data_9E4R
# 
_entry.id   9E4R 
# 
_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   9E4R         pdb_00009e4r 10.2210/pdb9e4r/pdb 
WWPDB D_1000289434 ?            ?                   
EMDB  EMD-47518    ?            ?                   
# 
_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       2025-03-19 
_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                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9E4R 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-25 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'Escherichia coli encapsulin-associated DyP peroxidase' 
_pdbx_database_related.db_id          EMD-47518 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              tgiessen@umich.edu 
_pdbx_contact_author.name_first         Tobias 
_pdbx_contact_author.name_last          Giessen 
_pdbx_contact_author.name_mi            W. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-6328-2031 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Andreas, M.P.' 1 0000-0001-8871-3053 
'Ubilla, N.C.'  2 0000-0003-0411-8674 
'Giessen, T.W.' 3 0000-0001-6328-2031 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Biorxiv 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2692-8205 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Structural and biochemical characterization of a widespread enterobacterial peroxidase encapsulin.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1101/2024.11.27.625667 
_citation.pdbx_database_id_PubMed   39651212 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Ubilla-Rodriguez, N.C.' 1 0000-0003-0411-8674 
primary 'Andreas, M.P.'          2 0000-0001-8871-3053 
primary 'Giessen, T.W.'          3 0000-0001-6328-2031 
# 
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 'Dyp-type peroxidase'             40644.516 1 ? ? ? ? 
2 non-polymer nat 'PROTOPORPHYRIN IX CONTAINING FE' 616.487   1 ? ? ? ? 
# 
_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       
;MHHHHHHGGSENLYFQSGGSGCPFSQSVSQPVDERLTRAAIFLVVTINPGKAAEVAVRAHCSILSSLIRGVGFRISDGGL
SCVMGVSEGGWERLFGDTKPEYLHVFREINGVHHAPSTPGDLLYHIRAARMDLCFELASRILSDLGNSVSVVDSVQGFRY
FDDRDLLGFVDGTENPVAQAAVDATLIGDEDMVFAGGSYVIVQKYLHDLDKWNAIPVEQQEKIIGREKLSDIELRDADKP
SYAHNVLTSIEEDGEDVDILRDNMPFGDPGKGEFGTYFIGYSRKPERIERMLENMFIGNPPGNYDRILDVSRAITGTLFF
VPTTSFLDSIEPQSAPGQQGDDVINTLRSTAIKGDIMPGSLNIGSLKKEV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MHHHHHHGGSENLYFQSGGSGCPFSQSVSQPVDERLTRAAIFLVVTINPGKAAEVAVRAHCSILSSLIRGVGFRISDGGL
SCVMGVSEGGWERLFGDTKPEYLHVFREINGVHHAPSTPGDLLYHIRAARMDLCFELASRILSDLGNSVSVVDSVQGFRY
FDDRDLLGFVDGTENPVAQAAVDATLIGDEDMVFAGGSYVIVQKYLHDLDKWNAIPVEQQEKIIGREKLSDIELRDADKP
SYAHNVLTSIEEDGEDVDILRDNMPFGDPGKGEFGTYFIGYSRKPERIERMLENMFIGNPPGNYDRILDVSRAITGTLFF
VPTTSFLDSIEPQSAPGQQGDDVINTLRSTAIKGDIMPGSLNIGSLKKEV
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        'PROTOPORPHYRIN IX CONTAINING FE' 
_pdbx_entity_nonpoly.comp_id     HEM 
# 
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   HIS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   GLY n 
1 9   GLY n 
1 10  SER n 
1 11  GLU n 
1 12  ASN n 
1 13  LEU n 
1 14  TYR n 
1 15  PHE n 
1 16  GLN n 
1 17  SER n 
1 18  GLY n 
1 19  GLY n 
1 20  SER n 
1 21  GLY n 
1 22  CYS n 
1 23  PRO n 
1 24  PHE n 
1 25  SER n 
1 26  GLN n 
1 27  SER n 
1 28  VAL n 
1 29  SER n 
1 30  GLN n 
1 31  PRO n 
1 32  VAL n 
1 33  ASP n 
1 34  GLU n 
1 35  ARG n 
1 36  LEU n 
1 37  THR n 
1 38  ARG n 
1 39  ALA n 
1 40  ALA n 
1 41  ILE n 
1 42  PHE n 
1 43  LEU n 
1 44  VAL n 
1 45  VAL n 
1 46  THR n 
1 47  ILE n 
1 48  ASN n 
1 49  PRO n 
1 50  GLY n 
1 51  LYS n 
1 52  ALA n 
1 53  ALA n 
1 54  GLU n 
1 55  VAL n 
1 56  ALA n 
1 57  VAL n 
1 58  ARG n 
1 59  ALA n 
1 60  HIS n 
1 61  CYS n 
1 62  SER n 
1 63  ILE n 
1 64  LEU n 
1 65  SER n 
1 66  SER n 
1 67  LEU n 
1 68  ILE n 
1 69  ARG n 
1 70  GLY n 
1 71  VAL n 
1 72  GLY n 
1 73  PHE n 
1 74  ARG n 
1 75  ILE n 
1 76  SER n 
1 77  ASP n 
1 78  GLY n 
1 79  GLY n 
1 80  LEU n 
1 81  SER n 
1 82  CYS n 
1 83  VAL n 
1 84  MET n 
1 85  GLY n 
1 86  VAL n 
1 87  SER n 
1 88  GLU n 
1 89  GLY n 
1 90  GLY n 
1 91  TRP n 
1 92  GLU n 
1 93  ARG n 
1 94  LEU n 
1 95  PHE n 
1 96  GLY n 
1 97  ASP n 
1 98  THR n 
1 99  LYS n 
1 100 PRO n 
1 101 GLU n 
1 102 TYR n 
1 103 LEU n 
1 104 HIS n 
1 105 VAL n 
1 106 PHE n 
1 107 ARG n 
1 108 GLU n 
1 109 ILE n 
1 110 ASN n 
1 111 GLY n 
1 112 VAL n 
1 113 HIS n 
1 114 HIS n 
1 115 ALA n 
1 116 PRO n 
1 117 SER n 
1 118 THR n 
1 119 PRO n 
1 120 GLY n 
1 121 ASP n 
1 122 LEU n 
1 123 LEU n 
1 124 TYR n 
1 125 HIS n 
1 126 ILE n 
1 127 ARG n 
1 128 ALA n 
1 129 ALA n 
1 130 ARG n 
1 131 MET n 
1 132 ASP n 
1 133 LEU n 
1 134 CYS n 
1 135 PHE n 
1 136 GLU n 
1 137 LEU n 
1 138 ALA n 
1 139 SER n 
1 140 ARG n 
1 141 ILE n 
1 142 LEU n 
1 143 SER n 
1 144 ASP n 
1 145 LEU n 
1 146 GLY n 
1 147 ASN n 
1 148 SER n 
1 149 VAL n 
1 150 SER n 
1 151 VAL n 
1 152 VAL n 
1 153 ASP n 
1 154 SER n 
1 155 VAL n 
1 156 GLN n 
1 157 GLY n 
1 158 PHE n 
1 159 ARG n 
1 160 TYR n 
1 161 PHE n 
1 162 ASP n 
1 163 ASP n 
1 164 ARG n 
1 165 ASP n 
1 166 LEU n 
1 167 LEU n 
1 168 GLY n 
1 169 PHE n 
1 170 VAL n 
1 171 ASP n 
1 172 GLY n 
1 173 THR n 
1 174 GLU n 
1 175 ASN n 
1 176 PRO n 
1 177 VAL n 
1 178 ALA n 
1 179 GLN n 
1 180 ALA n 
1 181 ALA n 
1 182 VAL n 
1 183 ASP n 
1 184 ALA n 
1 185 THR n 
1 186 LEU n 
1 187 ILE n 
1 188 GLY n 
1 189 ASP n 
1 190 GLU n 
1 191 ASP n 
1 192 MET n 
1 193 VAL n 
1 194 PHE n 
1 195 ALA n 
1 196 GLY n 
1 197 GLY n 
1 198 SER n 
1 199 TYR n 
1 200 VAL n 
1 201 ILE n 
1 202 VAL n 
1 203 GLN n 
1 204 LYS n 
1 205 TYR n 
1 206 LEU n 
1 207 HIS n 
1 208 ASP n 
1 209 LEU n 
1 210 ASP n 
1 211 LYS n 
1 212 TRP n 
1 213 ASN n 
1 214 ALA n 
1 215 ILE n 
1 216 PRO n 
1 217 VAL n 
1 218 GLU n 
1 219 GLN n 
1 220 GLN n 
1 221 GLU n 
1 222 LYS n 
1 223 ILE n 
1 224 ILE n 
1 225 GLY n 
1 226 ARG n 
1 227 GLU n 
1 228 LYS n 
1 229 LEU n 
1 230 SER n 
1 231 ASP n 
1 232 ILE n 
1 233 GLU n 
1 234 LEU n 
1 235 ARG n 
1 236 ASP n 
1 237 ALA n 
1 238 ASP n 
1 239 LYS n 
1 240 PRO n 
1 241 SER n 
1 242 TYR n 
1 243 ALA n 
1 244 HIS n 
1 245 ASN n 
1 246 VAL n 
1 247 LEU n 
1 248 THR n 
1 249 SER n 
1 250 ILE n 
1 251 GLU n 
1 252 GLU n 
1 253 ASP n 
1 254 GLY n 
1 255 GLU n 
1 256 ASP n 
1 257 VAL n 
1 258 ASP n 
1 259 ILE n 
1 260 LEU n 
1 261 ARG n 
1 262 ASP n 
1 263 ASN n 
1 264 MET n 
1 265 PRO n 
1 266 PHE n 
1 267 GLY n 
1 268 ASP n 
1 269 PRO n 
1 270 GLY n 
1 271 LYS n 
1 272 GLY n 
1 273 GLU n 
1 274 PHE n 
1 275 GLY n 
1 276 THR n 
1 277 TYR n 
1 278 PHE n 
1 279 ILE n 
1 280 GLY n 
1 281 TYR n 
1 282 SER n 
1 283 ARG n 
1 284 LYS n 
1 285 PRO n 
1 286 GLU n 
1 287 ARG n 
1 288 ILE n 
1 289 GLU n 
1 290 ARG n 
1 291 MET n 
1 292 LEU n 
1 293 GLU n 
1 294 ASN n 
1 295 MET n 
1 296 PHE n 
1 297 ILE n 
1 298 GLY n 
1 299 ASN n 
1 300 PRO n 
1 301 PRO n 
1 302 GLY n 
1 303 ASN n 
1 304 TYR n 
1 305 ASP n 
1 306 ARG n 
1 307 ILE n 
1 308 LEU n 
1 309 ASP n 
1 310 VAL n 
1 311 SER n 
1 312 ARG n 
1 313 ALA n 
1 314 ILE n 
1 315 THR n 
1 316 GLY n 
1 317 THR n 
1 318 LEU n 
1 319 PHE n 
1 320 PHE n 
1 321 VAL n 
1 322 PRO n 
1 323 THR n 
1 324 THR n 
1 325 SER n 
1 326 PHE n 
1 327 LEU n 
1 328 ASP n 
1 329 SER n 
1 330 ILE n 
1 331 GLU n 
1 332 PRO n 
1 333 GLN n 
1 334 SER n 
1 335 ALA n 
1 336 PRO n 
1 337 GLY n 
1 338 GLN n 
1 339 GLN n 
1 340 GLY n 
1 341 ASP n 
1 342 ASP n 
1 343 VAL n 
1 344 ILE n 
1 345 ASN n 
1 346 THR n 
1 347 LEU n 
1 348 ARG n 
1 349 SER n 
1 350 THR n 
1 351 ALA n 
1 352 ILE n 
1 353 LYS n 
1 354 GLY n 
1 355 ASP n 
1 356 ILE n 
1 357 MET n 
1 358 PRO n 
1 359 GLY n 
1 360 SER n 
1 361 LEU n 
1 362 ASN n 
1 363 ILE n 
1 364 GLY n 
1 365 SER n 
1 366 LEU n 
1 367 LYS n 
1 368 LYS n 
1 369 GLU n 
1 370 VAL 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                   370 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'FPI65_30880, FWK02_13910' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    KTE40 
_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      'Escherichia coli' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1169357 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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 
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 
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   -18 ?   ?   ?   A . n 
A 1 2   HIS 2   -17 ?   ?   ?   A . n 
A 1 3   HIS 3   -16 ?   ?   ?   A . n 
A 1 4   HIS 4   -15 ?   ?   ?   A . n 
A 1 5   HIS 5   -14 ?   ?   ?   A . n 
A 1 6   HIS 6   -13 ?   ?   ?   A . n 
A 1 7   HIS 7   -12 ?   ?   ?   A . n 
A 1 8   GLY 8   -11 ?   ?   ?   A . n 
A 1 9   GLY 9   -10 ?   ?   ?   A . n 
A 1 10  SER 10  -9  ?   ?   ?   A . n 
A 1 11  GLU 11  -8  ?   ?   ?   A . n 
A 1 12  ASN 12  -7  ?   ?   ?   A . n 
A 1 13  LEU 13  -6  ?   ?   ?   A . n 
A 1 14  TYR 14  -5  ?   ?   ?   A . n 
A 1 15  PHE 15  -4  ?   ?   ?   A . n 
A 1 16  GLN 16  -3  ?   ?   ?   A . n 
A 1 17  SER 17  -2  ?   ?   ?   A . n 
A 1 18  GLY 18  -1  ?   ?   ?   A . n 
A 1 19  GLY 19  0   ?   ?   ?   A . n 
A 1 20  SER 20  1   ?   ?   ?   A . n 
A 1 21  GLY 21  2   ?   ?   ?   A . n 
A 1 22  CYS 22  3   3   CYS CYS A . n 
A 1 23  PRO 23  4   4   PRO PRO A . n 
A 1 24  PHE 24  5   5   PHE PHE A . n 
A 1 25  SER 25  6   6   SER SER A . n 
A 1 26  GLN 26  7   7   GLN GLN A . n 
A 1 27  SER 27  8   8   SER SER A . n 
A 1 28  VAL 28  9   9   VAL VAL A . n 
A 1 29  SER 29  10  10  SER SER A . n 
A 1 30  GLN 30  11  11  GLN GLN A . n 
A 1 31  PRO 31  12  12  PRO PRO A . n 
A 1 32  VAL 32  13  13  VAL VAL A . n 
A 1 33  ASP 33  14  14  ASP ASP A . n 
A 1 34  GLU 34  15  15  GLU GLU A . n 
A 1 35  ARG 35  16  16  ARG ARG A . n 
A 1 36  LEU 36  17  17  LEU LEU A . n 
A 1 37  THR 37  18  18  THR THR A . n 
A 1 38  ARG 38  19  19  ARG ARG A . n 
A 1 39  ALA 39  20  20  ALA ALA A . n 
A 1 40  ALA 40  21  21  ALA ALA A . n 
A 1 41  ILE 41  22  22  ILE ILE A . n 
A 1 42  PHE 42  23  23  PHE PHE A . n 
A 1 43  LEU 43  24  24  LEU LEU A . n 
A 1 44  VAL 44  25  25  VAL VAL A . n 
A 1 45  VAL 45  26  26  VAL VAL A . n 
A 1 46  THR 46  27  27  THR THR A . n 
A 1 47  ILE 47  28  28  ILE ILE A . n 
A 1 48  ASN 48  29  29  ASN ASN A . n 
A 1 49  PRO 49  30  30  PRO PRO A . n 
A 1 50  GLY 50  31  31  GLY GLY A . n 
A 1 51  LYS 51  32  32  LYS LYS A . n 
A 1 52  ALA 52  33  33  ALA ALA A . n 
A 1 53  ALA 53  34  34  ALA ALA A . n 
A 1 54  GLU 54  35  35  GLU GLU A . n 
A 1 55  VAL 55  36  36  VAL VAL A . n 
A 1 56  ALA 56  37  37  ALA ALA A . n 
A 1 57  VAL 57  38  38  VAL VAL A . n 
A 1 58  ARG 58  39  39  ARG ARG A . n 
A 1 59  ALA 59  40  40  ALA ALA A . n 
A 1 60  HIS 60  41  41  HIS HIS A . n 
A 1 61  CYS 61  42  42  CYS CYS A . n 
A 1 62  SER 62  43  43  SER SER A . n 
A 1 63  ILE 63  44  44  ILE ILE A . n 
A 1 64  LEU 64  45  45  LEU LEU A . n 
A 1 65  SER 65  46  46  SER SER A . n 
A 1 66  SER 66  47  47  SER SER A . n 
A 1 67  LEU 67  48  48  LEU LEU A . n 
A 1 68  ILE 68  49  49  ILE ILE A . n 
A 1 69  ARG 69  50  50  ARG ARG A . n 
A 1 70  GLY 70  51  51  GLY GLY A . n 
A 1 71  VAL 71  52  52  VAL VAL A . n 
A 1 72  GLY 72  53  53  GLY GLY A . n 
A 1 73  PHE 73  54  54  PHE PHE A . n 
A 1 74  ARG 74  55  55  ARG ARG A . n 
A 1 75  ILE 75  56  56  ILE ILE A . n 
A 1 76  SER 76  57  57  SER SER A . n 
A 1 77  ASP 77  58  58  ASP ASP A . n 
A 1 78  GLY 78  59  59  GLY GLY A . n 
A 1 79  GLY 79  60  60  GLY GLY A . n 
A 1 80  LEU 80  61  61  LEU LEU A . n 
A 1 81  SER 81  62  62  SER SER A . n 
A 1 82  CYS 82  63  63  CYS CYS A . n 
A 1 83  VAL 83  64  64  VAL VAL A . n 
A 1 84  MET 84  65  65  MET MET A . n 
A 1 85  GLY 85  66  66  GLY GLY A . n 
A 1 86  VAL 86  67  67  VAL VAL A . n 
A 1 87  SER 87  68  68  SER SER A . n 
A 1 88  GLU 88  69  69  GLU GLU A . n 
A 1 89  GLY 89  70  70  GLY GLY A . n 
A 1 90  GLY 90  71  71  GLY GLY A . n 
A 1 91  TRP 91  72  72  TRP TRP A . n 
A 1 92  GLU 92  73  73  GLU GLU A . n 
A 1 93  ARG 93  74  74  ARG ARG A . n 
A 1 94  LEU 94  75  75  LEU LEU A . n 
A 1 95  PHE 95  76  76  PHE PHE A . n 
A 1 96  GLY 96  77  77  GLY GLY A . n 
A 1 97  ASP 97  78  78  ASP ASP A . n 
A 1 98  THR 98  79  79  THR THR A . n 
A 1 99  LYS 99  80  80  LYS LYS A . n 
A 1 100 PRO 100 81  81  PRO PRO A . n 
A 1 101 GLU 101 82  82  GLU GLU A . n 
A 1 102 TYR 102 83  83  TYR TYR A . n 
A 1 103 LEU 103 84  84  LEU LEU A . n 
A 1 104 HIS 104 85  85  HIS HIS A . n 
A 1 105 VAL 105 86  86  VAL VAL A . n 
A 1 106 PHE 106 87  87  PHE PHE A . n 
A 1 107 ARG 107 88  88  ARG ARG A . n 
A 1 108 GLU 108 89  89  GLU GLU A . n 
A 1 109 ILE 109 90  90  ILE ILE A . n 
A 1 110 ASN 110 91  91  ASN ASN A . n 
A 1 111 GLY 111 92  92  GLY GLY A . n 
A 1 112 VAL 112 93  93  VAL VAL A . n 
A 1 113 HIS 113 94  94  HIS HIS A . n 
A 1 114 HIS 114 95  95  HIS HIS A . n 
A 1 115 ALA 115 96  96  ALA ALA A . n 
A 1 116 PRO 116 97  97  PRO PRO A . n 
A 1 117 SER 117 98  98  SER SER A . n 
A 1 118 THR 118 99  99  THR THR A . n 
A 1 119 PRO 119 100 100 PRO PRO A . n 
A 1 120 GLY 120 101 101 GLY GLY A . n 
A 1 121 ASP 121 102 102 ASP ASP A . n 
A 1 122 LEU 122 103 103 LEU LEU A . n 
A 1 123 LEU 123 104 104 LEU LEU A . n 
A 1 124 TYR 124 105 105 TYR TYR A . n 
A 1 125 HIS 125 106 106 HIS HIS A . n 
A 1 126 ILE 126 107 107 ILE ILE A . n 
A 1 127 ARG 127 108 108 ARG ARG A . n 
A 1 128 ALA 128 109 109 ALA ALA A . n 
A 1 129 ALA 129 110 110 ALA ALA A . n 
A 1 130 ARG 130 111 111 ARG ARG A . n 
A 1 131 MET 131 112 112 MET MET A . n 
A 1 132 ASP 132 113 113 ASP ASP A . n 
A 1 133 LEU 133 114 114 LEU LEU A . n 
A 1 134 CYS 134 115 115 CYS CYS A . n 
A 1 135 PHE 135 116 116 PHE PHE A . n 
A 1 136 GLU 136 117 117 GLU GLU A . n 
A 1 137 LEU 137 118 118 LEU LEU A . n 
A 1 138 ALA 138 119 119 ALA ALA A . n 
A 1 139 SER 139 120 120 SER SER A . n 
A 1 140 ARG 140 121 121 ARG ARG A . n 
A 1 141 ILE 141 122 122 ILE ILE A . n 
A 1 142 LEU 142 123 123 LEU LEU A . n 
A 1 143 SER 143 124 124 SER SER A . n 
A 1 144 ASP 144 125 125 ASP ASP A . n 
A 1 145 LEU 145 126 126 LEU LEU A . n 
A 1 146 GLY 146 127 127 GLY GLY A . n 
A 1 147 ASN 147 128 128 ASN ASN A . n 
A 1 148 SER 148 129 129 SER SER A . n 
A 1 149 VAL 149 130 130 VAL VAL A . n 
A 1 150 SER 150 131 131 SER SER A . n 
A 1 151 VAL 151 132 132 VAL VAL A . n 
A 1 152 VAL 152 133 133 VAL VAL A . n 
A 1 153 ASP 153 134 134 ASP ASP A . n 
A 1 154 SER 154 135 135 SER SER A . n 
A 1 155 VAL 155 136 136 VAL VAL A . n 
A 1 156 GLN 156 137 137 GLN GLN A . n 
A 1 157 GLY 157 138 138 GLY GLY A . n 
A 1 158 PHE 158 139 139 PHE PHE A . n 
A 1 159 ARG 159 140 140 ARG ARG A . n 
A 1 160 TYR 160 141 141 TYR TYR A . n 
A 1 161 PHE 161 142 142 PHE PHE A . n 
A 1 162 ASP 162 143 143 ASP ASP A . n 
A 1 163 ASP 163 144 144 ASP ASP A . n 
A 1 164 ARG 164 145 145 ARG ARG A . n 
A 1 165 ASP 165 146 146 ASP ASP A . n 
A 1 166 LEU 166 147 147 LEU LEU A . n 
A 1 167 LEU 167 148 148 LEU LEU A . n 
A 1 168 GLY 168 149 149 GLY GLY A . n 
A 1 169 PHE 169 150 150 PHE PHE A . n 
A 1 170 VAL 170 151 151 VAL VAL A . n 
A 1 171 ASP 171 152 152 ASP ASP A . n 
A 1 172 GLY 172 153 153 GLY GLY A . n 
A 1 173 THR 173 154 154 THR THR A . n 
A 1 174 GLU 174 155 155 GLU GLU A . n 
A 1 175 ASN 175 156 156 ASN ASN A . n 
A 1 176 PRO 176 157 157 PRO PRO A . n 
A 1 177 VAL 177 158 158 VAL VAL A . n 
A 1 178 ALA 178 159 159 ALA ALA A . n 
A 1 179 GLN 179 160 160 GLN GLN A . n 
A 1 180 ALA 180 161 161 ALA ALA A . n 
A 1 181 ALA 181 162 162 ALA ALA A . n 
A 1 182 VAL 182 163 163 VAL VAL A . n 
A 1 183 ASP 183 164 164 ASP ASP A . n 
A 1 184 ALA 184 165 165 ALA ALA A . n 
A 1 185 THR 185 166 166 THR THR A . n 
A 1 186 LEU 186 167 167 LEU LEU A . n 
A 1 187 ILE 187 168 168 ILE ILE A . n 
A 1 188 GLY 188 169 169 GLY GLY A . n 
A 1 189 ASP 189 170 170 ASP ASP A . n 
A 1 190 GLU 190 171 171 GLU GLU A . n 
A 1 191 ASP 191 172 172 ASP ASP A . n 
A 1 192 MET 192 173 173 MET MET A . n 
A 1 193 VAL 193 174 174 VAL VAL A . n 
A 1 194 PHE 194 175 175 PHE PHE A . n 
A 1 195 ALA 195 176 176 ALA ALA A . n 
A 1 196 GLY 196 177 177 GLY GLY A . n 
A 1 197 GLY 197 178 178 GLY GLY A . n 
A 1 198 SER 198 179 179 SER SER A . n 
A 1 199 TYR 199 180 180 TYR TYR A . n 
A 1 200 VAL 200 181 181 VAL VAL A . n 
A 1 201 ILE 201 182 182 ILE ILE A . n 
A 1 202 VAL 202 183 183 VAL VAL A . n 
A 1 203 GLN 203 184 184 GLN GLN A . n 
A 1 204 LYS 204 185 185 LYS LYS A . n 
A 1 205 TYR 205 186 186 TYR TYR A . n 
A 1 206 LEU 206 187 187 LEU LEU A . n 
A 1 207 HIS 207 188 188 HIS HIS A . n 
A 1 208 ASP 208 189 189 ASP ASP A . n 
A 1 209 LEU 209 190 190 LEU LEU A . n 
A 1 210 ASP 210 191 191 ASP ASP A . n 
A 1 211 LYS 211 192 192 LYS LYS A . n 
A 1 212 TRP 212 193 193 TRP TRP A . n 
A 1 213 ASN 213 194 194 ASN ASN A . n 
A 1 214 ALA 214 195 195 ALA ALA A . n 
A 1 215 ILE 215 196 196 ILE ILE A . n 
A 1 216 PRO 216 197 197 PRO PRO A . n 
A 1 217 VAL 217 198 198 VAL VAL A . n 
A 1 218 GLU 218 199 199 GLU GLU A . n 
A 1 219 GLN 219 200 200 GLN GLN A . n 
A 1 220 GLN 220 201 201 GLN GLN A . n 
A 1 221 GLU 221 202 202 GLU GLU A . n 
A 1 222 LYS 222 203 203 LYS LYS A . n 
A 1 223 ILE 223 204 204 ILE ILE A . n 
A 1 224 ILE 224 205 205 ILE ILE A . n 
A 1 225 GLY 225 206 206 GLY GLY A . n 
A 1 226 ARG 226 207 207 ARG ARG A . n 
A 1 227 GLU 227 208 208 GLU GLU A . n 
A 1 228 LYS 228 209 209 LYS LYS A . n 
A 1 229 LEU 229 210 210 LEU LEU A . n 
A 1 230 SER 230 211 211 SER SER A . n 
A 1 231 ASP 231 212 212 ASP ASP A . n 
A 1 232 ILE 232 213 213 ILE ILE A . n 
A 1 233 GLU 233 214 214 GLU GLU A . n 
A 1 234 LEU 234 215 215 LEU LEU A . n 
A 1 235 ARG 235 216 216 ARG ARG A . n 
A 1 236 ASP 236 217 217 ASP ASP A . n 
A 1 237 ALA 237 218 218 ALA ALA A . n 
A 1 238 ASP 238 219 219 ASP ASP A . n 
A 1 239 LYS 239 220 220 LYS LYS A . n 
A 1 240 PRO 240 221 221 PRO PRO A . n 
A 1 241 SER 241 222 222 SER SER A . n 
A 1 242 TYR 242 223 223 TYR TYR A . n 
A 1 243 ALA 243 224 224 ALA ALA A . n 
A 1 244 HIS 244 225 225 HIS HIS A . n 
A 1 245 ASN 245 226 226 ASN ASN A . n 
A 1 246 VAL 246 227 227 VAL VAL A . n 
A 1 247 LEU 247 228 228 LEU LEU A . n 
A 1 248 THR 248 229 229 THR THR A . n 
A 1 249 SER 249 230 230 SER SER A . n 
A 1 250 ILE 250 231 231 ILE ILE A . n 
A 1 251 GLU 251 232 232 GLU GLU A . n 
A 1 252 GLU 252 233 233 GLU GLU A . n 
A 1 253 ASP 253 234 234 ASP ASP A . n 
A 1 254 GLY 254 235 235 GLY GLY A . n 
A 1 255 GLU 255 236 236 GLU GLU A . n 
A 1 256 ASP 256 237 237 ASP ASP A . n 
A 1 257 VAL 257 238 238 VAL VAL A . n 
A 1 258 ASP 258 239 239 ASP ASP A . n 
A 1 259 ILE 259 240 240 ILE ILE A . n 
A 1 260 LEU 260 241 241 LEU LEU A . n 
A 1 261 ARG 261 242 242 ARG ARG A . n 
A 1 262 ASP 262 243 243 ASP ASP A . n 
A 1 263 ASN 263 244 244 ASN ASN A . n 
A 1 264 MET 264 245 245 MET MET A . n 
A 1 265 PRO 265 246 246 PRO PRO A . n 
A 1 266 PHE 266 247 247 PHE PHE A . n 
A 1 267 GLY 267 248 248 GLY GLY A . n 
A 1 268 ASP 268 249 249 ASP ASP A . n 
A 1 269 PRO 269 250 250 PRO PRO A . n 
A 1 270 GLY 270 251 251 GLY GLY A . n 
A 1 271 LYS 271 252 252 LYS LYS A . n 
A 1 272 GLY 272 253 253 GLY GLY A . n 
A 1 273 GLU 273 254 254 GLU GLU A . n 
A 1 274 PHE 274 255 255 PHE PHE A . n 
A 1 275 GLY 275 256 256 GLY GLY A . n 
A 1 276 THR 276 257 257 THR THR A . n 
A 1 277 TYR 277 258 258 TYR TYR A . n 
A 1 278 PHE 278 259 259 PHE PHE A . n 
A 1 279 ILE 279 260 260 ILE ILE A . n 
A 1 280 GLY 280 261 261 GLY GLY A . n 
A 1 281 TYR 281 262 262 TYR TYR A . n 
A 1 282 SER 282 263 263 SER SER A . n 
A 1 283 ARG 283 264 264 ARG ARG A . n 
A 1 284 LYS 284 265 265 LYS LYS A . n 
A 1 285 PRO 285 266 266 PRO PRO A . n 
A 1 286 GLU 286 267 267 GLU GLU A . n 
A 1 287 ARG 287 268 268 ARG ARG A . n 
A 1 288 ILE 288 269 269 ILE ILE A . n 
A 1 289 GLU 289 270 270 GLU GLU A . n 
A 1 290 ARG 290 271 271 ARG ARG A . n 
A 1 291 MET 291 272 272 MET MET A . n 
A 1 292 LEU 292 273 273 LEU LEU A . n 
A 1 293 GLU 293 274 274 GLU GLU A . n 
A 1 294 ASN 294 275 275 ASN ASN A . n 
A 1 295 MET 295 276 276 MET MET A . n 
A 1 296 PHE 296 277 277 PHE PHE A . n 
A 1 297 ILE 297 278 278 ILE ILE A . n 
A 1 298 GLY 298 279 279 GLY GLY A . n 
A 1 299 ASN 299 280 280 ASN ASN A . n 
A 1 300 PRO 300 281 281 PRO PRO A . n 
A 1 301 PRO 301 282 282 PRO PRO A . n 
A 1 302 GLY 302 283 283 GLY GLY A . n 
A 1 303 ASN 303 284 284 ASN ASN A . n 
A 1 304 TYR 304 285 285 TYR TYR A . n 
A 1 305 ASP 305 286 286 ASP ASP A . n 
A 1 306 ARG 306 287 287 ARG ARG A . n 
A 1 307 ILE 307 288 288 ILE ILE A . n 
A 1 308 LEU 308 289 289 LEU LEU A . n 
A 1 309 ASP 309 290 290 ASP ASP A . n 
A 1 310 VAL 310 291 291 VAL VAL A . n 
A 1 311 SER 311 292 292 SER SER A . n 
A 1 312 ARG 312 293 293 ARG ARG A . n 
A 1 313 ALA 313 294 294 ALA ALA A . n 
A 1 314 ILE 314 295 295 ILE ILE A . n 
A 1 315 THR 315 296 296 THR THR A . n 
A 1 316 GLY 316 297 297 GLY GLY A . n 
A 1 317 THR 317 298 298 THR THR A . n 
A 1 318 LEU 318 299 299 LEU LEU A . n 
A 1 319 PHE 319 300 300 PHE PHE A . n 
A 1 320 PHE 320 301 301 PHE PHE A . n 
A 1 321 VAL 321 302 302 VAL VAL A . n 
A 1 322 PRO 322 303 303 PRO PRO A . n 
A 1 323 THR 323 304 304 THR THR A . n 
A 1 324 THR 324 305 305 THR THR A . n 
A 1 325 SER 325 306 306 SER SER A . n 
A 1 326 PHE 326 307 307 PHE PHE A . n 
A 1 327 LEU 327 308 308 LEU LEU A . n 
A 1 328 ASP 328 309 309 ASP ASP A . n 
A 1 329 SER 329 310 310 SER SER A . n 
A 1 330 ILE 330 311 311 ILE ILE A . n 
A 1 331 GLU 331 312 312 GLU GLU A . n 
A 1 332 PRO 332 313 313 PRO PRO A . n 
A 1 333 GLN 333 314 ?   ?   ?   A . n 
A 1 334 SER 334 315 ?   ?   ?   A . n 
A 1 335 ALA 335 316 ?   ?   ?   A . n 
A 1 336 PRO 336 317 ?   ?   ?   A . n 
A 1 337 GLY 337 318 ?   ?   ?   A . n 
A 1 338 GLN 338 319 ?   ?   ?   A . n 
A 1 339 GLN 339 320 ?   ?   ?   A . n 
A 1 340 GLY 340 321 ?   ?   ?   A . n 
A 1 341 ASP 341 322 ?   ?   ?   A . n 
A 1 342 ASP 342 323 ?   ?   ?   A . n 
A 1 343 VAL 343 324 ?   ?   ?   A . n 
A 1 344 ILE 344 325 ?   ?   ?   A . n 
A 1 345 ASN 345 326 ?   ?   ?   A . n 
A 1 346 THR 346 327 ?   ?   ?   A . n 
A 1 347 LEU 347 328 ?   ?   ?   A . n 
A 1 348 ARG 348 329 ?   ?   ?   A . n 
A 1 349 SER 349 330 ?   ?   ?   A . n 
A 1 350 THR 350 331 ?   ?   ?   A . n 
A 1 351 ALA 351 332 ?   ?   ?   A . n 
A 1 352 ILE 352 333 ?   ?   ?   A . n 
A 1 353 LYS 353 334 ?   ?   ?   A . n 
A 1 354 GLY 354 335 ?   ?   ?   A . n 
A 1 355 ASP 355 336 ?   ?   ?   A . n 
A 1 356 ILE 356 337 ?   ?   ?   A . n 
A 1 357 MET 357 338 ?   ?   ?   A . n 
A 1 358 PRO 358 339 ?   ?   ?   A . n 
A 1 359 GLY 359 340 ?   ?   ?   A . n 
A 1 360 SER 360 341 ?   ?   ?   A . n 
A 1 361 LEU 361 342 ?   ?   ?   A . n 
A 1 362 ASN 362 343 ?   ?   ?   A . n 
A 1 363 ILE 363 344 ?   ?   ?   A . n 
A 1 364 GLY 364 345 ?   ?   ?   A . n 
A 1 365 SER 365 346 ?   ?   ?   A . n 
A 1 366 LEU 366 347 ?   ?   ?   A . n 
A 1 367 LYS 367 348 ?   ?   ?   A . n 
A 1 368 LYS 368 349 ?   ?   ?   A . n 
A 1 369 GLU 369 350 ?   ?   ?   A . n 
A 1 370 VAL 370 351 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        HEM 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   HEM 
_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        ? 
# 
_pdbx_nonpoly_scheme.asym_id         B 
_pdbx_nonpoly_scheme.entity_id       2 
_pdbx_nonpoly_scheme.mon_id          HEM 
_pdbx_nonpoly_scheme.ndb_seq_num     1 
_pdbx_nonpoly_scheme.pdb_seq_num     401 
_pdbx_nonpoly_scheme.auth_seq_num    1 
_pdbx_nonpoly_scheme.pdb_mon_id      HEM 
_pdbx_nonpoly_scheme.auth_mon_id     HEM 
_pdbx_nonpoly_scheme.pdb_strand_id   A 
_pdbx_nonpoly_scheme.pdb_ins_code    . 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9E4R 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_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                         9E4R 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_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                   9E4R 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9E4R 
_struct.title                        'Escherichia coli encapsulin-associated DyP peroxidase' 
_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        9E4R 
_struct_keywords.text            'Dye-decolorizing peroxidase, peroxidase, DyP, encapsulin, 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 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A5C9AJY8_ECOLX 
_struct_ref.pdbx_db_accession          A0A5C9AJY8 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;GCPFSQSVSQPVDERLTRAAIFLVVTINPGKAAEVAVRAHCSILSSLIRGVGFRISDGGLSCVMGVSEGGWERLFGDTKP
EYLHVFREINGVHHAPSTPGDLLYHIRAARMDLCFELASRILSDLGNSVSVVDSVQGFRYFDDRDLLGFVDGTENPVAQA
AVDATLIGDEDMVFAGGSYVIVQKYLHDLDKWNAIPVEQQEKIIGREKLSDIELRDADKPSYAHNVLTSIEEDGEDVDIL
RDNMPFGDPGKGEFGTYFIGYSRKPERIERMLENMFIGNPPGNYDRILDVSRAITGTLFFVPTTSFLDSIEPQSAPGQQG
DDVINTLRSTAIKGDIMPGSLNIGSLKKEV
;
_struct_ref.pdbx_align_begin           2 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9E4R 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 21 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 370 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A5C9AJY8 
_struct_ref_seq.db_align_beg                  2 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  351 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       2 
_struct_ref_seq.pdbx_auth_seq_align_end       351 
# 
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 9E4R MET A 1  ? UNP A0A5C9AJY8 ? ? 'initiating methionine' -18 1  
1 9E4R HIS A 2  ? UNP A0A5C9AJY8 ? ? 'expression tag'        -17 2  
1 9E4R HIS A 3  ? UNP A0A5C9AJY8 ? ? 'expression tag'        -16 3  
1 9E4R HIS A 4  ? UNP A0A5C9AJY8 ? ? 'expression tag'        -15 4  
1 9E4R HIS A 5  ? UNP A0A5C9AJY8 ? ? 'expression tag'        -14 5  
1 9E4R HIS A 6  ? UNP A0A5C9AJY8 ? ? 'expression tag'        -13 6  
1 9E4R HIS A 7  ? UNP A0A5C9AJY8 ? ? 'expression tag'        -12 7  
1 9E4R GLY A 8  ? UNP A0A5C9AJY8 ? ? 'expression tag'        -11 8  
1 9E4R GLY A 9  ? UNP A0A5C9AJY8 ? ? 'expression tag'        -10 9  
1 9E4R SER A 10 ? UNP A0A5C9AJY8 ? ? 'expression tag'        -9  10 
1 9E4R GLU A 11 ? UNP A0A5C9AJY8 ? ? 'expression tag'        -8  11 
1 9E4R ASN A 12 ? UNP A0A5C9AJY8 ? ? 'expression tag'        -7  12 
1 9E4R LEU A 13 ? UNP A0A5C9AJY8 ? ? 'expression tag'        -6  13 
1 9E4R TYR A 14 ? UNP A0A5C9AJY8 ? ? 'expression tag'        -5  14 
1 9E4R PHE A 15 ? UNP A0A5C9AJY8 ? ? 'expression tag'        -4  15 
1 9E4R GLN A 16 ? UNP A0A5C9AJY8 ? ? 'expression tag'        -3  16 
1 9E4R SER A 17 ? UNP A0A5C9AJY8 ? ? 'expression tag'        -2  17 
1 9E4R GLY A 18 ? UNP A0A5C9AJY8 ? ? 'expression tag'        -1  18 
1 9E4R GLY A 19 ? UNP A0A5C9AJY8 ? ? 'expression tag'        0   19 
1 9E4R SER A 20 ? UNP A0A5C9AJY8 ? ? 'expression tag'        1   20 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 'complete point assembly'                ? hexameric 6 
2 'point asymmetric unit'                  ? monomeric 1 
3 'point asymmetric unit, std point frame' ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 '(1-6)' A,B 
2 1       A,B 
3 P       A,B 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
P 'transform to point frame' ?     ?     0.00009159  1.00000000  0.00002966  -116.49597 0.99999999  -0.00009159 0.00005910  
-116.48014 0.00005910  0.00002966  -1.00000000 116.46996 
1 'identity operation'       1_555 x,y,z 1.00000000  0.00000000  0.00000000  0.00000    0.00000000  1.00000000  0.00000000  
0.00000    0.00000000  0.00000000  1.00000000  0.00000   
2 'point symmetry operation' ?     ?     -0.49999999 0.86602541  -0.00006297 73.85698   -0.86602539 -0.50000000 -0.00009567 
275.61195  -0.00011434 0.00000669  0.99999999  0.01254   
3 'point symmetry operation' ?     ?     -0.50000000 -0.86602541 -0.00011434 275.61544  0.86602540  -0.50000000 0.00000670  
73.84395   -0.00006296 -0.00009567 0.99999999  0.01848   
4 'point symmetry operation' ?     ?     -0.99999998 0.00018318  0.00000000  232.94651  0.00018318  0.99999998  0.00005932  
-0.02824   0.00000000  0.00005933  -1.00000000 232.95369 
5 'point symmetry operation' ?     ?     0.49984135  -0.86611699 0.00006296  159.14002  -0.86611697 -0.49984135 -0.00003636 
275.59723  0.00006295  -0.00003635 -1.00000000 232.95750 
6 'point symmetry operation' ?     ?     0.50015862  0.86593380  0.00011434  -42.65540  0.86593379  -0.50015863 0.00006600  
73.86619   0.00011434  0.00006600  -0.99999999 232.93959 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 29  ? ARG A 35  ? SER A 10  ARG A 16  1 ? 7  
HELX_P HELX_P2  AA2 GLY A 50  ? ARG A 74  ? GLY A 31  ARG A 55  1 ? 25 
HELX_P HELX_P3  AA3 SER A 87  ? PHE A 95  ? SER A 68  PHE A 76  1 ? 9  
HELX_P HELX_P4  AA4 ARG A 130 ? GLY A 146 ? ARG A 111 GLY A 127 1 ? 17 
HELX_P HELX_P5  AA5 ALA A 178 ? LEU A 186 ? ALA A 159 LEU A 167 1 ? 9  
HELX_P HELX_P6  AA6 ASP A 191 ? ALA A 195 ? ASP A 172 ALA A 176 5 ? 5  
HELX_P HELX_P7  AA7 ASP A 208 ? ILE A 215 ? ASP A 189 ILE A 196 1 ? 8  
HELX_P HELX_P8  AA8 PRO A 216 ? GLY A 225 ? PRO A 197 GLY A 206 1 ? 10 
HELX_P HELX_P9  AA9 ALA A 243 ? THR A 248 ? ALA A 224 THR A 229 1 ? 6  
HELX_P HELX_P10 AB1 LYS A 284 ? ILE A 297 ? LYS A 265 ILE A 278 1 ? 14 
HELX_P HELX_P11 AB2 ASP A 305 ? ASP A 309 ? ASP A 286 ASP A 290 5 ? 5  
HELX_P HELX_P12 AB3 THR A 323 ? SER A 329 ? THR A 304 SER A 310 1 ? 7  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            metalc1 
_struct_conn.conn_type_id                  metalc 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           HIS 
_struct_conn.ptnr1_label_seq_id            244 
_struct_conn.ptnr1_label_atom_id           NE2 
_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                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           HEM 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           FE 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            HIS 
_struct_conn.ptnr1_auth_seq_id             225 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            HEM 
_struct_conn.ptnr2_auth_seq_id             401 
_struct_conn.ptnr2_symmetry                1_555 
_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               2.130 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_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 244 ? A HIS 225 ? 1_555 FE ? B HEM . ? A HEM 401 ? 1_555 NA ? B HEM . ? A HEM 401 ? 1_555 79.2  ? 
2  NE2 ? A HIS 244 ? A HIS 225 ? 1_555 FE ? B HEM . ? A HEM 401 ? 1_555 NB ? B HEM . ? A HEM 401 ? 1_555 84.1  ? 
3  NA  ? B HEM .   ? A HEM 401 ? 1_555 FE ? B HEM . ? A HEM 401 ? 1_555 NB ? B HEM . ? A HEM 401 ? 1_555 89.8  ? 
4  NE2 ? A HIS 244 ? A HIS 225 ? 1_555 FE ? B HEM . ? A HEM 401 ? 1_555 NC ? B HEM . ? A HEM 401 ? 1_555 103.2 ? 
5  NA  ? B HEM .   ? A HEM 401 ? 1_555 FE ? B HEM . ? A HEM 401 ? 1_555 NC ? B HEM . ? A HEM 401 ? 1_555 177.6 ? 
6  NB  ? B HEM .   ? A HEM 401 ? 1_555 FE ? B HEM . ? A HEM 401 ? 1_555 NC ? B HEM . ? A HEM 401 ? 1_555 90.1  ? 
7  NE2 ? A HIS 244 ? A HIS 225 ? 1_555 FE ? B HEM . ? A HEM 401 ? 1_555 ND ? B HEM . ? A HEM 401 ? 1_555 95.6  ? 
8  NA  ? B HEM .   ? A HEM 401 ? 1_555 FE ? B HEM . ? A HEM 401 ? 1_555 ND ? B HEM . ? A HEM 401 ? 1_555 90.3  ? 
9  NB  ? B HEM .   ? A HEM 401 ? 1_555 FE ? B HEM . ? A HEM 401 ? 1_555 ND ? B HEM . ? A HEM 401 ? 1_555 179.6 ? 
10 NC  ? B HEM .   ? A HEM 401 ? 1_555 FE ? B HEM . ? A HEM 401 ? 1_555 ND ? B HEM . ? A HEM 401 ? 1_555 89.9  ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          ASN 
_struct_mon_prot_cis.label_seq_id           299 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           ASN 
_struct_mon_prot_cis.auth_seq_id            280 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    300 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     281 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -1.28 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 2 ? 
AA3 ? 3 ? 
AA4 ? 4 ? 
AA5 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 SER A 81  ? VAL A 86  ? SER A 62  VAL A 67  
AA1 2 LEU A 122 ? ALA A 128 ? LEU A 103 ALA A 109 
AA1 3 ALA A 39  ? ILE A 47  ? ALA A 20  ILE A 28  
AA1 4 VAL A 149 ? PHE A 158 ? VAL A 130 PHE A 139 
AA2 1 ILE A 109 ? ASN A 110 ? ILE A 90  ASN A 91  
AA2 2 HIS A 114 ? ALA A 115 ? HIS A 95  ALA A 96  
AA3 1 LEU A 260 ? ARG A 261 ? LEU A 241 ARG A 242 
AA3 2 GLU A 273 ? SER A 282 ? GLU A 254 SER A 263 
AA3 3 MET A 264 ? ASP A 268 ? MET A 245 ASP A 249 
AA4 1 LEU A 260 ? ARG A 261 ? LEU A 241 ARG A 242 
AA4 2 GLU A 273 ? SER A 282 ? GLU A 254 SER A 263 
AA4 3 SER A 198 ? HIS A 207 ? SER A 179 HIS A 188 
AA4 4 SER A 311 ? VAL A 321 ? SER A 292 VAL A 302 
AA5 1 GLU A 251 ? GLU A 252 ? GLU A 232 GLU A 233 
AA5 2 GLU A 255 ? ASP A 256 ? GLU A 236 ASP A 237 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N SER A 81  ? N SER A 62  O ARG A 127 ? O ARG A 108 
AA1 2 3 O LEU A 122 ? O LEU A 103 N VAL A 45  ? N VAL A 26  
AA1 3 4 N THR A 46  ? N THR A 27  O SER A 150 ? O SER A 131 
AA2 1 2 N ILE A 109 ? N ILE A 90  O ALA A 115 ? O ALA A 96  
AA3 1 2 N LEU A 260 ? N LEU A 241 O TYR A 281 ? O TYR A 262 
AA3 2 3 O TYR A 277 ? O TYR A 258 N MET A 264 ? N MET A 245 
AA4 1 2 N LEU A 260 ? N LEU A 241 O TYR A 281 ? O TYR A 262 
AA4 2 3 O SER A 282 ? O SER A 263 N TYR A 199 ? N TYR A 180 
AA4 3 4 N VAL A 200 ? N VAL A 181 O PHE A 319 ? O PHE A 300 
AA5 1 2 N GLU A 252 ? N GLU A 233 O GLU A 255 ? O GLU A 236 
# 
_pdbx_entry_details.entry_id                   9E4R 
_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 ASP A 58  ? ? 38.90 32.05   
2 1 PHE A 142 ? ? 56.39 -132.06 
3 1 ALA A 159 ? ? 63.06 -119.69 
# 
_pdbx_point_symmetry.entry_id             9E4R 
_pdbx_point_symmetry.Schoenflies_symbol   D 
_pdbx_point_symmetry.circular_symmetry    3 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9E4R 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   'cross-correlation coefficient' 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   105.9 
_em_3d_fitting.ref_space         REAL 
_em_3d_fitting.ref_protocol      'FLEXIBLE FIT' 
# 
_em_3d_fitting_list.id                            1 
_em_3d_fitting_list.3d_fitting_id                 1 
_em_3d_fitting_list.pdb_entry_id                  . 
_em_3d_fitting_list.pdb_chain_id                  . 
_em_3d_fitting_list.pdb_chain_residue_range       . 
_em_3d_fitting_list.details                       ? 
_em_3d_fitting_list.chain_id                      ? 
_em_3d_fitting_list.chain_residue_range           ? 
_em_3d_fitting_list.source_name                   AlphaFold 
_em_3d_fitting_list.type                          'in silico model' 
_em_3d_fitting_list.accession_code                A0A747AN60 
_em_3d_fitting_list.initial_refinement_model_id   1 
# 
_em_3d_reconstruction.entry_id                    9E4R 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     'Local refinement with D3 symmetry and force re-do GS-split applied.' 
_em_3d_reconstruction.resolution                  3.31 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               10490 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       'Sample was prepared in 20 mM Tris pH 7.5, 150 mM NaCl.' 
_em_buffer.pH            7.5 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'Escherichia coli KTE40 encapsulin-associated DyP peroxidase' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
loop_
_em_image_scans.entry_id 
_em_image_scans.id 
_em_image_scans.number_digital_images 
_em_image_scans.details 
_em_image_scans.scanner_model 
_em_image_scans.sampling_size 
_em_image_scans.od_range 
_em_image_scans.quant_bit_size 
_em_image_scans.citation_id 
_em_image_scans.dimension_height 
_em_image_scans.dimension_width 
_em_image_scans.frames_per_image 
_em_image_scans.image_recording_id 
_em_image_scans.used_frames_per_image 
9E4R 1 ? ? ? ? ? ? ? 3838 3710 30 1 ? 
9E4R 2 ? ? ? ? ? ? ? 3838 3710 20 2 ? 
# 
loop_
_em_imaging.entry_id 
_em_imaging.id 
_em_imaging.astigmatism 
_em_imaging.electron_beam_tilt_params 
_em_imaging.residual_tilt 
_em_imaging.microscope_model 
_em_imaging.specimen_holder_type 
_em_imaging.specimen_holder_model 
_em_imaging.details 
_em_imaging.date 
_em_imaging.accelerating_voltage 
_em_imaging.illumination_mode 
_em_imaging.mode 
_em_imaging.nominal_cs 
_em_imaging.nominal_defocus_min 
_em_imaging.nominal_defocus_max 
_em_imaging.calibrated_defocus_min 
_em_imaging.calibrated_defocus_max 
_em_imaging.tilt_angle_min 
_em_imaging.tilt_angle_max 
_em_imaging.nominal_magnification 
_em_imaging.calibrated_magnification 
_em_imaging.electron_source 
_em_imaging.citation_id 
_em_imaging.temperature 
_em_imaging.detector_distance 
_em_imaging.recording_temperature_minimum 
_em_imaging.recording_temperature_maximum 
_em_imaging.alignment_procedure 
_em_imaging.c2_aperture_diameter 
_em_imaging.specimen_id 
_em_imaging.cryogen 
9E4R 1 ? ? ? 'FEI TALOS ARCTICA' ? ? ? ? 200 'FLOOD BEAM' 'BRIGHT FIELD' 2.7 1000 1800 ? ? ? ? 45000 ? 'FIELD EMISSION GUN' ? ? ? 
? ? ? ? 1 NITROGEN 
9E4R 2 ? ? ? 'TFS GLACIOS'       ? ? ? ? 200 'FLOOD BEAM' 'BRIGHT FIELD' 2.7 1000 1800 ? ? ? ? 45000 ? 'FIELD EMISSION GUN' ? ? ? 
? ? ? ? 1 ?        
# 
_em_sample_support.id               1 
_em_sample_support.film_material    ? 
_em_sample_support.method           ? 
_em_sample_support.grid_material    COPPER 
_em_sample_support.grid_mesh_size   200 
_em_sample_support.grid_type        'Quantifoil R1.2/1.3' 
_em_sample_support.details          'Grids were glow discharged for 60 seconds at 5 mA in vacuum.' 
_em_sample_support.specimen_id      1 
_em_sample_support.citation_id      ? 
# 
_em_vitrification.entry_id              9E4R 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              100 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   295 
_em_vitrification.instrument            'FEI VITROBOT MARK IV' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               
'Grids were frozen with the following parameters: blot force 20, blot time 4 seconds, humidty 100 percent, 22 degrees C.' 
# 
_em_experiment.entry_id                9E4R 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
_em_single_particle_entity.entry_id              9E4R 
_em_single_particle_entity.id                    1 
_em_single_particle_entity.image_processing_id   1 
_em_single_particle_entity.point_symmetry        D3 
# 
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 -18 ? A MET 1   
2  1 Y 1 A HIS -17 ? A HIS 2   
3  1 Y 1 A HIS -16 ? A HIS 3   
4  1 Y 1 A HIS -15 ? A HIS 4   
5  1 Y 1 A HIS -14 ? A HIS 5   
6  1 Y 1 A HIS -13 ? A HIS 6   
7  1 Y 1 A HIS -12 ? A HIS 7   
8  1 Y 1 A GLY -11 ? A GLY 8   
9  1 Y 1 A GLY -10 ? A GLY 9   
10 1 Y 1 A SER -9  ? A SER 10  
11 1 Y 1 A GLU -8  ? A GLU 11  
12 1 Y 1 A ASN -7  ? A ASN 12  
13 1 Y 1 A LEU -6  ? A LEU 13  
14 1 Y 1 A TYR -5  ? A TYR 14  
15 1 Y 1 A PHE -4  ? A PHE 15  
16 1 Y 1 A GLN -3  ? A GLN 16  
17 1 Y 1 A SER -2  ? A SER 17  
18 1 Y 1 A GLY -1  ? A GLY 18  
19 1 Y 1 A GLY 0   ? A GLY 19  
20 1 Y 1 A SER 1   ? A SER 20  
21 1 Y 1 A GLY 2   ? A GLY 21  
22 1 Y 1 A GLN 314 ? A GLN 333 
23 1 Y 1 A SER 315 ? A SER 334 
24 1 Y 1 A ALA 316 ? A ALA 335 
25 1 Y 1 A PRO 317 ? A PRO 336 
26 1 Y 1 A GLY 318 ? A GLY 337 
27 1 Y 1 A GLN 319 ? A GLN 338 
28 1 Y 1 A GLN 320 ? A GLN 339 
29 1 Y 1 A GLY 321 ? A GLY 340 
30 1 Y 1 A ASP 322 ? A ASP 341 
31 1 Y 1 A ASP 323 ? A ASP 342 
32 1 Y 1 A VAL 324 ? A VAL 343 
33 1 Y 1 A ILE 325 ? A ILE 344 
34 1 Y 1 A ASN 326 ? A ASN 345 
35 1 Y 1 A THR 327 ? A THR 346 
36 1 Y 1 A LEU 328 ? A LEU 347 
37 1 Y 1 A ARG 329 ? A ARG 348 
38 1 Y 1 A SER 330 ? A SER 349 
39 1 Y 1 A THR 331 ? A THR 350 
40 1 Y 1 A ALA 332 ? A ALA 351 
41 1 Y 1 A ILE 333 ? A ILE 352 
42 1 Y 1 A LYS 334 ? A LYS 353 
43 1 Y 1 A GLY 335 ? A GLY 354 
44 1 Y 1 A ASP 336 ? A ASP 355 
45 1 Y 1 A ILE 337 ? A ILE 356 
46 1 Y 1 A MET 338 ? A MET 357 
47 1 Y 1 A PRO 339 ? A PRO 358 
48 1 Y 1 A GLY 340 ? A GLY 359 
49 1 Y 1 A SER 341 ? A SER 360 
50 1 Y 1 A LEU 342 ? A LEU 361 
51 1 Y 1 A ASN 343 ? A ASN 362 
52 1 Y 1 A ILE 344 ? A ILE 363 
53 1 Y 1 A GLY 345 ? A GLY 364 
54 1 Y 1 A SER 346 ? A SER 365 
55 1 Y 1 A LEU 347 ? A LEU 366 
56 1 Y 1 A LYS 348 ? A LYS 367 
57 1 Y 1 A LYS 349 ? A LYS 368 
58 1 Y 1 A GLU 350 ? A GLU 369 
59 1 Y 1 A VAL 351 ? A VAL 370 
# 
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 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
HEM CHA  C  N N 137 
HEM CHB  C  N N 138 
HEM CHC  C  N N 139 
HEM CHD  C  N N 140 
HEM C1A  C  Y N 141 
HEM C2A  C  Y N 142 
HEM C3A  C  Y N 143 
HEM C4A  C  Y N 144 
HEM CMA  C  N N 145 
HEM CAA  C  N N 146 
HEM CBA  C  N N 147 
HEM CGA  C  N N 148 
HEM O1A  O  N N 149 
HEM O2A  O  N N 150 
HEM C1B  C  N N 151 
HEM C2B  C  N N 152 
HEM C3B  C  N N 153 
HEM C4B  C  N N 154 
HEM CMB  C  N N 155 
HEM CAB  C  N N 156 
HEM CBB  C  N N 157 
HEM C1C  C  Y N 158 
HEM C2C  C  Y N 159 
HEM C3C  C  Y N 160 
HEM C4C  C  Y N 161 
HEM CMC  C  N N 162 
HEM CAC  C  N N 163 
HEM CBC  C  N N 164 
HEM C1D  C  N N 165 
HEM C2D  C  N N 166 
HEM C3D  C  N N 167 
HEM C4D  C  N N 168 
HEM CMD  C  N N 169 
HEM CAD  C  N N 170 
HEM CBD  C  N N 171 
HEM CGD  C  N N 172 
HEM O1D  O  N N 173 
HEM O2D  O  N N 174 
HEM NA   N  Y N 175 
HEM NB   N  N N 176 
HEM NC   N  Y N 177 
HEM ND   N  N N 178 
HEM FE   FE N N 179 
HEM HHB  H  N N 180 
HEM HHC  H  N N 181 
HEM HHD  H  N N 182 
HEM HMA  H  N N 183 
HEM HMAA H  N N 184 
HEM HMAB H  N N 185 
HEM HAA  H  N N 186 
HEM HAAA H  N N 187 
HEM HBA  H  N N 188 
HEM HBAA H  N N 189 
HEM HMB  H  N N 190 
HEM HMBA H  N N 191 
HEM HMBB H  N N 192 
HEM HAB  H  N N 193 
HEM HBB  H  N N 194 
HEM HBBA H  N N 195 
HEM HMC  H  N N 196 
HEM HMCA H  N N 197 
HEM HMCB H  N N 198 
HEM HAC  H  N N 199 
HEM HBC  H  N N 200 
HEM HBCA H  N N 201 
HEM HMD  H  N N 202 
HEM HMDA H  N N 203 
HEM HMDB H  N N 204 
HEM HAD  H  N N 205 
HEM HADA H  N N 206 
HEM HBD  H  N N 207 
HEM HBDA H  N N 208 
HEM H2A  H  N N 209 
HEM H2D  H  N N 210 
HEM HHA  H  N N 211 
HIS N    N  N N 212 
HIS CA   C  N S 213 
HIS C    C  N N 214 
HIS O    O  N N 215 
HIS CB   C  N N 216 
HIS CG   C  Y N 217 
HIS ND1  N  Y N 218 
HIS CD2  C  Y N 219 
HIS CE1  C  Y N 220 
HIS NE2  N  Y N 221 
HIS OXT  O  N N 222 
HIS H    H  N N 223 
HIS H2   H  N N 224 
HIS HA   H  N N 225 
HIS HB2  H  N N 226 
HIS HB3  H  N N 227 
HIS HD1  H  N N 228 
HIS HD2  H  N N 229 
HIS HE1  H  N N 230 
HIS HE2  H  N N 231 
HIS HXT  H  N N 232 
ILE N    N  N N 233 
ILE CA   C  N S 234 
ILE C    C  N N 235 
ILE O    O  N N 236 
ILE CB   C  N S 237 
ILE CG1  C  N N 238 
ILE CG2  C  N N 239 
ILE CD1  C  N N 240 
ILE OXT  O  N N 241 
ILE H    H  N N 242 
ILE H2   H  N N 243 
ILE HA   H  N N 244 
ILE HB   H  N N 245 
ILE HG12 H  N N 246 
ILE HG13 H  N N 247 
ILE HG21 H  N N 248 
ILE HG22 H  N N 249 
ILE HG23 H  N N 250 
ILE HD11 H  N N 251 
ILE HD12 H  N N 252 
ILE HD13 H  N N 253 
ILE HXT  H  N N 254 
LEU N    N  N N 255 
LEU CA   C  N S 256 
LEU C    C  N N 257 
LEU O    O  N N 258 
LEU CB   C  N N 259 
LEU CG   C  N N 260 
LEU CD1  C  N N 261 
LEU CD2  C  N N 262 
LEU OXT  O  N N 263 
LEU H    H  N N 264 
LEU H2   H  N N 265 
LEU HA   H  N N 266 
LEU HB2  H  N N 267 
LEU HB3  H  N N 268 
LEU HG   H  N N 269 
LEU HD11 H  N N 270 
LEU HD12 H  N N 271 
LEU HD13 H  N N 272 
LEU HD21 H  N N 273 
LEU HD22 H  N N 274 
LEU HD23 H  N N 275 
LEU HXT  H  N N 276 
LYS N    N  N N 277 
LYS CA   C  N S 278 
LYS C    C  N N 279 
LYS O    O  N N 280 
LYS CB   C  N N 281 
LYS CG   C  N N 282 
LYS CD   C  N N 283 
LYS CE   C  N N 284 
LYS NZ   N  N N 285 
LYS OXT  O  N N 286 
LYS H    H  N N 287 
LYS H2   H  N N 288 
LYS HA   H  N N 289 
LYS HB2  H  N N 290 
LYS HB3  H  N N 291 
LYS HG2  H  N N 292 
LYS HG3  H  N N 293 
LYS HD2  H  N N 294 
LYS HD3  H  N N 295 
LYS HE2  H  N N 296 
LYS HE3  H  N N 297 
LYS HZ1  H  N N 298 
LYS HZ2  H  N N 299 
LYS HZ3  H  N N 300 
LYS HXT  H  N N 301 
MET N    N  N N 302 
MET CA   C  N S 303 
MET C    C  N N 304 
MET O    O  N N 305 
MET CB   C  N N 306 
MET CG   C  N N 307 
MET SD   S  N N 308 
MET CE   C  N N 309 
MET OXT  O  N N 310 
MET H    H  N N 311 
MET H2   H  N N 312 
MET HA   H  N N 313 
MET HB2  H  N N 314 
MET HB3  H  N N 315 
MET HG2  H  N N 316 
MET HG3  H  N N 317 
MET HE1  H  N N 318 
MET HE2  H  N N 319 
MET HE3  H  N N 320 
MET HXT  H  N N 321 
PHE N    N  N N 322 
PHE CA   C  N S 323 
PHE C    C  N N 324 
PHE O    O  N N 325 
PHE CB   C  N N 326 
PHE CG   C  Y N 327 
PHE CD1  C  Y N 328 
PHE CD2  C  Y N 329 
PHE CE1  C  Y N 330 
PHE CE2  C  Y N 331 
PHE CZ   C  Y N 332 
PHE OXT  O  N N 333 
PHE H    H  N N 334 
PHE H2   H  N N 335 
PHE HA   H  N N 336 
PHE HB2  H  N N 337 
PHE HB3  H  N N 338 
PHE HD1  H  N N 339 
PHE HD2  H  N N 340 
PHE HE1  H  N N 341 
PHE HE2  H  N N 342 
PHE HZ   H  N N 343 
PHE HXT  H  N N 344 
PRO N    N  N N 345 
PRO CA   C  N S 346 
PRO C    C  N N 347 
PRO O    O  N N 348 
PRO CB   C  N N 349 
PRO CG   C  N N 350 
PRO CD   C  N N 351 
PRO OXT  O  N N 352 
PRO H    H  N N 353 
PRO HA   H  N N 354 
PRO HB2  H  N N 355 
PRO HB3  H  N N 356 
PRO HG2  H  N N 357 
PRO HG3  H  N N 358 
PRO HD2  H  N N 359 
PRO HD3  H  N N 360 
PRO HXT  H  N N 361 
SER N    N  N N 362 
SER CA   C  N S 363 
SER C    C  N N 364 
SER O    O  N N 365 
SER CB   C  N N 366 
SER OG   O  N N 367 
SER OXT  O  N N 368 
SER H    H  N N 369 
SER H2   H  N N 370 
SER HA   H  N N 371 
SER HB2  H  N N 372 
SER HB3  H  N N 373 
SER HG   H  N N 374 
SER HXT  H  N N 375 
THR N    N  N N 376 
THR CA   C  N S 377 
THR C    C  N N 378 
THR O    O  N N 379 
THR CB   C  N R 380 
THR OG1  O  N N 381 
THR CG2  C  N N 382 
THR OXT  O  N N 383 
THR H    H  N N 384 
THR H2   H  N N 385 
THR HA   H  N N 386 
THR HB   H  N N 387 
THR HG1  H  N N 388 
THR HG21 H  N N 389 
THR HG22 H  N N 390 
THR HG23 H  N N 391 
THR HXT  H  N N 392 
TRP N    N  N N 393 
TRP CA   C  N S 394 
TRP C    C  N N 395 
TRP O    O  N N 396 
TRP CB   C  N N 397 
TRP CG   C  Y N 398 
TRP CD1  C  Y N 399 
TRP CD2  C  Y N 400 
TRP NE1  N  Y N 401 
TRP CE2  C  Y N 402 
TRP CE3  C  Y N 403 
TRP CZ2  C  Y N 404 
TRP CZ3  C  Y N 405 
TRP CH2  C  Y N 406 
TRP OXT  O  N N 407 
TRP H    H  N N 408 
TRP H2   H  N N 409 
TRP HA   H  N N 410 
TRP HB2  H  N N 411 
TRP HB3  H  N N 412 
TRP HD1  H  N N 413 
TRP HE1  H  N N 414 
TRP HE3  H  N N 415 
TRP HZ2  H  N N 416 
TRP HZ3  H  N N 417 
TRP HH2  H  N N 418 
TRP HXT  H  N N 419 
TYR N    N  N N 420 
TYR CA   C  N S 421 
TYR C    C  N N 422 
TYR O    O  N N 423 
TYR CB   C  N N 424 
TYR CG   C  Y N 425 
TYR CD1  C  Y N 426 
TYR CD2  C  Y N 427 
TYR CE1  C  Y N 428 
TYR CE2  C  Y N 429 
TYR CZ   C  Y N 430 
TYR OH   O  N N 431 
TYR OXT  O  N N 432 
TYR H    H  N N 433 
TYR H2   H  N N 434 
TYR HA   H  N N 435 
TYR HB2  H  N N 436 
TYR HB3  H  N N 437 
TYR HD1  H  N N 438 
TYR HD2  H  N N 439 
TYR HE1  H  N N 440 
TYR HE2  H  N N 441 
TYR HH   H  N N 442 
TYR HXT  H  N N 443 
VAL N    N  N N 444 
VAL CA   C  N S 445 
VAL C    C  N N 446 
VAL O    O  N N 447 
VAL CB   C  N N 448 
VAL CG1  C  N N 449 
VAL CG2  C  N N 450 
VAL OXT  O  N N 451 
VAL H    H  N N 452 
VAL H2   H  N N 453 
VAL HA   H  N N 454 
VAL HB   H  N N 455 
VAL HG11 H  N N 456 
VAL HG12 H  N N 457 
VAL HG13 H  N N 458 
VAL HG21 H  N N 459 
VAL HG22 H  N N 460 
VAL HG23 H  N N 461 
VAL HXT  H  N N 462 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HEM CHA C1A  sing N N 129 
HEM CHA C4D  doub N N 130 
HEM CHA HHA  sing N N 131 
HEM CHB C4A  sing N N 132 
HEM CHB C1B  doub N N 133 
HEM CHB HHB  sing N N 134 
HEM CHC C4B  sing N N 135 
HEM CHC C1C  doub N N 136 
HEM CHC HHC  sing N N 137 
HEM CHD C4C  doub N N 138 
HEM CHD C1D  sing N N 139 
HEM CHD HHD  sing N N 140 
HEM C1A C2A  doub Y N 141 
HEM C1A NA   sing Y N 142 
HEM C2A C3A  sing Y N 143 
HEM C2A CAA  sing N N 144 
HEM C3A C4A  doub Y N 145 
HEM C3A CMA  sing N N 146 
HEM C4A NA   sing Y N 147 
HEM CMA HMA  sing N N 148 
HEM CMA HMAA sing N N 149 
HEM CMA HMAB sing N N 150 
HEM CAA CBA  sing N N 151 
HEM CAA HAA  sing N N 152 
HEM CAA HAAA sing N N 153 
HEM CBA CGA  sing N N 154 
HEM CBA HBA  sing N N 155 
HEM CBA HBAA sing N N 156 
HEM CGA O1A  doub N N 157 
HEM CGA O2A  sing N N 158 
HEM C1B C2B  sing N N 159 
HEM C1B NB   sing N N 160 
HEM C2B C3B  doub N N 161 
HEM C2B CMB  sing N N 162 
HEM C3B C4B  sing N N 163 
HEM C3B CAB  sing N N 164 
HEM C4B NB   doub N N 165 
HEM CMB HMB  sing N N 166 
HEM CMB HMBA sing N N 167 
HEM CMB HMBB sing N N 168 
HEM CAB CBB  doub N N 169 
HEM CAB HAB  sing N N 170 
HEM CBB HBB  sing N N 171 
HEM CBB HBBA sing N N 172 
HEM C1C C2C  sing Y N 173 
HEM C1C NC   sing Y N 174 
HEM C2C C3C  doub Y N 175 
HEM C2C CMC  sing N N 176 
HEM C3C C4C  sing Y N 177 
HEM C3C CAC  sing N N 178 
HEM C4C NC   sing Y N 179 
HEM CMC HMC  sing N N 180 
HEM CMC HMCA sing N N 181 
HEM CMC HMCB sing N N 182 
HEM CAC CBC  doub N N 183 
HEM CAC HAC  sing N N 184 
HEM CBC HBC  sing N N 185 
HEM CBC HBCA sing N N 186 
HEM C1D C2D  sing N N 187 
HEM C1D ND   doub N N 188 
HEM C2D C3D  doub N N 189 
HEM C2D CMD  sing N N 190 
HEM C3D C4D  sing N N 191 
HEM C3D CAD  sing N N 192 
HEM C4D ND   sing N N 193 
HEM CMD HMD  sing N N 194 
HEM CMD HMDA sing N N 195 
HEM CMD HMDB sing N N 196 
HEM CAD CBD  sing N N 197 
HEM CAD HAD  sing N N 198 
HEM CAD HADA sing N N 199 
HEM CBD CGD  sing N N 200 
HEM CBD HBD  sing N N 201 
HEM CBD HBDA sing N N 202 
HEM CGD O1D  doub N N 203 
HEM CGD O2D  sing N N 204 
HEM O2A H2A  sing N N 205 
HEM O2D H2D  sing N N 206 
HEM FE  NA   sing N N 207 
HEM FE  NB   sing N N 208 
HEM FE  NC   sing N N 209 
HEM FE  ND   sing N N 210 
HIS N   CA   sing N N 211 
HIS N   H    sing N N 212 
HIS N   H2   sing N N 213 
HIS CA  C    sing N N 214 
HIS CA  CB   sing N N 215 
HIS CA  HA   sing N N 216 
HIS C   O    doub N N 217 
HIS C   OXT  sing N N 218 
HIS CB  CG   sing N N 219 
HIS CB  HB2  sing N N 220 
HIS CB  HB3  sing N N 221 
HIS CG  ND1  sing Y N 222 
HIS CG  CD2  doub Y N 223 
HIS ND1 CE1  doub Y N 224 
HIS ND1 HD1  sing N N 225 
HIS CD2 NE2  sing Y N 226 
HIS CD2 HD2  sing N N 227 
HIS CE1 NE2  sing Y N 228 
HIS CE1 HE1  sing N N 229 
HIS NE2 HE2  sing N N 230 
HIS OXT HXT  sing N N 231 
ILE N   CA   sing N N 232 
ILE N   H    sing N N 233 
ILE N   H2   sing N N 234 
ILE CA  C    sing N N 235 
ILE CA  CB   sing N N 236 
ILE CA  HA   sing N N 237 
ILE C   O    doub N N 238 
ILE C   OXT  sing N N 239 
ILE CB  CG1  sing N N 240 
ILE CB  CG2  sing N N 241 
ILE CB  HB   sing N N 242 
ILE CG1 CD1  sing N N 243 
ILE CG1 HG12 sing N N 244 
ILE CG1 HG13 sing N N 245 
ILE CG2 HG21 sing N N 246 
ILE CG2 HG22 sing N N 247 
ILE CG2 HG23 sing N N 248 
ILE CD1 HD11 sing N N 249 
ILE CD1 HD12 sing N N 250 
ILE CD1 HD13 sing N N 251 
ILE OXT HXT  sing N N 252 
LEU N   CA   sing N N 253 
LEU N   H    sing N N 254 
LEU N   H2   sing N N 255 
LEU CA  C    sing N N 256 
LEU CA  CB   sing N N 257 
LEU CA  HA   sing N N 258 
LEU C   O    doub N N 259 
LEU C   OXT  sing N N 260 
LEU CB  CG   sing N N 261 
LEU CB  HB2  sing N N 262 
LEU CB  HB3  sing N N 263 
LEU CG  CD1  sing N N 264 
LEU CG  CD2  sing N N 265 
LEU CG  HG   sing N N 266 
LEU CD1 HD11 sing N N 267 
LEU CD1 HD12 sing N N 268 
LEU CD1 HD13 sing N N 269 
LEU CD2 HD21 sing N N 270 
LEU CD2 HD22 sing N N 271 
LEU CD2 HD23 sing N N 272 
LEU OXT HXT  sing N N 273 
LYS N   CA   sing N N 274 
LYS N   H    sing N N 275 
LYS N   H2   sing N N 276 
LYS CA  C    sing N N 277 
LYS CA  CB   sing N N 278 
LYS CA  HA   sing N N 279 
LYS C   O    doub N N 280 
LYS C   OXT  sing N N 281 
LYS CB  CG   sing N N 282 
LYS CB  HB2  sing N N 283 
LYS CB  HB3  sing N N 284 
LYS CG  CD   sing N N 285 
LYS CG  HG2  sing N N 286 
LYS CG  HG3  sing N N 287 
LYS CD  CE   sing N N 288 
LYS CD  HD2  sing N N 289 
LYS CD  HD3  sing N N 290 
LYS CE  NZ   sing N N 291 
LYS CE  HE2  sing N N 292 
LYS CE  HE3  sing N N 293 
LYS NZ  HZ1  sing N N 294 
LYS NZ  HZ2  sing N N 295 
LYS NZ  HZ3  sing N N 296 
LYS OXT HXT  sing N N 297 
MET N   CA   sing N N 298 
MET N   H    sing N N 299 
MET N   H2   sing N N 300 
MET CA  C    sing N N 301 
MET CA  CB   sing N N 302 
MET CA  HA   sing N N 303 
MET C   O    doub N N 304 
MET C   OXT  sing N N 305 
MET CB  CG   sing N N 306 
MET CB  HB2  sing N N 307 
MET CB  HB3  sing N N 308 
MET CG  SD   sing N N 309 
MET CG  HG2  sing N N 310 
MET CG  HG3  sing N N 311 
MET SD  CE   sing N N 312 
MET CE  HE1  sing N N 313 
MET CE  HE2  sing N N 314 
MET CE  HE3  sing N N 315 
MET OXT HXT  sing N N 316 
PHE N   CA   sing N N 317 
PHE N   H    sing N N 318 
PHE N   H2   sing N N 319 
PHE CA  C    sing N N 320 
PHE CA  CB   sing N N 321 
PHE CA  HA   sing N N 322 
PHE C   O    doub N N 323 
PHE C   OXT  sing N N 324 
PHE CB  CG   sing N N 325 
PHE CB  HB2  sing N N 326 
PHE CB  HB3  sing N N 327 
PHE CG  CD1  doub Y N 328 
PHE CG  CD2  sing Y N 329 
PHE CD1 CE1  sing Y N 330 
PHE CD1 HD1  sing N N 331 
PHE CD2 CE2  doub Y N 332 
PHE CD2 HD2  sing N N 333 
PHE CE1 CZ   doub Y N 334 
PHE CE1 HE1  sing N N 335 
PHE CE2 CZ   sing Y N 336 
PHE CE2 HE2  sing N N 337 
PHE CZ  HZ   sing N N 338 
PHE OXT HXT  sing N N 339 
PRO N   CA   sing N N 340 
PRO N   CD   sing N N 341 
PRO N   H    sing N N 342 
PRO CA  C    sing N N 343 
PRO CA  CB   sing N N 344 
PRO CA  HA   sing N N 345 
PRO C   O    doub N N 346 
PRO C   OXT  sing N N 347 
PRO CB  CG   sing N N 348 
PRO CB  HB2  sing N N 349 
PRO CB  HB3  sing N N 350 
PRO CG  CD   sing N N 351 
PRO CG  HG2  sing N N 352 
PRO CG  HG3  sing N N 353 
PRO CD  HD2  sing N N 354 
PRO CD  HD3  sing N N 355 
PRO OXT HXT  sing N N 356 
SER N   CA   sing N N 357 
SER N   H    sing N N 358 
SER N   H2   sing N N 359 
SER CA  C    sing N N 360 
SER CA  CB   sing N N 361 
SER CA  HA   sing N N 362 
SER C   O    doub N N 363 
SER C   OXT  sing N N 364 
SER CB  OG   sing N N 365 
SER CB  HB2  sing N N 366 
SER CB  HB3  sing N N 367 
SER OG  HG   sing N N 368 
SER OXT HXT  sing N N 369 
THR N   CA   sing N N 370 
THR N   H    sing N N 371 
THR N   H2   sing N N 372 
THR CA  C    sing N N 373 
THR CA  CB   sing N N 374 
THR CA  HA   sing N N 375 
THR C   O    doub N N 376 
THR C   OXT  sing N N 377 
THR CB  OG1  sing N N 378 
THR CB  CG2  sing N N 379 
THR CB  HB   sing N N 380 
THR OG1 HG1  sing N N 381 
THR CG2 HG21 sing N N 382 
THR CG2 HG22 sing N N 383 
THR CG2 HG23 sing N N 384 
THR OXT HXT  sing N N 385 
TRP N   CA   sing N N 386 
TRP N   H    sing N N 387 
TRP N   H2   sing N N 388 
TRP CA  C    sing N N 389 
TRP CA  CB   sing N N 390 
TRP CA  HA   sing N N 391 
TRP C   O    doub N N 392 
TRP C   OXT  sing N N 393 
TRP CB  CG   sing N N 394 
TRP CB  HB2  sing N N 395 
TRP CB  HB3  sing N N 396 
TRP CG  CD1  doub Y N 397 
TRP CG  CD2  sing Y N 398 
TRP CD1 NE1  sing Y N 399 
TRP CD1 HD1  sing N N 400 
TRP CD2 CE2  doub Y N 401 
TRP CD2 CE3  sing Y N 402 
TRP NE1 CE2  sing Y N 403 
TRP NE1 HE1  sing N N 404 
TRP CE2 CZ2  sing Y N 405 
TRP CE3 CZ3  doub Y N 406 
TRP CE3 HE3  sing N N 407 
TRP CZ2 CH2  doub Y N 408 
TRP CZ2 HZ2  sing N N 409 
TRP CZ3 CH2  sing Y N 410 
TRP CZ3 HZ3  sing N N 411 
TRP CH2 HH2  sing N N 412 
TRP OXT HXT  sing N N 413 
TYR N   CA   sing N N 414 
TYR N   H    sing N N 415 
TYR N   H2   sing N N 416 
TYR CA  C    sing N N 417 
TYR CA  CB   sing N N 418 
TYR CA  HA   sing N N 419 
TYR C   O    doub N N 420 
TYR C   OXT  sing N N 421 
TYR CB  CG   sing N N 422 
TYR CB  HB2  sing N N 423 
TYR CB  HB3  sing N N 424 
TYR CG  CD1  doub Y N 425 
TYR CG  CD2  sing Y N 426 
TYR CD1 CE1  sing Y N 427 
TYR CD1 HD1  sing N N 428 
TYR CD2 CE2  doub Y N 429 
TYR CD2 HD2  sing N N 430 
TYR CE1 CZ   doub Y N 431 
TYR CE1 HE1  sing N N 432 
TYR CE2 CZ   sing Y N 433 
TYR CE2 HE2  sing N N 434 
TYR CZ  OH   sing N N 435 
TYR OH  HH   sing N N 436 
TYR OXT HXT  sing N N 437 
VAL N   CA   sing N N 438 
VAL N   H    sing N N 439 
VAL N   H2   sing N N 440 
VAL CA  C    sing N N 441 
VAL CA  CB   sing N N 442 
VAL CA  HA   sing N N 443 
VAL C   O    doub N N 444 
VAL C   OXT  sing N N 445 
VAL CB  CG1  sing N N 446 
VAL CB  CG2  sing N N 447 
VAL CB  HB   sing N N 448 
VAL CG1 HG11 sing N N 449 
VAL CG1 HG12 sing N N 450 
VAL CG1 HG13 sing N N 451 
VAL CG2 HG21 sing N N 452 
VAL CG2 HG22 sing N N 453 
VAL CG2 HG23 sing N N 454 
VAL OXT HXT  sing N N 455 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-10-25 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9E4R 
_em_admin.last_update        2025-03-19 
_em_admin.map_release_date   2025-03-19 
_em_admin.title              'Escherichia coli encapsulin-associated DyP peroxidase' 
# 
loop_
_em_buffer_component.buffer_id 
_em_buffer_component.concentration 
_em_buffer_component.concentration_units 
_em_buffer_component.formula 
_em_buffer_component.id 
_em_buffer_component.name 
1 150 mM NaCl     1 'sodium chloride'                 
1 20  mM C4H11NO3 2 'tris(hydroxymethyl)aminomethane' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          1169357 
_em_entity_assembly_naturalsource.organism             'Escherichia coli' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               KTE40 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          469008 
_em_entity_assembly_recombinant.organism             'Escherichia coli BL21(DE3)' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              
;Particles were picked from micrographs collected on two different grids using TFS Glacios and FEI Talos Arctica cryogenic electron microscopes.
;
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
loop_
_em_image_recording.average_exposure_time 
_em_image_recording.avg_electron_dose_per_subtomogram 
_em_image_recording.avg_electron_dose_per_image 
_em_image_recording.details 
_em_image_recording.detector_mode 
_em_image_recording.film_or_detector_model 
_em_image_recording.id 
_em_image_recording.imaging_id 
_em_image_recording.num_diffraction_images 
_em_image_recording.num_grids_imaged 
_em_image_recording.num_real_images 
6 ? 47.84 ? COUNTING 'GATAN K2 SUMMIT (4k x 4k)' 1 1 ? 1 123 
4 ? 46.24 ? COUNTING 'GATAN K2 SUMMIT (4k x 4k)' 2 2 ? 1 206 
# 
_em_particle_selection.details                  ? 
_em_particle_selection.id                       1 
_em_particle_selection.image_processing_id      1 
_em_particle_selection.method                   ? 
_em_particle_selection.num_particles_selected   115178 
_em_particle_selection.reference_model          ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'       ?                       1  1 ? ? cryoSPARC       4.5.1      
'IMAGE ACQUISITION'        ?                       2  ? ? 1 Leginon         ?          
MASKING                    ?                       3  ? ? ? ?               ?          
'CTF CORRECTION'           ?                       4  1 ? ? cryoSPARC       4.5.1      
'LAYERLINE INDEXING'       ?                       5  ? ? ? ?               ?          
'DIFFRACTION INDEXING'     ?                       6  ? ? ? ?               ?          
'MODEL FITTING'            ?                       7  ? 1 ? 'UCSF ChimeraX' 1.8        
OTHER                      ?                       8  ? ? ? ?               ?          
'IMAGE ACQUISITION'        ?                       9  ? ? 2 Leginon         ?          
'MODEL REFINEMENT'         'real space refinement' 10 ? 1 ? PHENIX          1.2.1-4887 
'MODEL REFINEMENT'         ?                       11 ? 1 ? Coot            0.9.8.1    
'INITIAL EULER ASSIGNMENT' ?                       12 1 ? ? cryoSPARC       4.5.1      
'FINAL EULER ASSIGNMENT'   ?                       13 1 ? ? cryoSPARC       4.5.1      
CLASSIFICATION             ?                       14 1 ? ? ?               ?          
RECONSTRUCTION             'Local Refinement'      15 1 ? ? cryoSPARC       4.5.1      
# 
_em_specimen.concentration           0.5 
_em_specimen.details                 'Sample was frozen on two grids, one at 0.5 mg/mL and the other at 0.25 mg/mL.' 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   A0A747AN60 
# 
_atom_sites.entry_id                    9E4R 
_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]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_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]   1.000000 
_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   . CYS A 1 22  ? 124.165 126.993 80.139  1.00 109.62 ? 3   CYS A N   1 
ATOM   2    C  CA  . CYS A 1 22  ? 123.414 126.694 81.353  1.00 109.62 ? 3   CYS A CA  1 
ATOM   3    C  C   . CYS A 1 22  ? 123.870 127.574 82.512  1.00 109.62 ? 3   CYS A C   1 
ATOM   4    O  O   . CYS A 1 22  ? 124.725 127.174 83.303  1.00 109.62 ? 3   CYS A O   1 
ATOM   5    C  CB  . CYS A 1 22  ? 123.559 125.217 81.723  1.00 109.62 ? 3   CYS A CB  1 
ATOM   6    S  SG  . CYS A 1 22  ? 122.806 124.075 80.540  1.00 109.62 ? 3   CYS A SG  1 
ATOM   7    N  N   . PRO A 1 23  ? 123.301 128.775 82.609  1.00 106.74 ? 4   PRO A N   1 
ATOM   8    C  CA  . PRO A 1 23  ? 123.683 129.686 83.697  1.00 106.74 ? 4   PRO A CA  1 
ATOM   9    C  C   . PRO A 1 23  ? 123.104 129.223 85.026  1.00 106.74 ? 4   PRO A C   1 
ATOM   10   O  O   . PRO A 1 23  ? 121.913 128.924 85.131  1.00 106.74 ? 4   PRO A O   1 
ATOM   11   C  CB  . PRO A 1 23  ? 123.088 131.028 83.259  1.00 106.74 ? 4   PRO A CB  1 
ATOM   12   C  CG  . PRO A 1 23  ? 121.923 130.651 82.404  1.00 106.74 ? 4   PRO A CG  1 
ATOM   13   C  CD  . PRO A 1 23  ? 122.312 129.378 81.699  1.00 106.74 ? 4   PRO A CD  1 
ATOM   14   N  N   . PHE A 1 24  ? 123.960 129.161 86.043  1.00 101.92 ? 5   PHE A N   1 
ATOM   15   C  CA  . PHE A 1 24  ? 123.526 128.764 87.375  1.00 101.92 ? 5   PHE A CA  1 
ATOM   16   C  C   . PHE A 1 24  ? 122.760 129.907 88.029  1.00 101.92 ? 5   PHE A C   1 
ATOM   17   O  O   . PHE A 1 24  ? 123.239 131.044 88.072  1.00 101.92 ? 5   PHE A O   1 
ATOM   18   C  CB  . PHE A 1 24  ? 124.719 128.361 88.245  1.00 101.92 ? 5   PHE A CB  1 
ATOM   19   C  CG  . PHE A 1 24  ? 125.693 127.431 87.567  1.00 101.92 ? 5   PHE A CG  1 
ATOM   20   C  CD1 . PHE A 1 24  ? 125.272 126.534 86.597  1.00 101.92 ? 5   PHE A CD1 1 
ATOM   21   C  CD2 . PHE A 1 24  ? 127.035 127.455 87.909  1.00 101.92 ? 5   PHE A CD2 1 
ATOM   22   C  CE1 . PHE A 1 24  ? 126.171 125.683 85.981  1.00 101.92 ? 5   PHE A CE1 1 
ATOM   23   C  CE2 . PHE A 1 24  ? 127.938 126.606 87.297  1.00 101.92 ? 5   PHE A CE2 1 
ATOM   24   C  CZ  . PHE A 1 24  ? 127.505 125.719 86.332  1.00 101.92 ? 5   PHE A CZ  1 
ATOM   25   N  N   . SER A 1 25  ? 121.569 129.603 88.533  1.00 94.79  ? 6   SER A N   1 
ATOM   26   C  CA  . SER A 1 25  ? 120.725 130.599 89.172  1.00 94.79  ? 6   SER A CA  1 
ATOM   27   C  C   . SER A 1 25  ? 120.964 130.637 90.675  1.00 94.79  ? 6   SER A C   1 
ATOM   28   O  O   . SER A 1 25  ? 121.389 129.652 91.285  1.00 94.79  ? 6   SER A O   1 
ATOM   29   C  CB  . SER A 1 25  ? 119.253 130.308 88.895  1.00 94.79  ? 6   SER A CB  1 
ATOM   30   O  OG  . SER A 1 25  ? 118.782 129.241 89.698  1.00 94.79  ? 6   SER A OG  1 
ATOM   31   N  N   . GLN A 1 26  ? 120.682 131.794 91.270  1.00 87.71  ? 7   GLN A N   1 
ATOM   32   C  CA  . GLN A 1 26  ? 120.847 131.955 92.703  1.00 87.71  ? 7   GLN A CA  1 
ATOM   33   C  C   . GLN A 1 26  ? 119.778 131.162 93.454  1.00 87.71  ? 7   GLN A C   1 
ATOM   34   O  O   . GLN A 1 26  ? 118.794 130.685 92.882  1.00 87.71  ? 7   GLN A O   1 
ATOM   35   C  CB  . GLN A 1 26  ? 120.782 133.432 93.088  1.00 87.71  ? 7   GLN A CB  1 
ATOM   36   C  CG  . GLN A 1 26  ? 121.680 134.329 92.256  1.00 87.71  ? 7   GLN A CG  1 
ATOM   37   C  CD  . GLN A 1 26  ? 122.189 135.525 93.033  1.00 87.71  ? 7   GLN A CD  1 
ATOM   38   O  OE1 . GLN A 1 26  ? 122.605 135.401 94.184  1.00 87.71  ? 7   GLN A OE1 1 
ATOM   39   N  NE2 . GLN A 1 26  ? 122.155 136.695 92.406  1.00 87.71  ? 7   GLN A NE2 1 
ATOM   40   N  N   . SER A 1 27  ? 119.987 131.022 94.763  1.00 90.94  ? 8   SER A N   1 
ATOM   41   C  CA  . SER A 1 27  ? 119.063 130.293 95.631  1.00 90.94  ? 8   SER A CA  1 
ATOM   42   C  C   . SER A 1 27  ? 117.837 131.166 95.886  1.00 90.94  ? 8   SER A C   1 
ATOM   43   O  O   . SER A 1 27  ? 117.677 131.789 96.939  1.00 90.94  ? 8   SER A O   1 
ATOM   44   C  CB  . SER A 1 27  ? 119.754 129.896 96.928  1.00 90.94  ? 8   SER A CB  1 
ATOM   45   O  OG  . SER A 1 27  ? 120.129 131.045 97.663  1.00 90.94  ? 8   SER A OG  1 
ATOM   46   N  N   . VAL A 1 28  ? 116.953 131.208 94.894  1.00 90.25  ? 9   VAL A N   1 
ATOM   47   C  CA  . VAL A 1 28  ? 115.738 132.013 94.986  1.00 90.25  ? 9   VAL A CA  1 
ATOM   48   C  C   . VAL A 1 28  ? 114.557 131.189 95.481  1.00 90.25  ? 9   VAL A C   1 
ATOM   49   O  O   . VAL A 1 28  ? 113.899 131.552 96.459  1.00 90.25  ? 9   VAL A O   1 
ATOM   50   C  CB  . VAL A 1 28  ? 115.434 132.665 93.621  1.00 90.25  ? 9   VAL A CB  1 
ATOM   51   C  CG1 . VAL A 1 28  ? 114.445 133.802 93.789  1.00 90.25  ? 9   VAL A CG1 1 
ATOM   52   C  CG2 . VAL A 1 28  ? 116.714 133.165 92.976  1.00 90.25  ? 9   VAL A CG2 1 
ATOM   53   N  N   . SER A 1 29  ? 114.271 130.069 94.817  1.00 97.82  ? 10  SER A N   1 
ATOM   54   C  CA  . SER A 1 29  ? 113.144 129.220 95.178  1.00 97.82  ? 10  SER A CA  1 
ATOM   55   C  C   . SER A 1 29  ? 113.534 128.016 96.024  1.00 97.82  ? 10  SER A C   1 
ATOM   56   O  O   . SER A 1 29  ? 112.685 127.493 96.753  1.00 97.82  ? 10  SER A O   1 
ATOM   57   C  CB  . SER A 1 29  ? 112.423 128.729 93.917  1.00 97.82  ? 10  SER A CB  1 
ATOM   58   O  OG  . SER A 1 29  ? 113.289 127.954 93.106  1.00 97.82  ? 10  SER A OG  1 
ATOM   59   N  N   . GLN A 1 30  ? 114.784 127.565 95.938  1.00 103.23 ? 11  GLN A N   1 
ATOM   60   C  CA  . GLN A 1 30  ? 115.215 126.403 96.713  1.00 103.23 ? 11  GLN A CA  1 
ATOM   61   C  C   . GLN A 1 30  ? 115.092 126.597 98.222  1.00 103.23 ? 11  GLN A C   1 
ATOM   62   O  O   . GLN A 1 30  ? 114.618 125.666 98.898  1.00 103.23 ? 11  GLN A O   1 
ATOM   63   C  CB  . GLN A 1 30  ? 116.646 126.030 96.310  1.00 103.23 ? 11  GLN A CB  1 
ATOM   64   C  CG  . GLN A 1 30  ? 117.447 125.330 97.395  1.00 103.23 ? 11  GLN A CG  1 
ATOM   65   C  CD  . GLN A 1 30  ? 118.928 125.279 97.079  1.00 103.23 ? 11  GLN A CD  1 
ATOM   66   O  OE1 . GLN A 1 30  ? 119.350 125.609 95.970  1.00 103.23 ? 11  GLN A OE1 1 
ATOM   67   N  NE2 . GLN A 1 30  ? 119.728 124.864 98.054  1.00 103.23 ? 11  GLN A NE2 1 
ATOM   68   N  N   . PRO A 1 31  ? 115.501 127.727 98.818  1.00 98.97  ? 12  PRO A N   1 
ATOM   69   C  CA  . PRO A 1 31  ? 115.332 127.863 100.277 1.00 98.97  ? 12  PRO A CA  1 
ATOM   70   C  C   . PRO A 1 31  ? 113.886 127.779 100.735 1.00 98.97  ? 12  PRO A C   1 
ATOM   71   O  O   . PRO A 1 31  ? 113.614 127.234 101.812 1.00 98.97  ? 12  PRO A O   1 
ATOM   72   C  CB  . PRO A 1 31  ? 115.943 129.242 100.565 1.00 98.97  ? 12  PRO A CB  1 
ATOM   73   C  CG  . PRO A 1 31  ? 116.929 129.434 99.470  1.00 98.97  ? 12  PRO A CG  1 
ATOM   74   C  CD  . PRO A 1 31  ? 116.235 128.880 98.265  1.00 98.97  ? 12  PRO A CD  1 
ATOM   75   N  N   . VAL A 1 32  ? 112.949 128.311 99.950  1.00 100.59 ? 13  VAL A N   1 
ATOM   76   C  CA  . VAL A 1 32  ? 111.543 128.288 100.344 1.00 100.59 ? 13  VAL A CA  1 
ATOM   77   C  C   . VAL A 1 32  ? 111.019 126.856 100.353 1.00 100.59 ? 13  VAL A C   1 
ATOM   78   O  O   . VAL A 1 32  ? 110.375 126.417 101.312 1.00 100.59 ? 13  VAL A O   1 
ATOM   79   C  CB  . VAL A 1 32  ? 110.711 129.193 99.417  1.00 100.59 ? 13  VAL A CB  1 
ATOM   80   C  CG1 . VAL A 1 32  ? 109.262 128.727 99.368  1.00 100.59 ? 13  VAL A CG1 1 
ATOM   81   C  CG2 . VAL A 1 32  ? 110.795 130.640 99.876  1.00 100.59 ? 13  VAL A CG2 1 
ATOM   82   N  N   . ASP A 1 33  ? 111.291 126.109 99.280  1.00 105.69 ? 14  ASP A N   1 
ATOM   83   C  CA  . ASP A 1 33  ? 110.852 124.720 99.201  1.00 105.69 ? 14  ASP A CA  1 
ATOM   84   C  C   . ASP A 1 33  ? 111.511 123.860 100.274 1.00 105.69 ? 14  ASP A C   1 
ATOM   85   O  O   . ASP A 1 33  ? 110.854 123.011 100.887 1.00 105.69 ? 14  ASP A O   1 
ATOM   86   C  CB  . ASP A 1 33  ? 111.142 124.157 97.810  1.00 105.69 ? 14  ASP A CB  1 
ATOM   87   C  CG  . ASP A 1 33  ? 110.719 125.099 96.701  1.00 105.69 ? 14  ASP A CG  1 
ATOM   88   O  OD1 . ASP A 1 33  ? 109.738 125.847 96.897  1.00 105.69 ? 14  ASP A OD1 1 
ATOM   89   O  OD2 . ASP A 1 33  ? 111.366 125.091 95.633  1.00 105.69 ? 14  ASP A OD2 1 
ATOM   90   N  N   . GLU A 1 34  ? 112.811 124.058 100.509 1.00 106.21 ? 15  GLU A N   1 
ATOM   91   C  CA  . GLU A 1 34  ? 113.481 123.336 101.587 1.00 106.21 ? 15  GLU A CA  1 
ATOM   92   C  C   . GLU A 1 34  ? 112.895 123.676 102.952 1.00 106.21 ? 15  GLU A C   1 
ATOM   93   O  O   . GLU A 1 34  ? 112.932 122.840 103.863 1.00 106.21 ? 15  GLU A O   1 
ATOM   94   C  CB  . GLU A 1 34  ? 114.981 123.639 101.565 1.00 106.21 ? 15  GLU A CB  1 
ATOM   95   C  CG  . GLU A 1 34  ? 115.859 122.606 102.270 1.00 106.21 ? 15  GLU A CG  1 
ATOM   96   C  CD  . GLU A 1 34  ? 115.507 121.170 101.918 1.00 106.21 ? 15  GLU A CD  1 
ATOM   97   O  OE1 . GLU A 1 34  ? 115.599 120.304 102.812 1.00 106.21 ? 15  GLU A OE1 1 
ATOM   98   O  OE2 . GLU A 1 34  ? 115.173 120.899 100.745 1.00 106.21 ? 15  GLU A OE2 1 
ATOM   99   N  N   . ARG A 1 35  ? 112.352 124.884 103.112 1.00 103.21 ? 16  ARG A N   1 
ATOM   100  C  CA  . ARG A 1 35  ? 111.681 125.313 104.341 1.00 103.21 ? 16  ARG A CA  1 
ATOM   101  C  C   . ARG A 1 35  ? 112.616 125.187 105.549 1.00 103.21 ? 16  ARG A C   1 
ATOM   102  O  O   . ARG A 1 35  ? 112.419 124.369 106.449 1.00 103.21 ? 16  ARG A O   1 
ATOM   103  C  CB  . ARG A 1 35  ? 110.387 124.519 104.562 1.00 103.21 ? 16  ARG A CB  1 
ATOM   104  C  CG  . ARG A 1 35  ? 109.357 125.232 105.424 1.00 103.21 ? 16  ARG A CG  1 
ATOM   105  C  CD  . ARG A 1 35  ? 107.937 124.912 104.981 1.00 103.21 ? 16  ARG A CD  1 
ATOM   106  N  NE  . ARG A 1 35  ? 107.752 125.074 103.544 1.00 103.21 ? 16  ARG A NE  1 
ATOM   107  C  CZ  . ARG A 1 35  ? 107.449 124.087 102.712 1.00 103.21 ? 16  ARG A CZ  1 
ATOM   108  N  NH1 . ARG A 1 35  ? 107.290 122.845 103.141 1.00 103.21 ? 16  ARG A NH1 1 
ATOM   109  N  NH2 . ARG A 1 35  ? 107.299 124.352 101.418 1.00 103.21 ? 16  ARG A NH2 1 
ATOM   110  N  N   . LEU A 1 36  ? 113.650 126.029 105.542 1.00 92.51  ? 17  LEU A N   1 
ATOM   111  C  CA  . LEU A 1 36  ? 114.576 126.093 106.662 1.00 92.51  ? 17  LEU A CA  1 
ATOM   112  C  C   . LEU A 1 36  ? 114.862 127.506 107.154 1.00 92.51  ? 17  LEU A C   1 
ATOM   113  O  O   . LEU A 1 36  ? 115.658 127.665 108.085 1.00 92.51  ? 17  LEU A O   1 
ATOM   114  C  CB  . LEU A 1 36  ? 115.906 125.417 106.293 1.00 92.51  ? 17  LEU A CB  1 
ATOM   115  C  CG  . LEU A 1 36  ? 116.148 124.020 106.869 1.00 92.51  ? 17  LEU A CG  1 
ATOM   116  C  CD1 . LEU A 1 36  ? 117.428 123.424 106.305 1.00 92.51  ? 17  LEU A CD1 1 
ATOM   117  C  CD2 . LEU A 1 36  ? 116.202 124.070 108.387 1.00 92.51  ? 17  LEU A CD2 1 
ATOM   118  N  N   . THR A 1 37  ? 114.244 128.529 106.569 1.00 81.95  ? 18  THR A N   1 
ATOM   119  C  CA  . THR A 1 37  ? 114.530 129.913 106.948 1.00 81.95  ? 18  THR A CA  1 
ATOM   120  C  C   . THR A 1 37  ? 113.826 130.233 108.265 1.00 81.95  ? 18  THR A C   1 
ATOM   121  O  O   . THR A 1 37  ? 112.668 130.652 108.303 1.00 81.95  ? 18  THR A O   1 
ATOM   122  C  CB  . THR A 1 37  ? 114.133 130.867 105.822 1.00 81.95  ? 18  THR A CB  1 
ATOM   123  O  OG1 . THR A 1 37  ? 114.306 132.225 106.246 1.00 81.95  ? 18  THR A OG1 1 
ATOM   124  C  CG2 . THR A 1 37  ? 112.699 130.623 105.336 1.00 81.95  ? 18  THR A CG2 1 
ATOM   125  N  N   . ARG A 1 38  ? 114.540 130.029 109.371 1.00 76.44  ? 19  ARG A N   1 
ATOM   126  C  CA  . ARG A 1 38  ? 114.059 130.446 110.681 1.00 76.44  ? 19  ARG A CA  1 
ATOM   127  C  C   . ARG A 1 38  ? 114.475 131.863 111.051 1.00 76.44  ? 19  ARG A C   1 
ATOM   128  O  O   . ARG A 1 38  ? 114.030 132.372 112.084 1.00 76.44  ? 19  ARG A O   1 
ATOM   129  C  CB  . ARG A 1 38  ? 114.557 129.477 111.758 1.00 76.44  ? 19  ARG A CB  1 
ATOM   130  C  CG  . ARG A 1 38  ? 113.717 128.222 111.904 1.00 76.44  ? 19  ARG A CG  1 
ATOM   131  C  CD  . ARG A 1 38  ? 113.733 127.711 113.335 1.00 76.44  ? 19  ARG A CD  1 
ATOM   132  N  NE  . ARG A 1 38  ? 112.993 128.587 114.235 1.00 76.44  ? 19  ARG A NE  1 
ATOM   133  C  CZ  . ARG A 1 38  ? 113.550 129.356 115.160 1.00 76.44  ? 19  ARG A CZ  1 
ATOM   134  N  NH1 . ARG A 1 38  ? 114.861 129.382 115.341 1.00 76.44  ? 19  ARG A NH1 1 
ATOM   135  N  NH2 . ARG A 1 38  ? 112.773 130.119 115.924 1.00 76.44  ? 19  ARG A NH2 1 
ATOM   136  N  N   . ALA A 1 39  ? 115.317 132.504 110.243 1.00 70.42  ? 20  ALA A N   1 
ATOM   137  C  CA  . ALA A 1 39  ? 115.759 133.866 110.499 1.00 70.42  ? 20  ALA A CA  1 
ATOM   138  C  C   . ALA A 1 39  ? 116.236 134.474 109.191 1.00 70.42  ? 20  ALA A C   1 
ATOM   139  O  O   . ALA A 1 39  ? 116.765 133.772 108.324 1.00 70.42  ? 20  ALA A O   1 
ATOM   140  C  CB  . ALA A 1 39  ? 116.873 133.911 111.550 1.00 70.42  ? 20  ALA A CB  1 
ATOM   141  N  N   . ALA A 1 40  ? 116.043 135.785 109.052 1.00 65.82  ? 21  ALA A N   1 
ATOM   142  C  CA  . ALA A 1 40  ? 116.407 136.458 107.816 1.00 65.82  ? 21  ALA A CA  1 
ATOM   143  C  C   . ALA A 1 40  ? 116.767 137.905 108.108 1.00 65.82  ? 21  ALA A C   1 
ATOM   144  O  O   . ALA A 1 40  ? 116.349 138.486 109.112 1.00 65.82  ? 21  ALA A O   1 
ATOM   145  C  CB  . ALA A 1 40  ? 115.281 136.391 106.779 1.00 65.82  ? 21  ALA A CB  1 
ATOM   146  N  N   . ILE A 1 41  ? 117.557 138.476 107.207 1.00 64.73  ? 22  ILE A N   1 
ATOM   147  C  CA  . ILE A 1 41  ? 117.959 139.874 107.266 1.00 64.73  ? 22  ILE A CA  1 
ATOM   148  C  C   . ILE A 1 41  ? 117.762 140.477 105.884 1.00 64.73  ? 22  ILE A C   1 
ATOM   149  O  O   . ILE A 1 41  ? 118.295 139.961 104.892 1.00 64.73  ? 22  ILE A O   1 
ATOM   150  C  CB  . ILE A 1 41  ? 119.416 140.043 107.728 1.00 64.73  ? 22  ILE A CB  1 
ATOM   151  C  CG1 . ILE A 1 41  ? 119.551 139.688 109.210 1.00 64.73  ? 22  ILE A CG1 1 
ATOM   152  C  CG2 . ILE A 1 41  ? 119.888 141.462 107.482 1.00 64.73  ? 22  ILE A CG2 1 
ATOM   153  C  CD1 . ILE A 1 41  ? 120.958 139.841 109.743 1.00 64.73  ? 22  ILE A CD1 1 
ATOM   154  N  N   . PHE A 1 42  ? 116.983 141.551 105.817 1.00 63.55  ? 23  PHE A N   1 
ATOM   155  C  CA  . PHE A 1 42  ? 116.816 142.336 104.602 1.00 63.55  ? 23  PHE A CA  1 
ATOM   156  C  C   . PHE A 1 42  ? 117.662 143.593 104.739 1.00 63.55  ? 23  PHE A C   1 
ATOM   157  O  O   . PHE A 1 42  ? 117.412 144.416 105.627 1.00 63.55  ? 23  PHE A O   1 
ATOM   158  C  CB  . PHE A 1 42  ? 115.348 142.694 104.374 1.00 63.55  ? 23  PHE A CB  1 
ATOM   159  C  CG  . PHE A 1 42  ? 114.416 141.520 104.460 1.00 63.55  ? 23  PHE A CG  1 
ATOM   160  C  CD1 . PHE A 1 42  ? 114.125 140.767 103.338 1.00 63.55  ? 23  PHE A CD1 1 
ATOM   161  C  CD2 . PHE A 1 42  ? 113.828 141.173 105.664 1.00 63.55  ? 23  PHE A CD2 1 
ATOM   162  C  CE1 . PHE A 1 42  ? 113.266 139.689 103.415 1.00 63.55  ? 23  PHE A CE1 1 
ATOM   163  C  CE2 . PHE A 1 42  ? 112.970 140.096 105.747 1.00 63.55  ? 23  PHE A CE2 1 
ATOM   164  C  CZ  . PHE A 1 42  ? 112.689 139.353 104.621 1.00 63.55  ? 23  PHE A CZ  1 
ATOM   165  N  N   . LEU A 1 43  ? 118.662 143.738 103.873 1.00 67.06  ? 24  LEU A N   1 
ATOM   166  C  CA  . LEU A 1 43  ? 119.597 144.856 103.938 1.00 67.06  ? 24  LEU A CA  1 
ATOM   167  C  C   . LEU A 1 43  ? 119.553 145.604 102.613 1.00 67.06  ? 24  LEU A C   1 
ATOM   168  O  O   . LEU A 1 43  ? 120.042 145.103 101.597 1.00 67.06  ? 24  LEU A O   1 
ATOM   169  C  CB  . LEU A 1 43  ? 121.009 144.361 104.245 1.00 67.06  ? 24  LEU A CB  1 
ATOM   170  C  CG  . LEU A 1 43  ? 122.087 145.423 104.453 1.00 67.06  ? 24  LEU A CG  1 
ATOM   171  C  CD1 . LEU A 1 43  ? 121.840 146.188 105.739 1.00 67.06  ? 24  LEU A CD1 1 
ATOM   172  C  CD2 . LEU A 1 43  ? 123.464 144.784 104.465 1.00 67.06  ? 24  LEU A CD2 1 
ATOM   173  N  N   . VAL A 1 44  ? 118.969 146.797 102.624 1.00 69.97  ? 25  VAL A N   1 
ATOM   174  C  CA  . VAL A 1 44  ? 118.883 147.649 101.445 1.00 69.97  ? 25  VAL A CA  1 
ATOM   175  C  C   . VAL A 1 44  ? 119.874 148.785 101.635 1.00 69.97  ? 25  VAL A C   1 
ATOM   176  O  O   . VAL A 1 44  ? 119.742 149.580 102.574 1.00 69.97  ? 25  VAL A O   1 
ATOM   177  C  CB  . VAL A 1 44  ? 117.461 148.187 101.232 1.00 69.97  ? 25  VAL A CB  1 
ATOM   178  C  CG1 . VAL A 1 44  ? 117.418 149.097 100.016 1.00 69.97  ? 25  VAL A CG1 1 
ATOM   179  C  CG2 . VAL A 1 44  ? 116.477 147.042 101.084 1.00 69.97  ? 25  VAL A CG2 1 
ATOM   180  N  N   . VAL A 1 45  ? 120.865 148.861 100.745 1.00 70.82  ? 26  VAL A N   1 
ATOM   181  C  CA  . VAL A 1 45  ? 121.922 149.856 100.836 1.00 70.82  ? 26  VAL A CA  1 
ATOM   182  C  C   . VAL A 1 45  ? 121.998 150.621 99.523  1.00 70.82  ? 26  VAL A C   1 
ATOM   183  O  O   . VAL A 1 45  ? 121.542 150.158 98.475  1.00 70.82  ? 26  VAL A O   1 
ATOM   184  C  CB  . VAL A 1 45  ? 123.293 149.227 101.166 1.00 70.82  ? 26  VAL A CB  1 
ATOM   185  C  CG1 . VAL A 1 45  ? 123.188 148.328 102.385 1.00 70.82  ? 26  VAL A CG1 1 
ATOM   186  C  CG2 . VAL A 1 45  ? 123.822 148.450 99.975  1.00 70.82  ? 26  VAL A CG2 1 
ATOM   187  N  N   . THR A 1 46  ? 122.581 151.812 99.596  1.00 74.87  ? 27  THR A N   1 
ATOM   188  C  CA  . THR A 1 46  ? 122.773 152.666 98.436  1.00 74.87  ? 27  THR A CA  1 
ATOM   189  C  C   . THR A 1 46  ? 124.263 152.884 98.211  1.00 74.87  ? 27  THR A C   1 
ATOM   190  O  O   . THR A 1 46  ? 125.051 152.941 99.160  1.00 74.87  ? 27  THR A O   1 
ATOM   191  C  CB  . THR A 1 46  ? 122.056 154.016 98.600  1.00 74.87  ? 27  THR A CB  1 
ATOM   192  O  OG1 . THR A 1 46  ? 122.226 154.798 97.412  1.00 74.87  ? 27  THR A OG1 1 
ATOM   193  C  CG2 . THR A 1 46  ? 122.605 154.782 99.794  1.00 74.87  ? 27  THR A CG2 1 
ATOM   194  N  N   . ILE A 1 47  ? 124.645 152.987 96.944  1.00 79.62  ? 28  ILE A N   1 
ATOM   195  C  CA  . ILE A 1 47  ? 126.047 153.157 96.583  1.00 79.62  ? 28  ILE A CA  1 
ATOM   196  C  C   . ILE A 1 47  ? 126.409 154.632 96.684  1.00 79.62  ? 28  ILE A C   1 
ATOM   197  O  O   . ILE A 1 47  ? 125.726 155.494 96.117  1.00 79.62  ? 28  ILE A O   1 
ATOM   198  C  CB  . ILE A 1 47  ? 126.314 152.609 95.173  1.00 79.62  ? 28  ILE A CB  1 
ATOM   199  C  CG1 . ILE A 1 47  ? 126.489 151.091 95.220  1.00 79.62  ? 28  ILE A CG1 1 
ATOM   200  C  CG2 . ILE A 1 47  ? 127.550 153.252 94.573  1.00 79.62  ? 28  ILE A CG2 1 
ATOM   201  C  CD1 . ILE A 1 47  ? 126.675 150.459 93.862  1.00 79.62  ? 28  ILE A CD1 1 
ATOM   202  N  N   . ASN A 1 48  ? 127.482 154.926 97.413  1.00 84.34  ? 29  ASN A N   1 
ATOM   203  C  CA  . ASN A 1 48  ? 127.922 156.301 97.570  1.00 84.34  ? 29  ASN A CA  1 
ATOM   204  C  C   . ASN A 1 48  ? 128.434 156.846 96.237  1.00 84.34  ? 29  ASN A C   1 
ATOM   205  O  O   . ASN A 1 48  ? 128.942 156.091 95.404  1.00 84.34  ? 29  ASN A O   1 
ATOM   206  C  CB  . ASN A 1 48  ? 129.017 156.393 98.628  1.00 84.34  ? 29  ASN A CB  1 
ATOM   207  C  CG  . ASN A 1 48  ? 128.476 156.764 99.993  1.00 84.34  ? 29  ASN A CG  1 
ATOM   208  O  OD1 . ASN A 1 48  ? 127.624 157.643 100.118 1.00 84.34  ? 29  ASN A OD1 1 
ATOM   209  N  ND2 . ASN A 1 48  ? 128.967 156.091 101.027 1.00 84.34  ? 29  ASN A ND2 1 
ATOM   210  N  N   . PRO A 1 49  ? 128.301 158.152 96.007  1.00 89.54  ? 30  PRO A N   1 
ATOM   211  C  CA  . PRO A 1 49  ? 128.799 158.729 94.754  1.00 89.54  ? 30  PRO A CA  1 
ATOM   212  C  C   . PRO A 1 49  ? 130.306 158.570 94.626  1.00 89.54  ? 30  PRO A C   1 
ATOM   213  O  O   . PRO A 1 49  ? 131.045 158.591 95.614  1.00 89.54  ? 30  PRO A O   1 
ATOM   214  C  CB  . PRO A 1 49  ? 128.399 160.205 94.857  1.00 89.54  ? 30  PRO A CB  1 
ATOM   215  C  CG  . PRO A 1 49  ? 127.287 160.231 95.855  1.00 89.54  ? 30  PRO A CG  1 
ATOM   216  C  CD  . PRO A 1 49  ? 127.613 159.153 96.839  1.00 89.54  ? 30  PRO A CD  1 
ATOM   217  N  N   . GLY A 1 50  ? 130.757 158.407 93.385  1.00 95.56  ? 31  GLY A N   1 
ATOM   218  C  CA  . GLY A 1 50  ? 132.166 158.225 93.102  1.00 95.56  ? 31  GLY A CA  1 
ATOM   219  C  C   . GLY A 1 50  ? 132.459 156.917 92.397  1.00 95.56  ? 31  GLY A C   1 
ATOM   220  O  O   . GLY A 1 50  ? 131.734 155.933 92.572  1.00 95.56  ? 31  GLY A O   1 
ATOM   221  N  N   . LYS A 1 51  ? 133.524 156.895 91.593  1.00 94.86  ? 32  LYS A N   1 
ATOM   222  C  CA  . LYS A 1 51  ? 133.874 155.684 90.859  1.00 94.86  ? 32  LYS A CA  1 
ATOM   223  C  C   . LYS A 1 51  ? 134.495 154.631 91.771  1.00 94.86  ? 32  LYS A C   1 
ATOM   224  O  O   . LYS A 1 51  ? 134.351 153.429 91.516  1.00 94.86  ? 32  LYS A O   1 
ATOM   225  C  CB  . LYS A 1 51  ? 134.818 156.026 89.706  1.00 94.86  ? 32  LYS A CB  1 
ATOM   226  C  CG  . LYS A 1 51  ? 135.265 154.825 88.889  1.00 94.86  ? 32  LYS A CG  1 
ATOM   227  C  CD  . LYS A 1 51  ? 134.222 154.461 87.843  1.00 94.86  ? 32  LYS A CD  1 
ATOM   228  C  CE  . LYS A 1 51  ? 134.711 153.346 86.932  1.00 94.86  ? 32  LYS A CE  1 
ATOM   229  N  NZ  . LYS A 1 51  ? 133.608 152.419 86.553  1.00 94.86  ? 32  LYS A NZ  1 
ATOM   230  N  N   . ALA A 1 52  ? 135.180 155.059 92.834  1.00 93.19  ? 33  ALA A N   1 
ATOM   231  C  CA  . ALA A 1 52  ? 135.829 154.112 93.735  1.00 93.19  ? 33  ALA A CA  1 
ATOM   232  C  C   . ALA A 1 52  ? 134.814 153.202 94.416  1.00 93.19  ? 33  ALA A C   1 
ATOM   233  O  O   . ALA A 1 52  ? 135.064 152.002 94.588  1.00 93.19  ? 33  ALA A O   1 
ATOM   234  C  CB  . ALA A 1 52  ? 136.659 154.862 94.775  1.00 93.19  ? 33  ALA A CB  1 
ATOM   235  N  N   . ALA A 1 53  ? 133.668 153.753 94.822  1.00 90.26  ? 34  ALA A N   1 
ATOM   236  C  CA  . ALA A 1 53  ? 132.631 152.924 95.427  1.00 90.26  ? 34  ALA A CA  1 
ATOM   237  C  C   . ALA A 1 53  ? 132.111 151.888 94.440  1.00 90.26  ? 34  ALA A C   1 
ATOM   238  O  O   . ALA A 1 53  ? 131.888 150.726 94.804  1.00 90.26  ? 34  ALA A O   1 
ATOM   239  C  CB  . ALA A 1 53  ? 131.489 153.802 95.938  1.00 90.26  ? 34  ALA A CB  1 
ATOM   240  N  N   . GLU A 1 54  ? 131.916 152.289 93.181  1.00 91.55  ? 35  GLU A N   1 
ATOM   241  C  CA  . GLU A 1 54  ? 131.476 151.344 92.161  1.00 91.55  ? 35  GLU A CA  1 
ATOM   242  C  C   . GLU A 1 54  ? 132.507 150.242 91.957  1.00 91.55  ? 35  GLU A C   1 
ATOM   243  O  O   . GLU A 1 54  ? 132.150 149.066 91.820  1.00 91.55  ? 35  GLU A O   1 
ATOM   244  C  CB  . GLU A 1 54  ? 131.206 152.077 90.847  1.00 91.55  ? 35  GLU A CB  1 
ATOM   245  C  CG  . GLU A 1 54  ? 130.084 153.096 90.924  1.00 91.55  ? 35  GLU A CG  1 
ATOM   246  C  CD  . GLU A 1 54  ? 130.211 154.180 89.873  1.00 91.55  ? 35  GLU A CD  1 
ATOM   247  O  OE1 . GLU A 1 54  ? 131.097 154.061 89.000  1.00 91.55  ? 35  GLU A OE1 1 
ATOM   248  O  OE2 . GLU A 1 54  ? 129.428 155.151 89.918  1.00 91.55  ? 35  GLU A OE2 1 
ATOM   249  N  N   . VAL A 1 55  ? 133.792 150.604 91.936  1.00 90.88  ? 36  VAL A N   1 
ATOM   250  C  CA  . VAL A 1 55  ? 134.847 149.608 91.768  1.00 90.88  ? 36  VAL A CA  1 
ATOM   251  C  C   . VAL A 1 55  ? 134.852 148.634 92.940  1.00 90.88  ? 36  VAL A C   1 
ATOM   252  O  O   . VAL A 1 55  ? 134.993 147.419 92.756  1.00 90.88  ? 36  VAL A O   1 
ATOM   253  C  CB  . VAL A 1 55  ? 136.213 150.298 91.597  1.00 90.88  ? 36  VAL A CB  1 
ATOM   254  C  CG1 . VAL A 1 55  ? 137.334 149.273 91.621  1.00 90.88  ? 36  VAL A CG1 1 
ATOM   255  C  CG2 . VAL A 1 55  ? 136.245 151.092 90.301  1.00 90.88  ? 36  VAL A CG2 1 
ATOM   256  N  N   . ALA A 1 56  ? 134.702 149.150 94.162  1.00 89.01  ? 37  ALA A N   1 
ATOM   257  C  CA  . ALA A 1 56  ? 134.691 148.282 95.336  1.00 89.01  ? 37  ALA A CA  1 
ATOM   258  C  C   . ALA A 1 56  ? 133.505 147.325 95.307  1.00 89.01  ? 37  ALA A C   1 
ATOM   259  O  O   . ALA A 1 56  ? 133.648 146.134 95.615  1.00 89.01  ? 37  ALA A O   1 
ATOM   260  C  CB  . ALA A 1 56  ? 134.673 149.123 96.612  1.00 89.01  ? 37  ALA A CB  1 
ATOM   261  N  N   . VAL A 1 57  ? 132.322 147.827 94.942  1.00 87.51  ? 38  VAL A N   1 
ATOM   262  C  CA  . VAL A 1 57  ? 131.146 146.964 94.859  1.00 87.51  ? 38  VAL A CA  1 
ATOM   263  C  C   . VAL A 1 57  ? 131.338 145.902 93.783  1.00 87.51  ? 38  VAL A C   1 
ATOM   264  O  O   . VAL A 1 57  ? 131.007 144.725 93.983  1.00 87.51  ? 38  VAL A O   1 
ATOM   265  C  CB  . VAL A 1 57  ? 129.880 147.804 94.608  1.00 87.51  ? 38  VAL A CB  1 
ATOM   266  C  CG1 . VAL A 1 57  ? 128.683 146.900 94.373  1.00 87.51  ? 38  VAL A CG1 1 
ATOM   267  C  CG2 . VAL A 1 57  ? 129.619 148.725 95.786  1.00 87.51  ? 38  VAL A CG2 1 
ATOM   268  N  N   . ARG A 1 58  ? 131.880 146.296 92.628  1.00 89.64  ? 39  ARG A N   1 
ATOM   269  C  CA  . ARG A 1 58  ? 132.098 145.341 91.549  1.00 89.64  ? 39  ARG A CA  1 
ATOM   270  C  C   . ARG A 1 58  ? 133.111 144.277 91.951  1.00 89.64  ? 39  ARG A C   1 
ATOM   271  O  O   . ARG A 1 58  ? 132.988 143.111 91.557  1.00 89.64  ? 39  ARG A O   1 
ATOM   272  C  CB  . ARG A 1 58  ? 132.554 146.078 90.290  1.00 89.64  ? 39  ARG A CB  1 
ATOM   273  C  CG  . ARG A 1 58  ? 131.850 145.628 89.026  1.00 89.64  ? 39  ARG A CG  1 
ATOM   274  C  CD  . ARG A 1 58  ? 132.158 146.537 87.845  1.00 89.64  ? 39  ARG A CD  1 
ATOM   275  N  NE  . ARG A 1 58  ? 132.006 147.949 88.174  1.00 89.64  ? 39  ARG A NE  1 
ATOM   276  C  CZ  . ARG A 1 58  ? 133.007 148.815 88.240  1.00 89.64  ? 39  ARG A CZ  1 
ATOM   277  N  NH1 . ARG A 1 58  ? 134.256 148.447 88.008  1.00 89.64  ? 39  ARG A NH1 1 
ATOM   278  N  NH2 . ARG A 1 58  ? 132.749 150.084 88.545  1.00 89.64  ? 39  ARG A NH2 1 
ATOM   279  N  N   . ALA A 1 59  ? 134.122 144.659 92.734  1.00 90.52  ? 40  ALA A N   1 
ATOM   280  C  CA  . ALA A 1 59  ? 135.085 143.680 93.227  1.00 90.52  ? 40  ALA A CA  1 
ATOM   281  C  C   . ALA A 1 59  ? 134.439 142.718 94.216  1.00 90.52  ? 40  ALA A C   1 
ATOM   282  O  O   . ALA A 1 59  ? 134.669 141.505 94.151  1.00 90.52  ? 40  ALA A O   1 
ATOM   283  C  CB  . ALA A 1 59  ? 136.277 144.390 93.867  1.00 90.52  ? 40  ALA A CB  1 
ATOM   284  N  N   . HIS A 1 60  ? 133.629 143.240 95.141  1.00 88.74  ? 41  HIS A N   1 
ATOM   285  C  CA  . HIS A 1 60  ? 132.973 142.387 96.127  1.00 88.74  ? 41  HIS A CA  1 
ATOM   286  C  C   . HIS A 1 60  ? 131.922 141.480 95.495  1.00 88.74  ? 41  HIS A C   1 
ATOM   287  O  O   . HIS A 1 60  ? 131.566 140.448 96.083  1.00 88.74  ? 41  HIS A O   1 
ATOM   288  C  CB  . HIS A 1 60  ? 132.345 143.254 97.222  1.00 88.74  ? 41  HIS A CB  1 
ATOM   289  C  CG  . HIS A 1 60  ? 131.296 142.552 98.026  1.00 88.74  ? 41  HIS A CG  1 
ATOM   290  N  ND1 . HIS A 1 60  ? 129.948 142.780 97.852  1.00 88.74  ? 41  HIS A ND1 1 
ATOM   291  C  CD2 . HIS A 1 60  ? 131.397 141.626 99.009  1.00 88.74  ? 41  HIS A CD2 1 
ATOM   292  C  CE1 . HIS A 1 60  ? 129.264 142.024 98.692  1.00 88.74  ? 41  HIS A CE1 1 
ATOM   293  N  NE2 . HIS A 1 60  ? 130.119 141.315 99.406  1.00 88.74  ? 41  HIS A NE2 1 
ATOM   294  N  N   . CYS A 1 61  ? 131.421 141.846 94.313  1.00 90.27  ? 42  CYS A N   1 
ATOM   295  C  CA  . CYS A 1 61  ? 130.427 141.018 93.635  1.00 90.27  ? 42  CYS A CA  1 
ATOM   296  C  C   . CYS A 1 61  ? 130.960 139.618 93.357  1.00 90.27  ? 42  CYS A C   1 
ATOM   297  O  O   . CYS A 1 61  ? 130.249 138.625 93.552  1.00 90.27  ? 42  CYS A O   1 
ATOM   298  C  CB  . CYS A 1 61  ? 129.993 141.689 92.333  1.00 90.27  ? 42  CYS A CB  1 
ATOM   299  S  SG  . CYS A 1 61  ? 128.773 143.001 92.534  1.00 90.27  ? 42  CYS A SG  1 
ATOM   300  N  N   . SER A 1 62  ? 132.209 139.515 92.902  1.00 89.26  ? 43  SER A N   1 
ATOM   301  C  CA  . SER A 1 62  ? 132.781 138.221 92.551  1.00 89.26  ? 43  SER A CA  1 
ATOM   302  C  C   . SER A 1 62  ? 133.165 137.387 93.766  1.00 89.26  ? 43  SER A C   1 
ATOM   303  O  O   . SER A 1 62  ? 133.318 136.168 93.638  1.00 89.26  ? 43  SER A O   1 
ATOM   304  C  CB  . SER A 1 62  ? 134.007 138.416 91.657  1.00 89.26  ? 43  SER A CB  1 
ATOM   305  O  OG  . SER A 1 62  ? 135.101 138.923 92.398  1.00 89.26  ? 43  SER A OG  1 
ATOM   306  N  N   . ILE A 1 63  ? 133.321 138.007 94.938  1.00 86.73  ? 44  ILE A N   1 
ATOM   307  C  CA  . ILE A 1 63  ? 133.699 137.293 96.153  1.00 86.73  ? 44  ILE A CA  1 
ATOM   308  C  C   . ILE A 1 63  ? 132.512 137.054 97.076  1.00 86.73  ? 44  ILE A C   1 
ATOM   309  O  O   . ILE A 1 63  ? 132.667 136.409 98.126  1.00 86.73  ? 44  ILE A O   1 
ATOM   310  C  CB  . ILE A 1 63  ? 134.824 138.044 96.896  1.00 86.73  ? 44  ILE A CB  1 
ATOM   311  C  CG1 . ILE A 1 63  ? 135.708 137.064 97.669  1.00 86.73  ? 44  ILE A CG1 1 
ATOM   312  C  CG2 . ILE A 1 63  ? 134.249 139.117 97.813  1.00 86.73  ? 44  ILE A CG2 1 
ATOM   313  C  CD1 . ILE A 1 63  ? 136.454 136.091 96.784  1.00 86.73  ? 44  ILE A CD1 1 
ATOM   314  N  N   . LEU A 1 64  ? 131.333 137.572 96.723  1.00 85.07  ? 45  LEU A N   1 
ATOM   315  C  CA  . LEU A 1 64  ? 130.130 137.300 97.507  1.00 85.07  ? 45  LEU A CA  1 
ATOM   316  C  C   . LEU A 1 64  ? 129.876 135.803 97.666  1.00 85.07  ? 45  LEU A C   1 
ATOM   317  O  O   . LEU A 1 64  ? 129.519 135.344 98.756  1.00 85.07  ? 45  LEU A O   1 
ATOM   318  C  CB  . LEU A 1 64  ? 128.924 137.978 96.858  1.00 85.07  ? 45  LEU A CB  1 
ATOM   319  C  CG  . LEU A 1 64  ? 127.546 137.620 97.418  1.00 85.07  ? 45  LEU A CG  1 
ATOM   320  C  CD1 . LEU A 1 64  ? 127.435 138.025 98.877  1.00 85.07  ? 45  LEU A CD1 1 
ATOM   321  C  CD2 . LEU A 1 64  ? 126.449 138.271 96.593  1.00 85.07  ? 45  LEU A CD2 1 
ATOM   322  N  N   . SER A 1 65  ? 130.039 135.027 96.591  1.00 82.47  ? 46  SER A N   1 
ATOM   323  C  CA  . SER A 1 65  ? 129.769 133.592 96.674  1.00 82.47  ? 46  SER A CA  1 
ATOM   324  C  C   . SER A 1 65  ? 130.750 132.890 97.608  1.00 82.47  ? 46  SER A C   1 
ATOM   325  O  O   . SER A 1 65  ? 130.356 132.019 98.396  1.00 82.47  ? 46  SER A O   1 
ATOM   326  C  CB  . SER A 1 65  ? 129.816 132.968 95.280  1.00 82.47  ? 46  SER A CB  1 
ATOM   327  O  OG  . SER A 1 65  ? 131.137 132.968 94.768  1.00 82.47  ? 46  SER A OG  1 
ATOM   328  N  N   . SER A 1 66  ? 132.033 133.252 97.528  1.00 83.06  ? 47  SER A N   1 
ATOM   329  C  CA  . SER A 1 66  ? 133.022 132.666 98.425  1.00 83.06  ? 47  SER A CA  1 
ATOM   330  C  C   . SER A 1 66  ? 132.726 133.027 99.873  1.00 83.06  ? 47  SER A C   1 
ATOM   331  O  O   . SER A 1 66  ? 132.855 132.184 100.771 1.00 83.06  ? 47  SER A O   1 
ATOM   332  C  CB  . SER A 1 66  ? 134.425 133.125 98.031  1.00 83.06  ? 47  SER A CB  1 
ATOM   333  O  OG  . SER A 1 66  ? 135.412 132.451 98.792  1.00 83.06  ? 47  SER A OG  1 
ATOM   334  N  N   . LEU A 1 67  ? 132.327 134.277 100.120 1.00 81.44  ? 48  LEU A N   1 
ATOM   335  C  CA  . LEU A 1 67  ? 131.923 134.672 101.466 1.00 81.44  ? 48  LEU A CA  1 
ATOM   336  C  C   . LEU A 1 67  ? 130.740 133.844 101.948 1.00 81.44  ? 48  LEU A C   1 
ATOM   337  O  O   . LEU A 1 67  ? 130.711 133.404 103.103 1.00 81.44  ? 48  LEU A O   1 
ATOM   338  C  CB  . LEU A 1 67  ? 131.577 136.160 101.497 1.00 81.44  ? 48  LEU A CB  1 
ATOM   339  C  CG  . LEU A 1 67  ? 132.645 137.129 102.004 1.00 81.44  ? 48  LEU A CG  1 
ATOM   340  C  CD1 . LEU A 1 67  ? 134.021 136.763 101.469 1.00 81.44  ? 48  LEU A CD1 1 
ATOM   341  C  CD2 . LEU A 1 67  ? 132.278 138.550 101.620 1.00 81.44  ? 48  LEU A CD2 1 
ATOM   342  N  N   . ILE A 1 68  ? 129.752 133.632 101.078 1.00 78.24  ? 49  ILE A N   1 
ATOM   343  C  CA  . ILE A 1 68  ? 128.564 132.866 101.450 1.00 78.24  ? 49  ILE A CA  1 
ATOM   344  C  C   . ILE A 1 68  ? 128.961 131.454 101.861 1.00 78.24  ? 49  ILE A C   1 
ATOM   345  O  O   . ILE A 1 68  ? 128.555 130.950 102.919 1.00 78.24  ? 49  ILE A O   1 
ATOM   346  C  CB  . ILE A 1 68  ? 127.564 132.845 100.281 1.00 78.24  ? 49  ILE A CB  1 
ATOM   347  C  CG1 . ILE A 1 68  ? 126.650 134.065 100.322 1.00 78.24  ? 49  ILE A CG1 1 
ATOM   348  C  CG2 . ILE A 1 68  ? 126.719 131.580 100.317 1.00 78.24  ? 49  ILE A CG2 1 
ATOM   349  C  CD1 . ILE A 1 68  ? 125.896 134.272 99.028  1.00 78.24  ? 49  ILE A CD1 1 
ATOM   350  N  N   . ARG A 1 69  ? 129.796 130.812 101.039 1.00 81.65  ? 50  ARG A N   1 
ATOM   351  C  CA  . ARG A 1 69  ? 130.216 129.444 101.325 1.00 81.65  ? 50  ARG A CA  1 
ATOM   352  C  C   . ARG A 1 69  ? 131.000 129.382 102.628 1.00 81.65  ? 50  ARG A C   1 
ATOM   353  O  O   . ARG A 1 69  ? 130.751 128.514 103.474 1.00 81.65  ? 50  ARG A O   1 
ATOM   354  C  CB  . ARG A 1 69  ? 131.045 128.896 100.164 1.00 81.65  ? 50  ARG A CB  1 
ATOM   355  C  CG  . ARG A 1 69  ? 130.215 128.298 99.041  1.00 81.65  ? 50  ARG A CG  1 
ATOM   356  C  CD  . ARG A 1 69  ? 130.902 127.089 98.431  1.00 81.65  ? 50  ARG A CD  1 
ATOM   357  N  NE  . ARG A 1 69  ? 132.053 127.465 97.618  1.00 81.65  ? 50  ARG A NE  1 
ATOM   358  C  CZ  . ARG A 1 69  ? 131.976 128.047 96.429  1.00 81.65  ? 50  ARG A CZ  1 
ATOM   359  N  NH1 . ARG A 1 69  ? 130.811 128.322 95.866  1.00 81.65  ? 50  ARG A NH1 1 
ATOM   360  N  NH2 . ARG A 1 69  ? 133.098 128.357 95.785  1.00 81.65  ? 50  ARG A NH2 1 
ATOM   361  N  N   . GLY A 1 70  ? 131.944 130.307 102.815 1.00 80.22  ? 51  GLY A N   1 
ATOM   362  C  CA  . GLY A 1 70  ? 132.749 130.281 104.024 1.00 80.22  ? 51  GLY A CA  1 
ATOM   363  C  C   . GLY A 1 70  ? 131.903 130.472 105.267 1.00 80.22  ? 51  GLY A C   1 
ATOM   364  O  O   . GLY A 1 70  ? 132.051 129.748 106.254 1.00 80.22  ? 51  GLY A O   1 
ATOM   365  N  N   . VAL A 1 71  ? 131.003 131.458 105.235 1.00 78.41  ? 52  VAL A N   1 
ATOM   366  C  CA  . VAL A 1 71  ? 130.218 131.792 106.415 1.00 78.41  ? 52  VAL A CA  1 
ATOM   367  C  C   . VAL A 1 71  ? 129.233 130.679 106.756 1.00 78.41  ? 52  VAL A C   1 
ATOM   368  O  O   . VAL A 1 71  ? 128.988 130.405 107.937 1.00 78.41  ? 52  VAL A O   1 
ATOM   369  C  CB  . VAL A 1 71  ? 129.501 133.140 106.214 1.00 78.41  ? 52  VAL A CB  1 
ATOM   370  C  CG1 . VAL A 1 71  ? 128.504 133.393 107.332 1.00 78.41  ? 52  VAL A CG1 1 
ATOM   371  C  CG2 . VAL A 1 71  ? 130.513 134.269 106.156 1.00 78.41  ? 52  VAL A CG2 1 
ATOM   372  N  N   . GLY A 1 72  ? 128.675 129.994 105.755 1.00 79.51  ? 53  GLY A N   1 
ATOM   373  C  CA  . GLY A 1 72  ? 127.658 129.013 106.070 1.00 79.51  ? 53  GLY A CA  1 
ATOM   374  C  C   . GLY A 1 72  ? 128.047 127.554 106.013 1.00 79.51  ? 53  GLY A C   1 
ATOM   375  O  O   . GLY A 1 72  ? 127.202 126.696 106.286 1.00 79.51  ? 53  GLY A O   1 
ATOM   376  N  N   . PHE A 1 73  ? 129.294 127.237 105.667 1.00 84.10  ? 54  PHE A N   1 
ATOM   377  C  CA  . PHE A 1 73  ? 129.731 125.845 105.669 1.00 84.10  ? 54  PHE A CA  1 
ATOM   378  C  C   . PHE A 1 73  ? 129.947 125.326 107.090 1.00 84.10  ? 54  PHE A C   1 
ATOM   379  O  O   . PHE A 1 73  ? 129.716 124.142 107.360 1.00 84.10  ? 54  PHE A O   1 
ATOM   380  C  CB  . PHE A 1 73  ? 131.010 125.694 104.841 1.00 84.10  ? 54  PHE A CB  1 
ATOM   381  C  CG  . PHE A 1 73  ? 131.587 124.300 104.846 1.00 84.10  ? 54  PHE A CG  1 
ATOM   382  C  CD1 . PHE A 1 73  ? 130.760 123.186 104.842 1.00 84.10  ? 54  PHE A CD1 1 
ATOM   383  C  CD2 . PHE A 1 73  ? 132.954 124.104 104.868 1.00 84.10  ? 54  PHE A CD2 1 
ATOM   384  C  CE1 . PHE A 1 73  ? 131.287 121.910 104.849 1.00 84.10  ? 54  PHE A CE1 1 
ATOM   385  C  CE2 . PHE A 1 73  ? 133.488 122.829 104.875 1.00 84.10  ? 54  PHE A CE2 1 
ATOM   386  C  CZ  . PHE A 1 73  ? 132.653 121.732 104.866 1.00 84.10  ? 54  PHE A CZ  1 
ATOM   387  N  N   . ARG A 1 74  ? 130.349 126.202 108.017 1.00 88.89  ? 55  ARG A N   1 
ATOM   388  C  CA  . ARG A 1 74  ? 130.656 125.765 109.377 1.00 88.89  ? 55  ARG A CA  1 
ATOM   389  C  C   . ARG A 1 74  ? 129.446 125.242 110.136 1.00 88.89  ? 55  ARG A C   1 
ATOM   390  O  O   . ARG A 1 74  ? 129.581 124.311 110.938 1.00 88.89  ? 55  ARG A O   1 
ATOM   391  C  CB  . ARG A 1 74  ? 131.164 126.947 110.196 1.00 88.89  ? 55  ARG A CB  1 
ATOM   392  C  CG  . ARG A 1 74  ? 132.084 126.600 111.334 1.00 88.89  ? 55  ARG A CG  1 
ATOM   393  C  CD  . ARG A 1 74  ? 132.690 127.845 111.989 1.00 88.89  ? 55  ARG A CD  1 
ATOM   394  N  NE  . ARG A 1 74  ? 133.397 128.740 111.084 1.00 88.89  ? 55  ARG A NE  1 
ATOM   395  C  CZ  . ARG A 1 74  ? 132.818 129.763 110.468 1.00 88.89  ? 55  ARG A CZ  1 
ATOM   396  N  NH1 . ARG A 1 74  ? 131.538 130.045 110.648 1.00 88.89  ? 55  ARG A NH1 1 
ATOM   397  N  NH2 . ARG A 1 74  ? 133.539 130.529 109.660 1.00 88.89  ? 55  ARG A NH2 1 
ATOM   398  N  N   . ILE A 1 75  ? 128.269 125.803 109.906 1.00 85.80  ? 56  ILE A N   1 
ATOM   399  C  CA  . ILE A 1 75  ? 127.066 125.398 110.627 1.00 85.80  ? 56  ILE A CA  1 
ATOM   400  C  C   . ILE A 1 75  ? 126.257 124.493 109.707 1.00 85.80  ? 56  ILE A C   1 
ATOM   401  O  O   . ILE A 1 75  ? 125.485 124.962 108.867 1.00 85.80  ? 56  ILE A O   1 
ATOM   402  C  CB  . ILE A 1 75  ? 126.264 126.602 111.113 1.00 85.80  ? 56  ILE A CB  1 
ATOM   403  C  CG1 . ILE A 1 75  ? 127.097 127.416 112.103 1.00 85.80  ? 56  ILE A CG1 1 
ATOM   404  C  CG2 . ILE A 1 75  ? 124.978 126.148 111.781 1.00 85.80  ? 56  ILE A CG2 1 
ATOM   405  C  CD1 . ILE A 1 75  ? 127.564 126.625 113.303 1.00 85.80  ? 56  ILE A CD1 1 
ATOM   406  N  N   . SER A 1 76  ? 126.477 123.180 109.824 1.00 90.46  ? 57  SER A N   1 
ATOM   407  C  CA  . SER A 1 76  ? 125.743 122.229 108.999 1.00 90.46  ? 57  SER A CA  1 
ATOM   408  C  C   . SER A 1 76  ? 124.247 122.472 109.160 1.00 90.46  ? 57  SER A C   1 
ATOM   409  O  O   . SER A 1 76  ? 123.824 123.083 110.147 1.00 90.46  ? 57  SER A O   1 
ATOM   410  C  CB  . SER A 1 76  ? 126.098 120.790 109.377 1.00 90.46  ? 57  SER A CB  1 
ATOM   411  O  OG  . SER A 1 76  ? 125.650 120.487 110.687 1.00 90.46  ? 57  SER A OG  1 
ATOM   412  N  N   . ASP A 1 77  ? 123.442 121.948 108.234 1.00 92.58  ? 58  ASP A N   1 
ATOM   413  C  CA  . ASP A 1 77  ? 121.991 122.128 108.219 1.00 92.58  ? 58  ASP A CA  1 
ATOM   414  C  C   . ASP A 1 77  ? 121.575 123.541 108.629 1.00 92.58  ? 58  ASP A C   1 
ATOM   415  O  O   . ASP A 1 77  ? 120.485 123.746 109.173 1.00 92.58  ? 58  ASP A O   1 
ATOM   416  C  CB  . ASP A 1 77  ? 121.327 121.062 109.108 1.00 92.58  ? 58  ASP A CB  1 
ATOM   417  C  CG  . ASP A 1 77  ? 121.539 121.301 110.601 1.00 92.58  ? 58  ASP A CG  1 
ATOM   418  O  OD1 . ASP A 1 77  ? 122.351 120.564 111.199 1.00 92.58  ? 58  ASP A OD1 1 
ATOM   419  O  OD2 . ASP A 1 77  ? 120.880 122.182 111.192 1.00 92.58  ? 58  ASP A OD2 1 
ATOM   420  N  N   . GLY A 1 78  ? 122.413 124.532 108.308 1.00 85.76  ? 59  GLY A N   1 
ATOM   421  C  CA  . GLY A 1 78  ? 122.086 125.917 108.590 1.00 85.76  ? 59  GLY A CA  1 
ATOM   422  C  C   . GLY A 1 78  ? 121.209 126.571 107.551 1.00 85.76  ? 59  GLY A C   1 
ATOM   423  O  O   . GLY A 1 78  ? 120.551 127.572 107.851 1.00 85.76  ? 59  GLY A O   1 
ATOM   424  N  N   . GLY A 1 79  ? 121.184 126.024 106.340 1.00 81.47  ? 60  GLY A N   1 
ATOM   425  C  CA  . GLY A 1 79  ? 120.358 126.569 105.278 1.00 81.47  ? 60  GLY A CA  1 
ATOM   426  C  C   . GLY A 1 79  ? 120.667 128.011 104.945 1.00 81.47  ? 60  GLY A C   1 
ATOM   427  O  O   . GLY A 1 79  ? 119.748 128.787 104.651 1.00 81.47  ? 60  GLY A O   1 
ATOM   428  N  N   . LEU A 1 80  ? 121.942 128.394 104.982 1.00 73.52  ? 61  LEU A N   1 
ATOM   429  C  CA  . LEU A 1 80  ? 122.300 129.784 104.742 1.00 73.52  ? 61  LEU A CA  1 
ATOM   430  C  C   . LEU A 1 80  ? 122.264 130.063 103.248 1.00 73.52  ? 61  LEU A C   1 
ATOM   431  O  O   . LEU A 1 80  ? 122.834 129.312 102.450 1.00 73.52  ? 61  LEU A O   1 
ATOM   432  C  CB  . LEU A 1 80  ? 123.681 130.109 105.308 1.00 73.52  ? 61  LEU A CB  1 
ATOM   433  C  CG  . LEU A 1 80  ? 124.159 131.519 104.944 1.00 73.52  ? 61  LEU A CG  1 
ATOM   434  C  CD1 . LEU A 1 80  ? 123.244 132.563 105.556 1.00 73.52  ? 61  LEU A CD1 1 
ATOM   435  C  CD2 . LEU A 1 80  ? 125.589 131.760 105.378 1.00 73.52  ? 61  LEU A CD2 1 
ATOM   436  N  N   . SER A 1 81  ? 121.590 131.144 102.876 1.00 74.82  ? 62  SER A N   1 
ATOM   437  C  CA  . SER A 1 81  ? 121.518 131.584 101.495 1.00 74.82  ? 62  SER A CA  1 
ATOM   438  C  C   . SER A 1 81  ? 121.453 133.100 101.478 1.00 74.82  ? 62  SER A C   1 
ATOM   439  O  O   . SER A 1 81  ? 121.021 133.726 102.448 1.00 74.82  ? 62  SER A O   1 
ATOM   440  C  CB  . SER A 1 81  ? 120.303 130.986 100.779 1.00 74.82  ? 62  SER A CB  1 
ATOM   441  O  OG  . SER A 1 81  ? 119.096 131.522 101.292 1.00 74.82  ? 62  SER A OG  1 
ATOM   442  N  N   . CYS A 1 82  ? 121.899 133.689 100.375 1.00 72.86  ? 63  CYS A N   1 
ATOM   443  C  CA  . CYS A 1 82  ? 121.871 135.135 100.230 1.00 72.86  ? 63  CYS A CA  1 
ATOM   444  C  C   . CYS A 1 82  ? 121.557 135.465 98.783  1.00 72.86  ? 63  CYS A C   1 
ATOM   445  O  O   . CYS A 1 82  ? 122.191 134.935 97.866  1.00 72.86  ? 63  CYS A O   1 
ATOM   446  C  CB  . CYS A 1 82  ? 123.200 135.769 100.652 1.00 72.86  ? 63  CYS A CB  1 
ATOM   447  S  SG  . CYS A 1 82  ? 123.293 137.554 100.400 1.00 72.86  ? 63  CYS A SG  1 
ATOM   448  N  N   . VAL A 1 83  ? 120.580 136.343 98.590  1.00 71.47  ? 64  VAL A N   1 
ATOM   449  C  CA  . VAL A 1 83  ? 120.171 136.807 97.272  1.00 71.47  ? 64  VAL A CA  1 
ATOM   450  C  C   . VAL A 1 83  ? 120.552 138.273 97.158  1.00 71.47  ? 64  VAL A C   1 
ATOM   451  O  O   . VAL A 1 83  ? 120.164 139.090 98.004  1.00 71.47  ? 64  VAL A O   1 
ATOM   452  C  CB  . VAL A 1 83  ? 118.666 136.606 97.044  1.00 71.47  ? 64  VAL A CB  1 
ATOM   453  C  CG1 . VAL A 1 83  ? 118.242 137.236 95.731  1.00 71.47  ? 64  VAL A CG1 1 
ATOM   454  C  CG2 . VAL A 1 83  ? 118.323 135.127 97.067  1.00 71.47  ? 64  VAL A CG2 1 
ATOM   455  N  N   . MET A 1 84  ? 121.317 138.605 96.125  1.00 73.60  ? 65  MET A N   1 
ATOM   456  C  CA  . MET A 1 84  ? 121.728 139.976 95.868  1.00 73.60  ? 65  MET A CA  1 
ATOM   457  C  C   . MET A 1 84  ? 120.953 140.506 94.672  1.00 73.60  ? 65  MET A C   1 
ATOM   458  O  O   . MET A 1 84  ? 120.920 139.869 93.614  1.00 73.60  ? 65  MET A O   1 
ATOM   459  C  CB  . MET A 1 84  ? 123.234 140.066 95.610  1.00 73.60  ? 65  MET A CB  1 
ATOM   460  C  CG  . MET A 1 84  ? 123.622 141.199 94.679  1.00 73.60  ? 65  MET A CG  1 
ATOM   461  S  SD  . MET A 1 84  ? 125.378 141.586 94.699  1.00 73.60  ? 65  MET A SD  1 
ATOM   462  C  CE  . MET A 1 84  ? 125.416 142.938 93.528  1.00 73.60  ? 65  MET A CE  1 
ATOM   463  N  N   . GLY A 1 85  ? 120.328 141.660 94.849  1.00 71.08  ? 66  GLY A N   1 
ATOM   464  C  CA  . GLY A 1 85  ? 119.558 142.279 93.792  1.00 71.08  ? 66  GLY A CA  1 
ATOM   465  C  C   . GLY A 1 85  ? 120.028 143.695 93.541  1.00 71.08  ? 66  GLY A C   1 
ATOM   466  O  O   . GLY A 1 85  ? 120.467 144.396 94.450  1.00 71.08  ? 66  GLY A O   1 
ATOM   467  N  N   . VAL A 1 86  ? 119.922 144.111 92.283  1.00 72.07  ? 67  VAL A N   1 
ATOM   468  C  CA  . VAL A 1 86  ? 120.367 145.428 91.847  1.00 72.07  ? 67  VAL A CA  1 
ATOM   469  C  C   . VAL A 1 86  ? 119.175 146.164 91.256  1.00 72.07  ? 67  VAL A C   1 
ATOM   470  O  O   . VAL A 1 86  ? 118.460 145.617 90.408  1.00 72.07  ? 67  VAL A O   1 
ATOM   471  C  CB  . VAL A 1 86  ? 121.509 145.329 90.819  1.00 72.07  ? 67  VAL A CB  1 
ATOM   472  C  CG1 . VAL A 1 86  ? 122.090 146.699 90.545  1.00 72.07  ? 67  VAL A CG1 1 
ATOM   473  C  CG2 . VAL A 1 86  ? 122.586 144.375 91.311  1.00 72.07  ? 67  VAL A CG2 1 
ATOM   474  N  N   . SER A 1 87  ? 118.961 147.398 91.703  1.00 77.74  ? 68  SER A N   1 
ATOM   475  C  CA  . SER A 1 87  ? 117.862 148.208 91.205  1.00 77.74  ? 68  SER A CA  1 
ATOM   476  C  C   . SER A 1 87  ? 118.255 148.863 89.883  1.00 77.74  ? 68  SER A C   1 
ATOM   477  O  O   . SER A 1 87  ? 119.333 148.622 89.335  1.00 77.74  ? 68  SER A O   1 
ATOM   478  C  CB  . SER A 1 87  ? 117.459 149.254 92.239  1.00 77.74  ? 68  SER A CB  1 
ATOM   479  O  OG  . SER A 1 87  ? 118.384 150.326 92.263  1.00 77.74  ? 68  SER A OG  1 
ATOM   480  N  N   . GLU A 1 88  ? 117.362 149.705 89.361  1.00 85.69  ? 69  GLU A N   1 
ATOM   481  C  CA  . GLU A 1 88  ? 117.625 150.358 88.083  1.00 85.69  ? 69  GLU A CA  1 
ATOM   482  C  C   . GLU A 1 88  ? 118.793 151.332 88.195  1.00 85.69  ? 69  GLU A C   1 
ATOM   483  O  O   . GLU A 1 88  ? 119.700 151.328 87.355  1.00 85.69  ? 69  GLU A O   1 
ATOM   484  C  CB  . GLU A 1 88  ? 116.363 151.068 87.588  1.00 85.69  ? 69  GLU A CB  1 
ATOM   485  C  CG  . GLU A 1 88  ? 116.595 152.076 86.471  1.00 85.69  ? 69  GLU A CG  1 
ATOM   486  C  CD  . GLU A 1 88  ? 116.795 153.488 86.984  1.00 85.69  ? 69  GLU A CD  1 
ATOM   487  O  OE1 . GLU A 1 88  ? 116.761 153.684 88.217  1.00 85.69  ? 69  GLU A OE1 1 
ATOM   488  O  OE2 . GLU A 1 88  ? 116.985 154.402 86.155  1.00 85.69  ? 69  GLU A OE2 1 
ATOM   489  N  N   . GLY A 1 89  ? 118.785 152.176 89.228  1.00 83.67  ? 70  GLY A N   1 
ATOM   490  C  CA  . GLY A 1 89  ? 119.873 153.126 89.401  1.00 83.67  ? 70  GLY A CA  1 
ATOM   491  C  C   . GLY A 1 89  ? 121.204 152.452 89.673  1.00 83.67  ? 70  GLY A C   1 
ATOM   492  O  O   . GLY A 1 89  ? 122.235 152.842 89.119  1.00 83.67  ? 70  GLY A O   1 
ATOM   493  N  N   . GLY A 1 90  ? 121.199 151.429 90.530  1.00 84.49  ? 71  GLY A N   1 
ATOM   494  C  CA  . GLY A 1 90  ? 122.425 150.695 90.794  1.00 84.49  ? 71  GLY A CA  1 
ATOM   495  C  C   . GLY A 1 90  ? 122.967 150.009 89.556  1.00 84.49  ? 71  GLY A C   1 
ATOM   496  O  O   . GLY A 1 90  ? 124.177 150.007 89.313  1.00 84.49  ? 71  GLY A O   1 
ATOM   497  N  N   . TRP A 1 91  ? 122.076 149.430 88.748  1.00 84.62  ? 72  TRP A N   1 
ATOM   498  C  CA  . TRP A 1 91  ? 122.515 148.785 87.518  1.00 84.62  ? 72  TRP A CA  1 
ATOM   499  C  C   . TRP A 1 91  ? 123.066 149.807 86.536  1.00 84.62  ? 72  TRP A C   1 
ATOM   500  O  O   . TRP A 1 91  ? 124.075 149.554 85.873  1.00 84.62  ? 72  TRP A O   1 
ATOM   501  C  CB  . TRP A 1 91  ? 121.361 148.003 86.891  1.00 84.62  ? 72  TRP A CB  1 
ATOM   502  C  CG  . TRP A 1 91  ? 121.737 147.264 85.644  1.00 84.62  ? 72  TRP A CG  1 
ATOM   503  C  CD1 . TRP A 1 91  ? 121.877 147.785 84.392  1.00 84.62  ? 72  TRP A CD1 1 
ATOM   504  C  CD2 . TRP A 1 91  ? 122.016 145.864 85.529  1.00 84.62  ? 72  TRP A CD2 1 
ATOM   505  N  NE1 . TRP A 1 91  ? 122.230 146.798 83.505  1.00 84.62  ? 72  TRP A NE1 1 
ATOM   506  C  CE2 . TRP A 1 91  ? 122.321 145.609 84.178  1.00 84.62  ? 72  TRP A CE2 1 
ATOM   507  C  CE3 . TRP A 1 91  ? 122.039 144.803 86.437  1.00 84.62  ? 72  TRP A CE3 1 
ATOM   508  C  CZ2 . TRP A 1 91  ? 122.644 144.337 83.714  1.00 84.62  ? 72  TRP A CZ2 1 
ATOM   509  C  CZ3 . TRP A 1 91  ? 122.360 143.541 85.974  1.00 84.62  ? 72  TRP A CZ3 1 
ATOM   510  C  CH2 . TRP A 1 91  ? 122.658 143.319 84.625  1.00 84.62  ? 72  TRP A CH2 1 
ATOM   511  N  N   . GLU A 1 92  ? 122.442 150.984 86.461  1.00 89.00  ? 73  GLU A N   1 
ATOM   512  C  CA  . GLU A 1 92  ? 122.948 152.039 85.588  1.00 89.00  ? 73  GLU A CA  1 
ATOM   513  C  C   . GLU A 1 92  ? 124.325 152.510 86.036  1.00 89.00  ? 73  GLU A C   1 
ATOM   514  O  O   . GLU A 1 92  ? 125.194 152.794 85.204  1.00 89.00  ? 73  GLU A O   1 
ATOM   515  C  CB  . GLU A 1 92  ? 121.963 153.207 85.549  1.00 89.00  ? 73  GLU A CB  1 
ATOM   516  C  CG  . GLU A 1 92  ? 121.984 153.984 84.244  1.00 89.00  ? 73  GLU A CG  1 
ATOM   517  C  CD  . GLU A 1 92  ? 120.866 153.574 83.305  1.00 89.00  ? 73  GLU A CD  1 
ATOM   518  O  OE1 . GLU A 1 92  ? 119.690 153.848 83.622  1.00 89.00  ? 73  GLU A OE1 1 
ATOM   519  O  OE2 . GLU A 1 92  ? 121.165 152.976 82.250  1.00 89.00  ? 73  GLU A OE2 1 
ATOM   520  N  N   . ARG A 1 93  ? 124.543 152.600 87.348  1.00 87.62  ? 74  ARG A N   1 
ATOM   521  C  CA  . ARG A 1 93  ? 125.825 153.073 87.861  1.00 87.62  ? 74  ARG A CA  1 
ATOM   522  C  C   . ARG A 1 93  ? 126.921 152.020 87.741  1.00 87.62  ? 74  ARG A C   1 
ATOM   523  O  O   . ARG A 1 93  ? 128.094 152.376 87.585  1.00 87.62  ? 74  ARG A O   1 
ATOM   524  C  CB  . ARG A 1 93  ? 125.685 153.523 89.315  1.00 87.62  ? 74  ARG A CB  1 
ATOM   525  C  CG  . ARG A 1 93  ? 124.770 154.722 89.500  1.00 87.62  ? 74  ARG A CG  1 
ATOM   526  C  CD  . ARG A 1 93  ? 124.685 155.134 90.958  1.00 87.62  ? 74  ARG A CD  1 
ATOM   527  N  NE  . ARG A 1 93  ? 125.959 154.952 91.644  1.00 87.62  ? 74  ARG A NE  1 
ATOM   528  C  CZ  . ARG A 1 93  ? 126.955 155.826 91.608  1.00 87.62  ? 74  ARG A CZ  1 
ATOM   529  N  NH1 . ARG A 1 93  ? 126.860 156.955 90.925  1.00 87.62  ? 74  ARG A NH1 1 
ATOM   530  N  NH2 . ARG A 1 93  ? 128.077 155.559 92.269  1.00 87.62  ? 74  ARG A NH2 1 
ATOM   531  N  N   . LEU A 1 94  ? 126.574 150.735 87.807  1.00 84.88  ? 75  LEU A N   1 
ATOM   532  C  CA  . LEU A 1 94  ? 127.562 149.662 87.881  1.00 84.88  ? 75  LEU A CA  1 
ATOM   533  C  C   . LEU A 1 94  ? 127.843 149.028 86.523  1.00 84.88  ? 75  LEU A C   1 
ATOM   534  O  O   . LEU A 1 94  ? 129.005 148.916 86.122  1.00 84.88  ? 75  LEU A O   1 
ATOM   535  C  CB  . LEU A 1 94  ? 127.097 148.584 88.868  1.00 84.88  ? 75  LEU A CB  1 
ATOM   536  C  CG  . LEU A 1 94  ? 127.083 148.963 90.348  1.00 84.88  ? 75  LEU A CG  1 
ATOM   537  C  CD1 . LEU A 1 94  ? 126.495 147.836 91.180  1.00 84.88  ? 75  LEU A CD1 1 
ATOM   538  C  CD2 . LEU A 1 94  ? 128.483 149.308 90.821  1.00 84.88  ? 75  LEU A CD2 1 
ATOM   539  N  N   . PHE A 1 95  ? 126.804 148.606 85.810  1.00 87.42  ? 76  PHE A N   1 
ATOM   540  C  CA  . PHE A 1 95  ? 126.925 147.990 84.494  1.00 87.42  ? 76  PHE A CA  1 
ATOM   541  C  C   . PHE A 1 95  ? 126.205 148.872 83.486  1.00 87.42  ? 76  PHE A C   1 
ATOM   542  O  O   . PHE A 1 95  ? 124.982 149.026 83.555  1.00 87.42  ? 76  PHE A O   1 
ATOM   543  C  CB  . PHE A 1 95  ? 126.350 146.572 84.486  1.00 87.42  ? 76  PHE A CB  1 
ATOM   544  C  CG  . PHE A 1 95  ? 126.424 145.880 85.816  1.00 87.42  ? 76  PHE A CG  1 
ATOM   545  C  CD1 . PHE A 1 95  ? 127.583 145.236 86.212  1.00 87.42  ? 76  PHE A CD1 1 
ATOM   546  C  CD2 . PHE A 1 95  ? 125.333 145.868 86.668  1.00 87.42  ? 76  PHE A CD2 1 
ATOM   547  C  CE1 . PHE A 1 95  ? 127.654 144.595 87.434  1.00 87.42  ? 76  PHE A CE1 1 
ATOM   548  C  CE2 . PHE A 1 95  ? 125.398 145.229 87.891  1.00 87.42  ? 76  PHE A CE2 1 
ATOM   549  C  CZ  . PHE A 1 95  ? 126.560 144.592 88.275  1.00 87.42  ? 76  PHE A CZ  1 
ATOM   550  N  N   . GLY A 1 96  ? 126.943 149.400 82.518  1.00 93.69  ? 77  GLY A N   1 
ATOM   551  C  CA  . GLY A 1 96  ? 126.310 150.314 81.595  1.00 93.69  ? 77  GLY A CA  1 
ATOM   552  C  C   . GLY A 1 96  ? 125.756 149.675 80.346  1.00 93.69  ? 77  GLY A C   1 
ATOM   553  O  O   . GLY A 1 96  ? 125.335 150.387 79.428  1.00 93.69  ? 77  GLY A O   1 
ATOM   554  N  N   . ASP A 1 97  ? 125.746 148.349 80.281  1.00 99.40  ? 78  ASP A N   1 
ATOM   555  C  CA  . ASP A 1 97  ? 125.236 147.641 79.123  1.00 99.40  ? 78  ASP A CA  1 
ATOM   556  C  C   . ASP A 1 97  ? 123.713 147.591 79.225  1.00 99.40  ? 78  ASP A C   1 
ATOM   557  O  O   . ASP A 1 97  ? 123.126 148.013 80.226  1.00 99.40  ? 78  ASP A O   1 
ATOM   558  C  CB  . ASP A 1 97  ? 125.842 146.238 79.048  1.00 99.40  ? 78  ASP A CB  1 
ATOM   559  C  CG  . ASP A 1 97  ? 125.584 145.556 77.718  1.00 99.40  ? 78  ASP A CG  1 
ATOM   560  O  OD1 . ASP A 1 97  ? 125.084 146.226 76.791  1.00 99.40  ? 78  ASP A OD1 1 
ATOM   561  O  OD2 . ASP A 1 97  ? 125.888 144.350 77.599  1.00 99.40  ? 78  ASP A OD2 1 
ATOM   562  N  N   . THR A 1 98  ? 123.065 147.112 78.161  1.00 92.62  ? 79  THR A N   1 
ATOM   563  C  CA  . THR A 1 98  ? 121.608 147.051 78.129  1.00 92.62  ? 79  THR A CA  1 
ATOM   564  C  C   . THR A 1 98  ? 121.067 146.406 79.401  1.00 92.62  ? 79  THR A C   1 
ATOM   565  O  O   . THR A 1 98  ? 121.637 145.443 79.920  1.00 92.62  ? 79  THR A O   1 
ATOM   566  C  CB  . THR A 1 98  ? 121.131 146.282 76.893  1.00 92.62  ? 79  THR A CB  1 
ATOM   567  O  OG1 . THR A 1 98  ? 119.699 146.237 76.879  1.00 92.62  ? 79  THR A OG1 1 
ATOM   568  C  CG2 . THR A 1 98  ? 121.689 144.863 76.878  1.00 92.62  ? 79  THR A CG2 1 
ATOM   569  N  N   . LYS A 1 99  ? 119.972 146.955 79.910  1.00 88.69  ? 80  LYS A N   1 
ATOM   570  C  CA  . LYS A 1 99  ? 119.353 146.450 81.127  1.00 88.69  ? 80  LYS A CA  1 
ATOM   571  C  C   . LYS A 1 99  ? 118.287 145.422 80.785  1.00 88.69  ? 80  LYS A C   1 
ATOM   572  O  O   . LYS A 1 99  ? 117.895 145.273 79.625  1.00 88.69  ? 80  LYS A O   1 
ATOM   573  C  CB  . LYS A 1 99  ? 118.733 147.612 81.900  1.00 88.69  ? 80  LYS A CB  1 
ATOM   574  C  CG  . LYS A 1 99  ? 119.599 148.850 82.018  1.00 88.69  ? 80  LYS A CG  1 
ATOM   575  C  CD  . LYS A 1 99  ? 118.928 149.879 82.919  1.00 88.69  ? 80  LYS A CD  1 
ATOM   576  C  CE  . LYS A 1 99  ? 117.454 150.030 82.587  1.00 88.69  ? 80  LYS A CE  1 
ATOM   577  N  NZ  . LYS A 1 99  ? 116.996 151.443 82.649  1.00 88.69  ? 80  LYS A NZ  1 
ATOM   578  N  N   . PRO A 1 100 ? 117.799 144.673 81.777  1.00 85.24  ? 81  PRO A N   1 
ATOM   579  C  CA  . PRO A 1 100 ? 116.723 143.715 81.505  1.00 85.24  ? 81  PRO A CA  1 
ATOM   580  C  C   . PRO A 1 100 ? 115.473 144.417 80.994  1.00 85.24  ? 81  PRO A C   1 
ATOM   581  O  O   . PRO A 1 100 ? 115.306 145.631 81.128  1.00 85.24  ? 81  PRO A O   1 
ATOM   582  C  CB  . PRO A 1 100 ? 116.486 143.046 82.863  1.00 85.24  ? 81  PRO A CB  1 
ATOM   583  C  CG  . PRO A 1 100 ? 117.772 143.215 83.589  1.00 85.24  ? 81  PRO A CG  1 
ATOM   584  C  CD  . PRO A 1 100 ? 118.310 144.538 83.152  1.00 85.24  ? 81  PRO A CD  1 
ATOM   585  N  N   . GLU A 1 101 ? 114.584 143.623 80.396  1.00 87.95  ? 82  GLU A N   1 
ATOM   586  C  CA  . GLU A 1 101 ? 113.413 144.191 79.735  1.00 87.95  ? 82  GLU A CA  1 
ATOM   587  C  C   . GLU A 1 101 ? 112.491 144.895 80.725  1.00 87.95  ? 82  GLU A C   1 
ATOM   588  O  O   . GLU A 1 101 ? 111.993 145.992 80.448  1.00 87.95  ? 82  GLU A O   1 
ATOM   589  C  CB  . GLU A 1 101 ? 112.658 143.095 78.985  1.00 87.95  ? 82  GLU A CB  1 
ATOM   590  C  CG  . GLU A 1 101 ? 111.763 143.609 77.873  1.00 87.95  ? 82  GLU A CG  1 
ATOM   591  C  CD  . GLU A 1 101 ? 111.509 142.567 76.802  1.00 87.95  ? 82  GLU A CD  1 
ATOM   592  O  OE1 . GLU A 1 101 ? 111.138 141.429 77.157  1.00 87.95  ? 82  GLU A OE1 1 
ATOM   593  O  OE2 . GLU A 1 101 ? 111.683 142.884 75.607  1.00 87.95  ? 82  GLU A OE2 1 
ATOM   594  N  N   . TYR A 1 102 ? 112.257 144.284 81.886  1.00 84.66  ? 83  TYR A N   1 
ATOM   595  C  CA  . TYR A 1 102 ? 111.268 144.766 82.843  1.00 84.66  ? 83  TYR A CA  1 
ATOM   596  C  C   . TYR A 1 102 ? 111.893 145.431 84.066  1.00 84.66  ? 83  TYR A C   1 
ATOM   597  O  O   . TYR A 1 102 ? 111.233 145.547 85.103  1.00 84.66  ? 83  TYR A O   1 
ATOM   598  C  CB  . TYR A 1 102 ? 110.356 143.619 83.274  1.00 84.66  ? 83  TYR A CB  1 
ATOM   599  C  CG  . TYR A 1 102 ? 109.734 142.873 82.118  1.00 84.66  ? 83  TYR A CG  1 
ATOM   600  C  CD1 . TYR A 1 102 ? 108.850 143.505 81.254  1.00 84.66  ? 83  TYR A CD1 1 
ATOM   601  C  CD2 . TYR A 1 102 ? 110.037 141.538 81.885  1.00 84.66  ? 83  TYR A CD2 1 
ATOM   602  C  CE1 . TYR A 1 102 ? 108.280 142.827 80.195  1.00 84.66  ? 83  TYR A CE1 1 
ATOM   603  C  CE2 . TYR A 1 102 ? 109.473 140.852 80.827  1.00 84.66  ? 83  TYR A CE2 1 
ATOM   604  C  CZ  . TYR A 1 102 ? 108.595 141.502 79.986  1.00 84.66  ? 83  TYR A CZ  1 
ATOM   605  O  OH  . TYR A 1 102 ? 108.030 140.824 78.930  1.00 84.66  ? 83  TYR A OH  1 
ATOM   606  N  N   . LEU A 1 103 ? 113.145 145.869 83.975  1.00 80.54  ? 84  LEU A N   1 
ATOM   607  C  CA  . LEU A 1 103 ? 113.799 146.546 85.088  1.00 80.54  ? 84  LEU A CA  1 
ATOM   608  C  C   . LEU A 1 103 ? 113.516 148.042 85.006  1.00 80.54  ? 84  LEU A C   1 
ATOM   609  O  O   . LEU A 1 103 ? 113.885 148.698 84.026  1.00 80.54  ? 84  LEU A O   1 
ATOM   610  C  CB  . LEU A 1 103 ? 115.303 146.282 85.078  1.00 80.54  ? 84  LEU A CB  1 
ATOM   611  C  CG  . LEU A 1 103 ? 116.077 146.873 86.257  1.00 80.54  ? 84  LEU A CG  1 
ATOM   612  C  CD1 . LEU A 1 103 ? 115.493 146.387 87.572  1.00 80.54  ? 84  LEU A CD1 1 
ATOM   613  C  CD2 . LEU A 1 103 ? 117.551 146.524 86.164  1.00 80.54  ? 84  LEU A CD2 1 
ATOM   614  N  N   . HIS A 1 104 ? 112.861 148.574 86.035  1.00 85.32  ? 85  HIS A N   1 
ATOM   615  C  CA  . HIS A 1 104 ? 112.489 149.981 86.073  1.00 85.32  ? 85  HIS A CA  1 
ATOM   616  C  C   . HIS A 1 104 ? 112.272 150.386 87.523  1.00 85.32  ? 85  HIS A C   1 
ATOM   617  O  O   . HIS A 1 104 ? 112.185 149.542 88.419  1.00 85.32  ? 85  HIS A O   1 
ATOM   618  C  CB  . HIS A 1 104 ? 111.238 150.252 85.233  1.00 85.32  ? 85  HIS A CB  1 
ATOM   619  C  CG  . HIS A 1 104 ? 110.084 149.358 85.565  1.00 85.32  ? 85  HIS A CG  1 
ATOM   620  N  ND1 . HIS A 1 104 ? 109.362 149.477 86.733  1.00 85.32  ? 85  HIS A ND1 1 
ATOM   621  C  CD2 . HIS A 1 104 ? 109.526 148.331 84.881  1.00 85.32  ? 85  HIS A CD2 1 
ATOM   622  C  CE1 . HIS A 1 104 ? 108.410 148.562 86.755  1.00 85.32  ? 85  HIS A CE1 1 
ATOM   623  N  NE2 . HIS A 1 104 ? 108.487 147.853 85.643  1.00 85.32  ? 85  HIS A NE2 1 
ATOM   624  N  N   . VAL A 1 105 ? 112.189 151.698 87.744  1.00 87.53  ? 86  VAL A N   1 
ATOM   625  C  CA  . VAL A 1 105 ? 111.919 152.221 89.077  1.00 87.53  ? 86  VAL A CA  1 
ATOM   626  C  C   . VAL A 1 105 ? 110.519 151.807 89.509  1.00 87.53  ? 86  VAL A C   1 
ATOM   627  O  O   . VAL A 1 105 ? 109.572 151.824 88.712  1.00 87.53  ? 86  VAL A O   1 
ATOM   628  C  CB  . VAL A 1 105 ? 112.079 153.751 89.095  1.00 87.53  ? 86  VAL A CB  1 
ATOM   629  C  CG1 . VAL A 1 105 ? 111.885 154.293 90.502  1.00 87.53  ? 86  VAL A CG1 1 
ATOM   630  C  CG2 . VAL A 1 105 ? 113.440 154.148 88.546  1.00 87.53  ? 86  VAL A CG2 1 
ATOM   631  N  N   . PHE A 1 106 ? 110.386 151.419 90.777  1.00 88.34  ? 87  PHE A N   1 
ATOM   632  C  CA  . PHE A 1 106 ? 109.094 150.996 91.302  1.00 88.34  ? 87  PHE A CA  1 
ATOM   633  C  C   . PHE A 1 106 ? 108.077 152.124 91.191  1.00 88.34  ? 87  PHE A C   1 
ATOM   634  O  O   . PHE A 1 106 ? 108.358 153.269 91.556  1.00 88.34  ? 87  PHE A O   1 
ATOM   635  C  CB  . PHE A 1 106 ? 109.242 150.552 92.757  1.00 88.34  ? 87  PHE A CB  1 
ATOM   636  C  CG  . PHE A 1 106 ? 107.958 150.093 93.386  1.00 88.34  ? 87  PHE A CG  1 
ATOM   637  C  CD1 . PHE A 1 106 ? 107.454 148.832 93.120  1.00 88.34  ? 87  PHE A CD1 1 
ATOM   638  C  CD2 . PHE A 1 106 ? 107.258 150.920 94.248  1.00 88.34  ? 87  PHE A CD2 1 
ATOM   639  C  CE1 . PHE A 1 106 ? 106.275 148.405 93.698  1.00 88.34  ? 87  PHE A CE1 1 
ATOM   640  C  CE2 . PHE A 1 106 ? 106.078 150.499 94.828  1.00 88.34  ? 87  PHE A CE2 1 
ATOM   641  C  CZ  . PHE A 1 106 ? 105.586 149.240 94.553  1.00 88.34  ? 87  PHE A CZ  1 
ATOM   642  N  N   . ARG A 1 107 ? 106.893 151.795 90.683  1.00 93.35  ? 88  ARG A N   1 
ATOM   643  C  CA  . ARG A 1 107 ? 105.835 152.776 90.478  1.00 93.35  ? 88  ARG A CA  1 
ATOM   644  C  C   . ARG A 1 107 ? 105.007 152.915 91.749  1.00 93.35  ? 88  ARG A C   1 
ATOM   645  O  O   . ARG A 1 107 ? 104.468 151.926 92.256  1.00 93.35  ? 88  ARG A O   1 
ATOM   646  C  CB  . ARG A 1 107 ? 104.945 152.372 89.303  1.00 93.35  ? 88  ARG A CB  1 
ATOM   647  C  CG  . ARG A 1 107 ? 105.569 151.350 88.369  1.00 93.35  ? 88  ARG A CG  1 
ATOM   648  C  CD  . ARG A 1 107 ? 105.064 151.530 86.946  1.00 93.35  ? 88  ARG A CD  1 
ATOM   649  N  NE  . ARG A 1 107 ? 105.733 152.632 86.265  1.00 93.35  ? 88  ARG A NE  1 
ATOM   650  C  CZ  . ARG A 1 107 ? 106.839 152.506 85.545  1.00 93.35  ? 88  ARG A CZ  1 
ATOM   651  N  NH1 . ARG A 1 107 ? 107.429 151.334 85.384  1.00 93.35  ? 88  ARG A NH1 1 
ATOM   652  N  NH2 . ARG A 1 107 ? 107.365 153.585 84.971  1.00 93.35  ? 88  ARG A NH2 1 
ATOM   653  N  N   . GLU A 1 108 ? 104.909 154.139 92.258  1.00 94.31  ? 89  GLU A N   1 
ATOM   654  C  CA  . GLU A 1 108 ? 104.055 154.409 93.404  1.00 94.31  ? 89  GLU A CA  1 
ATOM   655  C  C   . GLU A 1 108 ? 102.586 154.306 93.005  1.00 94.31  ? 89  GLU A C   1 
ATOM   656  O  O   . GLU A 1 108 ? 102.211 154.550 91.855  1.00 94.31  ? 89  GLU A O   1 
ATOM   657  C  CB  . GLU A 1 108 ? 104.360 155.791 93.985  1.00 94.31  ? 89  GLU A CB  1 
ATOM   658  C  CG  . GLU A 1 108 ? 103.509 156.917 93.426  1.00 94.31  ? 89  GLU A CG  1 
ATOM   659  C  CD  . GLU A 1 108 ? 104.207 158.261 93.496  1.00 94.31  ? 89  GLU A CD  1 
ATOM   660  O  OE1 . GLU A 1 108 ? 105.164 158.394 94.287  1.00 94.31  ? 89  GLU A OE1 1 
ATOM   661  O  OE2 . GLU A 1 108 ? 103.801 159.183 92.757  1.00 94.31  ? 89  GLU A OE2 1 
ATOM   662  N  N   . ILE A 1 109 ? 101.753 153.919 93.967  1.00 91.56  ? 90  ILE A N   1 
ATOM   663  C  CA  . ILE A 1 109 ? 100.326 153.718 93.744  1.00 91.56  ? 90  ILE A CA  1 
ATOM   664  C  C   . ILE A 1 109 ? 99.559  154.682 94.636  1.00 91.56  ? 90  ILE A C   1 
ATOM   665  O  O   . ILE A 1 109 ? 99.774  154.713 95.853  1.00 91.56  ? 90  ILE A O   1 
ATOM   666  C  CB  . ILE A 1 109 ? 99.906  152.264 94.023  1.00 91.56  ? 90  ILE A CB  1 
ATOM   667  C  CG1 . ILE A 1 109 ? 100.785 151.296 93.233  1.00 91.56  ? 90  ILE A CG1 1 
ATOM   668  C  CG2 . ILE A 1 109 ? 98.442  152.060 93.677  1.00 91.56  ? 90  ILE A CG2 1 
ATOM   669  C  CD1 . ILE A 1 109 ? 100.497 149.845 93.520  1.00 91.56  ? 90  ILE A CD1 1 
ATOM   670  N  N   . ASN A 1 110 ? 98.666  155.460 94.031  1.00 99.45  ? 91  ASN A N   1 
ATOM   671  C  CA  . ASN A 1 110 ? 97.869  156.460 94.737  1.00 99.45  ? 91  ASN A CA  1 
ATOM   672  C  C   . ASN A 1 110 ? 96.394  156.116 94.557  1.00 99.45  ? 91  ASN A C   1 
ATOM   673  O  O   . ASN A 1 110 ? 95.740  156.590 93.625  1.00 99.45  ? 91  ASN A O   1 
ATOM   674  C  CB  . ASN A 1 110 ? 98.184  157.867 94.230  1.00 99.45  ? 91  ASN A CB  1 
ATOM   675  C  CG  . ASN A 1 110 ? 99.350  158.502 94.960  1.00 99.45  ? 91  ASN A CG  1 
ATOM   676  O  OD1 . ASN A 1 110 ? 99.554  158.266 96.151  1.00 99.45  ? 91  ASN A OD1 1 
ATOM   677  N  ND2 . ASN A 1 110 ? 100.123 159.313 94.249  1.00 99.45  ? 91  ASN A ND2 1 
ATOM   678  N  N   . GLY A 1 111 ? 95.874  155.285 95.456  1.00 97.34  ? 92  GLY A N   1 
ATOM   679  C  CA  . GLY A 1 111 ? 94.462  154.963 95.475  1.00 97.34  ? 92  GLY A CA  1 
ATOM   680  C  C   . GLY A 1 111 ? 93.837  155.330 96.804  1.00 97.34  ? 92  GLY A C   1 
ATOM   681  O  O   . GLY A 1 111 ? 94.023  156.449 97.292  1.00 97.34  ? 92  GLY A O   1 
ATOM   682  N  N   . VAL A 1 112 ? 93.090  154.400 97.403  1.00 94.09  ? 93  VAL A N   1 
ATOM   683  C  CA  . VAL A 1 112 ? 92.592  154.623 98.753  1.00 94.09  ? 93  VAL A CA  1 
ATOM   684  C  C   . VAL A 1 112 ? 93.732  154.623 99.762  1.00 94.09  ? 93  VAL A C   1 
ATOM   685  O  O   . VAL A 1 112 ? 93.609  155.225 100.835 1.00 94.09  ? 93  VAL A O   1 
ATOM   686  C  CB  . VAL A 1 112 ? 91.522  153.577 99.119  1.00 94.09  ? 93  VAL A CB  1 
ATOM   687  C  CG1 . VAL A 1 112 ? 90.536  153.409 97.974  1.00 94.09  ? 93  VAL A CG1 1 
ATOM   688  C  CG2 . VAL A 1 112 ? 92.166  152.247 99.467  1.00 94.09  ? 93  VAL A CG2 1 
ATOM   689  N  N   . HIS A 1 113 ? 94.841  153.959 99.444  1.00 92.24  ? 94  HIS A N   1 
ATOM   690  C  CA  . HIS A 1 113 ? 96.039  153.964 100.267 1.00 92.24  ? 94  HIS A CA  1 
ATOM   691  C  C   . HIS A 1 113 ? 97.234  154.315 99.393  1.00 92.24  ? 94  HIS A C   1 
ATOM   692  O  O   . HIS A 1 113 ? 97.163  154.271 98.163  1.00 92.24  ? 94  HIS A O   1 
ATOM   693  C  CB  . HIS A 1 113 ? 96.261  152.612 100.956 1.00 92.24  ? 94  HIS A CB  1 
ATOM   694  C  CG  . HIS A 1 113 ? 95.328  152.355 102.099 1.00 92.24  ? 94  HIS A CG  1 
ATOM   695  N  ND1 . HIS A 1 113 ? 94.255  151.496 102.005 1.00 92.24  ? 94  HIS A ND1 1 
ATOM   696  C  CD2 . HIS A 1 113 ? 95.310  152.845 103.361 1.00 92.24  ? 94  HIS A CD2 1 
ATOM   697  C  CE1 . HIS A 1 113 ? 93.614  151.468 103.160 1.00 92.24  ? 94  HIS A CE1 1 
ATOM   698  N  NE2 . HIS A 1 113 ? 94.234  152.277 104.000 1.00 92.24  ? 94  HIS A NE2 1 
ATOM   699  N  N   . HIS A 1 114 ? 98.339  154.667 100.041 1.00 89.87  ? 95  HIS A N   1 
ATOM   700  C  CA  . HIS A 1 114 ? 99.548  155.099 99.354  1.00 89.87  ? 95  HIS A CA  1 
ATOM   701  C  C   . HIS A 1 114 ? 100.660 154.084 99.574  1.00 89.87  ? 95  HIS A C   1 
ATOM   702  O  O   . HIS A 1 114 ? 100.913 153.670 100.710 1.00 89.87  ? 95  HIS A O   1 
ATOM   703  C  CB  . HIS A 1 114 ? 99.988  156.481 99.841  1.00 89.87  ? 95  HIS A CB  1 
ATOM   704  C  CG  . HIS A 1 114 ? 101.294 156.935 99.269  1.00 89.87  ? 95  HIS A CG  1 
ATOM   705  N  ND1 . HIS A 1 114 ? 102.328 157.399 100.053 1.00 89.87  ? 95  HIS A ND1 1 
ATOM   706  C  CD2 . HIS A 1 114 ? 101.734 156.997 97.990  1.00 89.87  ? 95  HIS A CD2 1 
ATOM   707  C  CE1 . HIS A 1 114 ? 103.349 157.728 99.281  1.00 89.87  ? 95  HIS A CE1 1 
ATOM   708  N  NE2 . HIS A 1 114 ? 103.014 157.493 98.025  1.00 89.87  ? 95  HIS A NE2 1 
ATOM   709  N  N   . ALA A 1 115 ? 101.317 153.686 98.486  1.00 88.37  ? 96  ALA A N   1 
ATOM   710  C  CA  . ALA A 1 115 ? 102.474 152.798 98.546  1.00 88.37  ? 96  ALA A CA  1 
ATOM   711  C  C   . ALA A 1 115 ? 103.703 153.562 98.074  1.00 88.37  ? 96  ALA A C   1 
ATOM   712  O  O   . ALA A 1 115 ? 103.925 153.694 96.860  1.00 88.37  ? 96  ALA A O   1 
ATOM   713  C  CB  . ALA A 1 115 ? 102.252 151.551 97.686  1.00 88.37  ? 96  ALA A CB  1 
ATOM   714  N  N   . PRO A 1 116 ? 104.528 154.080 98.979  1.00 86.91  ? 97  PRO A N   1 
ATOM   715  C  CA  . PRO A 1 116 ? 105.632 154.949 98.563  1.00 86.91  ? 97  PRO A CA  1 
ATOM   716  C  C   . PRO A 1 116 ? 106.767 154.169 97.918  1.00 86.91  ? 97  PRO A C   1 
ATOM   717  O  O   . PRO A 1 116 ? 106.899 152.953 98.068  1.00 86.91  ? 97  PRO A O   1 
ATOM   718  C  CB  . PRO A 1 116 ? 106.082 155.594 99.876  1.00 86.91  ? 97  PRO A CB  1 
ATOM   719  C  CG  . PRO A 1 116 ? 105.757 154.568 100.907 1.00 86.91  ? 97  PRO A CG  1 
ATOM   720  C  CD  . PRO A 1 116 ? 104.487 153.900 100.441 1.00 86.91  ? 97  PRO A CD  1 
ATOM   721  N  N   . SER A 1 117 ? 107.594 154.906 97.182  1.00 83.93  ? 98  SER A N   1 
ATOM   722  C  CA  . SER A 1 117 ? 108.814 154.387 96.585  1.00 83.93  ? 98  SER A CA  1 
ATOM   723  C  C   . SER A 1 117 ? 110.013 154.937 97.343  1.00 83.93  ? 98  SER A C   1 
ATOM   724  O  O   . SER A 1 117 ? 110.053 156.124 97.681  1.00 83.93  ? 98  SER A O   1 
ATOM   725  C  CB  . SER A 1 117 ? 108.911 154.765 95.105  1.00 83.93  ? 98  SER A CB  1 
ATOM   726  O  OG  . SER A 1 117 ? 110.085 154.232 94.520  1.00 83.93  ? 98  SER A OG  1 
ATOM   727  N  N   . THR A 1 118 ? 110.989 154.074 97.610  1.00 83.36  ? 99  THR A N   1 
ATOM   728  C  CA  . THR A 1 118 ? 112.118 154.469 98.434  1.00 83.36  ? 99  THR A CA  1 
ATOM   729  C  C   . THR A 1 118 ? 113.433 154.229 97.703  1.00 83.36  ? 99  THR A C   1 
ATOM   730  O  O   . THR A 1 118 ? 113.531 153.325 96.867  1.00 83.36  ? 99  THR A O   1 
ATOM   731  C  CB  . THR A 1 118 ? 112.128 153.694 99.757  1.00 83.36  ? 99  THR A CB  1 
ATOM   732  O  OG1 . THR A 1 118 ? 111.914 152.302 99.496  1.00 83.36  ? 99  THR A OG1 1 
ATOM   733  C  CG2 . THR A 1 118 ? 111.036 154.206 100.682 1.00 83.36  ? 99  THR A CG2 1 
ATOM   734  N  N   . PRO A 1 119 ? 114.459 155.029 97.993  1.00 86.61  ? 100 PRO A N   1 
ATOM   735  C  CA  . PRO A 1 119 ? 115.759 154.824 97.346  1.00 86.61  ? 100 PRO A CA  1 
ATOM   736  C  C   . PRO A 1 119 ? 116.376 153.489 97.733  1.00 86.61  ? 100 PRO A C   1 
ATOM   737  O  O   . PRO A 1 119 ? 116.168 152.976 98.835  1.00 86.61  ? 100 PRO A O   1 
ATOM   738  C  CB  . PRO A 1 119 ? 116.602 155.997 97.860  1.00 86.61  ? 100 PRO A CB  1 
ATOM   739  C  CG  . PRO A 1 119 ? 115.607 157.026 98.284  1.00 86.61  ? 100 PRO A CG  1 
ATOM   740  C  CD  . PRO A 1 119 ? 114.438 156.254 98.810  1.00 86.61  ? 100 PRO A CD  1 
ATOM   741  N  N   . GLY A 1 120 ? 117.145 152.929 96.805  1.00 80.38  ? 101 GLY A N   1 
ATOM   742  C  CA  . GLY A 1 120 ? 117.833 151.675 97.037  1.00 80.38  ? 101 GLY A CA  1 
ATOM   743  C  C   . GLY A 1 120 ? 118.628 151.227 95.830  1.00 80.38  ? 101 GLY A C   1 
ATOM   744  O  O   . GLY A 1 120 ? 118.134 151.281 94.701  1.00 80.38  ? 101 GLY A O   1 
ATOM   745  N  N   . ASP A 1 121 ? 119.860 150.784 96.053  1.00 76.61  ? 102 ASP A N   1 
ATOM   746  C  CA  . ASP A 1 121 ? 120.742 150.359 94.974  1.00 76.61  ? 102 ASP A CA  1 
ATOM   747  C  C   . ASP A 1 121 ? 121.094 148.884 95.033  1.00 76.61  ? 102 ASP A C   1 
ATOM   748  O  O   . ASP A 1 121 ? 121.151 148.228 93.991  1.00 76.61  ? 102 ASP A O   1 
ATOM   749  C  CB  . ASP A 1 121 ? 122.032 151.190 94.989  1.00 76.61  ? 102 ASP A CB  1 
ATOM   750  C  CG  . ASP A 1 121 ? 121.791 152.644 94.636  1.00 76.61  ? 102 ASP A CG  1 
ATOM   751  O  OD1 . ASP A 1 121 ? 120.944 152.910 93.758  1.00 76.61  ? 102 ASP A OD1 1 
ATOM   752  O  OD2 . ASP A 1 121 ? 122.446 153.521 95.236  1.00 76.61  ? 102 ASP A OD2 1 
ATOM   753  N  N   . LEU A 1 122 ? 121.337 148.343 96.223  1.00 71.73  ? 103 LEU A N   1 
ATOM   754  C  CA  . LEU A 1 122 ? 121.661 146.935 96.393  1.00 71.73  ? 103 LEU A CA  1 
ATOM   755  C  C   . LEU A 1 122 ? 120.797 146.344 97.495  1.00 71.73  ? 103 LEU A C   1 
ATOM   756  O  O   . LEU A 1 122 ? 120.612 146.956 98.552  1.00 71.73  ? 103 LEU A O   1 
ATOM   757  C  CB  . LEU A 1 122 ? 123.143 146.735 96.727  1.00 71.73  ? 103 LEU A CB  1 
ATOM   758  C  CG  . LEU A 1 122 ? 124.153 147.403 95.793  1.00 71.73  ? 103 LEU A CG  1 
ATOM   759  C  CD1 . LEU A 1 122 ? 125.555 147.304 96.365  1.00 71.73  ? 103 LEU A CD1 1 
ATOM   760  C  CD2 . LEU A 1 122 ? 124.092 146.778 94.411  1.00 71.73  ? 103 LEU A CD2 1 
ATOM   761  N  N   . LEU A 1 123 ? 120.267 145.153 97.239  1.00 68.24  ? 104 LEU A N   1 
ATOM   762  C  CA  . LEU A 1 123 ? 119.432 144.431 98.188  1.00 68.24  ? 104 LEU A CA  1 
ATOM   763  C  C   . LEU A 1 123 ? 120.101 143.113 98.538  1.00 68.24  ? 104 LEU A C   1 
ATOM   764  O  O   . LEU A 1 123 ? 120.477 142.351 97.643  1.00 68.24  ? 104 LEU A O   1 
ATOM   765  C  CB  . LEU A 1 123 ? 118.038 144.172 97.612  1.00 68.24  ? 104 LEU A CB  1 
ATOM   766  C  CG  . LEU A 1 123 ? 117.186 143.132 98.346  1.00 68.24  ? 104 LEU A CG  1 
ATOM   767  C  CD1 . LEU A 1 123 ? 116.622 143.696 99.636  1.00 68.24  ? 104 LEU A CD1 1 
ATOM   768  C  CD2 . LEU A 1 123 ? 116.073 142.615 97.451  1.00 68.24  ? 104 LEU A CD2 1 
ATOM   769  N  N   . TYR A 1 124 ? 120.243 142.845 99.832  1.00 67.71  ? 105 TYR A N   1 
ATOM   770  C  CA  . TYR A 1 124 ? 120.779 141.585 100.331 1.00 67.71  ? 105 TYR A CA  1 
ATOM   771  C  C   . TYR A 1 124 ? 119.694 140.914 101.160 1.00 67.71  ? 105 TYR A C   1 
ATOM   772  O  O   . TYR A 1 124 ? 119.320 141.415 102.226 1.00 67.71  ? 105 TYR A O   1 
ATOM   773  C  CB  . TYR A 1 124 ? 122.045 141.805 101.157 1.00 67.71  ? 105 TYR A CB  1 
ATOM   774  C  CG  . TYR A 1 124 ? 123.192 142.412 100.384 1.00 67.71  ? 105 TYR A CG  1 
ATOM   775  C  CD1 . TYR A 1 124 ? 124.081 141.610 99.683  1.00 67.71  ? 105 TYR A CD1 1 
ATOM   776  C  CD2 . TYR A 1 124 ? 123.393 143.784 100.364 1.00 67.71  ? 105 TYR A CD2 1 
ATOM   777  C  CE1 . TYR A 1 124 ? 125.132 142.158 98.978  1.00 67.71  ? 105 TYR A CE1 1 
ATOM   778  C  CE2 . TYR A 1 124 ? 124.443 144.341 99.662  1.00 67.71  ? 105 TYR A CE2 1 
ATOM   779  C  CZ  . TYR A 1 124 ? 125.309 143.523 98.971  1.00 67.71  ? 105 TYR A CZ  1 
ATOM   780  O  OH  . TYR A 1 124 ? 126.356 144.072 98.269  1.00 67.71  ? 105 TYR A OH  1 
ATOM   781  N  N   . HIS A 1 125 ? 119.180 139.797 100.660 1.00 67.10  ? 106 HIS A N   1 
ATOM   782  C  CA  . HIS A 1 125 ? 118.200 138.987 101.374 1.00 67.10  ? 106 HIS A CA  1 
ATOM   783  C  C   . HIS A 1 125 ? 118.936 137.760 101.895 1.00 67.10  ? 106 HIS A C   1 
ATOM   784  O  O   . HIS A 1 125 ? 119.258 136.850 101.129 1.00 67.10  ? 106 HIS A O   1 
ATOM   785  C  CB  . HIS A 1 125 ? 117.042 138.610 100.457 1.00 67.10  ? 106 HIS A CB  1 
ATOM   786  C  CG  . HIS A 1 125 ? 115.988 137.780 101.119 1.00 67.10  ? 106 HIS A CG  1 
ATOM   787  N  ND1 . HIS A 1 125 ? 115.128 136.969 100.411 1.00 67.10  ? 106 HIS A ND1 1 
ATOM   788  C  CD2 . HIS A 1 125 ? 115.657 137.631 102.423 1.00 67.10  ? 106 HIS A CD2 1 
ATOM   789  C  CE1 . HIS A 1 125 ? 114.310 136.359 101.250 1.00 67.10  ? 106 HIS A CE1 1 
ATOM   790  N  NE2 . HIS A 1 125 ? 114.610 136.743 102.477 1.00 67.10  ? 106 HIS A NE2 1 
ATOM   791  N  N   . ILE A 1 126 ? 119.231 137.750 103.193 1.00 64.86  ? 107 ILE A N   1 
ATOM   792  C  CA  . ILE A 1 126 ? 119.987 136.676 103.827 1.00 64.86  ? 107 ILE A CA  1 
ATOM   793  C  C   . ILE A 1 126 ? 119.022 135.823 104.635 1.00 64.86  ? 107 ILE A C   1 
ATOM   794  O  O   . ILE A 1 126 ? 118.212 136.354 105.400 1.00 64.86  ? 107 ILE A O   1 
ATOM   795  C  CB  . ILE A 1 126 ? 121.109 137.233 104.719 1.00 64.86  ? 107 ILE A CB  1 
ATOM   796  C  CG1 . ILE A 1 126 ? 121.987 138.200 103.924 1.00 64.86  ? 107 ILE A CG1 1 
ATOM   797  C  CG2 . ILE A 1 126 ? 121.944 136.104 105.292 1.00 64.86  ? 107 ILE A CG2 1 
ATOM   798  C  CD1 . ILE A 1 126 ? 122.941 138.997 104.777 1.00 64.86  ? 107 ILE A CD1 1 
ATOM   799  N  N   . ARG A 1 127 ? 119.106 134.506 104.464 1.00 72.41  ? 108 ARG A N   1 
ATOM   800  C  CA  . ARG A 1 127 ? 118.229 133.565 105.146 1.00 72.41  ? 108 ARG A CA  1 
ATOM   801  C  C   . ARG A 1 127 ? 119.061 132.452 105.761 1.00 72.41  ? 108 ARG A C   1 
ATOM   802  O  O   . ARG A 1 127 ? 120.021 131.977 105.150 1.00 72.41  ? 108 ARG A O   1 
ATOM   803  C  CB  . ARG A 1 127 ? 117.196 132.967 104.187 1.00 72.41  ? 108 ARG A CB  1 
ATOM   804  C  CG  . ARG A 1 127 ? 116.163 133.956 103.687 1.00 72.41  ? 108 ARG A CG  1 
ATOM   805  C  CD  . ARG A 1 127 ? 115.254 133.312 102.658 1.00 72.41  ? 108 ARG A CD  1 
ATOM   806  N  NE  . ARG A 1 127 ? 115.915 133.171 101.367 1.00 72.41  ? 108 ARG A NE  1 
ATOM   807  C  CZ  . ARG A 1 127 ? 115.309 132.780 100.254 1.00 72.41  ? 108 ARG A CZ  1 
ATOM   808  N  NH1 . ARG A 1 127 ? 114.021 132.480 100.238 1.00 72.41  ? 108 ARG A NH1 1 
ATOM   809  N  NH2 . ARG A 1 127 ? 116.013 132.690 99.130  1.00 72.41  ? 108 ARG A NH2 1 
ATOM   810  N  N   . ALA A 1 128 ? 118.690 132.035 106.969 1.00 73.40  ? 109 ALA A N   1 
ATOM   811  C  CA  . ALA A 1 128 ? 119.369 130.919 107.613 1.00 73.40  ? 109 ALA A CA  1 
ATOM   812  C  C   . ALA A 1 128 ? 118.459 130.339 108.682 1.00 73.40  ? 109 ALA A C   1 
ATOM   813  O  O   . ALA A 1 128 ? 117.481 130.966 109.097 1.00 73.40  ? 109 ALA A O   1 
ATOM   814  C  CB  . ALA A 1 128 ? 120.710 131.344 108.218 1.00 73.40  ? 109 ALA A CB  1 
ATOM   815  N  N   . ALA A 1 129 ? 118.792 129.126 109.119 1.00 75.89  ? 110 ALA A N   1 
ATOM   816  C  CA  . ALA A 1 129 ? 118.043 128.479 110.187 1.00 75.89  ? 110 ALA A CA  1 
ATOM   817  C  C   . ALA A 1 129 ? 118.363 129.050 111.560 1.00 75.89  ? 110 ALA A C   1 
ATOM   818  O  O   . ALA A 1 129 ? 117.660 128.729 112.525 1.00 75.89  ? 110 ALA A O   1 
ATOM   819  C  CB  . ALA A 1 129 ? 118.312 126.973 110.183 1.00 75.89  ? 110 ALA A CB  1 
ATOM   820  N  N   . ARG A 1 130 ? 119.400 129.875 111.673 1.00 76.62  ? 111 ARG A N   1 
ATOM   821  C  CA  . ARG A 1 130 ? 119.768 130.504 112.931 1.00 76.62  ? 111 ARG A CA  1 
ATOM   822  C  C   . ARG A 1 130 ? 120.122 131.962 112.674 1.00 76.62  ? 111 ARG A C   1 
ATOM   823  O  O   . ARG A 1 130 ? 120.605 132.318 111.597 1.00 76.62  ? 111 ARG A O   1 
ATOM   824  C  CB  . ARG A 1 130 ? 120.940 129.772 113.601 1.00 76.62  ? 111 ARG A CB  1 
ATOM   825  C  CG  . ARG A 1 130 ? 120.603 128.351 114.038 1.00 76.62  ? 111 ARG A CG  1 
ATOM   826  C  CD  . ARG A 1 130 ? 121.759 127.381 113.826 1.00 76.62  ? 111 ARG A CD  1 
ATOM   827  N  NE  . ARG A 1 130 ? 122.799 127.518 114.839 1.00 76.62  ? 111 ARG A NE  1 
ATOM   828  C  CZ  . ARG A 1 130 ? 123.885 128.266 114.703 1.00 76.62  ? 111 ARG A CZ  1 
ATOM   829  N  NH1 . ARG A 1 130 ? 124.121 128.946 113.594 1.00 76.62  ? 111 ARG A NH1 1 
ATOM   830  N  NH2 . ARG A 1 130 ? 124.759 128.328 115.703 1.00 76.62  ? 111 ARG A NH2 1 
ATOM   831  N  N   . MET A 1 131 ? 119.869 132.804 113.678 1.00 76.14  ? 112 MET A N   1 
ATOM   832  C  CA  . MET A 1 131 ? 120.064 134.241 113.511 1.00 76.14  ? 112 MET A CA  1 
ATOM   833  C  C   . MET A 1 131 ? 121.546 134.580 113.391 1.00 76.14  ? 112 MET A C   1 
ATOM   834  O  O   . MET A 1 131 ? 121.919 135.481 112.630 1.00 76.14  ? 112 MET A O   1 
ATOM   835  C  CB  . MET A 1 131 ? 119.423 134.980 114.691 1.00 76.14  ? 112 MET A CB  1 
ATOM   836  C  CG  . MET A 1 131 ? 119.757 136.464 114.860 1.00 76.14  ? 112 MET A CG  1 
ATOM   837  S  SD  . MET A 1 131 ? 119.852 137.447 113.348 1.00 76.14  ? 112 MET A SD  1 
ATOM   838  C  CE  . MET A 1 131 ? 118.119 137.588 112.923 1.00 76.14  ? 112 MET A CE  1 
ATOM   839  N  N   . ASP A 1 132 ? 122.402 133.845 114.105 1.00 75.01  ? 113 ASP A N   1 
ATOM   840  C  CA  . ASP A 1 132 ? 123.823 134.174 114.150 1.00 75.01  ? 113 ASP A CA  1 
ATOM   841  C  C   . ASP A 1 132 ? 124.478 134.076 112.777 1.00 75.01  ? 113 ASP A C   1 
ATOM   842  O  O   . ASP A 1 132 ? 125.391 134.850 112.474 1.00 75.01  ? 113 ASP A O   1 
ATOM   843  C  CB  . ASP A 1 132 ? 124.536 133.271 115.156 1.00 75.01  ? 113 ASP A CB  1 
ATOM   844  C  CG  . ASP A 1 132 ? 124.230 131.802 114.943 1.00 75.01  ? 113 ASP A CG  1 
ATOM   845  O  OD1 . ASP A 1 132 ? 124.400 131.308 113.809 1.00 75.01  ? 113 ASP A OD1 1 
ATOM   846  O  OD2 . ASP A 1 132 ? 123.814 131.138 115.916 1.00 75.01  ? 113 ASP A OD2 1 
ATOM   847  N  N   . LEU A 1 133 ? 124.044 133.129 111.942 1.00 72.35  ? 114 LEU A N   1 
ATOM   848  C  CA  . LEU A 1 133 ? 124.608 133.019 110.599 1.00 72.35  ? 114 LEU A CA  1 
ATOM   849  C  C   . LEU A 1 133 ? 124.309 134.264 109.774 1.00 72.35  ? 114 LEU A C   1 
ATOM   850  O  O   . LEU A 1 133 ? 125.197 134.811 109.106 1.00 72.35  ? 114 LEU A O   1 
ATOM   851  C  CB  . LEU A 1 133 ? 124.068 131.770 109.903 1.00 72.35  ? 114 LEU A CB  1 
ATOM   852  C  CG  . LEU A 1 133 ? 124.547 130.437 110.471 1.00 72.35  ? 114 LEU A CG  1 
ATOM   853  C  CD1 . LEU A 1 133 ? 123.887 129.275 109.750 1.00 72.35  ? 114 LEU A CD1 1 
ATOM   854  C  CD2 . LEU A 1 133 ? 126.056 130.352 110.357 1.00 72.35  ? 114 LEU A CD2 1 
ATOM   855  N  N   . CYS A 1 134 ? 123.058 134.729 109.810 1.00 72.07  ? 115 CYS A N   1 
ATOM   856  C  CA  . CYS A 1 134 ? 122.706 135.957 109.106 1.00 72.07  ? 115 CYS A CA  1 
ATOM   857  C  C   . CYS A 1 134 ? 123.473 137.144 109.667 1.00 72.07  ? 115 CYS A C   1 
ATOM   858  O  O   . CYS A 1 134 ? 123.935 138.009 108.913 1.00 72.07  ? 115 CYS A O   1 
ATOM   859  C  CB  . CYS A 1 134 ? 121.201 136.206 109.196 1.00 72.07  ? 115 CYS A CB  1 
ATOM   860  S  SG  . CYS A 1 134 ? 120.183 134.727 109.040 1.00 72.07  ? 115 CYS A SG  1 
ATOM   861  N  N   . PHE A 1 135 ? 123.614 137.203 110.993 1.00 73.47  ? 116 PHE A N   1 
ATOM   862  C  CA  . PHE A 1 135 ? 124.386 138.272 111.619 1.00 73.47  ? 116 PHE A CA  1 
ATOM   863  C  C   . PHE A 1 135 ? 125.816 138.294 111.097 1.00 73.47  ? 116 PHE A C   1 
ATOM   864  O  O   . PHE A 1 135 ? 126.329 139.345 110.695 1.00 73.47  ? 116 PHE A O   1 
ATOM   865  C  CB  . PHE A 1 135 ? 124.377 138.091 113.136 1.00 73.47  ? 116 PHE A CB  1 
ATOM   866  C  CG  . PHE A 1 135 ? 125.006 139.224 113.886 1.00 73.47  ? 116 PHE A CG  1 
ATOM   867  C  CD1 . PHE A 1 135 ? 124.935 140.516 113.404 1.00 73.47  ? 116 PHE A CD1 1 
ATOM   868  C  CD2 . PHE A 1 135 ? 125.690 138.991 115.064 1.00 73.47  ? 116 PHE A CD2 1 
ATOM   869  C  CE1 . PHE A 1 135 ? 125.518 141.559 114.093 1.00 73.47  ? 116 PHE A CE1 1 
ATOM   870  C  CE2 . PHE A 1 135 ? 126.273 140.029 115.757 1.00 73.47  ? 116 PHE A CE2 1 
ATOM   871  C  CZ  . PHE A 1 135 ? 126.188 141.313 115.271 1.00 73.47  ? 116 PHE A CZ  1 
ATOM   872  N  N   . GLU A 1 136 ? 126.475 137.133 111.098 1.00 74.74  ? 117 GLU A N   1 
ATOM   873  C  CA  . GLU A 1 136 ? 127.862 137.057 110.654 1.00 74.74  ? 117 GLU A CA  1 
ATOM   874  C  C   . GLU A 1 136 ? 127.992 137.426 109.184 1.00 74.74  ? 117 GLU A C   1 
ATOM   875  O  O   . GLU A 1 136 ? 128.904 138.170 108.801 1.00 74.74  ? 117 GLU A O   1 
ATOM   876  C  CB  . GLU A 1 136 ? 128.415 135.654 110.907 1.00 74.74  ? 117 GLU A CB  1 
ATOM   877  C  CG  . GLU A 1 136 ? 129.788 135.387 110.301 1.00 74.74  ? 117 GLU A CG  1 
ATOM   878  C  CD  . GLU A 1 136 ? 130.930 135.993 111.102 1.00 74.74  ? 117 GLU A CD  1 
ATOM   879  O  OE1 . GLU A 1 136 ? 130.792 137.129 111.603 1.00 74.74  ? 117 GLU A OE1 1 
ATOM   880  O  OE2 . GLU A 1 136 ? 131.977 135.324 111.231 1.00 74.74  ? 117 GLU A OE2 1 
ATOM   881  N  N   . LEU A 1 137 ? 127.088 136.918 108.342 1.00 71.70  ? 118 LEU A N   1 
ATOM   882  C  CA  . LEU A 1 137 ? 127.171 137.212 106.916 1.00 71.70  ? 118 LEU A CA  1 
ATOM   883  C  C   . LEU A 1 137 ? 126.960 138.697 106.645 1.00 71.70  ? 118 LEU A C   1 
ATOM   884  O  O   . LEU A 1 137 ? 127.695 139.300 105.853 1.00 71.70  ? 118 LEU A O   1 
ATOM   885  C  CB  . LEU A 1 137 ? 126.154 136.371 106.146 1.00 71.70  ? 118 LEU A CB  1 
ATOM   886  C  CG  . LEU A 1 137 ? 126.226 136.449 104.621 1.00 71.70  ? 118 LEU A CG  1 
ATOM   887  C  CD1 . LEU A 1 137 ? 127.667 136.381 104.145 1.00 71.70  ? 118 LEU A CD1 1 
ATOM   888  C  CD2 . LEU A 1 137 ? 125.405 135.334 103.998 1.00 71.70  ? 118 LEU A CD2 1 
ATOM   889  N  N   . ALA A 1 138 ? 125.967 139.307 107.298 1.00 71.98  ? 119 ALA A N   1 
ATOM   890  C  CA  . ALA A 1 138 ? 125.718 140.731 107.099 1.00 71.98  ? 119 ALA A CA  1 
ATOM   891  C  C   . ALA A 1 138 ? 126.885 141.570 107.599 1.00 71.98  ? 119 ALA A C   1 
ATOM   892  O  O   . ALA A 1 138 ? 127.282 142.545 106.948 1.00 71.98  ? 119 ALA A O   1 
ATOM   893  C  CB  . ALA A 1 138 ? 124.423 141.141 107.798 1.00 71.98  ? 119 ALA A CB  1 
ATOM   894  N  N   . SER A 1 139 ? 127.450 141.208 108.754 1.00 73.25  ? 120 SER A N   1 
ATOM   895  C  CA  . SER A 1 139 ? 128.599 141.940 109.271 1.00 73.25  ? 120 SER A CA  1 
ATOM   896  C  C   . SER A 1 139 ? 129.784 141.844 108.321 1.00 73.25  ? 120 SER A C   1 
ATOM   897  O  O   . SER A 1 139 ? 130.458 142.846 108.058 1.00 73.25  ? 120 SER A O   1 
ATOM   898  C  CB  . SER A 1 139 ? 128.977 141.415 110.655 1.00 73.25  ? 120 SER A CB  1 
ATOM   899  O  OG  . SER A 1 139 ? 130.326 141.719 110.963 1.00 73.25  ? 120 SER A OG  1 
ATOM   900  N  N   . ARG A 1 140 ? 130.047 140.649 107.786 1.00 76.57  ? 121 ARG A N   1 
ATOM   901  C  CA  . ARG A 1 140 ? 131.150 140.487 106.845 1.00 76.57  ? 121 ARG A CA  1 
ATOM   902  C  C   . ARG A 1 140 ? 130.919 141.294 105.575 1.00 76.57  ? 121 ARG A C   1 
ATOM   903  O  O   . ARG A 1 140 ? 131.841 141.947 105.070 1.00 76.57  ? 121 ARG A O   1 
ATOM   904  C  CB  . ARG A 1 140 ? 131.345 139.009 106.513 1.00 76.57  ? 121 ARG A CB  1 
ATOM   905  C  CG  . ARG A 1 140 ? 132.107 138.234 107.570 1.00 76.57  ? 121 ARG A CG  1 
ATOM   906  C  CD  . ARG A 1 140 ? 133.579 138.131 107.213 1.00 76.57  ? 121 ARG A CD  1 
ATOM   907  N  NE  . ARG A 1 140 ? 134.409 137.873 108.383 1.00 76.57  ? 121 ARG A NE  1 
ATOM   908  C  CZ  . ARG A 1 140 ? 135.653 138.308 108.528 1.00 76.57  ? 121 ARG A CZ  1 
ATOM   909  N  NH1 . ARG A 1 140 ? 136.249 139.023 107.588 1.00 76.57  ? 121 ARG A NH1 1 
ATOM   910  N  NH2 . ARG A 1 140 ? 136.316 138.017 109.643 1.00 76.57  ? 121 ARG A NH2 1 
ATOM   911  N  N   . ILE A 1 141 ? 129.694 141.266 105.046 1.00 74.55  ? 122 ILE A N   1 
ATOM   912  C  CA  . ILE A 1 141 ? 129.393 142.003 103.820 1.00 74.55  ? 122 ILE A CA  1 
ATOM   913  C  C   . ILE A 1 141 ? 129.586 143.498 104.038 1.00 74.55  ? 122 ILE A C   1 
ATOM   914  O  O   . ILE A 1 141 ? 130.212 144.188 103.224 1.00 74.55  ? 122 ILE A O   1 
ATOM   915  C  CB  . ILE A 1 141 ? 127.966 141.685 103.339 1.00 74.55  ? 122 ILE A CB  1 
ATOM   916  C  CG1 . ILE A 1 141 ? 127.882 140.245 102.829 1.00 74.55  ? 122 ILE A CG1 1 
ATOM   917  C  CG2 . ILE A 1 141 ? 127.534 142.672 102.266 1.00 74.55  ? 122 ILE A CG2 1 
ATOM   918  C  CD1 . ILE A 1 141 ? 126.724 139.992 101.891 1.00 74.55  ? 122 ILE A CD1 1 
ATOM   919  N  N   . LEU A 1 142 ? 129.056 144.020 105.147 1.00 74.60  ? 123 LEU A N   1 
ATOM   920  C  CA  . LEU A 1 142 ? 129.176 145.449 105.413 1.00 74.60  ? 123 LEU A CA  1 
ATOM   921  C  C   . LEU A 1 142 ? 130.622 145.852 105.674 1.00 74.60  ? 123 LEU A C   1 
ATOM   922  O  O   . LEU A 1 142 ? 131.061 146.917 105.226 1.00 74.60  ? 123 LEU A O   1 
ATOM   923  C  CB  . LEU A 1 142 ? 128.280 145.841 106.586 1.00 74.60  ? 123 LEU A CB  1 
ATOM   924  C  CG  . LEU A 1 142 ? 126.806 146.017 106.216 1.00 74.60  ? 123 LEU A CG  1 
ATOM   925  C  CD1 . LEU A 1 142 ? 126.049 146.705 107.331 1.00 74.60  ? 123 LEU A CD1 1 
ATOM   926  C  CD2 . LEU A 1 142 ? 126.666 146.795 104.916 1.00 74.60  ? 123 LEU A CD2 1 
ATOM   927  N  N   . SER A 1 143 ? 131.383 145.015 106.385 1.00 78.68  ? 124 SER A N   1 
ATOM   928  C  CA  . SER A 1 143 ? 132.788 145.325 106.624 1.00 78.68  ? 124 SER A CA  1 
ATOM   929  C  C   . SER A 1 143 ? 133.583 145.335 105.324 1.00 78.68  ? 124 SER A C   1 
ATOM   930  O  O   . SER A 1 143 ? 134.434 146.208 105.116 1.00 78.68  ? 124 SER A O   1 
ATOM   931  C  CB  . SER A 1 143 ? 133.386 144.323 107.610 1.00 78.68  ? 124 SER A CB  1 
ATOM   932  O  OG  . SER A 1 143 ? 134.717 144.671 107.947 1.00 78.68  ? 124 SER A OG  1 
ATOM   933  N  N   . ASP A 1 144 ? 133.327 144.369 104.439 1.00 81.74  ? 125 ASP A N   1 
ATOM   934  C  CA  . ASP A 1 144 ? 134.023 144.345 103.157 1.00 81.74  ? 125 ASP A CA  1 
ATOM   935  C  C   . ASP A 1 144 ? 133.649 145.546 102.299 1.00 81.74  ? 125 ASP A C   1 
ATOM   936  O  O   . ASP A 1 144 ? 134.512 146.132 101.635 1.00 81.74  ? 125 ASP A O   1 
ATOM   937  C  CB  . ASP A 1 144 ? 133.724 143.041 102.420 1.00 81.74  ? 125 ASP A CB  1 
ATOM   938  C  CG  . ASP A 1 144 ? 134.547 141.879 102.937 1.00 81.74  ? 125 ASP A CG  1 
ATOM   939  O  OD1 . ASP A 1 144 ? 135.276 142.063 103.935 1.00 81.74  ? 125 ASP A OD1 1 
ATOM   940  O  OD2 . ASP A 1 144 ? 134.473 140.784 102.344 1.00 81.74  ? 125 ASP A OD2 1 
ATOM   941  N  N   . LEU A 1 145 ? 132.370 145.928 102.295 1.00 78.33  ? 126 LEU A N   1 
ATOM   942  C  CA  . LEU A 1 145 ? 131.955 147.088 101.514 1.00 78.33  ? 126 LEU A CA  1 
ATOM   943  C  C   . LEU A 1 145 ? 132.521 148.383 102.084 1.00 78.33  ? 126 LEU A C   1 
ATOM   944  O  O   . LEU A 1 145 ? 132.817 149.313 101.325 1.00 78.33  ? 126 LEU A O   1 
ATOM   945  C  CB  . LEU A 1 145 ? 130.430 147.150 101.438 1.00 78.33  ? 126 LEU A CB  1 
ATOM   946  C  CG  . LEU A 1 145 ? 129.801 146.151 100.464 1.00 78.33  ? 126 LEU A CG  1 
ATOM   947  C  CD1 . LEU A 1 145 ? 128.306 146.383 100.329 1.00 78.33  ? 126 LEU A CD1 1 
ATOM   948  C  CD2 . LEU A 1 145 ? 130.482 146.232 99.108  1.00 78.33  ? 126 LEU A CD2 1 
ATOM   949  N  N   . GLY A 1 146 ? 132.685 148.460 103.401 1.00 77.61  ? 127 GLY A N   1 
ATOM   950  C  CA  . GLY A 1 146 ? 133.314 149.628 103.998 1.00 77.61  ? 127 GLY A CA  1 
ATOM   951  C  C   . GLY A 1 146 ? 132.460 150.869 103.832 1.00 77.61  ? 127 GLY A C   1 
ATOM   952  O  O   . GLY A 1 146 ? 131.249 150.856 104.078 1.00 77.61  ? 127 GLY A O   1 
ATOM   953  N  N   . ASN A 1 147 ? 133.096 151.958 103.412 1.00 80.57  ? 128 ASN A N   1 
ATOM   954  C  CA  . ASN A 1 147 ? 132.426 153.237 103.222 1.00 80.57  ? 128 ASN A CA  1 
ATOM   955  C  C   . ASN A 1 147 ? 131.833 153.404 101.829 1.00 80.57  ? 128 ASN A C   1 
ATOM   956  O  O   . ASN A 1 147 ? 131.225 154.443 101.551 1.00 80.57  ? 128 ASN A O   1 
ATOM   957  C  CB  . ASN A 1 147 ? 133.398 154.386 103.545 1.00 80.57  ? 128 ASN A CB  1 
ATOM   958  C  CG  . ASN A 1 147 ? 134.494 154.569 102.495 1.00 80.57  ? 128 ASN A CG  1 
ATOM   959  O  OD1 . ASN A 1 147 ? 134.242 154.609 101.290 1.00 80.57  ? 128 ASN A OD1 1 
ATOM   960  N  ND2 . ASN A 1 147 ? 135.731 154.681 102.965 1.00 80.57  ? 128 ASN A ND2 1 
ATOM   961  N  N   . SER A 1 148 ? 131.998 152.414 100.949 1.00 81.95  ? 129 SER A N   1 
ATOM   962  C  CA  . SER A 1 148 ? 131.491 152.531 99.588  1.00 81.95  ? 129 SER A CA  1 
ATOM   963  C  C   . SER A 1 148 ? 129.970 152.564 99.530  1.00 81.95  ? 129 SER A C   1 
ATOM   964  O  O   . SER A 1 148 ? 129.413 153.078 98.555  1.00 81.95  ? 129 SER A O   1 
ATOM   965  C  CB  . SER A 1 148 ? 132.016 151.379 98.733  1.00 81.95  ? 129 SER A CB  1 
ATOM   966  O  OG  . SER A 1 148 ? 133.361 151.075 99.058  1.00 81.95  ? 129 SER A OG  1 
ATOM   967  N  N   . VAL A 1 149 ? 129.286 152.034 100.546 1.00 79.53  ? 130 VAL A N   1 
ATOM   968  C  CA  . VAL A 1 149 ? 127.832 151.980 100.562 1.00 79.53  ? 130 VAL A CA  1 
ATOM   969  C  C   . VAL A 1 149 ? 127.322 152.611 101.850 1.00 79.53  ? 130 VAL A C   1 
ATOM   970  O  O   . VAL A 1 149 ? 128.029 152.693 102.856 1.00 79.53  ? 130 VAL A O   1 
ATOM   971  C  CB  . VAL A 1 149 ? 127.296 150.538 100.430 1.00 79.53  ? 130 VAL A CB  1 
ATOM   972  C  CG1 . VAL A 1 149 ? 127.823 149.886 99.162  1.00 79.53  ? 130 VAL A CG1 1 
ATOM   973  C  CG2 . VAL A 1 149 ? 127.666 149.721 101.655 1.00 79.53  ? 130 VAL A CG2 1 
ATOM   974  N  N   . SER A 1 150 ? 126.074 153.067 101.800 1.00 76.51  ? 131 SER A N   1 
ATOM   975  C  CA  . SER A 1 150 ? 125.382 153.618 102.956 1.00 76.51  ? 131 SER A CA  1 
ATOM   976  C  C   . SER A 1 150 ? 124.129 152.797 103.215 1.00 76.51  ? 131 SER A C   1 
ATOM   977  O  O   . SER A 1 150 ? 123.318 152.593 102.306 1.00 76.51  ? 131 SER A O   1 
ATOM   978  C  CB  . SER A 1 150 ? 125.020 155.088 102.733 1.00 76.51  ? 131 SER A CB  1 
ATOM   979  O  OG  . SER A 1 150 ? 126.184 155.881 102.579 1.00 76.51  ? 131 SER A OG  1 
ATOM   980  N  N   . VAL A 1 151 ? 123.972 152.330 104.452 1.00 72.01  ? 132 VAL A N   1 
ATOM   981  C  CA  . VAL A 1 151 ? 122.845 151.470 104.793 1.00 72.01  ? 132 VAL A CA  1 
ATOM   982  C  C   . VAL A 1 151 ? 121.574 152.306 104.844 1.00 72.01  ? 132 VAL A C   1 
ATOM   983  O  O   . VAL A 1 151 ? 121.486 153.283 105.597 1.00 72.01  ? 132 VAL A O   1 
ATOM   984  C  CB  . VAL A 1 151 ? 123.088 150.748 106.124 1.00 72.01  ? 132 VAL A CB  1 
ATOM   985  C  CG1 . VAL A 1 151 ? 121.890 149.885 106.480 1.00 72.01  ? 132 VAL A CG1 1 
ATOM   986  C  CG2 . VAL A 1 151 ? 124.350 149.907 106.045 1.00 72.01  ? 132 VAL A CG2 1 
ATOM   987  N  N   . VAL A 1 152 ? 120.584 151.925 104.044 1.00 74.13  ? 133 VAL A N   1 
ATOM   988  C  CA  . VAL A 1 152 ? 119.293 152.605 104.048 1.00 74.13  ? 133 VAL A CA  1 
ATOM   989  C  C   . VAL A 1 152 ? 118.306 151.902 104.969 1.00 74.13  ? 133 VAL A C   1 
ATOM   990  O  O   . VAL A 1 152 ? 117.679 152.533 105.823 1.00 74.13  ? 133 VAL A O   1 
ATOM   991  C  CB  . VAL A 1 152 ? 118.743 152.709 102.610 1.00 74.13  ? 133 VAL A CB  1 
ATOM   992  C  CG1 . VAL A 1 152 ? 117.367 153.354 102.614 1.00 74.13  ? 133 VAL A CG1 1 
ATOM   993  C  CG2 . VAL A 1 152 ? 119.701 153.496 101.735 1.00 74.13  ? 133 VAL A CG2 1 
ATOM   994  N  N   . ASP A 1 153 ? 118.159 150.588 104.814 1.00 75.47  ? 134 ASP A N   1 
ATOM   995  C  CA  . ASP A 1 153 ? 117.264 149.804 105.652 1.00 75.47  ? 134 ASP A CA  1 
ATOM   996  C  C   . ASP A 1 153 ? 117.958 148.518 106.069 1.00 75.47  ? 134 ASP A C   1 
ATOM   997  O  O   . ASP A 1 153 ? 118.689 147.915 105.279 1.00 75.47  ? 134 ASP A O   1 
ATOM   998  C  CB  . ASP A 1 153 ? 115.951 149.474 104.929 1.00 75.47  ? 134 ASP A CB  1 
ATOM   999  C  CG  . ASP A 1 153 ? 114.945 150.606 104.999 1.00 75.47  ? 134 ASP A CG  1 
ATOM   1000 O  OD1 . ASP A 1 153 ? 115.277 151.730 104.572 1.00 75.47  ? 134 ASP A OD1 1 
ATOM   1001 O  OD2 . ASP A 1 153 ? 113.819 150.371 105.486 1.00 75.47  ? 134 ASP A OD2 1 
ATOM   1002 N  N   . SER A 1 154 ? 117.710 148.096 107.308 1.00 71.80  ? 135 SER A N   1 
ATOM   1003 C  CA  . SER A 1 154 ? 118.263 146.845 107.824 1.00 71.80  ? 135 SER A CA  1 
ATOM   1004 C  C   . SER A 1 154 ? 117.222 146.242 108.761 1.00 71.80  ? 135 SER A C   1 
ATOM   1005 O  O   . SER A 1 154 ? 117.071 146.698 109.898 1.00 71.80  ? 135 SER A O   1 
ATOM   1006 C  CB  . SER A 1 154 ? 119.587 147.080 108.536 1.00 71.80  ? 135 SER A CB  1 
ATOM   1007 O  OG  . SER A 1 154 ? 120.072 145.882 109.115 1.00 71.80  ? 135 SER A OG  1 
ATOM   1008 N  N   . VAL A 1 155 ? 116.514 145.223 108.282 1.00 67.68  ? 136 VAL A N   1 
ATOM   1009 C  CA  . VAL A 1 155 ? 115.402 144.625 109.010 1.00 67.68  ? 136 VAL A CA  1 
ATOM   1010 C  C   . VAL A 1 155 ? 115.757 143.185 109.348 1.00 67.68  ? 136 VAL A C   1 
ATOM   1011 O  O   . VAL A 1 155 ? 116.159 142.416 108.468 1.00 67.68  ? 136 VAL A O   1 
ATOM   1012 C  CB  . VAL A 1 155 ? 114.098 144.687 108.196 1.00 67.68  ? 136 VAL A CB  1 
ATOM   1013 C  CG1 . VAL A 1 155 ? 112.959 144.061 108.977 1.00 67.68  ? 136 VAL A CG1 1 
ATOM   1014 C  CG2 . VAL A 1 155 ? 113.773 146.125 107.831 1.00 67.68  ? 136 VAL A CG2 1 
ATOM   1015 N  N   . GLN A 1 156 ? 115.606 142.825 110.621 1.00 65.52  ? 137 GLN A N   1 
ATOM   1016 C  CA  . GLN A 1 156 ? 115.867 141.472 111.099 1.00 65.52  ? 137 GLN A CA  1 
ATOM   1017 C  C   . GLN A 1 156 ? 114.530 140.780 111.331 1.00 65.52  ? 137 GLN A C   1 
ATOM   1018 O  O   . GLN A 1 156 ? 113.825 141.085 112.299 1.00 65.52  ? 137 GLN A O   1 
ATOM   1019 C  CB  . GLN A 1 156 ? 116.699 141.494 112.378 1.00 65.52  ? 137 GLN A CB  1 
ATOM   1020 C  CG  . GLN A 1 156 ? 118.118 141.992 112.193 1.00 65.52  ? 137 GLN A CG  1 
ATOM   1021 C  CD  . GLN A 1 156 ? 118.625 142.752 113.400 1.00 65.52  ? 137 GLN A CD  1 
ATOM   1022 O  OE1 . GLN A 1 156 ? 118.321 143.931 113.578 1.00 65.52  ? 137 GLN A OE1 1 
ATOM   1023 N  NE2 . GLN A 1 156 ? 119.396 142.076 114.242 1.00 65.52  ? 137 GLN A NE2 1 
ATOM   1024 N  N   . GLY A 1 157 ? 114.185 139.849 110.450 1.00 67.36  ? 138 GLY A N   1 
ATOM   1025 C  CA  . GLY A 1 157 ? 112.945 139.109 110.548 1.00 67.36  ? 138 GLY A CA  1 
ATOM   1026 C  C   . GLY A 1 157 ? 113.157 137.703 111.078 1.00 67.36  ? 138 GLY A C   1 
ATOM   1027 O  O   . GLY A 1 157 ? 114.221 137.110 110.908 1.00 67.36  ? 138 GLY A O   1 
ATOM   1028 N  N   . PHE A 1 158 ? 112.115 137.168 111.707 1.00 67.80  ? 139 PHE A N   1 
ATOM   1029 C  CA  . PHE A 1 158 ? 112.160 135.854 112.328 1.00 67.80  ? 139 PHE A CA  1 
ATOM   1030 C  C   . PHE A 1 158 ? 110.846 135.134 112.068 1.00 67.80  ? 139 PHE A C   1 
ATOM   1031 O  O   . PHE A 1 158 ? 109.805 135.764 111.868 1.00 67.80  ? 139 PHE A O   1 
ATOM   1032 C  CB  . PHE A 1 158 ? 112.412 135.954 113.836 1.00 67.80  ? 139 PHE A CB  1 
ATOM   1033 C  CG  . PHE A 1 158 ? 111.503 136.921 114.533 1.00 67.80  ? 139 PHE A CG  1 
ATOM   1034 C  CD1 . PHE A 1 158 ? 110.263 136.519 114.996 1.00 67.80  ? 139 PHE A CD1 1 
ATOM   1035 C  CD2 . PHE A 1 158 ? 111.889 138.235 114.722 1.00 67.80  ? 139 PHE A CD2 1 
ATOM   1036 C  CE1 . PHE A 1 158 ? 109.427 137.410 115.632 1.00 67.80  ? 139 PHE A CE1 1 
ATOM   1037 C  CE2 . PHE A 1 158 ? 111.058 139.129 115.358 1.00 67.80  ? 139 PHE A CE2 1 
ATOM   1038 C  CZ  . PHE A 1 158 ? 109.827 138.716 115.813 1.00 67.80  ? 139 PHE A CZ  1 
ATOM   1039 N  N   . ARG A 1 159 ? 110.904 133.806 112.076 1.00 76.64  ? 140 ARG A N   1 
ATOM   1040 C  CA  . ARG A 1 159 ? 109.706 132.995 111.906 1.00 76.64  ? 140 ARG A CA  1 
ATOM   1041 C  C   . ARG A 1 159 ? 108.894 133.021 113.193 1.00 76.64  ? 140 ARG A C   1 
ATOM   1042 O  O   . ARG A 1 159 ? 109.424 132.762 114.277 1.00 76.64  ? 140 ARG A O   1 
ATOM   1043 C  CB  . ARG A 1 159 ? 110.075 131.561 111.530 1.00 76.64  ? 140 ARG A CB  1 
ATOM   1044 C  CG  . ARG A 1 159 ? 108.946 130.563 111.713 1.00 76.64  ? 140 ARG A CG  1 
ATOM   1045 C  CD  . ARG A 1 159 ? 109.331 129.185 111.199 1.00 76.64  ? 140 ARG A CD  1 
ATOM   1046 N  NE  . ARG A 1 159 ? 109.768 128.300 112.272 1.00 76.64  ? 140 ARG A NE  1 
ATOM   1047 C  CZ  . ARG A 1 159 ? 110.330 127.114 112.082 1.00 76.64  ? 140 ARG A CZ  1 
ATOM   1048 N  NH1 . ARG A 1 159 ? 110.545 126.637 110.867 1.00 76.64  ? 140 ARG A NH1 1 
ATOM   1049 N  NH2 . ARG A 1 159 ? 110.682 126.387 113.138 1.00 76.64  ? 140 ARG A NH2 1 
ATOM   1050 N  N   . TYR A 1 160 ? 107.606 133.333 113.072 1.00 73.23  ? 141 TYR A N   1 
ATOM   1051 C  CA  . TYR A 1 160 ? 106.729 133.515 114.223 1.00 73.23  ? 141 TYR A CA  1 
ATOM   1052 C  C   . TYR A 1 160 ? 105.842 132.286 114.379 1.00 73.23  ? 141 TYR A C   1 
ATOM   1053 O  O   . TYR A 1 160 ? 104.931 132.062 113.575 1.00 73.23  ? 141 TYR A O   1 
ATOM   1054 C  CB  . TYR A 1 160 ? 105.888 134.779 114.058 1.00 73.23  ? 141 TYR A CB  1 
ATOM   1055 C  CG  . TYR A 1 160 ? 105.020 135.114 115.247 1.00 73.23  ? 141 TYR A CG  1 
ATOM   1056 C  CD1 . TYR A 1 160 ? 105.570 135.626 116.412 1.00 73.23  ? 141 TYR A CD1 1 
ATOM   1057 C  CD2 . TYR A 1 160 ? 103.646 134.924 115.201 1.00 73.23  ? 141 TYR A CD2 1 
ATOM   1058 C  CE1 . TYR A 1 160 ? 104.778 135.936 117.500 1.00 73.23  ? 141 TYR A CE1 1 
ATOM   1059 C  CE2 . TYR A 1 160 ? 102.846 135.231 116.283 1.00 73.23  ? 141 TYR A CE2 1 
ATOM   1060 C  CZ  . TYR A 1 160 ? 103.416 135.737 117.429 1.00 73.23  ? 141 TYR A CZ  1 
ATOM   1061 O  OH  . TYR A 1 160 ? 102.622 136.044 118.509 1.00 73.23  ? 141 TYR A OH  1 
ATOM   1062 N  N   . PHE A 1 161 ? 106.110 131.502 115.421 1.00 74.13  ? 142 PHE A N   1 
ATOM   1063 C  CA  . PHE A 1 161 ? 105.353 130.289 115.758 1.00 74.13  ? 142 PHE A CA  1 
ATOM   1064 C  C   . PHE A 1 161 ? 105.374 129.355 114.549 1.00 74.13  ? 142 PHE A C   1 
ATOM   1065 O  O   . PHE A 1 161 ? 106.451 129.126 113.977 1.00 74.13  ? 142 PHE A O   1 
ATOM   1066 C  CB  . PHE A 1 161 ? 103.970 130.679 116.261 1.00 74.13  ? 142 PHE A CB  1 
ATOM   1067 C  CG  . PHE A 1 161 ? 103.952 131.132 117.691 1.00 74.13  ? 142 PHE A CG  1 
ATOM   1068 C  CD1 . PHE A 1 161 ? 104.202 132.452 118.018 1.00 74.13  ? 142 PHE A CD1 1 
ATOM   1069 C  CD2 . PHE A 1 161 ? 103.690 130.233 118.709 1.00 74.13  ? 142 PHE A CD2 1 
ATOM   1070 C  CE1 . PHE A 1 161 ? 104.186 132.868 119.334 1.00 74.13  ? 142 PHE A CE1 1 
ATOM   1071 C  CE2 . PHE A 1 161 ? 103.674 130.642 120.026 1.00 74.13  ? 142 PHE A CE2 1 
ATOM   1072 C  CZ  . PHE A 1 161 ? 103.922 131.961 120.339 1.00 74.13  ? 142 PHE A CZ  1 
ATOM   1073 N  N   . ASP A 1 162 ? 104.238 128.807 114.131 1.00 79.99  ? 143 ASP A N   1 
ATOM   1074 C  CA  . ASP A 1 162 ? 104.181 127.829 113.048 1.00 79.99  ? 143 ASP A CA  1 
ATOM   1075 C  C   . ASP A 1 162 ? 103.827 128.517 111.730 1.00 79.99  ? 143 ASP A C   1 
ATOM   1076 O  O   . ASP A 1 162 ? 102.721 128.403 111.199 1.00 79.99  ? 143 ASP A O   1 
ATOM   1077 C  CB  . ASP A 1 162 ? 103.186 126.730 113.407 1.00 79.99  ? 143 ASP A CB  1 
ATOM   1078 C  CG  . ASP A 1 162 ? 101.861 127.289 113.889 1.00 79.99  ? 143 ASP A CG  1 
ATOM   1079 O  OD1 . ASP A 1 162 ? 101.871 128.357 114.536 1.00 79.99  ? 143 ASP A OD1 1 
ATOM   1080 O  OD2 . ASP A 1 162 ? 100.813 126.661 113.649 1.00 79.99  ? 143 ASP A OD2 1 
ATOM   1081 N  N   . ASP A 1 163 ? 104.815 129.247 111.208 1.00 79.87  ? 144 ASP A N   1 
ATOM   1082 C  CA  . ASP A 1 163 ? 104.712 129.944 109.924 1.00 79.87  ? 144 ASP A CA  1 
ATOM   1083 C  C   . ASP A 1 163 ? 103.555 130.938 109.901 1.00 79.87  ? 144 ASP A C   1 
ATOM   1084 O  O   . ASP A 1 163 ? 102.961 131.190 108.850 1.00 79.87  ? 144 ASP A O   1 
ATOM   1085 C  CB  . ASP A 1 163 ? 104.588 128.954 108.762 1.00 79.87  ? 144 ASP A CB  1 
ATOM   1086 C  CG  . ASP A 1 163 ? 105.818 128.083 108.606 1.00 79.87  ? 144 ASP A CG  1 
ATOM   1087 O  OD1 . ASP A 1 163 ? 106.881 128.453 109.147 1.00 79.87  ? 144 ASP A OD1 1 
ATOM   1088 O  OD2 . ASP A 1 163 ? 105.724 127.031 107.941 1.00 79.87  ? 144 ASP A OD2 1 
ATOM   1089 N  N   . ARG A 1 164 ? 103.225 131.510 111.052 1.00 77.18  ? 145 ARG A N   1 
ATOM   1090 C  CA  . ARG A 1 164 ? 102.188 132.524 111.149 1.00 77.18  ? 145 ARG A CA  1 
ATOM   1091 C  C   . ARG A 1 164 ? 102.810 133.914 111.149 1.00 77.18  ? 145 ARG A C   1 
ATOM   1092 O  O   . ARG A 1 164 ? 103.927 134.113 111.632 1.00 77.18  ? 145 ARG A O   1 
ATOM   1093 C  CB  . ARG A 1 164 ? 101.348 132.327 112.412 1.00 77.18  ? 145 ARG A CB  1 
ATOM   1094 C  CG  . ARG A 1 164 ? 100.577 131.020 112.436 1.00 77.18  ? 145 ARG A CG  1 
ATOM   1095 C  CD  . ARG A 1 164 ? 99.747  130.884 113.699 1.00 77.18  ? 145 ARG A CD  1 
ATOM   1096 N  NE  . ARG A 1 164 ? 99.044  129.607 113.745 1.00 77.18  ? 145 ARG A NE  1 
ATOM   1097 C  CZ  . ARG A 1 164 ? 97.869  129.380 113.176 1.00 77.18  ? 145 ARG A CZ  1 
ATOM   1098 N  NH1 . ARG A 1 164 ? 97.227  130.327 112.513 1.00 77.18  ? 145 ARG A NH1 1 
ATOM   1099 N  NH2 . ARG A 1 164 ? 97.322  128.172 113.276 1.00 77.18  ? 145 ARG A NH2 1 
ATOM   1100 N  N   . ASP A 1 165 ? 102.078 134.875 110.597 1.00 77.98  ? 146 ASP A N   1 
ATOM   1101 C  CA  . ASP A 1 165 ? 102.496 136.264 110.657 1.00 77.98  ? 146 ASP A CA  1 
ATOM   1102 C  C   . ASP A 1 165 ? 101.924 136.919 111.913 1.00 77.98  ? 146 ASP A C   1 
ATOM   1103 O  O   . ASP A 1 165 ? 101.233 136.287 112.715 1.00 77.98  ? 146 ASP A O   1 
ATOM   1104 C  CB  . ASP A 1 165 ? 102.093 137.001 109.378 1.00 77.98  ? 146 ASP A CB  1 
ATOM   1105 C  CG  . ASP A 1 165 ? 100.595 136.983 109.130 1.00 77.98  ? 146 ASP A CG  1 
ATOM   1106 O  OD1 . ASP A 1 165 ? 99.824  137.391 110.022 1.00 77.98  ? 146 ASP A OD1 1 
ATOM   1107 O  OD2 . ASP A 1 165 ? 100.186 136.560 108.029 1.00 77.98  ? 146 ASP A OD2 1 
ATOM   1108 N  N   . LEU A 1 166 ? 102.216 138.209 112.090 1.00 76.73  ? 147 LEU A N   1 
ATOM   1109 C  CA  . LEU A 1 166 ? 101.803 138.903 113.305 1.00 76.73  ? 147 LEU A CA  1 
ATOM   1110 C  C   . LEU A 1 166 ? 100.294 139.081 113.402 1.00 76.73  ? 147 LEU A C   1 
ATOM   1111 O  O   . LEU A 1 166 ? 99.790  139.380 114.489 1.00 76.73  ? 147 LEU A O   1 
ATOM   1112 C  CB  . LEU A 1 166 ? 102.495 140.263 113.390 1.00 76.73  ? 147 LEU A CB  1 
ATOM   1113 C  CG  . LEU A 1 166 ? 104.008 140.191 113.597 1.00 76.73  ? 147 LEU A CG  1 
ATOM   1114 C  CD1 . LEU A 1 166 ? 104.589 141.571 113.840 1.00 76.73  ? 147 LEU A CD1 1 
ATOM   1115 C  CD2 . LEU A 1 166 ? 104.336 139.255 114.746 1.00 76.73  ? 147 LEU A CD2 1 
ATOM   1116 N  N   . LEU A 1 167 ? 99.562  138.906 112.302 1.00 79.23  ? 148 LEU A N   1 
ATOM   1117 C  CA  . LEU A 1 167 ? 98.110  139.002 112.348 1.00 79.23  ? 148 LEU A CA  1 
ATOM   1118 C  C   . LEU A 1 167 ? 97.445  137.710 112.800 1.00 79.23  ? 148 LEU A C   1 
ATOM   1119 O  O   . LEU A 1 167 ? 96.222  137.692 112.978 1.00 79.23  ? 148 LEU A O   1 
ATOM   1120 C  CB  . LEU A 1 167 ? 97.566  139.408 110.976 1.00 79.23  ? 148 LEU A CB  1 
ATOM   1121 C  CG  . LEU A 1 167 ? 98.223  140.633 110.339 1.00 79.23  ? 148 LEU A CG  1 
ATOM   1122 C  CD1 . LEU A 1 167 ? 97.555  140.969 109.021 1.00 79.23  ? 148 LEU A CD1 1 
ATOM   1123 C  CD2 . LEU A 1 167 ? 98.175  141.823 111.283 1.00 79.23  ? 148 LEU A CD2 1 
ATOM   1124 N  N   . GLY A 1 168 ? 98.211  136.637 112.991 1.00 79.84  ? 149 GLY A N   1 
ATOM   1125 C  CA  . GLY A 1 168 ? 97.675  135.383 113.470 1.00 79.84  ? 149 GLY A CA  1 
ATOM   1126 C  C   . GLY A 1 168 ? 97.258  134.398 112.401 1.00 79.84  ? 149 GLY A C   1 
ATOM   1127 O  O   . GLY A 1 168 ? 96.782  133.307 112.741 1.00 79.84  ? 149 GLY A O   1 
ATOM   1128 N  N   . PHE A 1 169 ? 97.421  134.735 111.126 1.00 79.74  ? 150 PHE A N   1 
ATOM   1129 C  CA  . PHE A 1 169 ? 97.030  133.862 110.030 1.00 79.74  ? 150 PHE A CA  1 
ATOM   1130 C  C   . PHE A 1 169 ? 98.262  133.225 109.403 1.00 79.74  ? 150 PHE A C   1 
ATOM   1131 O  O   . PHE A 1 169 ? 99.303  133.872 109.258 1.00 79.74  ? 150 PHE A O   1 
ATOM   1132 C  CB  . PHE A 1 169 ? 96.242  134.633 108.969 1.00 79.74  ? 150 PHE A CB  1 
ATOM   1133 C  CG  . PHE A 1 169 ? 94.821  134.921 109.361 1.00 79.74  ? 150 PHE A CG  1 
ATOM   1134 C  CD1 . PHE A 1 169 ? 94.524  135.950 110.236 1.00 79.74  ? 150 PHE A CD1 1 
ATOM   1135 C  CD2 . PHE A 1 169 ? 93.783  134.158 108.856 1.00 79.74  ? 150 PHE A CD2 1 
ATOM   1136 C  CE1 . PHE A 1 169 ? 93.218  136.216 110.598 1.00 79.74  ? 150 PHE A CE1 1 
ATOM   1137 C  CE2 . PHE A 1 169 ? 92.475  134.419 109.215 1.00 79.74  ? 150 PHE A CE2 1 
ATOM   1138 C  CZ  . PHE A 1 169 ? 92.193  135.449 110.086 1.00 79.74  ? 150 PHE A CZ  1 
ATOM   1139 N  N   . VAL A 1 170 ? 98.137  131.950 109.034 1.00 80.18  ? 151 VAL A N   1 
ATOM   1140 C  CA  . VAL A 1 170 ? 99.228  131.248 108.370 1.00 80.18  ? 151 VAL A CA  1 
ATOM   1141 C  C   . VAL A 1 170 ? 99.446  131.845 106.987 1.00 80.18  ? 151 VAL A C   1 
ATOM   1142 O  O   . VAL A 1 170 ? 98.496  132.035 106.217 1.00 80.18  ? 151 VAL A O   1 
ATOM   1143 C  CB  . VAL A 1 170 ? 98.933  129.744 108.287 1.00 80.18  ? 151 VAL A CB  1 
ATOM   1144 C  CG1 . VAL A 1 170 ? 100.069 129.021 107.585 1.00 80.18  ? 151 VAL A CG1 1 
ATOM   1145 C  CG2 . VAL A 1 170 ? 98.710  129.172 109.676 1.00 80.18  ? 151 VAL A CG2 1 
ATOM   1146 N  N   . ASP A 1 171 ? 100.701 132.146 106.667 1.00 82.52  ? 152 ASP A N   1 
ATOM   1147 C  CA  . ASP A 1 171 ? 101.069 132.818 105.430 1.00 82.52  ? 152 ASP A CA  1 
ATOM   1148 C  C   . ASP A 1 171 ? 102.027 131.916 104.665 1.00 82.52  ? 152 ASP A C   1 
ATOM   1149 O  O   . ASP A 1 171 ? 102.886 131.260 105.261 1.00 82.52  ? 152 ASP A O   1 
ATOM   1150 C  CB  . ASP A 1 171 ? 101.708 134.190 105.728 1.00 82.52  ? 152 ASP A CB  1 
ATOM   1151 C  CG  . ASP A 1 171 ? 102.388 134.827 104.515 1.00 82.52  ? 152 ASP A CG  1 
ATOM   1152 O  OD1 . ASP A 1 171 ? 102.313 134.295 103.387 1.00 82.52  ? 152 ASP A OD1 1 
ATOM   1153 O  OD2 . ASP A 1 171 ? 103.010 135.893 104.700 1.00 82.52  ? 152 ASP A OD2 1 
ATOM   1154 N  N   . GLY A 1 172 ? 101.876 131.888 103.344 1.00 86.81  ? 153 GLY A N   1 
ATOM   1155 C  CA  . GLY A 1 172 ? 102.725 131.083 102.493 1.00 86.81  ? 153 GLY A CA  1 
ATOM   1156 C  C   . GLY A 1 172 ? 102.127 129.781 102.011 1.00 86.81  ? 153 GLY A C   1 
ATOM   1157 O  O   . GLY A 1 172 ? 102.849 128.976 101.411 1.00 86.81  ? 153 GLY A O   1 
ATOM   1158 N  N   . THR A 1 173 ? 100.837 129.541 102.262 1.00 85.98  ? 154 THR A N   1 
ATOM   1159 C  CA  . THR A 1 173 ? 100.239 128.252 101.927 1.00 85.98  ? 154 THR A CA  1 
ATOM   1160 C  C   . THR A 1 173 ? 100.174 128.046 100.418 1.00 85.98  ? 154 THR A C   1 
ATOM   1161 O  O   . THR A 1 173 ? 100.533 126.977 99.910  1.00 85.98  ? 154 THR A O   1 
ATOM   1162 C  CB  . THR A 1 173 ? 98.839  128.156 102.541 1.00 85.98  ? 154 THR A CB  1 
ATOM   1163 O  OG1 . THR A 1 173 ? 98.939  127.790 103.922 1.00 85.98  ? 154 THR A OG1 1 
ATOM   1164 C  CG2 . THR A 1 173 ? 97.999  127.118 101.812 1.00 85.98  ? 154 THR A CG2 1 
ATOM   1165 N  N   . GLU A 1 174 ? 99.734  129.066 99.681  1.00 88.39  ? 155 GLU A N   1 
ATOM   1166 C  CA  . GLU A 1 174 ? 99.492  128.956 98.250  1.00 88.39  ? 155 GLU A CA  1 
ATOM   1167 C  C   . GLU A 1 174 ? 100.738 129.213 97.408  1.00 88.39  ? 155 GLU A C   1 
ATOM   1168 O  O   . GLU A 1 174 ? 100.614 129.507 96.213  1.00 88.39  ? 155 GLU A O   1 
ATOM   1169 C  CB  . GLU A 1 174 ? 98.375  129.915 97.835  1.00 88.39  ? 155 GLU A CB  1 
ATOM   1170 C  CG  . GLU A 1 174 ? 97.052  129.676 98.546  1.00 88.39  ? 155 GLU A CG  1 
ATOM   1171 C  CD  . GLU A 1 174 ? 96.456  128.316 98.238  1.00 88.39  ? 155 GLU A CD  1 
ATOM   1172 O  OE1 . GLU A 1 174 ? 96.657  127.816 97.112  1.00 88.39  ? 155 GLU A OE1 1 
ATOM   1173 O  OE2 . GLU A 1 174 ? 95.785  127.747 99.124  1.00 88.39  ? 155 GLU A OE2 1 
ATOM   1174 N  N   . ASN A 1 175 ? 101.926 129.112 97.993  1.00 89.07  ? 156 ASN A N   1 
ATOM   1175 C  CA  . ASN A 1 175 ? 103.141 129.322 97.222  1.00 89.07  ? 156 ASN A CA  1 
ATOM   1176 C  C   . ASN A 1 175 ? 103.398 128.131 96.301  1.00 89.07  ? 156 ASN A C   1 
ATOM   1177 O  O   . ASN A 1 175 ? 103.195 126.980 96.702  1.00 89.07  ? 156 ASN A O   1 
ATOM   1178 C  CB  . ASN A 1 175 ? 104.337 129.530 98.149  1.00 89.07  ? 156 ASN A CB  1 
ATOM   1179 C  CG  . ASN A 1 175 ? 104.510 130.976 98.560  1.00 89.07  ? 156 ASN A CG  1 
ATOM   1180 O  OD1 . ASN A 1 175 ? 103.766 131.852 98.117  1.00 89.07  ? 156 ASN A OD1 1 
ATOM   1181 N  ND2 . ASN A 1 175 ? 105.495 131.236 99.411  1.00 89.07  ? 156 ASN A ND2 1 
ATOM   1182 N  N   . PRO A 1 176 ? 103.835 128.371 95.067  1.00 92.57  ? 157 PRO A N   1 
ATOM   1183 C  CA  . PRO A 1 176 ? 104.210 127.257 94.190  1.00 92.57  ? 157 PRO A CA  1 
ATOM   1184 C  C   . PRO A 1 176 ? 105.418 126.510 94.731  1.00 92.57  ? 157 PRO A C   1 
ATOM   1185 O  O   . PRO A 1 176 ? 106.297 127.085 95.378  1.00 92.57  ? 157 PRO A O   1 
ATOM   1186 C  CB  . PRO A 1 176 ? 104.529 127.944 92.858  1.00 92.57  ? 157 PRO A CB  1 
ATOM   1187 C  CG  . PRO A 1 176 ? 104.871 129.346 93.230  1.00 92.57  ? 157 PRO A CG  1 
ATOM   1188 C  CD  . PRO A 1 176 ? 104.006 129.676 94.408  1.00 92.57  ? 157 PRO A CD  1 
ATOM   1189 N  N   . VAL A 1 177 ? 105.455 125.209 94.457  1.00 96.54  ? 158 VAL A N   1 
ATOM   1190 C  CA  . VAL A 1 177 ? 106.460 124.315 95.018  1.00 96.54  ? 158 VAL A CA  1 
ATOM   1191 C  C   . VAL A 1 177 ? 107.161 123.580 93.883  1.00 96.54  ? 158 VAL A C   1 
ATOM   1192 O  O   . VAL A 1 177 ? 106.519 123.150 92.919  1.00 96.54  ? 158 VAL A O   1 
ATOM   1193 C  CB  . VAL A 1 177 ? 105.830 123.320 96.016  1.00 96.54  ? 158 VAL A CB  1 
ATOM   1194 C  CG1 . VAL A 1 177 ? 104.578 122.689 95.423  1.00 96.54  ? 158 VAL A CG1 1 
ATOM   1195 C  CG2 . VAL A 1 177 ? 106.833 122.253 96.432  1.00 96.54  ? 158 VAL A CG2 1 
ATOM   1196 N  N   . ALA A 1 178 ? 108.485 123.454 93.998  1.00 96.44  ? 159 ALA A N   1 
ATOM   1197 C  CA  . ALA A 1 178 ? 109.320 122.652 93.096  1.00 96.44  ? 159 ALA A CA  1 
ATOM   1198 C  C   . ALA A 1 178 ? 109.233 123.239 91.691  1.00 96.44  ? 159 ALA A C   1 
ATOM   1199 O  O   . ALA A 1 178 ? 109.612 124.409 91.511  1.00 96.44  ? 159 ALA A O   1 
ATOM   1200 C  CB  . ALA A 1 178 ? 108.917 121.182 93.229  1.00 96.44  ? 159 ALA A CB  1 
ATOM   1201 N  N   . GLN A 1 179 ? 108.764 122.493 90.686  1.00 93.54  ? 160 GLN A N   1 
ATOM   1202 C  CA  . GLN A 1 179 ? 108.850 122.954 89.303  1.00 93.54  ? 160 GLN A CA  1 
ATOM   1203 C  C   . GLN A 1 179 ? 108.005 124.197 89.057  1.00 93.54  ? 160 GLN A C   1 
ATOM   1204 O  O   . GLN A 1 179 ? 108.391 125.057 88.255  1.00 93.54  ? 160 GLN A O   1 
ATOM   1205 C  CB  . GLN A 1 179 ? 108.431 121.833 88.353  1.00 93.54  ? 160 GLN A CB  1 
ATOM   1206 C  CG  . GLN A 1 179 ? 108.746 122.114 86.895  1.00 93.54  ? 160 GLN A CG  1 
ATOM   1207 C  CD  . GLN A 1 179 ? 110.216 122.399 86.665  1.00 93.54  ? 160 GLN A CD  1 
ATOM   1208 O  OE1 . GLN A 1 179 ? 111.085 121.661 87.129  1.00 93.54  ? 160 GLN A OE1 1 
ATOM   1209 N  NE2 . GLN A 1 179 ? 110.503 123.478 85.946  1.00 93.54  ? 160 GLN A NE2 1 
ATOM   1210 N  N   . ALA A 1 180 ? 106.856 124.308 89.727  1.00 92.78  ? 161 ALA A N   1 
ATOM   1211 C  CA  . ALA A 1 180 ? 106.008 125.480 89.541  1.00 92.78  ? 161 ALA A CA  1 
ATOM   1212 C  C   . ALA A 1 180 ? 106.728 126.747 89.977  1.00 92.78  ? 161 ALA A C   1 
ATOM   1213 O  O   . ALA A 1 180 ? 106.651 127.779 89.301  1.00 92.78  ? 161 ALA A O   1 
ATOM   1214 C  CB  . ALA A 1 180 ? 104.698 125.309 90.309  1.00 92.78  ? 161 ALA A CB  1 
ATOM   1215 N  N   . ALA A 1 181 ? 107.436 126.689 91.108  1.00 92.16  ? 162 ALA A N   1 
ATOM   1216 C  CA  . ALA A 1 181 ? 108.190 127.850 91.566  1.00 92.16  ? 162 ALA A CA  1 
ATOM   1217 C  C   . ALA A 1 181 ? 109.294 128.215 90.581  1.00 92.16  ? 162 ALA A C   1 
ATOM   1218 O  O   . ALA A 1 181 ? 109.513 129.396 90.294  1.00 92.16  ? 162 ALA A O   1 
ATOM   1219 C  CB  . ALA A 1 181 ? 108.774 127.583 92.952  1.00 92.16  ? 162 ALA A CB  1 
ATOM   1220 N  N   . VAL A 1 182 ? 109.980 127.212 90.030  1.00 90.58  ? 163 VAL A N   1 
ATOM   1221 C  CA  . VAL A 1 182 ? 111.035 127.492 89.060  1.00 90.58  ? 163 VAL A CA  1 
ATOM   1222 C  C   . VAL A 1 182 ? 110.452 128.172 87.830  1.00 90.58  ? 163 VAL A C   1 
ATOM   1223 O  O   . VAL A 1 182 ? 111.017 129.142 87.310  1.00 90.58  ? 163 VAL A O   1 
ATOM   1224 C  CB  . VAL A 1 182 ? 111.783 126.197 88.694  1.00 90.58  ? 163 VAL A CB  1 
ATOM   1225 C  CG1 . VAL A 1 182 ? 112.737 126.440 87.537  1.00 90.58  ? 163 VAL A CG1 1 
ATOM   1226 C  CG2 . VAL A 1 182 ? 112.537 125.664 89.902  1.00 90.58  ? 163 VAL A CG2 1 
ATOM   1227 N  N   . ASP A 1 183 ? 109.311 127.679 87.347  1.00 90.82  ? 164 ASP A N   1 
ATOM   1228 C  CA  . ASP A 1 183 ? 108.688 128.291 86.179  1.00 90.82  ? 164 ASP A CA  1 
ATOM   1229 C  C   . ASP A 1 183 ? 108.130 129.677 86.485  1.00 90.82  ? 164 ASP A C   1 
ATOM   1230 O  O   . ASP A 1 183 ? 108.032 130.513 85.580  1.00 90.82  ? 164 ASP A O   1 
ATOM   1231 C  CB  . ASP A 1 183 ? 107.582 127.385 85.639  1.00 90.82  ? 164 ASP A CB  1 
ATOM   1232 C  CG  . ASP A 1 183 ? 108.104 126.038 85.177  1.00 90.82  ? 164 ASP A CG  1 
ATOM   1233 O  OD1 . ASP A 1 183 ? 109.324 125.920 84.939  1.00 90.82  ? 164 ASP A OD1 1 
ATOM   1234 O  OD2 . ASP A 1 183 ? 107.294 125.095 85.054  1.00 90.82  ? 164 ASP A OD2 1 
ATOM   1235 N  N   . ALA A 1 184 ? 107.763 129.947 87.742  1.00 87.57  ? 165 ALA A N   1 
ATOM   1236 C  CA  . ALA A 1 184 ? 107.190 131.252 88.061  1.00 87.57  ? 165 ALA A CA  1 
ATOM   1237 C  C   . ALA A 1 184 ? 108.242 132.322 88.331  1.00 87.57  ? 165 ALA A C   1 
ATOM   1238 O  O   . ALA A 1 184 ? 107.991 133.503 88.068  1.00 87.57  ? 165 ALA A O   1 
ATOM   1239 C  CB  . ALA A 1 184 ? 106.260 131.130 89.268  1.00 87.57  ? 165 ALA A CB  1 
ATOM   1240 N  N   . THR A 1 185 ? 109.409 131.949 88.852  1.00 85.55  ? 166 THR A N   1 
ATOM   1241 C  CA  . THR A 1 185 ? 110.415 132.927 89.260  1.00 85.55  ? 166 THR A CA  1 
ATOM   1242 C  C   . THR A 1 185 ? 111.511 133.119 88.218  1.00 85.55  ? 166 THR A C   1 
ATOM   1243 O  O   . THR A 1 185 ? 111.852 134.255 87.881  1.00 85.55  ? 166 THR A O   1 
ATOM   1244 C  CB  . THR A 1 185 ? 111.031 132.576 90.623  1.00 85.55  ? 166 THR A CB  1 
ATOM   1245 O  OG1 . THR A 1 185 ? 112.128 131.668 90.455  1.00 85.55  ? 166 THR A OG1 1 
ATOM   1246 C  CG2 . THR A 1 185 ? 109.989 132.029 91.589  1.00 85.55  ? 166 THR A CG2 1 
ATOM   1247 N  N   . LEU A 1 186 ? 112.072 132.030 87.701  1.00 85.67  ? 167 LEU A N   1 
ATOM   1248 C  CA  . LEU A 1 186 ? 113.228 132.113 86.822  1.00 85.67  ? 167 LEU A CA  1 
ATOM   1249 C  C   . LEU A 1 186 ? 112.814 132.571 85.428  1.00 85.67  ? 167 LEU A C   1 
ATOM   1250 O  O   . LEU A 1 186 ? 111.835 132.073 84.863  1.00 85.67  ? 167 LEU A O   1 
ATOM   1251 C  CB  . LEU A 1 186 ? 113.907 130.748 86.745  1.00 85.67  ? 167 LEU A CB  1 
ATOM   1252 C  CG  . LEU A 1 186 ? 114.973 130.494 87.809  1.00 85.67  ? 167 LEU A CG  1 
ATOM   1253 C  CD1 . LEU A 1 186 ? 115.139 129.009 88.079  1.00 85.67  ? 167 LEU A CD1 1 
ATOM   1254 C  CD2 . LEU A 1 186 ? 116.268 131.104 87.376  1.00 85.67  ? 167 LEU A CD2 1 
ATOM   1255 N  N   . ILE A 1 187 ? 113.571 133.522 84.876  1.00 85.00  ? 168 ILE A N   1 
ATOM   1256 C  CA  . ILE A 1 187 ? 113.277 134.061 83.553  1.00 85.00  ? 168 ILE A CA  1 
ATOM   1257 C  C   . ILE A 1 187 ? 113.669 133.064 82.471  1.00 85.00  ? 168 ILE A C   1 
ATOM   1258 O  O   . ILE A 1 187 ? 114.751 132.462 82.513  1.00 85.00  ? 168 ILE A O   1 
ATOM   1259 C  CB  . ILE A 1 187 ? 114.004 135.402 83.350  1.00 85.00  ? 168 ILE A CB  1 
ATOM   1260 C  CG1 . ILE A 1 187 ? 113.424 136.477 84.268  1.00 85.00  ? 168 ILE A CG1 1 
ATOM   1261 C  CG2 . ILE A 1 187 ? 113.940 135.843 81.897  1.00 85.00  ? 168 ILE A CG2 1 
ATOM   1262 C  CD1 . ILE A 1 187 ? 114.370 137.627 84.516  1.00 85.00  ? 168 ILE A CD1 1 
ATOM   1263 N  N   . GLY A 1 188 ? 112.787 132.889 81.489  1.00 91.87  ? 169 GLY A N   1 
ATOM   1264 C  CA  . GLY A 1 188 ? 113.020 131.941 80.419  1.00 91.87  ? 169 GLY A CA  1 
ATOM   1265 C  C   . GLY A 1 188 ? 113.785 132.566 79.271  1.00 91.87  ? 169 GLY A C   1 
ATOM   1266 O  O   . GLY A 1 188 ? 114.867 133.125 79.473  1.00 91.87  ? 169 GLY A O   1 
ATOM   1267 N  N   . ASP A 1 189 ? 113.235 132.482 78.061  1.00 97.01  ? 170 ASP A N   1 
ATOM   1268 C  CA  . ASP A 1 189 ? 113.894 133.001 76.870  1.00 97.01  ? 170 ASP A CA  1 
ATOM   1269 C  C   . ASP A 1 189 ? 113.405 134.388 76.469  1.00 97.01  ? 170 ASP A C   1 
ATOM   1270 O  O   . ASP A 1 189 ? 113.850 134.908 75.441  1.00 97.01  ? 170 ASP A O   1 
ATOM   1271 C  CB  . ASP A 1 189 ? 113.704 132.032 75.698  1.00 97.01  ? 170 ASP A CB  1 
ATOM   1272 C  CG  . ASP A 1 189 ? 114.472 130.737 75.882  1.00 97.01  ? 170 ASP A CG  1 
ATOM   1273 O  OD1 . ASP A 1 189 ? 114.677 130.326 77.044  1.00 97.01  ? 170 ASP A OD1 1 
ATOM   1274 O  OD2 . ASP A 1 189 ? 114.870 130.131 74.865  1.00 97.01  ? 170 ASP A OD2 1 
ATOM   1275 N  N   . GLU A 1 190 ? 112.494 134.990 77.240  1.00 97.53  ? 171 GLU A N   1 
ATOM   1276 C  CA  . GLU A 1 190 ? 112.019 136.335 76.923  1.00 97.53  ? 171 GLU A CA  1 
ATOM   1277 C  C   . GLU A 1 190 ? 113.156 137.348 76.886  1.00 97.53  ? 171 GLU A C   1 
ATOM   1278 O  O   . GLU A 1 190 ? 113.108 138.308 76.109  1.00 97.53  ? 171 GLU A O   1 
ATOM   1279 C  CB  . GLU A 1 190 ? 110.951 136.774 77.928  1.00 97.53  ? 171 GLU A CB  1 
ATOM   1280 C  CG  . GLU A 1 190 ? 111.286 136.504 79.390  1.00 97.53  ? 171 GLU A CG  1 
ATOM   1281 C  CD  . GLU A 1 190 ? 110.905 135.104 79.840  1.00 97.53  ? 171 GLU A CD  1 
ATOM   1282 O  OE1 . GLU A 1 190 ? 110.793 134.206 78.979  1.00 97.53  ? 171 GLU A OE1 1 
ATOM   1283 O  OE2 . GLU A 1 190 ? 110.713 134.903 81.057  1.00 97.53  ? 171 GLU A OE2 1 
ATOM   1284 N  N   . ASP A 1 191 ? 114.188 137.152 77.717  1.00 99.16  ? 172 ASP A N   1 
ATOM   1285 C  CA  . ASP A 1 191 ? 115.369 138.019 77.755  1.00 99.16  ? 172 ASP A CA  1 
ATOM   1286 C  C   . ASP A 1 191 ? 116.575 137.094 77.924  1.00 99.16  ? 172 ASP A C   1 
ATOM   1287 O  O   . ASP A 1 191 ? 117.107 136.933 79.025  1.00 99.16  ? 172 ASP A O   1 
ATOM   1288 C  CB  . ASP A 1 191 ? 115.277 139.056 78.873  1.00 99.16  ? 172 ASP A CB  1 
ATOM   1289 C  CG  . ASP A 1 191 ? 116.062 140.316 78.562  1.00 99.16  ? 172 ASP A CG  1 
ATOM   1290 O  OD1 . ASP A 1 191 ? 116.834 140.310 77.580  1.00 99.16  ? 172 ASP A OD1 1 
ATOM   1291 O  OD2 . ASP A 1 191 ? 115.904 141.313 79.298  1.00 99.16  ? 172 ASP A OD2 1 
ATOM   1292 N  N   . MET A 1 192 ? 116.977 136.469 76.812  1.00 96.67  ? 173 MET A N   1 
ATOM   1293 C  CA  . MET A 1 192 ? 118.044 135.470 76.829  1.00 96.67  ? 173 MET A CA  1 
ATOM   1294 C  C   . MET A 1 192 ? 119.279 135.962 77.576  1.00 96.67  ? 173 MET A C   1 
ATOM   1295 O  O   . MET A 1 192 ? 119.785 135.282 78.475  1.00 96.67  ? 173 MET A O   1 
ATOM   1296 C  CB  . MET A 1 192 ? 118.404 135.078 75.396  1.00 96.67  ? 173 MET A CB  1 
ATOM   1297 C  CG  . MET A 1 192 ? 119.486 134.017 75.294  1.00 96.67  ? 173 MET A CG  1 
ATOM   1298 S  SD  . MET A 1 192 ? 118.827 132.344 75.418  1.00 96.67  ? 173 MET A SD  1 
ATOM   1299 C  CE  . MET A 1 192 ? 120.116 131.540 76.366  1.00 96.67  ? 173 MET A CE  1 
ATOM   1300 N  N   . VAL A 1 193 ? 119.789 137.139 77.203  1.00 94.75  ? 174 VAL A N   1 
ATOM   1301 C  CA  . VAL A 1 193 ? 121.011 137.707 77.772  1.00 94.75  ? 174 VAL A CA  1 
ATOM   1302 C  C   . VAL A 1 193 ? 120.971 137.728 79.300  1.00 94.75  ? 174 VAL A C   1 
ATOM   1303 O  O   . VAL A 1 193 ? 122.008 137.868 79.958  1.00 94.75  ? 174 VAL A O   1 
ATOM   1304 C  CB  . VAL A 1 193 ? 121.250 139.122 77.209  1.00 94.75  ? 174 VAL A CB  1 
ATOM   1305 C  CG1 . VAL A 1 193 ? 122.622 139.653 77.606  1.00 94.75  ? 174 VAL A CG1 1 
ATOM   1306 C  CG2 . VAL A 1 193 ? 121.091 139.122 75.698  1.00 94.75  ? 174 VAL A CG2 1 
ATOM   1307 N  N   . PHE A 1 194 ? 119.781 137.543 79.880  1.00 89.76  ? 175 PHE A N   1 
ATOM   1308 C  CA  . PHE A 1 194 ? 119.631 137.496 81.330  1.00 89.76  ? 175 PHE A CA  1 
ATOM   1309 C  C   . PHE A 1 194 ? 118.899 136.242 81.789  1.00 89.76  ? 175 PHE A C   1 
ATOM   1310 O  O   . PHE A 1 194 ? 118.289 136.253 82.863  1.00 89.76  ? 175 PHE A O   1 
ATOM   1311 C  CB  . PHE A 1 194 ? 118.916 138.745 81.849  1.00 89.76  ? 175 PHE A CB  1 
ATOM   1312 C  CG  . PHE A 1 194 ? 119.547 140.028 81.403  1.00 89.76  ? 175 PHE A CG  1 
ATOM   1313 C  CD1 . PHE A 1 194 ? 120.777 140.414 81.906  1.00 89.76  ? 175 PHE A CD1 1 
ATOM   1314 C  CD2 . PHE A 1 194 ? 118.916 140.846 80.484  1.00 89.76  ? 175 PHE A CD2 1 
ATOM   1315 C  CE1 . PHE A 1 194 ? 121.366 141.593 81.501  1.00 89.76  ? 175 PHE A CE1 1 
ATOM   1316 C  CE2 . PHE A 1 194 ? 119.501 142.027 80.075  1.00 89.76  ? 175 PHE A CE2 1 
ATOM   1317 C  CZ  . PHE A 1 194 ? 120.728 142.401 80.585  1.00 89.76  ? 175 PHE A CZ  1 
ATOM   1318 N  N   . ALA A 1 195 ? 118.918 135.181 80.984  1.00 88.44  ? 176 ALA A N   1 
ATOM   1319 C  CA  . ALA A 1 195 ? 118.292 133.926 81.377  1.00 88.44  ? 176 ALA A CA  1 
ATOM   1320 C  C   . ALA A 1 195 ? 118.812 133.495 82.740  1.00 88.44  ? 176 ALA A C   1 
ATOM   1321 O  O   . ALA A 1 195 ? 120.018 133.531 82.995  1.00 88.44  ? 176 ALA A O   1 
ATOM   1322 C  CB  . ALA A 1 195 ? 118.569 132.845 80.332  1.00 88.44  ? 176 ALA A CB  1 
ATOM   1323 N  N   . GLY A 1 196 ? 117.899 133.078 83.610  1.00 83.05  ? 177 GLY A N   1 
ATOM   1324 C  CA  . GLY A 1 196 ? 118.242 132.690 84.959  1.00 83.05  ? 177 GLY A CA  1 
ATOM   1325 C  C   . GLY A 1 196 ? 118.084 133.779 86.001  1.00 83.05  ? 177 GLY A C   1 
ATOM   1326 O  O   . GLY A 1 196 ? 118.232 133.493 87.196  1.00 83.05  ? 177 GLY A O   1 
ATOM   1327 N  N   . GLY A 1 197 ? 117.823 135.018 85.593  1.00 83.13  ? 178 GLY A N   1 
ATOM   1328 C  CA  . GLY A 1 197 ? 117.589 136.086 86.539  1.00 83.13  ? 178 GLY A CA  1 
ATOM   1329 C  C   . GLY A 1 197 ? 116.151 136.102 87.022  1.00 83.13  ? 178 GLY A C   1 
ATOM   1330 O  O   . GLY A 1 197 ? 115.337 135.241 86.691  1.00 83.13  ? 178 GLY A O   1 
ATOM   1331 N  N   . SER A 1 198 ? 115.836 137.113 87.828  1.00 77.61  ? 179 SER A N   1 
ATOM   1332 C  CA  . SER A 1 198 ? 114.483 137.267 88.347  1.00 77.61  ? 179 SER A CA  1 
ATOM   1333 C  C   . SER A 1 198 ? 114.273 138.722 88.738  1.00 77.61  ? 179 SER A C   1 
ATOM   1334 O  O   . SER A 1 198 ? 115.206 139.527 88.732  1.00 77.61  ? 179 SER A O   1 
ATOM   1335 C  CB  . SER A 1 198 ? 114.235 136.339 89.540  1.00 77.61  ? 179 SER A CB  1 
ATOM   1336 O  OG  . SER A 1 198 ? 112.873 136.361 89.925  1.00 77.61  ? 179 SER A OG  1 
ATOM   1337 N  N   . TYR A 1 199 ? 113.033 139.052 89.088  1.00 73.89  ? 180 TYR A N   1 
ATOM   1338 C  CA  . TYR A 1 199 ? 112.686 140.368 89.603  1.00 73.89  ? 180 TYR A CA  1 
ATOM   1339 C  C   . TYR A 1 199 ? 112.115 140.202 91.001  1.00 73.89  ? 180 TYR A C   1 
ATOM   1340 O  O   . TYR A 1 199 ? 111.272 139.328 91.230  1.00 73.89  ? 180 TYR A O   1 
ATOM   1341 C  CB  . TYR A 1 199 ? 111.678 141.078 88.698  1.00 73.89  ? 180 TYR A CB  1 
ATOM   1342 C  CG  . TYR A 1 199 ? 112.183 141.342 87.300  1.00 73.89  ? 180 TYR A CG  1 
ATOM   1343 C  CD1 . TYR A 1 199 ? 112.091 140.372 86.314  1.00 73.89  ? 180 TYR A CD1 1 
ATOM   1344 C  CD2 . TYR A 1 199 ? 112.751 142.563 86.967  1.00 73.89  ? 180 TYR A CD2 1 
ATOM   1345 C  CE1 . TYR A 1 199 ? 112.547 140.611 85.035  1.00 73.89  ? 180 TYR A CE1 1 
ATOM   1346 C  CE2 . TYR A 1 199 ? 113.212 142.810 85.691  1.00 73.89  ? 180 TYR A CE2 1 
ATOM   1347 C  CZ  . TYR A 1 199 ? 113.108 141.829 84.729  1.00 73.89  ? 180 TYR A CZ  1 
ATOM   1348 O  OH  . TYR A 1 199 ? 113.563 142.065 83.455  1.00 73.89  ? 180 TYR A OH  1 
ATOM   1349 N  N   . VAL A 1 200 ? 112.565 141.037 91.931  1.00 68.13  ? 181 VAL A N   1 
ATOM   1350 C  CA  . VAL A 1 200 ? 112.143 140.960 93.323  1.00 68.13  ? 181 VAL A CA  1 
ATOM   1351 C  C   . VAL A 1 200 ? 111.541 142.300 93.719  1.00 68.13  ? 181 VAL A C   1 
ATOM   1352 O  O   . VAL A 1 200 ? 112.089 143.358 93.392  1.00 68.13  ? 181 VAL A O   1 
ATOM   1353 C  CB  . VAL A 1 200 ? 113.308 140.570 94.252  1.00 68.13  ? 181 VAL A CB  1 
ATOM   1354 C  CG1 . VAL A 1 200 ? 114.473 141.524 94.091  1.00 68.13  ? 181 VAL A CG1 1 
ATOM   1355 C  CG2 . VAL A 1 200 ? 112.846 140.545 95.693  1.00 68.13  ? 181 VAL A CG2 1 
ATOM   1356 N  N   . ILE A 1 201 ? 110.394 142.254 94.388  1.00 71.82  ? 182 ILE A N   1 
ATOM   1357 C  CA  . ILE A 1 201 ? 109.731 143.446 94.900  1.00 71.82  ? 182 ILE A CA  1 
ATOM   1358 C  C   . ILE A 1 201 ? 109.648 143.326 96.413  1.00 71.82  ? 182 ILE A C   1 
ATOM   1359 O  O   . ILE A 1 201 ? 109.137 142.327 96.932  1.00 71.82  ? 182 ILE A O   1 
ATOM   1360 C  CB  . ILE A 1 201 ? 108.334 143.636 94.282  1.00 71.82  ? 182 ILE A CB  1 
ATOM   1361 C  CG1 . ILE A 1 201 ? 108.461 144.083 92.826  1.00 71.82  ? 182 ILE A CG1 1 
ATOM   1362 C  CG2 . ILE A 1 201 ? 107.529 144.645 95.082  1.00 71.82  ? 182 ILE A CG2 1 
ATOM   1363 C  CD1 . ILE A 1 201 ? 107.153 144.501 92.197  1.00 71.82  ? 182 ILE A CD1 1 
ATOM   1364 N  N   . VAL A 1 202 ? 110.158 144.334 97.115  1.00 69.59  ? 183 VAL A N   1 
ATOM   1365 C  CA  . VAL A 1 202 ? 110.211 144.331 98.571  1.00 69.59  ? 183 VAL A CA  1 
ATOM   1366 C  C   . VAL A 1 202 ? 109.374 145.488 99.095  1.00 69.59  ? 183 VAL A C   1 
ATOM   1367 O  O   . VAL A 1 202 ? 109.399 146.592 98.541  1.00 69.59  ? 183 VAL A O   1 
ATOM   1368 C  CB  . VAL A 1 202 ? 111.660 144.417 99.094  1.00 69.59  ? 183 VAL A CB  1 
ATOM   1369 C  CG1 . VAL A 1 202 ? 112.430 143.167 98.713  1.00 69.59  ? 183 VAL A CG1 1 
ATOM   1370 C  CG2 . VAL A 1 202 ? 112.357 145.651 98.548  1.00 69.59  ? 183 VAL A CG2 1 
ATOM   1371 N  N   . GLN A 1 203 ? 108.610 145.218 100.151 1.00 70.57  ? 184 GLN A N   1 
ATOM   1372 C  CA  . GLN A 1 203 ? 107.822 146.226 100.841 1.00 70.57  ? 184 GLN A CA  1 
ATOM   1373 C  C   . GLN A 1 203 ? 107.870 145.959 102.337 1.00 70.57  ? 184 GLN A C   1 
ATOM   1374 O  O   . GLN A 1 203 ? 108.093 144.829 102.776 1.00 70.57  ? 184 GLN A O   1 
ATOM   1375 C  CB  . GLN A 1 203 ? 106.365 146.250 100.367 1.00 70.57  ? 184 GLN A CB  1 
ATOM   1376 C  CG  . GLN A 1 203 ? 106.163 146.869 99.001  1.00 70.57  ? 184 GLN A CG  1 
ATOM   1377 C  CD  . GLN A 1 203 ? 104.702 147.109 98.694  1.00 70.57  ? 184 GLN A CD  1 
ATOM   1378 O  OE1 . GLN A 1 203 ? 103.912 146.171 98.615  1.00 70.57  ? 184 GLN A OE1 1 
ATOM   1379 N  NE2 . GLN A 1 203 ? 104.334 148.372 98.522  1.00 70.57  ? 184 GLN A NE2 1 
ATOM   1380 N  N   . LYS A 1 204 ? 107.664 147.015 103.114 1.00 70.87  ? 185 LYS A N   1 
ATOM   1381 C  CA  . LYS A 1 204 ? 107.653 146.933 104.569 1.00 70.87  ? 185 LYS A CA  1 
ATOM   1382 C  C   . LYS A 1 204 ? 106.330 147.485 105.078 1.00 70.87  ? 185 LYS A C   1 
ATOM   1383 O  O   . LYS A 1 204 ? 105.977 148.630 104.777 1.00 70.87  ? 185 LYS A O   1 
ATOM   1384 C  CB  . LYS A 1 204 ? 108.834 147.702 105.165 1.00 70.87  ? 185 LYS A CB  1 
ATOM   1385 C  CG  . LYS A 1 204 ? 108.636 148.155 106.599 1.00 70.87  ? 185 LYS A CG  1 
ATOM   1386 C  CD  . LYS A 1 204 ? 109.956 148.166 107.353 1.00 70.87  ? 185 LYS A CD  1 
ATOM   1387 C  CE  . LYS A 1 204 ? 110.677 149.492 107.189 1.00 70.87  ? 185 LYS A CE  1 
ATOM   1388 N  NZ  . LYS A 1 204 ? 111.912 149.556 108.015 1.00 70.87  ? 185 LYS A NZ  1 
ATOM   1389 N  N   . TYR A 1 205 ? 105.598 146.676 105.844 1.00 70.68  ? 186 TYR A N   1 
ATOM   1390 C  CA  . TYR A 1 205 ? 104.298 147.059 106.371 1.00 70.68  ? 186 TYR A CA  1 
ATOM   1391 C  C   . TYR A 1 205 ? 104.366 147.131 107.888 1.00 70.68  ? 186 TYR A C   1 
ATOM   1392 O  O   . TYR A 1 205 ? 104.925 146.240 108.533 1.00 70.68  ? 186 TYR A O   1 
ATOM   1393 C  CB  . TYR A 1 205 ? 103.212 146.060 105.954 1.00 70.68  ? 186 TYR A CB  1 
ATOM   1394 C  CG  . TYR A 1 205 ? 102.870 146.081 104.483 1.00 70.68  ? 186 TYR A CG  1 
ATOM   1395 C  CD1 . TYR A 1 205 ? 101.933 146.972 103.980 1.00 70.68  ? 186 TYR A CD1 1 
ATOM   1396 C  CD2 . TYR A 1 205 ? 103.474 145.200 103.598 1.00 70.68  ? 186 TYR A CD2 1 
ATOM   1397 C  CE1 . TYR A 1 205 ? 101.615 146.991 102.638 1.00 70.68  ? 186 TYR A CE1 1 
ATOM   1398 C  CE2 . TYR A 1 205 ? 103.162 145.211 102.255 1.00 70.68  ? 186 TYR A CE2 1 
ATOM   1399 C  CZ  . TYR A 1 205 ? 102.232 146.109 101.780 1.00 70.68  ? 186 TYR A CZ  1 
ATOM   1400 O  OH  . TYR A 1 205 ? 101.919 146.124 100.442 1.00 70.68  ? 186 TYR A OH  1 
ATOM   1401 N  N   . LEU A 1 206 ? 103.788 148.188 108.453 1.00 74.45  ? 187 LEU A N   1 
ATOM   1402 C  CA  . LEU A 1 206 ? 103.665 148.353 109.896 1.00 74.45  ? 187 LEU A CA  1 
ATOM   1403 C  C   . LEU A 1 206 ? 102.218 148.123 110.305 1.00 74.45  ? 187 LEU A C   1 
ATOM   1404 O  O   . LEU A 1 206 ? 101.306 148.746 109.753 1.00 74.45  ? 187 LEU A O   1 
ATOM   1405 C  CB  . LEU A 1 206 ? 104.124 149.746 110.334 1.00 74.45  ? 187 LEU A CB  1 
ATOM   1406 C  CG  . LEU A 1 206 ? 105.620 150.036 110.229 1.00 74.45  ? 187 LEU A CG  1 
ATOM   1407 C  CD1 . LEU A 1 206 ? 105.905 151.485 110.580 1.00 74.45  ? 187 LEU A CD1 1 
ATOM   1408 C  CD2 . LEU A 1 206 ? 106.408 149.100 111.128 1.00 74.45  ? 187 LEU A CD2 1 
ATOM   1409 N  N   . HIS A 1 207 ? 102.012 147.235 111.272 1.00 75.93  ? 188 HIS A N   1 
ATOM   1410 C  CA  . HIS A 1 207 ? 100.679 146.783 111.640 1.00 75.93  ? 188 HIS A CA  1 
ATOM   1411 C  C   . HIS A 1 207 ? 100.116 147.587 112.806 1.00 75.93  ? 188 HIS A C   1 
ATOM   1412 O  O   . HIS A 1 207 ? 100.849 148.052 113.683 1.00 75.93  ? 188 HIS A O   1 
ATOM   1413 C  CB  . HIS A 1 207 ? 100.696 145.298 112.001 1.00 75.93  ? 188 HIS A CB  1 
ATOM   1414 C  CG  . HIS A 1 207 ? 100.960 144.396 110.836 1.00 75.93  ? 188 HIS A CG  1 
ATOM   1415 N  ND1 . HIS A 1 207 ? 100.190 144.410 109.694 1.00 75.93  ? 188 HIS A ND1 1 
ATOM   1416 C  CD2 . HIS A 1 207 ? 101.909 143.451 110.638 1.00 75.93  ? 188 HIS A CD2 1 
ATOM   1417 C  CE1 . HIS A 1 207 ? 100.652 143.513 108.842 1.00 75.93  ? 188 HIS A CE1 1 
ATOM   1418 N  NE2 . HIS A 1 207 ? 101.695 142.917 109.391 1.00 75.93  ? 188 HIS A NE2 1 
ATOM   1419 N  N   . ASP A 1 208 ? 98.794  147.747 112.800 1.00 83.61  ? 189 ASP A N   1 
ATOM   1420 C  CA  . ASP A 1 208 ? 98.045  148.318 113.919 1.00 83.61  ? 189 ASP A CA  1 
ATOM   1421 C  C   . ASP A 1 208 ? 97.363  147.143 114.614 1.00 83.61  ? 189 ASP A C   1 
ATOM   1422 O  O   . ASP A 1 208 ? 96.211  146.812 114.333 1.00 83.61  ? 189 ASP A O   1 
ATOM   1423 C  CB  . ASP A 1 208 ? 97.045  149.362 113.436 1.00 83.61  ? 189 ASP A CB  1 
ATOM   1424 C  CG  . ASP A 1 208 ? 96.434  150.163 114.573 1.00 83.61  ? 189 ASP A CG  1 
ATOM   1425 O  OD1 . ASP A 1 208 ? 96.577  149.755 115.744 1.00 83.61  ? 189 ASP A OD1 1 
ATOM   1426 O  OD2 . ASP A 1 208 ? 95.806  151.205 114.292 1.00 83.61  ? 189 ASP A OD2 1 
ATOM   1427 N  N   . LEU A 1 209 ? 98.095  146.508 115.532 1.00 84.51  ? 190 LEU A N   1 
ATOM   1428 C  CA  . LEU A 1 209 ? 97.608  145.283 116.158 1.00 84.51  ? 190 LEU A CA  1 
ATOM   1429 C  C   . LEU A 1 209 ? 96.389  145.518 117.042 1.00 84.51  ? 190 LEU A C   1 
ATOM   1430 O  O   . LEU A 1 209 ? 95.555  144.620 117.179 1.00 84.51  ? 190 LEU A O   1 
ATOM   1431 C  CB  . LEU A 1 209 ? 98.727  144.631 116.969 1.00 84.51  ? 190 LEU A CB  1 
ATOM   1432 C  CG  . LEU A 1 209 ? 99.870  144.021 116.158 1.00 84.51  ? 190 LEU A CG  1 
ATOM   1433 C  CD1 . LEU A 1 209 ? 100.805 143.236 117.062 1.00 84.51  ? 190 LEU A CD1 1 
ATOM   1434 C  CD2 . LEU A 1 209 ? 99.328  143.136 115.049 1.00 84.51  ? 190 LEU A CD2 1 
ATOM   1435 N  N   . ASP A 1 210 ? 96.275  146.688 117.673 1.00 87.85  ? 191 ASP A N   1 
ATOM   1436 C  CA  . ASP A 1 210 ? 95.104  146.955 118.506 1.00 87.85  ? 191 ASP A CA  1 
ATOM   1437 C  C   . ASP A 1 210 ? 93.822  146.977 117.679 1.00 87.85  ? 191 ASP A C   1 
ATOM   1438 O  O   . ASP A 1 210 ? 92.812  146.366 118.061 1.00 87.85  ? 191 ASP A O   1 
ATOM   1439 C  CB  . ASP A 1 210 ? 95.283  148.277 119.251 1.00 87.85  ? 191 ASP A CB  1 
ATOM   1440 C  CG  . ASP A 1 210 ? 96.282  148.175 120.385 1.00 87.85  ? 191 ASP A CG  1 
ATOM   1441 O  OD1 . ASP A 1 210 ? 96.529  147.048 120.860 1.00 87.85  ? 191 ASP A OD1 1 
ATOM   1442 O  OD2 . ASP A 1 210 ? 96.820  149.223 120.800 1.00 87.85  ? 191 ASP A OD2 1 
ATOM   1443 N  N   . LYS A 1 211 ? 93.866  147.618 116.508 1.00 86.18  ? 192 LYS A N   1 
ATOM   1444 C  CA  . LYS A 1 211 ? 92.695  147.636 115.638 1.00 86.18  ? 192 LYS A CA  1 
ATOM   1445 C  C   . LYS A 1 211 ? 92.401  146.248 115.093 1.00 86.18  ? 192 LYS A C   1 
ATOM   1446 O  O   . LYS A 1 211 ? 91.233  145.863 114.968 1.00 86.18  ? 192 LYS A O   1 
ATOM   1447 C  CB  . LYS A 1 211 ? 92.900  148.632 114.498 1.00 86.18  ? 192 LYS A CB  1 
ATOM   1448 C  CG  . LYS A 1 211 ? 91.630  148.962 113.733 1.00 86.18  ? 192 LYS A CG  1 
ATOM   1449 C  CD  . LYS A 1 211 ? 91.734  150.313 113.045 1.00 86.18  ? 192 LYS A CD  1 
ATOM   1450 C  CE  . LYS A 1 211 ? 90.891  150.353 111.782 1.00 86.18  ? 192 LYS A CE  1 
ATOM   1451 N  NZ  . LYS A 1 211 ? 89.564  149.709 111.981 1.00 86.18  ? 192 LYS A NZ  1 
ATOM   1452 N  N   . TRP A 1 212 ? 93.441  145.481 114.759 1.00 85.17  ? 193 TRP A N   1 
ATOM   1453 C  CA  . TRP A 1 212 ? 93.198  144.155 114.208 1.00 85.17  ? 193 TRP A CA  1 
ATOM   1454 C  C   . TRP A 1 212 ? 92.591  143.253 115.272 1.00 85.17  ? 193 TRP A C   1 
ATOM   1455 O  O   . TRP A 1 212 ? 91.689  142.458 114.984 1.00 85.17  ? 193 TRP A O   1 
ATOM   1456 C  CB  . TRP A 1 212 ? 94.498  143.562 113.669 1.00 85.17  ? 193 TRP A CB  1 
ATOM   1457 C  CG  . TRP A 1 212 ? 94.328  142.229 113.017 1.00 85.17  ? 193 TRP A CG  1 
ATOM   1458 C  CD1 . TRP A 1 212 ? 94.778  141.028 113.480 1.00 85.17  ? 193 TRP A CD1 1 
ATOM   1459 C  CD2 . TRP A 1 212 ? 93.668  141.959 111.776 1.00 85.17  ? 193 TRP A CD2 1 
ATOM   1460 N  NE1 . TRP A 1 212 ? 94.434  140.026 112.606 1.00 85.17  ? 193 TRP A NE1 1 
ATOM   1461 C  CE2 . TRP A 1 212 ? 93.752  140.572 111.551 1.00 85.17  ? 193 TRP A CE2 1 
ATOM   1462 C  CE3 . TRP A 1 212 ? 93.011  142.756 110.834 1.00 85.17  ? 193 TRP A CE3 1 
ATOM   1463 C  CZ2 . TRP A 1 212 ? 93.206  139.964 110.423 1.00 85.17  ? 193 TRP A CZ2 1 
ATOM   1464 C  CZ3 . TRP A 1 212 ? 92.469  142.151 109.716 1.00 85.17  ? 193 TRP A CZ3 1 
ATOM   1465 C  CH2 . TRP A 1 212 ? 92.570  140.769 109.520 1.00 85.17  ? 193 TRP A CH2 1 
ATOM   1466 N  N   . ASN A 1 213 ? 93.082  143.362 116.509 1.00 86.03  ? 194 ASN A N   1 
ATOM   1467 C  CA  . ASN A 1 213 ? 92.614  142.496 117.580 1.00 86.03  ? 194 ASN A CA  1 
ATOM   1468 C  C   . ASN A 1 213 ? 91.195  142.856 117.989 1.00 86.03  ? 194 ASN A C   1 
ATOM   1469 O  O   . ASN A 1 213 ? 90.433  141.981 118.416 1.00 86.03  ? 194 ASN A O   1 
ATOM   1470 C  CB  . ASN A 1 213 ? 93.556  142.580 118.780 1.00 86.03  ? 194 ASN A CB  1 
ATOM   1471 C  CG  . ASN A 1 213 ? 94.622  141.504 118.759 1.00 86.03  ? 194 ASN A CG  1 
ATOM   1472 O  OD1 . ASN A 1 213 ? 94.392  140.396 118.276 1.00 86.03  ? 194 ASN A OD1 1 
ATOM   1473 N  ND2 . ASN A 1 213 ? 95.797  141.826 119.285 1.00 86.03  ? 194 ASN A ND2 1 
ATOM   1474 N  N   . ALA A 1 214 ? 90.821  144.136 117.872 1.00 86.58  ? 195 ALA A N   1 
ATOM   1475 C  CA  . ALA A 1 214 ? 89.450  144.515 118.192 1.00 86.58  ? 195 ALA A CA  1 
ATOM   1476 C  C   . ALA A 1 214 ? 88.456  143.977 117.171 1.00 86.58  ? 195 ALA A C   1 
ATOM   1477 O  O   . ALA A 1 214 ? 87.263  143.876 117.477 1.00 86.58  ? 195 ALA A O   1 
ATOM   1478 C  CB  . ALA A 1 214 ? 89.331  146.036 118.286 1.00 86.58  ? 195 ALA A CB  1 
ATOM   1479 N  N   . ILE A 1 215 ? 88.920  143.636 115.977 1.00 85.93  ? 196 ILE A N   1 
ATOM   1480 C  CA  . ILE A 1 215 ? 88.053  143.081 114.931 1.00 85.93  ? 196 ILE A CA  1 
ATOM   1481 C  C   . ILE A 1 215 ? 87.616  141.674 115.330 1.00 85.93  ? 196 ILE A C   1 
ATOM   1482 O  O   . ILE A 1 215 ? 88.454  140.877 115.788 1.00 85.93  ? 196 ILE A O   1 
ATOM   1483 C  CB  . ILE A 1 215 ? 88.783  143.075 113.586 1.00 85.93  ? 196 ILE A CB  1 
ATOM   1484 C  CG1 . ILE A 1 215 ? 89.047  144.507 113.119 1.00 85.93  ? 196 ILE A CG1 1 
ATOM   1485 C  CG2 . ILE A 1 215 ? 87.992  142.322 112.543 1.00 85.93  ? 196 ILE A CG2 1 
ATOM   1486 C  CD1 . ILE A 1 215 ? 89.786  144.591 111.803 1.00 85.93  ? 196 ILE A CD1 1 
ATOM   1487 N  N   . PRO A 1 216 ? 86.336  141.326 115.191 1.00 88.93  ? 197 PRO A N   1 
ATOM   1488 C  CA  . PRO A 1 216 ? 85.895  139.972 115.546 1.00 88.93  ? 197 PRO A CA  1 
ATOM   1489 C  C   . PRO A 1 216 ? 86.576  138.920 114.683 1.00 88.93  ? 197 PRO A C   1 
ATOM   1490 O  O   . PRO A 1 216 ? 87.028  139.185 113.567 1.00 88.93  ? 197 PRO A O   1 
ATOM   1491 C  CB  . PRO A 1 216 ? 84.384  140.009 115.289 1.00 88.93  ? 197 PRO A CB  1 
ATOM   1492 C  CG  . PRO A 1 216 ? 84.022  141.455 115.367 1.00 88.93  ? 197 PRO A CG  1 
ATOM   1493 C  CD  . PRO A 1 216 ? 85.206  142.195 114.822 1.00 88.93  ? 197 PRO A CD  1 
ATOM   1494 N  N   . VAL A 1 217 ? 86.652  137.703 115.229 1.00 85.30  ? 198 VAL A N   1 
ATOM   1495 C  CA  . VAL A 1 217 ? 87.362  136.619 114.554 1.00 85.30  ? 198 VAL A CA  1 
ATOM   1496 C  C   . VAL A 1 217 ? 86.705  136.270 113.224 1.00 85.30  ? 198 VAL A C   1 
ATOM   1497 O  O   . VAL A 1 217 ? 87.392  135.907 112.263 1.00 85.30  ? 198 VAL A O   1 
ATOM   1498 C  CB  . VAL A 1 217 ? 87.454  135.391 115.482 1.00 85.30  ? 198 VAL A CB  1 
ATOM   1499 C  CG1 . VAL A 1 217 ? 88.144  134.232 114.779 1.00 85.30  ? 198 VAL A CG1 1 
ATOM   1500 C  CG2 . VAL A 1 217 ? 88.185  135.753 116.763 1.00 85.30  ? 198 VAL A CG2 1 
ATOM   1501 N  N   . GLU A 1 218 ? 85.378  136.384 113.135 1.00 89.55  ? 199 GLU A N   1 
ATOM   1502 C  CA  . GLU A 1 218 ? 84.697  136.083 111.878 1.00 89.55  ? 199 GLU A CA  1 
ATOM   1503 C  C   . GLU A 1 218 ? 85.001  137.134 110.814 1.00 89.55  ? 199 GLU A C   1 
ATOM   1504 O  O   . GLU A 1 218 ? 85.103  136.813 109.623 1.00 89.55  ? 199 GLU A O   1 
ATOM   1505 C  CB  . GLU A 1 218 ? 83.189  135.968 112.107 1.00 89.55  ? 199 GLU A CB  1 
ATOM   1506 C  CG  . GLU A 1 218 ? 82.791  135.052 113.257 1.00 89.55  ? 199 GLU A CG  1 
ATOM   1507 C  CD  . GLU A 1 218 ? 82.756  135.764 114.597 1.00 89.55  ? 199 GLU A CD  1 
ATOM   1508 O  OE1 . GLU A 1 218 ? 83.811  136.273 115.032 1.00 89.55  ? 199 GLU A OE1 1 
ATOM   1509 O  OE2 . GLU A 1 218 ? 81.672  135.816 115.214 1.00 89.55  ? 199 GLU A OE2 1 
ATOM   1510 N  N   . GLN A 1 219 ? 85.141  138.396 111.219 1.00 86.50  ? 200 GLN A N   1 
ATOM   1511 C  CA  . GLN A 1 219 ? 85.478  139.428 110.246 1.00 86.50  ? 200 GLN A CA  1 
ATOM   1512 C  C   . GLN A 1 219 ? 86.886  139.230 109.696 1.00 86.50  ? 200 GLN A C   1 
ATOM   1513 O  O   . GLN A 1 219 ? 87.113  139.404 108.495 1.00 86.50  ? 200 GLN A O   1 
ATOM   1514 C  CB  . GLN A 1 219 ? 85.323  140.812 110.871 1.00 86.50  ? 200 GLN A CB  1 
ATOM   1515 C  CG  . GLN A 1 219 ? 84.000  141.485 110.552 1.00 86.50  ? 200 GLN A CG  1 
ATOM   1516 C  CD  . GLN A 1 219 ? 83.945  142.021 109.134 1.00 86.50  ? 200 GLN A CD  1 
ATOM   1517 O  OE1 . GLN A 1 219 ? 84.956  142.061 108.433 1.00 86.50  ? 200 GLN A OE1 1 
ATOM   1518 N  NE2 . GLN A 1 219 ? 82.759  142.435 108.705 1.00 86.50  ? 200 GLN A NE2 1 
ATOM   1519 N  N   . GLN A 1 220 ? 87.842  138.859 110.551 1.00 84.38  ? 201 GLN A N   1 
ATOM   1520 C  CA  . GLN A 1 220 ? 89.171  138.500 110.060 1.00 84.38  ? 201 GLN A CA  1 
ATOM   1521 C  C   . GLN A 1 220 ? 89.106  137.264 109.172 1.00 84.38  ? 201 GLN A C   1 
ATOM   1522 O  O   . GLN A 1 220 ? 89.805  137.177 108.153 1.00 84.38  ? 201 GLN A O   1 
ATOM   1523 C  CB  . GLN A 1 220 ? 90.114  138.255 111.237 1.00 84.38  ? 201 GLN A CB  1 
ATOM   1524 C  CG  . GLN A 1 220 ? 90.189  139.399 112.230 1.00 84.38  ? 201 GLN A CG  1 
ATOM   1525 C  CD  . GLN A 1 220 ? 91.143  139.113 113.373 1.00 84.38  ? 201 GLN A CD  1 
ATOM   1526 O  OE1 . GLN A 1 220 ? 91.733  138.036 113.448 1.00 84.38  ? 201 GLN A OE1 1 
ATOM   1527 N  NE2 . GLN A 1 220 ? 91.293  140.075 114.273 1.00 84.38  ? 201 GLN A NE2 1 
ATOM   1528 N  N   . GLU A 1 221 ? 88.269  136.298 109.556 1.00 89.10  ? 202 GLU A N   1 
ATOM   1529 C  CA  . GLU A 1 221 ? 88.003  135.116 108.746 1.00 89.10  ? 202 GLU A CA  1 
ATOM   1530 C  C   . GLU A 1 221 ? 87.639  135.504 107.320 1.00 89.10  ? 202 GLU A C   1 
ATOM   1531 O  O   . GLU A 1 221 ? 88.191  134.972 106.350 1.00 89.10  ? 202 GLU A O   1 
ATOM   1532 C  CB  . GLU A 1 221 ? 86.862  134.329 109.396 1.00 89.10  ? 202 GLU A CB  1 
ATOM   1533 C  CG  . GLU A 1 221 ? 87.197  132.972 109.980 1.00 89.10  ? 202 GLU A CG  1 
ATOM   1534 C  CD  . GLU A 1 221 ? 87.417  131.906 108.937 1.00 89.10  ? 202 GLU A CD  1 
ATOM   1535 O  OE1 . GLU A 1 221 ? 87.330  132.207 107.728 1.00 89.10  ? 202 GLU A OE1 1 
ATOM   1536 O  OE2 . GLU A 1 221 ? 87.640  130.748 109.338 1.00 89.10  ? 202 GLU A OE2 1 
ATOM   1537 N  N   . LYS A 1 222 ? 86.702  136.443 107.182 1.00 88.89  ? 203 LYS A N   1 
ATOM   1538 C  CA  . LYS A 1 222 ? 86.249  136.852 105.856 1.00 88.89  ? 203 LYS A CA  1 
ATOM   1539 C  C   . LYS A 1 222 ? 87.285  137.718 105.145 1.00 88.89  ? 203 LYS A C   1 
ATOM   1540 O  O   . LYS A 1 222 ? 87.444  137.622 103.922 1.00 88.89  ? 203 LYS A O   1 
ATOM   1541 C  CB  . LYS A 1 222 ? 84.914  137.587 105.964 1.00 88.89  ? 203 LYS A CB  1 
ATOM   1542 C  CG  . LYS A 1 222 ? 83.822  136.770 106.633 1.00 88.89  ? 203 LYS A CG  1 
ATOM   1543 C  CD  . LYS A 1 222 ? 82.493  136.931 105.921 1.00 88.89  ? 203 LYS A CD  1 
ATOM   1544 C  CE  . LYS A 1 222 ? 81.483  135.911 106.416 1.00 88.89  ? 203 LYS A CE  1 
ATOM   1545 N  NZ  . LYS A 1 222 ? 82.057  134.538 106.442 1.00 88.89  ? 203 LYS A NZ  1 
ATOM   1546 N  N   . ILE A 1 223 ? 87.994  138.572 105.887 1.00 85.28  ? 204 ILE A N   1 
ATOM   1547 C  CA  . ILE A 1 223 ? 88.946  139.491 105.267 1.00 85.28  ? 204 ILE A CA  1 
ATOM   1548 C  C   . ILE A 1 223 ? 90.116  138.728 104.660 1.00 85.28  ? 204 ILE A C   1 
ATOM   1549 O  O   . ILE A 1 223 ? 90.499  138.962 103.508 1.00 85.28  ? 204 ILE A O   1 
ATOM   1550 C  CB  . ILE A 1 223 ? 89.423  140.541 106.286 1.00 85.28  ? 204 ILE A CB  1 
ATOM   1551 C  CG1 . ILE A 1 223 ? 88.325  141.575 106.539 1.00 85.28  ? 204 ILE A CG1 1 
ATOM   1552 C  CG2 . ILE A 1 223 ? 90.690  141.221 105.799 1.00 85.28  ? 204 ILE A CG2 1 
ATOM   1553 C  CD1 . ILE A 1 223 ? 88.589  142.463 107.732 1.00 85.28  ? 204 ILE A CD1 1 
ATOM   1554 N  N   . ILE A 1 224 ? 90.704  137.803 105.422 1.00 83.86  ? 205 ILE A N   1 
ATOM   1555 C  CA  . ILE A 1 224 ? 91.836  137.044 104.899 1.00 83.86  ? 205 ILE A CA  1 
ATOM   1556 C  C   . ILE A 1 224 ? 91.378  136.106 103.790 1.00 83.86  ? 205 ILE A C   1 
ATOM   1557 O  O   . ILE A 1 224 ? 92.054  135.952 102.765 1.00 83.86  ? 205 ILE A O   1 
ATOM   1558 C  CB  . ILE A 1 224 ? 92.544  136.284 106.035 1.00 83.86  ? 205 ILE A CB  1 
ATOM   1559 C  CG1 . ILE A 1 224 ? 93.223  137.269 106.986 1.00 83.86  ? 205 ILE A CG1 1 
ATOM   1560 C  CG2 . ILE A 1 224 ? 93.569  135.315 105.472 1.00 83.86  ? 205 ILE A CG2 1 
ATOM   1561 C  CD1 . ILE A 1 224 ? 94.347  138.048 106.347 1.00 83.86  ? 205 ILE A CD1 1 
ATOM   1562 N  N   . GLY A 1 225 ? 90.222  135.476 103.968 1.00 88.40  ? 206 GLY A N   1 
ATOM   1563 C  CA  . GLY A 1 225 ? 89.700  134.507 103.032 1.00 88.40  ? 206 GLY A CA  1 
ATOM   1564 C  C   . GLY A 1 225 ? 90.029  133.067 103.348 1.00 88.40  ? 206 GLY A C   1 
ATOM   1565 O  O   . GLY A 1 225 ? 89.567  132.172 102.628 1.00 88.40  ? 206 GLY A O   1 
ATOM   1566 N  N   . ARG A 1 226 ? 90.806  132.812 104.391 1.00 86.86  ? 207 ARG A N   1 
ATOM   1567 C  CA  . ARG A 1 226 ? 91.074  131.464 104.867 1.00 86.86  ? 207 ARG A CA  1 
ATOM   1568 C  C   . ARG A 1 226 ? 90.579  131.372 106.308 1.00 86.86  ? 207 ARG A C   1 
ATOM   1569 O  O   . ARG A 1 226 ? 89.926  132.285 106.818 1.00 86.86  ? 207 ARG A O   1 
ATOM   1570 C  CB  . ARG A 1 226 ? 92.566  131.142 104.762 1.00 86.86  ? 207 ARG A CB  1 
ATOM   1571 C  CG  . ARG A 1 226 ? 93.152  131.294 103.369 1.00 86.86  ? 207 ARG A CG  1 
ATOM   1572 C  CD  . ARG A 1 226 ? 94.520  130.636 103.275 1.00 86.86  ? 207 ARG A CD  1 
ATOM   1573 N  NE  . ARG A 1 226 ? 94.447  129.182 103.329 1.00 86.86  ? 207 ARG A NE  1 
ATOM   1574 C  CZ  . ARG A 1 226 ? 94.286  128.401 102.270 1.00 86.86  ? 207 ARG A CZ  1 
ATOM   1575 N  NH1 . ARG A 1 226 ? 94.174  128.904 101.051 1.00 86.86  ? 207 ARG A NH1 1 
ATOM   1576 N  NH2 . ARG A 1 226 ? 94.240  127.082 102.436 1.00 86.86  ? 207 ARG A NH2 1 
ATOM   1577 N  N   . GLU A 1 227 ? 90.900  130.270 106.971 1.00 89.68  ? 208 GLU A N   1 
ATOM   1578 C  CA  . GLU A 1 227 ? 90.569  130.117 108.378 1.00 89.68  ? 208 GLU A CA  1 
ATOM   1579 C  C   . GLU A 1 227 ? 91.812  130.382 109.217 1.00 89.68  ? 208 GLU A C   1 
ATOM   1580 O  O   . GLU A 1 227 ? 92.942  130.326 108.726 1.00 89.68  ? 208 GLU A O   1 
ATOM   1581 C  CB  . GLU A 1 227 ? 89.982  128.731 108.660 1.00 89.68  ? 208 GLU A CB  1 
ATOM   1582 C  CG  . GLU A 1 227 ? 88.810  128.392 107.740 1.00 89.68  ? 208 GLU A CG  1 
ATOM   1583 C  CD  . GLU A 1 227 ? 88.358  126.952 107.839 1.00 89.68  ? 208 GLU A CD  1 
ATOM   1584 O  OE1 . GLU A 1 227 ? 88.940  126.199 108.641 1.00 89.68  ? 208 GLU A OE1 1 
ATOM   1585 O  OE2 . GLU A 1 227 ? 87.416  126.573 107.112 1.00 89.68  ? 208 GLU A OE2 1 
ATOM   1586 N  N   . LYS A 1 228 ? 91.596  130.670 110.500 1.00 82.38  ? 209 LYS A N   1 
ATOM   1587 C  CA  . LYS A 1 228 ? 92.723  131.039 111.355 1.00 82.38  ? 209 LYS A CA  1 
ATOM   1588 C  C   . LYS A 1 228 ? 93.458  129.792 111.836 1.00 82.38  ? 209 LYS A C   1 
ATOM   1589 O  O   . LYS A 1 228 ? 94.604  129.543 111.448 1.00 82.38  ? 209 LYS A O   1 
ATOM   1590 C  CB  . LYS A 1 228 ? 92.226  131.886 112.531 1.00 82.38  ? 209 LYS A CB  1 
ATOM   1591 C  CG  . LYS A 1 228 ? 93.324  132.566 113.329 1.00 82.38  ? 209 LYS A CG  1 
ATOM   1592 C  CD  . LYS A 1 228 ? 92.813  133.862 113.943 1.00 82.38  ? 209 LYS A CD  1 
ATOM   1593 C  CE  . LYS A 1 228 ? 93.924  134.643 114.621 1.00 82.38  ? 209 LYS A CE  1 
ATOM   1594 N  NZ  . LYS A 1 228 ? 93.453  135.972 115.098 1.00 82.38  ? 209 LYS A NZ  1 
ATOM   1595 N  N   . LEU A 1 229 ? 92.806  128.997 112.684 1.00 84.82  ? 210 LEU A N   1 
ATOM   1596 C  CA  . LEU A 1 229 ? 93.450  127.812 113.240 1.00 84.82  ? 210 LEU A CA  1 
ATOM   1597 C  C   . LEU A 1 229 ? 93.596  126.723 112.184 1.00 84.82  ? 210 LEU A C   1 
ATOM   1598 O  O   . LEU A 1 229 ? 94.701  126.236 111.917 1.00 84.82  ? 210 LEU A O   1 
ATOM   1599 C  CB  . LEU A 1 229 ? 92.659  127.299 114.446 1.00 84.82  ? 210 LEU A CB  1 
ATOM   1600 C  CG  . LEU A 1 229 ? 93.440  126.453 115.454 1.00 84.82  ? 210 LEU A CG  1 
ATOM   1601 C  CD1 . LEU A 1 229 ? 94.883  126.916 115.550 1.00 84.82  ? 210 LEU A CD1 1 
ATOM   1602 C  CD2 . LEU A 1 229 ? 92.777  126.502 116.815 1.00 84.82  ? 210 LEU A CD2 1 
ATOM   1603 N  N   . SER A 1 230 ? 92.477  126.323 111.574 1.00 90.71  ? 211 SER A N   1 
ATOM   1604 C  CA  . SER A 1 230 ? 92.473  125.216 110.624 1.00 90.71  ? 211 SER A CA  1 
ATOM   1605 C  C   . SER A 1 230 ? 93.204  125.528 109.323 1.00 90.71  ? 211 SER A C   1 
ATOM   1606 O  O   . SER A 1 230 ? 93.554  124.589 108.600 1.00 90.71  ? 211 SER A O   1 
ATOM   1607 C  CB  . SER A 1 230 ? 91.041  124.784 110.325 1.00 90.71  ? 211 SER A CB  1 
ATOM   1608 O  OG  . SER A 1 230 ? 90.505  124.045 111.408 1.00 90.71  ? 211 SER A OG  1 
ATOM   1609 N  N   . ASP A 1 231 ? 93.458  126.803 109.016 1.00 89.98  ? 212 ASP A N   1 
ATOM   1610 C  CA  . ASP A 1 231 ? 94.223  127.205 107.830 1.00 89.98  ? 212 ASP A CA  1 
ATOM   1611 C  C   . ASP A 1 231 ? 93.625  126.574 106.556 1.00 89.98  ? 212 ASP A C   1 
ATOM   1612 O  O   . ASP A 1 231 ? 94.314  126.323 105.564 1.00 89.98  ? 212 ASP A O   1 
ATOM   1613 C  CB  . ASP A 1 231 ? 95.712  126.856 108.020 1.00 89.98  ? 212 ASP A CB  1 
ATOM   1614 C  CG  . ASP A 1 231 ? 96.594  127.182 106.814 1.00 89.98  ? 212 ASP A CG  1 
ATOM   1615 O  OD1 . ASP A 1 231 ? 97.788  126.820 106.860 1.00 89.98  ? 212 ASP A OD1 1 
ATOM   1616 O  OD2 . ASP A 1 231 ? 96.156  127.896 105.887 1.00 89.98  ? 212 ASP A OD2 1 
ATOM   1617 N  N   . ILE A 1 232 ? 92.343  126.241 106.586 1.00 90.15  ? 213 ILE A N   1 
ATOM   1618 C  CA  . ILE A 1 232 ? 91.659  125.687 105.426 1.00 90.15  ? 213 ILE A CA  1 
ATOM   1619 C  C   . ILE A 1 232 ? 90.958  126.840 104.725 1.00 90.15  ? 213 ILE A C   1 
ATOM   1620 O  O   . ILE A 1 232 ? 90.587  127.836 105.353 1.00 90.15  ? 213 ILE A O   1 
ATOM   1621 C  CB  . ILE A 1 232 ? 90.670  124.577 105.851 1.00 90.15  ? 213 ILE A CB  1 
ATOM   1622 C  CG1 . ILE A 1 232 ? 91.433  123.347 106.340 1.00 90.15  ? 213 ILE A CG1 1 
ATOM   1623 C  CG2 . ILE A 1 232 ? 89.745  124.169 104.714 1.00 90.15  ? 213 ILE A CG2 1 
ATOM   1624 C  CD1 . ILE A 1 232 ? 92.462  122.844 105.347 1.00 90.15  ? 213 ILE A CD1 1 
ATOM   1625 N  N   . GLU A 1 233 ? 90.791  126.728 103.410 1.00 91.47  ? 214 GLU A N   1 
ATOM   1626 C  CA  . GLU A 1 233 ? 90.235  127.846 102.665 1.00 91.47  ? 214 GLU A CA  1 
ATOM   1627 C  C   . GLU A 1 233 ? 88.730  127.950 102.915 1.00 91.47  ? 214 GLU A C   1 
ATOM   1628 O  O   . GLU A 1 233 ? 88.137  127.184 103.679 1.00 91.47  ? 214 GLU A O   1 
ATOM   1629 C  CB  . GLU A 1 233 ? 90.544  127.684 101.178 1.00 91.47  ? 214 GLU A CB  1 
ATOM   1630 C  CG  . GLU A 1 233 ? 90.639  128.993 100.401 1.00 91.47  ? 214 GLU A CG  1 
ATOM   1631 C  CD  . GLU A 1 233 ? 91.017  128.783 98.948  1.00 91.47  ? 214 GLU A CD  1 
ATOM   1632 O  OE1 . GLU A 1 233 ? 91.170  127.613 98.544  1.00 91.47  ? 214 GLU A OE1 1 
ATOM   1633 O  OE2 . GLU A 1 233 ? 91.159  129.782 98.211  1.00 91.47  ? 214 GLU A OE2 1 
ATOM   1634 N  N   . LEU A 1 234 ? 88.106  128.918 102.253 1.00 94.87  ? 215 LEU A N   1 
ATOM   1635 C  CA  . LEU A 1 234 ? 86.671  129.137 102.327 1.00 94.87  ? 215 LEU A CA  1 
ATOM   1636 C  C   . LEU A 1 234 ? 86.048  128.928 100.956 1.00 94.87  ? 215 LEU A C   1 
ATOM   1637 O  O   . LEU A 1 234 ? 86.691  129.146 99.924  1.00 94.87  ? 215 LEU A O   1 
ATOM   1638 C  CB  . LEU A 1 234 ? 86.341  130.543 102.835 1.00 94.87  ? 215 LEU A CB  1 
ATOM   1639 C  CG  . LEU A 1 234 ? 86.829  130.913 104.235 1.00 94.87  ? 215 LEU A CG  1 
ATOM   1640 C  CD1 . LEU A 1 234 ? 86.478  132.354 104.545 1.00 94.87  ? 215 LEU A CD1 1 
ATOM   1641 C  CD2 . LEU A 1 234 ? 86.234  129.981 105.271 1.00 94.87  ? 215 LEU A CD2 1 
ATOM   1642 N  N   . ARG A 1 235 ? 84.793  128.495 100.950 1.00 103.59 ? 216 ARG A N   1 
ATOM   1643 C  CA  . ARG A 1 235 ? 84.106  128.236 99.695  1.00 103.59 ? 216 ARG A CA  1 
ATOM   1644 C  C   . ARG A 1 235 ? 83.830  129.551 98.974  1.00 103.59 ? 216 ARG A C   1 
ATOM   1645 O  O   . ARG A 1 235 ? 83.658  130.601 99.599  1.00 103.59 ? 216 ARG A O   1 
ATOM   1646 C  CB  . ARG A 1 235 ? 82.800  127.483 99.945  1.00 103.59 ? 216 ARG A CB  1 
ATOM   1647 C  CG  . ARG A 1 235 ? 82.989  126.094 100.528 1.00 103.59 ? 216 ARG A CG  1 
ATOM   1648 C  CD  . ARG A 1 235 ? 81.798  125.690 101.378 1.00 103.59 ? 216 ARG A CD  1 
ATOM   1649 N  NE  . ARG A 1 235 ? 81.579  126.622 102.478 1.00 103.59 ? 216 ARG A NE  1 
ATOM   1650 C  CZ  . ARG A 1 235 ? 82.167  126.532 103.663 1.00 103.59 ? 216 ARG A CZ  1 
ATOM   1651 N  NH1 . ARG A 1 235 ? 83.020  125.558 103.939 1.00 103.59 ? 216 ARG A NH1 1 
ATOM   1652 N  NH2 . ARG A 1 235 ? 81.894  127.441 104.594 1.00 103.59 ? 216 ARG A NH2 1 
ATOM   1653 N  N   . ASP A 1 236 ? 83.795  129.486 97.641  1.00 106.83 ? 217 ASP A N   1 
ATOM   1654 C  CA  . ASP A 1 236 ? 83.607  130.694 96.843  1.00 106.83 ? 217 ASP A CA  1 
ATOM   1655 C  C   . ASP A 1 236 ? 82.288  131.392 97.144  1.00 106.83 ? 217 ASP A C   1 
ATOM   1656 O  O   . ASP A 1 236 ? 82.164  132.595 96.892  1.00 106.83 ? 217 ASP A O   1 
ATOM   1657 C  CB  . ASP A 1 236 ? 83.692  130.357 95.354  1.00 106.83 ? 217 ASP A CB  1 
ATOM   1658 C  CG  . ASP A 1 236 ? 85.091  129.962 94.927  1.00 106.83 ? 217 ASP A CG  1 
ATOM   1659 O  OD1 . ASP A 1 236 ? 86.060  130.408 95.576  1.00 106.83 ? 217 ASP A OD1 1 
ATOM   1660 O  OD2 . ASP A 1 236 ? 85.221  129.206 93.941  1.00 106.83 ? 217 ASP A OD2 1 
ATOM   1661 N  N   . ALA A 1 237 ? 81.303  130.670 97.676  1.00 105.25 ? 218 ALA A N   1 
ATOM   1662 C  CA  . ALA A 1 237 ? 80.050  131.284 98.090  1.00 105.25 ? 218 ALA A CA  1 
ATOM   1663 C  C   . ALA A 1 237 ? 80.174  132.059 99.395  1.00 105.25 ? 218 ALA A C   1 
ATOM   1664 O  O   . ALA A 1 237 ? 79.277  132.846 99.715  1.00 105.25 ? 218 ALA A O   1 
ATOM   1665 C  CB  . ALA A 1 237 ? 78.961  130.218 98.229  1.00 105.25 ? 218 ALA A CB  1 
ATOM   1666 N  N   . ASP A 1 238 ? 81.253  131.857 100.153 1.00 101.54 ? 219 ASP A N   1 
ATOM   1667 C  CA  . ASP A 1 238 ? 81.431  132.509 101.442 1.00 101.54 ? 219 ASP A CA  1 
ATOM   1668 C  C   . ASP A 1 238 ? 82.523  133.569 101.454 1.00 101.54 ? 219 ASP A C   1 
ATOM   1669 O  O   . ASP A 1 238 ? 82.594  134.342 102.416 1.00 101.54 ? 219 ASP A O   1 
ATOM   1670 C  CB  . ASP A 1 238 ? 81.737  131.465 102.527 1.00 101.54 ? 219 ASP A CB  1 
ATOM   1671 C  CG  . ASP A 1 238 ? 80.623  130.452 102.690 1.00 101.54 ? 219 ASP A CG  1 
ATOM   1672 O  OD1 . ASP A 1 238 ? 79.442  130.841 102.575 1.00 101.54 ? 219 ASP A OD1 1 
ATOM   1673 O  OD2 . ASP A 1 238 ? 80.928  129.266 102.935 1.00 101.54 ? 219 ASP A OD2 1 
ATOM   1674 N  N   . LYS A 1 239 ? 83.376  133.627 100.432 1.00 96.53  ? 220 LYS A N   1 
ATOM   1675 C  CA  . LYS A 1 239 ? 84.413  134.650 100.367 1.00 96.53  ? 220 LYS A CA  1 
ATOM   1676 C  C   . LYS A 1 239 ? 83.875  135.887 99.663  1.00 96.53  ? 220 LYS A C   1 
ATOM   1677 O  O   . LYS A 1 239 ? 83.500  135.799 98.486  1.00 96.53  ? 220 LYS A O   1 
ATOM   1678 C  CB  . LYS A 1 239 ? 85.641  134.137 99.634  1.00 96.53  ? 220 LYS A CB  1 
ATOM   1679 C  CG  . LYS A 1 239 ? 86.491  133.172 100.435 1.00 96.53  ? 220 LYS A CG  1 
ATOM   1680 C  CD  . LYS A 1 239 ? 87.802  132.876 99.724  1.00 96.53  ? 220 LYS A CD  1 
ATOM   1681 C  CE  . LYS A 1 239 ? 87.578  132.057 98.466  1.00 96.53  ? 220 LYS A CE  1 
ATOM   1682 N  NZ  . LYS A 1 239 ? 88.862  131.615 97.857  1.00 96.53  ? 220 LYS A NZ  1 
ATOM   1683 N  N   . PRO A 1 240 ? 83.808  137.038 100.329 1.00 92.78  ? 221 PRO A N   1 
ATOM   1684 C  CA  . PRO A 1 240 ? 83.353  138.260 99.655  1.00 92.78  ? 221 PRO A CA  1 
ATOM   1685 C  C   . PRO A 1 240 ? 84.296  138.661 98.530  1.00 92.78  ? 221 PRO A C   1 
ATOM   1686 O  O   . PRO A 1 240 ? 85.362  138.078 98.321  1.00 92.78  ? 221 PRO A O   1 
ATOM   1687 C  CB  . PRO A 1 240 ? 83.342  139.319 100.762 1.00 92.78  ? 221 PRO A CB  1 
ATOM   1688 C  CG  . PRO A 1 240 ? 83.746  138.637 102.020 1.00 92.78  ? 221 PRO A CG  1 
ATOM   1689 C  CD  . PRO A 1 240 ? 83.839  137.170 101.794 1.00 92.78  ? 221 PRO A CD  1 
ATOM   1690 N  N   . SER A 1 241 ? 83.884  139.695 97.795  1.00 95.99  ? 222 SER A N   1 
ATOM   1691 C  CA  . SER A 1 241 ? 84.682  140.186 96.678  1.00 95.99  ? 222 SER A CA  1 
ATOM   1692 C  C   . SER A 1 241 ? 85.976  140.850 97.127  1.00 95.99  ? 222 SER A C   1 
ATOM   1693 O  O   . SER A 1 241 ? 86.890  141.009 96.310  1.00 95.99  ? 222 SER A O   1 
ATOM   1694 C  CB  . SER A 1 241 ? 83.864  141.167 95.837  1.00 95.99  ? 222 SER A CB  1 
ATOM   1695 O  OG  . SER A 1 241 ? 84.704  142.124 95.214  1.00 95.99  ? 222 SER A OG  1 
ATOM   1696 N  N   . TYR A 1 242 ? 86.079  141.243 98.397  1.00 92.26  ? 223 TYR A N   1 
ATOM   1697 C  CA  . TYR A 1 242 ? 87.269  141.908 98.915  1.00 92.26  ? 223 TYR A CA  1 
ATOM   1698 C  C   . TYR A 1 242 ? 88.109  141.002 99.809  1.00 92.26  ? 223 TYR A C   1 
ATOM   1699 O  O   . TYR A 1 242 ? 88.865  141.499 100.650 1.00 92.26  ? 223 TYR A O   1 
ATOM   1700 C  CB  . TYR A 1 242 ? 86.890  143.185 99.668  1.00 92.26  ? 223 TYR A CB  1 
ATOM   1701 C  CG  . TYR A 1 242 ? 86.011  142.972 100.881 1.00 92.26  ? 223 TYR A CG  1 
ATOM   1702 C  CD1 . TYR A 1 242 ? 84.658  142.695 100.747 1.00 92.26  ? 223 TYR A CD1 1 
ATOM   1703 C  CD2 . TYR A 1 242 ? 86.541  143.031 102.160 1.00 92.26  ? 223 TYR A CD2 1 
ATOM   1704 C  CE1 . TYR A 1 242 ? 83.855  142.503 101.855 1.00 92.26  ? 223 TYR A CE1 1 
ATOM   1705 C  CE2 . TYR A 1 242 ? 85.748  142.835 103.273 1.00 92.26  ? 223 TYR A CE2 1 
ATOM   1706 C  CZ  . TYR A 1 242 ? 84.407  142.570 103.115 1.00 92.26  ? 223 TYR A CZ  1 
ATOM   1707 O  OH  . TYR A 1 242 ? 83.614  142.373 104.221 1.00 92.26  ? 223 TYR A OH  1 
ATOM   1708 N  N   . ALA A 1 243 ? 87.994  139.688 99.650  1.00 87.93  ? 224 ALA A N   1 
ATOM   1709 C  CA  . ALA A 1 243 ? 88.882  138.779 100.357 1.00 87.93  ? 224 ALA A CA  1 
ATOM   1710 C  C   . ALA A 1 243 ? 90.309  138.933 99.843  1.00 87.93  ? 224 ALA A C   1 
ATOM   1711 O  O   . ALA A 1 243 ? 90.541  139.194 98.660  1.00 87.93  ? 224 ALA A O   1 
ATOM   1712 C  CB  . ALA A 1 243 ? 88.415  137.334 100.195 1.00 87.93  ? 224 ALA A CB  1 
ATOM   1713 N  N   . HIS A 1 244 ? 91.272  138.778 100.755 1.00 85.01  ? 225 HIS A N   1 
ATOM   1714 C  CA  . HIS A 1 244 ? 92.668  139.009 100.395 1.00 85.01  ? 225 HIS A CA  1 
ATOM   1715 C  C   . HIS A 1 244 ? 93.140  138.025 99.333  1.00 85.01  ? 225 HIS A C   1 
ATOM   1716 O  O   . HIS A 1 244 ? 93.819  138.415 98.376  1.00 85.01  ? 225 HIS A O   1 
ATOM   1717 C  CB  . HIS A 1 244 ? 93.553  138.923 101.638 1.00 85.01  ? 225 HIS A CB  1 
ATOM   1718 C  CG  . HIS A 1 244 ? 95.008  139.133 101.357 1.00 85.01  ? 225 HIS A CG  1 
ATOM   1719 N  ND1 . HIS A 1 244 ? 95.504  140.310 100.841 1.00 85.01  ? 225 HIS A ND1 1 
ATOM   1720 C  CD2 . HIS A 1 244 ? 96.075  138.317 101.524 1.00 85.01  ? 225 HIS A CD2 1 
ATOM   1721 C  CE1 . HIS A 1 244 ? 96.813  140.210 100.701 1.00 85.01  ? 225 HIS A CE1 1 
ATOM   1722 N  NE2 . HIS A 1 244 ? 97.185  139.010 101.109 1.00 85.01  ? 225 HIS A NE2 1 
ATOM   1723 N  N   . ASN A 1 245 ? 92.789  136.747 99.475  1.00 87.80  ? 226 ASN A N   1 
ATOM   1724 C  CA  . ASN A 1 245 ? 93.198  135.755 98.488  1.00 87.80  ? 226 ASN A CA  1 
ATOM   1725 C  C   . ASN A 1 245 ? 92.384  135.821 97.201  1.00 87.80  ? 226 ASN A C   1 
ATOM   1726 O  O   . ASN A 1 245 ? 92.776  135.201 96.207  1.00 87.80  ? 226 ASN A O   1 
ATOM   1727 C  CB  . ASN A 1 245 ? 93.172  134.347 99.118  1.00 87.80  ? 226 ASN A CB  1 
ATOM   1728 C  CG  . ASN A 1 245 ? 91.783  133.694 99.141  1.00 87.80  ? 226 ASN A CG  1 
ATOM   1729 O  OD1 . ASN A 1 245 ? 90.804  134.201 98.597  1.00 87.80  ? 226 ASN A OD1 1 
ATOM   1730 N  ND2 . ASN A 1 245 ? 91.711  132.535 99.786  1.00 87.80  ? 226 ASN A ND2 1 
ATOM   1731 N  N   . VAL A 1 246 ? 91.264  136.546 97.198  1.00 88.13  ? 227 VAL A N   1 
ATOM   1732 C  CA  . VAL A 1 246 ? 90.494  136.729 95.973  1.00 88.13  ? 227 VAL A CA  1 
ATOM   1733 C  C   . VAL A 1 246 ? 91.071  137.866 95.139  1.00 88.13  ? 227 VAL A C   1 
ATOM   1734 O  O   . VAL A 1 246 ? 91.209  137.747 93.916  1.00 88.13  ? 227 VAL A O   1 
ATOM   1735 C  CB  . VAL A 1 246 ? 89.011  136.967 96.308  1.00 88.13  ? 227 VAL A CB  1 
ATOM   1736 C  CG1 . VAL A 1 246 ? 88.244  137.385 95.064  1.00 88.13  ? 227 VAL A CG1 1 
ATOM   1737 C  CG2 . VAL A 1 246 ? 88.399  135.716 96.913  1.00 88.13  ? 227 VAL A CG2 1 
ATOM   1738 N  N   . LEU A 1 247 ? 91.425  138.981 95.783  1.00 88.34  ? 228 LEU A N   1 
ATOM   1739 C  CA  . LEU A 1 247 ? 91.956  140.123 95.047  1.00 88.34  ? 228 LEU A CA  1 
ATOM   1740 C  C   . LEU A 1 247 ? 93.356  139.851 94.517  1.00 88.34  ? 228 LEU A C   1 
ATOM   1741 O  O   . LEU A 1 247 ? 93.754  140.428 93.498  1.00 88.34  ? 228 LEU A O   1 
ATOM   1742 C  CB  . LEU A 1 247 ? 91.962  141.365 95.936  1.00 88.34  ? 228 LEU A CB  1 
ATOM   1743 C  CG  . LEU A 1 247 ? 90.598  141.978 96.248  1.00 88.34  ? 228 LEU A CG  1 
ATOM   1744 C  CD1 . LEU A 1 247 ? 90.743  143.121 97.237  1.00 88.34  ? 228 LEU A CD1 1 
ATOM   1745 C  CD2 . LEU A 1 247 ? 89.923  142.452 94.974  1.00 88.34  ? 228 LEU A CD2 1 
ATOM   1746 N  N   . THR A 1 248 ? 94.113  138.986 95.184  1.00 88.48  ? 229 THR A N   1 
ATOM   1747 C  CA  . THR A 1 248 ? 95.472  138.666 94.773  1.00 88.48  ? 229 THR A CA  1 
ATOM   1748 C  C   . THR A 1 248 ? 95.538  137.510 93.785  1.00 88.48  ? 229 THR A C   1 
ATOM   1749 O  O   . THR A 1 248 ? 96.640  137.097 93.415  1.00 88.48  ? 229 THR A O   1 
ATOM   1750 C  CB  . THR A 1 248 ? 96.335  138.338 95.994  1.00 88.48  ? 229 THR A CB  1 
ATOM   1751 O  OG1 . THR A 1 248 ? 95.750  137.248 96.716  1.00 88.48  ? 229 THR A OG1 1 
ATOM   1752 C  CG2 . THR A 1 248 ? 96.449  139.548 96.905  1.00 88.48  ? 229 THR A CG2 1 
ATOM   1753 N  N   . SER A 1 249 ? 94.399  136.972 93.359  1.00 94.41  ? 230 SER A N   1 
ATOM   1754 C  CA  . SER A 1 249 ? 94.362  135.894 92.377  1.00 94.41  ? 230 SER A CA  1 
ATOM   1755 C  C   . SER A 1 249 ? 94.115  136.507 91.003  1.00 94.41  ? 230 SER A C   1 
ATOM   1756 O  O   . SER A 1 249 ? 93.017  136.997 90.720  1.00 94.41  ? 230 SER A O   1 
ATOM   1757 C  CB  . SER A 1 249 ? 93.284  134.873 92.730  1.00 94.41  ? 230 SER A CB  1 
ATOM   1758 O  OG  . SER A 1 249 ? 93.574  134.236 93.963  1.00 94.41  ? 230 SER A OG  1 
ATOM   1759 N  N   . ILE A 1 250 ? 95.140  136.475 90.149  1.00 106.46 ? 231 ILE A N   1 
ATOM   1760 C  CA  . ILE A 1 250 ? 95.067  137.043 88.812  1.00 106.46 ? 231 ILE A CA  1 
ATOM   1761 C  C   . ILE A 1 250 ? 95.545  136.008 87.802  1.00 106.46 ? 231 ILE A C   1 
ATOM   1762 O  O   . ILE A 1 250 ? 96.205  135.025 88.145  1.00 106.46 ? 231 ILE A O   1 
ATOM   1763 C  CB  . ILE A 1 250 ? 95.880  138.353 88.693  1.00 106.46 ? 231 ILE A CB  1 
ATOM   1764 C  CG1 . ILE A 1 250 ? 97.286  138.195 89.285  1.00 106.46 ? 231 ILE A CG1 1 
ATOM   1765 C  CG2 . ILE A 1 250 ? 95.143  139.494 89.373  1.00 106.46 ? 231 ILE A CG2 1 
ATOM   1766 C  CD1 . ILE A 1 250 ? 98.327  137.664 88.322  1.00 106.46 ? 231 ILE A CD1 1 
ATOM   1767 N  N   . GLU A 1 251 ? 95.199  136.244 86.538  1.00 117.49 ? 232 GLU A N   1 
ATOM   1768 C  CA  . GLU A 1 251 ? 95.459  135.297 85.466  1.00 117.49 ? 232 GLU A CA  1 
ATOM   1769 C  C   . GLU A 1 251 ? 96.088  136.013 84.279  1.00 117.49 ? 232 GLU A C   1 
ATOM   1770 O  O   . GLU A 1 251 ? 95.864  137.206 84.061  1.00 117.49 ? 232 GLU A O   1 
ATOM   1771 C  CB  . GLU A 1 251 ? 94.170  134.585 85.021  1.00 117.49 ? 232 GLU A CB  1 
ATOM   1772 C  CG  . GLU A 1 251 ? 93.162  135.479 84.302  1.00 117.49 ? 232 GLU A CG  1 
ATOM   1773 C  CD  . GLU A 1 251 ? 92.395  136.400 85.237  1.00 117.49 ? 232 GLU A CD  1 
ATOM   1774 O  OE1 . GLU A 1 251 ? 92.716  136.442 86.443  1.00 117.49 ? 232 GLU A OE1 1 
ATOM   1775 O  OE2 . GLU A 1 251 ? 91.466  137.086 84.761  1.00 117.49 ? 232 GLU A OE2 1 
ATOM   1776 N  N   . GLU A 1 252 ? 96.885  135.267 83.516  1.00 119.77 ? 233 GLU A N   1 
ATOM   1777 C  CA  . GLU A 1 252 ? 97.477  135.752 82.276  1.00 119.77 ? 233 GLU A CA  1 
ATOM   1778 C  C   . GLU A 1 252 ? 97.137  134.779 81.159  1.00 119.77 ? 233 GLU A C   1 
ATOM   1779 O  O   . GLU A 1 252 ? 97.357  133.571 81.298  1.00 119.77 ? 233 GLU A O   1 
ATOM   1780 C  CB  . GLU A 1 252 ? 98.997  135.906 82.399  1.00 119.77 ? 233 GLU A CB  1 
ATOM   1781 C  CG  . GLU A 1 252 ? 99.443  137.204 83.052  1.00 119.77 ? 233 GLU A CG  1 
ATOM   1782 C  CD  . GLU A 1 252 ? 100.952 137.322 83.139  1.00 119.77 ? 233 GLU A CD  1 
ATOM   1783 O  OE1 . GLU A 1 252 ? 101.652 136.435 82.608  1.00 119.77 ? 233 GLU A OE1 1 
ATOM   1784 O  OE2 . GLU A 1 252 ? 101.439 138.306 83.734  1.00 119.77 ? 233 GLU A OE2 1 
ATOM   1785 N  N   . ASP A 1 253 ? 96.602  135.309 80.057  1.00 127.85 ? 234 ASP A N   1 
ATOM   1786 C  CA  . ASP A 1 253 ? 96.227  134.513 78.887  1.00 127.85 ? 234 ASP A CA  1 
ATOM   1787 C  C   . ASP A 1 253 ? 95.251  133.396 79.250  1.00 127.85 ? 234 ASP A C   1 
ATOM   1788 O  O   . ASP A 1 253 ? 95.282  132.313 78.662  1.00 127.85 ? 234 ASP A O   1 
ATOM   1789 C  CB  . ASP A 1 253 ? 97.461  133.934 78.187  1.00 127.85 ? 234 ASP A CB  1 
ATOM   1790 C  CG  . ASP A 1 253 ? 98.405  135.009 77.686  1.00 127.85 ? 234 ASP A CG  1 
ATOM   1791 O  OD1 . ASP A 1 253 ? 97.918  136.061 77.220  1.00 127.85 ? 234 ASP A OD1 1 
ATOM   1792 O  OD2 . ASP A 1 253 ? 99.635  134.802 77.756  1.00 127.85 ? 234 ASP A OD2 1 
ATOM   1793 N  N   . GLY A 1 254 ? 94.380  133.652 80.224  1.00 126.64 ? 235 GLY A N   1 
ATOM   1794 C  CA  . GLY A 1 254 ? 93.409  132.675 80.665  1.00 126.64 ? 235 GLY A CA  1 
ATOM   1795 C  C   . GLY A 1 254 ? 93.922  131.650 81.651  1.00 126.64 ? 235 GLY A C   1 
ATOM   1796 O  O   . GLY A 1 254 ? 93.142  130.795 82.089  1.00 126.64 ? 235 GLY A O   1 
ATOM   1797 N  N   . GLU A 1 255 ? 95.199  131.703 82.018  1.00 125.19 ? 236 GLU A N   1 
ATOM   1798 C  CA  . GLU A 1 255 ? 95.789  130.765 82.962  1.00 125.19 ? 236 GLU A CA  1 
ATOM   1799 C  C   . GLU A 1 255 ? 96.257  131.508 84.204  1.00 125.19 ? 236 GLU A C   1 
ATOM   1800 O  O   . GLU A 1 255 ? 96.857  132.583 84.107  1.00 125.19 ? 236 GLU A O   1 
ATOM   1801 C  CB  . GLU A 1 255 ? 96.967  130.009 82.337  1.00 125.19 ? 236 GLU A CB  1 
ATOM   1802 C  CG  . GLU A 1 255 ? 96.576  129.053 81.224  1.00 125.19 ? 236 GLU A CG  1 
ATOM   1803 C  CD  . GLU A 1 255 ? 97.726  128.163 80.794  1.00 125.19 ? 236 GLU A CD  1 
ATOM   1804 O  OE1 . GLU A 1 255 ? 98.856  128.370 81.285  1.00 125.19 ? 236 GLU A OE1 1 
ATOM   1805 O  OE2 . GLU A 1 255 ? 97.500  127.256 79.966  1.00 125.19 ? 236 GLU A OE2 1 
ATOM   1806 N  N   . ASP A 1 256 ? 95.976  130.930 85.369  1.00 119.25 ? 237 ASP A N   1 
ATOM   1807 C  CA  . ASP A 1 256 ? 96.428  131.516 86.622  1.00 119.25 ? 237 ASP A CA  1 
ATOM   1808 C  C   . ASP A 1 256 ? 97.945  131.427 86.728  1.00 119.25 ? 237 ASP A C   1 
ATOM   1809 O  O   . ASP A 1 256 ? 98.547  130.398 86.408  1.00 119.25 ? 237 ASP A O   1 
ATOM   1810 C  CB  . ASP A 1 256 ? 95.774  130.807 87.806  1.00 119.25 ? 237 ASP A CB  1 
ATOM   1811 C  CG  . ASP A 1 256 ? 95.584  129.324 87.563  1.00 119.25 ? 237 ASP A CG  1 
ATOM   1812 O  OD1 . ASP A 1 256 ? 96.036  128.832 86.508  1.00 119.25 ? 237 ASP A OD1 1 
ATOM   1813 O  OD2 . ASP A 1 256 ? 94.983  128.651 88.426  1.00 119.25 ? 237 ASP A OD2 1 
ATOM   1814 N  N   . VAL A 1 257 ? 98.563  132.513 87.182  1.00 106.96 ? 238 VAL A N   1 
ATOM   1815 C  CA  . VAL A 1 257 ? 100.009 132.591 87.346  1.00 106.96 ? 238 VAL A CA  1 
ATOM   1816 C  C   . VAL A 1 257 ? 100.311 132.940 88.796  1.00 106.96 ? 238 VAL A C   1 
ATOM   1817 O  O   . VAL A 1 257 ? 99.682  133.835 89.371  1.00 106.96 ? 238 VAL A O   1 
ATOM   1818 C  CB  . VAL A 1 257 ? 100.638 133.619 86.387  1.00 106.96 ? 238 VAL A CB  1 
ATOM   1819 C  CG1 . VAL A 1 257 ? 100.665 133.068 84.971  1.00 106.96 ? 238 VAL A CG1 1 
ATOM   1820 C  CG2 . VAL A 1 257 ? 99.869  134.928 86.427  1.00 106.96 ? 238 VAL A CG2 1 
ATOM   1821 N  N   . ASP A 1 258 ? 101.262 132.223 89.386  1.00 100.16 ? 239 ASP A N   1 
ATOM   1822 C  CA  . ASP A 1 258 ? 101.614 132.376 90.788  1.00 100.16 ? 239 ASP A CA  1 
ATOM   1823 C  C   . ASP A 1 258 ? 102.952 133.088 90.929  1.00 100.16 ? 239 ASP A C   1 
ATOM   1824 O  O   . ASP A 1 258 ? 103.763 133.132 90.000  1.00 100.16 ? 239 ASP A O   1 
ATOM   1825 C  CB  . ASP A 1 258 ? 101.675 131.014 91.489  1.00 100.16 ? 239 ASP A CB  1 
ATOM   1826 C  CG  . ASP A 1 258 ? 100.385 130.228 91.354  1.00 100.16 ? 239 ASP A CG  1 
ATOM   1827 O  OD1 . ASP A 1 258 ? 99.431  130.749 90.740  1.00 100.16 ? 239 ASP A OD1 1 
ATOM   1828 O  OD2 . ASP A 1 258 ? 100.327 129.089 91.863  1.00 100.16 ? 239 ASP A OD2 1 
ATOM   1829 N  N   . ILE A 1 259 ? 103.171 133.652 92.117  1.00 85.63  ? 240 ILE A N   1 
ATOM   1830 C  CA  . ILE A 1 259 ? 104.428 134.296 92.472  1.00 85.63  ? 240 ILE A CA  1 
ATOM   1831 C  C   . ILE A 1 259 ? 104.912 133.695 93.783  1.00 85.63  ? 240 ILE A C   1 
ATOM   1832 O  O   . ILE A 1 259 ? 104.140 133.121 94.554  1.00 85.63  ? 240 ILE A O   1 
ATOM   1833 C  CB  . ILE A 1 259 ? 104.303 135.829 92.600  1.00 85.63  ? 240 ILE A CB  1 
ATOM   1834 C  CG1 . ILE A 1 259 ? 103.474 136.196 93.830  1.00 85.63  ? 240 ILE A CG1 1 
ATOM   1835 C  CG2 . ILE A 1 259 ? 103.687 136.423 91.346  1.00 85.63  ? 240 ILE A CG2 1 
ATOM   1836 C  CD1 . ILE A 1 259 ? 103.493 137.669 94.154  1.00 85.63  ? 240 ILE A CD1 1 
ATOM   1837 N  N   . LEU A 1 260 ? 106.211 133.829 94.028  1.00 81.24  ? 241 LEU A N   1 
ATOM   1838 C  CA  . LEU A 1 260 ? 106.844 133.260 95.210  1.00 81.24  ? 241 LEU A CA  1 
ATOM   1839 C  C   . LEU A 1 260 ? 106.982 134.350 96.264  1.00 81.24  ? 241 LEU A C   1 
ATOM   1840 O  O   . LEU A 1 260 ? 107.600 135.390 96.010  1.00 81.24  ? 241 LEU A O   1 
ATOM   1841 C  CB  . LEU A 1 260 ? 108.209 132.669 94.860  1.00 81.24  ? 241 LEU A CB  1 
ATOM   1842 C  CG  . LEU A 1 260 ? 108.916 131.884 95.964  1.00 81.24  ? 241 LEU A CG  1 
ATOM   1843 C  CD1 . LEU A 1 260 ? 108.183 130.584 96.246  1.00 81.24  ? 241 LEU A CD1 1 
ATOM   1844 C  CD2 . LEU A 1 260 ? 110.361 131.618 95.585  1.00 81.24  ? 241 LEU A CD2 1 
ATOM   1845 N  N   . ARG A 1 261 ? 106.411 134.111 97.442  1.00 79.60  ? 242 ARG A N   1 
ATOM   1846 C  CA  . ARG A 1 261 ? 106.417 135.074 98.534  1.00 79.60  ? 242 ARG A CA  1 
ATOM   1847 C  C   . ARG A 1 261 ? 107.114 134.479 99.748  1.00 79.60  ? 242 ARG A C   1 
ATOM   1848 O  O   . ARG A 1 261 ? 106.945 133.295 100.055 1.00 79.60  ? 242 ARG A O   1 
ATOM   1849 C  CB  . ARG A 1 261 ? 104.994 135.487 98.913  1.00 79.60  ? 242 ARG A CB  1 
ATOM   1850 C  CG  . ARG A 1 261 ? 104.201 136.111 97.783  1.00 79.60  ? 242 ARG A CG  1 
ATOM   1851 C  CD  . ARG A 1 261 ? 102.741 136.240 98.171  1.00 79.60  ? 242 ARG A CD  1 
ATOM   1852 N  NE  . ARG A 1 261 ? 102.111 134.937 98.343  1.00 79.60  ? 242 ARG A NE  1 
ATOM   1853 C  CZ  . ARG A 1 261 ? 101.699 134.453 99.507  1.00 79.60  ? 242 ARG A CZ  1 
ATOM   1854 N  NH1 . ARG A 1 261 ? 101.840 135.139 100.630 1.00 79.60  ? 242 ARG A NH1 1 
ATOM   1855 N  NH2 . ARG A 1 261 ? 101.134 133.250 99.547  1.00 79.60  ? 242 ARG A NH2 1 
ATOM   1856 N  N   . ASP A 1 262 ? 107.896 135.306 100.435 1.00 75.77  ? 243 ASP A N   1 
ATOM   1857 C  CA  . ASP A 1 262 ? 108.617 134.888 101.634 1.00 75.77  ? 243 ASP A CA  1 
ATOM   1858 C  C   . ASP A 1 262 ? 108.474 135.946 102.724 1.00 75.77  ? 243 ASP A C   1 
ATOM   1859 O  O   . ASP A 1 262 ? 109.454 136.385 103.327 1.00 75.77  ? 243 ASP A O   1 
ATOM   1860 C  CB  . ASP A 1 262 ? 110.086 134.612 101.318 1.00 75.77  ? 243 ASP A CB  1 
ATOM   1861 C  CG  . ASP A 1 262 ? 110.786 133.840 102.419 1.00 75.77  ? 243 ASP A CG  1 
ATOM   1862 O  OD1 . ASP A 1 262 ? 110.093 133.149 103.196 1.00 75.77  ? 243 ASP A OD1 1 
ATOM   1863 O  OD2 . ASP A 1 262 ? 112.027 133.926 102.511 1.00 75.77  ? 243 ASP A OD2 1 
ATOM   1864 N  N   . ASN A 1 263 ? 107.239 136.389 102.966 1.00 71.85  ? 244 ASN A N   1 
ATOM   1865 C  CA  . ASN A 1 263 ? 107.003 137.436 103.953 1.00 71.85  ? 244 ASN A CA  1 
ATOM   1866 C  C   . ASN A 1 263 ? 107.518 137.001 105.318 1.00 71.85  ? 244 ASN A C   1 
ATOM   1867 O  O   . ASN A 1 263 ? 107.350 135.849 105.723 1.00 71.85  ? 244 ASN A O   1 
ATOM   1868 C  CB  . ASN A 1 263 ? 105.511 137.747 104.046 1.00 71.85  ? 244 ASN A CB  1 
ATOM   1869 C  CG  . ASN A 1 263 ? 104.926 138.159 102.721 1.00 71.85  ? 244 ASN A CG  1 
ATOM   1870 O  OD1 . ASN A 1 263 ? 105.655 138.372 101.756 1.00 71.85  ? 244 ASN A OD1 1 
ATOM   1871 N  ND2 . ASN A 1 263 ? 103.605 138.269 102.662 1.00 71.85  ? 244 ASN A ND2 1 
ATOM   1872 N  N   . MET A 1 264 ? 108.153 137.927 106.033 1.00 67.79  ? 245 MET A N   1 
ATOM   1873 C  CA  . MET A 1 264 ? 108.755 137.596 107.321 1.00 67.79  ? 245 MET A CA  1 
ATOM   1874 C  C   . MET A 1 264 ? 108.300 138.607 108.366 1.00 67.79  ? 245 MET A C   1 
ATOM   1875 O  O   . MET A 1 264 ? 108.442 139.826 108.148 1.00 67.79  ? 245 MET A O   1 
ATOM   1876 C  CB  . MET A 1 264 ? 110.277 137.522 107.208 1.00 67.79  ? 245 MET A CB  1 
ATOM   1877 C  CG  . MET A 1 264 ? 110.710 136.163 106.668 1.00 67.79  ? 245 MET A CG  1 
ATOM   1878 S  SD  . MET A 1 264 ? 111.042 134.879 107.886 1.00 67.79  ? 245 MET A SD  1 
ATOM   1879 C  CE  . MET A 1 264 ? 112.474 135.545 108.706 1.00 67.79  ? 245 MET A CE  1 
ATOM   1880 N  N   . PRO A 1 265 ? 107.722 138.166 109.481 1.00 68.28  ? 246 PRO A N   1 
ATOM   1881 C  CA  . PRO A 1 265 ? 107.406 139.099 110.568 1.00 68.28  ? 246 PRO A CA  1 
ATOM   1882 C  C   . PRO A 1 265 ? 108.658 139.665 111.219 1.00 68.28  ? 246 PRO A C   1 
ATOM   1883 O  O   . PRO A 1 265 ? 109.717 139.033 111.243 1.00 68.28  ? 246 PRO A O   1 
ATOM   1884 C  CB  . PRO A 1 265 ? 106.616 138.236 111.558 1.00 68.28  ? 246 PRO A CB  1 
ATOM   1885 C  CG  . PRO A 1 265 ? 106.125 137.078 110.754 1.00 68.28  ? 246 PRO A CG  1 
ATOM   1886 C  CD  . PRO A 1 265 ? 107.191 136.820 109.740 1.00 68.28  ? 246 PRO A CD  1 
ATOM   1887 N  N   . PHE A 1 266 ? 108.522 140.877 111.753 1.00 69.98  ? 247 PHE A N   1 
ATOM   1888 C  CA  . PHE A 1 266 ? 109.616 141.552 112.439 1.00 69.98  ? 247 PHE A CA  1 
ATOM   1889 C  C   . PHE A 1 266 ? 109.030 142.588 113.386 1.00 69.98  ? 247 PHE A C   1 
ATOM   1890 O  O   . PHE A 1 266 ? 107.846 142.930 113.313 1.00 69.98  ? 247 PHE A O   1 
ATOM   1891 C  CB  . PHE A 1 266 ? 110.575 142.214 111.447 1.00 69.98  ? 247 PHE A CB  1 
ATOM   1892 C  CG  . PHE A 1 266 ? 110.099 143.547 110.944 1.00 69.98  ? 247 PHE A CG  1 
ATOM   1893 C  CD1 . PHE A 1 266 ? 109.164 143.623 109.928 1.00 69.98  ? 247 PHE A CD1 1 
ATOM   1894 C  CD2 . PHE A 1 266 ? 110.583 144.724 111.489 1.00 69.98  ? 247 PHE A CD2 1 
ATOM   1895 C  CE1 . PHE A 1 266 ? 108.723 144.845 109.466 1.00 69.98  ? 247 PHE A CE1 1 
ATOM   1896 C  CE2 . PHE A 1 266 ? 110.144 145.947 111.031 1.00 69.98  ? 247 PHE A CE2 1 
ATOM   1897 C  CZ  . PHE A 1 266 ? 109.213 146.007 110.018 1.00 69.98  ? 247 PHE A CZ  1 
ATOM   1898 N  N   . GLY A 1 267 ? 109.871 143.085 114.278 1.00 79.28  ? 248 GLY A N   1 
ATOM   1899 C  CA  . GLY A 1 267 ? 109.463 144.163 115.154 1.00 79.28  ? 248 GLY A CA  1 
ATOM   1900 C  C   . GLY A 1 267 ? 110.329 144.251 116.391 1.00 79.28  ? 248 GLY A C   1 
ATOM   1901 O  O   . GLY A 1 267 ? 111.218 143.433 116.626 1.00 79.28  ? 248 GLY A O   1 
ATOM   1902 N  N   . ASP A 1 268 ? 110.036 145.281 117.181 1.00 90.68  ? 249 ASP A N   1 
ATOM   1903 C  CA  . ASP A 1 268 ? 110.681 145.515 118.468 1.00 90.68  ? 249 ASP A CA  1 
ATOM   1904 C  C   . ASP A 1 268 ? 109.590 145.819 119.486 1.00 90.68  ? 249 ASP A C   1 
ATOM   1905 O  O   . ASP A 1 268 ? 108.868 146.829 119.335 1.00 90.68  ? 249 ASP A O   1 
ATOM   1906 C  CB  . ASP A 1 268 ? 111.690 146.664 118.379 1.00 90.68  ? 249 ASP A CB  1 
ATOM   1907 C  CG  . ASP A 1 268 ? 112.604 146.738 119.589 1.00 90.68  ? 249 ASP A CG  1 
ATOM   1908 O  OD1 . ASP A 1 268 ? 112.327 146.058 120.599 1.00 90.68  ? 249 ASP A OD1 1 
ATOM   1909 O  OD2 . ASP A 1 268 ? 113.604 147.484 119.528 1.00 90.68  ? 249 ASP A OD2 1 
ATOM   1910 N  N   . PRO A 1 269 ? 109.402 144.974 120.504 1.00 89.78  ? 250 PRO A N   1 
ATOM   1911 C  CA  . PRO A 1 269 ? 108.359 145.255 121.507 1.00 89.78  ? 250 PRO A CA  1 
ATOM   1912 C  C   . PRO A 1 269 ? 108.574 146.554 122.263 1.00 89.78  ? 250 PRO A C   1 
ATOM   1913 O  O   . PRO A 1 269 ? 107.598 147.242 122.589 1.00 89.78  ? 250 PRO A O   1 
ATOM   1914 C  CB  . PRO A 1 269 ? 108.441 144.042 122.445 1.00 89.78  ? 250 PRO A CB  1 
ATOM   1915 C  CG  . PRO A 1 269 ? 109.121 142.983 121.653 1.00 89.78  ? 250 PRO A CG  1 
ATOM   1916 C  CD  . PRO A 1 269 ? 110.083 143.695 120.759 1.00 89.78  ? 250 PRO A CD  1 
ATOM   1917 N  N   . GLY A 1 270 ? 109.829 146.912 122.545 1.00 93.26  ? 251 GLY A N   1 
ATOM   1918 C  CA  . GLY A 1 270 ? 110.092 148.077 123.377 1.00 93.26  ? 251 GLY A CA  1 
ATOM   1919 C  C   . GLY A 1 270 ? 109.559 149.366 122.784 1.00 93.26  ? 251 GLY A C   1 
ATOM   1920 O  O   . GLY A 1 270 ? 108.988 150.197 123.493 1.00 93.26  ? 251 GLY A O   1 
ATOM   1921 N  N   . LYS A 1 271 ? 109.735 149.551 121.480 1.00 94.18  ? 252 LYS A N   1 
ATOM   1922 C  CA  . LYS A 1 271 ? 109.182 150.704 120.787 1.00 94.18  ? 252 LYS A CA  1 
ATOM   1923 C  C   . LYS A 1 271 ? 107.762 150.460 120.297 1.00 94.18  ? 252 LYS A C   1 
ATOM   1924 O  O   . LYS A 1 271 ? 107.171 151.353 119.681 1.00 94.18  ? 252 LYS A O   1 
ATOM   1925 C  CB  . LYS A 1 271 ? 110.081 151.089 119.608 1.00 94.18  ? 252 LYS A CB  1 
ATOM   1926 C  CG  . LYS A 1 271 ? 111.549 150.773 119.834 1.00 94.18  ? 252 LYS A CG  1 
ATOM   1927 C  CD  . LYS A 1 271 ? 112.428 151.431 118.785 1.00 94.18  ? 252 LYS A CD  1 
ATOM   1928 C  CE  . LYS A 1 271 ? 113.895 151.118 119.025 1.00 94.18  ? 252 LYS A CE  1 
ATOM   1929 N  NZ  . LYS A 1 271 ? 114.074 149.864 119.809 1.00 94.18  ? 252 LYS A NZ  1 
ATOM   1930 N  N   . GLY A 1 272 ? 107.207 149.280 120.559 1.00 88.91  ? 253 GLY A N   1 
ATOM   1931 C  CA  . GLY A 1 272 ? 105.872 148.960 120.096 1.00 88.91  ? 253 GLY A CA  1 
ATOM   1932 C  C   . GLY A 1 272 ? 105.763 148.809 118.598 1.00 88.91  ? 253 GLY A C   1 
ATOM   1933 O  O   . GLY A 1 272 ? 104.684 149.026 118.038 1.00 88.91  ? 253 GLY A O   1 
ATOM   1934 N  N   . GLU A 1 273 ? 106.852 148.442 117.929 1.00 85.95  ? 254 GLU A N   1 
ATOM   1935 C  CA  . GLU A 1 273 ? 106.880 148.356 116.476 1.00 85.95  ? 254 GLU A CA  1 
ATOM   1936 C  C   . GLU A 1 273 ? 106.628 146.915 116.054 1.00 85.95  ? 254 GLU A C   1 
ATOM   1937 O  O   . GLU A 1 273 ? 107.356 146.009 116.468 1.00 85.95  ? 254 GLU A O   1 
ATOM   1938 C  CB  . GLU A 1 273 ? 108.216 148.853 115.925 1.00 85.95  ? 254 GLU A CB  1 
ATOM   1939 C  CG  . GLU A 1 273 ? 108.173 149.235 114.457 1.00 85.95  ? 254 GLU A CG  1 
ATOM   1940 C  CD  . GLU A 1 273 ? 109.218 150.270 114.094 1.00 85.95  ? 254 GLU A CD  1 
ATOM   1941 O  OE1 . GLU A 1 273 ? 110.418 149.926 114.081 1.00 85.95  ? 254 GLU A OE1 1 
ATOM   1942 O  OE2 . GLU A 1 273 ? 108.838 151.428 113.820 1.00 85.95  ? 254 GLU A OE2 1 
ATOM   1943 N  N   . PHE A 1 274 ? 105.600 146.708 115.238 1.00 76.83  ? 255 PHE A N   1 
ATOM   1944 C  CA  . PHE A 1 274 ? 105.251 145.394 114.721 1.00 76.83  ? 255 PHE A CA  1 
ATOM   1945 C  C   . PHE A 1 274 ? 105.042 145.512 113.221 1.00 76.83  ? 255 PHE A C   1 
ATOM   1946 O  O   . PHE A 1 274 ? 104.375 146.441 112.757 1.00 76.83  ? 255 PHE A O   1 
ATOM   1947 C  CB  . PHE A 1 274 ? 103.982 144.843 115.384 1.00 76.83  ? 255 PHE A CB  1 
ATOM   1948 C  CG  . PHE A 1 274 ? 104.052 144.784 116.884 1.00 76.83  ? 255 PHE A CG  1 
ATOM   1949 C  CD1 . PHE A 1 274 ? 103.806 145.911 117.650 1.00 76.83  ? 255 PHE A CD1 1 
ATOM   1950 C  CD2 . PHE A 1 274 ? 104.354 143.598 117.529 1.00 76.83  ? 255 PHE A CD2 1 
ATOM   1951 C  CE1 . PHE A 1 274 ? 103.868 145.858 119.027 1.00 76.83  ? 255 PHE A CE1 1 
ATOM   1952 C  CE2 . PHE A 1 274 ? 104.417 143.538 118.906 1.00 76.83  ? 255 PHE A CE2 1 
ATOM   1953 C  CZ  . PHE A 1 274 ? 104.174 144.669 119.656 1.00 76.83  ? 255 PHE A CZ  1 
ATOM   1954 N  N   . GLY A 1 275 ? 105.589 144.569 112.458 1.00 72.87  ? 256 GLY A N   1 
ATOM   1955 C  CA  . GLY A 1 275 ? 105.431 144.682 111.022 1.00 72.87  ? 256 GLY A CA  1 
ATOM   1956 C  C   . GLY A 1 275 ? 105.761 143.400 110.296 1.00 72.87  ? 256 GLY A C   1 
ATOM   1957 O  O   . GLY A 1 275 ? 106.221 142.415 110.879 1.00 72.87  ? 256 GLY A O   1 
ATOM   1958 N  N   . THR A 1 276 ? 105.519 143.442 108.991 1.00 68.75  ? 257 THR A N   1 
ATOM   1959 C  CA  . THR A 1 276 ? 105.787 142.328 108.093 1.00 68.75  ? 257 THR A CA  1 
ATOM   1960 C  C   . THR A 1 276 ? 106.582 142.833 106.899 1.00 68.75  ? 257 THR A C   1 
ATOM   1961 O  O   . THR A 1 276 ? 106.231 143.856 106.301 1.00 68.75  ? 257 THR A O   1 
ATOM   1962 C  CB  . THR A 1 276 ? 104.485 141.670 107.624 1.00 68.75  ? 257 THR A CB  1 
ATOM   1963 O  OG1 . THR A 1 276 ? 103.762 141.179 108.759 1.00 68.75  ? 257 THR A OG1 1 
ATOM   1964 C  CG2 . THR A 1 276 ? 104.779 140.514 106.682 1.00 68.75  ? 257 THR A CG2 1 
ATOM   1965 N  N   . TYR A 1 277 ? 107.653 142.124 106.560 1.00 67.00  ? 258 TYR A N   1 
ATOM   1966 C  CA  . TYR A 1 277 ? 108.459 142.437 105.389 1.00 67.00  ? 258 TYR A CA  1 
ATOM   1967 C  C   . TYR A 1 277 ? 108.004 141.520 104.261 1.00 67.00  ? 258 TYR A C   1 
ATOM   1968 O  O   . TYR A 1 277 ? 108.244 140.307 104.301 1.00 67.00  ? 258 TYR A O   1 
ATOM   1969 C  CB  . TYR A 1 277 ? 109.947 142.270 105.686 1.00 67.00  ? 258 TYR A CB  1 
ATOM   1970 C  CG  . TYR A 1 277 ? 110.832 143.222 104.915 1.00 67.00  ? 258 TYR A CG  1 
ATOM   1971 C  CD1 . TYR A 1 277 ? 111.295 142.901 103.647 1.00 67.00  ? 258 TYR A CD1 1 
ATOM   1972 C  CD2 . TYR A 1 277 ? 111.197 144.448 105.453 1.00 67.00  ? 258 TYR A CD2 1 
ATOM   1973 C  CE1 . TYR A 1 277 ? 112.103 143.771 102.941 1.00 67.00  ? 258 TYR A CE1 1 
ATOM   1974 C  CE2 . TYR A 1 277 ? 112.002 145.324 104.755 1.00 67.00  ? 258 TYR A CE2 1 
ATOM   1975 C  CZ  . TYR A 1 277 ? 112.452 144.981 103.500 1.00 67.00  ? 258 TYR A CZ  1 
ATOM   1976 O  OH  . TYR A 1 277 ? 113.256 145.852 102.802 1.00 67.00  ? 258 TYR A OH  1 
ATOM   1977 N  N   . PHE A 1 278 ? 107.317 142.097 103.278 1.00 68.20  ? 259 PHE A N   1 
ATOM   1978 C  CA  . PHE A 1 278 ? 106.840 141.364 102.116 1.00 68.20  ? 259 PHE A CA  1 
ATOM   1979 C  C   . PHE A 1 278 ? 107.923 141.348 101.049 1.00 68.20  ? 259 PHE A C   1 
ATOM   1980 O  O   . PHE A 1 278 ? 108.480 142.395 100.706 1.00 68.20  ? 259 PHE A O   1 
ATOM   1981 C  CB  . PHE A 1 278 ? 105.565 142.010 101.568 1.00 68.20  ? 259 PHE A CB  1 
ATOM   1982 C  CG  . PHE A 1 278 ? 105.259 141.649 100.139 1.00 68.20  ? 259 PHE A CG  1 
ATOM   1983 C  CD1 . PHE A 1 278 ? 104.676 140.436 99.822  1.00 68.20  ? 259 PHE A CD1 1 
ATOM   1984 C  CD2 . PHE A 1 278 ? 105.543 142.535 99.114  1.00 68.20  ? 259 PHE A CD2 1 
ATOM   1985 C  CE1 . PHE A 1 278 ? 104.392 140.109 98.510  1.00 68.20  ? 259 PHE A CE1 1 
ATOM   1986 C  CE2 . PHE A 1 278 ? 105.262 142.213 97.801  1.00 68.20  ? 259 PHE A CE2 1 
ATOM   1987 C  CZ  . PHE A 1 278 ? 104.685 140.998 97.500  1.00 68.20  ? 259 PHE A CZ  1 
ATOM   1988 N  N   . ILE A 1 279 ? 108.224 140.162 100.532 1.00 69.21  ? 260 ILE A N   1 
ATOM   1989 C  CA  . ILE A 1 279 ? 109.190 139.997 99.456  1.00 69.21  ? 260 ILE A CA  1 
ATOM   1990 C  C   . ILE A 1 279 ? 108.587 139.066 98.414  1.00 69.21  ? 260 ILE A C   1 
ATOM   1991 O  O   . ILE A 1 279 ? 108.021 138.022 98.757  1.00 69.21  ? 260 ILE A O   1 
ATOM   1992 C  CB  . ILE A 1 279 ? 110.543 139.470 99.976  1.00 69.21  ? 260 ILE A CB  1 
ATOM   1993 C  CG1 . ILE A 1 279 ? 111.589 139.475 98.861  1.00 69.21  ? 260 ILE A CG1 1 
ATOM   1994 C  CG2 . ILE A 1 279 ? 110.402 138.099 100.616 1.00 69.21  ? 260 ILE A CG2 1 
ATOM   1995 C  CD1 . ILE A 1 279 ? 113.009 139.574 99.363  1.00 69.21  ? 260 ILE A CD1 1 
ATOM   1996 N  N   . GLY A 1 280 ? 108.674 139.460 97.148  1.00 71.53  ? 261 GLY A N   1 
ATOM   1997 C  CA  . GLY A 1 280 ? 108.077 138.672 96.090  1.00 71.53  ? 261 GLY A CA  1 
ATOM   1998 C  C   . GLY A 1 280 ? 108.976 138.508 94.885  1.00 71.53  ? 261 GLY A C   1 
ATOM   1999 O  O   . GLY A 1 280 ? 109.460 139.497 94.327  1.00 71.53  ? 261 GLY A O   1 
ATOM   2000 N  N   . TYR A 1 281 ? 109.205 137.263 94.479  1.00 74.67  ? 262 TYR A N   1 
ATOM   2001 C  CA  . TYR A 1 281 ? 110.040 136.947 93.329  1.00 74.67  ? 262 TYR A CA  1 
ATOM   2002 C  C   . TYR A 1 281 ? 109.157 136.585 92.144  1.00 74.67  ? 262 TYR A C   1 
ATOM   2003 O  O   . TYR A 1 281 ? 108.103 135.964 92.310  1.00 74.67  ? 262 TYR A O   1 
ATOM   2004 C  CB  . TYR A 1 281 ? 110.986 135.787 93.641  1.00 74.67  ? 262 TYR A CB  1 
ATOM   2005 C  CG  . TYR A 1 281 ? 111.967 136.066 94.755  1.00 74.67  ? 262 TYR A CG  1 
ATOM   2006 C  CD1 . TYR A 1 281 ? 113.019 136.952 94.577  1.00 74.67  ? 262 TYR A CD1 1 
ATOM   2007 C  CD2 . TYR A 1 281 ? 111.843 135.436 95.985  1.00 74.67  ? 262 TYR A CD2 1 
ATOM   2008 C  CE1 . TYR A 1 281 ? 113.919 137.204 95.594  1.00 74.67  ? 262 TYR A CE1 1 
ATOM   2009 C  CE2 . TYR A 1 281 ? 112.736 135.683 97.007  1.00 74.67  ? 262 TYR A CE2 1 
ATOM   2010 C  CZ  . TYR A 1 281 ? 113.771 136.568 96.806  1.00 74.67  ? 262 TYR A CZ  1 
ATOM   2011 O  OH  . TYR A 1 281 ? 114.663 136.816 97.823  1.00 74.67  ? 262 TYR A OH  1 
ATOM   2012 N  N   . SER A 1 282 ? 109.588 136.974 90.949  1.00 79.24  ? 263 SER A N   1 
ATOM   2013 C  CA  . SER A 1 282 ? 108.811 136.680 89.754  1.00 79.24  ? 263 SER A CA  1 
ATOM   2014 C  C   . SER A 1 282 ? 109.725 136.687 88.539  1.00 79.24  ? 263 SER A C   1 
ATOM   2015 O  O   . SER A 1 282 ? 110.833 137.227 88.570  1.00 79.24  ? 263 SER A O   1 
ATOM   2016 C  CB  . SER A 1 282 ? 107.669 137.684 89.570  1.00 79.24  ? 263 SER A CB  1 
ATOM   2017 O  OG  . SER A 1 282 ? 106.901 137.372 88.421  1.00 79.24  ? 263 SER A OG  1 
ATOM   2018 N  N   . ARG A 1 283 ? 109.253 136.041 87.472  1.00 83.54  ? 264 ARG A N   1 
ATOM   2019 C  CA  . ARG A 1 283 ? 109.876 136.213 86.168  1.00 83.54  ? 264 ARG A CA  1 
ATOM   2020 C  C   . ARG A 1 283 ? 109.395 137.478 85.475  1.00 83.54  ? 264 ARG A C   1 
ATOM   2021 O  O   . ARG A 1 283 ? 110.025 137.921 84.509  1.00 83.54  ? 264 ARG A O   1 
ATOM   2022 C  CB  . ARG A 1 283 ? 109.599 134.996 85.283  1.00 83.54  ? 264 ARG A CB  1 
ATOM   2023 C  CG  . ARG A 1 283 ? 108.204 134.972 84.682  1.00 83.54  ? 264 ARG A CG  1 
ATOM   2024 C  CD  . ARG A 1 283 ? 107.880 133.610 84.091  1.00 83.54  ? 264 ARG A CD  1 
ATOM   2025 N  NE  . ARG A 1 283 ? 108.783 133.251 83.006  1.00 83.54  ? 264 ARG A NE  1 
ATOM   2026 C  CZ  . ARG A 1 283 ? 109.109 132.007 82.684  1.00 83.54  ? 264 ARG A CZ  1 
ATOM   2027 N  NH1 . ARG A 1 283 ? 108.624 130.971 83.349  1.00 83.54  ? 264 ARG A NH1 1 
ATOM   2028 N  NH2 . ARG A 1 283 ? 109.941 131.796 81.669  1.00 83.54  ? 264 ARG A NH2 1 
ATOM   2029 N  N   . LYS A 1 284 ? 108.296 138.061 85.948  1.00 87.35  ? 265 LYS A N   1 
ATOM   2030 C  CA  . LYS A 1 284 ? 107.745 139.299 85.417  1.00 87.35  ? 265 LYS A CA  1 
ATOM   2031 C  C   . LYS A 1 284 ? 107.171 140.133 86.555  1.00 87.35  ? 265 LYS A C   1 
ATOM   2032 O  O   . LYS A 1 284 ? 106.224 139.701 87.224  1.00 87.35  ? 265 LYS A O   1 
ATOM   2033 C  CB  . LYS A 1 284 ? 106.664 139.008 84.375  1.00 87.35  ? 265 LYS A CB  1 
ATOM   2034 C  CG  . LYS A 1 284 ? 107.198 138.632 83.002  1.00 87.35  ? 265 LYS A CG  1 
ATOM   2035 C  CD  . LYS A 1 284 ? 106.073 138.362 82.009  1.00 87.35  ? 265 LYS A CD  1 
ATOM   2036 C  CE  . LYS A 1 284 ? 104.892 139.304 82.203  1.00 87.35  ? 265 LYS A CE  1 
ATOM   2037 N  NZ  . LYS A 1 284 ? 105.266 140.734 82.016  1.00 87.35  ? 265 LYS A NZ  1 
ATOM   2038 N  N   . PRO A 1 285 ? 107.713 141.328 86.811  1.00 86.92  ? 266 PRO A N   1 
ATOM   2039 C  CA  . PRO A 1 285 ? 107.160 142.177 87.877  1.00 86.92  ? 266 PRO A CA  1 
ATOM   2040 C  C   . PRO A 1 285 ? 105.766 142.698 87.577  1.00 86.92  ? 266 PRO A C   1 
ATOM   2041 O  O   . PRO A 1 285 ? 105.131 143.265 88.477  1.00 86.92  ? 266 PRO A O   1 
ATOM   2042 C  CB  . PRO A 1 285 ? 108.172 143.323 87.972  1.00 86.92  ? 266 PRO A CB  1 
ATOM   2043 C  CG  . PRO A 1 285 ? 108.790 143.382 86.619  1.00 86.92  ? 266 PRO A CG  1 
ATOM   2044 C  CD  . PRO A 1 285 ? 108.859 141.961 86.138  1.00 86.92  ? 266 PRO A CD  1 
ATOM   2045 N  N   . GLU A 1 286 ? 105.282 142.538 86.342  1.00 92.19  ? 267 GLU A N   1 
ATOM   2046 C  CA  . GLU A 1 286 ? 103.943 142.998 85.994  1.00 92.19  ? 267 GLU A CA  1 
ATOM   2047 C  C   . GLU A 1 286 ? 102.894 142.295 86.848  1.00 92.19  ? 267 GLU A C   1 
ATOM   2048 O  O   . GLU A 1 286 ? 101.914 142.913 87.271  1.00 92.19  ? 267 GLU A O   1 
ATOM   2049 C  CB  . GLU A 1 286 ? 103.704 142.753 84.501  1.00 92.19  ? 267 GLU A CB  1 
ATOM   2050 C  CG  . GLU A 1 286 ? 102.264 142.752 83.965  1.00 92.19  ? 267 GLU A CG  1 
ATOM   2051 C  CD  . GLU A 1 286 ? 101.439 143.960 84.382  1.00 92.19  ? 267 GLU A CD  1 
ATOM   2052 O  OE1 . GLU A 1 286 ? 101.551 145.005 83.710  1.00 92.19  ? 267 GLU A OE1 1 
ATOM   2053 O  OE2 . GLU A 1 286 ? 100.622 143.855 85.318  1.00 92.19  ? 267 GLU A OE2 1 
ATOM   2054 N  N   . ARG A 1 287 ? 103.114 141.017 87.162  1.00 93.65  ? 268 ARG A N   1 
ATOM   2055 C  CA  . ARG A 1 287 ? 102.168 140.286 88.000  1.00 93.65  ? 268 ARG A CA  1 
ATOM   2056 C  C   . ARG A 1 287 ? 102.071 140.903 89.391  1.00 93.65  ? 268 ARG A C   1 
ATOM   2057 O  O   . ARG A 1 287 ? 100.971 141.135 89.908  1.00 93.65  ? 268 ARG A O   1 
ATOM   2058 C  CB  . ARG A 1 287 ? 102.584 138.818 88.089  1.00 93.65  ? 268 ARG A CB  1 
ATOM   2059 C  CG  . ARG A 1 287 ? 102.668 138.121 86.744  1.00 93.65  ? 268 ARG A CG  1 
ATOM   2060 C  CD  . ARG A 1 287 ? 103.224 136.715 86.882  1.00 93.65  ? 268 ARG A CD  1 
ATOM   2061 N  NE  . ARG A 1 287 ? 103.350 136.052 85.590  1.00 93.65  ? 268 ARG A NE  1 
ATOM   2062 C  CZ  . ARG A 1 287 ? 103.848 134.836 85.416  1.00 93.65  ? 268 ARG A CZ  1 
ATOM   2063 N  NH1 . ARG A 1 287 ? 104.284 134.115 86.436  1.00 93.65  ? 268 ARG A NH1 1 
ATOM   2064 N  NH2 . ARG A 1 287 ? 103.912 134.330 84.188  1.00 93.65  ? 268 ARG A NH2 1 
ATOM   2065 N  N   . ILE A 1 288 ? 103.220 141.182 90.010  1.00 83.94  ? 269 ILE A N   1 
ATOM   2066 C  CA  . ILE A 1 288 ? 103.217 141.755 91.353  1.00 83.94  ? 269 ILE A CA  1 
ATOM   2067 C  C   . ILE A 1 288 ? 102.649 143.169 91.335  1.00 83.94  ? 269 ILE A C   1 
ATOM   2068 O  O   . ILE A 1 288 ? 101.943 143.578 92.264  1.00 83.94  ? 269 ILE A O   1 
ATOM   2069 C  CB  . ILE A 1 288 ? 104.632 141.718 91.954  1.00 83.94  ? 269 ILE A CB  1 
ATOM   2070 C  CG1 . ILE A 1 288 ? 105.236 140.323 91.801  1.00 83.94  ? 269 ILE A CG1 1 
ATOM   2071 C  CG2 . ILE A 1 288 ? 104.598 142.110 93.417  1.00 83.94  ? 269 ILE A CG2 1 
ATOM   2072 C  CD1 . ILE A 1 288 ? 106.690 140.239 92.201  1.00 83.94  ? 269 ILE A CD1 1 
ATOM   2073 N  N   . GLU A 1 289 ? 102.944 143.938 90.284  1.00 89.28  ? 270 GLU A N   1 
ATOM   2074 C  CA  . GLU A 1 289 ? 102.376 145.279 90.182  1.00 89.28  ? 270 GLU A CA  1 
ATOM   2075 C  C   . GLU A 1 289 ? 100.860 145.230 90.025  1.00 89.28  ? 270 GLU A C   1 
ATOM   2076 O  O   . GLU A 1 289 ? 100.143 146.054 90.603  1.00 89.28  ? 270 GLU A O   1 
ATOM   2077 C  CB  . GLU A 1 289 ? 103.020 146.031 89.019  1.00 89.28  ? 270 GLU A CB  1 
ATOM   2078 C  CG  . GLU A 1 289 ? 104.493 146.330 89.232  1.00 89.28  ? 270 GLU A CG  1 
ATOM   2079 C  CD  . GLU A 1 289 ? 105.109 147.069 88.063  1.00 89.28  ? 270 GLU A CD  1 
ATOM   2080 O  OE1 . GLU A 1 289 ? 104.932 146.620 86.912  1.00 89.28  ? 270 GLU A OE1 1 
ATOM   2081 O  OE2 . GLU A 1 289 ? 105.773 148.099 88.299  1.00 89.28  ? 270 GLU A OE2 1 
ATOM   2082 N  N   . ARG A 1 290 ? 100.354 144.267 89.251  1.00 90.91  ? 271 ARG A N   1 
ATOM   2083 C  CA  . ARG A 1 290 ? 98.912  144.097 89.109  1.00 90.91  ? 271 ARG A CA  1 
ATOM   2084 C  C   . ARG A 1 290 ? 98.274  143.706 90.433  1.00 90.91  ? 271 ARG A C   1 
ATOM   2085 O  O   . ARG A 1 290 ? 97.194  144.195 90.785  1.00 90.91  ? 271 ARG A O   1 
ATOM   2086 C  CB  . ARG A 1 290 ? 98.612  143.040 88.049  1.00 90.91  ? 271 ARG A CB  1 
ATOM   2087 C  CG  . ARG A 1 290 ? 97.280  143.227 87.346  1.00 90.91  ? 271 ARG A CG  1 
ATOM   2088 C  CD  . ARG A 1 290 ? 96.678  141.885 86.956  1.00 90.91  ? 271 ARG A CD  1 
ATOM   2089 N  NE  . ARG A 1 290 ? 97.455  141.199 85.931  1.00 90.91  ? 271 ARG A NE  1 
ATOM   2090 C  CZ  . ARG A 1 290 ? 97.388  141.461 84.633  1.00 90.91  ? 271 ARG A CZ  1 
ATOM   2091 N  NH1 . ARG A 1 290 ? 96.579  142.392 84.156  1.00 90.91  ? 271 ARG A NH1 1 
ATOM   2092 N  NH2 . ARG A 1 290 ? 98.151  140.768 83.791  1.00 90.91  ? 271 ARG A NH2 1 
ATOM   2093 N  N   . MET A 1 291 ? 98.927  142.814 91.176  1.00 86.03  ? 272 MET A N   1 
ATOM   2094 C  CA  . MET A 1 291 ? 98.419  142.424 92.486  1.00 86.03  ? 272 MET A CA  1 
ATOM   2095 C  C   . MET A 1 291 ? 98.383  143.615 93.437  1.00 86.03  ? 272 MET A C   1 
ATOM   2096 O  O   . MET A 1 291 ? 97.412  143.799 94.183  1.00 86.03  ? 272 MET A O   1 
ATOM   2097 C  CB  . MET A 1 291 ? 99.308  141.315 93.047  1.00 86.03  ? 272 MET A CB  1 
ATOM   2098 C  CG  . MET A 1 291 ? 98.968  139.925 92.544  1.00 86.03  ? 272 MET A CG  1 
ATOM   2099 S  SD  . MET A 1 291 ? 100.358 138.801 92.783  1.00 86.03  ? 272 MET A SD  1 
ATOM   2100 C  CE  . MET A 1 291 ? 99.600  137.211 92.480  1.00 86.03  ? 272 MET A CE  1 
ATOM   2101 N  N   . LEU A 1 292 ? 99.429  144.445 93.409  1.00 86.06  ? 273 LEU A N   1 
ATOM   2102 C  CA  . LEU A 1 292 ? 99.460  145.642 94.242  1.00 86.06  ? 273 LEU A CA  1 
ATOM   2103 C  C   . LEU A 1 292 ? 98.366  146.624 93.843  1.00 86.06  ? 273 LEU A C   1 
ATOM   2104 O  O   . LEU A 1 292 ? 97.738  147.250 94.704  1.00 86.06  ? 273 LEU A O   1 
ATOM   2105 C  CB  . LEU A 1 292 ? 100.835 146.302 94.158  1.00 86.06  ? 273 LEU A CB  1 
ATOM   2106 C  CG  . LEU A 1 292 ? 101.940 145.618 94.961  1.00 86.06  ? 273 LEU A CG  1 
ATOM   2107 C  CD1 . LEU A 1 292 ? 103.288 146.252 94.668  1.00 86.06  ? 273 LEU A CD1 1 
ATOM   2108 C  CD2 . LEU A 1 292 ? 101.618 145.687 96.437  1.00 86.06  ? 273 LEU A CD2 1 
ATOM   2109 N  N   . GLU A 1 293 ? 98.135  146.783 92.538  1.00 93.21  ? 274 GLU A N   1 
ATOM   2110 C  CA  . GLU A 1 293 ? 97.069  147.662 92.071  1.00 93.21  ? 274 GLU A CA  1 
ATOM   2111 C  C   . GLU A 1 293 ? 95.705  147.163 92.524  1.00 93.21  ? 274 GLU A C   1 
ATOM   2112 O  O   . GLU A 1 293 ? 94.847  147.956 92.928  1.00 93.21  ? 274 GLU A O   1 
ATOM   2113 C  CB  . GLU A 1 293 ? 97.119  147.779 90.549  1.00 93.21  ? 274 GLU A CB  1 
ATOM   2114 C  CG  . GLU A 1 293 ? 98.263  148.640 90.037  1.00 93.21  ? 274 GLU A CG  1 
ATOM   2115 C  CD  . GLU A 1 293 ? 98.302  148.720 88.526  1.00 93.21  ? 274 GLU A CD  1 
ATOM   2116 O  OE1 . GLU A 1 293 ? 97.449  148.081 87.876  1.00 93.21  ? 274 GLU A OE1 1 
ATOM   2117 O  OE2 . GLU A 1 293 ? 99.186  149.421 87.989  1.00 93.21  ? 274 GLU A OE2 1 
ATOM   2118 N  N   . ASN A 1 294 ? 95.483  145.849 92.459  1.00 89.86  ? 275 ASN A N   1 
ATOM   2119 C  CA  . ASN A 1 294 ? 94.214  145.297 92.920  1.00 89.86  ? 275 ASN A CA  1 
ATOM   2120 C  C   . ASN A 1 294 ? 94.040  145.506 94.418  1.00 89.86  ? 275 ASN A C   1 
ATOM   2121 O  O   . ASN A 1 294 ? 92.939  145.822 94.885  1.00 89.86  ? 275 ASN A O   1 
ATOM   2122 C  CB  . ASN A 1 294 ? 94.123  143.812 92.568  1.00 89.86  ? 275 ASN A CB  1 
ATOM   2123 C  CG  . ASN A 1 294 ? 93.786  143.580 91.109  1.00 89.86  ? 275 ASN A CG  1 
ATOM   2124 O  OD1 . ASN A 1 294 ? 93.401  144.505 90.395  1.00 89.86  ? 275 ASN A OD1 1 
ATOM   2125 N  ND2 . ASN A 1 294 ? 93.919  142.337 90.661  1.00 89.86  ? 275 ASN A ND2 1 
ATOM   2126 N  N   . MET A 1 295 ? 95.113  145.327 95.191  1.00 87.05  ? 276 MET A N   1 
ATOM   2127 C  CA  . MET A 1 295 ? 95.001  145.472 96.639  1.00 87.05  ? 276 MET A CA  1 
ATOM   2128 C  C   . MET A 1 295 ? 94.775  146.925 97.046  1.00 87.05  ? 276 MET A C   1 
ATOM   2129 O  O   . MET A 1 295 ? 93.941  147.206 97.915  1.00 87.05  ? 276 MET A O   1 
ATOM   2130 C  CB  . MET A 1 295 ? 96.248  144.915 97.323  1.00 87.05  ? 276 MET A CB  1 
ATOM   2131 C  CG  . MET A 1 295 ? 96.303  143.400 97.369  1.00 87.05  ? 276 MET A CG  1 
ATOM   2132 S  SD  . MET A 1 295 ? 97.735  142.791 98.275  1.00 87.05  ? 276 MET A SD  1 
ATOM   2133 C  CE  . MET A 1 295 ? 97.858  144.015 99.575  1.00 87.05  ? 276 MET A CE  1 
ATOM   2134 N  N   . PHE A 1 296 ? 95.502  147.862 96.436  1.00 87.68  ? 277 PHE A N   1 
ATOM   2135 C  CA  . PHE A 1 296 ? 95.440  149.264 96.844  1.00 87.68  ? 277 PHE A CA  1 
ATOM   2136 C  C   . PHE A 1 296 ? 94.321  150.032 96.143  1.00 87.68  ? 277 PHE A C   1 
ATOM   2137 O  O   . PHE A 1 296 ? 93.463  150.628 96.803  1.00 87.68  ? 277 PHE A O   1 
ATOM   2138 C  CB  . PHE A 1 296 ? 96.790  149.942 96.586  1.00 87.68  ? 277 PHE A CB  1 
ATOM   2139 C  CG  . PHE A 1 296 ? 97.828  149.643 97.627  1.00 87.68  ? 277 PHE A CG  1 
ATOM   2140 C  CD1 . PHE A 1 296 ? 98.499  148.432 97.628  1.00 87.68  ? 277 PHE A CD1 1 
ATOM   2141 C  CD2 . PHE A 1 296 ? 98.136  150.575 98.603  1.00 87.68  ? 277 PHE A CD2 1 
ATOM   2142 C  CE1 . PHE A 1 296 ? 99.456  148.156 98.585  1.00 87.68  ? 277 PHE A CE1 1 
ATOM   2143 C  CE2 . PHE A 1 296 ? 99.092  150.304 99.562  1.00 87.68  ? 277 PHE A CE2 1 
ATOM   2144 C  CZ  . PHE A 1 296 ? 99.752  149.093 99.553  1.00 87.68  ? 277 PHE A CZ  1 
ATOM   2145 N  N   . ILE A 1 297 ? 94.319  150.033 94.809  1.00 93.73  ? 278 ILE A N   1 
ATOM   2146 C  CA  . ILE A 1 297 ? 93.288  150.765 94.079  1.00 93.73  ? 278 ILE A CA  1 
ATOM   2147 C  C   . ILE A 1 297 ? 91.941  150.068 94.213  1.00 93.73  ? 278 ILE A C   1 
ATOM   2148 O  O   . ILE A 1 297 ? 90.912  150.715 94.445  1.00 93.73  ? 278 ILE A O   1 
ATOM   2149 C  CB  . ILE A 1 297 ? 93.696  150.937 92.604  1.00 93.73  ? 278 ILE A CB  1 
ATOM   2150 C  CG1 . ILE A 1 297 ? 94.876  151.903 92.486  1.00 93.73  ? 278 ILE A CG1 1 
ATOM   2151 C  CG2 . ILE A 1 297 ? 92.522  151.434 91.777  1.00 93.73  ? 278 ILE A CG2 1 
ATOM   2152 C  CD1 . ILE A 1 297 ? 95.561  151.864 91.139  1.00 93.73  ? 278 ILE A CD1 1 
ATOM   2153 N  N   . GLY A 1 298 ? 91.924  148.754 94.080  1.00 94.59  ? 279 GLY A N   1 
ATOM   2154 C  CA  . GLY A 1 298 ? 90.692  147.992 94.187  1.00 94.59  ? 279 GLY A CA  1 
ATOM   2155 C  C   . GLY A 1 298 ? 90.279  147.431 92.839  1.00 94.59  ? 279 GLY A C   1 
ATOM   2156 O  O   . GLY A 1 298 ? 90.445  148.074 91.795  1.00 94.59  ? 279 GLY A O   1 
ATOM   2157 N  N   . ASN A 1 299 ? 89.730  146.220 92.860  1.00 95.45  ? 280 ASN A N   1 
ATOM   2158 C  CA  . ASN A 1 299 ? 89.239  145.552 91.656  1.00 95.45  ? 280 ASN A CA  1 
ATOM   2159 C  C   . ASN A 1 299 ? 87.825  145.061 91.940  1.00 95.45  ? 280 ASN A C   1 
ATOM   2160 O  O   . ASN A 1 299 ? 87.647  144.009 92.579  1.00 95.45  ? 280 ASN A O   1 
ATOM   2161 C  CB  . ASN A 1 299 ? 90.157  144.406 91.246  1.00 95.45  ? 280 ASN A CB  1 
ATOM   2162 C  CG  . ASN A 1 299 ? 89.446  143.350 90.422  1.00 95.45  ? 280 ASN A CG  1 
ATOM   2163 O  OD1 . ASN A 1 299 ? 88.983  143.619 89.314  1.00 95.45  ? 280 ASN A OD1 1 
ATOM   2164 N  ND2 . ASN A 1 299 ? 89.354  142.141 90.962  1.00 95.45  ? 280 ASN A ND2 1 
ATOM   2165 N  N   . PRO A 1 300 ? 86.791  145.802 91.517  1.00 98.60  ? 281 PRO A N   1 
ATOM   2166 C  CA  . PRO A 1 300 ? 86.818  147.092 90.807  1.00 98.60  ? 281 PRO A CA  1 
ATOM   2167 C  C   . PRO A 1 300 ? 87.256  148.228 91.728  1.00 98.60  ? 281 PRO A C   1 
ATOM   2168 O  O   . PRO A 1 300 ? 87.317  148.024 92.937  1.00 98.60  ? 281 PRO A O   1 
ATOM   2169 C  CB  . PRO A 1 300 ? 85.365  147.247 90.336  1.00 98.60  ? 281 PRO A CB  1 
ATOM   2170 C  CG  . PRO A 1 300 ? 84.571  146.544 91.390  1.00 98.60  ? 281 PRO A CG  1 
ATOM   2171 C  CD  . PRO A 1 300 ? 85.410  145.350 91.764  1.00 98.60  ? 281 PRO A CD  1 
ATOM   2172 N  N   . PRO A 1 301 ? 87.580  149.409 91.196  1.00 98.47  ? 282 PRO A N   1 
ATOM   2173 C  CA  . PRO A 1 301 ? 88.073  150.494 92.055  1.00 98.47  ? 282 PRO A CA  1 
ATOM   2174 C  C   . PRO A 1 301 ? 87.101  150.816 93.180  1.00 98.47  ? 282 PRO A C   1 
ATOM   2175 O  O   . PRO A 1 301 ? 85.884  150.854 92.987  1.00 98.47  ? 282 PRO A O   1 
ATOM   2176 C  CB  . PRO A 1 301 ? 88.220  151.670 91.085  1.00 98.47  ? 282 PRO A CB  1 
ATOM   2177 C  CG  . PRO A 1 301 ? 88.479  151.027 89.771  1.00 98.47  ? 282 PRO A CG  1 
ATOM   2178 C  CD  . PRO A 1 301 ? 87.661  149.764 89.767  1.00 98.47  ? 282 PRO A CD  1 
ATOM   2179 N  N   . GLY A 1 302 ? 87.658  151.047 94.367  1.00 96.08  ? 283 GLY A N   1 
ATOM   2180 C  CA  . GLY A 1 302 ? 86.890  151.244 95.572  1.00 96.08  ? 283 GLY A CA  1 
ATOM   2181 C  C   . GLY A 1 302 ? 86.734  150.000 96.421  1.00 96.08  ? 283 GLY A C   1 
ATOM   2182 O  O   . GLY A 1 302 ? 86.415  150.114 97.610  1.00 96.08  ? 283 GLY A O   1 
ATOM   2183 N  N   . ASN A 1 303 ? 86.951  148.823 95.844  1.00 97.35  ? 284 ASN A N   1 
ATOM   2184 C  CA  . ASN A 1 303 ? 86.856  147.560 96.574  1.00 97.35  ? 284 ASN A CA  1 
ATOM   2185 C  C   . ASN A 1 303 ? 88.246  147.091 97.002  1.00 97.35  ? 284 ASN A C   1 
ATOM   2186 O  O   . ASN A 1 303 ? 88.756  146.060 96.564  1.00 97.35  ? 284 ASN A O   1 
ATOM   2187 C  CB  . ASN A 1 303 ? 86.152  146.511 95.719  1.00 97.35  ? 284 ASN A CB  1 
ATOM   2188 C  CG  . ASN A 1 303 ? 85.127  145.716 96.499  1.00 97.35  ? 284 ASN A CG  1 
ATOM   2189 O  OD1 . ASN A 1 303 ? 85.462  145.018 97.454  1.00 97.35  ? 284 ASN A OD1 1 
ATOM   2190 N  ND2 . ASN A 1 303 ? 83.867  145.819 96.094  1.00 97.35  ? 284 ASN A ND2 1 
ATOM   2191 N  N   . TYR A 1 304 ? 88.860  147.880 97.878  1.00 93.60  ? 285 TYR A N   1 
ATOM   2192 C  CA  . TYR A 1 304 ? 90.220  147.616 98.319  1.00 93.60  ? 285 TYR A CA  1 
ATOM   2193 C  C   . TYR A 1 304 ? 90.245  146.535 99.397  1.00 93.60  ? 285 TYR A C   1 
ATOM   2194 O  O   . TYR A 1 304 ? 89.225  146.191 99.998  1.00 93.60  ? 285 TYR A O   1 
ATOM   2195 C  CB  . TYR A 1 304 ? 90.870  148.896 98.843  1.00 93.60  ? 285 TYR A CB  1 
ATOM   2196 C  CG  . TYR A 1 304 ? 90.242  149.431 100.110 1.00 93.60  ? 285 TYR A CG  1 
ATOM   2197 C  CD1 . TYR A 1 304 ? 89.106  150.227 100.062 1.00 93.60  ? 285 TYR A CD1 1 
ATOM   2198 C  CD2 . TYR A 1 304 ? 90.790  149.148 101.353 1.00 93.60  ? 285 TYR A CD2 1 
ATOM   2199 C  CE1 . TYR A 1 304 ? 88.530  150.720 101.217 1.00 93.60  ? 285 TYR A CE1 1 
ATOM   2200 C  CE2 . TYR A 1 304 ? 90.221  149.634 102.512 1.00 93.60  ? 285 TYR A CE2 1 
ATOM   2201 C  CZ  . TYR A 1 304 ? 89.092  150.420 102.439 1.00 93.60  ? 285 TYR A CZ  1 
ATOM   2202 O  OH  . TYR A 1 304 ? 88.524  150.908 103.592 1.00 93.60  ? 285 TYR A OH  1 
ATOM   2203 N  N   . ASP A 1 305 ? 91.441  146.001 99.635  1.00 90.53  ? 286 ASP A N   1 
ATOM   2204 C  CA  . ASP A 1 305 ? 91.639  144.994 100.667 1.00 90.53  ? 286 ASP A CA  1 
ATOM   2205 C  C   . ASP A 1 305 ? 91.669  145.649 102.042 1.00 90.53  ? 286 ASP A C   1 
ATOM   2206 O  O   . ASP A 1 305 ? 92.362  146.649 102.247 1.00 90.53  ? 286 ASP A O   1 
ATOM   2207 C  CB  . ASP A 1 305 ? 92.938  144.229 100.416 1.00 90.53  ? 286 ASP A CB  1 
ATOM   2208 C  CG  . ASP A 1 305 ? 93.007  142.923 101.183 1.00 90.53  ? 286 ASP A CG  1 
ATOM   2209 O  OD1 . ASP A 1 305 ? 92.219  142.741 102.134 1.00 90.53  ? 286 ASP A OD1 1 
ATOM   2210 O  OD2 . ASP A 1 305 ? 93.856  142.077 100.834 1.00 90.53  ? 286 ASP A OD2 1 
ATOM   2211 N  N   . ARG A 1 306 ? 90.922  145.075 102.989 1.00 87.75  ? 287 ARG A N   1 
ATOM   2212 C  CA  . ARG A 1 306 ? 90.854  145.629 104.336 1.00 87.75  ? 287 ARG A CA  1 
ATOM   2213 C  C   . ARG A 1 306 ? 92.155  145.465 105.107 1.00 87.75  ? 287 ARG A C   1 
ATOM   2214 O  O   . ARG A 1 306 ? 92.305  146.082 106.168 1.00 87.75  ? 287 ARG A O   1 
ATOM   2215 C  CB  . ARG A 1 306 ? 89.715  144.978 105.120 1.00 87.75  ? 287 ARG A CB  1 
ATOM   2216 C  CG  . ARG A 1 306 ? 88.411  144.887 104.358 1.00 87.75  ? 287 ARG A CG  1 
ATOM   2217 C  CD  . ARG A 1 306 ? 87.910  146.249 103.913 1.00 87.75  ? 287 ARG A CD  1 
ATOM   2218 N  NE  . ARG A 1 306 ? 86.751  146.126 103.037 1.00 87.75  ? 287 ARG A NE  1 
ATOM   2219 C  CZ  . ARG A 1 306 ? 86.227  147.123 102.339 1.00 87.75  ? 287 ARG A CZ  1 
ATOM   2220 N  NH1 . ARG A 1 306 ? 86.730  148.345 102.395 1.00 87.75  ? 287 ARG A NH1 1 
ATOM   2221 N  NH2 . ARG A 1 306 ? 85.173  146.889 101.563 1.00 87.75  ? 287 ARG A NH2 1 
ATOM   2222 N  N   . ILE A 1 307 ? 93.088  144.652 104.607 1.00 84.35  ? 288 ILE A N   1 
ATOM   2223 C  CA  . ILE A 1 307 ? 94.366  144.465 105.287 1.00 84.35  ? 288 ILE A CA  1 
ATOM   2224 C  C   . ILE A 1 307 ? 95.108  145.791 105.393 1.00 84.35  ? 288 ILE A C   1 
ATOM   2225 O  O   . ILE A 1 307 ? 95.747  146.086 106.411 1.00 84.35  ? 288 ILE A O   1 
ATOM   2226 C  CB  . ILE A 1 307 ? 95.201  143.397 104.555 1.00 84.35  ? 288 ILE A CB  1 
ATOM   2227 C  CG1 . ILE A 1 307 ? 94.762  141.997 104.982 1.00 84.35  ? 288 ILE A CG1 1 
ATOM   2228 C  CG2 . ILE A 1 307 ? 96.687  143.587 104.818 1.00 84.35  ? 288 ILE A CG2 1 
ATOM   2229 C  CD1 . ILE A 1 307 ? 95.133  141.652 106.400 1.00 84.35  ? 288 ILE A CD1 1 
ATOM   2230 N  N   . LEU A 1 308 ? 95.016  146.621 104.352 1.00 86.48  ? 289 LEU A N   1 
ATOM   2231 C  CA  . LEU A 1 308 ? 95.651  147.932 104.377 1.00 86.48  ? 289 LEU A CA  1 
ATOM   2232 C  C   . LEU A 1 308 ? 95.031  148.862 105.412 1.00 86.48  ? 289 LEU A C   1 
ATOM   2233 O  O   . LEU A 1 308 ? 95.635  149.888 105.741 1.00 86.48  ? 289 LEU A O   1 
ATOM   2234 C  CB  . LEU A 1 308 ? 95.576  148.569 102.990 1.00 86.48  ? 289 LEU A CB  1 
ATOM   2235 C  CG  . LEU A 1 308 ? 96.141  147.711 101.858 1.00 86.48  ? 289 LEU A CG  1 
ATOM   2236 C  CD1 . LEU A 1 308 ? 96.038  148.438 100.529 1.00 86.48  ? 289 LEU A CD1 1 
ATOM   2237 C  CD2 . LEU A 1 308 ? 97.581  147.320 102.152 1.00 86.48  ? 289 LEU A CD2 1 
ATOM   2238 N  N   . ASP A 1 309 ? 93.845  148.534 105.929 1.00 88.64  ? 290 ASP A N   1 
ATOM   2239 C  CA  . ASP A 1 309 ? 93.237  149.352 106.972 1.00 88.64  ? 290 ASP A CA  1 
ATOM   2240 C  C   . ASP A 1 309 ? 93.963  149.223 108.303 1.00 88.64  ? 290 ASP A C   1 
ATOM   2241 O  O   . ASP A 1 309 ? 93.831  150.108 109.155 1.00 88.64  ? 290 ASP A O   1 
ATOM   2242 C  CB  . ASP A 1 309 ? 91.764  148.980 107.146 1.00 88.64  ? 290 ASP A CB  1 
ATOM   2243 C  CG  . ASP A 1 309 ? 90.859  149.732 106.192 1.00 88.64  ? 290 ASP A CG  1 
ATOM   2244 O  OD1 . ASP A 1 309 ? 91.385  150.427 105.298 1.00 88.64  ? 290 ASP A OD1 1 
ATOM   2245 O  OD2 . ASP A 1 309 ? 89.624  149.629 106.337 1.00 88.64  ? 290 ASP A OD2 1 
ATOM   2246 N  N   . VAL A 1 310 ? 94.723  148.148 108.502 1.00 81.32  ? 291 VAL A N   1 
ATOM   2247 C  CA  . VAL A 1 310 ? 95.508  147.950 109.712 1.00 81.32  ? 291 VAL A CA  1 
ATOM   2248 C  C   . VAL A 1 310 ? 97.000  147.877 109.434 1.00 81.32  ? 291 VAL A C   1 
ATOM   2249 O  O   . VAL A 1 310 ? 97.788  147.776 110.380 1.00 81.32  ? 291 VAL A O   1 
ATOM   2250 C  CB  . VAL A 1 310 ? 95.049  146.694 110.480 1.00 81.32  ? 291 VAL A CB  1 
ATOM   2251 C  CG1 . VAL A 1 310 ? 93.570  146.786 110.811 1.00 81.32  ? 291 VAL A CG1 1 
ATOM   2252 C  CG2 . VAL A 1 310 ? 95.343  145.443 109.672 1.00 81.32  ? 291 VAL A CG2 1 
ATOM   2253 N  N   . SER A 1 311 ? 97.415  147.926 108.170 1.00 78.72  ? 292 SER A N   1 
ATOM   2254 C  CA  . SER A 1 311 ? 98.821  147.844 107.799 1.00 78.72  ? 292 SER A CA  1 
ATOM   2255 C  C   . SER A 1 311 ? 99.186  149.049 106.947 1.00 78.72  ? 292 SER A C   1 
ATOM   2256 O  O   . SER A 1 311 ? 98.473  149.378 105.994 1.00 78.72  ? 292 SER A O   1 
ATOM   2257 C  CB  . SER A 1 311 ? 99.118  146.549 107.039 1.00 78.72  ? 292 SER A CB  1 
ATOM   2258 O  OG  . SER A 1 311 ? 98.563  145.431 107.708 1.00 78.72  ? 292 SER A OG  1 
ATOM   2259 N  N   . ARG A 1 312 ? 100.292 149.701 107.292 1.00 79.12  ? 293 ARG A N   1 
ATOM   2260 C  CA  . ARG A 1 312 ? 100.772 150.881 106.586 1.00 79.12  ? 293 ARG A CA  1 
ATOM   2261 C  C   . ARG A 1 312 ? 102.087 150.555 105.891 1.00 79.12  ? 293 ARG A C   1 
ATOM   2262 O  O   . ARG A 1 312 ? 103.015 150.042 106.523 1.00 79.12  ? 293 ARG A O   1 
ATOM   2263 C  CB  . ARG A 1 312 ? 100.962 152.055 107.548 1.00 79.12  ? 293 ARG A CB  1 
ATOM   2264 C  CG  . ARG A 1 312 ? 101.795 153.192 106.981 1.00 79.12  ? 293 ARG A CG  1 
ATOM   2265 C  CD  . ARG A 1 312 ? 101.626 154.491 107.765 1.00 79.12  ? 293 ARG A CD  1 
ATOM   2266 N  NE  . ARG A 1 312 ? 102.133 154.399 109.130 1.00 79.12  ? 293 ARG A NE  1 
ATOM   2267 C  CZ  . ARG A 1 312 ? 101.402 154.081 110.190 1.00 79.12  ? 293 ARG A CZ  1 
ATOM   2268 N  NH1 . ARG A 1 312 ? 100.104 153.842 110.089 1.00 79.12  ? 293 ARG A NH1 1 
ATOM   2269 N  NH2 . ARG A 1 312 ? 101.985 154.009 111.383 1.00 79.12  ? 293 ARG A NH2 1 
ATOM   2270 N  N   . ALA A 1 313 ? 102.163 150.857 104.598 1.00 78.83  ? 294 ALA A N   1 
ATOM   2271 C  CA  . ALA A 1 313 ? 103.378 150.642 103.825 1.00 78.83  ? 294 ALA A CA  1 
ATOM   2272 C  C   . ALA A 1 313 ? 104.228 151.904 103.842 1.00 78.83  ? 294 ALA A C   1 
ATOM   2273 O  O   . ALA A 1 313 ? 103.747 152.989 103.501 1.00 78.83  ? 294 ALA A O   1 
ATOM   2274 C  CB  . ALA A 1 313 ? 103.041 150.248 102.387 1.00 78.83  ? 294 ALA A CB  1 
ATOM   2275 N  N   . ILE A 1 314 ? 105.490 151.759 104.241 1.00 79.49  ? 295 ILE A N   1 
ATOM   2276 C  CA  . ILE A 1 314 ? 106.413 152.885 104.319 1.00 79.49  ? 295 ILE A CA  1 
ATOM   2277 C  C   . ILE A 1 314 ? 107.637 152.714 103.434 1.00 79.49  ? 295 ILE A C   1 
ATOM   2278 O  O   . ILE A 1 314 ? 108.353 153.699 103.201 1.00 79.49  ? 295 ILE A O   1 
ATOM   2279 C  CB  . ILE A 1 314 ? 106.856 153.154 105.774 1.00 79.49  ? 295 ILE A CB  1 
ATOM   2280 C  CG1 . ILE A 1 314 ? 107.922 152.144 106.201 1.00 79.49  ? 295 ILE A CG1 1 
ATOM   2281 C  CG2 . ILE A 1 314 ? 105.660 153.115 106.714 1.00 79.49  ? 295 ILE A CG2 1 
ATOM   2282 C  CD1 . ILE A 1 314 ? 108.135 152.073 107.696 1.00 79.49  ? 295 ILE A CD1 1 
ATOM   2283 N  N   . THR A 1 315 ? 107.908 151.510 102.935 1.00 79.64  ? 296 THR A N   1 
ATOM   2284 C  CA  . THR A 1 315 ? 109.073 151.257 102.098 1.00 79.64  ? 296 THR A CA  1 
ATOM   2285 C  C   . THR A 1 315 ? 108.694 150.267 101.010 1.00 79.64  ? 296 THR A C   1 
ATOM   2286 O  O   . THR A 1 315 ? 108.062 149.247 101.295 1.00 79.64  ? 296 THR A O   1 
ATOM   2287 C  CB  . THR A 1 315 ? 110.241 150.710 102.929 1.00 79.64  ? 296 THR A CB  1 
ATOM   2288 O  OG1 . THR A 1 315 ? 110.629 151.681 103.909 1.00 79.64  ? 296 THR A OG1 1 
ATOM   2289 C  CG2 . THR A 1 315 ? 111.433 150.386 102.042 1.00 79.64  ? 296 THR A CG2 1 
ATOM   2290 N  N   . GLY A 1 316 ? 109.087 150.569 99.773  1.00 78.05  ? 297 GLY A N   1 
ATOM   2291 C  CA  . GLY A 1 316 ? 108.824 149.699 98.642  1.00 78.05  ? 297 GLY A CA  1 
ATOM   2292 C  C   . GLY A 1 316 ? 109.801 149.919 97.505  1.00 78.05  ? 297 GLY A C   1 
ATOM   2293 O  O   . GLY A 1 316 ? 110.017 151.057 97.079  1.00 78.05  ? 297 GLY A O   1 
ATOM   2294 N  N   . THR A 1 317 ? 110.399 148.840 97.003  1.00 76.91  ? 298 THR A N   1 
ATOM   2295 C  CA  . THR A 1 317 ? 111.435 148.953 95.985  1.00 76.91  ? 298 THR A CA  1 
ATOM   2296 C  C   . THR A 1 317 ? 111.438 147.700 95.117  1.00 76.91  ? 298 THR A C   1 
ATOM   2297 O  O   . THR A 1 317 ? 110.940 146.642 95.512  1.00 76.91  ? 298 THR A O   1 
ATOM   2298 C  CB  . THR A 1 317 ? 112.821 149.170 96.614  1.00 76.91  ? 298 THR A CB  1 
ATOM   2299 O  OG1 . THR A 1 317 ? 112.712 150.070 97.724  1.00 76.91  ? 298 THR A OG1 1 
ATOM   2300 C  CG2 . THR A 1 317 ? 113.781 149.781 95.603  1.00 76.91  ? 298 THR A CG2 1 
ATOM   2301 N  N   . LEU A 1 318 ? 111.993 147.842 93.913  1.00 73.23  ? 299 LEU A N   1 
ATOM   2302 C  CA  . LEU A 1 318 ? 112.128 146.755 92.953  1.00 73.23  ? 299 LEU A CA  1 
ATOM   2303 C  C   . LEU A 1 318 ? 113.596 146.566 92.594  1.00 73.23  ? 299 LEU A C   1 
ATOM   2304 O  O   . LEU A 1 318 ? 114.313 147.540 92.345  1.00 73.23  ? 299 LEU A O   1 
ATOM   2305 C  CB  . LEU A 1 318 ? 111.307 147.038 91.687  1.00 73.23  ? 299 LEU A CB  1 
ATOM   2306 C  CG  . LEU A 1 318 ? 111.155 145.934 90.637  1.00 73.23  ? 299 LEU A CG  1 
ATOM   2307 C  CD1 . LEU A 1 318 ? 109.812 146.062 89.941  1.00 73.23  ? 299 LEU A CD1 1 
ATOM   2308 C  CD2 . LEU A 1 318 ? 112.275 145.987 89.612  1.00 73.23  ? 299 LEU A CD2 1 
ATOM   2309 N  N   . PHE A 1 319 ? 114.037 145.310 92.563  1.00 70.02  ? 300 PHE A N   1 
ATOM   2310 C  CA  . PHE A 1 319 ? 115.410 144.964 92.233  1.00 70.02  ? 300 PHE A CA  1 
ATOM   2311 C  C   . PHE A 1 319 ? 115.430 143.825 91.221  1.00 70.02  ? 300 PHE A C   1 
ATOM   2312 O  O   . PHE A 1 319 ? 114.460 143.077 91.072  1.00 70.02  ? 300 PHE A O   1 
ATOM   2313 C  CB  . PHE A 1 319 ? 116.213 144.555 93.477  1.00 70.02  ? 300 PHE A CB  1 
ATOM   2314 C  CG  . PHE A 1 319 ? 116.218 145.585 94.569  1.00 70.02  ? 300 PHE A CG  1 
ATOM   2315 C  CD1 . PHE A 1 319 ? 117.193 146.565 94.608  1.00 70.02  ? 300 PHE A CD1 1 
ATOM   2316 C  CD2 . PHE A 1 319 ? 115.259 145.561 95.565  1.00 70.02  ? 300 PHE A CD2 1 
ATOM   2317 C  CE1 . PHE A 1 319 ? 117.205 147.509 95.615  1.00 70.02  ? 300 PHE A CE1 1 
ATOM   2318 C  CE2 . PHE A 1 319 ? 115.266 146.501 96.574  1.00 70.02  ? 300 PHE A CE2 1 
ATOM   2319 C  CZ  . PHE A 1 319 ? 116.240 147.476 96.599  1.00 70.02  ? 300 PHE A CZ  1 
ATOM   2320 N  N   . PHE A 1 320 ? 116.558 143.705 90.527  1.00 72.31  ? 301 PHE A N   1 
ATOM   2321 C  CA  . PHE A 1 320 ? 116.808 142.626 89.582  1.00 72.31  ? 301 PHE A CA  1 
ATOM   2322 C  C   . PHE A 1 320 ? 117.854 141.689 90.169  1.00 72.31  ? 301 PHE A C   1 
ATOM   2323 O  O   . PHE A 1 320 ? 118.885 142.145 90.673  1.00 72.31  ? 301 PHE A O   1 
ATOM   2324 C  CB  . PHE A 1 320 ? 117.284 143.177 88.237  1.00 72.31  ? 301 PHE A CB  1 
ATOM   2325 C  CG  . PHE A 1 320 ? 117.745 142.119 87.277  1.00 72.31  ? 301 PHE A CG  1 
ATOM   2326 C  CD1 . PHE A 1 320 ? 116.840 141.252 86.694  1.00 72.31  ? 301 PHE A CD1 1 
ATOM   2327 C  CD2 . PHE A 1 320 ? 119.086 141.992 86.958  1.00 72.31  ? 301 PHE A CD2 1 
ATOM   2328 C  CE1 . PHE A 1 320 ? 117.261 140.278 85.811  1.00 72.31  ? 301 PHE A CE1 1 
ATOM   2329 C  CE2 . PHE A 1 320 ? 119.513 141.020 86.076  1.00 72.31  ? 301 PHE A CE2 1 
ATOM   2330 C  CZ  . PHE A 1 320 ? 118.599 140.163 85.502  1.00 72.31  ? 301 PHE A CZ  1 
ATOM   2331 N  N   . VAL A 1 321 ? 117.594 140.388 90.101  1.00 75.04  ? 302 VAL A N   1 
ATOM   2332 C  CA  . VAL A 1 321 ? 118.483 139.369 90.644  1.00 75.04  ? 302 VAL A CA  1 
ATOM   2333 C  C   . VAL A 1 321 ? 119.151 138.654 89.472  1.00 75.04  ? 302 VAL A C   1 
ATOM   2334 O  O   . VAL A 1 321 ? 118.496 137.868 88.770  1.00 75.04  ? 302 VAL A O   1 
ATOM   2335 C  CB  . VAL A 1 321 ? 117.727 138.378 91.538  1.00 75.04  ? 302 VAL A CB  1 
ATOM   2336 C  CG1 . VAL A 1 321 ? 118.660 137.279 92.016  1.00 75.04  ? 302 VAL A CG1 1 
ATOM   2337 C  CG2 . VAL A 1 321 ? 117.099 139.102 92.715  1.00 75.04  ? 302 VAL A CG2 1 
ATOM   2338 N  N   . PRO A 1 322 ? 120.433 138.894 89.217  1.00 79.12  ? 303 PRO A N   1 
ATOM   2339 C  CA  . PRO A 1 322 ? 121.130 138.192 88.137  1.00 79.12  ? 303 PRO A CA  1 
ATOM   2340 C  C   . PRO A 1 322 ? 121.581 136.805 88.578  1.00 79.12  ? 303 PRO A C   1 
ATOM   2341 O  O   . PRO A 1 322 ? 121.485 136.425 89.745  1.00 79.12  ? 303 PRO A O   1 
ATOM   2342 C  CB  . PRO A 1 322 ? 122.328 139.099 87.848  1.00 79.12  ? 303 PRO A CB  1 
ATOM   2343 C  CG  . PRO A 1 322 ? 122.605 139.755 89.154  1.00 79.12  ? 303 PRO A CG  1 
ATOM   2344 C  CD  . PRO A 1 322 ? 121.271 139.939 89.829  1.00 79.12  ? 303 PRO A CD  1 
ATOM   2345 N  N   . THR A 1 323 ? 122.084 136.047 87.608  1.00 85.62  ? 304 THR A N   1 
ATOM   2346 C  CA  . THR A 1 323 ? 122.539 134.691 87.869  1.00 85.62  ? 304 THR A CA  1 
ATOM   2347 C  C   . THR A 1 323 ? 123.850 134.695 88.651  1.00 85.62  ? 304 THR A C   1 
ATOM   2348 O  O   . THR A 1 323 ? 124.591 135.682 88.677  1.00 85.62  ? 304 THR A O   1 
ATOM   2349 C  CB  . THR A 1 323 ? 122.731 133.924 86.563  1.00 85.62  ? 304 THR A CB  1 
ATOM   2350 O  OG1 . THR A 1 323 ? 123.840 134.475 85.844  1.00 85.62  ? 304 THR A OG1 1 
ATOM   2351 C  CG2 . THR A 1 323 ? 121.494 134.037 85.710  1.00 85.62  ? 304 THR A CG2 1 
ATOM   2352 N  N   . THR A 1 324 ? 124.130 133.560 89.296  1.00 87.87  ? 305 THR A N   1 
ATOM   2353 C  CA  . THR A 1 324 ? 125.376 133.417 90.041  1.00 87.87  ? 305 THR A CA  1 
ATOM   2354 C  C   . THR A 1 324 ? 126.584 133.477 89.115  1.00 87.87  ? 305 THR A C   1 
ATOM   2355 O  O   . THR A 1 324 ? 127.607 134.083 89.454  1.00 87.87  ? 305 THR A O   1 
ATOM   2356 C  CB  . THR A 1 324 ? 125.370 132.106 90.828  1.00 87.87  ? 305 THR A CB  1 
ATOM   2357 O  OG1 . THR A 1 324 ? 124.183 132.032 91.626  1.00 87.87  ? 305 THR A OG1 1 
ATOM   2358 C  CG2 . THR A 1 324 ? 126.586 132.024 91.735  1.00 87.87  ? 305 THR A CG2 1 
ATOM   2359 N  N   . SER A 1 325 ? 126.486 132.847 87.941  1.00 88.88  ? 306 SER A N   1 
ATOM   2360 C  CA  . SER A 1 325 ? 127.591 132.879 86.988  1.00 88.88  ? 306 SER A CA  1 
ATOM   2361 C  C   . SER A 1 325 ? 127.867 134.298 86.509  1.00 88.88  ? 306 SER A C   1 
ATOM   2362 O  O   . SER A 1 325 ? 129.028 134.693 86.349  1.00 88.88  ? 306 SER A O   1 
ATOM   2363 C  CB  . SER A 1 325 ? 127.290 131.961 85.804  1.00 88.88  ? 306 SER A CB  1 
ATOM   2364 O  OG  . SER A 1 325 ? 127.034 130.637 86.238  1.00 88.88  ? 306 SER A OG  1 
ATOM   2365 N  N   . PHE A 1 326 ? 126.811 135.081 86.274  1.00 87.77  ? 307 PHE A N   1 
ATOM   2366 C  CA  . PHE A 1 326 ? 127.005 136.470 85.871  1.00 87.77  ? 307 PHE A CA  1 
ATOM   2367 C  C   . PHE A 1 326 ? 127.721 137.262 86.956  1.00 87.77  ? 307 PHE A C   1 
ATOM   2368 O  O   . PHE A 1 326 ? 128.603 138.074 86.659  1.00 87.77  ? 307 PHE A O   1 
ATOM   2369 C  CB  . PHE A 1 326 ? 125.662 137.116 85.531  1.00 87.77  ? 307 PHE A CB  1 
ATOM   2370 C  CG  . PHE A 1 326 ? 125.766 138.565 85.149  1.00 87.77  ? 307 PHE A CG  1 
ATOM   2371 C  CD1 . PHE A 1 326 ? 126.055 138.932 83.846  1.00 87.77  ? 307 PHE A CD1 1 
ATOM   2372 C  CD2 . PHE A 1 326 ? 125.565 139.562 86.090  1.00 87.77  ? 307 PHE A CD2 1 
ATOM   2373 C  CE1 . PHE A 1 326 ? 126.150 140.263 83.491  1.00 87.77  ? 307 PHE A CE1 1 
ATOM   2374 C  CE2 . PHE A 1 326 ? 125.659 140.894 85.741  1.00 87.77  ? 307 PHE A CE2 1 
ATOM   2375 C  CZ  . PHE A 1 326 ? 125.950 141.245 84.439  1.00 87.77  ? 307 PHE A CZ  1 
ATOM   2376 N  N   . LEU A 1 327 ? 127.353 137.040 88.220  1.00 87.59  ? 308 LEU A N   1 
ATOM   2377 C  CA  . LEU A 1 327 ? 128.044 137.710 89.317  1.00 87.59  ? 308 LEU A CA  1 
ATOM   2378 C  C   . LEU A 1 327 ? 129.506 137.290 89.390  1.00 87.59  ? 308 LEU A C   1 
ATOM   2379 O  O   . LEU A 1 327 ? 130.392 138.127 89.600  1.00 87.59  ? 308 LEU A O   1 
ATOM   2380 C  CB  . LEU A 1 327 ? 127.339 137.420 90.641  1.00 87.59  ? 308 LEU A CB  1 
ATOM   2381 C  CG  . LEU A 1 327 ? 125.967 138.065 90.834  1.00 87.59  ? 308 LEU A CG  1 
ATOM   2382 C  CD1 . LEU A 1 327 ? 125.374 137.658 92.171  1.00 87.59  ? 308 LEU A CD1 1 
ATOM   2383 C  CD2 . LEU A 1 327 ? 126.067 139.577 90.723  1.00 87.59  ? 308 LEU A CD2 1 
ATOM   2384 N  N   . ASP A 1 328 ? 129.779 135.996 89.216  1.00 87.79  ? 309 ASP A N   1 
ATOM   2385 C  CA  . ASP A 1 328 ? 131.153 135.510 89.262  1.00 87.79  ? 309 ASP A CA  1 
ATOM   2386 C  C   . ASP A 1 328 ? 131.965 135.931 88.045  1.00 87.79  ? 309 ASP A C   1 
ATOM   2387 O  O   . ASP A 1 328 ? 133.196 135.839 88.079  1.00 87.79  ? 309 ASP A O   1 
ATOM   2388 C  CB  . ASP A 1 328 ? 131.166 133.986 89.390  1.00 87.79  ? 309 ASP A CB  1 
ATOM   2389 C  CG  . ASP A 1 328 ? 130.763 133.514 90.772  1.00 87.79  ? 309 ASP A CG  1 
ATOM   2390 O  OD1 . ASP A 1 328 ? 130.783 134.336 91.712  1.00 87.79  ? 309 ASP A OD1 1 
ATOM   2391 O  OD2 . ASP A 1 328 ? 130.428 132.320 90.920  1.00 87.79  ? 309 ASP A OD2 1 
ATOM   2392 N  N   . SER A 1 329 ? 131.314 136.386 86.978  1.00 89.77  ? 310 SER A N   1 
ATOM   2393 C  CA  . SER A 1 329 ? 132.003 136.719 85.739  1.00 89.77  ? 310 SER A CA  1 
ATOM   2394 C  C   . SER A 1 329 ? 132.342 138.199 85.606  1.00 89.77  ? 310 SER A C   1 
ATOM   2395 O  O   . SER A 1 329 ? 132.876 138.601 84.568  1.00 89.77  ? 310 SER A O   1 
ATOM   2396 C  CB  . SER A 1 329 ? 131.161 136.279 84.537  1.00 89.77  ? 310 SER A CB  1 
ATOM   2397 O  OG  . SER A 1 329 ? 130.980 134.874 84.528  1.00 89.77  ? 310 SER A OG  1 
ATOM   2398 N  N   . ILE A 1 330 ? 132.053 139.019 86.612  1.00 91.70  ? 311 ILE A N   1 
ATOM   2399 C  CA  . ILE A 1 330 ? 132.349 140.445 86.523  1.00 91.70  ? 311 ILE A CA  1 
ATOM   2400 C  C   . ILE A 1 330 ? 133.813 140.678 86.867  1.00 91.70  ? 311 ILE A C   1 
ATOM   2401 O  O   . ILE A 1 330 ? 134.324 140.146 87.860  1.00 91.70  ? 311 ILE A O   1 
ATOM   2402 C  CB  . ILE A 1 330 ? 131.433 141.263 87.446  1.00 91.70  ? 311 ILE A CB  1 
ATOM   2403 C  CG1 . ILE A 1 330 ? 130.000 140.742 87.399  1.00 91.70  ? 311 ILE A CG1 1 
ATOM   2404 C  CG2 . ILE A 1 330 ? 131.454 142.722 87.039  1.00 91.70  ? 311 ILE A CG2 1 
ATOM   2405 C  CD1 . ILE A 1 330 ? 129.205 141.057 88.645  1.00 91.70  ? 311 ILE A CD1 1 
ATOM   2406 N  N   . GLU A 1 331 ? 134.492 141.476 86.045  1.00 100.24 ? 312 GLU A N   1 
ATOM   2407 C  CA  . GLU A 1 331 ? 135.871 141.861 86.290  1.00 100.24 ? 312 GLU A CA  1 
ATOM   2408 C  C   . GLU A 1 331 ? 135.929 143.306 86.757  1.00 100.24 ? 312 GLU A C   1 
ATOM   2409 O  O   . GLU A 1 331 ? 135.353 144.184 86.100  1.00 100.24 ? 312 GLU A O   1 
ATOM   2410 C  CB  . GLU A 1 331 ? 136.718 141.689 85.025  1.00 100.24 ? 312 GLU A CB  1 
ATOM   2411 C  CG  . GLU A 1 331 ? 136.902 140.243 84.596  1.00 100.24 ? 312 GLU A CG  1 
ATOM   2412 C  CD  . GLU A 1 331 ? 137.995 140.080 83.559  1.00 100.24 ? 312 GLU A CD  1 
ATOM   2413 O  OE1 . GLU A 1 331 ? 138.559 141.104 83.122  1.00 100.24 ? 312 GLU A OE1 1 
ATOM   2414 O  OE2 . GLU A 1 331 ? 138.290 138.926 83.182  1.00 100.24 ? 312 GLU A OE2 1 
ATOM   2415 N  N   . PRO A 1 332 ? 136.600 143.595 87.882  1.00 101.54 ? 313 PRO A N   1 
ATOM   2416 C  CA  . PRO A 1 332 ? 136.728 144.950 88.430  1.00 101.54 ? 313 PRO A CA  1 
ATOM   2417 C  C   . PRO A 1 332 ? 137.366 145.929 87.448  1.00 101.54 ? 313 PRO A C   1 
ATOM   2418 O  O   . PRO A 1 332 ? 136.645 146.726 86.848  1.00 101.54 ? 313 PRO A O   1 
ATOM   2419 C  CB  . PRO A 1 332 ? 137.630 144.752 89.657  1.00 101.54 ? 313 PRO A CB  1 
ATOM   2420 C  CG  . PRO A 1 332 ? 138.273 143.410 89.458  1.00 101.54 ? 313 PRO A CG  1 
ATOM   2421 C  CD  . PRO A 1 332 ? 137.244 142.598 88.751  1.00 101.54 ? 313 PRO A CD  1 
HETATM 2422 C  CHA . HEM B 2 .   ? 97.639  135.283 100.391 1.00 50.95  ? 401 HEM A CHA 1 
HETATM 2423 C  CHB . HEM B 2 .   ? 98.809  137.868 104.326 1.00 50.95  ? 401 HEM A CHB 1 
HETATM 2424 C  CHC . HEM B 2 .   ? 100.439 141.416 101.457 1.00 50.95  ? 401 HEM A CHC 1 
HETATM 2425 C  CHD . HEM B 2 .   ? 100.021 138.477 97.628  1.00 50.95  ? 401 HEM A CHD 1 
HETATM 2426 C  C1A . HEM B 2 .   ? 97.808  135.658 101.705 1.00 50.95  ? 401 HEM A C1A 1 
HETATM 2427 C  C2A . HEM B 2 .   ? 97.457  134.883 102.876 1.00 50.95  ? 401 HEM A C2A 1 
HETATM 2428 C  C3A . HEM B 2 .   ? 97.779  135.597 103.957 1.00 50.95  ? 401 HEM A C3A 1 
HETATM 2429 C  C4A . HEM B 2 .   ? 98.349  136.853 103.515 1.00 50.95  ? 401 HEM A C4A 1 
HETATM 2430 C  CMA . HEM B 2 .   ? 97.583  135.166 105.425 1.00 50.95  ? 401 HEM A CMA 1 
HETATM 2431 C  CAA . HEM B 2 .   ? 96.819  133.479 102.875 1.00 50.95  ? 401 HEM A CAA 1 
HETATM 2432 C  CBA . HEM B 2 .   ? 97.915  132.437 103.063 1.00 50.95  ? 401 HEM A CBA 1 
HETATM 2433 C  CGA . HEM B 2 .   ? 98.426  132.005 101.716 1.00 50.95  ? 401 HEM A CGA 1 
HETATM 2434 O  O1A . HEM B 2 .   ? 99.552  131.451 101.652 1.00 50.95  ? 401 HEM A O1A 1 
HETATM 2435 O  O2A . HEM B 2 .   ? 97.710  132.219 100.705 1.00 50.95  ? 401 HEM A O2A 1 
HETATM 2436 C  C1B . HEM B 2 .   ? 99.371  139.051 103.899 1.00 50.95  ? 401 HEM A C1B 1 
HETATM 2437 C  C2B . HEM B 2 .   ? 99.910  140.094 104.747 1.00 50.95  ? 401 HEM A C2B 1 
HETATM 2438 C  C3B . HEM B 2 .   ? 100.365 141.082 103.953 1.00 50.95  ? 401 HEM A C3B 1 
HETATM 2439 C  C4B . HEM B 2 .   ? 100.122 140.684 102.581 1.00 50.95  ? 401 HEM A C4B 1 
HETATM 2440 C  CMB . HEM B 2 .   ? 99.922  140.005 106.290 1.00 50.95  ? 401 HEM A CMB 1 
HETATM 2441 C  CAB . HEM B 2 .   ? 101.036 142.432 104.319 1.00 50.95  ? 401 HEM A CAB 1 
HETATM 2442 C  CBB . HEM B 2 .   ? 101.277 142.855 105.564 1.00 50.95  ? 401 HEM A CBB 1 
HETATM 2443 C  C1C . HEM B 2 .   ? 100.487 140.930 100.168 1.00 50.95  ? 401 HEM A C1C 1 
HETATM 2444 C  C2C . HEM B 2 .   ? 100.965 141.645 99.002  1.00 50.95  ? 401 HEM A C2C 1 
HETATM 2445 C  C3C . HEM B 2 .   ? 100.848 140.830 97.938  1.00 50.95  ? 401 HEM A C3C 1 
HETATM 2446 C  C4C . HEM B 2 .   ? 100.294 139.578 98.409  1.00 50.95  ? 401 HEM A C4C 1 
HETATM 2447 C  CMC . HEM B 2 .   ? 101.498 143.094 99.060  1.00 50.95  ? 401 HEM A CMC 1 
HETATM 2448 C  CAC . HEM B 2 .   ? 101.205 141.064 96.447  1.00 50.95  ? 401 HEM A CAC 1 
HETATM 2449 C  CBC . HEM B 2 .   ? 101.727 142.189 95.951  1.00 50.95  ? 401 HEM A CBC 1 
HETATM 2450 C  C1D . HEM B 2 .   ? 99.374  137.336 98.046  1.00 50.95  ? 401 HEM A C1D 1 
HETATM 2451 C  C2D . HEM B 2 .   ? 99.139  136.148 97.256  1.00 50.95  ? 401 HEM A C2D 1 
HETATM 2452 C  C3D . HEM B 2 .   ? 98.483  135.267 98.009  1.00 50.95  ? 401 HEM A C3D 1 
HETATM 2453 C  C4D . HEM B 2 .   ? 98.275  135.860 99.315  1.00 50.95  ? 401 HEM A C4D 1 
HETATM 2454 C  CMD . HEM B 2 .   ? 99.571  135.935 95.791  1.00 50.95  ? 401 HEM A CMD 1 
HETATM 2455 C  CAD . HEM B 2 .   ? 98.033  133.864 97.552  1.00 50.95  ? 401 HEM A CAD 1 
HETATM 2456 C  CBD . HEM B 2 .   ? 96.517  133.852 97.386  1.00 50.95  ? 401 HEM A CBD 1 
HETATM 2457 C  CGD . HEM B 2 .   ? 96.118  132.743 96.450  1.00 50.95  ? 401 HEM A CGD 1 
HETATM 2458 O  O1D . HEM B 2 .   ? 97.023  132.084 95.878  1.00 50.95  ? 401 HEM A O1D 1 
HETATM 2459 O  O2D . HEM B 2 .   ? 94.894  132.521 96.269  1.00 50.95  ? 401 HEM A O2D 1 
HETATM 2460 N  NA  . HEM B 2 .   ? 98.349  136.854 102.134 1.00 50.95  ? 401 HEM A NA  1 
HETATM 2461 N  NB  . HEM B 2 .   ? 99.516  139.444 102.585 1.00 50.95  ? 401 HEM A NB  1 
HETATM 2462 N  NC  . HEM B 2 .   ? 100.087 139.673 99.769  1.00 50.95  ? 401 HEM A NC  1 
HETATM 2463 N  ND  . HEM B 2 .   ? 98.833  137.124 99.299  1.00 50.95  ? 401 HEM A ND  1 
HETATM 2464 FE FE  . HEM B 2 .   ? 99.180  138.281 100.944 1.00 50.95  ? 401 HEM A FE  1 
# 
