 C  CB  . VAL   B 1 228 ? 23.14   10.397  -6.264  1   53.2  ? 213 VAL   B CB  1 
ATOM   4689 C  CG1 . VAL   B 1 228 ? 24.483  9.956   -6.832  1   53.67 ? 213 VAL   B CG1 1 
ATOM   4690 C  CG2 . VAL   B 1 228 ? 23.159  10.354  -4.737  1   53.21 ? 213 VAL   B CG2 1 
ATOM   4691 N  N   . PHE   B 1 229 ? 21.946  11.619  -9.081  1   52.24 ? 214 PHE   B N   1 
ATOM   4692 C  CA  . PHE   B 1 229 ? 21.946  11.743  -10.536 1   52.52 ? 214 PHE   B CA  1 
ATOM   4693 C  C   . PHE   B 1 229 ? 22.145  13.188  -11.047 1   52.39 ? 214 PHE   B C   1 
ATOM   4694 O  O   . PHE   B 1 229 ? 22.73   13.378  -12.12  1   52.04 ? 214 PHE   B O   1 
ATOM   4695 C  CB  . PHE   B 1 229 ? 20.594  11.277  -11.04  1   52.88 ? 214 PHE   B CB  1 
ATOM   4696 C  CG  . PHE   B 1 229 ? 20.619  10.265  -12.14  1   54.28 ? 214 PHE   B CG  1 
ATOM   4697 C  CD1 . PHE   B 1 229 ? 21.016  10.62   -13.412 1   55.21 ? 214 PHE   B CD1 1 
ATOM   4698 C  CD2 . PHE   B 1 229 ? 20.188  8.964   -11.917 1   55.51 ? 214 PHE   B CD2 1 
ATOM   4699 C  CE1 . PHE   B 1 229 ? 20.988  9.7     -14.437 1   56.02 ? 214 PHE   B CE1 1 
ATOM   4700 C  CE2 . PHE   B 1 229 ? 20.183  8.034   -12.942 1   55.99 ? 214 PHE   B CE2 1 
ATOM   4701 C  CZ  . PHE   B 1 229 ? 20.562  8.414   -14.198 1   55.84 ? 214 PHE   B CZ  1 
ATOM   4702 N  N   . HIS   B 1 230 ? 21.617  14.199  -10.305 1   51.85 ? 215 HIS   B N   1 
ATOM   4703 C  CA  . HIS   B 1 230 ? 21.664  15.619  -10.696 1   51.77 ? 215 HIS   B CA  1 
ATOM   4704 C  C   . HIS   B 1 230 ? 23.078  16.143  -10.984 1   50.43 ? 215 HIS   B C   1 
ATOM   4705 O  O   . HIS   B 1 230 ? 23.239  17.057  -11.789 1   49.57 ? 215 HIS   B O   1 
ATOM   4706 C  CB  . HIS   B 1 230 ? 20.977  16.519  -9.642  1   53.33 ? 215 HIS   B CB  1 
ATOM   4707 C  CG  . HIS   B 1 230 ? 19.518  16.239  -9.407  1   56.79 ? 215 HIS   B CG  1 
ATOM   4708 N  ND1 . HIS   B 1 230 ? 18.772  15.476  -10.288 1   59.01 ? 215 HIS   B ND1 1 
ATOM   4709 C  CD2 . HIS   B 1 230 ? 18.712  16.652  -8.398  1   58.33 ? 215 HIS   B CD2 1 
ATOM   4710 C  CE1 . HIS   B 1 230 ? 17.544  15.437  -9.785  1   59.71 ? 215 HIS   B CE1 1 
ATOM   4711 N  NE2 . HIS   B 1 230 ? 17.457  16.134  -8.651  1   59.58 ? 215 HIS   B NE2 1 
ATOM   4712 N  N   . GLN   B 1 231 ? 24.093  15.553  -10.32  1   49.91 ? 216 GLN   B N   1 
ATOM   4713 C  CA  . GLN   B 1 231 ? 25.505  15.911  -10.445 1   49.5  ? 216 GLN   B CA  1 
ATOM   4714 C  C   . GLN   B 1 231 ? 26.055  15.77   -11.842 1   49.1  ? 216 GLN   B C   1 
ATOM   4715 O  O   . GLN   B 1 231 ? 27.122  16.299  -12.107 1   48.33 ? 216 GLN   B O   1 
ATOM   4716 C  CB  . GLN   B 1 231 ? 26.37   15.02   -9.554  1   50.99 ? 216 GLN   B CB  1 
ATOM   4717 C  CG  . GLN   B 1 231 ? 26.067  15.093  -8.088  1   54.36 ? 216 GLN   B CG  1 
ATOM   4718 C  CD  . GLN   B 1 231 ? 26.953  14.095  -7.41   1   57.91 ? 216 GLN   B CD  1 
ATOM   4719 O  OE1 . GLN   B 1 231 ? 27.989  14.438  -6.849  1   58.18 ? 216 GLN   B OE1 1 
ATOM   4720 N  NE2 . GLN   B 1 231 ? 26.585  12.821  -7.486  1   59.27 ? 216 GLN   B NE2 1 
ATOM   4721 N  N   . ILE   B 1 232 ? 25.392  15.006  -12.719 1   49.28 ? 217 ILE   B N   1 
ATOM   4722 C  CA  . ILE   B 1 232 ? 25.876  14.775  -14.083 1   49.74 ? 217 ILE   B CA  1 
ATOM   4723 C  C   . ILE   B 1 232 ? 26.162  16.077  -14.838 1   50.04 ? 217 ILE   B C   1 
ATOM   4724 O  O   . ILE   B 1 232 ? 27.193  16.177  -15.507 1   49.95 ? 217 ILE   B O   1 
ATOM   4725 C  CB  . ILE   B 1 232 ? 24.91   13.845  -14.874 1   49.93 ? 217 ILE   B CB  1 
ATOM   4726 C  CG1 . ILE   B 1 232 ? 25.582  13.276  -16.141 1   50.65 ? 217 ILE   B CG1 1 
ATOM   4727 C  CG2 . ILE   B 1 232 ? 23.581  14.533  -15.197 1   50.39 ? 217 ILE   B CG2 1 
ATOM   4728 C  CD1 . ILE   B 1 232 ? 26.477  12.029  -15.858 1   51.35 ? 217 ILE   B CD1 1 
ATOM   4729 N  N   . HIS   B 1 233 ? 25.273  17.085  -14.679 1   50.21 ? 218 HIS   B N   1 
ATOM   4730 C  CA  . HIS   B 1 233 ? 25.363  18.39   -15.345 1   50.41 ? 218 HIS   B CA  1 
ATOM   4731 C  C   . HIS   B 1 233 ? 26.614  19.167  -14.96  1   51.12 ? 218 HIS   B C   1 
ATOM   4732 O  O   . HIS   B 1 233 ? 27.158  19.888  -15.787 1   51.49 ? 218 HIS   B O   1 
ATOM   4733 C  CB  . HIS   B 1 233 ? 24.108  19.228  -15.074 1   50.18 ? 218 HIS   B CB  1 
ATOM   4734 C  CG  . HIS   B 1 233 ? 22.837  18.511  -15.393 1   50.49 ? 218 HIS   B CG  1 
ATOM   4735 N  ND1 . HIS   B 1 233 ? 22.328  18.481  -16.679 1   51.85 ? 218 HIS   B ND1 1 
ATOM   4736 C  CD2 . HIS   B 1 233 ? 22      17.836  -14.574 1   51.21 ? 218 HIS   B CD2 1 
ATOM   4737 C  CE1 . HIS   B 1 233 ? 21.205  17.786  -16.601 1   52.29 ? 218 HIS   B CE1 1 
ATOM   4738 N  NE2 . HIS   B 1 233 ? 20.966  17.377  -15.353 1   52.1  ? 218 HIS   B NE2 1 
ATOM   4739 N  N   . ASP   B 1 234 ? 27.101  18.979  -13.731 1   51.2  ? 219 ASP   B N   1 
ATOM   4740 C  CA  . ASP   B 1 234 ? 28.294  19.678  -13.267 1   51.55 ? 219 ASP   B CA  1 
ATOM   4741 C  C   . ASP   B 1 234 ? 29.584  19.058  -13.741 1   51.53 ? 219 ASP   B C   1 
ATOM   4742 O  O   . ASP   B 1 234 ? 30.609  19.743  -13.732 1   51.92 ? 219 ASP   B O   1 
ATOM   4743 C  CB  . ASP   B 1 234 ? 28.314  19.727  -11.731 1   53.56 ? 219 ASP   B CB  1 
ATOM   4744 C  CG  . ASP   B 1 234 ? 27.127  20.463  -11.148 1   58.54 ? 219 ASP   B CG  1 
ATOM   4745 O  OD1 . ASP   B 1 234 ? 26.729  21.496  -11.724 1   58.68 ? 219 ASP   B OD1 1 
ATOM   4746 O  OD2 . ASP   B 1 234 ? 26.591  20.001  -10.121 1   61.77 ? 219 ASP   B OD2 1 
ATOM   4747 N  N   . HIS   B 1 235 ? 29.578  17.764  -14.106 1   50.98 ? 220 HIS   B N   1 
ATOM   4748 C  CA  . HIS   B 1 235 ? 30.84   17.087  -14.43  1   50.45 ? 220 HIS   B CA  1 
ATOM   4749 C  C   . HIS   B 1 235 ? 30.955  16.544  -15.854 1   49.95 ? 220 HIS   B C   1 
ATOM   4750 O  O   . HIS   B 1 235 ? 32.009  16.005  -16.221 1   50.43 ? 220 HIS   B O   1 
ATOM   4751 C  CB  . HIS   B 1 235 ? 31.103  15.984  -13.408 1   51.21 ? 220 HIS   B CB  1 
ATOM   4752 C  CG  . HIS   B 1 235 ? 30.976  16.467  -11.993 1   54.45 ? 220 HIS   B CG  1 
ATOM   4753 N  ND1 . HIS   B 1 235 ? 31.808  17.451  -11.489 1   56.69 ? 220 HIS   B ND1 1 
ATOM   4754 C  CD2 . HIS   B 1 235 ? 30.085  16.123  -11.039 1   55.64 ? 220 HIS   B CD2 1 
ATOM   4755 C  CE1 . HIS   B 1 235 ? 31.41   17.659  -10.245 1   57.15 ? 220 HIS   B CE1 1 
ATOM   4756 N  NE2 . HIS   B 1 235 ? 30.383  16.881  -9.926  1   57.05 ? 220 HIS   B NE2 1 
ATOM   4757 N  N   . VAL   B 1 236 ? 29.893  16.678  -16.656 1   48.7  ? 221 VAL   B N   1 
ATOM   4758 C  CA  . VAL   B 1 236 ? 29.929  16.204  -18.032 1   48.49 ? 221 VAL   B CA  1 
ATOM   4759 C  C   . VAL   B 1 236 ? 29.396  17.305  -18.929 1   48.49 ? 221 VAL   B C   1 
ATOM   4760 O  O   . VAL   B 1 236 ? 28.385  17.929  -18.592 1   48.89 ? 221 VAL   B O   1 
ATOM   4761 C  CB  . VAL   B 1 236 ? 29.123  14.883  -18.245 1   48.59 ? 221 VAL   B CB  1 
ATOM   4762 C  CG1 . VAL   B 1 236 ? 29.429  14.27   -19.611 1   48.81 ? 221 VAL   B CG1 1 
ATOM   4763 C  CG2 . VAL   B 1 236 ? 29.381  13.867  -17.131 1   48.19 ? 221 VAL   B CG2 1 
ATOM   4764 N  N   . ASN   B 1 237 ? 30.061  17.559  -20.064 1   47.98 ? 222 ASN   B N   1 
ATOM   4765 C  CA  . ASN   B 1 237 ? 29.546  18.535  -21.015 1   47.81 ? 222 ASN   B CA  1 
ATOM   4766 C  C   . ASN   B 1 237 ? 29.154  17.81   -22.302 1   46.12 ? 222 ASN   B C   1 
ATOM   4767 O  O   . ASN   B 1 237 ? 29.877  16.902  -22.755 1   45.36 ? 222 ASN   B O   1 
ATOM   4768 C  CB  . ASN   B 1 237 ? 30.492  19.713  -21.241 1   50.37 ? 222 ASN   B CB  1 
ATOM   4769 C  CG  . ASN   B 1 237 ? 31.713  19.389  -22.048 1   55.35 ? 222 ASN   B CG  1 
ATOM   4770 O  OD1 . ASN   B 1 237 ? 32.77   19.039  -21.497 1   59    ? 222 ASN   B OD1 1 
ATOM   4771 N  ND2 . ASN   B 1 237 ? 31.601  19.51   -23.366 1   54.64 ? 222 ASN   B ND2 1 
ATOM   4772 N  N   . PRO   B 1 238 ? 27.981  18.179  -22.864 1   45.22 ? 223 PRO   B N   1 
ATOM   4773 C  CA  . PRO   B 1 238 ? 27.466  17.476  -24.053 1   44.93 ? 223 PRO   B CA  1 
ATOM   4774 C  C   . PRO   B 1 238 ? 28.432  17.279  -25.22  1   44.98 ? 223 PRO   B C   1 
ATOM   4775 O  O   . PRO   B 1 238 ? 28.496  16.172  -25.75  1   45.12 ? 223 PRO   B O   1 
ATOM   4776 C  CB  . PRO   B 1 238 ? 26.256  18.32   -24.469 1   45.2  ? 223 PRO   B CB  1 
ATOM   4777 C  CG  . PRO   B 1 238 ? 25.778  18.937  -23.207 1   45.9  ? 223 PRO   B CG  1 
ATOM   4778 C  CD  . PRO   B 1 238 ? 27.011  19.186  -22.373 1   44.54 ? 223 PRO   B CD  1 
ATOM   4779 N  N   . LYS   B 1 239 ? 29.172  18.329  -25.623 1   44.83 ? 224 LYS   B N   1 
ATOM   4780 C  CA  . LYS   B 1 239 ? 30.096  18.26   -26.754 1   44.92 ? 224 LYS   B CA  1 
ATOM   4781 C  C   . LYS   B 1 239 ? 31.172  17.184  -26.589 1   44.21 ? 224 LYS   B C   1 
ATOM   4782 O  O   . LYS   B 1 239 ? 31.333  16.329  -27.471 1   44.77 ? 224 LYS   B O   1 
ATOM   4783 C  CB  . LYS   B 1 239 ? 30.744  19.647  -27.024 1   47.46 ? 224 LYS   B CB  1 
ATOM   4784 N  N   . ALA   B 1 240 ? 31.907  17.228  -25.473 1   43.19 ? 225 ALA   B N   1 
ATOM   4785 C  CA  . ALA   B 1 240 ? 32.992  16.287  -25.213 1   42.8  ? 225 ALA   B CA  1 
ATOM   4786 C  C   . ALA   B 1 240 ? 32.47   14.875  -25.05  1   42.41 ? 225 ALA   B C   1 
ATOM   4787 O  O   . ALA   B 1 240 ? 33.07   13.937  -25.573 1   42.31 ? 225 ALA   B O   1 
ATOM   4788 C  CB  . ALA   B 1 240 ? 33.761  16.705  -23.981 1   42.58 ? 225 ALA   B CB  1 
ATOM   4789 N  N   . PHE   B 1 241 ? 31.344  14.713  -24.351 1   42.31 ? 226 PHE   B N   1 
ATOM   4790 C  CA  . PHE   B 1 241 ? 30.747  13.382  -24.169 1   42.15 ? 226 PHE   B CA  1 
ATOM   4791 C  C   . PHE   B 1 241 ? 30.344  12.779  -25.529 1   42.19 ? 226 PHE   B C   1 
ATOM   4792 O  O   . PHE   B 1 241 ? 30.675  11.629  -25.833 1   41.06 ? 226 PHE   B O   1 
ATOM   4793 C  CB  . PHE   B 1 241 ? 29.512  13.464  -23.233 1   41.6  ? 226 PHE   B CB  1 
ATOM   4794 C  CG  . PHE   B 1 241 ? 28.763  12.152  -23.169 1   41.99 ? 226 PHE   B CG  1 
ATOM   4795 C  CD1 . PHE   B 1 241 ? 29.197  11.13   -22.34  1   42.86 ? 226 PHE   B CD1 1 
ATOM   4796 C  CD2 . PHE   B 1 241 ? 27.683  11.91   -24.005 1   42.29 ? 226 PHE   B CD2 1 
ATOM   4797 C  CE1 . PHE   B 1 241 ? 28.543  9.904   -22.321 1   43.5  ? 226 PHE   B CE1 1 
ATOM   4798 C  CE2 . PHE   B 1 241 ? 27.042  10.682  -23.996 1   43.19 ? 226 PHE   B CE2 1 
ATOM   4799 C  CZ  . PHE   B 1 241 ? 27.466  9.693   -23.142 1   43.19 ? 226 PHE   B CZ  1 
ATOM   4800 N  N   . PHE   B 1 242 ? 29.575  13.547  -26.322 1   42.94 ? 227 PHE   B N   1 
ATOM   4801 C  CA  . PHE   B 1 242 ? 29.064  13.041  -27.588 1   43.47 ? 227 PHE   B CA  1 
ATOM   4802 C  C   . PHE   B 1 242 ? 30.16   12.791  -28.627 1   44.68 ? 227 PHE   B C   1 
ATOM   4803 O  O   . PHE   B 1 242 ? 30.171  11.728  -29.25  1   44.6  ? 227 PHE   B O   1 
ATOM   4804 C  CB  . PHE   B 1 242 ? 27.952  13.952  -28.151 1   42.57 ? 227 PHE   B CB  1 
ATOM   4805 C  CG  . PHE   B 1 242 ? 27.406  13.473  -29.478 1   42.51 ? 227 PHE   B CG  1 
ATOM   4806 C  CD1 . PHE   B 1 242 ? 26.471  12.454  -29.534 1   43.3  ? 227 PHE   B CD1 1 
ATOM   4807 C  CD2 . PHE   B 1 242 ? 27.849  14.025  -30.67  1   42.81 ? 227 PHE   B CD2 1 
ATOM   4808 C  CE1 . PHE   B 1 242 ? 25.98   12.007  -30.765 1   44.11 ? 227 PHE   B CE1 1 
ATOM   4809 C  CE2 . PHE   B 1 242 ? 27.39   13.55   -31.894 1   43.24 ? 227 PHE   B CE2 1 
ATOM   4810 C  CZ  . PHE   B 1 242 ? 26.468  12.538  -31.937 1   43.09 ? 227 PHE   B CZ  1 
ATOM   4811 N  N   . SER   B 1 243 ? 31.047  13.765  -28.835 1   45.12 ? 228 SER   B N   1 
ATOM   4812 C  CA  . SER   B 1 243 ? 32.043  13.649  -29.895 1   46.02 ? 228 SER   B CA  1 
ATOM   4813 C  C   . SER   B 1 243 ? 33.295  12.875  -29.507 1   46.79 ? 228 SER   B C   1 
ATOM   4814 O  O   . SER   B 1 243 ? 33.96   12.337  -30.395 1   47.25 ? 228 SER   B O   1 
ATOM   4815 C  CB  . SER   B 1 243 ? 32.406  15.025  -30.454 1   47.58 ? 228 SER   B CB  1 
ATOM   4816 O  OG  . SER   B 1 243 ? 32.933  15.87   -29.445 1   50.06 ? 228 SER   B OG  1 
ATOM   4817 N  N   . VAL   B 1 244 ? 33.61   12.777  -28.2   1   46.7  ? 229 VAL   B N   1 
ATOM   4818 C  CA  . VAL   B 1 244 ? 34.823  12.082  -27.781 1   46.4  ? 229 VAL   B CA  1 
ATOM   4819 C  C   . VAL   B 1 244 ? 34.555  10.786  -26.976 1   44.9  ? 229 VAL   B C   1 
ATOM   4820 O  O   . VAL   B 1 244 ? 34.861  9.699   -27.473 1   44.92 ? 229 VAL   B O   1 
ATOM   4821 C  CB  . VAL   B 1 244 ? 35.793  13.038  -27.04  1   47.74 ? 229 VAL   B CB  1 
ATOM   4822 C  CG1 . VAL   B 1 244 ? 37.065  12.301  -26.615 1   48.68 ? 229 VAL   B CG1 1 
ATOM   4823 C  CG2 . VAL   B 1 244 ? 36.111  14.274  -27.886 1   48.49 ? 229 VAL   B CG2 1 
ATOM   4824 N  N   . LEU   B 1 245 ? 33.987  10.879  -25.763 1   43.21 ? 230 LEU   B N   1 
ATOM   4825 C  CA  . LEU   B 1 245 ? 33.801  9.708   -24.915 1   42.06 ? 230 LEU   B CA  1 
ATOM   4826 C  C   . LEU   B 1 245 ? 32.982  8.6     -25.557 1   41.3  ? 230 LEU   B C   1 
ATOM   4827 O  O   . LEU   B 1 245 ? 33.387  7.444   -25.497 1   41.51 ? 230 LEU   B O   1 
ATOM   4828 C  CB  . LEU   B 1 245 ? 33.218  10.102  -23.542 1   42.05 ? 230 LEU   B CB  1 
ATOM   4829 C  CG  . LEU   B 1 245 ? 33.316  9.016   -22.457 1   43.5  ? 230 LEU   B CG  1 
ATOM   4830 C  CD1 . LEU   B 1 245 ? 34.764  8.552   -22.24  1   43.76 ? 230 LEU   B CD1 1 
ATOM   4831 C  CD2 . LEU   B 1 245 ? 32.709  9.493   -21.156 1   43.94 ? 230 LEU   B CD2 1 
ATOM   4832 N  N   . ARG   B 1 246 ? 31.845  8.948   -26.172 1   40.23 ? 231 ARG   B N   1 
ATOM   4833 C  CA  . ARG   B 1 246 ? 30.944  8.006   -26.842 1   40.14 ? 231 ARG   B CA  1 
ATOM   4834 C  C   . ARG   B 1 246 ? 31.66   7.107   -27.872 1   39.37 ? 231 ARG   B C   1 
ATOM   4835 O  O   . ARG   B 1 246 ? 31.368  5.919   -27.946 1   39.16 ? 231 ARG   B O   1 
ATOM   4836 C  CB  . ARG   B 1 246 ? 29.781  8.794   -27.492 1   41.47 ? 231 ARG   B CB  1 
ATOM   4837 C  CG  . ARG   B 1 246 ? 28.709  7.947   -28.165 1   45.78 ? 231 ARG   B CG  1 
ATOM   4838 C  CD  . ARG   B 1 246 ? 27.664  8.82    -28.86  1   49.6  ? 231 ARG   B CD  1 
ATOM   4839 N  NE  . ARG   B 1 246 ? 28.278  9.702   -29.863 1   53.06 ? 231 ARG   B NE  1 
ATOM   4840 C  CZ  . ARG   B 1 246 ? 28.447  9.384   -31.144 1   55.25 ? 231 ARG   B CZ  1 
ATOM   4841 N  NH1 . ARG   B 1 246 ? 28.02   8.217   -31.607 1   55.86 ? 231 ARG   B NH1 1 
ATOM   4842 N  NH2 . ARG   B 1 246 ? 29.024  10.241  -31.976 1   55.03 ? 231 ARG   B NH2 1 
ATOM   4843 N  N   . ILE   B 1 247 ? 32.608  7.665   -28.648 1   39.11 ? 232 ILE   B N   1 
ATOM   4844 C  CA  . ILE   B 1 247 ? 33.358  6.896   -29.648 1   40.13 ? 232 ILE   B CA  1 
ATOM   4845 C  C   . ILE   B 1 247 ? 34.181  5.764   -29.018 1   38.9  ? 232 ILE   B C   1 
ATOM   4846 O  O   . ILE   B 1 247 ? 34.164  4.651   -29.529 1   38.39 ? 232 ILE   B O   1 
ATOM   4847 C  CB  . ILE   B 1 247 ? 34.253  7.834   -30.527 1   42.62 ? 232 ILE   B CB  1 
ATOM   4848 C  CG1 . ILE   B 1 247 ? 33.43   8.945   -31.216 1   44.62 ? 232 ILE   B CG1 1 
ATOM   4849 C  CG2 . ILE   B 1 247 ? 35.111  7.058   -31.52  1   43.34 ? 232 ILE   B CG2 1 
ATOM   4850 C  CD1 . ILE   B 1 247 ? 32.47   8.462   -32.308 1   46.37 ? 232 ILE   B CD1 1 
ATOM   4851 N  N   . TYR   B 1 248 ? 34.91   6.04    -27.928 1   38.74 ? 233 TYR   B N   1 
ATOM   4852 C  CA  . TYR   B 1 248 ? 35.747  5.026   -27.285 1   39.33 ? 233 TYR   B CA  1 
ATOM   4853 C  C   . TYR   B 1 248 ? 34.977  3.914   -26.613 1   39.87 ? 233 TYR   B C   1 
ATOM   4854 O  O   . TYR   B 1 248 ? 35.525  2.816   -26.422 1   40.2  ? 233 TYR   B O   1 
ATOM   4855 C  CB  . TYR   B 1 248 ? 36.727  5.673   -26.296 1   39.71 ? 233 TYR   B CB  1 
ATOM   4856 C  CG  . TYR   B 1 248 ? 37.807  6.408   -27.044 1   40.41 ? 233 TYR   B CG  1 
ATOM   4857 C  CD1 . TYR   B 1 248 ? 38.849  5.719   -27.65  1   40.75 ? 233 TYR   B CD1 1 
ATOM   4858 C  CD2 . TYR   B 1 248 ? 37.712  7.775   -27.27  1   41.54 ? 233 TYR   B CD2 1 
ATOM   4859 C  CE1 . TYR   B 1 248 ? 39.815  6.383   -28.397 1   41.64 ? 233 TYR   B CE1 1 
ATOM   4860 C  CE2 . TYR   B 1 248 ? 38.659  8.448   -28.028 1   42.51 ? 233 TYR   B CE2 1 
ATOM   4861 C  CZ  . TYR   B 1 248 ? 39.712  7.745   -28.587 1   43.4  ? 233 TYR   B CZ  1 
ATOM   4862 O  OH  . TYR   B 1 248 ? 40.664  8.407   -29.319 1   45.72 ? 233 TYR   B OH  1 
ATOM   4863 N  N   . LEU   B 1 249 ? 33.711  4.184   -26.239 1   39.3  ? 234 LEU   B N   1 
ATOM   4864 C  CA  . LEU   B 1 249 ? 32.902  3.177   -25.554 1   39.61 ? 234 LEU   B CA  1 
ATOM   4865 C  C   . LEU   B 1 249 ? 32.081  2.289   -26.512 1   39.62 ? 234 LEU   B C   1 
ATOM   4866 O  O   . LEU   B 1 249 ? 31.374  1.403   -26.044 1   39.67 ? 234 LEU   B O   1 
ATOM   4867 C  CB  . LEU   B 1 249 ? 32.02   3.853   -24.483 1   39.68 ? 234 LEU   B CB  1 
ATOM   4868 C  CG  . LEU   B 1 249 ? 32.82   4.618   -23.427 1   41.27 ? 234 LEU   B CG  1 
ATOM   4869 C  CD1 . LEU   B 1 249 ? 31.925  5.463   -22.537 1   42.02 ? 234 LEU   B CD1 1 
ATOM   4870 C  CD2 . LEU   B 1 249 ? 33.684  3.671   -22.61  1   42.25 ? 234 LEU   B CD2 1 
ATOM   4871 N  N   . SER   B 1 250 ? 32.229  2.466   -27.845 1   38.98 ? 235 SER   B N   1 
ATOM   4872 C  CA  . SER   B 1 250 ? 31.533  1.618   -28.803 1   38.92 ? 235 SER   B CA  1 
ATOM   4873 C  C   . SER   B 1 250 ? 32.084  0.224   -28.832 1   38.54 ? 235 SER   B C   1 
ATOM   4874 O  O   . SER   B 1 250 ? 33.288  0.024   -28.674 1   38.71 ? 235 SER   B O   1 
ATOM   4875 C  CB  . SER   B 1 250 ? 31.656  2.176   -30.211 1   40.64 ? 235 SER   B CB  1 
ATOM   4876 O  OG  . SER   B 1 250 ? 31.04   3.444   -30.257 1   44.28 ? 235 SER   B OG  1 
ATOM   4877 N  N   . GLY   B 1 251 ? 31.209  -0.728  -29.102 1   37.63 ? 236 GLY   B N   1 
ATOM   4878 C  CA  . GLY   B 1 251 ? 31.608  -2.105  -29.249 1   38.2  ? 236 GLY   B CA  1 
ATOM   4879 C  C   . GLY   B 1 251 ? 31.608  -2.523  -30.706 1   39.08 ? 236 GLY   B C   1 
ATOM   4880 O  O   . GLY   B 1 251 ? 31.646  -1.691  -31.621 1   39.02 ? 236 GLY   B O   1 
ATOM   4881 N  N   . TRP   B 1 252 ? 31.575  -3.819  -30.923 1   39.22 ? 237 TRP   B N   1 
ATOM   4882 C  CA  . TRP   B 1 252 ? 31.614  -4.363  -32.272 1   39.48 ? 237 TRP   B CA  1 
ATOM   4883 C  C   . TRP   B 1 252 ? 30.566  -5.442  -32.448 1   41.14 ? 237 TRP   B C   1 
ATOM   4884 O  O   . TRP   B 1 252 ? 30.904  -6.573  -32.73  1   41.95 ? 237 TRP   B O   1 
ATOM   4885 C  CB  . TRP   B 1 252 ? 33.036  -4.831  -32.669 1   38.16 ? 237 TRP   B CB  1 
ATOM   4886 C  CG  . TRP   B 1 252 ? 33.913  -5.324  -31.543 1   36.85 ? 237 TRP   B CG  1 
ATOM   4887 C  CD1 . TRP   B 1 252 ? 34.04   -6.61   -31.098 1   36.88 ? 237 TRP   B CD1 1 
ATOM   4888 C  CD2 . TRP   B 1 252 ? 34.779  -4.526  -30.716 1   36.31 ? 237 TRP   B CD2 1 
ATOM   4889 N  NE1 . TRP   B 1 252 ? 34.938  -6.661  -30.055 1   36.83 ? 237 TRP   B NE1 1 
ATOM   4890 C  CE2 . TRP   B 1 252 ? 35.401  -5.395  -29.797 1   36.4  ? 237 TRP   B CE2 1 
ATOM   4891 C  CE3 . TRP   B 1 252 ? 35.06   -3.153  -30.639 1   36.71 ? 237 TRP   B CE3 1 
ATOM   4892 C  CZ2 . TRP   B 1 252 ? 36.29   -4.936  -28.816 1   36.91 ? 237 TRP   B CZ2 1 
ATOM   4893 C  CZ3 . TRP   B 1 252 ? 35.955  -2.706  -29.678 1   37.03 ? 237 TRP   B CZ3 1 
ATOM   4894 C  CH2 . TRP   B 1 252 ? 36.554  -3.589  -28.782 1   36.84 ? 237 TRP   B CH2 1 
ATOM   4895 N  N   . LYS   B 1 253 ? 29.299  -5.094  -32.244 1   41.62 ? 238 LYS   B N   1 
ATOM   4896 C  CA  . LYS   B 1 253 ? 28.186  -6.007  -32.455 1   43.21 ? 238 LYS   B CA  1 
ATOM   4897 C  C   . LYS   B 1 253 ? 27.16   -5.193  -33.202 1   44.99 ? 238 LYS   B C   1 
ATOM   4898 O  O   . LYS   B 1 253 ? 26.661  -4.209  -32.661 1   45.67 ? 238 LYS   B O   1 
ATOM   4899 C  CB  . LYS   B 1 253 ? 27.611  -6.511  -31.133 1   45.15 ? 238 LYS   B CB  1 
ATOM   4900 C  CG  . LYS   B 1 253 ? 26.596  -7.631  -31.337 1   49.88 ? 238 LYS   B CG  1 
ATOM   4901 C  CD  . LYS   B 1 253 ? 25.961  -8.042  -30.045 1   54.5  ? 238 LYS   B CD  1 
ATOM   4902 C  CE  . LYS   B 1 253 ? 24.809  -8.987  -30.277 1   60.38 ? 238 LYS   B CE  1 
ATOM   4903 N  NZ  . LYS   B 1 253 ? 25.276  -10.399 -30.348 1   64.49 ? 238 LYS   B NZ  1 
ATOM   4904 N  N   . GLY   B 1 254 ? 26.898  -5.551  -34.455 1   45.64 ? 239 GLY   B N   1 
ATOM   4905 C  CA  . GLY   B 1 254 ? 26.01   -4.768  -35.297 1   46.69 ? 239 GLY   B CA  1 
ATOM   4906 C  C   . GLY   B 1 254 ? 26.589  -3.394  -35.596 1   48.15 ? 239 GLY   B C   1 
ATOM   4907 O  O   . GLY   B 1 254 ? 25.846  -2.449  -35.856 1   48.71 ? 239 GLY   B O   1 
ATOM   4908 N  N   . ASN   B 1 255 ? 27.931  -3.262  -35.552 1   48.59 ? 240 ASN   B N   1 
ATOM   4909 C  CA  . ASN   B 1 255 ? 28.598  -1.999  -35.812 1   48.95 ? 240 ASN   B CA  1 
ATOM   4910 C  C   . ASN   B 1 255 ? 29.074  -1.979  -37.256 1   50.76 ? 240 ASN   B C   1 
ATOM   4911 O  O   . ASN   B 1 255 ? 29.945  -2.767  -37.618 1   51.13 ? 240 ASN   B O   1 
ATOM   4912 C  CB  . ASN   B 1 255 ? 29.779  -1.809  -34.861 1   48.05 ? 240 ASN   B CB  1 
ATOM   4913 C  CG  . ASN   B 1 255 ? 30.292  -0.392  -34.879 1   50.26 ? 240 ASN   B CG  1 
ATOM   4914 O  OD1 . ASN   B 1 255 ? 30.163  0.328   -35.881 1   51.53 ? 240 ASN   B OD1 1 
ATOM   4915 N  ND2 . ASN   B 1 255 ? 30.872  0.059   -33.774 1   49.55 ? 240 ASN   B ND2 1 
ATOM   4916 N  N   . PRO   B 1 256 ? 28.56   -1.044  -38.078 1   51.63 ? 241 PRO   B N   1 
ATOM   4917 C  CA  . PRO   B 1 256 ? 28.995  -0.98   -39.483 1   52.14 ? 241 PRO   B CA  1 
ATOM   4918 C  C   . PRO   B 1 256 ? 30.496  -0.759  -39.668 1   53.02 ? 241 PRO   B C   1 
ATOM   4919 O  O   . PRO   B 1 256 ? 31.037  -1.191  -40.687 1   53.22 ? 241 PRO   B O   1 
ATOM   4920 C  CB  . PRO   B 1 256 ? 28.173  0.174   -40.062 1   52.94 ? 241 PRO   B CB  1 
ATOM   4921 C  CG  . PRO   B 1 256 ? 26.999  0.318   -39.147 1   53.43 ? 241 PRO   B CG  1 
ATOM   4922 C  CD  . PRO   B 1 256 ? 27.513  -0.046  -37.786 1   51.53 ? 241 PRO   B CD  1 
ATOM   4923 N  N   . GLN   B 1 257 ? 31.18   -0.125  -38.685 1   53.05 ? 242 GLN   B N   1 
ATOM   4924 C  CA  . GLN   B 1 257 ? 32.633  0.069   -38.764 1   53.65 ? 242 GLN   B CA  1 
ATOM   4925 C  C   . GLN   B 1 257 ? 33.426  -1.238  -38.589 1   54.26 ? 242 GLN   B C   1 
ATOM   4926 O  O   . GLN   B 1 257 ? 34.57   -1.316  -39.018 1   54.13 ? 242 GLN   B O   1 
ATOM   4927 C  CB  . GLN   B 1 257 ? 33.107  1.116   -37.761 1   54.92 ? 242 GLN   B CB  1 
ATOM   4928 C  CG  . GLN   B 1 257 ? 32.393  2.437   -37.898 1   59.1  ? 242 GLN   B CG  1 
ATOM   4929 C  CD  . GLN   B 1 257 ? 33.129  3.564   -37.21  1   65.21 ? 242 GLN   B CD  1 
ATOM   4930 O  OE1 . GLN   B 1 257 ? 34.048  3.377   -36.402 1   67.21 ? 242 GLN   B OE1 1 
ATOM   4931 N  NE2 . GLN   B 1 257 ? 32.748  4.781   -37.525 1   66.44 ? 242 GLN   B NE2 1 
ATOM   4932 N  N   . LEU   B 1 258 ? 32.829  -2.244  -37.938 1   54.88 ? 243 LEU   B N   1 
ATOM   4933 C  CA  . LEU   B 1 258 ? 33.423  -3.558  -37.713 1   56.06 ? 243 LEU   B CA  1 
ATOM   4934 C  C   . LEU   B 1 258 ? 32.287  -4.573  -37.902 1   57.16 ? 243 LEU   B C   1 
ATOM   4935 O  O   . LEU   B 1 258 ? 31.939  -5.31   -36.981 1   57.6  ? 243 LEU   B O   1 
ATOM   4936 C  CB  . LEU   B 1 258 ? 33.997  -3.661  -36.287 1   56.44 ? 243 LEU   B CB  1 
ATOM   4937 C  CG  . LEU   B 1 258 ? 35.433  -3.249  -36.095 1   58.27 ? 243 LEU   B CG  1 
ATOM   4938 C  CD1 . LEU   B 1 258 ? 35.515  -1.808  -35.682 1   59.04 ? 243 LEU   B CD1 1 
ATOM   4939 C  CD2 . LEU   B 1 258 ? 36.085  -4.086  -35.028 1   59    ? 243 LEU   B CD2 1 
ATOM   4940 N  N   . SER   B 1 259 ? 31.691  -4.584  -39.106 1   57.47 ? 244 SER   B N   1 
ATOM   4941 C  CA  . SER   B 1 259 ? 30.53   -5.407  -39.467 1   58.2  ? 244 SER   B CA  1 
ATOM   4942 C  C   . SER   B 1 259 ? 30.622  -6.899  -39.101 1   57.78 ? 244 SER   B C   1 
ATOM   4943 O  O   . SER   B 1 259 ? 29.584  -7.505  -38.842 1   57.73 ? 244 SER   B O   1 
ATOM   4944 C  CB  . SER   B 1 259 ? 30.186  -5.251  -40.948 1   60.47 ? 244 SER   B CB  1 
ATOM   4945 O  OG  . SER   B 1 259 ? 31.287  -5.537  -41.798 1   63.57 ? 244 SER   B OG  1 
ATOM   4946 N  N   . ASP   B 1 260 ? 31.824  -7.487  -39.058 1   57.54 ? 245 ASP   B N   1 
ATOM   4947 C  CA  . ASP   B 1 260 ? 31.958  -8.912  -38.693 1   57.81 ? 245 ASP   B CA  1 
ATOM   4948 C  C   . ASP   B 1 260 ? 32.497  -9.159  -37.27  1   56.9  ? 245 ASP   B C   1 
ATOM   4949 O  O   . ASP   B 1 260 ? 32.584  -10.313 -36.828 1   57.1  ? 245 ASP   B O   1 
ATOM   4950 C  CB  . ASP   B 1 260 ? 32.852  -9.639  -39.711 1   60.75 ? 245 ASP   B CB  1 
ATOM   4951 C  CG  . ASP   B 1 260 ? 32.346  -9.509  -41.132 1   66.97 ? 245 ASP   B CG  1 
ATOM   4952 O  OD1 . ASP   B 1 260 ? 31.113  -9.622  -41.339 1   67.95 ? 245 ASP   B OD1 1 
ATOM   4953 O  OD2 . ASP   B 1 260 ? 33.175  -9.281  -42.034 1   69.99 ? 245 ASP   B OD2 1 
ATOM   4954 N  N   . GLY   B 1 261 ? 32.854  -8.089  -36.57  1   55.48 ? 246 GLY   B N   1 
ATOM   4955 C  CA  . GLY   B 1 261 ? 33.431  -8.196  -35.245 1   54.61 ? 246 GLY   B CA  1 
ATOM   4956 C  C   . GLY   B 1 261 ? 34.913  -7.897  -35.264 1   53.57 ? 246 GLY   B C   1 
ATOM   4957 O  O   . GLY   B 1 261 ? 35.429  -7.275  -36.198 1   53.14 ? 246 GLY   B O   1 
ATOM   4958 N  N   . LEU   B 1 262 ? 35.607  -8.34   -34.229 1   52.92 ? 247 LEU   B N   1 
ATOM   4959 C  CA  . LEU   B 1 262 ? 37.025  -8.07   -34.075 1   52.52 ? 247 LEU   B CA  1 
ATOM   4960 C  C   . LEU   B 1 262 ? 37.786  -9.365  -34.057 1   52.92 ? 247 LEU   B C   1 
ATOM   4961 O  O   . LEU   B 1 262 ? 37.336  -10.327 -33.435 1   52.91 ? 247 LEU   B O   1 
ATOM   4962 C  CB  . LEU   B 1 262 ? 37.24   -7.324  -32.743 1   52.27 ? 247 LEU   B CB  1 
ATOM   4963 C  CG  . LEU   B 1 262 ? 38.668  -6.921  -32.393 1   52.77 ? 247 LEU   B CG  1 
ATOM   4964 C  CD1 . LEU   B 1 262 ? 39.154  -5.805  -33.307 1   53.49 ? 247 LEU   B CD1 1 
ATOM   4965 C  CD2 . LEU   B 1 262 ? 38.784  -6.505  -30.922 1   52.68 ? 247 LEU   B CD2 1 
ATOM   4966 N  N   . VAL   B 1 263 ? 38.949  -9.401  -34.73  1   53.24 ? 248 VAL   B N   1 
ATOM   4967 C  CA  . VAL   B 1 263 ? 39.782  -10.593 -34.707 1   53.45 ? 248 VAL   B CA  1 
ATOM   4968 C  C   . VAL   B 1 263 ? 40.627  -10.55  -33.449 1   53.73 ? 248 VAL   B C   1 
ATOM   4969 O  O   . VAL   B 1 263 ? 41.357  -9.589  -33.242 1   53.49 ? 248 VAL   B O   1 
ATOM   4970 C  CB  . VAL   B 1 263 ? 40.65   -10.774 -35.985 1   53.75 ? 248 VAL   B CB  1 
ATOM   4971 C  CG1 . VAL   B 1 263 ? 41.532  -12.016 -35.862 1   54.2  ? 248 VAL   B CG1 1 
ATOM   4972 C  CG2 . VAL   B 1 263 ? 39.772  -10.866 -37.23  1   54.12 ? 248 VAL   B CG2 1 
ATOM   4973 N  N   . TYR   B 1 264 ? 40.499  -11.565 -32.589 1   54.67 ? 249 TYR   B N   1 
ATOM   4974 C  CA  . TYR   B 1 264 ? 41.292  -11.675 -31.368 1   56.28 ? 249 TYR   B CA  1 
ATOM   4975 C  C   . TYR   B 1 264 ? 42.424  -12.637 -31.734 1   58.68 ? 249 TYR   B C   1 
ATOM   4976 O  O   . TYR   B 1 264 ? 42.339  -13.84  -31.478 1   59.16 ? 249 TYR   B O   1 
ATOM   4977 C  CB  . TYR   B 1 264 ? 40.437  -12.219 -30.205 1   55.81 ? 249 TYR   B CB  1 
ATOM   4978 C  CG  . TYR   B 1 264 ? 39.395  -11.232 -29.712 1   55.97 ? 249 TYR   B CG  1 
ATOM   4979 C  CD1 . TYR   B 1 264 ? 38.121  -11.206 -30.259 1   56.35 ? 249 TYR   B CD1 1 
ATOM   4980 C  CD2 . TYR   B 1 264 ? 39.685  -10.33  -28.695 1   56.53 ? 249 TYR   B CD2 1 
ATOM   4981 C  CE1 . TYR   B 1 264 ? 37.162  -10.311 -29.808 1   56.95 ? 249 TYR   B CE1 1 
ATOM   4982 C  CE2 . TYR   B 1 264 ? 38.734  -9.43   -28.238 1   57.1  ? 249 TYR   B CE2 1 
ATOM   4983 C  CZ  . TYR   B 1 264 ? 37.473  -9.421  -28.801 1   57.83 ? 249 TYR   B CZ  1 
ATOM   4984 O  OH  . TYR   B 1 264 ? 36.526  -8.531  -28.358 1   59.35 ? 249 TYR   B OH  1 
ATOM   4985 N  N   . GLU   B 1 265 ? 43.446  -12.092 -32.415 1   59.72 ? 250 GLU   B N   1 
ATOM   4986 C  CA  . GLU   B 1 265 ? 44.573  -12.833 -32.973 1   60.88 ? 250 GLU   B CA  1 
ATOM   4987 C  C   . GLU   B 1 265 ? 45.222  -13.814 -32.015 1   61.95 ? 250 GLU   B C   1 
ATOM   4988 O  O   . GLU   B 1 265 ? 45.572  -13.454 -30.898 1   62.1  ? 250 GLU   B O   1 
ATOM   4989 C  CB  . GLU   B 1 265 ? 45.607  -11.862 -33.538 1   63.07 ? 250 GLU   B CB  1 
ATOM   4990 C  CG  . GLU   B 1 265 ? 46.705  -12.535 -34.337 1   66.91 ? 250 GLU   B CG  1 
ATOM   4991 C  CD  . GLU   B 1 265 ? 47.697  -11.531 -34.872 1   70.62 ? 250 GLU   B CD  1 
ATOM   4992 O  OE1 . GLU   B 1 265 ? 47.646  -11.252 -36.092 1   72.01 ? 250 GLU   B OE1 1 
ATOM   4993 O  OE2 . GLU   B 1 265 ? 48.503  -11.003 -34.069 1   70.63 ? 250 GLU   B OE2 1 
ATOM   4994 N  N   . GLY   B 1 266 ? 45.344  -15.062 -32.447 1   62.55 ? 251 GLY   B N   1 
ATOM   4995 C  CA  . GLY   B 1 266 ? 45.961  -16.095 -31.624 1   63.16 ? 251 GLY   B CA  1 
ATOM   4996 C  C   . GLY   B 1 266 ? 45.015  -16.822 -30.691 1   63.15 ? 251 GLY   B C   1 
ATOM   4997 O  O   . GLY   B 1 266 ? 45.357  -17.893 -30.185 1   63.11 ? 251 GLY   B O   1 
ATOM   4998 N  N   . PHE   B 1 267 ? 43.824  -16.254 -30.438 1   63.07 ? 252 PHE   B N   1 
ATOM   4999 C  CA  . PHE   B 1 267 ? 42.857  -16.89  -29.542 1   63.1  ? 252 PHE   B CA  1 
ATOM   5000 C  C   . PHE   B 1 267 ? 41.708  -17.57  -30.303 1   63.87 ? 252 PHE   B C   1 
ATOM   5001 O  O   . PHE   B 1 267 ? 41.392  -18.726 -30.019 1   64.01 ? 252 PHE   B O   1 
ATOM   5002 C  CB  . PHE   B 1 267 ? 42.343  -15.91  -28.478 1   62.39 ? 252 PHE   B CB  1 
ATOM   5003 C  CG  . PHE   B 1 267 ? 41.746  -16.639 -27.302 1   62.3  ? 252 PHE   B CG  1 
ATOM   5004 C  CD1 . PHE   B 1 267 ? 42.541  -17.062 -26.253 1   62.72 ? 252 PHE   B CD1 1 
ATOM   5005 C  CD2 . PHE   B 1 267 ? 40.396  -16.94  -27.265 1   62.8  ? 252 PHE   B CD2 1 
ATOM   5006 C  CE1 . PHE   B 1 267 ? 41.99   -17.746 -25.178 1   63.31 ? 252 PHE   B CE1 1 
ATOM   5007 C  CE2 . PHE   B 1 267 ? 39.848  -17.616 -26.187 1   63.24 ? 252 PHE   B CE2 1 
ATOM   5008 C  CZ  . PHE   B 1 267 ? 40.648  -18.019 -25.153 1   63.06 ? 252 PHE   B CZ  1 
ATOM   5009 N  N   . TRP   B 1 268 ? 41.072  -16.849 -31.247 1   64.17 ? 253 TRP   B N   1 
ATOM   5010 C  CA  . TRP   B 1 268 ? 40.002  -17.379 -32.102 1   65.17 ? 253 TRP   B CA  1 
ATOM   5011 C  C   . TRP   B 1 268 ? 40.366  -17.082 -33.553 1   65.66 ? 253 TRP   B C   1 
ATOM   5012 O  O   . TRP   B 1 268 ? 40.94   -16.034 -33.841 1   65.74 ? 253 TRP   B O   1 
ATOM   5013 C  CB  . TRP   B 1 268 ? 38.635  -16.735 -31.808 1   65.58 ? 253 TRP   B CB  1 
ATOM   5014 C  CG  . TRP   B 1 268 ? 38.046  -17.058 -30.465 1   66.66 ? 253 TRP   B CG  1 
ATOM   5015 C  CD1 . TRP   B 1 268 ? 37.715  -18.291 -29.985 1   67.46 ? 253 TRP   B CD1 1 
ATOM   5016 C  CD2 . TRP   B 1 268 ? 37.623  -16.114 -29.474 1   66.86 ? 253 TRP   B CD2 1 
ATOM   5017 N  NE1 . TRP   B 1 268 ? 37.162  -18.176 -28.732 1   67.77 ? 253 TRP   B NE1 1 
ATOM   5018 C  CE2 . TRP   B 1 268 ? 37.08   -16.848 -28.401 1   67.66 ? 253 TRP   B CE2 1 
ATOM   5019 C  CE3 . TRP   B 1 268 ? 37.672  -14.717 -29.379 1   67.3  ? 253 TRP   B CE3 1 
ATOM   5020 C  CZ2 . TRP   B 1 268 ? 36.606  -16.231 -27.242 1   68.39 ? 253 TRP   B CZ2 1 
ATOM   5021 C  CZ3 . TRP   B 1 268 ? 37.184  -14.108 -28.239 1   68.11 ? 253 TRP   B CZ3 1 
ATOM   5022 C  CH2 . TRP   B 1 268 ? 36.673  -14.861 -27.182 1   68.33 ? 253 TRP   B CH2 1 
ATOM   5023 N  N   . GLU   B 1 269 ? 39.998  -17.975 -34.478 1   65.85 ? 254 GLU   B N   1 
ATOM   5024 C  CA  . GLU   B 1 269 ? 40.308  -17.772 -35.894 1   65.78 ? 254 GLU   B CA  1 
ATOM   5025 C  C   . GLU   B 1 269 ? 39.413  -16.731 -36.56  1   65.27 ? 254 GLU   B C   1 
ATOM   5026 O  O   . GLU   B 1 269 ? 39.915  -15.891 -37.303 1   65.43 ? 254 GLU   B O   1 
ATOM   5027 C  CB  . GLU   B 1 269 ? 40.258  -19.101 -36.665 1   68.01 ? 254 GLU   B CB  1 
ATOM   5028 N  N   . ASP   B 1 270 ? 38.096  -16.791 -36.314 1   64.67 ? 255 ASP   B N   1 
ATOM   5029 C  CA  . ASP   B 1 270 ? 37.127  -15.862 -36.914 1   64.56 ? 255 ASP   B CA  1 
ATOM   5030 C  C   . ASP   B 1 270 ? 36.864  -14.619 -36.045 1   63.77 ? 255 ASP   B C   1 
ATOM   5031 O  O   . ASP   B 1 270 ? 37.006  -14.688 -34.822 1   64.16 ? 255 ASP   B O   1 
ATOM   5032 C  CB  . ASP   B 1 270 ? 35.806  -16.601 -37.163 1   66.56 ? 255 ASP   B CB  1 
ATOM   5033 N  N   . PRO   B 1 271 ? 36.49   -13.474 -36.647 1   62.57 ? 256 PRO   B N   1 
ATOM   5034 C  CA  . PRO   B 1 271 ? 36.197  -12.284 -35.83  1   61.58 ? 256 PRO   B CA  1 
ATOM   5035 C  C   . PRO   B 1 271 ? 34.958  -12.485 -34.957 1   60.08 ? 256 PRO   B C   1 
ATOM   5036 O  O   . PRO   B 1 271 ? 34.019  -13.166 -35.366 1   60.42 ? 256 PRO   B O   1 
ATOM   5037 C  CB  . PRO   B 1 271 ? 35.985  -11.178 -36.871 1   62.62 ? 256 PRO   B CB  1 
ATOM   5038 C  CG  . PRO   B 1 271 ? 35.57   -11.895 -38.104 1   63.37 ? 256 PRO   B CG  1 
ATOM   5039 C  CD  . PRO   B 1 271 ? 36.278  -13.217 -38.085 1   62.01 ? 256 PRO   B CD  1 
ATOM   5040 N  N   . LYS   B 1 272 ? 34.976  -11.936 -33.732 1   58.21 ? 257 LYS   B N   1 
ATOM   5041 C  CA  . LYS   B 1 272 ? 33.859  -12.087 -32.8   1   56.24 ? 257 LYS   B CA  1 
ATOM   5042 C  C   . LYS   B 1 272 ? 33.18   -10.766 -32.498 1   53.61 ? 257 LYS   B C   1 
ATOM   5043 O  O   . LYS   B 1 272 ? 33.833  -9.732  -32.384 1   52.61 ? 257 LYS   B O   1 
ATOM   5044 C  CB  . LYS   B 1 272 ? 34.324  -12.716 -31.49  1   58.32 ? 257 LYS   B CB  1 
ATOM   5045 C  CG  . LYS   B 1 272 ? 35.035  -14.037 -31.672 1   62.75 ? 257 LYS   B CG  1 
ATOM   5046 C  CD  . LYS   B 1 272 ? 34.099  -15.13  -32.139 1   67.59 ? 257 LYS   B CD  1 
ATOM   5047 C  CE  . LYS   B 1 272 ? 34.81   -16.46  -32.197 1   71.23 ? 257 LYS   B CE  1 
ATOM   5048 N  NZ  . LYS   B 1 272 ? 34.139  -17.396 -33.131 1   74.02 ? 257 LYS   B NZ  1 
ATOM   5049 N  N   . GLU   B 1 273 ? 31.863  -10.82  -32.338 1   52.03 ? 258 GLU   B N   1 
ATOM   5050 C  CA  . GLU   B 1 273 ? 31.062  -9.653  -32.02  1   50.74 ? 258 GLU   B CA  1 
ATOM   5051 C  C   . GLU   B 1 273 ? 30.744  -9.593  -30.537 1   48.73 ? 258 GLU   B C   1 
ATOM   5052 O  O   . GLU   B 1 273 ? 30.27   -10.576 -29.964 1   49.03 ? 258 GLU   B O   1 
ATOM   5053 C  CB  . GLU   B 1 273 ? 29.754  -9.664  -32.808 1   52.63 ? 258 GLU   B CB  1 
ATOM   5054 C  CG  . GLU   B 1 273 ? 29.94   -9.323  -34.273 1   57.68 ? 258 GLU   B CG  1 
ATOM   5055 C  CD  . GLU   B 1 273 ? 28.626  -9.045  -34.968 1   63.94 ? 258 GLU   B CD  1 
ATOM   5056 O  OE1 . GLU   B 1 273 ? 27.792  -9.973  -35.045 1   66.48 ? 258 GLU   B OE1 1 
ATOM   5057 O  OE2 . GLU   B 1 273 ? 28.415  -7.893  -35.408 1   65.55 ? 258 GLU   B OE2 1 
ATOM   5058 N  N   . PHE   B 1 274 ? 30.994  -8.435  -29.918 1   45.88 ? 259 PHE   B N   1 
ATOM   5059 C  CA  . PHE   B 1 274 ? 30.657  -8.212  -28.516 1   43.22 ? 259 PHE   B CA  1 
ATOM   5060 C  C   . PHE   B 1 274 ? 30.08   -6.817  -28.397 1   40.28 ? 259 PHE   B C   1 
ATOM   5061 O  O   . PHE   B 1 274 ? 30.571  -5.891  -29.054 1   39.78 ? 259 PHE   B O   1 
ATOM   5062 C  CB  . PHE   B 1 274 ? 31.872  -8.385  -27.59  1   43.11 ? 259 PHE   B CB  1 
ATOM   5063 C  CG  . PHE   B 1 274 ? 32.371  -9.803  -27.493 1   44.71 ? 259 PHE   B CG  1 
ATOM   5064 C  CD1 . PHE   B 1 274 ? 31.618  -10.779 -26.866 1   45.86 ? 259 PHE   B CD1 1 
ATOM   5065 C  CD2 . PHE   B 1 274 ? 33.568  -10.176 -28.084 1   45.71 ? 259 PHE   B CD2 1 
ATOM   5066 C  CE1 . PHE   B 1 274 ? 32.058  -12.094 -26.828 1   46.85 ? 259 PHE   B CE1 1 
ATOM   5067 C  CE2 . PHE   B 1 274 ? 33.995  -11.493 -28.054 1   46.52 ? 259 PHE   B CE2 1 
ATOM   5068 C  CZ  . PHE   B 1 274 ? 33.245  -12.44  -27.418 1   46.42 ? 259 PHE   B CZ  1 
ATOM   5069 N  N   . ALA   B 1 275 ? 29.028  -6.659  -27.584 1   38.29 ? 260 ALA   B N   1 
ATOM   5070 C  CA  . ALA   B 1 275 ? 28.421  -5.348  -27.395 1   37.59 ? 260 ALA   B CA  1 
ATOM   5071 C  C   . ALA   B 1 275 ? 29.317  -4.474  -26.529 1   35.99 ? 260 ALA   B C   1 
ATOM   5072 O  O   . ALA   B 1 275 ? 30.063  -4.974  -25.682 1   35.66 ? 260 ALA   B O   1 
ATOM   5073 C  CB  . ALA   B 1 275 ? 27.036  -5.485  -26.757 1   38.02 ? 260 ALA   B CB  1 
ATOM   5074 N  N   . GLY   B 1 276 ? 29.281  -3.171  -26.781 1   35.19 ? 261 GLY   B N   1 
ATOM   5075 C  CA  . GLY   B 1 276 ? 30.06   -2.233  -25.989 1   34.9  ? 261 GLY   B CA  1 
ATOM   5076 C  C   . GLY   B 1 276 ? 29.518  -2.107  -24.578 1   34.41 ? 261 GLY   B C   1 
ATOM   5077 O  O   . GLY   B 1 276 ? 28.393  -2.54   -24.288 1   33.69 ? 261 GLY   B O   1 
ATOM   5078 N  N   . GLY   B 1 277 ? 30.317  -1.514  -23.704 1   34.02 ? 262 GLY   B N   1 
ATOM   5079 C  CA  . GLY   B 1 277 ? 29.959  -1.285  -22.31  1   34.21 ? 262 GLY   B CA  1 
ATOM   5080 C  C   . GLY   B 1 277 ? 28.674  -0.495  -22.191 1   34.47 ? 262 GLY   B C   1 
ATOM   5081 O  O   . GLY   B 1 277 ? 28.469  0.498   -22.893 1   34.53 ? 262 GLY   B O   1 
ATOM   5082 N  N   . SER   B 1 278 ? 27.767  -0.977  -21.347 1   34.04 ? 263 SER   B N   1 
ATOM   5083 C  CA  . SER   B 1 278 ? 26.464  -0.377  -21.208 1   32.97 ? 263 SER   B CA  1 
ATOM   5084 C  C   . SER   B 1 278 ? 25.978  -0.357  -19.77  1   32.61 ? 263 SER   B C   1 
ATOM   5085 O  O   . SER   B 1 278 ? 26.202  -1.319  -19.028 1   31.92 ? 263 SER   B O   1 
ATOM   5086 C  CB  . SER   B 1 278 ? 25.464  -1.156  -22.06  1   33.81 ? 263 SER   B CB  1 
ATOM   5087 O  OG  . SER   B 1 278 ? 24.142  -0.669  -21.934 1   35.82 ? 263 SER   B OG  1 
ATOM   5088 N  N   . ALA   B 1 279 ? 25.215  0.689   -19.395 1   32.18 ? 264 ALA   B N   1 
ATOM   5089 C  CA  . ALA   B 1 279 ? 24.583  0.694   -18.076 1   31.46 ? 264 ALA   B CA  1 
ATOM   5090 C  C   . ALA   B 1 279 ? 23.417  -0.33   -18.026 1   31.34 ? 264 ALA   B C   1 
ATOM   5091 O  O   . ALA   B 1 279 ? 22.962  -0.647  -16.945 1   31.99 ? 264 ALA   B O   1 
ATOM   5092 C  CB  . ALA   B 1 279 ? 24.142  2.088   -17.687 1   30.8  ? 264 ALA   B CB  1 
ATOM   5093 N  N   . GLY   B 1 280 ? 23.013  -0.906  -19.164 1   30.91 ? 265 GLY   B N   1 
ATOM   5094 C  CA  . GLY   B 1 280 ? 22.126  -2.068  -19.206 1   31.89 ? 265 GLY   B CA  1 
ATOM   5095 C  C   . GLY   B 1 280 ? 22.801  -3.269  -18.519 1   32.19 ? 265 GLY   B C   1 
ATOM   5096 O  O   . GLY   B 1 280 ? 22.135  -4.232  -18.143 1   33.64 ? 265 GLY   B O   1 
ATOM   5097 N  N   . GLN   B 1 281 ? 24.123  -3.201  -18.278 1   31.23 ? 266 GLN   B N   1 
ATOM   5098 C  CA  . GLN   B 1 281 ? 24.932  -4.199  -17.557 1   30.69 ? 266 GLN   B CA  1 
ATOM   5099 C  C   . GLN   B 1 281 ? 24.933  -3.947  -16.039 1   30.79 ? 266 GLN   B C   1 
ATOM   5100 O  O   . GLN   B 1 281 ? 25.484  -4.746  -15.303 1   30.98 ? 266 GLN   B O   1 
ATOM   5101 C  CB  . GLN   B 1 281 ? 26.36   -4.264  -18.116 1   30.57 ? 266 GLN   B CB  1 
ATOM   5102 C  CG  . GLN   B 1 281 ? 26.414  -4.648  -19.59  1   30.96 ? 266 GLN   B CG  1 
ATOM   5103 C  CD  . GLN   B 1 281 ? 27.708  -4.313  -20.269 1   33.13 ? 266 GLN   B CD  1 
ATOM   5104 O  OE1 . GLN   B 1 281 ? 28.563  -3.59   -19.738 1   33.22 ? 266 GLN   B OE1 1 
ATOM   5105 N  NE2 . GLN   B 1 281 ? 27.878  -4.818  -21.485 1   32.24 ? 266 GLN   B NE2 1 
ATOM   5106 N  N   . SER   B 1 282 ? 24.342  -2.826  -15.562 1   30.85 ? 267 SER   B N   1 
ATOM   5107 C  CA  . SER   B 1 282 ? 24.245  -2.548  -14.137 1   31.05 ? 267 SER   B CA  1 
ATOM   5108 C  C   . SER   B 1 282 ? 23.319  -3.598  -13.502 1   31.1  ? 267 SER   B C   1 
ATOM   5109 O  O   . SER   B 1 282 ? 22.174  -3.772  -13.93  1   30.56 ? 267 SER   B O   1 
ATOM   5110 C  CB  . SER   B 1 282 ? 23.66   -1.155  -13.888 1   31.63 ? 267 SER   B CB  1 
ATOM   5111 O  OG  . SER   B 1 282 ? 23.347  -0.994  -12.514 1   32.31 ? 267 SER   B OG  1 
ATOM   5112 N  N   . SER   B 1 283 ? 23.827  -4.295  -12.497 1   31.41 ? 268 SER   B N   1 
ATOM   5113 C  CA  . SER   B 1 283 ? 23.052  -5.301  -11.774 1   31.41 ? 268 SER   B CA  1 
ATOM   5114 C  C   . SER   B 1 283 ? 22.055  -4.652  -10.821 1   31.69 ? 268 SER   B C   1 
ATOM   5115 O  O   . SER   B 1 283 ? 20.992  -5.224  -10.61  1   31.06 ? 268 SER   B O   1 
ATOM   5116 C  CB  . SER   B 1 283 ? 23.981  -6.187  -10.959 1   32.47 ? 268 SER   B CB  1 
ATOM   5117 O  OG  . SER   B 1 283 ? 24.87   -6.912  -11.795 1   35.29 ? 268 SER   B OG  1 
ATOM   5118 N  N   . VAL   B 1 284 ? 22.368  -3.474  -10.255 1   32.21 ? 269 VAL   B N   1 
ATOM   5119 C  CA  . VAL   B 1 284 ? 21.466  -2.866  -9.259  1   33.35 ? 269 VAL   B CA  1 
ATOM   5120 C  C   . VAL   B 1 284 ? 20.117  -2.422  -9.883  1   33.4  ? 269 VAL   B C   1 
ATOM   5121 O  O   . VAL   B 1 284 ? 19.067  -2.674  -9.285  1   33.18 ? 269 VAL   B O   1 
ATOM   5122 C  CB  . VAL   B 1 284 ? 22.141  -1.758  -8.42   1   35.18 ? 269 VAL   B CB  1 
ATOM   5123 C  CG1 . VAL   B 1 284 ? 22.202  -0.426  -9.179  1   35.65 ? 269 VAL   B CG1 1 
ATOM   5124 C  CG2 . VAL   B 1 284 ? 21.429  -1.589  -7.083  1   36.51 ? 269 VAL   B CG2 1 
ATOM   5125 N  N   . PHE   B 1 285 ? 20.126  -1.876  -11.107 1   32.78 ? 270 PHE   B N   1 
ATOM   5126 C  CA  . PHE   B 1 285 ? 18.896  -1.485  -11.772 1   33.84 ? 270 PHE   B CA  1 
ATOM   5127 C  C   . PHE   B 1 285 ? 18.108  -2.695  -12.241 1   33.49 ? 270 PHE   B C   1 
ATOM   5128 O  O   . PHE   B 1 285 ? 16.878  -2.702  -12.111 1   34.33 ? 270 PHE   B O   1 
ATOM   5129 C  CB  . PHE   B 1 285 ? 19.171  -0.509  -12.905 1   35.46 ? 270 PHE   B CB  1 
ATOM   5130 C  CG  . PHE   B 1 285 ? 19.39   0.865   -12.34  1   38.12 ? 270 PHE   B CG  1 
ATOM   5131 C  CD1 . PHE   B 1 285 ? 20.66   1.285   -11.975 1   39.42 ? 270 PHE   B CD1 1 
ATOM   5132 C  CD2 . PHE   B 1 285 ? 18.317  1.715   -12.111 1   40.37 ? 270 PHE   B CD2 1 
ATOM   5133 C  CE1 . PHE   B 1 285 ? 20.856  2.522   -11.382 1   41.02 ? 270 PHE   B CE1 1 
ATOM   5134 C  CE2 . PHE   B 1 285 ? 18.512  2.963   -11.534 1   41.87 ? 270 PHE   B CE2 1 
ATOM   5135 C  CZ  . PHE   B 1 285 ? 19.784  3.361   -11.172 1   41.77 ? 270 PHE   B CZ  1 
ATOM   5136 N  N   . GLN   B 1 286 ? 18.801  -3.742  -12.734 1   32.3  ? 271 GLN   B N   1 
ATOM   5137 C  CA  . GLN   B 1 286 ? 18.087  -4.973  -13.107 1   32.61 ? 271 GLN   B CA  1 
ATOM   5138 C  C   . GLN   B 1 286 ? 17.458  -5.629  -11.851 1   33.55 ? 271 GLN   B C   1 
ATOM   5139 O  O   . GLN   B 1 286 ? 16.366  -6.164  -11.929 1   34.38 ? 271 GLN   B O   1 
ATOM   5140 C  CB  . GLN   B 1 286 ? 18.994  -5.954  -13.87  1   33.1  ? 271 GLN   B CB  1 
ATOM   5141 C  CG  . GLN   B 1 286 ? 19.448  -5.398  -15.238 1   33.51 ? 271 GLN   B CG  1 
ATOM   5142 C  CD  . GLN   B 1 286 ? 19.426  -6.433  -16.325 1   34.54 ? 271 GLN   B CD  1 
ATOM   5143 O  OE1 . GLN   B 1 286 ? 18.705  -7.442  -16.246 1   34.81 ? 271 GLN   B OE1 1 
ATOM   5144 N  NE2 . GLN   B 1 286 ? 20.22   -6.216  -17.373 1   32.47 ? 271 GLN   B NE2 1 
ATOM   5145 N  N   A CYS   B 1 287 ? 18.145  -5.545  -10.703 0.5 33.57 ? 272 CYS   B N   1 
ATOM   5146 N  N   B CYS   B 1 287 ? 18.15   -5.558  -10.728 0.5 33.82 ? 272 CYS   B N   1 
ATOM   5147 C  CA  A CYS   B 1 287 ? 17.683  -6.096  -9.428  0.5 34.67 ? 272 CYS   B CA  1 
ATOM   5148 C  CA  B CYS   B 1 287 ? 17.745  -6.113  -9.447  0.5 35.18 ? 272 CYS   B CA  1 
ATOM   5149 C  C   A CYS   B 1 287 ? 16.378  -5.508  -8.978  0.5 35.77 ? 272 CYS   B C   1 
ATOM   5150 C  C   B CYS   B 1 287 ? 16.426  -5.502  -8.925  0.5 36.06 ? 272 CYS   B C   1 
ATOM   5151 O  O   A CYS   B 1 287 ? 15.497  -6.27   -8.604  0.5 35.87 ? 272 CYS   B O   1 
ATOM   5152 O  O   B CYS   B 1 287 ? 15.571  -6.264  -8.491  0.5 36.27 ? 272 CYS   B O   1 
ATOM   5153 C  CB  A CYS   B 1 287 ? 18.741  -5.97   -8.337  0.5 35.32 ? 272 CYS   B CB  1 
ATOM   5154 C  CB  B CYS   B 1 287 ? 18.899  -6.002  -8.45   0.5 36.46 ? 272 CYS   B CB  1 
ATOM   5155 S  SG  A CYS   B 1 287 ? 20.068  -7.186  -8.451  0.5 39.68 ? 272 CYS   B SG  1 
ATOM   5156 S  SG  B CYS   B 1 287 ? 18.423  -5.968  -6.709  0.5 42.76 ? 272 CYS   B SG  1 
ATOM   5157 N  N   . PHE   B 1 288 ? 16.228  -4.175  -9.023  1   36.4  ? 273 PHE   B N   1 
ATOM   5158 C  CA  . PHE   B 1 288 ? 14.971  -3.562  -8.585  1   38.03 ? 273 PHE   B CA  1 
ATOM   5159 C  C   . PHE   B 1 288 ? 13.815  -3.854  -9.554  1   35.5  ? 273 PHE   B C   1 
ATOM   5160 O  O   . PHE   B 1 288 ? 12.686  -4.018  -9.102  1   33.88 ? 273 PHE   B O   1 
ATOM   5161 C  CB  . PHE   B 1 288 ? 15.151  -2.078  -8.252  1   40.98 ? 273 PHE   B CB  1 
ATOM   5162 C  CG  . PHE   B 1 288 ? 15.88   -2.072  -6.926  1   44.59 ? 273 PHE   B CG  1 
ATOM   5163 C  CD1 . PHE   B 1 288 ? 15.292  -2.62   -5.792  1   47.01 ? 273 PHE   B CD1 1 
ATOM   5164 C  CD2 . PHE   B 1 288 ? 17.21   -1.704  -6.852  1   46.71 ? 273 PHE   B CD2 1 
ATOM   5165 C  CE1 . PHE   B 1 288 ? 16.003  -2.739  -4.598  1   48.34 ? 273 PHE   B CE1 1 
ATOM   5166 C  CE2 . PHE   B 1 288 ? 17.924  -1.832  -5.662  1   48.03 ? 273 PHE   B CE2 1 
ATOM   5167 C  CZ  . PHE   B 1 288 ? 17.324  -2.364  -4.549  1   48.24 ? 273 PHE   B CZ  1 
ATOM   5168 N  N   . ASP   B 1 289 ? 14.103  -4.058  -10.847 1   34.4  ? 274 ASP   B N   1 
ATOM   5169 C  CA  . ASP   B 1 289 ? 13.054  -4.448  -11.794 1   33.8  ? 274 ASP   B CA  1 
ATOM   5170 C  C   . ASP   B 1 289 ? 12.621  -5.893  -11.468 1   33.6  ? 274 ASP   B C   1 
ATOM   5171 O  O   . ASP   B 1 289 ? 11.418  -6.202  -11.507 1   33.8  ? 274 ASP   B O   1 
ATOM   5172 C  CB  . ASP   B 1 289 ? 13.545  -4.354  -13.237 1   35.42 ? 274 ASP   B CB  1 
ATOM   5173 C  CG  . ASP   B 1 289 ? 13.612  -2.921  -13.749 1   41.16 ? 274 ASP   B CG  1 
ATOM   5174 O  OD1 . ASP   B 1 289 ? 12.811  -2.096  -13.291 1   41    ? 274 ASP   B OD1 1 
ATOM   5175 O  OD2 . ASP   B 1 289 ? 14.475  -2.633  -14.618 1   44.14 ? 274 ASP   B OD2 1 
ATOM   5176 N  N   . VAL   B 1 290 ? 13.59   -6.774  -11.14  1   32.49 ? 275 VAL   B N   1 
ATOM   5177 C  CA  . VAL   B 1 290 ? 13.249  -8.147  -10.777 1   32.97 ? 275 VAL   B CA  1 
ATOM   5178 C  C   . VAL   B 1 290 ? 12.467  -8.157  -9.441  1   33.79 ? 275 VAL   B C   1 
ATOM   5179 O  O   . VAL   B 1 290 ? 11.41   -8.77   -9.341  1   34.21 ? 275 VAL   B O   1 
ATOM   5180 C  CB  . VAL   B 1 290 ? 14.497  -9.054  -10.711 1   32.67 ? 275 VAL   B CB  1 
ATOM   5181 C  CG1 . VAL   B 1 290 ? 14.135  -10.403 -10.082 1   32.32 ? 275 VAL   B CG1 1 
ATOM   5182 C  CG2 . VAL   B 1 290 ? 15.105  -9.248  -12.104 1   32.22 ? 275 VAL   B CG2 1 
ATOM   5183 N  N   . LEU   B 1 291 ? 12.965  -7.443  -8.448  1   33.95 ? 276 LEU   B N   1 
ATOM   5184 C  CA  . LEU   B 1 291 ? 12.338  -7.372  -7.137  1   35.81 ? 276 LEU   B CA  1 
ATOM   5185 C  C   . LEU   B 1 291 ? 10.888  -6.885  -7.202  1   36.8  ? 276 LEU   B C   1 
ATOM   5186 O  O   . LEU   B 1 291 ? 10.005  -7.476  -6.576  1   37.24 ? 276 LEU   B O   1 
ATOM   5187 C  CB  . LEU   B 1 291 ? 13.162  -6.472  -6.209  1   36.63 ? 276 LEU   B CB  1 
ATOM   5188 C  CG  . LEU   B 1 291 ? 12.575  -6.265  -4.804  1   39.58 ? 276 LEU   B CG  1 
ATOM   5189 C  CD1 . LEU   B 1 291 ? 12.759  -7.515  -3.95   1   39.8  ? 276 LEU   B CD1 1 
ATOM   5190 C  CD2 . LEU   B 1 291 ? 13.178  -5.062  -4.153  1   40.8  ? 276 LEU   B CD2 1 
ATOM   5191 N  N   . LEU   B 1 292 ? 10.637  -5.843  -7.989  1   35.78 ? 277 LEU   B N   1 
ATOM   5192 C  CA  . LEU   B 1 292 ? 9.304   -5.279  -8.085  1   35.79 ? 277 LEU   B CA  1 
ATOM   5193 C  C   . LEU   B 1 292 ? 8.395   -5.913  -9.137  1   35.81 ? 277 LEU   B C   1 
ATOM   5194 O  O   . LEU   B 1 292 ? 7.298   -5.406  -9.358  1   36.47 ? 277 LEU   B O   1 
ATOM   5195 C  CB  . LEU   B 1 292 ? 9.409   -3.771  -8.291  1   35.69 ? 277 LEU   B CB  1 
ATOM   5196 C  CG  . LEU   B 1 292 ? 10.177  -3.029  -7.179  1   36    ? 277 LEU   B CG  1 
ATOM   5197 C  CD1 . LEU   B 1 292 ? 10.413  -1.573  -7.574  1   35.65 ? 277 LEU   B CD1 1 
ATOM   5198 C  CD2 . LEU   B 1 292 ? 9.454   -3.141  -5.831  1   36.47 ? 277 LEU   B CD2 1 
ATOM   5199 N  N   . GLY   B 1 293 ? 8.823   -7.01   -9.756  1   35.65 ? 278 GLY   B N   1 
ATOM   5200 C  CA  . GLY   B 1 293 ? 8.027   -7.72   -10.755 1   36.1  ? 278 GLY   B CA  1 
ATOM   5201 C  C   . GLY   B 1 293 ? 7.812   -6.98   -12.057 1   37.12 ? 278 GLY   B C   1 
ATOM   5202 O  O   . GLY   B 1 293 ? 6.852   -7.264  -12.779 1   37.31 ? 278 GLY   B O   1 
ATOM   5203 N  N   . ILE   B 1 294 ? 8.685   -6      -12.352 1   37.36 ? 279 ILE   B N   1 
ATOM   5204 C  CA  . ILE   B 1 294 ? 8.633   -5.234  -13.584 1   38.87 ? 279 ILE   B CA  1 
ATOM   5205 C  C   . ILE   B 1 294 ? 9.356   -6.148  -14.558 1   41.84 ? 279 ILE   B C   1 
ATOM   5206 O  O   . ILE   B 1 294 ? 10.591  -6.283  -14.499 1   43.6  ? 279 ILE   B O   1 
ATOM   5207 C  CB  . ILE   B 1 294 ? 9.392   -3.885  -13.386 1   39.19 ? 279 ILE   B CB  1 
ATOM   5208 C  CG1 . ILE   B 1 294 ? 8.698   -3.034  -12.281 1   39.76 ? 279 ILE   B CG1 1 
ATOM   5209 C  CG2 . ILE   B 1 294 ? 9.457   -3.112  -14.702 1   39.85 ? 279 ILE   B CG2 1 
ATOM   5210 C  CD1 . ILE   B 1 294 ? 9.553   -2.088  -11.629 1   41.57 ? 279 ILE   B CD1 1 
ATOM   5211 N  N   . GLN   B 1 295 ? 8.604   -6.841  -15.393 1   41.85 ? 280 GLN   B N   1 
ATOM   5212 C  CA  . GLN   B 1 295 ? 9.172   -7.848  -16.282 1   42.27 ? 280 GLN   B CA  1 
ATOM   5213 C  C   . GLN   B 1 295 ? 9.864   -7.243  -17.488 1   41.31 ? 280 GLN   B C   1 
ATOM   5214 O  O   . GLN   B 1 295 ? 9.347   -7.328  -18.605 1   41.74 ? 280 GLN   B O   1 
ATOM   5215 C  CB  . GLN   B 1 295 ? 8.087   -8.846  -16.701 1   44.6  ? 280 GLN   B CB  1 
ATOM   5216 C  CG  . GLN   B 1 295 ? 7.408   -9.516  -15.511 1   50.66 ? 280 GLN   B CG  1 
ATOM   5217 C  CD  . GLN   B 1 295 ? 6.449   -10.616 -15.925 1   58.38 ? 280 GLN   B CD  1 
ATOM   5218 O  OE1 . GLN   B 1 295 ? 6.299   -11.624 -15.227 1   61.31 ? 280 GLN   B OE1 1 
ATOM   5219 N  NE2 . GLN   B 1 295 ? 5.779   -10.463 -17.068 1   59.38 ? 280 GLN   B NE2 1 
ATOM   5220 N  N   . GLN   B 1 296 ? 11.02   -6.607  -17.26  1   40.23 ? 281 GLN   B N   1 
ATOM   5221 C  CA  . GLN   B 1 296 ? 11.78   -5.956  -18.321 1   40.21 ? 281 GLN   B CA  1 
ATOM   5222 C  C   . GLN   B 1 296 ? 12.258  -6.917  -19.393 1   41.15 ? 281 GLN   B C   1 
ATOM   5223 O  O   . GLN   B 1 296 ? 12.376  -6.522  -20.544 1   41.42 ? 281 GLN   B O   1 
ATOM   5224 C  CB  . GLN   B 1 296 ? 12.983  -5.188  -17.758 1   40.26 ? 281 GLN   B CB  1 
ATOM   5225 C  CG  . GLN   B 1 296 ? 12.623  -4.008  -16.887 1   41.88 ? 281 GLN   B CG  1 
ATOM   5226 C  CD  . GLN   B 1 296 ? 12.036  -2.814  -17.604 1   44.32 ? 281 GLN   B CD  1 
ATOM   5227 O  OE1 . GLN   B 1 296 ? 11.794  -2.802  -18.819 1   44.42 ? 281 GLN   B OE1 1 
ATOM   5228 N  NE2 . GLN   B 1 296 ? 11.779  -1.767  -16.85  1   46.05 ? 281 GLN   B NE2 1 
ATOM   5229 N  N   . THR   B 1 297 ? 12.518  -8.177  -19.025 1   40.97 ? 282 THR   B N   1 
ATOM   5230 C  CA  . THR   B 1 297 ? 13.015  -9.188  -19.958 1   41.24 ? 282 THR   B CA  1 
ATOM   5231 C  C   . THR   B 1 297 ? 11.899  -10.049 -20.62  1   41.97 ? 282 THR   B C   1 
ATOM   5232 O  O   . THR   B 1 297 ? 12.206  -10.947 -21.403 1   42.51 ? 282 THR   B O   1 
ATOM   5233 C  CB  . THR   B 1 297 ? 14.056  -10.034 -19.243 1   42.65 ? 282 THR   B CB  1 
ATOM   5234 O  OG1 . THR   B 1 297 ? 13.426  -10.609 -18.091 1   44.47 ? 282 THR   B OG1 1 
ATOM   5235 C  CG2 . THR   B 1 297 ? 15.289  -9.201  -18.809 1   42.32 ? 282 THR   B CG2 1 
ATOM   5236 N  N   . ALA   B 1 298 ? 10.623  -9.759  -20.346 1   41.48 ? 283 ALA   B N   1 
ATOM   5237 C  CA  . ALA   B 1 298 ? 9.511   -10.492 -20.956 1   42.38 ? 283 ALA   B CA  1 
ATOM   5238 C  C   . ALA   B 1 298 ? 9.037   -9.845  -22.285 1   43.44 ? 283 ALA   B C   1 
ATOM   5239 O  O   . ALA   B 1 298 ? 9.285   -8.669  -22.518 1   43.11 ? 283 ALA   B O   1 
ATOM   5240 C  CB  . ALA   B 1 298 ? 8.339   -10.527 -19.974 1   42.03 ? 283 ALA   B CB  1 
ATOM   5241 N  N   . GLY   B 1 299 ? 8.318   -10.6   -23.117 1   44.25 ? 284 GLY   B N   1 
ATOM   5242 C  CA  . GLY   B 1 299 ? 7.645   -10.035 -24.282 1   45.3  ? 284 GLY   B CA  1 
ATOM   5243 C  C   . GLY   B 1 299 ? 8.21    -10.112 -25.69  1   46.2  ? 284 GLY   B C   1 
ATOM   5244 O  O   . GLY   B 1 299 ? 7.529   -9.683  -26.636 1   46.25 ? 284 GLY   B O   1 
ATOM   5245 N  N   . GLY   B 1 300 ? 9.448   -10.576 -25.845 1   45.94 ? 285 GLY   B N   1 
ATOM   5246 C  CA  . GLY   B 1 300 ? 10.08   -10.719 -27.154 1   46.56 ? 285 GLY   B CA  1 
ATOM   5247 C  C   . GLY   B 1 300 ? 10.602  -9.462  -27.837 1   46.83 ? 285 GLY   B C   1 
ATOM   5248 O  O   . GLY   B 1 300 ? 11.227  -9.541  -28.905 1   47.53 ? 285 GLY   B O   1 
ATOM   5249 N  N   . GLY   B 1 301 ? 10.333  -8.306  -27.248 1   45.9  ? 286 GLY   B N   1 
ATOM   5250 C  CA  . GLY   B 1 301 ? 10.779  -7.038  -27.81  1   45.78 ? 286 GLY   B CA  1 
ATOM   5251 C  C   . GLY   B 1 301 ? 12.274  -6.843  -27.761 1   45.41 ? 286 GLY   B C   1 
ATOM   5252 O  O   . GLY   B 1 301 ? 12.982  -7.581  -27.079 1   45.12 ? 286 GLY   B O   1 
ATOM   5253 N  N   . HIS   B 1 302 ? 12.771  -5.833  -28.48  1   45.19 ? 287 HIS   B N   1 
ATOM   5254 C  CA  . HIS   B 1 302 ? 14.2    -5.557  -28.523 1   45.18 ? 287 HIS   B CA  1 
ATOM   5255 C  C   . HIS   B 1 302 ? 14.779  -5.114  -27.179 1   42.56 ? 287 HIS   B C   1 
ATOM   5256 O  O   . HIS   B 1 302 ? 15.901  -5.487  -26.85  1   42.22 ? 287 HIS   B O   1 
ATOM   5257 C  CB  . HIS   B 1 302 ? 14.528  -4.553  -29.636 1   48.03 ? 287 HIS   B CB  1 
ATOM   5258 C  CG  . HIS   B 1 302 ? 14.239  -5.09   -31.005 1   54.13 ? 287 HIS   B CG  1 
ATOM   5259 N  ND1 . HIS   B 1 302 ? 13.286  -4.508  -31.821 1   57.16 ? 287 HIS   B ND1 1 
ATOM   5260 C  CD2 . HIS   B 1 302 ? 14.761  -6.166  -31.644 1   55.96 ? 287 HIS   B CD2 1 
ATOM   5261 C  CE1 . HIS   B 1 302 ? 13.275  -5.23   -32.933 1   58.01 ? 287 HIS   B CE1 1 
ATOM   5262 N  NE2 . HIS   B 1 302 ? 14.143  -6.24   -32.871 1   57.58 ? 287 HIS   B NE2 1 
ATOM   5263 N  N   . ALA   B 1 303 ? 14.028  -4.324  -26.409 1   40.91 ? 288 ALA   B N   1 
ATOM   5264 C  CA  . ALA   B 1 303 ? 14.511  -3.835  -25.111 1   39.89 ? 288 ALA   B CA  1 
ATOM   5265 C  C   . ALA   B 1 303 ? 14.721  -4.984  -24.128 1   38.71 ? 288 ALA   B C   1 
ATOM   5266 O  O   . ALA   B 1 303 ? 15.755  -5.026  -23.442 1   38.4  ? 288 ALA   B O   1 
ATOM   5267 C  CB  . ALA   B 1 303 ? 13.54   -2.827  -24.534 1   40.23 ? 288 ALA   B CB  1 
ATOM   5268 N  N   . ALA   B 1 304 ? 13.765  -5.95   -24.117 1   37.39 ? 289 ALA   B N   1 
ATOM   5269 C  CA  . ALA   B 1 304 ? 13.805  -7.162  -23.293 1   36.63 ? 289 ALA   B CA  1 
ATOM   5270 C  C   . ALA   B 1 304 ? 15.004  -8.029  -23.675 1   35.68 ? 289 ALA   B C   1 
ATOM   5271 O  O   . ALA   B 1 304 ? 15.729  -8.508  -22.8   1   35.84 ? 289 ALA   B O   1 
ATOM   5272 C  CB  . ALA   B 1 304 ? 12.501  -7.956  -23.479 1   36    ? 289 ALA   B CB  1 
ATOM   5273 N  N   . GLN   B 1 305 ? 15.229  -8.218  -24.983 1   34.27 ? 290 GLN   B N   1 
ATOM   5274 C  CA  . GLN   B 1 305 ? 16.33   -9.023  -25.477 1   34.69 ? 290 GLN   B CA  1 
ATOM   5275 C  C   . GLN   B 1 305 ? 17.663  -8.389  -25.084 1   34.59 ? 290 GLN   B C   1 
ATOM   5276 O  O   . GLN   B 1 305 ? 18.568  -9.097  -24.651 1   34.62 ? 290 GLN   B O   1 
ATOM   5277 C  CB  . GLN   B 1 305 ? 16.233  -9.159  -27.013 1   36.06 ? 290 GLN   B CB  1 
ATOM   5278 C  CG  . GLN   B 1 305 ? 17.36   -9.973  -27.632 1   40.42 ? 290 GLN   B CG  1 
ATOM   5279 C  CD  . GLN   B 1 305 ? 17.127  -11.417 -27.309 1   45.24 ? 290 GLN   B CD  1 
ATOM   5280 O  OE1 . GLN   B 1 305 ? 16.05   -11.941 -27.586 1   47.9  ? 290 GLN   B OE1 1 
ATOM   5281 N  NE2 . GLN   B 1 305 ? 18.103  -12.075 -26.702 1   45.09 ? 290 GLN   B NE2 1 
ATOM   5282 N  N   . PHE   B 1 306 ? 17.767  -7.052  -25.185 1   34.03 ? 291 PHE   B N   1 
ATOM   5283 C  CA  . PHE   B 1 306 ? 19.002  -6.358  -24.837 1   33.96 ? 291 PHE   B CA  1 
ATOM   5284 C  C   . PHE   B 1 306 ? 19.353  -6.509  -23.358 1   32.99 ? 291 PHE   B C   1 
ATOM   5285 O  O   . PHE   B 1 306 ? 20.471  -6.863  -23.049 1   32.75 ? 291 PHE   B O   1 
ATOM   5286 C  CB  . PHE   B 1 306 ? 18.926  -4.87   -25.245 1   34.54 ? 291 PHE   B CB  1 
ATOM   5287 C  CG  . PHE   B 1 306 ? 20.179  -4.098  -24.878 1   35.3  ? 291 PHE   B CG  1 
ATOM   5288 C  CD1 . PHE   B 1 306 ? 21.364  -4.292  -25.575 1   35.66 ? 291 PHE   B CD1 1 
ATOM   5289 C  CD2 . PHE   B 1 306 ? 20.181  -3.207  -23.815 1   35.75 ? 291 PHE   B CD2 1 
ATOM   5290 C  CE1 . PHE   B 1 306 ? 22.512  -3.589  -25.226 1   36.23 ? 291 PHE   B CE1 1 
ATOM   5291 C  CE2 . PHE   B 1 306 ? 21.327  -2.499  -23.485 1   36.32 ? 291 PHE   B CE2 1 
ATOM   5292 C  CZ  . PHE   B 1 306 ? 22.485  -2.695  -24.195 1   35.95 ? 291 PHE   B CZ  1 
ATOM   5293 N  N   . LEU   B 1 307 ? 18.395  -6.247  -22.446 1   32.4  ? 292 LEU   B N   1 
ATOM   5294 C  CA  . LEU   B 1 307 ? 18.642  -6.365  -21.009 1   32.1  ? 292 LEU   B CA  1 
ATOM   5295 C  C   . LEU   B 1 307 ? 18.943  -7.799  -20.592 1   31.73 ? 292 LEU   B C   1 
ATOM   5296 O  O   . LEU   B 1 307 ? 19.788  -8.012  -19.721 1   31.62 ? 292 LEU   B O   1 
ATOM   5297 C  CB  . LEU   B 1 307 ? 17.474  -5.778  -20.206 1   32.16 ? 292 LEU   B CB  1 
ATOM   5298 C  CG  . LEU   B 1 307 ? 17.368  -4.246  -20.282 1   33.13 ? 292 LEU   B CG  1 
ATOM   5299 C  CD1 . LEU   B 1 307 ? 16.021  -3.748  -19.703 1   33.64 ? 292 LEU   B CD1 1 
ATOM   5300 C  CD2 . LEU   B 1 307 ? 18.573  -3.558  -19.624 1   32.86 ? 292 LEU   B CD2 1 
ATOM   5301 N  N   . GLN   B 1 308 ? 18.325  -8.782  -21.256 1   32.11 ? 293 GLN   B N   1 
ATOM   5302 C  CA  . GLN   B 1 308 ? 18.628  -10.18  -20.963 1   33.25 ? 293 GLN   B CA  1 
ATOM   5303 C  C   . GLN   B 1 308 ? 20.061  -10.489 -21.415 1   34.24 ? 293 GLN   B C   1 
ATOM   5304 O  O   . GLN   B 1 308 ? 20.838  -11.045 -20.648 1   34.8  ? 293 GLN   B O   1 
ATOM   5305 C  CB  . GLN   B 1 308 ? 17.629  -11.119 -21.661 1   35.43 ? 293 GLN   B CB  1 
ATOM   5306 C  CG  . GLN   B 1 308 ? 17.86   -12.61  -21.331 1   39.39 ? 293 GLN   B CG  1 
ATOM   5307 C  CD  . GLN   B 1 308 ? 17.823  -12.919 -19.846 1   44.19 ? 293 GLN   B CD  1 
ATOM   5308 O  OE1 . GLN   B 1 308 ? 18.684  -13.633 -19.313 1   46.73 ? 293 GLN   B OE1 1 
ATOM   5309 N  NE2 . GLN   B 1 308 ? 16.845  -12.372 -19.138 1   44.63 ? 293 GLN   B NE2 1 
ATOM   5310 N  N   . ASP   B 1 309 ? 20.429  -10.086 -22.651 1   34.56 ? 294 ASP   B N   1 
ATOM   5311 C  CA  . ASP   B 1 309 ? 21.785  -10.333 -23.151 1   34.36 ? 294 ASP   B CA  1 
ATOM   5312 C  C   . ASP   B 1 309 ? 22.844  -9.664  -22.271 1   32.75 ? 294 ASP   B C   1 
ATOM   5313 O  O   . ASP   B 1 309 ? 23.928  -10.231 -22.095 1   32.14 ? 294 ASP   B O   1 
ATOM   5314 C  CB  . ASP   B 1 309 ? 21.929  -9.836  -24.607 1   37.12 ? 294 ASP   B CB  1 
ATOM   5315 C  CG  . ASP   B 1 309 ? 21.114  -10.601 -25.638 1   43.88 ? 294 ASP   B CG  1 
ATOM   5316 O  OD1 . ASP   B 1 309 ? 20.611  -11.695 -25.309 1   44.94 ? 294 ASP   B OD1 1 
ATOM   5317 O  OD2 . ASP   B 1 309 ? 20.951  -10.088 -26.761 1   47.36 ? 294 ASP   B OD2 1 
ATOM   5318 N  N   . MET   B 1 310 ? 22.538  -8.468  -21.699 1   31.64 ? 295 MET   B N   1 
ATOM   5319 C  CA  . MET   B 1 310 ? 23.526  -7.773  -20.877 1   31.57 ? 295 MET   B CA  1 
ATOM   5320 C  C   . MET   B 1 310 ? 23.888  -8.468  -19.583 1   31.63 ? 295 MET   B C   1 
ATOM   5321 O  O   . MET   B 1 310 ? 24.931  -8.143  -19.016 1   30.88 ? 295 MET   B O   1 
ATOM   5322 C  CB  . MET   B 1 310 ? 23.122  -6.319  -20.609 1   32.5  ? 295 MET   B CB  1 
ATOM   5323 C  CG  . MET   B 1 310 ? 23.144  -5.445  -21.864 1   33.9  ? 295 MET   B CG  1 
ATOM   5324 S  SD  . MET   B 1 310 ? 24.725  -5.479  -22.764 1   35.94 ? 295 MET   B SD  1 
ATOM   5325 C  CE  . MET   B 1 310 ? 24.306  -6.637  -24.191 1   31.23 ? 295 MET   B CE  1 
ATOM   5326 N  N   . ARG   B 1 311 ? 23.087  -9.447  -19.129 1   32.5  ? 296 ARG   B N   1 
ATOM   5327 C  CA  . ARG   B 1 311 ? 23.406  -10.226 -17.909 1   33.55 ? 296 ARG   B CA  1 
ATOM   5328 C  C   . ARG   B 1 311 ? 24.642  -11.081 -18.061 1   35.3  ? 296 ARG   B C   1 
ATOM   5329 O  O   . ARG   B 1 311 ? 25.384  -11.284 -17.098 1   35.1  ? 296 ARG   B O   1 
ATOM   5330 C  CB  . ARG   B 1 311 ? 22.229  -11.095 -17.497 1   34.17 ? 296 ARG   B CB  1 
ATOM   5331 C  CG  . ARG   B 1 311 ? 21.011  -10.251 -17.188 1   35.36 ? 296 ARG   B CG  1 
ATOM   5332 C  CD  . ARG   B 1 311 ? 19.965  -11.1   -16.533 1   37.12 ? 296 ARG   B CD  1 
ATOM   5333 N  NE  . ARG   B 1 311 ? 18.819  -10.298 -16.124 1   39.33 ? 296 ARG   B NE  1 
ATOM   5334 C  CZ  . ARG   B 1 311 ? 17.743  -10.785 -15.516 1   41.75 ? 296 ARG   B CZ  1 
ATOM   5335 N  NH1 . ARG   B 1 311 ? 17.663  -12.08  -15.229 1   40.83 ? 296 ARG   B NH1 1 
ATOM   5336 N  NH2 . ARG   B 1 311 ? 16.741  -9.981  -15.187 1   42.59 ? 296 ARG   B NH2 1 
ATOM   5337 N  N   . ARG   B 1 312 ? 24.9    -11.55  -19.287 1   36.74 ? 297 ARG   B N   1 
ATOM   5338 C  CA  . ARG   B 1 312 ? 26.116  -12.308 -19.565 1   38.38 ? 297 ARG   B CA  1 
ATOM   5339 C  C   . ARG   B 1 312 ? 27.368  -11.408 -19.576 1   37.31 ? 297 ARG   B C   1 
ATOM   5340 O  O   . ARG   B 1 312 ? 28.469  -11.919 -19.69  1   37.01 ? 297 ARG   B O   1 
ATOM   5341 C  CB  . ARG   B 1 312 ? 25.97   -13.072 -20.894 1   42.9  ? 297 ARG   B CB  1 
ATOM   5342 C  CG  . ARG   B 1 312 ? 26.348  -14.539 -20.764 1   51.85 ? 297 ARG   B CG  1 
ATOM   5343 C  CD  . ARG   B 1 312 ? 25.416  -15.458 -21.535 1   58.51 ? 297 ARG   B CD  1 
ATOM   5344 N  NE  . ARG   B 1 312 ? 24.575  -16.268 -20.649 1   64.8  ? 297 ARG   B NE  1 
ATOM   5345 C  CZ  . ARG   B 1 312 ? 24.922  -17.457 -20.155 1   70.07 ? 297 ARG   B CZ  1 
ATOM   5346 N  NH1 . ARG   B 1 312 ? 26.109  -17.984 -20.446 1   71.39 ? 297 ARG   B NH1 1 
ATOM   5347 N  NH2 . ARG   B 1 312 ? 24.083  -18.129 -19.372 1   69.65 ? 297 ARG   B NH2 1 
ATOM   5348 N  N   . TYR   B 1 313 ? 27.205  -10.075 -19.466 1   36.23 ? 298 TYR   B N   1 
ATOM   5349 C  CA  . TYR   B 1 313 ? 28.304  -9.13   -19.383 1   35.75 ? 298 TYR   B CA  1 
ATOM   5350 C  C   . TYR   B 1 313 ? 28.535  -8.648  -17.953 1   35.37 ? 298 TYR   B C   1 
ATOM   5351 O  O   . TYR   B 1 313 ? 29.355  -7.754  -17.742 1   35.97 ? 298 TYR   B O   1 
ATOM   5352 C  CB  . TYR   B 1 313 ? 28.04   -7.93   -20.28  1   35.78 ? 298 TYR   B CB  1 
ATOM   5353 C  CG  . TYR   B 1 313 ? 28.075  -8.228  -21.762 1   36.58 ? 298 TYR   B CG  1 
ATOM   5354 C  CD1 . TYR   B 1 313 ? 27.075  -8.973  -22.364 1   37.38 ? 298 TYR   B CD1 1 
ATOM   5355 C  CD2 . TYR   B 1 313 ? 29.06   -7.689  -22.576 1   37.27 ? 298 TYR   B CD2 1 
ATOM   5356 C  CE1 . TYR   B 1 313 ? 27.082  -9.218  -23.73  1   38.31 ? 298 TYR   B CE1 1 
ATOM   5357 C  CE2 . TYR   B 1 313 ? 29.051  -7.887  -23.951 1   38.16 ? 298 TYR   B CE2 1 
ATOM   5358 C  CZ  . TYR   B 1 313 ? 28.075  -8.676  -24.521 1   39.47 ? 298 TYR   B CZ  1 
ATOM   5359 O  OH  . TYR   B 1 313 ? 28.084  -8.907  -25.875 1   42.2  ? 298 TYR   B OH  1 
ATOM   5360 N  N   . MET   B 1 314 ? 27.79   -9.203  -16.969 1   34.1  ? 299 MET   B N   1 
ATOM   5361 C  CA  . MET   B 1 314 ? 27.927  -8.893  -15.554 1   33.48 ? 299 MET   B CA  1 
ATOM   5362 C  C   . MET   B 1 314 ? 28.841  -9.928  -14.927 1   33.24 ? 299 MET   B C   1 
ATOM   5363 O  O   . MET   B 1 314 ? 28.849  -11.06  -15.39  1   33.84 ? 299 MET   B O   1 
ATOM   5364 C  CB  . MET   B 1 314 ? 26.545  -9.019  -14.868 1   33.02 ? 299 MET   B CB  1 
ATOM   5365 C  CG  . MET   B 1 314 ? 25.502  -8.106  -15.451 1   33.5  ? 299 MET   B CG  1 
ATOM   5366 S  SD  . MET   B 1 314 ? 23.955  -8.315  -14.522 1   34.92 ? 299 MET   B SD  1 
ATOM   5367 C  CE  . MET   B 1 314 ? 22.929  -7.089  -15.34  1   27.36 ? 299 MET   B CE  1 
ATOM   5368 N  N   . PRO   B 1 315 ? 29.524  -9.622  -13.808 1   33.03 ? 300 PRO   B N   1 
ATOM   5369 C  CA  . PRO   B 1 315 ? 30.295  -10.665 -13.11  1   33.94 ? 300 PRO   B CA  1 
ATOM   5370 C  C   . PRO   B 1 315 ? 29.388  -11.854 -12.74  1   35.38 ? 300 PRO   B C   1 
ATOM   5371 O  O   . PRO   B 1 315 ? 28.187  -11.675 -12.491 1   35.49 ? 300 PRO   B O   1 
ATOM   5372 C  CB  . PRO   B 1 315 ? 30.823  -9.946  -11.863 1   34.79 ? 300 PRO   B CB  1 
ATOM   5373 C  CG  . PRO   B 1 315 ? 30.857  -8.502  -12.252 1   35.31 ? 300 PRO   B CG  1 
ATOM   5374 C  CD  . PRO   B 1 315 ? 29.63   -8.325  -13.121 1   32.97 ? 300 PRO   B CD  1 
ATOM   5375 N  N   . PRO   B 1 316 ? 29.913  -13.084 -12.85  1   35.72 ? 301 PRO   B N   1 
ATOM   5376 C  CA  . PRO   B 1 316 ? 29.07   -14.26  -12.629 1   35.85 ? 301 PRO   B CA  1 
ATOM   5377 C  C   . PRO   B 1 316 ? 28.337  -14.278 -11.294 1   35.59 ? 301 PRO   B C   1 
ATOM   5378 O  O   . PRO   B 1 316 ? 27.169  -14.611 -11.311 1   36.2  ? 301 PRO   B O   1 
ATOM   5379 C  CB  . PRO   B 1 316 ? 30.027  -15.452 -12.81  1   37.06 ? 301 PRO   B CB  1 
ATOM   5380 C  CG  . PRO   B 1 316 ? 31.392  -14.873 -12.761 1   37.4  ? 301 PRO   B CG  1 
ATOM   5381 C  CD  . PRO   B 1 316 ? 31.292  -13.456 -13.216 1   35.29 ? 301 PRO   B CD  1 
ATOM   5382 N  N   . ALA   B 1 317 ? 28.946  -13.849 -10.193 1   35.55 ? 302 ALA   B N   1 
ATOM   5383 C  CA  . ALA   B 1 317 ? 28.257  -13.818 -8.9    1   36.14 ? 302 ALA   B CA  1 
ATOM   5384 C  C   . ALA   B 1 317 ? 27.047  -12.878 -8.911  1   35.96 ? 302 ALA   B C   1 
ATOM   5385 O  O   . ALA   B 1 317 ? 26.048  -13.167 -8.255  1   35.5  ? 302 ALA   B O   1 
ATOM   5386 C  CB  . ALA   B 1 317 ? 29.212  -13.429 -7.791  1   36.47 ? 302 ALA   B CB  1 
ATOM   5387 N  N   . HIS   B 1 318 ? 27.127  -11.764 -9.681  1   35.36 ? 303 HIS   B N   1 
ATOM   5388 C  CA  . HIS   B 1 318 ? 26.034  -10.776 -9.807  1   34.25 ? 303 HIS   B CA  1 
ATOM   5389 C  C   . HIS   B 1 318 ? 24.921  -11.261 -10.718 1   33.78 ? 303 HIS   B C   1 
ATOM   5390 O  O   . HIS   B 1 318 ? 23.746  -11.011 -10.466 1   33.39 ? 303 HIS   B O   1 
ATOM   5391 C  CB  . HIS   B 1 318 ? 26.609  -9.428  -10.246 1   34.38 ? 303 HIS   B CB  1 
ATOM   5392 C  CG  . HIS   B 1 318 ? 27.648  -8.882  -9.304  1   34.9  ? 303 HIS   B CG  1 
ATOM   5393 N  ND1 . HIS   B 1 318 ? 28.396  -7.767  -9.632  1   36.7  ? 303 HIS   B ND1 1 
ATOM   5394 C  CD2 . HIS   B 1 318 ? 27.963  -9.256  -8.035  1   35.62 ? 303 HIS   B CD2 1 
ATOM   5395 C  CE1 . HIS   B 1 318 ? 29.173  -7.537  -8.584  1   37.29 ? 303 HIS   B CE1 1 
ATOM   5396 N  NE2 . HIS   B 1 318 ? 28.94   -8.41   -7.596  1   36.74 ? 303 HIS   B NE2 1 
ATOM   5397 N  N   . ARG   B 1 319 ? 25.288  -11.996 -11.758 1   33.57 ? 304 ARG   B N   1 
ATOM   5398 C  CA  . ARG   B 1 319 ? 24.36   -12.659 -12.658 1   34.75 ? 304 ARG   B CA  1 
ATOM   5399 C  C   . ARG   B 1 319 ? 23.62   -13.777 -11.834 1   35.04 ? 304 ARG   B C   1 
ATOM   5400 O  O   . ARG   B 1 319 ? 22.421  -13.984 -12.005 1   35.57 ? 304 ARG   B O   1 
ATOM   5401 C  CB  . ARG   B 1 319 ? 25.202  -13.286 -13.767 1   37.15 ? 304 ARG   B CB  1 
ATOM   5402 C  CG  . ARG   B 1 319 ? 24.478  -13.906 -14.953 1   43.4  ? 304 ARG   B CG  1 
ATOM   5403 C  CD  . ARG   B 1 319 ? 25.506  -14.544 -15.937 1   47.84 ? 304 ARG   B CD  1 
ATOM   5404 N  NE  . ARG   B 1 319 ? 26.791  -13.826 -15.966 1   49.79 ? 304 ARG   B NE  1 
ATOM   5405 C  CZ  . ARG   B 1 319 ? 27.939  -14.343 -16.394 1   52.88 ? 304 ARG   B CZ  1 
ATOM   5406 N  NH1 . ARG   B 1 319 ? 27.976  -15.572 -16.889 1   54.01 ? 304 ARG   B NH1 1 
ATOM   5407 N  NH2 . ARG   B 1 319 ? 29.056  -13.624 -16.347 1   51.61 ? 304 ARG   B NH2 1 
ATOM   5408 N  N   . ASN   B 1 320 ? 24.334  -14.48  -10.935 1   34.75 ? 305 ASN   B N   1 
ATOM   5409 C  CA  . ASN   B 1 320 ? 23.757  -15.524 -10.07  1   34.99 ? 305 ASN   B CA  1 
ATOM   5410 C  C   . ASN   B 1 320 ? 22.758  -14.887 -9.092  1   34.68 ? 305 ASN   B C   1 
ATOM   5411 O  O   . ASN   B 1 320 ? 21.693  -15.46  -8.817  1   35.24 ? 305 ASN   B O   1 
ATOM   5412 C  CB  . ASN   B 1 320 ? 24.858  -16.233 -9.258  1   36.24 ? 305 ASN   B CB  1 
ATOM   5413 C  CG  . ASN   B 1 320 ? 25.791  -17.091 -10.09  1   38.84 ? 305 ASN   B CG  1 
ATOM   5414 O  OD1 . ASN   B 1 320 ? 25.532  -17.365 -11.264 1   39.97 ? 305 ASN   B OD1 1 
ATOM   5415 N  ND2 . ASN   B 1 320 ? 26.896  -17.523 -9.493  1   39.68 ? 305 ASN   B ND2 1 
ATOM   5416 N  N   . PHE   B 1 321 ? 23.098  -13.697 -8.566  1   33.07 ? 306 PHE   B N   1 
ATOM   5417 C  CA  . PHE   B 1 321 ? 22.216  -12.974 -7.663  1   33.21 ? 306 PHE   B CA  1 
ATOM   5418 C  C   . PHE   B 1 321 ? 20.893  -12.649 -8.339  1   32.73 ? 306 PHE   B C   1 
ATOM   5419 O  O   . PHE   B 1 321 ? 19.837  -12.905 -7.751  1   31.53 ? 306 PHE   B O   1 
ATOM   5420 C  CB  . PHE   B 1 321 ? 22.888  -11.709 -7.13   1   33.71 ? 306 PHE   B CB  1 
ATOM   5421 C  CG  . PHE   B 1 321 ? 22.02   -10.987 -6.133  1   34.77 ? 306 PHE   B CG  1 
ATOM   5422 C  CD1 . PHE   B 1 321 ? 21.807  -11.51  -4.868  1   35.88 ? 306 PHE   B CD1 1 
ATOM   5423 C  CD2 . PHE   B 1 321 ? 21.318  -9.849  -6.497  1   35.26 ? 306 PHE   B CD2 1 
ATOM   5424 C  CE1 . PHE   B 1 321 ? 20.979  -10.846 -3.953  1   36.35 ? 306 PHE   B CE1 1 
ATOM   5425 C  CE2 . PHE   B 1 321 ? 20.495  -9.198  -5.588  1   35.76 ? 306 PHE   B CE2 1 
ATOM   5426 C  CZ  . PHE   B 1 321 ? 20.337  -9.693  -4.322  1   35.71 ? 306 PHE   B CZ  1 
ATOM   5427 N  N   . LEU   B 1 322 ? 20.946  -12.162 -9.604  1   33.45 ? 307 LEU   B N   1 
ATOM   5428 C  CA  . LEU   B 1 322 ? 19.74   -11.863 -10.378 1   34.83 ? 307 LEU   B CA  1 
ATOM   5429 C  C   . LEU   B 1 322 ? 18.848  -13.106 -10.579 1   36.31 ? 307 LEU   B C   1 
ATOM   5430 O  O   . LEU   B 1 322 ? 17.637  -13.014 -10.383 1   35.74 ? 307 LEU   B O   1 
ATOM   5431 C  CB  . LEU   B 1 322 ? 20.086  -11.223 -11.725 1   35.17 ? 307 LEU   B CB  1 
ATOM   5432 C  CG  . LEU   B 1 322 ? 20.501  -9.765  -11.637 1   37.34 ? 307 LEU   B CG  1 
ATOM   5433 C  CD1 . LEU   B 1 322 ? 20.975  -9.234  -12.983 1   37.34 ? 307 LEU   B CD1 1 
ATOM   5434 C  CD2 . LEU   B 1 322 ? 19.336  -8.931  -11.242 1   38.21 ? 307 LEU   B CD2 1 
ATOM   5435 N  N   . CYS   B 1 323 ? 19.436  -14.259 -10.95  1   37.64 ? 308 CYS   B N   1 
ATOM   5436 C  CA  . CYS   B 1 323 ? 18.733  -15.555 -11.092 1   39.64 ? 308 CYS   B CA  1 
ATOM   5437 C  C   . CYS   B 1 323 ? 17.991  -15.892 -9.779  1   39.83 ? 308 CYS   B C   1 
ATOM   5438 O  O   . CYS   B 1 323 ? 16.838  -16.28  -9.808  1   40.19 ? 308 CYS   B O   1 
ATOM   5439 C  CB  . CYS   B 1 323 ? 19.749  -16.658 -11.433 1   41.67 ? 308 CYS   B CB  1 
ATOM   5440 S  SG  . CYS   B 1 323 ? 19.178  -18.356 -11.081 1   47.28 ? 308 CYS   B SG  1 
ATOM   5441 N  N   . SER   B 1 324 ? 18.697  -15.803 -8.659  1   40.19 ? 309 SER   B N   1 
ATOM   5442 C  CA  . SER   B 1 324 ? 18.206  -16.102 -7.323  1   41.24 ? 309 SER   B CA  1 
ATOM   5443 C  C   . SER   B 1 324 ? 17.052  -15.175 -6.949  1   41.67 ? 309 SER   B C   1 
ATOM   5444 O  O   . SER   B 1 324 ? 16.072  -15.627 -6.34   1   41.48 ? 309 SER   B O   1 
ATOM   5445 C  CB  . SER   B 1 324 ? 19.327  -15.956 -6.303  1   43.51 ? 309 SER   B CB  1 
ATOM   5446 O  OG  . SER   B 1 324 ? 20.271  -17.013 -6.377  1   48.01 ? 309 SER   B OG  1 
ATOM   5447 N  N   . LEU   B 1 325 ? 17.155  -13.876 -7.307  1   41.02 ? 310 LEU   B N   1 
ATOM   5448 C  CA  . LEU   B 1 325 ? 16.062  -12.943 -7.053  1   41.49 ? 310 LEU   B CA  1 
ATOM   5449 C  C   . LEU   B 1 325 ? 14.826  -13.358 -7.837  1   41.22 ? 310 LEU   B C   1 
ATOM   5450 O  O   . LEU   B 1 325 ? 13.72   -13.302 -7.306  1   40.99 ? 310 LEU   B O   1 
ATOM   5451 C  CB  . LEU   B 1 325 ? 16.442  -11.521 -7.486  1   42.11 ? 310 LEU   B CB  1 
ATOM   5452 C  CG  . LEU   B 1 325 ? 17.077  -10.625 -6.474  1   44.84 ? 310 LEU   B CG  1 
ATOM   5453 C  CD1 . LEU   B 1 325 ? 17.189  -9.233  -7.043  1   45.7  ? 310 LEU   B CD1 1 
ATOM   5454 C  CD2 . LEU   B 1 325 ? 16.235  -10.554 -5.197  1   45.62 ? 310 LEU   B CD2 1 
ATOM   5455 N  N   . GLU   B 1 326 ? 15.024  -13.775 -9.104  1   41.34 ? 311 GLU   B N   1 
ATOM   5456 C  CA  . GLU   B 1 326 ? 13.972  -14.214 -10.01  1   43    ? 311 GLU   B CA  1 
ATOM   5457 C  C   . GLU   B 1 326 ? 13.291  -15.487 -9.562  1   44.63 ? 311 GLU   B C   1 
ATOM   5458 O  O   . GLU   B 1 326 ? 12.129  -15.691 -9.912  1   45.86 ? 311 GLU   B O   1 
ATOM   5459 C  CB  . GLU   B 1 326 ? 14.549  -14.439 -11.405 1   45.38 ? 311 GLU   B CB  1 
ATOM   5460 C  CG  . GLU   B 1 326 ? 14.298  -13.288 -12.349 1   50.52 ? 311 GLU   B CG  1 
ATOM   5461 C  CD  . GLU   B 1 326 ? 15.119  -13.326 -13.624 1   56.73 ? 311 GLU   B CD  1 
ATOM   5462 O  OE1 . GLU   B 1 326 ? 16.055  -14.155 -13.717 1   58.03 ? 311 GLU   B OE1 1 
ATOM   5463 O  OE2 . GLU   B 1 326 ? 14.824  -12.52  -14.533 1   57.98 ? 311 GLU   B OE2 1 
ATOM   5464 N  N   . SER   B 1 327 ? 14.012  -16.352 -8.843  1   44.69 ? 312 SER   B N   1 
ATOM   5465 C  CA  . SER   B 1 327 ? 13.51   -17.626 -8.331  1   45.87 ? 312 SER   B CA  1 
ATOM   5466 C  C   . SER   B 1 327 ? 12.601  -17.444 -7.101  1   45.16 ? 312 SER   B C   1 
ATOM   5467 O  O   . SER   B 1 327 ? 11.847  -18.353 -6.766  1   45.35 ? 312 SER   B O   1 
ATOM   5468 C  CB  . SER   B 1 327 ? 14.671  -18.556 -7.994  1   49.14 ? 312 SER   B CB  1 
ATOM   5469 O  OG  . SER   B 1 327 ? 15.393  -18.914 -9.168  1   55.1  ? 312 SER   B OG  1 
ATOM   5470 N  N   . ASN   B 1 328 ? 12.696  -16.291 -6.419  1   43.71 ? 313 ASN   B N   1 
ATOM   5471 C  CA  . ASN   B 1 328 ? 11.876  -15.99  -5.259  1   42.82 ? 313 ASN   B CA  1 
ATOM   5472 C  C   . ASN   B 1 328 ? 10.472  -15.59  -5.676  1   42.23 ? 313 ASN   B C   1 
ATOM   5473 O  O   . ASN   B 1 328 ? 10.259  -15.178 -6.818  1   42.28 ? 313 ASN   B O   1 
ATOM   5474 C  CB  . ASN   B 1 328 ? 12.534  -14.891 -4.441  1   42.8  ? 313 ASN   B CB  1 
ATOM   5475 C  CG  . ASN   B 1 328 ? 13.605  -15.435 -3.569  1   44.17 ? 313 ASN   B CG  1 
ATOM   5476 O  OD1 . ASN   B 1 328 ? 14.751  -15.624 -4.006  1   45.2  ? 313 ASN   B OD1 1 
ATOM   5477 N  ND2 . ASN   B 1 328 ? 13.242  -15.745 -2.333  1   43.56 ? 313 ASN   B ND2 1 
ATOM   5478 N  N   . PRO   B 1 329 ? 9.476   -15.733 -4.782  1   42.13 ? 314 PRO   B N   1 
ATOM   5479 C  CA  . PRO   B 1 329 ? 8.109   -15.331 -5.158  1   41.41 ? 314 PRO   B CA  1 
ATOM   5480 C  C   . PRO   B 1 329 ? 8.028   -13.855 -5.533  1   40.78 ? 314 PRO   B C   1 
ATOM   5481 O  O   . PRO   B 1 329 ? 8.862   -13.044 -5.136  1   40.96 ? 314 PRO   B O   1 
ATOM   5482 C  CB  . PRO   B 1 329 ? 7.259   -15.635 -3.912  1   42.7  ? 314 PRO   B CB  1 
ATOM   5483 C  CG  . PRO   B 1 329 ? 8.147   -16.275 -2.926  1   43.51 ? 314 PRO   B CG  1 
ATOM   5484 C  CD  . PRO   B 1 329 ? 9.573   -16.188 -3.38   1   41.84 ? 314 PRO   B CD  1 
ATOM   5485 N  N   . SER   B 1 330 ? 7.038   -13.522 -6.323  1   39.91 ? 315 SER   B N   1 
ATOM   5486 C  CA  . SER   B 1 330 ? 6.808   -12.175 -6.795  1   39.59 ? 315 SER   B CA  1 
ATOM   5487 C  C   . SER   B 1 330 ? 6.235   -11.271 -5.684  1   39.55 ? 315 SER   B C   1 
ATOM   5488 O  O   . SER   B 1 330 ? 5.167   -11.55  -5.124  1   38.14 ? 315 SER   B O   1 
ATOM   5489 C  CB  . SER   B 1 330 ? 5.839   -12.221 -7.969  1   39.99 ? 315 SER   B CB  1 
ATOM   5490 O  OG  . SER   B 1 330 ? 5.463   -10.929 -8.411  1   42.54 ? 315 SER   B OG  1 
ATOM   5491 N  N   . VAL   B 1 331 ? 6.944   -10.176 -5.393  1   39.29 ? 316 VAL   B N   1 
ATOM   5492 C  CA  . VAL   B 1 331 ? 6.516   -9.161  -4.445  1   39.27 ? 316 VAL   B CA  1 
ATOM   5493 C  C   . VAL   B 1 331 ? 5.232   -8.512  -4.956  1   38.28 ? 316 VAL   B C   1 
ATOM   5494 O  O   . VAL   B 1 331 ? 4.294   -8.317  -4.184  1   38.18 ? 316 VAL   B O   1 
ATOM   5495 C  CB  . VAL   B 1 331 ? 7.645   -8.116  -4.258  1   40.02 ? 316 VAL   B CB  1 
ATOM   5496 C  CG1 . VAL   B 1 331 ? 7.161   -6.912  -3.468  1   40.34 ? 316 VAL   B CG1 1 
ATOM   5497 C  CG2 . VAL   B 1 331 ? 8.852   -8.753  -3.583  1   40.32 ? 316 VAL   B CG2 1 
ATOM   5498 N  N   . ARG   B 1 332 ? 5.18    -8.205  -6.267  1   37.37 ? 317 ARG   B N   1 
ATOM   5499 C  CA  . ARG   B 1 332 ? 4.037   -7.592  -6.921  1   37.18 ? 317 ARG   B CA  1 
ATOM   5500 C  C   . ARG   B 1 332 ? 2.798   -8.471  -6.797  1   38.1  ? 317 ARG   B C   1 
ATOM   5501 O  O   . ARG   B 1 332 ? 1.734   -7.959  -6.497  1   37.1  ? 317 ARG   B O   1 
ATOM   5502 C  CB  . ARG   B 1 332 ? 4.335   -7.341  -8.404  1   37.03 ? 317 ARG   B CB  1 
ATOM   5503 C  CG  . ARG   B 1 332 ? 3.152   -6.763  -9.175  1   37.9  ? 317 ARG   B CG  1 
ATOM   5504 C  CD  . ARG   B 1 332 ? 3.537   -6.34   -10.574 1   39.25 ? 317 ARG   B CD  1 
ATOM   5505 N  NE  . ARG   B 1 332 ? 2.726   -5.199  -11.02  1   40.09 ? 317 ARG   B NE  1 
ATOM   5506 C  CZ  . ARG   B 1 332 ? 1.62    -5.32   -11.747 1   45.51 ? 317 ARG   B CZ  1 
ATOM   5507 N  NH1 . ARG   B 1 332 ? 1.178   -6.521  -12.105 1   48.13 ? 317 ARG   B NH1 1 
ATOM   5508 N  NH2 . ARG   B 1 332 ? 0.924   -4.247  -12.091 1   46.25 ? 317 ARG   B NH2 1 
ATOM   5509 N  N   . GLU   B 1 333 ? 2.934   -9.78   -7.063  1   38.63 ? 318 GLU   B N   1 
ATOM   5510 C  CA  . GLU   B 1 333 ? 1.817   -10.711 -6.969  1   39.98 ? 318 GLU   B CA  1 
ATOM   5511 C  C   . GLU   B 1 333 ? 1.317   -10.8   -5.534  1   39.53 ? 318 GLU   B C   1 
ATOM   5512 O  O   . GLU   B 1 333 ? 0.102   -10.774 -5.312  1   39.69 ? 318 GLU   B O   1 
ATOM   5513 C  CB  . GLU   B 1 333 ? 2.224   -12.087 -7.512  1   44.66 ? 318 GLU   B CB  1 
ATOM   5514 C  CG  . GLU   B 1 333 ? 1.117   -12.817 -8.245  1   53.82 ? 318 GLU   B CG  1 
ATOM   5515 C  CD  . GLU   B 1 333 ? 0.658   -12.202 -9.555  1   63.47 ? 318 GLU   B CD  1 
ATOM   5516 O  OE1 . GLU   B 1 333 ? -0.29   -12.765 -10.15  1   65.49 ? 318 GLU   B OE1 1 
ATOM   5517 O  OE2 . GLU   B 1 333 ? 1.233   -11.173 -9.989  1   65.31 ? 318 GLU   B OE2 1 
ATOM   5518 N  N   . PHE   B 1 334 ? 2.244   -10.842 -4.559  1   38.59 ? 319 PHE   B N   1 
ATOM   5519 C  CA  . PHE   B 1 334 ? 1.888   -10.885 -3.138  1   39.25 ? 319 PHE   B CA  1 
ATOM   5520 C  C   . PHE   B 1 334 ? 1.078   -9.639  -2.751  1   38.92 ? 319 PHE   B C   1 
ATOM   5521 O  O   . PHE   B 1 334 ? 0.011   -9.765  -2.167  1   38.33 ? 319 PHE   B O   1 
ATOM   5522 C  CB  . PHE   B 1 334 ? 3.157   -10.98  -2.269  1   39.75 ? 319 PHE   B CB  1 
ATOM   5523 C  CG  . PHE   B 1 334 ? 2.917   -11.17  -0.784  1   41.06 ? 319 PHE   B CG  1 
ATOM   5524 C  CD1 . PHE   B 1 334 ? 2.672   -10.083 0.044   1   41.84 ? 319 PHE   B CD1 1 
ATOM   5525 C  CD2 . PHE   B 1 334 ? 2.96    -12.434 -0.212  1   41.77 ? 319 PHE   B CD2 1 
ATOM   5526 C  CE1 . PHE   B 1 334 ? 2.446   -10.262 1.406   1   42.38 ? 319 PHE   B CE1 1 
ATOM   5527 C  CE2 . PHE   B 1 334 ? 2.757   -12.604 1.153   1   42.52 ? 319 PHE   B CE2 1 
ATOM   5528 C  CZ  . PHE   B 1 334 ? 2.522   -11.514 1.956   1   42.3  ? 319 PHE   B CZ  1 
ATOM   5529 N  N   . VAL   B 1 335 ? 1.576   -8.437  -3.101  1   38.63 ? 320 VAL   B N   1 
ATOM   5530 C  CA  . VAL   B 1 335 ? 0.923   -7.178  -2.78   1   38.31 ? 320 VAL   B CA  1 
ATOM   5531 C  C   . VAL   B 1 335 ? -0.445  -7.076  -3.472  1   39.66 ? 320 VAL   B C   1 
ATOM   5532 O  O   . VAL   B 1 335 ? -1.429  -6.653  -2.856  1   39.76 ? 320 VAL   B O   1 
ATOM   5533 C  CB  . VAL   B 1 335 ? 1.857   -5.992  -3.107  1   37.57 ? 320 VAL   B CB  1 
ATOM   5534 C  CG1 . VAL   B 1 335 ? 1.097   -4.682  -3.065  1   38.07 ? 320 VAL   B CG1 1 
ATOM   5535 C  CG2 . VAL   B 1 335 ? 3.034   -5.949  -2.144  1   37.11 ? 320 VAL   B CG2 1 
ATOM   5536 N  N   . LEU   B 1 336 ? -0.519  -7.488  -4.73   1   40.55 ? 321 LEU   B N   1 
ATOM   5537 C  CA  . LEU   B 1 336 ? -1.762  -7.448  -5.487  1   42.95 ? 321 LEU   B CA  1 
ATOM   5538 C  C   . LEU   B 1 336 ? -2.85   -8.351  -4.879  1   44.42 ? 321 LEU   B C   1 
ATOM   5539 O  O   . LEU   B 1 336 ? -4.036  -8.071  -5.052  1   45.66 ? 321 LEU   B O   1 
ATOM   5540 C  CB  . LEU   B 1 336 ? -1.513  -7.922  -6.922  1   44.23 ? 321 LEU   B CB  1 
ATOM   5541 C  CG  . LEU   B 1 336 ? -1.331  -6.868  -7.973  1   47.45 ? 321 LEU   B CG  1 
ATOM   5542 C  CD1 . LEU   B 1 336 ? -0.959  -7.504  -9.313  1   48.21 ? 321 LEU   B CD1 1 
ATOM   5543 C  CD2 . LEU   B 1 336 ? -2.585  -6.01   -8.109  1   48.54 ? 321 LEU   B CD2 1 
ATOM   5544 N  N   . SER   B 1 337 ? -2.457  -9.431  -4.2    1   44.25 ? 322 SER   B N   1 
ATOM   5545 C  CA  . SER   B 1 337 ? -3.41   -10.392 -3.673  1   44.61 ? 322 SER   B CA  1 
ATOM   5546 C  C   . SER   B 1 337 ? -3.933  -10.086 -2.269  1   45.65 ? 322 SER   B C   1 
ATOM   5547 O  O   . SER   B 1 337 ? -4.722  -10.877 -1.757  1   46.07 ? 322 SER   B O   1 
ATOM   5548 C  CB  . SER   B 1 337 ? -2.784  -11.777 -3.67   1   44.12 ? 322 SER   B CB  1 
ATOM   5549 O  OG  . SER   B 1 337 ? -1.818  -11.895 -2.637  1   46    ? 322 SER   B OG  1 
ATOM   5550 N  N   . LYS   B 1 338 ? -3.483  -8.987  -1.629  1   45.14 ? 323 LYS   B N   1 
ATOM   5551 C  CA  . LYS   B 1 338 ? -3.843  -8.756  -0.237  1   44.45 ? 323 LYS   B CA  1 
ATOM   5552 C  C   . LYS   B 1 338 ? -4.967  -7.768  0.075   1   43.8  ? 323 LYS   B C   1 
ATOM   5553 O  O   . LYS   B 1 338 ? -5.326  -7.693  1.264   1   45.1  ? 323 LYS   B O   1 
ATOM   5554 C  CB  . LYS   B 1 338 ? -2.602  -8.354  0.567   1   46.19 ? 323 LYS   B CB  1 
ATOM   5555 C  CG  . LYS   B 1 338 ? -1.524  -9.431  0.659   1   49.93 ? 323 LYS   B CG  1 
ATOM   5556 C  CD  . LYS   B 1 338 ? -2.068  -10.842 0.879   1   54.18 ? 323 LYS   B CD  1 
ATOM   5557 C  CE  . LYS   B 1 338 ? -0.963  -11.794 1.117   1   58.86 ? 323 LYS   B CE  1 
ATOM   5558 N  NZ  . LYS   B 1 338 ? -0.228  -11.336 2.315   1   63.53 ? 323 LYS   B NZ  1 
ATOM   5559 N  N   . GLY   B 1 339 ? -5.529  -7.065  -0.921  1   41.25 ? 324 GLY   B N   1 
ATOM   5560 C  CA  . GLY   B 1 339 ? -6.586  -6.06   -0.724  1   40.42 ? 324 GLY   B CA  1 
ATOM   5561 C  C   . GLY   B 1 339 ? -6.25   -5.058  0.368   1   39.41 ? 324 GLY   B C   1 
ATOM   5562 O  O   . GLY   B 1 339 ? -7.057  -4.777  1.256   1   39.4  ? 324 GLY   B O   1 
ATOM   5563 N  N   . ASP   B 1 340 ? -5.004  -4.571  0.347   1   37.86 ? 325 ASP   B N   1 
ATOM   5564 C  CA  . ASP   B 1 340 ? -4.461  -3.738  1.386   1   36.81 ? 325 ASP   B CA  1 
ATOM   5565 C  C   . ASP   B 1 340 ? -3.888  -2.469  0.754   1   37.53 ? 325 ASP   B C   1 
ATOM   5566 O  O   . ASP   B 1 340 ? -2.799  -2.503  0.174   1   36.82 ? 325 ASP   B O   1 
ATOM   5567 C  CB  . ASP   B 1 340 ? -3.373  -4.578  2.055   1   36.31 ? 325 ASP   B CB  1 
ATOM   5568 C  CG  . ASP   B 1 340 ? -2.644  -4.011  3.239   1   38.56 ? 325 ASP   B CG  1 
ATOM   5569 O  OD1 . ASP   B 1 340 ? -2.485  -2.765  3.309   1   38.92 ? 325 ASP   B OD1 1 
ATOM   5570 O  OD2 . ASP   B 1 340 ? -2.18   -4.807  4.07    1   39.57 ? 325 ASP   B OD2 1 
ATOM   5571 N  N   . ALA   B 1 341 ? -4.628  -1.366  0.871   1   38.07 ? 326 ALA   B N   1 
ATOM   5572 C  CA  . ALA   B 1 341 ? -4.27   -0.061  0.325   1   38.81 ? 326 ALA   B CA  1 
ATOM   5573 C  C   . ALA   B 1 341 ? -2.9    0.44    0.782   1   38.6  ? 326 ALA   B C   1 
ATOM   5574 O  O   . ALA   B 1 341 ? -2.139  0.9     -0.051  1   38.18 ? 326 ALA   B O   1 
ATOM   5575 C  CB  . ALA   B 1 341 ? -5.352  0.961   0.648   1   38.96 ? 326 ALA   B CB  1 
ATOM   5576 N  N   . GLY   B 1 342 ? -2.58   0.313   2.065   1   38.31 ? 327 GLY   B N   1 
ATOM   5577 C  CA  . GLY   B 1 342 ? -1.276  0.729   2.579   1   38.53 ? 327 GLY   B CA  1 
ATOM   5578 C  C   . GLY   B 1 342 ? -0.11   -0.025  1.95    1   38.13 ? 327 GLY   B C   1 
ATOM   5579 O  O   . GLY   B 1 342 ? 0.924   0.559   1.619   1   37.78 ? 327 GLY   B O   1 
ATOM   5580 N  N   . LEU   B 1 343 ? -0.265  -1.332  1.773   1   37.77 ? 328 LEU   B N   1 
ATOM   5581 C  CA  . LEU   B 1 343 ? 0.765   -2.164  1.164   1   38.09 ? 328 LEU   B CA  1 
ATOM   5582 C  C   . LEU   B 1 343 ? 0.892   -1.836  -0.348  1   37.98 ? 328 LEU   B C   1 
ATOM   5583 O  O   . LEU   B 1 343 ? 2.011   -1.772  -0.872  1   38.18 ? 328 LEU   B O   1 
ATOM   5584 C  CB  . LEU   B 1 343 ? 0.385   -3.63   1.384   1   38.17 ? 328 LEU   B CB  1 
ATOM   5585 C  CG  . LEU   B 1 343 ? 1.466   -4.67   1.337   1   39.54 ? 328 LEU   B CG  1 
ATOM   5586 C  CD1 . LEU   B 1 343 ? 2.598   -4.363  2.332   1   39.77 ? 328 LEU   B CD1 1 
ATOM   5587 C  CD2 . LEU   B 1 343 ? 0.867   -6.057  1.608   1   39.95 ? 328 LEU   B CD2 1 
ATOM   5588 N  N   A ARG   B 1 344 ? -0.239  -1.617  -1.03   0.5 37.8  ? 329 ARG   B N   1 
ATOM   5589 N  N   B ARG   B 1 344 ? -0.244  -1.614  -1.022  0.5 38.09 ? 329 ARG   B N   1 
ATOM   5590 C  CA  A ARG   B 1 344 ? -0.223  -1.258  -2.445  0.5 38.61 ? 329 ARG   B CA  1 
ATOM   5591 C  CA  B ARG   B 1 344 ? -0.278  -1.249  -2.437  0.5 39.19 ? 329 ARG   B CA  1 
ATOM   5592 C  C   A ARG   B 1 344 ? 0.445   0.097   -2.649  0.5 39.81 ? 329 ARG   B C   1 
ATOM   5593 C  C   B ARG   B 1 344 ? 0.415   0.096   -2.655  0.5 40.08 ? 329 ARG   B C   1 
ATOM   5594 O  O   A ARG   B 1 344 ? 1.19    0.269   -3.616  0.5 39.73 ? 329 ARG   B O   1 
ATOM   5595 O  O   B ARG   B 1 344 ? 1.156   0.256   -3.63   0.5 40.01 ? 329 ARG   B O   1 
ATOM   5596 C  CB  A ARG   B 1 344 ? -1.639  -1.226  -3.037  0.5 39.39 ? 329 ARG   B CB  1 
ATOM   5597 C  CB  B ARG   B 1 344 ? -1.728  -1.172  -2.953  0.5 40.77 ? 329 ARG   B CB  1 
ATOM   5598 C  CG  A ARG   B 1 344 ? -2.22   -2.615  -3.317  0.5 40.86 ? 329 ARG   B CG  1 
ATOM   5599 C  CG  B ARG   B 1 344 ? -2.358  -2.541  -3.207  0.5 43.88 ? 329 ARG   B CG  1 
ATOM   5600 C  CD  A ARG   B 1 344 ? -3.427  -2.579  -4.251  0.5 41.82 ? 329 ARG   B CD  1 
ATOM   5601 C  CD  B ARG   B 1 344 ? -3.852  -2.449  -3.475  0.5 46.52 ? 329 ARG   B CD  1 
ATOM   5602 N  NE  A ARG   B 1 344 ? -4.429  -1.594  -3.832  0.5 42.72 ? 329 ARG   B NE  1 
ATOM   5603 N  NE  B ARG   B 1 344 ? -4.162  -2.496  -4.903  0.5 48.38 ? 329 ARG   B NE  1 
ATOM   5604 C  CZ  A ARG   B 1 344 ? -5.388  -1.83   -2.943  0.5 42.26 ? 329 ARG   B CZ  1 
ATOM   5605 C  CZ  B ARG   B 1 344 ? -4.535  -3.591  -5.558  0.5 50.12 ? 329 ARG   B CZ  1 
ATOM   5606 N  NH1 A ARG   B 1 344 ? -5.498  -3.023  -2.378  0.5 40    ? 329 ARG   B NH1 1 
ATOM   5607 N  NH1 B ARG   B 1 344 ? -4.801  -3.536  -6.858  0.5 48.4  ? 329 ARG   B NH1 1 
ATOM   5608 N  NH2 A ARG   B 1 344 ? -6.247  -0.874  -2.618  0.5 41.93 ? 329 ARG   B NH2 1 
ATOM   5609 N  NH2 B ARG   B 1 344 ? -4.65   -4.749  -4.92   0.5 50.77 ? 329 ARG   B NH2 1 
ATOM   5610 N  N   . GLU   B 1 345 ? 0.18    1.052   -1.737  1   40.36 ? 330 GLU   B N   1 
ATOM   5611 C  CA  . GLU   B 1 345 ? 0.757   2.391   -1.786  1   41.18 ? 330 GLU   B CA  1 
ATOM   5612 C  C   . GLU   B 1 345 ? 2.273   2.335   -1.605  1   40.34 ? 330 GLU   B C   1 
ATOM   5613 O  O   . GLU   B 1 345 ? 2.979   3.038   -2.33   1   41.31 ? 330 GLU   B O   1 
ATOM   5614 C  CB  . GLU   B 1 345 ? 0.099   3.337   -0.739  1   44.63 ? 330 GLU   B CB  1 
ATOM   5615 C  CG  . GLU   B 1 345 ? 0.799   4.686   -0.6    1   53.81 ? 330 GLU   B CG  1 
ATOM   5616 C  CD  . GLU   B 1 345 ? 0.375   5.579   0.554   1   66.66 ? 330 GLU   B CD  1 
ATOM   5617 O  OE1 . GLU   B 1 345 ? -0.677  6.246   0.42    1   69.67 ? 330 GLU   B OE1 1 
ATOM   5618 O  OE2 . GLU   B 1 345 ? 1.102   5.637   1.576   1   69.77 ? 330 GLU   B OE2 1 
ATOM   5619 N  N   . ALA   B 1 346 ? 2.767   1.523   -0.656  1   38.63 ? 331 ALA   B N   1 
ATOM   5620 C  CA  . ALA   B 1 346 ? 4.201   1.341   -0.429  1   38.24 ? 331 ALA   B CA  1 
ATOM   5621 C  C   . ALA   B 1 346 ? 4.872   0.717   -1.681  1   37.7  ? 331 ALA   B C   1 
ATOM   5622 O  O   . ALA   B 1 346 ? 5.962   1.133   -2.077  1   37.96 ? 331 ALA   B O   1 
ATOM   5623 C  CB  . ALA   B 1 346 ? 4.442   0.454   0.794   1   38.03 ? 331 ALA   B CB  1 
ATOM   5624 N  N   . TYR   B 1 347 ? 4.215   -0.259  -2.304  1   36.5  ? 332 TYR   B N   1 
ATOM   5625 C  CA  . TYR   B 1 347 ? 4.753   -0.891  -3.504  1   35.82 ? 332 TYR   B CA  1 
ATOM   5626 C  C   . TYR   B 1 347 ? 4.82    0.142   -4.645  1   37.32 ? 332 TYR   B C   1 
ATOM   5627 O  O   . TYR   B 1 347 ? 5.828   0.227   -5.365  1   37.6  ? 332 TYR   B O   1 
ATOM   5628 C  CB  . TYR   B 1 347 ? 3.914   -2.114  -3.914  1   33.81 ? 332 TYR   B CB  1 
ATOM   5629 C  CG  . TYR   B 1 347 ? 4.287   -2.621  -5.29   1   32.06 ? 332 TYR   B CG  1 
ATOM   5630 C  CD1 . TYR   B 1 347 ? 3.647   -2.143  -6.423  1   31.29 ? 332 TYR   B CD1 1 
ATOM   5631 C  CD2 . TYR   B 1 347 ? 5.298   -3.558  -5.458  1   31.92 ? 332 TYR   B CD2 1 
ATOM   5632 C  CE1 . TYR   B 1 347 ? 3.999   -2.578  -7.684  1   31.83 ? 332 TYR   B CE1 1 
ATOM   5633 C  CE2 . TYR   B 1 347 ? 5.657   -4.004  -6.719  1   31.73 ? 332 TYR   B CE2 1 
ATOM   5634 C  CZ  . TYR   B 1 347 ? 5.018   -3.493  -7.83   1   32.39 ? 332 TYR   B CZ  1 
ATOM   5635 O  OH  . TYR   B 1 347 ? 5.358   -3.917  -9.083  1   33.13 ? 332 TYR   B OH  1 
ATOM   5636 N  N   . ASP   B 1 348 ? 3.748   0.923   -4.796  1   37.7  ? 333 ASP   B N   1 
ATOM   5637 C  CA  . ASP   B 1 348 ? 3.655   1.956   -5.812  1   38.78 ? 333 ASP   B CA  1 
ATOM   5638 C  C   . ASP   B 1 348 ? 4.663   3.071   -5.616  1   40    ? 333 ASP   B C   1 
ATOM   5639 O  O   . ASP   B 1 348 ? 5.136   3.619   -6.608  1   40.36 ? 333 ASP   B O   1 
ATOM   5640 C  CB  . ASP   B 1 348 ? 2.228   2.502   -5.926  1   39.4  ? 333 ASP   B CB  1 
ATOM   5641 C  CG  . ASP   B 1 348 ? 1.328   1.71    -6.854  1   42.77 ? 333 ASP   B CG  1 
ATOM   5642 O  OD1 . ASP   B 1 348 ? 1.792   0.716   -7.427  1   43.22 ? 333 ASP   B OD1 1 
ATOM   5643 O  OD2 . ASP   B 1 348 ? 0.166   2.091   -7.017  1   45.45 ? 333 ASP   B OD2 1 
ATOM   5644 N  N   . ALA   B 1 349 ? 5.044   3.366   -4.361  1   39.91 ? 334 ALA   B N   1 
ATOM   5645 C  CA  . ALA   B 1 349 ? 6.086   4.353   -4.089  1   40.23 ? 334 ALA   B CA  1 
ATOM   5646 C  C   . ALA   B 1 349 ? 7.433   3.864   -4.67   1   40.33 ? 334 ALA   B C   1 
ATOM   5647 O  O   . ALA   B 1 349 ? 8.218   4.686   -5.127  1   40.36 ? 334 ALA   B O   1 
ATOM   5648 C  CB  . ALA   B 1 349 ? 6.223   4.571   -2.591  1   40.33 ? 334 ALA   B CB  1 
ATOM   5649 N  N   . CYS   B 1 350 ? 7.702   2.532   -4.656  1   39.56 ? 335 CYS   B N   1 
ATOM   5650 C  CA  . CYS   B 1 350 ? 8.94    1.971   -5.204  1   38.96 ? 335 CYS   B CA  1 
ATOM   5651 C  C   . CYS   B 1 350 ? 8.936   2.108   -6.723  1   39.29 ? 335 CYS   B C   1 
ATOM   5652 O  O   . CYS   B 1 350 ? 9.919   2.544   -7.305  1   39.87 ? 335 CYS   B O   1 
ATOM   5653 C  CB  . CYS   B 1 350 ? 9.119   0.514   -4.788  1   39.02 ? 335 CYS   B CB  1 
ATOM   5654 S  SG  . CYS   B 1 350 ? 9.468   0.271   -3.037  1   39.73 ? 335 CYS   B SG  1 
ATOM   5655 N  N   . VAL   B 1 351 ? 7.843   1.72    -7.364  1   38.98 ? 336 VAL   B N   1 
ATOM   5656 C  CA  . VAL   B 1 351 ? 7.704   1.822   -8.802  1   39.44 ? 336 VAL   B CA  1 
ATOM   5657 C  C   . VAL   B 1 351 ? 7.771   3.28    -9.268  1   40.18 ? 336 VAL   B C   1 
ATOM   5658 O  O   . VAL   B 1 351 ? 8.507   3.579   -10.206 1   40.03 ? 336 VAL   B O   1 
ATOM   5659 C  CB  . VAL   B 1 351 ? 6.424   1.127   -9.264  1   39.63 ? 336 VAL   B CB  1 
ATOM   5660 C  CG1 . VAL   B 1 351 ? 6.233   1.305   -10.765 1   40.32 ? 336 VAL   B CG1 1 
ATOM   5661 C  CG2 . VAL   B 1 351 ? 6.465   -0.353  -8.886  1   39.13 ? 336 VAL   B CG2 1 
ATOM   5662 N  N   . LYS   B 1 352 ? 7.075   4.192   -8.569  1   40.11 ? 337 LYS   B N   1 
ATOM   5663 C  CA  . LYS   B 1 352 ? 7.103   5.622   -8.892  1   40.76 ? 337 LYS   B CA  1 
ATOM   5664 C  C   . LYS   B 1 352 ? 8.512   6.208   -8.819  1   40.18 ? 337 LYS   B C   1 
ATOM   5665 O  O   . LYS   B 1 352 ? 8.895   6.965   -9.707  1   39.85 ? 337 LYS   B O   1 
ATOM   5666 C  CB  . LYS   B 1 352 ? 6.164   6.408   -7.975  1   43.54 ? 337 LYS   B CB  1 
ATOM   5667 C  CG  . LYS   B 1 352 ? 4.881   6.791   -8.682  1   49.51 ? 337 LYS   B CG  1 
ATOM   5668 C  CD  . LYS   B 1 352 ? 4.059   7.714   -7.835  1   55.58 ? 337 LYS   B CD  1 
ATOM   5669 C  CE  . LYS   B 1 352 ? 3.431   7.046   -6.632  1   59.91 ? 337 LYS   B CE  1 
ATOM   5670 N  NZ  . LYS   B 1 352 ? 2.186   6.329   -7.013  1   63.1  ? 337 LYS   B NZ  1 
ATOM   5671 N  N   . ALA   B 1 353 ? 9.285   5.827   -7.784  1   39.98 ? 338 ALA   B N   1 
ATOM   5672 C  CA  . ALA   B 1 353 ? 10.67   6.252   -7.627  1   39.85 ? 338 ALA   B CA  1 
ATOM   5673 C  C   . ALA   B 1 353 ? 11.549  5.771   -8.815  1   40.09 ? 338 ALA   B C   1 
ATOM   5674 O  O   . ALA   B 1 353 ? 12.435  6.504   -9.249  1   40.27 ? 338 ALA   B O   1 
ATOM   5675 C  CB  . ALA   B 1 353 ? 11.238  5.745   -6.319  1   39.43 ? 338 ALA   B CB  1 
ATOM   5676 N  N   . LEU   B 1 354 ? 11.289  4.563   -9.34   1   39.29 ? 339 LEU   B N   1 
ATOM   5677 C  CA  . LEU   B 1 354 ? 12.028  4.019   -10.481 1   39.4  ? 339 LEU   B CA  1 
ATOM   5678 C  C   . LEU   B 1 354 ? 11.613  4.761   -11.752 1   39.18 ? 339 LEU   B C   1 
ATOM   5679 O  O   . LEU   B 1 354 ? 12.462  5.043   -12.601 1   38.78 ? 339 LEU   B O   1 
ATOM   5680 C  CB  . LEU   B 1 354 ? 11.716  2.513   -10.608 1   39.29 ? 339 LEU   B CB  1 
ATOM   5681 C  CG  . LEU   B 1 354 ? 12.753  1.561   -11.143 1   40.95 ? 339 LEU   B CG  1 
ATOM   5682 C  CD1 . LEU   B 1 354 ? 14.186  1.847   -10.608 1   41.07 ? 339 LEU   B CD1 1 
ATOM   5683 C  CD2 . LEU   B 1 354 ? 12.365  0.133   -10.794 1   41.51 ? 339 LEU   B CD2 1 
ATOM   5684 N  N   . VAL   B 1 355 ? 10.308  5.079   -11.892 1   38.46 ? 340 VAL   B N   1 
ATOM   5685 C  CA  . VAL   B 1 355 ? 9.815   5.855   -13.023 1   38.9  ? 340 VAL   B CA  1 
ATOM   5686 C  C   . VAL   B 1 355 ? 10.467  7.241   -13.01  1   39.2  ? 340 VAL   B C   1 
ATOM   5687 O  O   . VAL   B 1 355 ? 10.9    7.709   -14.055 1   39.37 ? 340 VAL   B O   1 
ATOM   5688 C  CB  . VAL   B 1 355 ? 8.266   5.962   -13.06  1   39.63 ? 340 VAL   B CB  1 
ATOM   5689 C  CG1 . VAL   B 1 355 ? 7.803   6.968   -14.113 1   39.94 ? 340 VAL   B CG1 1 
ATOM   5690 C  CG2 . VAL   B 1 355 ? 7.617   4.596   -13.293 1   39.85 ? 340 VAL   B CG2 1 
ATOM   5691 N  N   . SER   B 1 356 ? 10.576  7.867   -11.841 1   39.78 ? 341 SER   B N   1 
ATOM   5692 C  CA  . SER   B 1 356 ? 11.187  9.19    -11.732 1   40.88 ? 341 SER   B CA  1 
ATOM   5693 C  C   . SER   B 1 356 ? 12.667  9.167   -12.122 1   39.89 ? 341 SER   B C   1 
ATOM   5694 O  O   . SER   B 1 356 ? 13.109  10.075  -12.824 1   40.01 ? 341 SER   B O   1 
ATOM   5695 C  CB  . SER   B 1 356 ? 10.996  9.774   -10.34  1   43.84 ? 341 SER   B CB  1 
ATOM   5696 O  OG  . SER   B 1 356 ? 9.598   9.879   -10.12  1   48.97 ? 341 SER   B OG  1 
ATOM   5697 N  N   . LEU   B 1 357 ? 13.417  8.116   -11.721 1   38.51 ? 342 LEU   B N   1 
ATOM   5698 C  CA  . LEU   B 1 357 ? 14.824  7.967   -12.117 1   38.24 ? 342 LEU   B CA  1 
ATOM   5699 C  C   . LEU   B 1 357 ? 14.932  7.883   -13.638 1   37.57 ? 342 LEU   B C   1 
ATOM   5700 O  O   . LEU   B 1 357 ? 15.728  8.61    -14.257 1   38.59 ? 342 LEU   B O   1 
ATOM   5701 C  CB  . LEU   B 1 357 ? 15.439  6.709   -11.49  1   39.01 ? 342 LEU   B CB  1 
ATOM   5702 C  CG  . LEU   B 1 357 ? 15.982  6.873   -10.09  1   42.25 ? 342 LEU   B CG  1 
ATOM   5703 C  CD1 . LEU   B 1 357 ? 16.022  5.542   -9.369  1   43.11 ? 342 LEU   B CD1 1 
ATOM   5704 C  CD2 . LEU   B 1 357 ? 17.374  7.448   -10.139 1   43.87 ? 342 LEU   B CD2 1 
ATOM   5705 N  N   . ARG   B 1 358 ? 14.111  7.03    -14.249 1   35.28 ? 343 ARG   B N   1 
ATOM   5706 C  CA  . ARG   B 1 358 ? 14.17   6.814   -15.68  1   34.93 ? 343 ARG   B CA  1 
ATOM   5707 C  C   . ARG   B 1 358 ? 13.709  8.028   -16.487 1   36.29 ? 343 ARG   B C   1 
ATOM   5708 O  O   . ARG   B 1 358 ? 14.258  8.283   -17.567 1   35.96 ? 343 ARG   B O   1 
ATOM   5709 C  CB  . ARG   B 1 358 ? 13.421  5.529   -16.057 1   34.23 ? 343 ARG   B CB  1 
ATOM   5710 C  CG  . ARG   B 1 358 ? 14.132  4.31    -15.447 1   33.17 ? 343 ARG   B CG  1 
ATOM   5711 C  CD  . ARG   B 1 358 ? 13.521  2.984   -15.84  1   32.93 ? 343 ARG   B CD  1 
ATOM   5712 N  NE  . ARG   B 1 358 ? 14.535  1.953   -15.675 1   34.32 ? 343 ARG   B NE  1 
ATOM   5713 C  CZ  . ARG   B 1 358 ? 14.351  0.789   -15.064 1   34.87 ? 343 ARG   B CZ  1 
ATOM   5714 N  NH1 . ARG   B 1 358 ? 13.161  0.477   -14.563 1   33.15 ? 343 ARG   B NH1 1 
ATOM   5715 N  NH2 . ARG   B 1 358 ? 15.357  -0.081  -14.957 1   32.39 ? 343 ARG   B NH2 1 
ATOM   5716 N  N   . SER   B 1 359 ? 12.74   8.794   -15.963 1   36.96 ? 344 SER   B N   1 
ATOM   5717 C  CA  . SER   B 1 359 ? 12.25   9.996   -16.648 1   38.04 ? 344 SER   B CA  1 
ATOM   5718 C  C   . SER   B 1 359 ? 13.337  11.08   -16.639 1   38.23 ? 344 SER   B C   1 
ATOM   5719 O  O   . SER   B 1 359 ? 13.56   11.739  -17.655 1   38.44 ? 344 SER   B O   1 
ATOM   5720 C  CB  . SER   B 1 359 ? 10.98   10.521  -15.971 1   39.8  ? 344 SER   B CB  1 
ATOM   5721 O  OG  . SER   B 1 359 ? 9.922   9.596   -16.163 1   42.61 ? 344 SER   B OG  1 
ATOM   5722 N  N   . TYR   B 1 360 ? 14.031  11.236  -15.512 1   37.39 ? 345 TYR   B N   1 
ATOM   5723 C  CA  . TYR   B 1 360 ? 15.091  12.21   -15.401 1   38    ? 345 TYR   B CA  1 
ATOM   5724 C  C   . TYR   B 1 360 ? 16.269  11.857  -16.342 1   38.03 ? 345 TYR   B C   1 
ATOM   5725 O  O   . TYR   B 1 360 ? 16.826  12.73   -17.025 1   38.74 ? 345 TYR   B O   1 
ATOM   5726 C  CB  . TYR   B 1 360 ? 15.55   12.28   -13.947 1   38.93 ? 345 TYR   B CB  1 
ATOM   5727 C  CG  . TYR   B 1 360 ? 16.538  13.395  -13.736 1   42.01 ? 345 TYR   B CG  1 
ATOM   5728 C  CD1 . TYR   B 1 360 ? 16.117  14.715  -13.653 1   43.51 ? 345 TYR   B CD1 1 
ATOM   5729 C  CD2 . TYR   B 1 360 ? 17.902  13.141  -13.694 1   43.84 ? 345 TYR   B CD2 1 
ATOM   5730 C  CE1 . TYR   B 1 360 ? 17.029  15.752  -13.496 1   45.03 ? 345 TYR   B CE1 1 
ATOM   5731 C  CE2 . TYR   B 1 360 ? 18.819  14.166  -13.514 1   45.13 ? 345 TYR   B CE2 1 
ATOM   5732 C  CZ  . TYR   B 1 360 ? 18.381  15.475  -13.438 1   46.16 ? 345 TYR   B CZ  1 
ATOM   5733 O  OH  . TYR   B 1 360 ? 19.289  16.497  -13.296 1   48.63 ? 345 TYR   B OH  1 
ATOM   5734 N  N   . HIS   B 1 361 ? 16.602  10.561  -16.409 1   36.21 ? 346 HIS   B N   1 
ATOM   5735 C  CA  . HIS   B 1 361 ? 17.652  10.019  -17.241 1   34.64 ? 346 HIS   B CA  1 
ATOM   5736 C  C   . HIS   B 1 361 ? 17.307  10.247  -18.722 1   35.03 ? 346 HIS   B C   1 
ATOM   5737 O  O   . HIS   B 1 361 ? 18.209  10.56   -19.503 1   34.78 ? 346 HIS   B O   1 
ATOM   5738 C  CB  . HIS   B 1 361 ? 17.843  8.522   -16.881 1   33.37 ? 346 HIS   B CB  1 
ATOM   5739 C  CG  . HIS   B 1 361 ? 18.848  7.783   -17.699 1   32.6  ? 346 HIS   B CG  1 
ATOM   5740 N  ND1 . HIS   B 1 361 ? 18.471  7.049   -18.797 1   34.99 ? 346 HIS   B ND1 1 
ATOM   5741 C  CD2 . HIS   B 1 361 ? 20.179  7.657   -17.522 1   32.6  ? 346 HIS   B CD2 1 
ATOM   5742 C  CE1 . HIS   B 1 361 ? 19.575  6.506   -19.261 1   35.64 ? 346 HIS   B CE1 1 
ATOM   5743 N  NE2 . HIS   B 1 361 ? 20.629  6.851   -18.524 1   34.98 ? 346 HIS   B NE2 1 
ATOM   5744 N  N   . LEU   B 1 362 ? 16.025  10.147  -19.112 1   34.7  ? 347 LEU   B N   1 
ATOM   5745 C  CA  . LEU   B 1 362 ? 15.62   10.428  -20.499 1   36.26 ? 347 LEU   B CA  1 
ATOM   5746 C  C   . LEU   B 1 362 ? 15.915  11.905  -20.866 1   37.51 ? 347 LEU   B C   1 
ATOM   5747 O  O   . LEU   B 1 362 ? 16.335  12.187  -21.992 1   37.74 ? 347 LEU   B O   1 
ATOM   5748 C  CB  . LEU   B 1 362 ? 14.132  10.152  -20.707 1   36.05 ? 347 LEU   B CB  1 
ATOM   5749 C  CG  . LEU   B 1 362 ? 13.829  8.758   -21.157 1   37.85 ? 347 LEU   B CG  1 
ATOM   5750 C  CD1 . LEU   B 1 362 ? 12.371  8.418   -20.936 1   38.35 ? 347 LEU   B CD1 1 
ATOM   5751 C  CD2 . LEU   B 1 362 ? 14.266  8.567   -22.592 1   38.18 ? 347 LEU   B CD2 1 
ATOM   5752 N  N   . GLN   B 1 363 ? 15.696  12.826  -19.919 1   37.78 ? 348 GLN   B N   1 
ATOM   5753 C  CA  . GLN   B 1 363 ? 15.973  14.241  -20.148 1   39.26 ? 348 GLN   B CA  1 
ATOM   5754 C  C   . GLN   B 1 363 ? 17.476  14.462  -20.312 1   39.97 ? 348 GLN   B C   1 
ATOM   5755 O  O   . GLN   B 1 363 ? 17.877  15.28   -21.129 1   40.71 ? 348 GLN   B O   1 
ATOM   5756 C  CB  . GLN   B 1 363 ? 15.395  15.085  -19.003 1   41.09 ? 348 GLN   B CB  1 
ATOM   5757 C  CG  . GLN   B 1 363 ? 13.889  14.956  -18.947 1   45.63 ? 348 GLN   B CG  1 
ATOM   5758 C  CD  . GLN   B 1 363 ? 13.272  15.721  -17.794 1   50.99 ? 348 GLN   B CD  1 
ATOM   5759 O  OE1 . GLN   B 1 363 ? 13.473  16.921  -17.635 1   53.6  ? 348 GLN   B OE1 1 
ATOM   5760 N  NE2 . GLN   B 1 363 ? 12.473  15.043  -16.997 1   51.26 ? 348 GLN   B NE2 1 
ATOM   5761 N  N   . ILE   B 1 364 ? 18.304  13.692  -19.576 1   39.39 ? 349 ILE   B N   1 
ATOM   5762 C  CA  . ILE   B 1 364 ? 19.759  13.73   -19.671 1   39.67 ? 349 ILE   B CA  1 
ATOM   5763 C  C   . ILE   B 1 364 ? 20.198  13.247  -21.042 1   39.07 ? 349 ILE   B C   1 
ATOM   5764 O  O   . ILE   B 1 364 ? 21.052  13.876  -21.662 1   38.96 ? 349 ILE   B O   1 
ATOM   5765 C  CB  . ILE   B 1 364 ? 20.355  12.882  -18.534 1   40.9  ? 349 ILE   B CB  1 
ATOM   5766 C  CG1 . ILE   B 1 364 ? 20.245  13.675  -17.218 1   42.54 ? 349 ILE   B CG1 1 
ATOM   5767 C  CG2 . ILE   B 1 364 ? 21.803  12.389  -18.833 1   41.5  ? 349 ILE   B CG2 1 
ATOM   5768 C  CD1 . ILE   B 1 364 ? 20.56   12.907  -16.084 1   44.85 ? 349 ILE   B CD1 1 
ATOM   5769 N  N   . VAL   B 1 365 ? 19.616  12.155  -21.526 1   38.09 ? 350 VAL   B N   1 
ATOM   5770 C  CA  . VAL   B 1 365 ? 19.982  11.625  -22.833 1   38.21 ? 350 VAL   B CA  1 
ATOM   5771 C  C   . VAL   B 1 365 ? 19.598  12.625  -23.948 1   37.95 ? 350 VAL   B C   1 
ATOM   5772 O  O   . VAL   B 1 365 ? 20.338  12.759  -24.914 1   37.78 ? 350 VAL   B O   1 
ATOM   5773 C  CB  . VAL   B 1 365 ? 19.455  10.188  -23.051 1   38.66 ? 350 VAL   B CB  1 
ATOM   5774 C  CG1 . VAL   B 1 365 ? 19.841  9.658   -24.421 1   38.96 ? 350 VAL   B CG1 1 
ATOM   5775 C  CG2 . VAL   B 1 365 ? 19.981  9.259   -21.972 1   39.07 ? 350 VAL   B CG2 1 
ATOM   5776 N  N   . THR   B 1 366 ? 18.501  13.386  -23.779 1   37.72 ? 351 THR   B N   1 
ATOM   5777 C  CA  . THR   B 1 366 ? 18.112  14.401  -24.772 1   37.98 ? 351 THR   B CA  1 
ATOM   5778 C  C   . THR   B 1 366 ? 19.214  15.49   -24.83  1   37.96 ? 351 THR   B C   1 
ATOM   5779 O  O   . THR   B 1 366 ? 19.669  15.859  -25.915 1   38.04 ? 351 THR   B O   1 
ATOM   5780 C  CB  . THR   B 1 366 ? 16.753  15.024  -24.386 1   39.54 ? 351 THR   B CB  1 
ATOM   5781 O  OG1 . THR   B 1 366 ? 15.742  14.022  -24.456 1   40.53 ? 351 THR   B OG1 1 
ATOM   5782 C  CG2 . THR   B 1 366 ? 16.352  16.181  -25.307 1   39.69 ? 351 THR   B CG2 1 
ATOM   5783 N  N   . LYS   B 1 367 ? 19.672  15.94   -23.662 1   37.74 ? 352 LYS   B N   1 
ATOM   5784 C  CA  . LYS   B 1 367 ? 20.739  16.931  -23.556 1   38.64 ? 352 LYS   B CA  1 
ATOM   5785 C  C   . LYS   B 1 367 ? 22.111  16.438  -24.069 1   39.34 ? 352 LYS   B C   1 
ATOM   5786 O  O   . LYS   B 1 367 ? 22.804  17.184  -24.751 1   40.05 ? 352 LYS   B O   1 
ATOM   5787 C  CB  . LYS   B 1 367 ? 20.867  17.399  -22.089 1   39.68 ? 352 LYS   B CB  1 
ATOM   5788 C  CG  . LYS   B 1 367 ? 22.06   18.316  -21.813 1   42.36 ? 352 LYS   B CG  1 
ATOM   5789 C  CD  . LYS   B 1 367 ? 22.063  18.848  -20.376 1   46.13 ? 352 LYS   B CD  1 
ATOM   5790 C  CE  . LYS   B 1 367 ? 23.381  19.516  -20.067 1   49.08 ? 352 LYS   B CE  1 
ATOM   5791 N  NZ  . LYS   B 1 367 ? 23.425  20.059  -18.686 1   49.2  ? 352 LYS   B NZ  1 
ATOM   5792 N  N   . TYR   B 1 368 ? 22.521  15.21   -23.724 1   38.69 ? 353 TYR   B N   1 
ATOM   5793 C  CA  . TYR   B 1 368 ? 23.863  14.728  -24.038 1   38.28 ? 353 TYR   B CA  1 
ATOM   5794 C  C   . TYR   B 1 368 ? 24.016  13.964  -25.34  1   38.09 ? 353 TYR   B C   1 
ATOM   5795 O  O   . TYR   B 1 368 ? 25.141  13.834  -25.816 1   38.28 ? 353 TYR   B O   1 
ATOM   5796 C  CB  . TYR   B 1 368 ? 24.388  13.887  -22.88  1   38.23 ? 353 TYR   B CB  1 
ATOM   5797 C  CG  . TYR   B 1 368 ? 24.774  14.737  -21.696 1   39.15 ? 353 TYR   B CG  1 
ATOM   5798 C  CD1 . TYR   B 1 368 ? 23.846  15.07   -20.722 1   40.03 ? 353 TYR   B CD1 1 
ATOM   5799 C  CD2 . TYR   B 1 368 ? 26.062  15.238  -21.566 1   40.3  ? 353 TYR   B CD2 1 
ATOM   5800 C  CE1 . TYR   B 1 368 ? 24.185  15.884  -19.655 1   41.33 ? 353 TYR   B CE1 1 
ATOM   5801 C  CE2 . TYR   B 1 368 ? 26.413  16.056  -20.505 1   41.08 ? 353 TYR   B CE2 1 
ATOM   5802 C  CZ  . TYR   B 1 368 ? 25.469  16.384  -19.553 1   42.69 ? 353 TYR   B CZ  1 
ATOM   5803 O  OH  . TYR   B 1 368 ? 25.829  17.183  -18.488 1   45.21 ? 353 TYR   B OH  1 
ATOM   5804 N  N   . ILE   B 1 369 ? 22.926  13.419  -25.894 1   37.9  ? 354 ILE   B N   1 
ATOM   5805 C  CA  . ILE   B 1 369 ? 23.01   12.657  -27.135 1   38.43 ? 354 ILE   B CA  1 
ATOM   5806 C  C   . ILE   B 1 369 ? 22.143  13.259  -28.244 1   39.53 ? 354 ILE   B C   1 
ATOM   5807 O  O   . ILE   B 1 369 ? 22.663  13.542  -29.325 1   40.02 ? 354 ILE   B O   1 
ATOM   5808 C  CB  . ILE   B 1 369 ? 22.738  11.13   -26.935 1   38.53 ? 354 ILE   B CB  1 
ATOM   5809 C  CG1 . ILE   B 1 369 ? 23.941  10.45   -26.225 1   39.04 ? 354 ILE   B CG1 1 
ATOM   5810 C  CG2 . ILE   B 1 369 ? 22.474  10.427  -28.289 1   38.59 ? 354 ILE   B CG2 1 
ATOM   5811 C  CD1 . ILE   B 1 369 ? 23.755  9.008   -25.934 1   40.8  ? 354 ILE   B CD1 1 
ATOM   5812 N  N   . LEU   B 1 370 ? 20.841  13.419  -28     1   39.11 ? 355 LEU   B N   1 
ATOM   5813 C  CA  . LEU   B 1 370 ? 19.914  13.879  -29.031 1   40.5  ? 355 LEU   B CA  1 
ATOM   5814 C  C   . LEU   B 1 370 ? 20.253  15.257  -29.628 1   40.88 ? 355 LEU   B C   1 
ATOM   5815 O  O   . LEU   B 1 370 ? 20.422  15.394  -30.849 1   40.9  ? 355 LEU   B O   1 
ATOM   5816 C  CB  . LEU   B 1 370 ? 18.469  13.853  -28.48  1   41.07 ? 355 LEU   B CB  1 
ATOM   5817 C  CG  . LEU   B 1 370 ? 17.382  13.422  -29.435 1   44.2  ? 355 LEU   B CG  1 
ATOM   5818 C  CD1 . LEU   B 1 370 ? 17.486  11.91   -29.775 1   44.94 ? 355 LEU   B CD1 1 
ATOM   5819 C  CD2 . LEU   B 1 370 ? 16.004  13.76   -28.853 1   45.24 ? 355 LEU   B CD2 1 
ATOM   5820 N  N   . ILE   B 1 371 ? 20.358  16.266  -28.769 1   41.25 ? 356 ILE   B N   1 
ATOM   5821 C  CA  . ILE   B 1 371 ? 20.654  17.614  -29.209 1   42.44 ? 356 ILE   B CA  1 
ATOM   5822 C  C   . ILE   B 1 371 ? 22.058  17.692  -29.844 1   44.26 ? 356 ILE   B C   1 
ATOM   5823 O  O   . ILE   B 1 371 ? 22.115  18.077  -31.012 1   44.59 ? 356 ILE   B O   1 
ATOM   5824 C  CB  . ILE   B 1 371 ? 20.393  18.613  -28.069 1   42.48 ? 356 ILE   B CB  1 
ATOM   5825 C  CG1 . ILE   B 1 371 ? 18.87   18.656  -27.8   1   42.48 ? 356 ILE   B CG1 1 
ATOM   5826 C  CG2 . ILE   B 1 371 ? 20.982  19.99   -28.423 1   42.97 ? 356 ILE   B CG2 1 
ATOM   5827 C  CD1 . ILE   B 1 371 ? 18.435  19.475  -26.648 1   43.27 ? 356 ILE   B CD1 1 
ATOM   5828 N  N   . PRO   B 1 372 ? 23.16   17.187  -29.218 1   44.81 ? 357 PRO   B N   1 
ATOM   5829 C  CA  . PRO   B 1 372 ? 24.466  17.211  -29.911 1   45.12 ? 357 PRO   B CA  1 
ATOM   5830 C  C   . PRO   B 1 372 ? 24.494  16.473  -31.247 1   45.47 ? 357 PRO   B C   1 
ATOM   5831 O  O   . PRO   B 1 372 ? 25.156  16.952  -32.17  1   45.5  ? 357 PRO   B O   1 
ATOM   5832 C  CB  . PRO   B 1 372 ? 25.424  16.568  -28.899 1   45.64 ? 357 PRO   B CB  1 
ATOM   5833 C  CG  . PRO   B 1 372 ? 24.806  16.843  -27.583 1   45.91 ? 357 PRO   B CG  1 
ATOM   5834 C  CD  . PRO   B 1 372 ? 23.316  16.677  -27.842 1   44.7  ? 357 PRO   B CD  1 
ATOM   5835 N  N   . ALA   B 1 373 ? 23.751  15.354  -31.383 1   45.32 ? 358 ALA   B N   1 
ATOM   5836 C  CA  . ALA   B 1 373 ? 23.698  14.632  -32.66  1   45.97 ? 358 ALA   B CA  1 
ATOM   5837 C  C   . ALA   B 1 373 ? 23.117  15.496  -33.79  1   46.63 ? 358 ALA   B C   1 
ATOM   5838 O  O   . ALA   B 1 373 ? 23.5    15.335  -34.951 1   46.97 ? 358 ALA   B O   1 
ATOM   5839 C  CB  . ALA   B 1 373 ? 22.89   13.349  -32.517 1   45.86 ? 358 ALA   B CB  1 
ATOM   5840 N  N   . SER   B 1 374 ? 22.199  16.405  -33.443 1   46.85 ? 359 SER   B N   1 
ATOM   5841 C  CA  . SER   B 1 374 ? 21.552  17.31   -34.387 1   47.9  ? 359 SER   B CA  1 
ATOM   5842 C  C   . SER   B 1 374 ? 22.45   18.506  -34.788 1   50.24 ? 359 SER   B C   1 
ATOM   5843 O  O   . SER   B 1 374 ? 22.122  19.192  -35.751 1   50.96 ? 359 SER   B O   1 
ATOM   5844 C  CB  . SER   B 1 374 ? 20.235  17.819  -33.8   1   47.08 ? 359 SER   B CB  1 
ATOM   5845 O  OG  . SER   B 1 374 ? 20.441  18.805  -32.799 1   46.32 ? 359 SER   B OG  1 
ATOM   5846 N  N   . GLN   B 1 375 ? 23.55   18.77   -34.05  1   51.21 ? 360 GLN   B N   1 
ATOM   5847 C  CA  . GLN   B 1 375 ? 24.462  19.898  -34.298 1   52.81 ? 360 GLN   B CA  1 
ATOM   5848 C  C   . GLN   B 1 375 ? 25.86   19.501  -34.829 1   53.61 ? 360 GLN   B C   1 
ATOM   5849 O  O   . GLN   B 1 375 ? 26.062  18.424  -35.398 1   54.14 ? 360 GLN   B O   1 
ATOM   5850 C  CB  . GLN   B 1 375 ? 24.626  20.736  -33.011 1   55.41 ? 360 GLN   B CB  1 
ATOM   5851 C  CG  . GLN   B 1 375 ? 23.305  21.148  -32.366 1   60.26 ? 360 GLN   B CG  1 
ATOM   5852 C  CD  . GLN   B 1 375 ? 23.497  21.73   -30.977 1   66.22 ? 360 GLN   B CD  1 
ATOM   5853 O  OE1 . GLN   B 1 375 ? 24.422  21.362  -30.232 1   67.57 ? 360 GLN   B OE1 1 
ATOM   5854 N  NE2 . GLN   B 1 375 ? 22.61   22.642  -30.592 1   66.6  ? 360 GLN   B NE2 1 
ATOM   5855 N  N   . GLY   B 1 395 ? 19.573  9.573   -35.167 1   55.86 ? 380 GLY   B N   1 
ATOM   5856 C  CA  . GLY   B 1 395 ? 20.642  10.175  -34.378 1   56.07 ? 380 GLY   B CA  1 
ATOM   5857 C  C   . GLY   B 1 395 ? 20.359  10.057  -32.892 1   55.92 ? 380 GLY   B C   1 
ATOM   5858 O  O   . GLY   B 1 395 ? 20.002  11.048  -32.235 1   56.42 ? 380 GLY   B O   1 
ATOM   5859 N  N   . GLY   B 1 396 ? 20.509  8.834   -32.363 1   54.49 ? 381 GLY   B N   1 
ATOM   5860 C  CA  . GLY   B 1 396 ? 20.214  8.553   -30.963 1   53.16 ? 381 GLY   B CA  1 
ATOM   5861 C  C   . GLY   B 1 396 ? 18.732  8.316   -30.682 1   51.5  ? 381 GLY   B C   1 
ATOM   5862 O  O   . GLY   B 1 396 ? 18.341  8.127   -29.53  1   50.63 ? 381 GLY   B O   1 
ATOM   5863 N  N   . THR   B 1 397 ? 17.889  8.319   -31.729 1   50.16 ? 382 THR   B N   1 
ATOM   5864 C  CA  . THR   B 1 397 ? 16.461  8.071   -31.629 1   49.31 ? 382 THR   B CA  1 
ATOM   5865 C  C   . THR   B 1 397 ? 16.215  6.613   -31.209 1   48.55 ? 382 THR   B C   1 
ATOM   5866 O  O   . THR   B 1 397 ? 15.3    6.353   -30.426 1   48.21 ? 382 THR   B O   1 
ATOM   5867 C  CB  . THR   B 1 397 ? 15.805  8.402   -32.98  1   50.39 ? 382 THR   B CB  1 
ATOM   5868 O  OG1 . THR   B 1 397 ? 15.939  9.806   -33.245 1   50.92 ? 382 THR   B OG1 1 
ATOM   5869 C  CG2 . THR   B 1 397 ? 14.331  7.978   -33.057 1   51.03 ? 382 THR   B CG2 1 
ATOM   5870 N  N   . ASP   B 1 398 ? 17.028  5.666   -31.717 1   47.81 ? 383 ASP   B N   1 
ATOM   5871 C  CA  . ASP   B 1 398 ? 16.9    4.252   -31.357 1   47.59 ? 383 ASP   B CA  1 
ATOM   5872 C  C   . ASP   B 1 398 ? 17.184  4.062   -29.861 1   46.03 ? 383 ASP   B C   1 
ATOM   5873 O  O   . ASP   B 1 398 ? 16.514  3.248   -29.212 1   45.89 ? 383 ASP   B O   1 
ATOM   5874 C  CB  . ASP   B 1 398 ? 17.857  3.384   -32.184 1   50.73 ? 383 ASP   B CB  1 
ATOM   5875 C  CG  . ASP   B 1 398 ? 17.408  3.172   -33.612 1   60.63 ? 383 ASP   B CG  1 
ATOM   5876 O  OD1 . ASP   B 1 398 ? 16.622  4.013   -34.121 1   62.34 ? 383 ASP   B OD1 1 
ATOM   5877 O  OD2 . ASP   B 1 398 ? 17.84   2.157   -34.232 1   64.24 ? 383 ASP   B OD2 1 
ATOM   5878 N  N   . LEU   B 1 399 ? 18.177  4.821   -29.323 1   44.47 ? 384 LEU   B N   1 
ATOM   5879 C  CA  . LEU   B 1 399 ? 18.572  4.802   -27.918 1   43.61 ? 384 LEU   B CA  1 
ATOM   5880 C  C   . LEU   B 1 399 ? 17.422  5.337   -27.064 1   42.53 ? 384 LEU   B C   1 
ATOM   5881 O  O   . LEU   B 1 399 ? 17.113  4.763   -26.022 1   42.06 ? 384 LEU   B O   1 
ATOM   5882 C  CB  . LEU   B 1 399 ? 19.822  5.666   -27.677 1   43.48 ? 384 LEU   B CB  1 
ATOM   5883 C  CG  . LEU   B 1 399 ? 21.119  5.231   -28.357 1   45.27 ? 384 LEU   B CG  1 
ATOM   5884 C  CD1 . LEU   B 1 399 ? 22.24   6.229   -28.073 1   45.48 ? 384 LEU   B CD1 1 
ATOM   5885 C  CD2 . LEU   B 1 399 ? 21.524  3.831   -27.925 1   45.68 ? 384 LEU   B CD2 1 
ATOM   5886 N  N   . MET   B 1 400 ? 16.778  6.426   -27.512 1   41.55 ? 385 MET   B N   1 
ATOM   5887 C  CA  . MET   B 1 400 ? 15.652  7.021   -26.789 1   40.82 ? 385 MET   B CA  1 
ATOM   5888 C  C   . MET   B 1 400 ? 14.473  6.074   -26.762 1   39.62 ? 385 MET   B C   1 
ATOM   5889 O  O   . MET   B 1 400 ? 13.825  5.958   -25.74  1   38.87 ? 385 MET   B O   1 
ATOM   5890 C  CB  . MET   B 1 400 ? 15.221  8.361   -27.415 1   41.14 ? 385 MET   B CB  1 
ATOM   5891 C  CG  . MET   B 1 400 ? 16.275  9.406   -27.384 1   42.51 ? 385 MET   B CG  1 
ATOM   5892 S  SD  . MET   B 1 400 ? 16.634  10.064  -25.767 1   47.54 ? 385 MET   B SD  1 
ATOM   5893 C  CE  . MET   B 1 400 ? 15.082  10.815  -25.358 1   46.57 ? 385 MET   B CE  1 
ATOM   5894 N  N   . ASN   B 1 401 ? 14.197  5.396   -27.873 1   39.7  ? 386 ASN   B N   1 
ATOM   5895 C  CA  . ASN   B 1 401 ? 13.09   4.452   -27.965 1   39.82 ? 386 ASN   B CA  1 
ATOM   5896 C  C   . ASN   B 1 401 ? 13.291  3.269   -27.015 1   39.23 ? 386 ASN   B C   1 
ATOM   5897 O  O   . ASN   B 1 401 ? 12.321  2.79    -26.409 1   39.71 ? 386 ASN   B O   1 
ATOM   5898 C  CB  . ASN   B 1 401 ? 12.898  3.992   -29.409 1   41.41 ? 386 ASN   B CB  1 
ATOM   5899 C  CG  . ASN   B 1 401 ? 12.268  5.071   -30.289 1   46.22 ? 386 ASN   B CG  1 
ATOM   5900 O  OD1 . ASN   B 1 401 ? 11.714  6.085   -29.801 1   46.82 ? 386 ASN   B OD1 1 
ATOM   5901 N  ND2 . ASN   B 1 401 ? 12.355  4.887   -31.609 1   46.81 ? 386 ASN   B ND2 1 
ATOM   5902 N  N   . PHE   B 1 402 ? 14.548  2.821   -26.854 1   37.96 ? 387 PHE   B N   1 
ATOM   5903 C  CA  . PHE   B 1 402 ? 14.86   1.75    -25.921 1   37.08 ? 387 PHE   B CA  1 
ATOM   5904 C  C   . PHE   B 1 402 ? 14.575  2.25    -24.484 1   36.56 ? 387 PHE   B C   1 
ATOM   5905 O  O   . PHE   B 1 402 ? 13.894  1.568   -23.714 1   36.76 ? 387 PHE   B O   1 
ATOM   5906 C  CB  . PHE   B 1 402 ? 16.332  1.292   -26.062 1   36.11 ? 387 PHE   B CB  1 
ATOM   5907 C  CG  . PHE   B 1 402 ? 16.874  0.54    -24.856 1   36.05 ? 387 PHE   B CG  1 
ATOM   5908 C  CD1 . PHE   B 1 402 ? 16.495  -0.768  -24.605 1   36.44 ? 387 PHE   B CD1 1 
ATOM   5909 C  CD2 . PHE   B 1 402 ? 17.723  1.159   -23.953 1   36.05 ? 387 PHE   B CD2 1 
ATOM   5910 C  CE1 . PHE   B 1 402 ? 16.97   -1.443  -23.473 1   36.63 ? 387 PHE   B CE1 1 
ATOM   5911 C  CE2 . PHE   B 1 402 ? 18.201  0.475   -22.831 1   36.36 ? 387 PHE   B CE2 1 
ATOM   5912 C  CZ  . PHE   B 1 402 ? 17.811  -0.81   -22.596 1   35.84 ? 387 PHE   B CZ  1 
ATOM   5913 N  N   . LEU   B 1 403 ? 15.072  3.438   -24.141 1   35.45 ? 388 LEU   B N   1 
ATOM   5914 C  CA  . LEU   B 1 403 ? 14.893  3.982   -22.807 1   35.28 ? 388 LEU   B CA  1 
ATOM   5915 C  C   . LEU   B 1 403 ? 13.414  4.259   -22.471 1   35.88 ? 388 LEU   B C   1 
ATOM   5916 O  O   . LEU   B 1 403 ? 12.975  4.062   -21.336 1   35.45 ? 388 LEU   B O   1 
ATOM   5917 C  CB  . LEU   B 1 403 ? 15.739  5.245   -22.664 1   35.26 ? 388 LEU   B CB  1 
ATOM   5918 C  CG  . LEU   B 1 403 ? 17.254  5.041   -22.66  1   35.34 ? 388 LEU   B CG  1 
ATOM   5919 C  CD1 . LEU   B 1 403 ? 17.961  6.39    -22.575 1   35.03 ? 388 LEU   B CD1 1 
ATOM   5920 C  CD2 . LEU   B 1 403 ? 17.681  4.137   -21.475 1   34.87 ? 388 LEU   B CD2 1 
ATOM   5921 N  N   . LYS   B 1 404 ? 12.648  4.696   -23.469 1   36.43 ? 389 LYS   B N   1 
ATOM   5922 C  CA  . LYS   B 1 404 ? 11.226  4.965   -23.323 1   37.2  ? 389 LYS   B CA  1 
ATOM   5923 C  C   . LYS   B 1 404 ? 10.432  3.661   -23.166 1   37.96 ? 389 LYS   B C   1 
ATOM   5924 O  O   . LYS   B 1 404 ? 9.466   3.645   -22.427 1   38.78 ? 389 LYS   B O   1 
ATOM   5925 C  CB  . LYS   B 1 404 ? 10.715  5.849   -24.477 1   38.14 ? 389 LYS   B CB  1 
ATOM   5926 C  CG  . LYS   B 1 404 ? 11.239  7.269   -24.269 1   40.56 ? 389 LYS   B CG  1 
ATOM   5927 C  CD  . LYS   B 1 404 ? 10.603  8.317   -25.119 1   42.35 ? 389 LYS   B CD  1 
ATOM   5928 C  CE  . LYS   B 1 404 ? 11.227  8.411   -26.473 1   42.04 ? 389 LYS   B CE  1 
ATOM   5929 N  NZ  . LYS   B 1 404 ? 10.671  9.533   -27.259 1   40.33 ? 389 LYS   B NZ  1 
ATOM   5930 N  N   . THR   B 1 405 ? 10.876  2.564   -23.784 1   37.52 ? 390 THR   B N   1 
ATOM   5931 C  CA  . THR   B 1 405 ? 10.253  1.261   -23.621 1   37.86 ? 390 THR   B CA  1 
ATOM   5932 C  C   . THR   B 1 405 ? 10.452  0.756   -22.176 1   38.02 ? 390 THR   B C   1 
ATOM   5933 O  O   . THR   B 1 405 ? 9.488   0.338   -21.529 1   38.36 ? 390 THR   B O   1 
ATOM   5934 C  CB  . THR   B 1 405 ? 10.828  0.278   -24.637 1   39.13 ? 390 THR   B CB  1 
ATOM   5935 O  OG1 . THR   B 1 405 ? 10.412  0.672   -25.943 1   40.3  ? 390 THR   B OG1 1 
ATOM   5936 C  CG2 . THR   B 1 405 ? 10.388  -1.166  -24.362 1   39.71 ? 390 THR   B CG2 1 
ATOM   5937 N  N   . VAL   B 1 406 ? 11.684  0.861   -21.666 1   37.1  ? 391 VAL   B N   1 
ATOM   5938 C  CA  . VAL   B 1 406 ? 12.039  0.459   -20.306 1   37.2  ? 391 VAL   B CA  1 
ATOM   5939 C  C   . VAL   B 1 406 ? 11.234  1.288   -19.308 1   37.38 ? 391 VAL   B C   1 
ATOM   5940 O  O   . VAL   B 1 406 ? 10.647  0.743   -18.383 1   37.19 ? 391 VAL   B O   1 
ATOM   5941 C  CB  . VAL   B 1 406 ? 13.575  0.587   -20.072 1   36.7  ? 391 VAL   B CB  1 
ATOM   5942 C  CG1 . VAL   B 1 406 ? 13.941  0.308   -18.627 1   36.29 ? 391 VAL   B CG1 1 
ATOM   5943 C  CG2 . VAL   B 1 406 ? 14.34   -0.361  -21.005 1   37.01 ? 391 VAL   B CG2 1 
ATOM   5944 N  N   . ARG   B 1 407 ? 11.19   2.601   -19.52  1   37.38 ? 392 ARG   B N   1 
ATOM   5945 C  CA  . ARG   B 1 407 ? 10.435  3.485   -18.648 1   37.93 ? 392 ARG   B CA  1 
ATOM   5946 C  C   . ARG   B 1 407 ? 8.932   3.155   -18.666 1   38.41 ? 392 ARG   B C   1 
ATOM   5947 O  O   . ARG   B 1 407 ? 8.316   3.122   -17.602 1   38.78 ? 392 ARG   B O   1 
ATOM   5948 C  CB  . ARG   B 1 407 ? 10.672  4.97    -19     1   39.19 ? 392 ARG   B CB  1 
ATOM   5949 C  CG  . ARG   B 1 407 ? 9.841   5.858   -18.116 1   42.04 ? 392 ARG   B CG  1 
ATOM   5950 C  CD  . ARG   B 1 407 ? 9.845   7.286   -18.469 1   45.29 ? 392 ARG   B CD  1 
ATOM   5951 N  NE  . ARG   B 1 407 ? 9.294   7.65    -19.782 1   46.35 ? 392 ARG   B NE  1 
ATOM   5952 C  CZ  . ARG   B 1 407 ? 9.155   8.919   -20.174 1   47.52 ? 392 ARG   B CZ  1 
ATOM   5953 N  NH1 . ARG   B 1 407 ? 9.482   9.914   -19.357 1   46.5  ? 392 ARG   B NH1 1 
ATOM   5954 N  NH2 . ARG   B 1 407 ? 8.69    9.2     -21.385 1   46.96 ? 392 ARG   B NH2 1 
ATOM   5955 N  N   A SER   B 1 408 ? 8.348   2.929   -19.856 0.5 38.54 ? 393 SER   B N   1 
ATOM   5956 N  N   B SER   B 1 408 ? 8.356   2.928   -19.865 0.5 38.15 ? 393 SER   B N   1 
ATOM   5957 C  CA  A SER   B 1 408 ? 6.924   2.621   -19.968 0.5 39.13 ? 393 SER   B CA  1 
ATOM   5958 C  CA  B SER   B 1 408 ? 6.937   2.613   -20.046 0.5 38.36 ? 393 SER   B CA  1 
ATOM   5959 C  C   A SER   B 1 408 ? 6.568   1.302   -19.3   0.5 38.99 ? 393 SER   B C   1 
ATOM   5960 C  C   B SER   B 1 408 ? 6.565   1.308   -19.337 0.5 38.63 ? 393 SER   B C   1 
ATOM   5961 O  O   A SER   B 1 408 ? 5.537   1.232   -18.643 0.5 38.75 ? 393 SER   B O   1 
ATOM   5962 O  O   B SER   B 1 408 ? 5.527   1.258   -18.687 0.5 38.35 ? 393 SER   B O   1 
ATOM   5963 C  CB  A SER   B 1 408 ? 6.473   2.609   -21.421 0.5 40.68 ? 393 SER   B CB  1 
ATOM   5964 C  CB  B SER   B 1 408 ? 6.588   2.516   -21.53  0.5 38.81 ? 393 SER   B CB  1 
ATOM   5965 O  OG  A SER   B 1 408 ? 6.431   3.936   -21.913 0.5 43.91 ? 393 SER   B OG  1 
ATOM   5966 O  OG  B SER   B 1 408 ? 5.22    2.217   -21.753 0.5 40.2  ? 393 SER   B OG  1 
ATOM   5967 N  N   . THR   B 1 409 ? 7.419   0.271   -19.443 1   38.56 ? 394 THR   B N   1 
ATOM   5968 C  CA  . THR   B 1 409 ? 7.207   -1.024  -18.791 1   38.74 ? 394 THR   B CA  1 
ATOM   5969 C  C   . THR   B 1 409 ? 7.179   -0.827  -17.237 1   39.55 ? 394 THR   B C   1 
ATOM   5970 O  O   . THR   B 1 409 ? 6.336   -1.413  -16.522 1   40.35 ? 394 THR   B O   1 
ATOM   5971 C  CB  . THR   B 1 409 ? 8.313   -2.016  -19.226 1   38.92 ? 394 THR   B CB  1 
ATOM   5972 O  OG1 . THR   B 1 409 ? 8.323   -2.148  -20.649 1   39.41 ? 394 THR   B OG1 1 
ATOM   5973 C  CG2 . THR   B 1 409 ? 8.136   -3.393  -18.587 1   38.08 ? 394 THR   B CG2 1 
ATOM   5974 N  N   . THR   B 1 410 ? 8.044   0.072   -16.739 1   38.62 ? 395 THR   B N   1 
ATOM   5975 C  CA  . THR   B 1 410 ? 8.061   0.441   -15.33  1   38.51 ? 395 THR   B CA  1 
ATOM   5976 C  C   . THR   B 1 410 ? 6.754   1.15    -14.933 1   40.64 ? 395 THR   B C   1 
ATOM   5977 O  O   . THR   B 1 410 ? 6.146   0.794   -13.93  1   40.72 ? 395 THR   B O   1 
ATOM   5978 C  CB  . THR   B 1 410 ? 9.277   1.312   -14.995 1   37.17 ? 395 THR   B CB  1 
ATOM   5979 O  OG1 . THR   B 1 410 ? 10.451  0.793   -15.634 1   38.3  ? 395 THR   B OG1 1 
ATOM   5980 C  CG2 . THR   B 1 410 ? 9.487   1.459   -13.507 1   35.34 ? 395 THR   B CG2 1 
ATOM   5981 N  N   . GLU   B 1 411 ? 6.325   2.157   -15.707 1   41.92 ? 396 GLU   B N   1 
ATOM   5982 C  CA  . GLU   B 1 411 ? 5.083   2.912   -15.451 1   43.33 ? 396 GLU   B CA  1 
ATOM   5983 C  C   . GLU   B 1 411 ? 3.867   1.968   -15.405 1   43.43 ? 396 GLU   B C   1 
ATOM   5984 O  O   . GLU   B 1 411 ? 3.027   2.098   -14.52  1   42.82 ? 396 GLU   B O   1 
ATOM   5985 C  CB  . GLU   B 1 411 ? 4.856   3.977   -16.551 1   46.51 ? 396 GLU   B CB  1 
ATOM   5986 C  CG  . GLU   B 1 411 ? 5.37    5.37    -16.237 1   55.42 ? 396 GLU   B CG  1 
ATOM   5987 C  CD  . GLU   B 1 411 ? 5.462   6.333   -17.416 1   66.17 ? 396 GLU   B CD  1 
ATOM   5988 O  OE1 . GLU   B 1 411 ? 5.39    5.875   -18.582 1   66.49 ? 396 GLU   B OE1 1 
ATOM   5989 O  OE2 . GLU   B 1 411 ? 5.621   7.552   -17.168 1   70.98 ? 396 GLU   B OE2 1 
ATOM   5990 N  N   . LYS   B 1 412 ? 3.791   1.013   -16.353 1   43.58 ? 397 LYS   B N   1 
ATOM   5991 C  CA  . LYS   B 1 412 ? 2.691   0.052   -16.43  1   44.58 ? 397 LYS   B CA  1 
ATOM   5992 C  C   . LYS   B 1 412 ? 2.65    -0.96   -15.267 1   45.21 ? 397 LYS   B C   1 
ATOM   5993 O  O   . LYS   B 1 412 ? 1.722   -1.769  -15.189 1   45.71 ? 397 LYS   B O   1 
ATOM   5994 C  CB  . LYS   B 1 412 ? 2.698   -0.672  -17.785 1   46.5  ? 397 LYS   B CB  1 
ATOM   5995 C  CG  . LYS   B 1 412 ? 2.288   0.228   -18.94  1   51.35 ? 397 LYS   B CG  1 
ATOM   5996 C  CD  . LYS   B 1 412 ? 2.215   -0.538  -20.258 1   57.02 ? 397 LYS   B CD  1 
ATOM   5997 C  CE  . LYS   B 1 412 ? 3.556   -1.055  -20.708 1   62    ? 397 LYS   B CE  1 
ATOM   5998 N  NZ  . LYS   B 1 412 ? 3.671   -1.027  -22.191 1   65.3  ? 397 LYS   B NZ  1 
ATOM   5999 N  N   . SER   B 1 413 ? 3.66    -0.948  -14.394 1   44.45 ? 398 SER   B N   1 
ATOM   6000 C  CA  . SER   B 1 413 ? 3.679   -1.818  -13.231 1   44.75 ? 398 SER   B CA  1 
ATOM   6001 C  C   . SER   B 1 413 ? 2.975   -1.184  -12.025 1   45.45 ? 398 SER   B C   1 
ATOM   6002 O  O   . SER   B 1 413 ? 2.769   -1.87   -11.029 1   45    ? 398 SER   B O   1 
ATOM   6003 C  CB  . SER   B 1 413 ? 5.101   -2.205  -12.864 1   44.71 ? 398 SER   B CB  1 
ATOM   6004 O  OG  . SER   B 1 413 ? 5.655   -2.969  -13.919 1   48.19 ? 398 SER   B OG  1 
ATOM   6005 N  N   . LEU   B 1 414 ? 2.599   0.116   -12.095 1   46.31 ? 399 LEU   B N   1 
ATOM   6006 C  CA  . LEU   B 1 414 ? 1.893   0.763   -11.001 1   47.66 ? 399 LEU   B CA  1 
ATOM   6007 C  C   . LEU   B 1 414 ? 0.535   0.064   -10.808 1   50.07 ? 399 LEU   B C   1 
ATOM   6008 O  O   . LEU   B 1 414 ? -0.112  -0.321  -11.78  1   50.09 ? 399 LEU   B O   1 
ATOM   6009 C  CB  . LEU   B 1 414 ? 1.69    2.257   -11.282 1   47.16 ? 399 LEU   B CB  1 
ATOM   6010 C  CG  . LEU   B 1 414 ? 2.931   3.168   -11.137 1   48.24 ? 399 LEU   B CG  1 
ATOM   6011 C  CD1 . LEU   B 1 414 ? 2.659   4.547   -11.69  1   48.62 ? 399 LEU   B CD1 1 
ATOM   6012 C  CD2 . LEU   B 1 414 ? 3.38    3.286   -9.701  1   47.99 ? 399 LEU   B CD2 1 
ATOM   6013 N  N   . LEU   B 1 415 ? 0.191   -0.229  -9.565  1   51.98 ? 400 LEU   B N   1 
ATOM   6014 C  CA  . LEU   B 1 415 ? -1.066  -0.896  -9.247  1   53.85 ? 400 LEU   B CA  1 
ATOM   6015 C  C   . LEU   B 1 415 ? -2.202  0.095   -9.363  1   56.68 ? 400 LEU   B C   1 
ATOM   6016 O  O   . LEU   B 1 415 ? -3.242  -0.238  -9.931  1   57.24 ? 400 LEU   B O   1 
ATOM   6017 C  CB  . LEU   B 1 415 ? -1.007  -1.501  -7.841  1   53.58 ? 400 LEU   B CB  1 
ATOM   6018 C  CG  . LEU   B 1 415 ? 0.157   -2.444  -7.594  1   54.35 ? 400 LEU   B CG  1 
ATOM   6019 C  CD1 . LEU   B 1 415 ? 0.132   -2.961  -6.2    1   54.73 ? 400 LEU   B CD1 1 
ATOM   6020 C  CD2 . LEU   B 1 415 ? 0.177   -3.58   -8.588  1   54.83 ? 400 LEU   B CD2 1 
ATOM   6021 N  N   . LYS   B 1 416 ? -1.995  1.341   -8.874  1   58.01 ? 401 LYS   B N   1 
ATOM   6022 C  CA  . LYS   B 1 416 ? -3.029  2.358   -8.973  1   59.54 ? 401 LYS   B CA  1 
ATOM   6023 C  C   . LYS   B 1 416 ? -2.753  3.297   -10.133 1   60.41 ? 401 LYS   B C   1 
ATOM   6024 O  O   . LYS   B 1 416 ? -3.255  3.037   -11.225 1   61.01 ? 401 LYS   B O   1 
ATOM   6025 C  CB  . LYS   B 1 416 ? -3.182  3.121   -7.661  1   61.29 ? 401 LYS   B CB  1 
HETATM 6026 C  CHA . HEM   C 2 .   ? 16.504  -29.907 -32.006 1   29.35 ? 501 HEM   A CHA 1 
HETATM 6027 C  CHB . HEM   C 2 .   ? 14.315  -32.152 -35.636 1   29.29 ? 501 HEM   A CHB 1 
HETATM 6028 C  CHC . HEM   C 2 .   ? 13.101  -35.882 -32.8   1   29.68 ? 501 HEM   A CHC 1 
HETATM 6029 C  CHD . HEM   C 2 .   ? 15.246  -33.557 -29.087 1   26.79 ? 501 HEM   A CHD 1 
HETATM 6030 C  C1A . HEM   C 2 .   ? 15.938  -30.162 -33.257 1   30.15 ? 501 HEM   A C1A 1 
HETATM 6031 C  C2A . HEM   C 2 .   ? 16.008  -29.263 -34.403 1   31.14 ? 501 HEM   A C2A 1 
HETATM 6032 C  C3A . HEM   C 2 .   ? 15.397  -29.912 -35.443 1   30.71 ? 501 HEM   A C3A 1 
HETATM 6033 C  C4A . HEM   C 2 .   ? 14.958  -31.195 -34.922 1   29.63 ? 501 HEM   A C4A 1 
HETATM 6034 C  CMA . HEM   C 2 .   ? 15.177  -29.422 -36.845 1   31.07 ? 501 HEM   A CMA 1 
HETATM 6035 C  CAA . HEM   C 2 .   ? 16.642  -27.901 -34.476 1   32.74 ? 501 HEM   A CAA 1 
HETATM 6036 C  CBA . HEM   C 2 .   ? 15.92   -26.835 -33.64  1   34.17 ? 501 HEM   A CBA 1 
HETATM 6037 C  CGA . HEM   C 2 .   ? 14.64   -26.304 -34.222 1   36.06 ? 501 HEM   A CGA 1 
HETATM 6038 O  O1A . HEM   C 2 .   ? 13.728  -25.926 -33.52  1   36.11 ? 501 HEM   A O1A 1 
HETATM 6039 O  O2A . HEM   C 2 .   ? 14.583  -26.245 -35.519 1   37.71 ? 501 HEM   A O2A 1 
HETATM 6040 C  C1B . HEM   C 2 .   ? 13.828  -33.39  -35.213 1   29.34 ? 501 HEM   A C1B 1 
HETATM 6041 C  C2B . HEM   C 2 .   ? 13.166  -34.322 -36.092 1   29.71 ? 501 HEM   A C2B 1 
HETATM 6042 C  C3B . HEM   C 2 .   ? 12.806  -35.38  -35.268 1   30.46 ? 501 HEM   A C3B 1 
HETATM 6043 C  C4B . HEM   C 2 .   ? 13.261  -35.096 -33.934 1   29.67 ? 501 HEM   A C4B 1 
HETATM 6044 C  CMB . HEM   C 2 .   ? 13.008  -34.142 -37.573 1   28.91 ? 501 HEM   A CMB 1 
HETATM 6045 C  CAB . HEM   C 2 .   ? 12.07   -36.581 -35.666 1   31.58 ? 501 HEM   A CAB 1 
HETATM 6046 C  CBB . HEM   C 2 .   ? 10.999  -36.616 -36.482 1   32.29 ? 501 HEM   A CBB 1 
HETATM 6047 C  C1C . HEM   C 2 .   ? 13.529  -35.537 -31.479 1   29.28 ? 501 HEM   A C1C 1 
HETATM 6048 C  C2C . HEM   C 2 .   ? 13.195  -36.277 -30.277 1   28.77 ? 501 HEM   A C2C 1 
HETATM 6049 C  C3C . HEM   C 2 .   ? 13.781  -35.577 -29.255 1   28.65 ? 501 HEM   A C3C 1 
HETATM 6050 C  C4C . HEM   C 2 .   ? 14.475  -34.465 -29.808 1   27.79 ? 501 HEM   A C4C 1 
HETATM 6051 C  CMC . HEM   C 2 .   ? 12.439  -37.573 -30.234 1   29.55 ? 501 HEM   A CMC 1 
HETATM 6052 C  CAC . HEM   C 2 .   ? 13.747  -35.878 -27.824 1   29.4  ? 501 HEM   A CAC 1 
HETATM 6053 C  CBC . HEM   C 2 .   ? 13.173  -35.202 -26.846 1   30.17 ? 501 HEM   A CBC 1 
HETATM 6054 C  C1D . HEM   C 2 .   ? 15.88   -32.398 -29.581 1   27.08 ? 501 HEM   A C1D 1 
HETATM 6055 C  C2D . HEM   C 2 .   ? 16.662  -31.473 -28.779 1   27.58 ? 501 HEM   A C2D 1 
HETATM 6056 C  C3D . HEM   C 2 .   ? 17.036  -30.452 -29.623 1   28.3  ? 501 HEM   A C3D 1 
HETATM 6057 C  C4D . HEM   C 2 .   ? 16.453  -30.753 -30.912 1   28.72 ? 501 HEM   A C4D 1 
HETATM 6058 C  CMD . HEM   C 2 .   ? 16.909  -31.591 -27.306 1   27.06 ? 501 HEM   A CMD 1 
HETATM 6059 C  CAD . HEM   C 2 .   ? 17.867  -29.238 -29.319 1   28.66 ? 501 HEM   A CAD 1 
HETATM 6060 C  CBD . HEM   C 2 .   ? 19.293  -29.358 -29.849 1   28.73 ? 501 HEM   A CBD 1 
HETATM 6061 C  CGD . HEM   C 2 .   ? 20.17   -30.292 -29.062 1   28.44 ? 501 HEM   A CGD 1 
HETATM 6062 O  O1D . HEM   C 2 .   ? 20.939  -31.071 -29.603 1   29.49 ? 501 HEM   A O1D 1 
HETATM 6063 O  O2D . HEM   C 2 .   ? 20.092  -30.149 -27.766 1   26.74 ? 501 HEM   A O2D 1 
HETATM 6064 N  NA  . HEM   C 2 .   ? 15.292  -31.313 -33.587 1   29.27 ? 501 HEM   A NA  1 
HETATM 6065 N  NB  . HEM   C 2 .   ? 13.883  -33.868 -33.938 1   29.63 ? 501 HEM   A NB  1 
HETATM 6066 N  NC  . HEM   C 2 .   ? 14.295  -34.457 -31.185 1   28.61 ? 501 HEM   A NC  1 
HETATM 6067 N  ND  . HEM   C 2 .   ? 15.768  -31.957 -30.852 1   28.06 ? 501 HEM   A ND  1 
HETATM 6068 FE FE  . HEM   C 2 .   ? 14.821  -32.914 -32.398 1   28.7  ? 501 HEM   A FE  1 
HETATM 6069 N  N1  . A1H6R D 3 .   ? 11.57   -30.71  -31.846 1   34.46 ? 502 A1H6R A N1  1 
HETATM 6070 C  C4  . A1H6R D 3 .   ? 10.602  -28.8   -37.356 1   40.97 ? 502 A1H6R A C4  1 
HETATM 6071 C  C5  . A1H6R D 3 .   ? 10.82   -27.402 -36.744 1   41.08 ? 502 A1H6R A C5  1 
HETATM 6072 C  C6  . A1H6R D 3 .   ? 10.518  -27.407 -35.229 1   40.75 ? 502 A1H6R A C6  1 
HETATM 6073 C  C7  . A1H6R D 3 .   ? 10.615  -29.681 -32.322 1   34.76 ? 502 A1H6R A C7  1 
HETATM 6074 C  C8  . A1H6R D 3 .   ? 9.424   -29.793 -31.414 1   34.52 ? 502 A1H6R A C8  1 
HETATM 6075 C  C10 . A1H6R D 3 .   ? 6.915   -29.682 -31.637 1   34.17 ? 502 A1H6R A C10 1 
HETATM 6076 C  C13 . A1H6R D 3 .   ? 7.981   -28.353 -29.932 1   33.49 ? 502 A1H6R A C13 1 
HETATM 6077 C  C15 . A1H6R D 3 .   ? 11.846  -32.767 -31.097 1   32.94 ? 502 A1H6R A C15 1 
HETATM 6078 O  O   . A1H6R D 3 .   ? 12.423  -28.14  -32.621 1   35.29 ? 502 A1H6R A O   1 
HETATM 6079 C  C   . A1H6R D 3 .   ? 11.088  -28.433 -33.005 1   36.09 ? 502 A1H6R A C   1 
HETATM 6080 C  C1  . A1H6R D 3 .   ? 11.353  -28.458 -34.51  1   39.04 ? 502 A1H6R A C1  1 
HETATM 6081 C  C3  . A1H6R D 3 .   ? 11.389  -29.866 -36.585 1   40.49 ? 502 A1H6R A C3  1 
HETATM 6082 C  C2  . A1H6R D 3 .   ? 11.056  -29.821 -35.089 1   39.98 ? 502 A1H6R A C2  1 
HETATM 6083 C  C16 . A1H6R D 3 .   ? 12.754  -31.144 -32.423 1   33.85 ? 502 A1H6R A C16 1 
HETATM 6084 N  N   . A1H6R D 3 .   ? 12.916  -32.391 -31.87  1   33.18 ? 502 A1H6R A N   1 
HETATM 6085 C  C14 . A1H6R D 3 .   ? 10.923  -31.788 -31.358 1   33.95 ? 502 A1H6R A C14 1 
HETATM 6086 S  S   . A1H6R D 3 .   ? 9.444   -31.373 -30.625 1   34.47 ? 502 A1H6R A S   1 
HETATM 6087 C  C9  . A1H6R D 3 .   ? 8.203   -28.946 -31.323 1   34.1  ? 502 A1H6R A C9  1 
HETATM 6088 C  C12 . A1H6R D 3 .   ? 6.501   -27.968 -29.934 1   33.75 ? 502 A1H6R A C12 1 
HETATM 6089 C  C11 . A1H6R D 3 .   ? 5.836   -28.782 -31.042 1   34.14 ? 502 A1H6R A C11 1 
HETATM 6090 C  CHA . HEM   E 2 .   ? 20.978  3.283   -20.23  1   32.04 ? 501 HEM   B CHA 1 
HETATM 6091 C  CHB . HEM   E 2 .   ? 22.95   7.407   -21.757 1   33.84 ? 501 HEM   B CHB 1 
HETATM 6092 C  CHC . HEM   E 2 .   ? 23.929  8.787   -17.205 1   33.35 ? 501 HEM   B CHC 1 
HETATM 6093 C  CHD . HEM   E 2 .   ? 22.092  4.511   -15.707 1   30.71 ? 501 HEM   B CHD 1 
HETATM 6094 C  C1A . HEM   E 2 .   ? 21.519  4.281   -21.074 1   33.26 ? 501 HEM   B C1A 1 
HETATM 6095 C  C2A . HEM   E 2 .   ? 21.476  4.25    -22.527 1   33.87 ? 501 HEM   B C2A 1 
HETATM 6096 C  C3A . HEM   E 2 .   ? 22.014  5.434   -22.959 1   34.04 ? 501 HEM   B C3A 1 
HETATM 6097 C  C4A . HEM   E 2 .   ? 22.399  6.164   -21.769 1   33.66 ? 501 HEM   B C4A 1 
HETATM 6098 C  CMA . HEM   E 2 .   ? 22.183  5.92    -24.367 1   33.8  ? 501 HEM   B CMA 1 
HETATM 6099 C  CAA . HEM   E 2 .   ? 20.979  3.132   -23.403 1   35.53 ? 501 HEM   B CAA 1 
HETATM 6100 C  CBA . HEM   E 2 .   ? 21.865  1.887   -23.358 1   36.96 ? 501 HEM   B CBA 1 
HETATM 6101 C  CGA . HEM   E 2 .   ? 23.117  2.006   -24.179 1   38.7  ? 501 HEM   B CGA 1 
HETATM 6102 O  O1A . HEM   E 2 .   ? 23.134  2.598   -25.251 1   40.36 ? 501 HEM   B O1A 1 
HETATM 6103 O  O2A . HEM   E 2 .   ? 24.185  1.461   -23.639 1   37.95 ? 501 HEM   B O2A 1 
HETATM 6104 C  C1B . HEM   E 2 .   ? 23.341  8.184   -20.664 1   34.31 ? 501 HEM   B C1B 1 
HETATM 6105 C  C2B . HEM   E 2 .   ? 23.875  9.528   -20.785 1   35.71 ? 501 HEM   B C2B 1 
HETATM 6106 C  C3B . HEM   E 2 .   ? 24.163  9.908   -19.497 1   35.97 ? 501 HEM   B C3B 1 
HETATM 6107 C  C4B . HEM   E 2 .   ? 23.795  8.83    -18.603 1   34.4  ? 501 HEM   B C4B 1 
HETATM 6108 C  CMB . HEM   E 2 .   ? 24.029  10.28   -22.076 1   36.17 ? 501 HEM   B CMB 1 
HETATM 6109 C  CAB . HEM   E 2 .   ? 24.807  11.159  -19.095 1   37.43 ? 501 HEM   B CAB 1 
HETATM 6110 C  CBB . HEM   E 2 .   ? 25.825  11.764  -19.68  1   38.19 ? 501 HEM   B CBB 1 
HETATM 6111 C  C1C . HEM   E 2 .   ? 23.564  7.676   -16.378 1   32.97 ? 501 HEM   B C1C 1 
HETATM 6112 C  C2C . HEM   E 2 .   ? 23.84   7.573   -14.949 1   32.41 ? 501 HEM   B C2C 1 
HETATM 6113 C  C3C . HEM   E 2 .   ? 23.347  6.347   -14.568 1   31.63 ? 501 HEM   B C3C 1 
HETATM 6114 C  C4C . HEM   E 2 .   ? 22.775  5.734   -15.724 1   31.32 ? 501 HEM   B C4C 1 
HETATM 6115 C  CMC . HEM   E 2 .   ? 24.513  8.617   -14.108 1   32.62 ? 501 HEM   B CMC 1 
HETATM 6116 C  CAC . HEM   E 2 .   ? 23.413  5.734   -13.237 1   31.88 ? 501 HEM   B CAC 1 
HETATM 6117 C  CBC . HEM   E 2 .   ? 24.036  4.615   -12.837 1   31.8  ? 501 HEM   B CBC 1 
HETATM 6118 C  C1D . HEM   E 2 .   ? 21.525  3.844   -16.788 1   30.43 ? 501 HEM   B C1D 1 
HETATM 6119 C  C2D . HEM   E 2 .   ? 20.82   2.58    -16.702 1   30.83 ? 501 HEM   B C2D 1 
HETATM 6120 C  C3D . HEM   E 2 .   ? 20.497  2.231   -17.994 1   30.77 ? 501 HEM   B C3D 1 
HETATM 6121 C  C4D . HEM   E 2 .   ? 21.024  3.285   -18.848 1   31.51 ? 501 HEM   B C4D 1 
HETATM 6122 C  CMD . HEM   E 2 .   ? 20.562  1.816   -15.437 1   30.97 ? 501 HEM   B CMD 1 
HETATM 6123 C  CAD . HEM   E 2 .   ? 19.74   1.026   -18.477 1   29.96 ? 501 HEM   B CAD 1 
HETATM 6124 C  CBD . HEM   E 2 .   ? 18.297  1.357   -18.844 1   30.11 ? 501 HEM   B CBD 1 
HETATM 6125 C  CGD . HEM   E 2 .   ? 17.395  1.577   -17.659 1   30.52 ? 501 HEM   B CGD 1 
HETATM 6126 O  O1D . HEM   E 2 .   ? 16.573  2.474   -17.611 1   30.95 ? 501 HEM   B O1D 1 
HETATM 6127 O  O2D . HEM   E 2 .   ? 17.538  0.7     -16.697 1   29.58 ? 501 HEM   B O2D 1 
HETATM 6128 N  NA  . HEM   E 2 .   ? 22.094  5.431   -20.638 1   32.84 ? 501 HEM   B NA  1 
HETATM 6129 N  NB  . HEM   E 2 .   ? 23.295  7.786   -19.373 1   34.08 ? 501 HEM   B NB  1 
HETATM 6130 N  NC  . HEM   E 2 .   ? 22.925  6.554   -16.833 1   30.81 ? 501 HEM   B NC  1 
HETATM 6131 N  ND  . HEM   E 2 .   ? 21.628  4.252   -18.076 1   31.5  ? 501 HEM   B ND  1 
HETATM 6132 FE FE  . HEM   E 2 .   ? 22.486  5.994   -18.726 1   32.52 ? 501 HEM   B FE  1 
HETATM 6133 N  N1  . A1H6R F 3 .   ? 25.955  4.143   -19.451 1   35.38 ? 502 A1H6R B N1  1 
HETATM 6134 C  C4  . A1H6R F 3 .   ? 27.463  6.511   -24.413 1   40.69 ? 502 A1H6R B C4  1 
HETATM 6135 C  C5  . A1H6R F 3 .   ? 26.273  5.585   -24.71  1   40.75 ? 502 A1H6R B C5  1 
HETATM 6136 C  C6  . A1H6R F 3 .   ? 25.887  4.762   -23.46  1   40.12 ? 502 A1H6R B C6  1 
HETATM 6137 C  C7  . A1H6R F 3 .   ? 27.011  3.692   -20.401 1   36.34 ? 502 A1H6R B C7  1 
HETATM 6138 C  C8  . A1H6R F 3 .   ? 28.202  3.353   -19.556 1   36.51 ? 502 A1H6R B C8  1 
HETATM 6139 C  C10 . A1H6R F 3 .   ? 29.746  1.365   -19.273 1   37.66 ? 502 A1H6R B C10 1 
HETATM 6140 C  C13 . A1H6R F 3 .   ? 30.726  3.554   -19.574 1   37.61 ? 502 A1H6R B C13 1 
HETATM 6141 C  C15 . A1H6R F 3 .   ? 25.516  5.231   -17.543 1   34.02 ? 502 A1H6R B C15 1 
HETATM 6142 O  O   . A1H6R F 3 .   ? 25.327  2.613   -21.689 1   37.2  ? 502 A1H6R B O   1 
HETATM 6143 C  C   . A1H6R F 3 .   ? 26.674  3.088   -21.716 1   37.6  ? 502 A1H6R B C   1 
HETATM 6144 C  C1  . A1H6R F 3 .   ? 27.073  3.948   -22.953 1   39.29 ? 502 A1H6R B C1  1 
HETATM 6145 C  C3  . A1H6R F 3 .   ? 28.652  5.717   -23.852 1   40.39 ? 502 A1H6R B C3  1 
HETATM 6146 C  C2  . A1H6R F 3 .   ? 28.232  4.891   -22.616 1   39.94 ? 502 A1H6R B C2  1 
HETATM 6147 C  C16 . A1H6R F 3 .   ? 24.744  4.786   -19.658 1   34.84 ? 502 A1H6R B C16 1 
HETATM 6148 N  N   . A1H6R F 3 .   ? 24.471  5.326   -18.42  1   34.53 ? 502 A1H6R B N   1 
HETATM 6149 C  C14 . A1H6R F 3 .   ? 26.487  4.702   -18.351 1   35.02 ? 502 A1H6R B C14 1 
HETATM 6150 S  S   . A1H6R F 3 .   ? 27.996  4.053   -17.97  1   36.1  ? 502 A1H6R B S   1 
HETATM 6151 C  C9  . A1H6R F 3 .   ? 29.5    2.727   -19.911 1   37.45 ? 502 A1H6R B C9  1 
HETATM 6152 C  C12 . A1H6R F 3 .   ? 31.857  2.518   -19.627 1   38.55 ? 502 A1H6R B C12 1 
HETATM 6153 C  C11 . A1H6R F 3 .   ? 31.235  1.124   -19.49  1   38.1  ? 502 A1H6R B C11 1 
HETATM 6154 O  O   . HOH   G 4 .   ? 6.594   -30.875 -13.699 1   37.02 ? 601 HOH   A O   1 
HETATM 6155 O  O   . HOH   G 4 .   ? -12.824 -16.541 -26.571 1   36.66 ? 602 HOH   A O   1 
HETATM 6156 O  O   . HOH   G 4 .   ? -3.796  -36.422 -19.143 1   40.14 ? 603 HOH   A O   1 
HETATM 6157 O  O   . HOH   G 4 .   ? 12.176  -17.336 -14.468 1   49.38 ? 604 HOH   A O   1 
HETATM 6158 O  O   . HOH   G 4 .   ? -9.287  -34.111 -42.075 1   50.51 ? 605 HOH   A O   1 
HETATM 6159 O  O   . HOH   G 4 .   ? 15.165  -17.343 -13.241 1   46.49 ? 606 HOH   A O   1 
HETATM 6160 O  O   . HOH   G 4 .   ? -18.017 -22.146 -24.766 1   45.97 ? 607 HOH   A O   1 
HETATM 6161 O  O   . HOH   G 4 .   ? 34.18   -43.001 -19.95  1   41.53 ? 608 HOH   A O   1 
HETATM 6162 O  O   . HOH   G 4 .   ? 21.61   -27.183 -24.415 1   33.47 ? 609 HOH   A O   1 
HETATM 6163 O  O   . HOH   G 4 .   ? -7.131  -31.432 -32.989 1   41.99 ? 610 HOH   A O   1 
HETATM 6164 O  O   . HOH   G 4 .   ? 32.785  -43.317 -22.067 1   52.91 ? 611 HOH   A O   1 
HETATM 6165 O  O   . HOH   G 4 .   ? -0.326  -7.105  -31.584 1   41.99 ? 612 HOH   A O   1 
HETATM 6166 O  O   . HOH   G 4 .   ? 11.902  -32.445 -6.393  1   57.71 ? 613 HOH   A O   1 
HETATM 6167 O  O   . HOH   G 4 .   ? -10.894 -33.576 -36.598 1   41.3  ? 614 HOH   A O   1 
HETATM 6168 O  O   . HOH   G 4 .   ? -3.711  -48.948 -22.5   1   47.79 ? 615 HOH   A O   1 
HETATM 6169 O  O   . HOH   G 4 .   ? 13.792  -15.283 -25.238 1   41.42 ? 616 HOH   A O   1 
HETATM 6170 O  O   . HOH   G 4 .   ? -13.987 -35.56  -36.252 1   38.15 ? 617 HOH   A O   1 
HETATM 6171 O  O   . HOH   G 4 .   ? -3.014  -36.355 -36.857 1   47.26 ? 618 HOH   A O   1 
HETATM 6172 O  O   . HOH   G 4 .   ? 37.507  -31.467 -23.413 1   31.96 ? 619 HOH   A O   1 
HETATM 6173 O  O   . HOH   G 4 .   ? 28.411  -28.123 -13.251 1   42.29 ? 620 HOH   A O   1 
HETATM 6174 O  O   . HOH   G 4 .   ? 28.008  -43.311 -22.284 1   36.45 ? 621 HOH   A O   1 
HETATM 6175 O  O   . HOH   G 4 .   ? -0.888  -45.502 -28.421 1   44.36 ? 622 HOH   A O   1 
HETATM 6176 O  O   . HOH   G 4 .   ? 27.02   -45.94  -16.343 1   47.96 ? 623 HOH   A O   1 
HETATM 6177 O  O   . HOH   G 4 .   ? 14.617  -37.737 -11.64  1   41.35 ? 624 HOH   A O   1 
HETATM 6178 O  O   . HOH   G 4 .   ? 34.711  -44.602 -13.691 1   38.05 ? 625 HOH   A O   1 
HETATM 6179 O  O   . HOH   G 4 .   ? 3.973   -21.278 -15.923 1   45.28 ? 626 HOH   A O   1 
HETATM 6180 O  O   . HOH   G 4 .   ? -8.774  -23.973 -43.575 1   48.51 ? 627 HOH   A O   1 
HETATM 6181 O  O   . HOH   G 4 .   ? 0.578   -25.838 -21.648 1   30.14 ? 628 HOH   A O   1 
HETATM 6182 O  O   . HOH   G 4 .   ? 19.641  -28.222 -25.978 1   33.34 ? 629 HOH   A O   1 
HETATM 6183 O  O   . HOH   G 4 .   ? 0.134   -22.054 -26.265 1   26.36 ? 630 HOH   A O   1 
HETATM 6184 O  O   . HOH   G 4 .   ? 12.072  -24.018 -34.389 1   47.49 ? 631 HOH   A O   1 
HETATM 6185 O  O   . HOH   G 4 .   ? 11.439  -13.831 -28.594 1   48.91 ? 632 HOH   A O   1 
HETATM 6186 O  O   . HOH   G 4 .   ? 36.51   -40.623 -23.116 1   48.68 ? 633 HOH   A O   1 
HETATM 6187 O  O   . HOH   G 4 .   ? 12.962  -25.091 -37.313 1   48.19 ? 634 HOH   A O   1 
HETATM 6188 O  O   . HOH   G 4 .   ? 17.962  -16.538 -31.359 1   44.14 ? 635 HOH   A O   1 
HETATM 6189 O  O   . HOH   G 4 .   ? 5.051   -33.142 -9.367  1   56.13 ? 636 HOH   A O   1 
HETATM 6190 O  O   . HOH   G 4 .   ? 39.070  -39.762 -31.717 1   51.85 ? 637 HOH   A O   1 
HETATM 6191 O  O   . HOH   G 4 .   ? -13.452 -20.315 -42.711 1   36.52 ? 638 HOH   A O   1 
HETATM 6192 O  O   . HOH   G 4 .   ? 37.818  -45.687 -4.161  1   36.77 ? 639 HOH   A O   1 
HETATM 6193 O  O   . HOH   G 4 .   ? -3.149  -29.584 -18.188 1   30.8  ? 640 HOH   A O   1 
HETATM 6194 O  O   . HOH   G 4 .   ? -13.563 -14.373 -32.584 1   59.19 ? 641 HOH   A O   1 
HETATM 6195 O  O   . HOH   G 4 .   ? 24.446  -42.52  -31.713 1   42.91 ? 642 HOH   A O   1 
HETATM 6196 O  O   . HOH   G 4 .   ? 4       -22.357 -41.9   1   37.4  ? 643 HOH   A O   1 
HETATM 6197 O  O   . HOH   G 4 .   ? 28.339  -39.726 0.327   1   63.28 ? 644 HOH   A O   1 
HETATM 6198 O  O   . HOH   G 4 .   ? 39.495  -37.451 -6.696  1   38.29 ? 645 HOH   A O   1 
HETATM 6199 O  O   . HOH   G 4 .   ? 10.857  -12.024 -30.265 1   39.92 ? 646 HOH   A O   1 
HETATM 6200 O  O   . HOH   G 4 .   ? 12.127  -22.007 -32.647 1   40.16 ? 647 HOH   A O   1 
HETATM 6201 O  O   . HOH   G 4 .   ? 33.006  -27.803 -22.244 1   48.68 ? 648 HOH   A O   1 
HETATM 6202 O  O   . HOH   G 4 .   ? 9.786   -42.254 -15.401 1   48.96 ? 649 HOH   A O   1 
HETATM 6203 O  O   . HOH   G 4 .   ? 31.594  -27.848 -4.344  1   47.36 ? 650 HOH   A O   1 
HETATM 6204 O  O   . HOH   G 4 .   ? 16.979  -28.45  -25.107 1   26.81 ? 651 HOH   A O   1 
HETATM 6205 O  O   . HOH   G 4 .   ? 39.664  -27.229 -12.682 1   43.84 ? 652 HOH   A O   1 
HETATM 6206 O  O   . HOH   G 4 .   ? 11.873  -34.04  -18.34  1   31.56 ? 653 HOH   A O   1 
HETATM 6207 O  O   . HOH   G 4 .   ? 0.852   -12.266 -23.122 1   42.32 ? 654 HOH   A O   1 
HETATM 6208 O  O   . HOH   G 4 .   ? 26.945  -26.13  -12.29  1   39.47 ? 655 HOH   A O   1 
HETATM 6209 O  O   . HOH   G 4 .   ? 28.761  -28.592 -4.932  1   36.81 ? 656 HOH   A O   1 
HETATM 6210 O  O   . HOH   G 4 .   ? 34.12   -26.713 -9.273  1   39.33 ? 657 HOH   A O   1 
HETATM 6211 O  O   . HOH   G 4 .   ? 7.658   -21.245 -29.273 1   32.09 ? 658 HOH   A O   1 
HETATM 6212 O  O   . HOH   G 4 .   ? -3.289  -11.891 -17.239 1   46.8  ? 659 HOH   A O   1 
HETATM 6213 O  O   . HOH   G 4 .   ? 22.856  -42.002 -25.111 1   35.64 ? 660 HOH   A O   1 
HETATM 6214 O  O   . HOH   G 4 .   ? 10.487  -27.383 -19.424 1   33.08 ? 661 HOH   A O   1 
HETATM 6215 O  O   . HOH   G 4 .   ? 11.54   -29.652 -20.767 1   27.34 ? 662 HOH   A O   1 
HETATM 6216 O  O   . HOH   G 4 .   ? 21.617  -33.559 -33.278 1   28.94 ? 663 HOH   A O   1 
HETATM 6217 O  O   . HOH   G 4 .   ? 41.487  -35.232 -13.288 1   51.12 ? 664 HOH   A O   1 
HETATM 6218 O  O   . HOH   G 4 .   ? 8.613   -24.825 -23.582 1   26.51 ? 665 HOH   A O   1 
HETATM 6219 O  O   . HOH   G 4 .   ? 5.736   -28.644 -17.782 1   31.05 ? 666 HOH   A O   1 
HETATM 6220 O  O   . HOH   G 4 .   ? -3.23   -30.382 -20.855 1   30.57 ? 667 HOH   A O   1 
HETATM 6221 O  O   . HOH   G 4 .   ? 19.019  -25.36  -1.688  1   52.51 ? 668 HOH   A O   1 
HETATM 6222 O  O   . HOH   G 4 .   ? 10.027  -26.259 -21.807 1   28.31 ? 669 HOH   A O   1 
HETATM 6223 O  O   . HOH   G 4 .   ? 22.726  -31.626 -31.753 1   30.89 ? 670 HOH   A O   1 
HETATM 6224 O  O   . HOH   G 4 .   ? 10.191  -42.961 -21.294 1   35.96 ? 671 HOH   A O   1 
HETATM 6225 O  O   . HOH   G 4 .   ? 10.417  -29.951 -8.121  1   38.43 ? 672 HOH   A O   1 
HETATM 6226 O  O   . HOH   G 4 .   ? -6.774  -32.691 -42.016 1   33.66 ? 673 HOH   A O   1 
HETATM 6227 O  O   . HOH   G 4 .   ? 29.058  -32.234 -35.11  1   42.53 ? 674 HOH   A O   1 
HETATM 6228 O  O   . HOH   G 4 .   ? 5.059   -10.768 -44.393 1   48.61 ? 675 HOH   A O   1 
HETATM 6229 O  O   . HOH   G 4 .   ? 37.096  -35.834 -3.104  1   48.39 ? 676 HOH   A O   1 
HETATM 6230 O  O   . HOH   G 4 .   ? 3.262   -13.458 -22.105 1   39.79 ? 677 HOH   A O   1 
HETATM 6231 O  O   . HOH   G 4 .   ? -17.393 -21.274 -33.089 1   44.37 ? 678 HOH   A O   1 
HETATM 6232 O  O   . HOH   G 4 .   ? 18.232  -14.507 -24.039 1   48.09 ? 679 HOH   A O   1 
HETATM 6233 O  O   . HOH   G 4 .   ? 26.676  -26.912 -4.689  1   40.67 ? 680 HOH   A O   1 
HETATM 6234 O  O   . HOH   G 4 .   ? 2.841   -35.057 -26.012 1   44.57 ? 681 HOH   A O   1 
HETATM 6235 O  O   . HOH   G 4 .   ? 23.078  -17.892 -12.801 1   49.4  ? 682 HOH   A O   1 
HETATM 6236 O  O   . HOH   G 4 .   ? -13.655 -29.667 -22.37  1   48.47 ? 683 HOH   A O   1 
HETATM 6237 O  O   . HOH   G 4 .   ? 15.533  -33.719 -4.166  1   51.36 ? 684 HOH   A O   1 
HETATM 6238 O  O   . HOH   G 4 .   ? 26.103  -41.904 -5.693  1   40.89 ? 685 HOH   A O   1 
HETATM 6239 O  O   . HOH   G 4 .   ? -5.619  -21.709 -46.166 1   45.29 ? 686 HOH   A O   1 
HETATM 6240 O  O   . HOH   G 4 .   ? 30.315  -28.492 -15.132 1   43.51 ? 687 HOH   A O   1 
HETATM 6241 O  O   . HOH   G 4 .   ? 20.336  -17.252 -32.788 1   39.14 ? 688 HOH   A O   1 
HETATM 6242 O  O   . HOH   G 4 .   ? 2.102   -44.645 -35.041 1   47.2  ? 689 HOH   A O   1 
HETATM 6243 O  O   . HOH   G 4 .   ? -16.921 -23.567 -31.633 1   38.74 ? 690 HOH   A O   1 
HETATM 6244 O  O   . HOH   G 4 .   ? -5.639  -36.461 -36.528 1   42.56 ? 691 HOH   A O   1 
HETATM 6245 O  O   . HOH   G 4 .   ? -12.029 -34.007 -42.858 1   49.31 ? 692 HOH   A O   1 
HETATM 6246 O  O   . HOH   G 4 .   ? 7.977   -43.118 -19.738 1   38.54 ? 693 HOH   A O   1 
HETATM 6247 O  O   . HOH   G 4 .   ? 25.733  -37.04  -2.183  1   45.58 ? 694 HOH   A O   1 
HETATM 6248 O  O   . HOH   G 4 .   ? 7.858   -40.784 -46.273 1   48.69 ? 695 HOH   A O   1 
HETATM 6249 O  O   . HOH   G 4 .   ? 10.673  -19.578 -35.538 1   50.06 ? 696 HOH   A O   1 
HETATM 6250 O  O   . HOH   G 4 .   ? 8.357   -8.367  -31.335 1   48.42 ? 697 HOH   A O   1 
HETATM 6251 O  O   . HOH   G 4 .   ? 5.715   -45.43  -15.982 1   50.62 ? 698 HOH   A O   1 
HETATM 6252 O  O   . HOH   G 4 .   ? 26.202  -31.178 2.112   1   70.05 ? 699 HOH   A O   1 
HETATM 6253 O  O   . HOH   G 4 .   ? 0.584   -20.735 -31.59  1   39.84 ? 700 HOH   A O   1 
HETATM 6254 O  O   . HOH   G 4 .   ? 22.231  -24.975 -22.715 1   53.52 ? 701 HOH   A O   1 
HETATM 6255 O  O   . HOH   G 4 .   ? -12.879 -11.533 -32.463 1   39.7  ? 702 HOH   A O   1 
HETATM 6256 O  O   . HOH   G 4 .   ? 2.086   -38.299 -14.767 1   42.4  ? 703 HOH   A O   1 
HETATM 6257 O  O   . HOH   G 4 .   ? 6.568   -22.941 -13.941 1   34.89 ? 704 HOH   A O   1 
HETATM 6258 O  O   . HOH   G 4 .   ? -10.539 -22.028 -42.637 1   35.65 ? 705 HOH   A O   1 
HETATM 6259 O  O   . HOH   G 4 .   ? 26.968  -20.893 -33.816 1   60.96 ? 706 HOH   A O   1 
HETATM 6260 O  O   . HOH   G 4 .   ? 19.317  -23.587 -45.082 1   60.27 ? 707 HOH   A O   1 
HETATM 6261 O  O   . HOH   G 4 .   ? -3.314  -27.846 -11.05  1   46.91 ? 708 HOH   A O   1 
HETATM 6262 O  O   . HOH   G 4 .   ? 0.314   -2.256  -26.679 1   59.08 ? 709 HOH   A O   1 
HETATM 6263 O  O   . HOH   G 4 .   ? 2.226   -2.465  -28.433 1   43.14 ? 710 HOH   A O   1 
HETATM 6264 O  O   . HOH   G 4 .   ? 8.967   -13.339 -18.037 1   50.81 ? 711 HOH   A O   1 
HETATM 6265 O  O   . HOH   G 4 .   ? -0.433  -27.134 -49.147 1   63.2  ? 712 HOH   A O   1 
HETATM 6266 O  O   . HOH   G 4 .   ? 34.196  -46.314 -6.434  1   59.07 ? 713 HOH   A O   1 
HETATM 6267 O  O   . HOH   G 4 .   ? 27.882  -36.724 -0.355  1   46.68 ? 714 HOH   A O   1 
HETATM 6268 O  O   . HOH   G 4 .   ? 5.424   -25.547 -14.418 1   51.38 ? 715 HOH   A O   1 
HETATM 6269 O  O   . HOH   G 4 .   ? 11.809  -49.121 -30.869 1   52.8  ? 716 HOH   A O   1 
HETATM 6270 O  O   . HOH   G 4 .   ? 13.368  -22.249 -5.471  1   48.73 ? 717 HOH   A O   1 
HETATM 6271 O  O   . HOH   G 4 .   ? 5.184   -30.919 -11.141 1   49.89 ? 718 HOH   A O   1 
HETATM 6272 O  O   . HOH   G 4 .   ? 4.932   -28.98  -14.874 1   45.26 ? 719 HOH   A O   1 
HETATM 6273 O  O   . HOH   G 4 .   ? 24.443  -44.091 -25.418 1   37.65 ? 720 HOH   A O   1 
HETATM 6274 O  O   . HOH   G 4 .   ? 30.38   -44.541 -22.363 1   44.16 ? 721 HOH   A O   1 
HETATM 6275 O  O   . HOH   G 4 .   ? 14.037  -27.441 -0.443  1   66.97 ? 722 HOH   A O   1 
HETATM 6276 O  O   . HOH   G 4 .   ? 20.206  -46.184 -36.556 1   63.65 ? 723 HOH   A O   1 
HETATM 6277 O  O   . HOH   G 4 .   ? 35.974  -46.408 -17.038 1   60.55 ? 724 HOH   A O   1 
HETATM 6278 O  O   . HOH   G 4 .   ? 8.435   -43.614 -17.065 1   39.16 ? 725 HOH   A O   1 
HETATM 6279 O  O   . HOH   H 4 .   ? 12.645  -7.443  -14.976 1   43.72 ? 601 HOH   B O   1 
HETATM 6280 O  O   . HOH   H 4 .   ? -3.606  -5.684  -2.487  1   80.32 ? 602 HOH   B O   1 
HETATM 6281 O  O   . HOH   H 4 .   ? 50.978  -8.934  -23.45  1   46.4  ? 603 HOH   B O   1 
HETATM 6282 O  O   . HOH   H 4 .   ? 13.542  8.182   -7.731  1   48.97 ? 604 HOH   B O   1 
HETATM 6283 O  O   . HOH   H 4 .   ? 34.413  4.319   -11.836 1   51.29 ? 605 HOH   B O   1 
HETATM 6284 O  O   . HOH   H 4 .   ? 39.024  -13.839 -33.509 1   65.99 ? 606 HOH   B O   1 
HETATM 6285 O  O   . HOH   H 4 .   ? 40.941  -4.22   -8.799  1   43.18 ? 607 HOH   B O   1 
HETATM 6286 O  O   . HOH   H 4 .   ? 13.929  -10.212 -15.601 1   42.23 ? 608 HOH   B O   1 
HETATM 6287 O  O   . HOH   H 4 .   ? 37.941  -5.52   -19.963 1   35.04 ? 609 HOH   B O   1 
HETATM 6288 O  O   . HOH   H 4 .   ? 16.362  -3.9    -15.906 1   36.19 ? 610 HOH   B O   1 
HETATM 6289 O  O   . HOH   H 4 .   ? 28.059  -11.382 -28.821 1   53.1  ? 611 HOH   B O   1 
HETATM 6290 O  O   . HOH   H 4 .   ? 20.75   -7.586  -27.514 1   41.04 ? 612 HOH   B O   1 
HETATM 6291 O  O   . HOH   H 4 .   ? 8.108   5.944   -21.703 1   38.46 ? 613 HOH   B O   1 
HETATM 6292 O  O   . HOH   H 4 .   ? 4.712   -7.473  10.781  1   40.06 ? 614 HOH   B O   1 
HETATM 6293 O  O   . HOH   H 4 .   ? 10.481  -10.925 -10.563 1   56.4  ? 615 HOH   B O   1 
HETATM 6294 O  O   . HOH   H 4 .   ? 46.332  6.983   -31.869 1   54.59 ? 616 HOH   B O   1 
HETATM 6295 O  O   . HOH   H 4 .   ? 33.648  4.188   -32.099 1   35.26 ? 617 HOH   B O   1 
HETATM 6296 O  O   . HOH   H 4 .   ? 37.237  -5.224  -13.929 1   36.96 ? 618 HOH   B O   1 
HETATM 6297 O  O   . HOH   H 4 .   ? 9.217   5.907   1.494   1   44.52 ? 619 HOH   B O   1 
HETATM 6298 O  O   . HOH   H 4 .   ? 29.387  -5.475  -16.35  1   32.08 ? 620 HOH   B O   1 
HETATM 6299 O  O   . HOH   H 4 .   ? 33.408  -0.669  0.884   1   46.69 ? 621 HOH   B O   1 
HETATM 6300 O  O   . HOH   H 4 .   ? 27.24   -10.636 -0.98   1   41.65 ? 622 HOH   B O   1 
HETATM 6301 O  O   . HOH   H 4 .   ? 20.825  -2.105  -15.555 1   28.46 ? 623 HOH   B O   1 
HETATM 6302 O  O   . HOH   H 4 .   ? 25.868  -2.601  -25.244 1   45.98 ? 624 HOH   B O   1 
HETATM 6303 O  O   . HOH   H 4 .   ? 19.426  13.788  -32.783 1   46.34 ? 625 HOH   B O   1 
HETATM 6304 O  O   . HOH   H 4 .   ? 10.93   -10.883 -17.079 1   52.34 ? 626 HOH   B O   1 
HETATM 6305 O  O   . HOH   H 4 .   ? 18.124  -1.93   -16.401 1   32.34 ? 627 HOH   B O   1 
HETATM 6306 O  O   . HOH   H 4 .   ? 20.722  -13.859 -23.677 1   46.27 ? 628 HOH   B O   1 
HETATM 6307 O  O   . HOH   H 4 .   ? 13.531  14.171  -22.877 1   34.68 ? 629 HOH   B O   1 
HETATM 6308 O  O   . HOH   H 4 .   ? -2.081  -7.524  3.935   1   42.44 ? 630 HOH   B O   1 
HETATM 6309 O  O   . HOH   H 4 .   ? 33.072  12.522  -32.964 1   51.79 ? 631 HOH   B O   1 
HETATM 6310 O  O   . HOH   H 4 .   ? 15.697  6.543   -19.095 1   27.7  ? 632 HOH   B O   1 
HETATM 6311 O  O   . HOH   H 4 .   ? 28.125  -2.143  -31.646 1   48.11 ? 633 HOH   B O   1 
HETATM 6312 O  O   . HOH   H 4 .   ? 0.431   -10.967 5.773   1   56.54 ? 634 HOH   B O   1 
HETATM 6313 O  O   . HOH   H 4 .   ? 9.337   -7.107  -24.787 1   44.2  ? 635 HOH   B O   1 
HETATM 6314 O  O   . HOH   H 4 .   ? 27.524  -5.925  -11.504 1   32.89 ? 636 HOH   B O   1 
HETATM 6315 O  O   . HOH   H 4 .   ? 27.9    -5.391  -14.104 1   32.31 ? 637 HOH   B O   1 
HETATM 6316 O  O   . HOH   H 4 .   ? 37.503  5.86    -34.588 1   43.57 ? 638 HOH   B O   1 
HETATM 6317 O  O   . HOH   H 4 .   ? -9.833  -4.752  1.272   1   47.39 ? 639 HOH   B O   1 
HETATM 6318 O  O   . HOH   H 4 .   ? -1.153  -2.375  10.843  1   38.6  ? 640 HOH   B O   1 
HETATM 6319 O  O   . HOH   H 4 .   ? 11.157  -12.18  -7.289  1   40.86 ? 641 HOH   B O   1 
HETATM 6320 O  O   . HOH   H 4 .   ? 10.798  -3.67   7.645   1   42.11 ? 642 HOH   B O   1 
HETATM 6321 O  O   . HOH   H 4 .   ? 26.241  -3.389  -11.3   1   29.87 ? 643 HOH   B O   1 
HETATM 6322 O  O   . HOH   H 4 .   ? 11.618  -11.324 -24.129 1   54.46 ? 644 HOH   B O   1 
HETATM 6323 O  O   . HOH   H 4 .   ? 25.397  -1.328  -6.623  1   40.75 ? 645 HOH   B O   1 
HETATM 6324 O  O   . HOH   H 4 .   ? 37.571  -2.973  -24.909 1   45.61 ? 646 HOH   B O   1 
HETATM 6325 O  O   . HOH   H 4 .   ? 25.135  2.936   -27.216 1   50.16 ? 647 HOH   B O   1 
HETATM 6326 O  O   . HOH   H 4 .   ? 14.684  4.039   -19.068 1   34.23 ? 648 HOH   B O   1 
HETATM 6327 O  O   . HOH   H 4 .   ? 30.548  -4.686  -22.845 1   32.66 ? 649 HOH   B O   1 
HETATM 6328 O  O   . HOH   H 4 .   ? 34.613  -6.638  -38.876 1   65.3  ? 650 HOH   B O   1 
HETATM 6329 O  O   . HOH   H 4 .   ? 34.709  15.029  -16.064 1   47.88 ? 651 HOH   B O   1 
HETATM 6330 O  O   . HOH   H 4 .   ? 48.31   5.114   -32.33  1   43.56 ? 652 HOH   B O   1 
HETATM 6331 O  O   . HOH   H 4 .   ? -0.417  0.772   8.358   1   49.17 ? 653 HOH   B O   1 
HETATM 6332 O  O   . HOH   H 4 .   ? 26.666  -17.335 -13.971 1   51.93 ? 654 HOH   B O   1 
HETATM 6333 O  O   . HOH   H 4 .   ? 44.24   13.17   -25.437 1   43.28 ? 655 HOH   B O   1 
HETATM 6334 O  O   . HOH   H 4 .   ? 40.793  -2.074  -10.43  1   45.41 ? 656 HOH   B O   1 
HETATM 6335 O  O   . HOH   H 4 .   ? 10.426  2.556   6.302   1   48.37 ? 657 HOH   B O   1 
HETATM 6336 O  O   . HOH   H 4 .   ? 37.53   15.715  -18.648 1   48.7  ? 658 HOH   B O   1 
HETATM 6337 O  O   . HOH   H 4 .   ? 15.718  -6.97   -14.78  1   47.7  ? 659 HOH   B O   1 
HETATM 6338 O  O   . HOH   H 4 .   ? 10.952  -5.131  -24.998 1   43.59 ? 660 HOH   B O   1 
HETATM 6339 O  O   . HOH   H 4 .   ? 43.574  -4.165  -38.732 1   57.42 ? 661 HOH   B O   1 
HETATM 6340 O  O   . HOH   H 4 .   ? 10.593  -9.09   -13     1   47.87 ? 662 HOH   B O   1 
HETATM 6341 O  O   . HOH   H 4 .   ? 31.949  -12.763 -9.675  1   41.55 ? 663 HOH   B O   1 
HETATM 6342 O  O   . HOH   H 4 .   ? 11.089  -3.037  -27.242 1   51.99 ? 664 HOH   B O   1 
HETATM 6343 O  O   . HOH   H 4 .   ? 31.732  3.293   -33.51  1   50.96 ? 665 HOH   B O   1 
HETATM 6344 O  O   . HOH   H 4 .   ? 9.005   9.192   -6.745  1   46.07 ? 666 HOH   B O   1 
HETATM 6345 O  O   . HOH   H 4 .   ? 9.723   -10.906 8.822   1   41.62 ? 667 HOH   B O   1 
HETATM 6346 O  O   . HOH   H 4 .   ? 48.043  5.542   -35.166 1   43.97 ? 668 HOH   B O   1 
HETATM 6347 O  O   . HOH   H 4 .   ? 11.658  10.317  -6.976  1   47.43 ? 669 HOH   B O   1 
HETATM 6348 O  O   . HOH   H 4 .   ? 23.379  -6.874  -27.905 1   47.65 ? 670 HOH   B O   1 
HETATM 6349 O  O   . HOH   H 4 .   ? 58.086  -1.234  -32.156 1   62.27 ? 671 HOH   B O   1 
HETATM 6350 O  O   . HOH   H 4 .   ? -4.081  6.207   -7.887  1   73.95 ? 672 HOH   B O   1 
# 
