data_8ZGI
# 
_entry.id   8ZGI 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8ZGI         pdb_00008zgi 10.2210/pdb8zgi/pdb 
WWPDB D_1300047732 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-12 ? 
2 'Structure model' 1 1 2025-04-09 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume' 
2 2 'Structure model' '_citation.page_first'     
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8ZGI 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-09 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_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_contact_author.id                 2 
_pdbx_contact_author.email              qiang_chen@scu.edu.cn 
_pdbx_contact_author.name_first         Qiang 
_pdbx_contact_author.name_last          Chen 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-2398-4482 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Chen, Q.' 1 ? 
'Yu, Y.'   2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Mol.Cell 
_citation.journal_id_ASTM           MOCEFL 
_citation.journal_id_CSD            2168 
_citation.journal_id_ISSN           1097-2765 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            85 
_citation.language                  ? 
_citation.page_first                1176 
_citation.page_last                 ? 
_citation.title                     'DUF4297 and HerA form abortosome to mediate bacterial immunity against phage infection.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.molcel.2024.12.010 
_citation.pdbx_database_id_PubMed   40010342 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Tang, D.' 1 ? 
primary 'Liu, T.'  2 ? 
primary 'Chen, Y.' 3 ? 
primary 'Zhu, Z.'  4 ? 
primary 'Chen, H.' 5 ? 
primary 'Chen, Q.' 6 ? 
primary 'Yu, Y.'   7 ? 
# 
_entity.id                         1 
_entity.type                       polymer 
_entity.src_method                 man 
_entity.pdbx_description           'Restriction endonuclease' 
_entity.formula_weight             46971.949 
_entity.pdbx_number_of_molecules   2 
_entity.pdbx_ec                    ? 
_entity.pdbx_mutation              ? 
_entity.pdbx_fragment              ? 
_entity.details                    ? 
# 
_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       
;MDRSAVDTIRGYCYQVDKTIIEIFSLPQMDDSIDIECIEDVDVYNDGHLTAIQCKYYESTDYNHSVISKPIRLMLSHFKD
NKEKGANYYLYGHYKSGQEKLTLPLKVDFFKSNFLTYTEKKIKHEYHIENGLTEEDLQAFLDRLVININAKSFDDQKKET
IQIIKNHFQCEDYEAEHYLYSNAFRKTYDISCNKKDRRIKKSDFVESINKSKVLFNIWFYQYEGRKEYLRKLKESFIRRS
VNTSPYARFFILEFQDKTDIKTVKDCIYKIQSNWSNLSKRTDRPYSPFLLFHGTSDANLYELKNQLFNEDLIFTDGYPFK
GSVFTPKMLIEGFSNKEIHFQFINDIDDFNETLNSINIRKEVYQFYTENCLDIPSQLPQVNIQVKDFADIKEIV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MDRSAVDTIRGYCYQVDKTIIEIFSLPQMDDSIDIECIEDVDVYNDGHLTAIQCKYYESTDYNHSVISKPIRLMLSHFKD
NKEKGANYYLYGHYKSGQEKLTLPLKVDFFKSNFLTYTEKKIKHEYHIENGLTEEDLQAFLDRLVININAKSFDDQKKET
IQIIKNHFQCEDYEAEHYLYSNAFRKTYDISCNKKDRRIKKSDFVESINKSKVLFNIWFYQYEGRKEYLRKLKESFIRRS
VNTSPYARFFILEFQDKTDIKTVKDCIYKIQSNWSNLSKRTDRPYSPFLLFHGTSDANLYELKNQLFNEDLIFTDGYPFK
GSVFTPKMLIEGFSNKEIHFQFINDIDDFNETLNSINIRKEVYQFYTENCLDIPSQLPQVNIQVKDFADIKEIV
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
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   ASP n 
1 3   ARG n 
1 4   SER n 
1 5   ALA n 
1 6   VAL n 
1 7   ASP n 
1 8   THR n 
1 9   ILE n 
1 10  ARG n 
1 11  GLY n 
1 12  TYR n 
1 13  CYS n 
1 14  TYR n 
1 15  GLN n 
1 16  VAL n 
1 17  ASP n 
1 18  LYS n 
1 19  THR n 
1 20  ILE n 
1 21  ILE n 
1 22  GLU n 
1 23  ILE n 
1 24  PHE n 
1 25  SER n 
1 26  LEU n 
1 27  PRO n 
1 28  GLN n 
1 29  MET n 
1 30  ASP n 
1 31  ASP n 
1 32  SER n 
1 33  ILE n 
1 34  ASP n 
1 35  ILE n 
1 36  GLU n 
1 37  CYS n 
1 38  ILE n 
1 39  GLU n 
1 40  ASP n 
1 41  VAL n 
1 42  ASP n 
1 43  VAL n 
1 44  TYR n 
1 45  ASN n 
1 46  ASP n 
1 47  GLY n 
1 48  HIS n 
1 49  LEU n 
1 50  THR n 
1 51  ALA n 
1 52  ILE n 
1 53  GLN n 
1 54  CYS n 
1 55  LYS n 
1 56  TYR n 
1 57  TYR n 
1 58  GLU n 
1 59  SER n 
1 60  THR n 
1 61  ASP n 
1 62  TYR n 
1 63  ASN n 
1 64  HIS n 
1 65  SER n 
1 66  VAL n 
1 67  ILE n 
1 68  SER n 
1 69  LYS n 
1 70  PRO n 
1 71  ILE n 
1 72  ARG n 
1 73  LEU n 
1 74  MET n 
1 75  LEU n 
1 76  SER n 
1 77  HIS n 
1 78  PHE n 
1 79  LYS n 
1 80  ASP n 
1 81  ASN n 
1 82  LYS n 
1 83  GLU n 
1 84  LYS n 
1 85  GLY n 
1 86  ALA n 
1 87  ASN n 
1 88  TYR n 
1 89  TYR n 
1 90  LEU n 
1 91  TYR n 
1 92  GLY n 
1 93  HIS n 
1 94  TYR n 
1 95  LYS n 
1 96  SER n 
1 97  GLY n 
1 98  GLN n 
1 99  GLU n 
1 100 LYS n 
1 101 LEU n 
1 102 THR n 
1 103 LEU n 
1 104 PRO n 
1 105 LEU n 
1 106 LYS n 
1 107 VAL n 
1 108 ASP n 
1 109 PHE n 
1 110 PHE n 
1 111 LYS n 
1 112 SER n 
1 113 ASN n 
1 114 PHE n 
1 115 LEU n 
1 116 THR n 
1 117 TYR n 
1 118 THR n 
1 119 GLU n 
1 120 LYS n 
1 121 LYS n 
1 122 ILE n 
1 123 LYS n 
1 124 HIS n 
1 125 GLU n 
1 126 TYR n 
1 127 HIS n 
1 128 ILE n 
1 129 GLU n 
1 130 ASN n 
1 131 GLY n 
1 132 LEU n 
1 133 THR n 
1 134 GLU n 
1 135 GLU n 
1 136 ASP n 
1 137 LEU n 
1 138 GLN n 
1 139 ALA n 
1 140 PHE n 
1 141 LEU n 
1 142 ASP n 
1 143 ARG n 
1 144 LEU n 
1 145 VAL n 
1 146 ILE n 
1 147 ASN n 
1 148 ILE n 
1 149 ASN n 
1 150 ALA n 
1 151 LYS n 
1 152 SER n 
1 153 PHE n 
1 154 ASP n 
1 155 ASP n 
1 156 GLN n 
1 157 LYS n 
1 158 LYS n 
1 159 GLU n 
1 160 THR n 
1 161 ILE n 
1 162 GLN n 
1 163 ILE n 
1 164 ILE n 
1 165 LYS n 
1 166 ASN n 
1 167 HIS n 
1 168 PHE n 
1 169 GLN n 
1 170 CYS n 
1 171 GLU n 
1 172 ASP n 
1 173 TYR n 
1 174 GLU n 
1 175 ALA n 
1 176 GLU n 
1 177 HIS n 
1 178 TYR n 
1 179 LEU n 
1 180 TYR n 
1 181 SER n 
1 182 ASN n 
1 183 ALA n 
1 184 PHE n 
1 185 ARG n 
1 186 LYS n 
1 187 THR n 
1 188 TYR n 
1 189 ASP n 
1 190 ILE n 
1 191 SER n 
1 192 CYS n 
1 193 ASN n 
1 194 LYS n 
1 195 LYS n 
1 196 ASP n 
1 197 ARG n 
1 198 ARG n 
1 199 ILE n 
1 200 LYS n 
1 201 LYS n 
1 202 SER n 
1 203 ASP n 
1 204 PHE n 
1 205 VAL n 
1 206 GLU n 
1 207 SER n 
1 208 ILE n 
1 209 ASN n 
1 210 LYS n 
1 211 SER n 
1 212 LYS n 
1 213 VAL n 
1 214 LEU n 
1 215 PHE n 
1 216 ASN n 
1 217 ILE n 
1 218 TRP n 
1 219 PHE n 
1 220 TYR n 
1 221 GLN n 
1 222 TYR n 
1 223 GLU n 
1 224 GLY n 
1 225 ARG n 
1 226 LYS n 
1 227 GLU n 
1 228 TYR n 
1 229 LEU n 
1 230 ARG n 
1 231 LYS n 
1 232 LEU n 
1 233 LYS n 
1 234 GLU n 
1 235 SER n 
1 236 PHE n 
1 237 ILE n 
1 238 ARG n 
1 239 ARG n 
1 240 SER n 
1 241 VAL n 
1 242 ASN n 
1 243 THR n 
1 244 SER n 
1 245 PRO n 
1 246 TYR n 
1 247 ALA n 
1 248 ARG n 
1 249 PHE n 
1 250 PHE n 
1 251 ILE n 
1 252 LEU n 
1 253 GLU n 
1 254 PHE n 
1 255 GLN n 
1 256 ASP n 
1 257 LYS n 
1 258 THR n 
1 259 ASP n 
1 260 ILE n 
1 261 LYS n 
1 262 THR n 
1 263 VAL n 
1 264 LYS n 
1 265 ASP n 
1 266 CYS n 
1 267 ILE n 
1 268 TYR n 
1 269 LYS n 
1 270 ILE n 
1 271 GLN n 
1 272 SER n 
1 273 ASN n 
1 274 TRP n 
1 275 SER n 
1 276 ASN n 
1 277 LEU n 
1 278 SER n 
1 279 LYS n 
1 280 ARG n 
1 281 THR n 
1 282 ASP n 
1 283 ARG n 
1 284 PRO n 
1 285 TYR n 
1 286 SER n 
1 287 PRO n 
1 288 PHE n 
1 289 LEU n 
1 290 LEU n 
1 291 PHE n 
1 292 HIS n 
1 293 GLY n 
1 294 THR n 
1 295 SER n 
1 296 ASP n 
1 297 ALA n 
1 298 ASN n 
1 299 LEU n 
1 300 TYR n 
1 301 GLU n 
1 302 LEU n 
1 303 LYS n 
1 304 ASN n 
1 305 GLN n 
1 306 LEU n 
1 307 PHE n 
1 308 ASN n 
1 309 GLU n 
1 310 ASP n 
1 311 LEU n 
1 312 ILE n 
1 313 PHE n 
1 314 THR n 
1 315 ASP n 
1 316 GLY n 
1 317 TYR n 
1 318 PRO n 
1 319 PHE n 
1 320 LYS n 
1 321 GLY n 
1 322 SER n 
1 323 VAL n 
1 324 PHE n 
1 325 THR n 
1 326 PRO n 
1 327 LYS n 
1 328 MET n 
1 329 LEU n 
1 330 ILE n 
1 331 GLU n 
1 332 GLY n 
1 333 PHE n 
1 334 SER n 
1 335 ASN n 
1 336 LYS n 
1 337 GLU n 
1 338 ILE n 
1 339 HIS n 
1 340 PHE n 
1 341 GLN n 
1 342 PHE n 
1 343 ILE n 
1 344 ASN n 
1 345 ASP n 
1 346 ILE n 
1 347 ASP n 
1 348 ASP n 
1 349 PHE n 
1 350 ASN n 
1 351 GLU n 
1 352 THR n 
1 353 LEU n 
1 354 ASN n 
1 355 SER n 
1 356 ILE n 
1 357 ASN n 
1 358 ILE n 
1 359 ARG n 
1 360 LYS n 
1 361 GLU n 
1 362 VAL n 
1 363 TYR n 
1 364 GLN n 
1 365 PHE n 
1 366 TYR n 
1 367 THR n 
1 368 GLU n 
1 369 ASN n 
1 370 CYS n 
1 371 LEU n 
1 372 ASP n 
1 373 ILE n 
1 374 PRO n 
1 375 SER n 
1 376 GLN n 
1 377 LEU n 
1 378 PRO n 
1 379 GLN n 
1 380 VAL n 
1 381 ASN n 
1 382 ILE n 
1 383 GLN n 
1 384 VAL n 
1 385 LYS n 
1 386 ASP n 
1 387 PHE n 
1 388 ALA n 
1 389 ASP n 
1 390 ILE n 
1 391 LYS n 
1 392 GLU n 
1 393 ILE n 
1 394 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                   394 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CG692_10945 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     562 
_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  
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   1   ?   ?   ?   A . n 
A 1 2   ASP 2   2   ?   ?   ?   A . n 
A 1 3   ARG 3   3   ?   ?   ?   A . n 
A 1 4   SER 4   4   4   SER SER A . n 
A 1 5   ALA 5   5   5   ALA ALA A . n 
A 1 6   VAL 6   6   6   VAL VAL A . n 
A 1 7   ASP 7   7   7   ASP ASP A . n 
A 1 8   THR 8   8   8   THR THR A . n 
A 1 9   ILE 9   9   9   ILE ILE A . n 
A 1 10  ARG 10  10  10  ARG ARG A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  TYR 12  12  12  TYR TYR A . n 
A 1 13  CYS 13  13  13  CYS CYS A . n 
A 1 14  TYR 14  14  14  TYR TYR A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  ASP 17  17  17  ASP ASP A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  THR 19  19  19  THR THR A . n 
A 1 20  ILE 20  20  20  ILE ILE A . n 
A 1 21  ILE 21  21  21  ILE ILE A . n 
A 1 22  GLU 22  22  22  GLU GLU A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  PHE 24  24  24  PHE PHE A . n 
A 1 25  SER 25  25  25  SER SER A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  PRO 27  27  27  PRO PRO A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  MET 29  29  29  MET MET A . n 
A 1 30  ASP 30  30  30  ASP ASP A . n 
A 1 31  ASP 31  31  31  ASP ASP A . n 
A 1 32  SER 32  32  32  SER SER A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  GLU 36  36  36  GLU GLU A . n 
A 1 37  CYS 37  37  37  CYS CYS A . n 
A 1 38  ILE 38  38  38  ILE ILE A . n 
A 1 39  GLU 39  39  39  GLU GLU A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  ASP 42  42  42  ASP ASP A . n 
A 1 43  VAL 43  43  43  VAL VAL A . n 
A 1 44  TYR 44  44  44  TYR TYR A . n 
A 1 45  ASN 45  45  45  ASN ASN A . n 
A 1 46  ASP 46  46  46  ASP ASP A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  HIS 48  48  48  HIS HIS A . n 
A 1 49  LEU 49  49  49  LEU LEU A . n 
A 1 50  THR 50  50  50  THR THR A . n 
A 1 51  ALA 51  51  51  ALA ALA A . n 
A 1 52  ILE 52  52  52  ILE ILE A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  CYS 54  54  54  CYS CYS A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  TYR 56  56  56  TYR TYR A . n 
A 1 57  TYR 57  57  57  TYR TYR A . n 
A 1 58  GLU 58  58  58  GLU GLU A . n 
A 1 59  SER 59  59  59  SER SER A . n 
A 1 60  THR 60  60  60  THR THR A . n 
A 1 61  ASP 61  61  61  ASP ASP A . n 
A 1 62  TYR 62  62  62  TYR TYR A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  VAL 66  66  66  VAL VAL A . n 
A 1 67  ILE 67  67  67  ILE ILE A . n 
A 1 68  SER 68  68  68  SER SER A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  PRO 70  70  70  PRO PRO A . n 
A 1 71  ILE 71  71  71  ILE ILE A . n 
A 1 72  ARG 72  72  72  ARG ARG A . n 
A 1 73  LEU 73  73  73  LEU LEU A . n 
A 1 74  MET 74  74  74  MET MET A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  SER 76  76  76  SER SER A . n 
A 1 77  HIS 77  77  77  HIS HIS A . n 
A 1 78  PHE 78  78  78  PHE PHE A . n 
A 1 79  LYS 79  79  79  LYS LYS A . n 
A 1 80  ASP 80  80  80  ASP ASP A . n 
A 1 81  ASN 81  81  81  ASN ASN A . n 
A 1 82  LYS 82  82  82  LYS LYS A . n 
A 1 83  GLU 83  83  83  GLU GLU A . n 
A 1 84  LYS 84  84  84  LYS LYS A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  ALA 86  86  86  ALA ALA A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  TYR 89  89  89  TYR TYR A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  TYR 91  91  91  TYR TYR A . n 
A 1 92  GLY 92  92  92  GLY GLY A . n 
A 1 93  HIS 93  93  93  HIS HIS A . n 
A 1 94  TYR 94  94  94  TYR TYR A . n 
A 1 95  LYS 95  95  95  LYS LYS A . n 
A 1 96  SER 96  96  96  SER SER A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  GLN 98  98  98  GLN GLN A . n 
A 1 99  GLU 99  99  99  GLU GLU A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 LEU 101 101 101 LEU LEU A . n 
A 1 102 THR 102 102 102 THR THR A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 PRO 104 104 104 PRO PRO A . n 
A 1 105 LEU 105 105 105 LEU LEU A . n 
A 1 106 LYS 106 106 106 LYS LYS A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 ASP 108 108 108 ASP ASP A . n 
A 1 109 PHE 109 109 109 PHE PHE A . n 
A 1 110 PHE 110 110 110 PHE PHE A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 SER 112 112 112 SER SER A . n 
A 1 113 ASN 113 113 113 ASN ASN A . n 
A 1 114 PHE 114 114 114 PHE PHE A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 THR 116 116 116 THR THR A . n 
A 1 117 TYR 117 117 117 TYR TYR A . n 
A 1 118 THR 118 118 118 THR THR A . n 
A 1 119 GLU 119 119 119 GLU GLU A . n 
A 1 120 LYS 120 120 120 LYS LYS A . n 
A 1 121 LYS 121 121 121 LYS LYS A . n 
A 1 122 ILE 122 122 122 ILE ILE A . n 
A 1 123 LYS 123 123 123 LYS LYS A . n 
A 1 124 HIS 124 124 124 HIS HIS A . n 
A 1 125 GLU 125 125 125 GLU GLU A . n 
A 1 126 TYR 126 126 126 TYR TYR A . n 
A 1 127 HIS 127 127 127 HIS HIS A . n 
A 1 128 ILE 128 128 128 ILE ILE A . n 
A 1 129 GLU 129 129 129 GLU GLU A . n 
A 1 130 ASN 130 130 130 ASN ASN A . n 
A 1 131 GLY 131 131 131 GLY GLY A . n 
A 1 132 LEU 132 132 132 LEU LEU A . n 
A 1 133 THR 133 133 133 THR THR A . n 
A 1 134 GLU 134 134 134 GLU GLU A . n 
A 1 135 GLU 135 135 135 GLU GLU A . n 
A 1 136 ASP 136 136 136 ASP ASP A . n 
A 1 137 LEU 137 137 137 LEU LEU A . n 
A 1 138 GLN 138 138 138 GLN GLN A . n 
A 1 139 ALA 139 139 139 ALA ALA A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 ASP 142 142 142 ASP ASP A . n 
A 1 143 ARG 143 143 143 ARG ARG A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 VAL 145 145 145 VAL VAL A . n 
A 1 146 ILE 146 146 146 ILE ILE A . n 
A 1 147 ASN 147 147 147 ASN ASN A . n 
A 1 148 ILE 148 148 148 ILE ILE A . n 
A 1 149 ASN 149 149 149 ASN ASN A . n 
A 1 150 ALA 150 150 150 ALA ALA A . n 
A 1 151 LYS 151 151 151 LYS LYS A . n 
A 1 152 SER 152 152 152 SER SER A . n 
A 1 153 PHE 153 153 153 PHE PHE A . n 
A 1 154 ASP 154 154 154 ASP ASP A . n 
A 1 155 ASP 155 155 155 ASP ASP A . n 
A 1 156 GLN 156 156 156 GLN GLN A . n 
A 1 157 LYS 157 157 157 LYS LYS A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 GLU 159 159 159 GLU GLU A . n 
A 1 160 THR 160 160 160 THR THR A . n 
A 1 161 ILE 161 161 161 ILE ILE A . n 
A 1 162 GLN 162 162 162 GLN GLN A . n 
A 1 163 ILE 163 163 163 ILE ILE A . n 
A 1 164 ILE 164 164 164 ILE ILE A . n 
A 1 165 LYS 165 165 165 LYS LYS A . n 
A 1 166 ASN 166 166 166 ASN ASN A . n 
A 1 167 HIS 167 167 167 HIS HIS A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 GLN 169 169 169 GLN GLN A . n 
A 1 170 CYS 170 170 170 CYS CYS A . n 
A 1 171 GLU 171 171 171 GLU GLU A . n 
A 1 172 ASP 172 172 172 ASP ASP A . n 
A 1 173 TYR 173 173 173 TYR TYR A . n 
A 1 174 GLU 174 174 174 GLU GLU A . n 
A 1 175 ALA 175 175 175 ALA ALA A . n 
A 1 176 GLU 176 176 176 GLU GLU A . n 
A 1 177 HIS 177 177 177 HIS HIS A . n 
A 1 178 TYR 178 178 178 TYR TYR A . n 
A 1 179 LEU 179 179 179 LEU LEU A . n 
A 1 180 TYR 180 180 180 TYR TYR A . n 
A 1 181 SER 181 181 181 SER SER A . n 
A 1 182 ASN 182 182 182 ASN ASN A . n 
A 1 183 ALA 183 183 183 ALA ALA A . n 
A 1 184 PHE 184 184 184 PHE PHE A . n 
A 1 185 ARG 185 185 185 ARG ARG A . n 
A 1 186 LYS 186 186 186 LYS LYS A . n 
A 1 187 THR 187 187 187 THR THR A . n 
A 1 188 TYR 188 188 188 TYR TYR A . n 
A 1 189 ASP 189 189 189 ASP ASP A . n 
A 1 190 ILE 190 190 190 ILE ILE A . n 
A 1 191 SER 191 191 191 SER SER A . n 
A 1 192 CYS 192 192 192 CYS CYS A . n 
A 1 193 ASN 193 193 193 ASN ASN A . n 
A 1 194 LYS 194 194 194 LYS LYS A . n 
A 1 195 LYS 195 195 195 LYS LYS A . n 
A 1 196 ASP 196 196 196 ASP ASP A . n 
A 1 197 ARG 197 197 197 ARG ARG A . n 
A 1 198 ARG 198 198 198 ARG ARG A . n 
A 1 199 ILE 199 199 199 ILE ILE A . n 
A 1 200 LYS 200 200 200 LYS LYS A . n 
A 1 201 LYS 201 201 201 LYS LYS A . n 
A 1 202 SER 202 202 202 SER SER A . n 
A 1 203 ASP 203 203 203 ASP ASP A . n 
A 1 204 PHE 204 204 204 PHE PHE A . n 
A 1 205 VAL 205 205 205 VAL VAL A . n 
A 1 206 GLU 206 206 206 GLU GLU A . n 
A 1 207 SER 207 207 207 SER SER A . n 
A 1 208 ILE 208 208 208 ILE ILE A . n 
A 1 209 ASN 209 209 209 ASN ASN A . n 
A 1 210 LYS 210 210 210 LYS LYS A . n 
A 1 211 SER 211 211 211 SER SER A . n 
A 1 212 LYS 212 212 212 LYS LYS A . n 
A 1 213 VAL 213 213 213 VAL VAL A . n 
A 1 214 LEU 214 214 214 LEU LEU A . n 
A 1 215 PHE 215 215 215 PHE PHE A . n 
A 1 216 ASN 216 216 216 ASN ASN A . n 
A 1 217 ILE 217 217 217 ILE ILE A . n 
A 1 218 TRP 218 218 218 TRP TRP A . n 
A 1 219 PHE 219 219 219 PHE PHE A . n 
A 1 220 TYR 220 220 220 TYR TYR A . n 
A 1 221 GLN 221 221 221 GLN GLN A . n 
A 1 222 TYR 222 222 222 TYR TYR A . n 
A 1 223 GLU 223 223 223 GLU GLU A . n 
A 1 224 GLY 224 224 224 GLY GLY A . n 
A 1 225 ARG 225 225 225 ARG ARG A . n 
A 1 226 LYS 226 226 226 LYS LYS A . n 
A 1 227 GLU 227 227 227 GLU GLU A . n 
A 1 228 TYR 228 228 228 TYR TYR A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 ARG 230 230 230 ARG ARG A . n 
A 1 231 LYS 231 231 231 LYS LYS A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 LYS 233 233 233 LYS LYS A . n 
A 1 234 GLU 234 234 234 GLU GLU A . n 
A 1 235 SER 235 235 235 SER SER A . n 
A 1 236 PHE 236 236 236 PHE PHE A . n 
A 1 237 ILE 237 237 237 ILE ILE A . n 
A 1 238 ARG 238 238 238 ARG ARG A . n 
A 1 239 ARG 239 239 239 ARG ARG A . n 
A 1 240 SER 240 240 240 SER SER A . n 
A 1 241 VAL 241 241 241 VAL VAL A . n 
A 1 242 ASN 242 242 242 ASN ASN A . n 
A 1 243 THR 243 243 243 THR THR A . n 
A 1 244 SER 244 244 244 SER SER A . n 
A 1 245 PRO 245 245 245 PRO PRO A . n 
A 1 246 TYR 246 246 246 TYR TYR A . n 
A 1 247 ALA 247 247 247 ALA ALA A . n 
A 1 248 ARG 248 248 248 ARG ARG A . n 
A 1 249 PHE 249 249 249 PHE PHE A . n 
A 1 250 PHE 250 250 250 PHE PHE A . n 
A 1 251 ILE 251 251 251 ILE ILE A . n 
A 1 252 LEU 252 252 252 LEU LEU A . n 
A 1 253 GLU 253 253 253 GLU GLU A . n 
A 1 254 PHE 254 254 254 PHE PHE A . n 
A 1 255 GLN 255 255 255 GLN GLN A . n 
A 1 256 ASP 256 256 256 ASP ASP A . n 
A 1 257 LYS 257 257 257 LYS LYS A . n 
A 1 258 THR 258 258 258 THR THR A . n 
A 1 259 ASP 259 259 259 ASP ASP A . n 
A 1 260 ILE 260 260 260 ILE ILE A . n 
A 1 261 LYS 261 261 261 LYS LYS A . n 
A 1 262 THR 262 262 262 THR THR A . n 
A 1 263 VAL 263 263 263 VAL VAL A . n 
A 1 264 LYS 264 264 264 LYS LYS A . n 
A 1 265 ASP 265 265 265 ASP ASP A . n 
A 1 266 CYS 266 266 266 CYS CYS A . n 
A 1 267 ILE 267 267 267 ILE ILE A . n 
A 1 268 TYR 268 268 268 TYR TYR A . n 
A 1 269 LYS 269 269 269 LYS LYS A . n 
A 1 270 ILE 270 270 270 ILE ILE A . n 
A 1 271 GLN 271 271 271 GLN GLN A . n 
A 1 272 SER 272 272 272 SER SER A . n 
A 1 273 ASN 273 273 273 ASN ASN A . n 
A 1 274 TRP 274 274 274 TRP TRP A . n 
A 1 275 SER 275 275 275 SER SER A . n 
A 1 276 ASN 276 276 276 ASN ASN A . n 
A 1 277 LEU 277 277 277 LEU LEU A . n 
A 1 278 SER 278 278 278 SER SER A . n 
A 1 279 LYS 279 279 279 LYS LYS A . n 
A 1 280 ARG 280 280 280 ARG ARG A . n 
A 1 281 THR 281 281 281 THR THR A . n 
A 1 282 ASP 282 282 282 ASP ASP A . n 
A 1 283 ARG 283 283 283 ARG ARG A . n 
A 1 284 PRO 284 284 284 PRO PRO A . n 
A 1 285 TYR 285 285 285 TYR TYR A . n 
A 1 286 SER 286 286 286 SER SER A . n 
A 1 287 PRO 287 287 287 PRO PRO A . n 
A 1 288 PHE 288 288 288 PHE PHE A . n 
A 1 289 LEU 289 289 289 LEU LEU A . n 
A 1 290 LEU 290 290 290 LEU LEU A . n 
A 1 291 PHE 291 291 291 PHE PHE A . n 
A 1 292 HIS 292 292 292 HIS HIS A . n 
A 1 293 GLY 293 293 293 GLY GLY A . n 
A 1 294 THR 294 294 294 THR THR A . n 
A 1 295 SER 295 295 295 SER SER A . n 
A 1 296 ASP 296 296 296 ASP ASP A . n 
A 1 297 ALA 297 297 297 ALA ALA A . n 
A 1 298 ASN 298 298 298 ASN ASN A . n 
A 1 299 LEU 299 299 299 LEU LEU A . n 
A 1 300 TYR 300 300 300 TYR TYR A . n 
A 1 301 GLU 301 301 301 GLU GLU A . n 
A 1 302 LEU 302 302 302 LEU LEU A . n 
A 1 303 LYS 303 303 303 LYS LYS A . n 
A 1 304 ASN 304 304 304 ASN ASN A . n 
A 1 305 GLN 305 305 305 GLN GLN A . n 
A 1 306 LEU 306 306 306 LEU LEU A . n 
A 1 307 PHE 307 307 307 PHE PHE A . n 
A 1 308 ASN 308 308 308 ASN ASN A . n 
A 1 309 GLU 309 309 309 GLU GLU A . n 
A 1 310 ASP 310 310 310 ASP ASP A . n 
A 1 311 LEU 311 311 311 LEU LEU A . n 
A 1 312 ILE 312 312 312 ILE ILE A . n 
A 1 313 PHE 313 313 313 PHE PHE A . n 
A 1 314 THR 314 314 314 THR THR A . n 
A 1 315 ASP 315 315 315 ASP ASP A . n 
A 1 316 GLY 316 316 316 GLY GLY A . n 
A 1 317 TYR 317 317 317 TYR TYR A . n 
A 1 318 PRO 318 318 318 PRO PRO A . n 
A 1 319 PHE 319 319 319 PHE PHE A . n 
A 1 320 LYS 320 320 320 LYS LYS A . n 
A 1 321 GLY 321 321 321 GLY GLY A . n 
A 1 322 SER 322 322 322 SER SER A . n 
A 1 323 VAL 323 323 323 VAL VAL A . n 
A 1 324 PHE 324 324 324 PHE PHE A . n 
A 1 325 THR 325 325 325 THR THR A . n 
A 1 326 PRO 326 326 326 PRO PRO A . n 
A 1 327 LYS 327 327 327 LYS LYS A . n 
A 1 328 MET 328 328 328 MET MET A . n 
A 1 329 LEU 329 329 329 LEU LEU A . n 
A 1 330 ILE 330 330 330 ILE ILE A . n 
A 1 331 GLU 331 331 331 GLU GLU A . n 
A 1 332 GLY 332 332 332 GLY GLY A . n 
A 1 333 PHE 333 333 333 PHE PHE A . n 
A 1 334 SER 334 334 334 SER SER A . n 
A 1 335 ASN 335 335 335 ASN ASN A . n 
A 1 336 LYS 336 336 336 LYS LYS A . n 
A 1 337 GLU 337 337 337 GLU GLU A . n 
A 1 338 ILE 338 338 338 ILE ILE A . n 
A 1 339 HIS 339 339 339 HIS HIS A . n 
A 1 340 PHE 340 340 340 PHE PHE A . n 
A 1 341 GLN 341 341 341 GLN GLN A . n 
A 1 342 PHE 342 342 342 PHE PHE A . n 
A 1 343 ILE 343 343 343 ILE ILE A . n 
A 1 344 ASN 344 344 344 ASN ASN A . n 
A 1 345 ASP 345 345 345 ASP ASP A . n 
A 1 346 ILE 346 346 346 ILE ILE A . n 
A 1 347 ASP 347 347 347 ASP ASP A . n 
A 1 348 ASP 348 348 348 ASP ASP A . n 
A 1 349 PHE 349 349 349 PHE PHE A . n 
A 1 350 ASN 350 350 350 ASN ASN A . n 
A 1 351 GLU 351 351 351 GLU GLU A . n 
A 1 352 THR 352 352 352 THR THR A . n 
A 1 353 LEU 353 353 353 LEU LEU A . n 
A 1 354 ASN 354 354 354 ASN ASN A . n 
A 1 355 SER 355 355 355 SER SER A . n 
A 1 356 ILE 356 356 356 ILE ILE A . n 
A 1 357 ASN 357 357 357 ASN ASN A . n 
A 1 358 ILE 358 358 358 ILE ILE A . n 
A 1 359 ARG 359 359 359 ARG ARG A . n 
A 1 360 LYS 360 360 360 LYS LYS A . n 
A 1 361 GLU 361 361 361 GLU GLU A . n 
A 1 362 VAL 362 362 362 VAL VAL A . n 
A 1 363 TYR 363 363 363 TYR TYR A . n 
A 1 364 GLN 364 364 364 GLN GLN A . n 
A 1 365 PHE 365 365 365 PHE PHE A . n 
A 1 366 TYR 366 366 366 TYR TYR A . n 
A 1 367 THR 367 367 367 THR THR A . n 
A 1 368 GLU 368 368 368 GLU GLU A . n 
A 1 369 ASN 369 369 369 ASN ASN A . n 
A 1 370 CYS 370 370 370 CYS CYS A . n 
A 1 371 LEU 371 371 371 LEU LEU A . n 
A 1 372 ASP 372 372 372 ASP ASP A . n 
A 1 373 ILE 373 373 373 ILE ILE A . n 
A 1 374 PRO 374 374 374 PRO PRO A . n 
A 1 375 SER 375 375 375 SER SER A . n 
A 1 376 GLN 376 376 376 GLN GLN A . n 
A 1 377 LEU 377 377 377 LEU LEU A . n 
A 1 378 PRO 378 378 378 PRO PRO A . n 
A 1 379 GLN 379 379 379 GLN GLN A . n 
A 1 380 VAL 380 380 380 VAL VAL A . n 
A 1 381 ASN 381 381 381 ASN ASN A . n 
A 1 382 ILE 382 382 382 ILE ILE A . n 
A 1 383 GLN 383 383 383 GLN GLN A . n 
A 1 384 VAL 384 384 384 VAL VAL A . n 
A 1 385 LYS 385 385 385 LYS LYS A . n 
A 1 386 ASP 386 386 386 ASP ASP A . n 
A 1 387 PHE 387 387 387 PHE PHE A . n 
A 1 388 ALA 388 388 388 ALA ALA A . n 
A 1 389 ASP 389 389 389 ASP ASP A . n 
A 1 390 ILE 390 390 390 ILE ILE A . n 
A 1 391 LYS 391 391 391 LYS LYS A . n 
A 1 392 GLU 392 392 392 GLU GLU A . n 
A 1 393 ILE 393 393 393 ILE ILE A . n 
A 1 394 VAL 394 394 394 VAL VAL A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   ASP 2   2   ?   ?   ?   B . n 
B 1 3   ARG 3   3   ?   ?   ?   B . n 
B 1 4   SER 4   4   4   SER SER B . n 
B 1 5   ALA 5   5   5   ALA ALA B . n 
B 1 6   VAL 6   6   6   VAL VAL B . n 
B 1 7   ASP 7   7   7   ASP ASP B . n 
B 1 8   THR 8   8   8   THR THR B . n 
B 1 9   ILE 9   9   9   ILE ILE B . n 
B 1 10  ARG 10  10  10  ARG ARG B . n 
B 1 11  GLY 11  11  11  GLY GLY B . n 
B 1 12  TYR 12  12  12  TYR TYR B . n 
B 1 13  CYS 13  13  13  CYS CYS B . n 
B 1 14  TYR 14  14  14  TYR TYR B . n 
B 1 15  GLN 15  15  15  GLN GLN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  ASP 17  17  17  ASP ASP B . n 
B 1 18  LYS 18  18  18  LYS LYS B . n 
B 1 19  THR 19  19  19  THR THR B . n 
B 1 20  ILE 20  20  20  ILE ILE B . n 
B 1 21  ILE 21  21  21  ILE ILE B . n 
B 1 22  GLU 22  22  22  GLU GLU B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  PHE 24  24  24  PHE PHE B . n 
B 1 25  SER 25  25  25  SER SER B . n 
B 1 26  LEU 26  26  26  LEU LEU B . n 
B 1 27  PRO 27  27  27  PRO PRO B . n 
B 1 28  GLN 28  28  28  GLN GLN B . n 
B 1 29  MET 29  29  29  MET MET B . n 
B 1 30  ASP 30  30  30  ASP ASP B . n 
B 1 31  ASP 31  31  31  ASP ASP B . n 
B 1 32  SER 32  32  32  SER SER B . n 
B 1 33  ILE 33  33  33  ILE ILE B . n 
B 1 34  ASP 34  34  34  ASP ASP B . n 
B 1 35  ILE 35  35  35  ILE ILE B . n 
B 1 36  GLU 36  36  36  GLU GLU B . n 
B 1 37  CYS 37  37  37  CYS CYS B . n 
B 1 38  ILE 38  38  38  ILE ILE B . n 
B 1 39  GLU 39  39  39  GLU GLU B . n 
B 1 40  ASP 40  40  40  ASP ASP B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  ASP 42  42  42  ASP ASP B . n 
B 1 43  VAL 43  43  43  VAL VAL B . n 
B 1 44  TYR 44  44  44  TYR TYR B . n 
B 1 45  ASN 45  45  45  ASN ASN B . n 
B 1 46  ASP 46  46  46  ASP ASP B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  HIS 48  48  48  HIS HIS B . n 
B 1 49  LEU 49  49  49  LEU LEU B . n 
B 1 50  THR 50  50  50  THR THR B . n 
B 1 51  ALA 51  51  51  ALA ALA B . n 
B 1 52  ILE 52  52  52  ILE ILE B . n 
B 1 53  GLN 53  53  53  GLN GLN B . n 
B 1 54  CYS 54  54  54  CYS CYS B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  TYR 56  56  56  TYR TYR B . n 
B 1 57  TYR 57  57  57  TYR TYR B . n 
B 1 58  GLU 58  58  58  GLU GLU B . n 
B 1 59  SER 59  59  59  SER SER B . n 
B 1 60  THR 60  60  60  THR THR B . n 
B 1 61  ASP 61  61  61  ASP ASP B . n 
B 1 62  TYR 62  62  62  TYR TYR B . n 
B 1 63  ASN 63  63  63  ASN ASN B . n 
B 1 64  HIS 64  64  64  HIS HIS B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  VAL 66  66  66  VAL VAL B . n 
B 1 67  ILE 67  67  67  ILE ILE B . n 
B 1 68  SER 68  68  68  SER SER B . n 
B 1 69  LYS 69  69  69  LYS LYS B . n 
B 1 70  PRO 70  70  70  PRO PRO B . n 
B 1 71  ILE 71  71  71  ILE ILE B . n 
B 1 72  ARG 72  72  72  ARG ARG B . n 
B 1 73  LEU 73  73  73  LEU LEU B . n 
B 1 74  MET 74  74  74  MET MET B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  SER 76  76  76  SER SER B . n 
B 1 77  HIS 77  77  77  HIS HIS B . n 
B 1 78  PHE 78  78  78  PHE PHE B . n 
B 1 79  LYS 79  79  79  LYS LYS B . n 
B 1 80  ASP 80  80  80  ASP ASP B . n 
B 1 81  ASN 81  81  81  ASN ASN B . n 
B 1 82  LYS 82  82  82  LYS LYS B . n 
B 1 83  GLU 83  83  83  GLU GLU B . n 
B 1 84  LYS 84  84  84  LYS LYS B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  ALA 86  86  86  ALA ALA B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  TYR 88  88  88  TYR TYR B . n 
B 1 89  TYR 89  89  89  TYR TYR B . n 
B 1 90  LEU 90  90  90  LEU LEU B . n 
B 1 91  TYR 91  91  91  TYR TYR B . n 
B 1 92  GLY 92  92  92  GLY GLY B . n 
B 1 93  HIS 93  93  93  HIS HIS B . n 
B 1 94  TYR 94  94  94  TYR TYR B . n 
B 1 95  LYS 95  95  95  LYS LYS B . n 
B 1 96  SER 96  96  96  SER SER B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  GLN 98  98  98  GLN GLN B . n 
B 1 99  GLU 99  99  99  GLU GLU B . n 
B 1 100 LYS 100 100 100 LYS LYS B . n 
B 1 101 LEU 101 101 101 LEU LEU B . n 
B 1 102 THR 102 102 102 THR THR B . n 
B 1 103 LEU 103 103 103 LEU LEU B . n 
B 1 104 PRO 104 104 104 PRO PRO B . n 
B 1 105 LEU 105 105 105 LEU LEU B . n 
B 1 106 LYS 106 106 106 LYS LYS B . n 
B 1 107 VAL 107 107 107 VAL VAL B . n 
B 1 108 ASP 108 108 108 ASP ASP B . n 
B 1 109 PHE 109 109 109 PHE PHE B . n 
B 1 110 PHE 110 110 110 PHE PHE B . n 
B 1 111 LYS 111 111 111 LYS LYS B . n 
B 1 112 SER 112 112 112 SER SER B . n 
B 1 113 ASN 113 113 113 ASN ASN B . n 
B 1 114 PHE 114 114 114 PHE PHE B . n 
B 1 115 LEU 115 115 115 LEU LEU B . n 
B 1 116 THR 116 116 116 THR THR B . n 
B 1 117 TYR 117 117 117 TYR TYR B . n 
B 1 118 THR 118 118 118 THR THR B . n 
B 1 119 GLU 119 119 119 GLU GLU B . n 
B 1 120 LYS 120 120 120 LYS LYS B . n 
B 1 121 LYS 121 121 121 LYS LYS B . n 
B 1 122 ILE 122 122 122 ILE ILE B . n 
B 1 123 LYS 123 123 123 LYS LYS B . n 
B 1 124 HIS 124 124 124 HIS HIS B . n 
B 1 125 GLU 125 125 125 GLU GLU B . n 
B 1 126 TYR 126 126 126 TYR TYR B . n 
B 1 127 HIS 127 127 127 HIS HIS B . n 
B 1 128 ILE 128 128 128 ILE ILE B . n 
B 1 129 GLU 129 129 129 GLU GLU B . n 
B 1 130 ASN 130 130 130 ASN ASN B . n 
B 1 131 GLY 131 131 131 GLY GLY B . n 
B 1 132 LEU 132 132 132 LEU LEU B . n 
B 1 133 THR 133 133 133 THR THR B . n 
B 1 134 GLU 134 134 134 GLU GLU B . n 
B 1 135 GLU 135 135 135 GLU GLU B . n 
B 1 136 ASP 136 136 136 ASP ASP B . n 
B 1 137 LEU 137 137 137 LEU LEU B . n 
B 1 138 GLN 138 138 138 GLN GLN B . n 
B 1 139 ALA 139 139 139 ALA ALA B . n 
B 1 140 PHE 140 140 140 PHE PHE B . n 
B 1 141 LEU 141 141 141 LEU LEU B . n 
B 1 142 ASP 142 142 142 ASP ASP B . n 
B 1 143 ARG 143 143 143 ARG ARG B . n 
B 1 144 LEU 144 144 144 LEU LEU B . n 
B 1 145 VAL 145 145 145 VAL VAL B . n 
B 1 146 ILE 146 146 146 ILE ILE B . n 
B 1 147 ASN 147 147 147 ASN ASN B . n 
B 1 148 ILE 148 148 148 ILE ILE B . n 
B 1 149 ASN 149 149 149 ASN ASN B . n 
B 1 150 ALA 150 150 150 ALA ALA B . n 
B 1 151 LYS 151 151 151 LYS LYS B . n 
B 1 152 SER 152 152 152 SER SER B . n 
B 1 153 PHE 153 153 153 PHE PHE B . n 
B 1 154 ASP 154 154 154 ASP ASP B . n 
B 1 155 ASP 155 155 155 ASP ASP B . n 
B 1 156 GLN 156 156 156 GLN GLN B . n 
B 1 157 LYS 157 157 157 LYS LYS B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 GLU 159 159 159 GLU GLU B . n 
B 1 160 THR 160 160 160 THR THR B . n 
B 1 161 ILE 161 161 161 ILE ILE B . n 
B 1 162 GLN 162 162 162 GLN GLN B . n 
B 1 163 ILE 163 163 163 ILE ILE B . n 
B 1 164 ILE 164 164 164 ILE ILE B . n 
B 1 165 LYS 165 165 165 LYS LYS B . n 
B 1 166 ASN 166 166 166 ASN ASN B . n 
B 1 167 HIS 167 167 167 HIS HIS B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 GLN 169 169 169 GLN GLN B . n 
B 1 170 CYS 170 170 170 CYS CYS B . n 
B 1 171 GLU 171 171 171 GLU GLU B . n 
B 1 172 ASP 172 172 172 ASP ASP B . n 
B 1 173 TYR 173 173 173 TYR TYR B . n 
B 1 174 GLU 174 174 174 GLU GLU B . n 
B 1 175 ALA 175 175 175 ALA ALA B . n 
B 1 176 GLU 176 176 176 GLU GLU B . n 
B 1 177 HIS 177 177 177 HIS HIS B . n 
B 1 178 TYR 178 178 178 TYR TYR B . n 
B 1 179 LEU 179 179 179 LEU LEU B . n 
B 1 180 TYR 180 180 180 TYR TYR B . n 
B 1 181 SER 181 181 181 SER SER B . n 
B 1 182 ASN 182 182 182 ASN ASN B . n 
B 1 183 ALA 183 183 183 ALA ALA B . n 
B 1 184 PHE 184 184 184 PHE PHE B . n 
B 1 185 ARG 185 185 185 ARG ARG B . n 
B 1 186 LYS 186 186 186 LYS LYS B . n 
B 1 187 THR 187 187 187 THR THR B . n 
B 1 188 TYR 188 188 188 TYR TYR B . n 
B 1 189 ASP 189 189 189 ASP ASP B . n 
B 1 190 ILE 190 190 190 ILE ILE B . n 
B 1 191 SER 191 191 191 SER SER B . n 
B 1 192 CYS 192 192 192 CYS CYS B . n 
B 1 193 ASN 193 193 193 ASN ASN B . n 
B 1 194 LYS 194 194 194 LYS LYS B . n 
B 1 195 LYS 195 195 195 LYS LYS B . n 
B 1 196 ASP 196 196 196 ASP ASP B . n 
B 1 197 ARG 197 197 197 ARG ARG B . n 
B 1 198 ARG 198 198 198 ARG ARG B . n 
B 1 199 ILE 199 199 199 ILE ILE B . n 
B 1 200 LYS 200 200 200 LYS LYS B . n 
B 1 201 LYS 201 201 201 LYS LYS B . n 
B 1 202 SER 202 202 202 SER SER B . n 
B 1 203 ASP 203 203 203 ASP ASP B . n 
B 1 204 PHE 204 204 204 PHE PHE B . n 
B 1 205 VAL 205 205 205 VAL VAL B . n 
B 1 206 GLU 206 206 206 GLU GLU B . n 
B 1 207 SER 207 207 207 SER SER B . n 
B 1 208 ILE 208 208 208 ILE ILE B . n 
B 1 209 ASN 209 209 209 ASN ASN B . n 
B 1 210 LYS 210 210 210 LYS LYS B . n 
B 1 211 SER 211 211 211 SER SER B . n 
B 1 212 LYS 212 212 212 LYS LYS B . n 
B 1 213 VAL 213 213 213 VAL VAL B . n 
B 1 214 LEU 214 214 214 LEU LEU B . n 
B 1 215 PHE 215 215 215 PHE PHE B . n 
B 1 216 ASN 216 216 216 ASN ASN B . n 
B 1 217 ILE 217 217 217 ILE ILE B . n 
B 1 218 TRP 218 218 218 TRP TRP B . n 
B 1 219 PHE 219 219 219 PHE PHE B . n 
B 1 220 TYR 220 220 220 TYR TYR B . n 
B 1 221 GLN 221 221 221 GLN GLN B . n 
B 1 222 TYR 222 222 222 TYR TYR B . n 
B 1 223 GLU 223 223 223 GLU GLU B . n 
B 1 224 GLY 224 224 224 GLY GLY B . n 
B 1 225 ARG 225 225 225 ARG ARG B . n 
B 1 226 LYS 226 226 226 LYS LYS B . n 
B 1 227 GLU 227 227 227 GLU GLU B . n 
B 1 228 TYR 228 228 228 TYR TYR B . n 
B 1 229 LEU 229 229 229 LEU LEU B . n 
B 1 230 ARG 230 230 230 ARG ARG B . n 
B 1 231 LYS 231 231 231 LYS LYS B . n 
B 1 232 LEU 232 232 232 LEU LEU B . n 
B 1 233 LYS 233 233 233 LYS LYS B . n 
B 1 234 GLU 234 234 234 GLU GLU B . n 
B 1 235 SER 235 235 235 SER SER B . n 
B 1 236 PHE 236 236 236 PHE PHE B . n 
B 1 237 ILE 237 237 237 ILE ILE B . n 
B 1 238 ARG 238 238 238 ARG ARG B . n 
B 1 239 ARG 239 239 239 ARG ARG B . n 
B 1 240 SER 240 240 240 SER SER B . n 
B 1 241 VAL 241 241 241 VAL VAL B . n 
B 1 242 ASN 242 242 242 ASN ASN B . n 
B 1 243 THR 243 243 243 THR THR B . n 
B 1 244 SER 244 244 244 SER SER B . n 
B 1 245 PRO 245 245 245 PRO PRO B . n 
B 1 246 TYR 246 246 246 TYR TYR B . n 
B 1 247 ALA 247 247 247 ALA ALA B . n 
B 1 248 ARG 248 248 248 ARG ARG B . n 
B 1 249 PHE 249 249 249 PHE PHE B . n 
B 1 250 PHE 250 250 250 PHE PHE B . n 
B 1 251 ILE 251 251 251 ILE ILE B . n 
B 1 252 LEU 252 252 252 LEU LEU B . n 
B 1 253 GLU 253 253 253 GLU GLU B . n 
B 1 254 PHE 254 254 254 PHE PHE B . n 
B 1 255 GLN 255 255 255 GLN GLN B . n 
B 1 256 ASP 256 256 256 ASP ASP B . n 
B 1 257 LYS 257 257 257 LYS LYS B . n 
B 1 258 THR 258 258 258 THR THR B . n 
B 1 259 ASP 259 259 259 ASP ASP B . n 
B 1 260 ILE 260 260 260 ILE ILE B . n 
B 1 261 LYS 261 261 261 LYS LYS B . n 
B 1 262 THR 262 262 262 THR THR B . n 
B 1 263 VAL 263 263 263 VAL VAL B . n 
B 1 264 LYS 264 264 264 LYS LYS B . n 
B 1 265 ASP 265 265 265 ASP ASP B . n 
B 1 266 CYS 266 266 266 CYS CYS B . n 
B 1 267 ILE 267 267 267 ILE ILE B . n 
B 1 268 TYR 268 268 268 TYR TYR B . n 
B 1 269 LYS 269 269 269 LYS LYS B . n 
B 1 270 ILE 270 270 270 ILE ILE B . n 
B 1 271 GLN 271 271 271 GLN GLN B . n 
B 1 272 SER 272 272 272 SER SER B . n 
B 1 273 ASN 273 273 273 ASN ASN B . n 
B 1 274 TRP 274 274 274 TRP TRP B . n 
B 1 275 SER 275 275 275 SER SER B . n 
B 1 276 ASN 276 276 276 ASN ASN B . n 
B 1 277 LEU 277 277 277 LEU LEU B . n 
B 1 278 SER 278 278 278 SER SER B . n 
B 1 279 LYS 279 279 279 LYS LYS B . n 
B 1 280 ARG 280 280 280 ARG ARG B . n 
B 1 281 THR 281 281 281 THR THR B . n 
B 1 282 ASP 282 282 282 ASP ASP B . n 
B 1 283 ARG 283 283 283 ARG ARG B . n 
B 1 284 PRO 284 284 284 PRO PRO B . n 
B 1 285 TYR 285 285 285 TYR TYR B . n 
B 1 286 SER 286 286 286 SER SER B . n 
B 1 287 PRO 287 287 287 PRO PRO B . n 
B 1 288 PHE 288 288 288 PHE PHE B . n 
B 1 289 LEU 289 289 289 LEU LEU B . n 
B 1 290 LEU 290 290 290 LEU LEU B . n 
B 1 291 PHE 291 291 291 PHE PHE B . n 
B 1 292 HIS 292 292 292 HIS HIS B . n 
B 1 293 GLY 293 293 293 GLY GLY B . n 
B 1 294 THR 294 294 294 THR THR B . n 
B 1 295 SER 295 295 295 SER SER B . n 
B 1 296 ASP 296 296 296 ASP ASP B . n 
B 1 297 ALA 297 297 297 ALA ALA B . n 
B 1 298 ASN 298 298 298 ASN ASN B . n 
B 1 299 LEU 299 299 299 LEU LEU B . n 
B 1 300 TYR 300 300 300 TYR TYR B . n 
B 1 301 GLU 301 301 301 GLU GLU B . n 
B 1 302 LEU 302 302 302 LEU LEU B . n 
B 1 303 LYS 303 303 303 LYS LYS B . n 
B 1 304 ASN 304 304 304 ASN ASN B . n 
B 1 305 GLN 305 305 305 GLN GLN B . n 
B 1 306 LEU 306 306 306 LEU LEU B . n 
B 1 307 PHE 307 307 307 PHE PHE B . n 
B 1 308 ASN 308 308 308 ASN ASN B . n 
B 1 309 GLU 309 309 309 GLU GLU B . n 
B 1 310 ASP 310 310 310 ASP ASP B . n 
B 1 311 LEU 311 311 311 LEU LEU B . n 
B 1 312 ILE 312 312 312 ILE ILE B . n 
B 1 313 PHE 313 313 313 PHE PHE B . n 
B 1 314 THR 314 314 314 THR THR B . n 
B 1 315 ASP 315 315 315 ASP ASP B . n 
B 1 316 GLY 316 316 316 GLY GLY B . n 
B 1 317 TYR 317 317 317 TYR TYR B . n 
B 1 318 PRO 318 318 318 PRO PRO B . n 
B 1 319 PHE 319 319 319 PHE PHE B . n 
B 1 320 LYS 320 320 320 LYS LYS B . n 
B 1 321 GLY 321 321 321 GLY GLY B . n 
B 1 322 SER 322 322 322 SER SER B . n 
B 1 323 VAL 323 323 323 VAL VAL B . n 
B 1 324 PHE 324 324 324 PHE PHE B . n 
B 1 325 THR 325 325 325 THR THR B . n 
B 1 326 PRO 326 326 326 PRO PRO B . n 
B 1 327 LYS 327 327 327 LYS LYS B . n 
B 1 328 MET 328 328 328 MET MET B . n 
B 1 329 LEU 329 329 329 LEU LEU B . n 
B 1 330 ILE 330 330 330 ILE ILE B . n 
B 1 331 GLU 331 331 331 GLU GLU B . n 
B 1 332 GLY 332 332 332 GLY GLY B . n 
B 1 333 PHE 333 333 333 PHE PHE B . n 
B 1 334 SER 334 334 334 SER SER B . n 
B 1 335 ASN 335 335 335 ASN ASN B . n 
B 1 336 LYS 336 336 336 LYS LYS B . n 
B 1 337 GLU 337 337 337 GLU GLU B . n 
B 1 338 ILE 338 338 338 ILE ILE B . n 
B 1 339 HIS 339 339 339 HIS HIS B . n 
B 1 340 PHE 340 340 340 PHE PHE B . n 
B 1 341 GLN 341 341 341 GLN GLN B . n 
B 1 342 PHE 342 342 342 PHE PHE B . n 
B 1 343 ILE 343 343 343 ILE ILE B . n 
B 1 344 ASN 344 344 344 ASN ASN B . n 
B 1 345 ASP 345 345 345 ASP ASP B . n 
B 1 346 ILE 346 346 346 ILE ILE B . n 
B 1 347 ASP 347 347 347 ASP ASP B . n 
B 1 348 ASP 348 348 348 ASP ASP B . n 
B 1 349 PHE 349 349 349 PHE PHE B . n 
B 1 350 ASN 350 350 350 ASN ASN B . n 
B 1 351 GLU 351 351 351 GLU GLU B . n 
B 1 352 THR 352 352 352 THR THR B . n 
B 1 353 LEU 353 353 353 LEU LEU B . n 
B 1 354 ASN 354 354 354 ASN ASN B . n 
B 1 355 SER 355 355 355 SER SER B . n 
B 1 356 ILE 356 356 356 ILE ILE B . n 
B 1 357 ASN 357 357 357 ASN ASN B . n 
B 1 358 ILE 358 358 358 ILE ILE B . n 
B 1 359 ARG 359 359 359 ARG ARG B . n 
B 1 360 LYS 360 360 360 LYS LYS B . n 
B 1 361 GLU 361 361 361 GLU GLU B . n 
B 1 362 VAL 362 362 362 VAL VAL B . n 
B 1 363 TYR 363 363 363 TYR TYR B . n 
B 1 364 GLN 364 364 364 GLN GLN B . n 
B 1 365 PHE 365 365 365 PHE PHE B . n 
B 1 366 TYR 366 366 366 TYR TYR B . n 
B 1 367 THR 367 367 367 THR THR B . n 
B 1 368 GLU 368 368 368 GLU GLU B . n 
B 1 369 ASN 369 369 369 ASN ASN B . n 
B 1 370 CYS 370 370 370 CYS CYS B . n 
B 1 371 LEU 371 371 371 LEU LEU B . n 
B 1 372 ASP 372 372 372 ASP ASP B . n 
B 1 373 ILE 373 373 373 ILE ILE B . n 
B 1 374 PRO 374 374 374 PRO PRO B . n 
B 1 375 SER 375 375 375 SER SER B . n 
B 1 376 GLN 376 376 376 GLN GLN B . n 
B 1 377 LEU 377 377 377 LEU LEU B . n 
B 1 378 PRO 378 378 378 PRO PRO B . n 
B 1 379 GLN 379 379 379 GLN GLN B . n 
B 1 380 VAL 380 380 380 VAL VAL B . n 
B 1 381 ASN 381 381 381 ASN ASN B . n 
B 1 382 ILE 382 382 382 ILE ILE B . n 
B 1 383 GLN 383 383 383 GLN GLN B . n 
B 1 384 VAL 384 384 384 VAL VAL B . n 
B 1 385 LYS 385 385 385 LYS LYS B . n 
B 1 386 ASP 386 386 386 ASP ASP B . n 
B 1 387 PHE 387 387 387 PHE PHE B . n 
B 1 388 ALA 388 388 388 ALA ALA B . n 
B 1 389 ASP 389 389 389 ASP ASP B . n 
B 1 390 ILE 390 390 390 ILE ILE B . n 
B 1 391 LYS 391 391 391 LYS LYS B . n 
B 1 392 GLU 392 392 392 GLU GLU B . n 
B 1 393 ILE 393 393 393 ILE ILE B . n 
B 1 394 VAL 394 394 394 VAL VAL B . n 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.15.2_3472: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8ZGI 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     144.296 
_cell.length_a_esd                 ? 
_cell.length_b                     144.296 
_cell.length_b_esd                 ? 
_cell.length_c                     262.742 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        24 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8ZGI 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                178 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 61 2 2' 
_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                   8ZGI 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             4.20 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          70.73 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;800 mM Sodium phosphate monobasic
1200 mM Potassium phosphate dibasic
100 mM Sodium acetate pH 4.5
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-11-18 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97915 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97915 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          108.33 
_reflns.entry_id                                       8ZGI 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.2 
_reflns.d_resolution_low                               50 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     27392 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                38.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.99 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    3.2 
_reflns_shell.d_res_low                                     3.39 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4282 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.546 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8ZGI 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            3.200 
_refine.ls_d_res_low                             22.311 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     27274 
_refine.ls_number_reflns_R_free                  997 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.93 
_refine.ls_percent_reflns_R_free                 3.66 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2839 
_refine.ls_R_factor_R_free                       0.3219 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2826 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 33.39 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.43 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       3.200 
_refine_hist.d_res_low                        22.311 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               6575 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        6575 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.002 ? 6729 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.455 ? 9072 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 4.685 ? 4051 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.039 ? 962  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.002 ? 1167 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 3.2004 3.3686 . . 139 3666 100.00 . . . . 0.3386 . . . . . . . . . . . 0.3496 
'X-RAY DIFFRACTION' 3.3686 3.5789 . . 139 3663 100.00 . . . . 0.3216 . . . . . . . . . . . 0.3778 
'X-RAY DIFFRACTION' 3.5789 3.8539 . . 139 3693 100.00 . . . . 0.3108 . . . . . . . . . . . 0.3279 
'X-RAY DIFFRACTION' 3.8539 4.2393 . . 142 3727 100.00 . . . . 0.2874 . . . . . . . . . . . 0.3737 
'X-RAY DIFFRACTION' 4.2393 4.8473 . . 141 3739 100.00 . . . . 0.2660 . . . . . . . . . . . 0.3205 
'X-RAY DIFFRACTION' 4.8473 6.0865 . . 144 3797 100.00 . . . . 0.2864 . . . . . . . . . . . 0.3269 
'X-RAY DIFFRACTION' 6.0865 22.311 . . 153 3992 100.00 . . . . 0.2644 . . . . . . . . . . . 0.2835 
# 
_struct.entry_id                     8ZGI 
_struct.title                        'Crystal structure of DUF4297 from E.Coli' 
_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        8ZGI 
_struct_keywords.text            'Nuclease, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    8ZGI 
_struct_ref.pdbx_db_accession          8ZGI 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8ZGI A 1 ? 394 ? 8ZGI 1 ? 394 ? 1 394 
2 1 8ZGI B 1 ? 394 ? 8ZGI 1 ? 394 ? 1 394 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1400  ? 
1 MORE         -11   ? 
1 'SSA (A^2)'  40620 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ALA A 5   ? CYS A 13  ? ALA A 5   CYS A 13  1 ? 9  
HELX_P HELX_P2  AA2 CYS A 13  ? SER A 25  ? CYS A 13  SER A 25  1 ? 13 
HELX_P HELX_P3  AA3 ILE A 67  ? ASN A 81  ? ILE A 67  ASN A 81  1 ? 15 
HELX_P HELX_P4  AA4 GLY A 97  ? LEU A 101 ? GLY A 97  LEU A 101 5 ? 5  
HELX_P HELX_P5  AA5 LYS A 106 ? PHE A 114 ? LYS A 106 PHE A 114 1 ? 9  
HELX_P HELX_P6  AA6 THR A 133 ? ARG A 143 ? THR A 133 ARG A 143 1 ? 11 
HELX_P HELX_P7  AA7 SER A 152 ? GLN A 169 ? SER A 152 GLN A 169 1 ? 18 
HELX_P HELX_P8  AA8 GLU A 171 ? GLU A 176 ? GLU A 171 GLU A 176 1 ? 6  
HELX_P HELX_P9  AA9 TYR A 178 ? ASN A 193 ? TYR A 178 ASN A 193 1 ? 16 
HELX_P HELX_P10 AB1 LYS A 200 ? GLU A 206 ? LYS A 200 GLU A 206 1 ? 7  
HELX_P HELX_P11 AB2 TRP A 218 ? GLY A 224 ? TRP A 218 GLY A 224 1 ? 7  
HELX_P HELX_P12 AB3 GLY A 224 ? PHE A 236 ? GLY A 224 PHE A 236 1 ? 13 
HELX_P HELX_P13 AB4 PHE A 236 ? VAL A 241 ? PHE A 236 VAL A 241 1 ? 6  
HELX_P HELX_P14 AB5 ASP A 259 ? TRP A 274 ? ASP A 259 TRP A 274 1 ? 16 
HELX_P HELX_P15 AB6 SER A 295 ? GLU A 309 ? SER A 295 GLU A 309 1 ? 15 
HELX_P HELX_P16 AB7 PRO A 326 ? ASN A 335 ? PRO A 326 ASN A 335 1 ? 10 
HELX_P HELX_P17 AB8 ILE A 346 ? SER A 355 ? ILE A 346 SER A 355 1 ? 10 
HELX_P HELX_P18 AB9 ASP A 386 ? ILE A 390 ? ASP A 386 ILE A 390 5 ? 5  
HELX_P HELX_P19 AC1 ALA B 5   ? LEU B 26  ? ALA B 5   LEU B 26  1 ? 22 
HELX_P HELX_P20 AC2 ILE B 67  ? ASP B 80  ? ILE B 67  ASP B 80  1 ? 14 
HELX_P HELX_P21 AC3 GLY B 97  ? LEU B 101 ? GLY B 97  LEU B 101 5 ? 5  
HELX_P HELX_P22 AC4 LYS B 106 ? SER B 112 ? LYS B 106 SER B 112 1 ? 7  
HELX_P HELX_P23 AC5 GLU B 125 ? ASN B 130 ? GLU B 125 ASN B 130 1 ? 6  
HELX_P HELX_P24 AC6 THR B 133 ? ARG B 143 ? THR B 133 ARG B 143 1 ? 11 
HELX_P HELX_P25 AC7 SER B 152 ? GLN B 169 ? SER B 152 GLN B 169 1 ? 18 
HELX_P HELX_P26 AC8 ASP B 172 ? HIS B 177 ? ASP B 172 HIS B 177 1 ? 6  
HELX_P HELX_P27 AC9 TYR B 178 ? ASN B 193 ? TYR B 178 ASN B 193 1 ? 16 
HELX_P HELX_P28 AD1 LYS B 200 ? GLU B 206 ? LYS B 200 GLU B 206 1 ? 7  
HELX_P HELX_P29 AD2 ASN B 216 ? GLY B 224 ? ASN B 216 GLY B 224 1 ? 9  
HELX_P HELX_P30 AD3 GLY B 224 ? ILE B 237 ? GLY B 224 ILE B 237 1 ? 14 
HELX_P HELX_P31 AD4 ASP B 259 ? TRP B 274 ? ASP B 259 TRP B 274 1 ? 16 
HELX_P HELX_P32 AD5 SER B 295 ? PHE B 307 ? SER B 295 PHE B 307 1 ? 13 
HELX_P HELX_P33 AD6 PRO B 326 ? ASN B 335 ? PRO B 326 ASN B 335 1 ? 10 
HELX_P HELX_P34 AD7 ASP B 345 ? ASN B 354 ? ASP B 345 ASN B 354 1 ? 10 
HELX_P HELX_P35 AD8 ASP B 386 ? ILE B 390 ? ASP B 386 ILE B 390 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 LEU 103 A . ? LEU 103 A PRO 104 A ? PRO 104 A 1 2.29 
2 LEU 103 B . ? LEU 103 B PRO 104 B ? PRO 104 B 1 2.72 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 2 ? 
AA3 ? 5 ? 
AA4 ? 2 ? 
AA5 ? 3 ? 
AA6 ? 2 ? 
AA7 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA4 1 2 ? parallel      
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA6 1 2 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? parallel      
AA7 3 4 ? parallel      
AA7 4 5 ? parallel      
AA7 5 6 ? 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 ILE A 52  ? LYS A 55  ? ILE A 52  LYS A 55  
AA1 2 TYR A 88  ? GLY A 92  ? TYR A 88  GLY A 92  
AA1 3 LEU A 144 ? ASN A 147 ? LEU A 144 ASN A 147 
AA2 1 THR A 116 ? GLU A 119 ? THR A 116 GLU A 119 
AA2 2 ILE A 122 ? GLU A 125 ? ILE A 122 GLU A 125 
AA3 1 LYS A 212 ? VAL A 213 ? LYS A 212 VAL A 213 
AA3 2 GLN A 379 ? GLN A 383 ? GLN A 379 GLN A 383 
AA3 3 LYS A 360 ? TYR A 366 ? LYS A 360 TYR A 366 
AA3 4 ALA A 247 ? GLU A 253 ? ALA A 247 GLU A 253 
AA3 5 PHE A 288 ? HIS A 292 ? PHE A 288 HIS A 292 
AA4 1 PHE A 313 ? THR A 314 ? PHE A 313 THR A 314 
AA4 2 PHE A 340 ? GLN A 341 ? PHE A 340 GLN A 341 
AA5 1 ILE B 52  ? LYS B 55  ? ILE B 52  LYS B 55  
AA5 2 TYR B 88  ? GLY B 92  ? TYR B 88  GLY B 92  
AA5 3 LEU B 144 ? ASN B 147 ? LEU B 144 ASN B 147 
AA6 1 THR B 118 ? GLU B 119 ? THR B 118 GLU B 119 
AA6 2 ILE B 122 ? LYS B 123 ? ILE B 122 LYS B 123 
AA7 1 LYS B 212 ? VAL B 213 ? LYS B 212 VAL B 213 
AA7 2 GLN B 379 ? GLN B 383 ? GLN B 379 GLN B 383 
AA7 3 LYS B 360 ? TYR B 366 ? LYS B 360 TYR B 366 
AA7 4 ALA B 247 ? GLU B 253 ? ALA B 247 GLU B 253 
AA7 5 PHE B 288 ? HIS B 292 ? PHE B 288 HIS B 292 
AA7 6 GLN B 341 ? ILE B 343 ? GLN B 341 ILE B 343 
# 
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 LYS A 55  ? N LYS A 55  O TYR A 91  ? O TYR A 91  
AA1 2 3 N LEU A 90  ? N LEU A 90  O VAL A 145 ? O VAL A 145 
AA2 1 2 N GLU A 119 ? N GLU A 119 O ILE A 122 ? O ILE A 122 
AA3 1 2 N VAL A 213 ? N VAL A 213 O ASN A 381 ? O ASN A 381 
AA3 2 3 O VAL A 380 ? O VAL A 380 N GLN A 364 ? N GLN A 364 
AA3 3 4 O GLU A 361 ? O GLU A 361 N PHE A 249 ? N PHE A 249 
AA3 4 5 N LEU A 252 ? N LEU A 252 O LEU A 290 ? O LEU A 290 
AA4 1 2 N THR A 314 ? N THR A 314 O PHE A 340 ? O PHE A 340 
AA5 1 2 N LYS B 55  ? N LYS B 55  O TYR B 91  ? O TYR B 91  
AA5 2 3 N GLY B 92  ? N GLY B 92  O ASN B 147 ? O ASN B 147 
AA6 1 2 N GLU B 119 ? N GLU B 119 O ILE B 122 ? O ILE B 122 
AA7 1 2 N VAL B 213 ? N VAL B 213 O GLN B 383 ? O GLN B 383 
AA7 2 3 O VAL B 380 ? O VAL B 380 N GLN B 364 ? N GLN B 364 
AA7 3 4 O PHE B 365 ? O PHE B 365 N ILE B 251 ? N ILE B 251 
AA7 4 5 N PHE B 250 ? N PHE B 250 O PHE B 288 ? O PHE B 288 
AA7 5 6 N LEU B 289 ? N LEU B 289 O GLN B 341 ? O GLN B 341 
# 
_pdbx_entry_details.entry_id                   8ZGI 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A HIS 64  ? ? OG  A SER 68  ? ? 2.02 
2 1 OD2 A ASP 61  ? ? OG  A SER 96  ? ? 2.05 
3 1 NZ  A LYS 151 ? ? OE2 A GLU 159 ? ? 2.08 
4 1 OH  A TYR 268 ? ? OE2 A GLU 309 ? ? 2.11 
5 1 OE2 B GLU 223 ? ? NZ  B LYS 231 ? ? 2.13 
6 1 OG  A SER 76  ? ? OH  A TYR 126 ? ? 2.15 
7 1 OG  B SER 76  ? ? OH  B TYR 126 ? ? 2.18 
8 1 OE1 B GLU 361 ? ? OH  B TYR 363 ? ? 2.18 
# 
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 ILE A 33  ? ? -172.22 141.30  
2  1 CYS A 37  ? ? -93.99  -65.80  
3  1 ASP A 42  ? ? 59.49   74.31   
4  1 ASP A 46  ? ? 65.50   -0.16   
5  1 HIS A 48  ? ? -102.08 -166.26 
6  1 LEU A 49  ? ? 62.46   70.14   
7  1 THR A 50  ? ? -98.89  42.45   
8  1 HIS A 64  ? ? 70.30   -12.25  
9  1 LYS A 194 ? ? -99.35  37.22   
10 1 SER A 211 ? ? 59.97   11.71   
11 1 LEU A 277 ? ? -98.96  57.40   
12 1 PHE A 324 ? ? -69.66  99.18   
13 1 PRO A 378 ? ? -69.61  72.23   
14 1 CYS B 37  ? ? -96.95  -60.33  
15 1 ASN B 81  ? ? -93.62  33.62   
16 1 SER B 112 ? ? -93.45  47.10   
17 1 ASN B 113 ? ? -134.54 -36.87  
18 1 ASN B 149 ? ? -95.57  56.81   
19 1 THR B 243 ? ? -143.58 43.59   
20 1 ASP B 256 ? ? -82.38  49.86   
21 1 LYS B 257 ? ? -142.33 10.62   
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1  x,y,z          
2  x-y,x,z+1/6    
3  y,-x+y,z+5/6   
4  -y,x-y,z+1/3   
5  -x+y,-x,z+2/3  
6  x-y,-y,-z      
7  -x,-x+y,-z+2/3 
8  -x,-y,z+1/2    
9  y,x,-z+1/3     
10 -y,-x,-z+5/6   
11 -x+y,y,-z+1/2  
12 x,x-y,-z+1/6   
# 
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 1 ? A MET 1 
2 1 Y 1 A ASP 2 ? A ASP 2 
3 1 Y 1 A ARG 3 ? A ARG 3 
4 1 Y 1 B MET 1 ? B MET 1 
5 1 Y 1 B ASP 2 ? B ASP 2 
6 1 Y 1 B ARG 3 ? B ARG 3 
# 
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 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
ILE N    N N N 158 
ILE CA   C N S 159 
ILE C    C N N 160 
ILE O    O N N 161 
ILE CB   C N S 162 
ILE CG1  C N N 163 
ILE CG2  C N N 164 
ILE CD1  C N N 165 
ILE OXT  O N N 166 
ILE H    H N N 167 
ILE H2   H N N 168 
ILE HA   H N N 169 
ILE HB   H N N 170 
ILE HG12 H N N 171 
ILE HG13 H N N 172 
ILE HG21 H N N 173 
ILE HG22 H N N 174 
ILE HG23 H N N 175 
ILE HD11 H N N 176 
ILE HD12 H N N 177 
ILE HD13 H N N 178 
ILE HXT  H N N 179 
LEU N    N N N 180 
LEU CA   C N S 181 
LEU C    C N N 182 
LEU O    O N N 183 
LEU CB   C N N 184 
LEU CG   C N N 185 
LEU CD1  C N N 186 
LEU CD2  C N N 187 
LEU OXT  O N N 188 
LEU H    H N N 189 
LEU H2   H N N 190 
LEU HA   H N N 191 
LEU HB2  H N N 192 
LEU HB3  H N N 193 
LEU HG   H N N 194 
LEU HD11 H N N 195 
LEU HD12 H N N 196 
LEU HD13 H N N 197 
LEU HD21 H N N 198 
LEU HD22 H N N 199 
LEU HD23 H N N 200 
LEU HXT  H N N 201 
LYS N    N N N 202 
LYS CA   C N S 203 
LYS C    C N N 204 
LYS O    O N N 205 
LYS CB   C N N 206 
LYS CG   C N N 207 
LYS CD   C N N 208 
LYS CE   C N N 209 
LYS NZ   N N N 210 
LYS OXT  O N N 211 
LYS H    H N N 212 
LYS H2   H N N 213 
LYS HA   H N N 214 
LYS HB2  H N N 215 
LYS HB3  H N N 216 
LYS HG2  H N N 217 
LYS HG3  H N N 218 
LYS HD2  H N N 219 
LYS HD3  H N N 220 
LYS HE2  H N N 221 
LYS HE3  H N N 222 
LYS HZ1  H N N 223 
LYS HZ2  H N N 224 
LYS HZ3  H N N 225 
LYS HXT  H N N 226 
MET N    N N N 227 
MET CA   C N S 228 
MET C    C N N 229 
MET O    O N N 230 
MET CB   C N N 231 
MET CG   C N N 232 
MET SD   S N N 233 
MET CE   C N N 234 
MET OXT  O N N 235 
MET H    H N N 236 
MET H2   H N N 237 
MET HA   H N N 238 
MET HB2  H N N 239 
MET HB3  H N N 240 
MET HG2  H N N 241 
MET HG3  H N N 242 
MET HE1  H N N 243 
MET HE2  H N N 244 
MET HE3  H N N 245 
MET HXT  H N N 246 
PHE N    N N N 247 
PHE CA   C N S 248 
PHE C    C N N 249 
PHE O    O N N 250 
PHE CB   C N N 251 
PHE CG   C Y N 252 
PHE CD1  C Y N 253 
PHE CD2  C Y N 254 
PHE CE1  C Y N 255 
PHE CE2  C Y N 256 
PHE CZ   C Y N 257 
PHE OXT  O N N 258 
PHE H    H N N 259 
PHE H2   H N N 260 
PHE HA   H N N 261 
PHE HB2  H N N 262 
PHE HB3  H N N 263 
PHE HD1  H N N 264 
PHE HD2  H N N 265 
PHE HE1  H N N 266 
PHE HE2  H N N 267 
PHE HZ   H N N 268 
PHE HXT  H N N 269 
PRO N    N N N 270 
PRO CA   C N S 271 
PRO C    C N N 272 
PRO O    O N N 273 
PRO CB   C N N 274 
PRO CG   C N N 275 
PRO CD   C N N 276 
PRO OXT  O N N 277 
PRO H    H N N 278 
PRO HA   H N N 279 
PRO HB2  H N N 280 
PRO HB3  H N N 281 
PRO HG2  H N N 282 
PRO HG3  H N N 283 
PRO HD2  H N N 284 
PRO HD3  H N N 285 
PRO HXT  H N N 286 
SER N    N N N 287 
SER CA   C N S 288 
SER C    C N N 289 
SER O    O N N 290 
SER CB   C N N 291 
SER OG   O N N 292 
SER OXT  O N N 293 
SER H    H N N 294 
SER H2   H N N 295 
SER HA   H N N 296 
SER HB2  H N N 297 
SER HB3  H N N 298 
SER HG   H N N 299 
SER HXT  H N N 300 
THR N    N N N 301 
THR CA   C N S 302 
THR C    C N N 303 
THR O    O N N 304 
THR CB   C N R 305 
THR OG1  O N N 306 
THR CG2  C N N 307 
THR OXT  O N N 308 
THR H    H N N 309 
THR H2   H N N 310 
THR HA   H N N 311 
THR HB   H N N 312 
THR HG1  H N N 313 
THR HG21 H N N 314 
THR HG22 H N N 315 
THR HG23 H N N 316 
THR HXT  H N N 317 
TRP N    N N N 318 
TRP CA   C N S 319 
TRP C    C N N 320 
TRP O    O N N 321 
TRP CB   C N N 322 
TRP CG   C Y N 323 
TRP CD1  C Y N 324 
TRP CD2  C Y N 325 
TRP NE1  N Y N 326 
TRP CE2  C Y N 327 
TRP CE3  C Y N 328 
TRP CZ2  C Y N 329 
TRP CZ3  C Y N 330 
TRP CH2  C Y N 331 
TRP OXT  O N N 332 
TRP H    H N N 333 
TRP H2   H N N 334 
TRP HA   H N N 335 
TRP HB2  H N N 336 
TRP HB3  H N N 337 
TRP HD1  H N N 338 
TRP HE1  H N N 339 
TRP HE3  H N N 340 
TRP HZ2  H N N 341 
TRP HZ3  H N N 342 
TRP HH2  H N N 343 
TRP HXT  H N N 344 
TYR N    N N N 345 
TYR CA   C N S 346 
TYR C    C N N 347 
TYR O    O N N 348 
TYR CB   C N N 349 
TYR CG   C Y N 350 
TYR CD1  C Y N 351 
TYR CD2  C Y N 352 
TYR CE1  C Y N 353 
TYR CE2  C Y N 354 
TYR CZ   C Y N 355 
TYR OH   O N N 356 
TYR OXT  O N N 357 
TYR H    H N N 358 
TYR H2   H N N 359 
TYR HA   H N N 360 
TYR HB2  H N N 361 
TYR HB3  H N N 362 
TYR HD1  H N N 363 
TYR HD2  H N N 364 
TYR HE1  H N N 365 
TYR HE2  H N N 366 
TYR HH   H N N 367 
TYR HXT  H N N 368 
VAL N    N N N 369 
VAL CA   C N S 370 
VAL C    C N N 371 
VAL O    O N N 372 
VAL CB   C N N 373 
VAL CG1  C N N 374 
VAL CG2  C N N 375 
VAL OXT  O N N 376 
VAL H    H N N 377 
VAL H2   H N N 378 
VAL HA   H N N 379 
VAL HB   H N N 380 
VAL HG11 H N N 381 
VAL HG12 H N N 382 
VAL HG13 H N N 383 
VAL HG21 H N N 384 
VAL HG22 H N N 385 
VAL HG23 H N N 386 
VAL HXT  H N N 387 
# 
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 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
PHE N   CA   sing N N 235 
PHE N   H    sing N N 236 
PHE N   H2   sing N N 237 
PHE CA  C    sing N N 238 
PHE CA  CB   sing N N 239 
PHE CA  HA   sing N N 240 
PHE C   O    doub N N 241 
PHE C   OXT  sing N N 242 
PHE CB  CG   sing N N 243 
PHE CB  HB2  sing N N 244 
PHE CB  HB3  sing N N 245 
PHE CG  CD1  doub Y N 246 
PHE CG  CD2  sing Y N 247 
PHE CD1 CE1  sing Y N 248 
PHE CD1 HD1  sing N N 249 
PHE CD2 CE2  doub Y N 250 
PHE CD2 HD2  sing N N 251 
PHE CE1 CZ   doub Y N 252 
PHE CE1 HE1  sing N N 253 
PHE CE2 CZ   sing Y N 254 
PHE CE2 HE2  sing N N 255 
PHE CZ  HZ   sing N N 256 
PHE OXT HXT  sing N N 257 
PRO N   CA   sing N N 258 
PRO N   CD   sing N N 259 
PRO N   H    sing N N 260 
PRO CA  C    sing N N 261 
PRO CA  CB   sing N N 262 
PRO CA  HA   sing N N 263 
PRO C   O    doub N N 264 
PRO C   OXT  sing N N 265 
PRO CB  CG   sing N N 266 
PRO CB  HB2  sing N N 267 
PRO CB  HB3  sing N N 268 
PRO CG  CD   sing N N 269 
PRO CG  HG2  sing N N 270 
PRO CG  HG3  sing N N 271 
PRO CD  HD2  sing N N 272 
PRO CD  HD3  sing N N 273 
PRO OXT HXT  sing N N 274 
SER N   CA   sing N N 275 
SER N   H    sing N N 276 
SER N   H2   sing N N 277 
SER CA  C    sing N N 278 
SER CA  CB   sing N N 279 
SER CA  HA   sing N N 280 
SER C   O    doub N N 281 
SER C   OXT  sing N N 282 
SER CB  OG   sing N N 283 
SER CB  HB2  sing N N 284 
SER CB  HB3  sing N N 285 
SER OG  HG   sing N N 286 
SER OXT HXT  sing N N 287 
THR N   CA   sing N N 288 
THR N   H    sing N N 289 
THR N   H2   sing N N 290 
THR CA  C    sing N N 291 
THR CA  CB   sing N N 292 
THR CA  HA   sing N N 293 
THR C   O    doub N N 294 
THR C   OXT  sing N N 295 
THR CB  OG1  sing N N 296 
THR CB  CG2  sing N N 297 
THR CB  HB   sing N N 298 
THR OG1 HG1  sing N N 299 
THR CG2 HG21 sing N N 300 
THR CG2 HG22 sing N N 301 
THR CG2 HG23 sing N N 302 
THR OXT HXT  sing N N 303 
TRP N   CA   sing N N 304 
TRP N   H    sing N N 305 
TRP N   H2   sing N N 306 
TRP CA  C    sing N N 307 
TRP CA  CB   sing N N 308 
TRP CA  HA   sing N N 309 
TRP C   O    doub N N 310 
TRP C   OXT  sing N N 311 
TRP CB  CG   sing N N 312 
TRP CB  HB2  sing N N 313 
TRP CB  HB3  sing N N 314 
TRP CG  CD1  doub Y N 315 
TRP CG  CD2  sing Y N 316 
TRP CD1 NE1  sing Y N 317 
TRP CD1 HD1  sing N N 318 
TRP CD2 CE2  doub Y N 319 
TRP CD2 CE3  sing Y N 320 
TRP NE1 CE2  sing Y N 321 
TRP NE1 HE1  sing N N 322 
TRP CE2 CZ2  sing Y N 323 
TRP CE3 CZ3  doub Y N 324 
TRP CE3 HE3  sing N N 325 
TRP CZ2 CH2  doub Y N 326 
TRP CZ2 HZ2  sing N N 327 
TRP CZ3 CH2  sing Y N 328 
TRP CZ3 HZ3  sing N N 329 
TRP CH2 HH2  sing N N 330 
TRP OXT HXT  sing N N 331 
TYR N   CA   sing N N 332 
TYR N   H    sing N N 333 
TYR N   H2   sing N N 334 
TYR CA  C    sing N N 335 
TYR CA  CB   sing N N 336 
TYR CA  HA   sing N N 337 
TYR C   O    doub N N 338 
TYR C   OXT  sing N N 339 
TYR CB  CG   sing N N 340 
TYR CB  HB2  sing N N 341 
TYR CB  HB3  sing N N 342 
TYR CG  CD1  doub Y N 343 
TYR CG  CD2  sing Y N 344 
TYR CD1 CE1  sing Y N 345 
TYR CD1 HD1  sing N N 346 
TYR CD2 CE2  doub Y N 347 
TYR CD2 HD2  sing N N 348 
TYR CE1 CZ   doub Y N 349 
TYR CE1 HE1  sing N N 350 
TYR CE2 CZ   sing Y N 351 
TYR CE2 HE2  sing N N 352 
TYR CZ  OH   sing N N 353 
TYR OH  HH   sing N N 354 
TYR OXT HXT  sing N N 355 
VAL N   CA   sing N N 356 
VAL N   H    sing N N 357 
VAL N   H2   sing N N 358 
VAL CA  C    sing N N 359 
VAL CA  CB   sing N N 360 
VAL CA  HA   sing N N 361 
VAL C   O    doub N N 362 
VAL C   OXT  sing N N 363 
VAL CB  CG1  sing N N 364 
VAL CB  CG2  sing N N 365 
VAL CB  HB   sing N N 366 
VAL CG1 HG11 sing N N 367 
VAL CG1 HG12 sing N N 368 
VAL CG1 HG13 sing N N 369 
VAL CG2 HG21 sing N N 370 
VAL CG2 HG22 sing N N 371 
VAL CG2 HG23 sing N N 372 
VAL OXT HXT  sing N N 373 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 61 2 2' 
_space_group.name_Hall        'P 61 2 (x,y,z+5/12)' 
_space_group.IT_number        178 
_space_group.crystal_system   hexagonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    8ZGI 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.006930 
_atom_sites.fract_transf_matrix[1][2]   0.004001 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008002 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.003806 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C   ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N   ? ? 6.96715 ?       ? ? 11.43723 ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O   ? ? 7.96527 ?       ? ? 9.05267  ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O1- ? ? 5.12366 3.84317 ? ? 3.49406  27.47979 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S   ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . SER A 1 4   ? -14.362  39.835 -12.286 1.00 100.29 ?  4   SER A N   1 
ATOM 2    C CA  . SER A 1 4   ? -15.042  40.834 -13.102 1.00 107.79 ?  4   SER A CA  1 
ATOM 3    C C   . SER A 1 4   ? -15.376  42.068 -12.275 1.00 95.47  ?  4   SER A C   1 
ATOM 4    O O   . SER A 1 4   ? -14.642  42.427 -11.352 1.00 98.58  ?  4   SER A O   1 
ATOM 5    C CB  . SER A 1 4   ? -16.319  40.251 -13.713 1.00 102.34 ?  4   SER A CB  1 
ATOM 6    O OG  . SER A 1 4   ? -17.297  40.010 -12.716 1.00 92.69  ?  4   SER A OG  1 
ATOM 7    N N   . ALA A 1 5   ? -16.488  42.716 -12.613 1.00 96.76  ?  5   ALA A N   1 
ATOM 8    C CA  . ALA A 1 5   ? -16.988  43.841 -11.836 1.00 107.48 ?  5   ALA A CA  1 
ATOM 9    C C   . ALA A 1 5   ? -17.623  43.409 -10.522 1.00 109.53 ?  5   ALA A C   1 
ATOM 10   O O   . ALA A 1 5   ? -17.993  44.272 -9.720  1.00 107.82 ?  5   ALA A O   1 
ATOM 11   C CB  . ALA A 1 5   ? -17.999  44.644 -12.657 1.00 83.01  ?  5   ALA A CB  1 
ATOM 12   N N   . VAL A 1 6   ? -17.765  42.103 -10.287 1.00 96.29  ?  6   VAL A N   1 
ATOM 13   C CA  . VAL A 1 6   ? -18.299  41.636 -9.013  1.00 93.94  ?  6   VAL A CA  1 
ATOM 14   C C   . VAL A 1 6   ? -17.284  41.852 -7.898  1.00 107.39 ?  6   VAL A C   1 
ATOM 15   O O   . VAL A 1 6   ? -17.662  42.093 -6.745  1.00 97.44  ?  6   VAL A O   1 
ATOM 16   C CB  . VAL A 1 6   ? -18.726  40.159 -9.123  1.00 88.56  ?  6   VAL A CB  1 
ATOM 17   C CG1 . VAL A 1 6   ? -17.543  39.282 -9.512  1.00 80.01  ?  6   VAL A CG1 1 
ATOM 18   C CG2 . VAL A 1 6   ? -19.355  39.680 -7.821  1.00 102.18 ?  6   VAL A CG2 1 
ATOM 19   N N   . ASP A 1 7   ? -15.987  41.786 -8.218  1.00 113.27 ?  7   ASP A N   1 
ATOM 20   C CA  . ASP A 1 7   ? -14.960  42.064 -7.219  1.00 94.57  ?  7   ASP A CA  1 
ATOM 21   C C   . ASP A 1 7   ? -15.094  43.472 -6.660  1.00 99.56  ?  7   ASP A C   1 
ATOM 22   O O   . ASP A 1 7   ? -14.687  43.730 -5.522  1.00 88.48  ?  7   ASP A O   1 
ATOM 23   C CB  . ASP A 1 7   ? -13.570  41.859 -7.820  1.00 100.08 ?  7   ASP A CB  1 
ATOM 24   C CG  . ASP A 1 7   ? -13.377  40.464 -8.373  1.00 110.30 ?  7   ASP A CG  1 
ATOM 25   O OD1 . ASP A 1 7   ? -13.850  39.502 -7.733  1.00 125.20 ?  7   ASP A OD1 1 
ATOM 26   O OD2 . ASP A 1 7   ? -12.753  40.329 -9.445  1.00 117.85 -1 7   ASP A OD2 1 
ATOM 27   N N   . THR A 1 8   ? -15.643  44.398 -7.448  1.00 110.25 ?  8   THR A N   1 
ATOM 28   C CA  . THR A 1 8   ? -16.022  45.697 -6.909  1.00 96.96  ?  8   THR A CA  1 
ATOM 29   C C   . THR A 1 8   ? -17.012  45.529 -5.761  1.00 94.03  ?  8   THR A C   1 
ATOM 30   O O   . THR A 1 8   ? -16.750  45.953 -4.630  1.00 99.60  ?  8   THR A O   1 
ATOM 31   C CB  . THR A 1 8   ? -16.606  46.571 -8.022  1.00 99.44  ?  8   THR A CB  1 
ATOM 32   O OG1 . THR A 1 8   ? -15.693  46.609 -9.128  1.00 100.58 ?  8   THR A OG1 1 
ATOM 33   C CG2 . THR A 1 8   ? -16.848  47.982 -7.526  1.00 106.98 ?  8   THR A CG2 1 
ATOM 34   N N   . ILE A 1 9   ? -18.147  44.878 -6.029  1.00 97.57  ?  9   ILE A N   1 
ATOM 35   C CA  . ILE A 1 9   ? -19.116  44.596 -4.971  1.00 105.50 ?  9   ILE A CA  1 
ATOM 36   C C   . ILE A 1 9   ? -18.508  43.668 -3.928  1.00 99.29  ?  9   ILE A C   1 
ATOM 37   O O   . ILE A 1 9   ? -18.587  43.924 -2.720  1.00 96.23  ?  9   ILE A O   1 
ATOM 38   C CB  . ILE A 1 9   ? -20.406  43.999 -5.564  1.00 112.20 ?  9   ILE A CB  1 
ATOM 39   C CG1 . ILE A 1 9   ? -20.980  44.919 -6.643  1.00 117.02 ?  9   ILE A CG1 1 
ATOM 40   C CG2 . ILE A 1 9   ? -21.429  43.734 -4.466  1.00 87.10  ?  9   ILE A CG2 1 
ATOM 41   C CD1 . ILE A 1 9   ? -20.694  44.451 -8.051  1.00 114.25 ?  9   ILE A CD1 1 
ATOM 42   N N   . ARG A 1 10  ? -17.886  42.578 -4.380  1.00 99.51  ?  10  ARG A N   1 
ATOM 43   C CA  . ARG A 1 10  ? -17.264  41.601 -3.487  1.00 94.43  ?  10  ARG A CA  1 
ATOM 44   C C   . ARG A 1 10  ? -15.984  42.222 -2.937  1.00 102.92 ?  10  ARG A C   1 
ATOM 45   O O   . ARG A 1 10  ? -14.869  41.946 -3.386  1.00 126.08 ?  10  ARG A O   1 
ATOM 46   C CB  . ARG A 1 10  ? -16.989  40.297 -4.227  1.00 120.60 ?  10  ARG A CB  1 
ATOM 47   C CG  . ARG A 1 10  ? -16.505  39.150 -3.354  1.00 106.80 ?  10  ARG A CG  1 
ATOM 48   C CD  . ARG A 1 10  ? -16.131  37.948 -4.211  1.00 102.08 ?  10  ARG A CD  1 
ATOM 49   N NE  . ARG A 1 10  ? -15.751  36.789 -3.408  1.00 124.35 ?  10  ARG A NE  1 
ATOM 50   C CZ  . ARG A 1 10  ? -15.278  35.654 -3.912  1.00 138.70 ?  10  ARG A CZ  1 
ATOM 51   N NH1 . ARG A 1 10  ? -15.114  35.523 -5.222  1.00 132.69 ?  10  ARG A NH1 1 
ATOM 52   N NH2 . ARG A 1 10  ? -14.960  34.651 -3.105  1.00 125.83 ?  10  ARG A NH2 1 
ATOM 53   N N   . GLY A 1 11  ? -16.158  43.067 -1.926  1.00 91.84  ?  11  GLY A N   1 
ATOM 54   C CA  . GLY A 1 11  ? -15.071  43.842 -1.366  1.00 100.50 ?  11  GLY A CA  1 
ATOM 55   C C   . GLY A 1 11  ? -15.519  45.224 -0.940  1.00 92.17  ?  11  GLY A C   1 
ATOM 56   O O   . GLY A 1 11  ? -15.025  45.758 0.058   1.00 97.55  ?  11  GLY A O   1 
ATOM 57   N N   . TYR A 1 12  ? -16.472  45.807 -1.673  1.00 74.90  ?  12  TYR A N   1 
ATOM 58   C CA  . TYR A 1 12  ? -17.149  46.996 -1.170  1.00 76.07  ?  12  TYR A CA  1 
ATOM 59   C C   . TYR A 1 12  ? -17.881  46.693 0.127   1.00 88.39  ?  12  TYR A C   1 
ATOM 60   O O   . TYR A 1 12  ? -18.090  47.591 0.950   1.00 90.70  ?  12  TYR A O   1 
ATOM 61   C CB  . TYR A 1 12  ? -18.123  47.540 -2.215  1.00 69.49  ?  12  TYR A CB  1 
ATOM 62   C CG  . TYR A 1 12  ? -17.704  48.855 -2.834  1.00 78.72  ?  12  TYR A CG  1 
ATOM 63   C CD1 . TYR A 1 12  ? -17.886  50.052 -2.157  1.00 67.85  ?  12  TYR A CD1 1 
ATOM 64   C CD2 . TYR A 1 12  ? -17.136  48.899 -4.099  1.00 73.51  ?  12  TYR A CD2 1 
ATOM 65   C CE1 . TYR A 1 12  ? -17.508  51.257 -2.722  1.00 70.91  ?  12  TYR A CE1 1 
ATOM 66   C CE2 . TYR A 1 12  ? -16.755  50.097 -4.672  1.00 84.08  ?  12  TYR A CE2 1 
ATOM 67   C CZ  . TYR A 1 12  ? -16.943  51.273 -3.980  1.00 85.76  ?  12  TYR A CZ  1 
ATOM 68   O OH  . TYR A 1 12  ? -16.564  52.468 -4.547  1.00 77.62  ?  12  TYR A OH  1 
ATOM 69   N N   . CYS A 1 13  ? -18.282  45.435 0.321   1.00 89.97  ?  13  CYS A N   1 
ATOM 70   C CA  . CYS A 1 13  ? -18.858  45.003 1.586   1.00 92.73  ?  13  CYS A CA  1 
ATOM 71   C C   . CYS A 1 13  ? -17.787  44.701 2.626   1.00 87.94  ?  13  CYS A C   1 
ATOM 72   O O   . CYS A 1 13  ? -18.044  44.833 3.827   1.00 92.53  ?  13  CYS A O   1 
ATOM 73   C CB  . CYS A 1 13  ? -19.738  43.772 1.364   1.00 99.21  ?  13  CYS A CB  1 
ATOM 74   S SG  . CYS A 1 13  ? -19.091  42.617 0.142   1.00 126.20 ?  13  CYS A SG  1 
ATOM 75   N N   . TYR A 1 14  ? -16.594  44.291 2.187   1.00 86.63  ?  14  TYR A N   1 
ATOM 76   C CA  . TYR A 1 14  ? -15.502  44.032 3.121   1.00 88.06  ?  14  TYR A CA  1 
ATOM 77   C C   . TYR A 1 14  ? -15.173  45.275 3.938   1.00 93.21  ?  14  TYR A C   1 
ATOM 78   O O   . TYR A 1 14  ? -15.047  45.210 5.166   1.00 101.47 ?  14  TYR A O   1 
ATOM 79   C CB  . TYR A 1 14  ? -14.267  43.538 2.362   1.00 88.86  ?  14  TYR A CB  1 
ATOM 80   C CG  . TYR A 1 14  ? -13.158  43.000 3.246   1.00 101.77 ?  14  TYR A CG  1 
ATOM 81   C CD1 . TYR A 1 14  ? -12.917  41.635 3.336   1.00 114.60 ?  14  TYR A CD1 1 
ATOM 82   C CD2 . TYR A 1 14  ? -12.337  43.857 3.971   1.00 103.13 ?  14  TYR A CD2 1 
ATOM 83   C CE1 . TYR A 1 14  ? -11.903  41.139 4.137   1.00 115.13 ?  14  TYR A CE1 1 
ATOM 84   C CE2 . TYR A 1 14  ? -11.322  43.371 4.773   1.00 105.19 ?  14  TYR A CE2 1 
ATOM 85   C CZ  . TYR A 1 14  ? -11.109  42.012 4.852   1.00 111.05 ?  14  TYR A CZ  1 
ATOM 86   O OH  . TYR A 1 14  ? -10.098  41.524 5.649   1.00 113.33 ?  14  TYR A OH  1 
ATOM 87   N N   . GLN A 1 15  ? -15.024  46.420 3.268   1.00 87.11  ?  15  GLN A N   1 
ATOM 88   C CA  . GLN A 1 15  ? -14.711  47.656 3.972   1.00 84.40  ?  15  GLN A CA  1 
ATOM 89   C C   . GLN A 1 15  ? -15.821  48.061 4.933   1.00 97.47  ?  15  GLN A C   1 
ATOM 90   O O   . GLN A 1 15  ? -15.554  48.764 5.913   1.00 94.31  ?  15  GLN A O   1 
ATOM 91   C CB  . GLN A 1 15  ? -14.438  48.773 2.963   1.00 90.42  ?  15  GLN A CB  1 
ATOM 92   C CG  . GLN A 1 15  ? -13.417  49.801 3.426   1.00 99.62  ?  15  GLN A CG  1 
ATOM 93   C CD  . GLN A 1 15  ? -14.038  50.950 4.192   1.00 112.23 ?  15  GLN A CD  1 
ATOM 94   O OE1 . GLN A 1 15  ? -15.259  51.051 4.302   1.00 123.15 ?  15  GLN A OE1 1 
ATOM 95   N NE2 . GLN A 1 15  ? -13.195  51.826 4.727   1.00 108.73 ?  15  GLN A NE2 1 
ATOM 96   N N   . VAL A 1 16  ? -17.056  47.626 4.680   1.00 105.51 ?  16  VAL A N   1 
ATOM 97   C CA  . VAL A 1 16  ? -18.143  47.886 5.619   1.00 106.80 ?  16  VAL A CA  1 
ATOM 98   C C   . VAL A 1 16  ? -18.001  47.003 6.853   1.00 104.07 ?  16  VAL A C   1 
ATOM 99   O O   . VAL A 1 16  ? -18.060  47.485 7.990   1.00 102.89 ?  16  VAL A O   1 
ATOM 100  C CB  . VAL A 1 16  ? -19.508  47.686 4.936   1.00 96.37  ?  16  VAL A CB  1 
ATOM 101  C CG1 . VAL A 1 16  ? -20.632  48.130 5.858   1.00 101.24 ?  16  VAL A CG1 1 
ATOM 102  C CG2 . VAL A 1 16  ? -19.560  48.455 3.628   1.00 89.37  ?  16  VAL A CG2 1 
ATOM 103  N N   . ASP A 1 17  ? -17.817  45.695 6.647   1.00 88.06  ?  17  ASP A N   1 
ATOM 104  C CA  . ASP A 1 17  ? -17.631  44.781 7.772   1.00 96.56  ?  17  ASP A CA  1 
ATOM 105  C C   . ASP A 1 17  ? -16.445  45.202 8.630   1.00 105.91 ?  17  ASP A C   1 
ATOM 106  O O   . ASP A 1 17  ? -16.545  45.264 9.860   1.00 96.25  ?  17  ASP A O   1 
ATOM 107  C CB  . ASP A 1 17  ? -17.447  43.351 7.265   1.00 94.54  ?  17  ASP A CB  1 
ATOM 108  C CG  . ASP A 1 17  ? -18.550  42.920 6.325   1.00 114.19 ?  17  ASP A CG  1 
ATOM 109  O OD1 . ASP A 1 17  ? -19.419  43.757 6.002   1.00 122.95 ?  17  ASP A OD1 1 
ATOM 110  O OD2 . ASP A 1 17  ? -18.553  41.741 5.910   1.00 127.64 -1 17  ASP A OD2 1 
ATOM 111  N N   . LYS A 1 18  ? -15.308  45.494 7.991   1.00 100.94 ?  18  LYS A N   1 
ATOM 112  C CA  . LYS A 1 18  ? -14.150  46.000 8.722   1.00 97.04  ?  18  LYS A CA  1 
ATOM 113  C C   . LYS A 1 18  ? -14.482  47.285 9.470   1.00 93.80  ?  18  LYS A C   1 
ATOM 114  O O   . LYS A 1 18  ? -13.888  47.567 10.516  1.00 100.74 ?  18  LYS A O   1 
ATOM 115  C CB  . LYS A 1 18  ? -12.982  46.220 7.755   1.00 90.19  ?  18  LYS A CB  1 
ATOM 116  C CG  . LYS A 1 18  ? -11.670  46.651 8.404   1.00 95.95  ?  18  LYS A CG  1 
ATOM 117  C CD  . LYS A 1 18  ? -11.476  48.162 8.345   1.00 99.76  ?  18  LYS A CD  1 
ATOM 118  C CE  . LYS A 1 18  ? -10.978  48.604 6.978   1.00 107.87 ?  18  LYS A CE  1 
ATOM 119  N NZ  . LYS A 1 18  ? -9.558   48.217 6.752   1.00 119.65 ?  18  LYS A NZ  1 
ATOM 120  N N   . THR A 1 19  ? -15.432  48.069 8.957   1.00 83.75  ?  19  THR A N   1 
ATOM 121  C CA  . THR A 1 19  ? -15.822  49.301 9.632   1.00 89.63  ?  19  THR A CA  1 
ATOM 122  C C   . THR A 1 19  ? -16.762  49.029 10.802  1.00 90.55  ?  19  THR A C   1 
ATOM 123  O O   . THR A 1 19  ? -16.622  49.642 11.866  1.00 100.28 ?  19  THR A O   1 
ATOM 124  C CB  . THR A 1 19  ? -16.470  50.261 8.636   1.00 95.47  ?  19  THR A CB  1 
ATOM 125  O OG1 . THR A 1 19  ? -15.589  50.459 7.523   1.00 105.04 ?  19  THR A OG1 1 
ATOM 126  C CG2 . THR A 1 19  ? -16.750  51.597 9.294   1.00 90.82  ?  19  THR A CG2 1 
ATOM 127  N N   . ILE A 1 20  ? -17.722  48.117 10.633  1.00 95.94  ?  20  ILE A N   1 
ATOM 128  C CA  . ILE A 1 20  ? -18.635  47.827 11.734  1.00 105.58 ?  20  ILE A CA  1 
ATOM 129  C C   . ILE A 1 20  ? -17.974  46.920 12.768  1.00 99.13  ?  20  ILE A C   1 
ATOM 130  O O   . ILE A 1 20  ? -18.357  46.935 13.944  1.00 110.65 ?  20  ILE A O   1 
ATOM 131  C CB  . ILE A 1 20  ? -19.954  47.230 11.211  1.00 101.81 ?  20  ILE A CB  1 
ATOM 132  C CG1 . ILE A 1 20  ? -19.805  45.744 10.891  1.00 100.19 ?  20  ILE A CG1 1 
ATOM 133  C CG2 . ILE A 1 20  ? -20.436  47.992 9.991   1.00 83.78  ?  20  ILE A CG2 1 
ATOM 134  C CD1 . ILE A 1 20  ? -21.096  44.976 11.046  1.00 100.05 ?  20  ILE A CD1 1 
ATOM 135  N N   . ILE A 1 21  ? -16.987  46.120 12.362  1.00 88.00  ?  21  ILE A N   1 
ATOM 136  C CA  . ILE A 1 21  ? -16.152  45.428 13.339  1.00 90.67  ?  21  ILE A CA  1 
ATOM 137  C C   . ILE A 1 21  ? -15.332  46.439 14.129  1.00 95.99  ?  21  ILE A C   1 
ATOM 138  O O   . ILE A 1 21  ? -15.108  46.276 15.335  1.00 101.37 ?  21  ILE A O   1 
ATOM 139  C CB  . ILE A 1 21  ? -15.263  44.385 12.634  1.00 87.06  ?  21  ILE A CB  1 
ATOM 140  C CG1 . ILE A 1 21  ? -16.086  43.153 12.254  1.00 106.97 ?  21  ILE A CG1 1 
ATOM 141  C CG2 . ILE A 1 21  ? -14.078  43.991 13.505  1.00 86.06  ?  21  ILE A CG2 1 
ATOM 142  C CD1 . ILE A 1 21  ? -16.567  42.349 13.444  1.00 114.88 ?  21  ILE A CD1 1 
ATOM 143  N N   . GLU A 1 22  ? -14.900  47.516 13.468  1.00 93.88  ?  22  GLU A N   1 
ATOM 144  C CA  . GLU A 1 22  ? -14.125  48.566 14.119  1.00 106.78 ?  22  GLU A CA  1 
ATOM 145  C C   . GLU A 1 22  ? -14.917  49.279 15.210  1.00 114.41 ?  22  GLU A C   1 
ATOM 146  O O   . GLU A 1 22  ? -14.319  49.966 16.047  1.00 126.62 ?  22  GLU A O   1 
ATOM 147  C CB  . GLU A 1 22  ? -13.648  49.566 13.060  1.00 110.56 ?  22  GLU A CB  1 
ATOM 148  C CG  . GLU A 1 22  ? -12.610  50.578 13.521  1.00 124.77 ?  22  GLU A CG  1 
ATOM 149  C CD  . GLU A 1 22  ? -12.096  51.435 12.376  1.00 129.72 ?  22  GLU A CD  1 
ATOM 150  O OE1 . GLU A 1 22  ? -12.051  50.933 11.233  1.00 123.15 ?  22  GLU A OE1 1 
ATOM 151  O OE2 . GLU A 1 22  ? -11.738  52.607 12.617  1.00 136.58 -1 22  GLU A OE2 1 
ATOM 152  N N   . ILE A 1 23  ? -16.236  49.121 15.233  1.00 105.24 ?  23  ILE A N   1 
ATOM 153  C CA  . ILE A 1 23  ? -17.094  49.793 16.204  1.00 125.20 ?  23  ILE A CA  1 
ATOM 154  C C   . ILE A 1 23  ? -17.429  48.886 17.381  1.00 122.11 ?  23  ILE A C   1 
ATOM 155  O O   . ILE A 1 23  ? -17.314  49.292 18.537  1.00 112.04 ?  23  ILE A O   1 
ATOM 156  C CB  . ILE A 1 23  ? -18.375  50.310 15.511  1.00 125.84 ?  23  ILE A CB  1 
ATOM 157  C CG1 . ILE A 1 23  ? -18.008  51.213 14.333  1.00 129.86 ?  23  ILE A CG1 1 
ATOM 158  C CG2 . ILE A 1 23  ? -19.257  51.052 16.503  1.00 113.20 ?  23  ILE A CG2 1 
ATOM 159  C CD1 . ILE A 1 23  ? -19.187  51.628 13.487  1.00 125.59 ?  23  ILE A CD1 1 
ATOM 160  N N   . PHE A 1 24  ? -17.851  47.649 17.106  1.00 121.62 ?  24  PHE A N   1 
ATOM 161  C CA  . PHE A 1 24  ? -18.207  46.739 18.190  1.00 122.82 ?  24  PHE A CA  1 
ATOM 162  C C   . PHE A 1 24  ? -16.987  46.304 18.991  1.00 125.45 ?  24  PHE A C   1 
ATOM 163  O O   . PHE A 1 24  ? -17.096  46.065 20.199  1.00 127.87 ?  24  PHE A O   1 
ATOM 164  C CB  . PHE A 1 24  ? -18.946  45.519 17.643  1.00 121.51 ?  24  PHE A CB  1 
ATOM 165  C CG  . PHE A 1 24  ? -20.436  45.694 17.578  1.00 138.25 ?  24  PHE A CG  1 
ATOM 166  C CD1 . PHE A 1 24  ? -20.998  46.960 17.593  1.00 132.19 ?  24  PHE A CD1 1 
ATOM 167  C CD2 . PHE A 1 24  ? -21.275  44.595 17.526  1.00 136.41 ?  24  PHE A CD2 1 
ATOM 168  C CE1 . PHE A 1 24  ? -22.368  47.126 17.540  1.00 130.85 ?  24  PHE A CE1 1 
ATOM 169  C CE2 . PHE A 1 24  ? -22.647  44.755 17.477  1.00 136.22 ?  24  PHE A CE2 1 
ATOM 170  C CZ  . PHE A 1 24  ? -23.193  46.022 17.482  1.00 131.02 ?  24  PHE A CZ  1 
ATOM 171  N N   . SER A 1 25  ? -15.825  46.189 18.344  1.00 125.82 ?  25  SER A N   1 
ATOM 172  C CA  . SER A 1 25  ? -14.606  45.878 19.082  1.00 122.31 ?  25  SER A CA  1 
ATOM 173  C C   . SER A 1 25  ? -14.235  47.003 20.038  1.00 119.97 ?  25  SER A C   1 
ATOM 174  O O   . SER A 1 25  ? -13.598  46.754 21.068  1.00 128.80 ?  25  SER A O   1 
ATOM 175  C CB  . SER A 1 25  ? -13.458  45.600 18.113  1.00 124.15 ?  25  SER A CB  1 
ATOM 176  O OG  . SER A 1 25  ? -13.731  44.462 17.314  1.00 107.49 ?  25  SER A OG  1 
ATOM 177  N N   . LEU A 1 26  ? -14.616  48.231 19.717  1.00 112.86 ?  26  LEU A N   1 
ATOM 178  C CA  . LEU A 1 26  ? -14.416  49.370 20.603  1.00 123.70 ?  26  LEU A CA  1 
ATOM 179  C C   . LEU A 1 26  ? -15.296  49.217 21.836  1.00 122.77 ?  26  LEU A C   1 
ATOM 180  O O   . LEU A 1 26  ? -16.527  49.259 21.708  1.00 128.32 ?  26  LEU A O   1 
ATOM 181  C CB  . LEU A 1 26  ? -14.741  50.672 19.869  1.00 116.09 ?  26  LEU A CB  1 
ATOM 182  C CG  . LEU A 1 26  ? -14.982  51.923 20.717  1.00 111.89 ?  26  LEU A CG  1 
ATOM 183  C CD1 . LEU A 1 26  ? -13.718  52.330 21.463  1.00 125.62 ?  26  LEU A CD1 1 
ATOM 184  C CD2 . LEU A 1 26  ? -15.499  53.063 19.855  1.00 108.78 ?  26  LEU A CD2 1 
ATOM 185  N N   . PRO A 1 27  ? -14.732  49.031 23.027  1.00 129.71 ?  27  PRO A N   1 
ATOM 186  C CA  . PRO A 1 27  ? -15.548  48.807 24.228  1.00 130.85 ?  27  PRO A CA  1 
ATOM 187  C C   . PRO A 1 27  ? -15.881  50.059 25.026  1.00 133.68 ?  27  PRO A C   1 
ATOM 188  O O   . PRO A 1 27  ? -16.425  49.930 26.127  1.00 136.21 ?  27  PRO A O   1 
ATOM 189  C CB  . PRO A 1 27  ? -14.645  47.881 25.051  1.00 129.81 ?  27  PRO A CB  1 
ATOM 190  C CG  . PRO A 1 27  ? -13.263  48.385 24.743  1.00 139.50 ?  27  PRO A CG  1 
ATOM 191  C CD  . PRO A 1 27  ? -13.292  48.925 23.322  1.00 128.70 ?  27  PRO A CD  1 
ATOM 192  N N   . GLN A 1 28  ? -15.569  51.251 24.511  1.00 129.37 ?  28  GLN A N   1 
ATOM 193  C CA  . GLN A 1 28  ? -15.804  52.474 25.272  1.00 122.67 ?  28  GLN A CA  1 
ATOM 194  C C   . GLN A 1 28  ? -17.283  52.670 25.581  1.00 125.76 ?  28  GLN A C   1 
ATOM 195  O O   . GLN A 1 28  ? -17.626  53.251 26.618  1.00 127.35 ?  28  GLN A O   1 
ATOM 196  C CB  . GLN A 1 28  ? -15.249  53.677 24.508  1.00 120.22 ?  28  GLN A CB  1 
ATOM 197  C CG  . GLN A 1 28  ? -15.365  55.001 25.246  1.00 142.20 ?  28  GLN A CG  1 
ATOM 198  C CD  . GLN A 1 28  ? -14.219  55.943 24.930  1.00 146.43 ?  28  GLN A CD  1 
ATOM 199  O OE1 . GLN A 1 28  ? -13.185  55.526 24.408  1.00 141.10 ?  28  GLN A OE1 1 
ATOM 200  N NE2 . GLN A 1 28  ? -14.396  57.219 25.250  1.00 137.19 ?  28  GLN A NE2 1 
ATOM 201  N N   . MET A 1 29  ? -18.167  52.189 24.703  1.00 128.25 ?  29  MET A N   1 
ATOM 202  C CA  . MET A 1 29  ? -19.616  52.301 24.884  1.00 127.55 ?  29  MET A CA  1 
ATOM 203  C C   . MET A 1 29  ? -20.050  53.756 25.038  1.00 132.13 ?  29  MET A C   1 
ATOM 204  O O   . MET A 1 29  ? -21.046  54.056 25.701  1.00 121.50 ?  29  MET A O   1 
ATOM 205  C CB  . MET A 1 29  ? -20.093  51.466 26.078  1.00 116.06 ?  29  MET A CB  1 
ATOM 206  C CG  . MET A 1 29  ? -21.521  50.957 25.964  1.00 115.69 ?  29  MET A CG  1 
ATOM 207  S SD  . MET A 1 29  ? -21.709  49.686 24.700  1.00 155.77 ?  29  MET A SD  1 
ATOM 208  C CE  . MET A 1 29  ? -23.478  49.410 24.755  1.00 103.56 ?  29  MET A CE  1 
ATOM 209  N N   . ASP A 1 30  ? -19.300  54.670 24.429  1.00 125.91 ?  30  ASP A N   1 
ATOM 210  C CA  . ASP A 1 30  ? -19.586  56.093 24.506  1.00 117.91 ?  30  ASP A CA  1 
ATOM 211  C C   . ASP A 1 30  ? -19.338  56.705 23.133  1.00 140.17 ?  30  ASP A C   1 
ATOM 212  O O   . ASP A 1 30  ? -18.954  56.017 22.184  1.00 133.02 ?  30  ASP A O   1 
ATOM 213  C CB  . ASP A 1 30  ? -18.740  56.768 25.592  1.00 141.44 ?  30  ASP A CB  1 
ATOM 214  C CG  . ASP A 1 30  ? -19.381  58.033 26.127  1.00 163.34 ?  30  ASP A CG  1 
ATOM 215  O OD1 . ASP A 1 30  ? -20.526  58.334 25.730  1.00 170.58 ?  30  ASP A OD1 1 
ATOM 216  O OD2 . ASP A 1 30  ? -18.742  58.727 26.946  1.00 154.18 -1 30  ASP A OD2 1 
ATOM 217  N N   . ASP A 1 31  ? -19.556  58.016 23.031  1.00 159.41 ?  31  ASP A N   1 
ATOM 218  C CA  . ASP A 1 31  ? -19.486  58.719 21.749  1.00 172.77 ?  31  ASP A CA  1 
ATOM 219  C C   . ASP A 1 31  ? -18.042  59.125 21.443  1.00 179.21 ?  31  ASP A C   1 
ATOM 220  O O   . ASP A 1 31  ? -17.650  60.290 21.518  1.00 180.77 ?  31  ASP A O   1 
ATOM 221  C CB  . ASP A 1 31  ? -20.422  59.922 21.764  1.00 178.34 ?  31  ASP A CB  1 
ATOM 222  C CG  . ASP A 1 31  ? -20.162  60.854 22.940  1.00 179.68 ?  31  ASP A CG  1 
ATOM 223  O OD1 . ASP A 1 31  ? -19.541  61.919 22.735  1.00 177.05 ?  31  ASP A OD1 1 
ATOM 224  O OD2 . ASP A 1 31  ? -20.585  60.526 24.070  1.00 185.96 -1 31  ASP A OD2 1 
ATOM 225  N N   . SER A 1 32  ? -17.232  58.126 21.079  1.00 172.99 ?  32  SER A N   1 
ATOM 226  C CA  . SER A 1 32  ? -15.868  58.412 20.623  1.00 174.04 ?  32  SER A CA  1 
ATOM 227  C C   . SER A 1 32  ? -15.465  57.353 19.593  1.00 166.40 ?  32  SER A C   1 
ATOM 228  O O   . SER A 1 32  ? -14.957  56.288 19.952  1.00 161.03 ?  32  SER A O   1 
ATOM 229  C CB  . SER A 1 32  ? -14.894  58.453 21.791  1.00 162.79 ?  32  SER A CB  1 
ATOM 230  O OG  . SER A 1 32  ? -15.278  59.417 22.755  1.00 161.79 ?  32  SER A OG  1 
ATOM 231  N N   . ILE A 1 33  ? -15.710  57.665 18.316  1.00 160.57 ?  33  ILE A N   1 
ATOM 232  C CA  . ILE A 1 33  ? -15.133  56.949 17.178  1.00 159.25 ?  33  ILE A CA  1 
ATOM 233  C C   . ILE A 1 33  ? -15.478  57.699 15.894  1.00 150.83 ?  33  ILE A C   1 
ATOM 234  O O   . ILE A 1 33  ? -16.594  58.209 15.743  1.00 154.09 ?  33  ILE A O   1 
ATOM 235  C CB  . ILE A 1 33  ? -15.617  55.485 17.123  1.00 156.10 ?  33  ILE A CB  1 
ATOM 236  C CG1 . ILE A 1 33  ? -15.179  54.799 15.825  1.00 138.16 ?  33  ILE A CG1 1 
ATOM 237  C CG2 . ILE A 1 33  ? -17.115  55.412 17.295  1.00 161.99 ?  33  ILE A CG2 1 
ATOM 238  C CD1 . ILE A 1 33  ? -13.683  54.604 15.705  1.00 129.01 ?  33  ILE A CD1 1 
ATOM 239  N N   . ASP A 1 34  ? -14.535  57.759 14.957  1.00 151.40 ?  34  ASP A N   1 
ATOM 240  C CA  . ASP A 1 34  ? -14.758  58.332 13.637  1.00 140.66 ?  34  ASP A CA  1 
ATOM 241  C C   . ASP A 1 34  ? -14.718  57.230 12.584  1.00 130.17 ?  34  ASP A C   1 
ATOM 242  O O   . ASP A 1 34  ? -14.377  56.079 12.866  1.00 135.25 ?  34  ASP A O   1 
ATOM 243  C CB  . ASP A 1 34  ? -13.722  59.418 13.331  1.00 153.09 ?  34  ASP A CB  1 
ATOM 244  C CG  . ASP A 1 34  ? -14.269  60.818 13.538  1.00 152.80 ?  34  ASP A CG  1 
ATOM 245  O OD1 . ASP A 1 34  ? -15.343  61.128 12.979  1.00 149.25 ?  34  ASP A OD1 1 
ATOM 246  O OD2 . ASP A 1 34  ? -13.633  61.604 14.270  1.00 149.93 -1 34  ASP A OD2 1 
ATOM 247  N N   . ILE A 1 35  ? -15.069  57.595 11.354  1.00 117.54 ?  35  ILE A N   1 
ATOM 248  C CA  . ILE A 1 35  ? -15.297  56.617 10.297  1.00 121.83 ?  35  ILE A CA  1 
ATOM 249  C C   . ILE A 1 35  ? -14.661  57.101 8.999   1.00 124.77 ?  35  ILE A C   1 
ATOM 250  O O   . ILE A 1 35  ? -14.652  58.301 8.704   1.00 120.99 ?  35  ILE A O   1 
ATOM 251  C CB  . ILE A 1 35  ? -16.807  56.350 10.111  1.00 118.60 ?  35  ILE A CB  1 
ATOM 252  C CG1 . ILE A 1 35  ? -17.045  55.187 9.147   1.00 115.84 ?  35  ILE A CG1 1 
ATOM 253  C CG2 . ILE A 1 35  ? -17.534  57.611 9.652   1.00 131.39 ?  35  ILE A CG2 1 
ATOM 254  C CD1 . ILE A 1 35  ? -18.493  54.765 9.058   1.00 104.64 ?  35  ILE A CD1 1 
ATOM 255  N N   . GLU A 1 36  ? -14.109  56.159 8.233   1.00 123.21 ?  36  GLU A N   1 
ATOM 256  C CA  . GLU A 1 36  ? -13.694  56.421 6.858   1.00 124.27 ?  36  GLU A CA  1 
ATOM 257  C C   . GLU A 1 36  ? -14.946  56.666 6.023   1.00 124.92 ?  36  GLU A C   1 
ATOM 258  O O   . GLU A 1 36  ? -15.740  55.745 5.800   1.00 132.23 ?  36  GLU A O   1 
ATOM 259  C CB  . GLU A 1 36  ? -12.886  55.240 6.329   1.00 111.16 ?  36  GLU A CB  1 
ATOM 260  C CG  . GLU A 1 36  ? -11.584  55.009 7.087   1.00 110.99 ?  36  GLU A CG  1 
ATOM 261  C CD  . GLU A 1 36  ? -10.918  53.695 6.729   1.00 121.31 ?  36  GLU A CD  1 
ATOM 262  O OE1 . GLU A 1 36  ? -11.588  52.837 6.118   1.00 121.89 ?  36  GLU A OE1 1 
ATOM 263  O OE2 . GLU A 1 36  ? -9.725   53.521 7.060   1.00 104.15 -1 36  GLU A OE2 1 
ATOM 264  N N   . CYS A 1 37  ? -15.133  57.904 5.562   1.00 129.75 ?  37  CYS A N   1 
ATOM 265  C CA  . CYS A 1 37  ? -16.490  58.403 5.298   1.00 144.01 ?  37  CYS A CA  1 
ATOM 266  C C   . CYS A 1 37  ? -16.989  58.245 3.863   1.00 138.72 ?  37  CYS A C   1 
ATOM 267  O O   . CYS A 1 37  ? -17.906  57.462 3.604   1.00 144.26 ?  37  CYS A O   1 
ATOM 268  C CB  . CYS A 1 37  ? -16.560  59.874 5.712   1.00 141.68 ?  37  CYS A CB  1 
ATOM 269  S SG  . CYS A 1 37  ? -18.147  60.397 6.400   1.00 137.14 ?  37  CYS A SG  1 
ATOM 270  N N   . ILE A 1 38  ? -16.370  58.939 2.914   1.00 122.93 ?  38  ILE A N   1 
ATOM 271  C CA  . ILE A 1 38  ? -17.065  59.332 1.688   1.00 133.28 ?  38  ILE A CA  1 
ATOM 272  C C   . ILE A 1 38  ? -16.946  58.247 0.623   1.00 136.97 ?  38  ILE A C   1 
ATOM 273  O O   . ILE A 1 38  ? -15.842  57.787 0.305   1.00 142.86 ?  38  ILE A O   1 
ATOM 274  C CB  . ILE A 1 38  ? -16.535  60.681 1.167   1.00 129.78 ?  38  ILE A CB  1 
ATOM 275  C CG1 . ILE A 1 38  ? -17.073  60.964 -0.238  1.00 141.25 ?  38  ILE A CG1 1 
ATOM 276  C CG2 . ILE A 1 38  ? -15.013  60.713 1.196   1.00 143.28 ?  38  ILE A CG2 1 
ATOM 277  C CD1 . ILE A 1 38  ? -16.712  62.337 -0.767  1.00 123.09 ?  38  ILE A CD1 1 
ATOM 278  N N   . GLU A 1 39  ? -18.094  57.831 0.076   1.00 132.28 ?  39  GLU A N   1 
ATOM 279  C CA  . GLU A 1 39  ? -18.139  56.939 -1.082  1.00 130.54 ?  39  GLU A CA  1 
ATOM 280  C C   . GLU A 1 39  ? -18.839  57.575 -2.277  1.00 133.35 ?  39  GLU A C   1 
ATOM 281  O O   . GLU A 1 39  ? -18.244  57.650 -3.358  1.00 136.83 ?  39  GLU A O   1 
ATOM 282  C CB  . GLU A 1 39  ? -18.820  55.615 -0.706  1.00 124.85 ?  39  GLU A CB  1 
ATOM 283  C CG  . GLU A 1 39  ? -18.569  55.154 0.723   1.00 118.77 ?  39  GLU A CG  1 
ATOM 284  C CD  . GLU A 1 39  ? -17.158  54.632 0.945   1.00 127.35 ?  39  GLU A CD  1 
ATOM 285  O OE1 . GLU A 1 39  ? -16.346  54.654 -0.005  1.00 154.39 ?  39  GLU A OE1 1 
ATOM 286  O OE2 . GLU A 1 39  ? -16.857  54.196 2.076   1.00 133.03 -1 39  GLU A OE2 1 
ATOM 287  N N   . ASP A 1 40  ? -20.083  58.040 -2.117  1.00 134.75 ?  40  ASP A N   1 
ATOM 288  C CA  . ASP A 1 40  ? -20.859  58.692 -3.178  1.00 141.52 ?  40  ASP A CA  1 
ATOM 289  C C   . ASP A 1 40  ? -20.984  57.781 -4.406  1.00 148.84 ?  40  ASP A C   1 
ATOM 290  O O   . ASP A 1 40  ? -20.466  58.062 -5.488  1.00 159.32 ?  40  ASP A O   1 
ATOM 291  C CB  . ASP A 1 40  ? -20.243  60.047 -3.550  1.00 146.57 ?  40  ASP A CB  1 
ATOM 292  C CG  . ASP A 1 40  ? -21.139  60.867 -4.458  1.00 156.96 ?  40  ASP A CG  1 
ATOM 293  O OD1 . ASP A 1 40  ? -22.095  61.487 -3.948  1.00 153.78 ?  40  ASP A OD1 1 
ATOM 294  O OD2 . ASP A 1 40  ? -20.887  60.890 -5.681  1.00 155.11 -1 40  ASP A OD2 1 
ATOM 295  N N   . VAL A 1 41  ? -21.692  56.672 -4.205  1.00 122.79 ?  41  VAL A N   1 
ATOM 296  C CA  . VAL A 1 41  ? -21.733  55.591 -5.183  1.00 129.21 ?  41  VAL A CA  1 
ATOM 297  C C   . VAL A 1 41  ? -23.004  55.622 -6.026  1.00 148.36 ?  41  VAL A C   1 
ATOM 298  O O   . VAL A 1 41  ? -22.934  55.456 -7.245  1.00 159.72 ?  41  VAL A O   1 
ATOM 299  C CB  . VAL A 1 41  ? -21.569  54.228 -4.478  1.00 125.34 ?  41  VAL A CB  1 
ATOM 300  C CG1 . VAL A 1 41  ? -21.758  53.086 -5.464  1.00 109.16 ?  41  VAL A CG1 1 
ATOM 301  C CG2 . VAL A 1 41  ? -20.211  54.139 -3.806  1.00 121.74 ?  41  VAL A CG2 1 
ATOM 302  N N   . ASP A 1 42  ? -24.172  55.829 -5.407  1.00 143.49 ?  42  ASP A N   1 
ATOM 303  C CA  . ASP A 1 42  ? -25.451  55.838 -6.127  1.00 151.88 ?  42  ASP A CA  1 
ATOM 304  C C   . ASP A 1 42  ? -25.688  54.494 -6.829  1.00 141.26 ?  42  ASP A C   1 
ATOM 305  O O   . ASP A 1 42  ? -25.577  54.363 -8.049  1.00 140.29 ?  42  ASP A O   1 
ATOM 306  C CB  . ASP A 1 42  ? -25.530  57.006 -7.118  1.00 178.55 ?  42  ASP A CB  1 
ATOM 307  C CG  . ASP A 1 42  ? -26.958  57.354 -7.490  1.00 177.85 ?  42  ASP A CG  1 
ATOM 308  O OD1 . ASP A 1 42  ? -27.506  58.318 -6.917  1.00 168.73 ?  42  ASP A OD1 1 
ATOM 309  O OD2 . ASP A 1 42  ? -27.537  56.655 -8.350  1.00 179.22 -1 42  ASP A OD2 1 
ATOM 310  N N   . VAL A 1 43  ? -26.027  53.497 -6.008  1.00 136.28 ?  43  VAL A N   1 
ATOM 311  C CA  . VAL A 1 43  ? -25.871  52.072 -6.299  1.00 117.48 ?  43  VAL A CA  1 
ATOM 312  C C   . VAL A 1 43  ? -26.940  51.567 -7.265  1.00 119.12 ?  43  VAL A C   1 
ATOM 313  O O   . VAL A 1 43  ? -27.111  50.353 -7.436  1.00 114.07 ?  43  VAL A O   1 
ATOM 314  C CB  . VAL A 1 43  ? -25.902  51.267 -4.984  1.00 107.82 ?  43  VAL A CB  1 
ATOM 315  C CG1 . VAL A 1 43  ? -25.260  49.891 -5.143  1.00 82.14  ?  43  VAL A CG1 1 
ATOM 316  C CG2 . VAL A 1 43  ? -25.225  52.046 -3.873  1.00 106.31 ?  43  VAL A CG2 1 
ATOM 317  N N   . TYR A 1 44  ? -27.688  52.490 -7.879  1.00 136.88 ?  44  TYR A N   1 
ATOM 318  C CA  . TYR A 1 44  ? -28.666  52.117 -8.901  1.00 146.38 ?  44  TYR A CA  1 
ATOM 319  C C   . TYR A 1 44  ? -28.090  51.119 -9.903  1.00 139.91 ?  44  TYR A C   1 
ATOM 320  O O   . TYR A 1 44  ? -28.726  50.110 -10.227 1.00 132.38 ?  44  TYR A O   1 
ATOM 321  C CB  . TYR A 1 44  ? -29.163  53.369 -9.627  1.00 136.46 ?  44  TYR A CB  1 
ATOM 322  C CG  . TYR A 1 44  ? -30.586  53.279 -10.142 1.00 138.09 ?  44  TYR A CG  1 
ATOM 323  C CD1 . TYR A 1 44  ? -31.318  54.427 -10.412 1.00 143.91 ?  44  TYR A CD1 1 
ATOM 324  C CD2 . TYR A 1 44  ? -31.194  52.049 -10.364 1.00 146.00 ?  44  TYR A CD2 1 
ATOM 325  C CE1 . TYR A 1 44  ? -32.614  54.354 -10.888 1.00 152.11 ?  44  TYR A CE1 1 
ATOM 326  C CE2 . TYR A 1 44  ? -32.491  51.965 -10.839 1.00 153.00 ?  44  TYR A CE2 1 
ATOM 327  C CZ  . TYR A 1 44  ? -33.196  53.122 -11.099 1.00 155.40 ?  44  TYR A CZ  1 
ATOM 328  O OH  . TYR A 1 44  ? -34.486  53.045 -11.571 1.00 158.36 ?  44  TYR A OH  1 
ATOM 329  N N   . ASN A 1 45  ? -26.884  51.383 -10.406 1.00 130.28 ?  45  ASN A N   1 
ATOM 330  C CA  . ASN A 1 45  ? -26.238  50.519 -11.388 1.00 131.90 ?  45  ASN A CA  1 
ATOM 331  C C   . ASN A 1 45  ? -25.081  49.718 -10.809 1.00 143.38 ?  45  ASN A C   1 
ATOM 332  O O   . ASN A 1 45  ? -25.023  48.500 -11.000 1.00 150.03 ?  45  ASN A O   1 
ATOM 333  C CB  . ASN A 1 45  ? -25.751  51.354 -12.581 1.00 141.69 ?  45  ASN A CB  1 
ATOM 334  C CG  . ASN A 1 45  ? -26.891  52.012 -13.335 1.00 149.98 ?  45  ASN A CG  1 
ATOM 335  O OD1 . ASN A 1 45  ? -27.986  52.183 -12.800 1.00 147.00 ?  45  ASN A OD1 1 
ATOM 336  N ND2 . ASN A 1 45  ? -26.639  52.383 -14.586 1.00 142.18 ?  45  ASN A ND2 1 
ATOM 337  N N   . ASP A 1 46  ? -24.133  50.383 -10.146 1.00 140.94 ?  46  ASP A N   1 
ATOM 338  C CA  . ASP A 1 46  ? -23.061  49.819 -9.323  1.00 129.89 ?  46  ASP A CA  1 
ATOM 339  C C   . ASP A 1 46  ? -22.041  48.988 -10.097 1.00 135.90 ?  46  ASP A C   1 
ATOM 340  O O   . ASP A 1 46  ? -21.093  48.482 -9.482  1.00 125.85 ?  46  ASP A O   1 
ATOM 341  C CB  . ASP A 1 46  ? -23.603  48.977 -8.154  1.00 127.12 ?  46  ASP A CB  1 
ATOM 342  C CG  . ASP A 1 46  ? -23.904  47.536 -8.540  1.00 120.92 ?  46  ASP A CG  1 
ATOM 343  O OD1 . ASP A 1 46  ? -22.972  46.704 -8.557  1.00 110.49 ?  46  ASP A OD1 1 
ATOM 344  O OD2 . ASP A 1 46  ? -25.083  47.229 -8.817  1.00 135.08 -1 46  ASP A OD2 1 
ATOM 345  N N   . GLY A 1 47  ? -22.185  48.832 -11.413 1.00 139.94 ?  47  GLY A N   1 
ATOM 346  C CA  . GLY A 1 47  ? -21.230  48.023 -12.154 1.00 119.76 ?  47  GLY A CA  1 
ATOM 347  C C   . GLY A 1 47  ? -19.846  48.645 -12.206 1.00 119.69 ?  47  GLY A C   1 
ATOM 348  O O   . GLY A 1 47  ? -18.835  47.944 -12.112 1.00 126.95 ?  47  GLY A O   1 
ATOM 349  N N   . HIS A 1 48  ? -19.784  49.963 -12.354 1.00 118.21 ?  48  HIS A N   1 
ATOM 350  C CA  . HIS A 1 48  ? -18.549  50.722 -12.452 1.00 127.58 ?  48  HIS A CA  1 
ATOM 351  C C   . HIS A 1 48  ? -18.262  51.399 -11.111 1.00 129.93 ?  48  HIS A C   1 
ATOM 352  O O   . HIS A 1 48  ? -18.856  51.059 -10.082 1.00 126.18 ?  48  HIS A O   1 
ATOM 353  C CB  . HIS A 1 48  ? -18.640  51.721 -13.608 1.00 131.39 ?  48  HIS A CB  1 
ATOM 354  C CG  . HIS A 1 48  ? -18.758  51.077 -14.957 1.00 152.09 ?  48  HIS A CG  1 
ATOM 355  N ND1 . HIS A 1 48  ? -19.530  49.959 -15.186 1.00 152.88 ?  48  HIS A ND1 1 
ATOM 356  C CD2 . HIS A 1 48  ? -18.201  51.399 -16.149 1.00 162.62 ?  48  HIS A CD2 1 
ATOM 357  C CE1 . HIS A 1 48  ? -19.443  49.618 -16.459 1.00 153.70 ?  48  HIS A CE1 1 
ATOM 358  N NE2 . HIS A 1 48  ? -18.643  50.476 -17.066 1.00 151.11 ?  48  HIS A NE2 1 
ATOM 359  N N   . LEU A 1 49  ? -17.327  52.354 -11.112 1.00 122.46 ?  49  LEU A N   1 
ATOM 360  C CA  . LEU A 1 49  ? -16.972  53.132 -9.921  1.00 131.85 ?  49  LEU A CA  1 
ATOM 361  C C   . LEU A 1 49  ? -16.407  52.223 -8.824  1.00 123.57 ?  49  LEU A C   1 
ATOM 362  O O   . LEU A 1 49  ? -17.021  51.975 -7.785  1.00 121.39 ?  49  LEU A O   1 
ATOM 363  C CB  . LEU A 1 49  ? -18.174  53.943 -9.414  1.00 131.67 ?  49  LEU A CB  1 
ATOM 364  C CG  . LEU A 1 49  ? -18.460  55.275 -10.115 1.00 129.20 ?  49  LEU A CG  1 
ATOM 365  C CD1 . LEU A 1 49  ? -18.922  55.070 -11.552 1.00 104.37 ?  49  LEU A CD1 1 
ATOM 366  C CD2 . LEU A 1 49  ? -19.488  56.073 -9.333  1.00 138.00 ?  49  LEU A CD2 1 
ATOM 367  N N   . THR A 1 50  ? -15.201  51.730 -9.102  1.00 122.20 ?  50  THR A N   1 
ATOM 368  C CA  . THR A 1 50  ? -14.571  50.630 -8.374  1.00 125.27 ?  50  THR A CA  1 
ATOM 369  C C   . THR A 1 50  ? -13.567  51.111 -7.330  1.00 125.09 ?  50  THR A C   1 
ATOM 370  O O   . THR A 1 50  ? -12.474  50.549 -7.214  1.00 117.98 ?  50  THR A O   1 
ATOM 371  C CB  . THR A 1 50  ? -13.889  49.679 -9.352  1.00 135.75 ?  50  THR A CB  1 
ATOM 372  O OG1 . THR A 1 50  ? -12.619  50.223 -9.736  1.00 139.44 ?  50  THR A OG1 1 
ATOM 373  C CG2 . THR A 1 50  ? -14.746  49.489 -10.599 1.00 131.59 ?  50  THR A CG2 1 
ATOM 374  N N   . ALA A 1 51  ? -13.896  52.162 -6.574  1.00 110.48 ?  51  ALA A N   1 
ATOM 375  C CA  . ALA A 1 51  ? -12.984  52.689 -5.561  1.00 100.73 ?  51  ALA A CA  1 
ATOM 376  C C   . ALA A 1 51  ? -12.593  51.666 -4.495  1.00 92.55  ?  51  ALA A C   1 
ATOM 377  O O   . ALA A 1 51  ? -11.679  51.945 -3.711  1.00 96.31  ?  51  ALA A O   1 
ATOM 378  C CB  . ALA A 1 51  ? -13.600  53.916 -4.884  1.00 108.61 ?  51  ALA A CB  1 
ATOM 379  N N   . ILE A 1 52  ? -13.246  50.505 -4.439  1.00 81.24  ?  52  ILE A N   1 
ATOM 380  C CA  . ILE A 1 52  ? -12.932  49.468 -3.460  1.00 85.77  ?  52  ILE A CA  1 
ATOM 381  C C   . ILE A 1 52  ? -13.053  48.108 -4.139  1.00 92.11  ?  52  ILE A C   1 
ATOM 382  O O   . ILE A 1 52  ? -13.997  47.867 -4.899  1.00 95.52  ?  52  ILE A O   1 
ATOM 383  C CB  . ILE A 1 52  ? -13.858  49.557 -2.226  1.00 90.43  ?  52  ILE A CB  1 
ATOM 384  C CG1 . ILE A 1 52  ? -13.497  50.771 -1.366  1.00 86.08  ?  52  ILE A CG1 1 
ATOM 385  C CG2 . ILE A 1 52  ? -13.765  48.296 -1.390  1.00 81.85  ?  52  ILE A CG2 1 
ATOM 386  C CD1 . ILE A 1 52  ? -14.309  50.881 -0.091  1.00 75.74  ?  52  ILE A CD1 1 
ATOM 387  N N   . GLN A 1 53  ? -12.098  47.216 -3.870  1.00 89.86  ?  53  GLN A N   1 
ATOM 388  C CA  . GLN A 1 53  ? -12.106  45.890 -4.475  1.00 92.97  ?  53  GLN A CA  1 
ATOM 389  C C   . GLN A 1 53  ? -11.507  44.880 -3.508  1.00 87.57  ?  53  GLN A C   1 
ATOM 390  O O   . GLN A 1 53  ? -10.920  45.238 -2.485  1.00 89.74  ?  53  GLN A O   1 
ATOM 391  C CB  . GLN A 1 53  ? -11.335  45.867 -5.801  1.00 80.49  ?  53  GLN A CB  1 
ATOM 392  C CG  . GLN A 1 53  ? -12.175  46.207 -7.019  1.00 104.50 ?  53  GLN A CG  1 
ATOM 393  C CD  . GLN A 1 53  ? -11.519  45.781 -8.315  1.00 116.82 ?  53  GLN A CD  1 
ATOM 394  O OE1 . GLN A 1 53  ? -10.383  45.305 -8.326  1.00 117.15 ?  53  GLN A OE1 1 
ATOM 395  N NE2 . GLN A 1 53  ? -12.240  45.937 -9.418  1.00 108.66 ?  53  GLN A NE2 1 
ATOM 396  N N   . CYS A 1 54  ? -11.663  43.603 -3.850  1.00 85.86  ?  54  CYS A N   1 
ATOM 397  C CA  . CYS A 1 54  ? -11.103  42.517 -3.059  1.00 85.77  ?  54  CYS A CA  1 
ATOM 398  C C   . CYS A 1 54  ? -10.917  41.314 -3.966  1.00 95.45  ?  54  CYS A C   1 
ATOM 399  O O   . CYS A 1 54  ? -11.848  40.934 -4.681  1.00 104.07 ?  54  CYS A O   1 
ATOM 400  C CB  . CYS A 1 54  ? -12.018  42.159 -1.889  1.00 99.68  ?  54  CYS A CB  1 
ATOM 401  S SG  . CYS A 1 54  ? -11.173  41.652 -0.388  1.00 138.68 ?  54  CYS A SG  1 
ATOM 402  N N   . LYS A 1 55  ? -9.725   40.719 -3.934  1.00 99.31  ?  55  LYS A N   1 
ATOM 403  C CA  . LYS A 1 55  ? -9.372   39.609 -4.809  1.00 96.34  ?  55  LYS A CA  1 
ATOM 404  C C   . LYS A 1 55  ? -8.965   38.404 -3.973  1.00 100.83 ?  55  LYS A C   1 
ATOM 405  O O   . LYS A 1 55  ? -8.285   38.544 -2.952  1.00 100.31 ?  55  LYS A O   1 
ATOM 406  C CB  . LYS A 1 55  ? -8.229   39.984 -5.764  1.00 86.80  ?  55  LYS A CB  1 
ATOM 407  C CG  . LYS A 1 55  ? -8.101   41.472 -6.075  1.00 81.57  ?  55  LYS A CG  1 
ATOM 408  C CD  . LYS A 1 55  ? -9.281   41.968 -6.893  1.00 75.04  ?  55  LYS A CD  1 
ATOM 409  C CE  . LYS A 1 55  ? -8.887   42.278 -8.327  1.00 93.85  ?  55  LYS A CE  1 
ATOM 410  N NZ  . LYS A 1 55  ? -9.946   43.047 -9.044  1.00 114.03 ?  55  LYS A NZ  1 
ATOM 411  N N   . TYR A 1 56  ? -9.376   37.218 -4.415  1.00 111.76 ?  56  TYR A N   1 
ATOM 412  C CA  . TYR A 1 56  ? -9.140   35.984 -3.672  1.00 100.91 ?  56  TYR A CA  1 
ATOM 413  C C   . TYR A 1 56  ? -8.640   34.882 -4.598  1.00 114.95 ?  56  TYR A C   1 
ATOM 414  O O   . TYR A 1 56  ? -9.197   33.785 -4.652  1.00 126.62 ?  56  TYR A O   1 
ATOM 415  C CB  . TYR A 1 56  ? -10.386  35.534 -2.913  1.00 109.95 ?  56  TYR A CB  1 
ATOM 416  C CG  . TYR A 1 56  ? -10.783  36.482 -1.811  1.00 120.29 ?  56  TYR A CG  1 
ATOM 417  C CD1 . TYR A 1 56  ? -10.344  36.282 -0.509  1.00 120.06 ?  56  TYR A CD1 1 
ATOM 418  C CD2 . TYR A 1 56  ? -11.604  37.573 -2.065  1.00 119.34 ?  56  TYR A CD2 1 
ATOM 419  C CE1 . TYR A 1 56  ? -10.699  37.151 0.508   1.00 122.01 ?  56  TYR A CE1 1 
ATOM 420  C CE2 . TYR A 1 56  ? -11.968  38.444 -1.054  1.00 112.05 ?  56  TYR A CE2 1 
ATOM 421  C CZ  . TYR A 1 56  ? -11.512  38.234 0.233   1.00 125.38 ?  56  TYR A CZ  1 
ATOM 422  O OH  . TYR A 1 56  ? -11.873  39.104 1.247   1.00 139.73 ?  56  TYR A OH  1 
ATOM 423  N N   . TYR A 1 57  ? -7.576   35.160 -5.352  1.00 128.51 ?  57  TYR A N   1 
ATOM 424  C CA  . TYR A 1 57  ? -6.941   34.076 -6.091  1.00 130.60 ?  57  TYR A CA  1 
ATOM 425  C C   . TYR A 1 57  ? -6.108   33.227 -5.140  1.00 128.41 ?  57  TYR A C   1 
ATOM 426  O O   . TYR A 1 57  ? -4.900   33.080 -5.337  1.00 126.71 ?  57  TYR A O   1 
ATOM 427  C CB  . TYR A 1 57  ? -6.048   34.597 -7.222  1.00 135.84 ?  57  TYR A CB  1 
ATOM 428  C CG  . TYR A 1 57  ? -6.718   35.392 -8.330  1.00 146.28 ?  57  TYR A CG  1 
ATOM 429  C CD1 . TYR A 1 57  ? -8.030   35.833 -8.227  1.00 142.33 ?  57  TYR A CD1 1 
ATOM 430  C CD2 . TYR A 1 57  ? -6.013   35.706 -9.488  1.00 140.34 ?  57  TYR A CD2 1 
ATOM 431  C CE1 . TYR A 1 57  ? -8.623   36.561 -9.251  1.00 138.61 ?  57  TYR A CE1 1 
ATOM 432  C CE2 . TYR A 1 57  ? -6.593   36.429 -10.509 1.00 133.14 ?  57  TYR A CE2 1 
ATOM 433  C CZ  . TYR A 1 57  ? -7.897   36.856 -10.389 1.00 133.04 ?  57  TYR A CZ  1 
ATOM 434  O OH  . TYR A 1 57  ? -8.460   37.576 -11.418 1.00 126.29 ?  57  TYR A OH  1 
ATOM 435  N N   . GLU A 1 58  ? -6.739   32.676 -4.098  1.00 137.46 ?  58  GLU A N   1 
ATOM 436  C CA  . GLU A 1 58  ? -5.996   31.910 -3.101  1.00 143.01 ?  58  GLU A CA  1 
ATOM 437  C C   . GLU A 1 58  ? -5.397   30.647 -3.711  1.00 165.37 ?  58  GLU A C   1 
ATOM 438  O O   . GLU A 1 58  ? -4.317   30.202 -3.308  1.00 172.74 ?  58  GLU A O   1 
ATOM 439  C CB  . GLU A 1 58  ? -6.905   31.567 -1.918  1.00 150.27 ?  58  GLU A CB  1 
ATOM 440  C CG  . GLU A 1 58  ? -6.395   30.431 -1.047  1.00 161.79 ?  58  GLU A CG  1 
ATOM 441  C CD  . GLU A 1 58  ? -7.140   29.131 -1.277  1.00 190.21 ?  58  GLU A CD  1 
ATOM 442  O OE1 . GLU A 1 58  ? -8.371   29.100 -1.062  1.00 193.16 ?  58  GLU A OE1 1 
ATOM 443  O OE2 . GLU A 1 58  ? -6.495   28.144 -1.691  1.00 219.80 -1 58  GLU A OE2 1 
ATOM 444  N N   . SER A 1 59  ? -6.092   30.054 -4.686  1.00 182.51 ?  59  SER A N   1 
ATOM 445  C CA  . SER A 1 59  ? -5.574   28.902 -5.420  1.00 178.79 ?  59  SER A CA  1 
ATOM 446  C C   . SER A 1 59  ? -4.232   29.191 -6.080  1.00 168.49 ?  59  SER A C   1 
ATOM 447  O O   . SER A 1 59  ? -3.501   28.259 -6.425  1.00 169.33 ?  59  SER A O   1 
ATOM 448  C CB  . SER A 1 59  ? -6.601   28.465 -6.470  1.00 171.55 ?  59  SER A CB  1 
ATOM 449  O OG  . SER A 1 59  ? -6.315   27.174 -6.984  1.00 171.38 ?  59  SER A OG  1 
ATOM 450  N N   . THR A 1 60  ? -3.903   30.458 -6.267  1.00 159.92 ?  60  THR A N   1 
ATOM 451  C CA  . THR A 1 60  ? -2.638   30.929 -6.812  1.00 157.68 ?  60  THR A CA  1 
ATOM 452  C C   . THR A 1 60  ? -2.026   31.943 -5.848  1.00 140.55 ?  60  THR A C   1 
ATOM 453  O O   . THR A 1 60  ? -2.494   32.130 -4.721  1.00 131.89 ?  60  THR A O   1 
ATOM 454  C CB  . THR A 1 60  ? -2.842   31.530 -8.205  1.00 159.83 ?  60  THR A CB  1 
ATOM 455  O OG1 . THR A 1 60  ? -4.099   32.223 -8.233  1.00 164.61 ?  60  THR A OG1 1 
ATOM 456  C CG2 . THR A 1 60  ? -2.843   30.429 -9.259  1.00 157.27 ?  60  THR A CG2 1 
ATOM 457  N N   . ASP A 1 61  ? -0.965   32.596 -6.299  1.00 129.22 ?  61  ASP A N   1 
ATOM 458  C CA  . ASP A 1 61  ? -0.240   33.559 -5.490  1.00 124.73 ?  61  ASP A CA  1 
ATOM 459  C C   . ASP A 1 61  ? -0.395   34.963 -6.059  1.00 111.03 ?  61  ASP A C   1 
ATOM 460  O O   . ASP A 1 61  ? -0.739   35.153 -7.229  1.00 121.44 ?  61  ASP A O   1 
ATOM 461  C CB  . ASP A 1 61  ? 1.245    33.184 -5.413  1.00 138.19 ?  61  ASP A CB  1 
ATOM 462  C CG  . ASP A 1 61  ? 1.457    31.692 -5.342  1.00 147.61 ?  61  ASP A CG  1 
ATOM 463  O OD1 . ASP A 1 61  ? 1.917    31.110 -6.348  1.00 156.65 ?  61  ASP A OD1 1 
ATOM 464  O OD2 . ASP A 1 61  ? 1.171    31.099 -4.280  1.00 156.24 -1 61  ASP A OD2 1 
ATOM 465  N N   . TYR A 1 62  ? -0.156   35.952 -5.200  1.00 97.17  ?  62  TYR A N   1 
ATOM 466  C CA  . TYR A 1 62  ? -0.056   37.328 -5.663  1.00 97.71  ?  62  TYR A CA  1 
ATOM 467  C C   . TYR A 1 62  ? 1.117    37.456 -6.627  1.00 106.78 ?  62  TYR A C   1 
ATOM 468  O O   . TYR A 1 62  ? 2.208    36.945 -6.364  1.00 102.93 ?  62  TYR A O   1 
ATOM 469  C CB  . TYR A 1 62  ? 0.107    38.278 -4.479  1.00 80.16  ?  62  TYR A CB  1 
ATOM 470  C CG  . TYR A 1 62  ? 0.565    39.651 -4.886  1.00 85.53  ?  62  TYR A CG  1 
ATOM 471  C CD1 . TYR A 1 62  ? 1.859    40.076 -4.623  1.00 86.66  ?  62  TYR A CD1 1 
ATOM 472  C CD2 . TYR A 1 62  ? -0.292   40.517 -5.546  1.00 86.09  ?  62  TYR A CD2 1 
ATOM 473  C CE1 . TYR A 1 62  ? 2.283    41.324 -4.999  1.00 91.73  ?  62  TYR A CE1 1 
ATOM 474  C CE2 . TYR A 1 62  ? 0.124    41.765 -5.924  1.00 84.54  ?  62  TYR A CE2 1 
ATOM 475  C CZ  . TYR A 1 62  ? 1.410    42.166 -5.649  1.00 93.09  ?  62  TYR A CZ  1 
ATOM 476  O OH  . TYR A 1 62  ? 1.823    43.417 -6.029  1.00 104.10 ?  62  TYR A OH  1 
ATOM 477  N N   . ASN A 1 63  ? 0.886    38.137 -7.750  1.00 97.24  ?  63  ASN A N   1 
ATOM 478  C CA  . ASN A 1 63  ? 1.818    38.134 -8.866  1.00 94.85  ?  63  ASN A CA  1 
ATOM 479  C C   . ASN A 1 63  ? 2.105    39.523 -9.425  1.00 110.32 ?  63  ASN A C   1 
ATOM 480  O O   . ASN A 1 63  ? 2.834    39.631 -10.417 1.00 130.50 ?  63  ASN A O   1 
ATOM 481  C CB  . ASN A 1 63  ? 1.268    37.220 -9.979  1.00 107.79 ?  63  ASN A CB  1 
ATOM 482  C CG  . ASN A 1 63  ? 2.324    36.802 -10.987 1.00 133.66 ?  63  ASN A CG  1 
ATOM 483  O OD1 . ASN A 1 63  ? 3.512    36.725 -10.670 1.00 130.54 ?  63  ASN A OD1 1 
ATOM 484  N ND2 . ASN A 1 63  ? 1.890    36.515 -12.208 1.00 125.61 ?  63  ASN A ND2 1 
ATOM 485  N N   . HIS A 1 64  ? 1.539    40.577 -8.829  1.00 90.77  ?  64  HIS A N   1 
ATOM 486  C CA  . HIS A 1 64  ? 1.690    41.972 -9.247  1.00 95.66  ?  64  HIS A CA  1 
ATOM 487  C C   . HIS A 1 64  ? 0.968    42.242 -10.556 1.00 105.40 ?  64  HIS A C   1 
ATOM 488  O O   . HIS A 1 64  ? 0.800    43.402 -10.944 1.00 111.67 ?  64  HIS A O   1 
ATOM 489  C CB  . HIS A 1 64  ? 3.147    42.384 -9.464  1.00 97.01  ?  64  HIS A CB  1 
ATOM 490  C CG  . HIS A 1 64  ? 4.067    42.033 -8.342  1.00 96.22  ?  64  HIS A CG  1 
ATOM 491  N ND1 . HIS A 1 64  ? 4.423    42.933 -7.362  1.00 103.40 ?  64  HIS A ND1 1 
ATOM 492  C CD2 . HIS A 1 64  ? 4.733    40.890 -8.061  1.00 93.06  ?  64  HIS A CD2 1 
ATOM 493  C CE1 . HIS A 1 64  ? 5.259    42.359 -6.517  1.00 102.60 ?  64  HIS A CE1 1 
ATOM 494  N NE2 . HIS A 1 64  ? 5.462    41.117 -6.918  1.00 101.81 ?  64  HIS A NE2 1 
ATOM 495  N N   . SER A 1 65  ? 0.541    41.185 -11.247 1.00 95.40  ?  65  SER A N   1 
ATOM 496  C CA  . SER A 1 65  ? -0.124   41.339 -12.531 1.00 95.56  ?  65  SER A CA  1 
ATOM 497  C C   . SER A 1 65  ? -1.621   41.119 -12.431 1.00 106.10 ?  65  SER A C   1 
ATOM 498  O O   . SER A 1 65  ? -2.361   41.549 -13.320 1.00 103.50 ?  65  SER A O   1 
ATOM 499  C CB  . SER A 1 65  ? 0.488    40.389 -13.573 1.00 88.32  ?  65  SER A CB  1 
ATOM 500  O OG  . SER A 1 65  ? 0.579    39.057 -13.094 1.00 104.55 ?  65  SER A OG  1 
ATOM 501  N N   . VAL A 1 66  ? -2.073   40.477 -11.357 1.00 103.72 ?  66  VAL A N   1 
ATOM 502  C CA  . VAL A 1 66  ? -3.498   40.315 -11.119 1.00 101.12 ?  66  VAL A CA  1 
ATOM 503  C C   . VAL A 1 66  ? -4.116   41.628 -10.646 1.00 104.31 ?  66  VAL A C   1 
ATOM 504  O O   . VAL A 1 66  ? -5.248   41.962 -11.018 1.00 110.07 ?  66  VAL A O   1 
ATOM 505  C CB  . VAL A 1 66  ? -3.719   39.156 -10.130 1.00 105.90 ?  66  VAL A CB  1 
ATOM 506  C CG1 . VAL A 1 66  ? -3.199   37.861 -10.737 1.00 102.52 ?  66  VAL A CG1 1 
ATOM 507  C CG2 . VAL A 1 66  ? -2.980   39.421 -8.827  1.00 98.46  ?  66  VAL A CG2 1 
ATOM 508  N N   . ILE A 1 67  ? -3.381   42.407 -9.848  1.00 89.29  ?  67  ILE A N   1 
ATOM 509  C CA  . ILE A 1 67  ? -3.885   43.670 -9.320  1.00 89.75  ?  67  ILE A CA  1 
ATOM 510  C C   . ILE A 1 67  ? -3.259   44.877 -10.015 1.00 93.66  ?  67  ILE A C   1 
ATOM 511  O O   . ILE A 1 67  ? -3.473   46.013 -9.580  1.00 79.42  ?  67  ILE A O   1 
ATOM 512  C CB  . ILE A 1 67  ? -3.694   43.754 -7.795  1.00 90.44  ?  67  ILE A CB  1 
ATOM 513  C CG1 . ILE A 1 67  ? -2.245   44.097 -7.433  1.00 98.62  ?  67  ILE A CG1 1 
ATOM 514  C CG2 . ILE A 1 67  ? -4.099   42.452 -7.128  1.00 81.13  ?  67  ILE A CG2 1 
ATOM 515  C CD1 . ILE A 1 67  ? -2.051   44.421 -5.960  1.00 90.57  ?  67  ILE A CD1 1 
ATOM 516  N N   . SER A 1 68  ? -2.494   44.663 -11.089 1.00 94.50  ?  68  SER A N   1 
ATOM 517  C CA  . SER A 1 68  ? -1.930   45.794 -11.823 1.00 98.98  ?  68  SER A CA  1 
ATOM 518  C C   . SER A 1 68  ? -3.031   46.670 -12.404 1.00 93.38  ?  68  SER A C   1 
ATOM 519  O O   . SER A 1 68  ? -3.046   47.889 -12.200 1.00 80.92  ?  68  SER A O   1 
ATOM 520  C CB  . SER A 1 68  ? -1.005   45.305 -12.938 1.00 96.77  ?  68  SER A CB  1 
ATOM 521  O OG  . SER A 1 68  ? 0.088    44.569 -12.434 1.00 111.88 ?  68  SER A OG  1 
ATOM 522  N N   . LYS A 1 69  ? -3.972   46.058 -13.130 1.00 84.62  ?  69  LYS A N   1 
ATOM 523  C CA  . LYS A 1 69  ? -5.005   46.851 -13.795 1.00 96.16  ?  69  LYS A CA  1 
ATOM 524  C C   . LYS A 1 69  ? -5.941   47.542 -12.811 1.00 91.10  ?  69  LYS A C   1 
ATOM 525  O O   . LYS A 1 69  ? -6.255   48.725 -13.028 1.00 77.03  ?  69  LYS A O   1 
ATOM 526  C CB  . LYS A 1 69  ? -5.775   45.982 -14.794 1.00 93.97  ?  69  LYS A CB  1 
ATOM 527  C CG  . LYS A 1 69  ? -6.849   46.745 -15.558 1.00 98.54  ?  69  LYS A CG  1 
ATOM 528  C CD  . LYS A 1 69  ? -7.815   45.802 -16.246 1.00 110.30 ?  69  LYS A CD  1 
ATOM 529  C CE  . LYS A 1 69  ? -8.573   46.521 -17.348 1.00 122.42 ?  69  LYS A CE  1 
ATOM 530  N NZ  . LYS A 1 69  ? -9.234   45.570 -18.284 1.00 138.14 ?  69  LYS A NZ  1 
ATOM 531  N N   . PRO A 1 70  ? -6.440   46.892 -11.748 1.00 79.20  ?  70  PRO A N   1 
ATOM 532  C CA  . PRO A 1 70  ? -7.299   47.629 -10.800 1.00 72.22  ?  70  PRO A CA  1 
ATOM 533  C C   . PRO A 1 70  ? -6.666   48.906 -10.271 1.00 79.78  ?  70  PRO A C   1 
ATOM 534  O O   . PRO A 1 70  ? -7.321   49.956 -10.249 1.00 90.59  ?  70  PRO A O   1 
ATOM 535  C CB  . PRO A 1 70  ? -7.547   46.604 -9.687  1.00 72.87  ?  70  PRO A CB  1 
ATOM 536  C CG  . PRO A 1 70  ? -7.420   45.290 -10.345 1.00 85.51  ?  70  PRO A CG  1 
ATOM 537  C CD  . PRO A 1 70  ? -6.422   45.445 -11.454 1.00 84.13  ?  70  PRO A CD  1 
ATOM 538  N N   . ILE A 1 71  ? -5.398   48.848 -9.854  1.00 81.63  ?  71  ILE A N   1 
ATOM 539  C CA  . ILE A 1 71  ? -4.719   50.042 -9.355  1.00 84.12  ?  71  ILE A CA  1 
ATOM 540  C C   . ILE A 1 71  ? -4.626   51.099 -10.450 1.00 81.36  ?  71  ILE A C   1 
ATOM 541  O O   . ILE A 1 71  ? -4.725   52.303 -10.183 1.00 81.78  ?  71  ILE A O   1 
ATOM 542  C CB  . ILE A 1 71  ? -3.331   49.672 -8.797  1.00 81.33  ?  71  ILE A CB  1 
ATOM 543  C CG1 . ILE A 1 71  ? -3.454   48.592 -7.722  1.00 85.07  ?  71  ILE A CG1 1 
ATOM 544  C CG2 . ILE A 1 71  ? -2.631   50.898 -8.230  1.00 74.40  ?  71  ILE A CG2 1 
ATOM 545  C CD1 . ILE A 1 71  ? -2.123   48.185 -7.111  1.00 87.38  ?  71  ILE A CD1 1 
ATOM 546  N N   . ARG A 1 72  ? -4.449   50.666 -11.701 1.00 82.71  ?  72  ARG A N   1 
ATOM 547  C CA  . ARG A 1 72  ? -4.390   51.613 -12.811 1.00 84.00  ?  72  ARG A CA  1 
ATOM 548  C C   . ARG A 1 72  ? -5.735   52.301 -13.014 1.00 86.77  ?  72  ARG A C   1 
ATOM 549  O O   . ARG A 1 72  ? -5.797   53.520 -13.208 1.00 83.07  ?  72  ARG A O   1 
ATOM 550  C CB  . ARG A 1 72  ? -3.948   50.901 -14.088 1.00 79.88  ?  72  ARG A CB  1 
ATOM 551  C CG  . ARG A 1 72  ? -2.494   50.462 -14.081 1.00 94.11  ?  72  ARG A CG  1 
ATOM 552  C CD  . ARG A 1 72  ? -1.958   50.302 -15.499 1.00 95.01  ?  72  ARG A CD  1 
ATOM 553  N NE  . ARG A 1 72  ? -2.453   49.079 -16.123 1.00 92.76  ?  72  ARG A NE  1 
ATOM 554  C CZ  . ARG A 1 72  ? -1.947   47.871 -15.900 1.00 92.46  ?  72  ARG A CZ  1 
ATOM 555  N NH1 . ARG A 1 72  ? -0.925   47.723 -15.067 1.00 100.63 ?  72  ARG A NH1 1 
ATOM 556  N NH2 . ARG A 1 72  ? -2.463   46.811 -16.508 1.00 90.16  ?  72  ARG A NH2 1 
ATOM 557  N N   . LEU A 1 73  ? -6.825   51.532 -12.974 1.00 80.44  ?  73  LEU A N   1 
ATOM 558  C CA  . LEU A 1 73  ? -8.149   52.136 -13.061 1.00 80.66  ?  73  LEU A CA  1 
ATOM 559  C C   . LEU A 1 73  ? -8.440   53.006 -11.846 1.00 80.68  ?  73  LEU A C   1 
ATOM 560  O O   . LEU A 1 73  ? -9.165   54.001 -11.955 1.00 88.60  ?  73  LEU A O   1 
ATOM 561  C CB  . LEU A 1 73  ? -9.215   51.050 -13.214 1.00 64.61  ?  73  LEU A CB  1 
ATOM 562  C CG  . LEU A 1 73  ? -8.976   50.021 -14.323 1.00 99.43  ?  73  LEU A CG  1 
ATOM 563  C CD1 . LEU A 1 73  ? -10.039  48.932 -14.285 1.00 95.03  ?  73  LEU A CD1 1 
ATOM 564  C CD2 . LEU A 1 73  ? -8.935   50.698 -15.685 1.00 89.75  ?  73  LEU A CD2 1 
ATOM 565  N N   . MET A 1 74  ? -7.885   52.649 -10.685 1.00 70.99  ?  74  MET A N   1 
ATOM 566  C CA  . MET A 1 74  ? -7.983   53.526 -9.524  1.00 79.00  ?  74  MET A CA  1 
ATOM 567  C C   . MET A 1 74  ? -7.258   54.840 -9.776  1.00 86.53  ?  74  MET A C   1 
ATOM 568  O O   . MET A 1 74  ? -7.756   55.914 -9.416  1.00 94.68  ?  74  MET A O   1 
ATOM 569  C CB  . MET A 1 74  ? -7.412   52.838 -8.284  1.00 83.17  ?  74  MET A CB  1 
ATOM 570  C CG  . MET A 1 74  ? -8.196   51.631 -7.797  1.00 95.90  ?  74  MET A CG  1 
ATOM 571  S SD  . MET A 1 74  ? -7.796   51.225 -6.085  1.00 115.93 ?  74  MET A SD  1 
ATOM 572  C CE  . MET A 1 74  ? -8.607   49.639 -5.901  1.00 82.62  ?  74  MET A CE  1 
ATOM 573  N N   . LEU A 1 75  ? -6.078   54.769 -10.396 1.00 86.61  ?  75  LEU A N   1 
ATOM 574  C CA  . LEU A 1 75  ? -5.287   55.970 -10.640 1.00 89.68  ?  75  LEU A CA  1 
ATOM 575  C C   . LEU A 1 75  ? -6.032   56.947 -11.540 1.00 102.34 ?  75  LEU A C   1 
ATOM 576  O O   . LEU A 1 75  ? -6.000   58.161 -11.308 1.00 102.85 ?  75  LEU A O   1 
ATOM 577  C CB  . LEU A 1 75  ? -3.939   55.587 -11.254 1.00 76.23  ?  75  LEU A CB  1 
ATOM 578  C CG  . LEU A 1 75  ? -2.837   56.648 -11.252 1.00 91.76  ?  75  LEU A CG  1 
ATOM 579  C CD1 . LEU A 1 75  ? -2.923   57.504 -9.999  1.00 92.49  ?  75  LEU A CD1 1 
ATOM 580  C CD2 . LEU A 1 75  ? -1.462   56.000 -11.370 1.00 87.61  ?  75  LEU A CD2 1 
ATOM 581  N N   . SER A 1 76  ? -6.716   56.435 -12.568 1.00 96.31  ?  76  SER A N   1 
ATOM 582  C CA  . SER A 1 76  ? -7.487   57.300 -13.455 1.00 94.79  ?  76  SER A CA  1 
ATOM 583  C C   . SER A 1 76  ? -8.559   58.068 -12.695 1.00 105.16 ?  76  SER A C   1 
ATOM 584  O O   . SER A 1 76  ? -8.860   59.217 -13.037 1.00 116.27 ?  76  SER A O   1 
ATOM 585  C CB  . SER A 1 76  ? -8.125   56.476 -14.573 1.00 95.47  ?  76  SER A CB  1 
ATOM 586  O OG  . SER A 1 76  ? -7.303   56.445 -15.726 1.00 104.34 ?  76  SER A OG  1 
ATOM 587  N N   . HIS A 1 77  ? -9.150   57.452 -11.669 1.00 86.55  ?  77  HIS A N   1 
ATOM 588  C CA  . HIS A 1 77  ? -10.143  58.155 -10.864 1.00 92.25  ?  77  HIS A CA  1 
ATOM 589  C C   . HIS A 1 77  ? -9.494   59.289 -10.080 1.00 106.68 ?  77  HIS A C   1 
ATOM 590  O O   . HIS A 1 77  ? -9.989   60.421 -10.082 1.00 112.73 ?  77  HIS A O   1 
ATOM 591  C CB  . HIS A 1 77  ? -10.846  57.173 -9.926  1.00 89.52  ?  77  HIS A CB  1 
ATOM 592  C CG  . HIS A 1 77  ? -12.077  57.726 -9.276  1.00 100.03 ?  77  HIS A CG  1 
ATOM 593  N ND1 . HIS A 1 77  ? -12.429  59.057 -9.348  1.00 111.46 ?  77  HIS A ND1 1 
ATOM 594  C CD2 . HIS A 1 77  ? -13.042  57.122 -8.542  1.00 118.15 ?  77  HIS A CD2 1 
ATOM 595  C CE1 . HIS A 1 77  ? -13.556  59.249 -8.685  1.00 120.09 ?  77  HIS A CE1 1 
ATOM 596  N NE2 . HIS A 1 77  ? -13.949  58.091 -8.187  1.00 132.44 ?  77  HIS A NE2 1 
ATOM 597  N N   . PHE A 1 78  ? -8.378   59.001 -9.403  1.00 98.25  ?  78  PHE A N   1 
ATOM 598  C CA  . PHE A 1 78  ? -7.635   60.050 -8.714  1.00 97.96  ?  78  PHE A CA  1 
ATOM 599  C C   . PHE A 1 78  ? -7.010   61.028 -9.699  1.00 106.97 ?  78  PHE A C   1 
ATOM 600  O O   . PHE A 1 78  ? -6.870   62.217 -9.388  1.00 109.78 ?  78  PHE A O   1 
ATOM 601  C CB  . PHE A 1 78  ? -6.565   59.426 -7.815  1.00 99.52  ?  78  PHE A CB  1 
ATOM 602  C CG  . PHE A 1 78  ? -5.703   60.431 -7.101  1.00 113.38 ?  78  PHE A CG  1 
ATOM 603  C CD1 . PHE A 1 78  ? -4.504   60.854 -7.653  1.00 109.40 ?  78  PHE A CD1 1 
ATOM 604  C CD2 . PHE A 1 78  ? -6.090   60.952 -5.877  1.00 124.29 ?  78  PHE A CD2 1 
ATOM 605  C CE1 . PHE A 1 78  ? -3.709   61.778 -7.000  1.00 108.10 ?  78  PHE A CE1 1 
ATOM 606  C CE2 . PHE A 1 78  ? -5.299   61.876 -5.219  1.00 134.38 ?  78  PHE A CE2 1 
ATOM 607  C CZ  . PHE A 1 78  ? -4.107   62.289 -5.781  1.00 119.71 ?  78  PHE A CZ  1 
ATOM 608  N N   . LYS A 1 79  ? -6.621   60.545 -10.882 1.00 107.85 ?  79  LYS A N   1 
ATOM 609  C CA  . LYS A 1 79  ? -6.085   61.428 -11.913 1.00 109.20 ?  79  LYS A CA  1 
ATOM 610  C C   . LYS A 1 79  ? -7.082   62.520 -12.282 1.00 117.30 ?  79  LYS A C   1 
ATOM 611  O O   . LYS A 1 79  ? -6.712   63.693 -12.411 1.00 124.00 ?  79  LYS A O   1 
ATOM 612  C CB  . LYS A 1 79  ? -5.701   60.606 -13.143 1.00 101.05 ?  79  LYS A CB  1 
ATOM 613  C CG  . LYS A 1 79  ? -5.740   61.352 -14.460 1.00 116.77 ?  79  LYS A CG  1 
ATOM 614  C CD  . LYS A 1 79  ? -5.486   60.394 -15.614 1.00 109.87 ?  79  LYS A CD  1 
ATOM 615  C CE  . LYS A 1 79  ? -5.633   61.090 -16.955 1.00 124.99 ?  79  LYS A CE  1 
ATOM 616  N NZ  . LYS A 1 79  ? -5.491   60.132 -18.085 1.00 126.93 ?  79  LYS A NZ  1 
ATOM 617  N N   . ASP A 1 80  ? -8.352   62.155 -12.448 1.00 111.30 ?  80  ASP A N   1 
ATOM 618  C CA  . ASP A 1 80  ? -9.383   63.117 -12.811 1.00 116.50 ?  80  ASP A CA  1 
ATOM 619  C C   . ASP A 1 80  ? -10.028  63.790 -11.608 1.00 120.12 ?  80  ASP A C   1 
ATOM 620  O O   . ASP A 1 80  ? -10.619  64.864 -11.763 1.00 132.80 ?  80  ASP A O   1 
ATOM 621  C CB  . ASP A 1 80  ? -10.472  62.432 -13.643 1.00 110.21 ?  80  ASP A CB  1 
ATOM 622  C CG  . ASP A 1 80  ? -9.943   61.872 -14.950 1.00 125.36 ?  80  ASP A CG  1 
ATOM 623  O OD1 . ASP A 1 80  ? -9.209   62.597 -15.654 1.00 128.75 ?  80  ASP A OD1 1 
ATOM 624  O OD2 . ASP A 1 80  ? -10.257  60.707 -15.272 1.00 133.42 -1 80  ASP A OD2 1 
ATOM 625  N N   . ASN A 1 81  ? -9.931   63.194 -10.423 1.00 111.70 ?  81  ASN A N   1 
ATOM 626  C CA  . ASN A 1 81  ? -10.625  63.670 -9.229  1.00 117.86 ?  81  ASN A CA  1 
ATOM 627  C C   . ASN A 1 81  ? -9.686   63.689 -8.028  1.00 125.28 ?  81  ASN A C   1 
ATOM 628  O O   . ASN A 1 81  ? -10.003  63.186 -6.948  1.00 117.88 ?  81  ASN A O   1 
ATOM 629  C CB  . ASN A 1 81  ? -11.853  62.810 -8.946  1.00 116.84 ?  81  ASN A CB  1 
ATOM 630  C CG  . ASN A 1 81  ? -12.894  62.901 -10.046 1.00 128.84 ?  81  ASN A CG  1 
ATOM 631  O OD1 . ASN A 1 81  ? -13.757  63.779 -10.027 1.00 146.48 ?  81  ASN A OD1 1 
ATOM 632  N ND2 . ASN A 1 81  ? -12.813  61.998 -11.017 1.00 119.96 ?  81  ASN A ND2 1 
ATOM 633  N N   . LYS A 1 82  ? -8.499   64.271 -8.213  1.00 132.19 ?  82  LYS A N   1 
ATOM 634  C CA  . LYS A 1 82  ? -7.549   64.397 -7.111  1.00 132.76 ?  82  LYS A CA  1 
ATOM 635  C C   . LYS A 1 82  ? -8.108   65.244 -5.973  1.00 136.89 ?  82  LYS A C   1 
ATOM 636  O O   . LYS A 1 82  ? -7.810   64.984 -4.801  1.00 133.12 ?  82  LYS A O   1 
ATOM 637  C CB  . LYS A 1 82  ? -6.237   64.996 -7.626  1.00 120.69 ?  82  LYS A CB  1 
ATOM 638  C CG  . LYS A 1 82  ? -5.303   65.513 -6.541  1.00 125.60 ?  82  LYS A CG  1 
ATOM 639  C CD  . LYS A 1 82  ? -4.126   66.273 -7.131  1.00 151.44 ?  82  LYS A CD  1 
ATOM 640  C CE  . LYS A 1 82  ? -3.255   66.873 -6.038  1.00 128.33 ?  82  LYS A CE  1 
ATOM 641  N NZ  . LYS A 1 82  ? -2.114   67.652 -6.596  1.00 122.83 ?  82  LYS A NZ  1 
ATOM 642  N N   . GLU A 1 83  ? -8.933   66.236 -6.291  1.00 143.23 ?  83  GLU A N   1 
ATOM 643  C CA  . GLU A 1 83  ? -9.386   67.229 -5.315  1.00 139.03 ?  83  GLU A CA  1 
ATOM 644  C C   . GLU A 1 83  ? -10.617  66.763 -4.541  1.00 137.05 ?  83  GLU A C   1 
ATOM 645  O O   . GLU A 1 83  ? -11.639  67.447 -4.498  1.00 140.10 ?  83  GLU A O   1 
ATOM 646  C CB  . GLU A 1 83  ? -9.659   68.548 -6.027  1.00 134.30 ?  83  GLU A CB  1 
ATOM 647  C CG  . GLU A 1 83  ? -8.509   69.026 -6.899  1.00 133.00 ?  83  GLU A CG  1 
ATOM 648  C CD  . GLU A 1 83  ? -8.922   70.127 -7.855  1.00 133.78 ?  83  GLU A CD  1 
ATOM 649  O OE1 . GLU A 1 83  ? -8.162   70.404 -8.807  1.00 138.83 ?  83  GLU A OE1 1 
ATOM 650  O OE2 . GLU A 1 83  ? -10.008  70.712 -7.659  1.00 135.65 -1 83  GLU A OE2 1 
ATOM 651  N N   . LYS A 1 84  ? -10.531  65.587 -3.915  1.00 128.65 ?  84  LYS A N   1 
ATOM 652  C CA  . LYS A 1 84  ? -11.609  65.085 -3.068  1.00 125.26 ?  84  LYS A CA  1 
ATOM 653  C C   . LYS A 1 84  ? -11.155  64.555 -1.716  1.00 130.09 ?  84  LYS A C   1 
ATOM 654  O O   . LYS A 1 84  ? -11.970  64.534 -0.786  1.00 134.21 ?  84  LYS A O   1 
ATOM 655  C CB  . LYS A 1 84  ? -12.393  63.974 -3.786  1.00 102.91 ?  84  LYS A CB  1 
ATOM 656  C CG  . LYS A 1 84  ? -13.490  64.477 -4.712  1.00 109.30 ?  84  LYS A CG  1 
ATOM 657  C CD  . LYS A 1 84  ? -12.955  64.830 -6.088  1.00 119.72 ?  84  LYS A CD  1 
ATOM 658  C CE  . LYS A 1 84  ? -14.075  65.279 -7.011  1.00 118.13 ?  84  LYS A CE  1 
ATOM 659  N NZ  . LYS A 1 84  ? -13.570  65.630 -8.365  1.00 109.67 ?  84  LYS A NZ  1 
ATOM 660  N N   . GLY A 1 85  ? -9.901   64.133 -1.567  1.00 123.60 ?  85  GLY A N   1 
ATOM 661  C CA  . GLY A 1 85  ? -9.419   63.625 -0.301  1.00 125.21 ?  85  GLY A CA  1 
ATOM 662  C C   . GLY A 1 85  ? -9.899   62.240 0.073   1.00 119.97 ?  85  GLY A C   1 
ATOM 663  O O   . GLY A 1 85  ? -9.570   61.768 1.168   1.00 125.64 ?  85  GLY A O   1 
ATOM 664  N N   . ALA A 1 86  ? -10.662  61.573 -0.790  1.00 114.09 ?  86  ALA A N   1 
ATOM 665  C CA  . ALA A 1 86  ? -11.128  60.228 -0.497  1.00 100.13 ?  86  ALA A CA  1 
ATOM 666  C C   . ALA A 1 86  ? -9.960   59.242 -0.526  1.00 96.55  ?  86  ALA A C   1 
ATOM 667  O O   . ALA A 1 86  ? -8.854   59.552 -0.980  1.00 111.69 ?  86  ALA A O   1 
ATOM 668  C CB  . ALA A 1 86  ? -12.209  59.806 -1.491  1.00 97.50  ?  86  ALA A CB  1 
ATOM 669  N N   . ASN A 1 87  ? -10.221  58.034 -0.037  1.00 94.85  ?  87  ASN A N   1 
ATOM 670  C CA  . ASN A 1 87  ? -9.205   56.998 0.079   1.00 85.29  ?  87  ASN A CA  1 
ATOM 671  C C   . ASN A 1 87  ? -9.587   55.795 -0.769  1.00 77.96  ?  87  ASN A C   1 
ATOM 672  O O   . ASN A 1 87  ? -10.769  55.459 -0.894  1.00 101.02 ?  87  ASN A O   1 
ATOM 673  C CB  . ASN A 1 87  ? -9.021   56.573 1.539   1.00 98.97  ?  87  ASN A CB  1 
ATOM 674  C CG  . ASN A 1 87  ? -8.546   57.711 2.420   1.00 100.67 ?  87  ASN A CG  1 
ATOM 675  O OD1 . ASN A 1 87  ? -9.335   58.562 2.833   1.00 110.54 ?  87  ASN A OD1 1 
ATOM 676  N ND2 . ASN A 1 87  ? -7.252   57.732 2.713   1.00 99.54  ?  87  ASN A ND2 1 
ATOM 677  N N   . TYR A 1 88  ? -8.580   55.154 -1.353  1.00 82.08  ?  88  TYR A N   1 
ATOM 678  C CA  . TYR A 1 88  ? -8.766   53.950 -2.149  1.00 92.24  ?  88  TYR A CA  1 
ATOM 679  C C   . TYR A 1 88  ? -8.329   52.734 -1.346  1.00 79.69  ?  88  TYR A C   1 
ATOM 680  O O   . TYR A 1 88  ? -7.299   52.761 -0.667  1.00 89.10  ?  88  TYR A O   1 
ATOM 681  C CB  . TYR A 1 88  ? -7.977   54.033 -3.457  1.00 94.51  ?  88  TYR A CB  1 
ATOM 682  C CG  . TYR A 1 88  ? -8.394   55.189 -4.333  1.00 95.35  ?  88  TYR A CG  1 
ATOM 683  C CD1 . TYR A 1 88  ? -9.428   55.051 -5.248  1.00 77.07  ?  88  TYR A CD1 1 
ATOM 684  C CD2 . TYR A 1 88  ? -7.763   56.422 -4.237  1.00 94.38  ?  88  TYR A CD2 1 
ATOM 685  C CE1 . TYR A 1 88  ? -9.817   56.106 -6.049  1.00 95.68  ?  88  TYR A CE1 1 
ATOM 686  C CE2 . TYR A 1 88  ? -8.146   57.484 -5.033  1.00 94.78  ?  88  TYR A CE2 1 
ATOM 687  C CZ  . TYR A 1 88  ? -9.174   57.319 -5.938  1.00 103.63 ?  88  TYR A CZ  1 
ATOM 688  O OH  . TYR A 1 88  ? -9.561   58.371 -6.734  1.00 109.22 ?  88  TYR A OH  1 
ATOM 689  N N   . TYR A 1 89  ? -9.117   51.666 -1.430  1.00 82.90  ?  89  TYR A N   1 
ATOM 690  C CA  . TYR A 1 89  ? -8.917   50.479 -0.612  1.00 93.52  ?  89  TYR A CA  1 
ATOM 691  C C   . TYR A 1 89  ? -8.740   49.256 -1.498  1.00 96.91  ?  89  TYR A C   1 
ATOM 692  O O   . TYR A 1 89  ? -9.445   49.094 -2.500  1.00 91.36  ?  89  TYR A O   1 
ATOM 693  C CB  . TYR A 1 89  ? -10.096  50.265 0.344   1.00 87.44  ?  89  TYR A CB  1 
ATOM 694  C CG  . TYR A 1 89  ? -10.399  51.464 1.215   1.00 84.02  ?  89  TYR A CG  1 
ATOM 695  C CD1 . TYR A 1 89  ? -9.879   51.564 2.497   1.00 88.68  ?  89  TYR A CD1 1 
ATOM 696  C CD2 . TYR A 1 89  ? -11.209  52.494 0.754   1.00 90.65  ?  89  TYR A CD2 1 
ATOM 697  C CE1 . TYR A 1 89  ? -10.152  52.658 3.295   1.00 101.36 ?  89  TYR A CE1 1 
ATOM 698  C CE2 . TYR A 1 89  ? -11.489  53.591 1.544   1.00 93.16  ?  89  TYR A CE2 1 
ATOM 699  C CZ  . TYR A 1 89  ? -10.958  53.668 2.812   1.00 104.58 ?  89  TYR A CZ  1 
ATOM 700  O OH  . TYR A 1 89  ? -11.235  54.760 3.601   1.00 91.18  ?  89  TYR A OH  1 
ATOM 701  N N   . LEU A 1 90  ? -7.799   48.394 -1.117  1.00 94.08  ?  90  LEU A N   1 
ATOM 702  C CA  . LEU A 1 90  ? -7.537   47.150 -1.827  1.00 81.20  ?  90  LEU A CA  1 
ATOM 703  C C   . LEU A 1 90  ? -7.161   46.087 -0.809  1.00 82.14  ?  90  LEU A C   1 
ATOM 704  O O   . LEU A 1 90  ? -6.318   46.328 0.059   1.00 86.51  ?  90  LEU A O   1 
ATOM 705  C CB  . LEU A 1 90  ? -6.417   47.324 -2.861  1.00 83.81  ?  90  LEU A CB  1 
ATOM 706  C CG  . LEU A 1 90  ? -6.478   46.471 -4.132  1.00 99.94  ?  90  LEU A CG  1 
ATOM 707  C CD1 . LEU A 1 90  ? -5.541   47.033 -5.188  1.00 90.10  ?  90  LEU A CD1 1 
ATOM 708  C CD2 . LEU A 1 90  ? -6.141   45.015 -3.849  1.00 93.91  ?  90  LEU A CD2 1 
ATOM 709  N N   . TYR A 1 91  ? -7.789   44.918 -0.912  1.00 85.48  ?  91  TYR A N   1 
ATOM 710  C CA  . TYR A 1 91  ? -7.537   43.813 -0.000  1.00 93.49  ?  91  TYR A CA  1 
ATOM 711  C C   . TYR A 1 91  ? -7.300   42.542 -0.806  1.00 86.61  ?  91  TYR A C   1 
ATOM 712  O O   . TYR A 1 91  ? -7.499   42.506 -2.025  1.00 91.87  ?  91  TYR A O   1 
ATOM 713  C CB  . TYR A 1 91  ? -8.701   43.624 0.982   1.00 84.28  ?  91  TYR A CB  1 
ATOM 714  C CG  . TYR A 1 91  ? -9.137   44.899 1.667   1.00 85.99  ?  91  TYR A CG  1 
ATOM 715  C CD1 . TYR A 1 91  ? -8.544   45.312 2.852   1.00 86.11  ?  91  TYR A CD1 1 
ATOM 716  C CD2 . TYR A 1 91  ? -10.145  45.689 1.129   1.00 83.19  ?  91  TYR A CD2 1 
ATOM 717  C CE1 . TYR A 1 91  ? -8.940   46.478 3.481   1.00 94.10  ?  91  TYR A CE1 1 
ATOM 718  C CE2 . TYR A 1 91  ? -10.548  46.856 1.750   1.00 93.38  ?  91  TYR A CE2 1 
ATOM 719  C CZ  . TYR A 1 91  ? -9.942   47.246 2.926   1.00 98.22  ?  91  TYR A CZ  1 
ATOM 720  O OH  . TYR A 1 91  ? -10.340  48.406 3.548   1.00 88.49  ?  91  TYR A OH  1 
ATOM 721  N N   . GLY A 1 92  ? -6.871   41.490 -0.117  1.00 84.21  ?  92  GLY A N   1 
ATOM 722  C CA  . GLY A 1 92  ? -6.574   40.241 -0.791  1.00 81.45  ?  92  GLY A CA  1 
ATOM 723  C C   . GLY A 1 92  ? -6.254   39.142 0.195   1.00 84.38  ?  92  GLY A C   1 
ATOM 724  O O   . GLY A 1 92  ? -5.882   39.398 1.346   1.00 83.19  ?  92  GLY A O   1 
ATOM 725  N N   . HIS A 1 93  ? -6.405   37.906 -0.278  1.00 88.20  ?  93  HIS A N   1 
ATOM 726  C CA  . HIS A 1 93  ? -6.116   36.721 0.527   1.00 104.76 ?  93  HIS A CA  1 
ATOM 727  C C   . HIS A 1 93  ? -5.685   35.611 -0.421  1.00 106.95 ?  93  HIS A C   1 
ATOM 728  O O   . HIS A 1 93  ? -6.509   35.079 -1.171  1.00 107.37 ?  93  HIS A O   1 
ATOM 729  C CB  . HIS A 1 93  ? -7.330   36.302 1.351   1.00 107.77 ?  93  HIS A CB  1 
ATOM 730  C CG  . HIS A 1 93  ? -7.156   35.000 2.070   1.00 104.25 ?  93  HIS A CG  1 
ATOM 731  N ND1 . HIS A 1 93  ? -6.807   34.927 3.401   1.00 110.87 ?  93  HIS A ND1 1 
ATOM 732  C CD2 . HIS A 1 93  ? -7.291   33.720 1.647   1.00 108.28 ?  93  HIS A CD2 1 
ATOM 733  C CE1 . HIS A 1 93  ? -6.729   33.660 3.767   1.00 116.60 ?  93  HIS A CE1 1 
ATOM 734  N NE2 . HIS A 1 93  ? -7.018   32.907 2.721   1.00 111.82 ?  93  HIS A NE2 1 
ATOM 735  N N   . TYR A 1 94  ? -4.402   35.261 -0.383  1.00 103.20 ?  94  TYR A N   1 
ATOM 736  C CA  . TYR A 1 94  ? -3.840   34.257 -1.272  1.00 107.20 ?  94  TYR A CA  1 
ATOM 737  C C   . TYR A 1 94  ? -3.146   33.182 -0.445  1.00 108.55 ?  94  TYR A C   1 
ATOM 738  O O   . TYR A 1 94  ? -2.839   33.379 0.734   1.00 107.41 ?  94  TYR A O   1 
ATOM 739  C CB  . TYR A 1 94  ? -2.847   34.876 -2.270  1.00 101.01 ?  94  TYR A CB  1 
ATOM 740  C CG  . TYR A 1 94  ? -3.315   36.178 -2.890  1.00 99.12  ?  94  TYR A CG  1 
ATOM 741  C CD1 . TYR A 1 94  ? -3.915   36.198 -4.143  1.00 110.03 ?  94  TYR A CD1 1 
ATOM 742  C CD2 . TYR A 1 94  ? -3.136   37.389 -2.231  1.00 93.28  ?  94  TYR A CD2 1 
ATOM 743  C CE1 . TYR A 1 94  ? -4.340   37.385 -4.713  1.00 110.74 ?  94  TYR A CE1 1 
ATOM 744  C CE2 . TYR A 1 94  ? -3.557   38.579 -2.793  1.00 89.49  ?  94  TYR A CE2 1 
ATOM 745  C CZ  . TYR A 1 94  ? -4.157   38.572 -4.033  1.00 94.62  ?  94  TYR A CZ  1 
ATOM 746  O OH  . TYR A 1 94  ? -4.575   39.756 -4.595  1.00 103.52 ?  94  TYR A OH  1 
ATOM 747  N N   . LYS A 1 95  ? -2.908   32.032 -1.078  1.00 116.18 ?  95  LYS A N   1 
ATOM 748  C CA  . LYS A 1 95  ? -2.152   30.965 -0.428  1.00 125.02 ?  95  LYS A CA  1 
ATOM 749  C C   . LYS A 1 95  ? -0.737   31.424 -0.105  1.00 123.83 ?  95  LYS A C   1 
ATOM 750  O O   . LYS A 1 95  ? -0.320   31.435 1.059   1.00 123.21 ?  95  LYS A O   1 
ATOM 751  C CB  . LYS A 1 95  ? -2.123   29.724 -1.320  1.00 134.39 ?  95  LYS A CB  1 
ATOM 752  C CG  . LYS A 1 95  ? -1.218   28.610 -0.826  1.00 144.16 ?  95  LYS A CG  1 
ATOM 753  C CD  . LYS A 1 95  ? -0.867   27.656 -1.959  1.00 170.21 ?  95  LYS A CD  1 
ATOM 754  C CE  . LYS A 1 95  ? 0.159    26.626 -1.515  1.00 192.18 ?  95  LYS A CE  1 
ATOM 755  N NZ  . LYS A 1 95  ? 0.666    25.816 -2.657  1.00 187.26 ?  95  LYS A NZ  1 
ATOM 756  N N   . SER A 1 96  ? 0.018    31.806 -1.131  1.00 116.02 ?  96  SER A N   1 
ATOM 757  C CA  . SER A 1 96  ? 1.374    32.306 -0.961  1.00 121.05 ?  96  SER A CA  1 
ATOM 758  C C   . SER A 1 96  ? 1.534    33.530 -1.855  1.00 116.24 ?  96  SER A C   1 
ATOM 759  O O   . SER A 1 96  ? 0.558    34.072 -2.382  1.00 107.36 ?  96  SER A O   1 
ATOM 760  C CB  . SER A 1 96  ? 2.407    31.215 -1.274  1.00 119.13 ?  96  SER A CB  1 
ATOM 761  O OG  . SER A 1 96  ? 2.193    30.659 -2.558  1.00 122.98 ?  96  SER A OG  1 
ATOM 762  N N   . GLY A 1 97  ? 2.777    33.976 -2.021  1.00 111.72 ?  97  GLY A N   1 
ATOM 763  C CA  . GLY A 1 97  ? 3.073    35.109 -2.866  1.00 108.58 ?  97  GLY A CA  1 
ATOM 764  C C   . GLY A 1 97  ? 2.942    36.461 -2.200  1.00 104.74 ?  97  GLY A C   1 
ATOM 765  O O   . GLY A 1 97  ? 3.266    37.476 -2.830  1.00 105.08 ?  97  GLY A O   1 
ATOM 766  N N   . GLN A 1 98  ? 2.474    36.514 -0.949  1.00 89.33  ?  98  GLN A N   1 
ATOM 767  C CA  . GLN A 1 98  ? 2.359    37.795 -0.259  1.00 97.94  ?  98  GLN A CA  1 
ATOM 768  C C   . GLN A 1 98  ? 3.721    38.435 -0.034  1.00 102.58 ?  98  GLN A C   1 
ATOM 769  O O   . GLN A 1 98  ? 3.820    39.661 0.093   1.00 100.29 ?  98  GLN A O   1 
ATOM 770  C CB  . GLN A 1 98  ? 1.637    37.623 1.079   1.00 103.36 ?  98  GLN A CB  1 
ATOM 771  C CG  . GLN A 1 98  ? 0.231    37.052 0.982   1.00 105.47 ?  98  GLN A CG  1 
ATOM 772  C CD  . GLN A 1 98  ? 0.215    35.538 0.970   1.00 99.64  ?  98  GLN A CD  1 
ATOM 773  O OE1 . GLN A 1 98  ? 1.263    34.898 0.902   1.00 90.87  ?  98  GLN A OE1 1 
ATOM 774  N NE2 . GLN A 1 98  ? -0.976   34.957 1.044   1.00 91.87  ?  98  GLN A NE2 1 
ATOM 775  N N   . GLU A 1 99  ? 4.779    37.623 0.022   1.00 99.52  ?  99  GLU A N   1 
ATOM 776  C CA  . GLU A 1 99  ? 6.120    38.139 0.267   1.00 101.24 ?  99  GLU A CA  1 
ATOM 777  C C   . GLU A 1 99  ? 6.635    38.999 -0.880  1.00 97.56  ?  99  GLU A C   1 
ATOM 778  O O   . GLU A 1 99  ? 7.605    39.740 -0.691  1.00 88.55  ?  99  GLU A O   1 
ATOM 779  C CB  . GLU A 1 99  ? 7.089    36.981 0.520   1.00 95.25  ?  99  GLU A CB  1 
ATOM 780  C CG  . GLU A 1 99  ? 7.164    35.963 -0.613  1.00 98.23  ?  99  GLU A CG  1 
ATOM 781  C CD  . GLU A 1 99  ? 6.049    34.934 -0.560  1.00 110.50 ?  99  GLU A CD  1 
ATOM 782  O OE1 . GLU A 1 99  ? 6.349    33.724 -0.648  1.00 106.23 ?  99  GLU A OE1 1 
ATOM 783  O OE2 . GLU A 1 99  ? 4.874    35.333 -0.425  1.00 120.51 -1 99  GLU A OE2 1 
ATOM 784  N N   . LYS A 1 100 ? 6.013    38.923 -2.058  1.00 95.57  ?  100 LYS A N   1 
ATOM 785  C CA  . LYS A 1 100 ? 6.498    39.674 -3.209  1.00 82.30  ?  100 LYS A CA  1 
ATOM 786  C C   . LYS A 1 100 ? 6.149    41.156 -3.146  1.00 88.17  ?  100 LYS A C   1 
ATOM 787  O O   . LYS A 1 100 ? 6.833    41.963 -3.785  1.00 100.19 ?  100 LYS A O   1 
ATOM 788  C CB  . LYS A 1 100 ? 5.948    39.070 -4.503  1.00 84.64  ?  100 LYS A CB  1 
ATOM 789  C CG  . LYS A 1 100 ? 6.452    37.669 -4.798  1.00 105.75 ?  100 LYS A CG  1 
ATOM 790  C CD  . LYS A 1 100 ? 5.933    37.168 -6.134  1.00 103.53 ?  100 LYS A CD  1 
ATOM 791  C CE  . LYS A 1 100 ? 6.390    35.744 -6.403  1.00 105.32 ?  100 LYS A CE  1 
ATOM 792  N NZ  . LYS A 1 100 ? 5.873    35.232 -7.701  1.00 101.72 ?  100 LYS A NZ  1 
ATOM 793  N N   . LEU A 1 101 ? 5.116    41.532 -2.396  1.00 86.65  ?  101 LEU A N   1 
ATOM 794  C CA  . LEU A 1 101 ? 4.720    42.934 -2.276  1.00 89.28  ?  101 LEU A CA  1 
ATOM 795  C C   . LEU A 1 101 ? 5.602    43.595 -1.224  1.00 95.33  ?  101 LEU A C   1 
ATOM 796  O O   . LEU A 1 101 ? 5.328    43.515 -0.024  1.00 101.34 ?  101 LEU A O   1 
ATOM 797  C CB  . LEU A 1 101 ? 3.244    43.047 -1.915  1.00 96.10  ?  101 LEU A CB  1 
ATOM 798  C CG  . LEU A 1 101 ? 2.699    44.459 -1.694  1.00 91.86  ?  101 LEU A CG  1 
ATOM 799  C CD1 . LEU A 1 101 ? 3.046    45.366 -2.869  1.00 86.52  ?  101 LEU A CD1 1 
ATOM 800  C CD2 . LEU A 1 101 ? 1.194    44.423 -1.461  1.00 96.26  ?  101 LEU A CD2 1 
ATOM 801  N N   . THR A 1 102 ? 6.673    44.245 -1.674  1.00 99.98  ?  102 THR A N   1 
ATOM 802  C CA  . THR A 1 102 ? 7.591    44.927 -0.767  1.00 107.62 ?  102 THR A CA  1 
ATOM 803  C C   . THR A 1 102 ? 6.901    46.148 -0.172  1.00 97.67  ?  102 THR A C   1 
ATOM 804  O O   . THR A 1 102 ? 6.702    47.155 -0.858  1.00 87.51  ?  102 THR A O   1 
ATOM 805  C CB  . THR A 1 102 ? 8.866    45.324 -1.506  1.00 111.31 ?  102 THR A CB  1 
ATOM 806  O OG1 . THR A 1 102 ? 9.486    44.152 -2.052  1.00 108.03 ?  102 THR A OG1 1 
ATOM 807  C CG2 . THR A 1 102 ? 9.837    46.012 -0.557  1.00 110.78 ?  102 THR A CG2 1 
ATOM 808  N N   . LEU A 1 103 ? 6.528    46.057 1.108   1.00 92.23  ?  103 LEU A N   1 
ATOM 809  C CA  . LEU A 1 103 ? 5.853    47.144 1.795   1.00 97.63  ?  103 LEU A CA  1 
ATOM 810  C C   . LEU A 1 103 ? 6.821    47.886 2.713   1.00 98.24  ?  103 LEU A C   1 
ATOM 811  O O   . LEU A 1 103 ? 7.726    47.277 3.292   1.00 99.16  ?  103 LEU A O   1 
ATOM 812  C CB  . LEU A 1 103 ? 4.673    46.613 2.615   1.00 110.87 ?  103 LEU A CB  1 
ATOM 813  C CG  . LEU A 1 103 ? 3.381    46.395 1.825   1.00 112.51 ?  103 LEU A CG  1 
ATOM 814  C CD1 . LEU A 1 103 ? 2.529    45.315 2.472   1.00 101.19 ?  103 LEU A CD1 1 
ATOM 815  C CD2 . LEU A 1 103 ? 2.603    47.697 1.701   1.00 115.45 ?  103 LEU A CD2 1 
ATOM 816  N N   . PRO A 1 104 ? 6.664    49.212 2.874   1.00 104.98 ?  104 PRO A N   1 
ATOM 817  C CA  . PRO A 1 104 ? 5.607    50.043 2.284   1.00 103.84 ?  104 PRO A CA  1 
ATOM 818  C C   . PRO A 1 104 ? 5.813    50.314 0.797   1.00 107.77 ?  104 PRO A C   1 
ATOM 819  O O   . PRO A 1 104 ? 6.862    49.981 0.246   1.00 113.73 ?  104 PRO A O   1 
ATOM 820  C CB  . PRO A 1 104 ? 5.705    51.340 3.087   1.00 95.87  ?  104 PRO A CB  1 
ATOM 821  C CG  . PRO A 1 104 ? 7.147    51.433 3.435   1.00 95.84  ?  104 PRO A CG  1 
ATOM 822  C CD  . PRO A 1 104 ? 7.595    50.015 3.688   1.00 118.09 ?  104 PRO A CD  1 
ATOM 823  N N   . LEU A 1 105 ? 4.811    50.914 0.160   1.00 101.27 ?  105 LEU A N   1 
ATOM 824  C CA  . LEU A 1 105 ? 4.875    51.183 -1.269  1.00 78.66  ?  105 LEU A CA  1 
ATOM 825  C C   . LEU A 1 105 ? 5.793    52.366 -1.542  1.00 86.05  ?  105 LEU A C   1 
ATOM 826  O O   . LEU A 1 105 ? 5.647    53.433 -0.938  1.00 94.84  ?  105 LEU A O   1 
ATOM 827  C CB  . LEU A 1 105 ? 3.479    51.456 -1.822  1.00 93.39  ?  105 LEU A CB  1 
ATOM 828  C CG  . LEU A 1 105 ? 2.624    50.215 -2.079  1.00 107.63 ?  105 LEU A CG  1 
ATOM 829  C CD1 . LEU A 1 105 ? 1.242    50.611 -2.566  1.00 106.48 ?  105 LEU A CD1 1 
ATOM 830  C CD2 . LEU A 1 105 ? 3.307    49.297 -3.079  1.00 78.37  ?  105 LEU A CD2 1 
ATOM 831  N N   . LYS A 1 106 ? 6.741    52.171 -2.453  1.00 91.73  ?  106 LYS A N   1 
ATOM 832  C CA  . LYS A 1 106 ? 7.652    53.217 -2.886  1.00 89.66  ?  106 LYS A CA  1 
ATOM 833  C C   . LYS A 1 106 ? 7.471    53.449 -4.381  1.00 97.24  ?  106 LYS A C   1 
ATOM 834  O O   . LYS A 1 106 ? 7.090    52.538 -5.123  1.00 85.38  ?  106 LYS A O   1 
ATOM 835  C CB  . LYS A 1 106 ? 9.107    52.853 -2.564  1.00 93.15  ?  106 LYS A CB  1 
ATOM 836  C CG  . LYS A 1 106 ? 9.353    52.610 -1.081  1.00 90.12  ?  106 LYS A CG  1 
ATOM 837  C CD  . LYS A 1 106 ? 10.779   52.162 -0.803  1.00 108.04 ?  106 LYS A CD  1 
ATOM 838  C CE  . LYS A 1 106 ? 11.010   51.975 0.690   1.00 94.99  ?  106 LYS A CE  1 
ATOM 839  N NZ  . LYS A 1 106 ? 12.403   51.550 1.002   1.00 104.06 ?  106 LYS A NZ  1 
ATOM 840  N N   . VAL A 1 107 ? 7.741    54.682 -4.814  1.00 99.65  ?  107 VAL A N   1 
ATOM 841  C CA  . VAL A 1 107 ? 7.418    55.082 -6.183  1.00 83.20  ?  107 VAL A CA  1 
ATOM 842  C C   . VAL A 1 107 ? 8.226    54.268 -7.187  1.00 92.46  ?  107 VAL A C   1 
ATOM 843  O O   . VAL A 1 107 ? 7.673    53.694 -8.132  1.00 98.02  ?  107 VAL A O   1 
ATOM 844  C CB  . VAL A 1 107 ? 7.644    56.592 -6.369  1.00 76.25  ?  107 VAL A CB  1 
ATOM 845  C CG1 . VAL A 1 107 ? 7.141    57.035 -7.735  1.00 96.02  ?  107 VAL A CG1 1 
ATOM 846  C CG2 . VAL A 1 107 ? 6.953    57.369 -5.263  1.00 79.57  ?  107 VAL A CG2 1 
ATOM 847  N N   . ASP A 1 108 ? 9.548    54.208 -6.999  1.00 94.69  ?  108 ASP A N   1 
ATOM 848  C CA  . ASP A 1 108 ? 10.398   53.486 -7.941  1.00 110.10 ?  108 ASP A CA  1 
ATOM 849  C C   . ASP A 1 108 ? 10.070   52.000 -7.996  1.00 114.80 ?  108 ASP A C   1 
ATOM 850  O O   . ASP A 1 108 ? 10.408   51.338 -8.984  1.00 124.36 ?  108 ASP A O   1 
ATOM 851  C CB  . ASP A 1 108 ? 11.870   53.691 -7.584  1.00 113.11 ?  108 ASP A CB  1 
ATOM 852  C CG  . ASP A 1 108 ? 12.421   54.995 -8.128  1.00 128.89 ?  108 ASP A CG  1 
ATOM 853  O OD1 . ASP A 1 108 ? 12.128   55.322 -9.297  1.00 119.31 ?  108 ASP A OD1 1 
ATOM 854  O OD2 . ASP A 1 108 ? 13.143   55.695 -7.387  1.00 146.26 -1 108 ASP A OD2 1 
ATOM 855  N N   . PHE A 1 109 ? 9.425    51.462 -6.962  1.00 100.62 ?  109 PHE A N   1 
ATOM 856  C CA  . PHE A 1 109 ? 8.886    50.110 -7.020  1.00 100.35 ?  109 PHE A CA  1 
ATOM 857  C C   . PHE A 1 109 ? 7.469    50.083 -7.572  1.00 103.43 ?  109 PHE A C   1 
ATOM 858  O O   . PHE A 1 109 ? 7.061    49.080 -8.169  1.00 99.88  ?  109 PHE A O   1 
ATOM 859  C CB  . PHE A 1 109 ? 8.912    49.470 -5.627  1.00 102.42 ?  109 PHE A CB  1 
ATOM 860  C CG  . PHE A 1 109 ? 8.262    48.116 -5.568  1.00 94.94  ?  109 PHE A CG  1 
ATOM 861  C CD1 . PHE A 1 109 ? 6.979    47.968 -5.067  1.00 106.91 ?  109 PHE A CD1 1 
ATOM 862  C CD2 . PHE A 1 109 ? 8.936    46.991 -6.014  1.00 105.63 ?  109 PHE A CD2 1 
ATOM 863  C CE1 . PHE A 1 109 ? 6.380    46.723 -5.013  1.00 114.86 ?  109 PHE A CE1 1 
ATOM 864  C CE2 . PHE A 1 109 ? 8.342    45.744 -5.962  1.00 103.86 ?  109 PHE A CE2 1 
ATOM 865  C CZ  . PHE A 1 109 ? 7.063    45.610 -5.461  1.00 101.19 ?  109 PHE A CZ  1 
ATOM 866  N N   . PHE A 1 110 ? 6.716    51.170 -7.386  1.00 101.54 ?  110 PHE A N   1 
ATOM 867  C CA  . PHE A 1 110 ? 5.349    51.243 -7.892  1.00 93.67  ?  110 PHE A CA  1 
ATOM 868  C C   . PHE A 1 110 ? 5.323    51.142 -9.414  1.00 99.44  ?  110 PHE A C   1 
ATOM 869  O O   . PHE A 1 110 ? 4.694    50.243 -9.982  1.00 97.90  ?  110 PHE A O   1 
ATOM 870  C CB  . PHE A 1 110 ? 4.698    52.547 -7.422  1.00 83.62  ?  110 PHE A CB  1 
ATOM 871  C CG  . PHE A 1 110 ? 3.251    52.690 -7.811  1.00 91.44  ?  110 PHE A CG  1 
ATOM 872  C CD1 . PHE A 1 110 ? 2.683    53.947 -7.946  1.00 81.25  ?  110 PHE A CD1 1 
ATOM 873  C CD2 . PHE A 1 110 ? 2.451    51.577 -8.015  1.00 91.01  ?  110 PHE A CD2 1 
ATOM 874  C CE1 . PHE A 1 110 ? 1.354    54.092 -8.296  1.00 64.30  ?  110 PHE A CE1 1 
ATOM 875  C CE2 . PHE A 1 110 ? 1.120    51.715 -8.365  1.00 78.80  ?  110 PHE A CE2 1 
ATOM 876  C CZ  . PHE A 1 110 ? 0.572    52.975 -8.505  1.00 59.53  ?  110 PHE A CZ  1 
ATOM 877  N N   . LYS A 1 111 ? 6.010    52.062 -10.093 1.00 94.02  ?  111 LYS A N   1 
ATOM 878  C CA  . LYS A 1 111 ? 5.979    52.099 -11.549 1.00 94.53  ?  111 LYS A CA  1 
ATOM 879  C C   . LYS A 1 111 ? 6.808    50.996 -12.193 1.00 86.00  ?  111 LYS A C   1 
ATOM 880  O O   . LYS A 1 111 ? 6.765    50.855 -13.420 1.00 95.90  ?  111 LYS A O   1 
ATOM 881  C CB  . LYS A 1 111 ? 6.462    53.461 -12.045 1.00 85.57  ?  111 LYS A CB  1 
ATOM 882  C CG  . LYS A 1 111 ? 7.703    53.964 -11.339 1.00 84.91  ?  111 LYS A CG  1 
ATOM 883  C CD  . LYS A 1 111 ? 7.898    55.447 -11.575 1.00 88.14  ?  111 LYS A CD  1 
ATOM 884  C CE  . LYS A 1 111 ? 9.054    55.983 -10.754 1.00 92.48  ?  111 LYS A CE  1 
ATOM 885  N NZ  . LYS A 1 111 ? 9.217    57.447 -10.946 1.00 98.33  ?  111 LYS A NZ  1 
ATOM 886  N N   . SER A 1 112 ? 7.554    50.218 -11.410 1.00 86.37  ?  112 SER A N   1 
ATOM 887  C CA  . SER A 1 112 ? 8.368    49.145 -11.963 1.00 96.71  ?  112 SER A CA  1 
ATOM 888  C C   . SER A 1 112 ? 7.604    47.839 -12.132 1.00 95.47  ?  112 SER A C   1 
ATOM 889  O O   . SER A 1 112 ? 8.015    46.999 -12.940 1.00 105.53 ?  112 SER A O   1 
ATOM 890  C CB  . SER A 1 112 ? 9.594    48.899 -11.079 1.00 95.45  ?  112 SER A CB  1 
ATOM 891  O OG  . SER A 1 112 ? 9.212    48.426 -9.800  1.00 106.32 ?  112 SER A OG  1 
ATOM 892  N N   . ASN A 1 113 ? 6.511    47.646 -11.394 1.00 94.65  ?  113 ASN A N   1 
ATOM 893  C CA  . ASN A 1 113 ? 5.729    46.419 -11.483 1.00 101.44 ?  113 ASN A CA  1 
ATOM 894  C C   . ASN A 1 113 ? 4.243    46.637 -11.718 1.00 100.47 ?  113 ASN A C   1 
ATOM 895  O O   . ASN A 1 113 ? 3.579    45.712 -12.203 1.00 102.60 ?  113 ASN A O   1 
ATOM 896  C CB  . ASN A 1 113 ? 5.903    45.577 -10.210 1.00 90.94  ?  113 ASN A CB  1 
ATOM 897  C CG  . ASN A 1 113 ? 7.299    45.005 -10.077 1.00 96.87  ?  113 ASN A CG  1 
ATOM 898  O OD1 . ASN A 1 113 ? 7.965    45.192 -9.060  1.00 87.93  ?  113 ASN A OD1 1 
ATOM 899  N ND2 . ASN A 1 113 ? 7.750    44.303 -11.110 1.00 98.86  ?  113 ASN A ND2 1 
ATOM 900  N N   . PHE A 1 114 ? 3.696    47.808 -11.396 1.00 92.28  ?  114 PHE A N   1 
ATOM 901  C CA  . PHE A 1 114 ? 2.276    48.082 -11.583 1.00 95.17  ?  114 PHE A CA  1 
ATOM 902  C C   . PHE A 1 114 ? 1.993    48.962 -12.791 1.00 88.19  ?  114 PHE A C   1 
ATOM 903  O O   . PHE A 1 114 ? 1.071    48.672 -13.559 1.00 88.37  ?  114 PHE A O   1 
ATOM 904  C CB  . PHE A 1 114 ? 1.696    48.751 -10.333 1.00 104.35 ?  114 PHE A CB  1 
ATOM 905  C CG  . PHE A 1 114 ? 1.756    47.895 -9.104  1.00 97.32  ?  114 PHE A CG  1 
ATOM 906  C CD1 . PHE A 1 114 ? 0.842    46.873 -8.910  1.00 97.84  ?  114 PHE A CD1 1 
ATOM 907  C CD2 . PHE A 1 114 ? 2.726    48.115 -8.142  1.00 99.11  ?  114 PHE A CD2 1 
ATOM 908  C CE1 . PHE A 1 114 ? 0.897    46.085 -7.778  1.00 97.74  ?  114 PHE A CE1 1 
ATOM 909  C CE2 . PHE A 1 114 ? 2.785    47.331 -7.008  1.00 109.24 ?  114 PHE A CE2 1 
ATOM 910  C CZ  . PHE A 1 114 ? 1.869    46.316 -6.826  1.00 110.22 ?  114 PHE A CZ  1 
ATOM 911  N N   . LEU A 1 115 ? 2.764    50.030 -12.975 1.00 84.12  ?  115 LEU A N   1 
ATOM 912  C CA  . LEU A 1 115 ? 2.560    50.957 -14.076 1.00 98.40  ?  115 LEU A CA  1 
ATOM 913  C C   . LEU A 1 115 ? 3.359    50.581 -15.317 1.00 93.55  ?  115 LEU A C   1 
ATOM 914  O O   . LEU A 1 115 ? 3.407    51.366 -16.270 1.00 95.26  ?  115 LEU A O   1 
ATOM 915  C CB  . LEU A 1 115 ? 2.914    52.377 -13.631 1.00 83.01  ?  115 LEU A CB  1 
ATOM 916  C CG  . LEU A 1 115 ? 2.359    52.773 -12.260 1.00 72.85  ?  115 LEU A CG  1 
ATOM 917  C CD1 . LEU A 1 115 ? 2.818    54.170 -11.876 1.00 86.78  ?  115 LEU A CD1 1 
ATOM 918  C CD2 . LEU A 1 115 ? 0.839    52.675 -12.242 1.00 75.71  ?  115 LEU A CD2 1 
ATOM 919  N N   . THR A 1 116 ? 3.982    49.405 -15.330 1.00 88.49  ?  116 THR A N   1 
ATOM 920  C CA  . THR A 1 116 ? 4.743    48.923 -16.479 1.00 85.52  ?  116 THR A CA  1 
ATOM 921  C C   . THR A 1 116 ? 4.219    47.542 -16.847 1.00 91.97  ?  116 THR A C   1 
ATOM 922  O O   . THR A 1 116 ? 4.443    46.573 -16.114 1.00 105.56 ?  116 THR A O   1 
ATOM 923  C CB  . THR A 1 116 ? 6.241    48.873 -16.178 1.00 81.92  ?  116 THR A CB  1 
ATOM 924  O OG1 . THR A 1 116 ? 6.713    50.190 -15.865 1.00 89.53  ?  116 THR A OG1 1 
ATOM 925  C CG2 . THR A 1 116 ? 7.005    48.340 -17.380 1.00 78.28  ?  116 THR A CG2 1 
ATOM 926  N N   . TYR A 1 117 ? 3.525    47.454 -17.980 1.00 96.33  ?  117 TYR A N   1 
ATOM 927  C CA  . TYR A 1 117 ? 2.890    46.218 -18.412 1.00 99.65  ?  117 TYR A CA  1 
ATOM 928  C C   . TYR A 1 117 ? 3.081    46.066 -19.915 1.00 107.86 ?  117 TYR A C   1 
ATOM 929  O O   . TYR A 1 117 ? 3.670    46.925 -20.579 1.00 111.16 ?  117 TYR A O   1 
ATOM 930  C CB  . TYR A 1 117 ? 1.404    46.201 -18.034 1.00 97.62  ?  117 TYR A CB  1 
ATOM 931  C CG  . TYR A 1 117 ? 0.620    47.390 -18.548 1.00 104.42 ?  117 TYR A CG  1 
ATOM 932  C CD1 . TYR A 1 117 ? 0.659    48.613 -17.888 1.00 105.04 ?  117 TYR A CD1 1 
ATOM 933  C CD2 . TYR A 1 117 ? -0.165   47.288 -19.688 1.00 94.73  ?  117 TYR A CD2 1 
ATOM 934  C CE1 . TYR A 1 117 ? -0.055   49.699 -18.353 1.00 97.00  ?  117 TYR A CE1 1 
ATOM 935  C CE2 . TYR A 1 117 ? -0.885   48.370 -20.160 1.00 106.26 ?  117 TYR A CE2 1 
ATOM 936  C CZ  . TYR A 1 117 ? -0.828   49.572 -19.486 1.00 104.68 ?  117 TYR A CZ  1 
ATOM 937  O OH  . TYR A 1 117 ? -1.542   50.653 -19.951 1.00 103.94 ?  117 TYR A OH  1 
ATOM 938  N N   . THR A 1 118 ? 2.573    44.960 -20.454 1.00 107.23 ?  118 THR A N   1 
ATOM 939  C CA  . THR A 1 118 ? 2.674    44.656 -21.875 1.00 108.07 ?  118 THR A CA  1 
ATOM 940  C C   . THR A 1 118 ? 1.287    44.365 -22.425 1.00 114.33 ?  118 THR A C   1 
ATOM 941  O O   . THR A 1 118 ? 0.579    43.495 -21.907 1.00 116.75 ?  118 THR A O   1 
ATOM 942  C CB  . THR A 1 118 ? 3.600    43.461 -22.126 1.00 109.52 ?  118 THR A CB  1 
ATOM 943  O OG1 . THR A 1 118 ? 4.916    43.765 -21.647 1.00 114.22 ?  118 THR A OG1 1 
ATOM 944  C CG2 . THR A 1 118 ? 3.667    43.144 -23.612 1.00 96.11  ?  118 THR A CG2 1 
ATOM 945  N N   . GLU A 1 119 ? 0.904    45.091 -23.474 1.00 110.73 ?  119 GLU A N   1 
ATOM 946  C CA  . GLU A 1 119 ? -0.405   44.946 -24.099 1.00 115.96 ?  119 GLU A CA  1 
ATOM 947  C C   . GLU A 1 119 ? -0.225   44.883 -25.608 1.00 120.46 ?  119 GLU A C   1 
ATOM 948  O O   . GLU A 1 119 ? 0.246    45.849 -26.218 1.00 109.45 ?  119 GLU A O   1 
ATOM 949  C CB  . GLU A 1 119 ? -1.330   46.103 -23.712 1.00 121.40 ?  119 GLU A CB  1 
ATOM 950  C CG  . GLU A 1 119 ? -2.804   45.828 -23.952 1.00 132.03 ?  119 GLU A CG  1 
ATOM 951  C CD  . GLU A 1 119 ? -3.678   47.032 -23.657 1.00 130.29 ?  119 GLU A CD  1 
ATOM 952  O OE1 . GLU A 1 119 ? -3.210   48.172 -23.859 1.00 142.22 ?  119 GLU A OE1 1 
ATOM 953  O OE2 . GLU A 1 119 ? -4.832   46.837 -23.221 1.00 113.02 -1 119 GLU A OE2 1 
ATOM 954  N N   . LYS A 1 120 ? -0.596   43.746 -26.202 1.00 123.01 ?  120 LYS A N   1 
ATOM 955  C CA  . LYS A 1 120 ? -0.531   43.543 -27.651 1.00 118.22 ?  120 LYS A CA  1 
ATOM 956  C C   . LYS A 1 120 ? 0.895    43.720 -28.174 1.00 128.28 ?  120 LYS A C   1 
ATOM 957  O O   . LYS A 1 120 ? 1.146    44.461 -29.127 1.00 130.13 ?  120 LYS A O   1 
ATOM 958  C CB  . LYS A 1 120 ? -1.505   44.470 -28.382 1.00 122.96 ?  120 LYS A CB  1 
ATOM 959  C CG  . LYS A 1 120 ? -2.931   44.412 -27.858 1.00 136.57 ?  120 LYS A CG  1 
ATOM 960  C CD  . LYS A 1 120 ? -3.801   45.475 -28.511 1.00 167.34 ?  120 LYS A CD  1 
ATOM 961  C CE  . LYS A 1 120 ? -5.184   45.523 -27.880 1.00 173.90 ?  120 LYS A CE  1 
ATOM 962  N NZ  . LYS A 1 120 ? -6.017   46.620 -28.445 1.00 177.14 ?  120 LYS A NZ  1 
ATOM 963  N N   . LYS A 1 121 ? 1.836    43.035 -27.526 1.00 126.47 ?  121 LYS A N   1 
ATOM 964  C CA  . LYS A 1 121 ? 3.252    43.003 -27.886 1.00 130.58 ?  121 LYS A CA  1 
ATOM 965  C C   . LYS A 1 121 ? 3.930    44.367 -27.798 1.00 124.14 ?  121 LYS A C   1 
ATOM 966  O O   . LYS A 1 121 ? 5.072    44.514 -28.249 1.00 134.44 ?  121 LYS A O   1 
ATOM 967  C CB  . LYS A 1 121 ? 3.465    42.407 -29.285 1.00 137.29 ?  121 LYS A CB  1 
ATOM 968  C CG  . LYS A 1 121 ? 3.203    40.912 -29.362 1.00 125.98 ?  121 LYS A CG  1 
ATOM 969  C CD  . LYS A 1 121 ? 3.632    40.345 -30.704 1.00 135.24 ?  121 LYS A CD  1 
ATOM 970  C CE  . LYS A 1 121 ? 3.559    38.827 -30.707 1.00 128.60 ?  121 LYS A CE  1 
ATOM 971  N NZ  . LYS A 1 121 ? 4.075    38.252 -31.979 1.00 125.82 ?  121 LYS A NZ  1 
ATOM 972  N N   . ILE A 1 122 ? 3.263    45.370 -27.233 1.00 113.95 ?  122 ILE A N   1 
ATOM 973  C CA  . ILE A 1 122 ? 3.886    46.654 -26.945 1.00 116.74 ?  122 ILE A CA  1 
ATOM 974  C C   . ILE A 1 122 ? 3.686    46.957 -25.467 1.00 119.09 ?  122 ILE A C   1 
ATOM 975  O O   . ILE A 1 122 ? 2.706    46.528 -24.849 1.00 119.88 ?  122 ILE A O   1 
ATOM 976  C CB  . ILE A 1 122 ? 3.333    47.795 -27.833 1.00 108.21 ?  122 ILE A CB  1 
ATOM 977  C CG1 . ILE A 1 122 ? 4.448    48.785 -28.178 1.00 122.67 ?  122 ILE A CG1 1 
ATOM 978  C CG2 . ILE A 1 122 ? 2.170    48.510 -27.159 1.00 84.29  ?  122 ILE A CG2 1 
ATOM 979  C CD1 . ILE A 1 122 ? 4.021    49.890 -29.118 1.00 124.15 ?  122 ILE A CD1 1 
ATOM 980  N N   . LYS A 1 123 ? 4.640    47.680 -24.892 1.00 105.94 ?  123 LYS A N   1 
ATOM 981  C CA  . LYS A 1 123 ? 4.624    47.986 -23.471 1.00 99.83  ?  123 LYS A CA  1 
ATOM 982  C C   . LYS A 1 123 ? 4.076    49.387 -23.229 1.00 101.56 ?  123 LYS A C   1 
ATOM 983  O O   . LYS A 1 123 ? 3.984    50.213 -24.140 1.00 107.80 ?  123 LYS A O   1 
ATOM 984  C CB  . LYS A 1 123 ? 6.027    47.861 -22.870 1.00 97.52  ?  123 LYS A CB  1 
ATOM 985  C CG  . LYS A 1 123 ? 6.939    49.039 -23.166 1.00 108.35 ?  123 LYS A CG  1 
ATOM 986  C CD  . LYS A 1 123 ? 8.184    48.996 -22.296 1.00 95.49  ?  123 LYS A CD  1 
ATOM 987  C CE  . LYS A 1 123 ? 9.042    50.233 -22.498 1.00 123.22 ?  123 LYS A CE  1 
ATOM 988  N NZ  . LYS A 1 123 ? 10.245   50.222 -21.621 1.00 129.91 ?  123 LYS A NZ  1 
ATOM 989  N N   . HIS A 1 124 ? 3.711    49.645 -21.976 1.00 99.06  ?  124 HIS A N   1 
ATOM 990  C CA  . HIS A 1 124 ? 3.157    50.929 -21.581 1.00 104.10 ?  124 HIS A CA  1 
ATOM 991  C C   . HIS A 1 124 ? 3.773    51.368 -20.262 1.00 103.65 ?  124 HIS A C   1 
ATOM 992  O O   . HIS A 1 124 ? 4.267    50.554 -19.479 1.00 96.84  ?  124 HIS A O   1 
ATOM 993  C CB  . HIS A 1 124 ? 1.629    50.873 -21.443 1.00 115.75 ?  124 HIS A CB  1 
ATOM 994  C CG  . HIS A 1 124 ? 0.916    50.519 -22.710 1.00 105.83 ?  124 HIS A CG  1 
ATOM 995  N ND1 . HIS A 1 124 ? 0.269    51.456 -23.485 1.00 109.99 ?  124 HIS A ND1 1 
ATOM 996  C CD2 . HIS A 1 124 ? 0.742    49.330 -23.334 1.00 102.55 ?  124 HIS A CD2 1 
ATOM 997  C CE1 . HIS A 1 124 ? -0.271   50.861 -24.533 1.00 116.30 ?  124 HIS A CE1 1 
ATOM 998  N NE2 . HIS A 1 124 ? 0.002    49.570 -24.466 1.00 103.72 ?  124 HIS A NE2 1 
ATOM 999  N N   . GLU A 1 125 ? 3.736    52.678 -20.029 1.00 102.14 ?  125 GLU A N   1 
ATOM 1000 C CA  . GLU A 1 125 ? 4.122    53.273 -18.751 1.00 99.40  ?  125 GLU A CA  1 
ATOM 1001 C C   . GLU A 1 125 ? 3.030    54.278 -18.395 1.00 110.88 ?  125 GLU A C   1 
ATOM 1002 O O   . GLU A 1 125 ? 2.989    55.379 -18.953 1.00 116.94 ?  125 GLU A O   1 
ATOM 1003 C CB  . GLU A 1 125 ? 5.498    53.927 -18.823 1.00 95.16  ?  125 GLU A CB  1 
ATOM 1004 C CG  . GLU A 1 125 ? 6.617    52.958 -19.176 1.00 93.94  ?  125 GLU A CG  1 
ATOM 1005 C CD  . GLU A 1 125 ? 7.989    53.594 -19.101 1.00 109.79 ?  125 GLU A CD  1 
ATOM 1006 O OE1 . GLU A 1 125 ? 8.303    54.205 -18.058 1.00 110.32 ?  125 GLU A OE1 1 
ATOM 1007 O OE2 . GLU A 1 125 ? 8.753    53.484 -20.082 1.00 120.88 -1 125 GLU A OE2 1 
ATOM 1008 N N   . TYR A 1 126 ? 2.147    53.884 -17.472 1.00 106.40 ?  126 TYR A N   1 
ATOM 1009 C CA  . TYR A 1 126 ? 0.933    54.654 -17.211 1.00 109.45 ?  126 TYR A CA  1 
ATOM 1010 C C   . TYR A 1 126 ? 1.249    56.084 -16.789 1.00 103.40 ?  126 TYR A C   1 
ATOM 1011 O O   . TYR A 1 126 ? 0.576    57.028 -17.220 1.00 113.49 ?  126 TYR A O   1 
ATOM 1012 C CB  . TYR A 1 126 ? 0.090    53.954 -16.145 1.00 106.59 ?  126 TYR A CB  1 
ATOM 1013 C CG  . TYR A 1 126 ? -1.342   54.439 -16.082 1.00 110.01 ?  126 TYR A CG  1 
ATOM 1014 C CD1 . TYR A 1 126 ? -1.680   55.578 -15.361 1.00 92.61  ?  126 TYR A CD1 1 
ATOM 1015 C CD2 . TYR A 1 126 ? -2.354   53.759 -16.745 1.00 97.55  ?  126 TYR A CD2 1 
ATOM 1016 C CE1 . TYR A 1 126 ? -2.986   56.025 -15.304 1.00 81.66  ?  126 TYR A CE1 1 
ATOM 1017 C CE2 . TYR A 1 126 ? -3.663   54.198 -16.693 1.00 98.44  ?  126 TYR A CE2 1 
ATOM 1018 C CZ  . TYR A 1 126 ? -3.972   55.331 -15.971 1.00 100.61 ?  126 TYR A CZ  1 
ATOM 1019 O OH  . TYR A 1 126 ? -5.273   55.772 -15.916 1.00 120.94 ?  126 TYR A OH  1 
ATOM 1020 N N   . HIS A 1 127 ? 2.266    56.267 -15.944 1.00 95.27  ?  127 HIS A N   1 
ATOM 1021 C CA  . HIS A 1 127 ? 2.623    57.613 -15.506 1.00 104.00 ?  127 HIS A CA  1 
ATOM 1022 C C   . HIS A 1 127 ? 3.171    58.444 -16.661 1.00 109.46 ?  127 HIS A C   1 
ATOM 1023 O O   . HIS A 1 127 ? 2.912    59.650 -16.742 1.00 115.93 ?  127 HIS A O   1 
ATOM 1024 C CB  . HIS A 1 127 ? 3.631    57.544 -14.358 1.00 104.82 ?  127 HIS A CB  1 
ATOM 1025 C CG  . HIS A 1 127 ? 4.886    56.801 -14.696 1.00 105.62 ?  127 HIS A CG  1 
ATOM 1026 N ND1 . HIS A 1 127 ? 4.893    55.466 -15.039 1.00 92.62  ?  127 HIS A ND1 1 
ATOM 1027 C CD2 . HIS A 1 127 ? 6.177    57.206 -14.742 1.00 103.13 ?  127 HIS A CD2 1 
ATOM 1028 C CE1 . HIS A 1 127 ? 6.133    55.081 -15.282 1.00 102.22 ?  127 HIS A CE1 1 
ATOM 1029 N NE2 . HIS A 1 127 ? 6.932    56.119 -15.109 1.00 110.43 ?  127 HIS A NE2 1 
ATOM 1030 N N   . ILE A 1 128 ? 3.930    57.818 -17.562 1.00 103.54 ?  128 ILE A N   1 
ATOM 1031 C CA  . ILE A 1 128 ? 4.420    58.524 -18.743 1.00 99.80  ?  128 ILE A CA  1 
ATOM 1032 C C   . ILE A 1 128 ? 3.270    58.824 -19.696 1.00 102.61 ?  128 ILE A C   1 
ATOM 1033 O O   . ILE A 1 128 ? 3.134    59.945 -20.202 1.00 92.22  ?  128 ILE A O   1 
ATOM 1034 C CB  . ILE A 1 128 ? 5.529    57.711 -19.434 1.00 98.49  ?  128 ILE A CB  1 
ATOM 1035 C CG1 . ILE A 1 128 ? 6.841    57.827 -18.655 1.00 97.70  ?  128 ILE A CG1 1 
ATOM 1036 C CG2 . ILE A 1 128 ? 5.714    58.164 -20.877 1.00 111.07 ?  128 ILE A CG2 1 
ATOM 1037 C CD1 . ILE A 1 128 ? 8.013    57.160 -19.336 1.00 103.97 ?  128 ILE A CD1 1 
ATOM 1038 N N   . GLU A 1 129 ? 2.420    57.830 -19.947 1.00 104.62 ?  129 GLU A N   1 
ATOM 1039 C CA  . GLU A 1 129 ? 1.275    57.966 -20.842 1.00 100.42 ?  129 GLU A CA  1 
ATOM 1040 C C   . GLU A 1 129 ? 0.139    58.789 -20.243 1.00 107.96 ?  129 GLU A C   1 
ATOM 1041 O O   . GLU A 1 129 ? -0.944   58.825 -20.838 1.00 120.21 ?  129 GLU A O   1 
ATOM 1042 C CB  . GLU A 1 129 ? 0.765    56.581 -21.242 1.00 100.87 ?  129 GLU A CB  1 
ATOM 1043 C CG  . GLU A 1 129 ? 1.809    55.719 -21.933 1.00 105.39 ?  129 GLU A CG  1 
ATOM 1044 C CD  . GLU A 1 129 ? 1.307    54.322 -22.241 1.00 108.68 ?  129 GLU A CD  1 
ATOM 1045 O OE1 . GLU A 1 129 ? 0.130    54.030 -21.944 1.00 119.20 ?  129 GLU A OE1 1 
ATOM 1046 O OE2 . GLU A 1 129 ? 2.092    53.516 -22.782 1.00 100.68 -1 129 GLU A OE2 1 
ATOM 1047 N N   . ASN A 1 130 ? 0.323    59.429 -19.088 1.00 113.72 ?  130 ASN A N   1 
ATOM 1048 C CA  . ASN A 1 130 ? -0.678   60.345 -18.561 1.00 105.42 ?  130 ASN A CA  1 
ATOM 1049 C C   . ASN A 1 130 ? -0.082   61.594 -17.927 1.00 105.81 ?  130 ASN A C   1 
ATOM 1050 O O   . ASN A 1 130 ? -0.840   62.411 -17.395 1.00 111.78 ?  130 ASN A O   1 
ATOM 1051 C CB  . ASN A 1 130 ? -1.577   59.630 -17.538 1.00 107.31 ?  130 ASN A CB  1 
ATOM 1052 C CG  . ASN A 1 130 ? -2.497   58.611 -18.185 1.00 106.81 ?  130 ASN A CG  1 
ATOM 1053 O OD1 . ASN A 1 130 ? -3.585   58.949 -18.650 1.00 111.55 ?  130 ASN A OD1 1 
ATOM 1054 N ND2 . ASN A 1 130 ? -2.060   57.358 -18.222 1.00 106.72 ?  130 ASN A ND2 1 
ATOM 1055 N N   . GLY A 1 131 ? 1.237    61.772 -17.969 1.00 114.15 ?  131 GLY A N   1 
ATOM 1056 C CA  . GLY A 1 131 ? 1.871    62.971 -17.456 1.00 121.04 ?  131 GLY A CA  1 
ATOM 1057 C C   . GLY A 1 131 ? 1.647    63.209 -15.978 1.00 117.06 ?  131 GLY A C   1 
ATOM 1058 O O   . GLY A 1 131 ? 0.977    64.172 -15.594 1.00 125.13 ?  131 GLY A O   1 
ATOM 1059 N N   . LEU A 1 132 ? 2.201    62.341 -15.135 1.00 118.59 ?  132 LEU A N   1 
ATOM 1060 C CA  . LEU A 1 132 ? 2.046    62.437 -13.689 1.00 112.15 ?  132 LEU A CA  1 
ATOM 1061 C C   . LEU A 1 132 ? 3.422    62.509 -13.045 1.00 111.07 ?  132 LEU A C   1 
ATOM 1062 O O   . LEU A 1 132 ? 4.222    61.577 -13.178 1.00 109.83 ?  132 LEU A O   1 
ATOM 1063 C CB  . LEU A 1 132 ? 1.259    61.246 -13.141 1.00 109.88 ?  132 LEU A CB  1 
ATOM 1064 C CG  . LEU A 1 132 ? -0.110   60.982 -13.772 1.00 114.68 ?  132 LEU A CG  1 
ATOM 1065 C CD1 . LEU A 1 132 ? -0.768   59.772 -13.128 1.00 73.58  ?  132 LEU A CD1 1 
ATOM 1066 C CD2 . LEU A 1 132 ? -1.003   62.209 -13.657 1.00 110.98 ?  132 LEU A CD2 1 
ATOM 1067 N N   . THR A 1 133 ? 3.693    63.612 -12.352 1.00 113.93 ?  133 THR A N   1 
ATOM 1068 C CA  . THR A 1 133 ? 4.936    63.732 -11.609 1.00 115.31 ?  133 THR A CA  1 
ATOM 1069 C C   . THR A 1 133 ? 4.935    62.772 -10.422 1.00 109.97 ?  133 THR A C   1 
ATOM 1070 O O   . THR A 1 133 ? 3.890    62.284 -9.983  1.00 115.01 ?  133 THR A O   1 
ATOM 1071 C CB  . THR A 1 133 ? 5.138    65.167 -11.119 1.00 127.40 ?  133 THR A CB  1 
ATOM 1072 O OG1 . THR A 1 133 ? 4.506    65.334 -9.843  1.00 119.31 ?  133 THR A OG1 1 
ATOM 1073 C CG2 . THR A 1 133 ? 4.538    66.157 -12.106 1.00 132.33 ?  133 THR A CG2 1 
ATOM 1074 N N   . GLU A 1 134 ? 6.133    62.498 -9.903  1.00 114.34 ?  134 GLU A N   1 
ATOM 1075 C CA  . GLU A 1 134 ? 6.241    61.609 -8.751  1.00 120.35 ?  134 GLU A CA  1 
ATOM 1076 C C   . GLU A 1 134 ? 5.618    62.226 -7.505  1.00 124.82 ?  134 GLU A C   1 
ATOM 1077 O O   . GLU A 1 134 ? 5.108    61.497 -6.646  1.00 126.44 ?  134 GLU A O   1 
ATOM 1078 C CB  . GLU A 1 134 ? 7.703    61.247 -8.499  1.00 130.89 ?  134 GLU A CB  1 
ATOM 1079 C CG  . GLU A 1 134 ? 8.353    60.505 -9.653  1.00 128.06 ?  134 GLU A CG  1 
ATOM 1080 C CD  . GLU A 1 134 ? 9.750    60.024 -9.321  1.00 134.26 ?  134 GLU A CD  1 
ATOM 1081 O OE1 . GLU A 1 134 ? 10.280   60.417 -8.260  1.00 143.17 ?  134 GLU A OE1 1 
ATOM 1082 O OE2 . GLU A 1 134 ? 10.316   59.249 -10.120 1.00 128.66 -1 134 GLU A OE2 1 
ATOM 1083 N N   . GLU A 1 135 ? 5.656    63.555 -7.384  1.00 129.96 ?  135 GLU A N   1 
ATOM 1084 C CA  . GLU A 1 135 ? 4.930    64.216 -6.304  1.00 124.79 ?  135 GLU A CA  1 
ATOM 1085 C C   . GLU A 1 135 ? 3.428    64.012 -6.456  1.00 118.86 ?  135 GLU A C   1 
ATOM 1086 O O   . GLU A 1 135 ? 2.728    63.740 -5.474  1.00 121.15 ?  135 GLU A O   1 
ATOM 1087 C CB  . GLU A 1 135 ? 5.269    65.707 -6.272  1.00 133.17 ?  135 GLU A CB  1 
ATOM 1088 C CG  . GLU A 1 135 ? 6.617    66.030 -5.648  1.00 151.19 ?  135 GLU A CG  1 
ATOM 1089 C CD  . GLU A 1 135 ? 7.757    65.941 -6.644  1.00 172.78 ?  135 GLU A CD  1 
ATOM 1090 O OE1 . GLU A 1 135 ? 8.671    65.117 -6.429  1.00 182.68 ?  135 GLU A OE1 1 
ATOM 1091 O OE2 . GLU A 1 135 ? 7.737    66.693 -7.641  1.00 188.74 -1 135 GLU A OE2 1 
ATOM 1092 N N   . ASP A 1 136 ? 2.916    64.144 -7.683  1.00 124.62 ?  136 ASP A N   1 
ATOM 1093 C CA  . ASP A 1 136 ? 1.507    63.860 -7.932  1.00 119.16 ?  136 ASP A CA  1 
ATOM 1094 C C   . ASP A 1 136 ? 1.182    62.396 -7.667  1.00 110.41 ?  136 ASP A C   1 
ATOM 1095 O O   . ASP A 1 136 ? 0.063    62.074 -7.251  1.00 123.82 ?  136 ASP A O   1 
ATOM 1096 C CB  . ASP A 1 136 ? 1.142    64.235 -9.369  1.00 118.95 ?  136 ASP A CB  1 
ATOM 1097 C CG  . ASP A 1 136 ? 1.463    65.682 -9.696  1.00 126.33 ?  136 ASP A CG  1 
ATOM 1098 O OD1 . ASP A 1 136 ? 2.084    66.363 -8.853  1.00 128.89 ?  136 ASP A OD1 1 
ATOM 1099 O OD2 . ASP A 1 136 ? 1.097    66.137 -10.800 1.00 133.15 -1 136 ASP A OD2 1 
ATOM 1100 N N   . LEU A 1 137 ? 2.143    61.499 -7.902  1.00 101.22 ?  137 LEU A N   1 
ATOM 1101 C CA  . LEU A 1 137 ? 1.927    60.084 -7.623  1.00 103.15 ?  137 LEU A CA  1 
ATOM 1102 C C   . LEU A 1 137 ? 1.948    59.794 -6.129  1.00 110.54 ?  137 LEU A C   1 
ATOM 1103 O O   . LEU A 1 137 ? 1.267    58.869 -5.670  1.00 118.11 ?  137 LEU A O   1 
ATOM 1104 C CB  . LEU A 1 137 ? 2.987    59.240 -8.331  1.00 103.74 ?  137 LEU A CB  1 
ATOM 1105 C CG  . LEU A 1 137 ? 2.839    59.007 -9.836  1.00 102.84 ?  137 LEU A CG  1 
ATOM 1106 C CD1 . LEU A 1 137 ? 3.926    58.066 -10.335 1.00 92.41  ?  137 LEU A CD1 1 
ATOM 1107 C CD2 . LEU A 1 137 ? 1.460    58.462 -10.166 1.00 109.18 ?  137 LEU A CD2 1 
ATOM 1108 N N   . GLN A 1 138 ? 2.722    60.564 -5.358  1.00 105.97 ?  138 GLN A N   1 
ATOM 1109 C CA  . GLN A 1 138 ? 2.888    60.266 -3.939  1.00 111.26 ?  138 GLN A CA  1 
ATOM 1110 C C   . GLN A 1 138 ? 1.565    60.359 -3.188  1.00 109.67 ?  138 GLN A C   1 
ATOM 1111 O O   . GLN A 1 138 ? 1.320    59.589 -2.252  1.00 117.42 ?  138 GLN A O   1 
ATOM 1112 C CB  . GLN A 1 138 ? 3.925    61.206 -3.324  1.00 116.64 ?  138 GLN A CB  1 
ATOM 1113 C CG  . GLN A 1 138 ? 4.348    60.820 -1.913  1.00 122.41 ?  138 GLN A CG  1 
ATOM 1114 C CD  . GLN A 1 138 ? 5.086    59.496 -1.863  1.00 125.96 ?  138 GLN A CD  1 
ATOM 1115 O OE1 . GLN A 1 138 ? 5.706    59.080 -2.842  1.00 124.88 ?  138 GLN A OE1 1 
ATOM 1116 N NE2 . GLN A 1 138 ? 5.018    58.822 -0.720  1.00 125.43 ?  138 GLN A NE2 1 
ATOM 1117 N N   . ALA A 1 139 ? 0.700    61.297 -3.583  1.00 93.85  ?  139 ALA A N   1 
ATOM 1118 C CA  . ALA A 1 139 ? -0.601   61.416 -2.933  1.00 104.79 ?  139 ALA A CA  1 
ATOM 1119 C C   . ALA A 1 139 ? -1.442   60.165 -3.136  1.00 109.96 ?  139 ALA A C   1 
ATOM 1120 O O   . ALA A 1 139 ? -2.204   59.779 -2.242  1.00 115.92 ?  139 ALA A O   1 
ATOM 1121 C CB  . ALA A 1 139 ? -1.341   62.649 -3.455  1.00 101.32 ?  139 ALA A CB  1 
ATOM 1122 N N   . PHE A 1 140 ? -1.313   59.516 -4.295  1.00 100.60 ?  140 PHE A N   1 
ATOM 1123 C CA  . PHE A 1 140 ? -2.092   58.312 -4.561  1.00 91.43  ?  140 PHE A CA  1 
ATOM 1124 C C   . PHE A 1 140 ? -1.664   57.165 -3.653  1.00 89.99  ?  140 PHE A C   1 
ATOM 1125 O O   . PHE A 1 140 ? -2.505   56.522 -3.013  1.00 99.16  ?  140 PHE A O   1 
ATOM 1126 C CB  . PHE A 1 140 ? -1.960   57.916 -6.031  1.00 94.80  ?  140 PHE A CB  1 
ATOM 1127 C CG  . PHE A 1 140 ? -2.762   56.703 -6.403  1.00 90.79  ?  140 PHE A CG  1 
ATOM 1128 C CD1 . PHE A 1 140 ? -2.157   55.461 -6.507  1.00 82.17  ?  140 PHE A CD1 1 
ATOM 1129 C CD2 . PHE A 1 140 ? -4.123   56.801 -6.642  1.00 84.61  ?  140 PHE A CD2 1 
ATOM 1130 C CE1 . PHE A 1 140 ? -2.891   54.341 -6.849  1.00 81.32  ?  140 PHE A CE1 1 
ATOM 1131 C CE2 . PHE A 1 140 ? -4.865   55.684 -6.985  1.00 86.92  ?  140 PHE A CE2 1 
ATOM 1132 C CZ  . PHE A 1 140 ? -4.247   54.452 -7.088  1.00 99.49  ?  140 PHE A CZ  1 
ATOM 1133 N N   . LEU A 1 141 ? -0.358   56.892 -3.586  1.00 89.30  ?  141 LEU A N   1 
ATOM 1134 C CA  . LEU A 1 141 ? 0.130    55.805 -2.742  1.00 90.87  ?  141 LEU A CA  1 
ATOM 1135 C C   . LEU A 1 141 ? -0.166   56.059 -1.270  1.00 94.84  ?  141 LEU A C   1 
ATOM 1136 O O   . LEU A 1 141 ? -0.346   55.107 -0.501  1.00 98.67  ?  141 LEU A O   1 
ATOM 1137 C CB  . LEU A 1 141 ? 1.631    55.605 -2.956  1.00 88.06  ?  141 LEU A CB  1 
ATOM 1138 C CG  . LEU A 1 141 ? 2.057    55.092 -4.333  1.00 84.66  ?  141 LEU A CG  1 
ATOM 1139 C CD1 . LEU A 1 141 ? 3.573    55.097 -4.465  1.00 89.67  ?  141 LEU A CD1 1 
ATOM 1140 C CD2 . LEU A 1 141 ? 1.500    53.699 -4.577  1.00 92.11  ?  141 LEU A CD2 1 
ATOM 1141 N N   . ASP A 1 142 ? -0.215   57.327 -0.858  1.00 98.33  ?  142 ASP A N   1 
ATOM 1142 C CA  . ASP A 1 142 ? -0.605   57.644 0.511   1.00 95.36  ?  142 ASP A CA  1 
ATOM 1143 C C   . ASP A 1 142 ? -2.085   57.357 0.735   1.00 97.48  ?  142 ASP A C   1 
ATOM 1144 O O   . ASP A 1 142 ? -2.458   56.685 1.704   1.00 96.96  ?  142 ASP A O   1 
ATOM 1145 C CB  . ASP A 1 142 ? -0.281   59.105 0.824   1.00 100.12 ?  142 ASP A CB  1 
ATOM 1146 C CG  . ASP A 1 142 ? 1.210    59.384 0.826   1.00 116.77 ?  142 ASP A CG  1 
ATOM 1147 O OD1 . ASP A 1 142 ? 1.999    58.417 0.767   1.00 115.49 ?  142 ASP A OD1 1 
ATOM 1148 O OD2 . ASP A 1 142 ? 1.593    60.572 0.885   1.00 121.99 -1 142 ASP A OD2 1 
ATOM 1149 N N   . ARG A 1 143 ? -2.944   57.859 -0.155  1.00 97.01  ?  143 ARG A N   1 
ATOM 1150 C CA  . ARG A 1 143 ? -4.372   57.573 -0.081  1.00 95.50  ?  143 ARG A CA  1 
ATOM 1151 C C   . ARG A 1 143 ? -4.698   56.114 -0.371  1.00 89.04  ?  143 ARG A C   1 
ATOM 1152 O O   . ARG A 1 143 ? -5.824   55.684 -0.099  1.00 89.28  ?  143 ARG A O   1 
ATOM 1153 C CB  . ARG A 1 143 ? -5.139   58.469 -1.055  1.00 87.84  ?  143 ARG A CB  1 
ATOM 1154 C CG  . ARG A 1 143 ? -4.979   59.959 -0.802  1.00 116.41 ?  143 ARG A CG  1 
ATOM 1155 C CD  . ARG A 1 143 ? -5.887   60.768 -1.715  1.00 135.47 ?  143 ARG A CD  1 
ATOM 1156 N NE  . ARG A 1 143 ? -5.632   62.202 -1.618  1.00 139.05 ?  143 ARG A NE  1 
ATOM 1157 C CZ  . ARG A 1 143 ? -6.390   63.135 -2.187  1.00 131.41 ?  143 ARG A CZ  1 
ATOM 1158 N NH1 . ARG A 1 143 ? -7.453   62.786 -2.899  1.00 122.13 ?  143 ARG A NH1 1 
ATOM 1159 N NH2 . ARG A 1 143 ? -6.084   64.418 -2.046  1.00 140.53 ?  143 ARG A NH2 1 
ATOM 1160 N N   . LEU A 1 144 ? -3.754   55.350 -0.914  1.00 82.57  ?  144 LEU A N   1 
ATOM 1161 C CA  . LEU A 1 144 ? -3.999   53.955 -1.247  1.00 79.39  ?  144 LEU A CA  1 
ATOM 1162 C C   . LEU A 1 144 ? -3.850   53.072 -0.015  1.00 79.79  ?  144 LEU A C   1 
ATOM 1163 O O   . LEU A 1 144 ? -2.975   53.295 0.828   1.00 81.51  ?  144 LEU A O   1 
ATOM 1164 C CB  . LEU A 1 144 ? -3.037   53.497 -2.343  1.00 68.83  ?  144 LEU A CB  1 
ATOM 1165 C CG  . LEU A 1 144 ? -3.042   52.026 -2.756  1.00 66.68  ?  144 LEU A CG  1 
ATOM 1166 C CD1 . LEU A 1 144 ? -4.421   51.595 -3.230  1.00 75.59  ?  144 LEU A CD1 1 
ATOM 1167 C CD2 . LEU A 1 144 ? -2.004   51.791 -3.839  1.00 88.40  ?  144 LEU A CD2 1 
ATOM 1168 N N   . VAL A 1 145 ? -4.713   52.064 0.084   1.00 78.38  ?  145 VAL A N   1 
ATOM 1169 C CA  . VAL A 1 145 ? -4.708   51.108 1.185   1.00 81.49  ?  145 VAL A CA  1 
ATOM 1170 C C   . VAL A 1 145 ? -4.689   49.713 0.575   1.00 78.19  ?  145 VAL A C   1 
ATOM 1171 O O   . VAL A 1 145 ? -5.667   49.295 -0.057  1.00 82.84  ?  145 VAL A O   1 
ATOM 1172 C CB  . VAL A 1 145 ? -5.919   51.279 2.111   1.00 79.70  ?  145 VAL A CB  1 
ATOM 1173 C CG1 . VAL A 1 145 ? -5.961   50.160 3.136   1.00 90.68  ?  145 VAL A CG1 1 
ATOM 1174 C CG2 . VAL A 1 145 ? -5.880   52.638 2.794   1.00 88.91  ?  145 VAL A CG2 1 
ATOM 1175 N N   . ILE A 1 146 ? -3.587   48.991 0.766   1.00 59.80  ?  146 ILE A N   1 
ATOM 1176 C CA  . ILE A 1 146 ? -3.410   47.654 0.212   1.00 69.19  ?  146 ILE A CA  1 
ATOM 1177 C C   . ILE A 1 146 ? -3.135   46.687 1.354   1.00 83.20  ?  146 ILE A C   1 
ATOM 1178 O O   . ILE A 1 146 ? -2.298   46.964 2.221   1.00 88.76  ?  146 ILE A O   1 
ATOM 1179 C CB  . ILE A 1 146 ? -2.272   47.609 -0.824  1.00 65.74  ?  146 ILE A CB  1 
ATOM 1180 C CG1 . ILE A 1 146 ? -2.635   48.447 -2.051  1.00 85.74  ?  146 ILE A CG1 1 
ATOM 1181 C CG2 . ILE A 1 146 ? -1.976   46.173 -1.229  1.00 68.54  ?  146 ILE A CG2 1 
ATOM 1182 C CD1 . ILE A 1 146 ? -1.720   48.222 -3.235  1.00 91.15  ?  146 ILE A CD1 1 
ATOM 1183 N N   . ASN A 1 147 ? -3.839   45.554 1.352   1.00 70.88  ?  147 ASN A N   1 
ATOM 1184 C CA  . ASN A 1 147 ? -3.645   44.525 2.374   1.00 73.69  ?  147 ASN A CA  1 
ATOM 1185 C C   . ASN A 1 147 ? -3.895   43.174 1.703   1.00 70.92  ?  147 ASN A C   1 
ATOM 1186 O O   . ASN A 1 147 ? -5.033   42.706 1.628   1.00 86.36  ?  147 ASN A O   1 
ATOM 1187 C CB  . ASN A 1 147 ? -4.568   44.747 3.564   1.00 71.09  ?  147 ASN A CB  1 
ATOM 1188 C CG  . ASN A 1 147 ? -4.222   43.864 4.753   1.00 82.49  ?  147 ASN A CG  1 
ATOM 1189 O OD1 . ASN A 1 147 ? -3.620   42.801 4.603   1.00 71.38  ?  147 ASN A OD1 1 
ATOM 1190 N ND2 . ASN A 1 147 ? -4.608   44.304 5.945   1.00 84.86  ?  147 ASN A ND2 1 
ATOM 1191 N N   . ILE A 1 148 ? -2.818   42.551 1.229   1.00 73.60  ?  148 ILE A N   1 
ATOM 1192 C CA  . ILE A 1 148 ? -2.915   41.228 0.623   1.00 74.14  ?  148 ILE A CA  1 
ATOM 1193 C C   . ILE A 1 148 ? -2.710   40.179 1.707   1.00 79.64  ?  148 ILE A C   1 
ATOM 1194 O O   . ILE A 1 148 ? -2.638   38.978 1.424   1.00 87.98  ?  148 ILE A O   1 
ATOM 1195 C CB  . ILE A 1 148 ? -1.900   41.054 -0.521  1.00 69.82  ?  148 ILE A CB  1 
ATOM 1196 C CG1 . ILE A 1 148 ? -0.472   41.060 0.026   1.00 95.58  ?  148 ILE A CG1 1 
ATOM 1197 C CG2 . ILE A 1 148 ? -2.084   42.146 -1.565  1.00 81.53  ?  148 ILE A CG2 1 
ATOM 1198 C CD1 . ILE A 1 148 ? 0.577    40.827 -1.033  1.00 91.27  ?  148 ILE A CD1 1 
ATOM 1199 N N   . ASN A 1 149 ? -2.613   40.634 2.957   1.00 74.46  ?  149 ASN A N   1 
ATOM 1200 C CA  . ASN A 1 149 ? -2.510   39.765 4.122   1.00 83.64  ?  149 ASN A CA  1 
ATOM 1201 C C   . ASN A 1 149 ? -3.789   39.776 4.952   1.00 96.41  ?  149 ASN A C   1 
ATOM 1202 O O   . ASN A 1 149 ? -3.754   39.487 6.152   1.00 104.07 ?  149 ASN A O   1 
ATOM 1203 C CB  . ASN A 1 149 ? -1.317   40.183 4.980   1.00 94.08  ?  149 ASN A CB  1 
ATOM 1204 C CG  . ASN A 1 149 ? -0.030   40.272 4.184   1.00 104.91 ?  149 ASN A CG  1 
ATOM 1205 O OD1 . ASN A 1 149 ? 0.307    39.363 3.426   1.00 91.48  ?  149 ASN A OD1 1 
ATOM 1206 N ND2 . ASN A 1 149 ? 0.688    41.381 4.337   1.00 111.66 ?  149 ASN A ND2 1 
ATOM 1207 N N   . ALA A 1 150 ? -4.918   40.107 4.333   1.00 82.25  ?  150 ALA A N   1 
ATOM 1208 C CA  . ALA A 1 150 ? -6.175   40.255 5.045   1.00 87.08  ?  150 ALA A CA  1 
ATOM 1209 C C   . ALA A 1 150 ? -6.886   38.913 5.181   1.00 96.52  ?  150 ALA A C   1 
ATOM 1210 O O   . ALA A 1 150 ? -6.555   37.928 4.516   1.00 92.62  ?  150 ALA A O   1 
ATOM 1211 C CB  . ALA A 1 150 ? -7.071   41.264 4.330   1.00 91.99  ?  150 ALA A CB  1 
ATOM 1212 N N   . LYS A 1 151 ? -7.884   38.889 6.059   1.00 96.74  ?  151 LYS A N   1 
ATOM 1213 C CA  . LYS A 1 151 ? -8.667   37.685 6.279   1.00 107.23 ?  151 LYS A CA  1 
ATOM 1214 C C   . LYS A 1 151 ? -9.532   37.375 5.061   1.00 116.31 ?  151 LYS A C   1 
ATOM 1215 O O   . LYS A 1 151 ? -9.835   38.244 4.238   1.00 119.90 ?  151 LYS A O   1 
ATOM 1216 C CB  . LYS A 1 151 ? -9.553   37.837 7.517   1.00 94.48  ?  151 LYS A CB  1 
ATOM 1217 C CG  . LYS A 1 151 ? -8.873   38.520 8.687   1.00 91.00  ?  151 LYS A CG  1 
ATOM 1218 C CD  . LYS A 1 151 ? -9.697   38.386 9.956   1.00 84.94  ?  151 LYS A CD  1 
ATOM 1219 C CE  . LYS A 1 151 ? -9.884   36.923 10.329  1.00 102.09 ?  151 LYS A CE  1 
ATOM 1220 N NZ  . LYS A 1 151 ? -10.603  36.767 11.622  1.00 102.75 ?  151 LYS A NZ  1 
ATOM 1221 N N   . SER A 1 152 ? -9.929   36.109 4.952   1.00 113.11 ?  152 SER A N   1 
ATOM 1222 C CA  . SER A 1 152 ? -10.807  35.698 3.866   1.00 110.43 ?  152 SER A CA  1 
ATOM 1223 C C   . SER A 1 152 ? -12.157  36.396 3.984   1.00 119.53 ?  152 SER A C   1 
ATOM 1224 O O   . SER A 1 152 ? -12.616  36.731 5.079   1.00 117.36 ?  152 SER A O   1 
ATOM 1225 C CB  . SER A 1 152 ? -10.995  34.180 3.877   1.00 114.89 ?  152 SER A CB  1 
ATOM 1226 O OG  . SER A 1 152 ? -11.884  33.769 2.851   1.00 124.90 ?  152 SER A OG  1 
ATOM 1227 N N   . PHE A 1 153 ? -12.791  36.626 2.830   1.00 115.83 ?  153 PHE A N   1 
ATOM 1228 C CA  . PHE A 1 153 ? -14.102  37.268 2.816   1.00 116.94 ?  153 PHE A CA  1 
ATOM 1229 C C   . PHE A 1 153 ? -15.111  36.479 3.639   1.00 120.47 ?  153 PHE A C   1 
ATOM 1230 O O   . PHE A 1 153 ? -15.922  37.061 4.369   1.00 107.58 ?  153 PHE A O   1 
ATOM 1231 C CB  . PHE A 1 153 ? -14.594  37.427 1.377   1.00 121.31 ?  153 PHE A CB  1 
ATOM 1232 C CG  . PHE A 1 153 ? -15.917  38.125 1.263   1.00 118.76 ?  153 PHE A CG  1 
ATOM 1233 C CD1 . PHE A 1 153 ? -16.979  37.521 0.611   1.00 114.81 ?  153 PHE A CD1 1 
ATOM 1234 C CD2 . PHE A 1 153 ? -16.101  39.384 1.809   1.00 105.21 ?  153 PHE A CD2 1 
ATOM 1235 C CE1 . PHE A 1 153 ? -18.199  38.160 0.504   1.00 114.14 ?  153 PHE A CE1 1 
ATOM 1236 C CE2 . PHE A 1 153 ? -17.317  40.028 1.706   1.00 100.70 ?  153 PHE A CE2 1 
ATOM 1237 C CZ  . PHE A 1 153 ? -18.368  39.414 1.053   1.00 113.22 ?  153 PHE A CZ  1 
ATOM 1238 N N   . ASP A 1 154 ? -15.072  35.149 3.537   1.00 119.75 ?  154 ASP A N   1 
ATOM 1239 C CA  . ASP A 1 154 ? -15.986  34.320 4.313   1.00 127.19 ?  154 ASP A CA  1 
ATOM 1240 C C   . ASP A 1 154 ? -15.671  34.394 5.802   1.00 115.51 ?  154 ASP A C   1 
ATOM 1241 O O   . ASP A 1 154 ? -16.581  34.513 6.630   1.00 115.49 ?  154 ASP A O   1 
ATOM 1242 C CB  . ASP A 1 154 ? -15.923  32.875 3.819   1.00 133.88 ?  154 ASP A CB  1 
ATOM 1243 C CG  . ASP A 1 154 ? -15.962  32.776 2.305   1.00 154.09 ?  154 ASP A CG  1 
ATOM 1244 O OD1 . ASP A 1 154 ? -14.993  33.226 1.657   1.00 142.90 ?  154 ASP A OD1 1 
ATOM 1245 O OD2 . ASP A 1 154 ? -16.958  32.254 1.763   1.00 195.15 -1 154 ASP A OD2 1 
ATOM 1246 N N   . ASP A 1 155 ? -14.385  34.337 6.161   1.00 105.92 ?  155 ASP A N   1 
ATOM 1247 C CA  . ASP A 1 155 ? -14.010  34.328 7.571   1.00 115.17 ?  155 ASP A CA  1 
ATOM 1248 C C   . ASP A 1 155 ? -14.283  35.668 8.242   1.00 103.57 ?  155 ASP A C   1 
ATOM 1249 O O   . ASP A 1 155 ? -14.602  35.706 9.435   1.00 100.77 ?  155 ASP A O   1 
ATOM 1250 C CB  . ASP A 1 155 ? -12.539  33.944 7.718   1.00 118.24 ?  155 ASP A CB  1 
ATOM 1251 C CG  . ASP A 1 155 ? -12.334  32.444 7.792   1.00 131.94 ?  155 ASP A CG  1 
ATOM 1252 O OD1 . ASP A 1 155 ? -13.042  31.785 8.583   1.00 136.26 ?  155 ASP A OD1 1 
ATOM 1253 O OD2 . ASP A 1 155 ? -11.471  31.921 7.055   1.00 130.22 -1 155 ASP A OD2 1 
ATOM 1254 N N   . GLN A 1 156 ? -14.164  36.774 7.503   1.00 102.27 ?  156 GLN A N   1 
ATOM 1255 C CA  . GLN A 1 156 ? -14.509  38.069 8.080   1.00 104.39 ?  156 GLN A CA  1 
ATOM 1256 C C   . GLN A 1 156 ? -16.015  38.228 8.225   1.00 113.10 ?  156 GLN A C   1 
ATOM 1257 O O   . GLN A 1 156 ? -16.480  38.881 9.167   1.00 106.25 ?  156 GLN A O   1 
ATOM 1258 C CB  . GLN A 1 156 ? -13.939  39.205 7.231   1.00 90.00  ?  156 GLN A CB  1 
ATOM 1259 C CG  . GLN A 1 156 ? -13.883  40.538 7.962   1.00 90.44  ?  156 GLN A CG  1 
ATOM 1260 C CD  . GLN A 1 156 ? -14.134  41.723 7.049   1.00 102.50 ?  156 GLN A CD  1 
ATOM 1261 O OE1 . GLN A 1 156 ? -14.850  41.614 6.054   1.00 123.31 ?  156 GLN A OE1 1 
ATOM 1262 N NE2 . GLN A 1 156 ? -13.547  42.865 7.387   1.00 82.09  ?  156 GLN A NE2 1 
ATOM 1263 N N   . LYS A 1 157 ? -16.789  37.649 7.304   1.00 113.58 ?  157 LYS A N   1 
ATOM 1264 C CA  . LYS A 1 157 ? -18.241  37.674 7.437   1.00 104.65 ?  157 LYS A CA  1 
ATOM 1265 C C   . LYS A 1 157 ? -18.688  36.898 8.669   1.00 108.42 ?  157 LYS A C   1 
ATOM 1266 O O   . LYS A 1 157 ? -19.553  37.359 9.422   1.00 109.67 ?  157 LYS A O   1 
ATOM 1267 C CB  . LYS A 1 157 ? -18.891  37.108 6.174   1.00 122.95 ?  157 LYS A CB  1 
ATOM 1268 C CG  . LYS A 1 157 ? -20.334  37.538 5.971   1.00 127.50 ?  157 LYS A CG  1 
ATOM 1269 C CD  . LYS A 1 157 ? -20.858  37.107 4.609   1.00 126.05 ?  157 LYS A CD  1 
ATOM 1270 C CE  . LYS A 1 157 ? -21.000  35.595 4.523   1.00 134.57 ?  157 LYS A CE  1 
ATOM 1271 N NZ  . LYS A 1 157 ? -21.530  35.160 3.200   1.00 136.75 ?  157 LYS A NZ  1 
ATOM 1272 N N   . LYS A 1 158 ? -18.104  35.718 8.893   1.00 110.27 ?  158 LYS A N   1 
ATOM 1273 C CA  . LYS A 1 158 ? -18.429  34.942 10.086  1.00 102.69 ?  158 LYS A CA  1 
ATOM 1274 C C   . LYS A 1 158 ? -17.939  35.640 11.348  1.00 98.65  ?  158 LYS A C   1 
ATOM 1275 O O   . LYS A 1 158 ? -18.647  35.671 12.361  1.00 109.57 ?  158 LYS A O   1 
ATOM 1276 C CB  . LYS A 1 158 ? -17.828  33.541 9.984   1.00 90.60  ?  158 LYS A CB  1 
ATOM 1277 C CG  . LYS A 1 158 ? -18.252  32.771 8.745   1.00 99.93  ?  158 LYS A CG  1 
ATOM 1278 C CD  . LYS A 1 158 ? -17.496  31.456 8.629   1.00 119.55 ?  158 LYS A CD  1 
ATOM 1279 C CE  . LYS A 1 158 ? -17.827  30.739 7.329   1.00 135.85 ?  158 LYS A CE  1 
ATOM 1280 N NZ  . LYS A 1 158 ? -17.058  29.472 7.182   1.00 131.02 ?  158 LYS A NZ  1 
ATOM 1281 N N   . GLU A 1 159 ? -16.724  36.197 11.310  1.00 97.65  ?  159 GLU A N   1 
ATOM 1282 C CA  . GLU A 1 159 ? -16.226  36.966 12.445  1.00 108.04 ?  159 GLU A CA  1 
ATOM 1283 C C   . GLU A 1 159 ? -17.135  38.147 12.755  1.00 103.90 ?  159 GLU A C   1 
ATOM 1284 O O   . GLU A 1 159 ? -17.294  38.522 13.922  1.00 110.27 ?  159 GLU A O   1 
ATOM 1285 C CB  . GLU A 1 159 ? -14.801  37.444 12.169  1.00 120.81 ?  159 GLU A CB  1 
ATOM 1286 C CG  . GLU A 1 159 ? -14.139  38.140 13.344  1.00 133.66 ?  159 GLU A CG  1 
ATOM 1287 C CD  . GLU A 1 159 ? -12.797  38.741 12.979  1.00 145.53 ?  159 GLU A CD  1 
ATOM 1288 O OE1 . GLU A 1 159 ? -12.709  39.982 12.870  1.00 145.24 ?  159 GLU A OE1 1 
ATOM 1289 O OE2 . GLU A 1 159 ? -11.831  37.972 12.798  1.00 149.09 -1 159 GLU A OE2 1 
ATOM 1290 N N   . THR A 1 160 ? -17.737  38.743 11.725  1.00 107.96 ?  160 THR A N   1 
ATOM 1291 C CA  . THR A 1 160 ? -18.732  39.783 11.947  1.00 99.06  ?  160 THR A CA  1 
ATOM 1292 C C   . THR A 1 160 ? -19.971  39.230 12.641  1.00 107.95 ?  160 THR A C   1 
ATOM 1293 O O   . THR A 1 160 ? -20.605  39.935 13.433  1.00 100.18 ?  160 THR A O   1 
ATOM 1294 C CB  . THR A 1 160 ? -19.110  40.431 10.614  1.00 95.43  ?  160 THR A CB  1 
ATOM 1295 O OG1 . THR A 1 160 ? -17.921  40.843 9.928   1.00 104.31 ?  160 THR A OG1 1 
ATOM 1296 C CG2 . THR A 1 160 ? -19.997  41.638 10.837  1.00 97.10  ?  160 THR A CG2 1 
ATOM 1297 N N   . ILE A 1 161 ? -20.319  37.971 12.369  1.00 115.27 ?  161 ILE A N   1 
ATOM 1298 C CA  . ILE A 1 161 ? -21.510  37.375 12.966  1.00 111.70 ?  161 ILE A CA  1 
ATOM 1299 C C   . ILE A 1 161 ? -21.271  37.054 14.436  1.00 119.27 ?  161 ILE A C   1 
ATOM 1300 O O   . ILE A 1 161 ? -22.074  37.411 15.304  1.00 121.87 ?  161 ILE A O   1 
ATOM 1301 C CB  . ILE A 1 161 ? -21.937  36.122 12.182  1.00 111.30 ?  161 ILE A CB  1 
ATOM 1302 C CG1 . ILE A 1 161 ? -22.292  36.492 10.743  1.00 98.88  ?  161 ILE A CG1 1 
ATOM 1303 C CG2 . ILE A 1 161 ? -23.111  35.441 12.868  1.00 124.70 ?  161 ILE A CG2 1 
ATOM 1304 C CD1 . ILE A 1 161 ? -22.404  35.300 9.823   1.00 109.17 ?  161 ILE A CD1 1 
ATOM 1305 N N   . GLN A 1 162 ? -20.168  36.361 14.737  1.00 115.38 ?  162 GLN A N   1 
ATOM 1306 C CA  . GLN A 1 162 ? -19.908  35.966 16.118  1.00 121.37 ?  162 GLN A CA  1 
ATOM 1307 C C   . GLN A 1 162 ? -19.756  37.179 17.026  1.00 114.63 ?  162 GLN A C   1 
ATOM 1308 O O   . GLN A 1 162 ? -20.037  37.095 18.227  1.00 135.48 ?  162 GLN A O   1 
ATOM 1309 C CB  . GLN A 1 162 ? -18.664  35.078 16.189  1.00 130.11 ?  162 GLN A CB  1 
ATOM 1310 C CG  . GLN A 1 162 ? -18.469  34.399 17.537  1.00 146.21 ?  162 GLN A CG  1 
ATOM 1311 C CD  . GLN A 1 162 ? -19.662  33.549 17.937  1.00 145.56 ?  162 GLN A CD  1 
ATOM 1312 O OE1 . GLN A 1 162 ? -20.194  33.684 19.038  1.00 149.61 ?  162 GLN A OE1 1 
ATOM 1313 N NE2 . GLN A 1 162 ? -20.086  32.665 17.040  1.00 141.31 ?  162 GLN A NE2 1 
ATOM 1314 N N   . ILE A 1 163 ? -19.325  38.314 16.474  1.00 93.83  ?  163 ILE A N   1 
ATOM 1315 C CA  . ILE A 1 163 ? -19.307  39.550 17.249  1.00 96.55  ?  163 ILE A CA  1 
ATOM 1316 C C   . ILE A 1 163 ? -20.719  40.109 17.389  1.00 120.39 ?  163 ILE A C   1 
ATOM 1317 O O   . ILE A 1 163 ? -21.085  40.648 18.441  1.00 125.24 ?  163 ILE A O   1 
ATOM 1318 C CB  . ILE A 1 163 ? -18.340  40.566 16.609  1.00 106.93 ?  163 ILE A CB  1 
ATOM 1319 C CG1 . ILE A 1 163 ? -16.967  40.501 17.286  1.00 123.74 ?  163 ILE A CG1 1 
ATOM 1320 C CG2 . ILE A 1 163 ? -18.900  41.981 16.673  1.00 106.36 ?  163 ILE A CG2 1 
ATOM 1321 C CD1 . ILE A 1 163 ? -16.240  39.184 17.101  1.00 136.96 ?  163 ILE A CD1 1 
ATOM 1322 N N   . ILE A 1 164 ? -21.541  39.971 16.345  1.00 123.28 ?  164 ILE A N   1 
ATOM 1323 C CA  . ILE A 1 164 ? -22.901  40.499 16.407  1.00 124.58 ?  164 ILE A CA  1 
ATOM 1324 C C   . ILE A 1 164 ? -23.741  39.696 17.395  1.00 121.28 ?  164 ILE A C   1 
ATOM 1325 O O   . ILE A 1 164 ? -24.701  40.221 17.973  1.00 121.35 ?  164 ILE A O   1 
ATOM 1326 C CB  . ILE A 1 164 ? -23.535  40.528 15.000  1.00 123.69 ?  164 ILE A CB  1 
ATOM 1327 C CG1 . ILE A 1 164 ? -24.382  41.789 14.820  1.00 136.41 ?  164 ILE A CG1 1 
ATOM 1328 C CG2 . ILE A 1 164 ? -24.419  39.315 14.760  1.00 117.15 ?  164 ILE A CG2 1 
ATOM 1329 C CD1 . ILE A 1 164 ? -23.566  43.045 14.625  1.00 119.88 ?  164 ILE A CD1 1 
ATOM 1330 N N   . LYS A 1 165 ? -23.399  38.423 17.613  1.00 116.75 ?  165 LYS A N   1 
ATOM 1331 C CA  . LYS A 1 165 ? -24.094  37.633 18.624  1.00 117.61 ?  165 LYS A CA  1 
ATOM 1332 C C   . LYS A 1 165 ? -23.596  37.965 20.024  1.00 118.71 ?  165 LYS A C   1 
ATOM 1333 O O   . LYS A 1 165 ? -24.381  37.989 20.978  1.00 117.55 ?  165 LYS A O   1 
ATOM 1334 C CB  . LYS A 1 165 ? -23.918  36.138 18.351  1.00 118.02 ?  165 LYS A CB  1 
ATOM 1335 C CG  . LYS A 1 165 ? -24.493  35.252 19.452  1.00 130.82 ?  165 LYS A CG  1 
ATOM 1336 C CD  . LYS A 1 165 ? -23.595  34.066 19.774  1.00 137.42 ?  165 LYS A CD  1 
ATOM 1337 C CE  . LYS A 1 165 ? -24.164  33.241 20.922  1.00 130.20 ?  165 LYS A CE  1 
ATOM 1338 N NZ  . LYS A 1 165 ? -23.297  32.078 21.262  1.00 119.90 ?  165 LYS A NZ  1 
ATOM 1339 N N   . ASN A 1 166 ? -22.296  38.239 20.161  1.00 118.65 ?  166 ASN A N   1 
ATOM 1340 C CA  . ASN A 1 166 ? -21.662  38.430 21.459  1.00 124.89 ?  166 ASN A CA  1 
ATOM 1341 C C   . ASN A 1 166 ? -21.739  39.868 21.949  1.00 135.38 ?  166 ASN A C   1 
ATOM 1342 O O   . ASN A 1 166 ? -20.891  40.296 22.743  1.00 144.93 ?  166 ASN A O   1 
ATOM 1343 C CB  . ASN A 1 166 ? -20.208  37.961 21.406  1.00 120.44 ?  166 ASN A CB  1 
ATOM 1344 C CG  . ASN A 1 166 ? -20.087  36.463 21.207  1.00 129.75 ?  166 ASN A CG  1 
ATOM 1345 O OD1 . ASN A 1 166 ? -21.057  35.792 20.855  1.00 114.78 ?  166 ASN A OD1 1 
ATOM 1346 N ND2 . ASN A 1 166 ? -18.891  35.930 21.431  1.00 145.44 ?  166 ASN A ND2 1 
ATOM 1347 N N   . HIS A 1 167 ? -22.727  40.634 21.489  1.00 106.22 ?  167 HIS A N   1 
ATOM 1348 C CA  . HIS A 1 167 ? -23.048  41.910 22.114  1.00 106.72 ?  167 HIS A CA  1 
ATOM 1349 C C   . HIS A 1 167 ? -24.252  41.800 23.042  1.00 129.99 ?  167 HIS A C   1 
ATOM 1350 O O   . HIS A 1 167 ? -24.181  42.237 24.194  1.00 151.01 ?  167 HIS A O   1 
ATOM 1351 C CB  . HIS A 1 167 ? -23.306  42.992 21.059  1.00 110.84 ?  167 HIS A CB  1 
ATOM 1352 C CG  . HIS A 1 167 ? -23.500  44.359 21.642  1.00 111.33 ?  167 HIS A CG  1 
ATOM 1353 N ND1 . HIS A 1 167 ? -24.731  44.832 22.041  1.00 118.62 ?  167 HIS A ND1 1 
ATOM 1354 C CD2 . HIS A 1 167 ? -22.615  45.352 21.900  1.00 113.92 ?  167 HIS A CD2 1 
ATOM 1355 C CE1 . HIS A 1 167 ? -24.598  46.056 22.519  1.00 118.18 ?  167 HIS A CE1 1 
ATOM 1356 N NE2 . HIS A 1 167 ? -23.324  46.396 22.444  1.00 114.22 ?  167 HIS A NE2 1 
ATOM 1357 N N   . PHE A 1 168 ? -25.361  41.218 22.571  1.00 119.59 ?  168 PHE A N   1 
ATOM 1358 C CA  . PHE A 1 168 ? -26.521  41.025 23.434  1.00 134.04 ?  168 PHE A CA  1 
ATOM 1359 C C   . PHE A 1 168 ? -27.136  39.638 23.263  1.00 128.91 ?  168 PHE A C   1 
ATOM 1360 O O   . PHE A 1 168 ? -28.354  39.474 23.395  1.00 122.50 ?  168 PHE A O   1 
ATOM 1361 C CB  . PHE A 1 168 ? -27.574  42.111 23.204  1.00 124.45 ?  168 PHE A CB  1 
ATOM 1362 C CG  . PHE A 1 168 ? -27.660  43.104 24.329  1.00 119.63 ?  168 PHE A CG  1 
ATOM 1363 C CD1 . PHE A 1 168 ? -28.714  43.063 25.226  1.00 103.04 ?  168 PHE A CD1 1 
ATOM 1364 C CD2 . PHE A 1 168 ? -26.678  44.069 24.500  1.00 125.02 ?  168 PHE A CD2 1 
ATOM 1365 C CE1 . PHE A 1 168 ? -28.790  43.963 26.267  1.00 115.61 ?  168 PHE A CE1 1 
ATOM 1366 C CE2 . PHE A 1 168 ? -26.752  44.976 25.543  1.00 125.71 ?  168 PHE A CE2 1 
ATOM 1367 C CZ  . PHE A 1 168 ? -27.811  44.920 26.426  1.00 128.54 ?  168 PHE A CZ  1 
ATOM 1368 N N   . GLN A 1 169 ? -26.306  38.634 22.965  1.00 126.95 ?  169 GLN A N   1 
ATOM 1369 C CA  . GLN A 1 169 ? -26.640  37.220 23.149  1.00 131.28 ?  169 GLN A CA  1 
ATOM 1370 C C   . GLN A 1 169 ? -27.896  36.821 22.365  1.00 126.13 ?  169 GLN A C   1 
ATOM 1371 O O   . GLN A 1 169 ? -28.936  36.471 22.924  1.00 130.73 ?  169 GLN A O   1 
ATOM 1372 C CB  . GLN A 1 169 ? -26.794  36.900 24.640  1.00 130.32 ?  169 GLN A CB  1 
ATOM 1373 C CG  . GLN A 1 169 ? -25.526  37.139 25.442  1.00 125.67 ?  169 GLN A CG  1 
ATOM 1374 C CD  . GLN A 1 169 ? -25.726  38.113 26.581  1.00 142.86 ?  169 GLN A CD  1 
ATOM 1375 O OE1 . GLN A 1 169 ? -26.845  38.314 27.051  1.00 148.93 ?  169 GLN A OE1 1 
ATOM 1376 N NE2 . GLN A 1 169 ? -24.640  38.731 27.027  1.00 134.45 ?  169 GLN A NE2 1 
ATOM 1377 N N   . CYS A 1 170 ? -27.766  36.887 21.047  1.00 117.36 ?  170 CYS A N   1 
ATOM 1378 C CA  . CYS A 1 170 ? -28.766  36.348 20.141  1.00 124.75 ?  170 CYS A CA  1 
ATOM 1379 C C   . CYS A 1 170 ? -28.357  34.935 19.716  1.00 136.82 ?  170 CYS A C   1 
ATOM 1380 O O   . CYS A 1 170 ? -27.435  34.334 20.277  1.00 136.96 ?  170 CYS A O   1 
ATOM 1381 C CB  . CYS A 1 170 ? -28.951  37.281 18.945  1.00 141.96 ?  170 CYS A CB  1 
ATOM 1382 S SG  . CYS A 1 170 ? -27.547  37.312 17.820  1.00 160.61 ?  170 CYS A SG  1 
ATOM 1383 N N   . GLU A 1 171 ? -29.051  34.385 18.723  1.00 160.82 ?  171 GLU A N   1 
ATOM 1384 C CA  . GLU A 1 171 ? -28.766  33.049 18.216  1.00 170.21 ?  171 GLU A CA  1 
ATOM 1385 C C   . GLU A 1 171 ? -28.098  33.139 16.850  1.00 161.03 ?  171 GLU A C   1 
ATOM 1386 O O   . GLU A 1 171 ? -28.431  34.010 16.040  1.00 147.87 ?  171 GLU A O   1 
ATOM 1387 C CB  . GLU A 1 171 ? -30.042  32.207 18.126  1.00 169.36 ?  171 GLU A CB  1 
ATOM 1388 C CG  . GLU A 1 171 ? -29.793  30.725 17.890  1.00 166.06 ?  171 GLU A CG  1 
ATOM 1389 C CD  . GLU A 1 171 ? -28.935  30.092 18.972  1.00 183.44 ?  171 GLU A CD  1 
ATOM 1390 O OE1 . GLU A 1 171 ? -29.034  30.512 20.146  1.00 190.53 ?  171 GLU A OE1 1 
ATOM 1391 O OE2 . GLU A 1 171 ? -28.155  29.172 18.647  1.00 193.99 -1 171 GLU A OE2 1 
ATOM 1392 N N   . ASP A 1 172 ? -27.154  32.227 16.599  1.00 169.44 ?  172 ASP A N   1 
ATOM 1393 C CA  . ASP A 1 172 ? -26.374  32.279 15.366  1.00 167.03 ?  172 ASP A CA  1 
ATOM 1394 C C   . ASP A 1 172 ? -27.204  31.870 14.154  1.00 152.21 ?  172 ASP A C   1 
ATOM 1395 O O   . ASP A 1 172 ? -27.068  32.461 13.076  1.00 152.76 ?  172 ASP A O   1 
ATOM 1396 C CB  . ASP A 1 172 ? -25.141  31.384 15.491  1.00 168.88 ?  172 ASP A CB  1 
ATOM 1397 C CG  . ASP A 1 172 ? -24.102  31.954 16.432  1.00 156.14 ?  172 ASP A CG  1 
ATOM 1398 O OD1 . ASP A 1 172 ? -24.256  33.122 16.846  1.00 148.23 ?  172 ASP A OD1 1 
ATOM 1399 O OD2 . ASP A 1 172 ? -23.132  31.237 16.756  1.00 156.44 -1 172 ASP A OD2 1 
ATOM 1400 N N   . TYR A 1 173 ? -28.067  30.864 14.307  1.00 149.72 ?  173 TYR A N   1 
ATOM 1401 C CA  . TYR A 1 173 ? -28.807  30.305 13.180  1.00 154.86 ?  173 TYR A CA  1 
ATOM 1402 C C   . TYR A 1 173 ? -29.829  31.276 12.600  1.00 158.92 ?  173 TYR A C   1 
ATOM 1403 O O   . TYR A 1 173 ? -30.498  30.934 11.617  1.00 147.43 ?  173 TYR A O   1 
ATOM 1404 C CB  . TYR A 1 173 ? -29.501  29.010 13.608  1.00 142.35 ?  173 TYR A CB  1 
ATOM 1405 C CG  . TYR A 1 173 ? -29.413  27.892 12.592  1.00 144.27 ?  173 TYR A CG  1 
ATOM 1406 C CD1 . TYR A 1 173 ? -30.372  27.752 11.597  1.00 138.93 ?  173 TYR A CD1 1 
ATOM 1407 C CD2 . TYR A 1 173 ? -28.372  26.974 12.632  1.00 136.78 ?  173 TYR A CD2 1 
ATOM 1408 C CE1 . TYR A 1 173 ? -30.294  26.728 10.670  1.00 133.04 ?  173 TYR A CE1 1 
ATOM 1409 C CE2 . TYR A 1 173 ? -28.286  25.948 11.711  1.00 120.92 ?  173 TYR A CE2 1 
ATOM 1410 C CZ  . TYR A 1 173 ? -29.250  25.830 10.732  1.00 122.22 ?  173 TYR A CZ  1 
ATOM 1411 O OH  . TYR A 1 173 ? -29.167  24.809 9.813   1.00 117.17 ?  173 TYR A OH  1 
ATOM 1412 N N   . GLU A 1 174 ? -29.960  32.473 13.175  1.00 156.24 ?  174 GLU A N   1 
ATOM 1413 C CA  . GLU A 1 174 ? -30.945  33.447 12.733  1.00 137.01 ?  174 GLU A CA  1 
ATOM 1414 C C   . GLU A 1 174 ? -30.394  34.861 12.616  1.00 131.80 ?  174 GLU A C   1 
ATOM 1415 O O   . GLU A 1 174 ? -31.028  35.696 11.958  1.00 130.17 ?  174 GLU A O   1 
ATOM 1416 C CB  . GLU A 1 174 ? -32.148  33.449 13.693  1.00 140.12 ?  174 GLU A CB  1 
ATOM 1417 C CG  . GLU A 1 174 ? -33.382  34.172 13.180  1.00 138.48 ?  174 GLU A CG  1 
ATOM 1418 C CD  . GLU A 1 174 ? -33.528  35.568 13.758  1.00 152.76 ?  174 GLU A CD  1 
ATOM 1419 O OE1 . GLU A 1 174 ? -34.679  36.037 13.878  1.00 160.94 ?  174 GLU A OE1 1 
ATOM 1420 O OE2 . GLU A 1 174 ? -32.500  36.194 14.097  1.00 142.67 -1 174 GLU A OE2 1 
ATOM 1421 N N   . ALA A 1 175 ? -29.228  35.150 13.201  1.00 144.16 ?  175 ALA A N   1 
ATOM 1422 C CA  . ALA A 1 175 ? -28.723  36.518 13.236  1.00 139.10 ?  175 ALA A CA  1 
ATOM 1423 C C   . ALA A 1 175 ? -28.083  36.943 11.922  1.00 142.01 ?  175 ALA A C   1 
ATOM 1424 O O   . ALA A 1 175 ? -28.111  38.133 11.585  1.00 131.36 ?  175 ALA A O   1 
ATOM 1425 C CB  . ALA A 1 175 ? -27.718  36.674 14.374  1.00 115.02 ?  175 ALA A CB  1 
ATOM 1426 N N   . GLU A 1 176 ? -27.510  36.004 11.168  1.00 142.05 ?  176 GLU A N   1 
ATOM 1427 C CA  . GLU A 1 176 ? -26.818  36.364 9.934   1.00 135.81 ?  176 GLU A CA  1 
ATOM 1428 C C   . GLU A 1 176 ? -27.761  36.841 8.836   1.00 148.79 ?  176 GLU A C   1 
ATOM 1429 O O   . GLU A 1 176 ? -27.283  37.203 7.754   1.00 169.11 ?  176 GLU A O   1 
ATOM 1430 C CB  . GLU A 1 176 ? -25.989  35.181 9.430   1.00 145.06 ?  176 GLU A CB  1 
ATOM 1431 C CG  . GLU A 1 176 ? -26.806  34.006 8.928   1.00 156.23 ?  176 GLU A CG  1 
ATOM 1432 C CD  . GLU A 1 176 ? -26.039  33.144 7.943   1.00 156.94 ?  176 GLU A CD  1 
ATOM 1433 O OE1 . GLU A 1 176 ? -25.119  33.669 7.280   1.00 157.72 ?  176 GLU A OE1 1 
ATOM 1434 O OE2 . GLU A 1 176 ? -26.356  31.941 7.833   1.00 164.13 -1 176 GLU A OE2 1 
ATOM 1435 N N   . HIS A 1 177 ? -29.071  36.852 9.077   1.00 144.39 ?  177 HIS A N   1 
ATOM 1436 C CA  . HIS A 1 177 ? -30.035  37.397 8.135   1.00 134.77 ?  177 HIS A CA  1 
ATOM 1437 C C   . HIS A 1 177 ? -30.786  38.598 8.691   1.00 126.12 ?  177 HIS A C   1 
ATOM 1438 O O   . HIS A 1 177 ? -31.571  39.213 7.959   1.00 134.28 ?  177 HIS A O   1 
ATOM 1439 C CB  . HIS A 1 177 ? -31.043  36.318 7.713   1.00 129.69 ?  177 HIS A CB  1 
ATOM 1440 C CG  . HIS A 1 177 ? -30.413  35.104 7.104   1.00 138.77 ?  177 HIS A CG  1 
ATOM 1441 N ND1 . HIS A 1 177 ? -30.030  34.011 7.851   1.00 148.84 ?  177 HIS A ND1 1 
ATOM 1442 C CD2 . HIS A 1 177 ? -30.104  34.808 5.819   1.00 142.42 ?  177 HIS A CD2 1 
ATOM 1443 C CE1 . HIS A 1 177 ? -29.510  33.095 7.054   1.00 147.33 ?  177 HIS A CE1 1 
ATOM 1444 N NE2 . HIS A 1 177 ? -29.543  33.554 5.815   1.00 146.69 ?  177 HIS A NE2 1 
ATOM 1445 N N   . TYR A 1 178 ? -30.572  38.948 9.960   1.00 112.01 ?  178 TYR A N   1 
ATOM 1446 C CA  . TYR A 1 178 ? -31.301  40.035 10.606  1.00 103.59 ?  178 TYR A CA  1 
ATOM 1447 C C   . TYR A 1 178 ? -30.390  41.190 11.002  1.00 103.01 ?  178 TYR A C   1 
ATOM 1448 O O   . TYR A 1 178 ? -30.620  42.323 10.568  1.00 95.54  ?  178 TYR A O   1 
ATOM 1449 C CB  . TYR A 1 178 ? -32.049  39.485 11.830  1.00 109.74 ?  178 TYR A CB  1 
ATOM 1450 C CG  . TYR A 1 178 ? -32.662  40.536 12.730  1.00 107.97 ?  178 TYR A CG  1 
ATOM 1451 C CD1 . TYR A 1 178 ? -32.651  40.382 14.111  1.00 104.84 ?  178 TYR A CD1 1 
ATOM 1452 C CD2 . TYR A 1 178 ? -33.267  41.671 12.204  1.00 101.38 ?  178 TYR A CD2 1 
ATOM 1453 C CE1 . TYR A 1 178 ? -33.212  41.333 14.940  1.00 109.06 ?  178 TYR A CE1 1 
ATOM 1454 C CE2 . TYR A 1 178 ? -33.827  42.628 13.025  1.00 99.03  ?  178 TYR A CE2 1 
ATOM 1455 C CZ  . TYR A 1 178 ? -33.798  42.453 14.391  1.00 107.86 ?  178 TYR A CZ  1 
ATOM 1456 O OH  . TYR A 1 178 ? -34.357  43.402 15.214  1.00 106.47 ?  178 TYR A OH  1 
ATOM 1457 N N   . LEU A 1 179 ? -29.354  40.940 11.807  1.00 118.35 ?  179 LEU A N   1 
ATOM 1458 C CA  . LEU A 1 179 ? -28.574  42.031 12.385  1.00 122.26 ?  179 LEU A CA  1 
ATOM 1459 C C   . LEU A 1 179 ? -27.494  42.527 11.433  1.00 121.49 ?  179 LEU A C   1 
ATOM 1460 O O   . LEU A 1 179 ? -27.267  43.737 11.327  1.00 101.81 ?  179 LEU A O   1 
ATOM 1461 C CB  . LEU A 1 179 ? -27.949  41.578 13.704  1.00 120.13 ?  179 LEU A CB  1 
ATOM 1462 C CG  . LEU A 1 179 ? -28.946  41.228 14.812  1.00 102.67 ?  179 LEU A CG  1 
ATOM 1463 C CD1 . LEU A 1 179 ? -28.338  40.224 15.778  1.00 110.30 ?  179 LEU A CD1 1 
ATOM 1464 C CD2 . LEU A 1 179 ? -29.404  42.482 15.543  1.00 95.68  ?  179 LEU A CD2 1 
ATOM 1465 N N   . TYR A 1 180 ? -26.806  41.603 10.756  1.00 126.52 ?  180 TYR A N   1 
ATOM 1466 C CA  . TYR A 1 180 ? -25.800  41.979 9.767   1.00 110.90 ?  180 TYR A CA  1 
ATOM 1467 C C   . TYR A 1 180 ? -26.381  42.916 8.713   1.00 105.63 ?  180 TYR A C   1 
ATOM 1468 O O   . TYR A 1 180 ? -25.734  43.889 8.309   1.00 112.47 ?  180 TYR A O   1 
ATOM 1469 C CB  . TYR A 1 180 ? -25.234  40.715 9.115   1.00 114.89 ?  180 TYR A CB  1 
ATOM 1470 C CG  . TYR A 1 180 ? -24.084  40.922 8.147   1.00 128.09 ?  180 TYR A CG  1 
ATOM 1471 C CD1 . TYR A 1 180 ? -23.764  39.941 7.217   1.00 139.14 ?  180 TYR A CD1 1 
ATOM 1472 C CD2 . TYR A 1 180 ? -23.306  42.074 8.175   1.00 125.54 ?  180 TYR A CD2 1 
ATOM 1473 C CE1 . TYR A 1 180 ? -22.721  40.105 6.330   1.00 138.67 ?  180 TYR A CE1 1 
ATOM 1474 C CE2 . TYR A 1 180 ? -22.255  42.248 7.286   1.00 127.04 ?  180 TYR A CE2 1 
ATOM 1475 C CZ  . TYR A 1 180 ? -21.968  41.257 6.368   1.00 132.74 ?  180 TYR A CZ  1 
ATOM 1476 O OH  . TYR A 1 180 ? -20.929  41.409 5.479   1.00 128.82 ?  180 TYR A OH  1 
ATOM 1477 N N   . SER A 1 181 ? -27.610  42.647 8.268   1.00 100.44 ?  181 SER A N   1 
ATOM 1478 C CA  . SER A 1 181 ? -28.202  43.433 7.191   1.00 100.53 ?  181 SER A CA  1 
ATOM 1479 C C   . SER A 1 181 ? -28.499  44.860 7.640   1.00 99.59  ?  181 SER A C   1 
ATOM 1480 O O   . SER A 1 181 ? -28.085  45.825 6.987   1.00 114.94 ?  181 SER A O   1 
ATOM 1481 C CB  . SER A 1 181 ? -29.473  42.750 6.684   1.00 97.29  ?  181 SER A CB  1 
ATOM 1482 O OG  . SER A 1 181 ? -30.102  43.525 5.678   1.00 94.54  ?  181 SER A OG  1 
ATOM 1483 N N   . ASN A 1 182 ? -29.222  45.015 8.754   1.00 86.20  ?  182 ASN A N   1 
ATOM 1484 C CA  . ASN A 1 182 ? -29.610  46.350 9.202   1.00 107.77 ?  182 ASN A CA  1 
ATOM 1485 C C   . ASN A 1 182 ? -28.405  47.186 9.617   1.00 96.11  ?  182 ASN A C   1 
ATOM 1486 O O   . ASN A 1 182 ? -28.448  48.418 9.527   1.00 97.40  ?  182 ASN A O   1 
ATOM 1487 C CB  . ASN A 1 182 ? -30.611  46.247 10.352  1.00 117.35 ?  182 ASN A CB  1 
ATOM 1488 C CG  . ASN A 1 182 ? -31.868  45.491 9.963   1.00 108.63 ?  182 ASN A CG  1 
ATOM 1489 O OD1 . ASN A 1 182 ? -32.833  46.079 9.474   1.00 119.95 ?  182 ASN A OD1 1 
ATOM 1490 N ND2 . ASN A 1 182 ? -31.862  44.183 10.179  1.00 109.77 ?  182 ASN A ND2 1 
ATOM 1491 N N   . ALA A 1 183 ? -27.329  46.543 10.072  1.00 105.48 ?  183 ALA A N   1 
ATOM 1492 C CA  . ALA A 1 183 ? -26.100  47.268 10.368  1.00 106.18 ?  183 ALA A CA  1 
ATOM 1493 C C   . ALA A 1 183 ? -25.364  47.668 9.097   1.00 108.10 ?  183 ALA A C   1 
ATOM 1494 O O   . ALA A 1 183 ? -24.684  48.701 9.077   1.00 114.67 ?  183 ALA A O   1 
ATOM 1495 C CB  . ALA A 1 183 ? -25.189  46.420 11.260  1.00 96.29  ?  183 ALA A CB  1 
ATOM 1496 N N   . PHE A 1 184 ? -25.486  46.865 8.038   1.00 107.05 ?  184 PHE A N   1 
ATOM 1497 C CA  . PHE A 1 184 ? -24.815  47.165 6.778   1.00 91.84  ?  184 PHE A CA  1 
ATOM 1498 C C   . PHE A 1 184 ? -25.323  48.474 6.182   1.00 102.12 ?  184 PHE A C   1 
ATOM 1499 O O   . PHE A 1 184 ? -24.553  49.418 5.973   1.00 106.02 ?  184 PHE A O   1 
ATOM 1500 C CB  . PHE A 1 184 ? -25.019  46.000 5.804   1.00 65.10  ?  184 PHE A CB  1 
ATOM 1501 C CG  . PHE A 1 184 ? -24.011  45.943 4.686   1.00 87.91  ?  184 PHE A CG  1 
ATOM 1502 C CD1 . PHE A 1 184 ? -23.318  44.773 4.429   1.00 98.97  ?  184 PHE A CD1 1 
ATOM 1503 C CD2 . PHE A 1 184 ? -23.780  47.042 3.872   1.00 98.25  ?  184 PHE A CD2 1 
ATOM 1504 C CE1 . PHE A 1 184 ? -22.400  44.709 3.400   1.00 93.11  ?  184 PHE A CE1 1 
ATOM 1505 C CE2 . PHE A 1 184 ? -22.864  46.983 2.843   1.00 97.11  ?  184 PHE A CE2 1 
ATOM 1506 C CZ  . PHE A 1 184 ? -22.175  45.815 2.605   1.00 95.61  ?  184 PHE A CZ  1 
ATOM 1507 N N   . ARG A 1 185 ? -26.624  48.540 5.888   1.00 99.17  ?  185 ARG A N   1 
ATOM 1508 C CA  . ARG A 1 185 ? -27.188  49.732 5.262   1.00 106.32 ?  185 ARG A CA  1 
ATOM 1509 C C   . ARG A 1 185 ? -27.044  50.953 6.162   1.00 114.43 ?  185 ARG A C   1 
ATOM 1510 O O   . ARG A 1 185 ? -26.822  52.065 5.668   1.00 118.12 ?  185 ARG A O   1 
ATOM 1511 C CB  . ARG A 1 185 ? -28.658  49.483 4.906   1.00 125.18 ?  185 ARG A CB  1 
ATOM 1512 C CG  . ARG A 1 185 ? -29.482  50.729 4.608   1.00 144.06 ?  185 ARG A CG  1 
ATOM 1513 C CD  . ARG A 1 185 ? -28.937  51.501 3.415   1.00 154.40 ?  185 ARG A CD  1 
ATOM 1514 N NE  . ARG A 1 185 ? -29.629  51.172 2.172   1.00 154.01 ?  185 ARG A NE  1 
ATOM 1515 C CZ  . ARG A 1 185 ? -29.421  51.796 1.017   1.00 149.66 ?  185 ARG A CZ  1 
ATOM 1516 N NH1 . ARG A 1 185 ? -28.538  52.783 0.943   1.00 142.07 ?  185 ARG A NH1 1 
ATOM 1517 N NH2 . ARG A 1 185 ? -30.096  51.435 -0.065  1.00 141.27 ?  185 ARG A NH2 1 
ATOM 1518 N N   . LYS A 1 186 ? -27.149  50.767 7.480   1.00 115.09 ?  186 LYS A N   1 
ATOM 1519 C CA  . LYS A 1 186 ? -27.006  51.890 8.401   1.00 120.89 ?  186 LYS A CA  1 
ATOM 1520 C C   . LYS A 1 186 ? -25.611  52.495 8.309   1.00 108.94 ?  186 LYS A C   1 
ATOM 1521 O O   . LYS A 1 186 ? -25.457  53.719 8.228   1.00 109.25 ?  186 LYS A O   1 
ATOM 1522 C CB  . LYS A 1 186 ? -27.307  51.434 9.830   1.00 121.55 ?  186 LYS A CB  1 
ATOM 1523 C CG  . LYS A 1 186 ? -27.428  52.571 10.833  1.00 135.37 ?  186 LYS A CG  1 
ATOM 1524 C CD  . LYS A 1 186 ? -28.506  53.564 10.414  1.00 146.12 ?  186 LYS A CD  1 
ATOM 1525 C CE  . LYS A 1 186 ? -28.886  54.496 11.556  1.00 137.02 ?  186 LYS A CE  1 
ATOM 1526 N NZ  . LYS A 1 186 ? -27.724  55.269 12.067  1.00 133.63 ?  186 LYS A NZ  1 
ATOM 1527 N N   . THR A 1 187 ? -24.579  51.648 8.319   1.00 109.73 ?  187 THR A N   1 
ATOM 1528 C CA  . THR A 1 187 ? -23.211  52.139 8.194   1.00 109.33 ?  187 THR A CA  1 
ATOM 1529 C C   . THR A 1 187 ? -22.984  52.804 6.842   1.00 111.78 ?  187 THR A C   1 
ATOM 1530 O O   . THR A 1 187 ? -22.324  53.846 6.757   1.00 114.41 ?  187 THR A O   1 
ATOM 1531 C CB  . THR A 1 187 ? -22.222  50.990 8.395   1.00 98.18  ?  187 THR A CB  1 
ATOM 1532 O OG1 . THR A 1 187 ? -22.538  50.295 9.606   1.00 110.70 ?  187 THR A OG1 1 
ATOM 1533 C CG2 . THR A 1 187 ? -20.799  51.519 8.475   1.00 94.74  ?  187 THR A CG2 1 
ATOM 1534 N N   . TYR A 1 188 ? -23.522  52.209 5.776   1.00 113.36 ?  188 TYR A N   1 
ATOM 1535 C CA  . TYR A 1 188 ? -23.361  52.769 4.438   1.00 100.09 ?  188 TYR A CA  1 
ATOM 1536 C C   . TYR A 1 188 ? -23.952  54.171 4.348   1.00 111.85 ?  188 TYR A C   1 
ATOM 1537 O O   . TYR A 1 188 ? -23.299  55.102 3.864   1.00 115.53 ?  188 TYR A O   1 
ATOM 1538 C CB  . TYR A 1 188 ? -24.004  51.834 3.413   1.00 101.15 ?  188 TYR A CB  1 
ATOM 1539 C CG  . TYR A 1 188 ? -23.722  52.201 1.976   1.00 108.45 ?  188 TYR A CG  1 
ATOM 1540 C CD1 . TYR A 1 188 ? -22.685  51.600 1.277   1.00 95.53  ?  188 TYR A CD1 1 
ATOM 1541 C CD2 . TYR A 1 188 ? -24.508  53.133 1.312   1.00 115.71 ?  188 TYR A CD2 1 
ATOM 1542 C CE1 . TYR A 1 188 ? -22.429  51.929 -0.036  1.00 87.88  ?  188 TYR A CE1 1 
ATOM 1543 C CE2 . TYR A 1 188 ? -24.261  53.466 0.001   1.00 109.81 ?  188 TYR A CE2 1 
ATOM 1544 C CZ  . TYR A 1 188 ? -23.222  52.863 -0.667  1.00 95.07  ?  188 TYR A CZ  1 
ATOM 1545 O OH  . TYR A 1 188 ? -22.977  53.195 -1.973  1.00 105.64 ?  188 TYR A OH  1 
ATOM 1546 N N   . ASP A 1 189 ? -25.196  54.338 4.804   1.00 112.78 ?  189 ASP A N   1 
ATOM 1547 C CA  . ASP A 1 189 ? -25.836  55.649 4.739   1.00 128.80 ?  189 ASP A CA  1 
ATOM 1548 C C   . ASP A 1 189 ? -25.114  56.671 5.609   1.00 132.80 ?  189 ASP A C   1 
ATOM 1549 O O   . ASP A 1 189 ? -25.079  57.859 5.268   1.00 139.85 ?  189 ASP A O   1 
ATOM 1550 C CB  . ASP A 1 189 ? -27.304  55.537 5.150   1.00 133.84 ?  189 ASP A CB  1 
ATOM 1551 C CG  . ASP A 1 189 ? -28.167  54.927 4.062   1.00 147.00 ?  189 ASP A CG  1 
ATOM 1552 O OD1 . ASP A 1 189 ? -27.750  54.955 2.885   1.00 157.22 ?  189 ASP A OD1 1 
ATOM 1553 O OD2 . ASP A 1 189 ? -29.262  54.418 4.384   1.00 164.14 -1 189 ASP A OD2 1 
ATOM 1554 N N   . ILE A 1 190 ? -24.537  56.234 6.730   1.00 124.94 ?  190 ILE A N   1 
ATOM 1555 C CA  . ILE A 1 190 ? -23.743  57.137 7.557   1.00 122.78 ?  190 ILE A CA  1 
ATOM 1556 C C   . ILE A 1 190 ? -22.449  57.507 6.847   1.00 122.06 ?  190 ILE A C   1 
ATOM 1557 O O   . ILE A 1 190 ? -22.003  58.660 6.895   1.00 130.74 ?  190 ILE A O   1 
ATOM 1558 C CB  . ILE A 1 190 ? -23.469  56.501 8.931   1.00 114.11 ?  190 ILE A CB  1 
ATOM 1559 C CG1 . ILE A 1 190 ? -24.761  56.393 9.739   1.00 133.29 ?  190 ILE A CG1 1 
ATOM 1560 C CG2 . ILE A 1 190 ? -22.422  57.298 9.697   1.00 114.66 ?  190 ILE A CG2 1 
ATOM 1561 C CD1 . ILE A 1 190 ? -24.621  55.541 10.977  1.00 128.40 ?  190 ILE A CD1 1 
ATOM 1562 N N   . SER A 1 191 ? -21.827  56.537 6.175   1.00 118.07 ?  191 SER A N   1 
ATOM 1563 C CA  . SER A 1 191 ? -20.554  56.783 5.508   1.00 127.21 ?  191 SER A CA  1 
ATOM 1564 C C   . SER A 1 191 ? -20.703  57.823 4.402   1.00 136.90 ?  191 SER A C   1 
ATOM 1565 O O   . SER A 1 191 ? -20.048  58.871 4.425   1.00 147.26 ?  191 SER A O   1 
ATOM 1566 C CB  . SER A 1 191 ? -19.998  55.470 4.953   1.00 108.33 ?  191 SER A CB  1 
ATOM 1567 O OG  . SER A 1 191 ? -19.661  54.579 6.003   1.00 114.00 ?  191 SER A OG  1 
ATOM 1568 N N   . CYS A 1 192 ? -21.576  57.550 3.427   1.00 127.32 ?  192 CYS A N   1 
ATOM 1569 C CA  . CYS A 1 192 ? -21.700  58.430 2.266   1.00 123.58 ?  192 CYS A CA  1 
ATOM 1570 C C   . CYS A 1 192 ? -22.045  59.858 2.674   1.00 147.06 ?  192 CYS A C   1 
ATOM 1571 O O   . CYS A 1 192 ? -21.580  60.819 2.050   1.00 152.49 ?  192 CYS A O   1 
ATOM 1572 C CB  . CYS A 1 192 ? -22.751  57.878 1.303   1.00 124.12 ?  192 CYS A CB  1 
ATOM 1573 S SG  . CYS A 1 192 ? -22.340  56.259 0.616   1.00 117.10 ?  192 CYS A SG  1 
ATOM 1574 N N   . ASN A 1 193 ? -22.856  60.020 3.716   1.00 153.69 ?  193 ASN A N   1 
ATOM 1575 C CA  . ASN A 1 193 ? -23.192  61.351 4.205   1.00 161.63 ?  193 ASN A CA  1 
ATOM 1576 C C   . ASN A 1 193 ? -21.994  61.956 4.926   1.00 156.19 ?  193 ASN A C   1 
ATOM 1577 O O   . ASN A 1 193 ? -21.470  61.369 5.880   1.00 154.06 ?  193 ASN A O   1 
ATOM 1578 C CB  . ASN A 1 193 ? -24.407  61.285 5.126   1.00 163.16 ?  193 ASN A CB  1 
ATOM 1579 C CG  . ASN A 1 193 ? -25.649  60.789 4.414   1.00 166.95 ?  193 ASN A CG  1 
ATOM 1580 O OD1 . ASN A 1 193 ? -25.826  61.019 3.217   1.00 165.13 ?  193 ASN A OD1 1 
ATOM 1581 N ND2 . ASN A 1 193 ? -26.516  60.100 5.146   1.00 167.52 ?  193 ASN A ND2 1 
ATOM 1582 N N   . LYS A 1 194 ? -21.562  63.129 4.470   1.00 155.30 ?  194 LYS A N   1 
ATOM 1583 C CA  . LYS A 1 194 ? -20.396  63.826 5.010   1.00 153.09 ?  194 LYS A CA  1 
ATOM 1584 C C   . LYS A 1 194 ? -20.796  64.924 5.986   1.00 164.70 ?  194 LYS A C   1 
ATOM 1585 O O   . LYS A 1 194 ? -20.170  65.988 6.036   1.00 165.62 ?  194 LYS A O   1 
ATOM 1586 C CB  . LYS A 1 194 ? -19.552  64.396 3.874   1.00 144.69 ?  194 LYS A CB  1 
ATOM 1587 C CG  . LYS A 1 194 ? -20.334  65.277 2.917   1.00 142.24 ?  194 LYS A CG  1 
ATOM 1588 C CD  . LYS A 1 194 ? -19.735  65.256 1.524   1.00 129.23 ?  194 LYS A CD  1 
ATOM 1589 C CE  . LYS A 1 194 ? -20.752  65.712 0.492   1.00 124.16 ?  194 LYS A CE  1 
ATOM 1590 N NZ  . LYS A 1 194 ? -22.013  64.923 0.577   1.00 126.10 ?  194 LYS A NZ  1 
ATOM 1591 N N   . LYS A 1 195 ? -21.835  64.681 6.783   1.00 182.57 ?  195 LYS A N   1 
ATOM 1592 C CA  . LYS A 1 195 ? -22.400  65.673 7.689   1.00 188.32 ?  195 LYS A CA  1 
ATOM 1593 C C   . LYS A 1 195 ? -21.614  65.807 8.986   1.00 191.86 ?  195 LYS A C   1 
ATOM 1594 O O   . LYS A 1 195 ? -22.173  66.293 9.978   1.00 193.63 ?  195 LYS A O   1 
ATOM 1595 C CB  . LYS A 1 195 ? -23.858  65.322 8.006   1.00 183.98 ?  195 LYS A CB  1 
ATOM 1596 C CG  . LYS A 1 195 ? -24.606  64.639 6.869   1.00 167.29 ?  195 LYS A CG  1 
ATOM 1597 C CD  . LYS A 1 195 ? -25.653  65.550 6.244   1.00 157.08 ?  195 LYS A CD  1 
ATOM 1598 C CE  . LYS A 1 195 ? -25.024  66.554 5.293   1.00 163.87 ?  195 LYS A CE  1 
ATOM 1599 N NZ  . LYS A 1 195 ? -26.050  67.244 4.464   1.00 155.87 ?  195 LYS A NZ  1 
ATOM 1600 N N   . ASP A 1 196 ? -20.347  65.384 8.998   1.00 188.73 ?  196 ASP A N   1 
ATOM 1601 C CA  . ASP A 1 196 ? -19.554  65.285 10.225  1.00 185.28 ?  196 ASP A CA  1 
ATOM 1602 C C   . ASP A 1 196 ? -20.244  64.356 11.220  1.00 179.67 ?  196 ASP A C   1 
ATOM 1603 O O   . ASP A 1 196 ? -20.247  64.592 12.430  1.00 171.66 ?  196 ASP A O   1 
ATOM 1604 C CB  . ASP A 1 196 ? -19.289  66.662 10.843  1.00 183.76 ?  196 ASP A CB  1 
ATOM 1605 C CG  . ASP A 1 196 ? -18.024  66.696 11.689  1.00 180.03 ?  196 ASP A CG  1 
ATOM 1606 O OD1 . ASP A 1 196 ? -17.810  65.773 12.503  1.00 173.32 ?  196 ASP A OD1 1 
ATOM 1607 O OD2 . ASP A 1 196 ? -17.241  67.658 11.540  1.00 178.30 -1 196 ASP A OD2 1 
ATOM 1608 N N   . ARG A 1 197 ? -20.851  63.294 10.695  1.00 173.44 ?  197 ARG A N   1 
ATOM 1609 C CA  . ARG A 1 197 ? -21.590  62.332 11.508  1.00 175.10 ?  197 ARG A CA  1 
ATOM 1610 C C   . ARG A 1 197 ? -20.637  61.225 11.934  1.00 162.61 ?  197 ARG A C   1 
ATOM 1611 O O   . ARG A 1 197 ? -20.324  60.321 11.155  1.00 148.87 ?  197 ARG A O   1 
ATOM 1612 C CB  . ARG A 1 197 ? -22.782  61.774 10.738  1.00 169.74 ?  197 ARG A CB  1 
ATOM 1613 C CG  . ARG A 1 197 ? -24.123  62.307 11.212  1.00 165.13 ?  197 ARG A CG  1 
ATOM 1614 C CD  . ARG A 1 197 ? -25.279  61.591 10.531  1.00 158.25 ?  197 ARG A CD  1 
ATOM 1615 N NE  . ARG A 1 197 ? -26.553  61.874 11.186  1.00 155.65 ?  197 ARG A NE  1 
ATOM 1616 C CZ  . ARG A 1 197 ? -27.723  61.382 10.792  1.00 149.89 ?  197 ARG A CZ  1 
ATOM 1617 N NH1 . ARG A 1 197 ? -27.788  60.579 9.739   1.00 139.62 ?  197 ARG A NH1 1 
ATOM 1618 N NH2 . ARG A 1 197 ? -28.831  61.695 11.451  1.00 136.12 ?  197 ARG A NH2 1 
ATOM 1619 N N   . ARG A 1 198 ? -20.171  61.300 13.174  1.00 152.17 ?  198 ARG A N   1 
ATOM 1620 C CA  . ARG A 1 198 ? -19.408  60.226 13.789  1.00 140.60 ?  198 ARG A CA  1 
ATOM 1621 C C   . ARG A 1 198 ? -20.334  59.417 14.687  1.00 141.45 ?  198 ARG A C   1 
ATOM 1622 O O   . ARG A 1 198 ? -21.234  59.968 15.327  1.00 158.60 ?  198 ARG A O   1 
ATOM 1623 C CB  . ARG A 1 198 ? -18.222  60.778 14.583  1.00 152.74 ?  198 ARG A CB  1 
ATOM 1624 C CG  . ARG A 1 198 ? -18.599  61.672 15.751  1.00 151.63 ?  198 ARG A CG  1 
ATOM 1625 C CD  . ARG A 1 198 ? -17.357  62.204 16.443  1.00 151.25 ?  198 ARG A CD  1 
ATOM 1626 N NE  . ARG A 1 198 ? -16.697  63.235 15.648  1.00 156.80 ?  198 ARG A NE  1 
ATOM 1627 C CZ  . ARG A 1 198 ? -15.625  63.912 16.046  1.00 166.98 ?  198 ARG A CZ  1 
ATOM 1628 N NH1 . ARG A 1 198 ? -15.090  64.834 15.256  1.00 169.87 ?  198 ARG A NH1 1 
ATOM 1629 N NH2 . ARG A 1 198 ? -15.087  63.668 17.233  1.00 164.54 ?  198 ARG A NH2 1 
ATOM 1630 N N   . ILE A 1 199 ? -20.119  58.116 14.718  1.00 140.55 ?  199 ILE A N   1 
ATOM 1631 C CA  . ILE A 1 199 ? -21.052  57.191 15.349  1.00 154.29 ?  199 ILE A CA  1 
ATOM 1632 C C   . ILE A 1 199 ? -20.720  57.056 16.829  1.00 159.84 ?  199 ILE A C   1 
ATOM 1633 O O   . ILE A 1 199 ? -19.584  57.273 17.262  1.00 157.74 ?  199 ILE A O   1 
ATOM 1634 C CB  . ILE A 1 199 ? -21.028  55.825 14.628  1.00 150.91 ?  199 ILE A CB  1 
ATOM 1635 C CG1 . ILE A 1 199 ? -22.141  54.910 15.144  1.00 149.60 ?  199 ILE A CG1 1 
ATOM 1636 C CG2 . ILE A 1 199 ? -19.667  55.163 14.775  1.00 143.96 ?  199 ILE A CG2 1 
ATOM 1637 C CD1 . ILE A 1 199 ? -22.088  53.517 14.576  1.00 145.05 ?  199 ILE A CD1 1 
ATOM 1638 N N   . LYS A 1 200 ? -21.739  56.724 17.617  1.00 162.94 ?  200 LYS A N   1 
ATOM 1639 C CA  . LYS A 1 200 ? -21.590  56.345 19.014  1.00 149.94 ?  200 LYS A CA  1 
ATOM 1640 C C   . LYS A 1 200 ? -22.084  54.913 19.163  1.00 134.58 ?  200 LYS A C   1 
ATOM 1641 O O   . LYS A 1 200 ? -23.173  54.581 18.684  1.00 135.48 ?  200 LYS A O   1 
ATOM 1642 C CB  . LYS A 1 200 ? -22.374  57.288 19.931  1.00 144.63 ?  200 LYS A CB  1 
ATOM 1643 C CG  . LYS A 1 200 ? -22.668  58.645 19.307  1.00 148.87 ?  200 LYS A CG  1 
ATOM 1644 C CD  . LYS A 1 200 ? -23.778  59.375 20.045  1.00 141.28 ?  200 LYS A CD  1 
ATOM 1645 C CE  . LYS A 1 200 ? -24.307  60.540 19.224  1.00 152.34 ?  200 LYS A CE  1 
ATOM 1646 N NZ  . LYS A 1 200 ? -25.563  61.104 19.793  1.00 147.42 ?  200 LYS A NZ  1 
ATOM 1647 N N   . LYS A 1 201 ? -21.277  54.066 19.812  1.00 120.58 ?  201 LYS A N   1 
ATOM 1648 C CA  . LYS A 1 201 ? -21.593  52.640 19.871  1.00 117.30 ?  201 LYS A CA  1 
ATOM 1649 C C   . LYS A 1 201 ? -22.961  52.382 20.489  1.00 139.25 ?  201 LYS A C   1 
ATOM 1650 O O   . LYS A 1 201 ? -23.650  51.433 20.096  1.00 141.10 ?  201 LYS A O   1 
ATOM 1651 C CB  . LYS A 1 201 ? -20.514  51.888 20.653  1.00 105.12 ?  201 LYS A CB  1 
ATOM 1652 C CG  . LYS A 1 201 ? -20.784  50.393 20.766  1.00 109.02 ?  201 LYS A CG  1 
ATOM 1653 C CD  . LYS A 1 201 ? -19.694  49.668 21.531  1.00 117.45 ?  201 LYS A CD  1 
ATOM 1654 C CE  . LYS A 1 201 ? -19.941  48.166 21.534  1.00 111.03 ?  201 LYS A CE  1 
ATOM 1655 N NZ  . LYS A 1 201 ? -18.825  47.414 22.170  1.00 110.90 ?  201 LYS A NZ  1 
ATOM 1656 N N   . SER A 1 202 ? -23.374  53.213 21.447  1.00 138.59 ?  202 SER A N   1 
ATOM 1657 C CA  . SER A 1 202 ? -24.671  53.021 22.086  1.00 130.96 ?  202 SER A CA  1 
ATOM 1658 C C   . SER A 1 202 ? -25.808  53.177 21.082  1.00 139.38 ?  202 SER A C   1 
ATOM 1659 O O   . SER A 1 202 ? -26.664  52.295 20.954  1.00 139.36 ?  202 SER A O   1 
ATOM 1660 C CB  . SER A 1 202 ? -24.829  54.005 23.247  1.00 140.44 ?  202 SER A CB  1 
ATOM 1661 O OG  . SER A 1 202 ? -23.679  54.001 24.078  1.00 141.97 ?  202 SER A OG  1 
ATOM 1662 N N   . ASP A 1 203 ? -25.824  54.295 20.351  1.00 137.38 ?  203 ASP A N   1 
ATOM 1663 C CA  . ASP A 1 203 ? -26.899  54.573 19.405  1.00 136.20 ?  203 ASP A CA  1 
ATOM 1664 C C   . ASP A 1 203 ? -26.973  53.546 18.284  1.00 138.65 ?  203 ASP A C   1 
ATOM 1665 O O   . ASP A 1 203 ? -28.040  53.382 17.682  1.00 144.49 ?  203 ASP A O   1 
ATOM 1666 C CB  . ASP A 1 203 ? -26.721  55.971 18.808  1.00 123.46 ?  203 ASP A CB  1 
ATOM 1667 C CG  . ASP A 1 203 ? -26.448  57.025 19.863  1.00 144.20 ?  203 ASP A CG  1 
ATOM 1668 O OD1 . ASP A 1 203 ? -25.575  56.796 20.725  1.00 153.69 ?  203 ASP A OD1 1 
ATOM 1669 O OD2 . ASP A 1 203 ? -27.103  58.086 19.821  1.00 154.70 -1 203 ASP A OD2 1 
ATOM 1670 N N   . PHE A 1 204 ? -25.867  52.862 17.985  1.00 132.43 ?  204 PHE A N   1 
ATOM 1671 C CA  . PHE A 1 204 ? -25.856  51.907 16.882  1.00 131.33 ?  204 PHE A CA  1 
ATOM 1672 C C   . PHE A 1 204 ? -26.764  50.717 17.167  1.00 132.51 ?  204 PHE A C   1 
ATOM 1673 O O   . PHE A 1 204 ? -27.636  50.383 16.358  1.00 129.75 ?  204 PHE A O   1 
ATOM 1674 C CB  . PHE A 1 204 ? -24.424  51.449 16.611  1.00 133.09 ?  204 PHE A CB  1 
ATOM 1675 C CG  . PHE A 1 204 ? -24.264  50.672 15.334  1.00 123.16 ?  204 PHE A CG  1 
ATOM 1676 C CD1 . PHE A 1 204 ? -23.763  49.382 15.353  1.00 123.57 ?  204 PHE A CD1 1 
ATOM 1677 C CD2 . PHE A 1 204 ? -24.621  51.227 14.115  1.00 122.74 ?  204 PHE A CD2 1 
ATOM 1678 C CE1 . PHE A 1 204 ? -23.608  48.662 14.184  1.00 116.72 ?  204 PHE A CE1 1 
ATOM 1679 C CE2 . PHE A 1 204 ? -24.469  50.511 12.939  1.00 122.36 ?  204 PHE A CE2 1 
ATOM 1680 C CZ  . PHE A 1 204 ? -23.962  49.226 12.975  1.00 112.22 ?  204 PHE A CZ  1 
ATOM 1681 N N   . VAL A 1 205 ? -26.579  50.070 18.319  1.00 132.44 ?  205 VAL A N   1 
ATOM 1682 C CA  . VAL A 1 205 ? -27.319  48.845 18.607  1.00 134.93 ?  205 VAL A CA  1 
ATOM 1683 C C   . VAL A 1 205 ? -28.789  49.149 18.877  1.00 127.75 ?  205 VAL A C   1 
ATOM 1684 O O   . VAL A 1 205 ? -29.677  48.397 18.458  1.00 116.93 ?  205 VAL A O   1 
ATOM 1685 C CB  . VAL A 1 205 ? -26.671  48.094 19.784  1.00 124.09 ?  205 VAL A CB  1 
ATOM 1686 C CG1 . VAL A 1 205 ? -27.198  46.666 19.856  1.00 118.14 ?  205 VAL A CG1 1 
ATOM 1687 C CG2 . VAL A 1 205 ? -25.155  48.106 19.652  1.00 106.91 ?  205 VAL A CG2 1 
ATOM 1688 N N   . GLU A 1 206 ? -29.072  50.251 19.574  1.00 130.43 ?  206 GLU A N   1 
ATOM 1689 C CA  . GLU A 1 206 ? -30.441  50.599 19.934  1.00 144.40 ?  206 GLU A CA  1 
ATOM 1690 C C   . GLU A 1 206 ? -31.209  51.247 18.788  1.00 140.94 ?  206 GLU A C   1 
ATOM 1691 O O   . GLU A 1 206 ? -32.259  51.853 19.028  1.00 142.23 ?  206 GLU A O   1 
ATOM 1692 C CB  . GLU A 1 206 ? -30.454  51.515 21.162  1.00 148.82 ?  206 GLU A CB  1 
ATOM 1693 C CG  . GLU A 1 206 ? -29.768  52.854 20.965  1.00 148.78 ?  206 GLU A CG  1 
ATOM 1694 C CD  . GLU A 1 206 ? -29.422  53.527 22.281  1.00 156.88 ?  206 GLU A CD  1 
ATOM 1695 O OE1 . GLU A 1 206 ? -28.380  54.212 22.350  1.00 146.69 ?  206 GLU A OE1 1 
ATOM 1696 O OE2 . GLU A 1 206 ? -30.192  53.368 23.250  1.00 169.05 -1 206 GLU A OE2 1 
ATOM 1697 N N   . SER A 1 207 ? -30.711  51.137 17.556  1.00 128.96 ?  207 SER A N   1 
ATOM 1698 C CA  . SER A 1 207 ? -31.399  51.678 16.392  1.00 135.44 ?  207 SER A CA  1 
ATOM 1699 C C   . SER A 1 207 ? -31.417  50.711 15.214  1.00 125.48 ?  207 SER A C   1 
ATOM 1700 O O   . SER A 1 207 ? -31.894  51.083 14.136  1.00 121.61 ?  207 SER A O   1 
ATOM 1701 C CB  . SER A 1 207 ? -30.762  53.007 15.963  1.00 128.52 ?  207 SER A CB  1 
ATOM 1702 O OG  . SER A 1 207 ? -29.380  52.844 15.696  1.00 131.59 ?  207 SER A OG  1 
ATOM 1703 N N   . ILE A 1 208 ? -30.922  49.484 15.386  1.00 117.15 ?  208 ILE A N   1 
ATOM 1704 C CA  . ILE A 1 208 ? -30.849  48.523 14.289  1.00 116.06 ?  208 ILE A CA  1 
ATOM 1705 C C   . ILE A 1 208 ? -31.478  47.197 14.700  1.00 130.38 ?  208 ILE A C   1 
ATOM 1706 O O   . ILE A 1 208 ? -31.336  46.188 13.999  1.00 131.96 ?  208 ILE A O   1 
ATOM 1707 C CB  . ILE A 1 208 ? -29.393  48.316 13.830  1.00 115.92 ?  208 ILE A CB  1 
ATOM 1708 C CG1 . ILE A 1 208 ? -28.560  47.675 14.942  1.00 118.59 ?  208 ILE A CG1 1 
ATOM 1709 C CG2 . ILE A 1 208 ? -28.775  49.633 13.374  1.00 122.19 ?  208 ILE A CG2 1 
ATOM 1710 C CD1 . ILE A 1 208 ? -28.157  46.242 14.662  1.00 115.09 ?  208 ILE A CD1 1 
ATOM 1711 N N   . ASN A 1 209 ? -32.185  47.184 15.832  1.00 133.38 ?  209 ASN A N   1 
ATOM 1712 C CA  . ASN A 1 209 ? -32.819  45.967 16.347  1.00 121.46 ?  209 ASN A CA  1 
ATOM 1713 C C   . ASN A 1 209 ? -34.286  46.267 16.643  1.00 119.88 ?  209 ASN A C   1 
ATOM 1714 O O   . ASN A 1 209 ? -34.630  46.714 17.740  1.00 129.67 ?  209 ASN A O   1 
ATOM 1715 C CB  . ASN A 1 209 ? -32.089  45.448 17.585  1.00 122.35 ?  209 ASN A CB  1 
ATOM 1716 C CG  . ASN A 1 209 ? -32.632  44.111 18.065  1.00 114.82 ?  209 ASN A CG  1 
ATOM 1717 O OD1 . ASN A 1 209 ? -33.362  43.429 17.345  1.00 107.00 ?  209 ASN A OD1 1 
ATOM 1718 N ND2 . ASN A 1 209 ? -32.277  43.733 19.288  1.00 114.05 ?  209 ASN A ND2 1 
ATOM 1719 N N   . LYS A 1 210 ? -35.153  46.011 15.655  1.00 111.66 ?  210 LYS A N   1 
ATOM 1720 C CA  . LYS A 1 210 ? -36.592  46.164 15.840  1.00 119.95 ?  210 LYS A CA  1 
ATOM 1721 C C   . LYS A 1 210 ? -37.370  45.005 15.222  1.00 110.78 ?  210 LYS A C   1 
ATOM 1722 O O   . LYS A 1 210 ? -38.544  45.178 14.870  1.00 102.93 ?  210 LYS A O   1 
ATOM 1723 C CB  . LYS A 1 210 ? -37.099  47.485 15.242  1.00 102.59 ?  210 LYS A CB  1 
ATOM 1724 C CG  . LYS A 1 210 ? -36.636  48.744 15.962  1.00 120.19 ?  210 LYS A CG  1 
ATOM 1725 C CD  . LYS A 1 210 ? -35.324  49.263 15.394  1.00 126.58 ?  210 LYS A CD  1 
ATOM 1726 C CE  . LYS A 1 210 ? -34.893  50.545 16.086  1.00 131.76 ?  210 LYS A CE  1 
ATOM 1727 N NZ  . LYS A 1 210 ? -34.757  50.363 17.557  1.00 138.46 ?  210 LYS A NZ  1 
ATOM 1728 N N   . SER A 1 211 ? -36.744  43.838 15.071  1.00 115.49 ?  211 SER A N   1 
ATOM 1729 C CA  . SER A 1 211 ? -37.330  42.649 14.455  1.00 112.67 ?  211 SER A CA  1 
ATOM 1730 C C   . SER A 1 211 ? -37.756  42.879 13.010  1.00 102.70 ?  211 SER A C   1 
ATOM 1731 O O   . SER A 1 211 ? -38.457  42.038 12.435  1.00 97.75  ?  211 SER A O   1 
ATOM 1732 C CB  . SER A 1 211 ? -38.516  42.117 15.271  1.00 117.23 ?  211 SER A CB  1 
ATOM 1733 O OG  . SER A 1 211 ? -38.089  41.634 16.533  1.00 101.55 ?  211 SER A OG  1 
ATOM 1734 N N   . LYS A 1 212 ? -37.351  43.994 12.406  1.00 110.14 ?  212 LYS A N   1 
ATOM 1735 C CA  . LYS A 1 212 ? -37.707  44.333 11.033  1.00 100.00 ?  212 LYS A CA  1 
ATOM 1736 C C   . LYS A 1 212 ? -36.457  44.224 10.168  1.00 94.73  ?  212 LYS A C   1 
ATOM 1737 O O   . LYS A 1 212 ? -35.497  44.981 10.351  1.00 91.31  ?  212 LYS A O   1 
ATOM 1738 C CB  . LYS A 1 212 ? -38.320  45.732 10.957  1.00 89.44  ?  212 LYS A CB  1 
ATOM 1739 C CG  . LYS A 1 212 ? -37.576  46.788 11.760  1.00 100.28 ?  212 LYS A CG  1 
ATOM 1740 C CD  . LYS A 1 212 ? -38.087  48.186 11.453  1.00 105.05 ?  212 LYS A CD  1 
ATOM 1741 C CE  . LYS A 1 212 ? -39.542  48.348 11.860  1.00 100.82 ?  212 LYS A CE  1 
ATOM 1742 N NZ  . LYS A 1 212 ? -40.015  49.745 11.658  1.00 121.79 ?  212 LYS A NZ  1 
ATOM 1743 N N   . VAL A 1 213 ? -36.466  43.279 9.234   1.00 91.59  ?  213 VAL A N   1 
ATOM 1744 C CA  . VAL A 1 213 ? -35.345  43.100 8.319   1.00 90.91  ?  213 VAL A CA  1 
ATOM 1745 C C   . VAL A 1 213 ? -35.465  44.129 7.203   1.00 92.35  ?  213 VAL A C   1 
ATOM 1746 O O   . VAL A 1 213 ? -36.449  44.138 6.455   1.00 108.98 ?  213 VAL A O   1 
ATOM 1747 C CB  . VAL A 1 213 ? -35.308  41.673 7.756   1.00 85.56  ?  213 VAL A CB  1 
ATOM 1748 C CG1 . VAL A 1 213 ? -34.297  41.576 6.626   1.00 71.44  ?  213 VAL A CG1 1 
ATOM 1749 C CG2 . VAL A 1 213 ? -34.972  40.682 8.859   1.00 98.80  ?  213 VAL A CG2 1 
ATOM 1750 N N   . LEU A 1 214 ? -34.469  45.000 7.092   1.00 93.05  ?  214 LEU A N   1 
ATOM 1751 C CA  . LEU A 1 214 ? -34.486  46.043 6.081   1.00 96.03  ?  214 LEU A CA  1 
ATOM 1752 C C   . LEU A 1 214 ? -33.843  45.544 4.790   1.00 99.43  ?  214 LEU A C   1 
ATOM 1753 O O   . LEU A 1 214 ? -33.244  44.469 4.733   1.00 104.63 ?  214 LEU A O   1 
ATOM 1754 C CB  . LEU A 1 214 ? -33.779  47.299 6.591   1.00 98.17  ?  214 LEU A CB  1 
ATOM 1755 C CG  . LEU A 1 214 ? -34.649  48.344 7.300   1.00 87.62  ?  214 LEU A CG  1 
ATOM 1756 C CD1 . LEU A 1 214 ? -35.544  47.724 8.365   1.00 90.49  ?  214 LEU A CD1 1 
ATOM 1757 C CD2 . LEU A 1 214 ? -33.777  49.432 7.905   1.00 56.92  ?  214 LEU A CD2 1 
ATOM 1758 N N   . PHE A 1 215 ? -33.975  46.350 3.740   1.00 91.16  ?  215 PHE A N   1 
ATOM 1759 C CA  . PHE A 1 215 ? -33.547  45.962 2.402   1.00 89.73  ?  215 PHE A CA  1 
ATOM 1760 C C   . PHE A 1 215 ? -32.064  46.272 2.239   1.00 93.63  ?  215 PHE A C   1 
ATOM 1761 O O   . PHE A 1 215 ? -31.662  47.441 2.233   1.00 113.13 ?  215 PHE A O   1 
ATOM 1762 C CB  . PHE A 1 215 ? -34.373  46.682 1.341   1.00 85.83  ?  215 PHE A CB  1 
ATOM 1763 C CG  . PHE A 1 215 ? -34.085  46.227 -0.061  1.00 90.73  ?  215 PHE A CG  1 
ATOM 1764 C CD1 . PHE A 1 215 ? -34.195  44.889 -0.402  1.00 96.84  ?  215 PHE A CD1 1 
ATOM 1765 C CD2 . PHE A 1 215 ? -33.705  47.133 -1.037  1.00 87.22  ?  215 PHE A CD2 1 
ATOM 1766 C CE1 . PHE A 1 215 ? -33.932  44.462 -1.689  1.00 103.00 ?  215 PHE A CE1 1 
ATOM 1767 C CE2 . PHE A 1 215 ? -33.439  46.712 -2.326  1.00 94.20  ?  215 PHE A CE2 1 
ATOM 1768 C CZ  . PHE A 1 215 ? -33.554  45.375 -2.653  1.00 94.99  ?  215 PHE A CZ  1 
ATOM 1769 N N   . ASN A 1 216 ? -31.253  45.226 2.105   1.00 85.96  ?  216 ASN A N   1 
ATOM 1770 C CA  . ASN A 1 216 ? -29.829  45.376 1.821   1.00 101.47 ?  216 ASN A CA  1 
ATOM 1771 C C   . ASN A 1 216 ? -29.674  45.478 0.311   1.00 105.74 ?  216 ASN A C   1 
ATOM 1772 O O   . ASN A 1 216 ? -29.685  44.469 -0.397  1.00 94.07  ?  216 ASN A O   1 
ATOM 1773 C CB  . ASN A 1 216 ? -29.034  44.203 2.379   1.00 100.88 ?  216 ASN A CB  1 
ATOM 1774 C CG  . ASN A 1 216 ? -27.544  44.384 2.210   1.00 103.09 ?  216 ASN A CG  1 
ATOM 1775 O OD1 . ASN A 1 216 ? -27.021  44.320 1.097   1.00 113.03 ?  216 ASN A OD1 1 
ATOM 1776 N ND2 . ASN A 1 216 ? -26.847  44.590 3.318   1.00 105.68 ?  216 ASN A ND2 1 
ATOM 1777 N N   . ILE A 1 217 ? -29.520  46.707 -0.188  1.00 106.07 ?  217 ILE A N   1 
ATOM 1778 C CA  . ILE A 1 217 ? -29.432  46.939 -1.625  1.00 97.24  ?  217 ILE A CA  1 
ATOM 1779 C C   . ILE A 1 217 ? -28.144  46.400 -2.228  1.00 97.10  ?  217 ILE A C   1 
ATOM 1780 O O   . ILE A 1 217 ? -27.971  46.455 -3.452  1.00 97.52  ?  217 ILE A O   1 
ATOM 1781 C CB  . ILE A 1 217 ? -29.586  48.446 -1.926  1.00 106.85 ?  217 ILE A CB  1 
ATOM 1782 C CG1 . ILE A 1 217 ? -30.202  48.660 -3.311  1.00 119.53 ?  217 ILE A CG1 1 
ATOM 1783 C CG2 . ILE A 1 217 ? -28.252  49.173 -1.781  1.00 100.32 ?  217 ILE A CG2 1 
ATOM 1784 C CD1 . ILE A 1 217 ? -30.701  50.070 -3.536  1.00 117.02 ?  217 ILE A CD1 1 
ATOM 1785 N N   . TRP A 1 218 ? -27.237  45.875 -1.403  1.00 101.56 ?  218 TRP A N   1 
ATOM 1786 C CA  . TRP A 1 218 ? -25.991  45.283 -1.873  1.00 101.61 ?  218 TRP A CA  1 
ATOM 1787 C C   . TRP A 1 218 ? -26.052  43.769 -1.987  1.00 99.23  ?  218 TRP A C   1 
ATOM 1788 O O   . TRP A 1 218 ? -25.515  43.209 -2.946  1.00 88.61  ?  218 TRP A O   1 
ATOM 1789 C CB  . TRP A 1 218 ? -24.836  45.664 -0.945  1.00 81.72  ?  218 TRP A CB  1 
ATOM 1790 C CG  . TRP A 1 218 ? -24.328  47.052 -1.156  1.00 87.68  ?  218 TRP A CG  1 
ATOM 1791 C CD1 . TRP A 1 218 ? -24.748  48.183 -0.521  1.00 94.86  ?  218 TRP A CD1 1 
ATOM 1792 C CD2 . TRP A 1 218 ? -23.288  47.460 -2.056  1.00 97.38  ?  218 TRP A CD2 1 
ATOM 1793 N NE1 . TRP A 1 218 ? -24.041  49.271 -0.972  1.00 90.70  ?  218 TRP A NE1 1 
ATOM 1794 C CE2 . TRP A 1 218 ? -23.138  48.854 -1.914  1.00 95.90  ?  218 TRP A CE2 1 
ATOM 1795 C CE3 . TRP A 1 218 ? -22.470  46.784 -2.970  1.00 86.84  ?  218 TRP A CE3 1 
ATOM 1796 C CZ2 . TRP A 1 218 ? -22.206  49.585 -2.650  1.00 78.14  ?  218 TRP A CZ2 1 
ATOM 1797 C CZ3 . TRP A 1 218 ? -21.544  47.515 -3.700  1.00 79.54  ?  218 TRP A CZ3 1 
ATOM 1798 C CH2 . TRP A 1 218 ? -21.421  48.899 -3.535  1.00 68.01  ?  218 TRP A CH2 1 
ATOM 1799 N N   . PHE A 1 219 ? -26.685  43.100 -1.020  1.00 100.68 ?  219 PHE A N   1 
ATOM 1800 C CA  . PHE A 1 219 ? -26.724  41.641 -1.018  1.00 103.23 ?  219 PHE A CA  1 
ATOM 1801 C C   . PHE A 1 219 ? -27.515  41.104 -2.204  1.00 111.67 ?  219 PHE A C   1 
ATOM 1802 O O   . PHE A 1 219 ? -27.065  40.186 -2.901  1.00 110.56 ?  219 PHE A O   1 
ATOM 1803 C CB  . PHE A 1 219 ? -27.320  41.134 0.296   1.00 106.39 ?  219 PHE A CB  1 
ATOM 1804 C CG  . PHE A 1 219 ? -26.408  41.288 1.481   1.00 115.83 ?  219 PHE A CG  1 
ATOM 1805 C CD1 . PHE A 1 219 ? -25.055  41.520 1.306   1.00 114.52 ?  219 PHE A CD1 1 
ATOM 1806 C CD2 . PHE A 1 219 ? -26.903  41.175 2.771   1.00 117.85 ?  219 PHE A CD2 1 
ATOM 1807 C CE1 . PHE A 1 219 ? -24.212  41.651 2.394   1.00 118.93 ?  219 PHE A CE1 1 
ATOM 1808 C CE2 . PHE A 1 219 ? -26.066  41.305 3.863   1.00 106.65 ?  219 PHE A CE2 1 
ATOM 1809 C CZ  . PHE A 1 219 ? -24.719  41.543 3.675   1.00 115.45 ?  219 PHE A CZ  1 
ATOM 1810 N N   . TYR A 1 220 ? -28.704  41.661 -2.447  1.00 110.85 ?  220 TYR A N   1 
ATOM 1811 C CA  . TYR A 1 220 ? -29.520  41.185 -3.558  1.00 114.73 ?  220 TYR A CA  1 
ATOM 1812 C C   . TYR A 1 220 ? -28.885  41.497 -4.906  1.00 117.16 ?  220 TYR A C   1 
ATOM 1813 O O   . TYR A 1 220 ? -29.209  40.836 -5.897  1.00 102.25 ?  220 TYR A O   1 
ATOM 1814 C CB  . TYR A 1 220 ? -30.930  41.775 -3.476  1.00 114.58 ?  220 TYR A CB  1 
ATOM 1815 C CG  . TYR A 1 220 ? -31.129  43.065 -4.235  1.00 117.51 ?  220 TYR A CG  1 
ATOM 1816 C CD1 . TYR A 1 220 ? -31.973  43.118 -5.337  1.00 114.52 ?  220 TYR A CD1 1 
ATOM 1817 C CD2 . TYR A 1 220 ? -30.490  44.232 -3.843  1.00 112.68 ?  220 TYR A CD2 1 
ATOM 1818 C CE1 . TYR A 1 220 ? -32.166  44.296 -6.033  1.00 129.13 ?  220 TYR A CE1 1 
ATOM 1819 C CE2 . TYR A 1 220 ? -30.676  45.413 -4.534  1.00 118.20 ?  220 TYR A CE2 1 
ATOM 1820 C CZ  . TYR A 1 220 ? -31.514  45.440 -5.627  1.00 132.35 ?  220 TYR A CZ  1 
ATOM 1821 O OH  . TYR A 1 220 ? -31.700  46.618 -6.314  1.00 143.36 ?  220 TYR A OH  1 
ATOM 1822 N N   . GLN A 1 221 ? -27.995  42.490 -4.965  1.00 115.00 ?  221 GLN A N   1 
ATOM 1823 C CA  . GLN A 1 221 ? -27.162  42.670 -6.147  1.00 114.14 ?  221 GLN A CA  1 
ATOM 1824 C C   . GLN A 1 221 ? -26.018  41.666 -6.176  1.00 95.81  ?  221 GLN A C   1 
ATOM 1825 O O   . GLN A 1 221 ? -25.578  41.259 -7.256  1.00 119.23 ?  221 GLN A O   1 
ATOM 1826 C CB  . GLN A 1 221 ? -26.610  44.096 -6.192  1.00 94.31  ?  221 GLN A CB  1 
ATOM 1827 C CG  . GLN A 1 221 ? -27.666  45.169 -6.412  1.00 107.06 ?  221 GLN A CG  1 
ATOM 1828 C CD  . GLN A 1 221 ? -27.793  45.583 -7.866  1.00 122.99 ?  221 GLN A CD  1 
ATOM 1829 O OE1 . GLN A 1 221 ? -27.597  46.750 -8.210  1.00 129.08 ?  221 GLN A OE1 1 
ATOM 1830 N NE2 . GLN A 1 221 ? -28.122  44.628 -8.729  1.00 125.38 ?  221 GLN A NE2 1 
ATOM 1831 N N   . TYR A 1 222 ? -25.531  41.263 -5.001  1.00 85.33  ?  222 TYR A N   1 
ATOM 1832 C CA  . TYR A 1 222 ? -24.444  40.294 -4.929  1.00 100.38 ?  222 TYR A CA  1 
ATOM 1833 C C   . TYR A 1 222 ? -24.938  38.897 -5.282  1.00 106.21 ?  222 TYR A C   1 
ATOM 1834 O O   . TYR A 1 222 ? -24.370  38.225 -6.152  1.00 104.79 ?  222 TYR A O   1 
ATOM 1835 C CB  . TYR A 1 222 ? -23.833  40.320 -3.524  1.00 111.42 ?  222 TYR A CB  1 
ATOM 1836 C CG  . TYR A 1 222 ? -22.746  39.300 -3.249  1.00 115.87 ?  222 TYR A CG  1 
ATOM 1837 C CD1 . TYR A 1 222 ? -21.953  38.788 -4.270  1.00 112.29 ?  222 TYR A CD1 1 
ATOM 1838 C CD2 . TYR A 1 222 ? -22.515  38.850 -1.956  1.00 113.98 ?  222 TYR A CD2 1 
ATOM 1839 C CE1 . TYR A 1 222 ? -20.962  37.858 -4.007  1.00 122.14 ?  222 TYR A CE1 1 
ATOM 1840 C CE2 . TYR A 1 222 ? -21.530  37.924 -1.685  1.00 120.67 ?  222 TYR A CE2 1 
ATOM 1841 C CZ  . TYR A 1 222 ? -20.756  37.431 -2.712  1.00 130.40 ?  222 TYR A CZ  1 
ATOM 1842 O OH  . TYR A 1 222 ? -19.774  36.506 -2.441  1.00 124.12 ?  222 TYR A OH  1 
ATOM 1843 N N   . GLU A 1 223 ? -26.002  38.443 -4.617  1.00 116.59 ?  223 GLU A N   1 
ATOM 1844 C CA  . GLU A 1 223 ? -26.473  37.080 -4.831  1.00 119.29 ?  223 GLU A CA  1 
ATOM 1845 C C   . GLU A 1 223 ? -27.423  36.989 -6.020  1.00 117.81 ?  223 GLU A C   1 
ATOM 1846 O O   . GLU A 1 223 ? -27.392  36.004 -6.765  1.00 125.93 ?  223 GLU A O   1 
ATOM 1847 C CB  . GLU A 1 223 ? -27.147  36.554 -3.564  1.00 117.05 ?  223 GLU A CB  1 
ATOM 1848 C CG  . GLU A 1 223 ? -26.212  36.427 -2.366  1.00 116.08 ?  223 GLU A CG  1 
ATOM 1849 C CD  . GLU A 1 223 ? -26.764  37.103 -1.128  1.00 120.89 ?  223 GLU A CD  1 
ATOM 1850 O OE1 . GLU A 1 223 ? -27.681  37.937 -1.270  1.00 124.86 ?  223 GLU A OE1 1 
ATOM 1851 O OE2 . GLU A 1 223 ? -26.278  36.809 -0.015  1.00 124.61 -1 223 GLU A OE2 1 
ATOM 1852 N N   . GLY A 1 224 ? -28.257  37.996 -6.217  1.00 110.40 ?  224 GLY A N   1 
ATOM 1853 C CA  . GLY A 1 224 ? -29.230  37.985 -7.297  1.00 115.25 ?  224 GLY A CA  1 
ATOM 1854 C C   . GLY A 1 224 ? -30.629  37.810 -6.736  1.00 112.47 ?  224 GLY A C   1 
ATOM 1855 O O   . GLY A 1 224 ? -30.842  37.062 -5.775  1.00 114.03 ?  224 GLY A O   1 
ATOM 1856 N N   . ARG A 1 225 ? -31.595  38.511 -7.339  1.00 104.35 ?  225 ARG A N   1 
ATOM 1857 C CA  . ARG A 1 225 ? -32.974  38.473 -6.856  1.00 91.62  ?  225 ARG A CA  1 
ATOM 1858 C C   . ARG A 1 225 ? -33.505  37.046 -6.783  1.00 99.68  ?  225 ARG A C   1 
ATOM 1859 O O   . ARG A 1 225 ? -34.131  36.652 -5.793  1.00 109.33 ?  225 ARG A O   1 
ATOM 1860 C CB  . ARG A 1 225 ? -33.863  39.331 -7.758  1.00 108.21 ?  225 ARG A CB  1 
ATOM 1861 C CG  . ARG A 1 225 ? -35.299  39.444 -7.283  1.00 98.89  ?  225 ARG A CG  1 
ATOM 1862 C CD  . ARG A 1 225 ? -36.176  40.104 -8.333  1.00 102.75 ?  225 ARG A CD  1 
ATOM 1863 N NE  . ARG A 1 225 ? -37.082  39.150 -8.969  1.00 129.50 ?  225 ARG A NE  1 
ATOM 1864 C CZ  . ARG A 1 225 ? -38.369  39.024 -8.663  1.00 110.30 ?  225 ARG A CZ  1 
ATOM 1865 N NH1 . ARG A 1 225 ? -38.908  39.791 -7.727  1.00 99.56  ?  225 ARG A NH1 1 
ATOM 1866 N NH2 . ARG A 1 225 ? -39.119  38.130 -9.294  1.00 92.68  ?  225 ARG A NH2 1 
ATOM 1867 N N   . LYS A 1 226 ? -33.266  36.256 -7.832  1.00 109.69 ?  226 LYS A N   1 
ATOM 1868 C CA  . LYS A 1 226 ? -33.696  34.862 -7.822  1.00 107.96 ?  226 LYS A CA  1 
ATOM 1869 C C   . LYS A 1 226 ? -33.061  34.088 -6.673  1.00 109.88 ?  226 LYS A C   1 
ATOM 1870 O O   . LYS A 1 226 ? -33.671  33.153 -6.141  1.00 119.01 ?  226 LYS A O   1 
ATOM 1871 C CB  . LYS A 1 226 ? -33.362  34.209 -9.164  1.00 125.76 ?  226 LYS A CB  1 
ATOM 1872 C CG  . LYS A 1 226 ? -33.727  32.737 -9.267  1.00 120.72 ?  226 LYS A CG  1 
ATOM 1873 C CD  . LYS A 1 226 ? -32.892  32.043 -10.330 1.00 124.10 ?  226 LYS A CD  1 
ATOM 1874 C CE  . LYS A 1 226 ? -33.032  30.533 -10.244 1.00 122.22 ?  226 LYS A CE  1 
ATOM 1875 N NZ  . LYS A 1 226 ? -32.016  29.835 -11.078 1.00 118.80 ?  226 LYS A NZ  1 
ATOM 1876 N N   . GLU A 1 227 ? -31.852  34.470 -6.266  1.00 119.43 ?  227 GLU A N   1 
ATOM 1877 C CA  . GLU A 1 227 ? -31.147  33.815 -5.171  1.00 128.29 ?  227 GLU A CA  1 
ATOM 1878 C C   . GLU A 1 227 ? -31.313  34.536 -3.840  1.00 121.55 ?  227 GLU A C   1 
ATOM 1879 O O   . GLU A 1 227 ? -31.378  33.884 -2.794  1.00 123.85 ?  227 GLU A O   1 
ATOM 1880 C CB  . GLU A 1 227 ? -29.656  33.695 -5.503  1.00 133.51 ?  227 GLU A CB  1 
ATOM 1881 C CG  . GLU A 1 227 ? -28.879  32.786 -4.565  1.00 152.12 ?  227 GLU A CG  1 
ATOM 1882 C CD  . GLU A 1 227 ? -29.251  31.326 -4.731  1.00 175.30 ?  227 GLU A CD  1 
ATOM 1883 O OE1 . GLU A 1 227 ? -29.681  30.942 -5.839  1.00 184.85 ?  227 GLU A OE1 1 
ATOM 1884 O OE2 . GLU A 1 227 ? -29.115  30.561 -3.753  1.00 185.55 -1 227 GLU A OE2 1 
ATOM 1885 N N   . TYR A 1 228 ? -31.382  35.870 -3.856  1.00 110.72 ?  228 TYR A N   1 
ATOM 1886 C CA  . TYR A 1 228 ? -31.575  36.619 -2.617  1.00 100.97 ?  228 TYR A CA  1 
ATOM 1887 C C   . TYR A 1 228 ? -32.921  36.305 -1.980  1.00 115.86 ?  228 TYR A C   1 
ATOM 1888 O O   . TYR A 1 228 ? -33.034  36.277 -0.749  1.00 114.34 ?  228 TYR A O   1 
ATOM 1889 C CB  . TYR A 1 228 ? -31.447  38.118 -2.890  1.00 103.41 ?  228 TYR A CB  1 
ATOM 1890 C CG  . TYR A 1 228 ? -32.079  39.009 -1.844  1.00 102.26 ?  228 TYR A CG  1 
ATOM 1891 C CD1 . TYR A 1 228 ? -33.304  39.622 -2.075  1.00 97.14  ?  228 TYR A CD1 1 
ATOM 1892 C CD2 . TYR A 1 228 ? -31.443  39.251 -0.634  1.00 99.16  ?  228 TYR A CD2 1 
ATOM 1893 C CE1 . TYR A 1 228 ? -33.882  40.442 -1.126  1.00 99.89  ?  228 TYR A CE1 1 
ATOM 1894 C CE2 . TYR A 1 228 ? -32.013  40.071 0.321   1.00 103.55 ?  228 TYR A CE2 1 
ATOM 1895 C CZ  . TYR A 1 228 ? -33.233  40.664 0.069   1.00 106.49 ?  228 TYR A CZ  1 
ATOM 1896 O OH  . TYR A 1 228 ? -33.806  41.481 1.017   1.00 117.29 ?  228 TYR A OH  1 
ATOM 1897 N N   . LEU A 1 229 ? -33.950  36.065 -2.795  1.00 112.86 ?  229 LEU A N   1 
ATOM 1898 C CA  . LEU A 1 229 ? -35.248  35.691 -2.247  1.00 107.57 ?  229 LEU A CA  1 
ATOM 1899 C C   . LEU A 1 229 ? -35.226  34.265 -1.709  1.00 108.43 ?  229 LEU A C   1 
ATOM 1900 O O   . LEU A 1 229 ? -35.881  33.966 -0.704  1.00 107.76 ?  229 LEU A O   1 
ATOM 1901 C CB  . LEU A 1 229 ? -36.336  35.853 -3.309  1.00 100.61 ?  229 LEU A CB  1 
ATOM 1902 C CG  . LEU A 1 229 ? -36.996  37.234 -3.412  1.00 105.01 ?  229 LEU A CG  1 
ATOM 1903 C CD1 . LEU A 1 229 ? -37.555  37.653 -2.069  1.00 109.64 ?  229 LEU A CD1 1 
ATOM 1904 C CD2 . LEU A 1 229 ? -36.040  38.292 -3.935  1.00 97.84  ?  229 LEU A CD2 1 
ATOM 1905 N N   . ARG A 1 230 ? -34.479  33.372 -2.365  1.00 106.70 ?  230 ARG A N   1 
ATOM 1906 C CA  . ARG A 1 230 ? -34.317  32.020 -1.840  1.00 113.46 ?  230 ARG A CA  1 
ATOM 1907 C C   . ARG A 1 230 ? -33.572  32.030 -0.512  1.00 123.02 ?  230 ARG A C   1 
ATOM 1908 O O   . ARG A 1 230 ? -33.861  31.211 0.368   1.00 127.58 ?  230 ARG A O   1 
ATOM 1909 C CB  . ARG A 1 230 ? -33.592  31.140 -2.862  1.00 114.69 ?  230 ARG A CB  1 
ATOM 1910 C CG  . ARG A 1 230 ? -32.469  30.288 -2.282  1.00 140.64 ?  230 ARG A CG  1 
ATOM 1911 C CD  . ARG A 1 230 ? -31.942  29.282 -3.296  1.00 155.72 ?  230 ARG A CD  1 
ATOM 1912 N NE  . ARG A 1 230 ? -30.533  28.961 -3.079  1.00 160.26 ?  230 ARG A NE  1 
ATOM 1913 C CZ  . ARG A 1 230 ? -30.068  28.245 -2.059  1.00 153.52 ?  230 ARG A CZ  1 
ATOM 1914 N NH1 . ARG A 1 230 ? -30.899  27.757 -1.148  1.00 139.82 ?  230 ARG A NH1 1 
ATOM 1915 N NH2 . ARG A 1 230 ? -28.767  28.010 -1.954  1.00 153.59 ?  230 ARG A NH2 1 
ATOM 1916 N N   . LYS A 1 231 ? -32.618  32.950 -0.346  1.00 122.97 ?  231 LYS A N   1 
ATOM 1917 C CA  . LYS A 1 231 ? -31.934  33.083 0.936   1.00 124.70 ?  231 LYS A CA  1 
ATOM 1918 C C   . LYS A 1 231 ? -32.890  33.531 2.033   1.00 118.34 ?  231 LYS A C   1 
ATOM 1919 O O   . LYS A 1 231 ? -32.698  33.183 3.203   1.00 122.99 ?  231 LYS A O   1 
ATOM 1920 C CB  . LYS A 1 231 ? -30.770  34.067 0.813   1.00 126.86 ?  231 LYS A CB  1 
ATOM 1921 C CG  . LYS A 1 231 ? -29.424  33.410 0.556   1.00 133.95 ?  231 LYS A CG  1 
ATOM 1922 C CD  . LYS A 1 231 ? -28.314  34.447 0.489   1.00 140.71 ?  231 LYS A CD  1 
ATOM 1923 C CE  . LYS A 1 231 ? -26.966  33.806 0.198   1.00 136.27 ?  231 LYS A CE  1 
ATOM 1924 N NZ  . LYS A 1 231 ? -26.414  33.104 1.388   1.00 133.12 ?  231 LYS A NZ  1 
ATOM 1925 N N   . LEU A 1 232 ? -33.922  34.299 1.678   1.00 111.25 ?  232 LEU A N   1 
ATOM 1926 C CA  . LEU A 1 232 ? -34.905  34.725 2.668   1.00 109.21 ?  232 LEU A CA  1 
ATOM 1927 C C   . LEU A 1 232 ? -35.873  33.600 3.013   1.00 111.08 ?  232 LEU A C   1 
ATOM 1928 O O   . LEU A 1 232 ? -36.274  33.458 4.174   1.00 112.62 ?  232 LEU A O   1 
ATOM 1929 C CB  . LEU A 1 232 ? -35.667  35.948 2.157   1.00 98.05  ?  232 LEU A CB  1 
ATOM 1930 C CG  . LEU A 1 232 ? -34.850  37.229 1.974   1.00 94.65  ?  232 LEU A CG  1 
ATOM 1931 C CD1 . LEU A 1 232 ? -35.760  38.390 1.609   1.00 93.93  ?  232 LEU A CD1 1 
ATOM 1932 C CD2 . LEU A 1 232 ? -34.045  37.547 3.225   1.00 92.39  ?  232 LEU A CD2 1 
ATOM 1933 N N   . LYS A 1 233 ? -36.261  32.799 2.019   1.00 108.79 ?  233 LYS A N   1 
ATOM 1934 C CA  . LYS A 1 233 ? -37.202  31.709 2.260   1.00 106.01 ?  233 LYS A CA  1 
ATOM 1935 C C   . LYS A 1 233 ? -36.598  30.645 3.169   1.00 118.16 ?  233 LYS A C   1 
ATOM 1936 O O   . LYS A 1 233 ? -37.185  30.278 4.193   1.00 127.14 ?  233 LYS A O   1 
ATOM 1937 C CB  . LYS A 1 233 ? -37.640  31.093 0.931   1.00 102.56 ?  233 LYS A CB  1 
ATOM 1938 C CG  . LYS A 1 233 ? -38.411  29.792 1.078   1.00 106.58 ?  233 LYS A CG  1 
ATOM 1939 C CD  . LYS A 1 233 ? -38.801  29.229 -0.278  1.00 110.78 ?  233 LYS A CD  1 
ATOM 1940 C CE  . LYS A 1 233 ? -39.574  27.928 -0.137  1.00 117.38 ?  233 LYS A CE  1 
ATOM 1941 N NZ  . LYS A 1 233 ? -39.988  27.389 -1.462  1.00 113.41 ?  233 LYS A NZ  1 
ATOM 1942 N N   . GLU A 1 234 ? -35.418  30.136 2.804   1.00 119.99 ?  234 GLU A N   1 
ATOM 1943 C CA  . GLU A 1 234 ? -34.805  29.049 3.561   1.00 127.16 ?  234 GLU A CA  1 
ATOM 1944 C C   . GLU A 1 234 ? -34.415  29.480 4.968   1.00 127.48 ?  234 GLU A C   1 
ATOM 1945 O O   . GLU A 1 234 ? -34.326  28.639 5.870   1.00 131.92 ?  234 GLU A O   1 
ATOM 1946 C CB  . GLU A 1 234 ? -33.577  28.523 2.817   1.00 134.68 ?  234 GLU A CB  1 
ATOM 1947 C CG  . GLU A 1 234 ? -33.884  27.871 1.481   1.00 130.39 ?  234 GLU A CG  1 
ATOM 1948 C CD  . GLU A 1 234 ? -34.401  26.455 1.628   1.00 147.93 ?  234 GLU A CD  1 
ATOM 1949 O OE1 . GLU A 1 234 ? -34.999  25.939 0.662   1.00 150.48 ?  234 GLU A OE1 1 
ATOM 1950 O OE2 . GLU A 1 234 ? -34.209  25.857 2.708   1.00 165.56 -1 234 GLU A OE2 1 
ATOM 1951 N N   . SER A 1 235 ? -34.178  30.773 5.178   1.00 125.94 ?  235 SER A N   1 
ATOM 1952 C CA  . SER A 1 235 ? -33.691  31.254 6.465   1.00 127.78 ?  235 SER A CA  1 
ATOM 1953 C C   . SER A 1 235 ? -34.826  31.547 7.440   1.00 118.08 ?  235 SER A C   1 
ATOM 1954 O O   . SER A 1 235 ? -34.785  31.108 8.593   1.00 130.09 ?  235 SER A O   1 
ATOM 1955 C CB  . SER A 1 235 ? -32.834  32.506 6.264   1.00 131.11 ?  235 SER A CB  1 
ATOM 1956 O OG  . SER A 1 235 ? -31.866  32.302 5.250   1.00 137.40 ?  235 SER A OG  1 
ATOM 1957 N N   . PHE A 1 236 ? -35.845  32.282 6.995   1.00 117.17 ?  236 PHE A N   1 
ATOM 1958 C CA  . PHE A 1 236 ? -36.894  32.752 7.894   1.00 122.48 ?  236 PHE A CA  1 
ATOM 1959 C C   . PHE A 1 236 ? -38.078  31.789 7.970   1.00 126.11 ?  236 PHE A C   1 
ATOM 1960 O O   . PHE A 1 236 ? -38.415  31.296 9.051   1.00 133.97 ?  236 PHE A O   1 
ATOM 1961 C CB  . PHE A 1 236 ? -37.374  34.142 7.461   1.00 127.11 ?  236 PHE A CB  1 
ATOM 1962 C CG  . PHE A 1 236 ? -36.351  35.227 7.650   1.00 129.12 ?  236 PHE A CG  1 
ATOM 1963 C CD1 . PHE A 1 236 ? -35.449  35.531 6.644   1.00 123.75 ?  236 PHE A CD1 1 
ATOM 1964 C CD2 . PHE A 1 236 ? -36.296  35.946 8.832   1.00 124.26 ?  236 PHE A CD2 1 
ATOM 1965 C CE1 . PHE A 1 236 ? -34.511  36.531 6.814   1.00 119.18 ?  236 PHE A CE1 1 
ATOM 1966 C CE2 . PHE A 1 236 ? -35.359  36.947 9.009   1.00 100.20 ?  236 PHE A CE2 1 
ATOM 1967 C CZ  . PHE A 1 236 ? -34.466  37.239 7.999   1.00 111.69 ?  236 PHE A CZ  1 
ATOM 1968 N N   . ILE A 1 237 ? -38.716  31.514 6.835   1.00 107.48 ?  237 ILE A N   1 
ATOM 1969 C CA  . ILE A 1 237 ? -40.014  30.843 6.854   1.00 111.28 ?  237 ILE A CA  1 
ATOM 1970 C C   . ILE A 1 237 ? -39.878  29.326 6.755   1.00 117.49 ?  237 ILE A C   1 
ATOM 1971 O O   . ILE A 1 237 ? -40.620  28.593 7.414   1.00 122.16 ?  237 ILE A O   1 
ATOM 1972 C CB  . ILE A 1 237 ? -40.915  31.418 5.738   1.00 110.20 ?  237 ILE A CB  1 
ATOM 1973 C CG1 . ILE A 1 237 ? -40.384  31.069 4.344   1.00 113.31 ?  237 ILE A CG1 1 
ATOM 1974 C CG2 . ILE A 1 237 ? -41.047  32.926 5.890   1.00 98.61  ?  237 ILE A CG2 1 
ATOM 1975 C CD1 . ILE A 1 237 ? -41.067  29.873 3.701   1.00 110.16 ?  237 ILE A CD1 1 
ATOM 1976 N N   . ARG A 1 238 ? -38.946  28.821 5.944   1.00 117.35 ?  238 ARG A N   1 
ATOM 1977 C CA  . ARG A 1 238 ? -38.809  27.374 5.808   1.00 124.61 ?  238 ARG A CA  1 
ATOM 1978 C C   . ARG A 1 238 ? -38.200  26.764 7.063   1.00 136.94 ?  238 ARG A C   1 
ATOM 1979 O O   . ARG A 1 238 ? -38.563  25.651 7.461   1.00 140.19 ?  238 ARG A O   1 
ATOM 1980 C CB  . ARG A 1 238 ? -37.972  27.038 4.574   1.00 136.32 ?  238 ARG A CB  1 
ATOM 1981 C CG  . ARG A 1 238 ? -38.331  25.709 3.926   1.00 147.06 ?  238 ARG A CG  1 
ATOM 1982 C CD  . ARG A 1 238 ? -37.683  25.568 2.556   1.00 145.93 ?  238 ARG A CD  1 
ATOM 1983 N NE  . ARG A 1 238 ? -38.070  24.328 1.889   1.00 160.70 ?  238 ARG A NE  1 
ATOM 1984 C CZ  . ARG A 1 238 ? -37.672  23.978 0.669   1.00 149.67 ?  238 ARG A CZ  1 
ATOM 1985 N NH1 . ARG A 1 238 ? -36.874  24.777 -0.025  1.00 133.02 ?  238 ARG A NH1 1 
ATOM 1986 N NH2 . ARG A 1 238 ? -38.072  22.829 0.142   1.00 138.44 ?  238 ARG A NH2 1 
ATOM 1987 N N   . ARG A 1 239 ? -37.268  27.480 7.694   1.00 138.44 ?  239 ARG A N   1 
ATOM 1988 C CA  . ARG A 1 239 ? -36.740  27.049 8.984   1.00 140.15 ?  239 ARG A CA  1 
ATOM 1989 C C   . ARG A 1 239 ? -37.822  27.079 10.056  1.00 133.14 ?  239 ARG A C   1 
ATOM 1990 O O   . ARG A 1 239 ? -37.863  26.207 10.931  1.00 139.86 ?  239 ARG A O   1 
ATOM 1991 C CB  . ARG A 1 239 ? -35.557  27.940 9.377   1.00 138.01 ?  239 ARG A CB  1 
ATOM 1992 C CG  . ARG A 1 239 ? -34.873  27.603 10.703  1.00 155.53 ?  239 ARG A CG  1 
ATOM 1993 C CD  . ARG A 1 239 ? -35.501  28.343 11.882  1.00 160.01 ?  239 ARG A CD  1 
ATOM 1994 N NE  . ARG A 1 239 ? -35.976  29.671 11.506  1.00 148.81 ?  239 ARG A NE  1 
ATOM 1995 C CZ  . ARG A 1 239 ? -36.836  30.387 12.224  1.00 139.08 ?  239 ARG A CZ  1 
ATOM 1996 N NH1 . ARG A 1 239 ? -37.319  29.902 13.360  1.00 133.48 ?  239 ARG A NH1 1 
ATOM 1997 N NH2 . ARG A 1 239 ? -37.216  31.586 11.806  1.00 140.33 ?  239 ARG A NH2 1 
ATOM 1998 N N   . SER A 1 240 ? -38.701  28.084 10.007  1.00 132.03 ?  240 SER A N   1 
ATOM 1999 C CA  . SER A 1 240 ? -39.663  28.297 11.085  1.00 141.06 ?  240 SER A CA  1 
ATOM 2000 C C   . SER A 1 240 ? -40.625  27.122 11.218  1.00 145.56 ?  240 SER A C   1 
ATOM 2001 O O   . SER A 1 240 ? -40.629  26.417 12.232  1.00 157.28 ?  240 SER A O   1 
ATOM 2002 C CB  . SER A 1 240 ? -40.431  29.600 10.849  1.00 128.68 ?  240 SER A CB  1 
ATOM 2003 O OG  . SER A 1 240 ? -41.306  29.487 9.740   1.00 128.08 ?  240 SER A OG  1 
ATOM 2004 N N   . VAL A 1 241 ? -41.444  26.888 10.194  1.00 134.39 ?  241 VAL A N   1 
ATOM 2005 C CA  . VAL A 1 241 ? -42.509  25.897 10.270  1.00 140.17 ?  241 VAL A CA  1 
ATOM 2006 C C   . VAL A 1 241 ? -42.539  25.082 8.985   1.00 143.08 ?  241 VAL A C   1 
ATOM 2007 O O   . VAL A 1 241 ? -42.266  25.591 7.893   1.00 142.60 ?  241 VAL A O   1 
ATOM 2008 C CB  . VAL A 1 241 ? -43.881  26.563 10.536  1.00 140.10 ?  241 VAL A CB  1 
ATOM 2009 C CG1 . VAL A 1 241 ? -44.269  27.478 9.383   1.00 135.63 ?  241 VAL A CG1 1 
ATOM 2010 C CG2 . VAL A 1 241 ? -44.955  25.513 10.792  1.00 135.01 ?  241 VAL A CG2 1 
ATOM 2011 N N   . ASN A 1 242 ? -42.860  23.797 9.126   1.00 145.27 ?  242 ASN A N   1 
ATOM 2012 C CA  . ASN A 1 242 ? -43.001  22.896 7.989   1.00 151.87 ?  242 ASN A CA  1 
ATOM 2013 C C   . ASN A 1 242 ? -44.396  22.301 7.882   1.00 151.14 ?  242 ASN A C   1 
ATOM 2014 O O   . ASN A 1 242 ? -44.993  22.332 6.800   1.00 162.58 ?  242 ASN A O   1 
ATOM 2015 C CB  . ASN A 1 242 ? -41.953  21.775 8.078   1.00 156.52 ?  242 ASN A CB  1 
ATOM 2016 C CG  . ASN A 1 242 ? -40.541  22.308 8.220   1.00 147.16 ?  242 ASN A CG  1 
ATOM 2017 O OD1 . ASN A 1 242 ? -40.158  22.813 9.275   1.00 147.23 ?  242 ASN A OD1 1 
ATOM 2018 N ND2 . ASN A 1 242 ? -39.757  22.197 7.154   1.00 134.13 ?  242 ASN A ND2 1 
ATOM 2019 N N   . THR A 1 243 ? -44.940  21.755 8.979   1.00 136.92 ?  243 THR A N   1 
ATOM 2020 C CA  . THR A 1 243 ? -46.235  21.085 8.927   1.00 146.32 ?  243 THR A CA  1 
ATOM 2021 C C   . THR A 1 243 ? -47.117  21.362 10.141  1.00 146.71 ?  243 THR A C   1 
ATOM 2022 O O   . THR A 1 243 ? -48.160  20.711 10.285  1.00 134.81 ?  243 THR A O   1 
ATOM 2023 C CB  . THR A 1 243 ? -46.055  19.564 8.789   1.00 148.64 ?  243 THR A CB  1 
ATOM 2024 O OG1 . THR A 1 243 ? -45.100  19.104 9.753   1.00 165.18 ?  243 THR A OG1 1 
ATOM 2025 C CG2 . THR A 1 243 ? -45.587  19.190 7.388   1.00 139.08 ?  243 THR A CG2 1 
ATOM 2026 N N   . SER A 1 244 ? -46.748  22.292 11.010  1.00 144.83 ?  244 SER A N   1 
ATOM 2027 C CA  . SER A 1 244 ? -47.453  22.439 12.281  1.00 139.17 ?  244 SER A CA  1 
ATOM 2028 C C   . SER A 1 244 ? -48.696  23.308 12.106  1.00 121.91 ?  244 SER A C   1 
ATOM 2029 O O   . SER A 1 244 ? -48.601  24.412 11.561  1.00 115.72 ?  244 SER A O   1 
ATOM 2030 C CB  . SER A 1 244 ? -46.532  23.051 13.329  1.00 134.95 ?  244 SER A CB  1 
ATOM 2031 O OG  . SER A 1 244 ? -45.358  22.273 13.492  1.00 132.90 ?  244 SER A OG  1 
ATOM 2032 N N   . PRO A 1 245 ? -49.874  22.849 12.553  1.00 115.92 ?  245 PRO A N   1 
ATOM 2033 C CA  . PRO A 1 245 ? -51.090  23.669 12.456  1.00 114.29 ?  245 PRO A CA  1 
ATOM 2034 C C   . PRO A 1 245 ? -51.153  24.717 13.557  1.00 105.17 ?  245 PRO A C   1 
ATOM 2035 O O   . PRO A 1 245 ? -51.441  24.406 14.717  1.00 109.17 ?  245 PRO A O   1 
ATOM 2036 C CB  . PRO A 1 245 ? -52.214  22.631 12.589  1.00 110.24 ?  245 PRO A CB  1 
ATOM 2037 C CG  . PRO A 1 245 ? -51.622  21.563 13.443  1.00 111.83 ?  245 PRO A CG  1 
ATOM 2038 C CD  . PRO A 1 245 ? -50.153  21.504 13.090  1.00 118.39 ?  245 PRO A CD  1 
ATOM 2039 N N   . TYR A 1 246 ? -50.911  25.973 13.188  1.00 100.50 ?  246 TYR A N   1 
ATOM 2040 C CA  . TYR A 1 246 ? -50.958  27.095 14.116  1.00 101.61 ?  246 TYR A CA  1 
ATOM 2041 C C   . TYR A 1 246 ? -51.870  28.179 13.551  1.00 98.93  ?  246 TYR A C   1 
ATOM 2042 O O   . TYR A 1 246 ? -52.438  28.042 12.463  1.00 109.18 ?  246 TYR A O   1 
ATOM 2043 C CB  . TYR A 1 246 ? -49.556  27.659 14.388  1.00 88.06  ?  246 TYR A CB  1 
ATOM 2044 C CG  . TYR A 1 246 ? -48.601  26.689 15.052  1.00 98.32  ?  246 TYR A CG  1 
ATOM 2045 C CD1 . TYR A 1 246 ? -49.053  25.759 15.980  1.00 99.90  ?  246 TYR A CD1 1 
ATOM 2046 C CD2 . TYR A 1 246 ? -47.244  26.712 14.759  1.00 111.93 ?  246 TYR A CD2 1 
ATOM 2047 C CE1 . TYR A 1 246 ? -48.183  24.874 16.591  1.00 107.43 ?  246 TYR A CE1 1 
ATOM 2048 C CE2 . TYR A 1 246 ? -46.365  25.834 15.366  1.00 111.32 ?  246 TYR A CE2 1 
ATOM 2049 C CZ  . TYR A 1 246 ? -46.840  24.917 16.280  1.00 105.43 ?  246 TYR A CZ  1 
ATOM 2050 O OH  . TYR A 1 246 ? -45.968  24.040 16.884  1.00 94.96  ?  246 TYR A OH  1 
ATOM 2051 N N   . ALA A 1 247 ? -52.010  29.267 14.307  1.00 80.51  ?  247 ALA A N   1 
ATOM 2052 C CA  . ALA A 1 247 ? -52.760  30.442 13.862  1.00 79.18  ?  247 ALA A CA  1 
ATOM 2053 C C   . ALA A 1 247 ? -51.765  31.419 13.247  1.00 92.33  ?  247 ALA A C   1 
ATOM 2054 O O   . ALA A 1 247 ? -51.268  32.335 13.905  1.00 78.44  ?  247 ALA A O   1 
ATOM 2055 C CB  . ALA A 1 247 ? -53.529  31.067 15.019  1.00 86.32  ?  247 ALA A CB  1 
ATOM 2056 N N   . ARG A 1 248 ? -51.471  31.221 11.964  1.00 94.32  ?  248 ARG A N   1 
ATOM 2057 C CA  . ARG A 1 248 ? -50.453  31.999 11.272  1.00 81.25  ?  248 ARG A CA  1 
ATOM 2058 C C   . ARG A 1 248 ? -51.086  33.190 10.565  1.00 81.81  ?  248 ARG A C   1 
ATOM 2059 O O   . ARG A 1 248 ? -52.109  33.047 9.888   1.00 89.57  ?  248 ARG A O   1 
ATOM 2060 C CB  . ARG A 1 248 ? -49.704  31.123 10.269  1.00 62.34  ?  248 ARG A CB  1 
ATOM 2061 C CG  . ARG A 1 248 ? -48.412  30.549 10.817  1.00 92.53  ?  248 ARG A CG  1 
ATOM 2062 C CD  . ARG A 1 248 ? -48.479  29.036 10.869  1.00 96.36  ?  248 ARG A CD  1 
ATOM 2063 N NE  . ARG A 1 248 ? -48.128  28.415 9.598   1.00 97.88  ?  248 ARG A NE  1 
ATOM 2064 C CZ  . ARG A 1 248 ? -47.954  27.108 9.439   1.00 118.22 ?  248 ARG A CZ  1 
ATOM 2065 N NH1 . ARG A 1 248 ? -48.105  26.293 10.472  1.00 111.60 ?  248 ARG A NH1 1 
ATOM 2066 N NH2 . ARG A 1 248 ? -47.635  26.614 8.252   1.00 131.02 ?  248 ARG A NH2 1 
ATOM 2067 N N   . PHE A 1 249 ? -50.469  34.357 10.718  1.00 83.20  ?  249 PHE A N   1 
ATOM 2068 C CA  . PHE A 1 249 ? -50.968  35.597 10.148  1.00 69.78  ?  249 PHE A CA  1 
ATOM 2069 C C   . PHE A 1 249 ? -50.004  36.107 9.086   1.00 80.82  ?  249 PHE A C   1 
ATOM 2070 O O   . PHE A 1 249 ? -48.802  35.830 9.130   1.00 94.37  ?  249 PHE A O   1 
ATOM 2071 C CB  . PHE A 1 249 ? -51.159  36.665 11.231  1.00 61.59  ?  249 PHE A CB  1 
ATOM 2072 C CG  . PHE A 1 249 ? -52.201  36.310 12.253  1.00 90.20  ?  249 PHE A CG  1 
ATOM 2073 C CD1 . PHE A 1 249 ? -53.458  36.888 12.211  1.00 96.30  ?  249 PHE A CD1 1 
ATOM 2074 C CD2 . PHE A 1 249 ? -51.919  35.404 13.263  1.00 82.06  ?  249 PHE A CD2 1 
ATOM 2075 C CE1 . PHE A 1 249 ? -54.417  36.563 13.152  1.00 96.92  ?  249 PHE A CE1 1 
ATOM 2076 C CE2 . PHE A 1 249 ? -52.873  35.074 14.205  1.00 73.64  ?  249 PHE A CE2 1 
ATOM 2077 C CZ  . PHE A 1 249 ? -54.124  35.655 14.151  1.00 75.73  ?  249 PHE A CZ  1 
ATOM 2078 N N   . PHE A 1 250 ? -50.545  36.858 8.125   1.00 79.51  ?  250 PHE A N   1 
ATOM 2079 C CA  . PHE A 1 250 ? -49.759  37.402 7.014   1.00 70.83  ?  250 PHE A CA  1 
ATOM 2080 C C   . PHE A 1 250 ? -50.227  38.835 6.767   1.00 75.95  ?  250 PHE A C   1 
ATOM 2081 O O   . PHE A 1 250 ? -51.186  39.067 6.027   1.00 87.03  ?  250 PHE A O   1 
ATOM 2082 C CB  . PHE A 1 250 ? -49.896  36.541 5.766   1.00 53.94  ?  250 PHE A CB  1 
ATOM 2083 C CG  . PHE A 1 250 ? -49.165  35.233 5.849   1.00 68.02  ?  250 PHE A CG  1 
ATOM 2084 C CD1 . PHE A 1 250 ? -47.892  35.102 5.321   1.00 82.42  ?  250 PHE A CD1 1 
ATOM 2085 C CD2 . PHE A 1 250 ? -49.754  34.133 6.449   1.00 73.39  ?  250 PHE A CD2 1 
ATOM 2086 C CE1 . PHE A 1 250 ? -47.217  33.899 5.395   1.00 85.61  ?  250 PHE A CE1 1 
ATOM 2087 C CE2 . PHE A 1 250 ? -49.084  32.928 6.527   1.00 86.55  ?  250 PHE A CE2 1 
ATOM 2088 C CZ  . PHE A 1 250 ? -47.814  32.812 6.000   1.00 82.83  ?  250 PHE A CZ  1 
ATOM 2089 N N   . ILE A 1 251 ? -49.541  39.788 7.386   1.00 71.92  ?  251 ILE A N   1 
ATOM 2090 C CA  . ILE A 1 251 ? -49.838  41.204 7.207   1.00 73.83  ?  251 ILE A CA  1 
ATOM 2091 C C   . ILE A 1 251 ? -49.071  41.711 5.995   1.00 88.31  ?  251 ILE A C   1 
ATOM 2092 O O   . ILE A 1 251 ? -47.872  41.443 5.848   1.00 90.51  ?  251 ILE A O   1 
ATOM 2093 C CB  . ILE A 1 251 ? -49.480  42.004 8.469   1.00 80.81  ?  251 ILE A CB  1 
ATOM 2094 C CG1 . ILE A 1 251 ? -50.074  41.323 9.703   1.00 83.17  ?  251 ILE A CG1 1 
ATOM 2095 C CG2 . ILE A 1 251 ? -49.976  43.436 8.351   1.00 75.16  ?  251 ILE A CG2 1 
ATOM 2096 C CD1 . ILE A 1 251 ? -49.878  42.096 10.981  1.00 92.10  ?  251 ILE A CD1 1 
ATOM 2097 N N   . LEU A 1 252 ? -49.760  42.444 5.125   1.00 91.47  ?  252 LEU A N   1 
ATOM 2098 C CA  . LEU A 1 252 ? -49.196  42.855 3.847   1.00 74.49  ?  252 LEU A CA  1 
ATOM 2099 C C   . LEU A 1 252 ? -49.511  44.319 3.590   1.00 88.91  ?  252 LEU A C   1 
ATOM 2100 O O   . LEU A 1 252 ? -50.658  44.746 3.745   1.00 95.71  ?  252 LEU A O   1 
ATOM 2101 C CB  . LEU A 1 252 ? -49.751  41.998 2.703   1.00 68.65  ?  252 LEU A CB  1 
ATOM 2102 C CG  . LEU A 1 252 ? -49.506  40.489 2.753   1.00 90.72  ?  252 LEU A CG  1 
ATOM 2103 C CD1 . LEU A 1 252 ? -50.392  39.771 1.749   1.00 94.87  ?  252 LEU A CD1 1 
ATOM 2104 C CD2 . LEU A 1 252 ? -48.047  40.179 2.482   1.00 95.21  ?  252 LEU A CD2 1 
ATOM 2105 N N   . GLU A 1 253 ? -48.493  45.084 3.204   1.00 91.64  ?  253 GLU A N   1 
ATOM 2106 C CA  . GLU A 1 253 ? -48.697  46.437 2.708   1.00 99.01  ?  253 GLU A CA  1 
ATOM 2107 C C   . GLU A 1 253 ? -48.791  46.411 1.190   1.00 116.62 ?  253 GLU A C   1 
ATOM 2108 O O   . GLU A 1 253 ? -47.955  45.799 0.518   1.00 119.51 ?  253 GLU A O   1 
ATOM 2109 C CB  . GLU A 1 253 ? -47.568  47.372 3.145   1.00 95.57  ?  253 GLU A CB  1 
ATOM 2110 C CG  . GLU A 1 253 ? -47.348  48.536 2.181   1.00 103.26 ?  253 GLU A CG  1 
ATOM 2111 C CD  . GLU A 1 253 ? -46.629  49.711 2.810   1.00 110.27 ?  253 GLU A CD  1 
ATOM 2112 O OE1 . GLU A 1 253 ? -47.139  50.256 3.811   1.00 110.30 ?  253 GLU A OE1 1 
ATOM 2113 O OE2 . GLU A 1 253 ? -45.556  50.094 2.299   1.00 115.47 -1 253 GLU A OE2 1 
ATOM 2114 N N   . PHE A 1 254 ? -49.813  47.072 0.656   1.00 110.19 ?  254 PHE A N   1 
ATOM 2115 C CA  . PHE A 1 254 ? -49.933  47.266 -0.780  1.00 111.32 ?  254 PHE A CA  1 
ATOM 2116 C C   . PHE A 1 254 ? -50.581  48.622 -1.013  1.00 116.79 ?  254 PHE A C   1 
ATOM 2117 O O   . PHE A 1 254 ? -51.618  48.931 -0.418  1.00 104.65 ?  254 PHE A O   1 
ATOM 2118 C CB  . PHE A 1 254 ? -50.728  46.122 -1.435  1.00 112.03 ?  254 PHE A CB  1 
ATOM 2119 C CG  . PHE A 1 254 ? -52.180  46.431 -1.677  1.00 105.83 ?  254 PHE A CG  1 
ATOM 2120 C CD1 . PHE A 1 254 ? -53.110  46.294 -0.659  1.00 108.91 ?  254 PHE A CD1 1 
ATOM 2121 C CD2 . PHE A 1 254 ? -52.617  46.840 -2.927  1.00 103.15 ?  254 PHE A CD2 1 
ATOM 2122 C CE1 . PHE A 1 254 ? -54.445  46.572 -0.879  1.00 121.58 ?  254 PHE A CE1 1 
ATOM 2123 C CE2 . PHE A 1 254 ? -53.952  47.119 -3.153  1.00 114.22 ?  254 PHE A CE2 1 
ATOM 2124 C CZ  . PHE A 1 254 ? -54.867  46.984 -2.128  1.00 117.01 ?  254 PHE A CZ  1 
ATOM 2125 N N   . GLN A 1 255 ? -49.941  49.443 -1.838  1.00 121.50 ?  255 GLN A N   1 
ATOM 2126 C CA  . GLN A 1 255 ? -50.421  50.788 -2.099  1.00 120.24 ?  255 GLN A CA  1 
ATOM 2127 C C   . GLN A 1 255 ? -51.376  50.785 -3.290  1.00 134.79 ?  255 GLN A C   1 
ATOM 2128 O O   . GLN A 1 255 ? -51.586  49.767 -3.951  1.00 126.43 ?  255 GLN A O   1 
ATOM 2129 C CB  . GLN A 1 255 ? -49.247  51.736 -2.347  1.00 115.34 ?  255 GLN A CB  1 
ATOM 2130 C CG  . GLN A 1 255 ? -49.071  52.799 -1.272  1.00 110.77 ?  255 GLN A CG  1 
ATOM 2131 C CD  . GLN A 1 255 ? -50.155  53.860 -1.311  1.00 134.32 ?  255 GLN A CD  1 
ATOM 2132 O OE1 . GLN A 1 255 ? -50.896  53.975 -2.288  1.00 129.53 ?  255 GLN A OE1 1 
ATOM 2133 N NE2 . GLN A 1 255 ? -50.249  54.647 -0.245  1.00 135.01 ?  255 GLN A NE2 1 
ATOM 2134 N N   . ASP A 1 256 ? -51.960  51.955 -3.560  1.00 141.47 ?  256 ASP A N   1 
ATOM 2135 C CA  . ASP A 1 256 ? -52.906  52.083 -4.663  1.00 139.51 ?  256 ASP A CA  1 
ATOM 2136 C C   . ASP A 1 256 ? -52.253  51.834 -6.016  1.00 135.51 ?  256 ASP A C   1 
ATOM 2137 O O   . ASP A 1 256 ? -52.948  51.463 -6.969  1.00 153.48 ?  256 ASP A O   1 
ATOM 2138 C CB  . ASP A 1 256 ? -53.555  53.469 -4.637  1.00 132.89 ?  256 ASP A CB  1 
ATOM 2139 C CG  . ASP A 1 256 ? -54.456  53.668 -3.430  1.00 130.12 ?  256 ASP A CG  1 
ATOM 2140 O OD1 . ASP A 1 256 ? -54.986  52.663 -2.913  1.00 121.48 ?  256 ASP A OD1 1 
ATOM 2141 O OD2 . ASP A 1 256 ? -54.629  54.825 -2.997  1.00 127.79 -1 256 ASP A OD2 1 
ATOM 2142 N N   . LYS A 1 257 ? -50.936  52.027 -6.122  1.00 120.22 ?  257 LYS A N   1 
ATOM 2143 C CA  . LYS A 1 257 ? -50.237  51.771 -7.377  1.00 123.84 ?  257 LYS A CA  1 
ATOM 2144 C C   . LYS A 1 257 ? -50.164  50.286 -7.712  1.00 126.25 ?  257 LYS A C   1 
ATOM 2145 O O   . LYS A 1 257 ? -49.926  49.936 -8.874  1.00 131.83 ?  257 LYS A O   1 
ATOM 2146 C CB  . LYS A 1 257 ? -48.824  52.347 -7.313  1.00 126.84 ?  257 LYS A CB  1 
ATOM 2147 C CG  . LYS A 1 257 ? -47.926  51.635 -6.310  1.00 120.60 ?  257 LYS A CG  1 
ATOM 2148 C CD  . LYS A 1 257 ? -46.570  52.309 -6.175  1.00 125.07 ?  257 LYS A CD  1 
ATOM 2149 C CE  . LYS A 1 257 ? -45.707  51.594 -5.145  1.00 114.11 ?  257 LYS A CE  1 
ATOM 2150 N NZ  . LYS A 1 257 ? -44.432  52.316 -4.882  1.00 119.67 ?  257 LYS A NZ  1 
ATOM 2151 N N   . THR A 1 258 ? -50.360  49.410 -6.730  1.00 116.40 ?  258 THR A N   1 
ATOM 2152 C CA  . THR A 1 258 ? -50.164  47.984 -6.946  1.00 109.76 ?  258 THR A CA  1 
ATOM 2153 C C   . THR A 1 258 ? -51.310  47.392 -7.757  1.00 118.83 ?  258 THR A C   1 
ATOM 2154 O O   . THR A 1 258 ? -52.468  47.796 -7.618  1.00 116.85 ?  258 THR A O   1 
ATOM 2155 C CB  . THR A 1 258 ? -50.042  47.260 -5.605  1.00 99.38  ?  258 THR A CB  1 
ATOM 2156 O OG1 . THR A 1 258 ? -49.312  48.080 -4.684  1.00 111.35 ?  258 THR A OG1 1 
ATOM 2157 C CG2 . THR A 1 258 ? -49.315  45.935 -5.777  1.00 96.37  ?  258 THR A CG2 1 
ATOM 2158 N N   . ASP A 1 259 ? -50.977  46.429 -8.612  1.00 123.47 ?  259 ASP A N   1 
ATOM 2159 C CA  . ASP A 1 259 ? -51.975  45.729 -9.405  1.00 121.57 ?  259 ASP A CA  1 
ATOM 2160 C C   . ASP A 1 259 ? -52.705  44.703 -8.546  1.00 109.28 ?  259 ASP A C   1 
ATOM 2161 O O   . ASP A 1 259 ? -52.130  44.100 -7.635  1.00 110.50 ?  259 ASP A O   1 
ATOM 2162 C CB  . ASP A 1 259 ? -51.318  45.046 -10.608 1.00 125.54 ?  259 ASP A CB  1 
ATOM 2163 C CG  . ASP A 1 259 ? -52.327  44.535 -11.626 1.00 127.68 ?  259 ASP A CG  1 
ATOM 2164 O OD1 . ASP A 1 259 ? -53.260  43.797 -11.244 1.00 124.81 ?  259 ASP A OD1 1 
ATOM 2165 O OD2 . ASP A 1 259 ? -52.182  44.872 -12.819 1.00 137.05 -1 259 ASP A OD2 1 
ATOM 2166 N N   . ILE A 1 260 ? -53.988  44.507 -8.848  1.00 110.63 ?  260 ILE A N   1 
ATOM 2167 C CA  . ILE A 1 260 ? -54.794  43.570 -8.072  1.00 97.08  ?  260 ILE A CA  1 
ATOM 2168 C C   . ILE A 1 260 ? -54.550  42.137 -8.525  1.00 92.80  ?  260 ILE A C   1 
ATOM 2169 O O   . ILE A 1 260 ? -54.428  41.227 -7.698  1.00 91.12  ?  260 ILE A O   1 
ATOM 2170 C CB  . ILE A 1 260 ? -56.283  43.951 -8.161  1.00 106.37 ?  260 ILE A CB  1 
ATOM 2171 C CG1 . ILE A 1 260 ? -56.498  45.372 -7.634  1.00 104.91 ?  260 ILE A CG1 1 
ATOM 2172 C CG2 . ILE A 1 260 ? -57.139  42.957 -7.390  1.00 77.21  ?  260 ILE A CG2 1 
ATOM 2173 C CD1 . ILE A 1 260 ? -57.942  45.823 -7.664  1.00 108.37 ?  260 ILE A CD1 1 
ATOM 2174 N N   . LYS A 1 261 ? -54.471  41.910 -9.840  1.00 101.68 ?  261 LYS A N   1 
ATOM 2175 C CA  . LYS A 1 261 ? -54.200  40.570 -10.349 1.00 100.77 ?  261 LYS A CA  1 
ATOM 2176 C C   . LYS A 1 261 ? -52.846  40.046 -9.887  1.00 96.49  ?  261 LYS A C   1 
ATOM 2177 O O   . LYS A 1 261 ? -52.645  38.827 -9.840  1.00 103.65 ?  261 LYS A O   1 
ATOM 2178 C CB  . LYS A 1 261 ? -54.280  40.567 -11.878 1.00 109.68 ?  261 LYS A CB  1 
ATOM 2179 C CG  . LYS A 1 261 ? -54.308  39.180 -12.504 1.00 94.70  ?  261 LYS A CG  1 
ATOM 2180 C CD  . LYS A 1 261 ? -54.650  39.245 -13.984 1.00 107.90 ?  261 LYS A CD  1 
ATOM 2181 C CE  . LYS A 1 261 ? -54.784  37.851 -14.577 1.00 119.28 ?  261 LYS A CE  1 
ATOM 2182 N NZ  . LYS A 1 261 ? -55.232  37.888 -15.997 1.00 94.93  ?  261 LYS A NZ  1 
ATOM 2183 N N   . THR A 1 262 ? -51.916  40.939 -9.540  1.00 103.88 ?  262 THR A N   1 
ATOM 2184 C CA  . THR A 1 262 ? -50.649  40.517 -8.955  1.00 105.16 ?  262 THR A CA  1 
ATOM 2185 C C   . THR A 1 262 ? -50.819  40.114 -7.495  1.00 98.82  ?  262 THR A C   1 
ATOM 2186 O O   . THR A 1 262 ? -50.249  39.110 -7.053  1.00 97.39  ?  262 THR A O   1 
ATOM 2187 C CB  . THR A 1 262 ? -49.615  41.638 -9.082  1.00 98.75  ?  262 THR A CB  1 
ATOM 2188 O OG1 . THR A 1 262 ? -49.339  41.885 -10.467 1.00 106.08 ?  262 THR A OG1 1 
ATOM 2189 C CG2 . THR A 1 262 ? -48.321  41.261 -8.373  1.00 105.74 ?  262 THR A CG2 1 
ATOM 2190 N N   . VAL A 1 263 ? -51.604  40.884 -6.736  1.00 103.20 ?  263 VAL A N   1 
ATOM 2191 C CA  . VAL A 1 263 ? -51.820  40.580 -5.324  1.00 89.28  ?  263 VAL A CA  1 
ATOM 2192 C C   . VAL A 1 263 ? -52.543  39.248 -5.165  1.00 86.61  ?  263 VAL A C   1 
ATOM 2193 O O   . VAL A 1 263 ? -52.259  38.477 -4.239  1.00 99.33  ?  263 VAL A O   1 
ATOM 2194 C CB  . VAL A 1 263 ? -52.590  41.730 -4.646  1.00 74.47  ?  263 VAL A CB  1 
ATOM 2195 C CG1 . VAL A 1 263 ? -53.050  41.325 -3.254  1.00 82.37  ?  263 VAL A CG1 1 
ATOM 2196 C CG2 . VAL A 1 263 ? -51.727  42.979 -4.582  1.00 82.51  ?  263 VAL A CG2 1 
ATOM 2197 N N   . LYS A 1 264 ? -53.483  38.953 -6.067  1.00 79.52  ?  264 LYS A N   1 
ATOM 2198 C CA  . LYS A 1 264 ? -54.256  37.719 -5.962  1.00 79.26  ?  264 LYS A CA  1 
ATOM 2199 C C   . LYS A 1 264 ? -53.355  36.494 -6.054  1.00 94.86  ?  264 LYS A C   1 
ATOM 2200 O O   . LYS A 1 264 ? -53.399  35.612 -5.188  1.00 94.87  ?  264 LYS A O   1 
ATOM 2201 C CB  . LYS A 1 264 ? -55.334  37.681 -7.045  1.00 92.35  ?  264 LYS A CB  1 
ATOM 2202 C CG  . LYS A 1 264 ? -56.422  38.726 -6.869  1.00 100.22 ?  264 LYS A CG  1 
ATOM 2203 C CD  . LYS A 1 264 ? -57.165  38.988 -8.168  1.00 93.61  ?  264 LYS A CD  1 
ATOM 2204 C CE  . LYS A 1 264 ? -57.739  37.704 -8.743  1.00 95.41  ?  264 LYS A CE  1 
ATOM 2205 N NZ  . LYS A 1 264 ? -58.515  37.948 -9.990  1.00 96.25  ?  264 LYS A NZ  1 
ATOM 2206 N N   . ASP A 1 265 ? -52.518  36.429 -7.093  1.00 100.28 ?  265 ASP A N   1 
ATOM 2207 C CA  . ASP A 1 265 ? -51.634  35.281 -7.272  1.00 100.67 ?  265 ASP A CA  1 
ATOM 2208 C C   . ASP A 1 265 ? -50.669  35.103 -6.106  1.00 97.56  ?  265 ASP A C   1 
ATOM 2209 O O   . ASP A 1 265 ? -50.096  34.020 -5.950  1.00 96.81  ?  265 ASP A O   1 
ATOM 2210 C CB  . ASP A 1 265 ? -50.859  35.417 -8.583  1.00 100.64 ?  265 ASP A CB  1 
ATOM 2211 C CG  . ASP A 1 265 ? -51.751  35.283 -9.802  1.00 111.14 ?  265 ASP A CG  1 
ATOM 2212 O OD1 . ASP A 1 265 ? -52.713  34.488 -9.750  1.00 116.04 ?  265 ASP A OD1 1 
ATOM 2213 O OD2 . ASP A 1 265 ? -51.490  35.971 -10.811 1.00 124.69 -1 265 ASP A OD2 1 
ATOM 2214 N N   . CYS A 1 266 ? -50.475  36.139 -5.288  1.00 90.42  ?  266 CYS A N   1 
ATOM 2215 C CA  . CYS A 1 266 ? -49.718  35.978 -4.052  1.00 99.94  ?  266 CYS A CA  1 
ATOM 2216 C C   . CYS A 1 266 ? -50.555  35.290 -2.980  1.00 98.73  ?  266 CYS A C   1 
ATOM 2217 O O   . CYS A 1 266 ? -50.043  34.449 -2.233  1.00 90.14  ?  266 CYS A O   1 
ATOM 2218 C CB  . CYS A 1 266 ? -49.227  37.338 -3.556  1.00 95.74  ?  266 CYS A CB  1 
ATOM 2219 S SG  . CYS A 1 266 ? -48.410  37.298 -1.943  1.00 87.95  ?  266 CYS A SG  1 
ATOM 2220 N N   . ILE A 1 267 ? -51.842  35.634 -2.897  1.00 93.43  ?  267 ILE A N   1 
ATOM 2221 C CA  . ILE A 1 267 ? -52.721  35.027 -1.903  1.00 86.81  ?  267 ILE A CA  1 
ATOM 2222 C C   . ILE A 1 267 ? -52.920  33.544 -2.195  1.00 93.28  ?  267 ILE A C   1 
ATOM 2223 O O   . ILE A 1 267 ? -53.025  32.725 -1.273  1.00 108.42 ?  267 ILE A O   1 
ATOM 2224 C CB  . ILE A 1 267 ? -54.060  35.786 -1.851  1.00 85.53  ?  267 ILE A CB  1 
ATOM 2225 C CG1 . ILE A 1 267 ? -53.825  37.241 -1.439  1.00 74.53  ?  267 ILE A CG1 1 
ATOM 2226 C CG2 . ILE A 1 267 ? -55.034  35.108 -0.899  1.00 84.64  ?  267 ILE A CG2 1 
ATOM 2227 C CD1 . ILE A 1 267 ? -55.083  38.078 -1.400  1.00 70.69  ?  267 ILE A CD1 1 
ATOM 2228 N N   . TYR A 1 268 ? -52.970  33.172 -3.478  1.00 84.49  ?  268 TYR A N   1 
ATOM 2229 C CA  . TYR A 1 268 ? -53.093  31.760 -3.831  1.00 100.80 ?  268 TYR A CA  1 
ATOM 2230 C C   . TYR A 1 268 ? -51.880  30.966 -3.362  1.00 109.27 ?  268 TYR A C   1 
ATOM 2231 O O   . TYR A 1 268 ? -52.011  29.812 -2.936  1.00 122.05 ?  268 TYR A O   1 
ATOM 2232 C CB  . TYR A 1 268 ? -53.277  31.604 -5.341  1.00 106.67 ?  268 TYR A CB  1 
ATOM 2233 C CG  . TYR A 1 268 ? -54.659  31.955 -5.843  1.00 83.35  ?  268 TYR A CG  1 
ATOM 2234 C CD1 . TYR A 1 268 ? -55.642  30.982 -5.969  1.00 83.88  ?  268 TYR A CD1 1 
ATOM 2235 C CD2 . TYR A 1 268 ? -54.977  33.257 -6.201  1.00 91.41  ?  268 TYR A CD2 1 
ATOM 2236 C CE1 . TYR A 1 268 ? -56.906  31.300 -6.432  1.00 97.75  ?  268 TYR A CE1 1 
ATOM 2237 C CE2 . TYR A 1 268 ? -56.236  33.585 -6.664  1.00 99.87  ?  268 TYR A CE2 1 
ATOM 2238 C CZ  . TYR A 1 268 ? -57.197  32.603 -6.778  1.00 97.98  ?  268 TYR A CZ  1 
ATOM 2239 O OH  . TYR A 1 268 ? -58.452  32.928 -7.239  1.00 100.06 ?  268 TYR A OH  1 
ATOM 2240 N N   . LYS A 1 269 ? -50.689  31.567 -3.434  1.00 103.48 ?  269 LYS A N   1 
ATOM 2241 C CA  . LYS A 1 269 ? -49.480  30.865 -3.016  1.00 118.66 ?  269 LYS A CA  1 
ATOM 2242 C C   . LYS A 1 269 ? -49.459  30.623 -1.512  1.00 117.74 ?  269 LYS A C   1 
ATOM 2243 O O   . LYS A 1 269 ? -48.915  29.610 -1.057  1.00 117.86 ?  269 LYS A O   1 
ATOM 2244 C CB  . LYS A 1 269 ? -48.241  31.652 -3.446  1.00 115.43 ?  269 LYS A CB  1 
ATOM 2245 C CG  . LYS A 1 269 ? -46.952  30.845 -3.424  1.00 112.90 ?  269 LYS A CG  1 
ATOM 2246 C CD  . LYS A 1 269 ? -46.965  29.751 -4.481  1.00 123.20 ?  269 LYS A CD  1 
ATOM 2247 C CE  . LYS A 1 269 ? -45.662  28.966 -4.482  1.00 127.81 ?  269 LYS A CE  1 
ATOM 2248 N NZ  . LYS A 1 269 ? -45.652  27.901 -5.524  1.00 96.12  ?  269 LYS A NZ  1 
ATOM 2249 N N   . ILE A 1 270 ? -50.040  31.531 -0.728  1.00 112.11 ?  270 ILE A N   1 
ATOM 2250 C CA  . ILE A 1 270 ? -50.092  31.339 0.719   1.00 93.15  ?  270 ILE A CA  1 
ATOM 2251 C C   . ILE A 1 270 ? -51.017  30.180 1.067   1.00 100.56 ?  270 ILE A C   1 
ATOM 2252 O O   . ILE A 1 270 ? -50.673  29.311 1.877   1.00 113.52 ?  270 ILE A O   1 
ATOM 2253 C CB  . ILE A 1 270 ? -50.530  32.638 1.418   1.00 96.09  ?  270 ILE A CB  1 
ATOM 2254 C CG1 . ILE A 1 270 ? -49.680  33.815 0.939   1.00 82.99  ?  270 ILE A CG1 1 
ATOM 2255 C CG2 . ILE A 1 270 ? -50.435  32.486 2.929   1.00 104.17 ?  270 ILE A CG2 1 
ATOM 2256 C CD1 . ILE A 1 270 ? -50.083  35.142 1.540   1.00 77.99  ?  270 ILE A CD1 1 
ATOM 2257 N N   . GLN A 1 271 ? -52.208  30.154 0.464   1.00 94.15  ?  271 GLN A N   1 
ATOM 2258 C CA  . GLN A 1 271 ? -53.149  29.070 0.728   1.00 98.67  ?  271 GLN A CA  1 
ATOM 2259 C C   . GLN A 1 271 ? -52.602  27.732 0.243   1.00 115.69 ?  271 GLN A C   1 
ATOM 2260 O O   . GLN A 1 271 ? -52.816  26.697 0.883   1.00 106.35 ?  271 GLN A O   1 
ATOM 2261 C CB  . GLN A 1 271 ? -54.497  29.382 0.072   1.00 92.68  ?  271 GLN A CB  1 
ATOM 2262 C CG  . GLN A 1 271 ? -55.410  28.180 -0.129  1.00 114.51 ?  271 GLN A CG  1 
ATOM 2263 C CD  . GLN A 1 271 ? -55.232  27.525 -1.487  1.00 140.44 ?  271 GLN A CD  1 
ATOM 2264 O OE1 . GLN A 1 271 ? -54.381  27.932 -2.278  1.00 134.75 ?  271 GLN A OE1 1 
ATOM 2265 N NE2 . GLN A 1 271 ? -56.032  26.501 -1.760  1.00 136.36 ?  271 GLN A NE2 1 
ATOM 2266 N N   . SER A 1 272 ? -51.890  27.732 -0.886  1.00 114.43 ?  272 SER A N   1 
ATOM 2267 C CA  . SER A 1 272 ? -51.357  26.482 -1.418  1.00 115.95 ?  272 SER A CA  1 
ATOM 2268 C C   . SER A 1 272 ? -50.286  25.899 -0.504  1.00 118.46 ?  272 SER A C   1 
ATOM 2269 O O   . SER A 1 272 ? -50.238  24.682 -0.291  1.00 126.87 ?  272 SER A O   1 
ATOM 2270 C CB  . SER A 1 272 ? -50.799  26.704 -2.823  1.00 118.78 ?  272 SER A CB  1 
ATOM 2271 O OG  . SER A 1 272 ? -49.662  27.548 -2.789  1.00 124.20 ?  272 SER A OG  1 
ATOM 2272 N N   . ASN A 1 273 ? -49.421  26.749 0.049   1.00 121.09 ?  273 ASN A N   1 
ATOM 2273 C CA  . ASN A 1 273 ? -48.336  26.286 0.906   1.00 126.26 ?  273 ASN A CA  1 
ATOM 2274 C C   . ASN A 1 273 ? -48.760  26.165 2.367   1.00 117.64 ?  273 ASN A C   1 
ATOM 2275 O O   . ASN A 1 273 ? -48.575  25.110 2.982   1.00 121.13 ?  273 ASN A O   1 
ATOM 2276 C CB  . ASN A 1 273 ? -47.131  27.226 0.784   1.00 123.39 ?  273 ASN A CB  1 
ATOM 2277 C CG  . ASN A 1 273 ? -46.573  27.281 -0.625  1.00 117.49 ?  273 ASN A CG  1 
ATOM 2278 O OD1 . ASN A 1 273 ? -46.385  28.358 -1.190  1.00 123.65 ?  273 ASN A OD1 1 
ATOM 2279 N ND2 . ASN A 1 273 ? -46.304  26.114 -1.200  1.00 123.38 ?  273 ASN A ND2 1 
ATOM 2280 N N   . TRP A 1 274 ? -49.320  27.230 2.937   1.00 114.76 ?  274 TRP A N   1 
ATOM 2281 C CA  . TRP A 1 274 ? -49.645  27.260 4.363   1.00 115.03 ?  274 TRP A CA  1 
ATOM 2282 C C   . TRP A 1 274 ? -51.124  26.938 4.579   1.00 116.58 ?  274 TRP A C   1 
ATOM 2283 O O   . TRP A 1 274 ? -51.922  27.768 5.018   1.00 105.50 ?  274 TRP A O   1 
ATOM 2284 C CB  . TRP A 1 274 ? -49.269  28.612 4.960   1.00 108.26 ?  274 TRP A CB  1 
ATOM 2285 C CG  . TRP A 1 274 ? -47.873  29.049 4.628   1.00 119.92 ?  274 TRP A CG  1 
ATOM 2286 C CD1 . TRP A 1 274 ? -47.504  30.217 4.031   1.00 111.01 ?  274 TRP A CD1 1 
ATOM 2287 C CD2 . TRP A 1 274 ? -46.659  28.325 4.877   1.00 137.59 ?  274 TRP A CD2 1 
ATOM 2288 N NE1 . TRP A 1 274 ? -46.138  30.268 3.892   1.00 121.13 ?  274 TRP A NE1 1 
ATOM 2289 C CE2 . TRP A 1 274 ? -45.597  29.118 4.402   1.00 131.92 ?  274 TRP A CE2 1 
ATOM 2290 C CE3 . TRP A 1 274 ? -46.369  27.083 5.452   1.00 137.70 ?  274 TRP A CE3 1 
ATOM 2291 C CZ2 . TRP A 1 274 ? -44.267  28.711 4.486   1.00 125.32 ?  274 TRP A CZ2 1 
ATOM 2292 C CZ3 . TRP A 1 274 ? -45.047  26.682 5.535   1.00 128.17 ?  274 TRP A CZ3 1 
ATOM 2293 C CH2 . TRP A 1 274 ? -44.013  27.493 5.054   1.00 128.79 ?  274 TRP A CH2 1 
ATOM 2294 N N   . SER A 1 275 ? -51.475  25.693 4.263   1.00 115.35 ?  275 SER A N   1 
ATOM 2295 C CA  . SER A 1 275 ? -52.806  25.156 4.515   1.00 102.75 ?  275 SER A CA  1 
ATOM 2296 C C   . SER A 1 275 ? -52.771  23.652 4.303   1.00 113.32 ?  275 SER A C   1 
ATOM 2297 O O   . SER A 1 275 ? -51.962  23.144 3.521   1.00 126.41 ?  275 SER A O   1 
ATOM 2298 C CB  . SER A 1 275 ? -53.870  25.778 3.601   1.00 114.46 ?  275 SER A CB  1 
ATOM 2299 O OG  . SER A 1 275 ? -53.953  27.180 3.769   1.00 115.32 ?  275 SER A OG  1 
ATOM 2300 N N   . ASN A 1 276 ? -53.654  22.948 5.011   1.00 111.80 ?  276 ASN A N   1 
ATOM 2301 C CA  . ASN A 1 276 ? -53.885  21.527 4.748   1.00 118.88 ?  276 ASN A CA  1 
ATOM 2302 C C   . ASN A 1 276 ? -55.355  21.248 5.065   1.00 119.53 ?  276 ASN A C   1 
ATOM 2303 O O   . ASN A 1 276 ? -55.705  20.907 6.197   1.00 123.28 ?  276 ASN A O   1 
ATOM 2304 C CB  . ASN A 1 276 ? -52.953  20.645 5.566   1.00 123.97 ?  276 ASN A CB  1 
ATOM 2305 C CG  . ASN A 1 276 ? -53.121  19.171 5.252   1.00 130.04 ?  276 ASN A CG  1 
ATOM 2306 O OD1 . ASN A 1 276 ? -53.584  18.802 4.173   1.00 135.15 ?  276 ASN A OD1 1 
ATOM 2307 N ND2 . ASN A 1 276 ? -52.745  18.317 6.198   1.00 147.14 ?  276 ASN A ND2 1 
ATOM 2308 N N   . LEU A 1 277 ? -56.202  21.399 4.053   1.00 124.74 ?  277 LEU A N   1 
ATOM 2309 C CA  . LEU A 1 277 ? -57.623  21.069 4.164   1.00 120.64 ?  277 LEU A CA  1 
ATOM 2310 C C   . LEU A 1 277 ? -57.892  19.689 3.565   1.00 126.77 ?  277 LEU A C   1 
ATOM 2311 O O   . LEU A 1 277 ? -58.700  19.518 2.652   1.00 135.74 ?  277 LEU A O   1 
ATOM 2312 C CB  . LEU A 1 277 ? -58.469  22.147 3.492   1.00 101.70 ?  277 LEU A CB  1 
ATOM 2313 C CG  . LEU A 1 277 ? -58.105  23.600 3.810   1.00 99.87  ?  277 LEU A CG  1 
ATOM 2314 C CD1 . LEU A 1 277 ? -59.079  24.559 3.145   1.00 92.97  ?  277 LEU A CD1 1 
ATOM 2315 C CD2 . LEU A 1 277 ? -58.067  23.837 5.313   1.00 100.10 ?  277 LEU A CD2 1 
ATOM 2316 N N   . SER A 1 278 ? -57.194  18.693 4.101   1.00 144.35 ?  278 SER A N   1 
ATOM 2317 C CA  . SER A 1 278 ? -57.269  17.344 3.562   1.00 135.93 ?  278 SER A CA  1 
ATOM 2318 C C   . SER A 1 278 ? -58.461  16.592 4.139   1.00 142.81 ?  278 SER A C   1 
ATOM 2319 O O   . SER A 1 278 ? -58.848  16.784 5.294   1.00 149.82 ?  278 SER A O   1 
ATOM 2320 C CB  . SER A 1 278 ? -55.981  16.574 3.856   1.00 140.57 ?  278 SER A CB  1 
ATOM 2321 O OG  . SER A 1 278 ? -54.865  17.185 3.232   1.00 144.19 ?  278 SER A OG  1 
ATOM 2322 N N   . LYS A 1 279 ? -59.046  15.723 3.312   1.00 144.17 ?  279 LYS A N   1 
ATOM 2323 C CA  . LYS A 1 279 ? -60.135  14.877 3.788   1.00 147.91 ?  279 LYS A CA  1 
ATOM 2324 C C   . LYS A 1 279 ? -59.619  13.761 4.685   1.00 155.73 ?  279 LYS A C   1 
ATOM 2325 O O   . LYS A 1 279 ? -60.364  13.253 5.531   1.00 157.28 ?  279 LYS A O   1 
ATOM 2326 C CB  . LYS A 1 279 ? -60.903  14.290 2.604   1.00 142.63 ?  279 LYS A CB  1 
ATOM 2327 C CG  . LYS A 1 279 ? -61.272  15.302 1.534   1.00 154.27 ?  279 LYS A CG  1 
ATOM 2328 C CD  . LYS A 1 279 ? -61.865  14.614 0.316   1.00 143.74 ?  279 LYS A CD  1 
ATOM 2329 C CE  . LYS A 1 279 ? -62.105  15.598 -0.817  1.00 134.13 ?  279 LYS A CE  1 
ATOM 2330 N NZ  . LYS A 1 279 ? -62.623  14.918 -2.037  1.00 128.51 ?  279 LYS A NZ  1 
ATOM 2331 N N   . ARG A 1 280 ? -58.354  13.373 4.519   1.00 154.31 ?  280 ARG A N   1 
ATOM 2332 C CA  . ARG A 1 280 ? -57.745  12.296 5.288   1.00 160.31 ?  280 ARG A CA  1 
ATOM 2333 C C   . ARG A 1 280 ? -56.816  12.819 6.381   1.00 155.50 ?  280 ARG A C   1 
ATOM 2334 O O   . ARG A 1 280 ? -55.816  12.173 6.710   1.00 142.04 ?  280 ARG A O   1 
ATOM 2335 C CB  . ARG A 1 280 ? -57.000  11.345 4.352   1.00 155.10 ?  280 ARG A CB  1 
ATOM 2336 C CG  . ARG A 1 280 ? -57.890  10.757 3.265   1.00 142.09 ?  280 ARG A CG  1 
ATOM 2337 C CD  . ARG A 1 280 ? -57.114  9.898  2.281   1.00 134.25 ?  280 ARG A CD  1 
ATOM 2338 N NE  . ARG A 1 280 ? -57.965  9.450  1.181   1.00 149.65 ?  280 ARG A NE  1 
ATOM 2339 C CZ  . ARG A 1 280 ? -57.551  8.689  0.174   1.00 156.31 ?  280 ARG A CZ  1 
ATOM 2340 N NH1 . ARG A 1 280 ? -56.290  8.283  0.118   1.00 151.48 ?  280 ARG A NH1 1 
ATOM 2341 N NH2 . ARG A 1 280 ? -58.401  8.332  -0.781  1.00 145.96 ?  280 ARG A NH2 1 
ATOM 2342 N N   . THR A 1 281 ? -57.130  13.983 6.945   1.00 159.16 ?  281 THR A N   1 
ATOM 2343 C CA  . THR A 1 281 ? -56.396  14.536 8.073   1.00 156.79 ?  281 THR A CA  1 
ATOM 2344 C C   . THR A 1 281 ? -57.381  14.885 9.180   1.00 154.08 ?  281 THR A C   1 
ATOM 2345 O O   . THR A 1 281 ? -58.582  15.044 8.946   1.00 150.08 ?  281 THR A O   1 
ATOM 2346 C CB  . THR A 1 281 ? -55.582  15.779 7.678   1.00 143.73 ?  281 THR A CB  1 
ATOM 2347 O OG1 . THR A 1 281 ? -54.629  16.076 8.705   1.00 136.09 ?  281 THR A OG1 1 
ATOM 2348 C CG2 . THR A 1 281 ? -56.494  16.981 7.489   1.00 138.42 ?  281 THR A CG2 1 
ATOM 2349 N N   . ASP A 1 282 ? -56.858  14.994 10.402  1.00 159.61 ?  282 ASP A N   1 
ATOM 2350 C CA  . ASP A 1 282 ? -57.676  15.309 11.563  1.00 156.10 ?  282 ASP A CA  1 
ATOM 2351 C C   . ASP A 1 282 ? -57.321  16.631 12.226  1.00 158.83 ?  282 ASP A C   1 
ATOM 2352 O O   . ASP A 1 282 ? -58.061  17.072 13.113  1.00 168.26 ?  282 ASP A O   1 
ATOM 2353 C CB  . ASP A 1 282 ? -57.579  14.185 12.608  1.00 164.69 ?  282 ASP A CB  1 
ATOM 2354 C CG  . ASP A 1 282 ? -58.212  12.891 12.134  1.00 176.63 ?  282 ASP A CG  1 
ATOM 2355 O OD1 . ASP A 1 282 ? -58.789  12.879 11.026  1.00 177.53 ?  282 ASP A OD1 1 
ATOM 2356 O OD2 . ASP A 1 282 ? -58.133  11.884 12.869  1.00 170.42 -1 282 ASP A OD2 1 
ATOM 2357 N N   . ARG A 1 283 ? -56.223  17.274 11.830  1.00 159.38 ?  283 ARG A N   1 
ATOM 2358 C CA  . ARG A 1 283 ? -55.806  18.557 12.395  1.00 145.42 ?  283 ARG A CA  1 
ATOM 2359 C C   . ARG A 1 283 ? -55.469  19.497 11.245  1.00 139.63 ?  283 ARG A C   1 
ATOM 2360 O O   . ARG A 1 283 ? -54.312  19.576 10.810  1.00 131.48 ?  283 ARG A O   1 
ATOM 2361 C CB  . ARG A 1 283 ? -54.623  18.384 13.346  1.00 153.91 ?  283 ARG A CB  1 
ATOM 2362 C CG  . ARG A 1 283 ? -54.964  17.619 14.619  1.00 171.30 ?  283 ARG A CG  1 
ATOM 2363 C CD  . ARG A 1 283 ? -53.794  17.583 15.591  1.00 170.40 ?  283 ARG A CD  1 
ATOM 2364 N NE  . ARG A 1 283 ? -54.224  17.235 16.943  1.00 170.98 ?  283 ARG A NE  1 
ATOM 2365 C CZ  . ARG A 1 283 ? -53.408  17.141 17.989  1.00 164.78 ?  283 ARG A CZ  1 
ATOM 2366 N NH1 . ARG A 1 283 ? -52.110  17.368 17.843  1.00 158.37 ?  283 ARG A NH1 1 
ATOM 2367 N NH2 . ARG A 1 283 ? -53.891  16.820 19.181  1.00 157.65 ?  283 ARG A NH2 1 
ATOM 2368 N N   . PRO A 1 284 ? -56.454  20.223 10.727  1.00 127.44 ?  284 PRO A N   1 
ATOM 2369 C CA  . PRO A 1 284 ? -56.219  21.118 9.593   1.00 113.83 ?  284 PRO A CA  1 
ATOM 2370 C C   . PRO A 1 284 ? -55.831  22.522 10.046  1.00 108.32 ?  284 PRO A C   1 
ATOM 2371 O O   . PRO A 1 284 ? -55.887  22.864 11.229  1.00 115.74 ?  284 PRO A O   1 
ATOM 2372 C CB  . PRO A 1 284 ? -57.581  21.130 8.892   1.00 111.66 ?  284 PRO A CB  1 
ATOM 2373 C CG  . PRO A 1 284 ? -58.550  21.021 10.028  1.00 103.27 ?  284 PRO A CG  1 
ATOM 2374 C CD  . PRO A 1 284 ? -57.883  20.155 11.082  1.00 120.70 ?  284 PRO A CD  1 
ATOM 2375 N N   . TYR A 1 285 ? -55.433  23.336 9.068   1.00 107.21 ?  285 TYR A N   1 
ATOM 2376 C CA  . TYR A 1 285 ? -55.079  24.722 9.340   1.00 102.04 ?  285 TYR A CA  1 
ATOM 2377 C C   . TYR A 1 285 ? -55.223  25.540 8.064   1.00 105.45 ?  285 TYR A C   1 
ATOM 2378 O O   . TYR A 1 285 ? -54.996  25.039 6.959   1.00 111.43 ?  285 TYR A O   1 
ATOM 2379 C CB  . TYR A 1 285 ? -53.656  24.846 9.901   1.00 103.89 ?  285 TYR A CB  1 
ATOM 2380 C CG  . TYR A 1 285 ? -52.566  24.244 9.037   1.00 116.94 ?  285 TYR A CG  1 
ATOM 2381 C CD1 . TYR A 1 285 ? -52.227  22.901 9.143   1.00 127.34 ?  285 TYR A CD1 1 
ATOM 2382 C CD2 . TYR A 1 285 ? -51.852  25.028 8.139   1.00 113.86 ?  285 TYR A CD2 1 
ATOM 2383 C CE1 . TYR A 1 285 ? -51.223  22.351 8.366   1.00 130.07 ?  285 TYR A CE1 1 
ATOM 2384 C CE2 . TYR A 1 285 ? -50.845  24.487 7.359   1.00 121.03 ?  285 TYR A CE2 1 
ATOM 2385 C CZ  . TYR A 1 285 ? -50.536  23.149 7.475   1.00 128.42 ?  285 TYR A CZ  1 
ATOM 2386 O OH  . TYR A 1 285 ? -49.536  22.607 6.700   1.00 131.48 ?  285 TYR A OH  1 
ATOM 2387 N N   . SER A 1 286 ? -55.608  26.802 8.234   1.00 81.29  ?  286 SER A N   1 
ATOM 2388 C CA  . SER A 1 286 ? -55.746  27.771 7.158   1.00 77.02  ?  286 SER A CA  1 
ATOM 2389 C C   . SER A 1 286 ? -55.264  29.123 7.661   1.00 99.54  ?  286 SER A C   1 
ATOM 2390 O O   . SER A 1 286 ? -55.424  29.437 8.847   1.00 95.48  ?  286 SER A O   1 
ATOM 2391 C CB  . SER A 1 286 ? -57.200  27.873 6.668   1.00 83.02  ?  286 SER A CB  1 
ATOM 2392 O OG  . SER A 1 286 ? -58.080  28.189 7.731   1.00 93.70  ?  286 SER A OG  1 
ATOM 2393 N N   . PRO A 1 287 ? -54.674  29.942 6.793   1.00 98.71  ?  287 PRO A N   1 
ATOM 2394 C CA  . PRO A 1 287 ? -53.982  31.149 7.248   1.00 87.88  ?  287 PRO A CA  1 
ATOM 2395 C C   . PRO A 1 287 ? -54.893  32.371 7.320   1.00 79.99  ?  287 PRO A C   1 
ATOM 2396 O O   . PRO A 1 287 ? -56.054  32.347 6.910   1.00 86.92  ?  287 PRO A O   1 
ATOM 2397 C CB  . PRO A 1 287 ? -52.907  31.339 6.171   1.00 83.11  ?  287 PRO A CB  1 
ATOM 2398 C CG  . PRO A 1 287 ? -53.576  30.854 4.926   1.00 83.33  ?  287 PRO A CG  1 
ATOM 2399 C CD  . PRO A 1 287 ? -54.538  29.756 5.337   1.00 86.57  ?  287 PRO A CD  1 
ATOM 2400 N N   . PHE A 1 288 ? -54.328  33.453 7.855   1.00 71.49  ?  288 PHE A N   1 
ATOM 2401 C CA  . PHE A 1 288 ? -55.012  34.729 8.005   1.00 80.14  ?  288 PHE A CA  1 
ATOM 2402 C C   . PHE A 1 288 ? -54.248  35.806 7.244   1.00 71.70  ?  288 PHE A C   1 
ATOM 2403 O O   . PHE A 1 288 ? -53.021  35.742 7.115   1.00 76.83  ?  288 PHE A O   1 
ATOM 2404 C CB  . PHE A 1 288 ? -55.139  35.136 9.486   1.00 69.27  ?  288 PHE A CB  1 
ATOM 2405 C CG  . PHE A 1 288 ? -55.780  34.089 10.360  1.00 77.41  ?  288 PHE A CG  1 
ATOM 2406 C CD1 . PHE A 1 288 ? -57.089  34.234 10.790  1.00 91.04  ?  288 PHE A CD1 1 
ATOM 2407 C CD2 . PHE A 1 288 ? -55.070  32.970 10.765  1.00 83.81  ?  288 PHE A CD2 1 
ATOM 2408 C CE1 . PHE A 1 288 ? -57.679  33.276 11.595  1.00 87.72  ?  288 PHE A CE1 1 
ATOM 2409 C CE2 . PHE A 1 288 ? -55.654  32.009 11.568  1.00 79.49  ?  288 PHE A CE2 1 
ATOM 2410 C CZ  . PHE A 1 288 ? -56.960  32.163 11.984  1.00 78.51  ?  288 PHE A CZ  1 
ATOM 2411 N N   . LEU A 1 289 ? -54.980  36.801 6.745   1.00 66.47  ?  289 LEU A N   1 
ATOM 2412 C CA  . LEU A 1 289 ? -54.398  37.904 5.990   1.00 67.22  ?  289 LEU A CA  1 
ATOM 2413 C C   . LEU A 1 289 ? -54.804  39.233 6.614   1.00 69.06  ?  289 LEU A C   1 
ATOM 2414 O O   . LEU A 1 289 ? -55.665  39.296 7.496   1.00 82.55  ?  289 LEU A O   1 
ATOM 2415 C CB  . LEU A 1 289 ? -54.825  37.873 4.516   1.00 62.33  ?  289 LEU A CB  1 
ATOM 2416 C CG  . LEU A 1 289 ? -54.469  36.649 3.671   1.00 72.90  ?  289 LEU A CG  1 
ATOM 2417 C CD1 . LEU A 1 289 ? -54.640  36.971 2.197   1.00 94.33  ?  289 LEU A CD1 1 
ATOM 2418 C CD2 . LEU A 1 289 ? -53.054  36.179 3.951   1.00 75.12  ?  289 LEU A CD2 1 
ATOM 2419 N N   . LEU A 1 290 ? -54.173  40.303 6.132   1.00 72.81  ?  290 LEU A N   1 
ATOM 2420 C CA  . LEU A 1 290 ? -54.441  41.666 6.572   1.00 78.00  ?  290 LEU A CA  1 
ATOM 2421 C C   . LEU A 1 290 ? -53.737  42.627 5.624   1.00 80.46  ?  290 LEU A C   1 
ATOM 2422 O O   . LEU A 1 290 ? -52.630  42.341 5.162   1.00 88.55  ?  290 LEU A O   1 
ATOM 2423 C CB  . LEU A 1 290 ? -53.964  41.893 8.015   1.00 76.90  ?  290 LEU A CB  1 
ATOM 2424 C CG  . LEU A 1 290 ? -54.016  43.320 8.565   1.00 63.68  ?  290 LEU A CG  1 
ATOM 2425 C CD1 . LEU A 1 290 ? -55.432  43.870 8.503   1.00 64.92  ?  290 LEU A CD1 1 
ATOM 2426 C CD2 . LEU A 1 290 ? -53.481  43.370 9.989   1.00 80.80  ?  290 LEU A CD2 1 
ATOM 2427 N N   . PHE A 1 291 ? -54.380  43.759 5.341   1.00 77.92  ?  291 PHE A N   1 
ATOM 2428 C CA  . PHE A 1 291 ? -53.835  44.743 4.417   1.00 73.34  ?  291 PHE A CA  1 
ATOM 2429 C C   . PHE A 1 291 ? -53.985  46.139 5.006   1.00 84.22  ?  291 PHE A C   1 
ATOM 2430 O O   . PHE A 1 291 ? -54.806  46.378 5.895   1.00 80.70  ?  291 PHE A O   1 
ATOM 2431 C CB  . PHE A 1 291 ? -54.521  44.675 3.046   1.00 74.69  ?  291 PHE A CB  1 
ATOM 2432 C CG  . PHE A 1 291 ? -54.227  43.415 2.284   1.00 74.50  ?  291 PHE A CG  1 
ATOM 2433 C CD1 . PHE A 1 291 ? -53.199  43.372 1.357   1.00 89.18  ?  291 PHE A CD1 1 
ATOM 2434 C CD2 . PHE A 1 291 ? -54.979  42.273 2.496   1.00 88.93  ?  291 PHE A CD2 1 
ATOM 2435 C CE1 . PHE A 1 291 ? -52.928  42.212 0.656   1.00 96.79  ?  291 PHE A CE1 1 
ATOM 2436 C CE2 . PHE A 1 291 ? -54.713  41.110 1.800   1.00 88.31  ?  291 PHE A CE2 1 
ATOM 2437 C CZ  . PHE A 1 291 ? -53.687  41.080 0.878   1.00 90.11  ?  291 PHE A CZ  1 
ATOM 2438 N N   . HIS A 1 292 ? -53.176  47.062 4.491   1.00 92.13  ?  292 HIS A N   1 
ATOM 2439 C CA  . HIS A 1 292 ? -53.201  48.450 4.934   1.00 100.31 ?  292 HIS A CA  1 
ATOM 2440 C C   . HIS A 1 292 ? -52.595  49.321 3.843   1.00 97.13  ?  292 HIS A C   1 
ATOM 2441 O O   . HIS A 1 292 ? -51.957  48.829 2.909   1.00 95.34  ?  292 HIS A O   1 
ATOM 2442 C CB  . HIS A 1 292 ? -52.455  48.634 6.262   1.00 96.46  ?  292 HIS A CB  1 
ATOM 2443 C CG  . HIS A 1 292 ? -51.042  48.135 6.243   1.00 101.70 ?  292 HIS A CG  1 
ATOM 2444 N ND1 . HIS A 1 292 ? -50.718  46.819 5.991   1.00 94.28  ?  292 HIS A ND1 1 
ATOM 2445 C CD2 . HIS A 1 292 ? -49.868  48.778 6.449   1.00 97.06  ?  292 HIS A CD2 1 
ATOM 2446 C CE1 . HIS A 1 292 ? -49.407  46.672 6.043   1.00 98.93  ?  292 HIS A CE1 1 
ATOM 2447 N NE2 . HIS A 1 292 ? -48.867  47.846 6.318   1.00 104.26 ?  292 HIS A NE2 1 
ATOM 2448 N N   . GLY A 1 293 ? -52.802  50.629 3.978   1.00 106.41 ?  293 GLY A N   1 
ATOM 2449 C CA  . GLY A 1 293 ? -52.288  51.587 3.018   1.00 119.74 ?  293 GLY A CA  1 
ATOM 2450 C C   . GLY A 1 293 ? -52.990  51.530 1.678   1.00 117.98 ?  293 GLY A C   1 
ATOM 2451 O O   . GLY A 1 293 ? -52.342  51.430 0.632   1.00 117.69 ?  293 GLY A O   1 
ATOM 2452 N N   . THR A 1 294 ? -54.317  51.604 1.696   1.00 118.07 ?  294 THR A N   1 
ATOM 2453 C CA  . THR A 1 294 ? -55.114  51.515 0.479   1.00 123.05 ?  294 THR A CA  1 
ATOM 2454 C C   . THR A 1 294 ? -56.475  52.144 0.752   1.00 115.93 ?  294 THR A C   1 
ATOM 2455 O O   . THR A 1 294 ? -56.727  52.683 1.833   1.00 120.56 ?  294 THR A O   1 
ATOM 2456 C CB  . THR A 1 294 ? -55.252  50.063 0.013   1.00 111.10 ?  294 THR A CB  1 
ATOM 2457 O OG1 . THR A 1 294 ? -55.899  50.027 -1.265  1.00 108.89 ?  294 THR A OG1 1 
ATOM 2458 C CG2 . THR A 1 294 ? -56.068  49.256 1.015   1.00 107.94 ?  294 THR A CG2 1 
ATOM 2459 N N   . SER A 1 295 ? -57.350  52.074 -0.244  1.00 107.27 ?  295 SER A N   1 
ATOM 2460 C CA  . SER A 1 295 ? -58.716  52.557 -0.123  1.00 107.21 ?  295 SER A CA  1 
ATOM 2461 C C   . SER A 1 295 ? -59.665  51.389 0.118   1.00 113.11 ?  295 SER A C   1 
ATOM 2462 O O   . SER A 1 295 ? -59.357  50.233 -0.188  1.00 104.81 ?  295 SER A O   1 
ATOM 2463 C CB  . SER A 1 295 ? -59.136  53.330 -1.375  1.00 114.31 ?  295 SER A CB  1 
ATOM 2464 O OG  . SER A 1 295 ? -59.436  52.450 -2.443  1.00 115.66 ?  295 SER A OG  1 
ATOM 2465 N N   . ASP A 1 296 ? -60.831  51.708 0.682   1.00 119.98 ?  296 ASP A N   1 
ATOM 2466 C CA  . ASP A 1 296 ? -61.799  50.672 1.026   1.00 107.24 ?  296 ASP A CA  1 
ATOM 2467 C C   . ASP A 1 296 ? -62.301  49.949 -0.218  1.00 95.83  ?  296 ASP A C   1 
ATOM 2468 O O   . ASP A 1 296 ? -62.399  48.716 -0.238  1.00 96.85  ?  296 ASP A O   1 
ATOM 2469 C CB  . ASP A 1 296 ? -62.967  51.284 1.800   1.00 118.56 ?  296 ASP A CB  1 
ATOM 2470 C CG  . ASP A 1 296 ? -62.513  52.065 3.016   1.00 134.00 ?  296 ASP A CG  1 
ATOM 2471 O OD1 . ASP A 1 296 ? -61.681  51.541 3.785   1.00 136.15 ?  296 ASP A OD1 1 
ATOM 2472 O OD2 . ASP A 1 296 ? -62.990  53.205 3.203   1.00 149.31 -1 296 ASP A OD2 1 
ATOM 2473 N N   . ALA A 1 297 ? -62.628  50.704 -1.270  1.00 105.28 ?  297 ALA A N   1 
ATOM 2474 C CA  . ALA A 1 297 ? -63.161  50.094 -2.485  1.00 95.49  ?  297 ALA A CA  1 
ATOM 2475 C C   . ALA A 1 297 ? -62.141  49.182 -3.154  1.00 93.81  ?  297 ALA A C   1 
ATOM 2476 O O   . ALA A 1 297 ? -62.514  48.161 -3.742  1.00 91.01  ?  297 ALA A O   1 
ATOM 2477 C CB  . ALA A 1 297 ? -63.625  51.178 -3.457  1.00 109.86 ?  297 ALA A CB  1 
ATOM 2478 N N   . ASN A 1 298 ? -60.855  49.533 -3.082  1.00 101.97 ?  298 ASN A N   1 
ATOM 2479 C CA  . ASN A 1 298 ? -59.824  48.668 -3.646  1.00 117.59 ?  298 ASN A CA  1 
ATOM 2480 C C   . ASN A 1 298 ? -59.749  47.342 -2.898  1.00 108.48 ?  298 ASN A C   1 
ATOM 2481 O O   . ASN A 1 298 ? -59.555  46.286 -3.512  1.00 100.40 ?  298 ASN A O   1 
ATOM 2482 C CB  . ASN A 1 298 ? -58.472  49.380 -3.630  1.00 116.71 ?  298 ASN A CB  1 
ATOM 2483 C CG  . ASN A 1 298 ? -58.389  50.496 -4.654  1.00 121.76 ?  298 ASN A CG  1 
ATOM 2484 O OD1 . ASN A 1 298 ? -58.885  51.601 -4.429  1.00 129.13 ?  298 ASN A OD1 1 
ATOM 2485 N ND2 . ASN A 1 298 ? -57.758  50.212 -5.787  1.00 109.82 ?  298 ASN A ND2 1 
ATOM 2486 N N   . LEU A 1 299 ? -59.899  47.377 -1.572  1.00 93.82  ?  299 LEU A N   1 
ATOM 2487 C CA  . LEU A 1 299 ? -59.963  46.138 -0.804  1.00 90.58  ?  299 LEU A CA  1 
ATOM 2488 C C   . LEU A 1 299 ? -61.243  45.369 -1.110  1.00 98.34  ?  299 LEU A C   1 
ATOM 2489 O O   . LEU A 1 299 ? -61.223  44.137 -1.220  1.00 99.63  ?  299 LEU A O   1 
ATOM 2490 C CB  . LEU A 1 299 ? -59.865  46.440 0.691   1.00 96.34  ?  299 LEU A CB  1 
ATOM 2491 C CG  . LEU A 1 299 ? -58.542  46.116 1.388   1.00 104.60 ?  299 LEU A CG  1 
ATOM 2492 C CD1 . LEU A 1 299 ? -58.665  46.341 2.886   1.00 107.66 ?  299 LEU A CD1 1 
ATOM 2493 C CD2 . LEU A 1 299 ? -58.112  44.688 1.094   1.00 111.23 ?  299 LEU A CD2 1 
ATOM 2494 N N   . TYR A 1 300 ? -62.364  46.079 -1.250  1.00 93.77  ?  300 TYR A N   1 
ATOM 2495 C CA  . TYR A 1 300 ? -63.636  45.420 -1.530  1.00 92.52  ?  300 TYR A CA  1 
ATOM 2496 C C   . TYR A 1 300 ? -63.632  44.782 -2.913  1.00 91.20  ?  300 TYR A C   1 
ATOM 2497 O O   . TYR A 1 300 ? -64.050  43.629 -3.077  1.00 73.24  ?  300 TYR A O   1 
ATOM 2498 C CB  . TYR A 1 300 ? -64.784  46.421 -1.400  1.00 107.23 ?  300 TYR A CB  1 
ATOM 2499 C CG  . TYR A 1 300 ? -64.977  46.962 -0.000  1.00 118.75 ?  300 TYR A CG  1 
ATOM 2500 C CD1 . TYR A 1 300 ? -64.501  46.271 1.107   1.00 112.04 ?  300 TYR A CD1 1 
ATOM 2501 C CD2 . TYR A 1 300 ? -65.634  48.167 0.213   1.00 122.26 ?  300 TYR A CD2 1 
ATOM 2502 C CE1 . TYR A 1 300 ? -64.676  46.764 2.388   1.00 114.61 ?  300 TYR A CE1 1 
ATOM 2503 C CE2 . TYR A 1 300 ? -65.814  48.668 1.489   1.00 117.92 ?  300 TYR A CE2 1 
ATOM 2504 C CZ  . TYR A 1 300 ? -65.333  47.963 2.573   1.00 120.30 ?  300 TYR A CZ  1 
ATOM 2505 O OH  . TYR A 1 300 ? -65.509  48.458 3.844   1.00 125.34 ?  300 TYR A OH  1 
ATOM 2506 N N   . GLU A 1 301 ? -63.166  45.521 -3.925  1.00 90.25  ?  301 GLU A N   1 
ATOM 2507 C CA  . GLU A 1 301 ? -63.094  44.970 -5.275  1.00 82.46  ?  301 GLU A CA  1 
ATOM 2508 C C   . GLU A 1 301 ? -62.172  43.759 -5.331  1.00 84.32  ?  301 GLU A C   1 
ATOM 2509 O O   . GLU A 1 301 ? -62.351  42.879 -6.182  1.00 77.51  ?  301 GLU A O   1 
ATOM 2510 C CB  . GLU A 1 301 ? -62.624  46.047 -6.256  1.00 96.05  ?  301 GLU A CB  1 
ATOM 2511 C CG  . GLU A 1 301 ? -62.681  45.637 -7.721  1.00 97.95  ?  301 GLU A CG  1 
ATOM 2512 C CD  . GLU A 1 301 ? -64.084  45.711 -8.294  1.00 109.16 ?  301 GLU A CD  1 
ATOM 2513 O OE1 . GLU A 1 301 ? -64.501  46.814 -8.708  1.00 112.59 ?  301 GLU A OE1 1 
ATOM 2514 O OE2 . GLU A 1 301 ? -64.770  44.668 -8.330  1.00 118.28 -1 301 GLU A OE2 1 
ATOM 2515 N N   . LEU A 1 302 ? -61.188  43.692 -4.432  1.00 84.27  ?  302 LEU A N   1 
ATOM 2516 C CA  . LEU A 1 302 ? -60.312  42.527 -4.372  1.00 82.24  ?  302 LEU A CA  1 
ATOM 2517 C C   . LEU A 1 302 ? -61.048  41.311 -3.823  1.00 85.20  ?  302 LEU A C   1 
ATOM 2518 O O   . LEU A 1 302 ? -60.880  40.195 -4.331  1.00 87.35  ?  302 LEU A O   1 
ATOM 2519 C CB  . LEU A 1 302 ? -59.082  42.844 -3.520  1.00 80.41  ?  302 LEU A CB  1 
ATOM 2520 C CG  . LEU A 1 302 ? -58.199  41.671 -3.086  1.00 86.56  ?  302 LEU A CG  1 
ATOM 2521 C CD1 . LEU A 1 302 ? -57.641  40.937 -4.294  1.00 93.15  ?  302 LEU A CD1 1 
ATOM 2522 C CD2 . LEU A 1 302 ? -57.076  42.149 -2.179  1.00 85.53  ?  302 LEU A CD2 1 
ATOM 2523 N N   . LYS A 1 303 ? -61.866  41.505 -2.785  1.00 83.99  ?  303 LYS A N   1 
ATOM 2524 C CA  . LYS A 1 303 ? -62.573  40.385 -2.168  1.00 80.16  ?  303 LYS A CA  1 
ATOM 2525 C C   . LYS A 1 303 ? -63.527  39.721 -3.153  1.00 83.37  ?  303 LYS A C   1 
ATOM 2526 O O   . LYS A 1 303 ? -63.592  38.488 -3.235  1.00 72.91  ?  303 LYS A O   1 
ATOM 2527 C CB  . LYS A 1 303 ? -63.339  40.860 -0.933  1.00 89.42  ?  303 LYS A CB  1 
ATOM 2528 C CG  . LYS A 1 303 ? -62.479  41.430 0.177   1.00 91.51  ?  303 LYS A CG  1 
ATOM 2529 C CD  . LYS A 1 303 ? -63.341  41.786 1.377   1.00 92.33  ?  303 LYS A CD  1 
ATOM 2530 C CE  . LYS A 1 303 ? -62.528  42.436 2.480   1.00 101.42 ?  303 LYS A CE  1 
ATOM 2531 N NZ  . LYS A 1 303 ? -63.381  42.781 3.649   1.00 103.62 ?  303 LYS A NZ  1 
ATOM 2532 N N   . ASN A 1 304 ? -64.288  40.527 -3.899  1.00 80.72  ?  304 ASN A N   1 
ATOM 2533 C CA  . ASN A 1 304 ? -65.284  39.976 -4.814  1.00 80.70  ?  304 ASN A CA  1 
ATOM 2534 C C   . ASN A 1 304 ? -64.643  39.058 -5.846  1.00 88.57  ?  304 ASN A C   1 
ATOM 2535 O O   . ASN A 1 304 ? -65.161  37.969 -6.124  1.00 86.28  ?  304 ASN A O   1 
ATOM 2536 C CB  . ASN A 1 304 ? -66.046  41.107 -5.504  1.00 76.52  ?  304 ASN A CB  1 
ATOM 2537 C CG  . ASN A 1 304 ? -66.658  42.083 -4.520  1.00 82.04  ?  304 ASN A CG  1 
ATOM 2538 O OD1 . ASN A 1 304 ? -66.404  43.286 -4.582  1.00 80.79  ?  304 ASN A OD1 1 
ATOM 2539 N ND2 . ASN A 1 304 ? -67.467  41.569 -3.601  1.00 90.16  ?  304 ASN A ND2 1 
ATOM 2540 N N   . GLN A 1 305 ? -63.513  39.476 -6.420  1.00 83.46  ?  305 GLN A N   1 
ATOM 2541 C CA  . GLN A 1 305 ? -62.841  38.651 -7.419  1.00 90.62  ?  305 GLN A CA  1 
ATOM 2542 C C   . GLN A 1 305 ? -62.416  37.312 -6.828  1.00 87.25  ?  305 GLN A C   1 
ATOM 2543 O O   . GLN A 1 305 ? -62.614  36.259 -7.444  1.00 82.29  ?  305 GLN A O   1 
ATOM 2544 C CB  . GLN A 1 305 ? -61.635  39.397 -7.991  1.00 92.15  ?  305 GLN A CB  1 
ATOM 2545 C CG  . GLN A 1 305 ? -61.985  40.709 -8.673  1.00 98.25  ?  305 GLN A CG  1 
ATOM 2546 C CD  . GLN A 1 305 ? -60.778  41.374 -9.303  1.00 93.64  ?  305 GLN A CD  1 
ATOM 2547 O OE1 . GLN A 1 305 ? -59.757  40.730 -9.546  1.00 87.62  ?  305 GLN A OE1 1 
ATOM 2548 N NE2 . GLN A 1 305 ? -60.887  42.670 -9.569  1.00 86.46  ?  305 GLN A NE2 1 
ATOM 2549 N N   . LEU A 1 306 ? -61.835  37.334 -5.626  1.00 88.18  ?  306 LEU A N   1 
ATOM 2550 C CA  . LEU A 1 306 ? -61.453  36.086 -4.974  1.00 85.55  ?  306 LEU A CA  1 
ATOM 2551 C C   . LEU A 1 306 ? -62.669  35.226 -4.659  1.00 92.80  ?  306 LEU A C   1 
ATOM 2552 O O   . LEU A 1 306 ? -62.566  33.994 -4.629  1.00 92.11  ?  306 LEU A O   1 
ATOM 2553 C CB  . LEU A 1 306 ? -60.661  36.375 -3.699  1.00 89.72  ?  306 LEU A CB  1 
ATOM 2554 C CG  . LEU A 1 306 ? -59.242  36.914 -3.889  1.00 100.71 ?  306 LEU A CG  1 
ATOM 2555 C CD1 . LEU A 1 306 ? -58.527  37.020 -2.552  1.00 100.01 ?  306 LEU A CD1 1 
ATOM 2556 C CD2 . LEU A 1 306 ? -58.456  36.038 -4.853  1.00 88.53  ?  306 LEU A CD2 1 
ATOM 2557 N N   . PHE A 1 307 ? -63.826  35.848 -4.429  1.00 89.82  ?  307 PHE A N   1 
ATOM 2558 C CA  . PHE A 1 307 ? -65.038  35.077 -4.182  1.00 89.56  ?  307 PHE A CA  1 
ATOM 2559 C C   . PHE A 1 307 ? -65.656  34.577 -5.483  1.00 94.96  ?  307 PHE A C   1 
ATOM 2560 O O   . PHE A 1 307 ? -66.105  33.428 -5.555  1.00 102.68 ?  307 PHE A O   1 
ATOM 2561 C CB  . PHE A 1 307 ? -66.047  35.915 -3.396  1.00 88.45  ?  307 PHE A CB  1 
ATOM 2562 C CG  . PHE A 1 307 ? -66.873  35.116 -2.428  1.00 94.33  ?  307 PHE A CG  1 
ATOM 2563 C CD1 . PHE A 1 307 ? -68.140  34.676 -2.774  1.00 81.85  ?  307 PHE A CD1 1 
ATOM 2564 C CD2 . PHE A 1 307 ? -66.381  34.803 -1.171  1.00 99.94  ?  307 PHE A CD2 1 
ATOM 2565 C CE1 . PHE A 1 307 ? -68.901  33.941 -1.885  1.00 85.70  ?  307 PHE A CE1 1 
ATOM 2566 C CE2 . PHE A 1 307 ? -67.137  34.068 -0.277  1.00 96.79  ?  307 PHE A CE2 1 
ATOM 2567 C CZ  . PHE A 1 307 ? -68.399  33.636 -0.635  1.00 82.21  ?  307 PHE A CZ  1 
ATOM 2568 N N   . ASN A 1 308 ? -65.691  35.422 -6.518  1.00 80.53  ?  308 ASN A N   1 
ATOM 2569 C CA  . ASN A 1 308 ? -66.226  34.987 -7.805  1.00 86.01  ?  308 ASN A CA  1 
ATOM 2570 C C   . ASN A 1 308 ? -65.353  33.915 -8.439  1.00 95.55  ?  308 ASN A C   1 
ATOM 2571 O O   . ASN A 1 308 ? -65.853  33.077 -9.197  1.00 115.54 ?  308 ASN A O   1 
ATOM 2572 C CB  . ASN A 1 308 ? -66.379  36.179 -8.749  1.00 96.55  ?  308 ASN A CB  1 
ATOM 2573 C CG  . ASN A 1 308 ? -67.236  37.281 -8.160  1.00 102.14 ?  308 ASN A CG  1 
ATOM 2574 O OD1 . ASN A 1 308 ? -66.915  38.464 -8.275  1.00 111.11 ?  308 ASN A OD1 1 
ATOM 2575 N ND2 . ASN A 1 308 ? -68.335  36.895 -7.521  1.00 106.32 ?  308 ASN A ND2 1 
ATOM 2576 N N   . GLU A 1 309 ? -64.054  33.925 -8.150  1.00 87.36  ?  309 GLU A N   1 
ATOM 2577 C CA  . GLU A 1 309 ? -63.160  32.857 -8.577  1.00 91.75  ?  309 GLU A CA  1 
ATOM 2578 C C   . GLU A 1 309 ? -63.302  31.602 -7.726  1.00 99.29  ?  309 GLU A C   1 
ATOM 2579 O O   . GLU A 1 309 ? -62.508  30.674 -7.891  1.00 98.78  ?  309 GLU A O   1 
ATOM 2580 C CB  . GLU A 1 309 ? -61.702  33.338 -8.553  1.00 89.55  ?  309 GLU A CB  1 
ATOM 2581 C CG  . GLU A 1 309 ? -61.355  34.347 -9.640  1.00 104.71 ?  309 GLU A CG  1 
ATOM 2582 C CD  . GLU A 1 309 ? -59.880  34.711 -9.642  1.00 103.70 ?  309 GLU A CD  1 
ATOM 2583 O OE1 . GLU A 1 309 ? -59.461  35.531 -10.488 1.00 110.19 ?  309 GLU A OE1 1 
ATOM 2584 O OE2 . GLU A 1 309 ? -59.139  34.182 -8.789  1.00 98.11  -1 309 GLU A OE2 1 
ATOM 2585 N N   . ASP A 1 310 ? -64.285  31.568 -6.827  1.00 100.29 ?  310 ASP A N   1 
ATOM 2586 C CA  . ASP A 1 310 ? -64.569  30.406 -5.989  1.00 113.44 ?  310 ASP A CA  1 
ATOM 2587 C C   . ASP A 1 310 ? -63.400  30.078 -5.064  1.00 104.86 ?  310 ASP A C   1 
ATOM 2588 O O   . ASP A 1 310 ? -63.050  28.913 -4.864  1.00 92.47  ?  310 ASP A O   1 
ATOM 2589 C CB  . ASP A 1 310 ? -64.957  29.189 -6.834  1.00 117.40 ?  310 ASP A CB  1 
ATOM 2590 C CG  . ASP A 1 310 ? -66.313  29.343 -7.499  1.00 119.59 ?  310 ASP A CG  1 
ATOM 2591 O OD1 . ASP A 1 310 ? -67.301  29.601 -6.782  1.00 121.07 ?  310 ASP A OD1 1 
ATOM 2592 O OD2 . ASP A 1 310 ? -66.388  29.224 -8.742  1.00 114.95 -1 310 ASP A OD2 1 
ATOM 2593 N N   . LEU A 1 311 ? -62.792  31.115 -4.497  1.00 94.16  ?  311 LEU A N   1 
ATOM 2594 C CA  . LEU A 1 311 ? -61.808  30.985 -3.425  1.00 90.87  ?  311 LEU A CA  1 
ATOM 2595 C C   . LEU A 1 311 ? -62.485  31.511 -2.164  1.00 99.20  ?  311 LEU A C   1 
ATOM 2596 O O   . LEU A 1 311 ? -62.515  32.721 -1.921  1.00 92.27  ?  311 LEU A O   1 
ATOM 2597 C CB  . LEU A 1 311 ? -60.526  31.747 -3.750  1.00 94.61  ?  311 LEU A CB  1 
ATOM 2598 C CG  . LEU A 1 311 ? -59.378  31.625 -2.746  1.00 94.62  ?  311 LEU A CG  1 
ATOM 2599 C CD1 . LEU A 1 311 ? -58.791  30.224 -2.768  1.00 88.93  ?  311 LEU A CD1 1 
ATOM 2600 C CD2 . LEU A 1 311 ? -58.302  32.661 -3.034  1.00 90.03  ?  311 LEU A CD2 1 
ATOM 2601 N N   . ILE A 1 312 ? -63.027  30.597 -1.367  1.00 101.91 ?  312 ILE A N   1 
ATOM 2602 C CA  . ILE A 1 312 ? -63.929  30.950 -0.277  1.00 89.77  ?  312 ILE A CA  1 
ATOM 2603 C C   . ILE A 1 312 ? -63.125  31.376 0.944   1.00 100.27 ?  312 ILE A C   1 
ATOM 2604 O O   . ILE A 1 312 ? -62.062  30.815 1.238   1.00 99.89  ?  312 ILE A O   1 
ATOM 2605 C CB  . ILE A 1 312 ? -64.855  29.764 0.046   1.00 97.36  ?  312 ILE A CB  1 
ATOM 2606 C CG1 . ILE A 1 312 ? -65.384  29.140 -1.248  1.00 105.54 ?  312 ILE A CG1 1 
ATOM 2607 C CG2 . ILE A 1 312 ? -66.013  30.212 0.922   1.00 100.24 ?  312 ILE A CG2 1 
ATOM 2608 C CD1 . ILE A 1 312 ? -66.172  27.866 -1.039  1.00 105.02 ?  312 ILE A CD1 1 
ATOM 2609 N N   . PHE A 1 313 ? -63.637  32.374 1.663   1.00 94.61  ?  313 PHE A N   1 
ATOM 2610 C CA  . PHE A 1 313 ? -62.984  32.882 2.861   1.00 79.18  ?  313 PHE A CA  1 
ATOM 2611 C C   . PHE A 1 313 ? -64.042  33.454 3.796   1.00 85.89  ?  313 PHE A C   1 
ATOM 2612 O O   . PHE A 1 313 ? -65.241  33.428 3.503   1.00 77.15  ?  313 PHE A O   1 
ATOM 2613 C CB  . PHE A 1 313 ? -61.928  33.937 2.512   1.00 88.86  ?  313 PHE A CB  1 
ATOM 2614 C CG  . PHE A 1 313 ? -62.498  35.199 1.923   1.00 84.62  ?  313 PHE A CG  1 
ATOM 2615 C CD1 . PHE A 1 313 ? -62.712  35.306 0.559   1.00 82.65  ?  313 PHE A CD1 1 
ATOM 2616 C CD2 . PHE A 1 313 ? -62.807  36.282 2.731   1.00 70.62  ?  313 PHE A CD2 1 
ATOM 2617 C CE1 . PHE A 1 313 ? -63.232  36.465 0.013   1.00 61.36  ?  313 PHE A CE1 1 
ATOM 2618 C CE2 . PHE A 1 313 ? -63.328  37.444 2.191   1.00 73.76  ?  313 PHE A CE2 1 
ATOM 2619 C CZ  . PHE A 1 313 ? -63.540  37.535 0.830   1.00 73.76  ?  313 PHE A CZ  1 
ATOM 2620 N N   . THR A 1 314 ? -63.583  33.981 4.929   1.00 82.47  ?  314 THR A N   1 
ATOM 2621 C CA  . THR A 1 314 ? -64.456  34.645 5.885   1.00 75.98  ?  314 THR A CA  1 
ATOM 2622 C C   . THR A 1 314 ? -63.687  35.780 6.544   1.00 77.99  ?  314 THR A C   1 
ATOM 2623 O O   . THR A 1 314 ? -62.478  35.681 6.768   1.00 81.45  ?  314 THR A O   1 
ATOM 2624 C CB  . THR A 1 314 ? -64.985  33.675 6.950   1.00 74.36  ?  314 THR A CB  1 
ATOM 2625 O OG1 . THR A 1 314 ? -65.589  34.416 8.018   1.00 98.54  ?  314 THR A OG1 1 
ATOM 2626 C CG2 . THR A 1 314 ? -63.855  32.822 7.507   1.00 62.33  ?  314 THR A CG2 1 
ATOM 2627 N N   . ASP A 1 315 ? -64.401  36.867 6.848   1.00 80.58  ?  315 ASP A N   1 
ATOM 2628 C CA  . ASP A 1 315 ? -63.802  38.038 7.477   1.00 81.33  ?  315 ASP A CA  1 
ATOM 2629 C C   . ASP A 1 315 ? -64.498  38.410 8.781   1.00 87.49  ?  315 ASP A C   1 
ATOM 2630 O O   . ASP A 1 315 ? -64.333  39.532 9.270   1.00 96.95  ?  315 ASP A O   1 
ATOM 2631 C CB  . ASP A 1 315 ? -63.812  39.227 6.516   1.00 80.88  ?  315 ASP A CB  1 
ATOM 2632 C CG  . ASP A 1 315 ? -65.210  39.741 6.242   1.00 94.75  ?  315 ASP A CG  1 
ATOM 2633 O OD1 . ASP A 1 315 ? -66.163  38.936 6.294   1.00 90.80  ?  315 ASP A OD1 1 
ATOM 2634 O OD2 . ASP A 1 315 ? -65.355  40.953 5.974   1.00 94.79  -1 315 ASP A OD2 1 
ATOM 2635 N N   . GLY A 1 316 ? -65.275  37.493 9.354   1.00 82.16  ?  316 GLY A N   1 
ATOM 2636 C CA  . GLY A 1 316 ? -66.001  37.765 10.575  1.00 84.86  ?  316 GLY A CA  1 
ATOM 2637 C C   . GLY A 1 316 ? -67.300  38.519 10.398  1.00 85.82  ?  316 GLY A C   1 
ATOM 2638 O O   . GLY A 1 316 ? -67.962  38.818 11.400  1.00 91.36  ?  316 GLY A O   1 
ATOM 2639 N N   . TYR A 1 317 ? -67.687  38.842 9.161   1.00 88.29  ?  317 TYR A N   1 
ATOM 2640 C CA  . TYR A 1 317 ? -68.928  39.553 8.862   1.00 74.46  ?  317 TYR A CA  1 
ATOM 2641 C C   . TYR A 1 317 ? -69.787  38.656 7.977   1.00 77.74  ?  317 TYR A C   1 
ATOM 2642 O O   . TYR A 1 317 ? -69.793  38.803 6.746   1.00 90.77  ?  317 TYR A O   1 
ATOM 2643 C CB  . TYR A 1 317 ? -68.654  40.894 8.183   1.00 104.44 ?  317 TYR A CB  1 
ATOM 2644 C CG  . TYR A 1 317 ? -67.917  41.894 9.048   1.00 88.50  ?  317 TYR A CG  1 
ATOM 2645 C CD1 . TYR A 1 317 ? -68.601  42.898 9.719   1.00 74.90  ?  317 TYR A CD1 1 
ATOM 2646 C CD2 . TYR A 1 317 ? -66.535  41.840 9.184   1.00 87.98  ?  317 TYR A CD2 1 
ATOM 2647 C CE1 . TYR A 1 317 ? -67.933  43.816 10.508  1.00 91.31  ?  317 TYR A CE1 1 
ATOM 2648 C CE2 . TYR A 1 317 ? -65.858  42.754 9.971   1.00 86.71  ?  317 TYR A CE2 1 
ATOM 2649 C CZ  . TYR A 1 317 ? -66.561  43.740 10.630  1.00 95.43  ?  317 TYR A CZ  1 
ATOM 2650 O OH  . TYR A 1 317 ? -65.892  44.652 11.414  1.00 81.28  ?  317 TYR A OH  1 
ATOM 2651 N N   . PRO A 1 318 ? -70.528  37.713 8.569   1.00 83.26  ?  318 PRO A N   1 
ATOM 2652 C CA  . PRO A 1 318 ? -71.346  36.795 7.761   1.00 81.06  ?  318 PRO A CA  1 
ATOM 2653 C C   . PRO A 1 318 ? -72.559  37.441 7.107   1.00 85.91  ?  318 PRO A C   1 
ATOM 2654 O O   . PRO A 1 318 ? -73.247  36.768 6.331   1.00 71.54  ?  318 PRO A O   1 
ATOM 2655 C CB  . PRO A 1 318 ? -71.776  35.731 8.780   1.00 71.51  ?  318 PRO A CB  1 
ATOM 2656 C CG  . PRO A 1 318 ? -71.755  36.449 10.090  1.00 80.14  ?  318 PRO A CG  1 
ATOM 2657 C CD  . PRO A 1 318 ? -70.589  37.389 10.005  1.00 84.30  ?  318 PRO A CD  1 
ATOM 2658 N N   . PHE A 1 319 ? -72.843  38.711 7.385   1.00 88.41  ?  319 PHE A N   1 
ATOM 2659 C CA  . PHE A 1 319 ? -73.976  39.408 6.787   1.00 70.41  ?  319 PHE A CA  1 
ATOM 2660 C C   . PHE A 1 319 ? -73.801  40.899 7.038   1.00 71.39  ?  319 PHE A C   1 
ATOM 2661 O O   . PHE A 1 319 ? -72.963  41.318 7.840   1.00 86.55  ?  319 PHE A O   1 
ATOM 2662 C CB  . PHE A 1 319 ? -75.314  38.907 7.346   1.00 81.81  ?  319 PHE A CB  1 
ATOM 2663 C CG  . PHE A 1 319 ? -75.356  38.807 8.848   1.00 84.88  ?  319 PHE A CG  1 
ATOM 2664 C CD1 . PHE A 1 319 ? -75.011  37.628 9.489   1.00 70.46  ?  319 PHE A CD1 1 
ATOM 2665 C CD2 . PHE A 1 319 ? -75.766  39.884 9.617   1.00 79.88  ?  319 PHE A CD2 1 
ATOM 2666 C CE1 . PHE A 1 319 ? -75.057  37.531 10.868  1.00 56.83  ?  319 PHE A CE1 1 
ATOM 2667 C CE2 . PHE A 1 319 ? -75.819  39.791 10.997  1.00 69.81  ?  319 PHE A CE2 1 
ATOM 2668 C CZ  . PHE A 1 319 ? -75.461  38.613 11.622  1.00 60.61  ?  319 PHE A CZ  1 
ATOM 2669 N N   . LYS A 1 320 ? -74.599  41.698 6.333   1.00 74.74  ?  320 LYS A N   1 
ATOM 2670 C CA  . LYS A 1 320 ? -74.551  43.141 6.525   1.00 73.78  ?  320 LYS A CA  1 
ATOM 2671 C C   . LYS A 1 320 ? -75.133  43.510 7.884   1.00 78.07  ?  320 LYS A C   1 
ATOM 2672 O O   . LYS A 1 320 ? -76.153  42.961 8.312   1.00 83.67  ?  320 LYS A O   1 
ATOM 2673 C CB  . LYS A 1 320 ? -75.310  43.862 5.412   1.00 66.43  ?  320 LYS A CB  1 
ATOM 2674 C CG  . LYS A 1 320 ? -75.234  45.379 5.512   1.00 86.70  ?  320 LYS A CG  1 
ATOM 2675 C CD  . LYS A 1 320 ? -75.461  46.053 4.171   1.00 85.13  ?  320 LYS A CD  1 
ATOM 2676 C CE  . LYS A 1 320 ? -75.141  47.538 4.252   1.00 116.03 ?  320 LYS A CE  1 
ATOM 2677 N NZ  . LYS A 1 320 ? -75.184  48.196 2.918   1.00 129.29 ?  320 LYS A NZ  1 
ATOM 2678 N N   . GLY A 1 321 ? -74.477  44.448 8.563   1.00 78.35  ?  321 GLY A N   1 
ATOM 2679 C CA  . GLY A 1 321 ? -74.851  44.812 9.910   1.00 83.24  ?  321 GLY A CA  1 
ATOM 2680 C C   . GLY A 1 321 ? -74.305  43.903 10.986  1.00 75.05  ?  321 GLY A C   1 
ATOM 2681 O O   . GLY A 1 321 ? -74.536  44.167 12.173  1.00 65.79  ?  321 GLY A O   1 
ATOM 2682 N N   . SER A 1 322 ? -73.595  42.842 10.611  1.00 85.12  ?  322 SER A N   1 
ATOM 2683 C CA  . SER A 1 322 ? -73.001  41.945 11.591  1.00 81.56  ?  322 SER A CA  1 
ATOM 2684 C C   . SER A 1 322 ? -71.850  42.632 12.308  1.00 80.48  ?  322 SER A C   1 
ATOM 2685 O O   . SER A 1 322 ? -70.965  43.213 11.672  1.00 95.00  ?  322 SER A O   1 
ATOM 2686 C CB  . SER A 1 322 ? -72.502  40.670 10.912  1.00 71.26  ?  322 SER A CB  1 
ATOM 2687 O OG  . SER A 1 322 ? -71.652  39.935 11.775  1.00 66.78  ?  322 SER A OG  1 
ATOM 2688 N N   . VAL A 1 323 ? -71.863  42.569 13.639  1.00 75.70  ?  323 VAL A N   1 
ATOM 2689 C CA  . VAL A 1 323 ? -70.681  42.960 14.387  1.00 84.17  ?  323 VAL A CA  1 
ATOM 2690 C C   . VAL A 1 323 ? -69.555  41.972 14.099  1.00 85.68  ?  323 VAL A C   1 
ATOM 2691 O O   . VAL A 1 323 ? -69.770  40.867 13.586  1.00 83.62  ?  323 VAL A O   1 
ATOM 2692 C CB  . VAL A 1 323 ? -70.986  43.040 15.891  1.00 73.81  ?  323 VAL A CB  1 
ATOM 2693 C CG1 . VAL A 1 323 ? -72.034  44.111 16.157  1.00 65.99  ?  323 VAL A CG1 1 
ATOM 2694 C CG2 . VAL A 1 323 ? -71.451  41.688 16.410  1.00 75.49  ?  323 VAL A CG2 1 
ATOM 2695 N N   . PHE A 1 324 ? -68.336  42.375 14.436  1.00 77.15  ?  324 PHE A N   1 
ATOM 2696 C CA  . PHE A 1 324 ? -67.171  41.561 14.100  1.00 81.59  ?  324 PHE A CA  1 
ATOM 2697 C C   . PHE A 1 324 ? -67.197  40.302 14.956  1.00 78.09  ?  324 PHE A C   1 
ATOM 2698 O O   . PHE A 1 324 ? -66.811  40.319 16.127  1.00 87.42  ?  324 PHE A O   1 
ATOM 2699 C CB  . PHE A 1 324 ? -65.885  42.350 14.308  1.00 92.26  ?  324 PHE A CB  1 
ATOM 2700 C CG  . PHE A 1 324 ? -64.642  41.540 14.086  1.00 84.43  ?  324 PHE A CG  1 
ATOM 2701 C CD1 . PHE A 1 324 ? -63.828  41.192 15.149  1.00 95.77  ?  324 PHE A CD1 1 
ATOM 2702 C CD2 . PHE A 1 324 ? -64.290  41.122 12.812  1.00 81.27  ?  324 PHE A CD2 1 
ATOM 2703 C CE1 . PHE A 1 324 ? -62.687  40.443 14.949  1.00 95.84  ?  324 PHE A CE1 1 
ATOM 2704 C CE2 . PHE A 1 324 ? -63.149  40.373 12.605  1.00 92.48  ?  324 PHE A CE2 1 
ATOM 2705 C CZ  . PHE A 1 324 ? -62.346  40.033 13.675  1.00 88.06  ?  324 PHE A CZ  1 
ATOM 2706 N N   . THR A 1 325 ? -67.673  39.204 14.369  1.00 67.17  ?  325 THR A N   1 
ATOM 2707 C CA  . THR A 1 325 ? -67.778  37.921 15.048  1.00 82.73  ?  325 THR A CA  1 
ATOM 2708 C C   . THR A 1 325 ? -66.561  37.067 14.713  1.00 75.96  ?  325 THR A C   1 
ATOM 2709 O O   . THR A 1 325 ? -66.469  36.513 13.610  1.00 82.82  ?  325 THR A O   1 
ATOM 2710 C CB  . THR A 1 325 ? -69.068  37.200 14.651  1.00 90.23  ?  325 THR A CB  1 
ATOM 2711 O OG1 . THR A 1 325 ? -70.188  38.059 14.897  1.00 88.56  ?  325 THR A OG1 1 
ATOM 2712 C CG2 . THR A 1 325 ? -69.234  35.925 15.460  1.00 91.90  ?  325 THR A CG2 1 
ATOM 2713 N N   . PRO A 1 326 ? -65.607  36.938 15.640  1.00 62.54  ?  326 PRO A N   1 
ATOM 2714 C CA  . PRO A 1 326 ? -64.365  36.223 15.319  1.00 82.35  ?  326 PRO A CA  1 
ATOM 2715 C C   . PRO A 1 326 ? -64.472  34.713 15.408  1.00 85.06  ?  326 PRO A C   1 
ATOM 2716 O O   . PRO A 1 326 ? -63.598  34.024 14.866  1.00 90.10  ?  326 PRO A O   1 
ATOM 2717 C CB  . PRO A 1 326 ? -63.380  36.762 16.363  1.00 72.42  ?  326 PRO A CB  1 
ATOM 2718 C CG  . PRO A 1 326 ? -64.248  37.050 17.545  1.00 79.95  ?  326 PRO A CG  1 
ATOM 2719 C CD  . PRO A 1 326 ? -65.583  37.507 16.998  1.00 76.56  ?  326 PRO A CD  1 
ATOM 2720 N N   . LYS A 1 327 ? -65.497  34.175 16.076  1.00 81.92  ?  327 LYS A N   1 
ATOM 2721 C CA  . LYS A 1 327 ? -65.581  32.727 16.248  1.00 86.00  ?  327 LYS A CA  1 
ATOM 2722 C C   . LYS A 1 327 ? -65.715  32.008 14.912  1.00 89.25  ?  327 LYS A C   1 
ATOM 2723 O O   . LYS A 1 327 ? -65.305  30.848 14.787  1.00 90.88  ?  327 LYS A O   1 
ATOM 2724 C CB  . LYS A 1 327 ? -66.747  32.368 17.173  1.00 92.38  ?  327 LYS A CB  1 
ATOM 2725 C CG  . LYS A 1 327 ? -66.721  30.924 17.661  1.00 104.58 ?  327 LYS A CG  1 
ATOM 2726 C CD  . LYS A 1 327 ? -67.742  30.674 18.762  1.00 128.30 ?  327 LYS A CD  1 
ATOM 2727 C CE  . LYS A 1 327 ? -67.605  29.267 19.329  1.00 132.23 ?  327 LYS A CE  1 
ATOM 2728 N NZ  . LYS A 1 327 ? -67.950  28.218 18.327  1.00 125.38 ?  327 LYS A NZ  1 
ATOM 2729 N N   . MET A 1 328 ? -66.278  32.675 13.901  1.00 84.97  ?  328 MET A N   1 
ATOM 2730 C CA  . MET A 1 328 ? -66.338  32.073 12.574  1.00 88.38  ?  328 MET A CA  1 
ATOM 2731 C C   . MET A 1 328 ? -64.955  31.964 11.947  1.00 84.65  ?  328 MET A C   1 
ATOM 2732 O O   . MET A 1 328 ? -64.719  31.072 11.124  1.00 88.26  ?  328 MET A O   1 
ATOM 2733 C CB  . MET A 1 328 ? -67.272  32.876 11.672  1.00 95.41  ?  328 MET A CB  1 
ATOM 2734 C CG  . MET A 1 328 ? -68.732  32.766 12.059  1.00 82.29  ?  328 MET A CG  1 
ATOM 2735 S SD  . MET A 1 328 ? -69.800  33.659 10.922  1.00 131.91 ?  328 MET A SD  1 
ATOM 2736 C CE  . MET A 1 328 ? -69.086  33.186 9.349   1.00 116.91 ?  328 MET A CE  1 
ATOM 2737 N N   . LEU A 1 329 ? -64.034  32.858 12.315  1.00 88.73  ?  329 LEU A N   1 
ATOM 2738 C CA  . LEU A 1 329 ? -62.652  32.705 11.877  1.00 89.47  ?  329 LEU A CA  1 
ATOM 2739 C C   . LEU A 1 329 ? -62.017  31.471 12.505  1.00 90.60  ?  329 LEU A C   1 
ATOM 2740 O O   . LEU A 1 329 ? -61.214  30.783 11.865  1.00 80.66  ?  329 LEU A O   1 
ATOM 2741 C CB  . LEU A 1 329 ? -61.847  33.958 12.217  1.00 59.57  ?  329 LEU A CB  1 
ATOM 2742 C CG  . LEU A 1 329 ? -62.300  35.250 11.536  1.00 78.83  ?  329 LEU A CG  1 
ATOM 2743 C CD1 . LEU A 1 329 ? -61.493  36.434 12.043  1.00 85.66  ?  329 LEU A CD1 1 
ATOM 2744 C CD2 . LEU A 1 329 ? -62.186  35.127 10.026  1.00 84.65  ?  329 LEU A CD2 1 
ATOM 2745 N N   . ILE A 1 330 ? -62.367  31.177 13.760  1.00 85.00  ?  330 ILE A N   1 
ATOM 2746 C CA  . ILE A 1 330 ? -61.919  29.938 14.387  1.00 83.34  ?  330 ILE A CA  1 
ATOM 2747 C C   . ILE A 1 330 ? -62.537  28.737 13.684  1.00 96.80  ?  330 ILE A C   1 
ATOM 2748 O O   . ILE A 1 330 ? -61.855  27.750 13.386  1.00 87.50  ?  330 ILE A O   1 
ATOM 2749 C CB  . ILE A 1 330 ? -62.253  29.941 15.890  1.00 84.37  ?  330 ILE A CB  1 
ATOM 2750 C CG1 . ILE A 1 330 ? -62.051  31.337 16.483  1.00 81.91  ?  330 ILE A CG1 1 
ATOM 2751 C CG2 . ILE A 1 330 ? -61.406  28.914 16.626  1.00 94.17  ?  330 ILE A CG2 1 
ATOM 2752 C CD1 . ILE A 1 330 ? -62.446  31.441 17.940  1.00 91.98  ?  330 ILE A CD1 1 
ATOM 2753 N N   . GLU A 1 331 ? -63.844  28.801 13.416  1.00 101.99 ?  331 GLU A N   1 
ATOM 2754 C CA  . GLU A 1 331 ? -64.493  27.739 12.655  1.00 99.49  ?  331 GLU A CA  1 
ATOM 2755 C C   . GLU A 1 331 ? -63.931  27.660 11.242  1.00 101.45 ?  331 GLU A C   1 
ATOM 2756 O O   . GLU A 1 331 ? -63.677  26.564 10.728  1.00 104.06 ?  331 GLU A O   1 
ATOM 2757 C CB  . GLU A 1 331 ? -66.005  27.962 12.624  1.00 105.57 ?  331 GLU A CB  1 
ATOM 2758 C CG  . GLU A 1 331 ? -66.663  27.933 13.994  1.00 117.81 ?  331 GLU A CG  1 
ATOM 2759 C CD  . GLU A 1 331 ? -68.161  28.154 13.926  1.00 137.31 ?  331 GLU A CD  1 
ATOM 2760 O OE1 . GLU A 1 331 ? -68.748  28.571 14.948  1.00 118.83 ?  331 GLU A OE1 1 
ATOM 2761 O OE2 . GLU A 1 331 ? -68.752  27.913 12.853  1.00 143.46 -1 331 GLU A OE2 1 
ATOM 2762 N N   . GLY A 1 332 ? -63.723  28.812 10.600  1.00 91.51  ?  332 GLY A N   1 
ATOM 2763 C CA  . GLY A 1 332 ? -63.105  28.815 9.286   1.00 82.84  ?  332 GLY A CA  1 
ATOM 2764 C C   . GLY A 1 332 ? -61.677  28.309 9.305   1.00 99.93  ?  332 GLY A C   1 
ATOM 2765 O O   . GLY A 1 332 ? -61.205  27.734 8.321   1.00 108.10 ?  332 GLY A O   1 
ATOM 2766 N N   . PHE A 1 333 ? -60.970  28.518 10.419  1.00 84.21  ?  333 PHE A N   1 
ATOM 2767 C CA  . PHE A 1 333 ? -59.622  27.976 10.557  1.00 79.90  ?  333 PHE A CA  1 
ATOM 2768 C C   . PHE A 1 333 ? -59.632  26.454 10.529  1.00 91.19  ?  333 PHE A C   1 
ATOM 2769 O O   . PHE A 1 333 ? -58.673  25.834 10.056  1.00 79.38  ?  333 PHE A O   1 
ATOM 2770 C CB  . PHE A 1 333 ? -58.986  28.488 11.850  1.00 94.99  ?  333 PHE A CB  1 
ATOM 2771 C CG  . PHE A 1 333 ? -57.819  27.670 12.324  1.00 98.71  ?  333 PHE A CG  1 
ATOM 2772 C CD1 . PHE A 1 333 ? -57.928  26.872 13.451  1.00 102.76 ?  333 PHE A CD1 1 
ATOM 2773 C CD2 . PHE A 1 333 ? -56.610  27.706 11.649  1.00 89.80  ?  333 PHE A CD2 1 
ATOM 2774 C CE1 . PHE A 1 333 ? -56.856  26.120 13.892  1.00 102.77 ?  333 PHE A CE1 1 
ATOM 2775 C CE2 . PHE A 1 333 ? -55.535  26.958 12.086  1.00 93.27  ?  333 PHE A CE2 1 
ATOM 2776 C CZ  . PHE A 1 333 ? -55.658  26.163 13.209  1.00 106.44 ?  333 PHE A CZ  1 
ATOM 2777 N N   . SER A 1 334 ? -60.708  25.838 11.018  1.00 107.48 ?  334 SER A N   1 
ATOM 2778 C CA  . SER A 1 334 ? -60.850  24.390 10.990  1.00 91.86  ?  334 SER A CA  1 
ATOM 2779 C C   . SER A 1 334 ? -61.745  23.896 9.862   1.00 91.94  ?  334 SER A C   1 
ATOM 2780 O O   . SER A 1 334 ? -61.668  22.715 9.507   1.00 101.17 ?  334 SER A O   1 
ATOM 2781 C CB  . SER A 1 334 ? -61.405  23.887 12.329  1.00 92.06  ?  334 SER A CB  1 
ATOM 2782 O OG  . SER A 1 334 ? -60.571  24.281 13.404  1.00 103.31 ?  334 SER A OG  1 
ATOM 2783 N N   . ASN A 1 335 ? -62.585  24.761 9.297   1.00 102.83 ?  335 ASN A N   1 
ATOM 2784 C CA  . ASN A 1 335 ? -63.432  24.361 8.183   1.00 106.87 ?  335 ASN A CA  1 
ATOM 2785 C C   . ASN A 1 335 ? -62.591  24.177 6.926   1.00 101.92 ?  335 ASN A C   1 
ATOM 2786 O O   . ASN A 1 335 ? -61.621  24.905 6.692   1.00 101.92 ?  335 ASN A O   1 
ATOM 2787 C CB  . ASN A 1 335 ? -64.525  25.406 7.942   1.00 96.85  ?  335 ASN A CB  1 
ATOM 2788 C CG  . ASN A 1 335 ? -65.580  24.946 6.945   1.00 99.98  ?  335 ASN A CG  1 
ATOM 2789 O OD1 . ASN A 1 335 ? -65.351  24.043 6.139   1.00 112.01 ?  335 ASN A OD1 1 
ATOM 2790 N ND2 . ASN A 1 335 ? -66.747  25.577 6.995   1.00 107.07 ?  335 ASN A ND2 1 
ATOM 2791 N N   . LYS A 1 336 ? -62.971  23.194 6.111   1.00 90.95  ?  336 LYS A N   1 
ATOM 2792 C CA  . LYS A 1 336 ? -62.279  22.924 4.859   1.00 87.45  ?  336 LYS A CA  1 
ATOM 2793 C C   . LYS A 1 336 ? -62.947  23.573 3.657   1.00 96.73  ?  336 LYS A C   1 
ATOM 2794 O O   . LYS A 1 336 ? -62.288  23.757 2.628   1.00 100.08 ?  336 LYS A O   1 
ATOM 2795 C CB  . LYS A 1 336 ? -62.168  21.411 4.636   1.00 95.76  ?  336 LYS A CB  1 
ATOM 2796 C CG  . LYS A 1 336 ? -61.626  20.670 5.849   1.00 102.32 ?  336 LYS A CG  1 
ATOM 2797 C CD  . LYS A 1 336 ? -61.470  19.183 5.591   1.00 104.06 ?  336 LYS A CD  1 
ATOM 2798 C CE  . LYS A 1 336 ? -61.091  18.454 6.871   1.00 120.75 ?  336 LYS A CE  1 
ATOM 2799 N NZ  . LYS A 1 336 ? -60.787  17.018 6.631   1.00 140.00 ?  336 LYS A NZ  1 
ATOM 2800 N N   . GLU A 1 337 ? -64.230  23.924 3.760   1.00 110.34 ?  337 GLU A N   1 
ATOM 2801 C CA  . GLU A 1 337 ? -64.874  24.735 2.734   1.00 107.04 ?  337 GLU A CA  1 
ATOM 2802 C C   . GLU A 1 337 ? -64.455  26.197 2.802   1.00 95.66  ?  337 GLU A C   1 
ATOM 2803 O O   . GLU A 1 337 ? -64.909  26.993 1.973   1.00 106.18 ?  337 GLU A O   1 
ATOM 2804 C CB  . GLU A 1 337 ? -66.396  24.627 2.850   1.00 124.80 ?  337 GLU A CB  1 
ATOM 2805 C CG  . GLU A 1 337 ? -66.966  23.298 2.378   1.00 131.74 ?  337 GLU A CG  1 
ATOM 2806 C CD  . GLU A 1 337 ? -68.475  23.330 2.226   1.00 147.54 ?  337 GLU A CD  1 
ATOM 2807 O OE1 . GLU A 1 337 ? -69.006  22.567 1.391   1.00 155.53 ?  337 GLU A OE1 1 
ATOM 2808 O OE2 . GLU A 1 337 ? -69.131  24.116 2.941   1.00 154.59 -1 337 GLU A OE2 1 
ATOM 2809 N N   . ILE A 1 338 ? -63.612  26.562 3.764   1.00 97.43  ?  338 ILE A N   1 
ATOM 2810 C CA  . ILE A 1 338 ? -63.074  27.910 3.895   1.00 104.70 ?  338 ILE A CA  1 
ATOM 2811 C C   . ILE A 1 338 ? -61.570  27.805 3.686   1.00 99.22  ?  338 ILE A C   1 
ATOM 2812 O O   . ILE A 1 338 ? -60.852  27.279 4.547   1.00 103.04 ?  338 ILE A O   1 
ATOM 2813 C CB  . ILE A 1 338 ? -63.404  28.534 5.257   1.00 90.03  ?  338 ILE A CB  1 
ATOM 2814 C CG1 . ILE A 1 338 ? -64.915  28.530 5.496   1.00 97.13  ?  338 ILE A CG1 1 
ATOM 2815 C CG2 . ILE A 1 338 ? -62.857  29.947 5.340   1.00 83.97  ?  338 ILE A CG2 1 
ATOM 2816 C CD1 . ILE A 1 338 ? -65.701  29.320 4.475   1.00 86.00  ?  338 ILE A CD1 1 
ATOM 2817 N N   . HIS A 1 339 ? -61.090  28.301 2.543   1.00 93.90  ?  339 HIS A N   1 
ATOM 2818 C CA  . HIS A 1 339 ? -59.681  28.138 2.198   1.00 99.93  ?  339 HIS A CA  1 
ATOM 2819 C C   . HIS A 1 339 ? -58.780  28.963 3.107   1.00 101.61 ?  339 HIS A C   1 
ATOM 2820 O O   . HIS A 1 339 ? -57.708  28.499 3.513   1.00 114.02 ?  339 HIS A O   1 
ATOM 2821 C CB  . HIS A 1 339 ? -59.452  28.515 0.735   1.00 107.71 ?  339 HIS A CB  1 
ATOM 2822 C CG  . HIS A 1 339 ? -60.240  27.688 -0.231  1.00 105.57 ?  339 HIS A CG  1 
ATOM 2823 N ND1 . HIS A 1 339 ? -61.491  28.054 -0.676  1.00 108.08 ?  339 HIS A ND1 1 
ATOM 2824 C CD2 . HIS A 1 339 ? -59.954  26.511 -0.836  1.00 96.66  ?  339 HIS A CD2 1 
ATOM 2825 C CE1 . HIS A 1 339 ? -61.943  27.139 -1.515  1.00 113.38 ?  339 HIS A CE1 1 
ATOM 2826 N NE2 . HIS A 1 339 ? -61.029  26.191 -1.629  1.00 115.69 ?  339 HIS A NE2 1 
ATOM 2827 N N   . PHE A 1 340 ? -59.190  30.186 3.433   1.00 101.96 ?  340 PHE A N   1 
ATOM 2828 C CA  . PHE A 1 340 ? -58.375  31.075 4.247   1.00 93.50  ?  340 PHE A CA  1 
ATOM 2829 C C   . PHE A 1 340 ? -59.292  32.054 4.968   1.00 87.16  ?  340 PHE A C   1 
ATOM 2830 O O   . PHE A 1 340 ? -60.511  32.050 4.779   1.00 83.29  ?  340 PHE A O   1 
ATOM 2831 C CB  . PHE A 1 340 ? -57.333  31.800 3.390   1.00 93.42  ?  340 PHE A CB  1 
ATOM 2832 C CG  . PHE A 1 340 ? -57.919  32.822 2.457   1.00 92.17  ?  340 PHE A CG  1 
ATOM 2833 C CD1 . PHE A 1 340 ? -58.469  32.440 1.245   1.00 93.37  ?  340 PHE A CD1 1 
ATOM 2834 C CD2 . PHE A 1 340 ? -57.913  34.166 2.791   1.00 87.96  ?  340 PHE A CD2 1 
ATOM 2835 C CE1 . PHE A 1 340 ? -59.007  33.380 0.386   1.00 105.36 ?  340 PHE A CE1 1 
ATOM 2836 C CE2 . PHE A 1 340 ? -58.448  35.110 1.937   1.00 81.85  ?  340 PHE A CE2 1 
ATOM 2837 C CZ  . PHE A 1 340 ? -58.995  34.717 0.732   1.00 103.36 ?  340 PHE A CZ  1 
ATOM 2838 N N   . GLN A 1 341 ? -58.693  32.902 5.799   1.00 83.74  ?  341 GLN A N   1 
ATOM 2839 C CA  . GLN A 1 341 ? -59.427  33.880 6.586   1.00 79.22  ?  341 GLN A CA  1 
ATOM 2840 C C   . GLN A 1 341 ? -58.977  35.285 6.212   1.00 84.16  ?  341 GLN A C   1 
ATOM 2841 O O   . GLN A 1 341 ? -57.845  35.496 5.766   1.00 93.37  ?  341 GLN A O   1 
ATOM 2842 C CB  . GLN A 1 341 ? -59.230  33.655 8.092   1.00 70.02  ?  341 GLN A CB  1 
ATOM 2843 C CG  . GLN A 1 341 ? -59.832  32.362 8.629   1.00 76.92  ?  341 GLN A CG  1 
ATOM 2844 C CD  . GLN A 1 341 ? -59.056  31.129 8.204   1.00 91.56  ?  341 GLN A CD  1 
ATOM 2845 O OE1 . GLN A 1 341 ? -59.637  30.085 7.915   1.00 96.29  ?  341 GLN A OE1 1 
ATOM 2846 N NE2 . GLN A 1 341 ? -57.734  31.245 8.171   1.00 93.05  ?  341 GLN A NE2 1 
ATOM 2847 N N   . PHE A 1 342 ? -59.873  36.248 6.403   1.00 73.95  ?  342 PHE A N   1 
ATOM 2848 C CA  . PHE A 1 342 ? -59.620  37.637 6.058   1.00 67.92  ?  342 PHE A CA  1 
ATOM 2849 C C   . PHE A 1 342 ? -59.831  38.521 7.279   1.00 71.92  ?  342 PHE A C   1 
ATOM 2850 O O   . PHE A 1 342 ? -60.676  38.238 8.133   1.00 96.74  ?  342 PHE A O   1 
ATOM 2851 C CB  . PHE A 1 342 ? -60.533  38.098 4.915   1.00 88.32  ?  342 PHE A CB  1 
ATOM 2852 C CG  . PHE A 1 342 ? -59.886  39.075 3.979   1.00 90.44  ?  342 PHE A CG  1 
ATOM 2853 C CD1 . PHE A 1 342 ? -59.839  40.424 4.290   1.00 90.00  ?  342 PHE A CD1 1 
ATOM 2854 C CD2 . PHE A 1 342 ? -59.325  38.647 2.787   1.00 79.12  ?  342 PHE A CD2 1 
ATOM 2855 C CE1 . PHE A 1 342 ? -59.245  41.327 3.431   1.00 102.27 ?  342 PHE A CE1 1 
ATOM 2856 C CE2 . PHE A 1 342 ? -58.729  39.546 1.923   1.00 83.25  ?  342 PHE A CE2 1 
ATOM 2857 C CZ  . PHE A 1 342 ? -58.690  40.888 2.246   1.00 93.89  ?  342 PHE A CZ  1 
ATOM 2858 N N   . ILE A 1 343 ? -59.044  39.592 7.362   1.00 73.97  ?  343 ILE A N   1 
ATOM 2859 C CA  . ILE A 1 343 ? -59.143  40.570 8.440   1.00 79.71  ?  343 ILE A CA  1 
ATOM 2860 C C   . ILE A 1 343 ? -59.177  41.952 7.806   1.00 67.86  ?  343 ILE A C   1 
ATOM 2861 O O   . ILE A 1 343 ? -58.202  42.369 7.168   1.00 74.76  ?  343 ILE A O   1 
ATOM 2862 C CB  . ILE A 1 343 ? -57.981  40.453 9.441   1.00 83.90  ?  343 ILE A CB  1 
ATOM 2863 C CG1 . ILE A 1 343 ? -57.905  39.032 10.009  1.00 75.42  ?  343 ILE A CG1 1 
ATOM 2864 C CG2 . ILE A 1 343 ? -58.141  41.467 10.564  1.00 78.26  ?  343 ILE A CG2 1 
ATOM 2865 C CD1 . ILE A 1 343 ? -56.738  38.804 10.946  1.00 70.17  ?  343 ILE A CD1 1 
ATOM 2866 N N   . ASN A 1 344 ? -60.294  42.659 7.981   1.00 75.39  ?  344 ASN A N   1 
ATOM 2867 C CA  . ASN A 1 344 ? -60.519  43.898 7.242   1.00 85.16  ?  344 ASN A CA  1 
ATOM 2868 C C   . ASN A 1 344 ? -59.614  45.021 7.736   1.00 73.45  ?  344 ASN A C   1 
ATOM 2869 O O   . ASN A 1 344 ? -58.772  45.530 6.988   1.00 82.20  ?  344 ASN A O   1 
ATOM 2870 C CB  . ASN A 1 344 ? -61.990  44.305 7.346   1.00 85.11  ?  344 ASN A CB  1 
ATOM 2871 C CG  . ASN A 1 344 ? -62.925  43.270 6.754   1.00 95.07  ?  344 ASN A CG  1 
ATOM 2872 O OD1 . ASN A 1 344 ? -62.506  42.168 6.400   1.00 102.66 ?  344 ASN A OD1 1 
ATOM 2873 N ND2 . ASN A 1 344 ? -64.201  43.620 6.641   1.00 97.86  ?  344 ASN A ND2 1 
ATOM 2874 N N   . ASP A 1 345 ? -59.766  45.416 8.994   1.00 75.49  ?  345 ASP A N   1 
ATOM 2875 C CA  . ASP A 1 345 ? -59.090  46.587 9.541   1.00 86.15  ?  345 ASP A CA  1 
ATOM 2876 C C   . ASP A 1 345 ? -58.142  46.177 10.667  1.00 83.90  ?  345 ASP A C   1 
ATOM 2877 O O   . ASP A 1 345 ? -57.957  44.994 10.962  1.00 81.57  ?  345 ASP A O   1 
ATOM 2878 C CB  . ASP A 1 345 ? -60.113  47.621 10.025  1.00 94.56  ?  345 ASP A CB  1 
ATOM 2879 C CG  . ASP A 1 345 ? -60.803  47.205 11.310  1.00 102.34 ?  345 ASP A CG  1 
ATOM 2880 O OD1 . ASP A 1 345 ? -60.217  47.396 12.395  1.00 100.97 ?  345 ASP A OD1 1 
ATOM 2881 O OD2 . ASP A 1 345 ? -61.938  46.688 11.235  1.00 110.86 -1 345 ASP A OD2 1 
ATOM 2882 N N   . ILE A 1 346 ? -57.538  47.183 11.296  1.00 90.82  ?  346 ILE A N   1 
ATOM 2883 C CA  . ILE A 1 346 ? -56.540  46.951 12.337  1.00 96.14  ?  346 ILE A CA  1 
ATOM 2884 C C   . ILE A 1 346 ? -57.190  46.761 13.704  1.00 98.96  ?  346 ILE A C   1 
ATOM 2885 O O   . ILE A 1 346 ? -56.765  45.905 14.483  1.00 100.14 ?  346 ILE A O   1 
ATOM 2886 C CB  . ILE A 1 346 ? -55.523  48.111 12.347  1.00 95.52  ?  346 ILE A CB  1 
ATOM 2887 C CG1 . ILE A 1 346 ? -54.670  48.086 13.618  1.00 85.63  ?  346 ILE A CG1 1 
ATOM 2888 C CG2 . ILE A 1 346 ? -56.234  49.452 12.196  1.00 98.58  ?  346 ILE A CG2 1 
ATOM 2889 C CD1 . ILE A 1 346 ? -53.773  46.868 13.729  1.00 83.21  ?  346 ILE A CD1 1 
ATOM 2890 N N   . ASP A 1 347 ? -58.221  47.550 14.021  1.00 103.97 ?  347 ASP A N   1 
ATOM 2891 C CA  . ASP A 1 347 ? -58.895  47.403 15.308  1.00 100.37 ?  347 ASP A CA  1 
ATOM 2892 C C   . ASP A 1 347 ? -59.490  46.008 15.459  1.00 90.73  ?  347 ASP A C   1 
ATOM 2893 O O   . ASP A 1 347 ? -59.490  45.439 16.558  1.00 99.86  ?  347 ASP A O   1 
ATOM 2894 C CB  . ASP A 1 347 ? -59.977  48.472 15.457  1.00 105.14 ?  347 ASP A CB  1 
ATOM 2895 C CG  . ASP A 1 347 ? -59.433  49.878 15.288  1.00 111.66 ?  347 ASP A CG  1 
ATOM 2896 O OD1 . ASP A 1 347 ? -58.195  50.044 15.307  1.00 112.26 ?  347 ASP A OD1 1 
ATOM 2897 O OD2 . ASP A 1 347 ? -60.243  50.816 15.133  1.00 128.82 -1 347 ASP A OD2 1 
ATOM 2898 N N   . ASP A 1 348 ? -59.996  45.438 14.365  1.00 87.96  ?  348 ASP A N   1 
ATOM 2899 C CA  . ASP A 1 348 ? -60.483  44.065 14.385  1.00 98.18  ?  348 ASP A CA  1 
ATOM 2900 C C   . ASP A 1 348 ? -59.355  43.045 14.445  1.00 89.92  ?  348 ASP A C   1 
ATOM 2901 O O   . ASP A 1 348 ? -59.620  41.869 14.716  1.00 93.02  ?  348 ASP A O   1 
ATOM 2902 C CB  . ASP A 1 348 ? -61.354  43.796 13.155  1.00 87.74  ?  348 ASP A CB  1 
ATOM 2903 C CG  . ASP A 1 348 ? -62.622  44.630 13.143  1.00 99.56  ?  348 ASP A CG  1 
ATOM 2904 O OD1 . ASP A 1 348 ? -62.846  45.390 14.109  1.00 114.59 ?  348 ASP A OD1 1 
ATOM 2905 O OD2 . ASP A 1 348 ? -63.394  44.525 12.167  1.00 87.74  -1 348 ASP A OD2 1 
ATOM 2906 N N   . PHE A 1 349 ? -58.111  43.463 14.203  1.00 87.95  ?  349 PHE A N   1 
ATOM 2907 C CA  . PHE A 1 349 ? -56.987  42.534 14.232  1.00 88.57  ?  349 PHE A CA  1 
ATOM 2908 C C   . PHE A 1 349 ? -56.557  42.228 15.663  1.00 88.10  ?  349 PHE A C   1 
ATOM 2909 O O   . PHE A 1 349 ? -56.338  41.065 16.016  1.00 77.18  ?  349 PHE A O   1 
ATOM 2910 C CB  . PHE A 1 349 ? -55.817  43.102 13.425  1.00 93.94  ?  349 PHE A CB  1 
ATOM 2911 C CG  . PHE A 1 349 ? -54.586  42.244 13.452  1.00 84.24  ?  349 PHE A CG  1 
ATOM 2912 C CD1 . PHE A 1 349 ? -53.347  42.794 13.738  1.00 58.28  ?  349 PHE A CD1 1 
ATOM 2913 C CD2 . PHE A 1 349 ? -54.667  40.887 13.191  1.00 84.93  ?  349 PHE A CD2 1 
ATOM 2914 C CE1 . PHE A 1 349 ? -52.212  42.005 13.762  1.00 76.59  ?  349 PHE A CE1 1 
ATOM 2915 C CE2 . PHE A 1 349 ? -53.537  40.094 13.214  1.00 83.69  ?  349 PHE A CE2 1 
ATOM 2916 C CZ  . PHE A 1 349 ? -52.308  40.653 13.500  1.00 84.23  ?  349 PHE A CZ  1 
ATOM 2917 N N   . ASN A 1 350 ? -56.424  43.264 16.497  1.00 83.86  ?  350 ASN A N   1 
ATOM 2918 C CA  . ASN A 1 350 ? -56.076  43.043 17.897  1.00 83.91  ?  350 ASN A CA  1 
ATOM 2919 C C   . ASN A 1 350 ? -57.144  42.219 18.603  1.00 95.89  ?  350 ASN A C   1 
ATOM 2920 O O   . ASN A 1 350 ? -56.827  41.337 19.410  1.00 102.09 ?  350 ASN A O   1 
ATOM 2921 C CB  . ASN A 1 350 ? -55.876  44.381 18.609  1.00 93.95  ?  350 ASN A CB  1 
ATOM 2922 C CG  . ASN A 1 350 ? -54.864  45.267 17.913  1.00 93.58  ?  350 ASN A CG  1 
ATOM 2923 O OD1 . ASN A 1 350 ? -53.891  44.784 17.334  1.00 104.64 ?  350 ASN A OD1 1 
ATOM 2924 N ND2 . ASN A 1 350 ? -55.086  46.575 17.970  1.00 75.61  ?  350 ASN A ND2 1 
ATOM 2925 N N   . GLU A 1 351 ? -58.417  42.493 18.310  1.00 88.05  ?  351 GLU A N   1 
ATOM 2926 C CA  . GLU A 1 351 ? -59.504  41.716 18.890  1.00 100.01 ?  351 GLU A CA  1 
ATOM 2927 C C   . GLU A 1 351 ? -59.490  40.268 18.418  1.00 85.11  ?  351 GLU A C   1 
ATOM 2928 O O   . GLU A 1 351 ? -60.026  39.397 19.112  1.00 87.78  ?  351 GLU A O   1 
ATOM 2929 C CB  . GLU A 1 351 ? -60.845  42.369 18.553  1.00 96.17  ?  351 GLU A CB  1 
ATOM 2930 C CG  . GLU A 1 351 ? -61.977  42.004 19.497  1.00 116.81 ?  351 GLU A CG  1 
ATOM 2931 C CD  . GLU A 1 351 ? -63.281  42.685 19.128  1.00 131.69 ?  351 GLU A CD  1 
ATOM 2932 O OE1 . GLU A 1 351 ? -63.938  42.236 18.167  1.00 122.12 ?  351 GLU A OE1 1 
ATOM 2933 O OE2 . GLU A 1 351 ? -63.646  43.673 19.801  1.00 152.48 -1 351 GLU A OE2 1 
ATOM 2934 N N   . THR A 1 352 ? -58.887  39.991 17.260  1.00 85.61  ?  352 THR A N   1 
ATOM 2935 C CA  . THR A 1 352 ? -58.782  38.618 16.781  1.00 84.30  ?  352 THR A CA  1 
ATOM 2936 C C   . THR A 1 352 ? -57.719  37.832 17.538  1.00 87.25  ?  352 THR A C   1 
ATOM 2937 O O   . THR A 1 352 ? -57.847  36.611 17.685  1.00 72.91  ?  352 THR A O   1 
ATOM 2938 C CB  . THR A 1 352 ? -58.474  38.603 15.281  1.00 77.82  ?  352 THR A CB  1 
ATOM 2939 O OG1 . THR A 1 352 ? -59.258  39.604 14.618  1.00 83.54  ?  352 THR A OG1 1 
ATOM 2940 C CG2 . THR A 1 352 ? -58.792  37.239 14.682  1.00 61.27  ?  352 THR A CG2 1 
ATOM 2941 N N   . LEU A 1 353 ? -56.675  38.506 18.025  1.00 98.86  ?  353 LEU A N   1 
ATOM 2942 C CA  . LEU A 1 353 ? -55.634  37.815 18.780  1.00 101.39 ?  353 LEU A CA  1 
ATOM 2943 C C   . LEU A 1 353 ? -56.135  37.394 20.156  1.00 100.70 ?  353 LEU A C   1 
ATOM 2944 O O   . LEU A 1 353 ? -55.820  36.296 20.629  1.00 102.34 ?  353 LEU A O   1 
ATOM 2945 C CB  . LEU A 1 353 ? -54.398  38.706 18.915  1.00 100.18 ?  353 LEU A CB  1 
ATOM 2946 C CG  . LEU A 1 353 ? -53.292  38.618 17.859  1.00 79.02  ?  353 LEU A CG  1 
ATOM 2947 C CD1 . LEU A 1 353 ? -53.860  38.566 16.451  1.00 78.32  ?  353 LEU A CD1 1 
ATOM 2948 C CD2 . LEU A 1 353 ? -52.329  39.786 18.004  1.00 90.74  ?  353 LEU A CD2 1 
ATOM 2949 N N   . ASN A 1 354 ? -56.913  38.258 20.813  1.00 94.22  ?  354 ASN A N   1 
ATOM 2950 C CA  . ASN A 1 354 ? -57.384  37.973 22.163  1.00 101.86 ?  354 ASN A CA  1 
ATOM 2951 C C   . ASN A 1 354 ? -58.323  36.775 22.216  1.00 99.09  ?  354 ASN A C   1 
ATOM 2952 O O   . ASN A 1 354 ? -58.471  36.165 23.281  1.00 126.85 ?  354 ASN A O   1 
ATOM 2953 C CB  . ASN A 1 354 ? -58.083  39.205 22.742  1.00 101.41 ?  354 ASN A CB  1 
ATOM 2954 C CG  . ASN A 1 354 ? -57.360  40.497 22.408  1.00 109.14 ?  354 ASN A CG  1 
ATOM 2955 O OD1 . ASN A 1 354 ? -56.171  40.492 22.089  1.00 112.36 ?  354 ASN A OD1 1 
ATOM 2956 N ND2 . ASN A 1 354 ? -58.079  41.612 22.480  1.00 107.14 ?  354 ASN A ND2 1 
ATOM 2957 N N   . SER A 1 355 ? -58.958  36.423 21.098  1.00 80.43  ?  355 SER A N   1 
ATOM 2958 C CA  . SER A 1 355 ? -59.938  35.347 21.056  1.00 95.31  ?  355 SER A CA  1 
ATOM 2959 C C   . SER A 1 355 ? -59.342  34.026 20.579  1.00 87.07  ?  355 SER A C   1 
ATOM 2960 O O   . SER A 1 355 ? -60.089  33.114 20.210  1.00 93.14  ?  355 SER A O   1 
ATOM 2961 C CB  . SER A 1 355 ? -61.116  35.745 20.166  1.00 89.73  ?  355 SER A CB  1 
ATOM 2962 O OG  . SER A 1 355 ? -61.632  37.011 20.541  1.00 96.09  ?  355 SER A OG  1 
ATOM 2963 N N   . ILE A 1 356 ? -58.016  33.903 20.579  1.00 86.68  ?  356 ILE A N   1 
ATOM 2964 C CA  . ILE A 1 356 ? -57.332  32.700 20.120  1.00 100.02 ?  356 ILE A CA  1 
ATOM 2965 C C   . ILE A 1 356 ? -56.389  32.227 21.217  1.00 105.32 ?  356 ILE A C   1 
ATOM 2966 O O   . ILE A 1 356 ? -55.698  33.038 21.845  1.00 106.55 ?  356 ILE A O   1 
ATOM 2967 C CB  . ILE A 1 356 ? -56.565  32.952 18.804  1.00 103.57 ?  356 ILE A CB  1 
ATOM 2968 C CG1 . ILE A 1 356 ? -57.524  33.413 17.705  1.00 93.55  ?  356 ILE A CG1 1 
ATOM 2969 C CG2 . ILE A 1 356 ? -55.826  31.705 18.362  1.00 94.40  ?  356 ILE A CG2 1 
ATOM 2970 C CD1 . ILE A 1 356 ? -56.853  33.648 16.370  1.00 78.50  ?  356 ILE A CD1 1 
ATOM 2971 N N   . ASN A 1 357 ? -56.359  30.915 21.447  1.00 110.09 ?  357 ASN A N   1 
ATOM 2972 C CA  . ASN A 1 357 ? -55.564  30.316 22.514  1.00 108.38 ?  357 ASN A CA  1 
ATOM 2973 C C   . ASN A 1 357 ? -54.654  29.221 21.974  1.00 108.64 ?  357 ASN A C   1 
ATOM 2974 O O   . ASN A 1 357 ? -54.510  28.154 22.578  1.00 109.93 ?  357 ASN A O   1 
ATOM 2975 C CB  . ASN A 1 357 ? -56.461  29.765 23.620  1.00 105.95 ?  357 ASN A CB  1 
ATOM 2976 C CG  . ASN A 1 357 ? -57.353  30.825 24.230  1.00 123.07 ?  357 ASN A CG  1 
ATOM 2977 O OD1 . ASN A 1 357 ? -57.020  32.010 24.229  1.00 127.29 ?  357 ASN A OD1 1 
ATOM 2978 N ND2 . ASN A 1 357 ? -58.497  30.403 24.756  1.00 139.06 ?  357 ASN A ND2 1 
ATOM 2979 N N   . ILE A 1 358 ? -54.024  29.464 20.827  1.00 98.68  ?  358 ILE A N   1 
ATOM 2980 C CA  . ILE A 1 358 ? -53.008  28.578 20.275  1.00 100.80 ?  358 ILE A CA  1 
ATOM 2981 C C   . ILE A 1 358 ? -51.853  29.430 19.759  1.00 94.96  ?  358 ILE A C   1 
ATOM 2982 O O   . ILE A 1 358 ? -51.871  30.661 19.854  1.00 82.81  ?  358 ILE A O   1 
ATOM 2983 C CB  . ILE A 1 358 ? -53.559  27.659 19.164  1.00 93.69  ?  358 ILE A CB  1 
ATOM 2984 C CG1 . ILE A 1 358 ? -54.544  28.412 18.270  1.00 98.60  ?  358 ILE A CG1 1 
ATOM 2985 C CG2 . ILE A 1 358 ? -54.210  26.422 19.770  1.00 86.36  ?  358 ILE A CG2 1 
ATOM 2986 C CD1 . ILE A 1 358 ? -55.058  27.591 17.109  1.00 98.27  ?  358 ILE A CD1 1 
ATOM 2987 N N   . ARG A 1 359 ? -50.835  28.758 19.222  1.00 92.02  ?  359 ARG A N   1 
ATOM 2988 C CA  . ARG A 1 359 ? -49.644  29.441 18.731  1.00 94.52  ?  359 ARG A CA  1 
ATOM 2989 C C   . ARG A 1 359 ? -50.007  30.465 17.662  1.00 98.47  ?  359 ARG A C   1 
ATOM 2990 O O   . ARG A 1 359 ? -50.812  30.196 16.766  1.00 101.84 ?  359 ARG A O   1 
ATOM 2991 C CB  . ARG A 1 359 ? -48.651  28.422 18.170  1.00 100.63 ?  359 ARG A CB  1 
ATOM 2992 C CG  . ARG A 1 359 ? -47.497  29.023 17.380  1.00 104.73 ?  359 ARG A CG  1 
ATOM 2993 C CD  . ARG A 1 359 ? -46.264  29.220 18.242  1.00 107.14 ?  359 ARG A CD  1 
ATOM 2994 N NE  . ARG A 1 359 ? -45.081  29.524 17.442  1.00 101.41 ?  359 ARG A NE  1 
ATOM 2995 C CZ  . ARG A 1 359 ? -43.863  29.693 17.945  1.00 101.96 ?  359 ARG A CZ  1 
ATOM 2996 N NH1 . ARG A 1 359 ? -43.661  29.583 19.251  1.00 119.75 ?  359 ARG A NH1 1 
ATOM 2997 N NH2 . ARG A 1 359 ? -42.844  29.969 17.142  1.00 95.56  ?  359 ARG A NH2 1 
ATOM 2998 N N   . LYS A 1 360 ? -49.402  31.648 17.761  1.00 90.82  ?  360 LYS A N   1 
ATOM 2999 C CA  . LYS A 1 360 ? -49.662  32.746 16.838  1.00 88.36  ?  360 LYS A CA  1 
ATOM 3000 C C   . LYS A 1 360 ? -48.341  33.253 16.283  1.00 87.75  ?  360 LYS A C   1 
ATOM 3001 O O   . LYS A 1 360 ? -47.442  33.617 17.048  1.00 97.25  ?  360 LYS A O   1 
ATOM 3002 C CB  . LYS A 1 360 ? -50.423  33.881 17.530  1.00 70.78  ?  360 LYS A CB  1 
ATOM 3003 C CG  . LYS A 1 360 ? -51.916  33.631 17.663  1.00 75.52  ?  360 LYS A CG  1 
ATOM 3004 C CD  . LYS A 1 360 ? -52.576  34.681 18.540  1.00 91.26  ?  360 LYS A CD  1 
ATOM 3005 C CE  . LYS A 1 360 ? -52.121  34.556 19.985  1.00 86.96  ?  360 LYS A CE  1 
ATOM 3006 N NZ  . LYS A 1 360 ? -52.784  35.562 20.859  1.00 82.97  ?  360 LYS A NZ  1 
ATOM 3007 N N   . GLU A 1 361 ? -48.228  33.274 14.958  1.00 85.35  ?  361 GLU A N   1 
ATOM 3008 C CA  . GLU A 1 361 ? -47.063  33.798 14.266  1.00 78.85  ?  361 GLU A CA  1 
ATOM 3009 C C   . GLU A 1 361 ? -47.491  34.940 13.354  1.00 85.52  ?  361 GLU A C   1 
ATOM 3010 O O   . GLU A 1 361 ? -48.646  35.021 12.926  1.00 98.59  ?  361 GLU A O   1 
ATOM 3011 C CB  . GLU A 1 361 ? -46.358  32.706 13.449  1.00 77.02  ?  361 GLU A CB  1 
ATOM 3012 C CG  . GLU A 1 361 ? -46.066  31.432 14.230  1.00 80.09  ?  361 GLU A CG  1 
ATOM 3013 C CD  . GLU A 1 361 ? -45.350  30.385 13.397  1.00 102.42 ?  361 GLU A CD  1 
ATOM 3014 O OE1 . GLU A 1 361 ? -44.883  30.722 12.288  1.00 121.31 ?  361 GLU A OE1 1 
ATOM 3015 O OE2 . GLU A 1 361 ? -45.255  29.225 13.849  1.00 96.69  -1 361 GLU A OE2 1 
ATOM 3016 N N   . VAL A 1 362 ? -46.548  35.832 13.060  1.00 82.36  ?  362 VAL A N   1 
ATOM 3017 C CA  . VAL A 1 362 ? -46.810  37.002 12.232  1.00 75.77  ?  362 VAL A CA  1 
ATOM 3018 C C   . VAL A 1 362 ? -45.740  37.090 11.154  1.00 79.53  ?  362 VAL A C   1 
ATOM 3019 O O   . VAL A 1 362 ? -44.543  37.013 11.453  1.00 93.60  ?  362 VAL A O   1 
ATOM 3020 C CB  . VAL A 1 362 ? -46.845  38.300 13.060  1.00 66.13  ?  362 VAL A CB  1 
ATOM 3021 C CG1 . VAL A 1 362 ? -46.979  39.493 12.140  1.00 66.51  ?  362 VAL A CG1 1 
ATOM 3022 C CG2 . VAL A 1 362 ? -47.991  38.265 14.059  1.00 73.34  ?  362 VAL A CG2 1 
ATOM 3023 N N   . TYR A 1 363 ? -46.172  37.246 9.906   1.00 69.22  ?  363 TYR A N   1 
ATOM 3024 C CA  . TYR A 1 363 ? -45.286  37.419 8.758   1.00 62.89  ?  363 TYR A CA  1 
ATOM 3025 C C   . TYR A 1 363 ? -45.702  38.718 8.074   1.00 79.20  ?  363 TYR A C   1 
ATOM 3026 O O   . TYR A 1 363 ? -46.570  38.719 7.197   1.00 88.49  ?  363 TYR A O   1 
ATOM 3027 C CB  . TYR A 1 363 ? -45.365  36.224 7.800   1.00 72.99  ?  363 TYR A CB  1 
ATOM 3028 C CG  . TYR A 1 363 ? -45.036  34.883 8.427   1.00 77.03  ?  363 TYR A CG  1 
ATOM 3029 C CD1 . TYR A 1 363 ? -43.826  34.253 8.168   1.00 81.85  ?  363 TYR A CD1 1 
ATOM 3030 C CD2 . TYR A 1 363 ? -45.943  34.239 9.259   1.00 88.38  ?  363 TYR A CD2 1 
ATOM 3031 C CE1 . TYR A 1 363 ? -43.522  33.027 8.732   1.00 98.94  ?  363 TYR A CE1 1 
ATOM 3032 C CE2 . TYR A 1 363 ? -45.648  33.013 9.828   1.00 91.65  ?  363 TYR A CE2 1 
ATOM 3033 C CZ  . TYR A 1 363 ? -44.437  32.411 9.561   1.00 95.03  ?  363 TYR A CZ  1 
ATOM 3034 O OH  . TYR A 1 363 ? -44.140  31.191 10.123  1.00 93.80  ?  363 TYR A OH  1 
ATOM 3035 N N   . GLN A 1 364 ? -45.088  39.826 8.478   1.00 83.74  ?  364 GLN A N   1 
ATOM 3036 C CA  . GLN A 1 364 ? -45.447  41.139 7.963   1.00 83.05  ?  364 GLN A CA  1 
ATOM 3037 C C   . GLN A 1 364 ? -44.494  41.560 6.852   1.00 76.95  ?  364 GLN A C   1 
ATOM 3038 O O   . GLN A 1 364 ? -43.281  41.351 6.945   1.00 87.00  ?  364 GLN A O   1 
ATOM 3039 C CB  . GLN A 1 364 ? -45.435  42.191 9.074   1.00 69.22  ?  364 GLN A CB  1 
ATOM 3040 C CG  . GLN A 1 364 ? -45.742  43.588 8.570   1.00 77.72  ?  364 GLN A CG  1 
ATOM 3041 C CD  . GLN A 1 364 ? -45.957  44.581 9.685   1.00 88.71  ?  364 GLN A CD  1 
ATOM 3042 O OE1 . GLN A 1 364 ? -46.402  45.703 9.450   1.00 86.99  ?  364 GLN A OE1 1 
ATOM 3043 N NE2 . GLN A 1 364 ? -45.631  44.181 10.906  1.00 97.35  ?  364 GLN A NE2 1 
ATOM 3044 N N   . PHE A 1 365 ? -45.056  42.155 5.802   1.00 90.02  ?  365 PHE A N   1 
ATOM 3045 C CA  . PHE A 1 365 ? -44.291  42.693 4.688   1.00 76.54  ?  365 PHE A CA  1 
ATOM 3046 C C   . PHE A 1 365 ? -44.767  44.108 4.397   1.00 87.75  ?  365 PHE A C   1 
ATOM 3047 O O   . PHE A 1 365 ? -45.939  44.438 4.595   1.00 98.91  ?  365 PHE A O   1 
ATOM 3048 C CB  . PHE A 1 365 ? -44.428  41.817 3.433   1.00 64.98  ?  365 PHE A CB  1 
ATOM 3049 C CG  . PHE A 1 365 ? -44.129  40.361 3.669   1.00 72.87  ?  365 PHE A CG  1 
ATOM 3050 C CD1 . PHE A 1 365 ? -42.872  39.847 3.399   1.00 89.57  ?  365 PHE A CD1 1 
ATOM 3051 C CD2 . PHE A 1 365 ? -45.103  39.507 4.161   1.00 82.58  ?  365 PHE A CD2 1 
ATOM 3052 C CE1 . PHE A 1 365 ? -42.592  38.509 3.613   1.00 100.05 ?  365 PHE A CE1 1 
ATOM 3053 C CE2 . PHE A 1 365 ? -44.830  38.169 4.377   1.00 89.29  ?  365 PHE A CE2 1 
ATOM 3054 C CZ  . PHE A 1 365 ? -43.573  37.670 4.103   1.00 90.48  ?  365 PHE A CZ  1 
ATOM 3055 N N   . TYR A 1 366 ? -43.845  44.944 3.926   1.00 81.94  ?  366 TYR A N   1 
ATOM 3056 C CA  . TYR A 1 366 ? -44.149  46.349 3.686   1.00 89.82  ?  366 TYR A CA  1 
ATOM 3057 C C   . TYR A 1 366 ? -43.138  46.915 2.701   1.00 96.92  ?  366 TYR A C   1 
ATOM 3058 O O   . TYR A 1 366 ? -42.107  46.302 2.411   1.00 97.15  ?  366 TYR A O   1 
ATOM 3059 C CB  . TYR A 1 366 ? -44.145  47.151 4.992   1.00 100.75 ?  366 TYR A CB  1 
ATOM 3060 C CG  . TYR A 1 366 ? -42.766  47.351 5.581   1.00 98.65  ?  366 TYR A CG  1 
ATOM 3061 C CD1 . TYR A 1 366 ? -42.093  46.302 6.194   1.00 94.37  ?  366 TYR A CD1 1 
ATOM 3062 C CD2 . TYR A 1 366 ? -42.136  48.587 5.524   1.00 94.95  ?  366 TYR A CD2 1 
ATOM 3063 C CE1 . TYR A 1 366 ? -40.833  46.477 6.732   1.00 79.10  ?  366 TYR A CE1 1 
ATOM 3064 C CE2 . TYR A 1 366 ? -40.875  48.772 6.061   1.00 92.65  ?  366 TYR A CE2 1 
ATOM 3065 C CZ  . TYR A 1 366 ? -40.230  47.713 6.663   1.00 84.97  ?  366 TYR A CZ  1 
ATOM 3066 O OH  . TYR A 1 366 ? -38.975  47.891 7.200   1.00 91.17  ?  366 TYR A OH  1 
ATOM 3067 N N   . THR A 1 367 ? -43.451  48.103 2.188   1.00 112.51 ?  367 THR A N   1 
ATOM 3068 C CA  . THR A 1 367 ? -42.574  48.835 1.283   1.00 111.46 ?  367 THR A CA  1 
ATOM 3069 C C   . THR A 1 367 ? -42.065  50.133 1.891   1.00 107.82 ?  367 THR A C   1 
ATOM 3070 O O   . THR A 1 367 ? -40.852  50.362 1.938   1.00 127.58 ?  367 THR A O   1 
ATOM 3071 C CB  . THR A 1 367 ? -43.301  49.131 -0.038  1.00 111.25 ?  367 THR A CB  1 
ATOM 3072 O OG1 . THR A 1 367 ? -44.445  49.955 0.217   1.00 114.87 ?  367 THR A OG1 1 
ATOM 3073 C CG2 . THR A 1 367 ? -43.751  47.837 -0.700  1.00 103.23 ?  367 THR A CG2 1 
ATOM 3074 N N   . GLU A 1 368 ? -42.966  50.994 2.364   1.00 89.65  ?  368 GLU A N   1 
ATOM 3075 C CA  . GLU A 1 368 ? -42.580  52.259 2.977   1.00 104.59 ?  368 GLU A CA  1 
ATOM 3076 C C   . GLU A 1 368 ? -43.152  52.481 4.368   1.00 108.16 ?  368 GLU A C   1 
ATOM 3077 O O   . GLU A 1 368 ? -42.643  53.351 5.085   1.00 110.47 ?  368 GLU A O   1 
ATOM 3078 C CB  . GLU A 1 368 ? -42.993  53.439 2.083   1.00 120.06 ?  368 GLU A CB  1 
ATOM 3079 C CG  . GLU A 1 368 ? -42.246  53.513 0.760   1.00 133.91 ?  368 GLU A CG  1 
ATOM 3080 C CD  . GLU A 1 368 ? -42.640  54.723 -0.065  1.00 153.58 ?  368 GLU A CD  1 
ATOM 3081 O OE1 . GLU A 1 368 ? -42.343  54.740 -1.278  1.00 157.07 ?  368 GLU A OE1 1 
ATOM 3082 O OE2 . GLU A 1 368 ? -43.247  55.658 0.500   1.00 163.44 -1 368 GLU A OE2 1 
ATOM 3083 N N   . ASN A 1 369 ? -44.179  51.739 4.778   1.00 105.05 ?  369 ASN A N   1 
ATOM 3084 C CA  . ASN A 1 369 ? -44.784  51.906 6.095   1.00 108.92 ?  369 ASN A CA  1 
ATOM 3085 C C   . ASN A 1 369 ? -45.049  50.536 6.698   1.00 107.11 ?  369 ASN A C   1 
ATOM 3086 O O   . ASN A 1 369 ? -45.776  49.727 6.115   1.00 100.15 ?  369 ASN A O   1 
ATOM 3087 C CB  . ASN A 1 369 ? -46.082  52.716 6.012   1.00 103.57 ?  369 ASN A CB  1 
ATOM 3088 C CG  . ASN A 1 369 ? -45.831  54.198 5.806   1.00 125.65 ?  369 ASN A CG  1 
ATOM 3089 O OD1 . ASN A 1 369 ? -44.865  54.753 6.329   1.00 125.70 ?  369 ASN A OD1 1 
ATOM 3090 N ND2 . ASN A 1 369 ? -46.702  54.846 5.042   1.00 127.98 ?  369 ASN A ND2 1 
ATOM 3091 N N   . CYS A 1 370 ? -44.463  50.281 7.863   1.00 109.33 ?  370 CYS A N   1 
ATOM 3092 C CA  . CYS A 1 370 ? -44.653  49.035 8.588   1.00 103.92 ?  370 CYS A CA  1 
ATOM 3093 C C   . CYS A 1 370 ? -45.553  49.276 9.793   1.00 107.90 ?  370 CYS A C   1 
ATOM 3094 O O   . CYS A 1 370 ? -45.609  50.384 10.335  1.00 113.96 ?  370 CYS A O   1 
ATOM 3095 C CB  . CYS A 1 370 ? -43.308  48.455 9.040   1.00 102.78 ?  370 CYS A CB  1 
ATOM 3096 S SG  . CYS A 1 370 ? -43.381  46.763 9.664   1.00 125.17 ?  370 CYS A SG  1 
ATOM 3097 N N   . LEU A 1 371 ? -46.259  48.229 10.209  1.00 101.67 ?  371 LEU A N   1 
ATOM 3098 C CA  . LEU A 1 371 ? -47.197  48.310 11.320  1.00 110.81 ?  371 LEU A CA  1 
ATOM 3099 C C   . LEU A 1 371 ? -46.532  47.809 12.595  1.00 116.58 ?  371 LEU A C   1 
ATOM 3100 O O   . LEU A 1 371 ? -45.977  46.706 12.619  1.00 112.62 ?  371 LEU A O   1 
ATOM 3101 C CB  . LEU A 1 371 ? -48.460  47.496 11.033  1.00 107.22 ?  371 LEU A CB  1 
ATOM 3102 C CG  . LEU A 1 371 ? -49.351  47.979 9.889   1.00 96.97  ?  371 LEU A CG  1 
ATOM 3103 C CD1 . LEU A 1 371 ? -50.542  47.050 9.717   1.00 79.57  ?  371 LEU A CD1 1 
ATOM 3104 C CD2 . LEU A 1 371 ? -49.811  49.407 10.135  1.00 90.25  ?  371 LEU A CD2 1 
ATOM 3105 N N   . ASP A 1 372 ? -46.589  48.622 13.646  1.00 137.04 ?  372 ASP A N   1 
ATOM 3106 C CA  . ASP A 1 372 ? -46.067  48.206 14.939  1.00 147.20 ?  372 ASP A CA  1 
ATOM 3107 C C   . ASP A 1 372 ? -46.920  47.080 15.510  1.00 128.89 ?  372 ASP A C   1 
ATOM 3108 O O   . ASP A 1 372 ? -48.151  47.114 15.442  1.00 125.36 ?  372 ASP A O   1 
ATOM 3109 C CB  . ASP A 1 372 ? -46.031  49.387 15.907  1.00 164.21 ?  372 ASP A CB  1 
ATOM 3110 C CG  . ASP A 1 372 ? -45.276  49.071 17.182  1.00 167.16 ?  372 ASP A CG  1 
ATOM 3111 O OD1 . ASP A 1 372 ? -44.055  48.817 17.105  1.00 155.25 ?  372 ASP A OD1 1 
ATOM 3112 O OD2 . ASP A 1 372 ? -45.904  49.074 18.262  1.00 184.42 -1 372 ASP A OD2 1 
ATOM 3113 N N   . ILE A 1 373 ? -46.255  46.077 16.074  1.00 121.78 ?  373 ILE A N   1 
ATOM 3114 C CA  . ILE A 1 373 ? -46.925  44.863 16.534  1.00 118.14 ?  373 ILE A CA  1 
ATOM 3115 C C   . ILE A 1 373 ? -46.503  44.580 17.971  1.00 132.61 ?  373 ILE A C   1 
ATOM 3116 O O   . ILE A 1 373 ? -45.336  44.805 18.324  1.00 135.25 ?  373 ILE A O   1 
ATOM 3117 C CB  . ILE A 1 373 ? -46.610  43.684 15.598  1.00 107.09 ?  373 ILE A CB  1 
ATOM 3118 C CG1 . ILE A 1 373 ? -47.261  43.921 14.236  1.00 105.48 ?  373 ILE A CG1 1 
ATOM 3119 C CG2 . ILE A 1 373 ? -47.070  42.357 16.188  1.00 98.61  ?  373 ILE A CG2 1 
ATOM 3120 C CD1 . ILE A 1 373 ? -47.219  42.733 13.337  1.00 80.32  ?  373 ILE A CD1 1 
ATOM 3121 N N   . PRO A 1 374 ? -47.418  44.130 18.834  1.00 123.13 ?  374 PRO A N   1 
ATOM 3122 C CA  . PRO A 1 374 ? -47.040  43.785 20.210  1.00 116.69 ?  374 PRO A CA  1 
ATOM 3123 C C   . PRO A 1 374 ? -45.828  42.865 20.259  1.00 116.42 ?  374 PRO A C   1 
ATOM 3124 O O   . PRO A 1 374 ? -45.721  41.899 19.500  1.00 98.27  ?  374 PRO A O   1 
ATOM 3125 C CB  . PRO A 1 374 ? -48.297  43.097 20.749  1.00 113.21 ?  374 PRO A CB  1 
ATOM 3126 C CG  . PRO A 1 374 ? -49.408  43.766 20.015  1.00 115.21 ?  374 PRO A CG  1 
ATOM 3127 C CD  . PRO A 1 374 ? -48.877  44.069 18.634  1.00 110.82 ?  374 PRO A CD  1 
ATOM 3128 N N   . SER A 1 375 ? -44.906  43.180 21.171  1.00 112.24 ?  375 SER A N   1 
ATOM 3129 C CA  . SER A 1 375 ? -43.616  42.504 21.246  1.00 109.43 ?  375 SER A CA  1 
ATOM 3130 C C   . SER A 1 375 ? -43.719  41.048 21.682  1.00 108.98 ?  375 SER A C   1 
ATOM 3131 O O   . SER A 1 375 ? -42.718  40.327 21.600  1.00 106.76 ?  375 SER A O   1 
ATOM 3132 C CB  . SER A 1 375 ? -42.694  43.258 22.206  1.00 114.26 ?  375 SER A CB  1 
ATOM 3133 O OG  . SER A 1 375 ? -42.885  44.659 22.100  1.00 136.75 ?  375 SER A OG  1 
ATOM 3134 N N   . GLN A 1 376 ? -44.889  40.597 22.138  1.00 117.65 ?  376 GLN A N   1 
ATOM 3135 C CA  . GLN A 1 376 ? -44.994  39.255 22.700  1.00 99.34  ?  376 GLN A CA  1 
ATOM 3136 C C   . GLN A 1 376 ? -44.945  38.184 21.616  1.00 96.97  ?  376 GLN A C   1 
ATOM 3137 O O   . GLN A 1 376 ? -44.378  37.106 21.828  1.00 103.35 ?  376 GLN A O   1 
ATOM 3138 C CB  . GLN A 1 376 ? -46.283  39.126 23.516  1.00 92.63  ?  376 GLN A CB  1 
ATOM 3139 C CG  . GLN A 1 376 ? -46.361  40.024 24.750  1.00 124.68 ?  376 GLN A CG  1 
ATOM 3140 C CD  . GLN A 1 376 ? -46.670  41.474 24.420  1.00 126.55 ?  376 GLN A CD  1 
ATOM 3141 O OE1 . GLN A 1 376 ? -46.774  41.849 23.253  1.00 110.51 ?  376 GLN A OE1 1 
ATOM 3142 N NE2 . GLN A 1 376 ? -46.818  42.297 25.452  1.00 144.06 ?  376 GLN A NE2 1 
ATOM 3143 N N   . LEU A 1 377 ? -45.524  38.461 20.450  1.00 93.61  ?  377 LEU A N   1 
ATOM 3144 C CA  . LEU A 1 377 ? -45.689  37.424 19.444  1.00 88.83  ?  377 LEU A CA  1 
ATOM 3145 C C   . LEU A 1 377 ? -44.435  37.278 18.588  1.00 92.67  ?  377 LEU A C   1 
ATOM 3146 O O   . LEU A 1 377 ? -43.705  38.251 18.370  1.00 108.09 ?  377 LEU A O   1 
ATOM 3147 C CB  . LEU A 1 377 ? -46.882  37.740 18.549  1.00 79.69  ?  377 LEU A CB  1 
ATOM 3148 C CG  . LEU A 1 377 ? -48.163  38.143 19.281  1.00 79.26  ?  377 LEU A CG  1 
ATOM 3149 C CD1 . LEU A 1 377 ? -48.383  39.649 19.203  1.00 82.95  ?  377 LEU A CD1 1 
ATOM 3150 C CD2 . LEU A 1 377 ? -49.359  37.387 18.727  1.00 83.65  ?  377 LEU A CD2 1 
ATOM 3151 N N   . PRO A 1 378 ? -44.168  36.065 18.089  1.00 77.77  ?  378 PRO A N   1 
ATOM 3152 C CA  . PRO A 1 378 ? -43.013  35.866 17.203  1.00 87.45  ?  378 PRO A CA  1 
ATOM 3153 C C   . PRO A 1 378 ? -43.210  36.529 15.849  1.00 88.97  ?  378 PRO A C   1 
ATOM 3154 O O   . PRO A 1 378 ? -43.418  35.851 14.837  1.00 68.25  ?  378 PRO A O   1 
ATOM 3155 C CB  . PRO A 1 378 ? -42.928  34.339 17.070  1.00 85.43  ?  378 PRO A CB  1 
ATOM 3156 C CG  . PRO A 1 378 ? -43.687  33.803 18.243  1.00 81.18  ?  378 PRO A CG  1 
ATOM 3157 C CD  . PRO A 1 378 ? -44.787  34.789 18.482  1.00 75.54  ?  378 PRO A CD  1 
ATOM 3158 N N   . GLN A 1 379 ? -43.145  37.856 15.824  1.00 90.53  ?  379 GLN A N   1 
ATOM 3159 C CA  . GLN A 1 379 ? -43.393  38.612 14.608  1.00 72.39  ?  379 GLN A CA  1 
ATOM 3160 C C   . GLN A 1 379 ? -42.158  38.630 13.715  1.00 84.03  ?  379 GLN A C   1 
ATOM 3161 O O   . GLN A 1 379 ? -41.019  38.551 14.185  1.00 97.08  ?  379 GLN A O   1 
ATOM 3162 C CB  . GLN A 1 379 ? -43.807  40.043 14.950  1.00 73.69  ?  379 GLN A CB  1 
ATOM 3163 C CG  . GLN A 1 379 ? -42.864  40.738 15.918  1.00 76.12  ?  379 GLN A CG  1 
ATOM 3164 C CD  . GLN A 1 379 ? -43.216  42.196 16.130  1.00 113.24 ?  379 GLN A CD  1 
ATOM 3165 O OE1 . GLN A 1 379 ? -42.881  43.054 15.313  1.00 112.90 ?  379 GLN A OE1 1 
ATOM 3166 N NE2 . GLN A 1 379 ? -43.893  42.485 17.235  1.00 113.20 ?  379 GLN A NE2 1 
ATOM 3167 N N   . VAL A 1 380 ? -42.399  38.731 12.410  1.00 93.52  ?  380 VAL A N   1 
ATOM 3168 C CA  . VAL A 1 380 ? -41.344  38.814 11.405  1.00 79.19  ?  380 VAL A CA  1 
ATOM 3169 C C   . VAL A 1 380 ? -41.711  39.950 10.459  1.00 71.82  ?  380 VAL A C   1 
ATOM 3170 O O   . VAL A 1 380 ? -42.655  39.825 9.669   1.00 102.51 ?  380 VAL A O   1 
ATOM 3171 C CB  . VAL A 1 380 ? -41.164  37.499 10.634  1.00 72.16  ?  380 VAL A CB  1 
ATOM 3172 C CG1 . VAL A 1 380 ? -40.139  37.671 9.523   1.00 70.36  ?  380 VAL A CG1 1 
ATOM 3173 C CG2 . VAL A 1 380 ? -40.744  36.381 11.576  1.00 77.53  ?  380 VAL A CG2 1 
ATOM 3174 N N   . ASN A 1 381 ? -40.977  41.055 10.542  1.00 74.03  ?  381 ASN A N   1 
ATOM 3175 C CA  . ASN A 1 381 ? -41.189  42.215 9.686   1.00 84.64  ?  381 ASN A CA  1 
ATOM 3176 C C   . ASN A 1 381 ? -40.088  42.263 8.635   1.00 83.75  ?  381 ASN A C   1 
ATOM 3177 O O   . ASN A 1 381 ? -38.906  42.112 8.962   1.00 102.67 ?  381 ASN A O   1 
ATOM 3178 C CB  . ASN A 1 381 ? -41.208  43.505 10.511  1.00 83.13  ?  381 ASN A CB  1 
ATOM 3179 C CG  . ASN A 1 381 ? -42.226  43.461 11.637  1.00 98.07  ?  381 ASN A CG  1 
ATOM 3180 O OD1 . ASN A 1 381 ? -43.108  42.602 11.659  1.00 94.29  ?  381 ASN A OD1 1 
ATOM 3181 N ND2 . ASN A 1 381 ? -42.107  44.389 12.581  1.00 102.13 ?  381 ASN A ND2 1 
ATOM 3182 N N   . ILE A 1 382 ? -40.475  42.471 7.377   1.00 85.89  ?  382 ILE A N   1 
ATOM 3183 C CA  . ILE A 1 382 ? -39.556  42.364 6.248   1.00 85.49  ?  382 ILE A CA  1 
ATOM 3184 C C   . ILE A 1 382 ? -39.851  43.480 5.255   1.00 94.31  ?  382 ILE A C   1 
ATOM 3185 O O   . ILE A 1 382 ? -41.008  43.695 4.878   1.00 102.63 ?  382 ILE A O   1 
ATOM 3186 C CB  . ILE A 1 382 ? -39.661  40.986 5.563   1.00 85.82  ?  382 ILE A CB  1 
ATOM 3187 C CG1 . ILE A 1 382 ? -38.868  39.938 6.347   1.00 76.10  ?  382 ILE A CG1 1 
ATOM 3188 C CG2 . ILE A 1 382 ? -39.173  41.055 4.121   1.00 95.47  ?  382 ILE A CG2 1 
ATOM 3189 C CD1 . ILE A 1 382 ? -38.874  38.566 5.708   1.00 67.90  ?  382 ILE A CD1 1 
ATOM 3190 N N   . GLN A 1 383 ? -38.803  44.182 4.829   1.00 96.83  ?  383 GLN A N   1 
ATOM 3191 C CA  . GLN A 1 383 ? -38.899  45.255 3.850   1.00 93.52  ?  383 GLN A CA  1 
ATOM 3192 C C   . GLN A 1 383 ? -38.476  44.746 2.477   1.00 89.20  ?  383 GLN A C   1 
ATOM 3193 O O   . GLN A 1 383 ? -37.547  43.941 2.360   1.00 95.17  ?  383 GLN A O   1 
ATOM 3194 C CB  . GLN A 1 383 ? -38.022  46.440 4.264   1.00 87.69  ?  383 GLN A CB  1 
ATOM 3195 C CG  . GLN A 1 383 ? -38.183  47.687 3.409   1.00 77.42  ?  383 GLN A CG  1 
ATOM 3196 C CD  . GLN A 1 383 ? -37.175  48.766 3.761   1.00 91.14  ?  383 GLN A CD  1 
ATOM 3197 O OE1 . GLN A 1 383 ? -36.086  48.477 4.257   1.00 89.19  ?  383 GLN A OE1 1 
ATOM 3198 N NE2 . GLN A 1 383 ? -37.535  50.019 3.504   1.00 70.94  ?  383 GLN A NE2 1 
ATOM 3199 N N   . VAL A 1 384 ? -39.162  45.222 1.436   1.00 90.90  ?  384 VAL A N   1 
ATOM 3200 C CA  . VAL A 1 384 ? -38.891  44.826 0.059   1.00 90.76  ?  384 VAL A CA  1 
ATOM 3201 C C   . VAL A 1 384 ? -39.060  46.040 -0.847  1.00 111.97 ?  384 VAL A C   1 
ATOM 3202 O O   . VAL A 1 384 ? -39.525  47.101 -0.427  1.00 120.65 ?  384 VAL A O   1 
ATOM 3203 C CB  . VAL A 1 384 ? -39.806  43.676 -0.415  1.00 91.67  ?  384 VAL A CB  1 
ATOM 3204 C CG1 . VAL A 1 384 ? -39.331  42.345 0.148   1.00 94.00  ?  384 VAL A CG1 1 
ATOM 3205 C CG2 . VAL A 1 384 ? -41.249  43.947 -0.018  1.00 87.95  ?  384 VAL A CG2 1 
ATOM 3206 N N   . LYS A 1 385 ? -38.670  45.869 -2.109  1.00 98.28  ?  385 LYS A N   1 
ATOM 3207 C CA  . LYS A 1 385 ? -38.837  46.909 -3.117  1.00 120.07 ?  385 LYS A CA  1 
ATOM 3208 C C   . LYS A 1 385 ? -40.197  46.828 -3.800  1.00 120.15 ?  385 LYS A C   1 
ATOM 3209 O O   . LYS A 1 385 ? -40.936  47.817 -3.840  1.00 119.06 ?  385 LYS A O   1 
ATOM 3210 C CB  . LYS A 1 385 ? -37.717  46.819 -4.160  1.00 130.35 ?  385 LYS A CB  1 
ATOM 3211 C CG  . LYS A 1 385 ? -36.479  47.627 -3.817  1.00 129.59 ?  385 LYS A CG  1 
ATOM 3212 C CD  . LYS A 1 385 ? -35.951  48.358 -5.043  1.00 138.67 ?  385 LYS A CD  1 
ATOM 3213 C CE  . LYS A 1 385 ? -36.977  49.340 -5.587  1.00 148.92 ?  385 LYS A CE  1 
ATOM 3214 N NZ  . LYS A 1 385 ? -36.496  50.021 -6.822  1.00 182.28 ?  385 LYS A NZ  1 
ATOM 3215 N N   . ASP A 1 386 ? -40.540  45.663 -4.342  1.00 119.21 ?  386 ASP A N   1 
ATOM 3216 C CA  . ASP A 1 386 ? -41.790  45.472 -5.058  1.00 125.45 ?  386 ASP A CA  1 
ATOM 3217 C C   . ASP A 1 386 ? -42.612  44.379 -4.387  1.00 100.48 ?  386 ASP A C   1 
ATOM 3218 O O   . ASP A 1 386 ? -42.076  43.503 -3.702  1.00 99.20  ?  386 ASP A O   1 
ATOM 3219 C CB  . ASP A 1 386 ? -41.535  45.110 -6.529  1.00 126.45 ?  386 ASP A CB  1 
ATOM 3220 C CG  . ASP A 1 386 ? -42.756  45.319 -7.406  1.00 120.56 ?  386 ASP A CG  1 
ATOM 3221 O OD1 . ASP A 1 386 ? -43.885  45.342 -6.872  1.00 113.46 ?  386 ASP A OD1 1 
ATOM 3222 O OD2 . ASP A 1 386 ? -42.586  45.457 -8.636  1.00 136.14 -1 386 ASP A OD2 1 
ATOM 3223 N N   . PHE A 1 387 ? -43.929  44.446 -4.597  1.00 91.94  ?  387 PHE A N   1 
ATOM 3224 C CA  . PHE A 1 387 ? -44.831  43.450 -4.026  1.00 85.12  ?  387 PHE A CA  1 
ATOM 3225 C C   . PHE A 1 387 ? -44.591  42.071 -4.627  1.00 94.99  ?  387 PHE A C   1 
ATOM 3226 O O   . PHE A 1 387 ? -44.697  41.055 -3.929  1.00 100.65 ?  387 PHE A O   1 
ATOM 3227 C CB  . PHE A 1 387 ? -46.282  43.887 -4.239  1.00 95.46  ?  387 PHE A CB  1 
ATOM 3228 C CG  . PHE A 1 387 ? -47.274  43.155 -3.378  1.00 97.15  ?  387 PHE A CG  1 
ATOM 3229 C CD1 . PHE A 1 387 ? -47.700  41.880 -3.715  1.00 95.86  ?  387 PHE A CD1 1 
ATOM 3230 C CD2 . PHE A 1 387 ? -47.789  43.748 -2.237  1.00 103.58 ?  387 PHE A CD2 1 
ATOM 3231 C CE1 . PHE A 1 387 ? -48.614  41.207 -2.926  1.00 109.21 ?  387 PHE A CE1 1 
ATOM 3232 C CE2 . PHE A 1 387 ? -48.704  43.082 -1.445  1.00 108.28 ?  387 PHE A CE2 1 
ATOM 3233 C CZ  . PHE A 1 387 ? -49.117  41.810 -1.790  1.00 111.92 ?  387 PHE A CZ  1 
ATOM 3234 N N   . ALA A 1 388 ? -44.262  42.013 -5.920  1.00 93.51  ?  388 ALA A N   1 
ATOM 3235 C CA  . ALA A 1 388 ? -44.175  40.743 -6.632  1.00 91.85  ?  388 ALA A CA  1 
ATOM 3236 C C   . ALA A 1 388 ? -43.084  39.823 -6.099  1.00 94.84  ?  388 ALA A C   1 
ATOM 3237 O O   . ALA A 1 388 ? -43.054  38.647 -6.480  1.00 91.25  ?  388 ALA A O   1 
ATOM 3238 C CB  . ALA A 1 388 ? -43.951  40.997 -8.124  1.00 91.47  ?  388 ALA A CB  1 
ATOM 3239 N N   . ASP A 1 389 ? -42.195  40.314 -5.236  1.00 95.28  ?  389 ASP A N   1 
ATOM 3240 C CA  . ASP A 1 389 ? -41.126  39.486 -4.693  1.00 103.91 ?  389 ASP A CA  1 
ATOM 3241 C C   . ASP A 1 389 ? -41.586  38.589 -3.551  1.00 92.00  ?  389 ASP A C   1 
ATOM 3242 O O   . ASP A 1 389 ? -40.823  37.709 -3.134  1.00 85.03  ?  389 ASP A O   1 
ATOM 3243 C CB  . ASP A 1 389 ? -39.974  40.370 -4.209  1.00 106.04 ?  389 ASP A CB  1 
ATOM 3244 C CG  . ASP A 1 389 ? -39.695  41.527 -5.146  1.00 115.94 ?  389 ASP A CG  1 
ATOM 3245 O OD1 . ASP A 1 389 ? -39.893  41.364 -6.368  1.00 116.03 ?  389 ASP A OD1 1 
ATOM 3246 O OD2 . ASP A 1 389 ? -39.277  42.599 -4.661  1.00 112.50 -1 389 ASP A OD2 1 
ATOM 3247 N N   . ILE A 1 390 ? -42.805  38.783 -3.044  1.00 90.93  ?  390 ILE A N   1 
ATOM 3248 C CA  . ILE A 1 390 ? -43.253  38.029 -1.879  1.00 96.39  ?  390 ILE A CA  1 
ATOM 3249 C C   . ILE A 1 390 ? -43.648  36.606 -2.257  1.00 94.43  ?  390 ILE A C   1 
ATOM 3250 O O   . ILE A 1 390 ? -43.478  35.680 -1.453  1.00 87.83  ?  390 ILE A O   1 
ATOM 3251 C CB  . ILE A 1 390 ? -44.411  38.770 -1.190  1.00 82.42  ?  390 ILE A CB  1 
ATOM 3252 C CG1 . ILE A 1 390 ? -43.991  40.199 -0.845  1.00 76.17  ?  390 ILE A CG1 1 
ATOM 3253 C CG2 . ILE A 1 390 ? -44.853  38.036 0.065   1.00 85.13  ?  390 ILE A CG2 1 
ATOM 3254 C CD1 . ILE A 1 390 ? -45.140  41.072 -0.394  1.00 73.05  ?  390 ILE A CD1 1 
ATOM 3255 N N   . LYS A 1 391 ? -44.174  36.406 -3.470  1.00 87.27  ?  391 LYS A N   1 
ATOM 3256 C CA  . LYS A 1 391 ? -44.586  35.072 -3.896  1.00 89.85  ?  391 LYS A CA  1 
ATOM 3257 C C   . LYS A 1 391 ? -43.436  34.078 -3.806  1.00 96.98  ?  391 LYS A C   1 
ATOM 3258 O O   . LYS A 1 391 ? -43.639  32.911 -3.454  1.00 101.70 ?  391 LYS A O   1 
ATOM 3259 C CB  . LYS A 1 391 ? -45.137  35.128 -5.322  1.00 111.90 ?  391 LYS A CB  1 
ATOM 3260 C CG  . LYS A 1 391 ? -45.402  33.762 -5.944  1.00 121.21 ?  391 LYS A CG  1 
ATOM 3261 C CD  . LYS A 1 391 ? -45.872  33.894 -7.385  1.00 124.04 ?  391 LYS A CD  1 
ATOM 3262 C CE  . LYS A 1 391 ? -46.053  32.532 -8.042  1.00 138.74 ?  391 LYS A CE  1 
ATOM 3263 N NZ  . LYS A 1 391 ? -46.562  32.650 -9.438  1.00 118.47 ?  391 LYS A NZ  1 
ATOM 3264 N N   . GLU A 1 392 ? -42.218  34.526 -4.104  1.00 103.35 ?  392 GLU A N   1 
ATOM 3265 C CA  . GLU A 1 392 ? -41.047  33.661 -4.115  1.00 103.33 ?  392 GLU A CA  1 
ATOM 3266 C C   . GLU A 1 392 ? -40.431  33.470 -2.734  1.00 107.44 ?  392 GLU A C   1 
ATOM 3267 O O   . GLU A 1 392 ? -39.275  33.040 -2.641  1.00 100.15 ?  392 GLU A O   1 
ATOM 3268 C CB  . GLU A 1 392 ? -39.997  34.212 -5.086  1.00 91.56  ?  392 GLU A CB  1 
ATOM 3269 C CG  . GLU A 1 392 ? -40.472  34.336 -6.532  1.00 93.15  ?  392 GLU A CG  1 
ATOM 3270 C CD  . GLU A 1 392 ? -41.293  35.589 -6.786  1.00 112.71 ?  392 GLU A CD  1 
ATOM 3271 O OE1 . GLU A 1 392 ? -41.577  36.327 -5.819  1.00 110.66 ?  392 GLU A OE1 1 
ATOM 3272 O OE2 . GLU A 1 392 ? -41.658  35.833 -7.956  1.00 120.09 -1 392 GLU A OE2 1 
ATOM 3273 N N   . ILE A 1 393 ? -41.163  33.778 -1.664  1.00 101.52 ?  393 ILE A N   1 
ATOM 3274 C CA  . ILE A 1 393 ? -40.659  33.567 -0.311  1.00 86.42  ?  393 ILE A CA  1 
ATOM 3275 C C   . ILE A 1 393 ? -41.521  32.534 0.397   1.00 103.67 ?  393 ILE A C   1 
ATOM 3276 O O   . ILE A 1 393 ? -41.031  31.769 1.235   1.00 100.15 ?  393 ILE A O   1 
ATOM 3277 C CB  . ILE A 1 393 ? -40.637  34.876 0.497   1.00 88.48  ?  393 ILE A CB  1 
ATOM 3278 C CG1 . ILE A 1 393 ? -40.199  36.048 -0.374  1.00 88.23  ?  393 ILE A CG1 1 
ATOM 3279 C CG2 . ILE A 1 393 ? -39.721  34.737 1.703   1.00 81.98  ?  393 ILE A CG2 1 
ATOM 3280 C CD1 . ILE A 1 393 ? -40.215  37.373 0.353   1.00 63.54  ?  393 ILE A CD1 1 
ATOM 3281 N N   . VAL A 1 394 ? -42.804  32.496 0.060   1.00 121.70 ?  394 VAL A N   1 
ATOM 3282 C CA  . VAL A 1 394 ? -43.760  31.702 0.816   1.00 114.28 ?  394 VAL A CA  1 
ATOM 3283 C C   . VAL A 1 394 ? -44.086  30.400 0.097   1.00 122.93 ?  394 VAL A C   1 
ATOM 3284 O O   . VAL A 1 394 ? -44.596  29.460 0.705   1.00 117.30 ?  394 VAL A O   1 
ATOM 3285 C CB  . VAL A 1 394 ? -45.039  32.508 1.086   1.00 97.69  ?  394 VAL A CB  1 
ATOM 3286 C CG1 . VAL A 1 394 ? -44.686  33.895 1.605   1.00 93.75  ?  394 VAL A CG1 1 
ATOM 3287 C CG2 . VAL A 1 394 ? -45.877  32.605 -0.177  1.00 110.08 ?  394 VAL A CG2 1 
ATOM 3288 N N   . SER B 1 4   ? -125.356 39.563 25.046  1.00 91.07  ?  4   SER B N   1 
ATOM 3289 C CA  . SER B 1 4   ? -126.446 39.456 24.084  1.00 96.44  ?  4   SER B CA  1 
ATOM 3290 C C   . SER B 1 4   ? -126.618 40.754 23.304  1.00 98.64  ?  4   SER B C   1 
ATOM 3291 O O   . SER B 1 4   ? -127.608 40.940 22.596  1.00 92.96  ?  4   SER B O   1 
ATOM 3292 C CB  . SER B 1 4   ? -127.753 39.089 24.787  1.00 109.70 ?  4   SER B CB  1 
ATOM 3293 O OG  . SER B 1 4   ? -128.835 39.088 23.872  1.00 100.96 ?  4   SER B OG  1 
ATOM 3294 N N   . ALA B 1 5   ? -125.647 41.654 23.444  1.00 99.35  ?  5   ALA B N   1 
ATOM 3295 C CA  . ALA B 1 5   ? -125.615 42.877 22.654  1.00 98.62  ?  5   ALA B CA  1 
ATOM 3296 C C   . ALA B 1 5   ? -125.142 42.637 21.228  1.00 97.37  ?  5   ALA B C   1 
ATOM 3297 O O   . ALA B 1 5   ? -124.993 43.602 20.470  1.00 104.28 ?  5   ALA B O   1 
ATOM 3298 C CB  . ALA B 1 5   ? -124.719 43.919 23.327  1.00 101.17 ?  5   ALA B CB  1 
ATOM 3299 N N   . VAL B 1 6   ? -124.897 41.379 20.853  1.00 97.82  ?  6   VAL B N   1 
ATOM 3300 C CA  . VAL B 1 6   ? -124.494 41.057 19.488  1.00 95.43  ?  6   VAL B CA  1 
ATOM 3301 C C   . VAL B 1 6   ? -125.597 41.419 18.503  1.00 101.77 ?  6   VAL B C   1 
ATOM 3302 O O   . VAL B 1 6   ? -125.326 41.692 17.327  1.00 100.73 ?  6   VAL B O   1 
ATOM 3303 C CB  . VAL B 1 6   ? -124.103 39.567 19.395  1.00 92.55  ?  6   VAL B CB  1 
ATOM 3304 C CG1 . VAL B 1 6   ? -125.275 38.678 19.797  1.00 74.90  ?  6   VAL B CG1 1 
ATOM 3305 C CG2 . VAL B 1 6   ? -123.596 39.217 18.002  1.00 112.63 ?  6   VAL B CG2 1 
ATOM 3306 N N   . ASP B 1 7   ? -126.853 41.441 18.965  1.00 106.92 ?  7   ASP B N   1 
ATOM 3307 C CA  . ASP B 1 7   ? -127.958 41.856 18.106  1.00 90.53  ?  7   ASP B CA  1 
ATOM 3308 C C   . ASP B 1 7   ? -127.730 43.247 17.531  1.00 82.70  ?  7   ASP B C   1 
ATOM 3309 O O   . ASP B 1 7   ? -128.251 43.568 16.457  1.00 87.38  ?  7   ASP B O   1 
ATOM 3310 C CB  . ASP B 1 7   ? -129.273 41.809 18.886  1.00 86.74  ?  7   ASP B CB  1 
ATOM 3311 C CG  . ASP B 1 7   ? -129.435 40.525 19.676  1.00 97.50  ?  7   ASP B CG  1 
ATOM 3312 O OD1 . ASP B 1 7   ? -128.878 39.491 19.251  1.00 107.96 ?  7   ASP B OD1 1 
ATOM 3313 O OD2 . ASP B 1 7   ? -130.119 40.550 20.721  1.00 92.43  -1 7   ASP B OD2 1 
ATOM 3314 N N   . THR B 1 8   ? -126.964 44.086 18.229  1.00 97.11  ?  8   THR B N   1 
ATOM 3315 C CA  . THR B 1 8   ? -126.533 45.353 17.651  1.00 104.02 ?  8   THR B CA  1 
ATOM 3316 C C   . THR B 1 8   ? -125.525 45.116 16.532  1.00 94.29  ?  8   THR B C   1 
ATOM 3317 O O   . THR B 1 8   ? -125.726 45.553 15.393  1.00 92.82  ?  8   THR B O   1 
ATOM 3318 C CB  . THR B 1 8   ? -125.941 46.253 18.738  1.00 108.12 ?  8   THR B CB  1 
ATOM 3319 O OG1 . THR B 1 8   ? -126.783 46.221 19.898  1.00 114.56 ?  8   THR B OG1 1 
ATOM 3320 C CG2 . THR B 1 8   ? -125.833 47.686 18.242  1.00 96.39  ?  8   THR B CG2 1 
ATOM 3321 N N   . ILE B 1 9   ? -124.433 44.410 16.839  1.00 97.22  ?  9   ILE B N   1 
ATOM 3322 C CA  . ILE B 1 9   ? -123.437 44.080 15.820  1.00 106.22 ?  9   ILE B CA  1 
ATOM 3323 C C   . ILE B 1 9   ? -124.072 43.251 14.710  1.00 99.90  ?  9   ILE B C   1 
ATOM 3324 O O   . ILE B 1 9   ? -124.039 43.622 13.531  1.00 90.65  ?  9   ILE B O   1 
ATOM 3325 C CB  . ILE B 1 9   ? -122.238 43.346 16.447  1.00 103.89 ?  9   ILE B CB  1 
ATOM 3326 C CG1 . ILE B 1 9   ? -121.474 44.268 17.402  1.00 120.56 ?  9   ILE B CG1 1 
ATOM 3327 C CG2 . ILE B 1 9   ? -121.316 42.805 15.365  1.00 82.19  ?  9   ILE B CG2 1 
ATOM 3328 C CD1 . ILE B 1 9   ? -121.909 44.161 18.850  1.00 117.94 ?  9   ILE B CD1 1 
ATOM 3329 N N   . ARG B 1 10  ? -124.664 42.114 15.076  1.00 107.54 ?  10  ARG B N   1 
ATOM 3330 C CA  . ARG B 1 10  ? -125.364 41.287 14.102  1.00 87.70  ?  10  ARG B CA  1 
ATOM 3331 C C   . ARG B 1 10  ? -126.663 41.978 13.717  1.00 85.62  ?  10  ARG B C   1 
ATOM 3332 O O   . ARG B 1 10  ? -127.695 41.804 14.374  1.00 103.72 ?  10  ARG B O   1 
ATOM 3333 C CB  . ARG B 1 10  ? -125.626 39.887 14.663  1.00 79.61  ?  10  ARG B CB  1 
ATOM 3334 C CG  . ARG B 1 10  ? -126.352 38.953 13.707  1.00 81.90  ?  10  ARG B CG  1 
ATOM 3335 C CD  . ARG B 1 10  ? -126.912 37.746 14.439  1.00 93.89  ?  10  ARG B CD  1 
ATOM 3336 N NE  . ARG B 1 10  ? -125.925 36.678 14.567  1.00 103.47 ?  10  ARG B NE  1 
ATOM 3337 C CZ  . ARG B 1 10  ? -126.139 35.536 15.214  1.00 116.43 ?  10  ARG B CZ  1 
ATOM 3338 N NH1 . ARG B 1 10  ? -127.308 35.309 15.796  1.00 113.76 ?  10  ARG B NH1 1 
ATOM 3339 N NH2 . ARG B 1 10  ? -125.182 34.621 15.279  1.00 125.03 ?  10  ARG B NH2 1 
ATOM 3340 N N   . GLY B 1 11  ? -126.613 42.766 12.647  1.00 85.74  ?  11  GLY B N   1 
ATOM 3341 C CA  . GLY B 1 11  ? -127.730 43.585 12.225  1.00 90.39  ?  11  GLY B CA  1 
ATOM 3342 C C   . GLY B 1 11  ? -127.262 44.945 11.758  1.00 95.34  ?  11  GLY B C   1 
ATOM 3343 O O   . GLY B 1 11  ? -127.817 45.504 10.807  1.00 84.97  ?  11  GLY B O   1 
ATOM 3344 N N   . TYR B 1 12  ? -126.216 45.478 12.398  1.00 91.39  ?  12  TYR B N   1 
ATOM 3345 C CA  . TYR B 1 12  ? -125.465 46.561 11.777  1.00 89.98  ?  12  TYR B CA  1 
ATOM 3346 C C   . TYR B 1 12  ? -124.866 46.101 10.458  1.00 86.32  ?  12  TYR B C   1 
ATOM 3347 O O   . TYR B 1 12  ? -124.726 46.897 9.522   1.00 77.90  ?  12  TYR B O   1 
ATOM 3348 C CB  . TYR B 1 12  ? -124.363 47.060 12.714  1.00 75.03  ?  12  TYR B CB  1 
ATOM 3349 C CG  . TYR B 1 12  ? -124.656 48.386 13.385  1.00 81.79  ?  12  TYR B CG  1 
ATOM 3350 C CD1 . TYR B 1 12  ? -124.459 49.585 12.713  1.00 79.42  ?  12  TYR B CD1 1 
ATOM 3351 C CD2 . TYR B 1 12  ? -125.114 48.439 14.694  1.00 89.85  ?  12  TYR B CD2 1 
ATOM 3352 C CE1 . TYR B 1 12  ? -124.720 50.800 13.324  1.00 95.12  ?  12  TYR B CE1 1 
ATOM 3353 C CE2 . TYR B 1 12  ? -125.377 49.646 15.312  1.00 72.98  ?  12  TYR B CE2 1 
ATOM 3354 C CZ  . TYR B 1 12  ? -125.179 50.822 14.624  1.00 81.06  ?  12  TYR B CZ  1 
ATOM 3355 O OH  . TYR B 1 12  ? -125.441 52.025 15.239  1.00 79.47  ?  12  TYR B OH  1 
ATOM 3356 N N   . CYS B 1 13  ? -124.509 44.819 10.371  1.00 79.29  ?  13  CYS B N   1 
ATOM 3357 C CA  . CYS B 1 13  ? -124.080 44.243 9.104   1.00 89.50  ?  13  CYS B CA  1 
ATOM 3358 C C   . CYS B 1 13  ? -125.245 44.132 8.130   1.00 95.14  ?  13  CYS B C   1 
ATOM 3359 O O   . CYS B 1 13  ? -125.093 44.425 6.938   1.00 95.69  ?  13  CYS B O   1 
ATOM 3360 C CB  . CYS B 1 13  ? -123.454 42.871 9.344   1.00 99.78  ?  13  CYS B CB  1 
ATOM 3361 S SG  . CYS B 1 13  ? -124.654 41.608 9.811   1.00 126.24 ?  13  CYS B SG  1 
ATOM 3362 N N   . TYR B 1 14  ? -126.412 43.705 8.622   1.00 80.36  ?  14  TYR B N   1 
ATOM 3363 C CA  . TYR B 1 14  ? -127.565 43.505 7.750   1.00 87.02  ?  14  TYR B CA  1 
ATOM 3364 C C   . TYR B 1 14  ? -127.900 44.770 6.972   1.00 82.51  ?  14  TYR B C   1 
ATOM 3365 O O   . TYR B 1 14  ? -128.241 44.705 5.785   1.00 89.07  ?  14  TYR B O   1 
ATOM 3366 C CB  . TYR B 1 14  ? -128.767 43.045 8.572   1.00 79.30  ?  14  TYR B CB  1 
ATOM 3367 C CG  . TYR B 1 14  ? -129.845 42.376 7.752   1.00 82.07  ?  14  TYR B CG  1 
ATOM 3368 C CD1 . TYR B 1 14  ? -129.843 41.001 7.558   1.00 91.25  ?  14  TYR B CD1 1 
ATOM 3369 C CD2 . TYR B 1 14  ? -130.867 43.118 7.174   1.00 87.43  ?  14  TYR B CD2 1 
ATOM 3370 C CE1 . TYR B 1 14  ? -130.827 40.383 6.810   1.00 87.68  ?  14  TYR B CE1 1 
ATOM 3371 C CE2 . TYR B 1 14  ? -131.856 42.509 6.425   1.00 98.76  ?  14  TYR B CE2 1 
ATOM 3372 C CZ  . TYR B 1 14  ? -131.830 41.141 6.246   1.00 93.69  ?  14  TYR B CZ  1 
ATOM 3373 O OH  . TYR B 1 14  ? -132.813 40.530 5.501   1.00 103.94 ?  14  TYR B OH  1 
ATOM 3374 N N   . GLN B 1 15  ? -127.804 45.932 7.622   1.00 70.24  ?  15  GLN B N   1 
ATOM 3375 C CA  . GLN B 1 15  ? -128.028 47.187 6.915   1.00 79.02  ?  15  GLN B CA  1 
ATOM 3376 C C   . GLN B 1 15  ? -126.952 47.416 5.862   1.00 78.46  ?  15  GLN B C   1 
ATOM 3377 O O   . GLN B 1 15  ? -127.253 47.832 4.738   1.00 89.83  ?  15  GLN B O   1 
ATOM 3378 C CB  . GLN B 1 15  ? -128.074 48.350 7.909   1.00 84.61  ?  15  GLN B CB  1 
ATOM 3379 C CG  . GLN B 1 15  ? -128.797 49.596 7.399   1.00 82.96  ?  15  GLN B CG  1 
ATOM 3380 C CD  . GLN B 1 15  ? -127.972 50.410 6.418   1.00 105.71 ?  15  GLN B CD  1 
ATOM 3381 O OE1 . GLN B 1 15  ? -126.744 50.340 6.410   1.00 113.89 ?  15  GLN B OE1 1 
ATOM 3382 N NE2 . GLN B 1 15  ? -128.651 51.187 5.581   1.00 117.60 ?  15  GLN B NE2 1 
ATOM 3383 N N   . VAL B 1 16  ? -125.691 47.146 6.206   1.00 85.97  ?  16  VAL B N   1 
ATOM 3384 C CA  . VAL B 1 16  ? -124.603 47.322 5.249   1.00 91.39  ?  16  VAL B CA  1 
ATOM 3385 C C   . VAL B 1 16  ? -124.745 46.338 4.095   1.00 97.23  ?  16  VAL B C   1 
ATOM 3386 O O   . VAL B 1 16  ? -124.593 46.704 2.923   1.00 99.62  ?  16  VAL B O   1 
ATOM 3387 C CB  . VAL B 1 16  ? -123.240 47.179 5.949   1.00 88.29  ?  16  VAL B CB  1 
ATOM 3388 C CG1 . VAL B 1 16  ? -122.109 47.277 4.936   1.00 97.04  ?  16  VAL B CG1 1 
ATOM 3389 C CG2 . VAL B 1 16  ? -123.086 48.238 7.029   1.00 88.48  ?  16  VAL B CG2 1 
ATOM 3390 N N   . ASP B 1 17  ? -125.033 45.072 4.409   1.00 92.23  ?  17  ASP B N   1 
ATOM 3391 C CA  . ASP B 1 17  ? -125.264 44.079 3.364   1.00 85.82  ?  17  ASP B CA  1 
ATOM 3392 C C   . ASP B 1 17  ? -126.412 44.499 2.454   1.00 93.62  ?  17  ASP B C   1 
ATOM 3393 O O   . ASP B 1 17  ? -126.279 44.490 1.225   1.00 84.36  ?  17  ASP B O   1 
ATOM 3394 C CB  . ASP B 1 17  ? -125.543 42.713 3.989   1.00 86.98  ?  17  ASP B CB  1 
ATOM 3395 C CG  . ASP B 1 17  ? -124.428 42.250 4.900   1.00 101.36 ?  17  ASP B CG  1 
ATOM 3396 O OD1 . ASP B 1 17  ? -123.503 43.046 5.167   1.00 116.95 ?  17  ASP B OD1 1 
ATOM 3397 O OD2 . ASP B 1 17  ? -124.476 41.086 5.353   1.00 101.96 -1 17  ASP B OD2 1 
ATOM 3398 N N   . LYS B 1 18  ? -127.553 44.864 3.045   1.00 89.49  ?  18  LYS B N   1 
ATOM 3399 C CA  . LYS B 1 18  ? -128.662 45.389 2.255   1.00 83.96  ?  18  LYS B CA  1 
ATOM 3400 C C   . LYS B 1 18  ? -128.236 46.621 1.467   1.00 91.03  ?  18  LYS B C   1 
ATOM 3401 O O   . LYS B 1 18  ? -128.612 46.784 0.300   1.00 108.16 ?  18  LYS B O   1 
ATOM 3402 C CB  . LYS B 1 18  ? -129.849 45.713 3.165   1.00 83.54  ?  18  LYS B CB  1 
ATOM 3403 C CG  . LYS B 1 18  ? -131.110 46.145 2.432   1.00 101.08 ?  18  LYS B CG  1 
ATOM 3404 C CD  . LYS B 1 18  ? -131.293 47.656 2.484   1.00 101.04 ?  18  LYS B CD  1 
ATOM 3405 C CE  . LYS B 1 18  ? -131.645 48.121 3.886   1.00 91.03  ?  18  LYS B CE  1 
ATOM 3406 N NZ  . LYS B 1 18  ? -132.054 49.552 3.913   1.00 109.87 ?  18  LYS B NZ  1 
ATOM 3407 N N   . THR B 1 19  ? -127.448 47.502 2.089   1.00 83.12  ?  19  THR B N   1 
ATOM 3408 C CA  . THR B 1 19  ? -126.898 48.640 1.363   1.00 91.28  ?  19  THR B CA  1 
ATOM 3409 C C   . THR B 1 19  ? -125.947 48.187 0.263   1.00 90.67  ?  19  THR B C   1 
ATOM 3410 O O   . THR B 1 19  ? -125.882 48.814 -0.801  1.00 102.07 ?  19  THR B O   1 
ATOM 3411 C CB  . THR B 1 19  ? -126.187 49.586 2.333   1.00 93.64  ?  19  THR B CB  1 
ATOM 3412 O OG1 . THR B 1 19  ? -127.071 49.915 3.412   1.00 92.48  ?  19  THR B OG1 1 
ATOM 3413 C CG2 . THR B 1 19  ? -125.764 50.862 1.629   1.00 88.55  ?  19  THR B CG2 1 
ATOM 3414 N N   . ILE B 1 20  ? -125.215 47.095 0.491   1.00 90.64  ?  20  ILE B N   1 
ATOM 3415 C CA  . ILE B 1 20  ? -124.315 46.569 -0.529  1.00 93.12  ?  20  ILE B CA  1 
ATOM 3416 C C   . ILE B 1 20  ? -125.100 45.873 -1.636  1.00 88.67  ?  20  ILE B C   1 
ATOM 3417 O O   . ILE B 1 20  ? -124.777 46.012 -2.821  1.00 90.96  ?  20  ILE B O   1 
ATOM 3418 C CB  . ILE B 1 20  ? -123.280 45.630 0.120   1.00 92.14  ?  20  ILE B CB  1 
ATOM 3419 C CG1 . ILE B 1 20  ? -122.163 46.446 0.779   1.00 95.21  ?  20  ILE B CG1 1 
ATOM 3420 C CG2 . ILE B 1 20  ? -122.703 44.661 -0.900  1.00 75.31  ?  20  ILE B CG2 1 
ATOM 3421 C CD1 . ILE B 1 20  ? -121.094 45.598 1.436   1.00 87.95  ?  20  ILE B CD1 1 
ATOM 3422 N N   . ILE B 1 21  ? -126.147 45.126 -1.270  1.00 88.15  ?  21  ILE B N   1 
ATOM 3423 C CA  . ILE B 1 21  ? -126.964 44.434 -2.265  1.00 81.84  ?  21  ILE B CA  1 
ATOM 3424 C C   . ILE B 1 21  ? -127.591 45.428 -3.236  1.00 87.94  ?  21  ILE B C   1 
ATOM 3425 O O   . ILE B 1 21  ? -127.596 45.210 -4.454  1.00 89.35  ?  21  ILE B O   1 
ATOM 3426 C CB  . ILE B 1 21  ? -128.034 43.570 -1.571  1.00 81.53  ?  21  ILE B CB  1 
ATOM 3427 C CG1 . ILE B 1 21  ? -127.385 42.387 -0.848  1.00 81.06  ?  21  ILE B CG1 1 
ATOM 3428 C CG2 . ILE B 1 21  ? -129.071 43.085 -2.575  1.00 80.71  ?  21  ILE B CG2 1 
ATOM 3429 C CD1 . ILE B 1 21  ? -126.978 41.265 -1.772  1.00 93.24  ?  21  ILE B CD1 1 
ATOM 3430 N N   . GLU B 1 22  ? -128.118 46.539 -2.718  1.00 88.94  ?  22  GLU B N   1 
ATOM 3431 C CA  . GLU B 1 22  ? -128.773 47.536 -3.556  1.00 104.75 ?  22  GLU B CA  1 
ATOM 3432 C C   . GLU B 1 22  ? -127.811 48.243 -4.502  1.00 110.98 ?  22  GLU B C   1 
ATOM 3433 O O   . GLU B 1 22  ? -128.268 48.891 -5.450  1.00 118.38 ?  22  GLU B O   1 
ATOM 3434 C CB  . GLU B 1 22  ? -129.491 48.564 -2.677  1.00 103.27 ?  22  GLU B CB  1 
ATOM 3435 C CG  . GLU B 1 22  ? -130.641 47.982 -1.868  1.00 122.09 ?  22  GLU B CG  1 
ATOM 3436 C CD  . GLU B 1 22  ? -131.387 49.029 -1.064  1.00 135.55 ?  22  GLU B CD  1 
ATOM 3437 O OE1 . GLU B 1 22  ? -130.827 50.123 -0.836  1.00 133.97 ?  22  GLU B OE1 1 
ATOM 3438 O OE2 . GLU B 1 22  ? -132.541 48.760 -0.666  1.00 130.02 -1 22  GLU B OE2 1 
ATOM 3439 N N   . ILE B 1 23  ? -126.503 48.138 -4.274  1.00 114.65 ?  23  ILE B N   1 
ATOM 3440 C CA  . ILE B 1 23  ? -125.533 48.764 -5.168  1.00 125.40 ?  23  ILE B CA  1 
ATOM 3441 C C   . ILE B 1 23  ? -125.277 47.884 -6.384  1.00 118.03 ?  23  ILE B C   1 
ATOM 3442 O O   . ILE B 1 23  ? -125.425 48.321 -7.531  1.00 117.63 ?  23  ILE B O   1 
ATOM 3443 C CB  . ILE B 1 23  ? -124.226 49.072 -4.415  1.00 113.80 ?  23  ILE B CB  1 
ATOM 3444 C CG1 . ILE B 1 23  ? -124.466 50.133 -3.341  1.00 108.65 ?  23  ILE B CG1 1 
ATOM 3445 C CG2 . ILE B 1 23  ? -123.145 49.520 -5.388  1.00 100.95 ?  23  ILE B CG2 1 
ATOM 3446 C CD1 . ILE B 1 23  ? -123.309 50.297 -2.384  1.00 116.79 ?  23  ILE B CD1 1 
ATOM 3447 N N   . PHE B 1 24  ? -124.888 46.628 -6.148  1.00 104.02 ?  24  PHE B N   1 
ATOM 3448 C CA  . PHE B 1 24  ? -124.581 45.726 -7.252  1.00 107.71 ?  24  PHE B CA  1 
ATOM 3449 C C   . PHE B 1 24  ? -125.819 45.389 -8.072  1.00 112.58 ?  24  PHE B C   1 
ATOM 3450 O O   . PHE B 1 24  ? -125.707 45.107 -9.271  1.00 121.21 ?  24  PHE B O   1 
ATOM 3451 C CB  . PHE B 1 24  ? -123.939 44.445 -6.721  1.00 102.16 ?  24  PHE B CB  1 
ATOM 3452 C CG  . PHE B 1 24  ? -122.453 44.540 -6.527  1.00 122.31 ?  24  PHE B CG  1 
ATOM 3453 C CD1 . PHE B 1 24  ? -121.917 45.370 -5.556  1.00 123.40 ?  24  PHE B CD1 1 
ATOM 3454 C CD2 . PHE B 1 24  ? -121.592 43.794 -7.314  1.00 114.82 ?  24  PHE B CD2 1 
ATOM 3455 C CE1 . PHE B 1 24  ? -120.549 45.455 -5.376  1.00 119.75 ?  24  PHE B CE1 1 
ATOM 3456 C CE2 . PHE B 1 24  ? -120.223 43.875 -7.140  1.00 111.15 ?  24  PHE B CE2 1 
ATOM 3457 C CZ  . PHE B 1 24  ? -119.701 44.707 -6.170  1.00 113.16 ?  24  PHE B CZ  1 
ATOM 3458 N N   . SER B 1 25  ? -127.000 45.399 -7.448  1.00 106.31 ?  25  SER B N   1 
ATOM 3459 C CA  . SER B 1 25  ? -128.229 45.152 -8.195  1.00 109.25 ?  25  SER B CA  1 
ATOM 3460 C C   . SER B 1 25  ? -128.466 46.237 -9.237  1.00 116.55 ?  25  SER B C   1 
ATOM 3461 O O   . SER B 1 25  ? -128.986 45.963 -10.324 1.00 111.16 ?  25  SER B O   1 
ATOM 3462 C CB  . SER B 1 25  ? -129.417 45.057 -7.239  1.00 103.99 ?  25  SER B CB  1 
ATOM 3463 O OG  . SER B 1 25  ? -130.637 44.943 -7.952  1.00 123.22 ?  25  SER B OG  1 
ATOM 3464 N N   . LEU B 1 26  ? -128.092 47.477 -8.919  1.00 105.31 ?  26  LEU B N   1 
ATOM 3465 C CA  . LEU B 1 26  ? -128.199 48.603 -9.837  1.00 102.64 ?  26  LEU B CA  1 
ATOM 3466 C C   . LEU B 1 26  ? -127.309 48.368 -11.051 1.00 113.18 ?  26  LEU B C   1 
ATOM 3467 O O   . LEU B 1 26  ? -126.079 48.341 -10.922 1.00 121.55 ?  26  LEU B O   1 
ATOM 3468 C CB  . LEU B 1 26  ? -127.812 49.904 -9.132  1.00 97.73  ?  26  LEU B CB  1 
ATOM 3469 C CG  . LEU B 1 26  ? -127.671 51.157 -10.000 1.00 119.81 ?  26  LEU B CG  1 
ATOM 3470 C CD1 . LEU B 1 26  ? -128.977 51.466 -10.717 1.00 126.61 ?  26  LEU B CD1 1 
ATOM 3471 C CD2 . LEU B 1 26  ? -127.214 52.344 -9.163  1.00 99.31  ?  26  LEU B CD2 1 
ATOM 3472 N N   . PRO B 1 27  ? -127.884 48.191 -12.240 1.00 131.66 ?  27  PRO B N   1 
ATOM 3473 C CA  . PRO B 1 27  ? -127.077 47.948 -13.444 1.00 127.29 ?  27  PRO B CA  1 
ATOM 3474 C C   . PRO B 1 27  ? -126.648 49.204 -14.189 1.00 126.13 ?  27  PRO B C   1 
ATOM 3475 O O   . PRO B 1 27  ? -126.160 49.087 -15.317 1.00 117.17 ?  27  PRO B O   1 
ATOM 3476 C CB  . PRO B 1 27  ? -128.039 47.123 -14.307 1.00 117.06 ?  27  PRO B CB  1 
ATOM 3477 C CG  . PRO B 1 27  ? -129.382 47.704 -13.981 1.00 114.41 ?  27  PRO B CG  1 
ATOM 3478 C CD  . PRO B 1 27  ? -129.327 48.159 -12.534 1.00 122.17 ?  27  PRO B CD  1 
ATOM 3479 N N   . GLN B 1 28  ? -126.813 50.387 -13.594 1.00 126.14 ?  28  GLN B N   1 
ATOM 3480 C CA  . GLN B 1 28  ? -126.543 51.624 -14.317 1.00 138.33 ?  28  GLN B CA  1 
ATOM 3481 C C   . GLN B 1 28  ? -125.052 51.837 -14.545 1.00 142.52 ?  28  GLN B C   1 
ATOM 3482 O O   . GLN B 1 28  ? -124.662 52.383 -15.584 1.00 144.56 ?  28  GLN B O   1 
ATOM 3483 C CB  . GLN B 1 28  ? -127.140 52.811 -13.561 1.00 130.31 ?  28  GLN B CB  1 
ATOM 3484 C CG  . GLN B 1 28  ? -128.201 53.578 -14.337 1.00 143.18 ?  28  GLN B CG  1 
ATOM 3485 C CD  . GLN B 1 28  ? -127.662 54.218 -15.602 1.00 152.26 ?  28  GLN B CD  1 
ATOM 3486 O OE1 . GLN B 1 28  ? -126.483 54.560 -15.686 1.00 154.01 ?  28  GLN B OE1 1 
ATOM 3487 N NE2 . GLN B 1 28  ? -128.527 54.382 -16.596 1.00 155.47 ?  28  GLN B NE2 1 
ATOM 3488 N N   . MET B 1 29  ? -124.210 51.414 -13.598 1.00 139.99 ?  29  MET B N   1 
ATOM 3489 C CA  . MET B 1 29  ? -122.768 51.666 -13.651 1.00 132.26 ?  29  MET B CA  1 
ATOM 3490 C C   . MET B 1 29  ? -122.480 53.161 -13.755 1.00 125.05 ?  29  MET B C   1 
ATOM 3491 O O   . MET B 1 29  ? -121.622 53.596 -14.526 1.00 112.07 ?  29  MET B O   1 
ATOM 3492 C CB  . MET B 1 29  ? -122.105 50.905 -14.804 1.00 112.30 ?  29  MET B CB  1 
ATOM 3493 C CG  . MET B 1 29  ? -121.864 49.431 -14.539 1.00 105.20 ?  29  MET B CG  1 
ATOM 3494 S SD  . MET B 1 29  ? -120.440 49.140 -13.473 1.00 133.20 ?  29  MET B SD  1 
ATOM 3495 C CE  . MET B 1 29  ? -120.299 47.359 -13.585 1.00 96.83  ?  29  MET B CE  1 
ATOM 3496 N N   . ASP B 1 30  ? -123.205 53.954 -12.976 1.00 133.14 ?  30  ASP B N   1 
ATOM 3497 C CA  . ASP B 1 30  ? -123.099 55.406 -13.048 1.00 135.68 ?  30  ASP B CA  1 
ATOM 3498 C C   . ASP B 1 30  ? -123.365 55.979 -11.658 1.00 146.84 ?  30  ASP B C   1 
ATOM 3499 O O   . ASP B 1 30  ? -123.291 55.266 -10.652 1.00 138.73 ?  30  ASP B O   1 
ATOM 3500 C CB  . ASP B 1 30  ? -124.044 55.964 -14.126 1.00 143.32 ?  30  ASP B CB  1 
ATOM 3501 C CG  . ASP B 1 30  ? -123.299 56.449 -15.358 1.00 161.00 ?  30  ASP B CG  1 
ATOM 3502 O OD1 . ASP B 1 30  ? -122.074 56.676 -15.263 1.00 164.89 ?  30  ASP B OD1 1 
ATOM 3503 O OD2 . ASP B 1 30  ? -123.937 56.601 -16.421 1.00 166.03 -1 30  ASP B OD2 1 
ATOM 3504 N N   . ASP B 1 31  ? -123.677 57.276 -11.607 1.00 154.28 ?  31  ASP B N   1 
ATOM 3505 C CA  . ASP B 1 31  ? -123.605 58.028 -10.358 1.00 161.27 ?  31  ASP B CA  1 
ATOM 3506 C C   . ASP B 1 31  ? -124.746 57.679 -9.405  1.00 149.27 ?  31  ASP B C   1 
ATOM 3507 O O   . ASP B 1 31  ? -124.513 57.333 -8.242  1.00 132.19 ?  31  ASP B O   1 
ATOM 3508 C CB  . ASP B 1 31  ? -123.611 59.529 -10.658 1.00 162.29 ?  31  ASP B CB  1 
ATOM 3509 C CG  . ASP B 1 31  ? -122.543 59.931 -11.654 1.00 157.26 ?  31  ASP B CG  1 
ATOM 3510 O OD1 . ASP B 1 31  ? -121.451 59.326 -11.638 1.00 160.49 ?  31  ASP B OD1 1 
ATOM 3511 O OD2 . ASP B 1 31  ? -122.797 60.857 -12.453 1.00 157.67 -1 31  ASP B OD2 1 
ATOM 3512 N N   . SER B 1 32  ? -125.986 57.765 -9.881  1.00 146.36 ?  32  SER B N   1 
ATOM 3513 C CA  . SER B 1 32  ? -127.141 57.991 -9.008  1.00 140.92 ?  32  SER B CA  1 
ATOM 3514 C C   . SER B 1 32  ? -127.413 56.788 -8.112  1.00 141.26 ?  32  SER B C   1 
ATOM 3515 O O   . SER B 1 32  ? -128.006 55.795 -8.539  1.00 139.05 ?  32  SER B O   1 
ATOM 3516 C CB  . SER B 1 32  ? -128.367 58.323 -9.850  1.00 130.66 ?  32  SER B CB  1 
ATOM 3517 O OG  . SER B 1 32  ? -128.169 59.515 -10.589 1.00 135.90 ?  32  SER B OG  1 
ATOM 3518 N N   . ILE B 1 33  ? -126.977 56.887 -6.854  1.00 142.73 ?  33  ILE B N   1 
ATOM 3519 C CA  . ILE B 1 33  ? -127.473 56.068 -5.751  1.00 141.86 ?  33  ILE B CA  1 
ATOM 3520 C C   . ILE B 1 33  ? -127.098 56.765 -4.446  1.00 139.19 ?  33  ILE B C   1 
ATOM 3521 O O   . ILE B 1 33  ? -125.950 57.188 -4.264  1.00 145.13 ?  33  ILE B O   1 
ATOM 3522 C CB  . ILE B 1 33  ? -126.933 54.624 -5.809  1.00 135.99 ?  33  ILE B CB  1 
ATOM 3523 C CG1 . ILE B 1 33  ? -127.192 53.893 -4.488  1.00 116.78 ?  33  ILE B CG1 1 
ATOM 3524 C CG2 . ILE B 1 33  ? -125.462 54.604 -6.185  1.00 130.41 ?  33  ILE B CG2 1 
ATOM 3525 C CD1 . ILE B 1 33  ? -128.655 53.602 -4.225  1.00 110.39 ?  33  ILE B CD1 1 
ATOM 3526 N N   . ASP B 1 34  ? -128.058 56.893 -3.531  1.00 130.53 ?  34  ASP B N   1 
ATOM 3527 C CA  . ASP B 1 34  ? -127.863 57.622 -2.285  1.00 125.99 ?  34  ASP B CA  1 
ATOM 3528 C C   . ASP B 1 34  ? -128.080 56.702 -1.090  1.00 121.99 ?  34  ASP B C   1 
ATOM 3529 O O   . ASP B 1 34  ? -128.905 55.784 -1.130  1.00 128.76 ?  34  ASP B O   1 
ATOM 3530 C CB  . ASP B 1 34  ? -128.804 58.830 -2.190  1.00 141.12 ?  34  ASP B CB  1 
ATOM 3531 C CG  . ASP B 1 34  ? -128.365 59.979 -3.076  1.00 152.84 ?  34  ASP B CG  1 
ATOM 3532 O OD1 . ASP B 1 34  ? -127.585 59.742 -4.023  1.00 155.36 ?  34  ASP B OD1 1 
ATOM 3533 O OD2 . ASP B 1 34  ? -128.796 61.124 -2.820  1.00 162.24 -1 34  ASP B OD2 1 
ATOM 3534 N N   . ILE B 1 35  ? -127.329 56.965 -0.022  1.00 103.39 ?  35  ILE B N   1 
ATOM 3535 C CA  . ILE B 1 35  ? -127.275 56.104 1.153   1.00 103.97 ?  35  ILE B CA  1 
ATOM 3536 C C   . ILE B 1 35  ? -127.759 56.882 2.370   1.00 119.73 ?  35  ILE B C   1 
ATOM 3537 O O   . ILE B 1 35  ? -127.399 58.049 2.557   1.00 110.03 ?  35  ILE B O   1 
ATOM 3538 C CB  . ILE B 1 35  ? -125.847 55.560 1.384   1.00 92.53  ?  35  ILE B CB  1 
ATOM 3539 C CG1 . ILE B 1 35  ? -125.613 54.278 0.579   1.00 92.19  ?  35  ILE B CG1 1 
ATOM 3540 C CG2 . ILE B 1 35  ? -125.581 55.309 2.863   1.00 103.73 ?  35  ILE B CG2 1 
ATOM 3541 C CD1 . ILE B 1 35  ? -125.487 54.482 -0.914  1.00 115.71 ?  35  ILE B CD1 1 
ATOM 3542 N N   . GLU B 1 36  ? -128.582 56.231 3.192   1.00 118.92 ?  36  GLU B N   1 
ATOM 3543 C CA  . GLU B 1 36  ? -128.929 56.762 4.506   1.00 119.48 ?  36  GLU B CA  1 
ATOM 3544 C C   . GLU B 1 36  ? -127.712 56.648 5.419   1.00 117.99 ?  36  GLU B C   1 
ATOM 3545 O O   . GLU B 1 36  ? -127.212 55.545 5.662   1.00 109.06 ?  36  GLU B O   1 
ATOM 3546 C CB  . GLU B 1 36  ? -130.126 56.006 5.072   1.00 116.63 ?  36  GLU B CB  1 
ATOM 3547 C CG  . GLU B 1 36  ? -131.371 56.107 4.197   1.00 112.26 ?  36  GLU B CG  1 
ATOM 3548 C CD  . GLU B 1 36  ? -132.175 54.820 4.154   1.00 112.73 ?  36  GLU B CD  1 
ATOM 3549 O OE1 . GLU B 1 36  ? -131.656 53.775 4.600   1.00 110.56 ?  36  GLU B OE1 1 
ATOM 3550 O OE2 . GLU B 1 36  ? -133.326 54.854 3.669   1.00 96.54  -1 36  GLU B OE2 1 
ATOM 3551 N N   . CYS B 1 37  ? -127.244 57.786 5.936   1.00 118.85 ?  37  CYS B N   1 
ATOM 3552 C CA  . CYS B 1 37  ? -125.843 57.939 6.320   1.00 128.87 ?  37  CYS B CA  1 
ATOM 3553 C C   . CYS B 1 37  ? -125.561 57.710 7.804   1.00 134.24 ?  37  CYS B C   1 
ATOM 3554 O O   . CYS B 1 37  ? -124.795 56.808 8.151   1.00 141.54 ?  37  CYS B O   1 
ATOM 3555 C CB  . CYS B 1 37  ? -125.358 59.338 5.911   1.00 136.26 ?  37  CYS B CB  1 
ATOM 3556 S SG  . CYS B 1 37  ? -125.085 59.548 4.135   1.00 118.42 ?  37  CYS B SG  1 
ATOM 3557 N N   . ILE B 1 38  ? -126.170 58.503 8.686   1.00 123.67 ?  38  ILE B N   1 
ATOM 3558 C CA  . ILE B 1 38  ? -125.642 58.723 10.033  1.00 146.08 ?  38  ILE B CA  1 
ATOM 3559 C C   . ILE B 1 38  ? -125.570 57.438 10.853  1.00 154.69 ?  38  ILE B C   1 
ATOM 3560 O O   . ILE B 1 38  ? -126.600 56.867 11.229  1.00 161.58 ?  38  ILE B O   1 
ATOM 3561 C CB  . ILE B 1 38  ? -126.481 59.780 10.776  1.00 144.52 ?  38  ILE B CB  1 
ATOM 3562 C CG1 . ILE B 1 38  ? -126.383 61.133 10.070  1.00 144.07 ?  38  ILE B CG1 1 
ATOM 3563 C CG2 . ILE B 1 38  ? -126.026 59.903 12.225  1.00 139.53 ?  38  ILE B CG2 1 
ATOM 3564 C CD1 . ILE B 1 38  ? -127.095 62.252 10.798  1.00 119.61 ?  38  ILE B CD1 1 
ATOM 3565 N N   . GLU B 1 39  ? -124.346 56.983 11.144  1.00 134.15 ?  39  GLU B N   1 
ATOM 3566 C CA  . GLU B 1 39  ? -124.125 55.882 12.078  1.00 130.49 ?  39  GLU B CA  1 
ATOM 3567 C C   . GLU B 1 39  ? -123.369 56.335 13.320  1.00 134.22 ?  39  GLU B C   1 
ATOM 3568 O O   . GLU B 1 39  ? -123.898 56.217 14.430  1.00 138.01 ?  39  GLU B O   1 
ATOM 3569 C CB  . GLU B 1 39  ? -123.364 54.740 11.389  1.00 138.48 ?  39  GLU B CB  1 
ATOM 3570 C CG  . GLU B 1 39  ? -123.791 54.440 9.962   1.00 123.73 ?  39  GLU B CG  1 
ATOM 3571 C CD  . GLU B 1 39  ? -125.195 53.881 9.873   1.00 129.89 ?  39  GLU B CD  1 
ATOM 3572 O OE1 . GLU B 1 39  ? -126.130 54.658 9.593   1.00 140.09 ?  39  GLU B OE1 1 
ATOM 3573 O OE2 . GLU B 1 39  ? -125.363 52.661 10.081  1.00 162.20 -1 39  GLU B OE2 1 
ATOM 3574 N N   . ASP B 1 40  ? -122.157 56.873 13.160  1.00 143.59 ?  40  ASP B N   1 
ATOM 3575 C CA  . ASP B 1 40  ? -121.332 57.398 14.252  1.00 152.59 ?  40  ASP B CA  1 
ATOM 3576 C C   . ASP B 1 40  ? -121.291 56.437 15.443  1.00 147.28 ?  40  ASP B C   1 
ATOM 3577 O O   . ASP B 1 40  ? -121.764 56.740 16.540  1.00 169.59 ?  40  ASP B O   1 
ATOM 3578 C CB  . ASP B 1 40  ? -121.823 58.785 14.681  1.00 170.83 ?  40  ASP B CB  1 
ATOM 3579 C CG  . ASP B 1 40  ? -120.752 59.594 15.397  1.00 164.45 ?  40  ASP B CG  1 
ATOM 3580 O OD1 . ASP B 1 40  ? -119.988 59.012 16.195  1.00 163.44 ?  40  ASP B OD1 1 
ATOM 3581 O OD2 . ASP B 1 40  ? -120.676 60.818 15.160  1.00 159.34 -1 40  ASP B OD2 1 
ATOM 3582 N N   . VAL B 1 41  ? -120.709 55.261 15.215  1.00 136.82 ?  41  VAL B N   1 
ATOM 3583 C CA  . VAL B 1 41  ? -120.740 54.217 16.238  1.00 144.46 ?  41  VAL B CA  1 
ATOM 3584 C C   . VAL B 1 41  ? -119.525 54.284 17.161  1.00 150.21 ?  41  VAL B C   1 
ATOM 3585 O O   . VAL B 1 41  ? -119.651 54.025 18.361  1.00 154.18 ?  41  VAL B O   1 
ATOM 3586 C CB  . VAL B 1 41  ? -120.887 52.825 15.585  1.00 122.00 ?  41  VAL B CB  1 
ATOM 3587 C CG1 . VAL B 1 41  ? -119.640 52.438 14.813  1.00 133.24 ?  41  VAL B CG1 1 
ATOM 3588 C CG2 . VAL B 1 41  ? -121.211 51.776 16.640  1.00 114.58 ?  41  VAL B CG2 1 
ATOM 3589 N N   . ASP B 1 42  ? -118.342 54.632 16.642  1.00 144.03 ?  42  ASP B N   1 
ATOM 3590 C CA  . ASP B 1 42  ? -117.114 54.702 17.441  1.00 157.37 ?  42  ASP B CA  1 
ATOM 3591 C C   . ASP B 1 42  ? -116.848 53.355 18.122  1.00 142.03 ?  42  ASP B C   1 
ATOM 3592 O O   . ASP B 1 42  ? -116.945 53.198 19.341  1.00 151.38 ?  42  ASP B O   1 
ATOM 3593 C CB  . ASP B 1 42  ? -117.173 55.852 18.455  1.00 180.30 ?  42  ASP B CB  1 
ATOM 3594 C CG  . ASP B 1 42  ? -115.796 56.380 18.818  1.00 184.31 ?  42  ASP B CG  1 
ATOM 3595 O OD1 . ASP B 1 42  ? -114.880 55.560 19.043  1.00 169.85 ?  42  ASP B OD1 1 
ATOM 3596 O OD2 . ASP B 1 42  ? -115.628 57.616 18.872  1.00 192.18 -1 42  ASP B OD2 1 
ATOM 3597 N N   . VAL B 1 43  ? -116.497 52.384 17.281  1.00 135.02 ?  43  VAL B N   1 
ATOM 3598 C CA  . VAL B 1 43  ? -116.674 50.960 17.553  1.00 135.34 ?  43  VAL B CA  1 
ATOM 3599 C C   . VAL B 1 43  ? -115.575 50.424 18.469  1.00 132.38 ?  43  VAL B C   1 
ATOM 3600 O O   . VAL B 1 43  ? -115.414 49.207 18.617  1.00 126.95 ?  43  VAL B O   1 
ATOM 3601 C CB  . VAL B 1 43  ? -116.735 50.181 16.221  1.00 121.20 ?  43  VAL B CB  1 
ATOM 3602 C CG1 . VAL B 1 43  ? -115.360 50.108 15.575  1.00 121.46 ?  43  VAL B CG1 1 
ATOM 3603 C CG2 . VAL B 1 43  ? -117.367 48.795 16.395  1.00 101.72 ?  43  VAL B CG2 1 
ATOM 3604 N N   . TYR B 1 44  ? -114.799 51.324 19.081  1.00 139.58 ?  44  TYR B N   1 
ATOM 3605 C CA  . TYR B 1 44  ? -113.878 50.911 20.139  1.00 140.66 ?  44  TYR B CA  1 
ATOM 3606 C C   . TYR B 1 44  ? -114.591 50.050 21.179  1.00 136.66 ?  44  TYR B C   1 
ATOM 3607 O O   . TYR B 1 44  ? -114.083 49.001 21.591  1.00 128.01 ?  44  TYR B O   1 
ATOM 3608 C CB  . TYR B 1 44  ? -113.244 52.144 20.793  1.00 132.39 ?  44  TYR B CB  1 
ATOM 3609 C CG  . TYR B 1 44  ? -111.886 51.905 21.435  1.00 137.94 ?  44  TYR B CG  1 
ATOM 3610 C CD1 . TYR B 1 44  ? -110.861 52.834 21.301  1.00 135.39 ?  44  TYR B CD1 1 
ATOM 3611 C CD2 . TYR B 1 44  ? -111.634 50.762 22.187  1.00 137.94 ?  44  TYR B CD2 1 
ATOM 3612 C CE1 . TYR B 1 44  ? -109.622 52.625 21.888  1.00 133.27 ?  44  TYR B CE1 1 
ATOM 3613 C CE2 . TYR B 1 44  ? -110.400 50.546 22.777  1.00 139.47 ?  44  TYR B CE2 1 
ATOM 3614 C CZ  . TYR B 1 44  ? -109.399 51.481 22.624  1.00 145.01 ?  44  TYR B CZ  1 
ATOM 3615 O OH  . TYR B 1 44  ? -108.173 51.267 23.211  1.00 147.72 ?  44  TYR B OH  1 
ATOM 3616 N N   . ASN B 1 45  ? -115.780 50.473 21.606  1.00 133.27 ?  45  ASN B N   1 
ATOM 3617 C CA  . ASN B 1 45  ? -116.598 49.696 22.529  1.00 131.73 ?  45  ASN B CA  1 
ATOM 3618 C C   . ASN B 1 45  ? -117.930 49.286 21.923  1.00 127.91 ?  45  ASN B C   1 
ATOM 3619 O O   . ASN B 1 45  ? -118.288 48.104 21.979  1.00 137.27 ?  45  ASN B O   1 
ATOM 3620 C CB  . ASN B 1 45  ? -116.832 50.489 23.824  1.00 140.55 ?  45  ASN B CB  1 
ATOM 3621 C CG  . ASN B 1 45  ? -115.878 50.085 24.928  1.00 135.07 ?  45  ASN B CG  1 
ATOM 3622 O OD1 . ASN B 1 45  ? -115.334 48.981 24.915  1.00 130.78 ?  45  ASN B OD1 1 
ATOM 3623 N ND2 . ASN B 1 45  ? -115.664 50.978 25.889  1.00 115.47 ?  45  ASN B ND2 1 
ATOM 3624 N N   . ASP B 1 46  ? -118.696 50.244 21.393  1.00 118.45 ?  46  ASP B N   1 
ATOM 3625 C CA  . ASP B 1 46  ? -119.883 50.015 20.569  1.00 111.42 ?  46  ASP B CA  1 
ATOM 3626 C C   . ASP B 1 46  ? -120.994 49.276 21.310  1.00 115.79 ?  46  ASP B C   1 
ATOM 3627 O O   . ASP B 1 46  ? -122.029 48.952 20.718  1.00 103.87 ?  46  ASP B O   1 
ATOM 3628 C CB  . ASP B 1 46  ? -119.504 49.270 19.276  1.00 116.24 ?  46  ASP B CB  1 
ATOM 3629 C CG  . ASP B 1 46  ? -119.410 47.758 19.454  1.00 116.34 ?  46  ASP B CG  1 
ATOM 3630 O OD1 . ASP B 1 46  ? -120.460 47.083 19.489  1.00 88.74  ?  46  ASP B OD1 1 
ATOM 3631 O OD2 . ASP B 1 46  ? -118.278 47.239 19.561  1.00 126.03 -1 46  ASP B OD2 1 
ATOM 3632 N N   . GLY B 1 47  ? -120.808 49.030 22.604  1.00 127.56 ?  47  GLY B N   1 
ATOM 3633 C CA  . GLY B 1 47  ? -121.729 48.200 23.354  1.00 110.03 ?  47  GLY B CA  1 
ATOM 3634 C C   . GLY B 1 47  ? -123.110 48.789 23.557  1.00 102.74 ?  47  GLY B C   1 
ATOM 3635 O O   . GLY B 1 47  ? -124.104 48.241 23.070  1.00 107.48 ?  47  GLY B O   1 
ATOM 3636 N N   . HIS B 1 48  ? -123.182 49.914 24.272  1.00 103.37 ?  48  HIS B N   1 
ATOM 3637 C CA  . HIS B 1 48  ? -124.474 50.442 24.697  1.00 111.57 ?  48  HIS B CA  1 
ATOM 3638 C C   . HIS B 1 48  ? -125.245 51.083 23.550  1.00 108.18 ?  48  HIS B C   1 
ATOM 3639 O O   . HIS B 1 48  ? -126.482 51.094 23.570  1.00 120.74 ?  48  HIS B O   1 
ATOM 3640 C CB  . HIS B 1 48  ? -124.278 51.455 25.825  1.00 123.80 ?  48  HIS B CB  1 
ATOM 3641 C CG  . HIS B 1 48  ? -123.920 50.837 27.140  1.00 136.77 ?  48  HIS B CG  1 
ATOM 3642 N ND1 . HIS B 1 48  ? -124.257 51.410 28.348  1.00 122.20 ?  48  HIS B ND1 1 
ATOM 3643 C CD2 . HIS B 1 48  ? -123.249 49.699 27.438  1.00 143.06 ?  48  HIS B CD2 1 
ATOM 3644 C CE1 . HIS B 1 48  ? -123.812 50.650 29.333  1.00 136.23 ?  48  HIS B CE1 1 
ATOM 3645 N NE2 . HIS B 1 48  ? -123.197 49.606 28.808  1.00 138.91 ?  48  HIS B NE2 1 
ATOM 3646 N N   . LEU B 1 49  ? -124.550 51.622 22.553  1.00 99.22  ?  49  LEU B N   1 
ATOM 3647 C CA  . LEU B 1 49  ? -125.203 52.383 21.494  1.00 128.39 ?  49  LEU B CA  1 
ATOM 3648 C C   . LEU B 1 49  ? -125.903 51.434 20.528  1.00 121.01 ?  49  LEU B C   1 
ATOM 3649 O O   . LEU B 1 49  ? -125.258 50.583 19.905  1.00 99.84  ?  49  LEU B O   1 
ATOM 3650 C CB  . LEU B 1 49  ? -124.186 53.254 20.761  1.00 136.85 ?  49  LEU B CB  1 
ATOM 3651 C CG  . LEU B 1 49  ? -123.486 54.330 21.598  1.00 127.66 ?  49  LEU B CG  1 
ATOM 3652 C CD1 . LEU B 1 49  ? -122.209 53.799 22.241  1.00 120.93 ?  49  LEU B CD1 1 
ATOM 3653 C CD2 . LEU B 1 49  ? -123.198 55.565 20.759  1.00 98.94  ?  49  LEU B CD2 1 
ATOM 3654 N N   . THR B 1 50  ? -127.224 51.582 20.400  1.00 126.77 ?  50  THR B N   1 
ATOM 3655 C CA  . THR B 1 50  ? -128.053 50.713 19.559  1.00 114.03 ?  50  THR B CA  1 
ATOM 3656 C C   . THR B 1 50  ? -128.884 51.582 18.617  1.00 107.27 ?  50  THR B C   1 
ATOM 3657 O O   . THR B 1 50  ? -129.986 52.012 18.966  1.00 101.77 ?  50  THR B O   1 
ATOM 3658 C CB  . THR B 1 50  ? -128.954 49.809 20.408  1.00 121.80 ?  50  THR B CB  1 
ATOM 3659 O OG1 . THR B 1 50  ? -130.051 50.575 20.923  1.00 118.34 ?  50  THR B OG1 1 
ATOM 3660 C CG2 . THR B 1 50  ? -128.181 49.192 21.566  1.00 104.49 ?  50  THR B CG2 1 
ATOM 3661 N N   . ALA B 1 51  ? -128.355 51.837 17.420  1.00 108.51 ?  51  ALA B N   1 
ATOM 3662 C CA  . ALA B 1 51  ? -129.127 52.480 16.366  1.00 92.84  ?  51  ALA B CA  1 
ATOM 3663 C C   . ALA B 1 51  ? -129.668 51.490 15.345  1.00 87.94  ?  51  ALA B C   1 
ATOM 3664 O O   . ALA B 1 51  ? -130.575 51.840 14.583  1.00 79.87  ?  51  ALA B O   1 
ATOM 3665 C CB  . ALA B 1 51  ? -128.278 53.538 15.649  1.00 91.40  ?  51  ALA B CB  1 
ATOM 3666 N N   . ILE B 1 52  ? -129.139 50.269 15.321  1.00 92.60  ?  52  ILE B N   1 
ATOM 3667 C CA  . ILE B 1 52  ? -129.565 49.226 14.396  1.00 76.38  ?  52  ILE B CA  1 
ATOM 3668 C C   . ILE B 1 52  ? -129.540 47.899 15.142  1.00 76.12  ?  52  ILE B C   1 
ATOM 3669 O O   . ILE B 1 52  ? -128.579 47.599 15.859  1.00 84.75  ?  52  ILE B O   1 
ATOM 3670 C CB  . ILE B 1 52  ? -128.658 49.170 13.148  1.00 77.51  ?  52  ILE B CB  1 
ATOM 3671 C CG1 . ILE B 1 52  ? -128.809 50.437 12.303  1.00 85.10  ?  52  ILE B CG1 1 
ATOM 3672 C CG2 . ILE B 1 52  ? -128.986 47.954 12.311  1.00 97.49  ?  52  ILE B CG2 1 
ATOM 3673 C CD1 . ILE B 1 52  ? -127.903 50.472 11.092  1.00 82.79  ?  52  ILE B CD1 1 
ATOM 3674 N N   . GLN B 1 53  ? -130.596 47.105 14.981  1.00 75.39  ?  53  GLN B N   1 
ATOM 3675 C CA  . GLN B 1 53  ? -130.679 45.814 15.649  1.00 90.60  ?  53  GLN B CA  1 
ATOM 3676 C C   . GLN B 1 53  ? -131.410 44.830 14.750  1.00 82.48  ?  53  GLN B C   1 
ATOM 3677 O O   . GLN B 1 53  ? -132.191 45.225 13.881  1.00 80.78  ?  53  GLN B O   1 
ATOM 3678 C CB  . GLN B 1 53  ? -131.391 45.919 17.000  1.00 83.33  ?  53  GLN B CB  1 
ATOM 3679 C CG  . GLN B 1 53  ? -130.874 44.955 18.050  1.00 104.24 ?  53  GLN B CG  1 
ATOM 3680 C CD  . GLN B 1 53  ? -130.643 45.635 19.382  1.00 107.53 ?  53  GLN B CD  1 
ATOM 3681 O OE1 . GLN B 1 53  ? -130.325 46.823 19.434  1.00 96.36  ?  53  GLN B OE1 1 
ATOM 3682 N NE2 . GLN B 1 53  ? -130.809 44.889 20.469  1.00 89.29  ?  53  GLN B NE2 1 
ATOM 3683 N N   . CYS B 1 54  ? -131.151 43.543 14.971  1.00 75.79  ?  54  CYS B N   1 
ATOM 3684 C CA  . CYS B 1 54  ? -131.740 42.492 14.149  1.00 89.49  ?  54  CYS B CA  1 
ATOM 3685 C C   . CYS B 1 54  ? -131.882 41.234 14.990  1.00 99.94  ?  54  CYS B C   1 
ATOM 3686 O O   . CYS B 1 54  ? -130.881 40.702 15.480  1.00 92.41  ?  54  CYS B O   1 
ATOM 3687 C CB  . CYS B 1 54  ? -130.883 42.220 12.916  1.00 98.77  ?  54  CYS B CB  1 
ATOM 3688 S SG  . CYS B 1 54  ? -131.741 41.393 11.568  1.00 134.23 ?  54  CYS B SG  1 
ATOM 3689 N N   . LYS B 1 55  ? -133.115 40.761 15.146  1.00 96.71  ?  55  LYS B N   1 
ATOM 3690 C CA  . LYS B 1 55  ? -133.423 39.572 15.928  1.00 93.55  ?  55  LYS B CA  1 
ATOM 3691 C C   . LYS B 1 55  ? -133.793 38.416 15.009  1.00 83.64  ?  55  LYS B C   1 
ATOM 3692 O O   . LYS B 1 55  ? -134.467 38.610 13.994  1.00 78.06  ?  55  LYS B O   1 
ATOM 3693 C CB  . LYS B 1 55  ? -134.576 39.841 16.902  1.00 87.51  ?  55  LYS B CB  1 
ATOM 3694 C CG  . LYS B 1 55  ? -134.591 41.242 17.488  1.00 78.27  ?  55  LYS B CG  1 
ATOM 3695 C CD  . LYS B 1 55  ? -133.743 41.317 18.744  1.00 68.43  ?  55  LYS B CD  1 
ATOM 3696 C CE  . LYS B 1 55  ? -133.779 42.711 19.344  1.00 79.77  ?  55  LYS B CE  1 
ATOM 3697 N NZ  . LYS B 1 55  ? -134.042 43.745 18.302  1.00 84.76  ?  55  LYS B NZ  1 
ATOM 3698 N N   . TYR B 1 56  ? -133.351 37.209 15.372  1.00 89.94  ?  56  TYR B N   1 
ATOM 3699 C CA  . TYR B 1 56  ? -133.710 35.987 14.649  1.00 91.71  ?  56  TYR B CA  1 
ATOM 3700 C C   . TYR B 1 56  ? -134.201 34.975 15.675  1.00 111.44 ?  56  TYR B C   1 
ATOM 3701 O O   . TYR B 1 56  ? -133.435 34.140 16.161  1.00 111.66 ?  56  TYR B O   1 
ATOM 3702 C CB  . TYR B 1 56  ? -132.532 35.439 13.830  1.00 100.67 ?  56  TYR B CB  1 
ATOM 3703 C CG  . TYR B 1 56  ? -131.968 36.413 12.826  1.00 109.90 ?  56  TYR B CG  1 
ATOM 3704 C CD1 . TYR B 1 56  ? -132.349 36.359 11.494  1.00 94.46  ?  56  TYR B CD1 1 
ATOM 3705 C CD2 . TYR B 1 56  ? -131.043 37.378 13.204  1.00 102.95 ?  56  TYR B CD2 1 
ATOM 3706 C CE1 . TYR B 1 56  ? -131.843 37.249 10.569  1.00 89.84  ?  56  TYR B CE1 1 
ATOM 3707 C CE2 . TYR B 1 56  ? -130.527 38.271 12.283  1.00 77.78  ?  56  TYR B CE2 1 
ATOM 3708 C CZ  . TYR B 1 56  ? -130.928 38.203 10.966  1.00 97.08  ?  56  TYR B CZ  1 
ATOM 3709 O OH  . TYR B 1 56  ? -130.413 39.093 10.047  1.00 120.47 ?  56  TYR B OH  1 
ATOM 3710 N N   . TYR B 1 57  ? -135.488 35.053 16.002  1.00 122.49 ?  57  TYR B N   1 
ATOM 3711 C CA  . TYR B 1 57  ? -136.127 34.056 16.855  1.00 134.85 ?  57  TYR B CA  1 
ATOM 3712 C C   . TYR B 1 57  ? -136.856 33.035 15.982  1.00 132.06 ?  57  TYR B C   1 
ATOM 3713 O O   . TYR B 1 57  ? -138.086 32.972 15.924  1.00 129.99 ?  57  TYR B O   1 
ATOM 3714 C CB  . TYR B 1 57  ? -137.072 34.726 17.854  1.00 136.42 ?  57  TYR B CB  1 
ATOM 3715 C CG  . TYR B 1 57  ? -136.408 35.378 19.051  1.00 139.08 ?  57  TYR B CG  1 
ATOM 3716 C CD1 . TYR B 1 57  ? -136.004 34.621 20.148  1.00 141.11 ?  57  TYR B CD1 1 
ATOM 3717 C CD2 . TYR B 1 57  ? -136.202 36.752 19.095  1.00 132.61 ?  57  TYR B CD2 1 
ATOM 3718 C CE1 . TYR B 1 57  ? -135.407 35.218 21.250  1.00 140.08 ?  57  TYR B CE1 1 
ATOM 3719 C CE2 . TYR B 1 57  ? -135.604 37.354 20.193  1.00 138.42 ?  57  TYR B CE2 1 
ATOM 3720 C CZ  . TYR B 1 57  ? -135.208 36.584 21.267  1.00 143.65 ?  57  TYR B CZ  1 
ATOM 3721 O OH  . TYR B 1 57  ? -134.613 37.180 22.358  1.00 138.56 ?  57  TYR B OH  1 
ATOM 3722 N N   . GLU B 1 58  ? -136.060 32.233 15.279  1.00 150.42 ?  58  GLU B N   1 
ATOM 3723 C CA  . GLU B 1 58  ? -136.618 31.057 14.638  1.00 158.44 ?  58  GLU B CA  1 
ATOM 3724 C C   . GLU B 1 58  ? -137.034 30.055 15.713  1.00 163.58 ?  58  GLU B C   1 
ATOM 3725 O O   . GLU B 1 58  ? -136.535 30.074 16.841  1.00 176.38 ?  58  GLU B O   1 
ATOM 3726 C CB  . GLU B 1 58  ? -135.610 30.432 13.675  1.00 162.32 ?  58  GLU B CB  1 
ATOM 3727 C CG  . GLU B 1 58  ? -135.964 30.615 12.203  1.00 142.59 ?  58  GLU B CG  1 
ATOM 3728 C CD  . GLU B 1 58  ? -137.326 30.050 11.851  1.00 157.87 ?  58  GLU B CD  1 
ATOM 3729 O OE1 . GLU B 1 58  ? -138.110 30.753 11.179  1.00 150.54 ?  58  GLU B OE1 1 
ATOM 3730 O OE2 . GLU B 1 58  ? -137.625 28.910 12.263  1.00 177.44 -1 58  GLU B OE2 1 
ATOM 3731 N N   . SER B 1 59  ? -137.977 29.182 15.353  1.00 161.16 ?  59  SER B N   1 
ATOM 3732 C CA  . SER B 1 59  ? -138.728 28.347 16.295  1.00 153.65 ?  59  SER B CA  1 
ATOM 3733 C C   . SER B 1 59  ? -139.430 29.175 17.370  1.00 151.59 ?  59  SER B C   1 
ATOM 3734 O O   . SER B 1 59  ? -139.776 28.654 18.438  1.00 168.57 ?  59  SER B O   1 
ATOM 3735 C CB  . SER B 1 59  ? -137.841 27.278 16.944  1.00 156.34 ?  59  SER B CB  1 
ATOM 3736 O OG  . SER B 1 59  ? -138.403 26.840 18.169  1.00 154.14 ?  59  SER B OG  1 
ATOM 3737 N N   . THR B 1 60  ? -139.643 30.460 17.090  1.00 136.93 ?  60  THR B N   1 
ATOM 3738 C CA  . THR B 1 60  ? -140.318 31.395 17.977  1.00 142.48 ?  60  THR B CA  1 
ATOM 3739 C C   . THR B 1 60  ? -141.149 32.334 17.114  1.00 118.10 ?  60  THR B C   1 
ATOM 3740 O O   . THR B 1 60  ? -140.901 32.486 15.916  1.00 110.77 ?  60  THR B O   1 
ATOM 3741 C CB  . THR B 1 60  ? -139.324 32.200 18.827  1.00 143.93 ?  60  THR B CB  1 
ATOM 3742 O OG1 . THR B 1 60  ? -138.194 31.384 19.157  1.00 153.47 ?  60  THR B OG1 1 
ATOM 3743 C CG2 . THR B 1 60  ? -139.982 32.716 20.109  1.00 121.41 ?  60  THR B CG2 1 
ATOM 3744 N N   . ASP B 1 61  ? -142.119 32.994 17.735  1.00 113.32 ?  61  ASP B N   1 
ATOM 3745 C CA  . ASP B 1 61  ? -143.092 33.805 17.017  1.00 113.97 ?  61  ASP B CA  1 
ATOM 3746 C C   . ASP B 1 61  ? -142.878 35.278 17.328  1.00 105.31 ?  61  ASP B C   1 
ATOM 3747 O O   . ASP B 1 61  ? -142.417 35.630 18.420  1.00 113.07 ?  61  ASP B O   1 
ATOM 3748 C CB  . ASP B 1 61  ? -144.514 33.387 17.388  1.00 133.41 ?  61  ASP B CB  1 
ATOM 3749 C CG  . ASP B 1 61  ? -144.664 31.881 17.485  1.00 147.21 ?  61  ASP B CG  1 
ATOM 3750 O OD1 . ASP B 1 61  ? -143.909 31.266 18.272  1.00 163.83 ?  61  ASP B OD1 1 
ATOM 3751 O OD2 . ASP B 1 61  ? -145.521 31.312 16.776  1.00 147.80 -1 61  ASP B OD2 1 
ATOM 3752 N N   . TYR B 1 62  ? -143.187 36.144 16.362  1.00 96.04  ?  62  TYR B N   1 
ATOM 3753 C CA  . TYR B 1 62  ? -143.095 37.561 16.673  1.00 90.85  ?  62  TYR B CA  1 
ATOM 3754 C C   . TYR B 1 62  ? -144.148 37.880 17.722  1.00 95.93  ?  62  TYR B C   1 
ATOM 3755 O O   . TYR B 1 62  ? -145.346 37.866 17.432  1.00 109.15 ?  62  TYR B O   1 
ATOM 3756 C CB  . TYR B 1 62  ? -143.264 38.435 15.419  1.00 89.98  ?  62  TYR B CB  1 
ATOM 3757 C CG  . TYR B 1 62  ? -143.662 39.872 15.718  1.00 98.41  ?  62  TYR B CG  1 
ATOM 3758 C CD1 . TYR B 1 62  ? -144.997 40.259 15.723  1.00 89.49  ?  62  TYR B CD1 1 
ATOM 3759 C CD2 . TYR B 1 62  ? -142.703 40.833 16.027  1.00 105.98 ?  62  TYR B CD2 1 
ATOM 3760 C CE1 . TYR B 1 62  ? -145.371 41.557 16.005  1.00 99.05  ?  62  TYR B CE1 1 
ATOM 3761 C CE2 . TYR B 1 62  ? -143.072 42.141 16.312  1.00 101.98 ?  62  TYR B CE2 1 
ATOM 3762 C CZ  . TYR B 1 62  ? -144.409 42.493 16.299  1.00 107.01 ?  62  TYR B CZ  1 
ATOM 3763 O OH  . TYR B 1 62  ? -144.805 43.777 16.580  1.00 110.82 ?  62  TYR B OH  1 
ATOM 3764 N N   . ASN B 1 63  ? -143.710 38.096 18.954  1.00 95.51  ?  63  ASN B N   1 
ATOM 3765 C CA  . ASN B 1 63  ? -144.550 38.725 19.955  1.00 101.55 ?  63  ASN B CA  1 
ATOM 3766 C C   . ASN B 1 63  ? -144.251 40.217 19.905  1.00 108.59 ?  63  ASN B C   1 
ATOM 3767 O O   . ASN B 1 63  ? -143.553 40.696 19.010  1.00 111.09 ?  63  ASN B O   1 
ATOM 3768 C CB  . ASN B 1 63  ? -144.301 38.127 21.338  1.00 103.11 ?  63  ASN B CB  1 
ATOM 3769 C CG  . ASN B 1 63  ? -145.559 38.069 22.184  1.00 119.89 ?  63  ASN B CG  1 
ATOM 3770 O OD1 . ASN B 1 63  ? -146.663 38.301 21.689  1.00 120.19 ?  63  ASN B OD1 1 
ATOM 3771 N ND2 . ASN B 1 63  ? -145.399 37.764 23.466  1.00 96.77  ?  63  ASN B ND2 1 
ATOM 3772 N N   . HIS B 1 64  ? -144.744 40.972 20.872  1.00 108.82 ?  64  HIS B N   1 
ATOM 3773 C CA  . HIS B 1 64  ? -144.339 42.356 20.995  1.00 91.68  ?  64  HIS B CA  1 
ATOM 3774 C C   . HIS B 1 64  ? -143.508 42.603 22.238  1.00 96.08  ?  64  HIS B C   1 
ATOM 3775 O O   . HIS B 1 64  ? -142.863 43.651 22.329  1.00 98.97  ?  64  HIS B O   1 
ATOM 3776 C CB  . HIS B 1 64  ? -145.571 43.274 20.970  1.00 95.28  ?  64  HIS B CB  1 
ATOM 3777 C CG  . HIS B 1 64  ? -146.571 42.891 19.921  1.00 110.82 ?  64  HIS B CG  1 
ATOM 3778 N ND1 . HIS B 1 64  ? -146.830 43.672 18.814  1.00 108.88 ?  64  HIS B ND1 1 
ATOM 3779 C CD2 . HIS B 1 64  ? -147.380 41.812 19.813  1.00 116.50 ?  64  HIS B CD2 1 
ATOM 3780 C CE1 . HIS B 1 64  ? -147.749 43.088 18.066  1.00 103.45 ?  64  HIS B CE1 1 
ATOM 3781 N NE2 . HIS B 1 64  ? -148.101 41.958 18.651  1.00 109.39 ?  64  HIS B NE2 1 
ATOM 3782 N N   . SER B 1 65  ? -143.469 41.651 23.175  1.00 97.68  ?  65  SER B N   1 
ATOM 3783 C CA  . SER B 1 65  ? -142.587 41.775 24.327  1.00 98.75  ?  65  SER B CA  1 
ATOM 3784 C C   . SER B 1 65  ? -141.123 41.596 23.952  1.00 102.98 ?  65  SER B C   1 
ATOM 3785 O O   . SER B 1 65  ? -140.249 41.922 24.761  1.00 102.82 ?  65  SER B O   1 
ATOM 3786 C CB  . SER B 1 65  ? -142.967 40.758 25.407  1.00 111.49 ?  65  SER B CB  1 
ATOM 3787 O OG  . SER B 1 65  ? -142.870 39.423 24.935  1.00 104.88 ?  65  SER B OG  1 
ATOM 3788 N N   . VAL B 1 66  ? -140.836 41.085 22.758  1.00 105.07 ?  66  VAL B N   1 
ATOM 3789 C CA  . VAL B 1 66  ? -139.459 40.837 22.339  1.00 98.77  ?  66  VAL B CA  1 
ATOM 3790 C C   . VAL B 1 66  ? -138.814 42.095 21.771  1.00 88.87  ?  66  VAL B C   1 
ATOM 3791 O O   . VAL B 1 66  ? -137.681 42.438 22.118  1.00 103.08 ?  66  VAL B O   1 
ATOM 3792 C CB  . VAL B 1 66  ? -139.421 39.672 21.326  1.00 118.84 ?  66  VAL B CB  1 
ATOM 3793 C CG1 . VAL B 1 66  ? -139.440 38.338 22.053  1.00 107.04 ?  66  VAL B CG1 1 
ATOM 3794 C CG2 . VAL B 1 66  ? -140.596 39.767 20.365  1.00 103.83 ?  66  VAL B CG2 1 
ATOM 3795 N N   . ILE B 1 67  ? -139.520 42.809 20.895  1.00 85.16  ?  67  ILE B N   1 
ATOM 3796 C CA  . ILE B 1 67  ? -138.994 44.025 20.287  1.00 84.28  ?  67  ILE B CA  1 
ATOM 3797 C C   . ILE B 1 67  ? -139.531 45.281 20.967  1.00 90.68  ?  67  ILE B C   1 
ATOM 3798 O O   . ILE B 1 67  ? -139.347 46.386 20.451  1.00 85.99  ?  67  ILE B O   1 
ATOM 3799 C CB  . ILE B 1 67  ? -139.278 44.058 18.775  1.00 68.74  ?  67  ILE B CB  1 
ATOM 3800 C CG1 . ILE B 1 67  ? -140.766 44.298 18.506  1.00 96.29  ?  67  ILE B CG1 1 
ATOM 3801 C CG2 . ILE B 1 67  ? -138.826 42.759 18.117  1.00 83.65  ?  67  ILE B CG2 1 
ATOM 3802 C CD1 . ILE B 1 67  ? -141.044 44.899 17.144  1.00 105.77 ?  67  ILE B CD1 1 
ATOM 3803 N N   . SER B 1 68  ? -140.190 45.138 22.120  1.00 83.24  ?  68  SER B N   1 
ATOM 3804 C CA  . SER B 1 68  ? -140.726 46.307 22.810  1.00 85.01  ?  68  SER B CA  1 
ATOM 3805 C C   . SER B 1 68  ? -139.607 47.216 23.300  1.00 94.12  ?  68  SER B C   1 
ATOM 3806 O O   . SER B 1 68  ? -139.578 48.410 22.982  1.00 91.73  ?  68  SER B O   1 
ATOM 3807 C CB  . SER B 1 68  ? -141.612 45.872 23.977  1.00 91.41  ?  68  SER B CB  1 
ATOM 3808 O OG  . SER B 1 68  ? -140.877 45.838 25.187  1.00 111.39 ?  68  SER B OG  1 
ATOM 3809 N N   . LYS B 1 69  ? -138.666 46.663 24.075  1.00 84.09  ?  69  LYS B N   1 
ATOM 3810 C CA  . LYS B 1 69  ? -137.599 47.497 24.628  1.00 91.35  ?  69  LYS B CA  1 
ATOM 3811 C C   . LYS B 1 69  ? -136.633 47.998 23.561  1.00 82.94  ?  69  LYS B C   1 
ATOM 3812 O O   . LYS B 1 69  ? -136.271 49.187 23.604  1.00 82.47  ?  69  LYS B O   1 
ATOM 3813 C CB  . LYS B 1 69  ? -136.871 46.744 25.747  1.00 96.31  ?  69  LYS B CB  1 
ATOM 3814 C CG  . LYS B 1 69  ? -135.669 47.491 26.303  1.00 93.90  ?  69  LYS B CG  1 
ATOM 3815 C CD  . LYS B 1 69  ? -134.859 46.632 27.259  1.00 94.44  ?  69  LYS B CD  1 
ATOM 3816 C CE  . LYS B 1 69  ? -133.702 47.426 27.849  1.00 111.69 ?  69  LYS B CE  1 
ATOM 3817 N NZ  . LYS B 1 69  ? -134.161 48.360 28.918  1.00 126.39 ?  69  LYS B NZ  1 
ATOM 3818 N N   . PRO B 1 70  ? -136.160 47.179 22.606  1.00 83.70  ?  70  PRO B N   1 
ATOM 3819 C CA  . PRO B 1 70  ? -135.293 47.731 21.548  1.00 75.09  ?  70  PRO B CA  1 
ATOM 3820 C C   . PRO B 1 70  ? -135.897 48.925 20.833  1.00 72.61  ?  70  PRO B C   1 
ATOM 3821 O O   . PRO B 1 70  ? -135.161 49.832 20.425  1.00 86.41  ?  70  PRO B O   1 
ATOM 3822 C CB  . PRO B 1 70  ? -135.104 46.546 20.594  1.00 71.25  ?  70  PRO B CB  1 
ATOM 3823 C CG  . PRO B 1 70  ? -135.275 45.353 21.435  1.00 73.69  ?  70  PRO B CG  1 
ATOM 3824 C CD  . PRO B 1 70  ? -136.249 45.708 22.520  1.00 85.09  ?  70  PRO B CD  1 
ATOM 3825 N N   . ILE B 1 71  ? -137.220 48.949 20.662  1.00 75.47  ?  71  ILE B N   1 
ATOM 3826 C CA  . ILE B 1 71  ? -137.863 50.133 20.106  1.00 85.36  ?  71  ILE B CA  1 
ATOM 3827 C C   . ILE B 1 71  ? -137.846 51.267 21.123  1.00 78.26  ?  71  ILE B C   1 
ATOM 3828 O O   . ILE B 1 71  ? -137.645 52.434 20.768  1.00 83.47  ?  71  ILE B O   1 
ATOM 3829 C CB  . ILE B 1 71  ? -139.294 49.801 19.641  1.00 80.40  ?  71  ILE B CB  1 
ATOM 3830 C CG1 . ILE B 1 71  ? -139.266 48.805 18.477  1.00 67.60  ?  71  ILE B CG1 1 
ATOM 3831 C CG2 . ILE B 1 71  ? -140.044 51.064 19.245  1.00 68.43  ?  71  ILE B CG2 1 
ATOM 3832 C CD1 . ILE B 1 71  ? -139.039 49.426 17.112  1.00 72.32  ?  71  ILE B CD1 1 
ATOM 3833 N N   . ARG B 1 72  ? -138.042 50.945 22.404  1.00 83.75  ?  72  ARG B N   1 
ATOM 3834 C CA  . ARG B 1 72  ? -138.068 51.992 23.422  1.00 87.49  ?  72  ARG B CA  1 
ATOM 3835 C C   . ARG B 1 72  ? -136.700 52.640 23.585  1.00 82.93  ?  72  ARG B C   1 
ATOM 3836 O O   . ARG B 1 72  ? -136.601 53.867 23.705  1.00 82.69  ?  72  ARG B O   1 
ATOM 3837 C CB  . ARG B 1 72  ? -138.552 51.427 24.756  1.00 78.47  ?  72  ARG B CB  1 
ATOM 3838 C CG  . ARG B 1 72  ? -140.043 51.148 24.809  1.00 85.13  ?  72  ARG B CG  1 
ATOM 3839 C CD  . ARG B 1 72  ? -140.507 50.972 26.245  1.00 93.67  ?  72  ARG B CD  1 
ATOM 3840 N NE  . ARG B 1 72  ? -139.818 49.879 26.924  1.00 93.81  ?  72  ARG B NE  1 
ATOM 3841 C CZ  . ARG B 1 72  ? -140.182 48.603 26.849  1.00 88.47  ?  72  ARG B CZ  1 
ATOM 3842 N NH1 . ARG B 1 72  ? -141.235 48.256 26.126  1.00 93.80  ?  72  ARG B NH1 1 
ATOM 3843 N NH2 . ARG B 1 72  ? -139.495 47.674 27.500  1.00 85.70  ?  72  ARG B NH2 1 
ATOM 3844 N N   . LEU B 1 73  ? -135.635 51.834 23.594  1.00 83.68  ?  73  LEU B N   1 
ATOM 3845 C CA  . LEU B 1 73  ? -134.290 52.392 23.684  1.00 87.15  ?  73  LEU B CA  1 
ATOM 3846 C C   . LEU B 1 73  ? -133.983 53.289 22.493  1.00 93.36  ?  73  LEU B C   1 
ATOM 3847 O O   . LEU B 1 73  ? -133.164 54.209 22.601  1.00 103.31 ?  73  LEU B O   1 
ATOM 3848 C CB  . LEU B 1 73  ? -133.257 51.268 23.787  1.00 75.00  ?  73  LEU B CB  1 
ATOM 3849 C CG  . LEU B 1 73  ? -133.177 50.528 25.126  1.00 97.43  ?  73  LEU B CG  1 
ATOM 3850 C CD1 . LEU B 1 73  ? -132.225 49.342 25.040  1.00 101.98 ?  73  LEU B CD1 1 
ATOM 3851 C CD2 . LEU B 1 73  ? -132.765 51.470 26.246  1.00 91.98  ?  73  LEU B CD2 1 
ATOM 3852 N N   . MET B 1 74  ? -134.629 53.039 21.352  1.00 91.61  ?  74  MET B N   1 
ATOM 3853 C CA  . MET B 1 74  ? -134.476 53.933 20.210  1.00 87.53  ?  74  MET B CA  1 
ATOM 3854 C C   . MET B 1 74  ? -135.188 55.257 20.457  1.00 93.64  ?  74  MET B C   1 
ATOM 3855 O O   . MET B 1 74  ? -134.693 56.319 20.060  1.00 105.06 ?  74  MET B O   1 
ATOM 3856 C CB  . MET B 1 74  ? -135.009 53.261 18.944  1.00 88.15  ?  74  MET B CB  1 
ATOM 3857 C CG  . MET B 1 74  ? -134.180 52.078 18.466  1.00 93.88  ?  74  MET B CG  1 
ATOM 3858 S SD  . MET B 1 74  ? -134.885 51.302 16.998  1.00 92.82  ?  74  MET B SD  1 
ATOM 3859 C CE  . MET B 1 74  ? -133.988 49.752 16.964  1.00 69.67  ?  74  MET B CE  1 
ATOM 3860 N N   . LEU B 1 75  ? -136.347 55.215 21.121  1.00 90.58  ?  75  LEU B N   1 
ATOM 3861 C CA  . LEU B 1 75  ? -137.082 56.442 21.409  1.00 92.84  ?  75  LEU B CA  1 
ATOM 3862 C C   . LEU B 1 75  ? -136.329 57.316 22.405  1.00 91.37  ?  75  LEU B C   1 
ATOM 3863 O O   . LEU B 1 75  ? -136.352 58.548 22.298  1.00 83.10  ?  75  LEU B O   1 
ATOM 3864 C CB  . LEU B 1 75  ? -138.480 56.105 21.928  1.00 83.43  ?  75  LEU B CB  1 
ATOM 3865 C CG  . LEU B 1 75  ? -139.589 57.108 21.597  1.00 73.88  ?  75  LEU B CG  1 
ATOM 3866 C CD1 . LEU B 1 75  ? -139.342 57.764 20.248  1.00 84.00  ?  75  LEU B CD1 1 
ATOM 3867 C CD2 . LEU B 1 75  ? -140.950 56.435 21.624  1.00 73.93  ?  75  LEU B CD2 1 
ATOM 3868 N N   . SER B 1 76  ? -135.665 56.699 23.386  1.00 93.01  ?  76  SER B N   1 
ATOM 3869 C CA  . SER B 1 76  ? -134.792 57.460 24.275  1.00 102.89 ?  76  SER B CA  1 
ATOM 3870 C C   . SER B 1 76  ? -133.668 58.123 23.491  1.00 105.19 ?  76  SER B C   1 
ATOM 3871 O O   . SER B 1 76  ? -133.332 59.289 23.731  1.00 124.15 ?  76  SER B O   1 
ATOM 3872 C CB  . SER B 1 76  ? -134.216 56.550 25.361  1.00 97.55  ?  76  SER B CB  1 
ATOM 3873 O OG  . SER B 1 76  ? -135.193 56.225 26.337  1.00 104.09 ?  76  SER B OG  1 
ATOM 3874 N N   . HIS B 1 77  ? -133.075 57.390 22.546  1.00 107.11 ?  77  HIS B N   1 
ATOM 3875 C CA  . HIS B 1 77  ? -132.070 57.953 21.655  1.00 110.38 ?  77  HIS B CA  1 
ATOM 3876 C C   . HIS B 1 77  ? -132.656 58.970 20.685  1.00 108.57 ?  77  HIS B C   1 
ATOM 3877 O O   . HIS B 1 77  ? -131.893 59.691 20.034  1.00 119.10 ?  77  HIS B O   1 
ATOM 3878 C CB  . HIS B 1 77  ? -131.377 56.827 20.885  1.00 106.82 ?  77  HIS B CB  1 
ATOM 3879 C CG  . HIS B 1 77  ? -130.105 57.242 20.214  1.00 118.18 ?  77  HIS B CG  1 
ATOM 3880 N ND1 . HIS B 1 77  ? -130.082 57.899 19.003  1.00 125.16 ?  77  HIS B ND1 1 
ATOM 3881 C CD2 . HIS B 1 77  ? -128.811 57.088 20.582  1.00 133.26 ?  77  HIS B CD2 1 
ATOM 3882 C CE1 . HIS B 1 77  ? -128.830 58.134 18.654  1.00 132.06 ?  77  HIS B CE1 1 
ATOM 3883 N NE2 . HIS B 1 77  ? -128.038 57.652 19.595  1.00 133.52 ?  77  HIS B NE2 1 
ATOM 3884 N N   . PHE B 1 78  ? -133.983 59.044 20.573  1.00 101.23 ?  78  PHE B N   1 
ATOM 3885 C CA  . PHE B 1 78  ? -134.653 60.011 19.714  1.00 103.66 ?  78  PHE B CA  1 
ATOM 3886 C C   . PHE B 1 78  ? -135.238 61.187 20.482  1.00 110.22 ?  78  PHE B C   1 
ATOM 3887 O O   . PHE B 1 78  ? -135.396 62.269 19.907  1.00 110.69 ?  78  PHE B O   1 
ATOM 3888 C CB  . PHE B 1 78  ? -135.765 59.321 18.911  1.00 101.01 ?  78  PHE B CB  1 
ATOM 3889 C CG  . PHE B 1 78  ? -136.627 60.268 18.115  1.00 109.64 ?  78  PHE B CG  1 
ATOM 3890 C CD1 . PHE B 1 78  ? -137.839 60.716 18.619  1.00 106.71 ?  78  PHE B CD1 1 
ATOM 3891 C CD2 . PHE B 1 78  ? -136.223 60.711 16.866  1.00 109.53 ?  78  PHE B CD2 1 
ATOM 3892 C CE1 . PHE B 1 78  ? -138.632 61.587 17.891  1.00 101.59 ?  78  PHE B CE1 1 
ATOM 3893 C CE2 . PHE B 1 78  ? -137.012 61.582 16.134  1.00 111.21 ?  78  PHE B CE2 1 
ATOM 3894 C CZ  . PHE B 1 78  ? -138.218 62.020 16.647  1.00 97.04  ?  78  PHE B CZ  1 
ATOM 3895 N N   . LYS B 1 79  ? -135.563 60.997 21.763  1.00 112.11 ?  79  LYS B N   1 
ATOM 3896 C CA  . LYS B 1 79  ? -136.142 62.071 22.565  1.00 117.78 ?  79  LYS B CA  1 
ATOM 3897 C C   . LYS B 1 79  ? -135.241 63.301 22.581  1.00 127.54 ?  79  LYS B C   1 
ATOM 3898 O O   . LYS B 1 79  ? -135.674 64.411 22.247  1.00 138.06 ?  79  LYS B O   1 
ATOM 3899 C CB  . LYS B 1 79  ? -136.403 61.573 23.988  1.00 129.26 ?  79  LYS B CB  1 
ATOM 3900 C CG  . LYS B 1 79  ? -136.867 62.653 24.950  1.00 142.60 ?  79  LYS B CG  1 
ATOM 3901 C CD  . LYS B 1 79  ? -136.719 62.200 26.394  1.00 141.58 ?  79  LYS B CD  1 
ATOM 3902 C CE  . LYS B 1 79  ? -137.085 63.313 27.365  1.00 143.16 ?  79  LYS B CE  1 
ATOM 3903 N NZ  . LYS B 1 79  ? -136.765 62.952 28.774  1.00 145.47 ?  79  LYS B NZ  1 
ATOM 3904 N N   . ASP B 1 80  ? -133.978 63.122 22.968  1.00 127.57 ?  80  ASP B N   1 
ATOM 3905 C CA  . ASP B 1 80  ? -133.063 64.256 23.056  1.00 144.16 ?  80  ASP B CA  1 
ATOM 3906 C C   . ASP B 1 80  ? -132.403 64.569 21.719  1.00 142.90 ?  80  ASP B C   1 
ATOM 3907 O O   . ASP B 1 80  ? -132.051 65.726 21.464  1.00 146.18 ?  80  ASP B O   1 
ATOM 3908 C CB  . ASP B 1 80  ? -132.002 63.986 24.121  1.00 148.83 ?  80  ASP B CB  1 
ATOM 3909 C CG  . ASP B 1 80  ? -131.440 62.587 24.032  1.00 143.00 ?  80  ASP B CG  1 
ATOM 3910 O OD1 . ASP B 1 80  ? -131.924 61.806 23.183  1.00 139.86 ?  80  ASP B OD1 1 
ATOM 3911 O OD2 . ASP B 1 80  ? -130.531 62.260 24.821  1.00 164.39 -1 80  ASP B OD2 1 
ATOM 3912 N N   . ASN B 1 81  ? -132.239 63.565 20.857  1.00 134.24 ?  81  ASN B N   1 
ATOM 3913 C CA  . ASN B 1 81  ? -131.646 63.739 19.535  1.00 128.83 ?  81  ASN B CA  1 
ATOM 3914 C C   . ASN B 1 81  ? -132.697 63.975 18.457  1.00 129.55 ?  81  ASN B C   1 
ATOM 3915 O O   . ASN B 1 81  ? -132.525 63.536 17.312  1.00 130.55 ?  81  ASN B O   1 
ATOM 3916 C CB  . ASN B 1 81  ? -130.777 62.530 19.185  1.00 120.94 ?  81  ASN B CB  1 
ATOM 3917 C CG  . ASN B 1 81  ? -129.548 62.424 20.067  1.00 125.57 ?  81  ASN B CG  1 
ATOM 3918 O OD1 . ASN B 1 81  ? -128.461 62.866 19.697  1.00 113.56 ?  81  ASN B OD1 1 
ATOM 3919 N ND2 . ASN B 1 81  ? -129.715 61.828 21.242  1.00 139.50 ?  81  ASN B ND2 1 
ATOM 3920 N N   . LYS B 1 82  ? -133.790 64.653 18.813  1.00 125.15 ?  82  LYS B N   1 
ATOM 3921 C CA  . LYS B 1 82  ? -134.922 64.879 17.921  1.00 123.64 ?  82  LYS B CA  1 
ATOM 3922 C C   . LYS B 1 82  ? -134.530 65.538 16.602  1.00 132.19 ?  82  LYS B C   1 
ATOM 3923 O O   . LYS B 1 82  ? -135.296 65.471 15.634  1.00 136.77 ?  82  LYS B O   1 
ATOM 3924 C CB  . LYS B 1 82  ? -135.952 65.734 18.671  1.00 127.39 ?  82  LYS B CB  1 
ATOM 3925 C CG  . LYS B 1 82  ? -137.288 65.943 17.985  1.00 124.38 ?  82  LYS B CG  1 
ATOM 3926 C CD  . LYS B 1 82  ? -138.204 66.762 18.883  1.00 129.20 ?  82  LYS B CD  1 
ATOM 3927 C CE  . LYS B 1 82  ? -139.222 67.553 18.084  1.00 135.95 ?  82  LYS B CE  1 
ATOM 3928 N NZ  . LYS B 1 82  ? -139.921 68.555 18.936  1.00 130.61 ?  82  LYS B NZ  1 
ATOM 3929 N N   . GLU B 1 83  ? -133.351 66.155 16.529  1.00 138.15 ?  83  GLU B N   1 
ATOM 3930 C CA  . GLU B 1 83  ? -132.933 66.904 15.352  1.00 144.07 ?  83  GLU B CA  1 
ATOM 3931 C C   . GLU B 1 83  ? -131.849 66.207 14.540  1.00 141.55 ?  83  GLU B C   1 
ATOM 3932 O O   . GLU B 1 83  ? -131.345 66.796 13.578  1.00 147.79 ?  83  GLU B O   1 
ATOM 3933 C CB  . GLU B 1 83  ? -132.442 68.296 15.768  1.00 157.99 ?  83  GLU B CB  1 
ATOM 3934 C CG  . GLU B 1 83  ? -133.467 69.111 16.537  1.00 164.39 ?  83  GLU B CG  1 
ATOM 3935 C CD  . GLU B 1 83  ? -132.888 69.732 17.794  1.00 180.09 ?  83  GLU B CD  1 
ATOM 3936 O OE1 . GLU B 1 83  ? -131.870 69.211 18.299  1.00 178.76 ?  83  GLU B OE1 1 
ATOM 3937 O OE2 . GLU B 1 83  ? -133.450 70.736 18.279  1.00 191.16 -1 83  GLU B OE2 1 
ATOM 3938 N N   . LYS B 1 84  ? -131.473 64.975 14.895  1.00 136.49 ?  84  LYS B N   1 
ATOM 3939 C CA  . LYS B 1 84  ? -130.387 64.306 14.182  1.00 130.74 ?  84  LYS B CA  1 
ATOM 3940 C C   . LYS B 1 84  ? -130.767 63.959 12.747  1.00 137.57 ?  84  LYS B C   1 
ATOM 3941 O O   . LYS B 1 84  ? -129.888 63.885 11.881  1.00 138.46 ?  84  LYS B O   1 
ATOM 3942 C CB  . LYS B 1 84  ? -129.956 63.048 14.935  1.00 126.80 ?  84  LYS B CB  1 
ATOM 3943 C CG  . LYS B 1 84  ? -129.048 63.323 16.122  1.00 122.81 ?  84  LYS B CG  1 
ATOM 3944 C CD  . LYS B 1 84  ? -127.704 63.880 15.676  1.00 130.19 ?  84  LYS B CD  1 
ATOM 3945 C CE  . LYS B 1 84  ? -126.774 64.085 16.862  1.00 129.16 ?  84  LYS B CE  1 
ATOM 3946 N NZ  . LYS B 1 84  ? -125.421 64.551 16.448  1.00 110.26 ?  84  LYS B NZ  1 
ATOM 3947 N N   . GLY B 1 85  ? -132.053 63.749 12.475  1.00 138.00 ?  85  GLY B N   1 
ATOM 3948 C CA  . GLY B 1 85  ? -132.486 63.430 11.125  1.00 134.42 ?  85  GLY B CA  1 
ATOM 3949 C C   . GLY B 1 85  ? -131.999 62.091 10.619  1.00 136.06 ?  85  GLY B C   1 
ATOM 3950 O O   . GLY B 1 85  ? -131.848 61.911 9.405   1.00 140.80 ?  85  GLY B O   1 
ATOM 3951 N N   . ALA B 1 86  ? -131.745 61.145 11.516  1.00 130.76 ?  86  ALA B N   1 
ATOM 3952 C CA  . ALA B 1 86  ? -131.264 59.823 11.148  1.00 115.56 ?  86  ALA B CA  1 
ATOM 3953 C C   . ALA B 1 86  ? -132.400 58.808 11.201  1.00 122.86 ?  86  ALA B C   1 
ATOM 3954 O O   . ALA B 1 86  ? -133.481 59.068 11.734  1.00 131.76 ?  86  ALA B O   1 
ATOM 3955 C CB  . ALA B 1 86  ? -130.116 59.393 12.067  1.00 118.77 ?  86  ALA B CB  1 
ATOM 3956 N N   . ASN B 1 87  ? -132.137 57.633 10.638  1.00 102.98 ?  87  ASN B N   1 
ATOM 3957 C CA  . ASN B 1 87  ? -133.114 56.560 10.556  1.00 93.68  ?  87  ASN B CA  1 
ATOM 3958 C C   . ASN B 1 87  ? -132.766 55.449 11.539  1.00 88.25  ?  87  ASN B C   1 
ATOM 3959 O O   . ASN B 1 87  ? -131.596 55.225 11.863  1.00 87.74  ?  87  ASN B O   1 
ATOM 3960 C CB  . ASN B 1 87  ? -133.184 55.989 9.136   1.00 91.86  ?  87  ASN B CB  1 
ATOM 3961 C CG  . ASN B 1 87  ? -134.177 56.726 8.261   1.00 96.80  ?  87  ASN B CG  1 
ATOM 3962 O OD1 . ASN B 1 87  ? -135.113 56.129 7.730   1.00 114.16 ?  87  ASN B OD1 1 
ATOM 3963 N ND2 . ASN B 1 87  ? -133.979 58.030 8.108   1.00 103.46 ?  87  ASN B ND2 1 
ATOM 3964 N N   . TYR B 1 88  ? -133.800 54.759 12.011  1.00 93.96  ?  88  TYR B N   1 
ATOM 3965 C CA  . TYR B 1 88  ? -133.656 53.623 12.909  1.00 88.66  ?  88  TYR B CA  1 
ATOM 3966 C C   . TYR B 1 88  ? -134.117 52.357 12.202  1.00 82.42  ?  88  TYR B C   1 
ATOM 3967 O O   . TYR B 1 88  ? -135.151 52.353 11.527  1.00 93.05  ?  88  TYR B O   1 
ATOM 3968 C CB  . TYR B 1 88  ? -134.458 53.833 14.194  1.00 83.21  ?  88  TYR B CB  1 
ATOM 3969 C CG  . TYR B 1 88  ? -133.841 54.848 15.126  1.00 85.40  ?  88  TYR B CG  1 
ATOM 3970 C CD1 . TYR B 1 88  ? -132.759 54.512 15.929  1.00 80.51  ?  88  TYR B CD1 1 
ATOM 3971 C CD2 . TYR B 1 88  ? -134.335 56.144 15.199  1.00 81.08  ?  88  TYR B CD2 1 
ATOM 3972 C CE1 . TYR B 1 88  ? -132.188 55.436 16.781  1.00 84.90  ?  88  TYR B CE1 1 
ATOM 3973 C CE2 . TYR B 1 88  ? -133.770 57.075 16.048  1.00 92.77  ?  88  TYR B CE2 1 
ATOM 3974 C CZ  . TYR B 1 88  ? -132.698 56.716 16.837  1.00 101.45 ?  88  TYR B CZ  1 
ATOM 3975 O OH  . TYR B 1 88  ? -132.132 57.639 17.685  1.00 122.72 ?  88  TYR B OH  1 
ATOM 3976 N N   . TYR B 1 89  ? -133.349 51.284 12.361  1.00 78.50  ?  89  TYR B N   1 
ATOM 3977 C CA  . TYR B 1 89  ? -133.569 50.048 11.627  1.00 85.22  ?  89  TYR B CA  1 
ATOM 3978 C C   . TYR B 1 89  ? -133.806 48.891 12.587  1.00 88.52  ?  89  TYR B C   1 
ATOM 3979 O O   . TYR B 1 89  ? -133.189 48.819 13.655  1.00 99.39  ?  89  TYR B O   1 
ATOM 3980 C CB  . TYR B 1 89  ? -132.378 49.731 10.720  1.00 89.54  ?  89  TYR B CB  1 
ATOM 3981 C CG  . TYR B 1 89  ? -132.104 50.800 9.689   1.00 95.29  ?  89  TYR B CG  1 
ATOM 3982 C CD1 . TYR B 1 89  ? -132.763 50.799 8.468   1.00 86.00  ?  89  TYR B CD1 1 
ATOM 3983 C CD2 . TYR B 1 89  ? -131.189 51.814 9.940   1.00 85.93  ?  89  TYR B CD2 1 
ATOM 3984 C CE1 . TYR B 1 89  ? -132.518 51.774 7.525   1.00 78.59  ?  89  TYR B CE1 1 
ATOM 3985 C CE2 . TYR B 1 89  ? -130.936 52.793 9.003   1.00 88.74  ?  89  TYR B CE2 1 
ATOM 3986 C CZ  . TYR B 1 89  ? -131.604 52.768 7.798   1.00 89.01  ?  89  TYR B CZ  1 
ATOM 3987 O OH  . TYR B 1 89  ? -131.355 53.742 6.862   1.00 103.90 ?  89  TYR B OH  1 
ATOM 3988 N N   . LEU B 1 90  ? -134.702 47.988 12.196  1.00 88.53  ?  90  LEU B N   1 
ATOM 3989 C CA  . LEU B 1 90  ? -134.958 46.768 12.954  1.00 83.88  ?  90  LEU B CA  1 
ATOM 3990 C C   . LEU B 1 90  ? -135.474 45.716 11.988  1.00 84.06  ?  90  LEU B C   1 
ATOM 3991 O O   . LEU B 1 90  ? -136.547 45.885 11.401  1.00 100.18 ?  90  LEU B O   1 
ATOM 3992 C CB  . LEU B 1 90  ? -135.966 47.013 14.080  1.00 88.58  ?  90  LEU B CB  1 
ATOM 3993 C CG  . LEU B 1 90  ? -135.825 46.170 15.353  1.00 93.02  ?  90  LEU B CG  1 
ATOM 3994 C CD1 . LEU B 1 90  ? -136.740 46.709 16.437  1.00 77.47  ?  90  LEU B CD1 1 
ATOM 3995 C CD2 . LEU B 1 90  ? -136.113 44.695 15.103  1.00 94.93  ?  90  LEU B CD2 1 
ATOM 3996 N N   . TYR B 1 91  ? -134.716 44.636 11.826  1.00 90.78  ?  91  TYR B N   1 
ATOM 3997 C CA  . TYR B 1 91  ? -135.079 43.551 10.931  1.00 102.50 ?  91  TYR B CA  1 
ATOM 3998 C C   . TYR B 1 91  ? -135.286 42.278 11.740  1.00 91.79  ?  91  TYR B C   1 
ATOM 3999 O O   . TYR B 1 91  ? -134.705 42.106 12.816  1.00 81.02  ?  91  TYR B O   1 
ATOM 4000 C CB  . TYR B 1 91  ? -134.002 43.329 9.859   1.00 95.86  ?  91  TYR B CB  1 
ATOM 4001 C CG  . TYR B 1 91  ? -133.641 44.572 9.074   1.00 91.14  ?  91  TYR B CG  1 
ATOM 4002 C CD1 . TYR B 1 91  ? -134.314 44.899 7.904   1.00 99.12  ?  91  TYR B CD1 1 
ATOM 4003 C CD2 . TYR B 1 91  ? -132.620 45.414 9.500   1.00 103.43 ?  91  TYR B CD2 1 
ATOM 4004 C CE1 . TYR B 1 91  ? -133.985 46.033 7.185   1.00 107.86 ?  91  TYR B CE1 1 
ATOM 4005 C CE2 . TYR B 1 91  ? -132.285 46.549 8.786   1.00 98.45  ?  91  TYR B CE2 1 
ATOM 4006 C CZ  . TYR B 1 91  ? -132.970 46.853 7.630   1.00 102.90 ?  91  TYR B CZ  1 
ATOM 4007 O OH  . TYR B 1 91  ? -132.640 47.982 6.917   1.00 98.43  ?  91  TYR B OH  1 
ATOM 4008 N N   . GLY B 1 92  ? -136.123 41.385 11.218  1.00 84.43  ?  92  GLY B N   1 
ATOM 4009 C CA  . GLY B 1 92  ? -136.437 40.159 11.925  1.00 79.91  ?  92  GLY B CA  1 
ATOM 4010 C C   . GLY B 1 92  ? -136.629 38.999 10.972  1.00 89.27  ?  92  GLY B C   1 
ATOM 4011 O O   . GLY B 1 92  ? -136.839 39.178 9.768   1.00 84.10  ?  92  GLY B O   1 
ATOM 4012 N N   . HIS B 1 93  ? -136.550 37.794 11.535  1.00 85.82  ?  93  HIS B N   1 
ATOM 4013 C CA  . HIS B 1 93  ? -136.750 36.567 10.766  1.00 87.50  ?  93  HIS B CA  1 
ATOM 4014 C C   . HIS B 1 93  ? -137.263 35.503 11.732  1.00 104.63 ?  93  HIS B C   1 
ATOM 4015 O O   . HIS B 1 93  ? -136.479 34.904 12.474  1.00 108.73 ?  93  HIS B O   1 
ATOM 4016 C CB  . HIS B 1 93  ? -135.463 36.131 10.079  1.00 93.66  ?  93  HIS B CB  1 
ATOM 4017 C CG  . HIS B 1 93  ? -135.607 34.892 9.251   1.00 97.39  ?  93  HIS B CG  1 
ATOM 4018 N ND1 . HIS B 1 93  ? -136.069 34.914 7.953   1.00 109.69 ?  93  HIS B ND1 1 
ATOM 4019 C CD2 . HIS B 1 93  ? -135.345 33.595 9.535   1.00 94.63  ?  93  HIS B CD2 1 
ATOM 4020 C CE1 . HIS B 1 93  ? -136.089 33.683 7.474   1.00 107.26 ?  93  HIS B CE1 1 
ATOM 4021 N NE2 . HIS B 1 93  ? -135.653 32.864 8.414   1.00 112.99 ?  93  HIS B NE2 1 
ATOM 4022 N N   . TYR B 1 94  ? -138.571 35.281 11.717  1.00 102.03 ?  94  TYR B N   1 
ATOM 4023 C CA  . TYR B 1 94  ? -139.236 34.325 12.589  1.00 105.10 ?  94  TYR B CA  1 
ATOM 4024 C C   . TYR B 1 94  ? -139.867 33.220 11.748  1.00 118.57 ?  94  TYR B C   1 
ATOM 4025 O O   . TYR B 1 94  ? -139.744 33.192 10.521  1.00 108.49 ?  94  TYR B O   1 
ATOM 4026 C CB  . TYR B 1 94  ? -140.294 35.020 13.450  1.00 100.56 ?  94  TYR B CB  1 
ATOM 4027 C CG  . TYR B 1 94  ? -139.781 36.223 14.207  1.00 95.72  ?  94  TYR B CG  1 
ATOM 4028 C CD1 . TYR B 1 94  ? -139.178 36.079 15.447  1.00 99.11  ?  94  TYR B CD1 1 
ATOM 4029 C CD2 . TYR B 1 94  ? -139.900 37.502 13.682  1.00 97.42  ?  94  TYR B CD2 1 
ATOM 4030 C CE1 . TYR B 1 94  ? -138.709 37.175 16.144  1.00 115.68 ?  94  TYR B CE1 1 
ATOM 4031 C CE2 . TYR B 1 94  ? -139.432 38.604 14.373  1.00 100.08 ?  94  TYR B CE2 1 
ATOM 4032 C CZ  . TYR B 1 94  ? -138.837 38.434 15.604  1.00 124.02 ?  94  TYR B CZ  1 
ATOM 4033 O OH  . TYR B 1 94  ? -138.368 39.524 16.300  1.00 122.58 ?  94  TYR B OH  1 
ATOM 4034 N N   . LYS B 1 95  ? -140.553 32.300 12.426  1.00 118.63 ?  95  LYS B N   1 
ATOM 4035 C CA  . LYS B 1 95  ? -141.304 31.249 11.752  1.00 112.46 ?  95  LYS B CA  1 
ATOM 4036 C C   . LYS B 1 95  ? -142.783 31.574 11.610  1.00 108.48 ?  95  LYS B C   1 
ATOM 4037 O O   . LYS B 1 95  ? -143.400 31.182 10.614  1.00 120.05 ?  95  LYS B O   1 
ATOM 4038 C CB  . LYS B 1 95  ? -141.153 29.917 12.497  1.00 122.61 ?  95  LYS B CB  1 
ATOM 4039 C CG  . LYS B 1 95  ? -141.647 29.941 13.935  1.00 144.15 ?  95  LYS B CG  1 
ATOM 4040 C CD  . LYS B 1 95  ? -141.934 28.537 14.445  1.00 149.19 ?  95  LYS B CD  1 
ATOM 4041 C CE  . LYS B 1 95  ? -142.556 28.570 15.833  1.00 158.58 ?  95  LYS B CE  1 
ATOM 4042 N NZ  . LYS B 1 95  ? -142.918 27.209 16.319  1.00 157.59 ?  95  LYS B NZ  1 
ATOM 4043 N N   . SER B 1 96  ? -143.360 32.281 12.577  1.00 112.66 ?  96  SER B N   1 
ATOM 4044 C CA  . SER B 1 96  ? -144.766 32.659 12.538  1.00 119.36 ?  96  SER B CA  1 
ATOM 4045 C C   . SER B 1 96  ? -144.946 33.891 13.414  1.00 107.58 ?  96  SER B C   1 
ATOM 4046 O O   . SER B 1 96  ? -143.995 34.385 14.027  1.00 111.33 ?  96  SER B O   1 
ATOM 4047 C CB  . SER B 1 96  ? -145.667 31.508 12.993  1.00 122.95 ?  96  SER B CB  1 
ATOM 4048 O OG  . SER B 1 96  ? -145.443 31.192 14.357  1.00 110.68 ?  96  SER B OG  1 
ATOM 4049 N N   . GLY B 1 97  ? -146.176 34.396 13.459  1.00 100.97 ?  97  GLY B N   1 
ATOM 4050 C CA  . GLY B 1 97  ? -146.500 35.544 14.274  1.00 95.74  ?  97  GLY B CA  1 
ATOM 4051 C C   . GLY B 1 97  ? -146.273 36.886 13.614  1.00 90.29  ?  97  GLY B C   1 
ATOM 4052 O O   . GLY B 1 97  ? -146.593 37.916 14.220  1.00 90.88  ?  97  GLY B O   1 
ATOM 4053 N N   . GLN B 1 98  ? -145.727 36.913 12.396  1.00 80.66  ?  98  GLN B N   1 
ATOM 4054 C CA  . GLN B 1 98  ? -145.520 38.188 11.717  1.00 85.93  ?  98  GLN B CA  1 
ATOM 4055 C C   . GLN B 1 98  ? -146.844 38.849 11.360  1.00 94.34  ?  98  GLN B C   1 
ATOM 4056 O O   . GLN B 1 98  ? -146.905 40.075 11.208  1.00 93.39  ?  98  GLN B O   1 
ATOM 4057 C CB  . GLN B 1 98  ? -144.673 37.999 10.459  1.00 93.39  ?  98  GLN B CB  1 
ATOM 4058 C CG  . GLN B 1 98  ? -143.459 37.094 10.625  1.00 93.55  ?  98  GLN B CG  1 
ATOM 4059 C CD  . GLN B 1 98  ? -143.797 35.630 10.437  1.00 92.69  ?  98  GLN B CD  1 
ATOM 4060 O OE1 . GLN B 1 98  ? -144.931 35.213 10.661  1.00 104.04 ?  98  GLN B OE1 1 
ATOM 4061 N NE2 . GLN B 1 98  ? -142.812 34.841 10.018  1.00 96.85  ?  98  GLN B NE2 1 
ATOM 4062 N N   . GLU B 1 99  ? -147.905 38.054 11.209  1.00 108.09 ?  99  GLU B N   1 
ATOM 4063 C CA  . GLU B 1 99  ? -149.228 38.595 10.922  1.00 98.91  ?  99  GLU B CA  1 
ATOM 4064 C C   . GLU B 1 99  ? -149.743 39.487 12.043  1.00 93.65  ?  99  GLU B C   1 
ATOM 4065 O O   . GLU B 1 99  ? -150.636 40.307 11.805  1.00 95.98  ?  99  GLU B O   1 
ATOM 4066 C CB  . GLU B 1 99  ? -150.220 37.456 10.670  1.00 85.76  ?  99  GLU B CB  1 
ATOM 4067 C CG  . GLU B 1 99  ? -150.312 36.435 11.802  1.00 101.37 ?  99  GLU B CG  1 
ATOM 4068 C CD  . GLU B 1 99  ? -149.186 35.418 11.774  1.00 110.20 ?  99  GLU B CD  1 
ATOM 4069 O OE1 . GLU B 1 99  ? -149.470 34.206 11.895  1.00 107.26 ?  99  GLU B OE1 1 
ATOM 4070 O OE2 . GLU B 1 99  ? -148.018 35.828 11.622  1.00 109.72 -1 99  GLU B OE2 1 
ATOM 4071 N N   . LYS B 1 100 ? -149.203 39.345 13.257  1.00 87.40  ?  100 LYS B N   1 
ATOM 4072 C CA  . LYS B 1 100 ? -149.662 40.158 14.379  1.00 73.78  ?  100 LYS B CA  1 
ATOM 4073 C C   . LYS B 1 100 ? -149.344 41.635 14.176  1.00 80.30  ?  100 LYS B C   1 
ATOM 4074 O O   . LYS B 1 100 ? -150.071 42.497 14.682  1.00 86.74  ?  100 LYS B O   1 
ATOM 4075 C CB  . LYS B 1 100 ? -149.037 39.655 15.680  1.00 73.29  ?  100 LYS B CB  1 
ATOM 4076 C CG  . LYS B 1 100 ? -149.306 38.186 15.972  1.00 78.37  ?  100 LYS B CG  1 
ATOM 4077 C CD  . LYS B 1 100 ? -148.472 37.710 17.149  1.00 92.58  ?  100 LYS B CD  1 
ATOM 4078 C CE  . LYS B 1 100 ? -148.600 36.212 17.365  1.00 104.02 ?  100 LYS B CE  1 
ATOM 4079 N NZ  . LYS B 1 100 ? -147.718 35.745 18.472  1.00 110.75 ?  100 LYS B NZ  1 
ATOM 4080 N N   . LEU B 1 101 ? -148.272 41.945 13.450  1.00 92.20  ?  101 LEU B N   1 
ATOM 4081 C CA  . LEU B 1 101 ? -147.928 43.331 13.174  1.00 95.61  ?  101 LEU B CA  1 
ATOM 4082 C C   . LEU B 1 101 ? -148.977 43.977 12.272  1.00 91.37  ?  101 LEU B C   1 
ATOM 4083 O O   . LEU B 1 101 ? -149.764 43.302 11.601  1.00 120.51 ?  101 LEU B O   1 
ATOM 4084 C CB  . LEU B 1 101 ? -146.545 43.422 12.527  1.00 93.16  ?  101 LEU B CB  1 
ATOM 4085 C CG  . LEU B 1 101 ? -145.828 44.775 12.583  1.00 104.69 ?  101 LEU B CG  1 
ATOM 4086 C CD1 . LEU B 1 101 ? -145.751 45.303 14.004  1.00 66.31  ?  101 LEU B CD1 1 
ATOM 4087 C CD2 . LEU B 1 101 ? -144.439 44.669 11.971  1.00 91.35  ?  101 LEU B CD2 1 
ATOM 4088 N N   . THR B 1 102 ? -148.978 45.309 12.260  1.00 80.18  ?  102 THR B N   1 
ATOM 4089 C CA  . THR B 1 102 ? -149.944 46.097 11.494  1.00 94.52  ?  102 THR B CA  1 
ATOM 4090 C C   . THR B 1 102 ? -149.179 47.165 10.717  1.00 94.88  ?  102 THR B C   1 
ATOM 4091 O O   . THR B 1 102 ? -148.902 48.248 11.239  1.00 92.36  ?  102 THR B O   1 
ATOM 4092 C CB  . THR B 1 102 ? -150.998 46.712 12.409  1.00 106.10 ?  102 THR B CB  1 
ATOM 4093 O OG1 . THR B 1 102 ? -151.634 45.676 13.168  1.00 99.32  ?  102 THR B OG1 1 
ATOM 4094 C CG2 . THR B 1 102 ? -152.047 47.449 11.592  1.00 112.91 ?  102 THR B CG2 1 
ATOM 4095 N N   . LEU B 1 103 ? -148.833 46.854 9.468   1.00 96.39  ?  103 LEU B N   1 
ATOM 4096 C CA  . LEU B 1 103 ? -148.212 47.858 8.614   1.00 100.04 ?  103 LEU B CA  1 
ATOM 4097 C C   . LEU B 1 103 ? -149.252 48.465 7.687   1.00 113.29 ?  103 LEU B C   1 
ATOM 4098 O O   . LEU B 1 103 ? -150.044 47.721 7.090   1.00 129.60 ?  103 LEU B O   1 
ATOM 4099 C CB  . LEU B 1 103 ? -147.078 47.251 7.794   1.00 114.93 ?  103 LEU B CB  1 
ATOM 4100 C CG  . LEU B 1 103 ? -145.723 47.196 8.499   1.00 128.10 ?  103 LEU B CG  1 
ATOM 4101 C CD1 . LEU B 1 103 ? -144.716 46.425 7.663   1.00 121.25 ?  103 LEU B CD1 1 
ATOM 4102 C CD2 . LEU B 1 103 ? -145.220 48.601 8.795   1.00 131.86 ?  103 LEU B CD2 1 
ATOM 4103 N N   . PRO B 1 104 ? -149.290 49.798 7.525   1.00 110.18 ?  104 PRO B N   1 
ATOM 4104 C CA  . PRO B 1 104 ? -148.369 50.770 8.125   1.00 110.33 ?  104 PRO B CA  1 
ATOM 4105 C C   . PRO B 1 104 ? -148.580 50.957 9.626   1.00 108.73 ?  104 PRO B C   1 
ATOM 4106 O O   . PRO B 1 104 ? -149.719 51.008 10.092  1.00 100.75 ?  104 PRO B O   1 
ATOM 4107 C CB  . PRO B 1 104 ? -148.691 52.061 7.369   1.00 113.09 ?  104 PRO B CB  1 
ATOM 4108 C CG  . PRO B 1 104 ? -150.126 51.920 7.009   1.00 124.77 ?  104 PRO B CG  1 
ATOM 4109 C CD  . PRO B 1 104 ? -150.333 50.458 6.719   1.00 116.97 ?  104 PRO B CD  1 
ATOM 4110 N N   . LEU B 1 105 ? -147.479 51.044 10.368  1.00 105.04 ?  105 LEU B N   1 
ATOM 4111 C CA  . LEU B 1 105 ? -147.549 51.163 11.818  1.00 84.75  ?  105 LEU B CA  1 
ATOM 4112 C C   . LEU B 1 105 ? -148.188 52.490 12.204  1.00 88.94  ?  105 LEU B C   1 
ATOM 4113 O O   . LEU B 1 105 ? -147.637 53.560 11.923  1.00 86.55  ?  105 LEU B O   1 
ATOM 4114 C CB  . LEU B 1 105 ? -146.157 51.043 12.427  1.00 72.48  ?  105 LEU B CB  1 
ATOM 4115 C CG  . LEU B 1 105 ? -145.951 49.873 13.388  1.00 93.82  ?  105 LEU B CG  1 
ATOM 4116 C CD1 . LEU B 1 105 ? -144.659 50.054 14.159  1.00 91.55  ?  105 LEU B CD1 1 
ATOM 4117 C CD2 . LEU B 1 105 ? -147.132 49.732 14.339  1.00 108.92 ?  105 LEU B CD2 1 
ATOM 4118 N N   . LYS B 1 106 ? -149.345 52.420 12.850  1.00 76.26  ?  106 LYS B N   1 
ATOM 4119 C CA  . LYS B 1 106 ? -150.059 53.604 13.296  1.00 75.85  ?  106 LYS B CA  1 
ATOM 4120 C C   . LYS B 1 106 ? -149.746 53.893 14.761  1.00 89.23  ?  106 LYS B C   1 
ATOM 4121 O O   . LYS B 1 106 ? -149.142 53.086 15.471  1.00 84.09  ?  106 LYS B O   1 
ATOM 4122 C CB  . LYS B 1 106 ? -151.566 53.432 13.085  1.00 99.65  ?  106 LYS B CB  1 
ATOM 4123 C CG  . LYS B 1 106 ? -152.063 54.001 11.766  1.00 100.61 ?  106 LYS B CG  1 
ATOM 4124 C CD  . LYS B 1 106 ? -153.527 54.396 11.847  1.00 116.52 ?  106 LYS B CD  1 
ATOM 4125 C CE  . LYS B 1 106 ? -153.878 55.413 10.773  1.00 111.53 ?  106 LYS B CE  1 
ATOM 4126 N NZ  . LYS B 1 106 ? -155.223 56.012 10.993  1.00 109.92 ?  106 LYS B NZ  1 
ATOM 4127 N N   . VAL B 1 107 ? -150.175 55.074 15.207  1.00 97.18  ?  107 VAL B N   1 
ATOM 4128 C CA  . VAL B 1 107 ? -149.839 55.537 16.549  1.00 86.08  ?  107 VAL B CA  1 
ATOM 4129 C C   . VAL B 1 107 ? -150.561 54.709 17.607  1.00 91.78  ?  107 VAL B C   1 
ATOM 4130 O O   . VAL B 1 107 ? -149.980 54.360 18.642  1.00 73.02  ?  107 VAL B O   1 
ATOM 4131 C CB  . VAL B 1 107 ? -150.154 57.038 16.677  1.00 91.29  ?  107 VAL B CB  1 
ATOM 4132 C CG1 . VAL B 1 107 ? -150.154 57.468 18.132  1.00 89.70  ?  107 VAL B CG1 1 
ATOM 4133 C CG2 . VAL B 1 107 ? -149.151 57.855 15.874  1.00 95.93  ?  107 VAL B CG2 1 
ATOM 4134 N N   . ASP B 1 108 ? -151.833 54.378 17.367  1.00 109.51 ?  108 ASP B N   1 
ATOM 4135 C CA  . ASP B 1 108 ? -152.600 53.604 18.340  1.00 98.41  ?  108 ASP B CA  1 
ATOM 4136 C C   . ASP B 1 108 ? -151.949 52.252 18.606  1.00 91.68  ?  108 ASP B C   1 
ATOM 4137 O O   . ASP B 1 108 ? -151.797 51.838 19.761  1.00 97.25  ?  108 ASP B O   1 
ATOM 4138 C CB  . ASP B 1 108 ? -154.038 53.420 17.853  1.00 92.59  ?  108 ASP B CB  1 
ATOM 4139 C CG  . ASP B 1 108 ? -154.881 54.664 18.042  1.00 119.38 ?  108 ASP B CG  1 
ATOM 4140 O OD1 . ASP B 1 108 ? -154.686 55.635 17.283  1.00 149.05 ?  108 ASP B OD1 1 
ATOM 4141 O OD2 . ASP B 1 108 ? -155.738 54.672 18.951  1.00 125.42 -1 108 ASP B OD2 1 
ATOM 4142 N N   . PHE B 1 109 ? -151.558 51.546 17.542  1.00 89.44  ?  109 PHE B N   1 
ATOM 4143 C CA  . PHE B 1 109 ? -150.883 50.265 17.718  1.00 86.75  ?  109 PHE B CA  1 
ATOM 4144 C C   . PHE B 1 109 ? -149.512 50.438 18.355  1.00 93.45  ?  109 PHE B C   1 
ATOM 4145 O O   . PHE B 1 109 ? -149.012 49.516 19.009  1.00 101.54 ?  109 PHE B O   1 
ATOM 4146 C CB  . PHE B 1 109 ? -150.761 49.545 16.375  1.00 88.93  ?  109 PHE B CB  1 
ATOM 4147 C CG  . PHE B 1 109 ? -150.606 48.056 16.497  1.00 87.95  ?  109 PHE B CG  1 
ATOM 4148 C CD1 . PHE B 1 109 ? -149.368 47.457 16.329  1.00 98.05  ?  109 PHE B CD1 1 
ATOM 4149 C CD2 . PHE B 1 109 ? -151.699 47.256 16.784  1.00 97.16  ?  109 PHE B CD2 1 
ATOM 4150 C CE1 . PHE B 1 109 ? -149.225 46.086 16.442  1.00 104.16 ?  109 PHE B CE1 1 
ATOM 4151 C CE2 . PHE B 1 109 ? -151.562 45.885 16.898  1.00 101.38 ?  109 PHE B CE2 1 
ATOM 4152 C CZ  . PHE B 1 109 ? -150.324 45.300 16.727  1.00 100.91 ?  109 PHE B CZ  1 
ATOM 4153 N N   . PHE B 1 110 ? -148.891 51.606 18.179  1.00 95.63  ?  110 PHE B N   1 
ATOM 4154 C CA  . PHE B 1 110 ? -147.596 51.854 18.803  1.00 85.41  ?  110 PHE B CA  1 
ATOM 4155 C C   . PHE B 1 110 ? -147.728 51.968 20.317  1.00 82.57  ?  110 PHE B C   1 
ATOM 4156 O O   . PHE B 1 110 ? -146.909 51.413 21.059  1.00 88.04  ?  110 PHE B O   1 
ATOM 4157 C CB  . PHE B 1 110 ? -146.970 53.122 18.221  1.00 81.46  ?  110 PHE B CB  1 
ATOM 4158 C CG  . PHE B 1 110 ? -145.520 53.306 18.575  1.00 82.78  ?  110 PHE B CG  1 
ATOM 4159 C CD1 . PHE B 1 110 ? -144.940 54.564 18.534  1.00 81.16  ?  110 PHE B CD1 1 
ATOM 4160 C CD2 . PHE B 1 110 ? -144.732 52.223 18.933  1.00 83.42  ?  110 PHE B CD2 1 
ATOM 4161 C CE1 . PHE B 1 110 ? -143.607 54.740 18.853  1.00 67.79  ?  110 PHE B CE1 1 
ATOM 4162 C CE2 . PHE B 1 110 ? -143.399 52.393 19.254  1.00 79.17  ?  110 PHE B CE2 1 
ATOM 4163 C CZ  . PHE B 1 110 ? -142.836 53.653 19.213  1.00 72.87  ?  110 PHE B CZ  1 
ATOM 4164 N N   . LYS B 1 111 ? -148.749 52.681 20.793  1.00 97.66  ?  111 LYS B N   1 
ATOM 4165 C CA  . LYS B 1 111 ? -148.912 52.898 22.225  1.00 80.32  ?  111 LYS B CA  1 
ATOM 4166 C C   . LYS B 1 111 ? -149.143 51.595 22.981  1.00 81.69  ?  111 LYS B C   1 
ATOM 4167 O O   . LYS B 1 111 ? -148.302 51.188 23.788  1.00 88.00  ?  111 LYS B O   1 
ATOM 4168 C CB  . LYS B 1 111 ? -150.068 53.865 22.491  1.00 87.77  ?  111 LYS B CB  1 
ATOM 4169 C CG  . LYS B 1 111 ? -149.825 55.287 22.017  1.00 78.44  ?  111 LYS B CG  1 
ATOM 4170 C CD  . LYS B 1 111 ? -151.109 56.096 22.070  1.00 68.85  ?  111 LYS B CD  1 
ATOM 4171 C CE  . LYS B 1 111 ? -150.877 57.538 21.661  1.00 83.84  ?  111 LYS B CE  1 
ATOM 4172 N NZ  . LYS B 1 111 ? -152.160 58.228 21.357  1.00 110.58 ?  111 LYS B NZ  1 
ATOM 4173 N N   . SER B 1 112 ? -150.268 50.932 22.733  1.00 79.21  ?  112 SER B N   1 
ATOM 4174 C CA  . SER B 1 112 ? -150.621 49.750 23.521  1.00 88.76  ?  112 SER B CA  1 
ATOM 4175 C C   . SER B 1 112 ? -150.150 48.451 22.873  1.00 89.85  ?  112 SER B C   1 
ATOM 4176 O O   . SER B 1 112 ? -150.903 47.484 22.769  1.00 107.76 ?  112 SER B O   1 
ATOM 4177 C CB  . SER B 1 112 ? -152.127 49.724 23.751  1.00 98.89  ?  112 SER B CB  1 
ATOM 4178 O OG  . SER B 1 112 ? -152.828 49.906 22.533  1.00 80.09  ?  112 SER B OG  1 
ATOM 4179 N N   . ASN B 1 113 ? -148.903 48.416 22.433  1.00 77.46  ?  113 ASN B N   1 
ATOM 4180 C CA  . ASN B 1 113 ? -148.217 47.165 22.123  1.00 88.53  ?  113 ASN B CA  1 
ATOM 4181 C C   . ASN B 1 113 ? -146.806 47.119 22.687  1.00 91.99  ?  113 ASN B C   1 
ATOM 4182 O O   . ASN B 1 113 ? -146.355 46.057 23.126  1.00 86.59  ?  113 ASN B O   1 
ATOM 4183 C CB  . ASN B 1 113 ? -148.191 46.927 20.610  1.00 103.20 ?  113 ASN B CB  1 
ATOM 4184 C CG  . ASN B 1 113 ? -149.563 46.611 20.053  1.00 95.80  ?  113 ASN B CG  1 
ATOM 4185 O OD1 . ASN B 1 113 ? -149.938 45.448 19.917  1.00 106.13 ?  113 ASN B OD1 1 
ATOM 4186 N ND2 . ASN B 1 113 ? -150.326 47.651 19.736  1.00 92.61  ?  113 ASN B ND2 1 
ATOM 4187 N N   . PHE B 1 114 ? -146.100 48.245 22.681  1.00 93.10  ?  114 PHE B N   1 
ATOM 4188 C CA  . PHE B 1 114 ? -144.740 48.352 23.189  1.00 99.73  ?  114 PHE B CA  1 
ATOM 4189 C C   . PHE B 1 114 ? -144.601 49.402 24.277  1.00 96.18  ?  114 PHE B C   1 
ATOM 4190 O O   . PHE B 1 114 ? -143.877 49.184 25.251  1.00 108.35 ?  114 PHE B O   1 
ATOM 4191 C CB  . PHE B 1 114 ? -143.766 48.689 22.048  1.00 107.54 ?  114 PHE B CB  1 
ATOM 4192 C CG  . PHE B 1 114 ? -144.095 48.017 20.745  1.00 107.00 ?  114 PHE B CG  1 
ATOM 4193 C CD1 . PHE B 1 114 ? -143.671 46.723 20.489  1.00 107.76 ?  114 PHE B CD1 1 
ATOM 4194 C CD2 . PHE B 1 114 ? -144.807 48.690 19.766  1.00 101.48 ?  114 PHE B CD2 1 
ATOM 4195 C CE1 . PHE B 1 114 ? -143.968 46.108 19.287  1.00 105.13 ?  114 PHE B CE1 1 
ATOM 4196 C CE2 . PHE B 1 114 ? -145.105 48.081 18.563  1.00 102.19 ?  114 PHE B CE2 1 
ATOM 4197 C CZ  . PHE B 1 114 ? -144.685 46.788 18.323  1.00 109.01 ?  114 PHE B CZ  1 
ATOM 4198 N N   . LEU B 1 115 ? -145.277 50.542 24.132  1.00 66.77  ?  115 LEU B N   1 
ATOM 4199 C CA  . LEU B 1 115 ? -145.157 51.615 25.110  1.00 89.35  ?  115 LEU B CA  1 
ATOM 4200 C C   . LEU B 1 115 ? -145.991 51.347 26.356  1.00 91.66  ?  115 LEU B C   1 
ATOM 4201 O O   . LEU B 1 115 ? -145.585 51.725 27.460  1.00 92.81  ?  115 LEU B O   1 
ATOM 4202 C CB  . LEU B 1 115 ? -145.560 52.946 24.473  1.00 96.02  ?  115 LEU B CB  1 
ATOM 4203 C CG  . LEU B 1 115 ? -144.897 53.255 23.129  1.00 76.30  ?  115 LEU B CG  1 
ATOM 4204 C CD1 . LEU B 1 115 ? -145.264 54.653 22.654  1.00 80.01  ?  115 LEU B CD1 1 
ATOM 4205 C CD2 . LEU B 1 115 ? -143.385 53.094 23.221  1.00 64.60  ?  115 LEU B CD2 1 
ATOM 4206 N N   . THR B 1 116 ? -147.149 50.704 26.205  1.00 94.21  ?  116 THR B N   1 
ATOM 4207 C CA  . THR B 1 116 ? -147.972 50.313 27.350  1.00 88.22  ?  116 THR B CA  1 
ATOM 4208 C C   . THR B 1 116 ? -147.493 48.964 27.893  1.00 95.19  ?  116 THR B C   1 
ATOM 4209 O O   . THR B 1 116 ? -148.196 47.954 27.873  1.00 114.75 ?  116 THR B O   1 
ATOM 4210 C CB  . THR B 1 116 ? -149.445 50.273 26.961  1.00 85.16  ?  116 THR B CB  1 
ATOM 4211 O OG1 . THR B 1 116 ? -149.761 51.426 26.170  1.00 91.25  ?  116 THR B OG1 1 
ATOM 4212 C CG2 . THR B 1 116 ? -150.326 50.273 28.205  1.00 93.48  ?  116 THR B CG2 1 
ATOM 4213 N N   . TYR B 1 117 ? -146.257 48.967 28.379  1.00 90.46  ?  117 TYR B N   1 
ATOM 4214 C CA  . TYR B 1 117 ? -145.597 47.763 28.856  1.00 91.22  ?  117 TYR B CA  1 
ATOM 4215 C C   . TYR B 1 117 ? -145.708 47.653 30.373  1.00 90.14  ?  117 TYR B C   1 
ATOM 4216 O O   . TYR B 1 117 ? -146.145 48.577 31.065  1.00 86.55  ?  117 TYR B O   1 
ATOM 4217 C CB  . TYR B 1 117 ? -144.130 47.746 28.415  1.00 96.86  ?  117 TYR B CB  1 
ATOM 4218 C CG  . TYR B 1 117 ? -143.260 48.801 29.067  1.00 90.26  ?  117 TYR B CG  1 
ATOM 4219 C CD1 . TYR B 1 117 ? -143.152 50.074 28.522  1.00 92.11  ?  117 TYR B CD1 1 
ATOM 4220 C CD2 . TYR B 1 117 ? -142.519 48.514 30.207  1.00 77.76  ?  117 TYR B CD2 1 
ATOM 4221 C CE1 . TYR B 1 117 ? -142.354 51.039 29.110  1.00 86.46  ?  117 TYR B CE1 1 
ATOM 4222 C CE2 . TYR B 1 117 ? -141.715 49.471 30.798  1.00 84.40  ?  117 TYR B CE2 1 
ATOM 4223 C CZ  . TYR B 1 117 ? -141.634 50.731 30.244  1.00 77.93  ?  117 TYR B CZ  1 
ATOM 4224 O OH  . TYR B 1 117 ? -140.837 51.688 30.829  1.00 69.07  ?  117 TYR B OH  1 
ATOM 4225 N N   . THR B 1 118 ? -145.298 46.497 30.887  1.00 87.39  ?  118 THR B N   1 
ATOM 4226 C CA  . THR B 1 118 ? -145.368 46.194 32.308  1.00 90.52  ?  118 THR B CA  1 
ATOM 4227 C C   . THR B 1 118 ? -144.001 45.737 32.793  1.00 102.90 ?  118 THR B C   1 
ATOM 4228 O O   . THR B 1 118 ? -143.330 44.944 32.125  1.00 110.83 ?  118 THR B O   1 
ATOM 4229 C CB  . THR B 1 118 ? -146.421 45.114 32.595  1.00 90.51  ?  118 THR B CB  1 
ATOM 4230 O OG1 . THR B 1 118 ? -147.696 45.546 32.101  1.00 105.81 ?  118 THR B OG1 1 
ATOM 4231 C CG2 . THR B 1 118 ? -146.529 44.848 34.089  1.00 84.97  ?  118 THR B CG2 1 
ATOM 4232 N N   . GLU B 1 119 ? -143.593 46.242 33.955  1.00 98.91  ?  119 GLU B N   1 
ATOM 4233 C CA  . GLU B 1 119 ? -142.289 45.920 34.519  1.00 99.29  ?  119 GLU B CA  1 
ATOM 4234 C C   . GLU B 1 119 ? -142.375 45.981 36.036  1.00 107.72 ?  119 GLU B C   1 
ATOM 4235 O O   . GLU B 1 119 ? -142.816 46.992 36.590  1.00 109.95 ?  119 GLU B O   1 
ATOM 4236 C CB  . GLU B 1 119 ? -141.216 46.885 34.003  1.00 104.96 ?  119 GLU B CB  1 
ATOM 4237 C CG  . GLU B 1 119 ? -139.828 46.642 34.569  1.00 113.72 ?  119 GLU B CG  1 
ATOM 4238 C CD  . GLU B 1 119 ? -138.768 47.476 33.878  1.00 136.56 ?  119 GLU B CD  1 
ATOM 4239 O OE1 . GLU B 1 119 ? -138.640 47.367 32.641  1.00 149.15 ?  119 GLU B OE1 1 
ATOM 4240 O OE2 . GLU B 1 119 ? -138.068 48.245 34.570  1.00 152.42 -1 119 GLU B OE2 1 
ATOM 4241 N N   . LYS B 1 120 ? -141.958 44.897 36.694  1.00 108.72 ?  120 LYS B N   1 
ATOM 4242 C CA  . LYS B 1 120 ? -141.977 44.796 38.156  1.00 101.59 ?  120 LYS B CA  1 
ATOM 4243 C C   . LYS B 1 120 ? -143.389 44.987 38.706  1.00 98.09  ?  120 LYS B C   1 
ATOM 4244 O O   . LYS B 1 120 ? -143.594 45.669 39.712  1.00 91.72  ?  120 LYS B O   1 
ATOM 4245 C CB  . LYS B 1 120 ? -141.004 45.790 38.794  1.00 101.81 ?  120 LYS B CB  1 
ATOM 4246 C CG  . LYS B 1 120 ? -139.576 45.667 38.292  1.00 124.35 ?  120 LYS B CG  1 
ATOM 4247 C CD  . LYS B 1 120 ? -138.729 46.847 38.739  1.00 134.00 ?  120 LYS B CD  1 
ATOM 4248 C CE  . LYS B 1 120 ? -137.328 46.770 38.153  1.00 130.53 ?  120 LYS B CE  1 
ATOM 4249 N NZ  . LYS B 1 120 ? -136.510 47.965 38.499  1.00 111.73 ?  120 LYS B NZ  1 
ATOM 4250 N N   . LYS B 1 121 ? -144.368 44.371 38.038  1.00 108.41 ?  121 LYS B N   1 
ATOM 4251 C CA  . LYS B 1 121 ? -145.785 44.483 38.395  1.00 105.59 ?  121 LYS B CA  1 
ATOM 4252 C C   . LYS B 1 121 ? -146.273 45.930 38.358  1.00 109.03 ?  121 LYS B C   1 
ATOM 4253 O O   . LYS B 1 121 ? -147.243 46.286 39.030  1.00 121.75 ?  121 LYS B O   1 
ATOM 4254 C CB  . LYS B 1 121 ? -146.073 43.858 39.764  1.00 110.35 ?  121 LYS B CB  1 
ATOM 4255 C CG  . LYS B 1 121 ? -146.058 42.338 39.774  1.00 109.83 ?  121 LYS B CG  1 
ATOM 4256 C CD  . LYS B 1 121 ? -146.458 41.796 41.137  1.00 125.47 ?  121 LYS B CD  1 
ATOM 4257 C CE  . LYS B 1 121 ? -146.532 40.278 41.131  1.00 127.61 ?  121 LYS B CE  1 
ATOM 4258 N NZ  . LYS B 1 121 ? -146.931 39.738 42.460  1.00 130.44 ?  121 LYS B NZ  1 
ATOM 4259 N N   . ILE B 1 122 ? -145.610 46.774 37.570  1.00 90.61  ?  122 ILE B N   1 
ATOM 4260 C CA  . ILE B 1 122 ? -146.002 48.166 37.385  1.00 99.46  ?  122 ILE B CA  1 
ATOM 4261 C C   . ILE B 1 122 ? -146.372 48.365 35.924  1.00 98.30  ?  122 ILE B C   1 
ATOM 4262 O O   . ILE B 1 122 ? -145.622 47.959 35.029  1.00 91.30  ?  122 ILE B O   1 
ATOM 4263 C CB  . ILE B 1 122 ? -144.881 49.140 37.792  1.00 104.38 ?  122 ILE B CB  1 
ATOM 4264 C CG1 . ILE B 1 122 ? -144.266 48.733 39.131  1.00 111.61 ?  122 ILE B CG1 1 
ATOM 4265 C CG2 . ILE B 1 122 ? -145.411 50.563 37.857  1.00 111.98 ?  122 ILE B CG2 1 
ATOM 4266 C CD1 . ILE B 1 122 ? -143.110 49.608 39.562  1.00 122.81 ?  122 ILE B CD1 1 
ATOM 4267 N N   . LYS B 1 123 ? -147.520 48.991 35.684  1.00 96.89  ?  123 LYS B N   1 
ATOM 4268 C CA  . LYS B 1 123 ? -147.933 49.314 34.327  1.00 82.81  ?  123 LYS B CA  1 
ATOM 4269 C C   . LYS B 1 123 ? -147.283 50.621 33.892  1.00 93.59  ?  123 LYS B C   1 
ATOM 4270 O O   . LYS B 1 123 ? -147.385 51.636 34.587  1.00 101.69 ?  123 LYS B O   1 
ATOM 4271 C CB  . LYS B 1 123 ? -149.454 49.421 34.236  1.00 75.91  ?  123 LYS B CB  1 
ATOM 4272 C CG  . LYS B 1 123 ? -149.956 49.908 32.887  1.00 65.59  ?  123 LYS B CG  1 
ATOM 4273 C CD  . LYS B 1 123 ? -151.455 50.147 32.909  1.00 68.52  ?  123 LYS B CD  1 
ATOM 4274 C CE  . LYS B 1 123 ? -151.934 50.747 31.599  1.00 87.67  ?  123 LYS B CE  1 
ATOM 4275 N NZ  . LYS B 1 123 ? -153.394 51.033 31.623  1.00 116.72 ?  123 LYS B NZ  1 
ATOM 4276 N N   . HIS B 1 124 ? -146.613 50.593 32.744  1.00 91.39  ?  124 HIS B N   1 
ATOM 4277 C CA  . HIS B 1 124 ? -145.899 51.749 32.228  1.00 98.80  ?  124 HIS B CA  1 
ATOM 4278 C C   . HIS B 1 124 ? -146.516 52.215 30.917  1.00 94.66  ?  124 HIS B C   1 
ATOM 4279 O O   . HIS B 1 124 ? -147.077 51.421 30.158  1.00 90.85  ?  124 HIS B O   1 
ATOM 4280 C CB  . HIS B 1 124 ? -144.416 51.438 32.004  1.00 93.72  ?  124 HIS B CB  1 
ATOM 4281 C CG  . HIS B 1 124 ? -143.617 51.352 33.266  1.00 87.97  ?  124 HIS B CG  1 
ATOM 4282 N ND1 . HIS B 1 124 ? -142.627 52.258 33.582  1.00 80.41  ?  124 HIS B ND1 1 
ATOM 4283 C CD2 . HIS B 1 124 ? -143.658 50.467 34.290  1.00 100.15 ?  124 HIS B CD2 1 
ATOM 4284 C CE1 . HIS B 1 124 ? -142.094 51.935 34.746  1.00 88.53  ?  124 HIS B CE1 1 
ATOM 4285 N NE2 . HIS B 1 124 ? -142.702 50.853 35.197  1.00 98.53  ?  124 HIS B NE2 1 
ATOM 4286 N N   . GLU B 1 125 ? -146.405 53.519 30.666  1.00 87.80  ?  125 GLU B N   1 
ATOM 4287 C CA  . GLU B 1 125 ? -146.769 54.128 29.384  1.00 87.15  ?  125 GLU B CA  1 
ATOM 4288 C C   . GLU B 1 125 ? -145.633 55.090 29.042  1.00 82.20  ?  125 GLU B C   1 
ATOM 4289 O O   . GLU B 1 125 ? -145.643 56.248 29.467  1.00 94.25  ?  125 GLU B O   1 
ATOM 4290 C CB  . GLU B 1 125 ? -148.117 54.834 29.448  1.00 97.87  ?  125 GLU B CB  1 
ATOM 4291 C CG  . GLU B 1 125 ? -149.264 53.957 29.922  1.00 95.56  ?  125 GLU B CG  1 
ATOM 4292 C CD  . GLU B 1 125 ? -150.604 54.656 29.826  1.00 107.28 ?  125 GLU B CD  1 
ATOM 4293 O OE1 . GLU B 1 125 ? -150.821 55.388 28.838  1.00 107.34 ?  125 GLU B OE1 1 
ATOM 4294 O OE2 . GLU B 1 125 ? -151.439 54.476 30.737  1.00 120.11 -1 125 GLU B OE2 1 
ATOM 4295 N N   . TYR B 1 126 ? -144.657 54.596 28.273  1.00 90.60  ?  126 TYR B N   1 
ATOM 4296 C CA  . TYR B 1 126 ? -143.438 55.360 28.023  1.00 95.03  ?  126 TYR B CA  1 
ATOM 4297 C C   . TYR B 1 126 ? -143.729 56.715 27.389  1.00 88.98  ?  126 TYR B C   1 
ATOM 4298 O O   . TYR B 1 126 ? -142.986 57.676 27.615  1.00 92.59  ?  126 TYR B O   1 
ATOM 4299 C CB  . TYR B 1 126 ? -142.484 54.552 27.140  1.00 91.64  ?  126 TYR B CB  1 
ATOM 4300 C CG  . TYR B 1 126 ? -141.087 55.130 27.054  1.00 95.47  ?  126 TYR B CG  1 
ATOM 4301 C CD1 . TYR B 1 126 ? -140.758 56.062 26.077  1.00 95.08  ?  126 TYR B CD1 1 
ATOM 4302 C CD2 . TYR B 1 126 ? -140.101 54.751 27.955  1.00 103.03 ?  126 TYR B CD2 1 
ATOM 4303 C CE1 . TYR B 1 126 ? -139.485 56.595 25.997  1.00 92.72  ?  126 TYR B CE1 1 
ATOM 4304 C CE2 . TYR B 1 126 ? -138.825 55.278 27.883  1.00 114.38 ?  126 TYR B CE2 1 
ATOM 4305 C CZ  . TYR B 1 126 ? -138.523 56.200 26.903  1.00 100.01 ?  126 TYR B CZ  1 
ATOM 4306 O OH  . TYR B 1 126 ? -137.255 56.729 26.828  1.00 97.48  ?  126 TYR B OH  1 
ATOM 4307 N N   . HIS B 1 127 ? -144.802 56.816 26.603  1.00 88.45  ?  127 HIS B N   1 
ATOM 4308 C CA  . HIS B 1 127 ? -145.130 58.088 25.966  1.00 93.87  ?  127 HIS B CA  1 
ATOM 4309 C C   . HIS B 1 127 ? -145.671 59.091 26.981  1.00 91.81  ?  127 HIS B C   1 
ATOM 4310 O O   . HIS B 1 127 ? -145.212 60.237 27.039  1.00 104.20 ?  127 HIS B O   1 
ATOM 4311 C CB  . HIS B 1 127 ? -146.130 57.863 24.830  1.00 100.30 ?  127 HIS B CB  1 
ATOM 4312 C CG  . HIS B 1 127 ? -147.374 57.142 25.250  1.00 102.51 ?  127 HIS B CG  1 
ATOM 4313 N ND1 . HIS B 1 127 ? -147.385 55.803 25.577  1.00 95.38  ?  127 HIS B ND1 1 
ATOM 4314 C CD2 . HIS B 1 127 ? -148.649 57.575 25.394  1.00 100.54 ?  127 HIS B CD2 1 
ATOM 4315 C CE1 . HIS B 1 127 ? -148.613 55.442 25.905  1.00 94.71  ?  127 HIS B CE1 1 
ATOM 4316 N NE2 . HIS B 1 127 ? -149.398 56.499 25.803  1.00 91.97  ?  127 HIS B NE2 1 
ATOM 4317 N N   . ILE B 1 128 ? -146.646 58.677 27.792  1.00 92.39  ?  128 ILE B N   1 
ATOM 4318 C CA  . ILE B 1 128 ? -147.227 59.585 28.777  1.00 98.06  ?  128 ILE B CA  1 
ATOM 4319 C C   . ILE B 1 128 ? -146.238 59.858 29.905  1.00 91.07  ?  128 ILE B C   1 
ATOM 4320 O O   . ILE B 1 128 ? -146.179 60.972 30.440  1.00 92.32  ?  128 ILE B O   1 
ATOM 4321 C CB  . ILE B 1 128 ? -148.561 59.017 29.299  1.00 102.20 ?  128 ILE B CB  1 
ATOM 4322 C CG1 . ILE B 1 128 ? -149.657 59.192 28.244  1.00 101.42 ?  128 ILE B CG1 1 
ATOM 4323 C CG2 . ILE B 1 128 ? -148.971 59.684 30.604  1.00 100.97 ?  128 ILE B CG2 1 
ATOM 4324 C CD1 . ILE B 1 128 ? -150.998 58.628 28.650  1.00 103.30 ?  128 ILE B CD1 1 
ATOM 4325 N N   . GLU B 1 129 ? -145.438 58.855 30.275  1.00 91.33  ?  129 GLU B N   1 
ATOM 4326 C CA  . GLU B 1 129 ? -144.433 59.042 31.317  1.00 90.25  ?  129 GLU B CA  1 
ATOM 4327 C C   . GLU B 1 129 ? -143.450 60.145 30.940  1.00 90.41  ?  129 GLU B C   1 
ATOM 4328 O O   . GLU B 1 129 ? -143.280 61.125 31.674  1.00 101.02 ?  129 GLU B O   1 
ATOM 4329 C CB  . GLU B 1 129 ? -143.694 57.727 31.578  1.00 84.23  ?  129 GLU B CB  1 
ATOM 4330 C CG  . GLU B 1 129 ? -144.460 56.728 32.433  1.00 77.85  ?  129 GLU B CG  1 
ATOM 4331 C CD  . GLU B 1 129 ? -143.635 55.498 32.768  1.00 87.40  ?  129 GLU B CD  1 
ATOM 4332 O OE1 . GLU B 1 129 ? -144.230 54.466 33.144  1.00 92.62  ?  129 GLU B OE1 1 
ATOM 4333 O OE2 . GLU B 1 129 ? -142.393 55.562 32.652  1.00 106.09 -1 129 GLU B OE2 1 
ATOM 4334 N N   . ASN B 1 130 ? -142.797 60.006 29.788  1.00 99.72  ?  130 ASN B N   1 
ATOM 4335 C CA  . ASN B 1 130 ? -141.801 60.973 29.346  1.00 105.88 ?  130 ASN B CA  1 
ATOM 4336 C C   . ASN B 1 130 ? -142.413 62.199 28.675  1.00 105.28 ?  130 ASN B C   1 
ATOM 4337 O O   . ASN B 1 130 ? -141.676 62.982 28.065  1.00 103.31 ?  130 ASN B O   1 
ATOM 4338 C CB  . ASN B 1 130 ? -140.802 60.302 28.400  1.00 84.14  ?  130 ASN B CB  1 
ATOM 4339 C CG  . ASN B 1 130 ? -139.928 59.284 29.107  1.00 93.52  ?  130 ASN B CG  1 
ATOM 4340 O OD1 . ASN B 1 130 ? -138.947 59.640 29.759  1.00 115.70 ?  130 ASN B OD1 1 
ATOM 4341 N ND2 . ASN B 1 130 ? -140.284 58.011 28.987  1.00 102.66 ?  130 ASN B ND2 1 
ATOM 4342 N N   . GLY B 1 131 ? -143.728 62.384 28.779  1.00 106.12 ?  131 GLY B N   1 
ATOM 4343 C CA  . GLY B 1 131 ? -144.384 63.569 28.260  1.00 114.48 ?  131 GLY B CA  1 
ATOM 4344 C C   . GLY B 1 131 ? -144.174 63.803 26.779  1.00 118.16 ?  131 GLY B C   1 
ATOM 4345 O O   . GLY B 1 131 ? -143.515 64.770 26.386  1.00 122.97 ?  131 GLY B O   1 
ATOM 4346 N N   . LEU B 1 132 ? -144.725 62.926 25.948  1.00 116.48 ?  132 LEU B N   1 
ATOM 4347 C CA  . LEU B 1 132 ? -144.572 63.012 24.505  1.00 105.60 ?  132 LEU B CA  1 
ATOM 4348 C C   . LEU B 1 132 ? -145.941 63.104 23.842  1.00 106.63 ?  132 LEU B C   1 
ATOM 4349 O O   . LEU B 1 132 ? -146.978 62.829 24.451  1.00 122.97 ?  132 LEU B O   1 
ATOM 4350 C CB  . LEU B 1 132 ? -143.795 61.806 23.962  1.00 101.22 ?  132 LEU B CB  1 
ATOM 4351 C CG  . LEU B 1 132 ? -142.355 61.664 24.459  1.00 108.12 ?  132 LEU B CG  1 
ATOM 4352 C CD1 . LEU B 1 132 ? -141.713 60.402 23.902  1.00 92.04  ?  132 LEU B CD1 1 
ATOM 4353 C CD2 . LEU B 1 132 ? -141.537 62.893 24.091  1.00 118.69 ?  132 LEU B CD2 1 
ATOM 4354 N N   . THR B 1 133 ? -145.928 63.502 22.573  1.00 109.87 ?  133 THR B N   1 
ATOM 4355 C CA  . THR B 1 133 ? -147.138 63.632 21.777  1.00 120.94 ?  133 THR B CA  1 
ATOM 4356 C C   . THR B 1 133 ? -146.968 62.860 20.477  1.00 119.31 ?  133 THR B C   1 
ATOM 4357 O O   . THR B 1 133 ? -145.850 62.573 20.043  1.00 124.22 ?  133 THR B O   1 
ATOM 4358 C CB  . THR B 1 133 ? -147.466 65.101 21.473  1.00 114.18 ?  133 THR B CB  1 
ATOM 4359 O OG1 . THR B 1 133 ? -146.314 65.746 20.915  1.00 101.04 ?  133 THR B OG1 1 
ATOM 4360 C CG2 . THR B 1 133 ? -147.885 65.828 22.742  1.00 109.09 ?  133 THR B CG2 1 
ATOM 4361 N N   . GLU B 1 134 ? -148.104 62.527 19.856  1.00 116.66 ?  134 GLU B N   1 
ATOM 4362 C CA  . GLU B 1 134 ? -148.070 61.789 18.598  1.00 116.82 ?  134 GLU B CA  1 
ATOM 4363 C C   . GLU B 1 134 ? -147.313 62.552 17.520  1.00 114.73 ?  134 GLU B C   1 
ATOM 4364 O O   . GLU B 1 134 ? -146.706 61.937 16.638  1.00 116.62 ?  134 GLU B O   1 
ATOM 4365 C CB  . GLU B 1 134 ? -149.491 61.471 18.126  1.00 128.40 ?  134 GLU B CB  1 
ATOM 4366 C CG  . GLU B 1 134 ? -150.389 62.686 17.927  1.00 129.60 ?  134 GLU B CG  1 
ATOM 4367 C CD  . GLU B 1 134 ? -151.009 63.184 19.219  1.00 137.69 ?  134 GLU B CD  1 
ATOM 4368 O OE1 . GLU B 1 134 ? -150.655 62.659 20.295  1.00 139.09 ?  134 GLU B OE1 1 
ATOM 4369 O OE2 . GLU B 1 134 ? -151.852 64.103 19.157  1.00 141.58 -1 134 GLU B OE2 1 
ATOM 4370 N N   . GLU B 1 135 ? -147.335 63.887 17.573  1.00 117.37 ?  135 GLU B N   1 
ATOM 4371 C CA  . GLU B 1 135 ? -146.547 64.678 16.634  1.00 127.67 ?  135 GLU B CA  1 
ATOM 4372 C C   . GLU B 1 135 ? -145.064 64.352 16.743  1.00 108.28 ?  135 GLU B C   1 
ATOM 4373 O O   . GLU B 1 135 ? -144.344 64.387 15.739  1.00 109.30 ?  135 GLU B O   1 
ATOM 4374 C CB  . GLU B 1 135 ? -146.792 66.168 16.873  1.00 142.99 ?  135 GLU B CB  1 
ATOM 4375 C CG  . GLU B 1 135 ? -148.266 66.538 16.944  1.00 151.15 ?  135 GLU B CG  1 
ATOM 4376 C CD  . GLU B 1 135 ? -148.489 68.001 17.270  1.00 176.13 ?  135 GLU B CD  1 
ATOM 4377 O OE1 . GLU B 1 135 ? -147.697 68.845 16.801  1.00 180.60 ?  135 GLU B OE1 1 
ATOM 4378 O OE2 . GLU B 1 135 ? -149.458 68.307 17.997  1.00 197.13 -1 135 GLU B OE2 1 
ATOM 4379 N N   . ASP B 1 136 ? -144.591 64.032 17.948  1.00 112.46 ?  136 ASP B N   1 
ATOM 4380 C CA  . ASP B 1 136 ? -143.238 63.527 18.130  1.00 124.59 ?  136 ASP B CA  1 
ATOM 4381 C C   . ASP B 1 136 ? -143.158 62.016 17.965  1.00 113.05 ?  136 ASP B C   1 
ATOM 4382 O O   . ASP B 1 136 ? -142.111 61.498 17.559  1.00 105.49 ?  136 ASP B O   1 
ATOM 4383 C CB  . ASP B 1 136 ? -142.706 63.918 19.512  1.00 119.46 ?  136 ASP B CB  1 
ATOM 4384 C CG  . ASP B 1 136 ? -142.620 65.420 19.700  1.00 138.68 ?  136 ASP B CG  1 
ATOM 4385 O OD1 . ASP B 1 136 ? -142.872 66.159 18.726  1.00 142.41 ?  136 ASP B OD1 1 
ATOM 4386 O OD2 . ASP B 1 136 ? -142.301 65.860 20.824  1.00 140.56 -1 136 ASP B OD2 1 
ATOM 4387 N N   . LEU B 1 137 ? -144.243 61.300 18.272  1.00 103.99 ?  137 LEU B N   1 
ATOM 4388 C CA  . LEU B 1 137 ? -144.249 59.850 18.102  1.00 111.26 ?  137 LEU B CA  1 
ATOM 4389 C C   . LEU B 1 137 ? -144.325 59.472 16.628  1.00 108.68 ?  137 LEU B C   1 
ATOM 4390 O O   . LEU B 1 137 ? -143.588 58.594 16.164  1.00 104.70 ?  137 LEU B O   1 
ATOM 4391 C CB  . LEU B 1 137 ? -145.413 59.233 18.879  1.00 113.64 ?  137 LEU B CB  1 
ATOM 4392 C CG  . LEU B 1 137 ? -145.416 59.418 20.398  1.00 109.05 ?  137 LEU B CG  1 
ATOM 4393 C CD1 . LEU B 1 137 ? -146.601 58.698 21.023  1.00 107.25 ?  137 LEU B CD1 1 
ATOM 4394 C CD2 . LEU B 1 137 ? -144.109 58.934 21.005  1.00 95.04  ?  137 LEU B CD2 1 
ATOM 4395 N N   . GLN B 1 138 ? -145.221 60.119 15.877  1.00 110.12 ?  138 GLN B N   1 
ATOM 4396 C CA  . GLN B 1 138 ? -145.313 59.848 14.445  1.00 99.19  ?  138 GLN B CA  1 
ATOM 4397 C C   . GLN B 1 138 ? -144.006 60.188 13.742  1.00 96.31  ?  138 GLN B C   1 
ATOM 4398 O O   . GLN B 1 138 ? -143.586 59.478 12.820  1.00 115.94 ?  138 GLN B O   1 
ATOM 4399 C CB  . GLN B 1 138 ? -146.477 60.629 13.832  1.00 97.36  ?  138 GLN B CB  1 
ATOM 4400 C CG  . GLN B 1 138 ? -146.674 60.397 12.343  1.00 105.72 ?  138 GLN B CG  1 
ATOM 4401 C CD  . GLN B 1 138 ? -146.944 58.943 12.011  1.00 113.64 ?  138 GLN B CD  1 
ATOM 4402 O OE1 . GLN B 1 138 ? -147.737 58.278 12.679  1.00 120.61 ?  138 GLN B OE1 1 
ATOM 4403 N NE2 . GLN B 1 138 ? -146.285 58.441 10.974  1.00 122.37 ?  138 GLN B NE2 1 
ATOM 4404 N N   . ALA B 1 139 ? -143.344 61.267 14.169  1.00 87.51  ?  139 ALA B N   1 
ATOM 4405 C CA  . ALA B 1 139 ? -142.044 61.614 13.604  1.00 106.07 ?  139 ALA B CA  1 
ATOM 4406 C C   . ALA B 1 139 ? -141.028 60.500 13.815  1.00 106.75 ?  139 ALA B C   1 
ATOM 4407 O O   . ALA B 1 139 ? -140.154 60.287 12.968  1.00 108.69 ?  139 ALA B O   1 
ATOM 4408 C CB  . ALA B 1 139 ? -141.536 62.921 14.215  1.00 108.38 ?  139 ALA B CB  1 
ATOM 4409 N N   . PHE B 1 140 ? -141.123 59.784 14.937  1.00 108.18 ?  140 PHE B N   1 
ATOM 4410 C CA  . PHE B 1 140 ? -140.241 58.644 15.162  1.00 99.21  ?  140 PHE B CA  1 
ATOM 4411 C C   . PHE B 1 140 ? -140.601 57.482 14.244  1.00 94.34  ?  140 PHE B C   1 
ATOM 4412 O O   . PHE B 1 140 ? -139.720 56.864 13.635  1.00 102.18 ?  140 PHE B O   1 
ATOM 4413 C CB  . PHE B 1 140 ? -140.300 58.216 16.628  1.00 91.39  ?  140 PHE B CB  1 
ATOM 4414 C CG  . PHE B 1 140 ? -139.575 56.934 16.911  1.00 95.50  ?  140 PHE B CG  1 
ATOM 4415 C CD1 . PHE B 1 140 ? -140.275 55.751 17.076  1.00 93.63  ?  140 PHE B CD1 1 
ATOM 4416 C CD2 . PHE B 1 140 ? -138.192 56.908 17.000  1.00 100.09 ?  140 PHE B CD2 1 
ATOM 4417 C CE1 . PHE B 1 140 ? -139.612 54.568 17.334  1.00 89.49  ?  140 PHE B CE1 1 
ATOM 4418 C CE2 . PHE B 1 140 ? -137.523 55.727 17.257  1.00 92.35  ?  140 PHE B CE2 1 
ATOM 4419 C CZ  . PHE B 1 140 ? -138.234 54.555 17.423  1.00 94.24  ?  140 PHE B CZ  1 
ATOM 4420 N N   . LEU B 1 141 ? -141.895 57.165 14.139  1.00 86.54  ?  141 LEU B N   1 
ATOM 4421 C CA  . LEU B 1 141 ? -142.327 56.110 13.227  1.00 95.28  ?  141 LEU B CA  1 
ATOM 4422 C C   . LEU B 1 141 ? -141.997 56.451 11.781  1.00 95.06  ?  141 LEU B C   1 
ATOM 4423 O O   . LEU B 1 141 ? -141.771 55.549 10.966  1.00 96.12  ?  141 LEU B O   1 
ATOM 4424 C CB  . LEU B 1 141 ? -143.827 55.858 13.383  1.00 102.12 ?  141 LEU B CB  1 
ATOM 4425 C CG  . LEU B 1 141 ? -144.289 55.271 14.718  1.00 83.14  ?  141 LEU B CG  1 
ATOM 4426 C CD1 . LEU B 1 141 ? -145.804 55.332 14.835  1.00 82.10  ?  141 LEU B CD1 1 
ATOM 4427 C CD2 . LEU B 1 141 ? -143.790 53.842 14.876  1.00 73.76  ?  141 LEU B CD2 1 
ATOM 4428 N N   . ASP B 1 142 ? -141.967 57.743 11.443  1.00 98.51  ?  142 ASP B N   1 
ATOM 4429 C CA  . ASP B 1 142 ? -141.575 58.158 10.101  1.00 106.72 ?  142 ASP B CA  1 
ATOM 4430 C C   . ASP B 1 142 ? -140.127 57.805 9.789   1.00 101.78 ?  142 ASP B C   1 
ATOM 4431 O O   . ASP B 1 142 ? -139.769 57.689 8.612   1.00 114.17 ?  142 ASP B O   1 
ATOM 4432 C CB  . ASP B 1 142 ? -141.788 59.663 9.934   1.00 103.40 ?  142 ASP B CB  1 
ATOM 4433 C CG  . ASP B 1 142 ? -143.254 60.045 9.886   1.00 100.33 ?  142 ASP B CG  1 
ATOM 4434 O OD1 . ASP B 1 142 ? -144.109 59.143 10.011  1.00 113.02 ?  142 ASP B OD1 1 
ATOM 4435 O OD2 . ASP B 1 142 ? -143.553 61.248 9.727   1.00 91.92  -1 142 ASP B OD2 1 
ATOM 4436 N N   . ARG B 1 143 ? -139.288 57.641 10.811  1.00 95.71  ?  143 ARG B N   1 
ATOM 4437 C CA  . ARG B 1 143 ? -137.887 57.284 10.634  1.00 101.00 ?  143 ARG B CA  1 
ATOM 4438 C C   . ARG B 1 143 ? -137.577 55.871 11.112  1.00 92.09  ?  143 ARG B C   1 
ATOM 4439 O O   . ARG B 1 143 ? -136.401 55.525 11.272  1.00 84.21  ?  143 ARG B O   1 
ATOM 4440 C CB  . ARG B 1 143 ? -136.990 58.285 11.364  1.00 92.95  ?  143 ARG B CB  1 
ATOM 4441 C CG  . ARG B 1 143 ? -137.194 59.732 10.955  1.00 117.71 ?  143 ARG B CG  1 
ATOM 4442 C CD  . ARG B 1 143 ? -136.274 60.641 11.749  1.00 126.57 ?  143 ARG B CD  1 
ATOM 4443 N NE  . ARG B 1 143 ? -136.515 62.052 11.472  1.00 140.34 ?  143 ARG B NE  1 
ATOM 4444 C CZ  . ARG B 1 143 ? -135.915 63.048 12.114  1.00 150.54 ?  143 ARG B CZ  1 
ATOM 4445 N NH1 . ARG B 1 143 ? -135.039 62.788 13.077  1.00 139.83 ?  143 ARG B NH1 1 
ATOM 4446 N NH2 . ARG B 1 143 ? -136.193 64.304 11.797  1.00 155.65 ?  143 ARG B NH2 1 
ATOM 4447 N N   . LEU B 1 144 ? -138.594 55.047 11.338  1.00 94.61  ?  144 LEU B N   1 
ATOM 4448 C CA  . LEU B 1 144 ? -138.414 53.700 11.857  1.00 82.22  ?  144 LEU B CA  1 
ATOM 4449 C C   . LEU B 1 144 ? -138.616 52.677 10.748  1.00 87.83  ?  144 LEU B C   1 
ATOM 4450 O O   . LEU B 1 144 ? -139.540 52.799 9.938   1.00 95.69  ?  144 LEU B O   1 
ATOM 4451 C CB  . LEU B 1 144 ? -139.386 53.429 13.005  1.00 82.17  ?  144 LEU B CB  1 
ATOM 4452 C CG  . LEU B 1 144 ? -139.241 52.099 13.741  1.00 63.01  ?  144 LEU B CG  1 
ATOM 4453 C CD1 . LEU B 1 144 ? -137.796 51.856 14.144  1.00 83.25  ?  144 LEU B CD1 1 
ATOM 4454 C CD2 . LEU B 1 144 ? -140.151 52.080 14.955  1.00 88.43  ?  144 LEU B CD2 1 
ATOM 4455 N N   . VAL B 1 145 ? -137.751 51.666 10.722  1.00 76.32  ?  145 VAL B N   1 
ATOM 4456 C CA  . VAL B 1 145 ? -137.779 50.618 9.707   1.00 75.28  ?  145 VAL B CA  1 
ATOM 4457 C C   . VAL B 1 145 ? -137.934 49.283 10.422  1.00 82.94  ?  145 VAL B C   1 
ATOM 4458 O O   . VAL B 1 145 ? -137.004 48.822 11.098  1.00 85.31  ?  145 VAL B O   1 
ATOM 4459 C CB  . VAL B 1 145 ? -136.516 50.630 8.834   1.00 73.51  ?  145 VAL B CB  1 
ATOM 4460 C CG1 . VAL B 1 145 ? -136.590 49.539 7.777   1.00 86.23  ?  145 VAL B CG1 1 
ATOM 4461 C CG2 . VAL B 1 145 ? -136.324 51.995 8.191   1.00 86.29  ?  145 VAL B CG2 1 
ATOM 4462 N N   . ILE B 1 146 ? -139.101 48.659 10.275  1.00 78.36  ?  146 ILE B N   1 
ATOM 4463 C CA  . ILE B 1 146 ? -139.382 47.357 10.872  1.00 82.89  ?  146 ILE B CA  1 
ATOM 4464 C C   . ILE B 1 146 ? -139.846 46.416 9.772   1.00 97.41  ?  146 ILE B C   1 
ATOM 4465 O O   . ILE B 1 146 ? -140.869 46.669 9.125   1.00 106.04 ?  146 ILE B O   1 
ATOM 4466 C CB  . ILE B 1 146 ? -140.439 47.436 11.985  1.00 84.23  ?  146 ILE B CB  1 
ATOM 4467 C CG1 . ILE B 1 146 ? -140.312 48.742 12.767  1.00 93.10  ?  146 ILE B CG1 1 
ATOM 4468 C CG2 . ILE B 1 146 ? -140.317 46.239 12.919  1.00 74.81  ?  146 ILE B CG2 1 
ATOM 4469 C CD1 . ILE B 1 146 ? -141.295 48.854 13.902  1.00 83.25  ?  146 ILE B CD1 1 
ATOM 4470 N N   . ASN B 1 147 ? -139.100 45.331 9.564   1.00 86.48  ?  147 ASN B N   1 
ATOM 4471 C CA  . ASN B 1 147 ? -139.477 44.281 8.615   1.00 94.62  ?  147 ASN B CA  1 
ATOM 4472 C C   . ASN B 1 147 ? -139.156 42.943 9.277   1.00 90.43  ?  147 ASN B C   1 
ATOM 4473 O O   . ASN B 1 147 ? -138.039 42.432 9.159   1.00 92.83  ?  147 ASN B O   1 
ATOM 4474 C CB  . ASN B 1 147 ? -138.752 44.443 7.285   1.00 87.33  ?  147 ASN B CB  1 
ATOM 4475 C CG  . ASN B 1 147 ? -139.057 43.317 6.314   1.00 95.18  ?  147 ASN B CG  1 
ATOM 4476 O OD1 . ASN B 1 147 ? -140.089 42.653 6.418   1.00 108.31 ?  147 ASN B OD1 1 
ATOM 4477 N ND2 . ASN B 1 147 ? -138.154 43.093 5.365   1.00 100.93 ?  147 ASN B ND2 1 
ATOM 4478 N N   . ILE B 1 148 ? -140.142 42.379 9.979   1.00 69.55  ?  148 ILE B N   1 
ATOM 4479 C CA  . ILE B 1 148 ? -139.971 41.055 10.564  1.00 69.83  ?  148 ILE B CA  1 
ATOM 4480 C C   . ILE B 1 148 ? -140.064 39.952 9.524   1.00 76.39  ?  148 ILE B C   1 
ATOM 4481 O O   . ILE B 1 148 ? -139.730 38.799 9.819   1.00 81.09  ?  148 ILE B O   1 
ATOM 4482 C CB  . ILE B 1 148 ? -141.002 40.822 11.686  1.00 82.25  ?  148 ILE B CB  1 
ATOM 4483 C CG1 . ILE B 1 148 ? -142.403 41.225 11.223  1.00 98.52  ?  148 ILE B CG1 1 
ATOM 4484 C CG2 . ILE B 1 148 ? -140.607 41.596 12.934  1.00 89.40  ?  148 ILE B CG2 1 
ATOM 4485 C CD1 . ILE B 1 148 ? -143.453 41.141 12.309  1.00 84.53  ?  148 ILE B CD1 1 
ATOM 4486 N N   . ASN B 1 149 ? -140.519 40.279 8.319   1.00 86.13  ?  149 ASN B N   1 
ATOM 4487 C CA  . ASN B 1 149 ? -140.497 39.356 7.186   1.00 95.74  ?  149 ASN B CA  1 
ATOM 4488 C C   . ASN B 1 149 ? -139.251 39.591 6.332   1.00 88.22  ?  149 ASN B C   1 
ATOM 4489 O O   . ASN B 1 149 ? -139.327 39.850 5.132   1.00 103.16 ?  149 ASN B O   1 
ATOM 4490 C CB  . ASN B 1 149 ? -141.767 39.515 6.356   1.00 94.22  ?  149 ASN B CB  1 
ATOM 4491 C CG  . ASN B 1 149 ? -142.986 39.818 7.204   1.00 90.81  ?  149 ASN B CG  1 
ATOM 4492 O OD1 . ASN B 1 149 ? -143.636 38.908 7.715   1.00 84.81  ?  149 ASN B OD1 1 
ATOM 4493 N ND2 . ASN B 1 149 ? -143.298 41.100 7.365   1.00 89.46  ?  149 ASN B ND2 1 
ATOM 4494 N N   . ALA B 1 150 ? -138.087 39.493 6.965   1.00 96.19  ?  150 ALA B N   1 
ATOM 4495 C CA  . ALA B 1 150 ? -136.818 39.745 6.300   1.00 101.86 ?  150 ALA B CA  1 
ATOM 4496 C C   . ALA B 1 150 ? -136.053 38.442 6.109   1.00 99.98  ?  150 ALA B C   1 
ATOM 4497 O O   . ALA B 1 150 ? -136.417 37.390 6.641   1.00 96.55  ?  150 ALA B O   1 
ATOM 4498 C CB  . ALA B 1 150 ? -135.973 40.749 7.093   1.00 87.57  ?  150 ALA B CB  1 
ATOM 4499 N N   . LYS B 1 151 ? -134.975 38.529 5.337   1.00 108.80 ?  151 LYS B N   1 
ATOM 4500 C CA  . LYS B 1 151 ? -134.149 37.367 5.060   1.00 96.47  ?  151 LYS B CA  1 
ATOM 4501 C C   . LYS B 1 151 ? -133.376 36.950 6.308   1.00 93.91  ?  151 LYS B C   1 
ATOM 4502 O O   . LYS B 1 151 ? -133.174 37.733 7.240   1.00 98.30  ?  151 LYS B O   1 
ATOM 4503 C CB  . LYS B 1 151 ? -133.176 37.664 3.919   1.00 90.79  ?  151 LYS B CB  1 
ATOM 4504 C CG  . LYS B 1 151 ? -133.822 38.335 2.722   1.00 109.96 ?  151 LYS B CG  1 
ATOM 4505 C CD  . LYS B 1 151 ? -132.823 38.558 1.602   1.00 108.93 ?  151 LYS B CD  1 
ATOM 4506 C CE  . LYS B 1 151 ? -133.479 39.246 0.417   1.00 121.15 ?  151 LYS B CE  1 
ATOM 4507 N NZ  . LYS B 1 151 ? -132.534 39.398 -0.722  1.00 117.24 ?  151 LYS B NZ  1 
ATOM 4508 N N   . SER B 1 152 ? -132.946 35.692 6.318   1.00 104.52 ?  152 SER B N   1 
ATOM 4509 C CA  . SER B 1 152 ? -132.108 35.202 7.400   1.00 99.99  ?  152 SER B CA  1 
ATOM 4510 C C   . SER B 1 152 ? -130.739 35.877 7.359   1.00 89.85  ?  152 SER B C   1 
ATOM 4511 O O   . SER B 1 152 ? -130.315 36.421 6.337   1.00 74.52  ?  152 SER B O   1 
ATOM 4512 C CB  . SER B 1 152 ? -131.947 33.684 7.312   1.00 89.85  ?  152 SER B CB  1 
ATOM 4513 O OG  . SER B 1 152 ? -131.102 33.199 8.341   1.00 91.54  ?  152 SER B OG  1 
ATOM 4514 N N   . PHE B 1 153 ? -130.046 35.839 8.498   1.00 97.23  ?  153 PHE B N   1 
ATOM 4515 C CA  . PHE B 1 153 ? -128.701 36.403 8.563   1.00 95.01  ?  153 PHE B CA  1 
ATOM 4516 C C   . PHE B 1 153 ? -127.750 35.645 7.645   1.00 114.95 ?  153 PHE B C   1 
ATOM 4517 O O   . PHE B 1 153 ? -127.010 36.249 6.860   1.00 108.52 ?  153 PHE B O   1 
ATOM 4518 C CB  . PHE B 1 153 ? -128.193 36.385 10.006  1.00 90.52  ?  153 PHE B CB  1 
ATOM 4519 C CG  . PHE B 1 153 ? -126.727 36.692 10.140  1.00 106.08 ?  153 PHE B CG  1 
ATOM 4520 C CD1 . PHE B 1 153 ? -125.811 35.679 10.376  1.00 124.77 ?  153 PHE B CD1 1 
ATOM 4521 C CD2 . PHE B 1 153 ? -126.264 37.992 10.028  1.00 84.80  ?  153 PHE B CD2 1 
ATOM 4522 C CE1 . PHE B 1 153 ? -124.461 35.958 10.498  1.00 121.35 ?  153 PHE B CE1 1 
ATOM 4523 C CE2 . PHE B 1 153 ? -124.917 38.275 10.149  1.00 91.95  ?  153 PHE B CE2 1 
ATOM 4524 C CZ  . PHE B 1 153 ? -124.015 37.259 10.384  1.00 113.54 ?  153 PHE B CZ  1 
ATOM 4525 N N   . ASP B 1 154 ? -127.760 34.313 7.731   1.00 120.05 ?  154 ASP B N   1 
ATOM 4526 C CA  . ASP B 1 154 ? -126.879 33.509 6.892   1.00 120.92 ?  154 ASP B CA  1 
ATOM 4527 C C   . ASP B 1 154 ? -127.339 33.516 5.439   1.00 104.86 ?  154 ASP B C   1 
ATOM 4528 O O   . ASP B 1 154 ? -126.516 33.639 4.524   1.00 103.95 ?  154 ASP B O   1 
ATOM 4529 C CB  . ASP B 1 154 ? -126.812 32.079 7.427   1.00 137.74 ?  154 ASP B CB  1 
ATOM 4530 C CG  . ASP B 1 154 ? -126.726 32.028 8.941   1.00 143.57 ?  154 ASP B CG  1 
ATOM 4531 O OD1 . ASP B 1 154 ? -127.787 31.969 9.597   1.00 143.75 ?  154 ASP B OD1 1 
ATOM 4532 O OD2 . ASP B 1 154 ? -125.597 32.049 9.474   1.00 165.06 -1 154 ASP B OD2 1 
ATOM 4533 N N   . ASP B 1 155 ? -128.648 33.378 5.208   1.00 108.35 ?  155 ASP B N   1 
ATOM 4534 C CA  . ASP B 1 155 ? -129.163 33.372 3.843   1.00 100.30 ?  155 ASP B CA  1 
ATOM 4535 C C   . ASP B 1 155 ? -128.879 34.692 3.138   1.00 100.14 ?  155 ASP B C   1 
ATOM 4536 O O   . ASP B 1 155 ? -128.585 34.711 1.938   1.00 103.29 ?  155 ASP B O   1 
ATOM 4537 C CB  . ASP B 1 155 ? -130.662 33.072 3.850   1.00 106.32 ?  155 ASP B CB  1 
ATOM 4538 C CG  . ASP B 1 155 ? -130.979 31.708 4.431   1.00 116.74 ?  155 ASP B CG  1 
ATOM 4539 O OD1 . ASP B 1 155 ? -130.173 30.774 4.238   1.00 124.24 ?  155 ASP B OD1 1 
ATOM 4540 O OD2 . ASP B 1 155 ? -132.036 31.569 5.081   1.00 103.15 -1 155 ASP B OD2 1 
ATOM 4541 N N   . GLN B 1 156 ? -128.960 35.808 3.867   1.00 95.53  ?  156 GLN B N   1 
ATOM 4542 C CA  . GLN B 1 156 ? -128.585 37.092 3.284   1.00 95.78  ?  156 GLN B CA  1 
ATOM 4543 C C   . GLN B 1 156 ? -127.077 37.195 3.105   1.00 98.48  ?  156 GLN B C   1 
ATOM 4544 O O   . GLN B 1 156 ? -126.607 37.817 2.145   1.00 92.03  ?  156 GLN B O   1 
ATOM 4545 C CB  . GLN B 1 156 ? -129.101 38.236 4.157   1.00 95.65  ?  156 GLN B CB  1 
ATOM 4546 C CG  . GLN B 1 156 ? -129.531 39.478 3.394   1.00 88.08  ?  156 GLN B CG  1 
ATOM 4547 C CD  . GLN B 1 156 ? -128.464 40.550 3.376   1.00 103.20 ?  156 GLN B CD  1 
ATOM 4548 O OE1 . GLN B 1 156 ? -127.277 40.255 3.259   1.00 123.85 ?  156 GLN B OE1 1 
ATOM 4549 N NE2 . GLN B 1 156 ? -128.883 41.806 3.499   1.00 82.73  ?  156 GLN B NE2 1 
ATOM 4550 N N   . LYS B 1 157 ? -126.307 36.589 4.012   1.00 103.80 ?  157 LYS B N   1 
ATOM 4551 C CA  . LYS B 1 157 ? -124.856 36.582 3.868   1.00 102.85 ?  157 LYS B CA  1 
ATOM 4552 C C   . LYS B 1 157 ? -124.427 35.726 2.682   1.00 108.62 ?  157 LYS B C   1 
ATOM 4553 O O   . LYS B 1 157 ? -123.545 36.123 1.911   1.00 115.45 ?  157 LYS B O   1 
ATOM 4554 C CB  . LYS B 1 157 ? -124.206 36.085 5.160   1.00 102.86 ?  157 LYS B CB  1 
ATOM 4555 C CG  . LYS B 1 157 ? -122.791 36.589 5.392   1.00 105.04 ?  157 LYS B CG  1 
ATOM 4556 C CD  . LYS B 1 157 ? -122.347 36.322 6.824   1.00 124.01 ?  157 LYS B CD  1 
ATOM 4557 C CE  . LYS B 1 157 ? -120.961 36.885 7.097   1.00 119.39 ?  157 LYS B CE  1 
ATOM 4558 N NZ  . LYS B 1 157 ? -120.580 36.772 8.533   1.00 97.25  ?  157 LYS B NZ  1 
ATOM 4559 N N   . LYS B 1 158 ? -125.037 34.548 2.521   1.00 104.84 ?  158 LYS B N   1 
ATOM 4560 C CA  . LYS B 1 158 ? -124.779 33.734 1.336   1.00 93.66  ?  158 LYS B CA  1 
ATOM 4561 C C   . LYS B 1 158 ? -125.205 34.467 0.072   1.00 100.70 ?  158 LYS B C   1 
ATOM 4562 O O   . LYS B 1 158 ? -124.484 34.475 -0.933  1.00 102.74 ?  158 LYS B O   1 
ATOM 4563 C CB  . LYS B 1 158 ? -125.512 32.397 1.441   1.00 89.56  ?  158 LYS B CB  1 
ATOM 4564 C CG  . LYS B 1 158 ? -125.039 31.481 2.554   1.00 103.06 ?  158 LYS B CG  1 
ATOM 4565 C CD  . LYS B 1 158 ? -125.821 30.175 2.523   1.00 108.36 ?  158 LYS B CD  1 
ATOM 4566 C CE  . LYS B 1 158 ? -125.499 29.286 3.711   1.00 107.66 ?  158 LYS B CE  1 
ATOM 4567 N NZ  . LYS B 1 158 ? -126.341 28.055 3.710   1.00 123.51 ?  158 LYS B NZ  1 
ATOM 4568 N N   . GLU B 1 159 ? -126.388 35.085 0.106   1.00 92.23  ?  159 GLU B N   1 
ATOM 4569 C CA  . GLU B 1 159 ? -126.898 35.793 -1.063  1.00 93.17  ?  159 GLU B CA  1 
ATOM 4570 C C   . GLU B 1 159 ? -125.984 36.946 -1.454  1.00 93.51  ?  159 GLU B C   1 
ATOM 4571 O O   . GLU B 1 159 ? -125.731 37.171 -2.643  1.00 92.54  ?  159 GLU B O   1 
ATOM 4572 C CB  . GLU B 1 159 ? -128.311 36.299 -0.782  1.00 109.49 ?  159 GLU B CB  1 
ATOM 4573 C CG  . GLU B 1 159 ? -129.149 36.541 -2.016  1.00 122.55 ?  159 GLU B CG  1 
ATOM 4574 C CD  . GLU B 1 159 ? -130.494 37.149 -1.681  1.00 140.32 ?  159 GLU B CD  1 
ATOM 4575 O OE1 . GLU B 1 159 ? -130.520 38.282 -1.158  1.00 137.73 ?  159 GLU B OE1 1 
ATOM 4576 O OE2 . GLU B 1 159 ? -131.524 36.488 -1.931  1.00 157.11 -1 159 GLU B OE2 1 
ATOM 4577 N N   . THR B 1 160 ? -125.474 37.685 -0.465  1.00 102.66 ?  160 THR B N   1 
ATOM 4578 C CA  . THR B 1 160 ? -124.592 38.810 -0.759  1.00 103.76 ?  160 THR B CA  1 
ATOM 4579 C C   . THR B 1 160 ? -123.289 38.351 -1.399  1.00 99.27  ?  160 THR B C   1 
ATOM 4580 O O   . THR B 1 160 ? -122.716 39.069 -2.226  1.00 100.31 ?  160 THR B O   1 
ATOM 4581 C CB  . THR B 1 160 ? -124.310 39.601 0.519   1.00 102.06 ?  160 THR B CB  1 
ATOM 4582 O OG1 . THR B 1 160 ? -125.533 39.791 1.243   1.00 95.01  ?  160 THR B OG1 1 
ATOM 4583 C CG2 . THR B 1 160 ? -123.716 40.961 0.186   1.00 84.13  ?  160 THR B CG2 1 
ATOM 4584 N N   . ILE B 1 161 ? -122.808 37.161 -1.035  1.00 97.70  ?  161 ILE B N   1 
ATOM 4585 C CA  . ILE B 1 161 ? -121.572 36.647 -1.616  1.00 106.41 ?  161 ILE B CA  1 
ATOM 4586 C C   . ILE B 1 161 ? -121.776 36.301 -3.086  1.00 112.81 ?  161 ILE B C   1 
ATOM 4587 O O   . ILE B 1 161 ? -120.938 36.625 -3.937  1.00 110.51 ?  161 ILE B O   1 
ATOM 4588 C CB  . ILE B 1 161 ? -121.072 35.433 -0.814  1.00 108.64 ?  161 ILE B CB  1 
ATOM 4589 C CG1 . ILE B 1 161 ? -120.613 35.863 0.578   1.00 96.23  ?  161 ILE B CG1 1 
ATOM 4590 C CG2 . ILE B 1 161 ? -119.941 34.732 -1.552  1.00 96.68  ?  161 ILE B CG2 1 
ATOM 4591 C CD1 . ILE B 1 161 ? -120.243 34.705 1.474   1.00 94.41  ?  161 ILE B CD1 1 
ATOM 4592 N N   . GLN B 1 162 ? -122.889 35.634 -3.406  1.00 112.82 ?  162 GLN B N   1 
ATOM 4593 C CA  . GLN B 1 162 ? -123.151 35.243 -4.788  1.00 103.07 ?  162 GLN B CA  1 
ATOM 4594 C C   . GLN B 1 162 ? -123.270 36.453 -5.703  1.00 96.36  ?  162 GLN B C   1 
ATOM 4595 O O   . GLN B 1 162 ? -122.943 36.364 -6.892  1.00 105.71 ?  162 GLN B O   1 
ATOM 4596 C CB  . GLN B 1 162 ? -124.420 34.394 -4.861  1.00 95.75  ?  162 GLN B CB  1 
ATOM 4597 C CG  . GLN B 1 162 ? -124.355 33.107 -4.056  1.00 98.16  ?  162 GLN B CG  1 
ATOM 4598 C CD  . GLN B 1 162 ? -123.286 32.156 -4.559  1.00 110.49 ?  162 GLN B CD  1 
ATOM 4599 O OE1 . GLN B 1 162 ? -122.130 32.223 -4.140  1.00 112.83 ?  162 GLN B OE1 1 
ATOM 4600 N NE2 . GLN B 1 162 ? -123.668 31.264 -5.466  1.00 107.58 ?  162 GLN B NE2 1 
ATOM 4601 N N   . ILE B 1 163 ? -123.735 37.587 -5.175  1.00 90.57  ?  163 ILE B N   1 
ATOM 4602 C CA  . ILE B 1 163 ? -123.807 38.801 -5.980  1.00 94.40  ?  163 ILE B CA  1 
ATOM 4603 C C   . ILE B 1 163 ? -122.412 39.265 -6.373  1.00 100.62 ?  163 ILE B C   1 
ATOM 4604 O O   . ILE B 1 163 ? -122.219 39.846 -7.448  1.00 112.09 ?  163 ILE B O   1 
ATOM 4605 C CB  . ILE B 1 163 ? -124.577 39.897 -5.216  1.00 94.10  ?  163 ILE B CB  1 
ATOM 4606 C CG1 . ILE B 1 163 ? -125.962 39.396 -4.812  1.00 93.67  ?  163 ILE B CG1 1 
ATOM 4607 C CG2 . ILE B 1 163 ? -124.727 41.135 -6.070  1.00 78.54  ?  163 ILE B CG2 1 
ATOM 4608 C CD1 . ILE B 1 163 ? -126.876 39.108 -5.982  1.00 98.15  ?  163 ILE B CD1 1 
ATOM 4609 N N   . ILE B 1 164 ? -121.417 39.003 -5.526  1.00 98.64  ?  164 ILE B N   1 
ATOM 4610 C CA  . ILE B 1 164 ? -120.060 39.461 -5.804  1.00 108.61 ?  164 ILE B CA  1 
ATOM 4611 C C   . ILE B 1 164 ? -119.335 38.488 -6.725  1.00 109.96 ?  164 ILE B C   1 
ATOM 4612 O O   . ILE B 1 164 ? -118.646 38.904 -7.663  1.00 99.13  ?  164 ILE B O   1 
ATOM 4613 C CB  . ILE B 1 164 ? -119.294 39.671 -4.486  1.00 102.64 ?  164 ILE B CB  1 
ATOM 4614 C CG1 . ILE B 1 164 ? -120.105 40.553 -3.535  1.00 110.22 ?  164 ILE B CG1 1 
ATOM 4615 C CG2 . ILE B 1 164 ? -117.943 40.300 -4.755  1.00 86.31  ?  164 ILE B CG2 1 
ATOM 4616 C CD1 . ILE B 1 164 ? -120.515 41.883 -4.132  1.00 108.80 ?  164 ILE B CD1 1 
ATOM 4617 N N   . LYS B 1 165 ? -119.472 37.182 -6.469  1.00 108.49 ?  165 LYS B N   1 
ATOM 4618 C CA  . LYS B 1 165 ? -118.805 36.182 -7.298  1.00 108.04 ?  165 LYS B CA  1 
ATOM 4619 C C   . LYS B 1 165 ? -119.229 36.287 -8.756  1.00 107.63 ?  165 LYS B C   1 
ATOM 4620 O O   . LYS B 1 165 ? -118.433 35.997 -9.655  1.00 111.16 ?  165 LYS B O   1 
ATOM 4621 C CB  . LYS B 1 165 ? -119.090 34.780 -6.755  1.00 98.84  ?  165 LYS B CB  1 
ATOM 4622 C CG  . LYS B 1 165 ? -118.347 33.661 -7.477  1.00 99.94  ?  165 LYS B CG  1 
ATOM 4623 C CD  . LYS B 1 165 ? -119.298 32.566 -7.943  1.00 114.37 ?  165 LYS B CD  1 
ATOM 4624 C CE  . LYS B 1 165 ? -120.177 33.035 -9.091  1.00 104.11 ?  165 LYS B CE  1 
ATOM 4625 N NZ  . LYS B 1 165 ? -121.149 31.989 -9.512  1.00 101.65 ?  165 LYS B NZ  1 
ATOM 4626 N N   . ASN B 1 166 ? -120.474 36.694 -9.013  1.00 99.86  ?  166 ASN B N   1 
ATOM 4627 C CA  . ASN B 1 166 ? -120.930 36.863 -10.389 1.00 105.54 ?  166 ASN B CA  1 
ATOM 4628 C C   . ASN B 1 166 ? -120.186 38.000 -11.079 1.00 117.84 ?  166 ASN B C   1 
ATOM 4629 O O   . ASN B 1 166 ? -119.762 37.869 -12.233 1.00 123.23 ?  166 ASN B O   1 
ATOM 4630 C CB  . ASN B 1 166 ? -122.438 37.115 -10.412 1.00 109.07 ?  166 ASN B CB  1 
ATOM 4631 C CG  . ASN B 1 166 ? -123.237 35.923 -9.924  1.00 123.08 ?  166 ASN B CG  1 
ATOM 4632 O OD1 . ASN B 1 166 ? -122.794 34.779 -10.024 1.00 123.74 ?  166 ASN B OD1 1 
ATOM 4633 N ND2 . ASN B 1 166 ? -124.425 36.186 -9.390  1.00 135.46 ?  166 ASN B ND2 1 
ATOM 4634 N N   . HIS B 1 167 ? -120.017 39.126 -10.383 1.00 105.14 ?  167 HIS B N   1 
ATOM 4635 C CA  . HIS B 1 167 ? -119.396 40.294 -10.997 1.00 100.90 ?  167 HIS B CA  1 
ATOM 4636 C C   . HIS B 1 167 ? -117.907 40.084 -11.245 1.00 112.47 ?  167 HIS B C   1 
ATOM 4637 O O   . HIS B 1 167 ? -117.349 40.670 -12.180 1.00 116.23 ?  167 HIS B O   1 
ATOM 4638 C CB  . HIS B 1 167 ? -119.619 41.526 -10.119 1.00 83.09  ?  167 HIS B CB  1 
ATOM 4639 C CG  . HIS B 1 167 ? -119.259 42.819 -10.783 1.00 88.67  ?  167 HIS B CG  1 
ATOM 4640 N ND1 . HIS B 1 167 ? -117.960 43.168 -11.080 1.00 95.41  ?  167 HIS B ND1 1 
ATOM 4641 C CD2 . HIS B 1 167 ? -120.031 43.847 -11.207 1.00 110.15 ?  167 HIS B CD2 1 
ATOM 4642 C CE1 . HIS B 1 167 ? -117.946 44.356 -11.659 1.00 109.06 ?  167 HIS B CE1 1 
ATOM 4643 N NE2 . HIS B 1 167 ? -119.191 44.789 -11.748 1.00 113.84 ?  167 HIS B NE2 1 
ATOM 4644 N N   . PHE B 1 168 ? -117.248 39.264 -10.427 1.00 117.54 ?  168 PHE B N   1 
ATOM 4645 C CA  . PHE B 1 168 ? -115.813 39.055 -10.539 1.00 112.22 ?  168 PHE B CA  1 
ATOM 4646 C C   . PHE B 1 168 ? -115.430 37.697 -11.109 1.00 119.06 ?  168 PHE B C   1 
ATOM 4647 O O   . PHE B 1 168 ? -114.274 37.525 -11.513 1.00 124.64 ?  168 PHE B O   1 
ATOM 4648 C CB  . PHE B 1 168 ? -115.140 39.231 -9.168  1.00 108.49 ?  168 PHE B CB  1 
ATOM 4649 C CG  . PHE B 1 168 ? -115.220 40.632 -8.624  1.00 115.52 ?  168 PHE B CG  1 
ATOM 4650 C CD1 . PHE B 1 168 ? -114.242 41.566 -8.930  1.00 117.64 ?  168 PHE B CD1 1 
ATOM 4651 C CD2 . PHE B 1 168 ? -116.269 41.014 -7.804  1.00 107.14 ?  168 PHE B CD2 1 
ATOM 4652 C CE1 . PHE B 1 168 ? -114.311 42.855 -8.428  1.00 109.80 ?  168 PHE B CE1 1 
ATOM 4653 C CE2 . PHE B 1 168 ? -116.343 42.301 -7.300  1.00 111.87 ?  168 PHE B CE2 1 
ATOM 4654 C CZ  . PHE B 1 168 ? -115.362 43.222 -7.612  1.00 110.85 ?  168 PHE B CZ  1 
ATOM 4655 N N   . GLN B 1 169 ? -116.357 36.737 -11.157 1.00 122.65 ?  169 GLN B N   1 
ATOM 4656 C CA  . GLN B 1 169 ? -116.065 35.376 -11.613 1.00 127.27 ?  169 GLN B CA  1 
ATOM 4657 C C   . GLN B 1 169 ? -114.921 34.756 -10.815 1.00 109.83 ?  169 GLN B C   1 
ATOM 4658 O O   . GLN B 1 169 ? -114.119 33.985 -11.349 1.00 123.52 ?  169 GLN B O   1 
ATOM 4659 C CB  . GLN B 1 169 ? -115.754 35.346 -13.112 1.00 136.30 ?  169 GLN B CB  1 
ATOM 4660 C CG  . GLN B 1 169 ? -116.777 36.070 -13.974 1.00 140.55 ?  169 GLN B CG  1 
ATOM 4661 C CD  . GLN B 1 169 ? -116.351 36.164 -15.427 1.00 180.32 ?  169 GLN B CD  1 
ATOM 4662 O OE1 . GLN B 1 169 ? -115.328 35.607 -15.823 1.00 185.91 ?  169 GLN B OE1 1 
ATOM 4663 N NE2 . GLN B 1 169 ? -117.135 36.876 -16.229 1.00 194.31 ?  169 GLN B NE2 1 
ATOM 4664 N N   . CYS B 1 170 ? -114.842 35.090 -9.530  1.00 112.66 ?  170 CYS B N   1 
ATOM 4665 C CA  . CYS B 1 170 ? -113.730 34.687 -8.683  1.00 120.45 ?  170 CYS B CA  1 
ATOM 4666 C C   . CYS B 1 170 ? -114.004 33.313 -8.074  1.00 106.20 ?  170 CYS B C   1 
ATOM 4667 O O   . CYS B 1 170 ? -114.950 32.615 -8.450  1.00 106.32 ?  170 CYS B O   1 
ATOM 4668 C CB  . CYS B 1 170 ? -113.483 35.741 -7.605  1.00 121.67 ?  170 CYS B CB  1 
ATOM 4669 S SG  . CYS B 1 170 ? -114.730 35.775 -6.298  1.00 110.94 ?  170 CYS B SG  1 
ATOM 4670 N N   . GLU B 1 171 ? -113.167 32.914 -7.123  1.00 115.85 ?  171 GLU B N   1 
ATOM 4671 C CA  . GLU B 1 171 ? -113.287 31.638 -6.438  1.00 125.30 ?  171 GLU B CA  1 
ATOM 4672 C C   . GLU B 1 171 ? -114.052 31.818 -5.128  1.00 119.77 ?  171 GLU B C   1 
ATOM 4673 O O   . GLU B 1 171 ? -114.327 32.936 -4.687  1.00 120.26 ?  171 GLU B O   1 
ATOM 4674 C CB  . GLU B 1 171 ? -111.897 31.040 -6.184  1.00 121.71 ?  171 GLU B CB  1 
ATOM 4675 C CG  . GLU B 1 171 ? -111.876 29.531 -5.974  1.00 133.54 ?  171 GLU B CG  1 
ATOM 4676 C CD  . GLU B 1 171 ? -112.094 28.761 -7.262  1.00 129.00 ?  171 GLU B CD  1 
ATOM 4677 O OE1 . GLU B 1 171 ? -111.407 29.066 -8.260  1.00 121.15 ?  171 GLU B OE1 1 
ATOM 4678 O OE2 . GLU B 1 171 ? -112.952 27.854 -7.278  1.00 123.32 -1 171 GLU B OE2 1 
ATOM 4679 N N   . ASP B 1 172 ? -114.404 30.688 -4.509  1.00 115.81 ?  172 ASP B N   1 
ATOM 4680 C CA  . ASP B 1 172 ? -115.167 30.722 -3.264  1.00 116.21 ?  172 ASP B CA  1 
ATOM 4681 C C   . ASP B 1 172 ? -114.392 31.430 -2.159  1.00 112.05 ?  172 ASP B C   1 
ATOM 4682 O O   . ASP B 1 172 ? -114.897 32.373 -1.537  1.00 108.61 ?  172 ASP B O   1 
ATOM 4683 C CB  . ASP B 1 172 ? -115.538 29.301 -2.840  1.00 128.29 ?  172 ASP B CB  1 
ATOM 4684 C CG  . ASP B 1 172 ? -116.645 28.711 -3.691  1.00 138.42 ?  172 ASP B CG  1 
ATOM 4685 O OD1 . ASP B 1 172 ? -117.188 29.438 -4.550  1.00 140.37 ?  172 ASP B OD1 1 
ATOM 4686 O OD2 . ASP B 1 172 ? -116.973 27.520 -3.503  1.00 141.38 -1 172 ASP B OD2 1 
ATOM 4687 N N   . TYR B 1 173 ? -113.161 30.984 -1.894  1.00 112.92 ?  173 TYR B N   1 
ATOM 4688 C CA  . TYR B 1 173 ? -112.341 31.640 -0.880  1.00 108.07 ?  173 TYR B CA  1 
ATOM 4689 C C   . TYR B 1 173 ? -112.007 33.074 -1.268  1.00 104.61 ?  173 TYR B C   1 
ATOM 4690 O O   . TYR B 1 173 ? -111.772 33.916 -0.393  1.00 105.07 ?  173 TYR B O   1 
ATOM 4691 C CB  . TYR B 1 173 ? -111.053 30.849 -0.645  1.00 110.80 ?  173 TYR B CB  1 
ATOM 4692 C CG  . TYR B 1 173 ? -111.251 29.510 0.029   1.00 128.63 ?  173 TYR B CG  1 
ATOM 4693 C CD1 . TYR B 1 173 ? -111.560 29.431 1.380   1.00 123.33 ?  173 TYR B CD1 1 
ATOM 4694 C CD2 . TYR B 1 173 ? -111.119 28.325 -0.684  1.00 137.06 ?  173 TYR B CD2 1 
ATOM 4695 C CE1 . TYR B 1 173 ? -111.738 28.209 2.003   1.00 126.62 ?  173 TYR B CE1 1 
ATOM 4696 C CE2 . TYR B 1 173 ? -111.295 27.098 -0.070  1.00 137.45 ?  173 TYR B CE2 1 
ATOM 4697 C CZ  . TYR B 1 173 ? -111.605 27.047 1.274   1.00 142.06 ?  173 TYR B CZ  1 
ATOM 4698 O OH  . TYR B 1 173 ? -111.781 25.829 1.890   1.00 147.12 ?  173 TYR B OH  1 
ATOM 4699 N N   . GLU B 1 174 ? -111.981 33.371 -2.565  1.00 103.87 ?  174 GLU B N   1 
ATOM 4700 C CA  . GLU B 1 174 ? -111.635 34.698 -3.054  1.00 101.14 ?  174 GLU B CA  1 
ATOM 4701 C C   . GLU B 1 174 ? -112.773 35.702 -2.913  1.00 103.07 ?  174 GLU B C   1 
ATOM 4702 O O   . GLU B 1 174 ? -112.595 36.869 -3.281  1.00 104.99 ?  174 GLU B O   1 
ATOM 4703 C CB  . GLU B 1 174 ? -111.201 34.613 -4.521  1.00 109.13 ?  174 GLU B CB  1 
ATOM 4704 C CG  . GLU B 1 174 ? -110.206 35.680 -4.947  1.00 108.65 ?  174 GLU B CG  1 
ATOM 4705 C CD  . GLU B 1 174 ? -109.854 35.590 -6.418  1.00 122.46 ?  174 GLU B CD  1 
ATOM 4706 O OE1 . GLU B 1 174 ? -110.097 36.571 -7.151  1.00 121.14 ?  174 GLU B OE1 1 
ATOM 4707 O OE2 . GLU B 1 174 ? -109.333 34.536 -6.842  1.00 131.01 -1 174 GLU B OE2 1 
ATOM 4708 N N   . ALA B 1 175 ? -113.927 35.290 -2.392  1.00 96.46  ?  175 ALA B N   1 
ATOM 4709 C CA  . ALA B 1 175 ? -115.082 36.171 -2.264  1.00 90.57  ?  175 ALA B CA  1 
ATOM 4710 C C   . ALA B 1 175 ? -115.507 36.384 -0.821  1.00 102.61 ?  175 ALA B C   1 
ATOM 4711 O O   . ALA B 1 175 ? -115.735 37.528 -0.411  1.00 111.45 ?  175 ALA B O   1 
ATOM 4712 C CB  . ALA B 1 175 ? -116.261 35.614 -3.077  1.00 88.77  ?  175 ALA B CB  1 
ATOM 4713 N N   . GLU B 1 176 ? -115.625 35.311 -0.035  1.00 94.84  ?  176 GLU B N   1 
ATOM 4714 C CA  . GLU B 1 176 ? -116.143 35.439 1.324   1.00 105.75 ?  176 GLU B CA  1 
ATOM 4715 C C   . GLU B 1 176 ? -115.166 36.176 2.233   1.00 111.91 ?  176 GLU B C   1 
ATOM 4716 O O   . GLU B 1 176 ? -115.584 36.967 3.087   1.00 119.17 ?  176 GLU B O   1 
ATOM 4717 C CB  . GLU B 1 176 ? -116.470 34.054 1.888   1.00 104.13 ?  176 GLU B CB  1 
ATOM 4718 C CG  . GLU B 1 176 ? -116.343 33.916 3.407   1.00 119.27 ?  176 GLU B CG  1 
ATOM 4719 C CD  . GLU B 1 176 ? -117.542 34.453 4.172   1.00 119.33 ?  176 GLU B CD  1 
ATOM 4720 O OE1 . GLU B 1 176 ? -118.128 35.470 3.750   1.00 127.02 ?  176 GLU B OE1 1 
ATOM 4721 O OE2 . GLU B 1 176 ? -117.900 33.849 5.206   1.00 116.89 -1 176 GLU B OE2 1 
ATOM 4722 N N   . HIS B 1 177 ? -113.867 35.946 2.059   1.00 105.50 ?  177 HIS B N   1 
ATOM 4723 C CA  . HIS B 1 177 ? -112.860 36.502 2.950   1.00 116.15 ?  177 HIS B CA  1 
ATOM 4724 C C   . HIS B 1 177 ? -112.053 37.629 2.321   1.00 100.06 ?  177 HIS B C   1 
ATOM 4725 O O   . HIS B 1 177 ? -111.229 38.240 3.010   1.00 97.11  ?  177 HIS B O   1 
ATOM 4726 C CB  . HIS B 1 177 ? -111.913 35.392 3.423   1.00 110.19 ?  177 HIS B CB  1 
ATOM 4727 C CG  . HIS B 1 177 ? -112.618 34.186 3.961   1.00 115.06 ?  177 HIS B CG  1 
ATOM 4728 N ND1 . HIS B 1 177 ? -113.086 34.111 5.255   1.00 113.64 ?  177 HIS B ND1 1 
ATOM 4729 C CD2 . HIS B 1 177 ? -112.939 33.008 3.375   1.00 108.14 ?  177 HIS B CD2 1 
ATOM 4730 C CE1 . HIS B 1 177 ? -113.663 32.938 5.444   1.00 113.91 ?  177 HIS B CE1 1 
ATOM 4731 N NE2 . HIS B 1 177 ? -113.586 32.250 4.319   1.00 100.68 ?  177 HIS B NE2 1 
ATOM 4732 N N   . TYR B 1 178 ? -112.259 37.921 1.037   1.00 90.43  ?  178 TYR B N   1 
ATOM 4733 C CA  . TYR B 1 178 ? -111.527 38.988 0.363   1.00 88.28  ?  178 TYR B CA  1 
ATOM 4734 C C   . TYR B 1 178 ? -112.448 40.125 -0.060  1.00 94.28  ?  178 TYR B C   1 
ATOM 4735 O O   . TYR B 1 178 ? -112.219 41.274 0.331   1.00 85.25  ?  178 TYR B O   1 
ATOM 4736 C CB  . TYR B 1 178 ? -110.777 38.413 -0.847  1.00 88.72  ?  178 TYR B CB  1 
ATOM 4737 C CG  . TYR B 1 178 ? -110.121 39.436 -1.759  1.00 87.82  ?  178 TYR B CG  1 
ATOM 4738 C CD1 . TYR B 1 178 ? -109.952 39.169 -3.111  1.00 94.81  ?  178 TYR B CD1 1 
ATOM 4739 C CD2 . TYR B 1 178 ? -109.634 40.643 -1.267  1.00 95.48  ?  178 TYR B CD2 1 
ATOM 4740 C CE1 . TYR B 1 178 ? -109.354 40.085 -3.954  1.00 93.64  ?  178 TYR B CE1 1 
ATOM 4741 C CE2 . TYR B 1 178 ? -109.034 41.566 -2.103  1.00 94.81  ?  178 TYR B CE2 1 
ATOM 4742 C CZ  . TYR B 1 178 ? -108.895 41.279 -3.445  1.00 95.31  ?  178 TYR B CZ  1 
ATOM 4743 O OH  . TYR B 1 178 ? -108.296 42.188 -4.287  1.00 100.76 ?  178 TYR B OH  1 
ATOM 4744 N N   . LEU B 1 179 ? -113.492 39.840 -0.840  1.00 100.79 ?  179 LEU B N   1 
ATOM 4745 C CA  . LEU B 1 179 ? -114.293 40.908 -1.429  1.00 91.05  ?  179 LEU B CA  1 
ATOM 4746 C C   . LEU B 1 179 ? -115.382 41.394 -0.480  1.00 95.38  ?  179 LEU B C   1 
ATOM 4747 O O   . LEU B 1 179 ? -115.628 42.601 -0.383  1.00 94.26  ?  179 LEU B O   1 
ATOM 4748 C CB  . LEU B 1 179 ? -114.896 40.427 -2.748  1.00 95.26  ?  179 LEU B CB  1 
ATOM 4749 C CG  . LEU B 1 179 ? -113.875 39.807 -3.703  1.00 96.83  ?  179 LEU B CG  1 
ATOM 4750 C CD1 . LEU B 1 179 ? -114.555 39.138 -4.884  1.00 103.92 ?  179 LEU B CD1 1 
ATOM 4751 C CD2 . LEU B 1 179 ? -112.893 40.863 -4.185  1.00 100.59 ?  179 LEU B CD2 1 
ATOM 4752 N N   . TYR B 1 180 ? -116.048 40.469 0.215   1.00 103.38 ?  180 TYR B N   1 
ATOM 4753 C CA  . TYR B 1 180 ? -117.082 40.850 1.172   1.00 107.58 ?  180 TYR B CA  1 
ATOM 4754 C C   . TYR B 1 180 ? -116.513 41.726 2.284   1.00 107.97 ?  180 TYR B C   1 
ATOM 4755 O O   . TYR B 1 180 ? -117.134 42.718 2.685   1.00 106.68 ?  180 TYR B O   1 
ATOM 4756 C CB  . TYR B 1 180 ? -117.729 39.591 1.753   1.00 100.67 ?  180 TYR B CB  1 
ATOM 4757 C CG  . TYR B 1 180 ? -118.895 39.830 2.687   1.00 102.43 ?  180 TYR B CG  1 
ATOM 4758 C CD1 . TYR B 1 180 ? -119.246 38.879 3.635   1.00 110.50 ?  180 TYR B CD1 1 
ATOM 4759 C CD2 . TYR B 1 180 ? -119.659 40.988 2.608   1.00 93.54  ?  180 TYR B CD2 1 
ATOM 4760 C CE1 . TYR B 1 180 ? -120.308 39.080 4.490   1.00 103.47 ?  180 TYR B CE1 1 
ATOM 4761 C CE2 . TYR B 1 180 ? -120.725 41.199 3.462   1.00 101.81 ?  180 TYR B CE2 1 
ATOM 4762 C CZ  . TYR B 1 180 ? -121.045 40.239 4.400   1.00 104.11 ?  180 TYR B CZ  1 
ATOM 4763 O OH  . TYR B 1 180 ? -122.104 40.433 5.255   1.00 96.92  ?  180 TYR B OH  1 
ATOM 4764 N N   . SER B 1 181 ? -115.329 41.377 2.789   1.00 100.23 ?  181 SER B N   1 
ATOM 4765 C CA  . SER B 1 181 ? -114.756 42.108 3.916   1.00 95.42  ?  181 SER B CA  1 
ATOM 4766 C C   . SER B 1 181 ? -114.390 43.535 3.524   1.00 95.16  ?  181 SER B C   1 
ATOM 4767 O O   . SER B 1 181 ? -114.729 44.489 4.234   1.00 98.85  ?  181 SER B O   1 
ATOM 4768 C CB  . SER B 1 181 ? -113.536 41.361 4.454   1.00 93.82  ?  181 SER B CB  1 
ATOM 4769 O OG  . SER B 1 181 ? -113.899 40.077 4.932   1.00 103.12 ?  181 SER B OG  1 
ATOM 4770 N N   . ASN B 1 182 ? -113.697 43.702 2.395   1.00 92.99  ?  182 ASN B N   1 
ATOM 4771 C CA  . ASN B 1 182 ? -113.292 45.040 1.974   1.00 98.83  ?  182 ASN B CA  1 
ATOM 4772 C C   . ASN B 1 182 ? -114.486 45.888 1.553   1.00 90.86  ?  182 ASN B C   1 
ATOM 4773 O O   . ASN B 1 182 ? -114.468 47.110 1.736   1.00 93.26  ?  182 ASN B O   1 
ATOM 4774 C CB  . ASN B 1 182 ? -112.273 44.952 0.840   1.00 96.25  ?  182 ASN B CB  1 
ATOM 4775 C CG  . ASN B 1 182 ? -111.133 44.006 1.156   1.00 95.46  ?  182 ASN B CG  1 
ATOM 4776 O OD1 . ASN B 1 182 ? -110.796 43.788 2.320   1.00 91.73  ?  182 ASN B OD1 1 
ATOM 4777 N ND2 . ASN B 1 182 ? -110.529 43.439 0.119   1.00 98.90  ?  182 ASN B ND2 1 
ATOM 4778 N N   . ALA B 1 183 ? -115.524 45.267 0.990   1.00 87.26  ?  183 ALA B N   1 
ATOM 4779 C CA  . ALA B 1 183 ? -116.738 46.008 0.667   1.00 105.66 ?  183 ALA B CA  1 
ATOM 4780 C C   . ALA B 1 183 ? -117.493 46.439 1.916   1.00 98.10  ?  183 ALA B C   1 
ATOM 4781 O O   . ALA B 1 183 ? -118.320 47.354 1.842   1.00 84.32  ?  183 ALA B O   1 
ATOM 4782 C CB  . ALA B 1 183 ? -117.650 45.168 -0.227  1.00 93.60  ?  183 ALA B CB  1 
ATOM 4783 N N   . PHE B 1 184 ? -117.224 45.806 3.058   1.00 97.98  ?  184 PHE B N   1 
ATOM 4784 C CA  . PHE B 1 184 ? -117.907 46.155 4.297   1.00 87.40  ?  184 PHE B CA  1 
ATOM 4785 C C   . PHE B 1 184 ? -117.373 47.462 4.873   1.00 96.42  ?  184 PHE B C   1 
ATOM 4786 O O   . PHE B 1 184 ? -118.115 48.441 5.012   1.00 96.63  ?  184 PHE B O   1 
ATOM 4787 C CB  . PHE B 1 184 ? -117.759 45.012 5.306   1.00 87.86  ?  184 PHE B CB  1 
ATOM 4788 C CG  . PHE B 1 184 ? -118.844 44.965 6.342   1.00 106.01 ?  184 PHE B CG  1 
ATOM 4789 C CD1 . PHE B 1 184 ? -119.382 43.753 6.738   1.00 95.52  ?  184 PHE B CD1 1 
ATOM 4790 C CD2 . PHE B 1 184 ? -119.313 46.125 6.936   1.00 112.93 ?  184 PHE B CD2 1 
ATOM 4791 C CE1 . PHE B 1 184 ? -120.373 43.703 7.694   1.00 99.26  ?  184 PHE B CE1 1 
ATOM 4792 C CE2 . PHE B 1 184 ? -120.301 46.081 7.891   1.00 108.95 ?  184 PHE B CE2 1 
ATOM 4793 C CZ  . PHE B 1 184 ? -120.829 44.870 8.271   1.00 107.57 ?  184 PHE B CZ  1 
ATOM 4794 N N   . ARG B 1 185 ? -116.083 47.494 5.221   1.00 96.23  ?  185 ARG B N   1 
ATOM 4795 C CA  . ARG B 1 185 ? -115.508 48.699 5.805   1.00 102.52 ?  185 ARG B CA  1 
ATOM 4796 C C   . ARG B 1 185 ? -115.504 49.861 4.822   1.00 100.40 ?  185 ARG B C   1 
ATOM 4797 O O   . ARG B 1 185 ? -115.433 51.019 5.249   1.00 101.39 ?  185 ARG B O   1 
ATOM 4798 C CB  . ARG B 1 185 ? -114.090 48.422 6.311   1.00 110.39 ?  185 ARG B CB  1 
ATOM 4799 C CG  . ARG B 1 185 ? -113.034 48.318 5.224   1.00 105.57 ?  185 ARG B CG  1 
ATOM 4800 C CD  . ARG B 1 185 ? -111.797 47.590 5.731   1.00 102.60 ?  185 ARG B CD  1 
ATOM 4801 N NE  . ARG B 1 185 ? -111.264 48.182 6.957   1.00 105.79 ?  185 ARG B NE  1 
ATOM 4802 C CZ  . ARG B 1 185 ? -110.289 49.086 6.995   1.00 101.50 ?  185 ARG B CZ  1 
ATOM 4803 N NH1 . ARG B 1 185 ? -109.733 49.517 5.873   1.00 104.61 ?  185 ARG B NH1 1 
ATOM 4804 N NH2 . ARG B 1 185 ? -109.871 49.563 8.159   1.00 120.15 ?  185 ARG B NH2 1 
ATOM 4805 N N   . LYS B 1 186 ? -115.576 49.578 3.521   1.00 101.27 ?  186 LYS B N   1 
ATOM 4806 C CA  . LYS B 1 186 ? -115.770 50.637 2.538   1.00 109.26 ?  186 LYS B CA  1 
ATOM 4807 C C   . LYS B 1 186 ? -117.156 51.255 2.675   1.00 104.00 ?  186 LYS B C   1 
ATOM 4808 O O   . LYS B 1 186 ? -117.296 52.482 2.736   1.00 104.27 ?  186 LYS B O   1 
ATOM 4809 C CB  . LYS B 1 186 ? -115.557 50.083 1.129   1.00 98.72  ?  186 LYS B CB  1 
ATOM 4810 C CG  . LYS B 1 186 ? -115.800 51.082 0.011   1.00 120.89 ?  186 LYS B CG  1 
ATOM 4811 C CD  . LYS B 1 186 ? -114.838 52.255 0.078   1.00 125.69 ?  186 LYS B CD  1 
ATOM 4812 C CE  . LYS B 1 186 ? -114.965 53.130 -1.160  1.00 114.91 ?  186 LYS B CE  1 
ATOM 4813 N NZ  . LYS B 1 186 ? -116.378 53.523 -1.418  1.00 123.69 ?  186 LYS B NZ  1 
ATOM 4814 N N   . THR B 1 187 ? -118.193 50.416 2.733   1.00 93.62  ?  187 THR B N   1 
ATOM 4815 C CA  . THR B 1 187 ? -119.557 50.921 2.851   1.00 96.86  ?  187 THR B CA  1 
ATOM 4816 C C   . THR B 1 187 ? -119.774 51.623 4.186   1.00 103.34 ?  187 THR B C   1 
ATOM 4817 O O   . THR B 1 187 ? -120.360 52.711 4.238   1.00 99.72  ?  187 THR B O   1 
ATOM 4818 C CB  . THR B 1 187 ? -120.556 49.776 2.678   1.00 95.55  ?  187 THR B CB  1 
ATOM 4819 O OG1 . THR B 1 187 ? -120.318 49.116 1.429   1.00 107.60 ?  187 THR B OG1 1 
ATOM 4820 C CG2 . THR B 1 187 ? -121.981 50.307 2.700   1.00 100.02 ?  187 THR B CG2 1 
ATOM 4821 N N   . TYR B 1 188 ? -119.314 51.008 5.279   1.00 96.92  ?  188 TYR B N   1 
ATOM 4822 C CA  . TYR B 1 188 ? -119.457 51.613 6.601   1.00 96.30  ?  188 TYR B CA  1 
ATOM 4823 C C   . TYR B 1 188 ? -118.810 52.992 6.649   1.00 107.84 ?  188 TYR B C   1 
ATOM 4824 O O   . TYR B 1 188 ? -119.426 53.963 7.103   1.00 119.12 ?  188 TYR B O   1 
ATOM 4825 C CB  . TYR B 1 188 ? -118.858 50.685 7.663   1.00 95.26  ?  188 TYR B CB  1 
ATOM 4826 C CG  . TYR B 1 188 ? -118.537 51.357 8.982   1.00 104.49 ?  188 TYR B CG  1 
ATOM 4827 C CD1 . TYR B 1 188 ? -117.276 51.893 9.219   1.00 118.90 ?  188 TYR B CD1 1 
ATOM 4828 C CD2 . TYR B 1 188 ? -119.487 51.453 9.991   1.00 105.02 ?  188 TYR B CD2 1 
ATOM 4829 C CE1 . TYR B 1 188 ? -116.971 52.507 10.415  1.00 122.16 ?  188 TYR B CE1 1 
ATOM 4830 C CE2 . TYR B 1 188 ? -119.188 52.066 11.197  1.00 96.78  ?  188 TYR B CE2 1 
ATOM 4831 C CZ  . TYR B 1 188 ? -117.928 52.592 11.400  1.00 117.26 ?  188 TYR B CZ  1 
ATOM 4832 O OH  . TYR B 1 188 ? -117.610 53.207 12.588  1.00 136.99 ?  188 TYR B OH  1 
ATOM 4833 N N   . ASP B 1 189 ? -117.561 53.096 6.188   1.00 108.95 ?  189 ASP B N   1 
ATOM 4834 C CA  . ASP B 1 189 ? -116.867 54.380 6.215   1.00 115.41 ?  189 ASP B CA  1 
ATOM 4835 C C   . ASP B 1 189 ? -117.558 55.402 5.320   1.00 112.91 ?  189 ASP B C   1 
ATOM 4836 O O   . ASP B 1 189 ? -117.613 56.592 5.652   1.00 121.62 ?  189 ASP B O   1 
ATOM 4837 C CB  . ASP B 1 189 ? -115.408 54.196 5.795   1.00 130.22 ?  189 ASP B CB  1 
ATOM 4838 C CG  . ASP B 1 189 ? -114.524 53.752 6.943   1.00 142.20 ?  189 ASP B CG  1 
ATOM 4839 O OD1 . ASP B 1 189 ? -114.485 54.457 7.974   1.00 147.96 ?  189 ASP B OD1 1 
ATOM 4840 O OD2 . ASP B 1 189 ? -113.872 52.694 6.817   1.00 142.35 -1 189 ASP B OD2 1 
ATOM 4841 N N   . ILE B 1 190 ? -118.092 54.957 4.182   1.00 111.14 ?  190 ILE B N   1 
ATOM 4842 C CA  . ILE B 1 190 ? -118.816 55.864 3.297   1.00 112.72 ?  190 ILE B CA  1 
ATOM 4843 C C   . ILE B 1 190 ? -120.148 56.264 3.918   1.00 114.18 ?  190 ILE B C   1 
ATOM 4844 O O   . ILE B 1 190 ? -120.515 57.445 3.933   1.00 111.15 ?  190 ILE B O   1 
ATOM 4845 C CB  . ILE B 1 190 ? -119.007 55.226 1.909   1.00 104.52 ?  190 ILE B CB  1 
ATOM 4846 C CG1 . ILE B 1 190 ? -117.672 55.171 1.162   1.00 119.78 ?  190 ILE B CG1 1 
ATOM 4847 C CG2 . ILE B 1 190 ? -120.047 55.993 1.104   1.00 107.76 ?  190 ILE B CG2 1 
ATOM 4848 C CD1 . ILE B 1 190 ? -116.950 56.499 1.103   1.00 135.10 ?  190 ILE B CD1 1 
ATOM 4849 N N   . SER B 1 191 ? -120.893 55.286 4.442   1.00 115.53 ?  191 SER B N   1 
ATOM 4850 C CA  . SER B 1 191 ? -122.181 55.585 5.060   1.00 107.27 ?  191 SER B CA  1 
ATOM 4851 C C   . SER B 1 191 ? -122.014 56.515 6.256   1.00 108.24 ?  191 SER B C   1 
ATOM 4852 O O   . SER B 1 191 ? -122.748 57.499 6.397   1.00 115.59 ?  191 SER B O   1 
ATOM 4853 C CB  . SER B 1 191 ? -122.880 54.289 5.474   1.00 85.97  ?  191 SER B CB  1 
ATOM 4854 O OG  . SER B 1 191 ? -122.136 53.600 6.463   1.00 90.10  ?  191 SER B OG  1 
ATOM 4855 N N   . CYS B 1 192 ? -121.042 56.225 7.126   1.00 113.17 ?  192 CYS B N   1 
ATOM 4856 C CA  . CYS B 1 192 ? -120.810 57.072 8.294   1.00 112.37 ?  192 CYS B CA  1 
ATOM 4857 C C   . CYS B 1 192 ? -120.493 58.504 7.885   1.00 121.56 ?  192 CYS B C   1 
ATOM 4858 O O   . CYS B 1 192 ? -121.004 59.460 8.479   1.00 121.94 ?  192 CYS B O   1 
ATOM 4859 C CB  . CYS B 1 192 ? -119.678 56.499 9.144   1.00 108.45 ?  192 CYS B CB  1 
ATOM 4860 S SG  . CYS B 1 192 ? -120.121 55.019 10.055  1.00 116.37 ?  192 CYS B SG  1 
ATOM 4861 N N   . ASN B 1 193 ? -119.642 58.670 6.875   1.00 131.27 ?  193 ASN B N   1 
ATOM 4862 C CA  . ASN B 1 193 ? -119.277 60.003 6.422   1.00 137.38 ?  193 ASN B CA  1 
ATOM 4863 C C   . ASN B 1 193 ? -120.496 60.736 5.876   1.00 131.10 ?  193 ASN B C   1 
ATOM 4864 O O   . ASN B 1 193 ? -121.385 60.144 5.258   1.00 123.95 ?  193 ASN B O   1 
ATOM 4865 C CB  . ASN B 1 193 ? -118.183 59.925 5.358   1.00 133.51 ?  193 ASN B CB  1 
ATOM 4866 C CG  . ASN B 1 193 ? -116.801 59.742 5.956   1.00 141.07 ?  193 ASN B CG  1 
ATOM 4867 O OD1 . ASN B 1 193 ? -116.200 60.692 6.459   1.00 144.50 ?  193 ASN B OD1 1 
ATOM 4868 N ND2 . ASN B 1 193 ? -116.291 58.518 5.905   1.00 134.39 ?  193 ASN B ND2 1 
ATOM 4869 N N   . LYS B 1 194 ? -120.529 62.045 6.116   1.00 133.78 ?  194 LYS B N   1 
ATOM 4870 C CA  . LYS B 1 194 ? -121.659 62.892 5.760   1.00 129.88 ?  194 LYS B CA  1 
ATOM 4871 C C   . LYS B 1 194 ? -121.237 64.010 4.812   1.00 142.01 ?  194 LYS B C   1 
ATOM 4872 O O   . LYS B 1 194 ? -121.783 65.114 4.857   1.00 148.29 ?  194 LYS B O   1 
ATOM 4873 C CB  . LYS B 1 194 ? -122.306 63.463 7.021   1.00 125.18 ?  194 LYS B CB  1 
ATOM 4874 C CG  . LYS B 1 194 ? -121.319 63.660 8.160   1.00 120.25 ?  194 LYS B CG  1 
ATOM 4875 C CD  . LYS B 1 194 ? -122.018 63.719 9.506   1.00 106.47 ?  194 LYS B CD  1 
ATOM 4876 C CE  . LYS B 1 194 ? -121.013 63.646 10.644  1.00 110.06 ?  194 LYS B CE  1 
ATOM 4877 N NZ  . LYS B 1 194 ? -120.219 62.385 10.599  1.00 118.98 ?  194 LYS B NZ  1 
ATOM 4878 N N   . LYS B 1 195 ? -120.264 63.728 3.946   1.00 149.71 ?  195 LYS B N   1 
ATOM 4879 C CA  . LYS B 1 195 ? -119.760 64.689 2.974   1.00 149.75 ?  195 LYS B CA  1 
ATOM 4880 C C   . LYS B 1 195 ? -120.601 64.744 1.705   1.00 156.08 ?  195 LYS B C   1 
ATOM 4881 O O   . LYS B 1 195 ? -120.103 65.212 0.673   1.00 157.05 ?  195 LYS B O   1 
ATOM 4882 C CB  . LYS B 1 195 ? -118.306 64.362 2.618   1.00 144.42 ?  195 LYS B CB  1 
ATOM 4883 C CG  . LYS B 1 195 ? -117.369 64.216 3.813   1.00 127.65 ?  195 LYS B CG  1 
ATOM 4884 C CD  . LYS B 1 195 ? -116.949 65.563 4.384   1.00 134.91 ?  195 LYS B CD  1 
ATOM 4885 C CE  . LYS B 1 195 ? -117.743 65.920 5.632   1.00 135.20 ?  195 LYS B CE  1 
ATOM 4886 N NZ  . LYS B 1 195 ? -117.299 67.216 6.213   1.00 112.83 ?  195 LYS B NZ  1 
ATOM 4887 N N   . ASP B 1 196 ? -121.850 64.275 1.765   1.00 160.85 ?  196 ASP B N   1 
ATOM 4888 C CA  . ASP B 1 196 ? -122.717 64.167 0.590   1.00 170.93 ?  196 ASP B CA  1 
ATOM 4889 C C   . ASP B 1 196 ? -122.057 63.308 -0.486  1.00 172.61 ?  196 ASP B C   1 
ATOM 4890 O O   . ASP B 1 196 ? -122.067 63.643 -1.673  1.00 180.30 ?  196 ASP B O   1 
ATOM 4891 C CB  . ASP B 1 196 ? -123.094 65.546 0.041   1.00 168.43 ?  196 ASP B CB  1 
ATOM 4892 C CG  . ASP B 1 196 ? -124.394 65.531 -0.749  1.00 160.66 ?  196 ASP B CG  1 
ATOM 4893 O OD1 . ASP B 1 196 ? -124.671 64.530 -1.442  1.00 168.64 ?  196 ASP B OD1 1 
ATOM 4894 O OD2 . ASP B 1 196 ? -125.142 66.528 -0.675  1.00 157.11 -1 196 ASP B OD2 1 
ATOM 4895 N N   . ARG B 1 197 ? -121.466 62.193 -0.063  1.00 160.18 ?  197 ARG B N   1 
ATOM 4896 C CA  . ARG B 1 197 ? -120.754 61.293 -0.966  1.00 161.80 ?  197 ARG B CA  1 
ATOM 4897 C C   . ARG B 1 197 ? -121.748 60.291 -1.538  1.00 162.58 ?  197 ARG B C   1 
ATOM 4898 O O   . ARG B 1 197 ? -122.044 59.266 -0.918  1.00 148.90 ?  197 ARG B O   1 
ATOM 4899 C CB  . ARG B 1 197 ? -119.611 60.592 -0.242  1.00 162.89 ?  197 ARG B CB  1 
ATOM 4900 C CG  . ARG B 1 197 ? -118.231 61.076 -0.656  1.00 165.57 ?  197 ARG B CG  1 
ATOM 4901 C CD  . ARG B 1 197 ? -117.142 60.503 0.237   1.00 158.98 ?  197 ARG B CD  1 
ATOM 4902 N NE  . ARG B 1 197 ? -115.811 60.912 -0.203  1.00 160.45 ?  197 ARG B NE  1 
ATOM 4903 C CZ  . ARG B 1 197 ? -114.693 60.685 0.480   1.00 156.57 ?  197 ARG B CZ  1 
ATOM 4904 N NH1 . ARG B 1 197 ? -114.741 60.050 1.643   1.00 141.50 ?  197 ARG B NH1 1 
ATOM 4905 N NH2 . ARG B 1 197 ? -113.527 61.095 0.000   1.00 146.45 ?  197 ARG B NH2 1 
ATOM 4906 N N   . ARG B 1 198 ? -122.268 60.590 -2.725  1.00 165.89 ?  198 ARG B N   1 
ATOM 4907 C CA  . ARG B 1 198 ? -123.110 59.645 -3.446  1.00 156.90 ?  198 ARG B CA  1 
ATOM 4908 C C   . ARG B 1 198 ? -122.219 58.636 -4.161  1.00 152.51 ?  198 ARG B C   1 
ATOM 4909 O O   . ARG B 1 198 ? -121.432 59.003 -5.042  1.00 163.57 ?  198 ARG B O   1 
ATOM 4910 C CB  . ARG B 1 198 ? -124.026 60.377 -4.425  1.00 155.52 ?  198 ARG B CB  1 
ATOM 4911 C CG  . ARG B 1 198 ? -123.344 61.453 -5.257  1.00 162.90 ?  198 ARG B CG  1 
ATOM 4912 C CD  . ARG B 1 198 ? -124.327 62.103 -6.217  1.00 178.94 ?  198 ARG B CD  1 
ATOM 4913 N NE  . ARG B 1 198 ? -125.423 62.760 -5.509  1.00 186.17 ?  198 ARG B NE  1 
ATOM 4914 C CZ  . ARG B 1 198 ? -126.433 63.384 -6.107  1.00 186.74 ?  198 ARG B CZ  1 
ATOM 4915 N NH1 . ARG B 1 198 ? -127.385 63.954 -5.382  1.00 176.97 ?  198 ARG B NH1 1 
ATOM 4916 N NH2 . ARG B 1 198 ? -126.490 63.439 -7.431  1.00 190.50 ?  198 ARG B NH2 1 
ATOM 4917 N N   . ILE B 1 199 ? -122.334 57.367 -3.770  1.00 135.60 ?  199 ILE B N   1 
ATOM 4918 C CA  . ILE B 1 199 ? -121.437 56.338 -4.273  1.00 139.97 ?  199 ILE B CA  1 
ATOM 4919 C C   . ILE B 1 199 ? -121.711 56.083 -5.752  1.00 149.14 ?  199 ILE B C   1 
ATOM 4920 O O   . ILE B 1 199 ? -122.832 56.263 -6.244  1.00 154.57 ?  199 ILE B O   1 
ATOM 4921 C CB  . ILE B 1 199 ? -121.592 55.056 -3.433  1.00 126.94 ?  199 ILE B CB  1 
ATOM 4922 C CG1 . ILE B 1 199 ? -120.547 54.007 -3.813  1.00 126.62 ?  199 ILE B CG1 1 
ATOM 4923 C CG2 . ILE B 1 199 ? -122.992 54.485 -3.579  1.00 141.46 ?  199 ILE B CG2 1 
ATOM 4924 C CD1 . ILE B 1 199 ? -120.660 52.740 -3.003  1.00 113.91 ?  199 ILE B CD1 1 
ATOM 4925 N N   . LYS B 1 200 ? -120.668 55.685 -6.476  1.00 148.49 ?  200 LYS B N   1 
ATOM 4926 C CA  . LYS B 1 200 ? -120.766 55.328 -7.883  1.00 136.50 ?  200 LYS B CA  1 
ATOM 4927 C C   . LYS B 1 200 ? -120.395 53.861 -8.045  1.00 125.68 ?  200 LYS B C   1 
ATOM 4928 O O   . LYS B 1 200 ? -119.429 53.388 -7.438  1.00 129.41 ?  200 LYS B O   1 
ATOM 4929 C CB  . LYS B 1 200 ? -119.856 56.212 -8.741  1.00 133.52 ?  200 LYS B CB  1 
ATOM 4930 C CG  . LYS B 1 200 ? -119.994 57.699 -8.447  1.00 140.70 ?  200 LYS B CG  1 
ATOM 4931 C CD  . LYS B 1 200 ? -118.905 58.512 -9.128  1.00 141.19 ?  200 LYS B CD  1 
ATOM 4932 C CE  . LYS B 1 200 ? -118.948 59.966 -8.685  1.00 143.84 ?  200 LYS B CE  1 
ATOM 4933 N NZ  . LYS B 1 200 ? -117.854 60.772 -9.296  1.00 110.49 ?  200 LYS B NZ  1 
ATOM 4934 N N   . LYS B 1 201 ? -121.169 53.142 -8.863  1.00 113.50 ?  201 LYS B N   1 
ATOM 4935 C CA  . LYS B 1 201 ? -120.996 51.695 -8.964  1.00 107.14 ?  201 LYS B CA  1 
ATOM 4936 C C   . LYS B 1 201 ? -119.606 51.332 -9.474  1.00 117.58 ?  201 LYS B C   1 
ATOM 4937 O O   . LYS B 1 201 ? -118.910 50.505 -8.875  1.00 114.17 ?  201 LYS B O   1 
ATOM 4938 C CB  . LYS B 1 201 ? -122.067 51.090 -9.870  1.00 108.51 ?  201 LYS B CB  1 
ATOM 4939 C CG  . LYS B 1 201 ? -121.897 49.591 -10.064 1.00 102.55 ?  201 LYS B CG  1 
ATOM 4940 C CD  . LYS B 1 201 ? -122.996 48.997 -10.922 1.00 107.66 ?  201 LYS B CD  1 
ATOM 4941 C CE  . LYS B 1 201 ? -122.898 47.479 -10.951 1.00 111.68 ?  201 LYS B CE  1 
ATOM 4942 N NZ  . LYS B 1 201 ? -123.994 46.860 -11.745 1.00 121.82 ?  201 LYS B NZ  1 
ATOM 4943 N N   . SER B 1 202 ? -119.189 51.938 -10.588 1.00 132.15 ?  202 SER B N   1 
ATOM 4944 C CA  . SER B 1 202 ? -117.885 51.616 -11.161 1.00 129.66 ?  202 SER B CA  1 
ATOM 4945 C C   . SER B 1 202 ? -116.758 51.984 -10.204 1.00 132.85 ?  202 SER B C   1 
ATOM 4946 O O   . SER B 1 202 ? -115.829 51.197 -9.989  1.00 142.02 ?  202 SER B O   1 
ATOM 4947 C CB  . SER B 1 202 ? -117.712 52.328 -12.502 1.00 126.14 ?  202 SER B CB  1 
ATOM 4948 O OG  . SER B 1 202 ? -118.777 52.019 -13.384 1.00 123.12 ?  202 SER B OG  1 
ATOM 4949 N N   . ASP B 1 203 ? -116.825 53.182 -9.618  1.00 123.48 ?  203 ASP B N   1 
ATOM 4950 C CA  . ASP B 1 203 ? -115.777 53.621 -8.700  1.00 126.03 ?  203 ASP B CA  1 
ATOM 4951 C C   . ASP B 1 203 ? -115.710 52.732 -7.464  1.00 122.21 ?  203 ASP B C   1 
ATOM 4952 O O   . ASP B 1 203 ? -114.620 52.448 -6.956  1.00 119.99 ?  203 ASP B O   1 
ATOM 4953 C CB  . ASP B 1 203 ? -116.008 55.079 -8.302  1.00 116.45 ?  203 ASP B CB  1 
ATOM 4954 C CG  . ASP B 1 203 ? -116.161 55.992 -9.502  1.00 134.57 ?  203 ASP B CG  1 
ATOM 4955 O OD1 . ASP B 1 203 ? -117.070 55.749 -10.324 1.00 144.26 ?  203 ASP B OD1 1 
ATOM 4956 O OD2 . ASP B 1 203 ? -115.374 56.954 -9.623  1.00 144.73 -1 203 ASP B OD2 1 
ATOM 4957 N N   . PHE B 1 204 ? -116.864 52.285 -6.966  1.00 118.40 ?  204 PHE B N   1 
ATOM 4958 C CA  . PHE B 1 204 ? -116.880 51.443 -5.773  1.00 116.52 ?  204 PHE B CA  1 
ATOM 4959 C C   . PHE B 1 204 ? -116.266 50.075 -6.044  1.00 114.52 ?  204 PHE B C   1 
ATOM 4960 O O   . PHE B 1 204 ? -115.556 49.527 -5.192  1.00 105.51 ?  204 PHE B O   1 
ATOM 4961 C CB  . PHE B 1 204 ? -118.313 51.297 -5.260  1.00 109.12 ?  204 PHE B CB  1 
ATOM 4962 C CG  . PHE B 1 204 ? -118.481 50.227 -4.221  1.00 102.37 ?  204 PHE B CG  1 
ATOM 4963 C CD1 . PHE B 1 204 ? -119.091 49.026 -4.540  1.00 100.58 ?  204 PHE B CD1 1 
ATOM 4964 C CD2 . PHE B 1 204 ? -118.031 50.421 -2.925  1.00 102.02 ?  204 PHE B CD2 1 
ATOM 4965 C CE1 . PHE B 1 204 ? -119.249 48.038 -3.587  1.00 96.48  ?  204 PHE B CE1 1 
ATOM 4966 C CE2 . PHE B 1 204 ? -118.188 49.437 -1.968  1.00 100.36 ?  204 PHE B CE2 1 
ATOM 4967 C CZ  . PHE B 1 204 ? -118.797 48.244 -2.300  1.00 89.93  ?  204 PHE B CZ  1 
ATOM 4968 N N   . VAL B 1 205 ? -116.527 49.508 -7.223  1.00 113.78 ?  205 VAL B N   1 
ATOM 4969 C CA  . VAL B 1 205 ? -116.038 48.167 -7.526  1.00 122.86 ?  205 VAL B CA  1 
ATOM 4970 C C   . VAL B 1 205 ? -114.536 48.182 -7.786  1.00 133.15 ?  205 VAL B C   1 
ATOM 4971 O O   . VAL B 1 205 ? -113.797 47.330 -7.278  1.00 132.01 ?  205 VAL B O   1 
ATOM 4972 C CB  . VAL B 1 205 ? -116.817 47.577 -8.716  1.00 118.17 ?  205 VAL B CB  1 
ATOM 4973 C CG1 . VAL B 1 205 ? -116.204 46.258 -9.153  1.00 113.98 ?  205 VAL B CG1 1 
ATOM 4974 C CG2 . VAL B 1 205 ? -118.279 47.387 -8.347  1.00 112.73 ?  205 VAL B CG2 1 
ATOM 4975 N N   . GLU B 1 206 ? -114.059 49.147 -8.570  1.00 135.60 ?  206 GLU B N   1 
ATOM 4976 C CA  . GLU B 1 206 ? -112.653 49.196 -8.953  1.00 134.33 ?  206 GLU B CA  1 
ATOM 4977 C C   . GLU B 1 206 ? -111.758 49.811 -7.881  1.00 133.41 ?  206 GLU B C   1 
ATOM 4978 O O   . GLU B 1 206 ? -110.569 50.025 -8.142  1.00 150.24 ?  206 GLU B O   1 
ATOM 4979 C CB  . GLU B 1 206 ? -112.490 49.967 -10.267 1.00 149.61 ?  206 GLU B CB  1 
ATOM 4980 C CG  . GLU B 1 206 ? -112.691 51.469 -10.147 1.00 152.16 ?  206 GLU B CG  1 
ATOM 4981 C CD  . GLU B 1 206 ? -112.607 52.177 -11.486 1.00 156.28 ?  206 GLU B CD  1 
ATOM 4982 O OE1 . GLU B 1 206 ? -113.056 53.339 -11.576 1.00 151.77 ?  206 GLU B OE1 1 
ATOM 4983 O OE2 . GLU B 1 206 ? -112.095 51.569 -12.449 1.00 161.17 -1 206 GLU B OE2 1 
ATOM 4984 N N   . SER B 1 207 ? -112.287 50.095 -6.692  1.00 127.70 ?  207 SER B N   1 
ATOM 4985 C CA  . SER B 1 207 ? -111.498 50.660 -5.604  1.00 126.30 ?  207 SER B CA  1 
ATOM 4986 C C   . SER B 1 207 ? -111.401 49.728 -4.403  1.00 116.78 ?  207 SER B C   1 
ATOM 4987 O O   . SER B 1 207 ? -110.892 50.137 -3.355  1.00 129.96 ?  207 SER B O   1 
ATOM 4988 C CB  . SER B 1 207 ? -112.079 52.008 -5.170  1.00 132.77 ?  207 SER B CB  1 
ATOM 4989 O OG  . SER B 1 207 ? -113.432 51.877 -4.771  1.00 131.26 ?  207 SER B OG  1 
ATOM 4990 N N   . ILE B 1 208 ? -111.876 48.489 -4.527  1.00 104.66 ?  208 ILE B N   1 
ATOM 4991 C CA  . ILE B 1 208 ? -111.901 47.561 -3.402  1.00 103.64 ?  208 ILE B CA  1 
ATOM 4992 C C   . ILE B 1 208 ? -111.238 46.245 -3.787  1.00 99.95  ?  208 ILE B C   1 
ATOM 4993 O O   . ILE B 1 208 ? -111.419 45.226 -3.111  1.00 98.39  ?  208 ILE B O   1 
ATOM 4994 C CB  . ILE B 1 208 ? -113.343 47.330 -2.911  1.00 113.31 ?  208 ILE B CB  1 
ATOM 4995 C CG1 . ILE B 1 208 ? -114.216 46.772 -4.038  1.00 118.69 ?  208 ILE B CG1 1 
ATOM 4996 C CG2 . ILE B 1 208 ? -113.937 48.621 -2.362  1.00 114.81 ?  208 ILE B CG2 1 
ATOM 4997 C CD1 . ILE B 1 208 ? -114.544 45.297 -3.900  1.00 101.76 ?  208 ILE B CD1 1 
ATOM 4998 N N   . ASN B 1 209 ? -110.461 46.252 -4.870  1.00 95.95  ?  209 ASN B N   1 
ATOM 4999 C CA  . ASN B 1 209 ? -109.779 45.051 -5.355  1.00 98.88  ?  209 ASN B CA  1 
ATOM 5000 C C   . ASN B 1 209 ? -108.329 45.413 -5.666  1.00 107.13 ?  209 ASN B C   1 
ATOM 5001 O O   . ASN B 1 209 ? -108.018 45.886 -6.763  1.00 114.61 ?  209 ASN B O   1 
ATOM 5002 C CB  . ASN B 1 209 ? -110.493 44.473 -6.575  1.00 104.57 ?  209 ASN B CB  1 
ATOM 5003 C CG  . ASN B 1 209 ? -109.904 43.147 -7.022  1.00 110.87 ?  209 ASN B CG  1 
ATOM 5004 O OD1 . ASN B 1 209 ? -109.080 42.554 -6.327  1.00 100.24 ?  209 ASN B OD1 1 
ATOM 5005 N ND2 . ASN B 1 209 ? -110.328 42.675 -8.189  1.00 111.54 ?  209 ASN B ND2 1 
ATOM 5006 N N   . LYS B 1 210 ? -107.441 45.186 -4.692  1.00 106.45 ?  210 LYS B N   1 
ATOM 5007 C CA  . LYS B 1 210 ? -106.009 45.404 -4.868  1.00 117.40 ?  210 LYS B CA  1 
ATOM 5008 C C   . LYS B 1 210 ? -105.193 44.206 -4.392  1.00 105.18 ?  210 LYS B C   1 
ATOM 5009 O O   . LYS B 1 210 ? -104.019 44.366 -4.042  1.00 105.27 ?  210 LYS B O   1 
ATOM 5010 C CB  . LYS B 1 210 ? -105.548 46.667 -4.132  1.00 105.76 ?  210 LYS B CB  1 
ATOM 5011 C CG  . LYS B 1 210 ? -105.754 47.969 -4.893  1.00 120.13 ?  210 LYS B CG  1 
ATOM 5012 C CD  . LYS B 1 210 ? -107.172 48.495 -4.744  1.00 116.10 ?  210 LYS B CD  1 
ATOM 5013 C CE  . LYS B 1 210 ? -107.317 49.861 -5.394  1.00 127.95 ?  210 LYS B CE  1 
ATOM 5014 N NZ  . LYS B 1 210 ? -106.931 49.837 -6.831  1.00 138.74 ?  210 LYS B NZ  1 
ATOM 5015 N N   . SER B 1 211 ? -105.793 43.016 -4.362  1.00 106.50 ?  211 SER B N   1 
ATOM 5016 C CA  . SER B 1 211 ? -105.192 41.791 -3.838  1.00 108.98 ?  211 SER B CA  1 
ATOM 5017 C C   . SER B 1 211 ? -104.819 41.902 -2.364  1.00 102.80 ?  211 SER B C   1 
ATOM 5018 O O   . SER B 1 211 ? -104.116 41.030 -1.839  1.00 105.35 ?  211 SER B O   1 
ATOM 5019 C CB  . SER B 1 211 ? -103.966 41.364 -4.657  1.00 103.94 ?  211 SER B CB  1 
ATOM 5020 O OG  . SER B 1 211 ? -104.337 40.997 -5.974  1.00 114.15 ?  211 SER B OG  1 
ATOM 5021 N N   . LYS B 1 212 ? -105.275 42.949 -1.681  1.00 99.19  ?  212 LYS B N   1 
ATOM 5022 C CA  . LYS B 1 212 ? -105.001 43.160 -0.267  1.00 91.76  ?  212 LYS B CA  1 
ATOM 5023 C C   . LYS B 1 212 ? -106.258 42.866 0.539   1.00 88.93  ?  212 LYS B C   1 
ATOM 5024 O O   . LYS B 1 212 ? -107.347 43.336 0.195   1.00 97.00  ?  212 LYS B O   1 
ATOM 5025 C CB  . LYS B 1 212 ? -104.521 44.592 -0.010  1.00 80.11  ?  212 LYS B CB  1 
ATOM 5026 C CG  . LYS B 1 212 ? -105.449 45.672 -0.553  1.00 99.19  ?  212 LYS B CG  1 
ATOM 5027 C CD  . LYS B 1 212 ? -105.155 47.032 0.062   1.00 111.53 ?  212 LYS B CD  1 
ATOM 5028 C CE  . LYS B 1 212 ? -103.862 47.622 -0.477  1.00 107.83 ?  212 LYS B CE  1 
ATOM 5029 N NZ  . LYS B 1 212 ? -103.677 49.035 -0.042  1.00 113.89 ?  212 LYS B NZ  1 
ATOM 5030 N N   . VAL B 1 213 ? -106.108 42.076 1.597   1.00 79.67  ?  213 VAL B N   1 
ATOM 5031 C CA  . VAL B 1 213 ? -107.198 41.781 2.518   1.00 80.33  ?  213 VAL B CA  1 
ATOM 5032 C C   . VAL B 1 213 ? -107.092 42.753 3.684   1.00 90.92  ?  213 VAL B C   1 
ATOM 5033 O O   . VAL B 1 213 ? -106.091 42.758 4.411   1.00 101.47 ?  213 VAL B O   1 
ATOM 5034 C CB  . VAL B 1 213 ? -107.154 40.323 2.999   1.00 71.61  ?  213 VAL B CB  1 
ATOM 5035 C CG1 . VAL B 1 213 ? -108.395 39.997 3.814   1.00 84.64  ?  213 VAL B CG1 1 
ATOM 5036 C CG2 . VAL B 1 213 ? -107.030 39.381 1.810   1.00 78.55  ?  213 VAL B CG2 1 
ATOM 5037 N N   . LEU B 1 214 ? -108.120 43.577 3.860   1.00 90.46  ?  214 LEU B N   1 
ATOM 5038 C CA  . LEU B 1 214 ? -108.092 44.649 4.840   1.00 90.73  ?  214 LEU B CA  1 
ATOM 5039 C C   . LEU B 1 214 ? -108.572 44.137 6.197   1.00 103.74 ?  214 LEU B C   1 
ATOM 5040 O O   . LEU B 1 214 ? -108.988 42.985 6.347   1.00 109.37 ?  214 LEU B O   1 
ATOM 5041 C CB  . LEU B 1 214 ? -108.935 45.832 4.359   1.00 96.57  ?  214 LEU B CB  1 
ATOM 5042 C CG  . LEU B 1 214 ? -108.398 46.729 3.232   1.00 97.00  ?  214 LEU B CG  1 
ATOM 5043 C CD1 . LEU B 1 214 ? -108.258 45.992 1.906   1.00 101.99 ?  214 LEU B CD1 1 
ATOM 5044 C CD2 . LEU B 1 214 ? -109.283 47.953 3.057   1.00 98.71  ?  214 LEU B CD2 1 
ATOM 5045 N N   . PHE B 1 215 ? -108.510 45.005 7.203   1.00 88.54  ?  215 PHE B N   1 
ATOM 5046 C CA  . PHE B 1 215 ? -108.910 44.665 8.562   1.00 87.74  ?  215 PHE B CA  1 
ATOM 5047 C C   . PHE B 1 215 ? -110.354 45.097 8.781   1.00 93.54  ?  215 PHE B C   1 
ATOM 5048 O O   . PHE B 1 215 ? -110.685 46.279 8.629   1.00 93.72  ?  215 PHE B O   1 
ATOM 5049 C CB  . PHE B 1 215 ? -107.989 45.330 9.586   1.00 86.33  ?  215 PHE B CB  1 
ATOM 5050 C CG  . PHE B 1 215 ? -108.362 45.041 11.014  1.00 80.06  ?  215 PHE B CG  1 
ATOM 5051 C CD1 . PHE B 1 215 ? -108.150 43.787 11.560  1.00 66.00  ?  215 PHE B CD1 1 
ATOM 5052 C CD2 . PHE B 1 215 ? -108.926 46.027 11.808  1.00 87.77  ?  215 PHE B CD2 1 
ATOM 5053 C CE1 . PHE B 1 215 ? -108.493 43.519 12.873  1.00 73.80  ?  215 PHE B CE1 1 
ATOM 5054 C CE2 . PHE B 1 215 ? -109.271 45.766 13.122  1.00 90.53  ?  215 PHE B CE2 1 
ATOM 5055 C CZ  . PHE B 1 215 ? -109.054 44.510 13.655  1.00 85.64  ?  215 PHE B CZ  1 
ATOM 5056 N N   . ASN B 1 216 ? -111.207 44.142 9.137   1.00 74.66  ?  216 ASN B N   1 
ATOM 5057 C CA  . ASN B 1 216 ? -112.617 44.395 9.421   1.00 98.99  ?  216 ASN B CA  1 
ATOM 5058 C C   . ASN B 1 216 ? -112.811 44.267 10.928  1.00 92.93  ?  216 ASN B C   1 
ATOM 5059 O O   . ASN B 1 216 ? -112.894 43.156 11.460  1.00 93.72  ?  216 ASN B O   1 
ATOM 5060 C CB  . ASN B 1 216 ? -113.512 43.426 8.654   1.00 94.84  ?  216 ASN B CB  1 
ATOM 5061 C CG  . ASN B 1 216 ? -114.838 44.046 8.262   1.00 103.15 ?  216 ASN B CG  1 
ATOM 5062 O OD1 . ASN B 1 216 ? -115.406 43.714 7.223   1.00 108.53 ?  216 ASN B OD1 1 
ATOM 5063 N ND2 . ASN B 1 216 ? -115.336 44.955 9.093   1.00 103.91 ?  216 ASN B ND2 1 
ATOM 5064 N N   . ILE B 1 217 ? -112.881 45.411 11.613  1.00 81.40  ?  217 ILE B N   1 
ATOM 5065 C CA  . ILE B 1 217 ? -113.001 45.399 13.066  1.00 95.45  ?  217 ILE B CA  1 
ATOM 5066 C C   . ILE B 1 217 ? -114.327 44.795 13.512  1.00 90.02  ?  217 ILE B C   1 
ATOM 5067 O O   . ILE B 1 217 ? -114.425 44.278 14.632  1.00 85.64  ?  217 ILE B O   1 
ATOM 5068 C CB  . ILE B 1 217 ? -112.809 46.825 13.621  1.00 97.70  ?  217 ILE B CB  1 
ATOM 5069 C CG1 . ILE B 1 217 ? -112.760 46.812 15.150  1.00 95.69  ?  217 ILE B CG1 1 
ATOM 5070 C CG2 . ILE B 1 217 ? -113.910 47.749 13.121  1.00 84.64  ?  217 ILE B CG2 1 
ATOM 5071 C CD1 . ILE B 1 217 ? -112.357 48.135 15.759  1.00 120.99 ?  217 ILE B CD1 1 
ATOM 5072 N N   . TRP B 1 218 ? -115.352 44.829 12.656  1.00 84.44  ?  218 TRP B N   1 
ATOM 5073 C CA  . TRP B 1 218 ? -116.616 44.180 12.988  1.00 81.95  ?  218 TRP B CA  1 
ATOM 5074 C C   . TRP B 1 218 ? -116.446 42.670 13.091  1.00 91.61  ?  218 TRP B C   1 
ATOM 5075 O O   . TRP B 1 218 ? -116.839 42.058 14.090  1.00 98.24  ?  218 TRP B O   1 
ATOM 5076 C CB  . TRP B 1 218 ? -117.677 44.533 11.948  1.00 83.01  ?  218 TRP B CB  1 
ATOM 5077 C CG  . TRP B 1 218 ? -117.918 45.999 11.831  1.00 90.66  ?  218 TRP B CG  1 
ATOM 5078 C CD1 . TRP B 1 218 ? -117.262 46.876 11.019  1.00 94.69  ?  218 TRP B CD1 1 
ATOM 5079 C CD2 . TRP B 1 218 ? -118.883 46.768 12.558  1.00 84.01  ?  218 TRP B CD2 1 
ATOM 5080 N NE1 . TRP B 1 218 ? -117.760 48.145 11.192  1.00 86.28  ?  218 TRP B NE1 1 
ATOM 5081 C CE2 . TRP B 1 218 ? -118.757 48.104 12.132  1.00 84.74  ?  218 TRP B CE2 1 
ATOM 5082 C CE3 . TRP B 1 218 ? -119.842 46.456 13.526  1.00 93.79  ?  218 TRP B CE3 1 
ATOM 5083 C CZ2 . TRP B 1 218 ? -119.553 49.127 12.642  1.00 101.62 ?  218 TRP B CZ2 1 
ATOM 5084 C CZ3 . TRP B 1 218 ? -120.632 47.474 14.030  1.00 89.28  ?  218 TRP B CZ3 1 
ATOM 5085 C CH2 . TRP B 1 218 ? -120.483 48.793 13.587  1.00 86.59  ?  218 TRP B CH2 1 
ATOM 5086 N N   . PHE B 1 219 ? -115.862 42.051 12.061  1.00 91.36  ?  219 PHE B N   1 
ATOM 5087 C CA  . PHE B 1 219 ? -115.609 40.614 12.108  1.00 102.83 ?  219 PHE B CA  1 
ATOM 5088 C C   . PHE B 1 219 ? -114.653 40.264 13.241  1.00 103.28 ?  219 PHE B C   1 
ATOM 5089 O O   . PHE B 1 219 ? -114.788 39.212 13.878  1.00 109.62 ?  219 PHE B O   1 
ATOM 5090 C CB  . PHE B 1 219 ? -115.052 40.129 10.767  1.00 106.95 ?  219 PHE B CB  1 
ATOM 5091 C CG  . PHE B 1 219 ? -115.974 40.359 9.596   1.00 105.37 ?  219 PHE B CG  1 
ATOM 5092 C CD1 . PHE B 1 219 ? -117.299 40.721 9.786   1.00 91.52  ?  219 PHE B CD1 1 
ATOM 5093 C CD2 . PHE B 1 219 ? -115.506 40.216 8.300   1.00 108.95 ?  219 PHE B CD2 1 
ATOM 5094 C CE1 . PHE B 1 219 ? -118.138 40.932 8.709   1.00 101.59 ?  219 PHE B CE1 1 
ATOM 5095 C CE2 . PHE B 1 219 ? -116.341 40.427 7.218   1.00 109.71 ?  219 PHE B CE2 1 
ATOM 5096 C CZ  . PHE B 1 219 ? -117.657 40.785 7.423   1.00 107.40 ?  219 PHE B CZ  1 
ATOM 5097 N N   . TYR B 1 220 ? -113.677 41.137 13.504  1.00 97.44  ?  220 TYR B N   1 
ATOM 5098 C CA  . TYR B 1 220 ? -112.786 40.941 14.642  1.00 100.52 ?  220 TYR B CA  1 
ATOM 5099 C C   . TYR B 1 220 ? -113.541 41.013 15.963  1.00 99.56  ?  220 TYR B C   1 
ATOM 5100 O O   . TYR B 1 220 ? -113.163 40.344 16.932  1.00 101.83 ?  220 TYR B O   1 
ATOM 5101 C CB  . TYR B 1 220 ? -111.666 41.982 14.606  1.00 94.92  ?  220 TYR B CB  1 
ATOM 5102 C CG  . TYR B 1 220 ? -110.554 41.744 15.601  1.00 103.18 ?  220 TYR B CG  1 
ATOM 5103 C CD1 . TYR B 1 220 ? -109.443 40.984 15.261  1.00 95.32  ?  220 TYR B CD1 1 
ATOM 5104 C CD2 . TYR B 1 220 ? -110.608 42.293 16.875  1.00 103.98 ?  220 TYR B CD2 1 
ATOM 5105 C CE1 . TYR B 1 220 ? -108.422 40.769 16.165  1.00 99.13  ?  220 TYR B CE1 1 
ATOM 5106 C CE2 . TYR B 1 220 ? -109.592 42.084 17.786  1.00 101.49 ?  220 TYR B CE2 1 
ATOM 5107 C CZ  . TYR B 1 220 ? -108.502 41.322 17.426  1.00 102.30 ?  220 TYR B CZ  1 
ATOM 5108 O OH  . TYR B 1 220 ? -107.489 41.114 18.332  1.00 102.04 ?  220 TYR B OH  1 
ATOM 5109 N N   . GLN B 1 221 ? -114.606 41.814 16.024  1.00 80.11  ?  221 GLN B N   1 
ATOM 5110 C CA  . GLN B 1 221 ? -115.403 41.934 17.237  1.00 87.30  ?  221 GLN B CA  1 
ATOM 5111 C C   . GLN B 1 221 ? -116.607 41.003 17.258  1.00 97.63  ?  221 GLN B C   1 
ATOM 5112 O O   . GLN B 1 221 ? -117.164 40.760 18.334  1.00 114.99 ?  221 GLN B O   1 
ATOM 5113 C CB  . GLN B 1 221 ? -115.878 43.380 17.419  1.00 79.26  ?  221 GLN B CB  1 
ATOM 5114 C CG  . GLN B 1 221 ? -114.923 44.251 18.222  1.00 83.10  ?  221 GLN B CG  1 
ATOM 5115 C CD  . GLN B 1 221 ? -114.788 43.800 19.666  1.00 99.40  ?  221 GLN B CD  1 
ATOM 5116 O OE1 . GLN B 1 221 ? -115.654 43.104 20.197  1.00 88.31  ?  221 GLN B OE1 1 
ATOM 5117 N NE2 . GLN B 1 221 ? -113.694 44.193 20.308  1.00 113.13 ?  221 GLN B NE2 1 
ATOM 5118 N N   . TYR B 1 222 ? -117.019 40.476 16.104  1.00 95.45  ?  222 TYR B N   1 
ATOM 5119 C CA  . TYR B 1 222 ? -118.137 39.542 16.054  1.00 95.65  ?  222 TYR B CA  1 
ATOM 5120 C C   . TYR B 1 222 ? -117.694 38.095 16.211  1.00 93.80  ?  222 TYR B C   1 
ATOM 5121 O O   . TYR B 1 222 ? -118.453 37.275 16.740  1.00 98.50  ?  222 TYR B O   1 
ATOM 5122 C CB  . TYR B 1 222 ? -118.903 39.702 14.738  1.00 82.16  ?  222 TYR B CB  1 
ATOM 5123 C CG  . TYR B 1 222 ? -119.977 38.660 14.521  1.00 95.58  ?  222 TYR B CG  1 
ATOM 5124 C CD1 . TYR B 1 222 ? -121.086 38.596 15.352  1.00 105.95 ?  222 TYR B CD1 1 
ATOM 5125 C CD2 . TYR B 1 222 ? -119.879 37.739 13.487  1.00 100.94 ?  222 TYR B CD2 1 
ATOM 5126 C CE1 . TYR B 1 222 ? -122.070 37.644 15.160  1.00 103.10 ?  222 TYR B CE1 1 
ATOM 5127 C CE2 . TYR B 1 222 ? -120.858 36.783 13.286  1.00 101.66 ?  222 TYR B CE2 1 
ATOM 5128 C CZ  . TYR B 1 222 ? -121.951 36.741 14.125  1.00 101.00 ?  222 TYR B CZ  1 
ATOM 5129 O OH  . TYR B 1 222 ? -122.929 35.792 13.930  1.00 98.19  ?  222 TYR B OH  1 
ATOM 5130 N N   . GLU B 1 223 ? -116.479 37.766 15.768  1.00 93.18  ?  223 GLU B N   1 
ATOM 5131 C CA  . GLU B 1 223 ? -115.949 36.417 15.888  1.00 96.25  ?  223 GLU B CA  1 
ATOM 5132 C C   . GLU B 1 223 ? -114.812 36.299 16.890  1.00 105.80 ?  223 GLU B C   1 
ATOM 5133 O O   . GLU B 1 223 ? -114.579 35.202 17.407  1.00 98.16  ?  223 GLU B O   1 
ATOM 5134 C CB  . GLU B 1 223 ? -115.463 35.917 14.520  1.00 99.00  ?  223 GLU B CB  1 
ATOM 5135 C CG  . GLU B 1 223 ? -116.565 35.819 13.479  1.00 117.40 ?  223 GLU B CG  1 
ATOM 5136 C CD  . GLU B 1 223 ? -116.026 35.723 12.066  1.00 127.85 ?  223 GLU B CD  1 
ATOM 5137 O OE1 . GLU B 1 223 ? -114.912 36.229 11.818  1.00 127.99 ?  223 GLU B OE1 1 
ATOM 5138 O OE2 . GLU B 1 223 ? -116.719 35.142 11.204  1.00 129.32 -1 223 GLU B OE2 1 
ATOM 5139 N N   . GLY B 1 224 ? -114.111 37.386 17.178  1.00 99.09  ?  224 GLY B N   1 
ATOM 5140 C CA  . GLY B 1 224 ? -113.031 37.355 18.153  1.00 89.25  ?  224 GLY B CA  1 
ATOM 5141 C C   . GLY B 1 224 ? -111.701 36.977 17.539  1.00 94.94  ?  224 GLY B C   1 
ATOM 5142 O O   . GLY B 1 224 ? -111.621 36.219 16.576  1.00 98.68  ?  224 GLY B O   1 
ATOM 5143 N N   . ARG B 1 225 ? -110.630 37.537 18.114  1.00 95.13  ?  225 ARG B N   1 
ATOM 5144 C CA  . ARG B 1 225 ? -109.278 37.191 17.685  1.00 82.98  ?  225 ARG B CA  1 
ATOM 5145 C C   . ARG B 1 225 ? -109.036 35.691 17.753  1.00 93.58  ?  225 ARG B C   1 
ATOM 5146 O O   . ARG B 1 225 ? -108.278 35.144 16.942  1.00 98.07  ?  225 ARG B O   1 
ATOM 5147 C CB  . ARG B 1 225 ? -108.253 37.926 18.549  1.00 95.27  ?  225 ARG B CB  1 
ATOM 5148 C CG  . ARG B 1 225 ? -106.840 37.907 17.997  1.00 108.62 ?  225 ARG B CG  1 
ATOM 5149 C CD  . ARG B 1 225 ? -105.846 38.414 19.031  1.00 106.15 ?  225 ARG B CD  1 
ATOM 5150 N NE  . ARG B 1 225 ? -105.296 37.330 19.842  1.00 117.18 ?  225 ARG B NE  1 
ATOM 5151 C CZ  . ARG B 1 225 ? -104.138 36.725 19.596  1.00 106.76 ?  225 ARG B CZ  1 
ATOM 5152 N NH1 . ARG B 1 225 ? -103.397 37.099 18.561  1.00 89.22  ?  225 ARG B NH1 1 
ATOM 5153 N NH2 . ARG B 1 225 ? -103.719 35.748 20.386  1.00 97.42  ?  225 ARG B NH2 1 
ATOM 5154 N N   . LYS B 1 226 ? -109.657 35.015 18.723  1.00 104.36 ?  226 LYS B N   1 
ATOM 5155 C CA  . LYS B 1 226 ? -109.558 33.563 18.819  1.00 107.01 ?  226 LYS B CA  1 
ATOM 5156 C C   . LYS B 1 226 ? -110.024 32.887 17.534  1.00 108.05 ?  226 LYS B C   1 
ATOM 5157 O O   . LYS B 1 226 ? -109.477 31.854 17.134  1.00 104.76 ?  226 LYS B O   1 
ATOM 5158 C CB  . LYS B 1 226 ? -110.378 33.078 20.015  1.00 126.37 ?  226 LYS B CB  1 
ATOM 5159 C CG  . LYS B 1 226 ? -110.443 31.573 20.190  1.00 127.00 ?  226 LYS B CG  1 
ATOM 5160 C CD  . LYS B 1 226 ? -111.596 31.198 21.109  1.00 120.46 ?  226 LYS B CD  1 
ATOM 5161 C CE  . LYS B 1 226 ? -111.485 31.901 22.457  1.00 109.99 ?  226 LYS B CE  1 
ATOM 5162 N NZ  . LYS B 1 226 ? -112.661 31.618 23.325  1.00 118.64 ?  226 LYS B NZ  1 
ATOM 5163 N N   . GLU B 1 227 ? -111.027 33.459 16.872  1.00 112.33 ?  227 GLU B N   1 
ATOM 5164 C CA  . GLU B 1 227 ? -111.615 32.881 15.668  1.00 102.20 ?  227 GLU B CA  1 
ATOM 5165 C C   . GLU B 1 227 ? -111.287 33.654 14.402  1.00 91.79  ?  227 GLU B C   1 
ATOM 5166 O O   . GLU B 1 227 ? -111.112 33.045 13.345  1.00 98.46  ?  227 GLU B O   1 
ATOM 5167 C CB  . GLU B 1 227 ? -113.138 32.792 15.820  1.00 106.31 ?  227 GLU B CB  1 
ATOM 5168 C CG  . GLU B 1 227 ? -113.829 31.969 14.744  1.00 111.97 ?  227 GLU B CG  1 
ATOM 5169 C CD  . GLU B 1 227 ? -113.719 30.477 14.990  1.00 116.57 ?  227 GLU B CD  1 
ATOM 5170 O OE1 . GLU B 1 227 ? -113.376 30.085 16.126  1.00 122.07 ?  227 GLU B OE1 1 
ATOM 5171 O OE2 . GLU B 1 227 ? -113.982 29.696 14.052  1.00 124.55 -1 227 GLU B OE2 1 
ATOM 5172 N N   . TYR B 1 228 ? -111.212 34.986 14.483  1.00 89.23  ?  228 TYR B N   1 
ATOM 5173 C CA  . TYR B 1 228 ? -110.909 35.793 13.304  1.00 77.15  ?  228 TYR B CA  1 
ATOM 5174 C C   . TYR B 1 228 ? -109.586 35.376 12.672  1.00 85.14  ?  228 TYR B C   1 
ATOM 5175 O O   . TYR B 1 228 ? -109.471 35.309 11.442  1.00 89.05  ?  228 TYR B O   1 
ATOM 5176 C CB  . TYR B 1 228 ? -110.892 37.275 13.685  1.00 78.66  ?  228 TYR B CB  1 
ATOM 5177 C CG  . TYR B 1 228 ? -110.481 38.213 12.573  1.00 80.05  ?  228 TYR B CG  1 
ATOM 5178 C CD1 . TYR B 1 228 ? -109.154 38.585 12.407  1.00 80.19  ?  228 TYR B CD1 1 
ATOM 5179 C CD2 . TYR B 1 228 ? -111.423 38.738 11.698  1.00 95.97  ?  228 TYR B CD2 1 
ATOM 5180 C CE1 . TYR B 1 228 ? -108.774 39.443 11.395  1.00 77.15  ?  228 TYR B CE1 1 
ATOM 5181 C CE2 . TYR B 1 228 ? -111.052 39.598 10.683  1.00 89.67  ?  228 TYR B CE2 1 
ATOM 5182 C CZ  . TYR B 1 228 ? -109.727 39.947 10.536  1.00 81.93  ?  228 TYR B CZ  1 
ATOM 5183 O OH  . TYR B 1 228 ? -109.349 40.802 9.528   1.00 95.12  ?  228 TYR B OH  1 
ATOM 5184 N N   . LEU B 1 229 ? -108.576 35.089 13.495  1.00 82.23  ?  229 LEU B N   1 
ATOM 5185 C CA  . LEU B 1 229 ? -107.295 34.641 12.957  1.00 78.02  ?  229 LEU B CA  1 
ATOM 5186 C C   . LEU B 1 229 ? -107.380 33.223 12.409  1.00 88.56  ?  229 LEU B C   1 
ATOM 5187 O O   . LEU B 1 229 ? -106.700 32.900 11.428  1.00 93.51  ?  229 LEU B O   1 
ATOM 5188 C CB  . LEU B 1 229 ? -106.212 34.723 14.032  1.00 82.03  ?  229 LEU B CB  1 
ATOM 5189 C CG  . LEU B 1 229 ? -105.996 36.091 14.680  1.00 81.75  ?  229 LEU B CG  1 
ATOM 5190 C CD1 . LEU B 1 229 ? -104.786 36.044 15.599  1.00 88.23  ?  229 LEU B CD1 1 
ATOM 5191 C CD2 . LEU B 1 229 ? -105.834 37.168 13.620  1.00 78.50  ?  229 LEU B CD2 1 
ATOM 5192 N N   . ARG B 1 230 ? -108.197 32.366 13.028  1.00 92.20  ?  230 ARG B N   1 
ATOM 5193 C CA  . ARG B 1 230 ? -108.312 30.988 12.560  1.00 86.51  ?  230 ARG B CA  1 
ATOM 5194 C C   . ARG B 1 230 ? -108.923 30.929 11.166  1.00 88.39  ?  230 ARG B C   1 
ATOM 5195 O O   . ARG B 1 230 ? -108.527 30.096 10.342  1.00 92.24  ?  230 ARG B O   1 
ATOM 5196 C CB  . ARG B 1 230 ? -109.146 30.161 13.538  1.00 95.75  ?  230 ARG B CB  1 
ATOM 5197 C CG  . ARG B 1 230 ? -109.249 28.689 13.158  1.00 92.16  ?  230 ARG B CG  1 
ATOM 5198 C CD  . ARG B 1 230 ? -110.336 27.977 13.949  1.00 97.75  ?  230 ARG B CD  1 
ATOM 5199 N NE  . ARG B 1 230 ? -111.672 28.430 13.569  1.00 121.97 ?  230 ARG B NE  1 
ATOM 5200 C CZ  . ARG B 1 230 ? -112.348 27.966 12.522  1.00 117.17 ?  230 ARG B CZ  1 
ATOM 5201 N NH1 . ARG B 1 230 ? -111.816 27.029 11.749  1.00 99.96  ?  230 ARG B NH1 1 
ATOM 5202 N NH2 . ARG B 1 230 ? -113.557 28.438 12.248  1.00 120.04 ?  230 ARG B NH2 1 
ATOM 5203 N N   . LYS B 1 231 ? -109.896 31.800 10.886  1.00 81.86  ?  231 LYS B N   1 
ATOM 5204 C CA  . LYS B 1 231 ? -110.496 31.835 9.556   1.00 93.87  ?  231 LYS B CA  1 
ATOM 5205 C C   . LYS B 1 231 ? -109.467 32.223 8.503   1.00 91.12  ?  231 LYS B C   1 
ATOM 5206 O O   . LYS B 1 231 ? -109.374 31.586 7.448   1.00 99.12  ?  231 LYS B O   1 
ATOM 5207 C CB  . LYS B 1 231 ? -111.682 32.799 9.535   1.00 98.15  ?  231 LYS B CB  1 
ATOM 5208 C CG  . LYS B 1 231 ? -112.975 32.196 10.059  1.00 106.06 ?  231 LYS B CG  1 
ATOM 5209 C CD  . LYS B 1 231 ? -114.154 33.130 9.837   1.00 110.09 ?  231 LYS B CD  1 
ATOM 5210 C CE  . LYS B 1 231 ? -115.460 32.479 10.268  1.00 122.91 ?  231 LYS B CE  1 
ATOM 5211 N NZ  . LYS B 1 231 ? -116.633 33.366 10.030  1.00 135.70 ?  231 LYS B NZ  1 
ATOM 5212 N N   . LEU B 1 232 ? -108.680 33.268 8.774   1.00 83.80  ?  232 LEU B N   1 
ATOM 5213 C CA  . LEU B 1 232 ? -107.627 33.664 7.843   1.00 91.84  ?  232 LEU B CA  1 
ATOM 5214 C C   . LEU B 1 232 ? -106.650 32.522 7.598   1.00 82.68  ?  232 LEU B C   1 
ATOM 5215 O O   . LEU B 1 232 ? -106.144 32.354 6.482   1.00 82.89  ?  232 LEU B O   1 
ATOM 5216 C CB  . LEU B 1 232 ? -106.889 34.893 8.375   1.00 71.17  ?  232 LEU B CB  1 
ATOM 5217 C CG  . LEU B 1 232 ? -107.735 36.118 8.731   1.00 75.07  ?  232 LEU B CG  1 
ATOM 5218 C CD1 . LEU B 1 232 ? -106.843 37.314 9.021   1.00 66.01  ?  232 LEU B CD1 1 
ATOM 5219 C CD2 . LEU B 1 232 ? -108.726 36.441 7.623   1.00 81.10  ?  232 LEU B CD2 1 
ATOM 5220 N N   . LYS B 1 233 ? -106.372 31.728 8.633   1.00 83.24  ?  233 LYS B N   1 
ATOM 5221 C CA  . LYS B 1 233 ? -105.467 30.592 8.492   1.00 89.17  ?  233 LYS B CA  1 
ATOM 5222 C C   . LYS B 1 233 ? -106.046 29.541 7.550   1.00 110.97 ?  233 LYS B C   1 
ATOM 5223 O O   . LYS B 1 233 ? -105.399 29.126 6.581   1.00 109.10 ?  233 LYS B O   1 
ATOM 5224 C CB  . LYS B 1 233 ? -105.176 29.990 9.868   1.00 86.35  ?  233 LYS B CB  1 
ATOM 5225 C CG  . LYS B 1 233 ? -104.147 28.873 9.865   1.00 85.47  ?  233 LYS B CG  1 
ATOM 5226 C CD  . LYS B 1 233 ? -104.030 28.234 11.242  1.00 96.03  ?  233 LYS B CD  1 
ATOM 5227 C CE  . LYS B 1 233 ? -102.789 27.363 11.353  1.00 85.31  ?  233 LYS B CE  1 
ATOM 5228 N NZ  . LYS B 1 233 ? -101.541 28.174 11.359  1.00 93.77  ?  233 LYS B NZ  1 
ATOM 5229 N N   . GLU B 1 234 ? -107.271 29.091 7.823   1.00 115.81 ?  234 GLU B N   1 
ATOM 5230 C CA  . GLU B 1 234 ? -107.854 28.024 7.017   1.00 108.70 ?  234 GLU B CA  1 
ATOM 5231 C C   . GLU B 1 234 ? -108.238 28.503 5.621   1.00 100.69 ?  234 GLU B C   1 
ATOM 5232 O O   . GLU B 1 234 ? -108.227 27.710 4.673   1.00 112.24 ?  234 GLU B O   1 
ATOM 5233 C CB  . GLU B 1 234 ? -109.071 27.435 7.730   1.00 108.48 ?  234 GLU B CB  1 
ATOM 5234 C CG  . GLU B 1 234 ? -108.755 26.800 9.075   1.00 112.24 ?  234 GLU B CG  1 
ATOM 5235 C CD  . GLU B 1 234 ? -107.922 25.540 8.946   1.00 133.35 ?  234 GLU B CD  1 
ATOM 5236 O OE1 . GLU B 1 234 ? -106.922 25.409 9.685   1.00 120.49 ?  234 GLU B OE1 1 
ATOM 5237 O OE2 . GLU B 1 234 ? -108.263 24.682 8.106   1.00 149.06 -1 234 GLU B OE2 1 
ATOM 5238 N N   . SER B 1 235 ? -108.572 29.787 5.470   1.00 87.81  ?  235 SER B N   1 
ATOM 5239 C CA  . SER B 1 235 ? -109.110 30.272 4.202   1.00 104.38 ?  235 SER B CA  1 
ATOM 5240 C C   . SER B 1 235 ? -108.011 30.566 3.186   1.00 103.21 ?  235 SER B C   1 
ATOM 5241 O O   . SER B 1 235 ? -108.121 30.182 2.017   1.00 119.24 ?  235 SER B O   1 
ATOM 5242 C CB  . SER B 1 235 ? -109.959 31.522 4.434   1.00 95.21  ?  235 SER B CB  1 
ATOM 5243 O OG  . SER B 1 235 ? -110.946 31.287 5.422   1.00 126.19 ?  235 SER B OG  1 
ATOM 5244 N N   . PHE B 1 236 ? -106.954 31.258 3.606   1.00 101.56 ?  236 PHE B N   1 
ATOM 5245 C CA  . PHE B 1 236 ? -105.948 31.763 2.679   1.00 104.28 ?  236 PHE B CA  1 
ATOM 5246 C C   . PHE B 1 236 ? -104.724 30.867 2.556   1.00 106.18 ?  236 PHE B C   1 
ATOM 5247 O O   . PHE B 1 236 ? -104.249 30.629 1.442   1.00 113.38 ?  236 PHE B O   1 
ATOM 5248 C CB  . PHE B 1 236 ? -105.491 33.161 3.107   1.00 85.99  ?  236 PHE B CB  1 
ATOM 5249 C CG  . PHE B 1 236 ? -106.577 34.193 3.072   1.00 90.50  ?  236 PHE B CG  1 
ATOM 5250 C CD1 . PHE B 1 236 ? -107.014 34.720 1.869   1.00 83.99  ?  236 PHE B CD1 1 
ATOM 5251 C CD2 . PHE B 1 236 ? -107.153 34.646 4.247   1.00 98.56  ?  236 PHE B CD2 1 
ATOM 5252 C CE1 . PHE B 1 236 ? -108.010 35.673 1.838   1.00 81.60  ?  236 PHE B CE1 1 
ATOM 5253 C CE2 . PHE B 1 236 ? -108.149 35.601 4.222   1.00 106.14 ?  236 PHE B CE2 1 
ATOM 5254 C CZ  . PHE B 1 236 ? -108.577 36.116 3.015   1.00 106.65 ?  236 PHE B CZ  1 
ATOM 5255 N N   . ILE B 1 237 ? -104.193 30.368 3.668   1.00 79.93  ?  237 ILE B N   1 
ATOM 5256 C CA  . ILE B 1 237 ? -102.868 29.759 3.701   1.00 84.83  ?  237 ILE B CA  1 
ATOM 5257 C C   . ILE B 1 237 ? -102.945 28.235 3.816   1.00 103.61 ?  237 ILE B C   1 
ATOM 5258 O O   . ILE B 1 237 ? -102.415 27.516 2.967   1.00 110.87 ?  237 ILE B O   1 
ATOM 5259 C CB  . ILE B 1 237 ? -102.009 30.379 4.826   1.00 88.48  ?  237 ILE B CB  1 
ATOM 5260 C CG1 . ILE B 1 237 ? -100.746 29.568 5.099   1.00 102.17 ?  237 ILE B CG1 1 
ATOM 5261 C CG2 . ILE B 1 237 ? -102.812 30.611 6.095   1.00 97.89  ?  237 ILE B CG2 1 
ATOM 5262 C CD1 . ILE B 1 237 ? -99.860  30.252 6.108   1.00 119.58 ?  237 ILE B CD1 1 
ATOM 5263 N N   . ARG B 1 238 ? -103.620 27.723 4.846   1.00 100.59 ?  238 ARG B N   1 
ATOM 5264 C CA  . ARG B 1 238 ? -103.796 26.275 4.928   1.00 112.19 ?  238 ARG B CA  1 
ATOM 5265 C C   . ARG B 1 238 ? -104.760 25.742 3.871   1.00 121.74 ?  238 ARG B C   1 
ATOM 5266 O O   . ARG B 1 238 ? -104.969 24.526 3.801   1.00 133.02 ?  238 ARG B O   1 
ATOM 5267 C CB  . ARG B 1 238 ? -104.277 25.872 6.326   1.00 129.04 ?  238 ARG B CB  1 
ATOM 5268 C CG  . ARG B 1 238 ? -103.999 24.412 6.680   1.00 142.62 ?  238 ARG B CG  1 
ATOM 5269 C CD  . ARG B 1 238 ? -104.350 24.087 8.122   1.00 142.77 ?  238 ARG B CD  1 
ATOM 5270 N NE  . ARG B 1 238 ? -104.156 22.668 8.406   1.00 152.46 ?  238 ARG B NE  1 
ATOM 5271 C CZ  . ARG B 1 238 ? -104.335 22.107 9.597   1.00 150.80 ?  238 ARG B CZ  1 
ATOM 5272 N NH1 . ARG B 1 238 ? -104.714 22.845 10.631  1.00 120.14 ?  238 ARG B NH1 1 
ATOM 5273 N NH2 . ARG B 1 238 ? -104.131 20.806 9.756   1.00 146.97 ?  238 ARG B NH2 1 
ATOM 5274 N N   . ARG B 1 239 ? -105.343 26.622 3.056   1.00 123.21 ?  239 ARG B N   1 
ATOM 5275 C CA  . ARG B 1 239 ? -106.253 26.193 2.000   1.00 127.89 ?  239 ARG B CA  1 
ATOM 5276 C C   . ARG B 1 239 ? -105.573 25.219 1.044   1.00 132.82 ?  239 ARG B C   1 
ATOM 5277 O O   . ARG B 1 239 ? -106.011 24.074 0.885   1.00 146.05 ?  239 ARG B O   1 
ATOM 5278 C CB  . ARG B 1 239 ? -106.775 27.418 1.246   1.00 124.47 ?  239 ARG B CB  1 
ATOM 5279 C CG  . ARG B 1 239 ? -107.416 27.117 -0.099  1.00 136.74 ?  239 ARG B CG  1 
ATOM 5280 C CD  . ARG B 1 239 ? -106.723 27.902 -1.205  1.00 133.74 ?  239 ARG B CD  1 
ATOM 5281 N NE  . ARG B 1 239 ? -106.862 29.345 -1.033  1.00 129.22 ?  239 ARG B NE  1 
ATOM 5282 C CZ  . ARG B 1 239 ? -107.774 30.089 -1.651  1.00 126.40 ?  239 ARG B CZ  1 
ATOM 5283 N NH1 . ARG B 1 239 ? -108.634 29.529 -2.490  1.00 120.62 ?  239 ARG B NH1 1 
ATOM 5284 N NH2 . ARG B 1 239 ? -107.824 31.396 -1.432  1.00 124.88 ?  239 ARG B NH2 1 
ATOM 5285 N N   . SER B 1 240 ? -104.498 25.661 0.394   1.00 123.99 ?  240 SER B N   1 
ATOM 5286 C CA  . SER B 1 240 ? -103.851 24.877 -0.651  1.00 134.37 ?  240 SER B CA  1 
ATOM 5287 C C   . SER B 1 240 ? -102.405 24.523 -0.337  1.00 135.16 ?  240 SER B C   1 
ATOM 5288 O O   . SER B 1 240 ? -102.039 23.341 -0.384  1.00 145.14 ?  240 SER B O   1 
ATOM 5289 C CB  . SER B 1 240 ? -103.926 25.640 -1.982  1.00 134.35 ?  240 SER B CB  1 
ATOM 5290 O OG  . SER B 1 240 ? -103.371 26.938 -1.855  1.00 143.96 ?  240 SER B OG  1 
ATOM 5291 N N   . VAL B 1 241 ? -101.572 25.509 -0.011  1.00 128.09 ?  241 VAL B N   1 
ATOM 5292 C CA  . VAL B 1 241 ? -100.127 25.311 0.078   1.00 130.46 ?  241 VAL B CA  1 
ATOM 5293 C C   . VAL B 1 241 ? -99.803  24.567 1.373   1.00 131.81 ?  241 VAL B C   1 
ATOM 5294 O O   . VAL B 1 241 ? -99.983  25.103 2.470   1.00 136.59 ?  241 VAL B O   1 
ATOM 5295 C CB  . VAL B 1 241 ? -99.378  26.646 -0.010  1.00 114.47 ?  241 VAL B CB  1 
ATOM 5296 C CG1 . VAL B 1 241 ? -100.028 27.682 0.898   1.00 113.34 ?  241 VAL B CG1 1 
ATOM 5297 C CG2 . VAL B 1 241 ? -97.917  26.462 0.354   1.00 109.90 ?  241 VAL B CG2 1 
ATOM 5298 N N   . ASN B 1 242 ? -99.342  23.318 1.255   1.00 126.87 ?  242 ASN B N   1 
ATOM 5299 C CA  . ASN B 1 242 ? -98.961  22.553 2.438   1.00 125.51 ?  242 ASN B CA  1 
ATOM 5300 C C   . ASN B 1 242 ? -97.487  22.166 2.463   1.00 122.41 ?  242 ASN B C   1 
ATOM 5301 O O   . ASN B 1 242 ? -96.767  22.587 3.374   1.00 135.06 ?  242 ASN B O   1 
ATOM 5302 C CB  . ASN B 1 242 ? -99.843  21.301 2.541   1.00 127.45 ?  242 ASN B CB  1 
ATOM 5303 C CG  . ASN B 1 242 ? -101.278 21.627 2.907   1.00 136.55 ?  242 ASN B CG  1 
ATOM 5304 O OD1 . ASN B 1 242 ? -101.694 21.446 4.051   1.00 147.67 ?  242 ASN B OD1 1 
ATOM 5305 N ND2 . ASN B 1 242 ? -102.043 22.110 1.934   1.00 133.31 ?  242 ASN B ND2 1 
ATOM 5306 N N   . THR B 1 243 ? -97.004  21.385 1.493   1.00 108.79 ?  243 THR B N   1 
ATOM 5307 C CA  . THR B 1 243 ? -95.682  20.768 1.618   1.00 109.82 ?  243 THR B CA  1 
ATOM 5308 C C   . THR B 1 243 ? -94.949  20.708 0.281   1.00 103.83 ?  243 THR B C   1 
ATOM 5309 O O   . THR B 1 243 ? -94.334  19.691 -0.058  1.00 102.22 ?  243 THR B O   1 
ATOM 5310 C CB  . THR B 1 243 ? -95.787  19.369 2.225   1.00 113.97 ?  243 THR B CB  1 
ATOM 5311 O OG1 . THR B 1 243 ? -94.528  18.695 2.101   1.00 104.80 ?  243 THR B OG1 1 
ATOM 5312 C CG2 . THR B 1 243 ? -96.871  18.561 1.521   1.00 120.60 ?  243 THR B CG2 1 
ATOM 5313 N N   . SER B 1 244 ? -94.989  21.781 -0.494  1.00 109.16 ?  244 SER B N   1 
ATOM 5314 C CA  . SER B 1 244 ? -94.236  21.643 -1.733  1.00 94.94  ?  244 SER B CA  1 
ATOM 5315 C C   . SER B 1 244 ? -93.005  22.543 -1.727  1.00 94.42  ?  244 SER B C   1 
ATOM 5316 O O   . SER B 1 244 ? -93.076  23.688 -1.265  1.00 102.39 ?  244 SER B O   1 
ATOM 5317 C CB  . SER B 1 244 ? -95.104  21.973 -2.951  1.00 98.54  ?  244 SER B CB  1 
ATOM 5318 O OG  . SER B 1 244 ? -96.095  20.980 -3.149  1.00 103.27 ?  244 SER B OG  1 
ATOM 5319 N N   . PRO B 1 245 ? -91.866  22.056 -2.231  1.00 85.13  ?  245 PRO B N   1 
ATOM 5320 C CA  . PRO B 1 245 ? -90.629  22.850 -2.176  1.00 95.78  ?  245 PRO B CA  1 
ATOM 5321 C C   . PRO B 1 245 ? -90.644  24.045 -3.116  1.00 92.95  ?  245 PRO B C   1 
ATOM 5322 O O   . PRO B 1 245 ? -89.909  24.074 -4.109  1.00 89.91  ?  245 PRO B O   1 
ATOM 5323 C CB  . PRO B 1 245 ? -89.543  21.842 -2.580  1.00 83.69  ?  245 PRO B CB  1 
ATOM 5324 C CG  . PRO B 1 245 ? -90.179  20.490 -2.430  1.00 89.93  ?  245 PRO B CG  1 
ATOM 5325 C CD  . PRO B 1 245 ? -91.624  20.699 -2.744  1.00 90.83  ?  245 PRO B CD  1 
ATOM 5326 N N   . TYR B 1 246 ? -91.475  25.035 -2.811  1.00 91.85  ?  246 TYR B N   1 
ATOM 5327 C CA  . TYR B 1 246 ? -91.530  26.262 -3.588  1.00 82.96  ?  246 TYR B CA  1 
ATOM 5328 C C   . TYR B 1 246 ? -90.616  27.309 -2.956  1.00 76.57  ?  246 TYR B C   1 
ATOM 5329 O O   . TYR B 1 246 ? -89.863  27.029 -2.020  1.00 71.62  ?  246 TYR B O   1 
ATOM 5330 C CB  . TYR B 1 246 ? -92.968  26.765 -3.691  1.00 86.83  ?  246 TYR B CB  1 
ATOM 5331 C CG  . TYR B 1 246 ? -93.932  25.793 -4.333  1.00 91.47  ?  246 TYR B CG  1 
ATOM 5332 C CD1 . TYR B 1 246 ? -93.500  24.875 -5.281  1.00 88.81  ?  246 TYR B CD1 1 
ATOM 5333 C CD2 . TYR B 1 246 ? -95.279  25.801 -3.996  1.00 98.34  ?  246 TYR B CD2 1 
ATOM 5334 C CE1 . TYR B 1 246 ? -94.383  23.990 -5.872  1.00 93.77  ?  246 TYR B CE1 1 
ATOM 5335 C CE2 . TYR B 1 246 ? -96.168  24.922 -4.580  1.00 97.49  ?  246 TYR B CE2 1 
ATOM 5336 C CZ  . TYR B 1 246 ? -95.716  24.020 -5.519  1.00 89.56  ?  246 TYR B CZ  1 
ATOM 5337 O OH  . TYR B 1 246 ? -96.600  23.140 -6.100  1.00 94.16  ?  246 TYR B OH  1 
ATOM 5338 N N   . ALA B 1 247 ? -90.677  28.534 -3.468  1.00 85.43  ?  247 ALA B N   1 
ATOM 5339 C CA  . ALA B 1 247 ? -89.953  29.672 -2.914  1.00 70.09  ?  247 ALA B CA  1 
ATOM 5340 C C   . ALA B 1 247 ? -90.981  30.644 -2.351  1.00 83.05  ?  247 ALA B C   1 
ATOM 5341 O O   . ALA B 1 247 ? -91.649  31.358 -3.107  1.00 77.38  ?  247 ALA B O   1 
ATOM 5342 C CB  . ALA B 1 247 ? -89.080  30.338 -3.975  1.00 78.09  ?  247 ALA B CB  1 
ATOM 5343 N N   . ARG B 1 248 ? -91.109  30.669 -1.028  1.00 77.76  ?  248 ARG B N   1 
ATOM 5344 C CA  . ARG B 1 248 ? -92.113  31.479 -0.352  1.00 71.25  ?  248 ARG B CA  1 
ATOM 5345 C C   . ARG B 1 248 ? -91.449  32.706 0.258   1.00 75.93  ?  248 ARG B C   1 
ATOM 5346 O O   . ARG B 1 248 ? -90.398  32.595 0.898   1.00 77.89  ?  248 ARG B O   1 
ATOM 5347 C CB  . ARG B 1 248 ? -92.825  30.657 0.723   1.00 60.71  ?  248 ARG B CB  1 
ATOM 5348 C CG  . ARG B 1 248 ? -93.555  29.450 0.157   1.00 68.50  ?  248 ARG B CG  1 
ATOM 5349 C CD  . ARG B 1 248 ? -93.708  28.356 1.194   1.00 74.48  ?  248 ARG B CD  1 
ATOM 5350 N NE  . ARG B 1 248 ? -94.571  27.275 0.725   1.00 77.96  ?  248 ARG B NE  1 
ATOM 5351 C CZ  . ARG B 1 248 ? -94.131  26.205 0.071   1.00 89.76  ?  248 ARG B CZ  1 
ATOM 5352 N NH1 . ARG B 1 248 ? -92.839  26.073 -0.193  1.00 93.99  ?  248 ARG B NH1 1 
ATOM 5353 N NH2 . ARG B 1 248 ? -94.980  25.264 -0.321  1.00 98.45  ?  248 ARG B NH2 1 
ATOM 5354 N N   . PHE B 1 249 ? -92.065  33.870 0.061   1.00 60.50  ?  249 PHE B N   1 
ATOM 5355 C CA  . PHE B 1 249 ? -91.477  35.157 0.428   1.00 55.58  ?  249 PHE B CA  1 
ATOM 5356 C C   . PHE B 1 249 ? -92.395  35.851 1.429   1.00 77.46  ?  249 PHE B C   1 
ATOM 5357 O O   . PHE B 1 249 ? -93.361  36.516 1.044   1.00 88.61  ?  249 PHE B O   1 
ATOM 5358 C CB  . PHE B 1 249 ? -91.256  36.021 -0.815  1.00 64.88  ?  249 PHE B CB  1 
ATOM 5359 C CG  . PHE B 1 249 ? -90.327  35.408 -1.820  1.00 84.40  ?  249 PHE B CG  1 
ATOM 5360 C CD1 . PHE B 1 249 ? -88.980  35.724 -1.824  1.00 91.48  ?  249 PHE B CD1 1 
ATOM 5361 C CD2 . PHE B 1 249 ? -90.804  34.513 -2.764  1.00 78.64  ?  249 PHE B CD2 1 
ATOM 5362 C CE1 . PHE B 1 249 ? -88.124  35.159 -2.748  1.00 83.82  ?  249 PHE B CE1 1 
ATOM 5363 C CE2 . PHE B 1 249 ? -89.953  33.944 -3.691  1.00 81.95  ?  249 PHE B CE2 1 
ATOM 5364 C CZ  . PHE B 1 249 ? -88.612  34.267 -3.683  1.00 84.70  ?  249 PHE B CZ  1 
ATOM 5365 N N   . PHE B 1 250 ? -92.087  35.700 2.715   1.00 75.96  ?  250 PHE B N   1 
ATOM 5366 C CA  . PHE B 1 250 ? -92.852  36.364 3.762   1.00 66.98  ?  250 PHE B CA  1 
ATOM 5367 C C   . PHE B 1 250 ? -92.381  37.802 3.931   1.00 65.18  ?  250 PHE B C   1 
ATOM 5368 O O   . PHE B 1 250 ? -91.195  38.055 4.165   1.00 70.76  ?  250 PHE B O   1 
ATOM 5369 C CB  . PHE B 1 250 ? -92.727  35.606 5.083   1.00 58.91  ?  250 PHE B CB  1 
ATOM 5370 C CG  . PHE B 1 250 ? -93.460  34.299 5.098   1.00 68.29  ?  250 PHE B CG  1 
ATOM 5371 C CD1 . PHE B 1 250 ? -94.694  34.192 5.716   1.00 70.70  ?  250 PHE B CD1 1 
ATOM 5372 C CD2 . PHE B 1 250 ? -92.921  33.177 4.489   1.00 69.49  ?  250 PHE B CD2 1 
ATOM 5373 C CE1 . PHE B 1 250 ? -95.376  32.994 5.730   1.00 76.12  ?  250 PHE B CE1 1 
ATOM 5374 C CE2 . PHE B 1 250 ? -93.599  31.975 4.500   1.00 70.20  ?  250 PHE B CE2 1 
ATOM 5375 C CZ  . PHE B 1 250 ? -94.827  31.885 5.120   1.00 76.24  ?  250 PHE B CZ  1 
ATOM 5376 N N   . ILE B 1 251 ? -93.316  38.743 3.819   1.00 62.64  ?  251 ILE B N   1 
ATOM 5377 C CA  . ILE B 1 251 ? -93.032  40.169 3.921   1.00 65.35  ?  251 ILE B CA  1 
ATOM 5378 C C   . ILE B 1 251 ? -93.831  40.729 5.088   1.00 67.03  ?  251 ILE B C   1 
ATOM 5379 O O   . ILE B 1 251 ? -95.049  40.531 5.164   1.00 74.92  ?  251 ILE B O   1 
ATOM 5380 C CB  . ILE B 1 251 ? -93.375  40.907 2.615   1.00 78.15  ?  251 ILE B CB  1 
ATOM 5381 C CG1 . ILE B 1 251 ? -92.655  40.251 1.436   1.00 76.79  ?  251 ILE B CG1 1 
ATOM 5382 C CG2 . ILE B 1 251 ? -93.002  42.373 2.723   1.00 72.06  ?  251 ILE B CG2 1 
ATOM 5383 C CD1 . ILE B 1 251 ? -93.167  40.690 0.087   1.00 90.30  ?  251 ILE B CD1 1 
ATOM 5384 N N   . LEU B 1 252 ? -93.148  41.426 5.995   1.00 66.21  ?  252 LEU B N   1 
ATOM 5385 C CA  . LEU B 1 252 ? -93.760  41.908 7.224   1.00 69.28  ?  252 LEU B CA  1 
ATOM 5386 C C   . LEU B 1 252 ? -93.368  43.358 7.466   1.00 76.08  ?  252 LEU B C   1 
ATOM 5387 O O   . LEU B 1 252 ? -92.214  43.740 7.256   1.00 93.44  ?  252 LEU B O   1 
ATOM 5388 C CB  . LEU B 1 252 ? -93.340  41.048 8.426   1.00 72.49  ?  252 LEU B CB  1 
ATOM 5389 C CG  . LEU B 1 252 ? -93.491  39.532 8.271   1.00 76.97  ?  252 LEU B CG  1 
ATOM 5390 C CD1 . LEU B 1 252 ? -92.357  38.793 8.966   1.00 77.36  ?  252 LEU B CD1 1 
ATOM 5391 C CD2 . LEU B 1 252 ? -94.833  39.072 8.808   1.00 73.95  ?  252 LEU B CD2 1 
ATOM 5392 N N   . GLU B 1 253 ? -94.336  44.158 7.907   1.00 79.50  ?  253 GLU B N   1 
ATOM 5393 C CA  . GLU B 1 253 ? -94.098  45.539 8.303   1.00 94.00  ?  253 GLU B CA  1 
ATOM 5394 C C   . GLU B 1 253 ? -94.103  45.636 9.823   1.00 111.15 ?  253 GLU B C   1 
ATOM 5395 O O   . GLU B 1 253 ? -94.999  45.097 10.481  1.00 109.88 ?  253 GLU B O   1 
ATOM 5396 C CB  . GLU B 1 253 ? -95.156  46.475 7.715   1.00 94.60  ?  253 GLU B CB  1 
ATOM 5397 C CG  . GLU B 1 253 ? -95.497  47.661 8.610   1.00 98.88  ?  253 GLU B CG  1 
ATOM 5398 C CD  . GLU B 1 253 ? -96.420  48.659 7.943   1.00 119.85 ?  253 GLU B CD  1 
ATOM 5399 O OE1 . GLU B 1 253 ? -95.922  49.513 7.180   1.00 131.12 ?  253 GLU B OE1 1 
ATOM 5400 O OE2 . GLU B 1 253 ? -97.644  48.589 8.181   1.00 115.22 -1 253 GLU B OE2 1 
ATOM 5401 N N   . PHE B 1 254 ? -93.100  46.316 10.374  1.00 110.96 ?  254 PHE B N   1 
ATOM 5402 C CA  . PHE B 1 254 ? -93.048  46.571 11.809  1.00 113.35 ?  254 PHE B CA  1 
ATOM 5403 C C   . PHE B 1 254 ? -92.271  47.857 12.040  1.00 107.33 ?  254 PHE B C   1 
ATOM 5404 O O   . PHE B 1 254 ? -91.122  47.982 11.605  1.00 102.74 ?  254 PHE B O   1 
ATOM 5405 C CB  . PHE B 1 254 ? -92.423  45.389 12.568  1.00 125.49 ?  254 PHE B CB  1 
ATOM 5406 C CG  . PHE B 1 254 ? -90.928  45.276 12.424  1.00 113.06 ?  254 PHE B CG  1 
ATOM 5407 C CD1 . PHE B 1 254 ? -90.351  45.015 11.191  1.00 93.79  ?  254 PHE B CD1 1 
ATOM 5408 C CD2 . PHE B 1 254 ? -90.102  45.420 13.527  1.00 104.94 ?  254 PHE B CD2 1 
ATOM 5409 C CE1 . PHE B 1 254 ? -88.979  44.912 11.062  1.00 107.02 ?  254 PHE B CE1 1 
ATOM 5410 C CE2 . PHE B 1 254 ? -88.730  45.315 13.403  1.00 100.13 ?  254 PHE B CE2 1 
ATOM 5411 C CZ  . PHE B 1 254 ? -88.169  45.060 12.169  1.00 108.50 ?  254 PHE B CZ  1 
ATOM 5412 N N   . GLN B 1 255 ? -92.911  48.824 12.692  1.00 107.27 ?  255 GLN B N   1 
ATOM 5413 C CA  . GLN B 1 255 ? -92.265  50.095 12.976  1.00 127.51 ?  255 GLN B CA  1 
ATOM 5414 C C   . GLN B 1 255 ? -91.241  49.918 14.094  1.00 128.95 ?  255 GLN B C   1 
ATOM 5415 O O   . GLN B 1 255 ? -91.060  48.829 14.647  1.00 110.11 ?  255 GLN B O   1 
ATOM 5416 C CB  . GLN B 1 255 ? -93.303  51.155 13.339  1.00 124.36 ?  255 GLN B CB  1 
ATOM 5417 C CG  . GLN B 1 255 ? -94.166  51.627 12.172  1.00 121.71 ?  255 GLN B CG  1 
ATOM 5418 C CD  . GLN B 1 255 ? -95.144  50.573 11.693  1.00 122.15 ?  255 GLN B CD  1 
ATOM 5419 O OE1 . GLN B 1 255 ? -95.281  50.336 10.493  1.00 121.17 ?  255 GLN B OE1 1 
ATOM 5420 N NE2 . GLN B 1 255 ? -95.833  49.934 12.632  1.00 105.21 ?  255 GLN B NE2 1 
ATOM 5421 N N   . ASP B 1 256 ? -90.561  51.010 14.439  1.00 127.48 ?  256 ASP B N   1 
ATOM 5422 C CA  . ASP B 1 256 ? -89.573  50.951 15.508  1.00 125.13 ?  256 ASP B CA  1 
ATOM 5423 C C   . ASP B 1 256 ? -90.263  51.072 16.860  1.00 121.41 ?  256 ASP B C   1 
ATOM 5424 O O   . ASP B 1 256 ? -89.862  51.878 17.706  1.00 136.51 ?  256 ASP B O   1 
ATOM 5425 C CB  . ASP B 1 256 ? -88.525  52.051 15.330  1.00 137.75 ?  256 ASP B CB  1 
ATOM 5426 C CG  . ASP B 1 256 ? -87.763  51.920 14.025  1.00 132.96 ?  256 ASP B CG  1 
ATOM 5427 O OD1 . ASP B 1 256 ? -87.249  50.817 13.743  1.00 124.44 ?  256 ASP B OD1 1 
ATOM 5428 O OD2 . ASP B 1 256 ? -87.680  52.919 13.280  1.00 128.41 -1 256 ASP B OD2 1 
ATOM 5429 N N   . LYS B 1 257 ? -91.306  50.265 17.066  1.00 107.63 ?  257 LYS B N   1 
ATOM 5430 C CA  . LYS B 1 257 ? -92.027  50.235 18.331  1.00 110.30 ?  257 LYS B CA  1 
ATOM 5431 C C   . LYS B 1 257 ? -92.461  48.824 18.708  1.00 98.60  ?  257 LYS B C   1 
ATOM 5432 O O   . LYS B 1 257 ? -93.251  48.666 19.648  1.00 106.76 ?  257 LYS B O   1 
ATOM 5433 C CB  . LYS B 1 257 ? -93.248  51.164 18.273  1.00 126.57 ?  257 LYS B CB  1 
ATOM 5434 C CG  . LYS B 1 257 ? -94.155  50.925 17.074  1.00 131.03 ?  257 LYS B CG  1 
ATOM 5435 C CD  . LYS B 1 257 ? -95.191  52.031 16.935  1.00 135.78 ?  257 LYS B CD  1 
ATOM 5436 C CE  . LYS B 1 257 ? -96.077  51.809 15.718  1.00 136.83 ?  257 LYS B CE  1 
ATOM 5437 N NZ  . LYS B 1 257 ? -97.039  52.928 15.513  1.00 134.02 ?  257 LYS B NZ  1 
ATOM 5438 N N   . THR B 1 258 ? -91.976  47.802 18.010  1.00 103.24 ?  258 THR B N   1 
ATOM 5439 C CA  . THR B 1 258 ? -92.386  46.423 18.227  1.00 91.06  ?  258 THR B CA  1 
ATOM 5440 C C   . THR B 1 258 ? -91.287  45.666 18.962  1.00 80.82  ?  258 THR B C   1 
ATOM 5441 O O   . THR B 1 258 ? -90.097  45.872 18.703  1.00 89.24  ?  258 THR B O   1 
ATOM 5442 C CB  . THR B 1 258 ? -92.698  45.729 16.895  1.00 77.90  ?  258 THR B CB  1 
ATOM 5443 O OG1 . THR B 1 258 ? -93.620  46.528 16.144  1.00 108.67 ?  258 THR B OG1 1 
ATOM 5444 C CG2 . THR B 1 258 ? -93.311  44.356 17.132  1.00 86.35  ?  258 THR B CG2 1 
ATOM 5445 N N   . ASP B 1 259 ? -91.695  44.797 19.883  1.00 82.61  ?  259 ASP B N   1 
ATOM 5446 C CA  . ASP B 1 259 ? -90.740  43.975 20.612  1.00 77.85  ?  259 ASP B CA  1 
ATOM 5447 C C   . ASP B 1 259 ? -90.033  43.015 19.662  1.00 91.52  ?  259 ASP B C   1 
ATOM 5448 O O   . ASP B 1 259 ? -90.647  42.442 18.758  1.00 97.32  ?  259 ASP B O   1 
ATOM 5449 C CB  . ASP B 1 259 ? -91.455  43.196 21.717  1.00 86.63  ?  259 ASP B CB  1 
ATOM 5450 C CG  . ASP B 1 259 ? -90.504  42.373 22.563  1.00 95.13  ?  259 ASP B CG  1 
ATOM 5451 O OD1 . ASP B 1 259 ? -89.279  42.610 22.496  1.00 108.18 ?  259 ASP B OD1 1 
ATOM 5452 O OD2 . ASP B 1 259 ? -90.983  41.483 23.295  1.00 100.19 -1 259 ASP B OD2 1 
ATOM 5453 N N   . ILE B 1 260 ? -88.727  42.844 19.873  1.00 84.55  ?  260 ILE B N   1 
ATOM 5454 C CA  . ILE B 1 260 ? -87.956  41.925 19.041  1.00 70.29  ?  260 ILE B CA  1 
ATOM 5455 C C   . ILE B 1 260 ? -88.360  40.482 19.321  1.00 87.83  ?  260 ILE B C   1 
ATOM 5456 O O   . ILE B 1 260 ? -88.509  39.676 18.395  1.00 83.94  ?  260 ILE B O   1 
ATOM 5457 C CB  . ILE B 1 260 ? -86.447  42.147 19.254  1.00 83.11  ?  260 ILE B CB  1 
ATOM 5458 C CG1 . ILE B 1 260 ? -86.051  43.560 18.820  1.00 82.69  ?  260 ILE B CG1 1 
ATOM 5459 C CG2 . ILE B 1 260 ? -85.637  41.112 18.492  1.00 87.43  ?  260 ILE B CG2 1 
ATOM 5460 C CD1 . ILE B 1 260 ? -84.583  43.872 19.016  1.00 81.32  ?  260 ILE B CD1 1 
ATOM 5461 N N   . LYS B 1 261 ? -88.544  40.135 20.600  1.00 86.43  ?  261 LYS B N   1 
ATOM 5462 C CA  . LYS B 1 261 ? -88.992  38.791 20.955  1.00 82.30  ?  261 LYS B CA  1 
ATOM 5463 C C   . LYS B 1 261 ? -90.331  38.461 20.308  1.00 90.21  ?  261 LYS B C   1 
ATOM 5464 O O   . LYS B 1 261 ? -90.607  37.293 20.007  1.00 100.47 ?  261 LYS B O   1 
ATOM 5465 C CB  . LYS B 1 261 ? -89.079  38.662 22.477  1.00 72.77  ?  261 LYS B CB  1 
ATOM 5466 C CG  . LYS B 1 261 ? -89.696  37.366 22.979  1.00 79.38  ?  261 LYS B CG  1 
ATOM 5467 C CD  . LYS B 1 261 ? -88.839  36.162 22.628  1.00 80.01  ?  261 LYS B CD  1 
ATOM 5468 C CE  . LYS B 1 261 ? -89.442  34.888 23.197  1.00 80.13  ?  261 LYS B CE  1 
ATOM 5469 N NZ  . LYS B 1 261 ? -88.629  33.687 22.865  1.00 104.28 ?  261 LYS B NZ  1 
ATOM 5470 N N   . THR B 1 262 ? -91.169  39.473 20.079  1.00 72.30  ?  262 THR B N   1 
ATOM 5471 C CA  . THR B 1 262 ? -92.405  39.261 19.336  1.00 95.49  ?  262 THR B CA  1 
ATOM 5472 C C   . THR B 1 262 ? -92.123  38.887 17.886  1.00 86.46  ?  262 THR B C   1 
ATOM 5473 O O   . THR B 1 262 ? -92.901  38.150 17.270  1.00 87.97  ?  262 THR B O   1 
ATOM 5474 C CB  . THR B 1 262 ? -93.274  40.518 19.405  1.00 93.76  ?  262 THR B CB  1 
ATOM 5475 O OG1 . THR B 1 262 ? -93.523  40.850 20.777  1.00 96.92  ?  262 THR B OG1 1 
ATOM 5476 C CG2 . THR B 1 262 ? -94.607  40.298 18.705  1.00 95.93  ?  262 THR B CG2 1 
ATOM 5477 N N   . VAL B 1 263 ? -91.010  39.367 17.330  1.00 76.30  ?  263 VAL B N   1 
ATOM 5478 C CA  . VAL B 1 263 ? -90.706  39.090 15.931  1.00 80.83  ?  263 VAL B CA  1 
ATOM 5479 C C   . VAL B 1 263 ? -90.042  37.727 15.777  1.00 78.66  ?  263 VAL B C   1 
ATOM 5480 O O   . VAL B 1 263 ? -90.384  36.960 14.870  1.00 83.69  ?  263 VAL B O   1 
ATOM 5481 C CB  . VAL B 1 263 ? -89.835  40.214 15.346  1.00 67.00  ?  263 VAL B CB  1 
ATOM 5482 C CG1 . VAL B 1 263 ? -89.615  39.988 13.858  1.00 68.88  ?  263 VAL B CG1 1 
ATOM 5483 C CG2 . VAL B 1 263 ? -90.477  41.572 15.601  1.00 75.78  ?  263 VAL B CG2 1 
ATOM 5484 N N   . LYS B 1 264 ? -89.090  37.403 16.656  1.00 64.32  ?  264 LYS B N   1 
ATOM 5485 C CA  . LYS B 1 264 ? -88.368  36.140 16.531  1.00 65.85  ?  264 LYS B CA  1 
ATOM 5486 C C   . LYS B 1 264 ? -89.298  34.946 16.713  1.00 74.47  ?  264 LYS B C   1 
ATOM 5487 O O   . LYS B 1 264 ? -89.166  33.937 16.011  1.00 81.13  ?  264 LYS B O   1 
ATOM 5488 C CB  . LYS B 1 264 ? -87.220  36.091 17.538  1.00 63.79  ?  264 LYS B CB  1 
ATOM 5489 C CG  . LYS B 1 264 ? -85.960  36.797 17.066  1.00 66.73  ?  264 LYS B CG  1 
ATOM 5490 C CD  . LYS B 1 264 ? -85.226  37.465 18.216  1.00 84.76  ?  264 LYS B CD  1 
ATOM 5491 C CE  . LYS B 1 264 ? -84.973  36.491 19.354  1.00 90.36  ?  264 LYS B CE  1 
ATOM 5492 N NZ  . LYS B 1 264 ? -84.197  37.120 20.458  1.00 67.85  ?  264 LYS B NZ  1 
ATOM 5493 N N   . ASP B 1 265 ? -90.251  35.043 17.645  1.00 90.21  ?  265 ASP B N   1 
ATOM 5494 C CA  . ASP B 1 265 ? -91.204  33.954 17.842  1.00 89.91  ?  265 ASP B CA  1 
ATOM 5495 C C   . ASP B 1 265 ? -92.066  33.733 16.605  1.00 74.56  ?  265 ASP B C   1 
ATOM 5496 O O   . ASP B 1 265 ? -92.565  32.623 16.387  1.00 80.60  ?  265 ASP B O   1 
ATOM 5497 C CB  . ASP B 1 265 ? -92.082  34.236 19.063  1.00 111.84 ?  265 ASP B CB  1 
ATOM 5498 C CG  . ASP B 1 265 ? -91.385  33.908 20.371  1.00 106.45 ?  265 ASP B CG  1 
ATOM 5499 O OD1 . ASP B 1 265 ? -90.221  33.458 20.332  1.00 106.24 ?  265 ASP B OD1 1 
ATOM 5500 O OD2 . ASP B 1 265 ? -92.003  34.104 21.440  1.00 115.57 -1 265 ASP B OD2 1 
ATOM 5501 N N   . CYS B 1 266 ? -92.253  34.771 15.787  1.00 71.67  ?  266 CYS B N   1 
ATOM 5502 C CA  . CYS B 1 266 ? -92.954  34.610 14.518  1.00 79.15  ?  266 CYS B CA  1 
ATOM 5503 C C   . CYS B 1 266 ? -92.046  33.983 13.467  1.00 69.75  ?  266 CYS B C   1 
ATOM 5504 O O   . CYS B 1 266 ? -92.446  33.044 12.771  1.00 86.09  ?  266 CYS B O   1 
ATOM 5505 C CB  . CYS B 1 266 ? -93.483  35.960 14.033  1.00 74.66  ?  266 CYS B CB  1 
ATOM 5506 S SG  . CYS B 1 266 ? -94.062  35.965 12.319  1.00 103.12 ?  266 CYS B SG  1 
ATOM 5507 N N   . ILE B 1 267 ? -90.819  34.497 13.340  1.00 72.19  ?  267 ILE B N   1 
ATOM 5508 C CA  . ILE B 1 267 ? -89.853  33.927 12.403  1.00 77.63  ?  267 ILE B CA  1 
ATOM 5509 C C   . ILE B 1 267 ? -89.612  32.456 12.713  1.00 84.58  ?  267 ILE B C   1 
ATOM 5510 O O   . ILE B 1 267 ? -89.561  31.615 11.806  1.00 94.74  ?  267 ILE B O   1 
ATOM 5511 C CB  . ILE B 1 267 ? -88.540  34.732 12.436  1.00 74.67  ?  267 ILE B CB  1 
ATOM 5512 C CG1 . ILE B 1 267 ? -88.756  36.135 11.869  1.00 83.53  ?  267 ILE B CG1 1 
ATOM 5513 C CG2 . ILE B 1 267 ? -87.439  33.997 11.686  1.00 75.62  ?  267 ILE B CG2 1 
ATOM 5514 C CD1 . ILE B 1 267 ? -87.537  37.022 11.974  1.00 72.53  ?  267 ILE B CD1 1 
ATOM 5515 N N   . TYR B 1 268 ? -89.451  32.124 13.996  1.00 72.82  ?  268 TYR B N   1 
ATOM 5516 C CA  . TYR B 1 268 ? -89.268  30.729 14.382  1.00 73.59  ?  268 TYR B CA  1 
ATOM 5517 C C   . TYR B 1 268 ? -90.459  29.881 13.957  1.00 80.11  ?  268 TYR B C   1 
ATOM 5518 O O   . TYR B 1 268 ? -90.288  28.753 13.480  1.00 88.91  ?  268 TYR B O   1 
ATOM 5519 C CB  . TYR B 1 268 ? -89.042  30.626 15.891  1.00 78.88  ?  268 TYR B CB  1 
ATOM 5520 C CG  . TYR B 1 268 ? -87.587  30.700 16.299  1.00 74.68  ?  268 TYR B CG  1 
ATOM 5521 C CD1 . TYR B 1 268 ? -86.795  29.560 16.332  1.00 79.55  ?  268 TYR B CD1 1 
ATOM 5522 C CD2 . TYR B 1 268 ? -87.005  31.911 16.652  1.00 72.47  ?  268 TYR B CD2 1 
ATOM 5523 C CE1 . TYR B 1 268 ? -85.466  29.624 16.704  1.00 83.05  ?  268 TYR B CE1 1 
ATOM 5524 C CE2 . TYR B 1 268 ? -85.677  31.986 17.025  1.00 64.65  ?  268 TYR B CE2 1 
ATOM 5525 C CZ  . TYR B 1 268 ? -84.913  30.839 17.049  1.00 69.43  ?  268 TYR B CZ  1 
ATOM 5526 O OH  . TYR B 1 268 ? -83.590  30.908 17.420  1.00 82.66  ?  268 TYR B OH  1 
ATOM 5527 N N   . LYS B 1 269 ? -91.676  30.408 14.115  1.00 78.33  ?  269 LYS B N   1 
ATOM 5528 C CA  . LYS B 1 269 ? -92.855  29.674 13.668  1.00 81.34  ?  269 LYS B CA  1 
ATOM 5529 C C   . LYS B 1 269 ? -92.889  29.561 12.149  1.00 75.37  ?  269 LYS B C   1 
ATOM 5530 O O   . LYS B 1 269 ? -93.248  28.509 11.608  1.00 72.57  ?  269 LYS B O   1 
ATOM 5531 C CB  . LYS B 1 269 ? -94.127  30.344 14.188  1.00 79.25  ?  269 LYS B CB  1 
ATOM 5532 C CG  . LYS B 1 269 ? -95.409  29.680 13.710  1.00 80.67  ?  269 LYS B CG  1 
ATOM 5533 C CD  . LYS B 1 269 ? -96.328  29.331 14.871  1.00 88.06  ?  269 LYS B CD  1 
ATOM 5534 C CE  . LYS B 1 269 ? -97.505  28.487 14.405  1.00 109.67 ?  269 LYS B CE  1 
ATOM 5535 N NZ  . LYS B 1 269 ? -98.401  28.101 15.531  1.00 115.91 ?  269 LYS B NZ  1 
ATOM 5536 N N   . ILE B 1 270 ? -92.522  30.634 11.444  1.00 77.85  ?  270 ILE B N   1 
ATOM 5537 C CA  . ILE B 1 270 ? -92.426  30.572 9.987   1.00 74.63  ?  270 ILE B CA  1 
ATOM 5538 C C   . ILE B 1 270 ? -91.401  29.526 9.570   1.00 79.74  ?  270 ILE B C   1 
ATOM 5539 O O   . ILE B 1 270 ? -91.686  28.637 8.759   1.00 90.53  ?  270 ILE B O   1 
ATOM 5540 C CB  . ILE B 1 270 ? -92.084  31.957 9.408   1.00 72.25  ?  270 ILE B CB  1 
ATOM 5541 C CG1 . ILE B 1 270 ? -93.187  32.965 9.732   1.00 73.69  ?  270 ILE B CG1 1 
ATOM 5542 C CG2 . ILE B 1 270 ? -91.870  31.865 7.904   1.00 76.77  ?  270 ILE B CG2 1 
ATOM 5543 C CD1 . ILE B 1 270 ? -92.890  34.369 9.252   1.00 48.71  ?  270 ILE B CD1 1 
ATOM 5544 N N   . GLN B 1 271 ? -90.190  29.613 10.125  1.00 80.71  ?  271 GLN B N   1 
ATOM 5545 C CA  . GLN B 1 271 ? -89.147  28.658 9.766   1.00 87.68  ?  271 GLN B CA  1 
ATOM 5546 C C   . GLN B 1 271 ? -89.535  27.234 10.146  1.00 87.12  ?  271 GLN B C   1 
ATOM 5547 O O   . GLN B 1 271 ? -89.168  26.284 9.445   1.00 87.08  ?  271 GLN B O   1 
ATOM 5548 C CB  . GLN B 1 271 ? -87.824  29.061 10.425  1.00 71.87  ?  271 GLN B CB  1 
ATOM 5549 C CG  . GLN B 1 271 ? -86.655  28.121 10.154  1.00 74.71  ?  271 GLN B CG  1 
ATOM 5550 C CD  . GLN B 1 271 ? -86.571  26.980 11.149  1.00 100.84 ?  271 GLN B CD  1 
ATOM 5551 O OE1 . GLN B 1 271 ? -87.078  27.075 12.266  1.00 111.43 ?  271 GLN B OE1 1 
ATOM 5552 N NE2 . GLN B 1 271 ? -85.931  25.889 10.743  1.00 100.44 ?  271 GLN B NE2 1 
ATOM 5553 N N   . SER B 1 272 ? -90.284  27.062 11.235  1.00 88.50  ?  272 SER B N   1 
ATOM 5554 C CA  . SER B 1 272 ? -90.697  25.731 11.664  1.00 84.99  ?  272 SER B CA  1 
ATOM 5555 C C   . SER B 1 272 ? -91.868  25.179 10.861  1.00 83.08  ?  272 SER B C   1 
ATOM 5556 O O   . SER B 1 272 ? -92.153  23.981 10.962  1.00 104.24 ?  272 SER B O   1 
ATOM 5557 C CB  . SER B 1 272 ? -91.063  25.742 13.150  1.00 86.00  ?  272 SER B CB  1 
ATOM 5558 O OG  . SER B 1 272 ? -91.561  24.482 13.563  1.00 99.49  ?  272 SER B OG  1 
ATOM 5559 N N   . ASN B 1 273 ? -92.552  26.012 10.074  1.00 84.04  ?  273 ASN B N   1 
ATOM 5560 C CA  . ASN B 1 273 ? -93.693  25.567 9.287   1.00 76.69  ?  273 ASN B CA  1 
ATOM 5561 C C   . ASN B 1 273 ? -93.431  25.549 7.789   1.00 84.88  ?  273 ASN B C   1 
ATOM 5562 O O   . ASN B 1 273 ? -94.253  25.005 7.043   1.00 93.29  ?  273 ASN B O   1 
ATOM 5563 C CB  . ASN B 1 273 ? -94.917  26.451 9.570   1.00 76.69  ?  273 ASN B CB  1 
ATOM 5564 C CG  . ASN B 1 273 ? -95.354  26.402 11.021  1.00 81.49  ?  273 ASN B CG  1 
ATOM 5565 O OD1 . ASN B 1 273 ? -95.950  27.350 11.532  1.00 92.21  ?  273 ASN B OD1 1 
ATOM 5566 N ND2 . ASN B 1 273 ? -95.056  25.297 11.694  1.00 84.53  ?  273 ASN B ND2 1 
ATOM 5567 N N   . TRP B 1 274 ? -92.323  26.123 7.326   1.00 81.39  ?  274 TRP B N   1 
ATOM 5568 C CA  . TRP B 1 274 ? -92.006  26.188 5.904   1.00 84.00  ?  274 TRP B CA  1 
ATOM 5569 C C   . TRP B 1 274 ? -90.597  25.687 5.638   1.00 95.56  ?  274 TRP B C   1 
ATOM 5570 O O   . TRP B 1 274 ? -89.885  26.202 4.771   1.00 95.10  ?  274 TRP B O   1 
ATOM 5571 C CB  . TRP B 1 274 ? -92.191  27.606 5.371   1.00 87.38  ?  274 TRP B CB  1 
ATOM 5572 C CG  . TRP B 1 274 ? -93.501  28.186 5.761   1.00 102.66 ?  274 TRP B CG  1 
ATOM 5573 C CD1 . TRP B 1 274 ? -93.753  29.025 6.806   1.00 94.12  ?  274 TRP B CD1 1 
ATOM 5574 C CD2 . TRP B 1 274 ? -94.761  27.937 5.134   1.00 113.60 ?  274 TRP B CD2 1 
ATOM 5575 N NE1 . TRP B 1 274 ? -95.089  29.328 6.858   1.00 88.33  ?  274 TRP B NE1 1 
ATOM 5576 C CE2 . TRP B 1 274 ? -95.730  28.672 5.840   1.00 97.94  ?  274 TRP B CE2 1 
ATOM 5577 C CE3 . TRP B 1 274 ? -95.162  27.169 4.038   1.00 110.53 ?  274 TRP B CE3 1 
ATOM 5578 C CZ2 . TRP B 1 274 ? -97.070  28.663 5.485   1.00 87.18  ?  274 TRP B CZ2 1 
ATOM 5579 C CZ3 . TRP B 1 274 ? -96.496  27.164 3.686   1.00 98.13  ?  274 TRP B CZ3 1 
ATOM 5580 C CH2 . TRP B 1 274 ? -97.435  27.906 4.407   1.00 98.78  ?  274 TRP B CH2 1 
ATOM 5581 N N   . SER B 1 275 ? -90.176  24.664 6.376   1.00 91.22  ?  275 SER B N   1 
ATOM 5582 C CA  . SER B 1 275 ? -88.873  24.050 6.177   1.00 78.89  ?  275 SER B CA  1 
ATOM 5583 C C   . SER B 1 275 ? -89.010  22.546 6.342   1.00 93.40  ?  275 SER B C   1 
ATOM 5584 O O   . SER B 1 275 ? -89.592  22.077 7.324   1.00 98.22  ?  275 SER B O   1 
ATOM 5585 C CB  . SER B 1 275 ? -87.837  24.598 7.164   1.00 79.19  ?  275 SER B CB  1 
ATOM 5586 O OG  . SER B 1 275 ? -87.884  26.013 7.217   1.00 91.82  ?  275 SER B OG  1 
ATOM 5587 N N   . ASN B 1 276 ? -88.481  21.801 5.378   1.00 92.18  ?  276 ASN B N   1 
ATOM 5588 C CA  . ASN B 1 276 ? -88.420  20.345 5.429   1.00 105.72 ?  276 ASN B CA  1 
ATOM 5589 C C   . ASN B 1 276 ? -86.980  19.891 5.250   1.00 108.11 ?  276 ASN B C   1 
ATOM 5590 O O   . ASN B 1 276 ? -86.668  18.992 4.467   1.00 123.65 ?  276 ASN B O   1 
ATOM 5591 C CB  . ASN B 1 276 ? -89.330  19.712 4.379   1.00 108.25 ?  276 ASN B CB  1 
ATOM 5592 C CG  . ASN B 1 276 ? -89.655  18.260 4.685   1.00 120.23 ?  276 ASN B CG  1 
ATOM 5593 O OD1 . ASN B 1 276 ? -89.431  17.781 5.797   1.00 116.62 ?  276 ASN B OD1 1 
ATOM 5594 N ND2 . ASN B 1 276 ? -90.186  17.552 3.695   1.00 121.83 ?  276 ASN B ND2 1 
ATOM 5595 N N   . LEU B 1 277 ? -86.075  20.534 5.987   1.00 101.41 ?  277 LEU B N   1 
ATOM 5596 C CA  . LEU B 1 277 ? -84.658  20.205 5.928   1.00 104.18 ?  277 LEU B CA  1 
ATOM 5597 C C   . LEU B 1 277 ? -84.375  18.973 6.775   1.00 90.16  ?  277 LEU B C   1 
ATOM 5598 O O   . LEU B 1 277 ? -83.493  18.994 7.639   1.00 84.46  ?  277 LEU B O   1 
ATOM 5599 C CB  . LEU B 1 277 ? -83.814  21.388 6.408   1.00 97.19  ?  277 LEU B CB  1 
ATOM 5600 C CG  . LEU B 1 277 ? -84.126  22.744 5.774   1.00 90.88  ?  277 LEU B CG  1 
ATOM 5601 C CD1 . LEU B 1 277 ? -84.038  23.847 6.817   1.00 81.20  ?  277 LEU B CD1 1 
ATOM 5602 C CD2 . LEU B 1 277 ? -83.195  23.029 4.607   1.00 92.19  ?  277 LEU B CD2 1 
ATOM 5603 N N   . SER B 1 278 ? -85.115  17.896 6.531   1.00 115.55 ?  278 SER B N   1 
ATOM 5604 C CA  . SER B 1 278 ? -85.002  16.682 7.327   1.00 117.43 ?  278 SER B CA  1 
ATOM 5605 C C   . SER B 1 278 ? -83.777  15.886 6.886   1.00 115.46 ?  278 SER B C   1 
ATOM 5606 O O   . SER B 1 278 ? -82.979  16.325 6.055   1.00 103.90 ?  278 SER B O   1 
ATOM 5607 C CB  . SER B 1 278 ? -86.284  15.861 7.220   1.00 114.71 ?  278 SER B CB  1 
ATOM 5608 O OG  . SER B 1 278 ? -86.529  15.478 5.878   1.00 112.20 ?  278 SER B OG  1 
ATOM 5609 N N   . LYS B 1 279 ? -83.621  14.691 7.449   1.00 131.36 ?  279 LYS B N   1 
ATOM 5610 C CA  . LYS B 1 279 ? -82.506  13.812 7.132   1.00 136.49 ?  279 LYS B CA  1 
ATOM 5611 C C   . LYS B 1 279 ? -82.759  12.962 5.895   1.00 129.92 ?  279 LYS B C   1 
ATOM 5612 O O   . LYS B 1 279 ? -81.796  12.527 5.251   1.00 120.40 ?  279 LYS B O   1 
ATOM 5613 C CB  . LYS B 1 279 ? -82.212  12.893 8.326   1.00 126.15 ?  279 LYS B CB  1 
ATOM 5614 C CG  . LYS B 1 279 ? -82.284  13.593 9.674   1.00 119.82 ?  279 LYS B CG  1 
ATOM 5615 C CD  . LYS B 1 279 ? -82.999  12.735 10.707  1.00 129.43 ?  279 LYS B CD  1 
ATOM 5616 C CE  . LYS B 1 279 ? -83.230  13.507 11.991  1.00 139.22 ?  279 LYS B CE  1 
ATOM 5617 N NZ  . LYS B 1 279 ? -83.998  12.709 12.978  1.00 125.14 ?  279 LYS B NZ  1 
ATOM 5618 N N   . ARG B 1 280 ? -84.023  12.719 5.552   1.00 136.14 ?  280 ARG B N   1 
ATOM 5619 C CA  . ARG B 1 280 ? -84.384  11.834 4.453   1.00 136.67 ?  280 ARG B CA  1 
ATOM 5620 C C   . ARG B 1 280 ? -84.699  12.567 3.159   1.00 132.11 ?  280 ARG B C   1 
ATOM 5621 O O   . ARG B 1 280 ? -84.514  11.998 2.079   1.00 144.19 ?  280 ARG B O   1 
ATOM 5622 C CB  . ARG B 1 280 ? -85.600  10.988 4.844   1.00 142.62 ?  280 ARG B CB  1 
ATOM 5623 C CG  . ARG B 1 280 ? -86.842  11.825 5.115   1.00 133.97 ?  280 ARG B CG  1 
ATOM 5624 C CD  . ARG B 1 280 ? -88.094  10.989 5.310   1.00 127.67 ?  280 ARG B CD  1 
ATOM 5625 N NE  . ARG B 1 280 ? -89.301  11.805 5.193   1.00 135.53 ?  280 ARG B NE  1 
ATOM 5626 C CZ  . ARG B 1 280 ? -89.785  12.571 6.167   1.00 142.49 ?  280 ARG B CZ  1 
ATOM 5627 N NH1 . ARG B 1 280 ? -89.166  12.633 7.338   1.00 134.25 ?  280 ARG B NH1 1 
ATOM 5628 N NH2 . ARG B 1 280 ? -90.889  13.279 5.970   1.00 137.16 ?  280 ARG B NH2 1 
ATOM 5629 N N   . THR B 1 281 ? -85.172  13.809 3.243   1.00 131.49 ?  281 THR B N   1 
ATOM 5630 C CA  . THR B 1 281 ? -85.724  14.486 2.078   1.00 133.55 ?  281 THR B CA  1 
ATOM 5631 C C   . THR B 1 281 ? -84.626  14.850 1.087   1.00 130.17 ?  281 THR B C   1 
ATOM 5632 O O   . THR B 1 281 ? -83.651  15.521 1.438   1.00 132.11 ?  281 THR B O   1 
ATOM 5633 C CB  . THR B 1 281 ? -86.481  15.740 2.510   1.00 128.10 ?  281 THR B CB  1 
ATOM 5634 O OG1 . THR B 1 281 ? -87.451  15.394 3.505   1.00 133.05 ?  281 THR B OG1 1 
ATOM 5635 C CG2 . THR B 1 281 ? -87.191  16.366 1.322   1.00 117.11 ?  281 THR B CG2 1 
ATOM 5636 N N   . ASP B 1 282 ? -84.792  14.402 -0.154  1.00 129.84 ?  282 ASP B N   1 
ATOM 5637 C CA  . ASP B 1 282 ? -83.901  14.766 -1.245  1.00 141.59 ?  282 ASP B CA  1 
ATOM 5638 C C   . ASP B 1 282 ? -84.362  16.024 -1.970  1.00 134.89 ?  282 ASP B C   1 
ATOM 5639 O O   . ASP B 1 282 ? -83.670  16.491 -2.880  1.00 143.15 ?  282 ASP B O   1 
ATOM 5640 C CB  . ASP B 1 282 ? -83.784  13.598 -2.234  1.00 159.54 ?  282 ASP B CB  1 
ATOM 5641 C CG  . ASP B 1 282 ? -82.462  13.590 -2.984  1.00 177.17 ?  282 ASP B CG  1 
ATOM 5642 O OD1 . ASP B 1 282 ? -82.299  14.392 -3.927  1.00 174.26 ?  282 ASP B OD1 1 
ATOM 5643 O OD2 . ASP B 1 282 ? -81.582  12.779 -2.626  1.00 195.65 -1 282 ASP B OD2 1 
ATOM 5644 N N   . ARG B 1 283 ? -85.507  16.584 -1.582  1.00 133.51 ?  283 ARG B N   1 
ATOM 5645 C CA  . ARG B 1 283 ? -86.042  17.812 -2.170  1.00 126.06 ?  283 ARG B CA  1 
ATOM 5646 C C   . ARG B 1 283 ? -86.370  18.792 -1.048  1.00 116.01 ?  283 ARG B C   1 
ATOM 5647 O O   . ARG B 1 283 ? -87.543  19.041 -0.746  1.00 117.72 ?  283 ARG B O   1 
ATOM 5648 C CB  . ARG B 1 283 ? -87.278  17.515 -3.022  1.00 133.71 ?  283 ARG B CB  1 
ATOM 5649 C CG  . ARG B 1 283 ? -87.014  16.608 -4.217  1.00 146.65 ?  283 ARG B CG  1 
ATOM 5650 C CD  . ARG B 1 283 ? -88.284  16.358 -5.021  1.00 147.32 ?  283 ARG B CD  1 
ATOM 5651 N NE  . ARG B 1 283 ? -87.997  15.841 -6.357  1.00 156.06 ?  283 ARG B NE  1 
ATOM 5652 C CZ  . ARG B 1 283 ? -88.921  15.614 -7.286  1.00 153.34 ?  283 ARG B CZ  1 
ATOM 5653 N NH1 . ARG B 1 283 ? -90.198  15.857 -7.027  1.00 145.97 ?  283 ARG B NH1 1 
ATOM 5654 N NH2 . ARG B 1 283 ? -88.568  15.144 -8.476  1.00 153.10 ?  283 ARG B NH2 1 
ATOM 5655 N N   . PRO B 1 284 ? -85.355  19.364 -0.407  1.00 112.50 ?  284 PRO B N   1 
ATOM 5656 C CA  . PRO B 1 284 ? -85.598  20.249 0.735   1.00 106.50 ?  284 PRO B CA  1 
ATOM 5657 C C   . PRO B 1 284 ? -85.895  21.676 0.292   1.00 87.28  ?  284 PRO B C   1 
ATOM 5658 O O   . PRO B 1 284 ? -85.797  22.030 -0.884  1.00 101.18 ?  284 PRO B O   1 
ATOM 5659 C CB  . PRO B 1 284 ? -84.281  20.173 1.509   1.00 100.67 ?  284 PRO B CB  1 
ATOM 5660 C CG  . PRO B 1 284 ? -83.257  19.996 0.438   1.00 95.22  ?  284 PRO B CG  1 
ATOM 5661 C CD  . PRO B 1 284 ? -83.913  19.189 -0.664  1.00 106.39 ?  284 PRO B CD  1 
ATOM 5662 N N   . TYR B 1 285 ? -86.256  22.502 1.272   1.00 65.93  ?  285 TYR B N   1 
ATOM 5663 C CA  . TYR B 1 285 ? -86.574  23.901 1.016   1.00 78.72  ?  285 TYR B CA  1 
ATOM 5664 C C   . TYR B 1 285 ? -86.616  24.660 2.333   1.00 85.68  ?  285 TYR B C   1 
ATOM 5665 O O   . TYR B 1 285 ? -86.889  24.084 3.390   1.00 99.31  ?  285 TYR B O   1 
ATOM 5666 C CB  . TYR B 1 285 ? -87.909  24.052 0.272   1.00 95.42  ?  285 TYR B CB  1 
ATOM 5667 C CG  . TYR B 1 285 ? -89.123  23.594 1.051   1.00 73.93  ?  285 TYR B CG  1 
ATOM 5668 C CD1 . TYR B 1 285 ? -89.425  22.244 1.175   1.00 71.39  ?  285 TYR B CD1 1 
ATOM 5669 C CD2 . TYR B 1 285 ? -89.974  24.513 1.652   1.00 88.09  ?  285 TYR B CD2 1 
ATOM 5670 C CE1 . TYR B 1 285 ? -90.536  21.823 1.878   1.00 86.46  ?  285 TYR B CE1 1 
ATOM 5671 C CE2 . TYR B 1 285 ? -91.088  24.100 2.358   1.00 95.83  ?  285 TYR B CE2 1 
ATOM 5672 C CZ  . TYR B 1 285 ? -91.363  22.754 2.468   1.00 89.46  ?  285 TYR B CZ  1 
ATOM 5673 O OH  . TYR B 1 285 ? -92.469  22.335 3.169   1.00 103.78 ?  285 TYR B OH  1 
ATOM 5674 N N   . SER B 1 286 ? -86.342  25.958 2.249   1.00 70.52  ?  286 SER B N   1 
ATOM 5675 C CA  . SER B 1 286 ? -86.360  26.873 3.378   1.00 68.96  ?  286 SER B CA  1 
ATOM 5676 C C   . SER B 1 286 ? -86.908  28.213 2.910   1.00 75.50  ?  286 SER B C   1 
ATOM 5677 O O   . SER B 1 286 ? -86.659  28.623 1.770   1.00 76.92  ?  286 SER B O   1 
ATOM 5678 C CB  . SER B 1 286 ? -84.957  27.055 3.982   1.00 74.43  ?  286 SER B CB  1 
ATOM 5679 O OG  . SER B 1 286 ? -83.990  27.282 2.971   1.00 91.14  ?  286 SER B OG  1 
ATOM 5680 N N   . PRO B 1 287 ? -87.646  28.915 3.761   1.00 66.43  ?  287 PRO B N   1 
ATOM 5681 C CA  . PRO B 1 287 ? -88.414  30.083 3.316   1.00 59.92  ?  287 PRO B CA  1 
ATOM 5682 C C   . PRO B 1 287 ? -87.551  31.338 3.214   1.00 70.02  ?  287 PRO B C   1 
ATOM 5683 O O   . PRO B 1 287 ? -86.375  31.354 3.570   1.00 81.58  ?  287 PRO B O   1 
ATOM 5684 C CB  . PRO B 1 287 ? -89.473  30.223 4.410   1.00 56.14  ?  287 PRO B CB  1 
ATOM 5685 C CG  . PRO B 1 287 ? -88.778  29.736 5.638   1.00 65.48  ?  287 PRO B CG  1 
ATOM 5686 C CD  . PRO B 1 287 ? -87.865  28.623 5.188   1.00 70.96  ?  287 PRO B CD  1 
ATOM 5687 N N   . PHE B 1 288 ? -88.173  32.408 2.717   1.00 73.00  ?  288 PHE B N   1 
ATOM 5688 C CA  . PHE B 1 288 ? -87.549  33.715 2.567   1.00 68.00  ?  288 PHE B CA  1 
ATOM 5689 C C   . PHE B 1 288 ? -88.295  34.732 3.421   1.00 71.98  ?  288 PHE B C   1 
ATOM 5690 O O   . PHE B 1 288 ? -89.513  34.633 3.604   1.00 77.53  ?  288 PHE B O   1 
ATOM 5691 C CB  . PHE B 1 288 ? -87.554  34.189 1.103   1.00 77.39  ?  288 PHE B CB  1 
ATOM 5692 C CG  . PHE B 1 288 ? -86.673  33.383 0.189   1.00 74.87  ?  288 PHE B CG  1 
ATOM 5693 C CD1 . PHE B 1 288 ? -85.581  33.967 -0.429  1.00 85.03  ?  288 PHE B CD1 1 
ATOM 5694 C CD2 . PHE B 1 288 ? -86.950  32.051 -0.073  1.00 87.60  ?  288 PHE B CD2 1 
ATOM 5695 C CE1 . PHE B 1 288 ? -84.773  33.235 -1.278  1.00 95.85  ?  288 PHE B CE1 1 
ATOM 5696 C CE2 . PHE B 1 288 ? -86.146  31.313 -0.919  1.00 83.34  ?  288 PHE B CE2 1 
ATOM 5697 C CZ  . PHE B 1 288 ? -85.056  31.906 -1.523  1.00 74.70  ?  288 PHE B CZ  1 
ATOM 5698 N N   . LEU B 1 289 ? -87.560  35.719 3.933   1.00 76.44  ?  289 LEU B N   1 
ATOM 5699 C CA  . LEU B 1 289 ? -88.129  36.763 4.774   1.00 65.67  ?  289 LEU B CA  1 
ATOM 5700 C C   . LEU B 1 289 ? -87.659  38.132 4.306   1.00 67.41  ?  289 LEU B C   1 
ATOM 5701 O O   . LEU B 1 289 ? -86.542  38.286 3.805   1.00 78.57  ?  289 LEU B O   1 
ATOM 5702 C CB  . LEU B 1 289 ? -87.747  36.579 6.251   1.00 58.69  ?  289 LEU B CB  1 
ATOM 5703 C CG  . LEU B 1 289 ? -87.867  35.185 6.868   1.00 62.37  ?  289 LEU B CG  1 
ATOM 5704 C CD1 . LEU B 1 289 ? -87.389  35.215 8.306   1.00 92.11  ?  289 LEU B CD1 1 
ATOM 5705 C CD2 . LEU B 1 289 ? -89.296  34.681 6.795   1.00 64.89  ?  289 LEU B CD2 1 
ATOM 5706 N N   . LEU B 1 290 ? -88.525  39.129 4.482   1.00 68.71  ?  290 LEU B N   1 
ATOM 5707 C CA  . LEU B 1 290 ? -88.192  40.514 4.172   1.00 66.32  ?  290 LEU B CA  1 
ATOM 5708 C C   . LEU B 1 290 ? -89.001  41.435 5.072   1.00 64.97  ?  290 LEU B C   1 
ATOM 5709 O O   . LEU B 1 290 ? -90.215  41.259 5.210   1.00 70.28  ?  290 LEU B O   1 
ATOM 5710 C CB  . LEU B 1 290 ? -88.466  40.842 2.700   1.00 66.95  ?  290 LEU B CB  1 
ATOM 5711 C CG  . LEU B 1 290 ? -88.493  42.334 2.350   1.00 63.52  ?  290 LEU B CG  1 
ATOM 5712 C CD1 . LEU B 1 290 ? -87.108  42.950 2.467   1.00 66.81  ?  290 LEU B CD1 1 
ATOM 5713 C CD2 . LEU B 1 290 ? -89.066  42.557 0.958   1.00 83.20  ?  290 LEU B CD2 1 
ATOM 5714 N N   . PHE B 1 291 ? -88.329  42.412 5.672   1.00 75.35  ?  291 PHE B N   1 
ATOM 5715 C CA  . PHE B 1 291 ? -88.957  43.397 6.539   1.00 77.64  ?  291 PHE B CA  1 
ATOM 5716 C C   . PHE B 1 291 ? -88.819  44.784 5.925   1.00 81.41  ?  291 PHE B C   1 
ATOM 5717 O O   . PHE B 1 291 ? -88.128  44.980 4.922   1.00 93.25  ?  291 PHE B O   1 
ATOM 5718 C CB  . PHE B 1 291 ? -88.340  43.373 7.945   1.00 72.56  ?  291 PHE B CB  1 
ATOM 5719 C CG  . PHE B 1 291 ? -88.501  42.061 8.661   1.00 75.26  ?  291 PHE B CG  1 
ATOM 5720 C CD1 . PHE B 1 291 ? -89.516  41.880 9.586   1.00 76.88  ?  291 PHE B CD1 1 
ATOM 5721 C CD2 . PHE B 1 291 ? -87.630  41.011 8.417   1.00 70.78  ?  291 PHE B CD2 1 
ATOM 5722 C CE1 . PHE B 1 291 ? -89.661  40.676 10.250  1.00 81.74  ?  291 PHE B CE1 1 
ATOM 5723 C CE2 . PHE B 1 291 ? -87.772  39.805 9.076   1.00 76.55  ?  291 PHE B CE2 1 
ATOM 5724 C CZ  . PHE B 1 291 ? -88.789  39.637 9.993   1.00 82.43  ?  291 PHE B CZ  1 
ATOM 5725 N N   . HIS B 1 292 ? -89.488  45.753 6.545   1.00 74.94  ?  292 HIS B N   1 
ATOM 5726 C CA  . HIS B 1 292 ? -89.440  47.143 6.105   1.00 77.15  ?  292 HIS B CA  1 
ATOM 5727 C C   . HIS B 1 292 ? -90.058  48.010 7.194   1.00 88.98  ?  292 HIS B C   1 
ATOM 5728 O O   . HIS B 1 292 ? -90.596  47.508 8.184   1.00 101.37 ?  292 HIS B O   1 
ATOM 5729 C CB  . HIS B 1 292 ? -90.162  47.348 4.768   1.00 72.37  ?  292 HIS B CB  1 
ATOM 5730 C CG  . HIS B 1 292 ? -91.595  46.914 4.777   1.00 84.72  ?  292 HIS B CG  1 
ATOM 5731 N ND1 . HIS B 1 292 ? -91.979  45.609 4.999   1.00 82.69  ?  292 HIS B ND1 1 
ATOM 5732 C CD2 . HIS B 1 292 ? -92.739  47.614 4.587   1.00 84.67  ?  292 HIS B CD2 1 
ATOM 5733 C CE1 . HIS B 1 292 ? -93.296  45.523 4.945   1.00 82.40  ?  292 HIS B CE1 1 
ATOM 5734 N NE2 . HIS B 1 292 ? -93.781  46.726 4.697   1.00 77.97  ?  292 HIS B NE2 1 
ATOM 5735 N N   . GLY B 1 293 ? -89.971  49.322 6.997   1.00 87.16  ?  293 GLY B N   1 
ATOM 5736 C CA  . GLY B 1 293 ? -90.536  50.276 7.939   1.00 107.54 ?  293 GLY B CA  1 
ATOM 5737 C C   . GLY B 1 293 ? -89.834  50.324 9.278   1.00 106.28 ?  293 GLY B C   1 
ATOM 5738 O O   . GLY B 1 293 ? -90.497  50.405 10.320  1.00 103.85 ?  293 GLY B O   1 
ATOM 5739 N N   . THR B 1 294 ? -88.506  50.287 9.278   1.00 103.05 ?  294 THR B N   1 
ATOM 5740 C CA  . THR B 1 294 ? -87.732  50.299 10.511  1.00 110.54 ?  294 THR B CA  1 
ATOM 5741 C C   . THR B 1 294 ? -86.433  51.054 10.256  1.00 115.97 ?  294 THR B C   1 
ATOM 5742 O O   . THR B 1 294 ? -86.254  51.683 9.208   1.00 119.73 ?  294 THR B O   1 
ATOM 5743 C CB  . THR B 1 294 ? -87.473  48.870 11.005  1.00 117.77 ?  294 THR B CB  1 
ATOM 5744 O OG1 . THR B 1 294 ? -86.763  48.913 12.249  1.00 115.23 ?  294 THR B OG1 1 
ATOM 5745 C CG2 . THR B 1 294 ? -86.651  48.095 9.982   1.00 108.38 ?  294 THR B CG2 1 
ATOM 5746 N N   . SER B 1 295 ? -85.526  50.995 11.224  1.00 105.60 ?  295 SER B N   1 
ATOM 5747 C CA  . SER B 1 295 ? -84.188  51.543 11.083  1.00 94.44  ?  295 SER B CA  1 
ATOM 5748 C C   . SER B 1 295 ? -83.182  50.403 11.018  1.00 88.13  ?  295 SER B C   1 
ATOM 5749 O O   . SER B 1 295 ? -83.421  49.313 11.546  1.00 87.05  ?  295 SER B O   1 
ATOM 5750 C CB  . SER B 1 295 ? -83.843  52.480 12.244  1.00 102.71 ?  295 SER B CB  1 
ATOM 5751 O OG  . SER B 1 295 ? -83.497  51.747 13.407  1.00 96.97  ?  295 SER B OG  1 
ATOM 5752 N N   . ASP B 1 296 ? -82.052  50.662 10.356  1.00 95.22  ?  296 ASP B N   1 
ATOM 5753 C CA  . ASP B 1 296 ? -81.002  49.655 10.265  1.00 82.88  ?  296 ASP B CA  1 
ATOM 5754 C C   . ASP B 1 296 ? -80.469  49.253 11.633  1.00 83.47  ?  296 ASP B C   1 
ATOM 5755 O O   . ASP B 1 296 ? -79.902  48.164 11.768  1.00 77.85  ?  296 ASP B O   1 
ATOM 5756 C CB  . ASP B 1 296 ? -79.859  50.161 9.383   1.00 85.89  ?  296 ASP B CB  1 
ATOM 5757 C CG  . ASP B 1 296 ? -80.293  50.410 7.951   1.00 95.19  ?  296 ASP B CG  1 
ATOM 5758 O OD1 . ASP B 1 296 ? -81.469  50.138 7.630   1.00 107.72 ?  296 ASP B OD1 1 
ATOM 5759 O OD2 . ASP B 1 296 ? -79.458  50.874 7.146   1.00 89.61  -1 296 ASP B OD2 1 
ATOM 5760 N N   . ALA B 1 297 ? -80.638  50.102 12.649  1.00 86.16  ?  297 ALA B N   1 
ATOM 5761 C CA  . ALA B 1 297 ? -80.207  49.742 13.996  1.00 83.46  ?  297 ALA B CA  1 
ATOM 5762 C C   . ALA B 1 297 ? -80.987  48.542 14.521  1.00 89.30  ?  297 ALA B C   1 
ATOM 5763 O O   . ALA B 1 297 ? -80.401  47.577 15.025  1.00 77.88  ?  297 ALA B O   1 
ATOM 5764 C CB  . ALA B 1 297 ? -80.360  50.940 14.933  1.00 79.96  ?  297 ALA B CB  1 
ATOM 5765 N N   . ASN B 1 298 ? -82.317  48.586 14.409  1.00 90.78  ?  298 ASN B N   1 
ATOM 5766 C CA  . ASN B 1 298 ? -83.139  47.496 14.927  1.00 81.66  ?  298 ASN B CA  1 
ATOM 5767 C C   . ASN B 1 298 ? -83.006  46.241 14.073  1.00 83.88  ?  298 ASN B C   1 
ATOM 5768 O O   . ASN B 1 298 ? -82.905  45.130 14.607  1.00 75.24  ?  298 ASN B O   1 
ATOM 5769 C CB  . ASN B 1 298 ? -84.602  47.932 15.008  1.00 71.56  ?  298 ASN B CB  1 
ATOM 5770 C CG  . ASN B 1 298 ? -84.758  49.366 15.469  1.00 104.62 ?  298 ASN B CG  1 
ATOM 5771 O OD1 . ASN B 1 298 ? -84.615  50.301 14.683  1.00 113.49 ?  298 ASN B OD1 1 
ATOM 5772 N ND2 . ASN B 1 298 ? -85.057  49.546 16.750  1.00 114.03 ?  298 ASN B ND2 1 
ATOM 5773 N N   . LEU B 1 299 ? -83.006  46.396 12.747  1.00 73.85  ?  299 LEU B N   1 
ATOM 5774 C CA  . LEU B 1 299 ? -82.958  45.232 11.867  1.00 84.83  ?  299 LEU B CA  1 
ATOM 5775 C C   . LEU B 1 299 ? -81.628  44.497 11.984  1.00 85.16  ?  299 LEU B C   1 
ATOM 5776 O O   . LEU B 1 299 ? -81.592  43.261 11.955  1.00 80.58  ?  299 LEU B O   1 
ATOM 5777 C CB  . LEU B 1 299 ? -83.213  45.659 10.421  1.00 87.60  ?  299 LEU B CB  1 
ATOM 5778 C CG  . LEU B 1 299 ? -83.430  44.534 9.407   1.00 79.58  ?  299 LEU B CG  1 
ATOM 5779 C CD1 . LEU B 1 299 ? -84.688  44.790 8.592   1.00 82.97  ?  299 LEU B CD1 1 
ATOM 5780 C CD2 . LEU B 1 299 ? -82.221  44.384 8.494   1.00 92.29  ?  299 LEU B CD2 1 
ATOM 5781 N N   . TYR B 1 300 ? -80.524  45.236 12.119  1.00 77.30  ?  300 TYR B N   1 
ATOM 5782 C CA  . TYR B 1 300 ? -79.217  44.594 12.219  1.00 77.53  ?  300 TYR B CA  1 
ATOM 5783 C C   . TYR B 1 300 ? -79.046  43.884 13.557  1.00 73.37  ?  300 TYR B C   1 
ATOM 5784 O O   . TYR B 1 300 ? -78.539  42.757 13.606  1.00 74.75  ?  300 TYR B O   1 
ATOM 5785 C CB  . TYR B 1 300 ? -78.109  45.625 12.005  1.00 80.59  ?  300 TYR B CB  1 
ATOM 5786 C CG  . TYR B 1 300 ? -77.986  46.097 10.571  1.00 87.09  ?  300 TYR B CG  1 
ATOM 5787 C CD1 . TYR B 1 300 ? -78.603  45.404 9.538   1.00 91.09  ?  300 TYR B CD1 1 
ATOM 5788 C CD2 . TYR B 1 300 ? -77.262  47.239 10.253  1.00 74.42  ?  300 TYR B CD2 1 
ATOM 5789 C CE1 . TYR B 1 300 ? -78.494  45.829 8.227   1.00 85.11  ?  300 TYR B CE1 1 
ATOM 5790 C CE2 . TYR B 1 300 ? -77.147  47.672 8.945   1.00 78.25  ?  300 TYR B CE2 1 
ATOM 5791 C CZ  . TYR B 1 300 ? -77.766  46.963 7.936   1.00 84.55  ?  300 TYR B CZ  1 
ATOM 5792 O OH  . TYR B 1 300 ? -77.656  47.389 6.634   1.00 87.58  ?  300 TYR B OH  1 
ATOM 5793 N N   . GLU B 1 301 ? -79.457  44.528 14.653  1.00 69.81  ?  301 GLU B N   1 
ATOM 5794 C CA  . GLU B 1 301 ? -79.376  43.885 15.960  1.00 60.76  ?  301 GLU B CA  1 
ATOM 5795 C C   . GLU B 1 301 ? -80.276  42.659 16.034  1.00 74.24  ?  301 GLU B C   1 
ATOM 5796 O O   . GLU B 1 301 ? -79.948  41.689 16.728  1.00 70.82  ?  301 GLU B O   1 
ATOM 5797 C CB  . GLU B 1 301 ? -79.737  44.881 17.062  1.00 79.38  ?  301 GLU B CB  1 
ATOM 5798 C CG  . GLU B 1 301 ? -79.754  44.281 18.461  1.00 66.34  ?  301 GLU B CG  1 
ATOM 5799 C CD  . GLU B 1 301 ? -79.852  45.333 19.548  1.00 114.76 ?  301 GLU B CD  1 
ATOM 5800 O OE1 . GLU B 1 301 ? -79.574  45.005 20.721  1.00 129.79 ?  301 GLU B OE1 1 
ATOM 5801 O OE2 . GLU B 1 301 ? -80.207  46.488 19.232  1.00 142.35 -1 301 GLU B OE2 1 
ATOM 5802 N N   . LEU B 1 302 ? -81.413  42.687 15.333  1.00 77.16  ?  302 LEU B N   1 
ATOM 5803 C CA  . LEU B 1 302 ? -82.269  41.508 15.261  1.00 63.08  ?  302 LEU B CA  1 
ATOM 5804 C C   . LEU B 1 302 ? -81.514  40.320 14.680  1.00 63.98  ?  302 LEU B C   1 
ATOM 5805 O O   . LEU B 1 302 ? -81.629  39.194 15.179  1.00 68.89  ?  302 LEU B O   1 
ATOM 5806 C CB  . LEU B 1 302 ? -83.514  41.820 14.427  1.00 71.64  ?  302 LEU B CB  1 
ATOM 5807 C CG  . LEU B 1 302 ? -84.389  40.653 13.957  1.00 60.50  ?  302 LEU B CG  1 
ATOM 5808 C CD1 . LEU B 1 302 ? -84.856  39.801 15.129  1.00 57.51  ?  302 LEU B CD1 1 
ATOM 5809 C CD2 . LEU B 1 302 ? -85.578  41.160 13.151  1.00 61.42  ?  302 LEU B CD2 1 
ATOM 5810 N N   . LYS B 1 303 ? -80.727  40.554 13.628  1.00 76.06  ?  303 LYS B N   1 
ATOM 5811 C CA  . LYS B 1 303 ? -79.935  39.478 13.043  1.00 73.13  ?  303 LYS B CA  1 
ATOM 5812 C C   . LYS B 1 303 ? -78.809  39.041 13.972  1.00 81.61  ?  303 LYS B C   1 
ATOM 5813 O O   . LYS B 1 303 ? -78.417  37.869 13.958  1.00 82.89  ?  303 LYS B O   1 
ATOM 5814 C CB  . LYS B 1 303 ? -79.373  39.919 11.692  1.00 64.38  ?  303 LYS B CB  1 
ATOM 5815 C CG  . LYS B 1 303 ? -80.426  40.467 10.745  1.00 65.27  ?  303 LYS B CG  1 
ATOM 5816 C CD  . LYS B 1 303 ? -79.801  41.261 9.613   1.00 50.18  ?  303 LYS B CD  1 
ATOM 5817 C CE  . LYS B 1 303 ? -79.089  40.356 8.624   1.00 75.05  ?  303 LYS B CE  1 
ATOM 5818 N NZ  . LYS B 1 303 ? -78.531  41.137 7.487   1.00 75.99  ?  303 LYS B NZ  1 
ATOM 5819 N N   . ASN B 1 304 ? -78.283  39.961 14.784  1.00 69.39  ?  304 ASN B N   1 
ATOM 5820 C CA  . ASN B 1 304 ? -77.218  39.619 15.719  1.00 71.24  ?  304 ASN B CA  1 
ATOM 5821 C C   . ASN B 1 304 ? -77.718  38.783 16.890  1.00 82.87  ?  304 ASN B C   1 
ATOM 5822 O O   . ASN B 1 304 ? -76.901  38.187 17.598  1.00 105.62 ?  304 ASN B O   1 
ATOM 5823 C CB  . ASN B 1 304 ? -76.542  40.890 16.237  1.00 88.35  ?  304 ASN B CB  1 
ATOM 5824 C CG  . ASN B 1 304 ? -75.710  41.581 15.175  1.00 82.71  ?  304 ASN B CG  1 
ATOM 5825 O OD1 . ASN B 1 304 ? -74.928  40.944 14.470  1.00 74.45  ?  304 ASN B OD1 1 
ATOM 5826 N ND2 . ASN B 1 304 ? -75.872  42.895 15.058  1.00 92.31  ?  304 ASN B ND2 1 
ATOM 5827 N N   . GLN B 1 305 ? -79.030  38.734 17.116  1.00 64.66  ?  305 GLN B N   1 
ATOM 5828 C CA  . GLN B 1 305 ? -79.586  37.858 18.139  1.00 79.90  ?  305 GLN B CA  1 
ATOM 5829 C C   . GLN B 1 305 ? -79.846  36.453 17.620  1.00 79.61  ?  305 GLN B C   1 
ATOM 5830 O O   . GLN B 1 305 ? -79.815  35.495 18.402  1.00 74.73  ?  305 GLN B O   1 
ATOM 5831 C CB  . GLN B 1 305 ? -80.891  38.439 18.694  1.00 83.35  ?  305 GLN B CB  1 
ATOM 5832 C CG  . GLN B 1 305 ? -80.720  39.699 19.525  1.00 73.46  ?  305 GLN B CG  1 
ATOM 5833 C CD  . GLN B 1 305 ? -81.928  39.988 20.399  1.00 80.81  ?  305 GLN B CD  1 
ATOM 5834 O OE1 . GLN B 1 305 ? -82.692  39.084 20.743  1.00 83.39  ?  305 GLN B OE1 1 
ATOM 5835 N NE2 . GLN B 1 305 ? -82.107  41.252 20.763  1.00 85.21  ?  305 GLN B NE2 1 
ATOM 5836 N N   . LEU B 1 306 ? -80.095  36.308 16.318  1.00 75.56  ?  306 LEU B N   1 
ATOM 5837 C CA  . LEU B 1 306 ? -80.415  34.999 15.760  1.00 75.46  ?  306 LEU B CA  1 
ATOM 5838 C C   . LEU B 1 306 ? -79.160  34.170 15.516  1.00 88.73  ?  306 LEU B C   1 
ATOM 5839 O O   . LEU B 1 306 ? -79.163  32.956 15.748  1.00 97.64  ?  306 LEU B O   1 
ATOM 5840 C CB  . LEU B 1 306 ? -81.207  35.161 14.464  1.00 75.73  ?  306 LEU B CB  1 
ATOM 5841 C CG  . LEU B 1 306 ? -82.551  35.880 14.599  1.00 70.10  ?  306 LEU B CG  1 
ATOM 5842 C CD1 . LEU B 1 306 ? -82.880  36.641 13.327  1.00 73.95  ?  306 LEU B CD1 1 
ATOM 5843 C CD2 . LEU B 1 306 ? -83.659  34.897 14.939  1.00 67.69  ?  306 LEU B CD2 1 
ATOM 5844 N N   . PHE B 1 307 ? -78.083  34.803 15.043  1.00 92.38  ?  307 PHE B N   1 
ATOM 5845 C CA  . PHE B 1 307 ? -76.840  34.067 14.836  1.00 84.30  ?  307 PHE B CA  1 
ATOM 5846 C C   . PHE B 1 307 ? -76.230  33.623 16.159  1.00 93.74  ?  307 PHE B C   1 
ATOM 5847 O O   . PHE B 1 307 ? -75.535  32.601 16.206  1.00 106.95 ?  307 PHE B O   1 
ATOM 5848 C CB  . PHE B 1 307 ? -75.848  34.915 14.041  1.00 83.68  ?  307 PHE B CB  1 
ATOM 5849 C CG  . PHE B 1 307 ? -75.095  34.140 12.997  1.00 84.54  ?  307 PHE B CG  1 
ATOM 5850 C CD1 . PHE B 1 307 ? -74.014  33.349 13.349  1.00 91.26  ?  307 PHE B CD1 1 
ATOM 5851 C CD2 . PHE B 1 307 ? -75.473  34.196 11.665  1.00 79.39  ?  307 PHE B CD2 1 
ATOM 5852 C CE1 . PHE B 1 307 ? -73.320  32.632 12.392  1.00 88.50  ?  307 PHE B CE1 1 
ATOM 5853 C CE2 . PHE B 1 307 ? -74.783  33.481 10.702  1.00 69.95  ?  307 PHE B CE2 1 
ATOM 5854 C CZ  . PHE B 1 307 ? -73.705  32.698 11.067  1.00 76.43  ?  307 PHE B CZ  1 
ATOM 5855 N N   . ASN B 1 308 ? -76.473  34.372 17.238  1.00 85.90  ?  308 ASN B N   1 
ATOM 5856 C CA  . ASN B 1 308 ? -76.106  33.896 18.567  1.00 94.70  ?  308 ASN B CA  1 
ATOM 5857 C C   . ASN B 1 308 ? -77.065  32.821 19.060  1.00 97.07  ?  308 ASN B C   1 
ATOM 5858 O O   . ASN B 1 308 ? -76.670  31.957 19.850  1.00 107.68 ?  308 ASN B O   1 
ATOM 5859 C CB  . ASN B 1 308 ? -76.066  35.060 19.558  1.00 93.10  ?  308 ASN B CB  1 
ATOM 5860 C CG  . ASN B 1 308 ? -75.195  36.204 19.081  1.00 103.81 ?  308 ASN B CG  1 
ATOM 5861 O OD1 . ASN B 1 308 ? -74.441  36.067 18.118  1.00 113.49 ?  308 ASN B OD1 1 
ATOM 5862 N ND2 . ASN B 1 308 ? -75.296  37.344 19.755  1.00 106.15 ?  308 ASN B ND2 1 
ATOM 5863 N N   . GLU B 1 309 ? -78.320  32.861 18.613  1.00 81.54  ?  309 GLU B N   1 
ATOM 5864 C CA  . GLU B 1 309 ? -79.282  31.794 18.863  1.00 90.05  ?  309 GLU B CA  1 
ATOM 5865 C C   . GLU B 1 309 ? -79.064  30.585 17.961  1.00 94.47  ?  309 GLU B C   1 
ATOM 5866 O O   . GLU B 1 309 ? -79.881  29.657 17.988  1.00 99.23  ?  309 GLU B O   1 
ATOM 5867 C CB  . GLU B 1 309 ? -80.712  32.315 18.683  1.00 94.44  ?  309 GLU B CB  1 
ATOM 5868 C CG  . GLU B 1 309 ? -81.269  33.067 19.881  1.00 97.37  ?  309 GLU B CG  1 
ATOM 5869 C CD  . GLU B 1 309 ? -82.770  33.272 19.790  1.00 100.00 ?  309 GLU B CD  1 
ATOM 5870 O OE1 . GLU B 1 309 ? -83.319  34.028 20.618  1.00 115.05 ?  309 GLU B OE1 1 
ATOM 5871 O OE2 . GLU B 1 309 ? -83.400  32.679 18.888  1.00 92.14  -1 309 GLU B OE2 1 
ATOM 5872 N N   . ASP B 1 310 ? -77.995  30.592 17.162  1.00 97.38  ?  310 ASP B N   1 
ATOM 5873 C CA  . ASP B 1 310 ? -77.655  29.496 16.255  1.00 99.53  ?  310 ASP B CA  1 
ATOM 5874 C C   . ASP B 1 310 ? -78.744  29.258 15.213  1.00 89.43  ?  310 ASP B C   1 
ATOM 5875 O O   . ASP B 1 310 ? -78.984  28.121 14.797  1.00 95.09  ?  310 ASP B O   1 
ATOM 5876 C CB  . ASP B 1 310 ? -77.354  28.206 17.024  1.00 104.28 ?  310 ASP B CB  1 
ATOM 5877 C CG  . ASP B 1 310 ? -76.026  28.262 17.751  1.00 102.00 ?  310 ASP B CG  1 
ATOM 5878 O OD1 . ASP B 1 310 ? -75.032  28.712 17.143  1.00 100.07 ?  310 ASP B OD1 1 
ATOM 5879 O OD2 . ASP B 1 310 ? -75.976  27.856 18.932  1.00 106.18 -1 310 ASP B OD2 1 
ATOM 5880 N N   . LEU B 1 311 ? -79.415  30.325 14.785  1.00 87.06  ?  311 LEU B N   1 
ATOM 5881 C CA  . LEU B 1 311 ? -80.356  30.266 13.668  1.00 82.50  ?  311 LEU B CA  1 
ATOM 5882 C C   . LEU B 1 311 ? -79.619  30.814 12.450  1.00 92.58  ?  311 LEU B C   1 
ATOM 5883 O O   . LEU B 1 311 ? -79.596  32.020 12.202  1.00 90.70  ?  311 LEU B O   1 
ATOM 5884 C CB  . LEU B 1 311 ? -81.628  31.049 13.968  1.00 92.40  ?  311 LEU B CB  1 
ATOM 5885 C CG  . LEU B 1 311 ? -82.776  30.808 12.984  1.00 86.59  ?  311 LEU B CG  1 
ATOM 5886 C CD1 . LEU B 1 311 ? -83.179  29.341 12.980  1.00 76.80  ?  311 LEU B CD1 1 
ATOM 5887 C CD2 . LEU B 1 311 ? -83.971  31.690 13.305  1.00 69.04  ?  311 LEU B CD2 1 
ATOM 5888 N N   . ILE B 1 312 ? -79.015  29.910 11.686  1.00 89.65  ?  312 ILE B N   1 
ATOM 5889 C CA  . ILE B 1 312 ? -78.129  30.285 10.592  1.00 91.29  ?  312 ILE B CA  1 
ATOM 5890 C C   . ILE B 1 312 ? -78.956  30.642 9.365   1.00 99.33  ?  312 ILE B C   1 
ATOM 5891 O O   . ILE B 1 312 ? -79.931  29.958 9.029   1.00 93.57  ?  312 ILE B O   1 
ATOM 5892 C CB  . ILE B 1 312 ? -77.140  29.143 10.295  1.00 84.06  ?  312 ILE B CB  1 
ATOM 5893 C CG1 . ILE B 1 312 ? -76.379  28.762 11.567  1.00 84.46  ?  312 ILE B CG1 1 
ATOM 5894 C CG2 . ILE B 1 312 ? -76.168  29.541 9.196   1.00 84.29  ?  312 ILE B CG2 1 
ATOM 5895 C CD1 . ILE B 1 312 ? -75.463  27.570 11.400  1.00 119.70 ?  312 ILE B CD1 1 
ATOM 5896 N N   . PHE B 1 313 ? -78.566  31.719 8.690   1.00 86.51  ?  313 PHE B N   1 
ATOM 5897 C CA  . PHE B 1 313 ? -79.289  32.213 7.525   1.00 82.95  ?  313 PHE B CA  1 
ATOM 5898 C C   . PHE B 1 313 ? -78.288  32.848 6.565   1.00 86.14  ?  313 PHE B C   1 
ATOM 5899 O O   . PHE B 1 313 ? -77.073  32.684 6.707   1.00 90.63  ?  313 PHE B O   1 
ATOM 5900 C CB  . PHE B 1 313 ? -80.386  33.201 7.945   1.00 84.51  ?  313 PHE B CB  1 
ATOM 5901 C CG  . PHE B 1 313 ? -79.868  34.415 8.667   1.00 80.83  ?  313 PHE B CG  1 
ATOM 5902 C CD1 . PHE B 1 313 ? -79.615  34.374 10.029  1.00 83.82  ?  313 PHE B CD1 1 
ATOM 5903 C CD2 . PHE B 1 313 ? -79.636  35.598 7.984   1.00 66.11  ?  313 PHE B CD2 1 
ATOM 5904 C CE1 . PHE B 1 313 ? -79.139  35.488 10.695  1.00 71.74  ?  313 PHE B CE1 1 
ATOM 5905 C CE2 . PHE B 1 313 ? -79.160  36.716 8.644   1.00 56.00  ?  313 PHE B CE2 1 
ATOM 5906 C CZ  . PHE B 1 313 ? -78.912  36.660 10.002  1.00 55.12  ?  313 PHE B CZ  1 
ATOM 5907 N N   . THR B 1 314 ? -78.808  33.576 5.579   1.00 84.30  ?  314 THR B N   1 
ATOM 5908 C CA  . THR B 1 314 ? -77.978  34.286 4.616   1.00 87.23  ?  314 THR B CA  1 
ATOM 5909 C C   . THR B 1 314 ? -78.794  35.416 4.007   1.00 82.53  ?  314 THR B C   1 
ATOM 5910 O O   . THR B 1 314 ? -80.024  35.342 3.934   1.00 86.77  ?  314 THR B O   1 
ATOM 5911 C CB  . THR B 1 314 ? -77.455  33.353 3.517   1.00 91.63  ?  314 THR B CB  1 
ATOM 5912 O OG1 . THR B 1 314 ? -76.865  34.130 2.467   1.00 103.81 ?  314 THR B OG1 1 
ATOM 5913 C CG2 . THR B 1 314 ? -78.586  32.510 2.949   1.00 74.54  ?  314 THR B CG2 1 
ATOM 5914 N N   . ASP B 1 315 ? -78.095  36.468 3.573   1.00 80.16  ?  315 ASP B N   1 
ATOM 5915 C CA  . ASP B 1 315 ? -78.753  37.615 2.961   1.00 77.74  ?  315 ASP B CA  1 
ATOM 5916 C C   . ASP B 1 315 ? -77.986  38.109 1.741   1.00 87.71  ?  315 ASP B C   1 
ATOM 5917 O O   . ASP B 1 315 ? -78.072  39.290 1.384   1.00 95.39  ?  315 ASP B O   1 
ATOM 5918 C CB  . ASP B 1 315 ? -78.924  38.754 3.968   1.00 84.11  ?  315 ASP B CB  1 
ATOM 5919 C CG  . ASP B 1 315 ? -77.600  39.286 4.476   1.00 93.22  ?  315 ASP B CG  1 
ATOM 5920 O OD1 . ASP B 1 315 ? -76.611  38.523 4.472   1.00 94.20  ?  315 ASP B OD1 1 
ATOM 5921 O OD2 . ASP B 1 315 ? -77.550  40.466 4.882   1.00 88.94  -1 315 ASP B OD2 1 
ATOM 5922 N N   . GLY B 1 316 ? -77.232  37.226 1.092   1.00 80.14  ?  316 GLY B N   1 
ATOM 5923 C CA  . GLY B 1 316 ? -76.480  37.600 -0.089  1.00 84.46  ?  316 GLY B CA  1 
ATOM 5924 C C   . GLY B 1 316 ? -75.069  38.061 0.210   1.00 80.61  ?  316 GLY B C   1 
ATOM 5925 O O   . GLY B 1 316 ? -74.103  37.492 -0.306  1.00 83.90  ?  316 GLY B O   1 
ATOM 5926 N N   . TYR B 1 317 ? -74.939  39.089 1.034   1.00 98.81  ?  317 TYR B N   1 
ATOM 5927 C CA  . TYR B 1 317 ? -73.640  39.659 1.372   1.00 95.27  ?  317 TYR B CA  1 
ATOM 5928 C C   . TYR B 1 317 ? -72.870  38.719 2.293   1.00 79.89  ?  317 TYR B C   1 
ATOM 5929 O O   . TYR B 1 317 ? -73.295  38.515 3.438   1.00 69.94  ?  317 TYR B O   1 
ATOM 5930 C CB  . TYR B 1 317 ? -73.815  41.023 2.040   1.00 90.39  ?  317 TYR B CB  1 
ATOM 5931 C CG  . TYR B 1 317 ? -74.749  41.970 1.313   1.00 85.41  ?  317 TYR B CG  1 
ATOM 5932 C CD1 . TYR B 1 317 ? -74.252  42.925 0.437   1.00 102.75 ?  317 TYR B CD1 1 
ATOM 5933 C CD2 . TYR B 1 317 ? -76.124  41.926 1.521   1.00 83.69  ?  317 TYR B CD2 1 
ATOM 5934 C CE1 . TYR B 1 317 ? -75.096  43.797 -0.226  1.00 113.22 ?  317 TYR B CE1 1 
ATOM 5935 C CE2 . TYR B 1 317 ? -76.976  42.795 0.862   1.00 82.87  ?  317 TYR B CE2 1 
ATOM 5936 C CZ  . TYR B 1 317 ? -76.455  43.729 -0.010  1.00 86.48  ?  317 TYR B CZ  1 
ATOM 5937 O OH  . TYR B 1 317 ? -77.294  44.598 -0.669  1.00 93.33  ?  317 TYR B OH  1 
ATOM 5938 N N   . PRO B 1 318 ? -71.756  38.133 1.857   1.00 87.38  ?  318 PRO B N   1 
ATOM 5939 C CA  . PRO B 1 318 ? -70.969  37.260 2.736   1.00 87.89  ?  318 PRO B CA  1 
ATOM 5940 C C   . PRO B 1 318 ? -69.834  37.951 3.476   1.00 87.53  ?  318 PRO B C   1 
ATOM 5941 O O   . PRO B 1 318 ? -69.149  37.290 4.264   1.00 75.58  ?  318 PRO B O   1 
ATOM 5942 C CB  . PRO B 1 318 ? -70.411  36.215 1.753   1.00 81.23  ?  318 PRO B CB  1 
ATOM 5943 C CG  . PRO B 1 318 ? -70.646  36.785 0.344   1.00 80.19  ?  318 PRO B CG  1 
ATOM 5944 C CD  . PRO B 1 318 ? -71.182  38.174 0.504   1.00 83.58  ?  318 PRO B CD  1 
ATOM 5945 N N   . PHE B 1 319 ? -69.616  39.243 3.249   1.00 86.08  ?  319 PHE B N   1 
ATOM 5946 C CA  . PHE B 1 319 ? -68.558  39.976 3.932   1.00 78.26  ?  319 PHE B CA  1 
ATOM 5947 C C   . PHE B 1 319 ? -68.843  41.466 3.810   1.00 78.69  ?  319 PHE B C   1 
ATOM 5948 O O   . PHE B 1 319 ? -69.763  41.890 3.105   1.00 95.66  ?  319 PHE B O   1 
ATOM 5949 C CB  . PHE B 1 319 ? -67.174  39.624 3.373   1.00 88.57  ?  319 PHE B CB  1 
ATOM 5950 C CG  . PHE B 1 319 ? -67.118  39.557 1.874   1.00 88.86  ?  319 PHE B CG  1 
ATOM 5951 C CD1 . PHE B 1 319 ? -67.244  38.343 1.217   1.00 79.88  ?  319 PHE B CD1 1 
ATOM 5952 C CD2 . PHE B 1 319 ? -66.915  40.702 1.123   1.00 100.58 ?  319 PHE B CD2 1 
ATOM 5953 C CE1 . PHE B 1 319 ? -67.188  38.276 -0.161  1.00 73.12  ?  319 PHE B CE1 1 
ATOM 5954 C CE2 . PHE B 1 319 ? -66.855  40.641 -0.255  1.00 84.62  ?  319 PHE B CE2 1 
ATOM 5955 C CZ  . PHE B 1 319 ? -66.992  39.426 -0.898  1.00 68.12  ?  319 PHE B CZ  1 
ATOM 5956 N N   . LYS B 1 320 ? -68.049  42.258 4.528   1.00 82.11  ?  320 LYS B N   1 
ATOM 5957 C CA  . LYS B 1 320 ? -68.207  43.705 4.495   1.00 97.41  ?  320 LYS B CA  1 
ATOM 5958 C C   . LYS B 1 320 ? -67.940  44.243 3.097   1.00 96.95  ?  320 LYS B C   1 
ATOM 5959 O O   . LYS B 1 320 ? -67.082  43.735 2.369   1.00 94.07  ?  320 LYS B O   1 
ATOM 5960 C CB  . LYS B 1 320 ? -67.262  44.370 5.496   1.00 86.18  ?  320 LYS B CB  1 
ATOM 5961 C CG  . LYS B 1 320 ? -67.927  45.414 6.373   1.00 85.86  ?  320 LYS B CG  1 
ATOM 5962 C CD  . LYS B 1 320 ? -66.932  46.482 6.802   1.00 113.96 ?  320 LYS B CD  1 
ATOM 5963 C CE  . LYS B 1 320 ? -67.635  47.665 7.444   1.00 166.78 ?  320 LYS B CE  1 
ATOM 5964 N NZ  . LYS B 1 320 ? -66.702  48.801 7.682   1.00 164.83 ?  320 LYS B NZ  1 
ATOM 5965 N N   . GLY B 1 321 ? -68.686  45.281 2.725   1.00 110.55 ?  321 GLY B N   1 
ATOM 5966 C CA  . GLY B 1 321 ? -68.509  45.911 1.430   1.00 126.18 ?  321 GLY B CA  1 
ATOM 5967 C C   . GLY B 1 321 ? -68.782  45.014 0.247   1.00 117.68 ?  321 GLY B C   1 
ATOM 5968 O O   . GLY B 1 321 ? -68.327  45.308 -0.862  1.00 114.99 ?  321 GLY B O   1 
ATOM 5969 N N   . SER B 1 322 ? -69.513  43.922 0.447   1.00 108.54 ?  322 SER B N   1 
ATOM 5970 C CA  . SER B 1 322 ? -69.798  43.004 -0.641  1.00 96.15  ?  322 SER B CA  1 
ATOM 5971 C C   . SER B 1 322 ? -70.928  43.535 -1.520  1.00 98.75  ?  322 SER B C   1 
ATOM 5972 O O   . SER B 1 322 ? -71.566  44.549 -1.226  1.00 92.52  ?  322 SER B O   1 
ATOM 5973 C CB  . SER B 1 322 ? -70.164  41.624 -0.098  1.00 92.78  ?  322 SER B CB  1 
ATOM 5974 O OG  . SER B 1 322 ? -70.678  40.800 -1.130  1.00 81.89  ?  322 SER B OG  1 
ATOM 5975 N N   . VAL B 1 323 ? -71.168  42.826 -2.617  1.00 101.10 ?  323 VAL B N   1 
ATOM 5976 C CA  . VAL B 1 323 ? -72.288  43.096 -3.507  1.00 105.79 ?  323 VAL B CA  1 
ATOM 5977 C C   . VAL B 1 323 ? -73.260  41.931 -3.408  1.00 99.66  ?  323 VAL B C   1 
ATOM 5978 O O   . VAL B 1 323 ? -72.869  40.792 -3.125  1.00 85.76  ?  323 VAL B O   1 
ATOM 5979 C CB  . VAL B 1 323 ? -71.828  43.318 -4.964  1.00 92.85  ?  323 VAL B CB  1 
ATOM 5980 C CG1 . VAL B 1 323 ? -71.056  44.622 -5.079  1.00 100.48 ?  323 VAL B CG1 1 
ATOM 5981 C CG2 . VAL B 1 323 ? -70.976  42.152 -5.433  1.00 79.05  ?  323 VAL B CG2 1 
ATOM 5982 N N   . PHE B 1 324 ? -74.540  42.226 -3.630  1.00 83.87  ?  324 PHE B N   1 
ATOM 5983 C CA  . PHE B 1 324 ? -75.592  41.232 -3.452  1.00 77.49  ?  324 PHE B CA  1 
ATOM 5984 C C   . PHE B 1 324 ? -75.347  40.016 -4.336  1.00 75.13  ?  324 PHE B C   1 
ATOM 5985 O O   . PHE B 1 324 ? -75.356  40.117 -5.567  1.00 87.58  ?  324 PHE B O   1 
ATOM 5986 C CB  . PHE B 1 324 ? -76.954  41.855 -3.757  1.00 92.56  ?  324 PHE B CB  1 
ATOM 5987 C CG  . PHE B 1 324 ? -78.113  40.938 -3.495  1.00 84.02  ?  324 PHE B CG  1 
ATOM 5988 C CD1 . PHE B 1 324 ? -78.714  40.245 -4.532  1.00 84.61  ?  324 PHE B CD1 1 
ATOM 5989 C CD2 . PHE B 1 324 ? -78.598  40.762 -2.209  1.00 80.87  ?  324 PHE B CD2 1 
ATOM 5990 C CE1 . PHE B 1 324 ? -79.781  39.400 -4.294  1.00 84.88  ?  324 PHE B CE1 1 
ATOM 5991 C CE2 . PHE B 1 324 ? -79.664  39.916 -1.964  1.00 82.04  ?  324 PHE B CE2 1 
ATOM 5992 C CZ  . PHE B 1 324 ? -80.256  39.234 -3.009  1.00 89.95  ?  324 PHE B CZ  1 
ATOM 5993 N N   . THR B 1 325 ? -75.126  38.864 -3.699  1.00 81.95  ?  325 THR B N   1 
ATOM 5994 C CA  . THR B 1 325 ? -74.874  37.598 -4.380  1.00 93.62  ?  325 THR B CA  1 
ATOM 5995 C C   . THR B 1 325 ? -76.055  36.671 -4.127  1.00 79.58  ?  325 THR B C   1 
ATOM 5996 O O   . THR B 1 325 ? -76.083  35.948 -3.119  1.00 83.11  ?  325 THR B O   1 
ATOM 5997 C CB  . THR B 1 325 ? -73.567  36.964 -3.895  1.00 98.37  ?  325 THR B CB  1 
ATOM 5998 O OG1 . THR B 1 325 ? -72.494  37.903 -4.044  1.00 81.06  ?  325 THR B OG1 1 
ATOM 5999 C CG2 . THR B 1 325 ? -73.251  35.710 -4.698  1.00 82.50  ?  325 THR B CG2 1 
ATOM 6000 N N   . PRO B 1 326 ? -77.060  36.658 -5.007  1.00 78.96  ?  326 PRO B N   1 
ATOM 6001 C CA  . PRO B 1 326 ? -78.277  35.879 -4.725  1.00 90.30  ?  326 PRO B CA  1 
ATOM 6002 C C   . PRO B 1 326 ? -78.078  34.376 -4.764  1.00 93.53  ?  326 PRO B C   1 
ATOM 6003 O O   . PRO B 1 326 ? -78.908  33.654 -4.198  1.00 96.76  ?  326 PRO B O   1 
ATOM 6004 C CB  . PRO B 1 326 ? -79.248  36.333 -5.824  1.00 67.20  ?  326 PRO B CB  1 
ATOM 6005 C CG  . PRO B 1 326 ? -78.368  36.829 -6.921  1.00 93.52  ?  326 PRO B CG  1 
ATOM 6006 C CD  . PRO B 1 326 ? -77.176  37.439 -6.248  1.00 81.63  ?  326 PRO B CD  1 
ATOM 6007 N N   . LYS B 1 327 ? -77.024  33.875 -5.416  1.00 82.11  ?  327 LYS B N   1 
ATOM 6008 C CA  . LYS B 1 327 ? -76.851  32.428 -5.508  1.00 98.83  ?  327 LYS B CA  1 
ATOM 6009 C C   . LYS B 1 327 ? -76.632  31.800 -4.137  1.00 93.94  ?  327 LYS B C   1 
ATOM 6010 O O   . LYS B 1 327 ? -77.031  30.652 -3.910  1.00 107.66 ?  327 LYS B O   1 
ATOM 6011 C CB  . LYS B 1 327 ? -75.692  32.086 -6.446  1.00 92.42  ?  327 LYS B CB  1 
ATOM 6012 C CG  . LYS B 1 327 ? -75.443  30.589 -6.582  1.00 102.22 ?  327 LYS B CG  1 
ATOM 6013 C CD  . LYS B 1 327 ? -74.952  30.214 -7.970  1.00 113.80 ?  327 LYS B CD  1 
ATOM 6014 C CE  . LYS B 1 327 ? -74.793  28.705 -8.103  1.00 108.00 ?  327 LYS B CE  1 
ATOM 6015 N NZ  . LYS B 1 327 ? -76.081  27.987 -7.883  1.00 107.70 ?  327 LYS B NZ  1 
ATOM 6016 N N   . MET B 1 328 ? -76.013  32.534 -3.208  1.00 95.00  ?  328 MET B N   1 
ATOM 6017 C CA  . MET B 1 328 ? -75.864  32.018 -1.851  1.00 106.82 ?  328 MET B CA  1 
ATOM 6018 C C   . MET B 1 328 ? -77.214  31.840 -1.171  1.00 98.73  ?  328 MET B C   1 
ATOM 6019 O O   . MET B 1 328 ? -77.364  30.967 -0.308  1.00 103.39 ?  328 MET B O   1 
ATOM 6020 C CB  . MET B 1 328 ? -74.966  32.940 -1.028  1.00 101.63 ?  328 MET B CB  1 
ATOM 6021 C CG  . MET B 1 328 ? -73.490  32.806 -1.360  1.00 77.71  ?  328 MET B CG  1 
ATOM 6022 S SD  . MET B 1 328 ? -72.441  33.777 -0.264  1.00 139.04 ?  328 MET B SD  1 
ATOM 6023 C CE  . MET B 1 328 ? -72.746  32.969 1.305   1.00 104.53 ?  328 MET B CE  1 
ATOM 6024 N N   . LEU B 1 329 ? -78.206  32.654 -1.539  1.00 92.97  ?  329 LEU B N   1 
ATOM 6025 C CA  . LEU B 1 329 ? -79.567  32.407 -1.078  1.00 93.70  ?  329 LEU B CA  1 
ATOM 6026 C C   . LEU B 1 329 ? -80.118  31.127 -1.691  1.00 100.65 ?  329 LEU B C   1 
ATOM 6027 O O   . LEU B 1 329 ? -80.739  30.311 -1.001  1.00 111.05 ?  329 LEU B O   1 
ATOM 6028 C CB  . LEU B 1 329 ? -80.468  33.593 -1.418  1.00 77.79  ?  329 LEU B CB  1 
ATOM 6029 C CG  . LEU B 1 329 ? -79.966  34.977 -1.015  1.00 78.44  ?  329 LEU B CG  1 
ATOM 6030 C CD1 . LEU B 1 329 ? -80.989  36.030 -1.394  1.00 69.91  ?  329 LEU B CD1 1 
ATOM 6031 C CD2 . LEU B 1 329 ? -79.675  35.021 0.473   1.00 90.23  ?  329 LEU B CD2 1 
ATOM 6032 N N   . ILE B 1 330 ? -79.900  30.938 -2.995  1.00 97.47  ?  330 ILE B N   1 
ATOM 6033 C CA  . ILE B 1 330 ? -80.335  29.712 -3.654  1.00 110.57 ?  330 ILE B CA  1 
ATOM 6034 C C   . ILE B 1 330 ? -79.529  28.521 -3.150  1.00 112.80 ?  330 ILE B C   1 
ATOM 6035 O O   . ILE B 1 330 ? -80.063  27.419 -2.978  1.00 122.04 ?  330 ILE B O   1 
ATOM 6036 C CB  . ILE B 1 330 ? -80.232  29.863 -5.183  1.00 109.86 ?  330 ILE B CB  1 
ATOM 6037 C CG1 . ILE B 1 330 ? -81.007  31.096 -5.650  1.00 93.07  ?  330 ILE B CG1 1 
ATOM 6038 C CG2 . ILE B 1 330 ? -80.753  28.617 -5.880  1.00 121.76 ?  330 ILE B CG2 1 
ATOM 6039 C CD1 . ILE B 1 330 ? -80.962  31.316 -7.147  1.00 100.36 ?  330 ILE B CD1 1 
ATOM 6040 N N   . GLU B 1 331 ? -78.230  28.721 -2.909  1.00 105.37 ?  331 GLU B N   1 
ATOM 6041 C CA  . GLU B 1 331 ? -77.417  27.652 -2.337  1.00 105.00 ?  331 GLU B CA  1 
ATOM 6042 C C   . GLU B 1 331 ? -77.868  27.320 -0.921  1.00 106.59 ?  331 GLU B C   1 
ATOM 6043 O O   . GLU B 1 331 ? -77.982  26.143 -0.560  1.00 111.23 ?  331 GLU B O   1 
ATOM 6044 C CB  . GLU B 1 331 ? -75.940  28.047 -2.356  1.00 110.90 ?  331 GLU B CB  1 
ATOM 6045 C CG  . GLU B 1 331 ? -75.254  27.806 -3.691  1.00 122.31 ?  331 GLU B CG  1 
ATOM 6046 C CD  . GLU B 1 331 ? -73.768  28.099 -3.643  1.00 127.11 ?  331 GLU B CD  1 
ATOM 6047 O OE1 . GLU B 1 331 ? -73.400  29.283 -3.493  1.00 118.19 ?  331 GLU B OE1 1 
ATOM 6048 O OE2 . GLU B 1 331 ? -72.968  27.146 -3.750  1.00 145.82 -1 331 GLU B OE2 1 
ATOM 6049 N N   . GLY B 1 332 ? -78.135  28.344 -0.107  1.00 100.99 ?  332 GLY B N   1 
ATOM 6050 C CA  . GLY B 1 332 ? -78.675  28.116 1.221   1.00 92.41  ?  332 GLY B CA  1 
ATOM 6051 C C   . GLY B 1 332 ? -80.119  27.661 1.223   1.00 93.12  ?  332 GLY B C   1 
ATOM 6052 O O   . GLY B 1 332 ? -80.570  27.071 2.211   1.00 101.59 ?  332 GLY B O   1 
ATOM 6053 N N   . PHE B 1 333 ? -80.855  27.934 0.142   1.00 86.29  ?  333 PHE B N   1 
ATOM 6054 C CA  . PHE B 1 333 ? -82.224  27.441 0.026   1.00 70.16  ?  333 PHE B CA  1 
ATOM 6055 C C   . PHE B 1 333 ? -82.267  25.920 0.075   1.00 84.55  ?  333 PHE B C   1 
ATOM 6056 O O   . PHE B 1 333 ? -83.157  25.336 0.705   1.00 81.32  ?  333 PHE B O   1 
ATOM 6057 C CB  . PHE B 1 333 ? -82.853  27.959 -1.270  1.00 88.38  ?  333 PHE B CB  1 
ATOM 6058 C CG  . PHE B 1 333 ? -84.223  27.408 -1.551  1.00 87.77  ?  333 PHE B CG  1 
ATOM 6059 C CD1 . PHE B 1 333 ? -84.394  26.360 -2.442  1.00 81.37  ?  333 PHE B CD1 1 
ATOM 6060 C CD2 . PHE B 1 333 ? -85.341  27.943 -0.935  1.00 85.85  ?  333 PHE B CD2 1 
ATOM 6061 C CE1 . PHE B 1 333 ? -85.652  25.853 -2.708  1.00 78.98  ?  333 PHE B CE1 1 
ATOM 6062 C CE2 . PHE B 1 333 ? -86.603  27.441 -1.197  1.00 85.34  ?  333 PHE B CE2 1 
ATOM 6063 C CZ  . PHE B 1 333 ? -86.758  26.395 -2.085  1.00 86.80  ?  333 PHE B CZ  1 
ATOM 6064 N N   . SER B 1 334 ? -81.312  25.263 -0.579  1.00 109.31 ?  334 SER B N   1 
ATOM 6065 C CA  . SER B 1 334 ? -81.241  23.810 -0.604  1.00 106.52 ?  334 SER B CA  1 
ATOM 6066 C C   . SER B 1 334 ? -80.243  23.243 0.396   1.00 97.96  ?  334 SER B C   1 
ATOM 6067 O O   . SER B 1 334 ? -80.243  22.029 0.625   1.00 107.60 ?  334 SER B O   1 
ATOM 6068 C CB  . SER B 1 334 ? -80.881  23.323 -2.013  1.00 122.07 ?  334 SER B CB  1 
ATOM 6069 O OG  . SER B 1 334 ? -81.830  23.774 -2.964  1.00 131.52 ?  334 SER B OG  1 
ATOM 6070 N N   . ASN B 1 335 ? -79.400  24.082 0.993   1.00 99.98  ?  335 ASN B N   1 
ATOM 6071 C CA  . ASN B 1 335 ? -78.456  23.614 1.997   1.00 105.80 ?  335 ASN B CA  1 
ATOM 6072 C C   . ASN B 1 335 ? -79.158  23.512 3.344   1.00 99.34  ?  335 ASN B C   1 
ATOM 6073 O O   . ASN B 1 335 ? -79.892  24.422 3.746   1.00 100.63 ?  335 ASN B O   1 
ATOM 6074 C CB  . ASN B 1 335 ? -77.254  24.554 2.087   1.00 114.35 ?  335 ASN B CB  1 
ATOM 6075 C CG  . ASN B 1 335 ? -76.122  23.979 2.915   1.00 112.70 ?  335 ASN B CG  1 
ATOM 6076 O OD1 . ASN B 1 335 ? -76.287  23.687 4.100   1.00 108.69 ?  335 ASN B OD1 1 
ATOM 6077 N ND2 . ASN B 1 335 ? -74.963  23.807 2.291   1.00 126.03 ?  335 ASN B ND2 1 
ATOM 6078 N N   . LYS B 1 336 ? -78.931  22.402 4.042   1.00 102.29 ?  336 LYS B N   1 
ATOM 6079 C CA  . LYS B 1 336 ? -79.629  22.129 5.289   1.00 93.68  ?  336 LYS B CA  1 
ATOM 6080 C C   . LYS B 1 336 ? -78.965  22.769 6.500   1.00 95.72  ?  336 LYS B C   1 
ATOM 6081 O O   . LYS B 1 336 ? -79.611  22.897 7.546   1.00 94.61  ?  336 LYS B O   1 
ATOM 6082 C CB  . LYS B 1 336 ? -79.750  20.615 5.493   1.00 99.15  ?  336 LYS B CB  1 
ATOM 6083 C CG  . LYS B 1 336 ? -80.259  19.892 4.253   1.00 90.48  ?  336 LYS B CG  1 
ATOM 6084 C CD  . LYS B 1 336 ? -80.536  18.422 4.513   1.00 111.33 ?  336 LYS B CD  1 
ATOM 6085 C CE  . LYS B 1 336 ? -81.032  17.735 3.248   1.00 100.74 ?  336 LYS B CE  1 
ATOM 6086 N NZ  . LYS B 1 336 ? -81.449  16.327 3.493   1.00 113.08 ?  336 LYS B NZ  1 
ATOM 6087 N N   . GLU B 1 337 ? -77.699  23.178 6.387   1.00 98.96  ?  337 GLU B N   1 
ATOM 6088 C CA  . GLU B 1 337 ? -77.075  23.953 7.451   1.00 102.24 ?  337 GLU B CA  1 
ATOM 6089 C C   . GLU B 1 337 ? -77.626  25.371 7.526   1.00 93.01  ?  337 GLU B C   1 
ATOM 6090 O O   . GLU B 1 337 ? -77.414  26.050 8.537   1.00 82.78  ?  337 GLU B O   1 
ATOM 6091 C CB  . GLU B 1 337 ? -75.557  23.987 7.256   1.00 119.81 ?  337 GLU B CB  1 
ATOM 6092 C CG  . GLU B 1 337 ? -74.768  24.287 8.522   1.00 129.59 ?  337 GLU B CG  1 
ATOM 6093 C CD  . GLU B 1 337 ? -73.279  24.067 8.347   1.00 140.63 ?  337 GLU B CD  1 
ATOM 6094 O OE1 . GLU B 1 337 ? -72.870  23.602 7.262   1.00 138.83 ?  337 GLU B OE1 1 
ATOM 6095 O OE2 . GLU B 1 337 ? -72.517  24.356 9.294   1.00 142.41 -1 337 GLU B OE2 1 
ATOM 6096 N N   . ILE B 1 338 ? -78.326  25.824 6.489   1.00 93.91  ?  338 ILE B N   1 
ATOM 6097 C CA  . ILE B 1 338 ? -78.990  27.121 6.478   1.00 85.93  ?  338 ILE B CA  1 
ATOM 6098 C C   . ILE B 1 338 ? -80.458  26.904 6.811   1.00 84.37  ?  338 ILE B C   1 
ATOM 6099 O O   . ILE B 1 338 ? -81.142  26.109 6.153   1.00 90.84  ?  338 ILE B O   1 
ATOM 6100 C CB  . ILE B 1 338 ? -78.832  27.816 5.115   1.00 81.98  ?  338 ILE B CB  1 
ATOM 6101 C CG1 . ILE B 1 338 ? -77.376  27.755 4.650   1.00 75.79  ?  338 ILE B CG1 1 
ATOM 6102 C CG2 . ILE B 1 338 ? -79.305  29.257 5.197   1.00 83.10  ?  338 ILE B CG2 1 
ATOM 6103 C CD1 . ILE B 1 338 ? -76.425  28.557 5.510   1.00 89.38  ?  338 ILE B CD1 1 
ATOM 6104 N N   . HIS B 1 339 ? -80.946  27.608 7.831   1.00 77.81  ?  339 HIS B N   1 
ATOM 6105 C CA  . HIS B 1 339 ? -82.314  27.416 8.295   1.00 83.86  ?  339 HIS B CA  1 
ATOM 6106 C C   . HIS B 1 339 ? -83.328  28.250 7.523   1.00 81.63  ?  339 HIS B C   1 
ATOM 6107 O O   . HIS B 1 339 ? -84.456  27.792 7.308   1.00 71.57  ?  339 HIS B O   1 
ATOM 6108 C CB  . HIS B 1 339 ? -82.412  27.736 9.790   1.00 93.75  ?  339 HIS B CB  1 
ATOM 6109 C CG  . HIS B 1 339 ? -81.586  26.836 10.654  1.00 85.02  ?  339 HIS B CG  1 
ATOM 6110 N ND1 . HIS B 1 339 ? -80.238  27.036 10.863  1.00 80.55  ?  339 HIS B ND1 1 
ATOM 6111 C CD2 . HIS B 1 339 ? -81.915  25.727 11.359  1.00 71.44  ?  339 HIS B CD2 1 
ATOM 6112 C CE1 . HIS B 1 339 ? -79.773  26.091 11.661  1.00 83.55  ?  339 HIS B CE1 1 
ATOM 6113 N NE2 . HIS B 1 339 ? -80.770  25.284 11.976  1.00 80.80  ?  339 HIS B NE2 1 
ATOM 6114 N N   . PHE B 1 340 ? -82.959  29.456 7.101   1.00 78.88  ?  340 PHE B N   1 
ATOM 6115 C CA  . PHE B 1 340 ? -83.842  30.294 6.299   1.00 75.76  ?  340 PHE B CA  1 
ATOM 6116 C C   . PHE B 1 340 ? -82.986  31.285 5.518   1.00 77.66  ?  340 PHE B C   1 
ATOM 6117 O O   . PHE B 1 340 ? -81.759  31.308 5.642   1.00 77.30  ?  340 PHE B O   1 
ATOM 6118 C CB  . PHE B 1 340 ? -84.886  30.999 7.174   1.00 64.15  ?  340 PHE B CB  1 
ATOM 6119 C CG  . PHE B 1 340 ? -84.335  32.128 8.002   1.00 65.74  ?  340 PHE B CG  1 
ATOM 6120 C CD1 . PHE B 1 340 ? -83.799  31.888 9.256   1.00 70.47  ?  340 PHE B CD1 1 
ATOM 6121 C CD2 . PHE B 1 340 ? -84.378  33.434 7.537   1.00 63.43  ?  340 PHE B CD2 1 
ATOM 6122 C CE1 . PHE B 1 340 ? -83.300  32.925 10.023  1.00 77.53  ?  340 PHE B CE1 1 
ATOM 6123 C CE2 . PHE B 1 340 ? -83.880  34.474 8.299   1.00 63.24  ?  340 PHE B CE2 1 
ATOM 6124 C CZ  . PHE B 1 340 ? -83.342  34.219 9.544   1.00 69.40  ?  340 PHE B CZ  1 
ATOM 6125 N N   . GLN B 1 341 ? -83.647  32.104 4.705   1.00 75.31  ?  341 GLN B N   1 
ATOM 6126 C CA  . GLN B 1 341 ? -82.984  33.113 3.891   1.00 63.95  ?  341 GLN B CA  1 
ATOM 6127 C C   . GLN B 1 341 ? -83.522  34.491 4.243   1.00 66.19  ?  341 GLN B C   1 
ATOM 6128 O O   . GLN B 1 341 ? -84.717  34.653 4.513   1.00 84.43  ?  341 GLN B O   1 
ATOM 6129 C CB  . GLN B 1 341 ? -83.174  32.836 2.395   1.00 72.33  ?  341 GLN B CB  1 
ATOM 6130 C CG  . GLN B 1 341 ? -82.548  31.532 1.920   1.00 70.68  ?  341 GLN B CG  1 
ATOM 6131 C CD  . GLN B 1 341 ? -83.414  30.324 2.217   1.00 76.40  ?  341 GLN B CD  1 
ATOM 6132 O OE1 . GLN B 1 341 ? -82.915  29.273 2.618   1.00 88.45  ?  341 GLN B OE1 1 
ATOM 6133 N NE2 . GLN B 1 341 ? -84.718  30.467 2.018   1.00 87.96  ?  341 GLN B NE2 1 
ATOM 6134 N N   . PHE B 1 342 ? -82.636  35.482 4.234   1.00 63.47  ?  342 PHE B N   1 
ATOM 6135 C CA  . PHE B 1 342 ? -82.967  36.845 4.616   1.00 72.52  ?  342 PHE B CA  1 
ATOM 6136 C C   . PHE B 1 342 ? -82.854  37.773 3.414   1.00 77.38  ?  342 PHE B C   1 
ATOM 6137 O O   . PHE B 1 342 ? -82.010  37.580 2.534   1.00 92.92  ?  342 PHE B O   1 
ATOM 6138 C CB  . PHE B 1 342 ? -82.047  37.337 5.738   1.00 76.79  ?  342 PHE B CB  1 
ATOM 6139 C CG  . PHE B 1 342 ? -82.710  38.280 6.702   1.00 64.48  ?  342 PHE B CG  1 
ATOM 6140 C CD1 . PHE B 1 342 ? -82.935  39.602 6.357   1.00 58.99  ?  342 PHE B CD1 1 
ATOM 6141 C CD2 . PHE B 1 342 ? -83.100  37.845 7.958   1.00 73.57  ?  342 PHE B CD2 1 
ATOM 6142 C CE1 . PHE B 1 342 ? -83.542  40.472 7.243   1.00 66.77  ?  342 PHE B CE1 1 
ATOM 6143 C CE2 . PHE B 1 342 ? -83.708  38.709 8.849   1.00 67.30  ?  342 PHE B CE2 1 
ATOM 6144 C CZ  . PHE B 1 342 ? -83.929  40.024 8.491   1.00 78.90  ?  342 PHE B CZ  1 
ATOM 6145 N N   . ILE B 1 343 ? -83.721  38.782 3.384   1.00 65.65  ?  343 ILE B N   1 
ATOM 6146 C CA  . ILE B 1 343 ? -83.699  39.825 2.366   1.00 65.96  ?  343 ILE B CA  1 
ATOM 6147 C C   . ILE B 1 343 ? -83.749  41.168 3.079   1.00 64.01  ?  343 ILE B C   1 
ATOM 6148 O O   . ILE B 1 343 ? -84.631  41.399 3.913   1.00 80.45  ?  343 ILE B O   1 
ATOM 6149 C CB  . ILE B 1 343 ? -84.867  39.687 1.371   1.00 76.32  ?  343 ILE B CB  1 
ATOM 6150 C CG1 . ILE B 1 343 ? -84.778  38.353 0.624   1.00 62.90  ?  343 ILE B CG1 1 
ATOM 6151 C CG2 . ILE B 1 343 ? -84.872  40.846 0.388   1.00 70.62  ?  343 ILE B CG2 1 
ATOM 6152 C CD1 . ILE B 1 343 ? -85.938  38.094 -0.311  1.00 79.65  ?  343 ILE B CD1 1 
ATOM 6153 N N   . ASN B 1 344 ? -82.801  42.049 2.757   1.00 58.13  ?  344 ASN B N   1 
ATOM 6154 C CA  . ASN B 1 344 ? -82.654  43.292 3.507   1.00 82.04  ?  344 ASN B CA  1 
ATOM 6155 C C   . ASN B 1 344 ? -83.621  44.364 3.017   1.00 75.80  ?  344 ASN B C   1 
ATOM 6156 O O   . ASN B 1 344 ? -84.440  44.876 3.789   1.00 88.86  ?  344 ASN B O   1 
ATOM 6157 C CB  . ASN B 1 344 ? -81.208  43.788 3.418   1.00 100.46 ?  344 ASN B CB  1 
ATOM 6158 C CG  . ASN B 1 344 ? -80.205  42.728 3.823   1.00 95.80  ?  344 ASN B CG  1 
ATOM 6159 O OD1 . ASN B 1 344 ? -80.421  41.538 3.597   1.00 95.83  ?  344 ASN B OD1 1 
ATOM 6160 N ND2 . ASN B 1 344 ? -79.103  43.154 4.429   1.00 87.21  ?  344 ASN B ND2 1 
ATOM 6161 N N   . ASP B 1 345 ? -83.541  44.717 1.741   1.00 60.48  ?  345 ASP B N   1 
ATOM 6162 C CA  . ASP B 1 345 ? -84.335  45.797 1.172   1.00 88.48  ?  345 ASP B CA  1 
ATOM 6163 C C   . ASP B 1 345 ? -85.241  45.259 0.068   1.00 78.94  ?  345 ASP B C   1 
ATOM 6164 O O   . ASP B 1 345 ? -85.201  44.079 -0.286  1.00 72.88  ?  345 ASP B O   1 
ATOM 6165 C CB  . ASP B 1 345 ? -83.428  46.917 0.649   1.00 103.81 ?  345 ASP B CB  1 
ATOM 6166 C CG  . ASP B 1 345 ? -82.464  46.438 -0.423  1.00 101.66 ?  345 ASP B CG  1 
ATOM 6167 O OD1 . ASP B 1 345 ? -82.917  46.123 -1.543  1.00 86.31  ?  345 ASP B OD1 1 
ATOM 6168 O OD2 . ASP B 1 345 ? -81.248  46.381 -0.144  1.00 105.22 -1 345 ASP B OD2 1 
ATOM 6169 N N   . ILE B 1 346 ? -86.066  46.154 -0.477  1.00 77.54  ?  346 ILE B N   1 
ATOM 6170 C CA  . ILE B 1 346 ? -86.992  45.767 -1.534  1.00 81.55  ?  346 ILE B CA  1 
ATOM 6171 C C   . ILE B 1 346 ? -86.284  45.711 -2.885  1.00 85.00  ?  346 ILE B C   1 
ATOM 6172 O O   . ILE B 1 346 ? -86.684  44.943 -3.768  1.00 74.81  ?  346 ILE B O   1 
ATOM 6173 C CB  . ILE B 1 346 ? -88.195  46.730 -1.554  1.00 89.85  ?  346 ILE B CB  1 
ATOM 6174 C CG1 . ILE B 1 346 ? -89.196  46.341 -2.645  1.00 81.09  ?  346 ILE B CG1 1 
ATOM 6175 C CG2 . ILE B 1 346 ? -87.732  48.169 -1.729  1.00 93.99  ?  346 ILE B CG2 1 
ATOM 6176 C CD1 . ILE B 1 346 ? -89.832  44.987 -2.433  1.00 94.13  ?  346 ILE B CD1 1 
ATOM 6177 N N   . ASP B 1 347 ? -85.222  46.499 -3.068  1.00 96.67  ?  347 ASP B N   1 
ATOM 6178 C CA  . ASP B 1 347 ? -84.478  46.459 -4.324  1.00 93.51  ?  347 ASP B CA  1 
ATOM 6179 C C   . ASP B 1 347 ? -83.743  45.134 -4.481  1.00 91.45  ?  347 ASP B C   1 
ATOM 6180 O O   . ASP B 1 347 ? -83.820  44.491 -5.534  1.00 99.95  ?  347 ASP B O   1 
ATOM 6181 C CB  . ASP B 1 347 ? -83.504  47.635 -4.395  1.00 84.55  ?  347 ASP B CB  1 
ATOM 6182 C CG  . ASP B 1 347 ? -84.177  48.965 -4.123  1.00 96.89  ?  347 ASP B CG  1 
ATOM 6183 O OD1 . ASP B 1 347 ? -85.379  48.963 -3.785  1.00 91.20  ?  347 ASP B OD1 1 
ATOM 6184 O OD2 . ASP B 1 347 ? -83.507  50.011 -4.247  1.00 112.35 -1 347 ASP B OD2 1 
ATOM 6185 N N   . ASP B 1 348 ? -83.021  44.708 -3.440  1.00 94.35  ?  348 ASP B N   1 
ATOM 6186 C CA  . ASP B 1 348 ? -82.409  43.385 -3.459  1.00 100.22 ?  348 ASP B CA  1 
ATOM 6187 C C   . ASP B 1 348 ? -83.453  42.281 -3.527  1.00 87.19  ?  348 ASP B C   1 
ATOM 6188 O O   . ASP B 1 348 ? -83.144  41.173 -3.979  1.00 90.18  ?  348 ASP B O   1 
ATOM 6189 C CB  . ASP B 1 348 ? -81.521  43.190 -2.228  1.00 83.63  ?  348 ASP B CB  1 
ATOM 6190 C CG  . ASP B 1 348 ? -80.254  44.020 -2.286  1.00 97.00  ?  348 ASP B CG  1 
ATOM 6191 O OD1 . ASP B 1 348 ? -79.682  44.158 -3.388  1.00 104.15 ?  348 ASP B OD1 1 
ATOM 6192 O OD2 . ASP B 1 348 ? -79.829  44.533 -1.229  1.00 90.52  -1 348 ASP B OD2 1 
ATOM 6193 N N   . PHE B 1 349 ? -84.680  42.559 -3.083  1.00 94.41  ?  349 PHE B N   1 
ATOM 6194 C CA  . PHE B 1 349 ? -85.771  41.607 -3.262  1.00 91.29  ?  349 PHE B CA  1 
ATOM 6195 C C   . PHE B 1 349 ? -86.136  41.473 -4.734  1.00 85.81  ?  349 PHE B C   1 
ATOM 6196 O O   . PHE B 1 349 ? -86.272  40.358 -5.250  1.00 71.03  ?  349 PHE B O   1 
ATOM 6197 C CB  . PHE B 1 349 ? -86.983  42.044 -2.436  1.00 94.89  ?  349 PHE B CB  1 
ATOM 6198 C CG  . PHE B 1 349 ? -88.228  41.246 -2.707  1.00 92.30  ?  349 PHE B CG  1 
ATOM 6199 C CD1 . PHE B 1 349 ? -89.182  41.706 -3.602  1.00 87.96  ?  349 PHE B CD1 1 
ATOM 6200 C CD2 . PHE B 1 349 ? -88.448  40.039 -2.064  1.00 84.06  ?  349 PHE B CD2 1 
ATOM 6201 C CE1 . PHE B 1 349 ? -90.328  40.976 -3.853  1.00 77.14  ?  349 PHE B CE1 1 
ATOM 6202 C CE2 . PHE B 1 349 ? -89.592  39.305 -2.311  1.00 81.47  ?  349 PHE B CE2 1 
ATOM 6203 C CZ  . PHE B 1 349 ? -90.533  39.774 -3.206  1.00 76.55  ?  349 PHE B CZ  1 
ATOM 6204 N N   . ASN B 1 350 ? -86.295  42.605 -5.428  1.00 93.60  ?  350 ASN B N   1 
ATOM 6205 C CA  . ASN B 1 350 ? -86.665  42.572 -6.840  1.00 84.81  ?  350 ASN B CA  1 
ATOM 6206 C C   . ASN B 1 350 ? -85.634  41.816 -7.668  1.00 82.60  ?  350 ASN B C   1 
ATOM 6207 O O   . ASN B 1 350 ? -85.988  41.105 -8.616  1.00 91.89  ?  350 ASN B O   1 
ATOM 6208 C CB  . ASN B 1 350 ? -86.838  43.994 -7.372  1.00 82.08  ?  350 ASN B CB  1 
ATOM 6209 C CG  . ASN B 1 350 ? -87.996  44.722 -6.723  1.00 87.80  ?  350 ASN B CG  1 
ATOM 6210 O OD1 . ASN B 1 350 ? -89.068  44.152 -6.517  1.00 88.19  ?  350 ASN B OD1 1 
ATOM 6211 N ND2 . ASN B 1 350 ? -87.787  45.993 -6.400  1.00 90.40  ?  350 ASN B ND2 1 
ATOM 6212 N N   . GLU B 1 351 ? -84.352  41.955 -7.326  1.00 87.03  ?  351 GLU B N   1 
ATOM 6213 C CA  . GLU B 1 351 ? -83.298  41.240 -8.036  1.00 94.85  ?  351 GLU B CA  1 
ATOM 6214 C C   . GLU B 1 351 ? -83.275  39.752 -7.719  1.00 81.26  ?  351 GLU B C   1 
ATOM 6215 O O   . GLU B 1 351 ? -82.477  39.023 -8.318  1.00 89.02  ?  351 GLU B O   1 
ATOM 6216 C CB  . GLU B 1 351 ? -81.935  41.859 -7.717  1.00 104.58 ?  351 GLU B CB  1 
ATOM 6217 C CG  . GLU B 1 351 ? -81.746  43.260 -8.279  1.00 133.00 ?  351 GLU B CG  1 
ATOM 6218 C CD  . GLU B 1 351 ? -80.320  43.760 -8.148  1.00 144.48 ?  351 GLU B CD  1 
ATOM 6219 O OE1 . GLU B 1 351 ? -79.519  43.110 -7.443  1.00 127.18 ?  351 GLU B OE1 1 
ATOM 6220 O OE2 . GLU B 1 351 ? -80.001  44.807 -8.751  1.00 162.88 -1 351 GLU B OE2 1 
ATOM 6221 N N   . THR B 1 352 ? -84.122  39.284 -6.803  1.00 91.98  ?  352 THR B N   1 
ATOM 6222 C CA  . THR B 1 352 ? -84.153  37.873 -6.443  1.00 87.16  ?  352 THR B CA  1 
ATOM 6223 C C   . THR B 1 352 ? -85.185  37.081 -7.237  1.00 91.32  ?  352 THR B C   1 
ATOM 6224 O O   . THR B 1 352 ? -84.954  35.901 -7.526  1.00 99.18  ?  352 THR B O   1 
ATOM 6225 C CB  . THR B 1 352 ? -84.424  37.717 -4.943  1.00 86.59  ?  352 THR B CB  1 
ATOM 6226 O OG1 . THR B 1 352 ? -83.566  38.600 -4.209  1.00 84.41  ?  352 THR B OG1 1 
ATOM 6227 C CG2 . THR B 1 352 ? -84.160  36.287 -4.494  1.00 88.71  ?  352 THR B CG2 1 
ATOM 6228 N N   . LEU B 1 353 ? -86.313  37.696 -7.603  1.00 95.28  ?  353 LEU B N   1 
ATOM 6229 C CA  . LEU B 1 353 ? -87.332  36.977 -8.364  1.00 97.87  ?  353 LEU B CA  1 
ATOM 6230 C C   . LEU B 1 353 ? -86.796  36.540 -9.722  1.00 95.94  ?  353 LEU B C   1 
ATOM 6231 O O   . LEU B 1 353 ? -86.850  35.356 -10.075 1.00 90.83  ?  353 LEU B O   1 
ATOM 6232 C CB  . LEU B 1 353 ? -88.588  37.837 -8.537  1.00 106.14 ?  353 LEU B CB  1 
ATOM 6233 C CG  . LEU B 1 353 ? -89.348  38.355 -7.311  1.00 79.64  ?  353 LEU B CG  1 
ATOM 6234 C CD1 . LEU B 1 353 ? -89.353  37.334 -6.176  1.00 72.70  ?  353 LEU B CD1 1 
ATOM 6235 C CD2 . LEU B 1 353 ? -88.807  39.695 -6.852  1.00 62.60  ?  353 LEU B CD2 1 
ATOM 6236 N N   . ASN B 1 354 ? -86.270  37.488 -10.505 1.00 108.77 ?  354 ASN B N   1 
ATOM 6237 C CA  . ASN B 1 354 ? -85.733  37.150 -11.819 1.00 116.88 ?  354 ASN B CA  1 
ATOM 6238 C C   . ASN B 1 354 ? -84.549  36.195 -11.728 1.00 110.56 ?  354 ASN B C   1 
ATOM 6239 O O   . ASN B 1 354 ? -84.186  35.577 -12.735 1.00 118.75 ?  354 ASN B O   1 
ATOM 6240 C CB  . ASN B 1 354 ? -85.329  38.421 -12.568 1.00 114.48 ?  354 ASN B CB  1 
ATOM 6241 C CG  . ASN B 1 354 ? -84.611  39.417 -11.681 1.00 115.72 ?  354 ASN B CG  1 
ATOM 6242 O OD1 . ASN B 1 354 ? -84.722  39.367 -10.457 1.00 114.81 ?  354 ASN B OD1 1 
ATOM 6243 N ND2 . ASN B 1 354 ? -83.873  40.334 -12.297 1.00 126.18 ?  354 ASN B ND2 1 
ATOM 6244 N N   . SER B 1 355 ? -83.941  36.064 -10.549 1.00 101.64 ?  355 SER B N   1 
ATOM 6245 C CA  . SER B 1 355 ? -82.896  35.075 -10.320 1.00 104.50 ?  355 SER B CA  1 
ATOM 6246 C C   . SER B 1 355 ? -83.450  33.705 -9.953  1.00 103.53 ?  355 SER B C   1 
ATOM 6247 O O   . SER B 1 355 ? -82.743  32.703 -10.111 1.00 101.14 ?  355 SER B O   1 
ATOM 6248 C CB  . SER B 1 355 ? -81.951  35.551 -9.212  1.00 100.50 ?  355 SER B CB  1 
ATOM 6249 O OG  . SER B 1 355 ? -81.501  36.876 -9.450  1.00 111.11 ?  355 SER B OG  1 
ATOM 6250 N N   . ILE B 1 356 ? -84.688  33.637 -9.464  1.00 96.17  ?  356 ILE B N   1 
ATOM 6251 C CA  . ILE B 1 356 ? -85.340  32.378 -9.117  1.00 87.02  ?  356 ILE B CA  1 
ATOM 6252 C C   . ILE B 1 356 ? -86.113  31.878 -10.329 1.00 100.55 ?  356 ILE B C   1 
ATOM 6253 O O   . ILE B 1 356 ? -86.747  32.663 -11.045 1.00 111.56 ?  356 ILE B O   1 
ATOM 6254 C CB  . ILE B 1 356 ? -86.263  32.562 -7.896  1.00 96.16  ?  356 ILE B CB  1 
ATOM 6255 C CG1 . ILE B 1 356 ? -85.439  32.812 -6.633  1.00 84.24  ?  356 ILE B CG1 1 
ATOM 6256 C CG2 . ILE B 1 356 ? -87.161  31.346 -7.703  1.00 97.46  ?  356 ILE B CG2 1 
ATOM 6257 C CD1 . ILE B 1 356 ? -84.587  31.634 -6.224  1.00 77.08  ?  356 ILE B CD1 1 
ATOM 6258 N N   . ASN B 1 357 ? -86.058  30.569 -10.571 1.00 109.01 ?  357 ASN B N   1 
ATOM 6259 C CA  . ASN B 1 357 ? -86.726  29.951 -11.712 1.00 113.33 ?  357 ASN B CA  1 
ATOM 6260 C C   . ASN B 1 357 ? -87.605  28.790 -11.265 1.00 109.16 ?  357 ASN B C   1 
ATOM 6261 O O   . ASN B 1 357 ? -87.718  27.768 -11.949 1.00 108.57 ?  357 ASN B O   1 
ATOM 6262 C CB  . ASN B 1 357 ? -85.709  29.492 -12.756 1.00 107.44 ?  357 ASN B CB  1 
ATOM 6263 C CG  . ASN B 1 357 ? -84.930  30.648 -13.364 1.00 105.77 ?  357 ASN B CG  1 
ATOM 6264 O OD1 . ASN B 1 357 ? -85.419  31.776 -13.431 1.00 99.07  ?  357 ASN B OD1 1 
ATOM 6265 N ND2 . ASN B 1 357 ? -83.711  30.369 -13.812 1.00 109.17 ?  357 ASN B ND2 1 
ATOM 6266 N N   . ILE B 1 358 ? -88.246  28.930 -10.107 1.00 102.33 ?  358 ILE B N   1 
ATOM 6267 C CA  . ILE B 1 358 ? -89.182  27.948 -9.589  1.00 96.73  ?  358 ILE B CA  1 
ATOM 6268 C C   . ILE B 1 358 ? -90.468  28.690 -9.223  1.00 85.76  ?  358 ILE B C   1 
ATOM 6269 O O   . ILE B 1 358 ? -90.527  29.916 -9.293  1.00 80.55  ?  358 ILE B O   1 
ATOM 6270 C CB  . ILE B 1 358 ? -88.606  27.188 -8.376  1.00 87.35  ?  358 ILE B CB  1 
ATOM 6271 C CG1 . ILE B 1 358 ? -87.189  26.697 -8.681  1.00 111.89 ?  358 ILE B CG1 1 
ATOM 6272 C CG2 . ILE B 1 358 ? -89.431  25.955 -8.100  1.00 86.47  ?  358 ILE B CG2 1 
ATOM 6273 C CD1 . ILE B 1 358 ? -86.544  25.928 -7.549  1.00 123.24 ?  358 ILE B CD1 1 
ATOM 6274 N N   . ARG B 1 359 ? -91.505  27.942 -8.844  1.00 69.40  ?  359 ARG B N   1 
ATOM 6275 C CA  . ARG B 1 359 ? -92.729  28.548 -8.329  1.00 82.02  ?  359 ARG B CA  1 
ATOM 6276 C C   . ARG B 1 359 ? -92.420  29.509 -7.187  1.00 89.38  ?  359 ARG B C   1 
ATOM 6277 O O   . ARG B 1 359 ? -91.686  29.167 -6.256  1.00 82.66  ?  359 ARG B O   1 
ATOM 6278 C CB  . ARG B 1 359 ? -93.679  27.453 -7.849  1.00 91.01  ?  359 ARG B CB  1 
ATOM 6279 C CG  . ARG B 1 359 ? -94.800  27.926 -6.940  1.00 90.05  ?  359 ARG B CG  1 
ATOM 6280 C CD  . ARG B 1 359 ? -96.086  28.145 -7.702  1.00 94.63  ?  359 ARG B CD  1 
ATOM 6281 N NE  . ARG B 1 359 ? -97.171  28.557 -6.818  1.00 93.01  ?  359 ARG B NE  1 
ATOM 6282 C CZ  . ARG B 1 359 ? -98.421  28.733 -7.225  1.00 97.51  ?  359 ARG B CZ  1 
ATOM 6283 N NH1 . ARG B 1 359 ? -98.727  28.528 -8.498  1.00 99.76  ?  359 ARG B NH1 1 
ATOM 6284 N NH2 . ARG B 1 359 ? -99.363  29.102 -6.367  1.00 90.33  ?  359 ARG B NH2 1 
ATOM 6285 N N   . LYS B 1 360 ? -92.986  30.713 -7.252  1.00 86.28  ?  360 LYS B N   1 
ATOM 6286 C CA  . LYS B 1 360 ? -92.764  31.741 -6.240  1.00 77.06  ?  360 LYS B CA  1 
ATOM 6287 C C   . LYS B 1 360 ? -94.103  32.144 -5.640  1.00 78.45  ?  360 LYS B C   1 
ATOM 6288 O O   . LYS B 1 360 ? -95.023  32.524 -6.372  1.00 81.32  ?  360 LYS B O   1 
ATOM 6289 C CB  . LYS B 1 360 ? -92.072  32.964 -6.841  1.00 80.11  ?  360 LYS B CB  1 
ATOM 6290 C CG  . LYS B 1 360 ? -90.917  32.630 -7.756  1.00 81.82  ?  360 LYS B CG  1 
ATOM 6291 C CD  . LYS B 1 360 ? -90.469  33.847 -8.541  1.00 83.50  ?  360 LYS B CD  1 
ATOM 6292 C CE  . LYS B 1 360 ? -89.518  33.443 -9.651  1.00 78.77  ?  360 LYS B CE  1 
ATOM 6293 N NZ  . LYS B 1 360 ? -89.095  34.608 -10.470 1.00 91.61  ?  360 LYS B NZ  1 
ATOM 6294 N N   . GLU B 1 361 ? -94.207  32.071 -4.316  1.00 84.99  ?  361 GLU B N   1 
ATOM 6295 C CA  . GLU B 1 361 ? -95.388  32.516 -3.592  1.00 80.20  ?  361 GLU B CA  1 
ATOM 6296 C C   . GLU B 1 361 ? -95.022  33.694 -2.698  1.00 75.39  ?  361 GLU B C   1 
ATOM 6297 O O   . GLU B 1 361 ? -93.886  33.807 -2.230  1.00 81.33  ?  361 GLU B O   1 
ATOM 6298 C CB  . GLU B 1 361 ? -95.985  31.381 -2.753  1.00 78.34  ?  361 GLU B CB  1 
ATOM 6299 C CG  . GLU B 1 361 ? -96.268  30.109 -3.540  1.00 79.69  ?  361 GLU B CG  1 
ATOM 6300 C CD  . GLU B 1 361 ? -97.036  29.079 -2.734  1.00 101.31 ?  361 GLU B CD  1 
ATOM 6301 O OE1 . GLU B 1 361 ? -97.563  29.434 -1.660  1.00 113.87 ?  361 GLU B OE1 1 
ATOM 6302 O OE2 . GLU B 1 361 ? -97.112  27.913 -3.174  1.00 110.52 -1 361 GLU B OE2 1 
ATOM 6303 N N   . VAL B 1 362 ? -95.990  34.577 -2.468  1.00 69.45  ?  362 VAL B N   1 
ATOM 6304 C CA  . VAL B 1 362 ? -95.760  35.803 -1.713  1.00 67.58  ?  362 VAL B CA  1 
ATOM 6305 C C   . VAL B 1 362 ? -96.839  35.931 -0.649  1.00 66.75  ?  362 VAL B C   1 
ATOM 6306 O O   . VAL B 1 362 ? -98.033  35.962 -0.970  1.00 91.87  ?  362 VAL B O   1 
ATOM 6307 C CB  . VAL B 1 362 ? -95.749  37.046 -2.617  1.00 71.49  ?  362 VAL B CB  1 
ATOM 6308 C CG1 . VAL B 1 362 ? -95.616  38.297 -1.777  1.00 62.26  ?  362 VAL B CG1 1 
ATOM 6309 C CG2 . VAL B 1 362 ? -94.617  36.961 -3.627  1.00 77.78  ?  362 VAL B CG2 1 
ATOM 6310 N N   . TYR B 1 363 ? -96.421  36.003 0.612   1.00 66.24  ?  363 TYR B N   1 
ATOM 6311 C CA  . TYR B 1 363 ? -97.312  36.268 1.734   1.00 57.87  ?  363 TYR B CA  1 
ATOM 6312 C C   . TYR B 1 363 ? -96.836  37.538 2.420   1.00 69.03  ?  363 TYR B C   1 
ATOM 6313 O O   . TYR B 1 363 ? -95.738  37.564 2.986   1.00 83.78  ?  363 TYR B O   1 
ATOM 6314 C CB  . TYR B 1 363 ? -97.327  35.104 2.726   1.00 60.58  ?  363 TYR B CB  1 
ATOM 6315 C CG  . TYR B 1 363 ? -97.533  33.746 2.097   1.00 80.99  ?  363 TYR B CG  1 
ATOM 6316 C CD1 . TYR B 1 363 ? -98.802  33.196 1.983   1.00 88.40  ?  363 TYR B CD1 1 
ATOM 6317 C CD2 . TYR B 1 363 ? -96.454  33.008 1.628   1.00 83.03  ?  363 TYR B CD2 1 
ATOM 6318 C CE1 . TYR B 1 363 ? -98.992  31.953 1.412   1.00 101.81 ?  363 TYR B CE1 1 
ATOM 6319 C CE2 . TYR B 1 363 ? -96.633  31.767 1.056   1.00 85.15  ?  363 TYR B CE2 1 
ATOM 6320 C CZ  . TYR B 1 363 ? -97.901  31.245 0.951   1.00 100.86 ?  363 TYR B CZ  1 
ATOM 6321 O OH  . TYR B 1 363 ? -98.073  30.008 0.380   1.00 109.28 ?  363 TYR B OH  1 
ATOM 6322 N N   . GLN B 1 364 ? -97.649  38.588 2.367   1.00 67.84  ?  364 GLN B N   1 
ATOM 6323 C CA  . GLN B 1 364 ? -97.314  39.851 3.005   1.00 62.21  ?  364 GLN B CA  1 
ATOM 6324 C C   . GLN B 1 364 ? -98.292  40.137 4.134   1.00 63.95  ?  364 GLN B C   1 
ATOM 6325 O O   . GLN B 1 364 ? -99.495  39.891 4.007   1.00 73.81  ?  364 GLN B O   1 
ATOM 6326 C CB  . GLN B 1 364 ? -97.326  41.015 2.008   1.00 56.97  ?  364 GLN B CB  1 
ATOM 6327 C CG  . GLN B 1 364 ? -97.045  42.361 2.662   1.00 72.92  ?  364 GLN B CG  1 
ATOM 6328 C CD  . GLN B 1 364 ? -96.851  43.475 1.661   1.00 89.81  ?  364 GLN B CD  1 
ATOM 6329 O OE1 . GLN B 1 364 ? -96.754  44.645 2.029   1.00 99.43  ?  364 GLN B OE1 1 
ATOM 6330 N NE2 . GLN B 1 364 ? -96.798  43.120 0.386   1.00 85.23  ?  364 GLN B NE2 1 
ATOM 6331 N N   . PHE B 1 365 ? -97.763  40.653 5.239   1.00 76.14  ?  365 PHE B N   1 
ATOM 6332 C CA  . PHE B 1 365 ? -98.559  41.148 6.351   1.00 79.03  ?  365 PHE B CA  1 
ATOM 6333 C C   . PHE B 1 365 ? -98.163  42.591 6.626   1.00 76.71  ?  365 PHE B C   1 
ATOM 6334 O O   . PHE B 1 365 ? -96.986  42.949 6.528   1.00 77.43  ?  365 PHE B O   1 
ATOM 6335 C CB  . PHE B 1 365 ? -98.361  40.294 7.608   1.00 54.30  ?  365 PHE B CB  1 
ATOM 6336 C CG  . PHE B 1 365 ? -98.666  38.836 7.406   1.00 69.13  ?  365 PHE B CG  1 
ATOM 6337 C CD1 . PHE B 1 365 ? -99.954  38.358 7.575   1.00 73.99  ?  365 PHE B CD1 1 
ATOM 6338 C CD2 . PHE B 1 365 ? -97.668  37.944 7.047   1.00 78.90  ?  365 PHE B CD2 1 
ATOM 6339 C CE1 . PHE B 1 365 ? -100.242 37.019 7.393   1.00 86.09  ?  365 PHE B CE1 1 
ATOM 6340 C CE2 . PHE B 1 365 ? -97.950  36.603 6.863   1.00 73.53  ?  365 PHE B CE2 1 
ATOM 6341 C CZ  . PHE B 1 365 ? -99.239  36.140 7.036   1.00 62.99  ?  365 PHE B CZ  1 
ATOM 6342 N N   . TYR B 1 366 ? -99.148  43.418 6.963   1.00 65.26  ?  366 TYR B N   1 
ATOM 6343 C CA  . TYR B 1 366 ? -98.888  44.831 7.194   1.00 73.60  ?  366 TYR B CA  1 
ATOM 6344 C C   . TYR B 1 366 ? -99.949  45.383 8.132   1.00 94.11  ?  366 TYR B C   1 
ATOM 6345 O O   . TYR B 1 366 ? -101.008 44.780 8.327   1.00 96.81  ?  366 TYR B O   1 
ATOM 6346 C CB  . TYR B 1 366 ? -98.864  45.619 5.879   1.00 95.77  ?  366 TYR B CB  1 
ATOM 6347 C CG  . TYR B 1 366 ? -100.236 45.986 5.355   1.00 97.64  ?  366 TYR B CG  1 
ATOM 6348 C CD1 . TYR B 1 366 ? -100.996 45.068 4.642   1.00 79.85  ?  366 TYR B CD1 1 
ATOM 6349 C CD2 . TYR B 1 366 ? -100.767 47.253 5.565   1.00 95.40  ?  366 TYR B CD2 1 
ATOM 6350 C CE1 . TYR B 1 366 ? -102.249 45.398 4.160   1.00 75.55  ?  366 TYR B CE1 1 
ATOM 6351 C CE2 . TYR B 1 366 ? -102.018 47.592 5.087   1.00 97.74  ?  366 TYR B CE2 1 
ATOM 6352 C CZ  . TYR B 1 366 ? -102.754 46.661 4.385   1.00 90.89  ?  366 TYR B CZ  1 
ATOM 6353 O OH  . TYR B 1 366 ? -104.000 46.996 3.907   1.00 91.56  ?  366 TYR B OH  1 
ATOM 6354 N N   . THR B 1 367 ? -99.645  46.540 8.716   1.00 111.96 ?  367 THR B N   1 
ATOM 6355 C CA  . THR B 1 367 ? -100.578 47.254 9.579   1.00 106.32 ?  367 THR B CA  1 
ATOM 6356 C C   . THR B 1 367 ? -100.916 48.637 9.049   1.00 111.50 ?  367 THR B C   1 
ATOM 6357 O O   . THR B 1 367 ? -102.094 49.012 9.013   1.00 117.03 ?  367 THR B O   1 
ATOM 6358 C CB  . THR B 1 367 ? -100.011 47.367 11.005  1.00 101.72 ?  367 THR B CB  1 
ATOM 6359 O OG1 . THR B 1 367 ? -98.952  48.332 11.028  1.00 129.73 ?  367 THR B OG1 1 
ATOM 6360 C CG2 . THR B 1 367 ? -99.480  46.024 11.483  1.00 82.28  ?  367 THR B CG2 1 
ATOM 6361 N N   . GLU B 1 368 ? -99.914  49.411 8.632   1.00 110.12 ?  368 GLU B N   1 
ATOM 6362 C CA  . GLU B 1 368 ? -100.120 50.784 8.189   1.00 113.16 ?  368 GLU B CA  1 
ATOM 6363 C C   . GLU B 1 368 ? -99.781  50.989 6.722   1.00 115.15 ?  368 GLU B C   1 
ATOM 6364 O O   . GLU B 1 368 ? -100.598 51.542 5.975   1.00 127.75 ?  368 GLU B O   1 
ATOM 6365 C CB  . GLU B 1 368 ? -99.293  51.743 9.062   1.00 133.39 ?  368 GLU B CB  1 
ATOM 6366 C CG  . GLU B 1 368 ? -99.830  51.905 10.477  1.00 134.77 ?  368 GLU B CG  1 
ATOM 6367 C CD  . GLU B 1 368 ? -98.856  52.617 11.397  1.00 138.26 ?  368 GLU B CD  1 
ATOM 6368 O OE1 . GLU B 1 368 ? -97.730  52.111 11.581  1.00 130.00 ?  368 GLU B OE1 1 
ATOM 6369 O OE2 . GLU B 1 368 ? -99.217  53.684 11.937  1.00 147.28 -1 368 GLU B OE2 1 
ATOM 6370 N N   . ASN B 1 369 ? -98.600  50.563 6.282   1.00 112.16 ?  369 ASN B N   1 
ATOM 6371 C CA  . ASN B 1 369 ? -98.166  50.737 4.903   1.00 114.53 ?  369 ASN B CA  1 
ATOM 6372 C C   . ASN B 1 369 ? -97.880  49.382 4.272   1.00 113.66 ?  369 ASN B C   1 
ATOM 6373 O O   . ASN B 1 369 ? -97.258  48.514 4.893   1.00 95.36  ?  369 ASN B O   1 
ATOM 6374 C CB  . ASN B 1 369 ? -96.919  51.626 4.822   1.00 109.30 ?  369 ASN B CB  1 
ATOM 6375 C CG  . ASN B 1 369 ? -97.207  53.067 5.197   1.00 127.81 ?  369 ASN B CG  1 
ATOM 6376 O OD1 . ASN B 1 369 ? -97.018  53.471 6.345   1.00 139.21 ?  369 ASN B OD1 1 
ATOM 6377 N ND2 . ASN B 1 369 ? -97.669  53.851 4.230   1.00 115.57 ?  369 ASN B ND2 1 
ATOM 6378 N N   . CYS B 1 370 ? -98.335  49.210 3.036   1.00 119.97 ?  370 CYS B N   1 
ATOM 6379 C CA  . CYS B 1 370 ? -98.144  47.990 2.268   1.00 98.30  ?  370 CYS B CA  1 
ATOM 6380 C C   . CYS B 1 370 ? -97.090  48.225 1.189   1.00 101.37 ?  370 CYS B C   1 
ATOM 6381 O O   . CYS B 1 370 ? -96.600  49.342 0.994   1.00 104.92 ?  370 CYS B O   1 
ATOM 6382 C CB  . CYS B 1 370 ? -99.470  47.526 1.661   1.00 96.57  ?  370 CYS B CB  1 
ATOM 6383 S SG  . CYS B 1 370 ? -99.412  45.906 0.863   1.00 99.91  ?  370 CYS B SG  1 
ATOM 6384 N N   . LEU B 1 371 ? -96.743  47.155 0.479   1.00 95.78  ?  371 LEU B N   1 
ATOM 6385 C CA  . LEU B 1 371 ? -95.706  47.194 -0.544  1.00 104.13 ?  371 LEU B CA  1 
ATOM 6386 C C   . LEU B 1 371 ? -96.293  46.790 -1.887  1.00 120.90 ?  371 LEU B C   1 
ATOM 6387 O O   . LEU B 1 371 ? -96.967  45.760 -1.991  1.00 113.93 ?  371 LEU B O   1 
ATOM 6388 C CB  . LEU B 1 371 ? -94.539  46.273 -0.179  1.00 81.03  ?  371 LEU B CB  1 
ATOM 6389 C CG  . LEU B 1 371 ? -93.725  46.676 1.051   1.00 79.86  ?  371 LEU B CG  1 
ATOM 6390 C CD1 . LEU B 1 371 ? -92.575  45.709 1.270   1.00 60.67  ?  371 LEU B CD1 1 
ATOM 6391 C CD2 . LEU B 1 371 ? -93.214  48.103 0.914   1.00 95.12  ?  371 LEU B CD2 1 
ATOM 6392 N N   . ASP B 1 372 ? -96.038  47.606 -2.909  1.00 136.20 ?  372 ASP B N   1 
ATOM 6393 C CA  . ASP B 1 372 ? -96.459  47.267 -4.261  1.00 121.57 ?  372 ASP B CA  1 
ATOM 6394 C C   . ASP B 1 372 ? -95.747  46.007 -4.733  1.00 113.66 ?  372 ASP B C   1 
ATOM 6395 O O   . ASP B 1 372 ? -94.517  45.915 -4.679  1.00 127.44 ?  372 ASP B O   1 
ATOM 6396 C CB  . ASP B 1 372 ? -96.171  48.427 -5.214  1.00 140.10 ?  372 ASP B CB  1 
ATOM 6397 C CG  . ASP B 1 372 ? -97.227  49.511 -5.149  1.00 143.63 ?  372 ASP B CG  1 
ATOM 6398 O OD1 . ASP B 1 372 ? -98.429  49.173 -5.171  1.00 148.92 ?  372 ASP B OD1 1 
ATOM 6399 O OD2 . ASP B 1 372 ? -96.856  50.702 -5.081  1.00 149.80 -1 372 ASP B OD2 1 
ATOM 6400 N N   . ILE B 1 373 ? -96.525  45.035 -5.195  1.00 117.92 ?  373 ILE B N   1 
ATOM 6401 C CA  . ILE B 1 373 ? -95.987  43.753 -5.637  1.00 106.55 ?  373 ILE B CA  1 
ATOM 6402 C C   . ILE B 1 373 ? -96.535  43.457 -7.027  1.00 115.88 ?  373 ILE B C   1 
ATOM 6403 O O   . ILE B 1 373 ? -97.741  43.624 -7.262  1.00 112.62 ?  373 ILE B O   1 
ATOM 6404 C CB  . ILE B 1 373 ? -96.327  42.640 -4.633  1.00 109.00 ?  373 ILE B CB  1 
ATOM 6405 C CG1 . ILE B 1 373 ? -95.527  42.843 -3.346  1.00 113.42 ?  373 ILE B CG1 1 
ATOM 6406 C CG2 . ILE B 1 373 ? -96.057  41.263 -5.225  1.00 111.74 ?  373 ILE B CG2 1 
ATOM 6407 C CD1 . ILE B 1 373 ? -95.717  41.755 -2.336  1.00 96.13  ?  373 ILE B CD1 1 
ATOM 6408 N N   . PRO B 1 374 ? -95.694  43.041 -7.976  1.00 107.81 ?  374 PRO B N   1 
ATOM 6409 C CA  . PRO B 1 374 ? -96.181  42.801 -9.340  1.00 118.20 ?  374 PRO B CA  1 
ATOM 6410 C C   . PRO B 1 374 ? -97.295  41.765 -9.368  1.00 111.44 ?  374 PRO B C   1 
ATOM 6411 O O   . PRO B 1 374 ? -97.243  40.745 -8.677  1.00 98.64  ?  374 PRO B O   1 
ATOM 6412 C CB  . PRO B 1 374 ? -94.932  42.309 -10.083 1.00 116.49 ?  374 PRO B CB  1 
ATOM 6413 C CG  . PRO B 1 374 ? -93.976  41.884 -9.007  1.00 112.13 ?  374 PRO B CG  1 
ATOM 6414 C CD  . PRO B 1 374 ? -94.248  42.798 -7.858  1.00 92.99  ?  374 PRO B CD  1 
ATOM 6415 N N   . SER B 1 375 ? -98.316  42.046 -10.181 1.00 113.28 ?  375 SER B N   1 
ATOM 6416 C CA  . SER B 1 375 ? -99.476  41.169 -10.293 1.00 123.57 ?  375 SER B CA  1 
ATOM 6417 C C   . SER B 1 375 ? -99.137  39.812 -10.896 1.00 124.80 ?  375 SER B C   1 
ATOM 6418 O O   . SER B 1 375 ? -100.002 38.929 -10.911 1.00 131.24 ?  375 SER B O   1 
ATOM 6419 C CB  . SER B 1 375 ? -100.561 41.850 -11.130 1.00 134.36 ?  375 SER B CB  1 
ATOM 6420 O OG  . SER B 1 375 ? -100.026 42.352 -12.342 1.00 127.35 ?  375 SER B OG  1 
ATOM 6421 N N   . GLN B 1 376 ? -97.912  39.628 -11.394 1.00 124.12 ?  376 GLN B N   1 
ATOM 6422 C CA  . GLN B 1 376 ? -97.525  38.350 -11.982 1.00 114.87 ?  376 GLN B CA  1 
ATOM 6423 C C   . GLN B 1 376 ? -97.558  37.224 -10.957 1.00 100.36 ?  376 GLN B C   1 
ATOM 6424 O O   . GLN B 1 376 ? -97.886  36.082 -11.299 1.00 93.18  ?  376 GLN B O   1 
ATOM 6425 C CB  . GLN B 1 376 ? -96.128  38.463 -12.592 1.00 109.29 ?  376 GLN B CB  1 
ATOM 6426 C CG  . GLN B 1 376 ? -95.842  39.804 -13.248 1.00 117.56 ?  376 GLN B CG  1 
ATOM 6427 C CD  . GLN B 1 376 ? -94.367  40.007 -13.535 1.00 150.61 ?  376 GLN B CD  1 
ATOM 6428 O OE1 . GLN B 1 376 ? -93.590  39.052 -13.559 1.00 156.83 ?  376 GLN B OE1 1 
ATOM 6429 N NE2 . GLN B 1 376 ? -93.971  41.257 -13.743 1.00 137.08 ?  376 GLN B NE2 1 
ATOM 6430 N N   . LEU B 1 377 ? -97.225  37.525 -9.693  1.00 109.36 ?  377 LEU B N   1 
ATOM 6431 C CA  . LEU B 1 377 ? -97.076  36.541 -8.633  1.00 91.98  ?  377 LEU B CA  1 
ATOM 6432 C C   . LEU B 1 377 ? -98.370  36.385 -7.839  1.00 83.04  ?  377 LEU B C   1 
ATOM 6433 O O   . LEU B 1 377 ? -99.156  37.332 -7.725  1.00 95.27  ?  377 LEU B O   1 
ATOM 6434 C CB  . LEU B 1 377 ? -95.951  36.950 -7.688  1.00 91.33  ?  377 LEU B CB  1 
ATOM 6435 C CG  . LEU B 1 377 ? -94.544  36.604 -8.171  1.00 89.52  ?  377 LEU B CG  1 
ATOM 6436 C CD1 . LEU B 1 377 ? -93.499  37.052 -7.162  1.00 66.49  ?  377 LEU B CD1 1 
ATOM 6437 C CD2 . LEU B 1 377 ? -94.433  35.115 -8.451  1.00 74.09  ?  377 LEU B CD2 1 
ATOM 6438 N N   . PRO B 1 378 ? -98.613  35.196 -7.279  1.00 77.54  ?  378 PRO B N   1 
ATOM 6439 C CA  . PRO B 1 378 ? -99.788  35.015 -6.417  1.00 98.10  ?  378 PRO B CA  1 
ATOM 6440 C C   . PRO B 1 378 ? -99.611  35.677 -5.059  1.00 89.68  ?  378 PRO B C   1 
ATOM 6441 O O   . PRO B 1 378 ? -99.449  34.995 -4.042  1.00 81.88  ?  378 PRO B O   1 
ATOM 6442 C CB  . PRO B 1 378 ? -99.898  33.491 -6.296  1.00 90.35  ?  378 PRO B CB  1 
ATOM 6443 C CG  . PRO B 1 378 ? -98.495  33.010 -6.461  1.00 69.44  ?  378 PRO B CG  1 
ATOM 6444 C CD  . PRO B 1 378 ? -97.865  33.939 -7.466  1.00 76.91  ?  378 PRO B CD  1 
ATOM 6445 N N   . GLN B 1 379 ? -99.642  37.006 -5.033  1.00 87.37  ?  379 GLN B N   1 
ATOM 6446 C CA  . GLN B 1 379 ? -99.444  37.738 -3.792  1.00 69.41  ?  379 GLN B CA  1 
ATOM 6447 C C   . GLN B 1 379 ? -100.636 37.560 -2.857  1.00 73.97  ?  379 GLN B C   1 
ATOM 6448 O O   . GLN B 1 379 ? -101.785 37.434 -3.289  1.00 91.90  ?  379 GLN B O   1 
ATOM 6449 C CB  . GLN B 1 379 ? -99.222  39.223 -4.079  1.00 74.26  ?  379 GLN B CB  1 
ATOM 6450 C CG  . GLN B 1 379 ? -100.189 39.808 -5.095  1.00 74.07  ?  379 GLN B CG  1 
ATOM 6451 C CD  . GLN B 1 379 ? -100.090 41.317 -5.195  1.00 109.05 ?  379 GLN B CD  1 
ATOM 6452 O OE1 . GLN B 1 379 ? -99.955  42.011 -4.188  1.00 108.91 ?  379 GLN B OE1 1 
ATOM 6453 N NE2 . GLN B 1 379 ? -100.158 41.834 -6.416  1.00 120.35 ?  379 GLN B NE2 1 
ATOM 6454 N N   . VAL B 1 380 ? -100.345 37.543 -1.557  1.00 81.43  ?  380 VAL B N   1 
ATOM 6455 C CA  . VAL B 1 380 ? -101.356 37.444 -0.508  1.00 70.29  ?  380 VAL B CA  1 
ATOM 6456 C C   . VAL B 1 380 ? -101.020 38.523 0.515   1.00 63.01  ?  380 VAL B C   1 
ATOM 6457 O O   . VAL B 1 380 ? -100.148 38.328 1.370   1.00 84.03  ?  380 VAL B O   1 
ATOM 6458 C CB  . VAL B 1 380 ? -101.400 36.056 0.141   1.00 66.47  ?  380 VAL B CB  1 
ATOM 6459 C CG1 . VAL B 1 380 ? -102.471 36.009 1.220   1.00 55.31  ?  380 VAL B CG1 1 
ATOM 6460 C CG2 . VAL B 1 380 ? -101.657 34.985 -0.910  1.00 82.30  ?  380 VAL B CG2 1 
ATOM 6461 N N   . ASN B 1 381 ? -101.701 39.662 0.430   1.00 55.14  ?  381 ASN B N   1 
ATOM 6462 C CA  . ASN B 1 381 ? -101.463 40.801 1.307   1.00 59.47  ?  381 ASN B CA  1 
ATOM 6463 C C   . ASN B 1 381 ? -102.587 40.891 2.329   1.00 65.82  ?  381 ASN B C   1 
ATOM 6464 O O   . ASN B 1 381 ? -103.766 40.803 1.969   1.00 98.49  ?  381 ASN B O   1 
ATOM 6465 C CB  . ASN B 1 381 ? -101.367 42.095 0.498   1.00 69.44  ?  381 ASN B CB  1 
ATOM 6466 C CG  . ASN B 1 381 ? -100.691 41.890 -0.845  1.00 88.08  ?  381 ASN B CG  1 
ATOM 6467 O OD1 . ASN B 1 381 ? -99.793  41.057 -0.978  1.00 83.19  ?  381 ASN B OD1 1 
ATOM 6468 N ND2 . ASN B 1 381 ? -101.123 42.645 -1.848  1.00 110.97 ?  381 ASN B ND2 1 
ATOM 6469 N N   . ILE B 1 382 ? -102.224 41.070 3.598   1.00 66.14  ?  382 ILE B N   1 
ATOM 6470 C CA  . ILE B 1 382 ? -103.181 41.023 4.699   1.00 73.94  ?  382 ILE B CA  1 
ATOM 6471 C C   . ILE B 1 382 ? -102.896 42.165 5.664   1.00 84.31  ?  382 ILE B C   1 
ATOM 6472 O O   . ILE B 1 382 ? -101.757 42.340 6.109   1.00 93.90  ?  382 ILE B O   1 
ATOM 6473 C CB  . ILE B 1 382 ? -103.128 39.672 5.441   1.00 69.55  ?  382 ILE B CB  1 
ATOM 6474 C CG1 . ILE B 1 382 ? -103.705 38.555 4.569   1.00 67.82  ?  382 ILE B CG1 1 
ATOM 6475 C CG2 . ILE B 1 382 ? -103.870 39.757 6.768   1.00 75.59  ?  382 ILE B CG2 1 
ATOM 6476 C CD1 . ILE B 1 382 ? -103.671 37.193 5.226   1.00 76.81  ?  382 ILE B CD1 1 
ATOM 6477 N N   . GLN B 1 383 ? -103.930 42.937 5.987   1.00 76.72  ?  383 GLN B N   1 
ATOM 6478 C CA  . GLN B 1 383 ? -103.863 43.931 7.046   1.00 78.63  ?  383 GLN B CA  1 
ATOM 6479 C C   . GLN B 1 383 ? -104.227 43.290 8.380   1.00 82.77  ?  383 GLN B C   1 
ATOM 6480 O O   . GLN B 1 383 ? -105.065 42.387 8.447   1.00 91.93  ?  383 GLN B O   1 
ATOM 6481 C CB  . GLN B 1 383 ? -104.805 45.102 6.754   1.00 69.45  ?  383 GLN B CB  1 
ATOM 6482 C CG  . GLN B 1 383 ? -104.482 46.378 7.518   1.00 71.35  ?  383 GLN B CG  1 
ATOM 6483 C CD  . GLN B 1 383 ? -105.430 47.514 7.181   1.00 97.45  ?  383 GLN B CD  1 
ATOM 6484 O OE1 . GLN B 1 383 ? -106.608 47.292 6.900   1.00 108.10 ?  383 GLN B OE1 1 
ATOM 6485 N NE2 . GLN B 1 383 ? -104.919 48.740 7.207   1.00 94.16  ?  383 GLN B NE2 1 
ATOM 6486 N N   . VAL B 1 384 ? -103.587 43.767 9.448   1.00 80.09  ?  384 VAL B N   1 
ATOM 6487 C CA  . VAL B 1 384 ? -103.812 43.254 10.794  1.00 74.63  ?  384 VAL B CA  1 
ATOM 6488 C C   . VAL B 1 384 ? -103.809 44.419 11.775  1.00 79.28  ?  384 VAL B C   1 
ATOM 6489 O O   . VAL B 1 384 ? -103.404 45.537 11.452  1.00 95.78  ?  384 VAL B O   1 
ATOM 6490 C CB  . VAL B 1 384 ? -102.758 42.205 11.210  1.00 86.24  ?  384 VAL B CB  1 
ATOM 6491 C CG1 . VAL B 1 384 ? -103.079 40.851 10.597  1.00 80.21  ?  384 VAL B CG1 1 
ATOM 6492 C CG2 . VAL B 1 384 ? -101.364 42.664 10.811  1.00 70.50  ?  384 VAL B CG2 1 
ATOM 6493 N N   . LYS B 1 385 ? -104.271 44.138 12.993  1.00 78.70  ?  385 LYS B N   1 
ATOM 6494 C CA  . LYS B 1 385 ? -104.266 45.126 14.064  1.00 89.64  ?  385 LYS B CA  1 
ATOM 6495 C C   . LYS B 1 385 ? -102.946 45.127 14.827  1.00 84.83  ?  385 LYS B C   1 
ATOM 6496 O O   . LYS B 1 385 ? -102.335 46.183 15.016  1.00 83.62  ?  385 LYS B O   1 
ATOM 6497 C CB  . LYS B 1 385 ? -105.430 44.868 15.024  1.00 95.10  ?  385 LYS B CB  1 
ATOM 6498 C CG  . LYS B 1 385 ? -105.417 45.755 16.257  1.00 126.52 ?  385 LYS B CG  1 
ATOM 6499 C CD  . LYS B 1 385 ? -106.591 45.450 17.170  1.00 110.67 ?  385 LYS B CD  1 
ATOM 6500 C CE  . LYS B 1 385 ? -106.476 46.205 18.486  1.00 134.31 ?  385 LYS B CE  1 
ATOM 6501 N NZ  . LYS B 1 385 ? -106.460 47.682 18.293  1.00 156.82 ?  385 LYS B NZ  1 
ATOM 6502 N N   . ASP B 1 386 ? -102.496 43.955 15.268  1.00 81.48  ?  386 ASP B N   1 
ATOM 6503 C CA  . ASP B 1 386 ? -101.264 43.825 16.029  1.00 102.69 ?  386 ASP B CA  1 
ATOM 6504 C C   . ASP B 1 386 ? -100.358 42.798 15.366  1.00 94.44  ?  386 ASP B C   1 
ATOM 6505 O O   . ASP B 1 386 ? -100.828 41.833 14.756  1.00 85.37  ?  386 ASP B O   1 
ATOM 6506 C CB  . ASP B 1 386 ? -101.545 43.427 17.484  1.00 103.17 ?  386 ASP B CB  1 
ATOM 6507 C CG  . ASP B 1 386 ? -102.284 44.507 18.251  1.00 123.61 ?  386 ASP B CG  1 
ATOM 6508 O OD1 . ASP B 1 386 ? -102.061 45.702 17.963  1.00 116.05 ?  386 ASP B OD1 1 
ATOM 6509 O OD2 . ASP B 1 386 ? -103.091 44.162 19.139  1.00 146.28 -1 386 ASP B OD2 1 
ATOM 6510 N N   . PHE B 1 387 ? -99.048  43.023 15.492  1.00 84.42  ?  387 PHE B N   1 
ATOM 6511 C CA  . PHE B 1 387 ? -98.070  42.167 14.827  1.00 80.89  ?  387 PHE B CA  1 
ATOM 6512 C C   . PHE B 1 387 ? -98.126  40.737 15.350  1.00 88.31  ?  387 PHE B C   1 
ATOM 6513 O O   . PHE B 1 387 ? -97.943  39.782 14.585  1.00 86.64  ?  387 PHE B O   1 
ATOM 6514 C CB  . PHE B 1 387 ? -96.668  42.751 15.006  1.00 101.37 ?  387 PHE B CB  1 
ATOM 6515 C CG  . PHE B 1 387 ? -95.577  41.898 14.426  1.00 82.58  ?  387 PHE B CG  1 
ATOM 6516 C CD1 . PHE B 1 387 ? -94.847  41.039 15.232  1.00 85.13  ?  387 PHE B CD1 1 
ATOM 6517 C CD2 . PHE B 1 387 ? -95.276  41.957 13.076  1.00 83.23  ?  387 PHE B CD2 1 
ATOM 6518 C CE1 . PHE B 1 387 ? -93.842  40.254 14.703  1.00 86.05  ?  387 PHE B CE1 1 
ATOM 6519 C CE2 . PHE B 1 387 ? -94.271  41.175 12.541  1.00 75.51  ?  387 PHE B CE2 1 
ATOM 6520 C CZ  . PHE B 1 387 ? -93.552  40.322 13.355  1.00 65.41  ?  387 PHE B CZ  1 
ATOM 6521 N N   . ALA B 1 388 ? -98.376  40.566 16.649  1.00 86.03  ?  388 ALA B N   1 
ATOM 6522 C CA  . ALA B 1 388 ? -98.369  39.247 17.273  1.00 80.69  ?  388 ALA B CA  1 
ATOM 6523 C C   . ALA B 1 388 ? -99.478  38.331 16.768  1.00 83.92  ?  388 ALA B C   1 
ATOM 6524 O O   . ALA B 1 388 ? -99.503  37.157 17.154  1.00 70.86  ?  388 ALA B O   1 
ATOM 6525 C CB  . ALA B 1 388 ? -98.471  39.388 18.793  1.00 84.09  ?  388 ALA B CB  1 
ATOM 6526 N N   . ASP B 1 389 ? -100.382 38.824 15.924  1.00 81.23  ?  389 ASP B N   1 
ATOM 6527 C CA  . ASP B 1 389 ? -101.470 38.018 15.387  1.00 86.56  ?  389 ASP B CA  1 
ATOM 6528 C C   . ASP B 1 389 ? -101.057 37.193 14.176  1.00 83.17  ?  389 ASP B C   1 
ATOM 6529 O O   . ASP B 1 389 ? -101.919 36.566 13.552  1.00 98.40  ?  389 ASP B O   1 
ATOM 6530 C CB  . ASP B 1 389 ? -102.653 38.916 15.015  1.00 82.48  ?  389 ASP B CB  1 
ATOM 6531 C CG  . ASP B 1 389 ? -103.207 39.671 16.205  1.00 107.61 ?  389 ASP B CG  1 
ATOM 6532 O OD1 . ASP B 1 389 ? -103.153 39.131 17.330  1.00 103.25 ?  389 ASP B OD1 1 
ATOM 6533 O OD2 . ASP B 1 389 ? -103.699 40.803 16.014  1.00 113.88 -1 389 ASP B OD2 1 
ATOM 6534 N N   . ILE B 1 390 ? -99.773  37.171 13.835  1.00 69.35  ?  390 ILE B N   1 
ATOM 6535 C CA  . ILE B 1 390 ? -99.288  36.456 12.664  1.00 74.73  ?  390 ILE B CA  1 
ATOM 6536 C C   . ILE B 1 390 ? -98.819  35.051 13.018  1.00 87.09  ?  390 ILE B C   1 
ATOM 6537 O O   . ILE B 1 390 ? -98.997  34.119 12.233  1.00 88.23  ?  390 ILE B O   1 
ATOM 6538 C CB  . ILE B 1 390 ? -98.166  37.268 11.983  1.00 77.48  ?  390 ILE B CB  1 
ATOM 6539 C CG1 . ILE B 1 390 ? -98.685  38.656 11.607  1.00 65.88  ?  390 ILE B CG1 1 
ATOM 6540 C CG2 . ILE B 1 390 ? -97.649  36.546 10.750  1.00 73.21  ?  390 ILE B CG2 1 
ATOM 6541 C CD1 . ILE B 1 390 ? -97.608  39.606 11.146  1.00 55.98  ?  390 ILE B CD1 1 
ATOM 6542 N N   . LYS B 1 391 ? -98.216  34.890 14.200  1.00 90.75  ?  391 LYS B N   1 
ATOM 6543 C CA  . LYS B 1 391 ? -97.860  33.562 14.686  1.00 87.77  ?  391 LYS B CA  1 
ATOM 6544 C C   . LYS B 1 391 ? -99.067  32.632 14.698  1.00 92.68  ?  391 LYS B C   1 
ATOM 6545 O O   . LYS B 1 391 ? -98.933  31.430 14.443  1.00 101.56 ?  391 LYS B O   1 
ATOM 6546 C CB  . LYS B 1 391 ? -97.244  33.674 16.084  1.00 98.69  ?  391 LYS B CB  1 
ATOM 6547 C CG  . LYS B 1 391 ? -97.221  32.385 16.891  1.00 103.17 ?  391 LYS B CG  1 
ATOM 6548 C CD  . LYS B 1 391 ? -96.880  32.664 18.348  1.00 107.64 ?  391 LYS B CD  1 
ATOM 6549 C CE  . LYS B 1 391 ? -97.079  31.433 19.218  1.00 119.13 ?  391 LYS B CE  1 
ATOM 6550 N NZ  . LYS B 1 391 ? -96.861  31.736 20.661  1.00 108.41 ?  391 LYS B NZ  1 
ATOM 6551 N N   . GLU B 1 392 ? -100.253 33.173 14.970  1.00 100.09 ?  392 GLU B N   1 
ATOM 6552 C CA  . GLU B 1 392 ? -101.488 32.401 14.963  1.00 105.12 ?  392 GLU B CA  1 
ATOM 6553 C C   . GLU B 1 392 ? -102.087 32.248 13.570  1.00 96.10  ?  392 GLU B C   1 
ATOM 6554 O O   . GLU B 1 392 ? -103.186 31.698 13.444  1.00 89.50  ?  392 GLU B O   1 
ATOM 6555 C CB  . GLU B 1 392 ? -102.514 33.051 15.896  1.00 89.56  ?  392 GLU B CB  1 
ATOM 6556 C CG  . GLU B 1 392 ? -101.928 33.646 17.176  1.00 101.94 ?  392 GLU B CG  1 
ATOM 6557 C CD  . GLU B 1 392 ? -101.379 32.600 18.133  1.00 127.78 ?  392 GLU B CD  1 
ATOM 6558 O OE1 . GLU B 1 392 ? -100.336 31.984 17.827  1.00 147.51 ?  392 GLU B OE1 1 
ATOM 6559 O OE2 . GLU B 1 392 ? -101.994 32.394 19.201  1.00 152.20 -1 392 GLU B OE2 1 
ATOM 6560 N N   . ILE B 1 393 ? -101.402 32.717 12.531  1.00 89.72  ?  393 ILE B N   1 
ATOM 6561 C CA  . ILE B 1 393 ? -101.863 32.597 11.154  1.00 83.44  ?  393 ILE B CA  1 
ATOM 6562 C C   . ILE B 1 393 ? -100.973 31.653 10.354  1.00 89.38  ?  393 ILE B C   1 
ATOM 6563 O O   . ILE B 1 393 ? -101.460 30.724 9.708   1.00 82.27  ?  393 ILE B O   1 
ATOM 6564 C CB  . ILE B 1 393 ? -101.949 33.983 10.475  1.00 80.41  ?  393 ILE B CB  1 
ATOM 6565 C CG1 . ILE B 1 393 ? -103.024 34.842 11.142  1.00 73.54  ?  393 ILE B CG1 1 
ATOM 6566 C CG2 . ILE B 1 393 ? -102.229 33.834 8.987   1.00 73.15  ?  393 ILE B CG2 1 
ATOM 6567 C CD1 . ILE B 1 393 ? -103.150 36.227 10.546  1.00 62.41  ?  393 ILE B CD1 1 
ATOM 6568 N N   . VAL B 1 394 ? -99.663  31.875 10.390  1.00 99.53  ?  394 VAL B N   1 
ATOM 6569 C CA  . VAL B 1 394 ? -98.726  31.050 9.639   1.00 92.86  ?  394 VAL B CA  1 
ATOM 6570 C C   . VAL B 1 394 ? -98.488  29.721 10.349  1.00 97.33  ?  394 VAL B C   1 
ATOM 6571 O O   . VAL B 1 394 ? -97.780  28.851 9.842   1.00 89.20  ?  394 VAL B O   1 
ATOM 6572 C CB  . VAL B 1 394 ? -97.398  31.791 9.409   1.00 77.56  ?  394 VAL B CB  1 
ATOM 6573 C CG1 . VAL B 1 394 ? -97.646  33.116 8.703   1.00 75.12  ?  394 VAL B CG1 1 
ATOM 6574 C CG2 . VAL B 1 394 ? -96.674  32.008 10.729  1.00 79.20  ?  394 VAL B CG2 1 
ATOM 6575 O OXT . VAL B 1 394 ? -98.996  29.483 11.446  1.00 102.23 -1 394 VAL B OXT 1 
# 
