data_9ESF
# 
_entry.id   9ESF 
# 
_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   9ESF         pdb_00009esf 10.2210/pdb9esf/pdb 
WWPDB D_1292136169 ?            ?                   
# 
_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                        9ESF 
_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 'Tryptophan 2,3-dioxygenase'                            43304.668 4 1.13.11.11 ? ? ? 
2 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE'                       616.487   4 ?          ? ? ? 
3 non-polymer syn '(~{S})-cyclohexyl(imidazo[1,5-a]pyridin-5-yl)methanol' 230.306   4 ?          ? ? ? 
4 water       nat water                                                   18.015    6 ?          ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'TDO,Protein vermilion,Tryptamin 2,3-dioxygenase,Tryptophan oxygenase,TO,TRPO,Tryptophan pyrrolase,Tryptophanase' 
# 
_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       
;MGKIYGEYLMLDKLLDAQCMLSEEDKRPVHDEHLFIITHQAYELWFKQIIFEFDSIRDMLDAEVIDETKTLEIVKRLNRV
VLILKLLVDQVPILETMTPLDFMDFRKYLAPASGFQSLQFRLIENKLGVLTEQRVRYNQKYSDVFSDEEARNSIRNSEKD
PSLLELVQRWLERTPGLEESGFNFWAKFQESVDRFLEAQVQSAMEEPVEKAKNYRLMDIEKRREVYRSIFDPAVHDALVR
RGDRRFSHRALQGAIMITFYRDEPRFSQPHQLLTLLMDIDSLITKWRYNHVIMVQRMIGSQQLGTGGSSGYQYLRSTLSD
RYKVFLDLFNLSTFLIPREAIPPLDETIRKKLINKSVLEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGKIYGEYLMLDKLLDAQCMLSEEDKRPVHDEHLFIITHQAYELWFKQIIFEFDSIRDMLDAEVIDETKTLEIVKRLNRV
VLILKLLVDQVPILETMTPLDFMDFRKYLAPASGFQSLQFRLIENKLGVLTEQRVRYNQKYSDVFSDEEARNSIRNSEKD
PSLLELVQRWLERTPGLEESGFNFWAKFQESVDRFLEAQVQSAMEEPVEKAKNYRLMDIEKRREVYRSIFDPAVHDALVR
RGDRRFSHRALQGAIMITFYRDEPRFSQPHQLLTLLMDIDSLITKWRYNHVIMVQRMIGSQQLGTGGSSGYQYLRSTLSD
RYKVFLDLFNLSTFLIPREAIPPLDETIRKKLINKSVLEHHHHHH
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'PROTOPORPHYRIN IX CONTAINING FE'                       HEM   
3 '(~{S})-cyclohexyl(imidazo[1,5-a]pyridin-5-yl)methanol' A1H6U 
4 water                                                   HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   LYS n 
1 4   ILE n 
1 5   TYR n 
1 6   GLY n 
1 7   GLU n 
1 8   TYR n 
1 9   LEU n 
1 10  MET n 
1 11  LEU n 
1 12  ASP n 
1 13  LYS n 
1 14  LEU n 
1 15  LEU n 
1 16  ASP n 
1 17  ALA n 
1 18  GLN n 
1 19  CYS n 
1 20  MET n 
1 21  LEU n 
1 22  SER n 
1 23  GLU n 
1 24  GLU n 
1 25  ASP n 
1 26  LYS n 
1 27  ARG n 
1 28  PRO n 
1 29  VAL n 
1 30  HIS n 
1 31  ASP n 
1 32  GLU n 
1 33  HIS n 
1 34  LEU n 
1 35  PHE n 
1 36  ILE n 
1 37  ILE n 
1 38  THR n 
1 39  HIS n 
1 40  GLN n 
1 41  ALA n 
1 42  TYR n 
1 43  GLU n 
1 44  LEU n 
1 45  TRP n 
1 46  PHE n 
1 47  LYS n 
1 48  GLN n 
1 49  ILE n 
1 50  ILE n 
1 51  PHE n 
1 52  GLU n 
1 53  PHE n 
1 54  ASP n 
1 55  SER n 
1 56  ILE n 
1 57  ARG n 
1 58  ASP n 
1 59  MET n 
1 60  LEU n 
1 61  ASP n 
1 62  ALA n 
1 63  GLU n 
1 64  VAL n 
1 65  ILE n 
1 66  ASP n 
1 67  GLU n 
1 68  THR n 
1 69  LYS n 
1 70  THR n 
1 71  LEU n 
1 72  GLU n 
1 73  ILE n 
1 74  VAL n 
1 75  LYS n 
1 76  ARG n 
1 77  LEU n 
1 78  ASN n 
1 79  ARG n 
1 80  VAL n 
1 81  VAL n 
1 82  LEU n 
1 83  ILE n 
1 84  LEU n 
1 85  LYS n 
1 86  LEU n 
1 87  LEU n 
1 88  VAL n 
1 89  ASP n 
1 90  GLN n 
1 91  VAL n 
1 92  PRO n 
1 93  ILE n 
1 94  LEU n 
1 95  GLU n 
1 96  THR n 
1 97  MET n 
1 98  THR n 
1 99  PRO n 
1 100 LEU n 
1 101 ASP n 
1 102 PHE n 
1 103 MET n 
1 104 ASP n 
1 105 PHE n 
1 106 ARG n 
1 107 LYS n 
1 108 TYR n 
1 109 LEU n 
1 110 ALA n 
1 111 PRO n 
1 112 ALA n 
1 113 SER n 
1 114 GLY n 
1 115 PHE n 
1 116 GLN n 
1 117 SER n 
1 118 LEU n 
1 119 GLN n 
1 120 PHE n 
1 121 ARG n 
1 122 LEU n 
1 123 ILE n 
1 124 GLU n 
1 125 ASN n 
1 126 LYS n 
1 127 LEU n 
1 128 GLY n 
1 129 VAL n 
1 130 LEU n 
1 131 THR n 
1 132 GLU n 
1 133 GLN n 
1 134 ARG n 
1 135 VAL n 
1 136 ARG n 
1 137 TYR n 
1 138 ASN n 
1 139 GLN n 
1 140 LYS n 
1 141 TYR n 
1 142 SER n 
1 143 ASP n 
1 144 VAL n 
1 145 PHE n 
1 146 SER n 
1 147 ASP n 
1 148 GLU n 
1 149 GLU n 
1 150 ALA n 
1 151 ARG n 
1 152 ASN n 
1 153 SER n 
1 154 ILE n 
1 155 ARG n 
1 156 ASN n 
1 157 SER n 
1 158 GLU n 
1 159 LYS n 
1 160 ASP n 
1 161 PRO n 
1 162 SER n 
1 163 LEU n 
1 164 LEU n 
1 165 GLU n 
1 166 LEU n 
1 167 VAL n 
1 168 GLN n 
1 169 ARG n 
1 170 TRP n 
1 171 LEU n 
1 172 GLU n 
1 173 ARG n 
1 174 THR n 
1 175 PRO n 
1 176 GLY n 
1 177 LEU n 
1 178 GLU n 
1 179 GLU n 
1 180 SER n 
1 181 GLY n 
1 182 PHE n 
1 183 ASN n 
1 184 PHE n 
1 185 TRP n 
1 186 ALA n 
1 187 LYS n 
1 188 PHE n 
1 189 GLN n 
1 190 GLU n 
1 191 SER n 
1 192 VAL n 
1 193 ASP n 
1 194 ARG n 
1 195 PHE n 
1 196 LEU n 
1 197 GLU n 
1 198 ALA n 
1 199 GLN n 
1 200 VAL n 
1 201 GLN n 
1 202 SER n 
1 203 ALA n 
1 204 MET n 
1 205 GLU n 
1 206 GLU n 
1 207 PRO n 
1 208 VAL n 
1 209 GLU n 
1 210 LYS n 
1 211 ALA n 
1 212 LYS n 
1 213 ASN n 
1 214 TYR n 
1 215 ARG n 
1 216 LEU n 
1 217 MET n 
1 218 ASP n 
1 219 ILE n 
1 220 GLU n 
1 221 LYS n 
1 222 ARG n 
1 223 ARG n 
1 224 GLU n 
1 225 VAL n 
1 226 TYR n 
1 227 ARG n 
1 228 SER n 
1 229 ILE n 
1 230 PHE n 
1 231 ASP n 
1 232 PRO n 
1 233 ALA n 
1 234 VAL n 
1 235 HIS n 
1 236 ASP n 
1 237 ALA n 
1 238 LEU n 
1 239 VAL n 
1 240 ARG n 
1 241 ARG n 
1 242 GLY n 
1 243 ASP n 
1 244 ARG n 
1 245 ARG n 
1 246 PHE n 
1 247 SER n 
1 248 HIS n 
1 249 ARG n 
1 250 ALA n 
1 251 LEU n 
1 252 GLN n 
1 253 GLY n 
1 254 ALA n 
1 255 ILE n 
1 256 MET n 
1 257 ILE n 
1 258 THR n 
1 259 PHE n 
1 260 TYR n 
1 261 ARG n 
1 262 ASP n 
1 263 GLU n 
1 264 PRO n 
1 265 ARG n 
1 266 PHE n 
1 267 SER n 
1 268 GLN n 
1 269 PRO n 
1 270 HIS n 
1 271 GLN n 
1 272 LEU n 
1 273 LEU n 
1 274 THR n 
1 275 LEU n 
1 276 LEU n 
1 277 MET n 
1 278 ASP n 
1 279 ILE n 
1 280 ASP n 
1 281 SER n 
1 282 LEU n 
1 283 ILE n 
1 284 THR n 
1 285 LYS n 
1 286 TRP n 
1 287 ARG n 
1 288 TYR n 
1 289 ASN n 
1 290 HIS n 
1 291 VAL n 
1 292 ILE n 
1 293 MET n 
1 294 VAL n 
1 295 GLN n 
1 296 ARG n 
1 297 MET n 
1 298 ILE n 
1 299 GLY n 
1 300 SER n 
1 301 GLN n 
1 302 GLN n 
1 303 LEU n 
1 304 GLY n 
1 305 THR n 
1 306 GLY n 
1 307 GLY n 
1 308 SER n 
1 309 SER n 
1 310 GLY n 
1 311 TYR n 
1 312 GLN n 
1 313 TYR n 
1 314 LEU n 
1 315 ARG n 
1 316 SER n 
1 317 THR n 
1 318 LEU n 
1 319 SER n 
1 320 ASP n 
1 321 ARG n 
1 322 TYR n 
1 323 LYS n 
1 324 VAL n 
1 325 PHE n 
1 326 LEU n 
1 327 ASP n 
1 328 LEU n 
1 329 PHE n 
1 330 ASN n 
1 331 LEU n 
1 332 SER n 
1 333 THR n 
1 334 PHE n 
1 335 LEU n 
1 336 ILE n 
1 337 PRO n 
1 338 ARG n 
1 339 GLU n 
1 340 ALA n 
1 341 ILE n 
1 342 PRO n 
1 343 PRO n 
1 344 LEU n 
1 345 ASP n 
1 346 GLU n 
1 347 THR n 
1 348 ILE n 
1 349 ARG n 
1 350 LYS n 
1 351 LYS n 
1 352 LEU n 
1 353 ILE n 
1 354 ASN n 
1 355 LYS n 
1 356 SER n 
1 357 VAL n 
1 358 LEU n 
1 359 GLU n 
1 360 HIS n 
1 361 HIS n 
1 362 HIS n 
1 363 HIS n 
1 364 HIS n 
1 365 HIS 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                   365 
_entity_src_gen.gene_src_common_name               'fruit fly' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'v, CG5163' 
_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      'Drosophila melanogaster' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     7227 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1H6U non-polymer         . '(~{S})-cyclohexyl(imidazo[1,5-a]pyridin-5-yl)methanol' ?    'C14 H18 N2 O'     230.306 
ALA   'L-peptide linking' y ALANINE                                                 ?    'C3 H7 N O2'       89.093  
ARG   'L-peptide linking' y ARGININE                                                ?    'C6 H15 N4 O2 1'   175.209 
ASN   'L-peptide linking' y ASPARAGINE                                              ?    'C4 H8 N2 O3'      132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                         ?    'C4 H7 N O4'       133.103 
CYS   'L-peptide linking' y CYSTEINE                                                ?    'C3 H7 N O2 S'     121.158 
GLN   'L-peptide linking' y GLUTAMINE                                               ?    'C5 H10 N2 O3'     146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                         ?    'C5 H9 N O4'       147.129 
GLY   'peptide linking'   y GLYCINE                                                 ?    'C2 H5 N O2'       75.067  
HEM   non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE'                       HEME 'C34 H32 Fe N4 O4' 616.487 
HIS   'L-peptide linking' y HISTIDINE                                               ?    'C6 H10 N3 O2 1'   156.162 
HOH   non-polymer         . WATER                                                   ?    'H2 O'             18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                              ?    'C6 H13 N O2'      131.173 
LEU   'L-peptide linking' y LEUCINE                                                 ?    'C6 H13 N O2'      131.173 
LYS   'L-peptide linking' y LYSINE                                                  ?    'C6 H15 N2 O2 1'   147.195 
MET   'L-peptide linking' y METHIONINE                                              ?    'C5 H11 N O2 S'    149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                           ?    'C9 H11 N O2'      165.189 
PRO   'L-peptide linking' y PROLINE                                                 ?    'C5 H9 N O2'       115.130 
SER   'L-peptide linking' y SERINE                                                  ?    'C3 H7 N O3'       105.093 
THR   'L-peptide linking' y THREONINE                                               ?    'C4 H9 N O3'       119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                              ?    'C11 H12 N2 O2'    204.225 
TYR   'L-peptide linking' y TYROSINE                                                ?    'C9 H11 N O3'      181.189 
VAL   'L-peptide linking' y VALINE                                                  ?    'C5 H11 N O2'      117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   23  ?   ?   ?   A . n 
A 1 2   GLY 2   24  ?   ?   ?   A . n 
A 1 3   LYS 3   25  25  LYS LYS A . n 
A 1 4   ILE 4   26  26  ILE ILE A . n 
A 1 5   TYR 5   27  27  TYR TYR A . n 
A 1 6   GLY 6   28  28  GLY GLY A . n 
A 1 7   GLU 7   29  29  GLU GLU A . n 
A 1 8   TYR 8   30  30  TYR TYR A . n 
A 1 9   LEU 9   31  31  LEU LEU A . n 
A 1 10  MET 10  32  32  MET MET A . n 
A 1 11  LEU 11  33  33  LEU LEU A . n 
A 1 12  ASP 12  34  34  ASP ASP A . n 
A 1 13  LYS 13  35  35  LYS LYS A . n 
A 1 14  LEU 14  36  36  LEU LEU A . n 
A 1 15  LEU 15  37  37  LEU LEU A . n 
A 1 16  ASP 16  38  38  ASP ASP A . n 
A 1 17  ALA 17  39  39  ALA ALA A . n 
A 1 18  GLN 18  40  40  GLN GLN A . n 
A 1 19  CYS 19  41  41  CYS CYS A . n 
A 1 20  MET 20  42  42  MET MET A . n 
A 1 21  LEU 21  43  43  LEU LEU A . n 
A 1 22  SER 22  44  44  SER SER A . n 
A 1 23  GLU 23  45  45  GLU GLU A . n 
A 1 24  GLU 24  46  46  GLU GLU A . n 
A 1 25  ASP 25  47  47  ASP ASP A . n 
A 1 26  LYS 26  48  48  LYS LYS A . n 
A 1 27  ARG 27  49  49  ARG ARG A . n 
A 1 28  PRO 28  50  50  PRO PRO A . n 
A 1 29  VAL 29  51  51  VAL VAL A . n 
A 1 30  HIS 30  52  52  HIS HIS A . n 
A 1 31  ASP 31  53  53  ASP ASP A . n 
A 1 32  GLU 32  54  54  GLU GLU A . n 
A 1 33  HIS 33  55  55  HIS HIS A . n 
A 1 34  LEU 34  56  56  LEU LEU A . n 
A 1 35  PHE 35  57  57  PHE PHE A . n 
A 1 36  ILE 36  58  58  ILE ILE A . n 
A 1 37  ILE 37  59  59  ILE ILE A . n 
A 1 38  THR 38  60  60  THR THR A . n 
A 1 39  HIS 39  61  61  HIS HIS A . n 
A 1 40  GLN 40  62  62  GLN GLN A . n 
A 1 41  ALA 41  63  63  ALA ALA A . n 
A 1 42  TYR 42  64  64  TYR TYR A . n 
A 1 43  GLU 43  65  65  GLU GLU A . n 
A 1 44  LEU 44  66  66  LEU LEU A . n 
A 1 45  TRP 45  67  67  TRP TRP A . n 
A 1 46  PHE 46  68  68  PHE PHE A . n 
A 1 47  LYS 47  69  69  LYS LYS A . n 
A 1 48  GLN 48  70  70  GLN GLN A . n 
A 1 49  ILE 49  71  71  ILE ILE A . n 
A 1 50  ILE 50  72  72  ILE ILE A . n 
A 1 51  PHE 51  73  73  PHE PHE A . n 
A 1 52  GLU 52  74  74  GLU GLU A . n 
A 1 53  PHE 53  75  75  PHE PHE A . n 
A 1 54  ASP 54  76  76  ASP ASP A . n 
A 1 55  SER 55  77  77  SER SER A . n 
A 1 56  ILE 56  78  78  ILE ILE A . n 
A 1 57  ARG 57  79  79  ARG ARG A . n 
A 1 58  ASP 58  80  80  ASP ASP A . n 
A 1 59  MET 59  81  81  MET MET A . n 
A 1 60  LEU 60  82  82  LEU LEU A . n 
A 1 61  ASP 61  83  83  ASP ASP A . n 
A 1 62  ALA 62  84  84  ALA ALA A . n 
A 1 63  GLU 63  85  85  GLU GLU A . n 
A 1 64  VAL 64  86  86  VAL VAL A . n 
A 1 65  ILE 65  87  87  ILE ILE A . n 
A 1 66  ASP 66  88  88  ASP ASP A . n 
A 1 67  GLU 67  89  89  GLU GLU A . n 
A 1 68  THR 68  90  90  THR THR A . n 
A 1 69  LYS 69  91  91  LYS LYS A . n 
A 1 70  THR 70  92  92  THR THR A . n 
A 1 71  LEU 71  93  93  LEU LEU A . n 
A 1 72  GLU 72  94  94  GLU GLU A . n 
A 1 73  ILE 73  95  95  ILE ILE A . n 
A 1 74  VAL 74  96  96  VAL VAL A . n 
A 1 75  LYS 75  97  97  LYS LYS A . n 
A 1 76  ARG 76  98  98  ARG ARG A . n 
A 1 77  LEU 77  99  99  LEU LEU A . n 
A 1 78  ASN 78  100 100 ASN ASN A . n 
A 1 79  ARG 79  101 101 ARG ARG A . n 
A 1 80  VAL 80  102 102 VAL VAL A . n 
A 1 81  VAL 81  103 103 VAL VAL A . n 
A 1 82  LEU 82  104 104 LEU LEU A . n 
A 1 83  ILE 83  105 105 ILE ILE A . n 
A 1 84  LEU 84  106 106 LEU LEU A . n 
A 1 85  LYS 85  107 107 LYS LYS A . n 
A 1 86  LEU 86  108 108 LEU LEU A . n 
A 1 87  LEU 87  109 109 LEU LEU A . n 
A 1 88  VAL 88  110 110 VAL VAL A . n 
A 1 89  ASP 89  111 111 ASP ASP A . n 
A 1 90  GLN 90  112 112 GLN GLN A . n 
A 1 91  VAL 91  113 113 VAL VAL A . n 
A 1 92  PRO 92  114 114 PRO PRO A . n 
A 1 93  ILE 93  115 115 ILE ILE A . n 
A 1 94  LEU 94  116 116 LEU LEU A . n 
A 1 95  GLU 95  117 117 GLU GLU A . n 
A 1 96  THR 96  118 118 THR THR A . n 
A 1 97  MET 97  119 119 MET MET A . n 
A 1 98  THR 98  120 120 THR THR A . n 
A 1 99  PRO 99  121 121 PRO PRO A . n 
A 1 100 LEU 100 122 122 LEU LEU A . n 
A 1 101 ASP 101 123 123 ASP ASP A . n 
A 1 102 PHE 102 124 124 PHE PHE A . n 
A 1 103 MET 103 125 125 MET MET A . n 
A 1 104 ASP 104 126 126 ASP ASP A . n 
A 1 105 PHE 105 127 127 PHE PHE A . n 
A 1 106 ARG 106 128 128 ARG ARG A . n 
A 1 107 LYS 107 129 129 LYS LYS A . n 
A 1 108 TYR 108 130 130 TYR TYR A . n 
A 1 109 LEU 109 131 131 LEU LEU A . n 
A 1 110 ALA 110 132 ?   ?   ?   A . n 
A 1 111 PRO 111 133 ?   ?   ?   A . n 
A 1 112 ALA 112 134 ?   ?   ?   A . n 
A 1 113 SER 113 135 ?   ?   ?   A . n 
A 1 114 GLY 114 136 ?   ?   ?   A . n 
A 1 115 PHE 115 137 ?   ?   ?   A . n 
A 1 116 GLN 116 138 138 GLN GLN A . n 
A 1 117 SER 117 139 139 SER SER A . n 
A 1 118 LEU 118 140 140 LEU LEU A . n 
A 1 119 GLN 119 141 141 GLN GLN A . n 
A 1 120 PHE 120 142 142 PHE PHE A . n 
A 1 121 ARG 121 143 143 ARG ARG A . n 
A 1 122 LEU 122 144 144 LEU LEU A . n 
A 1 123 ILE 123 145 145 ILE ILE A . n 
A 1 124 GLU 124 146 146 GLU GLU A . n 
A 1 125 ASN 125 147 147 ASN ASN A . n 
A 1 126 LYS 126 148 148 LYS LYS A . n 
A 1 127 LEU 127 149 149 LEU LEU A . n 
A 1 128 GLY 128 150 150 GLY GLY A . n 
A 1 129 VAL 129 151 151 VAL VAL A . n 
A 1 130 LEU 130 152 152 LEU LEU A . n 
A 1 131 THR 131 153 153 THR THR A . n 
A 1 132 GLU 132 154 154 GLU GLU A . n 
A 1 133 GLN 133 155 155 GLN GLN A . n 
A 1 134 ARG 134 156 ?   ?   ?   A . n 
A 1 135 VAL 135 157 ?   ?   ?   A . n 
A 1 136 ARG 136 158 ?   ?   ?   A . n 
A 1 137 TYR 137 159 ?   ?   ?   A . n 
A 1 138 ASN 138 160 ?   ?   ?   A . n 
A 1 139 GLN 139 161 ?   ?   ?   A . n 
A 1 140 LYS 140 162 ?   ?   ?   A . n 
A 1 141 TYR 141 163 ?   ?   ?   A . n 
A 1 142 SER 142 164 ?   ?   ?   A . n 
A 1 143 ASP 143 165 ?   ?   ?   A . n 
A 1 144 VAL 144 166 ?   ?   ?   A . n 
A 1 145 PHE 145 167 ?   ?   ?   A . n 
A 1 146 SER 146 168 ?   ?   ?   A . n 
A 1 147 ASP 147 169 ?   ?   ?   A . n 
A 1 148 GLU 148 170 170 GLU GLU A . n 
A 1 149 GLU 149 171 171 GLU GLU A . n 
A 1 150 ALA 150 172 172 ALA ALA A . n 
A 1 151 ARG 151 173 173 ARG ARG A . n 
A 1 152 ASN 152 174 174 ASN ASN A . n 
A 1 153 SER 153 175 175 SER SER A . n 
A 1 154 ILE 154 176 176 ILE ILE A . n 
A 1 155 ARG 155 177 177 ARG ARG A . n 
A 1 156 ASN 156 178 178 ASN ASN A . n 
A 1 157 SER 157 179 179 SER SER A . n 
A 1 158 GLU 158 180 180 GLU GLU A . n 
A 1 159 LYS 159 181 181 LYS LYS A . n 
A 1 160 ASP 160 182 182 ASP ASP A . n 
A 1 161 PRO 161 183 183 PRO PRO A . n 
A 1 162 SER 162 184 184 SER SER A . n 
A 1 163 LEU 163 185 185 LEU LEU A . n 
A 1 164 LEU 164 186 186 LEU LEU A . n 
A 1 165 GLU 165 187 187 GLU GLU A . n 
A 1 166 LEU 166 188 188 LEU LEU A . n 
A 1 167 VAL 167 189 189 VAL VAL A . n 
A 1 168 GLN 168 190 190 GLN GLN A . n 
A 1 169 ARG 169 191 191 ARG ARG A . n 
A 1 170 TRP 170 192 192 TRP TRP A . n 
A 1 171 LEU 171 193 193 LEU LEU A . n 
A 1 172 GLU 172 194 194 GLU GLU A . n 
A 1 173 ARG 173 195 195 ARG ARG A . n 
A 1 174 THR 174 196 196 THR THR A . n 
A 1 175 PRO 175 197 197 PRO PRO A . n 
A 1 176 GLY 176 198 198 GLY GLY A . n 
A 1 177 LEU 177 199 199 LEU LEU A . n 
A 1 178 GLU 178 200 200 GLU GLU A . n 
A 1 179 GLU 179 201 201 GLU GLU A . n 
A 1 180 SER 180 202 202 SER SER A . n 
A 1 181 GLY 181 203 203 GLY GLY A . n 
A 1 182 PHE 182 204 204 PHE PHE A . n 
A 1 183 ASN 183 205 205 ASN ASN A . n 
A 1 184 PHE 184 206 206 PHE PHE A . n 
A 1 185 TRP 185 207 207 TRP TRP A . n 
A 1 186 ALA 186 208 208 ALA ALA A . n 
A 1 187 LYS 187 209 209 LYS LYS A . n 
A 1 188 PHE 188 210 210 PHE PHE A . n 
A 1 189 GLN 189 211 211 GLN GLN A . n 
A 1 190 GLU 190 212 212 GLU GLU A . n 
A 1 191 SER 191 213 213 SER SER A . n 
A 1 192 VAL 192 214 214 VAL VAL A . n 
A 1 193 ASP 193 215 215 ASP ASP A . n 
A 1 194 ARG 194 216 216 ARG ARG A . n 
A 1 195 PHE 195 217 217 PHE PHE A . n 
A 1 196 LEU 196 218 218 LEU LEU A . n 
A 1 197 GLU 197 219 219 GLU GLU A . n 
A 1 198 ALA 198 220 220 ALA ALA A . n 
A 1 199 GLN 199 221 221 GLN GLN A . n 
A 1 200 VAL 200 222 222 VAL VAL A . n 
A 1 201 GLN 201 223 223 GLN GLN A . n 
A 1 202 SER 202 224 224 SER SER A . n 
A 1 203 ALA 203 225 225 ALA ALA A . n 
A 1 204 MET 204 226 226 MET MET A . n 
A 1 205 GLU 205 227 227 GLU GLU A . n 
A 1 206 GLU 206 228 228 GLU GLU A . n 
A 1 207 PRO 207 229 229 PRO PRO A . n 
A 1 208 VAL 208 230 230 VAL VAL A . n 
A 1 209 GLU 209 231 231 GLU GLU A . n 
A 1 210 LYS 210 232 232 LYS LYS A . n 
A 1 211 ALA 211 233 233 ALA ALA A . n 
A 1 212 LYS 212 234 234 LYS LYS A . n 
A 1 213 ASN 213 235 235 ASN ASN A . n 
A 1 214 TYR 214 236 236 TYR TYR A . n 
A 1 215 ARG 215 237 237 ARG ARG A . n 
A 1 216 LEU 216 238 238 LEU LEU A . n 
A 1 217 MET 217 239 239 MET MET A . n 
A 1 218 ASP 218 240 240 ASP ASP A . n 
A 1 219 ILE 219 241 241 ILE ILE A . n 
A 1 220 GLU 220 242 242 GLU GLU A . n 
A 1 221 LYS 221 243 243 LYS LYS A . n 
A 1 222 ARG 222 244 244 ARG ARG A . n 
A 1 223 ARG 223 245 245 ARG ARG A . n 
A 1 224 GLU 224 246 246 GLU GLU A . n 
A 1 225 VAL 225 247 247 VAL VAL A . n 
A 1 226 TYR 226 248 248 TYR TYR A . n 
A 1 227 ARG 227 249 249 ARG ARG A . n 
A 1 228 SER 228 250 250 SER SER A . n 
A 1 229 ILE 229 251 251 ILE ILE A . n 
A 1 230 PHE 230 252 252 PHE PHE A . n 
A 1 231 ASP 231 253 253 ASP ASP A . n 
A 1 232 PRO 232 254 254 PRO PRO A . n 
A 1 233 ALA 233 255 255 ALA ALA A . n 
A 1 234 VAL 234 256 256 VAL VAL A . n 
A 1 235 HIS 235 257 257 HIS HIS A . n 
A 1 236 ASP 236 258 258 ASP ASP A . n 
A 1 237 ALA 237 259 259 ALA ALA A . n 
A 1 238 LEU 238 260 260 LEU LEU A . n 
A 1 239 VAL 239 261 261 VAL VAL A . n 
A 1 240 ARG 240 262 262 ARG ARG A . n 
A 1 241 ARG 241 263 263 ARG ARG A . n 
A 1 242 GLY 242 264 264 GLY GLY A . n 
A 1 243 ASP 243 265 265 ASP ASP A . n 
A 1 244 ARG 244 266 266 ARG ARG A . n 
A 1 245 ARG 245 267 267 ARG ARG A . n 
A 1 246 PHE 246 268 268 PHE PHE A . n 
A 1 247 SER 247 269 269 SER SER A . n 
A 1 248 HIS 248 270 270 HIS HIS A . n 
A 1 249 ARG 249 271 271 ARG ARG A . n 
A 1 250 ALA 250 272 272 ALA ALA A . n 
A 1 251 LEU 251 273 273 LEU LEU A . n 
A 1 252 GLN 252 274 274 GLN GLN A . n 
A 1 253 GLY 253 275 275 GLY GLY A . n 
A 1 254 ALA 254 276 276 ALA ALA A . n 
A 1 255 ILE 255 277 277 ILE ILE A . n 
A 1 256 MET 256 278 278 MET MET A . n 
A 1 257 ILE 257 279 279 ILE ILE A . n 
A 1 258 THR 258 280 280 THR THR A . n 
A 1 259 PHE 259 281 281 PHE PHE A . n 
A 1 260 TYR 260 282 282 TYR TYR A . n 
A 1 261 ARG 261 283 283 ARG ARG A . n 
A 1 262 ASP 262 284 284 ASP ASP A . n 
A 1 263 GLU 263 285 285 GLU GLU A . n 
A 1 264 PRO 264 286 286 PRO PRO A . n 
A 1 265 ARG 265 287 287 ARG ARG A . n 
A 1 266 PHE 266 288 288 PHE PHE A . n 
A 1 267 SER 267 289 289 SER SER A . n 
A 1 268 GLN 268 290 290 GLN GLN A . n 
A 1 269 PRO 269 291 291 PRO PRO A . n 
A 1 270 HIS 270 292 292 HIS HIS A . n 
A 1 271 GLN 271 293 293 GLN GLN A . n 
A 1 272 LEU 272 294 294 LEU LEU A . n 
A 1 273 LEU 273 295 295 LEU LEU A . n 
A 1 274 THR 274 296 296 THR THR A . n 
A 1 275 LEU 275 297 297 LEU LEU A . n 
A 1 276 LEU 276 298 298 LEU LEU A . n 
A 1 277 MET 277 299 299 MET MET A . n 
A 1 278 ASP 278 300 300 ASP ASP A . n 
A 1 279 ILE 279 301 301 ILE ILE A . n 
A 1 280 ASP 280 302 302 ASP ASP A . n 
A 1 281 SER 281 303 303 SER SER A . n 
A 1 282 LEU 282 304 304 LEU LEU A . n 
A 1 283 ILE 283 305 305 ILE ILE A . n 
A 1 284 THR 284 306 306 THR THR A . n 
A 1 285 LYS 285 307 307 LYS LYS A . n 
A 1 286 TRP 286 308 308 TRP TRP A . n 
A 1 287 ARG 287 309 309 ARG ARG A . n 
A 1 288 TYR 288 310 310 TYR TYR A . n 
A 1 289 ASN 289 311 311 ASN ASN A . n 
A 1 290 HIS 290 312 312 HIS HIS A . n 
A 1 291 VAL 291 313 313 VAL VAL A . n 
A 1 292 ILE 292 314 314 ILE ILE A . n 
A 1 293 MET 293 315 315 MET MET A . n 
A 1 294 VAL 294 316 316 VAL VAL A . n 
A 1 295 GLN 295 317 317 GLN GLN A . n 
A 1 296 ARG 296 318 318 ARG ARG A . n 
A 1 297 MET 297 319 319 MET MET A . n 
A 1 298 ILE 298 320 320 ILE ILE A . n 
A 1 299 GLY 299 321 321 GLY GLY A . n 
A 1 300 SER 300 322 322 SER SER A . n 
A 1 301 GLN 301 323 323 GLN GLN A . n 
A 1 302 GLN 302 324 324 GLN GLN A . n 
A 1 303 LEU 303 325 325 LEU LEU A . n 
A 1 304 GLY 304 326 326 GLY GLY A . n 
A 1 305 THR 305 327 327 THR THR A . n 
A 1 306 GLY 306 328 328 GLY GLY A . n 
A 1 307 GLY 307 329 329 GLY GLY A . n 
A 1 308 SER 308 330 330 SER SER A . n 
A 1 309 SER 309 331 331 SER SER A . n 
A 1 310 GLY 310 332 332 GLY GLY A . n 
A 1 311 TYR 311 333 333 TYR TYR A . n 
A 1 312 GLN 312 334 334 GLN GLN A . n 
A 1 313 TYR 313 335 335 TYR TYR A . n 
A 1 314 LEU 314 336 336 LEU LEU A . n 
A 1 315 ARG 315 337 337 ARG ARG A . n 
A 1 316 SER 316 338 338 SER SER A . n 
A 1 317 THR 317 339 339 THR THR A . n 
A 1 318 LEU 318 340 340 LEU LEU A . n 
A 1 319 SER 319 341 341 SER SER A . n 
A 1 320 ASP 320 342 342 ASP ASP A . n 
A 1 321 ARG 321 343 343 ARG ARG A . n 
A 1 322 TYR 322 344 344 TYR TYR A . n 
A 1 323 LYS 323 345 345 LYS LYS A . n 
A 1 324 VAL 324 346 346 VAL VAL A . n 
A 1 325 PHE 325 347 347 PHE PHE A . n 
A 1 326 LEU 326 348 348 LEU LEU A . n 
A 1 327 ASP 327 349 349 ASP ASP A . n 
A 1 328 LEU 328 350 350 LEU LEU A . n 
A 1 329 PHE 329 351 351 PHE PHE A . n 
A 1 330 ASN 330 352 352 ASN ASN A . n 
A 1 331 LEU 331 353 353 LEU LEU A . n 
A 1 332 SER 332 354 354 SER SER A . n 
A 1 333 THR 333 355 355 THR THR A . n 
A 1 334 PHE 334 356 356 PHE PHE A . n 
A 1 335 LEU 335 357 357 LEU LEU A . n 
A 1 336 ILE 336 358 358 ILE ILE A . n 
A 1 337 PRO 337 359 359 PRO PRO A . n 
A 1 338 ARG 338 360 360 ARG ARG A . n 
A 1 339 GLU 339 361 361 GLU GLU A . n 
A 1 340 ALA 340 362 362 ALA ALA A . n 
A 1 341 ILE 341 363 363 ILE ILE A . n 
A 1 342 PRO 342 364 364 PRO PRO A . n 
A 1 343 PRO 343 365 365 PRO PRO A . n 
A 1 344 LEU 344 366 366 LEU LEU A . n 
A 1 345 ASP 345 367 367 ASP ASP A . n 
A 1 346 GLU 346 368 368 GLU GLU A . n 
A 1 347 THR 347 369 ?   ?   ?   A . n 
A 1 348 ILE 348 370 ?   ?   ?   A . n 
A 1 349 ARG 349 371 ?   ?   ?   A . n 
A 1 350 LYS 350 372 ?   ?   ?   A . n 
A 1 351 LYS 351 373 ?   ?   ?   A . n 
A 1 352 LEU 352 374 ?   ?   ?   A . n 
A 1 353 ILE 353 375 ?   ?   ?   A . n 
A 1 354 ASN 354 376 ?   ?   ?   A . n 
A 1 355 LYS 355 377 ?   ?   ?   A . n 
A 1 356 SER 356 378 ?   ?   ?   A . n 
A 1 357 VAL 357 379 ?   ?   ?   A . n 
A 1 358 LEU 358 380 ?   ?   ?   A . n 
A 1 359 GLU 359 381 ?   ?   ?   A . n 
A 1 360 HIS 360 382 ?   ?   ?   A . n 
A 1 361 HIS 361 383 ?   ?   ?   A . n 
A 1 362 HIS 362 384 ?   ?   ?   A . n 
A 1 363 HIS 363 385 ?   ?   ?   A . n 
A 1 364 HIS 364 386 ?   ?   ?   A . n 
A 1 365 HIS 365 387 ?   ?   ?   A . n 
B 1 1   MET 1   23  ?   ?   ?   B . n 
B 1 2   GLY 2   24  ?   ?   ?   B . n 
B 1 3   LYS 3   25  25  LYS LYS B . n 
B 1 4   ILE 4   26  26  ILE ILE B . n 
B 1 5   TYR 5   27  27  TYR TYR B . n 
B 1 6   GLY 6   28  28  GLY GLY B . n 
B 1 7   GLU 7   29  29  GLU GLU B . n 
B 1 8   TYR 8   30  30  TYR TYR B . n 
B 1 9   LEU 9   31  31  LEU LEU B . n 
B 1 10  MET 10  32  32  MET MET B . n 
B 1 11  LEU 11  33  33  LEU LEU B . n 
B 1 12  ASP 12  34  34  ASP ASP B . n 
B 1 13  LYS 13  35  35  LYS LYS B . n 
B 1 14  LEU 14  36  36  LEU LEU B . n 
B 1 15  LEU 15  37  37  LEU LEU B . n 
B 1 16  ASP 16  38  38  ASP ASP B . n 
B 1 17  ALA 17  39  39  ALA ALA B . n 
B 1 18  GLN 18  40  40  GLN GLN B . n 
B 1 19  CYS 19  41  41  CYS CYS B . n 
B 1 20  MET 20  42  42  MET MET B . n 
B 1 21  LEU 21  43  43  LEU LEU B . n 
B 1 22  SER 22  44  44  SER SER B . n 
B 1 23  GLU 23  45  45  GLU GLU B . n 
B 1 24  GLU 24  46  46  GLU GLU B . n 
B 1 25  ASP 25  47  47  ASP ASP B . n 
B 1 26  LYS 26  48  48  LYS LYS B . n 
B 1 27  ARG 27  49  49  ARG ARG B . n 
B 1 28  PRO 28  50  50  PRO PRO B . n 
B 1 29  VAL 29  51  51  VAL VAL B . n 
B 1 30  HIS 30  52  52  HIS HIS B . n 
B 1 31  ASP 31  53  53  ASP ASP B . n 
B 1 32  GLU 32  54  54  GLU GLU B . n 
B 1 33  HIS 33  55  55  HIS HIS B . n 
B 1 34  LEU 34  56  56  LEU LEU B . n 
B 1 35  PHE 35  57  57  PHE PHE B . n 
B 1 36  ILE 36  58  58  ILE ILE B . n 
B 1 37  ILE 37  59  59  ILE ILE B . n 
B 1 38  THR 38  60  60  THR THR B . n 
B 1 39  HIS 39  61  61  HIS HIS B . n 
B 1 40  GLN 40  62  62  GLN GLN B . n 
B 1 41  ALA 41  63  63  ALA ALA B . n 
B 1 42  TYR 42  64  64  TYR TYR B . n 
B 1 43  GLU 43  65  65  GLU GLU B . n 
B 1 44  LEU 44  66  66  LEU LEU B . n 
B 1 45  TRP 45  67  67  TRP TRP B . n 
B 1 46  PHE 46  68  68  PHE PHE B . n 
B 1 47  LYS 47  69  69  LYS LYS B . n 
B 1 48  GLN 48  70  70  GLN GLN B . n 
B 1 49  ILE 49  71  71  ILE ILE B . n 
B 1 50  ILE 50  72  72  ILE ILE B . n 
B 1 51  PHE 51  73  73  PHE PHE B . n 
B 1 52  GLU 52  74  74  GLU GLU B . n 
B 1 53  PHE 53  75  75  PHE PHE B . n 
B 1 54  ASP 54  76  76  ASP ASP B . n 
B 1 55  SER 55  77  77  SER SER B . n 
B 1 56  ILE 56  78  78  ILE ILE B . n 
B 1 57  ARG 57  79  79  ARG ARG B . n 
B 1 58  ASP 58  80  80  ASP ASP B . n 
B 1 59  MET 59  81  81  MET MET B . n 
B 1 60  LEU 60  82  82  LEU LEU B . n 
B 1 61  ASP 61  83  83  ASP ASP B . n 
B 1 62  ALA 62  84  84  ALA ALA B . n 
B 1 63  GLU 63  85  85  GLU GLU B . n 
B 1 64  VAL 64  86  86  VAL VAL B . n 
B 1 65  ILE 65  87  87  ILE ILE B . n 
B 1 66  ASP 66  88  88  ASP ASP B . n 
B 1 67  GLU 67  89  89  GLU GLU B . n 
B 1 68  THR 68  90  90  THR THR B . n 
B 1 69  LYS 69  91  91  LYS LYS B . n 
B 1 70  THR 70  92  92  THR THR B . n 
B 1 71  LEU 71  93  93  LEU LEU B . n 
B 1 72  GLU 72  94  94  GLU GLU B . n 
B 1 73  ILE 73  95  95  ILE ILE B . n 
B 1 74  VAL 74  96  96  VAL VAL B . n 
B 1 75  LYS 75  97  97  LYS LYS B . n 
B 1 76  ARG 76  98  98  ARG ARG B . n 
B 1 77  LEU 77  99  99  LEU LEU B . n 
B 1 78  ASN 78  100 100 ASN ASN B . n 
B 1 79  ARG 79  101 101 ARG ARG B . n 
B 1 80  VAL 80  102 102 VAL VAL B . n 
B 1 81  VAL 81  103 103 VAL VAL B . n 
B 1 82  LEU 82  104 104 LEU LEU B . n 
B 1 83  ILE 83  105 105 ILE ILE B . n 
B 1 84  LEU 84  106 106 LEU LEU B . n 
B 1 85  LYS 85  107 107 LYS LYS B . n 
B 1 86  LEU 86  108 108 LEU LEU B . n 
B 1 87  LEU 87  109 109 LEU LEU B . n 
B 1 88  VAL 88  110 110 VAL VAL B . n 
B 1 89  ASP 89  111 111 ASP ASP B . n 
B 1 90  GLN 90  112 112 GLN GLN B . n 
B 1 91  VAL 91  113 113 VAL VAL B . n 
B 1 92  PRO 92  114 114 PRO PRO B . n 
B 1 93  ILE 93  115 115 ILE ILE B . n 
B 1 94  LEU 94  116 116 LEU LEU B . n 
B 1 95  GLU 95  117 117 GLU GLU B . n 
B 1 96  THR 96  118 118 THR THR B . n 
B 1 97  MET 97  119 119 MET MET B . n 
B 1 98  THR 98  120 120 THR THR B . n 
B 1 99  PRO 99  121 121 PRO PRO B . n 
B 1 100 LEU 100 122 122 LEU LEU B . n 
B 1 101 ASP 101 123 123 ASP ASP B . n 
B 1 102 PHE 102 124 124 PHE PHE B . n 
B 1 103 MET 103 125 125 MET MET B . n 
B 1 104 ASP 104 126 126 ASP ASP B . n 
B 1 105 PHE 105 127 127 PHE PHE B . n 
B 1 106 ARG 106 128 128 ARG ARG B . n 
B 1 107 LYS 107 129 129 LYS LYS B . n 
B 1 108 TYR 108 130 130 TYR TYR B . n 
B 1 109 LEU 109 131 131 LEU LEU B . n 
B 1 110 ALA 110 132 ?   ?   ?   B . n 
B 1 111 PRO 111 133 ?   ?   ?   B . n 
B 1 112 ALA 112 134 ?   ?   ?   B . n 
B 1 113 SER 113 135 ?   ?   ?   B . n 
B 1 114 GLY 114 136 ?   ?   ?   B . n 
B 1 115 PHE 115 137 ?   ?   ?   B . n 
B 1 116 GLN 116 138 138 GLN GLN B . n 
B 1 117 SER 117 139 139 SER SER B . n 
B 1 118 LEU 118 140 140 LEU LEU B . n 
B 1 119 GLN 119 141 141 GLN GLN B . n 
B 1 120 PHE 120 142 142 PHE PHE B . n 
B 1 121 ARG 121 143 143 ARG ARG B . n 
B 1 122 LEU 122 144 144 LEU LEU B . n 
B 1 123 ILE 123 145 145 ILE ILE B . n 
B 1 124 GLU 124 146 146 GLU GLU B . n 
B 1 125 ASN 125 147 147 ASN ASN B . n 
B 1 126 LYS 126 148 148 LYS LYS B . n 
B 1 127 LEU 127 149 149 LEU LEU B . n 
B 1 128 GLY 128 150 150 GLY GLY B . n 
B 1 129 VAL 129 151 151 VAL VAL B . n 
B 1 130 LEU 130 152 152 LEU LEU B . n 
B 1 131 THR 131 153 153 THR THR B . n 
B 1 132 GLU 132 154 154 GLU GLU B . n 
B 1 133 GLN 133 155 155 GLN GLN B . n 
B 1 134 ARG 134 156 ?   ?   ?   B . n 
B 1 135 VAL 135 157 ?   ?   ?   B . n 
B 1 136 ARG 136 158 ?   ?   ?   B . n 
B 1 137 TYR 137 159 ?   ?   ?   B . n 
B 1 138 ASN 138 160 ?   ?   ?   B . n 
B 1 139 GLN 139 161 ?   ?   ?   B . n 
B 1 140 LYS 140 162 ?   ?   ?   B . n 
B 1 141 TYR 141 163 ?   ?   ?   B . n 
B 1 142 SER 142 164 ?   ?   ?   B . n 
B 1 143 ASP 143 165 ?   ?   ?   B . n 
B 1 144 VAL 144 166 166 VAL ALA B . n 
B 1 145 PHE 145 167 167 PHE ALA B . n 
B 1 146 SER 146 168 168 SER ALA B . n 
B 1 147 ASP 147 169 169 ASP ALA B . n 
B 1 148 GLU 148 170 170 GLU GLU B . n 
B 1 149 GLU 149 171 171 GLU GLU B . n 
B 1 150 ALA 150 172 172 ALA ALA B . n 
B 1 151 ARG 151 173 173 ARG ARG B . n 
B 1 152 ASN 152 174 174 ASN ASN B . n 
B 1 153 SER 153 175 175 SER SER B . n 
B 1 154 ILE 154 176 176 ILE ILE B . n 
B 1 155 ARG 155 177 177 ARG ARG B . n 
B 1 156 ASN 156 178 178 ASN ASN B . n 
B 1 157 SER 157 179 179 SER SER B . n 
B 1 158 GLU 158 180 180 GLU GLU B . n 
B 1 159 LYS 159 181 181 LYS LYS B . n 
B 1 160 ASP 160 182 182 ASP ASP B . n 
B 1 161 PRO 161 183 183 PRO PRO B . n 
B 1 162 SER 162 184 184 SER SER B . n 
B 1 163 LEU 163 185 185 LEU LEU B . n 
B 1 164 LEU 164 186 186 LEU LEU B . n 
B 1 165 GLU 165 187 187 GLU GLU B . n 
B 1 166 LEU 166 188 188 LEU LEU B . n 
B 1 167 VAL 167 189 189 VAL VAL B . n 
B 1 168 GLN 168 190 190 GLN GLN B . n 
B 1 169 ARG 169 191 191 ARG ARG B . n 
B 1 170 TRP 170 192 192 TRP TRP B . n 
B 1 171 LEU 171 193 193 LEU LEU B . n 
B 1 172 GLU 172 194 194 GLU GLU B . n 
B 1 173 ARG 173 195 195 ARG ARG B . n 
B 1 174 THR 174 196 196 THR THR B . n 
B 1 175 PRO 175 197 197 PRO PRO B . n 
B 1 176 GLY 176 198 198 GLY GLY B . n 
B 1 177 LEU 177 199 199 LEU LEU B . n 
B 1 178 GLU 178 200 200 GLU GLU B . n 
B 1 179 GLU 179 201 201 GLU GLU B . n 
B 1 180 SER 180 202 202 SER SER B . n 
B 1 181 GLY 181 203 203 GLY GLY B . n 
B 1 182 PHE 182 204 204 PHE PHE B . n 
B 1 183 ASN 183 205 205 ASN ASN B . n 
B 1 184 PHE 184 206 206 PHE PHE B . n 
B 1 185 TRP 185 207 207 TRP TRP B . n 
B 1 186 ALA 186 208 208 ALA ALA B . n 
B 1 187 LYS 187 209 209 LYS LYS B . n 
B 1 188 PHE 188 210 210 PHE PHE B . n 
B 1 189 GLN 189 211 211 GLN GLN B . n 
B 1 190 GLU 190 212 212 GLU GLU B . n 
B 1 191 SER 191 213 213 SER SER B . n 
B 1 192 VAL 192 214 214 VAL VAL B . n 
B 1 193 ASP 193 215 215 ASP ASP B . n 
B 1 194 ARG 194 216 216 ARG ARG B . n 
B 1 195 PHE 195 217 217 PHE PHE B . n 
B 1 196 LEU 196 218 218 LEU LEU B . n 
B 1 197 GLU 197 219 219 GLU GLU B . n 
B 1 198 ALA 198 220 220 ALA ALA B . n 
B 1 199 GLN 199 221 221 GLN GLN B . n 
B 1 200 VAL 200 222 222 VAL VAL B . n 
B 1 201 GLN 201 223 223 GLN GLN B . n 
B 1 202 SER 202 224 224 SER SER B . n 
B 1 203 ALA 203 225 225 ALA ALA B . n 
B 1 204 MET 204 226 226 MET MET B . n 
B 1 205 GLU 205 227 227 GLU GLU B . n 
B 1 206 GLU 206 228 228 GLU GLU B . n 
B 1 207 PRO 207 229 229 PRO PRO B . n 
B 1 208 VAL 208 230 230 VAL VAL B . n 
B 1 209 GLU 209 231 231 GLU GLU B . n 
B 1 210 LYS 210 232 232 LYS LYS B . n 
B 1 211 ALA 211 233 233 ALA ALA B . n 
B 1 212 LYS 212 234 234 LYS LYS B . n 
B 1 213 ASN 213 235 235 ASN ASN B . n 
B 1 214 TYR 214 236 236 TYR TYR B . n 
B 1 215 ARG 215 237 237 ARG ARG B . n 
B 1 216 LEU 216 238 238 LEU LEU B . n 
B 1 217 MET 217 239 239 MET MET B . n 
B 1 218 ASP 218 240 240 ASP ASP B . n 
B 1 219 ILE 219 241 241 ILE ILE B . n 
B 1 220 GLU 220 242 242 GLU GLU B . n 
B 1 221 LYS 221 243 243 LYS LYS B . n 
B 1 222 ARG 222 244 244 ARG ARG B . n 
B 1 223 ARG 223 245 245 ARG ARG B . n 
B 1 224 GLU 224 246 246 GLU GLU B . n 
B 1 225 VAL 225 247 247 VAL VAL B . n 
B 1 226 TYR 226 248 248 TYR TYR B . n 
B 1 227 ARG 227 249 249 ARG ARG B . n 
B 1 228 SER 228 250 250 SER SER B . n 
B 1 229 ILE 229 251 251 ILE ILE B . n 
B 1 230 PHE 230 252 252 PHE PHE B . n 
B 1 231 ASP 231 253 253 ASP ASP B . n 
B 1 232 PRO 232 254 254 PRO PRO B . n 
B 1 233 ALA 233 255 255 ALA ALA B . n 
B 1 234 VAL 234 256 256 VAL VAL B . n 
B 1 235 HIS 235 257 257 HIS HIS B . n 
B 1 236 ASP 236 258 258 ASP ASP B . n 
B 1 237 ALA 237 259 259 ALA ALA B . n 
B 1 238 LEU 238 260 260 LEU LEU B . n 
B 1 239 VAL 239 261 261 VAL VAL B . n 
B 1 240 ARG 240 262 262 ARG ARG B . n 
B 1 241 ARG 241 263 263 ARG ARG B . n 
B 1 242 GLY 242 264 264 GLY GLY B . n 
B 1 243 ASP 243 265 265 ASP ASP B . n 
B 1 244 ARG 244 266 266 ARG ARG B . n 
B 1 245 ARG 245 267 267 ARG ARG B . n 
B 1 246 PHE 246 268 268 PHE PHE B . n 
B 1 247 SER 247 269 269 SER SER B . n 
B 1 248 HIS 248 270 270 HIS HIS B . n 
B 1 249 ARG 249 271 271 ARG ARG B . n 
B 1 250 ALA 250 272 272 ALA ALA B . n 
B 1 251 LEU 251 273 273 LEU LEU B . n 
B 1 252 GLN 252 274 274 GLN GLN B . n 
B 1 253 GLY 253 275 275 GLY GLY B . n 
B 1 254 ALA 254 276 276 ALA ALA B . n 
B 1 255 ILE 255 277 277 ILE ILE B . n 
B 1 256 MET 256 278 278 MET MET B . n 
B 1 257 ILE 257 279 279 ILE ILE B . n 
B 1 258 THR 258 280 280 THR THR B . n 
B 1 259 PHE 259 281 281 PHE PHE B . n 
B 1 260 TYR 260 282 282 TYR TYR B . n 
B 1 261 ARG 261 283 283 ARG ARG B . n 
B 1 262 ASP 262 284 284 ASP ASP B . n 
B 1 263 GLU 263 285 285 GLU GLU B . n 
B 1 264 PRO 264 286 286 PRO PRO B . n 
B 1 265 ARG 265 287 287 ARG ARG B . n 
B 1 266 PHE 266 288 288 PHE PHE B . n 
B 1 267 SER 267 289 289 SER SER B . n 
B 1 268 GLN 268 290 290 GLN GLN B . n 
B 1 269 PRO 269 291 291 PRO PRO B . n 
B 1 270 HIS 270 292 292 HIS HIS B . n 
B 1 271 GLN 271 293 293 GLN GLN B . n 
B 1 272 LEU 272 294 294 LEU LEU B . n 
B 1 273 LEU 273 295 295 LEU LEU B . n 
B 1 274 THR 274 296 296 THR THR B . n 
B 1 275 LEU 275 297 297 LEU LEU B . n 
B 1 276 LEU 276 298 298 LEU LEU B . n 
B 1 277 MET 277 299 299 MET MET B . n 
B 1 278 ASP 278 300 300 ASP ASP B . n 
B 1 279 ILE 279 301 301 ILE ILE B . n 
B 1 280 ASP 280 302 302 ASP ASP B . n 
B 1 281 SER 281 303 303 SER SER B . n 
B 1 282 LEU 282 304 304 LEU LEU B . n 
B 1 283 ILE 283 305 305 ILE ILE B . n 
B 1 284 THR 284 306 306 THR THR B . n 
B 1 285 LYS 285 307 307 LYS LYS B . n 
B 1 286 TRP 286 308 308 TRP TRP B . n 
B 1 287 ARG 287 309 309 ARG ARG B . n 
B 1 288 TYR 288 310 310 TYR TYR B . n 
B 1 289 ASN 289 311 311 ASN ASN B . n 
B 1 290 HIS 290 312 312 HIS HIS B . n 
B 1 291 VAL 291 313 313 VAL VAL B . n 
B 1 292 ILE 292 314 314 ILE ILE B . n 
B 1 293 MET 293 315 315 MET MET B . n 
B 1 294 VAL 294 316 316 VAL VAL B . n 
B 1 295 GLN 295 317 317 GLN GLN B . n 
B 1 296 ARG 296 318 318 ARG ARG B . n 
B 1 297 MET 297 319 319 MET MET B . n 
B 1 298 ILE 298 320 320 ILE ILE B . n 
B 1 299 GLY 299 321 321 GLY GLY B . n 
B 1 300 SER 300 322 322 SER SER B . n 
B 1 301 GLN 301 323 323 GLN GLN B . n 
B 1 302 GLN 302 324 324 GLN GLN B . n 
B 1 303 LEU 303 325 325 LEU LEU B . n 
B 1 304 GLY 304 326 326 GLY GLY B . n 
B 1 305 THR 305 327 327 THR THR B . n 
B 1 306 GLY 306 328 328 GLY GLY B . n 
B 1 307 GLY 307 329 329 GLY GLY B . n 
B 1 308 SER 308 330 330 SER SER B . n 
B 1 309 SER 309 331 331 SER SER B . n 
B 1 310 GLY 310 332 332 GLY GLY B . n 
B 1 311 TYR 311 333 333 TYR TYR B . n 
B 1 312 GLN 312 334 334 GLN GLN B . n 
B 1 313 TYR 313 335 335 TYR TYR B . n 
B 1 314 LEU 314 336 336 LEU LEU B . n 
B 1 315 ARG 315 337 337 ARG ARG B . n 
B 1 316 SER 316 338 338 SER SER B . n 
B 1 317 THR 317 339 339 THR THR B . n 
B 1 318 LEU 318 340 340 LEU LEU B . n 
B 1 319 SER 319 341 341 SER SER B . n 
B 1 320 ASP 320 342 342 ASP ASP B . n 
B 1 321 ARG 321 343 343 ARG ARG B . n 
B 1 322 TYR 322 344 344 TYR TYR B . n 
B 1 323 LYS 323 345 345 LYS LYS B . n 
B 1 324 VAL 324 346 346 VAL VAL B . n 
B 1 325 PHE 325 347 347 PHE PHE B . n 
B 1 326 LEU 326 348 348 LEU LEU B . n 
B 1 327 ASP 327 349 349 ASP ASP B . n 
B 1 328 LEU 328 350 350 LEU LEU B . n 
B 1 329 PHE 329 351 351 PHE PHE B . n 
B 1 330 ASN 330 352 352 ASN ASN B . n 
B 1 331 LEU 331 353 353 LEU LEU B . n 
B 1 332 SER 332 354 354 SER SER B . n 
B 1 333 THR 333 355 355 THR THR B . n 
B 1 334 PHE 334 356 356 PHE PHE B . n 
B 1 335 LEU 335 357 357 LEU LEU B . n 
B 1 336 ILE 336 358 358 ILE ILE B . n 
B 1 337 PRO 337 359 359 PRO PRO B . n 
B 1 338 ARG 338 360 360 ARG ARG B . n 
B 1 339 GLU 339 361 361 GLU GLU B . n 
B 1 340 ALA 340 362 362 ALA ALA B . n 
B 1 341 ILE 341 363 363 ILE ILE B . n 
B 1 342 PRO 342 364 364 PRO PRO B . n 
B 1 343 PRO 343 365 365 PRO PRO B . n 
B 1 344 LEU 344 366 366 LEU LEU B . n 
B 1 345 ASP 345 367 367 ASP ASP B . n 
B 1 346 GLU 346 368 368 GLU GLU B . n 
B 1 347 THR 347 369 ?   ?   ?   B . n 
B 1 348 ILE 348 370 ?   ?   ?   B . n 
B 1 349 ARG 349 371 ?   ?   ?   B . n 
B 1 350 LYS 350 372 ?   ?   ?   B . n 
B 1 351 LYS 351 373 ?   ?   ?   B . n 
B 1 352 LEU 352 374 ?   ?   ?   B . n 
B 1 353 ILE 353 375 ?   ?   ?   B . n 
B 1 354 ASN 354 376 ?   ?   ?   B . n 
B 1 355 LYS 355 377 ?   ?   ?   B . n 
B 1 356 SER 356 378 ?   ?   ?   B . n 
B 1 357 VAL 357 379 ?   ?   ?   B . n 
B 1 358 LEU 358 380 ?   ?   ?   B . n 
B 1 359 GLU 359 381 ?   ?   ?   B . n 
B 1 360 HIS 360 382 ?   ?   ?   B . n 
B 1 361 HIS 361 383 ?   ?   ?   B . n 
B 1 362 HIS 362 384 ?   ?   ?   B . n 
B 1 363 HIS 363 385 ?   ?   ?   B . n 
B 1 364 HIS 364 386 ?   ?   ?   B . n 
B 1 365 HIS 365 387 ?   ?   ?   B . n 
C 1 1   MET 1   23  ?   ?   ?   C . n 
C 1 2   GLY 2   24  ?   ?   ?   C . n 
C 1 3   LYS 3   25  ?   ?   ?   C . n 
C 1 4   ILE 4   26  26  ILE ILE C . n 
C 1 5   TYR 5   27  27  TYR TYR C . n 
C 1 6   GLY 6   28  28  GLY GLY C . n 
C 1 7   GLU 7   29  29  GLU GLU C . n 
C 1 8   TYR 8   30  30  TYR TYR C . n 
C 1 9   LEU 9   31  31  LEU LEU C . n 
C 1 10  MET 10  32  32  MET MET C . n 
C 1 11  LEU 11  33  33  LEU LEU C . n 
C 1 12  ASP 12  34  34  ASP ASP C . n 
C 1 13  LYS 13  35  35  LYS LYS C . n 
C 1 14  LEU 14  36  36  LEU LEU C . n 
C 1 15  LEU 15  37  37  LEU LEU C . n 
C 1 16  ASP 16  38  38  ASP ASP C . n 
C 1 17  ALA 17  39  39  ALA ALA C . n 
C 1 18  GLN 18  40  40  GLN GLN C . n 
C 1 19  CYS 19  41  41  CYS CYS C . n 
C 1 20  MET 20  42  42  MET MET C . n 
C 1 21  LEU 21  43  43  LEU LEU C . n 
C 1 22  SER 22  44  44  SER SER C . n 
C 1 23  GLU 23  45  45  GLU GLU C . n 
C 1 24  GLU 24  46  46  GLU GLU C . n 
C 1 25  ASP 25  47  47  ASP ASP C . n 
C 1 26  LYS 26  48  48  LYS LYS C . n 
C 1 27  ARG 27  49  49  ARG ARG C . n 
C 1 28  PRO 28  50  50  PRO PRO C . n 
C 1 29  VAL 29  51  51  VAL VAL C . n 
C 1 30  HIS 30  52  52  HIS HIS C . n 
C 1 31  ASP 31  53  53  ASP ASP C . n 
C 1 32  GLU 32  54  54  GLU GLU C . n 
C 1 33  HIS 33  55  55  HIS HIS C . n 
C 1 34  LEU 34  56  56  LEU LEU C . n 
C 1 35  PHE 35  57  57  PHE PHE C . n 
C 1 36  ILE 36  58  58  ILE ILE C . n 
C 1 37  ILE 37  59  59  ILE ILE C . n 
C 1 38  THR 38  60  60  THR THR C . n 
C 1 39  HIS 39  61  61  HIS HIS C . n 
C 1 40  GLN 40  62  62  GLN GLN C . n 
C 1 41  ALA 41  63  63  ALA ALA C . n 
C 1 42  TYR 42  64  64  TYR TYR C . n 
C 1 43  GLU 43  65  65  GLU GLU C . n 
C 1 44  LEU 44  66  66  LEU LEU C . n 
C 1 45  TRP 45  67  67  TRP TRP C . n 
C 1 46  PHE 46  68  68  PHE PHE C . n 
C 1 47  LYS 47  69  69  LYS LYS C . n 
C 1 48  GLN 48  70  70  GLN GLN C . n 
C 1 49  ILE 49  71  71  ILE ILE C . n 
C 1 50  ILE 50  72  72  ILE ILE C . n 
C 1 51  PHE 51  73  73  PHE PHE C . n 
C 1 52  GLU 52  74  74  GLU GLU C . n 
C 1 53  PHE 53  75  75  PHE PHE C . n 
C 1 54  ASP 54  76  76  ASP ASP C . n 
C 1 55  SER 55  77  77  SER SER C . n 
C 1 56  ILE 56  78  78  ILE ILE C . n 
C 1 57  ARG 57  79  79  ARG ARG C . n 
C 1 58  ASP 58  80  80  ASP ASP C . n 
C 1 59  MET 59  81  81  MET MET C . n 
C 1 60  LEU 60  82  82  LEU LEU C . n 
C 1 61  ASP 61  83  83  ASP ASP C . n 
C 1 62  ALA 62  84  84  ALA ALA C . n 
C 1 63  GLU 63  85  85  GLU GLU C . n 
C 1 64  VAL 64  86  86  VAL VAL C . n 
C 1 65  ILE 65  87  87  ILE ILE C . n 
C 1 66  ASP 66  88  88  ASP ASP C . n 
C 1 67  GLU 67  89  89  GLU GLU C . n 
C 1 68  THR 68  90  90  THR THR C . n 
C 1 69  LYS 69  91  91  LYS LYS C . n 
C 1 70  THR 70  92  92  THR THR C . n 
C 1 71  LEU 71  93  93  LEU LEU C . n 
C 1 72  GLU 72  94  94  GLU GLU C . n 
C 1 73  ILE 73  95  95  ILE ILE C . n 
C 1 74  VAL 74  96  96  VAL VAL C . n 
C 1 75  LYS 75  97  97  LYS LYS C . n 
C 1 76  ARG 76  98  98  ARG ARG C . n 
C 1 77  LEU 77  99  99  LEU LEU C . n 
C 1 78  ASN 78  100 100 ASN ASN C . n 
C 1 79  ARG 79  101 101 ARG ARG C . n 
C 1 80  VAL 80  102 102 VAL VAL C . n 
C 1 81  VAL 81  103 103 VAL VAL C . n 
C 1 82  LEU 82  104 104 LEU LEU C . n 
C 1 83  ILE 83  105 105 ILE ILE C . n 
C 1 84  LEU 84  106 106 LEU LEU C . n 
C 1 85  LYS 85  107 107 LYS LYS C . n 
C 1 86  LEU 86  108 108 LEU LEU C . n 
C 1 87  LEU 87  109 109 LEU LEU C . n 
C 1 88  VAL 88  110 110 VAL VAL C . n 
C 1 89  ASP 89  111 111 ASP ASP C . n 
C 1 90  GLN 90  112 112 GLN GLN C . n 
C 1 91  VAL 91  113 113 VAL VAL C . n 
C 1 92  PRO 92  114 114 PRO PRO C . n 
C 1 93  ILE 93  115 115 ILE ILE C . n 
C 1 94  LEU 94  116 116 LEU LEU C . n 
C 1 95  GLU 95  117 117 GLU GLU C . n 
C 1 96  THR 96  118 118 THR THR C . n 
C 1 97  MET 97  119 119 MET MET C . n 
C 1 98  THR 98  120 120 THR THR C . n 
C 1 99  PRO 99  121 121 PRO PRO C . n 
C 1 100 LEU 100 122 122 LEU LEU C . n 
C 1 101 ASP 101 123 123 ASP ASP C . n 
C 1 102 PHE 102 124 124 PHE PHE C . n 
C 1 103 MET 103 125 125 MET MET C . n 
C 1 104 ASP 104 126 126 ASP ASP C . n 
C 1 105 PHE 105 127 127 PHE PHE C . n 
C 1 106 ARG 106 128 128 ARG ARG C . n 
C 1 107 LYS 107 129 129 LYS LYS C . n 
C 1 108 TYR 108 130 130 TYR TYR C . n 
C 1 109 LEU 109 131 131 LEU LEU C . n 
C 1 110 ALA 110 132 132 ALA ALA C . n 
C 1 111 PRO 111 133 133 PRO PRO C . n 
C 1 112 ALA 112 134 134 ALA ALA C . n 
C 1 113 SER 113 135 135 SER SER C . n 
C 1 114 GLY 114 136 136 GLY GLY C . n 
C 1 115 PHE 115 137 137 PHE PHE C . n 
C 1 116 GLN 116 138 138 GLN GLN C . n 
C 1 117 SER 117 139 139 SER SER C . n 
C 1 118 LEU 118 140 140 LEU LEU C . n 
C 1 119 GLN 119 141 141 GLN GLN C . n 
C 1 120 PHE 120 142 142 PHE PHE C . n 
C 1 121 ARG 121 143 143 ARG ARG C . n 
C 1 122 LEU 122 144 144 LEU LEU C . n 
C 1 123 ILE 123 145 145 ILE ILE C . n 
C 1 124 GLU 124 146 146 GLU GLU C . n 
C 1 125 ASN 125 147 147 ASN ASN C . n 
C 1 126 LYS 126 148 148 LYS LYS C . n 
C 1 127 LEU 127 149 149 LEU LEU C . n 
C 1 128 GLY 128 150 150 GLY GLY C . n 
C 1 129 VAL 129 151 151 VAL VAL C . n 
C 1 130 LEU 130 152 152 LEU LEU C . n 
C 1 131 THR 131 153 153 THR THR C . n 
C 1 132 GLU 132 154 154 GLU GLU C . n 
C 1 133 GLN 133 155 ?   ?   ?   C . n 
C 1 134 ARG 134 156 ?   ?   ?   C . n 
C 1 135 VAL 135 157 ?   ?   ?   C . n 
C 1 136 ARG 136 158 ?   ?   ?   C . n 
C 1 137 TYR 137 159 ?   ?   ?   C . n 
C 1 138 ASN 138 160 ?   ?   ?   C . n 
C 1 139 GLN 139 161 ?   ?   ?   C . n 
C 1 140 LYS 140 162 ?   ?   ?   C . n 
C 1 141 TYR 141 163 ?   ?   ?   C . n 
C 1 142 SER 142 164 ?   ?   ?   C . n 
C 1 143 ASP 143 165 ?   ?   ?   C . n 
C 1 144 VAL 144 166 ?   ?   ?   C . n 
C 1 145 PHE 145 167 ?   ?   ?   C . n 
C 1 146 SER 146 168 168 SER ALA C . n 
C 1 147 ASP 147 169 169 ASP ASP C . n 
C 1 148 GLU 148 170 170 GLU GLU C . n 
C 1 149 GLU 149 171 171 GLU GLU C . n 
C 1 150 ALA 150 172 172 ALA ALA C . n 
C 1 151 ARG 151 173 173 ARG ARG C . n 
C 1 152 ASN 152 174 174 ASN ASN C . n 
C 1 153 SER 153 175 175 SER SER C . n 
C 1 154 ILE 154 176 176 ILE ILE C . n 
C 1 155 ARG 155 177 177 ARG ARG C . n 
C 1 156 ASN 156 178 178 ASN ASN C . n 
C 1 157 SER 157 179 179 SER SER C . n 
C 1 158 GLU 158 180 180 GLU GLU C . n 
C 1 159 LYS 159 181 181 LYS LYS C . n 
C 1 160 ASP 160 182 182 ASP ASP C . n 
C 1 161 PRO 161 183 183 PRO PRO C . n 
C 1 162 SER 162 184 184 SER SER C . n 
C 1 163 LEU 163 185 185 LEU LEU C . n 
C 1 164 LEU 164 186 186 LEU LEU C . n 
C 1 165 GLU 165 187 187 GLU GLU C . n 
C 1 166 LEU 166 188 188 LEU LEU C . n 
C 1 167 VAL 167 189 189 VAL VAL C . n 
C 1 168 GLN 168 190 190 GLN GLN C . n 
C 1 169 ARG 169 191 191 ARG ARG C . n 
C 1 170 TRP 170 192 192 TRP TRP C . n 
C 1 171 LEU 171 193 193 LEU LEU C . n 
C 1 172 GLU 172 194 194 GLU GLU C . n 
C 1 173 ARG 173 195 195 ARG ARG C . n 
C 1 174 THR 174 196 196 THR THR C . n 
C 1 175 PRO 175 197 197 PRO PRO C . n 
C 1 176 GLY 176 198 198 GLY GLY C . n 
C 1 177 LEU 177 199 199 LEU LEU C . n 
C 1 178 GLU 178 200 200 GLU GLU C . n 
C 1 179 GLU 179 201 201 GLU GLU C . n 
C 1 180 SER 180 202 202 SER SER C . n 
C 1 181 GLY 181 203 203 GLY GLY C . n 
C 1 182 PHE 182 204 204 PHE PHE C . n 
C 1 183 ASN 183 205 205 ASN ASN C . n 
C 1 184 PHE 184 206 206 PHE PHE C . n 
C 1 185 TRP 185 207 207 TRP TRP C . n 
C 1 186 ALA 186 208 208 ALA ALA C . n 
C 1 187 LYS 187 209 209 LYS LYS C . n 
C 1 188 PHE 188 210 210 PHE PHE C . n 
C 1 189 GLN 189 211 211 GLN GLN C . n 
C 1 190 GLU 190 212 212 GLU GLU C . n 
C 1 191 SER 191 213 213 SER SER C . n 
C 1 192 VAL 192 214 214 VAL VAL C . n 
C 1 193 ASP 193 215 215 ASP ASP C . n 
C 1 194 ARG 194 216 216 ARG ARG C . n 
C 1 195 PHE 195 217 217 PHE PHE C . n 
C 1 196 LEU 196 218 218 LEU LEU C . n 
C 1 197 GLU 197 219 219 GLU GLU C . n 
C 1 198 ALA 198 220 220 ALA ALA C . n 
C 1 199 GLN 199 221 221 GLN GLN C . n 
C 1 200 VAL 200 222 222 VAL VAL C . n 
C 1 201 GLN 201 223 223 GLN GLN C . n 
C 1 202 SER 202 224 224 SER SER C . n 
C 1 203 ALA 203 225 225 ALA ALA C . n 
C 1 204 MET 204 226 226 MET MET C . n 
C 1 205 GLU 205 227 227 GLU GLU C . n 
C 1 206 GLU 206 228 228 GLU GLU C . n 
C 1 207 PRO 207 229 229 PRO PRO C . n 
C 1 208 VAL 208 230 230 VAL VAL C . n 
C 1 209 GLU 209 231 231 GLU GLU C . n 
C 1 210 LYS 210 232 232 LYS LYS C . n 
C 1 211 ALA 211 233 233 ALA ALA C . n 
C 1 212 LYS 212 234 234 LYS LYS C . n 
C 1 213 ASN 213 235 235 ASN ASN C . n 
C 1 214 TYR 214 236 236 TYR TYR C . n 
C 1 215 ARG 215 237 237 ARG ARG C . n 
C 1 216 LEU 216 238 238 LEU LEU C . n 
C 1 217 MET 217 239 239 MET MET C . n 
C 1 218 ASP 218 240 240 ASP ASP C . n 
C 1 219 ILE 219 241 241 ILE ILE C . n 
C 1 220 GLU 220 242 242 GLU GLU C . n 
C 1 221 LYS 221 243 243 LYS LYS C . n 
C 1 222 ARG 222 244 244 ARG ARG C . n 
C 1 223 ARG 223 245 245 ARG ARG C . n 
C 1 224 GLU 224 246 246 GLU GLU C . n 
C 1 225 VAL 225 247 247 VAL VAL C . n 
C 1 226 TYR 226 248 248 TYR TYR C . n 
C 1 227 ARG 227 249 249 ARG ARG C . n 
C 1 228 SER 228 250 250 SER SER C . n 
C 1 229 ILE 229 251 251 ILE ILE C . n 
C 1 230 PHE 230 252 252 PHE PHE C . n 
C 1 231 ASP 231 253 253 ASP ASP C . n 
C 1 232 PRO 232 254 254 PRO PRO C . n 
C 1 233 ALA 233 255 255 ALA ALA C . n 
C 1 234 VAL 234 256 256 VAL VAL C . n 
C 1 235 HIS 235 257 257 HIS HIS C . n 
C 1 236 ASP 236 258 258 ASP ASP C . n 
C 1 237 ALA 237 259 259 ALA ALA C . n 
C 1 238 LEU 238 260 260 LEU LEU C . n 
C 1 239 VAL 239 261 261 VAL VAL C . n 
C 1 240 ARG 240 262 262 ARG ARG C . n 
C 1 241 ARG 241 263 263 ARG ARG C . n 
C 1 242 GLY 242 264 264 GLY GLY C . n 
C 1 243 ASP 243 265 265 ASP ASP C . n 
C 1 244 ARG 244 266 266 ARG ARG C . n 
C 1 245 ARG 245 267 267 ARG ARG C . n 
C 1 246 PHE 246 268 268 PHE PHE C . n 
C 1 247 SER 247 269 269 SER SER C . n 
C 1 248 HIS 248 270 270 HIS HIS C . n 
C 1 249 ARG 249 271 271 ARG ARG C . n 
C 1 250 ALA 250 272 272 ALA ALA C . n 
C 1 251 LEU 251 273 273 LEU LEU C . n 
C 1 252 GLN 252 274 274 GLN GLN C . n 
C 1 253 GLY 253 275 275 GLY GLY C . n 
C 1 254 ALA 254 276 276 ALA ALA C . n 
C 1 255 ILE 255 277 277 ILE ILE C . n 
C 1 256 MET 256 278 278 MET MET C . n 
C 1 257 ILE 257 279 279 ILE ILE C . n 
C 1 258 THR 258 280 280 THR THR C . n 
C 1 259 PHE 259 281 281 PHE PHE C . n 
C 1 260 TYR 260 282 282 TYR TYR C . n 
C 1 261 ARG 261 283 283 ARG ARG C . n 
C 1 262 ASP 262 284 284 ASP ASP C . n 
C 1 263 GLU 263 285 285 GLU GLU C . n 
C 1 264 PRO 264 286 286 PRO PRO C . n 
C 1 265 ARG 265 287 287 ARG ARG C . n 
C 1 266 PHE 266 288 288 PHE PHE C . n 
C 1 267 SER 267 289 289 SER SER C . n 
C 1 268 GLN 268 290 290 GLN GLN C . n 
C 1 269 PRO 269 291 291 PRO PRO C . n 
C 1 270 HIS 270 292 292 HIS HIS C . n 
C 1 271 GLN 271 293 293 GLN GLN C . n 
C 1 272 LEU 272 294 294 LEU LEU C . n 
C 1 273 LEU 273 295 295 LEU LEU C . n 
C 1 274 THR 274 296 296 THR THR C . n 
C 1 275 LEU 275 297 297 LEU LEU C . n 
C 1 276 LEU 276 298 298 LEU LEU C . n 
C 1 277 MET 277 299 299 MET MET C . n 
C 1 278 ASP 278 300 300 ASP ASP C . n 
C 1 279 ILE 279 301 301 ILE ILE C . n 
C 1 280 ASP 280 302 302 ASP ASP C . n 
C 1 281 SER 281 303 303 SER SER C . n 
C 1 282 LEU 282 304 304 LEU LEU C . n 
C 1 283 ILE 283 305 305 ILE ILE C . n 
C 1 284 THR 284 306 306 THR THR C . n 
C 1 285 LYS 285 307 307 LYS LYS C . n 
C 1 286 TRP 286 308 308 TRP TRP C . n 
C 1 287 ARG 287 309 309 ARG ARG C . n 
C 1 288 TYR 288 310 310 TYR TYR C . n 
C 1 289 ASN 289 311 311 ASN ASN C . n 
C 1 290 HIS 290 312 312 HIS HIS C . n 
C 1 291 VAL 291 313 313 VAL VAL C . n 
C 1 292 ILE 292 314 314 ILE ILE C . n 
C 1 293 MET 293 315 315 MET MET C . n 
C 1 294 VAL 294 316 316 VAL VAL C . n 
C 1 295 GLN 295 317 317 GLN GLN C . n 
C 1 296 ARG 296 318 318 ARG ARG C . n 
C 1 297 MET 297 319 319 MET MET C . n 
C 1 298 ILE 298 320 320 ILE ILE C . n 
C 1 299 GLY 299 321 321 GLY GLY C . n 
C 1 300 SER 300 322 322 SER SER C . n 
C 1 301 GLN 301 323 323 GLN GLN C . n 
C 1 302 GLN 302 324 324 GLN GLN C . n 
C 1 303 LEU 303 325 325 LEU LEU C . n 
C 1 304 GLY 304 326 326 GLY GLY C . n 
C 1 305 THR 305 327 327 THR THR C . n 
C 1 306 GLY 306 328 328 GLY GLY C . n 
C 1 307 GLY 307 329 329 GLY GLY C . n 
C 1 308 SER 308 330 330 SER SER C . n 
C 1 309 SER 309 331 331 SER SER C . n 
C 1 310 GLY 310 332 332 GLY GLY C . n 
C 1 311 TYR 311 333 333 TYR TYR C . n 
C 1 312 GLN 312 334 334 GLN GLN C . n 
C 1 313 TYR 313 335 335 TYR TYR C . n 
C 1 314 LEU 314 336 336 LEU LEU C . n 
C 1 315 ARG 315 337 337 ARG ARG C . n 
C 1 316 SER 316 338 338 SER SER C . n 
C 1 317 THR 317 339 339 THR THR C . n 
C 1 318 LEU 318 340 340 LEU LEU C . n 
C 1 319 SER 319 341 341 SER SER C . n 
C 1 320 ASP 320 342 342 ASP ASP C . n 
C 1 321 ARG 321 343 343 ARG ARG C . n 
C 1 322 TYR 322 344 344 TYR TYR C . n 
C 1 323 LYS 323 345 345 LYS LYS C . n 
C 1 324 VAL 324 346 346 VAL VAL C . n 
C 1 325 PHE 325 347 347 PHE PHE C . n 
C 1 326 LEU 326 348 348 LEU LEU C . n 
C 1 327 ASP 327 349 349 ASP ASP C . n 
C 1 328 LEU 328 350 350 LEU LEU C . n 
C 1 329 PHE 329 351 351 PHE PHE C . n 
C 1 330 ASN 330 352 352 ASN ASN C . n 
C 1 331 LEU 331 353 353 LEU LEU C . n 
C 1 332 SER 332 354 354 SER SER C . n 
C 1 333 THR 333 355 355 THR THR C . n 
C 1 334 PHE 334 356 356 PHE PHE C . n 
C 1 335 LEU 335 357 357 LEU LEU C . n 
C 1 336 ILE 336 358 358 ILE ILE C . n 
C 1 337 PRO 337 359 359 PRO PRO C . n 
C 1 338 ARG 338 360 360 ARG ARG C . n 
C 1 339 GLU 339 361 361 GLU GLU C . n 
C 1 340 ALA 340 362 362 ALA ALA C . n 
C 1 341 ILE 341 363 363 ILE ILE C . n 
C 1 342 PRO 342 364 364 PRO PRO C . n 
C 1 343 PRO 343 365 365 PRO PRO C . n 
C 1 344 LEU 344 366 366 LEU LEU C . n 
C 1 345 ASP 345 367 367 ASP ASP C . n 
C 1 346 GLU 346 368 368 GLU GLU C . n 
C 1 347 THR 347 369 ?   ?   ?   C . n 
C 1 348 ILE 348 370 ?   ?   ?   C . n 
C 1 349 ARG 349 371 ?   ?   ?   C . n 
C 1 350 LYS 350 372 ?   ?   ?   C . n 
C 1 351 LYS 351 373 ?   ?   ?   C . n 
C 1 352 LEU 352 374 ?   ?   ?   C . n 
C 1 353 ILE 353 375 ?   ?   ?   C . n 
C 1 354 ASN 354 376 ?   ?   ?   C . n 
C 1 355 LYS 355 377 ?   ?   ?   C . n 
C 1 356 SER 356 378 ?   ?   ?   C . n 
C 1 357 VAL 357 379 ?   ?   ?   C . n 
C 1 358 LEU 358 380 ?   ?   ?   C . n 
C 1 359 GLU 359 381 ?   ?   ?   C . n 
C 1 360 HIS 360 382 ?   ?   ?   C . n 
C 1 361 HIS 361 383 ?   ?   ?   C . n 
C 1 362 HIS 362 384 ?   ?   ?   C . n 
C 1 363 HIS 363 385 ?   ?   ?   C . n 
C 1 364 HIS 364 386 ?   ?   ?   C . n 
C 1 365 HIS 365 387 ?   ?   ?   C . n 
D 1 1   MET 1   23  ?   ?   ?   D . n 
D 1 2   GLY 2   24  ?   ?   ?   D . n 
D 1 3   LYS 3   25  25  LYS LYS D . n 
D 1 4   ILE 4   26  26  ILE ILE D . n 
D 1 5   TYR 5   27  27  TYR TYR D . n 
D 1 6   GLY 6   28  28  GLY GLY D . n 
D 1 7   GLU 7   29  29  GLU GLU D . n 
D 1 8   TYR 8   30  30  TYR TYR D . n 
D 1 9   LEU 9   31  31  LEU LEU D . n 
D 1 10  MET 10  32  32  MET MET D . n 
D 1 11  LEU 11  33  33  LEU LEU D . n 
D 1 12  ASP 12  34  34  ASP ASP D . n 
D 1 13  LYS 13  35  35  LYS LYS D . n 
D 1 14  LEU 14  36  36  LEU LEU D . n 
D 1 15  LEU 15  37  37  LEU LEU D . n 
D 1 16  ASP 16  38  38  ASP ASP D . n 
D 1 17  ALA 17  39  39  ALA ALA D . n 
D 1 18  GLN 18  40  40  GLN GLN D . n 
D 1 19  CYS 19  41  41  CYS CYS D . n 
D 1 20  MET 20  42  42  MET MET D . n 
D 1 21  LEU 21  43  43  LEU LEU D . n 
D 1 22  SER 22  44  44  SER SER D . n 
D 1 23  GLU 23  45  45  GLU GLU D . n 
D 1 24  GLU 24  46  46  GLU GLU D . n 
D 1 25  ASP 25  47  47  ASP ASP D . n 
D 1 26  LYS 26  48  48  LYS LYS D . n 
D 1 27  ARG 27  49  49  ARG ARG D . n 
D 1 28  PRO 28  50  50  PRO PRO D . n 
D 1 29  VAL 29  51  51  VAL VAL D . n 
D 1 30  HIS 30  52  52  HIS HIS D . n 
D 1 31  ASP 31  53  53  ASP ASP D . n 
D 1 32  GLU 32  54  54  GLU GLU D . n 
D 1 33  HIS 33  55  55  HIS HIS D . n 
D 1 34  LEU 34  56  56  LEU LEU D . n 
D 1 35  PHE 35  57  57  PHE PHE D . n 
D 1 36  ILE 36  58  58  ILE ILE D . n 
D 1 37  ILE 37  59  59  ILE ILE D . n 
D 1 38  THR 38  60  60  THR THR D . n 
D 1 39  HIS 39  61  61  HIS HIS D . n 
D 1 40  GLN 40  62  62  GLN GLN D . n 
D 1 41  ALA 41  63  63  ALA ALA D . n 
D 1 42  TYR 42  64  64  TYR TYR D . n 
D 1 43  GLU 43  65  65  GLU GLU D . n 
D 1 44  LEU 44  66  66  LEU LEU D . n 
D 1 45  TRP 45  67  67  TRP TRP D . n 
D 1 46  PHE 46  68  68  PHE PHE D . n 
D 1 47  LYS 47  69  69  LYS LYS D . n 
D 1 48  GLN 48  70  70  GLN GLN D . n 
D 1 49  ILE 49  71  71  ILE ILE D . n 
D 1 50  ILE 50  72  72  ILE ILE D . n 
D 1 51  PHE 51  73  73  PHE PHE D . n 
D 1 52  GLU 52  74  74  GLU GLU D . n 
D 1 53  PHE 53  75  75  PHE PHE D . n 
D 1 54  ASP 54  76  76  ASP ASP D . n 
D 1 55  SER 55  77  77  SER SER D . n 
D 1 56  ILE 56  78  78  ILE ILE D . n 
D 1 57  ARG 57  79  79  ARG ARG D . n 
D 1 58  ASP 58  80  80  ASP ASP D . n 
D 1 59  MET 59  81  81  MET MET D . n 
D 1 60  LEU 60  82  82  LEU LEU D . n 
D 1 61  ASP 61  83  83  ASP ASP D . n 
D 1 62  ALA 62  84  84  ALA ALA D . n 
D 1 63  GLU 63  85  85  GLU GLU D . n 
D 1 64  VAL 64  86  86  VAL VAL D . n 
D 1 65  ILE 65  87  87  ILE ILE D . n 
D 1 66  ASP 66  88  88  ASP ASP D . n 
D 1 67  GLU 67  89  89  GLU GLU D . n 
D 1 68  THR 68  90  90  THR THR D . n 
D 1 69  LYS 69  91  91  LYS LYS D . n 
D 1 70  THR 70  92  92  THR THR D . n 
D 1 71  LEU 71  93  93  LEU LEU D . n 
D 1 72  GLU 72  94  94  GLU GLU D . n 
D 1 73  ILE 73  95  95  ILE ILE D . n 
D 1 74  VAL 74  96  96  VAL VAL D . n 
D 1 75  LYS 75  97  97  LYS LYS D . n 
D 1 76  ARG 76  98  98  ARG ARG D . n 
D 1 77  LEU 77  99  99  LEU LEU D . n 
D 1 78  ASN 78  100 100 ASN ASN D . n 
D 1 79  ARG 79  101 101 ARG ARG D . n 
D 1 80  VAL 80  102 102 VAL VAL D . n 
D 1 81  VAL 81  103 103 VAL VAL D . n 
D 1 82  LEU 82  104 104 LEU LEU D . n 
D 1 83  ILE 83  105 105 ILE ILE D . n 
D 1 84  LEU 84  106 106 LEU LEU D . n 
D 1 85  LYS 85  107 107 LYS LYS D . n 
D 1 86  LEU 86  108 108 LEU LEU D . n 
D 1 87  LEU 87  109 109 LEU LEU D . n 
D 1 88  VAL 88  110 110 VAL VAL D . n 
D 1 89  ASP 89  111 111 ASP ASP D . n 
D 1 90  GLN 90  112 112 GLN GLN D . n 
D 1 91  VAL 91  113 113 VAL VAL D . n 
D 1 92  PRO 92  114 114 PRO PRO D . n 
D 1 93  ILE 93  115 115 ILE ILE D . n 
D 1 94  LEU 94  116 116 LEU LEU D . n 
D 1 95  GLU 95  117 117 GLU GLU D . n 
D 1 96  THR 96  118 118 THR THR D . n 
D 1 97  MET 97  119 119 MET MET D . n 
D 1 98  THR 98  120 120 THR THR D . n 
D 1 99  PRO 99  121 121 PRO PRO D . n 
D 1 100 LEU 100 122 122 LEU LEU D . n 
D 1 101 ASP 101 123 123 ASP ASP D . n 
D 1 102 PHE 102 124 124 PHE PHE D . n 
D 1 103 MET 103 125 125 MET MET D . n 
D 1 104 ASP 104 126 126 ASP ASP D . n 
D 1 105 PHE 105 127 127 PHE PHE D . n 
D 1 106 ARG 106 128 128 ARG ARG D . n 
D 1 107 LYS 107 129 129 LYS LYS D . n 
D 1 108 TYR 108 130 130 TYR TYR D . n 
D 1 109 LEU 109 131 131 LEU LEU D . n 
D 1 110 ALA 110 132 ?   ?   ?   D . n 
D 1 111 PRO 111 133 ?   ?   ?   D . n 
D 1 112 ALA 112 134 ?   ?   ?   D . n 
D 1 113 SER 113 135 ?   ?   ?   D . n 
D 1 114 GLY 114 136 ?   ?   ?   D . n 
D 1 115 PHE 115 137 ?   ?   ?   D . n 
D 1 116 GLN 116 138 138 GLN GLN D . n 
D 1 117 SER 117 139 139 SER SER D . n 
D 1 118 LEU 118 140 140 LEU LEU D . n 
D 1 119 GLN 119 141 141 GLN GLN D . n 
D 1 120 PHE 120 142 142 PHE PHE D . n 
D 1 121 ARG 121 143 143 ARG ARG D . n 
D 1 122 LEU 122 144 144 LEU LEU D . n 
D 1 123 ILE 123 145 145 ILE ILE D . n 
D 1 124 GLU 124 146 146 GLU GLU D . n 
D 1 125 ASN 125 147 147 ASN ASN D . n 
D 1 126 LYS 126 148 148 LYS LYS D . n 
D 1 127 LEU 127 149 149 LEU LEU D . n 
D 1 128 GLY 128 150 150 GLY GLY D . n 
D 1 129 VAL 129 151 151 VAL VAL D . n 
D 1 130 LEU 130 152 152 LEU LEU D . n 
D 1 131 THR 131 153 153 THR THR D . n 
D 1 132 GLU 132 154 154 GLU GLU D . n 
D 1 133 GLN 133 155 155 GLN GLN D . n 
D 1 134 ARG 134 156 156 ARG ALA D . n 
D 1 135 VAL 135 157 157 VAL ALA D . n 
D 1 136 ARG 136 158 158 ARG ALA D . n 
D 1 137 TYR 137 159 ?   ?   ?   D . n 
D 1 138 ASN 138 160 ?   ?   ?   D . n 
D 1 139 GLN 139 161 ?   ?   ?   D . n 
D 1 140 LYS 140 162 ?   ?   ?   D . n 
D 1 141 TYR 141 163 ?   ?   ?   D . n 
D 1 142 SER 142 164 ?   ?   ?   D . n 
D 1 143 ASP 143 165 ?   ?   ?   D . n 
D 1 144 VAL 144 166 166 VAL ALA D . n 
D 1 145 PHE 145 167 167 PHE ALA D . n 
D 1 146 SER 146 168 168 SER ALA D . n 
D 1 147 ASP 147 169 169 ASP ASP D . n 
D 1 148 GLU 148 170 170 GLU GLU D . n 
D 1 149 GLU 149 171 171 GLU GLU D . n 
D 1 150 ALA 150 172 172 ALA ALA D . n 
D 1 151 ARG 151 173 173 ARG ARG D . n 
D 1 152 ASN 152 174 174 ASN ASN D . n 
D 1 153 SER 153 175 175 SER SER D . n 
D 1 154 ILE 154 176 176 ILE ILE D . n 
D 1 155 ARG 155 177 177 ARG ARG D . n 
D 1 156 ASN 156 178 178 ASN ASN D . n 
D 1 157 SER 157 179 179 SER SER D . n 
D 1 158 GLU 158 180 180 GLU GLU D . n 
D 1 159 LYS 159 181 181 LYS LYS D . n 
D 1 160 ASP 160 182 182 ASP ASP D . n 
D 1 161 PRO 161 183 183 PRO PRO D . n 
D 1 162 SER 162 184 184 SER SER D . n 
D 1 163 LEU 163 185 185 LEU LEU D . n 
D 1 164 LEU 164 186 186 LEU LEU D . n 
D 1 165 GLU 165 187 187 GLU GLU D . n 
D 1 166 LEU 166 188 188 LEU LEU D . n 
D 1 167 VAL 167 189 189 VAL VAL D . n 
D 1 168 GLN 168 190 190 GLN GLN D . n 
D 1 169 ARG 169 191 191 ARG ARG D . n 
D 1 170 TRP 170 192 192 TRP TRP D . n 
D 1 171 LEU 171 193 193 LEU LEU D . n 
D 1 172 GLU 172 194 194 GLU GLU D . n 
D 1 173 ARG 173 195 195 ARG ARG D . n 
D 1 174 THR 174 196 196 THR THR D . n 
D 1 175 PRO 175 197 197 PRO PRO D . n 
D 1 176 GLY 176 198 198 GLY GLY D . n 
D 1 177 LEU 177 199 199 LEU LEU D . n 
D 1 178 GLU 178 200 200 GLU GLU D . n 
D 1 179 GLU 179 201 201 GLU GLU D . n 
D 1 180 SER 180 202 202 SER SER D . n 
D 1 181 GLY 181 203 203 GLY GLY D . n 
D 1 182 PHE 182 204 204 PHE PHE D . n 
D 1 183 ASN 183 205 205 ASN ASN D . n 
D 1 184 PHE 184 206 206 PHE PHE D . n 
D 1 185 TRP 185 207 207 TRP TRP D . n 
D 1 186 ALA 186 208 208 ALA ALA D . n 
D 1 187 LYS 187 209 209 LYS LYS D . n 
D 1 188 PHE 188 210 210 PHE PHE D . n 
D 1 189 GLN 189 211 211 GLN GLN D . n 
D 1 190 GLU 190 212 212 GLU GLU D . n 
D 1 191 SER 191 213 213 SER SER D . n 
D 1 192 VAL 192 214 214 VAL VAL D . n 
D 1 193 ASP 193 215 215 ASP ASP D . n 
D 1 194 ARG 194 216 216 ARG ARG D . n 
D 1 195 PHE 195 217 217 PHE PHE D . n 
D 1 196 LEU 196 218 218 LEU LEU D . n 
D 1 197 GLU 197 219 219 GLU GLU D . n 
D 1 198 ALA 198 220 220 ALA ALA D . n 
D 1 199 GLN 199 221 221 GLN GLN D . n 
D 1 200 VAL 200 222 222 VAL VAL D . n 
D 1 201 GLN 201 223 223 GLN GLN D . n 
D 1 202 SER 202 224 224 SER SER D . n 
D 1 203 ALA 203 225 225 ALA ALA D . n 
D 1 204 MET 204 226 226 MET MET D . n 
D 1 205 GLU 205 227 227 GLU GLU D . n 
D 1 206 GLU 206 228 228 GLU GLU D . n 
D 1 207 PRO 207 229 229 PRO PRO D . n 
D 1 208 VAL 208 230 230 VAL VAL D . n 
D 1 209 GLU 209 231 231 GLU GLU D . n 
D 1 210 LYS 210 232 232 LYS LYS D . n 
D 1 211 ALA 211 233 233 ALA ALA D . n 
D 1 212 LYS 212 234 234 LYS LYS D . n 
D 1 213 ASN 213 235 235 ASN ASN D . n 
D 1 214 TYR 214 236 236 TYR TYR D . n 
D 1 215 ARG 215 237 237 ARG ARG D . n 
D 1 216 LEU 216 238 238 LEU LEU D . n 
D 1 217 MET 217 239 239 MET MET D . n 
D 1 218 ASP 218 240 240 ASP ASP D . n 
D 1 219 ILE 219 241 241 ILE ILE D . n 
D 1 220 GLU 220 242 242 GLU GLU D . n 
D 1 221 LYS 221 243 243 LYS LYS D . n 
D 1 222 ARG 222 244 244 ARG ARG D . n 
D 1 223 ARG 223 245 245 ARG ARG D . n 
D 1 224 GLU 224 246 246 GLU GLU D . n 
D 1 225 VAL 225 247 247 VAL VAL D . n 
D 1 226 TYR 226 248 248 TYR TYR D . n 
D 1 227 ARG 227 249 249 ARG ARG D . n 
D 1 228 SER 228 250 250 SER SER D . n 
D 1 229 ILE 229 251 251 ILE ILE D . n 
D 1 230 PHE 230 252 252 PHE PHE D . n 
D 1 231 ASP 231 253 253 ASP ASP D . n 
D 1 232 PRO 232 254 254 PRO PRO D . n 
D 1 233 ALA 233 255 255 ALA ALA D . n 
D 1 234 VAL 234 256 256 VAL VAL D . n 
D 1 235 HIS 235 257 257 HIS HIS D . n 
D 1 236 ASP 236 258 258 ASP ASP D . n 
D 1 237 ALA 237 259 259 ALA ALA D . n 
D 1 238 LEU 238 260 260 LEU LEU D . n 
D 1 239 VAL 239 261 261 VAL VAL D . n 
D 1 240 ARG 240 262 262 ARG ARG D . n 
D 1 241 ARG 241 263 263 ARG ARG D . n 
D 1 242 GLY 242 264 264 GLY GLY D . n 
D 1 243 ASP 243 265 265 ASP ASP D . n 
D 1 244 ARG 244 266 266 ARG ARG D . n 
D 1 245 ARG 245 267 267 ARG ARG D . n 
D 1 246 PHE 246 268 268 PHE PHE D . n 
D 1 247 SER 247 269 269 SER SER D . n 
D 1 248 HIS 248 270 270 HIS HIS D . n 
D 1 249 ARG 249 271 271 ARG ARG D . n 
D 1 250 ALA 250 272 272 ALA ALA D . n 
D 1 251 LEU 251 273 273 LEU LEU D . n 
D 1 252 GLN 252 274 274 GLN GLN D . n 
D 1 253 GLY 253 275 275 GLY GLY D . n 
D 1 254 ALA 254 276 276 ALA ALA D . n 
D 1 255 ILE 255 277 277 ILE ILE D . n 
D 1 256 MET 256 278 278 MET MET D . n 
D 1 257 ILE 257 279 279 ILE ILE D . n 
D 1 258 THR 258 280 280 THR THR D . n 
D 1 259 PHE 259 281 281 PHE PHE D . n 
D 1 260 TYR 260 282 282 TYR TYR D . n 
D 1 261 ARG 261 283 283 ARG ARG D . n 
D 1 262 ASP 262 284 284 ASP ASP D . n 
D 1 263 GLU 263 285 285 GLU GLU D . n 
D 1 264 PRO 264 286 286 PRO PRO D . n 
D 1 265 ARG 265 287 287 ARG ARG D . n 
D 1 266 PHE 266 288 288 PHE PHE D . n 
D 1 267 SER 267 289 289 SER SER D . n 
D 1 268 GLN 268 290 290 GLN GLN D . n 
D 1 269 PRO 269 291 291 PRO PRO D . n 
D 1 270 HIS 270 292 292 HIS HIS D . n 
D 1 271 GLN 271 293 293 GLN GLN D . n 
D 1 272 LEU 272 294 294 LEU LEU D . n 
D 1 273 LEU 273 295 295 LEU LEU D . n 
D 1 274 THR 274 296 296 THR THR D . n 
D 1 275 LEU 275 297 297 LEU LEU D . n 
D 1 276 LEU 276 298 298 LEU LEU D . n 
D 1 277 MET 277 299 299 MET MET D . n 
D 1 278 ASP 278 300 300 ASP ASP D . n 
D 1 279 ILE 279 301 301 ILE ILE D . n 
D 1 280 ASP 280 302 302 ASP ASP D . n 
D 1 281 SER 281 303 303 SER SER D . n 
D 1 282 LEU 282 304 304 LEU LEU D . n 
D 1 283 ILE 283 305 305 ILE ILE D . n 
D 1 284 THR 284 306 306 THR THR D . n 
D 1 285 LYS 285 307 307 LYS LYS D . n 
D 1 286 TRP 286 308 308 TRP TRP D . n 
D 1 287 ARG 287 309 309 ARG ARG D . n 
D 1 288 TYR 288 310 310 TYR TYR D . n 
D 1 289 ASN 289 311 311 ASN ASN D . n 
D 1 290 HIS 290 312 312 HIS HIS D . n 
D 1 291 VAL 291 313 313 VAL VAL D . n 
D 1 292 ILE 292 314 314 ILE ILE D . n 
D 1 293 MET 293 315 315 MET MET D . n 
D 1 294 VAL 294 316 316 VAL VAL D . n 
D 1 295 GLN 295 317 317 GLN GLN D . n 
D 1 296 ARG 296 318 318 ARG ARG D . n 
D 1 297 MET 297 319 319 MET MET D . n 
D 1 298 ILE 298 320 320 ILE ILE D . n 
D 1 299 GLY 299 321 321 GLY GLY D . n 
D 1 300 SER 300 322 322 SER SER D . n 
D 1 301 GLN 301 323 323 GLN GLN D . n 
D 1 302 GLN 302 324 324 GLN GLN D . n 
D 1 303 LEU 303 325 325 LEU LEU D . n 
D 1 304 GLY 304 326 326 GLY GLY D . n 
D 1 305 THR 305 327 327 THR THR D . n 
D 1 306 GLY 306 328 328 GLY GLY D . n 
D 1 307 GLY 307 329 329 GLY GLY D . n 
D 1 308 SER 308 330 330 SER SER D . n 
D 1 309 SER 309 331 331 SER SER D . n 
D 1 310 GLY 310 332 332 GLY GLY D . n 
D 1 311 TYR 311 333 333 TYR TYR D . n 
D 1 312 GLN 312 334 334 GLN GLN D . n 
D 1 313 TYR 313 335 335 TYR TYR D . n 
D 1 314 LEU 314 336 336 LEU LEU D . n 
D 1 315 ARG 315 337 337 ARG ARG D . n 
D 1 316 SER 316 338 338 SER SER D . n 
D 1 317 THR 317 339 339 THR THR D . n 
D 1 318 LEU 318 340 340 LEU LEU D . n 
D 1 319 SER 319 341 341 SER SER D . n 
D 1 320 ASP 320 342 342 ASP ASP D . n 
D 1 321 ARG 321 343 343 ARG ARG D . n 
D 1 322 TYR 322 344 344 TYR TYR D . n 
D 1 323 LYS 323 345 345 LYS LYS D . n 
D 1 324 VAL 324 346 346 VAL VAL D . n 
D 1 325 PHE 325 347 347 PHE PHE D . n 
D 1 326 LEU 326 348 348 LEU LEU D . n 
D 1 327 ASP 327 349 349 ASP ASP D . n 
D 1 328 LEU 328 350 350 LEU LEU D . n 
D 1 329 PHE 329 351 351 PHE PHE D . n 
D 1 330 ASN 330 352 352 ASN ASN D . n 
D 1 331 LEU 331 353 353 LEU LEU D . n 
D 1 332 SER 332 354 354 SER SER D . n 
D 1 333 THR 333 355 355 THR THR D . n 
D 1 334 PHE 334 356 356 PHE PHE D . n 
D 1 335 LEU 335 357 357 LEU LEU D . n 
D 1 336 ILE 336 358 358 ILE ILE D . n 
D 1 337 PRO 337 359 359 PRO PRO D . n 
D 1 338 ARG 338 360 360 ARG ARG D . n 
D 1 339 GLU 339 361 361 GLU GLU D . n 
D 1 340 ALA 340 362 362 ALA ALA D . n 
D 1 341 ILE 341 363 363 ILE ILE D . n 
D 1 342 PRO 342 364 364 PRO PRO D . n 
D 1 343 PRO 343 365 365 PRO PRO D . n 
D 1 344 LEU 344 366 366 LEU LEU D . n 
D 1 345 ASP 345 367 367 ASP ASP D . n 
D 1 346 GLU 346 368 368 GLU GLU D . n 
D 1 347 THR 347 369 ?   ?   ?   D . n 
D 1 348 ILE 348 370 ?   ?   ?   D . n 
D 1 349 ARG 349 371 ?   ?   ?   D . n 
D 1 350 LYS 350 372 ?   ?   ?   D . n 
D 1 351 LYS 351 373 ?   ?   ?   D . n 
D 1 352 LEU 352 374 ?   ?   ?   D . n 
D 1 353 ILE 353 375 ?   ?   ?   D . n 
D 1 354 ASN 354 376 ?   ?   ?   D . n 
D 1 355 LYS 355 377 ?   ?   ?   D . n 
D 1 356 SER 356 378 ?   ?   ?   D . n 
D 1 357 VAL 357 379 ?   ?   ?   D . n 
D 1 358 LEU 358 380 ?   ?   ?   D . n 
D 1 359 GLU 359 381 ?   ?   ?   D . n 
D 1 360 HIS 360 382 ?   ?   ?   D . n 
D 1 361 HIS 361 383 ?   ?   ?   D . n 
D 1 362 HIS 362 384 ?   ?   ?   D . n 
D 1 363 HIS 363 385 ?   ?   ?   D . n 
D 1 364 HIS 364 386 ?   ?   ?   D . n 
D 1 365 HIS 365 387 ?   ?   ?   D . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1H6U 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1H6U 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 2 HEM   1 401 401 HEM   HEM A . 
F 3 A1H6U 1 402 1   A1H6U LIG A . 
G 2 HEM   1 401 401 HEM   HEM B . 
H 3 A1H6U 1 402 1   A1H6U LIG B . 
I 2 HEM   1 401 401 HEM   HEM C . 
J 3 A1H6U 1 402 1   A1H6U LIG C . 
K 2 HEM   1 401 401 HEM   HEM D . 
L 3 A1H6U 1 402 1   A1H6U LIG D . 
M 4 HOH   1 501 7   HOH   HOH A . 
M 4 HOH   2 502 4   HOH   HOH A . 
M 4 HOH   3 503 13  HOH   HOH A . 
N 4 HOH   1 501 2   HOH   HOH B . 
O 4 HOH   1 501 12  HOH   HOH D . 
O 4 HOH   2 502 1   HOH   HOH D . 
# 
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 B VAL 166 ? CG1 ? B VAL 144 CG1 
2  1 Y 1 B VAL 166 ? CG2 ? B VAL 144 CG2 
3  1 Y 1 B PHE 167 ? CG  ? B PHE 145 CG  
4  1 Y 1 B PHE 167 ? CD1 ? B PHE 145 CD1 
5  1 Y 1 B PHE 167 ? CD2 ? B PHE 145 CD2 
6  1 Y 1 B PHE 167 ? CE1 ? B PHE 145 CE1 
7  1 Y 1 B PHE 167 ? CE2 ? B PHE 145 CE2 
8  1 Y 1 B PHE 167 ? CZ  ? B PHE 145 CZ  
9  1 Y 1 B SER 168 ? OG  ? B SER 146 OG  
10 1 Y 1 B ASP 169 ? CG  ? B ASP 147 CG  
11 1 Y 1 B ASP 169 ? OD1 ? B ASP 147 OD1 
12 1 Y 1 B ASP 169 ? OD2 ? B ASP 147 OD2 
13 1 Y 1 C GLU 154 ? CG  ? C GLU 132 CG  
14 1 Y 1 C GLU 154 ? CD  ? C GLU 132 CD  
15 1 Y 1 C GLU 154 ? OE1 ? C GLU 132 OE1 
16 1 Y 1 C GLU 154 ? OE2 ? C GLU 132 OE2 
17 1 Y 1 C SER 168 ? OG  ? C SER 146 OG  
18 1 Y 1 D ARG 156 ? CG  ? D ARG 134 CG  
19 1 Y 1 D ARG 156 ? CD  ? D ARG 134 CD  
20 1 Y 1 D ARG 156 ? NE  ? D ARG 134 NE  
21 1 Y 1 D ARG 156 ? CZ  ? D ARG 134 CZ  
22 1 Y 1 D ARG 156 ? NH1 ? D ARG 134 NH1 
23 1 Y 1 D ARG 156 ? NH2 ? D ARG 134 NH2 
24 1 Y 1 D VAL 157 ? CG1 ? D VAL 135 CG1 
25 1 Y 1 D VAL 157 ? CG2 ? D VAL 135 CG2 
26 1 Y 1 D ARG 158 ? CG  ? D ARG 136 CG  
27 1 Y 1 D ARG 158 ? CD  ? D ARG 136 CD  
28 1 Y 1 D ARG 158 ? NE  ? D ARG 136 NE  
29 1 Y 1 D ARG 158 ? CZ  ? D ARG 136 CZ  
30 1 Y 1 D ARG 158 ? NH1 ? D ARG 136 NH1 
31 1 Y 1 D ARG 158 ? NH2 ? D ARG 136 NH2 
32 1 Y 1 D VAL 166 ? CG1 ? D VAL 144 CG1 
33 1 Y 1 D VAL 166 ? CG2 ? D VAL 144 CG2 
34 1 Y 1 D PHE 167 ? CG  ? D PHE 145 CG  
35 1 Y 1 D PHE 167 ? CD1 ? D PHE 145 CD1 
36 1 Y 1 D PHE 167 ? CD2 ? D PHE 145 CD2 
37 1 Y 1 D PHE 167 ? CE1 ? D PHE 145 CE1 
38 1 Y 1 D PHE 167 ? CE2 ? D PHE 145 CE2 
39 1 Y 1 D PHE 167 ? CZ  ? D PHE 145 CZ  
40 1 Y 1 D SER 168 ? OG  ? D SER 146 OG  
41 1 Y 1 D ASP 169 ? CG  ? D ASP 147 CG  
42 1 Y 1 D ASP 169 ? OD1 ? D ASP 147 OD1 
43 1 Y 1 D ASP 169 ? OD2 ? D ASP 147 OD2 
# 
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                  120 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9ESF 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     143.773 
_cell.length_a_esd                 ? 
_cell.length_b                     143.773 
_cell.length_b_esd                 ? 
_cell.length_c                     141.864 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        24 
_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                         9ESF 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                173 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 63' 
_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                   9ESF 
_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             2.44 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.66 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;100mM Na Citrate pH 5.50
18% PEG 3350
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 2M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2016-04-05 
_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                                       9ESF 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.50 
_reflns.d_resolution_low                               47.06 
_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                                     57451 
_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                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          4.92 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.57 
_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                                   .985 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.50 
_reflns_shell.d_res_low                                     2.65 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.62 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             9218 
_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                               4.48 
_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                                  .179 
_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]                            -4.4117 
_refine.aniso_B[1][2]                            0 
_refine.aniso_B[1][3]                            0 
_refine.aniso_B[2][2]                            -4.4117 
_refine.aniso_B[2][3]                            0 
_refine.aniso_B[3][3]                            8.8234 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               54.49 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.929 
_refine.correlation_coeff_Fo_to_Fc_free          0.908 
_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                                 9ESF 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.501 
_refine.ls_d_res_low                             47.06 
_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                     57388 
_refine.ls_number_reflns_R_free                  2870 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.9 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2466 
_refine.ls_R_factor_R_free                       0.2737 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2452 
_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   0.301 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.287 
_refine.pdbx_overall_SU_R_Blow_DPI               0.499 
_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             0.573 
_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                        9ESF 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.42 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.501 
_refine_hist.d_res_low                        47.06 
_refine_hist.number_atoms_solvent             6 
_refine_hist.number_atoms_total               11154 
_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        10908 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         240 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.007 ? 11408 ? t_bond_d                  2  HARMONIC     
'X-RAY DIFFRACTION' ? 0.8   ? 15402 ? t_angle_deg               2  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 4228  ? t_dihedral_angle_d        2  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? 2041  ? t_gen_planes              5  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 11408 ? t_it                      10 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 1409  ? t_chiral_improper_torsion 5  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? 8334  ? t_ideal_dist_contact      4  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? 2.41  ? ?     ? t_omega_torsion           ?  ?            
'X-RAY DIFFRACTION' ? 17.49 ? ?     ? t_other_torsion           ?  ?            
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.501 
_refine_ls_shell.d_res_low                        2.52 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             58 
_refine_ls_shell.number_reflns_R_work             ? 
_refine_ls_shell.percent_reflns_obs               96.57 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.3965 
_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                  0.4656 
# 
_struct.entry_id                     9ESF 
_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        9ESF 
_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 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 3 ? 
G N N 2 ? 
H N N 3 ? 
I N N 2 ? 
J N N 3 ? 
K N N 2 ? 
L N N 3 ? 
M N N 4 ? 
N N N 4 ? 
O N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    T23O_DROME 
_struct_ref.pdbx_db_accession          P20351 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;GKIYGEYLMLDKLLDAQCMLSEEDKRPVHDEHLFIITHQAYELWFKQIIFEFDSIRDMLDAEVIDETKTLEIVKRLNRVV
LILKLLVDQVPILETMTPLDFMDFRKYLAPASGFQSLQFRLIENKLGVLTEQRVRYNQKYSDVFSDEEARNSIRNSEKDP
SLLELVQRWLERTPGLEESGFNFWAKFQESVDRFLEAQVQSAMEEPVEKAKNYRLMDIEKRREVYRSIFDPAVHDALVRR
GDRRFSHRALQGAIMITFYRDEPRFSQPHQLLTLLMDIDSLITKWRYNHVIMVQRMIGSQQLGTGGSSGYQYLRSTLSDR
YKVFLDLFNLSTFLIPREAIPPLDETIRKKLINKSV
;
_struct_ref.pdbx_align_begin           24 
# 
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 9ESF A 2 ? 357 ? P20351 24 ? 379 ? 24 379 
2 1 9ESF B 2 ? 357 ? P20351 24 ? 379 ? 24 379 
3 1 9ESF C 2 ? 357 ? P20351 24 ? 379 ? 24 379 
4 1 9ESF D 2 ? 357 ? P20351 24 ? 379 ? 24 379 
# 
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 9ESF MET A 1   ? UNP P20351 ? ? 'initiating methionine' 23  1  
1 9ESF LEU A 358 ? UNP P20351 ? ? 'expression tag'        380 2  
1 9ESF GLU A 359 ? UNP P20351 ? ? 'expression tag'        381 3  
1 9ESF HIS A 360 ? UNP P20351 ? ? 'expression tag'        382 4  
1 9ESF HIS A 361 ? UNP P20351 ? ? 'expression tag'        383 5  
1 9ESF HIS A 362 ? UNP P20351 ? ? 'expression tag'        384 6  
1 9ESF HIS A 363 ? UNP P20351 ? ? 'expression tag'        385 7  
1 9ESF HIS A 364 ? UNP P20351 ? ? 'expression tag'        386 8  
1 9ESF HIS A 365 ? UNP P20351 ? ? 'expression tag'        387 9  
2 9ESF MET B 1   ? UNP P20351 ? ? 'initiating methionine' 23  10 
2 9ESF LEU B 358 ? UNP P20351 ? ? 'expression tag'        380 11 
2 9ESF GLU B 359 ? UNP P20351 ? ? 'expression tag'        381 12 
2 9ESF HIS B 360 ? UNP P20351 ? ? 'expression tag'        382 13 
2 9ESF HIS B 361 ? UNP P20351 ? ? 'expression tag'        383 14 
2 9ESF HIS B 362 ? UNP P20351 ? ? 'expression tag'        384 15 
2 9ESF HIS B 363 ? UNP P20351 ? ? 'expression tag'        385 16 
2 9ESF HIS B 364 ? UNP P20351 ? ? 'expression tag'        386 17 
2 9ESF HIS B 365 ? UNP P20351 ? ? 'expression tag'        387 18 
3 9ESF MET C 1   ? UNP P20351 ? ? 'initiating methionine' 23  19 
3 9ESF LEU C 358 ? UNP P20351 ? ? 'expression tag'        380 20 
3 9ESF GLU C 359 ? UNP P20351 ? ? 'expression tag'        381 21 
3 9ESF HIS C 360 ? UNP P20351 ? ? 'expression tag'        382 22 
3 9ESF HIS C 361 ? UNP P20351 ? ? 'expression tag'        383 23 
3 9ESF HIS C 362 ? UNP P20351 ? ? 'expression tag'        384 24 
3 9ESF HIS C 363 ? UNP P20351 ? ? 'expression tag'        385 25 
3 9ESF HIS C 364 ? UNP P20351 ? ? 'expression tag'        386 26 
3 9ESF HIS C 365 ? UNP P20351 ? ? 'expression tag'        387 27 
4 9ESF MET D 1   ? UNP P20351 ? ? 'initiating methionine' 23  28 
4 9ESF LEU D 358 ? UNP P20351 ? ? 'expression tag'        380 29 
4 9ESF GLU D 359 ? UNP P20351 ? ? 'expression tag'        381 30 
4 9ESF HIS D 360 ? UNP P20351 ? ? 'expression tag'        382 31 
4 9ESF HIS D 361 ? UNP P20351 ? ? 'expression tag'        383 32 
4 9ESF HIS D 362 ? UNP P20351 ? ? 'expression tag'        384 33 
4 9ESF HIS D 363 ? UNP P20351 ? ? 'expression tag'        385 34 
4 9ESF HIS D 364 ? UNP P20351 ? ? 'expression tag'        386 35 
4 9ESF HIS D 365 ? UNP P20351 ? ? 'expression tag'        387 36 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
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)' 25920 ? 
1 MORE         -193  ? 
1 'SSA (A^2)'  53590 ? 
# 
_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,I,J,K,L,M,N,O 
# 
_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 ILE A 4   ? LEU A 9   ? ILE A 26  LEU A 31  1 ? 6  
HELX_P HELX_P2  AA2 MET A 10  ? LEU A 15  ? MET A 32  LEU A 37  1 ? 6  
HELX_P HELX_P3  AA3 MET A 20  ? ASP A 25  ? MET A 42  ASP A 47  1 ? 6  
HELX_P HELX_P4  AA4 ASP A 31  ? ASP A 61  ? ASP A 53  ASP A 83  1 ? 31 
HELX_P HELX_P5  AA5 ASP A 66  ? ASP A 89  ? ASP A 88  ASP A 111 1 ? 24 
HELX_P HELX_P6  AA6 GLN A 90  ? GLU A 95  ? GLN A 112 GLU A 117 1 ? 6  
HELX_P HELX_P7  AA7 THR A 98  ? ASP A 104 ? THR A 120 ASP A 126 1 ? 7  
HELX_P HELX_P8  AA8 PHE A 105 ? LEU A 109 ? PHE A 127 LEU A 131 5 ? 5  
HELX_P HELX_P9  AA9 SER A 117 ? GLY A 128 ? SER A 139 GLY A 150 1 ? 12 
HELX_P HELX_P10 AB1 GLU A 149 ? ASP A 160 ? GLU A 171 ASP A 182 1 ? 12 
HELX_P HELX_P11 AB2 SER A 162 ? ARG A 173 ? SER A 184 ARG A 195 1 ? 12 
HELX_P HELX_P12 AB3 ASN A 183 ? GLU A 205 ? ASN A 205 GLU A 227 1 ? 23 
HELX_P HELX_P13 AB4 VAL A 208 ? ASP A 231 ? VAL A 230 ASP A 253 1 ? 24 
HELX_P HELX_P14 AB5 ASP A 231 ? ARG A 241 ? ASP A 253 ARG A 263 1 ? 11 
HELX_P HELX_P15 AB6 SER A 247 ? TYR A 260 ? SER A 269 TYR A 282 1 ? 14 
HELX_P HELX_P16 AB7 GLU A 263 ? GLY A 299 ? GLU A 285 GLY A 321 1 ? 37 
HELX_P HELX_P17 AB8 SER A 308 ? THR A 317 ? SER A 330 THR A 339 1 ? 10 
HELX_P HELX_P18 AB9 LEU A 318 ? LYS A 323 ? LEU A 340 LYS A 345 5 ? 6  
HELX_P HELX_P19 AC1 PHE A 325 ? LEU A 331 ? PHE A 347 LEU A 353 1 ? 7  
HELX_P HELX_P20 AC2 SER A 332 ? LEU A 335 ? SER A 354 LEU A 357 5 ? 4  
HELX_P HELX_P21 AC3 ILE B 4   ? LEU B 9   ? ILE B 26  LEU B 31  1 ? 6  
HELX_P HELX_P22 AC4 MET B 10  ? LEU B 15  ? MET B 32  LEU B 37  1 ? 6  
HELX_P HELX_P23 AC5 MET B 20  ? ASP B 25  ? MET B 42  ASP B 47  1 ? 6  
HELX_P HELX_P24 AC6 ASP B 31  ? ASP B 61  ? ASP B 53  ASP B 83  1 ? 31 
HELX_P HELX_P25 AC7 ASP B 66  ? ASP B 89  ? ASP B 88  ASP B 111 1 ? 24 
HELX_P HELX_P26 AC8 GLN B 90  ? GLU B 95  ? GLN B 112 GLU B 117 1 ? 6  
HELX_P HELX_P27 AC9 THR B 98  ? ASP B 104 ? THR B 120 ASP B 126 1 ? 7  
HELX_P HELX_P28 AD1 PHE B 105 ? LEU B 109 ? PHE B 127 LEU B 131 5 ? 5  
HELX_P HELX_P29 AD2 SER B 117 ? GLY B 128 ? SER B 139 GLY B 150 1 ? 12 
HELX_P HELX_P30 AD3 ASP B 147 ? ASP B 160 ? ASP B 169 ASP B 182 1 ? 14 
HELX_P HELX_P31 AD4 SER B 162 ? ARG B 173 ? SER B 184 ARG B 195 1 ? 12 
HELX_P HELX_P32 AD5 ASN B 183 ? GLU B 205 ? ASN B 205 GLU B 227 1 ? 23 
HELX_P HELX_P33 AD6 VAL B 208 ? ASP B 231 ? VAL B 230 ASP B 253 1 ? 24 
HELX_P HELX_P34 AD7 ASP B 231 ? ARG B 241 ? ASP B 253 ARG B 263 1 ? 11 
HELX_P HELX_P35 AD8 SER B 247 ? TYR B 260 ? SER B 269 TYR B 282 1 ? 14 
HELX_P HELX_P36 AD9 GLU B 263 ? GLY B 299 ? GLU B 285 GLY B 321 1 ? 37 
HELX_P HELX_P37 AE1 SER B 308 ? THR B 317 ? SER B 330 THR B 339 1 ? 10 
HELX_P HELX_P38 AE2 LEU B 318 ? LYS B 323 ? LEU B 340 LYS B 345 5 ? 6  
HELX_P HELX_P39 AE3 PHE B 325 ? LEU B 331 ? PHE B 347 LEU B 353 1 ? 7  
HELX_P HELX_P40 AE4 SER B 332 ? LEU B 335 ? SER B 354 LEU B 357 5 ? 4  
HELX_P HELX_P41 AE5 TYR C 5   ? LEU C 9   ? TYR C 27  LEU C 31  1 ? 5  
HELX_P HELX_P42 AE6 MET C 10  ? LEU C 15  ? MET C 32  LEU C 37  1 ? 6  
HELX_P HELX_P43 AE7 MET C 20  ? ASP C 25  ? MET C 42  ASP C 47  1 ? 6  
HELX_P HELX_P44 AE8 ASP C 31  ? ASP C 61  ? ASP C 53  ASP C 83  1 ? 31 
HELX_P HELX_P45 AE9 ASP C 66  ? ASP C 89  ? ASP C 88  ASP C 111 1 ? 24 
HELX_P HELX_P46 AF1 GLN C 90  ? GLU C 95  ? GLN C 112 GLU C 117 1 ? 6  
HELX_P HELX_P47 AF2 THR C 98  ? ASP C 104 ? THR C 120 ASP C 126 1 ? 7  
HELX_P HELX_P48 AF3 PHE C 105 ? LEU C 109 ? PHE C 127 LEU C 131 5 ? 5  
HELX_P HELX_P49 AF4 SER C 117 ? GLY C 128 ? SER C 139 GLY C 150 1 ? 12 
HELX_P HELX_P50 AF5 ASP C 147 ? ASP C 160 ? ASP C 169 ASP C 182 1 ? 14 
HELX_P HELX_P51 AF6 SER C 162 ? ARG C 173 ? SER C 184 ARG C 195 1 ? 12 
HELX_P HELX_P52 AF7 ASN C 183 ? GLU C 205 ? ASN C 205 GLU C 227 1 ? 23 
HELX_P HELX_P53 AF8 VAL C 208 ? ASP C 231 ? VAL C 230 ASP C 253 1 ? 24 
HELX_P HELX_P54 AF9 ASP C 231 ? ARG C 241 ? ASP C 253 ARG C 263 1 ? 11 
HELX_P HELX_P55 AG1 SER C 247 ? TYR C 260 ? SER C 269 TYR C 282 1 ? 14 
HELX_P HELX_P56 AG2 GLU C 263 ? ILE C 298 ? GLU C 285 ILE C 320 1 ? 36 
HELX_P HELX_P57 AG3 SER C 308 ? THR C 317 ? SER C 330 THR C 339 1 ? 10 
HELX_P HELX_P58 AG4 LEU C 318 ? LYS C 323 ? LEU C 340 LYS C 345 5 ? 6  
HELX_P HELX_P59 AG5 PHE C 325 ? LEU C 331 ? PHE C 347 LEU C 353 1 ? 7  
HELX_P HELX_P60 AG6 SER C 332 ? LEU C 335 ? SER C 354 LEU C 357 5 ? 4  
HELX_P HELX_P61 AG7 ILE D 4   ? LEU D 9   ? ILE D 26  LEU D 31  1 ? 6  
HELX_P HELX_P62 AG8 MET D 10  ? LEU D 15  ? MET D 32  LEU D 37  1 ? 6  
HELX_P HELX_P63 AG9 MET D 20  ? ASP D 25  ? MET D 42  ASP D 47  1 ? 6  
HELX_P HELX_P64 AH1 ASP D 31  ? ASP D 61  ? ASP D 53  ASP D 83  1 ? 31 
HELX_P HELX_P65 AH2 ASP D 66  ? ASP D 89  ? ASP D 88  ASP D 111 1 ? 24 
HELX_P HELX_P66 AH3 GLN D 90  ? GLU D 95  ? GLN D 112 GLU D 117 1 ? 6  
HELX_P HELX_P67 AH4 THR D 98  ? ASP D 104 ? THR D 120 ASP D 126 1 ? 7  
HELX_P HELX_P68 AH5 PHE D 105 ? LEU D 109 ? PHE D 127 LEU D 131 5 ? 5  
HELX_P HELX_P69 AH6 SER D 117 ? GLY D 128 ? SER D 139 GLY D 150 1 ? 12 
HELX_P HELX_P70 AH7 LEU D 130 ? ARG D 134 ? LEU D 152 ARG D 156 5 ? 5  
HELX_P HELX_P71 AH8 ASP D 147 ? ASP D 160 ? ASP D 169 ASP D 182 1 ? 14 
HELX_P HELX_P72 AH9 SER D 162 ? ARG D 173 ? SER D 184 ARG D 195 1 ? 12 
HELX_P HELX_P73 AI1 ASN D 183 ? GLU D 205 ? ASN D 205 GLU D 227 1 ? 23 
HELX_P HELX_P74 AI2 VAL D 208 ? ASP D 231 ? VAL D 230 ASP D 253 1 ? 24 
HELX_P HELX_P75 AI3 ASP D 231 ? ARG D 241 ? ASP D 253 ARG D 263 1 ? 11 
HELX_P HELX_P76 AI4 SER D 247 ? TYR D 260 ? SER D 269 TYR D 282 1 ? 14 
HELX_P HELX_P77 AI5 GLU D 263 ? GLY D 299 ? GLU D 285 GLY D 321 1 ? 37 
HELX_P HELX_P78 AI6 SER D 308 ? THR D 317 ? SER D 330 THR D 339 1 ? 10 
HELX_P HELX_P79 AI7 LEU D 318 ? LYS D 323 ? LEU D 340 LYS D 345 5 ? 6  
HELX_P HELX_P80 AI8 PHE D 325 ? LEU D 331 ? PHE D 347 LEU D 353 1 ? 7  
HELX_P HELX_P81 AI9 SER D 332 ? LEU D 335 ? SER D 354 LEU D 357 5 ? 4  
HELX_P HELX_P82 AJ1 PRO D 337 ? ILE D 341 ? PRO D 359 ILE D 363 5 ? 5  
# 
_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 
metalc1 metalc ? ? A HIS 290 NE2 ? ? ? 1_555 E HEM   . FE ? ? A HIS 312 A HEM   401 1_555 ? ? ? ? ? ? ? 2.117 ? ? 
metalc2 metalc ? ? E HEM .   FE  ? ? ? 1_555 F A1H6U . N2 ? ? A HEM 401 A A1H6U 402 1_555 ? ? ? ? ? ? ? 2.073 ? ? 
metalc3 metalc ? ? B HIS 290 NE2 ? ? ? 1_555 G HEM   . FE ? ? B HIS 312 B HEM   401 1_555 ? ? ? ? ? ? ? 2.133 ? ? 
metalc4 metalc ? ? G HEM .   FE  ? ? ? 1_555 H A1H6U . N2 ? ? B HEM 401 B A1H6U 402 1_555 ? ? ? ? ? ? ? 2.106 ? ? 
metalc5 metalc ? ? C HIS 290 NE2 ? ? ? 1_555 I HEM   . FE ? ? C HIS 312 C HEM   401 1_555 ? ? ? ? ? ? ? 2.154 ? ? 
metalc6 metalc ? ? I HEM .   FE  ? ? ? 1_555 J A1H6U . N2 ? ? C HEM 401 C A1H6U 402 1_555 ? ? ? ? ? ? ? 2.222 ? ? 
metalc7 metalc ? ? D HIS 290 NE2 ? ? ? 1_555 K HEM   . FE ? ? D HIS 312 D HEM   401 1_555 ? ? ? ? ? ? ? 2.107 ? ? 
metalc8 metalc ? ? K HEM .   FE  ? ? ? 1_555 L A1H6U . N2 ? ? D HEM 401 D A1H6U 402 1_555 ? ? ? ? ? ? ? 2.141 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
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 290 ? A HIS 312 ? 1_555 FE ? E HEM . ? A HEM 401 ? 1_555 NA ? E HEM   . ? A HEM   401 ? 1_555 100.6 ? 
2  NE2 ? A HIS 290 ? A HIS 312 ? 1_555 FE ? E HEM . ? A HEM 401 ? 1_555 NB ? E HEM   . ? A HEM   401 ? 1_555 94.2  ? 
3  NA  ? E HEM .   ? A HEM 401 ? 1_555 FE ? E HEM . ? A HEM 401 ? 1_555 NB ? E HEM   . ? A HEM   401 ? 1_555 91.2  ? 
4  NE2 ? A HIS 290 ? A HIS 312 ? 1_555 FE ? E HEM . ? A HEM 401 ? 1_555 NC ? E HEM   . ? A HEM   401 ? 1_555 86.2  ? 
5  NA  ? E HEM .   ? A HEM 401 ? 1_555 FE ? E HEM . ? A HEM 401 ? 1_555 NC ? E HEM   . ? A HEM   401 ? 1_555 173.2 ? 
6  NB  ? E HEM .   ? A HEM 401 ? 1_555 FE ? E HEM . ? A HEM 401 ? 1_555 NC ? E HEM   . ? A HEM   401 ? 1_555 88.3  ? 
7  NE2 ? A HIS 290 ? A HIS 312 ? 1_555 FE ? E HEM . ? A HEM 401 ? 1_555 ND ? E HEM   . ? A HEM   401 ? 1_555 96.7  ? 
8  NA  ? E HEM .   ? A HEM 401 ? 1_555 FE ? E HEM . ? A HEM 401 ? 1_555 ND ? E HEM   . ? A HEM   401 ? 1_555 89.0  ? 
9  NB  ? E HEM .   ? A HEM 401 ? 1_555 FE ? E HEM . ? A HEM 401 ? 1_555 ND ? E HEM   . ? A HEM   401 ? 1_555 168.9 ? 
10 NC  ? E HEM .   ? A HEM 401 ? 1_555 FE ? E HEM . ? A HEM 401 ? 1_555 ND ? E HEM   . ? A HEM   401 ? 1_555 90.1  ? 
11 NE2 ? A HIS 290 ? A HIS 312 ? 1_555 FE ? E HEM . ? A HEM 401 ? 1_555 N2 ? F A1H6U . ? A A1H6U 402 ? 1_555 168.6 ? 
12 NA  ? E HEM .   ? A HEM 401 ? 1_555 FE ? E HEM . ? A HEM 401 ? 1_555 N2 ? F A1H6U . ? A A1H6U 402 ? 1_555 90.3  ? 
13 NB  ? E HEM .   ? A HEM 401 ? 1_555 FE ? E HEM . ? A HEM 401 ? 1_555 N2 ? F A1H6U . ? A A1H6U 402 ? 1_555 88.6  ? 
14 NC  ? E HEM .   ? A HEM 401 ? 1_555 FE ? E HEM . ? A HEM 401 ? 1_555 N2 ? F A1H6U . ? A A1H6U 402 ? 1_555 82.9  ? 
15 ND  ? E HEM .   ? A HEM 401 ? 1_555 FE ? E HEM . ? A HEM 401 ? 1_555 N2 ? F A1H6U . ? A A1H6U 402 ? 1_555 80.3  ? 
16 NE2 ? B HIS 290 ? B HIS 312 ? 1_555 FE ? G HEM . ? B HEM 401 ? 1_555 NA ? G HEM   . ? B HEM   401 ? 1_555 100.1 ? 
17 NE2 ? B HIS 290 ? B HIS 312 ? 1_555 FE ? G HEM . ? B HEM 401 ? 1_555 NB ? G HEM   . ? B HEM   401 ? 1_555 92.3  ? 
18 NA  ? G HEM .   ? B HEM 401 ? 1_555 FE ? G HEM . ? B HEM 401 ? 1_555 NB ? G HEM   . ? B HEM   401 ? 1_555 90.9  ? 
19 NE2 ? B HIS 290 ? B HIS 312 ? 1_555 FE ? G HEM . ? B HEM 401 ? 1_555 NC ? G HEM   . ? B HEM   401 ? 1_555 86.8  ? 
20 NA  ? G HEM .   ? B HEM 401 ? 1_555 FE ? G HEM . ? B HEM 401 ? 1_555 NC ? G HEM   . ? B HEM   401 ? 1_555 173.1 ? 
21 NB  ? G HEM .   ? B HEM 401 ? 1_555 FE ? G HEM . ? B HEM 401 ? 1_555 NC ? G HEM   . ? B HEM   401 ? 1_555 88.7  ? 
22 NE2 ? B HIS 290 ? B HIS 312 ? 1_555 FE ? G HEM . ? B HEM 401 ? 1_555 ND ? G HEM   . ? B HEM   401 ? 1_555 96.7  ? 
23 NA  ? G HEM .   ? B HEM 401 ? 1_555 FE ? G HEM . ? B HEM 401 ? 1_555 ND ? G HEM   . ? B HEM   401 ? 1_555 89.2  ? 
24 NB  ? G HEM .   ? B HEM 401 ? 1_555 FE ? G HEM . ? B HEM 401 ? 1_555 ND ? G HEM   . ? B HEM   401 ? 1_555 170.8 ? 
25 NC  ? G HEM .   ? B HEM 401 ? 1_555 FE ? G HEM . ? B HEM 401 ? 1_555 ND ? G HEM   . ? B HEM   401 ? 1_555 90.1  ? 
26 NE2 ? B HIS 290 ? B HIS 312 ? 1_555 FE ? G HEM . ? B HEM 401 ? 1_555 N2 ? H A1H6U . ? B A1H6U 402 ? 1_555 170.3 ? 
27 NA  ? G HEM .   ? B HEM 401 ? 1_555 FE ? G HEM . ? B HEM 401 ? 1_555 N2 ? H A1H6U . ? B A1H6U 402 ? 1_555 88.2  ? 
28 NB  ? G HEM .   ? B HEM 401 ? 1_555 FE ? G HEM . ? B HEM 401 ? 1_555 N2 ? H A1H6U . ? B A1H6U 402 ? 1_555 82.6  ? 
29 NC  ? G HEM .   ? B HEM 401 ? 1_555 FE ? G HEM . ? B HEM 401 ? 1_555 N2 ? H A1H6U . ? B A1H6U 402 ? 1_555 84.9  ? 
30 ND  ? G HEM .   ? B HEM 401 ? 1_555 FE ? G HEM . ? B HEM 401 ? 1_555 N2 ? H A1H6U . ? B A1H6U 402 ? 1_555 88.2  ? 
31 NE2 ? C HIS 290 ? C HIS 312 ? 1_555 FE ? I HEM . ? C HEM 401 ? 1_555 NA ? I HEM   . ? C HEM   401 ? 1_555 98.6  ? 
32 NE2 ? C HIS 290 ? C HIS 312 ? 1_555 FE ? I HEM . ? C HEM 401 ? 1_555 NB ? I HEM   . ? C HEM   401 ? 1_555 93.3  ? 
33 NA  ? I HEM .   ? C HEM 401 ? 1_555 FE ? I HEM . ? C HEM 401 ? 1_555 NB ? I HEM   . ? C HEM   401 ? 1_555 90.0  ? 
34 NE2 ? C HIS 290 ? C HIS 312 ? 1_555 FE ? I HEM . ? C HEM 401 ? 1_555 NC ? I HEM   . ? C HEM   401 ? 1_555 86.2  ? 
35 NA  ? I HEM .   ? C HEM 401 ? 1_555 FE ? I HEM . ? C HEM 401 ? 1_555 NC ? I HEM   . ? C HEM   401 ? 1_555 175.1 ? 
36 NB  ? I HEM .   ? C HEM 401 ? 1_555 FE ? I HEM . ? C HEM 401 ? 1_555 NC ? I HEM   . ? C HEM   401 ? 1_555 89.0  ? 
37 NE2 ? C HIS 290 ? C HIS 312 ? 1_555 FE ? I HEM . ? C HEM 401 ? 1_555 ND ? I HEM   . ? C HEM   401 ? 1_555 96.3  ? 
38 NA  ? I HEM .   ? C HEM 401 ? 1_555 FE ? I HEM . ? C HEM 401 ? 1_555 ND ? I HEM   . ? C HEM   401 ? 1_555 89.9  ? 
39 NB  ? I HEM .   ? C HEM 401 ? 1_555 FE ? I HEM . ? C HEM 401 ? 1_555 ND ? I HEM   . ? C HEM   401 ? 1_555 170.4 ? 
40 NC  ? I HEM .   ? C HEM 401 ? 1_555 FE ? I HEM . ? C HEM 401 ? 1_555 ND ? I HEM   . ? C HEM   401 ? 1_555 90.3  ? 
41 NE2 ? C HIS 290 ? C HIS 312 ? 1_555 FE ? I HEM . ? C HEM 401 ? 1_555 N2 ? J A1H6U . ? C A1H6U 402 ? 1_555 173.6 ? 
42 NA  ? I HEM .   ? C HEM 401 ? 1_555 FE ? I HEM . ? C HEM 401 ? 1_555 N2 ? J A1H6U . ? C A1H6U 402 ? 1_555 87.7  ? 
43 NB  ? I HEM .   ? C HEM 401 ? 1_555 FE ? I HEM . ? C HEM 401 ? 1_555 N2 ? J A1H6U . ? C A1H6U 402 ? 1_555 85.6  ? 
44 NC  ? I HEM .   ? C HEM 401 ? 1_555 FE ? I HEM . ? C HEM 401 ? 1_555 N2 ? J A1H6U . ? C A1H6U 402 ? 1_555 87.5  ? 
45 ND  ? I HEM .   ? C HEM 401 ? 1_555 FE ? I HEM . ? C HEM 401 ? 1_555 N2 ? J A1H6U . ? C A1H6U 402 ? 1_555 84.8  ? 
46 NE2 ? D HIS 290 ? D HIS 312 ? 1_555 FE ? K HEM . ? D HEM 401 ? 1_555 NA ? K HEM   . ? D HEM   401 ? 1_555 100.0 ? 
47 NE2 ? D HIS 290 ? D HIS 312 ? 1_555 FE ? K HEM . ? D HEM 401 ? 1_555 NB ? K HEM   . ? D HEM   401 ? 1_555 93.6  ? 
48 NA  ? K HEM .   ? D HEM 401 ? 1_555 FE ? K HEM . ? D HEM 401 ? 1_555 NB ? K HEM   . ? D HEM   401 ? 1_555 89.9  ? 
49 NE2 ? D HIS 290 ? D HIS 312 ? 1_555 FE ? K HEM . ? D HEM 401 ? 1_555 NC ? K HEM   . ? D HEM   401 ? 1_555 86.8  ? 
50 NA  ? K HEM .   ? D HEM 401 ? 1_555 FE ? K HEM . ? D HEM 401 ? 1_555 NC ? K HEM   . ? D HEM   401 ? 1_555 173.1 ? 
51 NB  ? K HEM .   ? D HEM 401 ? 1_555 FE ? K HEM . ? D HEM 401 ? 1_555 NC ? K HEM   . ? D HEM   401 ? 1_555 88.9  ? 
52 NE2 ? D HIS 290 ? D HIS 312 ? 1_555 FE ? K HEM . ? D HEM 401 ? 1_555 ND ? K HEM   . ? D HEM   401 ? 1_555 97.0  ? 
53 NA  ? K HEM .   ? D HEM 401 ? 1_555 FE ? K HEM . ? D HEM 401 ? 1_555 ND ? K HEM   . ? D HEM   401 ? 1_555 89.0  ? 
54 NB  ? K HEM .   ? D HEM 401 ? 1_555 FE ? K HEM . ? D HEM 401 ? 1_555 ND ? K HEM   . ? D HEM   401 ? 1_555 169.4 ? 
55 NC  ? K HEM .   ? D HEM 401 ? 1_555 FE ? K HEM . ? D HEM 401 ? 1_555 ND ? K HEM   . ? D HEM   401 ? 1_555 91.0  ? 
56 NE2 ? D HIS 290 ? D HIS 312 ? 1_555 FE ? K HEM . ? D HEM 401 ? 1_555 N2 ? L A1H6U . ? D A1H6U 402 ? 1_555 170.2 ? 
57 NA  ? K HEM .   ? D HEM 401 ? 1_555 FE ? K HEM . ? D HEM 401 ? 1_555 N2 ? L A1H6U . ? D A1H6U 402 ? 1_555 88.6  ? 
58 NB  ? K HEM .   ? D HEM 401 ? 1_555 FE ? K HEM . ? D HEM 401 ? 1_555 N2 ? L A1H6U . ? D A1H6U 402 ? 1_555 81.8  ? 
59 NC  ? K HEM .   ? D HEM 401 ? 1_555 FE ? K HEM . ? D HEM 401 ? 1_555 N2 ? L A1H6U . ? D A1H6U 402 ? 1_555 84.4  ? 
60 ND  ? K HEM .   ? D HEM 401 ? 1_555 FE ? K HEM . ? D HEM 401 ? 1_555 N2 ? L A1H6U . ? D A1H6U 402 ? 1_555 87.6  ? 
# 
_pdbx_entry_details.entry_id                   9ESF 
_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   N 
# 
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 PHE A 347 ? ? -98.71  47.60  
2 1 PHE B 347 ? ? -97.68  49.34  
3 1 ASP B 367 ? ? -108.35 -69.46 
4 1 ALA C 134 ? ? 84.14   124.36 
5 1 ASP C 169 ? ? 169.26  160.85 
6 1 PHE C 347 ? ? -97.95  48.16  
7 1 ASP C 367 ? ? -108.64 -69.20 
8 1 PHE D 347 ? ? -99.84  47.62  
# 
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 23  ? A MET 1   
2   1 Y 1 A GLY 24  ? A GLY 2   
3   1 Y 1 A ALA 132 ? A ALA 110 
4   1 Y 1 A PRO 133 ? A PRO 111 
5   1 Y 1 A ALA 134 ? A ALA 112 
6   1 Y 1 A SER 135 ? A SER 113 
7   1 Y 1 A GLY 136 ? A GLY 114 
8   1 Y 1 A PHE 137 ? A PHE 115 
9   1 Y 1 A ARG 156 ? A ARG 134 
10  1 Y 1 A VAL 157 ? A VAL 135 
11  1 Y 1 A ARG 158 ? A ARG 136 
12  1 Y 1 A TYR 159 ? A TYR 137 
13  1 Y 1 A ASN 160 ? A ASN 138 
14  1 Y 1 A GLN 161 ? A GLN 139 
15  1 Y 1 A LYS 162 ? A LYS 140 
16  1 Y 1 A TYR 163 ? A TYR 141 
17  1 Y 1 A SER 164 ? A SER 142 
18  1 Y 1 A ASP 165 ? A ASP 143 
19  1 Y 1 A VAL 166 ? A VAL 144 
20  1 Y 1 A PHE 167 ? A PHE 145 
21  1 Y 1 A SER 168 ? A SER 146 
22  1 Y 1 A ASP 169 ? A ASP 147 
23  1 Y 1 A THR 369 ? A THR 347 
24  1 Y 1 A ILE 370 ? A ILE 348 
25  1 Y 1 A ARG 371 ? A ARG 349 
26  1 Y 1 A LYS 372 ? A LYS 350 
27  1 Y 1 A LYS 373 ? A LYS 351 
28  1 Y 1 A LEU 374 ? A LEU 352 
29  1 Y 1 A ILE 375 ? A ILE 353 
30  1 Y 1 A ASN 376 ? A ASN 354 
31  1 Y 1 A LYS 377 ? A LYS 355 
32  1 Y 1 A SER 378 ? A SER 356 
33  1 Y 1 A VAL 379 ? A VAL 357 
34  1 Y 1 A LEU 380 ? A LEU 358 
35  1 Y 1 A GLU 381 ? A GLU 359 
36  1 Y 1 A HIS 382 ? A HIS 360 
37  1 Y 1 A HIS 383 ? A HIS 361 
38  1 Y 1 A HIS 384 ? A HIS 362 
39  1 Y 1 A HIS 385 ? A HIS 363 
40  1 Y 1 A HIS 386 ? A HIS 364 
41  1 Y 1 A HIS 387 ? A HIS 365 
42  1 Y 1 B MET 23  ? B MET 1   
43  1 Y 1 B GLY 24  ? B GLY 2   
44  1 Y 1 B ALA 132 ? B ALA 110 
45  1 Y 1 B PRO 133 ? B PRO 111 
46  1 Y 1 B ALA 134 ? B ALA 112 
47  1 Y 1 B SER 135 ? B SER 113 
48  1 Y 1 B GLY 136 ? B GLY 114 
49  1 Y 1 B PHE 137 ? B PHE 115 
50  1 Y 1 B ARG 156 ? B ARG 134 
51  1 Y 1 B VAL 157 ? B VAL 135 
52  1 Y 1 B ARG 158 ? B ARG 136 
53  1 Y 1 B TYR 159 ? B TYR 137 
54  1 Y 1 B ASN 160 ? B ASN 138 
55  1 Y 1 B GLN 161 ? B GLN 139 
56  1 Y 1 B LYS 162 ? B LYS 140 
57  1 Y 1 B TYR 163 ? B TYR 141 
58  1 Y 1 B SER 164 ? B SER 142 
59  1 Y 1 B ASP 165 ? B ASP 143 
60  1 Y 1 B THR 369 ? B THR 347 
61  1 Y 1 B ILE 370 ? B ILE 348 
62  1 Y 1 B ARG 371 ? B ARG 349 
63  1 Y 1 B LYS 372 ? B LYS 350 
64  1 Y 1 B LYS 373 ? B LYS 351 
65  1 Y 1 B LEU 374 ? B LEU 352 
66  1 Y 1 B ILE 375 ? B ILE 353 
67  1 Y 1 B ASN 376 ? B ASN 354 
68  1 Y 1 B LYS 377 ? B LYS 355 
69  1 Y 1 B SER 378 ? B SER 356 
70  1 Y 1 B VAL 379 ? B VAL 357 
71  1 Y 1 B LEU 380 ? B LEU 358 
72  1 Y 1 B GLU 381 ? B GLU 359 
73  1 Y 1 B HIS 382 ? B HIS 360 
74  1 Y 1 B HIS 383 ? B HIS 361 
75  1 Y 1 B HIS 384 ? B HIS 362 
76  1 Y 1 B HIS 385 ? B HIS 363 
77  1 Y 1 B HIS 386 ? B HIS 364 
78  1 Y 1 B HIS 387 ? B HIS 365 
79  1 Y 1 C MET 23  ? C MET 1   
80  1 Y 1 C GLY 24  ? C GLY 2   
81  1 Y 1 C LYS 25  ? C LYS 3   
82  1 Y 1 C GLN 155 ? C GLN 133 
83  1 Y 1 C ARG 156 ? C ARG 134 
84  1 Y 1 C VAL 157 ? C VAL 135 
85  1 Y 1 C ARG 158 ? C ARG 136 
86  1 Y 1 C TYR 159 ? C TYR 137 
87  1 Y 1 C ASN 160 ? C ASN 138 
88  1 Y 1 C GLN 161 ? C GLN 139 
89  1 Y 1 C LYS 162 ? C LYS 140 
90  1 Y 1 C TYR 163 ? C TYR 141 
91  1 Y 1 C SER 164 ? C SER 142 
92  1 Y 1 C ASP 165 ? C ASP 143 
93  1 Y 1 C VAL 166 ? C VAL 144 
94  1 Y 1 C PHE 167 ? C PHE 145 
95  1 Y 1 C THR 369 ? C THR 347 
96  1 Y 1 C ILE 370 ? C ILE 348 
97  1 Y 1 C ARG 371 ? C ARG 349 
98  1 Y 1 C LYS 372 ? C LYS 350 
99  1 Y 1 C LYS 373 ? C LYS 351 
100 1 Y 1 C LEU 374 ? C LEU 352 
101 1 Y 1 C ILE 375 ? C ILE 353 
102 1 Y 1 C ASN 376 ? C ASN 354 
103 1 Y 1 C LYS 377 ? C LYS 355 
104 1 Y 1 C SER 378 ? C SER 356 
105 1 Y 1 C VAL 379 ? C VAL 357 
106 1 Y 1 C LEU 380 ? C LEU 358 
107 1 Y 1 C GLU 381 ? C GLU 359 
108 1 Y 1 C HIS 382 ? C HIS 360 
109 1 Y 1 C HIS 383 ? C HIS 361 
110 1 Y 1 C HIS 384 ? C HIS 362 
111 1 Y 1 C HIS 385 ? C HIS 363 
112 1 Y 1 C HIS 386 ? C HIS 364 
113 1 Y 1 C HIS 387 ? C HIS 365 
114 1 Y 1 D MET 23  ? D MET 1   
115 1 Y 1 D GLY 24  ? D GLY 2   
116 1 Y 1 D ALA 132 ? D ALA 110 
117 1 Y 1 D PRO 133 ? D PRO 111 
118 1 Y 1 D ALA 134 ? D ALA 112 
119 1 Y 1 D SER 135 ? D SER 113 
120 1 Y 1 D GLY 136 ? D GLY 114 
121 1 Y 1 D PHE 137 ? D PHE 115 
122 1 Y 1 D TYR 159 ? D TYR 137 
123 1 Y 1 D ASN 160 ? D ASN 138 
124 1 Y 1 D GLN 161 ? D GLN 139 
125 1 Y 1 D LYS 162 ? D LYS 140 
126 1 Y 1 D TYR 163 ? D TYR 141 
127 1 Y 1 D SER 164 ? D SER 142 
128 1 Y 1 D ASP 165 ? D ASP 143 
129 1 Y 1 D THR 369 ? D THR 347 
130 1 Y 1 D ILE 370 ? D ILE 348 
131 1 Y 1 D ARG 371 ? D ARG 349 
132 1 Y 1 D LYS 372 ? D LYS 350 
133 1 Y 1 D LYS 373 ? D LYS 351 
134 1 Y 1 D LEU 374 ? D LEU 352 
135 1 Y 1 D ILE 375 ? D ILE 353 
136 1 Y 1 D ASN 376 ? D ASN 354 
137 1 Y 1 D LYS 377 ? D LYS 355 
138 1 Y 1 D SER 378 ? D SER 356 
139 1 Y 1 D VAL 379 ? D VAL 357 
140 1 Y 1 D LEU 380 ? D LEU 358 
141 1 Y 1 D GLU 381 ? D GLU 359 
142 1 Y 1 D HIS 382 ? D HIS 360 
143 1 Y 1 D HIS 383 ? D HIS 361 
144 1 Y 1 D HIS 384 ? D HIS 362 
145 1 Y 1 D HIS 385 ? D HIS 363 
146 1 Y 1 D HIS 386 ? D HIS 364 
147 1 Y 1 D HIS 387 ? D HIS 365 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1H6U C5   C  Y N 1   
A1H6U C6   C  Y N 2   
A1H6U C7   C  Y N 3   
A1H6U C8   C  Y N 4   
A1H6U C13  C  N N 5   
A1H6U O    O  N N 6   
A1H6U C1   C  N S 7   
A1H6U CA   C  Y N 8   
A1H6U N    N  Y N 9   
A1H6U C3   C  Y N 10  
A1H6U CG2  C  Y N 11  
A1H6U N2   N  Y N 12  
A1H6U C9   C  N N 13  
A1H6U CD1  C  N N 14  
A1H6U CG1  C  N N 15  
A1H6U C12  C  N N 16  
A1H6U C14  C  N N 17  
A1H6U H4   H  N N 18  
A1H6U H5   H  N N 19  
A1H6U H6   H  N N 20  
A1H6U H7   H  N N 21  
A1H6U H16  H  N N 22  
A1H6U H15  H  N N 23  
A1H6U H1   H  N N 24  
A1H6U H2   H  N N 25  
A1H6U H3   H  N N 26  
A1H6U H8   H  N N 27  
A1H6U H10  H  N N 28  
A1H6U H9   H  N N 29  
A1H6U H12  H  N N 30  
A1H6U H11  H  N N 31  
A1H6U H13  H  N N 32  
A1H6U H14  H  N N 33  
A1H6U H18  H  N N 34  
A1H6U H17  H  N N 35  
ALA   N    N  N N 36  
ALA   CA   C  N S 37  
ALA   C    C  N N 38  
ALA   O    O  N N 39  
ALA   CB   C  N N 40  
ALA   OXT  O  N N 41  
ALA   H    H  N N 42  
ALA   H2   H  N N 43  
ALA   HA   H  N N 44  
ALA   HB1  H  N N 45  
ALA   HB2  H  N N 46  
ALA   HB3  H  N N 47  
ALA   HXT  H  N N 48  
ARG   N    N  N N 49  
ARG   CA   C  N S 50  
ARG   C    C  N N 51  
ARG   O    O  N N 52  
ARG   CB   C  N N 53  
ARG   CG   C  N N 54  
ARG   CD   C  N N 55  
ARG   NE   N  N N 56  
ARG   CZ   C  N N 57  
ARG   NH1  N  N N 58  
ARG   NH2  N  N N 59  
ARG   OXT  O  N N 60  
ARG   H    H  N N 61  
ARG   H2   H  N N 62  
ARG   HA   H  N N 63  
ARG   HB2  H  N N 64  
ARG   HB3  H  N N 65  
ARG   HG2  H  N N 66  
ARG   HG3  H  N N 67  
ARG   HD2  H  N N 68  
ARG   HD3  H  N N 69  
ARG   HE   H  N N 70  
ARG   HH11 H  N N 71  
ARG   HH12 H  N N 72  
ARG   HH21 H  N N 73  
ARG   HH22 H  N N 74  
ARG   HXT  H  N N 75  
ASN   N    N  N N 76  
ASN   CA   C  N S 77  
ASN   C    C  N N 78  
ASN   O    O  N N 79  
ASN   CB   C  N N 80  
ASN   CG   C  N N 81  
ASN   OD1  O  N N 82  
ASN   ND2  N  N N 83  
ASN   OXT  O  N N 84  
ASN   H    H  N N 85  
ASN   H2   H  N N 86  
ASN   HA   H  N N 87  
ASN   HB2  H  N N 88  
ASN   HB3  H  N N 89  
ASN   HD21 H  N N 90  
ASN   HD22 H  N N 91  
ASN   HXT  H  N N 92  
ASP   N    N  N N 93  
ASP   CA   C  N S 94  
ASP   C    C  N N 95  
ASP   O    O  N N 96  
ASP   CB   C  N N 97  
ASP   CG   C  N N 98  
ASP   OD1  O  N N 99  
ASP   OD2  O  N N 100 
ASP   OXT  O  N N 101 
ASP   H    H  N N 102 
ASP   H2   H  N N 103 
ASP   HA   H  N N 104 
ASP   HB2  H  N N 105 
ASP   HB3  H  N N 106 
ASP   HD2  H  N N 107 
ASP   HXT  H  N N 108 
CYS   N    N  N N 109 
CYS   CA   C  N R 110 
CYS   C    C  N N 111 
CYS   O    O  N N 112 
CYS   CB   C  N N 113 
CYS   SG   S  N N 114 
CYS   OXT  O  N N 115 
CYS   H    H  N N 116 
CYS   H2   H  N N 117 
CYS   HA   H  N N 118 
CYS   HB2  H  N N 119 
CYS   HB3  H  N N 120 
CYS   HG   H  N N 121 
CYS   HXT  H  N N 122 
GLN   N    N  N N 123 
GLN   CA   C  N S 124 
GLN   C    C  N N 125 
GLN   O    O  N N 126 
GLN   CB   C  N N 127 
GLN   CG   C  N N 128 
GLN   CD   C  N N 129 
GLN   OE1  O  N N 130 
GLN   NE2  N  N N 131 
GLN   OXT  O  N N 132 
GLN   H    H  N N 133 
GLN   H2   H  N N 134 
GLN   HA   H  N N 135 
GLN   HB2  H  N N 136 
GLN   HB3  H  N N 137 
GLN   HG2  H  N N 138 
GLN   HG3  H  N N 139 
GLN   HE21 H  N N 140 
GLN   HE22 H  N N 141 
GLN   HXT  H  N N 142 
GLU   N    N  N N 143 
GLU   CA   C  N S 144 
GLU   C    C  N N 145 
GLU   O    O  N N 146 
GLU   CB   C  N N 147 
GLU   CG   C  N N 148 
GLU   CD   C  N N 149 
GLU   OE1  O  N N 150 
GLU   OE2  O  N N 151 
GLU   OXT  O  N N 152 
GLU   H    H  N N 153 
GLU   H2   H  N N 154 
GLU   HA   H  N N 155 
GLU   HB2  H  N N 156 
GLU   HB3  H  N N 157 
GLU   HG2  H  N N 158 
GLU   HG3  H  N N 159 
GLU   HE2  H  N N 160 
GLU   HXT  H  N N 161 
GLY   N    N  N N 162 
GLY   CA   C  N N 163 
GLY   C    C  N N 164 
GLY   O    O  N N 165 
GLY   OXT  O  N N 166 
GLY   H    H  N N 167 
GLY   H2   H  N N 168 
GLY   HA2  H  N N 169 
GLY   HA3  H  N N 170 
GLY   HXT  H  N N 171 
HEM   CHA  C  N N 172 
HEM   CHB  C  N N 173 
HEM   CHC  C  N N 174 
HEM   CHD  C  N N 175 
HEM   C1A  C  Y N 176 
HEM   C2A  C  Y N 177 
HEM   C3A  C  Y N 178 
HEM   C4A  C  Y N 179 
HEM   CMA  C  N N 180 
HEM   CAA  C  N N 181 
HEM   CBA  C  N N 182 
HEM   CGA  C  N N 183 
HEM   O1A  O  N N 184 
HEM   O2A  O  N N 185 
HEM   C1B  C  N N 186 
HEM   C2B  C  N N 187 
HEM   C3B  C  N N 188 
HEM   C4B  C  N N 189 
HEM   CMB  C  N N 190 
HEM   CAB  C  N N 191 
HEM   CBB  C  N N 192 
HEM   C1C  C  Y N 193 
HEM   C2C  C  Y N 194 
HEM   C3C  C  Y N 195 
HEM   C4C  C  Y N 196 
HEM   CMC  C  N N 197 
HEM   CAC  C  N N 198 
HEM   CBC  C  N N 199 
HEM   C1D  C  N N 200 
HEM   C2D  C  N N 201 
HEM   C3D  C  N N 202 
HEM   C4D  C  N N 203 
HEM   CMD  C  N N 204 
HEM   CAD  C  N N 205 
HEM   CBD  C  N N 206 
HEM   CGD  C  N N 207 
HEM   O1D  O  N N 208 
HEM   O2D  O  N N 209 
HEM   NA   N  Y N 210 
HEM   NB   N  N N 211 
HEM   NC   N  Y N 212 
HEM   ND   N  N N 213 
HEM   FE   FE N N 214 
HEM   HHB  H  N N 215 
HEM   HHC  H  N N 216 
HEM   HHD  H  N N 217 
HEM   HMA  H  N N 218 
HEM   HMAA H  N N 219 
HEM   HMAB H  N N 220 
HEM   HAA  H  N N 221 
HEM   HAAA H  N N 222 
HEM   HBA  H  N N 223 
HEM   HBAA H  N N 224 
HEM   HMB  H  N N 225 
HEM   HMBA H  N N 226 
HEM   HMBB H  N N 227 
HEM   HAB  H  N N 228 
HEM   HBB  H  N N 229 
HEM   HBBA H  N N 230 
HEM   HMC  H  N N 231 
HEM   HMCA H  N N 232 
HEM   HMCB H  N N 233 
HEM   HAC  H  N N 234 
HEM   HBC  H  N N 235 
HEM   HBCA H  N N 236 
HEM   HMD  H  N N 237 
HEM   HMDA H  N N 238 
HEM   HMDB H  N N 239 
HEM   HAD  H  N N 240 
HEM   HADA H  N N 241 
HEM   HBD  H  N N 242 
HEM   HBDA H  N N 243 
HEM   H2A  H  N N 244 
HEM   H2D  H  N N 245 
HEM   HHA  H  N N 246 
HIS   N    N  N N 247 
HIS   CA   C  N S 248 
HIS   C    C  N N 249 
HIS   O    O  N N 250 
HIS   CB   C  N N 251 
HIS   CG   C  Y N 252 
HIS   ND1  N  Y N 253 
HIS   CD2  C  Y N 254 
HIS   CE1  C  Y N 255 
HIS   NE2  N  Y N 256 
HIS   OXT  O  N N 257 
HIS   H    H  N N 258 
HIS   H2   H  N N 259 
HIS   HA   H  N N 260 
HIS   HB2  H  N N 261 
HIS   HB3  H  N N 262 
HIS   HD1  H  N N 263 
HIS   HD2  H  N N 264 
HIS   HE1  H  N N 265 
HIS   HE2  H  N N 266 
HIS   HXT  H  N N 267 
HOH   O    O  N N 268 
HOH   H1   H  N N 269 
HOH   H2   H  N N 270 
ILE   N    N  N N 271 
ILE   CA   C  N S 272 
ILE   C    C  N N 273 
ILE   O    O  N N 274 
ILE   CB   C  N S 275 
ILE   CG1  C  N N 276 
ILE   CG2  C  N N 277 
ILE   CD1  C  N N 278 
ILE   OXT  O  N N 279 
ILE   H    H  N N 280 
ILE   H2   H  N N 281 
ILE   HA   H  N N 282 
ILE   HB   H  N N 283 
ILE   HG12 H  N N 284 
ILE   HG13 H  N N 285 
ILE   HG21 H  N N 286 
ILE   HG22 H  N N 287 
ILE   HG23 H  N N 288 
ILE   HD11 H  N N 289 
ILE   HD12 H  N N 290 
ILE   HD13 H  N N 291 
ILE   HXT  H  N N 292 
LEU   N    N  N N 293 
LEU   CA   C  N S 294 
LEU   C    C  N N 295 
LEU   O    O  N N 296 
LEU   CB   C  N N 297 
LEU   CG   C  N N 298 
LEU   CD1  C  N N 299 
LEU   CD2  C  N N 300 
LEU   OXT  O  N N 301 
LEU   H    H  N N 302 
LEU   H2   H  N N 303 
LEU   HA   H  N N 304 
LEU   HB2  H  N N 305 
LEU   HB3  H  N N 306 
LEU   HG   H  N N 307 
LEU   HD11 H  N N 308 
LEU   HD12 H  N N 309 
LEU   HD13 H  N N 310 
LEU   HD21 H  N N 311 
LEU   HD22 H  N N 312 
LEU   HD23 H  N N 313 
LEU   HXT  H  N N 314 
LYS   N    N  N N 315 
LYS   CA   C  N S 316 
LYS   C    C  N N 317 
LYS   O    O  N N 318 
LYS   CB   C  N N 319 
LYS   CG   C  N N 320 
LYS   CD   C  N N 321 
LYS   CE   C  N N 322 
LYS   NZ   N  N N 323 
LYS   OXT  O  N N 324 
LYS   H    H  N N 325 
LYS   H2   H  N N 326 
LYS   HA   H  N N 327 
LYS   HB2  H  N N 328 
LYS   HB3  H  N N 329 
LYS   HG2  H  N N 330 
LYS   HG3  H  N N 331 
LYS   HD2  H  N N 332 
LYS   HD3  H  N N 333 
LYS   HE2  H  N N 334 
LYS   HE3  H  N N 335 
LYS   HZ1  H  N N 336 
LYS   HZ2  H  N N 337 
LYS   HZ3  H  N N 338 
LYS   HXT  H  N N 339 
MET   N    N  N N 340 
MET   CA   C  N S 341 
MET   C    C  N N 342 
MET   O    O  N N 343 
MET   CB   C  N N 344 
MET   CG   C  N N 345 
MET   SD   S  N N 346 
MET   CE   C  N N 347 
MET   OXT  O  N N 348 
MET   H    H  N N 349 
MET   H2   H  N N 350 
MET   HA   H  N N 351 
MET   HB2  H  N N 352 
MET   HB3  H  N N 353 
MET   HG2  H  N N 354 
MET   HG3  H  N N 355 
MET   HE1  H  N N 356 
MET   HE2  H  N N 357 
MET   HE3  H  N N 358 
MET   HXT  H  N N 359 
PHE   N    N  N N 360 
PHE   CA   C  N S 361 
PHE   C    C  N N 362 
PHE   O    O  N N 363 
PHE   CB   C  N N 364 
PHE   CG   C  Y N 365 
PHE   CD1  C  Y N 366 
PHE   CD2  C  Y N 367 
PHE   CE1  C  Y N 368 
PHE   CE2  C  Y N 369 
PHE   CZ   C  Y N 370 
PHE   OXT  O  N N 371 
PHE   H    H  N N 372 
PHE   H2   H  N N 373 
PHE   HA   H  N N 374 
PHE   HB2  H  N N 375 
PHE   HB3  H  N N 376 
PHE   HD1  H  N N 377 
PHE   HD2  H  N N 378 
PHE   HE1  H  N N 379 
PHE   HE2  H  N N 380 
PHE   HZ   H  N N 381 
PHE   HXT  H  N N 382 
PRO   N    N  N N 383 
PRO   CA   C  N S 384 
PRO   C    C  N N 385 
PRO   O    O  N N 386 
PRO   CB   C  N N 387 
PRO   CG   C  N N 388 
PRO   CD   C  N N 389 
PRO   OXT  O  N N 390 
PRO   H    H  N N 391 
PRO   HA   H  N N 392 
PRO   HB2  H  N N 393 
PRO   HB3  H  N N 394 
PRO   HG2  H  N N 395 
PRO   HG3  H  N N 396 
PRO   HD2  H  N N 397 
PRO   HD3  H  N N 398 
PRO   HXT  H  N N 399 
SER   N    N  N N 400 
SER   CA   C  N S 401 
SER   C    C  N N 402 
SER   O    O  N N 403 
SER   CB   C  N N 404 
SER   OG   O  N N 405 
SER   OXT  O  N N 406 
SER   H    H  N N 407 
SER   H2   H  N N 408 
SER   HA   H  N N 409 
SER   HB2  H  N N 410 
SER   HB3  H  N N 411 
SER   HG   H  N N 412 
SER   HXT  H  N N 413 
THR   N    N  N N 414 
THR   CA   C  N S 415 
THR   C    C  N N 416 
THR   O    O  N N 417 
THR   CB   C  N R 418 
THR   OG1  O  N N 419 
THR   CG2  C  N N 420 
THR   OXT  O  N N 421 
THR   H    H  N N 422 
THR   H2   H  N N 423 
THR   HA   H  N N 424 
THR   HB   H  N N 425 
THR   HG1  H  N N 426 
THR   HG21 H  N N 427 
THR   HG22 H  N N 428 
THR   HG23 H  N N 429 
THR   HXT  H  N N 430 
TRP   N    N  N N 431 
TRP   CA   C  N S 432 
TRP   C    C  N N 433 
TRP   O    O  N N 434 
TRP   CB   C  N N 435 
TRP   CG   C  Y N 436 
TRP   CD1  C  Y N 437 
TRP   CD2  C  Y N 438 
TRP   NE1  N  Y N 439 
TRP   CE2  C  Y N 440 
TRP   CE3  C  Y N 441 
TRP   CZ2  C  Y N 442 
TRP   CZ3  C  Y N 443 
TRP   CH2  C  Y N 444 
TRP   OXT  O  N N 445 
TRP   H    H  N N 446 
TRP   H2   H  N N 447 
TRP   HA   H  N N 448 
TRP   HB2  H  N N 449 
TRP   HB3  H  N N 450 
TRP   HD1  H  N N 451 
TRP   HE1  H  N N 452 
TRP   HE3  H  N N 453 
TRP   HZ2  H  N N 454 
TRP   HZ3  H  N N 455 
TRP   HH2  H  N N 456 
TRP   HXT  H  N N 457 
TYR   N    N  N N 458 
TYR   CA   C  N S 459 
TYR   C    C  N N 460 
TYR   O    O  N N 461 
TYR   CB   C  N N 462 
TYR   CG   C  Y N 463 
TYR   CD1  C  Y N 464 
TYR   CD2  C  Y N 465 
TYR   CE1  C  Y N 466 
TYR   CE2  C  Y N 467 
TYR   CZ   C  Y N 468 
TYR   OH   O  N N 469 
TYR   OXT  O  N N 470 
TYR   H    H  N N 471 
TYR   H2   H  N N 472 
TYR   HA   H  N N 473 
TYR   HB2  H  N N 474 
TYR   HB3  H  N N 475 
TYR   HD1  H  N N 476 
TYR   HD2  H  N N 477 
TYR   HE1  H  N N 478 
TYR   HE2  H  N N 479 
TYR   HH   H  N N 480 
TYR   HXT  H  N N 481 
VAL   N    N  N N 482 
VAL   CA   C  N S 483 
VAL   C    C  N N 484 
VAL   O    O  N N 485 
VAL   CB   C  N N 486 
VAL   CG1  C  N N 487 
VAL   CG2  C  N N 488 
VAL   OXT  O  N N 489 
VAL   H    H  N N 490 
VAL   H2   H  N N 491 
VAL   HA   H  N N 492 
VAL   HB   H  N N 493 
VAL   HG11 H  N N 494 
VAL   HG12 H  N N 495 
VAL   HG13 H  N N 496 
VAL   HG21 H  N N 497 
VAL   HG22 H  N N 498 
VAL   HG23 H  N N 499 
VAL   HXT  H  N N 500 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1H6U O   C1   sing N N 1   
A1H6U C1  CA   sing N N 2   
A1H6U CA  N    sing Y N 3   
A1H6U N   C3   sing Y N 4   
A1H6U C3  CG2  sing Y N 5   
A1H6U CG2 C5   doub Y N 6   
A1H6U C5  C6   sing Y N 7   
A1H6U C3  C7   doub Y N 8   
A1H6U C7  N2   sing Y N 9   
A1H6U N2  C8   doub Y N 10  
A1H6U C1  C9   sing N N 11  
A1H6U C9  CD1  sing N N 12  
A1H6U CD1 CG1  sing N N 13  
A1H6U CG1 C12  sing N N 14  
A1H6U C12 C13  sing N N 15  
A1H6U C13 C14  sing N N 16  
A1H6U CA  C6   doub Y N 17  
A1H6U C8  N    sing Y N 18  
A1H6U C14 C9   sing N N 19  
A1H6U C5  H4   sing N N 20  
A1H6U C6  H5   sing N N 21  
A1H6U C7  H6   sing N N 22  
A1H6U C8  H7   sing N N 23  
A1H6U C13 H16  sing N N 24  
A1H6U C13 H15  sing N N 25  
A1H6U O   H1   sing N N 26  
A1H6U C1  H2   sing N N 27  
A1H6U CG2 H3   sing N N 28  
A1H6U C9  H8   sing N N 29  
A1H6U CD1 H10  sing N N 30  
A1H6U CD1 H9   sing N N 31  
A1H6U CG1 H12  sing N N 32  
A1H6U CG1 H11  sing N N 33  
A1H6U C12 H13  sing N N 34  
A1H6U C12 H14  sing N N 35  
A1H6U C14 H18  sing N N 36  
A1H6U C14 H17  sing N N 37  
ALA   N   CA   sing N N 38  
ALA   N   H    sing N N 39  
ALA   N   H2   sing N N 40  
ALA   CA  C    sing N N 41  
ALA   CA  CB   sing N N 42  
ALA   CA  HA   sing N N 43  
ALA   C   O    doub N N 44  
ALA   C   OXT  sing N N 45  
ALA   CB  HB1  sing N N 46  
ALA   CB  HB2  sing N N 47  
ALA   CB  HB3  sing N N 48  
ALA   OXT HXT  sing N N 49  
ARG   N   CA   sing N N 50  
ARG   N   H    sing N N 51  
ARG   N   H2   sing N N 52  
ARG   CA  C    sing N N 53  
ARG   CA  CB   sing N N 54  
ARG   CA  HA   sing N N 55  
ARG   C   O    doub N N 56  
ARG   C   OXT  sing N N 57  
ARG   CB  CG   sing N N 58  
ARG   CB  HB2  sing N N 59  
ARG   CB  HB3  sing N N 60  
ARG   CG  CD   sing N N 61  
ARG   CG  HG2  sing N N 62  
ARG   CG  HG3  sing N N 63  
ARG   CD  NE   sing N N 64  
ARG   CD  HD2  sing N N 65  
ARG   CD  HD3  sing N N 66  
ARG   NE  CZ   sing N N 67  
ARG   NE  HE   sing N N 68  
ARG   CZ  NH1  sing N N 69  
ARG   CZ  NH2  doub N N 70  
ARG   NH1 HH11 sing N N 71  
ARG   NH1 HH12 sing N N 72  
ARG   NH2 HH21 sing N N 73  
ARG   NH2 HH22 sing N N 74  
ARG   OXT HXT  sing N N 75  
ASN   N   CA   sing N N 76  
ASN   N   H    sing N N 77  
ASN   N   H2   sing N N 78  
ASN   CA  C    sing N N 79  
ASN   CA  CB   sing N N 80  
ASN   CA  HA   sing N N 81  
ASN   C   O    doub N N 82  
ASN   C   OXT  sing N N 83  
ASN   CB  CG   sing N N 84  
ASN   CB  HB2  sing N N 85  
ASN   CB  HB3  sing N N 86  
ASN   CG  OD1  doub N N 87  
ASN   CG  ND2  sing N N 88  
ASN   ND2 HD21 sing N N 89  
ASN   ND2 HD22 sing N N 90  
ASN   OXT HXT  sing N N 91  
ASP   N   CA   sing N N 92  
ASP   N   H    sing N N 93  
ASP   N   H2   sing N N 94  
ASP   CA  C    sing N N 95  
ASP   CA  CB   sing N N 96  
ASP   CA  HA   sing N N 97  
ASP   C   O    doub N N 98  
ASP   C   OXT  sing N N 99  
ASP   CB  CG   sing N N 100 
ASP   CB  HB2  sing N N 101 
ASP   CB  HB3  sing N N 102 
ASP   CG  OD1  doub N N 103 
ASP   CG  OD2  sing N N 104 
ASP   OD2 HD2  sing N N 105 
ASP   OXT HXT  sing N N 106 
CYS   N   CA   sing N N 107 
CYS   N   H    sing N N 108 
CYS   N   H2   sing N N 109 
CYS   CA  C    sing N N 110 
CYS   CA  CB   sing N N 111 
CYS   CA  HA   sing N N 112 
CYS   C   O    doub N N 113 
CYS   C   OXT  sing N N 114 
CYS   CB  SG   sing N N 115 
CYS   CB  HB2  sing N N 116 
CYS   CB  HB3  sing N N 117 
CYS   SG  HG   sing N N 118 
CYS   OXT HXT  sing N N 119 
GLN   N   CA   sing N N 120 
GLN   N   H    sing N N 121 
GLN   N   H2   sing N N 122 
GLN   CA  C    sing N N 123 
GLN   CA  CB   sing N N 124 
GLN   CA  HA   sing N N 125 
GLN   C   O    doub N N 126 
GLN   C   OXT  sing N N 127 
GLN   CB  CG   sing N N 128 
GLN   CB  HB2  sing N N 129 
GLN   CB  HB3  sing N N 130 
GLN   CG  CD   sing N N 131 
GLN   CG  HG2  sing N N 132 
GLN   CG  HG3  sing N N 133 
GLN   CD  OE1  doub N N 134 
GLN   CD  NE2  sing N N 135 
GLN   NE2 HE21 sing N N 136 
GLN   NE2 HE22 sing N N 137 
GLN   OXT HXT  sing N N 138 
GLU   N   CA   sing N N 139 
GLU   N   H    sing N N 140 
GLU   N   H2   sing N N 141 
GLU   CA  C    sing N N 142 
GLU   CA  CB   sing N N 143 
GLU   CA  HA   sing N N 144 
GLU   C   O    doub N N 145 
GLU   C   OXT  sing N N 146 
GLU   CB  CG   sing N N 147 
GLU   CB  HB2  sing N N 148 
GLU   CB  HB3  sing N N 149 
GLU   CG  CD   sing N N 150 
GLU   CG  HG2  sing N N 151 
GLU   CG  HG3  sing N N 152 
GLU   CD  OE1  doub N N 153 
GLU   CD  OE2  sing N N 154 
GLU   OE2 HE2  sing N N 155 
GLU   OXT HXT  sing N N 156 
GLY   N   CA   sing N N 157 
GLY   N   H    sing N N 158 
GLY   N   H2   sing N N 159 
GLY   CA  C    sing N N 160 
GLY   CA  HA2  sing N N 161 
GLY   CA  HA3  sing N N 162 
GLY   C   O    doub N N 163 
GLY   C   OXT  sing N N 164 
GLY   OXT HXT  sing N N 165 
HEM   CHA C1A  sing N N 166 
HEM   CHA C4D  doub N N 167 
HEM   CHA HHA  sing N N 168 
HEM   CHB C4A  sing N N 169 
HEM   CHB C1B  doub N N 170 
HEM   CHB HHB  sing N N 171 
HEM   CHC C4B  sing N N 172 
HEM   CHC C1C  doub N N 173 
HEM   CHC HHC  sing N N 174 
HEM   CHD C4C  doub N N 175 
HEM   CHD C1D  sing N N 176 
HEM   CHD HHD  sing N N 177 
HEM   C1A C2A  doub Y N 178 
HEM   C1A NA   sing Y N 179 
HEM   C2A C3A  sing Y N 180 
HEM   C2A CAA  sing N N 181 
HEM   C3A C4A  doub Y N 182 
HEM   C3A CMA  sing N N 183 
HEM   C4A NA   sing Y N 184 
HEM   CMA HMA  sing N N 185 
HEM   CMA HMAA sing N N 186 
HEM   CMA HMAB sing N N 187 
HEM   CAA CBA  sing N N 188 
HEM   CAA HAA  sing N N 189 
HEM   CAA HAAA sing N N 190 
HEM   CBA CGA  sing N N 191 
HEM   CBA HBA  sing N N 192 
HEM   CBA HBAA sing N N 193 
HEM   CGA O1A  doub N N 194 
HEM   CGA O2A  sing N N 195 
HEM   C1B C2B  sing N N 196 
HEM   C1B NB   sing N N 197 
HEM   C2B C3B  doub N N 198 
HEM   C2B CMB  sing N N 199 
HEM   C3B C4B  sing N N 200 
HEM   C3B CAB  sing N N 201 
HEM   C4B NB   doub N N 202 
HEM   CMB HMB  sing N N 203 
HEM   CMB HMBA sing N N 204 
HEM   CMB HMBB sing N N 205 
HEM   CAB CBB  doub N N 206 
HEM   CAB HAB  sing N N 207 
HEM   CBB HBB  sing N N 208 
HEM   CBB HBBA sing N N 209 
HEM   C1C C2C  sing Y N 210 
HEM   C1C NC   sing Y N 211 
HEM   C2C C3C  doub Y N 212 
HEM   C2C CMC  sing N N 213 
HEM   C3C C4C  sing Y N 214 
HEM   C3C CAC  sing N N 215 
HEM   C4C NC   sing Y N 216 
HEM   CMC HMC  sing N N 217 
HEM   CMC HMCA sing N N 218 
HEM   CMC HMCB sing N N 219 
HEM   CAC CBC  doub N N 220 
HEM   CAC HAC  sing N N 221 
HEM   CBC HBC  sing N N 222 
HEM   CBC HBCA sing N N 223 
HEM   C1D C2D  sing N N 224 
HEM   C1D ND   doub N N 225 
HEM   C2D C3D  doub N N 226 
HEM   C2D CMD  sing N N 227 
HEM   C3D C4D  sing N N 228 
HEM   C3D CAD  sing N N 229 
HEM   C4D ND   sing N N 230 
HEM   CMD HMD  sing N N 231 
HEM   CMD HMDA sing N N 232 
HEM   CMD HMDB sing N N 233 
HEM   CAD CBD  sing N N 234 
HEM   CAD HAD  sing N N 235 
HEM   CAD HADA sing N N 236 
HEM   CBD CGD  sing N N 237 
HEM   CBD HBD  sing N N 238 
HEM   CBD HBDA sing N N 239 
HEM   CGD O1D  doub N N 240 
HEM   CGD O2D  sing N N 241 
HEM   O2A H2A  sing N N 242 
HEM   O2D H2D  sing N N 243 
HEM   FE  NA   sing N N 244 
HEM   FE  NB   sing N N 245 
HEM   FE  NC   sing N N 246 
HEM   FE  ND   sing N N 247 
HIS   N   CA   sing N N 248 
HIS   N   H    sing N N 249 
HIS   N   H2   sing N N 250 
HIS   CA  C    sing N N 251 
HIS   CA  CB   sing N N 252 
HIS   CA  HA   sing N N 253 
HIS   C   O    doub N N 254 
HIS   C   OXT  sing N N 255 
HIS   CB  CG   sing N N 256 
HIS   CB  HB2  sing N N 257 
HIS   CB  HB3  sing N N 258 
HIS   CG  ND1  sing Y N 259 
HIS   CG  CD2  doub Y N 260 
HIS   ND1 CE1  doub Y N 261 
HIS   ND1 HD1  sing N N 262 
HIS   CD2 NE2  sing Y N 263 
HIS   CD2 HD2  sing N N 264 
HIS   CE1 NE2  sing Y N 265 
HIS   CE1 HE1  sing N N 266 
HIS   NE2 HE2  sing N N 267 
HIS   OXT HXT  sing N N 268 
HOH   O   H1   sing N N 269 
HOH   O   H2   sing N N 270 
ILE   N   CA   sing N N 271 
ILE   N   H    sing N N 272 
ILE   N   H2   sing N N 273 
ILE   CA  C    sing N N 274 
ILE   CA  CB   sing N N 275 
ILE   CA  HA   sing N N 276 
ILE   C   O    doub N N 277 
ILE   C   OXT  sing N N 278 
ILE   CB  CG1  sing N N 279 
ILE   CB  CG2  sing N N 280 
ILE   CB  HB   sing N N 281 
ILE   CG1 CD1  sing N N 282 
ILE   CG1 HG12 sing N N 283 
ILE   CG1 HG13 sing N N 284 
ILE   CG2 HG21 sing N N 285 
ILE   CG2 HG22 sing N N 286 
ILE   CG2 HG23 sing N N 287 
ILE   CD1 HD11 sing N N 288 
ILE   CD1 HD12 sing N N 289 
ILE   CD1 HD13 sing N N 290 
ILE   OXT HXT  sing N N 291 
LEU   N   CA   sing N N 292 
LEU   N   H    sing N N 293 
LEU   N   H2   sing N N 294 
LEU   CA  C    sing N N 295 
LEU   CA  CB   sing N N 296 
LEU   CA  HA   sing N N 297 
LEU   C   O    doub N N 298 
LEU   C   OXT  sing N N 299 
LEU   CB  CG   sing N N 300 
LEU   CB  HB2  sing N N 301 
LEU   CB  HB3  sing N N 302 
LEU   CG  CD1  sing N N 303 
LEU   CG  CD2  sing N N 304 
LEU   CG  HG   sing N N 305 
LEU   CD1 HD11 sing N N 306 
LEU   CD1 HD12 sing N N 307 
LEU   CD1 HD13 sing N N 308 
LEU   CD2 HD21 sing N N 309 
LEU   CD2 HD22 sing N N 310 
LEU   CD2 HD23 sing N N 311 
LEU   OXT HXT  sing N N 312 
LYS   N   CA   sing N N 313 
LYS   N   H    sing N N 314 
LYS   N   H2   sing N N 315 
LYS   CA  C    sing N N 316 
LYS   CA  CB   sing N N 317 
LYS   CA  HA   sing N N 318 
LYS   C   O    doub N N 319 
LYS   C   OXT  sing N N 320 
LYS   CB  CG   sing N N 321 
LYS   CB  HB2  sing N N 322 
LYS   CB  HB3  sing N N 323 
LYS   CG  CD   sing N N 324 
LYS   CG  HG2  sing N N 325 
LYS   CG  HG3  sing N N 326 
LYS   CD  CE   sing N N 327 
LYS   CD  HD2  sing N N 328 
LYS   CD  HD3  sing N N 329 
LYS   CE  NZ   sing N N 330 
LYS   CE  HE2  sing N N 331 
LYS   CE  HE3  sing N N 332 
LYS   NZ  HZ1  sing N N 333 
LYS   NZ  HZ2  sing N N 334 
LYS   NZ  HZ3  sing N N 335 
LYS   OXT HXT  sing N N 336 
MET   N   CA   sing N N 337 
MET   N   H    sing N N 338 
MET   N   H2   sing N N 339 
MET   CA  C    sing N N 340 
MET   CA  CB   sing N N 341 
MET   CA  HA   sing N N 342 
MET   C   O    doub N N 343 
MET   C   OXT  sing N N 344 
MET   CB  CG   sing N N 345 
MET   CB  HB2  sing N N 346 
MET   CB  HB3  sing N N 347 
MET   CG  SD   sing N N 348 
MET   CG  HG2  sing N N 349 
MET   CG  HG3  sing N N 350 
MET   SD  CE   sing N N 351 
MET   CE  HE1  sing N N 352 
MET   CE  HE2  sing N N 353 
MET   CE  HE3  sing N N 354 
MET   OXT HXT  sing N N 355 
PHE   N   CA   sing N N 356 
PHE   N   H    sing N N 357 
PHE   N   H2   sing N N 358 
PHE   CA  C    sing N N 359 
PHE   CA  CB   sing N N 360 
PHE   CA  HA   sing N N 361 
PHE   C   O    doub N N 362 
PHE   C   OXT  sing N N 363 
PHE   CB  CG   sing N N 364 
PHE   CB  HB2  sing N N 365 
PHE   CB  HB3  sing N N 366 
PHE   CG  CD1  doub Y N 367 
PHE   CG  CD2  sing Y N 368 
PHE   CD1 CE1  sing Y N 369 
PHE   CD1 HD1  sing N N 370 
PHE   CD2 CE2  doub Y N 371 
PHE   CD2 HD2  sing N N 372 
PHE   CE1 CZ   doub Y N 373 
PHE   CE1 HE1  sing N N 374 
PHE   CE2 CZ   sing Y N 375 
PHE   CE2 HE2  sing N N 376 
PHE   CZ  HZ   sing N N 377 
PHE   OXT HXT  sing N N 378 
PRO   N   CA   sing N N 379 
PRO   N   CD   sing N N 380 
PRO   N   H    sing N N 381 
PRO   CA  C    sing N N 382 
PRO   CA  CB   sing N N 383 
PRO   CA  HA   sing N N 384 
PRO   C   O    doub N N 385 
PRO   C   OXT  sing N N 386 
PRO   CB  CG   sing N N 387 
PRO   CB  HB2  sing N N 388 
PRO   CB  HB3  sing N N 389 
PRO   CG  CD   sing N N 390 
PRO   CG  HG2  sing N N 391 
PRO   CG  HG3  sing N N 392 
PRO   CD  HD2  sing N N 393 
PRO   CD  HD3  sing N N 394 
PRO   OXT HXT  sing N N 395 
SER   N   CA   sing N N 396 
SER   N   H    sing N N 397 
SER   N   H2   sing N N 398 
SER   CA  C    sing N N 399 
SER   CA  CB   sing N N 400 
SER   CA  HA   sing N N 401 
SER   C   O    doub N N 402 
SER   C   OXT  sing N N 403 
SER   CB  OG   sing N N 404 
SER   CB  HB2  sing N N 405 
SER   CB  HB3  sing N N 406 
SER   OG  HG   sing N N 407 
SER   OXT HXT  sing N N 408 
THR   N   CA   sing N N 409 
THR   N   H    sing N N 410 
THR   N   H2   sing N N 411 
THR   CA  C    sing N N 412 
THR   CA  CB   sing N N 413 
THR   CA  HA   sing N N 414 
THR   C   O    doub N N 415 
THR   C   OXT  sing N N 416 
THR   CB  OG1  sing N N 417 
THR   CB  CG2  sing N N 418 
THR   CB  HB   sing N N 419 
THR   OG1 HG1  sing N N 420 
THR   CG2 HG21 sing N N 421 
THR   CG2 HG22 sing N N 422 
THR   CG2 HG23 sing N N 423 
THR   OXT HXT  sing N N 424 
TRP   N   CA   sing N N 425 
TRP   N   H    sing N N 426 
TRP   N   H2   sing N N 427 
TRP   CA  C    sing N N 428 
TRP   CA  CB   sing N N 429 
TRP   CA  HA   sing N N 430 
TRP   C   O    doub N N 431 
TRP   C   OXT  sing N N 432 
TRP   CB  CG   sing N N 433 
TRP   CB  HB2  sing N N 434 
TRP   CB  HB3  sing N N 435 
TRP   CG  CD1  doub Y N 436 
TRP   CG  CD2  sing Y N 437 
TRP   CD1 NE1  sing Y N 438 
TRP   CD1 HD1  sing N N 439 
TRP   CD2 CE2  doub Y N 440 
TRP   CD2 CE3  sing Y N 441 
TRP   NE1 CE2  sing Y N 442 
TRP   NE1 HE1  sing N N 443 
TRP   CE2 CZ2  sing Y N 444 
TRP   CE3 CZ3  doub Y N 445 
TRP   CE3 HE3  sing N N 446 
TRP   CZ2 CH2  doub Y N 447 
TRP   CZ2 HZ2  sing N N 448 
TRP   CZ3 CH2  sing Y N 449 
TRP   CZ3 HZ3  sing N N 450 
TRP   CH2 HH2  sing N N 451 
TRP   OXT HXT  sing N N 452 
TYR   N   CA   sing N N 453 
TYR   N   H    sing N N 454 
TYR   N   H2   sing N N 455 
TYR   CA  C    sing N N 456 
TYR   CA  CB   sing N N 457 
TYR   CA  HA   sing N N 458 
TYR   C   O    doub N N 459 
TYR   C   OXT  sing N N 460 
TYR   CB  CG   sing N N 461 
TYR   CB  HB2  sing N N 462 
TYR   CB  HB3  sing N N 463 
TYR   CG  CD1  doub Y N 464 
TYR   CG  CD2  sing Y N 465 
TYR   CD1 CE1  sing Y N 466 
TYR   CD1 HD1  sing N N 467 
TYR   CD2 CE2  doub Y N 468 
TYR   CD2 HD2  sing N N 469 
TYR   CE1 CZ   doub Y N 470 
TYR   CE1 HE1  sing N N 471 
TYR   CE2 CZ   sing Y N 472 
TYR   CE2 HE2  sing N N 473 
TYR   CZ  OH   sing N N 474 
TYR   OH  HH   sing N N 475 
TYR   OXT HXT  sing N N 476 
VAL   N   CA   sing N N 477 
VAL   N   H    sing N N 478 
VAL   N   H2   sing N N 479 
VAL   CA  C    sing N N 480 
VAL   CA  CB   sing N N 481 
VAL   CA  HA   sing N N 482 
VAL   C   O    doub N N 483 
VAL   C   OXT  sing N N 484 
VAL   CB  CG1  sing N N 485 
VAL   CB  CG2  sing N N 486 
VAL   CB  HB   sing N N 487 
VAL   CG1 HG11 sing N N 488 
VAL   CG1 HG12 sing N N 489 
VAL   CG1 HG13 sing N N 490 
VAL   CG2 HG21 sing N N 491 
VAL   CG2 HG22 sing N N 492 
VAL   CG2 HG23 sing N N 493 
VAL   OXT HXT  sing N N 494 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4hka 
_pdbx_initial_refinement_model.details          'internal structure' 
# 
_atom_sites.entry_id                    9ESF 
_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]   0.006955 
_atom_sites.fract_transf_matrix[1][2]   0.004016 
_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]   0.008031 
_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]   0.007049 
_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   . LYS   A 1 3   ? 19.493 96.028  51.614 1   56.85  ? 25  LYS   A N   1 
ATOM   2     C  CA  . LYS   A 1 3   ? 20.324 96.126  52.821 1   57.33  ? 25  LYS   A CA  1 
ATOM   3     C  C   . LYS   A 1 3   ? 20.71  94.743  53.38  1   57.44  ? 25  LYS   A C   1 
ATOM   4     O  O   . LYS   A 1 3   ? 21.907 94.49   53.525 1   58.2   ? 25  LYS   A O   1 
ATOM   5     C  CB  . LYS   A 1 3   ? 19.677 96.996  53.913 1   59.06  ? 25  LYS   A CB  1 
ATOM   6     C  CG  . LYS   A 1 3   ? 19.16  98.34   53.426 1   62.75  ? 25  LYS   A CG  1 
ATOM   7     C  CD  . LYS   A 1 3   ? 18.316 98.988  54.519 1   67.01  ? 25  LYS   A CD  1 
ATOM   8     C  CE  . LYS   A 1 3   ? 18.039 100.457 54.307 1   70.71  ? 25  LYS   A CE  1 
ATOM   9     N  NZ  . LYS   A 1 3   ? 17.488 101.085 55.545 1   72.39  ? 25  LYS   A NZ  1 
ATOM   10    N  N   . ILE   A 1 4   ? 19.733 93.845  53.685 1   56.4   ? 26  ILE   A N   1 
ATOM   11    C  CA  . ILE   A 1 4   ? 20.093 92.501  54.169 1   56.22  ? 26  ILE   A CA  1 
ATOM   12    C  C   . ILE   A 1 4   ? 20.577 91.598  53.011 1   56.08  ? 26  ILE   A C   1 
ATOM   13    O  O   . ILE   A 1 4   ? 20.226 91.856  51.867 1   56.53  ? 26  ILE   A O   1 
ATOM   14    C  CB  . ILE   A 1 4   ? 18.965 91.835  54.989 1   56.34  ? 26  ILE   A CB  1 
ATOM   15    C  CG1 . ILE   A 1 4   ? 17.799 91.412  54.108 1   56.82  ? 26  ILE   A CG1 1 
ATOM   16    C  CG2 . ILE   A 1 4   ? 18.526 92.713  56.138 1   56.89  ? 26  ILE   A CG2 1 
ATOM   17    C  CD1 . ILE   A 1 4   ? 16.822 90.494  54.784 1   57.81  ? 26  ILE   A CD1 1 
ATOM   18    N  N   . TYR   A 1 5   ? 21.366 90.548  53.31  1   55.15  ? 27  TYR   A N   1 
ATOM   19    C  CA  . TYR   A 1 5   ? 21.94  89.603  52.332 1   54.42  ? 27  TYR   A CA  1 
ATOM   20    C  C   . TYR   A 1 5   ? 20.993 89.202  51.169 1   54.45  ? 27  TYR   A C   1 
ATOM   21    O  O   . TYR   A 1 5   ? 21.344 89.402  50.012 1   55.09  ? 27  TYR   A O   1 
ATOM   22    C  CB  . TYR   A 1 5   ? 22.486 88.352  53.064 1   53.72  ? 27  TYR   A CB  1 
ATOM   23    C  CG  . TYR   A 1 5   ? 23.222 87.352  52.193 1   53.41  ? 27  TYR   A CG  1 
ATOM   24    C  CD1 . TYR   A 1 5   ? 24.58  87.49   51.935 1   53.83  ? 27  TYR   A CD1 1 
ATOM   25    C  CD2 . TYR   A 1 5   ? 22.584 86.217  51.711 1   53.47  ? 27  TYR   A CD2 1 
ATOM   26    C  CE1 . TYR   A 1 5   ? 25.268 86.557  51.168 1   54.21  ? 27  TYR   A CE1 1 
ATOM   27    C  CE2 . TYR   A 1 5   ? 23.257 85.287  50.931 1   54.03  ? 27  TYR   A CE2 1 
ATOM   28    C  CZ  . TYR   A 1 5   ? 24.602 85.456  50.667 1   54.64  ? 27  TYR   A CZ  1 
ATOM   29    O  OH  . TYR   A 1 5   ? 25.262 84.538  49.89  1   55.49  ? 27  TYR   A OH  1 
ATOM   30    N  N   . GLY   A 1 6   ? 19.827 88.651  51.474 1   53.95  ? 28  GLY   A N   1 
ATOM   31    C  CA  . GLY   A 1 6   ? 18.882 88.204  50.459 1   53.93  ? 28  GLY   A CA  1 
ATOM   32    C  C   . GLY   A 1 6   ? 18.259 89.33   49.668 1   54.44  ? 28  GLY   A C   1 
ATOM   33    O  O   . GLY   A 1 6   ? 17.916 89.155  48.493 1   55.06  ? 28  GLY   A O   1 
ATOM   34    N  N   . GLU   A 1 7   ? 18.1   90.499  50.302 1   54.22  ? 29  GLU   A N   1 
ATOM   35    C  CA  . GLU   A 1 7   ? 17.525 91.662  49.637 1   54.6   ? 29  GLU   A CA  1 
ATOM   36    C  C   . GLU   A 1 7   ? 18.547 92.335  48.728 1   53.56  ? 29  GLU   A C   1 
ATOM   37    O  O   . GLU   A 1 7   ? 18.209 92.767  47.627 1   53.08  ? 29  GLU   A O   1 
ATOM   38    C  CB  . GLU   A 1 7   ? 16.984 92.661  50.663 1   58.37  ? 29  GLU   A CB  1 
ATOM   39    C  CG  . GLU   A 1 7   ? 15.611 92.284  51.194 1   66.49  ? 29  GLU   A CG  1 
ATOM   40    C  CD  . GLU   A 1 7   ? 15.198 93.011  52.461 1   76.21  ? 29  GLU   A CD  1 
ATOM   41    O  OE1 . GLU   A 1 7   ? 15.863 94.014  52.816 1   78.64  ? 29  GLU   A OE1 1 
ATOM   42    O  OE2 . GLU   A 1 7   ? 14.212 92.574  53.102 1   78.52  ? 29  GLU   A OE2 1 
ATOM   43    N  N   . TYR   A 1 8   ? 19.796 92.409  49.19  1   52.93  ? 30  TYR   A N   1 
ATOM   44    C  CA  . TYR   A 1 8   ? 20.895 93.018  48.465 1   52.75  ? 30  TYR   A CA  1 
ATOM   45    C  C   . TYR   A 1 8   ? 21.188 92.221  47.203 1   52.08  ? 30  TYR   A C   1 
ATOM   46    O  O   . TYR   A 1 8   ? 21.236 92.786  46.11  1   52.2   ? 30  TYR   A O   1 
ATOM   47    C  CB  . TYR   A 1 8   ? 22.139 93.115  49.368 1   52.94  ? 30  TYR   A CB  1 
ATOM   48    C  CG  . TYR   A 1 8   ? 23.359 93.639  48.646 1   53.8   ? 30  TYR   A CG  1 
ATOM   49    C  CD1 . TYR   A 1 8   ? 23.442 94.966  48.256 1   54.63  ? 30  TYR   A CD1 1 
ATOM   50    C  CD2 . TYR   A 1 8   ? 24.408 92.794  48.309 1   54.51  ? 30  TYR   A CD2 1 
ATOM   51    C  CE1 . TYR   A 1 8   ? 24.554 95.448  47.581 1   55.6   ? 30  TYR   A CE1 1 
ATOM   52    C  CE2 . TYR   A 1 8   ? 25.509 93.257  47.607 1   55.19  ? 30  TYR   A CE2 1 
ATOM   53    C  CZ  . TYR   A 1 8   ? 25.588 94.59   47.262 1   56.2   ? 30  TYR   A CZ  1 
ATOM   54    O  OH  . TYR   A 1 8   ? 26.7   95.05   46.615 1   57.46  ? 30  TYR   A OH  1 
ATOM   55    N  N   . LEU   A 1 9   ? 21.337 90.904  47.347 1   51.16  ? 31  LEU   A N   1 
ATOM   56    C  CA  . LEU   A 1 9   ? 21.618 90.047  46.21  1   50.88  ? 31  LEU   A CA  1 
ATOM   57    C  C   . LEU   A 1 9   ? 20.387 89.672  45.4   1   51.26  ? 31  LEU   A C   1 
ATOM   58    O  O   . LEU   A 1 9   ? 20.532 88.958  44.414 1   51.74  ? 31  LEU   A O   1 
ATOM   59    C  CB  . LEU   A 1 9   ? 22.345 88.785  46.663 1   50.54  ? 31  LEU   A CB  1 
ATOM   60    C  CG  . LEU   A 1 9   ? 23.636 89.003  47.416 1   51.27  ? 31  LEU   A CG  1 
ATOM   61    C  CD1 . LEU   A 1 9   ? 24.147 87.699  47.942 1   51.85  ? 31  LEU   A CD1 1 
ATOM   62    C  CD2 . LEU   A 1 9   ? 24.671 89.638  46.544 1   51.35  ? 31  LEU   A CD2 1 
ATOM   63    N  N   . MET   A 1 10  ? 19.18  90.107  45.808 1   51.1   ? 32  MET   A N   1 
ATOM   64    C  CA  . MET   A 1 10  ? 17.92  89.835  45.115 1   51.53  ? 32  MET   A CA  1 
ATOM   65    C  C   . MET   A 1 10  ? 17.74  88.355  44.829 1   52.32  ? 32  MET   A C   1 
ATOM   66    O  O   . MET   A 1 10  ? 17.493 87.934  43.702 1   52.53  ? 32  MET   A O   1 
ATOM   67    C  CB  . MET   A 1 10  ? 17.761 90.706  43.865 1   51.86  ? 32  MET   A CB  1 
ATOM   68    C  CG  . MET   A 1 10  ? 17.65  92.177  44.208 1   54.38  ? 32  MET   A CG  1 
ATOM   69    S  SD  . MET   A 1 10  ? 17.823 93.328  42.814 1   59.93  ? 32  MET   A SD  1 
ATOM   70    C  CE  . MET   A 1 10  ? 16.441 92.959  41.925 1   53.94  ? 32  MET   A CE  1 
ATOM   71    N  N   . LEU   A 1 11  ? 17.908 87.566  45.88  1   52.49  ? 33  LEU   A N   1 
ATOM   72    C  CA  . LEU   A 1 11  ? 17.774 86.127  45.807 1   53.02  ? 33  LEU   A CA  1 
ATOM   73    C  C   . LEU   A 1 11  ? 16.331 85.672  45.559 1   54.64  ? 33  LEU   A C   1 
ATOM   74    O  O   . LEU   A 1 11  ? 16.124 84.552  45.101 1   54.9   ? 33  LEU   A O   1 
ATOM   75    C  CB  . LEU   A 1 11  ? 18.388 85.49   47.058 1   52.39  ? 33  LEU   A CB  1 
ATOM   76    C  CG  . LEU   A 1 11  ? 19.848 85.876  47.317 1   52.61  ? 33  LEU   A CG  1 
ATOM   77    C  CD1 . LEU   A 1 11  ? 20.333 85.288  48.582 1   52.96  ? 33  LEU   A CD1 1 
ATOM   78    C  CD2 . LEU   A 1 11  ? 20.745 85.432  46.186 1   53.08  ? 33  LEU   A CD2 1 
ATOM   79    N  N   . ASP   A 1 12  ? 15.331 86.541  45.816 1   55.56  ? 34  ASP   A N   1 
ATOM   80    C  CA  . ASP   A 1 12  ? 13.939 86.207  45.509 1   56.67  ? 34  ASP   A CA  1 
ATOM   81    C  C   . ASP   A 1 12  ? 13.664 86.229  43.987 1   56.17  ? 34  ASP   A C   1 
ATOM   82    O  O   . ASP   A 1 12  ? 12.692 85.632  43.522 1   56.31  ? 34  ASP   A O   1 
ATOM   83    C  CB  . ASP   A 1 12  ? 12.98  87.13   46.266 1   60.41  ? 34  ASP   A CB  1 
ATOM   84    C  CG  . ASP   A 1 12  ? 12.752 86.723  47.723 1   69.05  ? 34  ASP   A CG  1 
ATOM   85    O  OD1 . ASP   A 1 12  ? 12.941 85.511  48.053 1   70.08  ? 34  ASP   A OD1 1 
ATOM   86    O  OD2 . ASP   A 1 12  ? 12.363 87.601  48.531 1   72.89  ? 34  ASP   A OD2 1 
ATOM   87    N  N   . LYS   A 1 13  ? 14.541 86.896  43.221 1   55.16  ? 35  LYS   A N   1 
ATOM   88    C  CA  . LYS   A 1 13  ? 14.48  87.024  41.777 1   54.45  ? 35  LYS   A CA  1 
ATOM   89    C  C   . LYS   A 1 13  ? 15.422 85.959  41.17  1   53.47  ? 35  LYS   A C   1 
ATOM   90    O  O   . LYS   A 1 13  ? 15.02  85.208  40.278 1   53.58  ? 35  LYS   A O   1 
ATOM   91    C  CB  . LYS   A 1 13  ? 14.935 88.451  41.413 1   56.1   ? 35  LYS   A CB  1 
ATOM   92    C  CG  . LYS   A 1 13  ? 14.658 88.877  39.999 1   60.4   ? 35  LYS   A CG  1 
ATOM   93    C  CD  . LYS   A 1 13  ? 15.022 90.338  39.794 1   65.05  ? 35  LYS   A CD  1 
ATOM   94    C  CE  . LYS   A 1 13  ? 13.913 91.273  40.208 1   69.38  ? 35  LYS   A CE  1 
ATOM   95    N  NZ  . LYS   A 1 13  ? 14.217 92.695  39.868 1   71.49  ? 35  LYS   A NZ  1 
ATOM   96    N  N   . LEU   A 1 14  ? 16.659 85.872  41.699 1   52.23  ? 36  LEU   A N   1 
ATOM   97    C  CA  . LEU   A 1 14  ? 17.688 84.944  41.245 1   51.56  ? 36  LEU   A CA  1 
ATOM   98    C  C   . LEU   A 1 14  ? 17.306 83.483  41.496 1   51.86  ? 36  LEU   A C   1 
ATOM   99    O  O   . LEU   A 1 14  ? 17.375 82.663  40.576 1   51.9   ? 36  LEU   A O   1 
ATOM   100   C  CB  . LEU   A 1 14  ? 19.046 85.275  41.904 1   50.96  ? 36  LEU   A CB  1 
ATOM   101   C  CG  . LEU   A 1 14  ? 20.235 84.428  41.439 1   51.07  ? 36  LEU   A CG  1 
ATOM   102   C  CD1 . LEU   A 1 14  ? 21.015 85.136  40.388 1   51.13  ? 36  LEU   A CD1 1 
ATOM   103   C  CD2 . LEU   A 1 14  ? 21.153 84.097  42.589 1   51.48  ? 36  LEU   A CD2 1 
ATOM   104   N  N   . LEU   A 1 15  ? 16.898 83.149  42.736 1   51.64  ? 37  LEU   A N   1 
ATOM   105   C  CA  . LEU   A 1 15  ? 16.525 81.774  43.071 1   51.62  ? 37  LEU   A CA  1 
ATOM   106   C  C   . LEU   A 1 15  ? 15.087 81.394  42.65  1   51.91  ? 37  LEU   A C   1 
ATOM   107   O  O   . LEU   A 1 15  ? 14.577 80.354  43.063 1   51.5   ? 37  LEU   A O   1 
ATOM   108   C  CB  . LEU   A 1 15  ? 16.781 81.473  44.557 1   51.38  ? 37  LEU   A CB  1 
ATOM   109   C  CG  . LEU   A 1 15  ? 18.204 81.072  45.042 1   52.18  ? 37  LEU   A CG  1 
ATOM   110   C  CD1 . LEU   A 1 15  ? 19.275 81.053  43.927 1   52.38  ? 37  LEU   A CD1 1 
ATOM   111   C  CD2 . LEU   A 1 15  ? 18.65  81.929  46.211 1   52.68  ? 37  LEU   A CD2 1 
ATOM   112   N  N   . ASP   A 1 16  ? 14.483 82.195  41.76  1   52.52  ? 38  ASP   A N   1 
ATOM   113   C  CA  . ASP   A 1 16  ? 13.167 81.943  41.185 1   53.69  ? 38  ASP   A CA  1 
ATOM   114   C  C   . ASP   A 1 16  ? 13.236 81.752  39.634 1   53.84  ? 38  ASP   A C   1 
ATOM   115   O  O   . ASP   A 1 16  ? 12.209 81.554  38.991 1   53.8   ? 38  ASP   A O   1 
ATOM   116   C  CB  . ASP   A 1 16  ? 12.228 83.094  41.564 1   56.62  ? 38  ASP   A CB  1 
ATOM   117   C  CG  . ASP   A 1 16  ? 10.745 82.816  41.41  1   62.9   ? 38  ASP   A CG  1 
ATOM   118   O  OD1 . ASP   A 1 16  ? 10.307 81.683  41.753 1   62.71  ? 38  ASP   A OD1 1 
ATOM   119   O  OD2 . ASP   A 1 16  ? 10.013 83.736  40.966 1   66.74  ? 38  ASP   A OD2 1 
ATOM   120   N  N   . ALA   A 1 17  ? 14.441 81.809  39.04  1   53.75  ? 39  ALA   A N   1 
ATOM   121   C  CA  . ALA   A 1 17  ? 14.644 81.646  37.604 1   53.99  ? 39  ALA   A CA  1 
ATOM   122   C  C   . ALA   A 1 17  ? 14.929 80.204  37.192 1   54.16  ? 39  ALA   A C   1 
ATOM   123   O  O   . ALA   A 1 17  ? 15.35  79.989  36.058 1   54.33  ? 39  ALA   A O   1 
ATOM   124   C  CB  . ALA   A 1 17  ? 15.784 82.542  37.131 1   54.07  ? 39  ALA   A CB  1 
ATOM   125   N  N   . GLN   A 1 18  ? 14.695 79.218  38.072 1   54.05  ? 40  GLN   A N   1 
ATOM   126   C  CA  . GLN   A 1 18  ? 14.97  77.824  37.724 1   54.44  ? 40  GLN   A CA  1 
ATOM   127   C  C   . GLN   A 1 18  ? 13.698 77.052  37.419 1   56     ? 40  GLN   A C   1 
ATOM   128   O  O   . GLN   A 1 18  ? 12.931 76.713  38.331 1   56.36  ? 40  GLN   A O   1 
ATOM   129   C  CB  . GLN   A 1 18  ? 15.818 77.138  38.797 1   53.98  ? 40  GLN   A CB  1 
ATOM   130   C  CG  . GLN   A 1 18  ? 17.187 77.786  38.963 1   54.38  ? 40  GLN   A CG  1 
ATOM   131   C  CD  . GLN   A 1 18  ? 17.111 79.042  39.784 1   55.81  ? 40  GLN   A CD  1 
ATOM   132   O  OE1 . GLN   A 1 18  ? 16.323 79.133  40.715 1   57.3   ? 40  GLN   A OE1 1 
ATOM   133   N  NE2 . GLN   A 1 18  ? 17.902 80.048  39.446 1   55.2   ? 40  GLN   A NE2 1 
ATOM   134   N  N   . CYS   A 1 19  ? 13.457 76.795  36.123 1   56.64  ? 41  CYS   A N   1 
ATOM   135   C  CA  . CYS   A 1 19  ? 12.248 76.099  35.714 1   57.8   ? 41  CYS   A CA  1 
ATOM   136   C  C   . CYS   A 1 19  ? 12.514 74.896  34.819 1   58.99  ? 41  CYS   A C   1 
ATOM   137   O  O   . CYS   A 1 19  ? 12.769 75.051  33.624 1   59.4   ? 41  CYS   A O   1 
ATOM   138   C  CB  . CYS   A 1 19  ? 11.263 77.069  35.073 1   58.38  ? 41  CYS   A CB  1 
ATOM   139   S  SG  . CYS   A 1 19  ? 9.649  76.342  34.693 1   61.51  ? 41  CYS   A SG  1 
ATOM   140   N  N   . MET   A 1 20  ? 12.427 73.69   35.399 1   59.24  ? 42  MET   A N   1 
ATOM   141   C  CA  . MET   A 1 20  ? 12.623 72.445  34.669 1   59.71  ? 42  MET   A CA  1 
ATOM   142   C  C   . MET   A 1 20  ? 11.381 72.14   33.851 1   61.12  ? 42  MET   A C   1 
ATOM   143   O  O   . MET   A 1 20  ? 10.301 71.997  34.419 1   61.8   ? 42  MET   A O   1 
ATOM   144   C  CB  . MET   A 1 20  ? 12.88  71.293  35.651 1   59.13  ? 42  MET   A CB  1 
ATOM   145   C  CG  . MET   A 1 20  ? 14.233 71.338  36.289 1   59.84  ? 42  MET   A CG  1 
ATOM   146   S  SD  . MET   A 1 20  ? 14.384 70.285  37.759 1   60.46  ? 42  MET   A SD  1 
ATOM   147   C  CE  . MET   A 1 20  ? 13.936 68.691  37.096 1   58.41  ? 42  MET   A CE  1 
ATOM   148   N  N   . LEU   A 1 21  ? 11.521 72.031  32.531 1   61.63  ? 43  LEU   A N   1 
ATOM   149   C  CA  . LEU   A 1 21  ? 10.397 71.695  31.659 1   62.83  ? 43  LEU   A CA  1 
ATOM   150   C  C   . LEU   A 1 21  ? 10.016 70.206  31.707 1   65.01  ? 43  LEU   A C   1 
ATOM   151   O  O   . LEU   A 1 21  ? 8.896  69.855  31.331 1   65     ? 43  LEU   A O   1 
ATOM   152   C  CB  . LEU   A 1 21  ? 10.653 72.157  30.228 1   62.31  ? 43  LEU   A CB  1 
ATOM   153   C  CG  . LEU   A 1 21  ? 11.006 73.631  30.071 1   62.98  ? 43  LEU   A CG  1 
ATOM   154   C  CD1 . LEU   A 1 21  ? 11.242 73.964  28.627 1   63.46  ? 43  LEU   A CD1 1 
ATOM   155   C  CD2 . LEU   A 1 21  ? 9.916  74.537  30.629 1   63.29  ? 43  LEU   A CD2 1 
ATOM   156   N  N   . SER   A 1 22  ? 10.93  69.335  32.18  1   66.67  ? 44  SER   A N   1 
ATOM   157   C  CA  . SER   A 1 22  ? 10.625 67.92   32.355 1   68.65  ? 44  SER   A CA  1 
ATOM   158   C  C   . SER   A 1 22  ? 9.712  67.771  33.592 1   71.43  ? 44  SER   A C   1 
ATOM   159   O  O   . SER   A 1 22  ? 8.762  66.998  33.557 1   71.71  ? 44  SER   A O   1 
ATOM   160   C  CB  . SER   A 1 22  ? 11.902 67.103  32.521 1   68.87  ? 44  SER   A CB  1 
ATOM   161   O  OG  . SER   A 1 22  ? 12.581 67.453  33.714 1   70.1   ? 44  SER   A OG  1 
ATOM   162   N  N   . GLU   A 1 23  ? 9.975  68.539  34.663 1   73.31  ? 45  GLU   A N   1 
ATOM   163   C  CA  . GLU   A 1 23  ? 9.161  68.544  35.88  1   75.82  ? 45  GLU   A CA  1 
ATOM   164   C  C   . GLU   A 1 23  ? 7.763  69.142  35.579 1   78.16  ? 45  GLU   A C   1 
ATOM   165   O  O   . GLU   A 1 23  ? 6.757  68.657  36.111 1   78.4   ? 45  GLU   A O   1 
ATOM   166   C  CB  . GLU   A 1 23  ? 9.867  69.372  36.962 1   78.28  ? 45  GLU   A CB  1 
ATOM   167   C  CG  . GLU   A 1 23  ? 9.244  69.296  38.343 1   83.19  ? 45  GLU   A CG  1 
ATOM   168   C  CD  . GLU   A 1 23  ? 9.907  70.196  39.373 1   89.18  ? 45  GLU   A CD  1 
ATOM   169   O  OE1 . GLU   A 1 23  ? 10.406 71.281  38.991 1   89.77  ? 45  GLU   A OE1 1 
ATOM   170   O  OE2 . GLU   A 1 23  ? 9.92   69.819  40.567 1   91.12  ? 45  GLU   A OE2 1 
ATOM   171   N  N   . GLU   A 1 24  ? 7.712  70.179  34.704 1   79.42  ? 46  GLU   A N   1 
ATOM   172   C  CA  . GLU   A 1 24  ? 6.499  70.865  34.23  1   80.89  ? 46  GLU   A CA  1 
ATOM   173   C  C   . GLU   A 1 24  ? 5.604  69.874  33.476 1   82     ? 46  GLU   A C   1 
ATOM   174   O  O   . GLU   A 1 24  ? 4.388  69.864  33.671 1   82.38  ? 46  GLU   A O   1 
ATOM   175   C  CB  . GLU   A 1 24  ? 6.891  72.061  33.319 1   83.37  ? 46  GLU   A CB  1 
ATOM   176   C  CG  . GLU   A 1 24  ? 5.794  72.623  32.418 1   88.22  ? 46  GLU   A CG  1 
ATOM   177   C  CD  . GLU   A 1 24  ? 5.868  72.218  30.955 1   95.61  ? 46  GLU   A CD  1 
ATOM   178   O  OE1 . GLU   A 1 24  ? 6.957  71.79   30.506 1   97.14  ? 46  GLU   A OE1 1 
ATOM   179   O  OE2 . GLU   A 1 24  ? 4.829  72.308  30.26  1   98.13  ? 46  GLU   A OE2 1 
ATOM   180   N  N   . ASP   A 1 25  ? 6.215  69.024  32.631 1   82.36  ? 47  ASP   A N   1 
ATOM   181   C  CA  . ASP   A 1 25  ? 5.486  68.016  31.854 1   82.96  ? 47  ASP   A CA  1 
ATOM   182   C  C   . ASP   A 1 25  ? 5.232  66.708  32.642 1   83.32  ? 47  ASP   A C   1 
ATOM   183   O  O   . ASP   A 1 25  ? 4.797  65.721  32.052 1   83.78  ? 47  ASP   A O   1 
ATOM   184   C  CB  . ASP   A 1 25  ? 6.247  67.708  30.559 1   84.54  ? 47  ASP   A CB  1 
ATOM   185   C  CG  . ASP   A 1 25  ? 5.355  67.565  29.342 1   88.73  ? 47  ASP   A CG  1 
ATOM   186   O  OD1 . ASP   A 1 25  ? 4.579  68.504  29.062 1   89.25  ? 47  ASP   A OD1 1 
ATOM   187   O  OD2 . ASP   A 1 25  ? 5.444  66.517  28.66  1   90.52  ? 47  ASP   A OD2 1 
ATOM   188   N  N   . LYS   A 1 26  ? 5.513  66.717  33.96  1   82.84  ? 48  LYS   A N   1 
ATOM   189   C  CA  . LYS   A 1 26  ? 5.396  65.644  34.933 1   82.82  ? 48  LYS   A CA  1 
ATOM   190   C  C   . LYS   A 1 26  ? 6.111  64.348  34.52  1   81.86  ? 48  LYS   A C   1 
ATOM   191   O  O   . LYS   A 1 26  ? 5.721  63.235  34.887 1   82.09  ? 48  LYS   A O   1 
ATOM   192   C  CB  . LYS   A 1 26  ? 3.958  65.435  35.341 1   85.54  ? 48  LYS   A CB  1 
ATOM   193   C  CG  . LYS   A 1 26  ? 3.602  66.465  36.421 1   90.56  ? 48  LYS   A CG  1 
ATOM   194   C  CD  . LYS   A 1 26  ? 4.27   66.093  37.766 1   95.55  ? 48  LYS   A CD  1 
ATOM   195   C  CE  . LYS   A 1 26  ? 3.773  66.877  38.954 1   99.77  ? 48  LYS   A CE  1 
ATOM   196   N  NZ  . LYS   A 1 26  ? 3.978  66.127  40.23  1   102.11 ? 48  LYS   A NZ  1 
ATOM   197   N  N   . ARG   A 1 27  ? 7.234  64.531  33.843 1   80.7   ? 49  ARG   A N   1 
ATOM   198   C  CA  . ARG   A 1 27  ? 8.162  63.481  33.468 1   80.24  ? 49  ARG   A CA  1 
ATOM   199   C  C   . ARG   A 1 27  ? 9.544  64.066  33.864 1   78.29  ? 49  ARG   A C   1 
ATOM   200   O  O   . ARG   A 1 27  ? 10.299 64.481  32.984 1   78.36  ? 49  ARG   A O   1 
ATOM   201   C  CB  . ARG   A 1 27  ? 8.087  63.229  31.954 1   82.7   ? 49  ARG   A CB  1 
ATOM   202   C  CG  . ARG   A 1 27  ? 6.804  62.566  31.479 1   87.77  ? 49  ARG   A CG  1 
ATOM   203   C  CD  . ARG   A 1 27  ? 6.611  62.687  29.966 1   93.53  ? 49  ARG   A CD  1 
ATOM   204   N  NE  . ARG   A 1 27  ? 7.733  62.154  29.181 1   98.81  ? 49  ARG   A NE  1 
ATOM   205   C  CZ  . ARG   A 1 27  ? 8.561  62.901  28.447 1   102.63 ? 49  ARG   A CZ  1 
ATOM   206   N  NH1 . ARG   A 1 27  ? 8.411  64.219  28.398 1   103.06 ? 49  ARG   A NH1 1 
ATOM   207   N  NH2 . ARG   A 1 27  ? 9.548  62.334  27.763 1   102.65 ? 49  ARG   A NH2 1 
ATOM   208   N  N   . PRO   A 1 28  ? 9.852  64.224  35.178 1   76.23  ? 50  PRO   A N   1 
ATOM   209   C  CA  . PRO   A 1 28  ? 11.1   64.91   35.545 1   74.22  ? 50  PRO   A CA  1 
ATOM   210   C  C   . PRO   A 1 28  ? 12.39  64.096  35.391 1   71.29  ? 50  PRO   A C   1 
ATOM   211   O  O   . PRO   A 1 28  ? 12.417 62.876  35.579 1   71.62  ? 50  PRO   A O   1 
ATOM   212   C  CB  . PRO   A 1 28  ? 10.858 65.364  36.989 1   75.34  ? 50  PRO   A CB  1 
ATOM   213   C  CG  . PRO   A 1 28  ? 9.821  64.461  37.513 1   76.42  ? 50  PRO   A CG  1 
ATOM   214   C  CD  . PRO   A 1 28  ? 9.062  63.853  36.372 1   75.43  ? 50  PRO   A CD  1 
ATOM   215   N  N   . VAL   A 1 29  ? 13.461 64.81   34.996 1   68.11  ? 51  VAL   A N   1 
ATOM   216   C  CA  . VAL   A 1 29  ? 14.816 64.304  34.821 1   65.53  ? 51  VAL   A CA  1 
ATOM   217   C  C   . VAL   A 1 29  ? 15.678 65.109  35.786 1   62.96  ? 51  VAL   A C   1 
ATOM   218   O  O   . VAL   A 1 29  ? 15.832 66.312  35.592 1   63.82  ? 51  VAL   A O   1 
ATOM   219   C  CB  . VAL   A 1 29  ? 15.315 64.496  33.369 1   65.73  ? 51  VAL   A CB  1 
ATOM   220   C  CG1 . VAL   A 1 29  ? 16.716 63.919  33.195 1   66.1   ? 51  VAL   A CG1 1 
ATOM   221   C  CG2 . VAL   A 1 29  ? 14.349 63.877  32.37  1   65.83  ? 51  VAL   A CG2 1 
ATOM   222   N  N   . HIS   A 1 30  ? 16.209 64.465  36.831 1   59.63  ? 52  HIS   A N   1 
ATOM   223   C  CA  . HIS   A 1 30  ? 17.023 65.088  37.871 1   56.88  ? 52  HIS   A CA  1 
ATOM   224   C  C   . HIS   A 1 30  ? 18.174 65.957  37.365 1   54.85  ? 52  HIS   A C   1 
ATOM   225   O  O   . HIS   A 1 30  ? 18.433 67.028  37.921 1   55.31  ? 52  HIS   A O   1 
ATOM   226   C  CB  . HIS   A 1 30  ? 17.569 64.005  38.811 1   56.74  ? 52  HIS   A CB  1 
ATOM   227   C  CG  . HIS   A 1 30  ? 18.308 64.55   39.989 1   57.98  ? 52  HIS   A CG  1 
ATOM   228   N  ND1 . HIS   A 1 30  ? 19.68  64.716  39.969 1   59.6   ? 52  HIS   A ND1 1 
ATOM   229   C  CD2 . HIS   A 1 30  ? 17.839 64.943  41.193 1   58.92  ? 52  HIS   A CD2 1 
ATOM   230   C  CE1 . HIS   A 1 30  ? 20     65.21   41.151 1   59.92  ? 52  HIS   A CE1 1 
ATOM   231   N  NE2 . HIS   A 1 30  ? 18.924 65.382  41.914 1   59.93  ? 52  HIS   A NE2 1 
ATOM   232   N  N   . ASP   A 1 31  ? 18.879 65.501  36.323 1   52.8   ? 53  ASP   A N   1 
ATOM   233   C  CA  . ASP   A 1 31  ? 20.028 66.224  35.786 1   50.97  ? 53  ASP   A CA  1 
ATOM   234   C  C   . ASP   A 1 31  ? 19.649 67.506  35.014 1   50.08  ? 53  ASP   A C   1 
ATOM   235   O  O   . ASP   A 1 31  ? 20.542 68.265  34.645 1   50.18  ? 53  ASP   A O   1 
ATOM   236   C  CB  . ASP   A 1 31  ? 20.927 65.293  34.953 1   51.22  ? 53  ASP   A CB  1 
ATOM   237   C  CG  . ASP   A 1 31  ? 21.713 64.257  35.761 1   54.36  ? 53  ASP   A CG  1 
ATOM   238   O  OD1 . ASP   A 1 31  ? 21.593 64.252  37.007 1   54.3   ? 53  ASP   A OD1 1 
ATOM   239   O  OD2 . ASP   A 1 31  ? 22.456 63.451  35.144 1   56.49  ? 53  ASP   A OD2 1 
ATOM   240   N  N   . GLU   A 1 32  ? 18.345 67.788  34.812 1   49.23  ? 54  GLU   A N   1 
ATOM   241   C  CA  . GLU   A 1 32  ? 17.932 69.028  34.138 1   48.75  ? 54  GLU   A CA  1 
ATOM   242   C  C   . GLU   A 1 32  ? 18.213 70.257  35.013 1   48.76  ? 54  GLU   A C   1 
ATOM   243   O  O   . GLU   A 1 32  ? 18.5   71.334  34.488 1   49.26  ? 54  GLU   A O   1 
ATOM   244   C  CB  . GLU   A 1 32  ? 16.452 69.003  33.711 1   50.05  ? 54  GLU   A CB  1 
ATOM   245   C  CG  . GLU   A 1 32  ? 16.101 70.217  32.865 1   52.68  ? 54  GLU   A CG  1 
ATOM   246   C  CD  . GLU   A 1 32  ? 14.681 70.351  32.367 1   56.66  ? 54  GLU   A CD  1 
ATOM   247   O  OE1 . GLU   A 1 32  ? 13.854 69.469  32.674 1   58.67  ? 54  GLU   A OE1 1 
ATOM   248   O  OE2 . GLU   A 1 32  ? 14.383 71.355  31.683 1   57.48  ? 54  GLU   A OE2 1 
ATOM   249   N  N   . HIS   A 1 33  ? 18.166 70.09   36.35  1   47.83  ? 55  HIS   A N   1 
ATOM   250   C  CA  . HIS   A 1 33  ? 18.468 71.152  37.294 1   47.25  ? 55  HIS   A CA  1 
ATOM   251   C  C   . HIS   A 1 33  ? 19.942 71.588  37.12  1   46.16  ? 55  HIS   A C   1 
ATOM   252   O  O   . HIS   A 1 33  ? 20.254 72.784  37.142 1   46.11  ? 55  HIS   A O   1 
ATOM   253   C  CB  . HIS   A 1 33  ? 18.209 70.638  38.714 1   48.47  ? 55  HIS   A CB  1 
ATOM   254   C  CG  . HIS   A 1 33  ? 18.063 71.714  39.751 1   51.13  ? 55  HIS   A CG  1 
ATOM   255   N  ND1 . HIS   A 1 33  ? 19.162 72.397  40.241 1   53.05  ? 55  HIS   A ND1 1 
ATOM   256   C  CD2 . HIS   A 1 33  ? 16.957 72.15   40.397 1   52.17  ? 55  HIS   A CD2 1 
ATOM   257   C  CE1 . HIS   A 1 33  ? 18.69  73.251  41.134 1   53.41  ? 55  HIS   A CE1 1 
ATOM   258   N  NE2 . HIS   A 1 33  ? 17.369 73.131  41.271 1   53.25  ? 55  HIS   A NE2 1 
ATOM   259   N  N   . LEU   A 1 34  ? 20.84  70.606  36.945 1   45.01  ? 56  LEU   A N   1 
ATOM   260   C  CA  . LEU   A 1 34  ? 22.258 70.846  36.755 1   44.36  ? 56  LEU   A CA  1 
ATOM   261   C  C   . LEU   A 1 34  ? 22.472 71.609  35.457 1   44.22  ? 56  LEU   A C   1 
ATOM   262   O  O   . LEU   A 1 34  ? 23.222 72.577  35.437 1   44.76  ? 56  LEU   A O   1 
ATOM   263   C  CB  . LEU   A 1 34  ? 23.024 69.51   36.741 1   44.06  ? 56  LEU   A CB  1 
ATOM   264   C  CG  . LEU   A 1 34  ? 24.515 69.623  36.504 1   44.92  ? 56  LEU   A CG  1 
ATOM   265   C  CD1 . LEU   A 1 34  ? 25.197 70.352  37.637 1   44.98  ? 56  LEU   A CD1 1 
ATOM   266   C  CD2 . LEU   A 1 34  ? 25.121 68.275  36.297 1   45.92  ? 56  LEU   A CD2 1 
ATOM   267   N  N   . PHE   A 1 35  ? 21.786 71.191  34.384 1   43.32  ? 57  PHE   A N   1 
ATOM   268   C  CA  . PHE   A 1 35  ? 21.829 71.821  33.073 1   42.75  ? 57  PHE   A CA  1 
ATOM   269   C  C   . PHE   A 1 35  ? 21.443 73.314  33.172 1   41.76  ? 57  PHE   A C   1 
ATOM   270   O  O   . PHE   A 1 35  ? 22.132 74.157  32.605 1   42.21  ? 57  PHE   A O   1 
ATOM   271   C  CB  . PHE   A 1 35  ? 20.897 71.063  32.11  1   43.09  ? 57  PHE   A CB  1 
ATOM   272   C  CG  . PHE   A 1 35  ? 21.014 71.467  30.662 1   44.45  ? 57  PHE   A CG  1 
ATOM   273   C  CD1 . PHE   A 1 35  ? 22.058 71.002  29.877 1   45.4   ? 57  PHE   A CD1 1 
ATOM   274   C  CD2 . PHE   A 1 35  ? 20.08  72.311  30.083 1   45.34  ? 57  PHE   A CD2 1 
ATOM   275   C  CE1 . PHE   A 1 35  ? 22.173 71.39   28.547 1   45.92  ? 57  PHE   A CE1 1 
ATOM   276   C  CE2 . PHE   A 1 35  ? 20.201 72.698  28.755 1   45.91  ? 57  PHE   A CE2 1 
ATOM   277   C  CZ  . PHE   A 1 35  ? 21.245 72.234  27.997 1   45.69  ? 57  PHE   A CZ  1 
ATOM   278   N  N   . ILE   A 1 36  ? 20.362 73.643  33.908 1   40.23  ? 58  ILE   A N   1 
ATOM   279   C  CA  . ILE   A 1 36  ? 19.91  75.028  34.089 1   39.05  ? 58  ILE   A CA  1 
ATOM   280   C  C   . ILE   A 1 36  ? 20.9   75.85   34.907 1   38.57  ? 58  ILE   A C   1 
ATOM   281   O  O   . ILE   A 1 36  ? 21.342 76.895  34.447 1   39     ? 58  ILE   A O   1 
ATOM   282   C  CB  . ILE   A 1 36  ? 18.48  75.074  34.682 1   38.78  ? 58  ILE   A CB  1 
ATOM   283   C  CG1 . ILE   A 1 36  ? 17.483 74.444  33.714 1   40.07  ? 58  ILE   A CG1 1 
ATOM   284   C  CG2 . ILE   A 1 36  ? 18.074 76.494  35.078 1   38.51  ? 58  ILE   A CG2 1 
ATOM   285   C  CD1 . ILE   A 1 36  ? 16.14  74.207  34.311 1   41.26  ? 58  ILE   A CD1 1 
ATOM   286   N  N   . ILE   A 1 37  ? 21.257 75.374  36.106 1   37.74  ? 59  ILE   A N   1 
ATOM   287   C  CA  . ILE   A 1 37  ? 22.198 76.05   36.986 1   37.46  ? 59  ILE   A CA  1 
ATOM   288   C  C   . ILE   A 1 37  ? 23.545 76.281  36.313 1   37.13  ? 59  ILE   A C   1 
ATOM   289   O  O   . ILE   A 1 37  ? 24.039 77.405  36.37  1   37.62  ? 59  ILE   A O   1 
ATOM   290   C  CB  . ILE   A 1 37  ? 22.318 75.291  38.334 1   37.81  ? 59  ILE   A CB  1 
ATOM   291   C  CG1 . ILE   A 1 37  ? 20.995 75.382  39.158 1   38.35  ? 59  ILE   A CG1 1 
ATOM   292   C  CG2 . ILE   A 1 37  ? 23.551 75.726  39.147 1   38.03  ? 59  ILE   A CG2 1 
ATOM   293   C  CD1 . ILE   A 1 37  ? 20.669 76.737  39.726 1   39.19  ? 59  ILE   A CD1 1 
ATOM   294   N  N   . THR   A 1 38  ? 24.12  75.263  35.636 1   36.02  ? 60  THR   A N   1 
ATOM   295   C  CA  . THR   A 1 38  ? 25.413 75.417  34.955 1   36.1   ? 60  THR   A CA  1 
ATOM   296   C  C   . THR   A 1 38  ? 25.352 76.538  33.907 1   36.51  ? 60  THR   A C   1 
ATOM   297   O  O   . THR   A 1 38  ? 26.24  77.376  33.845 1   36.69  ? 60  THR   A O   1 
ATOM   298   C  CB  . THR   A 1 38  ? 25.857 74.101  34.287 1   37     ? 60  THR   A CB  1 
ATOM   299   O  OG1 . THR   A 1 38  ? 25.884 73.037  35.243 1   38.32  ? 60  THR   A OG1 1 
ATOM   300   C  CG2 . THR   A 1 38  ? 27.215 74.217  33.596 1   36.65  ? 60  THR   A CG2 1 
ATOM   301   N  N   . HIS   A 1 39  ? 24.278 76.573  33.123 1   36.48  ? 61  HIS   A N   1 
ATOM   302   C  CA  . HIS   A 1 39  ? 24.091 77.574  32.095 1   37.15  ? 61  HIS   A CA  1 
ATOM   303   C  C   . HIS   A 1 39  ? 23.902 78.964  32.689 1   37.92  ? 61  HIS   A C   1 
ATOM   304   O  O   . HIS   A 1 39  ? 24.433 79.937  32.153 1   38.63  ? 61  HIS   A O   1 
ATOM   305   C  CB  . HIS   A 1 39  ? 22.912 77.182  31.199 1   37.81  ? 61  HIS   A CB  1 
ATOM   306   C  CG  . HIS   A 1 39  ? 23.29  76.324  30.024 1   38.95  ? 61  HIS   A CG  1 
ATOM   307   N  ND1 . HIS   A 1 39  ? 23.497 74.96   30.16  1   40.43  ? 61  HIS   A ND1 1 
ATOM   308   C  CD2 . HIS   A 1 39  ? 23.488 76.668  28.728 1   39.68  ? 61  HIS   A CD2 1 
ATOM   309   C  CE1 . HIS   A 1 39  ? 23.798 74.523  28.949 1   40.92  ? 61  HIS   A CE1 1 
ATOM   310   N  NE2 . HIS   A 1 39  ? 23.802 75.514  28.053 1   40.53  ? 61  HIS   A NE2 1 
ATOM   311   N  N   . GLN   A 1 40  ? 23.179 79.054  33.806 1   37.63  ? 62  GLN   A N   1 
ATOM   312   C  CA  . GLN   A 1 40  ? 22.949 80.315  34.493 1   38.17  ? 62  GLN   A CA  1 
ATOM   313   C  C   . GLN   A 1 40  ? 24.199 80.828  35.199 1   39.28  ? 62  GLN   A C   1 
ATOM   314   O  O   . GLN   A 1 40  ? 24.36  82.042  35.353 1   39.59  ? 62  GLN   A O   1 
ATOM   315   C  CB  . GLN   A 1 40  ? 21.814 80.167  35.494 1   39.13  ? 62  GLN   A CB  1 
ATOM   316   C  CG  . GLN   A 1 40  ? 20.46  80.016  34.841 1   40.59  ? 62  GLN   A CG  1 
ATOM   317   C  CD  . GLN   A 1 40  ? 19.377 79.813  35.877 1   44.41  ? 62  GLN   A CD  1 
ATOM   318   O  OE1 . GLN   A 1 40  ? 19.6   79.342  37.008 1   43.97  ? 62  GLN   A OE1 1 
ATOM   319   N  NE2 . GLN   A 1 40  ? 18.171 80.152  35.501 1   45.38  ? 62  GLN   A NE2 1 
ATOM   320   N  N   . ALA   A 1 41  ? 25.076 79.915  35.653 1   39.66  ? 63  ALA   A N   1 
ATOM   321   C  CA  . ALA   A 1 41  ? 26.338 80.308  36.272 1   40.48  ? 63  ALA   A CA  1 
ATOM   322   C  C   . ALA   A 1 41  ? 27.221 80.913  35.175 1   41.06  ? 63  ALA   A C   1 
ATOM   323   O  O   . ALA   A 1 41  ? 27.848 81.957  35.405 1   42.19  ? 63  ALA   A O   1 
ATOM   324   C  CB  . ALA   A 1 41  ? 27.021 79.113  36.887 1   40.82  ? 63  ALA   A CB  1 
ATOM   325   N  N   . TYR   A 1 42  ? 27.216 80.308  33.958 1   39.62  ? 64  TYR   A N   1 
ATOM   326   C  CA  . TYR   A 1 42  ? 27.935 80.821  32.803 1   39.14  ? 64  TYR   A CA  1 
ATOM   327   C  C   . TYR   A 1 42  ? 27.435 82.229  32.485 1   38.96  ? 64  TYR   A C   1 
ATOM   328   O  O   . TYR   A 1 42  ? 28.242 83.131  32.37  1   39.39  ? 64  TYR   A O   1 
ATOM   329   C  CB  . TYR   A 1 42  ? 27.73  79.909  31.571 1   38.78  ? 64  TYR   A CB  1 
ATOM   330   C  CG  . TYR   A 1 42  ? 28.778 78.831  31.419 1   38.98  ? 64  TYR   A CG  1 
ATOM   331   C  CD1 . TYR   A 1 42  ? 30.031 79.12   30.905 1   39.5   ? 64  TYR   A CD1 1 
ATOM   332   C  CD2 . TYR   A 1 42  ? 28.507 77.516  31.767 1   39.64  ? 64  TYR   A CD2 1 
ATOM   333   C  CE1 . TYR   A 1 42  ? 30.997 78.134  30.77  1   40.37  ? 64  TYR   A CE1 1 
ATOM   334   C  CE2 . TYR   A 1 42  ? 29.464 76.52   31.635 1   40.17  ? 64  TYR   A CE2 1 
ATOM   335   C  CZ  . TYR   A 1 42  ? 30.71  76.832  31.136 1   41.09  ? 64  TYR   A CZ  1 
ATOM   336   O  OH  . TYR   A 1 42  ? 31.673 75.859  31.028 1   42.05  ? 64  TYR   A OH  1 
ATOM   337   N  N   . GLU   A 1 43  ? 26.11  82.429  32.439 1   38.36  ? 65  GLU   A N   1 
ATOM   338   C  CA  . GLU   A 1 43  ? 25.507 83.715  32.097 1   38.25  ? 65  GLU   A CA  1 
ATOM   339   C  C   . GLU   A 1 43  ? 25.753 84.798  33.112 1   38.61  ? 65  GLU   A C   1 
ATOM   340   O  O   . GLU   A 1 43  ? 25.822 85.957  32.73  1   39.05  ? 65  GLU   A O   1 
ATOM   341   C  CB  . GLU   A 1 43  ? 24.014 83.565  31.803 1   39.29  ? 65  GLU   A CB  1 
ATOM   342   C  CG  . GLU   A 1 43  ? 23.741 82.803  30.519 1   41.06  ? 65  GLU   A CG  1 
ATOM   343   C  CD  . GLU   A 1 43  ? 24.104 83.514  29.228 1   46.09  ? 65  GLU   A CD  1 
ATOM   344   O  OE1 . GLU   A 1 43  ? 23.918 84.748  29.142 1   48.09  ? 65  GLU   A OE1 1 
ATOM   345   O  OE2 . GLU   A 1 43  ? 24.556 82.828  28.285 1   46.82  ? 65  GLU   A OE2 1 
ATOM   346   N  N   . LEU   A 1 44  ? 25.914 84.444  34.393 1   38.56  ? 66  LEU   A N   1 
ATOM   347   C  CA  . LEU   A 1 44  ? 26.238 85.431  35.414 1   38.8   ? 66  LEU   A CA  1 
ATOM   348   C  C   . LEU   A 1 44  ? 27.674 85.925  35.169 1   39     ? 66  LEU   A C   1 
ATOM   349   O  O   . LEU   A 1 44  ? 27.915 87.127  35.146 1   39.41  ? 66  LEU   A O   1 
ATOM   350   C  CB  . LEU   A 1 44  ? 26.13  84.825  36.831 1   39.4   ? 66  LEU   A CB  1 
ATOM   351   C  CG  . LEU   A 1 44  ? 24.747 84.685  37.456 1   40.67  ? 66  LEU   A CG  1 
ATOM   352   C  CD1 . LEU   A 1 44  ? 24.863 84.164  38.862 1   40.92  ? 66  LEU   A CD1 1 
ATOM   353   C  CD2 . LEU   A 1 44  ? 24.012 86      37.455 1   41.2   ? 66  LEU   A CD2 1 
ATOM   354   N  N   . TRP   A 1 45  ? 28.616 84.999  34.945 1   38.71  ? 67  TRP   A N   1 
ATOM   355   C  CA  . TRP   A 1 45  ? 30.011 85.341  34.681 1   38.61  ? 67  TRP   A CA  1 
ATOM   356   C  C   . TRP   A 1 45  ? 30.209 85.999  33.318 1   38.54  ? 67  TRP   A C   1 
ATOM   357   O  O   . TRP   A 1 45  ? 31.16  86.763  33.147 1   38.61  ? 67  TRP   A O   1 
ATOM   358   C  CB  . TRP   A 1 45  ? 30.933 84.125  34.883 1   38.57  ? 67  TRP   A CB  1 
ATOM   359   C  CG  . TRP   A 1 45  ? 31.034 83.679  36.321 1   38.95  ? 67  TRP   A CG  1 
ATOM   360   C  CD1 . TRP   A 1 45  ? 30.589 82.499  36.844 1   40.13  ? 67  TRP   A CD1 1 
ATOM   361   C  CD2 . TRP   A 1 45  ? 31.58  84.43   37.428 1   38.6   ? 67  TRP   A CD2 1 
ATOM   362   N  NE1 . TRP   A 1 45  ? 30.83  82.461  38.207 1   40.28  ? 67  TRP   A NE1 1 
ATOM   363   C  CE2 . TRP   A 1 45  ? 31.442 83.633  38.587 1   39.39  ? 67  TRP   A CE2 1 
ATOM   364   C  CE3 . TRP   A 1 45  ? 32.173 85.696  37.552 1   38.85  ? 67  TRP   A CE3 1 
ATOM   365   C  CZ2 . TRP   A 1 45  ? 31.879 84.06   39.843 1   39.28  ? 67  TRP   A CZ2 1 
ATOM   366   C  CZ3 . TRP   A 1 45  ? 32.616 86.109  38.798 1   39.25  ? 67  TRP   A CZ3 1 
ATOM   367   C  CH2 . TRP   A 1 45  ? 32.482 85.291  39.919 1   39.09  ? 67  TRP   A CH2 1 
ATOM   368   N  N   . PHE   A 1 46  ? 29.288 85.772  32.362 1   38.09  ? 68  PHE   A N   1 
ATOM   369   C  CA  . PHE   A 1 46  ? 29.337 86.454  31.074 1   37.9   ? 68  PHE   A CA  1 
ATOM   370   C  C   . PHE   A 1 46  ? 29.014 87.93   31.326 1   38.71  ? 68  PHE   A C   1 
ATOM   371   O  O   . PHE   A 1 46  ? 29.725 88.799  30.826 1   39.58  ? 68  PHE   A O   1 
ATOM   372   C  CB  . PHE   A 1 46  ? 28.337 85.846  30.078 1   37.38  ? 68  PHE   A CB  1 
ATOM   373   C  CG  . PHE   A 1 46  ? 28.707 84.517  29.45  1   37.54  ? 68  PHE   A CG  1 
ATOM   374   C  CD1 . PHE   A 1 46  ? 29.987 84.006  29.568 1   38.28  ? 68  PHE   A CD1 1 
ATOM   375   C  CD2 . PHE   A 1 46  ? 27.76  83.761  28.782 1   37.99  ? 68  PHE   A CD2 1 
ATOM   376   C  CE1 . PHE   A 1 46  ? 30.317 82.772  29.007 1   38.8   ? 68  PHE   A CE1 1 
ATOM   377   C  CE2 . PHE   A 1 46  ? 28.09  82.528  28.229 1   38.49  ? 68  PHE   A CE2 1 
ATOM   378   C  CZ  . PHE   A 1 46  ? 29.367 82.045  28.338 1   38.45  ? 68  PHE   A CZ  1 
ATOM   379   N  N   . LYS   A 1 47  ? 27.993 88.222  32.167 1   38.5   ? 69  LYS   A N   1 
ATOM   380   C  CA  . LYS   A 1 47  ? 27.626 89.592  32.525 1   38.71  ? 69  LYS   A CA  1 
ATOM   381   C  C   . LYS   A 1 47  ? 28.804 90.31   33.176 1   38.58  ? 69  LYS   A C   1 
ATOM   382   O  O   . LYS   A 1 47  ? 29.052 91.472  32.875 1   38.57  ? 69  LYS   A O   1 
ATOM   383   C  CB  . LYS   A 1 47  ? 26.389 89.611  33.44  1   40.8   ? 69  LYS   A CB  1 
ATOM   384   C  CG  . LYS   A 1 47  ? 25.866 91.013  33.719 1   43.71  ? 69  LYS   A CG  1 
ATOM   385   C  CD  . LYS   A 1 47  ? 24.415 91.031  34.178 1   47.16  ? 69  LYS   A CD  1 
ATOM   386   C  CE  . LYS   A 1 47  ? 24.064 92.41   34.7   1   50.73  ? 69  LYS   A CE  1 
ATOM   387   N  NZ  . LYS   A 1 47  ? 22.601 92.614  34.854 1   52.89  ? 69  LYS   A NZ  1 
ATOM   388   N  N   . GLN   A 1 48  ? 29.561 89.597  34.026 1   38.36  ? 70  GLN   A N   1 
ATOM   389   C  CA  . GLN   A 1 48  ? 30.751 90.128  34.684 1   37.91  ? 70  GLN   A CA  1 
ATOM   390   C  C   . GLN   A 1 48  ? 31.844 90.44   33.668 1   39.06  ? 70  GLN   A C   1 
ATOM   391   O  O   . GLN   A 1 48  ? 32.387 91.544  33.698 1   39.11  ? 70  GLN   A O   1 
ATOM   392   C  CB  . GLN   A 1 48  ? 31.284 89.165  35.762 1   37.16  ? 70  GLN   A CB  1 
ATOM   393   C  CG  . GLN   A 1 48  ? 32.381 89.792  36.63  1   36.33  ? 70  GLN   A CG  1 
ATOM   394   C  CD  . GLN   A 1 48  ? 31.856 90.974  37.41  1   35.65  ? 70  GLN   A CD  1 
ATOM   395   O  OE1 . GLN   A 1 48  ? 30.744 90.923  37.948 1   37.14  ? 70  GLN   A OE1 1 
ATOM   396   N  NE2 . GLN   A 1 48  ? 32.625 92.061  37.473 1   32.49  ? 70  GLN   A NE2 1 
ATOM   397   N  N   . ILE   A 1 49  ? 32.147 89.489  32.744 1   39.64  ? 71  ILE   A N   1 
ATOM   398   C  CA  . ILE   A 1 49  ? 33.164 89.689  31.701 1   40.31  ? 71  ILE   A CA  1 
ATOM   399   C  C   . ILE   A 1 49  ? 32.822 90.908  30.839 1   40.98  ? 71  ILE   A C   1 
ATOM   400   O  O   . ILE   A 1 49  ? 33.697 91.725  30.578 1   41.02  ? 71  ILE   A O   1 
ATOM   401   C  CB  . ILE   A 1 49  ? 33.383 88.402  30.853 1   40.78  ? 71  ILE   A CB  1 
ATOM   402   C  CG1 . ILE   A 1 49  ? 34     87.275  31.691 1   41.61  ? 71  ILE   A CG1 1 
ATOM   403   C  CG2 . ILE   A 1 49  ? 34.234 88.675  29.63  1   41.24  ? 71  ILE   A CG2 1 
ATOM   404   C  CD1 . ILE   A 1 49  ? 33.9   85.932  31.06  1   42.29  ? 71  ILE   A CD1 1 
ATOM   405   N  N   . ILE   A 1 50  ? 31.546 91.054  30.445 1   41.7   ? 72  ILE   A N   1 
ATOM   406   C  CA  . ILE   A 1 50  ? 31.069 92.181  29.631 1   42.68  ? 72  ILE   A CA  1 
ATOM   407   C  C   . ILE   A 1 50  ? 31.232 93.498  30.384 1   42.78  ? 72  ILE   A C   1 
ATOM   408   O  O   . ILE   A 1 50  ? 31.644 94.495  29.807 1   43.29  ? 72  ILE   A O   1 
ATOM   409   C  CB  . ILE   A 1 50  ? 29.597 91.949  29.203 1   43.92  ? 72  ILE   A CB  1 
ATOM   410   C  CG1 . ILE   A 1 50  ? 29.502 90.811  28.18  1   45.41  ? 72  ILE   A CG1 1 
ATOM   411   C  CG2 . ILE   A 1 50  ? 28.946 93.229  28.665 1   44.57  ? 72  ILE   A CG2 1 
ATOM   412   C  CD1 . ILE   A 1 50  ? 28.106 90.338  27.952 1   47.42  ? 72  ILE   A CD1 1 
ATOM   413   N  N   . PHE   A 1 51  ? 30.936 93.493  31.673 1   42.2   ? 73  PHE   A N   1 
ATOM   414   C  CA  . PHE   A 1 51  ? 31.053 94.669  32.52  1   41.76  ? 73  PHE   A CA  1 
ATOM   415   C  C   . PHE   A 1 51  ? 32.5   95.135  32.6   1   42.1   ? 73  PHE   A C   1 
ATOM   416   O  O   . PHE   A 1 51  ? 32.769 96.341  32.555 1   42.53  ? 73  PHE   A O   1 
ATOM   417   C  CB  . PHE   A 1 51  ? 30.5   94.355  33.917 1   41.06  ? 73  PHE   A CB  1 
ATOM   418   C  CG  . PHE   A 1 51  ? 30.347 95.577  34.783 1   41.45  ? 73  PHE   A CG  1 
ATOM   419   C  CD1 . PHE   A 1 51  ? 29.39  96.533  34.497 1   41.8   ? 73  PHE   A CD1 1 
ATOM   420   C  CD2 . PHE   A 1 51  ? 31.175 95.783  35.869 1   42.2   ? 73  PHE   A CD2 1 
ATOM   421   C  CE1 . PHE   A 1 51  ? 29.253 97.656  35.293 1   42.19  ? 73  PHE   A CE1 1 
ATOM   422   C  CE2 . PHE   A 1 51  ? 31.039 96.917  36.656 1   42.52  ? 73  PHE   A CE2 1 
ATOM   423   C  CZ  . PHE   A 1 51  ? 30.08  97.842  36.365 1   42.06  ? 73  PHE   A CZ  1 
ATOM   424   N  N   . GLU   A 1 52  ? 33.433 94.177  32.722 1   41.97  ? 74  GLU   A N   1 
ATOM   425   C  CA  . GLU   A 1 52  ? 34.86  94.468  32.811 1   42.43  ? 74  GLU   A CA  1 
ATOM   426   C  C   . GLU   A 1 52  ? 35.368 94.965  31.48  1   42.61  ? 74  GLU   A C   1 
ATOM   427   O  O   . GLU   A 1 52  ? 36.085 95.964  31.437 1   43.03  ? 74  GLU   A O   1 
ATOM   428   C  CB  . GLU   A 1 52  ? 35.665 93.23   33.277 1   44.68  ? 74  GLU   A CB  1 
ATOM   429   C  CG  . GLU   A 1 52  ? 35.308 92.739  34.673 1   49.09  ? 74  GLU   A CG  1 
ATOM   430   C  CD  . GLU   A 1 52  ? 35.49  93.721  35.818 1   54.46  ? 74  GLU   A CD  1 
ATOM   431   O  OE1 . GLU   A 1 52  ? 36.328 94.64   35.683 1   56.3   ? 74  GLU   A OE1 1 
ATOM   432   O  OE2 . GLU   A 1 52  ? 34.815 93.561  36.862 1   56.48  ? 74  GLU   A OE2 1 
ATOM   433   N  N   . PHE   A 1 53  ? 34.956 94.295  30.386 1   42.12  ? 75  PHE   A N   1 
ATOM   434   C  CA  . PHE   A 1 53  ? 35.338 94.656  29.037 1   42.16  ? 75  PHE   A CA  1 
ATOM   435   C  C   . PHE   A 1 53  ? 34.867 96.047  28.68  1   42.3   ? 75  PHE   A C   1 
ATOM   436   O  O   . PHE   A 1 53  ? 35.625 96.795  28.078 1   42.77  ? 75  PHE   A O   1 
ATOM   437   C  CB  . PHE   A 1 53  ? 34.792 93.634  28.029 1   41.95  ? 75  PHE   A CB  1 
ATOM   438   C  CG  . PHE   A 1 53  ? 35.665 92.431  27.742 1   42.29  ? 75  PHE   A CG  1 
ATOM   439   C  CD1 . PHE   A 1 53  ? 36.787 92.168  28.505 1   43.1   ? 75  PHE   A CD1 1 
ATOM   440   C  CD2 . PHE   A 1 53  ? 35.349 91.556  26.715 1   42.87  ? 75  PHE   A CD2 1 
ATOM   441   C  CE1 . PHE   A 1 53  ? 37.579 91.067  28.241 1   43.95  ? 75  PHE   A CE1 1 
ATOM   442   C  CE2 . PHE   A 1 53  ? 36.13  90.443  26.466 1   43.59  ? 75  PHE   A CE2 1 
ATOM   443   C  CZ  . PHE   A 1 53  ? 37.25  90.213  27.218 1   43.69  ? 75  PHE   A CZ  1 
ATOM   444   N  N   . ASP   A 1 54  ? 33.639 96.409  29.051 1   41.97  ? 76  ASP   A N   1 
ATOM   445   C  CA  . ASP   A 1 54  ? 33.112 97.731  28.736 1   42.3   ? 76  ASP   A CA  1 
ATOM   446   C  C   . ASP   A 1 54  ? 33.864 98.811  29.46  1   42.28  ? 76  ASP   A C   1 
ATOM   447   O  O   . ASP   A 1 54  ? 34.152 99.83   28.847 1   42.99  ? 76  ASP   A O   1 
ATOM   448   C  CB  . ASP   A 1 54  ? 31.606 97.827  28.974 1   44.5   ? 76  ASP   A CB  1 
ATOM   449   C  CG  . ASP   A 1 54  ? 30.794 97.147  27.884 1   50.06  ? 76  ASP   A CG  1 
ATOM   450   O  OD1 . ASP   A 1 54  ? 31.291 97.051  26.742 1   50.02  ? 76  ASP   A OD1 1 
ATOM   451   O  OD2 . ASP   A 1 54  ? 29.661 96.709  28.174 1   53.83  ? 76  ASP   A OD2 1 
ATOM   452   N  N   . SER   A 1 55  ? 34.274 98.568  30.71  1   41.25  ? 77  SER   A N   1 
ATOM   453   C  CA  . SER   A 1 55  ? 35.051 99.554  31.446 1   41.36  ? 77  SER   A CA  1 
ATOM   454   C  C   . SER   A 1 55  ? 36.477 99.703  30.864 1   42.06  ? 77  SER   A C   1 
ATOM   455   O  O   . SER   A 1 55  ? 36.983 100.825 30.741 1   41.33  ? 77  SER   A O   1 
ATOM   456   C  CB  . SER   A 1 55  ? 35.083 99.224  32.936 1   41.53  ? 77  SER   A CB  1 
ATOM   457   O  OG  . SER   A 1 55  ? 35.859 98.074  33.217 1   42.73  ? 77  SER   A OG  1 
ATOM   458   N  N   . ILE   A 1 56  ? 37.102 98.577  30.472 1   42.64  ? 78  ILE   A N   1 
ATOM   459   C  CA  . ILE   A 1 56  ? 38.426 98.592  29.839 1   43.55  ? 78  ILE   A CA  1 
ATOM   460   C  C   . ILE   A 1 56  ? 38.359 99.319  28.494 1   44.65  ? 78  ILE   A C   1 
ATOM   461   O  O   . ILE   A 1 56  ? 39.297 100.039 28.141 1   45.06  ? 78  ILE   A O   1 
ATOM   462   C  CB  . ILE   A 1 56  ? 38.992 97.154  29.684 1   43.77  ? 78  ILE   A CB  1 
ATOM   463   C  CG1 . ILE   A 1 56  ? 39.23  96.495  31.053 1   44.42  ? 78  ILE   A CG1 1 
ATOM   464   C  CG2 . ILE   A 1 56  ? 40.259 97.123  28.831 1   43.98  ? 78  ILE   A CG2 1 
ATOM   465   C  CD1 . ILE   A 1 56  ? 39.395 95.019  30.942 1   45.73  ? 78  ILE   A CD1 1 
ATOM   466   N  N   . ARG   A 1 57  ? 37.242 99.169  27.757 1   45.13  ? 79  ARG   A N   1 
ATOM   467   C  CA  . ARG   A 1 57  ? 37.06  99.838  26.475 1   46.22  ? 79  ARG   A CA  1 
ATOM   468   C  C   . ARG   A 1 57  ? 36.979 101.335 26.676 1   47.43  ? 79  ARG   A C   1 
ATOM   469   O  O   . ARG   A 1 57  ? 37.631 102.079 25.954 1   48.14  ? 79  ARG   A O   1 
ATOM   470   C  CB  . ARG   A 1 57  ? 35.806 99.335  25.753 1   47.89  ? 79  ARG   A CB  1 
ATOM   471   C  CG  . ARG   A 1 57  ? 35.926 97.944  25.111 1   50.49  ? 79  ARG   A CG  1 
ATOM   472   C  CD  . ARG   A 1 57  ? 34.792 97.554  24.168 1   52.96  ? 79  ARG   A CD  1 
ATOM   473   N  NE  . ARG   A 1 57  ? 33.498 98.108  24.569 1   57.18  ? 79  ARG   A NE  1 
ATOM   474   C  CZ  . ARG   A 1 57  ? 32.905 99.139  23.967 1   60.6   ? 79  ARG   A CZ  1 
ATOM   475   N  NH1 . ARG   A 1 57  ? 33.476 99.726  22.924 1   60.72  ? 79  ARG   A NH1 1 
ATOM   476   N  NH2 . ARG   A 1 57  ? 31.739 99.593  24.409 1   61.01  ? 79  ARG   A NH2 1 
ATOM   477   N  N   . ASP   A 1 58  ? 36.234 101.783 27.69  1   47.99  ? 80  ASP   A N   1 
ATOM   478   C  CA  . ASP   A 1 58  ? 36.096 103.2   28.019 1   49.13  ? 80  ASP   A CA  1 
ATOM   479   C  C   . ASP   A 1 58  ? 37.434 103.811 28.466 1   50.2   ? 80  ASP   A C   1 
ATOM   480   O  O   . ASP   A 1 58  ? 37.707 104.968 28.171 1   50.29  ? 80  ASP   A O   1 
ATOM   481   C  CB  . ASP   A 1 58  ? 35.013 103.393 29.093 1   51.3   ? 80  ASP   A CB  1 
ATOM   482   C  CG  . ASP   A 1 58  ? 33.614 102.961 28.662 1   57.04  ? 80  ASP   A CG  1 
ATOM   483   O  OD1 . ASP   A 1 58  ? 33.464 102.46  27.512 1   57.36  ? 80  ASP   A OD1 1 
ATOM   484   O  OD2 . ASP   A 1 58  ? 32.669 103.106 29.477 1   60.06  ? 80  ASP   A OD2 1 
ATOM   485   N  N   . MET   A 1 59  ? 38.271 103.025 29.156 1   50.97  ? 81  MET   A N   1 
ATOM   486   C  CA  . MET   A 1 59  ? 39.603 103.448 29.589 1   52.23  ? 81  MET   A CA  1 
ATOM   487   C  C   . MET   A 1 59  ? 40.571 103.523 28.402 1   53.61  ? 81  MET   A C   1 
ATOM   488   O  O   . MET   A 1 59  ? 41.446 104.389 28.37  1   53.44  ? 81  MET   A O   1 
ATOM   489   C  CB  . MET   A 1 59  ? 40.159 102.509 30.67  1   52.31  ? 81  MET   A CB  1 
ATOM   490   C  CG  . MET   A 1 59  ? 39.507 102.708 32.009 1   54.57  ? 81  MET   A CG  1 
ATOM   491   S  SD  . MET   A 1 59  ? 40.303 101.848 33.396 1   57.46  ? 81  MET   A SD  1 
ATOM   492   C  CE  . MET   A 1 59  ? 39.831 100.186 33.058 1   55.02  ? 81  MET   A CE  1 
ATOM   493   N  N   . LEU   A 1 60  ? 40.421 102.616 27.432 1   54.7   ? 82  LEU   A N   1 
ATOM   494   C  CA  . LEU   A 1 60  ? 41.265 102.628 26.235 1   56.3   ? 82  LEU   A CA  1 
ATOM   495   C  C   . LEU   A 1 60  ? 40.825 103.677 25.199 1   59.19  ? 82  LEU   A C   1 
ATOM   496   O  O   . LEU   A 1 60  ? 41.619 104.041 24.332 1   59.3   ? 82  LEU   A O   1 
ATOM   497   C  CB  . LEU   A 1 60  ? 41.319 101.241 25.588 1   55.32  ? 82  LEU   A CB  1 
ATOM   498   C  CG  . LEU   A 1 60  ? 42.124 100.21  26.324 1   55.27  ? 82  LEU   A CG  1 
ATOM   499   C  CD1 . LEU   A 1 60  ? 41.952 98.864  25.701 1   55.39  ? 82  LEU   A CD1 1 
ATOM   500   C  CD2 . LEU   A 1 60  ? 43.575 100.59  26.361 1   55.66  ? 82  LEU   A CD2 1 
ATOM   501   N  N   . ASP   A 1 61  ? 39.571 104.168 25.294 1   61.33  ? 83  ASP   A N   1 
ATOM   502   C  CA  . ASP   A 1 61  ? 39.03  105.178 24.39  1   63.87  ? 83  ASP   A CA  1 
ATOM   503   C  C   . ASP   A 1 61  ? 39.422 106.582 24.877 1   65.59  ? 83  ASP   A C   1 
ATOM   504   O  O   . ASP   A 1 61  ? 38.571 107.446 25.073 1   65.52  ? 83  ASP   A O   1 
ATOM   505   C  CB  . ASP   A 1 61  ? 37.501 105.043 24.274 1   66.64  ? 83  ASP   A CB  1 
ATOM   506   C  CG  . ASP   A 1 61  ? 36.94  105.562 22.956 1   72.89  ? 83  ASP   A CG  1 
ATOM   507   O  OD1 . ASP   A 1 61  ? 36.851 104.77  22     1   74.06  ? 83  ASP   A OD1 1 
ATOM   508   O  OD2 . ASP   A 1 61  ? 36.581 106.763 22.887 1   75.46  ? 83  ASP   A OD2 1 
ATOM   509   N  N   . ALA   A 1 62  ? 40.726 106.791 25.076 1   66.72  ? 84  ALA   A N   1 
ATOM   510   C  CA  . ALA   A 1 62  ? 41.32  108.055 25.499 1   68.06  ? 84  ALA   A CA  1 
ATOM   511   C  C   . ALA   A 1 62  ? 42.657 108.23  24.751 1   69.24  ? 84  ALA   A C   1 
ATOM   512   O  O   . ALA   A 1 62  ? 43.35  107.238 24.491 1   69.72  ? 84  ALA   A O   1 
ATOM   513   C  CB  . ALA   A 1 62  ? 41.559 108.038 27     1   68.3   ? 84  ALA   A CB  1 
ATOM   514   N  N   . GLU   A 1 63  ? 43.02  109.475 24.39  1   69.32  ? 85  GLU   A N   1 
ATOM   515   C  CA  . GLU   A 1 63  ? 44.276 109.71  23.668 1   69.77  ? 85  GLU   A CA  1 
ATOM   516   C  C   . GLU   A 1 63  ? 45.518 109.556 24.556 1   69.36  ? 85  GLU   A C   1 
ATOM   517   O  O   . GLU   A 1 63  ? 46.599 109.265 24.047 1   69.71  ? 85  GLU   A O   1 
ATOM   518   C  CB  . GLU   A 1 63  ? 44.257 111.061 22.94  1   73.04  ? 85  GLU   A CB  1 
ATOM   519   C  CG  . GLU   A 1 63  ? 43.652 110.965 21.548 1   79.42  ? 85  GLU   A CG  1 
ATOM   520   C  CD  . GLU   A 1 63  ? 44.645 111.09  20.409 1   88.03  ? 85  GLU   A CD  1 
ATOM   521   O  OE1 . GLU   A 1 63  ? 44.902 112.236 19.977 1   90.13  ? 85  GLU   A OE1 1 
ATOM   522   O  OE2 . GLU   A 1 63  ? 45.157 110.049 19.938 1   90.8   ? 85  GLU   A OE2 1 
ATOM   523   N  N   . VAL   A 1 64  ? 45.352 109.71  25.881 1   68.48  ? 86  VAL   A N   1 
ATOM   524   C  CA  . VAL   A 1 64  ? 46.404 109.553 26.885 1   67.94  ? 86  VAL   A CA  1 
ATOM   525   C  C   . VAL   A 1 64  ? 46.017 108.459 27.914 1   66.49  ? 86  VAL   A C   1 
ATOM   526   O  O   . VAL   A 1 64  ? 45.019 108.586 28.638 1   66.42  ? 86  VAL   A O   1 
ATOM   527   C  CB  . VAL   A 1 64  ? 46.752 110.904 27.574 1   69.28  ? 86  VAL   A CB  1 
ATOM   528   C  CG1 . VAL   A 1 64  ? 45.486 111.686 27.963 1   70.02  ? 86  VAL   A CG1 1 
ATOM   529   C  CG2 . VAL   A 1 64  ? 47.664 110.692 28.785 1   69.72  ? 86  VAL   A CG2 1 
ATOM   530   N  N   . ILE   A 1 65  ? 46.784 107.364 27.948 1   65.07  ? 87  ILE   A N   1 
ATOM   531   C  CA  . ILE   A 1 65  ? 46.529 106.281 28.901 1   63.82  ? 87  ILE   A CA  1 
ATOM   532   C  C   . ILE   A 1 65  ? 47.709 106.229 29.864 1   62.22  ? 87  ILE   A C   1 
ATOM   533   O  O   . ILE   A 1 65  ? 48.778 105.709 29.513 1   62.63  ? 87  ILE   A O   1 
ATOM   534   C  CB  . ILE   A 1 65  ? 46.257 104.938 28.187 1   63.96  ? 87  ILE   A CB  1 
ATOM   535   C  CG1 . ILE   A 1 65  ? 45.073 105.091 27.218 1   65.03  ? 87  ILE   A CG1 1 
ATOM   536   C  CG2 . ILE   A 1 65  ? 45.982 103.839 29.209 1   64.09  ? 87  ILE   A CG2 1 
ATOM   537   C  CD1 . ILE   A 1 65  ? 45.188 104.337 25.937 1   66.4   ? 87  ILE   A CD1 1 
ATOM   538   N  N   . ASP   A 1 66  ? 47.54  106.847 31.047 1   59.93  ? 88  ASP   A N   1 
ATOM   539   C  CA  . ASP   A 1 66  ? 48.626 106.947 32.01  1   58.4   ? 88  ASP   A CA  1 
ATOM   540   C  C   . ASP   A 1 66  ? 48.897 105.629 32.753 1   56.42  ? 88  ASP   A C   1 
ATOM   541   O  O   . ASP   A 1 66  ? 48.169 104.657 32.586 1   56.16  ? 88  ASP   A O   1 
ATOM   542   C  CB  . ASP   A 1 66  ? 48.416 108.139 32.972 1   59.84  ? 88  ASP   A CB  1 
ATOM   543   C  CG  . ASP   A 1 66  ? 47.252 107.998 33.918 1   64.3   ? 88  ASP   A CG  1 
ATOM   544   O  OD1 . ASP   A 1 66  ? 46.261 107.362 33.536 1   66     ? 88  ASP   A OD1 1 
ATOM   545   O  OD2 . ASP   A 1 66  ? 47.332 108.537 35.044 1   65.7   ? 88  ASP   A OD2 1 
ATOM   546   N  N   . GLU   A 1 67  ? 49.992 105.589 33.521 1   55.06  ? 89  GLU   A N   1 
ATOM   547   C  CA  . GLU   A 1 67  ? 50.424 104.423 34.268 1   54.42  ? 89  GLU   A CA  1 
ATOM   548   C  C   . GLU   A 1 67  ? 49.338 103.928 35.216 1   53.69  ? 89  GLU   A C   1 
ATOM   549   O  O   . GLU   A 1 67  ? 49.205 102.722 35.409 1   54.13  ? 89  GLU   A O   1 
ATOM   550   C  CB  . GLU   A 1 67  ? 51.68  104.766 35.076 1   56.67  ? 89  GLU   A CB  1 
ATOM   551   C  CG  . GLU   A 1 67  ? 52.91  105.151 34.273 1   61.95  ? 89  GLU   A CG  1 
ATOM   552   C  CD  . GLU   A 1 67  ? 54.16  105.17  35.136 1   69.31  ? 89  GLU   A CD  1 
ATOM   553   O  OE1 . GLU   A 1 67  ? 54.838 104.119 35.226 1   69.67  ? 89  GLU   A OE1 1 
ATOM   554   O  OE2 . GLU   A 1 67  ? 54.44  106.225 35.755 1   72.12  ? 89  GLU   A OE2 1 
ATOM   555   N  N   . THR   A 1 68  ? 48.576 104.852 35.822 1   52.52  ? 90  THR   A N   1 
ATOM   556   C  CA  . THR   A 1 68  ? 47.508 104.518 36.761 1   51.63  ? 90  THR   A CA  1 
ATOM   557   C  C   . THR   A 1 68  ? 46.346 103.806 36.069 1   51.5   ? 90  THR   A C   1 
ATOM   558   O  O   . THR   A 1 68  ? 45.894 102.773 36.558 1   51.38  ? 90  THR   A O   1 
ATOM   559   C  CB  . THR   A 1 68  ? 47.081 105.757 37.546 1   51.81  ? 90  THR   A CB  1 
ATOM   560   O  OG1 . THR   A 1 68  ? 48.242 106.333 38.155 1   52.31  ? 90  THR   A OG1 1 
ATOM   561   C  CG2 . THR   A 1 68  ? 46.023 105.444 38.593 1   51.83  ? 90  THR   A CG2 1 
ATOM   562   N  N   . LYS   A 1 69  ? 45.885 104.324 34.914 1   51.43  ? 91  LYS   A N   1 
ATOM   563   C  CA  . LYS   A 1 69  ? 44.812 103.661 34.17  1   51.53  ? 91  LYS   A CA  1 
ATOM   564   C  C   . LYS   A 1 69  ? 45.288 102.316 33.638 1   50.67  ? 91  LYS   A C   1 
ATOM   565   O  O   . LYS   A 1 69  ? 44.523 101.354 33.681 1   50.93  ? 91  LYS   A O   1 
ATOM   566   C  CB  . LYS   A 1 69  ? 44.271 104.538 33.037 1   54.07  ? 91  LYS   A CB  1 
ATOM   567   C  CG  . LYS   A 1 69  ? 43.532 105.775 33.529 1   60.48  ? 91  LYS   A CG  1 
ATOM   568   C  CD  . LYS   A 1 69  ? 42.174 105.478 34.178 1   66.43  ? 91  LYS   A CD  1 
ATOM   569   C  CE  . LYS   A 1 69  ? 41.688 106.646 35.015 1   70.89  ? 91  LYS   A CE  1 
ATOM   570   N  NZ  . LYS   A 1 69  ? 41.851 107.952 34.31  1   73.29  ? 91  LYS   A NZ  1 
ATOM   571   N  N   . THR   A 1 70  ? 46.561 102.233 33.197 1   49.58  ? 92  THR   A N   1 
ATOM   572   C  CA  . THR   A 1 70  ? 47.162 100.998 32.691 1   49.32  ? 92  THR   A CA  1 
ATOM   573   C  C   . THR   A 1 70  ? 47.122 99.872  33.737 1   48.34  ? 92  THR   A C   1 
ATOM   574   O  O   . THR   A 1 70  ? 46.733 98.76   33.405 1   48.31  ? 92  THR   A O   1 
ATOM   575   C  CB  . THR   A 1 70  ? 48.577 101.254 32.143 1   50.42  ? 92  THR   A CB  1 
ATOM   576   O  OG1 . THR   A 1 70  ? 48.498 102.159 31.035 1   50.95  ? 92  THR   A OG1 1 
ATOM   577   C  CG2 . THR   A 1 70  ? 49.27  99.962  31.709 1   50.81  ? 92  THR   A CG2 1 
ATOM   578   N  N   . LEU   A 1 71  ? 47.453 100.18  34.994 1   47.42  ? 93  LEU   A N   1 
ATOM   579   C  CA  . LEU   A 1 71  ? 47.425 99.236  36.116 1   47.15  ? 93  LEU   A CA  1 
ATOM   580   C  C   . LEU   A 1 71  ? 46.004 98.708  36.382 1   46.69  ? 93  LEU   A C   1 
ATOM   581   O  O   . LEU   A 1 71  ? 45.839 97.529  36.717 1   46.56  ? 93  LEU   A O   1 
ATOM   582   C  CB  . LEU   A 1 71  ? 47.938 99.921  37.381 1   47.34  ? 93  LEU   A CB  1 
ATOM   583   C  CG  . LEU   A 1 71  ? 49.435 100.115 37.497 1   48.7   ? 93  LEU   A CG  1 
ATOM   584   C  CD1 . LEU   A 1 71  ? 49.765 100.988 38.679 1   48.93  ? 93  LEU   A CD1 1 
ATOM   585   C  CD2 . LEU   A 1 71  ? 50.13  98.793  37.654 1   49.64  ? 93  LEU   A CD2 1 
ATOM   586   N  N   . GLU   A 1 72  ? 44.985 99.578  36.243 1   45.91  ? 94  GLU   A N   1 
ATOM   587   C  CA  . GLU   A 1 72  ? 43.584 99.182  36.433 1   45.45  ? 94  GLU   A CA  1 
ATOM   588   C  C   . GLU   A 1 72  ? 43.098 98.309  35.27  1   44.13  ? 94  GLU   A C   1 
ATOM   589   O  O   . GLU   A 1 72  ? 42.288 97.4    35.477 1   43.66  ? 94  GLU   A O   1 
ATOM   590   C  CB  . GLU   A 1 72  ? 42.681 100.411 36.631 1   48.15  ? 94  GLU   A CB  1 
ATOM   591   C  CG  . GLU   A 1 72  ? 41.302 100.075 37.182 1   53.51  ? 94  GLU   A CG  1 
ATOM   592   C  CD  . GLU   A 1 72  ? 41.248 99.658  38.639 1   60.91  ? 94  GLU   A CD  1 
ATOM   593   O  OE1 . GLU   A 1 72  ? 42.254 99.858  39.357 1   61.44  ? 94  GLU   A OE1 1 
ATOM   594   O  OE2 . GLU   A 1 72  ? 40.186 99.154  39.07  1   64.54  ? 94  GLU   A OE2 1 
ATOM   595   N  N   . ILE   A 1 73  ? 43.609 98.562  34.051 1   43.3   ? 95  ILE   A N   1 
ATOM   596   C  CA  . ILE   A 1 73  ? 43.283 97.734  32.892 1   42.91  ? 95  ILE   A CA  1 
ATOM   597   C  C   . ILE   A 1 73  ? 43.901 96.335  33.102 1   42.72  ? 95  ILE   A C   1 
ATOM   598   O  O   . ILE   A 1 73  ? 43.229 95.329  32.901 1   42.79  ? 95  ILE   A O   1 
ATOM   599   C  CB  . ILE   A 1 73  ? 43.749 98.399  31.581 1   43.14  ? 95  ILE   A CB  1 
ATOM   600   C  CG1 . ILE   A 1 73  ? 42.945 99.678  31.301 1   43.67  ? 95  ILE   A CG1 1 
ATOM   601   C  CG2 . ILE   A 1 73  ? 43.646 97.429  30.401 1   43.76  ? 95  ILE   A CG2 1 
ATOM   602   C  CD1 . ILE   A 1 73  ? 43.518 100.526 30.241 1   44.75  ? 95  ILE   A CD1 1 
ATOM   603   N  N   . VAL   A 1 74  ? 45.147 96.275  33.584 1   42.39  ? 96  VAL   A N   1 
ATOM   604   C  CA  . VAL   A 1 74  ? 45.814 95.007  33.891 1   42.63  ? 96  VAL   A CA  1 
ATOM   605   C  C   . VAL   A 1 74  ? 45.044 94.212  34.984 1   42.51  ? 96  VAL   A C   1 
ATOM   606   O  O   . VAL   A 1 74  ? 44.85  93.008  34.831 1   43.37  ? 96  VAL   A O   1 
ATOM   607   C  CB  . VAL   A 1 74  ? 47.306 95.237  34.236 1   43.15  ? 96  VAL   A CB  1 
ATOM   608   C  CG1 . VAL   A 1 74  ? 47.965 93.971  34.742 1   43.9   ? 96  VAL   A CG1 1 
ATOM   609   C  CG2 . VAL   A 1 74  ? 48.049 95.756  33.027 1   43.87  ? 96  VAL   A CG2 1 
ATOM   610   N  N   . LYS   A 1 75  ? 44.541 94.896  36.027 1   40.93  ? 97  LYS   A N   1 
ATOM   611   C  CA  . LYS   A 1 75  ? 43.783 94.263  37.102 1   39.83  ? 97  LYS   A CA  1 
ATOM   612   C  C   . LYS   A 1 75  ? 42.521 93.61   36.571 1   39.19  ? 97  LYS   A C   1 
ATOM   613   O  O   . LYS   A 1 75  ? 42.207 92.476  36.933 1   39.44  ? 97  LYS   A O   1 
ATOM   614   C  CB  . LYS   A 1 75  ? 43.431 95.294  38.202 1   40.84  ? 97  LYS   A CB  1 
ATOM   615   C  CG  . LYS   A 1 75  ? 42.519 94.739  39.304 1   44.09  ? 97  LYS   A CG  1 
ATOM   616   C  CD  . LYS   A 1 75  ? 42.621 95.495  40.598 1   48.96  ? 97  LYS   A CD  1 
ATOM   617   C  CE  . LYS   A 1 75  ? 41.75  96.722  40.62  1   53.49  ? 97  LYS   A CE  1 
ATOM   618   N  NZ  . LYS   A 1 75  ? 42.203 97.702  41.656 1   56.16  ? 97  LYS   A NZ  1 
ATOM   619   N  N   . ARG   A 1 76  ? 41.803 94.325  35.711 1   38.5   ? 98  ARG   A N   1 
ATOM   620   C  CA  . ARG   A 1 76  ? 40.547 93.849  35.149 1   38.37  ? 98  ARG   A CA  1 
ATOM   621   C  C   . ARG   A 1 76  ? 40.757 92.784  34.069 1   36.97  ? 98  ARG   A C   1 
ATOM   622   O  O   . ARG   A 1 76  ? 39.952 91.863  33.982 1   37.23  ? 98  ARG   A O   1 
ATOM   623   C  CB  . ARG   A 1 76  ? 39.679 95.033  34.671 1   40.03  ? 98  ARG   A CB  1 
ATOM   624   C  CG  . ARG   A 1 76  ? 39.39  95.982  35.827 1   43.37  ? 98  ARG   A CG  1 
ATOM   625   C  CD  . ARG   A 1 76  ? 38.638 97.224  35.432 1   47.54  ? 98  ARG   A CD  1 
ATOM   626   N  NE  . ARG   A 1 76  ? 38.412 98.081  36.6   1   50.26  ? 98  ARG   A NE  1 
ATOM   627   C  CZ  . ARG   A 1 76  ? 37.791 99.257  36.566 1   50.98  ? 98  ARG   A CZ  1 
ATOM   628   N  NH1 . ARG   A 1 76  ? 37.322 99.737  35.421 1   49.16  ? 98  ARG   A NH1 1 
ATOM   629   N  NH2 . ARG   A 1 76  ? 37.626 99.958  37.678 1   51.47  ? 98  ARG   A NH2 1 
ATOM   630   N  N   . LEU   A 1 77  ? 41.862 92.849  33.312 1   35.26  ? 99  LEU   A N   1 
ATOM   631   C  CA  . LEU   A 1 77  ? 42.155 91.808  32.321 1   34.34  ? 99  LEU   A CA  1 
ATOM   632   C  C   . LEU   A 1 77  ? 42.505 90.519  33.045 1   34.6   ? 99  LEU   A C   1 
ATOM   633   O  O   . LEU   A 1 77  ? 42.044 89.46   32.654 1   35.62  ? 99  LEU   A O   1 
ATOM   634   C  CB  . LEU   A 1 77  ? 43.306 92.215  31.398 1   33.7   ? 99  LEU   A CB  1 
ATOM   635   C  CG  . LEU   A 1 77  ? 42.993 93.239  30.319 1   33.24  ? 99  LEU   A CG  1 
ATOM   636   C  CD1 . LEU   A 1 77  ? 44.265 93.677  29.63  1   32.97  ? 99  LEU   A CD1 1 
ATOM   637   C  CD2 . LEU   A 1 77  ? 41.97  92.697  29.332 1   32.84  ? 99  LEU   A CD2 1 
ATOM   638   N  N   . ASN   A 1 78  ? 43.279 90.612  34.128 1   33.9   ? 100 ASN   A N   1 
ATOM   639   C  CA  . ASN   A 1 78  ? 43.652 89.48   34.948 1   33.96  ? 100 ASN   A CA  1 
ATOM   640   C  C   . ASN   A 1 78  ? 42.455 88.863  35.661 1   34.61  ? 100 ASN   A C   1 
ATOM   641   O  O   . ASN   A 1 78  ? 42.407 87.644  35.83  1   35.12  ? 100 ASN   A O   1 
ATOM   642   C  CB  . ASN   A 1 78  ? 44.711 89.897  35.926 1   34.76  ? 100 ASN   A CB  1 
ATOM   643   C  CG  . ASN   A 1 78  ? 45.262 88.743  36.692 1   38.36  ? 100 ASN   A CG  1 
ATOM   644   O  OD1 . ASN   A 1 78  ? 44.741 88.398  37.764 1   40.7   ? 100 ASN   A OD1 1 
ATOM   645   N  ND2 . ASN   A 1 78  ? 46.311 88.127  36.162 1   37.81  ? 100 ASN   A ND2 1 
ATOM   646   N  N   . ARG   A 1 79  ? 41.48  89.69   36.053 1   34.53  ? 101 ARG   A N   1 
ATOM   647   C  CA  . ARG   A 1 79  ? 40.242 89.231  36.675 1   34.56  ? 101 ARG   A CA  1 
ATOM   648   C  C   . ARG   A 1 79  ? 39.455 88.397  35.67  1   35.35  ? 101 ARG   A C   1 
ATOM   649   O  O   . ARG   A 1 79  ? 38.986 87.32   36.025 1   37.04  ? 101 ARG   A O   1 
ATOM   650   C  CB  . ARG   A 1 79  ? 39.415 90.439  37.112 1   35.07  ? 101 ARG   A CB  1 
ATOM   651   C  CG  . ARG   A 1 79  ? 38.084 90.097  37.76  1   34.83  ? 101 ARG   A CG  1 
ATOM   652   C  CD  . ARG   A 1 79  ? 37.365 91.364  38.133 1   35.3   ? 101 ARG   A CD  1 
ATOM   653   N  NE  . ARG   A 1 79  ? 38.102 92.074  39.173 1   36.94  ? 101 ARG   A NE  1 
ATOM   654   C  CZ  . ARG   A 1 79  ? 37.862 93.322  39.559 1   37.27  ? 101 ARG   A CZ  1 
ATOM   655   N  NH1 . ARG   A 1 79  ? 36.905 94.031  38.983 1   35.9   ? 101 ARG   A NH1 1 
ATOM   656   N  NH2 . ARG   A 1 79  ? 38.586 93.873  40.509 1   37.94  ? 101 ARG   A NH2 1 
ATOM   657   N  N   . VAL   A 1 80  ? 39.363 88.847  34.402 1   34.49  ? 102 VAL   A N   1 
ATOM   658   C  CA  . VAL   A 1 80  ? 38.686 88.124  33.329 1   34.39  ? 102 VAL   A CA  1 
ATOM   659   C  C   . VAL   A 1 80  ? 39.367 86.771  33.089 1   35.14  ? 102 VAL   A C   1 
ATOM   660   O  O   . VAL   A 1 80  ? 38.681 85.776  32.876 1   35.39  ? 102 VAL   A O   1 
ATOM   661   C  CB  . VAL   A 1 80  ? 38.589 88.988  32.039 1   34.44  ? 102 VAL   A CB  1 
ATOM   662   C  CG1 . VAL   A 1 80  ? 38.221 88.147  30.82  1   35.01  ? 102 VAL   A CG1 1 
ATOM   663   C  CG2 . VAL   A 1 80  ? 37.597 90.132  32.209 1   34.06  ? 102 VAL   A CG2 1 
ATOM   664   N  N   . VAL   A 1 81  ? 40.71  86.722  33.182 1   35.33  ? 103 VAL   A N   1 
ATOM   665   C  CA  . VAL   A 1 81  ? 41.507 85.502  33.026 1   36.06  ? 103 VAL   A CA  1 
ATOM   666   C  C   . VAL   A 1 81  ? 41.091 84.471  34.082 1   36.5   ? 103 VAL   A C   1 
ATOM   667   O  O   . VAL   A 1 81  ? 40.946 83.28   33.771 1   36.62  ? 103 VAL   A O   1 
ATOM   668   C  CB  . VAL   A 1 81  ? 43.03  85.832  33.089 1   36.91  ? 103 VAL   A CB  1 
ATOM   669   C  CG1 . VAL   A 1 81  ? 43.871 84.592  33.382 1   37.16  ? 103 VAL   A CG1 1 
ATOM   670   C  CG2 . VAL   A 1 81  ? 43.494 86.501  31.801 1   37.29  ? 103 VAL   A CG2 1 
ATOM   671   N  N   . LEU   A 1 82  ? 40.89  84.936  35.329 1   36.18  ? 104 LEU   A N   1 
ATOM   672   C  CA  . LEU   A 1 82  ? 40.463 84.089  36.435 1   36.27  ? 104 LEU   A CA  1 
ATOM   673   C  C   . LEU   A 1 82  ? 39.031 83.583  36.244 1   36.89  ? 104 LEU   A C   1 
ATOM   674   O  O   . LEU   A 1 82  ? 38.724 82.429  36.57  1   37.82  ? 104 LEU   A O   1 
ATOM   675   C  CB  . LEU   A 1 82  ? 40.584 84.865  37.75  1   36.14  ? 104 LEU   A CB  1 
ATOM   676   C  CG  . LEU   A 1 82  ? 42.002 85.238  38.21  1   37.01  ? 104 LEU   A CG  1 
ATOM   677   C  CD1 . LEU   A 1 82  ? 41.967 85.852  39.584 1   37.37  ? 104 LEU   A CD1 1 
ATOM   678   C  CD2 . LEU   A 1 82  ? 42.904 84.034  38.278 1   37.53  ? 104 LEU   A CD2 1 
ATOM   679   N  N   . ILE   A 1 83  ? 38.158 84.443  35.719 1   36.24  ? 105 ILE   A N   1 
ATOM   680   C  CA  . ILE   A 1 83  ? 36.769 84.076  35.461 1   36.56  ? 105 ILE   A CA  1 
ATOM   681   C  C   . ILE   A 1 83  ? 36.691 83.047  34.323 1   37.35  ? 105 ILE   A C   1 
ATOM   682   O  O   . ILE   A 1 83  ? 35.897 82.1    34.392 1   37.69  ? 105 ILE   A O   1 
ATOM   683   C  CB  . ILE   A 1 83  ? 35.958 85.352  35.139 1   36.47  ? 105 ILE   A CB  1 
ATOM   684   C  CG1 . ILE   A 1 83  ? 35.896 86.275  36.359 1   36.9   ? 105 ILE   A CG1 1 
ATOM   685   C  CG2 . ILE   A 1 83  ? 34.567 85.022  34.607 1   36.68  ? 105 ILE   A CG2 1 
ATOM   686   C  CD1 . ILE   A 1 83  ? 35.358 87.661  36.037 1   37.67  ? 105 ILE   A CD1 1 
ATOM   687   N  N   . LEU   A 1 84  ? 37.527 83.225  33.279 1   37.06  ? 106 LEU   A N   1 
ATOM   688   C  CA  . LEU   A 1 84  ? 37.568 82.302  32.146 1   37.2   ? 106 LEU   A CA  1 
ATOM   689   C  C   . LEU   A 1 84  ? 38.055 80.937  32.59  1   37.03  ? 106 LEU   A C   1 
ATOM   690   O  O   . LEU   A 1 84  ? 37.448 79.948  32.203 1   37.25  ? 106 LEU   A O   1 
ATOM   691   C  CB  . LEU   A 1 84  ? 38.426 82.846  30.991 1   37.47  ? 106 LEU   A CB  1 
ATOM   692   C  CG  . LEU   A 1 84  ? 37.73  83.871  30.089 1   38.48  ? 106 LEU   A CG  1 
ATOM   693   C  CD1 . LEU   A 1 84  ? 38.731 84.575  29.184 1   38.17  ? 106 LEU   A CD1 1 
ATOM   694   C  CD2 . LEU   A 1 84  ? 36.631 83.216  29.275 1   38.93  ? 106 LEU   A CD2 1 
ATOM   695   N  N   . LYS   A 1 85  ? 39.072 80.871  33.47  1   36.76  ? 107 LYS   A N   1 
ATOM   696   C  CA  . LYS   A 1 85  ? 39.554 79.587  33.999 1   37.39  ? 107 LYS   A CA  1 
ATOM   697   C  C   . LYS   A 1 85  ? 38.448 78.849  34.757 1   37.97  ? 107 LYS   A C   1 
ATOM   698   O  O   . LYS   A 1 85  ? 38.352 77.622  34.701 1   37.96  ? 107 LYS   A O   1 
ATOM   699   C  CB  . LYS   A 1 85  ? 40.752 79.786  34.936 1   38.92  ? 107 LYS   A CB  1 
ATOM   700   C  CG  . LYS   A 1 85  ? 42.053 80.091  34.22  1   43.84  ? 107 LYS   A CG  1 
ATOM   701   C  CD  . LYS   A 1 85  ? 43.192 80.234  35.215 1   49.54  ? 107 LYS   A CD  1 
ATOM   702   C  CE  . LYS   A 1 85  ? 44.399 80.953  34.655 1   53.65  ? 107 LYS   A CE  1 
ATOM   703   N  NZ  . LYS   A 1 85  ? 45.206 81.591  35.738 1   56.59  ? 107 LYS   A NZ  1 
ATOM   704   N  N   . LEU   A 1 86  ? 37.633 79.605  35.492 1   38.06  ? 108 LEU   A N   1 
ATOM   705   C  CA  . LEU   A 1 86  ? 36.525 79.065  36.263 1   38.22  ? 108 LEU   A CA  1 
ATOM   706   C  C   . LEU   A 1 86  ? 35.484 78.482  35.32  1   39.1   ? 108 LEU   A C   1 
ATOM   707   O  O   . LEU   A 1 86  ? 34.977 77.389  35.569 1   39.9   ? 108 LEU   A O   1 
ATOM   708   C  CB  . LEU   A 1 86  ? 35.913 80.174  37.136 1   37.93  ? 108 LEU   A CB  1 
ATOM   709   C  CG  . LEU   A 1 86  ? 34.859 79.74   38.154 1   38.43  ? 108 LEU   A CG  1 
ATOM   710   C  CD1 . LEU   A 1 86  ? 35.508 79.119  39.386 1   39.08  ? 108 LEU   A CD1 1 
ATOM   711   C  CD2 . LEU   A 1 86  ? 34.007 80.898  38.552 1   38.12  ? 108 LEU   A CD2 1 
ATOM   712   N  N   . LEU   A 1 87  ? 35.187 79.18   34.218 1   38.98  ? 109 LEU   A N   1 
ATOM   713   C  CA  . LEU   A 1 87  ? 34.221 78.698  33.237 1   39.26  ? 109 LEU   A CA  1 
ATOM   714   C  C   . LEU   A 1 87  ? 34.711 77.444  32.485 1   40.04  ? 109 LEU   A C   1 
ATOM   715   O  O   . LEU   A 1 87  ? 33.91  76.56   32.19  1   40.48  ? 109 LEU   A O   1 
ATOM   716   C  CB  . LEU   A 1 87  ? 33.811 79.824  32.286 1   39.1   ? 109 LEU   A CB  1 
ATOM   717   C  CG  . LEU   A 1 87  ? 33.147 81.045  32.956 1   40.09  ? 109 LEU   A CG  1 
ATOM   718   C  CD1 . LEU   A 1 87  ? 32.797 82.104  31.928 1   40.14  ? 109 LEU   A CD1 1 
ATOM   719   C  CD2 . LEU   A 1 87  ? 31.903 80.649  33.755 1   40.56  ? 109 LEU   A CD2 1 
ATOM   720   N  N   . VAL   A 1 88  ? 36.023 77.32   32.245 1   40.04  ? 110 VAL   A N   1 
ATOM   721   C  CA  . VAL   A 1 88  ? 36.57  76.106  31.615 1   40.38  ? 110 VAL   A CA  1 
ATOM   722   C  C   . VAL   A 1 88  ? 36.356 74.895  32.561 1   41.16  ? 110 VAL   A C   1 
ATOM   723   O  O   . VAL   A 1 88  ? 36.042 73.79   32.109 1   41.48  ? 110 VAL   A O   1 
ATOM   724   C  CB  . VAL   A 1 88  ? 38.057 76.299  31.217 1   40.03  ? 110 VAL   A CB  1 
ATOM   725   C  CG1 . VAL   A 1 88  ? 38.66  75.01   30.705 1   40.05  ? 110 VAL   A CG1 1 
ATOM   726   C  CG2 . VAL   A 1 88  ? 38.197 77.39   30.169 1   40.28  ? 110 VAL   A CG2 1 
ATOM   727   N  N   . ASP   A 1 89  ? 36.467 75.129  33.882 1   41.27  ? 111 ASP   A N   1 
ATOM   728   C  CA  . ASP   A 1 89  ? 36.262 74.116  34.918 1   41.47  ? 111 ASP   A CA  1 
ATOM   729   C  C   . ASP   A 1 89  ? 34.799 73.762  35.171 1   41.26  ? 111 ASP   A C   1 
ATOM   730   O  O   . ASP   A 1 89  ? 34.543 72.842  35.929 1   41.99  ? 111 ASP   A O   1 
ATOM   731   C  CB  . ASP   A 1 89  ? 36.92  74.557  36.235 1   42.98  ? 111 ASP   A CB  1 
ATOM   732   C  CG  . ASP   A 1 89  ? 38.437 74.578  36.212 1   47.88  ? 111 ASP   A CG  1 
ATOM   733   O  OD1 . ASP   A 1 89  ? 39.023 74.275  35.147 1   48.4   ? 111 ASP   A OD1 1 
ATOM   734   O  OD2 . ASP   A 1 89  ? 39.04  74.891  37.262 1   50.65  ? 111 ASP   A OD2 1 
ATOM   735   N  N   . GLN   A 1 90  ? 33.852 74.502  34.604 1   40.42  ? 112 GLN   A N   1 
ATOM   736   C  CA  . GLN   A 1 90  ? 32.437 74.203  34.765 1   40.41  ? 112 GLN   A CA  1 
ATOM   737   C  C   . GLN   A 1 90  ? 31.979 73.105  33.807 1   41.49  ? 112 GLN   A C   1 
ATOM   738   O  O   . GLN   A 1 90  ? 30.961 72.473  34.072 1   42.56  ? 112 GLN   A O   1 
ATOM   739   C  CB  . GLN   A 1 90  ? 31.574 75.46   34.613 1   41.18  ? 112 GLN   A CB  1 
ATOM   740   C  CG  . GLN   A 1 90  ? 31.79  76.486  35.721 1   43.45  ? 112 GLN   A CG  1 
ATOM   741   C  CD  . GLN   A 1 90  ? 30.741 77.582  35.777 1   45.83  ? 112 GLN   A CD  1 
ATOM   742   O  OE1 . GLN   A 1 90  ? 29.759 77.57   35.037 1   46.77  ? 112 GLN   A OE1 1 
ATOM   743   N  NE2 . GLN   A 1 90  ? 30.918 78.552  36.677 1   46.59  ? 112 GLN   A NE2 1 
ATOM   744   N  N   . VAL   A 1 91  ? 32.696 72.886  32.684 1   41.04  ? 113 VAL   A N   1 
ATOM   745   C  CA  . VAL   A 1 91  ? 32.388 71.824  31.723 1   40.45  ? 113 VAL   A CA  1 
ATOM   746   C  C   . VAL   A 1 91  ? 32.427 70.431  32.391 1   39.35  ? 113 VAL   A C   1 
ATOM   747   O  O   . VAL   A 1 91  ? 31.427 69.726  32.325 1   38.92  ? 113 VAL   A O   1 
ATOM   748   C  CB  . VAL   A 1 91  ? 33.281 71.894  30.459 1   41.24  ? 113 VAL   A CB  1 
ATOM   749   C  CG1 . VAL   A 1 91  ? 32.904 70.806  29.469 1   41.58  ? 113 VAL   A CG1 1 
ATOM   750   C  CG2 . VAL   A 1 91  ? 33.22  73.271  29.809 1   41.51  ? 113 VAL   A CG2 1 
ATOM   751   N  N   . PRO   A 1 92  ? 33.499 70.047  33.126 1   39.06  ? 114 PRO   A N   1 
ATOM   752   C  CA  . PRO   A 1 92  ? 33.496 68.726  33.785 1   39.23  ? 114 PRO   A CA  1 
ATOM   753   C  C   . PRO   A 1 92  ? 32.333 68.477  34.762 1   39.35  ? 114 PRO   A C   1 
ATOM   754   O  O   . PRO   A 1 92  ? 31.992 67.32   35.021 1   39.71  ? 114 PRO   A O   1 
ATOM   755   C  CB  . PRO   A 1 92  ? 34.862 68.676  34.481 1   39.54  ? 114 PRO   A CB  1 
ATOM   756   C  CG  . PRO   A 1 92  ? 35.702 69.63   33.732 1   39.53  ? 114 PRO   A CG  1 
ATOM   757   C  CD  . PRO   A 1 92  ? 34.789 70.735  33.339 1   38.16  ? 114 PRO   A CD  1 
ATOM   758   N  N   . ILE   A 1 93  ? 31.71  69.554  35.276 1   38.74  ? 115 ILE   A N   1 
ATOM   759   C  CA  . ILE   A 1 93  ? 30.562 69.454  36.175 1   38.55  ? 115 ILE   A CA  1 
ATOM   760   C  C   . ILE   A 1 93  ? 29.328 69.041  35.372 1   39.26  ? 115 ILE   A C   1 
ATOM   761   O  O   . ILE   A 1 93  ? 28.557 68.203  35.827 1   39.47  ? 115 ILE   A O   1 
ATOM   762   C  CB  . ILE   A 1 93  ? 30.322 70.775  36.944 1   38.19  ? 115 ILE   A CB  1 
ATOM   763   C  CG1 . ILE   A 1 93  ? 31.527 71.149  37.828 1   37.91  ? 115 ILE   A CG1 1 
ATOM   764   C  CG2 . ILE   A 1 93  ? 29.018 70.691  37.768 1   38.84  ? 115 ILE   A CG2 1 
ATOM   765   C  CD1 . ILE   A 1 93  ? 31.379 72.509  38.532 1   38.25  ? 115 ILE   A CD1 1 
ATOM   766   N  N   . LEU   A 1 94  ? 29.135 69.63   34.179 1   39.6   ? 116 LEU   A N   1 
ATOM   767   C  CA  . LEU   A 1 94  ? 28.013 69.247  33.325 1   40.2   ? 116 LEU   A CA  1 
ATOM   768   C  C   . LEU   A 1 94  ? 28.245 67.857  32.729 1   41.15  ? 116 LEU   A C   1 
ATOM   769   O  O   . LEU   A 1 94  ? 27.288 67.107  32.561 1   41.63  ? 116 LEU   A O   1 
ATOM   770   C  CB  . LEU   A 1 94  ? 27.717 70.292  32.231 1   40.16  ? 116 LEU   A CB  1 
ATOM   771   C  CG  . LEU   A 1 94  ? 26.364 70.143  31.515 1   41.11  ? 116 LEU   A CG  1 
ATOM   772   C  CD1 . LEU   A 1 94  ? 25.202 70.062  32.5   1   41.54  ? 116 LEU   A CD1 1 
ATOM   773   C  CD2 . LEU   A 1 94  ? 26.128 71.272  30.55  1   41.71  ? 116 LEU   A CD2 1 
ATOM   774   N  N   . GLU   A 1 95  ? 29.517 67.487  32.47  1   41.35  ? 117 GLU   A N   1 
ATOM   775   C  CA  . GLU   A 1 95  ? 29.884 66.161  31.98  1   42.11  ? 117 GLU   A CA  1 
ATOM   776   C  C   . GLU   A 1 95  ? 29.513 65.034  32.973 1   43.22  ? 117 GLU   A C   1 
ATOM   777   O  O   . GLU   A 1 95  ? 29.649 63.855  32.635 1   44.16  ? 117 GLU   A O   1 
ATOM   778   C  CB  . GLU   A 1 95  ? 31.382 66.099  31.636 1   43.66  ? 117 GLU   A CB  1 
ATOM   779   C  CG  . GLU   A 1 95  ? 31.768 66.934  30.432 1   46.08  ? 117 GLU   A CG  1 
ATOM   780   C  CD  . GLU   A 1 95  ? 33.21  66.769  30     1   49.97  ? 117 GLU   A CD  1 
ATOM   781   O  OE1 . GLU   A 1 95  ? 34.113 67.034  30.828 1   48.98  ? 117 GLU   A OE1 1 
ATOM   782   O  OE2 . GLU   A 1 95  ? 33.436 66.379  28.83  1   52.2   ? 117 GLU   A OE2 1 
ATOM   783   N  N   . THR   A 1 96  ? 29.073 65.387  34.196 1   42.81  ? 118 THR   A N   1 
ATOM   784   C  CA  . THR   A 1 96  ? 28.604 64.442  35.197 1   43.44  ? 118 THR   A CA  1 
ATOM   785   C  C   . THR   A 1 96  ? 27.257 63.801  34.756 1   44.39  ? 118 THR   A C   1 
ATOM   786   O  O   . THR   A 1 96  ? 26.969 62.65   35.114 1   44.68  ? 118 THR   A O   1 
ATOM   787   C  CB  . THR   A 1 96  ? 28.531 65.132  36.55  1   44.65  ? 118 THR   A CB  1 
ATOM   788   O  OG1 . THR   A 1 96  ? 29.839 65.574  36.903 1   45.12  ? 118 THR   A OG1 1 
ATOM   789   C  CG2 . THR   A 1 96  ? 28.048 64.218  37.628 1   46.34  ? 118 THR   A CG2 1 
ATOM   790   N  N   . MET   A 1 97  ? 26.474 64.532  33.928 1   44.55  ? 119 MET   A N   1 
ATOM   791   C  CA  . MET   A 1 97  ? 25.209 64.106  33.363 1   45.65  ? 119 MET   A CA  1 
ATOM   792   C  C   . MET   A 1 97  ? 25.432 63.037  32.289 1   47.23  ? 119 MET   A C   1 
ATOM   793   O  O   . MET   A 1 97  ? 26.34  63.176  31.469 1   47.92  ? 119 MET   A O   1 
ATOM   794   C  CB  . MET   A 1 97  ? 24.5   65.322  32.758 1   45.84  ? 119 MET   A CB  1 
ATOM   795   C  CG  . MET   A 1 97  ? 23.252 64.992  31.976 1   46.34  ? 119 MET   A CG  1 
ATOM   796   S  SD  . MET   A 1 97  ? 22.376 66.488  31.494 1   49.83  ? 119 MET   A SD  1 
ATOM   797   C  CE  . MET   A 1 97  ? 23.633 67.321  30.464 1   43.4   ? 119 MET   A CE  1 
ATOM   798   N  N   . THR   A 1 98  ? 24.626 61.962  32.301 1   47.61  ? 120 THR   A N   1 
ATOM   799   C  CA  . THR   A 1 98  ? 24.775 60.907  31.301 1   48.15  ? 120 THR   A CA  1 
ATOM   800   C  C   . THR   A 1 98  ? 24.06  61.279  30     1   48.48  ? 120 THR   A C   1 
ATOM   801   O  O   . THR   A 1 98  ? 23.082 62.03   30.015 1   48.36  ? 120 THR   A O   1 
ATOM   802   C  CB  . THR   A 1 98  ? 24.375 59.534  31.861 1   49.16  ? 120 THR   A CB  1 
ATOM   803   O  OG1 . THR   A 1 98  ? 22.956 59.432  31.967 1   50.57  ? 120 THR   A OG1 1 
ATOM   804   C  CG2 . THR   A 1 98  ? 25.059 59.22   33.167 1   49.12  ? 120 THR   A CG2 1 
ATOM   805   N  N   . PRO   A 1 99  ? 24.538 60.741  28.861 1   48.72  ? 121 PRO   A N   1 
ATOM   806   C  CA  . PRO   A 1 99  ? 23.897 61.055  27.579 1   48.85  ? 121 PRO   A CA  1 
ATOM   807   C  C   . PRO   A 1 99  ? 22.438 60.632  27.497 1   49.46  ? 121 PRO   A C   1 
ATOM   808   O  O   . PRO   A 1 99  ? 21.664 61.267  26.785 1   49.64  ? 121 PRO   A O   1 
ATOM   809   C  CB  . PRO   A 1 99  ? 24.751 60.289  26.562 1   49.25  ? 121 PRO   A CB  1 
ATOM   810   C  CG  . PRO   A 1 99  ? 26.052 60.037  27.249 1   49.58  ? 121 PRO   A CG  1 
ATOM   811   C  CD  . PRO   A 1 99  ? 25.697 59.845  28.677 1   48.19  ? 121 PRO   A CD  1 
ATOM   812   N  N   . LEU   A 1 100 ? 22.064 59.565  28.211 1   49.8   ? 122 LEU   A N   1 
ATOM   813   C  CA  . LEU   A 1 100 ? 20.688 59.054  28.222 1   50.72  ? 122 LEU   A CA  1 
ATOM   814   C  C   . LEU   A 1 100 ? 19.783 59.907  29.095 1   50.68  ? 122 LEU   A C   1 
ATOM   815   O  O   . LEU   A 1 100 ? 18.599 60.028  28.809 1   50.48  ? 122 LEU   A O   1 
ATOM   816   C  CB  . LEU   A 1 100 ? 20.622 57.6    28.688 1   51.49  ? 122 LEU   A CB  1 
ATOM   817   C  CG  . LEU   A 1 100 ? 21.639 56.661  28.092 1   53.43  ? 122 LEU   A CG  1 
ATOM   818   C  CD1 . LEU   A 1 100 ? 22.895 56.585  28.995 1   54.34  ? 122 LEU   A CD1 1 
ATOM   819   C  CD2 . LEU   A 1 100 ? 21.031 55.294  27.891 1   54.06  ? 122 LEU   A CD2 1 
ATOM   820   N  N   . ASP   A 1 101 ? 20.331 60.484  30.169 1   50.87  ? 123 ASP   A N   1 
ATOM   821   C  CA  . ASP   A 1 101 ? 19.602 61.401  31.029 1   51.15  ? 123 ASP   A CA  1 
ATOM   822   C  C   . ASP   A 1 101 ? 19.36  62.676  30.223 1   50.55  ? 123 ASP   A C   1 
ATOM   823   O  O   . ASP   A 1 101 ? 18.236 63.156  30.18  1   51.04  ? 123 ASP   A O   1 
ATOM   824   C  CB  . ASP   A 1 101 ? 20.399 61.698  32.313 1   53.73  ? 123 ASP   A CB  1 
ATOM   825   C  CG  . ASP   A 1 101 ? 20.29  60.621  33.381 1   59.6   ? 123 ASP   A CG  1 
ATOM   826   O  OD1 . ASP   A 1 101 ? 19.303 59.851  33.348 1   60.55  ? 123 ASP   A OD1 1 
ATOM   827   O  OD2 . ASP   A 1 101 ? 21.203 60.544  34.252 1   61.85  ? 123 ASP   A OD2 1 
ATOM   828   N  N   . PHE   A 1 102 ? 20.386 63.178  29.522 1   49.92  ? 124 PHE   A N   1 
ATOM   829   C  CA  . PHE   A 1 102 ? 20.257 64.354  28.66  1   50.37  ? 124 PHE   A CA  1 
ATOM   830   C  C   . PHE   A 1 102 ? 19.22  64.133  27.549 1   50.91  ? 124 PHE   A C   1 
ATOM   831   O  O   . PHE   A 1 102 ? 18.419 65.017  27.272 1   50.76  ? 124 PHE   A O   1 
ATOM   832   C  CB  . PHE   A 1 102 ? 21.61  64.721  28.049 1   50.12  ? 124 PHE   A CB  1 
ATOM   833   C  CG  . PHE   A 1 102 ? 21.553 65.982  27.23  1   50.85  ? 124 PHE   A CG  1 
ATOM   834   C  CD1 . PHE   A 1 102 ? 21.03  67.146  27.761 1   51.36  ? 124 PHE   A CD1 1 
ATOM   835   C  CD2 . PHE   A 1 102 ? 22.049 66.012  25.936 1   51.66  ? 124 PHE   A CD2 1 
ATOM   836   C  CE1 . PHE   A 1 102 ? 20.974 68.306  27.006 1   51.9   ? 124 PHE   A CE1 1 
ATOM   837   C  CE2 . PHE   A 1 102 ? 22.006 67.178  25.188 1   52.02  ? 124 PHE   A CE2 1 
ATOM   838   C  CZ  . PHE   A 1 102 ? 21.46  68.312  25.725 1   51.74  ? 124 PHE   A CZ  1 
ATOM   839   N  N   . MET   A 1 103 ? 19.208 62.933  26.948 1   51.35  ? 125 MET   A N   1 
ATOM   840   C  CA  . MET   A 1 103 ? 18.272 62.55   25.893 1   52.04  ? 125 MET   A CA  1 
ATOM   841   C  C   . MET   A 1 103 ? 16.8   62.627  26.35  1   52.81  ? 125 MET   A C   1 
ATOM   842   O  O   . MET   A 1 103 ? 15.923 62.94   25.541 1   53.3   ? 125 MET   A O   1 
ATOM   843   C  CB  . MET   A 1 103 ? 18.609 61.13   25.4   1   52.73  ? 125 MET   A CB  1 
ATOM   844   C  CG  . MET   A 1 103 ? 17.985 60.757  24.061 1   55.46  ? 125 MET   A CG  1 
ATOM   845   S  SD  . MET   A 1 103 ? 18.627 59.188  23.373 1   61.5   ? 125 MET   A SD  1 
ATOM   846   C  CE  . MET   A 1 103 ? 20.137 59.766  22.576 1   59.96  ? 125 MET   A CE  1 
ATOM   847   N  N   . ASP   A 1 104 ? 16.536 62.379  27.647 1   52.76  ? 126 ASP   A N   1 
ATOM   848   C  CA  . ASP   A 1 104 ? 15.183 62.36   28.212 1   53.13  ? 126 ASP   A CA  1 
ATOM   849   C  C   . ASP   A 1 104 ? 14.565 63.746  28.46  1   53.35  ? 126 ASP   A C   1 
ATOM   850   O  O   . ASP   A 1 104 ? 13.372 63.824  28.764 1   53.87  ? 126 ASP   A O   1 
ATOM   851   C  CB  . ASP   A 1 104 ? 15.133 61.508  29.494 1   54.65  ? 126 ASP   A CB  1 
ATOM   852   C  CG  . ASP   A 1 104 ? 15.314 60.008  29.274 1   58.58  ? 126 ASP   A CG  1 
ATOM   853   O  OD1 . ASP   A 1 104 ? 15.475 59.588  28.099 1   59.28  ? 126 ASP   A OD1 1 
ATOM   854   O  OD2 . ASP   A 1 104 ? 15.31  59.254  30.276 1   60.15  ? 126 ASP   A OD2 1 
ATOM   855   N  N   . PHE   A 1 105 ? 15.343 64.829  28.322 1   52.74  ? 127 PHE   A N   1 
ATOM   856   C  CA  . PHE   A 1 105 ? 14.797 66.18   28.48  1   52.6   ? 127 PHE   A CA  1 
ATOM   857   C  C   . PHE   A 1 105 ? 15.157 67.117  27.301 1   53.85  ? 127 PHE   A C   1 
ATOM   858   O  O   . PHE   A 1 105 ? 14.635 68.225  27.233 1   53.84  ? 127 PHE   A O   1 
ATOM   859   C  CB  . PHE   A 1 105 ? 15.157 66.801  29.848 1   51.7   ? 127 PHE   A CB  1 
ATOM   860   C  CG  . PHE   A 1 105 ? 16.575 67.289  30.079 1   51.33  ? 127 PHE   A CG  1 
ATOM   861   C  CD1 . PHE   A 1 105 ? 16.947 68.579  29.744 1   51.33  ? 127 PHE   A CD1 1 
ATOM   862   C  CD2 . PHE   A 1 105 ? 17.512 66.48   30.696 1   51.7   ? 127 PHE   A CD2 1 
ATOM   863   C  CE1 . PHE   A 1 105 ? 18.238 69.027  29.966 1   51.71  ? 127 PHE   A CE1 1 
ATOM   864   C  CE2 . PHE   A 1 105 ? 18.804 66.935  30.915 1   52.12  ? 127 PHE   A CE2 1 
ATOM   865   C  CZ  . PHE   A 1 105 ? 19.154 68.21   30.562 1   51.59  ? 127 PHE   A CZ  1 
ATOM   866   N  N   . ARG   A 1 106 ? 16.022 66.664  26.363 1   54.73  ? 128 ARG   A N   1 
ATOM   867   C  CA  . ARG   A 1 106 ? 16.463 67.399  25.171 1   55.97  ? 128 ARG   A CA  1 
ATOM   868   C  C   . ARG   A 1 106 ? 15.286 67.881  24.279 1   56.98  ? 128 ARG   A C   1 
ATOM   869   O  O   . ARG   A 1 106 ? 15.407 68.88   23.566 1   56.88  ? 128 ARG   A O   1 
ATOM   870   C  CB  . ARG   A 1 106 ? 17.406 66.502  24.371 1   57.53  ? 128 ARG   A CB  1 
ATOM   871   C  CG  . ARG   A 1 106 ? 18.13  67.2    23.245 1   62.13  ? 128 ARG   A CG  1 
ATOM   872   C  CD  . ARG   A 1 106 ? 19.397 66.454  22.871 1   66.99  ? 128 ARG   A CD  1 
ATOM   873   N  NE  . ARG   A 1 106 ? 19.127 65.111  22.353 1   70.55  ? 128 ARG   A NE  1 
ATOM   874   C  CZ  . ARG   A 1 106 ? 19.03  64.817  21.06  1   72.55  ? 128 ARG   A CZ  1 
ATOM   875   N  NH1 . ARG   A 1 106 ? 19.181 65.769  20.141 1   70.99  ? 128 ARG   A NH1 1 
ATOM   876   N  NH2 . ARG   A 1 106 ? 18.773 63.572  20.674 1   72.75  ? 128 ARG   A NH2 1 
ATOM   877   N  N   . LYS   A 1 107 ? 14.147 67.186  24.36  1   57.74  ? 129 LYS   A N   1 
ATOM   878   C  CA  . LYS   A 1 107 ? 12.919 67.467  23.62  1   59.12  ? 129 LYS   A CA  1 
ATOM   879   C  C   . LYS   A 1 107 ? 12.402 68.887  23.876 1   59.55  ? 129 LYS   A C   1 
ATOM   880   O  O   . LYS   A 1 107 ? 11.867 69.531  22.974 1   59.68  ? 129 LYS   A O   1 
ATOM   881   C  CB  . LYS   A 1 107 ? 11.825 66.468  24.042 1   62.27  ? 129 LYS   A CB  1 
ATOM   882   C  CG  . LYS   A 1 107 ? 12.258 65      24.043 1   68.66  ? 129 LYS   A CG  1 
ATOM   883   C  CD  . LYS   A 1 107 ? 12.748 64.503  25.422 1   74.57  ? 129 LYS   A CD  1 
ATOM   884   C  CE  . LYS   A 1 107 ? 12.562 63.007  25.595 1   79.08  ? 129 LYS   A CE  1 
ATOM   885   N  NZ  . LYS   A 1 107 ? 11.418 62.68   26.497 1   81.22  ? 129 LYS   A NZ  1 
ATOM   886   N  N   . TYR   A 1 108 ? 12.543 69.359  25.113 1   59.56  ? 130 TYR   A N   1 
ATOM   887   C  CA  . TYR   A 1 108 ? 12.058 70.672  25.531 1   60.53  ? 130 TYR   A CA  1 
ATOM   888   C  C   . TYR   A 1 108 ? 12.975 71.846  25.145 1   61.12  ? 130 TYR   A C   1 
ATOM   889   O  O   . TYR   A 1 108 ? 12.623 73.003  25.403 1   61.45  ? 130 TYR   A O   1 
ATOM   890   C  CB  . TYR   A 1 108 ? 11.829 70.688  27.054 1   60.94  ? 130 TYR   A CB  1 
ATOM   891   C  CG  . TYR   A 1 108 ? 11.01  69.528  27.581 1   62.23  ? 130 TYR   A CG  1 
ATOM   892   C  CD1 . TYR   A 1 108 ? 9.625  69.531  27.49  1   63.36  ? 130 TYR   A CD1 1 
ATOM   893   C  CD2 . TYR   A 1 108 ? 11.62  68.445  28.2   1   63.3   ? 130 TYR   A CD2 1 
ATOM   894   C  CE1 . TYR   A 1 108 ? 8.868  68.472  27.98  1   64.45  ? 130 TYR   A CE1 1 
ATOM   895   C  CE2 . TYR   A 1 108 ? 10.877 67.373  28.675 1   64.4   ? 130 TYR   A CE2 1 
ATOM   896   C  CZ  . TYR   A 1 108 ? 9.499  67.391  28.568 1   65.54  ? 130 TYR   A CZ  1 
ATOM   897   O  OH  . TYR   A 1 108 ? 8.762  66.341  29.065 1   67.13  ? 130 TYR   A OH  1 
ATOM   898   N  N   . LEU   A 1 109 ? 14.138 71.557  24.53  1   60.87  ? 131 LEU   A N   1 
ATOM   899   C  CA  . LEU   A 1 109 ? 15.14  72.554  24.16  1   60.78  ? 131 LEU   A CA  1 
ATOM   900   C  C   . LEU   A 1 109 ? 14.954 73.097  22.735 1   61.24  ? 131 LEU   A C   1 
ATOM   901   O  O   . LEU   A 1 109 ? 14.936 72.325  21.776 1   61.51  ? 131 LEU   A O   1 
ATOM   902   C  CB  . LEU   A 1 109 ? 16.538 71.92   24.321 1   60.37  ? 131 LEU   A CB  1 
ATOM   903   C  CG  . LEU   A 1 109 ? 17.309 72.015  25.663 1   60.67  ? 131 LEU   A CG  1 
ATOM   904   C  CD1 . LEU   A 1 109 ? 16.422 72.146  26.872 1   60.77  ? 131 LEU   A CD1 1 
ATOM   905   C  CD2 . LEU   A 1 109 ? 18.217 70.834  25.831 1   61.02  ? 131 LEU   A CD2 1 
ATOM   906   N  N   . GLN   A 1 116 ? 23.331 81.514  19.614 1   50.56  ? 138 GLN   A N   1 
ATOM   907   C  CA  . GLN   A 1 116 ? 22.895 80.789  20.804 1   51.74  ? 138 GLN   A CA  1 
ATOM   908   C  C   . GLN   A 1 116 ? 22.614 81.777  22.012 1   52.99  ? 138 GLN   A C   1 
ATOM   909   O  O   . GLN   A 1 116 ? 21.456 82.21   22.22  1   53.23  ? 138 GLN   A O   1 
ATOM   910   C  CB  . GLN   A 1 116 ? 23.907 79.653  21.156 1   52.32  ? 138 GLN   A CB  1 
ATOM   911   C  CG  . GLN   A 1 116 ? 23.39  78.694  22.201 1   54.38  ? 138 GLN   A CG  1 
ATOM   912   C  CD  . GLN   A 1 116 ? 22.32  77.817  21.62  1   58.44  ? 138 GLN   A CD  1 
ATOM   913   O  OE1 . GLN   A 1 116 ? 21.11  78.03   21.82  1   59.38  ? 138 GLN   A OE1 1 
ATOM   914   N  NE2 . GLN   A 1 116 ? 22.754 76.813  20.872 1   59.05  ? 138 GLN   A NE2 1 
ATOM   915   N  N   . SER   A 1 117 ? 23.698 82.147  22.774 1   52.49  ? 139 SER   A N   1 
ATOM   916   C  CA  . SER   A 1 117 ? 23.682 83.06   23.918 1   51.81  ? 139 SER   A CA  1 
ATOM   917   C  C   . SER   A 1 117 ? 23.973 84.478  23.441 1   51.13  ? 139 SER   A C   1 
ATOM   918   O  O   . SER   A 1 117 ? 24.96  84.689  22.734 1   51.31  ? 139 SER   A O   1 
ATOM   919   C  CB  . SER   A 1 117 ? 24.766 82.648  24.908 1   52.81  ? 139 SER   A CB  1 
ATOM   920   O  OG  . SER   A 1 117 ? 25.079 83.659  25.854 1   55.43  ? 139 SER   A OG  1 
ATOM   921   N  N   . LEU   A 1 118 ? 23.158 85.454  23.859 1   50.13  ? 140 LEU   A N   1 
ATOM   922   C  CA  . LEU   A 1 118 ? 23.404 86.848  23.49  1   49.8   ? 140 LEU   A CA  1 
ATOM   923   C  C   . LEU   A 1 118 ? 24.716 87.324  24.121 1   49.87  ? 140 LEU   A C   1 
ATOM   924   O  O   . LEU   A 1 118 ? 25.52  87.99   23.455 1   50.41  ? 140 LEU   A O   1 
ATOM   925   C  CB  . LEU   A 1 118 ? 22.249 87.751  23.966 1   49.72  ? 140 LEU   A CB  1 
ATOM   926   C  CG  . LEU   A 1 118 ? 22.48  89.265  23.852 1   50.5   ? 140 LEU   A CG  1 
ATOM   927   C  CD1 . LEU   A 1 118 ? 22.512 89.7    22.408 1   50.87  ? 140 LEU   A CD1 1 
ATOM   928   C  CD2 . LEU   A 1 118 ? 21.454 90.034  24.637 1   50.85  ? 140 LEU   A CD2 1 
ATOM   929   N  N   . GLN   A 1 119 ? 24.93  86.973  25.405 1   48.65  ? 141 GLN   A N   1 
ATOM   930   C  CA  . GLN   A 1 119 ? 26.103 87.405  26.135 1   47.84  ? 141 GLN   A CA  1 
ATOM   931   C  C   . GLN   A 1 119 ? 27.385 86.813  25.606 1   47.68  ? 141 GLN   A C   1 
ATOM   932   O  O   . GLN   A 1 119 ? 28.377 87.534  25.559 1   47.87  ? 141 GLN   A O   1 
ATOM   933   C  CB  . GLN   A 1 119 ? 25.938 87.168  27.635 1   48.19  ? 141 GLN   A CB  1 
ATOM   934   C  CG  . GLN   A 1 119 ? 24.954 88.163  28.235 1   47.5   ? 141 GLN   A CG  1 
ATOM   935   C  CD  . GLN   A 1 119 ? 25.024 88.24   29.724 1   46.12  ? 141 GLN   A CD  1 
ATOM   936   O  OE1 . GLN   A 1 119 ? 25.038 87.229  30.419 1   45.11  ? 141 GLN   A OE1 1 
ATOM   937   N  NE2 . GLN   A 1 119 ? 25.036 89.454  30.24  1   45.58  ? 141 GLN   A NE2 1 
ATOM   938   N  N   . PHE   A 1 120 ? 27.379 85.545  25.152 1   47.24  ? 142 PHE   A N   1 
ATOM   939   C  CA  . PHE   A 1 120 ? 28.6   84.955  24.593 1   47.57  ? 142 PHE   A CA  1 
ATOM   940   C  C   . PHE   A 1 120 ? 29.022 85.681  23.329 1   48.04  ? 142 PHE   A C   1 
ATOM   941   O  O   . PHE   A 1 120 ? 30.214 85.912  23.118 1   48.31  ? 142 PHE   A O   1 
ATOM   942   C  CB  . PHE   A 1 120 ? 28.434 83.463  24.305 1   47.66  ? 142 PHE   A CB  1 
ATOM   943   C  CG  . PHE   A 1 120 ? 29.711 82.822  23.809 1   48.29  ? 142 PHE   A CG  1 
ATOM   944   C  CD1 . PHE   A 1 120 ? 30.738 82.52   24.684 1   49.1   ? 142 PHE   A CD1 1 
ATOM   945   C  CD2 . PHE   A 1 120 ? 29.883 82.526  22.467 1   48.62  ? 142 PHE   A CD2 1 
ATOM   946   C  CE1 . PHE   A 1 120 ? 31.912 81.934  24.223 1   49.66  ? 142 PHE   A CE1 1 
ATOM   947   C  CE2 . PHE   A 1 120 ? 31.048 81.927  22.017 1   49.13  ? 142 PHE   A CE2 1 
ATOM   948   C  CZ  . PHE   A 1 120 ? 32.057 81.638  22.894 1   49.17  ? 142 PHE   A CZ  1 
ATOM   949   N  N   . ARG   A 1 121 ? 28.041 86.04   22.488 1   48.08  ? 143 ARG   A N   1 
ATOM   950   C  CA  . ARG   A 1 121 ? 28.282 86.77   21.252 1   48.4   ? 143 ARG   A CA  1 
ATOM   951   C  C   . ARG   A 1 121 ? 28.773 88.167  21.552 1   47.73  ? 143 ARG   A C   1 
ATOM   952   O  O   . ARG   A 1 121 ? 29.695 88.622  20.893 1   48.21  ? 143 ARG   A O   1 
ATOM   953   C  CB  . ARG   A 1 121 ? 27.023 86.799  20.372 1   50.51  ? 143 ARG   A CB  1 
ATOM   954   C  CG  . ARG   A 1 121 ? 27.031 85.734  19.279 1   54.97  ? 143 ARG   A CG  1 
ATOM   955   C  CD  . ARG   A 1 121 ? 27.984 86.072  18.138 1   59.53  ? 143 ARG   A CD  1 
ATOM   956   N  NE  . ARG   A 1 121 ? 27.662 87.335  17.446 1   63.1   ? 143 ARG   A NE  1 
ATOM   957   C  CZ  . ARG   A 1 121 ? 27.139 87.422  16.222 1   64.05  ? 143 ARG   A CZ  1 
ATOM   958   N  NH1 . ARG   A 1 121 ? 26.838 86.321  15.54  1   63.24  ? 143 ARG   A NH1 1 
ATOM   959   N  NH2 . ARG   A 1 121 ? 26.917 88.609  15.671 1   63.25  ? 143 ARG   A NH2 1 
ATOM   960   N  N   . LEU   A 1 122 ? 28.213 88.833  22.572 1   46.9   ? 144 LEU   A N   1 
ATOM   961   C  CA  . LEU   A 1 122 ? 28.679 90.164  22.963 1   46.83  ? 144 LEU   A CA  1 
ATOM   962   C  C   . LEU   A 1 122 ? 30.147 90.139  23.387 1   46.24  ? 144 LEU   A C   1 
ATOM   963   O  O   . LEU   A 1 122 ? 30.865 91.083  23.101 1   46.51  ? 144 LEU   A O   1 
ATOM   964   C  CB  . LEU   A 1 122 ? 27.824 90.761  24.091 1   47.3   ? 144 LEU   A CB  1 
ATOM   965   C  CG  . LEU   A 1 122 ? 26.397 91.149  23.731 1   49.11  ? 144 LEU   A CG  1 
ATOM   966   C  CD1 . LEU   A 1 122 ? 25.671 91.682  24.947 1   49.92  ? 144 LEU   A CD1 1 
ATOM   967   C  CD2 . LEU   A 1 122 ? 26.358 92.16   22.607 1   49.41  ? 144 LEU   A CD2 1 
ATOM   968   N  N   . ILE   A 1 123 ? 30.596 89.053  24.042 1   45.45  ? 145 ILE   A N   1 
ATOM   969   C  CA  . ILE   A 1 123 ? 31.985 88.88   24.46  1   45.19  ? 145 ILE   A CA  1 
ATOM   970   C  C   . ILE   A 1 123 ? 32.873 88.73   23.234 1   45.14  ? 145 ILE   A C   1 
ATOM   971   O  O   . ILE   A 1 123 ? 33.841 89.474  23.083 1   45.32  ? 145 ILE   A O   1 
ATOM   972   C  CB  . ILE   A 1 123 ? 32.133 87.696  25.444 1   45.45  ? 145 ILE   A CB  1 
ATOM   973   C  CG1 . ILE   A 1 123 ? 31.427 88.025  26.772 1   46.33  ? 145 ILE   A CG1 1 
ATOM   974   C  CG2 . ILE   A 1 123 ? 33.612 87.359  25.672 1   45.84  ? 145 ILE   A CG2 1 
ATOM   975   C  CD1 . ILE   A 1 123 ? 31.309 86.897  27.734 1   47.54  ? 145 ILE   A CD1 1 
ATOM   976   N  N   . GLU   A 1 124 ? 32.505 87.816  22.314 1   44.7   ? 146 GLU   A N   1 
ATOM   977   C  CA  . GLU   A 1 124 ? 33.216 87.584  21.054 1   44.48  ? 146 GLU   A CA  1 
ATOM   978   C  C   . GLU   A 1 124 ? 33.395 88.896  20.287 1   44.69  ? 146 GLU   A C   1 
ATOM   979   O  O   . GLU   A 1 124 ? 34.514 89.241  19.923 1   45.27  ? 146 GLU   A O   1 
ATOM   980   C  CB  . GLU   A 1 124 ? 32.445 86.578  20.174 1   45.99  ? 146 GLU   A CB  1 
ATOM   981   C  CG  . GLU   A 1 124 ? 32.648 85.125  20.54  1   49.67  ? 146 GLU   A CG  1 
ATOM   982   C  CD  . GLU   A 1 124 ? 31.91  84.181  19.611 1   55.33  ? 146 GLU   A CD  1 
ATOM   983   O  OE1 . GLU   A 1 124 ? 30.721 84.446  19.325 1   55.92  ? 146 GLU   A OE1 1 
ATOM   984   O  OE2 . GLU   A 1 124 ? 32.51  83.169  19.18  1   57.76  ? 146 GLU   A OE2 1 
ATOM   985   N  N   . ASN   A 1 125 ? 32.301 89.662  20.123 1   44.18  ? 147 ASN   A N   1 
ATOM   986   C  CA  . ASN   A 1 125 ? 32.318 90.932  19.417 1   44.23  ? 147 ASN   A CA  1 
ATOM   987   C  C   . ASN   A 1 125 ? 33.13  92.029  20.14  1   44.34  ? 147 ASN   A C   1 
ATOM   988   O  O   . ASN   A 1 125 ? 33.937 92.695  19.503 1   44.33  ? 147 ASN   A O   1 
ATOM   989   C  CB  . ASN   A 1 125 ? 30.899 91.402  19.138 1   44.86  ? 147 ASN   A CB  1 
ATOM   990   C  CG  . ASN   A 1 125 ? 30.128 90.54   18.177 1   47.41  ? 147 ASN   A CG  1 
ATOM   991   O  OD1 . ASN   A 1 125 ? 30.687 89.747  17.419 1   49.23  ? 147 ASN   A OD1 1 
ATOM   992   N  ND2 . ASN   A 1 125 ? 28.817 90.687  18.183 1   47.3   ? 147 ASN   A ND2 1 
ATOM   993   N  N   . LYS   A 1 126 ? 32.925 92.216  21.45  1   44.4   ? 148 LYS   A N   1 
ATOM   994   C  CA  . LYS   A 1 126 ? 33.652 93.233  22.208 1   44.79  ? 148 LYS   A CA  1 
ATOM   995   C  C   . LYS   A 1 126 ? 35.146 92.927  22.312 1   45.49  ? 148 LYS   A C   1 
ATOM   996   O  O   . LYS   A 1 126 ? 35.943 93.851  22.411 1   45.21  ? 148 LYS   A O   1 
ATOM   997   C  CB  . LYS   A 1 126 ? 33.041 93.447  23.599 1   45.84  ? 148 LYS   A CB  1 
ATOM   998   C  CG  . LYS   A 1 126 ? 31.683 94.109  23.592 1   48.18  ? 148 LYS   A CG  1 
ATOM   999   C  CD  . LYS   A 1 126 ? 30.952 93.831  24.901 1   50.83  ? 148 LYS   A CD  1 
ATOM   1000  C  CE  . LYS   A 1 126 ? 29.546 94.363  24.892 1   52.73  ? 148 LYS   A CE  1 
ATOM   1001  N  NZ  . LYS   A 1 126 ? 29.543 95.838  24.884 1   54.2   ? 148 LYS   A NZ  1 
ATOM   1002  N  N   . LEU   A 1 127 ? 35.527 91.648  22.306 1   46.64  ? 149 LEU   A N   1 
ATOM   1003  C  CA  . LEU   A 1 127 ? 36.94  91.276  22.324 1   48.32  ? 149 LEU   A CA  1 
ATOM   1004  C  C   . LEU   A 1 127 ? 37.528 91.618  20.944 1   51.1   ? 149 LEU   A C   1 
ATOM   1005  O  O   . LEU   A 1 127 ? 38.574 92.262  20.858 1   50.95  ? 149 LEU   A O   1 
ATOM   1006  C  CB  . LEU   A 1 127 ? 37.129 89.781  22.654 1   47.7   ? 149 LEU   A CB  1 
ATOM   1007  C  CG  . LEU   A 1 127 ? 38.585 89.324  22.792 1   48.67  ? 149 LEU   A CG  1 
ATOM   1008  C  CD1 . LEU   A 1 127 ? 39.295 90.043  23.929 1   49.04  ? 149 LEU   A CD1 1 
ATOM   1009  C  CD2 . LEU   A 1 127 ? 38.674 87.846  23.015 1   49.11  ? 149 LEU   A CD2 1 
ATOM   1010  N  N   . GLY   A 1 128 ? 36.83  91.223  19.88  1   53.31  ? 150 GLY   A N   1 
ATOM   1011  C  CA  . GLY   A 1 128 ? 37.269 91.546  18.535 1   56.09  ? 150 GLY   A CA  1 
ATOM   1012  C  C   . GLY   A 1 128 ? 37.177 90.429  17.523 1   59.13  ? 150 GLY   A C   1 
ATOM   1013  O  O   . GLY   A 1 128 ? 37.879 90.473  16.515 1   59.74  ? 150 GLY   A O   1 
ATOM   1014  N  N   . VAL   A 1 129 ? 36.305 89.435  17.745 1   61.07  ? 151 VAL   A N   1 
ATOM   1015  C  CA  . VAL   A 1 129 ? 36.106 88.363  16.766 1   63.55  ? 151 VAL   A CA  1 
ATOM   1016  C  C   . VAL   A 1 129 ? 35.423 89.006  15.542 1   66.84  ? 151 VAL   A C   1 
ATOM   1017  O  O   . VAL   A 1 129 ? 34.32  89.545  15.648 1   66.69  ? 151 VAL   A O   1 
ATOM   1018  C  CB  . VAL   A 1 129 ? 35.317 87.156  17.335 1   63.83  ? 151 VAL   A CB  1 
ATOM   1019  C  CG1 . VAL   A 1 129 ? 35.001 86.14   16.249 1   64.06  ? 151 VAL   A CG1 1 
ATOM   1020  C  CG2 . VAL   A 1 129 ? 36.083 86.492  18.468 1   64.4   ? 151 VAL   A CG2 1 
ATOM   1021  N  N   . LEU   A 1 130 ? 36.18  89.095  14.436 1   69.45  ? 152 LEU   A N   1 
ATOM   1022  C  CA  . LEU   A 1 130 ? 35.764 89.739  13.196 1   72.13  ? 152 LEU   A CA  1 
ATOM   1023  C  C   . LEU   A 1 130 ? 34.584 89.033  12.564 1   74.27  ? 152 LEU   A C   1 
ATOM   1024  O  O   . LEU   A 1 130 ? 34.631 87.822  12.344 1   74.53  ? 152 LEU   A O   1 
ATOM   1025  C  CB  . LEU   A 1 130 ? 36.942 89.821  12.208 1   72.85  ? 152 LEU   A CB  1 
ATOM   1026  C  CG  . LEU   A 1 130 ? 38.147 90.589  12.713 1   74.84  ? 152 LEU   A CG  1 
ATOM   1027  C  CD1 . LEU   A 1 130 ? 39.31  89.654  12.993 1   75.64  ? 152 LEU   A CD1 1 
ATOM   1028  C  CD2 . LEU   A 1 130 ? 38.542 91.684  11.745 1   75.59  ? 152 LEU   A CD2 1 
ATOM   1029  N  N   . THR   A 1 131 ? 33.531 89.803  12.262 1   75.67  ? 153 THR   A N   1 
ATOM   1030  C  CA  . THR   A 1 131 ? 32.282 89.322  11.668 1   77.72  ? 153 THR   A CA  1 
ATOM   1031  C  C   . THR   A 1 131 ? 32.503 88.54   10.345 1   79.49  ? 153 THR   A C   1 
ATOM   1032  O  O   . THR   A 1 131 ? 31.779 87.583  10.071 1   79.81  ? 153 THR   A O   1 
ATOM   1033  C  CB  . THR   A 1 131 ? 31.299 90.498  11.529 1   79.29  ? 153 THR   A CB  1 
ATOM   1034  O  OG1 . THR   A 1 131 ? 31.18  91.146  12.8   1   80.6   ? 153 THR   A OG1 1 
ATOM   1035  C  CG2 . THR   A 1 131 ? 29.923 90.061  11.05  1   79.61  ? 153 THR   A CG2 1 
ATOM   1036  N  N   . GLU   A 1 132 ? 33.551 88.88   9.581  1   80.43  ? 154 GLU   A N   1 
ATOM   1037  C  CA  . GLU   A 1 132 ? 33.859 88.179  8.335  1   81.96  ? 154 GLU   A CA  1 
ATOM   1038  C  C   . GLU   A 1 132 ? 34.588 86.829  8.531  1   82.72  ? 154 GLU   A C   1 
ATOM   1039  O  O   . GLU   A 1 132 ? 34.993 86.212  7.544  1   82.67  ? 154 GLU   A O   1 
ATOM   1040  C  CB  . GLU   A 1 132 ? 34.64  89.093  7.375  1   85.07  ? 154 GLU   A CB  1 
ATOM   1041  C  CG  . GLU   A 1 132 ? 35.943 89.616  7.954  1   91.35  ? 154 GLU   A CG  1 
ATOM   1042  C  CD  . GLU   A 1 132 ? 35.879 91.003  8.568  1   99.39  ? 154 GLU   A CD  1 
ATOM   1043  O  OE1 . GLU   A 1 132 ? 36.947 91.652  8.665  1   100.4  ? 154 GLU   A OE1 1 
ATOM   1044  O  OE2 . GLU   A 1 132 ? 34.768 91.443  8.949  1   102.24 ? 154 GLU   A OE2 1 
ATOM   1045  N  N   . GLN   A 1 133 ? 34.736 86.362  9.788  1   83.16  ? 155 GLN   A N   1 
ATOM   1046  C  CA  . GLN   A 1 133 ? 35.385 85.077  10.077 1   84.09  ? 155 GLN   A CA  1 
ATOM   1047  C  C   . GLN   A 1 133 ? 34.368 84.001  10.485 1   84.18  ? 155 GLN   A C   1 
ATOM   1048  O  O   . GLN   A 1 133 ? 33.3   84.319  11.01  1   84.2   ? 155 GLN   A O   1 
ATOM   1049  C  CB  . GLN   A 1 133 ? 36.463 85.225  11.163 1   86.22  ? 155 GLN   A CB  1 
ATOM   1050  C  CG  . GLN   A 1 133 ? 37.424 86.391  10.937 1   90.16  ? 155 GLN   A CG  1 
ATOM   1051  C  CD  . GLN   A 1 133 ? 38.23  86.26   9.669  1   95.32  ? 155 GLN   A CD  1 
ATOM   1052  O  OE1 . GLN   A 1 133 ? 38.317 87.194  8.873  1   97.01  ? 155 GLN   A OE1 1 
ATOM   1053  N  NE2 . GLN   A 1 133 ? 38.85  85.105  9.449  1   96.49  ? 155 GLN   A NE2 1 
ATOM   1054  N  N   . GLU   A 1 148 ? 14.374 93.039  19.951 1   66.08  ? 170 GLU   A N   1 
ATOM   1055  C  CA  . GLU   A 1 148 ? 14.952 94.298  19.47  1   66.84  ? 170 GLU   A CA  1 
ATOM   1056  C  C   . GLU   A 1 148 ? 16.003 94.886  20.402 1   66.61  ? 170 GLU   A C   1 
ATOM   1057  O  O   . GLU   A 1 148 ? 16.865 95.648  19.965 1   66.51  ? 170 GLU   A O   1 
ATOM   1058  C  CB  . GLU   A 1 148 ? 13.886 95.34   19.148 1   70.22  ? 170 GLU   A CB  1 
ATOM   1059  C  CG  . GLU   A 1 148 ? 14.347 96.286  18.055 1   76.94  ? 170 GLU   A CG  1 
ATOM   1060  C  CD  . GLU   A 1 148 ? 13.97  97.73   18.288 1   86     ? 170 GLU   A CD  1 
ATOM   1061  O  OE1 . GLU   A 1 148 ? 12.764 98.053  18.185 1   88.27  ? 170 GLU   A OE1 1 
ATOM   1062  O  OE2 . GLU   A 1 148 ? 14.886 98.542  18.559 1   88.61  ? 170 GLU   A OE2 1 
ATOM   1063  N  N   . GLU   A 1 149 ? 15.93  94.545  21.688 1   66.25  ? 171 GLU   A N   1 
ATOM   1064  C  CA  . GLU   A 1 149 ? 16.925 94.96   22.669 1   66.06  ? 171 GLU   A CA  1 
ATOM   1065  C  C   . GLU   A 1 149 ? 18.226 94.166  22.39  1   64.74  ? 171 GLU   A C   1 
ATOM   1066  O  O   . GLU   A 1 149 ? 19.316 94.742  22.403 1   65.08  ? 171 GLU   A O   1 
ATOM   1067  C  CB  . GLU   A 1 149 ? 16.413 94.654  24.084 1   69.44  ? 171 GLU   A CB  1 
ATOM   1068  C  CG  . GLU   A 1 149 ? 16.837 95.66   25.139 1   76.35  ? 171 GLU   A CG  1 
ATOM   1069  C  CD  . GLU   A 1 149 ? 15.883 96.832  25.319 1   84.68  ? 171 GLU   A CD  1 
ATOM   1070  O  OE1 . GLU   A 1 149 ? 15.069 96.805  26.274 1   86.12  ? 171 GLU   A OE1 1 
ATOM   1071  O  OE2 . GLU   A 1 149 ? 15.954 97.783  24.504 1   87.03  ? 171 GLU   A OE2 1 
ATOM   1072  N  N   . ALA   A 1 150 ? 18.092 92.851  22.089 1   62.75  ? 172 ALA   A N   1 
ATOM   1073  C  CA  . ALA   A 1 150 ? 19.192 91.951  21.751 1   61.3   ? 172 ALA   A CA  1 
ATOM   1074  C  C   . ALA   A 1 150 ? 19.819 92.299  20.397 1   59.87  ? 172 ALA   A C   1 
ATOM   1075  O  O   . ALA   A 1 150 ? 21.034 92.171  20.23  1   59.81  ? 172 ALA   A O   1 
ATOM   1076  C  CB  . ALA   A 1 150 ? 18.694 90.519  21.734 1   61.24  ? 172 ALA   A CB  1 
ATOM   1077  N  N   . ARG   A 1 151 ? 18.996 92.737  19.433 1   58.53  ? 173 ARG   A N   1 
ATOM   1078  C  CA  . ARG   A 1 151 ? 19.488 93.118  18.114 1   57.64  ? 173 ARG   A CA  1 
ATOM   1079  C  C   . ARG   A 1 151 ? 20.315 94.38   18.186 1   56.95  ? 173 ARG   A C   1 
ATOM   1080  O  O   . ARG   A 1 151 ? 21.359 94.466  17.551 1   56.91  ? 173 ARG   A O   1 
ATOM   1081  C  CB  . ARG   A 1 151 ? 18.34  93.274  17.122 1   58.6   ? 173 ARG   A CB  1 
ATOM   1082  C  CG  . ARG   A 1 151 ? 17.97  91.951  16.471 1   61.2   ? 173 ARG   A CG  1 
ATOM   1083  C  CD  . ARG   A 1 151 ? 17.124 92.098  15.222 1   64.18  ? 173 ARG   A CD  1 
ATOM   1084  N  NE  . ARG   A 1 151 ? 15.953 92.96   15.409 1   67.23  ? 173 ARG   A NE  1 
ATOM   1085  C  CZ  . ARG   A 1 151 ? 14.802 92.564  15.947 1   69.88  ? 173 ARG   A CZ  1 
ATOM   1086  N  NH1 . ARG   A 1 151 ? 14.659 91.317  16.385 1   69.77  ? 173 ARG   A NH1 1 
ATOM   1087  N  NH2 . ARG   A 1 151 ? 13.793 93.415  16.067 1   69.82  ? 173 ARG   A NH2 1 
ATOM   1088  N  N   . ASN   A 1 152 ? 19.858 95.348  18.977 1   56.64  ? 174 ASN   A N   1 
ATOM   1089  C  CA  . ASN   A 1 152 ? 20.55  96.613  19.21  1   56.95  ? 174 ASN   A CA  1 
ATOM   1090  C  C   . ASN   A 1 152 ? 21.881 96.343  19.903 1   56.91  ? 174 ASN   A C   1 
ATOM   1091  O  O   . ASN   A 1 152 ? 22.874 96.965  19.558 1   56.58  ? 174 ASN   A O   1 
ATOM   1092  C  CB  . ASN   A 1 152 ? 19.683 97.534  20.082 1   58.29  ? 174 ASN   A CB  1 
ATOM   1093  C  CG  . ASN   A 1 152 ? 20.189 98.95   20.221 1   61.78  ? 174 ASN   A CG  1 
ATOM   1094  O  OD1 . ASN   A 1 152 ? 20.299 99.697  19.231 1   63.4   ? 174 ASN   A OD1 1 
ATOM   1095  N  ND2 . ASN   A 1 152 ? 20.476 99.362  21.465 1   61.61  ? 174 ASN   A ND2 1 
ATOM   1096  N  N   . SER   A 1 153 ? 21.905 95.409  20.872 1   57.2   ? 175 SER   A N   1 
ATOM   1097  C  CA  . SER   A 1 153 ? 23.112 95.045  21.612 1   57.58  ? 175 SER   A CA  1 
ATOM   1098  C  C   . SER   A 1 153 ? 24.186 94.497  20.665 1   57.39  ? 175 SER   A C   1 
ATOM   1099  O  O   . SER   A 1 153 ? 25.334 94.943  20.718 1   56.97  ? 175 SER   A O   1 
ATOM   1100  C  CB  . SER   A 1 153 ? 22.789 94.021  22.697 1   59.13  ? 175 SER   A CB  1 
ATOM   1101  O  OG  . SER   A 1 153 ? 21.922 94.547  23.689 1   61.97  ? 175 SER   A OG  1 
ATOM   1102  N  N   . ILE   A 1 154 ? 23.802 93.561  19.776 1   57.34  ? 176 ILE   A N   1 
ATOM   1103  C  CA  . ILE   A 1 154 ? 24.727 92.967  18.824 1   57.79  ? 176 ILE   A CA  1 
ATOM   1104  C  C   . ILE   A 1 154 ? 25.162 93.983  17.775 1   58.47  ? 176 ILE   A C   1 
ATOM   1105  O  O   . ILE   A 1 154 ? 26.341 94.033  17.437 1   58.31  ? 176 ILE   A O   1 
ATOM   1106  C  CB  . ILE   A 1 154 ? 24.163 91.653  18.254 1   58.15  ? 176 ILE   A CB  1 
ATOM   1107  C  CG1 . ILE   A 1 154 ? 24.395 90.545  19.317 1   59.32  ? 176 ILE   A CG1 1 
ATOM   1108  C  CG2 . ILE   A 1 154 ? 24.785 91.296  16.89  1   58.35  ? 176 ILE   A CG2 1 
ATOM   1109  C  CD1 . ILE   A 1 154 ? 24.015 89.164  18.958 1   60.82  ? 176 ILE   A CD1 1 
ATOM   1110  N  N   . ARG   A 1 155 ? 24.256 94.868  17.347 1   59.3   ? 177 ARG   A N   1 
ATOM   1111  C  CA  . ARG   A 1 155 ? 24.596 95.93   16.407 1   60.57  ? 177 ARG   A CA  1 
ATOM   1112  C  C   . ARG   A 1 155 ? 25.681 96.833  17.005 1   60.28  ? 177 ARG   A C   1 
ATOM   1113  O  O   . ARG   A 1 155 ? 26.734 96.972  16.401 1   60.98  ? 177 ARG   A O   1 
ATOM   1114  C  CB  . ARG   A 1 155 ? 23.351 96.752  16.023 1   63.8   ? 177 ARG   A CB  1 
ATOM   1115  C  CG  . ARG   A 1 155 ? 22.908 96.567  14.582 1   70.73  ? 177 ARG   A CG  1 
ATOM   1116  C  CD  . ARG   A 1 155 ? 23.812 97.259  13.557 1   77.69  ? 177 ARG   A CD  1 
ATOM   1117  N  NE  . ARG   A 1 155 ? 24.057 96.423  12.371 1   83.84  ? 177 ARG   A NE  1 
ATOM   1118  C  CZ  . ARG   A 1 155 ? 23.254 96.358  11.312 1   88.33  ? 177 ARG   A CZ  1 
ATOM   1119  N  NH1 . ARG   A 1 155 ? 22.146 97.09   11.263 1   88.76  ? 177 ARG   A NH1 1 
ATOM   1120  N  NH2 . ARG   A 1 155 ? 23.554 95.561  10.292 1   88.91  ? 177 ARG   A NH2 1 
ATOM   1121  N  N   . ASN   A 1 156 ? 25.474 97.329  18.233 1   59.29  ? 178 ASN   A N   1 
ATOM   1122  C  CA  . ASN   A 1 156 ? 26.423 98.194  18.932 1   58.8   ? 178 ASN   A CA  1 
ATOM   1123  C  C   . ASN   A 1 156 ? 27.759 97.529  19.19  1   57.58  ? 178 ASN   A C   1 
ATOM   1124  O  O   . ASN   A 1 156 ? 28.777 98.197  19.107 1   57.65  ? 178 ASN   A O   1 
ATOM   1125  C  CB  . ASN   A 1 156 ? 25.832 98.722  20.246 1   60.29  ? 178 ASN   A CB  1 
ATOM   1126  C  CG  . ASN   A 1 156 ? 24.648 99.633  20.057 1   64.13  ? 178 ASN   A CG  1 
ATOM   1127  O  OD1 . ASN   A 1 156 ? 24.335 100.06  18.933 1   65.67  ? 178 ASN   A OD1 1 
ATOM   1128  N  ND2 . ASN   A 1 156 ? 23.949 99.934  21.151 1   64.58  ? 178 ASN   A ND2 1 
ATOM   1129  N  N   . SER   A 1 157 ? 27.77  96.227  19.493 1   56.46  ? 179 SER   A N   1 
ATOM   1130  C  CA  . SER   A 1 157 ? 29.015 95.495  19.74  1   55.94  ? 179 SER   A CA  1 
ATOM   1131  C  C   . SER   A 1 157 ? 29.896 95.369  18.478 1   55.7   ? 179 SER   A C   1 
ATOM   1132  O  O   . SER   A 1 157 ? 31.109 95.219  18.589 1   55.76  ? 179 SER   A O   1 
ATOM   1133  C  CB  . SER   A 1 157 ? 28.718 94.121  20.332 1   56.67  ? 179 SER   A CB  1 
ATOM   1134  O  OG  . SER   A 1 157 ? 28.199 93.238  19.353 1   58.58  ? 179 SER   A OG  1 
ATOM   1135  N  N   . GLU   A 1 158 ? 29.289 95.456  17.286 1   55.33  ? 180 GLU   A N   1 
ATOM   1136  C  CA  . GLU   A 1 158 ? 29.993 95.397  16.013 1   55.53  ? 180 GLU   A CA  1 
ATOM   1137  C  C   . GLU   A 1 158 ? 30.412 96.801  15.545 1   55.78  ? 180 GLU   A C   1 
ATOM   1138  O  O   . GLU   A 1 158 ? 31.49  96.971  14.963 1   55.65  ? 180 GLU   A O   1 
ATOM   1139  C  CB  . GLU   A 1 158 ? 29.104 94.725  14.957 1   57.92  ? 180 GLU   A CB  1 
ATOM   1140  C  CG  . GLU   A 1 158 ? 28.831 93.26   15.252 1   63.71  ? 180 GLU   A CG  1 
ATOM   1141  C  CD  . GLU   A 1 158 ? 27.825 92.576  14.344 1   71.08  ? 180 GLU   A CD  1 
ATOM   1142  O  OE1 . GLU   A 1 158 ? 27.095 93.296  13.622 1   73.24  ? 180 GLU   A OE1 1 
ATOM   1143  O  OE2 . GLU   A 1 158 ? 27.764 91.322  14.357 1   72.21  ? 180 GLU   A OE2 1 
ATOM   1144  N  N   . LYS   A 1 159 ? 29.562 97.806  15.803 1   55.95  ? 181 LYS   A N   1 
ATOM   1145  C  CA  . LYS   A 1 159 ? 29.816 99.191  15.4   1   56.66  ? 181 LYS   A CA  1 
ATOM   1146  C  C   . LYS   A 1 159 ? 30.839 99.899  16.287 1   55.97  ? 181 LYS   A C   1 
ATOM   1147  O  O   . LYS   A 1 159 ? 31.752 100.545 15.77  1   56.14  ? 181 LYS   A O   1 
ATOM   1148  C  CB  . LYS   A 1 159 ? 28.507 99.999  15.339 1   59.81  ? 181 LYS   A CB  1 
ATOM   1149  C  CG  . LYS   A 1 159 ? 27.48  99.43   14.368 1   66.35  ? 181 LYS   A CG  1 
ATOM   1150  C  CD  . LYS   A 1 159 ? 27.96  99.454  12.912 1   72.84  ? 181 LYS   A CD  1 
ATOM   1151  C  CE  . LYS   A 1 159 ? 26.923 98.883  11.97  1   77.89  ? 181 LYS   A CE  1 
ATOM   1152  N  NZ  . LYS   A 1 159 ? 27.129 99.357  10.571 1   80.69  ? 181 LYS   A NZ  1 
ATOM   1153  N  N   . ASP   A 1 160 ? 30.668 99.81   17.611 1   54.91  ? 182 ASP   A N   1 
ATOM   1154  C  CA  . ASP   A 1 160 ? 31.579 100.439 18.558 1   54.54  ? 182 ASP   A CA  1 
ATOM   1155  C  C   . ASP   A 1 160 ? 32.934 99.741  18.579 1   53.72  ? 182 ASP   A C   1 
ATOM   1156  O  O   . ASP   A 1 160 ? 33.023 98.544  18.283 1   53.85  ? 182 ASP   A O   1 
ATOM   1157  C  CB  . ASP   A 1 160 ? 30.941 100.503 19.956 1   56.55  ? 182 ASP   A CB  1 
ATOM   1158  C  CG  . ASP   A 1 160 ? 29.598 101.214 19.984 1   61.04  ? 182 ASP   A CG  1 
ATOM   1159  O  OD1 . ASP   A 1 160 ? 29.28  101.929 19.003 1   61.62  ? 182 ASP   A OD1 1 
ATOM   1160  O  OD2 . ASP   A 1 160 ? 28.861 101.046 20.976 1   63.24  ? 182 ASP   A OD2 1 
ATOM   1161  N  N   . PRO   A 1 161 ? 34.018 100.488 18.853 1   52.83  ? 183 PRO   A N   1 
ATOM   1162  C  CA  . PRO   A 1 161 ? 35.354 99.878  18.79  1   52.38  ? 183 PRO   A CA  1 
ATOM   1163  C  C   . PRO   A 1 161 ? 35.6   98.737  19.758 1   51.76  ? 183 PRO   A C   1 
ATOM   1164  O  O   . PRO   A 1 161 ? 35.423 98.889  20.957 1   52.16  ? 183 PRO   A O   1 
ATOM   1165  C  CB  . PRO   A 1 161 ? 36.3   101.054 19.038 1   52.97  ? 183 PRO   A CB  1 
ATOM   1166  C  CG  . PRO   A 1 161 ? 35.47  102.076 19.723 1   53.41  ? 183 PRO   A CG  1 
ATOM   1167  C  CD  . PRO   A 1 161 ? 34.1   101.929 19.155 1   51.97  ? 183 PRO   A CD  1 
ATOM   1168  N  N   . SER   A 1 162 ? 36.024 97.594  19.223 1   50.84  ? 184 SER   A N   1 
ATOM   1169  C  CA  . SER   A 1 162 ? 36.336 96.407  20.003 1   50.71  ? 184 SER   A CA  1 
ATOM   1170  C  C   . SER   A 1 162 ? 37.663 96.578  20.772 1   50.76  ? 184 SER   A C   1 
ATOM   1171  O  O   . SER   A 1 162 ? 38.361 97.583  20.587 1   51.43  ? 184 SER   A O   1 
ATOM   1172  C  CB  . SER   A 1 162 ? 36.403 95.19   19.078 1   51.85  ? 184 SER   A CB  1 
ATOM   1173  O  OG  . SER   A 1 162 ? 37.549 95.222  18.244 1   53.62  ? 184 SER   A OG  1 
ATOM   1174  N  N   . LEU   A 1 163 ? 38.012 95.614  21.64  1   50.08  ? 185 LEU   A N   1 
ATOM   1175  C  CA  . LEU   A 1 163 ? 39.28  95.663  22.36  1   50.4   ? 185 LEU   A CA  1 
ATOM   1176  C  C   . LEU   A 1 163 ? 40.461 95.557  21.386 1   50.09  ? 185 LEU   A C   1 
ATOM   1177  O  O   . LEU   A 1 163 ? 41.461 96.219  21.6   1   50.29  ? 185 LEU   A O   1 
ATOM   1178  C  CB  . LEU   A 1 163 ? 39.36  94.579  23.44  1   50.96  ? 185 LEU   A CB  1 
ATOM   1179  C  CG  . LEU   A 1 163 ? 38.543 94.863  24.696 1   52.75  ? 185 LEU   A CG  1 
ATOM   1180  C  CD1 . LEU   A 1 163 ? 38.589 93.685  25.632 1   53.61  ? 185 LEU   A CD1 1 
ATOM   1181  C  CD2 . LEU   A 1 163 ? 39.02  96.128  25.402 1   53.06  ? 185 LEU   A CD2 1 
ATOM   1182  N  N   . LEU   A 1 164 ? 40.318 94.79   20.292 1   49.51  ? 186 LEU   A N   1 
ATOM   1183  C  CA  . LEU   A 1 164 ? 41.337 94.652  19.25  1   49.44  ? 186 LEU   A CA  1 
ATOM   1184  C  C   . LEU   A 1 164 ? 41.629 96.004  18.591 1   49.93  ? 186 LEU   A C   1 
ATOM   1185  O  O   . LEU   A 1 164 ? 42.799 96.339  18.391 1   50.38  ? 186 LEU   A O   1 
ATOM   1186  C  CB  . LEU   A 1 164 ? 40.873 93.642  18.19  1   49.21  ? 186 LEU   A CB  1 
ATOM   1187  C  CG  . LEU   A 1 164 ? 41.786 93.438  16.992 1   50.69  ? 186 LEU   A CG  1 
ATOM   1188  C  CD1 . LEU   A 1 164 ? 43.147 92.901  17.407 1   51.35  ? 186 LEU   A CD1 1 
ATOM   1189  C  CD2 . LEU   A 1 164 ? 41.175 92.497  16.02  1   51.43  ? 186 LEU   A CD2 1 
ATOM   1190  N  N   . GLU   A 1 165 ? 40.577 96.791  18.272 1   49.51  ? 187 GLU   A N   1 
ATOM   1191  C  CA  . GLU   A 1 165 ? 40.757 98.098  17.649 1   49.6   ? 187 GLU   A CA  1 
ATOM   1192  C  C   . GLU   A 1 165 ? 41.392 99.092  18.616 1   48.95  ? 187 GLU   A C   1 
ATOM   1193  O  O   . GLU   A 1 165 ? 42.309 99.81   18.231 1   48.73  ? 187 GLU   A O   1 
ATOM   1194  C  CB  . GLU   A 1 165 ? 39.419 98.668  17.161 1   52.82  ? 187 GLU   A CB  1 
ATOM   1195  C  CG  . GLU   A 1 165 ? 38.701 97.87   16.096 1   59.79  ? 187 GLU   A CG  1 
ATOM   1196  C  CD  . GLU   A 1 165 ? 37.329 98.451  15.807 1   69.64  ? 187 GLU   A CD  1 
ATOM   1197  O  OE1 . GLU   A 1 165 ? 37.205 99.699  15.809 1   71.81  ? 187 GLU   A OE1 1 
ATOM   1198  O  OE2 . GLU   A 1 165 ? 36.374 97.664  15.608 1   72.73  ? 187 GLU   A OE2 1 
ATOM   1199  N  N   . LEU   A 1 166 ? 40.896 99.144  19.86  1   48.73  ? 188 LEU   A N   1 
ATOM   1200  C  CA  . LEU   A 1 166 ? 41.385 100.065 20.886 1   49.12  ? 188 LEU   A CA  1 
ATOM   1201  C  C   . LEU   A 1 166 ? 42.812 99.769  21.343 1   48.39  ? 188 LEU   A C   1 
ATOM   1202  O  O   . LEU   A 1 166 ? 43.554 100.699 21.674 1   48.59  ? 188 LEU   A O   1 
ATOM   1203  C  CB  . LEU   A 1 166 ? 40.427 100.091 22.082 1   49.92  ? 188 LEU   A CB  1 
ATOM   1204  C  CG  . LEU   A 1 166 ? 39.043 100.626 21.786 1   52.05  ? 188 LEU   A CG  1 
ATOM   1205  C  CD1 . LEU   A 1 166 ? 38.097 100.333 22.927 1   52.62  ? 188 LEU   A CD1 1 
ATOM   1206  C  CD2 . LEU   A 1 166 ? 39.09  102.115 21.483 1   52.87  ? 188 LEU   A CD2 1 
ATOM   1207  N  N   . VAL   A 1 167 ? 43.192 98.485  21.377 1   47.43  ? 189 VAL   A N   1 
ATOM   1208  C  CA  . VAL   A 1 167 ? 44.552 98.082  21.736 1   47     ? 189 VAL   A CA  1 
ATOM   1209  C  C   . VAL   A 1 167 ? 45.493 98.499  20.611 1   46.96  ? 189 VAL   A C   1 
ATOM   1210  O  O   . VAL   A 1 167 ? 46.566 99.015  20.891 1   47.45  ? 189 VAL   A O   1 
ATOM   1211  C  CB  . VAL   A 1 167 ? 44.647 96.57   22.093 1   47.1   ? 189 VAL   A CB  1 
ATOM   1212  C  CG1 . VAL   A 1 167 ? 46.052 96.006  21.877 1   47.59  ? 189 VAL   A CG1 1 
ATOM   1213  C  CG2 . VAL   A 1 167 ? 44.175 96.317  23.519 1   47.02  ? 189 VAL   A CG2 1 
ATOM   1214  N  N   . GLN   A 1 168 ? 45.078 98.321  19.344 1   46.55  ? 190 GLN   A N   1 
ATOM   1215  C  CA  . GLN   A 1 168 ? 45.875 98.721  18.19  1   46.93  ? 190 GLN   A CA  1 
ATOM   1216  C  C   . GLN   A 1 168 ? 46.197 100.204 18.218 1   47.04  ? 190 GLN   A C   1 
ATOM   1217  O  O   . GLN   A 1 168 ? 47.355 100.568 18.021 1   46.83  ? 190 GLN   A O   1 
ATOM   1218  C  CB  . GLN   A 1 168 ? 45.176 98.356  16.884 1   48.76  ? 190 GLN   A CB  1 
ATOM   1219  C  CG  . GLN   A 1 168 ? 45.556 96.983  16.383 1   53.37  ? 190 GLN   A CG  1 
ATOM   1220  C  CD  . GLN   A 1 168 ? 44.824 96.657  15.114 1   59.18  ? 190 GLN   A CD  1 
ATOM   1221  O  OE1 . GLN   A 1 168 ? 44.069 95.683  15.055 1   60.4   ? 190 GLN   A OE1 1 
ATOM   1222  N  NE2 . GLN   A 1 168 ? 45.03  97.469  14.069 1   60.31  ? 190 GLN   A NE2 1 
ATOM   1223  N  N   . ARG   A 1 169 ? 45.197 101.051 18.521 1   47.2   ? 191 ARG   A N   1 
ATOM   1224  C  CA  . ARG   A 1 169 ? 45.416 102.492 18.597 1   48.32  ? 191 ARG   A CA  1 
ATOM   1225  C  C   . ARG   A 1 169 ? 46.383 102.868 19.707 1   47.54  ? 191 ARG   A C   1 
ATOM   1226  O  O   . ARG   A 1 169 ? 47.199 103.766 19.514 1   47.55  ? 191 ARG   A O   1 
ATOM   1227  C  CB  . ARG   A 1 169 ? 44.095 103.247 18.724 1   51.8   ? 191 ARG   A CB  1 
ATOM   1228  C  CG  . ARG   A 1 169 ? 43.34  103.29  17.4   1   59.18  ? 191 ARG   A CG  1 
ATOM   1229  C  CD  . ARG   A 1 169 ? 41.849 103.494 17.625 1   66.19  ? 191 ARG   A CD  1 
ATOM   1230  N  NE  . ARG   A 1 169 ? 41.028 102.816 16.613 1   71.99  ? 191 ARG   A NE  1 
ATOM   1231  C  CZ  . ARG   A 1 169 ? 39.718 102.602 16.736 1   75.44  ? 191 ARG   A CZ  1 
ATOM   1232  N  NH1 . ARG   A 1 169 ? 39.068 103.015 17.82  1   75.73  ? 191 ARG   A NH1 1 
ATOM   1233  N  NH2 . ARG   A 1 169 ? 39.049 101.979 15.773 1   75.23  ? 191 ARG   A NH2 1 
ATOM   1234  N  N   . TRP   A 1 170 ? 46.324 102.148 20.84  1   46.59  ? 192 TRP   A N   1 
ATOM   1235  C  CA  . TRP   A 1 170 ? 47.203 102.33  21.983 1   46.26  ? 192 TRP   A CA  1 
ATOM   1236  C  C   . TRP   A 1 170 ? 48.63  101.968 21.585 1   46.69  ? 192 TRP   A C   1 
ATOM   1237  O  O   . TRP   A 1 170 ? 49.559 102.73  21.865 1   46.65  ? 192 TRP   A O   1 
ATOM   1238  C  CB  . TRP   A 1 170 ? 46.705 101.469 23.171 1   45.8   ? 192 TRP   A CB  1 
ATOM   1239  C  CG  . TRP   A 1 170 ? 47.668 101.315 24.316 1   45.65  ? 192 TRP   A CG  1 
ATOM   1240  C  CD1 . TRP   A 1 170 ? 48.007 102.26  25.244 1   46.42  ? 192 TRP   A CD1 1 
ATOM   1241  C  CD2 . TRP   A 1 170 ? 48.345 100.112 24.703 1   45.36  ? 192 TRP   A CD2 1 
ATOM   1242  N  NE1 . TRP   A 1 170 ? 48.896 101.731 26.154 1   46.57  ? 192 TRP   A NE1 1 
ATOM   1243  C  CE2 . TRP   A 1 170 ? 49.11  100.41  25.851 1   46.04  ? 192 TRP   A CE2 1 
ATOM   1244  C  CE3 . TRP   A 1 170 ? 48.383 98.813  24.188 1   45.61  ? 192 TRP   A CE3 1 
ATOM   1245  C  CZ2 . TRP   A 1 170 ? 49.907 99.459  26.481 1   46.25  ? 192 TRP   A CZ2 1 
ATOM   1246  C  CZ3 . TRP   A 1 170 ? 49.159 97.871  24.824 1   46.27  ? 192 TRP   A CZ3 1 
ATOM   1247  C  CH2 . TRP   A 1 170 ? 49.922 98.201  25.947 1   46.39  ? 192 TRP   A CH2 1 
ATOM   1248  N  N   . LEU   A 1 171 ? 48.792 100.826 20.892 1   47.12  ? 193 LEU   A N   1 
ATOM   1249  C  CA  . LEU   A 1 171 ? 50.072 100.302 20.418 1   47.82  ? 193 LEU   A CA  1 
ATOM   1250  C  C   . LEU   A 1 171 ? 50.726 101.234 19.42  1   48.68  ? 193 LEU   A C   1 
ATOM   1251  O  O   . LEU   A 1 171 ? 51.94  101.402 19.45  1   48.81  ? 193 LEU   A O   1 
ATOM   1252  C  CB  . LEU   A 1 171 ? 49.866 98.924  19.786 1   48.03  ? 193 LEU   A CB  1 
ATOM   1253  C  CG  . LEU   A 1 171 ? 49.734 97.764  20.763 1   49.13  ? 193 LEU   A CG  1 
ATOM   1254  C  CD1 . LEU   A 1 171 ? 49.266 96.524  20.052 1   49.47  ? 193 LEU   A CD1 1 
ATOM   1255  C  CD2 . LEU   A 1 171 ? 51.051 97.498  21.474 1   49.42  ? 193 LEU   A CD2 1 
ATOM   1256  N  N   . GLU   A 1 172 ? 49.921 101.84  18.537 1   49.58  ? 194 GLU   A N   1 
ATOM   1257  C  CA  . GLU   A 1 172 ? 50.37  102.794 17.514 1   50.63  ? 194 GLU   A CA  1 
ATOM   1258  C  C   . GLU   A 1 172 ? 50.98  104.061 18.144 1   51.74  ? 194 GLU   A C   1 
ATOM   1259  O  O   . GLU   A 1 172 ? 51.901 104.648 17.579 1   52.04  ? 194 GLU   A O   1 
ATOM   1260  C  CB  . GLU   A 1 172 ? 49.188 103.192 16.618 1   52.24  ? 194 GLU   A CB  1 
ATOM   1261  C  CG  . GLU   A 1 172 ? 48.799 102.157 15.58  1   56.03  ? 194 GLU   A CG  1 
ATOM   1262  C  CD  . GLU   A 1 172 ? 47.398 102.308 15.012 1   62.73  ? 194 GLU   A CD  1 
ATOM   1263  O  OE1 . GLU   A 1 172 ? 46.691 103.267 15.399 1   64.66  ? 194 GLU   A OE1 1 
ATOM   1264  O  OE2 . GLU   A 1 172 ? 46.996 101.45  14.193 1   64.45  ? 194 GLU   A OE2 1 
ATOM   1265  N  N   . ARG   A 1 173 ? 50.465 104.475 19.313 1   52.15  ? 195 ARG   A N   1 
ATOM   1266  C  CA  . ARG   A 1 173 ? 50.94  105.664 20.023 1   52.9   ? 195 ARG   A CA  1 
ATOM   1267  C  C   . ARG   A 1 173 ? 51.996 105.347 21.088 1   53.86  ? 195 ARG   A C   1 
ATOM   1268  O  O   . ARG   A 1 173 ? 52.215 106.157 21.984 1   53.85  ? 195 ARG   A O   1 
ATOM   1269  C  CB  . ARG   A 1 173 ? 49.752 106.428 20.638 1   54.27  ? 195 ARG   A CB  1 
ATOM   1270  C  CG  . ARG   A 1 173 ? 48.663 106.769 19.615 1   58.58  ? 195 ARG   A CG  1 
ATOM   1271  C  CD  . ARG   A 1 173 ? 47.625 107.752 20.125 1   63.01  ? 195 ARG   A CD  1 
ATOM   1272  N  NE  . ARG   A 1 173 ? 46.863 107.215 21.255 1   66.83  ? 195 ARG   A NE  1 
ATOM   1273  C  CZ  . ARG   A 1 173 ? 45.59  106.824 21.193 1   68.83  ? 195 ARG   A CZ  1 
ATOM   1274  N  NH1 . ARG   A 1 173 ? 44.912 106.918 20.051 1   66.62  ? 195 ARG   A NH1 1 
ATOM   1275  N  NH2 . ARG   A 1 173 ? 44.983 106.343 22.274 1   69.11  ? 195 ARG   A NH2 1 
ATOM   1276  N  N   . THR   A 1 174 ? 52.663 104.188 20.986 1   54.58  ? 196 THR   A N   1 
ATOM   1277  C  CA  . THR   A 1 174 ? 53.679 103.782 21.949 1   55.84  ? 196 THR   A CA  1 
ATOM   1278  C  C   . THR   A 1 174 ? 54.899 104.703 21.889 1   57.37  ? 196 THR   A C   1 
ATOM   1279  O  O   . THR   A 1 174 ? 55.478 104.9   20.819 1   57.81  ? 196 THR   A O   1 
ATOM   1280  C  CB  . THR   A 1 174 ? 54.053 102.292 21.741 1   56.71  ? 196 THR   A CB  1 
ATOM   1281  O  OG1 . THR   A 1 174 ? 52.975 101.468 22.186 1   57.17  ? 196 THR   A OG1 1 
ATOM   1282  C  CG2 . THR   A 1 174 ? 55.34  101.889 22.468 1   57.11  ? 196 THR   A CG2 1 
ATOM   1283  N  N   . PRO   A 1 175 ? 55.293 105.294 23.03  1   58.07  ? 197 PRO   A N   1 
ATOM   1284  C  CA  . PRO   A 1 175 ? 56.488 106.148 23.031 1   58.68  ? 197 PRO   A CA  1 
ATOM   1285  C  C   . PRO   A 1 175 ? 57.766 105.341 22.78  1   59.33  ? 197 PRO   A C   1 
ATOM   1286  O  O   . PRO   A 1 175 ? 58.044 104.333 23.443 1   59.55  ? 197 PRO   A O   1 
ATOM   1287  C  CB  . PRO   A 1 175 ? 56.464 106.794 24.417 1   59.3   ? 197 PRO   A CB  1 
ATOM   1288  C  CG  . PRO   A 1 175 ? 55.729 105.834 25.263 1   59.78  ? 197 PRO   A CG  1 
ATOM   1289  C  CD  . PRO   A 1 175 ? 54.711 105.17  24.378 1   57.97  ? 197 PRO   A CD  1 
ATOM   1290  N  N   . GLY   A 1 176 ? 58.519 105.802 21.802 1   59.33  ? 198 GLY   A N   1 
ATOM   1291  C  CA  . GLY   A 1 176 ? 59.741 105.161 21.34  1   59.69  ? 198 GLY   A CA  1 
ATOM   1292  C  C   . GLY   A 1 176 ? 59.71  104.869 19.851 1   59.99  ? 198 GLY   A C   1 
ATOM   1293  O  O   . GLY   A 1 176 ? 60.752 104.619 19.255 1   60.04  ? 198 GLY   A O   1 
ATOM   1294  N  N   . LEU   A 1 177 ? 58.513 104.904 19.235 1   60.39  ? 199 LEU   A N   1 
ATOM   1295  C  CA  . LEU   A 1 177 ? 58.287 104.661 17.814 1   61.25  ? 199 LEU   A CA  1 
ATOM   1296  C  C   . LEU   A 1 177 ? 58.561 105.894 16.958 1   62.74  ? 199 LEU   A C   1 
ATOM   1297  O  O   . LEU   A 1 177 ? 58.942 105.752 15.795 1   62.44  ? 199 LEU   A O   1 
ATOM   1298  C  CB  . LEU   A 1 177 ? 56.833 104.21  17.574 1   60.89  ? 199 LEU   A CB  1 
ATOM   1299  C  CG  . LEU   A 1 177 ? 56.445 102.787 17.961 1   61.58  ? 199 LEU   A CG  1 
ATOM   1300  C  CD1 . LEU   A 1 177 ? 55.029 102.483 17.514 1   61.95  ? 199 LEU   A CD1 1 
ATOM   1301  C  CD2 . LEU   A 1 177 ? 57.404 101.767 17.365 1   61.97  ? 199 LEU   A CD2 1 
ATOM   1302  N  N   . GLU   A 1 178 ? 58.32  107.096 17.511 1   64.2   ? 200 GLU   A N   1 
ATOM   1303  C  CA  . GLU   A 1 178 ? 58.479 108.355 16.782 1   66.08  ? 200 GLU   A CA  1 
ATOM   1304  C  C   . GLU   A 1 178 ? 59.915 108.61  16.297 1   67.48  ? 200 GLU   A C   1 
ATOM   1305  O  O   . GLU   A 1 178 ? 60.876 108.44  17.062 1   67.55  ? 200 GLU   A O   1 
ATOM   1306  C  CB  . GLU   A 1 178 ? 57.936 109.554 17.581 1   68.84  ? 200 GLU   A CB  1 
ATOM   1307  C  CG  . GLU   A 1 178 ? 58.454 109.665 19.003 1   74.89  ? 200 GLU   A CG  1 
ATOM   1308  C  CD  . GLU   A 1 178 ? 57.658 108.884 20.03  1   82.77  ? 200 GLU   A CD  1 
ATOM   1309  O  OE1 . GLU   A 1 178 ? 56.451 108.642 19.794 1   84.85  ? 200 GLU   A OE1 1 
ATOM   1310  O  OE2 . GLU   A 1 178 ? 58.248 108.498 21.067 1   84.16  ? 200 GLU   A OE2 1 
ATOM   1311  N  N   . GLU   A 1 179 ? 60.041 108.99  14.999 1   67.97  ? 201 GLU   A N   1 
ATOM   1312  C  CA  . GLU   A 1 179 ? 61.308 109.269 14.322 1   68.63  ? 201 GLU   A CA  1 
ATOM   1313  C  C   . GLU   A 1 179 ? 62.095 110.369 15.013 1   68.46  ? 201 GLU   A C   1 
ATOM   1314  O  O   . GLU   A 1 179 ? 63.322 110.29  15.083 1   68.74  ? 201 GLU   A O   1 
ATOM   1315  C  CB  . GLU   A 1 179 ? 61.067 109.668 12.856 1   71.79  ? 201 GLU   A CB  1 
ATOM   1316  C  CG  . GLU   A 1 179 ? 60.778 108.505 11.927 1   78.91  ? 201 GLU   A CG  1 
ATOM   1317  C  CD  . GLU   A 1 179 ? 61.201 108.726 10.482 1   87.19  ? 201 GLU   A CD  1 
ATOM   1318  O  OE1 . GLU   A 1 179 ? 60.314 108.955 9.629  1   88.23  ? 201 GLU   A OE1 1 
ATOM   1319  O  OE2 . GLU   A 1 179 ? 62.419 108.65  10.198 1   90.35  ? 201 GLU   A OE2 1 
ATOM   1320  N  N   . SER   A 1 180 ? 61.394 111.41  15.493 1   67.78  ? 202 SER   A N   1 
ATOM   1321  C  CA  . SER   A 1 180 ? 62.024 112.534 16.184 1   67.49  ? 202 SER   A CA  1 
ATOM   1322  C  C   . SER   A 1 180 ? 62.611 112.119 17.537 1   66.65  ? 202 SER   A C   1 
ATOM   1323  O  O   . SER   A 1 180 ? 63.645 112.642 17.945 1   66.78  ? 202 SER   A O   1 
ATOM   1324  C  CB  . SER   A 1 180 ? 61.022 113.668 16.375 1   69.05  ? 202 SER   A CB  1 
ATOM   1325  O  OG  . SER   A 1 180 ? 59.807 113.207 16.943 1   71.44  ? 202 SER   A OG  1 
ATOM   1326  N  N   . GLY   A 1 181 ? 61.95  111.183 18.21  1   65.75  ? 203 GLY   A N   1 
ATOM   1327  C  CA  . GLY   A 1 181 ? 62.385 110.676 19.505 1   65.26  ? 203 GLY   A CA  1 
ATOM   1328  C  C   . GLY   A 1 181 ? 63.35  109.504 19.432 1   64.21  ? 203 GLY   A C   1 
ATOM   1329  O  O   . GLY   A 1 181 ? 64.418 109.607 18.82  1   64.23  ? 203 GLY   A O   1 
ATOM   1330  N  N   . PHE   A 1 182 ? 62.978 108.379 20.063 1   62.85  ? 204 PHE   A N   1 
ATOM   1331  C  CA  . PHE   A 1 182 ? 63.816 107.188 20.094 1   62.06  ? 204 PHE   A CA  1 
ATOM   1332  C  C   . PHE   A 1 182 ? 64     106.511 18.717 1   60.92  ? 204 PHE   A C   1 
ATOM   1333  O  O   . PHE   A 1 182 ? 65.067 105.955 18.466 1   60.9   ? 204 PHE   A O   1 
ATOM   1334  C  CB  . PHE   A 1 182 ? 63.302 106.196 21.139 1   62.1   ? 204 PHE   A CB  1 
ATOM   1335  C  CG  . PHE   A 1 182 ? 64.231 105.03  21.378 1   63.01  ? 204 PHE   A CG  1 
ATOM   1336  C  CD1 . PHE   A 1 182 ? 65.455 105.215 21.998 1   63.9   ? 204 PHE   A CD1 1 
ATOM   1337  C  CD2 . PHE   A 1 182 ? 63.88  103.75  20.98  1   63.74  ? 204 PHE   A CD2 1 
ATOM   1338  C  CE1 . PHE   A 1 182 ? 66.31  104.146 22.205 1   64.52  ? 204 PHE   A CE1 1 
ATOM   1339  C  CE2 . PHE   A 1 182 ? 64.734 102.681 21.202 1   64.29  ? 204 PHE   A CE2 1 
ATOM   1340  C  CZ  . PHE   A 1 182 ? 65.938 102.885 21.815 1   64.21  ? 204 PHE   A CZ  1 
ATOM   1341  N  N   . ASN   A 1 183 ? 62.983 106.573 17.835 1   59.68  ? 205 ASN   A N   1 
ATOM   1342  C  CA  . ASN   A 1 183 ? 63.039 105.996 16.484 1   59.11  ? 205 ASN   A CA  1 
ATOM   1343  C  C   . ASN   A 1 183 ? 63.418 104.51  16.507 1   58.41  ? 205 ASN   A C   1 
ATOM   1344  O  O   . ASN   A 1 183 ? 64.456 104.128 15.986 1   58.56  ? 205 ASN   A O   1 
ATOM   1345  C  CB  . ASN   A 1 183 ? 64.004 106.809 15.617 1   60.36  ? 205 ASN   A CB  1 
ATOM   1346  C  CG  . ASN   A 1 183 ? 63.864 106.598 14.139 1   63.54  ? 205 ASN   A CG  1 
ATOM   1347  O  OD1 . ASN   A 1 183 ? 62.936 105.927 13.654 1   65.02  ? 205 ASN   A OD1 1 
ATOM   1348  N  ND2 . ASN   A 1 183 ? 64.791 107.177 13.398 1   63.77  ? 205 ASN   A ND2 1 
ATOM   1349  N  N   . PHE   A 1 184 ? 62.589 103.677 17.135 1   57.63  ? 206 PHE   A N   1 
ATOM   1350  C  CA  . PHE   A 1 184 ? 62.889 102.257 17.292 1   57.05  ? 206 PHE   A CA  1 
ATOM   1351  C  C   . PHE   A 1 184 ? 62.969 101.48  15.983 1   56.75  ? 206 PHE   A C   1 
ATOM   1352  O  O   . PHE   A 1 184 ? 63.929 100.744 15.791 1   56.46  ? 206 PHE   A O   1 
ATOM   1353  C  CB  . PHE   A 1 184 ? 61.897 101.581 18.275 1   56.64  ? 206 PHE   A CB  1 
ATOM   1354  C  CG  . PHE   A 1 184 ? 61.951 100.067 18.316 1   56.65  ? 206 PHE   A CG  1 
ATOM   1355  C  CD1 . PHE   A 1 184 ? 62.987 99.411  18.958 1   56.97  ? 206 PHE   A CD1 1 
ATOM   1356  C  CD2 . PHE   A 1 184 ? 60.978 99.306  17.69  1   57.31  ? 206 PHE   A CD2 1 
ATOM   1357  C  CE1 . PHE   A 1 184 ? 63.04  98.021  18.983 1   57.51  ? 206 PHE   A CE1 1 
ATOM   1358  C  CE2 . PHE   A 1 184 ? 61.045 97.915  17.701 1   57.84  ? 206 PHE   A CE2 1 
ATOM   1359  C  CZ  . PHE   A 1 184 ? 62.075 97.284  18.346 1   57.3   ? 206 PHE   A CZ  1 
ATOM   1360  N  N   . TRP   A 1 185 ? 61.954 101.585 15.116 1   56.77  ? 207 TRP   A N   1 
ATOM   1361  C  CA  . TRP   A 1 185 ? 61.903 100.791 13.891 1   56.8   ? 207 TRP   A CA  1 
ATOM   1362  C  C   . TRP   A 1 185 ? 63.14  100.931 13.012 1   56.62  ? 207 TRP   A C   1 
ATOM   1363  O  O   . TRP   A 1 185 ? 63.611 99.927  12.482 1   56.95  ? 207 TRP   A O   1 
ATOM   1364  C  CB  . TRP   A 1 185 ? 60.623 101.079 13.108 1   56.85  ? 207 TRP   A CB  1 
ATOM   1365  C  CG  . TRP   A 1 185 ? 60.125 99.934  12.268 1   57.75  ? 207 TRP   A CG  1 
ATOM   1366  C  CD1 . TRP   A 1 185 ? 59.968 99.919  10.913 1   58.67  ? 207 TRP   A CD1 1 
ATOM   1367  C  CD2 . TRP   A 1 185 ? 59.657 98.661  12.74  1   58.13  ? 207 TRP   A CD2 1 
ATOM   1368  N  NE1 . TRP   A 1 185 ? 59.44  98.713  10.51  1   59.02  ? 207 TRP   A NE1 1 
ATOM   1369  C  CE2 . TRP   A 1 185 ? 59.247 97.92   11.611 1   58.9   ? 207 TRP   A CE2 1 
ATOM   1370  C  CE3 . TRP   A 1 185 ? 59.558 98.069  14.005 1   58.82  ? 207 TRP   A CE3 1 
ATOM   1371  C  CZ2 . TRP   A 1 185 ? 58.747 96.621  11.714 1   59.73  ? 207 TRP   A CZ2 1 
ATOM   1372  C  CZ3 . TRP   A 1 185 ? 59.046 96.79   14.102 1   59.77  ? 207 TRP   A CZ3 1 
ATOM   1373  C  CH2 . TRP   A 1 185 ? 58.65  96.079  12.966 1   59.8   ? 207 TRP   A CH2 1 
ATOM   1374  N  N   . ALA   A 1 186 ? 63.7   102.147 12.904 1   56.04  ? 208 ALA   A N   1 
ATOM   1375  C  CA  . ALA   A 1 186 ? 64.896 102.396 12.106 1   55.85  ? 208 ALA   A CA  1 
ATOM   1376  C  C   . ALA   A 1 186 ? 66.134 101.773 12.747 1   55.79  ? 208 ALA   A C   1 
ATOM   1377  O  O   . ALA   A 1 186 ? 66.978 101.219 12.039 1   55.9   ? 208 ALA   A O   1 
ATOM   1378  C  CB  . ALA   A 1 186 ? 65.097 103.89  11.928 1   55.95  ? 208 ALA   A CB  1 
ATOM   1379  N  N   . LYS   A 1 187 ? 66.249 101.868 14.087 1   55.47  ? 209 LYS   A N   1 
ATOM   1380  C  CA  . LYS   A 1 187 ? 67.373 101.287 14.829 1   55.64  ? 209 LYS   A CA  1 
ATOM   1381  C  C   . LYS   A 1 187 ? 67.33  99.751  14.783 1   55.5   ? 209 LYS   A C   1 
ATOM   1382  O  O   . LYS   A 1 187 ? 68.381 99.115  14.747 1   55.49  ? 209 LYS   A O   1 
ATOM   1383  C  CB  . LYS   A 1 187 ? 67.378 101.769 16.287 1   57.53  ? 209 LYS   A CB  1 
ATOM   1384  C  CG  . LYS   A 1 187 ? 67.612 103.268 16.453 1   61.05  ? 209 LYS   A CG  1 
ATOM   1385  C  CD  . LYS   A 1 187 ? 67.47  103.688 17.908 1   64.09  ? 209 LYS   A CD  1 
ATOM   1386  C  CE  . LYS   A 1 187 ? 68.064 105.047 18.169 1   67.8   ? 209 LYS   A CE  1 
ATOM   1387  N  NZ  . LYS   A 1 187 ? 68.004 105.41  19.611 1   70.25  ? 209 LYS   A NZ  1 
ATOM   1388  N  N   . PHE   A 1 188 ? 66.11  99.169  14.781 1   55.15  ? 210 PHE   A N   1 
ATOM   1389  C  CA  . PHE   A 1 188 ? 65.833 97.729  14.717 1   55.07  ? 210 PHE   A CA  1 
ATOM   1390  C  C   . PHE   A 1 188 ? 66.236 97.179  13.337 1   55.57  ? 210 PHE   A C   1 
ATOM   1391  O  O   . PHE   A 1 188 ? 66.928 96.164  13.274 1   55.97  ? 210 PHE   A O   1 
ATOM   1392  C  CB  . PHE   A 1 188 ? 64.34  97.475  15.03  1   54.49  ? 210 PHE   A CB  1 
ATOM   1393  C  CG  . PHE   A 1 188 ? 63.797 96.066  14.923 1   54.51  ? 210 PHE   A CG  1 
ATOM   1394  C  CD1 . PHE   A 1 188 ? 64.586 94.973  15.233 1   54.77  ? 210 PHE   A CD1 1 
ATOM   1395  C  CD2 . PHE   A 1 188 ? 62.471 95.842  14.596 1   55.09  ? 210 PHE   A CD2 1 
ATOM   1396  C  CE1 . PHE   A 1 188 ? 64.086 93.684  15.123 1   55.21  ? 210 PHE   A CE1 1 
ATOM   1397  C  CE2 . PHE   A 1 188 ? 61.968 94.547  14.507 1   55.54  ? 210 PHE   A CE2 1 
ATOM   1398  C  CZ  . PHE   A 1 188 ? 62.78  93.478  14.767 1   55.09  ? 210 PHE   A CZ  1 
ATOM   1399  N  N   . GLN   A 1 189 ? 65.875 97.872  12.242 1   55.24  ? 211 GLN   A N   1 
ATOM   1400  C  CA  . GLN   A 1 189 ? 66.259 97.43   10.899 1   55.59  ? 211 GLN   A CA  1 
ATOM   1401  C  C   . GLN   A 1 189 ? 67.782 97.394  10.738 1   55.81  ? 211 GLN   A C   1 
ATOM   1402  O  O   . GLN   A 1 189 ? 68.317 96.458  10.15  1   56.08  ? 211 GLN   A O   1 
ATOM   1403  C  CB  . GLN   A 1 189 ? 65.656 98.346  9.837  1   57.56  ? 211 GLN   A CB  1 
ATOM   1404  C  CG  . GLN   A 1 189 ? 64.147 98.287  9.752  1   62.01  ? 211 GLN   A CG  1 
ATOM   1405  C  CD  . GLN   A 1 189 ? 63.673 98.571  8.348  1   68.24  ? 211 GLN   A CD  1 
ATOM   1406  O  OE1 . GLN   A 1 189 ? 64.229 98.057  7.362  1   70.13  ? 211 GLN   A OE1 1 
ATOM   1407  N  NE2 . GLN   A 1 189 ? 62.629 99.391  8.224  1   69.11  ? 211 GLN   A NE2 1 
ATOM   1408  N  N   . GLU   A 1 190 ? 68.474 98.397  11.287 1   55.61  ? 212 GLU   A N   1 
ATOM   1409  C  CA  . GLU   A 1 190 ? 69.924 98.502  11.244 1   56.04  ? 212 GLU   A CA  1 
ATOM   1410  C  C   . GLU   A 1 190 ? 70.577 97.409  12.085 1   55.64  ? 212 GLU   A C   1 
ATOM   1411  O  O   . GLU   A 1 190 ? 71.588 96.838  11.678 1   55.8   ? 212 GLU   A O   1 
ATOM   1412  C  CB  . GLU   A 1 190 ? 70.347 99.873  11.775 1   59.87  ? 212 GLU   A CB  1 
ATOM   1413  C  CG  . GLU   A 1 190 ? 70.803 100.853 10.714 1   68     ? 212 GLU   A CG  1 
ATOM   1414  C  CD  . GLU   A 1 190 ? 71.567 102.019 11.317 1   78.06  ? 212 GLU   A CD  1 
ATOM   1415  O  OE1 . GLU   A 1 190 ? 71.208 102.449 12.442 1   80.35  ? 212 GLU   A OE1 1 
ATOM   1416  O  OE2 . GLU   A 1 190 ? 72.54  102.484 10.677 1   80.22  ? 212 GLU   A OE2 1 
ATOM   1417  N  N   . SER   A 1 191 ? 70.012 97.133  13.268 1   54.95  ? 213 SER   A N   1 
ATOM   1418  C  CA  . SER   A 1 191 ? 70.511 96.105  14.169 1   55.13  ? 213 SER   A CA  1 
ATOM   1419  C  C   . SER   A 1 191 ? 70.385 94.737  13.536 1   54.98  ? 213 SER   A C   1 
ATOM   1420  O  O   . SER   A 1 191 ? 71.284 93.915  13.695 1   54.88  ? 213 SER   A O   1 
ATOM   1421  C  CB  . SER   A 1 191 ? 69.734 96.12   15.48  1   56.9   ? 213 SER   A CB  1 
ATOM   1422  O  OG  . SER   A 1 191 ? 69.977 97.306  16.217 1   59.79  ? 213 SER   A OG  1 
ATOM   1423  N  N   . VAL   A 1 192 ? 69.261 94.488  12.831 1   54.86  ? 214 VAL   A N   1 
ATOM   1424  C  CA  . VAL   A 1 192 ? 68.992 93.232  12.14  1   55.24  ? 214 VAL   A CA  1 
ATOM   1425  C  C   . VAL   A 1 192 ? 70.04  93.026  11.05  1   55.55  ? 214 VAL   A C   1 
ATOM   1426  O  O   . VAL   A 1 192 ? 70.621 91.946  10.95  1   55.15  ? 214 VAL   A O   1 
ATOM   1427  C  CB  . VAL   A 1 192 ? 67.535 93.202  11.599 1   55.68  ? 214 VAL   A CB  1 
ATOM   1428  C  CG1 . VAL   A 1 192 ? 67.359 92.196  10.469 1   56.09  ? 214 VAL   A CG1 1 
ATOM   1429  C  CG2 . VAL   A 1 192 ? 66.557 92.904  12.719 1   56.15  ? 214 VAL   A CG2 1 
ATOM   1430  N  N   . ASP   A 1 193 ? 70.305 94.08   10.264 1   55.95  ? 215 ASP   A N   1 
ATOM   1431  C  CA  . ASP   A 1 193 ? 71.268 94.039  9.169  1   56.49  ? 215 ASP   A CA  1 
ATOM   1432  C  C   . ASP   A 1 193 ? 72.661 93.703  9.648  1   56.4   ? 215 ASP   A C   1 
ATOM   1433  O  O   . ASP   A 1 193 ? 73.306 92.838  9.051  1   56.82  ? 215 ASP   A O   1 
ATOM   1434  C  CB  . ASP   A 1 193 ? 71.262 95.353  8.371  1   58.8   ? 215 ASP   A CB  1 
ATOM   1435  C  CG  . ASP   A 1 193 ? 70.068 95.523  7.448  1   63.72  ? 215 ASP   A CG  1 
ATOM   1436  O  OD1 . ASP   A 1 193 ? 69.312 94.533  7.257  1   64.63  ? 215 ASP   A OD1 1 
ATOM   1437  O  OD2 . ASP   A 1 193 ? 69.878 96.65   6.924  1   65.72  ? 215 ASP   A OD2 1 
ATOM   1438  N  N   . ARG   A 1 194 ? 73.11  94.34   10.739 1   55.55  ? 216 ARG   A N   1 
ATOM   1439  C  CA  . ARG   A 1 194 ? 74.423 94.064  11.303 1   55.61  ? 216 ARG   A CA  1 
ATOM   1440  C  C   . ARG   A 1 194 ? 74.491 92.685  11.968 1   54.96  ? 216 ARG   A C   1 
ATOM   1441  O  O   . ARG   A 1 194 ? 75.539 92.033  11.926 1   55.67  ? 216 ARG   A O   1 
ATOM   1442  C  CB  . ARG   A 1 194 ? 74.821 95.156  12.288 1   57.71  ? 216 ARG   A CB  1 
ATOM   1443  C  CG  . ARG   A 1 194 ? 75.124 96.47   11.597 1   63.05  ? 216 ARG   A CG  1 
ATOM   1444  C  CD  . ARG   A 1 194 ? 75.67  97.492  12.565 1   68.55  ? 216 ARG   A CD  1 
ATOM   1445  N  NE  . ARG   A 1 194 ? 74.669 97.871  13.565 1   74.24  ? 216 ARG   A NE  1 
ATOM   1446  C  CZ  . ARG   A 1 194 ? 73.85  98.916  13.453 1   77.42  ? 216 ARG   A CZ  1 
ATOM   1447  N  NH1 . ARG   A 1 194 ? 73.901 99.696  12.376 1   76.74  ? 216 ARG   A NH1 1 
ATOM   1448  N  NH2 . ARG   A 1 194 ? 72.971 99.186  14.415 1   77.47  ? 216 ARG   A NH2 1 
ATOM   1449  N  N   . PHE   A 1 195 ? 73.382 92.237  12.567 1   53.34  ? 217 PHE   A N   1 
ATOM   1450  C  CA  . PHE   A 1 195 ? 73.336 90.942  13.223 1   52.38  ? 217 PHE   A CA  1 
ATOM   1451  C  C   . PHE   A 1 195 ? 73.411 89.825  12.194 1   51.87  ? 217 PHE   A C   1 
ATOM   1452  O  O   . PHE   A 1 195 ? 74.175 88.868  12.365 1   52.17  ? 217 PHE   A O   1 
ATOM   1453  C  CB  . PHE   A 1 195 ? 72.077 90.809  14.101 1   51.95  ? 217 PHE   A CB  1 
ATOM   1454  C  CG  . PHE   A 1 195 ? 71.91  89.436  14.715 1   51.96  ? 217 PHE   A CG  1 
ATOM   1455  C  CD1 . PHE   A 1 195 ? 72.73  89.018  15.745 1   52.27  ? 217 PHE   A CD1 1 
ATOM   1456  C  CD2 . PHE   A 1 195 ? 70.959 88.553  14.232 1   52.22  ? 217 PHE   A CD2 1 
ATOM   1457  C  CE1 . PHE   A 1 195 ? 72.6   87.751  16.279 1   52.91  ? 217 PHE   A CE1 1 
ATOM   1458  C  CE2 . PHE   A 1 195 ? 70.833 87.286  14.769 1   52.59  ? 217 PHE   A CE2 1 
ATOM   1459  C  CZ  . PHE   A 1 195 ? 71.648 86.896  15.792 1   52.58  ? 217 PHE   A CZ  1 
ATOM   1460  N  N   . LEU   A 1 196 ? 72.626 89.943  11.127 1   51.15  ? 218 LEU   A N   1 
ATOM   1461  C  CA  . LEU   A 1 196 ? 72.618 88.939  10.075 1   50.99  ? 218 LEU   A CA  1 
ATOM   1462  C  C   . LEU   A 1 196 ? 73.935 88.901  9.323  1   51.25  ? 218 LEU   A C   1 
ATOM   1463  O  O   . LEU   A 1 196 ? 74.366 87.814  8.959  1   51.13  ? 218 LEU   A O   1 
ATOM   1464  C  CB  . LEU   A 1 196 ? 71.405 89.09   9.138  1   50.59  ? 218 LEU   A CB  1 
ATOM   1465  C  CG  . LEU   A 1 196 ? 70.042 88.833  9.797  1   50.83  ? 218 LEU   A CG  1 
ATOM   1466  C  CD1 . LEU   A 1 196 ? 68.909 89.067  8.82   1   50.84  ? 218 LEU   A CD1 1 
ATOM   1467  C  CD2 . LEU   A 1 196 ? 69.967 87.418  10.422 1   50.87  ? 218 LEU   A CD2 1 
ATOM   1468  N  N   . GLU   A 1 197 ? 74.624 90.049  9.177  1   51.61  ? 219 GLU   A N   1 
ATOM   1469  C  CA  . GLU   A 1 197 ? 75.951 90.089  8.557  1   52.74  ? 219 GLU   A CA  1 
ATOM   1470  C  C   . GLU   A 1 197 ? 76.941 89.31   9.424  1   52.94  ? 219 GLU   A C   1 
ATOM   1471  O  O   . GLU   A 1 197 ? 77.668 88.467  8.906  1   53.42  ? 219 GLU   A O   1 
ATOM   1472  C  CB  . GLU   A 1 197 ? 76.45  91.532  8.378  1   56.41  ? 219 GLU   A CB  1 
ATOM   1473  C  CG  . GLU   A 1 197 ? 75.952 92.214  7.111  1   64.17  ? 219 GLU   A CG  1 
ATOM   1474  C  CD  . GLU   A 1 197 ? 75.942 93.73   7.185  1   72.25  ? 219 GLU   A CD  1 
ATOM   1475  O  OE1 . GLU   A 1 197 ? 76.677 94.292  8.03   1   73.14  ? 219 GLU   A OE1 1 
ATOM   1476  O  OE2 . GLU   A 1 197 ? 75.184 94.357  6.41   1   76.15  ? 219 GLU   A OE2 1 
ATOM   1477  N  N   . ALA   A 1 198 ? 76.925 89.54   10.747 1   52.26  ? 220 ALA   A N   1 
ATOM   1478  C  CA  . ALA   A 1 198 ? 77.794 88.834  11.687 1   51.97  ? 220 ALA   A CA  1 
ATOM   1479  C  C   . ALA   A 1 198 ? 77.545 87.325  11.678 1   51.71  ? 220 ALA   A C   1 
ATOM   1480  O  O   . ALA   A 1 198 ? 78.478 86.539  11.884 1   51.83  ? 220 ALA   A O   1 
ATOM   1481  C  CB  . ALA   A 1 198 ? 77.594 89.385  13.085 1   52.07  ? 220 ALA   A CB  1 
ATOM   1482  N  N   . GLN   A 1 199 ? 76.286 86.924  11.448 1   51.42  ? 221 GLN   A N   1 
ATOM   1483  C  CA  . GLN   A 1 199 ? 75.885 85.522  11.351 1   52.07  ? 221 GLN   A CA  1 
ATOM   1484  C  C   . GLN   A 1 199 ? 76.441 84.863  10.09  1   52.77  ? 221 GLN   A C   1 
ATOM   1485  O  O   . GLN   A 1 199 ? 76.809 83.689  10.114 1   52.29  ? 221 GLN   A O   1 
ATOM   1486  C  CB  . GLN   A 1 199 ? 74.351 85.394  11.374 1   53.09  ? 221 GLN   A CB  1 
ATOM   1487  C  CG  . GLN   A 1 199 ? 73.747 85.517  12.767 1   54.86  ? 221 GLN   A CG  1 
ATOM   1488  C  CD  . GLN   A 1 199 ? 74.27  84.46   13.717 1   58.33  ? 221 GLN   A CD  1 
ATOM   1489  O  OE1 . GLN   A 1 199 ? 74.744 84.774  14.808 1   59.83  ? 221 GLN   A OE1 1 
ATOM   1490  N  NE2 . GLN   A 1 199 ? 74.218 83.184  13.325 1   59     ? 221 GLN   A NE2 1 
ATOM   1491  N  N   . VAL   A 1 200 ? 76.484 85.621  8.988  1   53.9   ? 222 VAL   A N   1 
ATOM   1492  C  CA  . VAL   A 1 200 ? 77.003 85.149  7.703  1   54.94  ? 222 VAL   A CA  1 
ATOM   1493  C  C   . VAL   A 1 200 ? 78.508 84.942  7.809  1   55.91  ? 222 VAL   A C   1 
ATOM   1494  O  O   . VAL   A 1 200 ? 79.004 83.904  7.379  1   55.78  ? 222 VAL   A O   1 
ATOM   1495  C  CB  . VAL   A 1 200 ? 76.606 86.08   6.526  1   55.27  ? 222 VAL   A CB  1 
ATOM   1496  C  CG1 . VAL   A 1 200 ? 77.363 85.717  5.26   1   55.84  ? 222 VAL   A CG1 1 
ATOM   1497  C  CG2 . VAL   A 1 200 ? 75.108 86.021  6.273  1   55.57  ? 222 VAL   A CG2 1 
ATOM   1498  N  N   . GLN   A 1 201 ? 79.221 85.888  8.451  1   56.51  ? 223 GLN   A N   1 
ATOM   1499  C  CA  . GLN   A 1 201 ? 80.665 85.777  8.637  1   57.34  ? 223 GLN   A CA  1 
ATOM   1500  C  C   . GLN   A 1 201 ? 81.023 84.597  9.53   1   58.78  ? 223 GLN   A C   1 
ATOM   1501  O  O   . GLN   A 1 201 ? 81.992 83.893  9.257  1   58.73  ? 223 GLN   A O   1 
ATOM   1502  C  CB  . GLN   A 1 201 ? 81.25  87.087  9.174  1   58.2   ? 223 GLN   A CB  1 
ATOM   1503  C  CG  . GLN   A 1 201 ? 81.025 88.298  8.263  1   60.77  ? 223 GLN   A CG  1 
ATOM   1504  C  CD  . GLN   A 1 201 ? 81.486 88.09   6.837  1   65.07  ? 223 GLN   A CD  1 
ATOM   1505  O  OE1 . GLN   A 1 201 ? 82.61  87.653  6.575  1   66.9   ? 223 GLN   A OE1 1 
ATOM   1506  N  NE2 . GLN   A 1 201 ? 80.618 88.395  5.882  1   65.02  ? 223 GLN   A NE2 1 
ATOM   1507  N  N   . SER   A 1 202 ? 80.198 84.339  10.554 1   59.85  ? 224 SER   A N   1 
ATOM   1508  C  CA  . SER   A 1 202 ? 80.373 83.219  11.47  1   61.16  ? 224 SER   A CA  1 
ATOM   1509  C  C   . SER   A 1 202 ? 80.107 81.889  10.753 1   62.15  ? 224 SER   A C   1 
ATOM   1510  O  O   . SER   A 1 202 ? 80.823 80.909  10.967 1   61.92  ? 224 SER   A O   1 
ATOM   1511  C  CB  . SER   A 1 202 ? 79.437 83.379  12.664 1   62.73  ? 224 SER   A CB  1 
ATOM   1512  O  OG  . SER   A 1 202 ? 79.551 82.293  13.569 1   64.98  ? 224 SER   A OG  1 
ATOM   1513  N  N   . ALA   A 1 203 ? 79.077 81.861  9.9    1   63.26  ? 225 ALA   A N   1 
ATOM   1514  C  CA  . ALA   A 1 203 ? 78.733 80.672  9.119  1   64.82  ? 225 ALA   A CA  1 
ATOM   1515  C  C   . ALA   A 1 203 ? 79.789 80.385  8.048  1   66.47  ? 225 ALA   A C   1 
ATOM   1516  O  O   . ALA   A 1 203 ? 79.98  79.23   7.686  1   66.97  ? 225 ALA   A O   1 
ATOM   1517  C  CB  . ALA   A 1 203 ? 77.372 80.842  8.466  1   65     ? 225 ALA   A CB  1 
ATOM   1518  N  N   . MET   A 1 204 ? 80.468 81.425  7.536  1   67.15  ? 226 MET   A N   1 
ATOM   1519  C  CA  . MET   A 1 204 ? 81.525 81.259  6.546  1   68.48  ? 226 MET   A CA  1 
ATOM   1520  C  C   . MET   A 1 204 ? 82.74  80.548  7.145  1   69.79  ? 226 MET   A C   1 
ATOM   1521  O  O   . MET   A 1 204 ? 83.406 79.784  6.447  1   70.18  ? 226 MET   A O   1 
ATOM   1522  C  CB  . MET   A 1 204 ? 81.94  82.611  5.936  1   69.36  ? 226 MET   A CB  1 
ATOM   1523  C  CG  . MET   A 1 204 ? 80.905 83.206  4.988  1   72.64  ? 226 MET   A CG  1 
ATOM   1524  S  SD  . MET   A 1 204 ? 80.37  82.084  3.664  1   80.49  ? 226 MET   A SD  1 
ATOM   1525  C  CE  . MET   A 1 204 ? 78.947 82.95   3.053  1   77.9   ? 226 MET   A CE  1 
ATOM   1526  N  N   . GLU   A 1 205 ? 83.016 80.771  8.439  1   70.21  ? 227 GLU   A N   1 
ATOM   1527  C  CA  . GLU   A 1 205 ? 84.135 80.127  9.124  1   71.35  ? 227 GLU   A CA  1 
ATOM   1528  C  C   . GLU   A 1 205 ? 83.817 78.706  9.636  1   72.2   ? 227 GLU   A C   1 
ATOM   1529  O  O   . GLU   A 1 205 ? 84.641 78.12   10.342 1   72.33  ? 227 GLU   A O   1 
ATOM   1530  C  CB  . GLU   A 1 205 ? 84.64  80.998  10.282 1   73.57  ? 227 GLU   A CB  1 
ATOM   1531  C  CG  . GLU   A 1 205 ? 85.095 82.383  9.86   1   78.41  ? 227 GLU   A CG  1 
ATOM   1532  C  CD  . GLU   A 1 205 ? 85.135 83.415  10.974 1   84.9   ? 227 GLU   A CD  1 
ATOM   1533  O  OE1 . GLU   A 1 205 ? 84.704 83.094  12.106 1   86.36  ? 227 GLU   A OE1 1 
ATOM   1534  O  OE2 . GLU   A 1 205 ? 85.58  84.556  10.71  1   86.75  ? 227 GLU   A OE2 1 
ATOM   1535  N  N   . GLU   A 1 206 ? 82.645 78.152  9.292  1   72.5   ? 228 GLU   A N   1 
ATOM   1536  C  CA  . GLU   A 1 206 ? 82.282 76.807  9.721  1   73.34  ? 228 GLU   A CA  1 
ATOM   1537  C  C   . GLU   A 1 206 ? 83.154 75.767  9.002  1   73.36  ? 228 GLU   A C   1 
ATOM   1538  O  O   . GLU   A 1 206 ? 83.267 75.776  7.774  1   73.22  ? 228 GLU   A O   1 
ATOM   1539  C  CB  . GLU   A 1 206 ? 80.792 76.538  9.466  1   76.45  ? 228 GLU   A CB  1 
ATOM   1540  C  CG  . GLU   A 1 206 ? 80.173 75.59   10.476 1   82.1   ? 228 GLU   A CG  1 
ATOM   1541  C  CD  . GLU   A 1 206 ? 79.831 76.249  11.802 1   88.83  ? 228 GLU   A CD  1 
ATOM   1542  O  OE1 . GLU   A 1 206 ? 79.635 77.486  11.828 1   90.31  ? 228 GLU   A OE1 1 
ATOM   1543  O  OE2 . GLU   A 1 206 ? 79.746 75.52   12.816 1   90.81  ? 228 GLU   A OE2 1 
ATOM   1544  N  N   . PRO   A 1 207 ? 83.816 74.886  9.764  1   73.41  ? 229 PRO   A N   1 
ATOM   1545  C  CA  . PRO   A 1 207 ? 84.7   73.896  9.125  1   73.29  ? 229 PRO   A CA  1 
ATOM   1546  C  C   . PRO   A 1 207 ? 83.946 72.848  8.31   1   73.05  ? 229 PRO   A C   1 
ATOM   1547  O  O   . PRO   A 1 207 ? 84.309 72.596  7.161  1   73.35  ? 229 PRO   A O   1 
ATOM   1548  C  CB  . PRO   A 1 207 ? 85.475 73.292  10.303 1   74.05  ? 229 PRO   A CB  1 
ATOM   1549  C  CG  . PRO   A 1 207 ? 84.598 73.521  11.5   1   74.43  ? 229 PRO   A CG  1 
ATOM   1550  C  CD  . PRO   A 1 207 ? 83.8   74.759  11.237 1   72.8   ? 229 PRO   A CD  1 
ATOM   1551  N  N   . VAL   A 1 208 ? 82.889 72.26   8.888  1   72.38  ? 230 VAL   A N   1 
ATOM   1552  C  CA  . VAL   A 1 208 ? 82.098 71.237  8.22   1   72.3   ? 230 VAL   A CA  1 
ATOM   1553  C  C   . VAL   A 1 208 ? 81.225 71.897  7.176  1   72.2   ? 230 VAL   A C   1 
ATOM   1554  O  O   . VAL   A 1 208 ? 80.577 72.895  7.466  1   72.44  ? 230 VAL   A O   1 
ATOM   1555  C  CB  . VAL   A 1 208 ? 81.279 70.408  9.232  1   73.03  ? 230 VAL   A CB  1 
ATOM   1556  C  CG1 . VAL   A 1 208 ? 80.517 69.28   8.542  1   73.56  ? 230 VAL   A CG1 1 
ATOM   1557  C  CG2 . VAL   A 1 208 ? 82.187 69.845  10.313 1   73.5   ? 230 VAL   A CG2 1 
ATOM   1558  N  N   . GLU   A 1 209 ? 81.251 71.379  5.948  1   71.73  ? 231 GLU   A N   1 
ATOM   1559  C  CA  . GLU   A 1 209 ? 80.481 71.951  4.856  1   71.81  ? 231 GLU   A CA  1 
ATOM   1560  C  C   . GLU   A 1 209 ? 78.97  71.826  5.074  1   71.18  ? 231 GLU   A C   1 
ATOM   1561  O  O   . GLU   A 1 209 ? 78.238 72.761  4.742  1   71.29  ? 231 GLU   A O   1 
ATOM   1562  C  CB  . GLU   A 1 209 ? 80.916 71.349  3.503  1   74.52  ? 231 GLU   A CB  1 
ATOM   1563  C  CG  . GLU   A 1 209 ? 80.328 72.034  2.277  1   80.12  ? 231 GLU   A CG  1 
ATOM   1564  C  CD  . GLU   A 1 209 ? 80.828 73.437  1.963  1   87.66  ? 231 GLU   A CD  1 
ATOM   1565  O  OE1 . GLU   A 1 209 ? 81.841 73.865  2.565  1   89.43  ? 231 GLU   A OE1 1 
ATOM   1566  O  OE2 . GLU   A 1 209 ? 80.21  74.104  1.099  1   89.17  ? 231 GLU   A OE2 1 
ATOM   1567  N  N   . LYS   A 1 210 ? 78.502 70.704  5.666  1   69.95  ? 232 LYS   A N   1 
ATOM   1568  C  CA  . LYS   A 1 210 ? 77.07  70.518  5.898  1   69.13  ? 232 LYS   A CA  1 
ATOM   1569  C  C   . LYS   A 1 210 ? 76.492 71.541  6.867  1   67.73  ? 232 LYS   A C   1 
ATOM   1570  O  O   . LYS   A 1 210 ? 75.397 72.06   6.638  1   67.63  ? 232 LYS   A O   1 
ATOM   1571  C  CB  . LYS   A 1 210 ? 76.733 69.091  6.358  1   71.17  ? 232 LYS   A CB  1 
ATOM   1572  C  CG  . LYS   A 1 210 ? 75.286 68.746  6.026  1   75.71  ? 232 LYS   A CG  1 
ATOM   1573  C  CD  . LYS   A 1 210 ? 74.832 67.416  6.584  1   80.68  ? 232 LYS   A CD  1 
ATOM   1574  C  CE  . LYS   A 1 210 ? 74.651 67.484  8.079  1   85.26  ? 232 LYS   A CE  1 
ATOM   1575  N  NZ  . LYS   A 1 210 ? 73.812 68.645  8.499  1   87.75  ? 232 LYS   A NZ  1 
ATOM   1576  N  N   . ALA   A 1 211 ? 77.233 71.829  7.944  1   66.54  ? 233 ALA   A N   1 
ATOM   1577  C  CA  . ALA   A 1 211 ? 76.839 72.792  8.971  1   65.93  ? 233 ALA   A CA  1 
ATOM   1578  C  C   . ALA   A 1 211 ? 76.816 74.226  8.418  1   65.42  ? 233 ALA   A C   1 
ATOM   1579  O  O   . ALA   A 1 211 ? 75.926 75.016  8.741  1   65.46  ? 233 ALA   A O   1 
ATOM   1580  C  CB  . ALA   A 1 211 ? 77.8   72.706  10.147 1   65.8   ? 233 ALA   A CB  1 
ATOM   1581  N  N   . LYS   A 1 212 ? 77.794 74.54   7.564  1   64.66  ? 234 LYS   A N   1 
ATOM   1582  C  CA  . LYS   A 1 212 ? 77.968 75.835  6.917  1   64.04  ? 234 LYS   A CA  1 
ATOM   1583  C  C   . LYS   A 1 212 ? 76.757 76.152  6.045  1   62.75  ? 234 LYS   A C   1 
ATOM   1584  O  O   . LYS   A 1 212 ? 76.212 77.252  6.126  1   62.75  ? 234 LYS   A O   1 
ATOM   1585  C  CB  . LYS   A 1 212 ? 79.261 75.787  6.081  1   65.99  ? 234 LYS   A CB  1 
ATOM   1586  C  CG  . LYS   A 1 212 ? 79.597 77.032  5.293  1   70.32  ? 234 LYS   A CG  1 
ATOM   1587  C  CD  . LYS   A 1 212 ? 80.934 76.807  4.61   1   75     ? 234 LYS   A CD  1 
ATOM   1588  C  CE  . LYS   A 1 212 ? 81.591 78.065  4.134  1   79.33  ? 234 LYS   A CE  1 
ATOM   1589  N  NZ  . LYS   A 1 212 ? 83.064 77.899  4.1    1   82.32  ? 234 LYS   A NZ  1 
ATOM   1590  N  N   . ASN   A 1 213 ? 76.32  75.179  5.238  1   61.58  ? 235 ASN   A N   1 
ATOM   1591  C  CA  . ASN   A 1 213 ? 75.178 75.346  4.345  1   61.09  ? 235 ASN   A CA  1 
ATOM   1592  C  C   . ASN   A 1 213 ? 73.883 75.453  5.115  1   59.67  ? 235 ASN   A C   1 
ATOM   1593  O  O   . ASN   A 1 213 ? 73.001 76.21   4.707  1   59.77  ? 235 ASN   A O   1 
ATOM   1594  C  CB  . ASN   A 1 213 ? 75.085 74.193  3.355  1   62.65  ? 235 ASN   A CB  1 
ATOM   1595  C  CG  . ASN   A 1 213 ? 76.323 74.007  2.532  1   65.64  ? 235 ASN   A CG  1 
ATOM   1596  O  OD1 . ASN   A 1 213 ? 77.109 74.939  2.32   1   66.49  ? 235 ASN   A OD1 1 
ATOM   1597  N  ND2 . ASN   A 1 213 ? 76.521 72.782  2.06   1   66.28  ? 235 ASN   A ND2 1 
ATOM   1598  N  N   . TYR   A 1 214 ? 73.757 74.709  6.231  1   58.2   ? 236 TYR   A N   1 
ATOM   1599  C  CA  . TYR   A 1 214 ? 72.562 74.759  7.061  1   57.28  ? 236 TYR   A CA  1 
ATOM   1600  C  C   . TYR   A 1 214 ? 72.374 76.159  7.62   1   55.21  ? 236 TYR   A C   1 
ATOM   1601  O  O   . TYR   A 1 214 ? 71.28  76.718  7.526  1   55.5   ? 236 TYR   A O   1 
ATOM   1602  C  CB  . TYR   A 1 214 ? 72.613 73.732  8.202  1   58.05  ? 236 TYR   A CB  1 
ATOM   1603  C  CG  . TYR   A 1 214 ? 71.331 73.719  9.013  1   59.97  ? 236 TYR   A CG  1 
ATOM   1604  C  CD1 . TYR   A 1 214 ? 70.193 73.079  8.541  1   61.23  ? 236 TYR   A CD1 1 
ATOM   1605  C  CD2 . TYR   A 1 214 ? 71.246 74.379  10.234 1   61.37  ? 236 TYR   A CD2 1 
ATOM   1606  C  CE1 . TYR   A 1 214 ? 69.012 73.068  9.274  1   62.35  ? 236 TYR   A CE1 1 
ATOM   1607  C  CE2 . TYR   A 1 214 ? 70.062 74.396  10.964 1   62.48  ? 236 TYR   A CE2 1 
ATOM   1608  C  CZ  . TYR   A 1 214 ? 68.947 73.735  10.481 1   63.47  ? 236 TYR   A CZ  1 
ATOM   1609  O  OH  . TYR   A 1 214 ? 67.774 73.721  11.196 1   65.15  ? 236 TYR   A OH  1 
ATOM   1610  N  N   . ARG   A 1 215 ? 73.459 76.74   8.154  1   53.11  ? 237 ARG   A N   1 
ATOM   1611  C  CA  . ARG   A 1 215 ? 73.439 78.084  8.708  1   51.49  ? 237 ARG   A CA  1 
ATOM   1612  C  C   . ARG   A 1 215 ? 73.122 79.123  7.647  1   50.56  ? 237 ARG   A C   1 
ATOM   1613  O  O   . ARG   A 1 215 ? 72.272 79.967  7.886  1   50.95  ? 237 ARG   A O   1 
ATOM   1614  C  CB  . ARG   A 1 215 ? 74.764 78.402  9.387  1   51.83  ? 237 ARG   A CB  1 
ATOM   1615  C  CG  . ARG   A 1 215 ? 75.016 77.572  10.636 1   53.49  ? 237 ARG   A CG  1 
ATOM   1616  C  CD  . ARG   A 1 215 ? 76.209 78.093  11.423 1   55.09  ? 237 ARG   A CD  1 
ATOM   1617  N  NE  . ARG   A 1 215 ? 75.981 79.454  11.917 1   55.96  ? 237 ARG   A NE  1 
ATOM   1618  C  CZ  . ARG   A 1 215 ? 76.871 80.16   12.606 1   57.38  ? 237 ARG   A CZ  1 
ATOM   1619  N  NH1 . ARG   A 1 215 ? 78.063 79.643  12.891 1   56.26  ? 237 ARG   A NH1 1 
ATOM   1620  N  NH2 . ARG   A 1 215 ? 76.576 81.39   13.019 1   57.51  ? 237 ARG   A NH2 1 
ATOM   1621  N  N   . LEU   A 1 216 ? 73.745 79.033  6.459  1   49.26  ? 238 LEU   A N   1 
ATOM   1622  C  CA  . LEU   A 1 216 ? 73.476 79.973  5.377  1   48.43  ? 238 LEU   A CA  1 
ATOM   1623  C  C   . LEU   A 1 216 ? 72.034 79.887  4.86   1   46.68  ? 238 LEU   A C   1 
ATOM   1624  O  O   . LEU   A 1 216 ? 71.437 80.918  4.524  1   46.26  ? 238 LEU   A O   1 
ATOM   1625  C  CB  . LEU   A 1 216 ? 74.483 79.796  4.24   1   49.16  ? 238 LEU   A CB  1 
ATOM   1626  C  CG  . LEU   A 1 216 ? 75.93  80.151  4.591  1   51.27  ? 238 LEU   A CG  1 
ATOM   1627  C  CD1 . LEU   A 1 216 ? 76.85  79.881  3.418  1   51.73  ? 238 LEU   A CD1 1 
ATOM   1628  C  CD2 . LEU   A 1 216 ? 76.062 81.608  5.019  1   52.04  ? 238 LEU   A CD2 1 
ATOM   1629  N  N   . MET   A 1 217 ? 71.467 78.666  4.802  1   45.24  ? 239 MET   A N   1 
ATOM   1630  C  CA  . MET   A 1 217 ? 70.07  78.498  4.39   1   44.26  ? 239 MET   A CA  1 
ATOM   1631  C  C   . MET   A 1 217 ? 69.166 79.134  5.471  1   43.74  ? 239 MET   A C   1 
ATOM   1632  O  O   . MET   A 1 217 ? 68.174 79.78   5.134  1   43.91  ? 239 MET   A O   1 
ATOM   1633  C  CB  . MET   A 1 217 ? 69.735 77      4.169  1   44.37  ? 239 MET   A CB  1 
ATOM   1634  C  CG  . MET   A 1 217 ? 68.228 76.628  4.289  1   45.91  ? 239 MET   A CG  1 
ATOM   1635  S  SD  . MET   A 1 217 ? 67.571 76.415  6.001  1   45.08  ? 239 MET   A SD  1 
ATOM   1636  C  CE  . MET   A 1 217 ? 67.854 74.719  6.268  1   41.02  ? 239 MET   A CE  1 
ATOM   1637  N  N   . ASP   A 1 218 ? 69.516 78.941  6.767  1   42.6   ? 240 ASP   A N   1 
ATOM   1638  C  CA  . ASP   A 1 218 ? 68.771 79.479  7.891  1   42.37  ? 240 ASP   A CA  1 
ATOM   1639  C  C   . ASP   A 1 218 ? 68.789 81.022  7.91   1   41.81  ? 240 ASP   A C   1 
ATOM   1640  O  O   . ASP   A 1 218 ? 67.737 81.63   8.09   1   41.65  ? 240 ASP   A O   1 
ATOM   1641  C  CB  . ASP   A 1 218 ? 69.278 78.876  9.208  1   44.08  ? 240 ASP   A CB  1 
ATOM   1642  C  CG  . ASP   A 1 218 ? 68.515 79.367  10.419 1   48     ? 240 ASP   A CG  1 
ATOM   1643  O  OD1 . ASP   A 1 218 ? 67.305 79.07   10.522 1   48.82  ? 240 ASP   A OD1 1 
ATOM   1644  O  OD2 . ASP   A 1 218 ? 69.128 80.05   11.272 1   49.75  ? 240 ASP   A OD2 1 
ATOM   1645  N  N   . ILE   A 1 219 ? 69.955 81.655  7.671  1   41.1   ? 241 ILE   A N   1 
ATOM   1646  C  CA  . ILE   A 1 219 ? 70.059 83.119  7.574  1   40.88  ? 241 ILE   A CA  1 
ATOM   1647  C  C   . ILE   A 1 219 ? 69.159 83.658  6.432  1   40.62  ? 241 ILE   A C   1 
ATOM   1648  O  O   . ILE   A 1 219 ? 68.572 84.728  6.555  1   40.21  ? 241 ILE   A O   1 
ATOM   1649  C  CB  . ILE   A 1 219 ? 71.535 83.56   7.411  1   41.09  ? 241 ILE   A CB  1 
ATOM   1650  C  CG1 . ILE   A 1 219 ? 72.366 83.138  8.618  1   41.77  ? 241 ILE   A CG1 1 
ATOM   1651  C  CG2 . ILE   A 1 219 ? 71.643 85.062  7.194  1   41.59  ? 241 ILE   A CG2 1 
ATOM   1652  C  CD1 . ILE   A 1 219 ? 73.806 83.067  8.321  1   43.19  ? 241 ILE   A CD1 1 
ATOM   1653  N  N   . GLU   A 1 220 ? 69.001 82.876  5.356  1   40.91  ? 242 GLU   A N   1 
ATOM   1654  C  CA  . GLU   A 1 220 ? 68.132 83.247  4.254  1   41.76  ? 242 GLU   A CA  1 
ATOM   1655  C  C   . GLU   A 1 220 ? 66.643 83.223  4.697  1   42.4   ? 242 GLU   A C   1 
ATOM   1656  O  O   . GLU   A 1 220 ? 65.872 84.11   4.319  1   42.76  ? 242 GLU   A O   1 
ATOM   1657  C  CB  . GLU   A 1 220 ? 68.424 82.363  3.022  1   43.58  ? 242 GLU   A CB  1 
ATOM   1658  C  CG  . GLU   A 1 220 ? 68.039 82.968  1.676  1   49.36  ? 242 GLU   A CG  1 
ATOM   1659  C  CD  . GLU   A 1 220 ? 68.388 84.433  1.448  1   56.98  ? 242 GLU   A CD  1 
ATOM   1660  O  OE1 . GLU   A 1 220 ? 69.588 84.788  1.546  1   55.85  ? 242 GLU   A OE1 1 
ATOM   1661  O  OE2 . GLU   A 1 220 ? 67.455 85.229  1.179  1   60.06  ? 242 GLU   A OE2 1 
ATOM   1662  N  N   . LYS   A 1 221 ? 66.269 82.255  5.561  1   42.26  ? 243 LYS   A N   1 
ATOM   1663  C  CA  . LYS   A 1 221 ? 64.918 82.153  6.121  1   42.47  ? 243 LYS   A CA  1 
ATOM   1664  C  C   . LYS   A 1 221 ? 64.63  83.352  7.034  1   42.55  ? 243 LYS   A C   1 
ATOM   1665  O  O   . LYS   A 1 221 ? 63.51  83.855  7.037  1   42.42  ? 243 LYS   A O   1 
ATOM   1666  C  CB  . LYS   A 1 221 ? 64.741 80.846  6.905  1   43.97  ? 243 LYS   A CB  1 
ATOM   1667  C  CG  . LYS   A 1 221 ? 65.037 79.592  6.096  1   47.44  ? 243 LYS   A CG  1 
ATOM   1668  C  CD  . LYS   A 1 221 ? 63.783 78.901  5.599  1   50.56  ? 243 LYS   A CD  1 
ATOM   1669  C  CE  . LYS   A 1 221 ? 64.112 77.484  5.189  1   52.82  ? 243 LYS   A CE  1 
ATOM   1670  N  NZ  . LYS   A 1 221 ? 62.904 76.694  4.861  1   54.29  ? 243 LYS   A NZ  1 
ATOM   1671  N  N   . ARG   A 1 222 ? 65.65  83.823  7.784  1   42.93  ? 244 ARG   A N   1 
ATOM   1672  C  CA  . ARG   A 1 222 ? 65.568 84.991  8.658  1   43.89  ? 244 ARG   A CA  1 
ATOM   1673  C  C   . ARG   A 1 222 ? 65.34  86.234  7.826  1   45.09  ? 244 ARG   A C   1 
ATOM   1674  O  O   . ARG   A 1 222 ? 64.456 87.021  8.159  1   45.59  ? 244 ARG   A O   1 
ATOM   1675  C  CB  . ARG   A 1 222 ? 66.84  85.158  9.512  1   45.21  ? 244 ARG   A CB  1 
ATOM   1676  C  CG  . ARG   A 1 222 ? 67.149 83.991  10.441 1   47.57  ? 244 ARG   A CG  1 
ATOM   1677  C  CD  . ARG   A 1 222 ? 65.993 83.65   11.391 1   50     ? 244 ARG   A CD  1 
ATOM   1678  N  NE  . ARG   A 1 222 ? 65.716 84.734  12.334 1   50.19  ? 244 ARG   A NE  1 
ATOM   1679  C  CZ  . ARG   A 1 222 ? 64.518 85.004  12.841 1   48.79  ? 244 ARG   A CZ  1 
ATOM   1680  N  NH1 . ARG   A 1 222 ? 63.467 84.27   12.507 1   45.78  ? 244 ARG   A NH1 1 
ATOM   1681  N  NH2 . ARG   A 1 222 ? 64.362 86.016  13.68  1   49.01  ? 244 ARG   A NH2 1 
ATOM   1682  N  N   . ARG   A 1 223 ? 66.079 86.388  6.697  1   45.33  ? 245 ARG   A N   1 
ATOM   1683  C  CA  . ARG   A 1 223 ? 65.921 87.518  5.775  1   45.7   ? 245 ARG   A CA  1 
ATOM   1684  C  C   . ARG   A 1 223 ? 64.474 87.642  5.3    1   45.66  ? 245 ARG   A C   1 
ATOM   1685  O  O   . ARG   A 1 223 ? 63.947 88.756  5.214  1   45.86  ? 245 ARG   A O   1 
ATOM   1686  C  CB  . ARG   A 1 223 ? 66.885 87.385  4.576  1   47.31  ? 245 ARG   A CB  1 
ATOM   1687  C  CG  . ARG   A 1 223 ? 68.342 87.632  4.95   1   50     ? 245 ARG   A CG  1 
ATOM   1688  C  CD  . ARG   A 1 223 ? 69.228 87.965  3.762  1   51.93  ? 245 ARG   A CD  1 
ATOM   1689  N  NE  . ARG   A 1 223 ? 70.639 87.705  4.066  1   54.47  ? 245 ARG   A NE  1 
ATOM   1690  C  CZ  . ARG   A 1 223 ? 71.446 88.561  4.69   1   57.23  ? 245 ARG   A CZ  1 
ATOM   1691  N  NH1 . ARG   A 1 223 ? 71     89.754  5.065  1   56.54  ? 245 ARG   A NH1 1 
ATOM   1692  N  NH2 . ARG   A 1 223 ? 72.707 88.23   4.944  1   57.68  ? 245 ARG   A NH2 1 
ATOM   1693  N  N   . GLU   A 1 224 ? 63.829 86.49   5.022  1   45.34  ? 246 GLU   A N   1 
ATOM   1694  C  CA  . GLU   A 1 224 ? 62.429 86.423  4.601  1   45.33  ? 246 GLU   A CA  1 
ATOM   1695  C  C   . GLU   A 1 224 ? 61.453 86.813  5.709  1   44.8   ? 246 GLU   A C   1 
ATOM   1696  O  O   . GLU   A 1 224 ? 60.419 87.424  5.432  1   44.73  ? 246 GLU   A O   1 
ATOM   1697  C  CB  . GLU   A 1 224 ? 62.088 85.036  4.073  1   48.07  ? 246 GLU   A CB  1 
ATOM   1698  C  CG  . GLU   A 1 224 ? 62.157 84.938  2.559  1   54.78  ? 246 GLU   A CG  1 
ATOM   1699  C  CD  . GLU   A 1 224 ? 61.517 86.067  1.773  1   61.73  ? 246 GLU   A CD  1 
ATOM   1700  O  OE1 . GLU   A 1 224 ? 60.266 86.15   1.741  1   62.34  ? 246 GLU   A OE1 1 
ATOM   1701  O  OE2 . GLU   A 1 224 ? 62.281 86.888  1.212  1   64.18  ? 246 GLU   A OE2 1 
ATOM   1702  N  N   . VAL   A 1 225 ? 61.781 86.461  6.963  1   44.21  ? 247 VAL   A N   1 
ATOM   1703  C  CA  . VAL   A 1 225 ? 60.989 86.812  8.139  1   44.17  ? 247 VAL   A CA  1 
ATOM   1704  C  C   . VAL   A 1 225 ? 60.988 88.339  8.289  1   44.82  ? 247 VAL   A C   1 
ATOM   1705  O  O   . VAL   A 1 225 ? 59.927 88.949  8.428  1   45.24  ? 247 VAL   A O   1 
ATOM   1706  C  CB  . VAL   A 1 225 ? 61.528 86.104  9.421  1   44.42  ? 247 VAL   A CB  1 
ATOM   1707  C  CG1 . VAL   A 1 225 ? 61.046 86.788  10.709 1   45.38  ? 247 VAL   A CG1 1 
ATOM   1708  C  CG2 . VAL   A 1 225 ? 61.16  84.636  9.432  1   44.42  ? 247 VAL   A CG2 1 
ATOM   1709  N  N   . TYR   A 1 226 ? 62.178 88.951  8.246  1   44.84  ? 248 TYR   A N   1 
ATOM   1710  C  CA  . TYR   A 1 226 ? 62.298 90.389  8.407  1   45.41  ? 248 TYR   A CA  1 
ATOM   1711  C  C   . TYR   A 1 226 ? 61.71  91.157  7.238  1   45.96  ? 248 TYR   A C   1 
ATOM   1712  O  O   . TYR   A 1 226 ? 61.25  92.276  7.43   1   46.13  ? 248 TYR   A O   1 
ATOM   1713  C  CB  . TYR   A 1 226 ? 63.736 90.798  8.724  1   45.18  ? 248 TYR   A CB  1 
ATOM   1714  C  CG  . TYR   A 1 226 ? 64.141 90.288  10.089 1   46.2   ? 248 TYR   A CG  1 
ATOM   1715  C  CD1 . TYR   A 1 226 ? 63.472 90.701  11.237 1   47.16  ? 248 TYR   A CD1 1 
ATOM   1716  C  CD2 . TYR   A 1 226 ? 65.139 89.336  10.228 1   47.28  ? 248 TYR   A CD2 1 
ATOM   1717  C  CE1 . TYR   A 1 226 ? 63.809 90.203  12.492 1   48.07  ? 248 TYR   A CE1 1 
ATOM   1718  C  CE2 . TYR   A 1 226 ? 65.479 88.822  11.478 1   48.27  ? 248 TYR   A CE2 1 
ATOM   1719  C  CZ  . TYR   A 1 226 ? 64.813 89.261  12.609 1   48.83  ? 248 TYR   A CZ  1 
ATOM   1720  O  OH  . TYR   A 1 226 ? 65.155 88.765  13.844 1   49.94  ? 248 TYR   A OH  1 
ATOM   1721  N  N   . ARG   A 1 227 ? 61.638 90.542  6.061  1   45.95  ? 249 ARG   A N   1 
ATOM   1722  C  CA  . ARG   A 1 227 ? 61.028 91.164  4.9    1   46.8   ? 249 ARG   A CA  1 
ATOM   1723  C  C   . ARG   A 1 227 ? 59.513 91.369  5.166  1   47.18  ? 249 ARG   A C   1 
ATOM   1724  O  O   . ARG   A 1 227 ? 58.968 92.423  4.842  1   47.19  ? 249 ARG   A O   1 
ATOM   1725  C  CB  . ARG   A 1 227 ? 61.253 90.277  3.675  1   48.38  ? 249 ARG   A CB  1 
ATOM   1726  C  CG  . ARG   A 1 227 ? 61.405 91.064  2.403  1   52.43  ? 249 ARG   A CG  1 
ATOM   1727  C  CD  . ARG   A 1 227 ? 61.59  90.16   1.213  1   56.93  ? 249 ARG   A CD  1 
ATOM   1728  N  NE  . ARG   A 1 227 ? 60.387 89.364  0.962  1   61.62  ? 249 ARG   A NE  1 
ATOM   1729  C  CZ  . ARG   A 1 227 ? 59.374 89.757  0.196  1   64.25  ? 249 ARG   A CZ  1 
ATOM   1730  N  NH1 . ARG   A 1 227 ? 59.404 90.945  -0.402 1   63.92  ? 249 ARG   A NH1 1 
ATOM   1731  N  NH2 . ARG   A 1 227 ? 58.32  88.969  0.028  1   64.23  ? 249 ARG   A NH2 1 
ATOM   1732  N  N   . SER   A 1 228 ? 58.865 90.389  5.819  1   47.18  ? 250 SER   A N   1 
ATOM   1733  C  CA  . SER   A 1 228 ? 57.442 90.445  6.164  1   47.6   ? 250 SER   A CA  1 
ATOM   1734  C  C   . SER   A 1 228 ? 57.078 91.56   7.155  1   47.08  ? 250 SER   A C   1 
ATOM   1735  O  O   . SER   A 1 228 ? 55.89  91.881  7.286  1   47.11  ? 250 SER   A O   1 
ATOM   1736  C  CB  . SER   A 1 228 ? 56.95  89.094  6.686  1   49.22  ? 250 SER   A CB  1 
ATOM   1737  O  OG  . SER   A 1 228 ? 57.491 88.795  7.964  1   52.07  ? 250 SER   A OG  1 
ATOM   1738  N  N   . ILE   A 1 229 ? 58.082 92.141  7.86   1   46.14  ? 251 ILE   A N   1 
ATOM   1739  C  CA  . ILE   A 1 229 ? 57.812 93.226  8.805  1   45.71  ? 251 ILE   A CA  1 
ATOM   1740  C  C   . ILE   A 1 229 ? 58.429 94.557  8.369  1   46.7   ? 251 ILE   A C   1 
ATOM   1741  O  O   . ILE   A 1 229 ? 57.875 95.612  8.662  1   46.39  ? 251 ILE   A O   1 
ATOM   1742  C  CB  . ILE   A 1 229 ? 58.175 92.877  10.258 1   44.95  ? 251 ILE   A CB  1 
ATOM   1743  C  CG1 . ILE   A 1 229 ? 59.634 92.433  10.415 1   44.74  ? 251 ILE   A CG1 1 
ATOM   1744  C  CG2 . ILE   A 1 229 ? 57.216 91.842  10.787 1   45.63  ? 251 ILE   A CG2 1 
ATOM   1745  C  CD1 . ILE   A 1 229 ? 60.129 92.482  11.815 1   44.73  ? 251 ILE   A CD1 1 
ATOM   1746  N  N   . PHE   A 1 230 ? 59.553 94.515  7.656  1   47.71  ? 252 PHE   A N   1 
ATOM   1747  C  CA  . PHE   A 1 230 ? 60.227 95.734  7.212  1   49.12  ? 252 PHE   A CA  1 
ATOM   1748  C  C   . PHE   A 1 230 ? 59.726 96.265  5.837  1   51.04  ? 252 PHE   A C   1 
ATOM   1749  O  O   . PHE   A 1 230 ? 60.1   97.368  5.421  1   50.93  ? 252 PHE   A O   1 
ATOM   1750  C  CB  . PHE   A 1 230 ? 61.745 95.535  7.247  1   48.72  ? 252 PHE   A CB  1 
ATOM   1751  C  CG  . PHE   A 1 230 ? 62.296 95.234  8.63   1   49.08  ? 252 PHE   A CG  1 
ATOM   1752  C  CD1 . PHE   A 1 230 ? 61.691 95.748  9.765  1   49.51  ? 252 PHE   A CD1 1 
ATOM   1753  C  CD2 . PHE   A 1 230 ? 63.434 94.456  8.789  1   49.76  ? 252 PHE   A CD2 1 
ATOM   1754  C  CE1 . PHE   A 1 230 ? 62.208 95.488  11.022 1   50.06  ? 252 PHE   A CE1 1 
ATOM   1755  C  CE2 . PHE   A 1 230 ? 63.958 94.214  10.053 1   50.31  ? 252 PHE   A CE2 1 
ATOM   1756  C  CZ  . PHE   A 1 230 ? 63.339 94.728  11.161 1   49.93  ? 252 PHE   A CZ  1 
ATOM   1757  N  N   . ASP   A 1 231 ? 58.851 95.495  5.161  1   52.35  ? 253 ASP   A N   1 
ATOM   1758  C  CA  . ASP   A 1 231 ? 58.217 95.886  3.908  1   54.17  ? 253 ASP   A CA  1 
ATOM   1759  C  C   . ASP   A 1 231 ? 56.74  95.988  4.227  1   55.51  ? 253 ASP   A C   1 
ATOM   1760  O  O   . ASP   A 1 231 ? 56.09  94.964  4.461  1   55.91  ? 253 ASP   A O   1 
ATOM   1761  C  CB  . ASP   A 1 231 ? 58.441 94.825  2.821  1   56.49  ? 253 ASP   A CB  1 
ATOM   1762  C  CG  . ASP   A 1 231 ? 58.039 95.256  1.418  1   61.86  ? 253 ASP   A CG  1 
ATOM   1763  O  OD1 . ASP   A 1 231 ? 57.279 96.254  1.29   1   61.98  ? 253 ASP   A OD1 1 
ATOM   1764  O  OD2 . ASP   A 1 231 ? 58.484 94.594  0.441  1   64.6   ? 253 ASP   A OD2 1 
ATOM   1765  N  N   . PRO   A 1 232 ? 56.198 97.219  4.262  1   55.89  ? 254 PRO   A N   1 
ATOM   1766  C  CA  . PRO   A 1 232 ? 54.782 97.384  4.604  1   56.49  ? 254 PRO   A CA  1 
ATOM   1767  C  C   . PRO   A 1 232 ? 53.834 96.718  3.617  1   57.63  ? 254 PRO   A C   1 
ATOM   1768  O  O   . PRO   A 1 232 ? 52.768 96.282  4.031  1   58.3   ? 254 PRO   A O   1 
ATOM   1769  C  CB  . PRO   A 1 232 ? 54.598 98.903  4.635  1   56.88  ? 254 PRO   A CB  1 
ATOM   1770  C  CG  . PRO   A 1 232 ? 55.963 99.461  4.755  1   57.03  ? 254 PRO   A CG  1 
ATOM   1771  C  CD  . PRO   A 1 232 ? 56.847 98.518  4.024  1   55.38  ? 254 PRO   A CD  1 
ATOM   1772  N  N   . ALA   A 1 233 ? 54.229 96.598  2.339  1   57.63  ? 255 ALA   A N   1 
ATOM   1773  C  CA  . ALA   A 1 233 ? 53.411 95.958  1.315  1   58.07  ? 255 ALA   A CA  1 
ATOM   1774  C  C   . ALA   A 1 233 ? 53.239 94.465  1.604  1   58.72  ? 255 ALA   A C   1 
ATOM   1775  O  O   . ALA   A 1 233 ? 52.141 93.935  1.42   1   59.01  ? 255 ALA   A O   1 
ATOM   1776  C  CB  . ALA   A 1 233 ? 54.034 96.167  -0.053 1   57.91  ? 255 ALA   A CB  1 
ATOM   1777  N  N   . VAL   A 1 234 ? 54.308 93.801  2.091  1   58.73  ? 256 VAL   A N   1 
ATOM   1778  C  CA  . VAL   A 1 234 ? 54.257 92.378  2.456  1   59.33  ? 256 VAL   A CA  1 
ATOM   1779  C  C   . VAL   A 1 234 ? 53.354 92.175  3.688  1   60.22  ? 256 VAL   A C   1 
ATOM   1780  O  O   . VAL   A 1 234 ? 52.592 91.209  3.748  1   60.53  ? 256 VAL   A O   1 
ATOM   1781  C  CB  . VAL   A 1 234 ? 55.672 91.769  2.66   1   59.34  ? 256 VAL   A CB  1 
ATOM   1782  C  CG1 . VAL   A 1 234 ? 55.588 90.292  3.005  1   59.43  ? 256 VAL   A CG1 1 
ATOM   1783  C  CG2 . VAL   A 1 234 ? 56.52  91.964  1.419  1   59.76  ? 256 VAL   A CG2 1 
ATOM   1784  N  N   . HIS   A 1 235 ? 53.417 93.112  4.646  1   60.45  ? 257 HIS   A N   1 
ATOM   1785  C  CA  . HIS   A 1 235 ? 52.576 93.07   5.829  1   61.2   ? 257 HIS   A CA  1 
ATOM   1786  C  C   . HIS   A 1 235 ? 51.105 93.242  5.427  1   61.62  ? 257 HIS   A C   1 
ATOM   1787  O  O   . HIS   A 1 235 ? 50.277 92.423  5.817  1   61.96  ? 257 HIS   A O   1 
ATOM   1788  C  CB  . HIS   A 1 235 ? 52.999 94.148  6.853  1   62.34  ? 257 HIS   A CB  1 
ATOM   1789  C  CG  . HIS   A 1 235 ? 52.036 94.301  7.998  1   65.03  ? 257 HIS   A CG  1 
ATOM   1790  N  ND1 . HIS   A 1 235 ? 52.009 93.394  9.049  1   66.88  ? 257 HIS   A ND1 1 
ATOM   1791  C  CD2 . HIS   A 1 235 ? 51.063 95.222  8.193  1   66.08  ? 257 HIS   A CD2 1 
ATOM   1792  C  CE1 . HIS   A 1 235 ? 51.031 93.795  9.845  1   67.25  ? 257 HIS   A CE1 1 
ATOM   1793  N  NE2 . HIS   A 1 235 ? 50.435 94.893  9.373  1   67.2   ? 257 HIS   A NE2 1 
ATOM   1794  N  N   . ASP   A 1 236 ? 50.789 94.277  4.627  1   61.51  ? 258 ASP   A N   1 
ATOM   1795  C  CA  . ASP   A 1 236 ? 49.426 94.567  4.173  1   61.93  ? 258 ASP   A CA  1 
ATOM   1796  C  C   . ASP   A 1 236 ? 48.79  93.389  3.447  1   61.73  ? 258 ASP   A C   1 
ATOM   1797  O  O   . ASP   A 1 236 ? 47.583 93.176  3.568  1   61.89  ? 258 ASP   A O   1 
ATOM   1798  C  CB  . ASP   A 1 236 ? 49.408 95.799  3.261  1   64.22  ? 258 ASP   A CB  1 
ATOM   1799  C  CG  . ASP   A 1 236 ? 49.781 97.102  3.94   1   70.38  ? 258 ASP   A CG  1 
ATOM   1800  O  OD1 . ASP   A 1 236 ? 49.825 97.133  5.204  1   71.03  ? 258 ASP   A OD1 1 
ATOM   1801  O  OD2 . ASP   A 1 236 ? 50.042 98.091  3.216  1   73.09  ? 258 ASP   A OD2 1 
ATOM   1802  N  N   . ALA   A 1 237 ? 49.604 92.618  2.708  1   61.15  ? 259 ALA   A N   1 
ATOM   1803  C  CA  . ALA   A 1 237 ? 49.137 91.443  1.983  1   61.03  ? 259 ALA   A CA  1 
ATOM   1804  C  C   . ALA   A 1 237 ? 48.686 90.345  2.951  1   60.68  ? 259 ALA   A C   1 
ATOM   1805  O  O   . ALA   A 1 237 ? 47.657 89.706  2.727  1   60.51  ? 259 ALA   A O   1 
ATOM   1806  C  CB  . ALA   A 1 237 ? 50.238 90.931  1.072  1   61.21  ? 259 ALA   A CB  1 
ATOM   1807  N  N   . LEU   A 1 238 ? 49.439 90.16   4.04   1   60.69  ? 260 LEU   A N   1 
ATOM   1808  C  CA  . LEU   A 1 238 ? 49.139 89.177  5.078  1   61.39  ? 260 LEU   A CA  1 
ATOM   1809  C  C   . LEU   A 1 238 ? 47.916 89.57   5.899  1   62.93  ? 260 LEU   A C   1 
ATOM   1810  O  O   . LEU   A 1 238 ? 47.206 88.688  6.377  1   63.02  ? 260 LEU   A O   1 
ATOM   1811  C  CB  . LEU   A 1 238 ? 50.347 88.996  5.998  1   60.96  ? 260 LEU   A CB  1 
ATOM   1812  C  CG  . LEU   A 1 238 ? 51.502 88.246  5.381  1   61.3   ? 260 LEU   A CG  1 
ATOM   1813  C  CD1 . LEU   A 1 238 ? 52.8   88.546  6.11   1   61.18  ? 260 LEU   A CD1 1 
ATOM   1814  C  CD2 . LEU   A 1 238 ? 51.187 86.756  5.273  1   61.82  ? 260 LEU   A CD2 1 
ATOM   1815  N  N   . VAL   A 1 239 ? 47.67  90.885  6.071  1   64.12  ? 261 VAL   A N   1 
ATOM   1816  C  CA  . VAL   A 1 239 ? 46.504 91.388  6.804  1   65.71  ? 261 VAL   A CA  1 
ATOM   1817  C  C   . VAL   A 1 239 ? 45.244 91.099  6      1   67.57  ? 261 VAL   A C   1 
ATOM   1818  O  O   . VAL   A 1 239 ? 44.266 90.587  6.548  1   67.81  ? 261 VAL   A O   1 
ATOM   1819  C  CB  . VAL   A 1 239 ? 46.63  92.891  7.158  1   66.27  ? 261 VAL   A CB  1 
ATOM   1820  C  CG1 . VAL   A 1 239 ? 45.322 93.434  7.72   1   66.87  ? 261 VAL   A CG1 1 
ATOM   1821  C  CG2 . VAL   A 1 239 ? 47.765 93.125  8.142  1   66.51  ? 261 VAL   A CG2 1 
ATOM   1822  N  N   . ARG   A 1 240 ? 45.291 91.369  4.687  1   68.81  ? 262 ARG   A N   1 
ATOM   1823  C  CA  . ARG   A 1 240 ? 44.181 91.102  3.771  1   70.47  ? 262 ARG   A CA  1 
ATOM   1824  C  C   . ARG   A 1 240 ? 43.933 89.599  3.62   1   71.01  ? 262 ARG   A C   1 
ATOM   1825  O  O   . ARG   A 1 240 ? 42.785 89.174  3.517  1   71.3   ? 262 ARG   A O   1 
ATOM   1826  C  CB  . ARG   A 1 240 ? 44.448 91.738  2.406  1   72.86  ? 262 ARG   A CB  1 
ATOM   1827  C  CG  . ARG   A 1 240 ? 44.331 93.256  2.423  1   77.91  ? 262 ARG   A CG  1 
ATOM   1828  C  CD  . ARG   A 1 240 ? 44.457 93.833  1.028  1   83.44  ? 262 ARG   A CD  1 
ATOM   1829  N  NE  . ARG   A 1 240 ? 45.835 94.209  0.707  1   88.67  ? 262 ARG   A NE  1 
ATOM   1830  C  CZ  . ARG   A 1 240 ? 46.667 93.476  -0.032 1   92.14  ? 262 ARG   A CZ  1 
ATOM   1831  N  NH1 . ARG   A 1 240 ? 46.268 92.311  -0.537 1   91.77  ? 262 ARG   A NH1 1 
ATOM   1832  N  NH2 . ARG   A 1 240 ? 47.898 93.907  -0.281 1   92.68  ? 262 ARG   A NH2 1 
ATOM   1833  N  N   . ARG   A 1 241 ? 45.01  88.801  3.631  1   70.88  ? 263 ARG   A N   1 
ATOM   1834  C  CA  . ARG   A 1 241 ? 44.962 87.342  3.566  1   71.33  ? 263 ARG   A CA  1 
ATOM   1835  C  C   . ARG   A 1 241 ? 44.346 86.719  4.858  1   70.19  ? 263 ARG   A C   1 
ATOM   1836  O  O   . ARG   A 1 241 ? 43.778 85.624  4.82   1   70.4   ? 263 ARG   A O   1 
ATOM   1837  C  CB  . ARG   A 1 241 ? 46.381 86.808  3.316  1   74.31  ? 263 ARG   A CB  1 
ATOM   1838  C  CG  . ARG   A 1 241 ? 46.51  85.296  3.329  1   80.02  ? 263 ARG   A CG  1 
ATOM   1839  C  CD  . ARG   A 1 241 ? 47.952 84.889  3.52   1   85.37  ? 263 ARG   A CD  1 
ATOM   1840  N  NE  . ARG   A 1 241 ? 48.543 84.397  2.278  1   89.98  ? 263 ARG   A NE  1 
ATOM   1841  C  CZ  . ARG   A 1 241 ? 49.774 83.9    2.177  1   93.26  ? 263 ARG   A CZ  1 
ATOM   1842  N  NH1 . ARG   A 1 241 ? 50.562 83.832  3.247  1   92.65  ? 263 ARG   A NH1 1 
ATOM   1843  N  NH2 . ARG   A 1 241 ? 50.228 83.471  1.005  1   93.8   ? 263 ARG   A NH2 1 
ATOM   1844  N  N   . GLY   A 1 242 ? 44.441 87.431  5.978  1   68.74  ? 264 GLY   A N   1 
ATOM   1845  C  CA  . GLY   A 1 242 ? 43.896 86.959  7.245  1   67.63  ? 264 GLY   A CA  1 
ATOM   1846  C  C   . GLY   A 1 242 ? 44.923 86.41   8.217  1   66.17  ? 264 GLY   A C   1 
ATOM   1847  O  O   . GLY   A 1 242 ? 44.571 86.032  9.336  1   66.04  ? 264 GLY   A O   1 
ATOM   1848  N  N   . ASP   A 1 243 ? 46.198 86.339  7.8    1   64.8   ? 265 ASP   A N   1 
ATOM   1849  C  CA  . ASP   A 1 243 ? 47.294 85.86   8.645  1   64.08  ? 265 ASP   A CA  1 
ATOM   1850  C  C   . ASP   A 1 243 ? 47.651 86.856  9.762  1   62.43  ? 265 ASP   A C   1 
ATOM   1851  O  O   . ASP   A 1 243 ? 48.188 86.466  10.81  1   62.62  ? 265 ASP   A O   1 
ATOM   1852  C  CB  . ASP   A 1 243 ? 48.527 85.538  7.792  1   66.69  ? 265 ASP   A CB  1 
ATOM   1853  C  CG  . ASP   A 1 243 ? 48.375 84.301  6.931  1   73.52  ? 265 ASP   A CG  1 
ATOM   1854  O  OD1 . ASP   A 1 243 ? 47.217 83.856  6.718  1   74.49  ? 265 ASP   A OD1 1 
ATOM   1855  O  OD2 . ASP   A 1 243 ? 49.407 83.783  6.458  1   77.12  ? 265 ASP   A OD2 1 
ATOM   1856  N  N   . ARG   A 1 244 ? 47.36  88.14   9.53   1   60.45  ? 266 ARG   A N   1 
ATOM   1857  C  CA  . ARG   A 1 244 ? 47.571 89.216  10.482 1   59.04  ? 266 ARG   A CA  1 
ATOM   1858  C  C   . ARG   A 1 244 ? 46.307 90.085  10.592 1   58.52  ? 266 ARG   A C   1 
ATOM   1859  O  O   . ARG   A 1 244 ? 45.482 90.13   9.681  1   58.72  ? 266 ARG   A O   1 
ATOM   1860  C  CB  . ARG   A 1 244 ? 48.794 90.053  10.089 1   58.57  ? 266 ARG   A CB  1 
ATOM   1861  C  CG  . ARG   A 1 244 ? 50.096 89.306  10.296 1   58.27  ? 266 ARG   A CG  1 
ATOM   1862  C  CD  . ARG   A 1 244 ? 51.295 90.139  9.947  1   58.75  ? 266 ARG   A CD  1 
ATOM   1863  N  NE  . ARG   A 1 244 ? 52.502 89.317  9.89   1   59.05  ? 266 ARG   A NE  1 
ATOM   1864  C  CZ  . ARG   A 1 244 ? 53.691 89.753  9.483  1   59.29  ? 266 ARG   A CZ  1 
ATOM   1865  N  NH1 . ARG   A 1 244 ? 53.846 91.014  9.094  1   58.63  ? 266 ARG   A NH1 1 
ATOM   1866  N  NH2 . ARG   A 1 244 ? 54.733 88.931  9.464  1   57.85  ? 266 ARG   A NH2 1 
ATOM   1867  N  N   . ARG   A 1 245 ? 46.139 90.74   11.726 1   57.76  ? 267 ARG   A N   1 
ATOM   1868  C  CA  . ARG   A 1 245 ? 45.004 91.62   11.99  1   57.61  ? 267 ARG   A CA  1 
ATOM   1869  C  C   . ARG   A 1 245 ? 45.483 93.047  12.238 1   56.08  ? 267 ARG   A C   1 
ATOM   1870  O  O   . ARG   A 1 245 ? 44.844 94.011  11.809 1   56.14  ? 267 ARG   A O   1 
ATOM   1871  C  CB  . ARG   A 1 245 ? 44.228 91.129  13.23  1   60.18  ? 267 ARG   A CB  1 
ATOM   1872  C  CG  . ARG   A 1 245 ? 43.191 90.055  12.937 1   64.97  ? 267 ARG   A CG  1 
ATOM   1873  C  CD  . ARG   A 1 245 ? 43.32  88.914  13.917 1   69.25  ? 267 ARG   A CD  1 
ATOM   1874  N  NE  . ARG   A 1 245 ? 42.125 88.075  13.943 1   73.35  ? 267 ARG   A NE  1 
ATOM   1875  C  CZ  . ARG   A 1 245 ? 41.938 87.008  13.174 1   76.64  ? 267 ARG   A CZ  1 
ATOM   1876  N  NH1 . ARG   A 1 245 ? 42.87  86.632  12.308 1   75.82  ? 267 ARG   A NH1 1 
ATOM   1877  N  NH2 . ARG   A 1 245 ? 40.825 86.299  13.276 1   77.86  ? 267 ARG   A NH2 1 
ATOM   1878  N  N   . PHE   A 1 246 ? 46.6   93.169  12.961 1   54.71  ? 268 PHE   A N   1 
ATOM   1879  C  CA  . PHE   A 1 246 ? 47.209 94.415  13.386 1   53.86  ? 268 PHE   A CA  1 
ATOM   1880  C  C   . PHE   A 1 246 ? 47.635 95.299  12.249 1   53.05  ? 268 PHE   A C   1 
ATOM   1881  O  O   . PHE   A 1 246 ? 48.091 94.818  11.214 1   53.3   ? 268 PHE   A O   1 
ATOM   1882  C  CB  . PHE   A 1 246 ? 48.453 94.121  14.229 1   53.31  ? 268 PHE   A CB  1 
ATOM   1883  C  CG  . PHE   A 1 246 ? 48.203 93.77   15.673 1   53.32  ? 268 PHE   A CG  1 
ATOM   1884  C  CD1 . PHE   A 1 246 ? 47.045 93.115  16.054 1   53.73  ? 268 PHE   A CD1 1 
ATOM   1885  C  CD2 . PHE   A 1 246 ? 49.157 94.031  16.637 1   53.52  ? 268 PHE   A CD2 1 
ATOM   1886  C  CE1 . PHE   A 1 246 ? 46.839 92.753  17.374 1   54.11  ? 268 PHE   A CE1 1 
ATOM   1887  C  CE2 . PHE   A 1 246 ? 48.951 93.658  17.953 1   54     ? 268 PHE   A CE2 1 
ATOM   1888  C  CZ  . PHE   A 1 246 ? 47.792 93.03   18.316 1   53.77  ? 268 PHE   A CZ  1 
ATOM   1889  N  N   . SER   A 1 247 ? 47.556 96.605  12.469 1   51.94  ? 269 SER   A N   1 
ATOM   1890  C  CA  . SER   A 1 247 ? 48.07  97.566  11.514 1   51.17  ? 269 SER   A CA  1 
ATOM   1891  C  C   . SER   A 1 247 ? 49.613 97.484  11.597 1   50.51  ? 269 SER   A C   1 
ATOM   1892  O  O   . SER   A 1 247 ? 50.154 97.022  12.607 1   50.66  ? 269 SER   A O   1 
ATOM   1893  C  CB  . SER   A 1 247 ? 47.62  98.964  11.905 1   52.03  ? 269 SER   A CB  1 
ATOM   1894  O  OG  . SER   A 1 247 ? 48.246 99.377  13.109 1   54.27  ? 269 SER   A OG  1 
ATOM   1895  N  N   . HIS   A 1 248 ? 50.321 97.959  10.57  1   49.59  ? 270 HIS   A N   1 
ATOM   1896  C  CA  . HIS   A 1 248 ? 51.783 97.948  10.572 1   48.98  ? 270 HIS   A CA  1 
ATOM   1897  C  C   . HIS   A 1 248 ? 52.377 98.647  11.841 1   47.9   ? 270 HIS   A C   1 
ATOM   1898  O  O   . HIS   A 1 248 ? 53.18  98.051  12.558 1   47.5   ? 270 HIS   A O   1 
ATOM   1899  C  CB  . HIS   A 1 248 ? 52.312 98.573  9.273  1   49.65  ? 270 HIS   A CB  1 
ATOM   1900  C  CG  . HIS   A 1 248 ? 53.764 98.326  9.05   1   52.3   ? 270 HIS   A CG  1 
ATOM   1901  N  ND1 . HIS   A 1 248 ? 54.265 97.044  8.93   1   54.41  ? 270 HIS   A ND1 1 
ATOM   1902  C  CD2 . HIS   A 1 248 ? 54.783 99.204  8.921  1   53.56  ? 270 HIS   A CD2 1 
ATOM   1903  C  CE1 . HIS   A 1 248 ? 55.568 97.179  8.757  1   54.69  ? 270 HIS   A CE1 1 
ATOM   1904  N  NE2 . HIS   A 1 248 ? 55.928 98.458  8.739  1   54.63  ? 270 HIS   A NE2 1 
ATOM   1905  N  N   . ARG   A 1 249 ? 51.887 99.852  12.169 1   47.03  ? 271 ARG   A N   1 
ATOM   1906  C  CA  . ARG   A 1 249 ? 52.358 100.585 13.339 1   46.37  ? 271 ARG   A CA  1 
ATOM   1907  C  C   . ARG   A 1 249 ? 51.985 99.938  14.679 1   45.72  ? 271 ARG   A C   1 
ATOM   1908  O  O   . ARG   A 1 249 ? 52.747 100.074 15.635 1   46.4   ? 271 ARG   A O   1 
ATOM   1909  C  CB  . ARG   A 1 249 ? 51.908 102.039 13.295 1   47.27  ? 271 ARG   A CB  1 
ATOM   1910  C  CG  . ARG   A 1 249 ? 52.704 102.92  14.234 1   50.14  ? 271 ARG   A CG  1 
ATOM   1911  C  CD  . ARG   A 1 249 ? 52.541 104.377 13.877 1   52.98  ? 271 ARG   A CD  1 
ATOM   1912  N  NE  . ARG   A 1 249 ? 53.146 105.255 14.875 1   54.81  ? 271 ARG   A NE  1 
ATOM   1913  C  CZ  . ARG   A 1 249 ? 54.42  105.634 14.869 1   56.23  ? 271 ARG   A CZ  1 
ATOM   1914  N  NH1 . ARG   A 1 249 ? 55.245 105.207 13.918 1   55.64  ? 271 ARG   A NH1 1 
ATOM   1915  N  NH2 . ARG   A 1 249 ? 54.879 106.444 15.812 1   55.79  ? 271 ARG   A NH2 1 
ATOM   1916  N  N   . ALA   A 1 250 ? 50.851 99.213  14.756 1   44.25  ? 272 ALA   A N   1 
ATOM   1917  C  CA  . ALA   A 1 250 ? 50.492 98.516  15.988 1   43.69  ? 272 ALA   A CA  1 
ATOM   1918  C  C   . ALA   A 1 250 ? 51.453 97.332  16.211 1   43.63  ? 272 ALA   A C   1 
ATOM   1919  O  O   . ALA   A 1 250 ? 51.855 97.078  17.346 1   44.06  ? 272 ALA   A O   1 
ATOM   1920  C  CB  . ALA   A 1 250 ? 49.06  98.029  15.932 1   43.6   ? 272 ALA   A CB  1 
ATOM   1921  N  N   . LEU   A 1 251 ? 51.852 96.638  15.122 1   42.77  ? 273 LEU   A N   1 
ATOM   1922  C  CA  . LEU   A 1 251 ? 52.823 95.548  15.151 1   42.23  ? 273 LEU   A CA  1 
ATOM   1923  C  C   . LEU   A 1 251 ? 54.212 96.067  15.568 1   41.84  ? 273 LEU   A C   1 
ATOM   1924  O  O   . LEU   A 1 251 ? 54.941 95.368  16.263 1   41.7   ? 273 LEU   A O   1 
ATOM   1925  C  CB  . LEU   A 1 251 ? 52.905 94.887  13.771 1   42.56  ? 273 LEU   A CB  1 
ATOM   1926  C  CG  . LEU   A 1 251 ? 53.768 93.616  13.702 1   44.41  ? 273 LEU   A CG  1 
ATOM   1927  C  CD1 . LEU   A 1 251 ? 53.216 92.534  14.613 1   45.39  ? 273 LEU   A CD1 1 
ATOM   1928  C  CD2 . LEU   A 1 251 ? 53.866 93.083  12.291 1   44.45  ? 273 LEU   A CD2 1 
ATOM   1929  N  N   . GLN   A 1 252 ? 54.563 97.302  15.177 1   41.65  ? 274 GLN   A N   1 
ATOM   1930  C  CA  . GLN   A 1 252 ? 55.833 97.905  15.564 1   42.08  ? 274 GLN   A CA  1 
ATOM   1931  C  C   . GLN   A 1 252 ? 55.856 98.129  17.068 1   42.53  ? 274 GLN   A C   1 
ATOM   1932  O  O   . GLN   A 1 252 ? 56.839 97.771  17.725 1   42.99  ? 274 GLN   A O   1 
ATOM   1933  C  CB  . GLN   A 1 252 ? 56.061 99.234  14.832 1   43.94  ? 274 GLN   A CB  1 
ATOM   1934  C  CG  . GLN   A 1 252 ? 56.117 99.115  13.305 1   47.13  ? 274 GLN   A CG  1 
ATOM   1935  C  CD  . GLN   A 1 252 ? 56.338 100.452 12.625 1   50.85  ? 274 GLN   A CD  1 
ATOM   1936  O  OE1 . GLN   A 1 252 ? 56.588 101.492 13.262 1   52.86  ? 274 GLN   A OE1 1 
ATOM   1937  N  NE2 . GLN   A 1 252 ? 56.265 100.451 11.305 1   50.01  ? 274 GLN   A NE2 1 
ATOM   1938  N  N   . GLY   A 1 253 ? 54.764 98.689  17.605 1   42.1   ? 275 GLY   A N   1 
ATOM   1939  C  CA  . GLY   A 1 253 ? 54.619 98.941  19.035 1   41.81  ? 275 GLY   A CA  1 
ATOM   1940  C  C   . GLY   A 1 253 ? 54.593 97.663  19.852 1   41.33  ? 275 GLY   A C   1 
ATOM   1941  O  O   . GLY   A 1 253 ? 55.183 97.61   20.929 1   41.21  ? 275 GLY   A O   1 
ATOM   1942  N  N   . ALA   A 1 254 ? 53.922 96.614  19.337 1   40.91  ? 276 ALA   A N   1 
ATOM   1943  C  CA  . ALA   A 1 254 ? 53.85  95.321  20.013 1   41.09  ? 276 ALA   A CA  1 
ATOM   1944  C  C   . ALA   A 1 254 ? 55.237 94.684  20.06  1   41.54  ? 276 ALA   A C   1 
ATOM   1945  O  O   . ALA   A 1 254 ? 55.627 94.184  21.106 1   41.36  ? 276 ALA   A O   1 
ATOM   1946  C  CB  . ALA   A 1 254 ? 52.865 94.398  19.304 1   40.9   ? 276 ALA   A CB  1 
ATOM   1947  N  N   . ILE   A 1 255 ? 55.992 94.737  18.945 1   42     ? 277 ILE   A N   1 
ATOM   1948  C  CA  . ILE   A 1 255 ? 57.356 94.199  18.859 1   42.64  ? 277 ILE   A CA  1 
ATOM   1949  C  C   . ILE   A 1 255 ? 58.275 94.954  19.827 1   43.96  ? 277 ILE   A C   1 
ATOM   1950  O  O   . ILE   A 1 255 ? 59.039 94.331  20.573 1   44.54  ? 277 ILE   A O   1 
ATOM   1951  C  CB  . ILE   A 1 255 ? 57.867 94.221  17.388 1   42.6   ? 277 ILE   A CB  1 
ATOM   1952  C  CG1 . ILE   A 1 255 ? 57.262 93.068  16.586 1   42.8   ? 277 ILE   A CG1 1 
ATOM   1953  C  CG2 . ILE   A 1 255 ? 59.402 94.203  17.288 1   43.05  ? 277 ILE   A CG2 1 
ATOM   1954  C  CD1 . ILE   A 1 255 ? 57.437 93.173  15.129 1   43.94  ? 277 ILE   A CD1 1 
ATOM   1955  N  N   . MET   A 1 256 ? 58.151 96.284  19.866 1   44.07  ? 278 MET   A N   1 
ATOM   1956  C  CA  . MET   A 1 256 ? 58.953 97.114  20.766 1   44.42  ? 278 MET   A CA  1 
ATOM   1957  C  C   . MET   A 1 256 ? 58.747 96.765  22.236 1   44.53  ? 278 MET   A C   1 
ATOM   1958  O  O   . MET   A 1 256 ? 59.725 96.626  22.977 1   45.05  ? 278 MET   A O   1 
ATOM   1959  C  CB  . MET   A 1 256 ? 58.659 98.6    20.544 1   45.03  ? 278 MET   A CB  1 
ATOM   1960  C  CG  . MET   A 1 256 ? 59.649 99.464  21.23  1   47.64  ? 278 MET   A CG  1 
ATOM   1961  S  SD  . MET   A 1 256 ? 59.313 101.206 21.052 1   56.21  ? 278 MET   A SD  1 
ATOM   1962  C  CE  . MET   A 1 256 ? 60.68  101.833 21.98  1   55.02  ? 278 MET   A CE  1 
ATOM   1963  N  N   . ILE   A 1 257 ? 57.483 96.601  22.653 1   43.92  ? 279 ILE   A N   1 
ATOM   1964  C  CA  . ILE   A 1 257 ? 57.144 96.238  24.023 1   44.15  ? 279 ILE   A CA  1 
ATOM   1965  C  C   . ILE   A 1 257 ? 57.749 94.886  24.392 1   44.26  ? 279 ILE   A C   1 
ATOM   1966  O  O   . ILE   A 1 257 ? 58.279 94.749  25.492 1   44.05  ? 279 ILE   A O   1 
ATOM   1967  C  CB  . ILE   A 1 257 ? 55.606 96.276  24.191 1   44.59  ? 279 ILE   A CB  1 
ATOM   1968  C  CG1 . ILE   A 1 257 ? 55.098 97.725  24.203 1   45.86  ? 279 ILE   A CG1 1 
ATOM   1969  C  CG2 . ILE   A 1 257 ? 55.153 95.54   25.421 1   44.75  ? 279 ILE   A CG2 1 
ATOM   1970  C  CD1 . ILE   A 1 257 ? 53.565 97.858  24.156 1   47.09  ? 279 ILE   A CD1 1 
ATOM   1971  N  N   . THR   A 1 258 ? 57.697 93.896  23.463 1   44.53  ? 280 THR   A N   1 
ATOM   1972  C  CA  . THR   A 1 258 ? 58.252 92.558  23.713 1   45.22  ? 280 THR   A CA  1 
ATOM   1973  C  C   . THR   A 1 258 ? 59.768 92.545  23.815 1   46.21  ? 280 THR   A C   1 
ATOM   1974  O  O   . THR   A 1 258 ? 60.322 91.63   24.414 1   47     ? 280 THR   A O   1 
ATOM   1975  C  CB  . THR   A 1 258 ? 57.758 91.514  22.701 1   45.91  ? 280 THR   A CB  1 
ATOM   1976  O  OG1 . THR   A 1 258 ? 58.177 91.859  21.383 1   47.14  ? 280 THR   A OG1 1 
ATOM   1977  C  CG2 . THR   A 1 258 ? 56.274 91.322  22.745 1   45.88  ? 280 THR   A CG2 1 
ATOM   1978  N  N   . PHE   A 1 259 ? 60.44  93.542  23.225 1   46.22  ? 281 PHE   A N   1 
ATOM   1979  C  CA  . PHE   A 1 259 ? 61.892 93.66   23.26  1   46.38  ? 281 PHE   A CA  1 
ATOM   1980  C  C   . PHE   A 1 259 ? 62.367 94.232  24.594 1   46.84  ? 281 PHE   A C   1 
ATOM   1981  O  O   . PHE   A 1 259 ? 63.405 93.815  25.114 1   46.55  ? 281 PHE   A O   1 
ATOM   1982  C  CB  . PHE   A 1 259 ? 62.376 94.554  22.113 1   45.96  ? 281 PHE   A CB  1 
ATOM   1983  C  CG  . PHE   A 1 259 ? 62.667 93.849  20.805 1   46.57  ? 281 PHE   A CG  1 
ATOM   1984  C  CD1 . PHE   A 1 259 ? 62.005 92.681  20.459 1   47.26  ? 281 PHE   A CD1 1 
ATOM   1985  C  CD2 . PHE   A 1 259 ? 63.579 94.37   19.906 1   47.2   ? 281 PHE   A CD2 1 
ATOM   1986  C  CE1 . PHE   A 1 259 ? 62.254 92.054  19.24  1   47.55  ? 281 PHE   A CE1 1 
ATOM   1987  C  CE2 . PHE   A 1 259 ? 63.844 93.723  18.704 1   47.42  ? 281 PHE   A CE2 1 
ATOM   1988  C  CZ  . PHE   A 1 259 ? 63.177 92.575  18.379 1   47.06  ? 281 PHE   A CZ  1 
ATOM   1989  N  N   . TYR   A 1 260 ? 61.625 95.195  25.138 1   47.54  ? 282 TYR   A N   1 
ATOM   1990  C  CA  . TYR   A 1 260 ? 62.013 95.863  26.375 1   49.13  ? 282 TYR   A CA  1 
ATOM   1991  C  C   . TYR   A 1 260 ? 61.108 95.553  27.558 1   50.69  ? 282 TYR   A C   1 
ATOM   1992  O  O   . TYR   A 1 260 ? 61.001 96.371  28.47  1   51.18  ? 282 TYR   A O   1 
ATOM   1993  C  CB  . TYR   A 1 260 ? 62.073 97.376  26.148 1   49.45  ? 282 TYR   A CB  1 
ATOM   1994  C  CG  . TYR   A 1 260 ? 62.95  97.769  24.977 1   50.49  ? 282 TYR   A CG  1 
ATOM   1995  C  CD1 . TYR   A 1 260 ? 64.332 97.689  25.061 1   51.36  ? 282 TYR   A CD1 1 
ATOM   1996  C  CD2 . TYR   A 1 260 ? 62.396 98.222  23.79  1   51.27  ? 282 TYR   A CD2 1 
ATOM   1997  C  CE1 . TYR   A 1 260 ? 65.141 98.057  23.996 1   52.36  ? 282 TYR   A CE1 1 
ATOM   1998  C  CE2 . TYR   A 1 260 ? 63.194 98.58   22.713 1   52.32  ? 282 TYR   A CE2 1 
ATOM   1999  C  CZ  . TYR   A 1 260 ? 64.569 98.497  22.821 1   53.34  ? 282 TYR   A CZ  1 
ATOM   2000  O  OH  . TYR   A 1 260 ? 65.377 98.871  21.778 1   54.99  ? 282 TYR   A OH  1 
ATOM   2001  N  N   . ARG   A 1 261 ? 60.489 94.363  27.565 1   51.4   ? 283 ARG   A N   1 
ATOM   2002  C  CA  . ARG   A 1 261 ? 59.564 93.918  28.612 1   52.34  ? 283 ARG   A CA  1 
ATOM   2003  C  C   . ARG   A 1 261 ? 60.184 93.864  30.003 1   53.3   ? 283 ARG   A C   1 
ATOM   2004  O  O   . ARG   A 1 261 ? 59.463 93.961  30.991 1   53.7   ? 283 ARG   A O   1 
ATOM   2005  C  CB  . ARG   A 1 261 ? 58.954 92.556  28.252 1   53.39  ? 283 ARG   A CB  1 
ATOM   2006  C  CG  . ARG   A 1 261 ? 60.005 91.489  28.022 1   55.31  ? 283 ARG   A CG  1 
ATOM   2007  C  CD  . ARG   A 1 261 ? 59.369 90.144  27.841 1   57.26  ? 283 ARG   A CD  1 
ATOM   2008  N  NE  . ARG   A 1 261 ? 58.839 89.627  29.101 1   59     ? 283 ARG   A NE  1 
ATOM   2009  C  CZ  . ARG   A 1 261 ? 58.237 88.448  29.234 1   59.98  ? 283 ARG   A CZ  1 
ATOM   2010  N  NH1 . ARG   A 1 261 ? 58.076 87.653  28.181 1   58.79  ? 283 ARG   A NH1 1 
ATOM   2011  N  NH2 . ARG   A 1 261 ? 57.79  88.055  30.421 1   59.43  ? 283 ARG   A NH2 1 
ATOM   2012  N  N   . ASP   A 1 262 ? 61.509 93.693  30.093 1   53.59  ? 284 ASP   A N   1 
ATOM   2013  C  CA  . ASP   A 1 262 ? 62.18  93.653  31.397 1   54.02  ? 284 ASP   A CA  1 
ATOM   2014  C  C   . ASP   A 1 262 ? 62.413 95.065  31.99  1   54.59  ? 284 ASP   A C   1 
ATOM   2015  O  O   . ASP   A 1 262 ? 62.692 95.186  33.182 1   54.75  ? 284 ASP   A O   1 
ATOM   2016  C  CB  . ASP   A 1 262 ? 63.473 92.818  31.336 1   55.4   ? 284 ASP   A CB  1 
ATOM   2017  C  CG  . ASP   A 1 262 ? 63.223 91.317  31.321 1   60.04  ? 284 ASP   A CG  1 
ATOM   2018  O  OD1 . ASP   A 1 262 ? 62.21  90.873  31.918 1   59.94  ? 284 ASP   A OD1 1 
ATOM   2019  O  OD2 . ASP   A 1 262 ? 64.043 90.581  30.718 1   63.36  ? 284 ASP   A OD2 1 
ATOM   2020  N  N   . GLU   A 1 263 ? 62.24  96.128  31.171 1   54.89  ? 285 GLU   A N   1 
ATOM   2021  C  CA  . GLU   A 1 263 ? 62.364 97.516  31.594 1   55.38  ? 285 GLU   A CA  1 
ATOM   2022  C  C   . GLU   A 1 263 ? 61.075 97.99   32.241 1   55.15  ? 285 GLU   A C   1 
ATOM   2023  O  O   . GLU   A 1 263 ? 59.997 97.73   31.719 1   54.88  ? 285 GLU   A O   1 
ATOM   2024  C  CB  . GLU   A 1 263 ? 62.71  98.415  30.403 1   58.13  ? 285 GLU   A CB  1 
ATOM   2025  C  CG  . GLU   A 1 263 ? 63.998 98.001  29.718 1   63.84  ? 285 GLU   A CG  1 
ATOM   2026  C  CD  . GLU   A 1 263 ? 65.221 97.996  30.616 1   69.23  ? 285 GLU   A CD  1 
ATOM   2027  O  OE1 . GLU   A 1 263 ? 65.37  98.943  31.424 1   69.11  ? 285 GLU   A OE1 1 
ATOM   2028  O  OE2 . GLU   A 1 263 ? 66.029 97.043  30.509 1   71.16  ? 285 GLU   A OE2 1 
ATOM   2029  N  N   . PRO   A 1 264 ? 61.177 98.712  33.369 1   55.28  ? 286 PRO   A N   1 
ATOM   2030  C  CA  . PRO   A 1 264 ? 59.963 99.173  34.071 1   55.5   ? 286 PRO   A CA  1 
ATOM   2031  C  C   . PRO   A 1 264 ? 58.925 99.897  33.21  1   56.02  ? 286 PRO   A C   1 
ATOM   2032  O  O   . PRO   A 1 264 ? 57.719 99.707  33.399 1   56.65  ? 286 PRO   A O   1 
ATOM   2033  C  CB  . PRO   A 1 264 ? 60.522 100.075 35.17  1   56.06  ? 286 PRO   A CB  1 
ATOM   2034  C  CG  . PRO   A 1 264 ? 61.9   99.574  35.397 1   56.42  ? 286 PRO   A CG  1 
ATOM   2035  C  CD  . PRO   A 1 264 ? 62.406 99.088  34.095 1   54.78  ? 286 PRO   A CD  1 
ATOM   2036  N  N   . ARG   A 1 265 ? 59.393 100.689 32.246 1   55.71  ? 287 ARG   A N   1 
ATOM   2037  C  CA  . ARG   A 1 265 ? 58.552 101.443 31.333 1   56.44  ? 287 ARG   A CA  1 
ATOM   2038  C  C   . ARG   A 1 265 ? 57.65  100.537 30.504 1   55.59  ? 287 ARG   A C   1 
ATOM   2039  O  O   . ARG   A 1 265 ? 56.517 100.906 30.203 1   55.91  ? 287 ARG   A O   1 
ATOM   2040  C  CB  . ARG   A 1 265 ? 59.442 102.239 30.374 1   59.89  ? 287 ARG   A CB  1 
ATOM   2041  C  CG  . ARG   A 1 265 ? 59.607 103.708 30.733 1   66.74  ? 287 ARG   A CG  1 
ATOM   2042  C  CD  . ARG   A 1 265 ? 60.75  104.386 29.967 1   73.54  ? 287 ARG   A CD  1 
ATOM   2043  N  NE  . ARG   A 1 265 ? 60.761 104.095 28.526 1   79.35  ? 287 ARG   A NE  1 
ATOM   2044  C  CZ  . ARG   A 1 265 ? 59.991 104.708 27.631 1   83.74  ? 287 ARG   A CZ  1 
ATOM   2045  N  NH1 . ARG   A 1 265 ? 59.13  105.645 28.015 1   84.07  ? 287 ARG   A NH1 1 
ATOM   2046  N  NH2 . ARG   A 1 265 ? 60.071 104.385 26.344 1   84.56  ? 287 ARG   A NH2 1 
ATOM   2047  N  N   . PHE   A 1 266 ? 58.158 99.368  30.105 1   54.23  ? 288 PHE   A N   1 
ATOM   2048  C  CA  . PHE   A 1 266 ? 57.415 98.449  29.247 1   52.95  ? 288 PHE   A CA  1 
ATOM   2049  C  C   . PHE   A 1 266 ? 56.921 97.192  29.945 1   51.59  ? 288 PHE   A C   1 
ATOM   2050  O  O   . PHE   A 1 266 ? 56.301 96.366  29.283 1   51.09  ? 288 PHE   A O   1 
ATOM   2051  C  CB  . PHE   A 1 266 ? 58.27  98.04   28.041 1   52.63  ? 288 PHE   A CB  1 
ATOM   2052  C  CG  . PHE   A 1 266 ? 58.678 99.169  27.138 1   53.5   ? 288 PHE   A CG  1 
ATOM   2053  C  CD1 . PHE   A 1 266 ? 59.858 99.854  27.35  1   54.15  ? 288 PHE   A CD1 1 
ATOM   2054  C  CD2 . PHE   A 1 266 ? 57.889 99.534  26.06  1   54.7   ? 288 PHE   A CD2 1 
ATOM   2055  C  CE1 . PHE   A 1 266 ? 60.24  100.883 26.505 1   54.96  ? 288 PHE   A CE1 1 
ATOM   2056  C  CE2 . PHE   A 1 266 ? 58.267 100.575 25.223 1   55.39  ? 288 PHE   A CE2 1 
ATOM   2057  C  CZ  . PHE   A 1 266 ? 59.436 101.246 25.456 1   55.03  ? 288 PHE   A CZ  1 
ATOM   2058  N  N   . SER   A 1 267 ? 57.177 97.03   31.254 1   51.04  ? 289 SER   A N   1 
ATOM   2059  C  CA  . SER   A 1 267 ? 56.745 95.824  31.966 1   50.95  ? 289 SER   A CA  1 
ATOM   2060  C  C   . SER   A 1 267 ? 55.222 95.714  32.094 1   49.76  ? 289 SER   A C   1 
ATOM   2061  O  O   . SER   A 1 267 ? 54.67  94.629  31.901 1   49.59  ? 289 SER   A O   1 
ATOM   2062  C  CB  . SER   A 1 267 ? 57.427 95.703  33.323 1   52.76  ? 289 SER   A CB  1 
ATOM   2063  O  OG  . SER   A 1 267 ? 56.845 96.568  34.282 1   56.94  ? 289 SER   A OG  1 
ATOM   2064  N  N   . GLN   A 1 268 ? 54.551 96.829  32.397 1   48.72  ? 290 GLN   A N   1 
ATOM   2065  C  CA  . GLN   A 1 268 ? 53.098 96.82   32.507 1   48.61  ? 290 GLN   A CA  1 
ATOM   2066  C  C   . GLN   A 1 268 ? 52.429 96.762  31.12  1   47.8   ? 290 GLN   A C   1 
ATOM   2067  O  O   . GLN   A 1 268 ? 51.572 95.889  30.937 1   48.2   ? 290 GLN   A O   1 
ATOM   2068  C  CB  . GLN   A 1 268 ? 52.574 97.954  33.399 1   51.01  ? 290 GLN   A CB  1 
ATOM   2069  C  CG  . GLN   A 1 268 ? 51.643 97.482  34.536 1   55.52  ? 290 GLN   A CG  1 
ATOM   2070  C  CD  . GLN   A 1 268 ? 52.14  96.299  35.355 1   60.58  ? 290 GLN   A CD  1 
ATOM   2071  O  OE1 . GLN   A 1 268 ? 53.337 96.158  35.657 1   61.81  ? 290 GLN   A OE1 1 
ATOM   2072  N  NE2 . GLN   A 1 268 ? 51.216 95.421  35.747 1   61.99  ? 290 GLN   A NE2 1 
ATOM   2073  N  N   . PRO   A 1 269 ? 52.867 97.529  30.086 1   46.3   ? 291 PRO   A N   1 
ATOM   2074  C  CA  . PRO   A 1 269 ? 52.282 97.351  28.75  1   45.64  ? 291 PRO   A CA  1 
ATOM   2075  C  C   . PRO   A 1 269 ? 52.403 95.911  28.237 1   45.54  ? 291 PRO   A C   1 
ATOM   2076  O  O   . PRO   A 1 269 ? 51.468 95.423  27.603 1   45.97  ? 291 PRO   A O   1 
ATOM   2077  C  CB  . PRO   A 1 269 ? 53.097 98.313  27.886 1   46.1   ? 291 PRO   A CB  1 
ATOM   2078  C  CG  . PRO   A 1 269 ? 53.58  99.338  28.817 1   46.34  ? 291 PRO   A CG  1 
ATOM   2079  C  CD  . PRO   A 1 269 ? 53.877 98.605  30.074 1   45.32  ? 291 PRO   A CD  1 
ATOM   2080  N  N   . HIS   A 1 270 ? 53.522 95.214  28.555 1   44.76  ? 292 HIS   A N   1 
ATOM   2081  C  CA  . HIS   A 1 270 ? 53.719 93.824  28.155 1   44.71  ? 292 HIS   A CA  1 
ATOM   2082  C  C   . HIS   A 1 270 ? 52.781 92.885  28.893 1   45.24  ? 292 HIS   A C   1 
ATOM   2083  O  O   . HIS   A 1 270 ? 52.283 91.921  28.314 1   45.72  ? 292 HIS   A O   1 
ATOM   2084  C  CB  . HIS   A 1 270 ? 55.163 93.371  28.357 1   45.45  ? 292 HIS   A CB  1 
ATOM   2085  C  CG  . HIS   A 1 270 ? 55.392 91.973  27.863 1   48.04  ? 292 HIS   A CG  1 
ATOM   2086  N  ND1 . HIS   A 1 270 ? 55.477 91.691  26.5   1   50.31  ? 292 HIS   A ND1 1 
ATOM   2087  C  CD2 . HIS   A 1 270 ? 55.476 90.815  28.555 1   48.91  ? 292 HIS   A CD2 1 
ATOM   2088  C  CE1 . HIS   A 1 270 ? 55.648 90.383  26.414 1   50.45  ? 292 HIS   A CE1 1 
ATOM   2089  N  NE2 . HIS   A 1 270 ? 55.653 89.812  27.623 1   50.3   ? 292 HIS   A NE2 1 
ATOM   2090  N  N   . GLN   A 1 271 ? 52.541 93.153  30.177 1   45.08  ? 293 GLN   A N   1 
ATOM   2091  C  CA  . GLN   A 1 271 ? 51.617 92.367  30.982 1   44.89  ? 293 GLN   A CA  1 
ATOM   2092  C  C   . GLN   A 1 271 ? 50.202 92.469  30.394 1   44.37  ? 293 GLN   A C   1 
ATOM   2093  O  O   . GLN   A 1 271 ? 49.498 91.465  30.333 1   44.44  ? 293 GLN   A O   1 
ATOM   2094  C  CB  . GLN   A 1 271 ? 51.679 92.819  32.45  1   47.2   ? 293 GLN   A CB  1 
ATOM   2095  C  CG  . GLN   A 1 271 ? 50.901 91.945  33.426 1   54.01  ? 293 GLN   A CG  1 
ATOM   2096  C  CD  . GLN   A 1 271 ? 51.266 90.476  33.348 1   63.35  ? 293 GLN   A CD  1 
ATOM   2097  O  OE1 . GLN   A 1 271 ? 52.422 90.102  33.087 1   67.34  ? 293 GLN   A OE1 1 
ATOM   2098  N  NE2 . GLN   A 1 271 ? 50.29  89.599  33.581 1   64.19  ? 293 GLN   A NE2 1 
ATOM   2099  N  N   . LEU   A 1 272 ? 49.833 93.659  29.874 1   43.82  ? 294 LEU   A N   1 
ATOM   2100  C  CA  . LEU   A 1 272 ? 48.554 93.91   29.204 1   43.97  ? 294 LEU   A CA  1 
ATOM   2101  C  C   . LEU   A 1 272 ? 48.422 93.01   27.948 1   43.78  ? 294 LEU   A C   1 
ATOM   2102  O  O   . LEU   A 1 272 ? 47.384 92.384  27.755 1   43.59  ? 294 LEU   A O   1 
ATOM   2103  C  CB  . LEU   A 1 272 ? 48.478 95.402  28.82  1   43.77  ? 294 LEU   A CB  1 
ATOM   2104  C  CG  . LEU   A 1 272 ? 47.109 95.993  28.541 1   43.92  ? 294 LEU   A CG  1 
ATOM   2105  C  CD1 . LEU   A 1 272 ? 47.081 97.464  28.918 1   43.33  ? 294 LEU   A CD1 1 
ATOM   2106  C  CD2 . LEU   A 1 272 ? 46.723 95.809  27.082 1   44.4   ? 294 LEU   A CD2 1 
ATOM   2107  N  N   . LEU   A 1 273 ? 49.478 92.936  27.117 1   43.51  ? 295 LEU   A N   1 
ATOM   2108  C  CA  . LEU   A 1 273 ? 49.491 92.083  25.922 1   43.71  ? 295 LEU   A CA  1 
ATOM   2109  C  C   . LEU   A 1 273 ? 49.396 90.606  26.302 1   42.97  ? 295 LEU   A C   1 
ATOM   2110  O  O   . LEU   A 1 273 ? 48.681 89.836  25.667 1   42.18  ? 295 LEU   A O   1 
ATOM   2111  C  CB  . LEU   A 1 273 ? 50.778 92.308  25.101 1   44.38  ? 295 LEU   A CB  1 
ATOM   2112  C  CG  . LEU   A 1 273 ? 50.981 93.704  24.497 1   46.36  ? 295 LEU   A CG  1 
ATOM   2113  C  CD1 . LEU   A 1 273 ? 52.245 93.746  23.664 1   46.83  ? 295 LEU   A CD1 1 
ATOM   2114  C  CD2 . LEU   A 1 273 ? 49.772 94.146  23.66  1   46.94  ? 295 LEU   A CD2 1 
ATOM   2115  N  N   . THR   A 1 274 ? 50.113 90.227  27.353 1   42.96  ? 296 THR   A N   1 
ATOM   2116  C  CA  . THR   A 1 274 ? 50.155 88.87   27.87  1   43.14  ? 296 THR   A CA  1 
ATOM   2117  C  C   . THR   A 1 274 ? 48.792 88.436  28.343 1   42.92  ? 296 THR   A C   1 
ATOM   2118  O  O   . THR   A 1 274 ? 48.375 87.322  28.034 1   43.69  ? 296 THR   A O   1 
ATOM   2119  C  CB  . THR   A 1 274 ? 51.221 88.794  28.947 1   44.59  ? 296 THR   A CB  1 
ATOM   2120  O  OG1 . THR   A 1 274 ? 52.481 88.943  28.296 1   45.92  ? 296 THR   A OG1 1 
ATOM   2121  C  CG2 . THR   A 1 274 ? 51.181 87.508  29.73  1   44.72  ? 296 THR   A CG2 1 
ATOM   2122  N  N   . LEU   A 1 275 ? 48.061 89.323  29.027 1   41.72  ? 297 LEU   A N   1 
ATOM   2123  C  CA  . LEU   A 1 275 ? 46.723 88.98   29.508 1   40.96  ? 297 LEU   A CA  1 
ATOM   2124  C  C   . LEU   A 1 275 ? 45.731 88.836  28.379 1   41.01  ? 297 LEU   A C   1 
ATOM   2125  O  O   . LEU   A 1 275 ? 44.878 87.958  28.436 1   41.5   ? 297 LEU   A O   1 
ATOM   2126  C  CB  . LEU   A 1 275 ? 46.238 89.975  30.56  1   40.52  ? 297 LEU   A CB  1 
ATOM   2127  C  CG  . LEU   A 1 275 ? 46.993 89.895  31.869 1   41.11  ? 297 LEU   A CG  1 
ATOM   2128  C  CD1 . LEU   A 1 275 ? 46.764 91.126  32.711 1   41.45  ? 297 LEU   A CD1 1 
ATOM   2129  C  CD2 . LEU   A 1 275 ? 46.66  88.602  32.612 1   41.13  ? 297 LEU   A CD2 1 
ATOM   2130  N  N   . LEU   A 1 276 ? 45.881 89.636  27.315 1   40.74  ? 298 LEU   A N   1 
ATOM   2131  C  CA  . LEU   A 1 276 ? 45.036 89.554  26.12  1   40.43  ? 298 LEU   A CA  1 
ATOM   2132  C  C   . LEU   A 1 276 ? 45.207 88.203  25.424 1   41.05  ? 298 LEU   A C   1 
ATOM   2133  O  O   . LEU   A 1 276 ? 44.235 87.626  24.924 1   40.93  ? 298 LEU   A O   1 
ATOM   2134  C  CB  . LEU   A 1 276 ? 45.389 90.688  25.16  1   40.09  ? 298 LEU   A CB  1 
ATOM   2135  C  CG  . LEU   A 1 276 ? 45.004 92.082  25.619 1   40.55  ? 298 LEU   A CG  1 
ATOM   2136  C  CD1 . LEU   A 1 276 ? 45.555 93.125  24.669 1   40.83  ? 298 LEU   A CD1 1 
ATOM   2137  C  CD2 . LEU   A 1 276 ? 43.512 92.21   25.768 1   40.84  ? 298 LEU   A CD2 1 
ATOM   2138  N  N   . MET   A 1 277 ? 46.451 87.7    25.394 1   41.62  ? 299 MET   A N   1 
ATOM   2139  C  CA  . MET   A 1 277 ? 46.766 86.394  24.822 1   42.19  ? 299 MET   A CA  1 
ATOM   2140  C  C   . MET   A 1 277 ? 46.224 85.277  25.705 1   42.48  ? 299 MET   A C   1 
ATOM   2141  O  O   . MET   A 1 277 ? 45.785 84.257  25.19  1   42.67  ? 299 MET   A O   1 
ATOM   2142  C  CB  . MET   A 1 277 ? 48.279 86.234  24.682 1   42.9   ? 299 MET   A CB  1 
ATOM   2143  C  CG  . MET   A 1 277 ? 48.838 86.886  23.451 1   44.98  ? 299 MET   A CG  1 
ATOM   2144  S  SD  . MET   A 1 277 ? 50.641 86.964  23.513 1   46.85  ? 299 MET   A SD  1 
ATOM   2145  C  CE  . MET   A 1 277 ? 51.028 85.206  23.475 1   46.54  ? 299 MET   A CE  1 
ATOM   2146  N  N   . ASP   A 1 278 ? 46.276 85.459  27.035 1   42.53  ? 300 ASP   A N   1 
ATOM   2147  C  CA  . ASP   A 1 278 ? 45.777 84.477  27.992 1   43.07  ? 300 ASP   A CA  1 
ATOM   2148  C  C   . ASP   A 1 278 ? 44.265 84.338  27.855 1   43.07  ? 300 ASP   A C   1 
ATOM   2149  O  O   . ASP   A 1 278 ? 43.77  83.216  27.873 1   43.56  ? 300 ASP   A O   1 
ATOM   2150  C  CB  . ASP   A 1 278 ? 46.2   84.834  29.429 1   45.55  ? 300 ASP   A CB  1 
ATOM   2151  C  CG  . ASP   A 1 278 ? 47.7   84.676  29.714 1   51.92  ? 300 ASP   A CG  1 
ATOM   2152  O  OD1 . ASP   A 1 278 ? 48.44  84.245  28.803 1   53.58  ? 300 ASP   A OD1 1 
ATOM   2153  O  OD2 . ASP   A 1 278 ? 48.134 85.009  30.838 1   54.17  ? 300 ASP   A OD2 1 
ATOM   2154  N  N   . ILE   A 1 279 ? 43.545 85.463  27.64  1   42.59  ? 301 ILE   A N   1 
ATOM   2155  C  CA  . ILE   A 1 279 ? 42.087 85.497  27.43  1   42.51  ? 301 ILE   A CA  1 
ATOM   2156  C  C   . ILE   A 1 279 ? 41.723 84.736  26.161 1   42.06  ? 301 ILE   A C   1 
ATOM   2157  O  O   . ILE   A 1 279 ? 40.801 83.919  26.156 1   41.62  ? 301 ILE   A O   1 
ATOM   2158  C  CB  . ILE   A 1 279 ? 41.566 86.972  27.388 1   42.86  ? 301 ILE   A CB  1 
ATOM   2159  C  CG1 . ILE   A 1 279 ? 41.524 87.578  28.804 1   43.78  ? 301 ILE   A CG1 1 
ATOM   2160  C  CG2 . ILE   A 1 279 ? 40.188 87.085  26.714 1   43.06  ? 301 ILE   A CG2 1 
ATOM   2161  C  CD1 . ILE   A 1 279 ? 41.565 89.091  28.833 1   44.78  ? 301 ILE   A CD1 1 
ATOM   2162  N  N   . ASP   A 1 280 ? 42.474 85.005  25.095 1   42.03  ? 302 ASP   A N   1 
ATOM   2163  C  CA  . ASP   A 1 280 ? 42.32  84.389  23.785 1   42.26  ? 302 ASP   A CA  1 
ATOM   2164  C  C   . ASP   A 1 280 ? 42.515 82.884  23.862 1   42.82  ? 302 ASP   A C   1 
ATOM   2165  O  O   . ASP   A 1 280 ? 41.717 82.128  23.296 1   43.13  ? 302 ASP   A O   1 
ATOM   2166  C  CB  . ASP   A 1 280 ? 43.349 84.997  22.832 1   43.81  ? 302 ASP   A CB  1 
ATOM   2167  C  CG  . ASP   A 1 280 ? 42.819 85.392  21.472 1   48.74  ? 302 ASP   A CG  1 
ATOM   2168  O  OD1 . ASP   A 1 280 ? 41.595 85.221  21.225 1   49.52  ? 302 ASP   A OD1 1 
ATOM   2169  O  OD2 . ASP   A 1 280 ? 43.616 85.864  20.65  1   51.02  ? 302 ASP   A OD2 1 
ATOM   2170  N  N   . SER   A 1 281 ? 43.565 82.448  24.581 1   43.05  ? 303 SER   A N   1 
ATOM   2171  C  CA  . SER   A 1 281 ? 43.892 81.039  24.776 1   43.66  ? 303 SER   A CA  1 
ATOM   2172  C  C   . SER   A 1 281 ? 42.816 80.324  25.588 1   43.64  ? 303 SER   A C   1 
ATOM   2173  O  O   . SER   A 1 281 ? 42.453 79.194  25.258 1   43.8   ? 303 SER   A O   1 
ATOM   2174  C  CB  . SER   A 1 281 ? 45.24  80.91   25.473 1   45.69  ? 303 SER   A CB  1 
ATOM   2175  O  OG  . SER   A 1 281 ? 46.113 80.1    24.706 1   49.57  ? 303 SER   A OG  1 
ATOM   2176  N  N   . LEU   A 1 282 ? 42.285 80.999  26.635 1   42.99  ? 304 LEU   A N   1 
ATOM   2177  C  CA  . LEU   A 1 282 ? 41.236 80.461  27.505 1   42.33  ? 304 LEU   A CA  1 
ATOM   2178  C  C   . LEU   A 1 282 ? 39.9   80.359  26.804 1   42.21  ? 304 LEU   A C   1 
ATOM   2179  O  O   . LEU   A 1 282 ? 39.147 79.433  27.085 1   42.12  ? 304 LEU   A O   1 
ATOM   2180  C  CB  . LEU   A 1 282 ? 41.121 81.264  28.808 1   41.9   ? 304 LEU   A CB  1 
ATOM   2181  C  CG  . LEU   A 1 282 ? 42.185 80.944  29.831 1   42.27  ? 304 LEU   A CG  1 
ATOM   2182  C  CD1 . LEU   A 1 282 ? 42.339 82.06   30.81  1   42.67  ? 304 LEU   A CD1 1 
ATOM   2183  C  CD2 . LEU   A 1 282 ? 41.893 79.626  30.513 1   42.54  ? 304 LEU   A CD2 1 
ATOM   2184  N  N   . ILE   A 1 283 ? 39.607 81.271  25.875 1   42.53  ? 305 ILE   A N   1 
ATOM   2185  C  CA  . ILE   A 1 283 ? 38.372 81.173  25.087 1   43.4   ? 305 ILE   A CA  1 
ATOM   2186  C  C   . ILE   A 1 283 ? 38.433 79.944  24.15  1   44.04  ? 305 ILE   A C   1 
ATOM   2187  O  O   . ILE   A 1 283 ? 37.442 79.234  23.986 1   44.16  ? 305 ILE   A O   1 
ATOM   2188  C  CB  . ILE   A 1 283 ? 38.015 82.497  24.377 1   43.85  ? 305 ILE   A CB  1 
ATOM   2189  C  CG1 . ILE   A 1 283 ? 37.583 83.531  25.412 1   44.78  ? 305 ILE   A CG1 1 
ATOM   2190  C  CG2 . ILE   A 1 283 ? 36.899 82.283  23.345 1   44.43  ? 305 ILE   A CG2 1 
ATOM   2191  C  CD1 . ILE   A 1 283 ? 37.433 84.894  24.886 1   46.35  ? 305 ILE   A CD1 1 
ATOM   2192  N  N   . THR   A 1 284 ? 39.621 79.63   23.633 1   44.59  ? 306 THR   A N   1 
ATOM   2193  C  CA  . THR   A 1 284 ? 39.821 78.447  22.801 1   45.55  ? 306 THR   A CA  1 
ATOM   2194  C  C   . THR   A 1 284 ? 39.758 77.173  23.65  1   46.34  ? 306 THR   A C   1 
ATOM   2195  O  O   . THR   A 1 284 ? 39.162 76.185  23.218 1   47.46  ? 306 THR   A O   1 
ATOM   2196  C  CB  . THR   A 1 284 ? 41.095 78.598  21.981 1   46.87  ? 306 THR   A CB  1 
ATOM   2197  O  OG1 . THR   A 1 284 ? 40.931 79.738  21.135 1   48.53  ? 306 THR   A OG1 1 
ATOM   2198  C  CG2 . THR   A 1 284 ? 41.392 77.373  21.147 1   46.86  ? 306 THR   A CG2 1 
ATOM   2199  N  N   . LYS   A 1 285 ? 40.3   77.213  24.881 1   45.78  ? 307 LYS   A N   1 
ATOM   2200  C  CA  . LYS   A 1 285 ? 40.224 76.095  25.821 1   46.06  ? 307 LYS   A CA  1 
ATOM   2201  C  C   . LYS   A 1 285 ? 38.765 75.813  26.218 1   46.66  ? 307 LYS   A C   1 
ATOM   2202  O  O   . LYS   A 1 285 ? 38.416 74.651  26.436 1   47.08  ? 307 LYS   A O   1 
ATOM   2203  C  CB  . LYS   A 1 285 ? 41.1   76.345  27.06  1   47.76  ? 307 LYS   A CB  1 
ATOM   2204  C  CG  . LYS   A 1 285 ? 42.59  76.394  26.723 1   51.14  ? 307 LYS   A CG  1 
ATOM   2205  C  CD  . LYS   A 1 285 ? 43.459 76.517  27.945 1   55.22  ? 307 LYS   A CD  1 
ATOM   2206  C  CE  . LYS   A 1 285 ? 44.925 76.507  27.591 1   59.27  ? 307 LYS   A CE  1 
ATOM   2207  N  NZ  . LYS   A 1 285 ? 45.79  76.931  28.731 1   61.11  ? 307 LYS   A NZ  1 
ATOM   2208  N  N   . TRP   A 1 286 ? 37.905 76.857  26.279 1   46.6   ? 308 TRP   A N   1 
ATOM   2209  C  CA  . TRP   A 1 286 ? 36.492 76.632  26.569 1   47.19  ? 308 TRP   A CA  1 
ATOM   2210  C  C   . TRP   A 1 286 ? 35.847 75.987  25.358 1   46.84  ? 308 TRP   A C   1 
ATOM   2211  O  O   . TRP   A 1 286 ? 35.096 75.031  25.514 1   47.03  ? 308 TRP   A O   1 
ATOM   2212  C  CB  . TRP   A 1 286 ? 35.726 77.917  26.975 1   47.76  ? 308 TRP   A CB  1 
ATOM   2213  C  CG  . TRP   A 1 286 ? 34.254 77.648  27.158 1   48.61  ? 308 TRP   A CG  1 
ATOM   2214  C  CD1 . TRP   A 1 286 ? 33.662 77.052  28.233 1   49.34  ? 308 TRP   A CD1 1 
ATOM   2215  C  CD2 . TRP   A 1 286 ? 33.234 77.748  26.145 1   48.95  ? 308 TRP   A CD2 1 
ATOM   2216  N  NE1 . TRP   A 1 286 ? 32.334 76.806  27.967 1   49.45  ? 308 TRP   A NE1 1 
ATOM   2217  C  CE2 . TRP   A 1 286 ? 32.047 77.221  26.692 1   49.17  ? 308 TRP   A CE2 1 
ATOM   2218  C  CE3 . TRP   A 1 286 ? 33.221 78.202  24.815 1   49.75  ? 308 TRP   A CE3 1 
ATOM   2219  C  CZ2 . TRP   A 1 286 ? 30.848 77.193  25.981 1   49.67  ? 308 TRP   A CZ2 1 
ATOM   2220  C  CZ3 . TRP   A 1 286 ? 32.034 78.156  24.107 1   50.3   ? 308 TRP   A CZ3 1 
ATOM   2221  C  CH2 . TRP   A 1 286 ? 30.86  77.679  24.697 1   50.08  ? 308 TRP   A CH2 1 
ATOM   2222  N  N   . ARG   A 1 287 ? 36.125 76.506  24.156 1   46.45  ? 309 ARG   A N   1 
ATOM   2223  C  CA  . ARG   A 1 287 ? 35.558 75.981  22.908 1   46.41  ? 309 ARG   A CA  1 
ATOM   2224  C  C   . ARG   A 1 287 ? 35.891 74.501  22.718 1   46.65  ? 309 ARG   A C   1 
ATOM   2225  O  O   . ARG   A 1 287 ? 35.048 73.732  22.243 1   46.49  ? 309 ARG   A O   1 
ATOM   2226  C  CB  . ARG   A 1 287 ? 36.097 76.76   21.713 1   46.82  ? 309 ARG   A CB  1 
ATOM   2227  C  CG  . ARG   A 1 287 ? 35.545 78.146  21.552 1   48.54  ? 309 ARG   A CG  1 
ATOM   2228  C  CD  . ARG   A 1 287 ? 35.982 78.666  20.204 1   50.08  ? 309 ARG   A CD  1 
ATOM   2229  N  NE  . ARG   A 1 287 ? 36.136 80.121  20.165 1   52.01  ? 309 ARG   A NE  1 
ATOM   2230  C  CZ  . ARG   A 1 287 ? 35.143 80.974  19.942 1   53.4   ? 309 ARG   A CZ  1 
ATOM   2231  N  NH1 . ARG   A 1 287 ? 35.378 82.279  19.9   1   52.66  ? 309 ARG   A NH1 1 
ATOM   2232  N  NH2 . ARG   A 1 287 ? 33.906 80.53   19.754 1   53.9   ? 309 ARG   A NH2 1 
ATOM   2233  N  N   . TYR   A 1 288 ? 37.126 74.114  23.079 1   46.59  ? 310 TYR   A N   1 
ATOM   2234  C  CA  . TYR   A 1 288 ? 37.575 72.742  22.955 1   47.25  ? 310 TYR   A CA  1 
ATOM   2235  C  C   . TYR   A 1 288 ? 36.859 71.867  23.975 1   47.37  ? 310 TYR   A C   1 
ATOM   2236  O  O   . TYR   A 1 288 ? 36.353 70.802  23.621 1   47.39  ? 310 TYR   A O   1 
ATOM   2237  C  CB  . TYR   A 1 288 ? 39.098 72.659  23.13  1   47.75  ? 310 TYR   A CB  1 
ATOM   2238  C  CG  . TYR   A 1 288 ? 39.628 71.242  23.093 1   49.26  ? 310 TYR   A CG  1 
ATOM   2239  C  CD1 . TYR   A 1 288 ? 39.811 70.579  21.888 1   50.29  ? 310 TYR   A CD1 1 
ATOM   2240  C  CD2 . TYR   A 1 288 ? 39.941 70.564  24.262 1   50.4   ? 310 TYR   A CD2 1 
ATOM   2241  C  CE1 . TYR   A 1 288 ? 40.298 69.278  21.848 1   51.46  ? 310 TYR   A CE1 1 
ATOM   2242  C  CE2 . TYR   A 1 288 ? 40.41  69.257  24.234 1   51.48  ? 310 TYR   A CE2 1 
ATOM   2243  C  CZ  . TYR   A 1 288 ? 40.604 68.623  23.025 1   52.68  ? 310 TYR   A CZ  1 
ATOM   2244  O  OH  . TYR   A 1 288 ? 41.082 67.335  22.998 1   55     ? 310 TYR   A OH  1 
ATOM   2245  N  N   . ASN   A 1 289 ? 36.814 72.31   25.244 1   46.83  ? 311 ASN   A N   1 
ATOM   2246  C  CA  . ASN   A 1 289 ? 36.161 71.559  26.302 1   46.45  ? 311 ASN   A CA  1 
ATOM   2247  C  C   . ASN   A 1 289 ? 34.686 71.374  26.026 1   46.01  ? 311 ASN   A C   1 
ATOM   2248  O  O   . ASN   A 1 289 ? 34.154 70.304  26.3   1   46.28  ? 311 ASN   A O   1 
ATOM   2249  C  CB  . ASN   A 1 289 ? 36.387 72.244  27.638 1   47.98  ? 311 ASN   A CB  1 
ATOM   2250  C  CG  . ASN   A 1 289 ? 37.606 71.758  28.391 1   51.45  ? 311 ASN   A CG  1 
ATOM   2251  O  OD1 . ASN   A 1 289 ? 37.639 71.766  29.626 1   52.95  ? 311 ASN   A OD1 1 
ATOM   2252  N  ND2 . ASN   A 1 289 ? 38.634 71.321  27.682 1   52.09  ? 311 ASN   A ND2 1 
ATOM   2253  N  N   . HIS   A 1 290 ? 34.037 72.401  25.46  1   45.56  ? 312 HIS   A N   1 
ATOM   2254  C  CA  . HIS   A 1 290 ? 32.631 72.397  25.078 1   46.18  ? 312 HIS   A CA  1 
ATOM   2255  C  C   . HIS   A 1 290 ? 32.387 71.397  23.939 1   47.83  ? 312 HIS   A C   1 
ATOM   2256  O  O   . HIS   A 1 290 ? 31.451 70.596  24.032 1   48.39  ? 312 HIS   A O   1 
ATOM   2257  C  CB  . HIS   A 1 290 ? 32.197 73.811  24.658 1   46.05  ? 312 HIS   A CB  1 
ATOM   2258  C  CG  . HIS   A 1 290 ? 30.805 73.904  24.11  1   46.89  ? 312 HIS   A CG  1 
ATOM   2259  N  ND1 . HIS   A 1 290 ? 30.572 74.259  22.79  1   48.14  ? 312 HIS   A ND1 1 
ATOM   2260  C  CD2 . HIS   A 1 290 ? 29.617 73.696  24.721 1   47.69  ? 312 HIS   A CD2 1 
ATOM   2261  C  CE1 . HIS   A 1 290 ? 29.258 74.253  22.641 1   48.41  ? 312 HIS   A CE1 1 
ATOM   2262  N  NE2 . HIS   A 1 290 ? 28.639 73.924  23.773 1   48.67  ? 312 HIS   A NE2 1 
ATOM   2263  N  N   . VAL   A 1 291 ? 33.245 71.405  22.89  1   48     ? 313 VAL   A N   1 
ATOM   2264  C  CA  . VAL   A 1 291 ? 33.106 70.497  21.749 1   48.39  ? 313 VAL   A CA  1 
ATOM   2265  C  C   . VAL   A 1 291 ? 33.327 69.025  22.171 1   48.44  ? 313 VAL   A C   1 
ATOM   2266  O  O   . VAL   A 1 291 ? 32.657 68.141  21.629 1   48.21  ? 313 VAL   A O   1 
ATOM   2267  C  CB  . VAL   A 1 291 ? 33.952 70.918  20.503 1   49.56  ? 313 VAL   A CB  1 
ATOM   2268  C  CG1 . VAL   A 1 291 ? 35.346 70.317  20.522 1   50.37  ? 313 VAL   A CG1 1 
ATOM   2269  C  CG2 . VAL   A 1 291 ? 33.254 70.531  19.211 1   50.29  ? 313 VAL   A CG2 1 
ATOM   2270  N  N   . ILE   A 1 292 ? 34.204 68.763  23.165 1   48.52  ? 314 ILE   A N   1 
ATOM   2271  C  CA  . ILE   A 1 292 ? 34.426 67.397  23.666 1   49.21  ? 314 ILE   A CA  1 
ATOM   2272  C  C   . ILE   A 1 292 ? 33.203 66.911  24.472 1   49.47  ? 314 ILE   A C   1 
ATOM   2273  O  O   . ILE   A 1 292 ? 32.816 65.745  24.389 1   49.8   ? 314 ILE   A O   1 
ATOM   2274  C  CB  . ILE   A 1 292 ? 35.735 67.305  24.484 1   50.08  ? 314 ILE   A CB  1 
ATOM   2275  C  CG1 . ILE   A 1 292 ? 36.949 67.61   23.613 1   51.29  ? 314 ILE   A CG1 1 
ATOM   2276  C  CG2 . ILE   A 1 292 ? 35.882 65.94   25.155 1   50.62  ? 314 ILE   A CG2 1 
ATOM   2277  C  CD1 . ILE   A 1 292 ? 37.161 66.629  22.436 1   52.6   ? 314 ILE   A CD1 1 
ATOM   2278  N  N   . MET   A 1 293 ? 32.575 67.823  25.217 1   49.25  ? 315 MET   A N   1 
ATOM   2279  C  CA  . MET   A 1 293 ? 31.381 67.538  25.997 1   49.16  ? 315 MET   A CA  1 
ATOM   2280  C  C   . MET   A 1 293 ? 30.21  67.254  25.067 1   49.37  ? 315 MET   A C   1 
ATOM   2281  O  O   . MET   A 1 293 ? 29.437 66.338  25.339 1   49.97  ? 315 MET   A O   1 
ATOM   2282  C  CB  . MET   A 1 293 ? 31.068 68.725  26.916 1   49.14  ? 315 MET   A CB  1 
ATOM   2283  C  CG  . MET   A 1 293 ? 29.752 68.593  27.653 1   50.52  ? 315 MET   A CG  1 
ATOM   2284  S  SD  . MET   A 1 293 ? 29.349 70.042  28.641 1   51.23  ? 315 MET   A SD  1 
ATOM   2285  C  CE  . MET   A 1 293 ? 29.411 71.326  27.409 1   48.5   ? 315 MET   A CE  1 
ATOM   2286  N  N   . VAL   A 1 294 ? 30.084 68.026  23.968 1   48.89  ? 316 VAL   A N   1 
ATOM   2287  C  CA  . VAL   A 1 294 ? 29.033 67.846  22.963 1   49.23  ? 316 VAL   A CA  1 
ATOM   2288  C  C   . VAL   A 1 294 ? 29.152 66.448  22.337 1   49.62  ? 316 VAL   A C   1 
ATOM   2289  O  O   . VAL   A 1 294 ? 28.159 65.751  22.175 1   49.32  ? 316 VAL   A O   1 
ATOM   2290  C  CB  . VAL   A 1 294 ? 29.108 68.961  21.882 1   49.79  ? 316 VAL   A CB  1 
ATOM   2291  C  CG1 . VAL   A 1 294 ? 28.229 68.645  20.676 1   50     ? 316 VAL   A CG1 1 
ATOM   2292  C  CG2 . VAL   A 1 294 ? 28.746 70.315  22.467 1   50.46  ? 316 VAL   A CG2 1 
ATOM   2293  N  N   . GLN   A 1 295 ? 30.378 66.024  22.039 1   50.13  ? 317 GLN   A N   1 
ATOM   2294  C  CA  . GLN   A 1 295 ? 30.641 64.713  21.455 1   51.02  ? 317 GLN   A CA  1 
ATOM   2295  C  C   . GLN   A 1 295 ? 30.411 63.565  22.44  1   51.27  ? 317 GLN   A C   1 
ATOM   2296  O  O   . GLN   A 1 295 ? 30.05  62.455  22.034 1   51.68  ? 317 GLN   A O   1 
ATOM   2297  C  CB  . GLN   A 1 295 ? 32.06  64.678  20.896 1   53.19  ? 317 GLN   A CB  1 
ATOM   2298  C  CG  . GLN   A 1 295 ? 32.199 63.717  19.741 1   57.54  ? 317 GLN   A CG  1 
ATOM   2299  C  CD  . GLN   A 1 295 ? 33.613 63.597  19.244 1   62.85  ? 317 GLN   A CD  1 
ATOM   2300  O  OE1 . GLN   A 1 295 ? 34.561 64.216  19.772 1   63.28  ? 317 GLN   A OE1 1 
ATOM   2301  N  NE2 . GLN   A 1 295 ? 33.773 62.794  18.188 1   64.25  ? 317 GLN   A NE2 1 
ATOM   2302  N  N   . ARG   A 1 296 ? 30.611 63.826  23.732 1   51.07  ? 318 ARG   A N   1 
ATOM   2303  C  CA  . ARG   A 1 296 ? 30.34  62.837  24.765 1   51.3   ? 318 ARG   A CA  1 
ATOM   2304  C  C   . ARG   A 1 296 ? 28.831 62.696  25.009 1   50.57  ? 318 ARG   A C   1 
ATOM   2305  O  O   . ARG   A 1 296 ? 28.376 61.61   25.347 1   50.29  ? 318 ARG   A O   1 
ATOM   2306  C  CB  . ARG   A 1 296 ? 31.048 63.213  26.068 1   53.47  ? 318 ARG   A CB  1 
ATOM   2307  C  CG  . ARG   A 1 296 ? 32.514 62.802  26.122 1   57.74  ? 318 ARG   A CG  1 
ATOM   2308  C  CD  . ARG   A 1 296 ? 33.114 63.176  27.473 1   61.96  ? 318 ARG   A CD  1 
ATOM   2309  N  NE  . ARG   A 1 296 ? 34.563 62.979  27.511 1   65.93  ? 318 ARG   A NE  1 
ATOM   2310  C  CZ  . ARG   A 1 296 ? 35.17  61.951  28.097 1   69.81  ? 318 ARG   A CZ  1 
ATOM   2311  N  NH1 . ARG   A 1 296 ? 34.457 61      28.693 1   69.85  ? 318 ARG   A NH1 1 
ATOM   2312  N  NH2 . ARG   A 1 296 ? 36.492 61.85   28.07  1   70.57  ? 318 ARG   A NH2 1 
ATOM   2313  N  N   . MET   A 1 297 ? 28.06  63.781  24.841 1   50.54  ? 319 MET   A N   1 
ATOM   2314  C  CA  . MET   A 1 297 ? 26.61  63.776  25.056 1   51.46  ? 319 MET   A CA  1 
ATOM   2315  C  C   . MET   A 1 297 ? 25.799 63.298  23.857 1   52.24  ? 319 MET   A C   1 
ATOM   2316  O  O   . MET   A 1 297 ? 24.851 62.538  24.031 1   52.45  ? 319 MET   A O   1 
ATOM   2317  C  CB  . MET   A 1 297 ? 26.1   65.185  25.417 1   52.1   ? 319 MET   A CB  1 
ATOM   2318  C  CG  . MET   A 1 297 ? 26.551 65.679  26.739 1   54.37  ? 319 MET   A CG  1 
ATOM   2319  S  SD  . MET   A 1 297 ? 25.815 64.824  28.148 1   55.6   ? 319 MET   A SD  1 
ATOM   2320  C  CE  . MET   A 1 297 ? 26.704 65.636  29.432 1   53.14  ? 319 MET   A CE  1 
ATOM   2321  N  N   . ILE   A 1 298 ? 26.081 63.834  22.661 1   52.52  ? 320 ILE   A N   1 
ATOM   2322  C  CA  . ILE   A 1 298 ? 25.283 63.529  21.486 1   53.08  ? 320 ILE   A CA  1 
ATOM   2323  C  C   . ILE   A 1 298 ? 26.095 63.031  20.275 1   53.66  ? 320 ILE   A C   1 
ATOM   2324  O  O   . ILE   A 1 298 ? 25.515 62.84   19.218 1   53.81  ? 320 ILE   A O   1 
ATOM   2325  C  CB  . ILE   A 1 298 ? 24.416 64.775  21.127 1   53.58  ? 320 ILE   A CB  1 
ATOM   2326  C  CG1 . ILE   A 1 298 ? 25.306 66      20.837 1   54.99  ? 320 ILE   A CG1 1 
ATOM   2327  C  CG2 . ILE   A 1 298 ? 23.379 65.081  22.222 1   53.79  ? 320 ILE   A CG2 1 
ATOM   2328  C  CD1 . ILE   A 1 298 ? 24.603 67.333  20.632 1   56.48  ? 320 ILE   A CD1 1 
ATOM   2329  N  N   . GLY   A 1 299 ? 27.402 62.829  20.421 1   53.93  ? 321 GLY   A N   1 
ATOM   2330  C  CA  . GLY   A 1 299 ? 28.263 62.401  19.317 1   54.41  ? 321 GLY   A CA  1 
ATOM   2331  C  C   . GLY   A 1 299 ? 28.412 63.454  18.233 1   54.61  ? 321 GLY   A C   1 
ATOM   2332  O  O   . GLY   A 1 299 ? 28.125 64.629  18.478 1   54.73  ? 321 GLY   A O   1 
ATOM   2333  N  N   . SER   A 1 300 ? 28.853 63.065  17.018 1   54.63  ? 322 SER   A N   1 
ATOM   2334  C  CA  . SER   A 1 300 ? 28.953 64.036  15.91  1   54.99  ? 322 SER   A CA  1 
ATOM   2335  C  C   . SER   A 1 300 ? 27.545 64.448  15.4   1   55.05  ? 322 SER   A C   1 
ATOM   2336  O  O   . SER   A 1 300 ? 27.319 65.593  14.994 1   55.32  ? 322 SER   A O   1 
ATOM   2337  C  CB  . SER   A 1 300 ? 29.824 63.497  14.78  1   56.67  ? 322 SER   A CB  1 
ATOM   2338  O  OG  . SER   A 1 300 ? 29.501 62.158  14.445 1   60.2   ? 322 SER   A OG  1 
ATOM   2339  N  N   . GLN   A 1 301 ? 26.585 63.518  15.49  1   54.63  ? 323 GLN   A N   1 
ATOM   2340  C  CA  . GLN   A 1 301 ? 25.193 63.745  15.121 1   54.37  ? 323 GLN   A CA  1 
ATOM   2341  C  C   . GLN   A 1 301 ? 24.253 62.858  15.947 1   53.42  ? 323 GLN   A C   1 
ATOM   2342  O  O   . GLN   A 1 301 ? 24.646 61.794  16.413 1   53.38  ? 323 GLN   A O   1 
ATOM   2343  C  CB  . GLN   A 1 301 ? 24.983 63.5    13.627 1   56.09  ? 323 GLN   A CB  1 
ATOM   2344  C  CG  . GLN   A 1 301 ? 25.478 62.15   13.155 1   58.78  ? 323 GLN   A CG  1 
ATOM   2345  C  CD  . GLN   A 1 301 ? 25.555 62.12   11.658 1   62.11  ? 323 GLN   A CD  1 
ATOM   2346  O  OE1 . GLN   A 1 301 ? 24.546 61.957  10.957 1   63.5   ? 323 GLN   A OE1 1 
ATOM   2347  N  NE2 . GLN   A 1 301 ? 26.761 62.288  11.144 1   62.06  ? 323 GLN   A NE2 1 
ATOM   2348  N  N   . GLN   A 1 302 ? 23.014 63.295  16.119 1   52.56  ? 324 GLN   A N   1 
ATOM   2349  C  CA  . GLN   A 1 302 ? 22.025 62.566  16.905 1   52.45  ? 324 GLN   A CA  1 
ATOM   2350  C  C   . GLN   A 1 302 ? 20.6   62.96   16.418 1   53.58  ? 324 GLN   A C   1 
ATOM   2351  O  O   . GLN   A 1 302 ? 20.448 63.851  15.581 1   53.73  ? 324 GLN   A O   1 
ATOM   2352  C  CB  . GLN   A 1 302 ? 22.249 62.866  18.415 1   52.02  ? 324 GLN   A CB  1 
ATOM   2353  C  CG  . GLN   A 1 302 ? 21.489 61.996  19.424 1   53.17  ? 324 GLN   A CG  1 
ATOM   2354  C  CD  . GLN   A 1 302 ? 21.595 60.499  19.255 1   55.06  ? 324 GLN   A CD  1 
ATOM   2355  O  OE1 . GLN   A 1 302 ? 22.653 59.902  19.427 1   56.9   ? 324 GLN   A OE1 1 
ATOM   2356  N  NE2 . GLN   A 1 302 ? 20.48  59.86   18.939 1   54.44  ? 324 GLN   A NE2 1 
ATOM   2357  N  N   . LEU   A 1 303 ? 19.571 62.268  16.904 1   54.22  ? 325 LEU   A N   1 
ATOM   2358  C  CA  . LEU   A 1 303 ? 18.188 62.508  16.549 1   55.61  ? 325 LEU   A CA  1 
ATOM   2359  C  C   . LEU   A 1 303 ? 17.781 63.934  16.909 1   56.56  ? 325 LEU   A C   1 
ATOM   2360  O  O   . LEU   A 1 303 ? 17.691 64.273  18.077 1   56.45  ? 325 LEU   A O   1 
ATOM   2361  C  CB  . LEU   A 1 303 ? 17.31  61.49   17.286 1   56.11  ? 325 LEU   A CB  1 
ATOM   2362  C  CG  . LEU   A 1 303 ? 15.925 61.294  16.717 1   57.64  ? 325 LEU   A CG  1 
ATOM   2363  C  CD1 . LEU   A 1 303 ? 15.992 60.684  15.327 1   58.62  ? 325 LEU   A CD1 1 
ATOM   2364  C  CD2 . LEU   A 1 303 ? 15.1   60.452  17.635 1   58.08  ? 325 LEU   A CD2 1 
ATOM   2365  N  N   . GLY   A 1 304 ? 17.569 64.756  15.896 1   57.46  ? 326 GLY   A N   1 
ATOM   2366  C  CA  . GLY   A 1 304 ? 17.211 66.159  16.065 1   59.07  ? 326 GLY   A CA  1 
ATOM   2367  C  C   . GLY   A 1 304 ? 18.279 67.111  15.557 1   61.1   ? 326 GLY   A C   1 
ATOM   2368  O  O   . GLY   A 1 304 ? 17.992 68.28   15.283 1   61.54  ? 326 GLY   A O   1 
ATOM   2369  N  N   . THR   A 1 305 ? 19.528 66.614  15.415 1   61.98  ? 327 THR   A N   1 
ATOM   2370  C  CA  . THR   A 1 305 ? 20.682 67.386  14.946 1   62.83  ? 327 THR   A CA  1 
ATOM   2371  C  C   . THR   A 1 305 ? 20.603 67.697  13.428 1   63.46  ? 327 THR   A C   1 
ATOM   2372  O  O   . THR   A 1 305 ? 21.043 68.767  12.984 1   63.63  ? 327 THR   A O   1 
ATOM   2373  C  CB  . THR   A 1 305 ? 21.993 66.674  15.34  1   64.25  ? 327 THR   A CB  1 
ATOM   2374  O  OG1 . THR   A 1 305 ? 21.913 66.261  16.703 1   65.16  ? 327 THR   A OG1 1 
ATOM   2375  C  CG2 . THR   A 1 305 ? 23.204 67.563  15.19  1   65     ? 327 THR   A CG2 1 
ATOM   2376  N  N   . GLY   A 1 306 ? 20.015 66.779  12.661 1   63.35  ? 328 GLY   A N   1 
ATOM   2377  C  CA  . GLY   A 1 306 ? 19.904 66.941  11.216 1   63.7   ? 328 GLY   A CA  1 
ATOM   2378  C  C   . GLY   A 1 306 ? 21.265 66.83   10.562 1   64     ? 328 GLY   A C   1 
ATOM   2379  O  O   . GLY   A 1 306 ? 21.643 67.667  9.744  1   63.9   ? 328 GLY   A O   1 
ATOM   2380  N  N   . GLY   A 1 307 ? 22.023 65.82   10.968 1   64.37  ? 329 GLY   A N   1 
ATOM   2381  C  CA  . GLY   A 1 307 ? 23.381 65.619  10.473 1   65.14  ? 329 GLY   A CA  1 
ATOM   2382  C  C   . GLY   A 1 307 ? 24.446 66.127  11.432 1   65.42  ? 329 GLY   A C   1 
ATOM   2383  O  O   . GLY   A 1 307 ? 24.134 66.516  12.555 1   65.63  ? 329 GLY   A O   1 
ATOM   2384  N  N   . SER   A 1 308 ? 25.716 66.13   11.009 1   65.26  ? 330 SER   A N   1 
ATOM   2385  C  CA  . SER   A 1 308 ? 26.813 66.581  11.865 1   65.72  ? 330 SER   A CA  1 
ATOM   2386  C  C   . SER   A 1 308 ? 27.198 68.045  11.624 1   66.1   ? 330 SER   A C   1 
ATOM   2387  O  O   . SER   A 1 308 ? 28.331 68.424  11.908 1   65.76  ? 330 SER   A O   1 
ATOM   2388  C  CB  . SER   A 1 308 ? 28.032 65.678  11.681 1   67.09  ? 330 SER   A CB  1 
ATOM   2389  O  OG  . SER   A 1 308 ? 28.498 65.663  10.339 1   69.02  ? 330 SER   A OG  1 
ATOM   2390  N  N   . SER   A 1 309 ? 26.261 68.866  11.111 1   66.37  ? 331 SER   A N   1 
ATOM   2391  C  CA  . SER   A 1 309 ? 26.509 70.273  10.774 1   66.85  ? 331 SER   A CA  1 
ATOM   2392  C  C   . SER   A 1 309 ? 26.844 71.164  11.975 1   66.42  ? 331 SER   A C   1 
ATOM   2393  O  O   . SER   A 1 309 ? 27.763 71.985  11.886 1   66.72  ? 331 SER   A O   1 
ATOM   2394  C  CB  . SER   A 1 309 ? 25.355 70.864  9.962  1   68.78  ? 331 SER   A CB  1 
ATOM   2395  O  OG  . SER   A 1 309 ? 24.073 70.373  10.324 1   71.77  ? 331 SER   A OG  1 
ATOM   2396  N  N   . GLY   A 1 310 ? 26.106 71      13.071 1   65.45  ? 332 GLY   A N   1 
ATOM   2397  C  CA  . GLY   A 1 310 ? 26.324 71.781  14.283 1   64.68  ? 332 GLY   A CA  1 
ATOM   2398  C  C   . GLY   A 1 310 ? 27.642 71.45   14.955 1   63.69  ? 332 GLY   A C   1 
ATOM   2399  O  O   . GLY   A 1 310 ? 28.351 72.351  15.406 1   63.8   ? 332 GLY   A O   1 
ATOM   2400  N  N   . TYR   A 1 311 ? 27.981 70.15   15.016 1   62.72  ? 333 TYR   A N   1 
ATOM   2401  C  CA  . TYR   A 1 311 ? 29.227 69.646  15.593 1   62.36  ? 333 TYR   A CA  1 
ATOM   2402  C  C   . TYR   A 1 311 ? 30.427 70.118  14.767 1   61.34  ? 333 TYR   A C   1 
ATOM   2403  O  O   . TYR   A 1 311 ? 31.424 70.574  15.331 1   61.29  ? 333 TYR   A O   1 
ATOM   2404  C  CB  . TYR   A 1 311 ? 29.177 68.109  15.674 1   62.82  ? 333 TYR   A CB  1 
ATOM   2405  C  CG  . TYR   A 1 311 ? 30.517 67.436  15.891 1   64.1   ? 333 TYR   A CG  1 
ATOM   2406  C  CD1 . TYR   A 1 311 ? 31.108 67.404  17.147 1   65.16  ? 333 TYR   A CD1 1 
ATOM   2407  C  CD2 . TYR   A 1 311 ? 31.186 66.822  14.841 1   65.11  ? 333 TYR   A CD2 1 
ATOM   2408  C  CE1 . TYR   A 1 311 ? 32.338 66.784  17.352 1   66.19  ? 333 TYR   A CE1 1 
ATOM   2409  C  CE2 . TYR   A 1 311 ? 32.41  66.191  15.035 1   66.14  ? 333 TYR   A CE2 1 
ATOM   2410  C  CZ  . TYR   A 1 311 ? 32.981 66.167  16.294 1   67.26  ? 333 TYR   A CZ  1 
ATOM   2411  O  OH  . TYR   A 1 311 ? 34.201 65.555  16.468 1   68.95  ? 333 TYR   A OH  1 
ATOM   2412  N  N   . GLN   A 1 312 ? 30.323 70.018  13.43  1   60.61  ? 334 GLN   A N   1 
ATOM   2413  C  CA  . GLN   A 1 312 ? 31.368 70.464  12.506 1   60.21  ? 334 GLN   A CA  1 
ATOM   2414  C  C   . GLN   A 1 312 ? 31.574 71.966  12.553 1   60.02  ? 334 GLN   A C   1 
ATOM   2415  O  O   . GLN   A 1 312 ? 32.698 72.421  12.342 1   60.43  ? 334 GLN   A O   1 
ATOM   2416  C  CB  . GLN   A 1 312 ? 31.107 69.993  11.065 1   60.9   ? 334 GLN   A CB  1 
ATOM   2417  C  CG  . GLN   A 1 312 ? 31.454 68.523  10.814 1   62.89  ? 334 GLN   A CG  1 
ATOM   2418  C  CD  . GLN   A 1 312 ? 32.872 68.14   11.2   1   66.36  ? 334 GLN   A CD  1 
ATOM   2419  O  OE1 . GLN   A 1 312 ? 33.108 67.072  11.775 1   67.74  ? 334 GLN   A OE1 1 
ATOM   2420  N  NE2 . GLN   A 1 312 ? 33.854 68.99   10.891 1   66.63  ? 334 GLN   A NE2 1 
ATOM   2421  N  N   . TYR   A 1 313 ? 30.509 72.742  12.851 1   59.45  ? 335 TYR   A N   1 
ATOM   2422  C  CA  . TYR   A 1 313 ? 30.623 74.186  13.012 1   59.77  ? 335 TYR   A CA  1 
ATOM   2423  C  C   . TYR   A 1 313 ? 31.481 74.451  14.252 1   59.78  ? 335 TYR   A C   1 
ATOM   2424  O  O   . TYR   A 1 313 ? 32.394 75.278  14.189 1   60.2   ? 335 TYR   A O   1 
ATOM   2425  C  CB  . TYR   A 1 313 ? 29.238 74.867  13.157 1   60.18  ? 335 TYR   A CB  1 
ATOM   2426  C  CG  . TYR   A 1 313 ? 29.324 76.243  13.792 1   61.65  ? 335 TYR   A CG  1 
ATOM   2427  C  CD1 . TYR   A 1 313 ? 29.846 77.321  13.092 1   63     ? 335 TYR   A CD1 1 
ATOM   2428  C  CD2 . TYR   A 1 313 ? 29.009 76.434  15.131 1   62.82  ? 335 TYR   A CD2 1 
ATOM   2429  C  CE1 . TYR   A 1 313 ? 29.993 78.57   13.688 1   64.18  ? 335 TYR   A CE1 1 
ATOM   2430  C  CE2 . TYR   A 1 313 ? 29.184 77.669  15.749 1   64.02  ? 335 TYR   A CE2 1 
ATOM   2431  C  CZ  . TYR   A 1 313 ? 29.66  78.741  15.019 1   65.12  ? 335 TYR   A CZ  1 
ATOM   2432  O  OH  . TYR   A 1 313 ? 29.807 79.975  15.61  1   66.73  ? 335 TYR   A OH  1 
ATOM   2433  N  N   . LEU   A 1 314 ? 31.191 73.749  15.37  1   58.9   ? 336 LEU   A N   1 
ATOM   2434  C  CA  . LEU   A 1 314 ? 31.93  73.924  16.61  1   58.79  ? 336 LEU   A CA  1 
ATOM   2435  C  C   . LEU   A 1 314 ? 33.409 73.578  16.427 1   59.25  ? 336 LEU   A C   1 
ATOM   2436  O  O   . LEU   A 1 314 ? 34.261 74.232  17.02  1   59.75  ? 336 LEU   A O   1 
ATOM   2437  C  CB  . LEU   A 1 314 ? 31.316 73.108  17.753 1   58.62  ? 336 LEU   A CB  1 
ATOM   2438  C  CG  . LEU   A 1 314 ? 29.897 73.448  18.184 1   59.42  ? 336 LEU   A CG  1 
ATOM   2439  C  CD1 . LEU   A 1 314 ? 29.451 72.518  19.267 1   59.76  ? 336 LEU   A CD1 1 
ATOM   2440  C  CD2 . LEU   A 1 314 ? 29.783 74.888  18.662 1   59.81  ? 336 LEU   A CD2 1 
ATOM   2441  N  N   . ARG   A 1 315 ? 33.724 72.588  15.58  1   58.96  ? 337 ARG   A N   1 
ATOM   2442  C  CA  . ARG   A 1 315 ? 35.117 72.228  15.307 1   58.82  ? 337 ARG   A CA  1 
ATOM   2443  C  C   . ARG   A 1 315 ? 35.849 73.284  14.473 1   57.63  ? 337 ARG   A C   1 
ATOM   2444  O  O   . ARG   A 1 315 ? 37.069 73.416  14.577 1   57.73  ? 337 ARG   A O   1 
ATOM   2445  C  CB  . ARG   A 1 315 ? 35.202 70.86   14.641 1   60.8   ? 337 ARG   A CB  1 
ATOM   2446  C  CG  . ARG   A 1 315 ? 35.008 69.731  15.623 1   65.56  ? 337 ARG   A CG  1 
ATOM   2447  C  CD  . ARG   A 1 315 ? 35.26  68.409  14.958 1   71.17  ? 337 ARG   A CD  1 
ATOM   2448  N  NE  . ARG   A 1 315 ? 36.684 68.098  14.828 1   76.63  ? 337 ARG   A NE  1 
ATOM   2449  C  CZ  . ARG   A 1 315 ? 37.265 67.702  13.695 1   80.3   ? 337 ARG   A CZ  1 
ATOM   2450  N  NH1 . ARG   A 1 315 ? 36.551 67.587  12.579 1   80.25  ? 337 ARG   A NH1 1 
ATOM   2451  N  NH2 . ARG   A 1 315 ? 38.566 67.429  13.668 1   80.52  ? 337 ARG   A NH2 1 
ATOM   2452  N  N   . SER   A 1 316 ? 35.112 74.045  13.669 1   56.42  ? 338 SER   A N   1 
ATOM   2453  C  CA  . SER   A 1 316 ? 35.696 75.115  12.877 1   56.49  ? 338 SER   A CA  1 
ATOM   2454  C  C   . SER   A 1 316 ? 35.983 76.383  13.729 1   55.85  ? 338 SER   A C   1 
ATOM   2455  O  O   . SER   A 1 316 ? 36.787 77.23   13.326 1   55.8   ? 338 SER   A O   1 
ATOM   2456  C  CB  . SER   A 1 316 ? 34.819 75.428  11.668 1   58.63  ? 338 SER   A CB  1 
ATOM   2457  O  OG  . SER   A 1 316 ? 33.604 76.059  12.038 1   62.41  ? 338 SER   A OG  1 
ATOM   2458  N  N   . THR   A 1 317 ? 35.334 76.512  14.91  1   54.86  ? 339 THR   A N   1 
ATOM   2459  C  CA  . THR   A 1 317 ? 35.597 77.624  15.826 1   53.79  ? 339 THR   A CA  1 
ATOM   2460  C  C   . THR   A 1 317 ? 36.93  77.453  16.585 1   53.67  ? 339 THR   A C   1 
ATOM   2461  O  O   . THR   A 1 317 ? 37.389 78.399  17.222 1   53.38  ? 339 THR   A O   1 
ATOM   2462  C  CB  . THR   A 1 317 ? 34.421 77.875  16.756 1   53.54  ? 339 THR   A CB  1 
ATOM   2463  O  OG1 . THR   A 1 317 ? 34.244 76.75   17.608 1   53.69  ? 339 THR   A OG1 1 
ATOM   2464  C  CG2 . THR   A 1 317 ? 33.152 78.154  16.005 1   53.72  ? 339 THR   A CG2 1 
ATOM   2465  N  N   . LEU   A 1 318 ? 37.564 76.272  16.492 1   53.99  ? 340 LEU   A N   1 
ATOM   2466  C  CA  . LEU   A 1 318 ? 38.86  76.009  17.115 1   55.44  ? 340 LEU   A CA  1 
ATOM   2467  C  C   . LEU   A 1 318 ? 40.054 76.546  16.291 1   57.63  ? 340 LEU   A C   1 
ATOM   2468  O  O   . LEU   A 1 318 ? 41.183 76.571  16.789 1   57.72  ? 340 LEU   A O   1 
ATOM   2469  C  CB  . LEU   A 1 318 ? 39.025 74.501  17.367 1   55.21  ? 340 LEU   A CB  1 
ATOM   2470  C  CG  . LEU   A 1 318 ? 37.91  73.828  18.152 1   55.79  ? 340 LEU   A CG  1 
ATOM   2471  C  CD1 . LEU   A 1 318 ? 38.14  72.354  18.259 1   56.01  ? 340 LEU   A CD1 1 
ATOM   2472  C  CD2 . LEU   A 1 318 ? 37.788 74.419  19.516 1   56.31  ? 340 LEU   A CD2 1 
ATOM   2473  N  N   . SER   A 1 319 ? 39.801 76.975  15.03  1   59.24  ? 341 SER   A N   1 
ATOM   2474  C  CA  . SER   A 1 319 ? 40.802 77.512  14.103 1   60.66  ? 341 SER   A CA  1 
ATOM   2475  C  C   . SER   A 1 319 ? 41.316 78.886  14.532 1   61.75  ? 341 SER   A C   1 
ATOM   2476  O  O   . SER   A 1 319 ? 40.667 79.591  15.318 1   62.37  ? 341 SER   A O   1 
ATOM   2477  C  CB  . SER   A 1 319 ? 40.222 77.596  12.692 1   62.23  ? 341 SER   A CB  1 
ATOM   2478  O  OG  . SER   A 1 319 ? 39.25  78.623  12.57  1   64.96  ? 341 SER   A OG  1 
ATOM   2479  N  N   . ASP   A 1 320 ? 42.469 79.285  13.984 1   61.69  ? 342 ASP   A N   1 
ATOM   2480  C  CA  . ASP   A 1 320 ? 43.049 80.585  14.287 1   62.22  ? 342 ASP   A CA  1 
ATOM   2481  C  C   . ASP   A 1 320 ? 42.235 81.765  13.711 1   62.14  ? 342 ASP   A C   1 
ATOM   2482  O  O   . ASP   A 1 320 ? 42.487 82.908  14.09  1   62.15  ? 342 ASP   A O   1 
ATOM   2483  C  CB  . ASP   A 1 320 ? 44.524 80.623  13.873 1   64.69  ? 342 ASP   A CB  1 
ATOM   2484  C  CG  . ASP   A 1 320 ? 45.418 79.732  14.732 1   71.55  ? 342 ASP   A CG  1 
ATOM   2485  O  OD1 . ASP   A 1 320 ? 44.974 79.319  15.834 1   72.69  ? 342 ASP   A OD1 1 
ATOM   2486  O  OD2 . ASP   A 1 320 ? 46.561 79.448  14.305 1   74.71  ? 342 ASP   A OD2 1 
ATOM   2487  N  N   . ARG   A 1 321 ? 41.211 81.486  12.871 1   61.86  ? 343 ARG   A N   1 
ATOM   2488  C  CA  . ARG   A 1 321 ? 40.275 82.501  12.38  1   62.14  ? 343 ARG   A CA  1 
ATOM   2489  C  C   . ARG   A 1 321 ? 39.443 83.074  13.544 1   61.22  ? 343 ARG   A C   1 
ATOM   2490  O  O   . ARG   A 1 321 ? 38.864 84.153  13.402 1   61.78  ? 343 ARG   A O   1 
ATOM   2491  C  CB  . ARG   A 1 321 ? 39.294 81.901  11.36  1   64.84  ? 343 ARG   A CB  1 
ATOM   2492  C  CG  . ARG   A 1 321 ? 39.951 81.065  10.276 1   70.78  ? 343 ARG   A CG  1 
ATOM   2493  C  CD  . ARG   A 1 321 ? 38.923 80.349  9.416  1   76.1   ? 343 ARG   A CD  1 
ATOM   2494  N  NE  . ARG   A 1 321 ? 38.253 81.26   8.483  1   80.98  ? 343 ARG   A NE  1 
ATOM   2495  C  CZ  . ARG   A 1 321 ? 36.954 81.548  8.516  1   84.69  ? 343 ARG   A CZ  1 
ATOM   2496  N  NH1 . ARG   A 1 321 ? 36.17  81.009  9.443  1   85.33  ? 343 ARG   A NH1 1 
ATOM   2497  N  NH2 . ARG   A 1 321 ? 36.431 82.383  7.626  1   84.45  ? 343 ARG   A NH2 1 
ATOM   2498  N  N   . TYR   A 1 322 ? 39.351 82.345  14.681 1   59.54  ? 344 TYR   A N   1 
ATOM   2499  C  CA  . TYR   A 1 322 ? 38.596 82.777  15.846 1   58.18  ? 344 TYR   A CA  1 
ATOM   2500  C  C   . TYR   A 1 322 ? 39.481 83.417  16.944 1   56.73  ? 344 TYR   A C   1 
ATOM   2501  O  O   . TYR   A 1 322 ? 38.945 84.063  17.841 1   56.81  ? 344 TYR   A O   1 
ATOM   2502  C  CB  . TYR   A 1 322 ? 37.733 81.631  16.368 1   57.95  ? 344 TYR   A CB  1 
ATOM   2503  C  CG  . TYR   A 1 322 ? 36.445 81.476  15.582 1   58.42  ? 344 TYR   A CG  1 
ATOM   2504  C  CD1 . TYR   A 1 322 ? 36.425 80.817  14.36  1   59.01  ? 344 TYR   A CD1 1 
ATOM   2505  C  CD2 . TYR   A 1 322 ? 35.259 82.041  16.034 1   59.35  ? 344 TYR   A CD2 1 
ATOM   2506  C  CE1 . TYR   A 1 322 ? 35.246 80.675  13.631 1   59.76  ? 344 TYR   A CE1 1 
ATOM   2507  C  CE2 . TYR   A 1 322 ? 34.076 81.914  15.312 1   60.18  ? 344 TYR   A CE2 1 
ATOM   2508  C  CZ  . TYR   A 1 322 ? 34.072 81.225  14.111 1   60.72  ? 344 TYR   A CZ  1 
ATOM   2509  O  OH  . TYR   A 1 322 ? 32.901 81.087  13.4   1   61.49  ? 344 TYR   A OH  1 
ATOM   2510  N  N   . LYS   A 1 323 ? 40.821 83.3    16.833 1   55.32  ? 345 LYS   A N   1 
ATOM   2511  C  CA  . LYS   A 1 323 ? 41.766 83.943  17.743 1   54.51  ? 345 LYS   A CA  1 
ATOM   2512  C  C   . LYS   A 1 323 ? 41.853 85.423  17.365 1   54.05  ? 345 LYS   A C   1 
ATOM   2513  O  O   . LYS   A 1 323 ? 42.2   85.744  16.238 1   54.99  ? 345 LYS   A O   1 
ATOM   2514  C  CB  . LYS   A 1 323 ? 43.151 83.289  17.638 1   55.71  ? 345 LYS   A CB  1 
ATOM   2515  C  CG  . LYS   A 1 323 ? 43.312 82.056  18.516 1   59.18  ? 345 LYS   A CG  1 
ATOM   2516  C  CD  . LYS   A 1 323 ? 44.376 82.263  19.581 1   62.99  ? 345 LYS   A CD  1 
ATOM   2517  C  CE  . LYS   A 1 323 ? 44.215 81.328  20.759 1   66.12  ? 345 LYS   A CE  1 
ATOM   2518  N  NZ  . LYS   A 1 323 ? 44.726 79.971  20.476 1   68.27  ? 345 LYS   A NZ  1 
ATOM   2519  N  N   . VAL   A 1 324 ? 41.497 86.315  18.281 1   52.6   ? 346 VAL   A N   1 
ATOM   2520  C  CA  . VAL   A 1 324 ? 41.487 87.759  18.075 1   51.43  ? 346 VAL   A CA  1 
ATOM   2521  C  C   . VAL   A 1 324 ? 42.889 88.383  18.002 1   50.5   ? 346 VAL   A C   1 
ATOM   2522  O  O   . VAL   A 1 324 ? 43.177 89.121  17.071 1   50.67  ? 346 VAL   A O   1 
ATOM   2523  C  CB  . VAL   A 1 324 ? 40.637 88.439  19.172 1   51.71  ? 346 VAL   A CB  1 
ATOM   2524  C  CG1 . VAL   A 1 324 ? 40.607 89.947  18.987 1   52.25  ? 346 VAL   A CG1 1 
ATOM   2525  C  CG2 . VAL   A 1 324 ? 39.234 87.861  19.217 1   51.83  ? 346 VAL   A CG2 1 
ATOM   2526  N  N   . PHE   A 1 325 ? 43.749 88.113  18.987 1   49.57  ? 347 PHE   A N   1 
ATOM   2527  C  CA  . PHE   A 1 325 ? 45.09  88.69   19.066 1   48.83  ? 347 PHE   A CA  1 
ATOM   2528  C  C   . PHE   A 1 325 ? 46.137 87.732  18.544 1   48.12  ? 347 PHE   A C   1 
ATOM   2529  O  O   . PHE   A 1 325 ? 47.191 87.542  19.146 1   47.95  ? 347 PHE   A O   1 
ATOM   2530  C  CB  . PHE   A 1 325 ? 45.405 89.158  20.499 1   48.19  ? 347 PHE   A CB  1 
ATOM   2531  C  CG  . PHE   A 1 325 ? 44.471 90.246  20.961 1   48.12  ? 347 PHE   A CG  1 
ATOM   2532  C  CD1 . PHE   A 1 325 ? 44.74  91.576  20.683 1   48.35  ? 347 PHE   A CD1 1 
ATOM   2533  C  CD2 . PHE   A 1 325 ? 43.302 89.936  21.64  1   49     ? 347 PHE   A CD2 1 
ATOM   2534  C  CE1 . PHE   A 1 325 ? 43.867 92.577  21.085 1   49.16  ? 347 PHE   A CE1 1 
ATOM   2535  C  CE2 . PHE   A 1 325 ? 42.436 90.938  22.055 1   49.73  ? 347 PHE   A CE2 1 
ATOM   2536  C  CZ  . PHE   A 1 325 ? 42.728 92.254  21.782 1   49.5   ? 347 PHE   A CZ  1 
ATOM   2537  N  N   . LEU   A 1 326 ? 45.839 87.177  17.381 1   47.74  ? 348 LEU   A N   1 
ATOM   2538  C  CA  . LEU   A 1 326 ? 46.647 86.232  16.628 1   47.81  ? 348 LEU   A CA  1 
ATOM   2539  C  C   . LEU   A 1 326 ? 48.091 86.711  16.38  1   47.04  ? 348 LEU   A C   1 
ATOM   2540  O  O   . LEU   A 1 326 ? 49.023 85.9    16.395 1   47.61  ? 348 LEU   A O   1 
ATOM   2541  C  CB  . LEU   A 1 326 ? 45.93  86.008  15.294 1   48.1   ? 348 LEU   A CB  1 
ATOM   2542  C  CG  . LEU   A 1 326 ? 46.36  84.804  14.497 1   49.28  ? 348 LEU   A CG  1 
ATOM   2543  C  CD1 . LEU   A 1 326 ? 46.024 83.547  15.229 1   49.72  ? 348 LEU   A CD1 1 
ATOM   2544  C  CD2 . LEU   A 1 326 ? 45.727 84.826  13.118 1   49.62  ? 348 LEU   A CD2 1 
ATOM   2545  N  N   . ASP   A 1 327 ? 48.265 88.02   16.152 1   45.68  ? 349 ASP   A N   1 
ATOM   2546  C  CA  . ASP   A 1 327 ? 49.561 88.641  15.897 1   45.41  ? 349 ASP   A CA  1 
ATOM   2547  C  C   . ASP   A 1 327 ? 50.502 88.571  17.069 1   45.19  ? 349 ASP   A C   1 
ATOM   2548  O  O   . ASP   A 1 327 ? 51.713 88.449  16.878 1   45.71  ? 349 ASP   A O   1 
ATOM   2549  C  CB  . ASP   A 1 327 ? 49.388 90.111  15.535 1   46.8   ? 349 ASP   A CB  1 
ATOM   2550  C  CG  . ASP   A 1 327 ? 48.553 90.3    14.306 1   51.64  ? 349 ASP   A CG  1 
ATOM   2551  O  OD1 . ASP   A 1 327 ? 47.34  89.96   14.351 1   52.86  ? 349 ASP   A OD1 1 
ATOM   2552  O  OD2 . ASP   A 1 327 ? 49.093 90.799  13.299 1   53.37  ? 349 ASP   A OD2 1 
ATOM   2553  N  N   . LEU   A 1 328 ? 49.957 88.706  18.277 1   44.42  ? 350 LEU   A N   1 
ATOM   2554  C  CA  . LEU   A 1 328 ? 50.74  88.715  19.494 1   44.39  ? 350 LEU   A CA  1 
ATOM   2555  C  C   . LEU   A 1 328 ? 51.433 87.391  19.753 1   44.83  ? 350 LEU   A C   1 
ATOM   2556  O  O   . LEU   A 1 328 ? 52.523 87.382  20.322 1   45.01  ? 350 LEU   A O   1 
ATOM   2557  C  CB  . LEU   A 1 328 ? 49.843 89.072  20.679 1   44.56  ? 350 LEU   A CB  1 
ATOM   2558  C  CG  . LEU   A 1 328 ? 49.24  90.458  20.709 1   45.7   ? 350 LEU   A CG  1 
ATOM   2559  C  CD1 . LEU   A 1 328 ? 48.425 90.642  21.981 1   46.2   ? 350 LEU   A CD1 1 
ATOM   2560  C  CD2 . LEU   A 1 328 ? 50.321 91.538  20.598 1   45.81  ? 350 LEU   A CD2 1 
ATOM   2561  N  N   . PHE   A 1 329 ? 50.813 86.274  19.344 1   44.92  ? 351 PHE   A N   1 
ATOM   2562  C  CA  . PHE   A 1 329 ? 51.366 84.936  19.56  1   45.27  ? 351 PHE   A CA  1 
ATOM   2563  C  C   . PHE   A 1 329 ? 52.655 84.689  18.786 1   46.44  ? 351 PHE   A C   1 
ATOM   2564  O  O   . PHE   A 1 329 ? 53.542 83.981  19.277 1   47.04  ? 351 PHE   A O   1 
ATOM   2565  C  CB  . PHE   A 1 329 ? 50.317 83.861  19.227 1   44.61  ? 351 PHE   A CB  1 
ATOM   2566  C  CG  . PHE   A 1 329 ? 49.197 83.78   20.241 1   44.48  ? 351 PHE   A CG  1 
ATOM   2567  C  CD1 . PHE   A 1 329 ? 49.295 82.949  21.346 1   44.63  ? 351 PHE   A CD1 1 
ATOM   2568  C  CD2 . PHE   A 1 329 ? 48.06  84.556  20.106 1   44.73  ? 351 PHE   A CD2 1 
ATOM   2569  C  CE1 . PHE   A 1 329 ? 48.28  82.903  22.295 1   44.65  ? 351 PHE   A CE1 1 
ATOM   2570  C  CE2 . PHE   A 1 329 ? 47.046 84.503  21.055 1   44.9   ? 351 PHE   A CE2 1 
ATOM   2571  C  CZ  . PHE   A 1 329 ? 47.16  83.668  22.133 1   44.45  ? 351 PHE   A CZ  1 
ATOM   2572  N  N   . ASN   A 1 330 ? 52.791 85.318  17.61  1   46.44  ? 352 ASN   A N   1 
ATOM   2573  C  CA  . ASN   A 1 330 ? 53.961 85.139  16.76  1   46.67  ? 352 ASN   A CA  1 
ATOM   2574  C  C   . ASN   A 1 330 ? 55.132 86.149  16.958 1   46.46  ? 352 ASN   A C   1 
ATOM   2575  O  O   . ASN   A 1 330 ? 56.192 85.949  16.365 1   46.4   ? 352 ASN   A O   1 
ATOM   2576  C  CB  . ASN   A 1 330 ? 53.51  85.152  15.317 1   48.37  ? 352 ASN   A CB  1 
ATOM   2577  C  CG  . ASN   A 1 330 ? 54.411 84.376  14.397 1   52.37  ? 352 ASN   A CG  1 
ATOM   2578  O  OD1 . ASN   A 1 330 ? 54.96  83.32   14.762 1   54.12  ? 352 ASN   A OD1 1 
ATOM   2579  N  ND2 . ASN   A 1 330 ? 54.6   84.894  13.19  1   52.95  ? 352 ASN   A ND2 1 
ATOM   2580  N  N   . LEU   A 1 331 ? 54.965 87.202  17.783 1   45.96  ? 353 LEU   A N   1 
ATOM   2581  C  CA  . LEU   A 1 331 ? 56.003 88.222  17.992 1   45.81  ? 353 LEU   A CA  1 
ATOM   2582  C  C   . LEU   A 1 331 ? 57.411 87.707  18.322 1   46.19  ? 353 LEU   A C   1 
ATOM   2583  O  O   . LEU   A 1 331 ? 58.383 88.418  18.078 1   46.4   ? 353 LEU   A O   1 
ATOM   2584  C  CB  . LEU   A 1 331 ? 55.58  89.23   19.066 1   45.89  ? 353 LEU   A CB  1 
ATOM   2585  C  CG  . LEU   A 1 331 ? 54.326 90.031  18.77  1   47.26  ? 353 LEU   A CG  1 
ATOM   2586  C  CD1 . LEU   A 1 331 ? 53.948 90.895  19.947 1   47.81  ? 353 LEU   A CD1 1 
ATOM   2587  C  CD2 . LEU   A 1 331 ? 54.497 90.877  17.558 1   47.67  ? 353 LEU   A CD2 1 
ATOM   2588  N  N   . SER   A 1 332 ? 57.537 86.498  18.883 1   46.35  ? 354 SER   A N   1 
ATOM   2589  C  CA  . SER   A 1 332 ? 58.857 85.945  19.211 1   46.56  ? 354 SER   A CA  1 
ATOM   2590  C  C   . SER   A 1 332 ? 59.681 85.521  17.989 1   46.53  ? 354 SER   A C   1 
ATOM   2591  O  O   . SER   A 1 332 ? 60.884 85.329  18.118 1   46.36  ? 354 SER   A O   1 
ATOM   2592  C  CB  . SER   A 1 332 ? 58.734 84.804  20.209 1   47.25  ? 354 SER   A CB  1 
ATOM   2593  O  OG  . SER   A 1 332 ? 58.369 85.327  21.47  1   48.39  ? 354 SER   A OG  1 
ATOM   2594  N  N   . THR   A 1 333 ? 59.036 85.393  16.813 1   46.5   ? 355 THR   A N   1 
ATOM   2595  C  CA  . THR   A 1 333 ? 59.673 85.047  15.535 1   47.01  ? 355 THR   A CA  1 
ATOM   2596  C  C   . THR   A 1 333 ? 60.656 86.137  15.085 1   47.78  ? 355 THR   A C   1 
ATOM   2597  O  O   . THR   A 1 333 ? 61.624 85.837  14.399 1   47.57  ? 355 THR   A O   1 
ATOM   2598  C  CB  . THR   A 1 333 ? 58.584 84.862  14.461 1   47.58  ? 355 THR   A CB  1 
ATOM   2599  O  OG1 . THR   A 1 333 ? 57.583 83.978  14.962 1   48.68  ? 355 THR   A OG1 1 
ATOM   2600  C  CG2 . THR   A 1 333 ? 59.123 84.344  13.138 1   47.09  ? 355 THR   A CG2 1 
ATOM   2601  N  N   . PHE   A 1 334 ? 60.399 87.397  15.478 1   48.44  ? 356 PHE   A N   1 
ATOM   2602  C  CA  . PHE   A 1 334 ? 61.174 88.586  15.112 1   49.32  ? 356 PHE   A CA  1 
ATOM   2603  C  C   . PHE   A 1 334 ? 62.268 88.979  16.106 1   49.45  ? 356 PHE   A C   1 
ATOM   2604  O  O   . PHE   A 1 334 ? 62.956 89.974  15.892 1   49.65  ? 356 PHE   A O   1 
ATOM   2605  C  CB  . PHE   A 1 334 ? 60.226 89.787  14.918 1   49.86  ? 356 PHE   A CB  1 
ATOM   2606  C  CG  . PHE   A 1 334 ? 58.96  89.452  14.168 1   51.31  ? 356 PHE   A CG  1 
ATOM   2607  C  CD1 . PHE   A 1 334 ? 59.008 89.002  12.857 1   52.5   ? 356 PHE   A CD1 1 
ATOM   2608  C  CD2 . PHE   A 1 334 ? 57.731 89.522  14.791 1   52.41  ? 356 PHE   A CD2 1 
ATOM   2609  C  CE1 . PHE   A 1 334 ? 57.849 88.645  12.187 1   53.18  ? 356 PHE   A CE1 1 
ATOM   2610  C  CE2 . PHE   A 1 334 ? 56.572 89.185  14.109 1   53.26  ? 356 PHE   A CE2 1 
ATOM   2611  C  CZ  . PHE   A 1 334 ? 56.638 88.749  12.813 1   52.96  ? 356 PHE   A CZ  1 
ATOM   2612  N  N   . LEU   A 1 335 ? 62.436 88.217  17.178 1   49.43  ? 357 LEU   A N   1 
ATOM   2613  C  CA  . LEU   A 1 335 ? 63.401 88.511  18.22  1   50.02  ? 357 LEU   A CA  1 
ATOM   2614  C  C   . LEU   A 1 335 ? 64.862 88.412  17.802 1   50.9   ? 357 LEU   A C   1 
ATOM   2615  O  O   . LEU   A 1 335 ? 65.245 87.504  17.064 1   51.3   ? 357 LEU   A O   1 
ATOM   2616  C  CB  . LEU   A 1 335 ? 63.142 87.571  19.403 1   50.07  ? 357 LEU   A CB  1 
ATOM   2617  C  CG  . LEU   A 1 335 ? 63.234 88.192  20.782 1   51.17  ? 357 LEU   A CG  1 
ATOM   2618  C  CD1 . LEU   A 1 335 ? 61.982 88.993  21.099 1   52.21  ? 357 LEU   A CD1 1 
ATOM   2619  C  CD2 . LEU   A 1 335 ? 63.423 87.133  21.816 1   51.24  ? 357 LEU   A CD2 1 
ATOM   2620  N  N   . ILE   A 1 336 ? 65.683 89.339  18.312 1   51.13  ? 358 ILE   A N   1 
ATOM   2621  C  CA  . ILE   A 1 336 ? 67.141 89.358  18.158 1   51.8   ? 358 ILE   A CA  1 
ATOM   2622  C  C   . ILE   A 1 336 ? 67.753 89.286  19.576 1   52.88  ? 358 ILE   A C   1 
ATOM   2623  O  O   . ILE   A 1 336 ? 67.079 89.65   20.546 1   53.28  ? 358 ILE   A O   1 
ATOM   2624  C  CB  . ILE   A 1 336 ? 67.657 90.573  17.342 1   52.25  ? 358 ILE   A CB  1 
ATOM   2625  C  CG1 . ILE   A 1 336 ? 66.976 91.886  17.753 1   53.28  ? 358 ILE   A CG1 1 
ATOM   2626  C  CG2 . ILE   A 1 336 ? 67.522 90.32   15.843 1   52.7   ? 358 ILE   A CG2 1 
ATOM   2627  C  CD1 . ILE   A 1 336 ? 67.596 93.131  17.135 1   54.15  ? 358 ILE   A CD1 1 
ATOM   2628  N  N   . PRO   A 1 337 ? 69.004 88.8    19.746 1   52.94  ? 359 PRO   A N   1 
ATOM   2629  C  CA  . PRO   A 1 337 ? 69.576 88.696  21.109 1   52.76  ? 359 PRO   A CA  1 
ATOM   2630  C  C   . PRO   A 1 337 ? 69.702 90.022  21.857 1   53.35  ? 359 PRO   A C   1 
ATOM   2631  O  O   . PRO   A 1 337 ? 69.679 91.069  21.232 1   52.95  ? 359 PRO   A O   1 
ATOM   2632  C  CB  . PRO   A 1 337 ? 70.949 88.063  20.875 1   53.39  ? 359 PRO   A CB  1 
ATOM   2633  C  CG  . PRO   A 1 337 ? 70.892 87.468  19.492 1   53.73  ? 359 PRO   A CG  1 
ATOM   2634  C  CD  . PRO   A 1 337 ? 69.94  88.305  18.718 1   52.32  ? 359 PRO   A CD  1 
ATOM   2635  N  N   . ARG   A 1 338 ? 69.847 89.98   23.195 1   54.32  ? 360 ARG   A N   1 
ATOM   2636  C  CA  . ARG   A 1 338 ? 69.957 91.174  24.044 1   55.42  ? 360 ARG   A CA  1 
ATOM   2637  C  C   . ARG   A 1 338 ? 71.002 92.173  23.551 1   56.25  ? 360 ARG   A C   1 
ATOM   2638  O  O   . ARG   A 1 338 ? 70.729 93.37   23.488 1   56.22  ? 360 ARG   A O   1 
ATOM   2639  C  CB  . ARG   A 1 338 ? 70.28  90.789  25.495 1   57.4   ? 360 ARG   A CB  1 
ATOM   2640  C  CG  . ARG   A 1 338 ? 69.229 89.917  26.155 1   61.01  ? 360 ARG   A CG  1 
ATOM   2641  C  CD  . ARG   A 1 338 ? 69.447 89.803  27.654 1   63.27  ? 360 ARG   A CD  1 
ATOM   2642  N  NE  . ARG   A 1 338 ? 68.339 89.086  28.281 1   65.4   ? 360 ARG   A NE  1 
ATOM   2643  C  CZ  . ARG   A 1 338 ? 67.242 89.665  28.754 1   67.91  ? 360 ARG   A CZ  1 
ATOM   2644  N  NH1 . ARG   A 1 338 ? 67.107 90.985  28.712 1   67.46  ? 360 ARG   A NH1 1 
ATOM   2645  N  NH2 . ARG   A 1 338 ? 66.283 88.933  29.301 1   69.1   ? 360 ARG   A NH2 1 
ATOM   2646  N  N   . GLU   A 1 339 ? 72.189 91.679  23.186 1   56.86  ? 361 GLU   A N   1 
ATOM   2647  C  CA  . GLU   A 1 339 ? 73.303 92.485  22.701 1   58.11  ? 361 GLU   A CA  1 
ATOM   2648  C  C   . GLU   A 1 339 ? 73.089 93.033  21.264 1   58.45  ? 361 GLU   A C   1 
ATOM   2649  O  O   . GLU   A 1 339 ? 73.805 93.946  20.843 1   58.8   ? 361 GLU   A O   1 
ATOM   2650  C  CB  . GLU   A 1 339 ? 74.609 91.676  22.795 1   62.02  ? 361 GLU   A CB  1 
ATOM   2651  C  CG  . GLU   A 1 339 ? 74.683 90.506  21.82  1   69.57  ? 361 GLU   A CG  1 
ATOM   2652  C  CD  . GLU   A 1 339 ? 74.108 89.176  22.277 1   78.12  ? 361 GLU   A CD  1 
ATOM   2653  O  OE1 . GLU   A 1 339 ? 73.414 89.142  23.321 1   79.01  ? 361 GLU   A OE1 1 
ATOM   2654  O  OE2 . GLU   A 1 339 ? 74.354 88.163  21.581 1   81.64  ? 361 GLU   A OE2 1 
ATOM   2655  N  N   . ALA   A 1 340 ? 72.118 92.488  20.518 1   58.06  ? 362 ALA   A N   1 
ATOM   2656  C  CA  . ALA   A 1 340 ? 71.794 92.982  19.187 1   58.57  ? 362 ALA   A CA  1 
ATOM   2657  C  C   . ALA   A 1 340 ? 70.705 94.072  19.249 1   59.99  ? 362 ALA   A C   1 
ATOM   2658  O  O   . ALA   A 1 340 ? 70.658 94.918  18.365 1   60.31  ? 362 ALA   A O   1 
ATOM   2659  C  CB  . ALA   A 1 340 ? 71.348 91.841  18.291 1   58.34  ? 362 ALA   A CB  1 
ATOM   2660  N  N   . ILE   A 1 341 ? 69.839 94.06   20.286 1   60.82  ? 363 ILE   A N   1 
ATOM   2661  C  CA  . ILE   A 1 341 ? 68.765 95.04   20.468 1   62.12  ? 363 ILE   A CA  1 
ATOM   2662  C  C   . ILE   A 1 341 ? 69.322 96.441  20.79  1   64.06  ? 363 ILE   A C   1 
ATOM   2663  O  O   . ILE   A 1 341 ? 70.183 96.586  21.664 1   64.04  ? 363 ILE   A O   1 
ATOM   2664  C  CB  . ILE   A 1 341 ? 67.783 94.543  21.561 1   62.26  ? 363 ILE   A CB  1 
ATOM   2665  C  CG1 . ILE   A 1 341 ? 67.119 93.233  21.143 1   62.93  ? 363 ILE   A CG1 1 
ATOM   2666  C  CG2 . ILE   A 1 341 ? 66.736 95.59   21.896 1   62.74  ? 363 ILE   A CG2 1 
ATOM   2667  C  CD1 . ILE   A 1 341 ? 66.266 92.602  22.181 1   63.74  ? 363 ILE   A CD1 1 
ATOM   2668  N  N   . PRO   A 1 342 ? 68.846 97.481  20.075 1   65.47  ? 364 PRO   A N   1 
ATOM   2669  C  CA  . PRO   A 1 342 ? 69.329 98.847  20.354 1   66.94  ? 364 PRO   A CA  1 
ATOM   2670  C  C   . PRO   A 1 342 ? 69.004 99.307  21.775 1   69.15  ? 364 PRO   A C   1 
ATOM   2671  O  O   . PRO   A 1 342 ? 67.867 99.175  22.225 1   69.56  ? 364 PRO   A O   1 
ATOM   2672  C  CB  . PRO   A 1 342 ? 68.618 99.7    19.301 1   67.3   ? 364 PRO   A CB  1 
ATOM   2673  C  CG  . PRO   A 1 342 ? 67.447 98.888  18.856 1   67.29  ? 364 PRO   A CG  1 
ATOM   2674  C  CD  . PRO   A 1 342 ? 67.838 97.457  18.997 1   65.25  ? 364 PRO   A CD  1 
ATOM   2675  N  N   . PRO   A 1 343 ? 70.006 99.812  22.516 1   70.38  ? 365 PRO   A N   1 
ATOM   2676  C  CA  . PRO   A 1 343 ? 69.765 100.205 23.917 1   71.51  ? 365 PRO   A CA  1 
ATOM   2677  C  C   . PRO   A 1 343 ? 68.874 101.428 24.105 1   73.31  ? 365 PRO   A C   1 
ATOM   2678  O  O   . PRO   A 1 343 ? 68.888 102.324 23.27  1   73.25  ? 365 PRO   A O   1 
ATOM   2679  C  CB  . PRO   A 1 343 ? 71.176 100.453 24.468 1   71.83  ? 365 PRO   A CB  1 
ATOM   2680  C  CG  . PRO   A 1 343 ? 72.117 99.902  23.442 1   71.88  ? 365 PRO   A CG  1 
ATOM   2681  C  CD  . PRO   A 1 343 ? 71.416 99.996  22.138 1   70.02  ? 365 PRO   A CD  1 
ATOM   2682  N  N   . LEU   A 1 344 ? 68.114 101.467 25.214 1   74.79  ? 366 LEU   A N   1 
ATOM   2683  C  CA  . LEU   A 1 344 ? 67.215 102.578 25.533 1   76.74  ? 366 LEU   A CA  1 
ATOM   2684  C  C   . LEU   A 1 344 ? 67.992 103.831 25.967 1   79.21  ? 366 LEU   A C   1 
ATOM   2685  O  O   . LEU   A 1 344 ? 68.853 103.749 26.843 1   79.45  ? 366 LEU   A O   1 
ATOM   2686  C  CB  . LEU   A 1 344 ? 66.222 102.154 26.627 1   76.66  ? 366 LEU   A CB  1 
ATOM   2687  C  CG  . LEU   A 1 344 ? 65.023 101.335 26.165 1   77.39  ? 366 LEU   A CG  1 
ATOM   2688  C  CD1 . LEU   A 1 344 ? 64.189 100.88  27.34  1   77.45  ? 366 LEU   A CD1 1 
ATOM   2689  C  CD2 . LEU   A 1 344 ? 64.162 102.134 25.214 1   77.96  ? 366 LEU   A CD2 1 
ATOM   2690  N  N   . ASP   A 1 345 ? 67.703 104.988 25.341 1   80.98  ? 367 ASP   A N   1 
ATOM   2691  C  CA  . ASP   A 1 345 ? 68.403 106.247 25.639 1   82.94  ? 367 ASP   A CA  1 
ATOM   2692  C  C   . ASP   A 1 345 ? 67.514 107.276 26.356 1   84.53  ? 367 ASP   A C   1 
ATOM   2693  O  O   . ASP   A 1 345 ? 67.749 107.559 27.533 1   84.89  ? 367 ASP   A O   1 
ATOM   2694  C  CB  . ASP   A 1 345 ? 69.045 106.846 24.363 1   84.62  ? 367 ASP   A CB  1 
ATOM   2695  C  CG  . ASP   A 1 345 ? 70.21  106.044 23.832 1   88.92  ? 367 ASP   A CG  1 
ATOM   2696  O  OD1 . ASP   A 1 345 ? 70.916 105.4   24.654 1   89.43  ? 367 ASP   A OD1 1 
ATOM   2697  O  OD2 . ASP   A 1 345 ? 70.424 106.059 22.598 1   91.12  ? 367 ASP   A OD2 1 
ATOM   2698  N  N   . GLU   A 1 346 ? 66.501 107.826 25.647 1   85.25  ? 368 GLU   A N   1 
ATOM   2699  C  CA  . GLU   A 1 346 ? 65.541 108.812 26.158 1   86.39  ? 368 GLU   A CA  1 
ATOM   2700  C  C   . GLU   A 1 346 ? 66.2   110.002 26.874 1   86.87  ? 368 GLU   A C   1 
ATOM   2701  O  O   . GLU   A 1 346 ? 66.03  111.149 26.454 1   87.08  ? 368 GLU   A O   1 
ATOM   2702  C  CB  . GLU   A 1 346 ? 64.463 108.149 27.048 1   88.91  ? 368 GLU   A CB  1 
ATOM   2703  C  CG  . GLU   A 1 346 ? 63.939 106.806 26.541 1   93.37  ? 368 GLU   A CG  1 
ATOM   2704  C  CD  . GLU   A 1 346 ? 63.033 106.806 25.321 1   98.63  ? 368 GLU   A CD  1 
ATOM   2705  O  OE1 . GLU   A 1 346 ? 62.563 105.708 24.942 1   99.59  ? 368 GLU   A OE1 1 
ATOM   2706  O  OE2 . GLU   A 1 346 ? 62.784 107.891 24.747 1   99.96  ? 368 GLU   A OE2 1 
ATOM   2707  N  N   . LYS   B 1 3   ? 67.617 53.059  53.482 1   50.6   ? 25  LYS   B N   1 
ATOM   2708  C  CA  . LYS   B 1 3   ? 66.851 53.041  54.723 1   51.27  ? 25  LYS   B CA  1 
ATOM   2709  C  C   . LYS   B 1 3   ? 66.475 54.465  55.168 1   51.04  ? 25  LYS   B C   1 
ATOM   2710  O  O   . LYS   B 1 3   ? 65.291 54.739  55.341 1   51.31  ? 25  LYS   B O   1 
ATOM   2711  C  CB  . LYS   B 1 3   ? 67.597 52.267  55.83  1   54.12  ? 25  LYS   B CB  1 
ATOM   2712  C  CG  . LYS   B 1 3   ? 66.765 51.149  56.448 1   58.75  ? 25  LYS   B CG  1 
ATOM   2713  C  CD  . LYS   B 1 3   ? 65.547 51.687  57.189 1   63.53  ? 25  LYS   B CD  1 
ATOM   2714  C  CE  . LYS   B 1 3   ? 64.706 50.563  57.721 1   68.19  ? 25  LYS   B CE  1 
ATOM   2715  N  NZ  . LYS   B 1 3   ? 63.591 51.068  58.553 1   71.23  ? 25  LYS   B NZ  1 
ATOM   2716  N  N   . ILE   B 1 4   ? 67.458 55.379  55.329 1   50.14  ? 26  ILE   B N   1 
ATOM   2717  C  CA  . ILE   B 1 4   ? 67.167 56.78   55.675 1   49.63  ? 26  ILE   B CA  1 
ATOM   2718  C  C   . ILE   B 1 4   ? 66.662 57.553  54.418 1   49.58  ? 26  ILE   B C   1 
ATOM   2719  O  O   . ILE   B 1 4   ? 66.966 57.155  53.297 1   49.98  ? 26  ILE   B O   1 
ATOM   2720  C  CB  . ILE   B 1 4   ? 68.396 57.464  56.328 1   49.71  ? 26  ILE   B CB  1 
ATOM   2721  C  CG1 . ILE   B 1 4   ? 69.519 57.732  55.311 1   49.88  ? 26  ILE   B CG1 1 
ATOM   2722  C  CG2 . ILE   B 1 4   ? 68.899 56.641  57.5   1   50.39  ? 26  ILE   B CG2 1 
ATOM   2723  C  CD1 . ILE   B 1 4   ? 70.613 58.601  55.794 1   50.87  ? 26  ILE   B CD1 1 
ATOM   2724  N  N   . TYR   B 1 5   ? 65.896 58.636  54.609 1   48.75  ? 27  TYR   B N   1 
ATOM   2725  C  CA  . TYR   B 1 5   ? 65.297 59.449  53.54  1   48.55  ? 27  TYR   B CA  1 
ATOM   2726  C  C   . TYR   B 1 5   ? 66.193 59.687  52.306 1   48.59  ? 27  TYR   B C   1 
ATOM   2727  O  O   . TYR   B 1 5   ? 65.783 59.379  51.183 1   49.01  ? 27  TYR   B O   1 
ATOM   2728  C  CB  . TYR   B 1 5   ? 64.802 60.792  54.116 1   48.53  ? 27  TYR   B CB  1 
ATOM   2729  C  CG  . TYR   B 1 5   ? 63.981 61.64   53.165 1   49.16  ? 27  TYR   B CG  1 
ATOM   2730  C  CD1 . TYR   B 1 5   ? 62.608 61.465  53.055 1   49.72  ? 27  TYR   B CD1 1 
ATOM   2731  C  CD2 . TYR   B 1 5   ? 64.558 62.691  52.463 1   49.88  ? 27  TYR   B CD2 1 
ATOM   2732  C  CE1 . TYR   B 1 5   ? 61.843 62.265  52.214 1   50.24  ? 27  TYR   B CE1 1 
ATOM   2733  C  CE2 . TYR   B 1 5   ? 63.8   63.499  51.621 1   50.39  ? 27  TYR   B CE2 1 
ATOM   2734  C  CZ  . TYR   B 1 5   ? 62.442 63.283  51.504 1   50.83  ? 27  TYR   B CZ  1 
ATOM   2735  O  OH  . TYR   B 1 5   ? 61.684 64.064  50.676 1   52.04  ? 27  TYR   B OH  1 
ATOM   2736  N  N   . GLY   B 1 6   ? 67.387 60.227  52.517 1   48.1   ? 28  GLY   B N   1 
ATOM   2737  C  CA  . GLY   B 1 6   ? 68.313 60.54   51.432 1   47.95  ? 28  GLY   B CA  1 
ATOM   2738  C  C   . GLY   B 1 6   ? 68.885 59.328  50.739 1   47.55  ? 28  GLY   B C   1 
ATOM   2739  O  O   . GLY   B 1 6   ? 69.198 59.375  49.549 1   47.83  ? 28  GLY   B O   1 
ATOM   2740  N  N   . GLU   B 1 7   ? 69.041 58.24   51.483 1   47.18  ? 29  GLU   B N   1 
ATOM   2741  C  CA  . GLU   B 1 7   ? 69.566 57.006  50.925 1   47.54  ? 29  GLU   B CA  1 
ATOM   2742  C  C   . GLU   B 1 7   ? 68.486 56.284  50.135 1   47.24  ? 29  GLU   B C   1 
ATOM   2743  O  O   . GLU   B 1 7   ? 68.763 55.762  49.06  1   47.77  ? 29  GLU   B O   1 
ATOM   2744  C  CB  . GLU   B 1 7   ? 70.109 56.097  52.034 1   50.15  ? 29  GLU   B CB  1 
ATOM   2745  C  CG  . GLU   B 1 7   ? 71.528 56.416  52.447 1   56.94  ? 29  GLU   B CG  1 
ATOM   2746  C  CD  . GLU   B 1 7   ? 71.979 55.729  53.725 1   67.65  ? 29  GLU   B CD  1 
ATOM   2747  O  OE1 . GLU   B 1 7   ? 71.256 54.829  54.223 1   69.8   ? 29  GLU   B OE1 1 
ATOM   2748  O  OE2 . GLU   B 1 7   ? 73.064 56.098  54.233 1   70.11  ? 29  GLU   B OE2 1 
ATOM   2749  N  N   . TYR   B 1 8   ? 67.26  56.252  50.677 1   46.2   ? 30  TYR   B N   1 
ATOM   2750  C  CA  . TYR   B 1 8   ? 66.095 55.605  50.102 1   45.42  ? 30  TYR   B CA  1 
ATOM   2751  C  C   . TYR   B 1 8   ? 65.776 56.23   48.762 1   45.71  ? 30  TYR   B C   1 
ATOM   2752  O  O   . TYR   B 1 8   ? 65.659 55.518  47.769 1   46.36  ? 30  TYR   B O   1 
ATOM   2753  C  CB  . TYR   B 1 8   ? 64.894 55.728  51.07  1   44.77  ? 30  TYR   B CB  1 
ATOM   2754  C  CG  . TYR   B 1 8   ? 63.628 55.118  50.521 1   45.19  ? 30  TYR   B CG  1 
ATOM   2755  C  CD1 . TYR   B 1 8   ? 63.497 53.743  50.389 1   45.63  ? 30  TYR   B CD1 1 
ATOM   2756  C  CD2 . TYR   B 1 8   ? 62.574 55.914  50.104 1   45.97  ? 30  TYR   B CD2 1 
ATOM   2757  C  CE1 . TYR   B 1 8   ? 62.345 53.176  49.867 1   46.26  ? 30  TYR   B CE1 1 
ATOM   2758  C  CE2 . TYR   B 1 8   ? 61.422 55.359  49.564 1   46.6   ? 30  TYR   B CE2 1 
ATOM   2759  C  CZ  . TYR   B 1 8   ? 61.311 53.987  49.449 1   47.11  ? 30  TYR   B CZ  1 
ATOM   2760  O  OH  . TYR   B 1 8   ? 60.169 53.425  48.94  1   48.28  ? 30  TYR   B OH  1 
ATOM   2761  N  N   . LEU   B 1 9   ? 65.661 57.565  48.726 1   44.93  ? 31  LEU   B N   1 
ATOM   2762  C  CA  . LEU   B 1 9   ? 65.342 58.279  47.507 1   44.45  ? 31  LEU   B CA  1 
ATOM   2763  C  C   . LEU   B 1 9   ? 66.544 58.552  46.624 1   44.65  ? 31  LEU   B C   1 
ATOM   2764  O  O   . LEU   B 1 9   ? 66.363 59.162  45.579 1   45.14  ? 31  LEU   B O   1 
ATOM   2765  C  CB  . LEU   B 1 9   ? 64.632 59.588  47.832 1   44.19  ? 31  LEU   B CB  1 
ATOM   2766  C  CG  . LEU   B 1 9   ? 63.327 59.45   48.571 1   44.85  ? 31  LEU   B CG  1 
ATOM   2767  C  CD1 . LEU   B 1 9   ? 62.83  60.797  48.999 1   45.64  ? 31  LEU   B CD1 1 
ATOM   2768  C  CD2 . LEU   B 1 9   ? 62.298 58.734  47.728 1   44.56  ? 31  LEU   B CD2 1 
ATOM   2769  N  N   . MET   B 1 10  ? 67.766 58.147  47.035 1   44.27  ? 32  MET   B N   1 
ATOM   2770  C  CA  . MET   B 1 10  ? 69.013 58.321  46.283 1   44.25  ? 32  MET   B CA  1 
ATOM   2771  C  C   . MET   B 1 10  ? 69.201 59.755  45.859 1   45.02  ? 32  MET   B C   1 
ATOM   2772  O  O   . MET   B 1 10  ? 69.402 60.053  44.686 1   45.54  ? 32  MET   B O   1 
ATOM   2773  C  CB  . MET   B 1 10  ? 69.095 57.339  45.103 1   44.34  ? 32  MET   B CB  1 
ATOM   2774  C  CG  . MET   B 1 10  ? 69.153 55.899  45.562 1   46.23  ? 32  MET   B CG  1 
ATOM   2775  S  SD  . MET   B 1 10  ? 68.953 54.664  44.252 1   48.71  ? 32  MET   B SD  1 
ATOM   2776  C  CE  . MET   B 1 10  ? 70.425 54.821  43.457 1   46.04  ? 32  MET   B CE  1 
ATOM   2777  N  N   . LEU   B 1 11  ? 69.078 60.655  46.823 1   45.1   ? 33  LEU   B N   1 
ATOM   2778  C  CA  . LEU   B 1 11  ? 69.201 62.084  46.568 1   45.57  ? 33  LEU   B CA  1 
ATOM   2779  C  C   . LEU   B 1 11  ? 70.628 62.512  46.222 1   46.23  ? 33  LEU   B C   1 
ATOM   2780  O  O   . LEU   B 1 11  ? 70.817 63.557  45.604 1   46.01  ? 33  LEU   B O   1 
ATOM   2781  C  CB  . LEU   B 1 11  ? 68.624 62.872  47.743 1   45.64  ? 33  LEU   B CB  1 
ATOM   2782  C  CG  . LEU   B 1 11  ? 67.18  62.522  48.09  1   46.72  ? 33  LEU   B CG  1 
ATOM   2783  C  CD1 . LEU   B 1 11  ? 66.748 63.233  49.322 1   47.1   ? 33  LEU   B CD1 1 
ATOM   2784  C  CD2 . LEU   B 1 11  ? 66.239 62.844  46.933 1   47.5   ? 33  LEU   B CD2 1 
ATOM   2785  N  N   . ASP   B 1 12  ? 71.633 61.682  46.569 1   46.74  ? 34  ASP   B N   1 
ATOM   2786  C  CA  . ASP   B 1 12  ? 73.028 61.929  46.179 1   47.53  ? 34  ASP   B CA  1 
ATOM   2787  C  C   . ASP   B 1 12  ? 73.219 61.781  44.65  1   46.44  ? 34  ASP   B C   1 
ATOM   2788  O  O   . ASP   B 1 12  ? 74.127 62.378  44.082 1   47.23  ? 34  ASP   B O   1 
ATOM   2789  C  CB  . ASP   B 1 12  ? 73.966 60.966  46.935 1   50.99  ? 34  ASP   B CB  1 
ATOM   2790  C  CG  . ASP   B 1 12  ? 74.115 61.347  48.396 1   60.38  ? 34  ASP   B CG  1 
ATOM   2791  O  OD1 . ASP   B 1 12  ? 74.269 62.566  48.681 1   62.35  ? 34  ASP   B OD1 1 
ATOM   2792  O  OD2 . ASP   B 1 12  ? 74.05  60.432  49.265 1   63.73  ? 34  ASP   B OD2 1 
ATOM   2793  N  N   . LYS   B 1 13  ? 72.352 60.988  44.006 1   44.66  ? 35  LYS   B N   1 
ATOM   2794  C  CA  . LYS   B 1 13  ? 72.345 60.706  42.588 1   43.95  ? 35  LYS   B CA  1 
ATOM   2795  C  C   . LYS   B 1 13  ? 71.369 61.674  41.894 1   43.45  ? 35  LYS   B C   1 
ATOM   2796  O  O   . LYS   B 1 13  ? 71.731 62.324  40.912 1   43.39  ? 35  LYS   B O   1 
ATOM   2797  C  CB  . LYS   B 1 13  ? 71.917 59.239  42.381 1   44.83  ? 35  LYS   B CB  1 
ATOM   2798  C  CG  . LYS   B 1 13  ? 72.333 58.643  41.059 1   48.15  ? 35  LYS   B CG  1 
ATOM   2799  C  CD  . LYS   B 1 13  ? 71.923 57.18   40.968 1   52.67  ? 35  LYS   B CD  1 
ATOM   2800  C  CE  . LYS   B 1 13  ? 72.988 56.252  41.496 1   56.58  ? 35  LYS   B CE  1 
ATOM   2801  N  NZ  . LYS   B 1 13  ? 72.624 54.812  41.336 1   58.27  ? 35  LYS   B NZ  1 
ATOM   2802  N  N   . LEU   B 1 14  ? 70.146 61.797  42.439 1   42.91  ? 36  LEU   B N   1 
ATOM   2803  C  CA  . LEU   B 1 14  ? 69.085 62.655  41.907 1   42.51  ? 36  LEU   B CA  1 
ATOM   2804  C  C   . LEU   B 1 14  ? 69.439 64.135  41.949 1   41.96  ? 36  LEU   B C   1 
ATOM   2805  O  O   . LEU   B 1 14  ? 69.316 64.826  40.935 1   42.12  ? 36  LEU   B O   1 
ATOM   2806  C  CB  . LEU   B 1 14  ? 67.756 62.394  42.647 1   42.55  ? 36  LEU   B CB  1 
ATOM   2807  C  CG  . LEU   B 1 14  ? 66.538 63.102  42.093 1   42.9   ? 36  LEU   B CG  1 
ATOM   2808  C  CD1 . LEU   B 1 14  ? 65.794 62.204  41.14  1   43.12  ? 36  LEU   B CD1 1 
ATOM   2809  C  CD2 . LEU   B 1 14  ? 65.64  63.581  43.204 1   42.97  ? 36  LEU   B CD2 1 
ATOM   2810  N  N   . LEU   B 1 15  ? 69.893 64.623  43.103 1   41.5   ? 37  LEU   B N   1 
ATOM   2811  C  CA  . LEU   B 1 15  ? 70.257 66.031  43.242 1   41.75  ? 37  LEU   B CA  1 
ATOM   2812  C  C   . LEU   B 1 15  ? 71.674 66.362  42.74  1   42.54  ? 37  LEU   B C   1 
ATOM   2813  O  O   . LEU   B 1 15  ? 72.204 67.432  43.027 1   42.43  ? 37  LEU   B O   1 
ATOM   2814  C  CB  . LEU   B 1 15  ? 70.046 66.52   44.685 1   41.45  ? 37  LEU   B CB  1 
ATOM   2815  C  CG  . LEU   B 1 15  ? 68.65  66.971  45.158 1   42.21  ? 37  LEU   B CG  1 
ATOM   2816  C  CD1 . LEU   B 1 15  ? 67.539 66.869  44.075 1   42.25  ? 37  LEU   B CD1 1 
ATOM   2817  C  CD2 . LEU   B 1 15  ? 68.26  66.255  46.436 1   42.8   ? 37  LEU   B CD2 1 
ATOM   2818  N  N   . ASP   B 1 16  ? 72.251 65.478  41.937 1   43.15  ? 38  ASP   B N   1 
ATOM   2819  C  CA  . ASP   B 1 16  ? 73.538 65.687  41.307 1   44.31  ? 38  ASP   B CA  1 
ATOM   2820  C  C   . ASP   B 1 16  ? 73.427 65.68   39.744 1   44.63  ? 38  ASP   B C   1 
ATOM   2821  O  O   . ASP   B 1 16  ? 74.43  65.852  39.054 1   45.27  ? 38  ASP   B O   1 
ATOM   2822  C  CB  . ASP   B 1 16  ? 74.532 64.63   41.812 1   47.31  ? 38  ASP   B CB  1 
ATOM   2823  C  CG  . ASP   B 1 16  ? 75.991 65.011  41.628 1   53.04  ? 38  ASP   B CG  1 
ATOM   2824  O  OD1 . ASP   B 1 16  ? 76.336 66.189  41.876 1   53.31  ? 38  ASP   B OD1 1 
ATOM   2825  O  OD2 . ASP   B 1 16  ? 76.783 64.137  41.239 1   56.29  ? 38  ASP   B OD2 1 
ATOM   2826  N  N   . ALA   B 1 17  ? 72.213 65.516  39.19  1   44.03  ? 39  ALA   B N   1 
ATOM   2827  C  CA  . ALA   B 1 17  ? 71.976 65.5    37.752 1   43.95  ? 39  ALA   B CA  1 
ATOM   2828  C  C   . ALA   B 1 17  ? 71.672 66.884  37.17  1   44.32  ? 39  ALA   B C   1 
ATOM   2829  O  O   . ALA   B 1 17  ? 71.185 66.961  36.047 1   44.34  ? 39  ALA   B O   1 
ATOM   2830  C  CB  . ALA   B 1 17  ? 70.828 64.556  37.434 1   43.84  ? 39  ALA   B CB  1 
ATOM   2831  N  N   . GLN   B 1 18  ? 71.947 67.974  37.906 1   44.59  ? 40  GLN   B N   1 
ATOM   2832  C  CA  . GLN   B 1 18  ? 71.64  69.32   37.401 1   45.19  ? 40  GLN   B CA  1 
ATOM   2833  C  C   . GLN   B 1 18  ? 72.907 70.067  37.014 1   47.13  ? 40  GLN   B C   1 
ATOM   2834  O  O   . GLN   B 1 18  ? 73.682 70.489  37.883 1   47.26  ? 40  GLN   B O   1 
ATOM   2835  C  CB  . GLN   B 1 18  ? 70.782 70.12   38.399 1   44.46  ? 40  GLN   B CB  1 
ATOM   2836  C  CG  . GLN   B 1 18  ? 69.427 69.474  38.685 1   42.88  ? 40  GLN   B CG  1 
ATOM   2837  C  CD  . GLN   B 1 18  ? 69.549 68.316  39.64  1   41.59  ? 40  GLN   B CD  1 
ATOM   2838  O  OE1 . GLN   B 1 18  ? 70.372 68.328  40.536 1   42.76  ? 40  GLN   B OE1 1 
ATOM   2839  N  NE2 . GLN   B 1 18  ? 68.761 67.278  39.456 1   40     ? 40  GLN   B NE2 1 
ATOM   2840  N  N   . CYS   B 1 19  ? 73.119 70.225  35.7   1   48.19  ? 41  CYS   B N   1 
ATOM   2841  C  CA  . CYS   B 1 19  ? 74.316 70.877  35.194 1   49.86  ? 41  CYS   B CA  1 
ATOM   2842  C  C   . CYS   B 1 19  ? 74.017 71.962  34.163 1   50.87  ? 41  CYS   B C   1 
ATOM   2843  O  O   . CYS   B 1 19  ? 73.718 71.667  33.003 1   51.25  ? 41  CYS   B O   1 
ATOM   2844  C  CB  . CYS   B 1 19  ? 75.291 69.835  34.652 1   51.65  ? 41  CYS   B CB  1 
ATOM   2845  S  SG  . CYS   B 1 19  ? 76.796 70.529  33.916 1   58.36  ? 41  CYS   B SG  1 
ATOM   2846  N  N   . MET   B 1 20  ? 74.155 73.217  34.576 1   51.39  ? 42  MET   B N   1 
ATOM   2847  C  CA  . MET   B 1 20  ? 73.918 74.356  33.704 1   52.46  ? 42  MET   B CA  1 
ATOM   2848  C  C   . MET   B 1 20  ? 75.136 74.594  32.841 1   54.01  ? 42  MET   B C   1 
ATOM   2849  O  O   . MET   B 1 20  ? 76.21  74.86   33.363 1   54.24  ? 42  MET   B O   1 
ATOM   2850  C  CB  . MET   B 1 20  ? 73.623 75.618  34.529 1   52.61  ? 42  MET   B CB  1 
ATOM   2851  C  CG  . MET   B 1 20  ? 72.247 75.621  35.155 1   53.86  ? 42  MET   B CG  1 
ATOM   2852  S  SD  . MET   B 1 20  ? 72.063 76.838  36.471 1   55.24  ? 42  MET   B SD  1 
ATOM   2853  C  CE  . MET   B 1 20  ? 72.535 78.363  35.606 1   49.76  ? 42  MET   B CE  1 
ATOM   2854  N  N   . LEU   B 1 21  ? 74.972 74.506  31.519 1   54.8   ? 43  LEU   B N   1 
ATOM   2855  C  CA  . LEU   B 1 21  ? 76.052 74.746  30.584 1   55.99  ? 43  LEU   B CA  1 
ATOM   2856  C  C   . LEU   B 1 21  ? 76.379 76.232  30.413 1   58.59  ? 43  LEU   B C   1 
ATOM   2857  O  O   . LEU   B 1 21  ? 77.475 76.564  29.959 1   58.92  ? 43  LEU   B O   1 
ATOM   2858  C  CB  . LEU   B 1 21  ? 75.752 74.074  29.243 1   55.25  ? 43  LEU   B CB  1 
ATOM   2859  C  CG  . LEU   B 1 21  ? 75.465 72.587  29.317 1   55.28  ? 43  LEU   B CG  1 
ATOM   2860  C  CD1 . LEU   B 1 21  ? 75.128 72.037  27.98  1   55.23  ? 43  LEU   B CD1 1 
ATOM   2861  C  CD2 . LEU   B 1 21  ? 76.628 71.834  29.911 1   55.88  ? 43  LEU   B CD2 1 
ATOM   2862  N  N   . SER   B 1 22  ? 75.449 77.128  30.776 1   60.21  ? 44  SER   B N   1 
ATOM   2863  C  CA  . SER   B 1 22  ? 75.716 78.561  30.731 1   62.24  ? 44  SER   B CA  1 
ATOM   2864  C  C   . SER   B 1 22  ? 76.644 78.93   31.907 1   64.48  ? 44  SER   B C   1 
ATOM   2865  O  O   . SER   B 1 22  ? 77.565 79.719  31.733 1   64.93  ? 44  SER   B O   1 
ATOM   2866  C  CB  . SER   B 1 22  ? 74.417 79.349  30.806 1   62.95  ? 44  SER   B CB  1 
ATOM   2867  O  OG  . SER   B 1 22  ? 73.782 79.142  32.056 1   64.67  ? 44  SER   B OG  1 
ATOM   2868  N  N   . GLU   B 1 23  ? 76.43  78.33   33.082 1   65.85  ? 45  GLU   B N   1 
ATOM   2869  C  CA  . GLU   B 1 23  ? 77.267 78.54   34.266 1   68.03  ? 45  GLU   B CA  1 
ATOM   2870  C  C   . GLU   B 1 23  ? 78.682 77.972  34.029 1   69.79  ? 45  GLU   B C   1 
ATOM   2871  O  O   . GLU   B 1 23  ? 79.673 78.583  34.441 1   69.81  ? 45  GLU   B O   1 
ATOM   2872  C  CB  . GLU   B 1 23  ? 76.617 77.845  35.471 1   70.9   ? 45  GLU   B CB  1 
ATOM   2873  C  CG  . GLU   B 1 23  ? 77.226 78.189  36.815 1   77.59  ? 45  GLU   B CG  1 
ATOM   2874  C  CD  . GLU   B 1 23  ? 76.582 77.43   37.964 1   86.68  ? 45  GLU   B CD  1 
ATOM   2875  O  OE1 . GLU   B 1 23  ? 76.186 76.258  37.757 1   88.52  ? 45  GLU   B OE1 1 
ATOM   2876  O  OE2 . GLU   B 1 23  ? 76.471 78.008  39.071 1   89.1   ? 45  GLU   B OE2 1 
ATOM   2877  N  N   . GLU   B 1 24  ? 78.758 76.81   33.333 1   71.09  ? 46  GLU   B N   1 
ATOM   2878  C  CA  . GLU   B 1 24  ? 79.983 76.096  32.947 1   72.68  ? 46  GLU   B CA  1 
ATOM   2879  C  C   . GLU   B 1 24  ? 80.822 76.995  32.026 1   73.54  ? 46  GLU   B C   1 
ATOM   2880  O  O   . GLU   B 1 24  ? 82.038 77.106  32.207 1   73.93  ? 46  GLU   B O   1 
ATOM   2881  C  CB  . GLU   B 1 24  ? 79.607 74.76   32.24  1   76.06  ? 46  GLU   B CB  1 
ATOM   2882  C  CG  . GLU   B 1 24  ? 80.686 74.11   31.375 1   82.36  ? 46  GLU   B CG  1 
ATOM   2883  C  CD  . GLU   B 1 24  ? 80.563 74.28   29.867 1   89.9   ? 46  GLU   B CD  1 
ATOM   2884  O  OE1 . GLU   B 1 24  ? 79.445 74.572  29.382 1   90.91  ? 46  GLU   B OE1 1 
ATOM   2885  O  OE2 . GLU   B 1 24  ? 81.596 74.148  29.171 1   92.73  ? 46  GLU   B OE2 1 
ATOM   2886  N  N   . ASP   B 1 25  ? 80.158 77.665  31.063 1   73.49  ? 47  ASP   B N   1 
ATOM   2887  C  CA  . ASP   B 1 25  ? 80.819 78.555  30.111 1   73.84  ? 47  ASP   B CA  1 
ATOM   2888  C  C   . ASP   B 1 25  ? 81.058 79.966  30.663 1   73.47  ? 47  ASP   B C   1 
ATOM   2889  O  O   . ASP   B 1 25  ? 81.373 80.865  29.883 1   73.97  ? 47  ASP   B O   1 
ATOM   2890  C  CB  . ASP   B 1 25  ? 79.999 78.634  28.818 1   76.17  ? 47  ASP   B CB  1 
ATOM   2891  C  CG  . ASP   B 1 25  ? 80.835 78.64   27.562 1   81.96  ? 47  ASP   B CG  1 
ATOM   2892  O  OD1 . ASP   B 1 25  ? 81.643 77.696  27.38  1   82.88  ? 47  ASP   B OD1 1 
ATOM   2893  O  OD2 . ASP   B 1 25  ? 80.675 79.577  26.75  1   84.68  ? 47  ASP   B OD2 1 
ATOM   2894  N  N   . LYS   B 1 26  ? 80.886 80.157  31.99  1   72.4   ? 48  LYS   B N   1 
ATOM   2895  C  CA  . LYS   B 1 26  ? 81.055 81.398  32.74  1   71.99  ? 48  LYS   B CA  1 
ATOM   2896  C  C   . LYS   B 1 26  ? 80.176 82.554  32.239 1   70.58  ? 48  LYS   B C   1 
ATOM   2897  O  O   . LYS   B 1 26  ? 80.495 83.723  32.47  1   70.82  ? 48  LYS   B O   1 
ATOM   2898  C  CB  . LYS   B 1 26  ? 82.533 81.804  32.826 1   74.47  ? 48  LYS   B CB  1 
ATOM   2899  C  CG  . LYS   B 1 26  ? 83.359 80.877  33.72  1   79.39  ? 48  LYS   B CG  1 
ATOM   2900  C  CD  . LYS   B 1 26  ? 82.884 80.92   35.193 1   84.5   ? 48  LYS   B CD  1 
ATOM   2901  C  CE  . LYS   B 1 26  ? 83.977 80.543  36.177 1   88.23  ? 48  LYS   B CE  1 
ATOM   2902  N  NZ  . LYS   B 1 26  ? 84.003 81.427  37.388 1   89.79  ? 48  LYS   B NZ  1 
ATOM   2903  N  N   . ARG   B 1 27  ? 79.052 82.22   31.583 1   68.86  ? 49  ARG   B N   1 
ATOM   2904  C  CA  . ARG   B 1 27  ? 78.047 83.17   31.108 1   67.6   ? 49  ARG   B CA  1 
ATOM   2905  C  C   . ARG   B 1 27  ? 76.697 82.619  31.619 1   64.44  ? 49  ARG   B C   1 
ATOM   2906  O  O   . ARG   B 1 27  ? 75.947 82.036  30.831 1   64.26  ? 49  ARG   B O   1 
ATOM   2907  C  CB  . ARG   B 1 27  ? 78.062 83.231  29.564 1   70.21  ? 49  ARG   B CB  1 
ATOM   2908  C  CG  . ARG   B 1 27  ? 79.353 83.764  28.97  1   75.16  ? 49  ARG   B CG  1 
ATOM   2909  C  CD  . ARG   B 1 27  ? 79.109 84.374  27.612 1   80.1   ? 49  ARG   B CD  1 
ATOM   2910  N  NE  . ARG   B 1 27  ? 78.475 85.691  27.711 1   84.43  ? 49  ARG   B NE  1 
ATOM   2911  C  CZ  . ARG   B 1 27  ? 77.257 85.978  27.259 1   87.43  ? 49  ARG   B CZ  1 
ATOM   2912  N  NH1 . ARG   B 1 27  ? 76.513 85.036  26.685 1   86.96  ? 49  ARG   B NH1 1 
ATOM   2913  N  NH2 . ARG   B 1 27  ? 76.771 87.208  27.379 1   87.88  ? 49  ARG   B NH2 1 
ATOM   2914  N  N   . PRO   B 1 28  ? 76.419 82.683  32.949 1   61.36  ? 50  PRO   B N   1 
ATOM   2915  C  CA  . PRO   B 1 28  ? 75.221 82.014  33.461 1   59.18  ? 50  PRO   B CA  1 
ATOM   2916  C  C   . PRO   B 1 28  ? 73.905 82.741  33.24  1   56.48  ? 50  PRO   B C   1 
ATOM   2917  O  O   . PRO   B 1 28  ? 73.831 83.966  33.314 1   56.59  ? 50  PRO   B O   1 
ATOM   2918  C  CB  . PRO   B 1 28  ? 75.526 81.803  34.941 1   60.05  ? 50  PRO   B CB  1 
ATOM   2919  C  CG  . PRO   B 1 28  ? 76.484 82.852  35.278 1   60.96  ? 50  PRO   B CG  1 
ATOM   2920  C  CD  . PRO   B 1 28  ? 77.204 83.29   34.04  1   60.09  ? 50  PRO   B CD  1 
ATOM   2921  N  N   . VAL   B 1 29  ? 72.865 81.943  32.946 1   53.74  ? 51  VAL   B N   1 
ATOM   2922  C  CA  . VAL   B 1 29  ? 71.492 82.364  32.729 1   51.37  ? 51  VAL   B CA  1 
ATOM   2923  C  C   . VAL   B 1 29  ? 70.696 81.668  33.81  1   49.02  ? 51  VAL   B C   1 
ATOM   2924  O  O   . VAL   B 1 29  ? 70.56  80.45   33.767 1   48.95  ? 51  VAL   B O   1 
ATOM   2925  C  CB  . VAL   B 1 29  ? 70.984 81.935  31.338 1   51.86  ? 51  VAL   B CB  1 
ATOM   2926  C  CG1 . VAL   B 1 29  ? 69.569 82.443  31.099 1   52.25  ? 51  VAL   B CG1 1 
ATOM   2927  C  CG2 . VAL   B 1 29  ? 71.922 82.407  30.241 1   52.26  ? 51  VAL   B CG2 1 
ATOM   2928  N  N   . HIS   B 1 30  ? 70.214 82.431  34.803 1   46.93  ? 52  HIS   B N   1 
ATOM   2929  C  CA  . HIS   B 1 30  ? 69.454 81.95   35.957 1   44.72  ? 52  HIS   B CA  1 
ATOM   2930  C  C   . HIS   B 1 30  ? 68.281 81.035  35.589 1   43.58  ? 52  HIS   B C   1 
ATOM   2931  O  O   . HIS   B 1 30  ? 68.07  80.023  36.258 1   43.52  ? 52  HIS   B O   1 
ATOM   2932  C  CB  . HIS   B 1 30  ? 68.973 83.157  36.777 1   43.91  ? 52  HIS   B CB  1 
ATOM   2933  C  CG  . HIS   B 1 30  ? 68.237 82.804  38.026 1   43.48  ? 52  HIS   B CG  1 
ATOM   2934  N  ND1 . HIS   B 1 30  ? 66.855 82.68   38.044 1   44.59  ? 52  HIS   B ND1 1 
ATOM   2935  C  CD2 . HIS   B 1 30  ? 68.713 82.6    39.277 1   44.26  ? 52  HIS   B CD2 1 
ATOM   2936  C  CE1 . HIS   B 1 30  ? 66.54  82.375  39.294 1   45.17  ? 52  HIS   B CE1 1 
ATOM   2937  N  NE2 . HIS   B 1 30  ? 67.626 82.314  40.072 1   45.22  ? 52  HIS   B NE2 1 
ATOM   2938  N  N   . ASP   B 1 31  ? 67.538 81.362  34.516 1   42.85  ? 53  ASP   B N   1 
ATOM   2939  C  CA  . ASP   B 1 31  ? 66.392 80.54   34.11  1   42.89  ? 53  ASP   B CA  1 
ATOM   2940  C  C   . ASP   B 1 31  ? 66.759 79.173  33.493 1   42.71  ? 53  ASP   B C   1 
ATOM   2941  O  O   . ASP   B 1 31  ? 65.849 78.373  33.257 1   43.28  ? 53  ASP   B O   1 
ATOM   2942  C  CB  . ASP   B 1 31  ? 65.435 81.304  33.197 1   44.42  ? 53  ASP   B CB  1 
ATOM   2943  C  CG  . ASP   B 1 31  ? 64.644 82.416  33.875 1   49.85  ? 53  ASP   B CG  1 
ATOM   2944  O  OD1 . ASP   B 1 31  ? 64.781 82.584  35.115 1   49.78  ? 53  ASP   B OD1 1 
ATOM   2945  O  OD2 . ASP   B 1 31  ? 63.895 83.131  33.164 1   53.78  ? 53  ASP   B OD2 1 
ATOM   2946  N  N   . GLU   B 1 32  ? 68.067 78.867  33.293 1   41.76  ? 54  GLU   B N   1 
ATOM   2947  C  CA  . GLU   B 1 32  ? 68.475 77.546  32.79  1   41.05  ? 54  GLU   B CA  1 
ATOM   2948  C  C   . GLU   B 1 32  ? 68.229 76.457  33.831 1   40.85  ? 54  GLU   B C   1 
ATOM   2949  O  O   . GLU   B 1 32  ? 67.922 75.323  33.464 1   41.19  ? 54  GLU   B O   1 
ATOM   2950  C  CB  . GLU   B 1 32  ? 69.94  77.517  32.329 1   42.54  ? 54  GLU   B CB  1 
ATOM   2951  C  CG  . GLU   B 1 32  ? 70.305 76.197  31.664 1   44.43  ? 54  GLU   B CG  1 
ATOM   2952  C  CD  . GLU   B 1 32  ? 71.727 76.041  31.176 1   47.98  ? 54  GLU   B CD  1 
ATOM   2953  O  OE1 . GLU   B 1 32  ? 72.531 76.98   31.356 1   49.63  ? 54  GLU   B OE1 1 
ATOM   2954  O  OE2 . GLU   B 1 32  ? 72.041 74.977  30.603 1   48.68  ? 54  GLU   B OE2 1 
ATOM   2955  N  N   . HIS   B 1 33  ? 68.314 76.805  35.13  1   40.53  ? 55  HIS   B N   1 
ATOM   2956  C  CA  . HIS   B 1 33  ? 68.038 75.88   36.222 1   40.74  ? 55  HIS   B CA  1 
ATOM   2957  C  C   . HIS   B 1 33  ? 66.569 75.408  36.143 1   40.65  ? 55  HIS   B C   1 
ATOM   2958  O  O   . HIS   B 1 33  ? 66.285 74.214  36.325 1   41.05  ? 55  HIS   B O   1 
ATOM   2959  C  CB  . HIS   B 1 33  ? 68.299 76.58   37.556 1   41.61  ? 55  HIS   B CB  1 
ATOM   2960  C  CG  . HIS   B 1 33  ? 68.472 75.652  38.727 1   44.18  ? 55  HIS   B CG  1 
ATOM   2961  N  ND1 . HIS   B 1 33  ? 67.392 74.991  39.294 1   46.02  ? 55  HIS   B ND1 1 
ATOM   2962  C  CD2 . HIS   B 1 33  ? 69.589 75.338  39.427 1   45.31  ? 55  HIS   B CD2 1 
ATOM   2963  C  CE1 . HIS   B 1 33  ? 67.886 74.294  40.309 1   46.5   ? 55  HIS   B CE1 1 
ATOM   2964  N  NE2 . HIS   B 1 33  ? 69.202 74.47   40.431 1   46.36  ? 55  HIS   B NE2 1 
ATOM   2965  N  N   . LEU   B 1 34  ? 65.646 76.35   35.864 1   39.54  ? 56  LEU   B N   1 
ATOM   2966  C  CA  . LEU   B 1 34  ? 64.221 76.054  35.743 1   38.96  ? 56  LEU   B CA  1 
ATOM   2967  C  C   . LEU   B 1 34  ? 63.984 75.126  34.569 1   38.36  ? 56  LEU   B C   1 
ATOM   2968  O  O   . LEU   B 1 34  ? 63.249 74.151  34.699 1   38.74  ? 56  LEU   B O   1 
ATOM   2969  C  CB  . LEU   B 1 34  ? 63.416 77.354  35.581 1   39.05  ? 56  LEU   B CB  1 
ATOM   2970  C  CG  . LEU   B 1 34  ? 61.917 77.186  35.342 1   39.84  ? 56  LEU   B CG  1 
ATOM   2971  C  CD1 . LEU   B 1 34  ? 61.213 76.578  36.58  1   39.6   ? 56  LEU   B CD1 1 
ATOM   2972  C  CD2 . LEU   B 1 34  ? 61.308 78.49   34.884 1   40.27  ? 56  LEU   B CD2 1 
ATOM   2973  N  N   . PHE   B 1 35  ? 64.636 75.412  33.431 1   37.2   ? 57  PHE   B N   1 
ATOM   2974  C  CA  . PHE   B 1 35  ? 64.547 74.615  32.218 1   36.43  ? 57  PHE   B CA  1 
ATOM   2975  C  C   . PHE   B 1 35  ? 64.944 73.149  32.488 1   36.32  ? 57  PHE   B C   1 
ATOM   2976  O  O   . PHE   B 1 35  ? 64.272 72.232  32.008 1   36.11  ? 57  PHE   B O   1 
ATOM   2977  C  CB  . PHE   B 1 35  ? 65.448 75.241  31.13  1   35.83  ? 57  PHE   B CB  1 
ATOM   2978  C  CG  . PHE   B 1 35  ? 65.296 74.633  29.749 1   35.63  ? 57  PHE   B CG  1 
ATOM   2979  C  CD1 . PHE   B 1 35  ? 64.234 74.981  28.936 1   35.58  ? 57  PHE   B CD1 1 
ATOM   2980  C  CD2 . PHE   B 1 35  ? 66.219 73.71   29.272 1   36     ? 57  PHE   B CD2 1 
ATOM   2981  C  CE1 . PHE   B 1 35  ? 64.083 74.404  27.681 1   36.67  ? 57  PHE   B CE1 1 
ATOM   2982  C  CE2 . PHE   B 1 35  ? 66.067 73.133  28.024 1   36.55  ? 57  PHE   B CE2 1 
ATOM   2983  C  CZ  . PHE   B 1 35  ? 65.007 73.496  27.224 1   36.75  ? 57  PHE   B CZ  1 
ATOM   2984  N  N   . ILE   B 1 36  ? 66.035 72.933  33.257 1   35.91  ? 58  ILE   B N   1 
ATOM   2985  C  CA  . ILE   B 1 36  ? 66.514 71.59   33.583 1   35.67  ? 58  ILE   B CA  1 
ATOM   2986  C  C   . ILE   B 1 36  ? 65.555 70.876  34.54  1   35.38  ? 58  ILE   B C   1 
ATOM   2987  O  O   . ILE   B 1 36  ? 65.078 69.792  34.221 1   35.56  ? 58  ILE   B O   1 
ATOM   2988  C  CB  . ILE   B 1 36  ? 67.974 71.632  34.117 1   35.88  ? 58  ILE   B CB  1 
ATOM   2989  C  CG1 . ILE   B 1 36  ? 68.948 72.111  33.034 1   35.62  ? 58  ILE   B CG1 1 
ATOM   2990  C  CG2 . ILE   B 1 36  ? 68.401 70.281  34.744 1   36.31  ? 58  ILE   B CG2 1 
ATOM   2991  C  CD1 . ILE   B 1 36  ? 70.319 72.404  33.556 1   36.17  ? 58  ILE   B CD1 1 
ATOM   2992  N  N   . ILE   B 1 37  ? 65.256 71.49   35.69  1   35.26  ? 59  ILE   B N   1 
ATOM   2993  C  CA  . ILE   B 1 37  ? 64.339 70.932  36.676 1   35.6   ? 59  ILE   B CA  1 
ATOM   2994  C  C   . ILE   B 1 37  ? 62.958 70.602  36.077 1   36.38  ? 59  ILE   B C   1 
ATOM   2995  O  O   . ILE   B 1 37  ? 62.472 69.488  36.296 1   37.35  ? 59  ILE   B O   1 
ATOM   2996  C  CB  . ILE   B 1 37  ? 64.247 71.844  37.91  1   35.68  ? 59  ILE   B CB  1 
ATOM   2997  C  CG1 . ILE   B 1 37  ? 65.598 71.876  38.679 1   36.8   ? 59  ILE   B CG1 1 
ATOM   2998  C  CG2 . ILE   B 1 37  ? 63.055 71.483  38.823 1   35.48  ? 59  ILE   B CG2 1 
ATOM   2999  C  CD1 . ILE   B 1 37  ? 65.954 70.608  39.442 1   37.83  ? 59  ILE   B CD1 1 
ATOM   3000  N  N   . THR   B 1 38  ? 62.354 71.52   35.288 1   35.28  ? 60  THR   B N   1 
ATOM   3001  C  CA  . THR   B 1 38  ? 61.044 71.272  34.66  1   35.18  ? 60  THR   B CA  1 
ATOM   3002  C  C   . THR   B 1 38  ? 61.096 70.022  33.767 1   35.69  ? 60  THR   B C   1 
ATOM   3003  O  O   . THR   B 1 38  ? 60.207 69.178  33.845 1   36.36  ? 60  THR   B O   1 
ATOM   3004  C  CB  . THR   B 1 38  ? 60.581 72.483  33.822 1   35.17  ? 60  THR   B CB  1 
ATOM   3005  O  OG1 . THR   B 1 38  ? 60.544 73.639  34.64  1   35.42  ? 60  THR   B OG1 1 
ATOM   3006  C  CG2 . THR   B 1 38  ? 59.226 72.264  33.16  1   35.59  ? 60  THR   B CG2 1 
ATOM   3007  N  N   . HIS   B 1 39  ? 62.159 69.892  32.959 1   34.82  ? 61  HIS   B N   1 
ATOM   3008  C  CA  . HIS   B 1 39  ? 62.326 68.757  32.071 1   34.87  ? 61  HIS   B CA  1 
ATOM   3009  C  C   . HIS   B 1 39  ? 62.532 67.476  32.833 1   34.55  ? 61  HIS   B C   1 
ATOM   3010  O  O   . HIS   B 1 39  ? 61.967 66.461  32.465 1   34.91  ? 61  HIS   B O   1 
ATOM   3011  C  CB  . HIS   B 1 39  ? 63.463 69.006  31.073 1   35.49  ? 61  HIS   B CB  1 
ATOM   3012  C  CG  . HIS   B 1 39  ? 63.015 69.696  29.818 1   37.34  ? 61  HIS   B CG  1 
ATOM   3013  N  ND1 . HIS   B 1 39  ? 62.838 71.076  29.771 1   39.32  ? 61  HIS   B ND1 1 
ATOM   3014  C  CD2 . HIS   B 1 39  ? 62.719 69.18   28.604 1   38.41  ? 61  HIS   B CD2 1 
ATOM   3015  C  CE1 . HIS   B 1 39  ? 62.442 71.349  28.54  1   39.42  ? 61  HIS   B CE1 1 
ATOM   3016  N  NE2 . HIS   B 1 39  ? 62.359 70.239  27.8   1   39.65  ? 61  HIS   B NE2 1 
ATOM   3017  N  N   . GLN   B 1 40  ? 63.294 67.522  33.917 1   34.29  ? 62  GLN   B N   1 
ATOM   3018  C  CA  . GLN   B 1 40  ? 63.544 66.355  34.757 1   34.65  ? 62  GLN   B CA  1 
ATOM   3019  C  C   . GLN   B 1 40  ? 62.308 65.935  35.561 1   36     ? 62  GLN   B C   1 
ATOM   3020  O  O   . GLN   B 1 40  ? 62.152 64.75   35.861 1   36.45  ? 62  GLN   B O   1 
ATOM   3021  C  CB  . GLN   B 1 40  ? 64.701 66.627  35.695 1   35.29  ? 62  GLN   B CB  1 
ATOM   3022  C  CG  . GLN   B 1 40  ? 66.044 66.729  34.999 1   36.17  ? 62  GLN   B CG  1 
ATOM   3023  C  CD  . GLN   B 1 40  ? 67.147 67.091  35.97  1   37.72  ? 62  GLN   B CD  1 
ATOM   3024  O  OE1 . GLN   B 1 40  ? 66.933 67.646  37.053 1   36.63  ? 62  GLN   B OE1 1 
ATOM   3025  N  NE2 . GLN   B 1 40  ? 68.363 66.779  35.6   1   38.88  ? 62  GLN   B NE2 1 
ATOM   3026  N  N   . ALA   B 1 41  ? 61.429 66.896  35.903 1   36.12  ? 63  ALA   B N   1 
ATOM   3027  C  CA  . ALA   B 1 41  ? 60.174 66.599  36.586 1   36.82  ? 63  ALA   B CA  1 
ATOM   3028  C  C   . ALA   B 1 41  ? 59.265 65.855  35.609 1   37.05  ? 63  ALA   B C   1 
ATOM   3029  O  O   . ALA   B 1 41  ? 58.651 64.852  35.99  1   37.49  ? 63  ALA   B O   1 
ATOM   3030  C  CB  . ALA   B 1 41  ? 59.505 67.881  37.04  1   37.44  ? 63  ALA   B CB  1 
ATOM   3031  N  N   . TYR   B 1 42  ? 59.235 66.295  34.319 1   36.25  ? 64  TYR   B N   1 
ATOM   3032  C  CA  . TYR   B 1 42  ? 58.493 65.635  33.265 1   35.93  ? 64  TYR   B CA  1 
ATOM   3033  C  C   . TYR   B 1 42  ? 58.988 64.199  33.122 1   35.71  ? 64  TYR   B C   1 
ATOM   3034  O  O   . TYR   B 1 42  ? 58.181 63.285  33.154 1   35.5   ? 64  TYR   B O   1 
ATOM   3035  C  CB  . TYR   B 1 42  ? 58.669 66.371  31.921 1   36.16  ? 64  TYR   B CB  1 
ATOM   3036  C  CG  . TYR   B 1 42  ? 57.605 67.41   31.632 1   37.08  ? 64  TYR   B CG  1 
ATOM   3037  C  CD1 . TYR   B 1 42  ? 56.345 67.039  31.181 1   37.57  ? 64  TYR   B CD1 1 
ATOM   3038  C  CD2 . TYR   B 1 42  ? 57.858 68.759  31.814 1   38.11  ? 64  TYR   B CD2 1 
ATOM   3039  C  CE1 . TYR   B 1 42  ? 55.361 67.99   30.932 1   38.38  ? 64  TYR   B CE1 1 
ATOM   3040  C  CE2 . TYR   B 1 42  ? 56.88  69.716  31.584 1   38.73  ? 64  TYR   B CE2 1 
ATOM   3041  C  CZ  . TYR   B 1 42  ? 55.639 69.331  31.122 1   39.09  ? 64  TYR   B CZ  1 
ATOM   3042  O  OH  . TYR   B 1 42  ? 54.687 70.292  30.895 1   39.5   ? 64  TYR   B OH  1 
ATOM   3043  N  N   . GLU   B 1 43  ? 60.306 64.001  33.061 1   35.9   ? 65  GLU   B N   1 
ATOM   3044  C  CA  . GLU   B 1 43  ? 60.917 62.683  32.87  1   36.41  ? 65  GLU   B CA  1 
ATOM   3045  C  C   . GLU   B 1 43  ? 60.703 61.744  34.024 1   36.05  ? 65  GLU   B C   1 
ATOM   3046  O  O   . GLU   B 1 43  ? 60.642 60.534  33.794 1   35.9   ? 65  GLU   B O   1 
ATOM   3047  C  CB  . GLU   B 1 43  ? 62.408 62.791  32.52  1   38.18  ? 65  GLU   B CB  1 
ATOM   3048  C  CG  . GLU   B 1 43  ? 62.639 63.398  31.146 1   39.76  ? 65  GLU   B CG  1 
ATOM   3049  C  CD  . GLU   B 1 43  ? 62.275 62.521  29.965 1   43.51  ? 65  GLU   B CD  1 
ATOM   3050  O  OE1 . GLU   B 1 43  ? 62.518 61.294  30.024 1   43.48  ? 65  GLU   B OE1 1 
ATOM   3051  O  OE2 . GLU   B 1 43  ? 61.776 63.072  28.96  1   45.32  ? 65  GLU   B OE2 1 
ATOM   3052  N  N   . LEU   B 1 44  ? 60.561 62.275  35.254 1   35.34  ? 66  LEU   B N   1 
ATOM   3053  C  CA  . LEU   B 1 44  ? 60.291 61.411  36.398 1   35.29  ? 66  LEU   B CA  1 
ATOM   3054  C  C   . LEU   B 1 44  ? 58.859 60.891  36.282 1   35.8   ? 66  LEU   B C   1 
ATOM   3055  O  O   . LEU   B 1 44  ? 58.616 59.695  36.453 1   35.64  ? 66  LEU   B O   1 
ATOM   3056  C  CB  . LEU   B 1 44  ? 60.478 62.154  37.73  1   35.19  ? 66  LEU   B CB  1 
ATOM   3057  C  CG  . LEU   B 1 44  ? 61.918 62.328  38.246 1   35.63  ? 66  LEU   B CG  1 
ATOM   3058  C  CD1 . LEU   B 1 44  ? 61.925 62.972  39.577 1   35.6   ? 66  LEU   B CD1 1 
ATOM   3059  C  CD2 . LEU   B 1 44  ? 62.645 61.002  38.335 1   35.94  ? 66  LEU   B CD2 1 
ATOM   3060  N  N   . TRP   B 1 45  ? 57.912 61.782  35.941 1   36.07  ? 67  TRP   B N   1 
ATOM   3061  C  CA  . TRP   B 1 45  ? 56.515 61.399  35.764 1   36.73  ? 67  TRP   B CA  1 
ATOM   3062  C  C   . TRP   B 1 45  ? 56.305 60.545  34.506 1   37.31  ? 67  TRP   B C   1 
ATOM   3063  O  O   . TRP   B 1 45  ? 55.382 59.745  34.475 1   37.35  ? 67  TRP   B O   1 
ATOM   3064  C  CB  . TRP   B 1 45  ? 55.579 62.623  35.83  1   36.93  ? 67  TRP   B CB  1 
ATOM   3065  C  CG  . TRP   B 1 45  ? 55.523 63.251  37.202 1   38.11  ? 67  TRP   B CG  1 
ATOM   3066  C  CD1 . TRP   B 1 45  ? 56     64.476  37.56  1   39.25  ? 67  TRP   B CD1 1 
ATOM   3067  C  CD2 . TRP   B 1 45  ? 55.033 62.642  38.416 1   38.51  ? 67  TRP   B CD2 1 
ATOM   3068  N  NE1 . TRP   B 1 45  ? 55.831 64.674  38.916 1   39.77  ? 67  TRP   B NE1 1 
ATOM   3069  C  CE2 . TRP   B 1 45  ? 55.233 63.565  39.46  1   39.33  ? 67  TRP   B CE2 1 
ATOM   3070  C  CE3 . TRP   B 1 45  ? 54.431 61.411  38.715 1   39.39  ? 67  TRP   B CE3 1 
ATOM   3071  C  CZ2 . TRP   B 1 45  ? 54.836 63.305  40.772 1   39.92  ? 67  TRP   B CZ2 1 
ATOM   3072  C  CZ3 . TRP   B 1 45  ? 54.026 61.162  40.014 1   39.89  ? 67  TRP   B CZ3 1 
ATOM   3073  C  CH2 . TRP   B 1 45  ? 54.227 62.103  41.022 1   40     ? 67  TRP   B CH2 1 
ATOM   3074  N  N   . PHE   B 1 46  ? 57.198 60.643  33.505 1   37.74  ? 68  PHE   B N   1 
ATOM   3075  C  CA  . PHE   B 1 46  ? 57.143 59.794  32.318 1   38.25  ? 68  PHE   B CA  1 
ATOM   3076  C  C   . PHE   B 1 46  ? 57.487 58.363  32.743 1   38.45  ? 68  PHE   B C   1 
ATOM   3077  O  O   . PHE   B 1 46  ? 56.773 57.431  32.398 1   38.75  ? 68  PHE   B O   1 
ATOM   3078  C  CB  . PHE   B 1 46  ? 58.12  60.29   31.236 1   38.49  ? 68  PHE   B CB  1 
ATOM   3079  C  CG  . PHE   B 1 46  ? 57.695 61.516  30.445 1   39.5   ? 68  PHE   B CG  1 
ATOM   3080  C  CD1 . PHE   B 1 46  ? 56.398 62.003  30.523 1   40.68  ? 68  PHE   B CD1 1 
ATOM   3081  C  CD2 . PHE   B 1 46  ? 58.606 62.21   29.676 1   39.9   ? 68  PHE   B CD2 1 
ATOM   3082  C  CE1 . PHE   B 1 46  ? 56.022 63.14   29.818 1   41.37  ? 68  PHE   B CE1 1 
ATOM   3083  C  CE2 . PHE   B 1 46  ? 58.226 63.344  28.973 1   40.71  ? 68  PHE   B CE2 1 
ATOM   3084  C  CZ  . PHE   B 1 46  ? 56.935 63.796  29.038 1   40.78  ? 68  PHE   B CZ  1 
ATOM   3085  N  N   . LYS   B 1 47  ? 58.528 58.195  33.564 1   38.56  ? 69  LYS   B N   1 
ATOM   3086  C  CA  . LYS   B 1 47  ? 58.926 56.893  34.095 1   38.77  ? 69  LYS   B CA  1 
ATOM   3087  C  C   . LYS   B 1 47  ? 57.771 56.26   34.896 1   39.68  ? 69  LYS   B C   1 
ATOM   3088  O  O   . LYS   B 1 47  ? 57.516 55.061  34.75  1   40.31  ? 69  LYS   B O   1 
ATOM   3089  C  CB  . LYS   B 1 47  ? 60.212 57.019  34.93  1   39.13  ? 69  LYS   B CB  1 
ATOM   3090  C  CG  . LYS   B 1 47  ? 60.75  55.679  35.39  1   41.57  ? 69  LYS   B CG  1 
ATOM   3091  C  CD  . LYS   B 1 47  ? 62.118 55.752  36.023 1   43.91  ? 69  LYS   B CD  1 
ATOM   3092  C  CE  . LYS   B 1 47  ? 62.407 54.45   36.738 1   47.48  ? 69  LYS   B CE  1 
ATOM   3093  N  NZ  . LYS   B 1 47  ? 63.862 54.184  36.945 1   50.19  ? 69  LYS   B NZ  1 
ATOM   3094  N  N   . GLN   B 1 48  ? 57.024 57.089  35.674 1   39.12  ? 70  GLN   B N   1 
ATOM   3095  C  CA  . GLN   B 1 48  ? 55.845 56.64   36.412 1   38.75  ? 70  GLN   B CA  1 
ATOM   3096  C  C   . GLN   B 1 48  ? 54.728 56.202  35.478 1   38.9   ? 70  GLN   B C   1 
ATOM   3097  O  O   . GLN   B 1 48  ? 54.202 55.105  35.651 1   38.74  ? 70  GLN   B O   1 
ATOM   3098  C  CB  . GLN   B 1 48  ? 55.321 57.721  37.37  1   39.27  ? 70  GLN   B CB  1 
ATOM   3099  C  CG  . GLN   B 1 48  ? 54.256 57.194  38.338 1   38.89  ? 70  GLN   B CG  1 
ATOM   3100  C  CD  . GLN   B 1 48  ? 54.823 56.117  39.242 1   37.49  ? 70  GLN   B CD  1 
ATOM   3101  O  OE1 . GLN   B 1 48  ? 55.911 56.258  39.777 1   37.85  ? 70  GLN   B OE1 1 
ATOM   3102  N  NE2 . GLN   B 1 48  ? 54.115 55.013  39.423 1   36.15  ? 70  GLN   B NE2 1 
ATOM   3103  N  N   . ILE   B 1 49  ? 54.392 57.025  34.462 1   39.19  ? 71  ILE   B N   1 
ATOM   3104  C  CA  . ILE   B 1 49  ? 53.339 56.7    33.482 1   39.75  ? 71  ILE   B CA  1 
ATOM   3105  C  C   . ILE   B 1 49  ? 53.647 55.399  32.764 1   39.66  ? 71  ILE   B C   1 
ATOM   3106  O  O   . ILE   B 1 49  ? 52.754 54.56   32.622 1   39.67  ? 71  ILE   B O   1 
ATOM   3107  C  CB  . ILE   B 1 49  ? 53.073 57.861  32.488 1   40.48  ? 71  ILE   B CB  1 
ATOM   3108  C  CG1 . ILE   B 1 49  ? 52.488 59.081  33.209 1   41.56  ? 71  ILE   B CG1 1 
ATOM   3109  C  CG2 . ILE   B 1 49  ? 52.145 57.432  31.363 1   40.9   ? 71  ILE   B CG2 1 
ATOM   3110  C  CD1 . ILE   B 1 49  ? 52.581 60.355  32.384 1   42.49  ? 71  ILE   B CD1 1 
ATOM   3111  N  N   . ILE   B 1 50  ? 54.922 55.208  32.359 1   39.44  ? 72  ILE   B N   1 
ATOM   3112  C  CA  . ILE   B 1 50  ? 55.365 53.982  31.679 1   39.67  ? 72  ILE   B CA  1 
ATOM   3113  C  C   . ILE   B 1 50  ? 55.202 52.772  32.585 1   40.06  ? 72  ILE   B C   1 
ATOM   3114  O  O   . ILE   B 1 50  ? 54.73  51.732  32.145 1   40.03  ? 72  ILE   B O   1 
ATOM   3115  C  CB  . ILE   B 1 50  ? 56.813 54.131  31.161 1   40.02  ? 72  ILE   B CB  1 
ATOM   3116  C  CG1 . ILE   B 1 50  ? 56.883 55.126  30.001 1   40.42  ? 72  ILE   B CG1 1 
ATOM   3117  C  CG2 . ILE   B 1 50  ? 57.415 52.786  30.745 1   40.68  ? 72  ILE   B CG2 1 
ATOM   3118  C  CD1 . ILE   B 1 50  ? 58.277 55.554  29.673 1   41.61  ? 72  ILE   B CD1 1 
ATOM   3119  N  N   . PHE   B 1 51  ? 55.55  52.927  33.861 1   40.43  ? 73  PHE   B N   1 
ATOM   3120  C  CA  . PHE   B 1 51  ? 55.443 51.872  34.848 1   41.01  ? 73  PHE   B CA  1 
ATOM   3121  C  C   . PHE   B 1 51  ? 53.994 51.441  35.03  1   42.07  ? 73  PHE   B C   1 
ATOM   3122  O  O   . PHE   B 1 51  ? 53.715 50.237  35.128 1   42.41  ? 73  PHE   B O   1 
ATOM   3123  C  CB  . PHE   B 1 51  ? 56.019 52.349  36.169 1   40.99  ? 73  PHE   B CB  1 
ATOM   3124  C  CG  . PHE   B 1 51  ? 56.191 51.241  37.171 1   42.03  ? 73  PHE   B CG  1 
ATOM   3125  C  CD1 . PHE   B 1 51  ? 57.153 50.258  36.986 1   42.54  ? 73  PHE   B CD1 1 
ATOM   3126  C  CD2 . PHE   B 1 51  ? 55.402 51.185  38.306 1   43.02  ? 73  PHE   B CD2 1 
ATOM   3127  C  CE1 . PHE   B 1 51  ? 57.317 49.246  37.918 1   43.44  ? 73  PHE   B CE1 1 
ATOM   3128  C  CE2 . PHE   B 1 51  ? 55.576 50.171  39.246 1   43.8   ? 73  PHE   B CE2 1 
ATOM   3129  C  CZ  . PHE   B 1 51  ? 56.528 49.209  39.047 1   43.4   ? 73  PHE   B CZ  1 
ATOM   3130  N  N   . GLU   B 1 52  ? 53.064 52.421  35.059 1   42.17  ? 74  GLU   B N   1 
ATOM   3131  C  CA  . GLU   B 1 52  ? 51.638 52.145  35.227 1   42.36  ? 74  GLU   B CA  1 
ATOM   3132  C  C   . GLU   B 1 52  ? 51.081 51.481  33.985 1   42.78  ? 74  GLU   B C   1 
ATOM   3133  O  O   . GLU   B 1 52  ? 50.371 50.486  34.09  1   42.86  ? 74  GLU   B O   1 
ATOM   3134  C  CB  . GLU   B 1 52  ? 50.844 53.415  35.577 1   43.48  ? 74  GLU   B CB  1 
ATOM   3135  C  CG  . GLU   B 1 52  ? 51.261 54.067  36.877 1   46.3   ? 74  GLU   B CG  1 
ATOM   3136  C  CD  . GLU   B 1 52  ? 51.093 53.246  38.144 1   51.22  ? 74  GLU   B CD  1 
ATOM   3137  O  OE1 . GLU   B 1 52  ? 50.257 52.314  38.157 1   48.79  ? 74  GLU   B OE1 1 
ATOM   3138  O  OE2 . GLU   B 1 52  ? 51.783 53.56   39.142 1   55.44  ? 74  GLU   B OE2 1 
ATOM   3139  N  N   . PHE   B 1 53  ? 51.453 52      32.813 1   42.92  ? 75  PHE   B N   1 
ATOM   3140  C  CA  . PHE   B 1 53  ? 51.042 51.454  31.534 1   43.49  ? 75  PHE   B CA  1 
ATOM   3141  C  C   . PHE   B 1 53  ? 51.507 50.024  31.348 1   43.73  ? 75  PHE   B C   1 
ATOM   3142  O  O   . PHE   B 1 53  ? 50.736 49.201  30.87  1   44.16  ? 75  PHE   B O   1 
ATOM   3143  C  CB  . PHE   B 1 53  ? 51.554 52.334  30.386 1   43.65  ? 75  PHE   B CB  1 
ATOM   3144  C  CG  . PHE   B 1 53  ? 50.671 53.497  29.99  1   44.51  ? 75  PHE   B CG  1 
ATOM   3145  C  CD1 . PHE   B 1 53  ? 49.542 53.82   30.73  1   45     ? 75  PHE   B CD1 1 
ATOM   3146  C  CD2 . PHE   B 1 53  ? 50.962 54.254  28.869 1   45.22  ? 75  PHE   B CD2 1 
ATOM   3147  C  CE1 . PHE   B 1 53  ? 48.719 54.863  30.348 1   45.61  ? 75  PHE   B CE1 1 
ATOM   3148  C  CE2 . PHE   B 1 53  ? 50.149 55.314  28.502 1   45.9   ? 75  PHE   B CE2 1 
ATOM   3149  C  CZ  . PHE   B 1 53  ? 49.035 55.613  29.247 1   45.62  ? 75  PHE   B CZ  1 
ATOM   3150  N  N   . ASP   B 1 54  ? 52.749 49.717  31.726 1   43.52  ? 76  ASP   B N   1 
ATOM   3151  C  CA  . ASP   B 1 54  ? 53.274 48.365  31.594 1   43.74  ? 76  ASP   B CA  1 
ATOM   3152  C  C   . ASP   B 1 54  ? 52.548 47.39   32.487 1   43.65  ? 76  ASP   B C   1 
ATOM   3153  O  O   . ASP   B 1 54  ? 52.258 46.3    32.039 1   43.89  ? 76  ASP   B O   1 
ATOM   3154  C  CB  . ASP   B 1 54  ? 54.784 48.321  31.799 1   45.84  ? 76  ASP   B CB  1 
ATOM   3155  C  CG  . ASP   B 1 54  ? 55.555 48.829  30.594 1   51.78  ? 76  ASP   B CG  1 
ATOM   3156  O  OD1 . ASP   B 1 54  ? 55.03  48.723  29.459 1   52.37  ? 76  ASP   B OD1 1 
ATOM   3157  O  OD2 . ASP   B 1 54  ? 56.684 49.331  30.783 1   55.08  ? 76  ASP   B OD2 1 
ATOM   3158  N  N   . SER   B 1 55  ? 52.164 47.801  33.699 1   43.48  ? 77  SER   B N   1 
ATOM   3159  C  CA  . SER   B 1 55  ? 51.408 46.936  34.598 1   43.61  ? 77  SER   B CA  1 
ATOM   3160  C  C   . SER   B 1 55  ? 49.969 46.736  34.117 1   44.62  ? 77  SER   B C   1 
ATOM   3161  O  O   . SER   B 1 55  ? 49.449 45.627  34.213 1   45.4   ? 77  SER   B O   1 
ATOM   3162  C  CB  . SER   B 1 55  ? 51.436 47.486  36.016 1   44.14  ? 77  SER   B CB  1 
ATOM   3163  O  OG  . SER   B 1 55  ? 50.67  48.672  36.158 1   45.34  ? 77  SER   B OG  1 
ATOM   3164  N  N   . ILE   B 1 56  ? 49.339 47.784  33.567 1   44.93  ? 78  ILE   B N   1 
ATOM   3165  C  CA  . ILE   B 1 56  ? 47.99  47.687  33.001 1   46.29  ? 78  ILE   B CA  1 
ATOM   3166  C  C   . ILE   B 1 56  ? 48     46.78   31.757 1   48.37  ? 78  ILE   B C   1 
ATOM   3167  O  O   . ILE   B 1 56  ? 47.057 46.019  31.541 1   48.66  ? 78  ILE   B O   1 
ATOM   3168  C  CB  . ILE   B 1 56  ? 47.41  49.084  32.67  1   45.96  ? 78  ILE   B CB  1 
ATOM   3169  C  CG1 . ILE   B 1 56  ? 47.204 49.911  33.947 1   46.21  ? 78  ILE   B CG1 1 
ATOM   3170  C  CG2 . ILE   B 1 56  ? 46.105 48.982  31.878 1   45.9   ? 78  ILE   B CG2 1 
ATOM   3171  C  CD1 . ILE   B 1 56  ? 47.029 51.352  33.663 1   46.92  ? 78  ILE   B CD1 1 
ATOM   3172  N  N   . ARG   B 1 57  ? 49.083 46.832  30.963 1   49.42  ? 79  ARG   B N   1 
ATOM   3173  C  CA  . ARG   B 1 57  ? 49.237 45.988  29.789 1   50.56  ? 79  ARG   B CA  1 
ATOM   3174  C  C   . ARG   B 1 57  ? 49.33  44.542  30.211 1   51.6   ? 79  ARG   B C   1 
ATOM   3175  O  O   . ARG   B 1 57  ? 48.654 43.704  29.624 1   51.71  ? 79  ARG   B O   1 
ATOM   3176  C  CB  . ARG   B 1 57  ? 50.48  46.372  28.979 1   52.19  ? 79  ARG   B CB  1 
ATOM   3177  C  CG  . ARG   B 1 57  ? 50.336 47.649  28.126 1   55.82  ? 79  ARG   B CG  1 
ATOM   3178  C  CD  . ARG   B 1 57  ? 51.453 47.893  27.102 1   59.24  ? 79  ARG   B CD  1 
ATOM   3179  N  NE  . ARG   B 1 57  ? 52.757 47.385  27.541 1   63.03  ? 79  ARG   B NE  1 
ATOM   3180  C  CZ  . ARG   B 1 57  ? 53.311 46.261  27.09  1   65.63  ? 79  ARG   B CZ  1 
ATOM   3181  N  NH1 . ARG   B 1 57  ? 52.698 45.535  26.162 1   64.31  ? 79  ARG   B NH1 1 
ATOM   3182  N  NH2 . ARG   B 1 57  ? 54.471 45.844  27.581 1   66.43  ? 79  ARG   B NH2 1 
ATOM   3183  N  N   . ASP   B 1 58  ? 50.111 44.245  31.264 1   52.46  ? 80  ASP   B N   1 
ATOM   3184  C  CA  . ASP   B 1 58  ? 50.263 42.876  31.769 1   54.04  ? 80  ASP   B CA  1 
ATOM   3185  C  C   . ASP   B 1 58  ? 48.94  42.332  32.309 1   55.8   ? 80  ASP   B C   1 
ATOM   3186  O  O   . ASP   B 1 58  ? 48.644 41.15   32.146 1   56.04  ? 80  ASP   B O   1 
ATOM   3187  C  CB  . ASP   B 1 58  ? 51.369 42.793  32.828 1   55.55  ? 80  ASP   B CB  1 
ATOM   3188  C  CG  . ASP   B 1 58  ? 52.759 43.184  32.345 1   60.56  ? 80  ASP   B CG  1 
ATOM   3189  O  OD1 . ASP   B 1 58  ? 52.901 43.539  31.152 1   61.09  ? 80  ASP   B OD1 1 
ATOM   3190  O  OD2 . ASP   B 1 58  ? 53.706 43.155  33.168 1   63.39  ? 80  ASP   B OD2 1 
ATOM   3191  N  N   . MET   B 1 59  ? 48.126 43.202  32.914 1   56.84  ? 81  MET   B N   1 
ATOM   3192  C  CA  . MET   B 1 59  ? 46.818 42.823  33.426 1   58.19  ? 81  MET   B CA  1 
ATOM   3193  C  C   . MET   B 1 59  ? 45.819 42.577  32.289 1   59.8   ? 81  MET   B C   1 
ATOM   3194  O  O   . MET   B 1 59  ? 44.967 41.7    32.399 1   60.04  ? 81  MET   B O   1 
ATOM   3195  C  CB  . MET   B 1 59  ? 46.294 43.895  34.389 1   58.42  ? 81  MET   B CB  1 
ATOM   3196  C  CG  . MET   B 1 59  ? 46.962 43.859  35.742 1   59.31  ? 81  MET   B CG  1 
ATOM   3197  S  SD  . MET   B 1 59  ? 46.106 44.877  36.963 1   60.2   ? 81  MET   B SD  1 
ATOM   3198  C  CE  . MET   B 1 59  ? 46.668 46.517  36.458 1   57.46  ? 81  MET   B CE  1 
ATOM   3199  N  N   . LEU   B 1 60  ? 45.924 43.346  31.2   1   60.74  ? 82  LEU   B N   1 
ATOM   3200  C  CA  . LEU   B 1 60  ? 45.043 43.181  30.043 1   62.09  ? 82  LEU   B CA  1 
ATOM   3201  C  C   . LEU   B 1 60  ? 45.459 42.02   29.127 1   64.33  ? 82  LEU   B C   1 
ATOM   3202  O  O   . LEU   B 1 60  ? 44.647 41.564  28.321 1   64.41  ? 82  LEU   B O   1 
ATOM   3203  C  CB  . LEU   B 1 60  ? 44.96  44.479  29.231 1   61.44  ? 82  LEU   B CB  1 
ATOM   3204  C  CG  . LEU   B 1 60  ? 44.177 45.608  29.863 1   61.36  ? 82  LEU   B CG  1 
ATOM   3205  C  CD1 . LEU   B 1 60  ? 44.301 46.851  29.051 1   61.54  ? 82  LEU   B CD1 1 
ATOM   3206  C  CD2 . LEU   B 1 60  ? 42.738 45.246  30.012 1   61.49  ? 82  LEU   B CD2 1 
ATOM   3207  N  N   . ASP   B 1 61  ? 46.714 41.539  29.252 1   65.97  ? 83  ASP   B N   1 
ATOM   3208  C  CA  . ASP   B 1 61  ? 47.26  40.431  28.464 1   68.07  ? 83  ASP   B CA  1 
ATOM   3209  C  C   . ASP   B 1 61  ? 46.882 39.096  29.115 1   70.28  ? 83  ASP   B C   1 
ATOM   3210  O  O   . ASP   B 1 61  ? 47.741 38.255  29.383 1   70.64  ? 83  ASP   B O   1 
ATOM   3211  C  CB  . ASP   B 1 61  ? 48.793 40.569  28.357 1   69.85  ? 83  ASP   B CB  1 
ATOM   3212  C  CG  . ASP   B 1 61  ? 49.405 39.885  27.152 1   73.97  ? 83  ASP   B CG  1 
ATOM   3213  O  OD1 . ASP   B 1 61  ? 49.484 40.529  26.084 1   74.63  ? 83  ASP   B OD1 1 
ATOM   3214  O  OD2 . ASP   B 1 61  ? 49.818 38.707  27.28  1   75.59  ? 83  ASP   B OD2 1 
ATOM   3215  N  N   . ALA   B 1 62  ? 45.586 38.922  29.403 1   71.62  ? 84  ALA   B N   1 
ATOM   3216  C  CA  . ALA   B 1 62  ? 45.025 37.721  30.025 1   73.02  ? 84  ALA   B CA  1 
ATOM   3217  C  C   . ALA   B 1 62  ? 43.638 37.453  29.434 1   74.16  ? 84  ALA   B C   1 
ATOM   3218  O  O   . ALA   B 1 62  ? 42.92  38.392  29.09  1   74.08  ? 84  ALA   B O   1 
ATOM   3219  C  CB  . ALA   B 1 62  ? 44.926 37.907  31.532 1   73.16  ? 84  ALA   B CB  1 
ATOM   3220  N  N   . GLU   B 1 63  ? 43.268 36.176  29.29  1   75.07  ? 85  GLU   B N   1 
ATOM   3221  C  CA  . GLU   B 1 63  ? 41.961 35.807  28.732 1   76.12  ? 85  GLU   B CA  1 
ATOM   3222  C  C   . GLU   B 1 63  ? 40.78  36.109  29.701 1   76.52  ? 85  GLU   B C   1 
ATOM   3223  O  O   . GLU   B 1 63  ? 39.641 36.3    29.26  1   76.79  ? 85  GLU   B O   1 
ATOM   3224  C  CB  . GLU   B 1 63  ? 41.966 34.331  28.29  1   78.41  ? 85  GLU   B CB  1 
ATOM   3225  C  CG  . GLU   B 1 63  ? 42.276 34.131  26.818 1   83.26  ? 85  GLU   B CG  1 
ATOM   3226  C  CD  . GLU   B 1 63  ? 41.06  33.79   25.972 1   90.49  ? 85  GLU   B CD  1 
ATOM   3227  O  OE1 . GLU   B 1 63  ? 40.65  32.604  25.966 1   92.74  ? 85  GLU   B OE1 1 
ATOM   3228  O  OE2 . GLU   B 1 63  ? 40.515 34.708  25.317 1   91.47  ? 85  GLU   B OE2 1 
ATOM   3229  N  N   . VAL   B 1 64  ? 41.074 36.155  31.016 1   76.06  ? 86  VAL   B N   1 
ATOM   3230  C  CA  . VAL   B 1 64  ? 40.111 36.423  32.083 1   75.41  ? 86  VAL   B CA  1 
ATOM   3231  C  C   . VAL   B 1 64  ? 40.468 37.708  32.844 1   73.74  ? 86  VAL   B C   1 
ATOM   3232  O  O   . VAL   B 1 64  ? 41.505 37.775  33.522 1   73.86  ? 86  VAL   B O   1 
ATOM   3233  C  CB  . VAL   B 1 64  ? 39.968 35.204  33.051 1   76.58  ? 86  VAL   B CB  1 
ATOM   3234  C  CG1 . VAL   B 1 64  ? 41.335 34.639  33.472 1   77.14  ? 86  VAL   B CG1 1 
ATOM   3235  C  CG2 . VAL   B 1 64  ? 39.118 35.559  34.272 1   76.94  ? 86  VAL   B CG2 1 
ATOM   3236  N  N   . ILE   B 1 65  ? 39.623 38.742  32.707 1   71.83  ? 87  ILE   B N   1 
ATOM   3237  C  CA  . ILE   B 1 65  ? 39.835 39.983  33.442 1   70.44  ? 87  ILE   B CA  1 
ATOM   3238  C  C   . ILE   B 1 65  ? 38.654 40.163  34.385 1   68.56  ? 87  ILE   B C   1 
ATOM   3239  O  O   . ILE   B 1 65  ? 37.593 40.639  33.978 1   68.79  ? 87  ILE   B O   1 
ATOM   3240  C  CB  . ILE   B 1 65  ? 40.105 41.2    32.528 1   70.77  ? 87  ILE   B CB  1 
ATOM   3241  C  CG1 . ILE   B 1 65  ? 41.305 40.912  31.588 1   71.86  ? 87  ILE   B CG1 1 
ATOM   3242  C  CG2 . ILE   B 1 65  ? 40.36  42.45   33.366 1   70.85  ? 87  ILE   B CG2 1 
ATOM   3243  C  CD1 . ILE   B 1 65  ? 41.155 41.44   30.186 1   73.29  ? 87  ILE   B CD1 1 
ATOM   3244  N  N   . ASP   B 1 66  ? 38.815 39.709  35.634 1   66.41  ? 88  ASP   B N   1 
ATOM   3245  C  CA  . ASP   B 1 66  ? 37.733 39.76   36.612 1   65.07  ? 88  ASP   B CA  1 
ATOM   3246  C  C   . ASP   B 1 66  ? 37.473 41.169  37.165 1   63.54  ? 88  ASP   B C   1 
ATOM   3247  O  O   . ASP   B 1 66  ? 38.202 42.104  36.846 1   63.75  ? 88  ASP   B O   1 
ATOM   3248  C  CB  . ASP   B 1 66  ? 37.949 38.727  37.746 1   66.12  ? 88  ASP   B CB  1 
ATOM   3249  C  CG  . ASP   B 1 66  ? 39.171 38.954  38.606 1   68.84  ? 88  ASP   B CG  1 
ATOM   3250  O  OD1 . ASP   B 1 66  ? 40.142 39.513  38.104 1   69.16  ? 88  ASP   B OD1 1 
ATOM   3251  O  OD2 . ASP   B 1 66  ? 39.155 38.544  39.779 1   70.96  ? 88  ASP   B OD2 1 
ATOM   3252  N  N   . GLU   B 1 67  ? 36.4   41.322  37.959 1   61.9   ? 89  GLU   B N   1 
ATOM   3253  C  CA  . GLU   B 1 67  ? 36.017 42.593  38.557 1   60.71  ? 89  GLU   B CA  1 
ATOM   3254  C  C   . GLU   B 1 67  ? 37.138 43.164  39.424 1   58.69  ? 89  GLU   B C   1 
ATOM   3255  O  O   . GLU   B 1 67  ? 37.304 44.377  39.47  1   59.22  ? 89  GLU   B O   1 
ATOM   3256  C  CB  . GLU   B 1 67  ? 34.778 42.424  39.436 1   63.39  ? 89  GLU   B CB  1 
ATOM   3257  C  CG  . GLU   B 1 67  ? 33.53  41.885  38.775 1   68.83  ? 89  GLU   B CG  1 
ATOM   3258  C  CD  . GLU   B 1 67  ? 32.368 41.932  39.749 1   77.99  ? 89  GLU   B CD  1 
ATOM   3259  O  OE1 . GLU   B 1 67  ? 31.678 42.977  39.777 1   80.74  ? 89  GLU   B OE1 1 
ATOM   3260  O  OE2 . GLU   B 1 67  ? 32.175 40.957  40.515 1   80.22  ? 89  GLU   B OE2 1 
ATOM   3261  N  N   . THR   B 1 68  ? 37.886 42.306  40.118 1   56.42  ? 90  THR   B N   1 
ATOM   3262  C  CA  . THR   B 1 68  ? 38.975 42.739  40.991 1   54.85  ? 90  THR   B CA  1 
ATOM   3263  C  C   . THR   B 1 68  ? 40.154 43.317  40.184 1   53.05  ? 90  THR   B C   1 
ATOM   3264  O  O   . THR   B 1 68  ? 40.664 44.382  40.543 1   53.28  ? 90  THR   B O   1 
ATOM   3265  C  CB  . THR   B 1 68  ? 39.371 41.605  41.96  1   55.85  ? 90  THR   B CB  1 
ATOM   3266  O  OG1 . THR   B 1 68  ? 38.197 41.1    42.612 1   56.65  ? 90  THR   B OG1 1 
ATOM   3267  C  CG2 . THR   B 1 68  ? 40.352 42.06   43.007 1   56.11  ? 90  THR   B CG2 1 
ATOM   3268  N  N   . LYS   B 1 69  ? 40.561 42.659  39.077 1   51.05  ? 91  LYS   B N   1 
ATOM   3269  C  CA  . LYS   B 1 69  ? 41.636 43.198  38.242 1   49.71  ? 91  LYS   B CA  1 
ATOM   3270  C  C   . LYS   B 1 69  ? 41.173 44.481  37.53  1   47.69  ? 91  LYS   B C   1 
ATOM   3271  O  O   . LYS   B 1 69  ? 41.963 45.412  37.379 1   47.33  ? 91  LYS   B O   1 
ATOM   3272  C  CB  . LYS   B 1 69  ? 42.133 42.165  37.224 1   51.66  ? 91  LYS   B CB  1 
ATOM   3273  C  CG  . LYS   B 1 69  ? 42.851 40.984  37.851 1   56.21  ? 91  LYS   B CG  1 
ATOM   3274  C  CD  . LYS   B 1 69  ? 44.27  41.301  38.252 1   61.78  ? 91  LYS   B CD  1 
ATOM   3275  C  CE  . LYS   B 1 69  ? 44.818 40.234  39.172 1   66.11  ? 91  LYS   B CE  1 
ATOM   3276  N  NZ  . LYS   B 1 69  ? 44.545 38.865  38.656 1   68.57  ? 91  LYS   B NZ  1 
ATOM   3277  N  N   . THR   B 1 70  ? 39.888 44.538  37.13  1   46.13  ? 92  THR   B N   1 
ATOM   3278  C  CA  . THR   B 1 70  ? 39.3   45.699  36.463 1   45.26  ? 92  THR   B CA  1 
ATOM   3279  C  C   . THR   B 1 70  ? 39.378 46.929  37.347 1   43.51  ? 92  THR   B C   1 
ATOM   3280  O  O   . THR   B 1 70  ? 39.767 47.98   36.873 1   43.59  ? 92  THR   B O   1 
ATOM   3281  C  CB  . THR   B 1 70  ? 37.873 45.401  35.977 1   46.84  ? 92  THR   B CB  1 
ATOM   3282  O  OG1 . THR   B 1 70  ? 37.914 44.374  34.984 1   48.07  ? 92  THR   B OG1 1 
ATOM   3283  C  CG2 . THR   B 1 70  ? 37.208 46.606  35.385 1   46.94  ? 92  THR   B CG2 1 
ATOM   3284  N  N   . LEU   B 1 71  ? 39.073 46.787  38.637 1   42.21  ? 93  LEU   B N   1 
ATOM   3285  C  CA  . LEU   B 1 71  ? 39.156 47.859  39.633 1   41.2   ? 93  LEU   B CA  1 
ATOM   3286  C  C   . LEU   B 1 71  ? 40.585 48.397  39.759 1   40.03  ? 93  LEU   B C   1 
ATOM   3287  O  O   . LEU   B 1 71  ? 40.771 49.6    39.891 1   40.39  ? 93  LEU   B O   1 
ATOM   3288  C  CB  . LEU   B 1 71  ? 38.68  47.342  41.012 1   41.16  ? 93  LEU   B CB  1 
ATOM   3289  C  CG  . LEU   B 1 71  ? 37.168 47.19   41.207 1   41.61  ? 93  LEU   B CG  1 
ATOM   3290  C  CD1 . LEU   B 1 71  ? 36.852 46.486  42.516 1   41.58  ? 93  LEU   B CD1 1 
ATOM   3291  C  CD2 . LEU   B 1 71  ? 36.498 48.536  41.224 1   42.31  ? 93  LEU   B CD2 1 
ATOM   3292  N  N   . GLU   B 1 72  ? 41.588 47.519  39.736 1   39.03  ? 94  GLU   B N   1 
ATOM   3293  C  CA  . GLU   B 1 72  ? 42.984 47.935  39.816 1   39.27  ? 94  GLU   B CA  1 
ATOM   3294  C  C   . GLU   B 1 72  ? 43.426 48.645  38.543 1   39.5   ? 94  GLU   B C   1 
ATOM   3295  O  O   . GLU   B 1 72  ? 44.216 49.58   38.608 1   40.5   ? 94  GLU   B O   1 
ATOM   3296  C  CB  . GLU   B 1 72  ? 43.895 46.736  40.131 1   42.19  ? 94  GLU   B CB  1 
ATOM   3297  C  CG  . GLU   B 1 72  ? 45.301 47.116  40.571 1   47.7   ? 94  GLU   B CG  1 
ATOM   3298  C  CD  . GLU   B 1 72  ? 45.4   47.747  41.946 1   56.4   ? 94  GLU   B CD  1 
ATOM   3299  O  OE1 . GLU   B 1 72  ? 44.429 47.628  42.728 1   59.1   ? 94  GLU   B OE1 1 
ATOM   3300  O  OE2 . GLU   B 1 72  ? 46.459 48.343  42.252 1   59.62  ? 94  GLU   B OE2 1 
ATOM   3301  N  N   . ILE   B 1 73  ? 42.899 48.242  37.389 1   39.11  ? 95  ILE   B N   1 
ATOM   3302  C  CA  . ILE   B 1 73  ? 43.193 48.914  36.125 1   39.35  ? 95  ILE   B CA  1 
ATOM   3303  C  C   . ILE   B 1 73  ? 42.599 50.324  36.174 1   39.93  ? 95  ILE   B C   1 
ATOM   3304  O  O   . ILE   B 1 73  ? 43.295 51.277  35.83  1   40.8   ? 95  ILE   B O   1 
ATOM   3305  C  CB  . ILE   B 1 73  ? 42.692 48.1    34.904 1   39.06  ? 95  ILE   B CB  1 
ATOM   3306  C  CG1 . ILE   B 1 73  ? 43.487 46.784  34.76  1   39.15  ? 95  ILE   B CG1 1 
ATOM   3307  C  CG2 . ILE   B 1 73  ? 42.795 48.921  33.623 1   38.93  ? 95  ILE   B CG2 1 
ATOM   3308  C  CD1 . ILE   B 1 73  ? 42.894 45.804  33.847 1   39.86  ? 95  ILE   B CD1 1 
ATOM   3309  N  N   . VAL   B 1 74  ? 41.353 50.467  36.686 1   39.12  ? 96  VAL   B N   1 
ATOM   3310  C  CA  . VAL   B 1 74  ? 40.702 51.768  36.84  1   38.87  ? 96  VAL   B CA  1 
ATOM   3311  C  C   . VAL   B 1 74  ? 41.489 52.703  37.802 1   39.57  ? 96  VAL   B C   1 
ATOM   3312  O  O   . VAL   B 1 74  ? 41.676 53.883  37.506 1   39.31  ? 96  VAL   B O   1 
ATOM   3313  C  CB  . VAL   B 1 74  ? 39.224 51.599  37.225 1   38.73  ? 96  VAL   B CB  1 
ATOM   3314  C  CG1 . VAL   B 1 74  ? 38.57  52.936  37.543 1   38.62  ? 96  VAL   B CG1 1 
ATOM   3315  C  CG2 . VAL   B 1 74  ? 38.471 50.908  36.109 1   39.43  ? 96  VAL   B CG2 1 
ATOM   3316  N  N   . LYS   B 1 75  ? 42.02  52.158  38.895 1   40.4   ? 97  LYS   B N   1 
ATOM   3317  C  CA  . LYS   B 1 75  ? 42.818 52.925  39.851 1   41.68  ? 97  LYS   B CA  1 
ATOM   3318  C  C   . LYS   B 1 75  ? 44.071 53.5    39.192 1   42.63  ? 97  LYS   B C   1 
ATOM   3319  O  O   . LYS   B 1 75  ? 44.396 54.676  39.382 1   43.12  ? 97  LYS   B O   1 
ATOM   3320  C  CB  . LYS   B 1 75  ? 43.214 52.029  41.042 1   43.99  ? 97  LYS   B CB  1 
ATOM   3321  C  CG  . LYS   B 1 75  ? 44.174 52.676  42.031 1   49.25  ? 97  LYS   B CG  1 
ATOM   3322  C  CD  . LYS   B 1 75  ? 44.036 52.093  43.439 1   55.01  ? 97  LYS   B CD  1 
ATOM   3323  C  CE  . LYS   B 1 75  ? 44.866 50.86   43.633 1   59.1   ? 97  LYS   B CE  1 
ATOM   3324  N  NZ  . LYS   B 1 75  ? 44.34  49.998  44.728 1   61.2   ? 97  LYS   B NZ  1 
ATOM   3325  N  N   . ARG   B 1 76  ? 44.767 52.667  38.411 1   42.65  ? 98  ARG   B N   1 
ATOM   3326  C  CA  . ARG   B 1 76  ? 46.001 53.054  37.734 1   42.77  ? 98  ARG   B CA  1 
ATOM   3327  C  C   . ARG   B 1 76  ? 45.754 53.962  36.536 1   42.85  ? 98  ARG   B C   1 
ATOM   3328  O  O   . ARG   B 1 76  ? 46.564 54.847  36.283 1   43.44  ? 98  ARG   B O   1 
ATOM   3329  C  CB  . ARG   B 1 76  ? 46.827 51.811  37.377 1   43.42  ? 98  ARG   B CB  1 
ATOM   3330  C  CG  . ARG   B 1 76  ? 47.18  51.034  38.638 1   44.51  ? 98  ARG   B CG  1 
ATOM   3331  C  CD  . ARG   B 1 76  ? 47.89  49.744  38.349 1   46.44  ? 98  ARG   B CD  1 
ATOM   3332  N  NE  . ARG   B 1 76  ? 48.145 49.026  39.596 1   48.32  ? 98  ARG   B NE  1 
ATOM   3333  C  CZ  . ARG   B 1 76  ? 48.789 47.868  39.682 1   49.29  ? 98  ARG   B CZ  1 
ATOM   3334  N  NH1 . ARG   B 1 76  ? 49.274 47.289  38.594 1   46.98  ? 98  ARG   B NH1 1 
ATOM   3335  N  NH2 . ARG   B 1 76  ? 48.976 47.291  40.864 1   49.86  ? 98  ARG   B NH2 1 
ATOM   3336  N  N   . LEU   B 1 77  ? 44.622 53.802  35.837 1   42.07  ? 99  LEU   B N   1 
ATOM   3337  C  CA  . LEU   B 1 77  ? 44.279 54.692  34.73  1   41.58  ? 99  LEU   B CA  1 
ATOM   3338  C  C   . LEU   B 1 77  ? 43.958 56.055  35.271 1   41.27  ? 99  LEU   B C   1 
ATOM   3339  O  O   . LEU   B 1 77  ? 44.436 57.035  34.727 1   41.92  ? 99  LEU   B O   1 
ATOM   3340  C  CB  . LEU   B 1 77  ? 43.103 54.168  33.903 1   41.69  ? 99  LEU   B CB  1 
ATOM   3341  C  CG  . LEU   B 1 77  ? 43.432 53.025  32.941 1   42.85  ? 99  LEU   B CG  1 
ATOM   3342  C  CD1 . LEU   B 1 77  ? 42.177 52.476  32.307 1   43.35  ? 99  LEU   B CD1 1 
ATOM   3343  C  CD2 . LEU   B 1 77  ? 44.437 53.454  31.871 1   42.83  ? 99  LEU   B CD2 1 
ATOM   3344  N  N   . ASN   B 1 78  ? 43.203 56.125  36.38  1   40.55  ? 100 ASN   B N   1 
ATOM   3345  C  CA  . ASN   B 1 78  ? 42.86  57.374  37.03  1   40.39  ? 100 ASN   B CA  1 
ATOM   3346  C  C   . ASN   B 1 78  ? 44.115 58.075  37.614 1   39.97  ? 100 ASN   B C   1 
ATOM   3347  O  O   . ASN   B 1 78  ? 44.216 59.303  37.573 1   40.43  ? 100 ASN   B O   1 
ATOM   3348  C  CB  . ASN   B 1 78  ? 41.818 57.12   38.084 1   42.09  ? 100 ASN   B CB  1 
ATOM   3349  C  CG  . ASN   B 1 78  ? 41.292 58.386  38.69  1   46.61  ? 100 ASN   B CG  1 
ATOM   3350  O  OD1 . ASN   B 1 78  ? 41.833 58.882  39.681 1   49.24  ? 100 ASN   B OD1 1 
ATOM   3351  N  ND2 . ASN   B 1 78  ? 40.227 58.937  38.118 1   46.36  ? 100 ASN   B ND2 1 
ATOM   3352  N  N   . ARG   B 1 79  ? 45.087 57.299  38.099 1   38.67  ? 101 ARG   B N   1 
ATOM   3353  C  CA  . ARG   B 1 79  ? 46.359 57.83   38.579 1   38.05  ? 101 ARG   B CA  1 
ATOM   3354  C  C   . ARG   B 1 79  ? 47.126 58.513  37.429 1   38.2   ? 101 ARG   B C   1 
ATOM   3355  O  O   . ARG   B 1 79  ? 47.625 59.616  37.61  1   38.61  ? 101 ARG   B O   1 
ATOM   3356  C  CB  . ARG   B 1 79  ? 47.194 56.696  39.162 1   38.21  ? 101 ARG   B CB  1 
ATOM   3357  C  CG  . ARG   B 1 79  ? 48.574 57.093  39.648 1   37.67  ? 101 ARG   B CG  1 
ATOM   3358  C  CD  . ARG   B 1 79  ? 49.29  55.884  40.162 1   38.43  ? 101 ARG   B CD  1 
ATOM   3359  N  NE  . ARG   B 1 79  ? 48.592 55.344  41.324 1   40.85  ? 101 ARG   B NE  1 
ATOM   3360  C  CZ  . ARG   B 1 79  ? 48.885 54.193  41.914 1   42.92  ? 101 ARG   B CZ  1 
ATOM   3361  N  NH1 . ARG   B 1 79  ? 49.863 53.427  41.447 1   42.92  ? 101 ARG   B NH1 1 
ATOM   3362  N  NH2 . ARG   B 1 79  ? 48.2   53.793  42.97  1   43.38  ? 101 ARG   B NH2 1 
ATOM   3363  N  N   . VAL   B 1 80  ? 47.174 57.886  36.24  1   37.77  ? 102 VAL   B N   1 
ATOM   3364  C  CA  . VAL   B 1 80  ? 47.816 58.442  35.044 1   37.45  ? 102 VAL   B CA  1 
ATOM   3365  C  C   . VAL   B 1 80  ? 47.104 59.733  34.62  1   37.89  ? 102 VAL   B C   1 
ATOM   3366  O  O   . VAL   B 1 80  ? 47.766 60.686  34.229 1   38.54  ? 102 VAL   B O   1 
ATOM   3367  C  CB  . VAL   B 1 80  ? 47.861 57.395  33.902 1   37.6   ? 102 VAL   B CB  1 
ATOM   3368  C  CG1 . VAL   B 1 80  ? 48.173 58.033  32.554 1   38.04  ? 102 VAL   B CG1 1 
ATOM   3369  C  CG2 . VAL   B 1 80  ? 48.858 56.292  34.216 1   37.6   ? 102 VAL   B CG2 1 
ATOM   3370  N  N   . VAL   B 1 81  ? 45.763 59.784  34.746 1   37.47  ? 103 VAL   B N   1 
ATOM   3371  C  CA  . VAL   B 1 81  ? 44.96  60.976  34.46  1   37.02  ? 103 VAL   B CA  1 
ATOM   3372  C  C   . VAL   B 1 81  ? 45.405 62.14   35.368 1   37.54  ? 103 VAL   B C   1 
ATOM   3373  O  O   . VAL   B 1 81  ? 45.526 63.268  34.901 1   38.14  ? 103 VAL   B O   1 
ATOM   3374  C  CB  . VAL   B 1 81  ? 43.456 60.653  34.635 1   37.04  ? 103 VAL   B CB  1 
ATOM   3375  C  CG1 . VAL   B 1 81  ? 42.614 61.918  34.793 1   37.21  ? 103 VAL   B CG1 1 
ATOM   3376  C  CG2 . VAL   B 1 81  ? 42.948 59.821  33.465 1   37.32  ? 103 VAL   B CG2 1 
ATOM   3377  N  N   . LEU   B 1 82  ? 45.664 61.861  36.658 1   37.18  ? 104 LEU   B N   1 
ATOM   3378  C  CA  . LEU   B 1 82  ? 46.115 62.876  37.603 1   37.29  ? 104 LEU   B CA  1 
ATOM   3379  C  C   . LEU   B 1 82  ? 47.538 63.337  37.275 1   37.35  ? 104 LEU   B C   1 
ATOM   3380  O  O   . LEU   B 1 82  ? 47.848 64.516  37.414 1   37.64  ? 104 LEU   B O   1 
ATOM   3381  C  CB  . LEU   B 1 82  ? 46.089 62.332  39.033 1   37.84  ? 104 LEU   B CB  1 
ATOM   3382  C  CG  . LEU   B 1 82  ? 44.737 61.99   39.653 1   39.46  ? 104 LEU   B CG  1 
ATOM   3383  C  CD1 . LEU   B 1 82  ? 44.919 61.535  41.069 1   39.35  ? 104 LEU   B CD1 1 
ATOM   3384  C  CD2 . LEU   B 1 82  ? 43.824 63.172  39.653 1   40.33  ? 104 LEU   B CD2 1 
ATOM   3385  N  N   . ILE   B 1 83  ? 48.402 62.408  36.861 1   36.72  ? 105 ILE   B N   1 
ATOM   3386  C  CA  . ILE   B 1 83  ? 49.776 62.721  36.492 1   36.76  ? 105 ILE   B CA  1 
ATOM   3387  C  C   . ILE   B 1 83  ? 49.814 63.577  35.229 1   36.79  ? 105 ILE   B C   1 
ATOM   3388  O  O   . ILE   B 1 83  ? 50.608 64.505  35.132 1   36.61  ? 105 ILE   B O   1 
ATOM   3389  C  CB  . ILE   B 1 83  ? 50.585 61.415  36.338 1   36.95  ? 105 ILE   B CB  1 
ATOM   3390  C  CG1 . ILE   B 1 83  ? 50.675 60.683  37.689 1   37.37  ? 105 ILE   B CG1 1 
ATOM   3391  C  CG2 . ILE   B 1 83  ? 51.969 61.689  35.761 1   37.07  ? 105 ILE   B CG2 1 
ATOM   3392  C  CD1 . ILE   B 1 83  ? 51.225 59.288  37.565 1   38.97  ? 105 ILE   B CD1 1 
ATOM   3393  N  N   . LEU   B 1 84  ? 48.933 63.289  34.275 1   36.98  ? 106 LEU   B N   1 
ATOM   3394  C  CA  . LEU   B 1 84  ? 48.855 64.05   33.041 1   37.45  ? 106 LEU   B CA  1 
ATOM   3395  C  C   . LEU   B 1 84  ? 48.357 65.448  33.323 1   37.82  ? 106 LEU   B C   1 
ATOM   3396  O  O   . LEU   B 1 84  ? 48.949 66.38   32.801 1   38.69  ? 106 LEU   B O   1 
ATOM   3397  C  CB  . LEU   B 1 84  ? 47.994 63.338  31.982 1   37.69  ? 106 LEU   B CB  1 
ATOM   3398  C  CG  . LEU   B 1 84  ? 48.693 62.187  31.219 1   37.76  ? 106 LEU   B CG  1 
ATOM   3399  C  CD1 . LEU   B 1 84  ? 47.707 61.364  30.441 1   37.52  ? 106 LEU   B CD1 1 
ATOM   3400  C  CD2 . LEU   B 1 84  ? 49.743 62.719  30.3   1   37.74  ? 106 LEU   B CD2 1 
ATOM   3401  N  N   . LYS   B 1 85  ? 47.346 65.622  34.209 1   37.08  ? 107 LYS   B N   1 
ATOM   3402  C  CA  . LYS   B 1 85  ? 46.858 66.961  34.58  1   36.83  ? 107 LYS   B CA  1 
ATOM   3403  C  C   . LYS   B 1 85  ? 47.967 67.806  35.19  1   36.14  ? 107 LYS   B C   1 
ATOM   3404  O  O   . LYS   B 1 85  ? 48.022 69.015  34.956 1   36.14  ? 107 LYS   B O   1 
ATOM   3405  C  CB  . LYS   B 1 85  ? 45.703 66.878  35.591 1   38.82  ? 107 LYS   B CB  1 
ATOM   3406  C  CG  . LYS   B 1 85  ? 44.365 66.435  35.02  1   42.9   ? 107 LYS   B CG  1 
ATOM   3407  C  CD  . LYS   B 1 85  ? 43.302 66.46   36.118 1   47.04  ? 107 LYS   B CD  1 
ATOM   3408  C  CE  . LYS   B 1 85  ? 42.088 65.595  35.84  1   49.86  ? 107 LYS   B CE  1 
ATOM   3409  N  NZ  . LYS   B 1 85  ? 41.421 65.149  37.114 1   49.86  ? 107 LYS   B NZ  1 
ATOM   3410  N  N   . LEU   B 1 86  ? 48.822 67.168  36.004 1   35.46  ? 108 LEU   B N   1 
ATOM   3411  C  CA  . LEU   B 1 86  ? 49.952 67.788  36.677 1   35.1   ? 108 LEU   B CA  1 
ATOM   3412  C  C   . LEU   B 1 86  ? 50.956 68.262  35.643 1   35.85  ? 108 LEU   B C   1 
ATOM   3413  O  O   . LEU   B 1 86  ? 51.445 69.391  35.739 1   36.49  ? 108 LEU   B O   1 
ATOM   3414  C  CB  . LEU   B 1 86  ? 50.609 66.773  37.625 1   34.85  ? 108 LEU   B CB  1 
ATOM   3415  C  CG  . LEU   B 1 86  ? 51.684 67.317  38.581 1   35.58  ? 108 LEU   B CG  1 
ATOM   3416  C  CD1 . LEU   B 1 86  ? 51.069 68.037  39.75  1   35.08  ? 108 LEU   B CD1 1 
ATOM   3417  C  CD2 . LEU   B 1 86  ? 52.602 66.221  39.052 1   35.91  ? 108 LEU   B CD2 1 
ATOM   3418  N  N   . LEU   B 1 87  ? 51.251 67.419  34.636 1   35.51  ? 109 LEU   B N   1 
ATOM   3419  C  CA  . LEU   B 1 87  ? 52.19  67.755  33.579 1   35.11  ? 109 LEU   B CA  1 
ATOM   3420  C  C   . LEU   B 1 87  ? 51.682 68.866  32.669 1   35.9   ? 109 LEU   B C   1 
ATOM   3421  O  O   . LEU   B 1 87  ? 52.482 69.692  32.235 1   37.08  ? 109 LEU   B O   1 
ATOM   3422  C  CB  . LEU   B 1 87  ? 52.596 66.509  32.798 1   34.64  ? 109 LEU   B CB  1 
ATOM   3423  C  CG  . LEU   B 1 87  ? 53.302 65.422  33.619 1   34.58  ? 109 LEU   B CG  1 
ATOM   3424  C  CD1 . LEU   B 1 87  ? 53.624 64.22   32.749 1   35.25  ? 109 LEU   B CD1 1 
ATOM   3425  C  CD2 . LEU   B 1 87  ? 54.546 65.946  34.317 1   33.94  ? 109 LEU   B CD2 1 
ATOM   3426  N  N   . VAL   B 1 88  ? 50.367 68.952  32.431 1   35.31  ? 110 VAL   B N   1 
ATOM   3427  C  CA  . VAL   B 1 88  ? 49.81  70.078  31.662 1   34.98  ? 110 VAL   B CA  1 
ATOM   3428  C  C   . VAL   B 1 88  ? 50.045 71.403  32.441 1   35.55  ? 110 VAL   B C   1 
ATOM   3429  O  O   . VAL   B 1 88  ? 50.359 72.435  31.854 1   35.62  ? 110 VAL   B O   1 
ATOM   3430  C  CB  . VAL   B 1 88  ? 48.32  69.869  31.349 1   34.76  ? 110 VAL   B CB  1 
ATOM   3431  C  CG1 . VAL   B 1 88  ? 47.729 71.096  30.682 1   35.07  ? 110 VAL   B CG1 1 
ATOM   3432  C  CG2 . VAL   B 1 88  ? 48.119 68.652  30.481 1   35.11  ? 110 VAL   B CG2 1 
ATOM   3433  N  N   . ASP   B 1 89  ? 49.95  71.35   33.769 1   36.15  ? 111 ASP   B N   1 
ATOM   3434  C  CA  . ASP   B 1 89  ? 50.163 72.498  34.641 1   37.37  ? 111 ASP   B CA  1 
ATOM   3435  C  C   . ASP   B 1 89  ? 51.624 72.903  34.816 1   38.47  ? 111 ASP   B C   1 
ATOM   3436  O  O   . ASP   B 1 89  ? 51.882 73.936  35.435 1   39.56  ? 111 ASP   B O   1 
ATOM   3437  C  CB  . ASP   B 1 89  ? 49.523 72.249  36.012 1   39.37  ? 111 ASP   B CB  1 
ATOM   3438  C  CG  . ASP   B 1 89  ? 48.009 72.246  36.014 1   46.13  ? 111 ASP   B CG  1 
ATOM   3439  O  OD1 . ASP   B 1 89  ? 47.409 72.395  34.924 1   48.69  ? 111 ASP   B OD1 1 
ATOM   3440  O  OD2 . ASP   B 1 89  ? 47.421 72.098  37.099 1   48.8   ? 111 ASP   B OD2 1 
ATOM   3441  N  N   . GLN   B 1 90  ? 52.575 72.092  34.332 1   37.91  ? 112 GLN   B N   1 
ATOM   3442  C  CA  . GLN   B 1 90  ? 53.992 72.42   34.43  1   37.91  ? 112 GLN   B CA  1 
ATOM   3443  C  C   . GLN   B 1 90  ? 54.419 73.383  33.328 1   38.49  ? 112 GLN   B C   1 
ATOM   3444  O  O   . GLN   B 1 90  ? 55.428 74.053  33.487 1   39.81  ? 112 GLN   B O   1 
ATOM   3445  C  CB  . GLN   B 1 90  ? 54.863 71.16   34.444 1   39.36  ? 112 GLN   B CB  1 
ATOM   3446  C  CG  . GLN   B 1 90  ? 54.68  70.316  35.716 1   42.42  ? 112 GLN   B CG  1 
ATOM   3447  C  CD  . GLN   B 1 90  ? 55.723 69.226  35.889 1   45.17  ? 112 GLN   B CD  1 
ATOM   3448  O  OE1 . GLN   B 1 90  ? 56.694 69.122  35.122 1   45.52  ? 112 GLN   B OE1 1 
ATOM   3449  N  NE2 . GLN   B 1 90  ? 55.541 68.386  36.914 1   45.51  ? 112 GLN   B NE2 1 
ATOM   3450  N  N   . VAL   B 1 91  ? 53.674 73.454  32.209 1   37.65  ? 113 VAL   B N   1 
ATOM   3451  C  CA  . VAL   B 1 91  ? 53.957 74.374  31.119 1   37.09  ? 113 VAL   B CA  1 
ATOM   3452  C  C   . VAL   B 1 91  ? 53.929 75.842  31.596 1   37.54  ? 113 VAL   B C   1 
ATOM   3453  O  O   . VAL   B 1 91  ? 54.922 76.541  31.393 1   38.05  ? 113 VAL   B O   1 
ATOM   3454  C  CB  . VAL   B 1 91  ? 53.04  74.129  29.897 1   36.76  ? 113 VAL   B CB  1 
ATOM   3455  C  CG1 . VAL   B 1 91  ? 53.379 75.072  28.753 1   36.43  ? 113 VAL   B CG1 1 
ATOM   3456  C  CG2 . VAL   B 1 91  ? 53.099 72.677  29.452 1   36.86  ? 113 VAL   B CG2 1 
ATOM   3457  N  N   . PRO   B 1 92  ? 52.87  76.329  32.297 1   37.06  ? 114 PRO   B N   1 
ATOM   3458  C  CA  . PRO   B 1 92  ? 52.884 77.735  32.756 1   36.86  ? 114 PRO   B CA  1 
ATOM   3459  C  C   . PRO   B 1 92  ? 54.059 78.115  33.665 1   36.74  ? 114 PRO   B C   1 
ATOM   3460  O  O   . PRO   B 1 92  ? 54.403 79.292  33.76  1   36.92  ? 114 PRO   B O   1 
ATOM   3461  C  CB  . PRO   B 1 92  ? 51.532 77.893  33.459 1   37.13  ? 114 PRO   B CB  1 
ATOM   3462  C  CG  . PRO   B 1 92  ? 50.676 76.807  32.89  1   37.01  ? 114 PRO   B CG  1 
ATOM   3463  C  CD  . PRO   B 1 92  ? 51.588 75.675  32.635 1   35.86  ? 114 PRO   B CD  1 
ATOM   3464  N  N   . ILE   B 1 93  ? 54.692 77.121  34.305 1   36.39  ? 115 ILE   B N   1 
ATOM   3465  C  CA  . ILE   B 1 93  ? 55.863 77.353  35.146 1   36.95  ? 115 ILE   B CA  1 
ATOM   3466  C  C   . ILE   B 1 93  ? 57.074 77.645  34.258 1   37.6   ? 115 ILE   B C   1 
ATOM   3467  O  O   . ILE   B 1 93  ? 57.847 78.556  34.566 1   38.39  ? 115 ILE   B O   1 
ATOM   3468  C  CB  . ILE   B 1 93  ? 56.125 76.161  36.094 1   37.25  ? 115 ILE   B CB  1 
ATOM   3469  C  CG1 . ILE   B 1 93  ? 54.924 75.928  37.04  1   38.01  ? 115 ILE   B CG1 1 
ATOM   3470  C  CG2 . ILE   B 1 93  ? 57.418 76.382  36.876 1   37.38  ? 115 ILE   B CG2 1 
ATOM   3471  C  CD1 . ILE   B 1 93  ? 55.046 74.66   37.913 1   39.16  ? 115 ILE   B CD1 1 
ATOM   3472  N  N   . LEU   B 1 94  ? 57.239 76.889  33.145 1   36.89  ? 116 LEU   B N   1 
ATOM   3473  C  CA  . LEU   B 1 94  ? 58.335 77.16   32.222 1   36.67  ? 116 LEU   B CA  1 
ATOM   3474  C  C   . LEU   B 1 94  ? 58.075 78.465  31.433 1   37.46  ? 116 LEU   B C   1 
ATOM   3475  O  O   . LEU   B 1 94  ? 59.024 79.191  31.111 1   37.81  ? 116 LEU   B O   1 
ATOM   3476  C  CB  . LEU   B 1 94  ? 58.623 75.975  31.29  1   35.97  ? 116 LEU   B CB  1 
ATOM   3477  C  CG  . LEU   B 1 94  ? 59.972 76.019  30.542 1   36.49  ? 116 LEU   B CG  1 
ATOM   3478  C  CD1 . LEU   B 1 94  ? 61.141 76.242  31.493 1   37.28  ? 116 LEU   B CD1 1 
ATOM   3479  C  CD2 . LEU   B 1 94  ? 60.222 74.743  29.779 1   36.48  ? 116 LEU   B CD2 1 
ATOM   3480  N  N   . GLU   B 1 95  ? 56.785 78.798  31.174 1   37.14  ? 117 GLU   B N   1 
ATOM   3481  C  CA  . GLU   B 1 95  ? 56.407 80.045  30.512 1   37.54  ? 117 GLU   B CA  1 
ATOM   3482  C  C   . GLU   B 1 95  ? 56.836 81.306  31.312 1   38.56  ? 117 GLU   B C   1 
ATOM   3483  O  O   . GLU   B 1 95  ? 56.755 82.421  30.784 1   39.34  ? 117 GLU   B O   1 
ATOM   3484  C  CB  . GLU   B 1 95  ? 54.905 80.072  30.204 1   39.35  ? 117 GLU   B CB  1 
ATOM   3485  C  CG  . GLU   B 1 95  ? 54.504 79.056  29.155 1   45.5   ? 117 GLU   B CG  1 
ATOM   3486  C  CD  . GLU   B 1 95  ? 53.05  79.081  28.733 1   53.43  ? 117 GLU   B CD  1 
ATOM   3487  O  OE1 . GLU   B 1 95  ? 52.172 78.894  29.607 1   56.16  ? 117 GLU   B OE1 1 
ATOM   3488  O  OE2 . GLU   B 1 95  ? 52.784 79.276  27.525 1   55.37  ? 117 GLU   B OE2 1 
ATOM   3489  N  N   . THR   B 1 96  ? 57.271 81.132  32.576 1   38.42  ? 118 THR   B N   1 
ATOM   3490  C  CA  . THR   B 1 96  ? 57.789 82.184  33.454 1   39.02  ? 118 THR   B CA  1 
ATOM   3491  C  C   . THR   B 1 96  ? 59.148 82.741  32.934 1   40.18  ? 118 THR   B C   1 
ATOM   3492  O  O   . THR   B 1 96  ? 59.505 83.889  33.218 1   40.07  ? 118 THR   B O   1 
ATOM   3493  C  CB  . THR   B 1 96  ? 57.872 81.645  34.882 1   39.71  ? 118 THR   B CB  1 
ATOM   3494  O  OG1 . THR   B 1 96  ? 56.563 81.279  35.285 1   39.98  ? 118 THR   B OG1 1 
ATOM   3495  C  CG2 . THR   B 1 96  ? 58.362 82.657  35.854 1   41.21  ? 118 THR   B CG2 1 
ATOM   3496  N  N   . MET   B 1 97  ? 59.874 81.927  32.136 1   40.84  ? 119 MET   B N   1 
ATOM   3497  C  CA  . MET   B 1 97  ? 61.144 82.261  31.517 1   41.73  ? 119 MET   B CA  1 
ATOM   3498  C  C   . MET   B 1 97  ? 60.911 83.183  30.319 1   42.68  ? 119 MET   B C   1 
ATOM   3499  O  O   . MET   B 1 97  ? 59.992 82.937  29.532 1   43.28  ? 119 MET   B O   1 
ATOM   3500  C  CB  . MET   B 1 97  ? 61.834 80.969  31.073 1   42     ? 119 MET   B CB  1 
ATOM   3501  C  CG  . MET   B 1 97  ? 63.078 81.183  30.247 1   43.14  ? 119 MET   B CG  1 
ATOM   3502  S  SD  . MET   B 1 97  ? 63.951 79.627  29.985 1   43.88  ? 119 MET   B SD  1 
ATOM   3503  C  CE  . MET   B 1 97  ? 62.678 78.681  29.105 1   40.76  ? 119 MET   B CE  1 
ATOM   3504  N  N   . THR   B 1 98  ? 61.719 84.251  30.184 1   42.38  ? 120 THR   B N   1 
ATOM   3505  C  CA  . THR   B 1 98  ? 61.547 85.165  29.063 1   42.24  ? 120 THR   B CA  1 
ATOM   3506  C  C   . THR   B 1 98  ? 62.216 84.619  27.81  1   41.94  ? 120 THR   B C   1 
ATOM   3507  O  O   . THR   B 1 98  ? 63.202 83.876  27.893 1   41.3   ? 120 THR   B O   1 
ATOM   3508  C  CB  . THR   B 1 98  ? 61.969 86.604  29.422 1   43.49  ? 120 THR   B CB  1 
ATOM   3509  O  OG1 . THR   B 1 98  ? 63.386 86.732  29.418 1   44.98  ? 120 THR   B OG1 1 
ATOM   3510  C  CG2 . THR   B 1 98  ? 61.377 87.077  30.718 1   43.36  ? 120 THR   B CG2 1 
ATOM   3511  N  N   . PRO   B 1 99  ? 61.676 84.981  26.622 1   42.09  ? 121 PRO   B N   1 
ATOM   3512  C  CA  . PRO   B 1 99  ? 62.269 84.498  25.367 1   42.39  ? 121 PRO   B CA  1 
ATOM   3513  C  C   . PRO   B 1 99  ? 63.722 84.924  25.153 1   43.21  ? 121 PRO   B C   1 
ATOM   3514  O  O   . PRO   B 1 99  ? 64.486 84.221  24.489 1   43.75  ? 121 PRO   B O   1 
ATOM   3515  C  CB  . PRO   B 1 99  ? 61.339 85.076  24.298 1   42.46  ? 121 PRO   B CB  1 
ATOM   3516  C  CG  . PRO   B 1 99  ? 60.074 85.393  25.016 1   42.43  ? 121 PRO   B CG  1 
ATOM   3517  C  CD  . PRO   B 1 99  ? 60.501 85.832  26.36  1   41.04  ? 121 PRO   B CD  1 
ATOM   3518  N  N   . LEU   B 1 100 ? 64.104 86.065  25.715 1   43.5   ? 122 LEU   B N   1 
ATOM   3519  C  CA  . LEU   B 1 100 ? 65.475 86.583  25.62  1   44.47  ? 122 LEU   B CA  1 
ATOM   3520  C  C   . LEU   B 1 100 ? 66.403 85.872  26.566 1   45     ? 122 LEU   B C   1 
ATOM   3521  O  O   . LEU   B 1 100 ? 67.573 85.725  26.25  1   45.15  ? 122 LEU   B O   1 
ATOM   3522  C  CB  . LEU   B 1 100 ? 65.533 88.086  25.861 1   44.91  ? 122 LEU   B CB  1 
ATOM   3523  C  CG  . LEU   B 1 100 ? 64.495 88.862  25.085 1   46.88  ? 122 LEU   B CG  1 
ATOM   3524  C  CD1 . LEU   B 1 100 ? 63.236 89.154  25.985 1   48.27  ? 122 LEU   B CD1 1 
ATOM   3525  C  CD2 . LEU   B 1 100 ? 65.117 90.026  24.337 1   46.83  ? 122 LEU   B CD2 1 
ATOM   3526  N  N   . ASP   B 1 101 ? 65.895 85.446  27.737 1   45.34  ? 123 ASP   B N   1 
ATOM   3527  C  CA  . ASP   B 1 101 ? 66.672 84.651  28.683 1   45.87  ? 123 ASP   B CA  1 
ATOM   3528  C  C   . ASP   B 1 101 ? 66.896 83.277  28.044 1   45.98  ? 123 ASP   B C   1 
ATOM   3529  O  O   . ASP   B 1 101 ? 68.013 82.787  28.05  1   46.35  ? 123 ASP   B O   1 
ATOM   3530  C  CB  . ASP   B 1 101 ? 65.944 84.5    30.029 1   47.72  ? 123 ASP   B CB  1 
ATOM   3531  C  CG  . ASP   B 1 101 ? 66.082 85.69   30.949 1   52.69  ? 123 ASP   B CG  1 
ATOM   3532  O  OD1 . ASP   B 1 101 ? 67.037 86.477  30.762 1   53.38  ? 123 ASP   B OD1 1 
ATOM   3533  O  OD2 . ASP   B 1 101 ? 65.226 85.842  31.857 1   55.26  ? 123 ASP   B OD2 1 
ATOM   3534  N  N   . PHE   B 1 102 ? 65.856 82.689  27.439 1   45.71  ? 124 PHE   B N   1 
ATOM   3535  C  CA  . PHE   B 1 102 ? 65.971 81.403  26.763 1   45.84  ? 124 PHE   B CA  1 
ATOM   3536  C  C   . PHE   B 1 102 ? 66.961 81.474  25.612 1   46.58  ? 124 PHE   B C   1 
ATOM   3537  O  O   . PHE   B 1 102 ? 67.758 80.56   25.437 1   46.73  ? 124 PHE   B O   1 
ATOM   3538  C  CB  . PHE   B 1 102 ? 64.606 80.946  26.251 1   45.2   ? 124 PHE   B CB  1 
ATOM   3539  C  CG  . PHE   B 1 102 ? 64.648 79.583  25.62  1   45.13  ? 124 PHE   B CG  1 
ATOM   3540  C  CD1 . PHE   B 1 102 ? 65.176 78.503  26.305 1   45.36  ? 124 PHE   B CD1 1 
ATOM   3541  C  CD2 . PHE   B 1 102 ? 64.13  79.373  24.354 1   45.76  ? 124 PHE   B CD2 1 
ATOM   3542  C  CE1 . PHE   B 1 102 ? 65.214 77.247  25.729 1   46.13  ? 124 PHE   B CE1 1 
ATOM   3543  C  CE2 . PHE   B 1 102 ? 64.149 78.111  23.783 1   46.62  ? 124 PHE   B CE2 1 
ATOM   3544  C  CZ  . PHE   B 1 102 ? 64.698 77.055  24.471 1   46.4   ? 124 PHE   B CZ  1 
ATOM   3545  N  N   . MET   B 1 103 ? 66.944 82.577  24.857 1   47.06  ? 125 MET   B N   1 
ATOM   3546  C  CA  . MET   B 1 103 ? 67.846 82.783  23.727 1   48.1   ? 125 MET   B CA  1 
ATOM   3547  C  C   . MET   B 1 103 ? 69.336 82.785  24.143 1   49     ? 125 MET   B C   1 
ATOM   3548  O  O   . MET   B 1 103 ? 70.192 82.371  23.362 1   49.86  ? 125 MET   B O   1 
ATOM   3549  C  CB  . MET   B 1 103 ? 67.479 84.091  23.005 1   48.99  ? 125 MET   B CB  1 
ATOM   3550  C  CG  . MET   B 1 103 ? 68.016 84.17   21.583 1   51.26  ? 125 MET   B CG  1 
ATOM   3551  S  SD  . MET   B 1 103 ? 67.42  85.586  20.604 1   55.48  ? 125 MET   B SD  1 
ATOM   3552  C  CE  . MET   B 1 103 ? 65.878 84.931  19.983 1   52.32  ? 125 MET   B CE  1 
ATOM   3553  N  N   . ASP   B 1 104 ? 69.634 83.204  25.381 1   48.88  ? 126 ASP   B N   1 
ATOM   3554  C  CA  . ASP   B 1 104 ? 70.992 83.301  25.909 1   49.33  ? 126 ASP   B CA  1 
ATOM   3555  C  C   . ASP   B 1 104 ? 71.624 81.974  26.335 1   49.71  ? 126 ASP   B C   1 
ATOM   3556  O  O   . ASP   B 1 104 ? 72.808 81.951  26.674 1   49.94  ? 126 ASP   B O   1 
ATOM   3557  C  CB  . ASP   B 1 104 ? 71.049 84.306  27.067 1   51.31  ? 126 ASP   B CB  1 
ATOM   3558  C  CG  . ASP   B 1 104 ? 70.872 85.761  26.662 1   57.06  ? 126 ASP   B CG  1 
ATOM   3559  O  OD1 . ASP   B 1 104 ? 70.728 86.036  25.421 1   57.86  ? 126 ASP   B OD1 1 
ATOM   3560  O  OD2 . ASP   B 1 104 ? 70.86  86.631  27.574 1   59.16  ? 126 ASP   B OD2 1 
ATOM   3561  N  N   . PHE   B 1 105 ? 70.86  80.879  26.336 1   49.62  ? 127 PHE   B N   1 
ATOM   3562  C  CA  . PHE   B 1 105 ? 71.42  79.566  26.676 1   50.1   ? 127 PHE   B CA  1 
ATOM   3563  C  C   . PHE   B 1 105 ? 71.027 78.478  25.654 1   51.35  ? 127 PHE   B C   1 
ATOM   3564  O  O   . PHE   B 1 105 ? 71.549 77.378  25.728 1   51.82  ? 127 PHE   B O   1 
ATOM   3565  C  CB  . PHE   B 1 105 ? 71.119 79.136  28.14  1   49.47  ? 127 PHE   B CB  1 
ATOM   3566  C  CG  . PHE   B 1 105 ? 69.717 78.681  28.478 1   49.4   ? 127 PHE   B CG  1 
ATOM   3567  C  CD1 . PHE   B 1 105 ? 69.345 77.359  28.33  1   49.57  ? 127 PHE   B CD1 1 
ATOM   3568  C  CD2 . PHE   B 1 105 ? 68.789 79.568  28.993 1   50.03  ? 127 PHE   B CD2 1 
ATOM   3569  C  CE1 . PHE   B 1 105 ? 68.065 76.944  28.649 1   50.08  ? 127 PHE   B CE1 1 
ATOM   3570  C  CE2 . PHE   B 1 105 ? 67.511 79.146  29.318 1   50.28  ? 127 PHE   B CE2 1 
ATOM   3571  C  CZ  . PHE   B 1 105 ? 67.163 77.835  29.156 1   49.89  ? 127 PHE   B CZ  1 
ATOM   3572  N  N   . ARG   B 1 106 ? 70.138 78.785  24.701 1   51.94  ? 128 ARG   B N   1 
ATOM   3573  C  CA  . ARG   B 1 106 ? 69.667 77.879  23.653 1   53.47  ? 128 ARG   B CA  1 
ATOM   3574  C  C   . ARG   B 1 106 ? 70.831 77.275  22.815 1   54.67  ? 128 ARG   B C   1 
ATOM   3575  O  O   . ARG   B 1 106 ? 70.695 76.186  22.262 1   54.99  ? 128 ARG   B O   1 
ATOM   3576  C  CB  . ARG   B 1 106 ? 68.689 78.658  22.747 1   55.02  ? 128 ARG   B CB  1 
ATOM   3577  C  CG  . ARG   B 1 106 ? 67.945 77.818  21.742 1   58.86  ? 128 ARG   B CG  1 
ATOM   3578  C  CD  . ARG   B 1 106 ? 66.693 78.517  21.266 1   63.36  ? 128 ARG   B CD  1 
ATOM   3579  N  NE  . ARG   B 1 106 ? 66.964 79.746  20.52  1   67.16  ? 128 ARG   B NE  1 
ATOM   3580  C  CZ  . ARG   B 1 106 ? 67.057 79.815  19.191 1   69.61  ? 128 ARG   B CZ  1 
ATOM   3581  N  NH1 . ARG   B 1 106 ? 66.933 78.717  18.448 1   69.02  ? 128 ARG   B NH1 1 
ATOM   3582  N  NH2 . ARG   B 1 106 ? 67.304 80.977  18.596 1   69     ? 128 ARG   B NH2 1 
ATOM   3583  N  N   . LYS   B 1 107 ? 71.973 77.982  22.759 1   54.88  ? 129 LYS   B N   1 
ATOM   3584  C  CA  . LYS   B 1 107 ? 73.188 77.604  22.042 1   55.6   ? 129 LYS   B CA  1 
ATOM   3585  C  C   . LYS   B 1 107 ? 73.724 76.248  22.513 1   55.59  ? 129 LYS   B C   1 
ATOM   3586  O  O   . LYS   B 1 107 ? 74.225 75.463  21.709 1   55.73  ? 129 LYS   B O   1 
ATOM   3587  C  CB  . LYS   B 1 107 ? 74.279 78.668  22.276 1   58.48  ? 129 LYS   B CB  1 
ATOM   3588  C  CG  . LYS   B 1 107 ? 73.828 80.12   22.077 1   63.73  ? 129 LYS   B CG  1 
ATOM   3589  C  CD  . LYS   B 1 107 ? 73.357 80.807  23.378 1   67.76  ? 129 LYS   B CD  1 
ATOM   3590  C  CE  . LYS   B 1 107 ? 73.517 82.313  23.321 1   71.67  ? 129 LYS   B CE  1 
ATOM   3591  N  NZ  . LYS   B 1 107 ? 74.685 82.793  24.12  1   73.73  ? 129 LYS   B NZ  1 
ATOM   3592  N  N   . TYR   B 1 108 ? 73.626 75.979  23.821 1   55.18  ? 130 TYR   B N   1 
ATOM   3593  C  CA  . TYR   B 1 108 ? 74.128 74.744  24.42  1   55.44  ? 130 TYR   B CA  1 
ATOM   3594  C  C   . TYR   B 1 108 ? 73.202 73.526  24.223 1   55.88  ? 130 TYR   B C   1 
ATOM   3595  O  O   . TYR   B 1 108 ? 73.541 72.43   24.667 1   56.26  ? 130 TYR   B O   1 
ATOM   3596  C  CB  . TYR   B 1 108 ? 74.416 74.957  25.919 1   55.64  ? 130 TYR   B CB  1 
ATOM   3597  C  CG  . TYR   B 1 108 ? 75.219 76.202  26.248 1   57.07  ? 130 TYR   B CG  1 
ATOM   3598  C  CD1 . TYR   B 1 108 ? 76.604 76.216  26.128 1   58.11  ? 130 TYR   B CD1 1 
ATOM   3599  C  CD2 . TYR   B 1 108 ? 74.598 77.35   26.717 1   58.32  ? 130 TYR   B CD2 1 
ATOM   3600  C  CE1 . TYR   B 1 108 ? 77.343 77.361  26.417 1   59.26  ? 130 TYR   B CE1 1 
ATOM   3601  C  CE2 . TYR   B 1 108 ? 75.324 78.501  27.002 1   59.47  ? 130 TYR   B CE2 1 
ATOM   3602  C  CZ  . TYR   B 1 108 ? 76.699 78.507  26.849 1   60.41  ? 130 TYR   B CZ  1 
ATOM   3603  O  OH  . TYR   B 1 108 ? 77.412 79.651  27.158 1   62.09  ? 130 TYR   B OH  1 
ATOM   3604  N  N   . LEU   B 1 109 ? 72.05  73.704  23.55  1   55.55  ? 131 LEU   B N   1 
ATOM   3605  C  CA  . LEU   B 1 109 ? 71.069 72.644  23.347 1   55.8   ? 131 LEU   B CA  1 
ATOM   3606  C  C   . LEU   B 1 109 ? 71.257 71.9    22.024 1   56.16  ? 131 LEU   B C   1 
ATOM   3607  O  O   . LEU   B 1 109 ? 71.247 72.522  20.96  1   56.55  ? 131 LEU   B O   1 
ATOM   3608  C  CB  . LEU   B 1 109 ? 69.653 73.264  23.426 1   55.97  ? 131 LEU   B CB  1 
ATOM   3609  C  CG  . LEU   B 1 109 ? 68.893 73.35   24.78  1   56.75  ? 131 LEU   B CG  1 
ATOM   3610  C  CD1 . LEU   B 1 109 ? 69.809 73.395  25.995 1   56.76  ? 131 LEU   B CD1 1 
ATOM   3611  C  CD2 . LEU   B 1 109 ? 67.957 74.537  24.789 1   57.41  ? 131 LEU   B CD2 1 
ATOM   3612  N  N   . GLN   B 1 116 ? 62.55  63.323  20.146 1   48.27  ? 138 GLN   B N   1 
ATOM   3613  C  CA  . GLN   B 1 116 ? 63.063 64.172  21.233 1   48.92  ? 138 GLN   B CA  1 
ATOM   3614  C  C   . GLN   B 1 116 ? 63.394 63.339  22.543 1   48.78  ? 138 GLN   B C   1 
ATOM   3615  O  O   . GLN   B 1 116 ? 64.552 62.928  22.753 1   49.04  ? 138 GLN   B O   1 
ATOM   3616  C  CB  . GLN   B 1 116 ? 62.102 65.369  21.492 1   49.86  ? 138 GLN   B CB  1 
ATOM   3617  C  CG  . GLN   B 1 116 ? 62.691 66.42   22.411 1   52.65  ? 138 GLN   B CG  1 
ATOM   3618  C  CD  . GLN   B 1 116 ? 63.712 67.223  21.675 1   57.96  ? 138 GLN   B CD  1 
ATOM   3619  O  OE1 . GLN   B 1 116 ? 64.919 67.021  21.804 1   60.37  ? 138 GLN   B OE1 1 
ATOM   3620  N  NE2 . GLN   B 1 116 ? 63.244 68.136  20.858 1   58.84  ? 138 GLN   B NE2 1 
ATOM   3621  N  N   . SER   B 1 117 ? 62.36  63.066  23.38  1   47.68  ? 139 SER   B N   1 
ATOM   3622  C  CA  . SER   B 1 117 ? 62.442 62.293  24.624 1   46.98  ? 139 SER   B CA  1 
ATOM   3623  C  C   . SER   B 1 117 ? 62.155 60.818  24.333 1   45.78  ? 139 SER   B C   1 
ATOM   3624  O  O   . SER   B 1 117 ? 61.129 60.513  23.721 1   45.77  ? 139 SER   B O   1 
ATOM   3625  C  CB  . SER   B 1 117 ? 61.391 62.804  25.607 1   47.92  ? 139 SER   B CB  1 
ATOM   3626  O  OG  . SER   B 1 117 ? 61.159 61.909  26.682 1   50.29  ? 139 SER   B OG  1 
ATOM   3627  N  N   . LEU   B 1 118 ? 63.02  59.906  24.798 1   44.43  ? 140 LEU   B N   1 
ATOM   3628  C  CA  . LEU   B 1 118 ? 62.785 58.475  24.601 1   43.7   ? 140 LEU   B CA  1 
ATOM   3629  C  C   . LEU   B 1 118 ? 61.522 58.049  25.364 1   42.97  ? 140 LEU   B C   1 
ATOM   3630  O  O   . LEU   B 1 118 ? 60.704 57.312  24.822 1   43.2   ? 140 LEU   B O   1 
ATOM   3631  C  CB  . LEU   B 1 118 ? 64     57.66   25.075 1   43.79  ? 140 LEU   B CB  1 
ATOM   3632  C  CG  . LEU   B 1 118 ? 63.811 56.145  25.138 1   45.22  ? 140 LEU   B CG  1 
ATOM   3633  C  CD1 . LEU   B 1 118 ? 63.741 55.546  23.75  1   45.48  ? 140 LEU   B CD1 1 
ATOM   3634  C  CD2 . LEU   B 1 118 ? 64.895 55.486  25.969 1   45.93  ? 140 LEU   B CD2 1 
ATOM   3635  N  N   . GLN   B 1 119 ? 61.353 58.551  26.6   1   42.09  ? 141 GLN   B N   1 
ATOM   3636  C  CA  . GLN   B 1 119 ? 60.21  58.219  27.428 1   41.69  ? 141 GLN   B CA  1 
ATOM   3637  C  C   . GLN   B 1 119 ? 58.886 58.73   26.881 1   42.83  ? 141 GLN   B C   1 
ATOM   3638  O  O   . GLN   B 1 119 ? 57.903 57.998  26.959 1   43.31  ? 141 GLN   B O   1 
ATOM   3639  C  CB  . GLN   B 1 119 ? 60.428 58.653  28.869 1   41.16  ? 141 GLN   B CB  1 
ATOM   3640  C  CG  . GLN   B 1 119 ? 61.407 57.73   29.543 1   40.81  ? 141 GLN   B CG  1 
ATOM   3641  C  CD  . GLN   B 1 119 ? 61.419 57.861  31.032 1   42.12  ? 141 GLN   B CD  1 
ATOM   3642  O  OE1 . GLN   B 1 119 ? 61.454 58.961  31.576 1   43.55  ? 141 GLN   B OE1 1 
ATOM   3643  N  NE2 . GLN   B 1 119 ? 61.424 56.726  31.722 1   41.73  ? 141 GLN   B NE2 1 
ATOM   3644  N  N   . PHE   B 1 120 ? 58.845 59.928  26.281 1   43.32  ? 142 PHE   B N   1 
ATOM   3645  C  CA  . PHE   B 1 120 ? 57.588 60.428  25.698 1   44.29  ? 142 PHE   B CA  1 
ATOM   3646  C  C   . PHE   B 1 120 ? 57.139 59.537  24.541 1   46.38  ? 142 PHE   B C   1 
ATOM   3647  O  O   . PHE   B 1 120 ? 55.937 59.278  24.388 1   47.23  ? 142 PHE   B O   1 
ATOM   3648  C  CB  . PHE   B 1 120 ? 57.713 61.881  25.223 1   43.29  ? 142 PHE   B CB  1 
ATOM   3649  C  CG  . PHE   B 1 120 ? 56.41  62.428  24.684 1   42.98  ? 142 PHE   B CG  1 
ATOM   3650  C  CD1 . PHE   B 1 120 ? 55.382 62.789  25.542 1   43.17  ? 142 PHE   B CD1 1 
ATOM   3651  C  CD2 . PHE   B 1 120 ? 56.208 62.571  23.316 1   43.22  ? 142 PHE   B CD2 1 
ATOM   3652  C  CE1 . PHE   B 1 120 ? 54.187 63.286  25.046 1   43.56  ? 142 PHE   B CE1 1 
ATOM   3653  C  CE2 . PHE   B 1 120 ? 55.024 63.097  22.824 1   43.45  ? 142 PHE   B CE2 1 
ATOM   3654  C  CZ  . PHE   B 1 120 ? 54.018 63.444  23.689 1   43.34  ? 142 PHE   B CZ  1 
ATOM   3655  N  N   . ARG   B 1 121 ? 58.107 59.074  23.725 1   46.78  ? 143 ARG   B N   1 
ATOM   3656  C  CA  . ARG   B 1 121 ? 57.841 58.191  22.599 1   47.58  ? 143 ARG   B CA  1 
ATOM   3657  C  C   . ARG   B 1 121 ? 57.37  56.838  23.1   1   46.86  ? 143 ARG   B C   1 
ATOM   3658  O  O   . ARG   B 1 121 ? 56.429 56.294  22.544 1   47.19  ? 143 ARG   B O   1 
ATOM   3659  C  CB  . ARG   B 1 121 ? 59.076 58.043  21.691 1   50.1   ? 143 ARG   B CB  1 
ATOM   3660  C  CG  . ARG   B 1 121 ? 59.023 58.918  20.439 1   55.51  ? 143 ARG   B CG  1 
ATOM   3661  C  CD  . ARG   B 1 121 ? 57.998 58.448  19.406 1   61.14  ? 143 ARG   B CD  1 
ATOM   3662  N  NE  . ARG   B 1 121 ? 58.289 57.114  18.862 1   65.87  ? 143 ARG   B NE  1 
ATOM   3663  C  CZ  . ARG   B 1 121 ? 58.714 56.879  17.619 1   68.07  ? 143 ARG   B CZ  1 
ATOM   3664  N  NH1 . ARG   B 1 121 ? 58.937 57.888  16.784 1   67.69  ? 143 ARG   B NH1 1 
ATOM   3665  N  NH2 . ARG   B 1 121 ? 58.936 55.633  17.208 1   67.05  ? 143 ARG   B NH2 1 
ATOM   3666  N  N   . LEU   B 1 122 ? 57.974 56.317  24.173 1   45.89  ? 144 LEU   B N   1 
ATOM   3667  C  CA  . LEU   B 1 122 ? 57.547 55.04   24.745 1   45.45  ? 144 LEU   B CA  1 
ATOM   3668  C  C   . LEU   B 1 122 ? 56.088 55.109  25.222 1   45.22  ? 144 LEU   B C   1 
ATOM   3669  O  O   . LEU   B 1 122 ? 55.37  54.142  25.051 1   45.4   ? 144 LEU   B O   1 
ATOM   3670  C  CB  . LEU   B 1 122 ? 58.464 54.609  25.888 1   45.3   ? 144 LEU   B CB  1 
ATOM   3671  C  CG  . LEU   B 1 122 ? 59.878 54.197  25.503 1   46.81  ? 144 LEU   B CG  1 
ATOM   3672  C  CD1 . LEU   B 1 122 ? 60.666 53.827  26.734 1   47.43  ? 144 LEU   B CD1 1 
ATOM   3673  C  CD2 . LEU   B 1 122 ? 59.874 53.023  24.539 1   47.71  ? 144 LEU   B CD2 1 
ATOM   3674  N  N   . ILE   B 1 123 ? 55.638 56.266  25.759 1   44.43  ? 145 ILE   B N   1 
ATOM   3675  C  CA  . ILE   B 1 123 ? 54.259 56.484  26.19  1   43.93  ? 145 ILE   B CA  1 
ATOM   3676  C  C   . ILE   B 1 123 ? 53.346 56.48   24.966 1   43.65  ? 145 ILE   B C   1 
ATOM   3677  O  O   . ILE   B 1 123 ? 52.356 55.756  24.946 1   43.33  ? 145 ILE   B O   1 
ATOM   3678  C  CB  . ILE   B 1 123 ? 54.131 57.807  26.998 1   44.46  ? 145 ILE   B CB  1 
ATOM   3679  C  CG1 . ILE   B 1 123 ? 54.876 57.692  28.339 1   45.38  ? 145 ILE   B CG1 1 
ATOM   3680  C  CG2 . ILE   B 1 123 ? 52.663 58.206  27.208 1   44.63  ? 145 ILE   B CG2 1 
ATOM   3681  C  CD1 . ILE   B 1 123 ? 54.994 58.955  29.118 1   46.44  ? 145 ILE   B CD1 1 
ATOM   3682  N  N   . GLU   B 1 124 ? 53.699 57.264  23.92  1   43.43  ? 146 GLU   B N   1 
ATOM   3683  C  CA  . GLU   B 1 124 ? 52.934 57.332  22.674 1   43.49  ? 146 GLU   B CA  1 
ATOM   3684  C  C   . GLU   B 1 124 ? 52.715 55.937  22.081 1   43.22  ? 146 GLU   B C   1 
ATOM   3685  O  O   . GLU   B 1 124 ? 51.583 55.569  21.783 1   42.85  ? 146 GLU   B O   1 
ATOM   3686  C  CB  . GLU   B 1 124 ? 53.652 58.226  21.651 1   45.67  ? 146 GLU   B CB  1 
ATOM   3687  C  CG  . GLU   B 1 124 ? 53.442 59.714  21.844 1   48.97  ? 146 GLU   B CG  1 
ATOM   3688  C  CD  . GLU   B 1 124 ? 54.102 60.538  20.756 1   52.94  ? 146 GLU   B CD  1 
ATOM   3689  O  OE1 . GLU   B 1 124 ? 55.292 60.286  20.453 1   54.35  ? 146 GLU   B OE1 1 
ATOM   3690  O  OE2 . GLU   B 1 124 ? 53.436 61.452  20.218 1   53.78  ? 146 GLU   B OE2 1 
ATOM   3691  N  N   . ASN   B 1 125 ? 53.798 55.14   22     1   43.04  ? 147 ASN   B N   1 
ATOM   3692  C  CA  . ASN   B 1 125 ? 53.782 53.783  21.46  1   42.92  ? 147 ASN   B CA  1 
ATOM   3693  C  C   . ASN   B 1 125 ? 53.005 52.807  22.342 1   43.79  ? 147 ASN   B C   1 
ATOM   3694  O  O   . ASN   B 1 125 ? 52.163 52.064  21.83  1   44.3   ? 147 ASN   B O   1 
ATOM   3695  C  CB  . ASN   B 1 125 ? 55.198 53.279  21.21  1   42.52  ? 147 ASN   B CB  1 
ATOM   3696  C  CG  . ASN   B 1 125 ? 55.918 54.008  20.112 1   43.71  ? 147 ASN   B CG  1 
ATOM   3697  O  OD1 . ASN   B 1 125 ? 55.311 54.697  19.286 1   45.42  ? 147 ASN   B OD1 1 
ATOM   3698  N  ND2 . ASN   B 1 125 ? 57.233 53.875  20.08  1   43.27  ? 147 ASN   B ND2 1 
ATOM   3699  N  N   . LYS   B 1 126 ? 53.255 52.817  23.665 1   43.58  ? 148 LYS   B N   1 
ATOM   3700  C  CA  . LYS   B 1 126 ? 52.549 51.926  24.577 1   43.9   ? 148 LYS   B CA  1 
ATOM   3701  C  C   . LYS   B 1 126 ? 51.055 52.234  24.669 1   44.6   ? 148 LYS   B C   1 
ATOM   3702  O  O   . LYS   B 1 126 ? 50.269 51.319  24.881 1   44.82  ? 148 LYS   B O   1 
ATOM   3703  C  CB  . LYS   B 1 126 ? 53.205 51.9    25.962 1   45.1   ? 148 LYS   B CB  1 
ATOM   3704  C  CG  . LYS   B 1 126 ? 54.581 51.239  25.979 1   47.84  ? 148 LYS   B CG  1 
ATOM   3705  C  CD  . LYS   B 1 126 ? 55.368 51.67   27.208 1   49.66  ? 148 LYS   B CD  1 
ATOM   3706  C  CE  . LYS   B 1 126 ? 56.773 51.153  27.2   1   51.49  ? 148 LYS   B CE  1 
ATOM   3707  N  NZ  . LYS   B 1 126 ? 56.785 49.686  27.39  1   54.16  ? 148 LYS   B NZ  1 
ATOM   3708  N  N   . LEU   B 1 127 ? 50.659 53.504  24.509 1   44.87  ? 149 LEU   B N   1 
ATOM   3709  C  CA  . LEU   B 1 127 ? 49.249 53.875  24.516 1   45.8   ? 149 LEU   B CA  1 
ATOM   3710  C  C   . LEU   B 1 127 ? 48.622 53.365  23.211 1   48.21  ? 149 LEU   B C   1 
ATOM   3711  O  O   . LEU   B 1 127 ? 47.583 52.703  23.246 1   48.06  ? 149 LEU   B O   1 
ATOM   3712  C  CB  . LEU   B 1 127 ? 49.059 55.399  24.672 1   45.2   ? 149 LEU   B CB  1 
ATOM   3713  C  CG  . LEU   B 1 127 ? 47.609 55.875  24.768 1   46.03  ? 149 LEU   B CG  1 
ATOM   3714  C  CD1 . LEU   B 1 127 ? 46.953 55.366  26.01  1   46.48  ? 149 LEU   B CD1 1 
ATOM   3715  C  CD2 . LEU   B 1 127 ? 47.517 57.369  24.737 1   46.53  ? 149 LEU   B CD2 1 
ATOM   3716  N  N   . GLY   B 1 128 ? 49.283 53.626  22.082 1   50.2   ? 150 GLY   B N   1 
ATOM   3717  C  CA  . GLY   B 1 128 ? 48.794 53.141  20.806 1   53.16  ? 150 GLY   B CA  1 
ATOM   3718  C  C   . GLY   B 1 128 ? 48.826 54.129  19.665 1   56.83  ? 150 GLY   B C   1 
ATOM   3719  O  O   . GLY   B 1 128 ? 48.095 53.965  18.683 1   56.98  ? 150 GLY   B O   1 
ATOM   3720  N  N   . VAL   B 1 129 ? 49.692 55.145  19.748 1   59.68  ? 151 VAL   B N   1 
ATOM   3721  C  CA  . VAL   B 1 129 ? 49.84  56.108  18.656 1   62.73  ? 151 VAL   B CA  1 
ATOM   3722  C  C   . VAL   B 1 129 ? 50.492 55.359  17.494 1   65.98  ? 151 VAL   B C   1 
ATOM   3723  O  O   . VAL   B 1 129 ? 51.568 54.779  17.656 1   65.88  ? 151 VAL   B O   1 
ATOM   3724  C  CB  . VAL   B 1 129 ? 50.642 57.363  19.068 1   63.54  ? 151 VAL   B CB  1 
ATOM   3725  C  CG1 . VAL   B 1 129 ? 50.916 58.251  17.864 1   64.13  ? 151 VAL   B CG1 1 
ATOM   3726  C  CG2 . VAL   B 1 129 ? 49.913 58.147  20.149 1   64.03  ? 151 VAL   B CG2 1 
ATOM   3727  N  N   . LEU   B 1 130 ? 49.753 55.23   16.389 1   68.82  ? 152 LEU   B N   1 
ATOM   3728  C  CA  . LEU   B 1 130 ? 50.212 54.471  15.222 1   71.9   ? 152 LEU   B CA  1 
ATOM   3729  C  C   . LEU   B 1 130 ? 51.373 55.152  14.505 1   74.14  ? 152 LEU   B C   1 
ATOM   3730  O  O   . LEU   B 1 130 ? 51.263 56.317  14.127 1   74.34  ? 152 LEU   B O   1 
ATOM   3731  C  CB  . LEU   B 1 130 ? 49.041 54.177  14.268 1   72.7   ? 152 LEU   B CB  1 
ATOM   3732  C  CG  . LEU   B 1 130 ? 47.877 53.391  14.906 1   74.92  ? 152 LEU   B CG  1 
ATOM   3733  C  CD1 . LEU   B 1 130 ? 46.638 54.266  15.081 1   76.09  ? 152 LEU   B CD1 1 
ATOM   3734  C  CD2 . LEU   B 1 130 ? 47.559 52.131  14.131 1   75.46  ? 152 LEU   B CD2 1 
ATOM   3735  N  N   . THR   B 1 131 ? 52.497 54.431  14.345 1   75.68  ? 153 THR   B N   1 
ATOM   3736  C  CA  . THR   B 1 131 ? 53.732 54.933  13.726 1   77.82  ? 153 THR   B CA  1 
ATOM   3737  C  C   . THR   B 1 131 ? 53.517 55.431  12.265 1   79.34  ? 153 THR   B C   1 
ATOM   3738  O  O   . THR   B 1 131 ? 54.199 56.359  11.825 1   79.13  ? 153 THR   B O   1 
ATOM   3739  C  CB  . THR   B 1 131 ? 54.832 53.865  13.878 1   79.63  ? 153 THR   B CB  1 
ATOM   3740  O  OG1 . THR   B 1 131 ? 55.004 53.603  15.279 1   80.58  ? 153 THR   B OG1 1 
ATOM   3741  C  CG2 . THR   B 1 131 ? 56.175 54.29   13.27  1   80.2   ? 153 THR   B CG2 1 
ATOM   3742  N  N   . GLU   B 1 132 ? 52.507 54.888  11.56  1   80.7   ? 154 GLU   B N   1 
ATOM   3743  C  CA  . GLU   B 1 132 ? 52.165 55.325  10.204 1   82.33  ? 154 GLU   B CA  1 
ATOM   3744  C  C   . GLU   B 1 132 ? 51.339 56.644  10.158 1   83.3   ? 154 GLU   B C   1 
ATOM   3745  O  O   . GLU   B 1 132 ? 50.897 57.054  9.08   1   83.57  ? 154 GLU   B O   1 
ATOM   3746  C  CB  . GLU   B 1 132 ? 51.449 54.201  9.435  1   85.21  ? 154 GLU   B CB  1 
ATOM   3747  C  CG  . GLU   B 1 132 ? 50.178 53.711  10.106 1   90.47  ? 154 GLU   B CG  1 
ATOM   3748  C  CD  . GLU   B 1 132 ? 50.351 52.453  10.935 1   97.06  ? 154 GLU   B CD  1 
ATOM   3749  O  OE1 . GLU   B 1 132 ? 49.342 51.738  11.141 1   98.67  ? 154 GLU   B OE1 1 
ATOM   3750  O  OE2 . GLU   B 1 132 ? 51.494 52.175  11.369 1   98.57  ? 154 GLU   B OE2 1 
ATOM   3751  N  N   . GLN   B 1 133 ? 51.151 57.311  11.318 1   83.5   ? 155 GLN   B N   1 
ATOM   3752  C  CA  . GLN   B 1 133 ? 50.425 58.577  11.403 1   84.01  ? 155 GLN   B CA  1 
ATOM   3753  C  C   . GLN   B 1 133 ? 51.392 59.762  11.606 1   84.07  ? 155 GLN   B C   1 
ATOM   3754  O  O   . GLN   B 1 133 ? 52.542 59.6    12.028 1   84     ? 155 GLN   B O   1 
ATOM   3755  C  CB  . GLN   B 1 133 ? 49.376 58.539  12.532 1   85.97  ? 155 GLN   B CB  1 
ATOM   3756  C  CG  . GLN   B 1 133 ? 48.468 57.305  12.526 1   89.45  ? 155 GLN   B CG  1 
ATOM   3757  C  CD  . GLN   B 1 133 ? 47.64  57.194  11.276 1   93.89  ? 155 GLN   B CD  1 
ATOM   3758  O  OE1 . GLN   B 1 133 ? 47.613 56.147  10.616 1   95.31  ? 155 GLN   B OE1 1 
ATOM   3759  N  NE2 . GLN   B 1 133 ? 46.945 58.27   10.924 1   94.52  ? 155 GLN   B NE2 1 
ATOM   3760  N  N   . VAL   B 1 144 ? 66.208 57.996  14.639 1   94.65  ? 166 VAL   B N   1 
ATOM   3761  C  CA  . VAL   B 1 144 ? 66.234 59.225  15.442 1   95.3   ? 166 VAL   B CA  1 
ATOM   3762  C  C   . VAL   B 1 144 ? 67.073 59.1    16.725 1   95.64  ? 166 VAL   B C   1 
ATOM   3763  O  O   . VAL   B 1 144 ? 67.525 60.11   17.266 1   95.53  ? 166 VAL   B O   1 
ATOM   3764  C  CB  . VAL   B 1 144 ? 64.818 59.668  15.782 1   95.53  ? 166 VAL   B CB  1 
ATOM   3765  N  N   . PHE   B 1 145 ? 67.265 57.868  17.213 1   95.8   ? 167 PHE   B N   1 
ATOM   3766  C  CA  . PHE   B 1 145 ? 68.052 57.588  18.409 1   96.44  ? 167 PHE   B CA  1 
ATOM   3767  C  C   . PHE   B 1 145 ? 69.054 56.48   18.063 1   96.99  ? 167 PHE   B C   1 
ATOM   3768  O  O   . PHE   B 1 145 ? 68.642 55.371  17.735 1   97.06  ? 167 PHE   B O   1 
ATOM   3769  C  CB  . PHE   B 1 145 ? 67.137 57.137  19.54  1   96.64  ? 167 PHE   B CB  1 
ATOM   3770  N  N   . SER   B 1 146 ? 70.365 56.782  18.112 1   97.1   ? 168 SER   B N   1 
ATOM   3771  C  CA  . SER   B 1 146 ? 71.402 55.814  17.757 1   97.4   ? 168 SER   B CA  1 
ATOM   3772  C  C   . SER   B 1 146 ? 71.863 54.896  18.901 1   97.81  ? 168 SER   B C   1 
ATOM   3773  O  O   . SER   B 1 146 ? 72.665 54.007  18.642 1   97.86  ? 168 SER   B O   1 
ATOM   3774  C  CB  . SER   B 1 146 ? 72.595 56.523  17.14  1   97.43  ? 168 SER   B CB  1 
ATOM   3775  N  N   . ASP   B 1 147 ? 71.371 55.084  20.148 1   97.93  ? 169 ASP   B N   1 
ATOM   3776  C  CA  . ASP   B 1 147 ? 71.762 54.223  21.279 1   98.49  ? 169 ASP   B CA  1 
ATOM   3777  C  C   . ASP   B 1 147 ? 71.148 52.826  21.153 1   98.78  ? 169 ASP   B C   1 
ATOM   3778  O  O   . ASP   B 1 147 ? 70.028 52.694  20.666 1   99.13  ? 169 ASP   B O   1 
ATOM   3779  C  CB  . ASP   B 1 147 ? 71.352 54.856  22.601 1   98.66  ? 169 ASP   B CB  1 
ATOM   3780  N  N   . GLU   B 1 148 ? 71.875 51.783  21.574 1   98.52  ? 170 GLU   B N   1 
ATOM   3781  C  CA  . GLU   B 1 148 ? 71.386 50.407  21.446 1   98.71  ? 170 GLU   B CA  1 
ATOM   3782  C  C   . GLU   B 1 148 ? 70.306 50.058  22.469 1   98.31  ? 170 GLU   B C   1 
ATOM   3783  O  O   . GLU   B 1 148 ? 69.437 49.225  22.195 1   98.56  ? 170 GLU   B O   1 
ATOM   3784  C  CB  . GLU   B 1 148 ? 72.554 49.414  21.518 1   101.08 ? 170 GLU   B CB  1 
ATOM   3785  C  CG  . GLU   B 1 148 ? 72.249 48.069  20.887 1   106    ? 170 GLU   B CG  1 
ATOM   3786  C  CD  . GLU   B 1 148 ? 72.649 46.889  21.749 1   112.52 ? 170 GLU   B CD  1 
ATOM   3787  O  OE1 . GLU   B 1 148 ? 73.869 46.67   21.93  1   113.94 ? 170 GLU   B OE1 1 
ATOM   3788  O  OE2 . GLU   B 1 148 ? 71.741 46.184  22.248 1   114.28 ? 170 GLU   B OE2 1 
ATOM   3789  N  N   . GLU   B 1 149 ? 70.382 50.665  23.654 1   97.51  ? 171 GLU   B N   1 
ATOM   3790  C  CA  . GLU   B 1 149 ? 69.389 50.443  24.693 1   97.13  ? 171 GLU   B CA  1 
ATOM   3791  C  C   . GLU   B 1 149 ? 68.081 51.14   24.27  1   96.45  ? 171 GLU   B C   1 
ATOM   3792  O  O   . GLU   B 1 149 ? 67.003 50.559  24.406 1   96.68  ? 171 GLU   B O   1 
ATOM   3793  C  CB  . GLU   B 1 149 ? 69.903 51.008  26.027 1   99.2   ? 171 GLU   B CB  1 
ATOM   3794  C  CG  . GLU   B 1 149 ? 69.115 50.543  27.236 1   103.82 ? 171 GLU   B CG  1 
ATOM   3795  C  CD  . GLU   B 1 149 ? 69.812 49.482  28.063 1   109.46 ? 171 GLU   B CD  1 
ATOM   3796  O  OE1 . GLU   B 1 149 ? 69.994 49.704  29.282 1   110.35 ? 171 GLU   B OE1 1 
ATOM   3797  O  OE2 . GLU   B 1 149 ? 70.183 48.431  27.491 1   111.36 ? 171 GLU   B OE2 1 
ATOM   3798  N  N   . ALA   B 1 150 ? 68.193 52.371  23.722 1   95.31  ? 172 ALA   B N   1 
ATOM   3799  C  CA  . ALA   B 1 150 ? 67.067 53.171  23.257 1   94.73  ? 172 ALA   B CA  1 
ATOM   3800  C  C   . ALA   B 1 150 ? 66.423 52.572  22.007 1   93.94  ? 172 ALA   B C   1 
ATOM   3801  O  O   . ALA   B 1 150 ? 65.203 52.657  21.852 1   93.99  ? 172 ALA   B O   1 
ATOM   3802  C  CB  . ALA   B 1 150 ? 67.523 54.593  22.977 1   94.81  ? 172 ALA   B CB  1 
ATOM   3803  N  N   . ARG   B 1 151 ? 67.234 51.964  21.121 1   92.96  ? 173 ARG   B N   1 
ATOM   3804  C  CA  . ARG   B 1 151 ? 66.722 51.343  19.901 1   92.41  ? 173 ARG   B CA  1 
ATOM   3805  C  C   . ARG   B 1 151 ? 65.899 50.116  20.234 1   91.2   ? 173 ARG   B C   1 
ATOM   3806  O  O   . ARG   B 1 151 ? 64.825 49.922  19.662 1   91.18  ? 173 ARG   B O   1 
ATOM   3807  C  CB  . ARG   B 1 151 ? 67.861 50.979  18.947 1   94.3   ? 173 ARG   B CB  1 
ATOM   3808  C  CG  . ARG   B 1 151 ? 68.163 52.092  17.968 1   98.58  ? 173 ARG   B CG  1 
ATOM   3809  C  CD  . ARG   B 1 151 ? 68.188 51.613  16.532 1   102.98 ? 173 ARG   B CD  1 
ATOM   3810  N  NE  . ARG   B 1 151 ? 67.528 52.567  15.636 1   107.08 ? 173 ARG   B NE  1 
ATOM   3811  C  CZ  . ARG   B 1 151 ? 68.149 53.564  15.008 1   110.07 ? 173 ARG   B CZ  1 
ATOM   3812  N  NH1 . ARG   B 1 151 ? 69.452 53.763  15.186 1   110.13 ? 173 ARG   B NH1 1 
ATOM   3813  N  NH2 . ARG   B 1 151 ? 67.467 54.386  14.217 1   109.88 ? 173 ARG   B NH2 1 
ATOM   3814  N  N   . ASN   B 1 152 ? 66.392 49.304  21.182 1   90.03  ? 174 ASN   B N   1 
ATOM   3815  C  CA  . ASN   B 1 152 ? 65.715 48.101  21.645 1   89.49  ? 174 ASN   B CA  1 
ATOM   3816  C  C   . ASN   B 1 152 ? 64.387 48.481  22.309 1   88.04  ? 174 ASN   B C   1 
ATOM   3817  O  O   . ASN   B 1 152 ? 63.379 47.819  22.069 1   88.28  ? 174 ASN   B O   1 
ATOM   3818  C  CB  . ASN   B 1 152 ? 66.61  47.341  22.637 1   91.26  ? 174 ASN   B CB  1 
ATOM   3819  C  CG  . ASN   B 1 152 ? 66.113 45.952  23.008 1   95.06  ? 174 ASN   B CG  1 
ATOM   3820  O  OD1 . ASN   B 1 152 ? 65.991 45.055  22.162 1   96.47  ? 174 ASN   B OD1 1 
ATOM   3821  N  ND2 . ASN   B 1 152 ? 65.834 45.732  24.287 1   95.61  ? 174 ASN   B ND2 1 
ATOM   3822  N  N   . SER   B 1 153 ? 64.386 49.565  23.116 1   86.24  ? 175 SER   B N   1 
ATOM   3823  C  CA  . SER   B 1 153 ? 63.198 50.06   23.811 1   84.85  ? 175 SER   B CA  1 
ATOM   3824  C  C   . SER   B 1 153 ? 62.093 50.447  22.834 1   83.14  ? 175 SER   B C   1 
ATOM   3825  O  O   . SER   B 1 153 ? 60.955 50.012  22.999 1   82.97  ? 175 SER   B O   1 
ATOM   3826  C  CB  . SER   B 1 153 ? 63.552 51.256  24.694 1   86.04  ? 175 SER   B CB  1 
ATOM   3827  O  OG  . SER   B 1 153 ? 64.454 50.91   25.731 1   88.12  ? 175 SER   B OG  1 
ATOM   3828  N  N   . ILE   B 1 154 ? 62.432 51.242  21.804 1   81.77  ? 176 ILE   B N   1 
ATOM   3829  C  CA  . ILE   B 1 154 ? 61.454 51.694  20.823 1   80.92  ? 176 ILE   B CA  1 
ATOM   3830  C  C   . ILE   B 1 154 ? 61     50.54   19.934 1   80.33  ? 176 ILE   B C   1 
ATOM   3831  O  O   . ILE   B 1 154 ? 59.811 50.452  19.631 1   80.29  ? 176 ILE   B O   1 
ATOM   3832  C  CB  . ILE   B 1 154 ? 61.957 52.943  20.061 1   81.07  ? 176 ILE   B CB  1 
ATOM   3833  C  CG1 . ILE   B 1 154 ? 61.72  54.181  20.955 1   81.82  ? 176 ILE   B CG1 1 
ATOM   3834  C  CG2 . ILE   B 1 154 ? 61.273 53.111  18.692 1   81.46  ? 176 ILE   B CG2 1 
ATOM   3835  C  CD1 . ILE   B 1 154 ? 62.085 55.523  20.383 1   83.05  ? 176 ILE   B CD1 1 
ATOM   3836  N  N   . ARG   B 1 155 ? 61.902 49.599  19.606 1   79.86  ? 177 ARG   B N   1 
ATOM   3837  C  CA  . ARG   B 1 155 ? 61.541 48.412  18.829 1   79.88  ? 177 ARG   B CA  1 
ATOM   3838  C  C   . ARG   B 1 155 ? 60.468 47.599  19.577 1   78.55  ? 177 ARG   B C   1 
ATOM   3839  O  O   . ARG   B 1 155 ? 59.393 47.36   19.034 1   78.58  ? 177 ARG   B O   1 
ATOM   3840  C  CB  . ARG   B 1 155 ? 62.789 47.547  18.56  1   82.58  ? 177 ARG   B CB  1 
ATOM   3841  C  CG  . ARG   B 1 155 ? 63.153 47.419  17.086 1   87.91  ? 177 ARG   B CG  1 
ATOM   3842  C  CD  . ARG   B 1 155 ? 62.285 46.387  16.378 1   92.79  ? 177 ARG   B CD  1 
ATOM   3843  N  NE  . ARG   B 1 155 ? 62.439 46.44   14.922 1   96.87  ? 177 ARG   B NE  1 
ATOM   3844  C  CZ  . ARG   B 1 155 ? 63.304 45.704  14.227 1   99.08  ? 177 ARG   B CZ  1 
ATOM   3845  N  NH1 . ARG   B 1 155 ? 64.111 44.849  14.847 1   98.62  ? 177 ARG   B NH1 1 
ATOM   3846  N  NH2 . ARG   B 1 155 ? 63.371 45.819  12.906 1   98.77  ? 177 ARG   B NH2 1 
ATOM   3847  N  N   . ASN   B 1 156 ? 60.724 47.282  20.855 1   77.4   ? 178 ASN   B N   1 
ATOM   3848  C  CA  . ASN   B 1 156 ? 59.8   46.529  21.693 1   77.09  ? 178 ASN   B CA  1 
ATOM   3849  C  C   . ASN   B 1 156 ? 58.464 47.247  21.929 1   75.53  ? 178 ASN   B C   1 
ATOM   3850  O  O   . ASN   B 1 156 ? 57.436 46.587  21.981 1   75.51  ? 178 ASN   B O   1 
ATOM   3851  C  CB  . ASN   B 1 156 ? 60.454 46.151  23.024 1   79.25  ? 178 ASN   B CB  1 
ATOM   3852  C  CG  . ASN   B 1 156 ? 61.635 45.217  22.881 1   83.34  ? 178 ASN   B CG  1 
ATOM   3853  O  OD1 . ASN   B 1 156 ? 61.894 44.667  21.804 1   84.91  ? 178 ASN   B OD1 1 
ATOM   3854  N  ND2 . ASN   B 1 156 ? 62.387 45.03   23.963 1   83.82  ? 178 ASN   B ND2 1 
ATOM   3855  N  N   . SER   B 1 157 ? 58.466 48.581  22.05  1   74.09  ? 179 SER   B N   1 
ATOM   3856  C  CA  . SER   B 1 157 ? 57.223 49.333  22.247 1   73.3   ? 179 SER   B CA  1 
ATOM   3857  C  C   . SER   B 1 157 ? 56.294 49.281  21.024 1   72.95  ? 179 SER   B C   1 
ATOM   3858  O  O   . SER   B 1 157 ? 55.082 49.452  21.164 1   73.4   ? 179 SER   B O   1 
ATOM   3859  C  CB  . SER   B 1 157 ? 57.518 50.777  22.631 1   74.06  ? 179 SER   B CB  1 
ATOM   3860  O  OG  . SER   B 1 157 ? 57.996 51.524  21.527 1   75.57  ? 179 SER   B OG  1 
ATOM   3861  N  N   . GLU   B 1 158 ? 56.856 49.023  19.83  1   72.06  ? 180 GLU   B N   1 
ATOM   3862  C  CA  . GLU   B 1 158 ? 56.095 48.906  18.594 1   71.63  ? 180 GLU   B CA  1 
ATOM   3863  C  C   . GLU   B 1 158 ? 55.661 47.454  18.352 1   71.46  ? 180 GLU   B C   1 
ATOM   3864  O  O   . GLU   B 1 158 ? 54.548 47.217  17.874 1   71.47  ? 180 GLU   B O   1 
ATOM   3865  C  CB  . GLU   B 1 158 ? 56.923 49.428  17.421 1   73.15  ? 180 GLU   B CB  1 
ATOM   3866  C  CG  . GLU   B 1 158 ? 57.177 50.92   17.513 1   77.34  ? 180 GLU   B CG  1 
ATOM   3867  C  CD  . GLU   B 1 158 ? 58.159 51.481  16.504 1   82.22  ? 180 GLU   B CD  1 
ATOM   3868  O  OE1 . GLU   B 1 158 ? 58.857 50.68   15.838 1   82.66  ? 180 GLU   B OE1 1 
ATOM   3869  O  OE2 . GLU   B 1 158 ? 58.238 52.726  16.389 1   84.07  ? 180 GLU   B OE2 1 
ATOM   3870  N  N   . LYS   B 1 159 ? 56.529 46.483  18.708 1   71.03  ? 181 LYS   B N   1 
ATOM   3871  C  CA  . LYS   B 1 159 ? 56.248 45.051  18.536 1   71.12  ? 181 LYS   B CA  1 
ATOM   3872  C  C   . LYS   B 1 159 ? 55.244 44.503  19.556 1   70.38  ? 181 LYS   B C   1 
ATOM   3873  O  O   . LYS   B 1 159 ? 54.279 43.841  19.169 1   70.45  ? 181 LYS   B O   1 
ATOM   3874  C  CB  . LYS   B 1 159 ? 57.548 44.22   18.558 1   73.43  ? 181 LYS   B CB  1 
ATOM   3875  C  CG  . LYS   B 1 159 ? 58.548 44.612  17.478 1   78.54  ? 181 LYS   B CG  1 
ATOM   3876  C  CD  . LYS   B 1 159 ? 58.015 44.366  16.075 1   83.79  ? 181 LYS   B CD  1 
ATOM   3877  C  CE  . LYS   B 1 159 ? 58.991 44.775  15.003 1   88.1   ? 181 LYS   B CE  1 
ATOM   3878  N  NZ  . LYS   B 1 159 ? 58.608 44.207  13.677 1   90.67  ? 181 LYS   B NZ  1 
ATOM   3879  N  N   . ASP   B 1 160 ? 55.475 44.77   20.855 1   69.39  ? 182 ASP   B N   1 
ATOM   3880  C  CA  . ASP   B 1 160 ? 54.594 44.309  21.925 1   68.57  ? 182 ASP   B CA  1 
ATOM   3881  C  C   . ASP   B 1 160 ? 53.22  44.992  21.853 1   67.43  ? 182 ASP   B C   1 
ATOM   3882  O  O   . ASP   B 1 160 ? 53.112 46.116  21.361 1   67.58  ? 182 ASP   B O   1 
ATOM   3883  C  CB  . ASP   B 1 160 ? 55.277 44.476  23.292 1   70.19  ? 182 ASP   B CB  1 
ATOM   3884  C  CG  . ASP   B 1 160 ? 56.648 43.805  23.382 1   75     ? 182 ASP   B CG  1 
ATOM   3885  O  OD1 . ASP   B 1 160 ? 56.958 42.957  22.512 1   76.13  ? 182 ASP   B OD1 1 
ATOM   3886  O  OD2 . ASP   B 1 160 ? 57.417 44.141  24.311 1   76.86  ? 182 ASP   B OD2 1 
ATOM   3887  N  N   . PRO   B 1 161 ? 52.142 44.285  22.233 1   66.3   ? 183 PRO   B N   1 
ATOM   3888  C  CA  . PRO   B 1 161 ? 50.795 44.875  22.1   1   65.53  ? 183 PRO   B CA  1 
ATOM   3889  C  C   . PRO   B 1 161 ? 50.556 46.145  22.914 1   64.23  ? 183 PRO   B C   1 
ATOM   3890  O  O   . PRO   B 1 161 ? 50.783 46.179  24.127 1   64.7   ? 183 PRO   B O   1 
ATOM   3891  C  CB  . PRO   B 1 161 ? 49.855 43.737  22.515 1   66.46  ? 183 PRO   B CB  1 
ATOM   3892  C  CG  . PRO   B 1 161 ? 50.699 42.823  23.328 1   67.14  ? 183 PRO   B CG  1 
ATOM   3893  C  CD  . PRO   B 1 161 ? 52.087 42.916  22.777 1   65.63  ? 183 PRO   B CD  1 
ATOM   3894  N  N   . SER   B 1 162 ? 50.087 47.192  22.231 1   62.14  ? 184 SER   B N   1 
ATOM   3895  C  CA  . SER   B 1 162 ? 49.789 48.475  22.849 1   60.6   ? 184 SER   B CA  1 
ATOM   3896  C  C   . SER   B 1 162 ? 48.483 48.409  23.667 1   58.93  ? 184 SER   B C   1 
ATOM   3897  O  O   . SER   B 1 162 ? 47.775 47.398  23.63  1   59.23  ? 184 SER   B O   1 
ATOM   3898  C  CB  . SER   B 1 162 ? 49.695 49.559  21.772 1   61.69  ? 184 SER   B CB  1 
ATOM   3899  O  OG  . SER   B 1 162 ? 48.52  49.418  20.991 1   63.41  ? 184 SER   B OG  1 
ATOM   3900  N  N   . LEU   B 1 163 ? 48.162 49.48   24.412 1   57.12  ? 185 LEU   B N   1 
ATOM   3901  C  CA  . LEU   B 1 163 ? 46.929 49.531  25.175 1   56.12  ? 185 LEU   B CA  1 
ATOM   3902  C  C   . LEU   B 1 163 ? 45.721 49.496  24.234 1   55.41  ? 185 LEU   B C   1 
ATOM   3903  O  O   . LEU   B 1 163 ? 44.732 48.861  24.571 1   55.7   ? 185 LEU   B O   1 
ATOM   3904  C  CB  . LEU   B 1 163 ? 46.892 50.754  26.096 1   55.97  ? 185 LEU   B CB  1 
ATOM   3905  C  CG  . LEU   B 1 163 ? 47.747 50.644  27.354 1   57.2   ? 185 LEU   B CG  1 
ATOM   3906  C  CD1 . LEU   B 1 163 ? 47.753 51.948  28.108 1   57.89  ? 185 LEU   B CD1 1 
ATOM   3907  C  CD2 . LEU   B 1 163 ? 47.242 49.542  28.262 1   57.71  ? 185 LEU   B CD2 1 
ATOM   3908  N  N   . LEU   B 1 164 ? 45.823 50.114  23.037 1   54.23  ? 186 LEU   B N   1 
ATOM   3909  C  CA  . LEU   B 1 164 ? 44.765 50.109  22.022 1   53.6   ? 186 LEU   B CA  1 
ATOM   3910  C  C   . LEU   B 1 164 ? 44.441 48.668  21.562 1   52.93  ? 186 LEU   B C   1 
ATOM   3911  O  O   . LEU   B 1 164 ? 43.263 48.311  21.451 1   52.49  ? 186 LEU   B O   1 
ATOM   3912  C  CB  . LEU   B 1 164 ? 45.197 50.967  20.828 1   53.66  ? 186 LEU   B CB  1 
ATOM   3913  C  CG  . LEU   B 1 164 ? 44.238 51.021  19.643 1   55.44  ? 186 LEU   B CG  1 
ATOM   3914  C  CD1 . LEU   B 1 164 ? 42.894 51.6    20.043 1   56.61  ? 186 LEU   B CD1 1 
ATOM   3915  C  CD2 . LEU   B 1 164 ? 44.817 51.836  18.52  1   55.77  ? 186 LEU   B CD2 1 
ATOM   3916  N  N   . GLU   B 1 165 ? 45.484 47.837  21.326 1   52.41  ? 187 GLU   B N   1 
ATOM   3917  C  CA  . GLU   B 1 165 ? 45.286 46.442  20.915 1   52.26  ? 187 GLU   B CA  1 
ATOM   3918  C  C   . GLU   B 1 165 ? 44.675 45.61   22.048 1   50.91  ? 187 GLU   B C   1 
ATOM   3919  O  O   . GLU   B 1 165 ? 43.711 44.892  21.825 1   50.81  ? 187 GLU   B O   1 
ATOM   3920  C  CB  . GLU   B 1 165 ? 46.598 45.782  20.461 1   55.68  ? 187 GLU   B CB  1 
ATOM   3921  C  CG  . GLU   B 1 165 ? 47.291 46.405  19.262 1   63.01  ? 187 GLU   B CG  1 
ATOM   3922  C  CD  . GLU   B 1 165 ? 48.661 45.79   19.032 1   72.93  ? 187 GLU   B CD  1 
ATOM   3923  O  OE1 . GLU   B 1 165 ? 48.797 44.556  19.214 1   75.43  ? 187 GLU   B OE1 1 
ATOM   3924  O  OE2 . GLU   B 1 165 ? 49.607 46.544  18.705 1   76.05  ? 187 GLU   B OE2 1 
ATOM   3925  N  N   . LEU   B 1 166 ? 45.236 45.704  23.253 1   49.87  ? 188 LEU   B N   1 
ATOM   3926  C  CA  . LEU   B 1 166 ? 44.778 44.952  24.419 1   49.24  ? 188 LEU   B CA  1 
ATOM   3927  C  C   . LEU   B 1 166 ? 43.36  45.328  24.879 1   48.72  ? 188 LEU   B C   1 
ATOM   3928  O  O   . LEU   B 1 166 ? 42.631 44.473  25.389 1   48.73  ? 188 LEU   B O   1 
ATOM   3929  C  CB  . LEU   B 1 166 ? 45.778 45.118  25.561 1   49.16  ? 188 LEU   B CB  1 
ATOM   3930  C  CG  . LEU   B 1 166 ? 47.169 44.561  25.29  1   50.08  ? 188 LEU   B CG  1 
ATOM   3931  C  CD1 . LEU   B 1 166 ? 48.133 45.002  26.354 1   50.5   ? 188 LEU   B CD1 1 
ATOM   3932  C  CD2 . LEU   B 1 166 ? 47.145 43.069  25.221 1   50.53  ? 188 LEU   B CD2 1 
ATOM   3933  N  N   . VAL   B 1 167 ? 42.976 46.6    24.714 1   48.14  ? 189 VAL   B N   1 
ATOM   3934  C  CA  . VAL   B 1 167 ? 41.627 47.069  25.057 1   48.27  ? 189 VAL   B CA  1 
ATOM   3935  C  C   . VAL   B 1 167 ? 40.634 46.5    24.053 1   48.45  ? 189 VAL   B C   1 
ATOM   3936  O  O   . VAL   B 1 167 ? 39.58  46.028  24.45  1   48.51  ? 189 VAL   B O   1 
ATOM   3937  C  CB  . VAL   B 1 167 ? 41.547 48.621  25.21  1   48.27  ? 189 VAL   B CB  1 
ATOM   3938  C  CG1 . VAL   B 1 167 ? 40.135 49.159  24.987 1   48.37  ? 189 VAL   B CG1 1 
ATOM   3939  C  CG2 . VAL   B 1 167 ? 42.07  49.044  26.576 1   48.4   ? 189 VAL   B CG2 1 
ATOM   3940  N  N   . GLN   B 1 168 ? 41.003 46.483  22.763 1   48.58  ? 190 GLN   B N   1 
ATOM   3941  C  CA  . GLN   B 1 168 ? 40.171 45.917  21.706 1   48.76  ? 190 GLN   B CA  1 
ATOM   3942  C  C   . GLN   B 1 168 ? 39.863 44.445  21.972 1   48.53  ? 190 GLN   B C   1 
ATOM   3943  O  O   . GLN   B 1 168 ? 38.704 44.051  21.845 1   48.88  ? 190 GLN   B O   1 
ATOM   3944  C  CB  . GLN   B 1 168 ? 40.829 46.088  20.336 1   50.09  ? 190 GLN   B CB  1 
ATOM   3945  C  CG  . GLN   B 1 168 ? 40.454 47.387  19.657 1   53.72  ? 190 GLN   B CG  1 
ATOM   3946  C  CD  . GLN   B 1 168 ? 41.136 47.522  18.321 1   58.44  ? 190 GLN   B CD  1 
ATOM   3947  O  OE1 . GLN   B 1 168 ? 41.892 48.462  18.082 1   60.27  ? 190 GLN   B OE1 1 
ATOM   3948  N  NE2 . GLN   B 1 168 ? 40.888 46.588  17.418 1   59.37  ? 190 GLN   B NE2 1 
ATOM   3949  N  N   . ARG   B 1 169 ? 40.883 43.654  22.377 1   47.56  ? 191 ARG   B N   1 
ATOM   3950  C  CA  A ARG   B 1 169 ? 40.726 42.234  22.689 0.5 47.64  ? 191 ARG   B CA  1 
ATOM   3951  C  CA  B ARG   B 1 169 ? 40.722 42.236  22.682 0.5 47.69  ? 191 ARG   B CA  1 
ATOM   3952  C  C   . ARG   B 1 169 ? 39.767 42.036  23.85  1   48.07  ? 191 ARG   B C   1 
ATOM   3953  O  O   . ARG   B 1 169 ? 38.951 41.111  23.826 1   49     ? 191 ARG   B O   1 
ATOM   3954  C  CB  A ARG   B 1 169 ? 42.085 41.603  23.032 0.5 48.4   ? 191 ARG   B CB  1 
ATOM   3955  C  CB  B ARG   B 1 169 ? 42.086 41.592  22.988 0.5 48.57  ? 191 ARG   B CB  1 
ATOM   3956  C  CG  A ARG   B 1 169 ? 43.094 41.705  21.902 0.5 50.21  ? 191 ARG   B CG  1 
ATOM   3957  C  CG  B ARG   B 1 169 ? 42.689 40.81   21.819 0.5 50.62  ? 191 ARG   B CG  1 
ATOM   3958  C  CD  A ARG   B 1 169 ? 44.472 41.245  22.329 0.5 52.19  ? 191 ARG   B CD  1 
ATOM   3959  C  CD  B ARG   B 1 169 ? 43.463 41.674  20.838 0.5 51.99  ? 191 ARG   B CD  1 
ATOM   3960  N  NE  A ARG   B 1 169 ? 45.488 41.654  21.357 0.5 53.65  ? 191 ARG   B NE  1 
ATOM   3961  N  NE  B ARG   B 1 169 ? 42.606 42.265  19.808 0.5 52.65  ? 191 ARG   B NE  1 
ATOM   3962  C  CZ  A ARG   B 1 169 ? 46.781 41.371  21.459 0.5 54.83  ? 191 ARG   B CZ  1 
ATOM   3963  C  CZ  B ARG   B 1 169 ? 43.039 43.066  18.841 0.5 52.84  ? 191 ARG   B CZ  1 
ATOM   3964  N  NH1 A ARG   B 1 169 ? 47.235 40.667  22.49  0.5 53.9   ? 191 ARG   B NH1 1 
ATOM   3965  N  NH1 B ARG   B 1 169 ? 42.188 43.568  17.961 0.5 51.92  ? 191 ARG   B NH1 1 
ATOM   3966  N  NH2 A ARG   B 1 169 ? 47.631 41.79   20.532 0.5 54.8   ? 191 ARG   B NH2 1 
ATOM   3967  N  NH2 B ARG   B 1 169 ? 44.326 43.375  18.751 0.5 52.34  ? 191 ARG   B NH2 1 
ATOM   3968  N  N   . TRP   B 1 170 ? 39.864 42.907  24.867 1   47.32  ? 192 TRP   B N   1 
ATOM   3969  C  CA  . TRP   B 1 170 ? 39.021 42.884  26.056 1   47.04  ? 192 TRP   B CA  1 
ATOM   3970  C  C   . TRP   B 1 170 ? 37.585 43.199  25.662 1   47.8   ? 192 TRP   B C   1 
ATOM   3971  O  O   . TRP   B 1 170 ? 36.675 42.497  26.089 1   47.76  ? 192 TRP   B O   1 
ATOM   3972  C  CB  . TRP   B 1 170 ? 39.566 43.893  27.101 1   46.33  ? 192 TRP   B CB  1 
ATOM   3973  C  CG  . TRP   B 1 170 ? 38.645 44.222  28.249 1   45.27  ? 192 TRP   B CG  1 
ATOM   3974  C  CD1 . TRP   B 1 170 ? 38.338 43.423  29.309 1   45.63  ? 192 TRP   B CD1 1 
ATOM   3975  C  CD2 . TRP   B 1 170 ? 37.975 45.474  28.483 1   44.44  ? 192 TRP   B CD2 1 
ATOM   3976  N  NE1 . TRP   B 1 170 ? 37.452 44.067  30.147 1   45.7   ? 192 TRP   B NE1 1 
ATOM   3977  C  CE2 . TRP   B 1 170 ? 37.231 45.336  29.675 1   45.2   ? 192 TRP   B CE2 1 
ATOM   3978  C  CE3 . TRP   B 1 170 ? 37.898 46.681  27.78  1   44.18  ? 192 TRP   B CE3 1 
ATOM   3979  C  CZ2 . TRP   B 1 170 ? 36.431 46.363  30.184 1   45.3   ? 192 TRP   B CZ2 1 
ATOM   3980  C  CZ3 . TRP   B 1 170 ? 37.106 47.694  28.288 1   44.77  ? 192 TRP   B CZ3 1 
ATOM   3981  C  CH2 . TRP   B 1 170 ? 36.381 47.531  29.474 1   44.86  ? 192 TRP   B CH2 1 
ATOM   3982  N  N   . LEU   B 1 171 ? 37.393 44.224  24.814 1   48.76  ? 193 LEU   B N   1 
ATOM   3983  C  CA  . LEU   B 1 171 ? 36.095 44.678  24.316 1   50.51  ? 193 LEU   B CA  1 
ATOM   3984  C  C   . LEU   B 1 171 ? 35.411 43.612  23.477 1   52.54  ? 193 LEU   B C   1 
ATOM   3985  O  O   . LEU   B 1 171 ? 34.191 43.458  23.558 1   52.59  ? 193 LEU   B O   1 
ATOM   3986  C  CB  . LEU   B 1 171 ? 36.255 45.953  23.486 1   50.55  ? 193 LEU   B CB  1 
ATOM   3987  C  CG  . LEU   B 1 171 ? 36.411 47.228  24.286 1   51.68  ? 193 LEU   B CG  1 
ATOM   3988  C  CD1 . LEU   B 1 171 ? 36.846 48.357  23.403 1   51.66  ? 193 LEU   B CD1 1 
ATOM   3989  C  CD2 . LEU   B 1 171 ? 35.124 47.57   25.015 1   52.47  ? 193 LEU   B CD2 1 
ATOM   3990  N  N   . GLU   B 1 172 ? 36.197 42.883  22.67  1   53.78  ? 194 GLU   B N   1 
ATOM   3991  C  CA  . GLU   B 1 172 ? 35.712 41.798  21.82  1   55.61  ? 194 GLU   B CA  1 
ATOM   3992  C  C   . GLU   B 1 172 ? 35.131 40.647  22.654 1   57.88  ? 194 GLU   B C   1 
ATOM   3993  O  O   . GLU   B 1 172 ? 34.175 40.003  22.231 1   58.13  ? 194 GLU   B O   1 
ATOM   3994  C  CB  . GLU   B 1 172 ? 36.852 41.271  20.934 1   57.02  ? 194 GLU   B CB  1 
ATOM   3995  C  CG  . GLU   B 1 172 ? 37.19  42.166  19.752 1   59.58  ? 194 GLU   B CG  1 
ATOM   3996  C  CD  . GLU   B 1 172 ? 38.557 41.925  19.135 1   64.46  ? 194 GLU   B CD  1 
ATOM   3997  O  OE1 . GLU   B 1 172 ? 39.28  41.01   19.598 1   66.34  ? 194 GLU   B OE1 1 
ATOM   3998  O  OE2 . GLU   B 1 172 ? 38.914 42.666  18.192 1   64.33  ? 194 GLU   B OE2 1 
ATOM   3999  N  N   . ARG   B 1 173 ? 35.693 40.4    23.843 1   59.56  ? 195 ARG   B N   1 
ATOM   4000  C  CA  . ARG   B 1 173 ? 35.226 39.336  24.728 1   61.5   ? 195 ARG   B CA  1 
ATOM   4001  C  C   . ARG   B 1 173 ? 34.23  39.812  25.777 1   61.96  ? 195 ARG   B C   1 
ATOM   4002  O  O   . ARG   B 1 173 ? 34.096 39.17   26.817 1   61.86  ? 195 ARG   B O   1 
ATOM   4003  C  CB  . ARG   B 1 173 ? 36.417 38.658  25.42  1   64.62  ? 195 ARG   B CB  1 
ATOM   4004  C  CG  . ARG   B 1 173 ? 37.45  38.125  24.443 1   70.67  ? 195 ARG   B CG  1 
ATOM   4005  C  CD  . ARG   B 1 173 ? 38.416 37.18   25.129 1   77.27  ? 195 ARG   B CD  1 
ATOM   4006  N  NE  . ARG   B 1 173 ? 39.244 37.875  26.115 1   83.54  ? 195 ARG   B NE  1 
ATOM   4007  C  CZ  . ARG   B 1 173 ? 40.519 38.208  25.927 1   87.77  ? 195 ARG   B CZ  1 
ATOM   4008  N  NH1 . ARG   B 1 173 ? 41.139 37.883  24.795 1   88.14  ? 195 ARG   B NH1 1 
ATOM   4009  N  NH2 . ARG   B 1 173 ? 41.188 38.854  26.876 1   87.88  ? 195 ARG   B NH2 1 
ATOM   4010  N  N   . THR   B 1 174 ? 33.54  40.924  25.521 1   62.51  ? 196 THR   B N   1 
ATOM   4011  C  CA  . THR   B 1 174 ? 32.565 41.469  26.457 1   63.59  ? 196 THR   B CA  1 
ATOM   4012  C  C   . THR   B 1 174 ? 31.369 40.534  26.563 1   64.36  ? 196 THR   B C   1 
ATOM   4013  O  O   . THR   B 1 174 ? 30.761 40.191  25.544 1   64.79  ? 196 THR   B O   1 
ATOM   4014  C  CB  . THR   B 1 174 ? 32.153 42.9    26.041 1   65.14  ? 196 THR   B CB  1 
ATOM   4015  O  OG1 . THR   B 1 174 ? 33.232 43.798  26.318 1   66.24  ? 196 THR   B OG1 1 
ATOM   4016  C  CG2 . THR   B 1 174 ? 30.898 43.389  26.762 1   65.59  ? 196 THR   B CG2 1 
ATOM   4017  N  N   . PRO   B 1 175 ? 31.039 40.081  27.79  1   64.25  ? 197 PRO   B N   1 
ATOM   4018  C  CA  . PRO   B 1 175 ? 29.867 39.203  27.95  1   64.06  ? 197 PRO   B CA  1 
ATOM   4019  C  C   . PRO   B 1 175 ? 28.565 39.948  27.648 1   63.49  ? 197 PRO   B C   1 
ATOM   4020  O  O   . PRO   B 1 175 ? 28.308 41.043  28.152 1   63.47  ? 197 PRO   B O   1 
ATOM   4021  C  CB  . PRO   B 1 175 ? 29.966 38.733  29.408 1   64.87  ? 197 PRO   B CB  1 
ATOM   4022  C  CG  . PRO   B 1 175 ? 30.741 39.797  30.101 1   65.31  ? 197 PRO   B CG  1 
ATOM   4023  C  CD  . PRO   B 1 175 ? 31.68  40.392  29.086 1   63.78  ? 197 PRO   B CD  1 
ATOM   4024  N  N   . GLY   B 1 176 ? 27.773 39.346  26.79  1   63.24  ? 198 GLY   B N   1 
ATOM   4025  C  CA  . GLY   B 1 176 ? 26.524 39.907  26.301 1   63.86  ? 198 GLY   B CA  1 
ATOM   4026  C  C   . GLY   B 1 176 ? 26.49  40.008  24.787 1   64.42  ? 198 GLY   B C   1 
ATOM   4027  O  O   . GLY   B 1 176 ? 25.422 40.158  24.201 1   64.3   ? 198 GLY   B O   1 
ATOM   4028  N  N   . LEU   B 1 177 ? 27.667 39.924  24.14  1   65.09  ? 199 LEU   B N   1 
ATOM   4029  C  CA  . LEU   B 1 177 ? 27.833 39.983  22.692 1   66.09  ? 199 LEU   B CA  1 
ATOM   4030  C  C   . LEU   B 1 177 ? 27.573 38.629  22.028 1   67.28  ? 199 LEU   B C   1 
ATOM   4031  O  O   . LEU   B 1 177 ? 27.18  38.6    20.864 1   67.32  ? 199 LEU   B O   1 
ATOM   4032  C  CB  . LEU   B 1 177 ? 29.27  40.419  22.341 1   65.83  ? 199 LEU   B CB  1 
ATOM   4033  C  CG  . LEU   B 1 177 ? 29.648 41.88   22.496 1   66.41  ? 199 LEU   B CG  1 
ATOM   4034  C  CD1 . LEU   B 1 177 ? 31.04  42.123  21.948 1   66.6   ? 199 LEU   B CD1 1 
ATOM   4035  C  CD2 . LEU   B 1 177 ? 28.67  42.777  21.772 1   66.84  ? 199 LEU   B CD2 1 
ATOM   4036  N  N   . GLU   B 1 178 ? 27.849 37.513  22.739 1   67.96  ? 200 GLU   B N   1 
ATOM   4037  C  CA  . GLU   B 1 178 ? 27.705 36.168  22.187 1   68.98  ? 200 GLU   B CA  1 
ATOM   4038  C  C   . GLU   B 1 178 ? 26.284 35.843  21.766 1   69.77  ? 200 GLU   B C   1 
ATOM   4039  O  O   . GLU   B 1 178 ? 25.33  36.109  22.498 1   69.95  ? 200 GLU   B O   1 
ATOM   4040  C  CB  . GLU   B 1 178 ? 28.277 35.085  23.114 1   71.31  ? 200 GLU   B CB  1 
ATOM   4041  C  CG  . GLU   B 1 178 ? 27.797 35.162  24.546 1   75.88  ? 200 GLU   B CG  1 
ATOM   4042  C  CD  . GLU   B 1 178 ? 28.614 36.081  25.427 1   82.62  ? 200 GLU   B CD  1 
ATOM   4043  O  OE1 . GLU   B 1 178 ? 29.811 36.298  25.128 1   83.97  ? 200 GLU   B OE1 1 
ATOM   4044  O  OE2 . GLU   B 1 178 ? 28.049 36.594  26.418 1   84.9   ? 200 GLU   B OE2 1 
ATOM   4045  N  N   . GLU   B 1 179 ? 26.163 35.295  20.55  1   70.11  ? 201 GLU   B N   1 
ATOM   4046  C  CA  . GLU   B 1 179 ? 24.903 34.933  19.915 1   71.06  ? 201 GLU   B CA  1 
ATOM   4047  C  C   . GLU   B 1 179 ? 24.13  33.902  20.707 1   71.04  ? 201 GLU   B C   1 
ATOM   4048  O  O   . GLU   B 1 179 ? 22.902 33.959  20.745 1   71.4   ? 201 GLU   B O   1 
ATOM   4049  C  CB  . GLU   B 1 179 ? 25.157 34.406  18.501 1   74.53  ? 201 GLU   B CB  1 
ATOM   4050  C  CG  . GLU   B 1 179 ? 25.577 35.469  17.501 1   80.8   ? 201 GLU   B CG  1 
ATOM   4051  C  CD  . GLU   B 1 179 ? 25.255 35.074  16.074 1   89.41  ? 201 GLU   B CD  1 
ATOM   4052  O  OE1 . GLU   B 1 179 ? 26.153 34.535  15.386 1   91.14  ? 201 GLU   B OE1 1 
ATOM   4053  O  OE2 . GLU   B 1 179 ? 24.092 35.277  15.653 1   92.25  ? 201 GLU   B OE2 1 
ATOM   4054  N  N   . SER   B 1 180 ? 24.837 32.949  21.324 1   70.48  ? 202 SER   B N   1 
ATOM   4055  C  CA  . SER   B 1 180 ? 24.203 31.914  22.134 1   70.53  ? 202 SER   B CA  1 
ATOM   4056  C  C   . SER   B 1 180 ? 23.625 32.495  23.439 1   70.4   ? 202 SER   B C   1 
ATOM   4057  O  O   . SER   B 1 180 ? 22.566 32.065  23.894 1   70.4   ? 202 SER   B O   1 
ATOM   4058  C  CB  . SER   B 1 180 ? 25.2   30.803  22.443 1   71.76  ? 202 SER   B CB  1 
ATOM   4059  O  OG  . SER   B 1 180 ? 26.401 31.33   22.981 1   74.27  ? 202 SER   B OG  1 
ATOM   4060  N  N   . GLY   B 1 181 ? 24.319 33.481  24.008 1   69.95  ? 203 GLY   B N   1 
ATOM   4061  C  CA  . GLY   B 1 181 ? 23.917 34.139  25.244 1   69.54  ? 203 GLY   B CA  1 
ATOM   4062  C  C   . GLY   B 1 181 ? 22.936 35.278  25.056 1   68.62  ? 203 GLY   B C   1 
ATOM   4063  O  O   . GLY   B 1 181 ? 21.851 35.076  24.498 1   68.75  ? 203 GLY   B O   1 
ATOM   4064  N  N   . PHE   B 1 182 ? 23.307 36.489  25.535 1   67.32  ? 204 PHE   B N   1 
ATOM   4065  C  CA  . PHE   B 1 182 ? 22.438 37.667  25.457 1   66.55  ? 204 PHE   B CA  1 
ATOM   4066  C  C   . PHE   B 1 182 ? 22.194 38.155  24.018 1   65.49  ? 204 PHE   B C   1 
ATOM   4067  O  O   . PHE   B 1 182 ? 21.106 38.647  23.729 1   65.27  ? 204 PHE   B O   1 
ATOM   4068  C  CB  . PHE   B 1 182 ? 22.952 38.802  26.362 1   66.47  ? 204 PHE   B CB  1 
ATOM   4069  C  CG  . PHE   B 1 182 ? 22.017 39.986  26.472 1   66.98  ? 204 PHE   B CG  1 
ATOM   4070  C  CD1 . PHE   B 1 182 ? 20.817 39.881  27.148 1   67.59  ? 204 PHE   B CD1 1 
ATOM   4071  C  CD2 . PHE   B 1 182 ? 22.336 41.201  25.891 1   67.83  ? 204 PHE   B CD2 1 
ATOM   4072  C  CE1 . PHE   B 1 182 ? 19.955 40.968  27.238 1   68.29  ? 204 PHE   B CE1 1 
ATOM   4073  C  CE2 . PHE   B 1 182 ? 21.469 42.287  25.983 1   68.41  ? 204 PHE   B CE2 1 
ATOM   4074  C  CZ  . PHE   B 1 182 ? 20.289 42.165  26.66  1   68.1   ? 204 PHE   B CZ  1 
ATOM   4075  N  N   . ASN   B 1 183 ? 23.185 37.996  23.122 1   64.66  ? 205 ASN   B N   1 
ATOM   4076  C  CA  . ASN   B 1 183 ? 23.07  38.395  21.715 1   64.4   ? 205 ASN   B CA  1 
ATOM   4077  C  C   . ASN   B 1 183 ? 22.654 39.868  21.568 1   63.3   ? 205 ASN   B C   1 
ATOM   4078  O  O   . ASN   B 1 183 ? 21.585 40.16   21.033 1   63.5   ? 205 ASN   B O   1 
ATOM   4079  C  CB  . ASN   B 1 183 ? 22.105 37.458  20.96  1   65.7   ? 205 ASN   B CB  1 
ATOM   4080  C  CG  . ASN   B 1 183 ? 22.263 37.477  19.46  1   68.91  ? 205 ASN   B CG  1 
ATOM   4081  O  OD1 . ASN   B 1 183 ? 23.155 38.13   18.898 1   70.01  ? 205 ASN   B OD1 1 
ATOM   4082  N  ND2 . ASN   B 1 183 ? 21.401 36.751  18.778 1   70     ? 205 ASN   B ND2 1 
ATOM   4083  N  N   . PHE   B 1 184 ? 23.495 40.788  22.052 1   62     ? 206 PHE   B N   1 
ATOM   4084  C  CA  . PHE   B 1 184 ? 23.191 42.215  22.022 1   61.16  ? 206 PHE   B CA  1 
ATOM   4085  C  C   . PHE   B 1 184 ? 23.06  42.802  20.618 1   60.07  ? 206 PHE   B C   1 
ATOM   4086  O  O   . PHE   B 1 184 ? 22.081 43.496  20.356 1   59.97  ? 206 PHE   B O   1 
ATOM   4087  C  CB  . PHE   B 1 184 ? 24.209 43.026  22.861 1   61.03  ? 206 PHE   B CB  1 
ATOM   4088  C  CG  . PHE   B 1 184 ? 24.147 44.533  22.684 1   61.38  ? 206 PHE   B CG  1 
ATOM   4089  C  CD1 . PHE   B 1 184 ? 23.127 45.273  23.257 1   61.98  ? 206 PHE   B CD1 1 
ATOM   4090  C  CD2 . PHE   B 1 184 ? 25.093 45.2    21.922 1   61.64  ? 206 PHE   B CD2 1 
ATOM   4091  C  CE1 . PHE   B 1 184 ? 23.063 46.648  23.079 1   62.22  ? 206 PHE   B CE1 1 
ATOM   4092  C  CE2 . PHE   B 1 184 ? 25.02  46.574  21.744 1   61.84  ? 206 PHE   B CE2 1 
ATOM   4093  C  CZ  . PHE   B 1 184 ? 24.009 47.285  22.321 1   61.66  ? 206 PHE   B CZ  1 
ATOM   4094  N  N   . TRP   B 1 185 ? 24.045 42.579  19.741 1   58.9   ? 207 TRP   B N   1 
ATOM   4095  C  CA  . TRP   B 1 185 ? 24.036 43.186  18.412 1   58.24  ? 207 TRP   B CA  1 
ATOM   4096  C  C   . TRP   B 1 185 ? 22.758 42.914  17.599 1   56.65  ? 207 TRP   B C   1 
ATOM   4097  O  O   . TRP   B 1 185 ? 22.263 43.821  16.926 1   56.54  ? 207 TRP   B O   1 
ATOM   4098  C  CB  . TRP   B 1 185 ? 25.292 42.791  17.629 1   58.47  ? 207 TRP   B CB  1 
ATOM   4099  C  CG  . TRP   B 1 185 ? 25.74  43.811  16.623 1   59.37  ? 207 TRP   B CG  1 
ATOM   4100  C  CD1 . TRP   B 1 185 ? 25.828 43.646  15.271 1   60.34  ? 207 TRP   B CD1 1 
ATOM   4101  C  CD2 . TRP   B 1 185 ? 26.216 45.133  16.898 1   59.68  ? 207 TRP   B CD2 1 
ATOM   4102  N  NE1 . TRP   B 1 185 ? 26.32  44.79   14.686 1   60.78  ? 207 TRP   B NE1 1 
ATOM   4103  C  CE2 . TRP   B 1 185 ? 26.561 45.722  15.664 1   60.54  ? 207 TRP   B CE2 1 
ATOM   4104  C  CE3 . TRP   B 1 185 ? 26.377 45.883  18.068 1   60.31  ? 207 TRP   B CE3 1 
ATOM   4105  C  CZ2 . TRP   B 1 185 ? 27.053 47.023  15.571 1   61.08  ? 207 TRP   B CZ2 1 
ATOM   4106  C  CZ3 . TRP   B 1 185 ? 26.865 47.173  17.97  1   61.26  ? 207 TRP   B CZ3 1 
ATOM   4107  C  CH2 . TRP   B 1 185 ? 27.196 47.729  16.735 1   61.17  ? 207 TRP   B CH2 1 
ATOM   4108  N  N   . ALA   B 1 186 ? 22.208 41.697  17.691 1   55.17  ? 208 ALA   B N   1 
ATOM   4109  C  CA  . ALA   B 1 186 ? 20.985 41.34   16.979 1   54.4   ? 208 ALA   B CA  1 
ATOM   4110  C  C   . ALA   B 1 186 ? 19.764 42.057  17.572 1   54.07  ? 208 ALA   B C   1 
ATOM   4111  O  O   . ALA   B 1 186 ? 18.882 42.51   16.836 1   54.36  ? 208 ALA   B O   1 
ATOM   4112  C  CB  . ALA   B 1 186 ? 20.782 39.836  17.034 1   54.23  ? 208 ALA   B CB  1 
ATOM   4113  N  N   . LYS   B 1 187 ? 19.715 42.156  18.906 1   53.14  ? 209 LYS   B N   1 
ATOM   4114  C  CA  . LYS   B 1 187 ? 18.624 42.834  19.605 1   52.5   ? 209 LYS   B CA  1 
ATOM   4115  C  C   . LYS   B 1 187 ? 18.662 44.344  19.35  1   52.48  ? 209 LYS   B C   1 
ATOM   4116  O  O   . LYS   B 1 187 ? 17.609 44.981  19.293 1   53.09  ? 209 LYS   B O   1 
ATOM   4117  C  CB  . LYS   B 1 187 ? 18.679 42.548  21.122 1   52.56  ? 209 LYS   B CB  1 
ATOM   4118  C  CG  . LYS   B 1 187 ? 18.459 41.089  21.483 1   52.9   ? 209 LYS   B CG  1 
ATOM   4119  C  CD  . LYS   B 1 187 ? 18.65  40.847  22.97  1   54.15  ? 209 LYS   B CD  1 
ATOM   4120  C  CE  . LYS   B 1 187 ? 18.11  39.512  23.401 1   55.12  ? 209 LYS   B CE  1 
ATOM   4121  N  NZ  . LYS   B 1 187 ? 18.229 39.31   24.859 1   55.32  ? 209 LYS   B NZ  1 
ATOM   4122  N  N   . PHE   B 1 188 ? 19.875 44.91   19.207 1   51.73  ? 210 PHE   B N   1 
ATOM   4123  C  CA  . PHE   B 1 188 ? 20.137 46.334  18.956 1   51.29  ? 210 PHE   B CA  1 
ATOM   4124  C  C   . PHE   B 1 188 ? 19.665 46.698  17.55  1   52.63  ? 210 PHE   B C   1 
ATOM   4125  O  O   . PHE   B 1 188 ? 18.954 47.688  17.381 1   52.69  ? 210 PHE   B O   1 
ATOM   4126  C  CB  . PHE   B 1 188 ? 21.641 46.627  19.156 1   49.64  ? 210 PHE   B CB  1 
ATOM   4127  C  CG  . PHE   B 1 188 ? 22.165 48.011  18.835 1   48.56  ? 210 PHE   B CG  1 
ATOM   4128  C  CD1 . PHE   B 1 188 ? 21.372 49.131  19.005 1   48.52  ? 210 PHE   B CD1 1 
ATOM   4129  C  CD2 . PHE   B 1 188 ? 23.482 48.2    18.473 1   48.41  ? 210 PHE   B CD2 1 
ATOM   4130  C  CE1 . PHE   B 1 188 ? 21.859 50.395  18.723 1   48.48  ? 210 PHE   B CE1 1 
ATOM   4131  C  CE2 . PHE   B 1 188 ? 23.965 49.47   18.204 1   48.57  ? 210 PHE   B CE2 1 
ATOM   4132  C  CZ  . PHE   B 1 188 ? 23.151 50.558  18.328 1   47.97  ? 210 PHE   B CZ  1 
ATOM   4133  N  N   . GLN   B 1 189 ? 19.986 45.86   16.552 1   53.51  ? 211 GLN   B N   1 
ATOM   4134  C  CA  . GLN   B 1 189 ? 19.537 46.102  15.186 1   54.87  ? 211 GLN   B CA  1 
ATOM   4135  C  C   . GLN   B 1 189 ? 18.009 46.123  15.104 1   56.07  ? 211 GLN   B C   1 
ATOM   4136  O  O   . GLN   B 1 189 ? 17.452 46.983  14.43  1   56.47  ? 211 GLN   B O   1 
ATOM   4137  C  CB  . GLN   B 1 189 ? 20.088 45.042  14.233 1   56.56  ? 211 GLN   B CB  1 
ATOM   4138  C  CG  . GLN   B 1 189 ? 21.586 45.083  14.056 1   60.62  ? 211 GLN   B CG  1 
ATOM   4139  C  CD  . GLN   B 1 189 ? 21.979 44.625  12.672 1   65.71  ? 211 GLN   B CD  1 
ATOM   4140  O  OE1 . GLN   B 1 189 ? 21.364 45.014  11.664 1   67.2   ? 211 GLN   B OE1 1 
ATOM   4141  N  NE2 . GLN   B 1 189 ? 23.015 43.791  12.591 1   66.55  ? 211 GLN   B NE2 1 
ATOM   4142  N  N   . GLU   B 1 190 ? 17.344 45.202  15.818 1   56.61  ? 212 GLU   B N   1 
ATOM   4143  C  CA  . GLU   B 1 190 ? 15.889 45.09   15.842 1   58.01  ? 212 GLU   B CA  1 
ATOM   4144  C  C   . GLU   B 1 190 ? 15.26  46.301  16.522 1   58.78  ? 212 GLU   B C   1 
ATOM   4145  O  O   . GLU   B 1 190 ? 14.235 46.813  16.057 1   59.08  ? 212 GLU   B O   1 
ATOM   4146  C  CB  . GLU   B 1 190 ? 15.48  43.818  16.586 1   61.52  ? 212 GLU   B CB  1 
ATOM   4147  C  CG  . GLU   B 1 190 ? 14.946 42.711  15.706 1   69.53  ? 212 GLU   B CG  1 
ATOM   4148  C  CD  . GLU   B 1 190 ? 14.272 41.617  16.513 1   78.67  ? 212 GLU   B CD  1 
ATOM   4149  O  OE1 . GLU   B 1 190 ? 14.727 41.345  17.649 1   80.03  ? 212 GLU   B OE1 1 
ATOM   4150  O  OE2 . GLU   B 1 190 ? 13.275 41.046  16.015 1   81.63  ? 212 GLU   B OE2 1 
ATOM   4151  N  N   . SER   B 1 191 ? 15.863 46.747  17.635 1   58.79  ? 213 SER   B N   1 
ATOM   4152  C  CA  . SER   B 1 191 ? 15.393 47.901  18.393 1   59.21  ? 213 SER   B CA  1 
ATOM   4153  C  C   . SER   B 1 191 ? 15.492 49.158  17.547 1   58.98  ? 213 SER   B C   1 
ATOM   4154  O  O   . SER   B 1 191 ? 14.569 49.97   17.562 1   58.98  ? 213 SER   B O   1 
ATOM   4155  C  CB  . SER   B 1 191 ? 16.225 48.072  19.657 1   61.28  ? 213 SER   B CB  1 
ATOM   4156  O  OG  . SER   B 1 191 ? 16.009 46.993  20.552 1   64.75  ? 213 SER   B OG  1 
ATOM   4157  N  N   . VAL   B 1 192 ? 16.602 49.303  16.793 1   58.57  ? 214 VAL   B N   1 
ATOM   4158  C  CA  . VAL   B 1 192 ? 16.844 50.441  15.917 1   58.62  ? 214 VAL   B CA  1 
ATOM   4159  C  C   . VAL   B 1 192 ? 15.785 50.48   14.836 1   58.61  ? 214 VAL   B C   1 
ATOM   4160  O  O   . VAL   B 1 192 ? 15.189 51.529  14.604 1   58.23  ? 214 VAL   B O   1 
ATOM   4161  C  CB  . VAL   B 1 192 ? 18.286 50.4    15.346 1   59.1   ? 214 VAL   B CB  1 
ATOM   4162  C  CG1 . VAL   B 1 192 ? 18.426 51.245  14.084 1   59.72  ? 214 VAL   B CG1 1 
ATOM   4163  C  CG2 . VAL   B 1 192 ? 19.282 50.86   16.393 1   59.46  ? 214 VAL   B CG2 1 
ATOM   4164  N  N   . ASP   B 1 193 ? 15.536 49.323  14.204 1   58.89  ? 215 ASP   B N   1 
ATOM   4165  C  CA  . ASP   B 1 193 ? 14.561 49.193  13.127 1   59.59  ? 215 ASP   B CA  1 
ATOM   4166  C  C   . ASP   B 1 193 ? 13.165 49.595  13.558 1   59.78  ? 215 ASP   B C   1 
ATOM   4167  O  O   . ASP   B 1 193 ? 12.515 50.36   12.849 1   60.23  ? 215 ASP   B O   1 
ATOM   4168  C  CB  . ASP   B 1 193 ? 14.569 47.768  12.549 1   61.79  ? 215 ASP   B CB  1 
ATOM   4169  C  CG  . ASP   B 1 193 ? 15.73  47.469  11.61  1   66.63  ? 215 ASP   B CG  1 
ATOM   4170  O  OD1 . ASP   B 1 193 ? 16.475 48.418  11.258 1   67.23  ? 215 ASP   B OD1 1 
ATOM   4171  O  OD2 . ASP   B 1 193 ? 15.893 46.284  11.223 1   68.73  ? 215 ASP   B OD2 1 
ATOM   4172  N  N   . ARG   B 1 194 ? 12.721 49.12   14.728 1   59.28  ? 216 ARG   B N   1 
ATOM   4173  C  CA  . ARG   B 1 194 ? 11.408 49.458  15.241 1   59.77  ? 216 ARG   B CA  1 
ATOM   4174  C  C   . ARG   B 1 194 ? 11.337 50.913  15.682 1   59.78  ? 216 ARG   B C   1 
ATOM   4175  O  O   . ARG   B 1 194 ? 10.303 51.549  15.504 1   60.06  ? 216 ARG   B O   1 
ATOM   4176  C  CB  . ARG   B 1 194 ? 11.035 48.54   16.407 1   61.65  ? 216 ARG   B CB  1 
ATOM   4177  C  CG  . ARG   B 1 194 ? 10.755 47.119  15.985 1   65.89  ? 216 ARG   B CG  1 
ATOM   4178  C  CD  . ARG   B 1 194 ? 10.229 46.313  17.152 1   70.34  ? 216 ARG   B CD  1 
ATOM   4179  N  NE  . ARG   B 1 194 ? 11.246 46.113  18.184 1   73.99  ? 216 ARG   B NE  1 
ATOM   4180  C  CZ  . ARG   B 1 194 ? 12.033 45.041  18.268 1   76.21  ? 216 ARG   B CZ  1 
ATOM   4181  N  NH1 . ARG   B 1 194 ? 11.934 44.064  17.373 1   75.42  ? 216 ARG   B NH1 1 
ATOM   4182  N  NH2 . ARG   B 1 194 ? 12.936 44.947  19.238 1   76.1   ? 216 ARG   B NH2 1 
ATOM   4183  N  N   . PHE   B 1 195 ? 12.421 51.433  16.27  1   59.36  ? 217 PHE   B N   1 
ATOM   4184  C  CA  . PHE   B 1 195 ? 12.467 52.814  16.734 1   59.49  ? 217 PHE   B CA  1 
ATOM   4185  C  C   . PHE   B 1 195 ? 12.378 53.784  15.567 1   59.78  ? 217 PHE   B C   1 
ATOM   4186  O  O   . PHE   B 1 195 ? 11.575 54.716  15.606 1   60.13  ? 217 PHE   B O   1 
ATOM   4187  C  CB  . PHE   B 1 195 ? 13.738 53.074  17.562 1   59.22  ? 217 PHE   B CB  1 
ATOM   4188  C  CG  . PHE   B 1 195 ? 13.892 54.505  18.006 1   59.58  ? 217 PHE   B CG  1 
ATOM   4189  C  CD1 . PHE   B 1 195 ? 13.088 55.027  19.003 1   60.32  ? 217 PHE   B CD1 1 
ATOM   4190  C  CD2 . PHE   B 1 195 ? 14.837 55.331  17.422 1   60.29  ? 217 PHE   B CD2 1 
ATOM   4191  C  CE1 . PHE   B 1 195 ? 13.204 56.354  19.386 1   60.92  ? 217 PHE   B CE1 1 
ATOM   4192  C  CE2 . PHE   B 1 195 ? 14.955 56.655  17.81  1   60.95  ? 217 PHE   B CE2 1 
ATOM   4193  C  CZ  . PHE   B 1 195 ? 14.134 57.158  18.787 1   60.73  ? 217 PHE   B CZ  1 
ATOM   4194  N  N   . LEU   B 1 196 ? 13.187 53.562  14.526 1   59.41  ? 218 LEU   B N   1 
ATOM   4195  C  CA  . LEU   B 1 196 ? 13.179 54.429  13.357 1   59.5   ? 218 LEU   B CA  1 
ATOM   4196  C  C   . LEU   B 1 196 ? 11.879 54.347  12.582 1   59.62  ? 218 LEU   B C   1 
ATOM   4197  O  O   . LEU   B 1 196 ? 11.419 55.371  12.082 1   59.46  ? 218 LEU   B O   1 
ATOM   4198  C  CB  . LEU   B 1 196 ? 14.394 54.191  12.456 1   59.39  ? 218 LEU   B CB  1 
ATOM   4199  C  CG  . LEU   B 1 196 ? 15.748 54.533  13.086 1   60.13  ? 218 LEU   B CG  1 
ATOM   4200  C  CD1 . LEU   B 1 196 ? 16.85  54.229  12.141 1   60.71  ? 218 LEU   B CD1 1 
ATOM   4201  C  CD2 . LEU   B 1 196 ? 15.826 55.992  13.53  1   60.15  ? 218 LEU   B CD2 1 
ATOM   4202  N  N   . GLU   B 1 197 ? 11.237 53.162  12.55  1   59.72  ? 219 GLU   B N   1 
ATOM   4203  C  CA  . GLU   B 1 197 ? 9.948  53.031  11.88  1   59.85  ? 219 GLU   B CA  1 
ATOM   4204  C  C   . GLU   B 1 197 ? 8.89   53.833  12.625 1   59.29  ? 219 GLU   B C   1 
ATOM   4205  O  O   . GLU   B 1 197 ? 8.131  54.572  12     1   59.62  ? 219 GLU   B O   1 
ATOM   4206  C  CB  . GLU   B 1 197 ? 9.532  51.568  11.737 1   62.78  ? 219 GLU   B CB  1 
ATOM   4207  C  CG  . GLU   B 1 197 ? 8.161  51.382  11.105 1   69.67  ? 219 GLU   B CG  1 
ATOM   4208  C  CD  . GLU   B 1 197 ? 7.827  52.157  9.838  1   77.86  ? 219 GLU   B CD  1 
ATOM   4209  O  OE1 . GLU   B 1 197 ? 8.754  52.688  9.18   1   80.23  ? 219 GLU   B OE1 1 
ATOM   4210  O  OE2 . GLU   B 1 197 ? 6.622  52.226  9.503  1   79.39  ? 219 GLU   B OE2 1 
ATOM   4211  N  N   . ALA   B 1 198 ? 8.89   53.749  13.96  1   58.55  ? 220 ALA   B N   1 
ATOM   4212  C  CA  . ALA   B 1 198 ? 7.966  54.51   14.803 1   58.56  ? 220 ALA   B CA  1 
ATOM   4213  C  C   . ALA   B 1 198 ? 8.159  56.021  14.63  1   58.22  ? 220 ALA   B C   1 
ATOM   4214  O  O   . ALA   B 1 198 ? 7.193  56.775  14.698 1   57.97  ? 220 ALA   B O   1 
ATOM   4215  C  CB  . ALA   B 1 198 ? 8.151  54.124  16.261 1   58.62  ? 220 ALA   B CB  1 
ATOM   4216  N  N   . GLN   B 1 199 ? 9.407  56.448  14.404 1   58.11  ? 221 GLN   B N   1 
ATOM   4217  C  CA  . GLN   B 1 199 ? 9.768  57.84   14.166 1   58.54  ? 221 GLN   B CA  1 
ATOM   4218  C  C   . GLN   B 1 199 ? 9.241  58.318  12.828 1   58.59  ? 221 GLN   B C   1 
ATOM   4219  O  O   . GLN   B 1 199 ? 8.853  59.475  12.721 1   58.76  ? 221 GLN   B O   1 
ATOM   4220  C  CB  . GLN   B 1 199 ? 11.299 58.025  14.218 1   60.28  ? 221 GLN   B CB  1 
ATOM   4221  C  CG  . GLN   B 1 199 ? 11.886 58.034  15.633 1   62.25  ? 221 GLN   B CG  1 
ATOM   4222  C  CD  . GLN   B 1 199 ? 11.285 59.118  16.478 1   65.57  ? 221 GLN   B CD  1 
ATOM   4223  O  OE1 . GLN   B 1 199 ? 10.731 58.855  17.544 1   67.97  ? 221 GLN   B OE1 1 
ATOM   4224  N  NE2 . GLN   B 1 199 ? 11.36  60.354  16.01  1   65.26  ? 221 GLN   B NE2 1 
ATOM   4225  N  N   . VAL   B 1 200 ? 9.237  57.44   11.806 1   58.34  ? 222 VAL   B N   1 
ATOM   4226  C  CA  . VAL   B 1 200 ? 8.729  57.764  10.473 1   58.49  ? 222 VAL   B CA  1 
ATOM   4227  C  C   . VAL   B 1 200 ? 7.22   57.928  10.519 1   58.48  ? 222 VAL   B C   1 
ATOM   4228  O  O   . VAL   B 1 200 ? 6.702  58.901  9.983  1   58.69  ? 222 VAL   B O   1 
ATOM   4229  C  CB  . VAL   B 1 200 ? 9.182  56.741  9.406  1   59.1   ? 222 VAL   B CB  1 
ATOM   4230  C  CG1 . VAL   B 1 200 ? 8.443  56.946  8.089  1   59.93  ? 222 VAL   B CG1 1 
ATOM   4231  C  CG2 . VAL   B 1 200 ? 10.681 56.834  9.187  1   59.31  ? 222 VAL   B CG2 1 
ATOM   4232  N  N   . GLN   B 1 201 ? 6.523  57.028  11.219 1   58.29  ? 223 GLN   B N   1 
ATOM   4233  C  CA  . GLN   B 1 201 ? 5.074  57.117  11.361 1   58.81  ? 223 GLN   B CA  1 
ATOM   4234  C  C   . GLN   B 1 201 ? 4.645  58.372  12.126 1   58.69  ? 223 GLN   B C   1 
ATOM   4235  O  O   . GLN   B 1 201 ? 3.653  59.009  11.769 1   58.4   ? 223 GLN   B O   1 
ATOM   4236  C  CB  . GLN   B 1 201 ? 4.52   55.845  12.022 1   60.92  ? 223 GLN   B CB  1 
ATOM   4237  C  CG  . GLN   B 1 201 ? 4.771  54.578  11.211 1   65.33  ? 223 GLN   B CG  1 
ATOM   4238  C  CD  . GLN   B 1 201 ? 4.271  54.677  9.777  1   70.83  ? 223 GLN   B CD  1 
ATOM   4239  O  OE1 . GLN   B 1 201 ? 3.113  55.038  9.511  1   72.41  ? 223 GLN   B OE1 1 
ATOM   4240  N  NE2 . GLN   B 1 201 ? 5.144  54.363  8.823  1   71.43  ? 223 GLN   B NE2 1 
ATOM   4241  N  N   . SER   B 1 202 ? 5.433  58.747  13.144 1   58.68  ? 224 SER   B N   1 
ATOM   4242  C  CA  . SER   B 1 202 ? 5.213  59.934  13.96  1   59.17  ? 224 SER   B CA  1 
ATOM   4243  C  C   . SER   B 1 202 ? 5.463  61.198  13.129 1   59.37  ? 224 SER   B C   1 
ATOM   4244  O  O   . SER   B 1 202 ? 4.709  62.166  13.24  1   59.15  ? 224 SER   B O   1 
ATOM   4245  C  CB  . SER   B 1 202 ? 6.132  59.902  15.179 1   60.49  ? 224 SER   B CB  1 
ATOM   4246  O  OG  . SER   B 1 202 ? 5.988  61.057  15.989 1   63.04  ? 224 SER   B OG  1 
ATOM   4247  N  N   . ALA   B 1 203 ? 6.52   61.181  12.291 1   59.46  ? 225 ALA   B N   1 
ATOM   4248  C  CA  . ALA   B 1 203 ? 6.853  62.298  11.405 1   59.84  ? 225 ALA   B CA  1 
ATOM   4249  C  C   . ALA   B 1 203 ? 5.81   62.453  10.303 1   60.15  ? 225 ALA   B C   1 
ATOM   4250  O  O   . ALA   B 1 203 ? 5.591  63.565  9.845  1   60.21  ? 225 ALA   B O   1 
ATOM   4251  C  CB  . ALA   B 1 203 ? 8.224  62.099  10.785 1   59.84  ? 225 ALA   B CB  1 
ATOM   4252  N  N   . MET   B 1 204 ? 5.172  61.349  9.868  1   60.31  ? 226 MET   B N   1 
ATOM   4253  C  CA  . MET   B 1 204 ? 4.137  61.395  8.833  1   61.1   ? 226 MET   B CA  1 
ATOM   4254  C  C   . MET   B 1 204 ? 2.891  62.127  9.316  1   61.84  ? 226 MET   B C   1 
ATOM   4255  O  O   . MET   B 1 204 ? 2.242  62.815  8.53   1   61.84  ? 226 MET   B O   1 
ATOM   4256  C  CB  . MET   B 1 204 ? 3.77   59.984  8.327  1   61.43  ? 226 MET   B CB  1 
ATOM   4257  C  CG  . MET   B 1 204 ? 4.836  59.344  7.467  1   63.15  ? 226 MET   B CG  1 
ATOM   4258  S  SD  . MET   B 1 204 ? 5.359  60.362  6.064  1   67.18  ? 226 MET   B SD  1 
ATOM   4259  C  CE  . MET   B 1 204 ? 6.739  59.39   5.481  1   66.65  ? 226 MET   B CE  1 
ATOM   4260  N  N   . GLU   B 1 205 ? 2.568  62      10.613 1   62.2   ? 227 GLU   B N   1 
ATOM   4261  C  CA  . GLU   B 1 205 ? 1.411  62.669  11.191 1   62.97  ? 227 GLU   B CA  1 
ATOM   4262  C  C   . GLU   B 1 205 ? 1.689  64.118  11.627 1   63.89  ? 227 GLU   B C   1 
ATOM   4263  O  O   . GLU   B 1 205 ? 0.834  64.721  12.279 1   63.9   ? 227 GLU   B O   1 
ATOM   4264  C  CB  . GLU   B 1 205 ? 0.893  61.873  12.386 1   64.78  ? 227 GLU   B CB  1 
ATOM   4265  C  CG  . GLU   B 1 205 ? 0.506  60.446  12.07  1   68.48  ? 227 GLU   B CG  1 
ATOM   4266  C  CD  . GLU   B 1 205 ? 0.086  59.721  13.328 1   73.66  ? 227 GLU   B CD  1 
ATOM   4267  O  OE1 . GLU   B 1 205 ? 0.843  59.761  14.327 1   74.87  ? 227 GLU   B OE1 1 
ATOM   4268  O  OE2 . GLU   B 1 205 ? -1.03  59.156  13.33  1   75.2   ? 227 GLU   B OE2 1 
ATOM   4269  N  N   . GLU   B 1 206 ? 2.869  64.677  11.286 1   64.31  ? 228 GLU   B N   1 
ATOM   4270  C  CA  . GLU   B 1 206 ? 3.211  66.04   11.67  1   65.06  ? 228 GLU   B CA  1 
ATOM   4271  C  C   . GLU   B 1 206 ? 2.314  67.044  10.941 1   65.74  ? 228 GLU   B C   1 
ATOM   4272  O  O   . GLU   B 1 206 ? 2.197  67.011  9.711  1   65.38  ? 228 GLU   B O   1 
ATOM   4273  C  CB  . GLU   B 1 206 ? 4.695  66.33   11.409 1   66.71  ? 228 GLU   B CB  1 
ATOM   4274  C  CG  . GLU   B 1 206 ? 5.288  67.357  12.355 1   70.05  ? 228 GLU   B CG  1 
ATOM   4275  C  CD  . GLU   B 1 206 ? 5.68   66.807  13.705 1   73.3   ? 228 GLU   B CD  1 
ATOM   4276  O  OE1 . GLU   B 1 206 ? 5.933  65.586  13.789 1   73.68  ? 228 GLU   B OE1 1 
ATOM   4277  O  OE2 . GLU   B 1 206 ? 5.749  67.592  14.676 1   74.73  ? 228 GLU   B OE2 1 
ATOM   4278  N  N   . PRO   B 1 207 ? 1.623  67.906  11.712 1   66.41  ? 229 PRO   B N   1 
ATOM   4279  C  CA  . PRO   B 1 207 ? 0.719  68.877  11.082 1   67.06  ? 229 PRO   B CA  1 
ATOM   4280  C  C   . PRO   B 1 207 ? 1.452  69.963  10.294 1   67.95  ? 229 PRO   B C   1 
ATOM   4281  O  O   . PRO   B 1 207 ? 1.033  70.28   9.18   1   68.43  ? 229 PRO   B O   1 
ATOM   4282  C  CB  . PRO   B 1 207 ? -0.084 69.437  12.259 1   67.62  ? 229 PRO   B CB  1 
ATOM   4283  C  CG  . PRO   B 1 207 ? 0.78   69.222  13.458 1   67.78  ? 229 PRO   B CG  1 
ATOM   4284  C  CD  . PRO   B 1 207 ? 1.63   68.024  13.187 1   66     ? 229 PRO   B CD  1 
ATOM   4285  N  N   . VAL   B 1 208 ? 2.552  70.518  10.848 1   67.83  ? 230 VAL   B N   1 
ATOM   4286  C  CA  . VAL   B 1 208 ? 3.33   71.544  10.153 1   68.09  ? 230 VAL   B CA  1 
ATOM   4287  C  C   . VAL   B 1 208 ? 4.187  70.856  9.091  1   67.78  ? 230 VAL   B C   1 
ATOM   4288  O  O   . VAL   B 1 208 ? 4.867  69.881  9.4    1   67.9   ? 230 VAL   B O   1 
ATOM   4289  C  CB  . VAL   B 1 208 ? 4.195  72.369  11.133 1   69.01  ? 230 VAL   B CB  1 
ATOM   4290  C  CG1 . VAL   B 1 208 ? 4.88   73.528  10.409 1   69.63  ? 230 VAL   B CG1 1 
ATOM   4291  C  CG2 . VAL   B 1 208 ? 3.368  72.864  12.319 1   69.2   ? 230 VAL   B CG2 1 
ATOM   4292  N  N   . GLU   B 1 209 ? 4.121  71.322  7.843  1   67.31  ? 231 GLU   B N   1 
ATOM   4293  C  CA  . GLU   B 1 209 ? 4.864  70.7    6.751  1   67.45  ? 231 GLU   B CA  1 
ATOM   4294  C  C   . GLU   B 1 209 ? 6.386  70.861  6.891  1   66.64  ? 231 GLU   B C   1 
ATOM   4295  O  O   . GLU   B 1 209 ? 7.126  69.93   6.57   1   66.32  ? 231 GLU   B O   1 
ATOM   4296  C  CB  . GLU   B 1 209 ? 4.349  71.208  5.391  1   70.31  ? 231 GLU   B CB  1 
ATOM   4297  C  CG  . GLU   B 1 209 ? 4.941  70.493  4.188  1   76.89  ? 231 GLU   B CG  1 
ATOM   4298  C  CD  . GLU   B 1 209 ? 4.488  69.067  3.933  1   84.35  ? 231 GLU   B CD  1 
ATOM   4299  O  OE1 . GLU   B 1 209 ? 3.519  68.617  4.586  1   86.75  ? 231 GLU   B OE1 1 
ATOM   4300  O  OE2 . GLU   B 1 209 ? 5.1    68.401  3.064  1   85.56  ? 231 GLU   B OE2 1 
ATOM   4301  N  N   . LYS   B 1 210 ? 6.845  72.012  7.425  1   66.05  ? 232 LYS   B N   1 
ATOM   4302  C  CA  . LYS   B 1 210 ? 8.275  72.259  7.622  1   66.25  ? 232 LYS   B CA  1 
ATOM   4303  C  C   . LYS   B 1 210 ? 8.897  71.261  8.597  1   65.94  ? 232 LYS   B C   1 
ATOM   4304  O  O   . LYS   B 1 210 ? 9.987  70.738  8.339  1   65.94  ? 232 LYS   B O   1 
ATOM   4305  C  CB  . LYS   B 1 210 ? 8.526  73.699  8.112  1   68.27  ? 232 LYS   B CB  1 
ATOM   4306  C  CG  . LYS   B 1 210 ? 10.011 74.066  8.171  1   72.25  ? 232 LYS   B CG  1 
ATOM   4307  C  CD  . LYS   B 1 210 ? 10.265 75.492  8.635  1   76.32  ? 232 LYS   B CD  1 
ATOM   4308  C  CE  . LYS   B 1 210 ? 9.725  75.754  10.017 1   80.47  ? 232 LYS   B CE  1 
ATOM   4309  N  NZ  . LYS   B 1 210 ? 10.252 74.785  11.011 1   82.82  ? 232 LYS   B NZ  1 
ATOM   4310  N  N   . ALA   B 1 211 ? 8.191  70.993  9.71   1   65.47  ? 233 ALA   B N   1 
ATOM   4311  C  CA  . ALA   B 1 211 ? 8.633  70.069  10.749 1   65.47  ? 233 ALA   B CA  1 
ATOM   4312  C  C   . ALA   B 1 211 ? 8.644  68.626  10.246 1   65.29  ? 233 ALA   B C   1 
ATOM   4313  O  O   . ALA   B 1 211 ? 9.55   67.865  10.573 1   65.29  ? 233 ALA   B O   1 
ATOM   4314  C  CB  . ALA   B 1 211 ? 7.734  70.197  11.968 1   65.52  ? 233 ALA   B CB  1 
ATOM   4315  N  N   . LYS   B 1 212 ? 7.646  68.265  9.437  1   64.95  ? 234 LYS   B N   1 
ATOM   4316  C  CA  . LYS   B 1 212 ? 7.493  66.938  8.852  1   65.09  ? 234 LYS   B CA  1 
ATOM   4317  C  C   . LYS   B 1 212 ? 8.701  66.569  7.979  1   64.69  ? 234 LYS   B C   1 
ATOM   4318  O  O   . LYS   B 1 212 ? 9.271  65.486  8.123  1   64.58  ? 234 LYS   B O   1 
ATOM   4319  C  CB  . LYS   B 1 212 ? 6.197  66.917  8.033  1   67.09  ? 234 LYS   B CB  1 
ATOM   4320  C  CG  . LYS   B 1 212 ? 5.924  65.623  7.289  1   72.06  ? 234 LYS   B CG  1 
ATOM   4321  C  CD  . LYS   B 1 212 ? 4.569  65.715  6.603  1   77.56  ? 234 LYS   B CD  1 
ATOM   4322  C  CE  . LYS   B 1 212 ? 4.129  64.379  6.056  1   81.87  ? 234 LYS   B CE  1 
ATOM   4323  N  NZ  . LYS   B 1 212 ? 4.741  64.112  4.72   1   83.91  ? 234 LYS   B NZ  1 
ATOM   4324  N  N   . ASN   B 1 213 ? 9.105  67.495  7.104  1   64.21  ? 235 ASN   B N   1 
ATOM   4325  C  CA  . ASN   B 1 213 ? 10.228 67.3    6.204  1   64.24  ? 235 ASN   B CA  1 
ATOM   4326  C  C   . ASN   B 1 213 ? 11.533 67.237  6.953  1   63.85  ? 235 ASN   B C   1 
ATOM   4327  O  O   . ASN   B 1 213 ? 12.395 66.429  6.599  1   64.14  ? 235 ASN   B O   1 
ATOM   4328  C  CB  . ASN   B 1 213 ? 10.273 68.422  5.175  1   65.69  ? 235 ASN   B CB  1 
ATOM   4329  C  CG  . ASN   B 1 213 ? 9.004  68.554  4.374  1   69     ? 235 ASN   B CG  1 
ATOM   4330  O  OD1 . ASN   B 1 213 ? 8.24   67.594  4.209  1   70.14  ? 235 ASN   B OD1 1 
ATOM   4331  N  ND2 . ASN   B 1 213 ? 8.754  69.753  3.86   1   69.86  ? 235 ASN   B ND2 1 
ATOM   4332  N  N   . TYR   B 1 214 ? 11.683 68.079  7.999  1   63.17  ? 236 TYR   B N   1 
ATOM   4333  C  CA  . TYR   B 1 214 ? 12.895 68.116  8.81   1   63.23  ? 236 TYR   B CA  1 
ATOM   4334  C  C   . TYR   B 1 214 ? 13.113 66.771  9.475  1   62.26  ? 236 TYR   B C   1 
ATOM   4335  O  O   . TYR   B 1 214 ? 14.218 66.232  9.412  1   62.59  ? 236 TYR   B O   1 
ATOM   4336  C  CB  . TYR   B 1 214 ? 12.835 69.233  9.866  1   64.01  ? 236 TYR   B CB  1 
ATOM   4337  C  CG  . TYR   B 1 214 ? 14.083 69.305  10.723 1   65.93  ? 236 TYR   B CG  1 
ATOM   4338  C  CD1 . TYR   B 1 214 ? 15.246 69.889  10.244 1   67.53  ? 236 TYR   B CD1 1 
ATOM   4339  C  CD2 . TYR   B 1 214 ? 14.105 68.771  12.005 1   67.16  ? 236 TYR   B CD2 1 
ATOM   4340  C  CE1 . TYR   B 1 214 ? 16.402 69.941  11.017 1   68.68  ? 236 TYR   B CE1 1 
ATOM   4341  C  CE2 . TYR   B 1 214 ? 15.255 68.811  12.785 1   68.35  ? 236 TYR   B CE2 1 
ATOM   4342  C  CZ  . TYR   B 1 214 ? 16.402 69.405  12.291 1   69.65  ? 236 TYR   B CZ  1 
ATOM   4343  O  OH  . TYR   B 1 214 ? 17.55  69.466  13.056 1   71.52  ? 236 TYR   B OH  1 
ATOM   4344  N  N   . ARG   B 1 215 ? 12.042 66.21   10.065 1   60.92  ? 237 ARG   B N   1 
ATOM   4345  C  CA  . ARG   B 1 215 ? 12.1   64.92   10.742 1   59.87  ? 237 ARG   B CA  1 
ATOM   4346  C  C   . ARG   B 1 215 ? 12.452 63.808  9.786  1   59     ? 237 ARG   B C   1 
ATOM   4347  O  O   . ARG   B 1 215 ? 13.327 63.022  10.103 1   58.94  ? 237 ARG   B O   1 
ATOM   4348  C  CB  . ARG   B 1 215 ? 10.786 64.616  11.467 1   60.31  ? 237 ARG   B CB  1 
ATOM   4349  C  CG  . ARG   B 1 215 ? 10.546 65.523  12.656 1   61.94  ? 237 ARG   B CG  1 
ATOM   4350  C  CD  . ARG   B 1 215 ? 9.351  65.082  13.478 1   63.96  ? 237 ARG   B CD  1 
ATOM   4351  N  NE  . ARG   B 1 215 ? 9.584  63.787  14.113 1   64.74  ? 237 ARG   B NE  1 
ATOM   4352  C  CZ  . ARG   B 1 215 ? 8.692  63.143  14.857 1   65.01  ? 237 ARG   B CZ  1 
ATOM   4353  N  NH1 . ARG   B 1 215 ? 7.496  63.674  15.084 1   63.81  ? 237 ARG   B NH1 1 
ATOM   4354  N  NH2 . ARG   B 1 215 ? 8.988  61.966  15.384 1   64.61  ? 237 ARG   B NH2 1 
ATOM   4355  N  N   . LEU   B 1 216 ? 11.828 63.774  8.597  1   58.22  ? 238 LEU   B N   1 
ATOM   4356  C  CA  . LEU   B 1 216 ? 12.11  62.739  7.602  1   57.9   ? 238 LEU   B CA  1 
ATOM   4357  C  C   . LEU   B 1 216 ? 13.543 62.807  7.076  1   57.37  ? 238 LEU   B C   1 
ATOM   4358  O  O   . LEU   B 1 216 ? 14.157 61.763  6.847  1   56.78  ? 238 LEU   B O   1 
ATOM   4359  C  CB  . LEU   B 1 216 ? 11.096 62.795  6.448  1   58.02  ? 238 LEU   B CB  1 
ATOM   4360  C  CG  . LEU   B 1 216 ? 9.664  62.447  6.828  1   58.95  ? 238 LEU   B CG  1 
ATOM   4361  C  CD1 . LEU   B 1 216 ? 8.748  62.637  5.657  1   59.1   ? 238 LEU   B CD1 1 
ATOM   4362  C  CD2 . LEU   B 1 216 ? 9.565  61.017  7.379  1   59.25  ? 238 LEU   B CD2 1 
ATOM   4363  N  N   . MET   B 1 217 ? 14.079 64.036  6.898  1   57.22  ? 239 MET   B N   1 
ATOM   4364  C  CA  . MET   B 1 217 ? 15.464 64.212  6.456  1   57.36  ? 239 MET   B CA  1 
ATOM   4365  C  C   . MET   B 1 217 ? 16.414 63.713  7.543  1   56.35  ? 239 MET   B C   1 
ATOM   4366  O  O   . MET   B 1 217 ? 17.401 63.038  7.239  1   56.41  ? 239 MET   B O   1 
ATOM   4367  C  CB  . MET   B 1 217 ? 15.759 65.686  6.127  1   59.39  ? 239 MET   B CB  1 
ATOM   4368  C  CG  . MET   B 1 217 ? 15.125 66.159  4.828  1   64.72  ? 239 MET   B CG  1 
ATOM   4369  S  SD  . MET   B 1 217 ? 16.035 67.5    4.001  1   75.42  ? 239 MET   B SD  1 
ATOM   4370  C  CE  . MET   B 1 217 ? 16.245 66.765  2.344  1   73.68  ? 239 MET   B CE  1 
ATOM   4371  N  N   . ASP   B 1 218 ? 16.085 64.024  8.818  1   55.27  ? 240 ASP   B N   1 
ATOM   4372  C  CA  . ASP   B 1 218 ? 16.85  63.63   9.988  1   54.63  ? 240 ASP   B CA  1 
ATOM   4373  C  C   . ASP   B 1 218 ? 16.858 62.119  10.197 1   53.36  ? 240 ASP   B C   1 
ATOM   4374  O  O   . ASP   B 1 218 ? 17.926 61.558  10.436 1   53.52  ? 240 ASP   B O   1 
ATOM   4375  C  CB  . ASP   B 1 218 ? 16.349 64.372  11.229 1   56.81  ? 240 ASP   B CB  1 
ATOM   4376  C  CG  . ASP   B 1 218 ? 17.17  64.081  12.463 1   62.21  ? 240 ASP   B CG  1 
ATOM   4377  O  OD1 . ASP   B 1 218 ? 18.403 64.337  12.437 1   62.55  ? 240 ASP   B OD1 1 
ATOM   4378  O  OD2 . ASP   B 1 218 ? 16.585 63.602  13.466 1   65.03  ? 240 ASP   B OD2 1 
ATOM   4379  N  N   . ILE   B 1 219 ? 15.696 61.448  10.063 1   52.16  ? 241 ILE   B N   1 
ATOM   4380  C  CA  . ILE   B 1 219 ? 15.612 59.98   10.176 1   51.74  ? 241 ILE   B CA  1 
ATOM   4381  C  C   . ILE   B 1 219 ? 16.498 59.308  9.126  1   51.58  ? 241 ILE   B C   1 
ATOM   4382  O  O   . ILE   B 1 219 ? 17.116 58.276  9.4    1   51.75  ? 241 ILE   B O   1 
ATOM   4383  C  CB  . ILE   B 1 219 ? 14.152 59.463  10.092 1   51.65  ? 241 ILE   B CB  1 
ATOM   4384  C  CG1 . ILE   B 1 219 ? 13.294 60.02   11.242 1   51.68  ? 241 ILE   B CG1 1 
ATOM   4385  C  CG2 . ILE   B 1 219 ? 14.115 57.929  10.076 1   52.03  ? 241 ILE   B CG2 1 
ATOM   4386  C  CD1 . ILE   B 1 219 ? 11.85  60.027  10.955 1   52.33  ? 241 ILE   B CD1 1 
ATOM   4387  N  N   . GLU   B 1 220 ? 16.6   59.923  7.944  1   51.14  ? 242 GLU   B N   1 
ATOM   4388  C  CA  . GLU   B 1 220 ? 17.443 59.413  6.888  1   51.57  ? 242 GLU   B CA  1 
ATOM   4389  C  C   . GLU   B 1 220 ? 18.933 59.49   7.268  1   50.73  ? 242 GLU   B C   1 
ATOM   4390  O  O   . GLU   B 1 220 ? 19.684 58.54   7.012  1   50.64  ? 242 GLU   B O   1 
ATOM   4391  C  CB  . GLU   B 1 220 ? 17.118 60.107  5.556  1   55.17  ? 242 GLU   B CB  1 
ATOM   4392  C  CG  . GLU   B 1 220 ? 17.39  59.253  4.324  1   62.88  ? 242 GLU   B CG  1 
ATOM   4393  C  CD  . GLU   B 1 220 ? 16.983 57.787  4.389  1   71.29  ? 242 GLU   B CD  1 
ATOM   4394  O  OE1 . GLU   B 1 220 ? 15.802 57.505  4.714  1   73.17  ? 242 GLU   B OE1 1 
ATOM   4395  O  OE2 . GLU   B 1 220 ? 17.855 56.922  4.129  1   72.68  ? 242 GLU   B OE2 1 
ATOM   4396  N  N   . LYS   B 1 221 ? 19.33  60.57   7.955  1   49.96  ? 243 LYS   B N   1 
ATOM   4397  C  CA  . LYS   B 1 221 ? 20.694 60.756  8.455  1   49.67  ? 243 LYS   B CA  1 
ATOM   4398  C  C   . LYS   B 1 221 ? 21.034 59.683  9.486  1   49     ? 243 LYS   B C   1 
ATOM   4399  O  O   . LYS   B 1 221 ? 22.163 59.191  9.497  1   48.22  ? 243 LYS   B O   1 
ATOM   4400  C  CB  . LYS   B 1 221 ? 20.859 62.161  9.07   1   51.88  ? 243 LYS   B CB  1 
ATOM   4401  C  CG  . LYS   B 1 221 ? 20.605 63.304  8.085  1   56.16  ? 243 LYS   B CG  1 
ATOM   4402  C  CD  . LYS   B 1 221 ? 21.876 63.698  7.297  1   59.79  ? 243 LYS   B CD  1 
ATOM   4403  C  CE  . LYS   B 1 221 ? 21.609 64.677  6.171  1   63.14  ? 243 LYS   B CE  1 
ATOM   4404  N  NZ  . LYS   B 1 221 ? 22.26  64.271  4.881  1   64.92  ? 243 LYS   B NZ  1 
ATOM   4405  N  N   . ARG   B 1 222 ? 20.038 59.312  10.339 1   49.27  ? 244 ARG   B N   1 
ATOM   4406  C  CA  . ARG   B 1 222 ? 20.151 58.261  11.354 1   49.83  ? 244 ARG   B CA  1 
ATOM   4407  C  C   . ARG   B 1 222 ? 20.35  56.909  10.688 1   50.79  ? 244 ARG   B C   1 
ATOM   4408  O  O   . ARG   B 1 222 ? 21.243 56.174  11.094 1   50.73  ? 244 ARG   B O   1 
ATOM   4409  C  CB  . ARG   B 1 222 ? 18.909 58.215  12.265 1   50.53  ? 244 ARG   B CB  1 
ATOM   4410  C  CG  . ARG   B 1 222 ? 18.629 59.509  13.03  1   51.93  ? 244 ARG   B CG  1 
ATOM   4411  C  CD  . ARG   B 1 222 ? 19.787 59.95   13.912 1   52.97  ? 244 ARG   B CD  1 
ATOM   4412  N  NE  . ARG   B 1 222 ? 20.104 58.963  14.945 1   53.26  ? 244 ARG   B NE  1 
ATOM   4413  C  CZ  . ARG   B 1 222 ? 21.326 58.743  15.418 1   54.74  ? 244 ARG   B CZ  1 
ATOM   4414  N  NH1 . ARG   B 1 222 ? 22.363 59.431  14.948 1   53.1   ? 244 ARG   B NH1 1 
ATOM   4415  N  NH2 . ARG   B 1 222 ? 21.526 57.825  16.357 1   55.47  ? 244 ARG   B NH2 1 
ATOM   4416  N  N   . ARG   B 1 223 ? 19.57  56.605  9.625  1   51.48  ? 245 ARG   B N   1 
ATOM   4417  C  CA  . ARG   B 1 223 ? 19.696 55.353  8.868  1   52.22  ? 245 ARG   B CA  1 
ATOM   4418  C  C   . ARG   B 1 223 ? 21.114 55.177  8.316  1   52.33  ? 245 ARG   B C   1 
ATOM   4419  O  O   . ARG   B 1 223 ? 21.644 54.064  8.31   1   52.41  ? 245 ARG   B O   1 
ATOM   4420  C  CB  . ARG   B 1 223 ? 18.676 55.3    7.723  1   54.06  ? 245 ARG   B CB  1 
ATOM   4421  C  CG  . ARG   B 1 223 ? 17.244 55.112  8.183  1   57.37  ? 245 ARG   B CG  1 
ATOM   4422  C  CD  . ARG   B 1 223 ? 16.357 54.67   7.034  1   61.07  ? 245 ARG   B CD  1 
ATOM   4423  N  NE  . ARG   B 1 223 ? 14.933 54.891  7.303  1   64.69  ? 245 ARG   B NE  1 
ATOM   4424  C  CZ  . ARG   B 1 223 ? 14.159 54.05   7.986  1   67.08  ? 245 ARG   B CZ  1 
ATOM   4425  N  NH1 . ARG   B 1 223 ? 14.667 52.936  8.504  1   67.38  ? 245 ARG   B NH1 1 
ATOM   4426  N  NH2 . ARG   B 1 223 ? 12.875 54.325  8.172  1   66.06  ? 245 ARG   B NH2 1 
ATOM   4427  N  N   . GLU   B 1 224 ? 21.73  56.28   7.866  1   52.18  ? 246 GLU   B N   1 
ATOM   4428  C  CA  . GLU   B 1 224 ? 23.103 56.268  7.371  1   52.62  ? 246 GLU   B CA  1 
ATOM   4429  C  C   . GLU   B 1 224 ? 24.11  56.008  8.483  1   52.36  ? 246 GLU   B C   1 
ATOM   4430  O  O   . GLU   B 1 224 ? 25.129 55.365  8.241  1   52.61  ? 246 GLU   B O   1 
ATOM   4431  C  CB  . GLU   B 1 224 ? 23.441 57.575  6.655  1   55.86  ? 246 GLU   B CB  1 
ATOM   4432  C  CG  . GLU   B 1 224 ? 23.24  57.51   5.149  1   64.24  ? 246 GLU   B CG  1 
ATOM   4433  C  CD  . GLU   B 1 224 ? 23.812 56.289  4.448  1   73.78  ? 246 GLU   B CD  1 
ATOM   4434  O  OE1 . GLU   B 1 224 ? 25.058 56.176  4.368  1   75.77  ? 246 GLU   B OE1 1 
ATOM   4435  O  OE2 . GLU   B 1 224 ? 23.011 55.434  4      1   76.52  ? 246 GLU   B OE2 1 
ATOM   4436  N  N   . VAL   B 1 225 ? 23.825 56.505  9.701  1   51.85  ? 247 VAL   B N   1 
ATOM   4437  C  CA  . VAL   B 1 225 ? 24.659 56.3    10.889 1   52.29  ? 247 VAL   B CA  1 
ATOM   4438  C  C   . VAL   B 1 225 ? 24.664 54.809  11.232 1   52.71  ? 247 VAL   B C   1 
ATOM   4439  O  O   . VAL   B 1 225 ? 25.731 54.213  11.393 1   53.04  ? 247 VAL   B O   1 
ATOM   4440  C  CB  . VAL   B 1 225 ? 24.197 57.18   12.096 1   52.52  ? 247 VAL   B CB  1 
ATOM   4441  C  CG1 . VAL   B 1 225 ? 24.723 56.659  13.432 1   52.67  ? 247 VAL   B CG1 1 
ATOM   4442  C  CG2 . VAL   B 1 225 ? 24.611 58.626  11.9   1   52.98  ? 247 VAL   B CG2 1 
ATOM   4443  N  N   . TYR   B 1 226 ? 23.472 54.203  11.319 1   52.42  ? 248 TYR   B N   1 
ATOM   4444  C  CA  . TYR   B 1 226 ? 23.361 52.79   11.666 1   52.3   ? 248 TYR   B CA  1 
ATOM   4445  C  C   . TYR   B 1 226 ? 23.883 51.872  10.58  1   52.85  ? 248 TYR   B C   1 
ATOM   4446  O  O   . TYR   B 1 226 ? 24.349 50.788  10.9   1   53.48  ? 248 TYR   B O   1 
ATOM   4447  C  CB  . TYR   B 1 226 ? 21.947 52.434  12.099 1   51.75  ? 248 TYR   B CB  1 
ATOM   4448  C  CG  . TYR   B 1 226 ? 21.584 53.133  13.391 1   52.06  ? 248 TYR   B CG  1 
ATOM   4449  C  CD1 . TYR   B 1 226 ? 22.285 52.88   14.561 1   52.81  ? 248 TYR   B CD1 1 
ATOM   4450  C  CD2 . TYR   B 1 226 ? 20.578 54.085  13.43  1   52.71  ? 248 TYR   B CD2 1 
ATOM   4451  C  CE1 . TYR   B 1 226 ? 21.958 53.523  15.749 1   53.76  ? 248 TYR   B CE1 1 
ATOM   4452  C  CE2 . TYR   B 1 226 ? 20.258 54.75   14.604 1   53.68  ? 248 TYR   B CE2 1 
ATOM   4453  C  CZ  . TYR   B 1 226 ? 20.945 54.465  15.765 1   54.51  ? 248 TYR   B CZ  1 
ATOM   4454  O  OH  . TYR   B 1 226 ? 20.611 55.129  16.921 1   55.67  ? 248 TYR   B OH  1 
ATOM   4455  N  N   . ARG   B 1 227 ? 23.906 52.328  9.324  1   52.56  ? 249 ARG   B N   1 
ATOM   4456  C  CA  . ARG   B 1 227 ? 24.485 51.575  8.225  1   53.11  ? 249 ARG   B CA  1 
ATOM   4457  C  C   . ARG   B 1 227 ? 25.989 51.393  8.464  1   53.37  ? 249 ARG   B C   1 
ATOM   4458  O  O   . ARG   B 1 227 ? 26.517 50.307  8.256  1   53.76  ? 249 ARG   B O   1 
ATOM   4459  C  CB  . ARG   B 1 227 ? 24.254 52.321  6.913  1   55.15  ? 249 ARG   B CB  1 
ATOM   4460  C  CG  . ARG   B 1 227 ? 24.019 51.388  5.74   1   59.34  ? 249 ARG   B CG  1 
ATOM   4461  C  CD  . ARG   B 1 227 ? 23.8   52.15   4.451  1   63.38  ? 249 ARG   B CD  1 
ATOM   4462  N  NE  . ARG   B 1 227 ? 24.99  52.909  4.053  1   66.62  ? 249 ARG   B NE  1 
ATOM   4463  C  CZ  . ARG   B 1 227 ? 25.973 52.424  3.299  1   69.35  ? 249 ARG   B CZ  1 
ATOM   4464  N  NH1 . ARG   B 1 227 ? 25.921 51.174  2.849  1   68.84  ? 249 ARG   B NH1 1 
ATOM   4465  N  NH2 . ARG   B 1 227 ? 27.008 53.189  2.975  1   69.74  ? 249 ARG   B NH2 1 
ATOM   4466  N  N   . SER   B 1 228 ? 26.663 52.434  8.967  1   53.31  ? 250 SER   B N   1 
ATOM   4467  C  CA  . SER   B 1 228 ? 28.09  52.402  9.27   1   53.62  ? 250 SER   B CA  1 
ATOM   4468  C  C   . SER   B 1 228 ? 28.483 51.423  10.378 1   53.64  ? 250 SER   B C   1 
ATOM   4469  O  O   . SER   B 1 228 ? 29.665 51.094  10.497 1   54.07  ? 250 SER   B O   1 
ATOM   4470  C  CB  . SER   B 1 228 ? 28.607 53.801  9.592  1   54.98  ? 250 SER   B CB  1 
ATOM   4471  O  OG  . SER   B 1 228 ? 28.136 54.259  10.849 1   57.39  ? 250 SER   B OG  1 
ATOM   4472  N  N   . ILE   B 1 229 ? 27.517 50.955  11.186 1   52.97  ? 251 ILE   B N   1 
ATOM   4473  C  CA  . ILE   B 1 229 ? 27.834 49.993  12.246 1   52.81  ? 251 ILE   B CA  1 
ATOM   4474  C  C   . ILE   B 1 229 ? 27.2   48.617  11.994 1   52.96  ? 251 ILE   B C   1 
ATOM   4475  O  O   . ILE   B 1 229 ? 27.768 47.609  12.387 1   52.62  ? 251 ILE   B O   1 
ATOM   4476  C  CB  . ILE   B 1 229 ? 27.526 50.532  13.672 1   52.47  ? 251 ILE   B CB  1 
ATOM   4477  C  CG1 . ILE   B 1 229 ? 26.078 51.005  13.813 1   52.98  ? 251 ILE   B CG1 1 
ATOM   4478  C  CG2 . ILE   B 1 229 ? 28.492 51.635  14.036 1   52.61  ? 251 ILE   B CG2 1 
ATOM   4479  C  CD1 . ILE   B 1 229 ? 25.653 51.161  15.206 1   53.99  ? 251 ILE   B CD1 1 
ATOM   4480  N  N   . PHE   B 1 230 ? 26.047 48.576  11.33  1   53.36  ? 252 PHE   B N   1 
ATOM   4481  C  CA  . PHE   B 1 230 ? 25.359 47.32   11.064 1   54.56  ? 252 PHE   B CA  1 
ATOM   4482  C  C   . PHE   B 1 230 ? 25.791 46.617  9.747  1   55.44  ? 252 PHE   B C   1 
ATOM   4483  O  O   . PHE   B 1 230 ? 25.392 45.475  9.49   1   55.36  ? 252 PHE   B O   1 
ATOM   4484  C  CB  . PHE   B 1 230 ? 23.845 47.532  11.13  1   54.53  ? 252 PHE   B CB  1 
ATOM   4485  C  CG  . PHE   B 1 230 ? 23.359 47.994  12.487 1   54.96  ? 252 PHE   B CG  1 
ATOM   4486  C  CD1 . PHE   B 1 230 ? 24.01  47.609  13.647 1   55.4   ? 252 PHE   B CD1 1 
ATOM   4487  C  CD2 . PHE   B 1 230 ? 22.231 48.785  12.601 1   55.73  ? 252 PHE   B CD2 1 
ATOM   4488  C  CE1 . PHE   B 1 230 ? 23.563 48.039  14.881 1   55.78  ? 252 PHE   B CE1 1 
ATOM   4489  C  CE2 . PHE   B 1 230 ? 21.767 49.185  13.846 1   56.06  ? 252 PHE   B CE2 1 
ATOM   4490  C  CZ  . PHE   B 1 230 ? 22.442 48.819  14.971 1   55.59  ? 252 PHE   B CZ  1 
ATOM   4491  N  N   . ASP   B 1 231 ? 26.615 47.29   8.937  1   55.67  ? 253 ASP   B N   1 
ATOM   4492  C  CA  . ASP   B 1 231 ? 27.18  46.726  7.725  1   56.5   ? 253 ASP   B CA  1 
ATOM   4493  C  C   . ASP   B 1 231 ? 28.678 46.668  7.986  1   56.85  ? 253 ASP   B C   1 
ATOM   4494  O  O   . ASP   B 1 231 ? 29.325 47.709  8.071  1   56.51  ? 253 ASP   B O   1 
ATOM   4495  C  CB  . ASP   B 1 231 ? 26.871 47.618  6.511  1   58.64  ? 253 ASP   B CB  1 
ATOM   4496  C  CG  . ASP   B 1 231 ? 27.246 47.041  5.152  1   63.74  ? 253 ASP   B CG  1 
ATOM   4497  O  OD1 . ASP   B 1 231 ? 28.036 46.071  5.112  1   64.67  ? 253 ASP   B OD1 1 
ATOM   4498  O  OD2 . ASP   B 1 231 ? 26.757 47.571  4.126  1   65.76  ? 253 ASP   B OD2 1 
ATOM   4499  N  N   . PRO   B 1 232 ? 29.237 45.461  8.175  1   57.67  ? 254 PRO   B N   1 
ATOM   4500  C  CA  . PRO   B 1 232 ? 30.673 45.354  8.477  1   58.49  ? 254 PRO   B CA  1 
ATOM   4501  C  C   . PRO   B 1 232 ? 31.572 45.889  7.373  1   59.47  ? 254 PRO   B C   1 
ATOM   4502  O  O   . PRO   B 1 232 ? 32.663 46.37   7.679  1   60.15  ? 254 PRO   B O   1 
ATOM   4503  C  CB  . PRO   B 1 232 ? 30.889 43.852  8.698  1   59.15  ? 254 PRO   B CB  1 
ATOM   4504  C  CG  . PRO   B 1 232 ? 29.519 43.291  8.942  1   59.47  ? 254 PRO   B CG  1 
ATOM   4505  C  CD  . PRO   B 1 232 ? 28.592 44.136  8.138  1   57.53  ? 254 PRO   B CD  1 
ATOM   4506  N  N   . ALA   B 1 233 ? 31.11  45.84   6.106  1   58.93  ? 255 ALA   B N   1 
ATOM   4507  C  CA  . ALA   B 1 233 ? 31.878 46.351  4.979  1   58.85  ? 255 ALA   B CA  1 
ATOM   4508  C  C   . ALA   B 1 233 ? 32.044 47.863  5.088  1   58.57  ? 255 ALA   B C   1 
ATOM   4509  O  O   . ALA   B 1 233 ? 33.122 48.374  4.789  1   58.81  ? 255 ALA   B O   1 
ATOM   4510  C  CB  . ALA   B 1 233 ? 31.197 45.99   3.666  1   58.85  ? 255 ALA   B CB  1 
ATOM   4511  N  N   . VAL   B 1 234 ? 30.987 48.574  5.523  1   57.89  ? 256 VAL   B N   1 
ATOM   4512  C  CA  . VAL   B 1 234 ? 31.036 50.027  5.695  1   57.69  ? 256 VAL   B CA  1 
ATOM   4513  C  C   . VAL   B 1 234 ? 31.977 50.398  6.851  1   58.15  ? 256 VAL   B C   1 
ATOM   4514  O  O   . VAL   B 1 234 ? 32.713 51.386  6.753  1   58.37  ? 256 VAL   B O   1 
ATOM   4515  C  CB  . VAL   B 1 234 ? 29.635 50.647  5.861  1   57.52  ? 256 VAL   B CB  1 
ATOM   4516  C  CG1 . VAL   B 1 234 ? 29.724 52.158  5.994  1   58.19  ? 256 VAL   B CG1 1 
ATOM   4517  C  CG2 . VAL   B 1 234 ? 28.756 50.283  4.694  1   57.43  ? 256 VAL   B CG2 1 
ATOM   4518  N  N   . HIS   B 1 235 ? 31.99  49.581  7.92   1   57.81  ? 257 HIS   B N   1 
ATOM   4519  C  CA  . HIS   B 1 235 ? 32.894 49.79   9.044  1   58.08  ? 257 HIS   B CA  1 
ATOM   4520  C  C   . HIS   B 1 235 ? 34.351 49.582  8.589  1   58.62  ? 257 HIS   B C   1 
ATOM   4521  O  O   . HIS   B 1 235 ? 35.193 50.441  8.839  1   58.44  ? 257 HIS   B O   1 
ATOM   4522  C  CB  . HIS   B 1 235 ? 32.54  48.866  10.227 1   58.11  ? 257 HIS   B CB  1 
ATOM   4523  C  CG  . HIS   B 1 235 ? 33.569 48.875  11.317 1   58.68  ? 257 HIS   B CG  1 
ATOM   4524  N  ND1 . HIS   B 1 235 ? 33.63  49.899  12.236 1   60.31  ? 257 HIS   B ND1 1 
ATOM   4525  C  CD2 . HIS   B 1 235 ? 34.574 48.006  11.568 1   59.34  ? 257 HIS   B CD2 1 
ATOM   4526  C  CE1 . HIS   B 1 235 ? 34.652 49.616  13.026 1   60.5   ? 257 HIS   B CE1 1 
ATOM   4527  N  NE2 . HIS   B 1 235 ? 35.25  48.487  12.662 1   60.31  ? 257 HIS   B NE2 1 
ATOM   4528  N  N   . ASP   B 1 236 ? 34.634 48.467  7.901  1   59.16  ? 258 ASP   B N   1 
ATOM   4529  C  CA  . ASP   B 1 236 ? 35.976 48.149  7.41   1   60.35  ? 258 ASP   B CA  1 
ATOM   4530  C  C   . ASP   B 1 236 ? 36.528 49.239  6.486  1   61.39  ? 258 ASP   B C   1 
ATOM   4531  O  O   . ASP   B 1 236 ? 37.736 49.497  6.491  1   61.4   ? 258 ASP   B O   1 
ATOM   4532  C  CB  . ASP   B 1 236 ? 35.982 46.794  6.691  1   61.89  ? 258 ASP   B CB  1 
ATOM   4533  C  CG  . ASP   B 1 236 ? 35.638 45.609  7.573  1   65.84  ? 258 ASP   B CG  1 
ATOM   4534  O  OD1 . ASP   B 1 236 ? 35.717 45.749  8.812  1   65.95  ? 258 ASP   B OD1 1 
ATOM   4535  O  OD2 . ASP   B 1 236 ? 35.27  44.541  7.019  1   67.96  ? 258 ASP   B OD2 1 
ATOM   4536  N  N   . ALA   B 1 237 ? 35.635 49.886  5.71   1   61.9   ? 259 ALA   B N   1 
ATOM   4537  C  CA  . ALA   B 1 237 ? 36.005 50.97   4.8    1   62.9   ? 259 ALA   B CA  1 
ATOM   4538  C  C   . ALA   B 1 237 ? 36.458 52.186  5.595  1   64.02  ? 259 ALA   B C   1 
ATOM   4539  O  O   . ALA   B 1 237 ? 37.443 52.82   5.223  1   64.39  ? 259 ALA   B O   1 
ATOM   4540  C  CB  . ALA   B 1 237 ? 34.837 51.335  3.899  1   62.91  ? 259 ALA   B CB  1 
ATOM   4541  N  N   . LEU   B 1 238 ? 35.768 52.486  6.712  1   64.07  ? 260 LEU   B N   1 
ATOM   4542  C  CA  . LEU   B 1 238 ? 36.105 53.589  7.61   1   64.35  ? 260 LEU   B CA  1 
ATOM   4543  C  C   . LEU   B 1 238 ? 37.4   53.347  8.362  1   64.05  ? 260 LEU   B C   1 
ATOM   4544  O  O   . LEU   B 1 238 ? 38.098 54.307  8.665  1   64.06  ? 260 LEU   B O   1 
ATOM   4545  C  CB  . LEU   B 1 238 ? 34.969 53.836  8.596  1   64.96  ? 260 LEU   B CB  1 
ATOM   4546  C  CG  . LEU   B 1 238 ? 33.736 54.464  7.977  1   66.92  ? 260 LEU   B CG  1 
ATOM   4547  C  CD1 . LEU   B 1 238 ? 32.536 54.239  8.821  1   67.36  ? 260 LEU   B CD1 1 
ATOM   4548  C  CD2 . LEU   B 1 238 ? 33.925 55.93   7.788  1   67.74  ? 260 LEU   B CD2 1 
ATOM   4549  N  N   . VAL   B 1 239 ? 37.725 52.079  8.666  1   63.97  ? 261 VAL   B N   1 
ATOM   4550  C  CA  . VAL   B 1 239 ? 38.966 51.723  9.359  1   64.39  ? 261 VAL   B CA  1 
ATOM   4551  C  C   . VAL   B 1 239 ? 40.15  51.964  8.419  1   65.29  ? 261 VAL   B C   1 
ATOM   4552  O  O   . VAL   B 1 239 ? 41.14  52.592  8.814  1   64.84  ? 261 VAL   B O   1 
ATOM   4553  C  CB  . VAL   B 1 239 ? 38.938 50.276  9.918  1   64.4   ? 261 VAL   B CB  1 
ATOM   4554  C  CG1 . VAL   B 1 239 ? 40.305 49.875  10.463 1   64.69  ? 261 VAL   B CG1 1 
ATOM   4555  C  CG2 . VAL   B 1 239 ? 37.872 50.124  10.996 1   64.58  ? 261 VAL   B CG2 1 
ATOM   4556  N  N   . ARG   B 1 240 ? 40.003 51.531  7.146  1   66.32  ? 262 ARG   B N   1 
ATOM   4557  C  CA  . ARG   B 1 240 ? 41.004 51.722  6.089  1   67.48  ? 262 ARG   B CA  1 
ATOM   4558  C  C   . ARG   B 1 240 ? 41.172 53.202  5.742  1   67.36  ? 262 ARG   B C   1 
ATOM   4559  O  O   . ARG   B 1 240 ? 42.287 53.664  5.509  1   67.73  ? 262 ARG   B O   1 
ATOM   4560  C  CB  . ARG   B 1 240 ? 40.623 50.918  4.842  1   70.1   ? 262 ARG   B CB  1 
ATOM   4561  C  CG  . ARG   B 1 240 ? 40.864 49.423  5.03   1   75.88  ? 262 ARG   B CG  1 
ATOM   4562  C  CD  . ARG   B 1 240 ? 40.65  48.635  3.748  1   80.99  ? 262 ARG   B CD  1 
ATOM   4563  N  NE  . ARG   B 1 240 ? 39.28  48.126  3.627  1   85.2   ? 262 ARG   B NE  1 
ATOM   4564  C  CZ  . ARG   B 1 240 ? 38.33  48.684  2.88   1   87.99  ? 262 ARG   B CZ  1 
ATOM   4565  N  NH1 . ARG   B 1 240 ? 38.585 49.786  2.18   1   87.59  ? 262 ARG   B NH1 1 
ATOM   4566  N  NH2 . ARG   B 1 240 ? 37.117 48.147  2.828  1   88.17  ? 262 ARG   B NH2 1 
ATOM   4567  N  N   . ARG   B 1 241 ? 40.062 53.947  5.741  1   66.73  ? 263 ARG   B N   1 
ATOM   4568  C  CA  . ARG   B 1 241 ? 40.012 55.388  5.495  1   66.41  ? 263 ARG   B CA  1 
ATOM   4569  C  C   . ARG   B 1 241 ? 40.677 56.198  6.65   1   65.62  ? 263 ARG   B C   1 
ATOM   4570  O  O   . ARG   B 1 241 ? 41.163 57.309  6.427  1   65.97  ? 263 ARG   B O   1 
ATOM   4571  C  CB  . ARG   B 1 241 ? 38.544 55.794  5.302  1   67.99  ? 263 ARG   B CB  1 
ATOM   4572  C  CG  . ARG   B 1 241 ? 38.276 57.276  5.166  1   71.8   ? 263 ARG   B CG  1 
ATOM   4573  C  CD  . ARG   B 1 241 ? 36.812 57.592  5.419  1   75.61  ? 263 ARG   B CD  1 
ATOM   4574  N  NE  . ARG   B 1 241 ? 36.01  57.612  4.192  1   79.28  ? 263 ARG   B NE  1 
ATOM   4575  C  CZ  . ARG   B 1 241 ? 34.73  57.973  4.137  1   81.75  ? 263 ARG   B CZ  1 
ATOM   4576  N  NH1 . ARG   B 1 241 ? 34.105 58.4    5.228  1   80.81  ? 263 ARG   B NH1 1 
ATOM   4577  N  NH2 . ARG   B 1 241 ? 34.084 57.97   2.977  1   82.53  ? 263 ARG   B NH2 1 
ATOM   4578  N  N   . GLY   B 1 242 ? 40.714 55.63   7.853  1   64.21  ? 264 GLY   B N   1 
ATOM   4579  C  CA  . GLY   B 1 242 ? 41.327 56.28   9.002  1   63.52  ? 264 GLY   B CA  1 
ATOM   4580  C  C   . GLY   B 1 242 ? 40.354 56.895  9.989  1   62.53  ? 264 GLY   B C   1 
ATOM   4581  O  O   . GLY   B 1 242 ? 40.777 57.386  11.042 1   63.34  ? 264 GLY   B O   1 
ATOM   4582  N  N   . ASP   B 1 243 ? 39.049 56.882  9.667  1   60.87  ? 265 ASP   B N   1 
ATOM   4583  C  CA  . ASP   B 1 243 ? 38.001 57.418  10.543 1   60.09  ? 265 ASP   B CA  1 
ATOM   4584  C  C   . ASP   B 1 243 ? 37.793 56.559  11.816 1   58.41  ? 265 ASP   B C   1 
ATOM   4585  O  O   . ASP   B 1 243 ? 37.326 57.062  12.837 1   58.2   ? 265 ASP   B O   1 
ATOM   4586  C  CB  . ASP   B 1 243 ? 36.681 57.571  9.771  1   62.23  ? 265 ASP   B CB  1 
ATOM   4587  C  CG  . ASP   B 1 243 ? 36.691 58.671  8.716  1   67.1   ? 265 ASP   B CG  1 
ATOM   4588  O  OD1 . ASP   B 1 243 ? 37.792 59.142  8.358  1   68.45  ? 265 ASP   B OD1 1 
ATOM   4589  O  OD2 . ASP   B 1 243 ? 35.591 59.056  8.242  1   68.51  ? 265 ASP   B OD2 1 
ATOM   4590  N  N   . ARG   B 1 244 ? 38.159 55.267  11.745 1   57.04  ? 266 ARG   B N   1 
ATOM   4591  C  CA  . ARG   B 1 244 ? 38.074 54.31   12.843 1   56.17  ? 266 ARG   B CA  1 
ATOM   4592  C  C   . ARG   B 1 244 ? 39.369 53.491  12.966 1   55.96  ? 266 ARG   B C   1 
ATOM   4593  O  O   . ARG   B 1 244 ? 40.14  53.393  12.014 1   56.33  ? 266 ARG   B O   1 
ATOM   4594  C  CB  . ARG   B 1 244 ? 36.862 53.383  12.65  1   56.21  ? 266 ARG   B CB  1 
ATOM   4595  C  CG  . ARG   B 1 244 ? 35.549 54.101  12.868 1   56.26  ? 266 ARG   B CG  1 
ATOM   4596  C  CD  . ARG   B 1 244 ? 34.361 53.2    12.709 1   56.86  ? 266 ARG   B CD  1 
ATOM   4597  N  NE  . ARG   B 1 244 ? 33.137 53.99   12.61  1   57.69  ? 266 ARG   B NE  1 
ATOM   4598  C  CZ  . ARG   B 1 244 ? 31.941 53.498  12.311 1   57.39  ? 266 ARG   B CZ  1 
ATOM   4599  N  NH1 . ARG   B 1 244 ? 31.787 52.199  12.086 1   55.22  ? 266 ARG   B NH1 1 
ATOM   4600  N  NH2 . ARG   B 1 244 ? 30.888 54.301  12.233 1   56.76  ? 266 ARG   B NH2 1 
ATOM   4601  N  N   . ARG   B 1 245 ? 39.612 52.929  14.149 1   55.38  ? 267 ARG   B N   1 
ATOM   4602  C  CA  . ARG   B 1 245 ? 40.776 52.1    14.467 1   55.32  ? 267 ARG   B CA  1 
ATOM   4603  C  C   . ARG   B 1 245 ? 40.32  50.71   14.947 1   53.9   ? 267 ARG   B C   1 
ATOM   4604  O  O   . ARG   B 1 245 ? 40.958 49.703  14.652 1   53.6   ? 267 ARG   B O   1 
ATOM   4605  C  CB  . ARG   B 1 245 ? 41.602 52.755  15.599 1   58.02  ? 267 ARG   B CB  1 
ATOM   4606  C  CG  . ARG   B 1 245 ? 42.633 53.776  15.151 1   63.94  ? 267 ARG   B CG  1 
ATOM   4607  C  CD  . ARG   B 1 245 ? 42.568 55.018  16.024 1   69.58  ? 267 ARG   B CD  1 
ATOM   4608  N  NE  . ARG   B 1 245 ? 43.758 55.864  15.877 1   74.53  ? 267 ARG   B NE  1 
ATOM   4609  C  CZ  . ARG   B 1 245 ? 43.88  56.831  14.968 1   78.02  ? 267 ARG   B CZ  1 
ATOM   4610  N  NH1 . ARG   B 1 245 ? 42.892 57.077  14.109 1   78     ? 267 ARG   B NH1 1 
ATOM   4611  N  NH2 . ARG   B 1 245 ? 44.993 57.548  14.901 1   78.43  ? 267 ARG   B NH2 1 
ATOM   4612  N  N   . PHE   B 1 246 ? 39.242 50.683  15.739 1   52.96  ? 268 PHE   B N   1 
ATOM   4613  C  CA  . PHE   B 1 246 ? 38.675 49.508  16.384 1   52.2   ? 268 PHE   B CA  1 
ATOM   4614  C  C   . PHE   B 1 246 ? 38.2   48.469  15.415 1   50.72  ? 268 PHE   B C   1 
ATOM   4615  O  O   . PHE   B 1 246 ? 37.693 48.803  14.345 1   50.89  ? 268 PHE   B O   1 
ATOM   4616  C  CB  . PHE   B 1 246 ? 37.469 49.912  17.241 1   52.3   ? 268 PHE   B CB  1 
ATOM   4617  C  CG  . PHE   B 1 246 ? 37.78  50.466  18.608 1   53.34  ? 268 PHE   B CG  1 
ATOM   4618  C  CD1 . PHE   B 1 246 ? 38.938 51.196  18.833 1   54.1   ? 268 PHE   B CD1 1 
ATOM   4619  C  CD2 . PHE   B 1 246 ? 36.877 50.325  19.649 1   54.15  ? 268 PHE   B CD2 1 
ATOM   4620  C  CE1 . PHE   B 1 246 ? 39.202 51.735  20.083 1   54.78  ? 268 PHE   B CE1 1 
ATOM   4621  C  CE2 . PHE   B 1 246 ? 37.138 50.874  20.891 1   54.74  ? 268 PHE   B CE2 1 
ATOM   4622  C  CZ  . PHE   B 1 246 ? 38.303 51.567  21.104 1   54.57  ? 268 PHE   B CZ  1 
ATOM   4623  N  N   . SER   B 1 247 ? 38.298 47.202  15.82  1   48.98  ? 269 SER   B N   1 
ATOM   4624  C  CA  . SER   B 1 247 ? 37.732 46.115  15.048 1   48.22  ? 269 SER   B CA  1 
ATOM   4625  C  C   . SER   B 1 247 ? 36.193 46.219  15.18  1   47.84  ? 269 SER   B C   1 
ATOM   4626  O  O   . SER   B 1 247 ? 35.694 46.84   16.125 1   48.26  ? 269 SER   B O   1 
ATOM   4627  C  CB  . SER   B 1 247 ? 38.2   44.781  15.608 1   48.87  ? 269 SER   B CB  1 
ATOM   4628  O  OG  . SER   B 1 247 ? 37.61  44.506  16.869 1   50.33  ? 269 SER   B OG  1 
ATOM   4629  N  N   . HIS   B 1 248 ? 35.439 45.595  14.269 1   46.98  ? 270 HIS   B N   1 
ATOM   4630  C  CA  . HIS   B 1 248 ? 33.981 45.635  14.326 1   46.72  ? 270 HIS   B CA  1 
ATOM   4631  C  C   . HIS   B 1 248 ? 33.442 45.128  15.683 1   47.23  ? 270 HIS   B C   1 
ATOM   4632  O  O   . HIS   B 1 248 ? 32.645 45.822  16.321 1   47.32  ? 270 HIS   B O   1 
ATOM   4633  C  CB  . HIS   B 1 248 ? 33.394 44.842  13.157 1   46.81  ? 270 HIS   B CB  1 
ATOM   4634  C  CG  . HIS   B 1 248 ? 31.925 45.033  12.968 1   48.15  ? 270 HIS   B CG  1 
ATOM   4635  N  ND1 . HIS   B 1 248 ? 31.395 46.275  12.682 1   49.85  ? 270 HIS   B ND1 1 
ATOM   4636  C  CD2 . HIS   B 1 248 ? 30.925 44.123  12.976 1   49.17  ? 270 HIS   B CD2 1 
ATOM   4637  C  CE1 . HIS   B 1 248 ? 30.093 46.091  12.561 1   50.2   ? 270 HIS   B CE1 1 
ATOM   4638  N  NE2 . HIS   B 1 248 ? 29.762 44.812  12.719 1   50.25  ? 270 HIS   B NE2 1 
ATOM   4639  N  N   . ARG   B 1 249 ? 33.966 43.978  16.165 1   47.03  ? 271 ARG   B N   1 
ATOM   4640  C  CA  . ARG   B 1 249 ? 33.532 43.393  17.428 1   47.46  ? 271 ARG   B CA  1 
ATOM   4641  C  C   . ARG   B 1 249 ? 33.928 44.214  18.657 1   47.11  ? 271 ARG   B C   1 
ATOM   4642  O  O   . ARG   B 1 249 ? 33.182 44.21   19.64  1   47.23  ? 271 ARG   B O   1 
ATOM   4643  C  CB  . ARG   B 1 249 ? 33.993 41.94   17.557 1   49.5   ? 271 ARG   B CB  1 
ATOM   4644  C  CG  . ARG   B 1 249 ? 33.26  41.199  18.659 1   53.65  ? 271 ARG   B CG  1 
ATOM   4645  C  CD  . ARG   B 1 249 ? 33.442 39.708  18.553 1   57.57  ? 271 ARG   B CD  1 
ATOM   4646  N  NE  . ARG   B 1 249 ? 32.906 39.012  19.721 1   60.62  ? 271 ARG   B NE  1 
ATOM   4647  C  CZ  . ARG   B 1 249 ? 31.641 38.628  19.849 1   63.58  ? 271 ARG   B CZ  1 
ATOM   4648  N  NH1 . ARG   B 1 249 ? 30.76  38.885  18.886 1   63.03  ? 271 ARG   B NH1 1 
ATOM   4649  N  NH2 . ARG   B 1 249 ? 31.242 37.994  20.944 1   63.95  ? 271 ARG   B NH2 1 
ATOM   4650  N  N   . ALA   B 1 250 ? 35.065 44.942  18.601 1   46.46  ? 272 ALA   B N   1 
ATOM   4651  C  CA  . ALA   B 1 250 ? 35.474 45.818  19.704 1   46.01  ? 272 ALA   B CA  1 
ATOM   4652  C  C   . ALA   B 1 250 ? 34.522 47.004  19.793 1   46.39  ? 272 ALA   B C   1 
ATOM   4653  O  O   . ALA   B 1 250 ? 34.152 47.404  20.89  1   46.7   ? 272 ALA   B O   1 
ATOM   4654  C  CB  . ALA   B 1 250 ? 36.899 46.303  19.511 1   45.86  ? 272 ALA   B CB  1 
ATOM   4655  N  N   . LEU   B 1 251 ? 34.084 47.538  18.648 1   46.77  ? 273 LEU   B N   1 
ATOM   4656  C  CA  . LEU   B 1 251 ? 33.119 48.631  18.602 1   47.81  ? 273 LEU   B CA  1 
ATOM   4657  C  C   . LEU   B 1 251 ? 31.736 48.178  19.119 1   48.76  ? 273 LEU   B C   1 
ATOM   4658  O  O   . LEU   B 1 251 ? 31.015 48.966  19.725 1   48.93  ? 273 LEU   B O   1 
ATOM   4659  C  CB  . LEU   B 1 251 ? 33.008 49.143  17.18  1   48.26  ? 273 LEU   B CB  1 
ATOM   4660  C  CG  . LEU   B 1 251 ? 32.139 50.366  16.99  1   50.75  ? 273 LEU   B CG  1 
ATOM   4661  C  CD1 . LEU   B 1 251 ? 32.723 51.557  17.718 1   51.73  ? 273 LEU   B CD1 1 
ATOM   4662  C  CD2 . LEU   B 1 251 ? 31.972 50.685  15.507 1   51.63  ? 273 LEU   B CD2 1 
ATOM   4663  N  N   . GLN   B 1 252 ? 31.38  46.899  18.911 1   49.06  ? 274 GLN   B N   1 
ATOM   4664  C  CA  . GLN   B 1 252 ? 30.122 46.345  19.417 1   49.51  ? 274 GLN   B CA  1 
ATOM   4665  C  C   . GLN   B 1 252 ? 30.171 46.333  20.944 1   49.86  ? 274 GLN   B C   1 
ATOM   4666  O  O   . GLN   B 1 252 ? 29.219 46.769  21.585 1   50.23  ? 274 GLN   B O   1 
ATOM   4667  C  CB  . GLN   B 1 252 ? 29.886 44.916  18.886 1   51.02  ? 274 GLN   B CB  1 
ATOM   4668  C  CG  . GLN   B 1 252 ? 29.765 44.813  17.365 1   54.28  ? 274 GLN   B CG  1 
ATOM   4669  C  CD  . GLN   B 1 252 ? 29.551 43.397  16.877 1   58.8   ? 274 GLN   B CD  1 
ATOM   4670  O  OE1 . GLN   B 1 252 ? 29.388 42.447  17.661 1   61.84  ? 274 GLN   B OE1 1 
ATOM   4671  N  NE2 . GLN   B 1 252 ? 29.541 43.22   15.563 1   58.08  ? 274 GLN   B NE2 1 
ATOM   4672  N  N   . GLY   B 1 253 ? 31.289 45.863  21.505 1   49.42  ? 275 GLY   B N   1 
ATOM   4673  C  CA  . GLY   B 1 253 ? 31.498 45.818  22.944 1   49.42  ? 275 GLY   B CA  1 
ATOM   4674  C  C   . GLY   B 1 253 ? 31.532 47.192  23.583 1   49.19  ? 275 GLY   B C   1 
ATOM   4675  O  O   . GLY   B 1 253 ? 30.964 47.394  24.658 1   49.48  ? 275 GLY   B O   1 
ATOM   4676  N  N   . ALA   B 1 254 ? 32.18  48.154  22.915 1   48.51  ? 276 ALA   B N   1 
ATOM   4677  C  CA  . ALA   B 1 254 ? 32.261 49.525  23.405 1   48.1   ? 276 ALA   B CA  1 
ATOM   4678  C  C   . ALA   B 1 254 ? 30.874 50.154  23.429 1   47.71  ? 276 ALA   B C   1 
ATOM   4679  O  O   . ALA   B 1 254 ? 30.514 50.771  24.429 1   48.02  ? 276 ALA   B O   1 
ATOM   4680  C  CB  . ALA   B 1 254 ? 33.206 50.343  22.536 1   48.26  ? 276 ALA   B CB  1 
ATOM   4681  N  N   . ILE   B 1 255 ? 30.075 49.941  22.367 1   46.98  ? 277 ILE   B N   1 
ATOM   4682  C  CA  . ILE   B 1 255 ? 28.704 50.454  22.272 1   46.97  ? 277 ILE   B CA  1 
ATOM   4683  C  C   . ILE   B 1 255 ? 27.83  49.847  23.363 1   46.86  ? 277 ILE   B C   1 
ATOM   4684  O  O   . ILE   B 1 255 ? 27.076 50.559  24.018 1   46.69  ? 277 ILE   B O   1 
ATOM   4685  C  CB  . ILE   B 1 255 ? 28.138 50.218  20.836 1   47.49  ? 277 ILE   B CB  1 
ATOM   4686  C  CG1 . ILE   B 1 255 ? 28.691 51.265  19.865 1   48.46  ? 277 ILE   B CG1 1 
ATOM   4687  C  CG2 . ILE   B 1 255 ? 26.605 50.192  20.792 1   47.83  ? 277 ILE   B CG2 1 
ATOM   4688  C  CD1 . ILE   B 1 255 ? 28.476 50.934  18.428 1   50.2   ? 277 ILE   B CD1 1 
ATOM   4689  N  N   . MET   B 1 256 ? 27.966 48.546  23.586 1   47.19  ? 278 MET   B N   1 
ATOM   4690  C  CA  . MET   B 1 256 ? 27.192 47.833  24.592 1   48.38  ? 278 MET   B CA  1 
ATOM   4691  C  C   . MET   B 1 256 ? 27.432 48.37   25.991 1   49.8   ? 278 MET   B C   1 
ATOM   4692  O  O   . MET   B 1 256 ? 26.474 48.601  26.724 1   50.25  ? 278 MET   B O   1 
ATOM   4693  C  CB  . MET   B 1 256 ? 27.497 46.33   24.558 1   48.94  ? 278 MET   B CB  1 
ATOM   4694  C  CG  . MET   B 1 256 ? 26.532 45.551  25.373 1   50.45  ? 278 MET   B CG  1 
ATOM   4695  S  SD  . MET   B 1 256 ? 26.932 43.816  25.486 1   54.36  ? 278 MET   B SD  1 
ATOM   4696  C  CE  . MET   B 1 256 ? 25.552 43.279  26.483 1   55.07  ? 278 MET   B CE  1 
ATOM   4697  N  N   . ILE   B 1 257 ? 28.711 48.586  26.36  1   49.93  ? 279 ILE   B N   1 
ATOM   4698  C  CA  . ILE   B 1 257 ? 29.085 49.127  27.647 1   50.07  ? 279 ILE   B CA  1 
ATOM   4699  C  C   . ILE   B 1 257 ? 28.485 50.525  27.826 1   51.12  ? 279 ILE   B C   1 
ATOM   4700  O  O   . ILE   B 1 257 ? 27.971 50.816  28.897 1   52.14  ? 279 ILE   B O   1 
ATOM   4701  C  CB  . ILE   B 1 257 ? 30.626 49.121  27.762 1   50.63  ? 279 ILE   B CB  1 
ATOM   4702  C  CG1 . ILE   B 1 257 ? 31.159 47.694  27.929 1   51.61  ? 279 ILE   B CG1 1 
ATOM   4703  C  CG2 . ILE   B 1 257 ? 31.11  50.002  28.9   1   50.93  ? 279 ILE   B CG2 1 
ATOM   4704  C  CD1 . ILE   B 1 257 ? 32.681 47.57   27.847 1   52.84  ? 279 ILE   B CD1 1 
ATOM   4705  N  N   . THR   B 1 258 ? 28.511 51.381  26.784 1   51.08  ? 280 THR   B N   1 
ATOM   4706  C  CA  . THR   B 1 258 ? 27.957 52.738  26.879 1   51.65  ? 280 THR   B CA  1 
ATOM   4707  C  C   . THR   B 1 258 ? 26.439 52.776  27.022 1   52.44  ? 280 THR   B C   1 
ATOM   4708  O  O   . THR   B 1 258 ? 25.896 53.774  27.493 1   52.56  ? 280 THR   B O   1 
ATOM   4709  C  CB  . THR   B 1 258 ? 28.42  53.618  25.721 1   53.2   ? 280 THR   B CB  1 
ATOM   4710  O  OG1 . THR   B 1 258 ? 27.955 53.087  24.484 1   54.25  ? 280 THR   B OG1 1 
ATOM   4711  C  CG2 . THR   B 1 258 ? 29.929 53.789  25.681 1   53.62  ? 280 THR   B CG2 1 
ATOM   4712  N  N   . PHE   B 1 259 ? 25.753 51.702  26.611 1   52.76  ? 281 PHE   B N   1 
ATOM   4713  C  CA  . PHE   B 1 259 ? 24.301 51.584  26.703 1   53.17  ? 281 PHE   B CA  1 
ATOM   4714  C  C   . PHE   B 1 259 ? 23.878 51.184  28.113 1   53.88  ? 281 PHE   B C   1 
ATOM   4715  O  O   . PHE   B 1 259 ? 22.853 51.664  28.615 1   54.01  ? 281 PHE   B O   1 
ATOM   4716  C  CB  . PHE   B 1 259 ? 23.798 50.525  25.713 1   52.92  ? 281 PHE   B CB  1 
ATOM   4717  C  CG  . PHE   B 1 259 ? 23.456 51.03   24.334 1   53.48  ? 281 PHE   B CG  1 
ATOM   4718  C  CD1 . PHE   B 1 259 ? 24.098 52.133  23.802 1   54.27  ? 281 PHE   B CD1 1 
ATOM   4719  C  CD2 . PHE   B 1 259 ? 22.512 50.385  23.558 1   54     ? 281 PHE   B CD2 1 
ATOM   4720  C  CE1 . PHE   B 1 259 ? 23.805 52.574  22.523 1   54.67  ? 281 PHE   B CE1 1 
ATOM   4721  C  CE2 . PHE   B 1 259 ? 22.211 50.84   22.29  1   54.37  ? 281 PHE   B CE2 1 
ATOM   4722  C  CZ  . PHE   B 1 259 ? 22.856 51.932  21.782 1   54.25  ? 281 PHE   B CZ  1 
ATOM   4723  N  N   . TYR   B 1 260 ? 24.661 50.288  28.752 1   53.94  ? 282 TYR   B N   1 
ATOM   4724  C  CA  . TYR   B 1 260 ? 24.338 49.78   30.08  1   54.23  ? 282 TYR   B CA  1 
ATOM   4725  C  C   . TYR   B 1 260 ? 25.281 50.265  31.163 1   54.69  ? 282 TYR   B C   1 
ATOM   4726  O  O   . TYR   B 1 260 ? 25.419 49.594  32.172 1   55.1   ? 282 TYR   B O   1 
ATOM   4727  C  CB  . TYR   B 1 260 ? 24.279 48.249  30.062 1   54.04  ? 282 TYR   B CB  1 
ATOM   4728  C  CG  . TYR   B 1 260 ? 23.371 47.692  28.988 1   54.86  ? 282 TYR   B CG  1 
ATOM   4729  C  CD1 . TYR   B 1 260 ? 21.994 47.774  29.103 1   55.82  ? 282 TYR   B CD1 1 
ATOM   4730  C  CD2 . TYR   B 1 260 ? 23.892 47.091  27.85  1   55.7   ? 282 TYR   B CD2 1 
ATOM   4731  C  CE1 . TYR   B 1 260 ? 21.155 47.269  28.115 1   56.57  ? 282 TYR   B CE1 1 
ATOM   4732  C  CE2 . TYR   B 1 260 ? 23.063 46.584  26.856 1   56.35  ? 282 TYR   B CE2 1 
ATOM   4733  C  CZ  . TYR   B 1 260 ? 21.695 46.679  26.991 1   57.21  ? 282 TYR   B CZ  1 
ATOM   4734  O  OH  . TYR   B 1 260 ? 20.869 46.163  26.027 1   58.73  ? 282 TYR   B OH  1 
ATOM   4735  N  N   . ARG   B 1 261 ? 25.883 51.448  30.988 1   54.93  ? 283 ARG   B N   1 
ATOM   4736  C  CA  . ARG   B 1 261 ? 26.829 52.058  31.933 1   55.63  ? 283 ARG   B CA  1 
ATOM   4737  C  C   . ARG   B 1 261 ? 26.244 52.309  33.315 1   56.55  ? 283 ARG   B C   1 
ATOM   4738  O  O   . ARG   B 1 261 ? 26.991 52.377  34.29  1   57.05  ? 283 ARG   B O   1 
ATOM   4739  C  CB  . ARG   B 1 261 ? 27.406 53.365  31.363 1   56.71  ? 283 ARG   B CB  1 
ATOM   4740  C  CG  . ARG   B 1 261 ? 26.332 54.386  31.002 1   59.57  ? 283 ARG   B CG  1 
ATOM   4741  C  CD  . ARG   B 1 261 ? 26.924 55.719  30.593 1   62.24  ? 283 ARG   B CD  1 
ATOM   4742  N  NE  . ARG   B 1 261 ? 27.51  56.423  31.734 1   64.42  ? 283 ARG   B NE  1 
ATOM   4743  C  CZ  . ARG   B 1 261 ? 28.143 57.59   31.653 1   66.74  ? 283 ARG   B CZ  1 
ATOM   4744  N  NH1 . ARG   B 1 261 ? 28.296 58.191  30.478 1   66.08  ? 283 ARG   B NH1 1 
ATOM   4745  N  NH2 . ARG   B 1 261 ? 28.642 58.159  32.744 1   67.16  ? 283 ARG   B NH2 1 
ATOM   4746  N  N   . ASP   B 1 262 ? 24.919 52.469  33.41  1   56.78  ? 284 ASP   B N   1 
ATOM   4747  C  CA  . ASP   B 1 262 ? 24.267 52.687  34.703 1   57.24  ? 284 ASP   B CA  1 
ATOM   4748  C  C   . ASP   B 1 262 ? 24.065 51.373  35.487 1   57.72  ? 284 ASP   B C   1 
ATOM   4749  O  O   . ASP   B 1 262 ? 23.751 51.425  36.675 1   58.12  ? 284 ASP   B O   1 
ATOM   4750  C  CB  . ASP   B 1 262 ? 22.951 53.487  34.549 1   58.66  ? 284 ASP   B CB  1 
ATOM   4751  C  CG  . ASP   B 1 262 ? 23.143 54.983  34.308 1   62.68  ? 284 ASP   B CG  1 
ATOM   4752  O  OD1 . ASP   B 1 262 ? 24.203 55.527  34.725 1   62.35  ? 284 ASP   B OD1 1 
ATOM   4753  O  OD2 . ASP   B 1 262 ? 22.228 55.617  33.714 1   65.25  ? 284 ASP   B OD2 1 
ATOM   4754  N  N   . GLU   B 1 263 ? 24.267 50.198  34.834 1   57.71  ? 285 GLU   B N   1 
ATOM   4755  C  CA  . GLU   B 1 263 ? 24.165 48.884  35.468 1   57.94  ? 285 GLU   B CA  1 
ATOM   4756  C  C   . GLU   B 1 263 ? 25.483 48.523  36.133 1   57.55  ? 285 GLU   B C   1 
ATOM   4757  O  O   . GLU   B 1 263 ? 26.537 48.694  35.528 1   57.55  ? 285 GLU   B O   1 
ATOM   4758  C  CB  . GLU   B 1 263 ? 23.796 47.802  34.446 1   60.45  ? 285 GLU   B CB  1 
ATOM   4759  C  CG  . GLU   B 1 263 ? 22.478 48.069  33.747 1   66.53  ? 285 GLU   B CG  1 
ATOM   4760  C  CD  . GLU   B 1 263 ? 21.292 48.169  34.686 1   74.04  ? 285 GLU   B CD  1 
ATOM   4761  O  OE1 . GLU   B 1 263 ? 21.211 47.366  35.647 1   74.91  ? 285 GLU   B OE1 1 
ATOM   4762  O  OE2 . GLU   B 1 263 ? 20.441 49.059  34.459 1   77.07  ? 285 GLU   B OE2 1 
ATOM   4763  N  N   . PRO   B 1 264 ? 25.433 47.999  37.376 1   56.87  ? 286 PRO   B N   1 
ATOM   4764  C  CA  . PRO   B 1 264 ? 26.676 47.621  38.085 1   56.4   ? 286 PRO   B CA  1 
ATOM   4765  C  C   . PRO   B 1 264 ? 27.679 46.775  37.293 1   56.53  ? 286 PRO   B C   1 
ATOM   4766  O  O   . PRO   B 1 264 ? 28.888 46.983  37.415 1   57.03  ? 286 PRO   B O   1 
ATOM   4767  C  CB  . PRO   B 1 264 ? 26.155 46.875  39.31  1   56.71  ? 286 PRO   B CB  1 
ATOM   4768  C  CG  . PRO   B 1 264 ? 24.807 47.451  39.54  1   57.03  ? 286 PRO   B CG  1 
ATOM   4769  C  CD  . PRO   B 1 264 ? 24.236 47.763  38.209 1   55.72  ? 286 PRO   B CD  1 
ATOM   4770  N  N   . ARG   B 1 265 ? 27.18  45.852  36.461 1   55.97  ? 287 ARG   B N   1 
ATOM   4771  C  CA  . ARG   B 1 265 ? 27.99  44.978  35.621 1   56.3   ? 287 ARG   B CA  1 
ATOM   4772  C  C   . ARG   B 1 265 ? 28.857 45.76   34.651 1   55.42  ? 287 ARG   B C   1 
ATOM   4773  O  O   . ARG   B 1 265 ? 29.987 45.354  34.375 1   55.54  ? 287 ARG   B O   1 
ATOM   4774  C  CB  . ARG   B 1 265 ? 27.072 44.065  34.801 1   59.49  ? 287 ARG   B CB  1 
ATOM   4775  C  CG  . ARG   B 1 265 ? 27.003 42.637  35.302 1   66.08  ? 287 ARG   B CG  1 
ATOM   4776  C  CD  . ARG   B 1 265 ? 25.838 41.859  34.69  1   71.89  ? 287 ARG   B CD  1 
ATOM   4777  N  NE  . ARG   B 1 265 ? 25.777 41.935  33.225 1   76.14  ? 287 ARG   B NE  1 
ATOM   4778  C  CZ  . ARG   B 1 265 ? 26.512 41.194  32.4   1   79.47  ? 287 ARG   B CZ  1 
ATOM   4779  N  NH1 . ARG   B 1 265 ? 27.394 40.324  32.884 1   79.19  ? 287 ARG   B NH1 1 
ATOM   4780  N  NH2 . ARG   B 1 265 ? 26.375 41.32   31.085 1   79.87  ? 287 ARG   B NH2 1 
ATOM   4781  N  N   . PHE   B 1 266 ? 28.325 46.869  34.119 1   54.34  ? 288 PHE   B N   1 
ATOM   4782  C  CA  . PHE   B 1 266 ? 29.019 47.67   33.126 1   53.8   ? 288 PHE   B CA  1 
ATOM   4783  C  C   . PHE   B 1 266 ? 29.528 49.013  33.618 1   52.79  ? 288 PHE   B C   1 
ATOM   4784  O  O   . PHE   B 1 266 ? 30.127 49.732  32.821 1   52.74  ? 288 PHE   B O   1 
ATOM   4785  C  CB  . PHE   B 1 266 ? 28.121 47.889  31.901 1   53.88  ? 288 PHE   B CB  1 
ATOM   4786  C  CG  . PHE   B 1 266 ? 27.705 46.634  31.171 1   54.82  ? 288 PHE   B CG  1 
ATOM   4787  C  CD1 . PHE   B 1 266 ? 26.535 45.977  31.503 1   55.66  ? 288 PHE   B CD1 1 
ATOM   4788  C  CD2 . PHE   B 1 266 ? 28.474 46.127  30.136 1   55.8   ? 288 PHE   B CD2 1 
ATOM   4789  C  CE1 . PHE   B 1 266 ? 26.144 44.836  30.814 1   56.49  ? 288 PHE   B CE1 1 
ATOM   4790  C  CE2 . PHE   B 1 266 ? 28.079 44.985  29.446 1   56.53  ? 288 PHE   B CE2 1 
ATOM   4791  C  CZ  . PHE   B 1 266 ? 26.924 44.343  29.795 1   56.35  ? 288 PHE   B CZ  1 
ATOM   4792  N  N   . SER   B 1 267 ? 29.313 49.365  34.905 1   51.75  ? 289 SER   B N   1 
ATOM   4793  C  CA  . SER   B 1 267 ? 29.752 50.665  35.421 1   50.94  ? 289 SER   B CA  1 
ATOM   4794  C  C   . SER   B 1 267 ? 31.275 50.811  35.468 1   49.42  ? 289 SER   B C   1 
ATOM   4795  O  O   . SER   B 1 267 ? 31.81  51.867  35.107 1   49.1   ? 289 SER   B O   1 
ATOM   4796  C  CB  . SER   B 1 267 ? 29.14  50.941  36.788 1   52.84  ? 289 SER   B CB  1 
ATOM   4797  O  OG  . SER   B 1 267 ? 29.805 50.213  37.809 1   56.27  ? 289 SER   B OG  1 
ATOM   4798  N  N   . GLN   B 1 268 ? 31.969 49.759  35.916 1   48.24  ? 290 GLN   B N   1 
ATOM   4799  C  CA  . GLN   B 1 268 ? 33.427 49.794  35.981 1   47.64  ? 290 GLN   B CA  1 
ATOM   4800  C  C   . GLN   B 1 268 ? 34.065 49.653  34.587 1   46.45  ? 290 GLN   B C   1 
ATOM   4801  O  O   . GLN   B 1 268 ? 34.909 50.491  34.26  1   46.37  ? 290 GLN   B O   1 
ATOM   4802  C  CB  . GLN   B 1 268 ? 33.975 48.803  37.015 1   49.21  ? 290 GLN   B CB  1 
ATOM   4803  C  CG  . GLN   B 1 268 ? 34.936 49.435  38.034 1   52.78  ? 290 GLN   B CG  1 
ATOM   4804  C  CD  . GLN   B 1 268 ? 34.508 50.757  38.656 1   57.25  ? 290 GLN   B CD  1 
ATOM   4805  O  OE1 . GLN   B 1 268 ? 33.328 51.011  38.941 1   59.96  ? 290 GLN   B OE1 1 
ATOM   4806  N  NE2 . GLN   B 1 268 ? 35.473 51.627  38.9   1   57.01  ? 290 GLN   B NE2 1 
ATOM   4807  N  N   . PRO   B 1 269 ? 33.611 48.739  33.688 1   45.39  ? 291 PRO   B N   1 
ATOM   4808  C  CA  . PRO   B 1 269 ? 34.148 48.742  32.312 1   44.52  ? 291 PRO   B CA  1 
ATOM   4809  C  C   . PRO   B 1 269 ? 33.981 50.099  31.617 1   43.68  ? 291 PRO   B C   1 
ATOM   4810  O  O   . PRO   B 1 269 ? 34.881 50.516  30.913 1   44.06  ? 291 PRO   B O   1 
ATOM   4811  C  CB  . PRO   B 1 269 ? 33.315 47.665  31.604 1   45.34  ? 291 PRO   B CB  1 
ATOM   4812  C  CG  . PRO   B 1 269 ? 32.868 46.767  32.685 1   46.03  ? 291 PRO   B CG  1 
ATOM   4813  C  CD  . PRO   B 1 269 ? 32.614 47.664  33.864 1   44.63  ? 291 PRO   B CD  1 
ATOM   4814  N  N   . HIS   B 1 270 ? 32.863 50.807  31.846 1   43     ? 292 HIS   B N   1 
ATOM   4815  C  CA  . HIS   B 1 270 ? 32.629 52.126  31.261 1   42.96  ? 292 HIS   B CA  1 
ATOM   4816  C  C   . HIS   B 1 270 ? 33.589 53.164  31.811 1   42.77  ? 292 HIS   B C   1 
ATOM   4817  O  O   . HIS   B 1 270 ? 34.073 54.015  31.066 1   42.86  ? 292 HIS   B O   1 
ATOM   4818  C  CB  . HIS   B 1 270 ? 31.191 52.602  31.475 1   43.93  ? 292 HIS   B CB  1 
ATOM   4819  C  CG  . HIS   B 1 270 ? 30.926 53.892  30.771 1   47.37  ? 292 HIS   B CG  1 
ATOM   4820  N  ND1 . HIS   B 1 270 ? 30.787 53.949  29.386 1   49.21  ? 292 HIS   B ND1 1 
ATOM   4821  C  CD2 . HIS   B 1 270 ? 30.877 55.151  31.265 1   48.92  ? 292 HIS   B CD2 1 
ATOM   4822  C  CE1 . HIS   B 1 270 ? 30.615 55.229  29.093 1   49.74  ? 292 HIS   B CE1 1 
ATOM   4823  N  NE2 . HIS   B 1 270 ? 30.661 55.993  30.187 1   50.06  ? 292 HIS   B NE2 1 
ATOM   4824  N  N   . GLN   B 1 271 ? 33.869 53.094  33.113 1   42.22  ? 293 GLN   B N   1 
ATOM   4825  C  CA  . GLN   B 1 271 ? 34.814 53.99   33.752 1   42.29  ? 293 GLN   B CA  1 
ATOM   4826  C  C   . GLN   B 1 271 ? 36.222 53.82   33.137 1   41.66  ? 293 GLN   B C   1 
ATOM   4827  O  O   . GLN   B 1 271 ? 36.909 54.811  32.912 1   41.86  ? 293 GLN   B O   1 
ATOM   4828  C  CB  . GLN   B 1 271 ? 34.796 53.769  35.271 1   44.47  ? 293 GLN   B CB  1 
ATOM   4829  C  CG  . GLN   B 1 271 ? 35.581 54.801  36.083 1   49.31  ? 293 GLN   B CG  1 
ATOM   4830  C  CD  . GLN   B 1 271 ? 35.198 56.238  35.79  1   55.59  ? 293 GLN   B CD  1 
ATOM   4831  O  OE1 . GLN   B 1 271 ? 34.035 56.565  35.506 1   59.09  ? 293 GLN   B OE1 1 
ATOM   4832  N  NE2 . GLN   B 1 271 ? 36.172 57.136  35.862 1   55.18  ? 293 GLN   B NE2 1 
ATOM   4833  N  N   . LEU   B 1 272 ? 36.595 52.585  32.772 1   41.02  ? 294 LEU   B N   1 
ATOM   4834  C  CA  . LEU   B 1 272 ? 37.858 52.239  32.111 1   40.79  ? 294 LEU   B CA  1 
ATOM   4835  C  C   . LEU   B 1 272 ? 37.931 52.929  30.736 1   41.33  ? 294 LEU   B C   1 
ATOM   4836  O  O   . LEU   B 1 272 ? 38.965 53.512  30.403 1   41.92  ? 294 LEU   B O   1 
ATOM   4837  C  CB  . LEU   B 1 272 ? 37.932 50.709  31.945 1   40.35  ? 294 LEU   B CB  1 
ATOM   4838  C  CG  . LEU   B 1 272 ? 39.286 50.084  31.656 1   40.54  ? 294 LEU   B CG  1 
ATOM   4839  C  CD1 . LEU   B 1 272 ? 39.363 48.686  32.264 1   40.46  ? 294 LEU   B CD1 1 
ATOM   4840  C  CD2 . LEU   B 1 272 ? 39.574 50.035  30.141 1   40.51  ? 294 LEU   B CD2 1 
ATOM   4841  N  N   . LEU   B 1 273 ? 36.838 52.874  29.947 1   40.58  ? 295 LEU   B N   1 
ATOM   4842  C  CA  . LEU   B 1 273 ? 36.79  53.523  28.643 1   40.73  ? 295 LEU   B CA  1 
ATOM   4843  C  C   . LEU   B 1 273 ? 36.886 55.039  28.776 1   41.14  ? 295 LEU   B C   1 
ATOM   4844  O  O   . LEU   B 1 273 ? 37.553 55.701  27.974 1   41.6   ? 295 LEU   B O   1 
ATOM   4845  C  CB  . LEU   B 1 273 ? 35.485 53.159  27.908 1   40.58  ? 295 LEU   B CB  1 
ATOM   4846  C  CG  . LEU   B 1 273 ? 35.294 51.699  27.522 1   41.22  ? 295 LEU   B CG  1 
ATOM   4847  C  CD1 . LEU   B 1 273 ? 33.991 51.521  26.764 1   41.71  ? 295 LEU   B CD1 1 
ATOM   4848  C  CD2 . LEU   B 1 273 ? 36.471 51.177  26.705 1   41.11  ? 295 LEU   B CD2 1 
ATOM   4849  N  N   . THR   B 1 274 ? 36.193 55.582  29.785 1   40.58  ? 296 THR   B N   1 
ATOM   4850  C  CA  . THR   B 1 274 ? 36.158 56.999  30.091 1   40.04  ? 296 THR   B CA  1 
ATOM   4851  C  C   . THR   B 1 274 ? 37.549 57.489  30.443 1   39.62  ? 296 THR   B C   1 
ATOM   4852  O  O   . THR   B 1 274 ? 37.956 58.535  29.961 1   39.88  ? 296 THR   B O   1 
ATOM   4853  C  CB  . THR   B 1 274 ? 35.133 57.232  31.199 1   41.3   ? 296 THR   B CB  1 
ATOM   4854  O  OG1 . THR   B 1 274 ? 33.836 56.974  30.667 1   42.84  ? 296 THR   B OG1 1 
ATOM   4855  C  CG2 . THR   B 1 274 ? 35.173 58.639  31.743 1   41.73  ? 296 THR   B CG2 1 
ATOM   4856  N  N   . LEU   B 1 275 ? 38.296 56.727  31.248 1   39.16  ? 297 LEU   B N   1 
ATOM   4857  C  CA  . LEU   B 1 275 ? 39.646 57.13   31.643 1   39.4   ? 297 LEU   B CA  1 
ATOM   4858  C  C   . LEU   B 1 275 ? 40.623 57.078  30.468 1   40.37  ? 297 LEU   B C   1 
ATOM   4859  O  O   . LEU   B 1 275 ? 41.509 57.923  30.375 1   41.15  ? 297 LEU   B O   1 
ATOM   4860  C  CB  . LEU   B 1 275 ? 40.147 56.307  32.825 1   38.73  ? 297 LEU   B CB  1 
ATOM   4861  C  CG  . LEU   B 1 275 ? 39.422 56.563  34.126 1   38.6   ? 297 LEU   B CG  1 
ATOM   4862  C  CD1 . LEU   B 1 275 ? 39.691 55.469  35.117 1   38.48  ? 297 LEU   B CD1 1 
ATOM   4863  C  CD2 . LEU   B 1 275 ? 39.777 57.927  34.677 1   39.12  ? 297 LEU   B CD2 1 
ATOM   4864  N  N   . LEU   B 1 276 ? 40.423 56.147  29.537 1   40.01  ? 298 LEU   B N   1 
ATOM   4865  C  CA  . LEU   B 1 276 ? 41.245 56.068  28.33  1   40.06  ? 298 LEU   B CA  1 
ATOM   4866  C  C   . LEU   B 1 276 ? 41.037 57.331  27.453 1   40.25  ? 298 LEU   B C   1 
ATOM   4867  O  O   . LEU   B 1 276 ? 41.981 57.841  26.843 1   40.28  ? 298 LEU   B O   1 
ATOM   4868  C  CB  . LEU   B 1 276 ? 40.877 54.81   27.532 1   39.46  ? 298 LEU   B CB  1 
ATOM   4869  C  CG  . LEU   B 1 276 ? 41.274 53.494  28.147 1   39.72  ? 298 LEU   B CG  1 
ATOM   4870  C  CD1 . LEU   B 1 276 ? 40.708 52.346  27.347 1   39.77  ? 298 LEU   B CD1 1 
ATOM   4871  C  CD2 . LEU   B 1 276 ? 42.766 53.383  28.262 1   40.16  ? 298 LEU   B CD2 1 
ATOM   4872  N  N   . MET   B 1 277 ? 39.797 57.811  27.381 1   39.94  ? 299 MET   B N   1 
ATOM   4873  C  CA  . MET   B 1 277 ? 39.479 59.012  26.63  1   40.49  ? 299 MET   B CA  1 
ATOM   4874  C  C   . MET   B 1 277 ? 40.048 60.252  27.326 1   41.23  ? 299 MET   B C   1 
ATOM   4875  O  O   . MET   B 1 277 ? 40.456 61.203  26.662 1   41.13  ? 299 MET   B O   1 
ATOM   4876  C  CB  . MET   B 1 277 ? 37.972 59.159  26.514 1   40.98  ? 299 MET   B CB  1 
ATOM   4877  C  CG  . MET   B 1 277 ? 37.378 58.369  25.407 1   42.77  ? 299 MET   B CG  1 
ATOM   4878  S  SD  . MET   B 1 277 ? 35.573 58.333  25.533 1   44.63  ? 299 MET   B SD  1 
ATOM   4879  C  CE  . MET   B 1 277 ? 35.207 59.991  25.304 1   44.88  ? 299 MET   B CE  1 
ATOM   4880  N  N   . ASP   B 1 278 ? 40.034 60.255  28.664 1   41.71  ? 300 ASP   B N   1 
ATOM   4881  C  CA  . ASP   B 1 278 ? 40.563 61.345  29.464 1   42.22  ? 300 ASP   B CA  1 
ATOM   4882  C  C   . ASP   B 1 278 ? 42.073 61.448  29.261 1   42.58  ? 300 ASP   B C   1 
ATOM   4883  O  O   . ASP   B 1 278 ? 42.569 62.556  29.103 1   43.31  ? 300 ASP   B O   1 
ATOM   4884  C  CB  . ASP   B 1 278 ? 40.177 61.162  30.947 1   43.4   ? 300 ASP   B CB  1 
ATOM   4885  C  CG  . ASP   B 1 278 ? 38.694 61.403  31.238 1   46.64  ? 300 ASP   B CG  1 
ATOM   4886  O  OD1 . ASP   B 1 278 ? 37.941 61.693  30.297 1   46.37  ? 300 ASP   B OD1 1 
ATOM   4887  O  OD2 . ASP   B 1 278 ? 38.295 61.298  32.404 1   49.4   ? 300 ASP   B OD2 1 
ATOM   4888  N  N   . ILE   B 1 279 ? 42.785 60.303  29.191 1   41.93  ? 301 ILE   B N   1 
ATOM   4889  C  CA  . ILE   B 1 279 ? 44.237 60.237  28.952 1   41.79  ? 301 ILE   B CA  1 
ATOM   4890  C  C   . ILE   B 1 279 ? 44.566 60.803  27.586 1   41.73  ? 301 ILE   B C   1 
ATOM   4891  O  O   . ILE   B 1 279 ? 45.505 61.587  27.448 1   42.2   ? 301 ILE   B O   1 
ATOM   4892  C  CB  . ILE   B 1 279 ? 44.771 58.778  29.117 1   42.01  ? 301 ILE   B CB  1 
ATOM   4893  C  CG1 . ILE   B 1 279 ? 44.851 58.374  30.603 1   42.01  ? 301 ILE   B CG1 1 
ATOM   4894  C  CG2 . ILE   B 1 279 ? 46.125 58.554  28.414 1   42.36  ? 301 ILE   B CG2 1 
ATOM   4895  C  CD1 . ILE   B 1 279 ? 44.817 56.897  30.835 1   42.8   ? 301 ILE   B CD1 1 
ATOM   4896  N  N   . ASP   B 1 280 ? 43.778 60.412  26.585 1   41.21  ? 302 ASP   B N   1 
ATOM   4897  C  CA  . ASP   B 1 280 ? 43.887 60.854  25.209 1   41.13  ? 302 ASP   B CA  1 
ATOM   4898  C  C   . ASP   B 1 280 ? 43.692 62.369  25.114 1   40.49  ? 302 ASP   B C   1 
ATOM   4899  O  O   . ASP   B 1 280 ? 44.478 63.053  24.461 1   40.45  ? 302 ASP   B O   1 
ATOM   4900  C  CB  . ASP   B 1 280 ? 42.819 60.134  24.383 1   44.31  ? 302 ASP   B CB  1 
ATOM   4901  C  CG  . ASP   B 1 280 ? 43.281 59.625  23.036 1   52.05  ? 302 ASP   B CG  1 
ATOM   4902  O  OD1 . ASP   B 1 280 ? 44.487 59.779  22.716 1   53.03  ? 302 ASP   B OD1 1 
ATOM   4903  O  OD2 . ASP   B 1 280 ? 42.445 59.064  22.299 1   55.74  ? 302 ASP   B OD2 1 
ATOM   4904  N  N   . SER   B 1 281 ? 42.654 62.889  25.78  1   40.22  ? 303 SER   B N   1 
ATOM   4905  C  CA  . SER   B 1 281 ? 42.342 64.307  25.805 1   40.79  ? 303 SER   B CA  1 
ATOM   4906  C  C   . SER   B 1 281 ? 43.44  65.118  26.514 1   40.48  ? 303 SER   B C   1 
ATOM   4907  O  O   . SER   B 1 281 ? 43.803 66.195  26.04  1   40.83  ? 303 SER   B O   1 
ATOM   4908  C  CB  . SER   B 1 281 ? 41.002 64.536  26.488 1   43.28  ? 303 SER   B CB  1 
ATOM   4909  O  OG  . SER   B 1 281 ? 40.121 65.229  25.618 1   47.55  ? 303 SER   B OG  1 
ATOM   4910  N  N   . LEU   B 1 282 ? 43.992 64.579  27.619 1   39.38  ? 304 LEU   B N   1 
ATOM   4911  C  CA  . LEU   B 1 282 ? 45.056 65.223  28.379 1   39     ? 304 LEU   B CA  1 
ATOM   4912  C  C   . LEU   B 1 282 ? 46.378 65.234  27.638 1   39.21  ? 304 LEU   B C   1 
ATOM   4913  O  O   . LEU   B 1 282 ? 47.146 66.185  27.799 1   39.67  ? 304 LEU   B O   1 
ATOM   4914  C  CB  . LEU   B 1 282 ? 45.216 64.596  29.763 1   38.7   ? 304 LEU   B CB  1 
ATOM   4915  C  CG  . LEU   B 1 282 ? 44.172 65.025  30.756 1   38.97  ? 304 LEU   B CG  1 
ATOM   4916  C  CD1 . LEU   B 1 282 ? 44.06  64.05   31.871 1   38.95  ? 304 LEU   B CD1 1 
ATOM   4917  C  CD2 . LEU   B 1 282 ? 44.449 66.407  31.256 1   39.58  ? 304 LEU   B CD2 1 
ATOM   4918  N  N   . ILE   B 1 283 ? 46.647 64.209  26.809 1   38.82  ? 305 ILE   B N   1 
ATOM   4919  C  CA  . ILE   B 1 283 ? 47.859 64.206  25.983 1   38.96  ? 305 ILE   B CA  1 
ATOM   4920  C  C   . ILE   B 1 283 ? 47.75  65.297  24.892 1   39.76  ? 305 ILE   B C   1 
ATOM   4921  O  O   . ILE   B 1 283 ? 48.72  66      24.643 1   40.75  ? 305 ILE   B O   1 
ATOM   4922  C  CB  . ILE   B 1 283 ? 48.187 62.793  25.449 1   38.7   ? 305 ILE   B CB  1 
ATOM   4923  C  CG1 . ILE   B 1 283 ? 48.703 61.914  26.593 1   38.77  ? 305 ILE   B CG1 1 
ATOM   4924  C  CG2 . ILE   B 1 283 ? 49.188 62.837  24.293 1   38.67  ? 305 ILE   B CG2 1 
ATOM   4925  C  CD1 . ILE   B 1 283 ? 48.826 60.496  26.248 1   39.91  ? 305 ILE   B CD1 1 
ATOM   4926  N  N   . THR   B 1 284 ? 46.547 65.539  24.36  1   39.67  ? 306 THR   B N   1 
ATOM   4927  C  CA  . THR   B 1 284 ? 46.305 66.617  23.404 1   40.34  ? 306 THR   B CA  1 
ATOM   4928  C  C   . THR   B 1 284 ? 46.361 67.993  24.084 1   40.63  ? 306 THR   B C   1 
ATOM   4929  O  O   . THR   B 1 284 ? 46.904 68.935  23.515 1   41.17  ? 306 THR   B O   1 
ATOM   4930  C  CB  . THR   B 1 284 ? 45.009 66.366  22.659 1   42.16  ? 306 THR   B CB  1 
ATOM   4931  O  OG1 . THR   B 1 284 ? 45.151 65.13   21.963 1   43.88  ? 306 THR   B OG1 1 
ATOM   4932  C  CG2 . THR   B 1 284 ? 44.699 67.453  21.673 1   42.52  ? 306 THR   B CG2 1 
ATOM   4933  N  N   . LYS   B 1 285 ? 45.87  68.101  25.321 1   40.16  ? 307 LYS   B N   1 
ATOM   4934  C  CA  . LYS   B 1 285 ? 45.959 69.346  26.09  1   40.08  ? 307 LYS   B CA  1 
ATOM   4935  C  C   . LYS   B 1 285 ? 47.419 69.695  26.399 1   40.46  ? 307 LYS   B C   1 
ATOM   4936  O  O   . LYS   B 1 285 ? 47.759 70.876  26.453 1   39.96  ? 307 LYS   B O   1 
ATOM   4937  C  CB  . LYS   B 1 285 ? 45.133 69.258  27.382 1   40.96  ? 307 LYS   B CB  1 
ATOM   4938  C  CG  . LYS   B 1 285 ? 43.639 69.156  27.113 1   43.15  ? 307 LYS   B CG  1 
ATOM   4939  C  CD  . LYS   B 1 285 ? 42.805 69.209  28.367 1   45.55  ? 307 LYS   B CD  1 
ATOM   4940  C  CE  . LYS   B 1 285 ? 41.349 69.166  27.984 1   48.97  ? 307 LYS   B CE  1 
ATOM   4941  N  NZ  . LYS   B 1 285 ? 40.456 69.043  29.164 1   51.28  ? 307 LYS   B NZ  1 
ATOM   4942  N  N   . TRP   B 1 286 ? 48.293 68.675  26.581 1   41.24  ? 308 TRP   B N   1 
ATOM   4943  C  CA  . TRP   B 1 286 ? 49.711 68.945  26.797 1   42.2   ? 308 TRP   B CA  1 
ATOM   4944  C  C   . TRP   B 1 286 ? 50.308 69.42   25.479 1   43     ? 308 TRP   B C   1 
ATOM   4945  O  O   . TRP   B 1 286 ? 51.055 70.381  25.469 1   43.36  ? 308 TRP   B O   1 
ATOM   4946  C  CB  . TRP   B 1 286 ? 50.488 67.725  27.327 1   42.37  ? 308 TRP   B CB  1 
ATOM   4947  C  CG  . TRP   B 1 286 ? 51.961 68.009  27.412 1   43.24  ? 308 TRP   B CG  1 
ATOM   4948  C  CD1 . TRP   B 1 286 ? 52.598 68.716  28.385 1   44.14  ? 308 TRP   B CD1 1 
ATOM   4949  C  CD2 . TRP   B 1 286 ? 52.934 67.786  26.38  1   43.5   ? 308 TRP   B CD2 1 
ATOM   4950  N  NE1 . TRP   B 1 286 ? 53.92  68.89   28.057 1   44.44  ? 308 TRP   B NE1 1 
ATOM   4951  C  CE2 . TRP   B 1 286 ? 54.151 68.336  26.826 1   44.18  ? 308 TRP   B CE2 1 
ATOM   4952  C  CE3 . TRP   B 1 286 ? 52.898 67.151  25.128 1   44.18  ? 308 TRP   B CE3 1 
ATOM   4953  C  CZ2 . TRP   B 1 286 ? 55.321 68.262  26.075 1   44.91  ? 308 TRP   B CZ2 1 
ATOM   4954  C  CZ3 . TRP   B 1 286 ? 54.054 67.099  24.374 1   45.01  ? 308 TRP   B CZ3 1 
ATOM   4955  C  CH2 . TRP   B 1 286 ? 55.251 67.638  24.854 1   45.15  ? 308 TRP   B CH2 1 
ATOM   4956  N  N   . ARG   B 1 287 ? 49.989 68.745  24.366 1   43.08  ? 309 ARG   B N   1 
ATOM   4957  C  CA  . ARG   B 1 287 ? 50.507 69.1    23.049 1   43.32  ? 309 ARG   B CA  1 
ATOM   4958  C  C   . ARG   B 1 287 ? 50.157 70.536  22.678 1   44.61  ? 309 ARG   B C   1 
ATOM   4959  O  O   . ARG   B 1 287 ? 50.972 71.229  22.066 1   45.33  ? 309 ARG   B O   1 
ATOM   4960  C  CB  . ARG   B 1 287 ? 49.935 68.159  21.989 1   43.04  ? 309 ARG   B CB  1 
ATOM   4961  C  CG  . ARG   B 1 287 ? 50.471 66.75   22.012 1   42.77  ? 309 ARG   B CG  1 
ATOM   4962  C  CD  . ARG   B 1 287 ? 49.988 66.05   20.767 1   42.96  ? 309 ARG   B CD  1 
ATOM   4963  N  NE  . ARG   B 1 287 ? 49.827 64.61   20.939 1   43.66  ? 309 ARG   B NE  1 
ATOM   4964  C  CZ  . ARG   B 1 287 ? 50.801 63.721  20.798 1   45.61  ? 309 ARG   B CZ  1 
ATOM   4965  N  NH1 . ARG   B 1 287 ? 50.552 62.426  20.955 1   44.94  ? 309 ARG   B NH1 1 
ATOM   4966  N  NH2 . ARG   B 1 287 ? 52.037 64.118  20.502 1   46.08  ? 309 ARG   B NH2 1 
ATOM   4967  N  N   . TYR   B 1 288 ? 48.947 70.974  23.036 1   44.8   ? 310 TYR   B N   1 
ATOM   4968  C  CA  . TYR   B 1 288 ? 48.486 72.316  22.737 1   45.74  ? 310 TYR   B CA  1 
ATOM   4969  C  C   . TYR   B 1 288 ? 49.225 73.318  23.602 1   45.5   ? 310 TYR   B C   1 
ATOM   4970  O  O   . TYR   B 1 288 ? 49.712 74.323  23.096 1   45.72  ? 310 TYR   B O   1 
ATOM   4971  C  CB  . TYR   B 1 288 ? 46.957 72.426  22.915 1   46.76  ? 310 TYR   B CB  1 
ATOM   4972  C  CG  . TYR   B 1 288 ? 46.425 73.834  22.735 1   48.94  ? 310 TYR   B CG  1 
ATOM   4973  C  CD1 . TYR   B 1 288 ? 46.222 74.366  21.468 1   50.21  ? 310 TYR   B CD1 1 
ATOM   4974  C  CD2 . TYR   B 1 288 ? 46.135 74.637  23.834 1   50.58  ? 310 TYR   B CD2 1 
ATOM   4975  C  CE1 . TYR   B 1 288 ? 45.743 75.66   21.296 1   51.73  ? 310 TYR   B CE1 1 
ATOM   4976  C  CE2 . TYR   B 1 288 ? 45.66  75.935  23.677 1   51.86  ? 310 TYR   B CE2 1 
ATOM   4977  C  CZ  . TYR   B 1 288 ? 45.459 76.443  22.405 1   53.25  ? 310 TYR   B CZ  1 
ATOM   4978  O  OH  . TYR   B 1 288 ? 44.994 77.735  22.253 1   55.33  ? 310 TYR   B OH  1 
ATOM   4979  N  N   . ASN   B 1 289 ? 49.333 73.044  24.897 1   45.15  ? 311 ASN   B N   1 
ATOM   4980  C  CA  . ASN   B 1 289 ? 50.022 73.933  25.827 1   44.92  ? 311 ASN   B CA  1 
ATOM   4981  C  C   . ASN   B 1 289 ? 51.482 74.089  25.477 1   44.5   ? 311 ASN   B C   1 
ATOM   4982  O  O   . ASN   B 1 289 ? 52.024 75.187  25.576 1   44.54  ? 311 ASN   B O   1 
ATOM   4983  C  CB  . ASN   B 1 289 ? 49.868 73.425  27.249 1   46.31  ? 311 ASN   B CB  1 
ATOM   4984  C  CG  . ASN   B 1 289 ? 48.672 73.97   27.973 1   50.37  ? 311 ASN   B CG  1 
ATOM   4985  O  OD1 . ASN   B 1 289 ? 48.713 74.153  29.19  1   53.07  ? 311 ASN   B OD1 1 
ATOM   4986  N  ND2 . ASN   B 1 289 ? 47.578 74.227  27.266 1   50.33  ? 311 ASN   B ND2 1 
ATOM   4987  N  N   . HIS   B 1 290 ? 52.117 72.988  25.066 1   44.46  ? 312 HIS   B N   1 
ATOM   4988  C  CA  . HIS   B 1 290 ? 53.508 72.93   24.635 1   44.61  ? 312 HIS   B CA  1 
ATOM   4989  C  C   . HIS   B 1 290 ? 53.702 73.768  23.364 1   44.43  ? 312 HIS   B C   1 
ATOM   4990  O  O   . HIS   B 1 290 ? 54.613 74.595  23.333 1   44.6   ? 312 HIS   B O   1 
ATOM   4991  C  CB  . HIS   B 1 290 ? 53.923 71.47   24.395 1   45.1   ? 312 HIS   B CB  1 
ATOM   4992  C  CG  . HIS   B 1 290 ? 55.295 71.303  23.828 1   47.3   ? 312 HIS   B CG  1 
ATOM   4993  N  ND1 . HIS   B 1 290 ? 55.492 70.786  22.56  1   49.18  ? 312 HIS   B ND1 1 
ATOM   4994  C  CD2 . HIS   B 1 290 ? 56.497 71.591  24.372 1   48.46  ? 312 HIS   B CD2 1 
ATOM   4995  C  CE1 . HIS   B 1 290 ? 56.803 70.777  22.371 1   49.56  ? 312 HIS   B CE1 1 
ATOM   4996  N  NE2 . HIS   B 1 290 ? 57.45  71.252  23.432 1   49.72  ? 312 HIS   B NE2 1 
ATOM   4997  N  N   . VAL   B 1 291 ? 52.819 73.601  22.353 1   43.91  ? 313 VAL   B N   1 
ATOM   4998  C  CA  . VAL   B 1 291 ? 52.91  74.343  21.091 1   44.38  ? 313 VAL   B CA  1 
ATOM   4999  C  C   . VAL   B 1 291 ? 52.713 75.875  21.299 1   44.47  ? 313 VAL   B C   1 
ATOM   5000  O  O   . VAL   B 1 291 ? 53.38  76.662  20.63  1   44.8   ? 313 VAL   B O   1 
ATOM   5001  C  CB  . VAL   B 1 291 ? 52.017 73.756  19.956 1   45.26  ? 313 VAL   B CB  1 
ATOM   5002  C  CG1 . VAL   B 1 291 ? 50.635 74.376  19.92  1   45.8   ? 313 VAL   B CG1 1 
ATOM   5003  C  CG2 . VAL   B 1 291 ? 52.686 73.939  18.608 1   46.53  ? 313 VAL   B CG2 1 
ATOM   5004  N  N   . ILE   B 1 292 ? 51.873 76.289  22.265 1   44.07  ? 314 ILE   B N   1 
ATOM   5005  C  CA  . ILE   B 1 292 ? 51.679 77.701  22.593 1   43.73  ? 314 ILE   B CA  1 
ATOM   5006  C  C   . ILE   B 1 292 ? 52.939 78.26   23.28  1   43.57  ? 314 ILE   B C   1 
ATOM   5007  O  O   . ILE   B 1 292 ? 53.329 79.401  23.036 1   44.21  ? 314 ILE   B O   1 
ATOM   5008  C  CB  . ILE   B 1 292 ? 50.401 77.887  23.463 1   44.27  ? 314 ILE   B CB  1 
ATOM   5009  C  CG1 . ILE   B 1 292 ? 49.137 77.477  22.696 1   45.23  ? 314 ILE   B CG1 1 
ATOM   5010  C  CG2 . ILE   B 1 292 ? 50.265 79.315  23.998 1   44.77  ? 314 ILE   B CG2 1 
ATOM   5011  C  CD1 . ILE   B 1 292 ? 48.864 78.314  21.404 1   46.44  ? 314 ILE   B CD1 1 
ATOM   5012  N  N   . MET   B 1 293 ? 53.589 77.452  24.115 1   43.13  ? 315 MET   B N   1 
ATOM   5013  C  CA  . MET   B 1 293 ? 54.809 77.845  24.821 1   43.65  ? 315 MET   B CA  1 
ATOM   5014  C  C   . MET   B 1 293 ? 55.965 78      23.842 1   43.94  ? 315 MET   B C   1 
ATOM   5015  O  O   . MET   B 1 293 ? 56.754 78.931  23.971 1   44.02  ? 315 MET   B O   1 
ATOM   5016  C  CB  . MET   B 1 293 ? 55.156 76.799  25.893 1   44.25  ? 315 MET   B CB  1 
ATOM   5017  C  CG  . MET   B 1 293 ? 56.482 77.039  26.572 1   45.88  ? 315 MET   B CG  1 
ATOM   5018  S  SD  . MET   B 1 293 ? 56.933 75.771  27.764 1   47.72  ? 315 MET   B SD  1 
ATOM   5019  C  CE  . MET   B 1 293 ? 56.77  74.269  26.75  1   46.29  ? 315 MET   B CE  1 
ATOM   5020  N  N   . VAL   B 1 294 ? 56.052 77.097  22.852 1   44.04  ? 316 VAL   B N   1 
ATOM   5021  C  CA  . VAL   B 1 294 ? 57.075 77.139  21.813 1   44.3   ? 316 VAL   B CA  1 
ATOM   5022  C  C   . VAL   B 1 294 ? 56.933 78.434  21.007 1   45.09  ? 316 VAL   B C   1 
ATOM   5023  O  O   . VAL   B 1 294 ? 57.922 79.102  20.728 1   45.28  ? 316 VAL   B O   1 
ATOM   5024  C  CB  . VAL   B 1 294 ? 56.953 75.902  20.907 1   44.81  ? 316 VAL   B CB  1 
ATOM   5025  C  CG1 . VAL   B 1 294 ? 57.822 76.036  19.66  1   45.43  ? 316 VAL   B CG1 1 
ATOM   5026  C  CG2 . VAL   B 1 294 ? 57.304 74.641  21.67  1   45.2   ? 316 VAL   B CG2 1 
ATOM   5027  N  N   . GLN   B 1 295 ? 55.696 78.806  20.668 1   45.07  ? 317 GLN   B N   1 
ATOM   5028  C  CA  . GLN   B 1 295 ? 55.432 80.016  19.915 1   45.77  ? 317 GLN   B CA  1 
ATOM   5029  C  C   . GLN   B 1 295 ? 55.703 81.296  20.731 1   46.92  ? 317 GLN   B C   1 
ATOM   5030  O  O   . GLN   B 1 295 ? 56.069 82.345  20.163 1   47.18  ? 317 GLN   B O   1 
ATOM   5031  C  CB  . GLN   B 1 295 ? 54     79.992  19.403 1   46.89  ? 317 GLN   B CB  1 
ATOM   5032  C  CG  . GLN   B 1 295 ? 53.833 80.791  18.13  1   49.69  ? 317 GLN   B CG  1 
ATOM   5033  C  CD  . GLN   B 1 295 ? 52.424 80.796  17.613 1   52.74  ? 317 GLN   B CD  1 
ATOM   5034  O  OE1 . GLN   B 1 295 ? 51.482 80.239  18.223 1   53.93  ? 317 GLN   B OE1 1 
ATOM   5035  N  NE2 . GLN   B 1 295 ? 52.259 81.434  16.458 1   52.37  ? 317 GLN   B NE2 1 
ATOM   5036  N  N   . ARG   B 1 296 ? 55.518 81.213  22.056 1   46.83  ? 318 ARG   B N   1 
ATOM   5037  C  CA  . ARG   B 1 296 ? 55.794 82.329  22.945 1   47.44  ? 318 ARG   B CA  1 
ATOM   5038  C  C   . ARG   B 1 296 ? 57.313 82.506  23.144 1   46.86  ? 318 ARG   B C   1 
ATOM   5039  O  O   . ARG   B 1 296 ? 57.768 83.627  23.365 1   46.51  ? 318 ARG   B O   1 
ATOM   5040  C  CB  . ARG   B 1 296 ? 55.116 82.107  24.301 1   50.29  ? 318 ARG   B CB  1 
ATOM   5041  C  CG  . ARG   B 1 296 ? 53.656 82.524  24.349 1   55.96  ? 318 ARG   B CG  1 
ATOM   5042  C  CD  . ARG   B 1 296 ? 53.122 82.293  25.755 1   61.62  ? 318 ARG   B CD  1 
ATOM   5043  N  NE  . ARG   B 1 296 ? 51.697 82.608  25.871 1   66.13  ? 318 ARG   B NE  1 
ATOM   5044  C  CZ  . ARG   B 1 296 ? 51.21  83.612  26.595 1   69.41  ? 318 ARG   B CZ  1 
ATOM   5045  N  NH1 . ARG   B 1 296 ? 52.029 84.416  27.267 1   69.4   ? 318 ARG   B NH1 1 
ATOM   5046  N  NH2 . ARG   B 1 296 ? 49.901 83.823  26.651 1   69.32  ? 318 ARG   B NH2 1 
ATOM   5047  N  N   . MET   B 1 297 ? 58.092 81.407  23.088 1   46.51  ? 319 MET   B N   1 
ATOM   5048  C  CA  . MET   B 1 297 ? 59.546 81.448  23.275 1   46.25  ? 319 MET   B CA  1 
ATOM   5049  C  C   . MET   B 1 297 ? 60.328 81.757  22     1   46.27  ? 319 MET   B C   1 
ATOM   5050  O  O   . MET   B 1 297 ? 61.263 82.542  22.054 1   46.54  ? 319 MET   B O   1 
ATOM   5051  C  CB  . MET   B 1 297 ? 60.068 80.11   23.822 1   46.24  ? 319 MET   B CB  1 
ATOM   5052  C  CG  . MET   B 1 297 ? 59.645 79.805  25.203 1   47.59  ? 319 MET   B CG  1 
ATOM   5053  S  SD  . MET   B 1 297 ? 60.406 80.852  26.444 1   49.75  ? 319 MET   B SD  1 
ATOM   5054  C  CE  . MET   B 1 297 ? 59.561 80.236  27.852 1   49.34  ? 319 MET   B CE  1 
ATOM   5055  N  N   . ILE   B 1 298 ? 60.034 81.055  20.887 1   45.78  ? 320 ILE   B N   1 
ATOM   5056  C  CA  . ILE   B 1 298 ? 60.801 81.173  19.655 1   45.68  ? 320 ILE   B CA  1 
ATOM   5057  C  C   . ILE   B 1 298 ? 59.968 81.446  18.396 1   46.12  ? 320 ILE   B C   1 
ATOM   5058  O  O   . ILE   B 1 298 ? 60.525 81.451  17.307 1   46.99  ? 320 ILE   B O   1 
ATOM   5059  C  CB  . ILE   B 1 298 ? 61.677 79.904  19.471 1   45.86  ? 320 ILE   B CB  1 
ATOM   5060  C  CG1 . ILE   B 1 298 ? 60.805 78.642  19.382 1   46.65  ? 320 ILE   B CG1 1 
ATOM   5061  C  CG2 . ILE   B 1 298 ? 62.731 79.783  20.585 1   46.29  ? 320 ILE   B CG2 1 
ATOM   5062  C  CD1 . ILE   B 1 298 ? 61.528 77.306  19.355 1   47.74  ? 320 ILE   B CD1 1 
ATOM   5063  N  N   . GLY   B 1 299 ? 58.669 81.675  18.539 1   45.63  ? 321 GLY   B N   1 
ATOM   5064  C  CA  . GLY   B 1 299 ? 57.775 81.928  17.412 1   45.51  ? 321 GLY   B CA  1 
ATOM   5065  C  C   . GLY   B 1 299 ? 57.6   80.738  16.488 1   45.23  ? 321 GLY   B C   1 
ATOM   5066  O  O   . GLY   B 1 299 ? 57.915 79.606  16.864 1   44.74  ? 321 GLY   B O   1 
ATOM   5067  N  N   . SER   B 1 300 ? 57.104 80.977  15.259 1   45.23  ? 322 SER   B N   1 
ATOM   5068  C  CA  . SER   B 1 300 ? 56.945 79.897  14.271 1   45.51  ? 322 SER   B CA  1 
ATOM   5069  C  C   . SER   B 1 300 ? 58.317 79.405  13.744 1   45.95  ? 322 SER   B C   1 
ATOM   5070  O  O   . SER   B 1 300 ? 58.476 78.222  13.417 1   46.24  ? 322 SER   B O   1 
ATOM   5071  C  CB  . SER   B 1 300 ? 56.039 80.335  13.127 1   46.32  ? 322 SER   B CB  1 
ATOM   5072  O  OG  . SER   B 1 300 ? 56.398 81.625  12.657 1   48.17  ? 322 SER   B OG  1 
ATOM   5073  N  N   . GLN   B 1 301 ? 59.316 80.313  13.721 1   45.52  ? 323 GLN   B N   1 
ATOM   5074  C  CA  . GLN   B 1 301 ? 60.69  80.041  13.324 1   45.45  ? 323 GLN   B CA  1 
ATOM   5075  C  C   . GLN   B 1 301 ? 61.658 81.032  13.987 1   45.31  ? 323 GLN   B C   1 
ATOM   5076  O  O   . GLN   B 1 301 ? 61.279 82.151  14.347 1   45.06  ? 323 GLN   B O   1 
ATOM   5077  C  CB  . GLN   B 1 301 ? 60.836 80.09   11.813 1   46.54  ? 323 GLN   B CB  1 
ATOM   5078  C  CG  . GLN   B 1 301 ? 60.317 81.376  11.199 1   48.77  ? 323 GLN   B CG  1 
ATOM   5079  C  CD  . GLN   B 1 301 ? 60.175 81.227  9.712  1   50.87  ? 323 GLN   B CD  1 
ATOM   5080  O  OE1 . GLN   B 1 301 ? 61.16  81.293  8.965  1   52.31  ? 323 GLN   B OE1 1 
ATOM   5081  N  NE2 . GLN   B 1 301 ? 58.946 81.014  9.267  1   50.26  ? 323 GLN   B NE2 1 
ATOM   5082  N  N   . GLN   B 1 302 ? 62.909 80.607  14.162 1   44.82  ? 324 GLN   B N   1 
ATOM   5083  C  CA  . GLN   B 1 302 ? 63.925 81.436  14.805 1   44.76  ? 324 GLN   B CA  1 
ATOM   5084  C  C   . GLN   B 1 302 ? 65.339 80.997  14.305 1   44.42  ? 324 GLN   B C   1 
ATOM   5085  O  O   . GLN   B 1 302 ? 65.458 80.059  13.515 1   44.19  ? 324 GLN   B O   1 
ATOM   5086  C  CB  . GLN   B 1 302 ? 63.744 81.352  16.352 1   45.81  ? 324 GLN   B CB  1 
ATOM   5087  C  CG  . GLN   B 1 302 ? 64.523 82.351  17.211 1   49.33  ? 324 GLN   B CG  1 
ATOM   5088  C  CD  . GLN   B 1 302 ? 64.435 83.813  16.839 1   54.04  ? 324 GLN   B CD  1 
ATOM   5089  O  OE1 . GLN   B 1 302 ? 63.388 84.448  16.946 1   56.12  ? 324 GLN   B OE1 1 
ATOM   5090  N  NE2 . GLN   B 1 302 ? 65.567 84.398  16.435 1   54.45  ? 324 GLN   B NE2 1 
ATOM   5091  N  N   . LEU   B 1 303 ? 66.385 81.715  14.711 1   44.25  ? 325 LEU   B N   1 
ATOM   5092  C  CA  . LEU   B 1 303 ? 67.758 81.422  14.354 1   44.9   ? 325 LEU   B CA  1 
ATOM   5093  C  C   . LEU   B 1 303 ? 68.157 80.034  14.851 1   45.86  ? 325 LEU   B C   1 
ATOM   5094  O  O   . LEU   B 1 303 ? 68.236 79.788  16.054 1   46.1   ? 325 LEU   B O   1 
ATOM   5095  C  CB  . LEU   B 1 303 ? 68.688 82.484  14.94  1   44.8   ? 325 LEU   B CB  1 
ATOM   5096  C  CG  . LEU   B 1 303 ? 70.047 82.565  14.285 1   46.43  ? 325 LEU   B CG  1 
ATOM   5097  C  CD1 . LEU   B 1 303 ? 69.938 83.126  12.882 1   46.92  ? 325 LEU   B CD1 1 
ATOM   5098  C  CD2 . LEU   B 1 303 ? 71.018 83.356  15.145 1   47.29  ? 325 LEU   B CD2 1 
ATOM   5099  N  N   . GLY   B 1 304 ? 68.383 79.143  13.9   1   46.41  ? 326 GLY   B N   1 
ATOM   5100  C  CA  . GLY   B 1 304 ? 68.749 77.753  14.131 1   47.59  ? 326 GLY   B CA  1 
ATOM   5101  C  C   . GLY   B 1 304 ? 67.663 76.767  13.745 1   48.66  ? 326 GLY   B C   1 
ATOM   5102  O  O   . GLY   B 1 304 ? 67.952 75.59   13.528 1   48.8   ? 326 GLY   B O   1 
ATOM   5103  N  N   . THR   B 1 305 ? 66.41  77.247  13.631 1   49.3   ? 327 THR   B N   1 
ATOM   5104  C  CA  . THR   B 1 305 ? 65.24  76.437  13.329 1   50.99  ? 327 THR   B CA  1 
ATOM   5105  C  C   . THR   B 1 305 ? 65.211 75.936  11.882 1   51.33  ? 327 THR   B C   1 
ATOM   5106  O  O   . THR   B 1 305 ? 64.699 74.834  11.627 1   51.65  ? 327 THR   B O   1 
ATOM   5107  C  CB  . THR   B 1 305 ? 63.954 77.19   13.723 1   54.17  ? 327 THR   B CB  1 
ATOM   5108  O  OG1 . THR   B 1 305 ? 64.112 77.713  15.056 1   56.05  ? 327 THR   B OG1 1 
ATOM   5109  C  CG2 . THR   B 1 305 ? 62.733 76.288  13.729 1   55.45  ? 327 THR   B CG2 1 
ATOM   5110  N  N   . GLY   B 1 306 ? 65.786 76.709  10.958 1   50.75  ? 328 GLY   B N   1 
ATOM   5111  C  CA  . GLY   B 1 306 ? 65.797 76.336  9.55   1   50.44  ? 328 GLY   B CA  1 
ATOM   5112  C  C   . GLY   B 1 306 ? 64.393 76.316  8.976  1   50.13  ? 328 GLY   B C   1 
ATOM   5113  O  O   . GLY   B 1 306 ? 63.986 75.338  8.337  1   49.8   ? 328 GLY   B O   1 
ATOM   5114  N  N   . GLY   B 1 307 ? 63.638 77.381  9.265  1   49.95  ? 329 GLY   B N   1 
ATOM   5115  C  CA  . GLY   B 1 307 ? 62.253 77.522  8.821  1   50.1   ? 329 GLY   B CA  1 
ATOM   5116  C  C   . GLY   B 1 307 ? 61.24  77.181  9.895  1   49.8   ? 329 GLY   B C   1 
ATOM   5117  O  O   . GLY   B 1 307 ? 61.603 76.969  11.048 1   49.8   ? 329 GLY   B O   1 
ATOM   5118  N  N   . SER   B 1 308 ? 59.956 77.141  9.535  1   49.5   ? 330 SER   B N   1 
ATOM   5119  C  CA  . SER   B 1 308 ? 58.892 76.833  10.492 1   49.28  ? 330 SER   B CA  1 
ATOM   5120  C  C   . SER   B 1 308 ? 58.479 75.356  10.471 1   48.33  ? 330 SER   B C   1 
ATOM   5121  O  O   . SER   B 1 308 ? 57.349 75.037  10.843 1   48.1   ? 330 SER   B O   1 
ATOM   5122  C  CB  . SER   B 1 308 ? 57.68  77.734  10.255 1   50.9   ? 330 SER   B CB  1 
ATOM   5123  O  OG  . SER   B 1 308 ? 57.131 77.565  8.959  1   53.62  ? 330 SER   B OG  1 
ATOM   5124  N  N   . SER   B 1 309 ? 59.403 74.455  10.074 1   47.57  ? 331 SER   B N   1 
ATOM   5125  C  CA  . SER   B 1 309 ? 59.123 73.017  9.958  1   47.15  ? 331 SER   B CA  1 
ATOM   5126  C  C   . SER   B 1 309 ? 58.811 72.329  11.283 1   45.94  ? 331 SER   B C   1 
ATOM   5127  O  O   . SER   B 1 309 ? 57.862 71.542  11.35  1   46.19  ? 331 SER   B O   1 
ATOM   5128  C  CB  . SER   B 1 309 ? 60.238 72.279  9.216  1   48.81  ? 331 SER   B CB  1 
ATOM   5129  O  OG  . SER   B 1 309 ? 61.54  72.784  9.467  1   51.84  ? 331 SER   B OG  1 
ATOM   5130  N  N   . GLY   B 1 310 ? 59.59  72.638  12.31  1   44.47  ? 332 GLY   B N   1 
ATOM   5131  C  CA  . GLY   B 1 310 ? 59.424 72.05   13.631 1   43.96  ? 332 GLY   B CA  1 
ATOM   5132  C  C   . GLY   B 1 310 ? 58.139 72.468  14.306 1   43.01  ? 332 GLY   B C   1 
ATOM   5133  O  O   . GLY   B 1 310 ? 57.447 71.64   14.898 1   42.02  ? 332 GLY   B O   1 
ATOM   5134  N  N   . TYR   B 1 311 ? 57.811 73.756  14.199 1   43.34  ? 333 TYR   B N   1 
ATOM   5135  C  CA  . TYR   B 1 311 ? 56.598 74.347  14.747 1   44.27  ? 333 TYR   B CA  1 
ATOM   5136  C  C   . TYR   B 1 311 ? 55.361 73.764  14.036 1   45.03  ? 333 TYR   B C   1 
ATOM   5137  O  O   . TYR   B 1 311 ? 54.396 73.395  14.699 1   45.39  ? 333 TYR   B O   1 
ATOM   5138  C  CB  . TYR   B 1 311 ? 56.668 75.877  14.592 1   44.62  ? 333 TYR   B CB  1 
ATOM   5139  C  CG  . TYR   B 1 311 ? 55.34  76.585  14.758 1   45.73  ? 333 TYR   B CG  1 
ATOM   5140  C  CD1 . TYR   B 1 311 ? 54.79  76.785  16.013 1   46.47  ? 333 TYR   B CD1 1 
ATOM   5141  C  CD2 . TYR   B 1 311 ? 54.626 77.034  13.655 1   46.74  ? 333 TYR   B CD2 1 
ATOM   5142  C  CE1 . TYR   B 1 311 ? 53.561 77.414  16.168 1   47.33  ? 333 TYR   B CE1 1 
ATOM   5143  C  CE2 . TYR   B 1 311 ? 53.403 77.673  13.799 1   47.42  ? 333 TYR   B CE2 1 
ATOM   5144  C  CZ  . TYR   B 1 311 ? 52.872 77.861  15.057 1   48     ? 333 TYR   B CZ  1 
ATOM   5145  O  OH  . TYR   B 1 311 ? 51.645 78.468  15.189 1   49.46  ? 333 TYR   B OH  1 
ATOM   5146  N  N   . GLN   B 1 312 ? 55.404 73.676  12.694 1   45.28  ? 334 GLN   B N   1 
ATOM   5147  C  CA  . GLN   B 1 312 ? 54.33  73.107  11.891 1   46.02  ? 334 GLN   B CA  1 
ATOM   5148  C  C   . GLN   B 1 312 ? 54.145 71.614  12.151 1   46.64  ? 334 GLN   B C   1 
ATOM   5149  O  O   . GLN   B 1 312 ? 53.033 71.114  12.018 1   46.29  ? 334 GLN   B O   1 
ATOM   5150  C  CB  . GLN   B 1 312 ? 54.551 73.362  10.392 1   47.8   ? 334 GLN   B CB  1 
ATOM   5151  C  CG  . GLN   B 1 312 ? 54.195 74.777  9.92   1   51.7   ? 334 GLN   B CG  1 
ATOM   5152  C  CD  . GLN   B 1 312 ? 52.791 75.209  10.285 1   56.86  ? 334 GLN   B CD  1 
ATOM   5153  O  OE1 . GLN   B 1 312 ? 52.573 76.348  10.737 1   57.89  ? 334 GLN   B OE1 1 
ATOM   5154  N  NE2 . GLN   B 1 312 ? 51.806 74.31   10.102 1   57.77  ? 334 GLN   B NE2 1 
ATOM   5155  N  N   . TYR   B 1 313 ? 55.222 70.9    12.524 1   47.4   ? 335 TYR   B N   1 
ATOM   5156  C  CA  . TYR   B 1 313 ? 55.126 69.49   12.87  1   48.53  ? 335 TYR   B CA  1 
ATOM   5157  C  C   . TYR   B 1 313 ? 54.33  69.392  14.179 1   49.35  ? 335 TYR   B C   1 
ATOM   5158  O  O   . TYR   B 1 313 ? 53.418 68.567  14.275 1   50.03  ? 335 TYR   B O   1 
ATOM   5159  C  CB  . TYR   B 1 313 ? 56.522 68.829  13.027 1   48.8   ? 335 TYR   B CB  1 
ATOM   5160  C  CG  . TYR   B 1 313 ? 56.473 67.556  13.85  1   50.47  ? 335 TYR   B CG  1 
ATOM   5161  C  CD1 . TYR   B 1 313 ? 55.897 66.4    13.342 1   51.84  ? 335 TYR   B CD1 1 
ATOM   5162  C  CD2 . TYR   B 1 313 ? 56.861 67.551  15.185 1   51.8   ? 335 TYR   B CD2 1 
ATOM   5163  C  CE1 . TYR   B 1 313 ? 55.772 65.252  14.118 1   53.28  ? 335 TYR   B CE1 1 
ATOM   5164  C  CE2 . TYR   B 1 313 ? 56.727 66.415  15.976 1   53.1   ? 335 TYR   B CE2 1 
ATOM   5165  C  CZ  . TYR   B 1 313 ? 56.196 65.26   15.436 1   54.42  ? 335 TYR   B CZ  1 
ATOM   5166  O  OH  . TYR   B 1 313 ? 56.085 64.122  16.21  1   56.47  ? 335 TYR   B OH  1 
ATOM   5167  N  N   . LEU   B 1 314 ? 54.671 70.226  15.178 1   48.78  ? 336 LEU   B N   1 
ATOM   5168  C  CA  . LEU   B 1 314 ? 53.979 70.207  16.459 1   48.86  ? 336 LEU   B CA  1 
ATOM   5169  C  C   . LEU   B 1 314 ? 52.494 70.526  16.288 1   49.9   ? 336 LEU   B C   1 
ATOM   5170  O  O   . LEU   B 1 314 ? 51.682 69.934  16.985 1   50.58  ? 336 LEU   B O   1 
ATOM   5171  C  CB  . LEU   B 1 314 ? 54.613 71.19   17.449 1   48.35  ? 336 LEU   B CB  1 
ATOM   5172  C  CG  . LEU   B 1 314 ? 56.059 70.967  17.85  1   48.51  ? 336 LEU   B CG  1 
ATOM   5173  C  CD1 . LEU   B 1 314 ? 56.508 72.063  18.788 1   48.81  ? 336 LEU   B CD1 1 
ATOM   5174  C  CD2 . LEU   B 1 314 ? 56.258 69.609  18.476 1   48.79  ? 336 LEU   B CD2 1 
ATOM   5175  N  N   . ARG   B 1 315 ? 52.133 71.418  15.346 1   50.11  ? 337 ARG   B N   1 
ATOM   5176  C  CA  . ARG   B 1 315 ? 50.734 71.745  15.084 1   50.99  ? 337 ARG   B CA  1 
ATOM   5177  C  C   . ARG   B 1 315 ? 49.974 70.593  14.43  1   50.98  ? 337 ARG   B C   1 
ATOM   5178  O  O   . ARG   B 1 315 ? 48.767 70.48   14.604 1   51.27  ? 337 ARG   B O   1 
ATOM   5179  C  CB  . ARG   B 1 315 ? 50.622 72.999  14.233 1   53.61  ? 337 ARG   B CB  1 
ATOM   5180  C  CG  . ARG   B 1 315 ? 50.858 74.264  15.006 1   59.67  ? 337 ARG   B CG  1 
ATOM   5181  C  CD  . ARG   B 1 315 ? 50.543 75.468  14.138 1   66.67  ? 337 ARG   B CD  1 
ATOM   5182  N  NE  . ARG   B 1 315 ? 49.105 75.727  14.009 1   72.68  ? 337 ARG   B NE  1 
ATOM   5183  C  CZ  . ARG   B 1 315 ? 48.485 75.976  12.855 1   75.98  ? 337 ARG   B CZ  1 
ATOM   5184  N  NH1 . ARG   B 1 315 ? 49.173 76.014  11.717 1   75.68  ? 337 ARG   B NH1 1 
ATOM   5185  N  NH2 . ARG   B 1 315 ? 47.175 76.195  12.831 1   76     ? 337 ARG   B NH2 1 
ATOM   5186  N  N   . SER   B 1 316 ? 50.67  69.741  13.688 1   50.71  ? 338 SER   B N   1 
ATOM   5187  C  CA  . SER   B 1 316 ? 50.067 68.583  13.062 1   51.42  ? 338 SER   B CA  1 
ATOM   5188  C  C   . SER   B 1 316 ? 49.819 67.441  14.066 1   52.22  ? 338 SER   B C   1 
ATOM   5189  O  O   . SER   B 1 316 ? 49.019 66.547  13.78  1   52.84  ? 338 SER   B O   1 
ATOM   5190  C  CB  . SER   B 1 316 ? 50.917 68.107  11.892 1   53.14  ? 338 SER   B CB  1 
ATOM   5191  O  OG  . SER   B 1 316 ? 52.127 67.506  12.323 1   55.97  ? 338 SER   B OG  1 
ATOM   5192  N  N   . THR   B 1 317 ? 50.5   67.453  15.233 1   52.09  ? 339 THR   B N   1 
ATOM   5193  C  CA  . THR   B 1 317 ? 50.272 66.464  16.282 1   52.42  ? 339 THR   B CA  1 
ATOM   5194  C  C   . THR   B 1 317 ? 48.959 66.727  17.044 1   53.46  ? 339 THR   B C   1 
ATOM   5195  O  O   . THR   B 1 317 ? 48.511 65.855  17.784 1   53.31  ? 339 THR   B O   1 
ATOM   5196  C  CB  . THR   B 1 317 ? 51.473 66.338  17.21  1   53.08  ? 339 THR   B CB  1 
ATOM   5197  O  OG1 . THR   B 1 317 ? 51.672 67.567  17.899 1   53.74  ? 339 THR   B OG1 1 
ATOM   5198  C  CG2 . THR   B 1 317 ? 52.729 65.951  16.479 1   53.29  ? 339 THR   B CG2 1 
ATOM   5199  N  N   . LEU   B 1 318 ? 48.322 67.9    16.843 1   54.3   ? 340 LEU   B N   1 
ATOM   5200  C  CA  . LEU   B 1 318 ? 47.043 68.222  17.465 1   55.81  ? 340 LEU   B CA  1 
ATOM   5201  C  C   . LEU   B 1 318 ? 45.834 67.602  16.708 1   58.01  ? 340 LEU   B C   1 
ATOM   5202  O  O   . LEU   B 1 318 ? 44.706 67.677  17.198 1   58.29  ? 340 LEU   B O   1 
ATOM   5203  C  CB  . LEU   B 1 318 ? 46.879 69.74   17.538 1   55.76  ? 340 LEU   B CB  1 
ATOM   5204  C  CG  . LEU   B 1 318 ? 48.013 70.529  18.162 1   56.5   ? 340 LEU   B CG  1 
ATOM   5205  C  CD1 . LEU   B 1 318 ? 47.743 72.018  18.069 1   56.97  ? 340 LEU   B CD1 1 
ATOM   5206  C  CD2 . LEU   B 1 318 ? 48.187 70.158  19.576 1   56.64  ? 340 LEU   B CD2 1 
ATOM   5207  N  N   . SER   B 1 319 ? 46.067 67.018  15.513 1   59.42  ? 341 SER   B N   1 
ATOM   5208  C  CA  . SER   B 1 319 ? 45.037 66.393  14.672 1   61.5   ? 341 SER   B CA  1 
ATOM   5209  C  C   . SER   B 1 319 ? 44.522 65.082  15.276 1   63.81  ? 341 SER   B C   1 
ATOM   5210  O  O   . SER   B 1 319 ? 45.207 64.474  16.111 1   64.1   ? 341 SER   B O   1 
ATOM   5211  C  CB  . SER   B 1 319 ? 45.571 66.131  13.258 1   61.89  ? 341 SER   B CB  1 
ATOM   5212  O  OG  . SER   B 1 319 ? 46.524 65.078  13.203 1   62.83  ? 341 SER   B OG  1 
ATOM   5213  N  N   . ASP   B 1 320 ? 43.328 64.624  14.82  1   64.78  ? 342 ASP   B N   1 
ATOM   5214  C  CA  . ASP   B 1 320 ? 42.741 63.374  15.295 1   65.79  ? 342 ASP   B CA  1 
ATOM   5215  C  C   . ASP   B 1 320 ? 43.518 62.117  14.831 1   66.18  ? 342 ASP   B C   1 
ATOM   5216  O  O   . ASP   B 1 320 ? 43.276 61.029  15.338 1   66.1   ? 342 ASP   B O   1 
ATOM   5217  C  CB  . ASP   B 1 320 ? 41.246 63.318  14.955 1   68.12  ? 342 ASP   B CB  1 
ATOM   5218  C  CG  . ASP   B 1 320 ? 40.393 64.283  15.797 1   72.86  ? 342 ASP   B CG  1 
ATOM   5219  O  OD1 . ASP   B 1 320 ? 40.94  64.9    16.746 1   73.34  ? 342 ASP   B OD1 1 
ATOM   5220  O  OD2 . ASP   B 1 320 ? 39.176 64.41   15.515 1   74.94  ? 342 ASP   B OD2 1 
ATOM   5221  N  N   . ARG   B 1 321 ? 44.524 62.286  13.958 1   66.71  ? 343 ARG   B N   1 
ATOM   5222  C  CA  . ARG   B 1 321 ? 45.442 61.209  13.557 1   67.35  ? 343 ARG   B CA  1 
ATOM   5223  C  C   . ARG   B 1 321 ? 46.332 60.782  14.756 1   65.91  ? 343 ARG   B C   1 
ATOM   5224  O  O   . ARG   B 1 321 ? 46.923 59.697  14.725 1   66.25  ? 343 ARG   B O   1 
ATOM   5225  C  CB  . ARG   B 1 321 ? 46.365 61.679  12.415 1   70.34  ? 343 ARG   B CB  1 
ATOM   5226  C  CG  . ARG   B 1 321 ? 45.641 62.401  11.281 1   76.3   ? 343 ARG   B CG  1 
ATOM   5227  C  CD  . ARG   B 1 321 ? 46.618 63.033  10.304 1   82.03  ? 343 ARG   B CD  1 
ATOM   5228  N  NE  . ARG   B 1 321 ? 47.299 62.025  9.484  1   87.14  ? 343 ARG   B NE  1 
ATOM   5229  C  CZ  . ARG   B 1 321 ? 48.608 61.791  9.512  1   90.4   ? 343 ARG   B CZ  1 
ATOM   5230  N  NH1 . ARG   B 1 321 ? 49.398 62.489  10.322 1   90.53  ? 343 ARG   B NH1 1 
ATOM   5231  N  NH2 . ARG   B 1 321 ? 49.14  60.86   8.725  1   90.22  ? 343 ARG   B NH2 1 
ATOM   5232  N  N   . TYR   B 1 322 ? 46.463 61.653  15.786 1   63.84  ? 344 TYR   B N   1 
ATOM   5233  C  CA  . TYR   B 1 322 ? 47.249 61.379  16.982 1   62.03  ? 344 TYR   B CA  1 
ATOM   5234  C  C   . TYR   B 1 322 ? 46.399 60.901  18.181 1   59.51  ? 344 TYR   B C   1 
ATOM   5235  O  O   . TYR   B 1 322 ? 46.957 60.423  19.162 1   59.4   ? 344 TYR   B O   1 
ATOM   5236  C  CB  . TYR   B 1 322 ? 48.119 62.591  17.332 1   62.15  ? 344 TYR   B CB  1 
ATOM   5237  C  CG  . TYR   B 1 322 ? 49.404 62.638  16.532 1   62.68  ? 344 TYR   B CG  1 
ATOM   5238  C  CD1 . TYR   B 1 322 ? 49.416 63.109  15.225 1   63.45  ? 344 TYR   B CD1 1 
ATOM   5239  C  CD2 . TYR   B 1 322 ? 50.596 62.163  17.064 1   63.32  ? 344 TYR   B CD2 1 
ATOM   5240  C  CE1 . TYR   B 1 322 ? 50.593 63.146  14.484 1   64.25  ? 344 TYR   B CE1 1 
ATOM   5241  C  CE2 . TYR   B 1 322 ? 51.775 62.181  16.329 1   64.03  ? 344 TYR   B CE2 1 
ATOM   5242  C  CZ  . TYR   B 1 322 ? 51.77  62.673  15.038 1   65     ? 344 TYR   B CZ  1 
ATOM   5243  O  OH  . TYR   B 1 322 ? 52.945 62.701  14.326 1   66.58  ? 344 TYR   B OH  1 
ATOM   5244  N  N   . LYS   B 1 323 ? 45.066 61.002  18.089 1   57.61  ? 345 LYS   B N   1 
ATOM   5245  C  CA  . LYS   B 1 323 ? 44.156 60.514  19.113 1   56.6   ? 345 LYS   B CA  1 
ATOM   5246  C  C   . LYS   B 1 323 ? 44.065 58.986  18.96  1   55.25  ? 345 LYS   B C   1 
ATOM   5247  O  O   . LYS   B 1 323 ? 43.689 58.495  17.894 1   55.58  ? 345 LYS   B O   1 
ATOM   5248  C  CB  . LYS   B 1 323 ? 42.77  61.171  18.973 1   57.9   ? 345 LYS   B CB  1 
ATOM   5249  C  CG  . LYS   B 1 323 ? 42.657 62.513  19.694 1   60.75  ? 345 LYS   B CG  1 
ATOM   5250  C  CD  . LYS   B 1 323 ? 41.652 62.434  20.838 1   64.41  ? 345 LYS   B CD  1 
ATOM   5251  C  CE  . LYS   B 1 323 ? 41.825 63.514  21.885 1   67.57  ? 345 LYS   B CE  1 
ATOM   5252  N  NZ  . LYS   B 1 323 ? 41.252 64.815  21.458 1   69.73  ? 345 LYS   B NZ  1 
ATOM   5253  N  N   . VAL   B 1 324 ? 44.477 58.245  19.995 1   53.36  ? 346 VAL   B N   1 
ATOM   5254  C  CA  . VAL   B 1 324 ? 44.496 56.786  20.005 1   52.25  ? 346 VAL   B CA  1 
ATOM   5255  C  C   . VAL   B 1 324 ? 43.097 56.15   20.059 1   51.6   ? 346 VAL   B C   1 
ATOM   5256  O  O   . VAL   B 1 324 ? 42.766 55.305  19.236 1   51.65  ? 346 VAL   B O   1 
ATOM   5257  C  CB  . VAL   B 1 324 ? 45.391 56.262  21.154 1   52.13  ? 346 VAL   B CB  1 
ATOM   5258  C  CG1 . VAL   B 1 324 ? 45.438 54.744  21.159 1   52.64  ? 346 VAL   B CG1 1 
ATOM   5259  C  CG2 . VAL   B 1 324 ? 46.782 56.846  21.079 1   52.16  ? 346 VAL   B CG2 1 
ATOM   5260  N  N   . PHE   B 1 325 ? 42.281 56.537  21.044 1   51.02  ? 347 PHE   B N   1 
ATOM   5261  C  CA  . PHE   B 1 325 ? 40.951 55.97   21.241 1   50.5   ? 347 PHE   B CA  1 
ATOM   5262  C  C   . PHE   B 1 325 ? 39.88  56.846  20.632 1   50.85  ? 347 PHE   B C   1 
ATOM   5263  O  O   . PHE   B 1 325 ? 38.856 57.126  21.257 1   51.08  ? 347 PHE   B O   1 
ATOM   5264  C  CB  . PHE   B 1 325 ? 40.704 55.711  22.722 1   49.52  ? 347 PHE   B CB  1 
ATOM   5265  C  CG  . PHE   B 1 325 ? 41.677 54.704  23.291 1   49.51  ? 347 PHE   B CG  1 
ATOM   5266  C  CD1 . PHE   B 1 325 ? 41.424 53.345  23.202 1   49.95  ? 347 PHE   B CD1 1 
ATOM   5267  C  CD2 . PHE   B 1 325 ? 42.853 55.115  23.896 1   49.62  ? 347 PHE   B CD2 1 
ATOM   5268  C  CE1 . PHE   B 1 325 ? 42.318 52.422  23.72  1   50.24  ? 347 PHE   B CE1 1 
ATOM   5269  C  CE2 . PHE   B 1 325 ? 43.749 54.186  24.402 1   49.99  ? 347 PHE   B CE2 1 
ATOM   5270  C  CZ  . PHE   B 1 325 ? 43.472 52.846  24.32  1   49.76  ? 347 PHE   B CZ  1 
ATOM   5271  N  N   . LEU   B 1 326 ? 40.119 57.22   19.373 1   50.51  ? 348 LEU   B N   1 
ATOM   5272  C  CA  . LEU   B 1 326 ? 39.284 58.058  18.535 1   50.89  ? 348 LEU   B CA  1 
ATOM   5273  C  C   . LEU   B 1 326 ? 37.834 57.547  18.435 1   50.74  ? 348 LEU   B C   1 
ATOM   5274  O  O   . LEU   B 1 326 ? 36.892 58.346  18.385 1   51.12  ? 348 LEU   B O   1 
ATOM   5275  C  CB  . LEU   B 1 326 ? 39.936 58.078  17.142 1   51.42  ? 348 LEU   B CB  1 
ATOM   5276  C  CG  . LEU   B 1 326 ? 39.458 59.16   16.201 1   53.56  ? 348 LEU   B CG  1 
ATOM   5277  C  CD1 . LEU   B 1 326 ? 39.826 60.521  16.73  1   54.31  ? 348 LEU   B CD1 1 
ATOM   5278  C  CD2 . LEU   B 1 326 ? 40.008 58.945  14.794 1   54.53  ? 348 LEU   B CD2 1 
ATOM   5279  N  N   . ASP   B 1 327 ? 37.664 56.22   18.392 1   50.1   ? 349 ASP   B N   1 
ATOM   5280  C  CA  . ASP   B 1 327 ? 36.361 55.572  18.267 1   50.39  ? 349 ASP   B CA  1 
ATOM   5281  C  C   . ASP   B 1 327 ? 35.475 55.783  19.476 1   50.47  ? 349 ASP   B C   1 
ATOM   5282  O  O   . ASP   B 1 327 ? 34.26  55.887  19.345 1   51.18  ? 349 ASP   B O   1 
ATOM   5283  C  CB  . ASP   B 1 327 ? 36.54  54.066  18.068 1   51.85  ? 349 ASP   B CB  1 
ATOM   5284  C  CG  . ASP   B 1 327 ? 37.329 53.709  16.843 1   54.71  ? 349 ASP   B CG  1 
ATOM   5285  O  OD1 . ASP   B 1 327 ? 38.521 54.066  16.781 1   55.22  ? 349 ASP   B OD1 1 
ATOM   5286  O  OD2 . ASP   B 1 327 ? 36.768 53.053  15.954 1   56.27  ? 349 ASP   B OD2 1 
ATOM   5287  N  N   . LEU   B 1 328 ? 36.079 55.8    20.658 1   49.81  ? 350 LEU   B N   1 
ATOM   5288  C  CA  . LEU   B 1 328 ? 35.358 55.946  21.909 1   49.36  ? 350 LEU   B CA  1 
ATOM   5289  C  C   . LEU   B 1 328 ? 34.648 57.275  22.028 1   49.76  ? 350 LEU   B C   1 
ATOM   5290  O  O   . LEU   B 1 328 ? 33.583 57.328  22.639 1   49.89  ? 350 LEU   B O   1 
ATOM   5291  C  CB  . LEU   B 1 328 ? 36.318 55.759  23.082 1   48.76  ? 350 LEU   B CB  1 
ATOM   5292  C  CG  . LEU   B 1 328 ? 36.949 54.387  23.258 1   49.2   ? 350 LEU   B CG  1 
ATOM   5293  C  CD1 . LEU   B 1 328 ? 37.779 54.358  24.507 1   49.87  ? 350 LEU   B CD1 1 
ATOM   5294  C  CD2 . LEU   B 1 328 ? 35.895 53.295  23.344 1   49.37  ? 350 LEU   B CD2 1 
ATOM   5295  N  N   . PHE   B 1 329 ? 35.232 58.349  21.452 1   49.75  ? 351 PHE   B N   1 
ATOM   5296  C  CA  . PHE   B 1 329 ? 34.66  59.693  21.509 1   49.89  ? 351 PHE   B CA  1 
ATOM   5297  C  C   . PHE   B 1 329 ? 33.333 59.818  20.778 1   51.34  ? 351 PHE   B C   1 
ATOM   5298  O  O   . PHE   B 1 329 ? 32.452 60.567  21.209 1   52.05  ? 351 PHE   B O   1 
ATOM   5299  C  CB  . PHE   B 1 329 ? 35.655 60.723  20.976 1   48.95  ? 351 PHE   B CB  1 
ATOM   5300  C  CG  . PHE   B 1 329 ? 36.819 60.968  21.901 1   48.75  ? 351 PHE   B CG  1 
ATOM   5301  C  CD1 . PHE   B 1 329 ? 36.762 61.956  22.868 1   49.35  ? 351 PHE   B CD1 1 
ATOM   5302  C  CD2 . PHE   B 1 329 ? 37.967 60.207  21.811 1   48.92  ? 351 PHE   B CD2 1 
ATOM   5303  C  CE1 . PHE   B 1 329 ? 37.824 62.158  23.74  1   49.58  ? 351 PHE   B CE1 1 
ATOM   5304  C  CE2 . PHE   B 1 329 ? 39.03  60.425  22.671 1   49.18  ? 351 PHE   B CE2 1 
ATOM   5305  C  CZ  . PHE   B 1 329 ? 38.953 61.397  23.626 1   49     ? 351 PHE   B CZ  1 
ATOM   5306  N  N   . ASN   B 1 330 ? 33.162 59.037  19.719 1   51.53  ? 352 ASN   B N   1 
ATOM   5307  C  CA  . ASN   B 1 330 ? 31.967 59.099  18.9   1   52.16  ? 352 ASN   B CA  1 
ATOM   5308  C  C   . ASN   B 1 330 ? 30.828 58.129  19.291 1   51.16  ? 352 ASN   B C   1 
ATOM   5309  O  O   . ASN   B 1 330 ? 29.736 58.24   18.729 1   51.72  ? 352 ASN   B O   1 
ATOM   5310  C  CB  . ASN   B 1 330 ? 32.375 58.886  17.438 1   54.81  ? 352 ASN   B CB  1 
ATOM   5311  C  CG  . ASN   B 1 330 ? 31.436 59.516  16.444 1   60.07  ? 352 ASN   B CG  1 
ATOM   5312  O  OD1 . ASN   B 1 330 ? 30.925 60.629  16.648 1   61.8   ? 352 ASN   B OD1 1 
ATOM   5313  N  ND2 . ASN   B 1 330 ? 31.173 58.802  15.354 1   61.28  ? 352 ASN   B ND2 1 
ATOM   5314  N  N   . LEU   B 1 331 ? 31.046 57.209  20.244 1   49.54  ? 353 LEU   B N   1 
ATOM   5315  C  CA  . LEU   B 1 331 ? 30.021 56.22   20.634 1   48.69  ? 353 LEU   B CA  1 
ATOM   5316  C  C   . LEU   B 1 331 ? 28.606 56.767  20.938 1   48.12  ? 353 LEU   B C   1 
ATOM   5317  O  O   . LEU   B 1 331 ? 27.63  56.029  20.804 1   47.85  ? 353 LEU   B O   1 
ATOM   5318  C  CB  . LEU   B 1 331 ? 30.495 55.375  21.815 1   48.4   ? 353 LEU   B CB  1 
ATOM   5319  C  CG  . LEU   B 1 331 ? 31.745 54.562  21.564 1   49.82  ? 353 LEU   B CG  1 
ATOM   5320  C  CD1 . LEU   B 1 331 ? 32.203 53.873  22.821 1   50.4   ? 353 LEU   B CD1 1 
ATOM   5321  C  CD2 . LEU   B 1 331 ? 31.53  53.559  20.481 1   50.53  ? 353 LEU   B CD2 1 
ATOM   5322  N  N   . SER   B 1 332 ? 28.486 58.03   21.352 1   48.05  ? 354 SER   B N   1 
ATOM   5323  C  CA  . SER   B 1 332 ? 27.175 58.609  21.649 1   48.21  ? 354 SER   B CA  1 
ATOM   5324  C  C   . SER   B 1 332 ? 26.318 58.851  20.405 1   49.04  ? 354 SER   B C   1 
ATOM   5325  O  O   . SER   B 1 332 ? 25.113 59.046  20.535 1   49.48  ? 354 SER   B O   1 
ATOM   5326  C  CB  . SER   B 1 332 ? 27.323 59.879  22.468 1   48.84  ? 354 SER   B CB  1 
ATOM   5327  O  OG  . SER   B 1 332 ? 27.869 59.561  23.733 1   51.01  ? 354 SER   B OG  1 
ATOM   5328  N  N   . THR   B 1 333 ? 26.93  58.835  19.204 1   49.07  ? 355 THR   B N   1 
ATOM   5329  C  CA  . THR   B 1 333 ? 26.236 59.01   17.92  1   49.67  ? 355 THR   B CA  1 
ATOM   5330  C  C   . THR   B 1 333 ? 25.243 57.87   17.652 1   49.19  ? 355 THR   B C   1 
ATOM   5331  O  O   . THR   B 1 333 ? 24.25  58.073  16.953 1   48.96  ? 355 THR   B O   1 
ATOM   5332  C  CB  . THR   B 1 333 ? 27.272 59.078  16.778 1   51.36  ? 355 THR   B CB  1 
ATOM   5333  O  OG1 . THR   B 1 333 ? 28.287 60.025  17.104 1   52.63  ? 355 THR   B OG1 1 
ATOM   5334  C  CG2 . THR   B 1 333 ? 26.667 59.444  15.448 1   51.81  ? 355 THR   B CG2 1 
ATOM   5335  N  N   . PHE   B 1 334 ? 25.519 56.673  18.203 1   48.88  ? 356 PHE   B N   1 
ATOM   5336  C  CA  . PHE   B 1 334 ? 24.725 55.453  18.003 1   49.24  ? 356 PHE   B CA  1 
ATOM   5337  C  C   . PHE   B 1 334 ? 23.646 55.207  19.07  1   49.63  ? 356 PHE   B C   1 
ATOM   5338  O  O   . PHE   B 1 334 ? 22.92  54.222  18.983 1   49.53  ? 356 PHE   B O   1 
ATOM   5339  C  CB  . PHE   B 1 334 ? 25.653 54.231  17.935 1   49.01  ? 356 PHE   B CB  1 
ATOM   5340  C  CG  . PHE   B 1 334 ? 26.896 54.461  17.114 1   49.71  ? 356 PHE   B CG  1 
ATOM   5341  C  CD1 . PHE   B 1 334 ? 26.809 54.733  15.759 1   50.34  ? 356 PHE   B CD1 1 
ATOM   5342  C  CD2 . PHE   B 1 334 ? 28.147 54.477  17.709 1   50.22  ? 356 PHE   B CD2 1 
ATOM   5343  C  CE1 . PHE   B 1 334 ? 27.944 54.993  15.017 1   50.63  ? 356 PHE   B CE1 1 
ATOM   5344  C  CE2 . PHE   B 1 334 ? 29.284 54.724  16.957 1   50.49  ? 356 PHE   B CE2 1 
ATOM   5345  C  CZ  . PHE   B 1 334 ? 29.175 54.971  15.618 1   50.29  ? 356 PHE   B CZ  1 
ATOM   5346  N  N   . LEU   B 1 335 ? 23.537 56.089  20.061 1   49.88  ? 357 LEU   B N   1 
ATOM   5347  C  CA  . LEU   B 1 335 ? 22.601 55.943  21.16  1   50.95  ? 357 LEU   B CA  1 
ATOM   5348  C  C   . LEU   B 1 335 ? 21.125 56.006  20.771 1   52.75  ? 357 LEU   B C   1 
ATOM   5349  O  O   . LEU   B 1 335 ? 20.721 56.827  19.925 1   53.32  ? 357 LEU   B O   1 
ATOM   5350  C  CB  . LEU   B 1 335 ? 22.881 57.034  22.19  1   51.05  ? 357 LEU   B CB  1 
ATOM   5351  C  CG  . LEU   B 1 335 ? 22.829 56.608  23.645 1   52.1   ? 357 LEU   B CG  1 
ATOM   5352  C  CD1 . LEU   B 1 335 ? 24.108 55.899  24.026 1   52.72  ? 357 LEU   B CD1 1 
ATOM   5353  C  CD2 . LEU   B 1 335 ? 22.621 57.805  24.538 1   52.04  ? 357 LEU   B CD2 1 
ATOM   5354  N  N   . ILE   B 1 336 ? 20.317 55.15   21.428 1   52.94  ? 358 ILE   B N   1 
ATOM   5355  C  CA  . ILE   B 1 336 ? 18.858 55.112  21.309 1   53.66  ? 358 ILE   B CA  1 
ATOM   5356  C  C   . ILE   B 1 336 ? 18.27  55.388  22.701 1   54.78  ? 358 ILE   B C   1 
ATOM   5357  O  O   . ILE   B 1 336 ? 18.955 55.155  23.702 1   54.87  ? 358 ILE   B O   1 
ATOM   5358  C  CB  . ILE   B 1 336 ? 18.322 53.791  20.696 1   53.94  ? 358 ILE   B CB  1 
ATOM   5359  C  CG1 . ILE   B 1 336 ? 19.043 52.549  21.262 1   54.62  ? 358 ILE   B CG1 1 
ATOM   5360  C  CG2 . ILE   B 1 336 ? 18.364 53.851  19.182 1   54.41  ? 358 ILE   B CG2 1 
ATOM   5361  C  CD1 . ILE   B 1 336 ? 18.456 51.23   20.832 1   55.77  ? 358 ILE   B CD1 1 
ATOM   5362  N  N   . PRO   B 1 337 ? 17.015 55.891  22.806 1   55.25  ? 359 PRO   B N   1 
ATOM   5363  C  CA  . PRO   B 1 337 ? 16.449 56.181  24.138 1   55.86  ? 359 PRO   B CA  1 
ATOM   5364  C  C   . PRO   B 1 337 ? 16.375 54.985  25.091 1   57.12  ? 359 PRO   B C   1 
ATOM   5365  O  O   . PRO   B 1 337 ? 16.404 53.846  24.637 1   56.97  ? 359 PRO   B O   1 
ATOM   5366  C  CB  . PRO   B 1 337 ? 15.054 56.723  23.819 1   56.09  ? 359 PRO   B CB  1 
ATOM   5367  C  CG  . PRO   B 1 337 ? 15.126 57.171  22.409 1   56.06  ? 359 PRO   B CG  1 
ATOM   5368  C  CD  . PRO   B 1 337 ? 16.066 56.243  21.733 1   54.34  ? 359 PRO   B CD  1 
ATOM   5369  N  N   . ARG   B 1 338 ? 16.249 55.245  26.415 1   58.21  ? 360 ARG   B N   1 
ATOM   5370  C  CA  . ARG   B 1 338 ? 16.178 54.209  27.445 1   59.73  ? 360 ARG   B CA  1 
ATOM   5371  C  C   . ARG   B 1 338 ? 15.145 53.118  27.12  1   61.37  ? 360 ARG   B C   1 
ATOM   5372  O  O   . ARG   B 1 338 ? 15.45  51.921  27.198 1   61.65  ? 360 ARG   B O   1 
ATOM   5373  C  CB  . ARG   B 1 338 ? 15.873 54.834  28.818 1   60.88  ? 360 ARG   B CB  1 
ATOM   5374  C  CG  . ARG   B 1 338 ? 16.963 55.76   29.325 1   63.41  ? 360 ARG   B CG  1 
ATOM   5375  C  CD  . ARG   B 1 338 ? 16.776 56.091  30.802 1   64.26  ? 360 ARG   B CD  1 
ATOM   5376  N  NE  . ARG   B 1 338 ? 17.808 56.993  31.32  1   63.99  ? 360 ARG   B NE  1 
ATOM   5377  C  CZ  . ARG   B 1 338 ? 19.005 56.597  31.736 1   65.4   ? 360 ARG   B CZ  1 
ATOM   5378  N  NH1 . ARG   B 1 338 ? 19.348 55.316  31.676 1   65.55  ? 360 ARG   B NH1 1 
ATOM   5379  N  NH2 . ARG   B 1 338 ? 19.875 57.48   32.206 1   65.22  ? 360 ARG   B NH2 1 
ATOM   5380  N  N   . GLU   B 1 339 ? 13.941 53.547  26.718 1   61.97  ? 361 GLU   B N   1 
ATOM   5381  C  CA  . GLU   B 1 339 ? 12.823 52.674  26.379 1   63.11  ? 361 GLU   B CA  1 
ATOM   5382  C  C   . GLU   B 1 339 ? 13.006 51.903  25.055 1   63.4   ? 361 GLU   B C   1 
ATOM   5383  O  O   . GLU   B 1 339 ? 12.295 50.933  24.811 1   63.54  ? 361 GLU   B O   1 
ATOM   5384  C  CB  . GLU   B 1 339 ? 11.515 53.475  26.386 1   66.36  ? 361 GLU   B CB  1 
ATOM   5385  C  CG  . GLU   B 1 339 ? 11.414 54.498  25.266 1   73.33  ? 361 GLU   B CG  1 
ATOM   5386  C  CD  . GLU   B 1 339 ? 11.976 55.884  25.53  1   81.91  ? 361 GLU   B CD  1 
ATOM   5387  O  OE1 . GLU   B 1 339 ? 12.696 56.069  26.541 1   82.06  ? 361 GLU   B OE1 1 
ATOM   5388  O  OE2 . GLU   B 1 339 ? 11.695 56.788  24.707 1   85.63  ? 361 GLU   B OE2 1 
ATOM   5389  N  N   . ALA   B 1 340 ? 13.958 52.319  24.214 1   63.5   ? 362 ALA   B N   1 
ATOM   5390  C  CA  . ALA   B 1 340 ? 14.257 51.632  22.957 1   63.97  ? 362 ALA   B CA  1 
ATOM   5391  C  C   . ALA   B 1 340 ? 15.366 50.586  23.139 1   64.38  ? 362 ALA   B C   1 
ATOM   5392  O  O   . ALA   B 1 340 ? 15.406 49.634  22.377 1   64.5   ? 362 ALA   B O   1 
ATOM   5393  C  CB  . ALA   B 1 340 ? 14.656 52.637  21.887 1   64.07  ? 362 ALA   B CB  1 
ATOM   5394  N  N   . ILE   B 1 341 ? 16.255 50.751  24.138 1   64.62  ? 363 ILE   B N   1 
ATOM   5395  C  CA  . ILE   B 1 341 ? 17.351 49.815  24.412 1   65.35  ? 363 ILE   B CA  1 
ATOM   5396  C  C   . ILE   B 1 341 ? 16.837 48.461  24.922 1   66.76  ? 363 ILE   B C   1 
ATOM   5397  O  O   . ILE   B 1 341 ? 16.007 48.43   25.834 1   66.81  ? 363 ILE   B O   1 
ATOM   5398  C  CB  . ILE   B 1 341 ? 18.363 50.456  25.409 1   65.07  ? 363 ILE   B CB  1 
ATOM   5399  C  CG1 . ILE   B 1 341 ? 18.995 51.72   24.815 1   65.26  ? 363 ILE   B CG1 1 
ATOM   5400  C  CG2 . ILE   B 1 341 ? 19.437 49.456  25.837 1   65.34  ? 363 ILE   B CG2 1 
ATOM   5401  C  CD1 . ILE   B 1 341 ? 19.862 52.476  25.724 1   65.85  ? 363 ILE   B CD1 1 
ATOM   5402  N  N   . PRO   B 1 342 ? 17.307 47.332  24.34  1   67.88  ? 364 PRO   B N   1 
ATOM   5403  C  CA  . PRO   B 1 342 ? 16.853 46.008  24.824 1   69.01  ? 364 PRO   B CA  1 
ATOM   5404  C  C   . PRO   B 1 342 ? 17.231 45.739  26.289 1   70.56  ? 364 PRO   B C   1 
ATOM   5405  O  O   . PRO   B 1 342 ? 18.384 45.908  26.672 1   70.64  ? 364 PRO   B O   1 
ATOM   5406  C  CB  . PRO   B 1 342 ? 17.528 45.016  23.863 1   69.13  ? 364 PRO   B CB  1 
ATOM   5407  C  CG  . PRO   B 1 342 ? 18.668 45.761  23.264 1   69.1   ? 364 PRO   B CG  1 
ATOM   5408  C  CD  . PRO   B 1 342 ? 18.276 47.21   23.234 1   67.34  ? 364 PRO   B CD  1 
ATOM   5409  N  N   . PRO   B 1 343 ? 16.259 45.356  27.132 1   71.6   ? 365 PRO   B N   1 
ATOM   5410  C  CA  . PRO   B 1 343 ? 16.559 45.142  28.554 1   72.8   ? 365 PRO   B CA  1 
ATOM   5411  C  C   . PRO   B 1 343 ? 17.437 43.932  28.852 1   74.68  ? 365 PRO   B C   1 
ATOM   5412  O  O   . PRO   B 1 343 ? 17.376 42.928  28.147 1   74.74  ? 365 PRO   B O   1 
ATOM   5413  C  CB  . PRO   B 1 343 ? 15.173 44.992  29.194 1   73.04  ? 365 PRO   B CB  1 
ATOM   5414  C  CG  . PRO   B 1 343 ? 14.199 45.454  28.167 1   73.14  ? 365 PRO   B CG  1 
ATOM   5415  C  CD  . PRO   B 1 343 ? 14.829 45.157  26.853 1   71.35  ? 365 PRO   B CD  1 
ATOM   5416  N  N   . LEU   B 1 344 ? 18.25  44.039  29.911 1   76.03  ? 366 LEU   B N   1 
ATOM   5417  C  CA  . LEU   B 1 344 ? 19.159 42.983  30.339 1   78.24  ? 366 LEU   B CA  1 
ATOM   5418  C  C   . LEU   B 1 344 ? 18.404 41.797  30.967 1   81.15  ? 366 LEU   B C   1 
ATOM   5419  O  O   . LEU   B 1 344 ? 17.578 41.991  31.862 1   81.23  ? 366 LEU   B O   1 
ATOM   5420  C  CB  . LEU   B 1 344 ? 20.188 43.552  31.325 1   77.95  ? 366 LEU   B CB  1 
ATOM   5421  C  CG  . LEU   B 1 344 ? 21.35  44.314  30.705 1   78.66  ? 366 LEU   B CG  1 
ATOM   5422  C  CD1 . LEU   B 1 344 ? 22.225 44.924  31.774 1   78.84  ? 366 LEU   B CD1 1 
ATOM   5423  C  CD2 . LEU   B 1 344 ? 22.181 43.407  29.831 1   79.11  ? 366 LEU   B CD2 1 
ATOM   5424  N  N   . ASP   B 1 345 ? 18.674 40.571  30.483 1   83.17  ? 367 ASP   B N   1 
ATOM   5425  C  CA  . ASP   B 1 345 ? 18.003 39.363  30.979 1   85.44  ? 367 ASP   B CA  1 
ATOM   5426  C  C   . ASP   B 1 345 ? 18.932 38.471  31.822 1   87.33  ? 367 ASP   B C   1 
ATOM   5427  O  O   . ASP   B 1 345 ? 18.751 38.41   33.041 1   87.86  ? 367 ASP   B O   1 
ATOM   5428  C  CB  . ASP   B 1 345 ? 17.333 38.577  29.833 1   87.47  ? 367 ASP   B CB  1 
ATOM   5429  C  CG  . ASP   B 1 345 ? 16.153 39.291  29.206 1   92.6   ? 367 ASP   B CG  1 
ATOM   5430  O  OD1 . ASP   B 1 345 ? 15.469 40.066  29.927 1   93.42  ? 367 ASP   B OD1 1 
ATOM   5431  O  OD2 . ASP   B 1 345 ? 15.901 39.07   28.001 1   94.92  ? 367 ASP   B OD2 1 
ATOM   5432  N  N   . GLU   B 1 346 ? 19.941 37.822  31.189 1   88.04  ? 368 GLU   B N   1 
ATOM   5433  C  CA  . GLU   B 1 346 ? 20.93  36.953  31.849 1   89.09  ? 368 GLU   B CA  1 
ATOM   5434  C  C   . GLU   B 1 346 ? 20.312 35.948  32.836 1   89.61  ? 368 GLU   B C   1 
ATOM   5435  O  O   . GLU   B 1 346 ? 20.702 34.782  32.88  1   89.86  ? 368 GLU   B O   1 
ATOM   5436  C  CB  . GLU   B 1 346 ? 22.044 37.777  32.535 1   91.58  ? 368 GLU   B CB  1 
ATOM   5437  C  CG  . GLU   B 1 346 ? 22.496 39.022  31.781 1   96.73  ? 368 GLU   B CG  1 
ATOM   5438  C  CD  . GLU   B 1 346 ? 23.363 38.831  30.551 1   102.54 ? 368 GLU   B CD  1 
ATOM   5439  O  OE1 . GLU   B 1 346 ? 23.817 39.857  29.995 1   102.74 ? 368 GLU   B OE1 1 
ATOM   5440  O  OE2 . GLU   B 1 346 ? 23.6   37.668  30.149 1   105    ? 368 GLU   B OE2 1 
ATOM   5441  N  N   . ILE   C 1 4   ? 72.135 67.283  23.033 1   50.1   ? 26  ILE   C N   1 
ATOM   5442  C  CA  . ILE   C 1 4   ? 71.798 65.874  23.33  1   50.39  ? 26  ILE   C CA  1 
ATOM   5443  C  C   . ILE   C 1 4   ? 70.937 65.782  24.555 1   49.83  ? 26  ILE   C C   1 
ATOM   5444  O  O   . ILE   C 1 4   ? 71.464 65.787  25.657 1   50.23  ? 26  ILE   C O   1 
ATOM   5445  C  CB  . ILE   C 1 4   ? 72.989 64.898  23.427 1   51.53  ? 26  ILE   C CB  1 
ATOM   5446  C  CG1 . ILE   C 1 4   ? 74.328 65.646  23.798 1   52.76  ? 26  ILE   C CG1 1 
ATOM   5447  C  CG2 . ILE   C 1 4   ? 73.086 64.031  22.144 1   51.9   ? 26  ILE   C CG2 1 
ATOM   5448  C  CD1 . ILE   C 1 4   ? 75.659 64.891  23.641 1   54.16  ? 26  ILE   C CD1 1 
ATOM   5449  N  N   . TYR   C 1 5   ? 69.614 65.727  24.356 1   48.84  ? 27  TYR   C N   1 
ATOM   5450  C  CA  . TYR   C 1 5   ? 68.575 65.695  25.381 1   48.61  ? 27  TYR   C CA  1 
ATOM   5451  C  C   . TYR   C 1 5   ? 68.927 64.864  26.634 1   48.34  ? 27  TYR   C C   1 
ATOM   5452  O  O   . TYR   C 1 5   ? 68.91  65.41   27.737 1   47.89  ? 27  TYR   C O   1 
ATOM   5453  C  CB  . TYR   C 1 5   ? 67.239 65.232  24.76  1   48.65  ? 27  TYR   C CB  1 
ATOM   5454  C  CG  . TYR   C 1 5   ? 66.034 65.356  25.668 1   49.31  ? 27  TYR   C CG  1 
ATOM   5455  C  CD1 . TYR   C 1 5   ? 65.306 66.536  25.733 1   50.31  ? 27  TYR   C CD1 1 
ATOM   5456  C  CD2 . TYR   C 1 5   ? 65.571 64.268  26.392 1   50.26  ? 27  TYR   C CD2 1 
ATOM   5457  C  CE1 . TYR   C 1 5   ? 64.184 66.649  26.546 1   51.23  ? 27  TYR   C CE1 1 
ATOM   5458  C  CE2 . TYR   C 1 5   ? 64.453 64.369  27.212 1   51.35  ? 27  TYR   C CE2 1 
ATOM   5459  C  CZ  . TYR   C 1 5   ? 63.753 65.557  27.273 1   52.14  ? 27  TYR   C CZ  1 
ATOM   5460  O  OH  . TYR   C 1 5   ? 62.649 65.657  28.076 1   53.54  ? 27  TYR   C OH  1 
ATOM   5461  N  N   . GLY   C 1 6   ? 69.24  63.575  26.454 1   48.16  ? 28  GLY   C N   1 
ATOM   5462  C  CA  . GLY   C 1 6   ? 69.558 62.672  27.555 1   48.06  ? 28  GLY   C CA  1 
ATOM   5463  C  C   . GLY   C 1 6   ? 70.819 63.025  28.299 1   47.96  ? 28  GLY   C C   1 
ATOM   5464  O  O   . GLY   C 1 6   ? 70.915 62.827  29.515 1   48.75  ? 28  GLY   C O   1 
ATOM   5465  N  N   . GLU   C 1 7   ? 71.791 63.552  27.578 1   47.42  ? 29  GLU   C N   1 
ATOM   5466  C  CA  . GLU   C 1 7   ? 73.054 63.951  28.172 1   47.83  ? 29  GLU   C CA  1 
ATOM   5467  C  C   . GLU   C 1 7   ? 72.943 65.298  28.883 1   46.94  ? 29  GLU   C C   1 
ATOM   5468  O  O   . GLU   C 1 7   ? 73.511 65.467  29.958 1   46.97  ? 29  GLU   C O   1 
ATOM   5469  C  CB  . GLU   C 1 7   ? 74.168 63.94   27.124 1   51.19  ? 29  GLU   C CB  1 
ATOM   5470  C  CG  . GLU   C 1 7   ? 74.921 62.621  27.139 1   58.86  ? 29  GLU   C CG  1 
ATOM   5471  C  CD  . GLU   C 1 7   ? 75.378 62.117  25.785 1   68.77  ? 29  GLU   C CD  1 
ATOM   5472  O  OE1 . GLU   C 1 7   ? 74.53  62.044  24.865 1   70.85  ? 29  GLU   C OE1 1 
ATOM   5473  O  OE2 . GLU   C 1 7   ? 76.585 61.807  25.639 1   71.95  ? 29  GLU   C OE2 1 
ATOM   5474  N  N   . TYR   C 1 8   ? 72.176 66.229  28.308 1   45.88  ? 30  TYR   C N   1 
ATOM   5475  C  CA  . TYR   C 1 8   ? 71.95  67.554  28.86  1   45.45  ? 30  TYR   C CA  1 
ATOM   5476  C  C   . TYR   C 1 8   ? 71.232 67.437  30.197 1   44.94  ? 30  TYR   C C   1 
ATOM   5477  O  O   . TYR   C 1 8   ? 71.682 67.99   31.204 1   45.06  ? 30  TYR   C O   1 
ATOM   5478  C  CB  . TYR   C 1 8   ? 71.134 68.42   27.873 1   45.23  ? 30  TYR   C CB  1 
ATOM   5479  C  CG  . TYR   C 1 8   ? 70.784 69.779  28.438 1   45.6   ? 30  TYR   C CG  1 
ATOM   5480  C  CD1 . TYR   C 1 8   ? 71.759 70.747  28.623 1   45.98  ? 30  TYR   C CD1 1 
ATOM   5481  C  CD2 . TYR   C 1 8   ? 69.49  70.074  28.845 1   46.21  ? 30  TYR   C CD2 1 
ATOM   5482  C  CE1 . TYR   C 1 8   ? 71.452 71.986  29.161 1   46.42  ? 30  TYR   C CE1 1 
ATOM   5483  C  CE2 . TYR   C 1 8   ? 69.174 71.309  29.398 1   46.82  ? 30  TYR   C CE2 1 
ATOM   5484  C  CZ  . TYR   C 1 8   ? 70.159 72.267  29.541 1   47.51  ? 30  TYR   C CZ  1 
ATOM   5485  O  OH  . TYR   C 1 8   ? 69.866 73.504  30.06  1   49.36  ? 30  TYR   C OH  1 
ATOM   5486  N  N   . LEU   C 1 9   ? 70.135 66.691  30.212 1   44.41  ? 31  LEU   C N   1 
ATOM   5487  C  CA  . LEU   C 1 9   ? 69.361 66.494  31.426 1   44.38  ? 31  LEU   C CA  1 
ATOM   5488  C  C   . LEU   C 1 9   ? 69.919 65.436  32.347 1   45.02  ? 31  LEU   C C   1 
ATOM   5489  O  O   . LEU   C 1 9   ? 69.335 65.235  33.401 1   45.52  ? 31  LEU   C O   1 
ATOM   5490  C  CB  . LEU   C 1 9   ? 67.908 66.17   31.09  1   44.02  ? 31  LEU   C CB  1 
ATOM   5491  C  CG  . LEU   C 1 9   ? 67.186 67.22   30.291 1   44.57  ? 31  LEU   C CG  1 
ATOM   5492  C  CD1 . LEU   C 1 9   ? 65.86  66.7    29.839 1   44.87  ? 31  LEU   C CD1 1 
ATOM   5493  C  CD2 . LEU   C 1 9   ? 67.033 68.498  31.091 1   45.1   ? 31  LEU   C CD2 1 
ATOM   5494  N  N   . MET   C 1 10  ? 71.014 64.738  31.959 1   45.01  ? 32  MET   C N   1 
ATOM   5495  C  CA  . MET   C 1 10  ? 71.687 63.698  32.741 1   45.12  ? 32  MET   C CA  1 
ATOM   5496  C  C   . MET   C 1 10  ? 70.713 62.653  33.217 1   45.59  ? 32  MET   C C   1 
ATOM   5497  O  O   . MET   C 1 10  ? 70.618 62.364  34.405 1   45.37  ? 32  MET   C O   1 
ATOM   5498  C  CB  . MET   C 1 10  ? 72.502 64.298  33.892 1   45.26  ? 32  MET   C CB  1 
ATOM   5499  C  CG  . MET   C 1 10  ? 73.607 65.204  33.406 1   46.17  ? 32  MET   C CG  1 
ATOM   5500  S  SD  . MET   C 1 10  ? 74.459 66.062  34.736 1   44.82  ? 32  MET   C SD  1 
ATOM   5501  C  CE  . MET   C 1 10  ? 75.36  64.718  35.451 1   43.99  ? 32  MET   C CE  1 
ATOM   5502  N  N   . LEU   C 1 11  ? 69.946 62.134  32.267 1   46.13  ? 33  LEU   C N   1 
ATOM   5503  C  CA  . LEU   C 1 11  ? 68.932 61.13   32.538 1   46.72  ? 33  LEU   C CA  1 
ATOM   5504  C  C   . LEU   C 1 11  ? 69.539 59.78   32.953 1   47.53  ? 33  LEU   C C   1 
ATOM   5505  O  O   . LEU   C 1 11  ? 68.852 58.977  33.571 1   47.15  ? 33  LEU   C O   1 
ATOM   5506  C  CB  . LEU   C 1 11  ? 67.975 61.016  31.342 1   46.53  ? 33  LEU   C CB  1 
ATOM   5507  C  CG  . LEU   C 1 11  ? 67.308 62.335  30.926 1   47.27  ? 33  LEU   C CG  1 
ATOM   5508  C  CD1 . LEU   C 1 11  ? 66.5   62.165  29.642 1   47.51  ? 33  LEU   C CD1 1 
ATOM   5509  C  CD2 . LEU   C 1 11  ? 66.436 62.893  32.05  1   47.35  ? 33  LEU   C CD2 1 
ATOM   5510  N  N   . ASP   C 1 12  ? 70.83  59.531  32.649 1   48.52  ? 34  ASP   C N   1 
ATOM   5511  C  CA  . ASP   C 1 12  ? 71.485 58.292  33.107 1   49.55  ? 34  ASP   C CA  1 
ATOM   5512  C  C   . ASP   C 1 12  ? 71.816 58.333  34.624 1   48.54  ? 34  ASP   C C   1 
ATOM   5513  O  O   . ASP   C 1 12  ? 72.073 57.303  35.241 1   48.38  ? 34  ASP   C O   1 
ATOM   5514  C  CB  . ASP   C 1 12  ? 72.713 57.951  32.251 1   53.23  ? 34  ASP   C CB  1 
ATOM   5515  C  CG  . ASP   C 1 12  ? 72.343 57.354  30.886 1   61.57  ? 34  ASP   C CG  1 
ATOM   5516  O  OD1 . ASP   C 1 12  ? 71.303 56.644  30.803 1   62.9   ? 34  ASP   C OD1 1 
ATOM   5517  O  OD2 . ASP   C 1 12  ? 73.096 57.591  29.902 1   64.47  ? 34  ASP   C OD2 1 
ATOM   5518  N  N   . LYS   C 1 13  ? 71.776 59.527  35.22  1   47.55  ? 35  LYS   C N   1 
ATOM   5519  C  CA  . LYS   C 1 13  ? 71.991 59.761  36.629 1   46.9   ? 35  LYS   C CA  1 
ATOM   5520  C  C   . LYS   C 1 13  ? 70.61  59.897  37.303 1   45.7   ? 35  LYS   C C   1 
ATOM   5521  O  O   . LYS   C 1 13  ? 70.348 59.251  38.32  1   45.66  ? 35  LYS   C O   1 
ATOM   5522  C  CB  . LYS   C 1 13  ? 72.794 61.058  36.779 1   49.47  ? 35  LYS   C CB  1 
ATOM   5523  C  CG  . LYS   C 1 13  ? 73.574 61.173  38.054 1   54.34  ? 35  LYS   C CG  1 
ATOM   5524  C  CD  . LYS   C 1 13  ? 74.895 61.777  37.678 1   60.43  ? 35  LYS   C CD  1 
ATOM   5525  C  CE  . LYS   C 1 13  ? 75.332 62.808  38.673 1   65.98  ? 35  LYS   C CE  1 
ATOM   5526  N  NZ  . LYS   C 1 13  ? 76.478 63.63   38.186 1   69.05  ? 35  LYS   C NZ  1 
ATOM   5527  N  N   . LEU   C 1 14  ? 69.717 60.708  36.702 1   44.7   ? 36  LEU   C N   1 
ATOM   5528  C  CA  . LEU   C 1 14  ? 68.365 60.975  37.201 1   44.37  ? 36  LEU   C CA  1 
ATOM   5529  C  C   . LEU   C 1 14  ? 67.48  59.744  37.183 1   44.35  ? 36  LEU   C C   1 
ATOM   5530  O  O   . LEU   C 1 14  ? 66.854 59.432  38.201 1   44.34  ? 36  LEU   C O   1 
ATOM   5531  C  CB  . LEU   C 1 14  ? 67.7   62.113  36.395 1   44.08  ? 36  LEU   C CB  1 
ATOM   5532  C  CG  . LEU   C 1 14  ? 66.341 62.573  36.902 1   44.25  ? 36  LEU   C CG  1 
ATOM   5533  C  CD1 . LEU   C 1 14  ? 66.492 63.725  37.835 1   44.66  ? 36  LEU   C CD1 1 
ATOM   5534  C  CD2 . LEU   C 1 14  ? 65.458 62.945  35.771 1   44.15  ? 36  LEU   C CD2 1 
ATOM   5535  N  N   . LEU   C 1 15  ? 67.418 59.048  36.029 1   44.07  ? 37  LEU   C N   1 
ATOM   5536  C  CA  . LEU   C 1 15  ? 66.603 57.843  35.874 1   44.32  ? 37  LEU   C CA  1 
ATOM   5537  C  C   . LEU   C 1 15  ? 67.284 56.566  36.398 1   45.44  ? 37  LEU   C C   1 
ATOM   5538  O  O   . LEU   C 1 15  ? 66.808 55.459  36.144 1   45.94  ? 37  LEU   C O   1 
ATOM   5539  C  CB  . LEU   C 1 15  ? 66.105 57.662  34.427 1   43.93  ? 37  LEU   C CB  1 
ATOM   5540  C  CG  . LEU   C 1 15  ? 64.829 58.421  33.934 1   44.61  ? 37  LEU   C CG  1 
ATOM   5541  C  CD1 . LEU   C 1 15  ? 64.195 59.352  34.985 1   44.83  ? 37  LEU   C CD1 1 
ATOM   5542  C  CD2 . LEU   C 1 15  ? 65.103 59.175  32.665 1   44.93  ? 37  LEU   C CD2 1 
ATOM   5543  N  N   . ASP   C 1 16  ? 68.328 56.724  37.213 1   45.54  ? 38  ASP   C N   1 
ATOM   5544  C  CA  . ASP   C 1 16  ? 69.011 55.622  37.878 1   46.01  ? 38  ASP   C CA  1 
ATOM   5545  C  C   . ASP   C 1 16  ? 68.811 55.687  39.421 1   45.26  ? 38  ASP   C C   1 
ATOM   5546  O  O   . ASP   C 1 16  ? 69.276 54.779  40.116 1   45.91  ? 38  ASP   C O   1 
ATOM   5547  C  CB  . ASP   C 1 16  ? 70.512 55.655  37.529 1   48.91  ? 38  ASP   C CB  1 
ATOM   5548  C  CG  . ASP   C 1 16  ? 71.283 54.367  37.762 1   55.35  ? 38  ASP   C CG  1 
ATOM   5549  O  OD1 . ASP   C 1 16  ? 70.751 53.287  37.42  1   56.48  ? 38  ASP   C OD1 1 
ATOM   5550  O  OD2 . ASP   C 1 16  ? 72.44  54.444  38.262 1   57.55  ? 38  ASP   C OD2 1 
ATOM   5551  N  N   . ALA   C 1 17  ? 68.111 56.74   39.947 1   43.43  ? 39  ALA   C N   1 
ATOM   5552  C  CA  . ALA   C 1 17  ? 67.876 56.939  41.369 1   42.25  ? 39  ALA   C CA  1 
ATOM   5553  C  C   . ALA   C 1 17  ? 66.605 56.278  41.886 1   41.29  ? 39  ALA   C C   1 
ATOM   5554  O  O   . ALA   C 1 17  ? 66.217 56.561  43.02  1   41.75  ? 39  ALA   C O   1 
ATOM   5555  C  CB  . ALA   C 1 17  ? 67.87  58.428  41.698 1   41.94  ? 39  ALA   C CB  1 
ATOM   5556  N  N   . GLN   C 1 18  ? 65.971 55.38   41.111 1   40.05  ? 40  GLN   C N   1 
ATOM   5557  C  CA  . GLN   C 1 18  ? 64.726 54.741  41.568 1   39.64  ? 40  GLN   C CA  1 
ATOM   5558  C  C   . GLN   C 1 18  ? 64.903 53.293  41.969 1   40.13  ? 40  GLN   C C   1 
ATOM   5559  O  O   . GLN   C 1 18  ? 65.039 52.423  41.107 1   40.38  ? 40  GLN   C O   1 
ATOM   5560  C  CB  . GLN   C 1 18  ? 63.606 54.891  40.54  1   39.75  ? 40  GLN   C CB  1 
ATOM   5561  C  CG  . GLN   C 1 18  ? 63.242 56.338  40.243 1   40.46  ? 40  GLN   C CG  1 
ATOM   5562  C  CD  . GLN   C 1 18  ? 64.25  56.975  39.316 1   42.69  ? 40  GLN   C CD  1 
ATOM   5563  O  OE1 . GLN   C 1 18  ? 64.794 56.327  38.424 1   43.8   ? 40  GLN   C OE1 1 
ATOM   5564  N  NE2 . GLN   C 1 18  ? 64.557 58.245  39.525 1   42.67  ? 40  GLN   C NE2 1 
ATOM   5565  N  N   . CYS   C 1 19  ? 64.89  53.027  43.276 1   40.46  ? 41  CYS   C N   1 
ATOM   5566  C  CA  . CYS   C 1 19  ? 65.107 51.675  43.766 1   42.01  ? 41  CYS   C CA  1 
ATOM   5567  C  C   . CYS   C 1 19  ? 64.101 51.218  44.808 1   42.69  ? 41  CYS   C C   1 
ATOM   5568  O  O   . CYS   C 1 19  ? 64.195 51.596  45.983 1   42.88  ? 41  CYS   C O   1 
ATOM   5569  C  CB  . CYS   C 1 19  ? 66.539 51.512  44.27  1   44.1   ? 41  CYS   C CB  1 
ATOM   5570  S  SG  . CYS   C 1 19  ? 66.931 49.851  44.883 1   50.73  ? 41  CYS   C SG  1 
ATOM   5571  N  N   . MET   C 1 20  ? 63.18  50.341  44.383 1   42.91  ? 42  MET   C N   1 
ATOM   5572  C  CA  . MET   C 1 20  ? 62.166 49.737  45.239 1   43.13  ? 42  MET   C CA  1 
ATOM   5573  C  C   . MET   C 1 20  ? 62.775 48.663  46.13  1   44.05  ? 42  MET   C C   1 
ATOM   5574  O  O   . MET   C 1 20  ? 63.272 47.654  45.632 1   44.02  ? 42  MET   C O   1 
ATOM   5575  C  CB  . MET   C 1 20  ? 61.059 49.108  44.389 1   42.77  ? 42  MET   C CB  1 
ATOM   5576  C  CG  . MET   C 1 20  ? 60.184 50.123  43.721 1   43.87  ? 42  MET   C CG  1 
ATOM   5577  S  SD  . MET   C 1 20  ? 59.162 49.436  42.399 1   44.98  ? 42  MET   C SD  1 
ATOM   5578  C  CE  . MET   C 1 20  ? 58.306 48.141  43.26  1   39.86  ? 42  MET   C CE  1 
ATOM   5579  N  N   . LEU   C 1 21  ? 62.727 48.868  47.451 1   44.75  ? 43  LEU   C N   1 
ATOM   5580  C  CA  . LEU   C 1 21  ? 63.228 47.899  48.421 1   45.49  ? 43  LEU   C CA  1 
ATOM   5581  C  C   . LEU   C 1 21  ? 62.298 46.702  48.599 1   47.35  ? 43  LEU   C C   1 
ATOM   5582  O  O   . LEU   C 1 21  ? 62.742 45.66   49.086 1   47.77  ? 43  LEU   C O   1 
ATOM   5583  C  CB  . LEU   C 1 21  ? 63.523 48.569  49.759 1   45.03  ? 43  LEU   C CB  1 
ATOM   5584  C  CG  . LEU   C 1 21  ? 64.452 49.765  49.678 1   45.51  ? 43  LEU   C CG  1 
ATOM   5585  C  CD1 . LEU   C 1 21  ? 64.603 50.431  51.023 1   45.66  ? 43  LEU   C CD1 1 
ATOM   5586  C  CD2 . LEU   C 1 21  ? 65.791 49.386  49.065 1   45.69  ? 43  LEU   C CD2 1 
ATOM   5587  N  N   . SER   C 1 22  ? 61.023 46.824  48.196 1   48.36  ? 44  SER   C N   1 
ATOM   5588  C  CA  . SER   C 1 22  ? 60.097 45.697  48.235 1   49.96  ? 44  SER   C CA  1 
ATOM   5589  C  C   . SER   C 1 22  ? 60.472 44.717  47.105 1   51.71  ? 44  SER   C C   1 
ATOM   5590  O  O   . SER   C 1 22  ? 60.468 43.507  47.315 1   51.54  ? 44  SER   C O   1 
ATOM   5591  C  CB  . SER   C 1 22  ? 58.654 46.172  48.081 1   50.82  ? 44  SER   C CB  1 
ATOM   5592  O  OG  . SER   C 1 22  ? 58.423 46.772  46.816 1   51.96  ? 44  SER   C OG  1 
ATOM   5593  N  N   . GLU   C 1 23  ? 60.835 45.244  45.925 1   53.31  ? 45  GLU   C N   1 
ATOM   5594  C  CA  . GLU   C 1 23  ? 61.267 44.449  44.781 1   55.37  ? 45  GLU   C CA  1 
ATOM   5595  C  C   . GLU   C 1 23  ? 62.608 43.737  45.1   1   56.98  ? 45  GLU   C C   1 
ATOM   5596  O  O   . GLU   C 1 23  ? 62.797 42.571  44.732 1   57.05  ? 45  GLU   C O   1 
ATOM   5597  C  CB  . GLU   C 1 23  ? 61.393 45.367  43.558 1   58.23  ? 45  GLU   C CB  1 
ATOM   5598  C  CG  . GLU   C 1 23  ? 61.549 44.636  42.239 1   65.64  ? 45  GLU   C CG  1 
ATOM   5599  C  CD  . GLU   C 1 23  ? 61.654 45.585  41.06  1   76.98  ? 45  GLU   C CD  1 
ATOM   5600  O  OE1 . GLU   C 1 23  ? 62.301 46.651  41.207 1   79.68  ? 45  GLU   C OE1 1 
ATOM   5601  O  OE2 . GLU   C 1 23  ? 61.08  45.267  39.991 1   80.74  ? 45  GLU   C OE2 1 
ATOM   5602  N  N   . GLU   C 1 24  ? 63.514 44.449  45.81  1   58.07  ? 46  GLU   C N   1 
ATOM   5603  C  CA  . GLU   C 1 24  ? 64.821 43.979  46.284 1   59.87  ? 46  GLU   C CA  1 
ATOM   5604  C  C   . GLU   C 1 24  ? 64.628 42.792  47.249 1   60.84  ? 46  GLU   C C   1 
ATOM   5605  O  O   . GLU   C 1 24  ? 65.336 41.792  47.149 1   61.6   ? 46  GLU   C O   1 
ATOM   5606  C  CB  . GLU   C 1 24  ? 65.577 45.146  46.98  1   63.53  ? 46  GLU   C CB  1 
ATOM   5607  C  CG  . GLU   C 1 24  ? 66.743 44.769  47.893 1   71.49  ? 46  GLU   C CG  1 
ATOM   5608  C  CD  . GLU   C 1 24  ? 66.478 44.762  49.397 1   83.81  ? 46  GLU   C CD  1 
ATOM   5609  O  OE1 . GLU   C 1 24  ? 65.513 45.424  49.849 1   86.42  ? 46  GLU   C OE1 1 
ATOM   5610  O  OE2 . GLU   C 1 24  ? 67.231 44.07   50.123 1   87.47  ? 46  GLU   C OE2 1 
ATOM   5611  N  N   . ASP   C 1 25  ? 63.648 42.885  48.156 1   60.66  ? 47  ASP   C N   1 
ATOM   5612  C  CA  . ASP   C 1 25  ? 63.367 41.816  49.114 1   61.08  ? 47  ASP   C CA  1 
ATOM   5613  C  C   . ASP   C 1 25  ? 62.474 40.703  48.547 1   60.97  ? 47  ASP   C C   1 
ATOM   5614  O  O   . ASP   C 1 25  ? 61.975 39.879  49.317 1   61.37  ? 47  ASP   C O   1 
ATOM   5615  C  CB  . ASP   C 1 25  ? 62.722 42.397  50.372 1   63.45  ? 47  ASP   C CB  1 
ATOM   5616  C  CG  . ASP   C 1 25  ? 63.196 41.765  51.668 1   68.65  ? 47  ASP   C CG  1 
ATOM   5617  O  OD1 . ASP   C 1 25  ? 64.431 41.716  51.89  1   69.78  ? 47  ASP   C OD1 1 
ATOM   5618  O  OD2 . ASP   C 1 25  ? 62.334 41.339  52.467 1   70.69  ? 47  ASP   C OD2 1 
ATOM   5619  N  N   . LYS   C 1 26  ? 62.276 40.686  47.214 1   60.28  ? 48  LYS   C N   1 
ATOM   5620  C  CA  . LYS   C 1 26  ? 61.493 39.722  46.454 1   60.44  ? 48  LYS   C CA  1 
ATOM   5621  C  C   . LYS   C 1 26  ? 60.014 39.672  46.845 1   60.19  ? 48  LYS   C C   1 
ATOM   5622  O  O   . LYS   C 1 26  ? 59.348 38.669  46.602 1   60.54  ? 48  LYS   C O   1 
ATOM   5623  C  CB  . LYS   C 1 26  ? 62.141 38.325  46.499 1   62.76  ? 48  LYS   C CB  1 
ATOM   5624  C  CG  . LYS   C 1 26  ? 63.489 38.244  45.76  1   67.51  ? 48  LYS   C CG  1 
ATOM   5625  C  CD  . LYS   C 1 26  ? 63.362 38.604  44.258 1   72.29  ? 48  LYS   C CD  1 
ATOM   5626  C  CE  . LYS   C 1 26  ? 64.691 38.866  43.581 1   75.66  ? 48  LYS   C CE  1 
ATOM   5627  N  NZ  . LYS   C 1 26  ? 64.506 39.507  42.246 1   77.73  ? 48  LYS   C NZ  1 
ATOM   5628  N  N   . ARG   C 1 27  ? 59.495 40.769  47.41  1   59.47  ? 49  ARG   C N   1 
ATOM   5629  C  CA  . ARG   C 1 27  ? 58.099 40.927  47.8   1   59.31  ? 49  ARG   C CA  1 
ATOM   5630  C  C   . ARG   C 1 27  ? 57.683 42.3    47.253 1   57.61  ? 49  ARG   C C   1 
ATOM   5631  O  O   . ARG   C 1 27  ? 57.57  43.258  48.025 1   58.05  ? 49  ARG   C O   1 
ATOM   5632  C  CB  . ARG   C 1 27  ? 57.986 40.922  49.338 1   62.35  ? 49  ARG   C CB  1 
ATOM   5633  C  CG  . ARG   C 1 27  ? 58.299 39.604  50.028 1   69.28  ? 49  ARG   C CG  1 
ATOM   5634  C  CD  . ARG   C 1 27  ? 58.514 39.786  51.528 1   76.03  ? 49  ARG   C CD  1 
ATOM   5635  N  NE  . ARG   C 1 27  ? 57.41  40.499  52.182 1   82.23  ? 49  ARG   C NE  1 
ATOM   5636  C  CZ  . ARG   C 1 27  ? 57.506 41.728  52.692 1   86.45  ? 49  ARG   C CZ  1 
ATOM   5637  N  NH1 . ARG   C 1 27  ? 58.659 42.388  52.641 1   86.94  ? 49  ARG   C NH1 1 
ATOM   5638  N  NH2 . ARG   C 1 27  ? 56.45  42.303  53.258 1   86.25  ? 49  ARG   C NH2 1 
ATOM   5639  N  N   . PRO   C 1 28  ? 57.539 42.465  45.922 1   55.51  ? 50  PRO   C N   1 
ATOM   5640  C  CA  . PRO   C 1 28  ? 57.27  43.811  45.386 1   53.97  ? 50  PRO   C CA  1 
ATOM   5641  C  C   . PRO   C 1 28  ? 55.852 44.357  45.574 1   52.91  ? 50  PRO   C C   1 
ATOM   5642  O  O   . PRO   C 1 28  ? 54.865 43.623  45.531 1   53.19  ? 50  PRO   C O   1 
ATOM   5643  C  CB  . PRO   C 1 28  ? 57.649 43.698  43.916 1   54.57  ? 50  PRO   C CB  1 
ATOM   5644  C  CG  . PRO   C 1 28  ? 57.537 42.27   43.594 1   55.43  ? 50  PRO   C CG  1 
ATOM   5645  C  CD  . PRO   C 1 28  ? 57.682 41.465  44.847 1   54.57  ? 50  PRO   C CD  1 
ATOM   5646  N  N   . VAL   C 1 29  ? 55.778 45.681  45.818 1   51.55  ? 51  VAL   C N   1 
ATOM   5647  C  CA  . VAL   C 1 29  ? 54.549 46.459  46.012 1   50.11  ? 51  VAL   C CA  1 
ATOM   5648  C  C   . VAL   C 1 29  ? 54.552 47.508  44.92  1   48.45  ? 51  VAL   C C   1 
ATOM   5649  O  O   . VAL   C 1 29  ? 55.385 48.406  44.955 1   48.87  ? 51  VAL   C O   1 
ATOM   5650  C  CB  . VAL   C 1 29  ? 54.496 47.138  47.405 1   50.25  ? 51  VAL   C CB  1 
ATOM   5651  C  CG1 . VAL   C 1 29  ? 53.185 47.892  47.596 1   50.5   ? 51  VAL   C CG1 1 
ATOM   5652  C  CG2 . VAL   C 1 29  ? 54.703 46.125  48.517 1   50.49  ? 51  VAL   C CG2 1 
ATOM   5653  N  N   . HIS   C 1 30  ? 53.65  47.384  43.947 1   46.59  ? 52  HIS   C N   1 
ATOM   5654  C  CA  . HIS   C 1 30  ? 53.552 48.273  42.795 1   45.53  ? 52  HIS   C CA  1 
ATOM   5655  C  C   . HIS   C 1 30  ? 53.532 49.782  43.126 1   44.88  ? 52  HIS   C C   1 
ATOM   5656  O  O   . HIS   C 1 30  ? 54.196 50.571  42.446 1   45.87  ? 52  HIS   C O   1 
ATOM   5657  C  CB  . HIS   C 1 30  ? 52.323 47.888  41.959 1   45.68  ? 52  HIS   C CB  1 
ATOM   5658  C  CG  . HIS   C 1 30  ? 52.216 48.629  40.671 1   46.47  ? 52  HIS   C CG  1 
ATOM   5659  N  ND1 . HIS   C 1 30  ? 51.47  49.792  40.566 1   48.16  ? 52  HIS   C ND1 1 
ATOM   5660  C  CD2 . HIS   C 1 30  ? 52.776 48.357  39.472 1   47.06  ? 52  HIS   C CD2 1 
ATOM   5661  C  CE1 . HIS   C 1 30  ? 51.606 50.193  39.314 1   48.24  ? 52  HIS   C CE1 1 
ATOM   5662  N  NE2 . HIS   C 1 30  ? 52.393 49.367  38.621 1   48.11  ? 52  HIS   C NE2 1 
ATOM   5663  N  N   . ASP   C 1 31  ? 52.78  50.182  44.168 1   42.91  ? 53  ASP   C N   1 
ATOM   5664  C  CA  . ASP   C 1 31  ? 52.671 51.587  44.543 1   41.11  ? 53  ASP   C CA  1 
ATOM   5665  C  C   . ASP   C 1 31  ? 53.95  52.179  45.18  1   39.7   ? 53  ASP   C C   1 
ATOM   5666  O  O   . ASP   C 1 31  ? 53.994 53.39   45.411 1   39.54  ? 53  ASP   C O   1 
ATOM   5667  C  CB  . ASP   C 1 31  ? 51.437 51.831  45.427 1   41.65  ? 53  ASP   C CB  1 
ATOM   5668  C  CG  . ASP   C 1 31  ? 50.096 51.706  44.705 1   45.2   ? 53  ASP   C CG  1 
ATOM   5669  O  OD1 . ASP   C 1 31  ? 50.099 51.492  43.47  1   46.31  ? 53  ASP   C OD1 1 
ATOM   5670  O  OD2 . ASP   C 1 31  ? 49.033 51.806  45.382 1   46.7   ? 53  ASP   C OD2 1 
ATOM   5671  N  N   . GLU   C 1 32  ? 54.998 51.362  45.419 1   38.36  ? 54  GLU   C N   1 
ATOM   5672  C  CA  . GLU   C 1 32  ? 56.252 51.884  45.971 1   37.37  ? 54  GLU   C CA  1 
ATOM   5673  C  C   . GLU   C 1 32  ? 56.974 52.777  44.952 1   37.89  ? 54  GLU   C C   1 
ATOM   5674  O  O   . GLU   C 1 32  ? 57.641 53.732  45.345 1   38.5   ? 54  GLU   C O   1 
ATOM   5675  C  CB  . GLU   C 1 32  ? 57.187 50.766  46.465 1   37.33  ? 54  GLU   C CB  1 
ATOM   5676  C  CG  . GLU   C 1 32  ? 58.431 51.326  47.137 1   39.3   ? 54  GLU   C CG  1 
ATOM   5677  C  CD  . GLU   C 1 32  ? 59.459 50.357  47.686 1   41.77  ? 54  GLU   C CD  1 
ATOM   5678  O  OE1 . GLU   C 1 32  ? 59.266 49.131  47.532 1   40.75  ? 54  GLU   C OE1 1 
ATOM   5679  O  OE2 . GLU   C 1 32  ? 60.467 50.824  48.267 1   42.69  ? 54  GLU   C OE2 1 
ATOM   5680  N  N   . HIS   C 1 33  ? 56.813 52.488  43.647 1   37.43  ? 55  HIS   C N   1 
ATOM   5681  C  CA  . HIS   C 1 33  ? 57.387 53.265  42.555 1   36.88  ? 55  HIS   C CA  1 
ATOM   5682  C  C   . HIS   C 1 33  ? 56.804 54.697  42.604 1   36.48  ? 55  HIS   C C   1 
ATOM   5683  O  O   . HIS   C 1 33  ? 57.54  55.677  42.42  1   36.74  ? 55  HIS   C O   1 
ATOM   5684  C  CB  . HIS   C 1 33  ? 57.032 52.587  41.218 1   37.23  ? 55  HIS   C CB  1 
ATOM   5685  C  CG  . HIS   C 1 33  ? 57.888 52.998  40.054 1   38.15  ? 55  HIS   C CG  1 
ATOM   5686  N  ND1 . HIS   C 1 33  ? 57.812 54.262  39.511 1   39.42  ? 55  HIS   C ND1 1 
ATOM   5687  C  CD2 . HIS   C 1 33  ? 58.787 52.278  39.35  1   39.08  ? 55  HIS   C CD2 1 
ATOM   5688  C  CE1 . HIS   C 1 33  ? 58.693 54.286  38.525 1   39.86  ? 55  HIS   C CE1 1 
ATOM   5689  N  NE2 . HIS   C 1 33  ? 59.29  53.109  38.377 1   39.79  ? 55  HIS   C NE2 1 
ATOM   5690  N  N   . LEU   C 1 34  ? 55.479 54.805  42.837 1   35.46  ? 56  LEU   C N   1 
ATOM   5691  C  CA  . LEU   C 1 34  ? 54.769 56.08   42.92  1   34.68  ? 56  LEU   C CA  1 
ATOM   5692  C  C   . LEU   C 1 34  ? 55.287 56.874  44.113 1   35.32  ? 56  LEU   C C   1 
ATOM   5693  O  O   . LEU   C 1 34  ? 55.548 58.063  43.986 1   35.2   ? 56  LEU   C O   1 
ATOM   5694  C  CB  . LEU   C 1 34  ? 53.255 55.832  43.051 1   33.79  ? 56  LEU   C CB  1 
ATOM   5695  C  CG  . LEU   C 1 34  ? 52.397 57.065  43.23  1   33.89  ? 56  LEU   C CG  1 
ATOM   5696  C  CD1 . LEU   C 1 34  ? 52.473 57.965  42.006 1   33.67  ? 56  LEU   C CD1 1 
ATOM   5697  C  CD2 . LEU   C 1 34  ? 50.964 56.693  43.61  1   34.1   ? 56  LEU   C CD2 1 
ATOM   5698  N  N   . PHE   C 1 35  ? 55.471 56.203  45.262 1   35.63  ? 57  PHE   C N   1 
ATOM   5699  C  CA  . PHE   C 1 35  ? 55.996 56.793  46.49  1   36.06  ? 57  PHE   C CA  1 
ATOM   5700  C  C   . PHE   C 1 35  ? 57.382 57.409  46.24  1   36.63  ? 57  PHE   C C   1 
ATOM   5701  O  O   . PHE   C 1 35  ? 57.64  58.525  46.684 1   36.48  ? 57  PHE   C O   1 
ATOM   5702  C  CB  . PHE   C 1 35  ? 56.072 55.716  47.596 1   35.98  ? 57  PHE   C CB  1 
ATOM   5703  C  CG  . PHE   C 1 35  ? 56.415 56.246  48.976 1   36.61  ? 57  PHE   C CG  1 
ATOM   5704  C  CD1 . PHE   C 1 35  ? 55.449 56.85   49.764 1   36.95  ? 57  PHE   C CD1 1 
ATOM   5705  C  CD2 . PHE   C 1 35  ? 57.703 56.124  49.487 1   37.02  ? 57  PHE   C CD2 1 
ATOM   5706  C  CE1 . PHE   C 1 35  ? 55.762 57.337  51.02  1   37.57  ? 57  PHE   C CE1 1 
ATOM   5707  C  CE2 . PHE   C 1 35  ? 58.015 56.62   50.742 1   37.73  ? 57  PHE   C CE2 1 
ATOM   5708  C  CZ  . PHE   C 1 35  ? 57.036 57.204  51.508 1   37.75  ? 57  PHE   C CZ  1 
ATOM   5709  N  N   . ILE   C 1 36  ? 58.266 56.692  45.509 1   37.03  ? 58  ILE   C N   1 
ATOM   5710  C  CA  . ILE   C 1 36  ? 59.611 57.182  45.214 1   37.82  ? 58  ILE   C CA  1 
ATOM   5711  C  C   . ILE   C 1 36  ? 59.579 58.359  44.25  1   38.6   ? 58  ILE   C C   1 
ATOM   5712  O  O   . ILE   C 1 36  ? 60.108 59.416  44.58  1   39.59  ? 58  ILE   C O   1 
ATOM   5713  C  CB  . ILE   C 1 36  ? 60.542 56.049  44.728 1   38.04  ? 58  ILE   C CB  1 
ATOM   5714  C  CG1 . ILE   C 1 36  ? 60.724 54.969  45.801 1   38.06  ? 58  ILE   C CG1 1 
ATOM   5715  C  CG2 . ILE   C 1 36  ? 61.891 56.614  44.222 1   38.54  ? 58  ILE   C CG2 1 
ATOM   5716  C  CD1 . ILE   C 1 36  ? 61.379 53.741  45.291 1   38.89  ? 58  ILE   C CD1 1 
ATOM   5717  N  N   . ILE   C 1 37  ? 58.943 58.188  43.085 1   38.12  ? 59  ILE   C N   1 
ATOM   5718  C  CA  . ILE   C 1 37  ? 58.807 59.244  42.083 1   38     ? 59  ILE   C CA  1 
ATOM   5719  C  C   . ILE   C 1 37  ? 58.153 60.513  42.655 1   37.88  ? 59  ILE   C C   1 
ATOM   5720  O  O   . ILE   C 1 37  ? 58.683 61.589  42.424 1   38.15  ? 59  ILE   C O   1 
ATOM   5721  C  CB  . ILE   C 1 37  ? 58.076 58.709  40.829 1   37.92  ? 59  ILE   C CB  1 
ATOM   5722  C  CG1 . ILE   C 1 37  ? 58.94  57.645  40.077 1   38.46  ? 59  ILE   C CG1 1 
ATOM   5723  C  CG2 . ILE   C 1 37  ? 57.588 59.848  39.908 1   37.62  ? 59  ILE   C CG2 1 
ATOM   5724  C  CD1 . ILE   C 1 37  ? 60.187 58.188  39.377 1   39.46  ? 59  ILE   C CD1 1 
ATOM   5725  N  N   . THR   C 1 38  ? 57.049 60.399  43.425 1   37.51  ? 60  THR   C N   1 
ATOM   5726  C  CA  . THR   C 1 38  ? 56.358 61.565  44.01  1   37.71  ? 60  THR   C CA  1 
ATOM   5727  C  C   . THR   C 1 38  ? 57.305 62.35   44.902 1   38.21  ? 60  THR   C C   1 
ATOM   5728  O  O   . THR   C 1 38  ? 57.368 63.569  44.807 1   38.76  ? 60  THR   C O   1 
ATOM   5729  C  CB  . THR   C 1 38  ? 55.105 61.163  44.832 1   38.44  ? 60  THR   C CB  1 
ATOM   5730  O  OG1 . THR   C 1 38  ? 54.219 60.383  44.048 1   38.84  ? 60  THR   C OG1 1 
ATOM   5731  C  CG2 . THR   C 1 38  ? 54.347 62.365  45.362 1   38.91  ? 60  THR   C CG2 1 
ATOM   5732  N  N   . HIS   C 1 39  ? 58.079 61.645  45.731 1   37.96  ? 61  HIS   C N   1 
ATOM   5733  C  CA  . HIS   C 1 39  ? 59.03  62.256  46.639 1   37.94  ? 61  HIS   C CA  1 
ATOM   5734  C  C   . HIS   C 1 39  ? 60.166 62.908  45.889 1   37.44  ? 61  HIS   C C   1 
ATOM   5735  O  O   . HIS   C 1 39  ? 60.594 63.992  46.258 1   38.26  ? 61  HIS   C O   1 
ATOM   5736  C  CB  . HIS   C 1 39  ? 59.544 61.232  47.658 1   39.46  ? 61  HIS   C CB  1 
ATOM   5737  C  CG  . HIS   C 1 39  ? 58.707 61.133  48.897 1   41.95  ? 61  HIS   C CG  1 
ATOM   5738  N  ND1 . HIS   C 1 39  ? 57.54  60.389  48.92  1   43.82  ? 61  HIS   C ND1 1 
ATOM   5739  C  CD2 . HIS   C 1 39  ? 58.892 61.697  50.114 1   43.37  ? 61  HIS   C CD2 1 
ATOM   5740  C  CE1 . HIS   C 1 39  ? 57.049 60.521  50.141 1   44.5   ? 61  HIS   C CE1 1 
ATOM   5741  N  NE2 . HIS   C 1 39  ? 57.826 61.3    50.898 1   44.53  ? 61  HIS   C NE2 1 
ATOM   5742  N  N   . GLN   C 1 40  ? 60.63  62.285  44.819 1   36.41  ? 62  GLN   C N   1 
ATOM   5743  C  CA  . GLN   C 1 40  ? 61.699 62.825  43.992 1   35.8   ? 62  GLN   C CA  1 
ATOM   5744  C  C   . GLN   C 1 40  ? 61.251 64.029  43.153 1   35.96  ? 62  GLN   C C   1 
ATOM   5745  O  O   . GLN   C 1 40  ? 62.06  64.899  42.842 1   35.68  ? 62  GLN   C O   1 
ATOM   5746  C  CB  . GLN   C 1 40  ? 62.256 61.724  43.106 1   35.75  ? 62  GLN   C CB  1 
ATOM   5747  C  CG  . GLN   C 1 40  ? 63.011 60.665  43.899 1   35.78  ? 62  GLN   C CG  1 
ATOM   5748  C  CD  . GLN   C 1 40  ? 63.542 59.573  43.008 1   37.39  ? 62  GLN   C CD  1 
ATOM   5749  O  OE1 . GLN   C 1 40  ? 63.051 59.341  41.906 1   39.4   ? 62  GLN   C OE1 1 
ATOM   5750  N  NE2 . GLN   C 1 40  ? 64.534 58.857  43.48  1   35.57  ? 62  GLN   C NE2 1 
ATOM   5751  N  N   . ALA   C 1 41  ? 59.969 64.078  42.784 1   36.23  ? 63  ALA   C N   1 
ATOM   5752  C  CA  . ALA   C 1 41  ? 59.399 65.221  42.08  1   36.71  ? 63  ALA   C CA  1 
ATOM   5753  C  C   . ALA   C 1 41  ? 59.362 66.394  43.062 1   37.35  ? 63  ALA   C C   1 
ATOM   5754  O  O   . ALA   C 1 41  ? 59.758 67.495  42.688 1   38.81  ? 63  ALA   C O   1 
ATOM   5755  C  CB  . ALA   C 1 41  ? 58.003 64.9    41.599 1   36.72  ? 63  ALA   C CB  1 
ATOM   5756  N  N   . TYR   C 1 42  ? 58.984 66.148  44.335 1   36.15  ? 64  TYR   C N   1 
ATOM   5757  C  CA  . TYR   C 1 42  ? 58.993 67.155  45.384 1   36.16  ? 64  TYR   C CA  1 
ATOM   5758  C  C   . TYR   C 1 42  ? 60.416 67.688  45.569 1   35.67  ? 64  TYR   C C   1 
ATOM   5759  O  O   . TYR   C 1 42  ? 60.605 68.893  45.558 1   36.32  ? 64  TYR   C O   1 
ATOM   5760  C  CB  . TYR   C 1 42  ? 58.503 66.565  46.737 1   36.27  ? 64  TYR   C CB  1 
ATOM   5761  C  CG  . TYR   C 1 42  ? 57.022 66.716  46.968 1   37.35  ? 64  TYR   C CG  1 
ATOM   5762  C  CD1 . TYR   C 1 42  ? 56.48  67.925  47.377 1   38.06  ? 64  TYR   C CD1 1 
ATOM   5763  C  CD2 . TYR   C 1 42  ? 56.16  65.647  46.781 1   38.9   ? 64  TYR   C CD2 1 
ATOM   5764  C  CE1 . TYR   C 1 42  ? 55.11  68.073  47.57  1   38.92  ? 64  TYR   C CE1 1 
ATOM   5765  C  CE2 . TYR   C 1 42  ? 54.789 65.785  46.955 1   39.78  ? 64  TYR   C CE2 1 
ATOM   5766  C  CZ  . TYR   C 1 42  ? 54.27  66.993  47.37  1   40.12  ? 64  TYR   C CZ  1 
ATOM   5767  O  OH  . TYR   C 1 42  ? 52.917 67.112  47.528 1   41.66  ? 64  TYR   C OH  1 
ATOM   5768  N  N   . GLU   C 1 43  ? 61.408 66.793  45.667 1   34.27  ? 65  GLU   C N   1 
ATOM   5769  C  CA  . GLU   C 1 43  ? 62.787 67.171  45.907 1   34.07  ? 65  GLU   C CA  1 
ATOM   5770  C  C   . GLU   C 1 43  ? 63.415 67.931  44.763 1   34.65  ? 65  GLU   C C   1 
ATOM   5771  O  O   . GLU   C 1 43  ? 64.31  68.75   45.008 1   34.6   ? 65  GLU   C O   1 
ATOM   5772  C  CB  . GLU   C 1 43  ? 63.632 65.958  46.298 1   34.59  ? 65  GLU   C CB  1 
ATOM   5773  C  CG  . GLU   C 1 43  ? 63.276 65.419  47.672 1   34.87  ? 65  GLU   C CG  1 
ATOM   5774  C  CD  . GLU   C 1 43  ? 63.656 66.284  48.86  1   35.99  ? 65  GLU   C CD  1 
ATOM   5775  O  OE1 . GLU   C 1 43  ? 64.744 66.902  48.838 1   37.05  ? 65  GLU   C OE1 1 
ATOM   5776  O  OE2 . GLU   C 1 43  ? 62.884 66.302  49.843 1   35.78  ? 65  GLU   C OE2 1 
ATOM   5777  N  N   . LEU   C 1 44  ? 62.955 67.687  43.522 1   34.56  ? 66  LEU   C N   1 
ATOM   5778  C  CA  . LEU   C 1 44  ? 63.469 68.426  42.384 1   35.4   ? 66  LEU   C CA  1 
ATOM   5779  C  C   . LEU   C 1 44  ? 62.954 69.866  42.491 1   36.19  ? 66  LEU   C C   1 
ATOM   5780  O  O   . LEU   C 1 44  ? 63.736 70.807  42.385 1   37.16  ? 66  LEU   C O   1 
ATOM   5781  C  CB  . LEU   C 1 44  ? 63.01  67.802  41.054 1   35.98  ? 66  LEU   C CB  1 
ATOM   5782  C  CG  . LEU   C 1 44  ? 63.816 66.605  40.538 1   38.32  ? 66  LEU   C CG  1 
ATOM   5783  C  CD1 . LEU   C 1 44  ? 63.334 66.177  39.161 1   38.49  ? 66  LEU   C CD1 1 
ATOM   5784  C  CD2 . LEU   C 1 44  ? 65.291 66.936  40.445 1   39.57  ? 66  LEU   C CD2 1 
ATOM   5785  N  N   . TRP   C 1 45  ? 61.659 70.04   42.776 1   35.41  ? 67  TRP   C N   1 
ATOM   5786  C  CA  . TRP   C 1 45  ? 61.078 71.366  42.908 1   34.94  ? 67  TRP   C CA  1 
ATOM   5787  C  C   . TRP   C 1 45  ? 61.561 72.087  44.172 1   35.92  ? 67  TRP   C C   1 
ATOM   5788  O  O   . TRP   C 1 45  ? 61.59  73.309  44.18  1   36.38  ? 67  TRP   C O   1 
ATOM   5789  C  CB  . TRP   C 1 45  ? 59.541 71.308  42.797 1   33.88  ? 67  TRP   C CB  1 
ATOM   5790  C  CG  . TRP   C 1 45  ? 59.047 70.933  41.427 1   32.39  ? 67  TRP   C CG  1 
ATOM   5791  C  CD1 . TRP   C 1 45  ? 58.374 69.8    41.077 1   32.9   ? 67  TRP   C CD1 1 
ATOM   5792  C  CD2 . TRP   C 1 45  ? 59.216 71.696  40.212 1   31.7   ? 67  TRP   C CD2 1 
ATOM   5793  N  NE1 . TRP   C 1 45  ? 58.131 69.794  39.709 1   33.15  ? 67  TRP   C NE1 1 
ATOM   5794  C  CE2 . TRP   C 1 45  ? 58.605 70.965  39.167 1   32.16  ? 67  TRP   C CE2 1 
ATOM   5795  C  CE3 . TRP   C 1 45  ? 59.805 72.936  39.913 1   31.49  ? 67  TRP   C CE3 1 
ATOM   5796  C  CZ2 . TRP   C 1 45  ? 58.551 71.443  37.864 1   31.82  ? 67  TRP   C CZ2 1 
ATOM   5797  C  CZ3 . TRP   C 1 45  ? 59.757 73.396  38.616 1   31.84  ? 67  TRP   C CZ3 1 
ATOM   5798  C  CH2 . TRP   C 1 45  ? 59.113 72.668  37.617 1   31.87  ? 67  TRP   C CH2 1 
ATOM   5799  N  N   . PHE   C 1 46  ? 62.01  71.353  45.205 1   36.1   ? 68  PHE   C N   1 
ATOM   5800  C  CA  . PHE   C 1 46  ? 62.587 71.961  46.405 1   36.6   ? 68  PHE   C CA  1 
ATOM   5801  C  C   . PHE   C 1 46  ? 63.922 72.595  46.017 1   36.85  ? 68  PHE   C C   1 
ATOM   5802  O  O   . PHE   C 1 46  ? 64.188 73.739  46.382 1   37.43  ? 68  PHE   C O   1 
ATOM   5803  C  CB  . PHE   C 1 46  ? 62.799 70.92   47.521 1   36.62  ? 68  PHE   C CB  1 
ATOM   5804  C  CG  . PHE   C 1 46  ? 61.562 70.465  48.264 1   37.65  ? 68  PHE   C CG  1 
ATOM   5805  C  CD1 . PHE   C 1 46  ? 60.359 71.14   48.129 1   38.94  ? 68  PHE   C CD1 1 
ATOM   5806  C  CD2 . PHE   C 1 46  ? 61.588 69.328  49.046 1   38.67  ? 68  PHE   C CD2 1 
ATOM   5807  C  CE1 . PHE   C 1 46  ? 59.211 70.695  48.782 1   39.91  ? 68  PHE   C CE1 1 
ATOM   5808  C  CE2 . PHE   C 1 46  ? 60.44  68.885  49.697 1   39.73  ? 68  PHE   C CE2 1 
ATOM   5809  C  CZ  . PHE   C 1 46  ? 59.26  69.573  49.566 1   39.64  ? 68  PHE   C CZ  1 
ATOM   5810  N  N   . LYS   C 1 47  ? 64.733 71.888  45.198 1   36.08  ? 69  LYS   C N   1 
ATOM   5811  C  CA  . LYS   C 1 47  ? 66.004 72.42   44.706 1   35.14  ? 69  LYS   C CA  1 
ATOM   5812  C  C   . LYS   C 1 47  ? 65.777 73.714  43.916 1   34.2   ? 69  LYS   C C   1 
ATOM   5813  O  O   . LYS   C 1 47  ? 66.525 74.674  44.083 1   33.97  ? 69  LYS   C O   1 
ATOM   5814  C  CB  . LYS   C 1 47  ? 66.745 71.361  43.865 1   35.46  ? 69  LYS   C CB  1 
ATOM   5815  C  CG  . LYS   C 1 47  ? 68.123 71.818  43.437 1   37.74  ? 69  LYS   C CG  1 
ATOM   5816  C  CD  . LYS   C 1 47  ? 69.015 70.689  43.038 1   40.6   ? 69  LYS   C CD  1 
ATOM   5817  C  CE  . LYS   C 1 47  ? 70.256 71.255  42.413 1   44.19  ? 69  LYS   C CE  1 
ATOM   5818  N  NZ  . LYS   C 1 47  ? 71.341 70.243  42.329 1   47.26  ? 69  LYS   C NZ  1 
ATOM   5819  N  N   . GLN   C 1 48  ? 64.712 73.746  43.102 1   33.93  ? 70  GLN   C N   1 
ATOM   5820  C  CA  . GLN   C 1 48  ? 64.331 74.926  42.32  1   34.31  ? 70  GLN   C CA  1 
ATOM   5821  C  C   . GLN   C 1 48  ? 63.921 76.072  43.231 1   34.69  ? 70  GLN   C C   1 
ATOM   5822  O  O   . GLN   C 1 48  ? 64.421 77.173  43.052 1   34.89  ? 70  GLN   C O   1 
ATOM   5823  C  CB  . GLN   C 1 48  ? 63.202 74.615  41.325 1   35.52  ? 70  GLN   C CB  1 
ATOM   5824  C  CG  . GLN   C 1 48  ? 62.908 75.775  40.369 1   37.58  ? 70  GLN   C CG  1 
ATOM   5825  C  CD  . GLN   C 1 48  ? 64.079 76.047  39.455 1   39.18  ? 70  GLN   C CD  1 
ATOM   5826  O  OE1 . GLN   C 1 48  ? 64.648 75.134  38.88  1   40.28  ? 70  GLN   C OE1 1 
ATOM   5827  N  NE2 . GLN   C 1 48  ? 64.475 77.3    39.295 1   38.31  ? 70  GLN   C NE2 1 
ATOM   5828  N  N   . ILE   C 1 49  ? 63.049 75.815  44.236 1   34.6   ? 71  ILE   C N   1 
ATOM   5829  C  CA  . ILE   C 1 49  ? 62.595 76.842  45.174 1   34.49  ? 71  ILE   C CA  1 
ATOM   5830  C  C   . ILE   C 1 49  ? 63.758 77.448  45.934 1   34.97  ? 71  ILE   C C   1 
ATOM   5831  O  O   . ILE   C 1 49  ? 63.818 78.671  46.082 1   35.06  ? 71  ILE   C O   1 
ATOM   5832  C  CB  . ILE   C 1 49  ? 61.477 76.316  46.107 1   34.51  ? 71  ILE   C CB  1 
ATOM   5833  C  CG1 . ILE   C 1 49  ? 60.198 75.99   45.315 1   34.62  ? 71  ILE   C CG1 1 
ATOM   5834  C  CG2 . ILE   C 1 49  ? 61.169 77.309  47.241 1   35.07  ? 71  ILE   C CG2 1 
ATOM   5835  C  CD1 . ILE   C 1 49  ? 59.273 75.128  46.112 1   35.75  ? 71  ILE   C CD1 1 
ATOM   5836  N  N   . ILE   C 1 50  ? 64.71  76.604  46.374 1   35.47  ? 72  ILE   C N   1 
ATOM   5837  C  CA  . ILE   C 1 50  ? 65.895 77.068  47.103 1   37.06  ? 72  ILE   C CA  1 
ATOM   5838  C  C   . ILE   C 1 50  ? 66.759 77.963  46.21  1   39.24  ? 72  ILE   C C   1 
ATOM   5839  O  O   . ILE   C 1 50  ? 67.266 78.99   46.664 1   39.65  ? 72  ILE   C O   1 
ATOM   5840  C  CB  . ILE   C 1 50  ? 66.709 75.884  47.671 1   37.13  ? 72  ILE   C CB  1 
ATOM   5841  C  CG1 . ILE   C 1 50  ? 65.958 75.176  48.786 1   37.35  ? 72  ILE   C CG1 1 
ATOM   5842  C  CG2 . ILE   C 1 50  ? 68.095 76.336  48.161 1   37.69  ? 72  ILE   C CG2 1 
ATOM   5843  C  CD1 . ILE   C 1 50  ? 66.566 73.832  49.14  1   38.14  ? 72  ILE   C CD1 1 
ATOM   5844  N  N   . PHE   C 1 51  ? 66.919 77.562  44.945 1   40.28  ? 73  PHE   C N   1 
ATOM   5845  C  CA  . PHE   C 1 51  ? 67.684 78.305  43.953 1   41.53  ? 73  PHE   C CA  1 
ATOM   5846  C  C   . PHE   C 1 51  ? 67.085 79.703  43.747 1   42.06  ? 73  PHE   C C   1 
ATOM   5847  O  O   . PHE   C 1 51  ? 67.835 80.677  43.665 1   42.64  ? 73  PHE   C O   1 
ATOM   5848  C  CB  . PHE   C 1 51  ? 67.706 77.538  42.618 1   41.69  ? 73  PHE   C CB  1 
ATOM   5849  C  CG  . PHE   C 1 51  ? 68.693 78.114  41.634 1   42.88  ? 73  PHE   C CG  1 
ATOM   5850  C  CD1 . PHE   C 1 51  ? 70.057 78      41.848 1   43.6   ? 73  PHE   C CD1 1 
ATOM   5851  C  CD2 . PHE   C 1 51  ? 68.26  78.801  40.514 1   43.73  ? 73  PHE   C CD2 1 
ATOM   5852  C  CE1 . PHE   C 1 51  ? 70.966 78.533  40.94  1   43.87  ? 73  PHE   C CE1 1 
ATOM   5853  C  CE2 . PHE   C 1 51  ? 69.174 79.334  39.614 1   44.09  ? 73  PHE   C CE2 1 
ATOM   5854  C  CZ  . PHE   C 1 51  ? 70.519 79.201  39.837 1   43.57  ? 73  PHE   C CZ  1 
ATOM   5855  N  N   . GLU   C 1 52  ? 65.746 79.794  43.668 1   41.4   ? 74  GLU   C N   1 
ATOM   5856  C  CA  . GLU   C 1 52  ? 65.046 81.056  43.466 1   41.71  ? 74  GLU   C CA  1 
ATOM   5857  C  C   . GLU   C 1 52  ? 65.15  81.909  44.702 1   42.33  ? 74  GLU   C C   1 
ATOM   5858  O  O   . GLU   C 1 52  ? 65.442 83.097  44.594 1   42.53  ? 74  GLU   C O   1 
ATOM   5859  C  CB  . GLU   C 1 52  ? 63.566 80.839  43.088 1   43.22  ? 74  GLU   C CB  1 
ATOM   5860  C  CG  . GLU   C 1 52  ? 63.349 80.084  41.787 1   46.11  ? 74  GLU   C CG  1 
ATOM   5861  C  CD  . GLU   C 1 52  ? 63.89  80.728  40.523 1   50.08  ? 74  GLU   C CD  1 
ATOM   5862  O  OE1 . GLU   C 1 52  ? 64.047 81.968  40.503 1   49.99  ? 74  GLU   C OE1 1 
ATOM   5863  O  OE2 . GLU   C 1 52  ? 64.135 79.991  39.541 1   52.33  ? 74  GLU   C OE2 1 
ATOM   5864  N  N   . PHE   C 1 53  ? 64.945 81.304  45.884 1   42.5   ? 75  PHE   C N   1 
ATOM   5865  C  CA  . PHE   C 1 53  ? 65.033 81.999  47.165 1   42.84  ? 75  PHE   C CA  1 
ATOM   5866  C  C   . PHE   C 1 53  ? 66.42  82.569  47.409 1   44.14  ? 75  PHE   C C   1 
ATOM   5867  O  O   . PHE   C 1 53  ? 66.53  83.698  47.876 1   44.8   ? 75  PHE   C O   1 
ATOM   5868  C  CB  . PHE   C 1 53  ? 64.647 81.065  48.312 1   42.03  ? 75  PHE   C CB  1 
ATOM   5869  C  CG  . PHE   C 1 53  ? 63.176 81.009  48.661 1   41.69  ? 75  PHE   C CG  1 
ATOM   5870  C  CD1 . PHE   C 1 53  ? 62.223 81.604  47.845 1   41.96  ? 75  PHE   C CD1 1 
ATOM   5871  C  CD2 . PHE   C 1 53  ? 62.746 80.355  49.8   1   41.59  ? 75  PHE   C CD2 1 
ATOM   5872  C  CE1 . PHE   C 1 53  ? 60.876 81.555  48.175 1   42.29  ? 75  PHE   C CE1 1 
ATOM   5873  C  CE2 . PHE   C 1 53  ? 61.401 80.285  50.111 1   42.24  ? 75  PHE   C CE2 1 
ATOM   5874  C  CZ  . PHE   C 1 53  ? 60.472 80.89   49.301 1   42.08  ? 75  PHE   C CZ  1 
ATOM   5875  N  N   . ASP   C 1 54  ? 67.475 81.813  47.073 1   44.04  ? 76  ASP   C N   1 
ATOM   5876  C  CA  . ASP   C 1 54  ? 68.828 82.284  47.256 1   44.18  ? 76  ASP   C CA  1 
ATOM   5877  C  C   . ASP   C 1 54  ? 69.117 83.443  46.357 1   44.94  ? 76  ASP   C C   1 
ATOM   5878  O  O   . ASP   C 1 54  ? 69.733 84.378  46.817 1   45.98  ? 76  ASP   C O   1 
ATOM   5879  C  CB  . ASP   C 1 54  ? 69.848 81.16   47.09  1   45.41  ? 76  ASP   C CB  1 
ATOM   5880  C  CG  . ASP   C 1 54  ? 69.963 80.282  48.322 1   49.75  ? 76  ASP   C CG  1 
ATOM   5881  O  OD1 . ASP   C 1 54  ? 69.714 80.788  49.444 1   48.46  ? 76  ASP   C OD1 1 
ATOM   5882  O  OD2 . ASP   C 1 54  ? 70.307 79.092  48.171 1   53.32  ? 76  ASP   C OD2 1 
ATOM   5883  N  N   . SER   C 1 55  ? 68.62  83.449  45.12  1   44.92  ? 77  SER   C N   1 
ATOM   5884  C  CA  . SER   C 1 55  ? 68.835 84.568  44.205 1   45.18  ? 77  SER   C CA  1 
ATOM   5885  C  C   . SER   C 1 55  ? 68.049 85.812  44.637 1   46.53  ? 77  SER   C C   1 
ATOM   5886  O  O   . SER   C 1 55  ? 68.58  86.918  44.556 1   47.32  ? 77  SER   C O   1 
ATOM   5887  C  CB  . SER   C 1 55  ? 68.512 84.173  42.774 1   45.61  ? 77  SER   C CB  1 
ATOM   5888  O  OG  . SER   C 1 55  ? 67.124 83.988  42.578 1   47.63  ? 77  SER   C OG  1 
ATOM   5889  N  N   . ILE   C 1 56  ? 66.827 85.637  45.163 1   46.68  ? 78  ILE   C N   1 
ATOM   5890  C  CA  . ILE   C 1 56  ? 66.028 86.75   45.689 1   47.35  ? 78  ILE   C CA  1 
ATOM   5891  C  C   . ILE   C 1 56  ? 66.69  87.327  46.94  1   48     ? 78  ILE   C C   1 
ATOM   5892  O  O   . ILE   C 1 56  ? 66.667 88.539  47.133 1   48.44  ? 78  ILE   C O   1 
ATOM   5893  C  CB  . ILE   C 1 56  ? 64.576 86.303  45.983 1   48.07  ? 78  ILE   C CB  1 
ATOM   5894  C  CG1 . ILE   C 1 56  ? 63.845 85.9    44.697 1   49.29  ? 78  ILE   C CG1 1 
ATOM   5895  C  CG2 . ILE   C 1 56  ? 63.792 87.386  46.73  1   48.57  ? 78  ILE   C CG2 1 
ATOM   5896  C  CD1 . ILE   C 1 56  ? 62.612 85.105  44.96  1   50.71  ? 78  ILE   C CD1 1 
ATOM   5897  N  N   . ARG   C 1 57  ? 67.3   86.47   47.777 1   48.13  ? 79  ARG   C N   1 
ATOM   5898  C  CA  . ARG   C 1 57  ? 67.998 86.913  48.976 1   49.23  ? 79  ARG   C CA  1 
ATOM   5899  C  C   . ARG   C 1 57  ? 69.204 87.754  48.59  1   50.31  ? 79  ARG   C C   1 
ATOM   5900  O  O   . ARG   C 1 57  ? 69.426 88.802  49.195 1   50.06  ? 79  ARG   C O   1 
ATOM   5901  C  CB  . ARG   C 1 57  ? 68.465 85.734  49.836 1   50.76  ? 79  ARG   C CB  1 
ATOM   5902  C  CG  . ARG   C 1 57  ? 67.368 85.041  50.653 1   53.78  ? 79  ARG   C CG  1 
ATOM   5903  C  CD  . ARG   C 1 57  ? 67.872 84.047  51.701 1   57.61  ? 79  ARG   C CD  1 
ATOM   5904  N  NE  . ARG   C 1 57  ? 69.133 83.392  51.33  1   63.24  ? 79  ARG   C NE  1 
ATOM   5905  C  CZ  . ARG   C 1 57  ? 70.313 83.673  51.885 1   67.15  ? 79  ARG   C CZ  1 
ATOM   5906  N  NH1 . ARG   C 1 57  ? 70.402 84.576  52.853 1   67.28  ? 79  ARG   C NH1 1 
ATOM   5907  N  NH2 . ARG   C 1 57  ? 71.411 83.045  51.479 1   67.43  ? 79  ARG   C NH2 1 
ATOM   5908  N  N   . ASP   C 1 58  ? 69.954 87.325  47.547 1   50.86  ? 80  ASP   C N   1 
ATOM   5909  C  CA  . ASP   C 1 58  ? 71.131 88.049  47.067 1   51.7   ? 80  ASP   C CA  1 
ATOM   5910  C  C   . ASP   C 1 58  ? 70.756 89.41   46.513 1   52.26  ? 80  ASP   C C   1 
ATOM   5911  O  O   . ASP   C 1 58  ? 71.501 90.369  46.702 1   52.29  ? 80  ASP   C O   1 
ATOM   5912  C  CB  . ASP   C 1 58  ? 71.911 87.217  46.034 1   53.6   ? 80  ASP   C CB  1 
ATOM   5913  C  CG  . ASP   C 1 58  ? 72.498 85.92   46.572 1   57.98  ? 80  ASP   C CG  1 
ATOM   5914  O  OD1 . ASP   C 1 58  ? 72.319 85.641  47.777 1   59.51  ? 80  ASP   C OD1 1 
ATOM   5915  O  OD2 . ASP   C 1 58  ? 73.115 85.167  45.778 1   59.73  ? 80  ASP   C OD2 1 
ATOM   5916  N  N   . MET   C 1 59  ? 69.593 89.498  45.848 1   52.46  ? 81  MET   C N   1 
ATOM   5917  C  CA  . MET   C 1 59  ? 69.074 90.744  45.293 1   52.76  ? 81  MET   C CA  1 
ATOM   5918  C  C   . MET   C 1 59  ? 68.595 91.683  46.403 1   54.36  ? 81  MET   C C   1 
ATOM   5919  O  O   . MET   C 1 59  ? 68.739 92.895  46.28  1   54.46  ? 81  MET   C O   1 
ATOM   5920  C  CB  . MET   C 1 59  ? 67.941 90.462  44.3   1   52.03  ? 81  MET   C CB  1 
ATOM   5921  C  CG  . MET   C 1 59  ? 68.43  89.897  42.997 1   52.01  ? 81  MET   C CG  1 
ATOM   5922  S  SD  . MET   C 1 59  ? 67.162 89.862  41.707 1   53.18  ? 81  MET   C SD  1 
ATOM   5923  C  CE  . MET   C 1 59  ? 66.2   88.469  42.216 1   50.71  ? 81  MET   C CE  1 
ATOM   5924  N  N   . LEU   C 1 60  ? 68.031 91.13   47.484 1   55.51  ? 82  LEU   C N   1 
ATOM   5925  C  CA  . LEU   C 1 60  ? 67.567 91.931  48.619 1   57.22  ? 82  LEU   C CA  1 
ATOM   5926  C  C   . LEU   C 1 60  ? 68.701 92.345  49.569 1   59.45  ? 82  LEU   C C   1 
ATOM   5927  O  O   . LEU   C 1 60  ? 68.518 93.263  50.365 1   59.73  ? 82  LEU   C O   1 
ATOM   5928  C  CB  . LEU   C 1 60  ? 66.481 91.184  49.402 1   57     ? 82  LEU   C CB  1 
ATOM   5929  C  CG  . LEU   C 1 60  ? 65.136 91.074  48.725 1   57.88  ? 82  LEU   C CG  1 
ATOM   5930  C  CD1 . LEU   C 1 60  ? 64.221 90.192  49.519 1   58.53  ? 82  LEU   C CD1 1 
ATOM   5931  C  CD2 . LEU   C 1 60  ? 64.513 92.429  48.539 1   58.17  ? 82  LEU   C CD2 1 
ATOM   5932  N  N   . ASP   C 1 61  ? 69.862 91.673  49.496 1   60.99  ? 83  ASP   C N   1 
ATOM   5933  C  CA  . ASP   C 1 61  ? 71.025 91.954  50.335 1   63.11  ? 83  ASP   C CA  1 
ATOM   5934  C  C   . ASP   C 1 61  ? 71.854 93.088  49.722 1   65.37  ? 83  ASP   C C   1 
ATOM   5935  O  O   . ASP   C 1 61  ? 73.061 92.943  49.512 1   65.59  ? 83  ASP   C O   1 
ATOM   5936  C  CB  . ASP   C 1 61  ? 71.866 90.677  50.501 1   64.63  ? 83  ASP   C CB  1 
ATOM   5937  C  CG  . ASP   C 1 61  ? 72.762 90.657  51.713 1   68.48  ? 83  ASP   C CG  1 
ATOM   5938  O  OD1 . ASP   C 1 61  ? 72.256 90.358  52.826 1   68.47  ? 83  ASP   C OD1 1 
ATOM   5939  O  OD2 . ASP   C 1 61  ? 73.972 90.915  51.55  1   71.22  ? 83  ASP   C OD2 1 
ATOM   5940  N  N   . ALA   C 1 62  ? 71.187 94.217  49.433 1   66.74  ? 84  ALA   C N   1 
ATOM   5941  C  CA  . ALA   C 1 62  ? 71.783 95.415  48.844 1   68.45  ? 84  ALA   C CA  1 
ATOM   5942  C  C   . ALA   C 1 62  ? 71.08  96.662  49.39  1   70.12  ? 84  ALA   C C   1 
ATOM   5943  O  O   . ALA   C 1 62  ? 69.873 96.624  49.654 1   70.4   ? 84  ALA   C O   1 
ATOM   5944  C  CB  . ALA   C 1 62  ? 71.65  95.368  47.331 1   68.58  ? 84  ALA   C CB  1 
ATOM   5945  N  N   . GLU   C 1 63  ? 71.823 97.772  49.561 1   70.88  ? 85  GLU   C N   1 
ATOM   5946  C  CA  . GLU   C 1 63  ? 71.228 99.018  50.07  1   71.89  ? 85  GLU   C CA  1 
ATOM   5947  C  C   . GLU   C 1 63  ? 70.318 99.726  49.043 1   72.12  ? 85  GLU   C C   1 
ATOM   5948  O  O   . GLU   C 1 63  ? 69.417 100.481 49.421 1   72.34  ? 85  GLU   C O   1 
ATOM   5949  C  CB  . GLU   C 1 63  ? 72.302 99.967  50.619 1   74.91  ? 85  GLU   C CB  1 
ATOM   5950  C  CG  . GLU   C 1 63  ? 72.653 99.677  52.068 1   81.38  ? 85  GLU   C CG  1 
ATOM   5951  C  CD  . GLU   C 1 63  ? 73.749 100.547 52.653 1   90.04  ? 85  GLU   C CD  1 
ATOM   5952  O  OE1 . GLU   C 1 63  ? 74.918 100.412 52.221 1   91.79  ? 85  GLU   C OE1 1 
ATOM   5953  O  OE2 . GLU   C 1 63  ? 73.44  101.357 53.556 1   92.81  ? 85  GLU   C OE2 1 
ATOM   5954  N  N   . VAL   C 1 64  ? 70.54  99.442  47.748 1   71.76  ? 86  VAL   C N   1 
ATOM   5955  C  CA  . VAL   C 1 64  ? 69.776 99.98   46.628 1   71.72  ? 86  VAL   C CA  1 
ATOM   5956  C  C   . VAL   C 1 64  ? 69.077 98.858  45.825 1   70.91  ? 86  VAL   C C   1 
ATOM   5957  O  O   . VAL   C 1 64  ? 69.733 98.014  45.198 1   71.12  ? 86  VAL   C O   1 
ATOM   5958  C  CB  . VAL   C 1 64  ? 70.661 100.872 45.714 1   72.97  ? 86  VAL   C CB  1 
ATOM   5959  C  CG1 . VAL   C 1 64  ? 72.005 100.202 45.389 1   73.57  ? 86  VAL   C CG1 1 
ATOM   5960  C  CG2 . VAL   C 1 64  ? 69.916 101.272 44.436 1   73.6   ? 86  VAL   C CG2 1 
ATOM   5961  N  N   . ILE   C 1 65  ? 67.739 98.833  45.867 1   69.73  ? 87  ILE   C N   1 
ATOM   5962  C  CA  . ILE   C 1 65  ? 66.975 97.845  45.106 1   68.84  ? 87  ILE   C CA  1 
ATOM   5963  C  C   . ILE   C 1 65  ? 66.145 98.622  44.094 1   67.46  ? 87  ILE   C C   1 
ATOM   5964  O  O   . ILE   C 1 65  ? 65.098 99.183  44.441 1   67.72  ? 87  ILE   C O   1 
ATOM   5965  C  CB  . ILE   C 1 65  ? 66.128 96.939  46.023 1   69.44  ? 87  ILE   C CB  1 
ATOM   5966  C  CG1 . ILE   C 1 65  ? 67.027 96.231  47.054 1   70.32  ? 87  ILE   C CG1 1 
ATOM   5967  C  CG2 . ILE   C 1 65  ? 65.341 95.927  45.193 1   70.09  ? 87  ILE   C CG2 1 
ATOM   5968  C  CD1 . ILE   C 1 65  ? 66.419 96.058  48.428 1   71.44  ? 87  ILE   C CD1 1 
ATOM   5969  N  N   . ASP   C 1 66  ? 66.655 98.729  42.857 1   65.67  ? 88  ASP   C N   1 
ATOM   5970  C  CA  . ASP   C 1 66  ? 65.986 99.527  41.833 1   64.5   ? 88  ASP   C CA  1 
ATOM   5971  C  C   . ASP   C 1 66  ? 64.733 98.847  41.258 1   62.77  ? 88  ASP   C C   1 
ATOM   5972  O  O   . ASP   C 1 66  ? 64.442 97.698  41.596 1   62.74  ? 88  ASP   C O   1 
ATOM   5973  C  CB  . ASP   C 1 66  ? 66.975 99.973  40.731 1   66.2   ? 88  ASP   C CB  1 
ATOM   5974  C  CG  . ASP   C 1 66  ? 67.56  98.861  39.89  1   71.04  ? 88  ASP   C CG  1 
ATOM   5975  O  OD1 . ASP   C 1 66  ? 67.749 97.753  40.425 1   71.68  ? 88  ASP   C OD1 1 
ATOM   5976  O  OD2 . ASP   C 1 66  ? 67.844 99.106  38.694 1   73.43  ? 88  ASP   C OD2 1 
ATOM   5977  N  N   . GLU   C 1 67  ? 63.959 99.588  40.438 1   61.19  ? 89  GLU   C N   1 
ATOM   5978  C  CA  . GLU   C 1 67  ? 62.735 99.09   39.829 1   60.02  ? 89  GLU   C CA  1 
ATOM   5979  C  C   . GLU   C 1 67  ? 62.987 97.828  39.001 1   58.49  ? 89  GLU   C C   1 
ATOM   5980  O  O   . GLU   C 1 67  ? 62.138 96.935  38.965 1   58.71  ? 89  GLU   C O   1 
ATOM   5981  C  CB  . GLU   C 1 67  ? 62.119 100.168 38.938 1   62.38  ? 89  GLU   C CB  1 
ATOM   5982  C  CG  . GLU   C 1 67  ? 61.562 101.368 39.674 1   68.24  ? 89  GLU   C CG  1 
ATOM   5983  C  CD  . GLU   C 1 67  ? 60.631 102.208 38.82  1   76.37  ? 89  GLU   C CD  1 
ATOM   5984  O  OE1 . GLU   C 1 67  ? 59.41  101.921 38.806 1   77.39  ? 89  GLU   C OE1 1 
ATOM   5985  O  OE2 . GLU   C 1 67  ? 61.124 103.148 38.155 1   79.51  ? 89  GLU   C OE2 1 
ATOM   5986  N  N   . THR   C 1 68  ? 64.152 97.753  38.343 1   56.67  ? 90  THR   C N   1 
ATOM   5987  C  CA  . THR   C 1 68  ? 64.497 96.62   37.496 1   55.53  ? 90  THR   C CA  1 
ATOM   5988  C  C   . THR   C 1 68  ? 64.753 95.349  38.331 1   54.96  ? 90  THR   C C   1 
ATOM   5989  O  O   . THR   C 1 68  ? 64.246 94.277  37.979 1   55.11  ? 90  THR   C O   1 
ATOM   5990  C  CB  . THR   C 1 68  ? 65.631 96.994  36.541 1   55.85  ? 90  THR   C CB  1 
ATOM   5991  O  OG1 . THR   C 1 68  ? 65.305 98.227  35.885 1   56.22  ? 90  THR   C OG1 1 
ATOM   5992  C  CG2 . THR   C 1 68  ? 65.857 95.932  35.486 1   56.19  ? 90  THR   C CG2 1 
ATOM   5993  N  N   . LYS   C 1 69  ? 65.483 95.466  39.459 1   53.96  ? 91  LYS   C N   1 
ATOM   5994  C  CA  . LYS   C 1 69  ? 65.699 94.308  40.333 1   53.32  ? 91  LYS   C CA  1 
ATOM   5995  C  C   . LYS   C 1 69  ? 64.391 93.895  41.009 1   51.94  ? 91  LYS   C C   1 
ATOM   5996  O  O   . LYS   C 1 69  ? 64.133 92.698  41.14  1   52.1   ? 91  LYS   C O   1 
ATOM   5997  C  CB  . LYS   C 1 69  ? 66.803 94.567  41.37  1   55.29  ? 91  LYS   C CB  1 
ATOM   5998  C  CG  . LYS   C 1 69  ? 68.209 94.688  40.755 1   59.96  ? 91  LYS   C CG  1 
ATOM   5999  C  CD  . LYS   C 1 69  ? 68.79  93.353  40.242 1   64.83  ? 91  LYS   C CD  1 
ATOM   6000  C  CE  . LYS   C 1 69  ? 68.796 93.2    38.722 1   68.65  ? 91  LYS   C CE  1 
ATOM   6001  N  NZ  . LYS   C 1 69  ? 69.543 94.291  38.032 1   70.27  ? 91  LYS   C NZ  1 
ATOM   6002  N  N   . THR   C 1 70  ? 63.544 94.879  41.383 1   50.22  ? 92  THR   C N   1 
ATOM   6003  C  CA  . THR   C 1 70  ? 62.243 94.632  42.008 1   49.19  ? 92  THR   C CA  1 
ATOM   6004  C  C   . THR   C 1 70  ? 61.362 93.776  41.116 1   47.62  ? 92  THR   C C   1 
ATOM   6005  O  O   . THR   C 1 70  ? 60.768 92.821  41.605 1   48.65  ? 92  THR   C O   1 
ATOM   6006  C  CB  . THR   C 1 70  ? 61.57  95.952  42.417 1   50.97  ? 92  THR   C CB  1 
ATOM   6007  O  OG1 . THR   C 1 70  ? 62.375 96.582  43.419 1   52.48  ? 92  THR   C OG1 1 
ATOM   6008  C  CG2 . THR   C 1 70  ? 60.131 95.762  42.937 1   51.21  ? 92  THR   C CG2 1 
ATOM   6009  N  N   . LEU   C 1 71  ? 61.331 94.065  39.808 1   45.17  ? 93  LEU   C N   1 
ATOM   6010  C  CA  . LEU   C 1 71  ? 60.559 93.301  38.821 1   43.47  ? 93  LEU   C CA  1 
ATOM   6011  C  C   . LEU   C 1 71  ? 61.023 91.839  38.725 1   41.8   ? 93  LEU   C C   1 
ATOM   6012  O  O   . LEU   C 1 71  ? 60.206 90.937  38.557 1   41.46  ? 93  LEU   C O   1 
ATOM   6013  C  CB  . LEU   C 1 71  ? 60.677 93.957  37.434 1   43.16  ? 93  LEU   C CB  1 
ATOM   6014  C  CG  . LEU   C 1 71  ? 59.871 95.215  37.204 1   43.93  ? 93  LEU   C CG  1 
ATOM   6015  C  CD1 . LEU   C 1 71  ? 60.216 95.799  35.872 1   44.04  ? 93  LEU   C CD1 1 
ATOM   6016  C  CD2 . LEU   C 1 71  ? 58.374 94.942  37.314 1   44.49  ? 93  LEU   C CD2 1 
ATOM   6017  N  N   . GLU   C 1 72  ? 62.329 91.616  38.799 1   41.09  ? 94  GLU   C N   1 
ATOM   6018  C  CA  . GLU   C 1 72  ? 62.891 90.274  38.732 1   41.11  ? 94  GLU   C CA  1 
ATOM   6019  C  C   . GLU   C 1 72  ? 62.583 89.497  40.019 1   40.89  ? 94  GLU   C C   1 
ATOM   6020  O  O   . GLU   C 1 72  ? 62.355 88.286  39.957 1   41.11  ? 94  GLU   C O   1 
ATOM   6021  C  CB  . GLU   C 1 72  ? 64.401 90.324  38.453 1   43.24  ? 94  GLU   C CB  1 
ATOM   6022  C  CG  . GLU   C 1 72  ? 64.984 88.989  38.014 1   47.62  ? 94  GLU   C CG  1 
ATOM   6023  C  CD  . GLU   C 1 72  ? 64.596 88.498  36.631 1   53.25  ? 94  GLU   C CD  1 
ATOM   6024  O  OE1 . GLU   C 1 72  ? 64.082 89.315  35.835 1   55.17  ? 94  GLU   C OE1 1 
ATOM   6025  O  OE2 . GLU   C 1 72  ? 64.824 87.302  36.333 1   54.81  ? 94  GLU   C OE2 1 
ATOM   6026  N  N   . ILE   C 1 73  ? 62.524 90.192  41.175 1   39.9   ? 95  ILE   C N   1 
ATOM   6027  C  CA  . ILE   C 1 73  ? 62.149 89.565  42.433 1   39.64  ? 95  ILE   C CA  1 
ATOM   6028  C  C   . ILE   C 1 73  ? 60.675 89.127  42.327 1   39.35  ? 95  ILE   C C   1 
ATOM   6029  O  O   . ILE   C 1 73  ? 60.353 87.991  42.661 1   39.95  ? 95  ILE   C O   1 
ATOM   6030  C  CB  . ILE   C 1 73  ? 62.399 90.516  43.635 1   40.23  ? 95  ILE   C CB  1 
ATOM   6031  C  CG1 . ILE   C 1 73  ? 63.903 90.759  43.84  1   40.67  ? 95  ILE   C CG1 1 
ATOM   6032  C  CG2 . ILE   C 1 73  ? 61.753 89.981  44.923 1   40.74  ? 95  ILE   C CG2 1 
ATOM   6033  C  CD1 . ILE   C 1 73  ? 64.228 91.862  44.766 1   41.28  ? 95  ILE   C CD1 1 
ATOM   6034  N  N   . VAL   C 1 74  ? 59.801 89.992  41.787 1   38.36  ? 96  VAL   C N   1 
ATOM   6035  C  CA  . VAL   C 1 74  ? 58.387 89.674  41.61  1   38.27  ? 96  VAL   C CA  1 
ATOM   6036  C  C   . VAL   C 1 74  ? 58.19  88.467  40.666 1   38.04  ? 96  VAL   C C   1 
ATOM   6037  O  O   . VAL   C 1 74  ? 57.388 87.586  40.972 1   38.19  ? 96  VAL   C O   1 
ATOM   6038  C  CB  . VAL   C 1 74  ? 57.598 90.933  41.183 1   39.25  ? 96  VAL   C CB  1 
ATOM   6039  C  CG1 . VAL   C 1 74  ? 56.169 90.6    40.781 1   39.26  ? 96  VAL   C CG1 1 
ATOM   6040  C  CG2 . VAL   C 1 74  ? 57.608 91.973  42.295 1   40.32  ? 96  VAL   C CG2 1 
ATOM   6041  N  N   . LYS   C 1 75  ? 58.978 88.38   39.573 1   37.48  ? 97  LYS   C N   1 
ATOM   6042  C  CA  . LYS   C 1 75  ? 58.914 87.257  38.64  1   37.18  ? 97  LYS   C CA  1 
ATOM   6043  C  C   . LYS   C 1 75  ? 59.26  85.938  39.334 1   37.71  ? 97  LYS   C C   1 
ATOM   6044  O  O   . LYS   C 1 75  ? 58.579 84.929  39.14  1   38.25  ? 97  LYS   C O   1 
ATOM   6045  C  CB  . LYS   C 1 75  ? 59.869 87.485  37.466 1   38.39  ? 97  LYS   C CB  1 
ATOM   6046  C  CG  . LYS   C 1 75  ? 59.967 86.292  36.504 1   40.96  ? 97  LYS   C CG  1 
ATOM   6047  C  CD  . LYS   C 1 75  ? 60.393 86.686  35.114 1   44.81  ? 97  LYS   C CD  1 
ATOM   6048  C  CE  . LYS   C 1 75  ? 61.867 86.899  34.955 1   48.38  ? 97  LYS   C CE  1 
ATOM   6049  N  NZ  . LYS   C 1 75  ? 62.145 87.901  33.873 1   50.75  ? 97  LYS   C NZ  1 
ATOM   6050  N  N   . ARG   C 1 76  ? 60.316 85.951  40.151 1   37.28  ? 98  ARG   C N   1 
ATOM   6051  C  CA  . ARG   C 1 76  ? 60.783 84.756  40.839 1   37.04  ? 98  ARG   C CA  1 
ATOM   6052  C  C   . ARG   C 1 76  ? 59.905 84.37   42.015 1   37.86  ? 98  ARG   C C   1 
ATOM   6053  O  O   . ARG   C 1 76  ? 59.748 83.175  42.277 1   38.27  ? 98  ARG   C O   1 
ATOM   6054  C  CB  . ARG   C 1 76  ? 62.25  84.917  41.228 1   36.89  ? 98  ARG   C CB  1 
ATOM   6055  C  CG  . ARG   C 1 76  ? 63.09  85.115  39.979 1   36.43  ? 98  ARG   C CG  1 
ATOM   6056  C  CD  . ARG   C 1 76  ? 64.52  85.383  40.3   1   36.01  ? 98  ARG   C CD  1 
ATOM   6057  N  NE  . ARG   C 1 76  ? 65.262 85.623  39.065 1   34     ? 98  ARG   C NE  1 
ATOM   6058  C  CZ  . ARG   C 1 76  ? 66.556 85.894  39.016 1   33.05  ? 98  ARG   C CZ  1 
ATOM   6059  N  NH1 . ARG   C 1 76  ? 67.27  85.968  40.134 1   30.32  ? 98  ARG   C NH1 1 
ATOM   6060  N  NH2 . ARG   C 1 76  ? 67.15  86.098  37.849 1   34.14  ? 98  ARG   C NH2 1 
ATOM   6061  N  N   . LEU   C 1 77  ? 59.268 85.356  42.681 1   37.51  ? 99  LEU   C N   1 
ATOM   6062  C  CA  . LEU   C 1 77  ? 58.326 85.052  43.759 1   37.32  ? 99  LEU   C CA  1 
ATOM   6063  C  C   . LEU   C 1 77  ? 57.075 84.41   43.166 1   37.11  ? 99  LEU   C C   1 
ATOM   6064  O  O   . LEU   C 1 77  ? 56.568 83.436  43.705 1   36.51  ? 99  LEU   C O   1 
ATOM   6065  C  CB  . LEU   C 1 77  ? 57.947 86.312  44.553 1   37.64  ? 99  LEU   C CB  1 
ATOM   6066  C  CG  . LEU   C 1 77  ? 58.999 86.836  45.527 1   38.91  ? 99  LEU   C CG  1 
ATOM   6067  C  CD1 . LEU   C 1 77  ? 58.605 88.187  46.085 1   39.29  ? 99  LEU   C CD1 1 
ATOM   6068  C  CD2 . LEU   C 1 77  ? 59.282 85.822  46.635 1   39.4   ? 99  LEU   C CD2 1 
ATOM   6069  N  N   . ASN   C 1 78  ? 56.606 84.927  42.027 1   37.71  ? 100 ASN   C N   1 
ATOM   6070  C  CA  . ASN   C 1 78  ? 55.44  84.395  41.339 1   38.27  ? 100 ASN   C CA  1 
ATOM   6071  C  C   . ASN   C 1 78  ? 55.716 82.982  40.778 1   38.32  ? 100 ASN   C C   1 
ATOM   6072  O  O   . ASN   C 1 78  ? 54.83  82.13   40.784 1   39.01  ? 100 ASN   C O   1 
ATOM   6073  C  CB  . ASN   C 1 78  ? 55.01  85.341  40.248 1   39.53  ? 100 ASN   C CB  1 
ATOM   6074  C  CG  . ASN   C 1 78  ? 53.703 84.93   39.641 1   44.52  ? 100 ASN   C CG  1 
ATOM   6075  O  OD1 . ASN   C 1 78  ? 53.658 84.127  38.714 1   46.32  ? 100 ASN   C OD1 1 
ATOM   6076  N  ND2 . ASN   C 1 78  ? 52.597 85.452  40.162 1   46.09  ? 100 ASN   C ND2 1 
ATOM   6077  N  N   . ARG   C 1 79  ? 56.948 82.725  40.339 1   37.22  ? 101 ARG   C N   1 
ATOM   6078  C  CA  . ARG   C 1 79  ? 57.362 81.412  39.861 1   36.55  ? 101 ARG   C CA  1 
ATOM   6079  C  C   . ARG   C 1 79  ? 57.273 80.4    41.016 1   36.53  ? 101 ARG   C C   1 
ATOM   6080  O  O   . ARG   C 1 79  ? 56.723 79.315  40.832 1   37     ? 101 ARG   C O   1 
ATOM   6081  C  CB  . ARG   C 1 79  ? 58.801 81.495  39.345 1   36.42  ? 101 ARG   C CB  1 
ATOM   6082  C  CG  . ARG   C 1 79  ? 59.393 80.169  38.913 1   36.15  ? 101 ARG   C CG  1 
ATOM   6083  C  CD  . ARG   C 1 79  ? 60.798 80.372  38.403 1   36.76  ? 101 ARG   C CD  1 
ATOM   6084  N  NE  . ARG   C 1 79  ? 60.785 81.146  37.16  1   37.39  ? 101 ARG   C NE  1 
ATOM   6085  C  CZ  . ARG   C 1 79  ? 61.854 81.7    36.605 1   37.89  ? 101 ARG   C CZ  1 
ATOM   6086  N  NH1 . ARG   C 1 79  ? 63.047 81.591  37.184 1   36.86  ? 101 ARG   C NH1 1 
ATOM   6087  N  NH2 . ARG   C 1 79  ? 61.744 82.365  35.467 1   38.24  ? 101 ARG   C NH2 1 
ATOM   6088  N  N   . VAL   C 1 80  ? 57.755 80.78   42.213 1   35.64  ? 102 VAL   C N   1 
ATOM   6089  C  CA  . VAL   C 1 80  ? 57.688 79.953  43.416 1   35.56  ? 102 VAL   C CA  1 
ATOM   6090  C  C   . VAL   C 1 80  ? 56.236 79.665  43.782 1   36.6   ? 102 VAL   C C   1 
ATOM   6091  O  O   . VAL   C 1 80  ? 55.931 78.533  44.131 1   37.96  ? 102 VAL   C O   1 
ATOM   6092  C  CB  . VAL   C 1 80  ? 58.49  80.586  44.581 1   35.76  ? 102 VAL   C CB  1 
ATOM   6093  C  CG1 . VAL   C 1 80  ? 58.147 79.947  45.92  1   36.17  ? 102 VAL   C CG1 1 
ATOM   6094  C  CG2 . VAL   C 1 80  ? 59.993 80.5    44.316 1   36.03  ? 102 VAL   C CG2 1 
ATOM   6095  N  N   . VAL   C 1 81  ? 55.33  80.658  43.632 1   35.92  ? 103 VAL   C N   1 
ATOM   6096  C  CA  . VAL   C 1 81  ? 53.891 80.522  43.885 1   35.49  ? 103 VAL   C CA  1 
ATOM   6097  C  C   . VAL   C 1 81  ? 53.304 79.417  42.987 1   34.99  ? 103 VAL   C C   1 
ATOM   6098  O  O   . VAL   C 1 81  ? 52.506 78.599  43.454 1   34.57  ? 103 VAL   C O   1 
ATOM   6099  C  CB  . VAL   C 1 81  ? 53.178 81.891  43.681 1   35.92  ? 103 VAL   C CB  1 
ATOM   6100  C  CG1 . VAL   C 1 81  ? 51.678 81.738  43.438 1   36.37  ? 103 VAL   C CG1 1 
ATOM   6101  C  CG2 . VAL   C 1 81  ? 53.438 82.813  44.854 1   36.04  ? 103 VAL   C CG2 1 
ATOM   6102  N  N   . LEU   C 1 82  ? 53.72  79.386  41.711 1   34.8   ? 104 LEU   C N   1 
ATOM   6103  C  CA  . LEU   C 1 82  ? 53.259 78.374  40.76  1   35.36  ? 104 LEU   C CA  1 
ATOM   6104  C  C   . LEU   C 1 82  ? 53.807 76.986  41.105 1   35.71  ? 104 LEU   C C   1 
ATOM   6105  O  O   . LEU   C 1 82  ? 53.097 75.998  40.969 1   35.82  ? 104 LEU   C O   1 
ATOM   6106  C  CB  . LEU   C 1 82  ? 53.667 78.744  39.331 1   35.66  ? 104 LEU   C CB  1 
ATOM   6107  C  CG  . LEU   C 1 82  ? 53.015 79.986  38.738 1   36.91  ? 104 LEU   C CG  1 
ATOM   6108  C  CD1 . LEU   C 1 82  ? 53.426 80.153  37.301 1   37.33  ? 104 LEU   C CD1 1 
ATOM   6109  C  CD2 . LEU   C 1 82  ? 51.501 79.917  38.818 1   36.92  ? 104 LEU   C CD2 1 
ATOM   6110  N  N   . ILE   C 1 83  ? 55.067 76.918  41.538 1   35.61  ? 105 ILE   C N   1 
ATOM   6111  C  CA  . ILE   C 1 83  ? 55.706 75.668  41.931 1   36.05  ? 105 ILE   C CA  1 
ATOM   6112  C  C   . ILE   C 1 83  ? 55.035 75.109  43.18  1   36.11  ? 105 ILE   C C   1 
ATOM   6113  O  O   . ILE   C 1 83  ? 54.797 73.909  43.263 1   35.99  ? 105 ILE   C O   1 
ATOM   6114  C  CB  . ILE   C 1 83  ? 57.228 75.888  42.133 1   36.68  ? 105 ILE   C CB  1 
ATOM   6115  C  CG1 . ILE   C 1 83  ? 57.902 76.288  40.807 1   37.98  ? 105 ILE   C CG1 1 
ATOM   6116  C  CG2 . ILE   C 1 83  ? 57.893 74.653  42.715 1   36.78  ? 105 ILE   C CG2 1 
ATOM   6117  C  CD1 . ILE   C 1 83  ? 59.349 76.78   40.974 1   39.39  ? 105 ILE   C CD1 1 
ATOM   6118  N  N   . LEU   C 1 84  ? 54.697 75.982  44.136 1   36.13  ? 106 LEU   C N   1 
ATOM   6119  C  CA  . LEU   C 1 84  ? 54.016 75.577  45.361 1   36.18  ? 106 LEU   C CA  1 
ATOM   6120  C  C   . LEU   C 1 84  ? 52.625 75.042  45.047 1   36.05  ? 106 LEU   C C   1 
ATOM   6121  O  O   . LEU   C 1 84  ? 52.284 74      45.563 1   36.21  ? 106 LEU   C O   1 
ATOM   6122  C  CB  . LEU   C 1 84  ? 53.966 76.718  46.401 1   36.31  ? 106 LEU   C CB  1 
ATOM   6123  C  CG  . LEU   C 1 84  ? 55.26  76.943  47.178 1   37.31  ? 106 LEU   C CG  1 
ATOM   6124  C  CD1 . LEU   C 1 84  ? 55.231 78.241  47.927 1   37.35  ? 106 LEU   C CD1 1 
ATOM   6125  C  CD2 . LEU   C 1 84  ? 55.536 75.798  48.122 1   38.4   ? 106 LEU   C CD2 1 
ATOM   6126  N  N   . LYS   C 1 85  ? 51.854 75.693  44.161 1   36.11  ? 107 LYS   C N   1 
ATOM   6127  C  CA  . LYS   C 1 85  ? 50.52  75.2    43.758 1   36.46  ? 107 LYS   C CA  1 
ATOM   6128  C  C   . LYS   C 1 85  ? 50.618 73.81   43.143 1   37.23  ? 107 LYS   C C   1 
ATOM   6129  O  O   . LYS   C 1 85  ? 49.733 72.986  43.344 1   37.69  ? 107 LYS   C O   1 
ATOM   6130  C  CB  . LYS   C 1 85  ? 49.863 76.129  42.713 1   37.33  ? 107 LYS   C CB  1 
ATOM   6131  C  CG  . LYS   C 1 85  ? 49.32  77.435  43.254 1   39.48  ? 107 LYS   C CG  1 
ATOM   6132  C  CD  . LYS   C 1 85  ? 48.639 78.233  42.17  1   42.03  ? 107 LYS   C CD  1 
ATOM   6133  C  CE  . LYS   C 1 85  ? 48.507 79.698  42.523 1   46.2   ? 107 LYS   C CE  1 
ATOM   6134  N  NZ  . LYS   C 1 85  ? 48.327 80.544  41.303 1   49.43  ? 107 LYS   C NZ  1 
ATOM   6135  N  N   . LEU   C 1 86  ? 51.672 73.572  42.353 1   37.13  ? 108 LEU   C N   1 
ATOM   6136  C  CA  . LEU   C 1 86  ? 51.931 72.294  41.704 1   37.3   ? 108 LEU   C CA  1 
ATOM   6137  C  C   . LEU   C 1 86  ? 52.227 71.233  42.766 1   37.75  ? 108 LEU   C C   1 
ATOM   6138  O  O   . LEU   C 1 86  ? 51.7   70.131  42.68  1   38.63  ? 108 LEU   C O   1 
ATOM   6139  C  CB  . LEU   C 1 86  ? 53.12  72.43   40.74  1   37.08  ? 108 LEU   C CB  1 
ATOM   6140  C  CG  . LEU   C 1 86  ? 53.413 71.24   39.843 1   37.49  ? 108 LEU   C CG  1 
ATOM   6141  C  CD1 . LEU   C 1 86  ? 52.522 71.263  38.641 1   37.92  ? 108 LEU   C CD1 1 
ATOM   6142  C  CD2 . LEU   C 1 86  ? 54.866 71.236  39.424 1   37.54  ? 108 LEU   C CD2 1 
ATOM   6143  N  N   . LEU   C 1 87  ? 53.027 71.569  43.791 1   36.8   ? 109 LEU   C N   1 
ATOM   6144  C  CA  . LEU   C 1 87  ? 53.339 70.633  44.863 1   36.04  ? 109 LEU   C CA  1 
ATOM   6145  C  C   . LEU   C 1 87  ? 52.125 70.294  45.733 1   35.61  ? 109 LEU   C C   1 
ATOM   6146  O  O   . LEU   C 1 87  ? 51.993 69.159  46.193 1   35.88  ? 109 LEU   C O   1 
ATOM   6147  C  CB  . LEU   C 1 87  ? 54.521 71.148  45.691 1   36.09  ? 109 LEU   C CB  1 
ATOM   6148  C  CG  . LEU   C 1 87  ? 55.845 71.326  44.917 1   37.39  ? 109 LEU   C CG  1 
ATOM   6149  C  CD1 . LEU   C 1 87  ? 56.949 71.88   45.826 1   37.46  ? 109 LEU   C CD1 1 
ATOM   6150  C  CD2 . LEU   C 1 87  ? 56.29  70.011  44.256 1   38.06  ? 109 LEU   C CD2 1 
ATOM   6151  N  N   . VAL   C 1 88  ? 51.2   71.244  45.921 1   35.21  ? 110 VAL   C N   1 
ATOM   6152  C  CA  . VAL   C 1 88  ? 49.957 70.968  46.649 1   34.91  ? 110 VAL   C CA  1 
ATOM   6153  C  C   . VAL   C 1 88  ? 49.126 69.933  45.845 1   35.34  ? 110 VAL   C C   1 
ATOM   6154  O  O   . VAL   C 1 88  ? 48.543 69.023  46.434 1   35.77  ? 110 VAL   C O   1 
ATOM   6155  C  CB  . VAL   C 1 88  ? 49.165 72.259  46.925 1   34.58  ? 110 VAL   C CB  1 
ATOM   6156  C  CG1 . VAL   C 1 88  ? 47.805 71.95   47.525 1   35.14  ? 110 VAL   C CG1 1 
ATOM   6157  C  CG2 . VAL   C 1 88  ? 49.949 73.189  47.822 1   34.56  ? 110 VAL   C CG2 1 
ATOM   6158  N  N   . ASP   C 1 89  ? 49.149 70.031  44.496 1   35.02  ? 111 ASP   C N   1 
ATOM   6159  C  CA  . ASP   C 1 89  ? 48.447 69.116  43.592 1   35.68  ? 111 ASP   C CA  1 
ATOM   6160  C  C   . ASP   C 1 89  ? 49.097 67.737  43.439 1   36.02  ? 111 ASP   C C   1 
ATOM   6161  O  O   . ASP   C 1 89  ? 48.515 66.869  42.79  1   36.75  ? 111 ASP   C O   1 
ATOM   6162  C  CB  . ASP   C 1 89  ? 48.25  69.752  42.219 1   37.39  ? 111 ASP   C CB  1 
ATOM   6163  C  CG  . ASP   C 1 89  ? 47.281 70.923  42.184 1   44.34  ? 111 ASP   C CG  1 
ATOM   6164  O  OD1 . ASP   C 1 89  ? 46.758 71.307  43.266 1   45.44  ? 111 ASP   C OD1 1 
ATOM   6165  O  OD2 . ASP   C 1 89  ? 47.051 71.472  41.076 1   48.01  ? 111 ASP   C OD2 1 
ATOM   6166  N  N   . GLN   C 1 90  ? 50.283 67.535  43.997 1   35.43  ? 112 GLN   C N   1 
ATOM   6167  C  CA  . GLN   C 1 90  ? 50.952 66.244  43.938 1   36.28  ? 112 GLN   C CA  1 
ATOM   6168  C  C   . GLN   C 1 90  ? 50.449 65.301  45.035 1   37.68  ? 112 GLN   C C   1 
ATOM   6169  O  O   . GLN   C 1 90  ? 50.576 64.088  44.892 1   38.01  ? 112 GLN   C O   1 
ATOM   6170  C  CB  . GLN   C 1 90  ? 52.477 66.396  43.995 1   37.17  ? 112 GLN   C CB  1 
ATOM   6171  C  CG  . GLN   C 1 90  ? 53.051 67.062  42.751 1   38.71  ? 112 GLN   C CG  1 
ATOM   6172  C  CD  . GLN   C 1 90  ? 54.547 66.982  42.637 1   42.59  ? 112 GLN   C CD  1 
ATOM   6173  O  OE1 . GLN   C 1 90  ? 55.232 66.368  43.465 1   44.84  ? 112 GLN   C OE1 1 
ATOM   6174  N  NE2 . GLN   C 1 90  ? 55.092 67.58   41.58  1   43.23  ? 112 GLN   C NE2 1 
ATOM   6175  N  N   . VAL   C 1 91  ? 49.881 65.849  46.134 1   37.78  ? 113 VAL   C N   1 
ATOM   6176  C  CA  . VAL   C 1 91  ? 49.315 65.055  47.224 1   37.02  ? 113 VAL   C CA  1 
ATOM   6177  C  C   . VAL   C 1 91  ? 48.189 64.141  46.728 1   36.95  ? 113 VAL   C C   1 
ATOM   6178  O  O   . VAL   C 1 91  ? 48.28  62.942  46.966 1   37.73  ? 113 VAL   C O   1 
ATOM   6179  C  CB  . VAL   C 1 91  ? 48.892 65.925  48.434 1   37.05  ? 113 VAL   C CB  1 
ATOM   6180  C  CG1 . VAL   C 1 91  ? 48.343 65.061  49.554 1   37.5   ? 113 VAL   C CG1 1 
ATOM   6181  C  CG2 . VAL   C 1 91  ? 50.057 66.77   48.939 1   36.88  ? 113 VAL   C CG2 1 
ATOM   6182  N  N   . PRO   C 1 92  ? 47.175 64.621  45.965 1   36.33  ? 114 PRO   C N   1 
ATOM   6183  C  CA  . PRO   C 1 92  ? 46.112 63.709  45.5   1   35.86  ? 114 PRO   C CA  1 
ATOM   6184  C  C   . PRO   C 1 92  ? 46.583 62.525  44.647 1   35.41  ? 114 PRO   C C   1 
ATOM   6185  O  O   . PRO   C 1 92  ? 45.878 61.505  44.574 1   34.84  ? 114 PRO   C O   1 
ATOM   6186  C  CB  . PRO   C 1 92  ? 45.177 64.628  44.713 1   36.38  ? 114 PRO   C CB  1 
ATOM   6187  C  CG  . PRO   C 1 92  ? 45.42  65.974  45.245 1   36.87  ? 114 PRO   C CG  1 
ATOM   6188  C  CD  . PRO   C 1 92  ? 46.883 66.011  45.563 1   35.72  ? 114 PRO   C CD  1 
ATOM   6189  N  N   . ILE   C 1 93  ? 47.787 62.654  44.024 1   34.78  ? 115 ILE   C N   1 
ATOM   6190  C  CA  . ILE   C 1 93  ? 48.399 61.601  43.225 1   34.31  ? 115 ILE   C CA  1 
ATOM   6191  C  C   . ILE   C 1 93  ? 48.913 60.505  44.157 1   34.5   ? 115 ILE   C C   1 
ATOM   6192  O  O   . ILE   C 1 93  ? 48.732 59.317  43.857 1   34.94  ? 115 ILE   C O   1 
ATOM   6193  C  CB  . ILE   C 1 93  ? 49.518 62.16   42.327 1   34.4   ? 115 ILE   C CB  1 
ATOM   6194  C  CG1 . ILE   C 1 93  ? 48.961 63.184  41.306 1   34.85  ? 115 ILE   C CG1 1 
ATOM   6195  C  CG2 . ILE   C 1 93  ? 50.295 61.046  41.644 1   34.62  ? 115 ILE   C CG2 1 
ATOM   6196  C  CD1 . ILE   C 1 93  ? 50.035 63.921  40.475 1   35.04  ? 115 ILE   C CD1 1 
ATOM   6197  N  N   . LEU   C 1 94  ? 49.538 60.886  45.292 1   33.76  ? 116 LEU   C N   1 
ATOM   6198  C  CA  . LEU   C 1 94  ? 50.005 59.892  46.251 1   34.23  ? 116 LEU   C CA  1 
ATOM   6199  C  C   . LEU   C 1 94  ? 48.824 59.274  47.01  1   36.2   ? 116 LEU   C C   1 
ATOM   6200  O  O   . LEU   C 1 94  ? 48.863 58.079  47.325 1   36.75  ? 116 LEU   C O   1 
ATOM   6201  C  CB  . LEU   C 1 94  ? 51.075 60.437  47.2   1   33.71  ? 116 LEU   C CB  1 
ATOM   6202  C  CG  . LEU   C 1 94  ? 51.898 59.392  47.987 1   33.89  ? 116 LEU   C CG  1 
ATOM   6203  C  CD1 . LEU   C 1 94  ? 52.514 58.347  47.075 1   34.02  ? 116 LEU   C CD1 1 
ATOM   6204  C  CD2 . LEU   C 1 94  ? 53.014 60.047  48.773 1   34.03  ? 116 LEU   C CD2 1 
ATOM   6205  N  N   . GLU   C 1 95  ? 47.736 60.062  47.24  1   36.7   ? 117 GLU   C N   1 
ATOM   6206  C  CA  . GLU   C 1 95  ? 46.507 59.581  47.884 1   37.19  ? 117 GLU   C CA  1 
ATOM   6207  C  C   . GLU   C 1 95  ? 45.814 58.462  47.089 1   37.72  ? 117 GLU   C C   1 
ATOM   6208  O  O   . GLU   C 1 95  ? 44.862 57.87   47.588 1   37.73  ? 117 GLU   C O   1 
ATOM   6209  C  CB  . GLU   C 1 95  ? 45.533 60.74   48.114 1   39.65  ? 117 GLU   C CB  1 
ATOM   6210  C  CG  . GLU   C 1 95  ? 46.012 61.726  49.161 1   45.14  ? 117 GLU   C CG  1 
ATOM   6211  C  CD  . GLU   C 1 95  ? 45.029 62.83   49.501 1   52.52  ? 117 GLU   C CD  1 
ATOM   6212  O  OE1 . GLU   C 1 95  ? 44.644 63.588  48.583 1   53.68  ? 117 GLU   C OE1 1 
ATOM   6213  O  OE2 . GLU   C 1 95  ? 44.654 62.948  50.689 1   55.46  ? 117 GLU   C OE2 1 
ATOM   6214  N  N   . THR   C 1 96  ? 46.27  58.197  45.841 1   37.9   ? 118 THR   C N   1 
ATOM   6215  C  CA  . THR   C 1 96  ? 45.786 57.132  44.957 1   37.86  ? 118 THR   C CA  1 
ATOM   6216  C  C   . THR   C 1 96  ? 46.179 55.749  45.515 1   37.54  ? 118 THR   C C   1 
ATOM   6217  O  O   . THR   C 1 96  ? 45.478 54.767  45.255 1   37.66  ? 118 THR   C O   1 
ATOM   6218  C  CB  . THR   C 1 96  ? 46.319 57.393  43.533 1   39.17  ? 118 THR   C CB  1 
ATOM   6219  O  OG1 . THR   C 1 96  ? 45.788 58.634  43.066 1   39.39  ? 118 THR   C OG1 1 
ATOM   6220  C  CG2 . THR   C 1 96  ? 45.935 56.34   42.557 1   40.83  ? 118 THR   C CG2 1 
ATOM   6221  N  N   . MET   C 1 97  ? 47.284 55.689  46.296 1   37.06  ? 119 MET   C N   1 
ATOM   6222  C  CA  . MET   C 1 97  ? 47.833 54.503  46.934 1   37.57  ? 119 MET   C CA  1 
ATOM   6223  C  C   . MET   C 1 97  ? 46.95  54.097  48.124 1   38.53  ? 119 MET   C C   1 
ATOM   6224  O  O   . MET   C 1 97  ? 46.534 54.958  48.907 1   39     ? 119 MET   C O   1 
ATOM   6225  C  CB  . MET   C 1 97  ? 49.276 54.812  47.39  1   37.72  ? 119 MET   C CB  1 
ATOM   6226  C  CG  . MET   C 1 97  ? 49.895 53.785  48.313 1   39.62  ? 119 MET   C CG  1 
ATOM   6227  S  SD  . MET   C 1 97  ? 51.646 54.14   48.671 1   42.63  ? 119 MET   C SD  1 
ATOM   6228  C  CE  . MET   C 1 97  ? 51.525 55.65   49.507 1   37.54  ? 119 MET   C CE  1 
ATOM   6229  N  N   . THR   C 1 98  ? 46.64  52.798  48.249 1   38.18  ? 120 THR   C N   1 
ATOM   6230  C  CA  . THR   C 1 98  ? 45.815 52.331  49.36  1   38.36  ? 120 THR   C CA  1 
ATOM   6231  C  C   . THR   C 1 98  ? 46.643 52.178  50.628 1   39.14  ? 120 THR   C C   1 
ATOM   6232  O  O   . THR   C 1 98  ? 47.854 51.898  50.561 1   39.22  ? 120 THR   C O   1 
ATOM   6233  C  CB  . THR   C 1 98  ? 45.013 51.067  48.997 1   38.53  ? 120 THR   C CB  1 
ATOM   6234  O  OG1 . THR   C 1 98  ? 45.851 49.903  48.987 1   38.6   ? 120 THR   C OG1 1 
ATOM   6235  C  CG2 . THR   C 1 98  ? 44.258 51.228  47.717 1   38.74  ? 120 THR   C CG2 1 
ATOM   6236  N  N   . PRO   C 1 99  ? 45.993 52.36   51.8   1   39.18  ? 121 PRO   C N   1 
ATOM   6237  C  CA  . PRO   C 1 99  ? 46.725 52.252  53.067 1   39.67  ? 121 PRO   C CA  1 
ATOM   6238  C  C   . PRO   C 1 99  ? 47.353 50.89   53.308 1   40.62  ? 121 PRO   C C   1 
ATOM   6239  O  O   . PRO   C 1 99  ? 48.37  50.812  53.983 1   40.6   ? 121 PRO   C O   1 
ATOM   6240  C  CB  . PRO   C 1 99  ? 45.662 52.588  54.117 1   40.15  ? 121 PRO   C CB  1 
ATOM   6241  C  CG  . PRO   C 1 99  ? 44.616 53.357  53.365 1   40.25  ? 121 PRO   C CG  1 
ATOM   6242  C  CD  . PRO   C 1 99  ? 44.583 52.724  52.028 1   38.53  ? 121 PRO   C CD  1 
ATOM   6243  N  N   . LEU   C 1 100 ? 46.753 49.828  52.758 1   41.65  ? 122 LEU   C N   1 
ATOM   6244  C  CA  . LEU   C 1 100 ? 47.252 48.454  52.883 1   43.37  ? 122 LEU   C CA  1 
ATOM   6245  C  C   . LEU   C 1 100 ? 48.417 48.202  51.95  1   44.12  ? 122 LEU   C C   1 
ATOM   6246  O  O   . LEU   C 1 100 ? 49.284 47.406  52.274 1   44.75  ? 122 LEU   C O   1 
ATOM   6247  C  CB  . LEU   C 1 100 ? 46.158 47.433  52.597 1   44.74  ? 122 LEU   C CB  1 
ATOM   6248  C  CG  . LEU   C 1 100 ? 44.829 47.66   53.281 1   47.9   ? 122 LEU   C CG  1 
ATOM   6249  C  CD1 . LEU   C 1 100 ? 43.88  48.544  52.395 1   49.1   ? 122 LEU   C CD1 1 
ATOM   6250  C  CD2 . LEU   C 1 100 ? 44.179 46.335  53.573 1   48.89  ? 122 LEU   C CD2 1 
ATOM   6251  N  N   . ASP   C 1 101 ? 48.441 48.866  50.784 1   44.2   ? 123 ASP   C N   1 
ATOM   6252  C  CA  . ASP   C 1 101 ? 49.558 48.782  49.865 1   44.93  ? 123 ASP   C CA  1 
ATOM   6253  C  C   . ASP   C 1 101 ? 50.738 49.499  50.532 1   45.67  ? 123 ASP   C C   1 
ATOM   6254  O  O   . ASP   C 1 101 ? 51.829 48.939  50.59  1   46.4   ? 123 ASP   C O   1 
ATOM   6255  C  CB  . ASP   C 1 101 ? 49.209 49.437  48.512 1   46.54  ? 123 ASP   C CB  1 
ATOM   6256  C  CG  . ASP   C 1 101 ? 48.444 48.542  47.557 1   50     ? 123 ASP   C CG  1 
ATOM   6257  O  OD1 . ASP   C 1 101 ? 48.538 47.303  47.706 1   50.65  ? 123 ASP   C OD1 1 
ATOM   6258  O  OD2 . ASP   C 1 101 ? 47.75  49.085  46.649 1   51.58  ? 123 ASP   C OD2 1 
ATOM   6259  N  N   . PHE   C 1 102 ? 50.5   50.692  51.116 1   45.24  ? 124 PHE   C N   1 
ATOM   6260  C  CA  . PHE   C 1 102 ? 51.538 51.433  51.824 1   45.31  ? 124 PHE   C CA  1 
ATOM   6261  C  C   . PHE   C 1 102 ? 52.1   50.625  52.989 1   46.44  ? 124 PHE   C C   1 
ATOM   6262  O  O   . PHE   C 1 102 ? 53.31  50.614  53.213 1   47.02  ? 124 PHE   C O   1 
ATOM   6263  C  CB  . PHE   C 1 102 ? 50.987 52.772  52.335 1   44.62  ? 124 PHE   C CB  1 
ATOM   6264  C  CG  . PHE   C 1 102 ? 52.035 53.626  53.001 1   44.85  ? 124 PHE   C CG  1 
ATOM   6265  C  CD1 . PHE   C 1 102 ? 53.24  53.895  52.368 1   45.4   ? 124 PHE   C CD1 1 
ATOM   6266  C  CD2 . PHE   C 1 102 ? 51.817 54.169  54.259 1   45.56  ? 124 PHE   C CD2 1 
ATOM   6267  C  CE1 . PHE   C 1 102 ? 54.223 54.662  52.991 1   45.8   ? 124 PHE   C CE1 1 
ATOM   6268  C  CE2 . PHE   C 1 102 ? 52.784 54.97   54.864 1   46     ? 124 PHE   C CE2 1 
ATOM   6269  C  CZ  . PHE   C 1 102 ? 53.987 55.199  54.231 1   45.66  ? 124 PHE   C CZ  1 
ATOM   6270  N  N   . MET   C 1 103 ? 51.225 49.931  53.717 1   46.71  ? 125 MET   C N   1 
ATOM   6271  C  CA  . MET   C 1 103 ? 51.599 49.12   54.871 1   47.77  ? 125 MET   C CA  1 
ATOM   6272  C  C   . MET   C 1 103 ? 52.571 47.992  54.513 1   47.81  ? 125 MET   C C   1 
ATOM   6273  O  O   . MET   C 1 103 ? 53.408 47.618  55.339 1   47.43  ? 125 MET   C O   1 
ATOM   6274  C  CB  . MET   C 1 103 ? 50.33  48.549  55.537 1   49.19  ? 125 MET   C CB  1 
ATOM   6275  C  CG  . MET   C 1 103 ? 50.5   48.179  56.995 1   52.14  ? 125 MET   C CG  1 
ATOM   6276  S  SD  . MET   C 1 103 ? 48.902 47.849  57.814 1   61.62  ? 125 MET   C SD  1 
ATOM   6277  C  CE  . MET   C 1 103 ? 48.476 49.428  58.384 1   59.86  ? 125 MET   C CE  1 
ATOM   6278  N  N   . ASP   C 1 104 ? 52.481 47.476  53.272 1   48.04  ? 126 ASP   C N   1 
ATOM   6279  C  CA  . ASP   C 1 104 ? 53.31  46.375  52.789 1   48.8   ? 126 ASP   C CA  1 
ATOM   6280  C  C   . ASP   C 1 104 ? 54.755 46.752  52.416 1   48.58  ? 126 ASP   C C   1 
ATOM   6281  O  O   . ASP   C 1 104 ? 55.575 45.856  52.187 1   48.32  ? 126 ASP   C O   1 
ATOM   6282  C  CB  . ASP   C 1 104 ? 52.628 45.655  51.622 1   51.63  ? 126 ASP   C CB  1 
ATOM   6283  C  CG  . ASP   C 1 104 ? 51.415 44.837  52.005 1   58.94  ? 126 ASP   C CG  1 
ATOM   6284  O  OD1 . ASP   C 1 104 ? 51.099 44.764  53.232 1   60.11  ? 126 ASP   C OD1 1 
ATOM   6285  O  OD2 . ASP   C 1 104 ? 50.763 44.275  51.083 1   62.12  ? 126 ASP   C OD2 1 
ATOM   6286  N  N   . PHE   C 1 105 ? 55.079 48.045  52.373 1   48.5   ? 127 PHE   C N   1 
ATOM   6287  C  CA  . PHE   C 1 105 ? 56.454 48.45   52.083 1   49.07  ? 127 PHE   C CA  1 
ATOM   6288  C  C   . PHE   C 1 105 ? 57.018 49.452  53.124 1   50.94  ? 127 PHE   C C   1 
ATOM   6289  O  O   . PHE   C 1 105 ? 58.205 49.742  53.094 1   51.52  ? 127 PHE   C O   1 
ATOM   6290  C  CB  . PHE   C 1 105 ? 56.623 48.934  50.625 1   47.85  ? 127 PHE   C CB  1 
ATOM   6291  C  CG  . PHE   C 1 105 ? 56.077 50.297  50.267 1   47.08  ? 127 PHE   C CG  1 
ATOM   6292  C  CD1 . PHE   C 1 105 ? 56.847 51.438  50.434 1   47.03  ? 127 PHE   C CD1 1 
ATOM   6293  C  CD2 . PHE   C 1 105 ? 54.821 50.432  49.697 1   47     ? 127 PHE   C CD2 1 
ATOM   6294  C  CE1 . PHE   C 1 105 ? 56.344 52.687  50.096 1   46.92  ? 127 PHE   C CE1 1 
ATOM   6295  C  CE2 . PHE   C 1 105 ? 54.323 51.688  49.358 1   46.87  ? 127 PHE   C CE2 1 
ATOM   6296  C  CZ  . PHE   C 1 105 ? 55.09  52.802  49.551 1   46.32  ? 127 PHE   C CZ  1 
ATOM   6297  N  N   . ARG   C 1 106 ? 56.196 49.923  54.06  1   51.91  ? 128 ARG   C N   1 
ATOM   6298  C  CA  . ARG   C 1 106 ? 56.567 50.851  55.128 1   53.6   ? 128 ARG   C CA  1 
ATOM   6299  C  C   . ARG   C 1 106 ? 57.735 50.334  56.019 1   54.9   ? 128 ARG   C C   1 
ATOM   6300  O  O   . ARG   C 1 106 ? 58.466 51.12   56.625 1   54.68  ? 128 ARG   C O   1 
ATOM   6301  C  CB  . ARG   C 1 106 ? 55.316 51.113  55.979 1   55.6   ? 128 ARG   C CB  1 
ATOM   6302  C  CG  . ARG   C 1 106 ? 55.445 52.242  56.98  1   59.96  ? 128 ARG   C CG  1 
ATOM   6303  C  CD  . ARG   C 1 106 ? 54.078 52.777  57.344 1   64.23  ? 128 ARG   C CD  1 
ATOM   6304  N  NE  . ARG   C 1 106 ? 53.267 51.786  58.049 1   67.78  ? 128 ARG   C NE  1 
ATOM   6305  C  CZ  . ARG   C 1 106 ? 53.167 51.709  59.37  1   69.51  ? 128 ARG   C CZ  1 
ATOM   6306  N  NH1 . ARG   C 1 106 ? 53.835 52.56   60.146 1   68.64  ? 128 ARG   C NH1 1 
ATOM   6307  N  NH2 . ARG   C 1 106 ? 52.412 50.77   59.93  1   68.69  ? 128 ARG   C NH2 1 
ATOM   6308  N  N   . LYS   C 1 107 ? 57.914 49.013  56.063 1   56     ? 129 LYS   C N   1 
ATOM   6309  C  CA  . LYS   C 1 107 ? 58.948 48.305  56.827 1   57.39  ? 129 LYS   C CA  1 
ATOM   6310  C  C   . LYS   C 1 107 ? 60.354 48.738  56.434 1   57.45  ? 129 LYS   C C   1 
ATOM   6311  O  O   . LYS   C 1 107 ? 61.242 48.795  57.283 1   57.45  ? 129 LYS   C O   1 
ATOM   6312  C  CB  . LYS   C 1 107 ? 58.833 46.789  56.576 1   60.7   ? 129 LYS   C CB  1 
ATOM   6313  C  CG  . LYS   C 1 107 ? 57.426 46.227  56.764 1   66.87  ? 129 LYS   C CG  1 
ATOM   6314  C  CD  . LYS   C 1 107 ? 56.608 46.172  55.467 1   72.41  ? 129 LYS   C CD  1 
ATOM   6315  C  CE  . LYS   C 1 107 ? 55.517 45.13   55.55  1   77.27  ? 129 LYS   C CE  1 
ATOM   6316  N  NZ  . LYS   C 1 107 ? 55.879 43.896  54.796 1   80.98  ? 129 LYS   C NZ  1 
ATOM   6317  N  N   . TYR   C 1 108 ? 60.553 49.023  55.138 1   57.21  ? 130 TYR   C N   1 
ATOM   6318  C  CA  . TYR   C 1 108 ? 61.84  49.418  54.57  1   57.62  ? 130 TYR   C CA  1 
ATOM   6319  C  C   . TYR   C 1 108 ? 62.206 50.899  54.796 1   59.23  ? 130 TYR   C C   1 
ATOM   6320  O  O   . TYR   C 1 108 ? 63.295 51.32   54.402 1   59.42  ? 130 TYR   C O   1 
ATOM   6321  C  CB  . TYR   C 1 108 ? 61.884 49.077  53.061 1   56.81  ? 130 TYR   C CB  1 
ATOM   6322  C  CG  . TYR   C 1 108 ? 61.441 47.665  52.722 1   56.54  ? 130 TYR   C CG  1 
ATOM   6323  C  CD1 . TYR   C 1 108 ? 62.292 46.584  52.903 1   57.05  ? 130 TYR   C CD1 1 
ATOM   6324  C  CD2 . TYR   C 1 108 ? 60.18  47.416  52.208 1   57     ? 130 TYR   C CD2 1 
ATOM   6325  C  CE1 . TYR   C 1 108 ? 61.882 45.285  52.619 1   57.75  ? 130 TYR   C CE1 1 
ATOM   6326  C  CE2 . TYR   C 1 108 ? 59.761 46.125  51.915 1   57.78  ? 130 TYR   C CE2 1 
ATOM   6327  C  CZ  . TYR   C 1 108 ? 60.614 45.059  52.119 1   58.59  ? 130 TYR   C CZ  1 
ATOM   6328  O  OH  . TYR   C 1 108 ? 60.196 43.783  51.813 1   59.78  ? 130 TYR   C OH  1 
ATOM   6329  N  N   . LEU   C 1 109 ? 61.32  51.679  55.443 1   60.06  ? 131 LEU   C N   1 
ATOM   6330  C  CA  . LEU   C 1 109 ? 61.493 53.123  55.679 1   60.97  ? 131 LEU   C CA  1 
ATOM   6331  C  C   . LEU   C 1 109 ? 62.035 53.466  57.108 1   61.99  ? 131 LEU   C C   1 
ATOM   6332  O  O   . LEU   C 1 109 ? 61.563 52.895  58.079 1   62.17  ? 131 LEU   C O   1 
ATOM   6333  C  CB  . LEU   C 1 109 ? 60.102 53.796  55.501 1   60.79  ? 131 LEU   C CB  1 
ATOM   6334  C  CG  . LEU   C 1 109 ? 59.601 54.318  54.126 1   61.66  ? 131 LEU   C CG  1 
ATOM   6335  C  CD1 . LEU   C 1 109 ? 60.179 53.571  52.945 1   61.96  ? 131 LEU   C CD1 1 
ATOM   6336  C  CD2 . LEU   C 1 109 ? 58.082 54.298  54.056 1   62.05  ? 131 LEU   C CD2 1 
ATOM   6337  N  N   . ALA   C 1 110 ? 62.947 54.454  57.249 1   62.66  ? 132 ALA   C N   1 
ATOM   6338  C  CA  . ALA   C 1 110 ? 63.414 54.906  58.574 1   63.86  ? 132 ALA   C CA  1 
ATOM   6339  C  C   . ALA   C 1 110 ? 62.675 56.207  58.941 1   65.24  ? 132 ALA   C C   1 
ATOM   6340  O  O   . ALA   C 1 110 ? 62.453 57.063  58.075 1   65.57  ? 132 ALA   C O   1 
ATOM   6341  C  CB  . ALA   C 1 110 ? 64.916 55.124  58.588 1   64     ? 132 ALA   C CB  1 
ATOM   6342  N  N   . PRO   C 1 111 ? 62.308 56.373  60.231 1   65.82  ? 133 PRO   C N   1 
ATOM   6343  C  CA  . PRO   C 1 111 ? 61.426 57.492  60.624 1   66.52  ? 133 PRO   C CA  1 
ATOM   6344  C  C   . PRO   C 1 111 ? 61.941 58.941  60.771 1   67.47  ? 133 PRO   C C   1 
ATOM   6345  O  O   . PRO   C 1 111 ? 61.094 59.785  61.082 1   67.88  ? 133 PRO   C O   1 
ATOM   6346  C  CB  . PRO   C 1 111 ? 60.905 57.046  61.993 1   67.11  ? 133 PRO   C CB  1 
ATOM   6347  C  CG  . PRO   C 1 111 ? 61.977 56.158  62.523 1   67.25  ? 133 PRO   C CG  1 
ATOM   6348  C  CD  . PRO   C 1 111 ? 62.441 55.395  61.327 1   65.42  ? 133 PRO   C CD  1 
ATOM   6349  N  N   . ALA   C 1 112 ? 63.252 59.263  60.568 1   67.54  ? 134 ALA   C N   1 
ATOM   6350  C  CA  . ALA   C 1 112 ? 63.864 60.626  60.693 1   67.88  ? 134 ALA   C CA  1 
ATOM   6351  C  C   . ALA   C 1 112 ? 64.27  61.027  62.129 1   68.4   ? 134 ALA   C C   1 
ATOM   6352  O  O   . ALA   C 1 112 ? 63.436 61.036  63.045 1   68.42  ? 134 ALA   C O   1 
ATOM   6353  C  CB  . ALA   C 1 112 ? 62.997 61.733  60.069 1   67.94  ? 134 ALA   C CB  1 
ATOM   6354  N  N   . SER   C 1 113 ? 65.564 61.391  62.3   1   68.53  ? 135 SER   C N   1 
ATOM   6355  C  CA  . SER   C 1 113 ? 66.141 61.811  63.582 1   68.94  ? 135 SER   C CA  1 
ATOM   6356  C  C   . SER   C 1 113 ? 65.657 63.213  63.981 1   68.93  ? 135 SER   C C   1 
ATOM   6357  O  O   . SER   C 1 113 ? 65.339 63.452  65.15  1   69.44  ? 135 SER   C O   1 
ATOM   6358  C  CB  . SER   C 1 113 ? 67.668 61.769  63.533 1   70.23  ? 135 SER   C CB  1 
ATOM   6359  O  OG  . SER   C 1 113 ? 68.202 60.701  64.299 1   72.5   ? 135 SER   C OG  1 
ATOM   6360  N  N   . GLY   C 1 114 ? 65.612 64.127  63.018 1   67.99  ? 136 GLY   C N   1 
ATOM   6361  C  CA  . GLY   C 1 114 ? 65.144 65.481  63.273 1   67.48  ? 136 GLY   C CA  1 
ATOM   6362  C  C   . GLY   C 1 114 ? 64.138 65.874  62.222 1   66.64  ? 136 GLY   C C   1 
ATOM   6363  O  O   . GLY   C 1 114 ? 62.955 65.514  62.299 1   66.58  ? 136 GLY   C O   1 
ATOM   6364  N  N   . PHE   C 1 115 ? 64.632 66.566  61.194 1   65.62  ? 137 PHE   C N   1 
ATOM   6365  C  CA  . PHE   C 1 115 ? 63.837 66.969  60.042 1   64.57  ? 137 PHE   C CA  1 
ATOM   6366  C  C   . PHE   C 1 115 ? 63.753 65.797  59.047 1   62.86  ? 137 PHE   C C   1 
ATOM   6367  O  O   . PHE   C 1 115 ? 64.696 65.012  58.925 1   63.16  ? 137 PHE   C O   1 
ATOM   6368  C  CB  . PHE   C 1 115 ? 64.455 68.213  59.377 1   64.63  ? 137 PHE   C CB  1 
ATOM   6369  C  CG  . PHE   C 1 115 ? 65.91  68.074  58.992 1   65.61  ? 137 PHE   C CG  1 
ATOM   6370  C  CD1 . PHE   C 1 115 ? 66.276 67.541  57.767 1   66.62  ? 137 PHE   C CD1 1 
ATOM   6371  C  CD2 . PHE   C 1 115 ? 66.911 68.486  59.85  1   66.43  ? 137 PHE   C CD2 1 
ATOM   6372  C  CE1 . PHE   C 1 115 ? 67.612 67.359  57.442 1   67.38  ? 137 PHE   C CE1 1 
ATOM   6373  C  CE2 . PHE   C 1 115 ? 68.247 68.315  59.514 1   67.23  ? 137 PHE   C CE2 1 
ATOM   6374  C  CZ  . PHE   C 1 115 ? 68.589 67.779  58.3   1   67.16  ? 137 PHE   C CZ  1 
ATOM   6375  N  N   . GLN   C 1 116 ? 62.633 65.669  58.35  1   61.12  ? 138 GLN   C N   1 
ATOM   6376  C  CA  . GLN   C 1 116 ? 62.473 64.618  57.344 1   60     ? 138 GLN   C CA  1 
ATOM   6377  C  C   . GLN   C 1 116 ? 63.393 64.91   56.113 1   58.57  ? 138 GLN   C C   1 
ATOM   6378  O  O   . GLN   C 1 116 ? 64.42  64.246  55.929 1   59.18  ? 138 GLN   C O   1 
ATOM   6379  C  CB  . GLN   C 1 116 ? 60.99  64.518  56.95  1   60.93  ? 138 GLN   C CB  1 
ATOM   6380  C  CG  . GLN   C 1 116 ? 60.648 63.295  56.143 1   63.28  ? 138 GLN   C CG  1 
ATOM   6381  C  CD  . GLN   C 1 116 ? 60.686 62.088  57.035 1   68.12  ? 138 GLN   C CD  1 
ATOM   6382  O  OE1 . GLN   C 1 116 ? 61.628 61.287  57.008 1   69.83  ? 138 GLN   C OE1 1 
ATOM   6383  N  NE2 . GLN   C 1 116 ? 59.681 61.95   57.885 1   69.06  ? 138 GLN   C NE2 1 
ATOM   6384  N  N   . SER   C 1 117 ? 63.074 65.967  55.35  1   56.28  ? 139 SER   C N   1 
ATOM   6385  C  CA  . SER   C 1 117 ? 63.803 66.417  54.177 1   54.43  ? 139 SER   C CA  1 
ATOM   6386  C  C   . SER   C 1 117 ? 64.738 67.582  54.522 1   52.44  ? 139 SER   C C   1 
ATOM   6387  O  O   . SER   C 1 117 ? 64.296 68.551  55.13  1   52.11  ? 139 SER   C O   1 
ATOM   6388  C  CB  . SER   C 1 117 ? 62.797 66.88   53.127 1   55.41  ? 139 SER   C CB  1 
ATOM   6389  O  OG  . SER   C 1 117 ? 63.391 67.613  52.069 1   57.64  ? 139 SER   C OG  1 
ATOM   6390  N  N   . LEU   C 1 118 ? 66.003 67.52   54.081 1   51.27  ? 140 LEU   C N   1 
ATOM   6391  C  CA  . LEU   C 1 118 ? 66.947 68.623  54.293 1   50.68  ? 140 LEU   C CA  1 
ATOM   6392  C  C   . LEU   C 1 118 ? 66.493 69.848  53.516 1   50.24  ? 140 LEU   C C   1 
ATOM   6393  O  O   . LEU   C 1 118 ? 66.538 70.959  54.035 1   50.29  ? 140 LEU   C O   1 
ATOM   6394  C  CB  . LEU   C 1 118 ? 68.382 68.231  53.875 1   50.6   ? 140 LEU   C CB  1 
ATOM   6395  C  CG  . LEU   C 1 118 ? 69.436 69.353  53.808 1   51.61  ? 140 LEU   C CG  1 
ATOM   6396  C  CD1 . LEU   C 1 118 ? 69.823 69.848  55.188 1   51.72  ? 140 LEU   C CD1 1 
ATOM   6397  C  CD2 . LEU   C 1 118 ? 70.669 68.91   53.039 1   52.09  ? 140 LEU   C CD2 1 
ATOM   6398  N  N   . GLN   C 1 119 ? 66.038 69.64   52.272 1   49.52  ? 141 GLN   C N   1 
ATOM   6399  C  CA  . GLN   C 1 119 ? 65.599 70.716  51.398 1   48.33  ? 141 GLN   C CA  1 
ATOM   6400  C  C   . GLN   C 1 119 ? 64.348 71.409  51.886 1   46.93  ? 141 GLN   C C   1 
ATOM   6401  O  O   . GLN   C 1 119 ? 64.282 72.629  51.781 1   47.27  ? 141 GLN   C O   1 
ATOM   6402  C  CB  . GLN   C 1 119 ? 65.451 70.224  49.956 1   49.47  ? 141 GLN   C CB  1 
ATOM   6403  C  CG  . GLN   C 1 119 ? 66.802 69.972  49.321 1   50.99  ? 141 GLN   C CG  1 
ATOM   6404  C  CD  . GLN   C 1 119 ? 66.739 69.87   47.826 1   53.47  ? 141 GLN   C CD  1 
ATOM   6405  O  OE1 . GLN   C 1 119 ? 65.929 69.135  47.261 1   54.06  ? 141 GLN   C OE1 1 
ATOM   6406  N  NE2 . GLN   C 1 119 ? 67.629 70.59   47.157 1   54.29  ? 141 GLN   C NE2 1 
ATOM   6407  N  N   . PHE   C 1 120 ? 63.385 70.678  52.463 1   45.55  ? 142 PHE   C N   1 
ATOM   6408  C  CA  . PHE   C 1 120 ? 62.172 71.316  52.984 1   44.97  ? 142 PHE   C CA  1 
ATOM   6409  C  C   . PHE   C 1 120 ? 62.509 72.241  54.144 1   44.55  ? 142 PHE   C C   1 
ATOM   6410  O  O   . PHE   C 1 120 ? 61.935 73.327  54.244 1   44.57  ? 142 PHE   C O   1 
ATOM   6411  C  CB  . PHE   C 1 120 ? 61.122 70.288  53.413 1   44.78  ? 142 PHE   C CB  1 
ATOM   6412  C  CG  . PHE   C 1 120 ? 59.845 70.932  53.902 1   45.33  ? 142 PHE   C CG  1 
ATOM   6413  C  CD1 . PHE   C 1 120 ? 58.94  71.485  53.008 1   46.28  ? 142 PHE   C CD1 1 
ATOM   6414  C  CD2 . PHE   C 1 120 ? 59.547 70.981  55.253 1   45.73  ? 142 PHE   C CD2 1 
ATOM   6415  C  CE1 . PHE   C 1 120 ? 57.761 72.066  53.459 1   46.81  ? 142 PHE   C CE1 1 
ATOM   6416  C  CE2 . PHE   C 1 120 ? 58.361 71.547  55.698 1   46.32  ? 142 PHE   C CE2 1 
ATOM   6417  C  CZ  . PHE   C 1 120 ? 57.486 72.106  54.804 1   46.26  ? 142 PHE   C CZ  1 
ATOM   6418  N  N   . ARG   C 1 121 ? 63.446 71.815  55.013 1   43.89  ? 143 ARG   C N   1 
ATOM   6419  C  CA  . ARG   C 1 121 ? 63.907 72.617  56.142 1   43.98  ? 143 ARG   C CA  1 
ATOM   6420  C  C   . ARG   C 1 121 ? 64.67  73.839  55.669 1   42.52  ? 143 ARG   C C   1 
ATOM   6421  O  O   . ARG   C 1 121 ? 64.468 74.917  56.21  1   42.31  ? 143 ARG   C O   1 
ATOM   6422  C  CB  . ARG   C 1 121 ? 64.764 71.796  57.115 1   46.97  ? 143 ARG   C CB  1 
ATOM   6423  C  CG  . ARG   C 1 121 ? 63.985 71.321  58.327 1   52.25  ? 143 ARG   C CG  1 
ATOM   6424  C  CD  . ARG   C 1 121 ? 63.667 72.43   59.32  1   57.23  ? 143 ARG   C CD  1 
ATOM   6425  N  NE  . ARG   C 1 121 ? 64.868 73.004  59.932 1   61.79  ? 143 ARG   C NE  1 
ATOM   6426  C  CZ  . ARG   C 1 121 ? 65.275 72.748  61.18  1   64.12  ? 143 ARG   C CZ  1 
ATOM   6427  N  NH1 . ARG   C 1 121 ? 64.588 71.909  61.953 1   63.2   ? 143 ARG   C NH1 1 
ATOM   6428  N  NH2 . ARG   C 1 121 ? 66.375 73.328  61.66  1   63.02  ? 143 ARG   C NH2 1 
ATOM   6429  N  N   . LEU   C 1 122 ? 65.497 73.697  54.631 1   41.74  ? 144 LEU   C N   1 
ATOM   6430  C  CA  . LEU   C 1 122 ? 66.227 74.83   54.071 1   41.57  ? 144 LEU   C CA  1 
ATOM   6431  C  C   . LEU   C 1 122 ? 65.255 75.898  53.539 1   41.52  ? 144 LEU   C C   1 
ATOM   6432  O  O   . LEU   C 1 122 ? 65.527 77.073  53.705 1   41.61  ? 144 LEU   C O   1 
ATOM   6433  C  CB  . LEU   C 1 122 ? 67.186 74.377  52.965 1   41.26  ? 144 LEU   C CB  1 
ATOM   6434  C  CG  . LEU   C 1 122 ? 68.416 73.591  53.404 1   41.91  ? 144 LEU   C CG  1 
ATOM   6435  C  CD1 . LEU   C 1 122 ? 69.25  73.21   52.211 1   42.11  ? 144 LEU   C CD1 1 
ATOM   6436  C  CD2 . LEU   C 1 122 ? 69.257 74.375  54.403 1   42.61  ? 144 LEU   C CD2 1 
ATOM   6437  N  N   . ILE   C 1 123 ? 64.102 75.485  52.973 1   41.03  ? 145 ILE   C N   1 
ATOM   6438  C  CA  . ILE   C 1 123 ? 63.066 76.399  52.485 1   40.85  ? 145 ILE   C CA  1 
ATOM   6439  C  C   . ILE   C 1 123 ? 62.426 77.118  53.663 1   41.09  ? 145 ILE   C C   1 
ATOM   6440  O  O   . ILE   C 1 123 ? 62.33  78.341  53.645 1   42.06  ? 145 ILE   C O   1 
ATOM   6441  C  CB  . ILE   C 1 123 ? 62.012 75.639  51.627 1   41.06  ? 145 ILE   C CB  1 
ATOM   6442  C  CG1 . ILE   C 1 123 ? 62.646 75.131  50.309 1   41.63  ? 145 ILE   C CG1 1 
ATOM   6443  C  CG2 . ILE   C 1 123 ? 60.76  76.505  51.364 1   41.13  ? 145 ILE   C CG2 1 
ATOM   6444  C  CD1 . ILE   C 1 123 ? 61.819 74.211  49.519 1   42.71  ? 145 ILE   C CD1 1 
ATOM   6445  N  N   . GLU   C 1 124 ? 62.018 76.367  54.705 1   40.18  ? 146 GLU   C N   1 
ATOM   6446  C  CA  . GLU   C 1 124 ? 61.413 76.913  55.924 1   39.61  ? 146 GLU   C CA  1 
ATOM   6447  C  C   . GLU   C 1 124 ? 62.334 77.963  56.556 1   39.16  ? 146 GLU   C C   1 
ATOM   6448  O  O   . GLU   C 1 124 ? 61.899 79.067  56.838 1   38.89  ? 146 GLU   C O   1 
ATOM   6449  C  CB  . GLU   C 1 124 ? 61.146 75.789  56.942 1   41.19  ? 146 GLU   C CB  1 
ATOM   6450  C  CG  . GLU   C 1 124 ? 59.894 74.975  56.687 1   45.08  ? 146 GLU   C CG  1 
ATOM   6451  C  CD  . GLU   C 1 124 ? 59.669 73.914  57.748 1   50.8   ? 146 GLU   C CD  1 
ATOM   6452  O  OE1 . GLU   C 1 124 ? 60.627 73.166  58.049 1   51.04  ? 146 GLU   C OE1 1 
ATOM   6453  O  OE2 . GLU   C 1 124 ? 58.531 73.81   58.261 1   53.65  ? 146 GLU   C OE2 1 
ATOM   6454  N  N   . ASN   C 1 125 ? 63.619 77.639  56.71  1   39.03  ? 147 ASN   C N   1 
ATOM   6455  C  CA  . ASN   C 1 125 ? 64.6   78.539  57.288 1   39.53  ? 147 ASN   C CA  1 
ATOM   6456  C  C   . ASN   C 1 125 ? 64.892 79.752  56.406 1   40.15  ? 147 ASN   C C   1 
ATOM   6457  O  O   . ASN   C 1 125 ? 64.891 80.872  56.922 1   40.52  ? 147 ASN   C O   1 
ATOM   6458  C  CB  . ASN   C 1 125 ? 65.882 77.795  57.611 1   40.94  ? 147 ASN   C CB  1 
ATOM   6459  C  CG  . ASN   C 1 125 ? 65.75  76.77   58.712 1   44.57  ? 147 ASN   C CG  1 
ATOM   6460  O  OD1 . ASN   C 1 125 ? 64.783 76.772  59.498 1   45.26  ? 147 ASN   C OD1 1 
ATOM   6461  N  ND2 . ASN   C 1 125 ? 66.733 75.863  58.792 1   45.46  ? 147 ASN   C ND2 1 
ATOM   6462  N  N   . LYS   C 1 126 ? 65.12  79.552  55.089 1   40.2   ? 148 LYS   C N   1 
ATOM   6463  C  CA  . LYS   C 1 126 ? 65.386 80.66   54.168 1   41.23  ? 148 LYS   C CA  1 
ATOM   6464  C  C   . LYS   C 1 126 ? 64.196 81.606  54.017 1   42.4   ? 148 LYS   C C   1 
ATOM   6465  O  O   . LYS   C 1 126 ? 64.398 82.789  53.774 1   42.03  ? 148 LYS   C O   1 
ATOM   6466  C  CB  . LYS   C 1 126 ? 65.871 80.172  52.8   1   43.08  ? 148 LYS   C CB  1 
ATOM   6467  C  CG  . LYS   C 1 126 ? 67.271 79.571  52.812 1   46.96  ? 148 LYS   C CG  1 
ATOM   6468  C  CD  . LYS   C 1 126 ? 67.485 78.678  51.594 1   50.09  ? 148 LYS   C CD  1 
ATOM   6469  C  CE  . LYS   C 1 126 ? 68.781 77.923  51.678 1   53.36  ? 148 LYS   C CE  1 
ATOM   6470  N  NZ  . LYS   C 1 126 ? 69.926 78.828  51.459 1   55.35  ? 148 LYS   C NZ  1 
ATOM   6471  N  N   . LEU   C 1 127 ? 62.96  81.1    54.156 1   43.58  ? 149 LEU   C N   1 
ATOM   6472  C  CA  . LEU   C 1 127 ? 61.772 81.958  54.104 1   44.95  ? 149 LEU   C CA  1 
ATOM   6473  C  C   . LEU   C 1 127 ? 61.714 82.767  55.405 1   46.99  ? 149 LEU   C C   1 
ATOM   6474  O  O   . LEU   C 1 127 ? 61.53  83.983  55.362 1   47.88  ? 149 LEU   C O   1 
ATOM   6475  C  CB  . LEU   C 1 127 ? 60.486 81.138  53.912 1   44.56  ? 149 LEU   C CB  1 
ATOM   6476  C  CG  . LEU   C 1 127 ? 59.223 81.959  53.764 1   45.61  ? 149 LEU   C CG  1 
ATOM   6477  C  CD1 . LEU   C 1 127 ? 59.253 82.763  52.498 1   46.37  ? 149 LEU   C CD1 1 
ATOM   6478  C  CD2 . LEU   C 1 127 ? 58.007 81.075  53.744 1   46.25  ? 149 LEU   C CD2 1 
ATOM   6479  N  N   . GLY   C 1 128 ? 61.928 82.104  56.542 1   47.57  ? 150 GLY   C N   1 
ATOM   6480  C  CA  . GLY   C 1 128 ? 61.946 82.779  57.828 1   49.01  ? 150 GLY   C CA  1 
ATOM   6481  C  C   . GLY   C 1 128 ? 61.17  82.105  58.942 1   50.62  ? 150 GLY   C C   1 
ATOM   6482  O  O   . GLY   C 1 128 ? 60.779 82.769  59.901 1   50.71  ? 150 GLY   C O   1 
ATOM   6483  N  N   . VAL   C 1 129 ? 60.953 80.797  58.849 1   52.09  ? 151 VAL   C N   1 
ATOM   6484  C  CA  . VAL   C 1 129 ? 60.229 80.053  59.877 1   54.28  ? 151 VAL   C CA  1 
ATOM   6485  C  C   . VAL   C 1 129 ? 61.094 79.832  61.122 1   56.62  ? 151 VAL   C C   1 
ATOM   6486  O  O   . VAL   C 1 129 ? 62.27  79.484  61.004 1   55.73  ? 151 VAL   C O   1 
ATOM   6487  C  CB  . VAL   C 1 129 ? 59.726 78.675  59.358 1   55.05  ? 151 VAL   C CB  1 
ATOM   6488  C  CG1 . VAL   C 1 129 ? 59.119 77.848  60.477 1   55.84  ? 151 VAL   C CG1 1 
ATOM   6489  C  CG2 . VAL   C 1 129 ? 58.73  78.815  58.227 1   55.68  ? 151 VAL   C CG2 1 
ATOM   6490  N  N   . LEU   C 1 130 ? 60.464 79.962  62.325 1   59.07  ? 152 LEU   C N   1 
ATOM   6491  C  CA  . LEU   C 1 130 ? 61.015 79.587  63.633 1   61.35  ? 152 LEU   C CA  1 
ATOM   6492  C  C   . LEU   C 1 130 ? 60.455 78.168  63.882 1   63.3   ? 152 LEU   C C   1 
ATOM   6493  O  O   . LEU   C 1 130 ? 59.263 78.026  64.179 1   63.34  ? 152 LEU   C O   1 
ATOM   6494  C  CB  . LEU   C 1 130 ? 60.61  80.555  64.771 1   61.78  ? 152 LEU   C CB  1 
ATOM   6495  C  CG  . LEU   C 1 130 ? 59.268 81.298  64.7   1   62.92  ? 152 LEU   C CG  1 
ATOM   6496  C  CD1 . LEU   C 1 130 ? 58.247 80.688  65.668 1   63.42  ? 152 LEU   C CD1 1 
ATOM   6497  C  CD2 . LEU   C 1 130 ? 59.466 82.77   65.042 1   63.17  ? 152 LEU   C CD2 1 
ATOM   6498  N  N   . THR   C 1 131 ? 61.294 77.125  63.644 1   64.39  ? 153 THR   C N   1 
ATOM   6499  C  CA  . THR   C 1 131 ? 60.903 75.709  63.712 1   65.59  ? 153 THR   C CA  1 
ATOM   6500  C  C   . THR   C 1 131 ? 60.689 75.212  65.146 1   66.3   ? 153 THR   C C   1 
ATOM   6501  O  O   . THR   C 1 131 ? 61.457 74.386  65.657 1   66.52  ? 153 THR   C O   1 
ATOM   6502  C  CB  . THR   C 1 131 ? 61.862 74.787  62.931 1   67.37  ? 153 THR   C CB  1 
ATOM   6503  O  OG1 . THR   C 1 131 ? 62.451 75.459  61.805 1   68.65  ? 153 THR   C OG1 1 
ATOM   6504  C  CG2 . THR   C 1 131 ? 61.164 73.51   62.456 1   68.02  ? 153 THR   C CG2 1 
ATOM   6505  N  N   . GLU   C 1 132 ? 59.602 75.674  65.772 1   66.21  ? 154 GLU   C N   1 
ATOM   6506  C  CA  . GLU   C 1 132 ? 59.234 75.316  67.14  1   66.38  ? 154 GLU   C CA  1 
ATOM   6507  C  C   . GLU   C 1 132 ? 58.419 74.02   67.206 1   66.33  ? 154 GLU   C C   1 
ATOM   6508  O  O   . GLU   C 1 132 ? 58.256 73.444  68.281 1   66.16  ? 154 GLU   C O   1 
ATOM   6509  C  CB  . GLU   C 1 132 ? 58.464 76.468  67.799 1   68.12  ? 154 GLU   C CB  1 
ATOM   6510  N  N   . SER   C 1 146 ? 72.441 66.691  60.029 1   67.68  ? 168 SER   C N   1 
ATOM   6511  C  CA  . SER   C 1 146 ? 72.762 65.338  60.491 1   68.69  ? 168 SER   C CA  1 
ATOM   6512  C  C   . SER   C 1 146 ? 73.721 64.601  59.506 1   69.44  ? 168 SER   C C   1 
ATOM   6513  O  O   . SER   C 1 146 ? 73.453 63.48   59.065 1   69.77  ? 168 SER   C O   1 
ATOM   6514  C  CB  . SER   C 1 146 ? 71.478 64.545  60.72  1   68.91  ? 168 SER   C CB  1 
ATOM   6515  N  N   . ASP   C 1 147 ? 74.864 65.265  59.223 1   69.45  ? 169 ASP   C N   1 
ATOM   6516  C  CA  . ASP   C 1 147 ? 76.037 65.019  58.319 1   69.44  ? 169 ASP   C CA  1 
ATOM   6517  C  C   . ASP   C 1 147 ? 76.838 66.362  58.32  1   68.89  ? 169 ASP   C C   1 
ATOM   6518  O  O   . ASP   C 1 147 ? 76.211 67.356  58.668 1   69.49  ? 169 ASP   C O   1 
ATOM   6519  C  CB  . ASP   C 1 147 ? 75.592 64.742  56.873 1   70.84  ? 169 ASP   C CB  1 
ATOM   6520  C  CG  . ASP   C 1 147 ? 76.784 64.502  55.992 1   74.24  ? 169 ASP   C CG  1 
ATOM   6521  O  OD1 . ASP   C 1 147 ? 77.609 63.656  56.354 1   74.7   ? 169 ASP   C OD1 1 
ATOM   6522  O  OD2 . ASP   C 1 147 ? 76.924 65.214  54.97  1   76     ? 169 ASP   C OD2 1 
ATOM   6523  N  N   . GLU   C 1 148 ? 78.155 66.448  57.937 1   67.47  ? 170 GLU   C N   1 
ATOM   6524  C  CA  . GLU   C 1 148 ? 78.82  67.777  58.03  1   66.74  ? 170 GLU   C CA  1 
ATOM   6525  C  C   . GLU   C 1 148 ? 78.416 68.735  56.926 1   66.41  ? 170 GLU   C C   1 
ATOM   6526  O  O   . GLU   C 1 148 ? 78.418 69.94   57.153 1   66.36  ? 170 GLU   C O   1 
ATOM   6527  C  CB  . GLU   C 1 148 ? 80.339 67.741  58.172 1   67.57  ? 170 GLU   C CB  1 
ATOM   6528  C  CG  . GLU   C 1 148 ? 80.831 67.752  59.613 1   69.71  ? 170 GLU   C CG  1 
ATOM   6529  C  CD  . GLU   C 1 148 ? 80.569 68.969  60.486 1   72.06  ? 170 GLU   C CD  1 
ATOM   6530  O  OE1 . GLU   C 1 148 ? 81.053 70.074  60.148 1   71.57  ? 170 GLU   C OE1 1 
ATOM   6531  O  OE2 . GLU   C 1 148 ? 79.931 68.799  61.55  1   72.62  ? 170 GLU   C OE2 1 
ATOM   6532  N  N   . GLU   C 1 149 ? 78.049 68.22   55.755 1   65.98  ? 171 GLU   C N   1 
ATOM   6533  C  CA  . GLU   C 1 149 ? 77.603 69.066  54.648 1   65.75  ? 171 GLU   C CA  1 
ATOM   6534  C  C   . GLU   C 1 149 ? 76.182 69.585  54.963 1   64.51  ? 171 GLU   C C   1 
ATOM   6535  O  O   . GLU   C 1 149 ? 75.902 70.778  54.792 1   64.66  ? 171 GLU   C O   1 
ATOM   6536  C  CB  . GLU   C 1 149 ? 77.602 68.247  53.342 1   68.76  ? 171 GLU   C CB  1 
ATOM   6537  C  CG  . GLU   C 1 149 ? 77.41  69.08   52.089 1   74.71  ? 171 GLU   C CG  1 
ATOM   6538  C  CD  . GLU   C 1 149 ? 78.671 69.316  51.279 1   80.54  ? 171 GLU   C CD  1 
ATOM   6539  O  OE1 . GLU   C 1 149 ? 78.577 69.272  50.031 1   81.3   ? 171 GLU   C OE1 1 
ATOM   6540  O  OE2 . GLU   C 1 149 ? 79.745 69.544  51.886 1   81.94  ? 171 GLU   C OE2 1 
ATOM   6541  N  N   . ALA   C 1 150 ? 75.303 68.677  55.451 1   62.88  ? 172 ALA   C N   1 
ATOM   6542  C  CA  . ALA   C 1 150 ? 73.924 68.986  55.811 1   61.77  ? 172 ALA   C CA  1 
ATOM   6543  C  C   . ALA   C 1 150 ? 73.857 69.87   57.06  1   60.87  ? 172 ALA   C C   1 
ATOM   6544  O  O   . ALA   C 1 150 ? 72.974 70.72   57.162 1   61.33  ? 172 ALA   C O   1 
ATOM   6545  C  CB  . ALA   C 1 150 ? 73.145 67.7    56.037 1   61.65  ? 172 ALA   C CB  1 
ATOM   6546  N  N   . ARG   C 1 151 ? 74.778 69.669  58.011 1   59.45  ? 173 ARG   C N   1 
ATOM   6547  C  CA  . ARG   C 1 151 ? 74.832 70.457  59.234 1   58.78  ? 173 ARG   C CA  1 
ATOM   6548  C  C   . ARG   C 1 151 ? 75.205 71.871  58.897 1   57.94  ? 173 ARG   C C   1 
ATOM   6549  O  O   . ARG   C 1 151 ? 74.608 72.786  59.443 1   58.1   ? 173 ARG   C O   1 
ATOM   6550  C  CB  . ARG   C 1 151 ? 75.852 69.894  60.24  1   60.29  ? 173 ARG   C CB  1 
ATOM   6551  C  CG  . ARG   C 1 151 ? 75.284 69.684  61.637 1   63.89  ? 173 ARG   C CG  1 
ATOM   6552  C  CD  . ARG   C 1 151 ? 76.366 69.554  62.686 1   66.65  ? 173 ARG   C CD  1 
ATOM   6553  N  NE  . ARG   C 1 151 ? 77.069 70.819  62.912 1   69.48  ? 173 ARG   C NE  1 
ATOM   6554  C  CZ  . ARG   C 1 151 ? 76.89  71.601  63.971 1   72.38  ? 173 ARG   C CZ  1 
ATOM   6555  N  NH1 . ARG   C 1 151 ? 77.577 72.73   64.094 1   72.85  ? 173 ARG   C NH1 1 
ATOM   6556  N  NH2 . ARG   C 1 151 ? 76.021 71.262  64.918 1   72.29  ? 173 ARG   C NH2 1 
ATOM   6557  N  N   . ASN   C 1 152 ? 76.192 72.058  58.006 1   57.12  ? 174 ASN   C N   1 
ATOM   6558  C  CA  . ASN   C 1 152 ? 76.659 73.368  57.579 1   56.8   ? 174 ASN   C CA  1 
ATOM   6559  C  C   . ASN   C 1 152 ? 75.55  74.103  56.839 1   55.85  ? 174 ASN   C C   1 
ATOM   6560  O  O   . ASN   C 1 152 ? 75.351 75.284  57.081 1   56.15  ? 174 ASN   C O   1 
ATOM   6561  C  CB  . ASN   C 1 152 ? 77.893 73.218  56.702 1   58.23  ? 174 ASN   C CB  1 
ATOM   6562  C  CG  . ASN   C 1 152 ? 78.67  74.491  56.544 1   61.47  ? 174 ASN   C CG  1 
ATOM   6563  O  OD1 . ASN   C 1 152 ? 79.146 75.082  57.52  1   61.66  ? 174 ASN   C OD1 1 
ATOM   6564  N  ND2 . ASN   C 1 152 ? 78.827 74.925  55.294 1   62.86  ? 174 ASN   C ND2 1 
ATOM   6565  N  N   . SER   C 1 153 ? 74.801 73.395  55.982 1   54.76  ? 175 SER   C N   1 
ATOM   6566  C  CA  . SER   C 1 153 ? 73.672 73.95   55.242 1   54.43  ? 175 SER   C CA  1 
ATOM   6567  C  C   . SER   C 1 153 ? 72.617 74.527  56.183 1   54.37  ? 175 SER   C C   1 
ATOM   6568  O  O   . SER   C 1 153 ? 72.217 75.675  56.018 1   54.33  ? 175 SER   C O   1 
ATOM   6569  C  CB  . SER   C 1 153 ? 73.023 72.877  54.364 1   55.85  ? 175 SER   C CB  1 
ATOM   6570  O  OG  . SER   C 1 153 ? 73.884 72.392  53.35  1   58.77  ? 175 SER   C OG  1 
ATOM   6571  N  N   . ILE   C 1 154 ? 72.176 73.737  57.183 1   54.32  ? 176 ILE   C N   1 
ATOM   6572  C  CA  . ILE   C 1 154 ? 71.15  74.149  58.135 1   54.07  ? 176 ILE   C CA  1 
ATOM   6573  C  C   . ILE   C 1 154 ? 71.672 75.227  59.069 1   54.11  ? 176 ILE   C C   1 
ATOM   6574  O  O   . ILE   C 1 154 ? 70.947 76.18   59.345 1   54.25  ? 176 ILE   C O   1 
ATOM   6575  C  CB  . ILE   C 1 154 ? 70.513 72.931  58.847 1   54.27  ? 176 ILE   C CB  1 
ATOM   6576  C  CG1 . ILE   C 1 154 ? 69.455 72.338  57.881 1   55.39  ? 176 ILE   C CG1 1 
ATOM   6577  C  CG2 . ILE   C 1 154 ? 69.905 73.292  60.226 1   54.43  ? 176 ILE   C CG2 1 
ATOM   6578  C  CD1 . ILE   C 1 154 ? 68.554 71.35   58.357 1   56.82  ? 176 ILE   C CD1 1 
ATOM   6579  N  N   . ARG   C 1 155 ? 72.948 75.157  59.466 1   54.14  ? 177 ARG   C N   1 
ATOM   6580  C  CA  . ARG   C 1 155 ? 73.549 76.186  60.315 1   54.55  ? 177 ARG   C CA  1 
ATOM   6581  C  C   . ARG   C 1 155 ? 73.504 77.537  59.608 1   54.27  ? 177 ARG   C C   1 
ATOM   6582  O  O   . ARG   C 1 155 ? 72.923 78.473  60.138 1   53.83  ? 177 ARG   C O   1 
ATOM   6583  C  CB  . ARG   C 1 155 ? 74.991 75.809  60.688 1   56.75  ? 177 ARG   C CB  1 
ATOM   6584  C  CG  . ARG   C 1 155 ? 75.176 75.456  62.157 1   62.2   ? 177 ARG   C CG  1 
ATOM   6585  C  CD  . ARG   C 1 155 ? 75.268 76.703  63.021 1   67.35  ? 177 ARG   C CD  1 
ATOM   6586  N  NE  . ARG   C 1 155 ? 75.13  76.401  64.448 1   70.93  ? 177 ARG   C NE  1 
ATOM   6587  C  CZ  . ARG   C 1 155 ? 76.152 76.153  65.267 1   73.72  ? 177 ARG   C CZ  1 
ATOM   6588  N  NH1 . ARG   C 1 155 ? 77.4   76.159  64.806 1   73.14  ? 177 ARG   C NH1 1 
ATOM   6589  N  NH2 . ARG   C 1 155 ? 75.934 75.886  66.55  1   73.56  ? 177 ARG   C NH2 1 
ATOM   6590  N  N   . ASN   C 1 156 ? 73.99  77.585  58.358 1   54.62  ? 178 ASN   C N   1 
ATOM   6591  C  CA  . ASN   C 1 156 ? 74.006 78.789  57.544 1   55.41  ? 178 ASN   C CA  1 
ATOM   6592  C  C   . ASN   C 1 156 ? 72.619 79.317  57.228 1   55.19  ? 178 ASN   C C   1 
ATOM   6593  O  O   . ASN   C 1 156 ? 72.449 80.517  57.202 1   55.85  ? 178 ASN   C O   1 
ATOM   6594  C  CB  . ASN   C 1 156 ? 74.82  78.574  56.267 1   57.87  ? 178 ASN   C CB  1 
ATOM   6595  C  CG  . ASN   C 1 156 ? 76.292 78.34   56.521 1   63.09  ? 178 ASN   C CG  1 
ATOM   6596  O  OD1 . ASN   C 1 156 ? 76.791 78.488  57.65  1   64.62  ? 178 ASN   C OD1 1 
ATOM   6597  N  ND2 . ASN   C 1 156 ? 77.026 77.952  55.479 1   64.53  ? 178 ASN   C ND2 1 
ATOM   6598  N  N   . SER   C 1 157 ? 71.622 78.451  57.021 1   54.6   ? 179 SER   C N   1 
ATOM   6599  C  CA  . SER   C 1 157 ? 70.246 78.896  56.741 1   54.33  ? 179 SER   C CA  1 
ATOM   6600  C  C   . SER   C 1 157 ? 69.608 79.612  57.935 1   54.52  ? 179 SER   C C   1 
ATOM   6601  O  O   . SER   C 1 157 ? 68.708 80.424  57.747 1   54.94  ? 179 SER   C O   1 
ATOM   6602  C  CB  . SER   C 1 157 ? 69.37  77.723  56.308 1   55.14  ? 179 SER   C CB  1 
ATOM   6603  O  OG  . SER   C 1 157 ? 69.067 76.858  57.392 1   56.57  ? 179 SER   C OG  1 
ATOM   6604  N  N   . GLU   C 1 158 ? 70.072 79.319  59.157 1   54.4   ? 180 GLU   C N   1 
ATOM   6605  C  CA  . GLU   C 1 158 ? 69.573 79.944  60.378 1   54.67  ? 180 GLU   C CA  1 
ATOM   6606  C  C   . GLU   C 1 158 ? 70.353 81.224  60.685 1   54.91  ? 180 GLU   C C   1 
ATOM   6607  O  O   . GLU   C 1 158 ? 69.765 82.207  61.126 1   54.78  ? 180 GLU   C O   1 
ATOM   6608  C  CB  . GLU   C 1 158 ? 69.682 78.963  61.555 1   56.45  ? 180 GLU   C CB  1 
ATOM   6609  C  CG  . GLU   C 1 158 ? 68.769 77.76   61.423 1   60.38  ? 180 GLU   C CG  1 
ATOM   6610  C  CD  . GLU   C 1 158 ? 68.995 76.645  62.429 1   64.74  ? 180 GLU   C CD  1 
ATOM   6611  O  OE1 . GLU   C 1 158 ? 70.041 76.66   63.117 1   64.53  ? 180 GLU   C OE1 1 
ATOM   6612  O  OE2 . GLU   C 1 158 ? 68.126 75.748  62.518 1   66.9   ? 180 GLU   C OE2 1 
ATOM   6613  N  N   . LYS   C 1 159 ? 71.673 81.211  60.447 1   55.21  ? 181 LYS   C N   1 
ATOM   6614  C  CA  . LYS   C 1 159 ? 72.534 82.359  60.717 1   56.2   ? 181 LYS   C CA  1 
ATOM   6615  C  C   . LYS   C 1 159 ? 72.374 83.472  59.675 1   56.11  ? 181 LYS   C C   1 
ATOM   6616  O  O   . LYS   C 1 159 ? 72.175 84.625  60.043 1   56.61  ? 181 LYS   C O   1 
ATOM   6617  C  CB  . LYS   C 1 159 ? 74.012 81.937  60.845 1   59.29  ? 181 LYS   C CB  1 
ATOM   6618  C  CG  . LYS   C 1 159 ? 74.288 80.851  61.898 1   65.78  ? 181 LYS   C CG  1 
ATOM   6619  C  CD  . LYS   C 1 159 ? 73.901 81.252  63.333 1   72.14  ? 181 LYS   C CD  1 
ATOM   6620  C  CE  . LYS   C 1 159 ? 74.113 80.123  64.331 1   76.91  ? 181 LYS   C CE  1 
ATOM   6621  N  NZ  . LYS   C 1 159 ? 73.198 80.232  65.509 1   79.7   ? 181 LYS   C NZ  1 
ATOM   6622  N  N   . ASP   C 1 160 ? 72.457 83.134  58.383 1   55.23  ? 182 ASP   C N   1 
ATOM   6623  C  CA  . ASP   C 1 160 ? 72.329 84.119  57.312 1   54.77  ? 182 ASP   C CA  1 
ATOM   6624  C  C   . ASP   C 1 160 ? 70.921 84.706  57.235 1   53.99  ? 182 ASP   C C   1 
ATOM   6625  O  O   . ASP   C 1 160 ? 69.956 84.05   57.623 1   54.05  ? 182 ASP   C O   1 
ATOM   6626  C  CB  . ASP   C 1 160 ? 72.797 83.538  55.967 1   56.36  ? 182 ASP   C CB  1 
ATOM   6627  C  CG  . ASP   C 1 160 ? 74.201 82.962  56.002 1   60.39  ? 182 ASP   C CG  1 
ATOM   6628  O  OD1 . ASP   C 1 160 ? 74.954 83.267  56.968 1   60.9   ? 182 ASP   C OD1 1 
ATOM   6629  O  OD2 . ASP   C 1 160 ? 74.547 82.199  55.076 1   62.13  ? 182 ASP   C OD2 1 
ATOM   6630  N  N   . PRO   C 1 161 ? 70.792 85.971  56.792 1   53.17  ? 183 PRO   C N   1 
ATOM   6631  C  CA  . PRO   C 1 161 ? 69.475 86.608  56.791 1   52.13  ? 183 PRO   C CA  1 
ATOM   6632  C  C   . PRO   C 1 161 ? 68.434 85.938  55.915 1   51.29  ? 183 PRO   C C   1 
ATOM   6633  O  O   . PRO   C 1 161 ? 68.634 85.728  54.718 1   51.74  ? 183 PRO   C O   1 
ATOM   6634  C  CB  . PRO   C 1 161 ? 69.771 88.046  56.354 1   52.8   ? 183 PRO   C CB  1 
ATOM   6635  C  CG  . PRO   C 1 161 ? 71.058 87.975  55.634 1   53.7   ? 183 PRO   C CG  1 
ATOM   6636  C  CD  . PRO   C 1 161 ? 71.838 86.907  56.335 1   52.63  ? 183 PRO   C CD  1 
ATOM   6637  N  N   . SER   C 1 162 ? 67.303 85.611  56.529 1   49.93  ? 184 SER   C N   1 
ATOM   6638  C  CA  . SER   C 1 162 ? 66.174 85.001  55.849 1   48.93  ? 184 SER   C CA  1 
ATOM   6639  C  C   . SER   C 1 162 ? 65.429 86.036  54.979 1   47.86  ? 184 SER   C C   1 
ATOM   6640  O  O   . SER   C 1 162 ? 65.747 87.229  55.013 1   47.92  ? 184 SER   C O   1 
ATOM   6641  C  CB  . SER   C 1 162 ? 65.233 84.381  56.882 1   49.92  ? 184 SER   C CB  1 
ATOM   6642  O  OG  . SER   C 1 162 ? 64.554 85.369  57.634 1   52.81  ? 184 SER   C OG  1 
ATOM   6643  N  N   . LEU   C 1 163 ? 64.439 85.587  54.197 1   46.81  ? 185 LEU   C N   1 
ATOM   6644  C  CA  . LEU   C 1 163 ? 63.632 86.495  53.398 1   46.73  ? 185 LEU   C CA  1 
ATOM   6645  C  C   . LEU   C 1 163 ? 62.852 87.466  54.302 1   47.2   ? 185 LEU   C C   1 
ATOM   6646  O  O   . LEU   C 1 163 ? 62.72  88.63   53.952 1   47.55  ? 185 LEU   C O   1 
ATOM   6647  C  CB  . LEU   C 1 163 ? 62.697 85.731  52.448 1   46.07  ? 185 LEU   C CB  1 
ATOM   6648  C  CG  . LEU   C 1 163 ? 63.366 85.137  51.218 1   46.31  ? 185 LEU   C CG  1 
ATOM   6649  C  CD1 . LEU   C 1 163 ? 62.395 84.326  50.424 1   46.5   ? 185 LEU   C CD1 1 
ATOM   6650  C  CD2 . LEU   C 1 163 ? 63.939 86.209  50.337 1   46.99  ? 185 LEU   C CD2 1 
ATOM   6651  N  N   . LEU   C 1 164 ? 62.401 87.008  55.476 1   47.18  ? 186 LEU   C N   1 
ATOM   6652  C  CA  . LEU   C 1 164 ? 61.706 87.85   56.452 1   48.26  ? 186 LEU   C CA  1 
ATOM   6653  C  C   . LEU   C 1 164 ? 62.595 89.025  56.921 1   49.5   ? 186 LEU   C C   1 
ATOM   6654  O  O   . LEU   C 1 164 ? 62.13  90.165  56.982 1   49.89  ? 186 LEU   C O   1 
ATOM   6655  C  CB  . LEU   C 1 164 ? 61.293 86.998  57.662 1   48.41  ? 186 LEU   C CB  1 
ATOM   6656  C  CG  . LEU   C 1 164 ? 60.603 87.725  58.805 1   49.93  ? 186 LEU   C CG  1 
ATOM   6657  C  CD1 . LEU   C 1 164 ? 59.327 88.382  58.349 1   50.47  ? 186 LEU   C CD1 1 
ATOM   6658  C  CD2 . LEU   C 1 164 ? 60.298 86.774  59.939 1   50.75  ? 186 LEU   C CD2 1 
ATOM   6659  N  N   . GLU   C 1 165 ? 63.871 88.749  57.237 1   49.71  ? 187 GLU   C N   1 
ATOM   6660  C  CA  . GLU   C 1 165 ? 64.796 89.784  57.683 1   50.18  ? 187 GLU   C CA  1 
ATOM   6661  C  C   . GLU   C 1 165 ? 65.12  90.761  56.56  1   49.3   ? 187 GLU   C C   1 
ATOM   6662  O  O   . GLU   C 1 165 ? 65.101 91.965  56.792 1   49.9   ? 187 GLU   C O   1 
ATOM   6663  C  CB  . GLU   C 1 165 ? 66.107 89.177  58.206 1   54.26  ? 187 GLU   C CB  1 
ATOM   6664  C  CG  . GLU   C 1 165 ? 65.987 88.27   59.414 1   62.07  ? 187 GLU   C CG  1 
ATOM   6665  C  CD  . GLU   C 1 165 ? 67.305 87.601  59.76  1   71.54  ? 187 GLU   C CD  1 
ATOM   6666  O  OE1 . GLU   C 1 165 ? 68.356 88.278  59.663 1   73.95  ? 187 GLU   C OE1 1 
ATOM   6667  O  OE2 . GLU   C 1 165 ? 67.29  86.395  60.106 1   73.86  ? 187 GLU   C OE2 1 
ATOM   6668  N  N   . LEU   C 1 166 ? 65.418 90.252  55.35  1   47.99  ? 188 LEU   C N   1 
ATOM   6669  C  CA  . LEU   C 1 166 ? 65.772 91.073  54.193 1   47.19  ? 188 LEU   C CA  1 
ATOM   6670  C  C   . LEU   C 1 166 ? 64.625 91.939  53.685 1   46.95  ? 188 LEU   C C   1 
ATOM   6671  O  O   . LEU   C 1 166 ? 64.861 93.049  53.203 1   46.96  ? 188 LEU   C O   1 
ATOM   6672  C  CB  . LEU   C 1 166 ? 66.33  90.194  53.073 1   47.07  ? 188 LEU   C CB  1 
ATOM   6673  C  CG  . LEU   C 1 166 ? 67.649 89.497  53.399 1   47.82  ? 188 LEU   C CG  1 
ATOM   6674  C  CD1 . LEU   C 1 166 ? 67.956 88.453  52.389 1   48.28  ? 188 LEU   C CD1 1 
ATOM   6675  C  CD2 . LEU   C 1 166 ? 68.794 90.483  53.513 1   47.73  ? 188 LEU   C CD2 1 
ATOM   6676  N  N   . VAL   C 1 167 ? 63.386 91.431  53.784 1   46.77  ? 189 VAL   C N   1 
ATOM   6677  C  CA  . VAL   C 1 167 ? 62.192 92.177  53.379 1   47.03  ? 189 VAL   C CA  1 
ATOM   6678  C  C   . VAL   C 1 167 ? 61.964 93.312  54.374 1   47.36  ? 189 VAL   C C   1 
ATOM   6679  O  O   . VAL   C 1 167 ? 61.657 94.426  53.949 1   47.49  ? 189 VAL   C O   1 
ATOM   6680  C  CB  . VAL   C 1 167 ? 60.949 91.256  53.185 1   47.34  ? 189 VAL   C CB  1 
ATOM   6681  C  CG1 . VAL   C 1 167 ? 59.627 92.006  53.352 1   47.43  ? 189 VAL   C CG1 1 
ATOM   6682  C  CG2 . VAL   C 1 167 ? 61.005 90.57   51.835 1   47.76  ? 189 VAL   C CG2 1 
ATOM   6683  N  N   . GLN   C 1 168 ? 62.173 93.046  55.686 1   47.23  ? 190 GLN   C N   1 
ATOM   6684  C  CA  . GLN   C 1 168 ? 62.036 94.051  56.73  1   47.9   ? 190 GLN   C CA  1 
ATOM   6685  C  C   . GLN   C 1 168 ? 62.981 95.219  56.491 1   48.83  ? 190 GLN   C C   1 
ATOM   6686  O  O   . GLN   C 1 168 ? 62.55  96.361  56.575 1   49.26  ? 190 GLN   C O   1 
ATOM   6687  C  CB  . GLN   C 1 168 ? 62.275 93.445  58.115 1   49.08  ? 190 GLN   C CB  1 
ATOM   6688  C  CG  . GLN   C 1 168 ? 61.014 92.909  58.776 1   51.13  ? 190 GLN   C CG  1 
ATOM   6689  C  CD  . GLN   C 1 168 ? 61.298 92.293  60.121 1   53.67  ? 190 GLN   C CD  1 
ATOM   6690  O  OE1 . GLN   C 1 168 ? 61.03  91.115  60.347 1   54.86  ? 190 GLN   C OE1 1 
ATOM   6691  N  NE2 . GLN   C 1 168 ? 61.856 93.071  61.045 1   53.36  ? 190 GLN   C NE2 1 
ATOM   6692  N  N   . ARG   C 1 169 ? 64.241 94.944  56.122 1   48.92  ? 191 ARG   C N   1 
ATOM   6693  C  CA  . ARG   C 1 169 ? 65.203 96.004  55.854 1   49.71  ? 191 ARG   C CA  1 
ATOM   6694  C  C   . ARG   C 1 169 ? 64.812 96.85   54.645 1   49.82  ? 191 ARG   C C   1 
ATOM   6695  O  O   . ARG   C 1 169 ? 64.992 98.074  54.67  1   50.7   ? 191 ARG   C O   1 
ATOM   6696  C  CB  . ARG   C 1 169 ? 66.613 95.435  55.725 1   52.08  ? 191 ARG   C CB  1 
ATOM   6697  C  CG  . ARG   C 1 169 ? 67.177 95.061  57.08  1   58.26  ? 191 ARG   C CG  1 
ATOM   6698  C  CD  . ARG   C 1 169 ? 68.267 94.025  56.965 1   64.88  ? 191 ARG   C CD  1 
ATOM   6699  N  NE  . ARG   C 1 169 ? 68.275 93.113  58.115 1   71.05  ? 191 ARG   C NE  1 
ATOM   6700  C  CZ  . ARG   C 1 169 ? 68.947 91.963  58.151 1   75.08  ? 191 ARG   C CZ  1 
ATOM   6701  N  NH1 . ARG   C 1 169 ? 69.668 91.573  57.104 1   75.9   ? 191 ARG   C NH1 1 
ATOM   6702  N  NH2 . ARG   C 1 169 ? 68.898 91.191  59.234 1   74.8   ? 191 ARG   C NH2 1 
ATOM   6703  N  N   . TRP   C 1 170 ? 64.233 96.207  53.615 1   48.43  ? 192 TRP   C N   1 
ATOM   6704  C  CA  . TRP   C 1 170 ? 63.75  96.862  52.407 1   47.77  ? 192 TRP   C CA  1 
ATOM   6705  C  C   . TRP   C 1 170 ? 62.553 97.782  52.75  1   46.79  ? 192 TRP   C C   1 
ATOM   6706  O  O   . TRP   C 1 170 ? 62.494 98.927  52.301 1   46.17  ? 192 TRP   C O   1 
ATOM   6707  C  CB  . TRP   C 1 170 ? 63.364 95.781  51.367 1   47.81  ? 192 TRP   C CB  1 
ATOM   6708  C  CG  . TRP   C 1 170 ? 62.566 96.265  50.184 1   48     ? 192 TRP   C CG  1 
ATOM   6709  C  CD1 . TRP   C 1 170 ? 63.022 96.992  49.125 1   48.63  ? 192 TRP   C CD1 1 
ATOM   6710  C  CD2 . TRP   C 1 170 ? 61.18  95.989  49.915 1   47.96  ? 192 TRP   C CD2 1 
ATOM   6711  N  NE1 . TRP   C 1 170 ? 61.995 97.227  48.234 1   48.89  ? 192 TRP   C NE1 1 
ATOM   6712  C  CE2 . TRP   C 1 170 ? 60.854 96.623  48.698 1   48.74  ? 192 TRP   C CE2 1 
ATOM   6713  C  CE3 . TRP   C 1 170 ? 60.181 95.285  50.597 1   48.2   ? 192 TRP   C CE3 1 
ATOM   6714  C  CZ2 . TRP   C 1 170 ? 59.573 96.575  48.155 1   49.6   ? 192 TRP   C CZ2 1 
ATOM   6715  C  CZ3 . TRP   C 1 170 ? 58.914 95.241  50.058 1   49.11  ? 192 TRP   C CZ3 1 
ATOM   6716  C  CH2 . TRP   C 1 170 ? 58.617 95.881  48.855 1   49.5   ? 192 TRP   C CH2 1 
ATOM   6717  N  N   . LEU   C 1 171 ? 61.627 97.275  53.573 1   46.45  ? 193 LEU   C N   1 
ATOM   6718  C  CA  . LEU   C 1 171 ? 60.44  97.979  54.038 1   46.78  ? 193 LEU   C CA  1 
ATOM   6719  C  C   . LEU   C 1 171 ? 60.809 99.188  54.885 1   48.42  ? 193 LEU   C C   1 
ATOM   6720  O  O   . LEU   C 1 171 ? 60.16  100.225 54.776 1   49.03  ? 193 LEU   C O   1 
ATOM   6721  C  CB  . LEU   C 1 171 ? 59.564 97.033  54.862 1   46.17  ? 193 LEU   C CB  1 
ATOM   6722  C  CG  . LEU   C 1 171 ? 58.707 96.078  54.067 1   46.52  ? 193 LEU   C CG  1 
ATOM   6723  C  CD1 . LEU   C 1 171 ? 58.113 95.029  54.963 1   46.57  ? 193 LEU   C CD1 1 
ATOM   6724  C  CD2 . LEU   C 1 171 ? 57.618 96.826  53.315 1   46.87  ? 193 LEU   C CD2 1 
ATOM   6725  N  N   . GLU   C 1 172 ? 61.852 99.059  55.727 1   48.91  ? 194 GLU   C N   1 
ATOM   6726  C  CA  . GLU   C 1 172 ? 62.361 100.13  56.589 1   49.58  ? 194 GLU   C CA  1 
ATOM   6727  C  C   . GLU   C 1 172 ? 62.884 101.318 55.755 1   51.04  ? 194 GLU   C C   1 
ATOM   6728  O  O   . GLU   C 1 172 ? 62.765 102.468 56.177 1   51.18  ? 194 GLU   C O   1 
ATOM   6729  C  CB  . GLU   C 1 172 ? 63.479 99.596  57.499 1   50.31  ? 194 GLU   C CB  1 
ATOM   6730  C  CG  . GLU   C 1 172 ? 62.981 98.748  58.656 1   55.02  ? 194 GLU   C CG  1 
ATOM   6731  C  CD  . GLU   C 1 172 ? 64.016 97.851  59.316 1   61.15  ? 194 GLU   C CD  1 
ATOM   6732  O  OE1 . GLU   C 1 172 ? 65.188 97.869  58.875 1   63.35  ? 194 GLU   C OE1 1 
ATOM   6733  O  OE2 . GLU   C 1 172 ? 63.657 97.124  60.271 1   61.54  ? 194 GLU   C OE2 1 
ATOM   6734  N  N   . ARG   C 1 173 ? 63.458 101.039 54.577 1   51.86  ? 195 ARG   C N   1 
ATOM   6735  C  CA  . ARG   C 1 173 ? 64.002 102.067 53.696 1   53.25  ? 195 ARG   C CA  1 
ATOM   6736  C  C   . ARG   C 1 173 ? 63.017 102.542 52.616 1   54.67  ? 195 ARG   C C   1 
ATOM   6737  O  O   . ARG   C 1 173 ? 63.442 103.131 51.618 1   54.58  ? 195 ARG   C O   1 
ATOM   6738  C  CB  . ARG   C 1 173 ? 65.302 101.574 53.052 1   54.82  ? 195 ARG   C CB  1 
ATOM   6739  C  CG  . ARG   C 1 173 ? 66.334 101.12  54.073 1   59.16  ? 195 ARG   C CG  1 
ATOM   6740  C  CD  . ARG   C 1 173 ? 67.708 100.953 53.455 1   64.14  ? 195 ARG   C CD  1 
ATOM   6741  N  NE  . ARG   C 1 173 ? 67.738 99.867  52.475 1   68.71  ? 195 ARG   C NE  1 
ATOM   6742  C  CZ  . ARG   C 1 173 ? 68.258 98.661  52.703 1   71.58  ? 195 ARG   C CZ  1 
ATOM   6743  N  NH1 . ARG   C 1 173 ? 68.814 98.378  53.879 1   69.59  ? 195 ARG   C NH1 1 
ATOM   6744  N  NH2 . ARG   C 1 173 ? 68.237 97.731  51.752 1   72.6   ? 195 ARG   C NH2 1 
ATOM   6745  N  N   . THR   C 1 174 ? 61.709 102.308 52.818 1   55.65  ? 196 THR   C N   1 
ATOM   6746  C  CA  . THR   C 1 174 ? 60.679 102.715 51.868 1   57.27  ? 196 THR   C CA  1 
ATOM   6747  C  C   . THR   C 1 174 ? 60.618 104.235 51.754 1   59.42  ? 196 THR   C C   1 
ATOM   6748  O  O   . THR   C 1 174 ? 60.482 104.931 52.765 1   60.11  ? 196 THR   C O   1 
ATOM   6749  C  CB  . THR   C 1 174 ? 59.313 102.107 52.265 1   58.14  ? 196 THR   C CB  1 
ATOM   6750  O  OG1 . THR   C 1 174 ? 59.336 100.71  52     1   59.6   ? 196 THR   C OG1 1 
ATOM   6751  C  CG2 . THR   C 1 174 ? 58.139 102.737 51.531 1   57.92  ? 196 THR   C CG2 1 
ATOM   6752  N  N   . PRO   C 1 175 ? 60.729 104.769 50.524 1   60.47  ? 197 PRO   C N   1 
ATOM   6753  C  CA  . PRO   C 1 175 ? 60.618 106.227 50.347 1   61.22  ? 197 PRO   C CA  1 
ATOM   6754  C  C   . PRO   C 1 175 ? 59.199 106.727 50.66  1   61.99  ? 197 PRO   C C   1 
ATOM   6755  O  O   . PRO   C 1 175 ? 58.194 106.195 50.176 1   62.22  ? 197 PRO   C O   1 
ATOM   6756  C  CB  . PRO   C 1 175 ? 60.995 106.432 48.874 1   61.79  ? 197 PRO   C CB  1 
ATOM   6757  C  CG  . PRO   C 1 175 ? 60.615 105.145 48.208 1   61.85  ? 197 PRO   C CG  1 
ATOM   6758  C  CD  . PRO   C 1 175 ? 60.887 104.072 49.23  1   60.17  ? 197 PRO   C CD  1 
ATOM   6759  N  N   . GLY   C 1 176 ? 59.14  107.739 51.498 1   62.15  ? 198 GLY   C N   1 
ATOM   6760  C  CA  . GLY   C 1 176 ? 57.893 108.31  51.976 1   62.82  ? 198 GLY   C CA  1 
ATOM   6761  C  C   . GLY   C 1 176 ? 57.782 108.275 53.492 1   63.42  ? 198 GLY   C C   1 
ATOM   6762  O  O   . GLY   C 1 176 ? 56.956 108.985 54.063 1   63.34  ? 198 GLY   C O   1 
ATOM   6763  N  N   . LEU   C 1 177 ? 58.626 107.46  54.157 1   63.9   ? 199 LEU   C N   1 
ATOM   6764  C  CA  . LEU   C 1 177 ? 58.67  107.314 55.605 1   65.08  ? 199 LEU   C CA  1 
ATOM   6765  C  C   . LEU   C 1 177 ? 59.497 108.411 56.279 1   66.34  ? 199 LEU   C C   1 
ATOM   6766  O  O   . LEU   C 1 177 ? 59.227 108.75  57.436 1   66.68  ? 199 LEU   C O   1 
ATOM   6767  C  CB  . LEU   C 1 177 ? 59.265 105.94  55.984 1   65.04  ? 199 LEU   C CB  1 
ATOM   6768  C  CG  . LEU   C 1 177 ? 58.402 104.698 55.808 1   65.72  ? 199 LEU   C CG  1 
ATOM   6769  C  CD1 . LEU   C 1 177 ? 59.098 103.492 56.387 1   65.81  ? 199 LEU   C CD1 1 
ATOM   6770  C  CD2 . LEU   C 1 177 ? 57.053 104.862 56.479 1   66.31  ? 199 LEU   C CD2 1 
ATOM   6771  N  N   . GLU   C 1 178 ? 60.526 108.929 55.579 1   66.89  ? 200 GLU   C N   1 
ATOM   6772  C  CA  . GLU   C 1 178 ? 61.428 109.949 56.125 1   68.06  ? 200 GLU   C CA  1 
ATOM   6773  C  C   . GLU   C 1 178 ? 60.73  111.266 56.477 1   68.55  ? 200 GLU   C C   1 
ATOM   6774  O  O   . GLU   C 1 178 ? 59.936 111.785 55.695 1   68.34  ? 200 GLU   C O   1 
ATOM   6775  C  CB  . GLU   C 1 178 ? 62.65  110.198 55.221 1   70.67  ? 200 GLU   C CB  1 
ATOM   6776  C  CG  . GLU   C 1 178 ? 62.317 110.465 53.77  1   76.32  ? 200 GLU   C CG  1 
ATOM   6777  C  CD  . GLU   C 1 178 ? 62.156 109.216 52.927 1   84.17  ? 200 GLU   C CD  1 
ATOM   6778  O  OE1 . GLU   C 1 178 ? 62.745 108.168 53.28  1   85.26  ? 200 GLU   C OE1 1 
ATOM   6779  O  OE2 . GLU   C 1 178 ? 61.419 109.286 51.917 1   86.71  ? 200 GLU   C OE2 1 
ATOM   6780  N  N   . GLU   C 1 179 ? 61.033 111.782 57.684 1   68.97  ? 201 GLU   C N   1 
ATOM   6781  C  CA  . GLU   C 1 179 ? 60.476 113.01  58.244 1   69.61  ? 201 GLU   C CA  1 
ATOM   6782  C  C   . GLU   C 1 179 ? 60.75  114.228 57.387 1   69.34  ? 201 GLU   C C   1 
ATOM   6783  O  O   . GLU   C 1 179 ? 59.881 115.091 57.258 1   69.52  ? 201 GLU   C O   1 
ATOM   6784  C  CB  . GLU   C 1 179 ? 61.006 113.238 59.661 1   72.73  ? 201 GLU   C CB  1 
ATOM   6785  C  CG  . GLU   C 1 179 ? 60.369 112.335 60.703 1   79.32  ? 201 GLU   C CG  1 
ATOM   6786  C  CD  . GLU   C 1 179 ? 60.338 112.943 62.095 1   88.03  ? 201 GLU   C CD  1 
ATOM   6787  O  OE1 . GLU   C 1 179 ? 61.244 112.633 62.904 1   89.95  ? 201 GLU   C OE1 1 
ATOM   6788  O  OE2 . GLU   C 1 179 ? 59.412 113.741 62.37  1   90.16  ? 201 GLU   C OE2 1 
ATOM   6789  N  N   . SER   C 1 180 ? 61.957 114.301 56.804 1   68.8   ? 202 SER   C N   1 
ATOM   6790  C  CA  . SER   C 1 180 ? 62.355 115.411 55.939 1   68.54  ? 202 SER   C CA  1 
ATOM   6791  C  C   . SER   C 1 180 ? 61.563 115.415 54.622 1   67.89  ? 202 SER   C C   1 
ATOM   6792  O  O   . SER   C 1 180 ? 61.223 116.477 54.103 1   68.14  ? 202 SER   C O   1 
ATOM   6793  C  CB  . SER   C 1 180 ? 63.851 115.354 55.656 1   69.83  ? 202 SER   C CB  1 
ATOM   6794  O  OG  . SER   C 1 180 ? 64.225 114.096 55.118 1   72.35  ? 202 SER   C OG  1 
ATOM   6795  N  N   . GLY   C 1 181 ? 61.265 114.227 54.108 1   66.8   ? 203 GLY   C N   1 
ATOM   6796  C  CA  . GLY   C 1 181 ? 60.519 114.063 52.867 1   65.67  ? 203 GLY   C CA  1 
ATOM   6797  C  C   . GLY   C 1 181 ? 59.014 114.062 53.047 1   63.85  ? 203 GLY   C C   1 
ATOM   6798  O  O   . GLY   C 1 181 ? 58.438 115.034 53.551 1   63.79  ? 203 GLY   C O   1 
ATOM   6799  N  N   . PHE   C 1 182 ? 58.366 112.964 52.631 1   61.99  ? 204 PHE   C N   1 
ATOM   6800  C  CA  . PHE   C 1 182 ? 56.914 112.861 52.702 1   60.63  ? 204 PHE   C CA  1 
ATOM   6801  C  C   . PHE   C 1 182 ? 56.373 112.757 54.132 1   59.44  ? 204 PHE   C C   1 
ATOM   6802  O  O   . PHE   C 1 182 ? 55.288 113.27  54.395 1   59.41  ? 204 PHE   C O   1 
ATOM   6803  C  CB  . PHE   C 1 182 ? 56.399 111.716 51.819 1   60.16  ? 204 PHE   C CB  1 
ATOM   6804  C  CG  . PHE   C 1 182 ? 54.895 111.671 51.695 1   60.5   ? 204 PHE   C CG  1 
ATOM   6805  C  CD1 . PHE   C 1 182 ? 54.208 112.662 51.015 1   61.05  ? 204 PHE   C CD1 1 
ATOM   6806  C  CD2 . PHE   C 1 182 ? 54.167 110.648 52.274 1   61.22  ? 204 PHE   C CD2 1 
ATOM   6807  C  CE1 . PHE   C 1 182 ? 52.825 112.627 50.918 1   61.56  ? 204 PHE   C CE1 1 
ATOM   6808  C  CE2 . PHE   C 1 182 ? 52.785 110.612 52.166 1   61.77  ? 204 PHE   C CE2 1 
ATOM   6809  C  CZ  . PHE   C 1 182 ? 52.125 111.6   51.486 1   61.45  ? 204 PHE   C CZ  1 
ATOM   6810  N  N   . ASN   C 1 183 ? 57.132 112.128 55.051 1   58.21  ? 205 ASN   C N   1 
ATOM   6811  C  CA  . ASN   C 1 183 ? 56.748 111.987 56.463 1   57.46  ? 205 ASN   C CA  1 
ATOM   6812  C  C   . ASN   C 1 183 ? 55.37  111.319 56.615 1   55.77  ? 205 ASN   C C   1 
ATOM   6813  O  O   . ASN   C 1 183 ? 54.449 111.935 57.143 1   56.43  ? 205 ASN   C O   1 
ATOM   6814  C  CB  . ASN   C 1 183 ? 56.787 113.371 57.144 1   58.99  ? 205 ASN   C CB  1 
ATOM   6815  C  CG  . ASN   C 1 183 ? 56.801 113.336 58.642 1   62.41  ? 205 ASN   C CG  1 
ATOM   6816  O  OD1 . ASN   C 1 183 ? 56.889 112.267 59.265 1   63.68  ? 205 ASN   C OD1 1 
ATOM   6817  N  ND2 . ASN   C 1 183 ? 56.731 114.514 59.24  1   63.05  ? 205 ASN   C ND2 1 
ATOM   6818  N  N   . PHE   C 1 184 ? 55.22  110.08  56.136 1   53.54  ? 206 PHE   C N   1 
ATOM   6819  C  CA  . PHE   C 1 184 ? 53.93  109.401 56.16  1   52.25  ? 206 PHE   C CA  1 
ATOM   6820  C  C   . PHE   C 1 184 ? 53.39  109.131 57.558 1   52.12  ? 206 PHE   C C   1 
ATOM   6821  O  O   . PHE   C 1 184 ? 52.223 109.424 57.802 1   51.98  ? 206 PHE   C O   1 
ATOM   6822  C  CB  . PHE   C 1 184 ? 53.955 108.108 55.321 1   51.3   ? 206 PHE   C CB  1 
ATOM   6823  C  CG  . PHE   C 1 184 ? 52.764 107.187 55.484 1   50.94  ? 206 PHE   C CG  1 
ATOM   6824  C  CD1 . PHE   C 1 184 ? 51.561 107.472 54.873 1   51.21  ? 206 PHE   C CD1 1 
ATOM   6825  C  CD2 . PHE   C 1 184 ? 52.855 106.037 56.252 1   51.41  ? 206 PHE   C CD2 1 
ATOM   6826  C  CE1 . PHE   C 1 184 ? 50.47  106.622 55.02  1   51.69  ? 206 PHE   C CE1 1 
ATOM   6827  C  CE2 . PHE   C 1 184 ? 51.756 105.205 56.42  1   51.78  ? 206 PHE   C CE2 1 
ATOM   6828  C  CZ  . PHE   C 1 184 ? 50.574 105.497 55.795 1   51.46  ? 206 PHE   C CZ  1 
ATOM   6829  N  N   . TRP   C 1 185 ? 54.194 108.544 58.453 1   52.17  ? 207 TRP   C N   1 
ATOM   6830  C  CA  . TRP   C 1 185 ? 53.704 108.157 59.774 1   53     ? 207 TRP   C CA  1 
ATOM   6831  C  C   . TRP   C 1 185 ? 53.068 109.299 60.565 1   54.16  ? 207 TRP   C C   1 
ATOM   6832  O  O   . TRP   C 1 185 ? 52.042 109.085 61.211 1   54.17  ? 207 TRP   C O   1 
ATOM   6833  C  CB  . TRP   C 1 185 ? 54.794 107.458 60.586 1   52.74  ? 207 TRP   C CB  1 
ATOM   6834  C  CG  . TRP   C 1 185 ? 54.272 106.459 61.592 1   52.98  ? 207 TRP   C CG  1 
ATOM   6835  C  CD1 . TRP   C 1 185 ? 54.433 106.503 62.946 1   53.6   ? 207 TRP   C CD1 1 
ATOM   6836  C  CD2 . TRP   C 1 185 ? 53.56  105.24  61.313 1   52.98  ? 207 TRP   C CD2 1 
ATOM   6837  N  NE1 . TRP   C 1 185 ? 53.871 105.391 63.528 1   53.81  ? 207 TRP   C NE1 1 
ATOM   6838  C  CE2 . TRP   C 1 185 ? 53.324 104.601 62.549 1   53.72  ? 207 TRP   C CE2 1 
ATOM   6839  C  CE3 . TRP   C 1 185 ? 53.107 104.621 60.139 1   53.26  ? 207 TRP   C CE3 1 
ATOM   6840  C  CZ2 . TRP   C 1 185 ? 52.653 103.38  62.642 1   54.2   ? 207 TRP   C CZ2 1 
ATOM   6841  C  CZ3 . TRP   C 1 185 ? 52.44  103.416 60.236 1   53.89  ? 207 TRP   C CZ3 1 
ATOM   6842  C  CH2 . TRP   C 1 185 ? 52.214 102.812 61.474 1   54.16  ? 207 TRP   C CH2 1 
ATOM   6843  N  N   . ALA   C 1 186 ? 53.638 110.514 60.478 1   54.75  ? 208 ALA   C N   1 
ATOM   6844  C  CA  . ALA   C 1 186 ? 53.1   111.676 61.185 1   55.47  ? 208 ALA   C CA  1 
ATOM   6845  C  C   . ALA   C 1 186 ? 51.778 112.152 60.552 1   55.5   ? 208 ALA   C C   1 
ATOM   6846  O  O   . ALA   C 1 186 ? 50.85  112.539 61.27  1   55.76  ? 208 ALA   C O   1 
ATOM   6847  C  CB  . ALA   C 1 186 ? 54.121 112.806 61.183 1   55.9   ? 208 ALA   C CB  1 
ATOM   6848  N  N   . LYS   C 1 187 ? 51.695 112.119 59.213 1   54.65  ? 209 LYS   C N   1 
ATOM   6849  C  CA  . LYS   C 1 187 ? 50.482 112.515 58.494 1   54.2   ? 209 LYS   C CA  1 
ATOM   6850  C  C   . LYS   C 1 187 ? 49.348 111.524 58.744 1   53.63  ? 209 LYS   C C   1 
ATOM   6851  O  O   . LYS   C 1 187 ? 48.188 111.938 58.808 1   54.3   ? 209 LYS   C O   1 
ATOM   6852  C  CB  . LYS   C 1 187 ? 50.761 112.626 56.988 1   55.59  ? 209 LYS   C CB  1 
ATOM   6853  C  CG  . LYS   C 1 187 ? 51.733 113.738 56.628 1   59     ? 209 LYS   C CG  1 
ATOM   6854  C  CD  . LYS   C 1 187 ? 52.057 113.738 55.146 1   63.46  ? 209 LYS   C CD  1 
ATOM   6855  C  CE  . LYS   C 1 187 ? 52.713 115.022 54.7   1   67.49  ? 209 LYS   C CE  1 
ATOM   6856  N  NZ  . LYS   C 1 187 ? 52.956 115.045 53.228 1   69.81  ? 209 LYS   C NZ  1 
ATOM   6857  N  N   . PHE   C 1 188 ? 49.689 110.221 58.882 1   52.29  ? 210 PHE   C N   1 
ATOM   6858  C  CA  . PHE   C 1 188 ? 48.776 109.113 59.141 1   51.74  ? 210 PHE   C CA  1 
ATOM   6859  C  C   . PHE   C 1 188 ? 48.183 109.246 60.536 1   52.32  ? 210 PHE   C C   1 
ATOM   6860  O  O   . PHE   C 1 188 ? 46.965 109.155 60.68  1   52.47  ? 210 PHE   C O   1 
ATOM   6861  C  CB  . PHE   C 1 188 ? 49.52  107.774 58.956 1   50.98  ? 210 PHE   C CB  1 
ATOM   6862  C  CG  . PHE   C 1 188 ? 48.784 106.48  59.261 1   50.4   ? 210 PHE   C CG  1 
ATOM   6863  C  CD1 . PHE   C 1 188 ? 47.419 106.367 59.047 1   50.52  ? 210 PHE   C CD1 1 
ATOM   6864  C  CD2 . PHE   C 1 188 ? 49.473 105.358 59.68  1   50.26  ? 210 PHE   C CD2 1 
ATOM   6865  C  CE1 . PHE   C 1 188 ? 46.75  105.184 59.335 1   50.73  ? 210 PHE   C CE1 1 
ATOM   6866  C  CE2 . PHE   C 1 188 ? 48.804 104.174 59.956 1   50.49  ? 210 PHE   C CE2 1 
ATOM   6867  C  CZ  . PHE   C 1 188 ? 47.447 104.094 59.783 1   50.28  ? 210 PHE   C CZ  1 
ATOM   6868  N  N   . GLN   C 1 189 ? 49.021 109.524 61.554 1   52.69  ? 211 GLN   C N   1 
ATOM   6869  C  CA  . GLN   C 1 189 ? 48.544 109.726 62.926 1   53.44  ? 211 GLN   C CA  1 
ATOM   6870  C  C   . GLN   C 1 189 ? 47.554 110.888 63.01  1   53.89  ? 211 GLN   C C   1 
ATOM   6871  O  O   . GLN   C 1 189 ? 46.544 110.774 63.695 1   53.89  ? 211 GLN   C O   1 
ATOM   6872  C  CB  . GLN   C 1 189 ? 49.705 109.985 63.886 1   55.28  ? 211 GLN   C CB  1 
ATOM   6873  C  CG  . GLN   C 1 189 ? 50.615 108.797 64.084 1   59.19  ? 211 GLN   C CG  1 
ATOM   6874  C  CD  . GLN   C 1 189 ? 51.207 108.793 65.471 1   64.63  ? 211 GLN   C CD  1 
ATOM   6875  O  OE1 . GLN   C 1 189 ? 50.507 109.01  66.475 1   66.09  ? 211 GLN   C OE1 1 
ATOM   6876  N  NE2 . GLN   C 1 189 ? 52.509 108.539 65.561 1   65.72  ? 211 GLN   C NE2 1 
ATOM   6877  N  N   . GLU   C 1 190 ? 47.836 111.992 62.304 1   54.13  ? 212 GLU   C N   1 
ATOM   6878  C  CA  . GLU   C 1 190 ? 46.979 113.171 62.267 1   55.16  ? 212 GLU   C CA  1 
ATOM   6879  C  C   . GLU   C 1 190 ? 45.658 112.871 61.561 1   56.09  ? 212 GLU   C C   1 
ATOM   6880  O  O   . GLU   C 1 190 ? 44.605 113.33  62.005 1   56.63  ? 212 GLU   C O   1 
ATOM   6881  C  CB  . GLU   C 1 190 ? 47.69  114.302 61.535 1   57.84  ? 212 GLU   C CB  1 
ATOM   6882  C  CG  . GLU   C 1 190 ? 48.169 115.431 62.419 1   64.48  ? 212 GLU   C CG  1 
ATOM   6883  C  CD  . GLU   C 1 190 ? 48.504 116.664 61.6   1   74.96  ? 212 GLU   C CD  1 
ATOM   6884  O  OE1 . GLU   C 1 190 ? 49.009 116.506 60.46  1   76.82  ? 212 GLU   C OE1 1 
ATOM   6885  O  OE2 . GLU   C 1 190 ? 48.225 117.787 62.084 1   77.85  ? 212 GLU   C OE2 1 
ATOM   6886  N  N   . SER   C 1 191 ? 45.714 112.118 60.448 1   56.12  ? 213 SER   C N   1 
ATOM   6887  C  CA  . SER   C 1 191 ? 44.527 111.731 59.685 1   56.21  ? 213 SER   C CA  1 
ATOM   6888  C  C   . SER   C 1 191 ? 43.63  110.833 60.528 1   56.27  ? 213 SER   C C   1 
ATOM   6889  O  O   . SER   C 1 191 ? 42.417 110.986 60.501 1   56.62  ? 213 SER   C O   1 
ATOM   6890  C  CB  . SER   C 1 191 ? 44.931 111.003 58.411 1   57.15  ? 213 SER   C CB  1 
ATOM   6891  O  OG  . SER   C 1 191 ? 45.626 111.872 57.535 1   59.33  ? 213 SER   C OG  1 
ATOM   6892  N  N   . VAL   C 1 192 ? 44.226 109.91  61.281 1   56.1   ? 214 VAL   C N   1 
ATOM   6893  C  CA  . VAL   C 1 192 ? 43.49  109.009 62.157 1   56.58  ? 214 VAL   C CA  1 
ATOM   6894  C  C   . VAL   C 1 192 ? 42.779 109.808 63.249 1   56.69  ? 214 VAL   C C   1 
ATOM   6895  O  O   . VAL   C 1 192 ? 41.594 109.592 63.494 1   56.34  ? 214 VAL   C O   1 
ATOM   6896  C  CB  . VAL   C 1 192 ? 44.443 107.93  62.735 1   57.13  ? 214 VAL   C CB  1 
ATOM   6897  C  CG1 . VAL   C 1 192 ? 43.887 107.3   64.01  1   57.65  ? 214 VAL   C CG1 1 
ATOM   6898  C  CG2 . VAL   C 1 192 ? 44.731 106.862 61.696 1   57.43  ? 214 VAL   C CG2 1 
ATOM   6899  N  N   . ASP   C 1 193 ? 43.507 110.74  63.882 1   57.08  ? 215 ASP   C N   1 
ATOM   6900  C  CA  . ASP   C 1 193 ? 42.983 111.579 64.954 1   57.76  ? 215 ASP   C CA  1 
ATOM   6901  C  C   . ASP   C 1 193 ? 41.785 112.387 64.51  1   58.02  ? 215 ASP   C C   1 
ATOM   6902  O  O   . ASP   C 1 193 ? 40.781 112.399 65.213 1   58.24  ? 215 ASP   C O   1 
ATOM   6903  C  CB  . ASP   C 1 193 ? 44.076 112.481 65.541 1   59.69  ? 215 ASP   C CB  1 
ATOM   6904  C  CG  . ASP   C 1 193 ? 45.041 111.77  66.485 1   65.45  ? 215 ASP   C CG  1 
ATOM   6905  O  OD1 . ASP   C 1 193 ? 44.796 110.573 66.809 1   66.04  ? 215 ASP   C OD1 1 
ATOM   6906  O  OD2 . ASP   C 1 193 ? 46.046 112.408 66.904 1   67.82  ? 215 ASP   C OD2 1 
ATOM   6907  N  N   . ARG   C 1 194 ? 41.859 113.011 63.332 1   57.83  ? 216 ARG   C N   1 
ATOM   6908  C  CA  . ARG   C 1 194 ? 40.749 113.79  62.813 1   58.24  ? 216 ARG   C CA  1 
ATOM   6909  C  C   . ARG   C 1 194 ? 39.595 112.906 62.338 1   57.64  ? 216 ARG   C C   1 
ATOM   6910  O  O   . ARG   C 1 194 ? 38.434 113.295 62.458 1   58.06  ? 216 ARG   C O   1 
ATOM   6911  C  CB  . ARG   C 1 194 ? 41.212 114.678 61.673 1   60.84  ? 216 ARG   C CB  1 
ATOM   6912  C  CG  . ARG   C 1 194 ? 42.096 115.814 62.121 1   66.57  ? 216 ARG   C CG  1 
ATOM   6913  C  CD  . ARG   C 1 194 ? 42.379 116.728 60.945 1   72.42  ? 216 ARG   C CD  1 
ATOM   6914  N  NE  . ARG   C 1 194 ? 43.197 116.073 59.917 1   77.52  ? 216 ARG   C NE  1 
ATOM   6915  C  CZ  . ARG   C 1 194 ? 44.525 116.141 59.867 1   80.99  ? 216 ARG   C CZ  1 
ATOM   6916  N  NH1 . ARG   C 1 194 ? 45.197 116.821 60.791 1   80.72  ? 216 ARG   C NH1 1 
ATOM   6917  N  NH2 . ARG   C 1 194 ? 45.191 115.524 58.898 1   81.27  ? 216 ARG   C NH2 1 
ATOM   6918  N  N   . PHE   C 1 195 ? 39.904 111.735 61.789 1   56.4   ? 217 PHE   C N   1 
ATOM   6919  C  CA  . PHE   C 1 195 ? 38.883 110.811 61.321 1   55.59  ? 217 PHE   C CA  1 
ATOM   6920  C  C   . PHE   C 1 195 ? 38.075 110.282 62.501 1   55.39  ? 217 PHE   C C   1 
ATOM   6921  O  O   . PHE   C 1 195 ? 36.843 110.279 62.455 1   55.42  ? 217 PHE   C O   1 
ATOM   6922  C  CB  . PHE   C 1 195 ? 39.516 109.651 60.523 1   54.93  ? 217 PHE   C CB  1 
ATOM   6923  C  CG  . PHE   C 1 195 ? 38.524 108.61  60.068 1   54.97  ? 217 PHE   C CG  1 
ATOM   6924  C  CD1 . PHE   C 1 195 ? 37.623 108.885 59.055 1   55.38  ? 217 PHE   C CD1 1 
ATOM   6925  C  CD2 . PHE   C 1 195 ? 38.481 107.363 60.665 1   55.34  ? 217 PHE   C CD2 1 
ATOM   6926  C  CE1 . PHE   C 1 195 ? 36.694 107.938 58.658 1   55.8   ? 217 PHE   C CE1 1 
ATOM   6927  C  CE2 . PHE   C 1 195 ? 37.56  106.415 60.255 1   55.78  ? 217 PHE   C CE2 1 
ATOM   6928  C  CZ  . PHE   C 1 195 ? 36.674 106.71  59.253 1   55.53  ? 217 PHE   C CZ  1 
ATOM   6929  N  N   . LEU   C 1 196 ? 38.763 109.853 63.568 1   54.9   ? 218 LEU   C N   1 
ATOM   6930  C  CA  . LEU   C 1 196 ? 38.086 109.343 64.754 1   54.76  ? 218 LEU   C CA  1 
ATOM   6931  C  C   . LEU   C 1 196 ? 37.309 110.42  65.489 1   54.25  ? 218 LEU   C C   1 
ATOM   6932  O  O   . LEU   C 1 196 ? 36.226 110.126 65.974 1   54.31  ? 218 LEU   C O   1 
ATOM   6933  C  CB  . LEU   C 1 196 ? 39.037 108.591 65.685 1   54.94  ? 218 LEU   C CB  1 
ATOM   6934  C  CG  . LEU   C 1 196 ? 39.651 107.327 65.092 1   56.23  ? 218 LEU   C CG  1 
ATOM   6935  C  CD1 . LEU   C 1 196 ? 40.612 106.704 66.07  1   57.06  ? 218 LEU   C CD1 1 
ATOM   6936  C  CD2 . LEU   C 1 196 ? 38.578 106.322 64.641 1   56.39  ? 218 LEU   C CD2 1 
ATOM   6937  N  N   . GLU   C 1 197 ? 37.786 111.676 65.475 1   53.94  ? 219 GLU   C N   1 
ATOM   6938  C  CA  . GLU   C 1 197 ? 37.055 112.806 66.066 1   54.17  ? 219 GLU   C CA  1 
ATOM   6939  C  C   . GLU   C 1 197 ? 35.755 113.045 65.293 1   53.77  ? 219 GLU   C C   1 
ATOM   6940  O  O   . GLU   C 1 197 ? 34.694 113.188 65.895 1   53.59  ? 219 GLU   C O   1 
ATOM   6941  C  CB  . GLU   C 1 197 ? 37.905 114.089 66.075 1   56.83  ? 219 GLU   C CB  1 
ATOM   6942  C  CG  . GLU   C 1 197 ? 38.86  114.184 67.249 1   63.73  ? 219 GLU   C CG  1 
ATOM   6943  C  CD  . GLU   C 1 197 ? 40.088 115.054 67.037 1   73.47  ? 219 GLU   C CD  1 
ATOM   6944  O  OE1 . GLU   C 1 197 ? 40.062 115.924 66.133 1   75.76  ? 219 GLU   C OE1 1 
ATOM   6945  O  OE2 . GLU   C 1 197 ? 41.082 114.856 67.776 1   76.04  ? 219 GLU   C OE2 1 
ATOM   6946  N  N   . ALA   C 1 198 ? 35.832 113.024 63.957 1   53.61  ? 220 ALA   C N   1 
ATOM   6947  C  CA  . ALA   C 1 198 ? 34.659 113.195 63.102 1   53.91  ? 220 ALA   C CA  1 
ATOM   6948  C  C   . ALA   C 1 198 ? 33.644 112.08  63.312 1   54.46  ? 220 ALA   C C   1 
ATOM   6949  O  O   . ALA   C 1 198 ? 32.443 112.321 63.207 1   54.28  ? 220 ALA   C O   1 
ATOM   6950  C  CB  . ALA   C 1 198 ? 35.079 113.241 61.648 1   53.76  ? 220 ALA   C CB  1 
ATOM   6951  N  N   . GLN   C 1 199 ? 34.132 110.86  63.599 1   54.98  ? 221 GLN   C N   1 
ATOM   6952  C  CA  . GLN   C 1 199 ? 33.306 109.688 63.862 1   55.96  ? 221 GLN   C CA  1 
ATOM   6953  C  C   . GLN   C 1 199 ? 32.579 109.826 65.197 1   56.56  ? 221 GLN   C C   1 
ATOM   6954  O  O   . GLN   C 1 199 ? 31.449 109.36  65.324 1   56.19  ? 221 GLN   C O   1 
ATOM   6955  C  CB  . GLN   C 1 199 ? 34.16  108.404 63.853 1   57.4   ? 221 GLN   C CB  1 
ATOM   6956  C  CG  . GLN   C 1 199 ? 34.52  107.9   62.456 1   59.59  ? 221 GLN   C CG  1 
ATOM   6957  C  CD  . GLN   C 1 199 ? 33.301 107.586 61.626 1   62.72  ? 221 GLN   C CD  1 
ATOM   6958  O  OE1 . GLN   C 1 199 ? 33.149 108.084 60.508 1   63.96  ? 221 GLN   C OE1 1 
ATOM   6959  N  NE2 . GLN   C 1 199 ? 32.402 106.759 62.156 1   62.89  ? 221 GLN   C NE2 1 
ATOM   6960  N  N   . VAL   C 1 200 ? 33.233 110.439 66.198 1   57.31  ? 222 VAL   C N   1 
ATOM   6961  C  CA  . VAL   C 1 200 ? 32.64  110.661 67.517 1   58.52  ? 222 VAL   C CA  1 
ATOM   6962  C  C   . VAL   C 1 200 ? 31.512 111.68  67.413 1   59.36  ? 222 VAL   C C   1 
ATOM   6963  O  O   . VAL   C 1 200 ? 30.432 111.446 67.947 1   59.07  ? 222 VAL   C O   1 
ATOM   6964  C  CB  . VAL   C 1 200 ? 33.701 111.059 68.581 1   59.39  ? 222 VAL   C CB  1 
ATOM   6965  C  CG1 . VAL   C 1 200 ? 33.036 111.498 69.881 1   60.07  ? 222 VAL   C CG1 1 
ATOM   6966  C  CG2 . VAL   C 1 200 ? 34.652 109.899 68.848 1   60.03  ? 222 VAL   C CG2 1 
ATOM   6967  N  N   . GLN   C 1 201 ? 31.736 112.768 66.659 1   60.27  ? 223 GLN   C N   1 
ATOM   6968  C  CA  . GLN   C 1 201 ? 30.722 113.8   66.455 1   61.66  ? 223 GLN   C CA  1 
ATOM   6969  C  C   . GLN   C 1 201 ? 29.527 113.267 65.692 1   62.66  ? 223 GLN   C C   1 
ATOM   6970  O  O   . GLN   C 1 201 ? 28.396 113.61  66.019 1   62.88  ? 223 GLN   C O   1 
ATOM   6971  C  CB  . GLN   C 1 201 ? 31.319 115.03  65.755 1   63.86  ? 223 GLN   C CB  1 
ATOM   6972  C  CG  . GLN   C 1 201 ? 32.438 115.708 66.562 1   68.71  ? 223 GLN   C CG  1 
ATOM   6973  C  CD  . GLN   C 1 201 ? 32.068 116.046 68.006 1   73.24  ? 223 GLN   C CD  1 
ATOM   6974  O  OE1 . GLN   C 1 201 ? 31.033 116.671 68.3   1   74.35  ? 223 GLN   C OE1 1 
ATOM   6975  N  NE2 . GLN   C 1 201 ? 32.917 115.635 68.939 1   73.55  ? 223 GLN   C NE2 1 
ATOM   6976  N  N   . SER   C 1 202 ? 29.774 112.388 64.711 1   63.22  ? 224 SER   C N   1 
ATOM   6977  C  CA  . SER   C 1 202 ? 28.74  111.748 63.911 1   64.15  ? 224 SER   C CA  1 
ATOM   6978  C  C   . SER   C 1 202 ? 27.934 110.758 64.769 1   65.59  ? 224 SER   C C   1 
ATOM   6979  O  O   . SER   C 1 202 ? 26.707 110.682 64.648 1   65.79  ? 224 SER   C O   1 
ATOM   6980  C  CB  . SER   C 1 202 ? 29.374 111.036 62.724 1   64.9   ? 224 SER   C CB  1 
ATOM   6981  O  OG  . SER   C 1 202 ? 28.395 110.385 61.935 1   66.99  ? 224 SER   C OG  1 
ATOM   6982  N  N   . ALA   C 1 203 ? 28.624 110.012 65.644 1   66.53  ? 225 ALA   C N   1 
ATOM   6983  C  CA  . ALA   C 1 203 ? 27.981 109.064 66.556 1   68.09  ? 225 ALA   C CA  1 
ATOM   6984  C  C   . ALA   C 1 203 ? 27.165 109.787 67.616 1   69.75  ? 225 ALA   C C   1 
ATOM   6985  O  O   . ALA   C 1 203 ? 26.174 109.233 68.082 1   70.16  ? 225 ALA   C O   1 
ATOM   6986  C  CB  . ALA   C 1 203 ? 29.019 108.181 67.226 1   68.3   ? 225 ALA   C CB  1 
ATOM   6987  N  N   . MET   C 1 204 ? 27.582 111.009 68.01  1   70.52  ? 226 MET   C N   1 
ATOM   6988  C  CA  . MET   C 1 204 ? 26.861 111.814 68.991 1   71.85  ? 226 MET   C CA  1 
ATOM   6989  C  C   . MET   C 1 204 ? 25.508 112.262 68.46  1   72.73  ? 226 MET   C C   1 
ATOM   6990  O  O   . MET   C 1 204 ? 24.562 112.369 69.237 1   73.23  ? 226 MET   C O   1 
ATOM   6991  C  CB  . MET   C 1 204 ? 27.689 113.031 69.452 1   73.01  ? 226 MET   C CB  1 
ATOM   6992  C  CG  . MET   C 1 204 ? 28.861 112.681 70.352 1   76.11  ? 226 MET   C CG  1 
ATOM   6993  S  SD  . MET   C 1 204 ? 28.401 111.69  71.783 1   85.98  ? 226 MET   C SD  1 
ATOM   6994  C  CE  . MET   C 1 204 ? 30.003 111.175 72.363 1   86.19  ? 226 MET   C CE  1 
ATOM   6995  N  N   . GLU   C 1 205 ? 25.401 112.502 67.143 1   72.88  ? 227 GLU   C N   1 
ATOM   6996  C  CA  . GLU   C 1 205 ? 24.146 112.911 66.512 1   73.52  ? 227 GLU   C CA  1 
ATOM   6997  C  C   . GLU   C 1 205 ? 23.203 111.751 66.183 1   73.61  ? 227 GLU   C C   1 
ATOM   6998  O  O   . GLU   C 1 205 ? 22.165 111.989 65.571 1   73.59  ? 227 GLU   C O   1 
ATOM   6999  C  CB  . GLU   C 1 205 ? 24.42  113.731 65.246 1   76.01  ? 227 GLU   C CB  1 
ATOM   7000  C  CG  . GLU   C 1 205 ? 25.215 114.989 65.52  1   81.38  ? 227 GLU   C CG  1 
ATOM   7001  C  CD  . GLU   C 1 205 ? 25.871 115.602 64.3   1   89.23  ? 227 GLU   C CD  1 
ATOM   7002  O  OE1 . GLU   C 1 205 ? 25.903 114.942 63.235 1   90.18  ? 227 GLU   C OE1 1 
ATOM   7003  O  OE2 . GLU   C 1 205 ? 26.372 116.743 64.418 1   92.44  ? 227 GLU   C OE2 1 
ATOM   7004  N  N   . GLU   C 1 206 ? 23.547 110.513 66.571 1   73.66  ? 228 GLU   C N   1 
ATOM   7005  C  CA  . GLU   C 1 206 ? 22.703 109.354 66.3   1   74.31  ? 228 GLU   C CA  1 
ATOM   7006  C  C   . GLU   C 1 206 ? 21.387 109.435 67.086 1   74.35  ? 228 GLU   C C   1 
ATOM   7007  O  O   . GLU   C 1 206 ? 21.389 109.605 68.309 1   74.27  ? 228 GLU   C O   1 
ATOM   7008  C  CB  . GLU   C 1 206 ? 23.447 108.047 66.622 1   77.01  ? 228 GLU   C CB  1 
ATOM   7009  C  CG  . GLU   C 1 206 ? 23.043 106.888 65.728 1   82.13  ? 228 GLU   C CG  1 
ATOM   7010  C  CD  . GLU   C 1 206 ? 23.682 106.92  64.353 1   89.23  ? 228 GLU   C CD  1 
ATOM   7011  O  OE1 . GLU   C 1 206 ? 24.762 107.537 64.208 1   90.62  ? 228 GLU   C OE1 1 
ATOM   7012  O  OE2 . GLU   C 1 206 ? 23.108 106.316 63.42  1   91.91  ? 228 GLU   C OE2 1 
ATOM   7013  N  N   . PRO   C 1 207 ? 20.247 109.347 66.382 1   74.17  ? 229 PRO   C N   1 
ATOM   7014  C  CA  . PRO   C 1 207 ? 18.956 109.439 67.079 1   74.16  ? 229 PRO   C CA  1 
ATOM   7015  C  C   . PRO   C 1 207 ? 18.657 108.234 67.965 1   74.5   ? 229 PRO   C C   1 
ATOM   7016  O  O   . PRO   C 1 207 ? 18.233 108.415 69.104 1   74.66  ? 229 PRO   C O   1 
ATOM   7017  C  CB  . PRO   C 1 207 ? 17.94  109.611 65.946 1   74.77  ? 229 PRO   C CB  1 
ATOM   7018  C  CG  . PRO   C 1 207 ? 18.597 109.036 64.745 1   75.29  ? 229 PRO   C CG  1 
ATOM   7019  C  CD  . PRO   C 1 207 ? 20.084 109.165 64.926 1   73.75  ? 229 PRO   C CD  1 
ATOM   7020  N  N   . VAL   C 1 208 ? 18.898 107.009 67.465 1   74.41  ? 230 VAL   C N   1 
ATOM   7021  C  CA  . VAL   C 1 208 ? 18.648 105.796 68.241 1   74.75  ? 230 VAL   C CA  1 
ATOM   7022  C  C   . VAL   C 1 208 ? 19.754 105.631 69.262 1   74.67  ? 230 VAL   C C   1 
ATOM   7023  O  O   . VAL   C 1 208 ? 20.926 105.737 68.91  1   74.81  ? 230 VAL   C O   1 
ATOM   7024  C  CB  . VAL   C 1 208 ? 18.513 104.553 67.337 1   75.73  ? 230 VAL   C CB  1 
ATOM   7025  C  CG1 . VAL   C 1 208 ? 18.119 103.323 68.152 1   76.18  ? 230 VAL   C CG1 1 
ATOM   7026  C  CG2 . VAL   C 1 208 ? 17.504 104.807 66.221 1   76.41  ? 230 VAL   C CG2 1 
ATOM   7027  N  N   . GLU   C 1 209 ? 19.392 105.428 70.532 1   74.32  ? 231 GLU   C N   1 
ATOM   7028  C  CA  . GLU   C 1 209 ? 20.381 105.312 71.594 1   74.35  ? 231 GLU   C CA  1 
ATOM   7029  C  C   . GLU   C 1 209 ? 21.25  104.053 71.462 1   73.87  ? 231 GLU   C C   1 
ATOM   7030  O  O   . GLU   C 1 209 ? 22.454 104.114 71.719 1   73.65  ? 231 GLU   C O   1 
ATOM   7031  C  CB  . GLU   C 1 209 ? 19.713 105.418 72.98  1   76.32  ? 231 GLU   C CB  1 
ATOM   7032  C  CG  . GLU   C 1 209 ? 20.685 105.528 74.149 1   80.7   ? 231 GLU   C CG  1 
ATOM   7033  C  CD  . GLU   C 1 209 ? 21.461 106.829 74.281 1   86.2   ? 231 GLU   C CD  1 
ATOM   7034  O  OE1 . GLU   C 1 209 ? 21.095 107.818 73.602 1   87.01  ? 231 GLU   C OE1 1 
ATOM   7035  O  OE2 . GLU   C 1 209 ? 22.432 106.861 75.075 1   87.64  ? 231 GLU   C OE2 1 
ATOM   7036  N  N   . LYS   C 1 210 ? 20.656 102.933 71.019 1   73.23  ? 232 LYS   C N   1 
ATOM   7037  C  CA  . LYS   C 1 210 ? 21.388 101.672 70.859 1   72.79  ? 232 LYS   C CA  1 
ATOM   7038  C  C   . LYS   C 1 210 ? 22.49  101.772 69.799 1   71.65  ? 232 LYS   C C   1 
ATOM   7039  O  O   . LYS   C 1 210 ? 23.601 101.283 70.018 1   71.87  ? 232 LYS   C O   1 
ATOM   7040  C  CB  . LYS   C 1 210 ? 20.412 100.539 70.538 1   74.95  ? 232 LYS   C CB  1 
ATOM   7041  C  CG  . LYS   C 1 210 ? 21.051 99.173  70.357 1   79.82  ? 232 LYS   C CG  1 
ATOM   7042  C  CD  . LYS   C 1 210 ? 20.003 98.088  70.059 1   85.1   ? 232 LYS   C CD  1 
ATOM   7043  C  CE  . LYS   C 1 210 ? 19.157 98.379  68.832 1   89.48  ? 232 LYS   C CE  1 
ATOM   7044  N  NZ  . LYS   C 1 210 ? 19.986 98.716  67.637 1   92.11  ? 232 LYS   C NZ  1 
ATOM   7045  N  N   . ALA   C 1 211 ? 22.19  102.446 68.674 1   70.15  ? 233 ALA   C N   1 
ATOM   7046  C  CA  . ALA   C 1 211 ? 23.13  102.657 67.575 1   69.06  ? 233 ALA   C CA  1 
ATOM   7047  C  C   . ALA   C 1 211 ? 24.271 103.593 67.99  1   67.78  ? 233 ALA   C C   1 
ATOM   7048  O  O   . ALA   C 1 211 ? 25.422 103.376 67.619 1   67.83  ? 233 ALA   C O   1 
ATOM   7049  C  CB  . ALA   C 1 211 ? 22.394 103.235 66.376 1   69.12  ? 233 ALA   C CB  1 
ATOM   7050  N  N   . LYS   C 1 212 ? 23.941 104.623 68.771 1   66.59  ? 234 LYS   C N   1 
ATOM   7051  C  CA  . LYS   C 1 212 ? 24.876 105.623 69.277 1   65.83  ? 234 LYS   C CA  1 
ATOM   7052  C  C   . LYS   C 1 212 ? 25.957 104.969 70.152 1   64.39  ? 234 LYS   C C   1 
ATOM   7053  O  O   . LYS   C 1 212 ? 27.146 105.226 69.975 1   64.35  ? 234 LYS   C O   1 
ATOM   7054  C  CB  . LYS   C 1 212 ? 24.082 106.677 70.073 1   67.49  ? 234 LYS   C CB  1 
ATOM   7055  C  CG  . LYS   C 1 212 ? 24.894 107.776 70.737 1   70.31  ? 234 LYS   C CG  1 
ATOM   7056  C  CD  . LYS   C 1 212 ? 23.93  108.735 71.405 1   73.54  ? 234 LYS   C CD  1 
ATOM   7057  C  CE  . LYS   C 1 212 ? 24.522 110.065 71.748 1   76.77  ? 234 LYS   C CE  1 
ATOM   7058  N  NZ  . LYS   C 1 212 ? 23.467 111.113 71.748 1   78.88  ? 234 LYS   C NZ  1 
ATOM   7059  N  N   . ASN   C 1 213 ? 25.537 104.099 71.069 1   63.05  ? 235 ASN   C N   1 
ATOM   7060  C  CA  . ASN   C 1 213 ? 26.443 103.407 71.974 1   62.02  ? 235 ASN   C CA  1 
ATOM   7061  C  C   . ASN   C 1 213 ? 27.297 102.395 71.235 1   60.67  ? 235 ASN   C C   1 
ATOM   7062  O  O   . ASN   C 1 213 ? 28.465 102.223 71.582 1   60.37  ? 235 ASN   C O   1 
ATOM   7063  C  CB  . ASN   C 1 213 ? 25.661 102.722 73.084 1   62.69  ? 235 ASN   C CB  1 
ATOM   7064  C  CG  . ASN   C 1 213 ? 24.774 103.665 73.853 1   64.56  ? 235 ASN   C CG  1 
ATOM   7065  O  OD1 . ASN   C 1 213 ? 25.018 104.874 73.935 1   64.96  ? 235 ASN   C OD1 1 
ATOM   7066  N  ND2 . ASN   C 1 213 ? 23.708 103.122 74.421 1   65.36  ? 235 ASN   C ND2 1 
ATOM   7067  N  N   . TYR   C 1 214 ? 26.725 101.73  70.201 1   59.41  ? 236 TYR   C N   1 
ATOM   7068  C  CA  . TYR   C 1 214 ? 27.464 100.764 69.389 1   58.08  ? 236 TYR   C CA  1 
ATOM   7069  C  C   . TYR   C 1 214 ? 28.618 101.463 68.691 1   55.18  ? 236 TYR   C C   1 
ATOM   7070  O  O   . TYR   C 1 214 ? 29.742 100.97  68.742 1   55.3   ? 236 TYR   C O   1 
ATOM   7071  C  CB  . TYR   C 1 214 ? 26.565 100.07  68.352 1   59.13  ? 236 TYR   C CB  1 
ATOM   7072  C  CG  . TYR   C 1 214 ? 27.316 99.009  67.573 1   61.52  ? 236 TYR   C CG  1 
ATOM   7073  C  CD1 . TYR   C 1 214 ? 27.571 97.764  68.128 1   63.11  ? 236 TYR   C CD1 1 
ATOM   7074  C  CD2 . TYR   C 1 214 ? 27.815 99.269  66.299 1   63.22  ? 236 TYR   C CD2 1 
ATOM   7075  C  CE1 . TYR   C 1 214 ? 28.283 96.793  67.432 1   64.49  ? 236 TYR   C CE1 1 
ATOM   7076  C  CE2 . TYR   C 1 214 ? 28.545 98.312  65.6   1   64.42  ? 236 TYR   C CE2 1 
ATOM   7077  C  CZ  . TYR   C 1 214 ? 28.787 97.077  66.177 1   65.7   ? 236 TYR   C CZ  1 
ATOM   7078  O  OH  . TYR   C 1 214 ? 29.488 96.101  65.506 1   67.56  ? 236 TYR   C OH  1 
ATOM   7079  N  N   . ARG   C 1 215 ? 28.346 102.633 68.082 1   52.57  ? 237 ARG   C N   1 
ATOM   7080  C  CA  . ARG   C 1 215 ? 29.361 103.426 67.393 1   50.66  ? 237 ARG   C CA  1 
ATOM   7081  C  C   . ARG   C 1 215 ? 30.453 103.916 68.336 1   49.95  ? 237 ARG   C C   1 
ATOM   7082  O  O   . ARG   C 1 215 ? 31.625 103.807 68.005 1   49.45  ? 237 ARG   C O   1 
ATOM   7083  C  CB  . ARG   C 1 215 ? 28.724 104.602 66.665 1   50.11  ? 237 ARG   C CB  1 
ATOM   7084  C  CG  . ARG   C 1 215 ? 27.842 104.167 65.51  1   50.23  ? 237 ARG   C CG  1 
ATOM   7085  C  CD  . ARG   C 1 215 ? 27.423 105.341 64.657 1   50.25  ? 237 ARG   C CD  1 
ATOM   7086  N  NE  . ARG   C 1 215 ? 28.573 105.965 64.001 1   49.72  ? 237 ARG   C NE  1 
ATOM   7087  C  CZ  . ARG   C 1 215 ? 28.503 107.029 63.208 1   48.49  ? 237 ARG   C CZ  1 
ATOM   7088  N  NH1 . ARG   C 1 215 ? 27.33  107.595 62.948 1   46.69  ? 237 ARG   C NH1 1 
ATOM   7089  N  NH2 . ARG   C 1 215 ? 29.604 107.531 62.666 1   47.25  ? 237 ARG   C NH2 1 
ATOM   7090  N  N   . LEU   C 1 216 ? 30.079 104.404 69.532 1   49.42  ? 238 LEU   C N   1 
ATOM   7091  C  CA  . LEU   C 1 216 ? 31.054 104.875 70.513 1   48.78  ? 238 LEU   C CA  1 
ATOM   7092  C  C   . LEU   C 1 216 ? 31.912 103.735 71.068 1   47.93  ? 238 LEU   C C   1 
ATOM   7093  O  O   . LEU   C 1 216 ? 33.097 103.941 71.325 1   47.49  ? 238 LEU   C O   1 
ATOM   7094  C  CB  . LEU   C 1 216 ? 30.362 105.655 71.636 1   48.93  ? 238 LEU   C CB  1 
ATOM   7095  C  CG  . LEU   C 1 216 ? 29.674 106.951 71.205 1   49.79  ? 238 LEU   C CG  1 
ATOM   7096  C  CD1 . LEU   C 1 216 ? 28.969 107.578 72.353 1   49.52  ? 238 LEU   C CD1 1 
ATOM   7097  C  CD2 . LEU   C 1 216 ? 30.664 107.94  70.59  1   50.85  ? 238 LEU   C CD2 1 
ATOM   7098  N  N   . MET   C 1 217 ? 31.328 102.529 71.227 1   47.67  ? 239 MET   C N   1 
ATOM   7099  C  CA  . MET   C 1 217 ? 32.082 101.343 71.669 1   48.15  ? 239 MET   C CA  1 
ATOM   7100  C  C   . MET   C 1 217 ? 33.066 100.946 70.554 1   48.56  ? 239 MET   C C   1 
ATOM   7101  O  O   . MET   C 1 217 ? 34.206 100.581 70.84  1   48.42  ? 239 MET   C O   1 
ATOM   7102  C  CB  . MET   C 1 217 ? 31.123 100.168 72.014 1   48.89  ? 239 MET   C CB  1 
ATOM   7103  C  CG  . MET   C 1 217 ? 31.759 98.757  71.975 1   51.12  ? 239 MET   C CG  1 
ATOM   7104  S  SD  . MET   C 1 217 ? 31.923 97.988  70.316 1   54.46  ? 239 MET   C SD  1 
ATOM   7105  C  CE  . MET   C 1 217 ? 30.454 97.072  70.226 1   50.12  ? 239 MET   C CE  1 
ATOM   7106  N  N   . ASP   C 1 218 ? 32.604 101.001 69.285 1   48.54  ? 240 ASP   C N   1 
ATOM   7107  C  CA  . ASP   C 1 218 ? 33.399 100.684 68.113 1   49.14  ? 240 ASP   C CA  1 
ATOM   7108  C  C   . ASP   C 1 218 ? 34.567 101.655 67.925 1   49.89  ? 240 ASP   C C   1 
ATOM   7109  O  O   . ASP   C 1 218 ? 35.68  101.2   67.686 1   50.76  ? 240 ASP   C O   1 
ATOM   7110  C  CB  . ASP   C 1 218 ? 32.51  100.613 66.873 1   50.75  ? 240 ASP   C CB  1 
ATOM   7111  C  CG  . ASP   C 1 218 ? 33.242 100.213 65.618 1   55.32  ? 240 ASP   C CG  1 
ATOM   7112  O  OD1 . ASP   C 1 218 ? 33.817 99.085  65.585 1   55.54  ? 240 ASP   C OD1 1 
ATOM   7113  O  OD2 . ASP   C 1 218 ? 33.221 100.999 64.658 1   57.88  ? 240 ASP   C OD2 1 
ATOM   7114  N  N   . ILE   C 1 219 ? 34.349 102.973 68.09  1   49.46  ? 241 ILE   C N   1 
ATOM   7115  C  CA  . ILE   C 1 219 ? 35.434 103.971 68.005 1   49.19  ? 241 ILE   C CA  1 
ATOM   7116  C  C   . ILE   C 1 219 ? 36.499 103.699 69.073 1   48.41  ? 241 ILE   C C   1 
ATOM   7117  O  O   . ILE   C 1 219 ? 37.681 103.904 68.825 1   48.87  ? 241 ILE   C O   1 
ATOM   7118  C  CB  . ILE   C 1 219 ? 34.891 105.424 68.084 1   49.62  ? 241 ILE   C CB  1 
ATOM   7119  C  CG1 . ILE   C 1 219 ? 33.945 105.715 66.911 1   50.67  ? 241 ILE   C CG1 1 
ATOM   7120  C  CG2 . ILE   C 1 219 ? 36.024 106.44  68.118 1   49.8   ? 241 ILE   C CG2 1 
ATOM   7121  C  CD1 . ILE   C 1 219 ? 33.001 106.81  67.186 1   52.19  ? 241 ILE   C CD1 1 
ATOM   7122  N  N   . GLU   C 1 220 ? 36.093 103.185 70.229 1   47.48  ? 242 GLU   C N   1 
ATOM   7123  C  CA  . GLU   C 1 220 ? 37.021 102.833 71.292 1   47.52  ? 242 GLU   C CA  1 
ATOM   7124  C  C   . GLU   C 1 220 ? 37.894 101.643 70.862 1   47.86  ? 242 GLU   C C   1 
ATOM   7125  O  O   . GLU   C 1 220 ? 39.096 101.641 71.135 1   48.35  ? 242 GLU   C O   1 
ATOM   7126  C  CB  . GLU   C 1 220 ? 36.268 102.573 72.613 1   48.51  ? 242 GLU   C CB  1 
ATOM   7127  C  CG  . GLU   C 1 220 ? 37.09  102.79  73.871 1   51.27  ? 242 GLU   C CG  1 
ATOM   7128  C  CD  . GLU   C 1 220 ? 37.931 104.05  73.947 1   56.19  ? 242 GLU   C CD  1 
ATOM   7129  O  OE1 . GLU   C 1 220 ? 37.385 105.161 73.76  1   54.76  ? 242 GLU   C OE1 1 
ATOM   7130  O  OE2 . GLU   C 1 220 ? 39.149 103.922 74.202 1   60.22  ? 242 GLU   C OE2 1 
ATOM   7131  N  N   . LYS   C 1 221 ? 37.311 100.675 70.129 1   47.35  ? 243 LYS   C N   1 
ATOM   7132  C  CA  . LYS   C 1 221 ? 38.038 99.518  69.598 1   46.98  ? 243 LYS   C CA  1 
ATOM   7133  C  C   . LYS   C 1 221 ? 39.09  99.977  68.566 1   46.74  ? 243 LYS   C C   1 
ATOM   7134  O  O   . LYS   C 1 221 ? 40.195 99.425  68.529 1   47.17  ? 243 LYS   C O   1 
ATOM   7135  C  CB  . LYS   C 1 221 ? 37.077 98.509  68.964 1   47.49  ? 243 LYS   C CB  1 
ATOM   7136  C  CG  . LYS   C 1 221 ? 36.006 98.007  69.909 1   49.95  ? 243 LYS   C CG  1 
ATOM   7137  C  CD  . LYS   C 1 221 ? 36.309 96.641  70.473 1   52.83  ? 243 LYS   C CD  1 
ATOM   7138  C  CE  . LYS   C 1 221 ? 35.03  96.018  70.986 1   55.7   ? 243 LYS   C CE  1 
ATOM   7139  N  NZ  . LYS   C 1 221 ? 35.227 94.625  71.448 1   58.02  ? 243 LYS   C NZ  1 
ATOM   7140  N  N   . ARG   C 1 222 ? 38.749 101.002 67.758 1   45.65  ? 244 ARG   C N   1 
ATOM   7141  C  CA  . ARG   C 1 222 ? 39.635 101.597 66.772 1   45.2   ? 244 ARG   C CA  1 
ATOM   7142  C  C   . ARG   C 1 222 ? 40.794 102.293 67.467 1   46.72  ? 244 ARG   C C   1 
ATOM   7143  O  O   . ARG   C 1 222 ? 41.94  102.07  67.075 1   46.79  ? 244 ARG   C O   1 
ATOM   7144  C  CB  . ARG   C 1 222 ? 38.891 102.587 65.876 1   44.6   ? 244 ARG   C CB  1 
ATOM   7145  C  CG  . ARG   C 1 222 ? 37.723 101.98  65.118 1   45.64  ? 244 ARG   C CG  1 
ATOM   7146  C  CD  . ARG   C 1 222 ? 38.094 100.795 64.239 1   46.4   ? 244 ARG   C CD  1 
ATOM   7147  N  NE  . ARG   C 1 222 ? 39.021 101.156 63.169 1   46.84  ? 244 ARG   C NE  1 
ATOM   7148  C  CZ  . ARG   C 1 222 ? 39.97  100.353 62.698 1   46.91  ? 244 ARG   C CZ  1 
ATOM   7149  N  NH1 . ARG   C 1 222 ? 40.131 99.132  63.204 1   46.92  ? 244 ARG   C NH1 1 
ATOM   7150  N  NH2 . ARG   C 1 222 ? 40.772 100.766 61.723 1   44.44  ? 244 ARG   C NH2 1 
ATOM   7151  N  N   . ARG   C 1 223 ? 40.519 103.077 68.551 1   47.43  ? 245 ARG   C N   1 
ATOM   7152  C  CA  . ARG   C 1 223 ? 41.548 103.769 69.351 1   47.73  ? 245 ARG   C CA  1 
ATOM   7153  C  C   . ARG   C 1 223 ? 42.589 102.788 69.852 1   47.11  ? 245 ARG   C C   1 
ATOM   7154  O  O   . ARG   C 1 223 ? 43.774 103.102 69.836 1   47.13  ? 245 ARG   C O   1 
ATOM   7155  C  CB  . ARG   C 1 223 ? 40.924 104.519 70.548 1   49.79  ? 245 ARG   C CB  1 
ATOM   7156  C  CG  . ARG   C 1 223 ? 40.156 105.756 70.133 1   53.8   ? 245 ARG   C CG  1 
ATOM   7157  C  CD  . ARG   C 1 223 ? 39.894 106.726 71.285 1   56.93  ? 245 ARG   C CD  1 
ATOM   7158  N  NE  . ARG   C 1 223 ? 38.82  107.676 70.972 1   59.67  ? 245 ARG   C NE  1 
ATOM   7159  C  CZ  . ARG   C 1 223 ? 38.983 108.786 70.248 1   62.44  ? 245 ARG   C CZ  1 
ATOM   7160  N  NH1 . ARG   C 1 223 ? 40.172 109.087 69.736 1   62.14  ? 245 ARG   C NH1 1 
ATOM   7161  N  NH2 . ARG   C 1 223 ? 37.952 109.584 70.002 1   62.73  ? 245 ARG   C NH2 1 
ATOM   7162  N  N   . GLU   C 1 224 ? 42.144 101.593 70.282 1   46.72  ? 246 GLU   C N   1 
ATOM   7163  C  CA  . GLU   C 1 224 ? 43.027 100.525 70.743 1   46.83  ? 246 GLU   C CA  1 
ATOM   7164  C  C   . GLU   C 1 224 ? 43.88  99.952  69.614 1   46.3   ? 246 GLU   C C   1 
ATOM   7165  O  O   . GLU   C 1 224 ? 45.029 99.611  69.845 1   45.94  ? 246 GLU   C O   1 
ATOM   7166  C  CB  . GLU   C 1 224 ? 42.222 99.398  71.392 1   49.58  ? 246 GLU   C CB  1 
ATOM   7167  C  CG  . GLU   C 1 224 ? 42.276 99.383  72.902 1   55.65  ? 246 GLU   C CG  1 
ATOM   7168  C  CD  . GLU   C 1 224 ? 43.606 99.716  73.555 1   63.12  ? 246 GLU   C CD  1 
ATOM   7169  O  OE1 . GLU   C 1 224 ? 44.532 98.871  73.504 1   63.7   ? 246 GLU   C OE1 1 
ATOM   7170  O  OE2 . GLU   C 1 224 ? 43.716 100.836 74.109 1   65.32  ? 246 GLU   C OE2 1 
ATOM   7171  N  N   . VAL   C 1 225 ? 43.311 99.836  68.406 1   46.19  ? 247 VAL   C N   1 
ATOM   7172  C  CA  . VAL   C 1 225 ? 43.998 99.333  67.222 1   46.82  ? 247 VAL   C CA  1 
ATOM   7173  C  C   . VAL   C 1 225 ? 45.141 100.276 66.878 1   47.91  ? 247 VAL   C C   1 
ATOM   7174  O  O   . VAL   C 1 225 ? 46.289 99.833  66.719 1   48.93  ? 247 VAL   C O   1 
ATOM   7175  C  CB  . VAL   C 1 225 ? 43.021 99.12   66.028 1   47.22  ? 247 VAL   C CB  1 
ATOM   7176  C  CG1 . VAL   C 1 225 ? 43.753 99.03   64.691 1   47.82  ? 247 VAL   C CG1 1 
ATOM   7177  C  CG2 . VAL   C 1 225 ? 42.156 97.884  66.238 1   47.54  ? 247 VAL   C CG2 1 
ATOM   7178  N  N   . TYR   C 1 226 ? 44.845 101.581 66.803 1   47.32  ? 248 TYR   C N   1 
ATOM   7179  C  CA  . TYR   C 1 226 ? 45.866 102.559 66.462 1   47.29  ? 248 TYR   C CA  1 
ATOM   7180  C  C   . TYR   C 1 226 ? 46.898 102.738 67.567 1   47.9   ? 248 TYR   C C   1 
ATOM   7181  O  O   . TYR   C 1 226 ? 48.029 103.076 67.27  1   47.97  ? 248 TYR   C O   1 
ATOM   7182  C  CB  . TYR   C 1 226 ? 45.236 103.873 66.025 1   47.32  ? 248 TYR   C CB  1 
ATOM   7183  C  CG  . TYR   C 1 226 ? 44.474 103.706 64.729 1   48.42  ? 248 TYR   C CG  1 
ATOM   7184  C  CD1 . TYR   C 1 226 ? 45.123 103.319 63.561 1   49.21  ? 248 TYR   C CD1 1 
ATOM   7185  C  CD2 . TYR   C 1 226 ? 43.098 103.872 64.682 1   49.36  ? 248 TYR   C CD2 1 
ATOM   7186  C  CE1 . TYR   C 1 226 ? 44.424 103.13  62.372 1   49.96  ? 248 TYR   C CE1 1 
ATOM   7187  C  CE2 . TYR   C 1 226 ? 42.388 103.685 63.5   1   50.41  ? 248 TYR   C CE2 1 
ATOM   7188  C  CZ  . TYR   C 1 226 ? 43.054 103.314 62.344 1   50.94  ? 248 TYR   C CZ  1 
ATOM   7189  O  OH  . TYR   C 1 226 ? 42.348 103.125 61.177 1   52.02  ? 248 TYR   C OH  1 
ATOM   7190  N  N   . ARG   C 1 227 ? 46.547 102.441 68.823 1   48     ? 249 ARG   C N   1 
ATOM   7191  C  CA  . ARG   C 1 227 ? 47.482 102.493 69.939 1   48.24  ? 249 ARG   C CA  1 
ATOM   7192  C  C   . ARG   C 1 227 ? 48.581 101.444 69.731 1   48.86  ? 249 ARG   C C   1 
ATOM   7193  O  O   . ARG   C 1 227 ? 49.752 101.722 69.972 1   49.04  ? 249 ARG   C O   1 
ATOM   7194  C  CB  . ARG   C 1 227 ? 46.738 102.211 71.245 1   49.13  ? 249 ARG   C CB  1 
ATOM   7195  C  CG  . ARG   C 1 227 ? 47.278 102.993 72.42  1   51.15  ? 249 ARG   C CG  1 
ATOM   7196  C  CD  . ARG   C 1 227 ? 46.52  102.673 73.684 1   52.07  ? 249 ARG   C CD  1 
ATOM   7197  N  NE  . ARG   C 1 227 ? 46.762 101.304 74.14  1   52.71  ? 249 ARG   C NE  1 
ATOM   7198  C  CZ  . ARG   C 1 227 ? 47.758 100.946 74.947 1   53.47  ? 249 ARG   C CZ  1 
ATOM   7199  N  NH1 . ARG   C 1 227 ? 48.649 101.846 75.354 1   53.19  ? 249 ARG   C NH1 1 
ATOM   7200  N  NH2 . ARG   C 1 227 ? 47.892 99.683  75.324 1   52.59  ? 249 ARG   C NH2 1 
ATOM   7201  N  N   . SER   C 1 228 ? 48.212 100.254 69.232 1   49.18  ? 250 SER   C N   1 
ATOM   7202  C  CA  . SER   C 1 228 ? 49.152 99.165  68.978 1   49.7   ? 250 SER   C CA  1 
ATOM   7203  C  C   . SER   C 1 228 ? 50.171 99.471  67.875 1   50.6   ? 250 SER   C C   1 
ATOM   7204  O  O   . SER   C 1 228 ? 51.167 98.763  67.776 1   50.58  ? 250 SER   C O   1 
ATOM   7205  C  CB  . SER   C 1 228 ? 48.403 97.875  68.661 1   50.04  ? 250 SER   C CB  1 
ATOM   7206  O  OG  . SER   C 1 228 ? 47.752 97.939  67.403 1   51.19  ? 250 SER   C OG  1 
ATOM   7207  N  N   . ILE   C 1 229 ? 49.93  100.51  67.04  1   50.92  ? 251 ILE   C N   1 
ATOM   7208  C  CA  . ILE   C 1 229 ? 50.872 100.874 65.984 1   51.19  ? 251 ILE   C CA  1 
ATOM   7209  C  C   . ILE   C 1 229 ? 51.511 102.249 66.229 1   51.97  ? 251 ILE   C C   1 
ATOM   7210  O  O   . ILE   C 1 229 ? 52.66  102.458 65.872 1   52.35  ? 251 ILE   C O   1 
ATOM   7211  C  CB  . ILE   C 1 229 ? 50.27  100.745 64.56  1   51.37  ? 251 ILE   C CB  1 
ATOM   7212  C  CG1 . ILE   C 1 229 ? 48.992 101.568 64.378 1   51.88  ? 251 ILE   C CG1 1 
ATOM   7213  C  CG2 . ILE   C 1 229 ? 50.022 99.293  64.212 1   52     ? 251 ILE   C CG2 1 
ATOM   7214  C  CD1 . ILE   C 1 229 ? 48.611 101.8   62.957 1   52.41  ? 251 ILE   C CD1 1 
ATOM   7215  N  N   . PHE   C 1 230 ? 50.794 103.164 66.862 1   52.29  ? 252 PHE   C N   1 
ATOM   7216  C  CA  . PHE   C 1 230 ? 51.307 104.505 67.126 1   53.23  ? 252 PHE   C CA  1 
ATOM   7217  C  C   . PHE   C 1 230 ? 52.09  104.636 68.448 1   54.28  ? 252 PHE   C C   1 
ATOM   7218  O  O   . PHE   C 1 230 ? 52.668 105.689 68.711 1   54.59  ? 252 PHE   C O   1 
ATOM   7219  C  CB  . PHE   C 1 230 ? 50.177 105.529 67.035 1   53.05  ? 252 PHE   C CB  1 
ATOM   7220  C  CG  . PHE   C 1 230 ? 49.519 105.606 65.671 1   53.19  ? 252 PHE   C CG  1 
ATOM   7221  C  CD1 . PHE   C 1 230 ? 50.234 105.324 64.517 1   53.6   ? 252 PHE   C CD1 1 
ATOM   7222  C  CD2 . PHE   C 1 230 ? 48.195 105.983 65.543 1   53.54  ? 252 PHE   C CD2 1 
ATOM   7223  C  CE1 . PHE   C 1 230 ? 49.629 105.399 63.271 1   53.86  ? 252 PHE   C CE1 1 
ATOM   7224  C  CE2 . PHE   C 1 230 ? 47.6   106.067 64.289 1   53.92  ? 252 PHE   C CE2 1 
ATOM   7225  C  CZ  . PHE   C 1 230 ? 48.32  105.777 63.165 1   53.45  ? 252 PHE   C CZ  1 
ATOM   7226  N  N   . ASP   C 1 231 ? 52.131 103.566 69.261 1   54.62  ? 253 ASP   C N   1 
ATOM   7227  C  CA  . ASP   C 1 231 ? 52.915 103.516 70.488 1   55.28  ? 253 ASP   C CA  1 
ATOM   7228  C  C   . ASP   C 1 231 ? 53.93  102.411 70.255 1   55.17  ? 253 ASP   C C   1 
ATOM   7229  O  O   . ASP   C 1 231 ? 53.554 101.241 70.207 1   54.77  ? 253 ASP   C O   1 
ATOM   7230  C  CB  . ASP   C 1 231 ? 52.038 103.193 71.711 1   57.57  ? 253 ASP   C CB  1 
ATOM   7231  C  CG  . ASP   C 1 231 ? 52.729 103.349 73.066 1   63.96  ? 253 ASP   C CG  1 
ATOM   7232  O  OD1 . ASP   C 1 231 ? 53.994 103.406 73.098 1   64.61  ? 253 ASP   C OD1 1 
ATOM   7233  O  OD2 . ASP   C 1 231 ? 52.008 103.411 74.099 1   67.02  ? 253 ASP   C OD2 1 
ATOM   7234  N  N   . PRO   C 1 232 ? 55.215 102.771 70.074 1   55.23  ? 254 PRO   C N   1 
ATOM   7235  C  CA  . PRO   C 1 232 ? 56.241 101.75  69.813 1   55.66  ? 254 PRO   C CA  1 
ATOM   7236  C  C   . PRO   C 1 232 ? 56.42  100.738 70.937 1   56.71  ? 254 PRO   C C   1 
ATOM   7237  O  O   . PRO   C 1 232 ? 56.754 99.589  70.666 1   57.09  ? 254 PRO   C O   1 
ATOM   7238  C  CB  . PRO   C 1 232 ? 57.516 102.566 69.57  1   55.98  ? 254 PRO   C CB  1 
ATOM   7239  C  CG  . PRO   C 1 232 ? 57.047 103.947 69.274 1   56.25  ? 254 PRO   C CG  1 
ATOM   7240  C  CD  . PRO   C 1 232 ? 55.79  104.126 70.06  1   54.7   ? 254 PRO   C CD  1 
ATOM   7241  N  N   . ALA   C 1 233 ? 56.151 101.14  72.178 1   56.87  ? 255 ALA   C N   1 
ATOM   7242  C  CA  . ALA   C 1 233 ? 56.247 100.243 73.318 1   57.41  ? 255 ALA   C CA  1 
ATOM   7243  C  C   . ALA   C 1 233 ? 55.186 99.143  73.232 1   57.69  ? 255 ALA   C C   1 
ATOM   7244  O  O   . ALA   C 1 233 ? 55.486 97.995  73.56  1   58.26  ? 255 ALA   C O   1 
ATOM   7245  C  CB  . ALA   C 1 233 ? 56.093 101.027 74.613 1   57.55  ? 255 ALA   C CB  1 
ATOM   7246  N  N   . VAL   C 1 234 ? 53.96  99.482  72.785 1   57.42  ? 256 VAL   C N   1 
ATOM   7247  C  CA  . VAL   C 1 234 ? 52.873 98.498  72.629 1   57.87  ? 256 VAL   C CA  1 
ATOM   7248  C  C   . VAL   C 1 234 ? 53.192 97.518  71.496 1   58.91  ? 256 VAL   C C   1 
ATOM   7249  O  O   . VAL   C 1 234 ? 52.907 96.326  71.613 1   59.03  ? 256 VAL   C O   1 
ATOM   7250  C  CB  . VAL   C 1 234 ? 51.485 99.165  72.449 1   57.83  ? 256 VAL   C CB  1 
ATOM   7251  C  CG1 . VAL   C 1 234 ? 50.378 98.126  72.318 1   57.73  ? 256 VAL   C CG1 1 
ATOM   7252  C  CG2 . VAL   C 1 234 ? 51.192 100.102 73.603 1   58.13  ? 256 VAL   C CG2 1 
ATOM   7253  N  N   . HIS   C 1 235 ? 53.829 98.013  70.423 1   59.79  ? 257 HIS   C N   1 
ATOM   7254  C  CA  . HIS   C 1 235 ? 54.249 97.187  69.302 1   61.14  ? 257 HIS   C CA  1 
ATOM   7255  C  C   . HIS   C 1 235 ? 55.337 96.224  69.773 1   62.78  ? 257 HIS   C C   1 
ATOM   7256  O  O   . HIS   C 1 235 ? 55.208 95.024  69.55  1   63.23  ? 257 HIS   C O   1 
ATOM   7257  C  CB  . HIS   C 1 235 ? 54.742 98.051  68.125 1   61.91  ? 257 HIS   C CB  1 
ATOM   7258  C  CG  . HIS   C 1 235 ? 55.386 97.258  67.031 1   64.39  ? 257 HIS   C CG  1 
ATOM   7259  N  ND1 . HIS   C 1 235 ? 54.632 96.559  66.104 1   66.4   ? 257 HIS   C ND1 1 
ATOM   7260  C  CD2 . HIS   C 1 235 ? 56.696 97.041  66.78  1   65.47  ? 257 HIS   C CD2 1 
ATOM   7261  C  CE1 . HIS   C 1 235 ? 55.502 95.948  65.318 1   66.71  ? 257 HIS   C CE1 1 
ATOM   7262  N  NE2 . HIS   C 1 235 ? 56.756 96.209  65.686 1   66.63  ? 257 HIS   C NE2 1 
ATOM   7263  N  N   . ASP   C 1 236 ? 56.381 96.735  70.455 1   63.49  ? 258 ASP   C N   1 
ATOM   7264  C  CA  . ASP   C 1 236 ? 57.485 95.921  70.968 1   64.53  ? 258 ASP   C CA  1 
ATOM   7265  C  C   . ASP   C 1 236 ? 57.006 94.816  71.902 1   65.34  ? 258 ASP   C C   1 
ATOM   7266  O  O   . ASP   C 1 236 ? 57.593 93.736  71.918 1   65.61  ? 258 ASP   C O   1 
ATOM   7267  C  CB  . ASP   C 1 236 ? 58.523 96.789  71.684 1   66.55  ? 258 ASP   C CB  1 
ATOM   7268  C  CG  . ASP   C 1 236 ? 59.231 97.797  70.797 1   72.22  ? 258 ASP   C CG  1 
ATOM   7269  O  OD1 . ASP   C 1 236 ? 59.161 97.649  69.55  1   72.55  ? 258 ASP   C OD1 1 
ATOM   7270  O  OD2 . ASP   C 1 236 ? 59.85  98.749  71.352 1   75.06  ? 258 ASP   C OD2 1 
ATOM   7271  N  N   . ALA   C 1 237 ? 55.937 95.074  72.662 1   65.62  ? 259 ALA   C N   1 
ATOM   7272  C  CA  . ALA   C 1 237 ? 55.362 94.091  73.573 1   66.56  ? 259 ALA   C CA  1 
ATOM   7273  C  C   . ALA   C 1 237 ? 54.76  92.918  72.792 1   67.3   ? 259 ALA   C C   1 
ATOM   7274  O  O   . ALA   C 1 237 ? 54.951 91.765  73.171 1   67.44  ? 259 ALA   C O   1 
ATOM   7275  C  CB  . ALA   C 1 237 ? 54.301 94.748  74.449 1   66.76  ? 259 ALA   C CB  1 
ATOM   7276  N  N   . LEU   C 1 238 ? 54.069 93.221  71.685 1   67.54  ? 260 LEU   C N   1 
ATOM   7277  C  CA  . LEU   C 1 238 ? 53.455 92.225  70.811 1   68.25  ? 260 LEU   C CA  1 
ATOM   7278  C  C   . LEU   C 1 238 ? 54.499 91.415  70.043 1   69.57  ? 260 LEU   C C   1 
ATOM   7279  O  O   . LEU   C 1 238 ? 54.249 90.254  69.735 1   69.62  ? 260 LEU   C O   1 
ATOM   7280  C  CB  . LEU   C 1 238 ? 52.507 92.913  69.821 1   68.01  ? 260 LEU   C CB  1 
ATOM   7281  C  CG  . LEU   C 1 238 ? 51.23  93.438  70.425 1   68.5   ? 260 LEU   C CG  1 
ATOM   7282  C  CD1 . LEU   C 1 238 ? 50.629 94.518  69.564 1   68.5   ? 260 LEU   C CD1 1 
ATOM   7283  C  CD2 . LEU   C 1 238 ? 50.264 92.304  70.706 1   68.89  ? 260 LEU   C CD2 1 
ATOM   7284  N  N   . VAL   C 1 239 ? 55.656 92.025  69.715 1   70.53  ? 261 VAL   C N   1 
ATOM   7285  C  CA  . VAL   C 1 239 ? 56.739 91.343  69.01  1   72.02  ? 261 VAL   C CA  1 
ATOM   7286  C  C   . VAL   C 1 239 ? 57.374 90.326  69.957 1   73.64  ? 261 VAL   C C   1 
ATOM   7287  O  O   . VAL   C 1 239 ? 57.585 89.176  69.56  1   74     ? 261 VAL   C O   1 
ATOM   7288  C  CB  . VAL   C 1 239 ? 57.785 92.329  68.435 1   72.79  ? 261 VAL   C CB  1 
ATOM   7289  C  CG1 . VAL   C 1 239 ? 59.001 91.583  67.901 1   73.42  ? 261 VAL   C CG1 1 
ATOM   7290  C  CG2 . VAL   C 1 239 ? 57.175 93.197  67.343 1   73.17  ? 261 VAL   C CG2 1 
ATOM   7291  N  N   . ARG   C 1 240 ? 57.617 90.732  71.23  1   74.39  ? 262 ARG   C N   1 
ATOM   7292  C  CA  . ARG   C 1 240 ? 58.168 89.863  72.279 1   75.54  ? 262 ARG   C CA  1 
ATOM   7293  C  C   . ARG   C 1 240 ? 57.201 88.733  72.627 1   76.13  ? 262 ARG   C C   1 
ATOM   7294  O  O   . ARG   C 1 240 ? 57.625 87.611  72.891 1   76.47  ? 262 ARG   C O   1 
ATOM   7295  C  CB  . ARG   C 1 240 ? 58.496 90.671  73.537 1   77.54  ? 262 ARG   C CB  1 
ATOM   7296  C  CG  . ARG   C 1 240 ? 59.744 91.514  73.376 1   82.33  ? 262 ARG   C CG  1 
ATOM   7297  C  CD  . ARG   C 1 240 ? 60.15  92.156  74.689 1   86.99  ? 262 ARG   C CD  1 
ATOM   7298  N  NE  . ARG   C 1 240 ? 59.623 93.514  74.817 1   91.04  ? 262 ARG   C NE  1 
ATOM   7299  C  CZ  . ARG   C 1 240 ? 58.566 93.844  75.551 1   93.86  ? 262 ARG   C CZ  1 
ATOM   7300  N  NH1 . ARG   C 1 240 ? 57.906 92.915  76.235 1   93.69  ? 262 ARG   C NH1 1 
ATOM   7301  N  NH2 . ARG   C 1 240 ? 58.158 95.107  75.608 1   93.86  ? 262 ARG   C NH2 1 
ATOM   7302  N  N   . ARG   C 1 241 ? 55.901 89.036  72.622 1   75.96  ? 263 ARG   C N   1 
ATOM   7303  C  CA  . ARG   C 1 241 ? 54.821 88.091  72.878 1   76.04  ? 263 ARG   C CA  1 
ATOM   7304  C  C   . ARG   C 1 241 ? 54.67  87.053  71.73  1   75.12  ? 263 ARG   C C   1 
ATOM   7305  O  O   . ARG   C 1 241 ? 54.206 85.933  71.963 1   75.21  ? 263 ARG   C O   1 
ATOM   7306  C  CB  . ARG   C 1 241 ? 53.523 88.886  73.088 1   78.25  ? 263 ARG   C CB  1 
ATOM   7307  C  CG  . ARG   C 1 241 ? 52.273 88.057  73.283 1   82.58  ? 263 ARG   C CG  1 
ATOM   7308  C  CD  . ARG   C 1 241 ? 51.048 88.908  73.056 1   87     ? 263 ARG   C CD  1 
ATOM   7309  N  NE  . ARG   C 1 241 ? 50.49  89.401  74.311 1   90.86  ? 263 ARG   C NE  1 
ATOM   7310  C  CZ  . ARG   C 1 241 ? 49.386 90.135  74.408 1   93.63  ? 263 ARG   C CZ  1 
ATOM   7311  N  NH1 . ARG   C 1 241 ? 48.705 90.473  73.318 1   93.31  ? 263 ARG   C NH1 1 
ATOM   7312  N  NH2 . ARG   C 1 241 ? 48.949 90.532  75.598 1   93.93  ? 263 ARG   C NH2 1 
ATOM   7313  N  N   . GLY   C 1 242 ? 55.08  87.421  70.517 1   73.98  ? 264 GLY   C N   1 
ATOM   7314  C  CA  . GLY   C 1 242 ? 55.003 86.529  69.364 1   73.46  ? 264 GLY   C CA  1 
ATOM   7315  C  C   . GLY   C 1 242 ? 53.877 86.824  68.391 1   72.61  ? 264 GLY   C C   1 
ATOM   7316  O  O   . GLY   C 1 242 ? 53.787 86.183  67.338 1   72.76  ? 264 GLY   C O   1 
ATOM   7317  N  N   . ASP   C 1 243 ? 53.003 87.798  68.733 1   71.33  ? 265 ASP   C N   1 
ATOM   7318  C  CA  . ASP   C 1 243 ? 51.874 88.213  67.887 1   70.32  ? 265 ASP   C CA  1 
ATOM   7319  C  C   . ASP   C 1 243 ? 52.334 88.942  66.601 1   68.3   ? 265 ASP   C C   1 
ATOM   7320  O  O   . ASP   C 1 243 ? 51.63  88.938  65.588 1   68.62  ? 265 ASP   C O   1 
ATOM   7321  C  CB  . ASP   C 1 243 ? 50.898 89.091  68.695 1   72.75  ? 265 ASP   C CB  1 
ATOM   7322  C  CG  . ASP   C 1 243 ? 50.119 88.346  69.768 1   78.09  ? 265 ASP   C CG  1 
ATOM   7323  O  OD1 . ASP   C 1 243 ? 50.538 87.226  70.139 1   78.87  ? 265 ASP   C OD1 1 
ATOM   7324  O  OD2 . ASP   C 1 243 ? 49.094 88.89   70.246 1   80.62  ? 265 ASP   C OD2 1 
ATOM   7325  N  N   . ARG   C 1 244 ? 53.513 89.57   66.657 1   66.16  ? 266 ARG   C N   1 
ATOM   7326  C  CA  . ARG   C 1 244 ? 54.135 90.269  65.543 1   64.54  ? 266 ARG   C CA  1 
ATOM   7327  C  C   . ARG   C 1 244 ? 55.597 89.847  65.406 1   63.66  ? 266 ARG   C C   1 
ATOM   7328  O  O   . ARG   C 1 244 ? 56.226 89.406  66.373 1   63.81  ? 266 ARG   C O   1 
ATOM   7329  C  CB  . ARG   C 1 244 ? 54.043 91.783  65.744 1   64.57  ? 266 ARG   C CB  1 
ATOM   7330  C  CG  . ARG   C 1 244 ? 52.644 92.299  65.54  1   65.46  ? 266 ARG   C CG  1 
ATOM   7331  C  CD  . ARG   C 1 244 ? 52.573 93.79   65.731 1   66.16  ? 266 ARG   C CD  1 
ATOM   7332  N  NE  . ARG   C 1 244 ? 51.182 94.228  65.762 1   66.06  ? 266 ARG   C NE  1 
ATOM   7333  C  CZ  . ARG   C 1 244 ? 50.789 95.468  66.009 1   64.81  ? 266 ARG   C CZ  1 
ATOM   7334  N  NH1 . ARG   C 1 244 ? 51.681 96.418  66.253 1   62.72  ? 266 ARG   C NH1 1 
ATOM   7335  N  NH2 . ARG   C 1 244 ? 49.498 95.769  66.017 1   64.1   ? 266 ARG   C NH2 1 
ATOM   7336  N  N   . ARG   C 1 245 ? 56.135 89.984  64.199 1   62.44  ? 267 ARG   C N   1 
ATOM   7337  C  CA  . ARG   C 1 245 ? 57.515 89.639  63.876 1   61.47  ? 267 ARG   C CA  1 
ATOM   7338  C  C   . ARG   C 1 245 ? 58.27  90.882  63.407 1   59.43  ? 267 ARG   C C   1 
ATOM   7339  O  O   . ARG   C 1 245 ? 59.437 91.065  63.746 1   59.67  ? 267 ARG   C O   1 
ATOM   7340  C  CB  . ARG   C 1 245 ? 57.543 88.572  62.753 1   63.51  ? 267 ARG   C CB  1 
ATOM   7341  C  CG  . ARG   C 1 245 ? 57.358 87.127  63.222 1   67.15  ? 267 ARG   C CG  1 
ATOM   7342  C  CD  . ARG   C 1 245 ? 56.329 86.403  62.37  1   70.87  ? 267 ARG   C CD  1 
ATOM   7343  N  NE  . ARG   C 1 245 ? 56.419 84.948  62.5   1   74.67  ? 267 ARG   C NE  1 
ATOM   7344  C  CZ  . ARG   C 1 245 ? 55.743 84.229  63.393 1   78.56  ? 267 ARG   C CZ  1 
ATOM   7345  N  NH1 . ARG   C 1 245 ? 54.924 84.821  64.254 1   78.47  ? 267 ARG   C NH1 1 
ATOM   7346  N  NH2 . ARG   C 1 245 ? 55.887 82.913  63.439 1   79.6   ? 267 ARG   C NH2 1 
ATOM   7347  N  N   . PHE   C 1 246 ? 57.601 91.721  62.613 1   57.35  ? 268 PHE   C N   1 
ATOM   7348  C  CA  . PHE   C 1 246 ? 58.158 92.909  61.992 1   56     ? 268 PHE   C CA  1 
ATOM   7349  C  C   . PHE   C 1 246 ? 58.647 93.935  62.964 1   54.3   ? 268 PHE   C C   1 
ATOM   7350  O  O   . PHE   C 1 246 ? 58.06  94.109  64.016 1   54     ? 268 PHE   C O   1 
ATOM   7351  C  CB  . PHE   C 1 246 ? 57.1   93.579  61.102 1   55.84  ? 268 PHE   C CB  1 
ATOM   7352  C  CG  . PHE   C 1 246 ? 56.906 92.989  59.73  1   56.04  ? 268 PHE   C CG  1 
ATOM   7353  C  CD1 . PHE   C 1 246 ? 57.073 91.635  59.51  1   56.46  ? 268 PHE   C CD1 1 
ATOM   7354  C  CD2 . PHE   C 1 246 ? 56.494 93.778  58.672 1   56.64  ? 268 PHE   C CD2 1 
ATOM   7355  C  CE1 . PHE   C 1 246 ? 56.87  91.092  58.255 1   57.01  ? 268 PHE   C CE1 1 
ATOM   7356  C  CE2 . PHE   C 1 246 ? 56.267 93.228  57.424 1   57.16  ? 268 PHE   C CE2 1 
ATOM   7357  C  CZ  . PHE   C 1 246 ? 56.465 91.889  57.221 1   56.84  ? 268 PHE   C CZ  1 
ATOM   7358  N  N   . SER   C 1 247 ? 59.686 94.671  62.577 1   53.39  ? 269 SER   C N   1 
ATOM   7359  C  CA  . SER   C 1 247 ? 60.162 95.802  63.346 1   52.86  ? 269 SER   C CA  1 
ATOM   7360  C  C   . SER   C 1 247 ? 59.116 96.919  63.176 1   52.65  ? 269 SER   C C   1 
ATOM   7361  O  O   . SER   C 1 247 ? 58.345 96.918  62.206 1   52.47  ? 269 SER   C O   1 
ATOM   7362  C  CB  . SER   C 1 247 ? 61.503 96.275  62.803 1   53.71  ? 269 SER   C CB  1 
ATOM   7363  O  OG  . SER   C 1 247 ? 61.371 96.904  61.538 1   55.62  ? 269 SER   C OG  1 
ATOM   7364  N  N   . HIS   C 1 248 ? 59.116 97.901  64.083 1   52.34  ? 270 HIS   C N   1 
ATOM   7365  C  CA  . HIS   C 1 248 ? 58.172 99.017  64.002 1   52.17  ? 270 HIS   C CA  1 
ATOM   7366  C  C   . HIS   C 1 248 ? 58.238 99.746  62.641 1   51.1   ? 270 HIS   C C   1 
ATOM   7367  O  O   . HIS   C 1 248 ? 57.212 99.888  61.976 1   51.11  ? 270 HIS   C O   1 
ATOM   7368  C  CB  . HIS   C 1 248 ? 58.408 99.983  65.172 1   53.53  ? 270 HIS   C CB  1 
ATOM   7369  C  CG  . HIS   C 1 248 ? 57.309 100.976 65.35  1   55.85  ? 270 HIS   C CG  1 
ATOM   7370  N  ND1 . HIS   C 1 248 ? 56.02  100.572 65.64  1   57.46  ? 270 HIS   C ND1 1 
ATOM   7371  C  CD2 . HIS   C 1 248 ? 57.344 102.329 65.29  1   56.97  ? 270 HIS   C CD2 1 
ATOM   7372  C  CE1 . HIS   C 1 248 ? 55.307 101.682 65.722 1   57.85  ? 270 HIS   C CE1 1 
ATOM   7373  N  NE2 . HIS   C 1 248 ? 56.058 102.766 65.517 1   58     ? 270 HIS   C NE2 1 
ATOM   7374  N  N   . ARG   C 1 249 ? 59.457 100.091 62.182 1   49.94  ? 271 ARG   C N   1 
ATOM   7375  C  CA  . ARG   C 1 249 ? 59.638 100.773 60.9   1   48.95  ? 271 ARG   C CA  1 
ATOM   7376  C  C   . ARG   C 1 249 ? 59.292 99.914  59.688 1   47.51  ? 271 ARG   C C   1 
ATOM   7377  O  O   . ARG   C 1 249 ? 58.838 100.461 58.68  1   47.36  ? 271 ARG   C O   1 
ATOM   7378  C  CB  . ARG   C 1 249 ? 61.044 101.357 60.771 1   50.26  ? 271 ARG   C CB  1 
ATOM   7379  C  CG  . ARG   C 1 249 ? 61.153 102.386 59.665 1   53.45  ? 271 ARG   C CG  1 
ATOM   7380  C  CD  . ARG   C 1 249 ? 62.381 103.239 59.831 1   58.25  ? 271 ARG   C CD  1 
ATOM   7381  N  NE  . ARG   C 1 249 ? 62.594 104.105 58.672 1   62.68  ? 271 ARG   C NE  1 
ATOM   7382  C  CZ  . ARG   C 1 249 ? 62.088 105.328 58.545 1   65.91  ? 271 ARG   C CZ  1 
ATOM   7383  N  NH1 . ARG   C 1 249 ? 61.316 105.84  59.499 1   65.54  ? 271 ARG   C NH1 1 
ATOM   7384  N  NH2 . ARG   C 1 249 ? 62.344 106.048 57.461 1   66.42  ? 271 ARG   C NH2 1 
ATOM   7385  N  N   . ALA   C 1 250 ? 59.466 98.581  59.776 1   46.51  ? 272 ALA   C N   1 
ATOM   7386  C  CA  . ALA   C 1 250 ? 59.083 97.705  58.661 1   46.09  ? 272 ALA   C CA  1 
ATOM   7387  C  C   . ALA   C 1 250 ? 57.564 97.679  58.527 1   46.12  ? 272 ALA   C C   1 
ATOM   7388  O  O   . ALA   C 1 250 ? 57.053 97.709  57.411 1   46.23  ? 272 ALA   C O   1 
ATOM   7389  C  CB  . ALA   C 1 250 ? 59.609 96.301  58.868 1   45.8   ? 272 ALA   C CB  1 
ATOM   7390  N  N   . LEU   C 1 251 ? 56.842 97.667  59.664 1   45.9   ? 273 LEU   C N   1 
ATOM   7391  C  CA  . LEU   C 1 251 ? 55.384 97.695  59.693 1   45.97  ? 273 LEU   C CA  1 
ATOM   7392  C  C   . LEU   C 1 251 ? 54.859 99.044  59.161 1   46.24  ? 273 LEU   C C   1 
ATOM   7393  O  O   . LEU   C 1 251 ? 53.802 99.087  58.53  1   46.56  ? 273 LEU   C O   1 
ATOM   7394  C  CB  . LEU   C 1 251 ? 54.895 97.44   61.119 1   46.13  ? 273 LEU   C CB  1 
ATOM   7395  C  CG  . LEU   C 1 251 ? 53.395 97.346  61.302 1   48.37  ? 273 LEU   C CG  1 
ATOM   7396  C  CD1 . LEU   C 1 251 ? 52.824 96.186  60.531 1   49.25  ? 273 LEU   C CD1 1 
ATOM   7397  C  CD2 . LEU   C 1 251 ? 53.041 97.192  62.769 1   49.64  ? 273 LEU   C CD2 1 
ATOM   7398  N  N   . GLN   C 1 252 ? 55.602 100.143 59.392 1   45.75  ? 274 GLN   C N   1 
ATOM   7399  C  CA  . GLN   C 1 252 ? 55.226 101.453 58.868 1   45.7   ? 274 GLN   C CA  1 
ATOM   7400  C  C   . GLN   C 1 252 ? 55.285 101.426 57.342 1   46.47  ? 274 GLN   C C   1 
ATOM   7401  O  O   . GLN   C 1 252 ? 54.333 101.863 56.696 1   47.19  ? 274 GLN   C O   1 
ATOM   7402  C  CB  . GLN   C 1 252 ? 56.155 102.55  59.397 1   46     ? 274 GLN   C CB  1 
ATOM   7403  C  CG  . GLN   C 1 252 ? 56.123 102.736 60.903 1   46.97  ? 274 GLN   C CG  1 
ATOM   7404  C  CD  . GLN   C 1 252 ? 57.06  103.824 61.388 1   47.4   ? 274 GLN   C CD  1 
ATOM   7405  O  OE1 . GLN   C 1 252 ? 57.685 104.557 60.609 1   47.35  ? 274 GLN   C OE1 1 
ATOM   7406  N  NE2 . GLN   C 1 252 ? 57.164 103.957 62.704 1   47.04  ? 274 GLN   C NE2 1 
ATOM   7407  N  N   . GLY   C 1 253 ? 56.377 100.874 56.792 1   45.99  ? 275 GLY   C N   1 
ATOM   7408  C  CA  . GLY   C 1 253 ? 56.578 100.75  55.353 1   45.83  ? 275 GLY   C CA  1 
ATOM   7409  C  C   . GLY   C 1 253 ? 55.571 99.832  54.698 1   45.58  ? 275 GLY   C C   1 
ATOM   7410  O  O   . GLY   C 1 253 ? 55.098 100.124 53.603 1   45.73  ? 275 GLY   C O   1 
ATOM   7411  N  N   . ALA   C 1 254 ? 55.223 98.72   55.374 1   45.07  ? 276 ALA   C N   1 
ATOM   7412  C  CA  . ALA   C 1 254 ? 54.24  97.76   54.873 1   44.88  ? 276 ALA   C CA  1 
ATOM   7413  C  C   . ALA   C 1 254 ? 52.858 98.414  54.821 1   44.43  ? 276 ALA   C C   1 
ATOM   7414  O  O   . ALA   C 1 254 ? 52.166 98.278  53.814 1   44.03  ? 276 ALA   C O   1 
ATOM   7415  C  CB  . ALA   C 1 254 ? 54.208 96.518  55.757 1   45     ? 276 ALA   C CB  1 
ATOM   7416  N  N   . ILE   C 1 255 ? 52.485 99.167  55.878 1   44.32  ? 277 ILE   C N   1 
ATOM   7417  C  CA  . ILE   C 1 255 ? 51.213 99.884  55.955 1   44.59  ? 277 ILE   C CA  1 
ATOM   7418  C  C   . ILE   C 1 255 ? 51.13  100.926 54.855 1   44.46  ? 277 ILE   C C   1 
ATOM   7419  O  O   . ILE   C 1 255 ? 50.105 101.023 54.174 1   44.49  ? 277 ILE   C O   1 
ATOM   7420  C  CB  . ILE   C 1 255 ? 51.001 100.477 57.376 1   45.5   ? 277 ILE   C CB  1 
ATOM   7421  C  CG1 . ILE   C 1 255 ? 50.539 99.382  58.348 1   46.49  ? 277 ILE   C CG1 1 
ATOM   7422  C  CG2 . ILE   C 1 255 ? 50.006 101.655 57.388 1   46.21  ? 277 ILE   C CG2 1 
ATOM   7423  C  CD1 . ILE   C 1 255 ? 50.627 99.764  59.774 1   48.14  ? 277 ILE   C CD1 1 
ATOM   7424  N  N   . MET   C 1 256 ? 52.23  101.656 54.637 1   44.33  ? 278 MET   C N   1 
ATOM   7425  C  CA  . MET   C 1 256 ? 52.297 102.693 53.621 1   44.89  ? 278 MET   C CA  1 
ATOM   7426  C  C   . MET   C 1 256 ? 52.048 102.15  52.219 1   45.81  ? 278 MET   C C   1 
ATOM   7427  O  O   . MET   C 1 256 ? 51.244 102.712 51.463 1   46.21  ? 278 MET   C O   1 
ATOM   7428  C  CB  . MET   C 1 256 ? 53.639 103.426 53.683 1   45.5   ? 278 MET   C CB  1 
ATOM   7429  C  CG  . MET   C 1 256 ? 53.635 104.647 52.83  1   48.68  ? 278 MET   C CG  1 
ATOM   7430  S  SD  . MET   C 1 256 ? 55.206 105.507 52.729 1   52.53  ? 278 MET   C SD  1 
ATOM   7431  C  CE  . MET   C 1 256 ? 54.684 106.873 51.718 1   48.66  ? 278 MET   C CE  1 
ATOM   7432  N  N   . ILE   C 1 257 ? 52.718 101.042 51.883 1   45.67  ? 279 ILE   C N   1 
ATOM   7433  C  CA  . ILE   C 1 257 ? 52.574 100.39  50.594 1   45.9   ? 279 ILE   C CA  1 
ATOM   7434  C  C   . ILE   C 1 257 ? 51.12  99.936  50.373 1   45.95  ? 279 ILE   C C   1 
ATOM   7435  O  O   . ILE   C 1 257 ? 50.59  100.128 49.284 1   45.81  ? 279 ILE   C O   1 
ATOM   7436  C  CB  . ILE   C 1 257 ? 53.594 99.227  50.51  1   46.39  ? 279 ILE   C CB  1 
ATOM   7437  C  CG1 . ILE   C 1 257 ? 55.025 99.754  50.359 1   46.84  ? 279 ILE   C CG1 1 
ATOM   7438  C  CG2 . ILE   C 1 257 ? 53.254 98.251  49.4   1   46.95  ? 279 ILE   C CG2 1 
ATOM   7439  C  CD1 . ILE   C 1 257 ? 56.117 98.666  50.47  1   47.65  ? 279 ILE   C CD1 1 
ATOM   7440  N  N   . THR   C 1 258 ? 50.464 99.374  51.411 1   46.21  ? 280 THR   C N   1 
ATOM   7441  C  CA  . THR   C 1 258 ? 49.067 98.911  51.302 1   46.68  ? 280 THR   C CA  1 
ATOM   7442  C  C   . THR   C 1 258 ? 48.054 100.045 51.134 1   46.95  ? 280 THR   C C   1 
ATOM   7443  O  O   . THR   C 1 258 ? 46.949 99.8    50.649 1   46.78  ? 280 THR   C O   1 
ATOM   7444  C  CB  . THR   C 1 258 ? 48.662 97.992  52.465 1   47.56  ? 280 THR   C CB  1 
ATOM   7445  O  OG1 . THR   C 1 258 ? 48.751 98.692  53.695 1   48.82  ? 280 THR   C OG1 1 
ATOM   7446  C  CG2 . THR   C 1 258 ? 49.475 96.741  52.529 1   47.7   ? 280 THR   C CG2 1 
ATOM   7447  N  N   . PHE   C 1 259 ? 48.426 101.268 51.537 1   47.25  ? 281 PHE   C N   1 
ATOM   7448  C  CA  . PHE   C 1 259 ? 47.576 102.443 51.417 1   48.21  ? 281 PHE   C CA  1 
ATOM   7449  C  C   . PHE   C 1 259 ? 47.625 103.006 49.997 1   49.21  ? 281 PHE   C C   1 
ATOM   7450  O  O   . PHE   C 1 259 ? 46.599 103.441 49.466 1   49.43  ? 281 PHE   C O   1 
ATOM   7451  C  CB  . PHE   C 1 259 ? 48.041 103.521 52.404 1   48.38  ? 281 PHE   C CB  1 
ATOM   7452  C  CG  . PHE   C 1 259 ? 47.393 103.481 53.765 1   49.45  ? 281 PHE   C CG  1 
ATOM   7453  C  CD1 . PHE   C 1 259 ? 46.942 102.289 54.302 1   50.23  ? 281 PHE   C CD1 1 
ATOM   7454  C  CD2 . PHE   C 1 259 ? 47.267 104.633 54.526 1   50.43  ? 281 PHE   C CD2 1 
ATOM   7455  C  CE1 . PHE   C 1 259 ? 46.368 102.255 55.563 1   51.01  ? 281 PHE   C CE1 1 
ATOM   7456  C  CE2 . PHE   C 1 259 ? 46.674 104.595 55.778 1   50.94  ? 281 PHE   C CE2 1 
ATOM   7457  C  CZ  . PHE   C 1 259 ? 46.228 103.409 56.287 1   50.65  ? 281 PHE   C CZ  1 
ATOM   7458  N  N   . TYR   C 1 260 ? 48.825 103.01  49.383 1   49.49  ? 282 TYR   C N   1 
ATOM   7459  C  CA  . TYR   C 1 260 ? 49.021 103.583 48.049 1   49.74  ? 282 TYR   C CA  1 
ATOM   7460  C  C   . TYR   C 1 260 ? 49.301 102.548 46.972 1   49.58  ? 282 TYR   C C   1 
ATOM   7461  O  O   . TYR   C 1 260 ? 49.934 102.876 45.977 1   49.98  ? 282 TYR   C O   1 
ATOM   7462  C  CB  . TYR   C 1 260 ? 50.151 104.619 48.084 1   49.83  ? 282 TYR   C CB  1 
ATOM   7463  C  CG  . TYR   C 1 260 ? 49.959 105.673 49.148 1   50.72  ? 282 TYR   C CG  1 
ATOM   7464  C  CD1 . TYR   C 1 260 ? 49.006 106.67  49.002 1   51.86  ? 282 TYR   C CD1 1 
ATOM   7465  C  CD2 . TYR   C 1 260 ? 50.728 105.673 50.3   1   51.88  ? 282 TYR   C CD2 1 
ATOM   7466  C  CE1 . TYR   C 1 260 ? 48.835 107.653 49.969 1   52.74  ? 282 TYR   C CE1 1 
ATOM   7467  C  CE2 . TYR   C 1 260 ? 50.553 106.637 51.284 1   53.1   ? 282 TYR   C CE2 1 
ATOM   7468  C  CZ  . TYR   C 1 260 ? 49.597 107.624 51.117 1   53.78  ? 282 TYR   C CZ  1 
ATOM   7469  O  OH  . TYR   C 1 260 ? 49.43  108.596 52.069 1   55.25  ? 282 TYR   C OH  1 
ATOM   7470  N  N   . ARG   C 1 261 ? 48.793 101.321 47.143 1   49.18  ? 283 ARG   C N   1 
ATOM   7471  C  CA  . ARG   C 1 261 ? 48.981 100.212 46.209 1   49.54  ? 283 ARG   C CA  1 
ATOM   7472  C  C   . ARG   C 1 261 ? 48.456 100.489 44.796 1   50.03  ? 283 ARG   C C   1 
ATOM   7473  O  O   . ARG   C 1 261 ? 48.924 99.874  43.84  1   50.27  ? 283 ARG   C O   1 
ATOM   7474  C  CB  . ARG   C 1 261 ? 48.347 98.937  46.768 1   50.7   ? 283 ARG   C CB  1 
ATOM   7475  C  CG  . ARG   C 1 261 ? 46.87  99.087  47.064 1   53.86  ? 283 ARG   C CG  1 
ATOM   7476  C  CD  . ARG   C 1 261 ? 46.234 97.775  47.464 1   57.18  ? 283 ARG   C CD  1 
ATOM   7477  N  NE  . ARG   C 1 261 ? 46.076 96.877  46.324 1   59.73  ? 283 ARG   C NE  1 
ATOM   7478  C  CZ  . ARG   C 1 261 ? 45.576 95.646  46.401 1   62.86  ? 283 ARG   C CZ  1 
ATOM   7479  N  NH1 . ARG   C 1 261 ? 45.198 95.145  47.573 1   61.78  ? 283 ARG   C NH1 1 
ATOM   7480  N  NH2 . ARG   C 1 261 ? 45.466 94.898  45.31  1   64.3   ? 283 ARG   C NH2 1 
ATOM   7481  N  N   . ASP   C 1 262 ? 47.476 101.397 44.662 1   50     ? 284 ASP   C N   1 
ATOM   7482  C  CA  . ASP   C 1 262 ? 46.9   101.774 43.364 1   50.14  ? 284 ASP   C CA  1 
ATOM   7483  C  C   . ASP   C 1 262 ? 47.791 102.777 42.587 1   49.41  ? 284 ASP   C C   1 
ATOM   7484  O  O   . ASP   C 1 262 ? 47.557 103.011 41.396 1   49.11  ? 284 ASP   C O   1 
ATOM   7485  C  CB  . ASP   C 1 262 ? 45.444 102.283 43.52  1   53.1   ? 284 ASP   C CB  1 
ATOM   7486  C  CG  . ASP   C 1 262 ? 44.433 101.177 43.837 1   61.11  ? 284 ASP   C CG  1 
ATOM   7487  O  OD1 . ASP   C 1 262 ? 44.641 100.018 43.377 1   62.06  ? 284 ASP   C OD1 1 
ATOM   7488  O  OD2 . ASP   C 1 262 ? 43.443 101.461 44.559 1   65.02  ? 284 ASP   C OD2 1 
ATOM   7489  N  N   . GLU   C 1 263 ? 48.821 103.353 43.258 1   48.95  ? 285 GLU   C N   1 
ATOM   7490  C  CA  . GLU   C 1 263 ? 49.769 104.276 42.652 1   49.02  ? 285 GLU   C CA  1 
ATOM   7491  C  C   . GLU   C 1 263 ? 50.91  103.497 42.044 1   48.57  ? 285 GLU   C C   1 
ATOM   7492  O  O   . GLU   C 1 263 ? 51.442 102.593 42.677 1   48.23  ? 285 GLU   C O   1 
ATOM   7493  C  CB  . GLU   C 1 263 ? 50.318 105.26  43.686 1   52.15  ? 285 GLU   C CB  1 
ATOM   7494  C  CG  . GLU   C 1 263 ? 49.241 106.103 44.342 1   58.5   ? 285 GLU   C CG  1 
ATOM   7495  C  CD  . GLU   C 1 263 ? 48.42  106.939 43.379 1   65.7   ? 285 GLU   C CD  1 
ATOM   7496  O  OE1 . GLU   C 1 263 ? 49.006 107.508 42.426 1   68.27  ? 285 GLU   C OE1 1 
ATOM   7497  O  OE2 . GLU   C 1 263 ? 47.185 107.022 43.577 1   67.46  ? 285 GLU   C OE2 1 
ATOM   7498  N  N   . PRO   C 1 264 ? 51.314 103.855 40.816 1   48.59  ? 286 PRO   C N   1 
ATOM   7499  C  CA  . PRO   C 1 264 ? 52.404 103.127 40.147 1   48.75  ? 286 PRO   C CA  1 
ATOM   7500  C  C   . PRO   C 1 264 ? 53.686 102.932 40.96  1   49.26  ? 286 PRO   C C   1 
ATOM   7501  O  O   . PRO   C 1 264 ? 54.316 101.874 40.857 1   49.13  ? 286 PRO   C O   1 
ATOM   7502  C  CB  . PRO   C 1 264 ? 52.644 103.957 38.89  1   49.33  ? 286 PRO   C CB  1 
ATOM   7503  C  CG  . PRO   C 1 264 ? 51.33  104.586 38.613 1   49.51  ? 286 PRO   C CG  1 
ATOM   7504  C  CD  . PRO   C 1 264 ? 50.745 104.898 39.94  1   48.06  ? 286 PRO   C CD  1 
ATOM   7505  N  N   . ARG   C 1 265 ? 54.049 103.93  41.784 1   49.7   ? 287 ARG   C N   1 
ATOM   7506  C  CA  . ARG   C 1 265 ? 55.227 103.907 42.655 1   50.61  ? 287 ARG   C CA  1 
ATOM   7507  C  C   . ARG   C 1 265 ? 55.187 102.773 43.652 1   49.74  ? 287 ARG   C C   1 
ATOM   7508  O  O   . ARG   C 1 265 ? 56.226 102.219 43.982 1   49.46  ? 287 ARG   C O   1 
ATOM   7509  C  CB  . ARG   C 1 265 ? 55.315 105.214 43.446 1   54     ? 287 ARG   C CB  1 
ATOM   7510  C  CG  . ARG   C 1 265 ? 56.316 106.227 42.89  1   60.09  ? 287 ARG   C CG  1 
ATOM   7511  C  CD  . ARG   C 1 265 ? 56.144 107.634 43.49  1   66.4   ? 287 ARG   C CD  1 
ATOM   7512  N  NE  . ARG   C 1 265 ? 56.002 107.644 44.953 1   72.78  ? 287 ARG   C NE  1 
ATOM   7513  C  CZ  . ARG   C 1 265 ? 57.02  107.554 45.81  1   77.39  ? 287 ARG   C CZ  1 
ATOM   7514  N  NH1 . ARG   C 1 265 ? 58.267 107.431 45.363 1   78.38  ? 287 ARG   C NH1 1 
ATOM   7515  N  NH2 . ARG   C 1 265 ? 56.798 107.569 47.12  1   77.54  ? 287 ARG   C NH2 1 
ATOM   7516  N  N   . PHE   C 1 266 ? 53.995 102.439 44.152 1   49.43  ? 288 PHE   C N   1 
ATOM   7517  C  CA  . PHE   C 1 266 ? 53.817 101.395 45.162 1   49.17  ? 288 PHE   C CA  1 
ATOM   7518  C  C   . PHE   C 1 266 ? 53.145 100.133 44.662 1   47.81  ? 288 PHE   C C   1 
ATOM   7519  O  O   . PHE   C 1 266 ? 52.958 99.226  45.472 1   48.18  ? 288 PHE   C O   1 
ATOM   7520  C  CB  . PHE   C 1 266 ? 53.01  101.932 46.357 1   49.5   ? 288 PHE   C CB  1 
ATOM   7521  C  CG  . PHE   C 1 266 ? 53.658 103.071 47.096 1   50.35  ? 288 PHE   C CG  1 
ATOM   7522  C  CD1 . PHE   C 1 266 ? 53.416 104.381 46.729 1   51.2   ? 288 PHE   C CD1 1 
ATOM   7523  C  CD2 . PHE   C 1 266 ? 54.505 102.832 48.162 1   51.24  ? 288 PHE   C CD2 1 
ATOM   7524  C  CE1 . PHE   C 1 266 ? 54.011 105.428 47.41  1   51.96  ? 288 PHE   C CE1 1 
ATOM   7525  C  CE2 . PHE   C 1 266 ? 55.102 103.88  48.842 1   51.88  ? 288 PHE   C CE2 1 
ATOM   7526  C  CZ  . PHE   C 1 266 ? 54.857 105.17  48.458 1   51.79  ? 288 PHE   C CZ  1 
ATOM   7527  N  N   . SER   C 1 267 ? 52.763 100.061 43.371 1   46.3   ? 289 SER   C N   1 
ATOM   7528  C  CA  . SER   C 1 267 ? 52.087 98.878  42.825 1   45.33  ? 289 SER   C CA  1 
ATOM   7529  C  C   . SER   C 1 267 ? 52.978 97.637  42.798 1   44.44  ? 289 SER   C C   1 
ATOM   7530  O  O   . SER   C 1 267 ? 52.513 96.552  43.155 1   44.65  ? 289 SER   C O   1 
ATOM   7531  C  CB  . SER   C 1 267 ? 51.5   99.156  41.448 1   45.89  ? 289 SER   C CB  1 
ATOM   7532  O  OG  . SER   C 1 267 ? 52.508 99.105  40.456 1   47.79  ? 289 SER   C OG  1 
ATOM   7533  N  N   . GLN   C 1 268 ? 54.239 97.786  42.377 1   43.47  ? 290 GLN   C N   1 
ATOM   7534  C  CA  . GLN   C 1 268 ? 55.161 96.654  42.358 1   43.62  ? 290 GLN   C CA  1 
ATOM   7535  C  C   . GLN   C 1 268 ? 55.619 96.271  43.779 1   43.61  ? 290 GLN   C C   1 
ATOM   7536  O  O   . GLN   C 1 268 ? 55.515 95.088  44.117 1   43.35  ? 290 GLN   C O   1 
ATOM   7537  C  CB  . GLN   C 1 268 ? 56.326 96.864  41.372 1   45.6   ? 290 GLN   C CB  1 
ATOM   7538  C  CG  . GLN   C 1 268 ? 56.524 95.712  40.368 1   48.6   ? 290 GLN   C CG  1 
ATOM   7539  C  CD  . GLN   C 1 268 ? 55.251 95.225  39.673 1   52.83  ? 290 GLN   C CD  1 
ATOM   7540  O  OE1 . GLN   C 1 268 ? 54.345 96.001  39.318 1   53.82  ? 290 GLN   C OE1 1 
ATOM   7541  N  NE2 . GLN   C 1 268 ? 55.163 93.914  39.442 1   53.84  ? 290 GLN   C NE2 1 
ATOM   7542  N  N   . PRO   C 1 269 ? 55.971 97.22   44.689 1   43.45  ? 291 PRO   C N   1 
ATOM   7543  C  CA  . PRO   C 1 269 ? 56.274 96.817  46.075 1   43.25  ? 291 PRO   C CA  1 
ATOM   7544  C  C   . PRO   C 1 269 ? 55.109 96.063  46.738 1   43.32  ? 291 PRO   C C   1 
ATOM   7545  O  O   . PRO   C 1 269 ? 55.343 95.112  47.479 1   43.66  ? 291 PRO   C O   1 
ATOM   7546  C  CB  . PRO   C 1 269 ? 56.553 98.149  46.769 1   43.49  ? 291 PRO   C CB  1 
ATOM   7547  C  CG  . PRO   C 1 269 ? 56.979 99.056  45.685 1   43.73  ? 291 PRO   C CG  1 
ATOM   7548  C  CD  . PRO   C 1 269 ? 56.154 98.673  44.511 1   42.47  ? 291 PRO   C CD  1 
ATOM   7549  N  N   . HIS   C 1 270 ? 53.856 96.449  46.438 1   42.93  ? 292 HIS   C N   1 
ATOM   7550  C  CA  . HIS   C 1 270 ? 52.678 95.761  46.972 1   42.97  ? 292 HIS   C CA  1 
ATOM   7551  C  C   . HIS   C 1 270 ? 52.537 94.352  46.41  1   43.73  ? 292 HIS   C C   1 
ATOM   7552  O  O   . HIS   C 1 270 ? 52.157 93.435  47.136 1   44.34  ? 292 HIS   C O   1 
ATOM   7553  C  CB  . HIS   C 1 270 ? 51.39  96.551  46.722 1   42.69  ? 292 HIS   C CB  1 
ATOM   7554  C  CG  . HIS   C 1 270 ? 50.21  95.906  47.382 1   43.29  ? 292 HIS   C CG  1 
ATOM   7555  N  ND1 . HIS   C 1 270 ? 50.03  95.968  48.758 1   44.44  ? 292 HIS   C ND1 1 
ATOM   7556  C  CD2 . HIS   C 1 270 ? 49.232 95.144  46.846 1   44.05  ? 292 HIS   C CD2 1 
ATOM   7557  C  CE1 . HIS   C 1 270 ? 48.939 95.268  49.007 1   44.98  ? 292 HIS   C CE1 1 
ATOM   7558  N  NE2 . HIS   C 1 270 ? 48.421 94.756  47.889 1   45.16  ? 292 HIS   C NE2 1 
ATOM   7559  N  N   . GLN   C 1 271 ? 52.838 94.18   45.12  1   43.57  ? 293 GLN   C N   1 
ATOM   7560  C  CA  . GLN   C 1 271 ? 52.806 92.879  44.467 1   43.9   ? 293 GLN   C CA  1 
ATOM   7561  C  C   . GLN   C 1 271 ? 53.813 91.923  45.126 1   43.37  ? 293 GLN   C C   1 
ATOM   7562  O  O   . GLN   C 1 271 ? 53.503 90.753  45.336 1   43.71  ? 293 GLN   C O   1 
ATOM   7563  C  CB  . GLN   C 1 271 ? 53.064 93.035  42.956 1   46.43  ? 293 GLN   C CB  1 
ATOM   7564  C  CG  . GLN   C 1 271 ? 52.814 91.776  42.121 1   52.06  ? 293 GLN   C CG  1 
ATOM   7565  C  CD  . GLN   C 1 271 ? 51.45  91.148  42.358 1   59.88  ? 293 GLN   C CD  1 
ATOM   7566  O  OE1 . GLN   C 1 271 ? 50.448 91.83   42.627 1   62.38  ? 293 GLN   C OE1 1 
ATOM   7567  N  NE2 . GLN   C 1 271 ? 51.382 89.824  42.263 1   61.15  ? 293 GLN   C NE2 1 
ATOM   7568  N  N   . LEU   C 1 272 ? 54.975 92.444  45.53  1   42.71  ? 294 LEU   C N   1 
ATOM   7569  C  CA  . LEU   C 1 272 ? 56.027 91.712  46.235 1   42.43  ? 294 LEU   C CA  1 
ATOM   7570  C  C   . LEU   C 1 272 ? 55.491 91.184  47.58  1   41.97  ? 294 LEU   C C   1 
ATOM   7571  O  O   . LEU   C 1 272 ? 55.689 90.004  47.901 1   42.15  ? 294 LEU   C O   1 
ATOM   7572  C  CB  . LEU   C 1 272 ? 57.232 92.652  46.467 1   42.19  ? 294 LEU   C CB  1 
ATOM   7573  C  CG  . LEU   C 1 272 ? 58.575 92.01   46.755 1   42.86  ? 294 LEU   C CG  1 
ATOM   7574  C  CD1 . LEU   C 1 272 ? 59.688 92.839  46.161 1   43.24  ? 294 LEU   C CD1 1 
ATOM   7575  C  CD2 . LEU   C 1 272 ? 58.784 91.814  48.236 1   42.93  ? 294 LEU   C CD2 1 
ATOM   7576  N  N   . LEU   C 1 273 ? 54.798 92.052  48.352 1   40.47  ? 295 LEU   C N   1 
ATOM   7577  C  CA  . LEU   C 1 273 ? 54.205 91.66   49.632 1   39.24  ? 295 LEU   C CA  1 
ATOM   7578  C  C   . LEU   C 1 273 ? 53.111 90.619  49.427 1   37.84  ? 295 LEU   C C   1 
ATOM   7579  O  O   . LEU   C 1 273 ? 53.004 89.669  50.198 1   38.13  ? 295 LEU   C O   1 
ATOM   7580  C  CB  . LEU   C 1 273 ? 53.616 92.892  50.358 1   39.1   ? 295 LEU   C CB  1 
ATOM   7581  C  CG  . LEU   C 1 273 ? 54.594 93.997  50.762 1   39.25  ? 295 LEU   C CG  1 
ATOM   7582  C  CD1 . LEU   C 1 273 ? 53.872 95.103  51.494 1   39.33  ? 295 LEU   C CD1 1 
ATOM   7583  C  CD2 . LEU   C 1 273 ? 55.753 93.45   51.592 1   39.47  ? 295 LEU   C CD2 1 
ATOM   7584  N  N   . THR   C 1 274 ? 52.31  90.803  48.389 1   36.61  ? 296 THR   C N   1 
ATOM   7585  C  CA  . THR   C 1 274 ? 51.22  89.919  48.042 1   36.77  ? 296 THR   C CA  1 
ATOM   7586  C  C   . THR   C 1 274 ? 51.736 88.53   47.714 1   36.6   ? 296 THR   C C   1 
ATOM   7587  O  O   . THR   C 1 274 ? 51.163 87.546  48.174 1   36.74  ? 296 THR   C O   1 
ATOM   7588  C  CB  . THR   C 1 274 ? 50.429 90.541  46.898 1   38.39  ? 296 THR   C CB  1 
ATOM   7589  O  OG1 . THR   C 1 274 ? 49.757 91.699  47.384 1   39.32  ? 296 THR   C OG1 1 
ATOM   7590  C  CG2 . THR   C 1 274 ? 49.415 89.577  46.288 1   39.18  ? 296 THR   C CG2 1 
ATOM   7591  N  N   . LEU   C 1 275 ? 52.847 88.444  46.962 1   36.01  ? 297 LEU   C N   1 
ATOM   7592  C  CA  . LEU   C 1 275 ? 53.405 87.144  46.601 1   35.87  ? 297 LEU   C CA  1 
ATOM   7593  C  C   . LEU   C 1 275 ? 54.016 86.425  47.798 1   37.9   ? 297 LEU   C C   1 
ATOM   7594  O  O   . LEU   C 1 275 ? 53.914 85.203  47.9   1   39.03  ? 297 LEU   C O   1 
ATOM   7595  C  CB  . LEU   C 1 275 ? 54.388 87.264  45.45  1   34.47  ? 297 LEU   C CB  1 
ATOM   7596  C  CG  . LEU   C 1 275 ? 53.782 87.658  44.122 1   32.45  ? 297 LEU   C CG  1 
ATOM   7597  C  CD1 . LEU   C 1 275 ? 54.831 88.102  43.189 1   32.06  ? 297 LEU   C CD1 1 
ATOM   7598  C  CD2 . LEU   C 1 275 ? 52.976 86.534  43.549 1   32.11  ? 297 LEU   C CD2 1 
ATOM   7599  N  N   . LEU   C 1 276 ? 54.571 87.181  48.754 1   38.04  ? 298 LEU   C N   1 
ATOM   7600  C  CA  . LEU   C 1 276 ? 55.118 86.616  49.98  1   38.05  ? 298 LEU   C CA  1 
ATOM   7601  C  C   . LEU   C 1 276 ? 53.988 85.976  50.804 1   39.36  ? 298 LEU   C C   1 
ATOM   7602  O  O   . LEU   C 1 276 ? 54.183 84.927  51.419 1   39.6   ? 298 LEU   C O   1 
ATOM   7603  C  CB  . LEU   C 1 276 ? 55.794 87.724  50.79  1   37.69  ? 298 LEU   C CB  1 
ATOM   7604  C  CG  . LEU   C 1 276 ? 57.086 88.271  50.218 1   38.65  ? 298 LEU   C CG  1 
ATOM   7605  C  CD1 . LEU   C 1 276 ? 57.564 89.471  51.013 1   39.01  ? 298 LEU   C CD1 1 
ATOM   7606  C  CD2 . LEU   C 1 276 ? 58.139 87.209  50.145 1   38.99  ? 298 LEU   C CD2 1 
ATOM   7607  N  N   . MET   C 1 277 ? 52.812 86.622  50.83  1   39.91  ? 299 MET   C N   1 
ATOM   7608  C  CA  . MET   C 1 277 ? 51.65  86.11   51.544 1   40.67  ? 299 MET   C CA  1 
ATOM   7609  C  C   . MET   C 1 277 ? 51.084 84.891  50.847 1   41.12  ? 299 MET   C C   1 
ATOM   7610  O  O   . MET   C 1 277 ? 50.627 83.975  51.515 1   41.49  ? 299 MET   C O   1 
ATOM   7611  C  CB  . MET   C 1 277 ? 50.581 87.186  51.64  1   41.46  ? 299 MET   C CB  1 
ATOM   7612  C  CG  . MET   C 1 277 ? 50.805 88.137  52.78  1   43.77  ? 299 MET   C CG  1 
ATOM   7613  S  SD  . MET   C 1 277 ? 49.744 89.574  52.598 1   46.11  ? 299 MET   C SD  1 
ATOM   7614  C  CE  . MET   C 1 277 ? 48.163 88.835  52.806 1   49.37  ? 299 MET   C CE  1 
ATOM   7615  N  N   . ASP   C 1 278 ? 51.109 84.878  49.511 1   41.02  ? 300 ASP   C N   1 
ATOM   7616  C  CA  . ASP   C 1 278 ? 50.638 83.752  48.723 1   41.39  ? 300 ASP   C CA  1 
ATOM   7617  C  C   . ASP   C 1 278 ? 51.516 82.522  48.98  1   40.76  ? 300 ASP   C C   1 
ATOM   7618  O  O   . ASP   C 1 278 ? 50.986 81.43   49.137 1   40.49  ? 300 ASP   C O   1 
ATOM   7619  C  CB  . ASP   C 1 278 ? 50.611 84.126  47.224 1   44.32  ? 300 ASP   C CB  1 
ATOM   7620  C  CG  . ASP   C 1 278 ? 49.495 85.092  46.831 1   51.66  ? 300 ASP   C CG  1 
ATOM   7621  O  OD1 . ASP   C 1 278 ? 48.713 85.5    47.725 1   53.35  ? 300 ASP   C OD1 1 
ATOM   7622  O  OD2 . ASP   C 1 278 ? 49.416 85.454  45.637 1   54.02  ? 300 ASP   C OD2 1 
ATOM   7623  N  N   . ILE   C 1 279 ? 52.849 82.709  49.075 1   40.78  ? 301 ILE   C N   1 
ATOM   7624  C  CA  . ILE   C 1 279 ? 53.818 81.627  49.349 1   41.08  ? 301 ILE   C CA  1 
ATOM   7625  C  C   . ILE   C 1 279 ? 53.546 81.04   50.724 1   41.4   ? 301 ILE   C C   1 
ATOM   7626  O  O   . ILE   C 1 279 ? 53.527 79.826  50.882 1   41.95  ? 301 ILE   C O   1 
ATOM   7627  C  CB  . ILE   C 1 279 ? 55.285 82.14   49.226 1   41.24  ? 301 ILE   C CB  1 
ATOM   7628  C  CG1 . ILE   C 1 279 ? 55.696 82.336  47.764 1   41.23  ? 301 ILE   C CG1 1 
ATOM   7629  C  CG2 . ILE   C 1 279 ? 56.301 81.247  49.972 1   41.85  ? 301 ILE   C CG2 1 
ATOM   7630  C  CD1 . ILE   C 1 279 ? 56.814 83.309  47.566 1   41.75  ? 301 ILE   C CD1 1 
ATOM   7631  N  N   . ASP   C 1 280 ? 53.335 81.912  51.71  1   41.22  ? 302 ASP   C N   1 
ATOM   7632  C  CA  . ASP   C 1 280 ? 53.034 81.56   53.101 1   41.16  ? 302 ASP   C CA  1 
ATOM   7633  C  C   . ASP   C 1 280 ? 51.758 80.728  53.18  1   40.57  ? 302 ASP   C C   1 
ATOM   7634  O  O   . ASP   C 1 280 ? 51.74  79.688  53.847 1   40.88  ? 302 ASP   C O   1 
ATOM   7635  C  CB  . ASP   C 1 280 ? 52.844 82.853  53.907 1   43.22  ? 302 ASP   C CB  1 
ATOM   7636  C  CG  . ASP   C 1 280 ? 53.54  82.885  55.244 1   49.03  ? 302 ASP   C CG  1 
ATOM   7637  O  OD1 . ASP   C 1 280 ? 54.211 81.874  55.601 1   49.82  ? 302 ASP   C OD1 1 
ATOM   7638  O  OD2 . ASP   C 1 280 ? 53.422 83.914  55.942 1   51.68  ? 302 ASP   C OD2 1 
ATOM   7639  N  N   . SER   C 1 281 ? 50.695 81.186  52.487 1   39.41  ? 303 SER   C N   1 
ATOM   7640  C  CA  . SER   C 1 281 ? 49.413 80.517  52.422 1   39.12  ? 303 SER   C CA  1 
ATOM   7641  C  C   . SER   C 1 281 ? 49.525 79.137  51.754 1   37.94  ? 303 SER   C C   1 
ATOM   7642  O  O   . SER   C 1 281 ? 48.918 78.18   52.237 1   37.69  ? 303 SER   C O   1 
ATOM   7643  C  CB  . SER   C 1 281 ? 48.415 81.38   51.665 1   41.67  ? 303 SER   C CB  1 
ATOM   7644  O  OG  . SER   C 1 281 ? 47.299 81.652  52.495 1   47.16  ? 303 SER   C OG  1 
ATOM   7645  N  N   . LEU   C 1 282 ? 50.319 79.041  50.655 1   36.34  ? 304 LEU   C N   1 
ATOM   7646  C  CA  . LEU   C 1 282 ? 50.526 77.8    49.91  1   34.85  ? 304 LEU   C CA  1 
ATOM   7647  C  C   . LEU   C 1 282 ? 51.343 76.791  50.691 1   35.39  ? 304 LEU   C C   1 
ATOM   7648  O  O   . LEU   C 1 282 ? 51.105 75.583  50.546 1   35.49  ? 304 LEU   C O   1 
ATOM   7649  C  CB  . LEU   C 1 282 ? 51.149 78.066  48.538 1   33.22  ? 304 LEU   C CB  1 
ATOM   7650  C  CG  . LEU   C 1 282 ? 50.162 78.556  47.516 1   32.23  ? 304 LEU   C CG  1 
ATOM   7651  C  CD1 . LEU   C 1 282 ? 50.843 79.276  46.397 1   32.43  ? 304 LEU   C CD1 1 
ATOM   7652  C  CD2 . LEU   C 1 282 ? 49.266 77.443  47.035 1   31.61  ? 304 LEU   C CD2 1 
ATOM   7653  N  N   . ILE   C 1 283 ? 52.283 77.259  51.532 1   35.25  ? 305 ILE   C N   1 
ATOM   7654  C  CA  . ILE   C 1 283 ? 53.036 76.331  52.376 1   36.35  ? 305 ILE   C CA  1 
ATOM   7655  C  C   . ILE   C 1 283 ? 52.108 75.721  53.468 1   37.46  ? 305 ILE   C C   1 
ATOM   7656  O  O   . ILE   C 1 283 ? 52.196 74.532  53.777 1   37.26  ? 305 ILE   C O   1 
ATOM   7657  C  CB  . ILE   C 1 283 ? 54.336 76.954  52.92  1   36.53  ? 305 ILE   C CB  1 
ATOM   7658  C  CG1 . ILE   C 1 283 ? 55.336 77.19   51.785 1   37.09  ? 305 ILE   C CG1 1 
ATOM   7659  C  CG2 . ILE   C 1 283 ? 54.946 76.1    54.041 1   36.67  ? 305 ILE   C CG2 1 
ATOM   7660  C  CD1 . ILE   C 1 283 ? 56.509 78.034  52.21  1   38.68  ? 305 ILE   C CD1 1 
ATOM   7661  N  N   . THR   C 1 284 ? 51.15  76.504  53.954 1   38.64  ? 306 THR   C N   1 
ATOM   7662  C  CA  . THR   C 1 284 ? 50.156 76.022  54.907 1   40.22  ? 306 THR   C CA  1 
ATOM   7663  C  C   . THR   C 1 284 ? 49.164 75.062  54.219 1   41.39  ? 306 THR   C C   1 
ATOM   7664  O  O   . THR   C 1 284 ? 48.788 74.046  54.809 1   42.17  ? 306 THR   C O   1 
ATOM   7665  C  CB  . THR   C 1 284 ? 49.497 77.2    55.608 1   41.5   ? 306 THR   C CB  1 
ATOM   7666  O  OG1 . THR   C 1 284 ? 50.521 77.903  56.316 1   43.25  ? 306 THR   C OG1 1 
ATOM   7667  C  CG2 . THR   C 1 284 ? 48.427 76.767  56.567 1   41.78  ? 306 THR   C CG2 1 
ATOM   7668  N  N   . LYS   C 1 285 ? 48.798 75.341  52.955 1   41.02  ? 307 LYS   C N   1 
ATOM   7669  C  CA  . LYS   C 1 285 ? 47.925 74.465  52.17  1   41.17  ? 307 LYS   C CA  1 
ATOM   7670  C  C   . LYS   C 1 285 ? 48.603 73.118  51.891 1   42.17  ? 307 LYS   C C   1 
ATOM   7671  O  O   . LYS   C 1 285 ? 47.923 72.097  51.832 1   42.84  ? 307 LYS   C O   1 
ATOM   7672  C  CB  . LYS   C 1 285 ? 47.475 75.147  50.87  1   41.73  ? 307 LYS   C CB  1 
ATOM   7673  C  CG  . LYS   C 1 285 ? 46.584 76.335  51.153 1   43.85  ? 307 LYS   C CG  1 
ATOM   7674  C  CD  . LYS   C 1 285 ? 46.019 76.926  49.908 1   47.37  ? 307 LYS   C CD  1 
ATOM   7675  C  CE  . LYS   C 1 285 ? 45.053 78.031  50.273 1   50.05  ? 307 LYS   C CE  1 
ATOM   7676  N  NZ  . LYS   C 1 285 ? 44.1   78.312  49.171 1   51.39  ? 307 LYS   C NZ  1 
ATOM   7677  N  N   . TRP   C 1 286 ? 49.933 73.105  51.745 1   42.31  ? 308 TRP   C N   1 
ATOM   7678  C  CA  . TRP   C 1 286 ? 50.649 71.854  51.564 1   42.85  ? 308 TRP   C CA  1 
ATOM   7679  C  C   . TRP   C 1 286 ? 50.622 71.099  52.888 1   43.5   ? 308 TRP   C C   1 
ATOM   7680  O  O   . TRP   C 1 286 ? 50.376 69.901  52.898 1   43.8   ? 308 TRP   C O   1 
ATOM   7681  C  CB  . TRP   C 1 286 ? 52.103 72.048  51.067 1   42.71  ? 308 TRP   C CB  1 
ATOM   7682  C  CG  . TRP   C 1 286 ? 52.833 70.736  51.002 1   43.15  ? 308 TRP   C CG  1 
ATOM   7683  C  CD1 . TRP   C 1 286 ? 52.705 69.78   50.037 1   43.83  ? 308 TRP   C CD1 1 
ATOM   7684  C  CD2 . TRP   C 1 286 ? 53.599 70.137  52.06  1   43.12  ? 308 TRP   C CD2 1 
ATOM   7685  N  NE1 . TRP   C 1 286 ? 53.396 68.647  50.399 1   44.12  ? 308 TRP   C NE1 1 
ATOM   7686  C  CE2 . TRP   C 1 286 ? 53.941 68.833  51.644 1   43.81  ? 308 TRP   C CE2 1 
ATOM   7687  C  CE3 . TRP   C 1 286 ? 54.023 70.577  53.323 1   43.57  ? 308 TRP   C CE3 1 
ATOM   7688  C  CZ2 . TRP   C 1 286 ? 54.712 67.979  52.43  1   44.54  ? 308 TRP   C CZ2 1 
ATOM   7689  C  CZ3 . TRP   C 1 286 ? 54.762 69.721  54.113 1   44.32  ? 308 TRP   C CZ3 1 
ATOM   7690  C  CH2 . TRP   C 1 286 ? 55.115 68.445  53.661 1   44.56  ? 308 TRP   C CH2 1 
ATOM   7691  N  N   . ARG   C 1 287 ? 50.891 71.785  54.002 1   43.52  ? 309 ARG   C N   1 
ATOM   7692  C  CA  . ARG   C 1 287 ? 50.9   71.175  55.317 1   44.29  ? 309 ARG   C CA  1 
ATOM   7693  C  C   . ARG   C 1 287 ? 49.558 70.534  55.655 1   46     ? 309 ARG   C C   1 
ATOM   7694  O  O   . ARG   C 1 287 ? 49.524 69.47   56.277 1   47.22  ? 309 ARG   C O   1 
ATOM   7695  C  CB  . ARG   C 1 287 ? 51.218 72.231  56.377 1   44.74  ? 309 ARG   C CB  1 
ATOM   7696  C  CG  . ARG   C 1 287 ? 52.655 72.69   56.407 1   45.29  ? 309 ARG   C CG  1 
ATOM   7697  C  CD  . ARG   C 1 287 ? 52.834 73.536  57.636 1   45.44  ? 309 ARG   C CD  1 
ATOM   7698  N  NE  . ARG   C 1 287 ? 53.858 74.564  57.482 1   44.85  ? 309 ARG   C NE  1 
ATOM   7699  C  CZ  . ARG   C 1 287 ? 55.16  74.355  57.662 1   43.86  ? 309 ARG   C CZ  1 
ATOM   7700  N  NH1 . ARG   C 1 287 ? 56.023 75.353  57.518 1   42.83  ? 309 ARG   C NH1 1 
ATOM   7701  N  NH2 . ARG   C 1 287 ? 55.609 73.142  57.979 1   40.88  ? 309 ARG   C NH2 1 
ATOM   7702  N  N   . TYR   C 1 288 ? 48.464 71.191  55.267 1   46.13  ? 310 TYR   C N   1 
ATOM   7703  C  CA  . TYR   C 1 288 ? 47.123 70.702  55.511 1   46.94  ? 310 TYR   C CA  1 
ATOM   7704  C  C   . TYR   C 1 288 ? 46.872 69.473  54.651 1   46.77  ? 310 TYR   C C   1 
ATOM   7705  O  O   . TYR   C 1 288 ? 46.434 68.457  55.165 1   46.38  ? 310 TYR   C O   1 
ATOM   7706  C  CB  . TYR   C 1 288 ? 46.07  71.812  55.246 1   47.67  ? 310 TYR   C CB  1 
ATOM   7707  C  CG  . TYR   C 1 288 ? 44.643 71.331  55.409 1   49.73  ? 310 TYR   C CG  1 
ATOM   7708  C  CD1 . TYR   C 1 288 ? 44.093 71.137  56.669 1   51.29  ? 310 TYR   C CD1 1 
ATOM   7709  C  CD2 . TYR   C 1 288 ? 43.863 71.01   54.305 1   51.45  ? 310 TYR   C CD2 1 
ATOM   7710  C  CE1 . TYR   C 1 288 ? 42.799 70.638  56.828 1   52.81  ? 310 TYR   C CE1 1 
ATOM   7711  C  CE2 . TYR   C 1 288 ? 42.559 70.529  54.45  1   52.82  ? 310 TYR   C CE2 1 
ATOM   7712  C  CZ  . TYR   C 1 288 ? 42.027 70.345  55.716 1   53.9   ? 310 TYR   C CZ  1 
ATOM   7713  O  OH  . TYR   C 1 288 ? 40.742 69.851  55.88  1   55.14  ? 310 TYR   C OH  1 
ATOM   7714  N  N   . ASN   C 1 289 ? 47.171 69.555  53.347 1   47     ? 311 ASN   C N   1 
ATOM   7715  C  CA  . ASN   C 1 289 ? 46.967 68.445  52.421 1   47.26  ? 311 ASN   C CA  1 
ATOM   7716  C  C   . ASN   C 1 289 ? 47.784 67.231  52.802 1   47.15  ? 311 ASN   C C   1 
ATOM   7717  O  O   . ASN   C 1 289 ? 47.287 66.106  52.689 1   47.77  ? 311 ASN   C O   1 
ATOM   7718  C  CB  . ASN   C 1 289 ? 47.289 68.869  51     1   48.55  ? 311 ASN   C CB  1 
ATOM   7719  C  CG  . ASN   C 1 289 ? 46.106 69.402  50.223 1   51.13  ? 311 ASN   C CG  1 
ATOM   7720  O  OD1 . ASN   C 1 289 ? 46.039 69.272  48.992 1   52.18  ? 311 ASN   C OD1 1 
ATOM   7721  N  ND2 . ASN   C 1 289 ? 45.158 70.022  50.905 1   51.45  ? 311 ASN   C ND2 1 
ATOM   7722  N  N   . HIS   C 1 290 ? 49.019 67.457  53.268 1   46.48  ? 312 HIS   C N   1 
ATOM   7723  C  CA  . HIS   C 1 290 ? 49.939 66.417  53.724 1   46.91  ? 312 HIS   C CA  1 
ATOM   7724  C  C   . HIS   C 1 290 ? 49.381 65.742  54.986 1   47.31  ? 312 HIS   C C   1 
ATOM   7725  O  O   . HIS   C 1 290 ? 49.334 64.506  55.025 1   47.67  ? 312 HIS   C O   1 
ATOM   7726  C  CB  . HIS   C 1 290 ? 51.323 67.024  54.005 1   47.58  ? 312 HIS   C CB  1 
ATOM   7727  C  CG  . HIS   C 1 290 ? 52.309 66.079  54.62  1   49.25  ? 312 HIS   C CG  1 
ATOM   7728  N  ND1 . HIS   C 1 290 ? 52.787 66.273  55.905 1   50.76  ? 312 HIS   C ND1 1 
ATOM   7729  C  CD2 . HIS   C 1 290 ? 52.889 64.973  54.101 1   50.4   ? 312 HIS   C CD2 1 
ATOM   7730  C  CE1 . HIS   C 1 290 ? 53.622 65.274  56.134 1   51.29  ? 312 HIS   C CE1 1 
ATOM   7731  N  NE2 . HIS   C 1 290 ? 53.715 64.464  55.079 1   51.6   ? 312 HIS   C NE2 1 
ATOM   7732  N  N   . VAL   C 1 291 ? 48.897 66.545  55.982 1   46.61  ? 313 VAL   C N   1 
ATOM   7733  C  CA  . VAL   C 1 291 ? 48.343 66.003  57.231 1   46.87  ? 313 VAL   C CA  1 
ATOM   7734  C  C   . VAL   C 1 291 ? 47.048 65.172  56.97  1   46.55  ? 313 VAL   C C   1 
ATOM   7735  O  O   . VAL   C 1 291 ? 46.84  64.16   57.637 1   46.39  ? 313 VAL   C O   1 
ATOM   7736  C  CB  . VAL   C 1 291 ? 48.179 67.059  58.374 1   47.58  ? 313 VAL   C CB  1 
ATOM   7737  C  CG1 . VAL   C 1 291 ? 46.797 67.704  58.378 1   48.09  ? 313 VAL   C CG1 1 
ATOM   7738  C  CG2 . VAL   C 1 291 ? 48.456 66.437  59.726 1   48.2   ? 313 VAL   C CG2 1 
ATOM   7739  N  N   . ILE   C 1 292 ? 46.236 65.554  55.968 1   46.03  ? 314 ILE   C N   1 
ATOM   7740  C  CA  . ILE   C 1 292 ? 45.025 64.802  55.611 1   45.91  ? 314 ILE   C CA  1 
ATOM   7741  C  C   . ILE   C 1 292 ? 45.396 63.454  54.967 1   45.33  ? 314 ILE   C C   1 
ATOM   7742  O  O   . ILE   C 1 292 ? 44.734 62.441  55.206 1   44.87  ? 314 ILE   C O   1 
ATOM   7743  C  CB  . ILE   C 1 292 ? 44.101 65.655  54.701 1   46.2   ? 314 ILE   C CB  1 
ATOM   7744  C  CG1 . ILE   C 1 292 ? 43.58  66.878  55.452 1   47.06  ? 314 ILE   C CG1 1 
ATOM   7745  C  CG2 . ILE   C 1 292 ? 42.944 64.832  54.121 1   46.75  ? 314 ILE   C CG2 1 
ATOM   7746  C  CD1 . ILE   C 1 292 ? 42.782 66.557  56.722 1   48.52  ? 314 ILE   C CD1 1 
ATOM   7747  N  N   . MET   C 1 293 ? 46.471 63.455  54.166 1   44.95  ? 315 MET   C N   1 
ATOM   7748  C  CA  . MET   C 1 293 ? 46.976 62.267  53.5   1   45.07  ? 315 MET   C CA  1 
ATOM   7749  C  C   . MET   C 1 293 ? 47.551 61.297  54.525 1   44.99  ? 315 MET   C C   1 
ATOM   7750  O  O   . MET   C 1 293 ? 47.311 60.099  54.431 1   44.53  ? 315 MET   C O   1 
ATOM   7751  C  CB  . MET   C 1 293 ? 48.036 62.659  52.461 1   45.64  ? 315 MET   C CB  1 
ATOM   7752  C  CG  . MET   C 1 293 ? 48.734 61.471  51.822 1   46.49  ? 315 MET   C CG  1 
ATOM   7753  S  SD  . MET   C 1 293 ? 50.05  61.937  50.684 1   44.04  ? 315 MET   C SD  1 
ATOM   7754  C  CE  . MET   C 1 293 ? 51.084 62.979  51.736 1   38.04  ? 315 MET   C CE  1 
ATOM   7755  N  N   . VAL   C 1 294 ? 48.291 61.822  55.515 1   45.34  ? 316 VAL   C N   1 
ATOM   7756  C  CA  . VAL   C 1 294 ? 48.876 61.037  56.599 1   45.53  ? 316 VAL   C CA  1 
ATOM   7757  C  C   . VAL   C 1 294 ? 47.768 60.322  57.384 1   45.98  ? 316 VAL   C C   1 
ATOM   7758  O  O   . VAL   C 1 294 ? 47.889 59.143  57.695 1   46.36  ? 316 VAL   C O   1 
ATOM   7759  C  CB  . VAL   C 1 294 ? 49.726 61.952  57.508 1   46.02  ? 316 VAL   C CB  1 
ATOM   7760  C  CG1 . VAL   C 1 294 ? 50.122 61.249  58.804 1   46.61  ? 316 VAL   C CG1 1 
ATOM   7761  C  CG2 . VAL   C 1 294 ? 50.958 62.447  56.768 1   46.37  ? 316 VAL   C CG2 1 
ATOM   7762  N  N   . GLN   C 1 295 ? 46.673 61.022  57.661 1   45.69  ? 317 GLN   C N   1 
ATOM   7763  C  CA  . GLN   C 1 295 ? 45.541 60.462  58.38  1   46.02  ? 317 GLN   C CA  1 
ATOM   7764  C  C   . GLN   C 1 295 ? 44.756 59.432  57.557 1   45.82  ? 317 GLN   C C   1 
ATOM   7765  O  O   . GLN   C 1 295 ? 44.147 58.515  58.111 1   45.57  ? 317 GLN   C O   1 
ATOM   7766  C  CB  . GLN   C 1 295 ? 44.624 61.584  58.842 1   49     ? 317 GLN   C CB  1 
ATOM   7767  C  CG  . GLN   C 1 295 ? 43.883 61.213  60.11  1   56.24  ? 317 GLN   C CG  1 
ATOM   7768  C  CD  . GLN   C 1 295 ? 42.919 62.269  60.572 1   63.16  ? 317 GLN   C CD  1 
ATOM   7769  O  OE1 . GLN   C 1 295 ? 42.706 63.306  59.917 1   64.61  ? 317 GLN   C OE1 1 
ATOM   7770  N  NE2 . GLN   C 1 295 ? 42.311 62.008  61.725 1   64.66  ? 317 GLN   C NE2 1 
ATOM   7771  N  N   . ARG   C 1 296 ? 44.761 59.589  56.234 1   45.87  ? 318 ARG   C N   1 
ATOM   7772  C  CA  . ARG   C 1 296 ? 44.11  58.654  55.332 1   45.92  ? 318 ARG   C CA  1 
ATOM   7773  C  C   . ARG   C 1 296 ? 44.951 57.377  55.193 1   44.36  ? 318 ARG   C C   1 
ATOM   7774  O  O   . ARG   C 1 296 ? 44.387 56.305  54.977 1   43.7   ? 318 ARG   C O   1 
ATOM   7775  C  CB  . ARG   C 1 296 ? 43.902 59.294  53.952 1   48.81  ? 318 ARG   C CB  1 
ATOM   7776  C  CG  . ARG   C 1 296 ? 42.661 60.165  53.814 1   54.43  ? 318 ARG   C CG  1 
ATOM   7777  C  CD  . ARG   C 1 296 ? 42.51  60.644  52.365 1   59.94  ? 318 ARG   C CD  1 
ATOM   7778  N  NE  . ARG   C 1 296 ? 41.373 61.556  52.195 1   65.03  ? 318 ARG   C NE  1 
ATOM   7779  C  CZ  . ARG   C 1 296 ? 40.244 61.247  51.563 1   68.86  ? 318 ARG   C CZ  1 
ATOM   7780  N  NH1 . ARG   C 1 296 ? 40.084 60.044  51.022 1   69.62  ? 318 ARG   C NH1 1 
ATOM   7781  N  NH2 . ARG   C 1 296 ? 39.264 62.134  51.474 1   69.17  ? 318 ARG   C NH2 1 
ATOM   7782  N  N   . MET   C 1 297 ? 46.289 57.49   55.294 1   43.78  ? 319 MET   C N   1 
ATOM   7783  C  CA  . MET   C 1 297 ? 47.202 56.353  55.158 1   44.34  ? 319 MET   C CA  1 
ATOM   7784  C  C   . MET   C 1 297 ? 47.415 55.57   56.448 1   44.96  ? 319 MET   C C   1 
ATOM   7785  O  O   . MET   C 1 297 ? 47.383 54.336  56.429 1   44.98  ? 319 MET   C O   1 
ATOM   7786  C  CB  . MET   C 1 297 ? 48.587 56.806  54.655 1   44.87  ? 319 MET   C CB  1 
ATOM   7787  C  CG  . MET   C 1 297 ? 48.6   57.306  53.265 1   46.96  ? 319 MET   C CG  1 
ATOM   7788  S  SD  . MET   C 1 297 ? 48.31  56.026  52.039 1   49.08  ? 319 MET   C SD  1 
ATOM   7789  C  CE  . MET   C 1 297 ? 48.292 57.06   50.583 1   44.97  ? 319 MET   C CE  1 
ATOM   7790  N  N   . ILE   C 1 298 ? 47.737 56.271  57.547 1   45.01  ? 320 ILE   C N   1 
ATOM   7791  C  CA  . ILE   C 1 298 ? 48.08  55.608  58.799 1   45.84  ? 320 ILE   C CA  1 
ATOM   7792  C  C   . ILE   C 1 298 ? 47.262 56.077  60.017 1   46.39  ? 320 ILE   C C   1 
ATOM   7793  O  O   . ILE   C 1 298 ? 47.507 55.604  61.111 1   46.87  ? 320 ILE   C O   1 
ATOM   7794  C  CB  . ILE   C 1 298 ? 49.617 55.756  59.05  1   46.44  ? 320 ILE   C CB  1 
ATOM   7795  C  CG1 . ILE   C 1 298 ? 50.023 57.251  59.145 1   47.32  ? 320 ILE   C CG1 1 
ATOM   7796  C  CG2 . ILE   C 1 298 ? 50.439 55      57.979 1   46.77  ? 320 ILE   C CG2 1 
ATOM   7797  C  CD1 . ILE   C 1 298 ? 51.464 57.566  59.248 1   48.19  ? 320 ILE   C CD1 1 
ATOM   7798  N  N   . GLY   C 1 299 ? 46.297 56.965  59.828 1   46.58  ? 321 GLY   C N   1 
ATOM   7799  C  CA  . GLY   C 1 299 ? 45.479 57.48   60.922 1   47.73  ? 321 GLY   C CA  1 
ATOM   7800  C  C   . GLY   C 1 299 ? 46.262 58.382  61.859 1   49.14  ? 321 GLY   C C   1 
ATOM   7801  O  O   . GLY   C 1 299 ? 47.351 58.849  61.503 1   49.98  ? 321 GLY   C O   1 
ATOM   7802  N  N   . SER   C 1 300 ? 45.738 58.636  63.072 1   49.04  ? 322 SER   C N   1 
ATOM   7803  C  CA  . SER   C 1 300 ? 46.467 59.445  64.058 1   49.21  ? 322 SER   C CA  1 
ATOM   7804  C  C   . SER   C 1 300 ? 47.695 58.69   64.614 1   49.4   ? 322 SER   C C   1 
ATOM   7805  O  O   . SER   C 1 300 ? 48.703 59.305  64.951 1   49.57  ? 322 SER   C O   1 
ATOM   7806  C  CB  . SER   C 1 300 ? 45.541 59.898  65.178 1   50.39  ? 322 SER   C CB  1 
ATOM   7807  O  OG  . SER   C 1 300 ? 44.744 58.83   65.661 1   53.14  ? 322 SER   C OG  1 
ATOM   7808  N  N   . GLN   C 1 301 ? 47.621 57.355  64.655 1   49.21  ? 323 GLN   C N   1 
ATOM   7809  C  CA  . GLN   C 1 301 ? 48.713 56.485  65.084 1   49.61  ? 323 GLN   C CA  1 
ATOM   7810  C  C   . GLN   C 1 301 ? 48.607 55.111  64.409 1   50.3   ? 323 GLN   C C   1 
ATOM   7811  O  O   . GLN   C 1 301 ? 47.518 54.676  64.023 1   50.31  ? 323 GLN   C O   1 
ATOM   7812  C  CB  . GLN   C 1 301 ? 48.738 56.338  66.605 1   50.07  ? 323 GLN   C CB  1 
ATOM   7813  C  CG  . GLN   C 1 301 ? 47.411 55.914  67.202 1   51.51  ? 323 GLN   C CG  1 
ATOM   7814  C  CD  . GLN   C 1 301 ? 47.348 56.2    68.682 1   51.88  ? 323 GLN   C CD  1 
ATOM   7815  O  OE1 . GLN   C 1 301 ? 47.859 55.448  69.516 1   51.98  ? 323 GLN   C OE1 1 
ATOM   7816  N  NE2 . GLN   C 1 301 ? 46.699 57.291  69.037 1   51.67  ? 323 GLN   C NE2 1 
ATOM   7817  N  N   . GLN   C 1 302 ? 49.743 54.434  64.254 1   50.35  ? 324 GLN   C N   1 
ATOM   7818  C  CA  . GLN   C 1 302 ? 49.794 53.109  63.623 1   50.32  ? 324 GLN   C CA  1 
ATOM   7819  C  C   . GLN   C 1 302 ? 51.048 52.342  64.131 1   51.34  ? 324 GLN   C C   1 
ATOM   7820  O  O   . GLN   C 1 302 ? 51.827 52.877  64.935 1   51.71  ? 324 GLN   C O   1 
ATOM   7821  C  CB  . GLN   C 1 302 ? 49.742 53.263  62.086 1   49.91  ? 324 GLN   C CB  1 
ATOM   7822  C  CG  . GLN   C 1 302 ? 49.501 52      61.255 1   49.9   ? 324 GLN   C CG  1 
ATOM   7823  C  CD  . GLN   C 1 302 ? 48.325 51.124  61.612 1   50.42  ? 324 GLN   C CD  1 
ATOM   7824  O  OE1 . GLN   C 1 302 ? 47.153 51.501  61.492 1   49.81  ? 324 GLN   C OE1 1 
ATOM   7825  N  NE2 . GLN   C 1 302 ? 48.634 49.892  62.004 1   50.65  ? 324 GLN   C NE2 1 
ATOM   7826  N  N   . LEU   C 1 303 ? 51.19  51.072  63.742 1   51.56  ? 325 LEU   C N   1 
ATOM   7827  C  CA  . LEU   C 1 303 ? 52.295 50.226  64.145 1   52.49  ? 325 LEU   C CA  1 
ATOM   7828  C  C   . LEU   C 1 303 ? 53.613 50.818  63.647 1   54.13  ? 325 LEU   C C   1 
ATOM   7829  O  O   . LEU   C 1 303 ? 53.851 50.88   62.451 1   54.71  ? 325 LEU   C O   1 
ATOM   7830  C  CB  . LEU   C 1 303 ? 52.086 48.81   63.597 1   52.29  ? 325 LEU   C CB  1 
ATOM   7831  C  CG  . LEU   C 1 303 ? 52.85  47.735  64.32  1   53.48  ? 325 LEU   C CG  1 
ATOM   7832  C  CD1 . LEU   C 1 303 ? 52.335 47.556  65.728 1   53.52  ? 325 LEU   C CD1 1 
ATOM   7833  C  CD2 . LEU   C 1 303 ? 52.783 46.436  63.572 1   54.39  ? 325 LEU   C CD2 1 
ATOM   7834  N  N   . GLY   C 1 304 ? 54.434 51.281  64.576 1   54.62  ? 326 GLY   C N   1 
ATOM   7835  C  CA  . GLY   C 1 304 ? 55.715 51.917  64.295 1   55.5   ? 326 GLY   C CA  1 
ATOM   7836  C  C   . GLY   C 1 304 ? 55.758 53.379  64.708 1   56.34  ? 326 GLY   C C   1 
ATOM   7837  O  O   . GLY   C 1 304 ? 56.836 53.931  64.951 1   56.24  ? 326 GLY   C O   1 
ATOM   7838  N  N   . THR   C 1 305 ? 54.573 54.012  64.809 1   56.83  ? 327 THR   C N   1 
ATOM   7839  C  CA  . THR   C 1 305 ? 54.406 55.421  65.142 1   57.84  ? 327 THR   C CA  1 
ATOM   7840  C  C   . THR   C 1 305 ? 54.726 55.727  66.612 1   58.55  ? 327 THR   C C   1 
ATOM   7841  O  O   . THR   C 1 305 ? 55.233 56.812  66.918 1   58.91  ? 327 THR   C O   1 
ATOM   7842  C  CB  . THR   C 1 305 ? 53.004 55.892  64.734 1   59.81  ? 327 THR   C CB  1 
ATOM   7843  O  OG1 . THR   C 1 305 ? 52.724 55.423  63.416 1   61.01  ? 327 THR   C OG1 1 
ATOM   7844  C  CG2 . THR   C 1 305 ? 52.881 57.401  64.725 1   61.07  ? 327 THR   C CG2 1 
ATOM   7845  N  N   . GLY   C 1 306 ? 54.449 54.767  67.497 1   58.4   ? 328 GLY   C N   1 
ATOM   7846  C  CA  . GLY   C 1 306 ? 54.674 54.931  68.925 1   58.56  ? 328 GLY   C CA  1 
ATOM   7847  C  C   . GLY   C 1 306 ? 53.763 55.996  69.505 1   58.33  ? 328 GLY   C C   1 
ATOM   7848  O  O   . GLY   C 1 306 ? 54.22  56.906  70.211 1   58.47  ? 328 GLY   C O   1 
ATOM   7849  N  N   . GLY   C 1 307 ? 52.478 55.895  69.165 1   57.68  ? 329 GLY   C N   1 
ATOM   7850  C  CA  . GLY   C 1 307 ? 51.467 56.851  69.603 1   57.5   ? 329 GLY   C CA  1 
ATOM   7851  C  C   . GLY   C 1 307 ? 51.139 57.89   68.547 1   56.95  ? 329 GLY   C C   1 
ATOM   7852  O  O   . GLY   C 1 307 ? 51.589 57.776  67.408 1   57.21  ? 329 GLY   C O   1 
ATOM   7853  N  N   . SER   C 1 308 ? 50.336 58.908  68.897 1   55.96  ? 330 SER   C N   1 
ATOM   7854  C  CA  . SER   C 1 308 ? 49.95  59.944  67.937 1   55.28  ? 330 SER   C CA  1 
ATOM   7855  C  C   . SER   C 1 308 ? 50.818 61.188  68.017 1   54.46  ? 330 SER   C C   1 
ATOM   7856  O  O   . SER   C 1 308 ? 50.368 62.258  67.616 1   54.03  ? 330 SER   C O   1 
ATOM   7857  C  CB  . SER   C 1 308 ? 48.474 60.312  68.081 1   56.59  ? 330 SER   C CB  1 
ATOM   7858  O  OG  . SER   C 1 308 ? 48.152 60.829  69.36  1   59.26  ? 330 SER   C OG  1 
ATOM   7859  N  N   . SER   C 1 309 ? 52.073 61.05   68.492 1   54.21  ? 331 SER   C N   1 
ATOM   7860  C  CA  . SER   C 1 309 ? 53.012 62.173  68.66  1   54.33  ? 331 SER   C CA  1 
ATOM   7861  C  C   . SER   C 1 309 ? 53.436 62.857  67.356 1   54.02  ? 331 SER   C C   1 
ATOM   7862  O  O   . SER   C 1 309 ? 53.458 64.089  67.288 1   54.27  ? 331 SER   C O   1 
ATOM   7863  C  CB  . SER   C 1 309 ? 54.242 61.757  69.466 1   56.06  ? 331 SER   C CB  1 
ATOM   7864  O  OG  . SER   C 1 309 ? 54.591 60.385  69.344 1   58.8   ? 331 SER   C OG  1 
ATOM   7865  N  N   . GLY   C 1 310 ? 53.765 62.056  66.342 1   53.17  ? 332 GLY   C N   1 
ATOM   7866  C  CA  . GLY   C 1 310 ? 54.172 62.564  65.037 1   52.39  ? 332 GLY   C CA  1 
ATOM   7867  C  C   . GLY   C 1 310 ? 53.044 63.251  64.295 1   51.29  ? 332 GLY   C C   1 
ATOM   7868  O  O   . GLY   C 1 310 ? 53.257 64.296  63.678 1   51.48  ? 332 GLY   C O   1 
ATOM   7869  N  N   . TYR   C 1 311 ? 51.829 62.674  64.367 1   50.24  ? 333 TYR   C N   1 
ATOM   7870  C  CA  . TYR   C 1 311 ? 50.628 63.221  63.738 1   49.82  ? 333 TYR   C CA  1 
ATOM   7871  C  C   . TYR   C 1 311 ? 50.255 64.545  64.398 1   48.88  ? 333 TYR   C C   1 
ATOM   7872  O  O   . TYR   C 1 311 ? 49.949 65.509  63.704 1   49.24  ? 333 TYR   C O   1 
ATOM   7873  C  CB  . TYR   C 1 311 ? 49.478 62.203  63.826 1   50.43  ? 333 TYR   C CB  1 
ATOM   7874  C  CG  . TYR   C 1 311 ? 48.096 62.775  63.579 1   51.9   ? 333 TYR   C CG  1 
ATOM   7875  C  CD1 . TYR   C 1 311 ? 47.648 63.037  62.29  1   53.07  ? 333 TYR   C CD1 1 
ATOM   7876  C  CD2 . TYR   C 1 311 ? 47.237 63.048  64.633 1   53.03  ? 333 TYR   C CD2 1 
ATOM   7877  C  CE1 . TYR   C 1 311 ? 46.388 63.568  62.06  1   54.16  ? 333 TYR   C CE1 1 
ATOM   7878  C  CE2 . TYR   C 1 311 ? 45.969 63.562  64.415 1   54.08  ? 333 TYR   C CE2 1 
ATOM   7879  C  CZ  . TYR   C 1 311 ? 45.549 63.825  63.127 1   55.42  ? 333 TYR   C CZ  1 
ATOM   7880  O  OH  . TYR   C 1 311 ? 44.305 64.371  62.915 1   58     ? 333 TYR   C OH  1 
ATOM   7881  N  N   . GLN   C 1 312 ? 50.292 64.59   65.743 1   47.66  ? 334 GLN   C N   1 
ATOM   7882  C  CA  . GLN   C 1 312 ? 49.992 65.788  66.518 1   46.21  ? 334 GLN   C CA  1 
ATOM   7883  C  C   . GLN   C 1 312 ? 51.008 66.892  66.287 1   44.54  ? 334 GLN   C C   1 
ATOM   7884  O  O   . GLN   C 1 312 ? 50.649 68.064  66.392 1   44.4   ? 334 GLN   C O   1 
ATOM   7885  C  CB  . GLN   C 1 312 ? 49.856 65.475  68.017 1   47.2   ? 334 GLN   C CB  1 
ATOM   7886  C  CG  . GLN   C 1 312 ? 48.526 64.851  68.421 1   50.03  ? 334 GLN   C CG  1 
ATOM   7887  C  CD  . GLN   C 1 312 ? 47.311 65.652  68.005 1   54.75  ? 334 GLN   C CD  1 
ATOM   7888  O  OE1 . GLN   C 1 312 ? 46.306 65.094  67.552 1   56.54  ? 334 GLN   C OE1 1 
ATOM   7889  N  NE2 . GLN   C 1 312 ? 47.363 66.973  68.154 1   55.6   ? 334 GLN   C NE2 1 
ATOM   7890  N  N   . TYR   C 1 313 ? 52.27  66.537  65.98  1   43.33  ? 335 TYR   C N   1 
ATOM   7891  C  CA  . TYR   C 1 313 ? 53.281 67.531  65.656 1   43.45  ? 335 TYR   C CA  1 
ATOM   7892  C  C   . TYR   C 1 313 ? 52.88  68.188  64.315 1   43.49  ? 335 TYR   C C   1 
ATOM   7893  O  O   . TYR   C 1 313 ? 52.907 69.416  64.208 1   43.21  ? 335 TYR   C O   1 
ATOM   7894  C  CB  . TYR   C 1 313 ? 54.691 66.914  65.549 1   43.56  ? 335 TYR   C CB  1 
ATOM   7895  C  CG  . TYR   C 1 313 ? 55.647 67.773  64.742 1   44.66  ? 335 TYR   C CG  1 
ATOM   7896  C  CD1 . TYR   C 1 313 ? 56.143 68.963  65.253 1   45.55  ? 335 TYR   C CD1 1 
ATOM   7897  C  CD2 . TYR   C 1 313 ? 55.957 67.456  63.425 1   45.92  ? 335 TYR   C CD2 1 
ATOM   7898  C  CE1 . TYR   C 1 313 ? 56.981 69.781  64.503 1   46.73  ? 335 TYR   C CE1 1 
ATOM   7899  C  CE2 . TYR   C 1 313 ? 56.769 68.281  62.652 1   46.97  ? 335 TYR   C CE2 1 
ATOM   7900  C  CZ  . TYR   C 1 313 ? 57.305 69.433  63.202 1   48.04  ? 335 TYR   C CZ  1 
ATOM   7901  O  OH  . TYR   C 1 313 ? 58.156 70.24   62.462 1   49.49  ? 335 TYR   C OH  1 
ATOM   7902  N  N   . LEU   C 1 314 ? 52.497 67.369  63.313 1   43.24  ? 336 LEU   C N   1 
ATOM   7903  C  CA  . LEU   C 1 314 ? 52.089 67.871  62.009 1   43.64  ? 336 LEU   C CA  1 
ATOM   7904  C  C   . LEU   C 1 314 ? 50.885 68.8    62.121 1   44.87  ? 336 LEU   C C   1 
ATOM   7905  O  O   . LEU   C 1 314 ? 50.828 69.794  61.389 1   45.4   ? 336 LEU   C O   1 
ATOM   7906  C  CB  . LEU   C 1 314 ? 51.775 66.726  61.037 1   42.99  ? 336 LEU   C CB  1 
ATOM   7907  C  CG  . LEU   C 1 314 ? 52.902 65.79   60.66  1   42.42  ? 336 LEU   C CG  1 
ATOM   7908  C  CD1 . LEU   C 1 314 ? 52.382 64.724  59.726 1   41.8   ? 336 LEU   C CD1 1 
ATOM   7909  C  CD2 . LEU   C 1 314 ? 54.078 66.555  60.047 1   42.58  ? 336 LEU   C CD2 1 
ATOM   7910  N  N   . ARG   C 1 315 ? 49.944 68.503  63.041 1   44.89  ? 337 ARG   C N   1 
ATOM   7911  C  CA  . ARG   C 1 315 ? 48.785 69.36   63.268 1   45.68  ? 337 ARG   C CA  1 
ATOM   7912  C  C   . ARG   C 1 315 ? 49.157 70.676  63.921 1   45.46  ? 337 ARG   C C   1 
ATOM   7913  O  O   . ARG   C 1 315 ? 48.471 71.66   63.706 1   46.18  ? 337 ARG   C O   1 
ATOM   7914  C  CB  . ARG   C 1 315 ? 47.717 68.653  64.09  1   48.39  ? 337 ARG   C CB  1 
ATOM   7915  C  CG  . ARG   C 1 315 ? 46.926 67.67   63.282 1   53.52  ? 337 ARG   C CG  1 
ATOM   7916  C  CD  . ARG   C 1 315 ? 45.818 67.114  64.125 1   59.57  ? 337 ARG   C CD  1 
ATOM   7917  N  NE  . ARG   C 1 315 ? 44.631 67.97   64.155 1   65.81  ? 337 ARG   C NE  1 
ATOM   7918  C  CZ  . ARG   C 1 315 ? 43.948 68.262  65.259 1   69.55  ? 337 ARG   C CZ  1 
ATOM   7919  N  NH1 . ARG   C 1 315 ? 44.348 67.8    66.438 1   69.97  ? 337 ARG   C NH1 1 
ATOM   7920  N  NH2 . ARG   C 1 315 ? 42.866 69.027  65.193 1   69.86  ? 337 ARG   C NH2 1 
ATOM   7921  N  N   . SER   C 1 316 ? 50.238 70.713  64.694 1   45.08  ? 338 SER   C N   1 
ATOM   7922  C  CA  . SER   C 1 316 ? 50.717 71.949  65.306 1   45.82  ? 338 SER   C CA  1 
ATOM   7923  C  C   . SER   C 1 316 ? 51.435 72.876  64.297 1   46.57  ? 338 SER   C C   1 
ATOM   7924  O  O   . SER   C 1 316 ? 51.598 74.067  64.564 1   46.46  ? 338 SER   C O   1 
ATOM   7925  C  CB  . SER   C 1 316 ? 51.611 71.646  66.504 1   46.99  ? 338 SER   C CB  1 
ATOM   7926  O  OG  . SER   C 1 316 ? 52.874 71.135  66.113 1   49.33  ? 338 SER   C OG  1 
ATOM   7927  N  N   . THR   C 1 317 ? 51.879 72.329  63.144 1   47.17  ? 339 THR   C N   1 
ATOM   7928  C  CA  . THR   C 1 317 ? 52.501 73.133  62.09  1   47.74  ? 339 THR   C CA  1 
ATOM   7929  C  C   . THR   C 1 317 ? 51.452 73.939  61.291 1   49.18  ? 339 THR   C C   1 
ATOM   7930  O  O   . THR   C 1 317 ? 51.824 74.82   60.518 1   49.25  ? 339 THR   C O   1 
ATOM   7931  C  CB  . THR   C 1 317 ? 53.415 72.286  61.206 1   47.72  ? 339 THR   C CB  1 
ATOM   7932  O  OG1 . THR   C 1 317 ? 52.615 71.324  60.533 1   48.47  ? 339 THR   C OG1 1 
ATOM   7933  C  CG2 . THR   C 1 317 ? 54.521 71.593  61.994 1   47.43  ? 339 THR   C CG2 1 
ATOM   7934  N  N   . LEU   C 1 318 ? 50.149 73.673  61.506 1   50.34  ? 340 LEU   C N   1 
ATOM   7935  C  CA  . LEU   C 1 318 ? 49.059 74.408  60.861 1   52.28  ? 340 LEU   C CA  1 
ATOM   7936  C  C   . LEU   C 1 318 ? 48.724 75.752  61.565 1   54.09  ? 340 LEU   C C   1 
ATOM   7937  O  O   . LEU   C 1 318 ? 47.938 76.543  61.04  1   53.93  ? 340 LEU   C O   1 
ATOM   7938  C  CB  . LEU   C 1 318 ? 47.806 73.526  60.786 1   52.34  ? 340 LEU   C CB  1 
ATOM   7939  C  CG  . LEU   C 1 318 ? 47.985 72.161  60.137 1   53.61  ? 340 LEU   C CG  1 
ATOM   7940  C  CD1 . LEU   C 1 318 ? 46.694 71.379  60.172 1   54     ? 340 LEU   C CD1 1 
ATOM   7941  C  CD2 . LEU   C 1 318 ? 48.423 72.301  58.712 1   54.45  ? 340 LEU   C CD2 1 
ATOM   7942  N  N   . SER   C 1 319 ? 49.319 75.999  62.746 1   55.68  ? 341 SER   C N   1 
ATOM   7943  C  CA  . SER   C 1 319 ? 49.124 77.214  63.535 1   57.6   ? 341 SER   C CA  1 
ATOM   7944  C  C   . SER   C 1 319 ? 49.82  78.44   62.924 1   59.25  ? 341 SER   C C   1 
ATOM   7945  O  O   . SER   C 1 319 ? 50.747 78.296  62.121 1   59.43  ? 341 SER   C O   1 
ATOM   7946  C  CB  . SER   C 1 319 ? 49.622 76.996  64.964 1   59.09  ? 341 SER   C CB  1 
ATOM   7947  O  OG  . SER   C 1 319 ? 51.037 76.928  65.036 1   61.42  ? 341 SER   C OG  1 
ATOM   7948  N  N   . ASP   C 1 320 ? 49.402 79.65   63.347 1   60.2   ? 342 ASP   C N   1 
ATOM   7949  C  CA  . ASP   C 1 320 ? 50.017 80.896  62.882 1   61.31  ? 342 ASP   C CA  1 
ATOM   7950  C  C   . ASP   C 1 320 ? 51.464 81.091  63.384 1   61.32  ? 342 ASP   C C   1 
ATOM   7951  O  O   . ASP   C 1 320 ? 52.158 81.976  62.896 1   61.47  ? 342 ASP   C O   1 
ATOM   7952  C  CB  . ASP   C 1 320 ? 49.132 82.105  63.2   1   64.25  ? 342 ASP   C CB  1 
ATOM   7953  C  CG  . ASP   C 1 320 ? 47.84  82.162  62.386 1   71.11  ? 342 ASP   C CG  1 
ATOM   7954  O  OD1 . ASP   C 1 320 ? 47.701 81.364  61.422 1   72     ? 342 ASP   C OD1 1 
ATOM   7955  O  OD2 . ASP   C 1 320 ? 46.969 83.008  62.71  1   74.18  ? 342 ASP   C OD2 1 
ATOM   7956  N  N   . ARG   C 1 321 ? 51.945 80.222  64.288 1   61.2   ? 343 ARG   C N   1 
ATOM   7957  C  CA  . ARG   C 1 321 ? 53.346 80.207  64.727 1   61.63  ? 343 ARG   C CA  1 
ATOM   7958  C  C   . ARG   C 1 321 ? 54.271 79.81   63.54  1   61.05  ? 343 ARG   C C   1 
ATOM   7959  O  O   . ARG   C 1 321 ? 55.473 80.074  63.585 1   61.4   ? 343 ARG   C O   1 
ATOM   7960  C  CB  . ARG   C 1 321 ? 53.548 79.182  65.867 1   63.9   ? 343 ARG   C CB  1 
ATOM   7961  C  CG  . ARG   C 1 321 ? 52.516 79.265  66.983 1   68.91  ? 343 ARG   C CG  1 
ATOM   7962  C  CD  . ARG   C 1 321 ? 52.61  78.078  67.925 1   74.12  ? 343 ARG   C CD  1 
ATOM   7963  N  NE  . ARG   C 1 321 ? 53.782 78.163  68.801 1   78.52  ? 343 ARG   C NE  1 
ATOM   7964  C  CZ  . ARG   C 1 321 ? 54.777 77.28   68.816 1   81.6   ? 343 ARG   C CZ  1 
ATOM   7965  N  NH1 . ARG   C 1 321 ? 54.752 76.226  68.009 1   81.44  ? 343 ARG   C NH1 1 
ATOM   7966  N  NH2 . ARG   C 1 321 ? 55.802 77.441  69.643 1   81.8   ? 343 ARG   C NH2 1 
ATOM   7967  N  N   . TYR   C 1 322 ? 53.718 79.143  62.502 1   59.68  ? 344 TYR   C N   1 
ATOM   7968  C  CA  . TYR   C 1 322 ? 54.462 78.71   61.332 1   58.6   ? 344 TYR   C CA  1 
ATOM   7969  C  C   . TYR   C 1 322 ? 54.32  79.667  60.121 1   56.79  ? 344 TYR   C C   1 
ATOM   7970  O  O   . TYR   C 1 322 ? 55.047 79.527  59.144 1   57.34  ? 344 TYR   C O   1 
ATOM   7971  C  CB  . TYR   C 1 322 ? 54.096 77.258  60.99  1   58.82  ? 344 TYR   C CB  1 
ATOM   7972  C  CG  . TYR   C 1 322 ? 54.866 76.262  61.837 1   59.85  ? 344 TYR   C CG  1 
ATOM   7973  C  CD1 . TYR   C 1 322 ? 54.475 75.974  63.137 1   60.99  ? 344 TYR   C CD1 1 
ATOM   7974  C  CD2 . TYR   C 1 322 ? 56.026 75.665  61.361 1   60.62  ? 344 TYR   C CD2 1 
ATOM   7975  C  CE1 . TYR   C 1 322 ? 55.189 75.075  63.922 1   62.01  ? 344 TYR   C CE1 1 
ATOM   7976  C  CE2 . TYR   C 1 322 ? 56.75  74.77   62.136 1   61.62  ? 344 TYR   C CE2 1 
ATOM   7977  C  CZ  . TYR   C 1 322 ? 56.33  74.476  63.417 1   62.97  ? 344 TYR   C CZ  1 
ATOM   7978  O  OH  . TYR   C 1 322 ? 57.051 73.575  64.171 1   64.79  ? 344 TYR   C OH  1 
ATOM   7979  N  N   . LYS   C 1 323 ? 53.42  80.646  60.197 1   54.74  ? 345 LYS   C N   1 
ATOM   7980  C  CA  . LYS   C 1 323 ? 53.258 81.646  59.164 1   53.59  ? 345 LYS   C CA  1 
ATOM   7981  C  C   . LYS   C 1 323 ? 54.362 82.687  59.372 1   52.74  ? 345 LYS   C C   1 
ATOM   7982  O  O   . LYS   C 1 323 ? 54.447 83.283  60.438 1   52.7   ? 345 LYS   C O   1 
ATOM   7983  C  CB  . LYS   C 1 323 ? 51.869 82.297  59.271 1   54.79  ? 345 LYS   C CB  1 
ATOM   7984  C  CG  . LYS   C 1 323 ? 50.774 81.531  58.541 1   58.1   ? 345 LYS   C CG  1 
ATOM   7985  C  CD  . LYS   C 1 323 ? 50.231 82.324  57.365 1   61.82  ? 345 LYS   C CD  1 
ATOM   7986  C  CE  . LYS   C 1 323 ? 49.581 81.457  56.312 1   65.35  ? 345 LYS   C CE  1 
ATOM   7987  N  NZ  . LYS   C 1 323 ? 48.199 81.05   56.683 1   68.21  ? 345 LYS   C NZ  1 
ATOM   7988  N  N   . VAL   C 1 324 ? 55.227 82.867  58.378 1   52.07  ? 346 VAL   C N   1 
ATOM   7989  C  CA  . VAL   C 1 324 ? 56.361 83.793  58.419 1   52.08  ? 346 VAL   C CA  1 
ATOM   7990  C  C   . VAL   C 1 324 ? 55.959 85.274  58.346 1   52.57  ? 346 VAL   C C   1 
ATOM   7991  O  O   . VAL   C 1 324 ? 56.386 86.074  59.17  1   52.7   ? 346 VAL   C O   1 
ATOM   7992  C  CB  . VAL   C 1 324 ? 57.39  83.445  57.31  1   52.01  ? 346 VAL   C CB  1 
ATOM   7993  C  CG1 . VAL   C 1 324 ? 58.583 84.388  57.346 1   52.13  ? 346 VAL   C CG1 1 
ATOM   7994  C  CG2 . VAL   C 1 324 ? 57.835 82      57.413 1   52.19  ? 346 VAL   C CG2 1 
ATOM   7995  N  N   . PHE   C 1 325 ? 55.172 85.648  57.341 1   52.85  ? 347 PHE   C N   1 
ATOM   7996  C  CA  . PHE   C 1 325 ? 54.783 87.029  57.118 1   53.26  ? 347 PHE   C CA  1 
ATOM   7997  C  C   . PHE   C 1 325 ? 53.409 87.298  57.692 1   54.23  ? 347 PHE   C C   1 
ATOM   7998  O  O   . PHE   C 1 325 ? 52.564 87.907  57.044 1   54.78  ? 347 PHE   C O   1 
ATOM   7999  C  CB  . PHE   C 1 325 ? 54.851 87.353  55.622 1   52.82  ? 347 PHE   C CB  1 
ATOM   8000  C  CG  . PHE   C 1 325 ? 56.252 87.26   55.077 1   52.89  ? 347 PHE   C CG  1 
ATOM   8001  C  CD1 . PHE   C 1 325 ? 57.123 88.33   55.18  1   53.62  ? 347 PHE   C CD1 1 
ATOM   8002  C  CD2 . PHE   C 1 325 ? 56.71  86.09   54.501 1   53.2   ? 347 PHE   C CD2 1 
ATOM   8003  C  CE1 . PHE   C 1 325 ? 58.422 88.235  54.698 1   54.34  ? 347 PHE   C CE1 1 
ATOM   8004  C  CE2 . PHE   C 1 325 ? 58.01  85.993  54.035 1   53.93  ? 347 PHE   C CE2 1 
ATOM   8005  C  CZ  . PHE   C 1 325 ? 58.857 87.068  54.128 1   53.92  ? 347 PHE   C CZ  1 
ATOM   8006  N  N   . LEU   C 1 326 ? 53.221 86.867  58.937 1   54.28  ? 348 LEU   C N   1 
ATOM   8007  C  CA  . LEU   C 1 326 ? 52.015 86.971  59.739 1   54.96  ? 348 LEU   C CA  1 
ATOM   8008  C  C   . LEU   C 1 326 ? 51.492 88.414  59.833 1   55.9   ? 348 LEU   C C   1 
ATOM   8009  O  O   . LEU   C 1 326 ? 50.273 88.634  59.859 1   56.77  ? 348 LEU   C O   1 
ATOM   8010  C  CB  . LEU   C 1 326 ? 52.361 86.451  61.14  1   55.13  ? 348 LEU   C CB  1 
ATOM   8011  C  CG  . LEU   C 1 326 ? 51.198 86.123  62.037 1   56.82  ? 348 LEU   C CG  1 
ATOM   8012  C  CD1 . LEU   C 1 326 ? 50.43  84.969  61.481 1   57.45  ? 348 LEU   C CD1 1 
ATOM   8013  C  CD2 . LEU   C 1 326 ? 51.665 85.864  63.484 1   57.56  ? 348 LEU   C CD2 1 
ATOM   8014  N  N   . ASP   C 1 327 ? 52.415 89.394  59.895 1   55.23  ? 349 ASP   C N   1 
ATOM   8015  C  CA  . ASP   C 1 327 ? 52.08  90.813  60.014 1   54.72  ? 349 ASP   C CA  1 
ATOM   8016  C  C   . ASP   C 1 327 ? 51.392 91.358  58.79  1   54.3   ? 349 ASP   C C   1 
ATOM   8017  O  O   . ASP   C 1 327 ? 50.538 92.241  58.917 1   55.4   ? 349 ASP   C O   1 
ATOM   8018  C  CB  . ASP   C 1 327 ? 53.338 91.637  60.255 1   55.98  ? 349 ASP   C CB  1 
ATOM   8019  C  CG  . ASP   C 1 327 ? 54.074 91.249  61.498 1   60.12  ? 349 ASP   C CG  1 
ATOM   8020  O  OD1 . ASP   C 1 327 ? 54.577 90.111  61.554 1   61.05  ? 349 ASP   C OD1 1 
ATOM   8021  O  OD2 . ASP   C 1 327 ? 54.177 92.091  62.411 1   62.22  ? 349 ASP   C OD2 1 
ATOM   8022  N  N   . LEU   C 1 328 ? 51.783 90.866  57.604 1   52.48  ? 350 LEU   C N   1 
ATOM   8023  C  CA  . LEU   C 1 328 ? 51.237 91.314  56.339 1   51.13  ? 350 LEU   C CA  1 
ATOM   8024  C  C   . LEU   C 1 328 ? 49.762 90.988  56.192 1   50.84  ? 350 LEU   C C   1 
ATOM   8025  O  O   . LEU   C 1 328 ? 49.035 91.745  55.561 1   51.21  ? 350 LEU   C O   1 
ATOM   8026  C  CB  . LEU   C 1 328 ? 52.028 90.694  55.18  1   50.48  ? 350 LEU   C CB  1 
ATOM   8027  C  CG  . LEU   C 1 328 ? 53.484 91.083  55.022 1   50.2   ? 350 LEU   C CG  1 
ATOM   8028  C  CD1 . LEU   C 1 328 ? 54.048 90.457  53.789 1   50.14  ? 350 LEU   C CD1 1 
ATOM   8029  C  CD2 . LEU   C 1 328 ? 53.647 92.589  54.942 1   50.49  ? 350 LEU   C CD2 1 
ATOM   8030  N  N   . PHE   C 1 329 ? 49.315 89.869  56.761 1   50.4   ? 351 PHE   C N   1 
ATOM   8031  C  CA  . PHE   C 1 329 ? 47.92  89.445  56.66  1   50.55  ? 351 PHE   C CA  1 
ATOM   8032  C  C   . PHE   C 1 329 ? 46.952 90.368  57.396 1   51.28  ? 351 PHE   C C   1 
ATOM   8033  O  O   . PHE   C 1 329 ? 45.796 90.513  56.984 1   52.13  ? 351 PHE   C O   1 
ATOM   8034  C  CB  . PHE   C 1 329 ? 47.764 88.007  57.171 1   50.01  ? 351 PHE   C CB  1 
ATOM   8035  C  CG  . PHE   C 1 329 ? 48.364 86.969  56.254 1   50.31  ? 351 PHE   C CG  1 
ATOM   8036  C  CD1 . PHE   C 1 329 ? 47.602 86.369  55.265 1   51.1   ? 351 PHE   C CD1 1 
ATOM   8037  C  CD2 . PHE   C 1 329 ? 49.686 86.579  56.391 1   50.67  ? 351 PHE   C CD2 1 
ATOM   8038  C  CE1 . PHE   C 1 329 ? 48.159 85.411  54.416 1   51.68  ? 351 PHE   C CE1 1 
ATOM   8039  C  CE2 . PHE   C 1 329 ? 50.241 85.633  55.537 1   51.33  ? 351 PHE   C CE2 1 
ATOM   8040  C  CZ  . PHE   C 1 329 ? 49.473 85.052  54.558 1   51.28  ? 351 PHE   C CZ  1 
ATOM   8041  N  N   . ASN   C 1 330 ? 47.421 91.015  58.458 1   50.77  ? 352 ASN   C N   1 
ATOM   8042  C  CA  . ASN   C 1 330 ? 46.568 91.867  59.268 1   51.12  ? 352 ASN   C CA  1 
ATOM   8043  C  C   . ASN   C 1 330 ? 46.563 93.36   58.885 1   50.69  ? 352 ASN   C C   1 
ATOM   8044  O  O   . ASN   C 1 330 ? 45.757 94.114  59.434 1   51.17  ? 352 ASN   C O   1 
ATOM   8045  C  CB  . ASN   C 1 330 ? 46.946 91.695  60.739 1   52.65  ? 352 ASN   C CB  1 
ATOM   8046  C  CG  . ASN   C 1 330 ? 45.825 91.984  61.7   1   55.85  ? 352 ASN   C CG  1 
ATOM   8047  O  OD1 . ASN   C 1 330 ? 44.643 91.67   61.452 1   56.38  ? 352 ASN   C OD1 1 
ATOM   8048  N  ND2 . ASN   C 1 330 ? 46.174 92.606  62.816 1   56.88  ? 352 ASN   C ND2 1 
ATOM   8049  N  N   . LEU   C 1 331 ? 47.428 93.789  57.949 1   49.31  ? 353 LEU   C N   1 
ATOM   8050  C  CA  . LEU   C 1 331 ? 47.543 95.199  57.556 1   48.24  ? 353 LEU   C CA  1 
ATOM   8051  C  C   . LEU   C 1 331 ? 46.221 95.924  57.23  1   47.9   ? 353 LEU   C C   1 
ATOM   8052  O  O   . LEU   C 1 331 ? 46.158 97.148  57.361 1   48.08  ? 353 LEU   C O   1 
ATOM   8053  C  CB  . LEU   C 1 331 ? 48.524 95.36   56.394 1   47.64  ? 353 LEU   C CB  1 
ATOM   8054  C  CG  . LEU   C 1 331 ? 49.951 94.941  56.684 1   48.55  ? 353 LEU   C CG  1 
ATOM   8055  C  CD1 . LEU   C 1 331 ? 50.809 95.047  55.455 1   49.23  ? 353 LEU   C CD1 1 
ATOM   8056  C  CD2 . LEU   C 1 331 ? 50.55  95.778  57.771 1   49.15  ? 353 LEU   C CD2 1 
ATOM   8057  N  N   . SER   C 1 332 ? 45.176 95.198  56.826 1   47.45  ? 354 SER   C N   1 
ATOM   8058  C  CA  . SER   C 1 332 ? 43.893 95.832  56.501 1   47.56  ? 354 SER   C CA  1 
ATOM   8059  C  C   . SER   C 1 332 ? 43.108 96.326  57.738 1   47.71  ? 354 SER   C C   1 
ATOM   8060  O  O   . SER   C 1 332 ? 42.171 97.102  57.6   1   47.41  ? 354 SER   C O   1 
ATOM   8061  C  CB  . SER   C 1 332 ? 43.051 94.91   55.633 1   48.43  ? 354 SER   C CB  1 
ATOM   8062  O  OG  . SER   C 1 332 ? 43.685 94.724  54.379 1   50.11  ? 354 SER   C OG  1 
ATOM   8063  N  N   . THR   C 1 333 ? 43.508 95.896  58.94  1   47.98  ? 355 THR   C N   1 
ATOM   8064  C  CA  . THR   C 1 333 ? 42.909 96.321  60.219 1   48.65  ? 355 THR   C CA  1 
ATOM   8065  C  C   . THR   C 1 333 ? 43.146 97.814  60.472 1   48.74  ? 355 THR   C C   1 
ATOM   8066  O  O   . THR   C 1 333 ? 42.34  98.45   61.148 1   48.77  ? 355 THR   C O   1 
ATOM   8067  C  CB  . THR   C 1 333 ? 43.535 95.504  61.374 1   50.15  ? 355 THR   C CB  1 
ATOM   8068  O  OG1 . THR   C 1 333 ? 43.449 94.117  61.058 1   52.01  ? 355 THR   C OG1 1 
ATOM   8069  C  CG2 . THR   C 1 333 ? 42.872 95.745  62.699 1   50.45  ? 355 THR   C CG2 1 
ATOM   8070  N  N   . PHE   C 1 334 ? 44.255 98.365  59.925 1   48.48  ? 356 PHE   C N   1 
ATOM   8071  C  CA  . PHE   C 1 334 ? 44.694 99.747  60.108 1   48.68  ? 356 PHE   C CA  1 
ATOM   8072  C  C   . PHE   C 1 334 ? 44.208 100.723 59.041 1   48.88  ? 356 PHE   C C   1 
ATOM   8073  O  O   . PHE   C 1 334 ? 44.49  101.914 59.139 1   49.53  ? 356 PHE   C O   1 
ATOM   8074  C  CB  . PHE   C 1 334 ? 46.233 99.81   60.209 1   48.59  ? 356 PHE   C CB  1 
ATOM   8075  C  CG  . PHE   C 1 334 ? 46.843 98.719  61.059 1   49.2   ? 356 PHE   C CG  1 
ATOM   8076  C  CD1 . PHE   C 1 334 ? 46.574 98.64   62.409 1   49.94  ? 356 PHE   C CD1 1 
ATOM   8077  C  CD2 . PHE   C 1 334 ? 47.629 97.736  60.492 1   50.09  ? 356 PHE   C CD2 1 
ATOM   8078  C  CE1 . PHE   C 1 334 ? 47.091 97.607  63.178 1   50.73  ? 356 PHE   C CE1 1 
ATOM   8079  C  CE2 . PHE   C 1 334 ? 48.157 96.712  61.267 1   50.74  ? 356 PHE   C CE2 1 
ATOM   8080  C  CZ  . PHE   C 1 334 ? 47.889 96.659  62.605 1   50.6   ? 356 PHE   C CZ  1 
ATOM   8081  N  N   . LEU   C 1 335 ? 43.488 100.239 58.039 1   48.33  ? 357 LEU   C N   1 
ATOM   8082  C  CA  . LEU   C 1 335 ? 43.004 101.043 56.922 1   48.28  ? 357 LEU   C CA  1 
ATOM   8083  C  C   . LEU   C 1 335 ? 41.996 102.138 57.289 1   48.6   ? 357 LEU   C C   1 
ATOM   8084  O  O   . LEU   C 1 335 ? 41.1   101.929 58.115 1   48.82  ? 357 LEU   C O   1 
ATOM   8085  C  CB  . LEU   C 1 335 ? 42.37  100.11  55.891 1   48.04  ? 357 LEU   C CB  1 
ATOM   8086  C  CG  . LEU   C 1 335 ? 42.659 100.423 54.449 1   49.39  ? 357 LEU   C CG  1 
ATOM   8087  C  CD1 . LEU   C 1 335 ? 44.028 99.911  54.054 1   49.93  ? 357 LEU   C CD1 1 
ATOM   8088  C  CD2 . LEU   C 1 335 ? 41.603 99.82   53.562 1   49.97  ? 357 LEU   C CD2 1 
ATOM   8089  N  N   . ILE   C 1 336 ? 42.141 103.298 56.638 1   48.34  ? 358 ILE   C N   1 
ATOM   8090  C  CA  . ILE   C 1 336 ? 41.224 104.436 56.737 1   48.92  ? 358 ILE   C CA  1 
ATOM   8091  C  C   . ILE   C 1 336 ? 40.642 104.694 55.333 1   50.34  ? 358 ILE   C C   1 
ATOM   8092  O  O   . ILE   C 1 336 ? 41.245 104.27  54.344 1   50.54  ? 358 ILE   C O   1 
ATOM   8093  C  CB  . ILE   C 1 336 ? 41.875 105.702 57.354 1   48.84  ? 358 ILE   C CB  1 
ATOM   8094  C  CG1 . ILE   C 1 336 ? 43.29  105.953 56.808 1   49.41  ? 358 ILE   C CG1 1 
ATOM   8095  C  CG2 . ILE   C 1 336 ? 41.852 105.636 58.866 1   49.12  ? 358 ILE   C CG2 1 
ATOM   8096  C  CD1 . ILE   C 1 336 ? 43.915 107.275 57.248 1   50.22  ? 358 ILE   C CD1 1 
ATOM   8097  N  N   . PRO   C 1 337 ? 39.471 105.356 55.194 1   51.16  ? 359 PRO   C N   1 
ATOM   8098  C  CA  . PRO   C 1 337 ? 38.908 105.57  53.84  1   51.9   ? 359 PRO   C CA  1 
ATOM   8099  C  C   . PRO   C 1 337 ? 39.808 106.369 52.892 1   53.25  ? 359 PRO   C C   1 
ATOM   8100  O  O   . PRO   C 1 337 ? 40.723 107.054 53.357 1   53.14  ? 359 PRO   C O   1 
ATOM   8101  C  CB  . PRO   C 1 337 ? 37.581 106.285 54.106 1   52.27  ? 359 PRO   C CB  1 
ATOM   8102  C  CG  . PRO   C 1 337 ? 37.296 106.088 55.557 1   52.44  ? 359 PRO   C CG  1 
ATOM   8103  C  CD  . PRO   C 1 337 ? 38.6   105.919 56.245 1   50.67  ? 359 PRO   C CD  1 
ATOM   8104  N  N   . ARG   C 1 338 ? 39.544 106.305 51.564 1   54.31  ? 360 ARG   C N   1 
ATOM   8105  C  CA  . ARG   C 1 338 ? 40.34  107.01  50.549 1   56.05  ? 360 ARG   C CA  1 
ATOM   8106  C  C   . ARG   C 1 338 ? 40.499 108.493 50.864 1   58.22  ? 360 ARG   C C   1 
ATOM   8107  O  O   . ARG   C 1 338 ? 41.604 109.032 50.8   1   58.83  ? 360 ARG   C O   1 
ATOM   8108  C  CB  . ARG   C 1 338 ? 39.722 106.855 49.144 1   57.26  ? 360 ARG   C CB  1 
ATOM   8109  C  CG  . ARG   C 1 338 ? 39.658 105.426 48.633 1   59.81  ? 360 ARG   C CG  1 
ATOM   8110  C  CD  . ARG   C 1 338 ? 39.385 105.362 47.141 1   60.95  ? 360 ARG   C CD  1 
ATOM   8111  N  NE  . ARG   C 1 338 ? 39.456 103.995 46.618 1   61.5   ? 360 ARG   C NE  1 
ATOM   8112  C  CZ  . ARG   C 1 338 ? 40.581 103.398 46.237 1   63.25  ? 360 ARG   C CZ  1 
ATOM   8113  N  NH1 . ARG   C 1 338 ? 41.744 104.036 46.324 1   62.93  ? 360 ARG   C NH1 1 
ATOM   8114  N  NH2 . ARG   C 1 338 ? 40.556 102.155 45.775 1   63.36  ? 360 ARG   C NH2 1 
ATOM   8115  N  N   . GLU   C 1 339 ? 39.391 109.142 51.233 1   59.3   ? 361 GLU   C N   1 
ATOM   8116  C  CA  . GLU   C 1 339 ? 39.346 110.562 51.553 1   61.06  ? 361 GLU   C CA  1 
ATOM   8117  C  C   . GLU   C 1 339 ? 40.038 110.925 52.878 1   61.92  ? 361 GLU   C C   1 
ATOM   8118  O  O   . GLU   C 1 339 ? 40.344 112.096 53.095 1   62.4   ? 361 GLU   C O   1 
ATOM   8119  C  CB  . GLU   C 1 339 ? 37.892 111.062 51.527 1   64.64  ? 361 GLU   C CB  1 
ATOM   8120  C  CG  . GLU   C 1 339 ? 37.005 110.469 52.61  1   71.96  ? 361 GLU   C CG  1 
ATOM   8121  C  CD  . GLU   C 1 339 ? 36.299 109.153 52.313 1   80     ? 361 GLU   C CD  1 
ATOM   8122  O  OE1 . GLU   C 1 339 ? 36.661 108.473 51.324 1   80.52  ? 361 GLU   C OE1 1 
ATOM   8123  O  OE2 . GLU   C 1 339 ? 35.384 108.794 53.092 1   83.15  ? 361 GLU   C OE2 1 
ATOM   8124  N  N   . ALA   C 1 340 ? 40.299 109.934 53.748 1   61.86  ? 362 ALA   C N   1 
ATOM   8125  C  CA  . ALA   C 1 340 ? 40.987 110.145 55.015 1   62.61  ? 362 ALA   C CA  1 
ATOM   8126  C  C   . ALA   C 1 340 ? 42.508 109.982 54.879 1   63.54  ? 362 ALA   C C   1 
ATOM   8127  O  O   . ALA   C 1 340 ? 43.25  110.563 55.666 1   63.66  ? 362 ALA   C O   1 
ATOM   8128  C  CB  . ALA   C 1 340 ? 40.443 109.204 56.087 1   62.62  ? 362 ALA   C CB  1 
ATOM   8129  N  N   . ILE   C 1 341 ? 42.973 109.194 53.893 1   64.02  ? 363 ILE   C N   1 
ATOM   8130  C  CA  . ILE   C 1 341 ? 44.396 108.958 53.65  1   64.9   ? 363 ILE   C CA  1 
ATOM   8131  C  C   . ILE   C 1 341 ? 45.099 110.23  53.142 1   66.15  ? 363 ILE   C C   1 
ATOM   8132  O  O   . ILE   C 1 341 ? 44.606 110.892 52.223 1   66.1   ? 363 ILE   C O   1 
ATOM   8133  C  CB  . ILE   C 1 341 ? 44.552 107.766 52.662 1   65.37  ? 363 ILE   C CB  1 
ATOM   8134  C  CG1 . ILE   C 1 341 ? 43.975 106.471 53.268 1   66.05  ? 363 ILE   C CG1 1 
ATOM   8135  C  CG2 . ILE   C 1 341 ? 46.001 107.568 52.218 1   65.88  ? 363 ILE   C CG2 1 
ATOM   8136  C  CD1 . ILE   C 1 341 ? 43.968 105.271 52.356 1   66.89  ? 363 ILE   C CD1 1 
ATOM   8137  N  N   . PRO   C 1 342 ? 46.249 110.593 53.744 1   67.27  ? 364 PRO   C N   1 
ATOM   8138  C  CA  . PRO   C 1 342 ? 46.981 111.786 53.281 1   68.37  ? 364 PRO   C CA  1 
ATOM   8139  C  C   . PRO   C 1 342 ? 47.441 111.664 51.831 1   70.41  ? 364 PRO   C C   1 
ATOM   8140  O  O   . PRO   C 1 342 ? 48.028 110.654 51.45  1   70.61  ? 364 PRO   C O   1 
ATOM   8141  C  CB  . PRO   C 1 342 ? 48.173 111.873 54.24  1   68.69  ? 364 PRO   C CB  1 
ATOM   8142  C  CG  . PRO   C 1 342 ? 48.313 110.525 54.832 1   68.77  ? 364 PRO   C CG  1 
ATOM   8143  C  CD  . PRO   C 1 342 ? 46.945 109.918 54.856 1   67.02  ? 364 PRO   C CD  1 
ATOM   8144  N  N   . PRO   C 1 343 ? 47.154 112.678 50.997 1   71.68  ? 365 PRO   C N   1 
ATOM   8145  C  CA  . PRO   C 1 343 ? 47.492 112.573 49.568 1   73.15  ? 365 PRO   C CA  1 
ATOM   8146  C  C   . PRO   C 1 343 ? 48.975 112.633 49.254 1   75.44  ? 365 PRO   C C   1 
ATOM   8147  O  O   . PRO   C 1 343 ? 49.708 113.317 49.956 1   75.61  ? 365 PRO   C O   1 
ATOM   8148  C  CB  . PRO   C 1 343 ? 46.744 113.752 48.934 1   73.47  ? 365 PRO   C CB  1 
ATOM   8149  C  CG  . PRO   C 1 343 ? 45.793 114.25  49.992 1   73.46  ? 365 PRO   C CG  1 
ATOM   8150  C  CD  . PRO   C 1 343 ? 46.429 113.924 51.296 1   71.38  ? 365 PRO   C CD  1 
ATOM   8151  N  N   . LEU   C 1 344 ? 49.414 111.929 48.194 1   77.21  ? 366 LEU   C N   1 
ATOM   8152  C  CA  . LEU   C 1 344 ? 50.819 111.904 47.781 1   79.57  ? 366 LEU   C CA  1 
ATOM   8153  C  C   . LEU   C 1 344 ? 51.252 113.234 47.15  1   82.36  ? 366 LEU   C C   1 
ATOM   8154  O  O   . LEU   C 1 344 ? 50.598 113.712 46.223 1   82.67  ? 366 LEU   C O   1 
ATOM   8155  C  CB  . LEU   C 1 344 ? 51.061 110.746 46.807 1   79.72  ? 366 LEU   C CB  1 
ATOM   8156  C  CG  . LEU   C 1 344 ? 51.249 109.374 47.438 1   81.12  ? 366 LEU   C CG  1 
ATOM   8157  C  CD1 . LEU   C 1 344 ? 51.397 108.315 46.377 1   81.65  ? 366 LEU   C CD1 1 
ATOM   8158  C  CD2 . LEU   C 1 344 ? 52.483 109.342 48.317 1   81.69  ? 366 LEU   C CD2 1 
ATOM   8159  N  N   . ASP   C 1 345 ? 52.338 113.842 47.66  1   84.25  ? 367 ASP   C N   1 
ATOM   8160  C  CA  . ASP   C 1 345 ? 52.812 115.142 47.163 1   86.61  ? 367 ASP   C CA  1 
ATOM   8161  C  C   . ASP   C 1 345 ? 54.121 115.045 46.356 1   88.11  ? 367 ASP   C C   1 
ATOM   8162  O  O   . ASP   C 1 345 ? 54.094 115.235 45.135 1   88.44  ? 367 ASP   C O   1 
ATOM   8163  C  CB  . ASP   C 1 345 ? 52.924 116.173 48.311 1   89.09  ? 367 ASP   C CB  1 
ATOM   8164  C  CG  . ASP   C 1 345 ? 51.591 116.595 48.894 1   94.86  ? 367 ASP   C CG  1 
ATOM   8165  O  OD1 . ASP   C 1 345 ? 50.592 116.627 48.133 1   95.68  ? 367 ASP   C OD1 1 
ATOM   8166  O  OD2 . ASP   C 1 345 ? 51.546 116.903 50.112 1   97.53  ? 367 ASP   C OD2 1 
ATOM   8167  N  N   . GLU   C 1 346 ? 55.249 114.728 47.035 1   88.71  ? 368 GLU   C N   1 
ATOM   8168  C  CA  . GLU   C 1 346 ? 56.582 114.569 46.444 1   89.61  ? 368 GLU   C CA  1 
ATOM   8169  C  C   . GLU   C 1 346 ? 56.99  115.738 45.532 1   89.63  ? 368 GLU   C C   1 
ATOM   8170  O  O   . GLU   C 1 346 ? 58.052 116.33  45.711 1   89.51  ? 368 GLU   C O   1 
ATOM   8171  C  CB  . GLU   C 1 346 ? 56.717 113.209 45.712 1   92.35  ? 368 GLU   C CB  1 
ATOM   8172  C  CG  . GLU   C 1 346 ? 56.065 112.02  46.412 1   96.97  ? 368 GLU   C CG  1 
ATOM   8173  C  CD  . GLU   C 1 346 ? 56.754 111.476 47.652 1   103.03 ? 368 GLU   C CD  1 
ATOM   8174  O  OE1 . GLU   C 1 346 ? 56.263 110.457 48.192 1   104.36 ? 368 GLU   C OE1 1 
ATOM   8175  O  OE2 . GLU   C 1 346 ? 57.78  112.055 48.08  1   104.65 ? 368 GLU   C OE2 1 
ATOM   8176  N  N   . LYS   D 1 3   ? 11.002 76.206  23.836 1   60.06  ? 25  LYS   D N   1 
ATOM   8177  C  CA  . LYS   D 1 3   ? 11.473 77.414  24.523 1   60.67  ? 25  LYS   D CA  1 
ATOM   8178  C  C   . LYS   D 1 3   ? 12.844 77.89   23.998 1   61.05  ? 25  LYS   D C   1 
ATOM   8179  O  O   . LYS   D 1 3   ? 13.761 77.069  23.837 1   61.6   ? 25  LYS   D O   1 
ATOM   8180  C  CB  . LYS   D 1 3   ? 11.562 77.154  26.035 1   62.55  ? 25  LYS   D CB  1 
ATOM   8181  C  CG  . LYS   D 1 3   ? 10.793 78.138  26.913 1   66.28  ? 25  LYS   D CG  1 
ATOM   8182  C  CD  . LYS   D 1 3   ? 10.803 77.674  28.372 1   70.21  ? 25  LYS   D CD  1 
ATOM   8183  C  CE  . LYS   D 1 3   ? 9.971  78.538  29.297 1   73.43  ? 25  LYS   D CE  1 
ATOM   8184  N  NZ  . LYS   D 1 3   ? 10.13  78.124  30.721 1   75.11  ? 25  LYS   D NZ  1 
ATOM   8185  N  N   . ILE   D 1 4   ? 12.992 79.214  23.744 1   60.38  ? 26  ILE   D N   1 
ATOM   8186  C  CA  . ILE   D 1 4   ? 14.281 79.782  23.304 1   60.15  ? 26  ILE   D CA  1 
ATOM   8187  C  C   . ILE   D 1 4   ? 15.263 79.915  24.501 1   59.61  ? 26  ILE   D C   1 
ATOM   8188  O  O   . ILE   D 1 4   ? 14.814 79.98   25.641 1   59.56  ? 26  ILE   D O   1 
ATOM   8189  C  CB  . ILE   D 1 4   ? 14.106 81.123  22.538 1   60.66  ? 26  ILE   D CB  1 
ATOM   8190  C  CG1 . ILE   D 1 4   ? 13.665 82.253  23.47  1   61.67  ? 26  ILE   D CG1 1 
ATOM   8191  C  CG2 . ILE   D 1 4   ? 13.163 80.977  21.364 1   60.92  ? 26  ILE   D CG2 1 
ATOM   8192  C  CD1 . ILE   D 1 4   ? 13.74  83.633  22.864 1   62.62  ? 26  ILE   D CD1 1 
ATOM   8193  N  N   . TYR   D 1 5   ? 16.587 79.94   24.246 1   59     ? 27  TYR   D N   1 
ATOM   8194  C  CA  . TYR   D 1 5   ? 17.655 80.004  25.265 1   58.7   ? 27  TYR   D CA  1 
ATOM   8195  C  C   . TYR   D 1 5   ? 17.384 80.97   26.438 1   58.43  ? 27  TYR   D C   1 
ATOM   8196  O  O   . TYR   D 1 5   ? 17.454 80.558  27.603 1   58.35  ? 27  TYR   D O   1 
ATOM   8197  C  CB  . TYR   D 1 5   ? 19.007 80.326  24.593 1   58.5   ? 27  TYR   D CB  1 
ATOM   8198  C  CG  . TYR   D 1 5   ? 20.222 80.281  25.501 1   58.49  ? 27  TYR   D CG  1 
ATOM   8199  C  CD1 . TYR   D 1 5   ? 20.907 79.092  25.719 1   59.26  ? 27  TYR   D CD1 1 
ATOM   8200  C  CD2 . TYR   D 1 5   ? 20.746 81.444  26.051 1   58.79  ? 27  TYR   D CD2 1 
ATOM   8201  C  CE1 . TYR   D 1 5   ? 22.051 79.053  26.507 1   60.06  ? 27  TYR   D CE1 1 
ATOM   8202  C  CE2 . TYR   D 1 5   ? 21.888 81.417  26.838 1   59.72  ? 27  TYR   D CE2 1 
ATOM   8203  C  CZ  . TYR   D 1 5   ? 22.549 80.222  27.051 1   60.85  ? 27  TYR   D CZ  1 
ATOM   8204  O  OH  . TYR   D 1 5   ? 23.675 80.186  27.836 1   62.3   ? 27  TYR   D OH  1 
ATOM   8205  N  N   . GLY   D 1 6   ? 17.072 82.227  26.121 1   58.02  ? 28  GLY   D N   1 
ATOM   8206  C  CA  . GLY   D 1 6   ? 16.794 83.243  27.127 1   58.08  ? 28  GLY   D CA  1 
ATOM   8207  C  C   . GLY   D 1 6   ? 15.525 82.992  27.913 1   57.94  ? 28  GLY   D C   1 
ATOM   8208  O  O   . GLY   D 1 6   ? 15.447 83.335  29.094 1   58.34  ? 28  GLY   D O   1 
ATOM   8209  N  N   . GLU   D 1 7   ? 14.518 82.391  27.271 1   57.33  ? 29  GLU   D N   1 
ATOM   8210  C  CA  . GLU   D 1 7   ? 13.251 82.085  27.927 1   57.3   ? 29  GLU   D CA  1 
ATOM   8211  C  C   . GLU   D 1 7   ? 13.372 80.835  28.796 1   55.95  ? 29  GLU   D C   1 
ATOM   8212  O  O   . GLU   D 1 7   ? 12.837 80.799  29.905 1   55.54  ? 29  GLU   D O   1 
ATOM   8213  C  CB  . GLU   D 1 7   ? 12.131 81.917  26.899 1   61.11  ? 29  GLU   D CB  1 
ATOM   8214  C  CG  . GLU   D 1 7   ? 11.559 83.237  26.406 1   68.89  ? 29  GLU   D CG  1 
ATOM   8215  C  CD  . GLU   D 1 7   ? 10.727 83.146  25.139 1   76.83  ? 29  GLU   D CD  1 
ATOM   8216  O  OE1 . GLU   D 1 7   ? 10.38  82.013  24.728 1   77.52  ? 29  GLU   D OE1 1 
ATOM   8217  O  OE2 . GLU   D 1 7   ? 10.429 84.212  24.553 1   79.53  ? 29  GLU   D OE2 1 
ATOM   8218  N  N   . TYR   D 1 8   ? 14.107 79.827  28.306 1   54.82  ? 30  TYR   D N   1 
ATOM   8219  C  CA  . TYR   D 1 8   ? 14.329 78.566  29.01  1   54.08  ? 30  TYR   D CA  1 
ATOM   8220  C  C   . TYR   D 1 8   ? 15.095 78.813  30.317 1   53.3   ? 30  TYR   D C   1 
ATOM   8221  O  O   . TYR   D 1 8   ? 14.668 78.377  31.387 1   53.29  ? 30  TYR   D O   1 
ATOM   8222  C  CB  . TYR   D 1 8   ? 15.074 77.568  28.101 1   53.66  ? 30  TYR   D CB  1 
ATOM   8223  C  CG  . TYR   D 1 8   ? 15.458 76.291  28.812 1   54.05  ? 30  TYR   D CG  1 
ATOM   8224  C  CD1 . TYR   D 1 8   ? 14.498 75.363  29.184 1   54.85  ? 30  TYR   D CD1 1 
ATOM   8225  C  CD2 . TYR   D 1 8   ? 16.78  76.026  29.141 1   54.96  ? 30  TYR   D CD2 1 
ATOM   8226  C  CE1 . TYR   D 1 8   ? 14.843 74.195  29.854 1   55.75  ? 30  TYR   D CE1 1 
ATOM   8227  C  CE2 . TYR   D 1 8   ? 17.136 74.865  29.819 1   55.93  ? 30  TYR   D CE2 1 
ATOM   8228  C  CZ  . TYR   D 1 8   ? 16.164 73.95   30.173 1   56.84  ? 30  TYR   D CZ  1 
ATOM   8229  O  OH  . TYR   D 1 8   ? 16.519 72.804  30.841 1   58.54  ? 30  TYR   D OH  1 
ATOM   8230  N  N   . LEU   D 1 9   ? 16.197 79.549  30.226 1   52.54  ? 31  LEU   D N   1 
ATOM   8231  C  CA  . LEU   D 1 9   ? 16.999 79.859  31.392 1   52.37  ? 31  LEU   D CA  1 
ATOM   8232  C  C   . LEU   D 1 9   ? 16.48  81.055  32.198 1   52.92  ? 31  LEU   D C   1 
ATOM   8233  O  O   . LEU   D 1 9   ? 17.088 81.392  33.211 1   53.21  ? 31  LEU   D O   1 
ATOM   8234  C  CB  . LEU   D 1 9   ? 18.456 80.081  30.981 1   51.88  ? 31  LEU   D CB  1 
ATOM   8235  C  CG  . LEU   D 1 9   ? 19.134 78.9    30.334 1   52.11  ? 31  LEU   D CG  1 
ATOM   8236  C  CD1 . LEU   D 1 9   ? 20.483 79.289  29.802 1   52.42  ? 31  LEU   D CD1 1 
ATOM   8237  C  CD2 . LEU   D 1 9   ? 19.235 77.741  31.296 1   52.18  ? 31  LEU   D CD2 1 
ATOM   8238  N  N   . MET   D 1 10  ? 15.394 81.719  31.744 1   52.63  ? 32  MET   D N   1 
ATOM   8239  C  CA  . MET   D 1 10  ? 14.79  82.872  32.407 1   52.82  ? 32  MET   D CA  1 
ATOM   8240  C  C   . MET   D 1 10  ? 15.805 83.947  32.707 1   53.14  ? 32  MET   D C   1 
ATOM   8241  O  O   . MET   D 1 10  ? 15.909 84.435  33.833 1   53.29  ? 32  MET   D O   1 
ATOM   8242  C  CB  . MET   D 1 10  ? 13.986 82.457  33.647 1   53.09  ? 32  MET   D CB  1 
ATOM   8243  C  CG  . MET   D 1 10  ? 12.82  81.569  33.288 1   54.42  ? 32  MET   D CG  1 
ATOM   8244  S  SD  . MET   D 1 10  ? 11.928 80.893  34.693 1   56.2   ? 32  MET   D SD  1 
ATOM   8245  C  CE  . MET   D 1 10  ? 11.3   82.373  35.41  1   53.19  ? 32  MET   D CE  1 
ATOM   8246  N  N   . LEU   D 1 11  ? 16.584 84.285  31.682 1   52.99  ? 33  LEU   D N   1 
ATOM   8247  C  CA  . LEU   D 1 11  ? 17.618 85.298  31.779 1   53.23  ? 33  LEU   D CA  1 
ATOM   8248  C  C   . LEU   D 1 11  ? 17.041 86.709  31.977 1   53.66  ? 33  LEU   D C   1 
ATOM   8249  O  O   . LEU   D 1 11  ? 17.747 87.58   32.46  1   53.72  ? 33  LEU   D O   1 
ATOM   8250  C  CB  . LEU   D 1 11  ? 18.552 85.207  30.566 1   53.3   ? 33  LEU   D CB  1 
ATOM   8251  C  CG  . LEU   D 1 11  ? 19.176 83.816  30.343 1   54.72  ? 33  LEU   D CG  1 
ATOM   8252  C  CD1 . LEU   D 1 11  ? 19.982 83.768  29.076 1   54.97  ? 33  LEU   D CD1 1 
ATOM   8253  C  CD2 . LEU   D 1 11  ? 20.04  83.404  31.515 1   55.35  ? 33  LEU   D CD2 1 
ATOM   8254  N  N   . ASP   D 1 12  ? 15.754 86.931  31.652 1   53.84  ? 34  ASP   D N   1 
ATOM   8255  C  CA  . ASP   D 1 12  ? 15.09  88.223  31.892 1   54.6   ? 34  ASP   D CA  1 
ATOM   8256  C  C   . ASP   D 1 12  ? 14.877 88.478  33.408 1   53.96  ? 34  ASP   D C   1 
ATOM   8257  O  O   . ASP   D 1 12  ? 14.766 89.631  33.836 1   53.88  ? 34  ASP   D O   1 
ATOM   8258  C  CB  . ASP   D 1 12  ? 13.746 88.295  31.145 1   57.81  ? 34  ASP   D CB  1 
ATOM   8259  C  CG  . ASP   D 1 12  ? 13.885 88.304  29.631 1   66.59  ? 34  ASP   D CG  1 
ATOM   8260  O  OD1 . ASP   D 1 12  ? 14.806 88.989  29.12  1   68.17  ? 34  ASP   D OD1 1 
ATOM   8261  O  OD2 . ASP   D 1 12  ? 13.074 87.622  28.951 1   70.49  ? 34  ASP   D OD2 1 
ATOM   8262  N  N   . LYS   D 1 13  ? 14.835 87.389  34.202 1   53.01  ? 35  LYS   D N   1 
ATOM   8263  C  CA  . LYS   D 1 13  ? 14.675 87.393  35.638 1   52.52  ? 35  LYS   D CA  1 
ATOM   8264  C  C   . LYS   D 1 13  ? 16.066 87.302  36.281 1   51.41  ? 35  LYS   D C   1 
ATOM   8265  O  O   . LYS   D 1 13  ? 16.377 88.096  37.165 1   51.72  ? 35  LYS   D O   1 
ATOM   8266  C  CB  . LYS   D 1 13  ? 13.799 86.191  36.043 1   54.9   ? 35  LYS   D CB  1 
ATOM   8267  C  CG  . LYS   D 1 13  ? 13.308 86.213  37.487 1   60.17  ? 35  LYS   D CG  1 
ATOM   8268  C  CD  . LYS   D 1 13  ? 12.298 85.102  37.748 1   66.47  ? 35  LYS   D CD  1 
ATOM   8269  C  CE  . LYS   D 1 13  ? 10.899 85.452  37.282 1   71.6   ? 35  LYS   D CE  1 
ATOM   8270  N  NZ  . LYS   D 1 13  ? 9.946  84.318  37.471 1   74.82  ? 35  LYS   D NZ  1 
ATOM   8271  N  N   . LEU   D 1 14  ? 16.913 86.353  35.816 1   50.14  ? 36  LEU   D N   1 
ATOM   8272  C  CA  . LEU   D 1 14  ? 18.266 86.12   36.344 1   49.33  ? 36  LEU   D CA  1 
ATOM   8273  C  C   . LEU   D 1 14  ? 19.195 87.307  36.129 1   48.94  ? 36  LEU   D C   1 
ATOM   8274  O  O   . LEU   D 1 14  ? 19.829 87.773  37.078 1   49.08  ? 36  LEU   D O   1 
ATOM   8275  C  CB  . LEU   D 1 14  ? 18.873 84.858  35.724 1   49.26  ? 36  LEU   D CB  1 
ATOM   8276  C  CG  . LEU   D 1 14  ? 20.223 84.452  36.279 1   50.54  ? 36  LEU   D CG  1 
ATOM   8277  C  CD1 . LEU   D 1 14  ? 20.058 83.424  37.368 1   51.15  ? 36  LEU   D CD1 1 
ATOM   8278  C  CD2 . LEU   D 1 14  ? 21.117 83.912  35.181 1   51.12  ? 36  LEU   D CD2 1 
ATOM   8279  N  N   . LEU   D 1 15  ? 19.258 87.818  34.892 1   48.4   ? 37  LEU   D N   1 
ATOM   8280  C  CA  . LEU   D 1 15  ? 20.103 88.967  34.569 1   48.34  ? 37  LEU   D CA  1 
ATOM   8281  C  C   . LEU   D 1 15  ? 19.468 90.318  34.94  1   48.62  ? 37  LEU   D C   1 
ATOM   8282  O  O   . LEU   D 1 15  ? 19.947 91.367  34.516 1   49.16  ? 37  LEU   D O   1 
ATOM   8283  C  CB  . LEU   D 1 15  ? 20.565 88.94   33.094 1   47.93  ? 37  LEU   D CB  1 
ATOM   8284  C  CG  . LEU   D 1 15  ? 21.79  88.067  32.67  1   47.82  ? 37  LEU   D CG  1 
ATOM   8285  C  CD1 . LEU   D 1 15  ? 22.432 87.257  33.828 1   47.86  ? 37  LEU   D CD1 1 
ATOM   8286  C  CD2 . LEU   D 1 15  ? 21.444 87.19   31.504 1   47.64  ? 37  LEU   D CD2 1 
ATOM   8287  N  N   . ASP   D 1 16  ? 18.446 90.295  35.792 1   48.24  ? 38  ASP   D N   1 
ATOM   8288  C  CA  . ASP   D 1 16  ? 17.829 91.498  36.31  1   48.56  ? 38  ASP   D CA  1 
ATOM   8289  C  C   . ASP   D 1 16  ? 17.954 91.597  37.872 1   48.39  ? 38  ASP   D C   1 
ATOM   8290  O  O   . ASP   D 1 16  ? 17.465 92.551  38.479 1   48.57  ? 38  ASP   D O   1 
ATOM   8291  C  CB  . ASP   D 1 16  ? 16.38  91.586  35.851 1   50.58  ? 38  ASP   D CB  1 
ATOM   8292  C  CG  . ASP   D 1 16  ? 15.782 92.9    36.262 1   55.73  ? 38  ASP   D CG  1 
ATOM   8293  O  OD1 . ASP   D 1 16  ? 16.177 93.934  35.677 1   57.53  ? 38  ASP   D OD1 1 
ATOM   8294  O  OD2 . ASP   D 1 16  ? 15.029 92.915  37.261 1   56.81  ? 38  ASP   D OD2 1 
ATOM   8295  N  N   . ALA   D 1 17  ? 18.629 90.634  38.511 1   47.92  ? 39  ALA   D N   1 
ATOM   8296  C  CA  . ALA   D 1 17  ? 18.842 90.635  39.952 1   48.3   ? 39  ALA   D CA  1 
ATOM   8297  C  C   . ALA   D 1 17  ? 20.118 91.379  40.372 1   49.16  ? 39  ALA   D C   1 
ATOM   8298  O  O   . ALA   D 1 17  ? 20.544 91.244  41.518 1   49.44  ? 39  ALA   D O   1 
ATOM   8299  C  CB  . ALA   D 1 17  ? 18.89  89.208  40.463 1   48.33  ? 39  ALA   D CB  1 
ATOM   8300  N  N   . GLN   D 1 18  ? 20.727 92.168  39.469 1   49.38  ? 40  GLN   D N   1 
ATOM   8301  C  CA  . GLN   D 1 18  ? 21.954 92.879  39.792 1   49.98  ? 40  GLN   D CA  1 
ATOM   8302  C  C   . GLN   D 1 18  ? 21.716 94.362  39.973 1   51.32  ? 40  GLN   D C   1 
ATOM   8303  O  O   . GLN   D 1 18  ? 21.502 95.09   39     1   51.73  ? 40  GLN   D O   1 
ATOM   8304  C  CB  . GLN   D 1 18  ? 23.061 92.603  38.758 1   49.83  ? 40  GLN   D CB  1 
ATOM   8305  C  CG  . GLN   D 1 18  ? 23.451 91.131  38.69  1   50.29  ? 40  GLN   D CG  1 
ATOM   8306  C  CD  . GLN   D 1 18  ? 22.472 90.348  37.865 1   52.94  ? 40  GLN   D CD  1 
ATOM   8307  O  OE1 . GLN   D 1 18  ? 21.939 90.846  36.881 1   54.71  ? 40  GLN   D OE1 1 
ATOM   8308  N  NE2 . GLN   D 1 18  ? 22.193 89.114  38.245 1   52.77  ? 40  GLN   D NE2 1 
ATOM   8309  N  N   . CYS   D 1 19  ? 21.777 94.811  41.218 1   51.68  ? 41  CYS   D N   1 
ATOM   8310  C  CA  . CYS   D 1 19  ? 21.567 96.211  41.518 1   52.86  ? 41  CYS   D CA  1 
ATOM   8311  C  C   . CYS   D 1 19  ? 22.626 96.748  42.476 1   53.68  ? 41  CYS   D C   1 
ATOM   8312  O  O   . CYS   D 1 19  ? 22.613 96.466  43.68  1   53.69  ? 41  CYS   D O   1 
ATOM   8313  C  CB  . CYS   D 1 19  ? 20.15  96.446  42.038 1   54.12  ? 41  CYS   D CB  1 
ATOM   8314  S  SG  . CYS   D 1 19  ? 19.804 98.158  42.529 1   58.15  ? 41  CYS   D SG  1 
ATOM   8315  N  N   . MET   D 1 20  ? 23.523 97.56   41.936 1   54.15  ? 42  MET   D N   1 
ATOM   8316  C  CA  . MET   D 1 20  ? 24.57  98.191  42.716 1   55.28  ? 42  MET   D CA  1 
ATOM   8317  C  C   . MET   D 1 20  ? 23.996 99.368  43.485 1   57.08  ? 42  MET   D C   1 
ATOM   8318  O  O   . MET   D 1 20  ? 23.493 100.311 42.874 1   57.81  ? 42  MET   D O   1 
ATOM   8319  C  CB  . MET   D 1 20  ? 25.682 98.696  41.785 1   55.38  ? 42  MET   D CB  1 
ATOM   8320  C  CG  . MET   D 1 20  ? 26.515 97.583  41.188 1   56.39  ? 42  MET   D CG  1 
ATOM   8321  S  SD  . MET   D 1 20  ? 27.492 98.091  39.745 1   55.85  ? 42  MET   D SD  1 
ATOM   8322  C  CE  . MET   D 1 20  ? 28.405 99.461  40.435 1   49.32  ? 42  MET   D CE  1 
ATOM   8323  N  N   . LEU   D 1 21  ? 24.085 99.332  44.818 1   57.7   ? 43  LEU   D N   1 
ATOM   8324  C  CA  . LEU   D 1 21  ? 23.615 100.423 45.663 1   58.66  ? 43  LEU   D CA  1 
ATOM   8325  C  C   . LEU   D 1 21  ? 24.542 101.642 45.643 1   60.81  ? 43  LEU   D C   1 
ATOM   8326  O  O   . LEU   D 1 21  ? 24.105 102.736 45.979 1   61.01  ? 43  LEU   D O   1 
ATOM   8327  C  CB  . LEU   D 1 21  ? 23.36  99.935  47.086 1   58.12  ? 43  LEU   D CB  1 
ATOM   8328  C  CG  . LEU   D 1 21  ? 22.425 98.74   47.199 1   59.03  ? 43  LEU   D CG  1 
ATOM   8329  C  CD1 . LEU   D 1 21  ? 22.254 98.325  48.618 1   59.33  ? 43  LEU   D CD1 1 
ATOM   8330  C  CD2 . LEU   D 1 21  ? 21.072 99.037  46.6   1   59.77  ? 43  LEU   D CD2 1 
ATOM   8331  N  N   . SER   D 1 22  ? 25.806 101.472 45.232 1   62.45  ? 44  SER   D N   1 
ATOM   8332  C  CA  . SER   D 1 22  ? 26.73  102.598 45.093 1   64.25  ? 44  SER   D CA  1 
ATOM   8333  C  C   . SER   D 1 22  ? 26.344 103.406 43.841 1   66.75  ? 44  SER   D C   1 
ATOM   8334  O  O   . SER   D 1 22  ? 26.355 104.628 43.874 1   66.79  ? 44  SER   D O   1 
ATOM   8335  C  CB  . SER   D 1 22  ? 28.17  102.105 44.987 1   64.62  ? 44  SER   D CB  1 
ATOM   8336  O  OG  . SER   D 1 22  ? 28.37  101.338 43.813 1   65.66  ? 44  SER   D OG  1 
ATOM   8337  N  N   . GLU   D 1 23  ? 25.961 102.721 42.754 1   68.81  ? 45  GLU   D N   1 
ATOM   8338  C  CA  . GLU   D 1 23  ? 25.515 103.353 41.511 1   71.26  ? 45  GLU   D CA  1 
ATOM   8339  C  C   . GLU   D 1 23  ? 24.172 104.082 41.741 1   73.44  ? 45  GLU   D C   1 
ATOM   8340  O  O   . GLU   D 1 23  ? 23.968 105.178 41.209 1   73.72  ? 45  GLU   D O   1 
ATOM   8341  C  CB  . GLU   D 1 23  ? 25.352 102.278 40.433 1   73.89  ? 45  GLU   D CB  1 
ATOM   8342  C  CG  . GLU   D 1 23  ? 25.108 102.815 39.039 1   79.66  ? 45  GLU   D CG  1 
ATOM   8343  C  CD  . GLU   D 1 23  ? 24.893 101.718 38.014 1   87.85  ? 45  GLU   D CD  1 
ATOM   8344  O  OE1 . GLU   D 1 23  ? 24.259 100.693 38.36  1   89.63  ? 45  GLU   D OE1 1 
ATOM   8345  O  OE2 . GLU   D 1 23  ? 25.363 101.88  36.864 1   90.44  ? 45  GLU   D OE2 1 
ATOM   8346  N  N   . GLU   D 1 24  ? 23.278 103.475 42.563 1   74.7   ? 46  GLU   D N   1 
ATOM   8347  C  CA  . GLU   D 1 24  ? 21.964 103.996 42.976 1   76.24  ? 46  GLU   D CA  1 
ATOM   8348  C  C   . GLU   D 1 24  ? 22.144 105.316 43.741 1   76.87  ? 46  GLU   D C   1 
ATOM   8349  O  O   . GLU   D 1 24  ? 21.406 106.274 43.507 1   77.12  ? 46  GLU   D O   1 
ATOM   8350  C  CB  . GLU   D 1 24  ? 21.241 102.94  43.861 1   79.57  ? 46  GLU   D CB  1 
ATOM   8351  C  CG  . GLU   D 1 24  ? 20.077 103.439 44.715 1   85.91  ? 46  GLU   D CG  1 
ATOM   8352  C  CD  . GLU   D 1 24  ? 20.365 103.644 46.197 1   94.27  ? 46  GLU   D CD  1 
ATOM   8353  O  OE1 . GLU   D 1 24  ? 21.335 103.04  46.713 1   94.75  ? 46  GLU   D OE1 1 
ATOM   8354  O  OE2 . GLU   D 1 24  ? 19.632 104.433 46.838 1   97.91  ? 46  GLU   D OE2 1 
ATOM   8355  N  N   . ASP   D 1 25  ? 23.15  105.366 44.632 1   76.92  ? 47  ASP   D N   1 
ATOM   8356  C  CA  . ASP   D 1 25  ? 23.448 106.554 45.431 1   77.6   ? 47  ASP   D CA  1 
ATOM   8357  C  C   . ASP   D 1 25  ? 24.339 107.585 44.699 1   77.95  ? 47  ASP   D C   1 
ATOM   8358  O  O   . ASP   D 1 25  ? 24.822 108.532 45.333 1   78.45  ? 47  ASP   D O   1 
ATOM   8359  C  CB  . ASP   D 1 25  ? 24.105 106.135 46.75  1   79.4   ? 47  ASP   D CB  1 
ATOM   8360  C  CG  . ASP   D 1 25  ? 23.626 106.923 47.942 1   83.71  ? 47  ASP   D CG  1 
ATOM   8361  O  OD1 . ASP   D 1 25  ? 22.396 106.975 48.162 1   84.3   ? 47  ASP   D OD1 1 
ATOM   8362  O  OD2 . ASP   D 1 25  ? 24.48  107.477 48.665 1   85.78  ? 47  ASP   D OD2 1 
ATOM   8363  N  N   . LYS   D 1 26  ? 24.555 107.389 43.377 1   77.32  ? 48  LYS   D N   1 
ATOM   8364  C  CA  . LYS   D 1 26  ? 25.358 108.202 42.468 1   77.04  ? 48  LYS   D CA  1 
ATOM   8365  C  C   . LYS   D 1 26  ? 26.82  108.351 42.898 1   76.21  ? 48  LYS   D C   1 
ATOM   8366  O  O   . LYS   D 1 26  ? 27.482 109.32  42.532 1   76.34  ? 48  LYS   D O   1 
ATOM   8367  C  CB  . LYS   D 1 26  ? 24.706 109.562 42.197 1   79.25  ? 48  LYS   D CB  1 
ATOM   8368  C  CG  . LYS   D 1 26  ? 23.413 109.45  41.395 1   83.91  ? 48  LYS   D CG  1 
ATOM   8369  C  CD  . LYS   D 1 26  ? 23.641 108.878 40.003 1   88.48  ? 48  LYS   D CD  1 
ATOM   8370  C  CE  . LYS   D 1 26  ? 22.341 108.585 39.303 1   92.77  ? 48  LYS   D CE  1 
ATOM   8371  N  NZ  . LYS   D 1 26  ? 22.563 108.259 37.868 1   95.71  ? 48  LYS   D NZ  1 
ATOM   8372  N  N   . ARG   D 1 27  ? 27.332 107.356 43.628 1   75.2   ? 49  ARG   D N   1 
ATOM   8373  C  CA  . ARG   D 1 27  ? 28.725 107.264 44.061 1   74.77  ? 49  ARG   D CA  1 
ATOM   8374  C  C   . ARG   D 1 27  ? 29.164 105.825 43.689 1   72.64  ? 49  ARG   D C   1 
ATOM   8375  O  O   . ARG   D 1 27  ? 29.277 104.975 44.58  1   73.02  ? 49  ARG   D O   1 
ATOM   8376  C  CB  . ARG   D 1 27  ? 28.808 107.472 45.585 1   77.61  ? 49  ARG   D CB  1 
ATOM   8377  C  CG  . ARG   D 1 27  ? 28.458 108.878 46.064 1   83.59  ? 49  ARG   D CG  1 
ATOM   8378  C  CD  . ARG   D 1 27  ? 28.191 108.937 47.57  1   89.56  ? 49  ARG   D CD  1 
ATOM   8379  N  NE  . ARG   D 1 27  ? 29.278 108.364 48.372 1   94.85  ? 49  ARG   D NE  1 
ATOM   8380  C  CZ  . ARG   D 1 27  ? 29.183 107.237 49.073 1   98.76  ? 49  ARG   D CZ  1 
ATOM   8381  N  NH1 . ARG   D 1 27  ? 28.047 106.552 49.092 1   98.72  ? 49  ARG   D NH1 1 
ATOM   8382  N  NH2 . ARG   D 1 27  ? 30.229 106.78  49.753 1   99.32  ? 49  ARG   D NH2 1 
ATOM   8383  N  N   . PRO   D 1 28  ? 29.306 105.484 42.38  1   69.86  ? 50  PRO   D N   1 
ATOM   8384  C  CA  . PRO   D 1 28  ? 29.55  104.078 42.026 1   67.46  ? 50  PRO   D CA  1 
ATOM   8385  C  C   . PRO   D 1 28  ? 30.965 103.566 42.259 1   64.16  ? 50  PRO   D C   1 
ATOM   8386  O  O   . PRO   D 1 28  ? 31.943 104.303 42.138 1   64.36  ? 50  PRO   D O   1 
ATOM   8387  C  CB  . PRO   D 1 28  ? 29.127 103.992 40.561 1   68.54  ? 50  PRO   D CB  1 
ATOM   8388  C  CG  . PRO   D 1 28  ? 29.273 105.362 40.041 1   69.56  ? 50  PRO   D CG  1 
ATOM   8389  C  CD  . PRO   D 1 28  ? 29.167 106.33  41.177 1   68.82  ? 50  PRO   D CD  1 
ATOM   8390  N  N   . VAL   D 1 29  ? 31.038 102.285 42.654 1   61.03  ? 51  VAL   D N   1 
ATOM   8391  C  CA  . VAL   D 1 29  ? 32.257 101.52  42.908 1   58.32  ? 51  VAL   D CA  1 
ATOM   8392  C  C   . VAL   D 1 29  ? 32.191 100.339 41.947 1   55.37  ? 51  VAL   D C   1 
ATOM   8393  O  O   . VAL   D 1 29  ? 31.335 99.476  42.128 1   55.32  ? 51  VAL   D O   1 
ATOM   8394  C  CB  . VAL   D 1 29  ? 32.324 101.011 44.371 1   58.7   ? 51  VAL   D CB  1 
ATOM   8395  C  CG1 . VAL   D 1 29  ? 33.613 100.255 44.62  1   58.99  ? 51  VAL   D CG1 1 
ATOM   8396  C  CG2 . VAL   D 1 29  ? 32.175 102.153 45.361 1   59.18  ? 51  VAL   D CG2 1 
ATOM   8397  N  N   . HIS   D 1 30  ? 33.058 100.319 40.91  1   52.66  ? 52  HIS   D N   1 
ATOM   8398  C  CA  . HIS   D 1 30  ? 33.098 99.276  39.88  1   50.57  ? 52  HIS   D CA  1 
ATOM   8399  C  C   . HIS   D 1 30  ? 33.123 97.834  40.421 1   49.14  ? 52  HIS   D C   1 
ATOM   8400  O  O   . HIS   D 1 30  ? 32.437 96.962  39.887 1   49.11  ? 52  HIS   D O   1 
ATOM   8401  C  CB  . HIS   D 1 30  ? 34.301 99.504  38.95  1   50.31  ? 52  HIS   D CB  1 
ATOM   8402  C  CG  . HIS   D 1 30  ? 34.375 98.538  37.804 1   49.88  ? 52  HIS   D CG  1 
ATOM   8403  N  ND1 . HIS   D 1 30  ? 35.154 97.401  37.87  1   51.06  ? 52  HIS   D ND1 1 
ATOM   8404  C  CD2 . HIS   D 1 30  ? 33.779 98.585  36.593 1   50.13  ? 52  HIS   D CD2 1 
ATOM   8405  C  CE1 . HIS   D 1 30  ? 34.995 96.787  36.713 1   51.02  ? 52  HIS   D CE1 1 
ATOM   8406  N  NE2 . HIS   D 1 30  ? 34.161 97.449  35.921 1   50.92  ? 52  HIS   D NE2 1 
ATOM   8407  N  N   . ASP   D 1 31  ? 33.89  97.59   41.493 1   47.86  ? 53  ASP   D N   1 
ATOM   8408  C  CA  . ASP   D 1 31  ? 34.01  96.252  42.057 1   46.77  ? 53  ASP   D CA  1 
ATOM   8409  C  C   . ASP   D 1 31  ? 32.747 95.757  42.783 1   45.86  ? 53  ASP   D C   1 
ATOM   8410  O  O   . ASP   D 1 31  ? 32.709 94.589  43.171 1   46.26  ? 53  ASP   D O   1 
ATOM   8411  C  CB  . ASP   D 1 31  ? 35.261 96.135  42.945 1   47.39  ? 53  ASP   D CB  1 
ATOM   8412  C  CG  . ASP   D 1 31  ? 36.582 96.19   42.189 1   50.59  ? 53  ASP   D CG  1 
ATOM   8413  O  OD1 . ASP   D 1 31  ? 36.551 96.251  40.943 1   52.17  ? 53  ASP   D OD1 1 
ATOM   8414  O  OD2 . ASP   D 1 31  ? 37.652 96.169  42.846 1   51.57  ? 53  ASP   D OD2 1 
ATOM   8415  N  N   . GLU   D 1 32  ? 31.697 96.594  42.916 1   44.58  ? 54  GLU   D N   1 
ATOM   8416  C  CA  . GLU   D 1 32  ? 30.449 96.138  43.541 1   43.85  ? 54  GLU   D CA  1 
ATOM   8417  C  C   . GLU   D 1 32  ? 29.704 95.125  42.656 1   42.44  ? 54  GLU   D C   1 
ATOM   8418  O  O   . GLU   D 1 32  ? 29.031 94.229  43.159 1   42.64  ? 54  GLU   D O   1 
ATOM   8419  C  CB  . GLU   D 1 32  ? 29.529 97.313  43.918 1   46.28  ? 54  GLU   D CB  1 
ATOM   8420  C  CG  . GLU   D 1 32  ? 28.329 96.845  44.719 1   49.01  ? 54  GLU   D CG  1 
ATOM   8421  C  CD  . GLU   D 1 32  ? 27.338 97.899  45.158 1   51.99  ? 54  GLU   D CD  1 
ATOM   8422  O  OE1 . GLU   D 1 32  ? 27.539 99.088  44.826 1   52.86  ? 54  GLU   D OE1 1 
ATOM   8423  O  OE2 . GLU   D 1 32  ? 26.338 97.529  45.816 1   51.68  ? 54  GLU   D OE2 1 
ATOM   8424  N  N   . HIS   D 1 33  ? 29.855 95.244  41.337 1   41.22  ? 55  HIS   D N   1 
ATOM   8425  C  CA  . HIS   D 1 33  ? 29.262 94.317  40.384 1   40.49  ? 55  HIS   D CA  1 
ATOM   8426  C  C   . HIS   D 1 33  ? 29.859 92.911  40.607 1   40.02  ? 55  HIS   D C   1 
ATOM   8427  O  O   . HIS   D 1 33  ? 29.131 91.91   40.58  1   39.97  ? 55  HIS   D O   1 
ATOM   8428  C  CB  . HIS   D 1 33  ? 29.577 94.797  38.958 1   40.73  ? 55  HIS   D CB  1 
ATOM   8429  C  CG  . HIS   D 1 33  ? 28.694 94.22   37.893 1   42.17  ? 55  HIS   D CG  1 
ATOM   8430  N  ND1 . HIS   D 1 33  ? 28.754 92.883  37.545 1   43.77  ? 55  HIS   D ND1 1 
ATOM   8431  C  CD2 . HIS   D 1 33  ? 27.782 94.831  37.105 1   42.97  ? 55  HIS   D CD2 1 
ATOM   8432  C  CE1 . HIS   D 1 33  ? 27.863 92.717  36.58  1   43.85  ? 55  HIS   D CE1 1 
ATOM   8433  N  NE2 . HIS   D 1 33  ? 27.264 93.862  36.272 1   43.85  ? 55  HIS   D NE2 1 
ATOM   8434  N  N   . LEU   D 1 34  ? 31.192 92.849  40.821 1   39.1   ? 56  LEU   D N   1 
ATOM   8435  C  CA  . LEU   D 1 34  ? 31.916 91.606  41.046 1   38.55  ? 56  LEU   D CA  1 
ATOM   8436  C  C   . LEU   D 1 34  ? 31.436 90.973  42.332 1   38.6   ? 56  LEU   D C   1 
ATOM   8437  O  O   . LEU   D 1 34  ? 31.18  89.772  42.361 1   39.46  ? 56  LEU   D O   1 
ATOM   8438  C  CB  . LEU   D 1 34  ? 33.433 91.859  41.08  1   38.31  ? 56  LEU   D CB  1 
ATOM   8439  C  CG  . LEU   D 1 34  ? 34.298 90.638  41.35  1   39     ? 56  LEU   D CG  1 
ATOM   8440  C  CD1 . LEU   D 1 34  ? 34.182 89.634  40.227 1   39.06  ? 56  LEU   D CD1 1 
ATOM   8441  C  CD2 . LEU   D 1 34  ? 35.73  91.027  41.605 1   39.4   ? 56  LEU   D CD2 1 
ATOM   8442  N  N   . PHE   D 1 35  ? 31.276 91.784  43.385 1   37.87  ? 57  PHE   D N   1 
ATOM   8443  C  CA  . PHE   D 1 35  ? 30.773 91.362  44.688 1   37.57  ? 57  PHE   D CA  1 
ATOM   8444  C  C   . PHE   D 1 35  ? 29.401 90.686  44.555 1   36.79  ? 57  PHE   D C   1 
ATOM   8445  O  O   . PHE   D 1 35  ? 29.204 89.613  45.108 1   36.81  ? 57  PHE   D O   1 
ATOM   8446  C  CB  . PHE   D 1 35  ? 30.705 92.582  45.634 1   37.63  ? 57  PHE   D CB  1 
ATOM   8447  C  CG  . PHE   D 1 35  ? 30.421 92.242  47.08  1   38.53  ? 57  PHE   D CG  1 
ATOM   8448  C  CD1 . PHE   D 1 35  ? 31.42  91.746  47.904 1   39.51  ? 57  PHE   D CD1 1 
ATOM   8449  C  CD2 . PHE   D 1 35  ? 29.155 92.418  47.615 1   39.08  ? 57  PHE   D CD2 1 
ATOM   8450  C  CE1 . PHE   D 1 35  ? 31.149 91.414  49.227 1   40.38  ? 57  PHE   D CE1 1 
ATOM   8451  C  CE2 . PHE   D 1 35  ? 28.886 92.087  48.935 1   39.88  ? 57  PHE   D CE2 1 
ATOM   8452  C  CZ  . PHE   D 1 35  ? 29.885 91.601  49.739 1   40.1   ? 57  PHE   D CZ  1 
ATOM   8453  N  N   . ILE   D 1 36  ? 28.473 91.297  43.8   1   36.19  ? 58  ILE   D N   1 
ATOM   8454  C  CA  . ILE   D 1 36  ? 27.135 90.756  43.601 1   36.18  ? 58  ILE   D CA  1 
ATOM   8455  C  C   . ILE   D 1 36  ? 27.163 89.461  42.786 1   36     ? 58  ILE   D C   1 
ATOM   8456  O  O   . ILE   D 1 36  ? 26.637 88.45   43.231 1   36.24  ? 58  ILE   D O   1 
ATOM   8457  C  CB  . ILE   D 1 36  ? 26.196 91.828  42.99  1   36.84  ? 58  ILE   D CB  1 
ATOM   8458  C  CG1 . ILE   D 1 36  ? 25.965 93.005  43.957 1   38.07  ? 58  ILE   D CG1 1 
ATOM   8459  C  CG2 . ILE   D 1 36  ? 24.877 91.237  42.539 1   36.92  ? 58  ILE   D CG2 1 
ATOM   8460  C  CD1 . ILE   D 1 36  ? 25.337 94.239  43.287 1   38.94  ? 58  ILE   D CD1 1 
ATOM   8461  N  N   . ILE   D 1 37  ? 27.782 89.482  41.603 1   35.55  ? 59  ILE   D N   1 
ATOM   8462  C  CA  . ILE   D 1 37  ? 27.888 88.311  40.72  1   34.62  ? 59  ILE   D CA  1 
ATOM   8463  C  C   . ILE   D 1 37  ? 28.559 87.122  41.414 1   34.25  ? 59  ILE   D C   1 
ATOM   8464  O  O   . ILE   D 1 37  ? 28.029 86.024  41.341 1   34.68  ? 59  ILE   D O   1 
ATOM   8465  C  CB  . ILE   D 1 37  ? 28.582 88.72   39.393 1   34.12  ? 59  ILE   D CB  1 
ATOM   8466  C  CG1 . ILE   D 1 37  ? 27.662 89.652  38.559 1   33.95  ? 59  ILE   D CG1 1 
ATOM   8467  C  CG2 . ILE   D 1 37  ? 29.102 87.525  38.595 1   34.29  ? 59  ILE   D CG2 1 
ATOM   8468  C  CD1 . ILE   D 1 37  ? 26.44  89.04   37.979 1   33.77  ? 59  ILE   D CD1 1 
ATOM   8469  N  N   . THR   D 1 38  ? 29.668 87.339  42.135 1   33.71  ? 60  THR   D N   1 
ATOM   8470  C  CA  . THR   D 1 38  ? 30.365 86.251  42.843 1   34.17  ? 60  THR   D CA  1 
ATOM   8471  C  C   . THR   D 1 38  ? 29.449 85.592  43.865 1   35.15  ? 60  THR   D C   1 
ATOM   8472  O  O   . THR   D 1 38  ? 29.382 84.371  43.923 1   35.73  ? 60  THR   D O   1 
ATOM   8473  C  CB  . THR   D 1 38  ? 31.647 86.746  43.546 1   34.43  ? 60  THR   D CB  1 
ATOM   8474  O  OG1 . THR   D 1 38  ? 32.508 87.434  42.638 1   34.54  ? 60  THR   D OG1 1 
ATOM   8475  C  CG2 . THR   D 1 38  ? 32.394 85.632  44.219 1   34.66  ? 60  THR   D CG2 1 
ATOM   8476  N  N   . HIS   D 1 39  ? 28.713 86.401  44.635 1   35.22  ? 61  HIS   D N   1 
ATOM   8477  C  CA  . HIS   D 1 39  ? 27.783 85.914  45.644 1   35.74  ? 61  HIS   D CA  1 
ATOM   8478  C  C   . HIS   D 1 39  ? 26.611 85.176  45.007 1   37.34  ? 61  HIS   D C   1 
ATOM   8479  O  O   . HIS   D 1 39  ? 26.179 84.15   45.518 1   38.13  ? 61  HIS   D O   1 
ATOM   8480  C  CB  . HIS   D 1 39  ? 27.286 87.072  46.509 1   35.83  ? 61  HIS   D CB  1 
ATOM   8481  C  CG  . HIS   D 1 39  ? 28.144 87.369  47.703 1   36.52  ? 61  HIS   D CG  1 
ATOM   8482  N  ND1 . HIS   D 1 39  ? 29.292 88.122  47.599 1   37.56  ? 61  HIS   D ND1 1 
ATOM   8483  C  CD2 . HIS   D 1 39  ? 27.972 87.015  48.997 1   37.88  ? 61  HIS   D CD2 1 
ATOM   8484  C  CE1 . HIS   D 1 39  ? 29.802 88.179  48.82  1   38.41  ? 61  HIS   D CE1 1 
ATOM   8485  N  NE2 . HIS   D 1 39  ? 29.047 87.525  49.695 1   38.79  ? 61  HIS   D NE2 1 
ATOM   8486  N  N   . GLN   D 1 40  ? 26.112 85.672  43.89  1   37.94  ? 62  GLN   D N   1 
ATOM   8487  C  CA  . GLN   D 1 40  ? 25.006 85.045  43.177 1   39.41  ? 62  GLN   D CA  1 
ATOM   8488  C  C   . GLN   D 1 40  ? 25.416 83.747  42.503 1   40.37  ? 62  GLN   D C   1 
ATOM   8489  O  O   . GLN   D 1 40  ? 24.584 82.859  42.329 1   40.81  ? 62  GLN   D O   1 
ATOM   8490  C  CB  . GLN   D 1 40  ? 24.427 86.008  42.141 1   41.92  ? 62  GLN   D CB  1 
ATOM   8491  C  CG  . GLN   D 1 40  ? 23.677 87.174  42.776 1   45.76  ? 62  GLN   D CG  1 
ATOM   8492  C  CD  . GLN   D 1 40  ? 23.193 88.171  41.763 1   49.94  ? 62  GLN   D CD  1 
ATOM   8493  O  OE1 . GLN   D 1 40  ? 23.693 88.254  40.638 1   51.7   ? 62  GLN   D OE1 1 
ATOM   8494  N  NE2 . GLN   D 1 40  ? 22.215 88.967  42.146 1   50.28  ? 62  GLN   D NE2 1 
ATOM   8495  N  N   . ALA   D 1 41  ? 26.688 83.635  42.095 1   40.44  ? 63  ALA   D N   1 
ATOM   8496  C  CA  . ALA   D 1 41  ? 27.199 82.404  41.51  1   40.42  ? 63  ALA   D CA  1 
ATOM   8497  C  C   . ALA   D 1 41  ? 27.27  81.343  42.644 1   39.35  ? 63  ALA   D C   1 
ATOM   8498  O  O   . ALA   D 1 41  ? 26.869 80.201  42.431 1   39.03  ? 63  ALA   D O   1 
ATOM   8499  C  CB  . ALA   D 1 41  ? 28.57  82.649  40.909 1   41.02  ? 63  ALA   D CB  1 
ATOM   8500  N  N   . TYR   D 1 42  ? 27.706 81.751  43.866 1   38.38  ? 64  TYR   D N   1 
ATOM   8501  C  CA  . TYR   D 1 42  ? 27.727 80.895  45.055 1   37.92  ? 64  TYR   D CA  1 
ATOM   8502  C  C   . TYR   D 1 42  ? 26.309 80.407  45.345 1   37.48  ? 64  TYR   D C   1 
ATOM   8503  O  O   . TYR   D 1 42  ? 26.115 79.215  45.48  1   37.87  ? 64  TYR   D O   1 
ATOM   8504  C  CB  . TYR   D 1 42  ? 28.248 81.652  46.294 1   37.61  ? 64  TYR   D CB  1 
ATOM   8505  C  CG  . TYR   D 1 42  ? 29.738 81.536  46.491 1   38.32  ? 64  TYR   D CG  1 
ATOM   8506  C  CD1 . TYR   D 1 42  ? 30.296 80.408  47.069 1   39.05  ? 64  TYR   D CD1 1 
ATOM   8507  C  CD2 . TYR   D 1 42  ? 30.591 82.557  46.104 1   39.3   ? 64  TYR   D CD2 1 
ATOM   8508  C  CE1 . TYR   D 1 42  ? 31.665 80.297  47.254 1   39.85  ? 64  TYR   D CE1 1 
ATOM   8509  C  CE2 . TYR   D 1 42  ? 31.961 82.453  46.273 1   40.18  ? 64  TYR   D CE2 1 
ATOM   8510  C  CZ  . TYR   D 1 42  ? 32.494 81.323  46.855 1   41.05  ? 64  TYR   D CZ  1 
ATOM   8511  O  OH  . TYR   D 1 42  ? 33.852 81.211  47.005 1   42.93  ? 64  TYR   D OH  1 
ATOM   8512  N  N   . GLU   D 1 43  ? 25.314 81.31   45.336 1   36.33  ? 65  GLU   D N   1 
ATOM   8513  C  CA  . GLU   D 1 43  ? 23.934 80.962  45.628 1   35.99  ? 65  GLU   D CA  1 
ATOM   8514  C  C   . GLU   D 1 43  ? 23.288 80.051  44.607 1   35.98  ? 65  GLU   D C   1 
ATOM   8515  O  O   . GLU   D 1 43  ? 22.43  79.251  44.972 1   35.79  ? 65  GLU   D O   1 
ATOM   8516  C  CB  . GLU   D 1 43  ? 23.093 82.216  45.853 1   37.49  ? 65  GLU   D CB  1 
ATOM   8517  C  CG  . GLU   D 1 43  ? 23.445 82.942  47.141 1   40.92  ? 65  GLU   D CG  1 
ATOM   8518  C  CD  . GLU   D 1 43  ? 23.118 82.219  48.434 1   46.72  ? 65  GLU   D CD  1 
ATOM   8519  O  OE1 . GLU   D 1 43  ? 22.049 81.57   48.511 1   47.96  ? 65  GLU   D OE1 1 
ATOM   8520  O  OE2 . GLU   D 1 43  ? 23.92  82.334  49.389 1   49.58  ? 65  GLU   D OE2 1 
ATOM   8521  N  N   . LEU   D 1 44  ? 23.706 80.136  43.337 1   36.13  ? 66  LEU   D N   1 
ATOM   8522  C  CA  . LEU   D 1 44  ? 23.188 79.244  42.311 1   36.25  ? 66  LEU   D CA  1 
ATOM   8523  C  C   . LEU   D 1 44  ? 23.71  77.838  42.593 1   37.25  ? 66  LEU   D C   1 
ATOM   8524  O  O   . LEU   D 1 44  ? 22.93  76.885  42.624 1   37.72  ? 66  LEU   D O   1 
ATOM   8525  C  CB  . LEU   D 1 44  ? 23.622 79.698  40.907 1   35.99  ? 66  LEU   D CB  1 
ATOM   8526  C  CG  . LEU   D 1 44  ? 22.822 80.819  40.231 1   36.66  ? 66  LEU   D CG  1 
ATOM   8527  C  CD1 . LEU   D 1 44  ? 23.306 81.031  38.812 1   36.63  ? 66  LEU   D CD1 1 
ATOM   8528  C  CD2 . LEU   D 1 44  ? 21.323 80.506  40.214 1   37.03  ? 66  LEU   D CD2 1 
ATOM   8529  N  N   . TRP   D 1 45  ? 25.018 77.715  42.869 1   37.66  ? 67  TRP   D N   1 
ATOM   8530  C  CA  . TRP   D 1 45  ? 25.62  76.423  43.168 1   38.62  ? 67  TRP   D CA  1 
ATOM   8531  C  C   . TRP   D 1 45  ? 25.187 75.868  44.522 1   39.53  ? 67  TRP   D C   1 
ATOM   8532  O  O   . TRP   D 1 45  ? 25.164 74.651  44.68  1   40.09  ? 67  TRP   D O   1 
ATOM   8533  C  CB  . TRP   D 1 45  ? 27.144 76.452  43.007 1   38.56  ? 67  TRP   D CB  1 
ATOM   8534  C  CG  . TRP   D 1 45  ? 27.599 76.65   41.585 1   38.69  ? 67  TRP   D CG  1 
ATOM   8535  C  CD1 . TRP   D 1 45  ? 28.288 77.719  41.087 1   39.42  ? 67  TRP   D CD1 1 
ATOM   8536  C  CD2 . TRP   D 1 45  ? 27.381 75.756  40.472 1   38.58  ? 67  TRP   D CD2 1 
ATOM   8537  N  NE1 . TRP   D 1 45  ? 28.502 77.558  39.731 1   39.66  ? 67  TRP   D NE1 1 
ATOM   8538  C  CE2 . TRP   D 1 45  ? 27.975 76.348  39.335 1   39.35  ? 67  TRP   D CE2 1 
ATOM   8539  C  CE3 . TRP   D 1 45  ? 26.751 74.511  40.328 1   38.61  ? 67  TRP   D CE3 1 
ATOM   8540  C  CZ2 . TRP   D 1 45  ? 27.934 75.743  38.071 1   39.27  ? 67  TRP   D CZ2 1 
ATOM   8541  C  CZ3 . TRP   D 1 45  ? 26.727 73.914  39.083 1   38.94  ? 67  TRP   D CZ3 1 
ATOM   8542  C  CH2 . TRP   D 1 45  ? 27.314 74.526  37.974 1   38.85  ? 67  TRP   D CH2 1 
ATOM   8543  N  N   . PHE   D 1 46  ? 24.762 76.734  45.47  1   39.47  ? 68  PHE   D N   1 
ATOM   8544  C  CA  . PHE   D 1 46  ? 24.207 76.291  46.752 1   38.99  ? 68  PHE   D CA  1 
ATOM   8545  C  C   . PHE   D 1 46  ? 22.866 75.598  46.469 1   38.96  ? 68  PHE   D C   1 
ATOM   8546  O  O   . PHE   D 1 46  ? 22.636 74.499  46.964 1   39.29  ? 68  PHE   D O   1 
ATOM   8547  C  CB  . PHE   D 1 46  ? 24.005 77.471  47.71  1   38.73  ? 68  PHE   D CB  1 
ATOM   8548  C  CG  . PHE   D 1 46  ? 25.24  78.021  48.391 1   39.56  ? 68  PHE   D CG  1 
ATOM   8549  C  CD1 . PHE   D 1 46  ? 26.451 77.343  48.33  1   40.41  ? 68  PHE   D CD1 1 
ATOM   8550  C  CD2 . PHE   D 1 46  ? 25.211 79.252  49.024 1   40.11  ? 68  PHE   D CD2 1 
ATOM   8551  C  CE1 . PHE   D 1 46  ? 27.591 77.869  48.921 1   40.89  ? 68  PHE   D CE1 1 
ATOM   8552  C  CE2 . PHE   D 1 46  ? 26.359 79.779  49.612 1   40.7   ? 68  PHE   D CE2 1 
ATOM   8553  C  CZ  . PHE   D 1 46  ? 27.535 79.074  49.574 1   40.56  ? 68  PHE   D CZ  1 
ATOM   8554  N  N   . LYS   D 1 47  ? 22.024 76.194  45.595 1   38.38  ? 69  LYS   D N   1 
ATOM   8555  C  CA  . LYS   D 1 47  ? 20.744 75.6    45.215 1   38.18  ? 69  LYS   D CA  1 
ATOM   8556  C  C   . LYS   D 1 47  ? 20.951 74.232  44.57  1   38.13  ? 69  LYS   D C   1 
ATOM   8557  O  O   . LYS   D 1 47  ? 20.204 73.299  44.857 1   38.43  ? 69  LYS   D O   1 
ATOM   8558  C  CB  . LYS   D 1 47  ? 19.939 76.541  44.299 1   39.55  ? 69  LYS   D CB  1 
ATOM   8559  C  CG  . LYS   D 1 47  ? 18.532 76.014  44.028 1   42.59  ? 69  LYS   D CG  1 
ATOM   8560  C  CD  . LYS   D 1 47  ? 17.609 77.052  43.441 1   45.22  ? 69  LYS   D CD  1 
ATOM   8561  C  CE  . LYS   D 1 47  ? 16.311 76.415  43.02  1   47.7   ? 69  LYS   D CE  1 
ATOM   8562  N  NZ  . LYS   D 1 47  ? 15.303 77.435  42.625 1   49.97  ? 69  LYS   D NZ  1 
ATOM   8563  N  N   . GLN   D 1 48  ? 22.014 74.095  43.758 1   37.79  ? 70  GLN   D N   1 
ATOM   8564  C  CA  . GLN   D 1 48  ? 22.362 72.823  43.116 1   37.33  ? 70  GLN   D CA  1 
ATOM   8565  C  C   . GLN   D 1 48  ? 22.791 71.777  44.13  1   36.56  ? 70  GLN   D C   1 
ATOM   8566  O  O   . GLN   D 1 48  ? 22.284 70.667  44.087 1   35.57  ? 70  GLN   D O   1 
ATOM   8567  C  CB  . GLN   D 1 48  ? 23.443 73.011  42.037 1   37.98  ? 70  GLN   D CB  1 
ATOM   8568  C  CG  . GLN   D 1 48  ? 23.665 71.742  41.207 1   38.12  ? 70  GLN   D CG  1 
ATOM   8569  C  CD  . GLN   D 1 48  ? 22.435 71.399  40.41  1   37.33  ? 70  GLN   D CD  1 
ATOM   8570  O  OE1 . GLN   D 1 48  ? 21.797 72.286  39.84  1   37.68  ? 70  GLN   D OE1 1 
ATOM   8571  N  NE2 . GLN   D 1 48  ? 22.075 70.12   40.357 1   35.99  ? 70  GLN   D NE2 1 
ATOM   8572  N  N   . ILE   D 1 49  ? 23.684 72.149  45.071 1   37.38  ? 71  ILE   D N   1 
ATOM   8573  C  CA  . ILE   D 1 49  ? 24.151 71.264  46.14  1   38.58  ? 71  ILE   D CA  1 
ATOM   8574  C  C   . ILE   D 1 49  ? 22.977 70.763  46.978 1   40.27  ? 71  ILE   D C   1 
ATOM   8575  O  O   . ILE   D 1 49  ? 22.9   69.565  47.251 1   40.92  ? 71  ILE   D O   1 
ATOM   8576  C  CB  . ILE   D 1 49  ? 25.248 71.933  47.008 1   39.11  ? 71  ILE   D CB  1 
ATOM   8577  C  CG1 . ILE   D 1 49  ? 26.524 72.192  46.204 1   39.75  ? 71  ILE   D CG1 1 
ATOM   8578  C  CG2 . ILE   D 1 49  ? 25.573 71.09   48.241 1   39.87  ? 71  ILE   D CG2 1 
ATOM   8579  C  CD1 . ILE   D 1 49  ? 27.472 73.135  46.887 1   40.64  ? 71  ILE   D CD1 1 
ATOM   8580  N  N   . ILE   D 1 50  ? 22.034 71.663  47.34  1   40.92  ? 72  ILE   D N   1 
ATOM   8581  C  CA  . ILE   D 1 50  ? 20.84  71.319  48.126 1   41.62  ? 72  ILE   D CA  1 
ATOM   8582  C  C   . ILE   D 1 50  ? 19.956 70.335  47.36  1   42.02  ? 72  ILE   D C   1 
ATOM   8583  O  O   . ILE   D 1 50  ? 19.448 69.376  47.937 1   42.08  ? 72  ILE   D O   1 
ATOM   8584  C  CB  . ILE   D 1 50  ? 20.061 72.597  48.535 1   42.29  ? 72  ILE   D CB  1 
ATOM   8585  C  CG1 . ILE   D 1 50  ? 20.847 73.415  49.568 1   43.17  ? 72  ILE   D CG1 1 
ATOM   8586  C  CG2 . ILE   D 1 50  ? 18.675 72.258  49.086 1   42.88  ? 72  ILE   D CG2 1 
ATOM   8587  C  CD1 . ILE   D 1 50  ? 20.314 74.806  49.791 1   44.24  ? 72  ILE   D CD1 1 
ATOM   8588  N  N   . PHE   D 1 51  ? 19.803 70.561  46.058 1   42.29  ? 73  PHE   D N   1 
ATOM   8589  C  CA  . PHE   D 1 51  ? 19.007 69.702  45.197 1   43.46  ? 73  PHE   D CA  1 
ATOM   8590  C  C   . PHE   D 1 51  ? 19.584 68.283  45.159 1   44.34  ? 73  PHE   D C   1 
ATOM   8591  O  O   . PHE   D 1 51  ? 18.833 67.301  45.207 1   44.7   ? 73  PHE   D O   1 
ATOM   8592  C  CB  . PHE   D 1 51  ? 18.962 70.29   43.787 1   43.78  ? 73  PHE   D CB  1 
ATOM   8593  C  CG  . PHE   D 1 51  ? 17.948 69.629  42.884 1   45.03  ? 73  PHE   D CG  1 
ATOM   8594  C  CD1 . PHE   D 1 51  ? 16.595 69.855  43.055 1   45.88  ? 73  PHE   D CD1 1 
ATOM   8595  C  CD2 . PHE   D 1 51  ? 18.348 68.784  41.863 1   45.94  ? 73  PHE   D CD2 1 
ATOM   8596  C  CE1 . PHE   D 1 51  ? 15.661 69.253  42.214 1   46.55  ? 73  PHE   D CE1 1 
ATOM   8597  C  CE2 . PHE   D 1 51  ? 17.41  68.17   41.036 1   46.72  ? 73  PHE   D CE2 1 
ATOM   8598  C  CZ  . PHE   D 1 51  ? 16.073 68.411  41.214 1   46.42  ? 73  PHE   D CZ  1 
ATOM   8599  N  N   . GLU   D 1 52  ? 20.922 68.182  45.083 1   44.42  ? 74  GLU   D N   1 
ATOM   8600  C  CA  . GLU   D 1 52  ? 21.601 66.898  45.032 1   44.98  ? 74  GLU   D CA  1 
ATOM   8601  C  C   . GLU   D 1 52  ? 21.505 66.195  46.366 1   45.68  ? 74  GLU   D C   1 
ATOM   8602  O  O   . GLU   D 1 52  ? 21.217 64.998  46.409 1   45.56  ? 74  GLU   D O   1 
ATOM   8603  C  CB  . GLU   D 1 52  ? 23.078 67.057  44.596 1   46.21  ? 74  GLU   D CB  1 
ATOM   8604  C  CG  . GLU   D 1 52  ? 23.275 67.612  43.197 1   47.47  ? 74  GLU   D CG  1 
ATOM   8605  C  CD  . GLU   D 1 52  ? 22.683 66.811  42.051 1   50.86  ? 74  GLU   D CD  1 
ATOM   8606  O  OE1 . GLU   D 1 52  ? 22.502 65.58   42.198 1   48.44  ? 74  GLU   D OE1 1 
ATOM   8607  O  OE2 . GLU   D 1 52  ? 22.419 67.42   40.988 1   54     ? 74  GLU   D OE2 1 
ATOM   8608  N  N   . PHE   D 1 53  ? 21.717 66.952  47.459 1   46.36  ? 75  PHE   D N   1 
ATOM   8609  C  CA  . PHE   D 1 53  ? 21.673 66.443  48.821 1   47.09  ? 75  PHE   D CA  1 
ATOM   8610  C  C   . PHE   D 1 53  ? 20.306 65.903  49.154 1   47.96  ? 75  PHE   D C   1 
ATOM   8611  O  O   . PHE   D 1 53  ? 20.202 64.832  49.748 1   48.16  ? 75  PHE   D O   1 
ATOM   8612  C  CB  . PHE   D 1 53  ? 22.085 67.533  49.82  1   46.99  ? 75  PHE   D CB  1 
ATOM   8613  C  CG  . PHE   D 1 53  ? 23.564 67.634  50.138 1   47.34  ? 75  PHE   D CG  1 
ATOM   8614  C  CD1 . PHE   D 1 53  ? 24.499 66.915  49.414 1   47.83  ? 75  PHE   D CD1 1 
ATOM   8615  C  CD2 . PHE   D 1 53  ? 24.013 68.44   51.17  1   48.02  ? 75  PHE   D CD2 1 
ATOM   8616  C  CE1 . PHE   D 1 53  ? 25.852 66.995  49.721 1   48.53  ? 75  PHE   D CE1 1 
ATOM   8617  C  CE2 . PHE   D 1 53  ? 25.369 68.544  51.453 1   48.7   ? 75  PHE   D CE2 1 
ATOM   8618  C  CZ  . PHE   D 1 53  ? 26.281 67.815  50.729 1   48.35  ? 75  PHE   D CZ  1 
ATOM   8619  N  N   . ASP   D 1 54  ? 19.253 66.615  48.745 1   48.34  ? 76  ASP   D N   1 
ATOM   8620  C  CA  . ASP   D 1 54  ? 17.903 66.175  49.027 1   49.1   ? 76  ASP   D CA  1 
ATOM   8621  C  C   . ASP   D 1 54  ? 17.585 64.885  48.315 1   49.43  ? 76  ASP   D C   1 
ATOM   8622  O  O   . ASP   D 1 54  ? 16.987 64.013  48.926 1   50.28  ? 76  ASP   D O   1 
ATOM   8623  C  CB  . ASP   D 1 54  ? 16.883 67.275  48.727 1   51.48  ? 76  ASP   D CB  1 
ATOM   8624  C  CG  . ASP   D 1 54  ? 16.826 68.328  49.815 1   57.36  ? 76  ASP   D CG  1 
ATOM   8625  O  OD1 . ASP   D 1 54  ? 17.136 67.991  50.987 1   58.79  ? 76  ASP   D OD1 1 
ATOM   8626  O  OD2 . ASP   D 1 54  ? 16.469 69.489  49.501 1   59.57  ? 76  ASP   D OD2 1 
ATOM   8627  N  N   . SER   D 1 55  ? 18.043 64.717  47.074 1   48.88  ? 77  SER   D N   1 
ATOM   8628  C  CA  . SER   D 1 55  ? 17.803 63.484  46.336 1   49.14  ? 77  SER   D CA  1 
ATOM   8629  C  C   . SER   D 1 55  ? 18.587 62.307  46.924 1   49.84  ? 77  SER   D C   1 
ATOM   8630  O  O   . SER   D 1 55  ? 18.051 61.202  47.014 1   49.88  ? 77  SER   D O   1 
ATOM   8631  C  CB  . SER   D 1 55  ? 18.111 63.673  44.857 1   49.88  ? 77  SER   D CB  1 
ATOM   8632  O  OG  . SER   D 1 55  ? 19.499 63.818  44.6   1   51.38  ? 77  SER   D OG  1 
ATOM   8633  N  N   . ILE   D 1 56  ? 19.833 62.547  47.356 1   50.28  ? 78  ILE   D N   1 
ATOM   8634  C  CA  . ILE   D 1 56  ? 20.647 61.505  47.991 1   51.54  ? 78  ILE   D CA  1 
ATOM   8635  C  C   . ILE   D 1 56  ? 20.025 61.089  49.328 1   53.76  ? 78  ILE   D C   1 
ATOM   8636  O  O   . ILE   D 1 56  ? 20.062 59.905  49.679 1   54.21  ? 78  ILE   D O   1 
ATOM   8637  C  CB  . ILE   D 1 56  ? 22.107 61.98   48.181 1   51.19  ? 78  ILE   D CB  1 
ATOM   8638  C  CG1 . ILE   D 1 56  ? 22.792 62.212  46.839 1   51.35  ? 78  ILE   D CG1 1 
ATOM   8639  C  CG2 . ILE   D 1 56  ? 22.911 61.016  49.065 1   51.16  ? 78  ILE   D CG2 1 
ATOM   8640  C  CD1 . ILE   D 1 56  ? 24.014 63.051  46.974 1   52.36  ? 78  ILE   D CD1 1 
ATOM   8641  N  N   . ARG   D 1 57  ? 19.448 62.06   50.072 1   55.02  ? 79  ARG   D N   1 
ATOM   8642  C  CA  . ARG   D 1 57  ? 18.785 61.785  51.345 1   56.68  ? 79  ARG   D CA  1 
ATOM   8643  C  C   . ARG   D 1 57  ? 17.572 60.887  51.125 1   57.2   ? 79  ARG   D C   1 
ATOM   8644  O  O   . ARG   D 1 57  ? 17.393 59.915  51.854 1   57.21  ? 79  ARG   D O   1 
ATOM   8645  C  CB  . ARG   D 1 57  ? 18.343 63.082  52.035 1   59.37  ? 79  ARG   D CB  1 
ATOM   8646  C  CG  . ARG   D 1 57  ? 19.464 63.883  52.707 1   64.27  ? 79  ARG   D CG  1 
ATOM   8647  C  CD  . ARG   D 1 57  ? 18.979 64.997  53.64  1   69.03  ? 79  ARG   D CD  1 
ATOM   8648  N  NE  . ARG   D 1 57  ? 17.739 65.637  53.188 1   73.63  ? 79  ARG   D NE  1 
ATOM   8649  C  CZ  . ARG   D 1 57  ? 16.546 65.432  53.742 1   77.29  ? 79  ARG   D CZ  1 
ATOM   8650  N  NH1 . ARG   D 1 57  ? 16.421 64.617  54.784 1   76.74  ? 79  ARG   D NH1 1 
ATOM   8651  N  NH2 . ARG   D 1 57  ? 15.47  66.04   53.258 1   78.29  ? 79  ARG   D NH2 1 
ATOM   8652  N  N   . ASP   D 1 58  ? 16.769 61.183  50.091 1   57.53  ? 80  ASP   D N   1 
ATOM   8653  C  CA  . ASP   D 1 58  ? 15.586 60.393  49.753 1   58.27  ? 80  ASP   D CA  1 
ATOM   8654  C  C   . ASP   D 1 58  ? 15.954 58.96   49.356 1   57.85  ? 80  ASP   D C   1 
ATOM   8655  O  O   . ASP   D 1 58  ? 15.225 58.027  49.685 1   57.95  ? 80  ASP   D O   1 
ATOM   8656  C  CB  . ASP   D 1 58  ? 14.778 61.092  48.643 1   61.5   ? 80  ASP   D CB  1 
ATOM   8657  C  CG  . ASP   D 1 58  ? 14.228 62.466  49.025 1   68.26  ? 80  ASP   D CG  1 
ATOM   8658  O  OD1 . ASP   D 1 58  ? 14.512 62.934  50.156 1   69.45  ? 80  ASP   D OD1 1 
ATOM   8659  O  OD2 . ASP   D 1 58  ? 13.535 63.082  48.189 1   71.27  ? 80  ASP   D OD2 1 
ATOM   8660  N  N   . MET   D 1 59  ? 17.094 58.789  48.677 1   57.47  ? 81  MET   D N   1 
ATOM   8661  C  CA  . MET   D 1 59  ? 17.605 57.484  48.274 1   58.01  ? 81  MET   D CA  1 
ATOM   8662  C  C   . MET   D 1 59  ? 18.123 56.688  49.47  1   58.98  ? 81  MET   D C   1 
ATOM   8663  O  O   . MET   D 1 59  ? 17.985 55.46   49.51  1   59.2   ? 81  MET   D O   1 
ATOM   8664  C  CB  . MET   D 1 59  ? 18.722 57.64   47.233 1   58.49  ? 81  MET   D CB  1 
ATOM   8665  C  CG  . MET   D 1 59  ? 18.207 57.989  45.853 1   60.11  ? 81  MET   D CG  1 
ATOM   8666  S  SD  . MET   D 1 59  ? 19.473 57.831  44.567 1   61.16  ? 81  MET   D SD  1 
ATOM   8667  C  CE  . MET   D 1 59  ? 20.363 59.334  44.815 1   57.9   ? 81  MET   D CE  1 
ATOM   8668  N  N   . LEU   D 1 60  ? 18.736 57.38   50.439 1   59.46  ? 82  LEU   D N   1 
ATOM   8669  C  CA  . LEU   D 1 60  ? 19.254 56.744  51.645 1   60.29  ? 82  LEU   D CA  1 
ATOM   8670  C  C   . LEU   D 1 60  ? 18.164 56.432  52.676 1   61.75  ? 82  LEU   D C   1 
ATOM   8671  O  O   . LEU   D 1 60  ? 18.401 55.629  53.582 1   62.38  ? 82  LEU   D O   1 
ATOM   8672  C  CB  . LEU   D 1 60  ? 20.335 57.618  52.283 1   60.12  ? 82  LEU   D CB  1 
ATOM   8673  C  CG  . LEU   D 1 60  ? 21.666 57.64   51.569 1   60.78  ? 82  LEU   D CG  1 
ATOM   8674  C  CD1 . LEU   D 1 60  ? 22.584 58.636  52.216 1   61.37  ? 82  LEU   D CD1 1 
ATOM   8675  C  CD2 . LEU   D 1 60  ? 22.305 56.253  51.558 1   60.83  ? 82  LEU   D CD2 1 
ATOM   8676  N  N   . ASP   D 1 61  ? 16.981 57.067  52.556 1   62.26  ? 83  ASP   D N   1 
ATOM   8677  C  CA  . ASP   D 1 61  ? 15.855 56.868  53.465 1   63.32  ? 83  ASP   D CA  1 
ATOM   8678  C  C   . ASP   D 1 61  ? 15.047 55.629  53.038 1   64.21  ? 83  ASP   D C   1 
ATOM   8679  O  O   . ASP   D 1 61  ? 13.837 55.708  52.833 1   64.54  ? 83  ASP   D O   1 
ATOM   8680  C  CB  . ASP   D 1 61  ? 14.974 58.136  53.489 1   64.94  ? 83  ASP   D CB  1 
ATOM   8681  C  CG  . ASP   D 1 61  ? 14.124 58.303  54.732 1   69.1   ? 83  ASP   D CG  1 
ATOM   8682  O  OD1 . ASP   D 1 61  ? 14.655 58.792  55.756 1   69.89  ? 83  ASP   D OD1 1 
ATOM   8683  O  OD2 . ASP   D 1 61  ? 12.923 57.967  54.676 1   71.08  ? 83  ASP   D OD2 1 
ATOM   8684  N  N   . ALA   D 1 62  ? 15.729 54.488  52.897 1   64.48  ? 84  ALA   D N   1 
ATOM   8685  C  CA  . ALA   D 1 62  ? 15.137 53.217  52.492 1   65.61  ? 84  ALA   D CA  1 
ATOM   8686  C  C   . ALA   D 1 62  ? 15.867 52.068  53.194 1   66.88  ? 84  ALA   D C   1 
ATOM   8687  O  O   . ALA   D 1 62  ? 17.075 52.159  53.418 1   66.9   ? 84  ALA   D O   1 
ATOM   8688  C  CB  . ALA   D 1 62  ? 15.248 53.049  50.979 1   65.65  ? 84  ALA   D CB  1 
ATOM   8689  N  N   . GLU   D 1 63  ? 15.148 50.977  53.524 1   67.71  ? 85  GLU   D N   1 
ATOM   8690  C  CA  . GLU   D 1 63  ? 15.759 49.815  54.192 1   68.79  ? 85  GLU   D CA  1 
ATOM   8691  C  C   . GLU   D 1 63  ? 16.694 48.997  53.281 1   68.5   ? 85  GLU   D C   1 
ATOM   8692  O  O   . GLU   D 1 63  ? 17.611 48.327  53.77  1   68.16  ? 85  GLU   D O   1 
ATOM   8693  C  CB  . GLU   D 1 63  ? 14.686 48.919  54.835 1   72.32  ? 85  GLU   D CB  1 
ATOM   8694  C  CG  . GLU   D 1 63  ? 14.389 49.28   56.28  1   79.51  ? 85  GLU   D CG  1 
ATOM   8695  C  CD  . GLU   D 1 63  ? 14.943 48.305  57.304 1   88.79  ? 85  GLU   D CD  1 
ATOM   8696  O  OE1 . GLU   D 1 63  ? 14.269 47.284  57.576 1   90.91  ? 85  GLU   D OE1 1 
ATOM   8697  O  OE2 . GLU   D 1 63  ? 16.044 48.564  57.843 1   91.66  ? 85  GLU   D OE2 1 
ATOM   8698  N  N   . VAL   D 1 64  ? 16.46  49.073  51.959 1   68.35  ? 86  VAL   D N   1 
ATOM   8699  C  CA  . VAL   D 1 64  ? 17.246 48.371  50.948 1   68.61  ? 86  VAL   D CA  1 
ATOM   8700  C  C   . VAL   D 1 64  ? 17.87  49.352  49.946 1   67.82  ? 86  VAL   D C   1 
ATOM   8701  O  O   . VAL   D 1 64  ? 17.161 50.048  49.215 1   68.17  ? 86  VAL   D O   1 
ATOM   8702  C  CB  . VAL   D 1 64  ? 16.42  47.268  50.238 1   70.1   ? 86  VAL   D CB  1 
ATOM   8703  C  CG1 . VAL   D 1 64  ? 15.044 47.787  49.809 1   70.77  ? 86  VAL   D CG1 1 
ATOM   8704  C  CG2 . VAL   D 1 64  ? 17.185 46.674  49.052 1   70.98  ? 86  VAL   D CG2 1 
ATOM   8705  N  N   . ILE   D 1 65  ? 19.201 49.434  49.941 1   66.65  ? 87  ILE   D N   1 
ATOM   8706  C  CA  . ILE   D 1 65  ? 19.907 50.308  49.01  1   66.05  ? 87  ILE   D CA  1 
ATOM   8707  C  C   . ILE   D 1 65  ? 20.74  49.405  48.106 1   64.57  ? 87  ILE   D C   1 
ATOM   8708  O  O   . ILE   D 1 65  ? 21.793 48.911  48.509 1   64.83  ? 87  ILE   D O   1 
ATOM   8709  C  CB  . ILE   D 1 65  ? 20.738 51.386  49.757 1   66.96  ? 87  ILE   D CB  1 
ATOM   8710  C  CG1 . ILE   D 1 65  ? 19.832 52.229  50.687 1   68.09  ? 87  ILE   D CG1 1 
ATOM   8711  C  CG2 . ILE   D 1 65  ? 21.479 52.283  48.771 1   67.36  ? 87  ILE   D CG2 1 
ATOM   8712  C  CD1 . ILE   D 1 65  ? 20.463 52.628  52.02  1   69.22  ? 87  ILE   D CD1 1 
ATOM   8713  N  N   . ASP   D 1 66  ? 20.219 49.115  46.914 1   62.98  ? 88  ASP   D N   1 
ATOM   8714  C  CA  . ASP   D 1 66  ? 20.885 48.204  45.981 1   61.87  ? 88  ASP   D CA  1 
ATOM   8715  C  C   . ASP   D 1 66  ? 22.103 48.835  45.263 1   60.1   ? 88  ASP   D C   1 
ATOM   8716  O  O   . ASP   D 1 66  ? 22.38  50.024  45.422 1   59.95  ? 88  ASP   D O   1 
ATOM   8717  C  CB  . ASP   D 1 66  ? 19.868 47.602  44.98  1   63.59  ? 88  ASP   D CB  1 
ATOM   8718  C  CG  . ASP   D 1 66  ? 19.238 48.594  44.022 1   68.78  ? 88  ASP   D CG  1 
ATOM   8719  O  OD1 . ASP   D 1 66  ? 19.078 49.759  44.4   1   69.41  ? 88  ASP   D OD1 1 
ATOM   8720  O  OD2 . ASP   D 1 66  ? 18.885 48.19   42.899 1   71.91  ? 88  ASP   D OD2 1 
ATOM   8721  N  N   . GLU   D 1 67  ? 22.851 48.017  44.512 1   58.48  ? 89  GLU   D N   1 
ATOM   8722  C  CA  . GLU   D 1 67  ? 24.022 48.443  43.771 1   57.83  ? 89  GLU   D CA  1 
ATOM   8723  C  C   . GLU   D 1 67  ? 23.704 49.596  42.811 1   56.64  ? 89  GLU   D C   1 
ATOM   8724  O  O   . GLU   D 1 67  ? 24.529 50.49   42.63  1   56.87  ? 89  GLU   D O   1 
ATOM   8725  C  CB  . GLU   D 1 67  ? 24.549 47.267  42.943 1   60.73  ? 89  GLU   D CB  1 
ATOM   8726  C  CG  . GLU   D 1 67  ? 25.161 46.117  43.711 1   66.18  ? 89  GLU   D CG  1 
ATOM   8727  C  CD  . GLU   D 1 67  ? 25.969 45.234  42.781 1   74.11  ? 89  GLU   D CD  1 
ATOM   8728  O  OE1 . GLU   D 1 67  ? 27.18  45.505  42.6   1   76.01  ? 89  GLU   D OE1 1 
ATOM   8729  O  OE2 . GLU   D 1 67  ? 25.38  44.297  42.196 1   76.88  ? 89  GLU   D OE2 1 
ATOM   8730  N  N   . THR   D 1 68  ? 22.525 49.556  42.177 1   55.05  ? 90  THR   D N   1 
ATOM   8731  C  CA  . THR   D 1 68  ? 22.111 50.571  41.222 1   53.98  ? 90  THR   D CA  1 
ATOM   8732  C  C   . THR   D 1 68  ? 21.867 51.928  41.906 1   53.13  ? 90  THR   D C   1 
ATOM   8733  O  O   . THR   D 1 68  ? 22.368 52.934  41.418 1   53.47  ? 90  THR   D O   1 
ATOM   8734  C  CB  . THR   D 1 68  ? 20.928 50.073  40.382 1   54.78  ? 90  THR   D CB  1 
ATOM   8735  O  OG1 . THR   D 1 68  ? 21.197 48.75   39.905 1   55.59  ? 90  THR   D OG1 1 
ATOM   8736  C  CG2 . THR   D 1 68  ? 20.647 50.97   39.198 1   54.74  ? 90  THR   D CG2 1 
ATOM   8737  N  N   . LYS   D 1 69  ? 21.155 51.964  43.05  1   52.09  ? 91  LYS   D N   1 
ATOM   8738  C  CA  . LYS   D 1 69  ? 20.944 53.221  43.777 1   51.19  ? 91  LYS   D CA  1 
ATOM   8739  C  C   . LYS   D 1 69  ? 22.264 53.737  44.343 1   49.55  ? 91  LYS   D C   1 
ATOM   8740  O  O   . LYS   D 1 69  ? 22.501 54.94   44.309 1   49.43  ? 91  LYS   D O   1 
ATOM   8741  C  CB  . LYS   D 1 69  ? 19.921 53.069  44.905 1   54.01  ? 91  LYS   D CB  1 
ATOM   8742  C  CG  . LYS   D 1 69  ? 18.505 52.816  44.416 1   60.73  ? 91  LYS   D CG  1 
ATOM   8743  C  CD  . LYS   D 1 69  ? 17.814 54.063  43.918 1   67.12  ? 91  LYS   D CD  1 
ATOM   8744  C  CE  . LYS   D 1 69  ? 16.5   53.714  43.258 1   71.56  ? 91  LYS   D CE  1 
ATOM   8745  N  NZ  . LYS   D 1 69  ? 15.673 52.825  44.121 1   74.08  ? 91  LYS   D NZ  1 
ATOM   8746  N  N   . THR   D 1 70  ? 23.141 52.827  44.817 1   48.16  ? 92  THR   D N   1 
ATOM   8747  C  CA  . THR   D 1 70  ? 24.455 53.18   45.353 1   47.42  ? 92  THR   D CA  1 
ATOM   8748  C  C   . THR   D 1 70  ? 25.3   53.93   44.325 1   46.62  ? 92  THR   D C   1 
ATOM   8749  O  O   . THR   D 1 70  ? 25.896 54.945  44.659 1   46.92  ? 92  THR   D O   1 
ATOM   8750  C  CB  . THR   D 1 70  ? 25.159 51.939  45.916 1   48.62  ? 92  THR   D CB  1 
ATOM   8751  O  OG1 . THR   D 1 70  ? 24.401 51.439  47.022 1   49.26  ? 92  THR   D OG1 1 
ATOM   8752  C  CG2 . THR   D 1 70  ? 26.591 52.226  46.369 1   48.94  ? 92  THR   D CG2 1 
ATOM   8753  N  N   . LEU   D 1 71  ? 25.289 53.476  43.061 1   45.67  ? 93  LEU   D N   1 
ATOM   8754  C  CA  . LEU   D 1 71  ? 26.015 54.099  41.955 1   44.7   ? 93  LEU   D CA  1 
ATOM   8755  C  C   . LEU   D 1 71  ? 25.507 55.516  41.679 1   43.59  ? 93  LEU   D C   1 
ATOM   8756  O  O   . LEU   D 1 71  ? 26.307 56.401  41.376 1   43.97  ? 93  LEU   D O   1 
ATOM   8757  C  CB  . LEU   D 1 71  ? 25.867 53.246  40.692 1   44.89  ? 93  LEU   D CB  1 
ATOM   8758  C  CG  . LEU   D 1 71  ? 26.719 51.997  40.621 1   45.99  ? 93  LEU   D CG  1 
ATOM   8759  C  CD1 . LEU   D 1 71  ? 26.329 51.153  39.443 1   46.02  ? 93  LEU   D CD1 1 
ATOM   8760  C  CD2 . LEU   D 1 71  ? 28.167 52.36   40.516 1   47.1   ? 93  LEU   D CD2 1 
ATOM   8761  N  N   . GLU   D 1 72  ? 24.187 55.729  41.765 1   42.04  ? 94  GLU   D N   1 
ATOM   8762  C  CA  . GLU   D 1 72  ? 23.601 57.05   41.551 1   41.46  ? 94  GLU   D CA  1 
ATOM   8763  C  C   . GLU   D 1 72  ? 23.928 58.002  42.716 1   41.06  ? 94  GLU   D C   1 
ATOM   8764  O  O   . GLU   D 1 72  ? 24.101 59.201  42.508 1   40.8   ? 94  GLU   D O   1 
ATOM   8765  C  CB  . GLU   D 1 72  ? 22.092 56.949  41.33  1   43.38  ? 94  GLU   D CB  1 
ATOM   8766  C  CG  . GLU   D 1 72  ? 21.474 58.208  40.752 1   47.38  ? 94  GLU   D CG  1 
ATOM   8767  C  CD  . GLU   D 1 72  ? 21.785 58.467  39.292 1   54.99  ? 94  GLU   D CD  1 
ATOM   8768  O  OE1 . GLU   D 1 72  ? 22.244 57.53   38.597 1   55.15  ? 94  GLU   D OE1 1 
ATOM   8769  O  OE2 . GLU   D 1 72  ? 21.551 59.611  38.837 1   59.42  ? 94  GLU   D OE2 1 
ATOM   8770  N  N   . ILE   D 1 73  ? 24.055 57.464  43.936 1   40.82  ? 95  ILE   D N   1 
ATOM   8771  C  CA  . ILE   D 1 73  ? 24.447 58.263  45.092 1   40.71  ? 95  ILE   D CA  1 
ATOM   8772  C  C   . ILE   D 1 73  ? 25.9   58.713  44.891 1   41.52  ? 95  ILE   D C   1 
ATOM   8773  O  O   . ILE   D 1 73  ? 26.191 59.895  45.049 1   42.35  ? 95  ILE   D O   1 
ATOM   8774  C  CB  . ILE   D 1 73  ? 24.242 57.488  46.414 1   40.31  ? 95  ILE   D CB  1 
ATOM   8775  C  CG1 . ILE   D 1 73  ? 22.751 57.241  46.689 1   39.96  ? 95  ILE   D CG1 1 
ATOM   8776  C  CG2 . ILE   D 1 73  ? 24.886 58.226  47.58  1   40.94  ? 95  ILE   D CG2 1 
ATOM   8777  C  CD1 . ILE   D 1 73  ? 22.472 56.265  47.754 1   40.05  ? 95  ILE   D CD1 1 
ATOM   8778  N  N   . VAL   D 1 74  ? 26.782 57.798  44.452 1   41.08  ? 96  VAL   D N   1 
ATOM   8779  C  CA  . VAL   D 1 74  ? 28.178 58.108  44.157 1   41.23  ? 96  VAL   D CA  1 
ATOM   8780  C  C   . VAL   D 1 74  ? 28.312 59.169  43.023 1   40.67  ? 96  VAL   D C   1 
ATOM   8781  O  O   . VAL   D 1 74  ? 29.1   60.098  43.147 1   40.73  ? 96  VAL   D O   1 
ATOM   8782  C  CB  . VAL   D 1 74  ? 28.975 56.809  43.878 1   42.33  ? 96  VAL   D CB  1 
ATOM   8783  C  CG1 . VAL   D 1 74  ? 30.382 57.111  43.385 1   43.2   ? 96  VAL   D CG1 1 
ATOM   8784  C  CG2 . VAL   D 1 74  ? 29.033 55.94   45.128 1   42.83  ? 96  VAL   D CG2 1 
ATOM   8785  N  N   . LYS   D 1 75  ? 27.487 59.081  41.977 1   39.91  ? 97  LYS   D N   1 
ATOM   8786  C  CA  . LYS   D 1 75  ? 27.5   60.048  40.884 1   39.74  ? 97  LYS   D CA  1 
ATOM   8787  C  C   . LYS   D 1 75  ? 27.184 61.457  41.37  1   39.3   ? 97  LYS   D C   1 
ATOM   8788  O  O   . LYS   D 1 75  ? 27.865 62.422  41.002 1   39.55  ? 97  LYS   D O   1 
ATOM   8789  C  CB  . LYS   D 1 75  ? 26.494 59.627  39.788 1   41.89  ? 97  LYS   D CB  1 
ATOM   8790  C  CG  . LYS   D 1 75  ? 26.357 60.634  38.636 1   45.98  ? 97  LYS   D CG  1 
ATOM   8791  C  CD  . LYS   D 1 75  ? 25.88  59.981  37.35  1   50.8   ? 97  LYS   D CD  1 
ATOM   8792  C  CE  . LYS   D 1 75  ? 24.381 59.887  37.258 1   55.43  ? 97  LYS   D CE  1 
ATOM   8793  N  NZ  . LYS   D 1 75  ? 23.93  58.87   36.264 1   57.32  ? 97  LYS   D NZ  1 
ATOM   8794  N  N   . ARG   D 1 76  ? 26.15  61.57   42.199 1   38.79  ? 98  ARG   D N   1 
ATOM   8795  C  CA  . ARG   D 1 76  ? 25.699 62.842  42.752 1   38.78  ? 98  ARG   D CA  1 
ATOM   8796  C  C   . ARG   D 1 76  ? 26.631 63.385  43.837 1   39.48  ? 98  ARG   D C   1 
ATOM   8797  O  O   . ARG   D 1 76  ? 26.831 64.599  43.903 1   40.1   ? 98  ARG   D O   1 
ATOM   8798  C  CB  . ARG   D 1 76  ? 24.244 62.732  43.222 1   39     ? 98  ARG   D CB  1 
ATOM   8799  C  CG  . ARG   D 1 76  ? 23.355 62.352  42.045 1   40.99  ? 98  ARG   D CG  1 
ATOM   8800  C  CD  . ARG   D 1 76  ? 21.922 62.125  42.42  1   43.37  ? 98  ARG   D CD  1 
ATOM   8801  N  NE  . ARG   D 1 76  ? 21.138 61.68   41.262 1   44.4   ? 98  ARG   D NE  1 
ATOM   8802  C  CZ  . ARG   D 1 76  ? 19.827 61.442  41.29  1   43.87  ? 98  ARG   D CZ  1 
ATOM   8803  N  NH1 . ARG   D 1 76  ? 19.138 61.621  42.406 1   43.41  ? 98  ARG   D NH1 1 
ATOM   8804  N  NH2 . ARG   D 1 76  ? 19.198 61.026  40.2   1   41.48  ? 98  ARG   D NH2 1 
ATOM   8805  N  N   . LEU   D 1 77  ? 27.258 62.505  44.639 1   39.02  ? 99  LEU   D N   1 
ATOM   8806  C  CA  . LEU   D 1 77  ? 28.227 62.955  45.644 1   39.19  ? 99  LEU   D CA  1 
ATOM   8807  C  C   . LEU   D 1 77  ? 29.458 63.506  44.954 1   38.76  ? 99  LEU   D C   1 
ATOM   8808  O  O   . LEU   D 1 77  ? 29.97  64.54   45.363 1   39.05  ? 99  LEU   D O   1 
ATOM   8809  C  CB  . LEU   D 1 77  ? 28.637 61.817  46.59  1   39.97  ? 99  LEU   D CB  1 
ATOM   8810  C  CG  . LEU   D 1 77  ? 27.632 61.437  47.67  1   41.58  ? 99  LEU   D CG  1 
ATOM   8811  C  CD1 . LEU   D 1 77  ? 28.098 60.202  48.429 1   42.31  ? 99  LEU   D CD1 1 
ATOM   8812  C  CD2 . LEU   D 1 77  ? 27.4   62.595  48.62  1   42.07  ? 99  LEU   D CD2 1 
ATOM   8813  N  N   . ASN   D 1 78  ? 29.903 62.847  43.877 1   38.14  ? 100 ASN   D N   1 
ATOM   8814  C  CA  . ASN   D 1 78  ? 31.059 63.277  43.107 1   37.78  ? 100 ASN   D CA  1 
ATOM   8815  C  C   . ASN   D 1 78  ? 30.792 64.589  42.383 1   37.65  ? 100 ASN   D C   1 
ATOM   8816  O  O   . ASN   D 1 78  ? 31.686 65.422  42.256 1   37.86  ? 100 ASN   D O   1 
ATOM   8817  C  CB  . ASN   D 1 78  ? 31.467 62.182  42.151 1   38.8   ? 100 ASN   D CB  1 
ATOM   8818  C  CG  . ASN   D 1 78  ? 32.748 62.48   41.424 1   41.44  ? 100 ASN   D CG  1 
ATOM   8819  O  OD1 . ASN   D 1 78  ? 32.73  63.072  40.329 1   42.58  ? 100 ASN   D OD1 1 
ATOM   8820  N  ND2 . ASN   D 1 78  ? 33.878 62.078  42.013 1   40.8   ? 100 ASN   D ND2 1 
ATOM   8821  N  N   . ARG   D 1 79  ? 29.555 64.797  41.937 1   37.38  ? 101 ARG   D N   1 
ATOM   8822  C  CA  . ARG   D 1 79  ? 29.137 66.041  41.299 1   37.07  ? 101 ARG   D CA  1 
ATOM   8823  C  C   . ARG   D 1 79  ? 29.261 67.198  42.308 1   37.25  ? 101 ARG   D C   1 
ATOM   8824  O  O   . ARG   D 1 79  ? 29.799 68.246  41.971 1   37.68  ? 101 ARG   D O   1 
ATOM   8825  C  CB  . ARG   D 1 79  ? 27.69  65.894  40.822 1   37.4   ? 101 ARG   D CB  1 
ATOM   8826  C  CG  . ARG   D 1 79  ? 27.097 67.137  40.209 1   38.59  ? 101 ARG   D CG  1 
ATOM   8827  C  CD  . ARG   D 1 79  ? 25.685 66.867  39.782 1   41.22  ? 101 ARG   D CD  1 
ATOM   8828  N  NE  . ARG   D 1 79  ? 25.637 65.839  38.747 1   44.89  ? 101 ARG   D NE  1 
ATOM   8829  C  CZ  . ARG   D 1 79  ? 24.523 65.273  38.295 1   47.91  ? 101 ARG   D CZ  1 
ATOM   8830  N  NH1 . ARG   D 1 79  ? 23.341 65.634  38.781 1   47.26  ? 101 ARG   D NH1 1 
ATOM   8831  N  NH2 . ARG   D 1 79  ? 24.581 64.346  37.35  1   48.82  ? 101 ARG   D NH2 1 
ATOM   8832  N  N   . VAL   D 1 80  ? 28.817 66.983  43.563 1   36.92  ? 102 VAL   D N   1 
ATOM   8833  C  CA  . VAL   D 1 80  ? 28.915 67.969  44.645 1   36.82  ? 102 VAL   D CA  1 
ATOM   8834  C  C   . VAL   D 1 80  ? 30.395 68.305  44.934 1   36.91  ? 102 VAL   D C   1 
ATOM   8835  O  O   . VAL   D 1 80  ? 30.726 69.46   45.172 1   36.28  ? 102 VAL   D O   1 
ATOM   8836  C  CB  . VAL   D 1 80  ? 28.148 67.486  45.911 1   37.15  ? 102 VAL   D CB  1 
ATOM   8837  C  CG1 . VAL   D 1 80  ? 28.516 68.308  47.137 1   37.42  ? 102 VAL   D CG1 1 
ATOM   8838  C  CG2 . VAL   D 1 80  ? 26.64  67.518  45.683 1   37.53  ? 102 VAL   D CG2 1 
ATOM   8839  N  N   . VAL   D 1 81  ? 31.284 67.294  44.865 1   37.36  ? 103 VAL   D N   1 
ATOM   8840  C  CA  . VAL   D 1 81  ? 32.731 67.447  45.069 1   38.09  ? 103 VAL   D CA  1 
ATOM   8841  C  C   . VAL   D 1 81  ? 33.305 68.414  44.029 1   38.77  ? 103 VAL   D C   1 
ATOM   8842  O  O   . VAL   D 1 81  ? 34.135 69.268  44.369 1   39.45  ? 103 VAL   D O   1 
ATOM   8843  C  CB  . VAL   D 1 81  ? 33.438 66.061  45.035 1   38.84  ? 103 VAL   D CB  1 
ATOM   8844  C  CG1 . VAL   D 1 81  ? 34.941 66.188  44.775 1   39.38  ? 103 VAL   D CG1 1 
ATOM   8845  C  CG2 . VAL   D 1 81  ? 33.189 65.302  46.33  1   39.15  ? 103 VAL   D CG2 1 
ATOM   8846  N  N   . LEU   D 1 82  ? 32.845 68.287  42.766 1   38.05  ? 104 LEU   D N   1 
ATOM   8847  C  CA  . LEU   D 1 82  ? 33.264 69.147  41.673 1   37.89  ? 104 LEU   D CA  1 
ATOM   8848  C  C   . LEU   D 1 82  ? 32.753 70.572  41.864 1   38.28  ? 104 LEU   D C   1 
ATOM   8849  O  O   . LEU   D 1 82  ? 33.473 71.53   41.553 1   38.47  ? 104 LEU   D O   1 
ATOM   8850  C  CB  . LEU   D 1 82  ? 32.77  68.588  40.325 1   37.83  ? 104 LEU   D CB  1 
ATOM   8851  C  CG  . LEU   D 1 82  ? 33.337 67.233  39.866 1   39.03  ? 104 LEU   D CG  1 
ATOM   8852  C  CD1 . LEU   D 1 82  ? 32.857 66.904  38.472 1   39.23  ? 104 LEU   D CD1 1 
ATOM   8853  C  CD2 . LEU   D 1 82  ? 34.863 67.194  39.915 1   39.58  ? 104 LEU   D CD2 1 
ATOM   8854  N  N   . ILE   D 1 83  ? 31.503 70.709  42.34  1   38.09  ? 105 ILE   D N   1 
ATOM   8855  C  CA  . ILE   D 1 83  ? 30.88  72.002  42.577 1   38.86  ? 105 ILE   D CA  1 
ATOM   8856  C  C   . ILE   D 1 83  ? 31.574 72.712  43.735 1   40.2   ? 105 ILE   D C   1 
ATOM   8857  O  O   . ILE   D 1 83  ? 31.784 73.927  43.681 1   40.91  ? 105 ILE   D O   1 
ATOM   8858  C  CB  . ILE   D 1 83  ? 29.371 71.815  42.842 1   39.66  ? 105 ILE   D CB  1 
ATOM   8859  C  CG1 . ILE   D 1 83  ? 28.642 71.272  41.605 1   40.05  ? 105 ILE   D CG1 1 
ATOM   8860  C  CG2 . ILE   D 1 83  ? 28.721 73.11   43.345 1   40.5   ? 105 ILE   D CG2 1 
ATOM   8861  C  CD1 . ILE   D 1 83  ? 27.227 70.851  41.878 1   40.41  ? 105 ILE   D CD1 1 
ATOM   8862  N  N   . LEU   D 1 84  ? 31.947 71.958  44.786 1   40.26  ? 106 LEU   D N   1 
ATOM   8863  C  CA  . LEU   D 1 84  ? 32.646 72.523  45.924 1   40.29  ? 106 LEU   D CA  1 
ATOM   8864  C  C   . LEU   D 1 84  ? 34.032 73.002  45.514 1   40.64  ? 106 LEU   D C   1 
ATOM   8865  O  O   . LEU   D 1 84  ? 34.396 74.108  45.902 1   41.85  ? 106 LEU   D O   1 
ATOM   8866  C  CB  . LEU   D 1 84  ? 32.711 71.542  47.093 1   40.04  ? 106 LEU   D CB  1 
ATOM   8867  C  CG  . LEU   D 1 84  ? 31.446 71.438  47.936 1   40.28  ? 106 LEU   D CG  1 
ATOM   8868  C  CD1 . LEU   D 1 84  ? 31.534 70.273  48.876 1   40.26  ? 106 LEU   D CD1 1 
ATOM   8869  C  CD2 . LEU   D 1 84  ? 31.213 72.699  48.721 1   40.6   ? 106 LEU   D CD2 1 
ATOM   8870  N  N   . LYS   D 1 85  ? 34.767 72.243  44.669 1   39.57  ? 107 LYS   D N   1 
ATOM   8871  C  CA  . LYS   D 1 85  ? 36.085 72.697  44.172 1   39.19  ? 107 LYS   D CA  1 
ATOM   8872  C  C   . LYS   D 1 85  ? 35.971 74.001  43.396 1   38.41  ? 107 LYS   D C   1 
ATOM   8873  O  O   . LYS   D 1 85  ? 36.855 74.845  43.468 1   38.61  ? 107 LYS   D O   1 
ATOM   8874  C  CB  . LYS   D 1 85  ? 36.735 71.657  43.262 1   41.07  ? 107 LYS   D CB  1 
ATOM   8875  C  CG  . LYS   D 1 85  ? 37.324 70.466  43.991 1   47.08  ? 107 LYS   D CG  1 
ATOM   8876  C  CD  . LYS   D 1 85  ? 37.975 69.522  42.996 1   53.59  ? 107 LYS   D CD  1 
ATOM   8877  C  CE  . LYS   D 1 85  ? 38.115 68.111  43.499 1   58.85  ? 107 LYS   D CE  1 
ATOM   8878  N  NZ  . LYS   D 1 85  ? 38.257 67.153  42.361 1   61.95  ? 107 LYS   D NZ  1 
ATOM   8879  N  N   . LEU   D 1 86  ? 34.888 74.156  42.653 1   37.92  ? 108 LEU   D N   1 
ATOM   8880  C  CA  . LEU   D 1 86  ? 34.608 75.343  41.864 1   38.52  ? 108 LEU   D CA  1 
ATOM   8881  C  C   . LEU   D 1 86  ? 34.39  76.538  42.785 1   38.42  ? 108 LEU   D C   1 
ATOM   8882  O  O   . LEU   D 1 86  ? 34.918 77.612  42.526 1   38.57  ? 108 LEU   D O   1 
ATOM   8883  C  CB  . LEU   D 1 86  ? 33.362 75.097  40.996 1   38.97  ? 108 LEU   D CB  1 
ATOM   8884  C  CG  . LEU   D 1 86  ? 33.114 76.107  39.9   1   41.18  ? 108 LEU   D CG  1 
ATOM   8885  C  CD1 . LEU   D 1 86  ? 33.945 75.78   38.688 1   41.82  ? 108 LEU   D CD1 1 
ATOM   8886  C  CD2 . LEU   D 1 86  ? 31.654 76.113  39.491 1   41.61  ? 108 LEU   D CD2 1 
ATOM   8887  N  N   . LEU   D 1 87  ? 33.642 76.341  43.878 1   38.08  ? 109 LEU   D N   1 
ATOM   8888  C  CA  . LEU   D 1 87  ? 33.368 77.393  44.843 1   38.22  ? 109 LEU   D CA  1 
ATOM   8889  C  C   . LEU   D 1 87  ? 34.62  77.824  45.623 1   38.24  ? 109 LEU   D C   1 
ATOM   8890  O  O   . LEU   D 1 87  ? 34.776 79.007  45.915 1   38.46  ? 109 LEU   D O   1 
ATOM   8891  C  CB  . LEU   D 1 87  ? 32.215 77.003  45.769 1   38.59  ? 109 LEU   D CB  1 
ATOM   8892  C  CG  . LEU   D 1 87  ? 30.867 76.739  45.08  1   40.22  ? 109 LEU   D CG  1 
ATOM   8893  C  CD1 . LEU   D 1 87  ? 29.816 76.357  46.091 1   41     ? 109 LEU   D CD1 1 
ATOM   8894  C  CD2 . LEU   D 1 87  ? 30.396 77.924  44.265 1   40.53  ? 109 LEU   D CD2 1 
ATOM   8895  N  N   . VAL   D 1 88  ? 35.543 76.898  45.901 1   37.71  ? 110 VAL   D N   1 
ATOM   8896  C  CA  . VAL   D 1 88  ? 36.812 77.249  46.543 1   37.48  ? 110 VAL   D CA  1 
ATOM   8897  C  C   . VAL   D 1 88  ? 37.63  78.165  45.597 1   38.27  ? 110 VAL   D C   1 
ATOM   8898  O  O   . VAL   D 1 88  ? 38.276 79.113  46.049 1   38.88  ? 110 VAL   D O   1 
ATOM   8899  C  CB  . VAL   D 1 88  ? 37.603 75.986  46.954 1   37.5   ? 110 VAL   D CB  1 
ATOM   8900  C  CG1 . VAL   D 1 88  ? 38.969 76.346  47.513 1   37.71  ? 110 VAL   D CG1 1 
ATOM   8901  C  CG2 . VAL   D 1 88  ? 36.825 75.173  47.963 1   37.91  ? 110 VAL   D CG2 1 
ATOM   8902  N  N   . ASP   D 1 89  ? 37.555 77.911  44.276 1   38.29  ? 111 ASP   D N   1 
ATOM   8903  C  CA  . ASP   D 1 89  ? 38.241 78.707  43.25  1   38.45  ? 111 ASP   D CA  1 
ATOM   8904  C  C   . ASP   D 1 89  ? 37.582 80.065  42.957 1   38.53  ? 111 ASP   D C   1 
ATOM   8905  O  O   . ASP   D 1 89  ? 38.133 80.844  42.183 1   39.1   ? 111 ASP   D O   1 
ATOM   8906  C  CB  . ASP   D 1 89  ? 38.387 77.909  41.947 1   39.85  ? 111 ASP   D CB  1 
ATOM   8907  C  CG  . ASP   D 1 89  ? 39.313 76.712  42.021 1   45.94  ? 111 ASP   D CG  1 
ATOM   8908  O  OD1 . ASP   D 1 89  ? 39.875 76.459  43.109 1   47.28  ? 111 ASP   D OD1 1 
ATOM   8909  O  OD2 . ASP   D 1 89  ? 39.465 76.011  40.989 1   49.19  ? 111 ASP   D OD2 1 
ATOM   8910  N  N   . GLN   D 1 90  ? 36.397 80.331  43.51  1   38.08  ? 112 GLN   D N   1 
ATOM   8911  C  CA  . GLN   D 1 90  ? 35.727 81.618  43.299 1   38.08  ? 112 GLN   D CA  1 
ATOM   8912  C  C   . GLN   D 1 90  ? 36.258 82.687  44.253 1   38.91  ? 112 GLN   D C   1 
ATOM   8913  O  O   . GLN   D 1 90  ? 36.113 83.878  43.969 1   39.33  ? 112 GLN   D O   1 
ATOM   8914  C  CB  . GLN   D 1 90  ? 34.196 81.496  43.394 1   38.14  ? 112 GLN   D CB  1 
ATOM   8915  C  CG  . GLN   D 1 90  ? 33.598 80.632  42.291 1   39.89  ? 112 GLN   D CG  1 
ATOM   8916  C  CD  . GLN   D 1 90  ? 32.09  80.719  42.177 1   43.06  ? 112 GLN   D CD  1 
ATOM   8917  O  OE1 . GLN   D 1 90  ? 31.419 81.46   42.895 1   45.04  ? 112 GLN   D OE1 1 
ATOM   8918  N  NE2 . GLN   D 1 90  ? 31.524 79.967  41.257 1   42.61  ? 112 GLN   D NE2 1 
ATOM   8919  N  N   . VAL   D 1 91  ? 36.853 82.279  45.393 1   39.04  ? 113 VAL   D N   1 
ATOM   8920  C  CA  . VAL   D 1 91  ? 37.427 83.211  46.353 1   39.63  ? 113 VAL   D CA  1 
ATOM   8921  C  C   . VAL   D 1 91  ? 38.546 84.073  45.714 1   40.06  ? 113 VAL   D C   1 
ATOM   8922  O  O   . VAL   D 1 91  ? 38.456 85.304  45.785 1   40.11  ? 113 VAL   D O   1 
ATOM   8923  C  CB  . VAL   D 1 91  ? 37.895 82.508  47.65  1   40.55  ? 113 VAL   D CB  1 
ATOM   8924  C  CG1 . VAL   D 1 91  ? 38.461 83.518  48.642 1   41.57  ? 113 VAL   D CG1 1 
ATOM   8925  C  CG2 . VAL   D 1 91  ? 36.77  81.704  48.277 1   40.54  ? 113 VAL   D CG2 1 
ATOM   8926  N  N   . PRO   D 1 92  ? 39.55  83.486  45.011 1   39.92  ? 114 PRO   D N   1 
ATOM   8927  C  CA  . PRO   D 1 92  ? 40.592 84.332  44.394 1   39.9   ? 114 PRO   D CA  1 
ATOM   8928  C  C   . PRO   D 1 92  ? 40.08  85.384  43.402 1   39.82  ? 114 PRO   D C   1 
ATOM   8929  O  O   . PRO   D 1 92  ? 40.77  86.385  43.17  1   39.49  ? 114 PRO   D O   1 
ATOM   8930  C  CB  . PRO   D 1 92  ? 41.527 83.323  43.73  1   40.4   ? 114 PRO   D CB  1 
ATOM   8931  C  CG  . PRO   D 1 92  ? 41.276 82.034  44.433 1   40.78  ? 114 PRO   D CG  1 
ATOM   8932  C  CD  . PRO   D 1 92  ? 39.832 82.049  44.801 1   39.32  ? 114 PRO   D CD  1 
ATOM   8933  N  N   . ILE   D 1 93  ? 38.868 85.168  42.835 1   39.38  ? 115 ILE   D N   1 
ATOM   8934  C  CA  . ILE   D 1 93  ? 38.237 86.111  41.922 1   39.56  ? 115 ILE   D CA  1 
ATOM   8935  C  C   . ILE   D 1 93  ? 37.76  87.327  42.704 1   40.04  ? 115 ILE   D C   1 
ATOM   8936  O  O   . ILE   D 1 93  ? 37.941 88.458  42.247 1   40.83  ? 115 ILE   D O   1 
ATOM   8937  C  CB  . ILE   D 1 93  ? 37.087 85.451  41.118 1   40.04  ? 115 ILE   D CB  1 
ATOM   8938  C  CG1 . ILE   D 1 93  ? 37.613 84.292  40.252 1   41.23  ? 115 ILE   D CG1 1 
ATOM   8939  C  CG2 . ILE   D 1 93  ? 36.351 86.478  40.259 1   40.13  ? 115 ILE   D CG2 1 
ATOM   8940  C  CD1 . ILE   D 1 93  ? 36.523 83.48   39.512 1   42.5   ? 115 ILE   D CD1 1 
ATOM   8941  N  N   . LEU   D 1 94  ? 37.145 87.11   43.878 1   39.61  ? 116 LEU   D N   1 
ATOM   8942  C  CA  . LEU   D 1 94  ? 36.701 88.228  44.701 1   39.99  ? 116 LEU   D CA  1 
ATOM   8943  C  C   . LEU   D 1 94  ? 37.896 88.936  45.358 1   39.8   ? 116 LEU   D C   1 
ATOM   8944  O  O   . LEU   D 1 94  ? 37.853 90.152  45.529 1   39.67  ? 116 LEU   D O   1 
ATOM   8945  C  CB  . LEU   D 1 94  ? 35.64  87.801  45.726 1   40.82  ? 116 LEU   D CB  1 
ATOM   8946  C  CG  . LEU   D 1 94  ? 34.858 88.938  46.413 1   42.49  ? 116 LEU   D CG  1 
ATOM   8947  C  CD1 . LEU   D 1 94  ? 34.216 89.872  45.387 1   42.81  ? 116 LEU   D CD1 1 
ATOM   8948  C  CD2 . LEU   D 1 94  ? 33.805 88.386  47.339 1   43.04  ? 116 LEU   D CD2 1 
ATOM   8949  N  N   . GLU   D 1 95  ? 38.984 88.187  45.661 1   39.53  ? 117 GLU   D N   1 
ATOM   8950  C  CA  . GLU   D 1 95  ? 40.227 88.739  46.199 1   39.81  ? 117 GLU   D CA  1 
ATOM   8951  C  C   . GLU   D 1 95  ? 40.894 89.75   45.25  1   40.21  ? 117 GLU   D C   1 
ATOM   8952  O  O   . GLU   D 1 95  ? 41.842 90.42   45.649 1   40.54  ? 117 GLU   D O   1 
ATOM   8953  C  CB  . GLU   D 1 95  ? 41.213 87.621  46.563 1   42.28  ? 117 GLU   D CB  1 
ATOM   8954  C  CG  . GLU   D 1 95  ? 40.778 86.805  47.758 1   48.13  ? 117 GLU   D CG  1 
ATOM   8955  C  CD  . GLU   D 1 95  ? 41.788 85.781  48.233 1   56.96  ? 117 GLU   D CD  1 
ATOM   8956  O  OE1 . GLU   D 1 95  ? 42.141 84.889  47.431 1   58.98  ? 117 GLU   D OE1 1 
ATOM   8957  O  OE2 . GLU   D 1 95  ? 42.214 85.854  49.411 1   60.26  ? 117 GLU   D OE2 1 
ATOM   8958  N  N   . THR   D 1 96  ? 40.41  89.856  44     1   40.26  ? 118 THR   D N   1 
ATOM   8959  C  CA  . THR   D 1 96  ? 40.874 90.826  42.999 1   40.72  ? 118 THR   D CA  1 
ATOM   8960  C  C   . THR   D 1 96  ? 40.465 92.264  43.387 1   41.13  ? 118 THR   D C   1 
ATOM   8961  O  O   . THR   D 1 96  ? 41.104 93.223  42.961 1   41.29  ? 118 THR   D O   1 
ATOM   8962  C  CB  . THR   D 1 96  ? 40.352 90.419  41.617 1   41.48  ? 118 THR   D CB  1 
ATOM   8963  O  OG1 . THR   D 1 96  ? 40.832 89.115  41.336 1   42.2   ? 118 THR   D OG1 1 
ATOM   8964  C  CG2 . THR   D 1 96  ? 40.857 91.301  40.524 1   42.53  ? 118 THR   D CG2 1 
ATOM   8965  N  N   . MET   D 1 97  ? 39.403 92.402  44.203 1   41.59  ? 119 MET   D N   1 
ATOM   8966  C  CA  . MET   D 1 97  ? 38.867 93.658  44.702 1   42.41  ? 119 MET   D CA  1 
ATOM   8967  C  C   . MET   D 1 97  ? 39.787 94.216  45.798 1   43.27  ? 119 MET   D C   1 
ATOM   8968  O  O   . MET   D 1 97  ? 40.268 93.453  46.629 1   43.32  ? 119 MET   D O   1 
ATOM   8969  C  CB  . MET   D 1 97  ? 37.443 93.423  45.227 1   42.56  ? 119 MET   D CB  1 
ATOM   8970  C  CG  . MET   D 1 97  ? 36.851 94.605  45.991 1   44.24  ? 119 MET   D CG  1 
ATOM   8971  S  SD  . MET   D 1 97  ? 35.126 94.331  46.486 1   44.46  ? 119 MET   D SD  1 
ATOM   8972  C  CE  . MET   D 1 97  ? 35.296 92.864  47.492 1   37.52  ? 119 MET   D CE  1 
ATOM   8973  N  N   . THR   D 1 98  ? 40.076 95.53   45.771 1   43.99  ? 120 THR   D N   1 
ATOM   8974  C  CA  . THR   D 1 98  ? 40.953 96.119  46.781 1   45.05  ? 120 THR   D CA  1 
ATOM   8975  C  C   . THR   D 1 98  ? 40.166 96.45   48.049 1   45.39  ? 120 THR   D C   1 
ATOM   8976  O  O   . THR   D 1 98  ? 38.959 96.717  47.989 1   45.52  ? 120 THR   D O   1 
ATOM   8977  C  CB  . THR   D 1 98  ? 41.777 97.292  46.227 1   46.93  ? 120 THR   D CB  1 
ATOM   8978  O  OG1 . THR   D 1 98  ? 40.975 98.459  46.103 1   48.65  ? 120 THR   D OG1 1 
ATOM   8979  C  CG2 . THR   D 1 98  ? 42.444 96.961  44.919 1   47.18  ? 120 THR   D CG2 1 
ATOM   8980  N  N   . PRO   D 1 99  ? 40.843 96.407  49.213 1   45.28  ? 121 PRO   D N   1 
ATOM   8981  C  CA  . PRO   D 1 99  ? 40.171 96.709  50.477 1   45.32  ? 121 PRO   D CA  1 
ATOM   8982  C  C   . PRO   D 1 99  ? 39.56  98.107  50.561 1   45.73  ? 121 PRO   D C   1 
ATOM   8983  O  O   . PRO   D 1 99  ? 38.575 98.299  51.26  1   46.06  ? 121 PRO   D O   1 
ATOM   8984  C  CB  . PRO   D 1 99  ? 41.296 96.535  51.504 1   46.06  ? 121 PRO   D CB  1 
ATOM   8985  C  CG  . PRO   D 1 99  ? 42.282 95.666  50.853 1   46.37  ? 121 PRO   D CG  1 
ATOM   8986  C  CD  . PRO   D 1 99  ? 42.262 96.088  49.44  1   44.91  ? 121 PRO   D CD  1 
ATOM   8987  N  N   . LEU   D 1 100 ? 40.147 99.076  49.863 1   46.11  ? 122 LEU   D N   1 
ATOM   8988  C  CA  . LEU   D 1 100 ? 39.667 100.461 49.814 1   47.06  ? 122 LEU   D CA  1 
ATOM   8989  C  C   . LEU   D 1 100 ? 38.474 100.591 48.88  1   47.89  ? 122 LEU   D C   1 
ATOM   8990  O  O   . LEU   D 1 100 ? 37.609 101.427 49.121 1   48.68  ? 122 LEU   D O   1 
ATOM   8991  C  CB  . LEU   D 1 100 ? 40.763 101.428 49.361 1   47.51  ? 122 LEU   D CB  1 
ATOM   8992  C  CG  . LEU   D 1 100 ? 42.11  101.276 50.032 1   49.38  ? 122 LEU   D CG  1 
ATOM   8993  C  CD1 . LEU   D 1 100 ? 43.029 100.311 49.219 1   50.21  ? 122 LEU   D CD1 1 
ATOM   8994  C  CD2 . LEU   D 1 100 ? 42.772 102.623 50.168 1   50.05  ? 122 LEU   D CD2 1 
ATOM   8995  N  N   . ASP   D 1 101 ? 38.42  99.784  47.809 1   47.52  ? 123 ASP   D N   1 
ATOM   8996  C  CA  . ASP   D 1 101 ? 37.271 99.753  46.923 1   47.98  ? 123 ASP   D CA  1 
ATOM   8997  C  C   . ASP   D 1 101 ? 36.109 99.13   47.703 1   47.22  ? 123 ASP   D C   1 
ATOM   8998  O  O   . ASP   D 1 101 ? 35.016 99.689  47.706 1   47.01  ? 123 ASP   D O   1 
ATOM   8999  C  CB  . ASP   D 1 101 ? 37.564 98.938  45.646 1   50.71  ? 123 ASP   D CB  1 
ATOM   9000  C  CG  . ASP   D 1 101 ? 38.341 99.702  44.585 1   56.66  ? 123 ASP   D CG  1 
ATOM   9001  O  OD1 . ASP   D 1 101 ? 38.356 100.953 44.647 1   57.29  ? 123 ASP   D OD1 1 
ATOM   9002  O  OD2 . ASP   D 1 101 ? 38.955 99.04   43.696 1   59.61  ? 123 ASP   D OD2 1 
ATOM   9003  N  N   . PHE   D 1 102 ? 36.362 98.027  48.424 1   46.76  ? 124 PHE   D N   1 
ATOM   9004  C  CA  . PHE   D 1 102 ? 35.333 97.383  49.242 1   47.2   ? 124 PHE   D CA  1 
ATOM   9005  C  C   . PHE   D 1 102 ? 34.813 98.327  50.326 1   47.99  ? 124 PHE   D C   1 
ATOM   9006  O  O   . PHE   D 1 102 ? 33.609 98.38   50.568 1   48.14  ? 124 PHE   D O   1 
ATOM   9007  C  CB  . PHE   D 1 102 ? 35.883 96.114  49.894 1   46.77  ? 124 PHE   D CB  1 
ATOM   9008  C  CG  . PHE   D 1 102 ? 34.843 95.357  50.681 1   47.06  ? 124 PHE   D CG  1 
ATOM   9009  C  CD1 . PHE   D 1 102 ? 33.639 94.996  50.101 1   47.49  ? 124 PHE   D CD1 1 
ATOM   9010  C  CD2 . PHE   D 1 102 ? 35.089 94.962  51.983 1   47.94  ? 124 PHE   D CD2 1 
ATOM   9011  C  CE1 . PHE   D 1 102 ? 32.686 94.289  50.82  1   47.88  ? 124 PHE   D CE1 1 
ATOM   9012  C  CE2 . PHE   D 1 102 ? 34.141 94.238  52.695 1   48.39  ? 124 PHE   D CE2 1 
ATOM   9013  C  CZ  . PHE   D 1 102 ? 32.944 93.915  52.11  1   47.85  ? 124 PHE   D CZ  1 
ATOM   9014  N  N   . MET   D 1 103 ? 35.714 99.102  50.945 1   48.13  ? 125 MET   D N   1 
ATOM   9015  C  CA  . MET   D 1 103 ? 35.374 100.059 51.99  1   48.95  ? 125 MET   D CA  1 
ATOM   9016  C  C   . MET   D 1 103 ? 34.384 101.136 51.499 1   49.94  ? 125 MET   D C   1 
ATOM   9017  O  O   . MET   D 1 103 ? 33.555 101.606 52.274 1   49.98  ? 125 MET   D O   1 
ATOM   9018  C  CB  . MET   D 1 103 ? 36.669 100.691 52.529 1   49.11  ? 125 MET   D CB  1 
ATOM   9019  C  CG  . MET   D 1 103 ? 36.52  101.459 53.814 1   50.8   ? 125 MET   D CG  1 
ATOM   9020  S  SD  . MET   D 1 103 ? 38.143 101.943 54.477 1   55.32  ? 125 MET   D SD  1 
ATOM   9021  C  CE  . MET   D 1 103 ? 38.479 100.551 55.501 1   52.88  ? 125 MET   D CE  1 
ATOM   9022  N  N   . ASP   D 1 104 ? 34.446 101.486 50.203 1   50.67  ? 126 ASP   D N   1 
ATOM   9023  C  CA  . ASP   D 1 104 ? 33.612 102.533 49.598 1   51.48  ? 126 ASP   D CA  1 
ATOM   9024  C  C   . ASP   D 1 104 ? 32.165 102.116 49.3   1   52.38  ? 126 ASP   D C   1 
ATOM   9025  O  O   . ASP   D 1 104 ? 31.36  102.975 48.942 1   52.79  ? 126 ASP   D O   1 
ATOM   9026  C  CB  . ASP   D 1 104 ? 34.28  103.111 48.34  1   52.5   ? 126 ASP   D CB  1 
ATOM   9027  C  CG  . ASP   D 1 104 ? 35.529 103.949 48.604 1   56.43  ? 126 ASP   D CG  1 
ATOM   9028  O  OD1 . ASP   D 1 104 ? 35.873 104.154 49.791 1   57.7   ? 126 ASP   D OD1 1 
ATOM   9029  O  OD2 . ASP   D 1 104 ? 36.171 104.385 47.624 1   57.74  ? 126 ASP   D OD2 1 
ATOM   9030  N  N   . PHE   D 1 105 ? 31.825 100.832 49.452 1   52.57  ? 127 PHE   D N   1 
ATOM   9031  C  CA  . PHE   D 1 105 ? 30.444 100.386 49.243 1   53.3   ? 127 PHE   D CA  1 
ATOM   9032  C  C   . PHE   D 1 105 ? 29.915 99.504  50.406 1   53.71  ? 127 PHE   D C   1 
ATOM   9033  O  O   . PHE   D 1 105 ? 28.731 99.19   50.437 1   54.28  ? 127 PHE   D O   1 
ATOM   9034  C  CB  . PHE   D 1 105 ? 30.237 99.721  47.866 1   53.5   ? 127 PHE   D CB  1 
ATOM   9035  C  CG  . PHE   D 1 105 ? 30.769 98.32   47.664 1   54.45  ? 127 PHE   D CG  1 
ATOM   9036  C  CD1 . PHE   D 1 105 ? 29.988 97.215  47.96  1   55.17  ? 127 PHE   D CD1 1 
ATOM   9037  C  CD2 . PHE   D 1 105 ? 32.013 98.109  47.099 1   55.39  ? 127 PHE   D CD2 1 
ATOM   9038  C  CE1 . PHE   D 1 105 ? 30.467 95.934  47.752 1   55.91  ? 127 PHE   D CE1 1 
ATOM   9039  C  CE2 . PHE   D 1 105 ? 32.483 96.824  46.882 1   56.11  ? 127 PHE   D CE2 1 
ATOM   9040  C  CZ  . PHE   D 1 105 ? 31.707 95.747  47.205 1   55.82  ? 127 PHE   D CZ  1 
ATOM   9041  N  N   . ARG   D 1 106 ? 30.775 99.129  51.364 1   53.25  ? 128 ARG   D N   1 
ATOM   9042  C  CA  . ARG   D 1 106 ? 30.438 98.319  52.541 1   53.47  ? 128 ARG   D CA  1 
ATOM   9043  C  C   . ARG   D 1 106 ? 29.264 98.935  53.374 1   53.36  ? 128 ARG   D C   1 
ATOM   9044  O  O   . ARG   D 1 106 ? 28.536 98.217  54.074 1   53.06  ? 128 ARG   D O   1 
ATOM   9045  C  CB  . ARG   D 1 106 ? 31.712 98.186  53.398 1   54.87  ? 128 ARG   D CB  1 
ATOM   9046  C  CG  . ARG   D 1 106 ? 31.63  97.222  54.558 1   58.58  ? 128 ARG   D CG  1 
ATOM   9047  C  CD  . ARG   D 1 106 ? 33.018 96.789  55.01  1   61.53  ? 128 ARG   D CD  1 
ATOM   9048  N  NE  . ARG   D 1 106 ? 33.827 97.883  55.559 1   63.42  ? 128 ARG   D NE  1 
ATOM   9049  C  CZ  . ARG   D 1 106 ? 33.91  98.181  56.857 1   65.31  ? 128 ARG   D CZ  1 
ATOM   9050  N  NH1 . ARG   D 1 106 ? 33.211 97.489  57.754 1   63.55  ? 128 ARG   D NH1 1 
ATOM   9051  N  NH2 . ARG   D 1 106 ? 34.678 99.187  57.267 1   65.24  ? 128 ARG   D NH2 1 
ATOM   9052  N  N   . LYS   D 1 107 ? 29.092 100.269 53.269 1   53.02  ? 129 LYS   D N   1 
ATOM   9053  C  CA  . LYS   D 1 107 ? 28.078 101.068 53.951 1   52.95  ? 129 LYS   D CA  1 
ATOM   9054  C  C   . LYS   D 1 107 ? 26.674 100.591 53.627 1   52.55  ? 129 LYS   D C   1 
ATOM   9055  O  O   . LYS   D 1 107 ? 25.809 100.608 54.495 1   52.69  ? 129 LYS   D O   1 
ATOM   9056  C  CB  . LYS   D 1 107 ? 28.199 102.544 53.532 1   54.93  ? 129 LYS   D CB  1 
ATOM   9057  C  CG  . LYS   D 1 107 ? 29.611 103.113 53.622 1   59.57  ? 129 LYS   D CG  1 
ATOM   9058  C  CD  . LYS   D 1 107 ? 30.365 103.037 52.291 1   63.69  ? 129 LYS   D CD  1 
ATOM   9059  C  CE  . LYS   D 1 107 ? 31.393 104.132 52.17  1   67.22  ? 129 LYS   D CE  1 
ATOM   9060  N  NZ  . LYS   D 1 107 ? 30.934 105.221 51.261 1   69.08  ? 129 LYS   D NZ  1 
ATOM   9061  N  N   . TYR   D 1 108 ? 26.445 100.175 52.381 1   52.02  ? 130 TYR   D N   1 
ATOM   9062  C  CA  . TYR   D 1 108 ? 25.134 99.728  51.91  1   52.12  ? 130 TYR   D CA  1 
ATOM   9063  C  C   . TYR   D 1 108 ? 24.78  98.279  52.294 1   52.5   ? 130 TYR   D C   1 
ATOM   9064  O  O   . TYR   D 1 108 ? 23.684 97.816  51.967 1   53.29  ? 130 TYR   D O   1 
ATOM   9065  C  CB  . TYR   D 1 108 ? 25.023 99.911  50.39  1   52.01  ? 130 TYR   D CB  1 
ATOM   9066  C  CG  . TYR   D 1 108 ? 25.464 101.266 49.874 1   52.83  ? 130 TYR   D CG  1 
ATOM   9067  C  CD1 . TYR   D 1 108 ? 24.607 102.355 49.904 1   53.89  ? 130 TYR   D CD1 1 
ATOM   9068  C  CD2 . TYR   D 1 108 ? 26.717 101.44  49.302 1   53.84  ? 130 TYR   D CD2 1 
ATOM   9069  C  CE1 . TYR   D 1 108 ? 24.991 103.591 49.395 1   55.08  ? 130 TYR   D CE1 1 
ATOM   9070  C  CE2 . TYR   D 1 108 ? 27.12  102.672 48.805 1   55.12  ? 130 TYR   D CE2 1 
ATOM   9071  C  CZ  . TYR   D 1 108 ? 26.254 103.749 48.853 1   56.48  ? 130 TYR   D CZ  1 
ATOM   9072  O  OH  . TYR   D 1 108 ? 26.647 104.968 48.349 1   58.54  ? 130 TYR   D OH  1 
ATOM   9073  N  N   . LEU   D 1 109 ? 25.689 97.57   52.991 1   51.67  ? 131 LEU   D N   1 
ATOM   9074  C  CA  . LEU   D 1 109 ? 25.504 96.178  53.405 1   51.18  ? 131 LEU   D CA  1 
ATOM   9075  C  C   . LEU   D 1 109 ? 24.831 96.043  54.786 1   51.25  ? 131 LEU   D C   1 
ATOM   9076  O  O   . LEU   D 1 109 ? 25.294 96.603  55.781 1   51.33  ? 131 LEU   D O   1 
ATOM   9077  C  CB  . LEU   D 1 109 ? 26.873 95.453  53.38  1   50.82  ? 131 LEU   D CB  1 
ATOM   9078  C  CG  . LEU   D 1 109 ? 27.379 94.761  52.067 1   51.36  ? 131 LEU   D CG  1 
ATOM   9079  C  CD1 . LEU   D 1 109 ? 26.763 95.323  50.784 1   51.27  ? 131 LEU   D CD1 1 
ATOM   9080  C  CD2 . LEU   D 1 109 ? 28.89  94.787  51.989 1   51.69  ? 131 LEU   D CD2 1 
ATOM   9081  N  N   . GLN   D 1 116 ? 23.972 84.269  58.026 1   50.37  ? 138 GLN   D N   1 
ATOM   9082  C  CA  . GLN   D 1 116 ? 24.273 85.019  56.803 1   51.2   ? 138 GLN   D CA  1 
ATOM   9083  C  C   . GLN   D 1 116 ? 23.364 84.562  55.592 1   51.38  ? 138 GLN   D C   1 
ATOM   9084  O  O   . GLN   D 1 116 ? 22.327 85.198  55.302 1   51.76  ? 138 GLN   D O   1 
ATOM   9085  C  CB  . GLN   D 1 116 ? 25.798 84.967  56.475 1   52.59  ? 138 GLN   D CB  1 
ATOM   9086  C  CG  . GLN   D 1 116 ? 26.212 85.955  55.4   1   55.77  ? 138 GLN   D CG  1 
ATOM   9087  C  CD  . GLN   D 1 116 ? 26.222 87.351  55.967 1   61.72  ? 138 GLN   D CD  1 
ATOM   9088  O  OE1 . GLN   D 1 116 ? 25.296 88.15   55.773 1   63.94  ? 138 GLN   D OE1 1 
ATOM   9089  N  NE2 . GLN   D 1 116 ? 27.263 87.665  56.714 1   62.63  ? 138 GLN   D NE2 1 
ATOM   9090  N  N   . SER   D 1 117 ? 23.742 83.435  54.932 1   50.13  ? 139 SER   D N   1 
ATOM   9091  C  CA  . SER   D 1 117 ? 23.041 82.844  53.796 1   49.09  ? 139 SER   D CA  1 
ATOM   9092  C  C   . SER   D 1 117 ? 22.118 81.742  54.283 1   48.06  ? 139 SER   D C   1 
ATOM   9093  O  O   . SER   D 1 117 ? 22.573 80.853  55.011 1   48.32  ? 139 SER   D O   1 
ATOM   9094  C  CB  . SER   D 1 117 ? 24.06  82.249  52.82  1   49.87  ? 139 SER   D CB  1 
ATOM   9095  O  OG  . SER   D 1 117 ? 23.488 81.37   51.865 1   51.83  ? 139 SER   D OG  1 
ATOM   9096  N  N   . LEU   D 1 118 ? 20.85  81.744  53.837 1   46.89  ? 140 LEU   D N   1 
ATOM   9097  C  CA  . LEU   D 1 118 ? 19.929 80.672  54.212 1   46.8   ? 140 LEU   D CA  1 
ATOM   9098  C  C   . LEU   D 1 118 ? 20.404 79.353  53.597 1   47.69  ? 140 LEU   D C   1 
ATOM   9099  O  O   . LEU   D 1 118 ? 20.379 78.319  54.272 1   48.77  ? 140 LEU   D O   1 
ATOM   9100  C  CB  . LEU   D 1 118 ? 18.496 80.979  53.732 1   46.71  ? 140 LEU   D CB  1 
ATOM   9101  C  CG  . LEU   D 1 118 ? 17.485 79.818  53.816 1   47.8   ? 140 LEU   D CG  1 
ATOM   9102  C  CD1 . LEU   D 1 118 ? 17.128 79.508  55.261 1   48.36  ? 140 LEU   D CD1 1 
ATOM   9103  C  CD2 . LEU   D 1 118 ? 16.26  80.073  52.966 1   47.9   ? 140 LEU   D CD2 1 
ATOM   9104  N  N   . GLN   D 1 119 ? 20.836 79.4    52.312 1   46.78  ? 141 GLN   D N   1 
ATOM   9105  C  CA  . GLN   D 1 119 ? 21.267 78.22   51.59  1   46.19  ? 141 GLN   D CA  1 
ATOM   9106  C  C   . GLN   D 1 119 ? 22.505 77.592  52.155 1   45.98  ? 141 GLN   D C   1 
ATOM   9107  O  O   . GLN   D 1 119 ? 22.545 76.369  52.22  1   45.74  ? 141 GLN   D O   1 
ATOM   9108  C  CB  . GLN   D 1 119 ? 21.406 78.502  50.093 1   46.8   ? 141 GLN   D CB  1 
ATOM   9109  C  CG  . GLN   D 1 119 ? 20.039 78.591  49.45  1   47.59  ? 141 GLN   D CG  1 
ATOM   9110  C  CD  . GLN   D 1 119 ? 20.056 78.502  47.954 1   47.85  ? 141 GLN   D CD  1 
ATOM   9111  O  OE1 . GLN   D 1 119 ? 20.849 79.15   47.275 1   46.47  ? 141 GLN   D OE1 1 
ATOM   9112  N  NE2 . GLN   D 1 119 ? 19.133 77.718  47.414 1   48.32  ? 141 GLN   D NE2 1 
ATOM   9113  N  N   . PHE   D 1 120 ? 23.488 78.391  52.611 1   46.42  ? 142 PHE   D N   1 
ATOM   9114  C  CA  . PHE   D 1 120 ? 24.704 77.827  53.207 1   47.62  ? 142 PHE   D CA  1 
ATOM   9115  C  C   . PHE   D 1 120 ? 24.375 77.054  54.495 1   48.01  ? 142 PHE   D C   1 
ATOM   9116  O  O   . PHE   D 1 120 ? 24.958 75.991  54.751 1   47.53  ? 142 PHE   D O   1 
ATOM   9117  C  CB  . PHE   D 1 120 ? 25.737 78.916  53.508 1   48.24  ? 142 PHE   D CB  1 
ATOM   9118  C  CG  . PHE   D 1 120 ? 27.032 78.357  54.058 1   49.55  ? 142 PHE   D CG  1 
ATOM   9119  C  CD1 . PHE   D 1 120 ? 27.953 77.748  53.221 1   50.64  ? 142 PHE   D CD1 1 
ATOM   9120  C  CD2 . PHE   D 1 120 ? 27.327 78.44   55.41  1   50.2   ? 142 PHE   D CD2 1 
ATOM   9121  C  CE1 . PHE   D 1 120 ? 29.14  77.228  53.725 1   51.26  ? 142 PHE   D CE1 1 
ATOM   9122  C  CE2 . PHE   D 1 120 ? 28.521 77.932  55.906 1   50.99  ? 142 PHE   D CE2 1 
ATOM   9123  C  CZ  . PHE   D 1 120 ? 29.416 77.322  55.062 1   50.98  ? 142 PHE   D CZ  1 
ATOM   9124  N  N   . ARG   D 1 121 ? 23.437 77.599  55.298 1   48.29  ? 143 ARG   D N   1 
ATOM   9125  C  CA  . ARG   D 1 121 ? 22.998 76.966  56.539 1   48.85  ? 143 ARG   D CA  1 
ATOM   9126  C  C   . ARG   D 1 121 ? 22.224 75.684  56.234 1   48.25  ? 143 ARG   D C   1 
ATOM   9127  O  O   . ARG   D 1 121 ? 22.419 74.684  56.918 1   48.5   ? 143 ARG   D O   1 
ATOM   9128  C  CB  . ARG   D 1 121 ? 22.166 77.934  57.391 1   51.16  ? 143 ARG   D CB  1 
ATOM   9129  C  CG  . ARG   D 1 121 ? 22.953 78.591  58.514 1   55.98  ? 143 ARG   D CG  1 
ATOM   9130  C  CD  . ARG   D 1 121 ? 23.29  77.625  59.653 1   61.92  ? 143 ARG   D CD  1 
ATOM   9131  N  NE  . ARG   D 1 121 ? 22.11  77.069  60.334 1   67.49  ? 143 ARG   D NE  1 
ATOM   9132  C  CZ  . ARG   D 1 121 ? 21.751 77.358  61.587 1   70.59  ? 143 ARG   D CZ  1 
ATOM   9133  N  NH1 . ARG   D 1 121 ? 22.466 78.217  62.308 1   70.81  ? 143 ARG   D NH1 1 
ATOM   9134  N  NH2 . ARG   D 1 121 ? 20.676 76.785  62.128 1   69.79  ? 143 ARG   D NH2 1 
ATOM   9135  N  N   . LEU   D 1 122 ? 21.397 75.684  55.183 1   47.43  ? 144 LEU   D N   1 
ATOM   9136  C  CA  . LEU   D 1 122 ? 20.673 74.476  54.79  1   47.48  ? 144 LEU   D CA  1 
ATOM   9137  C  C   . LEU   D 1 122 ? 21.644 73.354  54.398 1   48.95  ? 144 LEU   D C   1 
ATOM   9138  O  O   . LEU   D 1 122 ? 21.381 72.201  54.716 1   49.64  ? 144 LEU   D O   1 
ATOM   9139  C  CB  . LEU   D 1 122 ? 19.704 74.748  53.648 1   46.57  ? 144 LEU   D CB  1 
ATOM   9140  C  CG  . LEU   D 1 122 ? 18.492 75.581  53.975 1   46.77  ? 144 LEU   D CG  1 
ATOM   9141  C  CD1 . LEU   D 1 122 ? 17.656 75.793  52.735 1   47.29  ? 144 LEU   D CD1 1 
ATOM   9142  C  CD2 . LEU   D 1 122 ? 17.662 74.942  55.059 1   46.47  ? 144 LEU   D CD2 1 
ATOM   9143  N  N   . ILE   D 1 123 ? 22.781 73.693  53.752 1   48.7   ? 145 ILE   D N   1 
ATOM   9144  C  CA  . ILE   D 1 123 ? 23.808 72.719  53.385 1   48.71  ? 145 ILE   D CA  1 
ATOM   9145  C  C   . ILE   D 1 123 ? 24.465 72.156  54.647 1   48.88  ? 145 ILE   D C   1 
ATOM   9146  O  O   . ILE   D 1 123 ? 24.532 70.94   54.803 1   49.15  ? 145 ILE   D O   1 
ATOM   9147  C  CB  . ILE   D 1 123 ? 24.845 73.347  52.423 1   49.06  ? 145 ILE   D CB  1 
ATOM   9148  C  CG1 . ILE   D 1 123 ? 24.194 73.658  51.058 1   49.55  ? 145 ILE   D CG1 1 
ATOM   9149  C  CG2 . ILE   D 1 123 ? 26.067 72.435  52.252 1   49.47  ? 145 ILE   D CG2 1 
ATOM   9150  C  CD1 . ILE   D 1 123 ? 25.03  74.472  50.136 1   50.44  ? 145 ILE   D CD1 1 
ATOM   9151  N  N   . GLU   D 1 124 ? 24.902 73.037  55.574 1   48.67  ? 146 GLU   D N   1 
ATOM   9152  C  CA  . GLU   D 1 124 ? 25.512 72.65   56.852 1   48.72  ? 146 GLU   D CA  1 
ATOM   9153  C  C   . GLU   D 1 124 ? 24.596 71.683  57.615 1   49.78  ? 146 GLU   D C   1 
ATOM   9154  O  O   . GLU   D 1 124 ? 25.038 70.615  58.024 1   50.2   ? 146 GLU   D O   1 
ATOM   9155  C  CB  . GLU   D 1 124 ? 25.759 73.891  57.717 1   50.16  ? 146 GLU   D CB  1 
ATOM   9156  C  CG  . GLU   D 1 124 ? 27.004 74.672  57.368 1   54.82  ? 146 GLU   D CG  1 
ATOM   9157  C  CD  . GLU   D 1 124 ? 27.282 75.843  58.293 1   60.01  ? 146 GLU   D CD  1 
ATOM   9158  O  OE1 . GLU   D 1 124 ? 26.354 76.642  58.555 1   60.97  ? 146 GLU   D OE1 1 
ATOM   9159  O  OE2 . GLU   D 1 124 ? 28.446 75.978  58.735 1   61.74  ? 146 GLU   D OE2 1 
ATOM   9160  N  N   . ASN   D 1 125 ? 23.296 72.024  57.722 1   50     ? 147 ASN   D N   1 
ATOM   9161  C  CA  . ASN   D 1 125 ? 22.299 71.211  58.416 1   50.24  ? 147 ASN   D CA  1 
ATOM   9162  C  C   . ASN   D 1 125 ? 21.996 69.889  57.712 1   50.59  ? 147 ASN   D C   1 
ATOM   9163  O  O   . ASN   D 1 125 ? 21.981 68.848  58.375 1   51.22  ? 147 ASN   D O   1 
ATOM   9164  C  CB  . ASN   D 1 125 ? 21.016 72.005  58.645 1   50.55  ? 147 ASN   D CB  1 
ATOM   9165  C  CG  . ASN   D 1 125 ? 21.161 73.133  59.636 1   52.23  ? 147 ASN   D CG  1 
ATOM   9166  O  OD1 . ASN   D 1 125 ? 22.111 73.189  60.429 1   52.91  ? 147 ASN   D OD1 1 
ATOM   9167  N  ND2 . ASN   D 1 125 ? 20.213 74.055  59.613 1   52.1   ? 147 ASN   D ND2 1 
ATOM   9168  N  N   . LYS   D 1 126 ? 21.771 69.918  56.38  1   49.97  ? 148 LYS   D N   1 
ATOM   9169  C  CA  . LYS   D 1 126 ? 21.482 68.698  55.615 1   49.43  ? 148 LYS   D CA  1 
ATOM   9170  C  C   . LYS   D 1 126 ? 22.673 67.736  55.575 1   49.99  ? 148 LYS   D C   1 
ATOM   9171  O  O   . LYS   D 1 126 ? 22.466 66.533  55.527 1   49.99  ? 148 LYS   D O   1 
ATOM   9172  C  CB  . LYS   D 1 126 ? 20.967 69.013  54.21  1   48.95  ? 148 LYS   D CB  1 
ATOM   9173  C  CG  . LYS   D 1 126 ? 19.571 69.619  54.177 1   50.05  ? 148 LYS   D CG  1 
ATOM   9174  C  CD  . LYS   D 1 126 ? 19.324 70.36   52.871 1   51.29  ? 148 LYS   D CD  1 
ATOM   9175  C  CE  . LYS   D 1 126 ? 18.028 71.114  52.876 1   52.85  ? 148 LYS   D CE  1 
ATOM   9176  N  NZ  . LYS   D 1 126 ? 16.881 70.187  52.819 1   54.32  ? 148 LYS   D NZ  1 
ATOM   9177  N  N   . LEU   D 1 127 ? 23.909 68.255  55.609 1   50.54  ? 149 LEU   D N   1 
ATOM   9178  C  CA  . LEU   D 1 127 ? 25.09  67.403  55.646 1   51.66  ? 149 LEU   D CA  1 
ATOM   9179  C  C   . LEU   D 1 127 ? 25.166 66.755  57.028 1   54.23  ? 149 LEU   D C   1 
ATOM   9180  O  O   . LEU   D 1 127 ? 25.363 65.545  57.128 1   54.45  ? 149 LEU   D O   1 
ATOM   9181  C  CB  . LEU   D 1 127 ? 26.365 68.205  55.341 1   51.28  ? 149 LEU   D CB  1 
ATOM   9182  C  CG  . LEU   D 1 127 ? 27.652 67.387  55.237 1   51.77  ? 149 LEU   D CG  1 
ATOM   9183  C  CD1 . LEU   D 1 127 ? 27.592 66.412  54.092 1   52.06  ? 149 LEU   D CD1 1 
ATOM   9184  C  CD2 . LEU   D 1 127 ? 28.843 68.275  55.058 1   51.82  ? 149 LEU   D CD2 1 
ATOM   9185  N  N   . GLY   D 1 128 ? 24.957 67.545  58.079 1   56.25  ? 150 GLY   D N   1 
ATOM   9186  C  CA  . GLY   D 1 128 ? 24.947 67.014  59.429 1   59.1   ? 150 GLY   D CA  1 
ATOM   9187  C  C   . GLY   D 1 128 ? 25.71  67.801  60.465 1   62.23  ? 150 GLY   D C   1 
ATOM   9188  O  O   . GLY   D 1 128 ? 26.056 67.247  61.507 1   62.18  ? 150 GLY   D O   1 
ATOM   9189  N  N   . VAL   D 1 129 ? 25.96  69.101  60.221 1   64.69  ? 151 VAL   D N   1 
ATOM   9190  C  CA  . VAL   D 1 129 ? 26.642 69.955  61.203 1   67.33  ? 151 VAL   D CA  1 
ATOM   9191  C  C   . VAL   D 1 129 ? 25.707 70.088  62.404 1   69.86  ? 151 VAL   D C   1 
ATOM   9192  O  O   . VAL   D 1 129 ? 24.586 70.581  62.259 1   69.49  ? 151 VAL   D O   1 
ATOM   9193  C  CB  . VAL   D 1 129 ? 27.056 71.331  60.622 1   68.14  ? 151 VAL   D CB  1 
ATOM   9194  C  CG1 . VAL   D 1 129 ? 27.605 72.245  61.712 1   68.58  ? 151 VAL   D CG1 1 
ATOM   9195  C  CG2 . VAL   D 1 129 ? 28.083 71.16   59.51  1   68.78  ? 151 VAL   D CG2 1 
ATOM   9196  N  N   . LEU   D 1 130 ? 26.111 69.475  63.533 1   72.11  ? 152 LEU   D N   1 
ATOM   9197  C  CA  . LEU   D 1 130 ? 25.296 69.409  64.751 1   74.47  ? 152 LEU   D CA  1 
ATOM   9198  C  C   . LEU   D 1 130 ? 25.062 70.781  65.341 1   76.26  ? 152 LEU   D C   1 
ATOM   9199  O  O   . LEU   D 1 130 ? 26.02  71.519  65.582 1   76.62  ? 152 LEU   D O   1 
ATOM   9200  C  CB  . LEU   D 1 130 ? 25.916 68.46   65.788 1   75.04  ? 152 LEU   D CB  1 
ATOM   9201  C  CG  . LEU   D 1 130 ? 26.089 67.013  65.329 1   76.97  ? 152 LEU   D CG  1 
ATOM   9202  C  CD1 . LEU   D 1 130 ? 27.556 66.694  65.051 1   77.85  ? 152 LEU   D CD1 1 
ATOM   9203  C  CD2 . LEU   D 1 130 ? 25.545 66.046  66.357 1   77.49  ? 152 LEU   D CD2 1 
ATOM   9204  N  N   . THR   D 1 131 ? 23.784 71.13   65.556 1   77.18  ? 153 THR   D N   1 
ATOM   9205  C  CA  . THR   D 1 131 ? 23.349 72.434  66.076 1   78.47  ? 153 THR   D CA  1 
ATOM   9206  C  C   . THR   D 1 131 ? 24.049 72.81   67.415 1   79.67  ? 153 THR   D C   1 
ATOM   9207  O  O   . THR   D 1 131 ? 24.36  73.983  67.631 1   80.08  ? 153 THR   D O   1 
ATOM   9208  C  CB  . THR   D 1 131 ? 21.811 72.47   66.141 1   79.32  ? 153 THR   D CB  1 
ATOM   9209  O  OG1 . THR   D 1 131 ? 21.295 72.126  64.846 1   79.93  ? 153 THR   D OG1 1 
ATOM   9210  C  CG2 . THR   D 1 131 ? 21.268 73.827  66.582 1   79.58  ? 153 THR   D CG2 1 
ATOM   9211  N  N   . GLU   D 1 132 ? 24.389 71.807  68.251 1   79.94  ? 154 GLU   D N   1 
ATOM   9212  C  CA  . GLU   D 1 132 ? 25.083 72.028  69.522 1   80.44  ? 154 GLU   D CA  1 
ATOM   9213  C  C   . GLU   D 1 132 ? 26.6   72.292  69.368 1   80.78  ? 154 GLU   D C   1 
ATOM   9214  O  O   . GLU   D 1 132 ? 27.298 72.425  70.369 1   80.98  ? 154 GLU   D O   1 
ATOM   9215  C  CB  . GLU   D 1 132 ? 24.809 70.87   70.502 1   82.36  ? 154 GLU   D CB  1 
ATOM   9216  C  CG  . GLU   D 1 132 ? 25.239 69.505  69.991 1   85.63  ? 154 GLU   D CG  1 
ATOM   9217  C  CD  . GLU   D 1 132 ? 24.151 68.68   69.332 1   89.39  ? 154 GLU   D CD  1 
ATOM   9218  O  OE1 . GLU   D 1 132 ? 24.32  67.442  69.25  1   90.18  ? 154 GLU   D OE1 1 
ATOM   9219  O  OE2 . GLU   D 1 132 ? 23.131 69.265  68.9   1   90.27  ? 154 GLU   D OE2 1 
ATOM   9220  N  N   . GLN   D 1 133 ? 27.105 72.39   68.132 1   80.77  ? 155 GLN   D N   1 
ATOM   9221  C  CA  . GLN   D 1 133 ? 28.517 72.69   67.876 1   81.25  ? 155 GLN   D CA  1 
ATOM   9222  C  C   . GLN   D 1 133 ? 28.719 74.13   67.389 1   81.23  ? 155 GLN   D C   1 
ATOM   9223  O  O   . GLN   D 1 133 ? 29.823 74.652  67.487 1   81.26  ? 155 GLN   D O   1 
ATOM   9224  C  CB  . GLN   D 1 133 ? 29.111 71.725  66.841 1   83.14  ? 155 GLN   D CB  1 
ATOM   9225  C  CG  . GLN   D 1 133 ? 28.816 70.261  67.102 1   86.98  ? 155 GLN   D CG  1 
ATOM   9226  C  CD  . GLN   D 1 133 ? 29.385 69.783  68.414 1   92.49  ? 155 GLN   D CD  1 
ATOM   9227  O  OE1 . GLN   D 1 133 ? 28.687 69.162  69.221 1   94.65  ? 155 GLN   D OE1 1 
ATOM   9228  N  NE2 . GLN   D 1 133 ? 30.665 70.052  68.665 1   93.08  ? 155 GLN   D NE2 1 
ATOM   9229  N  N   . ARG   D 1 134 ? 27.676 74.754  66.827 1   81.14  ? 156 ARG   D N   1 
ATOM   9230  C  CA  . ARG   D 1 134 ? 27.779 76.114  66.327 1   81.65  ? 156 ARG   D CA  1 
ATOM   9231  C  C   . ARG   D 1 134 ? 28.194 77.107  67.423 1   81.9   ? 156 ARG   D C   1 
ATOM   9232  O  O   . ARG   D 1 134 ? 27.531 77.202  68.46  1   82.08  ? 156 ARG   D O   1 
ATOM   9233  C  CB  . ARG   D 1 134 ? 26.471 76.54   65.674 1   81.76  ? 156 ARG   D CB  1 
ATOM   9234  N  N   . VAL   D 1 135 ? 29.332 77.794  67.214 1   81.61  ? 157 VAL   D N   1 
ATOM   9235  C  CA  . VAL   D 1 135 ? 29.828 78.809  68.14  1   81.78  ? 157 VAL   D CA  1 
ATOM   9236  C  C   . VAL   D 1 135 ? 28.909 80.054  68.069 1   82.14  ? 157 VAL   D C   1 
ATOM   9237  O  O   . VAL   D 1 135 ? 28.301 80.308  67.023 1   82.51  ? 157 VAL   D O   1 
ATOM   9238  C  CB  . VAL   D 1 135 ? 31.259 79.184  67.779 1   81.65  ? 157 VAL   D CB  1 
ATOM   9239  N  N   . ARG   D 1 136 ? 28.767 80.804  69.177 1   81.75  ? 158 ARG   D N   1 
ATOM   9240  C  CA  . ARG   D 1 136 ? 27.906 81.993  69.184 1   81.68  ? 158 ARG   D CA  1 
ATOM   9241  C  C   . ARG   D 1 136 ? 28.653 83.222  68.682 1   81.31  ? 158 ARG   D C   1 
ATOM   9242  O  O   . ARG   D 1 136 ? 28.087 84.033  67.958 1   81.11  ? 158 ARG   D O   1 
ATOM   9243  C  CB  . ARG   D 1 136 ? 27.358 82.246  70.581 1   81.86  ? 158 ARG   D CB  1 
ATOM   9244  N  N   . VAL   D 1 144 ? 17.41  83.811  64.169 1   94.97  ? 166 VAL   D N   1 
ATOM   9245  C  CA  . VAL   D 1 144 ? 18.52  84.311  63.362 1   95.51  ? 166 VAL   D CA  1 
ATOM   9246  C  C   . VAL   D 1 144 ? 18.051 84.87   61.998 1   95.6   ? 166 VAL   D C   1 
ATOM   9247  O  O   . VAL   D 1 144 ? 18.688 85.773  61.451 1   95.6   ? 166 VAL   D O   1 
ATOM   9248  C  CB  . VAL   D 1 144 ? 19.553 83.21   63.162 1   95.79  ? 166 VAL   D CB  1 
ATOM   9249  N  N   . PHE   D 1 145 ? 16.942 84.331  61.458 1   95.31  ? 167 PHE   D N   1 
ATOM   9250  C  CA  . PHE   D 1 145 ? 16.361 84.749  60.181 1   95.41  ? 167 PHE   D CA  1 
ATOM   9251  C  C   . PHE   D 1 145 ? 14.888 85.087  60.417 1   95.47  ? 167 PHE   D C   1 
ATOM   9252  O  O   . PHE   D 1 145 ? 14.152 84.253  60.939 1   95.7   ? 167 PHE   D O   1 
ATOM   9253  C  CB  . PHE   D 1 145 ? 16.486 83.626  59.163 1   95.57  ? 167 PHE   D CB  1 
ATOM   9254  N  N   . SER   D 1 146 ? 14.453 86.294  60.035 1   95.07  ? 168 SER   D N   1 
ATOM   9255  C  CA  . SER   D 1 146 ? 13.089 86.759  60.29  1   95.22  ? 168 SER   D CA  1 
ATOM   9256  C  C   . SER   D 1 146 ? 11.964 86.165  59.408 1   95.18  ? 168 SER   D C   1 
ATOM   9257  O  O   . SER   D 1 146 ? 10.824 86.126  59.863 1   95.35  ? 168 SER   D O   1 
ATOM   9258  C  CB  . SER   D 1 146 ? 13.044 88.275  60.213 1   95.4   ? 168 SER   D CB  1 
ATOM   9259  N  N   . ASP   D 1 147 ? 12.253 85.747  58.166 1   94.78  ? 169 ASP   D N   1 
ATOM   9260  C  CA  . ASP   D 1 147 ? 11.228 85.226  57.252 1   94.76  ? 169 ASP   D CA  1 
ATOM   9261  C  C   . ASP   D 1 147 ? 10.594 83.906  57.708 1   94.77  ? 169 ASP   D C   1 
ATOM   9262  O  O   . ASP   D 1 147 ? 11.294 83.05   58.246 1   95.06  ? 169 ASP   D O   1 
ATOM   9263  C  CB  . ASP   D 1 147 ? 11.798 85.087  55.837 1   96.03  ? 169 ASP   D CB  1 
ATOM   9264  N  N   . GLU   D 1 148 ? 9.274  83.736  57.5   1   94.33  ? 170 GLU   D N   1 
ATOM   9265  C  CA  . GLU   D 1 148 ? 8.61   82.495  57.921 1   94.36  ? 170 GLU   D CA  1 
ATOM   9266  C  C   . GLU   D 1 148 ? 8.872  81.331  56.969 1   93.74  ? 170 GLU   D C   1 
ATOM   9267  O  O   . GLU   D 1 148 ? 8.818  80.179  57.397 1   93.85  ? 170 GLU   D O   1 
ATOM   9268  C  CB  . GLU   D 1 148 ? 7.11   82.68   58.19  1   96.9   ? 170 GLU   D CB  1 
ATOM   9269  C  CG  . GLU   D 1 148 ? 6.746  82.43   59.649 1   101.62 ? 170 GLU   D CG  1 
ATOM   9270  C  CD  . GLU   D 1 148 ? 6.036  81.121  59.952 1   107.29 ? 170 GLU   D CD  1 
ATOM   9271  O  OE1 . GLU   D 1 148 ? 4.812  81.039  59.697 1   108.81 ? 170 GLU   D OE1 1 
ATOM   9272  O  OE2 . GLU   D 1 148 ? 6.698  80.185  60.46  1   108.32 ? 170 GLU   D OE2 1 
ATOM   9273  N  N   . GLU   D 1 149 ? 9.167  81.619  55.691 1   92.91  ? 171 GLU   D N   1 
ATOM   9274  C  CA  . GLU   D 1 149 ? 9.521  80.569  54.735 1   92.45  ? 171 GLU   D CA  1 
ATOM   9275  C  C   . GLU   D 1 149 ? 10.949 80.064  55.06  1   91.05  ? 171 GLU   D C   1 
ATOM   9276  O  O   . GLU   D 1 149 ? 11.205 78.864  55.025 1   90.7   ? 171 GLU   D O   1 
ATOM   9277  C  CB  . GLU   D 1 149 ? 9.439  81.093  53.296 1   95.41  ? 171 GLU   D CB  1 
ATOM   9278  C  CG  . GLU   D 1 149 ? 9.51   79.989  52.254 1   101.68 ? 171 GLU   D CG  1 
ATOM   9279  C  CD  . GLU   D 1 149 ? 9.278  80.435  50.825 1   109.91 ? 171 GLU   D CD  1 
ATOM   9280  O  OE1 . GLU   D 1 149 ? 10.208 80.295  49.998 1   111.05 ? 171 GLU   D OE1 1 
ATOM   9281  O  OE2 . GLU   D 1 149 ? 8.161  80.92   50.528 1   113.06 ? 171 GLU   D OE2 1 
ATOM   9282  N  N   . ALA   D 1 150 ? 11.857 80.987  55.417 1   90.18  ? 172 ALA   D N   1 
ATOM   9283  C  CA  . ALA   D 1 150 ? 13.23  80.679  55.8   1   89.92  ? 172 ALA   D CA  1 
ATOM   9284  C  C   . ALA   D 1 150 ? 13.283 79.964  57.152 1   89.48  ? 172 ALA   D C   1 
ATOM   9285  O  O   . ALA   D 1 150 ? 14.138 79.099  57.352 1   89.71  ? 172 ALA   D O   1 
ATOM   9286  C  CB  . ALA   D 1 150 ? 14.05  81.957  55.863 1   90.05  ? 172 ALA   D CB  1 
ATOM   9287  N  N   . ARG   D 1 151 ? 12.377 80.321  58.081 1   88.64  ? 173 ARG   D N   1 
ATOM   9288  C  CA  . ARG   D 1 151 ? 12.331 79.686  59.397 1   88.17  ? 173 ARG   D CA  1 
ATOM   9289  C  C   . ARG   D 1 151 ? 11.867 78.231  59.262 1   87.12  ? 173 ARG   D C   1 
ATOM   9290  O  O   . ARG   D 1 151 ? 12.429 77.351  59.907 1   87.13  ? 173 ARG   D O   1 
ATOM   9291  C  CB  . ARG   D 1 151 ? 11.425 80.472  60.358 1   89.79  ? 173 ARG   D CB  1 
ATOM   9292  C  CG  . ARG   D 1 151 ? 11.83  80.335  61.823 1   93.37  ? 173 ARG   D CG  1 
ATOM   9293  C  CD  . ARG   D 1 151 ? 12.495 81.581  62.376 1   96.99  ? 173 ARG   D CD  1 
ATOM   9294  N  NE  . ARG   D 1 151 ? 11.522 82.646  62.611 1   99.77  ? 173 ARG   D NE  1 
ATOM   9295  C  CZ  . ARG   D 1 151 ? 11.799 83.8    63.212 1   101.36 ? 173 ARG   D CZ  1 
ATOM   9296  N  NH1 . ARG   D 1 151 ? 13.03  84.056  63.641 1   100.41 ? 173 ARG   D NH1 1 
ATOM   9297  N  NH2 . ARG   D 1 151 ? 10.848 84.706  63.387 1   101.4  ? 173 ARG   D NH2 1 
ATOM   9298  N  N   . ASN   D 1 152 ? 10.873 77.983  58.398 1   86.21  ? 174 ASN   D N   1 
ATOM   9299  C  CA  . ASN   D 1 152 ? 10.348 76.649  58.114 1   86.08  ? 174 ASN   D CA  1 
ATOM   9300  C  C   . ASN   D 1 152 ? 11.449 75.789  57.477 1   85.88  ? 174 ASN   D C   1 
ATOM   9301  O  O   . ASN   D 1 152 ? 11.596 74.622  57.831 1   86.19  ? 174 ASN   D O   1 
ATOM   9302  C  CB  . ASN   D 1 152 ? 9.139  76.749  57.166 1   87.02  ? 174 ASN   D CB  1 
ATOM   9303  C  CG  . ASN   D 1 152 ? 8.389  75.453  56.941 1   89.73  ? 174 ASN   D CG  1 
ATOM   9304  O  OD1 . ASN   D 1 152 ? 7.785  74.895  57.855 1   90.97  ? 174 ASN   D OD1 1 
ATOM   9305  N  ND2 . ASN   D 1 152 ? 8.382  74.958  55.713 1   89.97  ? 174 ASN   D ND2 1 
ATOM   9306  N  N   . SER   D 1 153 ? 12.234 76.375  56.557 1   85.13  ? 175 SER   D N   1 
ATOM   9307  C  CA  . SER   D 1 153 ? 13.324 75.681  55.88  1   84.68  ? 175 SER   D CA  1 
ATOM   9308  C  C   . SER   D 1 153 ? 14.38  75.197  56.874 1   83.8   ? 175 SER   D C   1 
ATOM   9309  O  O   . SER   D 1 153 ? 14.763 74.026  56.833 1   83.99  ? 175 SER   D O   1 
ATOM   9310  C  CB  . SER   D 1 153 ? 13.959 76.588  54.828 1   86.18  ? 175 SER   D CB  1 
ATOM   9311  O  OG  . SER   D 1 153 ? 13.051 76.941  53.795 1   88.76  ? 175 SER   D OG  1 
ATOM   9312  N  N   . ILE   D 1 154 ? 14.829 76.084  57.783 1   82.8   ? 176 ILE   D N   1 
ATOM   9313  C  CA  . ILE   D 1 154 ? 15.844 75.749  58.777 1   82.33  ? 176 ILE   D CA  1 
ATOM   9314  C  C   . ILE   D 1 154 ? 15.289 74.775  59.813 1   82.07  ? 176 ILE   D C   1 
ATOM   9315  O  O   . ILE   D 1 154 ? 15.993 73.843  60.198 1   82.28  ? 176 ILE   D O   1 
ATOM   9316  C  CB  . ILE   D 1 154 ? 16.501 77.02   59.369 1   82.67  ? 176 ILE   D CB  1 
ATOM   9317  C  CG1 . ILE   D 1 154 ? 17.554 77.531  58.363 1   83.73  ? 176 ILE   D CG1 1 
ATOM   9318  C  CG2 . ILE   D 1 154 ? 17.131 76.771  60.753 1   83.1   ? 176 ILE   D CG2 1 
ATOM   9319  C  CD1 . ILE   D 1 154 ? 18.388 78.72   58.76  1   85.08  ? 176 ILE   D CD1 1 
ATOM   9320  N  N   . ARG   D 1 155 ? 14.006 74.912  60.185 1   81.55  ? 177 ARG   D N   1 
ATOM   9321  C  CA  . ARG   D 1 155 ? 13.366 73.977  61.111 1   81.47  ? 177 ARG   D CA  1 
ATOM   9322  C  C   . ARG   D 1 155 ? 13.393 72.552  60.526 1   80.16  ? 177 ARG   D C   1 
ATOM   9323  O  O   . ARG   D 1 155 ? 13.915 71.647  61.171 1   80.51  ? 177 ARG   D O   1 
ATOM   9324  C  CB  . ARG   D 1 155 ? 11.917 74.406  61.408 1   83.98  ? 177 ARG   D CB  1 
ATOM   9325  C  CG  . ARG   D 1 155 ? 11.686 74.847  62.839 1   89.46  ? 177 ARG   D CG  1 
ATOM   9326  C  CD  . ARG   D 1 155 ? 11.549 73.672  63.797 1   94.65  ? 177 ARG   D CD  1 
ATOM   9327  N  NE  . ARG   D 1 155 ? 11.915 74.032  65.17  1   99.23  ? 177 ARG   D NE  1 
ATOM   9328  C  CZ  . ARG   D 1 155 ? 11.074 74.547  66.065 1   102.78 ? 177 ARG   D CZ  1 
ATOM   9329  N  NH1 . ARG   D 1 155 ? 9.803  74.764  65.745 1   102.91 ? 177 ARG   D NH1 1 
ATOM   9330  N  NH2 . ARG   D 1 155 ? 11.496 74.837  67.29  1   103.16 ? 177 ARG   D NH2 1 
ATOM   9331  N  N   . ASN   D 1 156 ? 12.933 72.387  59.27  1   78.36  ? 178 ASN   D N   1 
ATOM   9332  C  CA  . ASN   D 1 156 ? 12.901 71.095  58.587 1   77.14  ? 178 ASN   D CA  1 
ATOM   9333  C  C   . ASN   D 1 156 ? 14.282 70.49   58.383 1   75.75  ? 178 ASN   D C   1 
ATOM   9334  O  O   . ASN   D 1 156 ? 14.428 69.277  58.488 1   75.85  ? 178 ASN   D O   1 
ATOM   9335  C  CB  . ASN   D 1 156 ? 12.156 71.196  57.255 1   77.94  ? 178 ASN   D CB  1 
ATOM   9336  C  CG  . ASN   D 1 156 ? 10.696 71.536  57.397 1   80.64  ? 178 ASN   D CG  1 
ATOM   9337  O  OD1 . ASN   D 1 156 ? 10.134 71.516  58.493 1   81.84  ? 178 ASN   D OD1 1 
ATOM   9338  N  ND2 . ASN   D 1 156 ? 10.05  71.875  56.29  1   81.05  ? 178 ASN   D ND2 1 
ATOM   9339  N  N   . SER   D 1 157 ? 15.299 71.32   58.113 1   74.17  ? 179 SER   D N   1 
ATOM   9340  C  CA  . SER   D 1 157 ? 16.665 70.821  57.924 1   72.93  ? 179 SER   D CA  1 
ATOM   9341  C  C   . SER   D 1 157 ? 17.266 70.222  59.216 1   71.97  ? 179 SER   D C   1 
ATOM   9342  O  O   . SER   D 1 157 ? 18.154 69.372  59.15  1   71.94  ? 179 SER   D O   1 
ATOM   9343  C  CB  . SER   D 1 157 ? 17.563 71.921  57.367 1   73.18  ? 179 SER   D CB  1 
ATOM   9344  O  OG  . SER   D 1 157 ? 17.871 72.897  58.345 1   74.11  ? 179 SER   D OG  1 
ATOM   9345  N  N   . GLU   D 1 158 ? 16.763 70.653  60.383 1   71.1   ? 180 GLU   D N   1 
ATOM   9346  C  CA  . GLU   D 1 158 ? 17.2   70.162  61.686 1   70.56  ? 180 GLU   D CA  1 
ATOM   9347  C  C   . GLU   D 1 158 ? 16.364 68.958  62.133 1   69.63  ? 180 GLU   D C   1 
ATOM   9348  O  O   . GLU   D 1 158 ? 16.905 68.033  62.734 1   69.81  ? 180 GLU   D O   1 
ATOM   9349  C  CB  . GLU   D 1 158 ? 17.124 71.284  62.721 1   72.55  ? 180 GLU   D CB  1 
ATOM   9350  C  CG  . GLU   D 1 158 ? 18.1   72.412  62.432 1   77.34  ? 180 GLU   D CG  1 
ATOM   9351  C  CD  . GLU   D 1 158 ? 17.966 73.63   63.326 1   84.81  ? 180 GLU   D CD  1 
ATOM   9352  O  OE1 . GLU   D 1 158 ? 16.921 73.752  64.007 1   85.5   ? 180 GLU   D OE1 1 
ATOM   9353  O  OE2 . GLU   D 1 158 ? 18.901 74.467  63.34  1   87.77  ? 180 GLU   D OE2 1 
ATOM   9354  N  N   . LYS   D 1 159 ? 15.055 68.953  61.812 1   68.48  ? 181 LYS   D N   1 
ATOM   9355  C  CA  . LYS   D 1 159 ? 14.15  67.86   62.178 1   67.73  ? 181 LYS   D CA  1 
ATOM   9356  C  C   . LYS   D 1 159 ? 14.344 66.621  61.314 1   66.23  ? 181 LYS   D C   1 
ATOM   9357  O  O   . LYS   D 1 159 ? 14.465 65.521  61.843 1   66.55  ? 181 LYS   D O   1 
ATOM   9358  C  CB  . LYS   D 1 159 ? 12.672 68.313  62.136 1   70.03  ? 181 LYS   D CB  1 
ATOM   9359  C  CG  . LYS   D 1 159 ? 12.346 69.478  63.061 1   75.07  ? 181 LYS   D CG  1 
ATOM   9360  C  CD  . LYS   D 1 159 ? 12.551 69.121  64.523 1   80.15  ? 181 LYS   D CD  1 
ATOM   9361  C  CE  . LYS   D 1 159 ? 12.131 70.233  65.44  1   84.26  ? 181 LYS   D CE  1 
ATOM   9362  N  NZ  . LYS   D 1 159 ? 12.228 69.824  66.868 1   86.81  ? 181 LYS   D NZ  1 
ATOM   9363  N  N   . ASP   D 1 160 ? 14.35  66.792  59.988 1   64.61  ? 182 ASP   D N   1 
ATOM   9364  C  CA  . ASP   D 1 160 ? 14.509 65.687  59.054 1   63.42  ? 182 ASP   D CA  1 
ATOM   9365  C  C   . ASP   D 1 160 ? 15.93  65.095  59.109 1   61.99  ? 182 ASP   D C   1 
ATOM   9366  O  O   . ASP   D 1 160 ? 16.889 65.789  59.467 1   62.44  ? 182 ASP   D O   1 
ATOM   9367  C  CB  . ASP   D 1 160 ? 14.103 66.125  57.639 1   64.95  ? 182 ASP   D CB  1 
ATOM   9368  C  CG  . ASP   D 1 160 ? 12.7   66.715  57.557 1   68.95  ? 182 ASP   D CG  1 
ATOM   9369  O  OD1 . ASP   D 1 160 ? 11.902 66.493  58.5   1   68.58  ? 182 ASP   D OD1 1 
ATOM   9370  O  OD2 . ASP   D 1 160 ? 12.406 67.411  56.556 1   71.62  ? 182 ASP   D OD2 1 
ATOM   9371  N  N   . PRO   D 1 161 ? 16.068 63.786  58.851 1   60.05  ? 183 PRO   D N   1 
ATOM   9372  C  CA  . PRO   D 1 161 ? 17.386 63.154  58.989 1   58.84  ? 183 PRO   D CA  1 
ATOM   9373  C  C   . PRO   D 1 161 ? 18.458 63.69   58.057 1   56.85  ? 183 PRO   D C   1 
ATOM   9374  O  O   . PRO   D 1 161 ? 18.286 63.728  56.841 1   56.89  ? 183 PRO   D O   1 
ATOM   9375  C  CB  . PRO   D 1 161 ? 17.102 61.663  58.756 1   60.04  ? 183 PRO   D CB  1 
ATOM   9376  C  CG  . PRO   D 1 161 ? 15.824 61.633  57.993 1   60.74  ? 183 PRO   D CG  1 
ATOM   9377  C  CD  . PRO   D 1 161 ? 15.03  62.803  58.496 1   59.25  ? 183 PRO   D CD  1 
ATOM   9378  N  N   . SER   D 1 162 ? 19.58  64.083  58.642 1   55.16  ? 184 SER   D N   1 
ATOM   9379  C  CA  . SER   D 1 162 ? 20.722 64.589  57.896 1   54.37  ? 184 SER   D CA  1 
ATOM   9380  C  C   . SER   D 1 162 ? 21.471 63.452  57.148 1   54.05  ? 184 SER   D C   1 
ATOM   9381  O  O   . SER   D 1 162 ? 21.152 62.271  57.333 1   54.4   ? 184 SER   D O   1 
ATOM   9382  C  CB  . SER   D 1 162 ? 21.669 65.322  58.844 1   54.46  ? 184 SER   D CB  1 
ATOM   9383  O  OG  . SER   D 1 162 ? 22.356 64.417  59.692 1   54.94  ? 184 SER   D OG  1 
ATOM   9384  N  N   . LEU   D 1 163 ? 22.454 63.804  56.295 1   52.91  ? 185 LEU   D N   1 
ATOM   9385  C  CA  . LEU   D 1 163 ? 23.239 62.799  55.592 1   52.6   ? 185 LEU   D CA  1 
ATOM   9386  C  C   . LEU   D 1 163 ? 24.037 61.948  56.588 1   52.25  ? 185 LEU   D C   1 
ATOM   9387  O  O   . LEU   D 1 163 ? 24.176 60.753  56.376 1   52.61  ? 185 LEU   D O   1 
ATOM   9388  C  CB  . LEU   D 1 163 ? 24.154 63.443  54.534 1   52.56  ? 185 LEU   D CB  1 
ATOM   9389  C  CG  . LEU   D 1 163 ? 23.454 63.87   53.245 1   53.73  ? 185 LEU   D CG  1 
ATOM   9390  C  CD1 . LEU   D 1 163 ? 24.395 64.617  52.347 1   54.34  ? 185 LEU   D CD1 1 
ATOM   9391  C  CD2 . LEU   D 1 163 ? 22.886 62.662  52.497 1   54.13  ? 185 LEU   D CD2 1 
ATOM   9392  N  N   . LEU   D 1 164 ? 24.506 62.548  57.692 1   51.57  ? 186 LEU   D N   1 
ATOM   9393  C  CA  . LEU   D 1 164 ? 25.223 61.852  58.753 1   51.3   ? 186 LEU   D CA  1 
ATOM   9394  C  C   . LEU   D 1 164 ? 24.349 60.76   59.389 1   51.14  ? 186 LEU   D C   1 
ATOM   9395  O  O   . LEU   D 1 164 ? 24.83  59.645  59.594 1   51.72  ? 186 LEU   D O   1 
ATOM   9396  C  CB  . LEU   D 1 164 ? 25.662 62.863  59.822 1   51.19  ? 186 LEU   D CB  1 
ATOM   9397  C  CG  . LEU   D 1 164 ? 26.376 62.28   61.036 1   52.45  ? 186 LEU   D CG  1 
ATOM   9398  C  CD1 . LEU   D 1 164 ? 27.67  61.582  60.64  1   52.75  ? 186 LEU   D CD1 1 
ATOM   9399  C  CD2 . LEU   D 1 164 ? 26.646 63.35   62.064 1   53.13  ? 186 LEU   D CD2 1 
ATOM   9400  N  N   . GLU   D 1 165 ? 23.073 61.066  59.683 1   50.26  ? 187 GLU   D N   1 
ATOM   9401  C  CA  . GLU   D 1 165 ? 22.163 60.093  60.282 1   50.34  ? 187 GLU   D CA  1 
ATOM   9402  C  C   . GLU   D 1 165 ? 21.845 58.961  59.312 1   49.58  ? 187 GLU   D C   1 
ATOM   9403  O  O   . GLU   D 1 165 ? 21.887 57.797  59.711 1   49.89  ? 187 GLU   D O   1 
ATOM   9404  C  CB  . GLU   D 1 165 ? 20.84  60.746  60.722 1   53.9   ? 187 GLU   D CB  1 
ATOM   9405  C  CG  . GLU   D 1 165 ? 20.941 61.812  61.797 1   61.26  ? 187 GLU   D CG  1 
ATOM   9406  C  CD  . GLU   D 1 165 ? 19.602 62.489  62.045 1   69.72  ? 187 GLU   D CD  1 
ATOM   9407  O  OE1 . GLU   D 1 165 ? 18.57  61.779  62.007 1   71.64  ? 187 GLU   D OE1 1 
ATOM   9408  O  OE2 . GLU   D 1 165 ? 19.579 63.727  62.245 1   72.27  ? 187 GLU   D OE2 1 
ATOM   9409  N  N   . LEU   D 1 166 ? 21.522 59.299  58.049 1   48.55  ? 188 LEU   D N   1 
ATOM   9410  C  CA  . LEU   D 1 166 ? 21.159 58.343  57.009 1   48.29  ? 188 LEU   D CA  1 
ATOM   9411  C  C   . LEU   D 1 166 ? 22.302 57.419  56.609 1   48.46  ? 188 LEU   D C   1 
ATOM   9412  O  O   . LEU   D 1 166 ? 22.062 56.242  56.317 1   48.95  ? 188 LEU   D O   1 
ATOM   9413  C  CB  . LEU   D 1 166 ? 20.581 59.07   55.791 1   48.33  ? 188 LEU   D CB  1 
ATOM   9414  C  CG  . LEU   D 1 166 ? 19.268 59.796  56.05  1   49.59  ? 188 LEU   D CG  1 
ATOM   9415  C  CD1 . LEU   D 1 166 ? 18.92  60.706  54.915 1   50.31  ? 188 LEU   D CD1 1 
ATOM   9416  C  CD2 . LEU   D 1 166 ? 18.146 58.828  56.284 1   49.78  ? 188 LEU   D CD2 1 
ATOM   9417  N  N   . VAL   D 1 167 ? 23.537 57.943  56.593 1   47.92  ? 189 VAL   D N   1 
ATOM   9418  C  CA  . VAL   D 1 167 ? 24.734 57.156  56.287 1   47.8   ? 189 VAL   D CA  1 
ATOM   9419  C  C   . VAL   D 1 167 ? 24.994 56.175  57.435 1   47.78  ? 189 VAL   D C   1 
ATOM   9420  O  O   . VAL   D 1 167 ? 25.322 55.021  57.186 1   47.84  ? 189 VAL   D O   1 
ATOM   9421  C  CB  . VAL   D 1 167 ? 25.954 58.062  55.964 1   48.25  ? 189 VAL   D CB  1 
ATOM   9422  C  CG1 . VAL   D 1 167 ? 27.28  57.355  56.198 1   48.44  ? 189 VAL   D CG1 1 
ATOM   9423  C  CG2 . VAL   D 1 167 ? 25.874 58.563  54.533 1   48.95  ? 189 VAL   D CG2 1 
ATOM   9424  N  N   . GLN   D 1 168 ? 24.788 56.611  58.684 1   47.37  ? 190 GLN   D N   1 
ATOM   9425  C  CA  . GLN   D 1 168 ? 24.977 55.752  59.847 1   47.45  ? 190 GLN   D CA  1 
ATOM   9426  C  C   . GLN   D 1 168 ? 24.057 54.55   59.804 1   47.16  ? 190 GLN   D C   1 
ATOM   9427  O  O   . GLN   D 1 168 ? 24.515 53.436  60.033 1   46.54  ? 190 GLN   D O   1 
ATOM   9428  C  CB  . GLN   D 1 168 ? 24.768 56.534  61.141 1   48.55  ? 190 GLN   D CB  1 
ATOM   9429  C  CG  . GLN   D 1 168 ? 26.044 57.125  61.671 1   50.81  ? 190 GLN   D CG  1 
ATOM   9430  C  CD  . GLN   D 1 168 ? 25.794 57.884  62.934 1   54.07  ? 190 GLN   D CD  1 
ATOM   9431  O  OE1 . GLN   D 1 168 ? 26.034 59.089  62.999 1   56.76  ? 190 GLN   D OE1 1 
ATOM   9432  N  NE2 . GLN   D 1 168 ? 25.325 57.198  63.972 1   52.96  ? 190 GLN   D NE2 1 
ATOM   9433  N  N   . ARG   D 1 169 ? 22.783 54.763  59.446 1   47.37  ? 191 ARG   D N   1 
ATOM   9434  C  CA  . ARG   D 1 169 ? 21.827 53.666  59.344 1   47.94  ? 191 ARG   D CA  1 
ATOM   9435  C  C   . ARG   D 1 169 ? 22.213 52.688  58.249 1   47.41  ? 191 ARG   D C   1 
ATOM   9436  O  O   . ARG   D 1 169 ? 22.059 51.485  58.429 1   47.78  ? 191 ARG   D O   1 
ATOM   9437  C  CB  . ARG   D 1 169 ? 20.402 54.188  59.164 1   50.49  ? 191 ARG   D CB  1 
ATOM   9438  C  CG  . ARG   D 1 169 ? 19.849 54.786  60.445 1   56.91  ? 191 ARG   D CG  1 
ATOM   9439  C  CD  . ARG   D 1 169 ? 18.744 55.792  60.156 1   63.47  ? 191 ARG   D CD  1 
ATOM   9440  N  NE  . ARG   D 1 169 ? 18.688 56.863  61.162 1   68.6   ? 191 ARG   D NE  1 
ATOM   9441  C  CZ  . ARG   D 1 169 ? 17.975 57.983  61.03  1   71.78  ? 191 ARG   D CZ  1 
ATOM   9442  N  NH1 . ARG   D 1 169 ? 17.24  58.188  59.939 1   71.55  ? 191 ARG   D NH1 1 
ATOM   9443  N  NH2 . ARG   D 1 169 ? 17.981 58.899  61.992 1   71.86  ? 191 ARG   D NH2 1 
ATOM   9444  N  N   . TRP   D 1 170 ? 22.756 53.197  57.136 1   46.63  ? 192 TRP   D N   1 
ATOM   9445  C  CA  . TRP   D 1 170 ? 23.229 52.398  56.009 1   46.22  ? 192 TRP   D CA  1 
ATOM   9446  C  C   . TRP   D 1 170 ? 24.422 51.549  56.452 1   46.25  ? 192 TRP   D C   1 
ATOM   9447  O  O   . TRP   D 1 170 ? 24.454 50.348  56.193 1   46.38  ? 192 TRP   D O   1 
ATOM   9448  C  CB  . TRP   D 1 170 ? 23.596 53.329  54.826 1   45.62  ? 192 TRP   D CB  1 
ATOM   9449  C  CG  . TRP   D 1 170 ? 24.378 52.694  53.703 1   45.41  ? 192 TRP   D CG  1 
ATOM   9450  C  CD1 . TRP   D 1 170 ? 23.92  51.799  52.782 1   46.11  ? 192 TRP   D CD1 1 
ATOM   9451  C  CD2 . TRP   D 1 170 ? 25.739 52.971  53.35  1   44.93  ? 192 TRP   D CD2 1 
ATOM   9452  N  NE1 . TRP   D 1 170 ? 24.925 51.47   51.901 1   46.02  ? 192 TRP   D NE1 1 
ATOM   9453  C  CE2 . TRP   D 1 170 ? 26.055 52.169  52.234 1   45.55  ? 192 TRP   D CE2 1 
ATOM   9454  C  CE3 . TRP   D 1 170 ? 26.738 53.784  53.897 1   45.08  ? 192 TRP   D CE3 1 
ATOM   9455  C  CZ2 . TRP   D 1 170 ? 27.314 52.184  51.638 1   45.94  ? 192 TRP   D CZ2 1 
ATOM   9456  C  CZ3 . TRP   D 1 170 ? 27.988 53.782  53.316 1   45.74  ? 192 TRP   D CZ3 1 
ATOM   9457  C  CH2 . TRP   D 1 170 ? 28.266 52.991  52.197 1   45.86  ? 192 TRP   D CH2 1 
ATOM   9458  N  N   . LEU   D 1 171 ? 25.375 52.172  57.16  1   46.04  ? 193 LEU   D N   1 
ATOM   9459  C  CA  . LEU   D 1 171 ? 26.582 51.53   57.683 1   45.85  ? 193 LEU   D CA  1 
ATOM   9460  C  C   . LEU   D 1 171 ? 26.259 50.432  58.683 1   45.84  ? 193 LEU   D C   1 
ATOM   9461  O  O   . LEU   D 1 171 ? 26.919 49.396  58.682 1   45.33  ? 193 LEU   D O   1 
ATOM   9462  C  CB  . LEU   D 1 171 ? 27.485 52.58   58.34  1   45.58  ? 193 LEU   D CB  1 
ATOM   9463  C  CG  . LEU   D 1 171 ? 28.306 53.413  57.384 1   46.92  ? 193 LEU   D CG  1 
ATOM   9464  C  CD1 . LEU   D 1 171 ? 28.915 54.594  58.078 1   47.27  ? 193 LEU   D CD1 1 
ATOM   9465  C  CD2 . LEU   D 1 171 ? 29.381 52.578  56.729 1   47.77  ? 193 LEU   D CD2 1 
ATOM   9466  N  N   . GLU   D 1 172 ? 25.254 50.671  59.547 1   46.29  ? 194 GLU   D N   1 
ATOM   9467  C  CA  . GLU   D 1 172 ? 24.802 49.725  60.565 1   47.4   ? 194 GLU   D CA  1 
ATOM   9468  C  C   . GLU   D 1 172 ? 24.267 48.438  59.938 1   49.32  ? 194 GLU   D C   1 
ATOM   9469  O  O   . GLU   D 1 172 ? 24.436 47.356  60.506 1   49.36  ? 194 GLU   D O   1 
ATOM   9470  C  CB  . GLU   D 1 172 ? 23.703 50.36   61.411 1   48.82  ? 194 GLU   D CB  1 
ATOM   9471  C  CG  . GLU   D 1 172 ? 24.205 51.34   62.452 1   52.48  ? 194 GLU   D CG  1 
ATOM   9472  C  CD  . GLU   D 1 172 ? 23.156 52.304  62.981 1   55.95  ? 194 GLU   D CD  1 
ATOM   9473  O  OE1 . GLU   D 1 172 ? 21.977 52.201  62.572 1   55.03  ? 194 GLU   D OE1 1 
ATOM   9474  O  OE2 . GLU   D 1 172 ? 23.523 53.182  63.794 1   58.43  ? 194 GLU   D OE2 1 
ATOM   9475  N  N   . ARG   D 1 173 ? 23.622 48.559  58.761 1   50.57  ? 195 ARG   D N   1 
ATOM   9476  C  CA  . ARG   D 1 173 ? 23.048 47.431  58.042 1   52.04  ? 195 ARG   D CA  1 
ATOM   9477  C  C   . ARG   D 1 173 ? 23.98  46.819  57.021 1   53.02  ? 195 ARG   D C   1 
ATOM   9478  O  O   . ARG   D 1 173 ? 23.51  46.136  56.119 1   53.44  ? 195 ARG   D O   1 
ATOM   9479  C  CB  . ARG   D 1 173 ? 21.722 47.838  57.389 1   54.39  ? 195 ARG   D CB  1 
ATOM   9480  C  CG  . ARG   D 1 173 ? 20.724 48.419  58.401 1   60.23  ? 195 ARG   D CG  1 
ATOM   9481  C  CD  . ARG   D 1 173 ? 19.322 48.511  57.846 1   66.23  ? 195 ARG   D CD  1 
ATOM   9482  N  NE  . ARG   D 1 173 ? 19.269 49.412  56.696 1   72.43  ? 195 ARG   D NE  1 
ATOM   9483  C  CZ  . ARG   D 1 173 ? 18.731 50.626  56.717 1   76.42  ? 195 ARG   D CZ  1 
ATOM   9484  N  NH1 . ARG   D 1 173 ? 18.154 51.087  57.826 1   77.16  ? 195 ARG   D NH1 1 
ATOM   9485  N  NH2 . ARG   D 1 173 ? 18.75  51.386  55.626 1   76.28  ? 195 ARG   D NH2 1 
ATOM   9486  N  N   . THR   D 1 174 ? 25.292 47.035  57.159 1   53.67  ? 196 THR   D N   1 
ATOM   9487  C  CA  . THR   D 1 174 ? 26.285 46.508  56.227 1   54.75  ? 196 THR   D CA  1 
ATOM   9488  C  C   . THR   D 1 174 ? 26.358 45      56.329 1   55.43  ? 196 THR   D C   1 
ATOM   9489  O  O   . THR   D 1 174 ? 26.578 44.47   57.412 1   55.69  ? 196 THR   D O   1 
ATOM   9490  C  CB  . THR   D 1 174 ? 27.668 47.19   56.446 1   56.27  ? 196 THR   D CB  1 
ATOM   9491  O  OG1 . THR   D 1 174 ? 27.623 48.544  55.972 1   57.33  ? 196 THR   D OG1 1 
ATOM   9492  C  CG2 . THR   D 1 174 ? 28.8   46.467  55.749 1   56.76  ? 196 THR   D CG2 1 
ATOM   9493  N  N   . PRO   D 1 175 ? 26.134 44.288  55.213 1   55.95  ? 197 PRO   D N   1 
ATOM   9494  C  CA  . PRO   D 1 175 ? 26.242 42.822  55.253 1   56.16  ? 197 PRO   D CA  1 
ATOM   9495  C  C   . PRO   D 1 175 ? 27.685 42.378  55.523 1   56.73  ? 197 PRO   D C   1 
ATOM   9496  O  O   . PRO   D 1 175 ? 28.645 42.839  54.897 1   56.74  ? 197 PRO   D O   1 
ATOM   9497  C  CB  . PRO   D 1 175 ? 25.725 42.379  53.876 1   56.56  ? 197 PRO   D CB  1 
ATOM   9498  C  CG  . PRO   D 1 175 ? 25.945 43.546  52.99  1   57.01  ? 197 PRO   D CG  1 
ATOM   9499  C  CD  . PRO   D 1 175 ? 25.844 44.782  53.849 1   55.64  ? 197 PRO   D CD  1 
ATOM   9500  N  N   . GLY   D 1 176 ? 27.806 41.495  56.495 1   56.85  ? 198 GLY   D N   1 
ATOM   9501  C  CA  . GLY   D 1 176 ? 29.073 40.98   56.983 1   57.1   ? 198 GLY   D CA  1 
ATOM   9502  C  C   . GLY   D 1 176 ? 29.237 41.192  58.473 1   57.09  ? 198 GLY   D C   1 
ATOM   9503  O  O   . GLY   D 1 176 ? 30.079 40.547  59.097 1   57.06  ? 198 GLY   D O   1 
ATOM   9504  N  N   . LEU   D 1 177 ? 28.435 42.105  59.053 1   57.07  ? 199 LEU   D N   1 
ATOM   9505  C  CA  . LEU   D 1 177 ? 28.456 42.45   60.468 1   57.9   ? 199 LEU   D CA  1 
ATOM   9506  C  C   . LEU   D 1 177 ? 27.665 41.46   61.314 1   59.61  ? 199 LEU   D C   1 
ATOM   9507  O  O   . LEU   D 1 177 ? 27.979 41.299  62.492 1   59.83  ? 199 LEU   D O   1 
ATOM   9508  C  CB  . LEU   D 1 177 ? 27.864 43.859  60.688 1   57.4   ? 199 LEU   D CB  1 
ATOM   9509  C  CG  . LEU   D 1 177 ? 28.714 45.069  60.306 1   57.52  ? 199 LEU   D CG  1 
ATOM   9510  C  CD1 . LEU   D 1 177 ? 28.039 46.348  60.728 1   57.43  ? 199 LEU   D CD1 1 
ATOM   9511  C  CD2 . LEU   D 1 177 ? 30.098 44.997  60.917 1   57.95  ? 199 LEU   D CD2 1 
ATOM   9512  N  N   . GLU   D 1 178 ? 26.608 40.838  60.739 1   60.55  ? 200 GLU   D N   1 
ATOM   9513  C  CA  . GLU   D 1 178 ? 25.745 39.897  61.461 1   61.59  ? 200 GLU   D CA  1 
ATOM   9514  C  C   . GLU   D 1 178 ? 26.483 38.673  61.994 1   61.72  ? 200 GLU   D C   1 
ATOM   9515  O  O   . GLU   D 1 178 ? 27.271 38.058  61.278 1   61.54  ? 200 GLU   D O   1 
ATOM   9516  C  CB  . GLU   D 1 178 ? 24.519 39.485  60.638 1   64.5   ? 200 GLU   D CB  1 
ATOM   9517  C  CG  . GLU   D 1 178 ? 24.835 39.011  59.237 1   71.47  ? 200 GLU   D CG  1 
ATOM   9518  C  CD  . GLU   D 1 178 ? 24.918 40.116  58.2   1   80.85  ? 200 GLU   D CD  1 
ATOM   9519  O  OE1 . GLU   D 1 178 ? 24.305 41.19   58.407 1   83.53  ? 200 GLU   D OE1 1 
ATOM   9520  O  OE2 . GLU   D 1 178 ? 25.616 39.91   57.182 1   82.89  ? 200 GLU   D OE2 1 
ATOM   9521  N  N   . GLU   D 1 179 ? 26.233 38.354  63.276 1   61.79  ? 201 GLU   D N   1 
ATOM   9522  C  CA  . GLU   D 1 179 ? 26.858 37.251  63.999 1   62.29  ? 201 GLU   D CA  1 
ATOM   9523  C  C   . GLU   D 1 179 ? 26.579 35.905  63.367 1   62.34  ? 201 GLU   D C   1 
ATOM   9524  O  O   . GLU   D 1 179 ? 27.456 35.046  63.349 1   62.34  ? 201 GLU   D O   1 
ATOM   9525  C  CB  . GLU   D 1 179 ? 26.386 37.234  65.45  1   65.1   ? 201 GLU   D CB  1 
ATOM   9526  C  CG  . GLU   D 1 179 ? 27     38.311  66.319 1   71.39  ? 201 GLU   D CG  1 
ATOM   9527  C  CD  . GLU   D 1 179 ? 27.002 37.929  67.787 1   81.04  ? 201 GLU   D CD  1 
ATOM   9528  O  OE1 . GLU   D 1 179 ? 26.041 38.294  68.505 1   83.22  ? 201 GLU   D OE1 1 
ATOM   9529  O  OE2 . GLU   D 1 179 ? 27.962 37.246  68.214 1   84.09  ? 201 GLU   D OE2 1 
ATOM   9530  N  N   . SER   D 1 180 ? 25.357 35.713  62.86  1   62.23  ? 202 SER   D N   1 
ATOM   9531  C  CA  . SER   D 1 180 ? 24.971 34.464  62.202 1   62.47  ? 202 SER   D CA  1 
ATOM   9532  C  C   . SER   D 1 180 ? 25.716 34.268  60.881 1   62.3   ? 202 SER   D C   1 
ATOM   9533  O  O   . SER   D 1 180 ? 26.097 33.148  60.547 1   62.32  ? 202 SER   D O   1 
ATOM   9534  C  CB  . SER   D 1 180 ? 23.466 34.439  61.954 1   64.1   ? 202 SER   D CB  1 
ATOM   9535  O  OG  . SER   D 1 180 ? 23.017 35.642  61.348 1   66.9   ? 202 SER   D OG  1 
ATOM   9536  N  N   . GLY   D 1 181 ? 25.922 35.364  60.153 1   62.06  ? 203 GLY   D N   1 
ATOM   9537  C  CA  . GLY   D 1 181 ? 26.598 35.355  58.864 1   62.07  ? 203 GLY   D CA  1 
ATOM   9538  C  C   . GLY   D 1 181 ? 28.107 35.407  58.954 1   61.73  ? 203 GLY   D C   1 
ATOM   9539  O  O   . GLY   D 1 181 ? 28.732 34.538  59.57  1   61.74  ? 203 GLY   D O   1 
ATOM   9540  N  N   . PHE   D 1 182 ? 28.705 36.424  58.322 1   61.17  ? 204 PHE   D N   1 
ATOM   9541  C  CA  . PHE   D 1 182 ? 30.156 36.571  58.292 1   60.85  ? 204 PHE   D CA  1 
ATOM   9542  C  C   . PHE   D 1 182 ? 30.762 36.882  59.672 1   59.95  ? 204 PHE   D C   1 
ATOM   9543  O  O   . PHE   D 1 182 ? 31.869 36.428  59.944 1   60.1   ? 204 PHE   D O   1 
ATOM   9544  C  CB  . PHE   D 1 182 ? 30.59  37.594  57.232 1   60.87  ? 204 PHE   D CB  1 
ATOM   9545  C  CG  . PHE   D 1 182 ? 32.083 37.651  57.017 1   61.78  ? 204 PHE   D CG  1 
ATOM   9546  C  CD1 . PHE   D 1 182 ? 32.758 36.588  56.455 1   62.66  ? 204 PHE   D CD1 1 
ATOM   9547  C  CD2 . PHE   D 1 182 ? 32.813 38.767  57.391 1   62.57  ? 204 PHE   D CD2 1 
ATOM   9548  C  CE1 . PHE   D 1 182 ? 34.133 36.635  56.279 1   63.38  ? 204 PHE   D CE1 1 
ATOM   9549  C  CE2 . PHE   D 1 182 ? 34.189 38.815  57.205 1   63     ? 204 PHE   D CE2 1 
ATOM   9550  C  CZ  . PHE   D 1 182 ? 34.839 37.753  56.649 1   63     ? 204 PHE   D CZ  1 
ATOM   9551  N  N   . ASN   D 1 183 ? 30.04  37.619  60.541 1   58.67  ? 205 ASN   D N   1 
ATOM   9552  C  CA  . ASN   D 1 183 ? 30.498 37.957  61.895 1   57.98  ? 205 ASN   D CA  1 
ATOM   9553  C  C   . ASN   D 1 183 ? 31.874 38.628  61.878 1   56.4   ? 205 ASN   D C   1 
ATOM   9554  O  O   . ASN   D 1 183 ? 32.828 38.085  62.43  1   56.67  ? 205 ASN   D O   1 
ATOM   9555  C  CB  . ASN   D 1 183 ? 30.497 36.702  62.79  1   59.77  ? 205 ASN   D CB  1 
ATOM   9556  C  CG  . ASN   D 1 183 ? 30.525 36.996  64.27  1   64.23  ? 205 ASN   D CG  1 
ATOM   9557  O  OD1 . ASN   D 1 183 ? 30.443 38.158  64.711 1   66     ? 205 ASN   D OD1 1 
ATOM   9558  N  ND2 . ASN   D 1 183 ? 30.62  35.945  65.075 1   64.76  ? 205 ASN   D ND2 1 
ATOM   9559  N  N   . PHE   D 1 184 ? 31.985 39.786  61.219 1   54.78  ? 206 PHE   D N   1 
ATOM   9560  C  CA  . PHE   D 1 184 ? 33.266 40.475  61.065 1   53.92  ? 206 PHE   D CA  1 
ATOM   9561  C  C   . PHE   D 1 184 ? 33.911 40.914  62.382 1   53.63  ? 206 PHE   D C   1 
ATOM   9562  O  O   . PHE   D 1 184 ? 35.085 40.636  62.595 1   53.34  ? 206 PHE   D O   1 
ATOM   9563  C  CB  . PHE   D 1 184 ? 33.146 41.668  60.082 1   53.1   ? 206 PHE   D CB  1 
ATOM   9564  C  CG  . PHE   D 1 184 ? 34.336 42.604  60.048 1   52.68  ? 206 PHE   D CG  1 
ATOM   9565  C  CD1 . PHE   D 1 184 ? 35.512 42.234  59.419 1   52.91  ? 206 PHE   D CD1 1 
ATOM   9566  C  CD2 . PHE   D 1 184 ? 34.278 43.847  60.656 1   52.77  ? 206 PHE   D CD2 1 
ATOM   9567  C  CE1 . PHE   D 1 184 ? 36.602 43.091  59.395 1   53.4   ? 206 PHE   D CE1 1 
ATOM   9568  C  CE2 . PHE   D 1 184 ? 35.373 44.697  60.638 1   53.08  ? 206 PHE   D CE2 1 
ATOM   9569  C  CZ  . PHE   D 1 184 ? 36.527 44.313  60.011 1   52.94  ? 206 PHE   D CZ  1 
ATOM   9570  N  N   . TRP   D 1 185 ? 33.163 41.618  63.241 1   53.49  ? 207 TRP   D N   1 
ATOM   9571  C  CA  . TRP   D 1 185 ? 33.698 42.169  64.481 1   53.39  ? 207 TRP   D CA  1 
ATOM   9572  C  C   . TRP   D 1 185 ? 34.383 41.136  65.374 1   53.02  ? 207 TRP   D C   1 
ATOM   9573  O  O   . TRP   D 1 185 ? 35.448 41.429  65.912 1   53.7   ? 207 TRP   D O   1 
ATOM   9574  C  CB  . TRP   D 1 185 ? 32.616 42.95   65.234 1   53.57  ? 207 TRP   D CB  1 
ATOM   9575  C  CG  . TRP   D 1 185 ? 33.143 44.092  66.053 1   54.6   ? 207 TRP   D CG  1 
ATOM   9576  C  CD1 . TRP   D 1 185 ? 33.061 44.23   67.407 1   55.68  ? 207 TRP   D CD1 1 
ATOM   9577  C  CD2 . TRP   D 1 185 ? 33.832 45.263  65.569 1   54.98  ? 207 TRP   D CD2 1 
ATOM   9578  N  NE1 . TRP   D 1 185 ? 33.644 45.415  67.799 1   56.19  ? 207 TRP   D NE1 1 
ATOM   9579  C  CE2 . TRP   D 1 185 ? 34.127 46.066  66.689 1   55.8   ? 207 TRP   D CE2 1 
ATOM   9580  C  CE3 . TRP   D 1 185 ? 34.227 45.71   64.296 1   55.36  ? 207 TRP   D CE3 1 
ATOM   9581  C  CZ2 . TRP   D 1 185 ? 34.796 47.285  66.575 1   56.1   ? 207 TRP   D CZ2 1 
ATOM   9582  C  CZ3 . TRP   D 1 185 ? 34.884 46.92   64.188 1   55.98  ? 207 TRP   D CZ3 1 
ATOM   9583  C  CH2 . TRP   D 1 185 ? 35.169 47.688  65.318 1   56.11  ? 207 TRP   D CH2 1 
ATOM   9584  N  N   . ALA   D 1 186 ? 33.824 39.918  65.482 1   51.77  ? 208 ALA   D N   1 
ATOM   9585  C  CA  . ALA   D 1 186 ? 34.419 38.842  66.278 1   50.54  ? 208 ALA   D CA  1 
ATOM   9586  C  C   . ALA   D 1 186 ? 35.697 38.297  65.654 1   49.36  ? 208 ALA   D C   1 
ATOM   9587  O  O   . ALA   D 1 186 ? 36.65  37.992  66.361 1   49.3   ? 208 ALA   D O   1 
ATOM   9588  C  CB  . ALA   D 1 186 ? 33.414 37.72   66.459 1   50.68  ? 208 ALA   D CB  1 
ATOM   9589  N  N   . LYS   D 1 187 ? 35.711 38.156  64.328 1   48.79  ? 209 LYS   D N   1 
ATOM   9590  C  CA  . LYS   D 1 187 ? 36.877 37.661  63.599 1   48.5   ? 209 LYS   D CA  1 
ATOM   9591  C  C   . LYS   D 1 187 ? 38.031 38.678  63.635 1   47.99  ? 209 LYS   D C   1 
ATOM   9592  O  O   . LYS   D 1 187 ? 39.2   38.284  63.646 1   47.7   ? 209 LYS   D O   1 
ATOM   9593  C  CB  . LYS   D 1 187 ? 36.501 37.356  62.144 1   50.21  ? 209 LYS   D CB  1 
ATOM   9594  C  CG  . LYS   D 1 187 ? 35.531 36.205  61.989 1   53.34  ? 209 LYS   D CG  1 
ATOM   9595  C  CD  . LYS   D 1 187 ? 35.151 36.022  60.536 1   56.79  ? 209 LYS   D CD  1 
ATOM   9596  C  CE  . LYS   D 1 187 ? 34.425 34.724  60.308 1   59.95  ? 209 LYS   D CE  1 
ATOM   9597  N  NZ  . LYS   D 1 187 ? 34.127 34.518  58.866 1   62.53  ? 209 LYS   D NZ  1 
ATOM   9598  N  N   . PHE   D 1 188 ? 37.683 39.985  63.646 1   47.44  ? 210 PHE   D N   1 
ATOM   9599  C  CA  . PHE   D 1 188 ? 38.595 41.117  63.696 1   47.3   ? 210 PHE   D CA  1 
ATOM   9600  C  C   . PHE   D 1 188 ? 39.278 41.155  65.074 1   48.28  ? 210 PHE   D C   1 
ATOM   9601  O  O   . PHE   D 1 188 ? 40.5   41.268  65.149 1   48.44  ? 210 PHE   D O   1 
ATOM   9602  C  CB  . PHE   D 1 188 ? 37.808 42.409  63.373 1   46.57  ? 210 PHE   D CB  1 
ATOM   9603  C  CG  . PHE   D 1 188 ? 38.528 43.732  63.462 1   46.9   ? 210 PHE   D CG  1 
ATOM   9604  C  CD1 . PHE   D 1 188 ? 39.882 43.828  63.175 1   47.45  ? 210 PHE   D CD1 1 
ATOM   9605  C  CD2 . PHE   D 1 188 ? 37.839 44.892  63.763 1   47.3   ? 210 PHE   D CD2 1 
ATOM   9606  C  CE1 . PHE   D 1 188 ? 40.545 45.045  63.282 1   48.1   ? 210 PHE   D CE1 1 
ATOM   9607  C  CE2 . PHE   D 1 188 ? 38.501 46.112  63.844 1   48.04  ? 210 PHE   D CE2 1 
ATOM   9608  C  CZ  . PHE   D 1 188 ? 39.851 46.179  63.614 1   47.79  ? 210 PHE   D CZ  1 
ATOM   9609  N  N   . GLN   D 1 189 ? 38.508 40.988  66.157 1   48.74  ? 211 GLN   D N   1 
ATOM   9610  C  CA  . GLN   D 1 189 ? 39.066 40.976  67.504 1   49.7   ? 211 GLN   D CA  1 
ATOM   9611  C  C   . GLN   D 1 189 ? 40.071 39.831  67.677 1   50.61  ? 211 GLN   D C   1 
ATOM   9612  O  O   . GLN   D 1 189 ? 41.107 40.018  68.309 1   50.6   ? 211 GLN   D O   1 
ATOM   9613  C  CB  . GLN   D 1 189 ? 37.953 40.856  68.551 1   51.77  ? 211 GLN   D CB  1 
ATOM   9614  C  CG  . GLN   D 1 189 ? 37.004 42.049  68.624 1   55.59  ? 211 GLN   D CG  1 
ATOM   9615  C  CD  . GLN   D 1 189 ? 36.462 42.241  70.022 1   60.84  ? 211 GLN   D CD  1 
ATOM   9616  O  OE1 . GLN   D 1 189 ? 37.198 42.175  71.02  1   61.89  ? 211 GLN   D OE1 1 
ATOM   9617  N  NE2 . GLN   D 1 189 ? 35.161 42.485  70.125 1   62.54  ? 211 GLN   D NE2 1 
ATOM   9618  N  N   . GLU   D 1 190 ? 39.774 38.658  67.099 1   51.23  ? 212 GLU   D N   1 
ATOM   9619  C  CA  . GLU   D 1 190 ? 40.635 37.473  67.165 1   52.25  ? 212 GLU   D CA  1 
ATOM   9620  C  C   . GLU   D 1 190 ? 41.91  37.69   66.359 1   52.37  ? 212 GLU   D C   1 
ATOM   9621  O  O   . GLU   D 1 190 ? 42.989 37.296  66.796 1   52.91  ? 212 GLU   D O   1 
ATOM   9622  C  CB  . GLU   D 1 190 ? 39.888 36.261  66.594 1   56.01  ? 212 GLU   D CB  1 
ATOM   9623  C  CG  . GLU   D 1 190 ? 39.433 35.233  67.608 1   63.36  ? 212 GLU   D CG  1 
ATOM   9624  C  CD  . GLU   D 1 190 ? 39.066 33.925  66.928 1   74.33  ? 212 GLU   D CD  1 
ATOM   9625  O  OE1 . GLU   D 1 190 ? 38.508 33.971  65.804 1   75.9   ? 212 GLU   D OE1 1 
ATOM   9626  O  OE2 . GLU   D 1 190 ? 39.369 32.853  67.503 1   78.29  ? 212 GLU   D OE2 1 
ATOM   9627  N  N   . SER   D 1 191 ? 41.78  38.296  65.173 1   51.87  ? 213 SER   D N   1 
ATOM   9628  C  CA  . SER   D 1 191 ? 42.906 38.588  64.297 1   52.2   ? 213 SER   D CA  1 
ATOM   9629  C  C   . SER   D 1 191 ? 43.855 39.557  64.967 1   51.9   ? 213 SER   D C   1 
ATOM   9630  O  O   . SER   D 1 191 ? 45.064 39.383  64.866 1   51.69  ? 213 SER   D O   1 
ATOM   9631  C  CB  . SER   D 1 191 ? 42.419 39.189  62.981 1   54.01  ? 213 SER   D CB  1 
ATOM   9632  O  OG  . SER   D 1 191 ? 41.698 38.234  62.225 1   57     ? 213 SER   D OG  1 
ATOM   9633  N  N   . VAL   D 1 192 ? 43.302 40.588  65.637 1   51.65  ? 214 VAL   D N   1 
ATOM   9634  C  CA  . VAL   D 1 192 ? 44.063 41.606  66.345 1   51.5   ? 214 VAL   D CA  1 
ATOM   9635  C  C   . VAL   D 1 192 ? 44.856 40.935  67.467 1   51.46  ? 214 VAL   D C   1 
ATOM   9636  O  O   . VAL   D 1 192 ? 46.053 41.169  67.593 1   51.11  ? 214 VAL   D O   1 
ATOM   9637  C  CB  . VAL   D 1 192 ? 43.116 42.733  66.853 1   51.89  ? 214 VAL   D CB  1 
ATOM   9638  C  CG1 . VAL   D 1 192 ? 43.729 43.525  68.002 1   52.29  ? 214 VAL   D CG1 1 
ATOM   9639  C  CG2 . VAL   D 1 192 ? 42.72  43.659  65.719 1   52.17  ? 214 VAL   D CG2 1 
ATOM   9640  N  N   . ASP   D 1 193 ? 44.195 40.07   68.244 1   51.87  ? 215 ASP   D N   1 
ATOM   9641  C  CA  . ASP   D 1 193 ? 44.822 39.373  69.356 1   52.98  ? 215 ASP   D CA  1 
ATOM   9642  C  C   . ASP   D 1 193 ? 45.997 38.53   68.915 1   53.03  ? 215 ASP   D C   1 
ATOM   9643  O  O   . ASP   D 1 193 ? 47.055 38.622  69.526 1   53.5   ? 215 ASP   D O   1 
ATOM   9644  C  CB  . ASP   D 1 193 ? 43.804 38.526  70.132 1   56.06  ? 215 ASP   D CB  1 
ATOM   9645  C  CG  . ASP   D 1 193 ? 42.885 39.32   71.043 1   63.43  ? 215 ASP   D CG  1 
ATOM   9646  O  OD1 . ASP   D 1 193 ? 43.123 40.541  71.215 1   65.79  ? 215 ASP   D OD1 1 
ATOM   9647  O  OD2 . ASP   D 1 193 ? 41.916 38.725  71.578 1   65.61  ? 215 ASP   D OD2 1 
ATOM   9648  N  N   . ARG   D 1 194 ? 45.84  37.753  67.842 1   52.54  ? 216 ARG   D N   1 
ATOM   9649  C  CA  . ARG   D 1 194 ? 46.92  36.915  67.332 1   52.62  ? 216 ARG   D CA  1 
ATOM   9650  C  C   . ARG   D 1 194 ? 48.022 37.736  66.683 1   53.35  ? 216 ARG   D C   1 
ATOM   9651  O  O   . ARG   D 1 194 ? 49.191 37.367  66.785 1   53.75  ? 216 ARG   D O   1 
ATOM   9652  C  CB  . ARG   D 1 194 ? 46.383 35.909  66.317 1   52.8   ? 216 ARG   D CB  1 
ATOM   9653  C  CG  . ARG   D 1 194 ? 45.526 34.831  66.932 1   53.93  ? 216 ARG   D CG  1 
ATOM   9654  C  CD  . ARG   D 1 194 ? 45.186 33.778  65.898 1   54.92  ? 216 ARG   D CD  1 
ATOM   9655  N  NE  . ARG   D 1 194 ? 44.293 34.298  64.863 1   55.85  ? 216 ARG   D NE  1 
ATOM   9656  C  CZ  . ARG   D 1 194 ? 42.967 34.224  64.909 1   57.16  ? 216 ARG   D CZ  1 
ATOM   9657  N  NH1 . ARG   D 1 194 ? 42.361 33.658  65.949 1   56.75  ? 216 ARG   D NH1 1 
ATOM   9658  N  NH2 . ARG   D 1 194 ? 42.234 34.728  63.926 1   56.56  ? 216 ARG   D NH2 1 
ATOM   9659  N  N   . PHE   D 1 195 ? 47.659 38.836  66.008 1   53.16  ? 217 PHE   D N   1 
ATOM   9660  C  CA  . PHE   D 1 195 ? 48.635 39.697  65.358 1   53.66  ? 217 PHE   D CA  1 
ATOM   9661  C  C   . PHE   D 1 195 ? 49.509 40.383  66.394 1   54.05  ? 217 PHE   D C   1 
ATOM   9662  O  O   . PHE   D 1 195 ? 50.729 40.383  66.261 1   54.44  ? 217 PHE   D O   1 
ATOM   9663  C  CB  . PHE   D 1 195 ? 47.937 40.727  64.448 1   53.99  ? 217 PHE   D CB  1 
ATOM   9664  C  CG  . PHE   D 1 195 ? 48.867 41.755  63.842 1   54.87  ? 217 PHE   D CG  1 
ATOM   9665  C  CD1 . PHE   D 1 195 ? 49.744 41.408  62.833 1   55.73  ? 217 PHE   D CD1 1 
ATOM   9666  C  CD2 . PHE   D 1 195 ? 48.861 43.067  64.286 1   55.45  ? 217 PHE   D CD2 1 
ATOM   9667  C  CE1 . PHE   D 1 195 ? 50.622 42.342  62.31  1   56.54  ? 217 PHE   D CE1 1 
ATOM   9668  C  CE2 . PHE   D 1 195 ? 49.741 43.997  63.76  1   56.03  ? 217 PHE   D CE2 1 
ATOM   9669  C  CZ  . PHE   D 1 195 ? 50.618 43.629  62.782 1   56.17  ? 217 PHE   D CZ  1 
ATOM   9670  N  N   . LEU   D 1 196 ? 48.897 40.957  67.426 1   54.08  ? 218 LEU   D N   1 
ATOM   9671  C  CA  . LEU   D 1 196 ? 49.642 41.644  68.467 1   54.68  ? 218 LEU   D CA  1 
ATOM   9672  C  C   . LEU   D 1 196 ? 50.488 40.682  69.299 1   55.89  ? 218 LEU   D C   1 
ATOM   9673  O  O   . LEU   D 1 196 ? 51.585 41.055  69.694 1   55.96  ? 218 LEU   D O   1 
ATOM   9674  C  CB  . LEU   D 1 196 ? 48.729 42.525  69.331 1   54.22  ? 218 LEU   D CB  1 
ATOM   9675  C  CG  . LEU   D 1 196 ? 48.045 43.676  68.599 1   55.01  ? 218 LEU   D CG  1 
ATOM   9676  C  CD1 . LEU   D 1 196 ? 47.149 44.447  69.522 1   55.42  ? 218 LEU   D CD1 1 
ATOM   9677  C  CD2 . LEU   D 1 196 ? 49.052 44.618  67.967 1   55.61  ? 218 LEU   D CD2 1 
ATOM   9678  N  N   . GLU   D 1 197 ? 50.034 39.428  69.493 1   56.59  ? 219 GLU   D N   1 
ATOM   9679  C  CA  . GLU   D 1 197 ? 50.832 38.425  70.208 1   57.68  ? 219 GLU   D CA  1 
ATOM   9680  C  C   . GLU   D 1 197 ? 52.075 38.094  69.39  1   57.63  ? 219 GLU   D C   1 
ATOM   9681  O  O   . GLU   D 1 197 ? 53.173 38.053  69.937 1   57.55  ? 219 GLU   D O   1 
ATOM   9682  C  CB  . GLU   D 1 197 ? 50.025 37.142  70.46  1   61.78  ? 219 GLU   D CB  1 
ATOM   9683  C  CG  . GLU   D 1 197 ? 49.167 37.173  71.714 1   70.91  ? 219 GLU   D CG  1 
ATOM   9684  C  CD  . GLU   D 1 197 ? 47.939 36.274  71.671 1   82.32  ? 219 GLU   D CD  1 
ATOM   9685  O  OE1 . GLU   D 1 197 ? 47.935 35.29   70.891 1   84.69  ? 219 GLU   D OE1 1 
ATOM   9686  O  OE2 . GLU   D 1 197 ? 46.971 36.567  72.413 1   85.73  ? 219 GLU   D OE2 1 
ATOM   9687  N  N   . ALA   D 1 198 ? 51.911 37.914  68.066 1   57.6   ? 220 ALA   D N   1 
ATOM   9688  C  CA  . ALA   D 1 198 ? 53.022 37.638  67.155 1   57.98  ? 220 ALA   D CA  1 
ATOM   9689  C  C   . ALA   D 1 198 ? 54.012 38.802  67.107 1   58.52  ? 220 ALA   D C   1 
ATOM   9690  O  O   . ALA   D 1 198 ? 55.2   38.576  66.912 1   59     ? 220 ALA   D O   1 
ATOM   9691  C  CB  . ALA   D 1 198 ? 52.499 37.352  65.765 1   58.13  ? 220 ALA   D CB  1 
ATOM   9692  N  N   . GLN   D 1 199 ? 53.525 40.043  67.275 1   58.31  ? 221 GLN   D N   1 
ATOM   9693  C  CA  . GLN   D 1 199 ? 54.354 41.241  67.315 1   58.62  ? 221 GLN   D CA  1 
ATOM   9694  C  C   . GLN   D 1 199 ? 55.182 41.27   68.6   1   59.01  ? 221 GLN   D C   1 
ATOM   9695  O  O   . GLN   D 1 199 ? 56.31  41.741  68.572 1   59.14  ? 221 GLN   D O   1 
ATOM   9696  C  CB  . GLN   D 1 199 ? 53.483 42.505  67.235 1   59.86  ? 221 GLN   D CB  1 
ATOM   9697  C  CG  . GLN   D 1 199 ? 52.996 42.854  65.837 1   61.89  ? 221 GLN   D CG  1 
ATOM   9698  C  CD  . GLN   D 1 199 ? 54.131 43.108  64.884 1   65.2   ? 221 GLN   D CD  1 
ATOM   9699  O  OE1 . GLN   D 1 199 ? 54.207 42.514  63.802 1   66.46  ? 221 GLN   D OE1 1 
ATOM   9700  N  NE2 . GLN   D 1 199 ? 55.038 43.998  65.256 1   65.16  ? 221 GLN   D NE2 1 
ATOM   9701  N  N   . VAL   D 1 200 ? 54.62  40.788  69.729 1   59.06  ? 222 VAL   D N   1 
ATOM   9702  C  CA  . VAL   D 1 200 ? 55.316 40.732  71.017 1   59.2   ? 222 VAL   D CA  1 
ATOM   9703  C  C   . VAL   D 1 200 ? 56.431 39.695  70.947 1   59.96  ? 222 VAL   D C   1 
ATOM   9704  O  O   . VAL   D 1 200 ? 57.544 39.975  71.369 1   60.05  ? 222 VAL   D O   1 
ATOM   9705  C  CB  . VAL   D 1 200 ? 54.347 40.481  72.2   1   59.27  ? 222 VAL   D CB  1 
ATOM   9706  C  CG1 . VAL   D 1 200 ? 55.107 40.17   73.483 1   59.5   ? 222 VAL   D CG1 1 
ATOM   9707  C  CG2 . VAL   D 1 200 ? 53.417 41.671  72.407 1   59.55  ? 222 VAL   D CG2 1 
ATOM   9708  N  N   . GLN   D 1 201 ? 56.157 38.529  70.353 1   60.48  ? 223 GLN   D N   1 
ATOM   9709  C  CA  . GLN   D 1 201 ? 57.165 37.482  70.2   1   61.48  ? 223 GLN   D CA  1 
ATOM   9710  C  C   . GLN   D 1 201 ? 58.293 37.921  69.282 1   62.43  ? 223 GLN   D C   1 
ATOM   9711  O  O   . GLN   D 1 201 ? 59.451 37.637  69.562 1   62.75  ? 223 GLN   D O   1 
ATOM   9712  C  CB  . GLN   D 1 201 ? 56.53  36.175  69.697 1   63.02  ? 223 GLN   D CB  1 
ATOM   9713  C  CG  . GLN   D 1 201 ? 55.484 35.594  70.645 1   66.74  ? 223 GLN   D CG  1 
ATOM   9714  C  CD  . GLN   D 1 201 ? 55.984 35.411  72.069 1   71.82  ? 223 GLN   D CD  1 
ATOM   9715  O  OE1 . GLN   D 1 201 ? 57.049 34.83   72.316 1   73.45  ? 223 GLN   D OE1 1 
ATOM   9716  N  NE2 . GLN   D 1 201 ? 55.22  35.916  73.038 1   72.35  ? 223 GLN   D NE2 1 
ATOM   9717  N  N   . SER   D 1 202 ? 57.961 38.659  68.223 1   62.93  ? 224 SER   D N   1 
ATOM   9718  C  CA  . SER   D 1 202 ? 58.929 39.204  67.273 1   64.04  ? 224 SER   D CA  1 
ATOM   9719  C  C   . SER   D 1 202 ? 59.777 40.284  67.941 1   64.69  ? 224 SER   D C   1 
ATOM   9720  O  O   . SER   D 1 202 ? 60.984 40.338  67.711 1   64.99  ? 224 SER   D O   1 
ATOM   9721  C  CB  . SER   D 1 202 ? 58.208 39.786  66.059 1   65.39  ? 224 SER   D CB  1 
ATOM   9722  O  OG  . SER   D 1 202 ? 59.119 40.364  65.14  1   67.51  ? 224 SER   D OG  1 
ATOM   9723  N  N   . ALA   D 1 203 ? 59.144 41.134  68.774 1   64.73  ? 225 ALA   D N   1 
ATOM   9724  C  CA  . ALA   D 1 203 ? 59.833 42.186  69.52  1   65.48  ? 225 ALA   D CA  1 
ATOM   9725  C  C   . ALA   D 1 203 ? 60.746 41.601  70.592 1   66.45  ? 225 ALA   D C   1 
ATOM   9726  O  O   . ALA   D 1 203 ? 61.759 42.208  70.911 1   66.58  ? 225 ALA   D O   1 
ATOM   9727  C  CB  . ALA   D 1 203 ? 58.832 43.134  70.161 1   65.4   ? 225 ALA   D CB  1 
ATOM   9728  N  N   . MET   D 1 204 ? 60.387 40.44   71.164 1   67.07  ? 226 MET   D N   1 
ATOM   9729  C  CA  . MET   D 1 204 ? 61.202 39.781  72.18  1   67.95  ? 226 MET   D CA  1 
ATOM   9730  C  C   . MET   D 1 204 ? 62.524 39.271  71.588 1   68.91  ? 226 MET   D C   1 
ATOM   9731  O  O   . MET   D 1 204 ? 63.541 39.27   72.273 1   68.71  ? 226 MET   D O   1 
ATOM   9732  C  CB  . MET   D 1 204 ? 60.428 38.635  72.851 1   68.43  ? 226 MET   D CB  1 
ATOM   9733  C  CG  . MET   D 1 204 ? 59.34  39.098  73.791 1   70.13  ? 226 MET   D CG  1 
ATOM   9734  S  SD  . MET   D 1 204 ? 59.928 40.166  75.137 1   73.46  ? 226 MET   D SD  1 
ATOM   9735  C  CE  . MET   D 1 204 ? 58.375 40.767  75.76  1   70.35  ? 226 MET   D CE  1 
ATOM   9736  N  N   . GLU   D 1 205 ? 62.519 38.864  70.315 1   69.93  ? 227 GLU   D N   1 
ATOM   9737  C  CA  . GLU   D 1 205 ? 63.728 38.387  69.644 1   71.5   ? 227 GLU   D CA  1 
ATOM   9738  C  C   . GLU   D 1 205 ? 64.568 39.519  69.007 1   72.62  ? 227 GLU   D C   1 
ATOM   9739  O  O   . GLU   D 1 205 ? 65.474 39.239  68.217 1   72.64  ? 227 GLU   D O   1 
ATOM   9740  C  CB  . GLU   D 1 205 ? 63.371 37.34   68.584 1   74.09  ? 227 GLU   D CB  1 
ATOM   9741  C  CG  . GLU   D 1 205 ? 62.63  36.144  69.15  1   79.83  ? 227 GLU   D CG  1 
ATOM   9742  C  CD  . GLU   D 1 205 ? 61.837 35.344  68.137 1   88.62  ? 227 GLU   D CD  1 
ATOM   9743  O  OE1 . GLU   D 1 205 ? 61.727 35.786  66.97  1   91.26  ? 227 GLU   D OE1 1 
ATOM   9744  O  OE2 . GLU   D 1 205 ? 61.29  34.287  68.525 1   91.29  ? 227 GLU   D OE2 1 
ATOM   9745  N  N   . GLU   D 1 206 ? 64.266 40.786  69.334 1   73.19  ? 228 GLU   D N   1 
ATOM   9746  C  CA  . GLU   D 1 206 ? 65.018 41.913  68.795 1   74.27  ? 228 GLU   D CA  1 
ATOM   9747  C  C   . GLU   D 1 206 ? 66.413 41.945  69.411 1   74.97  ? 228 GLU   D C   1 
ATOM   9748  O  O   . GLU   D 1 206 ? 66.553 41.908  70.635 1   75.02  ? 228 GLU   D O   1 
ATOM   9749  C  CB  . GLU   D 1 206 ? 64.284 43.236  69.053 1   76.39  ? 228 GLU   D CB  1 
ATOM   9750  C  CG  . GLU   D 1 206 ? 64.571 44.299  68.011 1   80.8   ? 228 GLU   D CG  1 
ATOM   9751  C  CD  . GLU   D 1 206 ? 63.815 44.115  66.713 1   86.88  ? 228 GLU   D CD  1 
ATOM   9752  O  OE1 . GLU   D 1 206 ? 62.746 43.462  66.741 1   87.36  ? 228 GLU   D OE1 1 
ATOM   9753  O  OE2 . GLU   D 1 206 ? 64.284 44.631  65.672 1   88.95  ? 228 GLU   D OE2 1 
ATOM   9754  N  N   . PRO   D 1 207 ? 67.461 41.964  68.567 1   75.48  ? 229 PRO   D N   1 
ATOM   9755  C  CA  . PRO   D 1 207 ? 68.831 41.967  69.107 1   76.01  ? 229 PRO   D CA  1 
ATOM   9756  C  C   . PRO   D 1 207 ? 69.196 43.262  69.835 1   76.83  ? 229 PRO   D C   1 
ATOM   9757  O  O   . PRO   D 1 207 ? 69.741 43.203  70.939 1   76.77  ? 229 PRO   D O   1 
ATOM   9758  C  CB  . PRO   D 1 207 ? 69.705 41.706  67.875 1   76.54  ? 229 PRO   D CB  1 
ATOM   9759  C  CG  . PRO   D 1 207 ? 68.886 42.127  66.709 1   76.75  ? 229 PRO   D CG  1 
ATOM   9760  C  CD  . PRO   D 1 207 ? 67.445 41.971  67.089 1   75.04  ? 229 PRO   D CD  1 
ATOM   9761  N  N   . VAL   D 1 208 ? 68.856 44.427  69.236 1   77.2   ? 230 VAL   D N   1 
ATOM   9762  C  CA  . VAL   D 1 208 ? 69.113 45.746  69.819 1   77.81  ? 230 VAL   D CA  1 
ATOM   9763  C  C   . VAL   D 1 208 ? 68.125 45.974  70.973 1   78.08  ? 230 VAL   D C   1 
ATOM   9764  O  O   . VAL   D 1 208 ? 66.924 45.803  70.777 1   78.19  ? 230 VAL   D O   1 
ATOM   9765  C  CB  . VAL   D 1 208 ? 68.99  46.861  68.751 1   78.63  ? 230 VAL   D CB  1 
ATOM   9766  C  CG1 . VAL   D 1 208 ? 69.398 48.214  69.323 1   79.34  ? 230 VAL   D CG1 1 
ATOM   9767  C  CG2 . VAL   D 1 208 ? 69.802 46.531  67.501 1   79.1   ? 230 VAL   D CG2 1 
ATOM   9768  N  N   . GLU   D 1 209 ? 68.619 46.327  72.168 1   77.96  ? 231 GLU   D N   1 
ATOM   9769  C  CA  . GLU   D 1 209 ? 67.745 46.533  73.322 1   78.4   ? 231 GLU   D CA  1 
ATOM   9770  C  C   . GLU   D 1 209 ? 66.827 47.744  73.168 1   78.61  ? 231 GLU   D C   1 
ATOM   9771  O  O   . GLU   D 1 209 ? 65.663 47.683  73.577 1   78.95  ? 231 GLU   D O   1 
ATOM   9772  C  CB  . GLU   D 1 209 ? 68.563 46.617  74.624 1   80.98  ? 231 GLU   D CB  1 
ATOM   9773  C  CG  . GLU   D 1 209 ? 67.724 46.67   75.897 1   86.61  ? 231 GLU   D CG  1 
ATOM   9774  C  CD  . GLU   D 1 209 ? 66.989 45.4    76.29  1   93.61  ? 231 GLU   D CD  1 
ATOM   9775  O  OE1 . GLU   D 1 209 ? 67.282 44.332  75.704 1   95.7   ? 231 GLU   D OE1 1 
ATOM   9776  O  OE2 . GLU   D 1 209 ? 66.125 45.473  77.196 1   95.27  ? 231 GLU   D OE2 1 
ATOM   9777  N  N   . LYS   D 1 210 ? 67.331 48.83   72.551 1   78.03  ? 232 LYS   D N   1 
ATOM   9778  C  CA  . LYS   D 1 210 ? 66.539 50.045  72.357 1   77.52  ? 232 LYS   D CA  1 
ATOM   9779  C  C   . LYS   D 1 210 ? 65.34  49.799  71.434 1   76.69  ? 232 LYS   D C   1 
ATOM   9780  O  O   . LYS   D 1 210 ? 64.244 50.281  71.716 1   77.02  ? 232 LYS   D O   1 
ATOM   9781  C  CB  . LYS   D 1 210 ? 67.42  51.189  71.831 1   79.19  ? 232 LYS   D CB  1 
ATOM   9782  C  CG  . LYS   D 1 210 ? 66.687 52.52   71.716 1   83.2   ? 232 LYS   D CG  1 
ATOM   9783  C  CD  . LYS   D 1 210 ? 67.564 53.64   71.17  1   87.9   ? 232 LYS   D CD  1 
ATOM   9784  C  CE  . LYS   D 1 210 ? 68.116 53.337  69.795 1   91.94  ? 232 LYS   D CE  1 
ATOM   9785  N  NZ  . LYS   D 1 210 ? 67.061 52.941  68.821 1   94.24  ? 232 LYS   D NZ  1 
ATOM   9786  N  N   . ALA   D 1 211 ? 65.544 49.028  70.353 1   75.5   ? 233 ALA   D N   1 
ATOM   9787  C  CA  . ALA   D 1 211 ? 64.485 48.705  69.393 1   74.81  ? 233 ALA   D CA  1 
ATOM   9788  C  C   . ALA   D 1 211 ? 63.442 47.786  70.009 1   73.58  ? 233 ALA   D C   1 
ATOM   9789  O  O   . ALA   D 1 211 ? 62.261 47.93   69.717 1   74     ? 233 ALA   D O   1 
ATOM   9790  C  CB  . ALA   D 1 211 ? 65.072 48.054  68.15  1   75.04  ? 233 ALA   D CB  1 
ATOM   9791  N  N   . LYS   D 1 212 ? 63.877 46.856  70.863 1   71.76  ? 234 LYS   D N   1 
ATOM   9792  C  CA  . LYS   D 1 212 ? 63.026 45.902  71.558 1   70.47  ? 234 LYS   D CA  1 
ATOM   9793  C  C   . LYS   D 1 212 ? 62.017 46.631  72.451 1   68.78  ? 234 LYS   D C   1 
ATOM   9794  O  O   . LYS   D 1 212 ? 60.821 46.348  72.385 1   68.96  ? 234 LYS   D O   1 
ATOM   9795  C  CB  . LYS   D 1 212 ? 63.926 44.967  72.383 1   72.27  ? 234 LYS   D CB  1 
ATOM   9796  C  CG  . LYS   D 1 212 ? 63.221 43.953  73.252 1   76.09  ? 234 LYS   D CG  1 
ATOM   9797  C  CD  . LYS   D 1 212 ? 64.283 43.097  73.908 1   80.93  ? 234 LYS   D CD  1 
ATOM   9798  C  CE  . LYS   D 1 212 ? 63.76  41.821  74.496 1   85.01  ? 234 LYS   D CE  1 
ATOM   9799  N  NZ  . LYS   D 1 212 ? 64.817 40.775  74.487 1   87.06  ? 234 LYS   D NZ  1 
ATOM   9800  N  N   . ASN   D 1 213 ? 62.493 47.595  73.248 1   66.96  ? 235 ASN   D N   1 
ATOM   9801  C  CA  . ASN   D 1 213 ? 61.642 48.362  74.147 1   65.82  ? 235 ASN   D CA  1 
ATOM   9802  C  C   . ASN   D 1 213 ? 60.7   49.278  73.381 1   64.25  ? 235 ASN   D C   1 
ATOM   9803  O  O   . ASN   D 1 213 ? 59.555 49.455  73.801 1   64.23  ? 235 ASN   D O   1 
ATOM   9804  C  CB  . ASN   D 1 213 ? 62.487 49.178  75.11  1   67.41  ? 235 ASN   D CB  1 
ATOM   9805  C  CG  . ASN   D 1 213 ? 63.509 48.37   75.862 1   70.93  ? 235 ASN   D CG  1 
ATOM   9806  O  OD1 . ASN   D 1 213 ? 63.348 47.168  76.078 1   71.9   ? 235 ASN   D OD1 1 
ATOM   9807  N  ND2 . ASN   D 1 213 ? 64.598 49.018  76.256 1   71.92  ? 235 ASN   D ND2 1 
ATOM   9808  N  N   . TYR   D 1 214 ? 61.173 49.854  72.251 1   62.71  ? 236 TYR   D N   1 
ATOM   9809  C  CA  . TYR   D 1 214 ? 60.357 50.732  71.42  1   61.83  ? 236 TYR   D CA  1 
ATOM   9810  C  C   . TYR   D 1 214 ? 59.185 49.96   70.858 1   60.91  ? 236 TYR   D C   1 
ATOM   9811  O  O   . TYR   D 1 214 ? 58.06  50.45   70.913 1   61.45  ? 236 TYR   D O   1 
ATOM   9812  C  CB  . TYR   D 1 214 ? 61.168 51.357  70.282 1   61.86  ? 236 TYR   D CB  1 
ATOM   9813  C  CG  . TYR   D 1 214 ? 60.342 52.272  69.401 1   62.86  ? 236 TYR   D CG  1 
ATOM   9814  C  CD1 . TYR   D 1 214 ? 60.019 53.56   69.81  1   63.86  ? 236 TYR   D CD1 1 
ATOM   9815  C  CD2 . TYR   D 1 214 ? 59.888 51.851  68.159 1   63.78  ? 236 TYR   D CD2 1 
ATOM   9816  C  CE1 . TYR   D 1 214 ? 59.284 54.414  68.995 1   64.74  ? 236 TYR   D CE1 1 
ATOM   9817  C  CE2 . TYR   D 1 214 ? 59.13  52.689  67.346 1   64.82  ? 236 TYR   D CE2 1 
ATOM   9818  C  CZ  . TYR   D 1 214 ? 58.831 53.974  67.767 1   65.73  ? 236 TYR   D CZ  1 
ATOM   9819  O  OH  . TYR   D 1 214 ? 58.09  54.82   66.967 1   67.24  ? 236 TYR   D OH  1 
ATOM   9820  N  N   . ARG   D 1 215 ? 59.437 48.742  70.344 1   59.37  ? 237 ARG   D N   1 
ATOM   9821  C  CA  . ARG   D 1 215 ? 58.388 47.888  69.797 1   58.25  ? 237 ARG   D CA  1 
ATOM   9822  C  C   . ARG   D 1 215 ? 57.383 47.486  70.856 1   57.55  ? 237 ARG   D C   1 
ATOM   9823  O  O   . ARG   D 1 215 ? 56.192 47.579  70.602 1   57.82  ? 237 ARG   D O   1 
ATOM   9824  C  CB  . ARG   D 1 215 ? 58.97  46.648  69.137 1   58.63  ? 237 ARG   D CB  1 
ATOM   9825  C  CG  . ARG   D 1 215 ? 59.722 46.945  67.869 1   59.37  ? 237 ARG   D CG  1 
ATOM   9826  C  CD  . ARG   D 1 215 ? 60.107 45.667  67.174 1   60.17  ? 237 ARG   D CD  1 
ATOM   9827  N  NE  . ARG   D 1 215 ? 58.938 44.966  66.65  1   60.85  ? 237 ARG   D NE  1 
ATOM   9828  C  CZ  . ARG   D 1 215 ? 58.989 43.835  65.955 1   61.7   ? 237 ARG   D CZ  1 
ATOM   9829  N  NH1 . ARG   D 1 215 ? 60.154 43.253  65.705 1   61.92  ? 237 ARG   D NH1 1 
ATOM   9830  N  NH2 . ARG   D 1 215 ? 57.875 43.271  65.517 1   60.47  ? 237 ARG   D NH2 1 
ATOM   9831  N  N   . LEU   D 1 216 ? 57.844 47.105  72.053 1   56.55  ? 238 LEU   D N   1 
ATOM   9832  C  CA  . LEU   D 1 216 ? 56.944 46.731  73.136 1   56.16  ? 238 LEU   D CA  1 
ATOM   9833  C  C   . LEU   D 1 216 ? 56.08  47.905  73.604 1   55.41  ? 238 LEU   D C   1 
ATOM   9834  O  O   . LEU   D 1 216 ? 54.905 47.709  73.934 1   55.89  ? 238 LEU   D O   1 
ATOM   9835  C  CB  . LEU   D 1 216 ? 57.734 46.119  74.3   1   56.58  ? 238 LEU   D CB  1 
ATOM   9836  C  CG  . LEU   D 1 216 ? 58.422 44.792  74.002 1   58.1   ? 238 LEU   D CG  1 
ATOM   9837  C  CD1 . LEU   D 1 216 ? 59.236 44.334  75.188 1   58.59  ? 238 LEU   D CD1 1 
ATOM   9838  C  CD2 . LEU   D 1 216 ? 57.415 43.726  73.604 1   58.7   ? 238 LEU   D CD2 1 
ATOM   9839  N  N   . MET   D 1 217 ? 56.649 49.124  73.61  1   54.08  ? 239 MET   D N   1 
ATOM   9840  C  CA  . MET   D 1 217 ? 55.88  50.316  73.971 1   53.16  ? 239 MET   D CA  1 
ATOM   9841  C  C   . MET   D 1 217 ? 54.848 50.633  72.882 1   51.74  ? 239 MET   D C   1 
ATOM   9842  O  O   . MET   D 1 217 ? 53.724 51.023  73.193 1   51.86  ? 239 MET   D O   1 
ATOM   9843  C  CB  . MET   D 1 217 ? 56.799 51.517  74.318 1   53.81  ? 239 MET   D CB  1 
ATOM   9844  C  CG  . MET   D 1 217 ? 57.171 52.436  73.167 1   55.52  ? 239 MET   D CG  1 
ATOM   9845  S  SD  . MET   D 1 217 ? 55.961 53.712  72.723 1   57.3   ? 239 MET   D SD  1 
ATOM   9846  C  CE  . MET   D 1 217 ? 56.957 54.648  71.662 1   53     ? 239 MET   D CE  1 
ATOM   9847  N  N   . ASP   D 1 218 ? 55.229 50.426  71.615 1   50.34  ? 240 ASP   D N   1 
ATOM   9848  C  CA  . ASP   D 1 218 ? 54.383 50.645  70.456 1   50.13  ? 240 ASP   D CA  1 
ATOM   9849  C  C   . ASP   D 1 218 ? 53.202 49.658  70.418 1   50.05  ? 240 ASP   D C   1 
ATOM   9850  O  O   . ASP   D 1 218 ? 52.077 50.083  70.17  1   50.26  ? 240 ASP   D O   1 
ATOM   9851  C  CB  . ASP   D 1 218 ? 55.22  50.571  69.17  1   50.9   ? 240 ASP   D CB  1 
ATOM   9852  C  CG  . ASP   D 1 218 ? 54.435 50.822  67.909 1   53.14  ? 240 ASP   D CG  1 
ATOM   9853  O  OD1 . ASP   D 1 218 ? 53.858 51.929  67.772 1   53.93  ? 240 ASP   D OD1 1 
ATOM   9854  O  OD2 . ASP   D 1 218 ? 54.427 49.939  67.038 1   54.14  ? 240 ASP   D OD2 1 
ATOM   9855  N  N   . ILE   D 1 219 ? 53.438 48.36   70.71  1   49.3   ? 241 ILE   D N   1 
ATOM   9856  C  CA  . ILE   D 1 219 ? 52.366 47.354  70.786 1   48.57  ? 241 ILE   D CA  1 
ATOM   9857  C  C   . ILE   D 1 219 ? 51.355 47.745  71.868 1   47.53  ? 241 ILE   D C   1 
ATOM   9858  O  O   . ILE   D 1 219 ? 50.156 47.531  71.689 1   47.39  ? 241 ILE   D O   1 
ATOM   9859  C  CB  . ILE   D 1 219 ? 52.959 45.948  71.047 1   49.02  ? 241 ILE   D CB  1 
ATOM   9860  C  CG1 . ILE   D 1 219 ? 53.839 45.518  69.874 1   50.17  ? 241 ILE   D CG1 1 
ATOM   9861  C  CG2 . ILE   D 1 219 ? 51.871 44.92   71.318 1   49.27  ? 241 ILE   D CG2 1 
ATOM   9862  C  CD1 . ILE   D 1 219 ? 54.84  44.467  70.226 1   51.59  ? 241 ILE   D CD1 1 
ATOM   9863  N  N   . GLU   D 1 220 ? 51.829 48.372  72.962 1   46.59  ? 242 GLU   D N   1 
ATOM   9864  C  CA  . GLU   D 1 220 ? 50.951 48.846  74.016 1   46.56  ? 242 GLU   D CA  1 
ATOM   9865  C  C   . GLU   D 1 220 ? 50.055 49.998  73.529 1   45.84  ? 242 GLU   D C   1 
ATOM   9866  O  O   . GLU   D 1 220 ? 48.875 50.034  73.88  1   45.74  ? 242 GLU   D O   1 
ATOM   9867  C  CB  . GLU   D 1 220 ? 51.747 49.218  75.27  1   49.54  ? 242 GLU   D CB  1 
ATOM   9868  C  CG  . GLU   D 1 220 ? 50.947 49.129  76.567 1   55.82  ? 242 GLU   D CG  1 
ATOM   9869  C  CD  . GLU   D 1 220 ? 50.037 47.922  76.738 1   63.26  ? 242 GLU   D CD  1 
ATOM   9870  O  OE1 . GLU   D 1 220 ? 50.525 46.776  76.575 1   65.48  ? 242 GLU   D OE1 1 
ATOM   9871  O  OE2 . GLU   D 1 220 ? 48.829 48.127  77.014 1   64.25  ? 242 GLU   D OE2 1 
ATOM   9872  N  N   . LYS   D 1 221 ? 50.592 50.892  72.659 1   44.77  ? 243 LYS   D N   1 
ATOM   9873  C  CA  . LYS   D 1 221 ? 49.832 51.992  72.054 1   43.88  ? 243 LYS   D CA  1 
ATOM   9874  C  C   . LYS   D 1 221 ? 48.727 51.435  71.144 1   43.89  ? 243 LYS   D C   1 
ATOM   9875  O  O   . LYS   D 1 221 ? 47.621 51.985  71.107 1   44.19  ? 243 LYS   D O   1 
ATOM   9876  C  CB  . LYS   D 1 221 ? 50.753 52.917  71.259 1   44.34  ? 243 LYS   D CB  1 
ATOM   9877  C  CG  . LYS   D 1 221 ? 51.856 53.54   72.091 1   47.28  ? 243 LYS   D CG  1 
ATOM   9878  C  CD  . LYS   D 1 221 ? 51.418 54.842  72.781 1   51.17  ? 243 LYS   D CD  1 
ATOM   9879  C  CE  . LYS   D 1 221 ? 52.588 55.576  73.385 1   55.49  ? 243 LYS   D CE  1 
ATOM   9880  N  NZ  . LYS   D 1 221 ? 52.309 56.025  74.781 1   58.32  ? 243 LYS   D NZ  1 
ATOM   9881  N  N   . ARG   D 1 222 ? 49.02  50.316  70.446 1   43.13  ? 244 ARG   D N   1 
ATOM   9882  C  CA  . ARG   D 1 222 ? 48.071 49.622  69.585 1   42.83  ? 244 ARG   D CA  1 
ATOM   9883  C  C   . ARG   D 1 222 ? 46.957 49.026  70.426 1   43.72  ? 244 ARG   D C   1 
ATOM   9884  O  O   . ARG   D 1 222 ? 45.785 49.214  70.095 1   43.97  ? 244 ARG   D O   1 
ATOM   9885  C  CB  . ARG   D 1 222 ? 48.769 48.517  68.759 1   42.33  ? 244 ARG   D CB  1 
ATOM   9886  C  CG  . ARG   D 1 222 ? 49.882 49.004  67.851 1   42.58  ? 244 ARG   D CG  1 
ATOM   9887  C  CD  . ARG   D 1 222 ? 49.425 50.063  66.856 1   43.77  ? 244 ARG   D CD  1 
ATOM   9888  N  NE  . ARG   D 1 222 ? 48.367 49.569  65.979 1   43.42  ? 244 ARG   D NE  1 
ATOM   9889  C  CZ  . ARG   D 1 222 ? 47.377 50.315  65.501 1   43.48  ? 244 ARG   D CZ  1 
ATOM   9890  N  NH1 . ARG   D 1 222 ? 47.293 51.601  65.813 1   42.6   ? 244 ARG   D NH1 1 
ATOM   9891  N  NH2 . ARG   D 1 222 ? 46.456 49.779  64.717 1   42.5   ? 244 ARG   D NH2 1 
ATOM   9892  N  N   . ARG   D 1 223 ? 47.303 48.366  71.551 1   43.97  ? 245 ARG   D N   1 
ATOM   9893  C  CA  . ARG   D 1 223 ? 46.3   47.775  72.444 1   44.71  ? 245 ARG   D CA  1 
ATOM   9894  C  C   . ARG   D 1 223 ? 45.286 48.826  72.937 1   44.78  ? 245 ARG   D C   1 
ATOM   9895  O  O   . ARG   D 1 223 ? 44.091 48.537  73.024 1   45.22  ? 245 ARG   D O   1 
ATOM   9896  C  CB  . ARG   D 1 223 ? 46.964 47.069  73.634 1   46.73  ? 245 ARG   D CB  1 
ATOM   9897  C  CG  . ARG   D 1 223 ? 47.713 45.8    73.272 1   50.38  ? 245 ARG   D CG  1 
ATOM   9898  C  CD  . ARG   D 1 223 ? 48.03  44.965  74.503 1   54.64  ? 245 ARG   D CD  1 
ATOM   9899  N  NE  . ARG   D 1 223 ? 49.144 44.031  74.285 1   58.88  ? 245 ARG   D NE  1 
ATOM   9900  C  CZ  . ARG   D 1 223 ? 49.022 42.831  73.717 1   61.41  ? 245 ARG   D CZ  1 
ATOM   9901  N  NH1 . ARG   D 1 223 ? 47.839 42.41   73.281 1   61.14  ? 245 ARG   D NH1 1 
ATOM   9902  N  NH2 . ARG   D 1 223 ? 50.084 42.049  73.569 1   61.04  ? 245 ARG   D NH2 1 
ATOM   9903  N  N   . GLU   D 1 224 ? 45.763 50.047  73.215 1   44.24  ? 246 GLU   D N   1 
ATOM   9904  C  CA  . GLU   D 1 224 ? 44.958 51.178  73.659 1   44.18  ? 246 GLU   D CA  1 
ATOM   9905  C  C   . GLU   D 1 224 ? 44     51.642  72.541 1   43.77  ? 246 GLU   D C   1 
ATOM   9906  O  O   . GLU   D 1 224 ? 42.868 52.048  72.824 1   43.81  ? 246 GLU   D O   1 
ATOM   9907  C  CB  . GLU   D 1 224 ? 45.911 52.314  74.018 1   47.34  ? 246 GLU   D CB  1 
ATOM   9908  C  CG  . GLU   D 1 224 ? 45.666 52.981  75.346 1   55.86  ? 246 GLU   D CG  1 
ATOM   9909  C  CD  . GLU   D 1 224 ? 45.668 54.487  75.156 1   65.55  ? 246 GLU   D CD  1 
ATOM   9910  O  OE1 . GLU   D 1 224 ? 46.673 55.011  74.619 1   68.32  ? 246 GLU   D OE1 1 
ATOM   9911  O  OE2 . GLU   D 1 224 ? 44.66  55.14   75.515 1   67.52  ? 246 GLU   D OE2 1 
ATOM   9912  N  N   . VAL   D 1 225 ? 44.459 51.576  71.27  1   43.09  ? 247 VAL   D N   1 
ATOM   9913  C  CA  . VAL   D 1 225 ? 43.669 51.951  70.104 1   43.04  ? 247 VAL   D CA  1 
ATOM   9914  C  C   . VAL   D 1 225 ? 42.497 50.972  69.979 1   43.49  ? 247 VAL   D C   1 
ATOM   9915  O  O   . VAL   D 1 225 ? 41.343 51.397  69.841 1   43.48  ? 247 VAL   D O   1 
ATOM   9916  C  CB  . VAL   D 1 225 ? 44.553 51.972  68.818 1   43.48  ? 247 VAL   D CB  1 
ATOM   9917  C  CG1 . VAL   D 1 225 ? 43.726 51.855  67.548 1   43.89  ? 247 VAL   D CG1 1 
ATOM   9918  C  CG2 . VAL   D 1 225 ? 45.422 53.206  68.77  1   43.94  ? 247 VAL   D CG2 1 
ATOM   9919  N  N   . TYR   D 1 226 ? 42.796 49.661  70.032 1   43.47  ? 248 TYR   D N   1 
ATOM   9920  C  CA  . TYR   D 1 226 ? 41.775 48.636  69.897 1   44.08  ? 248 TYR   D CA  1 
ATOM   9921  C  C   . TYR   D 1 226 ? 40.812 48.61   71.08  1   44.7   ? 248 TYR   D C   1 
ATOM   9922  O  O   . TYR   D 1 226 ? 39.665 48.23   70.911 1   44.43  ? 248 TYR   D O   1 
ATOM   9923  C  CB  . TYR   D 1 226 ? 42.404 47.269  69.613 1   44.47  ? 248 TYR   D CB  1 
ATOM   9924  C  CG  . TYR   D 1 226 ? 43.077 47.252  68.261 1   45.88  ? 248 TYR   D CG  1 
ATOM   9925  C  CD1 . TYR   D 1 226 ? 42.353 47.477  67.101 1   46.76  ? 248 TYR   D CD1 1 
ATOM   9926  C  CD2 . TYR   D 1 226 ? 44.448 47.077  68.149 1   47.06  ? 248 TYR   D CD2 1 
ATOM   9927  C  CE1 . TYR   D 1 226 ? 42.968 47.484  65.857 1   47.85  ? 248 TYR   D CE1 1 
ATOM   9928  C  CE2 . TYR   D 1 226 ? 45.078 47.105  66.913 1   48.19  ? 248 TYR   D CE2 1 
ATOM   9929  C  CZ  . TYR   D 1 226 ? 44.333 47.296  65.767 1   49.26  ? 248 TYR   D CZ  1 
ATOM   9930  O  OH  . TYR   D 1 226 ? 44.964 47.33   64.546 1   51.36  ? 248 TYR   D OH  1 
ATOM   9931  N  N   . ARG   D 1 227 ? 41.242 49.089  72.253 1   45.33  ? 249 ARG   D N   1 
ATOM   9932  C  CA  . ARG   D 1 227 ? 40.387 49.206  73.422 1   46.27  ? 249 ARG   D CA  1 
ATOM   9933  C  C   . ARG   D 1 227 ? 39.252 50.196  73.122 1   46.27  ? 249 ARG   D C   1 
ATOM   9934  O  O   . ARG   D 1 227 ? 38.104 49.916  73.451 1   46.59  ? 249 ARG   D O   1 
ATOM   9935  C  CB  . ARG   D 1 227 ? 41.213 49.712  74.607 1   48.34  ? 249 ARG   D CB  1 
ATOM   9936  C  CG  . ARG   D 1 227 ? 40.807 49.14   75.951 1   52.96  ? 249 ARG   D CG  1 
ATOM   9937  C  CD  . ARG   D 1 227 ? 41.798 48.077  76.435 1   57.43  ? 249 ARG   D CD  1 
ATOM   9938  N  NE  . ARG   D 1 227 ? 43.177 48.577  76.513 1   60.94  ? 249 ARG   D NE  1 
ATOM   9939  C  CZ  . ARG   D 1 227 ? 44.244 47.815  76.75  1   62.69  ? 249 ARG   D CZ  1 
ATOM   9940  N  NH1 . ARG   D 1 227 ? 45.457 48.356  76.8   1   62.26  ? 249 ARG   D NH1 1 
ATOM   9941  N  NH2 . ARG   D 1 227 ? 44.105 46.51   76.958 1   62.32  ? 249 ARG   D NH2 1 
ATOM   9942  N  N   . SER   D 1 228 ? 39.568 51.311  72.431 1   45.56  ? 250 SER   D N   1 
ATOM   9943  C  CA  . SER   D 1 228 ? 38.598 52.34   72.058 1   45.28  ? 250 SER   D CA  1 
ATOM   9944  C  C   . SER   D 1 228 ? 37.531 51.876  71.059 1   44.52  ? 250 SER   D C   1 
ATOM   9945  O  O   . SER   D 1 228 ? 36.526 52.568  70.889 1   44.26  ? 250 SER   D O   1 
ATOM   9946  C  CB  . SER   D 1 228 ? 39.301 53.578  71.524 1   46.96  ? 250 SER   D CB  1 
ATOM   9947  O  OG  . SER   D 1 228 ? 39.861 53.314  70.248 1   50.04  ? 250 SER   D OG  1 
ATOM   9948  N  N   . ILE   D 1 229 ? 37.731 50.716  70.413 1   43.98  ? 251 ILE   D N   1 
ATOM   9949  C  CA  . ILE   D 1 229 ? 36.743 50.202  69.464 1   44.25  ? 251 ILE   D CA  1 
ATOM   9950  C  C   . ILE   D 1 229 ? 36.138 48.879  69.913 1   44.39  ? 251 ILE   D C   1 
ATOM   9951  O  O   . ILE   D 1 229 ? 34.974 48.616  69.62  1   44.69  ? 251 ILE   D O   1 
ATOM   9952  C  CB  . ILE   D 1 229 ? 37.247 50.128  67.997 1   44.36  ? 251 ILE   D CB  1 
ATOM   9953  C  CG1 . ILE   D 1 229 ? 38.537 49.308  67.871 1   44.88  ? 251 ILE   D CG1 1 
ATOM   9954  C  CG2 . ILE   D 1 229 ? 37.406 51.524  67.43  1   44.85  ? 251 ILE   D CG2 1 
ATOM   9955  C  CD1 . ILE   D 1 229 ? 38.861 48.879  66.478 1   46     ? 251 ILE   D CD1 1 
ATOM   9956  N  N   . PHE   D 1 230 ? 36.897 48.063  70.637 1   44.07  ? 252 PHE   D N   1 
ATOM   9957  C  CA  . PHE   D 1 230 ? 36.395 46.77   71.095 1   44.58  ? 252 PHE   D CA  1 
ATOM   9958  C  C   . PHE   D 1 230 ? 35.657 46.84   72.446 1   46.25  ? 252 PHE   D C   1 
ATOM   9959  O  O   . PHE   D 1 230 ? 35.054 45.846  72.859 1   47.14  ? 252 PHE   D O   1 
ATOM   9960  C  CB  . PHE   D 1 230 ? 37.516 45.73   71.095 1   43.78  ? 252 PHE   D CB  1 
ATOM   9961  C  CG  . PHE   D 1 230 ? 38.115 45.477  69.722 1   43.21  ? 252 PHE   D CG  1 
ATOM   9962  C  CD1 . PHE   D 1 230 ? 37.341 45.582  68.578 1   43.21  ? 252 PHE   D CD1 1 
ATOM   9963  C  CD2 . PHE   D 1 230 ? 39.439 45.101  69.584 1   43.34  ? 252 PHE   D CD2 1 
ATOM   9964  C  CE1 . PHE   D 1 230 ? 37.887 45.341  67.331 1   43.33  ? 252 PHE   D CE1 1 
ATOM   9965  C  CE2 . PHE   D 1 230 ? 39.976 44.833  68.33  1   43.57  ? 252 PHE   D CE2 1 
ATOM   9966  C  CZ  . PHE   D 1 230 ? 39.196 44.95   67.217 1   43.11  ? 252 PHE   D CZ  1 
ATOM   9967  N  N   . ASP   D 1 231 ? 35.675 48.015  73.115 1   46.25  ? 253 ASP   D N   1 
ATOM   9968  C  CA  . ASP   D 1 231 ? 34.952 48.257  74.355 1   46.77  ? 253 ASP   D CA  1 
ATOM   9969  C  C   . ASP   D 1 231 ? 33.933 49.324  74.006 1   47.31  ? 253 ASP   D C   1 
ATOM   9970  O  O   . ASP   D 1 231 ? 34.299 50.474  73.768 1   47.66  ? 253 ASP   D O   1 
ATOM   9971  C  CB  . ASP   D 1 231 ? 35.901 48.767  75.454 1   48.43  ? 253 ASP   D CB  1 
ATOM   9972  C  CG  . ASP   D 1 231 ? 35.311 48.858  76.854 1   52.28  ? 253 ASP   D CG  1 
ATOM   9973  O  OD1 . ASP   D 1 231 ? 34.063 48.797  76.982 1   53.02  ? 253 ASP   D OD1 1 
ATOM   9974  O  OD2 . ASP   D 1 231 ? 36.102 48.992  77.826 1   53.84  ? 253 ASP   D OD2 1 
ATOM   9975  N  N   . PRO   D 1 232 ? 32.642 48.957  73.94  1   47.2   ? 254 PRO   D N   1 
ATOM   9976  C  CA  . PRO   D 1 232 ? 31.612 49.944  73.576 1   47.11  ? 254 PRO   D CA  1 
ATOM   9977  C  C   . PRO   D 1 232 ? 31.493 51.103  74.558 1   47.66  ? 254 PRO   D C   1 
ATOM   9978  O  O   . PRO   D 1 232 ? 31.105 52.188  74.15  1   48.28  ? 254 PRO   D O   1 
ATOM   9979  C  CB  . PRO   D 1 232 ? 30.331 49.113  73.513 1   47.58  ? 254 PRO   D CB  1 
ATOM   9980  C  CG  . PRO   D 1 232 ? 30.793 47.703  73.378 1   47.92  ? 254 PRO   D CG  1 
ATOM   9981  C  CD  . PRO   D 1 232 ? 32.057 47.625  74.16  1   46.47  ? 254 PRO   D CD  1 
ATOM   9982  N  N   . ALA   D 1 233 ? 31.846 50.891  75.833 1   47.3   ? 255 ALA   D N   1 
ATOM   9983  C  CA  . ALA   D 1 233 ? 31.8   51.931  76.844 1   47.46  ? 255 ALA   D CA  1 
ATOM   9984  C  C   . ALA   D 1 233 ? 32.837 53.016  76.55  1   47.47  ? 255 ALA   D C   1 
ATOM   9985  O  O   . ALA   D 1 233 ? 32.54  54.2    76.717 1   47.75  ? 255 ALA   D O   1 
ATOM   9986  C  CB  . ALA   D 1 233 ? 32.037 51.328  78.215 1   47.8   ? 255 ALA   D CB  1 
ATOM   9987  N  N   . VAL   D 1 234 ? 34.039 52.62   76.093 1   47.1   ? 256 VAL   D N   1 
ATOM   9988  C  CA  . VAL   D 1 234 ? 35.093 53.572  75.731 1   47.58  ? 256 VAL   D CA  1 
ATOM   9989  C  C   . VAL   D 1 234 ? 34.681 54.383  74.488 1   48.14  ? 256 VAL   D C   1 
ATOM   9990  O  O   . VAL   D 1 234 ? 34.943 55.585  74.424 1   48.17  ? 256 VAL   D O   1 
ATOM   9991  C  CB  . VAL   D 1 234 ? 36.469 52.886  75.543 1   48.02  ? 256 VAL   D CB  1 
ATOM   9992  C  CG1 . VAL   D 1 234 ? 37.545 53.904  75.187 1   48.34  ? 256 VAL   D CG1 1 
ATOM   9993  C  CG2 . VAL   D 1 234 ? 36.864 52.131  76.793 1   48.54  ? 256 VAL   D CG2 1 
ATOM   9994  N  N   . HIS   D 1 235 ? 33.994 53.73   73.531 1   48.28  ? 257 HIS   D N   1 
ATOM   9995  C  CA  . HIS   D 1 235 ? 33.485 54.389  72.334 1   48.79  ? 257 HIS   D CA  1 
ATOM   9996  C  C   . HIS   D 1 235 ? 32.411 55.414  72.74  1   50.31  ? 257 HIS   D C   1 
ATOM   9997  O  O   . HIS   D 1 235 ? 32.499 56.569  72.331 1   50.09  ? 257 HIS   D O   1 
ATOM   9998  C  CB  . HIS   D 1 235 ? 32.919 53.367  71.316 1   48.26  ? 257 HIS   D CB  1 
ATOM   9999  C  CG  . HIS   D 1 235 ? 32.171 54.013  70.182 1   49.88  ? 257 HIS   D CG  1 
ATOM   10000 N  ND1 . HIS   D 1 235 ? 32.841 54.611  69.123 1   51.49  ? 257 HIS   D ND1 1 
ATOM   10001 C  CD2 . HIS   D 1 235 ? 30.835 54.183  70     1   50.92  ? 257 HIS   D CD2 1 
ATOM   10002 C  CE1 . HIS   D 1 235 ? 31.901 55.107  68.331 1   51.74  ? 257 HIS   D CE1 1 
ATOM   10003 N  NE2 . HIS   D 1 235 ? 30.678 54.877  68.816 1   51.85  ? 257 HIS   D NE2 1 
ATOM   10004 N  N   . ASP   D 1 236 ? 31.416 54.997  73.557 1   51.4   ? 258 ASP   D N   1 
ATOM   10005 C  CA  . ASP   D 1 236 ? 30.324 55.862  74.016 1   52.51  ? 258 ASP   D CA  1 
ATOM   10006 C  C   . ASP   D 1 236 ? 30.843 57.103  74.73  1   52.63  ? 258 ASP   D C   1 
ATOM   10007 O  O   . ASP   D 1 236 ? 30.24  58.172  74.61  1   52.8   ? 258 ASP   D O   1 
ATOM   10008 C  CB  . ASP   D 1 236 ? 29.367 55.092  74.937 1   54.93  ? 258 ASP   D CB  1 
ATOM   10009 C  CG  . ASP   D 1 236 ? 28.6   53.968  74.266 1   61.21  ? 258 ASP   D CG  1 
ATOM   10010 O  OD1 . ASP   D 1 236 ? 28.573 53.928  73.007 1   61.96  ? 258 ASP   D OD1 1 
ATOM   10011 O  OD2 . ASP   D 1 236 ? 28.034 53.117  74.998 1   64.29  ? 258 ASP   D OD2 1 
ATOM   10012 N  N   . ALA   D 1 237 ? 31.97  56.965  75.455 1   52.32  ? 259 ALA   D N   1 
ATOM   10013 C  CA  . ALA   D 1 237 ? 32.601 58.068  76.171 1   52.4   ? 259 ALA   D CA  1 
ATOM   10014 C  C   . ALA   D 1 237 ? 33.139 59.099  75.179 1   52.26  ? 259 ALA   D C   1 
ATOM   10015 O  O   . ALA   D 1 237 ? 32.954 60.298  75.385 1   53.08  ? 259 ALA   D O   1 
ATOM   10016 C  CB  . ALA   D 1 237 ? 33.717 57.547  77.06  1   52.44  ? 259 ALA   D CB  1 
ATOM   10017 N  N   . LEU   D 1 238 ? 33.748 58.633  74.083 1   51.1   ? 260 LEU   D N   1 
ATOM   10018 C  CA  . LEU   D 1 238 ? 34.285 59.489  73.022 1   50.41  ? 260 LEU   D CA  1 
ATOM   10019 C  C   . LEU   D 1 238 ? 33.189 60.171  72.216 1   50.95  ? 260 LEU   D C   1 
ATOM   10020 O  O   . LEU   D 1 238 ? 33.416 61.272  71.731 1   51.07  ? 260 LEU   D O   1 
ATOM   10021 C  CB  . LEU   D 1 238 ? 35.188 58.683  72.098 1   49.4   ? 260 LEU   D CB  1 
ATOM   10022 C  CG  . LEU   D 1 238 ? 36.508 58.285  72.707 1   49.23  ? 260 LEU   D CG  1 
ATOM   10023 C  CD1 . LEU   D 1 238 ? 37.101 57.102  71.989 1   49.31  ? 260 LEU   D CD1 1 
ATOM   10024 C  CD2 . LEU   D 1 238 ? 37.451 59.452  72.747 1   49.48  ? 260 LEU   D CD2 1 
ATOM   10025 N  N   . VAL   D 1 239 ? 32.009 59.531  72.074 1   51.31  ? 261 VAL   D N   1 
ATOM   10026 C  CA  . VAL   D 1 239 ? 30.866 60.11   71.365 1   52.28  ? 261 VAL   D CA  1 
ATOM   10027 C  C   . VAL   D 1 239 ? 30.304 61.271  72.184 1   53.63  ? 261 VAL   D C   1 
ATOM   10028 O  O   . VAL   D 1 239 ? 30.074 62.358  71.638 1   53.59  ? 261 VAL   D O   1 
ATOM   10029 C  CB  . VAL   D 1 239 ? 29.782 59.065  71.024 1   52.66  ? 261 VAL   D CB  1 
ATOM   10030 C  CG1 . VAL   D 1 239 ? 28.53  59.728  70.463 1   53.03  ? 261 VAL   D CG1 1 
ATOM   10031 C  CG2 . VAL   D 1 239 ? 30.318 58.048  70.029 1   53.23  ? 261 VAL   D CG2 1 
ATOM   10032 N  N   . ARG   D 1 240 ? 30.16  61.059  73.511 1   54.48  ? 262 ARG   D N   1 
ATOM   10033 C  CA  . ARG   D 1 240 ? 29.692 62.08   74.46  1   55.41  ? 262 ARG   D CA  1 
ATOM   10034 C  C   . ARG   D 1 240 ? 30.688 63.248  74.572 1   55.57  ? 262 ARG   D C   1 
ATOM   10035 O  O   . ARG   D 1 240 ? 30.292 64.412  74.686 1   55.35  ? 262 ARG   D O   1 
ATOM   10036 C  CB  . ARG   D 1 240 ? 29.44  61.456  75.836 1   57.06  ? 262 ARG   D CB  1 
ATOM   10037 C  CG  . ARG   D 1 240 ? 28.184 60.6    75.858 1   61.1   ? 262 ARG   D CG  1 
ATOM   10038 C  CD  . ARG   D 1 240 ? 27.852 60.124  77.265 1   65.35  ? 262 ARG   D CD  1 
ATOM   10039 N  NE  . ARG   D 1 240 ? 28.42  58.807  77.566 1   68.25  ? 262 ARG   D NE  1 
ATOM   10040 C  CZ  . ARG   D 1 240 ? 29.519 58.606  78.291 1   70.02  ? 262 ARG   D CZ  1 
ATOM   10041 N  NH1 . ARG   D 1 240 ? 30.189 59.638  78.797 1   69.26  ? 262 ARG   D NH1 1 
ATOM   10042 N  NH2 . ARG   D 1 240 ? 29.957 57.373  78.513 1   69.63  ? 262 ARG   D NH2 1 
ATOM   10043 N  N   . ARG   D 1 241 ? 31.977 62.923  74.511 1   55.6   ? 263 ARG   D N   1 
ATOM   10044 C  CA  . ARG   D 1 241 ? 33.08  63.876  74.539 1   56.24  ? 263 ARG   D CA  1 
ATOM   10045 C  C   . ARG   D 1 241 ? 33.149 64.725  73.233 1   56.02  ? 263 ARG   D C   1 
ATOM   10046 O  O   . ARG   D 1 241 ? 33.669 65.84   73.237 1   56.09  ? 263 ARG   D O   1 
ATOM   10047 C  CB  . ARG   D 1 241 ? 34.379 63.092  74.773 1   58.57  ? 263 ARG   D CB  1 
ATOM   10048 C  CG  . ARG   D 1 241 ? 35.626 63.903  74.787 1   63.68  ? 263 ARG   D CG  1 
ATOM   10049 C  CD  . ARG   D 1 241 ? 36.849 63.046  74.591 1   69.67  ? 263 ARG   D CD  1 
ATOM   10050 N  NE  . ARG   D 1 241 ? 37.575 62.812  75.839 1   74.82  ? 263 ARG   D NE  1 
ATOM   10051 C  CZ  . ARG   D 1 241 ? 38.735 62.161  75.923 1   78.58  ? 263 ARG   D CZ  1 
ATOM   10052 N  NH1 . ARG   D 1 241 ? 39.314 61.674  74.828 1   78.61  ? 263 ARG   D NH1 1 
ATOM   10053 N  NH2 . ARG   D 1 241 ? 39.328 61.995  77.102 1   79.16  ? 263 ARG   D NH2 1 
ATOM   10054 N  N   . GLY   D 1 242 ? 32.611 64.203  72.133 1   55.59  ? 264 GLY   D N   1 
ATOM   10055 C  CA  . GLY   D 1 242 ? 32.618 64.905  70.853 1   55.45  ? 264 GLY   D CA  1 
ATOM   10056 C  C   . GLY   D 1 242 ? 33.702 64.472  69.877 1   54.94  ? 264 GLY   D C   1 
ATOM   10057 O  O   . GLY   D 1 242 ? 33.748 64.967  68.75  1   55.15  ? 264 GLY   D O   1 
ATOM   10058 N  N   . ASP   D 1 243 ? 34.596 63.552  70.297 1   54.14  ? 265 ASP   D N   1 
ATOM   10059 C  CA  . ASP   D 1 243 ? 35.666 63.007  69.45  1   53.4   ? 265 ASP   D CA  1 
ATOM   10060 C  C   . ASP   D 1 243 ? 35.116 62.074  68.35  1   51.81  ? 265 ASP   D C   1 
ATOM   10061 O  O   . ASP   D 1 243 ? 35.774 61.866  67.33  1   51.96  ? 265 ASP   D O   1 
ATOM   10062 C  CB  . ASP   D 1 243 ? 36.708 62.273  70.303 1   55.81  ? 265 ASP   D CB  1 
ATOM   10063 C  CG  . ASP   D 1 243 ? 37.548 63.181  71.192 1   61.66  ? 265 ASP   D CG  1 
ATOM   10064 O  OD1 . ASP   D 1 243 ? 37.148 64.349  71.398 1   62.68  ? 265 ASP   D OD1 1 
ATOM   10065 O  OD2 . ASP   D 1 243 ? 38.601 62.719  71.691 1   64.16  ? 265 ASP   D OD2 1 
ATOM   10066 N  N   . ARG   D 1 244 ? 33.918 61.507  68.569 1   50.03  ? 266 ARG   D N   1 
ATOM   10067 C  CA  . ARG   D 1 244 ? 33.218 60.646  67.629 1   48.75  ? 266 ARG   D CA  1 
ATOM   10068 C  C   . ARG   D 1 244 ? 31.737 61.061  67.528 1   48.71  ? 266 ARG   D C   1 
ATOM   10069 O  O   . ARG   D 1 244 ? 31.177 61.669  68.438 1   48.87  ? 266 ARG   D O   1 
ATOM   10070 C  CB  . ARG   D 1 244 ? 33.351 59.173  68.039 1   48.21  ? 266 ARG   D CB  1 
ATOM   10071 C  CG  . ARG   D 1 244 ? 34.75  58.64   67.835 1   47.96  ? 266 ARG   D CG  1 
ATOM   10072 C  CD  . ARG   D 1 244 ? 34.881 57.186  68.185 1   48.3   ? 266 ARG   D CD  1 
ATOM   10073 N  NE  . ARG   D 1 244 ? 36.29  56.794  68.256 1   49.2   ? 266 ARG   D NE  1 
ATOM   10074 C  CZ  . ARG   D 1 244 ? 36.72  55.613  68.688 1   50.53  ? 266 ARG   D CZ  1 
ATOM   10075 N  NH1 . ARG   D 1 244 ? 35.852 54.684  69.081 1   50.67  ? 266 ARG   D NH1 1 
ATOM   10076 N  NH2 . ARG   D 1 244 ? 38.02  55.354  68.742 1   48.76  ? 266 ARG   D NH2 1 
ATOM   10077 N  N   . ARG   D 1 245 ? 31.12  60.747  66.407 1   48.34  ? 267 ARG   D N   1 
ATOM   10078 C  CA  . ARG   D 1 245 ? 29.721 61.048  66.119 1   48.66  ? 267 ARG   D CA  1 
ATOM   10079 C  C   . ARG   D 1 245 ? 28.943 59.768  65.861 1   48.13  ? 267 ARG   D C   1 
ATOM   10080 O  O   . ARG   D 1 245 ? 27.778 59.656  66.246 1   48.68  ? 267 ARG   D O   1 
ATOM   10081 C  CB  . ARG   D 1 245 ? 29.62  61.937  64.861 1   50.68  ? 267 ARG   D CB  1 
ATOM   10082 C  CG  . ARG   D 1 245 ? 29.73  63.419  65.13  1   55.24  ? 267 ARG   D CG  1 
ATOM   10083 C  CD  . ARG   D 1 245 ? 30.721 64.048  64.193 1   60     ? 267 ARG   D CD  1 
ATOM   10084 N  NE  . ARG   D 1 245 ? 30.588 65.503  64.149 1   65.07  ? 267 ARG   D NE  1 
ATOM   10085 C  CZ  . ARG   D 1 245 ? 31.261 66.343  64.929 1   69.46  ? 267 ARG   D CZ  1 
ATOM   10086 N  NH1 . ARG   D 1 245 ? 32.122 65.88   65.829 1   69.37  ? 267 ARG   D NH1 1 
ATOM   10087 N  NH2 . ARG   D 1 245 ? 31.081 67.651  64.815 1   70.5   ? 267 ARG   D NH2 1 
ATOM   10088 N  N   . PHE   D 1 246 ? 29.58  58.819  65.165 1   47.14  ? 268 PHE   D N   1 
ATOM   10089 C  CA  . PHE   D 1 246 ? 29.012 57.553  64.733 1   46.37  ? 268 PHE   D CA  1 
ATOM   10090 C  C   . PHE   D 1 246 ? 28.569 56.685  65.865 1   46.04  ? 268 PHE   D C   1 
ATOM   10091 O  O   . PHE   D 1 246 ? 29.169 56.696  66.94  1   46.75  ? 268 PHE   D O   1 
ATOM   10092 C  CB  . PHE   D 1 246 ? 30.042 56.769  63.906 1   45.88  ? 268 PHE   D CB  1 
ATOM   10093 C  CG  . PHE   D 1 246 ? 30.199 57.181  62.46  1   46.01  ? 268 PHE   D CG  1 
ATOM   10094 C  CD1 . PHE   D 1 246 ? 29.974 58.488  62.064 1   46.93  ? 268 PHE   D CD1 1 
ATOM   10095 C  CD2 . PHE   D 1 246 ? 30.64  56.283  61.516 1   46.09  ? 268 PHE   D CD2 1 
ATOM   10096 C  CE1 . PHE   D 1 246 ? 30.149 58.872  60.75  1   47.24  ? 268 PHE   D CE1 1 
ATOM   10097 C  CE2 . PHE   D 1 246 ? 30.826 56.675  60.21  1   46.9   ? 268 PHE   D CE2 1 
ATOM   10098 C  CZ  . PHE   D 1 246 ? 30.573 57.965  59.832 1   46.97  ? 268 PHE   D CZ  1 
ATOM   10099 N  N   . SER   D 1 247 ? 27.544 55.875  65.608 1   44.88  ? 269 SER   D N   1 
ATOM   10100 C  CA  . SER   D 1 247 ? 27.129 54.86   66.554 1   44.12  ? 269 SER   D CA  1 
ATOM   10101 C  C   . SER   D 1 247 ? 28.2   53.762  66.517 1   43.82  ? 269 SER   D C   1 
ATOM   10102 O  O   . SER   D 1 247 ? 28.922 53.638  65.512 1   44.18  ? 269 SER   D O   1 
ATOM   10103 C  CB  . SER   D 1 247 ? 25.794 54.272  66.124 1   45.08  ? 269 SER   D CB  1 
ATOM   10104 O  OG  . SER   D 1 247 ? 25.906 53.528  64.92  1   47.51  ? 269 SER   D OG  1 
ATOM   10105 N  N   . HIS   D 1 248 ? 28.292 52.94   67.565 1   43.32  ? 270 HIS   D N   1 
ATOM   10106 C  CA  . HIS   D 1 248 ? 29.264 51.846  67.583 1   43.92  ? 270 HIS   D CA  1 
ATOM   10107 C  C   . HIS   D 1 248 ? 29.135 50.92   66.337 1   44.41  ? 270 HIS   D C   1 
ATOM   10108 O  O   . HIS   D 1 248 ? 30.125 50.693  65.645 1   44.97  ? 270 HIS   D O   1 
ATOM   10109 C  CB  . HIS   D 1 248 ? 29.144 51.052  68.885 1   44.94  ? 270 HIS   D CB  1 
ATOM   10110 C  CG  . HIS   D 1 248 ? 30.273 50.096  69.112 1   47.38  ? 270 HIS   D CG  1 
ATOM   10111 N  ND1 . HIS   D 1 248 ? 31.571 50.541  69.257 1   49.36  ? 270 HIS   D ND1 1 
ATOM   10112 C  CD2 . HIS   D 1 248 ? 30.258 48.752  69.251 1   48.63  ? 270 HIS   D CD2 1 
ATOM   10113 C  CE1 . HIS   D 1 248 ? 32.306 49.46   69.452 1   49.73  ? 270 HIS   D CE1 1 
ATOM   10114 N  NE2 . HIS   D 1 248 ? 31.566 48.359  69.448 1   49.68  ? 270 HIS   D NE2 1 
ATOM   10115 N  N   . ARG   D 1 249 ? 27.904 50.51   65.989 1   44.06  ? 271 ARG   D N   1 
ATOM   10116 C  CA  . ARG   D 1 249 ? 27.673 49.652  64.827 1   44.79  ? 271 ARG   D CA  1 
ATOM   10117 C  C   . ARG   D 1 249 ? 27.973 50.319  63.471 1   44.63  ? 271 ARG   D C   1 
ATOM   10118 O  O   . ARG   D 1 249 ? 28.401 49.625  62.541 1   44.18  ? 271 ARG   D O   1 
ATOM   10119 C  CB  . ARG   D 1 249 ? 26.253 49.072  64.844 1   46.73  ? 271 ARG   D CB  1 
ATOM   10120 C  CG  . ARG   D 1 249 ? 26.083 47.892  63.897 1   50.02  ? 271 ARG   D CG  1 
ATOM   10121 C  CD  . ARG   D 1 249 ? 24.866 47.071  64.253 1   52.79  ? 271 ARG   D CD  1 
ATOM   10122 N  NE  . ARG   D 1 249 ? 24.603 46.022  63.269 1   55.53  ? 271 ARG   D NE  1 
ATOM   10123 C  CZ  . ARG   D 1 249 ? 25.128 44.801  63.313 1   57.83  ? 271 ARG   D CZ  1 
ATOM   10124 N  NH1 . ARG   D 1 249 ? 25.974 44.467  64.283 1   57.5   ? 271 ARG   D NH1 1 
ATOM   10125 N  NH2 . ARG   D 1 249 ? 24.825 43.909  62.382 1   58.21  ? 271 ARG   D NH2 1 
ATOM   10126 N  N   . ALA   D 1 250 ? 27.773 51.659  63.361 1   44.34  ? 272 ALA   D N   1 
ATOM   10127 C  CA  . ALA   D 1 250 ? 28.104 52.369  62.123 1   44.19  ? 272 ALA   D CA  1 
ATOM   10128 C  C   . ALA   D 1 250 ? 29.633 52.399  61.951 1   44.1   ? 272 ALA   D C   1 
ATOM   10129 O  O   . ALA   D 1 250 ? 30.118 52.231  60.837 1   44.38  ? 272 ALA   D O   1 
ATOM   10130 C  CB  . ALA   D 1 250 ? 27.55  53.778  62.142 1   44.19  ? 272 ALA   D CB  1 
ATOM   10131 N  N   . LEU   D 1 251 ? 30.386 52.551  63.055 1   43.3   ? 273 LEU   D N   1 
ATOM   10132 C  CA  . LEU   D 1 251 ? 31.843 52.522  63.037 1   43.36  ? 273 LEU   D CA  1 
ATOM   10133 C  C   . LEU   D 1 251 ? 32.367 51.122  62.651 1   43.26  ? 273 LEU   D C   1 
ATOM   10134 O  O   . LEU   D 1 251 ? 33.393 51.007  61.991 1   43.64  ? 273 LEU   D O   1 
ATOM   10135 C  CB  . LEU   D 1 251 ? 32.385 52.928  64.42  1   43.71  ? 273 LEU   D CB  1 
ATOM   10136 C  CG  . LEU   D 1 251 ? 33.894 53.057  64.518 1   44.84  ? 273 LEU   D CG  1 
ATOM   10137 C  CD1 . LEU   D 1 251 ? 34.394 54.156  63.623 1   45.76  ? 273 LEU   D CD1 1 
ATOM   10138 C  CD2 . LEU   D 1 251 ? 34.326 53.312  65.925 1   45.33  ? 273 LEU   D CD2 1 
ATOM   10139 N  N   . GLN   D 1 252 ? 31.654 50.061  63.042 1   42.78  ? 274 GLN   D N   1 
ATOM   10140 C  CA  . GLN   D 1 252 ? 32.025 48.693  62.677 1   42.11  ? 274 GLN   D CA  1 
ATOM   10141 C  C   . GLN   D 1 252 ? 31.895 48.531  61.158 1   41.24  ? 274 GLN   D C   1 
ATOM   10142 O  O   . GLN   D 1 252 ? 32.808 48.023  60.522 1   40.78  ? 274 GLN   D O   1 
ATOM   10143 C  CB  . GLN   D 1 252 ? 31.125 47.67   63.403 1   43.74  ? 274 GLN   D CB  1 
ATOM   10144 C  CG  . GLN   D 1 252 ? 31.229 47.701  64.923 1   47.22  ? 274 GLN   D CG  1 
ATOM   10145 C  CD  . GLN   D 1 252 ? 30.317 46.702  65.592 1   53.21  ? 274 GLN   D CD  1 
ATOM   10146 O  OE1 . GLN   D 1 252 ? 29.646 45.864  64.955 1   54.33  ? 274 GLN   D OE1 1 
ATOM   10147 N  NE2 . GLN   D 1 252 ? 30.269 46.769  66.913 1   54.51  ? 274 GLN   D NE2 1 
ATOM   10148 N  N   . GLY   D 1 253 ? 30.775 48.997  60.595 1   40.94  ? 275 GLY   D N   1 
ATOM   10149 C  CA  . GLY   D 1 253 ? 30.511 48.945  59.163 1   40.8   ? 275 GLY   D CA  1 
ATOM   10150 C  C   . GLY   D 1 253 ? 31.492 49.788  58.362 1   41.13  ? 275 GLY   D C   1 
ATOM   10151 O  O   . GLY   D 1 253 ? 31.952 49.363  57.3   1   41.63  ? 275 GLY   D O   1 
ATOM   10152 N  N   . ALA   D 1 254 ? 31.857 50.984  58.88  1   40.3   ? 276 ALA   D N   1 
ATOM   10153 C  CA  . ALA   D 1 254 ? 32.816 51.862  58.227 1   39.33  ? 276 ALA   D CA  1 
ATOM   10154 C  C   . ALA   D 1 254 ? 34.192 51.204  58.205 1   38.83  ? 276 ALA   D C   1 
ATOM   10155 O  O   . ALA   D 1 254 ? 34.836 51.187  57.157 1   39.03  ? 276 ALA   D O   1 
ATOM   10156 C  CB  . ALA   D 1 254 ? 32.865 53.21   58.933 1   39.21  ? 276 ALA   D CB  1 
ATOM   10157 N  N   . ILE   D 1 255 ? 34.62  50.617  59.337 1   38.22  ? 277 ILE   D N   1 
ATOM   10158 C  CA  . ILE   D 1 255 ? 35.898 49.913  59.431 1   38.55  ? 277 ILE   D CA  1 
ATOM   10159 C  C   . ILE   D 1 255 ? 35.938 48.726  58.453 1   39.93  ? 277 ILE   D C   1 
ATOM   10160 O  O   . ILE   D 1 255 ? 36.924 48.545  57.741 1   39.9   ? 277 ILE   D O   1 
ATOM   10161 C  CB  . ILE   D 1 255 ? 36.166 49.489  60.901 1   38.12  ? 277 ILE   D CB  1 
ATOM   10162 C  CG1 . ILE   D 1 255 ? 36.636 50.699  61.722 1   38.53  ? 277 ILE   D CG1 1 
ATOM   10163 C  CG2 . ILE   D 1 255 ? 37.174 48.324  61.02  1   38.24  ? 277 ILE   D CG2 1 
ATOM   10164 C  CD1 . ILE   D 1 255 ? 36.644 50.489  63.195 1   39.14  ? 277 ILE   D CD1 1 
ATOM   10165 N  N   . MET   D 1 256 ? 34.844 47.957  58.387 1   40.72  ? 278 MET   D N   1 
ATOM   10166 C  CA  . MET   D 1 256 ? 34.734 46.794  57.52  1   41.44  ? 278 MET   D CA  1 
ATOM   10167 C  C   . MET   D 1 256 ? 34.895 47.167  56.048 1   42.6   ? 278 MET   D C   1 
ATOM   10168 O  O   . MET   D 1 256 ? 35.656 46.518  55.329 1   43.52  ? 278 MET   D O   1 
ATOM   10169 C  CB  . MET   D 1 256 ? 33.406 46.079  57.745 1   41.9   ? 278 MET   D CB  1 
ATOM   10170 C  CG  . MET   D 1 256 ? 33.381 44.749  57.116 1   45.05  ? 278 MET   D CG  1 
ATOM   10171 S  SD  . MET   D 1 256 ? 31.801 43.908  57.243 1   52.51  ? 278 MET   D SD  1 
ATOM   10172 C  CE  . MET   D 1 256 ? 32.222 42.427  56.373 1   50.01  ? 278 MET   D CE  1 
ATOM   10173 N  N   . ILE   D 1 257 ? 34.224 48.231  55.609 1   42.14  ? 279 ILE   D N   1 
ATOM   10174 C  CA  . ILE   D 1 257 ? 34.321 48.716  54.236 1   41.84  ? 279 ILE   D CA  1 
ATOM   10175 C  C   . ILE   D 1 257 ? 35.768 49.124  53.892 1   41.97  ? 279 ILE   D C   1 
ATOM   10176 O  O   . ILE   D 1 257 ? 36.251 48.807  52.812 1   42.2   ? 279 ILE   D O   1 
ATOM   10177 C  CB  . ILE   D 1 257 ? 33.311 49.87   54.042 1   41.7   ? 279 ILE   D CB  1 
ATOM   10178 C  CG1 . ILE   D 1 257 ? 31.876 49.335  54.031 1   42.72  ? 279 ILE   D CG1 1 
ATOM   10179 C  CG2 . ILE   D 1 257 ? 33.605 50.653  52.787 1   41.84  ? 279 ILE   D CG2 1 
ATOM   10180 C  CD1 . ILE   D 1 257 ? 30.802 50.418  54.035 1   44.4   ? 279 ILE   D CD1 1 
ATOM   10181 N  N   . THR   D 1 258 ? 36.465 49.803  54.817 1   41.73  ? 280 THR   D N   1 
ATOM   10182 C  CA  . THR   D 1 258 ? 37.843 50.232  54.582 1   41.68  ? 280 THR   D CA  1 
ATOM   10183 C  C   . THR   D 1 258 ? 38.83  49.061  54.512 1   43.26  ? 280 THR   D C   1 
ATOM   10184 O  O   . THR   D 1 258 ? 39.915 49.208  53.944 1   43.47  ? 280 THR   D O   1 
ATOM   10185 C  CB  . THR   D 1 258 ? 38.278 51.293  55.6   1   41.45  ? 280 THR   D CB  1 
ATOM   10186 O  OG1 . THR   D 1 258 ? 38.239 50.757  56.921 1   42.18  ? 280 THR   D OG1 1 
ATOM   10187 C  CG2 . THR   D 1 258 ? 37.463 52.557  55.519 1   40.91  ? 280 THR   D CG2 1 
ATOM   10188 N  N   . PHE   D 1 259 ? 38.473 47.907  55.098 1   44.22  ? 281 PHE   D N   1 
ATOM   10189 C  CA  . PHE   D 1 259 ? 39.322 46.719  55.094 1   45.42  ? 281 PHE   D CA  1 
ATOM   10190 C  C   . PHE   D 1 259 ? 39.209 45.964  53.76  1   46.17  ? 281 PHE   D C   1 
ATOM   10191 O  O   . PHE   D 1 259 ? 40.191 45.422  53.253 1   46.28  ? 281 PHE   D O   1 
ATOM   10192 C  CB  . PHE   D 1 259 ? 38.913 45.794  56.238 1   45.86  ? 281 PHE   D CB  1 
ATOM   10193 C  CG  . PHE   D 1 259 ? 39.608 46.022  57.56  1   47.42  ? 281 PHE   D CG  1 
ATOM   10194 C  CD1 . PHE   D 1 259 ? 40.061 47.277  57.917 1   48.61  ? 281 PHE   D CD1 1 
ATOM   10195 C  CD2 . PHE   D 1 259 ? 39.768 44.988  58.464 1   48.47  ? 281 PHE   D CD2 1 
ATOM   10196 C  CE1 . PHE   D 1 259 ? 40.683 47.488  59.14  1   49.51  ? 281 PHE   D CE1 1 
ATOM   10197 C  CE2 . PHE   D 1 259 ? 40.413 45.199  59.675 1   49.4   ? 281 PHE   D CE2 1 
ATOM   10198 C  CZ  . PHE   D 1 259 ? 40.864 46.449  60.007 1   49.27  ? 281 PHE   D CZ  1 
ATOM   10199 N  N   . TYR   D 1 260 ? 38.002 45.918  53.201 1   46.27  ? 282 TYR   D N   1 
ATOM   10200 C  CA  . TYR   D 1 260 ? 37.742 45.177  51.98  1   46.77  ? 282 TYR   D CA  1 
ATOM   10201 C  C   . TYR   D 1 260 ? 37.414 46.071  50.794 1   47.57  ? 282 TYR   D C   1 
ATOM   10202 O  O   . TYR   D 1 260 ? 36.713 45.629  49.886 1   47.69  ? 282 TYR   D O   1 
ATOM   10203 C  CB  . TYR   D 1 260 ? 36.604 44.165  52.21  1   46.46  ? 282 TYR   D CB  1 
ATOM   10204 C  CG  . TYR   D 1 260 ? 36.832 43.259  53.395 1   46.87  ? 282 TYR   D CG  1 
ATOM   10205 C  CD1 . TYR   D 1 260 ? 37.78  42.256  53.352 1   47.98  ? 282 TYR   D CD1 1 
ATOM   10206 C  CD2 . TYR   D 1 260 ? 36.103 43.413  54.565 1   47.73  ? 282 TYR   D CD2 1 
ATOM   10207 C  CE1 . TYR   D 1 260 ? 37.998 41.422  54.44  1   49.06  ? 282 TYR   D CE1 1 
ATOM   10208 C  CE2 . TYR   D 1 260 ? 36.323 42.597  55.667 1   48.72  ? 282 TYR   D CE2 1 
ATOM   10209 C  CZ  . TYR   D 1 260 ? 37.275 41.601  55.601 1   49.68  ? 282 TYR   D CZ  1 
ATOM   10210 O  OH  . TYR   D 1 260 ? 37.505 40.768  56.668 1   50.85  ? 282 TYR   D OH  1 
ATOM   10211 N  N   . ARG   D 1 261 ? 37.964 47.298  50.772 1   47.76  ? 283 ARG   D N   1 
ATOM   10212 C  CA  . ARG   D 1 261 ? 37.748 48.286  49.715 1   48.31  ? 283 ARG   D CA  1 
ATOM   10213 C  C   . ARG   D 1 261 ? 38.218 47.821  48.33  1   48.73  ? 283 ARG   D C   1 
ATOM   10214 O  O   . ARG   D 1 261 ? 37.714 48.304  47.316 1   48.24  ? 283 ARG   D O   1 
ATOM   10215 C  CB  . ARG   D 1 261 ? 38.426 49.61   50.09  1   49.6   ? 283 ARG   D CB  1 
ATOM   10216 C  CG  . ARG   D 1 261 ? 39.912 49.458  50.327 1   52.44  ? 283 ARG   D CG  1 
ATOM   10217 C  CD  . ARG   D 1 261 ? 40.574 50.792  50.528 1   56.84  ? 283 ARG   D CD  1 
ATOM   10218 N  NE  . ARG   D 1 261 ? 40.687 51.548  49.281 1   60.46  ? 283 ARG   D NE  1 
ATOM   10219 C  CZ  . ARG   D 1 261 ? 41.193 52.778  49.195 1   63.22  ? 283 ARG   D CZ  1 
ATOM   10220 N  NH1 . ARG   D 1 261 ? 41.624 53.405  50.283 1   61.93  ? 283 ARG   D NH1 1 
ATOM   10221 N  NH2 . ARG   D 1 261 ? 41.26  53.394  48.02  1   64.22  ? 283 ARG   D NH2 1 
ATOM   10222 N  N   . ASP   D 1 262 ? 39.187 46.893  48.285 1   49.6   ? 284 ASP   D N   1 
ATOM   10223 C  CA  . ASP   D 1 262 ? 39.683 46.372  47.011 1   50.88  ? 284 ASP   D CA  1 
ATOM   10224 C  C   . ASP   D 1 262 ? 38.763 45.274  46.42  1   51.86  ? 284 ASP   D C   1 
ATOM   10225 O  O   . ASP   D 1 262 ? 38.889 44.951  45.238 1   51.59  ? 284 ASP   D O   1 
ATOM   10226 C  CB  . ASP   D 1 262 ? 41.153 45.913  47.115 1   52.54  ? 284 ASP   D CB  1 
ATOM   10227 C  CG  . ASP   D 1 262 ? 42.169 47.05   47.089 1   57.94  ? 284 ASP   D CG  1 
ATOM   10228 O  OD1 . ASP   D 1 262 ? 41.828 48.15   46.575 1   58.32  ? 284 ASP   D OD1 1 
ATOM   10229 O  OD2 . ASP   D 1 262 ? 43.317 46.836  47.56  1   61.06  ? 284 ASP   D OD2 1 
ATOM   10230 N  N   . GLU   D 1 263 ? 37.806 44.746  47.23  1   52.76  ? 285 GLU   D N   1 
ATOM   10231 C  CA  . GLU   D 1 263 ? 36.823 43.746  46.809 1   53.46  ? 285 GLU   D CA  1 
ATOM   10232 C  C   . GLU   D 1 263 ? 35.638 44.424  46.149 1   53.19  ? 285 GLU   D C   1 
ATOM   10233 O  O   . GLU   D 1 263 ? 35.139 45.426  46.65  1   52.7   ? 285 GLU   D O   1 
ATOM   10234 C  CB  . GLU   D 1 263 ? 36.332 42.916  48.001 1   57.05  ? 285 GLU   D CB  1 
ATOM   10235 C  CG  . GLU   D 1 263 ? 37.45  42.212  48.74  1   64.1   ? 285 GLU   D CG  1 
ATOM   10236 C  CD  . GLU   D 1 263 ? 38.281 41.281  47.886 1   72.93  ? 285 GLU   D CD  1 
ATOM   10237 O  OE1 . GLU   D 1 263 ? 37.69  40.557  47.051 1   74.97  ? 285 GLU   D OE1 1 
ATOM   10238 O  OE2 . GLU   D 1 263 ? 39.523 41.277  48.051 1   76.13  ? 285 GLU   D OE2 1 
ATOM   10239 N  N   . PRO   D 1 264 ? 35.153 43.856  45.034 1   53.51  ? 286 PRO   D N   1 
ATOM   10240 C  CA  . PRO   D 1 264 ? 34.039 44.49   44.303 1   53.83  ? 286 PRO   D CA  1 
ATOM   10241 C  C   . PRO   D 1 264 ? 32.801 44.837  45.136 1   54.43  ? 286 PRO   D C   1 
ATOM   10242 O  O   . PRO   D 1 264 ? 32.16  45.889  44.912 1   54.01  ? 286 PRO   D O   1 
ATOM   10243 C  CB  . PRO   D 1 264 ? 33.73  43.477  43.204 1   54.22  ? 286 PRO   D CB  1 
ATOM   10244 C  CG  . PRO   D 1 264 ? 35.032 42.779  42.974 1   54.38  ? 286 PRO   D CG  1 
ATOM   10245 C  CD  . PRO   D 1 264 ? 35.678 42.678  44.312 1   52.87  ? 286 PRO   D CD  1 
ATOM   10246 N  N   . ARG   D 1 265 ? 32.491 43.976  46.123 1   54.64  ? 287 ARG   D N   1 
ATOM   10247 C  CA  . ARG   D 1 265 ? 31.352 44.16   47.018 1   55.27  ? 287 ARG   D CA  1 
ATOM   10248 C  C   . ARG   D 1 265 ? 31.44  45.454  47.813 1   54.11  ? 287 ARG   D C   1 
ATOM   10249 O  O   . ARG   D 1 265 ? 30.418 46.084  48.073 1   54.25  ? 287 ARG   D O   1 
ATOM   10250 C  CB  . ARG   D 1 265 ? 31.285 42.988  47.998 1   58.7   ? 287 ARG   D CB  1 
ATOM   10251 C  CG  . ARG   D 1 265 ? 30.173 41.992  47.696 1   65.7   ? 287 ARG   D CG  1 
ATOM   10252 C  CD  . ARG   D 1 265 ? 30.348 40.666  48.444 1   71.98  ? 287 ARG   D CD  1 
ATOM   10253 N  NE  . ARG   D 1 265 ? 30.583 40.834  49.882 1   77.82  ? 287 ARG   D NE  1 
ATOM   10254 C  CZ  . ARG   D 1 265 ? 29.627 41.069  50.777 1   82.67  ? 287 ARG   D CZ  1 
ATOM   10255 N  NH1 . ARG   D 1 265 ? 28.36  41.189  50.392 1   83.75  ? 287 ARG   D NH1 1 
ATOM   10256 N  NH2 . ARG   D 1 265 ? 29.931 41.202  52.062 1   82.97  ? 287 ARG   D NH2 1 
ATOM   10257 N  N   . PHE   D 1 266 ? 32.654 45.84   48.212 1   52.95  ? 288 PHE   D N   1 
ATOM   10258 C  CA  . PHE   D 1 266 ? 32.876 47.018  49.047 1   52.49  ? 288 PHE   D CA  1 
ATOM   10259 C  C   . PHE   D 1 266 ? 33.541 48.192  48.348 1   51.65  ? 288 PHE   D C   1 
ATOM   10260 O  O   . PHE   D 1 266 ? 33.783 49.201  49.001 1   51.47  ? 288 PHE   D O   1 
ATOM   10261 C  CB  . PHE   D 1 266 ? 33.717 46.644  50.278 1   52.44  ? 288 PHE   D CB  1 
ATOM   10262 C  CG  . PHE   D 1 266 ? 33.079 45.628  51.187 1   53.6   ? 288 PHE   D CG  1 
ATOM   10263 C  CD1 . PHE   D 1 266 ? 33.321 44.275  51.018 1   54.43  ? 288 PHE   D CD1 1 
ATOM   10264 C  CD2 . PHE   D 1 266 ? 32.249 46.024  52.223 1   54.77  ? 288 PHE   D CD2 1 
ATOM   10265 C  CE1 . PHE   D 1 266 ? 32.753 43.341  51.873 1   55.16  ? 288 PHE   D CE1 1 
ATOM   10266 C  CE2 . PHE   D 1 266 ? 31.663 45.083  53.065 1   55.44  ? 288 PHE   D CE2 1 
ATOM   10267 C  CZ  . PHE   D 1 266 ? 31.918 43.749  52.883 1   55.09  ? 288 PHE   D CZ  1 
ATOM   10268 N  N   . SER   D 1 267 ? 33.86  48.076  47.053 1   51.16  ? 289 SER   D N   1 
ATOM   10269 C  CA  . SER   D 1 267 ? 34.527 49.162  46.334 1   50.81  ? 289 SER   D CA  1 
ATOM   10270 C  C   . SER   D 1 267 ? 33.645 50.404  46.193 1   49.54  ? 289 SER   D C   1 
ATOM   10271 O  O   . SER   D 1 267 ? 34.123 51.519  46.404 1   49.65  ? 289 SER   D O   1 
ATOM   10272 C  CB  . SER   D 1 267 ? 35.037 48.687  44.974 1   52.67  ? 289 SER   D CB  1 
ATOM   10273 O  OG  . SER   D 1 267 ? 33.983 48.542  44.036 1   55.72  ? 289 SER   D OG  1 
ATOM   10274 N  N   . GLN   D 1 268 ? 32.369 50.217  45.837 1   48.45  ? 290 GLN   D N   1 
ATOM   10275 C  CA  . GLN   D 1 268 ? 31.455 51.349  45.687 1   48.18  ? 290 GLN   D CA  1 
ATOM   10276 C  C   . GLN   D 1 268 ? 31.051 51.935  47.05  1   47.36  ? 290 GLN   D C   1 
ATOM   10277 O  O   . GLN   D 1 268 ? 31.181 53.155  47.213 1   47.73  ? 290 GLN   D O   1 
ATOM   10278 C  CB  . GLN   D 1 268 ? 30.261 51.006  44.779 1   49.98  ? 290 GLN   D CB  1 
ATOM   10279 C  CG  . GLN   D 1 268 ? 30.028 51.987  43.613 1   53.05  ? 290 GLN   D CG  1 
ATOM   10280 C  CD  . GLN   D 1 268 ? 31.257 52.438  42.838 1   56.94  ? 290 GLN   D CD  1 
ATOM   10281 O  OE1 . GLN   D 1 268 ? 32.2   51.671  42.569 1   57.9   ? 290 GLN   D OE1 1 
ATOM   10282 N  NE2 . GLN   D 1 268 ? 31.255 53.713  42.45  1   57.24  ? 290 GLN   D NE2 1 
ATOM   10283 N  N   . PRO   D 1 269 ? 30.71  51.121  48.09  1   45.81  ? 291 PRO   D N   1 
ATOM   10284 C  CA  . PRO   D 1 269 ? 30.476 51.708  49.418 1   44.54  ? 291 PRO   D CA  1 
ATOM   10285 C  C   . PRO   D 1 269 ? 31.658 52.548  49.924 1   43.04  ? 291 PRO   D C   1 
ATOM   10286 O  O   . PRO   D 1 269 ? 31.429 53.6    50.504 1   42.49  ? 291 PRO   D O   1 
ATOM   10287 C  CB  . PRO   D 1 269 ? 30.252 50.478  50.304 1   45.35  ? 291 PRO   D CB  1 
ATOM   10288 C  CG  . PRO   D 1 269 ? 29.756 49.43   49.374 1   45.89  ? 291 PRO   D CG  1 
ATOM   10289 C  CD  . PRO   D 1 269 ? 30.521 49.654  48.119 1   44.82  ? 291 PRO   D CD  1 
ATOM   10290 N  N   . HIS   D 1 270 ? 32.911 52.119  49.658 1   42.44  ? 292 HIS   D N   1 
ATOM   10291 C  CA  . HIS   D 1 270 ? 34.113 52.851  50.059 1   42.59  ? 292 HIS   D CA  1 
ATOM   10292 C  C   . HIS   D 1 270 ? 34.251 54.165  49.31  1   42.61  ? 292 HIS   D C   1 
ATOM   10293 O  O   . HIS   D 1 270 ? 34.657 55.174  49.89  1   43.14  ? 292 HIS   D O   1 
ATOM   10294 C  CB  . HIS   D 1 270 ? 35.385 52.018  49.872 1   44.17  ? 292 HIS   D CB  1 
ATOM   10295 C  CG  . HIS   D 1 270 ? 36.597 52.718  50.4   1   47.62  ? 292 HIS   D CG  1 
ATOM   10296 N  ND1 . HIS   D 1 270 ? 36.813 52.857  51.769 1   49.36  ? 292 HIS   D ND1 1 
ATOM   10297 C  CD2 . HIS   D 1 270 ? 37.569 53.382  49.733 1   49.39  ? 292 HIS   D CD2 1 
ATOM   10298 C  CE1 . HIS   D 1 270 ? 37.929 53.559  51.888 1   50.22  ? 292 HIS   D CE1 1 
ATOM   10299 N  NE2 . HIS   D 1 270 ? 38.423 53.897  50.693 1   50.81  ? 292 HIS   D NE2 1 
ATOM   10300 N  N   . GLN   D 1 271 ? 33.905 54.165  48.027 1   41.82  ? 293 GLN   D N   1 
ATOM   10301 C  CA  . GLN   D 1 271 ? 33.929 55.372  47.222 1   41.82  ? 293 GLN   D CA  1 
ATOM   10302 C  C   . GLN   D 1 271 ? 32.927 56.413  47.782 1   41.09  ? 293 GLN   D C   1 
ATOM   10303 O  O   . GLN   D 1 271 ? 33.233 57.6    47.824 1   40.61  ? 293 GLN   D O   1 
ATOM   10304 C  CB  . GLN   D 1 271 ? 33.657 55.016  45.744 1   44.41  ? 293 GLN   D CB  1 
ATOM   10305 C  CG  . GLN   D 1 271 ? 33.85  56.172  44.764 1   50.83  ? 293 GLN   D CG  1 
ATOM   10306 C  CD  . GLN   D 1 271 ? 35.192 56.884  44.891 1   59.09  ? 293 GLN   D CD  1 
ATOM   10307 O  OE1 . GLN   D 1 271 ? 36.236 56.29   45.224 1   62.17  ? 293 GLN   D OE1 1 
ATOM   10308 N  NE2 . GLN   D 1 271 ? 35.197 58.185  44.618 1   59.98  ? 293 GLN   D NE2 1 
ATOM   10309 N  N   . LEU   D 1 272 ? 31.779 55.944  48.292 1   40.96  ? 294 LEU   D N   1 
ATOM   10310 C  CA  . LEU   D 1 272 ? 30.756 56.775  48.916 1   41.55  ? 294 LEU   D CA  1 
ATOM   10311 C  C   . LEU   D 1 272 ? 31.325 57.436  50.179 1   41.33  ? 294 LEU   D C   1 
ATOM   10312 O  O   . LEU   D 1 272 ? 31.137 58.635  50.373 1   41.86  ? 294 LEU   D O   1 
ATOM   10313 C  CB  . LEU   D 1 272 ? 29.535 55.893  49.257 1   42.12  ? 294 LEU   D CB  1 
ATOM   10314 C  CG  . LEU   D 1 272 ? 28.201 56.569  49.565 1   43.02  ? 294 LEU   D CG  1 
ATOM   10315 C  CD1 . LEU   D 1 272 ? 27.033 55.664  49.167 1   43.41  ? 294 LEU   D CD1 1 
ATOM   10316 C  CD2 . LEU   D 1 272 ? 28.093 56.909  51.044 1   43.09  ? 294 LEU   D CD2 1 
ATOM   10317 N  N   . LEU   D 1 273 ? 32.026 56.67   51.029 1   40.31  ? 295 LEU   D N   1 
ATOM   10318 C  CA  . LEU   D 1 273 ? 32.64  57.225  52.248 1   39.59  ? 295 LEU   D CA  1 
ATOM   10319 C  C   . LEU   D 1 273 ? 33.732 58.237  51.895 1   39.15  ? 295 LEU   D C   1 
ATOM   10320 O  O   . LEU   D 1 273 ? 33.878 59.262  52.553 1   38.8   ? 295 LEU   D O   1 
ATOM   10321 C  CB  . LEU   D 1 273 ? 33.265 56.102  53.105 1   39.2   ? 295 LEU   D CB  1 
ATOM   10322 C  CG  . LEU   D 1 273 ? 32.314 55.039  53.671 1   39.47  ? 295 LEU   D CG  1 
ATOM   10323 C  CD1 . LEU   D 1 273 ? 33.067 54.043  54.53  1   38.93  ? 295 LEU   D CD1 1 
ATOM   10324 C  CD2 . LEU   D 1 273 ? 31.178 55.671  54.465 1   40.09  ? 295 LEU   D CD2 1 
ATOM   10325 N  N   . THR   D 1 274 ? 34.497 57.936  50.85  1   38.79  ? 296 THR   D N   1 
ATOM   10326 C  CA  . THR   D 1 274 ? 35.575 58.773  50.379 1   39.11  ? 296 THR   D CA  1 
ATOM   10327 C  C   . THR   D 1 274 ? 35.031 60.108  49.884 1   39.07  ? 296 THR   D C   1 
ATOM   10328 O  O   . THR   D 1 274 ? 35.606 61.154  50.194 1   38.88  ? 296 THR   D O   1 
ATOM   10329 C  CB  . THR   D 1 274 ? 36.358 57.989  49.329 1   40.27  ? 296 THR   D CB  1 
ATOM   10330 O  OG1 . THR   D 1 274 ? 37.018 56.914  50     1   40.94  ? 296 THR   D OG1 1 
ATOM   10331 C  CG2 . THR   D 1 274 ? 37.351 58.846  48.568 1   40.66  ? 296 THR   D CG2 1 
ATOM   10332 N  N   . LEU   D 1 275 ? 33.911 60.081  49.157 1   38.83  ? 297 LEU   D N   1 
ATOM   10333 C  CA  . LEU   D 1 275 ? 33.315 61.31   48.652 1   39.57  ? 297 LEU   D CA  1 
ATOM   10334 C  C   . LEU   D 1 275 ? 32.743 62.158  49.78  1   41.19  ? 297 LEU   D C   1 
ATOM   10335 O  O   . LEU   D 1 275 ? 32.84  63.386  49.718 1   42.07  ? 297 LEU   D O   1 
ATOM   10336 C  CB  . LEU   D 1 275 ? 32.258 61.037  47.571 1   39     ? 297 LEU   D CB  1 
ATOM   10337 C  CG  . LEU   D 1 275 ? 32.805 60.496  46.283 1   38.96  ? 297 LEU   D CG  1 
ATOM   10338 C  CD1 . LEU   D 1 275 ? 31.71  59.905  45.444 1   38.97  ? 297 LEU   D CD1 1 
ATOM   10339 C  CD2 . LEU   D 1 275 ? 33.593 61.542  45.549 1   39.13  ? 297 LEU   D CD2 1 
ATOM   10340 N  N   . LEU   D 1 276 ? 32.205 61.517  50.838 1   41.11  ? 298 LEU   D N   1 
ATOM   10341 C  CA  . LEU   D 1 276 ? 31.682 62.222  52.015 1   41.3   ? 298 LEU   D CA  1 
ATOM   10342 C  C   . LEU   D 1 276 ? 32.802 62.968  52.736 1   42.49  ? 298 LEU   D C   1 
ATOM   10343 O  O   . LEU   D 1 276 ? 32.601 64.085  53.207 1   42.89  ? 298 LEU   D O   1 
ATOM   10344 C  CB  . LEU   D 1 276 ? 31.023 61.227  52.97  1   40.76  ? 298 LEU   D CB  1 
ATOM   10345 C  CG  . LEU   D 1 276 ? 29.729 60.627  52.496 1   41.24  ? 298 LEU   D CG  1 
ATOM   10346 C  CD1 . LEU   D 1 276 ? 29.271 59.571  53.438 1   41.64  ? 298 LEU   D CD1 1 
ATOM   10347 C  CD2 . LEU   D 1 276 ? 28.662 61.695  52.302 1   41.81  ? 298 LEU   D CD2 1 
ATOM   10348 N  N   . MET   D 1 277 ? 33.98  62.355  52.815 1   43.19  ? 299 MET   D N   1 
ATOM   10349 C  CA  . MET   D 1 277 ? 35.153 62.975  53.417 1   44.58  ? 299 MET   D CA  1 
ATOM   10350 C  C   . MET   D 1 277 ? 35.677 64.11   52.548 1   45.79  ? 299 MET   D C   1 
ATOM   10351 O  O   . MET   D 1 277 ? 36.157 65.105  53.079 1   46.35  ? 299 MET   D O   1 
ATOM   10352 C  CB  . MET   D 1 277 ? 36.263 61.938  53.583 1   45.41  ? 299 MET   D CB  1 
ATOM   10353 C  CG  . MET   D 1 277 ? 36.118 61.117  54.822 1   47.15  ? 299 MET   D CG  1 
ATOM   10354 S  SD  . MET   D 1 277 ? 37.245 59.713  54.835 1   48.9   ? 299 MET   D SD  1 
ATOM   10355 C  CE  . MET   D 1 277 ? 38.803 60.543  54.822 1   48.7   ? 299 MET   D CE  1 
ATOM   10356 N  N   . ASP   D 1 278 ? 35.624 63.945  51.214 1   45.83  ? 300 ASP   D N   1 
ATOM   10357 C  CA  . ASP   D 1 278 ? 36.079 64.958  50.279 1   46.01  ? 300 ASP   D CA  1 
ATOM   10358 C  C   . ASP   D 1 278 ? 35.201 66.189  50.385 1   45.24  ? 300 ASP   D C   1 
ATOM   10359 O  O   . ASP   D 1 278 ? 35.73  67.29   50.399 1   44.91  ? 300 ASP   D O   1 
ATOM   10360 C  CB  . ASP   D 1 278 ? 36.129 64.405  48.837 1   48.71  ? 300 ASP   D CB  1 
ATOM   10361 C  CG  . ASP   D 1 278 ? 37.23  63.374  48.591 1   54.52  ? 300 ASP   D CG  1 
ATOM   10362 O  OD1 . ASP   D 1 278 ? 38.011 63.104  49.525 1   55.65  ? 300 ASP   D OD1 1 
ATOM   10363 O  OD2 . ASP   D 1 278 ? 37.284 62.812  47.474 1   57.29  ? 300 ASP   D OD2 1 
ATOM   10364 N  N   . ILE   D 1 279 ? 33.877 66.009  50.527 1   45.07  ? 301 ILE   D N   1 
ATOM   10365 C  CA  . ILE   D 1 279 ? 32.914 67.109  50.679 1   45.6   ? 301 ILE   D CA  1 
ATOM   10366 C  C   . ILE   D 1 279 ? 33.212 67.874  51.967 1   46.26  ? 301 ILE   D C   1 
ATOM   10367 O  O   . ILE   D 1 279 ? 33.249 69.107  51.966 1   47.09  ? 301 ILE   D O   1 
ATOM   10368 C  CB  . ILE   D 1 279 ? 31.457 66.568  50.647 1   45.97  ? 301 ILE   D CB  1 
ATOM   10369 C  CG1 . ILE   D 1 279 ? 31.033 66.189  49.22  1   46.59  ? 301 ILE   D CG1 1 
ATOM   10370 C  CG2 . ILE   D 1 279 ? 30.448 67.532  51.277 1   46.27  ? 301 ILE   D CG2 1 
ATOM   10371 C  CD1 . ILE   D 1 279 ? 29.897 65.182  49.163 1   47.64  ? 301 ILE   D CD1 1 
ATOM   10372 N  N   . ASP   D 1 280 ? 33.453 67.133  53.054 1   45.47  ? 302 ASP   D N   1 
ATOM   10373 C  CA  . ASP   D 1 280 ? 33.785 67.668  54.365 1   45.16  ? 302 ASP   D CA  1 
ATOM   10374 C  C   . ASP   D 1 280 ? 35.086 68.497  54.31  1   45.14  ? 302 ASP   D C   1 
ATOM   10375 O  O   . ASP   D 1 280 ? 35.15  69.61   54.845 1   45.51  ? 302 ASP   D O   1 
ATOM   10376 C  CB  . ASP   D 1 280 ? 33.956 66.487  55.326 1   46.81  ? 302 ASP   D CB  1 
ATOM   10377 C  CG  . ASP   D 1 280 ? 33.293 66.643  56.671 1   51.62  ? 302 ASP   D CG  1 
ATOM   10378 O  OD1 . ASP   D 1 280 ? 32.635 67.686  56.9   1   51.55  ? 302 ASP   D OD1 1 
ATOM   10379 O  OD2 . ASP   D 1 280 ? 33.437 65.733  57.502 1   54.86  ? 302 ASP   D OD2 1 
ATOM   10380 N  N   . SER   D 1 281 ? 36.116 67.951  53.651 1   44.52  ? 303 SER   D N   1 
ATOM   10381 C  CA  . SER   D 1 281 ? 37.411 68.598  53.489 1   44.31  ? 303 SER   D CA  1 
ATOM   10382 C  C   . SER   D 1 281 ? 37.302 69.86   52.639 1   43.9   ? 303 SER   D C   1 
ATOM   10383 O  O   . SER   D 1 281 ? 37.937 70.867  52.957 1   43.56  ? 303 SER   D O   1 
ATOM   10384 C  CB  . SER   D 1 281 ? 38.396 67.632  52.849 1   45.39  ? 303 SER   D CB  1 
ATOM   10385 O  OG  . SER   D 1 281 ? 39.526 67.483  53.681 1   48.23  ? 303 SER   D OG  1 
ATOM   10386 N  N   . LEU   D 1 282 ? 36.478 69.811  51.574 1   43.83  ? 304 LEU   D N   1 
ATOM   10387 C  CA  . LEU   D 1 282 ? 36.26  70.947  50.67  1   44.4   ? 304 LEU   D CA  1 
ATOM   10388 C  C   . LEU   D 1 282 ? 35.481 72.071  51.33  1   44.98  ? 304 LEU   D C   1 
ATOM   10389 O  O   . LEU   D 1 282 ? 35.724 73.247  51.027 1   45.52  ? 304 LEU   D O   1 
ATOM   10390 C  CB  . LEU   D 1 282 ? 35.597 70.522  49.355 1   44.15  ? 304 LEU   D CB  1 
ATOM   10391 C  CG  . LEU   D 1 282 ? 36.54  69.861  48.379 1   44.84  ? 304 LEU   D CG  1 
ATOM   10392 C  CD1 . LEU   D 1 282 ? 35.796 69.024  47.386 1   45.26  ? 304 LEU   D CD1 1 
ATOM   10393 C  CD2 . LEU   D 1 282 ? 37.411 70.87   47.718 1   45.41  ? 304 LEU   D CD2 1 
ATOM   10394 N  N   . ILE   D 1 283 ? 34.571 71.729  52.251 1   44.52  ? 305 ILE   D N   1 
ATOM   10395 C  CA  . ILE   D 1 283 ? 33.842 72.757  52.992 1   44.28  ? 305 ILE   D CA  1 
ATOM   10396 C  C   . ILE   D 1 283 ? 34.82  73.494  53.937 1   44.62  ? 305 ILE   D C   1 
ATOM   10397 O  O   . ILE   D 1 283 ? 34.756 74.707  54.058 1   44.49  ? 305 ILE   D O   1 
ATOM   10398 C  CB  . ILE   D 1 283 ? 32.567 72.178  53.666 1   43.78  ? 305 ILE   D CB  1 
ATOM   10399 C  CG1 . ILE   D 1 283 ? 31.523 71.84   52.593 1   43.93  ? 305 ILE   D CG1 1 
ATOM   10400 C  CG2 . ILE   D 1 283 ? 31.991 73.144  54.705 1   43.93  ? 305 ILE   D CG2 1 
ATOM   10401 C  CD1 . ILE   D 1 283 ? 30.373 71.073  53.086 1   45.18  ? 305 ILE   D CD1 1 
ATOM   10402 N  N   . THR   D 1 284 ? 35.785 72.782  54.512 1   45.4   ? 306 THR   D N   1 
ATOM   10403 C  CA  . THR   D 1 284 ? 36.814 73.385  55.363 1   46.75  ? 306 THR   D CA  1 
ATOM   10404 C  C   . THR   D 1 284 ? 37.802 74.226  54.521 1   47.43  ? 306 THR   D C   1 
ATOM   10405 O  O   . THR   D 1 284 ? 38.202 75.309  54.948 1   48.09  ? 306 THR   D O   1 
ATOM   10406 C  CB  . THR   D 1 284 ? 37.485 72.301  56.199 1   48.27  ? 306 THR   D CB  1 
ATOM   10407 O  OG1 . THR   D 1 284 ? 36.48  71.696  57.017 1   49.78  ? 306 THR   D OG1 1 
ATOM   10408 C  CG2 . THR   D 1 284 ? 38.622 72.839  57.044 1   48.25  ? 306 THR   D CG2 1 
ATOM   10409 N  N   . LYS   D 1 285 ? 38.141 73.762  53.309 1   47.04  ? 307 LYS   D N   1 
ATOM   10410 C  CA  . LYS   D 1 285 ? 38.996 74.515  52.388 1   47.04  ? 307 LYS   D CA  1 
ATOM   10411 C  C   . LYS   D 1 285 ? 38.313 75.832  51.974 1   47.07  ? 307 LYS   D C   1 
ATOM   10412 O  O   . LYS   D 1 285 ? 39.006 76.838  51.795 1   46.93  ? 307 LYS   D O   1 
ATOM   10413 C  CB  . LYS   D 1 285 ? 39.359 73.664  51.156 1   47.87  ? 307 LYS   D CB  1 
ATOM   10414 C  CG  . LYS   D 1 285 ? 40.252 72.489  51.513 1   50.98  ? 307 LYS   D CG  1 
ATOM   10415 C  CD  . LYS   D 1 285 ? 40.742 71.716  50.309 1   54.05  ? 307 LYS   D CD  1 
ATOM   10416 C  CE  . LYS   D 1 285 ? 41.684 70.613  50.731 1   57.31  ? 307 LYS   D CE  1 
ATOM   10417 N  NZ  . LYS   D 1 285 ? 41.933 69.624  49.643 1   58.55  ? 307 LYS   D NZ  1 
ATOM   10418 N  N   . TRP   D 1 286 ? 36.963 75.836  51.854 1   46.97  ? 308 TRP   D N   1 
ATOM   10419 C  CA  . TRP   D 1 286 ? 36.238 77.063  51.54  1   47.79  ? 308 TRP   D CA  1 
ATOM   10420 C  C   . TRP   D 1 286 ? 36.292 77.988  52.754 1   48.29  ? 308 TRP   D C   1 
ATOM   10421 O  O   . TRP   D 1 286 ? 36.542 79.183  52.611 1   47.96  ? 308 TRP   D O   1 
ATOM   10422 C  CB  . TRP   D 1 286 ? 34.768 76.82   51.11  1   47.85  ? 308 TRP   D CB  1 
ATOM   10423 C  CG  . TRP   D 1 286 ? 34.036 78.117  50.906 1   48.44  ? 308 TRP   D CG  1 
ATOM   10424 C  CD1 . TRP   D 1 286 ? 34.146 78.949  49.831 1   49.36  ? 308 TRP   D CD1 1 
ATOM   10425 C  CD2 . TRP   D 1 286 ? 33.298 78.849  51.903 1   48.67  ? 308 TRP   D CD2 1 
ATOM   10426 N  NE1 . TRP   D 1 286 ? 33.481 80.131  50.075 1   49.61  ? 308 TRP   D NE1 1 
ATOM   10427 C  CE2 . TRP   D 1 286 ? 32.963 80.1    51.344 1   49.14  ? 308 TRP   D CE2 1 
ATOM   10428 C  CE3 . TRP   D 1 286 ? 32.896 78.57   53.219 1   49.37  ? 308 TRP   D CE3 1 
ATOM   10429 C  CZ2 . TRP   D 1 286 ? 32.201 81.041  52.028 1   49.76  ? 308 TRP   D CZ2 1 
ATOM   10430 C  CZ3 . TRP   D 1 286 ? 32.157 79.515  53.903 1   50.23  ? 308 TRP   D CZ3 1 
ATOM   10431 C  CH2 . TRP   D 1 286 ? 31.807 80.728  53.303 1   50.29  ? 308 TRP   D CH2 1 
ATOM   10432 N  N   . ARG   D 1 287 ? 36.04  77.44   53.949 1   48.75  ? 309 ARG   D N   1 
ATOM   10433 C  CA  . ARG   D 1 287 ? 36.05  78.202  55.196 1   48.96  ? 309 ARG   D CA  1 
ATOM   10434 C  C   . ARG   D 1 287 ? 37.391 78.894  55.416 1   49.56  ? 309 ARG   D C   1 
ATOM   10435 O  O   . ARG   D 1 287 ? 37.422 80.036  55.879 1   49.93  ? 309 ARG   D O   1 
ATOM   10436 C  CB  . ARG   D 1 287 ? 35.755 77.279  56.38  1   49.01  ? 309 ARG   D CB  1 
ATOM   10437 C  CG  . ARG   D 1 287 ? 34.318 76.824  56.506 1   49.79  ? 309 ARG   D CG  1 
ATOM   10438 C  CD  . ARG   D 1 287 ? 34.133 76.136  57.851 1   50.46  ? 309 ARG   D CD  1 
ATOM   10439 N  NE  . ARG   D 1 287 ? 33.093 75.103  57.851 1   50.51  ? 309 ARG   D NE  1 
ATOM   10440 C  CZ  . ARG   D 1 287 ? 31.795 75.347  58.029 1   50.57  ? 309 ARG   D CZ  1 
ATOM   10441 N  NH1 . ARG   D 1 287 ? 30.92  74.346  58.044 1   49.11  ? 309 ARG   D NH1 1 
ATOM   10442 N  NH2 . ARG   D 1 287 ? 31.361 76.592  58.193 1   49.49  ? 309 ARG   D NH2 1 
ATOM   10443 N  N   . TYR   D 1 288 ? 38.488 78.198  55.085 1   49.64  ? 310 TYR   D N   1 
ATOM   10444 C  CA  . TYR   D 1 288 ? 39.826 78.738  55.24  1   50.79  ? 310 TYR   D CA  1 
ATOM   10445 C  C   . TYR   D 1 288 ? 40.058 79.844  54.226 1   51.54  ? 310 TYR   D C   1 
ATOM   10446 O  O   . TYR   D 1 288 ? 40.516 80.921  54.586 1   52.09  ? 310 TYR   D O   1 
ATOM   10447 C  CB  . TYR   D 1 288 ? 40.878 77.627  55.12  1   51.54  ? 310 TYR   D CB  1 
ATOM   10448 C  CG  . TYR   D 1 288 ? 42.309 78.128  55.131 1   53.28  ? 310 TYR   D CG  1 
ATOM   10449 C  CD1 . TYR   D 1 288 ? 42.946 78.456  56.321 1   54.31  ? 310 TYR   D CD1 1 
ATOM   10450 C  CD2 . TYR   D 1 288 ? 43.033 78.255  53.951 1   54.49  ? 310 TYR   D CD2 1 
ATOM   10451 C  CE1 . TYR   D 1 288 ? 44.263 78.916  56.333 1   55.47  ? 310 TYR   D CE1 1 
ATOM   10452 C  CE2 . TYR   D 1 288 ? 44.343 78.729  53.949 1   55.48  ? 310 TYR   D CE2 1 
ATOM   10453 C  CZ  . TYR   D 1 288 ? 44.961 79.047  55.141 1   56.54  ? 310 TYR   D CZ  1 
ATOM   10454 O  OH  . TYR   D 1 288 ? 46.264 79.511  55.113 1   58.12  ? 310 TYR   D OH  1 
ATOM   10455 N  N   . ASN   D 1 289 ? 39.719 79.597  52.962 1   51.43  ? 311 ASN   D N   1 
ATOM   10456 C  CA  . ASN   D 1 289 ? 39.894 80.585  51.904 1   51.28  ? 311 ASN   D CA  1 
ATOM   10457 C  C   . ASN   D 1 289 ? 39.09  81.849  52.164 1   50.7   ? 311 ASN   D C   1 
ATOM   10458 O  O   . ASN   D 1 289 ? 39.574 82.951  51.919 1   51.21  ? 311 ASN   D O   1 
ATOM   10459 C  CB  . ASN   D 1 289 ? 39.529 79.975  50.553 1   52.55  ? 311 ASN   D CB  1 
ATOM   10460 C  CG  . ASN   D 1 289 ? 40.681 79.334  49.822 1   55.28  ? 311 ASN   D CG  1 
ATOM   10461 O  OD1 . ASN   D 1 289 ? 40.681 79.235  48.591 1   57.07  ? 311 ASN   D OD1 1 
ATOM   10462 N  ND2 . ASN   D 1 289 ? 41.684 78.883  50.546 1   55.37  ? 311 ASN   D ND2 1 
ATOM   10463 N  N   . HIS   D 1 290 ? 37.877 81.685  52.674 1   49.66  ? 312 HIS   D N   1 
ATOM   10464 C  CA  . HIS   D 1 290 ? 36.984 82.772  53.024 1   49.24  ? 312 HIS   D CA  1 
ATOM   10465 C  C   . HIS   D 1 290 ? 37.571 83.601  54.184 1   49.37  ? 312 HIS   D C   1 
ATOM   10466 O  O   . HIS   D 1 290 ? 37.621 84.825  54.077 1   49.65  ? 312 HIS   D O   1 
ATOM   10467 C  CB  . HIS   D 1 290 ? 35.615 82.198  53.414 1   49.75  ? 312 HIS   D CB  1 
ATOM   10468 C  CG  . HIS   D 1 290 ? 34.642 83.216  53.909 1   52.04  ? 312 HIS   D CG  1 
ATOM   10469 N  ND1 . HIS   D 1 290 ? 34.195 83.207  55.214 1   54.13  ? 312 HIS   D ND1 1 
ATOM   10470 C  CD2 . HIS   D 1 290 ? 34.055 84.246  53.252 1   52.92  ? 312 HIS   D CD2 1 
ATOM   10471 C  CE1 . HIS   D 1 290 ? 33.349 84.221  55.31  1   54.51  ? 312 HIS   D CE1 1 
ATOM   10472 N  NE2 . HIS   D 1 290 ? 33.233 84.874  54.153 1   54.06  ? 312 HIS   D NE2 1 
ATOM   10473 N  N   . VAL   D 1 291 ? 38.071 82.941  55.259 1   48.61  ? 313 VAL   D N   1 
ATOM   10474 C  CA  . VAL   D 1 291 ? 38.637 83.634  56.41  1   48.16  ? 313 VAL   D CA  1 
ATOM   10475 C  C   . VAL   D 1 291 ? 39.912 84.423  56.04  1   47.95  ? 313 VAL   D C   1 
ATOM   10476 O  O   . VAL   D 1 291 ? 40.133 85.508  56.595 1   47.92  ? 313 VAL   D O   1 
ATOM   10477 C  CB  . VAL   D 1 291 ? 38.825 82.711  57.652 1   48.96  ? 313 VAL   D CB  1 
ATOM   10478 C  CG1 . VAL   D 1 291 ? 40.193 82.031  57.688 1   49.37  ? 313 VAL   D CG1 1 
ATOM   10479 C  CG2 . VAL   D 1 291 ? 38.601 83.499  58.93  1   49.59  ? 313 VAL   D CG2 1 
ATOM   10480 N  N   . ILE   D 1 292 ? 40.716 83.917  55.069 1   47.45  ? 314 ILE   D N   1 
ATOM   10481 C  CA  . ILE   D 1 292 ? 41.924 84.608  54.596 1   46.78  ? 314 ILE   D CA  1 
ATOM   10482 C  C   . ILE   D 1 292 ? 41.531 85.849  53.776 1   46.28  ? 314 ILE   D C   1 
ATOM   10483 O  O   . ILE   D 1 292 ? 42.172 86.901  53.882 1   46.54  ? 314 ILE   D O   1 
ATOM   10484 C  CB  . ILE   D 1 292 ? 42.833 83.633  53.8   1   46.73  ? 314 ILE   D CB  1 
ATOM   10485 C  CG1 . ILE   D 1 292 ? 43.362 82.517  54.704 1   47.26  ? 314 ILE   D CG1 1 
ATOM   10486 C  CG2 . ILE   D 1 292 ? 43.982 84.357  53.091 1   47.08  ? 314 ILE   D CG2 1 
ATOM   10487 C  CD1 . ILE   D 1 292 ? 44.218 82.977  55.85  1   48.26  ? 314 ILE   D CD1 1 
ATOM   10488 N  N   . MET   D 1 293 ? 40.457 85.731  52.986 1   45.48  ? 315 MET   D N   1 
ATOM   10489 C  CA  . MET   D 1 293 ? 39.943 86.823  52.171 1   45.65  ? 315 MET   D CA  1 
ATOM   10490 C  C   . MET   D 1 293 ? 39.38  87.93   53.07  1   46.21  ? 315 MET   D C   1 
ATOM   10491 O  O   . MET   D 1 293 ? 39.602 89.108  52.791 1   46.97  ? 315 MET   D O   1 
ATOM   10492 C  CB  . MET   D 1 293 ? 38.869 86.298  51.209 1   45.64  ? 315 MET   D CB  1 
ATOM   10493 C  CG  . MET   D 1 293 ? 38.163 87.385  50.444 1   47.81  ? 315 MET   D CG  1 
ATOM   10494 S  SD  . MET   D 1 293 ? 36.794 86.818  49.427 1   52.12  ? 315 MET   D SD  1 
ATOM   10495 C  CE  . MET   D 1 293 ? 35.831 85.897  50.617 1   46.9   ? 315 MET   D CE  1 
ATOM   10496 N  N   . VAL   D 1 294 ? 38.67  87.553  54.149 1   45.66  ? 316 VAL   D N   1 
ATOM   10497 C  CA  . VAL   D 1 294 ? 38.097 88.488  55.114 1   45.49  ? 316 VAL   D CA  1 
ATOM   10498 C  C   . VAL   D 1 294 ? 39.219 89.302  55.773 1   44.87  ? 316 VAL   D C   1 
ATOM   10499 O  O   . VAL   D 1 294 ? 39.098 90.511  55.921 1   44.56  ? 316 VAL   D O   1 
ATOM   10500 C  CB  . VAL   D 1 294 ? 37.247 87.723  56.164 1   46.56  ? 316 VAL   D CB  1 
ATOM   10501 C  CG1 . VAL   D 1 294 ? 36.853 88.622  57.331 1   47.15  ? 316 VAL   D CG1 1 
ATOM   10502 C  CG2 . VAL   D 1 294 ? 36.011 87.11   55.528 1   46.89  ? 316 VAL   D CG2 1 
ATOM   10503 N  N   . GLN   D 1 295 ? 40.328 88.644  56.117 1   44.65  ? 317 GLN   D N   1 
ATOM   10504 C  CA  . GLN   D 1 295 ? 41.475 89.3    56.739 1   44.89  ? 317 GLN   D CA  1 
ATOM   10505 C  C   . GLN   D 1 295 ? 42.24  90.205  55.77  1   46.25  ? 317 GLN   D C   1 
ATOM   10506 O  O   . GLN   D 1 295 ? 42.849 91.206  56.179 1   46.54  ? 317 GLN   D O   1 
ATOM   10507 C  CB  . GLN   D 1 295 ? 42.414 88.257  57.348 1   45.4   ? 317 GLN   D CB  1 
ATOM   10508 C  CG  . GLN   D 1 295 ? 43.273 88.847  58.46  1   47.02  ? 317 GLN   D CG  1 
ATOM   10509 C  CD  . GLN   D 1 295 ? 44.248 87.879  59.056 1   49.53  ? 317 GLN   D CD  1 
ATOM   10510 O  OE1 . GLN   D 1 295 ? 44.45  86.755  58.557 1   50.55  ? 317 GLN   D OE1 1 
ATOM   10511 N  NE2 . GLN   D 1 295 ? 44.867 88.308  60.157 1   48.84  ? 317 GLN   D NE2 1 
ATOM   10512 N  N   . ARG   D 1 296 ? 42.232 89.845  54.484 1   46.76  ? 318 ARG   D N   1 
ATOM   10513 C  CA  . ARG   D 1 296 ? 42.874 90.653  53.464 1   47.37  ? 318 ARG   D CA  1 
ATOM   10514 C  C   . ARG   D 1 296 ? 42.024 91.9    53.168 1   46.61  ? 318 ARG   D C   1 
ATOM   10515 O  O   . ARG   D 1 296 ? 42.589 92.94   52.841 1   46.85  ? 318 ARG   D O   1 
ATOM   10516 C  CB  . ARG   D 1 296 ? 43.078 89.827  52.185 1   50.42  ? 318 ARG   D CB  1 
ATOM   10517 C  CG  . ARG   D 1 296 ? 44.327 88.94   52.17  1   55.39  ? 318 ARG   D CG  1 
ATOM   10518 C  CD  . ARG   D 1 296 ? 44.434 88.218  50.828 1   59.96  ? 318 ARG   D CD  1 
ATOM   10519 N  NE  . ARG   D 1 296 ? 45.561 87.283  50.77  1   63.94  ? 318 ARG   D NE  1 
ATOM   10520 C  CZ  . ARG   D 1 296 ? 46.644 87.453  50.012 1   66.39  ? 318 ARG   D CZ  1 
ATOM   10521 N  NH1 . ARG   D 1 296 ? 46.769 88.535  49.251 1   66.2   ? 318 ARG   D NH1 1 
ATOM   10522 N  NH2 . ARG   D 1 296 ? 47.62  86.556  50.026 1   65.83  ? 318 ARG   D NH2 1 
ATOM   10523 N  N   . MET   D 1 297 ? 40.684 91.805  53.272 1   45.91  ? 319 MET   D N   1 
ATOM   10524 C  CA  . MET   D 1 297 ? 39.778 92.928  53.007 1   46.31  ? 319 MET   D CA  1 
ATOM   10525 C  C   . MET   D 1 297 ? 39.6   93.88   54.197 1   46.53  ? 319 MET   D C   1 
ATOM   10526 O  O   . MET   D 1 297 ? 39.643 95.1    54.017 1   46.73  ? 319 MET   D O   1 
ATOM   10527 C  CB  . MET   D 1 297 ? 38.377 92.43   52.612 1   47.19  ? 319 MET   D CB  1 
ATOM   10528 C  CG  . MET   D 1 297 ? 38.331 91.749  51.319 1   50.37  ? 319 MET   D CG  1 
ATOM   10529 S  SD  . MET   D 1 297 ? 38.511 92.842  49.892 1   51.75  ? 319 MET   D SD  1 
ATOM   10530 C  CE  . MET   D 1 297 ? 38.529 91.601  48.629 1   44.01  ? 319 MET   D CE  1 
ATOM   10531 N  N   . ILE   D 1 298 ? 39.284 93.34   55.387 1   46.06  ? 320 ILE   D N   1 
ATOM   10532 C  CA  . ILE   D 1 298 ? 38.969 94.173  56.544 1   46.12  ? 320 ILE   D CA  1 
ATOM   10533 C  C   . ILE   D 1 298 ? 39.787 93.865  57.801 1   46.2   ? 320 ILE   D C   1 
ATOM   10534 O  O   . ILE   D 1 298 ? 39.467 94.397  58.854 1   46.91  ? 320 ILE   D O   1 
ATOM   10535 C  CB  . ILE   D 1 298 ? 37.444 94.073  56.835 1   46.55  ? 320 ILE   D CB  1 
ATOM   10536 C  CG1 . ILE   D 1 298 ? 37.032 92.603  57.126 1   47.7   ? 320 ILE   D CG1 1 
ATOM   10537 C  CG2 . ILE   D 1 298 ? 36.604 94.705  55.709 1   46.66  ? 320 ILE   D CG2 1 
ATOM   10538 C  CD1 . ILE   D 1 298 ? 35.531 92.317  57.29  1   48.79  ? 320 ILE   D CD1 1 
ATOM   10539 N  N   . GLY   D 1 299 ? 40.805 93.01   57.703 1   45.53  ? 321 GLY   D N   1 
ATOM   10540 C  CA  . GLY   D 1 299 ? 41.63  92.624  58.847 1   45.13  ? 321 GLY   D CA  1 
ATOM   10541 C  C   . GLY   D 1 299 ? 40.868 91.832  59.893 1   44.69  ? 321 GLY   D C   1 
ATOM   10542 O  O   . GLY   D 1 299 ? 39.796 91.307  59.609 1   45.02  ? 321 GLY   D O   1 
ATOM   10543 N  N   . SER   D 1 300 ? 41.397 91.737  61.114 1   44.49  ? 322 SER   D N   1 
ATOM   10544 C  CA  . SER   D 1 300 ? 40.692 91.038  62.209 1   44.38  ? 322 SER   D CA  1 
ATOM   10545 C  C   . SER   D 1 300 ? 39.461 91.841  62.698 1   44.64  ? 322 SER   D C   1 
ATOM   10546 O  O   . SER   D 1 300 ? 38.471 91.264  63.134 1   44.15  ? 322 SER   D O   1 
ATOM   10547 C  CB  . SER   D 1 300 ? 41.643 90.729  63.355 1   45.18  ? 322 SER   D CB  1 
ATOM   10548 O  OG  . SER   D 1 300 ? 42.466 91.838  63.665 1   48.42  ? 322 SER   D OG  1 
ATOM   10549 N  N   . GLN   D 1 301 ? 39.522 93.176  62.563 1   45.22  ? 323 GLN   D N   1 
ATOM   10550 C  CA  . GLN   D 1 301 ? 38.477 94.125  62.926 1   45.86  ? 323 GLN   D CA  1 
ATOM   10551 C  C   . GLN   D 1 301 ? 38.601 95.411  62.104 1   46.27  ? 323 GLN   D C   1 
ATOM   10552 O  O   . GLN   D 1 301 ? 39.685 95.764  61.642 1   46.7   ? 323 GLN   D O   1 
ATOM   10553 C  CB  . GLN   D 1 301 ? 38.524 94.44   64.421 1   47.52  ? 323 GLN   D CB  1 
ATOM   10554 C  CG  . GLN   D 1 301 ? 39.876 94.938  64.899 1   51.17  ? 323 GLN   D CG  1 
ATOM   10555 C  CD  . GLN   D 1 301 ? 39.939 94.924  66.392 1   53.78  ? 323 GLN   D CD  1 
ATOM   10556 O  OE1 . GLN   D 1 301 ? 39.437 95.83   67.06  1   55.19  ? 323 GLN   D OE1 1 
ATOM   10557 N  NE2 . GLN   D 1 301 ? 40.55  93.886  66.937 1   53.72  ? 323 GLN   D NE2 1 
ATOM   10558 N  N   . GLN   D 1 302 ? 37.488 96.103  61.907 1   46.17  ? 324 GLN   D N   1 
ATOM   10559 C  CA  . GLN   D 1 302 ? 37.454 97.336  61.113 1   46.75  ? 324 GLN   D CA  1 
ATOM   10560 C  C   . GLN   D 1 302 ? 36.253 98.204  61.578 1   46.95  ? 324 GLN   D C   1 
ATOM   10561 O  O   . GLN   D 1 302 ? 35.471 97.767  62.416 1   47.13  ? 324 GLN   D O   1 
ATOM   10562 C  CB  . GLN   D 1 302 ? 37.401 96.97   59.599 1   47.8   ? 324 GLN   D CB  1 
ATOM   10563 C  CG  . GLN   D 1 302 ? 37.609 98.098  58.589 1   50.6   ? 324 GLN   D CG  1 
ATOM   10564 C  CD  . GLN   D 1 302 ? 38.827 98.972  58.802 1   55.96  ? 324 GLN   D CD  1 
ATOM   10565 O  OE1 . GLN   D 1 302 ? 39.979 98.531  58.726 1   58.67  ? 324 GLN   D OE1 1 
ATOM   10566 N  NE2 . GLN   D 1 302 ? 38.588 100.254 59.061 1   56.11  ? 324 GLN   D NE2 1 
ATOM   10567 N  N   . LEU   D 1 303 ? 36.139 99.435  61.078 1   47.08  ? 325 LEU   D N   1 
ATOM   10568 C  CA  . LEU   D 1 303 ? 35.067 100.346 61.438 1   48.18  ? 325 LEU   D CA  1 
ATOM   10569 C  C   . LEU   D 1 303 ? 33.71  99.767  61.086 1   49.88  ? 325 LEU   D C   1 
ATOM   10570 O  O   . LEU   D 1 303 ? 33.377 99.601  59.915 1   50.85  ? 325 LEU   D O   1 
ATOM   10571 C  CB  . LEU   D 1 303 ? 35.267 101.687 60.738 1   48.29  ? 325 LEU   D CB  1 
ATOM   10572 C  CG  . LEU   D 1 303 ? 34.59  102.862 61.436 1   49.66  ? 325 LEU   D CG  1 
ATOM   10573 C  CD1 . LEU   D 1 303 ? 35.25  103.157 62.779 1   50.18  ? 325 LEU   D CD1 1 
ATOM   10574 C  CD2 . LEU   D 1 303 ? 34.588 104.1   60.563 1   49.74  ? 325 LEU   D CD2 1 
ATOM   10575 N  N   . GLY   D 1 304 ? 32.953 99.431  62.109 1   50.4   ? 326 GLY   D N   1 
ATOM   10576 C  CA  . GLY   D 1 304 ? 31.643 98.822  61.955 1   51.73  ? 326 GLY   D CA  1 
ATOM   10577 C  C   . GLY   D 1 304 ? 31.573 97.429  62.545 1   53.28  ? 326 GLY   D C   1 
ATOM   10578 O  O   . GLY   D 1 304 ? 30.502 96.992  62.973 1   53.24  ? 326 GLY   D O   1 
ATOM   10579 N  N   . THR   D 1 305 ? 32.725 96.741  62.611 1   54.58  ? 327 THR   D N   1 
ATOM   10580 C  CA  . THR   D 1 305 ? 32.865 95.363  63.083 1   56.47  ? 327 THR   D CA  1 
ATOM   10581 C  C   . THR   D 1 305 ? 32.598 95.196  64.587 1   57.18  ? 327 THR   D C   1 
ATOM   10582 O  O   . THR   D 1 305 ? 32.066 94.15   65.004 1   57.03  ? 327 THR   D O   1 
ATOM   10583 C  CB  . THR   D 1 305 ? 34.242 94.798  62.666 1   59.26  ? 327 THR   D CB  1 
ATOM   10584 O  OG1 . THR   D 1 305 ? 34.486 95.114  61.282 1   60.66  ? 327 THR   D OG1 1 
ATOM   10585 C  CG2 . THR   D 1 305 ? 34.328 93.283  62.831 1   60.48  ? 327 THR   D CG2 1 
ATOM   10586 N  N   . GLY   D 1 306 ? 32.922 96.231  65.375 1   57.32  ? 328 GLY   D N   1 
ATOM   10587 C  CA  . GLY   D 1 306 ? 32.726 96.196  66.82  1   57.61  ? 328 GLY   D CA  1 
ATOM   10588 C  C   . GLY   D 1 306 ? 33.64  95.185  67.476 1   57.66  ? 328 GLY   D C   1 
ATOM   10589 O  O   . GLY   D 1 306 ? 33.211 94.374  68.303 1   57.65  ? 328 GLY   D O   1 
ATOM   10590 N  N   . GLY   D 1 307 ? 34.896 95.21   67.068 1   57.69  ? 329 GLY   D N   1 
ATOM   10591 C  CA  . GLY   D 1 307 ? 35.882 94.27   67.578 1   58.58  ? 329 GLY   D CA  1 
ATOM   10592 C  C   . GLY   D 1 307 ? 36.178 93.139  66.614 1   58.99  ? 329 GLY   D C   1 
ATOM   10593 O  O   . GLY   D 1 307 ? 35.687 93.132  65.488 1   59.09  ? 329 GLY   D O   1 
ATOM   10594 N  N   . SER   D 1 308 ? 36.991 92.171  67.043 1   59.03  ? 330 SER   D N   1 
ATOM   10595 C  CA  . SER   D 1 308 ? 37.358 91.037  66.197 1   59.61  ? 330 SER   D CA  1 
ATOM   10596 C  C   . SER   D 1 308 ? 36.485 89.802  66.415 1   60.01  ? 330 SER   D C   1 
ATOM   10597 O  O   . SER   D 1 308 ? 36.924 88.691  66.142 1   59.9   ? 330 SER   D O   1 
ATOM   10598 C  CB  . SER   D 1 308 ? 38.831 90.683  66.397 1   61.11  ? 330 SER   D CB  1 
ATOM   10599 O  OG  . SER   D 1 308 ? 39.12  90.319  67.736 1   63.03  ? 330 SER   D OG  1 
ATOM   10600 N  N   . SER   D 1 309 ? 35.245 89.998  66.881 1   60.47  ? 331 SER   D N   1 
ATOM   10601 C  CA  . SER   D 1 309 ? 34.304 88.918  67.187 1   60.91  ? 331 SER   D CA  1 
ATOM   10602 C  C   . SER   D 1 309 ? 33.883 88.079  65.974 1   60.3   ? 331 SER   D C   1 
ATOM   10603 O  O   . SER   D 1 309 ? 33.848 86.847  66.075 1   60.46  ? 331 SER   D O   1 
ATOM   10604 C  CB  . SER   D 1 309 ? 33.076 89.456  67.928 1   62.76  ? 331 SER   D CB  1 
ATOM   10605 O  OG  . SER   D 1 309 ? 32.644 90.738  67.494 1   65.51  ? 331 SER   D OG  1 
ATOM   10606 N  N   . GLY   D 1 310 ? 33.574 88.748  64.859 1   59.39  ? 332 GLY   D N   1 
ATOM   10607 C  CA  . GLY   D 1 310 ? 33.137 88.098  63.628 1   58.82  ? 332 GLY   D CA  1 
ATOM   10608 C  C   . GLY   D 1 310 ? 34.24  87.281  62.998 1   58.15  ? 332 GLY   D C   1 
ATOM   10609 O  O   . GLY   D 1 310 ? 34.008 86.156  62.549 1   58.27  ? 332 GLY   D O   1 
ATOM   10610 N  N   . TYR   D 1 311 ? 35.458 87.845  62.99  1   57.37  ? 333 TYR   D N   1 
ATOM   10611 C  CA  . TYR   D 1 311 ? 36.652 87.207  62.448 1   57.37  ? 333 TYR   D CA  1 
ATOM   10612 C  C   . TYR   D 1 311 ? 37.024 85.988  63.277 1   57.36  ? 333 TYR   D C   1 
ATOM   10613 O  O   . TYR   D 1 311 ? 37.312 84.927  62.721 1   57.69  ? 333 TYR   D O   1 
ATOM   10614 C  CB  . TYR   D 1 311 ? 37.8   88.228  62.397 1   57.43  ? 333 TYR   D CB  1 
ATOM   10615 C  CG  . TYR   D 1 311 ? 39.178 87.633  62.213 1   58.31  ? 333 TYR   D CG  1 
ATOM   10616 C  CD1 . TYR   D 1 311 ? 39.613 87.204  60.968 1   59.12  ? 333 TYR   D CD1 1 
ATOM   10617 C  CD2 . TYR   D 1 311 ? 40.058 87.531  63.277 1   59.35  ? 333 TYR   D CD2 1 
ATOM   10618 C  CE1 . TYR   D 1 311 ? 40.884 86.67   60.792 1   60.03  ? 333 TYR   D CE1 1 
ATOM   10619 C  CE2 . TYR   D 1 311 ? 41.335 87.008  63.112 1   60.19  ? 333 TYR   D CE2 1 
ATOM   10620 C  CZ  . TYR   D 1 311 ? 41.745 86.575  61.868 1   61.07  ? 333 TYR   D CZ  1 
ATOM   10621 O  OH  . TYR   D 1 311 ? 42.997 86.021  61.725 1   62.61  ? 333 TYR   D OH  1 
ATOM   10622 N  N   . GLN   D 1 312 ? 36.99  86.132  64.608 1   57.17  ? 334 GLN   D N   1 
ATOM   10623 C  CA  . GLN   D 1 312 ? 37.297 85.041  65.526 1   57.52  ? 334 GLN   D CA  1 
ATOM   10624 C  C   . GLN   D 1 312 ? 36.27  83.924  65.477 1   57.57  ? 334 GLN   D C   1 
ATOM   10625 O  O   . GLN   D 1 312 ? 36.623 82.767  65.721 1   57.61  ? 334 GLN   D O   1 
ATOM   10626 C  CB  . GLN   D 1 312 ? 37.481 85.539  66.958 1   59.12  ? 334 GLN   D CB  1 
ATOM   10627 C  CG  . GLN   D 1 312 ? 38.836 86.199  67.222 1   62.6   ? 334 GLN   D CG  1 
ATOM   10628 C  CD  . GLN   D 1 312 ? 40.04  85.345  66.875 1   66.63  ? 334 GLN   D CD  1 
ATOM   10629 O  OE1 . GLN   D 1 312 ? 41.03  85.845  66.332 1   68.33  ? 334 GLN   D OE1 1 
ATOM   10630 N  NE2 . GLN   D 1 312 ? 40.001 84.051  67.189 1   66.88  ? 334 GLN   D NE2 1 
ATOM   10631 N  N   . TYR   D 1 313 ? 35.005 84.253  65.142 1   57.3   ? 335 TYR   D N   1 
ATOM   10632 C  CA  . TYR   D 1 313 ? 33.97  83.241  64.984 1   57.62  ? 335 TYR   D CA  1 
ATOM   10633 C  C   . TYR   D 1 313 ? 34.336 82.391  63.753 1   57.92  ? 335 TYR   D C   1 
ATOM   10634 O  O   . TYR   D 1 313 ? 34.282 81.164  63.826 1   57.89  ? 335 TYR   D O   1 
ATOM   10635 C  CB  . TYR   D 1 313 ? 32.564 83.877  64.814 1   57.66  ? 335 TYR   D CB  1 
ATOM   10636 C  CG  . TYR   D 1 313 ? 31.568 82.932  64.162 1   58.62  ? 335 TYR   D CG  1 
ATOM   10637 C  CD1 . TYR   D 1 313 ? 31.051 81.848  64.859 1   59.45  ? 335 TYR   D CD1 1 
ATOM   10638 C  CD2 . TYR   D 1 313 ? 31.254 83.044  62.809 1   59.54  ? 335 TYR   D CD2 1 
ATOM   10639 C  CE1 . TYR   D 1 313 ? 30.204 80.931  64.247 1   60.65  ? 335 TYR   D CE1 1 
ATOM   10640 C  CE2 . TYR   D 1 313 ? 30.422 82.122  62.181 1   60.47  ? 335 TYR   D CE2 1 
ATOM   10641 C  CZ  . TYR   D 1 313 ? 29.883 81.075  62.909 1   61.66  ? 335 TYR   D CZ  1 
ATOM   10642 O  OH  . TYR   D 1 313 ? 29.02  80.179  62.319 1   63.12  ? 335 TYR   D OH  1 
ATOM   10643 N  N   . LEU   D 1 314 ? 34.704 83.052  62.629 1   57.74  ? 336 LEU   D N   1 
ATOM   10644 C  CA  . LEU   D 1 314 ? 35.052 82.355  61.394 1   57.74  ? 336 LEU   D CA  1 
ATOM   10645 C  C   . LEU   D 1 314 ? 36.261 81.435  61.612 1   58.04  ? 336 LEU   D C   1 
ATOM   10646 O  O   . LEU   D 1 314 ? 36.309 80.347  61.036 1   58.23  ? 336 LEU   D O   1 
ATOM   10647 C  CB  . LEU   D 1 314 ? 35.323 83.341  60.246 1   57.61  ? 336 LEU   D CB  1 
ATOM   10648 C  CG  . LEU   D 1 314 ? 34.181 84.256  59.797 1   58.25  ? 336 LEU   D CG  1 
ATOM   10649 C  CD1 . LEU   D 1 314 ? 34.65  85.188  58.715 1   58.53  ? 336 LEU   D CD1 1 
ATOM   10650 C  CD2 . LEU   D 1 314 ? 32.999 83.462  59.315 1   58.34  ? 336 LEU   D CD2 1 
ATOM   10651 N  N   . ARG   D 1 315 ? 37.217 81.845  62.467 1   57.78  ? 337 ARG   D N   1 
ATOM   10652 C  CA  . ARG   D 1 315 ? 38.376 81.009  62.769 1   57.92  ? 337 ARG   D CA  1 
ATOM   10653 C  C   . ARG   D 1 315 ? 38.005 79.773  63.603 1   58.05  ? 337 ARG   D C   1 
ATOM   10654 O  O   . ARG   D 1 315 ? 38.68  78.75   63.519 1   58.56  ? 337 ARG   D O   1 
ATOM   10655 C  CB  . ARG   D 1 315 ? 39.47  81.822  63.447 1   59.11  ? 337 ARG   D CB  1 
ATOM   10656 C  CG  . ARG   D 1 315 ? 40.193 82.734  62.49  1   62.92  ? 337 ARG   D CG  1 
ATOM   10657 C  CD  . ARG   D 1 315 ? 41.387 83.362  63.154 1   68.26  ? 337 ARG   D CD  1 
ATOM   10658 N  NE  . ARG   D 1 315 ? 42.516 82.438  63.276 1   73.28  ? 337 ARG   D NE  1 
ATOM   10659 C  CZ  . ARG   D 1 315 ? 43.241 82.282  64.381 1   76.77  ? 337 ARG   D CZ  1 
ATOM   10660 N  NH1 . ARG   D 1 315 ? 42.954 82.979  65.477 1   76.66  ? 337 ARG   D NH1 1 
ATOM   10661 N  NH2 . ARG   D 1 315 ? 44.252 81.423  64.403 1   77.42  ? 337 ARG   D NH2 1 
ATOM   10662 N  N   . SER   D 1 316 ? 36.932 79.858  64.394 1   57.38  ? 338 SER   D N   1 
ATOM   10663 C  CA  . SER   D 1 316 ? 36.456 78.732  65.187 1   57.11  ? 338 SER   D CA  1 
ATOM   10664 C  C   . SER   D 1 316 ? 35.683 77.703  64.33  1   57.27  ? 338 SER   D C   1 
ATOM   10665 O  O   . SER   D 1 316 ? 35.505 76.561  64.762 1   57.79  ? 338 SER   D O   1 
ATOM   10666 C  CB  . SER   D 1 316 ? 35.609 79.218  66.356 1   57.97  ? 338 SER   D CB  1 
ATOM   10667 O  OG  . SER   D 1 316 ? 34.337 79.689  65.944 1   60.12  ? 338 SER   D OG  1 
ATOM   10668 N  N   . THR   D 1 317 ? 35.212 78.097  63.129 1   56.58  ? 339 THR   D N   1 
ATOM   10669 C  CA  . THR   D 1 317 ? 34.547 77.167  62.222 1   56.51  ? 339 THR   D CA  1 
ATOM   10670 C  C   . THR   D 1 317 ? 35.552 76.225  61.517 1   57.29  ? 339 THR   D C   1 
ATOM   10671 O  O   . THR   D 1 317 ? 35.141 75.254  60.875 1   57.37  ? 339 THR   D O   1 
ATOM   10672 C  CB  . THR   D 1 317 ? 33.632 77.901  61.25  1   56.95  ? 339 THR   D CB  1 
ATOM   10673 O  OG1 . THR   D 1 317 ? 34.414 78.736  60.409 1   57.15  ? 339 THR   D OG1 1 
ATOM   10674 C  CG2 . THR   D 1 317 ? 32.578 78.725  61.964 1   57.44  ? 339 THR   D CG2 1 
ATOM   10675 N  N   . LEU   D 1 318 ? 36.866 76.499  61.647 1   57.45  ? 340 LEU   D N   1 
ATOM   10676 C  CA  . LEU   D 1 318 ? 37.919 75.666  61.082 1   58.24  ? 340 LEU   D CA  1 
ATOM   10677 C  C   . LEU   D 1 318 ? 38.225 74.426  61.959 1   59.96  ? 340 LEU   D C   1 
ATOM   10678 O  O   . LEU   D 1 318 ? 38.931 73.519  61.503 1   60.22  ? 340 LEU   D O   1 
ATOM   10679 C  CB  . LEU   D 1 318 ? 39.191 76.5    60.865 1   57.82  ? 340 LEU   D CB  1 
ATOM   10680 C  CG  . LEU   D 1 318 ? 39.025 77.766  60.028 1   58.23  ? 340 LEU   D CG  1 
ATOM   10681 C  CD1 . LEU   D 1 318 ? 40.316 78.53   59.942 1   58.44  ? 340 LEU   D CD1 1 
ATOM   10682 C  CD2 . LEU   D 1 318 ? 38.561 77.441  58.647 1   58.44  ? 340 LEU   D CD2 1 
ATOM   10683 N  N   . SER   D 1 319 ? 37.685 74.381  63.209 1   60.76  ? 341 SER   D N   1 
ATOM   10684 C  CA  . SER   D 1 319 ? 37.86  73.289  64.175 1   61.46  ? 341 SER   D CA  1 
ATOM   10685 C  C   . SER   D 1 319 ? 37.131 72.018  63.735 1   62.09  ? 341 SER   D C   1 
ATOM   10686 O  O   . SER   D 1 319 ? 36.188 72.065  62.935 1   62.34  ? 341 SER   D O   1 
ATOM   10687 C  CB  . SER   D 1 319 ? 37.364 73.71   65.561 1   62.43  ? 341 SER   D CB  1 
ATOM   10688 O  OG  . SER   D 1 319 ? 35.947 73.777  65.648 1   64.08  ? 341 SER   D OG  1 
ATOM   10689 N  N   . ASP   D 1 320 ? 37.546 70.882  64.297 1   62.12  ? 342 ASP   D N   1 
ATOM   10690 C  CA  . ASP   D 1 320 ? 36.932 69.601  63.987 1   62.34  ? 342 ASP   D CA  1 
ATOM   10691 C  C   . ASP   D 1 320 ? 35.495 69.46   64.529 1   62.24  ? 342 ASP   D C   1 
ATOM   10692 O  O   . ASP   D 1 320 ? 34.804 68.515  64.161 1   62.48  ? 342 ASP   D O   1 
ATOM   10693 C  CB  . ASP   D 1 320 ? 37.852 68.461  64.428 1   63.97  ? 342 ASP   D CB  1 
ATOM   10694 C  CG  . ASP   D 1 320 ? 39.149 68.419  63.631 1   68.12  ? 342 ASP   D CG  1 
ATOM   10695 O  OD1 . ASP   D 1 320 ? 39.173 68.962  62.497 1   68.05  ? 342 ASP   D OD1 1 
ATOM   10696 O  OD2 . ASP   D 1 320 ? 40.148 67.866  64.148 1   70.82  ? 342 ASP   D OD2 1 
ATOM   10697 N  N   . ARG   D 1 321 ? 35.015 70.437  65.316 1   61.94  ? 343 ARG   D N   1 
ATOM   10698 C  CA  . ARG   D 1 321 ? 33.622 70.502  65.768 1   62.22  ? 343 ARG   D CA  1 
ATOM   10699 C  C   . ARG   D 1 321 ? 32.679 70.756  64.565 1   60.84  ? 343 ARG   D C   1 
ATOM   10700 O  O   . ARG   D 1 321 ? 31.471 70.523  64.676 1   61.04  ? 343 ARG   D O   1 
ATOM   10701 C  CB  . ARG   D 1 321 ? 33.429 71.653  66.78  1   65.15  ? 343 ARG   D CB  1 
ATOM   10702 C  CG  . ARG   D 1 321 ? 34.437 71.659  67.909 1   71.09  ? 343 ARG   D CG  1 
ATOM   10703 C  CD  . ARG   D 1 321 ? 34.345 72.933  68.723 1   77.09  ? 343 ARG   D CD  1 
ATOM   10704 N  NE  . ARG   D 1 321 ? 33.173 72.942  69.602 1   82.11  ? 343 ARG   D NE  1 
ATOM   10705 C  CZ  . ARG   D 1 321 ? 32.184 73.831  69.529 1   84.71  ? 343 ARG   D CZ  1 
ATOM   10706 N  NH1 . ARG   D 1 321 ? 32.215 74.797  68.616 1   84.46  ? 343 ARG   D NH1 1 
ATOM   10707 N  NH2 . ARG   D 1 321 ? 31.159 73.765  70.372 1   84.4   ? 343 ARG   D NH2 1 
ATOM   10708 N  N   . TYR   D 1 322 ? 33.221 71.271  63.438 1   59.15  ? 344 TYR   D N   1 
ATOM   10709 C  CA  . TYR   D 1 322 ? 32.458 71.559  62.235 1   57.96  ? 344 TYR   D CA  1 
ATOM   10710 C  C   . TYR   D 1 322 ? 32.565 70.45   61.164 1   55.5   ? 344 TYR   D C   1 
ATOM   10711 O  O   . TYR   D 1 322 ? 31.766 70.44   60.227 1   55.4   ? 344 TYR   D O   1 
ATOM   10712 C  CB  . TYR   D 1 322 ? 32.83  72.943  61.688 1   58.53  ? 344 TYR   D CB  1 
ATOM   10713 C  CG  . TYR   D 1 322 ? 32.108 74.062  62.409 1   59.87  ? 344 TYR   D CG  1 
ATOM   10714 C  CD1 . TYR   D 1 322 ? 32.542 74.512  63.651 1   61.26  ? 344 TYR   D CD1 1 
ATOM   10715 C  CD2 . TYR   D 1 322 ? 30.953 74.621  61.884 1   60.88  ? 344 TYR   D CD2 1 
ATOM   10716 C  CE1 . TYR   D 1 322 ? 31.868 75.522  64.33  1   62.41  ? 344 TYR   D CE1 1 
ATOM   10717 C  CE2 . TYR   D 1 322 ? 30.269 75.63   62.552 1   62.11  ? 344 TYR   D CE2 1 
ATOM   10718 C  CZ  . TYR   D 1 322 ? 30.727 76.077  63.777 1   63.28  ? 344 TYR   D CZ  1 
ATOM   10719 O  OH  . TYR   D 1 322 ? 30.055 77.084  64.425 1   64.83  ? 344 TYR   D OH  1 
ATOM   10720 N  N   . LYS   D 1 323 ? 33.513 69.508  61.322 1   53.4   ? 345 LYS   D N   1 
ATOM   10721 C  CA  . LYS   D 1 323 ? 33.665 68.378  60.423 1   52.22  ? 345 LYS   D CA  1 
ATOM   10722 C  C   . LYS   D 1 323 ? 32.584 67.358  60.766 1   51.3   ? 345 LYS   D C   1 
ATOM   10723 O  O   . LYS   D 1 323 ? 32.537 66.891  61.894 1   52.1   ? 345 LYS   D O   1 
ATOM   10724 C  CB  . LYS   D 1 323 ? 35.057 67.762  60.575 1   53.42  ? 345 LYS   D CB  1 
ATOM   10725 C  CG  . LYS   D 1 323 ? 36.113 68.438  59.713 1   55.95  ? 345 LYS   D CG  1 
ATOM   10726 C  CD  . LYS   D 1 323 ? 36.656 67.486  58.654 1   58.52  ? 345 LYS   D CD  1 
ATOM   10727 C  CE  . LYS   D 1 323 ? 37.326 68.212  57.503 1   60.61  ? 345 LYS   D CE  1 
ATOM   10728 N  NZ  . LYS   D 1 323 ? 38.714 68.639  57.826 1   61.35  ? 345 LYS   D NZ  1 
ATOM   10729 N  N   . VAL   D 1 324 ? 31.683 67.064  59.827 1   49.78  ? 346 VAL   D N   1 
ATOM   10730 C  CA  . VAL   D 1 324 ? 30.562 66.157  60.009 1   49.29  ? 346 VAL   D CA  1 
ATOM   10731 C  C   . VAL   D 1 324 ? 30.973 64.686  60.101 1   49.06  ? 346 VAL   D C   1 
ATOM   10732 O  O   . VAL   D 1 324 ? 30.541 63.996  61.009 1   49.36  ? 346 VAL   D O   1 
ATOM   10733 C  CB  . VAL   D 1 324 ? 29.513 66.371  58.893 1   50.15  ? 346 VAL   D CB  1 
ATOM   10734 C  CG1 . VAL   D 1 324 ? 28.333 65.43   59.059 1   51.1   ? 346 VAL   D CG1 1 
ATOM   10735 C  CG2 . VAL   D 1 324 ? 29.042 67.809  58.85  1   50.55  ? 346 VAL   D CG2 1 
ATOM   10736 N  N   . PHE   D 1 325 ? 31.767 64.186  59.143 1   48.53  ? 347 PHE   D N   1 
ATOM   10737 C  CA  . PHE   D 1 325 ? 32.174 62.784  59.091 1   47.99  ? 347 PHE   D CA  1 
ATOM   10738 C  C   . PHE   D 1 325 ? 33.573 62.593  59.643 1   48.14  ? 347 PHE   D C   1 
ATOM   10739 O  O   . PHE   D 1 325 ? 34.41  61.911  59.055 1   48.12  ? 347 PHE   D O   1 
ATOM   10740 C  CB  . PHE   D 1 325 ? 32.052 62.25   57.666 1   47.44  ? 347 PHE   D CB  1 
ATOM   10741 C  CG  . PHE   D 1 325 ? 30.63  62.272  57.162 1   47.49  ? 347 PHE   D CG  1 
ATOM   10742 C  CD1 . PHE   D 1 325 ? 29.773 61.215  57.414 1   48.01  ? 347 PHE   D CD1 1 
ATOM   10743 C  CD2 . PHE   D 1 325 ? 30.147 63.357  56.448 1   48.04  ? 347 PHE   D CD2 1 
ATOM   10744 C  CE1 . PHE   D 1 325 ? 28.463 61.245  56.971 1   48.58  ? 347 PHE   D CE1 1 
ATOM   10745 C  CE2 . PHE   D 1 325 ? 28.839 63.383  55.997 1   48.69  ? 347 PHE   D CE2 1 
ATOM   10746 C  CZ  . PHE   D 1 325 ? 28.007 62.325  56.258 1   48.57  ? 347 PHE   D CZ  1 
ATOM   10747 N  N   . LEU   D 1 326 ? 33.791 63.194  60.805 1   47.99  ? 348 LEU   D N   1 
ATOM   10748 C  CA  . LEU   D 1 326 ? 35.008 63.2    61.595 1   48.19  ? 348 LEU   D CA  1 
ATOM   10749 C  C   . LEU   D 1 326 ? 35.579 61.791  61.848 1   48.44  ? 348 LEU   D C   1 
ATOM   10750 O  O   . LEU   D 1 326 ? 36.802 61.616  61.879 1   48.93  ? 348 LEU   D O   1 
ATOM   10751 C  CB  . LEU   D 1 326 ? 34.655 63.871  62.936 1   48.1   ? 348 LEU   D CB  1 
ATOM   10752 C  CG  . LEU   D 1 326 ? 35.824 64.335  63.776 1   49.36  ? 348 LEU   D CG  1 
ATOM   10753 C  CD1 . LEU   D 1 326 ? 36.618 65.403  63.067 1   50.06  ? 348 LEU   D CD1 1 
ATOM   10754 C  CD2 . LEU   D 1 326 ? 35.364 64.824  65.102 1   49.67  ? 348 LEU   D CD2 1 
ATOM   10755 N  N   . ASP   D 1 327 ? 34.686 60.801  62.065 1   47.54  ? 349 ASP   D N   1 
ATOM   10756 C  CA  . ASP   D 1 327 ? 35.039 59.402  62.338 1   46.29  ? 349 ASP   D CA  1 
ATOM   10757 C  C   . ASP   D 1 327 ? 35.733 58.728  61.179 1   44.99  ? 349 ASP   D C   1 
ATOM   10758 O  O   . ASP   D 1 327 ? 36.595 57.872  61.39  1   45.25  ? 349 ASP   D O   1 
ATOM   10759 C  CB  . ASP   D 1 327 ? 33.773 58.597  62.64  1   47.2   ? 349 ASP   D CB  1 
ATOM   10760 C  CG  . ASP   D 1 327 ? 33.04  59.116  63.833 1   49.51  ? 349 ASP   D CG  1 
ATOM   10761 O  OD1 . ASP   D 1 327 ? 32.552 60.266  63.769 1   49.97  ? 349 ASP   D OD1 1 
ATOM   10762 O  OD2 . ASP   D 1 327 ? 32.944 58.371  64.841 1   49.78  ? 349 ASP   D OD2 1 
ATOM   10763 N  N   . LEU   D 1 328 ? 35.304 59.062  59.955 1   43.22  ? 350 LEU   D N   1 
ATOM   10764 C  CA  . LEU   D 1 328 ? 35.819 58.473  58.731 1   41.63  ? 350 LEU   D CA  1 
ATOM   10765 C  C   . LEU   D 1 328 ? 37.28  58.795  58.499 1   40.46  ? 350 LEU   D C   1 
ATOM   10766 O  O   . LEU   D 1 328 ? 38.005 57.978  57.934 1   40.38  ? 350 LEU   D O   1 
ATOM   10767 C  CB  . LEU   D 1 328 ? 34.98  58.941  57.529 1   41.22  ? 350 LEU   D CB  1 
ATOM   10768 C  CG  . LEU   D 1 328 ? 33.521 58.525  57.473 1   41.37  ? 350 LEU   D CG  1 
ATOM   10769 C  CD1 . LEU   D 1 328 ? 32.916 58.982  56.188 1   41.32  ? 350 LEU   D CD1 1 
ATOM   10770 C  CD2 . LEU   D 1 328 ? 33.369 57.01   57.603 1   41.78  ? 350 LEU   D CD2 1 
ATOM   10771 N  N   . PHE   D 1 329 ? 37.718 59.981  58.924 1   39.65  ? 351 PHE   D N   1 
ATOM   10772 C  CA  . PHE   D 1 329 ? 39.1   60.417  58.744 1   39.57  ? 351 PHE   D CA  1 
ATOM   10773 C  C   . PHE   D 1 329 ? 40.104 59.573  59.542 1   41.18  ? 351 PHE   D C   1 
ATOM   10774 O  O   . PHE   D 1 329 ? 41.247 59.384  59.122 1   42.12  ? 351 PHE   D O   1 
ATOM   10775 C  CB  . PHE   D 1 329 ? 39.233 61.913  59.104 1   38.2   ? 351 PHE   D CB  1 
ATOM   10776 C  CG  . PHE   D 1 329 ? 38.601 62.818  58.073 1   37.81  ? 351 PHE   D CG  1 
ATOM   10777 C  CD1 . PHE   D 1 329 ? 39.323 63.252  56.968 1   38.62  ? 351 PHE   D CD1 1 
ATOM   10778 C  CD2 . PHE   D 1 329 ? 37.274 63.198  58.18  1   37.28  ? 351 PHE   D CD2 1 
ATOM   10779 C  CE1 . PHE   D 1 329 ? 38.73  64.069  56.007 1   38.45  ? 351 PHE   D CE1 1 
ATOM   10780 C  CE2 . PHE   D 1 329 ? 36.689 64.016  57.226 1   37.44  ? 351 PHE   D CE2 1 
ATOM   10781 C  CZ  . PHE   D 1 329 ? 37.421 64.454  56.153 1   37.62  ? 351 PHE   D CZ  1 
ATOM   10782 N  N   . ASN   D 1 330 ? 39.665 59.035  60.67  1   41.24  ? 352 ASN   D N   1 
ATOM   10783 C  CA  . ASN   D 1 330 ? 40.524 58.293  61.561 1   41.67  ? 352 ASN   D CA  1 
ATOM   10784 C  C   . ASN   D 1 330 ? 40.525 56.768  61.346 1   41.23  ? 352 ASN   D C   1 
ATOM   10785 O  O   . ASN   D 1 330 ? 41.345 56.079  61.945 1   41.71  ? 352 ASN   D O   1 
ATOM   10786 C  CB  . ASN   D 1 330 ? 40.141 58.653  62.999 1   43.34  ? 352 ASN   D CB  1 
ATOM   10787 C  CG  . ASN   D 1 330 ? 41.237 58.449  63.994 1   47.52  ? 352 ASN   D CG  1 
ATOM   10788 O  OD1 . ASN   D 1 330 ? 42.408 58.732  63.727 1   49.27  ? 352 ASN   D OD1 1 
ATOM   10789 N  ND2 . ASN   D 1 330 ? 40.876 57.931  65.163 1   48.57  ? 352 ASN   D ND2 1 
ATOM   10790 N  N   . LEU   D 1 331 ? 39.66  56.237  60.484 1   40.31  ? 353 LEU   D N   1 
ATOM   10791 C  CA  . LEU   D 1 331 ? 39.548 54.783  60.271 1   39.74  ? 353 LEU   D CA  1 
ATOM   10792 C  C   . LEU   D 1 331 ? 40.853 54.03   59.982 1   40.07  ? 353 LEU   D C   1 
ATOM   10793 O  O   . LEU   D 1 331 ? 40.919 52.823  60.231 1   40.16  ? 353 LEU   D O   1 
ATOM   10794 C  CB  . LEU   D 1 331 ? 38.533 54.464  59.173 1   38.89  ? 353 LEU   D CB  1 
ATOM   10795 C  CG  . LEU   D 1 331 ? 37.12  54.891  59.462 1   39.28  ? 353 LEU   D CG  1 
ATOM   10796 C  CD1 . LEU   D 1 331 ? 36.232 54.639  58.266 1   39.92  ? 353 LEU   D CD1 1 
ATOM   10797 C  CD2 . LEU   D 1 331 ? 36.582 54.206  60.683 1   39.16  ? 353 LEU   D CD2 1 
ATOM   10798 N  N   . SER   D 1 332 ? 41.881 54.715  59.45  1   39.98  ? 354 SER   D N   1 
ATOM   10799 C  CA  . SER   D 1 332 ? 43.151 54.041  59.161 1   39.62  ? 354 SER   D CA  1 
ATOM   10800 C  C   . SER   D 1 332 ? 43.971 53.705  60.417 1   39.87  ? 354 SER   D C   1 
ATOM   10801 O  O   . SER   D 1 332 ? 44.923 52.935  60.33  1   40.14  ? 354 SER   D O   1 
ATOM   10802 C  CB  . SER   D 1 332 ? 43.965 54.832  58.155 1   39.86  ? 354 SER   D CB  1 
ATOM   10803 O  OG  . SER   D 1 332 ? 43.3   54.807  56.903 1   41.36  ? 354 SER   D OG  1 
ATOM   10804 N  N   . THR   D 1 333 ? 43.595 54.274  61.584 1   39.34  ? 355 THR   D N   1 
ATOM   10805 C  CA  . THR   D 1 333 ? 44.248 54.026  62.862 1   39.17  ? 355 THR   D CA  1 
ATOM   10806 C  C   . THR   D 1 333 ? 44.033 52.582  63.312 1   39.5   ? 355 THR   D C   1 
ATOM   10807 O  O   . THR   D 1 333 ? 44.853 52.053  64.06  1   40     ? 355 THR   D O   1 
ATOM   10808 C  CB  . THR   D 1 333 ? 43.664 54.992  63.917 1   40.26  ? 355 THR   D CB  1 
ATOM   10809 O  OG1 . THR   D 1 333 ? 43.67  56.327  63.404 1   41.56  ? 355 THR   D OG1 1 
ATOM   10810 C  CG2 . THR   D 1 333 ? 44.38  54.926  65.259 1   39.72  ? 355 THR   D CG2 1 
ATOM   10811 N  N   . PHE   D 1 334 ? 42.914 51.955  62.889 1   39.26  ? 356 PHE   D N   1 
ATOM   10812 C  CA  . PHE   D 1 334 ? 42.503 50.598  63.267 1   39.65  ? 356 PHE   D CA  1 
ATOM   10813 C  C   . PHE   D 1 334 ? 42.931 49.505  62.293 1   40.64  ? 356 PHE   D C   1 
ATOM   10814 O  O   . PHE   D 1 334 ? 42.646 48.339  62.53  1   41.57  ? 356 PHE   D O   1 
ATOM   10815 C  CB  . PHE   D 1 334 ? 40.981 50.539  63.411 1   39.37  ? 356 PHE   D CB  1 
ATOM   10816 C  CG  . PHE   D 1 334 ? 40.391 51.726  64.133 1   39.92  ? 356 PHE   D CG  1 
ATOM   10817 C  CD1 . PHE   D 1 334 ? 40.71  51.98   65.452 1   40.62  ? 356 PHE   D CD1 1 
ATOM   10818 C  CD2 . PHE   D 1 334 ? 39.583 52.625  63.47  1   40.37  ? 356 PHE   D CD2 1 
ATOM   10819 C  CE1 . PHE   D 1 334 ? 40.212 53.094  66.096 1   41.1   ? 356 PHE   D CE1 1 
ATOM   10820 C  CE2 . PHE   D 1 334 ? 39.067 53.725  64.127 1   40.93  ? 356 PHE   D CE2 1 
ATOM   10821 C  CZ  . PHE   D 1 334 ? 39.375 53.945  65.437 1   40.69  ? 356 PHE   D CZ  1 
ATOM   10822 N  N   . LEU   D 1 335 ? 43.585 49.872  61.2   1   40.4   ? 357 LEU   D N   1 
ATOM   10823 C  CA  . LEU   D 1 335 ? 44.018 48.961  60.166 1   40.19  ? 357 LEU   D CA  1 
ATOM   10824 C  C   . LEU   D 1 335 ? 45.08  47.942  60.623 1   40.03  ? 357 LEU   D C   1 
ATOM   10825 O  O   . LEU   D 1 335 ? 46.018 48.271  61.368 1   39.8   ? 357 LEU   D O   1 
ATOM   10826 C  CB  . LEU   D 1 335 ? 44.571 49.785  58.998 1   40.05  ? 357 LEU   D CB  1 
ATOM   10827 C  CG  . LEU   D 1 335 ? 44.223 49.279  57.63  1   41.4   ? 357 LEU   D CG  1 
ATOM   10828 C  CD1 . LEU   D 1 335 ? 42.823 49.706  57.263 1   41.69  ? 357 LEU   D CD1 1 
ATOM   10829 C  CD2 . LEU   D 1 335 ? 45.235 49.765  56.606 1   42.2   ? 357 LEU   D CD2 1 
ATOM   10830 N  N   . ILE   D 1 336 ? 44.93  46.709  60.126 1   39.72  ? 358 ILE   D N   1 
ATOM   10831 C  CA  . ILE   D 1 336 ? 45.876 45.615  60.32  1   40.02  ? 358 ILE   D CA  1 
ATOM   10832 C  C   . ILE   D 1 336 ? 46.386 45.223  58.943 1   41.48  ? 358 ILE   D C   1 
ATOM   10833 O  O   . ILE   D 1 336 ? 45.706 45.476  57.949 1   41.79  ? 358 ILE   D O   1 
ATOM   10834 C  CB  . ILE   D 1 336 ? 45.286 44.418  61.116 1   39.73  ? 358 ILE   D CB  1 
ATOM   10835 C  CG1 . ILE   D 1 336 ? 43.843 44.085  60.692 1   40.29  ? 358 ILE   D CG1 1 
ATOM   10836 C  CG2 . ILE   D 1 336 ? 45.407 44.65   62.609 1   39.77  ? 358 ILE   D CG2 1 
ATOM   10837 C  CD1 . ILE   D 1 336 ? 43.275 42.831  61.345 1   41.07  ? 358 ILE   D CD1 1 
ATOM   10838 N  N   . PRO   D 1 337 ? 47.576 44.606  58.832 1   42.42  ? 359 PRO   D N   1 
ATOM   10839 C  CA  . PRO   D 1 337 ? 48.084 44.244  57.493 1   43.24  ? 359 PRO   D CA  1 
ATOM   10840 C  C   . PRO   D 1 337 ? 47.185 43.29   56.707 1   45.02  ? 359 PRO   D C   1 
ATOM   10841 O  O   . PRO   D 1 337 ? 46.336 42.63   57.307 1   45.15  ? 359 PRO   D O   1 
ATOM   10842 C  CB  . PRO   D 1 337 ? 49.448 43.625  57.791 1   43.39  ? 359 PRO   D CB  1 
ATOM   10843 C  CG  . PRO   D 1 337 ? 49.808 44.078  59.174 1   43.43  ? 359 PRO   D CG  1 
ATOM   10844 C  CD  . PRO   D 1 337 ? 48.522 44.223  59.9   1   41.69  ? 359 PRO   D CD  1 
ATOM   10845 N  N   . ARG   D 1 338 ? 47.379 43.184  55.365 1   46.22  ? 360 ARG   D N   1 
ATOM   10846 C  CA  . ARG   D 1 338 ? 46.582 42.275  54.513 1   47.53  ? 360 ARG   D CA  1 
ATOM   10847 C  C   . ARG   D 1 338 ? 46.52  40.842  55.082 1   49.17  ? 360 ARG   D C   1 
ATOM   10848 O  O   . ARG   D 1 338 ? 45.443 40.256  55.182 1   49.41  ? 360 ARG   D O   1 
ATOM   10849 C  CB  . ARG   D 1 338 ? 47.141 42.213  53.077 1   48.09  ? 360 ARG   D CB  1 
ATOM   10850 C  CG  . ARG   D 1 338 ? 47.116 43.524  52.327 1   50.14  ? 360 ARG   D CG  1 
ATOM   10851 C  CD  . ARG   D 1 338 ? 47.309 43.312  50.826 1   51.08  ? 360 ARG   D CD  1 
ATOM   10852 N  NE  . ARG   D 1 338 ? 47.287 44.579  50.087 1   52.52  ? 360 ARG   D NE  1 
ATOM   10853 C  CZ  . ARG   D 1 338 ? 46.178 45.181  49.667 1   54.63  ? 360 ARG   D CZ  1 
ATOM   10854 N  NH1 . ARG   D 1 338 ? 44.989 44.633  49.893 1   54.68  ? 360 ARG   D NH1 1 
ATOM   10855 N  NH2 . ARG   D 1 338 ? 46.247 46.331  49.011 1   54.56  ? 360 ARG   D NH2 1 
ATOM   10856 N  N   . GLU   D 1 339 ? 47.687 40.314  55.489 1   50.07  ? 361 GLU   D N   1 
ATOM   10857 C  CA  . GLU   D 1 339 ? 47.854 38.976  56.054 1   51.37  ? 361 GLU   D CA  1 
ATOM   10858 C  C   . GLU   D 1 339 ? 47.248 38.801  57.45  1   51.73  ? 361 GLU   D C   1 
ATOM   10859 O  O   . GLU   D 1 339 ? 47.172 37.678  57.937 1   52.33  ? 361 GLU   D O   1 
ATOM   10860 C  CB  . GLU   D 1 339 ? 49.336 38.576  56.048 1   54.58  ? 361 GLU   D CB  1 
ATOM   10861 C  CG  . GLU   D 1 339 ? 50.21  39.388  56.992 1   60.14  ? 361 GLU   D CG  1 
ATOM   10862 C  CD  . GLU   D 1 339 ? 50.837 40.645  56.411 1   66.79  ? 361 GLU   D CD  1 
ATOM   10863 O  OE1 . GLU   D 1 339 ? 50.402 41.102  55.327 1   66.75  ? 361 GLU   D OE1 1 
ATOM   10864 O  OE2 . GLU   D 1 339 ? 51.764 41.184  57.06  1   69.68  ? 361 GLU   D OE2 1 
ATOM   10865 N  N   . ALA   D 1 340 ? 46.84  39.887  58.1   1   51.14  ? 362 ALA   D N   1 
ATOM   10866 C  CA  . ALA   D 1 340 ? 46.187 39.809  59.4   1   50.95  ? 362 ALA   D CA  1 
ATOM   10867 C  C   . ALA   D 1 340 ? 44.662 39.897  59.267 1   51.22  ? 362 ALA   D C   1 
ATOM   10868 O  O   . ALA   D 1 340 ? 43.963 39.438  60.149 1   51.23  ? 362 ALA   D O   1 
ATOM   10869 C  CB  . ALA   D 1 340 ? 46.691 40.911  60.308 1   50.51  ? 362 ALA   D CB  1 
ATOM   10870 N  N   . ILE   D 1 341 ? 44.144 40.5    58.189 1   51.44  ? 363 ILE   D N   1 
ATOM   10871 C  CA  . ILE   D 1 341 ? 42.705 40.669  57.978 1   52.04  ? 363 ILE   D CA  1 
ATOM   10872 C  C   . ILE   D 1 341 ? 41.986 39.344  57.689 1   53.18  ? 363 ILE   D C   1 
ATOM   10873 O  O   . ILE   D 1 341 ? 42.45  38.575  56.845 1   53.01  ? 363 ILE   D O   1 
ATOM   10874 C  CB  . ILE   D 1 341 ? 42.467 41.722  56.865 1   52.12  ? 363 ILE   D CB  1 
ATOM   10875 C  CG1 . ILE   D 1 341 ? 43.025 43.084  57.285 1   52.84  ? 363 ILE   D CG1 1 
ATOM   10876 C  CG2 . ILE   D 1 341 ? 40.991 41.82   56.465 1   52.6   ? 363 ILE   D CG2 1 
ATOM   10877 C  CD1 . ILE   D 1 341 ? 42.985 44.131  56.215 1   54.18  ? 363 ILE   D CD1 1 
ATOM   10878 N  N   . PRO   D 1 342 ? 40.844 39.07   58.38  1   54.16  ? 364 PRO   D N   1 
ATOM   10879 C  CA  . PRO   D 1 342 ? 40.107 37.811  58.12  1   54.69  ? 364 PRO   D CA  1 
ATOM   10880 C  C   . PRO   D 1 342 ? 39.55  37.736  56.701 1   55.57  ? 364 PRO   D C   1 
ATOM   10881 O  O   . PRO   D 1 342 ? 38.898 38.673  56.255 1   55.71  ? 364 PRO   D O   1 
ATOM   10882 C  CB  . PRO   D 1 342 ? 38.981 37.821  59.162 1   55.21  ? 364 PRO   D CB  1 
ATOM   10883 C  CG  . PRO   D 1 342 ? 38.854 39.239  59.604 1   55.45  ? 364 PRO   D CG  1 
ATOM   10884 C  CD  . PRO   D 1 342 ? 40.19  39.887  59.43  1   53.7   ? 364 PRO   D CD  1 
ATOM   10885 N  N   . PRO   D 1 343 ? 39.815 36.64   55.965 1   55.96  ? 365 PRO   D N   1 
ATOM   10886 C  CA  . PRO   D 1 343 ? 39.364 36.565  54.572 1   56.59  ? 365 PRO   D CA  1 
ATOM   10887 C  C   . PRO   D 1 343 ? 37.857 36.423  54.407 1   58.65  ? 365 PRO   D C   1 
ATOM   10888 O  O   . PRO   D 1 343 ? 37.189 35.846  55.263 1   58.75  ? 365 PRO   D O   1 
ATOM   10889 C  CB  . PRO   D 1 343 ? 40.113 35.347  54.015 1   56.65  ? 365 PRO   D CB  1 
ATOM   10890 C  CG  . PRO   D 1 343 ? 41.165 35.033  55.005 1   56.81  ? 365 PRO   D CG  1 
ATOM   10891 C  CD  . PRO   D 1 343 ? 40.613 35.458  56.324 1   55.37  ? 365 PRO   D CD  1 
ATOM   10892 N  N   . LEU   D 1 344 ? 37.331 36.956  53.291 1   60.08  ? 366 LEU   D N   1 
ATOM   10893 C  CA  . LEU   D 1 344 ? 35.915 36.92   52.961 1   61.85  ? 366 LEU   D CA  1 
ATOM   10894 C  C   . LEU   D 1 344 ? 35.484 35.511  52.544 1   64.99  ? 366 LEU   D C   1 
ATOM   10895 O  O   . LEU   D 1 344 ? 36.109 34.912  51.67  1   65.4   ? 366 LEU   D O   1 
ATOM   10896 C  CB  . LEU   D 1 344 ? 35.62  37.932  51.842 1   61.28  ? 366 LEU   D CB  1 
ATOM   10897 C  CG  . LEU   D 1 344 ? 35.457 39.384  52.277 1   61.31  ? 366 LEU   D CG  1 
ATOM   10898 C  CD1 . LEU   D 1 344 ? 35.265 40.289  51.088 1   61.33  ? 366 LEU   D CD1 1 
ATOM   10899 C  CD2 . LEU   D 1 344 ? 34.287 39.539  53.202 1   61.5   ? 366 LEU   D CD2 1 
ATOM   10900 N  N   . ASP   D 1 345 ? 34.423 34.976  53.178 1   67.04  ? 367 ASP   D N   1 
ATOM   10901 C  CA  . ASP   D 1 345 ? 33.92  33.627  52.894 1   69.35  ? 367 ASP   D CA  1 
ATOM   10902 C  C   . ASP   D 1 345 ? 32.553 33.649  52.186 1   70.84  ? 367 ASP   D C   1 
ATOM   10903 O  O   . ASP   D 1 345 ? 32.48  33.296  51.011 1   71.19  ? 367 ASP   D O   1 
ATOM   10904 C  CB  . ASP   D 1 345 ? 33.873 32.77   54.182 1   72.14  ? 367 ASP   D CB  1 
ATOM   10905 C  CG  . ASP   D 1 345 ? 35.235 32.393  54.725 1   78.94  ? 367 ASP   D CG  1 
ATOM   10906 O  OD1 . ASP   D 1 345 ? 36.196 32.31   53.916 1   80.4   ? 367 ASP   D OD1 1 
ATOM   10907 O  OD2 . ASP   D 1 345 ? 35.344 32.171  55.959 1   81.28  ? 367 ASP   D OD2 1 
ATOM   10908 N  N   . GLU   D 1 346 ? 31.479 34.073  52.901 1   71.57  ? 368 GLU   D N   1 
ATOM   10909 C  CA  . GLU   D 1 346 ? 30.103 34.16   52.403 1   72.43  ? 368 GLU   D CA  1 
ATOM   10910 C  C   . GLU   D 1 346 ? 29.605 32.852  51.788 1   72.31  ? 368 GLU   D C   1 
ATOM   10911 O  O   . GLU   D 1 346 ? 28.654 32.268  52.303 1   72.14  ? 368 GLU   D O   1 
ATOM   10912 C  CB  . GLU   D 1 346 ? 29.912 35.354  51.436 1   75.2   ? 368 GLU   D CB  1 
ATOM   10913 C  CG  . GLU   D 1 346 ? 30.583 36.655  51.874 1   80.48  ? 368 GLU   D CG  1 
ATOM   10914 C  CD  . GLU   D 1 346 ? 29.988 37.395  53.064 1   87.36  ? 368 GLU   D CD  1 
ATOM   10915 O  OE1 . GLU   D 1 346 ? 30.541 38.459  53.43  1   88.62  ? 368 GLU   D OE1 1 
ATOM   10916 O  OE2 . GLU   D 1 346 ? 28.974 36.92   53.628 1   89.16  ? 368 GLU   D OE2 1 
HETATM 10917 C  CHA . HEM   E 2 .   ? 26.634 75.907  20.638 1   48.92  ? 401 HEM   A CHA 1 
HETATM 10918 C  CHB . HEM   E 2 .   ? 25.642 71.415  22.226 1   48.81  ? 401 HEM   A CHB 1 
HETATM 10919 C  CHC . HEM   E 2 .   ? 26.38  72.816  26.824 1   47.88  ? 401 HEM   A CHC 1 
HETATM 10920 C  CHD . HEM   E 2 .   ? 27.163 77.336  25.238 1   48.47  ? 401 HEM   A CHD 1 
HETATM 10921 C  C1A . HEM   E 2 .   ? 26.252 74.533  20.659 1   49.09  ? 401 HEM   A C1A 1 
HETATM 10922 C  C2A . HEM   E 2 .   ? 25.992 73.724  19.479 1   49.43  ? 401 HEM   A C2A 1 
HETATM 10923 C  C3A . HEM   E 2 .   ? 25.732 72.445  19.927 1   48.86  ? 401 HEM   A C3A 1 
HETATM 10924 C  C4A . HEM   E 2 .   ? 25.82  72.494  21.372 1   48.85  ? 401 HEM   A C4A 1 
HETATM 10925 C  CMA . HEM   E 2 .   ? 25.453 71.217  19.115 1   48.61  ? 401 HEM   A CMA 1 
HETATM 10926 C  CAA . HEM   E 2 .   ? 26.008 74.156  18.037 1   50.23  ? 401 HEM   A CAA 1 
HETATM 10927 C  CBA . HEM   E 2 .   ? 24.841 75.06   17.65  1   50.88  ? 401 HEM   A CBA 1 
HETATM 10928 C  CGA . HEM   E 2 .   ? 23.537 74.348  17.42  1   51.3   ? 401 HEM   A CGA 1 
HETATM 10929 O  O1A . HEM   E 2 .   ? 22.516 74.661  18.009 1   51.12  ? 401 HEM   A O1A 1 
HETATM 10930 O  O2A . HEM   E 2 .   ? 23.584 73.401  16.494 1   51.76  ? 401 HEM   A O2A 1 
HETATM 10931 C  C1B . HEM   E 2 .   ? 25.747 71.395  23.641 1   48.4   ? 401 HEM   A C1B 1 
HETATM 10932 C  C2B . HEM   E 2 .   ? 25.608 70.198  24.455 1   48.22  ? 401 HEM   A C2B 1 
HETATM 10933 C  C3B . HEM   E 2 .   ? 25.802 70.614  25.754 1   47.84  ? 401 HEM   A C3B 1 
HETATM 10934 C  C4B . HEM   E 2 .   ? 26.071 72.022  25.726 1   47.73  ? 401 HEM   A C4B 1 
HETATM 10935 C  CMB . HEM   E 2 .   ? 25.336 68.82   23.932 1   48.12  ? 401 HEM   A CMB 1 
HETATM 10936 C  CAB . HEM   E 2 .   ? 25.723 69.782  26.958 1   47.77  ? 401 HEM   A CAB 1 
HETATM 10937 C  CBB . HEM   E 2 .   ? 24.703 69.085  27.432 1   47.57  ? 401 HEM   A CBB 1 
HETATM 10938 C  C1C . HEM   E 2 .   ? 26.715 74.205  26.791 1   48.01  ? 401 HEM   A C1C 1 
HETATM 10939 C  C2C . HEM   E 2 .   ? 27.009 75.016  27.964 1   48.02  ? 401 HEM   A C2C 1 
HETATM 10940 C  C3C . HEM   E 2 .   ? 27.219 76.289  27.488 1   48.24  ? 401 HEM   A C3C 1 
HETATM 10941 C  C4C . HEM   E 2 .   ? 27.057 76.245  26.071 1   48.26  ? 401 HEM   A C4C 1 
HETATM 10942 C  CMC . HEM   E 2 .   ? 27.071 74.516  29.376 1   47.93  ? 401 HEM   A CMC 1 
HETATM 10943 C  CAC . HEM   E 2 .   ? 27.552 77.496  28.25  1   48.6   ? 401 HEM   A CAC 1 
HETATM 10944 C  CBC . HEM   E 2 .   ? 26.791 78.534  28.517 1   48.8   ? 401 HEM   A CBC 1 
HETATM 10945 C  C1D . HEM   E 2 .   ? 27.073 77.355  23.837 1   48.65  ? 401 HEM   A C1D 1 
HETATM 10946 C  C2D . HEM   E 2 .   ? 27.453 78.493  23.023 1   48.75  ? 401 HEM   A C2D 1 
HETATM 10947 C  C3D . HEM   E 2 .   ? 27.38  78.073  21.711 1   49.18  ? 401 HEM   A C3D 1 
HETATM 10948 C  C4D . HEM   E 2 .   ? 26.895 76.697  21.745 1   48.85  ? 401 HEM   A C4D 1 
HETATM 10949 C  CMD . HEM   E 2 .   ? 27.793 79.855  23.545 1   48.54  ? 401 HEM   A CMD 1 
HETATM 10950 C  CAD . HEM   E 2 .   ? 27.863 78.859  20.521 1   49.61  ? 401 HEM   A CAD 1 
HETATM 10951 C  CBD . HEM   E 2 .   ? 29.359 78.659  20.271 1   50.39  ? 401 HEM   A CBD 1 
HETATM 10952 C  CGD . HEM   E 2 .   ? 29.97  79.465  19.153 1   51.15  ? 401 HEM   A CGD 1 
HETATM 10953 O  O1D . HEM   E 2 .   ? 31.156 79.36   18.863 1   51.15  ? 401 HEM   A O1D 1 
HETATM 10954 O  O2D . HEM   E 2 .   ? 29.159 80.282  18.506 1   51.55  ? 401 HEM   A O2D 1 
HETATM 10955 N  NA  . HEM   E 2 .   ? 26.131 73.776  21.783 1   48.75  ? 401 HEM   A NA  1 
HETATM 10956 N  NB  . HEM   E 2 .   ? 26.02  72.481  24.411 1   47.92  ? 401 HEM   A NB  1 
HETATM 10957 N  NC  . HEM   E 2 .   ? 26.76  74.955  25.658 1   47.98  ? 401 HEM   A NC  1 
HETATM 10958 N  ND  . HEM   E 2 .   ? 26.725 76.287  23.062 1   48.54  ? 401 HEM   A ND  1 
HETATM 10959 FE FE  . HEM   E 2 .   ? 26.563 74.334  23.704 1   47.91  ? 401 HEM   A FE  1 
HETATM 10960 C  C5  . A1H6U F 3 .   ? 20.132 74.904  24.901 1   54.05  ? 402 A1H6U A C5  1 
HETATM 10961 C  C6  . A1H6U F 3 .   ? 20.11  74.457  23.535 1   53.81  ? 402 A1H6U A C6  1 
HETATM 10962 C  C7  . A1H6U F 3 .   ? 23.828 75.29   25.055 1   54.14  ? 402 A1H6U A C7  1 
HETATM 10963 C  C8  . A1H6U F 3 .   ? 23.748 74.509  23.084 1   54.18  ? 402 A1H6U A C8  1 
HETATM 10964 C  C13 . A1H6U F 3 .   ? 21.205 69.868  22.445 1   53.29  ? 402 A1H6U A C13 1 
HETATM 10965 O  O   . A1H6U F 3 .   ? 22.086 74.395  20.68  1   53.36  ? 402 A1H6U A O   1 
HETATM 10966 C  C1  . A1H6U F 3 .   ? 21.259 73.615  21.537 1   53.55  ? 402 A1H6U A C1  1 
HETATM 10967 C  CA  . A1H6U F 3 .   ? 21.265 74.194  22.914 1   53.95  ? 402 A1H6U A CA  1 
HETATM 10968 N  N   . A1H6U F 3 .   ? 22.453 74.539  23.535 1   54.22  ? 402 A1H6U A N   1 
HETATM 10969 C  C3  . A1H6U F 3 .   ? 22.5   75.03   24.808 1   54.13  ? 402 A1H6U A C3  1 
HETATM 10970 C  CG2 . A1H6U F 3 .   ? 21.29  75.171  25.514 1   54.12  ? 402 A1H6U A CG2 1 
HETATM 10971 N  N2  . A1H6U F 3 .   ? 24.604 74.955  23.975 1   54.1   ? 402 A1H6U A N2  1 
HETATM 10972 C  C9  . A1H6U F 3 .   ? 21.665 72.151  21.518 1   53.34  ? 402 A1H6U A C9  1 
HETATM 10973 C  CD1 . A1H6U F 3 .   ? 21.761 71.568  20.113 1   53.33  ? 402 A1H6U A CD1 1 
HETATM 10974 C  CG1 . A1H6U F 3 .   ? 22.212 70.112  20.139 1   53.42  ? 402 A1H6U A CG1 1 
HETATM 10975 C  C12 . A1H6U F 3 .   ? 21.386 69.234  21.075 1   53.48  ? 402 A1H6U A C12 1 
HETATM 10976 C  C14 . A1H6U F 3 .   ? 20.712 71.301  22.349 1   53.13  ? 402 A1H6U A C14 1 
HETATM 10977 C  CHA . HEM   G 2 .   ? 59.396 68.886  20.528 1   51.97  ? 401 HEM   B CHA 1 
HETATM 10978 C  CHB . HEM   G 2 .   ? 60.392 73.542  21.492 1   51.36  ? 401 HEM   B CHB 1 
HETATM 10979 C  CHC . HEM   G 2 .   ? 59.79  72.728  26.256 1   50.64  ? 401 HEM   B CHC 1 
HETATM 10980 C  CHD . HEM   G 2 .   ? 58.97  68.055  25.288 1   51.04  ? 401 HEM   B CHD 1 
HETATM 10981 C  C1A . HEM   G 2 .   ? 59.767 70.246  20.362 1   52.05  ? 401 HEM   B C1A 1 
HETATM 10982 C  C2A . HEM   G 2 .   ? 59.99  70.891  19.078 1   52.64  ? 401 HEM   B C2A 1 
HETATM 10983 C  C3A . HEM   G 2 .   ? 60.261 72.219  19.347 1   52.09  ? 401 HEM   B C3A 1 
HETATM 10984 C  C4A . HEM   G 2 .   ? 60.208 72.364  20.791 1   51.65  ? 401 HEM   B C4A 1 
HETATM 10985 C  CMA . HEM   G 2 .   ? 60.534 73.324  18.371 1   52.07  ? 401 HEM   B CMA 1 
HETATM 10986 C  CAA . HEM   G 2 .   ? 59.916 70.257  17.716 1   54.07  ? 401 HEM   B CAA 1 
HETATM 10987 C  CBA . HEM   G 2 .   ? 61.092 69.337  17.399 1   55.36  ? 401 HEM   B CBA 1 
HETATM 10988 C  CGA . HEM   G 2 .   ? 62.348 70.053  16.984 1   56.11  ? 401 HEM   B CGA 1 
HETATM 10989 O  O1A . HEM   G 2 .   ? 63.397 69.944  17.599 1   56.48  ? 401 HEM   B O1A 1 
HETATM 10990 O  O2A . HEM   G 2 .   ? 62.219 70.78   15.889 1   56.06  ? 401 HEM   B O2A 1 
HETATM 10991 C  C1B . HEM   G 2 .   ? 60.307 73.744  22.897 1   50.9   ? 401 HEM   B C1B 1 
HETATM 10992 C  C2B . HEM   G 2 .   ? 60.501 75.024  23.553 1   50.54  ? 401 HEM   B C2B 1 
HETATM 10993 C  C3B . HEM   G 2 .   ? 60.352 74.772  24.899 1   50.74  ? 401 HEM   B C3B 1 
HETATM 10994 C  C4B . HEM   G 2 .   ? 60.052 73.379  25.053 1   50.77  ? 401 HEM   B C4B 1 
HETATM 10995 C  CMB . HEM   G 2 .   ? 60.755 76.327  22.855 1   50.13  ? 401 HEM   B CMB 1 
HETATM 10996 C  CAB . HEM   G 2 .   ? 60.501 75.723  26.005 1   50.7   ? 401 HEM   B CAB 1 
HETATM 10997 C  CBB . HEM   G 2 .   ? 61.538 76.469  26.324 1   50.36  ? 401 HEM   B CBB 1 
HETATM 10998 C  C1C . HEM   G 2 .   ? 59.465 71.352  26.41  1   50.67  ? 401 HEM   B C1C 1 
HETATM 10999 C  C2C . HEM   G 2 .   ? 59.195 70.698  27.686 1   50.93  ? 401 HEM   B C2C 1 
HETATM 11000 C  C3C . HEM   G 2 .   ? 58.987 69.368  27.379 1   50.93  ? 401 HEM   B C3C 1 
HETATM 11001 C  C4C . HEM   G 2 .   ? 59.12  69.234  25.969 1   50.7   ? 401 HEM   B C4C 1 
HETATM 11002 C  CMC . HEM   G 2 .   ? 59.186 71.37   29.027 1   50.72  ? 401 HEM   B CMC 1 
HETATM 11003 C  CAC . HEM   G 2 .   ? 58.695 68.263  28.295 1   51.03  ? 401 HEM   B CAC 1 
HETATM 11004 C  CBC . HEM   G 2 .   ? 59.479 67.29   28.676 1   51.11  ? 401 HEM   B CBC 1 
HETATM 11005 C  C1D . HEM   G 2 .   ? 59.012 67.864  23.898 1   51.27  ? 401 HEM   B C1D 1 
HETATM 11006 C  C2D . HEM   G 2 .   ? 58.593 66.643  23.244 1   51.44  ? 401 HEM   B C2D 1 
HETATM 11007 C  C3D . HEM   G 2 .   ? 58.65  66.89   21.886 1   51.56  ? 401 HEM   B C3D 1 
HETATM 11008 C  C4D . HEM   G 2 .   ? 59.156 68.247  21.736 1   51.66  ? 401 HEM   B C4D 1 
HETATM 11009 C  CMD . HEM   G 2 .   ? 58.245 65.365  23.942 1   51.41  ? 401 HEM   B CMD 1 
HETATM 11010 C  CAD . HEM   G 2 .   ? 58.149 65.974  20.804 1   51.58  ? 401 HEM   B CAD 1 
HETATM 11011 C  CBD . HEM   G 2 .   ? 56.653 66.135  20.574 1   52.04  ? 401 HEM   B CBD 1 
HETATM 11012 C  CGD . HEM   G 2 .   ? 56.013 65.15   19.634 1   52.68  ? 401 HEM   B CGD 1 
HETATM 11013 O  O1D . HEM   G 2 .   ? 54.814 65.194  19.393 1   52.74  ? 401 HEM   B O1D 1 
HETATM 11014 O  O2D . HEM   G 2 .   ? 56.819 64.251  19.088 1   52.99  ? 401 HEM   B O2D 1 
HETATM 11015 N  NA  . HEM   G 2 .   ? 59.91  71.143  21.376 1   51.47  ? 401 HEM   B NA  1 
HETATM 11016 N  NB  . HEM   G 2 .   ? 60.033 72.769  23.802 1   50.6   ? 401 HEM   B NB  1 
HETATM 11017 N  NC  . HEM   G 2 .   ? 59.409 70.46   25.387 1   50.46  ? 401 HEM   B NC  1 
HETATM 11018 N  ND  . HEM   G 2 .   ? 59.363 68.817  22.987 1   51.02  ? 401 HEM   B ND  1 
HETATM 11019 FE FE  . HEM   G 2 .   ? 59.539 70.827  23.368 1   50.32  ? 401 HEM   B FE  1 
HETATM 11020 C  C5  . A1H6U H 3 .   ? 66.104 70.37   24.409 1   36.92  ? 402 A1H6U B C5  1 
HETATM 11021 C  C6  . A1H6U H 3 .   ? 66.081 70.641  23.004 1   36.91  ? 402 A1H6U B C6  1 
HETATM 11022 C  C7  . A1H6U H 3 .   ? 62.397 70.293  24.739 1   37.27  ? 402 A1H6U B C7  1 
HETATM 11023 C  C8  . A1H6U H 3 .   ? 62.448 70.713  22.642 1   37.22  ? 402 A1H6U B C8  1 
HETATM 11024 C  C13 . A1H6U H 3 .   ? 65.485 75.089  20.916 1   37.46  ? 402 A1H6U B C13 1 
HETATM 11025 O  O   . A1H6U H 3 .   ? 64.121 70.373  20.188 1   37.61  ? 402 A1H6U B O   1 
HETATM 11026 C  C1  . A1H6U H 3 .   ? 64.907 71.286  20.937 1   37.4   ? 402 A1H6U B C1  1 
HETATM 11027 C  CA  . A1H6U H 3 .   ? 64.924 70.843  22.366 1   37.15  ? 402 A1H6U B CA  1 
HETATM 11028 N  N   . A1H6U H 3 .   ? 63.752 70.645  23.054 1   37.19  ? 402 A1H6U B N   1 
HETATM 11029 C  C3  . A1H6U H 3 .   ? 63.726 70.377  24.395 1   37.24  ? 402 A1H6U B C3  1 
HETATM 11030 C  CG2 . A1H6U H 3 .   ? 64.952 70.273  25.08  1   37.11  ? 402 A1H6U B CG2 1 
HETATM 11031 N  N2  . A1H6U H 3 .   ? 61.606 70.528  23.638 1   37.44  ? 402 A1H6U B N2  1 
HETATM 11032 C  C9  . A1H6U H 3 .   ? 64.495 72.737  20.713 1   37.35  ? 402 A1H6U B C9  1 
HETATM 11033 C  CD1 . A1H6U H 3 .   ? 64.213 73.039  19.24  1   37.38  ? 402 A1H6U B CD1 1 
HETATM 11034 C  CG1 . A1H6U H 3 .   ? 64.043 74.523  18.938 1   37.61  ? 402 A1H6U B CG1 1 
HETATM 11035 C  C12 . A1H6U H 3 .   ? 65.227 75.336  19.44  1   37.75  ? 402 A1H6U B C12 1 
HETATM 11036 C  C14 . A1H6U H 3 .   ? 65.616 73.618  21.263 1   37.32  ? 402 A1H6U B C14 1 
HETATM 11037 C  CHA . HEM   I 2 .   ? 56.668 64.544  58.082 1   49.22  ? 401 HEM   C CHA 1 
HETATM 11038 C  CHB . HEM   I 2 .   ? 53.786 60.761  57.103 1   49.3   ? 401 HEM   C CHB 1 
HETATM 11039 C  CHC . HEM   I 2 .   ? 54.186 61.672  52.325 1   49.14  ? 401 HEM   C CHC 1 
HETATM 11040 C  CHD . HEM   I 2 .   ? 57.199 65.335  53.333 1   48.31  ? 401 HEM   C CHD 1 
HETATM 11041 C  C1A . HEM   I 2 .   ? 55.857 63.39   58.249 1   49.67  ? 401 HEM   C C1A 1 
HETATM 11042 C  C2A . HEM   I 2 .   ? 55.488 62.815  59.533 1   50.31  ? 401 HEM   C C2A 1 
HETATM 11043 C  C3A . HEM   I 2 .   ? 54.656 61.747  59.261 1   49.87  ? 401 HEM   C C3A 1 
HETATM 11044 C  C4A . HEM   I 2 .   ? 54.537 61.678  57.814 1   49.45  ? 401 HEM   C C4A 1 
HETATM 11045 C  CMA . HEM   I 2 .   ? 53.962 60.843  60.237 1   49.83  ? 401 HEM   C CMA 1 
HETATM 11046 C  CAA . HEM   I 2 .   ? 55.897 63.284  60.904 1   51.25  ? 401 HEM   C CAA 1 
HETATM 11047 C  CBA . HEM   I 2 .   ? 57.375 63.089  61.194 1   52.41  ? 401 HEM   C CBA 1 
HETATM 11048 C  CGA . HEM   I 2 .   ? 57.705 61.76   61.809 1   53.52  ? 401 HEM   C CGA 1 
HETATM 11049 O  O1A . HEM   I 2 .   ? 58.284 60.849  61.221 1   54     ? 401 HEM   C O1A 1 
HETATM 11050 O  O2A . HEM   I 2 .   ? 57.359 61.704  63.07  1   53.58  ? 401 HEM   C O2A 1 
HETATM 11051 C  C1B . HEM   I 2 .   ? 53.649 60.658  55.69  1   49.4   ? 401 HEM   C C1B 1 
HETATM 11052 C  C2B . HEM   I 2 .   ? 52.789 59.698  55.021 1   49.31  ? 401 HEM   C C2B 1 
HETATM 11053 C  C3B . HEM   I 2 .   ? 52.933 59.955  53.674 1   49.36  ? 401 HEM   C C3B 1 
HETATM 11054 C  C4B . HEM   I 2 .   ? 53.834 61.061  53.528 1   49.3   ? 401 HEM   C C4B 1 
HETATM 11055 C  CMB . HEM   I 2 .   ? 51.902 58.703  55.706 1   49.07  ? 401 HEM   C CMB 1 
HETATM 11056 C  CAB . HEM   I 2 .   ? 52.312 59.235  52.562 1   49.58  ? 401 HEM   C CAB 1 
HETATM 11057 C  CBB . HEM   I 2 .   ? 52.421 57.964  52.232 1   49.72  ? 401 HEM   C CBB 1 
HETATM 11058 C  C1C . HEM   I 2 .   ? 55.038 62.803  52.175 1   48.81  ? 401 HEM   C C1C 1 
HETATM 11059 C  C2C . HEM   I 2 .   ? 55.413 63.399  50.9   1   48.36  ? 401 HEM   C C2C 1 
HETATM 11060 C  C3C . HEM   I 2 .   ? 56.281 64.419  51.217 1   48.15  ? 401 HEM   C C3C 1 
HETATM 11061 C  C4C . HEM   I 2 .   ? 56.418 64.442  52.636 1   48.44  ? 401 HEM   C C4C 1 
HETATM 11062 C  CMC . HEM   I 2 .   ? 54.926 62.956  49.554 1   48.42  ? 401 HEM   C CMC 1 
HETATM 11063 C  CAC . HEM   I 2 .   ? 56.969 65.34   50.313 1   48.1   ? 401 HEM   C CAC 1 
HETATM 11064 C  CBC . HEM   I 2 .   ? 58.249 65.366  49.98  1   48.06  ? 401 HEM   C CBC 1 
HETATM 11065 C  C1D . HEM   I 2 .   ? 57.334 65.439  54.721 1   48.41  ? 401 HEM   C C1D 1 
HETATM 11066 C  C2D . HEM   I 2 .   ? 57.995 66.545  55.384 1   48.64  ? 401 HEM   C C2D 1 
HETATM 11067 C  C3D . HEM   I 2 .   ? 57.805 66.355  56.735 1   48.57  ? 401 HEM   C C3D 1 
HETATM 11068 C  C4D . HEM   I 2 .   ? 57.065 65.109  56.876 1   48.84  ? 401 HEM   C C4D 1 
HETATM 11069 C  CMD . HEM   I 2 .   ? 58.757 67.636  54.696 1   48.55  ? 401 HEM   C CMD 1 
HETATM 11070 C  CAD . HEM   I 2 .   ? 58.175 67.338  57.812 1   47.74  ? 401 HEM   C CAD 1 
HETATM 11071 C  CBD . HEM   I 2 .   ? 57.077 68.371  58.03  1   47.29  ? 401 HEM   C CBD 1 
HETATM 11072 C  CGD . HEM   I 2 .   ? 57.382 69.483  58.996 1   47.13  ? 401 HEM   C CGD 1 
HETATM 11073 O  O1D . HEM   I 2 .   ? 56.574 70.375  59.2   1   47.2   ? 401 HEM   C O1D 1 
HETATM 11074 O  O2D . HEM   I 2 .   ? 58.558 69.437  59.588 1   47.04  ? 401 HEM   C O2D 1 
HETATM 11075 N  NA  . HEM   I 2 .   ? 55.281 62.69   57.232 1   49.47  ? 401 HEM   C NA  1 
HETATM 11076 N  NB  . HEM   I 2 .   ? 54.272 61.468  54.786 1   49.23  ? 401 HEM   C NB  1 
HETATM 11077 N  NC  . HEM   I 2 .   ? 55.643 63.445  53.208 1   48.76  ? 401 HEM   C NC  1 
HETATM 11078 N  ND  . HEM   I 2 .   ? 56.796 64.576  55.622 1   48.56  ? 401 HEM   C ND  1 
HETATM 11079 FE FE  . HEM   I 2 .   ? 55.401 63.131  55.218 1   48.99  ? 401 HEM   C FE  1 
HETATM 11080 C  C5  . A1H6U J 3 .   ? 59.872 58.181  54.387 1   54.03  ? 402 A1H6U C C5  1 
HETATM 11081 C  C6  . A1H6U J 3 .   ? 59.68  58.07   55.806 1   54.12  ? 402 A1H6U C C6  1 
HETATM 11082 C  C7  . A1H6U J 3 .   ? 57.745 61.196  54.019 1   54.72  ? 402 A1H6U C C7  1 
HETATM 11083 C  C8  . A1H6U J 3 .   ? 57.453 60.948  56.106 1   54.84  ? 402 A1H6U C C8  1 
HETATM 11084 C  C13 . A1H6U J 3 .   ? 54.943 56.745  57.348 1   53.9   ? 402 A1H6U C C13 1 
HETATM 11085 O  O   . A1H6U J 3 .   ? 58.755 59.57   58.62  1   54.19  ? 402 A1H6U C O   1 
HETATM 11086 C  C1  . A1H6U J 3 .   ? 58.324 58.51   57.792 1   53.86  ? 402 A1H6U C C1  1 
HETATM 11087 C  CA  . A1H6U J 3 .   ? 58.753 58.825  56.404 1   54.25  ? 402 A1H6U C CA  1 
HETATM 11088 N  N   . A1H6U J 3 .   ? 58.212 59.881  55.703 1   54.59  ? 402 A1H6U C N   1 
HETATM 11089 C  C3  . A1H6U J 3 .   ? 58.401 60.034  54.359 1   54.43  ? 402 A1H6U C C3  1 
HETATM 11090 C  CG2 . A1H6U J 3 .   ? 59.175 59.076  53.68  1   54.05  ? 402 A1H6U C CG2 1 
HETATM 11091 N  N2  . A1H6U J 3 .   ? 57.147 61.76   55.115 1   54.76  ? 402 A1H6U C N2  1 
HETATM 11092 C  C9  . A1H6U J 3 .   ? 56.838 58.289  57.98  1   53.6   ? 402 A1H6U C C9  1 
HETATM 11093 C  CD1 . A1H6U J 3 .   ? 56.534 57.994  59.446 1   53.47  ? 402 A1H6U C CD1 1 
HETATM 11094 C  CG1 . A1H6U J 3 .   ? 55.144 57.446  59.712 1   53.45  ? 402 A1H6U C CG1 1 
HETATM 11095 C  C12 . A1H6U J 3 .   ? 54.794 56.293  58.791 1   53.76  ? 402 A1H6U C C12 1 
HETATM 11096 C  C14 . A1H6U J 3 .   ? 56.375 57.165  57.065 1   53.62  ? 402 A1H6U C C14 1 
HETATM 11097 C  CHA . HEM   K 2 .   ? 30.329 85.192  57.197 1   50.35  ? 401 HEM   D CHA 1 
HETATM 11098 C  CHB . HEM   K 2 .   ? 33.182 88.792  55.643 1   50.14  ? 401 HEM   D CHB 1 
HETATM 11099 C  CHC . HEM   K 2 .   ? 32.714 87.249  51.041 1   49.46  ? 401 HEM   D CHC 1 
HETATM 11100 C  CHD . HEM   K 2 .   ? 29.706 83.771  52.602 1   49.93  ? 401 HEM   D CHD 1 
HETATM 11101 C  C1A . HEM   K 2 .   ? 31.141 86.356  57.178 1   50.45  ? 401 HEM   D C1A 1 
HETATM 11102 C  C2A . HEM   K 2 .   ? 31.554 87.094  58.363 1   50.52  ? 401 HEM   D C2A 1 
HETATM 11103 C  C3A . HEM   K 2 .   ? 32.375 88.11   57.926 1   50.17  ? 401 HEM   D C3A 1 
HETATM 11104 C  C4A . HEM   K 2 .   ? 32.442 87.989  56.479 1   50.15  ? 401 HEM   D C4A 1 
HETATM 11105 C  CMA . HEM   K 2 .   ? 33.093 89.134  58.75  1   50.02  ? 401 HEM   D CMA 1 
HETATM 11106 C  CAA . HEM   K 2 .   ? 31.159 86.838  59.792 1   50.97  ? 401 HEM   D CAA 1 
HETATM 11107 C  CBA . HEM   K 2 .   ? 29.703 87.198  60.093 1   51.44  ? 401 HEM   D CBA 1 
HETATM 11108 C  CGA . HEM   K 2 .   ? 29.461 88.663  60.339 1   52.03  ? 401 HEM   D CGA 1 
HETATM 11109 O  O1A . HEM   K 2 .   ? 28.757 89.375  59.622 1   51.93  ? 401 HEM   D O1A 1 
HETATM 11110 O  O2A . HEM   K 2 .   ? 30.065 89.097  61.423 1   52.43  ? 401 HEM   D O2A 1 
HETATM 11111 C  C1B . HEM   K 2 .   ? 33.313 88.701  54.237 1   50.21  ? 401 HEM   D C1B 1 
HETATM 11112 C  C2B . HEM   K 2 .   ? 34.164 89.569  53.434 1   50.02  ? 401 HEM   D C2B 1 
HETATM 11113 C  C3B . HEM   K 2 .   ? 34.004 89.131  52.135 1   49.98  ? 401 HEM   D C3B 1 
HETATM 11114 C  C4B . HEM   K 2 .   ? 33.095 88.016  52.146 1   49.95  ? 401 HEM   D C4B 1 
HETATM 11115 C  CMB . HEM   K 2 .   ? 35.03  90.672  53.969 1   49.74  ? 401 HEM   D CMB 1 
HETATM 11116 C  CAB . HEM   K 2 .   ? 34.615 89.708  50.938 1   50.03  ? 401 HEM   D CAB 1 
HETATM 11117 C  CBB . HEM   K 2 .   ? 34.486 90.931  50.466 1   50.1   ? 401 HEM   D CBB 1 
HETATM 11118 C  C1C . HEM   K 2 .   ? 31.867 86.104  51.065 1   49.36  ? 401 HEM   D C1C 1 
HETATM 11119 C  C2C . HEM   K 2 .   ? 31.445 85.357  49.892 1   49.42  ? 401 HEM   D C2C 1 
HETATM 11120 C  C3C . HEM   K 2 .   ? 30.579 84.399  50.364 1   49.29  ? 401 HEM   D C3C 1 
HETATM 11121 C  C4C . HEM   K 2 .   ? 30.484 84.554  51.772 1   49.64  ? 401 HEM   D C4C 1 
HETATM 11122 C  CMC . HEM   K 2 .   ? 31.882 85.626  48.483 1   49.4   ? 401 HEM   D CMC 1 
HETATM 11123 C  CAC . HEM   K 2 .   ? 29.866 83.375  49.603 1   49.21  ? 401 HEM   D CAC 1 
HETATM 11124 C  CBC . HEM   K 2 .   ? 28.594 83.313  49.303 1   49.18  ? 401 HEM   D CBC 1 
HETATM 11125 C  C1D . HEM   K 2 .   ? 29.608 83.845  54.007 1   49.95  ? 401 HEM   D C1D 1 
HETATM 11126 C  C2D . HEM   K 2 .   ? 28.957 82.845  54.828 1   49.76  ? 401 HEM   D C2D 1 
HETATM 11127 C  C3D . HEM   K 2 .   ? 29.193 83.205  56.138 1   50.07  ? 401 HEM   D C3D 1 
HETATM 11128 C  C4D . HEM   K 2 .   ? 29.933 84.455  56.093 1   50.19  ? 401 HEM   D C4D 1 
HETATM 11129 C  CMD . HEM   K 2 .   ? 28.135 81.704  54.313 1   49.3   ? 401 HEM   D CMD 1 
HETATM 11130 C  CAD . HEM   K 2 .   ? 28.872 82.375  57.353 1   50.19  ? 401 HEM   D CAD 1 
HETATM 11131 C  CBD . HEM   K 2 .   ? 29.984 81.374  57.676 1   50.34  ? 401 HEM   D CBD 1 
HETATM 11132 C  CGD . HEM   K 2 .   ? 29.707 80.372  58.767 1   50.55  ? 401 HEM   D CGD 1 
HETATM 11133 O  O1D . HEM   K 2 .   ? 30.534 79.515  59.051 1   50.52  ? 401 HEM   D O1D 1 
HETATM 11134 O  O2D . HEM   K 2 .   ? 28.544 80.47   59.396 1   50.67  ? 401 HEM   D O2D 1 
HETATM 11135 N  NA  . HEM   K 2 .   ? 31.678 86.917  56.057 1   50.29  ? 401 HEM   D NA  1 
HETATM 11136 N  NB  . HEM   K 2 .   ? 32.679 87.78   53.46  1   50.16  ? 401 HEM   D NB  1 
HETATM 11137 N  NC  . HEM   K 2 .   ? 31.292 85.602  52.187 1   49.62  ? 401 HEM   D NC  1 
HETATM 11138 N  ND  . HEM   K 2 .   ? 30.18  84.811  54.774 1   50.06  ? 401 HEM   D ND  1 
HETATM 11139 FE FE  . HEM   K 2 .   ? 31.575 86.174  54.134 1   49.92  ? 401 HEM   D FE  1 
HETATM 11140 C  C5  . A1H6U L 3 .   ? 26.903 90.752  52.751 1   42.37  ? 402 A1H6U D C5  1 
HETATM 11141 C  C6  . A1H6U L 3 .   ? 27.396 91.26   53.999 1   42.44  ? 402 A1H6U D C6  1 
HETATM 11142 C  C7  . A1H6U L 3 .   ? 29.07  87.742  52.734 1   42.44  ? 402 A1H6U D C7  1 
HETATM 11143 C  C8  . A1H6U L 3 .   ? 29.794 88.549  54.561 1   43.09  ? 402 A1H6U D C8  1 
HETATM 11144 C  C13 . A1H6U L 3 .   ? 31.692 93.225  55.485 1   40.78  ? 402 A1H6U D C13 1 
HETATM 11145 O  O   . A1H6U L 3 .   ? 28.487 89.85   56.941 1   42.65  ? 402 A1H6U D O   1 
HETATM 11146 C  C1  . A1H6U L 3 .   ? 28.633 90.981  56.082 1   42.25  ? 402 A1H6U D C1  1 
HETATM 11147 C  CA  . A1H6U L 3 .   ? 28.364 90.61   54.656 1   42.66  ? 402 A1H6U D CA  1 
HETATM 11148 N  N   . A1H6U L 3 .   ? 28.849 89.437  54.104 1   43.06  ? 402 A1H6U D N   1 
HETATM 11149 C  C3  . A1H6U L 3 .   ? 28.394 88.925  52.919 1   42.57  ? 402 A1H6U D C3  1 
HETATM 11150 C  CG2 . A1H6U L 3 .   ? 27.394 89.625  52.225 1   42.29  ? 402 A1H6U D CG2 1 
HETATM 11151 N  N2  . A1H6U L 3 .   ? 29.954 87.52   53.756 1   42.57  ? 402 A1H6U D N2  1 
HETATM 11152 C  C9  . A1H6U L 3 .   ? 30.005 91.58   56.272 1   41.26  ? 402 A1H6U D C9  1 
HETATM 11153 C  CD1 . A1H6U L 3 .   ? 30.368 91.873  57.722 1   40.84  ? 402 A1H6U D CD1 1 
HETATM 11154 C  CG1 . A1H6U L 3 .   ? 31.822 92.321  57.843 1   40.63  ? 402 A1H6U D CG1 1 
HETATM 11155 C  C12 . A1H6U L 3 .   ? 32.159 93.474  56.914 1   40.78  ? 402 A1H6U D C12 1 
HETATM 11156 C  C14 . A1H6U L 3 .   ? 30.233 92.81   55.42  1   40.89  ? 402 A1H6U D C14 1 
HETATM 11157 O  O   . HOH   M 4 .   ? 60.021 88.987  24.713 1   48.41  ? 501 HOH   A O   1 
HETATM 11158 O  O   . HOH   M 4 .   ? 43.381 101.139 14.8   1   53.29  ? 502 HOH   A O   1 
HETATM 11159 O  O   . HOH   M 4 .   ? 21.302 88.986  56.623 1   37.98  ? 503 HOH   A O   1 
HETATM 11160 O  O   . HOH   N 4 .   ? 47.061 63.957  20.347 1   35.32  ? 501 HOH   B O   1 
HETATM 11161 O  O   . HOH   O 4 .   ? 45.241 42.71   72.026 1   43.98  ? 501 HOH   D O   1 
HETATM 11162 O  O   . HOH   O 4 .   ? 41.791 46.275  50.455 1   36.88  ? 502 HOH   D O   1 
# 
