data_9F1Y
# 
_entry.id   9F1Y 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9F1Y         pdb_00009f1y 10.2210/pdb9f1y/pdb 
WWPDB D_1292138023 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9F1Y 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-20 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              sofia.kapetanaki@aok.pte.hu 
_pdbx_contact_author.name_first         Sofia 
_pdbx_contact_author.name_last          Kapetanaki 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-1286-9929 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Kapetanaki, S.' 1 ? 
'Coquelle, N.'   2 ? 
'Weik, M.'       3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To be published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'SSX room temperature structure of Oscillatoria acuminata adenylyate cyclase.' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kapetanaki, S.' 1 ? 
primary 'Coquelle, N.'   2 ? 
primary 'Weik, M.'       3 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Family 3 adenylate cyclase'  44173.285 1   ? ? ? ? 
2 non-polymer syn 'FLAVIN-ADENINE DINUCLEOTIDE' 785.550   1   ? ? ? ? 
3 non-polymer syn 'CALCIUM ION'                 40.078    2   ? ? ? ? 
4 water       nat water                         18.015    199 ? ? ? ? 
# 
_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       
;MGSSHHHHHHSSGLVPRGSHMENLYFQGMKRLTYISKFSRPLSGDEIEAIGRISSQKNQQANVTGVLLCLDGIFFQILEG
EAEKIDRIYERILADERHTDILCLKSEVEVQERMFPDWSMQTINLDENTDFLIRPIKVLLQTLTESHRILEKYTQPSIFK
IISQGTNPLNIRPKAVEKIVFFSDIVSFSTFAEKLPVEEVVSVVNSYFSVCTAIITRQGGEVTKFIGDCVMAYFDGDCAD
QAIQASLDILMELEILRNSAPEGSPLRVLYSGIGLAKGKVIEGNIGSELKRDYTILGDAVNVAARLEALTRQLSQALVFS
SEVKNSATKSWNFIWLTDSELKGKSESIDIYSIDNEMTRKSSGGLEIARNIGHYLERVGDRQPSQIFGVKSLPL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSSGLVPRGSHMENLYFQGMKRLTYISKFSRPLSGDEIEAIGRISSQKNQQANVTGVLLCLDGIFFQILEG
EAEKIDRIYERILADERHTDILCLKSEVEVQERMFPDWSMQTINLDENTDFLIRPIKVLLQTLTESHRILEKYTQPSIFK
IISQGTNPLNIRPKAVEKIVFFSDIVSFSTFAEKLPVEEVVSVVNSYFSVCTAIITRQGGEVTKFIGDCVMAYFDGDCAD
QAIQASLDILMELEILRNSAPEGSPLRVLYSGIGLAKGKVIEGNIGSELKRDYTILGDAVNVAARLEALTRQLSQALVFS
SEVKNSATKSWNFIWLTDSELKGKSESIDIYSIDNEMTRKSSGGLEIARNIGHYLERVGDRQPSQIFGVKSLPL
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'FLAVIN-ADENINE DINUCLEOTIDE' FAD 
3 'CALCIUM ION'                 CA  
4 water                         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  SER n 
1 13  GLY n 
1 14  LEU n 
1 15  VAL n 
1 16  PRO n 
1 17  ARG n 
1 18  GLY n 
1 19  SER n 
1 20  HIS n 
1 21  MET n 
1 22  GLU n 
1 23  ASN n 
1 24  LEU n 
1 25  TYR n 
1 26  PHE n 
1 27  GLN n 
1 28  GLY n 
1 29  MET n 
1 30  LYS n 
1 31  ARG n 
1 32  LEU n 
1 33  THR n 
1 34  TYR n 
1 35  ILE n 
1 36  SER n 
1 37  LYS n 
1 38  PHE n 
1 39  SER n 
1 40  ARG n 
1 41  PRO n 
1 42  LEU n 
1 43  SER n 
1 44  GLY n 
1 45  ASP n 
1 46  GLU n 
1 47  ILE n 
1 48  GLU n 
1 49  ALA n 
1 50  ILE n 
1 51  GLY n 
1 52  ARG n 
1 53  ILE n 
1 54  SER n 
1 55  SER n 
1 56  GLN n 
1 57  LYS n 
1 58  ASN n 
1 59  GLN n 
1 60  GLN n 
1 61  ALA n 
1 62  ASN n 
1 63  VAL n 
1 64  THR n 
1 65  GLY n 
1 66  VAL n 
1 67  LEU n 
1 68  LEU n 
1 69  CYS n 
1 70  LEU n 
1 71  ASP n 
1 72  GLY n 
1 73  ILE n 
1 74  PHE n 
1 75  PHE n 
1 76  GLN n 
1 77  ILE n 
1 78  LEU n 
1 79  GLU n 
1 80  GLY n 
1 81  GLU n 
1 82  ALA n 
1 83  GLU n 
1 84  LYS n 
1 85  ILE n 
1 86  ASP n 
1 87  ARG n 
1 88  ILE n 
1 89  TYR n 
1 90  GLU n 
1 91  ARG n 
1 92  ILE n 
1 93  LEU n 
1 94  ALA n 
1 95  ASP n 
1 96  GLU n 
1 97  ARG n 
1 98  HIS n 
1 99  THR n 
1 100 ASP n 
1 101 ILE n 
1 102 LEU n 
1 103 CYS n 
1 104 LEU n 
1 105 LYS n 
1 106 SER n 
1 107 GLU n 
1 108 VAL n 
1 109 GLU n 
1 110 VAL n 
1 111 GLN n 
1 112 GLU n 
1 113 ARG n 
1 114 MET n 
1 115 PHE n 
1 116 PRO n 
1 117 ASP n 
1 118 TRP n 
1 119 SER n 
1 120 MET n 
1 121 GLN n 
1 122 THR n 
1 123 ILE n 
1 124 ASN n 
1 125 LEU n 
1 126 ASP n 
1 127 GLU n 
1 128 ASN n 
1 129 THR n 
1 130 ASP n 
1 131 PHE n 
1 132 LEU n 
1 133 ILE n 
1 134 ARG n 
1 135 PRO n 
1 136 ILE n 
1 137 LYS n 
1 138 VAL n 
1 139 LEU n 
1 140 LEU n 
1 141 GLN n 
1 142 THR n 
1 143 LEU n 
1 144 THR n 
1 145 GLU n 
1 146 SER n 
1 147 HIS n 
1 148 ARG n 
1 149 ILE n 
1 150 LEU n 
1 151 GLU n 
1 152 LYS n 
1 153 TYR n 
1 154 THR n 
1 155 GLN n 
1 156 PRO n 
1 157 SER n 
1 158 ILE n 
1 159 PHE n 
1 160 LYS n 
1 161 ILE n 
1 162 ILE n 
1 163 SER n 
1 164 GLN n 
1 165 GLY n 
1 166 THR n 
1 167 ASN n 
1 168 PRO n 
1 169 LEU n 
1 170 ASN n 
1 171 ILE n 
1 172 ARG n 
1 173 PRO n 
1 174 LYS n 
1 175 ALA n 
1 176 VAL n 
1 177 GLU n 
1 178 LYS n 
1 179 ILE n 
1 180 VAL n 
1 181 PHE n 
1 182 PHE n 
1 183 SER n 
1 184 ASP n 
1 185 ILE n 
1 186 VAL n 
1 187 SER n 
1 188 PHE n 
1 189 SER n 
1 190 THR n 
1 191 PHE n 
1 192 ALA n 
1 193 GLU n 
1 194 LYS n 
1 195 LEU n 
1 196 PRO n 
1 197 VAL n 
1 198 GLU n 
1 199 GLU n 
1 200 VAL n 
1 201 VAL n 
1 202 SER n 
1 203 VAL n 
1 204 VAL n 
1 205 ASN n 
1 206 SER n 
1 207 TYR n 
1 208 PHE n 
1 209 SER n 
1 210 VAL n 
1 211 CYS n 
1 212 THR n 
1 213 ALA n 
1 214 ILE n 
1 215 ILE n 
1 216 THR n 
1 217 ARG n 
1 218 GLN n 
1 219 GLY n 
1 220 GLY n 
1 221 GLU n 
1 222 VAL n 
1 223 THR n 
1 224 LYS n 
1 225 PHE n 
1 226 ILE n 
1 227 GLY n 
1 228 ASP n 
1 229 CYS n 
1 230 VAL n 
1 231 MET n 
1 232 ALA n 
1 233 TYR n 
1 234 PHE n 
1 235 ASP n 
1 236 GLY n 
1 237 ASP n 
1 238 CYS n 
1 239 ALA n 
1 240 ASP n 
1 241 GLN n 
1 242 ALA n 
1 243 ILE n 
1 244 GLN n 
1 245 ALA n 
1 246 SER n 
1 247 LEU n 
1 248 ASP n 
1 249 ILE n 
1 250 LEU n 
1 251 MET n 
1 252 GLU n 
1 253 LEU n 
1 254 GLU n 
1 255 ILE n 
1 256 LEU n 
1 257 ARG n 
1 258 ASN n 
1 259 SER n 
1 260 ALA n 
1 261 PRO n 
1 262 GLU n 
1 263 GLY n 
1 264 SER n 
1 265 PRO n 
1 266 LEU n 
1 267 ARG n 
1 268 VAL n 
1 269 LEU n 
1 270 TYR n 
1 271 SER n 
1 272 GLY n 
1 273 ILE n 
1 274 GLY n 
1 275 LEU n 
1 276 ALA n 
1 277 LYS n 
1 278 GLY n 
1 279 LYS n 
1 280 VAL n 
1 281 ILE n 
1 282 GLU n 
1 283 GLY n 
1 284 ASN n 
1 285 ILE n 
1 286 GLY n 
1 287 SER n 
1 288 GLU n 
1 289 LEU n 
1 290 LYS n 
1 291 ARG n 
1 292 ASP n 
1 293 TYR n 
1 294 THR n 
1 295 ILE n 
1 296 LEU n 
1 297 GLY n 
1 298 ASP n 
1 299 ALA n 
1 300 VAL n 
1 301 ASN n 
1 302 VAL n 
1 303 ALA n 
1 304 ALA n 
1 305 ARG n 
1 306 LEU n 
1 307 GLU n 
1 308 ALA n 
1 309 LEU n 
1 310 THR n 
1 311 ARG n 
1 312 GLN n 
1 313 LEU n 
1 314 SER n 
1 315 GLN n 
1 316 ALA n 
1 317 LEU n 
1 318 VAL n 
1 319 PHE n 
1 320 SER n 
1 321 SER n 
1 322 GLU n 
1 323 VAL n 
1 324 LYS n 
1 325 ASN n 
1 326 SER n 
1 327 ALA n 
1 328 THR n 
1 329 LYS n 
1 330 SER n 
1 331 TRP n 
1 332 ASN n 
1 333 PHE n 
1 334 ILE n 
1 335 TRP n 
1 336 LEU n 
1 337 THR n 
1 338 ASP n 
1 339 SER n 
1 340 GLU n 
1 341 LEU n 
1 342 LYS n 
1 343 GLY n 
1 344 LYS n 
1 345 SER n 
1 346 GLU n 
1 347 SER n 
1 348 ILE n 
1 349 ASP n 
1 350 ILE n 
1 351 TYR n 
1 352 SER n 
1 353 ILE n 
1 354 ASP n 
1 355 ASN n 
1 356 GLU n 
1 357 MET n 
1 358 THR n 
1 359 ARG n 
1 360 LYS n 
1 361 SER n 
1 362 SER n 
1 363 GLY n 
1 364 GLY n 
1 365 LEU n 
1 366 GLU n 
1 367 ILE n 
1 368 ALA n 
1 369 ARG n 
1 370 ASN n 
1 371 ILE n 
1 372 GLY n 
1 373 HIS n 
1 374 TYR n 
1 375 LEU n 
1 376 GLU n 
1 377 ARG n 
1 378 VAL n 
1 379 GLY n 
1 380 ASP n 
1 381 ARG n 
1 382 GLN n 
1 383 PRO n 
1 384 SER n 
1 385 GLN n 
1 386 ILE n 
1 387 PHE n 
1 388 GLY n 
1 389 VAL n 
1 390 LYS n 
1 391 SER n 
1 392 LEU n 
1 393 PRO n 
1 394 LEU 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                 Oscil6304_3613 
_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      'Oscillatoria acuminata' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     118323 
_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 
CA  non-polymer         . 'CALCIUM ION'                 ? 'Ca 2'              40.078  
CYS 'L-peptide linking' y CYSTEINE                      ? 'C3 H7 N O2 S'      121.158 
FAD non-polymer         . 'FLAVIN-ADENINE DINUCLEOTIDE' ? 'C27 H33 N9 O15 P2' 785.550 
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 
HOH non-polymer         . WATER                         ? 'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                    ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                       ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                        ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                    ? 'C5 H11 N O2 S'     149.211 
PHE 'L-peptide linking' y PHENYLALANINE                 ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                       ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                        ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                     ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                    ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                      ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                        ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -27 ?   ?   ?   A . n 
A 1 2   GLY 2   -26 ?   ?   ?   A . n 
A 1 3   SER 3   -25 ?   ?   ?   A . n 
A 1 4   SER 4   -24 ?   ?   ?   A . n 
A 1 5   HIS 5   -23 ?   ?   ?   A . n 
A 1 6   HIS 6   -22 ?   ?   ?   A . n 
A 1 7   HIS 7   -21 ?   ?   ?   A . n 
A 1 8   HIS 8   -20 ?   ?   ?   A . n 
A 1 9   HIS 9   -19 ?   ?   ?   A . n 
A 1 10  HIS 10  -18 ?   ?   ?   A . n 
A 1 11  SER 11  -17 ?   ?   ?   A . n 
A 1 12  SER 12  -16 ?   ?   ?   A . n 
A 1 13  GLY 13  -15 ?   ?   ?   A . n 
A 1 14  LEU 14  -14 ?   ?   ?   A . n 
A 1 15  VAL 15  -13 ?   ?   ?   A . n 
A 1 16  PRO 16  -12 ?   ?   ?   A . n 
A 1 17  ARG 17  -11 ?   ?   ?   A . n 
A 1 18  GLY 18  -10 ?   ?   ?   A . n 
A 1 19  SER 19  -9  ?   ?   ?   A . n 
A 1 20  HIS 20  -8  ?   ?   ?   A . n 
A 1 21  MET 21  -7  ?   ?   ?   A . n 
A 1 22  GLU 22  -6  ?   ?   ?   A . n 
A 1 23  ASN 23  -5  ?   ?   ?   A . n 
A 1 24  LEU 24  -4  ?   ?   ?   A . n 
A 1 25  TYR 25  -3  ?   ?   ?   A . n 
A 1 26  PHE 26  -2  ?   ?   ?   A . n 
A 1 27  GLN 27  -1  ?   ?   ?   A . n 
A 1 28  GLY 28  0   0   GLY GLY A . n 
A 1 29  MET 29  1   1   MET MET A . n 
A 1 30  LYS 30  2   2   LYS LYS A . n 
A 1 31  ARG 31  3   3   ARG ARG A . n 
A 1 32  LEU 32  4   4   LEU LEU A . n 
A 1 33  THR 33  5   5   THR THR A . n 
A 1 34  TYR 34  6   6   TYR TYR A . n 
A 1 35  ILE 35  7   7   ILE ILE A . n 
A 1 36  SER 36  8   8   SER SER A . n 
A 1 37  LYS 37  9   9   LYS LYS A . n 
A 1 38  PHE 38  10  10  PHE PHE A . n 
A 1 39  SER 39  11  11  SER SER A . n 
A 1 40  ARG 40  12  12  ARG ARG A . n 
A 1 41  PRO 41  13  13  PRO PRO A . n 
A 1 42  LEU 42  14  14  LEU LEU A . n 
A 1 43  SER 43  15  15  SER SER A . n 
A 1 44  GLY 44  16  16  GLY GLY A . n 
A 1 45  ASP 45  17  17  ASP ASP A . n 
A 1 46  GLU 46  18  18  GLU GLU A . n 
A 1 47  ILE 47  19  19  ILE ILE A . n 
A 1 48  GLU 48  20  20  GLU GLU A . n 
A 1 49  ALA 49  21  21  ALA ALA A . n 
A 1 50  ILE 50  22  22  ILE ILE A . n 
A 1 51  GLY 51  23  23  GLY GLY A . n 
A 1 52  ARG 52  24  24  ARG ARG A . n 
A 1 53  ILE 53  25  25  ILE ILE A . n 
A 1 54  SER 54  26  26  SER SER A . n 
A 1 55  SER 55  27  27  SER SER A . n 
A 1 56  GLN 56  28  28  GLN GLN A . n 
A 1 57  LYS 57  29  29  LYS LYS A . n 
A 1 58  ASN 58  30  30  ASN ASN A . n 
A 1 59  GLN 59  31  31  GLN GLN A . n 
A 1 60  GLN 60  32  32  GLN GLN A . n 
A 1 61  ALA 61  33  33  ALA ALA A . n 
A 1 62  ASN 62  34  34  ASN ASN A . n 
A 1 63  VAL 63  35  35  VAL VAL A . n 
A 1 64  THR 64  36  36  THR THR A . n 
A 1 65  GLY 65  37  37  GLY GLY A . n 
A 1 66  VAL 66  38  38  VAL VAL A . n 
A 1 67  LEU 67  39  39  LEU LEU A . n 
A 1 68  LEU 68  40  40  LEU LEU A . n 
A 1 69  CYS 69  41  41  CYS CYS A . n 
A 1 70  LEU 70  42  42  LEU LEU A . n 
A 1 71  ASP 71  43  43  ASP ASP A . n 
A 1 72  GLY 72  44  44  GLY GLY A . n 
A 1 73  ILE 73  45  45  ILE ILE A . n 
A 1 74  PHE 74  46  46  PHE PHE A . n 
A 1 75  PHE 75  47  47  PHE PHE A . n 
A 1 76  GLN 76  48  48  GLN GLN A . n 
A 1 77  ILE 77  49  49  ILE ILE A . n 
A 1 78  LEU 78  50  50  LEU LEU A . n 
A 1 79  GLU 79  51  51  GLU GLU A . n 
A 1 80  GLY 80  52  52  GLY GLY A . n 
A 1 81  GLU 81  53  53  GLU GLU A . n 
A 1 82  ALA 82  54  54  ALA ALA A . n 
A 1 83  GLU 83  55  55  GLU GLU A . n 
A 1 84  LYS 84  56  56  LYS LYS A . n 
A 1 85  ILE 85  57  57  ILE ILE A . n 
A 1 86  ASP 86  58  58  ASP ASP A . n 
A 1 87  ARG 87  59  59  ARG ARG A . n 
A 1 88  ILE 88  60  60  ILE ILE A . n 
A 1 89  TYR 89  61  61  TYR TYR A . n 
A 1 90  GLU 90  62  62  GLU GLU A . n 
A 1 91  ARG 91  63  63  ARG ARG A . n 
A 1 92  ILE 92  64  64  ILE ILE A . n 
A 1 93  LEU 93  65  65  LEU LEU A . n 
A 1 94  ALA 94  66  66  ALA ALA A . n 
A 1 95  ASP 95  67  67  ASP ASP A . n 
A 1 96  GLU 96  68  68  GLU GLU A . n 
A 1 97  ARG 97  69  69  ARG ARG A . n 
A 1 98  HIS 98  70  70  HIS HIS A . n 
A 1 99  THR 99  71  71  THR THR A . n 
A 1 100 ASP 100 72  72  ASP ASP A . n 
A 1 101 ILE 101 73  73  ILE ILE A . n 
A 1 102 LEU 102 74  74  LEU LEU A . n 
A 1 103 CYS 103 75  75  CYS CYS A . n 
A 1 104 LEU 104 76  76  LEU LEU A . n 
A 1 105 LYS 105 77  77  LYS LYS A . n 
A 1 106 SER 106 78  78  SER SER A . n 
A 1 107 GLU 107 79  79  GLU GLU A . n 
A 1 108 VAL 108 80  80  VAL VAL A . n 
A 1 109 GLU 109 81  81  GLU GLU A . n 
A 1 110 VAL 110 82  82  VAL VAL A . n 
A 1 111 GLN 111 83  83  GLN GLN A . n 
A 1 112 GLU 112 84  84  GLU GLU A . n 
A 1 113 ARG 113 85  85  ARG ARG A . n 
A 1 114 MET 114 86  86  MET MET A . n 
A 1 115 PHE 115 87  87  PHE PHE A . n 
A 1 116 PRO 116 88  88  PRO PRO A . n 
A 1 117 ASP 117 89  89  ASP ASP A . n 
A 1 118 TRP 118 90  90  TRP TRP A . n 
A 1 119 SER 119 91  91  SER SER A . n 
A 1 120 MET 120 92  92  MET MET A . n 
A 1 121 GLN 121 93  93  GLN GLN A . n 
A 1 122 THR 122 94  94  THR THR A . n 
A 1 123 ILE 123 95  95  ILE ILE A . n 
A 1 124 ASN 124 96  96  ASN ASN A . n 
A 1 125 LEU 125 97  97  LEU LEU A . n 
A 1 126 ASP 126 98  98  ASP ASP A . n 
A 1 127 GLU 127 99  99  GLU GLU A . n 
A 1 128 ASN 128 100 100 ASN ASN A . n 
A 1 129 THR 129 101 101 THR THR A . n 
A 1 130 ASP 130 102 102 ASP ASP A . n 
A 1 131 PHE 131 103 103 PHE PHE A . n 
A 1 132 LEU 132 104 104 LEU LEU A . n 
A 1 133 ILE 133 105 105 ILE ILE A . n 
A 1 134 ARG 134 106 106 ARG ARG A . n 
A 1 135 PRO 135 107 107 PRO PRO A . n 
A 1 136 ILE 136 108 108 ILE ILE A . n 
A 1 137 LYS 137 109 109 LYS LYS A . n 
A 1 138 VAL 138 110 110 VAL VAL A . n 
A 1 139 LEU 139 111 111 LEU LEU A . n 
A 1 140 LEU 140 112 112 LEU LEU A . n 
A 1 141 GLN 141 113 113 GLN GLN A . n 
A 1 142 THR 142 114 114 THR THR A . n 
A 1 143 LEU 143 115 115 LEU LEU A . n 
A 1 144 THR 144 116 116 THR THR A . n 
A 1 145 GLU 145 117 117 GLU GLU A . n 
A 1 146 SER 146 118 118 SER SER A . n 
A 1 147 HIS 147 119 119 HIS HIS A . n 
A 1 148 ARG 148 120 120 ARG ARG A . n 
A 1 149 ILE 149 121 121 ILE ILE A . n 
A 1 150 LEU 150 122 122 LEU LEU A . n 
A 1 151 GLU 151 123 123 GLU GLU A . n 
A 1 152 LYS 152 124 124 LYS LYS A . n 
A 1 153 TYR 153 125 125 TYR TYR A . n 
A 1 154 THR 154 126 126 THR THR A . n 
A 1 155 GLN 155 127 127 GLN GLN A . n 
A 1 156 PRO 156 128 128 PRO PRO A . n 
A 1 157 SER 157 129 129 SER SER A . n 
A 1 158 ILE 158 130 130 ILE ILE A . n 
A 1 159 PHE 159 131 131 PHE PHE A . n 
A 1 160 LYS 160 132 132 LYS LYS A . n 
A 1 161 ILE 161 133 133 ILE ILE A . n 
A 1 162 ILE 162 134 134 ILE ILE A . n 
A 1 163 SER 163 135 135 SER SER A . n 
A 1 164 GLN 164 136 136 GLN GLN A . n 
A 1 165 GLY 165 137 137 GLY GLY A . n 
A 1 166 THR 166 138 138 THR THR A . n 
A 1 167 ASN 167 139 139 ASN ASN A . n 
A 1 168 PRO 168 140 140 PRO PRO A . n 
A 1 169 LEU 169 141 141 LEU LEU A . n 
A 1 170 ASN 170 142 142 ASN ASN A . n 
A 1 171 ILE 171 143 143 ILE ILE A . n 
A 1 172 ARG 172 144 144 ARG ARG A . n 
A 1 173 PRO 173 145 145 PRO PRO A . n 
A 1 174 LYS 174 146 146 LYS LYS A . n 
A 1 175 ALA 175 147 147 ALA ALA A . n 
A 1 176 VAL 176 148 148 VAL VAL A . n 
A 1 177 GLU 177 149 149 GLU GLU A . n 
A 1 178 LYS 178 150 150 LYS LYS A . n 
A 1 179 ILE 179 151 151 ILE ILE A . n 
A 1 180 VAL 180 152 152 VAL VAL A . n 
A 1 181 PHE 181 153 153 PHE PHE A . n 
A 1 182 PHE 182 154 154 PHE PHE A . n 
A 1 183 SER 183 155 155 SER SER A . n 
A 1 184 ASP 184 156 156 ASP ASP A . n 
A 1 185 ILE 185 157 157 ILE ILE A . n 
A 1 186 VAL 186 158 158 VAL VAL A . n 
A 1 187 SER 187 159 159 SER SER A . n 
A 1 188 PHE 188 160 160 PHE PHE A . n 
A 1 189 SER 189 161 161 SER SER A . n 
A 1 190 THR 190 162 162 THR THR A . n 
A 1 191 PHE 191 163 163 PHE PHE A . n 
A 1 192 ALA 192 164 164 ALA ALA A . n 
A 1 193 GLU 193 165 165 GLU GLU A . n 
A 1 194 LYS 194 166 166 LYS LYS A . n 
A 1 195 LEU 195 167 167 LEU LEU A . n 
A 1 196 PRO 196 168 168 PRO PRO A . n 
A 1 197 VAL 197 169 169 VAL VAL A . n 
A 1 198 GLU 198 170 170 GLU GLU A . n 
A 1 199 GLU 199 171 171 GLU GLU A . n 
A 1 200 VAL 200 172 172 VAL VAL A . n 
A 1 201 VAL 201 173 173 VAL VAL A . n 
A 1 202 SER 202 174 174 SER SER A . n 
A 1 203 VAL 203 175 175 VAL VAL A . n 
A 1 204 VAL 204 176 176 VAL VAL A . n 
A 1 205 ASN 205 177 177 ASN ASN A . n 
A 1 206 SER 206 178 178 SER SER A . n 
A 1 207 TYR 207 179 179 TYR TYR A . n 
A 1 208 PHE 208 180 180 PHE PHE A . n 
A 1 209 SER 209 181 181 SER SER A . n 
A 1 210 VAL 210 182 182 VAL VAL A . n 
A 1 211 CYS 211 183 183 CYS CYS A . n 
A 1 212 THR 212 184 184 THR THR A . n 
A 1 213 ALA 213 185 185 ALA ALA A . n 
A 1 214 ILE 214 186 186 ILE ILE A . n 
A 1 215 ILE 215 187 187 ILE ILE A . n 
A 1 216 THR 216 188 188 THR THR A . n 
A 1 217 ARG 217 189 189 ARG ARG A . n 
A 1 218 GLN 218 190 190 GLN GLN A . n 
A 1 219 GLY 219 191 191 GLY GLY A . n 
A 1 220 GLY 220 192 192 GLY GLY A . n 
A 1 221 GLU 221 193 193 GLU GLU A . n 
A 1 222 VAL 222 194 194 VAL VAL A . n 
A 1 223 THR 223 195 195 THR THR A . n 
A 1 224 LYS 224 196 196 LYS LYS A . n 
A 1 225 PHE 225 197 197 PHE PHE A . n 
A 1 226 ILE 226 198 198 ILE ILE A . n 
A 1 227 GLY 227 199 199 GLY GLY A . n 
A 1 228 ASP 228 200 200 ASP ASP A . n 
A 1 229 CYS 229 201 201 CYS CYS A . n 
A 1 230 VAL 230 202 202 VAL VAL A . n 
A 1 231 MET 231 203 203 MET MET A . n 
A 1 232 ALA 232 204 204 ALA ALA A . n 
A 1 233 TYR 233 205 205 TYR TYR A . n 
A 1 234 PHE 234 206 206 PHE PHE A . n 
A 1 235 ASP 235 207 207 ASP ASP A . n 
A 1 236 GLY 236 208 208 GLY GLY A . n 
A 1 237 ASP 237 209 209 ASP ASP A . n 
A 1 238 CYS 238 210 210 CYS CYS A . n 
A 1 239 ALA 239 211 211 ALA ALA A . n 
A 1 240 ASP 240 212 212 ASP ASP A . n 
A 1 241 GLN 241 213 213 GLN GLN A . n 
A 1 242 ALA 242 214 214 ALA ALA A . n 
A 1 243 ILE 243 215 215 ILE ILE A . n 
A 1 244 GLN 244 216 216 GLN GLN A . n 
A 1 245 ALA 245 217 217 ALA ALA A . n 
A 1 246 SER 246 218 218 SER SER A . n 
A 1 247 LEU 247 219 219 LEU LEU A . n 
A 1 248 ASP 248 220 220 ASP ASP A . n 
A 1 249 ILE 249 221 221 ILE ILE A . n 
A 1 250 LEU 250 222 222 LEU LEU A . n 
A 1 251 MET 251 223 223 MET MET A . n 
A 1 252 GLU 252 224 224 GLU GLU A . n 
A 1 253 LEU 253 225 225 LEU LEU A . n 
A 1 254 GLU 254 226 226 GLU GLU A . n 
A 1 255 ILE 255 227 227 ILE ILE A . n 
A 1 256 LEU 256 228 228 LEU LEU A . n 
A 1 257 ARG 257 229 229 ARG ARG A . n 
A 1 258 ASN 258 230 230 ASN ASN A . n 
A 1 259 SER 259 231 231 SER SER A . n 
A 1 260 ALA 260 232 232 ALA ALA A . n 
A 1 261 PRO 261 233 233 PRO PRO A . n 
A 1 262 GLU 262 234 234 GLU GLU A . n 
A 1 263 GLY 263 235 235 GLY GLY A . n 
A 1 264 SER 264 236 236 SER SER A . n 
A 1 265 PRO 265 237 237 PRO PRO A . n 
A 1 266 LEU 266 238 238 LEU LEU A . n 
A 1 267 ARG 267 239 239 ARG ARG A . n 
A 1 268 VAL 268 240 240 VAL VAL A . n 
A 1 269 LEU 269 241 241 LEU LEU A . n 
A 1 270 TYR 270 242 242 TYR TYR A . n 
A 1 271 SER 271 243 243 SER SER A . n 
A 1 272 GLY 272 244 244 GLY GLY A . n 
A 1 273 ILE 273 245 245 ILE ILE A . n 
A 1 274 GLY 274 246 246 GLY GLY A . n 
A 1 275 LEU 275 247 247 LEU LEU A . n 
A 1 276 ALA 276 248 248 ALA ALA A . n 
A 1 277 LYS 277 249 249 LYS LYS A . n 
A 1 278 GLY 278 250 250 GLY GLY A . n 
A 1 279 LYS 279 251 251 LYS LYS A . n 
A 1 280 VAL 280 252 252 VAL VAL A . n 
A 1 281 ILE 281 253 253 ILE ILE A . n 
A 1 282 GLU 282 254 254 GLU GLU A . n 
A 1 283 GLY 283 255 255 GLY GLY A . n 
A 1 284 ASN 284 256 256 ASN ASN A . n 
A 1 285 ILE 285 257 257 ILE ILE A . n 
A 1 286 GLY 286 258 258 GLY GLY A . n 
A 1 287 SER 287 259 259 SER SER A . n 
A 1 288 GLU 288 260 260 GLU GLU A . n 
A 1 289 LEU 289 261 261 LEU LEU A . n 
A 1 290 LYS 290 262 262 LYS LYS A . n 
A 1 291 ARG 291 263 263 ARG ARG A . n 
A 1 292 ASP 292 264 264 ASP ASP A . n 
A 1 293 TYR 293 265 265 TYR TYR A . n 
A 1 294 THR 294 266 266 THR THR A . n 
A 1 295 ILE 295 267 267 ILE ILE A . n 
A 1 296 LEU 296 268 268 LEU LEU A . n 
A 1 297 GLY 297 269 269 GLY GLY A . n 
A 1 298 ASP 298 270 270 ASP ASP A . n 
A 1 299 ALA 299 271 271 ALA ALA A . n 
A 1 300 VAL 300 272 272 VAL VAL A . n 
A 1 301 ASN 301 273 273 ASN ASN A . n 
A 1 302 VAL 302 274 274 VAL VAL A . n 
A 1 303 ALA 303 275 275 ALA ALA A . n 
A 1 304 ALA 304 276 276 ALA ALA A . n 
A 1 305 ARG 305 277 277 ARG ARG A . n 
A 1 306 LEU 306 278 278 LEU LEU A . n 
A 1 307 GLU 307 279 279 GLU GLU A . n 
A 1 308 ALA 308 280 280 ALA ALA A . n 
A 1 309 LEU 309 281 281 LEU LEU A . n 
A 1 310 THR 310 282 282 THR THR A . n 
A 1 311 ARG 311 283 283 ARG ARG A . n 
A 1 312 GLN 312 284 284 GLN GLN A . n 
A 1 313 LEU 313 285 285 LEU LEU A . n 
A 1 314 SER 314 286 286 SER SER A . n 
A 1 315 GLN 315 287 287 GLN GLN A . n 
A 1 316 ALA 316 288 288 ALA ALA A . n 
A 1 317 LEU 317 289 289 LEU LEU A . n 
A 1 318 VAL 318 290 290 VAL VAL A . n 
A 1 319 PHE 319 291 291 PHE PHE A . n 
A 1 320 SER 320 292 292 SER SER A . n 
A 1 321 SER 321 293 293 SER SER A . n 
A 1 322 GLU 322 294 294 GLU GLU A . n 
A 1 323 VAL 323 295 295 VAL VAL A . n 
A 1 324 LYS 324 296 296 LYS LYS A . n 
A 1 325 ASN 325 297 297 ASN ASN A . n 
A 1 326 SER 326 298 298 SER SER A . n 
A 1 327 ALA 327 299 299 ALA ALA A . n 
A 1 328 THR 328 300 300 THR THR A . n 
A 1 329 LYS 329 301 301 LYS LYS A . n 
A 1 330 SER 330 302 302 SER SER A . n 
A 1 331 TRP 331 303 303 TRP TRP A . n 
A 1 332 ASN 332 304 304 ASN ASN A . n 
A 1 333 PHE 333 305 305 PHE PHE A . n 
A 1 334 ILE 334 306 306 ILE ILE A . n 
A 1 335 TRP 335 307 307 TRP TRP A . n 
A 1 336 LEU 336 308 308 LEU LEU A . n 
A 1 337 THR 337 309 309 THR THR A . n 
A 1 338 ASP 338 310 310 ASP ASP A . n 
A 1 339 SER 339 311 311 SER SER A . n 
A 1 340 GLU 340 312 312 GLU GLU A . n 
A 1 341 LEU 341 313 313 LEU LEU A . n 
A 1 342 LYS 342 314 314 LYS LYS A . n 
A 1 343 GLY 343 315 315 GLY GLY A . n 
A 1 344 LYS 344 316 316 LYS LYS A . n 
A 1 345 SER 345 317 317 SER SER A . n 
A 1 346 GLU 346 318 318 GLU GLU A . n 
A 1 347 SER 347 319 319 SER SER A . n 
A 1 348 ILE 348 320 320 ILE ILE A . n 
A 1 349 ASP 349 321 321 ASP ASP A . n 
A 1 350 ILE 350 322 322 ILE ILE A . n 
A 1 351 TYR 351 323 323 TYR TYR A . n 
A 1 352 SER 352 324 324 SER SER A . n 
A 1 353 ILE 353 325 325 ILE ILE A . n 
A 1 354 ASP 354 326 326 ASP ASP A . n 
A 1 355 ASN 355 327 327 ASN ASN A . n 
A 1 356 GLU 356 328 328 GLU GLU A . n 
A 1 357 MET 357 329 329 MET MET A . n 
A 1 358 THR 358 330 330 THR THR A . n 
A 1 359 ARG 359 331 331 ARG ARG A . n 
A 1 360 LYS 360 332 332 LYS LYS A . n 
A 1 361 SER 361 333 333 SER SER A . n 
A 1 362 SER 362 334 334 SER SER A . n 
A 1 363 GLY 363 335 ?   ?   ?   A . n 
A 1 364 GLY 364 336 336 GLY GLY A . n 
A 1 365 LEU 365 337 337 LEU LEU A . n 
A 1 366 GLU 366 338 338 GLU GLU A . n 
A 1 367 ILE 367 339 339 ILE ILE A . n 
A 1 368 ALA 368 340 340 ALA ALA A . n 
A 1 369 ARG 369 341 341 ARG ARG A . n 
A 1 370 ASN 370 342 342 ASN ASN A . n 
A 1 371 ILE 371 343 343 ILE ILE A . n 
A 1 372 GLY 372 344 344 GLY GLY A . n 
A 1 373 HIS 373 345 345 HIS HIS A . n 
A 1 374 TYR 374 346 346 TYR TYR A . n 
A 1 375 LEU 375 347 347 LEU LEU A . n 
A 1 376 GLU 376 348 348 GLU GLU A . n 
A 1 377 ARG 377 349 349 ARG ARG A . n 
A 1 378 VAL 378 350 350 VAL VAL A . n 
A 1 379 GLY 379 351 ?   ?   ?   A . n 
A 1 380 ASP 380 352 ?   ?   ?   A . n 
A 1 381 ARG 381 353 ?   ?   ?   A . n 
A 1 382 GLN 382 354 ?   ?   ?   A . n 
A 1 383 PRO 383 355 ?   ?   ?   A . n 
A 1 384 SER 384 356 ?   ?   ?   A . n 
A 1 385 GLN 385 357 ?   ?   ?   A . n 
A 1 386 ILE 386 358 ?   ?   ?   A . n 
A 1 387 PHE 387 359 ?   ?   ?   A . n 
A 1 388 GLY 388 360 ?   ?   ?   A . n 
A 1 389 VAL 389 361 ?   ?   ?   A . n 
A 1 390 LYS 390 362 ?   ?   ?   A . n 
A 1 391 SER 391 363 ?   ?   ?   A . n 
A 1 392 LEU 392 364 ?   ?   ?   A . n 
A 1 393 PRO 393 365 ?   ?   ?   A . n 
A 1 394 LEU 394 366 ?   ?   ?   A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 FAD 1   401 400 FAD FMN A . 
C 3 CA  1   402 1   CA  CA  A . 
D 3 CA  1   403 2   CA  CA  A . 
E 4 HOH 1   501 71  HOH HOH A . 
E 4 HOH 2   502 198 HOH HOH A . 
E 4 HOH 3   503 14  HOH HOH A . 
E 4 HOH 4   504 299 HOH HOH A . 
E 4 HOH 5   505 315 HOH HOH A . 
E 4 HOH 6   506 209 HOH HOH A . 
E 4 HOH 7   507 257 HOH HOH A . 
E 4 HOH 8   508 89  HOH HOH A . 
E 4 HOH 9   509 109 HOH HOH A . 
E 4 HOH 10  510 252 HOH HOH A . 
E 4 HOH 11  511 160 HOH HOH A . 
E 4 HOH 12  512 185 HOH HOH A . 
E 4 HOH 13  513 6   HOH HOH A . 
E 4 HOH 14  514 281 HOH HOH A . 
E 4 HOH 15  515 32  HOH HOH A . 
E 4 HOH 16  516 118 HOH HOH A . 
E 4 HOH 17  517 24  HOH HOH A . 
E 4 HOH 18  518 93  HOH HOH A . 
E 4 HOH 19  519 39  HOH HOH A . 
E 4 HOH 20  520 57  HOH HOH A . 
E 4 HOH 21  521 196 HOH HOH A . 
E 4 HOH 22  522 142 HOH HOH A . 
E 4 HOH 23  523 27  HOH HOH A . 
E 4 HOH 24  524 13  HOH HOH A . 
E 4 HOH 25  525 127 HOH HOH A . 
E 4 HOH 26  526 49  HOH HOH A . 
E 4 HOH 27  527 105 HOH HOH A . 
E 4 HOH 28  528 62  HOH HOH A . 
E 4 HOH 29  529 91  HOH HOH A . 
E 4 HOH 30  530 278 HOH HOH A . 
E 4 HOH 31  531 78  HOH HOH A . 
E 4 HOH 32  532 195 HOH HOH A . 
E 4 HOH 33  533 55  HOH HOH A . 
E 4 HOH 34  534 66  HOH HOH A . 
E 4 HOH 35  535 126 HOH HOH A . 
E 4 HOH 36  536 131 HOH HOH A . 
E 4 HOH 37  537 46  HOH HOH A . 
E 4 HOH 38  538 145 HOH HOH A . 
E 4 HOH 39  539 112 HOH HOH A . 
E 4 HOH 40  540 104 HOH HOH A . 
E 4 HOH 41  541 64  HOH HOH A . 
E 4 HOH 42  542 133 HOH HOH A . 
E 4 HOH 43  543 276 HOH HOH A . 
E 4 HOH 44  544 42  HOH HOH A . 
E 4 HOH 45  545 163 HOH HOH A . 
E 4 HOH 46  546 65  HOH HOH A . 
E 4 HOH 47  547 54  HOH HOH A . 
E 4 HOH 48  548 11  HOH HOH A . 
E 4 HOH 49  549 63  HOH HOH A . 
E 4 HOH 50  550 182 HOH HOH A . 
E 4 HOH 51  551 277 HOH HOH A . 
E 4 HOH 52  552 25  HOH HOH A . 
E 4 HOH 53  553 144 HOH HOH A . 
E 4 HOH 54  554 8   HOH HOH A . 
E 4 HOH 55  555 271 HOH HOH A . 
E 4 HOH 56  556 245 HOH HOH A . 
E 4 HOH 57  557 205 HOH HOH A . 
E 4 HOH 58  558 159 HOH HOH A . 
E 4 HOH 59  559 234 HOH HOH A . 
E 4 HOH 60  560 213 HOH HOH A . 
E 4 HOH 61  561 60  HOH HOH A . 
E 4 HOH 62  562 172 HOH HOH A . 
E 4 HOH 63  563 30  HOH HOH A . 
E 4 HOH 64  564 190 HOH HOH A . 
E 4 HOH 65  565 152 HOH HOH A . 
E 4 HOH 66  566 70  HOH HOH A . 
E 4 HOH 67  567 95  HOH HOH A . 
E 4 HOH 68  568 53  HOH HOH A . 
E 4 HOH 69  569 10  HOH HOH A . 
E 4 HOH 70  570 151 HOH HOH A . 
E 4 HOH 71  571 44  HOH HOH A . 
E 4 HOH 72  572 26  HOH HOH A . 
E 4 HOH 73  573 50  HOH HOH A . 
E 4 HOH 74  574 125 HOH HOH A . 
E 4 HOH 75  575 221 HOH HOH A . 
E 4 HOH 76  576 22  HOH HOH A . 
E 4 HOH 77  577 81  HOH HOH A . 
E 4 HOH 78  578 23  HOH HOH A . 
E 4 HOH 79  579 48  HOH HOH A . 
E 4 HOH 80  580 316 HOH HOH A . 
E 4 HOH 81  581 116 HOH HOH A . 
E 4 HOH 82  582 165 HOH HOH A . 
E 4 HOH 83  583 52  HOH HOH A . 
E 4 HOH 84  584 67  HOH HOH A . 
E 4 HOH 85  585 7   HOH HOH A . 
E 4 HOH 86  586 83  HOH HOH A . 
E 4 HOH 87  587 138 HOH HOH A . 
E 4 HOH 88  588 324 HOH HOH A . 
E 4 HOH 89  589 9   HOH HOH A . 
E 4 HOH 90  590 18  HOH HOH A . 
E 4 HOH 91  591 88  HOH HOH A . 
E 4 HOH 92  592 201 HOH HOH A . 
E 4 HOH 93  593 31  HOH HOH A . 
E 4 HOH 94  594 79  HOH HOH A . 
E 4 HOH 95  595 90  HOH HOH A . 
E 4 HOH 96  596 43  HOH HOH A . 
E 4 HOH 97  597 157 HOH HOH A . 
E 4 HOH 98  598 192 HOH HOH A . 
E 4 HOH 99  599 300 HOH HOH A . 
E 4 HOH 100 600 260 HOH HOH A . 
E 4 HOH 101 601 184 HOH HOH A . 
E 4 HOH 102 602 117 HOH HOH A . 
E 4 HOH 103 603 15  HOH HOH A . 
E 4 HOH 104 604 12  HOH HOH A . 
E 4 HOH 105 605 206 HOH HOH A . 
E 4 HOH 106 606 5   HOH HOH A . 
E 4 HOH 107 607 29  HOH HOH A . 
E 4 HOH 108 608 45  HOH HOH A . 
E 4 HOH 109 609 261 HOH HOH A . 
E 4 HOH 110 610 227 HOH HOH A . 
E 4 HOH 111 611 92  HOH HOH A . 
E 4 HOH 112 612 20  HOH HOH A . 
E 4 HOH 113 613 247 HOH HOH A . 
E 4 HOH 114 614 28  HOH HOH A . 
E 4 HOH 115 615 72  HOH HOH A . 
E 4 HOH 116 616 114 HOH HOH A . 
E 4 HOH 117 617 321 HOH HOH A . 
E 4 HOH 118 618 74  HOH HOH A . 
E 4 HOH 119 619 21  HOH HOH A . 
E 4 HOH 120 620 233 HOH HOH A . 
E 4 HOH 121 621 249 HOH HOH A . 
E 4 HOH 122 622 68  HOH HOH A . 
E 4 HOH 123 623 17  HOH HOH A . 
E 4 HOH 124 624 75  HOH HOH A . 
E 4 HOH 125 625 242 HOH HOH A . 
E 4 HOH 126 626 38  HOH HOH A . 
E 4 HOH 127 627 86  HOH HOH A . 
E 4 HOH 128 628 129 HOH HOH A . 
E 4 HOH 129 629 35  HOH HOH A . 
E 4 HOH 130 630 148 HOH HOH A . 
E 4 HOH 131 631 82  HOH HOH A . 
E 4 HOH 132 632 274 HOH HOH A . 
E 4 HOH 133 633 4   HOH HOH A . 
E 4 HOH 134 634 106 HOH HOH A . 
E 4 HOH 135 635 194 HOH HOH A . 
E 4 HOH 136 636 319 HOH HOH A . 
E 4 HOH 137 637 320 HOH HOH A . 
E 4 HOH 138 638 240 HOH HOH A . 
E 4 HOH 139 639 189 HOH HOH A . 
E 4 HOH 140 640 181 HOH HOH A . 
E 4 HOH 141 641 3   HOH HOH A . 
E 4 HOH 142 642 141 HOH HOH A . 
E 4 HOH 143 643 166 HOH HOH A . 
E 4 HOH 144 644 285 HOH HOH A . 
E 4 HOH 145 645 41  HOH HOH A . 
E 4 HOH 146 646 286 HOH HOH A . 
E 4 HOH 147 647 16  HOH HOH A . 
E 4 HOH 148 648 36  HOH HOH A . 
E 4 HOH 149 649 235 HOH HOH A . 
E 4 HOH 150 650 76  HOH HOH A . 
E 4 HOH 151 651 297 HOH HOH A . 
E 4 HOH 152 652 212 HOH HOH A . 
E 4 HOH 153 653 191 HOH HOH A . 
E 4 HOH 154 654 59  HOH HOH A . 
E 4 HOH 155 655 296 HOH HOH A . 
E 4 HOH 156 656 284 HOH HOH A . 
E 4 HOH 157 657 56  HOH HOH A . 
E 4 HOH 158 658 130 HOH HOH A . 
E 4 HOH 159 659 132 HOH HOH A . 
E 4 HOH 160 660 246 HOH HOH A . 
E 4 HOH 161 661 301 HOH HOH A . 
E 4 HOH 162 662 124 HOH HOH A . 
E 4 HOH 163 663 154 HOH HOH A . 
E 4 HOH 164 664 322 HOH HOH A . 
E 4 HOH 165 665 243 HOH HOH A . 
E 4 HOH 166 666 232 HOH HOH A . 
E 4 HOH 167 667 113 HOH HOH A . 
E 4 HOH 168 668 136 HOH HOH A . 
E 4 HOH 169 669 203 HOH HOH A . 
E 4 HOH 170 670 204 HOH HOH A . 
E 4 HOH 171 671 199 HOH HOH A . 
E 4 HOH 172 672 69  HOH HOH A . 
E 4 HOH 173 673 202 HOH HOH A . 
E 4 HOH 174 674 128 HOH HOH A . 
E 4 HOH 175 675 250 HOH HOH A . 
E 4 HOH 176 676 241 HOH HOH A . 
E 4 HOH 177 677 108 HOH HOH A . 
E 4 HOH 178 678 180 HOH HOH A . 
E 4 HOH 179 679 119 HOH HOH A . 
E 4 HOH 180 680 318 HOH HOH A . 
E 4 HOH 181 681 120 HOH HOH A . 
E 4 HOH 182 682 121 HOH HOH A . 
E 4 HOH 183 683 210 HOH HOH A . 
E 4 HOH 184 684 317 HOH HOH A . 
E 4 HOH 185 685 61  HOH HOH A . 
E 4 HOH 186 686 207 HOH HOH A . 
E 4 HOH 187 687 87  HOH HOH A . 
E 4 HOH 188 688 140 HOH HOH A . 
E 4 HOH 189 689 80  HOH HOH A . 
E 4 HOH 190 690 139 HOH HOH A . 
E 4 HOH 191 691 47  HOH HOH A . 
E 4 HOH 192 692 323 HOH HOH A . 
E 4 HOH 193 693 220 HOH HOH A . 
E 4 HOH 194 694 251 HOH HOH A . 
E 4 HOH 195 695 135 HOH HOH A . 
E 4 HOH 196 696 110 HOH HOH A . 
E 4 HOH 197 697 143 HOH HOH A . 
E 4 HOH 198 698 99  HOH HOH A . 
E 4 HOH 199 699 161 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 132 ? CG  ? A LYS 160 CG  
2  1 Y 1 A LYS 132 ? CD  ? A LYS 160 CD  
3  1 Y 1 A LYS 132 ? CE  ? A LYS 160 CE  
4  1 Y 1 A LYS 132 ? NZ  ? A LYS 160 NZ  
5  1 Y 1 A ARG 144 ? CG  ? A ARG 172 CG  
6  1 Y 1 A ARG 144 ? CD  ? A ARG 172 CD  
7  1 Y 1 A ARG 144 ? NE  ? A ARG 172 NE  
8  1 Y 1 A ARG 144 ? CZ  ? A ARG 172 CZ  
9  1 Y 1 A ARG 144 ? NH1 ? A ARG 172 NH1 
10 1 Y 1 A ARG 144 ? NH2 ? A ARG 172 NH2 
11 1 Y 1 A GLU 260 ? CG  ? A GLU 288 CG  
12 1 Y 1 A GLU 260 ? CD  ? A GLU 288 CD  
13 1 Y 1 A GLU 260 ? OE1 ? A GLU 288 OE1 
14 1 Y 1 A GLU 260 ? OE2 ? A GLU 288 OE2 
15 1 N 1 A FAD 401 ? PA  ? B FAD 1   PA  
16 1 N 1 A FAD 401 ? O1A ? B FAD 1   O1A 
17 1 N 1 A FAD 401 ? O2A ? B FAD 1   O2A 
18 1 N 1 A FAD 401 ? O5B ? B FAD 1   O5B 
19 1 N 1 A FAD 401 ? C5B ? B FAD 1   C5B 
20 1 N 1 A FAD 401 ? C4B ? B FAD 1   C4B 
21 1 N 1 A FAD 401 ? O4B ? B FAD 1   O4B 
22 1 N 1 A FAD 401 ? C3B ? B FAD 1   C3B 
23 1 N 1 A FAD 401 ? O3B ? B FAD 1   O3B 
24 1 N 1 A FAD 401 ? C2B ? B FAD 1   C2B 
25 1 N 1 A FAD 401 ? O2B ? B FAD 1   O2B 
26 1 N 1 A FAD 401 ? C1B ? B FAD 1   C1B 
27 1 N 1 A FAD 401 ? N9A ? B FAD 1   N9A 
28 1 N 1 A FAD 401 ? C8A ? B FAD 1   C8A 
29 1 N 1 A FAD 401 ? N7A ? B FAD 1   N7A 
30 1 N 1 A FAD 401 ? C5A ? B FAD 1   C5A 
31 1 N 1 A FAD 401 ? C6A ? B FAD 1   C6A 
32 1 N 1 A FAD 401 ? N6A ? B FAD 1   N6A 
33 1 N 1 A FAD 401 ? N1A ? B FAD 1   N1A 
34 1 N 1 A FAD 401 ? C2A ? B FAD 1   C2A 
35 1 N 1 A FAD 401 ? N3A ? B FAD 1   N3A 
36 1 N 1 A FAD 401 ? C4A ? B FAD 1   C4A 
# 
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  ? ? ? '(1.19.2_4158: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? 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                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9F1Y 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     101.284 
_cell.length_a_esd                 ? 
_cell.length_b                     53.455 
_cell.length_b_esd                 ? 
_cell.length_c                     71.840 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9F1Y 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 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                   9F1Y 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.51 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          51.08 
_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              8.5 
_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    '0.06 M divalents, 0.1 M Tris-Bicine, 30% v/v PEG550 MME-PEG20000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 2M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-09-12 
_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   0.98 
_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                        'ESRF BEAMLINE MASSIF-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.98 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MASSIF-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9F1Y 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.95 
_reflns.d_resolution_low                               47.27 
_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                                     29158 
_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                                6.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.96 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.086 
_reflns.pdbx_Rpim_I_all                                0.034 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       186652 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.079 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.95 
_reflns_shell.d_res_low                                     2.00 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           13233 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2022 
_reflns_shell.percent_possible_obs                          99.8 
_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                               6.5 
_reflns_shell.pdbx_chi_squared                              0.96 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.6 
_reflns_shell.pdbx_Rrim_I_all                               1.331 
_reflns_shell.pdbx_Rpim_I_all                               0.514 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.702 
_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                                  1.225 
_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                                 9F1Y 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.95 
_refine.ls_d_res_low                             47.27 
_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                     29158 
_refine.ls_number_reflns_R_free                  2808 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.62 
_refine.ls_percent_reflns_R_free                 5.18 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1995 
_refine.ls_R_factor_R_free                       0.2273 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1980 
_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                          1.10 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       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                 25.93 
_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                            0.27 
_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                       1.95 
_refine_hist.d_res_low                        47.27 
_refine_hist.number_atoms_solvent             199 
_refine_hist.number_atoms_total               2977 
_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        2745 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         33 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008  ? 2849 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.921  ? 3860 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 11.181 ? 392  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.060  ? 449  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.010  ? 490  ? f_plane_restr      ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.95 
_refine_ls_shell.d_res_low                        1.98 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             133 
_refine_ls_shell.number_reflns_R_work             2577 
_refine_ls_shell.percent_reflns_obs               99.00 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.3549 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   ? 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.3949 
# 
_struct.entry_id                     9F1Y 
_struct.title                        'Crystal structure of Oscillatoria acuminata adenylyate cyclase at 100K' 
_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        9F1Y 
_struct_keywords.text            'FAD, , adenylate cyclase, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    K9TLZ5_9CYAN 
_struct_ref.pdbx_db_accession          K9TLZ5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MKRLTYISKFSRPLSGDEIEAIGRISSQKNQQANVTGVLLCLDGIFFQILEGEAEKIDRIYERILADERHTDILCLKSEV
EVQERMFPDWSMQTINLDENTDFLIRPIKVLLQTLTESHRILEKYTQPSIFKIISQGTNPLNIRPKAVEKIVFFSDIVSF
STFAEKLPVEEVVSVVNSYFSVCTAIITRQGGEVTKFIGDCVMAYFDGDCADQAIQASLDILMELEILRNSAPEGSPLRV
LYSGIGLAKGKVIEGNIGSELKRDYTILGDAVNVAARLEALTRQLSQALVFSSEVKNSATKSWNFIWLTDSELKGKSESI
DIYSIDNEMTRKSSGGLEIARNIGHYLERVGDRQPSQIFGVKSLPL
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9F1Y 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 29 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 394 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             K9TLZ5 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  366 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       366 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9F1Y MET A 1  ? UNP K9TLZ5 ? ? 'initiating methionine' -27 1  
1 9F1Y GLY A 2  ? UNP K9TLZ5 ? ? 'expression tag'        -26 2  
1 9F1Y SER A 3  ? UNP K9TLZ5 ? ? 'expression tag'        -25 3  
1 9F1Y SER A 4  ? UNP K9TLZ5 ? ? 'expression tag'        -24 4  
1 9F1Y HIS A 5  ? UNP K9TLZ5 ? ? 'expression tag'        -23 5  
1 9F1Y HIS A 6  ? UNP K9TLZ5 ? ? 'expression tag'        -22 6  
1 9F1Y HIS A 7  ? UNP K9TLZ5 ? ? 'expression tag'        -21 7  
1 9F1Y HIS A 8  ? UNP K9TLZ5 ? ? 'expression tag'        -20 8  
1 9F1Y HIS A 9  ? UNP K9TLZ5 ? ? 'expression tag'        -19 9  
1 9F1Y HIS A 10 ? UNP K9TLZ5 ? ? 'expression tag'        -18 10 
1 9F1Y SER A 11 ? UNP K9TLZ5 ? ? 'expression tag'        -17 11 
1 9F1Y SER A 12 ? UNP K9TLZ5 ? ? 'expression tag'        -16 12 
1 9F1Y GLY A 13 ? UNP K9TLZ5 ? ? 'expression tag'        -15 13 
1 9F1Y LEU A 14 ? UNP K9TLZ5 ? ? 'expression tag'        -14 14 
1 9F1Y VAL A 15 ? UNP K9TLZ5 ? ? 'expression tag'        -13 15 
1 9F1Y PRO A 16 ? UNP K9TLZ5 ? ? 'expression tag'        -12 16 
1 9F1Y ARG A 17 ? UNP K9TLZ5 ? ? 'expression tag'        -11 17 
1 9F1Y GLY A 18 ? UNP K9TLZ5 ? ? 'expression tag'        -10 18 
1 9F1Y SER A 19 ? UNP K9TLZ5 ? ? 'expression tag'        -9  19 
1 9F1Y HIS A 20 ? UNP K9TLZ5 ? ? 'expression tag'        -8  20 
1 9F1Y MET A 21 ? UNP K9TLZ5 ? ? 'expression tag'        -7  21 
1 9F1Y GLU A 22 ? UNP K9TLZ5 ? ? 'expression tag'        -6  22 
1 9F1Y ASN A 23 ? UNP K9TLZ5 ? ? 'expression tag'        -5  23 
1 9F1Y LEU A 24 ? UNP K9TLZ5 ? ? 'expression tag'        -4  24 
1 9F1Y TYR A 25 ? UNP K9TLZ5 ? ? 'expression tag'        -3  25 
1 9F1Y PHE A 26 ? UNP K9TLZ5 ? ? 'expression tag'        -2  26 
1 9F1Y GLN A 27 ? UNP K9TLZ5 ? ? 'expression tag'        -1  27 
1 9F1Y GLY A 28 ? UNP K9TLZ5 ? ? 'expression tag'        0   28 
# 
_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)' 10260 ? 
1 MORE         -121  ? 
1 'SSA (A^2)'  29310 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z   1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
2 'crystal symmetry operation' 2_555 -x,-y,z -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 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 SER A 43  ? ASN A 62  ? SER A 15  ASN A 34  1 ? 20 
HELX_P HELX_P2  AA2 ALA A 82  ? ASP A 95  ? ALA A 54  ASP A 67  1 ? 14 
HELX_P HELX_P3  AA3 LEU A 132 ? TYR A 153 ? LEU A 104 TYR A 125 1 ? 22 
HELX_P HELX_P4  AA4 GLN A 155 ? GLN A 164 ? GLN A 127 GLN A 136 1 ? 10 
HELX_P HELX_P5  AA5 ASN A 167 ? ILE A 171 ? ASN A 139 ILE A 143 5 ? 5  
HELX_P HELX_P6  AA6 SER A 187 ? LEU A 195 ? SER A 159 LEU A 167 1 ? 9  
HELX_P HELX_P7  AA7 PRO A 196 ? GLN A 218 ? PRO A 168 GLN A 190 1 ? 23 
HELX_P HELX_P8  AA8 CYS A 238 ? ALA A 260 ? CYS A 210 ALA A 232 1 ? 23 
HELX_P HELX_P9  AA9 SER A 264 ? LEU A 269 ? SER A 236 LEU A 241 5 ? 6  
HELX_P HELX_P10 AB1 ASP A 298 ? SER A 314 ? ASP A 270 SER A 286 1 ? 17 
HELX_P HELX_P11 AB2 SER A 321 ? ALA A 327 ? SER A 293 ALA A 299 1 ? 7  
HELX_P HELX_P12 AB3 LEU A 365 ? ARG A 377 ? LEU A 337 ARG A 349 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A ASP 117 O   ? ? ? 1_555 C CA  . CA ? ? A ASP 89  A CA  402 1_556 ? ? ? ? ? ? ? 2.427 ? ? 
metalc2  metalc ? ? A ASP 184 OD2 ? ? ? 1_555 D CA  . CA ? ? A ASP 156 A CA  403 1_555 ? ? ? ? ? ? ? 2.434 ? ? 
metalc3  metalc ? ? A ASP 228 OD1 ? ? ? 1_555 D CA  . CA ? ? A ASP 200 A CA  403 1_555 ? ? ? ? ? ? ? 3.058 ? ? 
metalc4  metalc ? ? A ASP 228 OD2 ? ? ? 1_555 D CA  . CA ? ? A ASP 200 A CA  403 1_555 ? ? ? ? ? ? ? 2.381 ? ? 
metalc5  metalc ? ? A ASP 298 OD1 ? ? ? 1_555 D CA  . CA ? ? A ASP 270 A CA  403 2_555 ? ? ? ? ? ? ? 2.689 ? ? 
metalc6  metalc ? ? A ASP 338 OD1 ? ? ? 1_555 C CA  . CA ? ? A ASP 310 A CA  402 1_555 ? ? ? ? ? ? ? 2.543 ? ? 
metalc7  metalc ? ? A ASP 338 OD2 ? ? ? 1_555 C CA  . CA ? ? A ASP 310 A CA  402 1_555 ? ? ? ? ? ? ? 2.346 ? ? 
metalc8  metalc ? ? A ASP 349 OD1 ? ? ? 1_555 C CA  . CA ? ? A ASP 321 A CA  402 1_555 ? ? ? ? ? ? ? 2.374 ? ? 
metalc9  metalc ? ? C CA  .   CA  ? ? ? 1_555 E HOH . O  ? ? A CA  402 A HOH 606 1_555 ? ? ? ? ? ? ? 2.345 ? ? 
metalc10 metalc ? ? C CA  .   CA  ? ? ? 1_555 E HOH . O  ? ? A CA  402 A HOH 647 1_554 ? ? ? ? ? ? ? 2.517 ? ? 
metalc11 metalc ? ? C CA  .   CA  ? ? ? 1_555 E HOH . O  ? ? A CA  402 A HOH 648 1_555 ? ? ? ? ? ? ? 2.378 ? ? 
metalc12 metalc ? ? D CA  .   CA  ? ? ? 1_555 E HOH . O  ? ? A CA  403 A HOH 502 2_555 ? ? ? ? ? ? ? 2.307 ? ? 
metalc13 metalc ? ? D CA  .   CA  ? ? ? 1_555 E HOH . O  ? ? A CA  403 A HOH 521 1_555 ? ? ? ? ? ? ? 2.836 ? ? 
metalc14 metalc ? ? D CA  .   CA  ? ? ? 1_555 E HOH . O  ? ? A CA  403 A HOH 532 1_555 ? ? ? ? ? ? ? 2.333 ? ? 
metalc15 metalc ? ? D CA  .   CA  ? ? ? 1_555 E HOH . O  ? ? A CA  403 A HOH 632 1_555 ? ? ? ? ? ? ? 3.089 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O   ? A ASP 117 ? A ASP 89  ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 OD1 ? A ASP 338 ? A ASP 310 ? 1_555 28.6  ? 
2  O   ? A ASP 117 ? A ASP 89  ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 OD2 ? A ASP 338 ? A ASP 310 ? 1_555 27.1  ? 
3  OD1 ? A ASP 338 ? A ASP 310 ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 OD2 ? A ASP 338 ? A ASP 310 ? 1_555 1.5   ? 
4  O   ? A ASP 117 ? A ASP 89  ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 OD1 ? A ASP 349 ? A ASP 321 ? 1_555 29.0  ? 
5  OD1 ? A ASP 338 ? A ASP 310 ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 OD1 ? A ASP 349 ? A ASP 321 ? 1_555 2.2   ? 
6  OD2 ? A ASP 338 ? A ASP 310 ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 OD1 ? A ASP 349 ? A ASP 321 ? 1_555 2.8   ? 
7  O   ? A ASP 117 ? A ASP 89  ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 606 ? 1_555 26.4  ? 
8  OD1 ? A ASP 338 ? A ASP 310 ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 606 ? 1_555 3.1   ? 
9  OD2 ? A ASP 338 ? A ASP 310 ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 606 ? 1_555 2.2   ? 
10 OD1 ? A ASP 349 ? A ASP 321 ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 606 ? 1_555 2.7   ? 
11 O   ? A ASP 117 ? A ASP 89  ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 647 ? 1_554 29.3  ? 
12 OD1 ? A ASP 338 ? A ASP 310 ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 647 ? 1_554 2.4   ? 
13 OD2 ? A ASP 338 ? A ASP 310 ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 647 ? 1_554 3.1   ? 
14 OD1 ? A ASP 349 ? A ASP 321 ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 647 ? 1_554 0.3   ? 
15 O   ? E HOH .   ? A HOH 606 ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 647 ? 1_554 2.9   ? 
16 O   ? A ASP 117 ? A ASP 89  ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 648 ? 1_555 27.8  ? 
17 OD1 ? A ASP 338 ? A ASP 310 ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 648 ? 1_555 3.8   ? 
18 OD2 ? A ASP 338 ? A ASP 310 ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 648 ? 1_555 3.6   ? 
19 OD1 ? A ASP 349 ? A ASP 321 ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 648 ? 1_555 2.0   ? 
20 O   ? E HOH .   ? A HOH 606 ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 648 ? 1_555 2.0   ? 
21 O   ? E HOH .   ? A HOH 647 ? 1_554 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 648 ? 1_555 2.1   ? 
22 OD2 ? A ASP 184 ? A ASP 156 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 OD1 ? A ASP 228 ? A ASP 200 ? 1_555 129.4 ? 
23 OD2 ? A ASP 184 ? A ASP 156 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 OD2 ? A ASP 228 ? A ASP 200 ? 1_555 104.2 ? 
24 OD1 ? A ASP 228 ? A ASP 200 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 OD2 ? A ASP 228 ? A ASP 200 ? 1_555 44.9  ? 
25 OD2 ? A ASP 184 ? A ASP 156 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 OD1 ? A ASP 298 ? A ASP 270 ? 1_555 72.9  ? 
26 OD1 ? A ASP 228 ? A ASP 200 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 OD1 ? A ASP 298 ? A ASP 270 ? 1_555 84.4  ? 
27 OD2 ? A ASP 228 ? A ASP 200 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 OD1 ? A ASP 298 ? A ASP 270 ? 1_555 112.7 ? 
28 OD2 ? A ASP 184 ? A ASP 156 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 502 ? 2_555 86.0  ? 
29 OD1 ? A ASP 228 ? A ASP 200 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 502 ? 2_555 102.2 ? 
30 OD2 ? A ASP 228 ? A ASP 200 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 502 ? 2_555 144.0 ? 
31 OD1 ? A ASP 298 ? A ASP 270 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 502 ? 2_555 36.9  ? 
32 OD2 ? A ASP 184 ? A ASP 156 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 521 ? 1_555 83.9  ? 
33 OD1 ? A ASP 228 ? A ASP 200 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 521 ? 1_555 67.2  ? 
34 OD2 ? A ASP 228 ? A ASP 200 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 521 ? 1_555 97.4  ? 
35 OD1 ? A ASP 298 ? A ASP 270 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 521 ? 1_555 17.4  ? 
36 O   ? E HOH .   ? A HOH 502 ? 2_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 521 ? 1_555 48.7  ? 
37 OD2 ? A ASP 184 ? A ASP 156 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 532 ? 1_555 101.0 ? 
38 OD1 ? A ASP 228 ? A ASP 200 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 532 ? 1_555 123.0 ? 
39 OD2 ? A ASP 228 ? A ASP 200 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 532 ? 1_555 105.1 ? 
40 OD1 ? A ASP 298 ? A ASP 270 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 532 ? 1_555 142.1 ? 
41 O   ? E HOH .   ? A HOH 502 ? 2_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 532 ? 1_555 106.6 ? 
42 O   ? E HOH .   ? A HOH 521 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 532 ? 1_555 154.8 ? 
43 OD2 ? A ASP 184 ? A ASP 156 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 632 ? 1_555 79.5  ? 
44 OD1 ? A ASP 228 ? A ASP 200 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 632 ? 1_555 135.2 ? 
45 OD2 ? A ASP 228 ? A ASP 200 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 632 ? 1_555 174.5 ? 
46 OD1 ? A ASP 298 ? A ASP 270 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 632 ? 1_555 72.0  ? 
47 O   ? E HOH .   ? A HOH 502 ? 2_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 632 ? 1_555 39.2  ? 
48 O   ? E HOH .   ? A HOH 521 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 632 ? 1_555 86.8  ? 
49 O   ? E HOH .   ? A HOH 532 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 632 ? 1_555 70.1  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? parallel      
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 HIS A 98  ? VAL A 110 ? HIS A 70  VAL A 82  
AA1 2 MET A 29  ? PHE A 38  ? MET A 1   PHE A 10  
AA1 3 ILE A 73  ? GLU A 81  ? ILE A 45  GLU A 53  
AA1 4 THR A 64  ? LEU A 70  ? THR A 36  LEU A 42  
AA1 5 GLN A 121 ? ASN A 124 ? GLN A 93  ASN A 96  
AA2 1 GLU A 221 ? ILE A 226 ? GLU A 193 ILE A 198 
AA2 2 CYS A 229 ? ASP A 235 ? CYS A 201 ASP A 207 
AA2 3 LYS A 174 ? ILE A 185 ? LYS A 146 ILE A 157 
AA2 4 SER A 271 ? GLY A 286 ? SER A 243 GLY A 258 
AA2 5 ARG A 291 ? ILE A 295 ? ARG A 263 ILE A 267 
AA3 1 GLU A 221 ? ILE A 226 ? GLU A 193 ILE A 198 
AA3 2 CYS A 229 ? ASP A 235 ? CYS A 201 ASP A 207 
AA3 3 LYS A 174 ? ILE A 185 ? LYS A 146 ILE A 157 
AA3 4 SER A 271 ? GLY A 286 ? SER A 243 GLY A 258 
AA3 5 LEU A 317 ? SER A 320 ? LEU A 289 SER A 292 
AA3 6 ILE A 348 ? ILE A 353 ? ILE A 320 ILE A 325 
AA3 7 PHE A 333 ? SER A 339 ? PHE A 305 SER A 311 
# 
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 O GLU A 107 ? O GLU A 79  N ARG A 31  ? N ARG A 3   
AA1 2 3 N LYS A 30  ? N LYS A 2   O GLY A 80  ? O GLY A 52  
AA1 3 4 O PHE A 75  ? O PHE A 47  N LEU A 68  ? N LEU A 40  
AA1 4 5 N LEU A 67  ? N LEU A 39  O GLN A 121 ? O GLN A 93  
AA2 1 2 N ILE A 226 ? N ILE A 198 O CYS A 229 ? O CYS A 201 
AA2 2 3 O ALA A 232 ? O ALA A 204 N PHE A 181 ? N PHE A 153 
AA2 3 4 N PHE A 182 ? N PHE A 154 O GLY A 274 ? O GLY A 246 
AA2 4 5 N ILE A 281 ? N ILE A 253 O ILE A 295 ? O ILE A 267 
AA3 1 2 N ILE A 226 ? N ILE A 198 O CYS A 229 ? O CYS A 201 
AA3 2 3 O ALA A 232 ? O ALA A 204 N PHE A 181 ? N PHE A 153 
AA3 3 4 N PHE A 182 ? N PHE A 154 O GLY A 274 ? O GLY A 246 
AA3 4 5 N ILE A 273 ? N ILE A 245 O VAL A 318 ? O VAL A 290 
AA3 5 6 N PHE A 319 ? N PHE A 291 O TYR A 351 ? O TYR A 323 
AA3 6 7 O ILE A 350 ? O ILE A 322 N THR A 337 ? N THR A 309 
# 
_pdbx_entry_details.entry_id                   9F1Y 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_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 HOH 610 ? ? O A HOH 653 ? ? 1.98 
2 1 O   A HOH 594 ? ? O A HOH 657 ? ? 2.04 
3 1 OE1 A GLN 28  ? A O A HOH 501 ? ? 2.17 
4 1 O   A HOH 549 ? ? O A HOH 633 ? ? 2.17 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 502 ? ? 1_555 O A HOH 632 ? ? 2_555 1.96 
2 1 O A HOH 670 ? ? 1_555 O A HOH 678 ? ? 3_545 1.96 
3 1 O A HOH 656 ? ? 1_555 O A HOH 657 ? ? 1_554 2.05 
4 1 O A HOH 502 ? ? 1_555 O A HOH 521 ? ? 2_555 2.17 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    GLU 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     260 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             67.94 
_pdbx_validate_torsion.psi             -40.91 
# 
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 -27 ? A MET 1   
2  1 Y 1 A GLY -26 ? A GLY 2   
3  1 Y 1 A SER -25 ? A SER 3   
4  1 Y 1 A SER -24 ? A SER 4   
5  1 Y 1 A HIS -23 ? A HIS 5   
6  1 Y 1 A HIS -22 ? A HIS 6   
7  1 Y 1 A HIS -21 ? A HIS 7   
8  1 Y 1 A HIS -20 ? A HIS 8   
9  1 Y 1 A HIS -19 ? A HIS 9   
10 1 Y 1 A HIS -18 ? A HIS 10  
11 1 Y 1 A SER -17 ? A SER 11  
12 1 Y 1 A SER -16 ? A SER 12  
13 1 Y 1 A GLY -15 ? A GLY 13  
14 1 Y 1 A LEU -14 ? A LEU 14  
15 1 Y 1 A VAL -13 ? A VAL 15  
16 1 Y 1 A PRO -12 ? A PRO 16  
17 1 Y 1 A ARG -11 ? A ARG 17  
18 1 Y 1 A GLY -10 ? A GLY 18  
19 1 Y 1 A SER -9  ? A SER 19  
20 1 Y 1 A HIS -8  ? A HIS 20  
21 1 Y 1 A MET -7  ? A MET 21  
22 1 Y 1 A GLU -6  ? A GLU 22  
23 1 Y 1 A ASN -5  ? A ASN 23  
24 1 Y 1 A LEU -4  ? A LEU 24  
25 1 Y 1 A TYR -3  ? A TYR 25  
26 1 Y 1 A PHE -2  ? A PHE 26  
27 1 Y 1 A GLN -1  ? A GLN 27  
28 1 Y 1 A GLY 335 ? A GLY 363 
29 1 Y 1 A GLY 351 ? A GLY 379 
30 1 Y 1 A ASP 352 ? A ASP 380 
31 1 Y 1 A ARG 353 ? A ARG 381 
32 1 Y 1 A GLN 354 ? A GLN 382 
33 1 Y 1 A PRO 355 ? A PRO 383 
34 1 Y 1 A SER 356 ? A SER 384 
35 1 Y 1 A GLN 357 ? A GLN 385 
36 1 Y 1 A ILE 358 ? A ILE 386 
37 1 Y 1 A PHE 359 ? A PHE 387 
38 1 Y 1 A GLY 360 ? A GLY 388 
39 1 Y 1 A VAL 361 ? A VAL 389 
40 1 Y 1 A LYS 362 ? A LYS 390 
41 1 Y 1 A SER 363 ? A SER 391 
42 1 Y 1 A LEU 364 ? A LEU 392 
43 1 Y 1 A PRO 365 ? A PRO 393 
44 1 Y 1 A LEU 366 ? A LEU 394 
# 
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  
CA  CA     CA N N 74  
CYS N      N  N N 75  
CYS CA     C  N R 76  
CYS C      C  N N 77  
CYS O      O  N N 78  
CYS CB     C  N N 79  
CYS SG     S  N N 80  
CYS OXT    O  N N 81  
CYS H      H  N N 82  
CYS H2     H  N N 83  
CYS HA     H  N N 84  
CYS HB2    H  N N 85  
CYS HB3    H  N N 86  
CYS HG     H  N N 87  
CYS HXT    H  N N 88  
FAD PA     P  N R 89  
FAD O1A    O  N N 90  
FAD O2A    O  N N 91  
FAD O5B    O  N N 92  
FAD C5B    C  N N 93  
FAD C4B    C  N R 94  
FAD O4B    O  N N 95  
FAD C3B    C  N S 96  
FAD O3B    O  N N 97  
FAD C2B    C  N R 98  
FAD O2B    O  N N 99  
FAD C1B    C  N R 100 
FAD N9A    N  Y N 101 
FAD C8A    C  Y N 102 
FAD N7A    N  Y N 103 
FAD C5A    C  Y N 104 
FAD C6A    C  Y N 105 
FAD N6A    N  N N 106 
FAD N1A    N  Y N 107 
FAD C2A    C  Y N 108 
FAD N3A    N  Y N 109 
FAD C4A    C  Y N 110 
FAD N1     N  N N 111 
FAD C2     C  N N 112 
FAD O2     O  N N 113 
FAD N3     N  N N 114 
FAD C4     C  N N 115 
FAD O4     O  N N 116 
FAD C4X    C  N N 117 
FAD N5     N  N N 118 
FAD C5X    C  Y N 119 
FAD C6     C  Y N 120 
FAD C7     C  Y N 121 
FAD C7M    C  N N 122 
FAD C8     C  Y N 123 
FAD C8M    C  N N 124 
FAD C9     C  Y N 125 
FAD C9A    C  Y N 126 
FAD N10    N  N N 127 
FAD C10    C  N N 128 
FAD "C1'"  C  N N 129 
FAD "C2'"  C  N S 130 
FAD "O2'"  O  N N 131 
FAD "C3'"  C  N S 132 
FAD "O3'"  O  N N 133 
FAD "C4'"  C  N R 134 
FAD "O4'"  O  N N 135 
FAD "C5'"  C  N N 136 
FAD "O5'"  O  N N 137 
FAD P      P  N R 138 
FAD O1P    O  N N 139 
FAD O2P    O  N N 140 
FAD O3P    O  N N 141 
FAD HOA2   H  N N 142 
FAD H51A   H  N N 143 
FAD H52A   H  N N 144 
FAD H4B    H  N N 145 
FAD H3B    H  N N 146 
FAD HO3A   H  N N 147 
FAD H2B    H  N N 148 
FAD HO2A   H  N N 149 
FAD H1B    H  N N 150 
FAD H8A    H  N N 151 
FAD H61A   H  N N 152 
FAD H62A   H  N N 153 
FAD H2A    H  N N 154 
FAD HN3    H  N N 155 
FAD H6     H  N N 156 
FAD HM71   H  N N 157 
FAD HM72   H  N N 158 
FAD HM73   H  N N 159 
FAD HM81   H  N N 160 
FAD HM82   H  N N 161 
FAD HM83   H  N N 162 
FAD H9     H  N N 163 
FAD "H1'1" H  N N 164 
FAD "H1'2" H  N N 165 
FAD "H2'"  H  N N 166 
FAD "HO2'" H  N N 167 
FAD "H3'"  H  N N 168 
FAD "HO3'" H  N N 169 
FAD "H4'"  H  N N 170 
FAD "HO4'" H  N N 171 
FAD "H5'1" H  N N 172 
FAD "H5'2" H  N N 173 
FAD HOP2   H  N N 174 
GLN N      N  N N 175 
GLN CA     C  N S 176 
GLN C      C  N N 177 
GLN O      O  N N 178 
GLN CB     C  N N 179 
GLN CG     C  N N 180 
GLN CD     C  N N 181 
GLN OE1    O  N N 182 
GLN NE2    N  N N 183 
GLN OXT    O  N N 184 
GLN H      H  N N 185 
GLN H2     H  N N 186 
GLN HA     H  N N 187 
GLN HB2    H  N N 188 
GLN HB3    H  N N 189 
GLN HG2    H  N N 190 
GLN HG3    H  N N 191 
GLN HE21   H  N N 192 
GLN HE22   H  N N 193 
GLN HXT    H  N N 194 
GLU N      N  N N 195 
GLU CA     C  N S 196 
GLU C      C  N N 197 
GLU O      O  N N 198 
GLU CB     C  N N 199 
GLU CG     C  N N 200 
GLU CD     C  N N 201 
GLU OE1    O  N N 202 
GLU OE2    O  N N 203 
GLU OXT    O  N N 204 
GLU H      H  N N 205 
GLU H2     H  N N 206 
GLU HA     H  N N 207 
GLU HB2    H  N N 208 
GLU HB3    H  N N 209 
GLU HG2    H  N N 210 
GLU HG3    H  N N 211 
GLU HE2    H  N N 212 
GLU HXT    H  N N 213 
GLY N      N  N N 214 
GLY CA     C  N N 215 
GLY C      C  N N 216 
GLY O      O  N N 217 
GLY OXT    O  N N 218 
GLY H      H  N N 219 
GLY H2     H  N N 220 
GLY HA2    H  N N 221 
GLY HA3    H  N N 222 
GLY HXT    H  N N 223 
HIS N      N  N N 224 
HIS CA     C  N S 225 
HIS C      C  N N 226 
HIS O      O  N N 227 
HIS CB     C  N N 228 
HIS CG     C  Y N 229 
HIS ND1    N  Y N 230 
HIS CD2    C  Y N 231 
HIS CE1    C  Y N 232 
HIS NE2    N  Y N 233 
HIS OXT    O  N N 234 
HIS H      H  N N 235 
HIS H2     H  N N 236 
HIS HA     H  N N 237 
HIS HB2    H  N N 238 
HIS HB3    H  N N 239 
HIS HD1    H  N N 240 
HIS HD2    H  N N 241 
HIS HE1    H  N N 242 
HIS HE2    H  N N 243 
HIS HXT    H  N N 244 
HOH O      O  N N 245 
HOH H1     H  N N 246 
HOH H2     H  N N 247 
ILE N      N  N N 248 
ILE CA     C  N S 249 
ILE C      C  N N 250 
ILE O      O  N N 251 
ILE CB     C  N S 252 
ILE CG1    C  N N 253 
ILE CG2    C  N N 254 
ILE CD1    C  N N 255 
ILE OXT    O  N N 256 
ILE H      H  N N 257 
ILE H2     H  N N 258 
ILE HA     H  N N 259 
ILE HB     H  N N 260 
ILE HG12   H  N N 261 
ILE HG13   H  N N 262 
ILE HG21   H  N N 263 
ILE HG22   H  N N 264 
ILE HG23   H  N N 265 
ILE HD11   H  N N 266 
ILE HD12   H  N N 267 
ILE HD13   H  N N 268 
ILE HXT    H  N N 269 
LEU N      N  N N 270 
LEU CA     C  N S 271 
LEU C      C  N N 272 
LEU O      O  N N 273 
LEU CB     C  N N 274 
LEU CG     C  N N 275 
LEU CD1    C  N N 276 
LEU CD2    C  N N 277 
LEU OXT    O  N N 278 
LEU H      H  N N 279 
LEU H2     H  N N 280 
LEU HA     H  N N 281 
LEU HB2    H  N N 282 
LEU HB3    H  N N 283 
LEU HG     H  N N 284 
LEU HD11   H  N N 285 
LEU HD12   H  N N 286 
LEU HD13   H  N N 287 
LEU HD21   H  N N 288 
LEU HD22   H  N N 289 
LEU HD23   H  N N 290 
LEU HXT    H  N N 291 
LYS N      N  N N 292 
LYS CA     C  N S 293 
LYS C      C  N N 294 
LYS O      O  N N 295 
LYS CB     C  N N 296 
LYS CG     C  N N 297 
LYS CD     C  N N 298 
LYS CE     C  N N 299 
LYS NZ     N  N N 300 
LYS OXT    O  N N 301 
LYS H      H  N N 302 
LYS H2     H  N N 303 
LYS HA     H  N N 304 
LYS HB2    H  N N 305 
LYS HB3    H  N N 306 
LYS HG2    H  N N 307 
LYS HG3    H  N N 308 
LYS HD2    H  N N 309 
LYS HD3    H  N N 310 
LYS HE2    H  N N 311 
LYS HE3    H  N N 312 
LYS HZ1    H  N N 313 
LYS HZ2    H  N N 314 
LYS HZ3    H  N N 315 
LYS HXT    H  N N 316 
MET N      N  N N 317 
MET CA     C  N S 318 
MET C      C  N N 319 
MET O      O  N N 320 
MET CB     C  N N 321 
MET CG     C  N N 322 
MET SD     S  N N 323 
MET CE     C  N N 324 
MET OXT    O  N N 325 
MET H      H  N N 326 
MET H2     H  N N 327 
MET HA     H  N N 328 
MET HB2    H  N N 329 
MET HB3    H  N N 330 
MET HG2    H  N N 331 
MET HG3    H  N N 332 
MET HE1    H  N N 333 
MET HE2    H  N N 334 
MET HE3    H  N N 335 
MET HXT    H  N N 336 
PHE N      N  N N 337 
PHE CA     C  N S 338 
PHE C      C  N N 339 
PHE O      O  N N 340 
PHE CB     C  N N 341 
PHE CG     C  Y N 342 
PHE CD1    C  Y N 343 
PHE CD2    C  Y N 344 
PHE CE1    C  Y N 345 
PHE CE2    C  Y N 346 
PHE CZ     C  Y N 347 
PHE OXT    O  N N 348 
PHE H      H  N N 349 
PHE H2     H  N N 350 
PHE HA     H  N N 351 
PHE HB2    H  N N 352 
PHE HB3    H  N N 353 
PHE HD1    H  N N 354 
PHE HD2    H  N N 355 
PHE HE1    H  N N 356 
PHE HE2    H  N N 357 
PHE HZ     H  N N 358 
PHE HXT    H  N N 359 
PRO N      N  N N 360 
PRO CA     C  N S 361 
PRO C      C  N N 362 
PRO O      O  N N 363 
PRO CB     C  N N 364 
PRO CG     C  N N 365 
PRO CD     C  N N 366 
PRO OXT    O  N N 367 
PRO H      H  N N 368 
PRO HA     H  N N 369 
PRO HB2    H  N N 370 
PRO HB3    H  N N 371 
PRO HG2    H  N N 372 
PRO HG3    H  N N 373 
PRO HD2    H  N N 374 
PRO HD3    H  N N 375 
PRO HXT    H  N N 376 
SER N      N  N N 377 
SER CA     C  N S 378 
SER C      C  N N 379 
SER O      O  N N 380 
SER CB     C  N N 381 
SER OG     O  N N 382 
SER OXT    O  N N 383 
SER H      H  N N 384 
SER H2     H  N N 385 
SER HA     H  N N 386 
SER HB2    H  N N 387 
SER HB3    H  N N 388 
SER HG     H  N N 389 
SER HXT    H  N N 390 
THR N      N  N N 391 
THR CA     C  N S 392 
THR C      C  N N 393 
THR O      O  N N 394 
THR CB     C  N R 395 
THR OG1    O  N N 396 
THR CG2    C  N N 397 
THR OXT    O  N N 398 
THR H      H  N N 399 
THR H2     H  N N 400 
THR HA     H  N N 401 
THR HB     H  N N 402 
THR HG1    H  N N 403 
THR HG21   H  N N 404 
THR HG22   H  N N 405 
THR HG23   H  N N 406 
THR HXT    H  N N 407 
TRP N      N  N N 408 
TRP CA     C  N S 409 
TRP C      C  N N 410 
TRP O      O  N N 411 
TRP CB     C  N N 412 
TRP CG     C  Y N 413 
TRP CD1    C  Y N 414 
TRP CD2    C  Y N 415 
TRP NE1    N  Y N 416 
TRP CE2    C  Y N 417 
TRP CE3    C  Y N 418 
TRP CZ2    C  Y N 419 
TRP CZ3    C  Y N 420 
TRP CH2    C  Y N 421 
TRP OXT    O  N N 422 
TRP H      H  N N 423 
TRP H2     H  N N 424 
TRP HA     H  N N 425 
TRP HB2    H  N N 426 
TRP HB3    H  N N 427 
TRP HD1    H  N N 428 
TRP HE1    H  N N 429 
TRP HE3    H  N N 430 
TRP HZ2    H  N N 431 
TRP HZ3    H  N N 432 
TRP HH2    H  N N 433 
TRP HXT    H  N N 434 
TYR N      N  N N 435 
TYR CA     C  N S 436 
TYR C      C  N N 437 
TYR O      O  N N 438 
TYR CB     C  N N 439 
TYR CG     C  Y N 440 
TYR CD1    C  Y N 441 
TYR CD2    C  Y N 442 
TYR CE1    C  Y N 443 
TYR CE2    C  Y N 444 
TYR CZ     C  Y N 445 
TYR OH     O  N N 446 
TYR OXT    O  N N 447 
TYR H      H  N N 448 
TYR H2     H  N N 449 
TYR HA     H  N N 450 
TYR HB2    H  N N 451 
TYR HB3    H  N N 452 
TYR HD1    H  N N 453 
TYR HD2    H  N N 454 
TYR HE1    H  N N 455 
TYR HE2    H  N N 456 
TYR HH     H  N N 457 
TYR HXT    H  N N 458 
VAL N      N  N N 459 
VAL CA     C  N S 460 
VAL C      C  N N 461 
VAL O      O  N N 462 
VAL CB     C  N N 463 
VAL CG1    C  N N 464 
VAL CG2    C  N N 465 
VAL OXT    O  N N 466 
VAL H      H  N N 467 
VAL H2     H  N N 468 
VAL HA     H  N N 469 
VAL HB     H  N N 470 
VAL HG11   H  N N 471 
VAL HG12   H  N N 472 
VAL HG13   H  N N 473 
VAL HG21   H  N N 474 
VAL HG22   H  N N 475 
VAL HG23   H  N N 476 
VAL HXT    H  N N 477 
# 
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  
FAD PA    O1A    doub N N 83  
FAD PA    O2A    sing N N 84  
FAD PA    O5B    sing N N 85  
FAD PA    O3P    sing N N 86  
FAD O2A   HOA2   sing N N 87  
FAD O5B   C5B    sing N N 88  
FAD C5B   C4B    sing N N 89  
FAD C5B   H51A   sing N N 90  
FAD C5B   H52A   sing N N 91  
FAD C4B   O4B    sing N N 92  
FAD C4B   C3B    sing N N 93  
FAD C4B   H4B    sing N N 94  
FAD O4B   C1B    sing N N 95  
FAD C3B   O3B    sing N N 96  
FAD C3B   C2B    sing N N 97  
FAD C3B   H3B    sing N N 98  
FAD O3B   HO3A   sing N N 99  
FAD C2B   O2B    sing N N 100 
FAD C2B   C1B    sing N N 101 
FAD C2B   H2B    sing N N 102 
FAD O2B   HO2A   sing N N 103 
FAD C1B   N9A    sing N N 104 
FAD C1B   H1B    sing N N 105 
FAD N9A   C8A    sing Y N 106 
FAD N9A   C4A    sing Y N 107 
FAD C8A   N7A    doub Y N 108 
FAD C8A   H8A    sing N N 109 
FAD N7A   C5A    sing Y N 110 
FAD C5A   C6A    sing Y N 111 
FAD C5A   C4A    doub Y N 112 
FAD C6A   N6A    sing N N 113 
FAD C6A   N1A    doub Y N 114 
FAD N6A   H61A   sing N N 115 
FAD N6A   H62A   sing N N 116 
FAD N1A   C2A    sing Y N 117 
FAD C2A   N3A    doub Y N 118 
FAD C2A   H2A    sing N N 119 
FAD N3A   C4A    sing Y N 120 
FAD N1    C2     sing N N 121 
FAD N1    C10    doub N N 122 
FAD C2    O2     doub N N 123 
FAD C2    N3     sing N N 124 
FAD N3    C4     sing N N 125 
FAD N3    HN3    sing N N 126 
FAD C4    O4     doub N N 127 
FAD C4    C4X    sing N N 128 
FAD C4X   N5     doub N N 129 
FAD C4X   C10    sing N N 130 
FAD N5    C5X    sing N N 131 
FAD C5X   C6     doub Y N 132 
FAD C5X   C9A    sing Y N 133 
FAD C6    C7     sing Y N 134 
FAD C6    H6     sing N N 135 
FAD C7    C7M    sing N N 136 
FAD C7    C8     doub Y N 137 
FAD C7M   HM71   sing N N 138 
FAD C7M   HM72   sing N N 139 
FAD C7M   HM73   sing N N 140 
FAD C8    C8M    sing N N 141 
FAD C8    C9     sing Y N 142 
FAD C8M   HM81   sing N N 143 
FAD C8M   HM82   sing N N 144 
FAD C8M   HM83   sing N N 145 
FAD C9    C9A    doub Y N 146 
FAD C9    H9     sing N N 147 
FAD C9A   N10    sing N N 148 
FAD N10   C10    sing N N 149 
FAD N10   "C1'"  sing N N 150 
FAD "C1'" "C2'"  sing N N 151 
FAD "C1'" "H1'1" sing N N 152 
FAD "C1'" "H1'2" sing N N 153 
FAD "C2'" "O2'"  sing N N 154 
FAD "C2'" "C3'"  sing N N 155 
FAD "C2'" "H2'"  sing N N 156 
FAD "O2'" "HO2'" sing N N 157 
FAD "C3'" "O3'"  sing N N 158 
FAD "C3'" "C4'"  sing N N 159 
FAD "C3'" "H3'"  sing N N 160 
FAD "O3'" "HO3'" sing N N 161 
FAD "C4'" "O4'"  sing N N 162 
FAD "C4'" "C5'"  sing N N 163 
FAD "C4'" "H4'"  sing N N 164 
FAD "O4'" "HO4'" sing N N 165 
FAD "C5'" "O5'"  sing N N 166 
FAD "C5'" "H5'1" sing N N 167 
FAD "C5'" "H5'2" sing N N 168 
FAD "O5'" P      sing N N 169 
FAD P     O1P    doub N N 170 
FAD P     O2P    sing N N 171 
FAD P     O3P    sing N N 172 
FAD O2P   HOP2   sing N N 173 
GLN N     CA     sing N N 174 
GLN N     H      sing N N 175 
GLN N     H2     sing N N 176 
GLN CA    C      sing N N 177 
GLN CA    CB     sing N N 178 
GLN CA    HA     sing N N 179 
GLN C     O      doub N N 180 
GLN C     OXT    sing N N 181 
GLN CB    CG     sing N N 182 
GLN CB    HB2    sing N N 183 
GLN CB    HB3    sing N N 184 
GLN CG    CD     sing N N 185 
GLN CG    HG2    sing N N 186 
GLN CG    HG3    sing N N 187 
GLN CD    OE1    doub N N 188 
GLN CD    NE2    sing N N 189 
GLN NE2   HE21   sing N N 190 
GLN NE2   HE22   sing N N 191 
GLN OXT   HXT    sing N N 192 
GLU N     CA     sing N N 193 
GLU N     H      sing N N 194 
GLU N     H2     sing N N 195 
GLU CA    C      sing N N 196 
GLU CA    CB     sing N N 197 
GLU CA    HA     sing N N 198 
GLU C     O      doub N N 199 
GLU C     OXT    sing N N 200 
GLU CB    CG     sing N N 201 
GLU CB    HB2    sing N N 202 
GLU CB    HB3    sing N N 203 
GLU CG    CD     sing N N 204 
GLU CG    HG2    sing N N 205 
GLU CG    HG3    sing N N 206 
GLU CD    OE1    doub N N 207 
GLU CD    OE2    sing N N 208 
GLU OE2   HE2    sing N N 209 
GLU OXT   HXT    sing N N 210 
GLY N     CA     sing N N 211 
GLY N     H      sing N N 212 
GLY N     H2     sing N N 213 
GLY CA    C      sing N N 214 
GLY CA    HA2    sing N N 215 
GLY CA    HA3    sing N N 216 
GLY C     O      doub N N 217 
GLY C     OXT    sing N N 218 
GLY OXT   HXT    sing N N 219 
HIS N     CA     sing N N 220 
HIS N     H      sing N N 221 
HIS N     H2     sing N N 222 
HIS CA    C      sing N N 223 
HIS CA    CB     sing N N 224 
HIS CA    HA     sing N N 225 
HIS C     O      doub N N 226 
HIS C     OXT    sing N N 227 
HIS CB    CG     sing N N 228 
HIS CB    HB2    sing N N 229 
HIS CB    HB3    sing N N 230 
HIS CG    ND1    sing Y N 231 
HIS CG    CD2    doub Y N 232 
HIS ND1   CE1    doub Y N 233 
HIS ND1   HD1    sing N N 234 
HIS CD2   NE2    sing Y N 235 
HIS CD2   HD2    sing N N 236 
HIS CE1   NE2    sing Y N 237 
HIS CE1   HE1    sing N N 238 
HIS NE2   HE2    sing N N 239 
HIS OXT   HXT    sing N N 240 
HOH O     H1     sing N N 241 
HOH O     H2     sing N N 242 
ILE N     CA     sing N N 243 
ILE N     H      sing N N 244 
ILE N     H2     sing N N 245 
ILE CA    C      sing N N 246 
ILE CA    CB     sing N N 247 
ILE CA    HA     sing N N 248 
ILE C     O      doub N N 249 
ILE C     OXT    sing N N 250 
ILE CB    CG1    sing N N 251 
ILE CB    CG2    sing N N 252 
ILE CB    HB     sing N N 253 
ILE CG1   CD1    sing N N 254 
ILE CG1   HG12   sing N N 255 
ILE CG1   HG13   sing N N 256 
ILE CG2   HG21   sing N N 257 
ILE CG2   HG22   sing N N 258 
ILE CG2   HG23   sing N N 259 
ILE CD1   HD11   sing N N 260 
ILE CD1   HD12   sing N N 261 
ILE CD1   HD13   sing N N 262 
ILE OXT   HXT    sing N N 263 
LEU N     CA     sing N N 264 
LEU N     H      sing N N 265 
LEU N     H2     sing N N 266 
LEU CA    C      sing N N 267 
LEU CA    CB     sing N N 268 
LEU CA    HA     sing N N 269 
LEU C     O      doub N N 270 
LEU C     OXT    sing N N 271 
LEU CB    CG     sing N N 272 
LEU CB    HB2    sing N N 273 
LEU CB    HB3    sing N N 274 
LEU CG    CD1    sing N N 275 
LEU CG    CD2    sing N N 276 
LEU CG    HG     sing N N 277 
LEU CD1   HD11   sing N N 278 
LEU CD1   HD12   sing N N 279 
LEU CD1   HD13   sing N N 280 
LEU CD2   HD21   sing N N 281 
LEU CD2   HD22   sing N N 282 
LEU CD2   HD23   sing N N 283 
LEU OXT   HXT    sing N N 284 
LYS N     CA     sing N N 285 
LYS N     H      sing N N 286 
LYS N     H2     sing N N 287 
LYS CA    C      sing N N 288 
LYS CA    CB     sing N N 289 
LYS CA    HA     sing N N 290 
LYS C     O      doub N N 291 
LYS C     OXT    sing N N 292 
LYS CB    CG     sing N N 293 
LYS CB    HB2    sing N N 294 
LYS CB    HB3    sing N N 295 
LYS CG    CD     sing N N 296 
LYS CG    HG2    sing N N 297 
LYS CG    HG3    sing N N 298 
LYS CD    CE     sing N N 299 
LYS CD    HD2    sing N N 300 
LYS CD    HD3    sing N N 301 
LYS CE    NZ     sing N N 302 
LYS CE    HE2    sing N N 303 
LYS CE    HE3    sing N N 304 
LYS NZ    HZ1    sing N N 305 
LYS NZ    HZ2    sing N N 306 
LYS NZ    HZ3    sing N N 307 
LYS OXT   HXT    sing N N 308 
MET N     CA     sing N N 309 
MET N     H      sing N N 310 
MET N     H2     sing N N 311 
MET CA    C      sing N N 312 
MET CA    CB     sing N N 313 
MET CA    HA     sing N N 314 
MET C     O      doub N N 315 
MET C     OXT    sing N N 316 
MET CB    CG     sing N N 317 
MET CB    HB2    sing N N 318 
MET CB    HB3    sing N N 319 
MET CG    SD     sing N N 320 
MET CG    HG2    sing N N 321 
MET CG    HG3    sing N N 322 
MET SD    CE     sing N N 323 
MET CE    HE1    sing N N 324 
MET CE    HE2    sing N N 325 
MET CE    HE3    sing N N 326 
MET OXT   HXT    sing N N 327 
PHE N     CA     sing N N 328 
PHE N     H      sing N N 329 
PHE N     H2     sing N N 330 
PHE CA    C      sing N N 331 
PHE CA    CB     sing N N 332 
PHE CA    HA     sing N N 333 
PHE C     O      doub N N 334 
PHE C     OXT    sing N N 335 
PHE CB    CG     sing N N 336 
PHE CB    HB2    sing N N 337 
PHE CB    HB3    sing N N 338 
PHE CG    CD1    doub Y N 339 
PHE CG    CD2    sing Y N 340 
PHE CD1   CE1    sing Y N 341 
PHE CD1   HD1    sing N N 342 
PHE CD2   CE2    doub Y N 343 
PHE CD2   HD2    sing N N 344 
PHE CE1   CZ     doub Y N 345 
PHE CE1   HE1    sing N N 346 
PHE CE2   CZ     sing Y N 347 
PHE CE2   HE2    sing N N 348 
PHE CZ    HZ     sing N N 349 
PHE OXT   HXT    sing N N 350 
PRO N     CA     sing N N 351 
PRO N     CD     sing N N 352 
PRO N     H      sing N N 353 
PRO CA    C      sing N N 354 
PRO CA    CB     sing N N 355 
PRO CA    HA     sing N N 356 
PRO C     O      doub N N 357 
PRO C     OXT    sing N N 358 
PRO CB    CG     sing N N 359 
PRO CB    HB2    sing N N 360 
PRO CB    HB3    sing N N 361 
PRO CG    CD     sing N N 362 
PRO CG    HG2    sing N N 363 
PRO CG    HG3    sing N N 364 
PRO CD    HD2    sing N N 365 
PRO CD    HD3    sing N N 366 
PRO OXT   HXT    sing N N 367 
SER N     CA     sing N N 368 
SER N     H      sing N N 369 
SER N     H2     sing N N 370 
SER CA    C      sing N N 371 
SER CA    CB     sing N N 372 
SER CA    HA     sing N N 373 
SER C     O      doub N N 374 
SER C     OXT    sing N N 375 
SER CB    OG     sing N N 376 
SER CB    HB2    sing N N 377 
SER CB    HB3    sing N N 378 
SER OG    HG     sing N N 379 
SER OXT   HXT    sing N N 380 
THR N     CA     sing N N 381 
THR N     H      sing N N 382 
THR N     H2     sing N N 383 
THR CA    C      sing N N 384 
THR CA    CB     sing N N 385 
THR CA    HA     sing N N 386 
THR C     O      doub N N 387 
THR C     OXT    sing N N 388 
THR CB    OG1    sing N N 389 
THR CB    CG2    sing N N 390 
THR CB    HB     sing N N 391 
THR OG1   HG1    sing N N 392 
THR CG2   HG21   sing N N 393 
THR CG2   HG22   sing N N 394 
THR CG2   HG23   sing N N 395 
THR OXT   HXT    sing N N 396 
TRP N     CA     sing N N 397 
TRP N     H      sing N N 398 
TRP N     H2     sing N N 399 
TRP CA    C      sing N N 400 
TRP CA    CB     sing N N 401 
TRP CA    HA     sing N N 402 
TRP C     O      doub N N 403 
TRP C     OXT    sing N N 404 
TRP CB    CG     sing N N 405 
TRP CB    HB2    sing N N 406 
TRP CB    HB3    sing N N 407 
TRP CG    CD1    doub Y N 408 
TRP CG    CD2    sing Y N 409 
TRP CD1   NE1    sing Y N 410 
TRP CD1   HD1    sing N N 411 
TRP CD2   CE2    doub Y N 412 
TRP CD2   CE3    sing Y N 413 
TRP NE1   CE2    sing Y N 414 
TRP NE1   HE1    sing N N 415 
TRP CE2   CZ2    sing Y N 416 
TRP CE3   CZ3    doub Y N 417 
TRP CE3   HE3    sing N N 418 
TRP CZ2   CH2    doub Y N 419 
TRP CZ2   HZ2    sing N N 420 
TRP CZ3   CH2    sing Y N 421 
TRP CZ3   HZ3    sing N N 422 
TRP CH2   HH2    sing N N 423 
TRP OXT   HXT    sing N N 424 
TYR N     CA     sing N N 425 
TYR N     H      sing N N 426 
TYR N     H2     sing N N 427 
TYR CA    C      sing N N 428 
TYR CA    CB     sing N N 429 
TYR CA    HA     sing N N 430 
TYR C     O      doub N N 431 
TYR C     OXT    sing N N 432 
TYR CB    CG     sing N N 433 
TYR CB    HB2    sing N N 434 
TYR CB    HB3    sing N N 435 
TYR CG    CD1    doub Y N 436 
TYR CG    CD2    sing Y N 437 
TYR CD1   CE1    sing Y N 438 
TYR CD1   HD1    sing N N 439 
TYR CD2   CE2    doub Y N 440 
TYR CD2   HD2    sing N N 441 
TYR CE1   CZ     doub Y N 442 
TYR CE1   HE1    sing N N 443 
TYR CE2   CZ     sing Y N 444 
TYR CE2   HE2    sing N N 445 
TYR CZ    OH     sing N N 446 
TYR OH    HH     sing N N 447 
TYR OXT   HXT    sing N N 448 
VAL N     CA     sing N N 449 
VAL N     H      sing N N 450 
VAL N     H2     sing N N 451 
VAL CA    C      sing N N 452 
VAL CA    CB     sing N N 453 
VAL CA    HA     sing N N 454 
VAL C     O      doub N N 455 
VAL C     OXT    sing N N 456 
VAL CB    CG1    sing N N 457 
VAL CB    CG2    sing N N 458 
VAL CB    HB     sing N N 459 
VAL CG1   HG11   sing N N 460 
VAL CG1   HG12   sing N N 461 
VAL CG1   HG13   sing N N 462 
VAL CG2   HG21   sing N N 463 
VAL CG2   HG22   sing N N 464 
VAL CG2   HG23   sing N N 465 
VAL OXT   HXT    sing N N 466 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4yut 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9F1Y 
_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]   0.009873 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.018707 
_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]   0.013920 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CA 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . GLY A 1 28  ? 11.671  26.246  41.306  1.00 64.17  ? 0   GLY A N     1 
ATOM   2    C  CA    . GLY A 1 28  ? 10.477  25.445  41.555  1.00 66.90  ? 0   GLY A CA    1 
ATOM   3    C  C     . GLY A 1 28  ? 10.847  24.103  42.175  1.00 58.95  ? 0   GLY A C     1 
ATOM   4    O  O     . GLY A 1 28  ? 11.911  23.544  41.874  1.00 54.52  ? 0   GLY A O     1 
ATOM   5    N  N     . MET A 1 29  ? 9.963   23.590  43.032  1.00 56.56  ? 1   MET A N     1 
ATOM   6    C  CA    . MET A 1 29  ? 10.138  22.259  43.596  1.00 53.39  ? 1   MET A CA    1 
ATOM   7    C  C     . MET A 1 29  ? 9.626   21.188  42.648  1.00 48.46  ? 1   MET A C     1 
ATOM   8    O  O     . MET A 1 29  ? 8.623   21.370  41.949  1.00 54.09  ? 1   MET A O     1 
ATOM   9    C  CB    . MET A 1 29  ? 9.427   22.128  44.941  1.00 58.63  ? 1   MET A CB    1 
ATOM   10   C  CG    . MET A 1 29  ? 10.222  22.688  46.111  1.00 58.64  ? 1   MET A CG    1 
ATOM   11   S  SD    . MET A 1 29  ? 9.862   21.803  47.641  1.00 59.47  ? 1   MET A SD    1 
ATOM   12   C  CE    . MET A 1 29  ? 9.862   23.171  48.805  1.00 60.84  ? 1   MET A CE    1 
ATOM   13   N  N     . LYS A 1 30  ? 10.324  20.062  42.647  1.00 40.61  ? 2   LYS A N     1 
ATOM   14   C  CA    . LYS A 1 30  ? 10.031  18.912  41.811  1.00 41.73  ? 2   LYS A CA    1 
ATOM   15   C  C     . LYS A 1 30  ? 9.845   17.682  42.694  1.00 47.89  ? 2   LYS A C     1 
ATOM   16   O  O     . LYS A 1 30  ? 10.498  17.549  43.738  1.00 39.07  ? 2   LYS A O     1 
ATOM   17   C  CB    . LYS A 1 30  ? 11.171  18.683  40.812  1.00 43.48  ? 2   LYS A CB    1 
ATOM   18   C  CG    . LYS A 1 30  ? 10.907  17.621  39.775  1.00 51.62  ? 2   LYS A CG    1 
ATOM   19   C  CD    . LYS A 1 30  ? 12.106  17.479  38.858  1.00 54.24  ? 2   LYS A CD    1 
ATOM   20   C  CE    . LYS A 1 30  ? 11.682  17.109  37.437  1.00 62.50  ? 2   LYS A CE    1 
ATOM   21   N  NZ    . LYS A 1 30  ? 12.855  16.702  36.607  1.00 60.39  ? 2   LYS A NZ    1 
ATOM   22   N  N     . ARG A 1 31  ? 8.950   16.779  42.281  1.00 45.26  ? 3   ARG A N     1 
ATOM   23   C  CA    . ARG A 1 31  ? 8.759   15.514  42.989  1.00 40.67  ? 3   ARG A CA    1 
ATOM   24   C  C     . ARG A 1 31  ? 8.645   14.375  41.987  1.00 39.52  ? 3   ARG A C     1 
ATOM   25   O  O     . ARG A 1 31  ? 7.760   14.389  41.126  1.00 47.57  ? 3   ARG A O     1 
ATOM   26   C  CB    . ARG A 1 31  ? 7.530   15.561  43.899  1.00 38.24  ? 3   ARG A CB    1 
ATOM   27   C  CG    . ARG A 1 31  ? 7.260   14.239  44.606  1.00 39.54  ? 3   ARG A CG    1 
ATOM   28   C  CD    . ARG A 1 31  ? 6.317   14.377  45.802  1.00 44.34  ? 3   ARG A CD    1 
ATOM   29   N  NE    . ARG A 1 31  ? 5.077   15.053  45.448  1.00 37.23  ? 3   ARG A NE    1 
ATOM   30   C  CZ    . ARG A 1 31  ? 4.666   16.191  45.984  1.00 43.06  ? 3   ARG A CZ    1 
ATOM   31   N  NH1   . ARG A 1 31  ? 5.320   16.763  46.979  1.00 46.71  ? 3   ARG A NH1   1 
ATOM   32   N  NH2   . ARG A 1 31  ? 3.557   16.758  45.524  1.00 43.39  ? 3   ARG A NH2   1 
ATOM   33   N  N     . LEU A 1 32  ? 9.529   13.389  42.104  1.00 38.05  ? 4   LEU A N     1 
ATOM   34   C  CA    . LEU A 1 32  ? 9.566   12.232  41.220  1.00 36.01  ? 4   LEU A CA    1 
ATOM   35   C  C     . LEU A 1 32  ? 9.152   10.982  41.982  1.00 33.93  ? 4   LEU A C     1 
ATOM   36   O  O     . LEU A 1 32  ? 9.527   10.806  43.143  1.00 38.20  ? 4   LEU A O     1 
ATOM   37   C  CB    . LEU A 1 32  ? 10.976  12.003  40.659  1.00 40.61  ? 4   LEU A CB    1 
ATOM   38   C  CG    . LEU A 1 32  ? 11.724  13.056  39.844  1.00 49.59  ? 4   LEU A CG    1 
ATOM   39   C  CD1   . LEU A 1 32  ? 13.111  12.524  39.485  1.00 40.17  ? 4   LEU A CD1   1 
ATOM   40   C  CD2   . LEU A 1 32  ? 10.948  13.403  38.589  1.00 52.67  ? 4   LEU A CD2   1 
ATOM   41   N  N     . THR A 1 33  ? 8.424   10.095  41.318  1.00 34.88  ? 5   THR A N     1 
ATOM   42   C  CA    . THR A 1 33  ? 8.082   8.788   41.853  1.00 32.04  ? 5   THR A CA    1 
ATOM   43   C  C     . THR A 1 33  ? 8.535   7.744   40.854  1.00 35.55  ? 5   THR A C     1 
ATOM   44   O  O     . THR A 1 33  ? 8.205   7.845   39.667  1.00 39.47  ? 5   THR A O     1 
ATOM   45   C  CB    . THR A 1 33  ? 6.575   8.613   42.076  1.00 31.92  ? 5   THR A CB    1 
ATOM   46   O  OG1   . THR A 1 33  ? 6.091   9.601   42.978  1.00 34.17  ? 5   THR A OG1   1 
ATOM   47   C  CG2   . THR A 1 33  ? 6.304   7.257   42.652  1.00 30.02  ? 5   THR A CG2   1 
ATOM   48   N  N     . TYR A 1 34  ? 9.242   6.722   41.327  1.00 25.59  ? 6   TYR A N     1 
ATOM   49   C  CA    . TYR A 1 34  ? 9.722   5.694   40.423  1.00 33.91  ? 6   TYR A CA    1 
ATOM   50   C  C     . TYR A 1 34  ? 9.663   4.330   41.095  1.00 30.95  ? 6   TYR A C     1 
ATOM   51   O  O     . TYR A 1 34  ? 9.580   4.206   42.322  1.00 32.63  ? 6   TYR A O     1 
ATOM   52   C  CB    . TYR A 1 34  ? 11.149  6.005   39.907  1.00 37.64  ? 6   TYR A CB    1 
ATOM   53   C  CG    . TYR A 1 34  ? 12.255  5.745   40.920  1.00 34.62  ? 6   TYR A CG    1 
ATOM   54   C  CD1   . TYR A 1 34  ? 12.802  4.475   41.078  1.00 32.05  ? 6   TYR A CD1   1 
ATOM   55   C  CD2   . TYR A 1 34  ? 12.761  6.775   41.701  1.00 36.84  ? 6   TYR A CD2   1 
ATOM   56   C  CE1   . TYR A 1 34  ? 13.791  4.226   42.007  1.00 29.42  ? 6   TYR A CE1   1 
ATOM   57   C  CE2   . TYR A 1 34  ? 13.770  6.541   42.628  1.00 37.13  ? 6   TYR A CE2   1 
ATOM   58   C  CZ    . TYR A 1 34  ? 14.276  5.259   42.772  1.00 34.45  ? 6   TYR A CZ    1 
ATOM   59   O  OH    . TYR A 1 34  ? 15.259  5.003   43.703  1.00 33.52  ? 6   TYR A OH    1 
ATOM   60   N  N     . ILE A 1 35  ? 9.696   3.298   40.255  1.00 30.39  ? 7   ILE A N     1 
ATOM   61   C  CA    . ILE A 1 35  ? 9.810   1.919   40.696  1.00 32.71  ? 7   ILE A CA    1 
ATOM   62   C  C     . ILE A 1 35  ? 10.967  1.287   39.950  1.00 35.80  ? 7   ILE A C     1 
ATOM   63   O  O     . ILE A 1 35  ? 11.317  1.697   38.838  1.00 35.87  ? 7   ILE A O     1 
ATOM   64   C  CB    . ILE A 1 35  ? 8.514   1.112   40.481  1.00 31.98  ? 7   ILE A CB    1 
ATOM   65   C  CG1   . ILE A 1 35  ? 8.097   1.101   39.007  1.00 33.29  ? 7   ILE A CG1   1 
ATOM   66   C  CG2   . ILE A 1 35  ? 7.405   1.704   41.304  1.00 34.30  ? 7   ILE A CG2   1 
ATOM   67   C  CD1   . ILE A 1 35  ? 6.976   0.117   38.744  1.00 35.84  ? 7   ILE A CD1   1 
ATOM   68   N  N     . SER A 1 36  ? 11.570  0.287   40.578  1.00 31.72  ? 8   SER A N     1 
ATOM   69   C  CA    . SER A 1 36  ? 12.712  -0.387  39.997  1.00 39.46  ? 8   SER A CA    1 
ATOM   70   C  C     . SER A 1 36  ? 12.756  -1.791  40.563  1.00 41.83  ? 8   SER A C     1 
ATOM   71   O  O     . SER A 1 36  ? 11.974  -2.150  41.451  1.00 31.58  ? 8   SER A O     1 
ATOM   72   C  CB    . SER A 1 36  ? 14.016  0.371   40.283  1.00 42.96  ? 8   SER A CB    1 
ATOM   73   O  OG    . SER A 1 36  ? 14.395  0.216   41.647  1.00 38.39  ? 8   SER A OG    1 
ATOM   74   N  N     . LYS A 1 37  ? 13.716  -2.566  40.074  1.00 34.81  ? 9   LYS A N     1 
ATOM   75   C  CA    . LYS A 1 37  ? 13.865  -3.972  40.407  1.00 38.94  ? 9   LYS A CA    1 
ATOM   76   C  C     . LYS A 1 37  ? 15.274  -4.195  40.923  1.00 46.45  ? 9   LYS A C     1 
ATOM   77   O  O     . LYS A 1 37  ? 16.219  -3.576  40.428  1.00 47.19  ? 9   LYS A O     1 
ATOM   78   C  CB    . LYS A 1 37  ? 13.588  -4.844  39.164  1.00 47.25  ? 9   LYS A CB    1 
ATOM   79   C  CG    . LYS A 1 37  ? 13.609  -6.348  39.405  1.00 50.79  ? 9   LYS A CG    1 
ATOM   80   C  CD    . LYS A 1 37  ? 12.831  -7.114  38.321  1.00 60.73  ? 9   LYS A CD    1 
ATOM   81   C  CE    . LYS A 1 37  ? 13.127  -6.575  36.925  1.00 63.59  ? 9   LYS A CE    1 
ATOM   82   N  NZ    . LYS A 1 37  ? 13.150  -7.623  35.851  1.00 65.77  ? 9   LYS A NZ    1 
ATOM   83   N  N     . PHE A 1 38  ? 15.413  -5.049  41.940  1.00 42.82  ? 10  PHE A N     1 
ATOM   84   C  CA    . PHE A 1 38  ? 16.743  -5.448  42.383  1.00 37.70  ? 10  PHE A CA    1 
ATOM   85   C  C     . PHE A 1 38  ? 17.449  -6.154  41.229  1.00 48.54  ? 10  PHE A C     1 
ATOM   86   O  O     . PHE A 1 38  ? 16.921  -7.115  40.655  1.00 43.32  ? 10  PHE A O     1 
ATOM   87   C  CB    . PHE A 1 38  ? 16.672  -6.396  43.587  1.00 42.42  ? 10  PHE A CB    1 
ATOM   88   C  CG    . PHE A 1 38  ? 16.137  -5.778  44.876  1.00 39.83  ? 10  PHE A CG    1 
ATOM   89   C  CD1   . PHE A 1 38  ? 15.395  -4.610  44.885  1.00 36.96  ? 10  PHE A CD1   1 
ATOM   90   C  CD2   . PHE A 1 38  ? 16.364  -6.418  46.085  1.00 40.34  ? 10  PHE A CD2   1 
ATOM   91   C  CE1   . PHE A 1 38  ? 14.896  -4.087  46.083  1.00 40.77  ? 10  PHE A CE1   1 
ATOM   92   C  CE2   . PHE A 1 38  ? 15.875  -5.899  47.281  1.00 42.22  ? 10  PHE A CE2   1 
ATOM   93   C  CZ    . PHE A 1 38  ? 15.147  -4.732  47.276  1.00 37.15  ? 10  PHE A CZ    1 
ATOM   94   N  N     . SER A 1 39  ? 18.633  -5.672  40.869  1.00 51.19  ? 11  SER A N     1 
ATOM   95   C  CA    . SER A 1 39  ? 19.424  -6.360  39.858  1.00 50.11  ? 11  SER A CA    1 
ATOM   96   C  C     . SER A 1 39  ? 20.303  -7.456  40.456  1.00 49.55  ? 11  SER A C     1 
ATOM   97   O  O     . SER A 1 39  ? 21.081  -8.080  39.729  1.00 64.62  ? 11  SER A O     1 
ATOM   98   C  CB    . SER A 1 39  ? 20.256  -5.343  39.068  1.00 55.23  ? 11  SER A CB    1 
ATOM   99   O  OG    . SER A 1 39  ? 21.131  -4.625  39.908  1.00 47.37  ? 11  SER A OG    1 
ATOM   100  N  N     . ARG A 1 40  ? 20.177  -7.704  41.754  1.00 43.85  ? 12  ARG A N     1 
ATOM   101  C  CA    . ARG A 1 40  ? 20.829  -8.789  42.477  1.00 46.56  ? 12  ARG A CA    1 
ATOM   102  C  C     . ARG A 1 40  ? 20.234  -8.825  43.885  1.00 47.53  ? 12  ARG A C     1 
ATOM   103  O  O     . ARG A 1 40  ? 19.674  -7.829  44.336  1.00 43.99  ? 12  ARG A O     1 
ATOM   104  C  CB    . ARG A 1 40  ? 22.350  -8.582  42.545  1.00 51.90  ? 12  ARG A CB    1 
ATOM   105  C  CG    . ARG A 1 40  ? 22.767  -7.259  43.187  1.00 58.83  ? 12  ARG A CG    1 
ATOM   106  C  CD    . ARG A 1 40  ? 24.157  -7.355  43.830  1.00 65.53  ? 12  ARG A CD    1 
ATOM   107  N  NE    . ARG A 1 40  ? 24.650  -6.062  44.296  1.00 57.67  ? 12  ARG A NE    1 
ATOM   108  C  CZ    . ARG A 1 40  ? 24.977  -5.783  45.552  1.00 67.80  ? 12  ARG A CZ    1 
ATOM   109  N  NH1   . ARG A 1 40  ? 24.855  -6.683  46.518  1.00 70.66  ? 12  ARG A NH1   1 
ATOM   110  N  NH2   . ARG A 1 40  ? 25.445  -4.570  45.847  1.00 58.69  ? 12  ARG A NH2   1 
ATOM   111  N  N     . PRO A 1 41  ? 20.330  -9.955  44.584  1.00 51.85  ? 13  PRO A N     1 
ATOM   112  C  CA    . PRO A 1 41  ? 19.748  -10.027 45.936  1.00 54.58  ? 13  PRO A CA    1 
ATOM   113  C  C     . PRO A 1 41  ? 20.375  -9.012  46.887  1.00 56.86  ? 13  PRO A C     1 
ATOM   114  O  O     . PRO A 1 41  ? 21.592  -8.812  46.898  1.00 51.17  ? 13  PRO A O     1 
ATOM   115  C  CB    . PRO A 1 41  ? 20.047  -11.462 46.391  1.00 51.19  ? 13  PRO A CB    1 
ATOM   116  C  CG    . PRO A 1 41  ? 20.610  -12.178 45.221  1.00 56.13  ? 13  PRO A CG    1 
ATOM   117  C  CD    . PRO A 1 41  ? 20.633  -11.281 44.027  1.00 53.30  ? 13  PRO A CD    1 
ATOM   118  N  N     . LEU A 1 42  ? 19.527  -8.374  47.697  1.00 49.60  ? 14  LEU A N     1 
ATOM   119  C  CA    . LEU A 1 42  ? 19.954  -7.399  48.695  1.00 43.79  ? 14  LEU A CA    1 
ATOM   120  C  C     . LEU A 1 42  ? 19.327  -7.753  50.034  1.00 51.74  ? 14  LEU A C     1 
ATOM   121  O  O     . LEU A 1 42  ? 18.123  -8.022  50.110  1.00 49.16  ? 14  LEU A O     1 
ATOM   122  C  CB    . LEU A 1 42  ? 19.564  -5.972  48.301  1.00 38.01  ? 14  LEU A CB    1 
ATOM   123  C  CG    . LEU A 1 42  ? 20.046  -5.414  46.969  1.00 48.20  ? 14  LEU A CG    1 
ATOM   124  C  CD1   . LEU A 1 42  ? 19.389  -4.082  46.668  1.00 39.03  ? 14  LEU A CD1   1 
ATOM   125  C  CD2   . LEU A 1 42  ? 21.560  -5.266  46.990  1.00 49.29  ? 14  LEU A CD2   1 
ATOM   126  N  N     . SER A 1 43  ? 20.138  -7.749  51.085  1.00 44.44  ? 15  SER A N     1 
ATOM   127  C  CA    . SER A 1 43  ? 19.655  -8.058  52.419  1.00 43.33  ? 15  SER A CA    1 
ATOM   128  C  C     . SER A 1 43  ? 18.925  -6.859  53.015  1.00 42.25  ? 15  SER A C     1 
ATOM   129  O  O     . SER A 1 43  ? 18.999  -5.732  52.507  1.00 38.87  ? 15  SER A O     1 
ATOM   130  C  CB    . SER A 1 43  ? 20.816  -8.438  53.327  1.00 47.53  ? 15  SER A CB    1 
ATOM   131  O  OG    . SER A 1 43  ? 21.678  -7.323  53.470  1.00 41.63  ? 15  SER A OG    1 
ATOM   132  N  N     . GLY A 1 44  ? 18.237  -7.109  54.131  1.00 46.83  ? 16  GLY A N     1 
ATOM   133  C  CA    . GLY A 1 44  ? 17.577  -6.024  54.839  1.00 46.80  ? 16  GLY A CA    1 
ATOM   134  C  C     . GLY A 1 44  ? 18.566  -5.015  55.397  1.00 45.61  ? 16  GLY A C     1 
ATOM   135  O  O     . GLY A 1 44  ? 18.328  -3.804  55.337  1.00 38.18  ? 16  GLY A O     1 
ATOM   136  N  N     . ASP A 1 45  ? 19.688  -5.500  55.945  1.00 43.84  ? 17  ASP A N     1 
ATOM   137  C  CA    . ASP A 1 45  ? 20.741  -4.600  56.402  1.00 45.34  ? 17  ASP A CA    1 
ATOM   138  C  C     . ASP A 1 45  ? 21.283  -3.754  55.254  1.00 42.85  ? 17  ASP A C     1 
ATOM   139  O  O     . ASP A 1 45  ? 21.550  -2.558  55.424  1.00 44.37  ? 17  ASP A O     1 
ATOM   140  C  CB    . ASP A 1 45  ? 21.865  -5.401  57.060  1.00 50.21  ? 17  ASP A CB    1 
ATOM   141  C  CG    . ASP A 1 45  ? 21.570  -5.732  58.511  1.00 54.36  ? 17  ASP A CG    1 
ATOM   142  O  OD1   . ASP A 1 45  ? 20.595  -5.175  59.058  1.00 57.49  ? 17  ASP A OD1   1 
ATOM   143  O  OD2   . ASP A 1 45  ? 22.308  -6.542  59.108  1.00 57.94  ? 17  ASP A OD2   1 
ATOM   144  N  N     . GLU A 1 46  ? 21.440  -4.350  54.074  1.00 40.43  ? 18  GLU A N     1 
ATOM   145  C  CA    . GLU A 1 46  ? 21.949  -3.591  52.934  1.00 44.26  ? 18  GLU A CA    1 
ATOM   146  C  C     . GLU A 1 46  ? 20.943  -2.555  52.456  1.00 37.96  ? 18  GLU A C     1 
ATOM   147  O  O     . GLU A 1 46  ? 21.329  -1.453  52.046  1.00 36.50  ? 18  GLU A O     1 
ATOM   148  C  CB    . GLU A 1 46  ? 22.343  -4.544  51.803  1.00 45.16  ? 18  GLU A CB    1 
ATOM   149  C  CG    . GLU A 1 46  ? 23.730  -5.194  52.027  1.00 50.15  ? 18  GLU A CG    1 
ATOM   150  C  CD    . GLU A 1 46  ? 24.086  -6.219  50.965  1.00 61.32  ? 18  GLU A CD    1 
ATOM   151  O  OE1   . GLU A 1 46  ? 23.150  -6.843  50.413  1.00 56.82  ? 18  GLU A OE1   1 
ATOM   152  O  OE2   . GLU A 1 46  ? 25.294  -6.407  50.687  1.00 70.61  ? 18  GLU A OE2   1 
ATOM   153  N  N     . ILE A 1 47  ? 19.650  -2.886  52.496  1.00 40.00  ? 19  ILE A N     1 
ATOM   154  C  CA    . ILE A 1 47  ? 18.619  -1.909  52.146  1.00 33.49  ? 19  ILE A CA    1 
ATOM   155  C  C     . ILE A 1 47  ? 18.598  -0.778  53.170  1.00 35.51  ? 19  ILE A C     1 
ATOM   156  O  O     . ILE A 1 47  ? 18.467  0.403   52.820  1.00 33.77  ? 19  ILE A O     1 
ATOM   157  C  CB    . ILE A 1 47  ? 17.256  -2.621  52.032  1.00 33.34  ? 19  ILE A CB    1 
ATOM   158  C  CG1   . ILE A 1 47  ? 17.286  -3.601  50.842  1.00 35.82  ? 19  ILE A CG1   1 
ATOM   159  C  CG2   . ILE A 1 47  ? 16.101  -1.591  51.933  1.00 27.15  ? 19  ILE A CG2   1 
ATOM   160  C  CD1   . ILE A 1 47  ? 16.252  -4.708  50.918  1.00 44.79  ? 19  ILE A CD1   1 
ATOM   161  N  N     . GLU A 1 48  ? 18.743  -1.131  54.447  1.00 32.18  ? 20  GLU A N     1 
ATOM   162  C  CA    . GLU A 1 48  ? 18.738  -0.166  55.536  1.00 34.41  ? 20  GLU A CA    1 
ATOM   163  C  C     . GLU A 1 48  ? 19.871  0.839   55.397  1.00 37.78  ? 20  GLU A C     1 
ATOM   164  O  O     . GLU A 1 48  ? 19.686  2.036   55.656  1.00 33.75  ? 20  GLU A O     1 
ATOM   165  C  CB    . GLU A 1 48  ? 18.853  -0.929  56.855  1.00 36.33  ? 20  GLU A CB    1 
ATOM   166  C  CG    . GLU A 1 48  ? 18.813  -0.087  58.106  1.00 44.11  ? 20  GLU A CG    1 
ATOM   167  C  CD    . GLU A 1 48  ? 18.822  -0.947  59.363  1.00 56.50  ? 20  GLU A CD    1 
ATOM   168  O  OE1   . GLU A 1 48  ? 19.796  -1.717  59.552  1.00 62.22  ? 20  GLU A OE1   1 
ATOM   169  O  OE2   . GLU A 1 48  ? 17.850  -0.860  60.156  1.00 65.45  ? 20  GLU A OE2   1 
ATOM   170  N  N     . ALA A 1 49  ? 21.058  0.368   55.006  1.00 34.04  ? 21  ALA A N     1 
ATOM   171  C  CA    . ALA A 1 49  ? 22.184  1.272   54.829  1.00 36.94  ? 21  ALA A CA    1 
ATOM   172  C  C     . ALA A 1 49  ? 21.937  2.238   53.682  1.00 33.50  ? 21  ALA A C     1 
ATOM   173  O  O     . ALA A 1 49  ? 22.224  3.436   53.803  1.00 35.80  ? 21  ALA A O     1 
ATOM   174  C  CB    . ALA A 1 49  ? 23.465  0.473   54.599  1.00 44.16  ? 21  ALA A CB    1 
ATOM   175  N  N     . ILE A 1 50  ? 21.413  1.737   52.559  1.00 30.90  ? 22  ILE A N     1 
ATOM   176  C  CA    . ILE A 1 50  ? 21.062  2.622   51.452  1.00 33.12  ? 22  ILE A CA    1 
ATOM   177  C  C     . ILE A 1 50  ? 20.162  3.738   51.950  1.00 32.18  ? 22  ILE A C     1 
ATOM   178  O  O     . ILE A 1 50  ? 20.384  4.922   51.666  1.00 33.34  ? 22  ILE A O     1 
ATOM   179  C  CB    . ILE A 1 50  ? 20.396  1.830   50.312  1.00 36.30  ? 22  ILE A CB    1 
ATOM   180  C  CG1   . ILE A 1 50  ? 21.426  0.946   49.599  1.00 37.88  ? 22  ILE A CG1   1 
ATOM   181  C  CG2   . ILE A 1 50  ? 19.708  2.765   49.315  1.00 33.12  ? 22  ILE A CG2   1 
ATOM   182  C  CD1   . ILE A 1 50  ? 20.823  0.118   48.490  1.00 36.24  ? 22  ILE A CD1   1 
ATOM   183  N  N     . GLY A 1 51  ? 19.151  3.375   52.735  1.00 36.08  ? 23  GLY A N     1 
ATOM   184  C  CA    . GLY A 1 51  ? 18.238  4.377   53.251  1.00 34.14  ? 23  GLY A CA    1 
ATOM   185  C  C     . GLY A 1 51  ? 18.932  5.389   54.141  1.00 34.61  ? 23  GLY A C     1 
ATOM   186  O  O     . GLY A 1 51  ? 18.703  6.597   54.023  1.00 34.92  ? 23  GLY A O     1 
ATOM   187  N  N     A ARG A 1 52  ? 19.797  4.911   55.042  0.58 33.09  ? 24  ARG A N     1 
ATOM   188  N  N     B ARG A 1 52  ? 19.804  4.907   55.035  0.42 33.13  ? 24  ARG A N     1 
ATOM   189  C  CA    A ARG A 1 52  ? 20.457  5.814   55.984  0.58 32.59  ? 24  ARG A CA    1 
ATOM   190  C  CA    B ARG A 1 52  ? 20.455  5.795   55.995  0.42 32.62  ? 24  ARG A CA    1 
ATOM   191  C  C     A ARG A 1 52  ? 21.456  6.716   55.273  0.58 32.10  ? 24  ARG A C     1 
ATOM   192  C  C     B ARG A 1 52  ? 21.482  6.694   55.310  0.42 32.10  ? 24  ARG A C     1 
ATOM   193  O  O     A ARG A 1 52  ? 21.567  7.906   55.592  0.58 30.23  ? 24  ARG A O     1 
ATOM   194  O  O     B ARG A 1 52  ? 21.631  7.866   55.675  0.42 30.27  ? 24  ARG A O     1 
ATOM   195  C  CB    A ARG A 1 52  ? 21.164  5.024   57.087  0.58 35.62  ? 24  ARG A CB    1 
ATOM   196  C  CB    B ARG A 1 52  ? 21.115  4.974   57.111  0.42 35.62  ? 24  ARG A CB    1 
ATOM   197  C  CG    A ARG A 1 52  ? 20.246  4.518   58.194  0.58 35.92  ? 24  ARG A CG    1 
ATOM   198  C  CG    B ARG A 1 52  ? 20.149  4.123   57.974  0.42 35.62  ? 24  ARG A CG    1 
ATOM   199  C  CD    A ARG A 1 52  ? 21.042  4.228   59.462  0.58 36.11  ? 24  ARG A CD    1 
ATOM   200  C  CD    B ARG A 1 52  ? 20.462  4.245   59.471  0.42 36.10  ? 24  ARG A CD    1 
ATOM   201  N  NE    A ARG A 1 52  ? 21.332  5.450   60.203  0.58 30.68  ? 24  ARG A NE    1 
ATOM   202  N  NE    B ARG A 1 52  ? 20.090  3.066   60.254  0.42 36.61  ? 24  ARG A NE    1 
ATOM   203  C  CZ    A ARG A 1 52  ? 22.540  5.976   60.382  0.58 32.68  ? 24  ARG A CZ    1 
ATOM   204  C  CZ    B ARG A 1 52  ? 20.949  2.277   60.892  0.42 36.66  ? 24  ARG A CZ    1 
ATOM   205  N  NH1   A ARG A 1 52  ? 23.637  5.384   59.924  0.58 17.81  ? 24  ARG A NH1   1 
ATOM   206  N  NH1   B ARG A 1 52  ? 22.255  2.505   60.870  0.42 33.42  ? 24  ARG A NH1   1 
ATOM   207  N  NH2   A ARG A 1 52  ? 22.646  7.131   61.025  0.58 26.50  ? 24  ARG A NH2   1 
ATOM   208  N  NH2   B ARG A 1 52  ? 20.486  1.241   61.584  0.42 39.17  ? 24  ARG A NH2   1 
ATOM   209  N  N     . ILE A 1 53  ? 22.192  6.168   54.307  1.00 35.71  ? 25  ILE A N     1 
ATOM   210  C  CA    . ILE A 1 53  ? 23.112  6.996   53.533  1.00 32.07  ? 25  ILE A CA    1 
ATOM   211  C  C     . ILE A 1 53  ? 22.334  7.960   52.644  1.00 35.10  ? 25  ILE A C     1 
ATOM   212  O  O     . ILE A 1 53  ? 22.688  9.141   52.540  1.00 32.92  ? 25  ILE A O     1 
ATOM   213  C  CB    . ILE A 1 53  ? 24.092  6.114   52.734  1.00 42.34  ? 25  ILE A CB    1 
ATOM   214  C  CG1   . ILE A 1 53  ? 24.924  5.253   53.696  1.00 45.36  ? 25  ILE A CG1   1 
ATOM   215  C  CG2   . ILE A 1 53  ? 25.050  6.961   51.900  1.00 44.14  ? 25  ILE A CG2   1 
ATOM   216  C  CD1   . ILE A 1 53  ? 25.750  4.181   53.001  1.00 45.58  ? 25  ILE A CD1   1 
ATOM   217  N  N     . SER A 1 54  ? 21.217  7.498   52.047  1.00 31.49  ? 26  SER A N     1 
ATOM   218  C  CA    . SER A 1 54  ? 20.355  8.413   51.290  1.00 34.13  ? 26  SER A CA    1 
ATOM   219  C  C     . SER A 1 54  ? 19.854  9.552   52.169  1.00 28.52  ? 26  SER A C     1 
ATOM   220  O  O     . SER A 1 54  ? 19.802  10.712  51.739  1.00 29.67  ? 26  SER A O     1 
ATOM   221  C  CB    . SER A 1 54  ? 19.167  7.654   50.684  1.00 35.39  ? 26  SER A CB    1 
ATOM   222  O  OG    . SER A 1 54  ? 19.625  6.659   49.775  1.00 33.91  ? 26  SER A OG    1 
ATOM   223  N  N     . SER A 1 55  ? 19.461  9.240   53.402  1.00 26.48  ? 27  SER A N     1 
ATOM   224  C  CA    . SER A 1 55  ? 19.020  10.292  54.305  1.00 24.69  ? 27  SER A CA    1 
ATOM   225  C  C     . SER A 1 55  ? 20.126  11.319  54.526  1.00 28.10  ? 27  SER A C     1 
ATOM   226  O  O     . SER A 1 55  ? 19.886  12.531  54.478  1.00 29.15  ? 27  SER A O     1 
ATOM   227  C  CB    . SER A 1 55  ? 18.580  9.683   55.631  1.00 28.91  ? 27  SER A CB    1 
ATOM   228  O  OG    . SER A 1 55  ? 18.097  10.698  56.479  1.00 29.07  ? 27  SER A OG    1 
ATOM   229  N  N     . GLN A 1 56  ? 21.343  10.849  54.789  1.00 29.52  ? 28  GLN A N     1 
ATOM   230  C  CA    A GLN A 1 56  ? 22.451  11.770  55.030  0.55 30.42  ? 28  GLN A CA    1 
ATOM   231  C  CA    B GLN A 1 56  ? 22.447  11.769  55.033  0.45 30.42  ? 28  GLN A CA    1 
ATOM   232  C  C     . GLN A 1 56  ? 22.656  12.699  53.841  1.00 30.82  ? 28  GLN A C     1 
ATOM   233  O  O     . GLN A 1 56  ? 22.739  13.923  54.000  1.00 27.11  ? 28  GLN A O     1 
ATOM   234  C  CB    A GLN A 1 56  ? 23.734  10.995  55.332  0.55 30.60  ? 28  GLN A CB    1 
ATOM   235  C  CB    B GLN A 1 56  ? 23.718  10.980  55.341  0.45 30.59  ? 28  GLN A CB    1 
ATOM   236  C  CG    A GLN A 1 56  ? 24.943  11.914  55.593  0.55 32.04  ? 28  GLN A CG    1 
ATOM   237  C  CG    B GLN A 1 56  ? 24.920  11.860  55.656  0.45 32.05  ? 28  GLN A CG    1 
ATOM   238  C  CD    A GLN A 1 56  ? 26.207  11.150  55.930  0.55 32.04  ? 28  GLN A CD    1 
ATOM   239  C  CD    B GLN A 1 56  ? 25.902  11.918  54.519  0.45 31.67  ? 28  GLN A CD    1 
ATOM   240  O  OE1   A GLN A 1 56  ? 26.511  10.133  55.312  0.55 35.89  ? 28  GLN A OE1   1 
ATOM   241  O  OE1   B GLN A 1 56  ? 26.385  10.887  54.049  0.45 33.45  ? 28  GLN A OE1   1 
ATOM   242  N  NE2   A GLN A 1 56  ? 26.952  11.637  56.918  0.55 31.95  ? 28  GLN A NE2   1 
ATOM   243  N  NE2   B GLN A 1 56  ? 26.212  13.123  54.069  0.45 36.75  ? 28  GLN A NE2   1 
ATOM   244  N  N     . LYS A 1 57  ? 22.723  12.132  52.633  1.00 30.76  ? 29  LYS A N     1 
ATOM   245  C  CA    . LYS A 1 57  ? 22.940  12.943  51.437  1.00 32.11  ? 29  LYS A CA    1 
ATOM   246  C  C     . LYS A 1 57  ? 21.769  13.866  51.154  1.00 27.41  ? 29  LYS A C     1 
ATOM   247  O  O     . LYS A 1 57  ? 21.962  15.045  50.834  1.00 28.34  ? 29  LYS A O     1 
ATOM   248  C  CB    . LYS A 1 57  ? 23.210  12.036  50.239  1.00 31.26  ? 29  LYS A CB    1 
ATOM   249  C  CG    . LYS A 1 57  ? 24.450  11.198  50.456  1.00 39.55  ? 29  LYS A CG    1 
ATOM   250  C  CD    . LYS A 1 57  ? 24.788  10.332  49.258  1.00 50.62  ? 29  LYS A CD    1 
ATOM   251  C  CE    . LYS A 1 57  ? 26.103  9.602   49.510  1.00 57.28  ? 29  LYS A CE    1 
ATOM   252  N  NZ    . LYS A 1 57  ? 26.418  8.606   48.459  1.00 57.63  ? 29  LYS A NZ    1 
ATOM   253  N  N     . ASN A 1 58  ? 20.537  13.363  51.261  1.00 33.11  ? 30  ASN A N     1 
ATOM   254  C  CA    . ASN A 1 58  ? 19.397  14.217  50.950  1.00 31.16  ? 30  ASN A CA    1 
ATOM   255  C  C     . ASN A 1 58  ? 19.275  15.367  51.941  1.00 30.18  ? 30  ASN A C     1 
ATOM   256  O  O     . ASN A 1 58  ? 18.831  16.460  51.568  1.00 28.43  ? 30  ASN A O     1 
ATOM   257  C  CB    . ASN A 1 58  ? 18.090  13.403  50.924  1.00 32.57  ? 30  ASN A CB    1 
ATOM   258  C  CG    . ASN A 1 58  ? 18.017  12.469  49.732  1.00 32.97  ? 30  ASN A CG    1 
ATOM   259  O  OD1   . ASN A 1 58  ? 18.837  12.558  48.820  1.00 34.91  ? 30  ASN A OD1   1 
ATOM   260  N  ND2   . ASN A 1 58  ? 17.025  11.588  49.719  1.00 29.88  ? 30  ASN A ND2   1 
ATOM   261  N  N     . GLN A 1 59  ? 19.613  15.129  53.220  1.00 28.65  ? 31  GLN A N     1 
ATOM   262  C  CA    . GLN A 1 59  ? 19.597  16.223  54.191  1.00 36.00  ? 31  GLN A CA    1 
ATOM   263  C  C     . GLN A 1 59  ? 20.525  17.347  53.751  1.00 30.51  ? 31  GLN A C     1 
ATOM   264  O  O     . GLN A 1 59  ? 20.182  18.527  53.890  1.00 34.38  ? 31  GLN A O     1 
ATOM   265  C  CB    . GLN A 1 59  ? 19.995  15.729  55.591  1.00 23.84  ? 31  GLN A CB    1 
ATOM   266  C  CG    . GLN A 1 59  ? 19.780  16.755  56.699  1.00 30.75  ? 31  GLN A CG    1 
ATOM   267  C  CD    . GLN A 1 59  ? 20.927  17.769  56.840  1.00 32.82  ? 31  GLN A CD    1 
ATOM   268  O  OE1   . GLN A 1 59  ? 22.072  17.467  56.537  1.00 32.81  ? 31  GLN A OE1   1 
ATOM   269  N  NE2   . GLN A 1 59  ? 20.606  18.971  57.308  1.00 32.01  ? 31  GLN A NE2   1 
ATOM   270  N  N     . GLN A 1 60  ? 21.709  17.000  53.230  1.00 30.03  ? 32  GLN A N     1 
ATOM   271  C  CA    . GLN A 1 60  ? 22.632  18.039  52.773  1.00 36.61  ? 32  GLN A CA    1 
ATOM   272  C  C     . GLN A 1 60  ? 22.111  18.752  51.517  1.00 41.31  ? 32  GLN A C     1 
ATOM   273  O  O     . GLN A 1 60  ? 22.514  19.889  51.250  1.00 36.67  ? 32  GLN A O     1 
ATOM   274  C  CB    . GLN A 1 60  ? 24.015  17.446  52.484  1.00 33.37  ? 32  GLN A CB    1 
ATOM   275  C  CG    . GLN A 1 60  ? 24.914  17.142  53.727  1.00 37.05  ? 32  GLN A CG    1 
ATOM   276  C  CD    . GLN A 1 60  ? 25.226  18.368  54.588  1.00 46.52  ? 32  GLN A CD    1 
ATOM   277  O  OE1   . GLN A 1 60  ? 26.153  19.130  54.301  1.00 45.62  ? 32  GLN A OE1   1 
ATOM   278  N  NE2   . GLN A 1 60  ? 24.482  18.522  55.697  1.00 38.00  ? 32  GLN A NE2   1 
ATOM   279  N  N     . ALA A 1 61  ? 21.222  18.116  50.750  1.00 28.93  ? 33  ALA A N     1 
ATOM   280  C  CA    . ALA A 1 61  ? 20.639  18.699  49.542  1.00 38.22  ? 33  ALA A CA    1 
ATOM   281  C  C     . ALA A 1 61  ? 19.294  19.351  49.789  1.00 35.79  ? 33  ALA A C     1 
ATOM   282  O  O     . ALA A 1 61  ? 18.742  19.967  48.877  1.00 42.85  ? 33  ALA A O     1 
ATOM   283  C  CB    . ALA A 1 61  ? 20.488  17.629  48.454  1.00 36.17  ? 33  ALA A CB    1 
ATOM   284  N  N     . ASN A 1 62  ? 18.756  19.237  51.001  1.00 39.44  ? 34  ASN A N     1 
ATOM   285  C  CA    . ASN A 1 62  ? 17.425  19.736  51.323  1.00 41.34  ? 34  ASN A CA    1 
ATOM   286  C  C     . ASN A 1 62  ? 16.384  19.017  50.463  1.00 42.55  ? 34  ASN A C     1 
ATOM   287  O  O     . ASN A 1 62  ? 15.452  19.619  49.924  1.00 40.72  ? 34  ASN A O     1 
ATOM   288  C  CB    . ASN A 1 62  ? 17.344  21.258  51.168  1.00 48.67  ? 34  ASN A CB    1 
ATOM   289  C  CG    . ASN A 1 62  ? 16.038  21.825  51.688  1.00 52.36  ? 34  ASN A CG    1 
ATOM   290  O  OD1   . ASN A 1 62  ? 15.560  21.425  52.752  1.00 57.69  ? 34  ASN A OD1   1 
ATOM   291  N  ND2   . ASN A 1 62  ? 15.449  22.752  50.938  1.00 50.17  ? 34  ASN A ND2   1 
ATOM   292  N  N     . VAL A 1 63  ? 16.570  17.709  50.334  1.00 37.89  ? 35  VAL A N     1 
ATOM   293  C  CA    . VAL A 1 63  ? 15.692  16.816  49.588  1.00 37.90  ? 35  VAL A CA    1 
ATOM   294  C  C     . VAL A 1 63  ? 15.010  15.874  50.577  1.00 34.79  ? 35  VAL A C     1 
ATOM   295  O  O     . VAL A 1 63  ? 15.623  15.473  51.574  1.00 31.50  ? 35  VAL A O     1 
ATOM   296  C  CB    . VAL A 1 63  ? 16.522  16.048  48.541  1.00 32.57  ? 35  VAL A CB    1 
ATOM   297  C  CG1   . VAL A 1 63  ? 15.827  14.777  48.102  1.00 31.89  ? 35  VAL A CG1   1 
ATOM   298  C  CG2   . VAL A 1 63  ? 16.822  16.951  47.340  1.00 34.44  ? 35  VAL A CG2   1 
ATOM   299  N  N     . THR A 1 64  ? 13.744  15.533  50.321  1.00 30.32  ? 36  THR A N     1 
ATOM   300  C  CA    . THR A 1 64  ? 12.995  14.658  51.226  1.00 35.17  ? 36  THR A CA    1 
ATOM   301  C  C     . THR A 1 64  ? 12.327  13.531  50.440  1.00 32.77  ? 36  THR A C     1 
ATOM   302  O  O     . THR A 1 64  ? 12.287  13.545  49.209  1.00 26.25  ? 36  THR A O     1 
ATOM   303  C  CB    . THR A 1 64  ? 11.956  15.438  52.060  1.00 31.83  ? 36  THR A CB    1 
ATOM   304  O  OG1   . THR A 1 64  ? 11.116  16.244  51.228  1.00 31.93  ? 36  THR A OG1   1 
ATOM   305  C  CG2   . THR A 1 64  ? 12.637  16.348  53.074  1.00 31.43  ? 36  THR A CG2   1 
ATOM   306  N  N     . GLY A 1 65  ? 11.837  12.518  51.148  1.00 29.32  ? 37  GLY A N     1 
ATOM   307  C  CA    . GLY A 1 65  ? 11.098  11.457  50.466  1.00 24.60  ? 37  GLY A CA    1 
ATOM   308  C  C     . GLY A 1 65  ? 11.081  10.160  51.269  1.00 31.06  ? 37  GLY A C     1 
ATOM   309  O  O     . GLY A 1 65  ? 11.364  10.145  52.473  1.00 27.54  ? 37  GLY A O     1 
ATOM   310  N  N     . VAL A 1 66  ? 10.778  9.076   50.560  1.00 24.61  ? 38  VAL A N     1 
ATOM   311  C  CA    . VAL A 1 66  ? 10.527  7.781   51.183  1.00 27.46  ? 38  VAL A CA    1 
ATOM   312  C  C     . VAL A 1 66  ? 10.973  6.690   50.222  1.00 27.27  ? 38  VAL A C     1 
ATOM   313  O  O     . VAL A 1 66  ? 10.771  6.789   49.006  1.00 29.94  ? 38  VAL A O     1 
ATOM   314  C  CB    . VAL A 1 66  ? 9.039   7.605   51.571  1.00 28.17  ? 38  VAL A CB    1 
ATOM   315  C  CG1   . VAL A 1 66  ? 8.109   7.733   50.349  1.00 27.53  ? 38  VAL A CG1   1 
ATOM   316  C  CG2   . VAL A 1 66  ? 8.809   6.235   52.275  1.00 25.58  ? 38  VAL A CG2   1 
ATOM   317  N  N     . LEU A 1 67  ? 11.576  5.646   50.776  1.00 27.85  ? 39  LEU A N     1 
ATOM   318  C  CA    . LEU A 1 67  ? 12.032  4.478   50.026  1.00 29.79  ? 39  LEU A CA    1 
ATOM   319  C  C     . LEU A 1 67  ? 11.401  3.232   50.630  1.00 35.65  ? 39  LEU A C     1 
ATOM   320  O  O     . LEU A 1 67  ? 11.495  3.010   51.848  1.00 30.30  ? 39  LEU A O     1 
ATOM   321  C  CB    . LEU A 1 67  ? 13.573  4.379   50.051  1.00 30.32  ? 39  LEU A CB    1 
ATOM   322  C  CG    . LEU A 1 67  ? 14.303  3.165   49.451  1.00 32.42  ? 39  LEU A CG    1 
ATOM   323  C  CD1   . LEU A 1 67  ? 14.130  3.050   47.949  1.00 31.74  ? 39  LEU A CD1   1 
ATOM   324  C  CD2   . LEU A 1 67  ? 15.801  3.197   49.837  1.00 27.91  ? 39  LEU A CD2   1 
ATOM   325  N  N     . LEU A 1 68  ? 10.728  2.435   49.788  1.00 27.84  ? 40  LEU A N     1 
ATOM   326  C  CA    . LEU A 1 68  ? 10.083  1.210   50.229  1.00 25.56  ? 40  LEU A CA    1 
ATOM   327  C  C     . LEU A 1 68  ? 10.557  0.063   49.357  1.00 32.29  ? 40  LEU A C     1 
ATOM   328  O  O     . LEU A 1 68  ? 10.823  0.241   48.168  1.00 30.41  ? 40  LEU A O     1 
ATOM   329  C  CB    . LEU A 1 68  ? 8.522   1.301   50.178  1.00 25.98  ? 40  LEU A CB    1 
ATOM   330  C  CG    . LEU A 1 68  ? 7.857   2.513   50.830  1.00 25.55  ? 40  LEU A CG    1 
ATOM   331  C  CD1   . LEU A 1 68  ? 7.680   3.620   49.819  1.00 28.64  ? 40  LEU A CD1   1 
ATOM   332  C  CD2   . LEU A 1 68  ? 6.497   2.118   51.435  1.00 27.46  ? 40  LEU A CD2   1 
ATOM   333  N  N     . CYS A 1 69  ? 10.686  -1.109  49.956  1.00 28.97  ? 41  CYS A N     1 
ATOM   334  C  CA    . CYS A 1 69  ? 11.056  -2.282  49.197  1.00 27.99  ? 41  CYS A CA    1 
ATOM   335  C  C     . CYS A 1 69  ? 10.034  -3.364  49.467  1.00 35.87  ? 41  CYS A C     1 
ATOM   336  O  O     . CYS A 1 69  ? 9.447   -3.422  50.547  1.00 32.80  ? 41  CYS A O     1 
ATOM   337  C  CB    . CYS A 1 69  ? 12.461  -2.763  49.544  1.00 27.88  ? 41  CYS A CB    1 
ATOM   338  S  SG    . CYS A 1 69  ? 12.608  -3.447  51.182  1.00 37.17  ? 41  CYS A SG    1 
ATOM   339  N  N     . LEU A 1 70  ? 9.797   -4.200  48.463  1.00 34.97  ? 42  LEU A N     1 
ATOM   340  C  CA    . LEU A 1 70  ? 8.866   -5.318  48.607  1.00 40.12  ? 42  LEU A CA    1 
ATOM   341  C  C     . LEU A 1 70  ? 9.255   -6.371  47.583  1.00 32.49  ? 42  LEU A C     1 
ATOM   342  O  O     . LEU A 1 70  ? 9.099   -6.136  46.380  1.00 37.84  ? 42  LEU A O     1 
ATOM   343  C  CB    . LEU A 1 70  ? 7.417   -4.872  48.408  1.00 35.78  ? 42  LEU A CB    1 
ATOM   344  C  CG    . LEU A 1 70  ? 6.351   -5.979  48.354  1.00 36.71  ? 42  LEU A CG    1 
ATOM   345  C  CD1   . LEU A 1 70  ? 6.251   -6.706  49.701  1.00 40.10  ? 42  LEU A CD1   1 
ATOM   346  C  CD2   . LEU A 1 70  ? 4.965   -5.422  47.958  1.00 36.10  ? 42  LEU A CD2   1 
ATOM   347  N  N     . ASP A 1 71  ? 9.788   -7.502  48.055  1.00 33.80  ? 43  ASP A N     1 
ATOM   348  C  CA    . ASP A 1 71  ? 10.034  -8.666  47.199  1.00 42.66  ? 43  ASP A CA    1 
ATOM   349  C  C     . ASP A 1 71  ? 10.881  -8.316  45.963  1.00 41.03  ? 43  ASP A C     1 
ATOM   350  O  O     . ASP A 1 71  ? 10.552  -8.670  44.830  1.00 37.06  ? 43  ASP A O     1 
ATOM   351  C  CB    . ASP A 1 71  ? 8.690   -9.288  46.802  1.00 45.01  ? 43  ASP A CB    1 
ATOM   352  C  CG    . ASP A 1 71  ? 8.838   -10.622 46.119  1.00 54.36  ? 43  ASP A CG    1 
ATOM   353  O  OD1   . ASP A 1 71  ? 9.135   -11.619 46.812  1.00 53.63  ? 43  ASP A OD1   1 
ATOM   354  O  OD2   . ASP A 1 71  ? 8.626   -10.666 44.888  1.00 66.53  ? 43  ASP A OD2   1 
ATOM   355  N  N     . GLY A 1 72  ? 11.992  -7.614  46.188  1.00 38.31  ? 44  GLY A N     1 
ATOM   356  C  CA    . GLY A 1 72  ? 12.896  -7.283  45.102  1.00 37.31  ? 44  GLY A CA    1 
ATOM   357  C  C     . GLY A 1 72  ? 12.442  -6.130  44.239  1.00 42.40  ? 44  GLY A C     1 
ATOM   358  O  O     . GLY A 1 72  ? 12.928  -5.974  43.112  1.00 43.41  ? 44  GLY A O     1 
ATOM   359  N  N     . ILE A 1 73  ? 11.511  -5.325  44.730  1.00 37.14  ? 45  ILE A N     1 
ATOM   360  C  CA    . ILE A 1 73  ? 11.058  -4.109  44.075  1.00 33.96  ? 45  ILE A CA    1 
ATOM   361  C  C     . ILE A 1 73  ? 11.424  -2.940  44.972  1.00 38.47  ? 45  ILE A C     1 
ATOM   362  O  O     . ILE A 1 73  ? 11.174  -2.986  46.183  1.00 38.23  ? 45  ILE A O     1 
ATOM   363  C  CB    . ILE A 1 73  ? 9.528   -4.121  43.874  1.00 39.87  ? 45  ILE A CB    1 
ATOM   364  C  CG1   . ILE A 1 73  ? 9.048   -5.415  43.217  1.00 42.25  ? 45  ILE A CG1   1 
ATOM   365  C  CG2   . ILE A 1 73  ? 9.073   -2.866  43.115  1.00 32.21  ? 45  ILE A CG2   1 
ATOM   366  C  CD1   . ILE A 1 73  ? 7.535   -5.626  43.421  1.00 39.89  ? 45  ILE A CD1   1 
ATOM   367  N  N     . PHE A 1 74  ? 11.965  -1.879  44.388  1.00 31.54  ? 46  PHE A N     1 
ATOM   368  C  CA    . PHE A 1 74  ? 12.103  -0.613  45.092  1.00 35.46  ? 46  PHE A CA    1 
ATOM   369  C  C     . PHE A 1 74  ? 11.002  0.334   44.632  1.00 36.61  ? 46  PHE A C     1 
ATOM   370  O  O     . PHE A 1 74  ? 10.660  0.370   43.443  1.00 31.54  ? 46  PHE A O     1 
ATOM   371  C  CB    . PHE A 1 74  ? 13.453  0.049   44.822  1.00 31.82  ? 46  PHE A CB    1 
ATOM   372  C  CG    . PHE A 1 74  ? 14.596  -0.530  45.595  1.00 32.71  ? 46  PHE A CG    1 
ATOM   373  C  CD1   . PHE A 1 74  ? 14.573  -0.570  46.977  1.00 31.14  ? 46  PHE A CD1   1 
ATOM   374  C  CD2   . PHE A 1 74  ? 15.739  -0.957  44.933  1.00 31.71  ? 46  PHE A CD2   1 
ATOM   375  C  CE1   . PHE A 1 74  ? 15.651  -1.092  47.692  1.00 36.01  ? 46  PHE A CE1   1 
ATOM   376  C  CE2   . PHE A 1 74  ? 16.836  -1.450  45.640  1.00 34.07  ? 46  PHE A CE2   1 
ATOM   377  C  CZ    . PHE A 1 74  ? 16.790  -1.526  47.021  1.00 37.30  ? 46  PHE A CZ    1 
ATOM   378  N  N     . PHE A 1 75  ? 10.449  1.094   45.579  1.00 28.39  ? 47  PHE A N     1 
ATOM   379  C  CA    . PHE A 1 75  ? 9.613   2.252   45.288  1.00 28.99  ? 47  PHE A CA    1 
ATOM   380  C  C     . PHE A 1 75  ? 10.260  3.435   45.981  1.00 30.83  ? 47  PHE A C     1 
ATOM   381  O  O     . PHE A 1 75  ? 10.636  3.328   47.154  1.00 31.68  ? 47  PHE A O     1 
ATOM   382  C  CB    . PHE A 1 75  ? 8.167   2.128   45.814  1.00 29.35  ? 47  PHE A CB    1 
ATOM   383  C  CG    . PHE A 1 75  ? 7.499   0.801   45.549  1.00 32.50  ? 47  PHE A CG    1 
ATOM   384  C  CD1   . PHE A 1 75  ? 7.727   -0.283  46.386  1.00 36.21  ? 47  PHE A CD1   1 
ATOM   385  C  CD2   . PHE A 1 75  ? 6.586   0.655   44.514  1.00 34.08  ? 47  PHE A CD2   1 
ATOM   386  C  CE1   . PHE A 1 75  ? 7.090   -1.506  46.174  1.00 35.83  ? 47  PHE A CE1   1 
ATOM   387  C  CE2   . PHE A 1 75  ? 5.943   -0.574  44.297  1.00 31.78  ? 47  PHE A CE2   1 
ATOM   388  C  CZ    . PHE A 1 75  ? 6.196   -1.645  45.130  1.00 35.29  ? 47  PHE A CZ    1 
ATOM   389  N  N     . GLN A 1 76  ? 10.368  4.561   45.282  1.00 28.20  ? 48  GLN A N     1 
ATOM   390  C  CA    . GLN A 1 76  ? 10.885  5.762   45.916  1.00 29.37  ? 48  GLN A CA    1 
ATOM   391  C  C     . GLN A 1 76  ? 10.150  6.994   45.416  1.00 28.44  ? 48  GLN A C     1 
ATOM   392  O  O     . GLN A 1 76  ? 9.817   7.101   44.228  1.00 30.69  ? 48  GLN A O     1 
ATOM   393  C  CB    . GLN A 1 76  ? 12.392  5.946   45.671  1.00 25.45  ? 48  GLN A CB    1 
ATOM   394  C  CG    . GLN A 1 76  ? 12.948  7.108   46.485  1.00 28.16  ? 48  GLN A CG    1 
ATOM   395  C  CD    . GLN A 1 76  ? 14.453  7.146   46.506  1.00 41.22  ? 48  GLN A CD    1 
ATOM   396  O  OE1   . GLN A 1 76  ? 15.123  6.565   45.640  1.00 41.87  ? 48  GLN A OE1   1 
ATOM   397  N  NE2   . GLN A 1 76  ? 15.002  7.813   47.508  1.00 41.92  ? 48  GLN A NE2   1 
ATOM   398  N  N     . ILE A 1 77  ? 9.883   7.907   46.348  1.00 27.44  ? 49  ILE A N     1 
ATOM   399  C  CA    . ILE A 1 77  ? 9.436   9.260   46.059  1.00 26.40  ? 49  ILE A CA    1 
ATOM   400  C  C     . ILE A 1 77  ? 10.549  10.209  46.495  1.00 37.75  ? 49  ILE A C     1 
ATOM   401  O  O     . ILE A 1 77  ? 11.046  10.105  47.622  1.00 28.70  ? 49  ILE A O     1 
ATOM   402  C  CB    . ILE A 1 77  ? 8.119   9.574   46.788  1.00 32.74  ? 49  ILE A CB    1 
ATOM   403  C  CG1   . ILE A 1 77  ? 7.040   8.548   46.399  1.00 32.92  ? 49  ILE A CG1   1 
ATOM   404  C  CG2   . ILE A 1 77  ? 7.653   10.998  46.496  1.00 29.69  ? 49  ILE A CG2   1 
ATOM   405  C  CD1   . ILE A 1 77  ? 5.767   8.614   47.273  1.00 25.64  ? 49  ILE A CD1   1 
ATOM   406  N  N     . LEU A 1 78  ? 10.940  11.125  45.610  1.00 32.38  ? 50  LEU A N     1 
ATOM   407  C  CA    . LEU A 1 78  ? 11.946  12.146  45.898  1.00 34.66  ? 50  LEU A CA    1 
ATOM   408  C  C     . LEU A 1 78  ? 11.368  13.528  45.636  1.00 38.16  ? 50  LEU A C     1 
ATOM   409  O  O     . LEU A 1 78  ? 10.777  13.754  44.576  1.00 36.43  ? 50  LEU A O     1 
ATOM   410  C  CB    . LEU A 1 78  ? 13.181  11.960  45.018  1.00 40.71  ? 50  LEU A CB    1 
ATOM   411  C  CG    . LEU A 1 78  ? 14.324  11.096  45.513  1.00 45.01  ? 50  LEU A CG    1 
ATOM   412  C  CD1   . LEU A 1 78  ? 15.468  11.179  44.518  1.00 39.43  ? 50  LEU A CD1   1 
ATOM   413  C  CD2   . LEU A 1 78  ? 14.759  11.587  46.880  1.00 44.90  ? 50  LEU A CD2   1 
ATOM   414  N  N     . GLU A 1 79  ? 11.572  14.463  46.568  1.00 35.50  ? 51  GLU A N     1 
ATOM   415  C  CA    . GLU A 1 79  ? 11.086  15.825  46.383  1.00 38.25  ? 51  GLU A CA    1 
ATOM   416  C  C     . GLU A 1 79  ? 12.125  16.844  46.843  1.00 42.04  ? 51  GLU A C     1 
ATOM   417  O  O     . GLU A 1 79  ? 12.841  16.643  47.829  1.00 36.29  ? 51  GLU A O     1 
ATOM   418  C  CB    . GLU A 1 79  ? 9.760   16.063  47.115  1.00 32.87  ? 51  GLU A CB    1 
ATOM   419  C  CG    . GLU A 1 79  ? 9.898   16.043  48.605  1.00 31.88  ? 51  GLU A CG    1 
ATOM   420  C  CD    . GLU A 1 79  ? 8.591   15.807  49.340  1.00 40.08  ? 51  GLU A CD    1 
ATOM   421  O  OE1   . GLU A 1 79  ? 7.504   15.879  48.712  1.00 41.97  ? 51  GLU A OE1   1 
ATOM   422  O  OE2   . GLU A 1 79  ? 8.660   15.533  50.561  1.00 31.41  ? 51  GLU A OE2   1 
ATOM   423  N  N     . GLY A 1 80  ? 12.189  17.946  46.110  1.00 39.98  ? 52  GLY A N     1 
ATOM   424  C  CA    . GLY A 1 80  ? 13.141  18.994  46.400  1.00 41.55  ? 52  GLY A CA    1 
ATOM   425  C  C     . GLY A 1 80  ? 13.278  19.924  45.210  1.00 51.61  ? 52  GLY A C     1 
ATOM   426  O  O     . GLY A 1 80  ? 12.496  19.873  44.261  1.00 46.68  ? 52  GLY A O     1 
ATOM   427  N  N     . GLU A 1 81  ? 14.297  20.774  45.288  1.00 46.33  ? 53  GLU A N     1 
ATOM   428  C  CA    . GLU A 1 81  ? 14.585  21.701  44.204  1.00 51.83  ? 53  GLU A CA    1 
ATOM   429  C  C     . GLU A 1 81  ? 14.902  20.929  42.925  1.00 43.74  ? 53  GLU A C     1 
ATOM   430  O  O     . GLU A 1 81  ? 15.656  19.950  42.943  1.00 41.26  ? 53  GLU A O     1 
ATOM   431  C  CB    . GLU A 1 81  ? 15.750  22.613  44.607  1.00 52.15  ? 53  GLU A CB    1 
ATOM   432  C  CG    . GLU A 1 81  ? 15.955  23.810  43.699  1.00 57.12  ? 53  GLU A CG    1 
ATOM   433  C  CD    . GLU A 1 81  ? 16.828  23.483  42.498  1.00 64.98  ? 53  GLU A CD    1 
ATOM   434  O  OE1   . GLU A 1 81  ? 17.956  22.975  42.705  1.00 67.62  ? 53  GLU A OE1   1 
ATOM   435  O  OE2   . GLU A 1 81  ? 16.378  23.719  41.349  1.00 63.63  ? 53  GLU A OE2   1 
ATOM   436  N  N     . ALA A 1 82  ? 14.312  21.376  41.809  1.00 45.38  ? 54  ALA A N     1 
ATOM   437  C  CA    . ALA A 1 82  ? 14.352  20.597  40.564  1.00 51.68  ? 54  ALA A CA    1 
ATOM   438  C  C     . ALA A 1 82  ? 15.781  20.245  40.144  1.00 51.25  ? 54  ALA A C     1 
ATOM   439  O  O     . ALA A 1 82  ? 16.071  19.095  39.783  1.00 46.41  ? 54  ALA A O     1 
ATOM   440  C  CB    . ALA A 1 82  ? 13.644  21.363  39.447  1.00 47.69  ? 54  ALA A CB    1 
ATOM   441  N  N     . GLU A 1 83  ? 16.686  21.229  40.170  1.00 56.97  ? 55  GLU A N     1 
ATOM   442  C  CA    . GLU A 1 83  ? 18.075  20.970  39.798  1.00 55.59  ? 55  GLU A CA    1 
ATOM   443  C  C     . GLU A 1 83  ? 18.696  19.905  40.697  1.00 54.71  ? 55  GLU A C     1 
ATOM   444  O  O     . GLU A 1 83  ? 19.363  18.983  40.213  1.00 53.16  ? 55  GLU A O     1 
ATOM   445  C  CB    . GLU A 1 83  ? 18.882  22.272  39.856  1.00 68.97  ? 55  GLU A CB    1 
ATOM   446  C  CG    . GLU A 1 83  ? 20.393  22.121  39.667  1.00 71.12  ? 55  GLU A CG    1 
ATOM   447  C  CD    . GLU A 1 83  ? 20.833  22.118  38.201  1.00 85.12  ? 55  GLU A CD    1 
ATOM   448  O  OE1   . GLU A 1 83  ? 20.177  21.459  37.358  1.00 77.28  ? 55  GLU A OE1   1 
ATOM   449  O  OE2   . GLU A 1 83  ? 21.862  22.764  37.897  1.00 85.36  ? 55  GLU A OE2   1 
ATOM   450  N  N     . LYS A 1 84  ? 18.480  20.005  42.011  1.00 49.74  ? 56  LYS A N     1 
ATOM   451  C  CA    . LYS A 1 84  ? 19.029  18.996  42.914  1.00 53.67  ? 56  LYS A CA    1 
ATOM   452  C  C     . LYS A 1 84  ? 18.382  17.632  42.690  1.00 47.20  ? 56  LYS A C     1 
ATOM   453  O  O     . LYS A 1 84  ? 19.062  16.598  42.736  1.00 46.67  ? 56  LYS A O     1 
ATOM   454  C  CB    . LYS A 1 84  ? 18.859  19.450  44.360  1.00 48.72  ? 56  LYS A CB    1 
ATOM   455  C  CG    . LYS A 1 84  ? 19.903  20.484  44.786  1.00 52.46  ? 56  LYS A CG    1 
ATOM   456  C  CD    . LYS A 1 84  ? 19.411  21.277  45.978  1.00 46.16  ? 56  LYS A CD    1 
ATOM   457  C  CE    . LYS A 1 84  ? 20.536  22.009  46.681  1.00 55.97  ? 56  LYS A CE    1 
ATOM   458  N  NZ    . LYS A 1 84  ? 20.182  23.426  46.972  1.00 63.17  ? 56  LYS A NZ    1 
ATOM   459  N  N     . ILE A 1 85  ? 17.069  17.606  42.449  1.00 46.49  ? 57  ILE A N     1 
ATOM   460  C  CA    . ILE A 1 85  ? 16.389  16.334  42.223  1.00 46.28  ? 57  ILE A CA    1 
ATOM   461  C  C     . ILE A 1 85  ? 17.007  15.606  41.033  1.00 48.09  ? 57  ILE A C     1 
ATOM   462  O  O     . ILE A 1 85  ? 17.309  14.405  41.107  1.00 44.48  ? 57  ILE A O     1 
ATOM   463  C  CB    . ILE A 1 85  ? 14.874  16.557  42.043  1.00 44.75  ? 57  ILE A CB    1 
ATOM   464  C  CG1   . ILE A 1 85  ? 14.221  16.939  43.373  1.00 42.95  ? 57  ILE A CG1   1 
ATOM   465  C  CG2   . ILE A 1 85  ? 14.206  15.294  41.565  1.00 44.59  ? 57  ILE A CG2   1 
ATOM   466  C  CD1   . ILE A 1 85  ? 14.515  15.942  44.487  1.00 43.84  ? 57  ILE A CD1   1 
ATOM   467  N  N     . ASP A 1 86  ? 17.255  16.335  39.931  1.00 49.88  ? 58  ASP A N     1 
ATOM   468  C  CA    . ASP A 1 86  ? 17.768  15.682  38.723  1.00 51.63  ? 58  ASP A CA    1 
ATOM   469  C  C     . ASP A 1 86  ? 19.178  15.139  38.937  1.00 52.47  ? 58  ASP A C     1 
ATOM   470  O  O     . ASP A 1 86  ? 19.497  14.036  38.471  1.00 52.37  ? 58  ASP A O     1 
ATOM   471  C  CB    . ASP A 1 86  ? 17.721  16.641  37.525  1.00 54.15  ? 58  ASP A CB    1 
ATOM   472  C  CG    . ASP A 1 86  ? 16.281  16.912  37.033  1.00 66.06  ? 58  ASP A CG    1 
ATOM   473  O  OD1   . ASP A 1 86  ? 15.503  15.946  36.860  1.00 62.18  ? 58  ASP A OD1   1 
ATOM   474  O  OD2   . ASP A 1 86  ? 15.920  18.096  36.826  1.00 66.11  ? 58  ASP A OD2   1 
ATOM   475  N  N     . ARG A 1 87  ? 20.030  15.884  39.649  1.00 50.11  ? 59  ARG A N     1 
ATOM   476  C  CA    . ARG A 1 87  ? 21.365  15.380  39.967  1.00 48.44  ? 59  ARG A CA    1 
ATOM   477  C  C     . ARG A 1 87  ? 21.280  14.045  40.682  1.00 49.35  ? 59  ARG A C     1 
ATOM   478  O  O     . ARG A 1 87  ? 21.956  13.079  40.304  1.00 44.53  ? 59  ARG A O     1 
ATOM   479  C  CB    . ARG A 1 87  ? 22.136  16.388  40.827  1.00 57.33  ? 59  ARG A CB    1 
ATOM   480  C  CG    . ARG A 1 87  ? 22.249  17.792  40.239  1.00 65.94  ? 59  ARG A CG    1 
ATOM   481  C  CD    . ARG A 1 87  ? 23.344  17.848  39.169  1.00 65.76  ? 59  ARG A CD    1 
ATOM   482  N  NE    . ARG A 1 87  ? 22.859  17.583  37.816  1.00 65.37  ? 59  ARG A NE    1 
ATOM   483  C  CZ    . ARG A 1 87  ? 21.825  18.177  37.230  1.00 64.09  ? 59  ARG A CZ    1 
ATOM   484  N  NH1   . ARG A 1 87  ? 21.212  19.213  37.780  1.00 60.62  ? 59  ARG A NH1   1 
ATOM   485  N  NH2   . ARG A 1 87  ? 21.419  17.740  36.042  1.00 60.50  ? 59  ARG A NH2   1 
ATOM   486  N  N     . ILE A 1 88  ? 20.428  13.969  41.711  1.00 43.34  ? 60  ILE A N     1 
ATOM   487  C  CA    . ILE A 1 88  ? 20.289  12.735  42.476  1.00 43.13  ? 60  ILE A CA    1 
ATOM   488  C  C     . ILE A 1 88  ? 19.721  11.633  41.599  1.00 42.88  ? 60  ILE A C     1 
ATOM   489  O  O     . ILE A 1 88  ? 20.180  10.480  41.634  1.00 38.87  ? 60  ILE A O     1 
ATOM   490  C  CB    . ILE A 1 88  ? 19.411  12.979  43.717  1.00 46.83  ? 60  ILE A CB    1 
ATOM   491  C  CG1   . ILE A 1 88  ? 20.132  13.895  44.708  1.00 42.43  ? 60  ILE A CG1   1 
ATOM   492  C  CG2   . ILE A 1 88  ? 19.063  11.661  44.384  1.00 33.05  ? 60  ILE A CG2   1 
ATOM   493  C  CD1   . ILE A 1 88  ? 19.225  14.465  45.754  1.00 45.97  ? 60  ILE A CD1   1 
ATOM   494  N  N     . TYR A 1 89  ? 18.718  11.967  40.785  1.00 44.41  ? 61  TYR A N     1 
ATOM   495  C  CA    . TYR A 1 89  ? 18.065  10.921  40.012  1.00 47.25  ? 61  TYR A CA    1 
ATOM   496  C  C     . TYR A 1 89  ? 18.996  10.388  38.937  1.00 47.47  ? 61  TYR A C     1 
ATOM   497  O  O     . TYR A 1 89  ? 19.002  9.179   38.662  1.00 45.61  ? 61  TYR A O     1 
ATOM   498  C  CB    . TYR A 1 89  ? 16.764  11.440  39.412  1.00 49.78  ? 61  TYR A CB    1 
ATOM   499  C  CG    . TYR A 1 89  ? 15.963  10.358  38.747  1.00 50.46  ? 61  TYR A CG    1 
ATOM   500  C  CD1   . TYR A 1 89  ? 15.286  9.406   39.513  1.00 48.93  ? 61  TYR A CD1   1 
ATOM   501  C  CD2   . TYR A 1 89  ? 15.901  10.254  37.363  1.00 39.50  ? 61  TYR A CD2   1 
ATOM   502  C  CE1   . TYR A 1 89  ? 14.546  8.396   38.909  1.00 47.71  ? 61  TYR A CE1   1 
ATOM   503  C  CE2   . TYR A 1 89  ? 15.159  9.256   36.752  1.00 45.32  ? 61  TYR A CE2   1 
ATOM   504  C  CZ    . TYR A 1 89  ? 14.483  8.331   37.524  1.00 49.13  ? 61  TYR A CZ    1 
ATOM   505  O  OH    . TYR A 1 89  ? 13.756  7.331   36.920  1.00 53.26  ? 61  TYR A OH    1 
ATOM   506  N  N     . GLU A 1 90  ? 19.818  11.271  38.349  1.00 48.37  ? 62  GLU A N     1 
ATOM   507  C  CA    . GLU A 1 90  ? 20.894  10.828  37.462  1.00 45.93  ? 62  GLU A CA    1 
ATOM   508  C  C     . GLU A 1 90  ? 21.793  9.810   38.155  1.00 43.62  ? 62  GLU A C     1 
ATOM   509  O  O     . GLU A 1 90  ? 22.141  8.772   37.579  1.00 49.24  ? 62  GLU A O     1 
ATOM   510  C  CB    . GLU A 1 90  ? 21.724  12.024  36.999  1.00 52.71  ? 62  GLU A CB    1 
ATOM   511  C  CG    . GLU A 1 90  ? 21.184  12.738  35.787  1.00 66.58  ? 62  GLU A CG    1 
ATOM   512  C  CD    . GLU A 1 90  ? 22.252  13.569  35.110  1.00 72.96  ? 62  GLU A CD    1 
ATOM   513  O  OE1   . GLU A 1 90  ? 23.428  13.454  35.515  1.00 74.79  ? 62  GLU A OE1   1 
ATOM   514  O  OE2   . GLU A 1 90  ? 21.920  14.322  34.171  1.00 83.38  ? 62  GLU A OE2   1 
ATOM   515  N  N     . ARG A 1 91  ? 22.181  10.096  39.402  1.00 43.93  ? 63  ARG A N     1 
ATOM   516  C  CA    . ARG A 1 91  ? 23.004  9.153   40.153  1.00 38.89  ? 63  ARG A CA    1 
ATOM   517  C  C     . ARG A 1 91  ? 22.257  7.858   40.415  1.00 45.10  ? 63  ARG A C     1 
ATOM   518  O  O     . ARG A 1 91  ? 22.826  6.767   40.282  1.00 42.02  ? 63  ARG A O     1 
ATOM   519  C  CB    . ARG A 1 91  ? 23.453  9.787   41.468  1.00 46.80  ? 63  ARG A CB    1 
ATOM   520  C  CG    . ARG A 1 91  ? 24.907  10.156  41.511  1.00 45.20  ? 63  ARG A CG    1 
ATOM   521  C  CD    . ARG A 1 91  ? 25.346  10.634  42.881  1.00 54.53  ? 63  ARG A CD    1 
ATOM   522  N  NE    . ARG A 1 91  ? 24.873  11.981  43.176  1.00 56.84  ? 63  ARG A NE    1 
ATOM   523  C  CZ    . ARG A 1 91  ? 24.136  12.319  44.225  1.00 57.31  ? 63  ARG A CZ    1 
ATOM   524  N  NH1   . ARG A 1 91  ? 23.773  11.429  45.136  1.00 50.98  ? 63  ARG A NH1   1 
ATOM   525  N  NH2   . ARG A 1 91  ? 23.774  13.592  44.376  1.00 50.35  ? 63  ARG A NH2   1 
ATOM   526  N  N     . ILE A 1 92  ? 20.978  7.962   40.798  1.00 44.42  ? 64  ILE A N     1 
ATOM   527  C  CA    . ILE A 1 92  ? 20.158  6.777   41.050  1.00 46.57  ? 64  ILE A CA    1 
ATOM   528  C  C     . ILE A 1 92  ? 20.067  5.912   39.797  1.00 43.46  ? 64  ILE A C     1 
ATOM   529  O  O     . ILE A 1 92  ? 20.248  4.688   39.853  1.00 47.00  ? 64  ILE A O     1 
ATOM   530  C  CB    . ILE A 1 92  ? 18.764  7.197   41.556  1.00 45.42  ? 64  ILE A CB    1 
ATOM   531  C  CG1   . ILE A 1 92  ? 18.872  7.764   42.979  1.00 44.67  ? 64  ILE A CG1   1 
ATOM   532  C  CG2   . ILE A 1 92  ? 17.787  6.028   41.504  1.00 41.33  ? 64  ILE A CG2   1 
ATOM   533  C  CD1   . ILE A 1 92  ? 17.640  8.508   43.438  1.00 42.55  ? 64  ILE A CD1   1 
ATOM   534  N  N     . LEU A 1 93  ? 19.796  6.533   38.647  1.00 35.44  ? 65  LEU A N     1 
ATOM   535  C  CA    . LEU A 1 93  ? 19.738  5.777   37.391  1.00 48.10  ? 65  LEU A CA    1 
ATOM   536  C  C     . LEU A 1 93  ? 20.990  4.931   37.174  1.00 49.02  ? 65  LEU A C     1 
ATOM   537  O  O     . LEU A 1 93  ? 20.901  3.787   36.706  1.00 48.59  ? 65  LEU A O     1 
ATOM   538  C  CB    . LEU A 1 93  ? 19.540  6.727   36.212  1.00 46.97  ? 65  LEU A CB    1 
ATOM   539  C  CG    . LEU A 1 93  ? 18.179  7.416   36.149  1.00 48.83  ? 65  LEU A CG    1 
ATOM   540  C  CD1   . LEU A 1 93  ? 18.186  8.529   35.109  1.00 52.22  ? 65  LEU A CD1   1 
ATOM   541  C  CD2   . LEU A 1 93  ? 17.073  6.406   35.864  1.00 42.12  ? 65  LEU A CD2   1 
ATOM   542  N  N     . ALA A 1 94  ? 22.162  5.467   37.541  1.00 38.37  ? 66  ALA A N     1 
ATOM   543  C  CA    . ALA A 1 94  ? 23.454  4.814   37.351  1.00 48.38  ? 66  ALA A CA    1 
ATOM   544  C  C     . ALA A 1 94  ? 23.789  3.768   38.410  1.00 50.04  ? 66  ALA A C     1 
ATOM   545  O  O     . ALA A 1 94  ? 24.761  3.025   38.227  1.00 51.92  ? 66  ALA A O     1 
ATOM   546  C  CB    . ALA A 1 94  ? 24.576  5.861   37.335  1.00 42.76  ? 66  ALA A CB    1 
ATOM   547  N  N     . ASP A 1 95  ? 23.046  3.701   39.517  1.00 47.57  ? 67  ASP A N     1 
ATOM   548  C  CA    . ASP A 1 95  ? 23.366  2.748   40.575  1.00 45.93  ? 67  ASP A CA    1 
ATOM   549  C  C     . ASP A 1 95  ? 23.170  1.311   40.078  1.00 54.75  ? 67  ASP A C     1 
ATOM   550  O  O     . ASP A 1 95  ? 22.076  0.929   39.643  1.00 50.50  ? 67  ASP A O     1 
ATOM   551  C  CB    . ASP A 1 95  ? 22.508  3.031   41.806  1.00 38.06  ? 67  ASP A CB    1 
ATOM   552  C  CG    . ASP A 1 95  ? 22.993  2.317   43.023  1.00 36.97  ? 67  ASP A CG    1 
ATOM   553  O  OD1   . ASP A 1 95  ? 23.209  1.088   42.961  1.00 42.35  ? 67  ASP A OD1   1 
ATOM   554  O  OD2   . ASP A 1 95  ? 23.158  2.979   44.073  1.00 47.54  ? 67  ASP A OD2   1 
ATOM   555  N  N     . GLU A 1 96  ? 24.234  0.507   40.166  1.00 53.56  ? 68  GLU A N     1 
ATOM   556  C  CA    . GLU A 1 96  ? 24.206  -0.857  39.643  1.00 57.67  ? 68  GLU A CA    1 
ATOM   557  C  C     . GLU A 1 96  ? 23.254  -1.763  40.402  1.00 54.12  ? 68  GLU A C     1 
ATOM   558  O  O     . GLU A 1 96  ? 22.881  -2.822  39.883  1.00 50.68  ? 68  GLU A O     1 
ATOM   559  C  CB    . GLU A 1 96  ? 25.608  -1.475  39.682  1.00 53.16  ? 68  GLU A CB    1 
ATOM   560  C  CG    . GLU A 1 96  ? 26.691  -0.593  39.073  1.00 74.96  ? 68  GLU A CG    1 
ATOM   561  C  CD    . GLU A 1 96  ? 27.997  -1.343  38.821  1.00 88.10  ? 68  GLU A CD    1 
ATOM   562  O  OE1   . GLU A 1 96  ? 28.874  -1.349  39.718  1.00 79.26  ? 68  GLU A OE1   1 
ATOM   563  O  OE2   . GLU A 1 96  ? 28.136  -1.934  37.726  1.00 89.44  ? 68  GLU A OE2   1 
ATOM   564  N  N     . ARG A 1 97  ? 22.859  -1.378  41.614  1.00 53.42  ? 69  ARG A N     1 
ATOM   565  C  CA    . ARG A 1 97  ? 22.136  -2.274  42.503  1.00 47.86  ? 69  ARG A CA    1 
ATOM   566  C  C     . ARG A 1 97  ? 20.661  -2.421  42.139  1.00 47.95  ? 69  ARG A C     1 
ATOM   567  O  O     . ARG A 1 97  ? 19.972  -3.263  42.735  1.00 41.57  ? 69  ARG A O     1 
ATOM   568  C  CB    . ARG A 1 97  ? 22.295  -1.783  43.943  1.00 44.96  ? 69  ARG A CB    1 
ATOM   569  C  CG    . ARG A 1 97  ? 23.740  -1.795  44.401  1.00 47.38  ? 69  ARG A CG    1 
ATOM   570  C  CD    . ARG A 1 97  ? 23.900  -1.117  45.731  1.00 45.42  ? 69  ARG A CD    1 
ATOM   571  N  NE    . ARG A 1 97  ? 23.593  0.309   45.666  1.00 44.95  ? 69  ARG A NE    1 
ATOM   572  C  CZ    . ARG A 1 97  ? 23.895  1.161   46.636  1.00 37.53  ? 69  ARG A CZ    1 
ATOM   573  N  NH1   . ARG A 1 97  ? 24.498  0.755   47.742  1.00 34.05  ? 69  ARG A NH1   1 
ATOM   574  N  NH2   . ARG A 1 97  ? 23.586  2.448   46.494  1.00 38.32  ? 69  ARG A NH2   1 
ATOM   575  N  N     . HIS A 1 98  ? 20.160  -1.650  41.173  1.00 42.12  ? 70  HIS A N     1 
ATOM   576  C  CA    . HIS A 1 98  ? 18.821  -1.909  40.672  1.00 47.35  ? 70  HIS A CA    1 
ATOM   577  C  C     . HIS A 1 98  ? 18.755  -1.621  39.174  1.00 53.05  ? 70  HIS A C     1 
ATOM   578  O  O     . HIS A 1 98  ? 19.630  -0.964  38.599  1.00 48.35  ? 70  HIS A O     1 
ATOM   579  C  CB    . HIS A 1 98  ? 17.761  -1.117  41.464  1.00 41.13  ? 70  HIS A CB    1 
ATOM   580  C  CG    . HIS A 1 98  ? 17.869  0.368   41.333  1.00 42.69  ? 70  HIS A CG    1 
ATOM   581  N  ND1   . HIS A 1 98  ? 16.902  1.223   41.820  1.00 38.73  ? 70  HIS A ND1   1 
ATOM   582  C  CD2   . HIS A 1 98  ? 18.808  1.153   40.755  1.00 36.92  ? 70  HIS A CD2   1 
ATOM   583  C  CE1   . HIS A 1 98  ? 17.253  2.471   41.567  1.00 38.58  ? 70  HIS A CE1   1 
ATOM   584  N  NE2   . HIS A 1 98  ? 18.404  2.456   40.919  1.00 41.06  ? 70  HIS A NE2   1 
ATOM   585  N  N     . THR A 1 99  ? 17.686  -2.130  38.553  1.00 48.16  ? 71  THR A N     1 
ATOM   586  C  CA    . THR A 1 99  ? 17.484  -2.098  37.112  1.00 48.79  ? 71  THR A CA    1 
ATOM   587  C  C     . THR A 1 99  ? 16.020  -1.823  36.799  1.00 51.87  ? 71  THR A C     1 
ATOM   588  O  O     . THR A 1 99  ? 15.157  -1.803  37.688  1.00 45.36  ? 71  THR A O     1 
ATOM   589  C  CB    . THR A 1 99  ? 17.930  -3.418  36.451  1.00 49.81  ? 71  THR A CB    1 
ATOM   590  O  OG1   . THR A 1 99  ? 18.185  -3.203  35.058  1.00 53.58  ? 71  THR A OG1   1 
ATOM   591  C  CG2   . THR A 1 99  ? 16.885  -4.511  36.625  1.00 53.28  ? 71  THR A CG2   1 
ATOM   592  N  N     . ASP A 1 100 ? 15.759  -1.619  35.507  1.00 48.23  ? 72  ASP A N     1 
ATOM   593  C  CA    . ASP A 1 100 ? 14.427  -1.374  34.969  1.00 44.45  ? 72  ASP A CA    1 
ATOM   594  C  C     . ASP A 1 100 ? 13.728  -0.246  35.719  1.00 50.64  ? 72  ASP A C     1 
ATOM   595  O  O     . ASP A 1 100 ? 12.593  -0.382  36.182  1.00 47.27  ? 72  ASP A O     1 
ATOM   596  C  CB    . ASP A 1 100 ? 13.591  -2.652  34.991  1.00 58.48  ? 72  ASP A CB    1 
ATOM   597  C  CG    . ASP A 1 100 ? 14.286  -3.792  34.297  1.00 59.92  ? 72  ASP A CG    1 
ATOM   598  O  OD1   . ASP A 1 100 ? 15.227  -3.511  33.527  1.00 61.55  ? 72  ASP A OD1   1 
ATOM   599  O  OD2   . ASP A 1 100 ? 13.883  -4.957  34.494  1.00 63.35  ? 72  ASP A OD2   1 
ATOM   600  N  N     . ILE A 1 101 ? 14.426  0.880   35.835  1.00 43.10  ? 73  ILE A N     1 
ATOM   601  C  CA    . ILE A 1 101 ? 13.923  2.019   36.591  1.00 50.13  ? 73  ILE A CA    1 
ATOM   602  C  C     . ILE A 1 101 ? 12.907  2.776   35.745  1.00 49.15  ? 73  ILE A C     1 
ATOM   603  O  O     . ILE A 1 101 ? 13.254  3.322   34.693  1.00 54.34  ? 73  ILE A O     1 
ATOM   604  C  CB    . ILE A 1 101 ? 15.069  2.939   37.025  1.00 36.70  ? 73  ILE A CB    1 
ATOM   605  C  CG1   . ILE A 1 101 ? 16.101  2.161   37.852  1.00 43.33  ? 73  ILE A CG1   1 
ATOM   606  C  CG2   . ILE A 1 101 ? 14.526  4.117   37.813  1.00 39.99  ? 73  ILE A CG2   1 
ATOM   607  C  CD1   . ILE A 1 101 ? 17.537  2.677   37.686  1.00 46.34  ? 73  ILE A CD1   1 
ATOM   608  N  N     . LEU A 1 102 ? 11.657  2.830   36.220  1.00 41.78  ? 74  LEU A N     1 
ATOM   609  C  CA    . LEU A 1 102 ? 10.552  3.473   35.515  1.00 44.71  ? 74  LEU A CA    1 
ATOM   610  C  C     . LEU A 1 102 ? 9.954   4.586   36.369  1.00 41.06  ? 74  LEU A C     1 
ATOM   611  O  O     . LEU A 1 102 ? 9.409   4.322   37.447  1.00 40.59  ? 74  LEU A O     1 
ATOM   612  C  CB    . LEU A 1 102 ? 9.471   2.450   35.161  1.00 42.78  ? 74  LEU A CB    1 
ATOM   613  C  CG    . LEU A 1 102 ? 8.264   3.092   34.475  1.00 48.39  ? 74  LEU A CG    1 
ATOM   614  C  CD1   . LEU A 1 102 ? 8.631   3.485   33.043  1.00 50.63  ? 74  LEU A CD1   1 
ATOM   615  C  CD2   . LEU A 1 102 ? 7.062   2.157   34.496  1.00 46.25  ? 74  LEU A CD2   1 
ATOM   616  N  N     . CYS A 1 103 ? 10.031  5.820   35.877  1.00 40.11  ? 75  CYS A N     1 
ATOM   617  C  CA    . CYS A 1 103 ? 9.415   6.968   36.544  1.00 38.93  ? 75  CYS A CA    1 
ATOM   618  C  C     . CYS A 1 103 ? 7.909   6.984   36.288  1.00 45.65  ? 75  CYS A C     1 
ATOM   619  O  O     . CYS A 1 103 ? 7.465   7.219   35.158  1.00 39.47  ? 75  CYS A O     1 
ATOM   620  C  CB    . CYS A 1 103 ? 10.050  8.264   36.057  1.00 39.83  ? 75  CYS A CB    1 
ATOM   621  S  SG    . CYS A 1 103 ? 9.252   9.750   36.683  1.00 49.48  ? 75  CYS A SG    1 
ATOM   622  N  N     . LEU A 1 104 ? 7.117   6.779   37.344  1.00 37.41  ? 76  LEU A N     1 
ATOM   623  C  CA    . LEU A 1 104 ? 5.662   6.768   37.211  1.00 38.52  ? 76  LEU A CA    1 
ATOM   624  C  C     . LEU A 1 104 ? 5.072   8.169   37.156  1.00 43.01  ? 76  LEU A C     1 
ATOM   625  O  O     . LEU A 1 104 ? 4.055   8.389   36.489  1.00 42.54  ? 76  LEU A O     1 
ATOM   626  C  CB    . LEU A 1 104 ? 5.028   6.010   38.375  1.00 42.51  ? 76  LEU A CB    1 
ATOM   627  C  CG    . LEU A 1 104 ? 5.483   4.572   38.555  1.00 41.83  ? 76  LEU A CG    1 
ATOM   628  C  CD1   . LEU A 1 104 ? 4.918   4.019   39.841  1.00 38.48  ? 76  LEU A CD1   1 
ATOM   629  C  CD2   . LEU A 1 104 ? 5.053   3.761   37.364  1.00 42.11  ? 76  LEU A CD2   1 
ATOM   630  N  N     . LYS A 1 105 ? 5.674   9.122   37.852  1.00 43.24  ? 77  LYS A N     1 
ATOM   631  C  CA    . LYS A 1 105 ? 5.090   10.447  37.959  1.00 40.37  ? 77  LYS A CA    1 
ATOM   632  C  C     . LYS A 1 105 ? 6.206   11.447  38.150  1.00 38.70  ? 77  LYS A C     1 
ATOM   633  O  O     . LYS A 1 105 ? 7.147   11.191  38.904  1.00 40.67  ? 77  LYS A O     1 
ATOM   634  C  CB    . LYS A 1 105 ? 4.116   10.544  39.134  1.00 39.45  ? 77  LYS A CB    1 
ATOM   635  C  CG    . LYS A 1 105 ? 3.493   11.912  39.277  1.00 37.69  ? 77  LYS A CG    1 
ATOM   636  C  CD    . LYS A 1 105 ? 2.604   11.982  40.489  1.00 45.65  ? 77  LYS A CD    1 
ATOM   637  C  CE    . LYS A 1 105 ? 1.241   11.455  40.187  1.00 50.62  ? 77  LYS A CE    1 
ATOM   638  N  NZ    . LYS A 1 105 ? 0.268   11.945  41.201  1.00 59.16  ? 77  LYS A NZ    1 
ATOM   639  N  N     . SER A 1 106 ? 6.084   12.594  37.496  1.00 41.82  ? 78  SER A N     1 
ATOM   640  C  CA    . SER A 1 106 ? 7.051   13.673  37.651  1.00 41.12  ? 78  SER A CA    1 
ATOM   641  C  C     . SER A 1 106 ? 6.283   14.973  37.819  1.00 45.90  ? 78  SER A C     1 
ATOM   642  O  O     . SER A 1 106 ? 5.699   15.473  36.854  1.00 53.53  ? 78  SER A O     1 
ATOM   643  C  CB    . SER A 1 106 ? 7.996   13.748  36.453  1.00 42.69  ? 78  SER A CB    1 
ATOM   644  O  OG    . SER A 1 106 ? 8.753   14.933  36.512  1.00 52.12  ? 78  SER A OG    1 
ATOM   645  N  N     . GLU A 1 107 ? 6.281   15.521  39.032  1.00 41.53  ? 79  GLU A N     1 
ATOM   646  C  CA    . GLU A 1 107 ? 5.571   16.756  39.329  1.00 41.59  ? 79  GLU A CA    1 
ATOM   647  C  C     . GLU A 1 107 ? 6.541   17.926  39.318  1.00 51.21  ? 79  GLU A C     1 
ATOM   648  O  O     . GLU A 1 107 ? 7.659   17.825  39.831  1.00 52.78  ? 79  GLU A O     1 
ATOM   649  C  CB    . GLU A 1 107 ? 4.869   16.681  40.688  1.00 44.67  ? 79  GLU A CB    1 
ATOM   650  C  CG    . GLU A 1 107 ? 3.838   15.572  40.814  1.00 48.14  ? 79  GLU A CG    1 
ATOM   651  C  CD    . GLU A 1 107 ? 3.504   15.246  42.268  1.00 49.02  ? 79  GLU A CD    1 
ATOM   652  O  OE1   . GLU A 1 107 ? 2.705   15.993  42.870  1.00 39.74  ? 79  GLU A OE1   1 
ATOM   653  O  OE2   . GLU A 1 107 ? 4.066   14.261  42.812  1.00 42.18  ? 79  GLU A OE2   1 
ATOM   654  N  N     . VAL A 1 108 ? 6.110   19.031  38.717  1.00 54.84  ? 80  VAL A N     1 
ATOM   655  C  CA    . VAL A 1 108 ? 6.878   20.265  38.692  1.00 51.24  ? 80  VAL A CA    1 
ATOM   656  C  C     . VAL A 1 108 ? 6.060   21.339  39.390  1.00 56.55  ? 80  VAL A C     1 
ATOM   657  O  O     . VAL A 1 108 ? 4.858   21.180  39.628  1.00 56.43  ? 80  VAL A O     1 
ATOM   658  C  CB    . VAL A 1 108 ? 7.250   20.696  37.258  1.00 67.19  ? 80  VAL A CB    1 
ATOM   659  C  CG1   . VAL A 1 108 ? 8.138   19.643  36.598  1.00 56.29  ? 80  VAL A CG1   1 
ATOM   660  C  CG2   . VAL A 1 108 ? 5.984   20.932  36.432  1.00 50.41  ? 80  VAL A CG2   1 
ATOM   661  N  N     . GLU A 1 109 ? 6.733   22.440  39.729  1.00 59.34  ? 81  GLU A N     1 
ATOM   662  C  CA    . GLU A 1 109 ? 6.106   23.556  40.437  1.00 62.08  ? 81  GLU A CA    1 
ATOM   663  C  C     . GLU A 1 109 ? 5.276   23.054  41.616  1.00 56.87  ? 81  GLU A C     1 
ATOM   664  O  O     . GLU A 1 109 ? 4.096   23.378  41.762  1.00 55.73  ? 81  GLU A O     1 
ATOM   665  C  CB    . GLU A 1 109 ? 5.244   24.395  39.491  1.00 72.84  ? 81  GLU A CB    1 
ATOM   666  C  CG    . GLU A 1 109 ? 6.016   25.229  38.473  1.00 77.47  ? 81  GLU A CG    1 
ATOM   667  C  CD    . GLU A 1 109 ? 5.103   25.806  37.396  1.00 91.70  ? 81  GLU A CD    1 
ATOM   668  O  OE1   . GLU A 1 109 ? 4.374   25.020  36.745  1.00 86.18  ? 81  GLU A OE1   1 
ATOM   669  O  OE2   . GLU A 1 109 ? 5.097   27.046  37.216  1.00 93.74  ? 81  GLU A OE2   1 
ATOM   670  N  N     . VAL A 1 110 ? 5.901   22.231  42.452  1.00 51.53  ? 82  VAL A N     1 
ATOM   671  C  CA    . VAL A 1 110 ? 5.206   21.628  43.584  1.00 50.20  ? 82  VAL A CA    1 
ATOM   672  C  C     . VAL A 1 110 ? 5.096   22.653  44.704  1.00 49.08  ? 82  VAL A C     1 
ATOM   673  O  O     . VAL A 1 110 ? 6.081   23.311  45.060  1.00 52.53  ? 82  VAL A O     1 
ATOM   674  C  CB    . VAL A 1 110 ? 5.936   20.363  44.055  1.00 52.39  ? 82  VAL A CB    1 
ATOM   675  C  CG1   . VAL A 1 110 ? 5.564   20.042  45.490  1.00 52.33  ? 82  VAL A CG1   1 
ATOM   676  C  CG2   . VAL A 1 110 ? 5.620   19.201  43.126  1.00 49.28  ? 82  VAL A CG2   1 
ATOM   677  N  N     . GLN A 1 111 ? 3.893   22.798  45.262  1.00 49.16  ? 83  GLN A N     1 
ATOM   678  C  CA    . GLN A 1 111 ? 3.679   23.844  46.257  1.00 53.78  ? 83  GLN A CA    1 
ATOM   679  C  C     . GLN A 1 111 ? 4.220   23.464  47.636  1.00 60.39  ? 83  GLN A C     1 
ATOM   680  O  O     . GLN A 1 111 ? 4.802   24.312  48.324  1.00 57.58  ? 83  GLN A O     1 
ATOM   681  C  CB    . GLN A 1 111 ? 2.194   24.196  46.326  1.00 57.13  ? 83  GLN A CB    1 
ATOM   682  C  CG    . GLN A 1 111 ? 1.715   25.036  45.141  1.00 66.24  ? 83  GLN A CG    1 
ATOM   683  C  CD    . GLN A 1 111 ? 2.850   25.819  44.493  1.00 65.01  ? 83  GLN A CD    1 
ATOM   684  O  OE1   . GLN A 1 111 ? 3.405   25.406  43.473  1.00 67.09  ? 83  GLN A OE1   1 
ATOM   685  N  NE2   . GLN A 1 111 ? 3.205   26.954  45.091  1.00 65.79  ? 83  GLN A NE2   1 
ATOM   686  N  N     . GLU A 1 112 ? 4.041   22.215  48.071  1.00 60.28  ? 84  GLU A N     1 
ATOM   687  C  CA    . GLU A 1 112 ? 4.555   21.823  49.376  1.00 57.79  ? 84  GLU A CA    1 
ATOM   688  C  C     . GLU A 1 112 ? 4.978   20.362  49.359  1.00 50.42  ? 84  GLU A C     1 
ATOM   689  O  O     . GLU A 1 112 ? 4.519   19.564  48.537  1.00 43.63  ? 84  GLU A O     1 
ATOM   690  C  CB    . GLU A 1 112 ? 3.539   22.054  50.505  1.00 62.79  ? 84  GLU A CB    1 
ATOM   691  C  CG    . GLU A 1 112 ? 2.406   21.060  50.577  1.00 59.30  ? 84  GLU A CG    1 
ATOM   692  C  CD    . GLU A 1 112 ? 1.123   21.579  49.943  1.00 84.68  ? 84  GLU A CD    1 
ATOM   693  O  OE1   . GLU A 1 112 ? 1.208   22.422  49.022  1.00 81.89  ? 84  GLU A OE1   1 
ATOM   694  O  OE2   . GLU A 1 112 ? 0.026   21.153  50.381  1.00 94.05  ? 84  GLU A OE2   1 
ATOM   695  N  N     . ARG A 1 113 ? 5.859   20.024  50.301  1.00 39.20  ? 85  ARG A N     1 
ATOM   696  C  CA    . ARG A 1 113 ? 6.410   18.683  50.406  1.00 38.22  ? 85  ARG A CA    1 
ATOM   697  C  C     . ARG A 1 113 ? 5.388   17.713  50.985  1.00 35.50  ? 85  ARG A C     1 
ATOM   698  O  O     . ARG A 1 113 ? 4.561   18.077  51.826  1.00 44.05  ? 85  ARG A O     1 
ATOM   699  C  CB    . ARG A 1 113 ? 7.666   18.690  51.283  1.00 39.77  ? 85  ARG A CB    1 
ATOM   700  C  CG    . ARG A 1 113 ? 8.765   19.597  50.767  1.00 36.40  ? 85  ARG A CG    1 
ATOM   701  C  CD    . ARG A 1 113 ? 9.888   19.779  51.766  1.00 41.91  ? 85  ARG A CD    1 
ATOM   702  N  NE    . ARG A 1 113 ? 10.959  20.564  51.161  1.00 42.88  ? 85  ARG A NE    1 
ATOM   703  C  CZ    . ARG A 1 113 ? 12.023  20.046  50.562  1.00 39.70  ? 85  ARG A CZ    1 
ATOM   704  N  NH1   . ARG A 1 113 ? 12.233  18.739  50.532  1.00 35.89  ? 85  ARG A NH1   1 
ATOM   705  N  NH2   . ARG A 1 113 ? 12.889  20.859  49.964  1.00 41.03  ? 85  ARG A NH2   1 
ATOM   706  N  N     . MET A 1 114 ? 5.451   16.464  50.519  1.00 33.73  ? 86  MET A N     1 
ATOM   707  C  CA    . MET A 1 114 ? 4.669   15.408  51.150  1.00 34.88  ? 86  MET A CA    1 
ATOM   708  C  C     . MET A 1 114 ? 5.354   14.868  52.397  1.00 41.52  ? 86  MET A C     1 
ATOM   709  O  O     . MET A 1 114 ? 4.674   14.419  53.324  1.00 35.40  ? 86  MET A O     1 
ATOM   710  C  CB    . MET A 1 114 ? 4.435   14.253  50.186  1.00 35.12  ? 86  MET A CB    1 
ATOM   711  C  CG    . MET A 1 114 ? 3.039   14.242  49.560  1.00 45.52  ? 86  MET A CG    1 
ATOM   712  S  SD    . MET A 1 114 ? 2.983   13.351  47.986  1.00 56.32  ? 86  MET A SD    1 
ATOM   713  C  CE    . MET A 1 114 ? 1.333   13.818  47.393  1.00 37.30  ? 86  MET A CE    1 
ATOM   714  N  N     . PHE A 1 115 ? 6.685   14.898  52.439  1.00 30.10  ? 87  PHE A N     1 
ATOM   715  C  CA    . PHE A 1 115 ? 7.453   14.226  53.481  1.00 31.18  ? 87  PHE A CA    1 
ATOM   716  C  C     . PHE A 1 115 ? 8.465   15.188  54.099  1.00 28.79  ? 87  PHE A C     1 
ATOM   717  O  O     . PHE A 1 115 ? 9.664   14.906  54.141  1.00 28.21  ? 87  PHE A O     1 
ATOM   718  C  CB    . PHE A 1 115 ? 8.121   12.980  52.896  1.00 27.69  ? 87  PHE A CB    1 
ATOM   719  C  CG    . PHE A 1 115 ? 7.161   12.083  52.140  1.00 35.06  ? 87  PHE A CG    1 
ATOM   720  C  CD1   . PHE A 1 115 ? 6.181   11.365  52.827  1.00 28.23  ? 87  PHE A CD1   1 
ATOM   721  C  CD2   . PHE A 1 115 ? 7.224   11.960  50.754  1.00 30.99  ? 87  PHE A CD2   1 
ATOM   722  C  CE1   . PHE A 1 115 ? 5.292   10.525  52.160  1.00 26.88  ? 87  PHE A CE1   1 
ATOM   723  C  CE2   . PHE A 1 115 ? 6.332   11.121  50.066  1.00 28.52  ? 87  PHE A CE2   1 
ATOM   724  C  CZ    . PHE A 1 115 ? 5.377   10.396  50.770  1.00 30.65  ? 87  PHE A CZ    1 
ATOM   725  N  N     . PRO A 1 116 ? 8.001   16.334  54.619  1.00 33.82  ? 88  PRO A N     1 
ATOM   726  C  CA    . PRO A 1 116 ? 8.948   17.405  55.000  1.00 33.05  ? 88  PRO A CA    1 
ATOM   727  C  C     . PRO A 1 116 ? 9.976   17.007  56.052  1.00 35.67  ? 88  PRO A C     1 
ATOM   728  O  O     . PRO A 1 116 ? 11.085  17.559  56.057  1.00 34.45  ? 88  PRO A O     1 
ATOM   729  C  CB    . PRO A 1 116 ? 8.022   18.516  55.511  1.00 29.56  ? 88  PRO A CB    1 
ATOM   730  C  CG    . PRO A 1 116 ? 6.792   17.800  55.954  1.00 29.76  ? 88  PRO A CG    1 
ATOM   731  C  CD    . PRO A 1 116 ? 6.613   16.670  54.992  1.00 32.33  ? 88  PRO A CD    1 
ATOM   732  N  N     . ASP A 1 117 ? 9.664   16.064  56.935  1.00 30.15  ? 89  ASP A N     1 
ATOM   733  C  CA    . ASP A 1 117 ? 10.607  15.680  57.977  1.00 34.21  ? 89  ASP A CA    1 
ATOM   734  C  C     . ASP A 1 117 ? 11.396  14.428  57.633  1.00 35.16  ? 89  ASP A C     1 
ATOM   735  O  O     . ASP A 1 117 ? 12.111  13.909  58.485  1.00 29.21  ? 89  ASP A O     1 
ATOM   736  C  CB    . ASP A 1 117 ? 9.865   15.508  59.298  1.00 36.12  ? 89  ASP A CB    1 
ATOM   737  C  CG    . ASP A 1 117 ? 9.168   16.780  59.714  1.00 38.79  ? 89  ASP A CG    1 
ATOM   738  O  OD1   . ASP A 1 117 ? 9.862   17.822  59.756  1.00 41.22  ? 89  ASP A OD1   1 
ATOM   739  O  OD2   . ASP A 1 117 ? 7.941   16.750  59.932  1.00 40.62  ? 89  ASP A OD2   1 
ATOM   740  N  N     . TRP A 1 118 ? 11.282  13.924  56.410  1.00 24.78  ? 90  TRP A N     1 
ATOM   741  C  CA    . TRP A 1 118 ? 11.956  12.689  56.012  1.00 25.22  ? 90  TRP A CA    1 
ATOM   742  C  C     . TRP A 1 118 ? 12.997  13.026  54.952  1.00 29.26  ? 90  TRP A C     1 
ATOM   743  O  O     . TRP A 1 118 ? 12.669  13.077  53.768  1.00 33.24  ? 90  TRP A O     1 
ATOM   744  C  CB    . TRP A 1 118 ? 10.949  11.654  55.460  1.00 24.74  ? 90  TRP A CB    1 
ATOM   745  C  CG    . TRP A 1 118 ? 9.903   11.179  56.409  1.00 30.72  ? 90  TRP A CG    1 
ATOM   746  C  CD1   . TRP A 1 118 ? 9.798   11.458  57.748  1.00 26.01  ? 90  TRP A CD1   1 
ATOM   747  C  CD2   . TRP A 1 118 ? 8.811   10.303  56.095  1.00 27.91  ? 90  TRP A CD2   1 
ATOM   748  N  NE1   . TRP A 1 118 ? 8.703   10.823  58.277  1.00 25.47  ? 90  TRP A NE1   1 
ATOM   749  C  CE2   . TRP A 1 118 ? 8.080   10.102  57.287  1.00 29.26  ? 90  TRP A CE2   1 
ATOM   750  C  CE3   . TRP A 1 118 ? 8.383   9.668   54.919  1.00 26.76  ? 90  TRP A CE3   1 
ATOM   751  C  CZ2   . TRP A 1 118 ? 6.934   9.288   57.340  1.00 27.67  ? 90  TRP A CZ2   1 
ATOM   752  C  CZ3   . TRP A 1 118 ? 7.239   8.841   54.976  1.00 29.86  ? 90  TRP A CZ3   1 
ATOM   753  C  CH2   . TRP A 1 118 ? 6.529   8.674   56.176  1.00 28.03  ? 90  TRP A CH2   1 
ATOM   754  N  N     . SER A 1 119 ? 14.249  13.259  55.353  1.00 32.27  ? 91  SER A N     1 
ATOM   755  C  CA    . SER A 1 119 ? 15.292  13.368  54.339  1.00 29.02  ? 91  SER A CA    1 
ATOM   756  C  C     . SER A 1 119 ? 15.312  12.113  53.478  1.00 28.80  ? 91  SER A C     1 
ATOM   757  O  O     . SER A 1 119 ? 15.372  12.194  52.248  1.00 27.08  ? 91  SER A O     1 
ATOM   758  C  CB    . SER A 1 119 ? 16.659  13.610  54.989  1.00 24.42  ? 91  SER A CB    1 
ATOM   759  O  OG    . SER A 1 119 ? 16.674  14.864  55.659  1.00 28.94  ? 91  SER A OG    1 
ATOM   760  N  N     . MET A 1 120 ? 15.289  10.940  54.111  1.00 26.82  ? 92  MET A N     1 
ATOM   761  C  CA    . MET A 1 120 ? 14.884  9.711   53.432  1.00 29.18  ? 92  MET A CA    1 
ATOM   762  C  C     . MET A 1 120 ? 14.358  8.757   54.496  1.00 30.21  ? 92  MET A C     1 
ATOM   763  O  O     . MET A 1 120 ? 15.117  8.329   55.366  1.00 30.91  ? 92  MET A O     1 
ATOM   764  C  CB    . MET A 1 120 ? 16.025  9.032   52.657  1.00 30.74  ? 92  MET A CB    1 
ATOM   765  C  CG    . MET A 1 120 ? 15.506  7.815   51.849  1.00 33.56  ? 92  MET A CG    1 
ATOM   766  S  SD    . MET A 1 120 ? 14.018  8.022   50.797  1.00 35.47  ? 92  MET A SD    1 
ATOM   767  C  CE    . MET A 1 120 ? 14.095  9.709   50.188  1.00 32.54  ? 92  MET A CE    1 
ATOM   768  N  N     . GLN A 1 121 ? 13.074  8.413   54.430  1.00 29.28  ? 93  GLN A N     1 
ATOM   769  C  CA    . GLN A 1 121 ? 12.497  7.400   55.317  1.00 27.93  ? 93  GLN A CA    1 
ATOM   770  C  C     . GLN A 1 121 ? 12.455  6.066   54.596  1.00 29.32  ? 93  GLN A C     1 
ATOM   771  O  O     . GLN A 1 121 ? 11.959  5.985   53.470  1.00 32.74  ? 93  GLN A O     1 
ATOM   772  C  CB    . GLN A 1 121 ? 11.081  7.772   55.753  1.00 27.06  ? 93  GLN A CB    1 
ATOM   773  C  CG    . GLN A 1 121 ? 10.350  6.705   56.567  1.00 25.80  ? 93  GLN A CG    1 
ATOM   774  C  CD    . GLN A 1 121 ? 10.806  6.631   58.026  1.00 29.02  ? 93  GLN A CD    1 
ATOM   775  O  OE1   . GLN A 1 121 ? 11.676  7.386   58.470  1.00 26.20  ? 93  GLN A OE1   1 
ATOM   776  N  NE2   . GLN A 1 121 ? 10.219  5.707   58.772  1.00 26.44  ? 93  GLN A NE2   1 
ATOM   777  N  N     . THR A 1 122 ? 12.906  5.016   55.267  1.00 28.09  ? 94  THR A N     1 
ATOM   778  C  CA    . THR A 1 122 ? 13.024  3.696   54.670  1.00 29.25  ? 94  THR A CA    1 
ATOM   779  C  C     . THR A 1 122 ? 12.011  2.748   55.298  1.00 33.13  ? 94  THR A C     1 
ATOM   780  O  O     . THR A 1 122 ? 11.893  2.672   56.528  1.00 30.14  ? 94  THR A O     1 
ATOM   781  C  CB    . THR A 1 122 ? 14.451  3.189   54.844  1.00 33.51  ? 94  THR A CB    1 
ATOM   782  O  OG1   . THR A 1 122 ? 15.326  4.116   54.184  1.00 35.76  ? 94  THR A OG1   1 
ATOM   783  C  CG2   . THR A 1 122 ? 14.621  1.790   54.238  1.00 29.22  ? 94  THR A CG2   1 
ATOM   784  N  N     . ILE A 1 123 ? 11.249  2.061   54.452  1.00 30.16  ? 95  ILE A N     1 
ATOM   785  C  CA    . ILE A 1 123 ? 10.150  1.205   54.890  1.00 28.43  ? 95  ILE A CA    1 
ATOM   786  C  C     . ILE A 1 123 ? 10.333  -0.134  54.194  1.00 31.09  ? 95  ILE A C     1 
ATOM   787  O  O     . ILE A 1 123 ? 9.981   -0.280  53.020  1.00 28.55  ? 95  ILE A O     1 
ATOM   788  C  CB    . ILE A 1 123 ? 8.778   1.801   54.562  1.00 29.90  ? 95  ILE A CB    1 
ATOM   789  C  CG1   . ILE A 1 123 ? 8.624   3.198   55.181  1.00 27.59  ? 95  ILE A CG1   1 
ATOM   790  C  CG2   . ILE A 1 123 ? 7.667   0.877   55.034  1.00 24.50  ? 95  ILE A CG2   1 
ATOM   791  C  CD1   . ILE A 1 123 ? 7.268   3.865   54.817  1.00 24.25  ? 95  ILE A CD1   1 
ATOM   792  N  N     . ASN A 1 124 ? 10.865  -1.114  54.913  1.00 33.04  ? 96  ASN A N     1 
ATOM   793  C  CA    . ASN A 1 124 ? 11.031  -2.457  54.374  1.00 38.20  ? 96  ASN A CA    1 
ATOM   794  C  C     . ASN A 1 124 ? 9.723   -3.207  54.575  1.00 37.33  ? 96  ASN A C     1 
ATOM   795  O  O     . ASN A 1 124 ? 9.389   -3.589  55.701  1.00 33.05  ? 96  ASN A O     1 
ATOM   796  C  CB    . ASN A 1 124 ? 12.191  -3.183  55.052  1.00 34.64  ? 96  ASN A CB    1 
ATOM   797  C  CG    . ASN A 1 124 ? 12.502  -4.528  54.395  1.00 43.82  ? 96  ASN A CG    1 
ATOM   798  O  OD1   . ASN A 1 124 ? 11.600  -5.326  54.123  1.00 40.21  ? 96  ASN A OD1   1 
ATOM   799  N  ND2   . ASN A 1 124 ? 13.780  -4.781  54.132  1.00 43.99  ? 96  ASN A ND2   1 
ATOM   800  N  N     . LEU A 1 125 ? 8.981   -3.416  53.482  1.00 32.45  ? 97  LEU A N     1 
ATOM   801  C  CA    . LEU A 1 125 ? 7.701   -4.099  53.592  1.00 29.38  ? 97  LEU A CA    1 
ATOM   802  C  C     . LEU A 1 125 ? 7.848   -5.597  53.786  1.00 32.69  ? 97  LEU A C     1 
ATOM   803  O  O     . LEU A 1 125 ? 6.951   -6.221  54.359  1.00 30.93  ? 97  LEU A O     1 
ATOM   804  C  CB    . LEU A 1 125 ? 6.845   -3.814  52.361  1.00 32.03  ? 97  LEU A CB    1 
ATOM   805  C  CG    . LEU A 1 125 ? 6.463   -2.343  52.357  1.00 32.71  ? 97  LEU A CG    1 
ATOM   806  C  CD1   . LEU A 1 125 ? 5.890   -1.956  51.010  1.00 32.75  ? 97  LEU A CD1   1 
ATOM   807  C  CD2   . LEU A 1 125 ? 5.484   -2.089  53.504  1.00 28.66  ? 97  LEU A CD2   1 
ATOM   808  N  N     . ASP A 1 126 ? 8.944   -6.196  53.314  1.00 31.04  ? 98  ASP A N     1 
ATOM   809  C  CA    . ASP A 1 126 ? 9.156   -7.620  53.559  1.00 34.08  ? 98  ASP A CA    1 
ATOM   810  C  C     . ASP A 1 126 ? 9.108   -7.922  55.042  1.00 34.59  ? 98  ASP A C     1 
ATOM   811  O  O     . ASP A 1 126 ? 8.483   -8.900  55.468  1.00 45.04  ? 98  ASP A O     1 
ATOM   812  C  CB    . ASP A 1 126 ? 10.498  -8.073  52.980  1.00 29.11  ? 98  ASP A CB    1 
ATOM   813  C  CG    . ASP A 1 126 ? 10.545  -7.970  51.483  1.00 35.16  ? 98  ASP A CG    1 
ATOM   814  O  OD1   . ASP A 1 126 ? 9.619   -8.483  50.827  1.00 35.19  ? 98  ASP A OD1   1 
ATOM   815  O  OD2   . ASP A 1 126 ? 11.494  -7.337  50.956  1.00 42.77  ? 98  ASP A OD2   1 
ATOM   816  N  N     . GLU A 1 127 ? 9.755   -7.086  55.841  1.00 38.26  ? 99  GLU A N     1 
ATOM   817  C  CA    . GLU A 1 127 ? 9.809   -7.288  57.282  1.00 38.54  ? 99  GLU A CA    1 
ATOM   818  C  C     . GLU A 1 127 ? 8.567   -6.785  58.001  1.00 34.84  ? 99  GLU A C     1 
ATOM   819  O  O     . GLU A 1 127 ? 8.397   -7.071  59.189  1.00 36.57  ? 99  GLU A O     1 
ATOM   820  C  CB    . GLU A 1 127 ? 11.053  -6.600  57.841  1.00 37.69  ? 99  GLU A CB    1 
ATOM   821  C  CG    . GLU A 1 127 ? 12.338  -7.141  57.215  1.00 47.42  ? 99  GLU A CG    1 
ATOM   822  C  CD    . GLU A 1 127 ? 13.589  -6.395  57.654  1.00 46.10  ? 99  GLU A CD    1 
ATOM   823  O  OE1   . GLU A 1 127 ? 13.548  -5.715  58.703  1.00 55.21  ? 99  GLU A OE1   1 
ATOM   824  O  OE2   . GLU A 1 127 ? 14.614  -6.502  56.942  1.00 51.57  ? 99  GLU A OE2   1 
ATOM   825  N  N     . ASN A 1 128 ? 7.686   -6.064  57.330  1.00 32.95  ? 100 ASN A N     1 
ATOM   826  C  CA    . ASN A 1 128 ? 6.523   -5.550  58.035  1.00 37.26  ? 100 ASN A CA    1 
ATOM   827  C  C     . ASN A 1 128 ? 5.483   -6.654  58.159  1.00 31.04  ? 100 ASN A C     1 
ATOM   828  O  O     . ASN A 1 128 ? 5.204   -7.358  57.186  1.00 36.53  ? 100 ASN A O     1 
ATOM   829  C  CB    . ASN A 1 128 ? 5.943   -4.339  57.314  1.00 38.50  ? 100 ASN A CB    1 
ATOM   830  C  CG    . ASN A 1 128 ? 4.888   -3.636  58.142  1.00 37.97  ? 100 ASN A CG    1 
ATOM   831  O  OD1   . ASN A 1 128 ? 3.749   -4.104  58.239  1.00 32.90  ? 100 ASN A OD1   1 
ATOM   832  N  ND2   . ASN A 1 128 ? 5.265   -2.516  58.761  1.00 28.82  ? 100 ASN A ND2   1 
ATOM   833  N  N     . THR A 1 129 ? 4.923   -6.814  59.360  1.00 34.91  ? 101 THR A N     1 
ATOM   834  C  CA    . THR A 1 129 ? 3.900   -7.824  59.632  1.00 41.55  ? 101 THR A CA    1 
ATOM   835  C  C     . THR A 1 129 ? 2.614   -7.208  60.180  1.00 38.20  ? 101 THR A C     1 
ATOM   836  O  O     . THR A 1 129 ? 1.808   -7.915  60.780  1.00 37.59  ? 101 THR A O     1 
ATOM   837  C  CB    . THR A 1 129 ? 4.414   -8.891  60.611  1.00 43.37  ? 101 THR A CB    1 
ATOM   838  O  OG1   . THR A 1 129 ? 4.595   -8.320  61.916  1.00 43.45  ? 101 THR A OG1   1 
ATOM   839  C  CG2   . THR A 1 129 ? 5.738   -9.488  60.150  1.00 41.70  ? 101 THR A CG2   1 
ATOM   840  N  N     . ASP A 1 130 ? 2.416   -5.906  60.001  1.00 33.90  ? 102 ASP A N     1 
ATOM   841  C  CA    . ASP A 1 130 ? 1.240   -5.254  60.550  1.00 30.84  ? 102 ASP A CA    1 
ATOM   842  C  C     . ASP A 1 130 ? -0.024  -5.780  59.873  1.00 35.08  ? 102 ASP A C     1 
ATOM   843  O  O     . ASP A 1 130 ? -0.063  -6.006  58.658  1.00 31.34  ? 102 ASP A O     1 
ATOM   844  C  CB    . ASP A 1 130 ? 1.334   -3.739  60.365  1.00 26.29  ? 102 ASP A CB    1 
ATOM   845  C  CG    . ASP A 1 130 ? 2.486   -3.125  61.142  1.00 35.53  ? 102 ASP A CG    1 
ATOM   846  O  OD1   . ASP A 1 130 ? 3.081   -3.819  61.996  1.00 38.65  ? 102 ASP A OD1   1 
ATOM   847  O  OD2   . ASP A 1 130 ? 2.854   -1.971  60.833  1.00 33.16  ? 102 ASP A OD2   1 
ATOM   848  N  N     . PHE A 1 131 ? -1.075  -5.903  60.678  1.00 30.86  ? 103 PHE A N     1 
ATOM   849  C  CA    . PHE A 1 131 ? -2.327  -6.531  60.267  1.00 33.36  ? 103 PHE A CA    1 
ATOM   850  C  C     . PHE A 1 131 ? -2.899  -5.924  58.990  1.00 30.21  ? 103 PHE A C     1 
ATOM   851  O  O     . PHE A 1 131 ? -3.312  -6.647  58.079  1.00 32.70  ? 103 PHE A O     1 
ATOM   852  C  CB    . PHE A 1 131 ? -3.344  -6.392  61.399  1.00 29.07  ? 103 PHE A CB    1 
ATOM   853  C  CG    . PHE A 1 131 ? -4.667  -7.015  61.096  1.00 30.91  ? 103 PHE A CG    1 
ATOM   854  C  CD1   . PHE A 1 131 ? -4.843  -8.393  61.224  1.00 32.78  ? 103 PHE A CD1   1 
ATOM   855  C  CD2   . PHE A 1 131 ? -5.728  -6.242  60.668  1.00 31.59  ? 103 PHE A CD2   1 
ATOM   856  C  CE1   . PHE A 1 131 ? -6.069  -8.970  60.949  1.00 30.04  ? 103 PHE A CE1   1 
ATOM   857  C  CE2   . PHE A 1 131 ? -6.955  -6.816  60.407  1.00 33.53  ? 103 PHE A CE2   1 
ATOM   858  C  CZ    . PHE A 1 131 ? -7.119  -8.180  60.541  1.00 32.11  ? 103 PHE A CZ    1 
ATOM   859  N  N     . LEU A 1 132 ? -3.024  -4.596  58.949  1.00 28.88  ? 104 LEU A N     1 
ATOM   860  C  CA    . LEU A 1 132 ? -3.638  -3.954  57.802  1.00 28.79  ? 104 LEU A CA    1 
ATOM   861  C  C     . LEU A 1 132 ? -2.681  -3.851  56.620  1.00 29.74  ? 104 LEU A C     1 
ATOM   862  O  O     . LEU A 1 132 ? -3.136  -3.828  55.471  1.00 33.01  ? 104 LEU A O     1 
ATOM   863  C  CB    . LEU A 1 132 ? -4.150  -2.563  58.173  1.00 30.79  ? 104 LEU A CB    1 
ATOM   864  C  CG    . LEU A 1 132 ? -5.349  -2.499  59.134  1.00 33.92  ? 104 LEU A CG    1 
ATOM   865  C  CD1   . LEU A 1 132 ? -5.536  -1.088  59.627  1.00 40.98  ? 104 LEU A CD1   1 
ATOM   866  C  CD2   . LEU A 1 132 ? -6.628  -3.002  58.460  1.00 31.75  ? 104 LEU A CD2   1 
ATOM   867  N  N     . ILE A 1 133 ? -1.368  -3.780  56.878  1.00 26.94  ? 105 ILE A N     1 
ATOM   868  C  CA    . ILE A 1 133 ? -0.409  -3.674  55.783  1.00 30.08  ? 105 ILE A CA    1 
ATOM   869  C  C     . ILE A 1 133 ? -0.305  -4.965  54.964  1.00 28.37  ? 105 ILE A C     1 
ATOM   870  O  O     . ILE A 1 133 ? 0.061   -4.910  53.783  1.00 30.78  ? 105 ILE A O     1 
ATOM   871  C  CB    . ILE A 1 133 ? 0.964   -3.213  56.328  1.00 32.09  ? 105 ILE A CB    1 
ATOM   872  C  CG1   . ILE A 1 133 ? 0.906   -1.726  56.699  1.00 34.51  ? 105 ILE A CG1   1 
ATOM   873  C  CG2   . ILE A 1 133 ? 2.060   -3.409  55.309  1.00 28.36  ? 105 ILE A CG2   1 
ATOM   874  C  CD1   . ILE A 1 133 ? 2.215   -1.159  57.236  1.00 30.85  ? 105 ILE A CD1   1 
ATOM   875  N  N     . ARG A 1 134 ? -0.648  -6.124  55.532  1.00 23.73  ? 106 ARG A N     1 
ATOM   876  C  CA    . ARG A 1 134 ? -0.523  -7.370  54.772  1.00 27.65  ? 106 ARG A CA    1 
ATOM   877  C  C     . ARG A 1 134 ? -1.321  -7.374  53.468  1.00 30.24  ? 106 ARG A C     1 
ATOM   878  O  O     . ARG A 1 134 ? -0.724  -7.663  52.415  1.00 30.75  ? 106 ARG A O     1 
ATOM   879  C  CB    . ARG A 1 134 ? -0.876  -8.572  55.653  1.00 30.20  ? 106 ARG A CB    1 
ATOM   880  C  CG    . ARG A 1 134 ? -0.556  -9.910  54.965  1.00 39.23  ? 106 ARG A CG    1 
ATOM   881  C  CD    . ARG A 1 134 ? -0.891  -11.130 55.804  1.00 33.47  ? 106 ARG A CD    1 
ATOM   882  N  NE    . ARG A 1 134 ? -2.320  -11.355 55.990  1.00 39.42  ? 106 ARG A NE    1 
ATOM   883  C  CZ    . ARG A 1 134 ? -3.045  -12.181 55.248  1.00 40.24  ? 106 ARG A CZ    1 
ATOM   884  N  NH1   . ARG A 1 134 ? -2.547  -12.758 54.165  1.00 35.96  ? 106 ARG A NH1   1 
ATOM   885  N  NH2   . ARG A 1 134 ? -4.296  -12.437 55.604  1.00 37.03  ? 106 ARG A NH2   1 
ATOM   886  N  N     . PRO A 1 135 ? -2.633  -7.075  53.439  1.00 29.34  ? 107 PRO A N     1 
ATOM   887  C  CA    . PRO A 1 135 ? -3.328  -7.054  52.134  1.00 30.18  ? 107 PRO A CA    1 
ATOM   888  C  C     . PRO A 1 135 ? -2.877  -5.911  51.243  1.00 31.14  ? 107 PRO A C     1 
ATOM   889  O  O     . PRO A 1 135 ? -2.947  -6.022  50.015  1.00 28.37  ? 107 PRO A O     1 
ATOM   890  C  CB    . PRO A 1 135 ? -4.804  -6.909  52.521  1.00 29.19  ? 107 PRO A CB    1 
ATOM   891  C  CG    . PRO A 1 135 ? -4.752  -6.172  53.821  1.00 28.79  ? 107 PRO A CG    1 
ATOM   892  C  CD    . PRO A 1 135 ? -3.548  -6.728  54.541  1.00 29.33  ? 107 PRO A CD    1 
ATOM   893  N  N     . ILE A 1 136 ? -2.411  -4.809  51.828  1.00 30.81  ? 108 ILE A N     1 
ATOM   894  C  CA    . ILE A 1 136 ? -1.872  -3.721  51.024  1.00 31.33  ? 108 ILE A CA    1 
ATOM   895  C  C     . ILE A 1 136 ? -0.630  -4.189  50.265  1.00 30.28  ? 108 ILE A C     1 
ATOM   896  O  O     . ILE A 1 136 ? -0.446  -3.863  49.082  1.00 29.37  ? 108 ILE A O     1 
ATOM   897  C  CB    . ILE A 1 136 ? -1.578  -2.501  51.914  1.00 35.84  ? 108 ILE A CB    1 
ATOM   898  C  CG1   . ILE A 1 136 ? -2.865  -1.977  52.561  1.00 29.09  ? 108 ILE A CG1   1 
ATOM   899  C  CG2   . ILE A 1 136 ? -0.933  -1.424  51.095  1.00 38.25  ? 108 ILE A CG2   1 
ATOM   900  C  CD1   . ILE A 1 136 ? -2.599  -0.970  53.690  1.00 32.08  ? 108 ILE A CD1   1 
ATOM   901  N  N     . LYS A 1 137 ? 0.221   -4.993  50.915  1.00 31.84  ? 109 LYS A N     1 
ATOM   902  C  CA    . LYS A 1 137 ? 1.403   -5.522  50.233  1.00 33.60  ? 109 LYS A CA    1 
ATOM   903  C  C     . LYS A 1 137 ? 1.016   -6.376  49.028  1.00 35.79  ? 109 LYS A C     1 
ATOM   904  O  O     . LYS A 1 137 ? 1.617   -6.264  47.952  1.00 36.27  ? 109 LYS A O     1 
ATOM   905  C  CB    . LYS A 1 137 ? 2.263   -6.325  51.212  1.00 30.31  ? 109 LYS A CB    1 
ATOM   906  C  CG    . LYS A 1 137 ? 3.089   -5.468  52.150  1.00 30.20  ? 109 LYS A CG    1 
ATOM   907  C  CD    . LYS A 1 137 ? 3.597   -6.259  53.362  1.00 29.29  ? 109 LYS A CD    1 
ATOM   908  C  CE    . LYS A 1 137 ? 4.417   -7.481  52.968  1.00 34.15  ? 109 LYS A CE    1 
ATOM   909  N  NZ    . LYS A 1 137 ? 4.867   -8.141  54.223  1.00 28.20  ? 109 LYS A NZ    1 
ATOM   910  N  N     . VAL A 1 138 ? 0.024   -7.251  49.190  1.00 35.81  ? 110 VAL A N     1 
ATOM   911  C  CA    . VAL A 1 138 ? -0.394  -8.098  48.073  1.00 31.42  ? 110 VAL A CA    1 
ATOM   912  C  C     . VAL A 1 138 ? -0.867  -7.237  46.911  1.00 35.21  ? 110 VAL A C     1 
ATOM   913  O  O     . VAL A 1 138 ? -0.533  -7.502  45.752  1.00 35.64  ? 110 VAL A O     1 
ATOM   914  C  CB    . VAL A 1 138 ? -1.499  -9.077  48.513  1.00 32.13  ? 110 VAL A CB    1 
ATOM   915  C  CG1   . VAL A 1 138 ? -2.091  -9.768  47.283  1.00 34.36  ? 110 VAL A CG1   1 
ATOM   916  C  CG2   . VAL A 1 138 ? -0.972  -10.083 49.521  1.00 32.84  ? 110 VAL A CG2   1 
ATOM   917  N  N     . LEU A 1 139 ? -1.638  -6.182  47.210  1.00 31.70  ? 111 LEU A N     1 
ATOM   918  C  CA    . LEU A 1 139 ? -2.147  -5.264  46.188  1.00 34.87  ? 111 LEU A CA    1 
ATOM   919  C  C     . LEU A 1 139 ? -1.026  -4.462  45.532  1.00 32.24  ? 111 LEU A C     1 
ATOM   920  O  O     . LEU A 1 139 ? -1.002  -4.295  44.305  1.00 35.07  ? 111 LEU A O     1 
ATOM   921  C  CB    . LEU A 1 139 ? -3.169  -4.327  46.833  1.00 36.65  ? 111 LEU A CB    1 
ATOM   922  C  CG    . LEU A 1 139 ? -3.984  -3.322  46.045  1.00 40.55  ? 111 LEU A CG    1 
ATOM   923  C  CD1   . LEU A 1 139 ? -5.008  -4.041  45.182  1.00 43.42  ? 111 LEU A CD1   1 
ATOM   924  C  CD2   . LEU A 1 139 ? -4.674  -2.384  47.028  1.00 37.50  ? 111 LEU A CD2   1 
ATOM   925  N  N     . LEU A 1 140 ? -0.118  -3.907  46.341  1.00 34.55  ? 112 LEU A N     1 
ATOM   926  C  CA    . LEU A 1 140 ? 1.079   -3.274  45.799  1.00 34.28  ? 112 LEU A CA    1 
ATOM   927  C  C     . LEU A 1 140 ? 1.799   -4.203  44.833  1.00 31.60  ? 112 LEU A C     1 
ATOM   928  O  O     . LEU A 1 140 ? 2.178   -3.805  43.729  1.00 34.20  ? 112 LEU A O     1 
ATOM   929  C  CB    . LEU A 1 140 ? 2.026   -2.874  46.934  1.00 35.97  ? 112 LEU A CB    1 
ATOM   930  C  CG    . LEU A 1 140 ? 1.849   -1.522  47.601  1.00 37.24  ? 112 LEU A CG    1 
ATOM   931  C  CD1   . LEU A 1 140 ? 2.959   -1.354  48.649  1.00 38.51  ? 112 LEU A CD1   1 
ATOM   932  C  CD2   . LEU A 1 140 ? 1.866   -0.391  46.554  1.00 36.02  ? 112 LEU A CD2   1 
ATOM   933  N  N     . GLN A 1 141 ? 2.020   -5.450  45.243  1.00 40.31  ? 113 GLN A N     1 
ATOM   934  C  CA    . GLN A 1 141 ? 2.743   -6.369  44.373  1.00 37.67  ? 113 GLN A CA    1 
ATOM   935  C  C     . GLN A 1 141 ? 1.976   -6.591  43.074  1.00 39.62  ? 113 GLN A C     1 
ATOM   936  O  O     . GLN A 1 141 ? 2.545   -6.517  41.981  1.00 38.78  ? 113 GLN A O     1 
ATOM   937  C  CB    . GLN A 1 141 ? 2.989   -7.692  45.087  1.00 39.04  ? 113 GLN A CB    1 
ATOM   938  C  CG    . GLN A 1 141 ? 3.723   -8.681  44.209  1.00 48.18  ? 113 GLN A CG    1 
ATOM   939  C  CD    . GLN A 1 141 ? 4.980   -9.199  44.849  1.00 51.69  ? 113 GLN A CD    1 
ATOM   940  O  OE1   . GLN A 1 141 ? 4.940   -9.798  45.923  1.00 59.49  ? 113 GLN A OE1   1 
ATOM   941  N  NE2   . GLN A 1 141 ? 6.113   -8.965  44.200  1.00 54.70  ? 113 GLN A NE2   1 
ATOM   942  N  N     . THR A 1 142 ? 0.668   -6.822  43.181  1.00 35.87  ? 114 THR A N     1 
ATOM   943  C  CA    . THR A 1 142 ? -0.140  -7.120  42.004  1.00 36.75  ? 114 THR A CA    1 
ATOM   944  C  C     . THR A 1 142 ? -0.195  -5.932  41.050  1.00 37.36  ? 114 THR A C     1 
ATOM   945  O  O     . THR A 1 142 ? -0.081  -6.105  39.833  1.00 34.83  ? 114 THR A O     1 
ATOM   946  C  CB    . THR A 1 142 ? -1.537  -7.538  42.448  1.00 37.48  ? 114 THR A CB    1 
ATOM   947  O  OG1   . THR A 1 142 ? -1.456  -8.828  43.058  1.00 39.84  ? 114 THR A OG1   1 
ATOM   948  C  CG2   . THR A 1 142 ? -2.486  -7.609  41.268  1.00 33.52  ? 114 THR A CG2   1 
ATOM   949  N  N     . LEU A 1 143 ? -0.356  -4.715  41.586  1.00 32.57  ? 115 LEU A N     1 
ATOM   950  C  CA    . LEU A 1 143 ? -0.404  -3.525  40.740  1.00 34.68  ? 115 LEU A CA    1 
ATOM   951  C  C     . LEU A 1 143 ? 0.912   -3.312  40.011  1.00 41.44  ? 115 LEU A C     1 
ATOM   952  O  O     . LEU A 1 143 ? 0.931   -2.838  38.868  1.00 37.77  ? 115 LEU A O     1 
ATOM   953  C  CB    . LEU A 1 143 ? -0.716  -2.294  41.588  1.00 32.35  ? 115 LEU A CB    1 
ATOM   954  C  CG    . LEU A 1 143 ? -2.139  -1.795  41.743  1.00 42.95  ? 115 LEU A CG    1 
ATOM   955  C  CD1   . LEU A 1 143 ? -2.162  -0.756  42.863  1.00 40.45  ? 115 LEU A CD1   1 
ATOM   956  C  CD2   . LEU A 1 143 ? -2.603  -1.179  40.435  1.00 45.03  ? 115 LEU A CD2   1 
ATOM   957  N  N     . THR A 1 144 ? 2.027   -3.618  40.682  1.00 36.66  ? 116 THR A N     1 
ATOM   958  C  CA    . THR A 1 144 ? 3.349   -3.447  40.096  1.00 30.08  ? 116 THR A CA    1 
ATOM   959  C  C     . THR A 1 144 ? 3.596   -4.465  38.990  1.00 39.49  ? 116 THR A C     1 
ATOM   960  O  O     . THR A 1 144 ? 4.093   -4.116  37.914  1.00 41.83  ? 116 THR A O     1 
ATOM   961  C  CB    . THR A 1 144 ? 4.417   -3.577  41.195  1.00 41.62  ? 116 THR A CB    1 
ATOM   962  O  OG1   . THR A 1 144 ? 4.260   -2.522  42.153  1.00 41.91  ? 116 THR A OG1   1 
ATOM   963  C  CG2   . THR A 1 144 ? 5.810   -3.499  40.613  1.00 32.80  ? 116 THR A CG2   1 
ATOM   964  N  N     . GLU A 1 145 ? 3.285   -5.742  39.248  1.00 38.77  ? 117 GLU A N     1 
ATOM   965  C  CA    . GLU A 1 145 ? 3.430   -6.761  38.209  1.00 41.38  ? 117 GLU A CA    1 
ATOM   966  C  C     . GLU A 1 145 ? 2.545   -6.442  37.009  1.00 42.05  ? 117 GLU A C     1 
ATOM   967  O  O     . GLU A 1 145 ? 2.976   -6.557  35.857  1.00 37.57  ? 117 GLU A O     1 
ATOM   968  C  CB    . GLU A 1 145 ? 3.077   -8.143  38.766  1.00 40.42  ? 117 GLU A CB    1 
ATOM   969  C  CG    . GLU A 1 145 ? 4.032   -8.662  39.826  1.00 45.93  ? 117 GLU A CG    1 
ATOM   970  C  CD    . GLU A 1 145 ? 3.447   -9.823  40.625  1.00 52.91  ? 117 GLU A CD    1 
ATOM   971  O  OE1   . GLU A 1 145 ? 2.257   -10.166 40.412  1.00 59.59  ? 117 GLU A OE1   1 
ATOM   972  O  OE2   . GLU A 1 145 ? 4.174   -10.371 41.481  1.00 54.95  ? 117 GLU A OE2   1 
ATOM   973  N  N     . SER A 1 146 ? 1.303   -6.032  37.263  1.00 37.42  ? 118 SER A N     1 
ATOM   974  C  CA    . SER A 1 146 ? 0.420   -5.639  36.172  1.00 39.96  ? 118 SER A CA    1 
ATOM   975  C  C     . SER A 1 146 ? 1.028   -4.485  35.388  1.00 44.43  ? 118 SER A C     1 
ATOM   976  O  O     . SER A 1 146 ? 1.121   -4.525  34.156  1.00 47.12  ? 118 SER A O     1 
ATOM   977  C  CB    . SER A 1 146 ? -0.954  -5.258  36.733  1.00 37.91  ? 118 SER A CB    1 
ATOM   978  O  OG    . SER A 1 146 ? -1.827  -4.836  35.697  1.00 48.18  ? 118 SER A OG    1 
ATOM   979  N  N     . HIS A 1 147 ? 1.483   -3.463  36.102  1.00 44.23  ? 119 HIS A N     1 
ATOM   980  C  CA    . HIS A 1 147 ? 2.112   -2.313  35.468  1.00 42.90  ? 119 HIS A CA    1 
ATOM   981  C  C     . HIS A 1 147 ? 3.296   -2.718  34.599  1.00 43.37  ? 119 HIS A C     1 
ATOM   982  O  O     . HIS A 1 147 ? 3.551   -2.101  33.558  1.00 45.21  ? 119 HIS A O     1 
ATOM   983  C  CB    . HIS A 1 147 ? 2.568   -1.337  36.543  1.00 41.70  ? 119 HIS A CB    1 
ATOM   984  C  CG    . HIS A 1 147 ? 2.645   0.065   36.063  1.00 40.16  ? 119 HIS A CG    1 
ATOM   985  N  ND1   . HIS A 1 147 ? 3.646   0.504   35.228  1.00 35.65  ? 119 HIS A ND1   1 
ATOM   986  C  CD2   . HIS A 1 147 ? 1.811   1.115   36.251  1.00 40.77  ? 119 HIS A CD2   1 
ATOM   987  C  CE1   . HIS A 1 147 ? 3.442   1.778   34.944  1.00 49.25  ? 119 HIS A CE1   1 
ATOM   988  N  NE2   . HIS A 1 147 ? 2.334   2.171   35.549  1.00 47.76  ? 119 HIS A NE2   1 
ATOM   989  N  N     . ARG A 1 148 ? 4.044   -3.741  35.018  1.00 45.56  ? 120 ARG A N     1 
ATOM   990  C  CA    . ARG A 1 148 ? 5.191   -4.195  34.231  1.00 38.21  ? 120 ARG A CA    1 
ATOM   991  C  C     . ARG A 1 148 ? 4.749   -4.909  32.958  1.00 47.51  ? 120 ARG A C     1 
ATOM   992  O  O     . ARG A 1 148 ? 5.408   -4.802  31.915  1.00 48.48  ? 120 ARG A O     1 
ATOM   993  C  CB    . ARG A 1 148 ? 6.061   -5.116  35.076  1.00 43.25  ? 120 ARG A CB    1 
ATOM   994  C  CG    . ARG A 1 148 ? 6.777   -4.434  36.231  1.00 45.89  ? 120 ARG A CG    1 
ATOM   995  C  CD    . ARG A 1 148 ? 7.596   -3.247  35.757  1.00 49.69  ? 120 ARG A CD    1 
ATOM   996  N  NE    . ARG A 1 148 ? 8.772   -3.107  36.602  1.00 58.67  ? 120 ARG A NE    1 
ATOM   997  C  CZ    . ARG A 1 148 ? 9.733   -2.210  36.437  1.00 55.26  ? 120 ARG A CZ    1 
ATOM   998  N  NH1   . ARG A 1 148 ? 9.691   -1.317  35.457  1.00 48.60  ? 120 ARG A NH1   1 
ATOM   999  N  NH2   . ARG A 1 148 ? 10.775  -2.227  37.263  1.00 44.19  ? 120 ARG A NH2   1 
ATOM   1000 N  N     . ILE A 1 149 ? 3.650   -5.659  33.025  1.00 47.68  ? 121 ILE A N     1 
ATOM   1001 C  CA    . ILE A 1 149 ? 3.071   -6.233  31.815  1.00 47.49  ? 121 ILE A CA    1 
ATOM   1002 C  C     . ILE A 1 149 ? 2.717   -5.126  30.832  1.00 48.23  ? 121 ILE A C     1 
ATOM   1003 O  O     . ILE A 1 149 ? 3.185   -5.111  29.687  1.00 44.08  ? 121 ILE A O     1 
ATOM   1004 C  CB    . ILE A 1 149 ? 1.846   -7.097  32.166  1.00 50.47  ? 121 ILE A CB    1 
ATOM   1005 C  CG1   . ILE A 1 149 ? 2.272   -8.254  33.077  1.00 48.66  ? 121 ILE A CG1   1 
ATOM   1006 C  CG2   . ILE A 1 149 ? 1.154   -7.593  30.909  1.00 51.86  ? 121 ILE A CG2   1 
ATOM   1007 C  CD1   . ILE A 1 149 ? 1.289   -9.410  33.118  1.00 55.32  ? 121 ILE A CD1   1 
ATOM   1008 N  N     . LEU A 1 150 ? 1.897   -4.171  31.281  1.00 49.89  ? 122 LEU A N     1 
ATOM   1009 C  CA    . LEU A 1 150 ? 1.454   -3.072  30.425  1.00 51.74  ? 122 LEU A CA    1 
ATOM   1010 C  C     . LEU A 1 150 ? 2.613   -2.306  29.816  1.00 54.29  ? 122 LEU A C     1 
ATOM   1011 O  O     . LEU A 1 150 ? 2.483   -1.747  28.718  1.00 53.40  ? 122 LEU A O     1 
ATOM   1012 C  CB    . LEU A 1 150 ? 0.583   -2.103  31.226  1.00 52.87  ? 122 LEU A CB    1 
ATOM   1013 C  CG    . LEU A 1 150 ? -0.920  -2.222  31.026  1.00 55.21  ? 122 LEU A CG    1 
ATOM   1014 C  CD1   . LEU A 1 150 ? -1.369  -3.666  31.228  1.00 54.91  ? 122 LEU A CD1   1 
ATOM   1015 C  CD2   . LEU A 1 150 ? -1.620  -1.292  31.999  1.00 57.84  ? 122 LEU A CD2   1 
ATOM   1016 N  N     . GLU A 1 151 ? 3.740   -2.248  30.524  1.00 47.85  ? 123 GLU A N     1 
ATOM   1017 C  CA    . GLU A 1 151 ? 4.895   -1.499  30.054  1.00 48.37  ? 123 GLU A CA    1 
ATOM   1018 C  C     . GLU A 1 151 ? 5.491   -2.118  28.792  1.00 54.33  ? 123 GLU A C     1 
ATOM   1019 O  O     . GLU A 1 151 ? 6.025   -1.396  27.939  1.00 53.35  ? 123 GLU A O     1 
ATOM   1020 C  CB    . GLU A 1 151 ? 5.928   -1.432  31.183  1.00 43.37  ? 123 GLU A CB    1 
ATOM   1021 C  CG    . GLU A 1 151 ? 7.083   -0.497  30.963  1.00 56.93  ? 123 GLU A CG    1 
ATOM   1022 C  CD    . GLU A 1 151 ? 8.235   -0.790  31.917  1.00 68.79  ? 123 GLU A CD    1 
ATOM   1023 O  OE1   . GLU A 1 151 ? 7.972   -1.350  33.010  1.00 60.54  ? 123 GLU A OE1   1 
ATOM   1024 O  OE2   . GLU A 1 151 ? 9.397   -0.478  31.567  1.00 64.45  ? 123 GLU A OE2   1 
ATOM   1025 N  N     . LYS A 1 152 ? 5.413   -3.446  28.659  1.00 46.91  ? 124 LYS A N     1 
ATOM   1026 C  CA    . LYS A 1 152 ? 5.884   -4.117  27.453  1.00 49.72  ? 124 LYS A CA    1 
ATOM   1027 C  C     . LYS A 1 152 ? 4.985   -3.855  26.255  1.00 47.56  ? 124 LYS A C     1 
ATOM   1028 O  O     . LYS A 1 152 ? 5.435   -4.001  25.116  1.00 49.25  ? 124 LYS A O     1 
ATOM   1029 C  CB    . LYS A 1 152 ? 5.978   -5.624  27.699  1.00 50.33  ? 124 LYS A CB    1 
ATOM   1030 C  CG    . LYS A 1 152 ? 7.036   -6.029  28.710  1.00 46.43  ? 124 LYS A CG    1 
ATOM   1031 C  CD    . LYS A 1 152 ? 8.383   -5.456  28.301  1.00 58.59  ? 124 LYS A CD    1 
ATOM   1032 C  CE    . LYS A 1 152 ? 9.473   -5.874  29.262  1.00 59.19  ? 124 LYS A CE    1 
ATOM   1033 N  NZ    . LYS A 1 152 ? 9.474   -7.349  29.374  1.00 59.85  ? 124 LYS A NZ    1 
ATOM   1034 N  N     . TYR A 1 153 ? 3.725   -3.488  26.485  1.00 46.10  ? 125 TYR A N     1 
ATOM   1035 C  CA    . TYR A 1 153 ? 2.733   -3.358  25.429  1.00 47.42  ? 125 TYR A CA    1 
ATOM   1036 C  C     . TYR A 1 153 ? 2.387   -1.907  25.118  1.00 46.42  ? 125 TYR A C     1 
ATOM   1037 O  O     . TYR A 1 153 ? 1.402   -1.658  24.420  1.00 47.88  ? 125 TYR A O     1 
ATOM   1038 C  CB    . TYR A 1 153 ? 1.472   -4.140  25.803  1.00 43.95  ? 125 TYR A CB    1 
ATOM   1039 C  CG    . TYR A 1 153 ? 1.662   -5.637  25.778  1.00 42.60  ? 125 TYR A CG    1 
ATOM   1040 C  CD1   . TYR A 1 153 ? 2.173   -6.313  26.874  1.00 43.87  ? 125 TYR A CD1   1 
ATOM   1041 C  CD2   . TYR A 1 153 ? 1.343   -6.376  24.652  1.00 46.20  ? 125 TYR A CD2   1 
ATOM   1042 C  CE1   . TYR A 1 153 ? 2.365   -7.678  26.850  1.00 42.66  ? 125 TYR A CE1   1 
ATOM   1043 C  CE2   . TYR A 1 153 ? 1.528   -7.744  24.617  1.00 36.09  ? 125 TYR A CE2   1 
ATOM   1044 C  CZ    . TYR A 1 153 ? 2.035   -8.392  25.717  1.00 51.98  ? 125 TYR A CZ    1 
ATOM   1045 O  OH    . TYR A 1 153 ? 2.215   -9.760  25.680  1.00 56.24  ? 125 TYR A OH    1 
ATOM   1046 N  N     . THR A 1 154 ? 3.166   -0.946  25.625  1.00 50.47  ? 126 THR A N     1 
ATOM   1047 C  CA    . THR A 1 154 ? 3.042   0.470   25.284  1.00 61.61  ? 126 THR A CA    1 
ATOM   1048 C  C     . THR A 1 154 ? 4.365   1.000   24.748  1.00 63.67  ? 126 THR A C     1 
ATOM   1049 O  O     . THR A 1 154 ? 5.438   0.452   25.025  1.00 66.82  ? 126 THR A O     1 
ATOM   1050 C  CB    . THR A 1 154 ? 2.636   1.347   26.488  1.00 60.43  ? 126 THR A CB    1 
ATOM   1051 O  OG1   . THR A 1 154 ? 3.686   1.353   27.461  1.00 52.39  ? 126 THR A OG1   1 
ATOM   1052 C  CG2   . THR A 1 154 ? 1.383   0.860   27.129  1.00 56.98  ? 126 THR A CG2   1 
ATOM   1053 N  N     . GLN A 1 155 ? 4.282   2.105   23.984  1.00 67.80  ? 127 GLN A N     1 
ATOM   1054 C  CA    . GLN A 1 155 ? 5.504   2.710   23.464  1.00 65.27  ? 127 GLN A CA    1 
ATOM   1055 C  C     . GLN A 1 155 ? 6.269   3.402   24.592  1.00 66.74  ? 127 GLN A C     1 
ATOM   1056 O  O     . GLN A 1 155 ? 5.661   4.080   25.429  1.00 63.64  ? 127 GLN A O     1 
ATOM   1057 C  CB    . GLN A 1 155 ? 5.191   3.732   22.372  1.00 62.92  ? 127 GLN A CB    1 
ATOM   1058 C  CG    . GLN A 1 155 ? 4.986   3.227   20.921  1.00 62.87  ? 127 GLN A CG    1 
ATOM   1059 C  CD    . GLN A 1 155 ? 5.710   1.926   20.554  1.00 66.20  ? 127 GLN A CD    1 
ATOM   1060 O  OE1   . GLN A 1 155 ? 5.090   0.994   20.030  1.00 70.04  ? 127 GLN A OE1   1 
ATOM   1061 N  NE2   . GLN A 1 155 ? 7.024   1.868   20.799  1.00 60.48  ? 127 GLN A NE2   1 
ATOM   1062 N  N     . PRO A 1 156 ? 7.603   3.255   24.632  1.00 64.13  ? 128 PRO A N     1 
ATOM   1063 C  CA    . PRO A 1 156 ? 8.402   3.992   25.623  1.00 65.34  ? 128 PRO A CA    1 
ATOM   1064 C  C     . PRO A 1 156 ? 8.374   5.503   25.446  1.00 61.43  ? 128 PRO A C     1 
ATOM   1065 O  O     . PRO A 1 156 ? 8.945   6.219   26.269  1.00 68.20  ? 128 PRO A O     1 
ATOM   1066 C  CB    . PRO A 1 156 ? 9.817   3.439   25.409  1.00 68.45  ? 128 PRO A CB    1 
ATOM   1067 C  CG    . PRO A 1 156 ? 9.599   2.074   24.827  1.00 69.74  ? 128 PRO A CG    1 
ATOM   1068 C  CD    . PRO A 1 156 ? 8.381   2.198   23.963  1.00 66.24  ? 128 PRO A CD    1 
ATOM   1069 N  N     . SER A 1 157 ? 7.728   6.014   24.393  1.00 65.88  ? 129 SER A N     1 
ATOM   1070 C  CA    . SER A 1 157 ? 7.594   7.460   24.258  1.00 65.64  ? 129 SER A CA    1 
ATOM   1071 C  C     . SER A 1 157 ? 6.506   8.032   25.162  1.00 57.72  ? 129 SER A C     1 
ATOM   1072 O  O     . SER A 1 157 ? 6.567   9.220   25.495  1.00 55.38  ? 129 SER A O     1 
ATOM   1073 C  CB    . SER A 1 157 ? 7.318   7.843   22.799  1.00 59.93  ? 129 SER A CB    1 
ATOM   1074 O  OG    . SER A 1 157 ? 6.032   7.409   22.396  1.00 66.43  ? 129 SER A OG    1 
ATOM   1075 N  N     . ILE A 1 158 ? 5.523   7.224   25.574  1.00 56.61  ? 130 ILE A N     1 
ATOM   1076 C  CA    . ILE A 1 158 ? 4.549   7.701   26.559  1.00 54.49  ? 130 ILE A CA    1 
ATOM   1077 C  C     . ILE A 1 158 ? 5.214   7.863   27.926  1.00 59.15  ? 130 ILE A C     1 
ATOM   1078 O  O     . ILE A 1 158 ? 4.930   8.817   28.663  1.00 56.99  ? 130 ILE A O     1 
ATOM   1079 C  CB    . ILE A 1 158 ? 3.317   6.770   26.616  1.00 61.53  ? 130 ILE A CB    1 
ATOM   1080 C  CG1   . ILE A 1 158 ? 2.265   7.158   25.558  1.00 64.45  ? 130 ILE A CG1   1 
ATOM   1081 C  CG2   . ILE A 1 158 ? 2.648   6.799   27.987  1.00 58.69  ? 130 ILE A CG2   1 
ATOM   1082 C  CD1   . ILE A 1 158 ? 2.733   7.136   24.105  1.00 60.50  ? 130 ILE A CD1   1 
ATOM   1083 N  N     . PHE A 1 159 ? 6.129   6.955   28.275  1.00 55.21  ? 131 PHE A N     1 
ATOM   1084 C  CA    . PHE A 1 159 ? 6.870   7.109   29.522  1.00 58.00  ? 131 PHE A CA    1 
ATOM   1085 C  C     . PHE A 1 159 ? 7.822   8.291   29.465  1.00 58.36  ? 131 PHE A C     1 
ATOM   1086 O  O     . PHE A 1 159 ? 8.050   8.948   30.490  1.00 53.44  ? 131 PHE A O     1 
ATOM   1087 C  CB    . PHE A 1 159 ? 7.638   5.830   29.852  1.00 59.70  ? 131 PHE A CB    1 
ATOM   1088 C  CG    . PHE A 1 159 ? 6.760   4.623   29.992  1.00 63.42  ? 131 PHE A CG    1 
ATOM   1089 C  CD1   . PHE A 1 159 ? 5.770   4.587   30.965  1.00 56.43  ? 131 PHE A CD1   1 
ATOM   1090 C  CD2   . PHE A 1 159 ? 6.916   3.530   29.151  1.00 66.97  ? 131 PHE A CD2   1 
ATOM   1091 C  CE1   . PHE A 1 159 ? 4.953   3.483   31.098  1.00 58.60  ? 131 PHE A CE1   1 
ATOM   1092 C  CE2   . PHE A 1 159 ? 6.100   2.422   29.275  1.00 63.29  ? 131 PHE A CE2   1 
ATOM   1093 C  CZ    . PHE A 1 159 ? 5.115   2.398   30.254  1.00 58.73  ? 131 PHE A CZ    1 
ATOM   1094 N  N     . LYS A 1 160 ? 8.390   8.570   28.287  1.00 60.51  ? 132 LYS A N     1 
ATOM   1095 C  CA    . LYS A 1 160 ? 9.227   9.754   28.130  1.00 61.24  ? 132 LYS A CA    1 
ATOM   1096 C  C     . LYS A 1 160 ? 8.421   11.019  28.375  1.00 57.47  ? 132 LYS A C     1 
ATOM   1097 O  O     . LYS A 1 160 ? 8.878   11.928  29.077  1.00 59.56  ? 132 LYS A O     1 
ATOM   1098 C  CB    . LYS A 1 160 ? 9.862   9.776   26.737  1.00 59.57  ? 132 LYS A CB    1 
ATOM   1099 N  N     . ILE A 1 161 ? 7.210   11.086  27.818  1.00 53.81  ? 133 ILE A N     1 
ATOM   1100 C  CA    . ILE A 1 161 ? 6.310   12.201  28.105  1.00 59.96  ? 133 ILE A CA    1 
ATOM   1101 C  C     . ILE A 1 161 ? 6.030   12.284  29.602  1.00 54.74  ? 133 ILE A C     1 
ATOM   1102 O  O     . ILE A 1 161 ? 5.982   13.376  30.177  1.00 60.97  ? 133 ILE A O     1 
ATOM   1103 C  CB    . ILE A 1 161 ? 5.005   12.064  27.290  1.00 56.94  ? 133 ILE A CB    1 
ATOM   1104 C  CG1   . ILE A 1 161 ? 5.267   12.258  25.791  1.00 61.29  ? 133 ILE A CG1   1 
ATOM   1105 C  CG2   . ILE A 1 161 ? 3.957   13.060  27.757  1.00 62.59  ? 133 ILE A CG2   1 
ATOM   1106 C  CD1   . ILE A 1 161 ? 4.259   11.541  24.896  1.00 55.36  ? 133 ILE A CD1   1 
ATOM   1107 N  N     . ILE A 1 162 ? 5.866   11.133  30.255  1.00 54.48  ? 134 ILE A N     1 
ATOM   1108 C  CA    . ILE A 1 162 ? 5.518   11.109  31.675  1.00 59.79  ? 134 ILE A CA    1 
ATOM   1109 C  C     . ILE A 1 162 ? 6.690   11.587  32.526  1.00 63.73  ? 134 ILE A C     1 
ATOM   1110 O  O     . ILE A 1 162 ? 6.520   12.404  33.440  1.00 63.26  ? 134 ILE A O     1 
ATOM   1111 C  CB    . ILE A 1 162 ? 5.069   9.697   32.085  1.00 54.41  ? 134 ILE A CB    1 
ATOM   1112 C  CG1   . ILE A 1 162 ? 3.626   9.457   31.643  1.00 51.33  ? 134 ILE A CG1   1 
ATOM   1113 C  CG2   . ILE A 1 162 ? 5.221   9.510   33.589  1.00 52.50  ? 134 ILE A CG2   1 
ATOM   1114 C  CD1   . ILE A 1 162 ? 3.268   7.993   31.506  1.00 46.83  ? 134 ILE A CD1   1 
ATOM   1115 N  N     . SER A 1 163 ? 7.895   11.077  32.243  1.00 61.45  ? 135 SER A N     1 
ATOM   1116 C  CA    . SER A 1 163 ? 9.095   11.488  32.967  1.00 64.41  ? 135 SER A CA    1 
ATOM   1117 C  C     . SER A 1 163 ? 9.365   12.983  32.851  1.00 68.18  ? 135 SER A C     1 
ATOM   1118 O  O     . SER A 1 163 ? 10.048  13.549  33.713  1.00 73.21  ? 135 SER A O     1 
ATOM   1119 C  CB    . SER A 1 163 ? 10.303  10.714  32.447  1.00 64.99  ? 135 SER A CB    1 
ATOM   1120 O  OG    . SER A 1 163 ? 10.052  9.321   32.498  1.00 71.13  ? 135 SER A OG    1 
ATOM   1121 N  N     . GLN A 1 164 ? 8.860   13.627  31.800  1.00 68.07  ? 136 GLN A N     1 
ATOM   1122 C  CA    . GLN A 1 164 ? 9.025   15.060  31.594  1.00 64.33  ? 136 GLN A CA    1 
ATOM   1123 C  C     . GLN A 1 164 ? 8.014   15.895  32.370  1.00 66.39  ? 136 GLN A C     1 
ATOM   1124 O  O     . GLN A 1 164 ? 8.086   17.128  32.326  1.00 69.21  ? 136 GLN A O     1 
ATOM   1125 C  CB    . GLN A 1 164 ? 8.940   15.375  30.096  1.00 68.87  ? 136 GLN A CB    1 
ATOM   1126 C  CG    . GLN A 1 164 ? 10.146  14.868  29.307  1.00 70.31  ? 136 GLN A CG    1 
ATOM   1127 C  CD    . GLN A 1 164 ? 9.909   14.838  27.811  1.00 72.65  ? 136 GLN A CD    1 
ATOM   1128 O  OE1   . GLN A 1 164 ? 8.838   15.223  27.334  1.00 74.68  ? 136 GLN A OE1   1 
ATOM   1129 N  NE2   . GLN A 1 164 ? 10.911  14.380  27.059  1.00 69.03  ? 136 GLN A NE2   1 
ATOM   1130 N  N     . GLY A 1 165 ? 7.087   15.264  33.084  1.00 62.25  ? 137 GLY A N     1 
ATOM   1131 C  CA    . GLY A 1 165 ? 6.155   15.994  33.913  1.00 64.34  ? 137 GLY A CA    1 
ATOM   1132 C  C     . GLY A 1 165 ? 4.860   16.378  33.247  1.00 65.20  ? 137 GLY A C     1 
ATOM   1133 O  O     . GLY A 1 165 ? 4.213   17.330  33.696  1.00 66.19  ? 137 GLY A O     1 
ATOM   1134 N  N     . THR A 1 166 ? 4.454   15.672  32.191  1.00 66.20  ? 138 THR A N     1 
ATOM   1135 C  CA    . THR A 1 166 ? 3.250   16.015  31.445  1.00 73.70  ? 138 THR A CA    1 
ATOM   1136 C  C     . THR A 1 166 ? 2.414   14.762  31.211  1.00 70.68  ? 138 THR A C     1 
ATOM   1137 O  O     . THR A 1 166 ? 2.947   13.715  30.826  1.00 65.94  ? 138 THR A O     1 
ATOM   1138 C  CB    . THR A 1 166 ? 3.594   16.695  30.105  1.00 68.80  ? 138 THR A CB    1 
ATOM   1139 O  OG1   . THR A 1 166 ? 4.538   15.899  29.381  1.00 70.86  ? 138 THR A OG1   1 
ATOM   1140 C  CG2   . THR A 1 166 ? 4.185   18.088  30.339  1.00 62.82  ? 138 THR A CG2   1 
ATOM   1141 N  N     . ASN A 1 167 ? 1.115   14.870  31.460  1.00 67.07  ? 139 ASN A N     1 
ATOM   1142 C  CA    . ASN A 1 167 ? 0.202   13.771  31.190  1.00 66.51  ? 139 ASN A CA    1 
ATOM   1143 C  C     . ASN A 1 167 ? 0.057   13.621  29.682  1.00 63.36  ? 139 ASN A C     1 
ATOM   1144 O  O     . ASN A 1 167 ? -0.374  14.575  29.018  1.00 62.40  ? 139 ASN A O     1 
ATOM   1145 C  CB    . ASN A 1 167 ? -1.153  14.036  31.847  1.00 62.66  ? 139 ASN A CB    1 
ATOM   1146 C  CG    . ASN A 1 167 ? -2.083  12.822  31.811  1.00 61.67  ? 139 ASN A CG    1 
ATOM   1147 O  OD1   . ASN A 1 167 ? -2.085  12.029  30.863  1.00 61.62  ? 139 ASN A OD1   1 
ATOM   1148 N  ND2   . ASN A 1 167 ? -2.900  12.691  32.849  1.00 57.72  ? 139 ASN A ND2   1 
ATOM   1149 N  N     . PRO A 1 168 ? 0.421   12.469  29.098  1.00 67.76  ? 140 PRO A N     1 
ATOM   1150 C  CA    . PRO A 1 168 ? 0.238   12.279  27.645  1.00 62.69  ? 140 PRO A CA    1 
ATOM   1151 C  C     . PRO A 1 168 ? -1.189  12.525  27.158  1.00 65.06  ? 140 PRO A C     1 
ATOM   1152 O  O     . PRO A 1 168 ? -1.375  12.928  26.000  1.00 56.40  ? 140 PRO A O     1 
ATOM   1153 C  CB    . PRO A 1 168 ? 0.664   10.824  27.407  1.00 64.10  ? 140 PRO A CB    1 
ATOM   1154 C  CG    . PRO A 1 168 ? 1.277   10.331  28.679  1.00 63.33  ? 140 PRO A CG    1 
ATOM   1155 C  CD    . PRO A 1 168 ? 1.141   11.367  29.751  1.00 66.74  ? 140 PRO A CD    1 
ATOM   1156 N  N     . LEU A 1 169 ? -2.207  12.301  27.999  1.00 64.58  ? 141 LEU A N     1 
ATOM   1157 C  CA    . LEU A 1 169 ? -3.578  12.629  27.627  1.00 58.65  ? 141 LEU A CA    1 
ATOM   1158 C  C     . LEU A 1 169 ? -3.819  14.131  27.510  1.00 61.33  ? 141 LEU A C     1 
ATOM   1159 O  O     . LEU A 1 169 ? -4.867  14.532  26.991  1.00 60.53  ? 141 LEU A O     1 
ATOM   1160 C  CB    . LEU A 1 169 ? -4.553  12.034  28.645  1.00 65.50  ? 141 LEU A CB    1 
ATOM   1161 C  CG    . LEU A 1 169 ? -4.576  10.509  28.793  1.00 65.90  ? 141 LEU A CG    1 
ATOM   1162 C  CD1   . LEU A 1 169 ? -5.356  10.115  30.042  1.00 59.68  ? 141 LEU A CD1   1 
ATOM   1163 C  CD2   . LEU A 1 169 ? -5.179  9.850   27.551  1.00 56.38  ? 141 LEU A CD2   1 
ATOM   1164 N  N     . ASN A 1 170 ? -2.880  14.965  27.967  1.00 64.65  ? 142 ASN A N     1 
ATOM   1165 C  CA    . ASN A 1 170 ? -3.042  16.412  27.955  1.00 66.60  ? 142 ASN A CA    1 
ATOM   1166 C  C     . ASN A 1 170 ? -2.245  17.109  26.860  1.00 65.29  ? 142 ASN A C     1 
ATOM   1167 O  O     . ASN A 1 170 ? -2.306  18.338  26.759  1.00 65.55  ? 142 ASN A O     1 
ATOM   1168 C  CB    . ASN A 1 170 ? -2.652  17.001  29.316  1.00 69.72  ? 142 ASN A CB    1 
ATOM   1169 C  CG    . ASN A 1 170 ? -3.636  16.632  30.415  1.00 70.62  ? 142 ASN A CG    1 
ATOM   1170 O  OD1   . ASN A 1 170 ? -3.260  16.496  31.585  1.00 64.80  ? 142 ASN A OD1   1 
ATOM   1171 N  ND2   . ASN A 1 170 ? -4.899  16.447  30.039  1.00 67.58  ? 142 ASN A ND2   1 
ATOM   1172 N  N     . ILE A 1 171 ? -1.494  16.365  26.045  1.00 61.97  ? 143 ILE A N     1 
ATOM   1173 C  CA    . ILE A 1 171 ? -0.762  16.973  24.939  1.00 62.84  ? 143 ILE A CA    1 
ATOM   1174 C  C     . ILE A 1 171 ? -1.739  17.630  23.973  1.00 56.99  ? 143 ILE A C     1 
ATOM   1175 O  O     . ILE A 1 171 ? -2.714  17.009  23.534  1.00 56.16  ? 143 ILE A O     1 
ATOM   1176 C  CB    . ILE A 1 171 ? 0.100   15.914  24.234  1.00 61.12  ? 143 ILE A CB    1 
ATOM   1177 C  CG1   . ILE A 1 171 ? 1.056   15.261  25.234  1.00 67.65  ? 143 ILE A CG1   1 
ATOM   1178 C  CG2   . ILE A 1 171 ? 0.850   16.518  23.048  1.00 61.22  ? 143 ILE A CG2   1 
ATOM   1179 C  CD1   . ILE A 1 171 ? 2.338   16.043  25.471  1.00 64.22  ? 143 ILE A CD1   1 
ATOM   1180 N  N     . ARG A 1 172 ? -1.481  18.952  23.639  1.00 59.10  ? 144 ARG A N     1 
ATOM   1181 C  CA    . ARG A 1 172 ? -2.265  19.709  22.672  1.00 54.81  ? 144 ARG A CA    1 
ATOM   1182 C  C     . ARG A 1 172 ? -1.715  19.497  21.262  1.00 55.40  ? 144 ARG A C     1 
ATOM   1183 O  O     . ARG A 1 172 ? -0.513  19.270  21.083  1.00 53.82  ? 144 ARG A O     1 
ATOM   1184 C  CB    . ARG A 1 172 ? -2.247  21.196  23.013  1.00 55.47  ? 144 ARG A CB    1 
ATOM   1185 N  N     . PRO A 1 173 ? -2.577  19.578  20.248  1.00 50.75  ? 145 PRO A N     1 
ATOM   1186 C  CA    . PRO A 1 173 ? -2.173  19.168  18.894  1.00 46.95  ? 145 PRO A CA    1 
ATOM   1187 C  C     . PRO A 1 173 ? -1.061  20.025  18.298  1.00 42.16  ? 145 PRO A C     1 
ATOM   1188 O  O     . PRO A 1 173 ? -1.059  21.250  18.422  1.00 45.27  ? 145 PRO A O     1 
ATOM   1189 C  CB    . PRO A 1 173 ? -3.472  19.291  18.082  1.00 40.46  ? 145 PRO A CB    1 
ATOM   1190 C  CG    . PRO A 1 173 ? -4.443  20.036  18.960  1.00 45.36  ? 145 PRO A CG    1 
ATOM   1191 C  CD    . PRO A 1 173 ? -4.032  19.770  20.363  1.00 45.98  ? 145 PRO A CD    1 
ATOM   1192 N  N     . LYS A 1 174 ? -0.125  19.356  17.618  1.00 36.30  ? 146 LYS A N     1 
ATOM   1193 C  CA    . LYS A 1 174 ? 1.036   19.976  16.984  1.00 35.55  ? 146 LYS A CA    1 
ATOM   1194 C  C     . LYS A 1 174 ? 1.375   19.248  15.686  1.00 32.47  ? 146 LYS A C     1 
ATOM   1195 O  O     . LYS A 1 174 ? 1.393   18.016  15.652  1.00 37.06  ? 146 LYS A O     1 
ATOM   1196 C  CB    . LYS A 1 174 ? 2.250   19.931  17.937  1.00 39.74  ? 146 LYS A CB    1 
ATOM   1197 C  CG    . LYS A 1 174 ? 3.189   21.137  17.906  1.00 48.38  ? 146 LYS A CG    1 
ATOM   1198 C  CD    . LYS A 1 174 ? 4.207   21.068  19.069  1.00 47.51  ? 146 LYS A CD    1 
ATOM   1199 C  CE    . LYS A 1 174 ? 5.285   19.987  18.880  1.00 61.08  ? 146 LYS A CE    1 
ATOM   1200 N  NZ    . LYS A 1 174 ? 6.366   20.044  19.934  1.00 57.54  ? 146 LYS A NZ    1 
ATOM   1201 N  N     . ALA A 1 175 ? 1.645   20.003  14.623  1.00 29.66  ? 147 ALA A N     1 
ATOM   1202 C  CA    . ALA A 1 175 ? 2.189   19.431  13.397  1.00 33.98  ? 147 ALA A CA    1 
ATOM   1203 C  C     . ALA A 1 175 ? 3.709   19.499  13.470  1.00 37.20  ? 147 ALA A C     1 
ATOM   1204 O  O     . ALA A 1 175 ? 4.269   20.558  13.771  1.00 32.76  ? 147 ALA A O     1 
ATOM   1205 C  CB    . ALA A 1 175 ? 1.696   20.174  12.158  1.00 34.16  ? 147 ALA A CB    1 
ATOM   1206 N  N     . VAL A 1 176 ? 4.370   18.366  13.232  1.00 35.42  ? 148 VAL A N     1 
ATOM   1207 C  CA    A VAL A 1 176 ? 5.823   18.288  13.292  0.52 34.22  ? 148 VAL A CA    1 
ATOM   1208 C  CA    B VAL A 1 176 ? 5.825   18.260  13.313  0.48 34.24  ? 148 VAL A CA    1 
ATOM   1209 C  C     . VAL A 1 176 ? 6.310   17.468  12.108  1.00 37.42  ? 148 VAL A C     1 
ATOM   1210 O  O     . VAL A 1 176 ? 5.762   16.404  11.804  1.00 35.66  ? 148 VAL A O     1 
ATOM   1211 C  CB    A VAL A 1 176 ? 6.306   17.673  14.620  0.52 38.13  ? 148 VAL A CB    1 
ATOM   1212 C  CB    B VAL A 1 176 ? 6.301   17.570  14.611  0.48 38.09  ? 148 VAL A CB    1 
ATOM   1213 C  CG1   A VAL A 1 176 ? 5.572   16.387  14.899  0.52 34.89  ? 148 VAL A CG1   1 
ATOM   1214 C  CG1   B VAL A 1 176 ? 7.776   17.879  14.867  0.48 34.65  ? 148 VAL A CG1   1 
ATOM   1215 C  CG2   A VAL A 1 176 ? 7.814   17.450  14.596  0.52 34.81  ? 148 VAL A CG2   1 
ATOM   1216 C  CG2   B VAL A 1 176 ? 5.453   17.973  15.822  0.48 35.21  ? 148 VAL A CG2   1 
ATOM   1217 N  N     . GLU A 1 177 ? 7.332   17.965  11.432  1.00 40.42  ? 149 GLU A N     1 
ATOM   1218 C  CA    . GLU A 1 177 ? 7.915   17.204  10.338  1.00 37.44  ? 149 GLU A CA    1 
ATOM   1219 C  C     . GLU A 1 177 ? 8.881   16.174  10.915  1.00 34.22  ? 149 GLU A C     1 
ATOM   1220 O  O     . GLU A 1 177 ? 9.708   16.502  11.771  1.00 38.55  ? 149 GLU A O     1 
ATOM   1221 C  CB    . GLU A 1 177 ? 8.642   18.125  9.368   1.00 44.91  ? 149 GLU A CB    1 
ATOM   1222 C  CG    . GLU A 1 177 ? 8.406   17.770  7.915   1.00 48.85  ? 149 GLU A CG    1 
ATOM   1223 C  CD    . GLU A 1 177 ? 9.136   18.707  6.979   1.00 61.17  ? 149 GLU A CD    1 
ATOM   1224 O  OE1   . GLU A 1 177 ? 8.698   18.834  5.810   1.00 72.61  ? 149 GLU A OE1   1 
ATOM   1225 O  OE2   . GLU A 1 177 ? 10.159  19.293  7.408   1.00 60.03  ? 149 GLU A OE2   1 
ATOM   1226 N  N     . LYS A 1 178 ? 8.747   14.925  10.482  1.00 30.65  ? 150 LYS A N     1 
ATOM   1227 C  CA    . LYS A 1 178 ? 9.617   13.852  10.913  1.00 29.25  ? 150 LYS A CA    1 
ATOM   1228 C  C     . LYS A 1 178 ? 10.193  13.143  9.703   1.00 33.22  ? 150 LYS A C     1 
ATOM   1229 O  O     . LYS A 1 178 ? 9.620   13.160  8.610   1.00 29.99  ? 150 LYS A O     1 
ATOM   1230 C  CB    . LYS A 1 178 ? 8.887   12.806  11.765  1.00 30.84  ? 150 LYS A CB    1 
ATOM   1231 C  CG    . LYS A 1 178 ? 8.132   13.336  12.979  1.00 29.09  ? 150 LYS A CG    1 
ATOM   1232 C  CD    . LYS A 1 178 ? 9.067   13.628  14.110  1.00 30.26  ? 150 LYS A CD    1 
ATOM   1233 C  CE    . LYS A 1 178 ? 8.296   13.638  15.439  1.00 43.22  ? 150 LYS A CE    1 
ATOM   1234 N  NZ    . LYS A 1 178 ? 9.090   14.281  16.516  1.00 39.70  ? 150 LYS A NZ    1 
ATOM   1235 N  N     . ILE A 1 179 ? 11.322  12.484  9.924   1.00 25.08  ? 151 ILE A N     1 
ATOM   1236 C  CA    . ILE A 1 179 ? 11.777  11.459  8.999   1.00 32.56  ? 151 ILE A CA    1 
ATOM   1237 C  C     . ILE A 1 179 ? 11.046  10.185  9.366   1.00 29.38  ? 151 ILE A C     1 
ATOM   1238 O  O     . ILE A 1 179 ? 11.120  9.737   10.513  1.00 30.85  ? 151 ILE A O     1 
ATOM   1239 C  CB    . ILE A 1 179 ? 13.299  11.258  9.096   1.00 32.63  ? 151 ILE A CB    1 
ATOM   1240 C  CG1   . ILE A 1 179 ? 14.036  12.589  8.896   1.00 32.36  ? 151 ILE A CG1   1 
ATOM   1241 C  CG2   . ILE A 1 179 ? 13.754  10.220  8.069   1.00 25.67  ? 151 ILE A CG2   1 
ATOM   1242 C  CD1   . ILE A 1 179 ? 13.949  13.116  7.502   1.00 35.00  ? 151 ILE A CD1   1 
ATOM   1243 N  N     . VAL A 1 180 ? 10.352  9.585   8.409   1.00 23.00  ? 152 VAL A N     1 
ATOM   1244 C  CA    . VAL A 1 180 ? 9.618   8.355   8.664   1.00 24.12  ? 152 VAL A CA    1 
ATOM   1245 C  C     . VAL A 1 180 ? 10.373  7.181   8.057   1.00 22.67  ? 152 VAL A C     1 
ATOM   1246 O  O     . VAL A 1 180 ? 10.766  7.219   6.888   1.00 24.56  ? 152 VAL A O     1 
ATOM   1247 C  CB    . VAL A 1 180 ? 8.178   8.417   8.132   1.00 29.96  ? 152 VAL A CB    1 
ATOM   1248 C  CG1   . VAL A 1 180 ? 7.422   7.236   8.662   1.00 30.32  ? 152 VAL A CG1   1 
ATOM   1249 C  CG2   . VAL A 1 180 ? 7.511   9.713   8.584   1.00 33.32  ? 152 VAL A CG2   1 
ATOM   1250 N  N     . PHE A 1 181 ? 10.526  6.134   8.855   1.00 23.05  ? 153 PHE A N     1 
ATOM   1251 C  CA    . PHE A 1 181 ? 11.247  4.912   8.544   1.00 27.30  ? 153 PHE A CA    1 
ATOM   1252 C  C     . PHE A 1 181 ? 10.220  3.795   8.399   1.00 23.76  ? 153 PHE A C     1 
ATOM   1253 O  O     . PHE A 1 181 ? 9.374   3.616   9.282   1.00 25.67  ? 153 PHE A O     1 
ATOM   1254 C  CB    . PHE A 1 181 ? 12.241  4.635   9.689   1.00 24.88  ? 153 PHE A CB    1 
ATOM   1255 C  CG    . PHE A 1 181 ? 12.919  3.289   9.639   1.00 22.76  ? 153 PHE A CG    1 
ATOM   1256 C  CD1   . PHE A 1 181 ? 12.230  2.129   9.969   1.00 19.75  ? 153 PHE A CD1   1 
ATOM   1257 C  CD2   . PHE A 1 181 ? 14.281  3.197   9.331   1.00 22.81  ? 153 PHE A CD2   1 
ATOM   1258 C  CE1   . PHE A 1 181 ? 12.841  0.898   9.938   1.00 25.03  ? 153 PHE A CE1   1 
ATOM   1259 C  CE2   . PHE A 1 181 ? 14.919  1.971   9.318   1.00 21.68  ? 153 PHE A CE2   1 
ATOM   1260 C  CZ    . PHE A 1 181 ? 14.209  0.814   9.626   1.00 26.03  ? 153 PHE A CZ    1 
ATOM   1261 N  N     . PHE A 1 182 ? 10.278  3.066   7.283   1.00 18.92  ? 154 PHE A N     1 
ATOM   1262 C  CA    . PHE A 1 182 ? 9.500   1.846   7.072   1.00 21.61  ? 154 PHE A CA    1 
ATOM   1263 C  C     . PHE A 1 182 ? 10.447  0.758   6.600   1.00 24.86  ? 154 PHE A C     1 
ATOM   1264 O  O     . PHE A 1 182 ? 11.093  0.906   5.561   1.00 23.91  ? 154 PHE A O     1 
ATOM   1265 C  CB    . PHE A 1 182 ? 8.407   2.028   6.009   1.00 23.19  ? 154 PHE A CB    1 
ATOM   1266 C  CG    . PHE A 1 182 ? 7.310   2.927   6.415   1.00 28.76  ? 154 PHE A CG    1 
ATOM   1267 C  CD1   . PHE A 1 182 ? 6.315   2.487   7.270   1.00 28.14  ? 154 PHE A CD1   1 
ATOM   1268 C  CD2   . PHE A 1 182 ? 7.255   4.222   5.936   1.00 28.57  ? 154 PHE A CD2   1 
ATOM   1269 C  CE1   . PHE A 1 182 ? 5.280   3.333   7.633   1.00 34.84  ? 154 PHE A CE1   1 
ATOM   1270 C  CE2   . PHE A 1 182 ? 6.208   5.062   6.287   1.00 30.68  ? 154 PHE A CE2   1 
ATOM   1271 C  CZ    . PHE A 1 182 ? 5.240   4.622   7.136   1.00 26.89  ? 154 PHE A CZ    1 
ATOM   1272 N  N     . SER A 1 183 ? 10.506  -0.341  7.326   1.00 24.43  ? 155 SER A N     1 
ATOM   1273 C  CA    . SER A 1 183 ? 11.211  -1.517  6.846   1.00 26.51  ? 155 SER A CA    1 
ATOM   1274 C  C     . SER A 1 183 ? 10.250  -2.696  6.836   1.00 28.82  ? 155 SER A C     1 
ATOM   1275 O  O     . SER A 1 183 ? 9.285   -2.726  7.597   1.00 30.48  ? 155 SER A O     1 
ATOM   1276 C  CB    . SER A 1 183 ? 12.423  -1.838  7.720   1.00 27.53  ? 155 SER A CB    1 
ATOM   1277 O  OG    . SER A 1 183 ? 12.004  -2.258  9.015   1.00 30.71  ? 155 SER A OG    1 
ATOM   1278 N  N     . ASP A 1 184 ? 10.516  -3.689  5.985   1.00 25.55  ? 156 ASP A N     1 
ATOM   1279 C  CA    . ASP A 1 184 ? 9.711   -4.898  6.038   1.00 24.29  ? 156 ASP A CA    1 
ATOM   1280 C  C     . ASP A 1 184 ? 10.584  -6.096  5.669   1.00 31.27  ? 156 ASP A C     1 
ATOM   1281 O  O     . ASP A 1 184 ? 11.776  -5.963  5.365   1.00 27.31  ? 156 ASP A O     1 
ATOM   1282 C  CB    . ASP A 1 184 ? 8.456   -4.740  5.164   1.00 27.32  ? 156 ASP A CB    1 
ATOM   1283 C  CG    . ASP A 1 184 ? 8.697   -5.034  3.697   1.00 31.51  ? 156 ASP A CG    1 
ATOM   1284 O  OD1   . ASP A 1 184 ? 9.712   -4.598  3.116   1.00 38.52  ? 156 ASP A OD1   1 
ATOM   1285 O  OD2   . ASP A 1 184 ? 7.834   -5.712  3.113   1.00 41.46  ? 156 ASP A OD2   1 
ATOM   1286 N  N     . ILE A 1 185 ? 9.996   -7.284  5.749   1.00 26.58  ? 157 ILE A N     1 
ATOM   1287 C  CA    . ILE A 1 185 ? 10.727  -8.530  5.574   1.00 25.32  ? 157 ILE A CA    1 
ATOM   1288 C  C     . ILE A 1 185 ? 10.496  -9.000  4.150   1.00 26.39  ? 157 ILE A C     1 
ATOM   1289 O  O     . ILE A 1 185 ? 9.351   -9.117  3.723   1.00 27.50  ? 157 ILE A O     1 
ATOM   1290 C  CB    . ILE A 1 185 ? 10.265  -9.598  6.580   1.00 28.83  ? 157 ILE A CB    1 
ATOM   1291 C  CG1   . ILE A 1 185 ? 10.646  -9.195  8.014   1.00 25.00  ? 157 ILE A CG1   1 
ATOM   1292 C  CG2   . ILE A 1 185 ? 10.921  -10.946 6.220   1.00 23.39  ? 157 ILE A CG2   1 
ATOM   1293 C  CD1   . ILE A 1 185 ? 10.293  -10.248 9.070   1.00 25.90  ? 157 ILE A CD1   1 
ATOM   1294 N  N     . VAL A 1 186 ? 11.577  -9.264  3.410   1.00 27.42  ? 158 VAL A N     1 
ATOM   1295 C  CA    . VAL A 1 186 ? 11.425  -9.692  2.021   1.00 28.66  ? 158 VAL A CA    1 
ATOM   1296 C  C     . VAL A 1 186 ? 10.753  -11.049 1.995   1.00 28.52  ? 158 VAL A C     1 
ATOM   1297 O  O     . VAL A 1 186 ? 11.145  -11.964 2.726   1.00 26.32  ? 158 VAL A O     1 
ATOM   1298 C  CB    . VAL A 1 186 ? 12.776  -9.735  1.308   1.00 28.92  ? 158 VAL A CB    1 
ATOM   1299 C  CG1   . VAL A 1 186 ? 12.588  -10.309 -0.133  1.00 29.22  ? 158 VAL A CG1   1 
ATOM   1300 C  CG2   . VAL A 1 186 ? 13.400  -8.341  1.304   1.00 23.24  ? 158 VAL A CG2   1 
ATOM   1301 N  N     . SER A 1 187 ? 9.675   -11.157 1.215   1.00 27.74  ? 159 SER A N     1 
ATOM   1302 C  CA    . SER A 1 187 ? 9.028   -12.438 0.978   1.00 30.69  ? 159 SER A CA    1 
ATOM   1303 C  C     . SER A 1 187 ? 8.558   -13.063 2.286   1.00 27.83  ? 159 SER A C     1 
ATOM   1304 O  O     . SER A 1 187 ? 8.665   -14.268 2.497   1.00 30.08  ? 159 SER A O     1 
ATOM   1305 C  CB    . SER A 1 187 ? 9.976   -13.369 0.221   1.00 33.67  ? 159 SER A CB    1 
ATOM   1306 O  OG    . SER A 1 187 ? 9.249   -14.301 -0.542  1.00 48.29  ? 159 SER A OG    1 
ATOM   1307 N  N     . PHE A 1 188 ? 8.013   -12.230 3.172   1.00 23.10  ? 160 PHE A N     1 
ATOM   1308 C  CA    . PHE A 1 188 ? 7.592   -12.727 4.471   1.00 29.24  ? 160 PHE A CA    1 
ATOM   1309 C  C     . PHE A 1 188 ? 6.563   -13.845 4.368   1.00 28.95  ? 160 PHE A C     1 
ATOM   1310 O  O     . PHE A 1 188 ? 6.554   -14.752 5.206   1.00 30.85  ? 160 PHE A O     1 
ATOM   1311 C  CB    . PHE A 1 188 ? 7.008   -11.601 5.295   1.00 30.27  ? 160 PHE A CB    1 
ATOM   1312 C  CG    . PHE A 1 188 ? 6.405   -12.072 6.547   1.00 35.93  ? 160 PHE A CG    1 
ATOM   1313 C  CD1   . PHE A 1 188 ? 7.214   -12.425 7.608   1.00 34.59  ? 160 PHE A CD1   1 
ATOM   1314 C  CD2   . PHE A 1 188 ? 5.031   -12.203 6.669   1.00 37.06  ? 160 PHE A CD2   1 
ATOM   1315 C  CE1   . PHE A 1 188 ? 6.654   -12.884 8.776   1.00 39.26  ? 160 PHE A CE1   1 
ATOM   1316 C  CE2   . PHE A 1 188 ? 4.478   -12.673 7.838   1.00 40.63  ? 160 PHE A CE2   1 
ATOM   1317 C  CZ    . PHE A 1 188 ? 5.292   -12.999 8.889   1.00 30.95  ? 160 PHE A CZ    1 
ATOM   1318 N  N     . SER A 1 189 ? 5.680   -13.791 3.365   1.00 29.03  ? 161 SER A N     1 
ATOM   1319 C  CA    . SER A 1 189 ? 4.638   -14.799 3.244   1.00 37.37  ? 161 SER A CA    1 
ATOM   1320 C  C     . SER A 1 189 ? 5.221   -16.191 3.047   1.00 35.16  ? 161 SER A C     1 
ATOM   1321 O  O     . SER A 1 189 ? 4.584   -17.177 3.424   1.00 35.48  ? 161 SER A O     1 
ATOM   1322 C  CB    . SER A 1 189 ? 3.704   -14.444 2.084   1.00 36.26  ? 161 SER A CB    1 
ATOM   1323 O  OG    . SER A 1 189 ? 4.472   -14.112 0.942   1.00 39.65  ? 161 SER A OG    1 
ATOM   1324 N  N     . THR A 1 190 ? 6.430   -16.294 2.469   1.00 30.29  ? 162 THR A N     1 
ATOM   1325 C  CA    . THR A 1 190 ? 7.069   -17.603 2.307   1.00 31.30  ? 162 THR A CA    1 
ATOM   1326 C  C     . THR A 1 190 ? 7.398   -18.242 3.654   1.00 32.70  ? 162 THR A C     1 
ATOM   1327 O  O     . THR A 1 190 ? 7.252   -19.456 3.821   1.00 36.81  ? 162 THR A O     1 
ATOM   1328 C  CB    . THR A 1 190 ? 8.345   -17.483 1.468   1.00 31.83  ? 162 THR A CB    1 
ATOM   1329 O  OG1   . THR A 1 190 ? 8.081   -16.749 0.274   1.00 37.37  ? 162 THR A OG1   1 
ATOM   1330 C  CG2   . THR A 1 190 ? 8.891   -18.852 1.111   1.00 35.34  ? 162 THR A CG2   1 
ATOM   1331 N  N     . PHE A 1 191 ? 7.873   -17.455 4.620   1.00 31.02  ? 163 PHE A N     1 
ATOM   1332 C  CA    . PHE A 1 191 ? 8.110   -18.014 5.949   1.00 33.61  ? 163 PHE A CA    1 
ATOM   1333 C  C     . PHE A 1 191 ? 6.840   -18.645 6.504   1.00 36.36  ? 163 PHE A C     1 
ATOM   1334 O  O     . PHE A 1 191 ? 6.831   -19.821 6.898   1.00 30.07  ? 163 PHE A O     1 
ATOM   1335 C  CB    . PHE A 1 191 ? 8.611   -16.931 6.901   1.00 28.07  ? 163 PHE A CB    1 
ATOM   1336 C  CG    . PHE A 1 191 ? 9.987   -16.413 6.573   1.00 28.04  ? 163 PHE A CG    1 
ATOM   1337 C  CD1   . PHE A 1 191 ? 10.172  -15.516 5.548   1.00 20.83  ? 163 PHE A CD1   1 
ATOM   1338 C  CD2   . PHE A 1 191 ? 11.098  -16.841 7.297   1.00 25.64  ? 163 PHE A CD2   1 
ATOM   1339 C  CE1   . PHE A 1 191 ? 11.435  -15.036 5.254   1.00 31.92  ? 163 PHE A CE1   1 
ATOM   1340 C  CE2   . PHE A 1 191 ? 12.365  -16.373 7.008   1.00 24.89  ? 163 PHE A CE2   1 
ATOM   1341 C  CZ    . PHE A 1 191 ? 12.540  -15.471 5.985   1.00 25.72  ? 163 PHE A CZ    1 
ATOM   1342 N  N     . ALA A 1 192 ? 5.751   -17.867 6.535   1.00 28.67  ? 164 ALA A N     1 
ATOM   1343 C  CA    . ALA A 1 192 ? 4.488   -18.367 7.066   1.00 40.18  ? 164 ALA A CA    1 
ATOM   1344 C  C     . ALA A 1 192 ? 4.032   -19.617 6.327   1.00 34.59  ? 164 ALA A C     1 
ATOM   1345 O  O     . ALA A 1 192 ? 3.488   -20.540 6.936   1.00 41.19  ? 164 ALA A O     1 
ATOM   1346 C  CB    . ALA A 1 192 ? 3.419   -17.276 6.984   1.00 39.18  ? 164 ALA A CB    1 
ATOM   1347 N  N     . GLU A 1 193 ? 4.272   -19.678 5.021   1.00 35.14  ? 165 GLU A N     1 
ATOM   1348 C  CA    . GLU A 1 193 ? 3.815   -20.824 4.252   1.00 38.46  ? 165 GLU A CA    1 
ATOM   1349 C  C     . GLU A 1 193 ? 4.685   -22.056 4.447   1.00 41.63  ? 165 GLU A C     1 
ATOM   1350 O  O     . GLU A 1 193 ? 4.188   -23.175 4.291   1.00 43.08  ? 165 GLU A O     1 
ATOM   1351 C  CB    . GLU A 1 193 ? 3.746   -20.459 2.769   1.00 36.53  ? 165 GLU A CB    1 
ATOM   1352 C  CG    . GLU A 1 193 ? 2.510   -19.636 2.413   1.00 43.24  ? 165 GLU A CG    1 
ATOM   1353 C  CD    . GLU A 1 193 ? 2.700   -18.760 1.190   1.00 54.32  ? 165 GLU A CD    1 
ATOM   1354 O  OE1   . GLU A 1 193 ? 3.794   -18.802 0.581   1.00 54.34  ? 165 GLU A OE1   1 
ATOM   1355 O  OE2   . GLU A 1 193 ? 1.745   -18.024 0.842   1.00 59.86  ? 165 GLU A OE2   1 
ATOM   1356 N  N     . LYS A 1 194 ? 5.965   -21.896 4.778   1.00 35.52  ? 166 LYS A N     1 
ATOM   1357 C  CA    . LYS A 1 194 ? 6.860   -23.044 4.789   1.00 36.13  ? 166 LYS A CA    1 
ATOM   1358 C  C     . LYS A 1 194 ? 7.304   -23.492 6.171   1.00 38.54  ? 166 LYS A C     1 
ATOM   1359 O  O     . LYS A 1 194 ? 7.817   -24.608 6.303   1.00 35.38  ? 166 LYS A O     1 
ATOM   1360 C  CB    . LYS A 1 194 ? 8.100   -22.748 3.942   1.00 36.05  ? 166 LYS A CB    1 
ATOM   1361 C  CG    . LYS A 1 194 ? 7.756   -22.392 2.533   1.00 38.66  ? 166 LYS A CG    1 
ATOM   1362 C  CD    . LYS A 1 194 ? 8.549   -23.207 1.527   1.00 51.94  ? 166 LYS A CD    1 
ATOM   1363 C  CE    . LYS A 1 194 ? 8.037   -22.953 0.112   1.00 44.70  ? 166 LYS A CE    1 
ATOM   1364 N  NZ    . LYS A 1 194 ? 7.479   -24.197 -0.488  1.00 60.44  ? 166 LYS A NZ    1 
ATOM   1365 N  N     . LEU A 1 195 ? 7.126   -22.672 7.191   1.00 35.38  ? 167 LEU A N     1 
ATOM   1366 C  CA    . LEU A 1 195 ? 7.667   -23.002 8.494   1.00 30.33  ? 167 LEU A CA    1 
ATOM   1367 C  C     . LEU A 1 195 ? 6.543   -23.187 9.497   1.00 34.85  ? 167 LEU A C     1 
ATOM   1368 O  O     . LEU A 1 195 ? 5.500   -22.535 9.388   1.00 35.50  ? 167 LEU A O     1 
ATOM   1369 C  CB    . LEU A 1 195 ? 8.589   -21.900 9.028   1.00 36.09  ? 167 LEU A CB    1 
ATOM   1370 C  CG    . LEU A 1 195 ? 9.798   -21.436 8.231   1.00 32.51  ? 167 LEU A CG    1 
ATOM   1371 C  CD1   . LEU A 1 195 ? 10.563  -20.383 9.035   1.00 32.44  ? 167 LEU A CD1   1 
ATOM   1372 C  CD2   . LEU A 1 195 ? 10.680  -22.642 7.940   1.00 39.43  ? 167 LEU A CD2   1 
ATOM   1373 N  N     . PRO A 1 196 ? 6.743   -24.024 10.509  1.00 40.11  ? 168 PRO A N     1 
ATOM   1374 C  CA    . PRO A 1 196 ? 5.811   -24.032 11.632  1.00 37.64  ? 168 PRO A CA    1 
ATOM   1375 C  C     . PRO A 1 196 ? 5.729   -22.653 12.268  1.00 39.06  ? 168 PRO A C     1 
ATOM   1376 O  O     . PRO A 1 196 ? 6.681   -21.868 12.256  1.00 37.68  ? 168 PRO A O     1 
ATOM   1377 C  CB    . PRO A 1 196 ? 6.409   -25.067 12.589  1.00 42.67  ? 168 PRO A CB    1 
ATOM   1378 C  CG    . PRO A 1 196 ? 7.816   -25.220 12.167  1.00 43.44  ? 168 PRO A CG    1 
ATOM   1379 C  CD    . PRO A 1 196 ? 7.866   -24.954 10.712  1.00 36.82  ? 168 PRO A CD    1 
ATOM   1380 N  N     . VAL A 1 197 ? 4.556   -22.369 12.821  1.00 37.28  ? 169 VAL A N     1 
ATOM   1381 C  CA    . VAL A 1 197 ? 4.216   -21.027 13.269  1.00 30.35  ? 169 VAL A CA    1 
ATOM   1382 C  C     . VAL A 1 197 ? 5.163   -20.535 14.358  1.00 33.16  ? 169 VAL A C     1 
ATOM   1383 O  O     . VAL A 1 197 ? 5.500   -19.345 14.404  1.00 31.17  ? 169 VAL A O     1 
ATOM   1384 C  CB    . VAL A 1 197 ? 2.740   -21.034 13.722  1.00 34.04  ? 169 VAL A CB    1 
ATOM   1385 C  CG1   . VAL A 1 197 ? 2.563   -21.938 14.925  1.00 34.81  ? 169 VAL A CG1   1 
ATOM   1386 C  CG2   . VAL A 1 197 ? 2.270   -19.643 14.031  1.00 36.71  ? 169 VAL A CG2   1 
ATOM   1387 N  N     . GLU A 1 198 ? 5.638   -21.431 15.229  1.00 35.75  ? 170 GLU A N     1 
ATOM   1388 C  CA    . GLU A 1 198 ? 6.546   -20.998 16.286  1.00 32.14  ? 170 GLU A CA    1 
ATOM   1389 C  C     . GLU A 1 198 ? 7.857   -20.474 15.706  1.00 33.46  ? 170 GLU A C     1 
ATOM   1390 O  O     . GLU A 1 198 ? 8.479   -19.568 16.283  1.00 31.25  ? 170 GLU A O     1 
ATOM   1391 C  CB    . GLU A 1 198 ? 6.811   -22.139 17.276  1.00 39.31  ? 170 GLU A CB    1 
ATOM   1392 C  CG    . GLU A 1 198 ? 7.273   -23.454 16.644  1.00 45.65  ? 170 GLU A CG    1 
ATOM   1393 C  CD    . GLU A 1 198 ? 6.137   -24.393 16.231  1.00 52.91  ? 170 GLU A CD    1 
ATOM   1394 O  OE1   . GLU A 1 198 ? 4.940   -24.025 16.336  1.00 51.73  ? 170 GLU A OE1   1 
ATOM   1395 O  OE2   . GLU A 1 198 ? 6.457   -25.524 15.793  1.00 62.76  ? 170 GLU A OE2   1 
ATOM   1396 N  N     . GLU A 1 199 ? 8.264   -20.999 14.552  1.00 36.31  ? 171 GLU A N     1 
ATOM   1397 C  CA    . GLU A 1 199 ? 9.510   -20.577 13.917  1.00 33.27  ? 171 GLU A CA    1 
ATOM   1398 C  C     . GLU A 1 199 ? 9.356   -19.256 13.164  1.00 37.12  ? 171 GLU A C     1 
ATOM   1399 O  O     . GLU A 1 199 ? 10.315  -18.468 13.106  1.00 30.81  ? 171 GLU A O     1 
ATOM   1400 C  CB    . GLU A 1 199 ? 10.006  -21.680 12.979  1.00 36.04  ? 171 GLU A CB    1 
ATOM   1401 C  CG    . GLU A 1 199 ? 10.767  -22.793 13.718  1.00 43.66  ? 171 GLU A CG    1 
ATOM   1402 C  CD    . GLU A 1 199 ? 11.226  -23.923 12.809  1.00 61.87  ? 171 GLU A CD    1 
ATOM   1403 O  OE1   . GLU A 1 199 ? 11.105  -25.096 13.220  1.00 70.97  ? 171 GLU A OE1   1 
ATOM   1404 O  OE2   . GLU A 1 199 ? 11.759  -23.644 11.707  1.00 55.71  ? 171 GLU A OE2   1 
ATOM   1405 N  N     . VAL A 1 200 ? 8.177   -19.008 12.573  1.00 28.24  ? 172 VAL A N     1 
ATOM   1406 C  CA    . VAL A 1 200 ? 7.863   -17.686 12.026  1.00 30.76  ? 172 VAL A CA    1 
ATOM   1407 C  C     . VAL A 1 200 ? 7.957   -16.631 13.114  1.00 27.17  ? 172 VAL A C     1 
ATOM   1408 O  O     . VAL A 1 200 ? 8.569   -15.568 12.934  1.00 31.10  ? 172 VAL A O     1 
ATOM   1409 C  CB    . VAL A 1 200 ? 6.458   -17.675 11.384  1.00 34.91  ? 172 VAL A CB    1 
ATOM   1410 C  CG1   . VAL A 1 200 ? 6.170   -16.317 10.799  1.00 28.02  ? 172 VAL A CG1   1 
ATOM   1411 C  CG2   . VAL A 1 200 ? 6.312   -18.746 10.314  1.00 27.82  ? 172 VAL A CG2   1 
ATOM   1412 N  N     . VAL A 1 201 ? 7.304   -16.884 14.247  1.00 26.57  ? 173 VAL A N     1 
ATOM   1413 C  CA    . VAL A 1 201 ? 7.391   -15.940 15.352  1.00 24.82  ? 173 VAL A CA    1 
ATOM   1414 C  C     . VAL A 1 201 ? 8.849   -15.705 15.732  1.00 25.92  ? 173 VAL A C     1 
ATOM   1415 O  O     . VAL A 1 201 ? 9.265   -14.570 15.989  1.00 29.96  ? 173 VAL A O     1 
ATOM   1416 C  CB    . VAL A 1 201 ? 6.561   -16.450 16.542  1.00 27.05  ? 173 VAL A CB    1 
ATOM   1417 C  CG1   . VAL A 1 201 ? 6.972   -15.744 17.842  1.00 27.79  ? 173 VAL A CG1   1 
ATOM   1418 C  CG2   . VAL A 1 201 ? 5.096   -16.226 16.255  1.00 31.13  ? 173 VAL A CG2   1 
ATOM   1419 N  N     . SER A 1 202 ? 9.646   -16.771 15.789  1.00 27.99  ? 174 SER A N     1 
ATOM   1420 C  CA    . SER A 1 202 ? 11.042  -16.602 16.167  1.00 30.16  ? 174 SER A CA    1 
ATOM   1421 C  C     . SER A 1 202 ? 11.764  -15.684 15.185  1.00 28.57  ? 174 SER A C     1 
ATOM   1422 O  O     . SER A 1 202 ? 12.494  -14.775 15.600  1.00 29.08  ? 174 SER A O     1 
ATOM   1423 C  CB    . SER A 1 202 ? 11.729  -17.963 16.250  1.00 35.62  ? 174 SER A CB    1 
ATOM   1424 O  OG    . SER A 1 202 ? 13.081  -17.811 16.639  1.00 36.90  ? 174 SER A OG    1 
ATOM   1425 N  N     . VAL A 1 203 ? 11.517  -15.858 13.879  1.00 26.80  ? 175 VAL A N     1 
ATOM   1426 C  CA    . VAL A 1 203 ? 12.164  -15.005 12.877  1.00 27.02  ? 175 VAL A CA    1 
ATOM   1427 C  C     . VAL A 1 203 ? 11.695  -13.558 12.998  1.00 28.37  ? 175 VAL A C     1 
ATOM   1428 O  O     . VAL A 1 203 ? 12.505  -12.629 12.946  1.00 24.74  ? 175 VAL A O     1 
ATOM   1429 C  CB    . VAL A 1 203 ? 11.922  -15.553 11.462  1.00 26.82  ? 175 VAL A CB    1 
ATOM   1430 C  CG1   . VAL A 1 203 ? 12.373  -14.546 10.419  1.00 28.65  ? 175 VAL A CG1   1 
ATOM   1431 C  CG2   . VAL A 1 203 ? 12.687  -16.856 11.290  1.00 31.70  ? 175 VAL A CG2   1 
ATOM   1432 N  N     . VAL A 1 204 ? 10.384  -13.323 13.121  1.00 26.94  ? 176 VAL A N     1 
ATOM   1433 C  CA    . VAL A 1 204 ? 9.949   -11.928 13.145  1.00 25.31  ? 176 VAL A CA    1 
ATOM   1434 C  C     . VAL A 1 204 ? 10.474  -11.246 14.396  1.00 25.02  ? 176 VAL A C     1 
ATOM   1435 O  O     . VAL A 1 204 ? 10.837  -10.070 14.369  1.00 28.24  ? 176 VAL A O     1 
ATOM   1436 C  CB    . VAL A 1 204 ? 8.414   -11.805 13.015  1.00 34.97  ? 176 VAL A CB    1 
ATOM   1437 C  CG1   . VAL A 1 204 ? 7.910   -12.594 11.846  1.00 29.07  ? 176 VAL A CG1   1 
ATOM   1438 C  CG2   . VAL A 1 204 ? 7.702   -12.211 14.279  1.00 27.50  ? 176 VAL A CG2   1 
ATOM   1439 N  N     . ASN A 1 205 ? 10.552  -11.985 15.509  1.00 31.08  ? 177 ASN A N     1 
ATOM   1440 C  CA    . ASN A 1 205 ? 11.085  -11.411 16.741  1.00 31.20  ? 177 ASN A CA    1 
ATOM   1441 C  C     . ASN A 1 205 ? 12.553  -11.045 16.590  1.00 26.86  ? 177 ASN A C     1 
ATOM   1442 O  O     . ASN A 1 205 ? 12.984  -9.994  17.070  1.00 31.04  ? 177 ASN A O     1 
ATOM   1443 C  CB    . ASN A 1 205 ? 10.897  -12.381 17.909  1.00 33.42  ? 177 ASN A CB    1 
ATOM   1444 C  CG    . ASN A 1 205 ? 9.467   -12.414 18.422  1.00 33.50  ? 177 ASN A CG    1 
ATOM   1445 O  OD1   . ASN A 1 205 ? 8.580   -11.721 17.908  1.00 30.95  ? 177 ASN A OD1   1 
ATOM   1446 N  ND2   . ASN A 1 205 ? 9.238   -13.220 19.456  1.00 31.72  ? 177 ASN A ND2   1 
ATOM   1447 N  N     . SER A 1 206 ? 13.344  -11.917 15.959  1.00 27.49  ? 178 SER A N     1 
ATOM   1448 C  CA    . SER A 1 206 ? 14.742  -11.582 15.706  1.00 29.02  ? 178 SER A CA    1 
ATOM   1449 C  C     . SER A 1 206 ? 14.839  -10.323 14.858  1.00 30.51  ? 178 SER A C     1 
ATOM   1450 O  O     . SER A 1 206 ? 15.712  -9.477  15.082  1.00 24.98  ? 178 SER A O     1 
ATOM   1451 C  CB    . SER A 1 206 ? 15.461  -12.734 15.004  1.00 27.99  ? 178 SER A CB    1 
ATOM   1452 O  OG    . SER A 1 206 ? 15.632  -13.852 15.854  1.00 31.45  ? 178 SER A OG    1 
ATOM   1453 N  N     . TYR A 1 207 ? 13.936  -10.187 13.879  1.00 26.33  ? 179 TYR A N     1 
ATOM   1454 C  CA    . TYR A 1 207 ? 13.920  -9.024  13.000  1.00 19.06  ? 179 TYR A CA    1 
ATOM   1455 C  C     . TYR A 1 207 ? 13.519  -7.775  13.756  1.00 26.44  ? 179 TYR A C     1 
ATOM   1456 O  O     . TYR A 1 207 ? 14.214  -6.754  13.698  1.00 26.95  ? 179 TYR A O     1 
ATOM   1457 C  CB    . TYR A 1 207 ? 12.948  -9.274  11.844  1.00 22.35  ? 179 TYR A CB    1 
ATOM   1458 C  CG    . TYR A 1 207 ? 12.764  -8.095  10.928  1.00 24.30  ? 179 TYR A CG    1 
ATOM   1459 C  CD1   . TYR A 1 207 ? 13.806  -7.665  10.141  1.00 24.61  ? 179 TYR A CD1   1 
ATOM   1460 C  CD2   . TYR A 1 207 ? 11.552  -7.425  10.846  1.00 30.72  ? 179 TYR A CD2   1 
ATOM   1461 C  CE1   . TYR A 1 207 ? 13.668  -6.606  9.297   1.00 35.22  ? 179 TYR A CE1   1 
ATOM   1462 C  CE2   . TYR A 1 207 ? 11.405  -6.339  9.979   1.00 31.09  ? 179 TYR A CE2   1 
ATOM   1463 C  CZ    . TYR A 1 207 ? 12.472  -5.951  9.218   1.00 22.20  ? 179 TYR A CZ    1 
ATOM   1464 O  OH    . TYR A 1 207 ? 12.405  -4.881  8.351   1.00 38.06  ? 179 TYR A OH    1 
ATOM   1465 N  N     . PHE A 1 208 ? 12.389  -7.831  14.472  1.00 21.94  ? 180 PHE A N     1 
ATOM   1466 C  CA    . PHE A 1 208 ? 11.962  -6.658  15.228  1.00 22.55  ? 180 PHE A CA    1 
ATOM   1467 C  C     . PHE A 1 208 ? 13.008  -6.252  16.255  1.00 24.57  ? 180 PHE A C     1 
ATOM   1468 O  O     . PHE A 1 208 ? 13.179  -5.060  16.521  1.00 26.51  ? 180 PHE A O     1 
ATOM   1469 C  CB    . PHE A 1 208 ? 10.630  -6.921  15.938  1.00 27.30  ? 180 PHE A CB    1 
ATOM   1470 C  CG    . PHE A 1 208 ? 9.440   -6.935  15.035  1.00 30.92  ? 180 PHE A CG    1 
ATOM   1471 C  CD1   . PHE A 1 208 ? 9.428   -6.227  13.850  1.00 29.99  ? 180 PHE A CD1   1 
ATOM   1472 C  CD2   . PHE A 1 208 ? 8.330   -7.682  15.369  1.00 26.31  ? 180 PHE A CD2   1 
ATOM   1473 C  CE1   . PHE A 1 208 ? 8.305   -6.243  13.016  1.00 30.81  ? 180 PHE A CE1   1 
ATOM   1474 C  CE2   . PHE A 1 208 ? 7.207   -7.700  14.544  1.00 32.56  ? 180 PHE A CE2   1 
ATOM   1475 C  CZ    . PHE A 1 208 ? 7.202   -6.980  13.367  1.00 28.39  ? 180 PHE A CZ    1 
ATOM   1476 N  N     . SER A 1 209 ? 13.729  -7.214  16.833  1.00 28.16  ? 181 SER A N     1 
ATOM   1477 C  CA    . SER A 1 209 ? 14.719  -6.850  17.848  1.00 28.14  ? 181 SER A CA    1 
ATOM   1478 C  C     . SER A 1 209 ? 15.883  -6.081  17.233  1.00 26.63  ? 181 SER A C     1 
ATOM   1479 O  O     . SER A 1 209 ? 16.345  -5.081  17.800  1.00 25.12  ? 181 SER A O     1 
ATOM   1480 C  CB    . SER A 1 209 ? 15.230  -8.105  18.550  1.00 33.99  ? 181 SER A CB    1 
ATOM   1481 O  OG    . SER A 1 209 ? 14.208  -8.661  19.359  1.00 38.54  ? 181 SER A OG    1 
ATOM   1482 N  N     . VAL A 1 210 ? 16.368  -6.539  16.073  1.00 23.67  ? 182 VAL A N     1 
ATOM   1483 C  CA    . VAL A 1 210 ? 17.497  -5.882  15.408  1.00 26.02  ? 182 VAL A CA    1 
ATOM   1484 C  C     . VAL A 1 210 ? 17.121  -4.456  15.055  1.00 27.02  ? 182 VAL A C     1 
ATOM   1485 O  O     . VAL A 1 210 ? 17.849  -3.504  15.361  1.00 25.65  ? 182 VAL A O     1 
ATOM   1486 C  CB    . VAL A 1 210 ? 17.927  -6.672  14.152  1.00 25.95  ? 182 VAL A CB    1 
ATOM   1487 C  CG1   . VAL A 1 210 ? 18.872  -5.824  13.251  1.00 27.02  ? 182 VAL A CG1   1 
ATOM   1488 C  CG2   . VAL A 1 210 ? 18.592  -7.968  14.528  1.00 28.45  ? 182 VAL A CG2   1 
ATOM   1489 N  N     . CYS A 1 211 ? 15.952  -4.293  14.428  1.00 24.71  ? 183 CYS A N     1 
ATOM   1490 C  CA    . CYS A 1 211 ? 15.508  -2.971  14.001  1.00 25.23  ? 183 CYS A CA    1 
ATOM   1491 C  C     . CYS A 1 211 ? 15.357  -2.048  15.193  1.00 23.35  ? 183 CYS A C     1 
ATOM   1492 O  O     . CYS A 1 211 ? 15.892  -0.933  15.198  1.00 29.23  ? 183 CYS A O     1 
ATOM   1493 C  CB    . CYS A 1 211 ? 14.184  -3.081  13.231  1.00 23.18  ? 183 CYS A CB    1 
ATOM   1494 S  SG    . CYS A 1 211 ? 14.369  -4.002  11.650  1.00 24.66  ? 183 CYS A SG    1 
ATOM   1495 N  N     . THR A 1 212 ? 14.645  -2.509  16.228  1.00 23.13  ? 184 THR A N     1 
ATOM   1496 C  CA    . THR A 1 212 ? 14.307  -1.640  17.351  1.00 25.76  ? 184 THR A CA    1 
ATOM   1497 C  C     . THR A 1 212 ? 15.552  -1.160  18.099  1.00 26.37  ? 184 THR A C     1 
ATOM   1498 O  O     . THR A 1 212 ? 15.662  0.032   18.436  1.00 28.72  ? 184 THR A O     1 
ATOM   1499 C  CB    . THR A 1 212 ? 13.340  -2.374  18.290  1.00 26.24  ? 184 THR A CB    1 
ATOM   1500 O  OG1   . THR A 1 212 ? 12.118  -2.659  17.580  1.00 29.54  ? 184 THR A OG1   1 
ATOM   1501 C  CG2   . THR A 1 212 ? 13.035  -1.517  19.506  1.00 35.48  ? 184 THR A CG2   1 
ATOM   1502 N  N     . ALA A 1 213 ? 16.509  -2.062  18.344  1.00 27.44  ? 185 ALA A N     1 
ATOM   1503 C  CA    . ALA A 1 213 ? 17.739  -1.680  19.049  1.00 31.04  ? 185 ALA A CA    1 
ATOM   1504 C  C     . ALA A 1 213 ? 18.526  -0.627  18.278  1.00 24.33  ? 185 ALA A C     1 
ATOM   1505 O  O     . ALA A 1 213 ? 18.981  0.365   18.856  1.00 26.84  ? 185 ALA A O     1 
ATOM   1506 C  CB    . ALA A 1 213 ? 18.617  -2.903  19.292  1.00 31.18  ? 185 ALA A CB    1 
ATOM   1507 N  N     . ILE A 1 214 ? 18.656  -0.798  16.960  1.00 25.88  ? 186 ILE A N     1 
ATOM   1508 C  CA    . ILE A 1 214 ? 19.469  0.134   16.184  1.00 27.61  ? 186 ILE A CA    1 
ATOM   1509 C  C     . ILE A 1 214 ? 18.771  1.482   16.034  1.00 27.87  ? 186 ILE A C     1 
ATOM   1510 O  O     . ILE A 1 214 ? 19.409  2.538   16.154  1.00 26.74  ? 186 ILE A O     1 
ATOM   1511 C  CB    . ILE A 1 214 ? 19.835  -0.486  14.826  1.00 25.83  ? 186 ILE A CB    1 
ATOM   1512 C  CG1   . ILE A 1 214 ? 20.782  -1.666  15.039  1.00 29.50  ? 186 ILE A CG1   1 
ATOM   1513 C  CG2   . ILE A 1 214 ? 20.530  0.533   13.927  1.00 25.01  ? 186 ILE A CG2   1 
ATOM   1514 C  CD1   . ILE A 1 214 ? 21.126  -2.373  13.757  1.00 27.79  ? 186 ILE A CD1   1 
ATOM   1515 N  N     . ILE A 1 215 ? 17.462  1.478   15.746  1.00 24.48  ? 187 ILE A N     1 
ATOM   1516 C  CA    . ILE A 1 215 ? 16.714  2.737   15.643  1.00 24.84  ? 187 ILE A CA    1 
ATOM   1517 C  C     . ILE A 1 215 ? 16.820  3.532   16.941  1.00 24.93  ? 187 ILE A C     1 
ATOM   1518 O  O     . ILE A 1 215 ? 17.080  4.745   16.936  1.00 26.31  ? 187 ILE A O     1 
ATOM   1519 C  CB    . ILE A 1 215 ? 15.245  2.460   15.274  1.00 27.13  ? 187 ILE A CB    1 
ATOM   1520 C  CG1   . ILE A 1 215 ? 15.142  2.044   13.812  1.00 22.31  ? 187 ILE A CG1   1 
ATOM   1521 C  CG2   . ILE A 1 215 ? 14.360  3.701   15.518  1.00 27.27  ? 187 ILE A CG2   1 
ATOM   1522 C  CD1   . ILE A 1 215 ? 13.802  1.433   13.486  1.00 22.72  ? 187 ILE A CD1   1 
ATOM   1523 N  N     . THR A 1 216 ? 16.636  2.851   18.074  1.00 23.59  ? 188 THR A N     1 
ATOM   1524 C  CA    . THR A 1 216 ? 16.738  3.515   19.372  1.00 30.08  ? 188 THR A CA    1 
ATOM   1525 C  C     . THR A 1 216 ? 18.147  4.032   19.616  1.00 30.22  ? 188 THR A C     1 
ATOM   1526 O  O     . THR A 1 216 ? 18.332  5.178   20.035  1.00 30.24  ? 188 THR A O     1 
ATOM   1527 C  CB    . THR A 1 216 ? 16.329  2.551   20.481  1.00 31.28  ? 188 THR A CB    1 
ATOM   1528 O  OG1   . THR A 1 216 ? 15.003  2.075   20.224  1.00 30.22  ? 188 THR A OG1   1 
ATOM   1529 C  CG2   . THR A 1 216 ? 16.376  3.248   21.828  1.00 41.55  ? 188 THR A CG2   1 
ATOM   1530 N  N     . ARG A 1 217 ? 19.160  3.202   19.343  1.00 27.31  ? 189 ARG A N     1 
ATOM   1531 C  CA    . ARG A 1 217 ? 20.542  3.657   19.468  1.00 32.48  ? 189 ARG A CA    1 
ATOM   1532 C  C     . ARG A 1 217 ? 20.771  4.938   18.678  1.00 32.90  ? 189 ARG A C     1 
ATOM   1533 O  O     . ARG A 1 217 ? 21.517  5.825   19.118  1.00 30.42  ? 189 ARG A O     1 
ATOM   1534 C  CB    . ARG A 1 217 ? 21.502  2.555   19.004  1.00 37.57  ? 189 ARG A CB    1 
ATOM   1535 C  CG    . ARG A 1 217 ? 22.939  2.807   19.386  1.00 42.17  ? 189 ARG A CG    1 
ATOM   1536 C  CD    . ARG A 1 217 ? 23.907  2.543   18.254  1.00 53.04  ? 189 ARG A CD    1 
ATOM   1537 N  NE    . ARG A 1 217 ? 23.900  1.159   17.787  1.00 53.88  ? 189 ARG A NE    1 
ATOM   1538 C  CZ    . ARG A 1 217 ? 23.994  0.802   16.510  1.00 49.20  ? 189 ARG A CZ    1 
ATOM   1539 N  NH1   . ARG A 1 217 ? 23.959  1.700   15.533  1.00 46.86  ? 189 ARG A NH1   1 
ATOM   1540 N  NH2   . ARG A 1 217 ? 24.138  -0.485  16.205  1.00 51.19  ? 189 ARG A NH2   1 
ATOM   1541 N  N     . GLN A 1 218 ? 20.122  5.066   17.516  1.00 27.15  ? 190 GLN A N     1 
ATOM   1542 C  CA    . GLN A 1 218 ? 20.360  6.198   16.627  1.00 25.59  ? 190 GLN A CA    1 
ATOM   1543 C  C     . GLN A 1 218 ? 19.437  7.376   16.907  1.00 26.35  ? 190 GLN A C     1 
ATOM   1544 O  O     . GLN A 1 218 ? 19.445  8.360   16.152  1.00 30.23  ? 190 GLN A O     1 
ATOM   1545 C  CB    . GLN A 1 218 ? 20.226  5.748   15.174  1.00 29.47  ? 190 GLN A CB    1 
ATOM   1546 C  CG    . GLN A 1 218 ? 21.422  4.894   14.710  1.00 26.43  ? 190 GLN A CG    1 
ATOM   1547 C  CD    . GLN A 1 218 ? 22.726  5.678   14.646  1.00 38.38  ? 190 GLN A CD    1 
ATOM   1548 O  OE1   . GLN A 1 218 ? 22.732  6.900   14.482  1.00 33.53  ? 190 GLN A OE1   1 
ATOM   1549 N  NE2   . GLN A 1 218 ? 23.842  4.968   14.775  1.00 39.36  ? 190 GLN A NE2   1 
ATOM   1550 N  N     . GLY A 1 219 ? 18.673  7.315   17.990  1.00 29.06  ? 191 GLY A N     1 
ATOM   1551 C  CA    . GLY A 1 219 ? 17.854  8.424   18.423  1.00 28.84  ? 191 GLY A CA    1 
ATOM   1552 C  C     . GLY A 1 219 ? 16.477  8.480   17.813  1.00 32.26  ? 191 GLY A C     1 
ATOM   1553 O  O     . GLY A 1 219 ? 15.784  9.489   17.982  1.00 34.06  ? 191 GLY A O     1 
ATOM   1554 N  N     . GLY A 1 220 ? 16.070  7.455   17.073  1.00 31.31  ? 192 GLY A N     1 
ATOM   1555 C  CA    . GLY A 1 220 ? 14.719  7.381   16.570  1.00 28.72  ? 192 GLY A CA    1 
ATOM   1556 C  C     . GLY A 1 220 ? 13.842  6.634   17.538  1.00 33.15  ? 192 GLY A C     1 
ATOM   1557 O  O     . GLY A 1 220 ? 14.285  6.129   18.564  1.00 30.80  ? 192 GLY A O     1 
ATOM   1558 N  N     . GLU A 1 221 ? 12.565  6.540   17.198  1.00 29.74  ? 193 GLU A N     1 
ATOM   1559 C  CA    . GLU A 1 221 ? 11.658  5.757   18.029  1.00 37.37  ? 193 GLU A CA    1 
ATOM   1560 C  C     . GLU A 1 221 ? 10.731  4.936   17.145  1.00 33.54  ? 193 GLU A C     1 
ATOM   1561 O  O     . GLU A 1 221 ? 10.189  5.446   16.158  1.00 27.09  ? 193 GLU A O     1 
ATOM   1562 C  CB    . GLU A 1 221 ? 10.848  6.652   18.982  1.00 34.87  ? 193 GLU A CB    1 
ATOM   1563 C  CG    . GLU A 1 221 ? 9.786   7.538   18.325  1.00 47.47  ? 193 GLU A CG    1 
ATOM   1564 C  CD    . GLU A 1 221 ? 9.500   8.836   19.107  1.00 69.79  ? 193 GLU A CD    1 
ATOM   1565 O  OE1   . GLU A 1 221 ? 8.513   8.865   19.877  1.00 73.45  ? 193 GLU A OE1   1 
ATOM   1566 O  OE2   . GLU A 1 221 ? 10.256  9.826   18.947  1.00 70.49  ? 193 GLU A OE2   1 
ATOM   1567 N  N     . VAL A 1 222 ? 10.560  3.665   17.494  1.00 25.01  ? 194 VAL A N     1 
ATOM   1568 C  CA    . VAL A 1 222 ? 9.611   2.810   16.794  1.00 28.53  ? 194 VAL A CA    1 
ATOM   1569 C  C     . VAL A 1 222 ? 8.210   3.174   17.274  1.00 36.34  ? 194 VAL A C     1 
ATOM   1570 O  O     . VAL A 1 222 ? 7.953   3.229   18.484  1.00 32.29  ? 194 VAL A O     1 
ATOM   1571 C  CB    . VAL A 1 222 ? 9.934   1.322   17.045  1.00 31.16  ? 194 VAL A CB    1 
ATOM   1572 C  CG1   . VAL A 1 222 ? 8.779   0.424   16.598  1.00 30.52  ? 194 VAL A CG1   1 
ATOM   1573 C  CG2   . VAL A 1 222 ? 11.208  0.914   16.319  1.00 29.44  ? 194 VAL A CG2   1 
ATOM   1574 N  N     . THR A 1 223 ? 7.308   3.477   16.338  1.00 33.44  ? 195 THR A N     1 
ATOM   1575 C  CA    . THR A 1 223 ? 5.944   3.820   16.714  1.00 29.67  ? 195 THR A CA    1 
ATOM   1576 C  C     . THR A 1 223 ? 4.984   2.663   16.599  1.00 35.70  ? 195 THR A C     1 
ATOM   1577 O  O     . THR A 1 223 ? 4.047   2.587   17.392  1.00 33.41  ? 195 THR A O     1 
ATOM   1578 C  CB    . THR A 1 223 ? 5.390   4.974   15.878  1.00 43.62  ? 195 THR A CB    1 
ATOM   1579 O  OG1   . THR A 1 223 ? 5.608   4.721   14.483  1.00 42.98  ? 195 THR A OG1   1 
ATOM   1580 C  CG2   . THR A 1 223 ? 6.056   6.216   16.276  1.00 35.62  ? 195 THR A CG2   1 
ATOM   1581 N  N     . LYS A 1 224 ? 5.189   1.758   15.647  1.00 32.23  ? 196 LYS A N     1 
ATOM   1582 C  CA    . LYS A 1 224 ? 4.349   0.574   15.610  1.00 35.81  ? 196 LYS A CA    1 
ATOM   1583 C  C     . LYS A 1 224 ? 4.908   -0.433  14.622  1.00 30.73  ? 196 LYS A C     1 
ATOM   1584 O  O     . LYS A 1 224 ? 5.721   -0.110  13.759  1.00 27.75  ? 196 LYS A O     1 
ATOM   1585 C  CB    . LYS A 1 224 ? 2.905   0.915   15.238  1.00 39.10  ? 196 LYS A CB    1 
ATOM   1586 C  CG    . LYS A 1 224 ? 2.752   1.635   13.936  1.00 30.38  ? 196 LYS A CG    1 
ATOM   1587 C  CD    . LYS A 1 224 ? 1.337   2.239   13.826  1.00 41.15  ? 196 LYS A CD    1 
ATOM   1588 C  CE    . LYS A 1 224 ? 1.047   3.196   14.978  1.00 36.91  ? 196 LYS A CE    1 
ATOM   1589 N  NZ    . LYS A 1 224 ? -0.280  3.858   14.898  1.00 34.65  ? 196 LYS A NZ    1 
ATOM   1590 N  N     . PHE A 1 225 ? 4.446   -1.659  14.776  1.00 25.29  ? 197 PHE A N     1 
ATOM   1591 C  CA    . PHE A 1 225 ? 4.596   -2.710  13.794  1.00 28.12  ? 197 PHE A CA    1 
ATOM   1592 C  C     . PHE A 1 225 ? 3.290   -2.821  13.019  1.00 32.60  ? 197 PHE A C     1 
ATOM   1593 O  O     . PHE A 1 225 ? 2.212   -2.875  13.619  1.00 30.57  ? 197 PHE A O     1 
ATOM   1594 C  CB    . PHE A 1 225 ? 4.927   -4.035  14.481  1.00 26.92  ? 197 PHE A CB    1 
ATOM   1595 C  CG    . PHE A 1 225 ? 6.132   -3.964  15.383  1.00 33.09  ? 197 PHE A CG    1 
ATOM   1596 C  CD1   . PHE A 1 225 ? 7.313   -3.355  14.951  1.00 29.29  ? 197 PHE A CD1   1 
ATOM   1597 C  CD2   . PHE A 1 225 ? 6.078   -4.477  16.670  1.00 32.59  ? 197 PHE A CD2   1 
ATOM   1598 C  CE1   . PHE A 1 225 ? 8.433   -3.280  15.796  1.00 32.35  ? 197 PHE A CE1   1 
ATOM   1599 C  CE2   . PHE A 1 225 ? 7.187   -4.401  17.513  1.00 37.08  ? 197 PHE A CE2   1 
ATOM   1600 C  CZ    . PHE A 1 225 ? 8.360   -3.810  17.073  1.00 34.18  ? 197 PHE A CZ    1 
ATOM   1601 N  N     . ILE A 1 226 ? 3.386   -2.821  11.699  1.00 30.42  ? 198 ILE A N     1 
ATOM   1602 C  CA    . ILE A 1 226 ? 2.243   -3.062  10.824  1.00 31.06  ? 198 ILE A CA    1 
ATOM   1603 C  C     . ILE A 1 226 ? 2.554   -4.367  10.110  1.00 28.71  ? 198 ILE A C     1 
ATOM   1604 O  O     . ILE A 1 226 ? 3.326   -4.375  9.146   1.00 25.64  ? 198 ILE A O     1 
ATOM   1605 C  CB    . ILE A 1 226 ? 2.028   -1.920  9.827   1.00 35.68  ? 198 ILE A CB    1 
ATOM   1606 C  CG1   . ILE A 1 226 ? 1.998   -0.565  10.534  1.00 33.53  ? 198 ILE A CG1   1 
ATOM   1607 C  CG2   . ILE A 1 226 ? 0.754   -2.138  9.041   1.00 29.86  ? 198 ILE A CG2   1 
ATOM   1608 C  CD1   . ILE A 1 226 ? 2.481   0.568   9.621   1.00 30.79  ? 198 ILE A CD1   1 
ATOM   1609 N  N     . GLY A 1 227 ? 1.991   -5.468  10.590  1.00 27.16  ? 199 GLY A N     1 
ATOM   1610 C  CA    . GLY A 1 227 ? 2.445   -6.764  10.125  1.00 25.92  ? 199 GLY A CA    1 
ATOM   1611 C  C     . GLY A 1 227 ? 3.954   -6.894  10.316  1.00 28.41  ? 199 GLY A C     1 
ATOM   1612 O  O     . GLY A 1 227 ? 4.500   -6.591  11.382  1.00 23.19  ? 199 GLY A O     1 
ATOM   1613 N  N     . ASP A 1 228 ? 4.652   -7.336  9.277   1.00 29.11  ? 200 ASP A N     1 
ATOM   1614 C  CA    . ASP A 1 228 ? 6.110   -7.432  9.344   1.00 24.45  ? 200 ASP A CA    1 
ATOM   1615 C  C     . ASP A 1 228 ? 6.794   -6.101  9.098   1.00 27.72  ? 200 ASP A C     1 
ATOM   1616 O  O     . ASP A 1 228 ? 8.024   -6.061  8.985   1.00 28.26  ? 200 ASP A O     1 
ATOM   1617 C  CB    . ASP A 1 228 ? 6.627   -8.459  8.331   1.00 26.52  ? 200 ASP A CB    1 
ATOM   1618 C  CG    . ASP A 1 228 ? 6.264   -8.097  6.910   1.00 30.72  ? 200 ASP A CG    1 
ATOM   1619 O  OD1   . ASP A 1 228 ? 5.079   -7.889  6.635   1.00 27.74  ? 200 ASP A OD1   1 
ATOM   1620 O  OD2   . ASP A 1 228 ? 7.169   -8.013  6.063   1.00 30.06  ? 200 ASP A OD2   1 
ATOM   1621 N  N     . CYS A 1 229 ? 6.040   -5.016  8.995   1.00 26.01  ? 201 CYS A N     1 
ATOM   1622 C  CA    . CYS A 1 229 ? 6.616   -3.701  8.750   1.00 24.53  ? 201 CYS A CA    1 
ATOM   1623 C  C     . CYS A 1 229 ? 6.903   -2.959  10.055  1.00 29.67  ? 201 CYS A C     1 
ATOM   1624 O  O     . CYS A 1 229 ? 6.032   -2.836  10.925  1.00 28.41  ? 201 CYS A O     1 
ATOM   1625 C  CB    . CYS A 1 229 ? 5.685   -2.876  7.866   1.00 28.48  ? 201 CYS A CB    1 
ATOM   1626 S  SG    . CYS A 1 229 ? 6.210   -1.183  7.753   1.00 35.16  ? 201 CYS A SG    1 
ATOM   1627 N  N     . VAL A 1 230 ? 8.135   -2.478  10.188  1.00 24.28  ? 202 VAL A N     1 
ATOM   1628 C  CA    . VAL A 1 230 ? 8.551   -1.623  11.293  1.00 27.93  ? 202 VAL A CA    1 
ATOM   1629 C  C     . VAL A 1 230 ? 8.387   -0.174  10.861  1.00 25.18  ? 202 VAL A C     1 
ATOM   1630 O  O     . VAL A 1 230 ? 8.972   0.241   9.857   1.00 26.50  ? 202 VAL A O     1 
ATOM   1631 C  CB    . VAL A 1 230 ? 10.012  -1.907  11.689  1.00 28.29  ? 202 VAL A CB    1 
ATOM   1632 C  CG1   . VAL A 1 230 ? 10.493  -0.899  12.687  1.00 26.12  ? 202 VAL A CG1   1 
ATOM   1633 C  CG2   . VAL A 1 230 ? 10.151  -3.312  12.253  1.00 27.60  ? 202 VAL A CG2   1 
ATOM   1634 N  N     . MET A 1 231 ? 7.618   0.604   11.625  1.00 24.12  ? 203 MET A N     1 
ATOM   1635 C  CA    . MET A 1 231 ? 7.420   2.029   11.375  1.00 21.03  ? 203 MET A CA    1 
ATOM   1636 C  C     . MET A 1 231 ? 8.089   2.850   12.478  1.00 24.25  ? 203 MET A C     1 
ATOM   1637 O  O     . MET A 1 231 ? 7.875   2.590   13.666  1.00 27.31  ? 203 MET A O     1 
ATOM   1638 C  CB    . MET A 1 231 ? 5.923   2.370   11.316  1.00 25.66  ? 203 MET A CB    1 
ATOM   1639 C  CG    . MET A 1 231 ? 5.638   3.849   11.046  1.00 26.00  ? 203 MET A CG    1 
ATOM   1640 S  SD    . MET A 1 231 ? 3.821   4.188   11.039  1.00 34.47  ? 203 MET A SD    1 
ATOM   1641 C  CE    . MET A 1 231 ? 3.856   5.969   11.043  1.00 34.25  ? 203 MET A CE    1 
ATOM   1642 N  N     . ALA A 1 232 ? 8.859   3.869   12.095  1.00 22.08  ? 204 ALA A N     1 
ATOM   1643 C  CA    . ALA A 1 232 ? 9.617   4.617   13.089  1.00 24.64  ? 204 ALA A CA    1 
ATOM   1644 C  C     . ALA A 1 232 ? 9.751   6.066   12.651  1.00 25.61  ? 204 ALA A C     1 
ATOM   1645 O  O     . ALA A 1 232 ? 9.608   6.411   11.475  1.00 25.04  ? 204 ALA A O     1 
ATOM   1646 C  CB    . ALA A 1 232 ? 11.011  4.011   13.325  1.00 22.57  ? 204 ALA A CB    1 
ATOM   1647 N  N     . TYR A 1 233 ? 10.014  6.912   13.624  1.00 20.77  ? 205 TYR A N     1 
ATOM   1648 C  CA    . TYR A 1 233 ? 10.214  8.327   13.394  1.00 25.04  ? 205 TYR A CA    1 
ATOM   1649 C  C     . TYR A 1 233 ? 11.614  8.707   13.811  1.00 26.05  ? 205 TYR A C     1 
ATOM   1650 O  O     . TYR A 1 233 ? 12.122  8.207   14.810  1.00 25.23  ? 205 TYR A O     1 
ATOM   1651 C  CB    . TYR A 1 233 ? 9.246   9.173   14.210  1.00 28.03  ? 205 TYR A CB    1 
ATOM   1652 C  CG    . TYR A 1 233 ? 7.806   9.062   13.808  1.00 31.89  ? 205 TYR A CG    1 
ATOM   1653 C  CD1   . TYR A 1 233 ? 7.438   8.953   12.476  1.00 28.94  ? 205 TYR A CD1   1 
ATOM   1654 C  CD2   . TYR A 1 233 ? 6.805   9.041   14.775  1.00 34.59  ? 205 TYR A CD2   1 
ATOM   1655 C  CE1   . TYR A 1 233 ? 6.081   8.852   12.106  1.00 30.22  ? 205 TYR A CE1   1 
ATOM   1656 C  CE2   . TYR A 1 233 ? 5.459   8.935   14.424  1.00 35.86  ? 205 TYR A CE2   1 
ATOM   1657 C  CZ    . TYR A 1 233 ? 5.111   8.830   13.090  1.00 38.09  ? 205 TYR A CZ    1 
ATOM   1658 O  OH    . TYR A 1 233 ? 3.789   8.719   12.752  1.00 40.00  ? 205 TYR A OH    1 
ATOM   1659 N  N     . PHE A 1 234 ? 12.208  9.608   13.056  1.00 28.61  ? 206 PHE A N     1 
ATOM   1660 C  CA    . PHE A 1 234 ? 13.369  10.372  13.466  1.00 28.98  ? 206 PHE A CA    1 
ATOM   1661 C  C     . PHE A 1 234 ? 12.965  11.840  13.423  1.00 31.98  ? 206 PHE A C     1 
ATOM   1662 O  O     . PHE A 1 234 ? 12.078  12.207  12.657  1.00 32.17  ? 206 PHE A O     1 
ATOM   1663 C  CB    . PHE A 1 234 ? 14.565  10.096  12.533  1.00 25.52  ? 206 PHE A CB    1 
ATOM   1664 C  CG    . PHE A 1 234 ? 15.165  8.726   12.700  1.00 23.83  ? 206 PHE A CG    1 
ATOM   1665 C  CD1   . PHE A 1 234 ? 14.600  7.616   12.079  1.00 23.92  ? 206 PHE A CD1   1 
ATOM   1666 C  CD2   . PHE A 1 234 ? 16.303  8.547   13.486  1.00 26.42  ? 206 PHE A CD2   1 
ATOM   1667 C  CE1   . PHE A 1 234 ? 15.161  6.351   12.241  1.00 23.94  ? 206 PHE A CE1   1 
ATOM   1668 C  CE2   . PHE A 1 234 ? 16.867  7.274   13.653  1.00 28.24  ? 206 PHE A CE2   1 
ATOM   1669 C  CZ    . PHE A 1 234 ? 16.298  6.183   13.027  1.00 25.05  ? 206 PHE A CZ    1 
ATOM   1670 N  N     . ASP A 1 235 ? 13.585  12.675  14.264  1.00 30.83  ? 207 ASP A N     1 
ATOM   1671 C  CA    . ASP A 1 235 ? 13.369  14.117  14.181  1.00 34.63  ? 207 ASP A CA    1 
ATOM   1672 C  C     . ASP A 1 235 ? 13.624  14.608  12.760  1.00 34.25  ? 207 ASP A C     1 
ATOM   1673 O  O     . ASP A 1 235 ? 14.438  14.045  12.028  1.00 35.14  ? 207 ASP A O     1 
ATOM   1674 C  CB    . ASP A 1 235 ? 14.296  14.866  15.144  1.00 39.73  ? 207 ASP A CB    1 
ATOM   1675 C  CG    . ASP A 1 235 ? 13.910  14.679  16.604  1.00 44.93  ? 207 ASP A CG    1 
ATOM   1676 O  OD1   . ASP A 1 235 ? 12.768  14.245  16.868  1.00 45.90  ? 207 ASP A OD1   1 
ATOM   1677 O  OD2   . ASP A 1 235 ? 14.750  14.980  17.491  1.00 55.19  ? 207 ASP A OD2   1 
ATOM   1678 N  N     . GLY A 1 236 ? 12.921  15.675  12.363  1.00 32.45  ? 208 GLY A N     1 
ATOM   1679 C  CA    . GLY A 1 236 ? 12.995  16.126  10.984  1.00 30.35  ? 208 GLY A CA    1 
ATOM   1680 C  C     . GLY A 1 236 ? 14.380  16.550  10.537  1.00 37.68  ? 208 GLY A C     1 
ATOM   1681 O  O     . GLY A 1 236 ? 14.665  16.547  9.335   1.00 41.92  ? 208 GLY A O     1 
ATOM   1682 N  N     . ASP A 1 237 ? 15.249  16.915  11.473  1.00 38.93  ? 209 ASP A N     1 
ATOM   1683 C  CA    . ASP A 1 237 ? 16.613  17.297  11.149  1.00 39.26  ? 209 ASP A CA    1 
ATOM   1684 C  C     . ASP A 1 237 ? 17.610  16.157  11.346  1.00 39.60  ? 209 ASP A C     1 
ATOM   1685 O  O     . ASP A 1 237 ? 18.819  16.385  11.244  1.00 44.18  ? 209 ASP A O     1 
ATOM   1686 C  CB    . ASP A 1 237 ? 17.026  18.524  11.976  1.00 42.37  ? 209 ASP A CB    1 
ATOM   1687 C  CG    . ASP A 1 237 ? 17.161  18.225  13.468  1.00 52.76  ? 209 ASP A CG    1 
ATOM   1688 O  OD1   . ASP A 1 237 ? 16.369  17.421  14.011  1.00 57.51  ? 209 ASP A OD1   1 
ATOM   1689 O  OD2   . ASP A 1 237 ? 18.063  18.807  14.110  1.00 63.69  ? 209 ASP A OD2   1 
ATOM   1690 N  N     . CYS A 1 238 ? 17.146  14.929  11.572  1.00 36.31  ? 210 CYS A N     1 
ATOM   1691 C  CA    . CYS A 1 238 ? 18.047  13.817  11.862  1.00 32.17  ? 210 CYS A CA    1 
ATOM   1692 C  C     . CYS A 1 238 ? 18.099  12.783  10.742  1.00 29.36  ? 210 CYS A C     1 
ATOM   1693 O  O     . CYS A 1 238 ? 18.199  11.584  10.998  1.00 25.96  ? 210 CYS A O     1 
ATOM   1694 C  CB    . CYS A 1 238 ? 17.678  13.147  13.177  1.00 33.41  ? 210 CYS A CB    1 
ATOM   1695 S  SG    . CYS A 1 238 ? 18.018  14.155  14.617  1.00 43.79  ? 210 CYS A SG    1 
ATOM   1696 N  N     . ALA A 1 239 ? 18.077  13.243  9.489   1.00 29.04  ? 211 ALA A N     1 
ATOM   1697 C  CA    . ALA A 1 239 ? 18.148  12.319  8.360   1.00 34.11  ? 211 ALA A CA    1 
ATOM   1698 C  C     . ALA A 1 239 ? 19.442  11.520  8.378   1.00 25.00  ? 211 ALA A C     1 
ATOM   1699 O  O     . ALA A 1 239 ? 19.455  10.347  7.996   1.00 24.27  ? 211 ALA A O     1 
ATOM   1700 C  CB    . ALA A 1 239 ? 18.028  13.075  7.031   1.00 25.41  ? 211 ALA A CB    1 
ATOM   1701 N  N     . ASP A 1 240 ? 20.541  12.150  8.794   1.00 25.07  ? 212 ASP A N     1 
ATOM   1702 C  CA    . ASP A 1 240 ? 21.820  11.445  8.862   1.00 31.52  ? 212 ASP A CA    1 
ATOM   1703 C  C     . ASP A 1 240 ? 21.723  10.231  9.771   1.00 25.58  ? 212 ASP A C     1 
ATOM   1704 O  O     . ASP A 1 240 ? 22.269  9.169   9.460   1.00 27.49  ? 212 ASP A O     1 
ATOM   1705 C  CB    . ASP A 1 240 ? 22.914  12.388  9.348   1.00 32.37  ? 212 ASP A CB    1 
ATOM   1706 C  CG    . ASP A 1 240 ? 23.248  13.453  8.334   1.00 35.11  ? 212 ASP A CG    1 
ATOM   1707 O  OD1   . ASP A 1 240 ? 23.565  13.096  7.184   1.00 36.68  ? 212 ASP A OD1   1 
ATOM   1708 O  OD2   . ASP A 1 240 ? 23.186  14.654  8.683   1.00 40.11  ? 212 ASP A OD2   1 
ATOM   1709 N  N     . GLN A 1 241 ? 20.995  10.366  10.887  1.00 26.68  ? 213 GLN A N     1 
ATOM   1710 C  CA    . GLN A 1 241 ? 20.836  9.270   11.833  1.00 23.67  ? 213 GLN A CA    1 
ATOM   1711 C  C     . GLN A 1 241 ? 19.926  8.190   11.269  1.00 26.08  ? 213 GLN A C     1 
ATOM   1712 O  O     . GLN A 1 241 ? 20.141  6.995   11.501  1.00 28.69  ? 213 GLN A O     1 
ATOM   1713 C  CB    . GLN A 1 241 ? 20.258  9.802   13.152  1.00 23.69  ? 213 GLN A CB    1 
ATOM   1714 C  CG    . GLN A 1 241 ? 21.275  10.509  14.067  1.00 31.84  ? 213 GLN A CG    1 
ATOM   1715 C  CD    . GLN A 1 241 ? 21.829  11.776  13.461  1.00 41.74  ? 213 GLN A CD    1 
ATOM   1716 O  OE1   . GLN A 1 241 ? 21.076  12.664  13.020  1.00 39.85  ? 213 GLN A OE1   1 
ATOM   1717 N  NE2   . GLN A 1 241 ? 23.159  11.872  13.418  1.00 37.94  ? 213 GLN A NE2   1 
ATOM   1718 N  N     . ALA A 1 242 ? 18.871  8.596   10.568  1.00 25.76  ? 214 ALA A N     1 
ATOM   1719 C  CA    . ALA A 1 242 ? 17.991  7.618   9.935   1.00 25.11  ? 214 ALA A CA    1 
ATOM   1720 C  C     . ALA A 1 242 ? 18.731  6.824   8.862   1.00 22.80  ? 214 ALA A C     1 
ATOM   1721 O  O     . ALA A 1 242 ? 18.526  5.614   8.733   1.00 25.05  ? 214 ALA A O     1 
ATOM   1722 C  CB    . ALA A 1 242 ? 16.763  8.315   9.342   1.00 20.66  ? 214 ALA A CB    1 
ATOM   1723 N  N     . ILE A 1 243 ? 19.588  7.483   8.078   1.00 20.55  ? 215 ILE A N     1 
ATOM   1724 C  CA    . ILE A 1 243 ? 20.373  6.748   7.088   1.00 21.73  ? 215 ILE A CA    1 
ATOM   1725 C  C     . ILE A 1 243 ? 21.355  5.806   7.772   1.00 23.88  ? 215 ILE A C     1 
ATOM   1726 O  O     . ILE A 1 243 ? 21.497  4.637   7.381   1.00 22.46  ? 215 ILE A O     1 
ATOM   1727 C  CB    . ILE A 1 243 ? 21.091  7.714   6.128   1.00 24.35  ? 215 ILE A CB    1 
ATOM   1728 C  CG1   . ILE A 1 243 ? 20.067  8.439   5.229   1.00 25.63  ? 215 ILE A CG1   1 
ATOM   1729 C  CG2   . ILE A 1 243 ? 22.073  6.950   5.230   1.00 21.65  ? 215 ILE A CG2   1 
ATOM   1730 C  CD1   . ILE A 1 243 ? 20.631  9.724   4.571   1.00 24.22  ? 215 ILE A CD1   1 
ATOM   1731 N  N     . GLN A 1 244 ? 22.042  6.288   8.805   1.00 26.46  ? 216 GLN A N     1 
ATOM   1732 C  CA    . GLN A 1 244 ? 22.989  5.426   9.506   1.00 27.82  ? 216 GLN A CA    1 
ATOM   1733 C  C     . GLN A 1 244 ? 22.272  4.241   10.123  1.00 24.13  ? 216 GLN A C     1 
ATOM   1734 O  O     . GLN A 1 244 ? 22.746  3.104   10.040  1.00 24.72  ? 216 GLN A O     1 
ATOM   1735 C  CB    . GLN A 1 244 ? 23.729  6.213   10.593  1.00 21.92  ? 216 GLN A CB    1 
ATOM   1736 C  CG    . GLN A 1 244 ? 24.880  5.450   11.191  1.00 27.00  ? 216 GLN A CG    1 
ATOM   1737 C  CD    . GLN A 1 244 ? 25.976  5.254   10.167  1.00 31.64  ? 216 GLN A CD    1 
ATOM   1738 O  OE1   . GLN A 1 244 ? 26.659  6.210   9.783   1.00 35.10  ? 216 GLN A OE1   1 
ATOM   1739 N  NE2   . GLN A 1 244 ? 26.111  4.034   9.675   1.00 29.36  ? 216 GLN A NE2   1 
ATOM   1740 N  N     . ALA A 1 245 ? 21.122  4.489   10.752  1.00 22.47  ? 217 ALA A N     1 
ATOM   1741 C  CA    . ALA A 1 245 ? 20.339  3.384   11.299  1.00 23.86  ? 217 ALA A CA    1 
ATOM   1742 C  C     . ALA A 1 245 ? 19.997  2.365   10.226  1.00 20.94  ? 217 ALA A C     1 
ATOM   1743 O  O     . ALA A 1 245 ? 20.121  1.158   10.452  1.00 22.07  ? 217 ALA A O     1 
ATOM   1744 C  CB    . ALA A 1 245 ? 19.069  3.909   11.972  1.00 20.67  ? 217 ALA A CB    1 
ATOM   1745 N  N     . SER A 1 246 ? 19.589  2.825   9.042   1.00 18.84  ? 218 SER A N     1 
ATOM   1746 C  CA    . SER A 1 246 ? 19.246  1.897   7.962   1.00 21.05  ? 218 SER A CA    1 
ATOM   1747 C  C     . SER A 1 246 ? 20.440  1.052   7.548   1.00 22.42  ? 218 SER A C     1 
ATOM   1748 O  O     . SER A 1 246 ? 20.329  -0.171  7.381   1.00 20.27  ? 218 SER A O     1 
ATOM   1749 C  CB    . SER A 1 246 ? 18.718  2.685   6.763   1.00 20.16  ? 218 SER A CB    1 
ATOM   1750 O  OG    . SER A 1 246 ? 17.559  3.424   7.135   1.00 22.77  ? 218 SER A OG    1 
ATOM   1751 N  N     . LEU A 1 247 ? 21.590  1.696   7.346   1.00 20.58  ? 219 LEU A N     1 
ATOM   1752 C  CA    . LEU A 1 247 ? 22.792  0.954   6.981   1.00 26.78  ? 219 LEU A CA    1 
ATOM   1753 C  C     . LEU A 1 247 ? 23.173  -0.035  8.072   1.00 22.03  ? 219 LEU A C     1 
ATOM   1754 O  O     . LEU A 1 247 ? 23.524  -1.187  7.783   1.00 25.90  ? 219 LEU A O     1 
ATOM   1755 C  CB    . LEU A 1 247 ? 23.927  1.937   6.699   1.00 23.98  ? 219 LEU A CB    1 
ATOM   1756 C  CG    . LEU A 1 247 ? 23.650  2.756   5.431   1.00 27.86  ? 219 LEU A CG    1 
ATOM   1757 C  CD1   . LEU A 1 247 ? 24.623  3.921   5.295   1.00 28.05  ? 219 LEU A CD1   1 
ATOM   1758 C  CD2   . LEU A 1 247 ? 23.713  1.860   4.209   1.00 27.04  ? 219 LEU A CD2   1 
ATOM   1759 N  N     . ASP A 1 248 ? 23.116  0.396   9.339   1.00 24.11  ? 220 ASP A N     1 
ATOM   1760 C  CA    . ASP A 1 248 ? 23.486  -0.491  10.434  1.00 26.51  ? 220 ASP A CA    1 
ATOM   1761 C  C     . ASP A 1 248 ? 22.560  -1.699  10.494  1.00 25.16  ? 220 ASP A C     1 
ATOM   1762 O  O     . ASP A 1 248 ? 23.013  -2.827  10.723  1.00 23.51  ? 220 ASP A O     1 
ATOM   1763 C  CB    . ASP A 1 248 ? 23.473  0.266   11.765  1.00 29.48  ? 220 ASP A CB    1 
ATOM   1764 C  CG    . ASP A 1 248 ? 24.677  1.194   11.921  1.00 33.03  ? 220 ASP A CG    1 
ATOM   1765 O  OD1   . ASP A 1 248 ? 25.569  1.178   11.037  1.00 35.13  ? 220 ASP A OD1   1 
ATOM   1766 O  OD2   . ASP A 1 248 ? 24.720  1.955   12.910  1.00 35.24  ? 220 ASP A OD2   1 
ATOM   1767 N  N     . ILE A 1 249 ? 21.265  -1.497  10.240  1.00 24.16  ? 221 ILE A N     1 
ATOM   1768 C  CA    . ILE A 1 249 ? 20.344  -2.630  10.239  1.00 24.32  ? 221 ILE A CA    1 
ATOM   1769 C  C     . ILE A 1 249 ? 20.715  -3.611  9.139   1.00 20.36  ? 221 ILE A C     1 
ATOM   1770 O  O     . ILE A 1 249 ? 20.755  -4.828  9.353   1.00 24.65  ? 221 ILE A O     1 
ATOM   1771 C  CB    . ILE A 1 249 ? 18.887  -2.146  10.098  1.00 22.60  ? 221 ILE A CB    1 
ATOM   1772 C  CG1   . ILE A 1 249 ? 18.451  -1.456  11.389  1.00 20.42  ? 221 ILE A CG1   1 
ATOM   1773 C  CG2   . ILE A 1 249 ? 17.979  -3.319  9.805   1.00 21.44  ? 221 ILE A CG2   1 
ATOM   1774 C  CD1   . ILE A 1 249 ? 17.015  -0.881  11.300  1.00 25.27  ? 221 ILE A CD1   1 
ATOM   1775 N  N     . LEU A 1 250 ? 20.975  -3.097  7.942   1.00 21.25  ? 222 LEU A N     1 
ATOM   1776 C  CA    . LEU A 1 250 ? 21.337  -3.971  6.840   1.00 25.46  ? 222 LEU A CA    1 
ATOM   1777 C  C     . LEU A 1 250 ? 22.627  -4.714  7.153   1.00 24.79  ? 222 LEU A C     1 
ATOM   1778 O  O     . LEU A 1 250 ? 22.732  -5.920  6.903   1.00 27.39  ? 222 LEU A O     1 
ATOM   1779 C  CB    . LEU A 1 250 ? 21.460  -3.168  5.542   1.00 24.45  ? 222 LEU A CB    1 
ATOM   1780 C  CG    . LEU A 1 250 ? 20.147  -2.537  5.041   1.00 25.78  ? 222 LEU A CG    1 
ATOM   1781 C  CD1   . LEU A 1 250 ? 20.366  -1.758  3.757   1.00 31.81  ? 222 LEU A CD1   1 
ATOM   1782 C  CD2   . LEU A 1 250 ? 19.048  -3.584  4.857   1.00 26.35  ? 222 LEU A CD2   1 
ATOM   1783 N  N     . MET A 1 251 ? 23.606  -4.011  7.723   1.00 21.75  ? 223 MET A N     1 
ATOM   1784 C  CA    A MET A 1 251 ? 24.860  -4.658  8.106   0.49 27.49  ? 223 MET A CA    1 
ATOM   1785 C  CA    B MET A 1 251 ? 24.855  -4.659  8.098   0.51 27.34  ? 223 MET A CA    1 
ATOM   1786 C  C     . MET A 1 251 ? 24.619  -5.766  9.119   1.00 26.26  ? 223 MET A C     1 
ATOM   1787 O  O     . MET A 1 251 ? 25.188  -6.857  9.006   1.00 25.59  ? 223 MET A O     1 
ATOM   1788 C  CB    A MET A 1 251 ? 25.850  -3.632  8.682   0.49 29.58  ? 223 MET A CB    1 
ATOM   1789 C  CB    B MET A 1 251 ? 25.816  -3.608  8.655   0.51 29.58  ? 223 MET A CB    1 
ATOM   1790 C  CG    A MET A 1 251 ? 26.824  -4.232  9.725   0.49 33.21  ? 223 MET A CG    1 
ATOM   1791 C  CG    B MET A 1 251 ? 27.177  -4.118  9.025   0.51 33.49  ? 223 MET A CG    1 
ATOM   1792 S  SD    A MET A 1 251 ? 28.008  -3.071  10.470  0.49 37.18  ? 223 MET A SD    1 
ATOM   1793 S  SD    B MET A 1 251 ? 28.285  -2.710  9.036   0.51 37.20  ? 223 MET A SD    1 
ATOM   1794 C  CE    A MET A 1 251 ? 26.952  -2.188  11.622  0.49 33.49  ? 223 MET A CE    1 
ATOM   1795 C  CE    B MET A 1 251 ? 28.315  -2.287  7.303   0.51 34.83  ? 223 MET A CE    1 
ATOM   1796 N  N     . GLU A 1 252 ? 23.772  -5.508  10.121  1.00 22.29  ? 224 GLU A N     1 
ATOM   1797 C  CA    . GLU A 1 252 ? 23.545  -6.512  11.157  1.00 21.50  ? 224 GLU A CA    1 
ATOM   1798 C  C     . GLU A 1 252 ? 22.757  -7.697  10.632  1.00 26.44  ? 224 GLU A C     1 
ATOM   1799 O  O     . GLU A 1 252 ? 22.956  -8.827  11.094  1.00 22.80  ? 224 GLU A O     1 
ATOM   1800 C  CB    . GLU A 1 252 ? 22.814  -5.893  12.358  1.00 26.28  ? 224 GLU A CB    1 
ATOM   1801 C  CG    . GLU A 1 252 ? 23.649  -4.874  13.074  1.00 36.12  ? 224 GLU A CG    1 
ATOM   1802 C  CD    . GLU A 1 252 ? 24.788  -5.509  13.852  1.00 44.00  ? 224 GLU A CD    1 
ATOM   1803 O  OE1   . GLU A 1 252 ? 24.697  -6.719  14.170  1.00 50.53  ? 224 GLU A OE1   1 
ATOM   1804 O  OE2   . GLU A 1 252 ? 25.773  -4.802  14.142  1.00 48.90  ? 224 GLU A OE2   1 
ATOM   1805 N  N     . LEU A 1 253 ? 21.844  -7.473  9.684   1.00 24.19  ? 225 LEU A N     1 
ATOM   1806 C  CA    . LEU A 1 253 ? 21.121  -8.613  9.139   1.00 21.62  ? 225 LEU A CA    1 
ATOM   1807 C  C     . LEU A 1 253 ? 22.038  -9.475  8.274   1.00 20.85  ? 225 LEU A C     1 
ATOM   1808 O  O     . LEU A 1 253 ? 21.915  -10.701 8.282   1.00 24.92  ? 225 LEU A O     1 
ATOM   1809 C  CB    . LEU A 1 253 ? 19.889  -8.132  8.360   1.00 24.67  ? 225 LEU A CB    1 
ATOM   1810 C  CG    . LEU A 1 253 ? 18.720  -7.607  9.225   1.00 22.74  ? 225 LEU A CG    1 
ATOM   1811 C  CD1   . LEU A 1 253 ? 17.599  -7.065  8.315   1.00 20.22  ? 225 LEU A CD1   1 
ATOM   1812 C  CD2   . LEU A 1 253 ? 18.160  -8.676  10.144  1.00 23.23  ? 225 LEU A CD2   1 
ATOM   1813 N  N     . GLU A 1 254 ? 22.985  -8.866  7.551   1.00 25.46  ? 226 GLU A N     1 
ATOM   1814 C  CA    . GLU A 1 254 ? 23.972  -9.667  6.821   1.00 25.83  ? 226 GLU A CA    1 
ATOM   1815 C  C     . GLU A 1 254 ? 24.791  -10.522 7.780   1.00 23.65  ? 226 GLU A C     1 
ATOM   1816 O  O     . GLU A 1 254 ? 25.000  -11.721 7.540   1.00 25.51  ? 226 GLU A O     1 
ATOM   1817 C  CB    . GLU A 1 254 ? 24.907  -8.776  5.999   1.00 22.21  ? 226 GLU A CB    1 
ATOM   1818 C  CG    . GLU A 1 254 ? 26.050  -9.524  5.277   1.00 25.86  ? 226 GLU A CG    1 
ATOM   1819 C  CD    . GLU A 1 254 ? 25.564  -10.319 4.060   1.00 36.16  ? 226 GLU A CD    1 
ATOM   1820 O  OE1   . GLU A 1 254 ? 26.069  -11.443 3.799   1.00 49.22  ? 226 GLU A OE1   1 
ATOM   1821 O  OE2   . GLU A 1 254 ? 24.662  -9.822  3.350   1.00 46.45  ? 226 GLU A OE2   1 
ATOM   1822 N  N     . ILE A 1 255 ? 25.236  -9.934  8.887   1.00 22.97  ? 227 ILE A N     1 
ATOM   1823 C  CA    . ILE A 1 255 ? 25.979  -10.706 9.885   1.00 24.56  ? 227 ILE A CA    1 
ATOM   1824 C  C     . ILE A 1 255 ? 25.107  -11.803 10.462  1.00 24.61  ? 227 ILE A C     1 
ATOM   1825 O  O     . ILE A 1 255 ? 25.557  -12.944 10.651  1.00 25.46  ? 227 ILE A O     1 
ATOM   1826 C  CB    . ILE A 1 255 ? 26.526  -9.781  10.990  1.00 20.32  ? 227 ILE A CB    1 
ATOM   1827 C  CG1   . ILE A 1 255 ? 27.635  -8.884  10.438  1.00 29.18  ? 227 ILE A CG1   1 
ATOM   1828 C  CG2   . ILE A 1 255 ? 27.042  -10.607 12.164  1.00 30.46  ? 227 ILE A CG2   1 
ATOM   1829 C  CD1   . ILE A 1 255 ? 27.917  -7.659  11.271  1.00 29.19  ? 227 ILE A CD1   1 
ATOM   1830 N  N     . LEU A 1 256 ? 23.840  -11.481 10.746  1.00 27.03  ? 228 LEU A N     1 
ATOM   1831 C  CA    . LEU A 1 256 ? 22.912  -12.487 11.256  1.00 27.33  ? 228 LEU A CA    1 
ATOM   1832 C  C     . LEU A 1 256 ? 22.742  -13.648 10.275  1.00 26.49  ? 228 LEU A C     1 
ATOM   1833 O  O     . LEU A 1 256 ? 22.787  -14.821 10.673  1.00 25.43  ? 228 LEU A O     1 
ATOM   1834 C  CB    . LEU A 1 256 ? 21.565  -11.839 11.563  1.00 24.78  ? 228 LEU A CB    1 
ATOM   1835 C  CG    . LEU A 1 256 ? 20.607  -12.723 12.334  1.00 31.23  ? 228 LEU A CG    1 
ATOM   1836 C  CD1   . LEU A 1 256 ? 21.191  -13.067 13.734  1.00 26.14  ? 228 LEU A CD1   1 
ATOM   1837 C  CD2   . LEU A 1 256 ? 19.262  -11.999 12.485  1.00 29.15  ? 228 LEU A CD2   1 
ATOM   1838 N  N     . ARG A 1 257 ? 22.513  -13.344 8.990   1.00 23.54  ? 229 ARG A N     1 
ATOM   1839 C  CA    . ARG A 1 257 ? 22.400  -14.413 7.989   1.00 26.37  ? 229 ARG A CA    1 
ATOM   1840 C  C     . ARG A 1 257 ? 23.667  -15.267 7.947   1.00 26.34  ? 229 ARG A C     1 
ATOM   1841 O  O     . ARG A 1 257 ? 23.603  -16.501 7.864   1.00 24.99  ? 229 ARG A O     1 
ATOM   1842 C  CB    . ARG A 1 257 ? 22.149  -13.835 6.588   1.00 23.63  ? 229 ARG A CB    1 
ATOM   1843 C  CG    . ARG A 1 257 ? 20.783  -13.228 6.352   1.00 22.66  ? 229 ARG A CG    1 
ATOM   1844 C  CD    . ARG A 1 257 ? 20.576  -12.930 4.881   1.00 22.94  ? 229 ARG A CD    1 
ATOM   1845 N  NE    . ARG A 1 257 ? 21.389  -11.816 4.397   1.00 25.39  ? 229 ARG A NE    1 
ATOM   1846 C  CZ    . ARG A 1 257 ? 21.044  -10.542 4.527   1.00 24.61  ? 229 ARG A CZ    1 
ATOM   1847 N  NH1   . ARG A 1 257 ? 19.929  -10.188 5.157   1.00 22.23  ? 229 ARG A NH1   1 
ATOM   1848 N  NH2   . ARG A 1 257 ? 21.808  -9.605  3.983   1.00 23.05  ? 229 ARG A NH2   1 
ATOM   1849 N  N     . ASN A 1 258 ? 24.829  -14.620 7.936   1.00 22.67  ? 230 ASN A N     1 
ATOM   1850 C  CA    . ASN A 1 258 ? 26.061  -15.372 7.740   1.00 28.24  ? 230 ASN A CA    1 
ATOM   1851 C  C     . ASN A 1 258 ? 26.356  -16.272 8.933   1.00 29.39  ? 230 ASN A C     1 
ATOM   1852 O  O     . ASN A 1 258 ? 26.933  -17.347 8.767   1.00 26.46  ? 230 ASN A O     1 
ATOM   1853 C  CB    . ASN A 1 258 ? 27.241  -14.434 7.505   1.00 29.76  ? 230 ASN A CB    1 
ATOM   1854 C  CG    . ASN A 1 258 ? 27.091  -13.607 6.268   1.00 32.09  ? 230 ASN A CG    1 
ATOM   1855 O  OD1   . ASN A 1 258 ? 26.314  -13.934 5.370   1.00 34.07  ? 230 ASN A OD1   1 
ATOM   1856 N  ND2   . ASN A 1 258 ? 27.830  -12.515 6.208   1.00 33.34  ? 230 ASN A ND2   1 
ATOM   1857 N  N     . SER A 1 259 ? 25.949  -15.862 10.130  1.00 26.78  ? 231 SER A N     1 
ATOM   1858 C  CA    . SER A 1 259 ? 26.429  -16.491 11.344  1.00 31.62  ? 231 SER A CA    1 
ATOM   1859 C  C     . SER A 1 259 ? 25.420  -17.453 11.953  1.00 28.06  ? 231 SER A C     1 
ATOM   1860 O  O     . SER A 1 259 ? 25.743  -18.123 12.934  1.00 28.53  ? 231 SER A O     1 
ATOM   1861 C  CB    . SER A 1 259 ? 26.826  -15.412 12.349  1.00 27.45  ? 231 SER A CB    1 
ATOM   1862 O  OG    . SER A 1 259 ? 25.679  -14.695 12.765  1.00 32.31  ? 231 SER A OG    1 
ATOM   1863 N  N     . ALA A 1 260 ? 24.230  -17.568 11.368  1.00 27.29  ? 232 ALA A N     1 
ATOM   1864 C  CA    . ALA A 1 260 ? 23.195  -18.439 11.890  1.00 30.37  ? 232 ALA A CA    1 
ATOM   1865 C  C     . ALA A 1 260 ? 23.592  -19.909 11.768  1.00 29.93  ? 232 ALA A C     1 
ATOM   1866 O  O     . ALA A 1 260 ? 24.424  -20.274 10.930  1.00 31.68  ? 232 ALA A O     1 
ATOM   1867 C  CB    . ALA A 1 260 ? 21.878  -18.191 11.146  1.00 30.12  ? 232 ALA A CB    1 
ATOM   1868 N  N     . PRO A 1 261 ? 23.000  -20.774 12.593  1.00 32.67  ? 233 PRO A N     1 
ATOM   1869 C  CA    . PRO A 1 261 ? 23.268  -22.212 12.476  1.00 31.73  ? 233 PRO A CA    1 
ATOM   1870 C  C     . PRO A 1 261 ? 22.908  -22.737 11.098  1.00 35.40  ? 233 PRO A C     1 
ATOM   1871 O  O     . PRO A 1 261 ? 22.092  -22.155 10.379  1.00 34.62  ? 233 PRO A O     1 
ATOM   1872 C  CB    . PRO A 1 261 ? 22.376  -22.830 13.564  1.00 32.55  ? 233 PRO A CB    1 
ATOM   1873 C  CG    . PRO A 1 261 ? 22.180  -21.738 14.562  1.00 36.21  ? 233 PRO A CG    1 
ATOM   1874 C  CD    . PRO A 1 261 ? 22.174  -20.456 13.776  1.00 34.45  ? 233 PRO A CD    1 
ATOM   1875 N  N     . GLU A 1 262 ? 23.547  -23.851 10.717  1.00 32.41  ? 234 GLU A N     1 
ATOM   1876 C  CA    . GLU A 1 262 ? 23.188  -24.503 9.466   1.00 30.80  ? 234 GLU A CA    1 
ATOM   1877 C  C     . GLU A 1 262 ? 21.685  -24.764 9.438   1.00 28.02  ? 234 GLU A C     1 
ATOM   1878 O  O     . GLU A 1 262 ? 21.109  -25.208 10.430  1.00 33.05  ? 234 GLU A O     1 
ATOM   1879 C  CB    . GLU A 1 262 ? 23.956  -25.823 9.296   1.00 31.73  ? 234 GLU A CB    1 
ATOM   1880 C  CG    . GLU A 1 262 ? 25.442  -25.637 9.104   1.00 50.66  ? 234 GLU A CG    1 
ATOM   1881 C  CD    . GLU A 1 262 ? 26.195  -26.913 8.713   1.00 51.30  ? 234 GLU A CD    1 
ATOM   1882 O  OE1   . GLU A 1 262 ? 25.549  -27.936 8.385   1.00 57.00  ? 234 GLU A OE1   1 
ATOM   1883 O  OE2   . GLU A 1 262 ? 27.448  -26.877 8.755   1.00 59.75  ? 234 GLU A OE2   1 
ATOM   1884 N  N     . GLY A 1 263 ? 21.045  -24.465 8.307   1.00 31.64  ? 235 GLY A N     1 
ATOM   1885 C  CA    . GLY A 1 263 ? 19.623  -24.739 8.163   1.00 30.41  ? 235 GLY A CA    1 
ATOM   1886 C  C     . GLY A 1 263 ? 18.686  -23.802 8.903   1.00 32.04  ? 235 GLY A C     1 
ATOM   1887 O  O     . GLY A 1 263 ? 17.477  -24.048 8.920   1.00 34.25  ? 235 GLY A O     1 
ATOM   1888 N  N     . SER A 1 264 ? 19.206  -22.737 9.525   1.00 33.90  ? 236 SER A N     1 
ATOM   1889 C  CA    . SER A 1 264 ? 18.385  -21.795 10.272  1.00 30.34  ? 236 SER A CA    1 
ATOM   1890 C  C     . SER A 1 264 ? 17.580  -20.911 9.320   1.00 35.26  ? 236 SER A C     1 
ATOM   1891 O  O     . SER A 1 264 ? 18.086  -20.495 8.276   1.00 26.43  ? 236 SER A O     1 
ATOM   1892 C  CB    . SER A 1 264 ? 19.242  -20.912 11.163  1.00 31.12  ? 236 SER A CB    1 
ATOM   1893 O  OG    . SER A 1 264 ? 18.534  -19.729 11.492  1.00 29.59  ? 236 SER A OG    1 
ATOM   1894 N  N     . PRO A 1 265 ? 16.325  -20.599 9.661   1.00 32.66  ? 237 PRO A N     1 
ATOM   1895 C  CA    . PRO A 1 265 ? 15.549  -19.684 8.811   1.00 29.49  ? 237 PRO A CA    1 
ATOM   1896 C  C     . PRO A 1 265 ? 16.141  -18.298 8.763   1.00 25.49  ? 237 PRO A C     1 
ATOM   1897 O  O     . PRO A 1 265 ? 15.922  -17.588 7.775   1.00 28.85  ? 237 PRO A O     1 
ATOM   1898 C  CB    . PRO A 1 265 ? 14.154  -19.667 9.465   1.00 28.01  ? 237 PRO A CB    1 
ATOM   1899 C  CG    . PRO A 1 265 ? 14.094  -20.906 10.300  1.00 33.97  ? 237 PRO A CG    1 
ATOM   1900 C  CD    . PRO A 1 265 ? 15.530  -21.138 10.776  1.00 30.01  ? 237 PRO A CD    1 
ATOM   1901 N  N     . LEU A 1 266 ? 16.906  -17.895 9.784   1.00 23.65  ? 238 LEU A N     1 
ATOM   1902 C  CA    . LEU A 1 266 ? 17.503  -16.563 9.759   1.00 26.46  ? 238 LEU A CA    1 
ATOM   1903 C  C     . LEU A 1 266 ? 18.440  -16.370 8.577   1.00 27.07  ? 238 LEU A C     1 
ATOM   1904 O  O     . LEU A 1 266 ? 18.690  -15.222 8.188   1.00 26.85  ? 238 LEU A O     1 
ATOM   1905 C  CB    . LEU A 1 266 ? 18.226  -16.282 11.073  1.00 22.88  ? 238 LEU A CB    1 
ATOM   1906 C  CG    . LEU A 1 266 ? 17.350  -16.396 12.326  1.00 29.39  ? 238 LEU A CG    1 
ATOM   1907 C  CD1   . LEU A 1 266 ? 18.169  -16.167 13.597  1.00 28.61  ? 238 LEU A CD1   1 
ATOM   1908 C  CD2   . LEU A 1 266 ? 16.250  -15.357 12.264  1.00 27.98  ? 238 LEU A CD2   1 
ATOM   1909 N  N     . ARG A 1 267 ? 18.926  -17.451 7.960   1.00 23.75  ? 239 ARG A N     1 
ATOM   1910 C  CA    . ARG A 1 267 ? 19.825  -17.283 6.819   1.00 29.75  ? 239 ARG A CA    1 
ATOM   1911 C  C     . ARG A 1 267 ? 19.142  -16.593 5.634   1.00 28.35  ? 239 ARG A C     1 
ATOM   1912 O  O     . ARG A 1 267 ? 19.835  -16.028 4.773   1.00 27.26  ? 239 ARG A O     1 
ATOM   1913 C  CB    . ARG A 1 267 ? 20.427  -18.650 6.422   1.00 27.25  ? 239 ARG A CB    1 
ATOM   1914 C  CG    . ARG A 1 267 ? 21.307  -18.647 5.161   1.00 28.87  ? 239 ARG A CG    1 
ATOM   1915 C  CD    . ARG A 1 267 ? 22.464  -19.664 5.226   1.00 27.61  ? 239 ARG A CD    1 
ATOM   1916 N  NE    . ARG A 1 267 ? 23.430  -19.278 6.245   1.00 24.53  ? 239 ARG A NE    1 
ATOM   1917 C  CZ    . ARG A 1 267 ? 23.522  -19.846 7.442   1.00 26.96  ? 239 ARG A CZ    1 
ATOM   1918 N  NH1   . ARG A 1 267 ? 22.851  -20.952 7.741   1.00 22.64  ? 239 ARG A NH1   1 
ATOM   1919 N  NH2   . ARG A 1 267 ? 24.294  -19.286 8.369   1.00 25.91  ? 239 ARG A NH2   1 
ATOM   1920 N  N     . VAL A 1 268 ? 17.806  -16.588 5.570   1.00 26.59  ? 240 VAL A N     1 
ATOM   1921 C  CA    . VAL A 1 268 ? 17.133  -15.941 4.447   1.00 25.54  ? 240 VAL A CA    1 
ATOM   1922 C  C     . VAL A 1 268 ? 16.240  -14.810 4.934   1.00 34.77  ? 240 VAL A C     1 
ATOM   1923 O  O     . VAL A 1 268 ? 15.247  -14.449 4.274   1.00 27.02  ? 240 VAL A O     1 
ATOM   1924 C  CB    . VAL A 1 268 ? 16.344  -16.955 3.582   1.00 27.82  ? 240 VAL A CB    1 
ATOM   1925 C  CG1   . VAL A 1 268 ? 17.324  -17.807 2.745   1.00 31.53  ? 240 VAL A CG1   1 
ATOM   1926 C  CG2   . VAL A 1 268 ? 15.471  -17.856 4.446   1.00 29.42  ? 240 VAL A CG2   1 
ATOM   1927 N  N     . LEU A 1 269 ? 16.595  -14.239 6.085   1.00 28.80  ? 241 LEU A N     1 
ATOM   1928 C  CA    . LEU A 1 269 ? 15.928  -13.038 6.572   1.00 25.75  ? 241 LEU A CA    1 
ATOM   1929 C  C     . LEU A 1 269 ? 16.582  -11.812 5.934   1.00 21.99  ? 241 LEU A C     1 
ATOM   1930 O  O     . LEU A 1 269 ? 17.748  -11.502 6.196   1.00 26.31  ? 241 LEU A O     1 
ATOM   1931 C  CB    . LEU A 1 269 ? 15.974  -12.981 8.094   1.00 22.52  ? 241 LEU A CB    1 
ATOM   1932 C  CG    . LEU A 1 269 ? 15.449  -11.727 8.774   1.00 25.52  ? 241 LEU A CG    1 
ATOM   1933 C  CD1   . LEU A 1 269 ? 13.987  -11.465 8.351   1.00 21.64  ? 241 LEU A CD1   1 
ATOM   1934 C  CD2   . LEU A 1 269 ? 15.578  -11.828 10.305  1.00 24.41  ? 241 LEU A CD2   1 
ATOM   1935 N  N     . TYR A 1 270 ? 15.838  -11.137 5.074   1.00 24.93  ? 242 TYR A N     1 
ATOM   1936 C  CA    . TYR A 1 270 ? 16.287  -9.955  4.359   1.00 24.28  ? 242 TYR A CA    1 
ATOM   1937 C  C     . TYR A 1 270 ? 15.315  -8.822  4.620   1.00 26.46  ? 242 TYR A C     1 
ATOM   1938 O  O     . TYR A 1 270 ? 14.112  -9.043  4.748   1.00 24.87  ? 242 TYR A O     1 
ATOM   1939 C  CB    . TYR A 1 270 ? 16.363  -10.187 2.837   1.00 23.24  ? 242 TYR A CB    1 
ATOM   1940 C  CG    . TYR A 1 270 ? 17.419  -11.178 2.393   1.00 28.45  ? 242 TYR A CG    1 
ATOM   1941 C  CD1   . TYR A 1 270 ? 17.161  -12.531 2.354   1.00 28.21  ? 242 TYR A CD1   1 
ATOM   1942 C  CD2   . TYR A 1 270 ? 18.672  -10.741 1.994   1.00 20.30  ? 242 TYR A CD2   1 
ATOM   1943 C  CE1   . TYR A 1 270 ? 18.140  -13.437 1.926   1.00 24.78  ? 242 TYR A CE1   1 
ATOM   1944 C  CE2   . TYR A 1 270 ? 19.653  -11.627 1.587   1.00 27.06  ? 242 TYR A CE2   1 
ATOM   1945 C  CZ    . TYR A 1 270 ? 19.377  -12.971 1.547   1.00 25.22  ? 242 TYR A CZ    1 
ATOM   1946 O  OH    . TYR A 1 270 ? 20.359  -13.855 1.150   1.00 32.32  ? 242 TYR A OH    1 
ATOM   1947 N  N     . SER A 1 271 ? 15.813  -7.596  4.625   1.00 25.27  ? 243 SER A N     1 
ATOM   1948 C  CA    . SER A 1 271 ? 14.907  -6.471  4.798   1.00 29.97  ? 243 SER A CA    1 
ATOM   1949 C  C     . SER A 1 271 ? 14.968  -5.506  3.622   1.00 29.15  ? 243 SER A C     1 
ATOM   1950 O  O     . SER A 1 271 ? 16.010  -5.363  2.978   1.00 29.86  ? 243 SER A O     1 
ATOM   1951 C  CB    . SER A 1 271 ? 15.224  -5.728  6.082   1.00 27.01  ? 243 SER A CB    1 
ATOM   1952 O  OG    . SER A 1 271 ? 14.281  -4.715  6.299   1.00 30.46  ? 243 SER A OG    1 
ATOM   1953 N  N     . GLY A 1 272 ? 13.833  -4.848  3.339   1.00 20.85  ? 244 GLY A N     1 
ATOM   1954 C  CA    . GLY A 1 272 ? 13.819  -3.626  2.555   1.00 22.95  ? 244 GLY A CA    1 
ATOM   1955 C  C     . GLY A 1 272 ? 13.591  -2.461  3.502   1.00 27.50  ? 244 GLY A C     1 
ATOM   1956 O  O     . GLY A 1 272 ? 12.907  -2.607  4.499   1.00 26.22  ? 244 GLY A O     1 
ATOM   1957 N  N     . ILE A 1 273 ? 14.170  -1.293  3.201   1.00 20.17  ? 245 ILE A N     1 
ATOM   1958 C  CA    . ILE A 1 273 ? 13.994  -0.129  4.068   1.00 23.58  ? 245 ILE A CA    1 
ATOM   1959 C  C     . ILE A 1 273 ? 13.692  1.100   3.222   1.00 23.18  ? 245 ILE A C     1 
ATOM   1960 O  O     . ILE A 1 273 ? 14.394  1.365   2.242   1.00 25.56  ? 245 ILE A O     1 
ATOM   1961 C  CB    . ILE A 1 273 ? 15.241  0.132   4.928   1.00 25.04  ? 245 ILE A CB    1 
ATOM   1962 C  CG1   . ILE A 1 273 ? 15.609  -1.087  5.765   1.00 23.29  ? 245 ILE A CG1   1 
ATOM   1963 C  CG2   . ILE A 1 273 ? 15.052  1.397   5.788   1.00 22.19  ? 245 ILE A CG2   1 
ATOM   1964 C  CD1   . ILE A 1 273 ? 16.777  -0.817  6.734   1.00 26.00  ? 245 ILE A CD1   1 
ATOM   1965 N  N     . GLY A 1 274 ? 12.687  1.868   3.616   1.00 21.19  ? 246 GLY A N     1 
ATOM   1966 C  CA    . GLY A 1 274 ? 12.355  3.108   2.922   1.00 19.24  ? 246 GLY A CA    1 
ATOM   1967 C  C     . GLY A 1 274 ? 12.310  4.260   3.898   1.00 20.48  ? 246 GLY A C     1 
ATOM   1968 O  O     . GLY A 1 274 ? 11.817  4.116   5.008   1.00 22.45  ? 246 GLY A O     1 
ATOM   1969 N  N     . LEU A 1 275 ? 12.836  5.412   3.476   1.00 19.45  ? 247 LEU A N     1 
ATOM   1970 C  CA    . LEU A 1 275 ? 12.766  6.618   4.304   1.00 22.01  ? 247 LEU A CA    1 
ATOM   1971 C  C     . LEU A 1 275 ? 12.083  7.729   3.524   1.00 23.66  ? 247 LEU A C     1 
ATOM   1972 O  O     . LEU A 1 275 ? 12.320  7.892   2.323   1.00 21.04  ? 247 LEU A O     1 
ATOM   1973 C  CB    . LEU A 1 275 ? 14.151  7.132   4.757   1.00 23.10  ? 247 LEU A CB    1 
ATOM   1974 C  CG    . LEU A 1 275 ? 15.146  6.126   5.317   1.00 25.64  ? 247 LEU A CG    1 
ATOM   1975 C  CD1   . LEU A 1 275 ? 16.526  6.799   5.522   1.00 21.18  ? 247 LEU A CD1   1 
ATOM   1976 C  CD2   . LEU A 1 275 ? 14.624  5.522   6.592   1.00 25.22  ? 247 LEU A CD2   1 
ATOM   1977 N  N     . ALA A 1 276 ? 11.216  8.480   4.207   1.00 23.10  ? 248 ALA A N     1 
ATOM   1978 C  CA    . ALA A 1 276 ? 10.603  9.660   3.621   1.00 24.75  ? 248 ALA A CA    1 
ATOM   1979 C  C     . ALA A 1 276 ? 10.459  10.702  4.716   1.00 29.72  ? 248 ALA A C     1 
ATOM   1980 O  O     . ALA A 1 276 ? 10.725  10.426  5.886   1.00 30.37  ? 248 ALA A O     1 
ATOM   1981 C  CB    . ALA A 1 276 ? 9.240   9.327   2.979   1.00 26.88  ? 248 ALA A CB    1 
ATOM   1982 N  N     . LYS A 1 277 ? 10.071  11.918  4.337   1.00 27.56  ? 249 LYS A N     1 
ATOM   1983 C  CA    . LYS A 1 277 ? 9.627   12.898  5.321   1.00 34.22  ? 249 LYS A CA    1 
ATOM   1984 C  C     . LYS A 1 277 ? 8.111   12.930  5.351   1.00 39.14  ? 249 LYS A C     1 
ATOM   1985 O  O     . LYS A 1 277 ? 7.450   12.809  4.311   1.00 34.03  ? 249 LYS A O     1 
ATOM   1986 C  CB    . LYS A 1 277 ? 10.162  14.301  5.040   1.00 34.85  ? 249 LYS A CB    1 
ATOM   1987 C  CG    . LYS A 1 277 ? 11.645  14.410  5.186   1.00 38.75  ? 249 LYS A CG    1 
ATOM   1988 C  CD    . LYS A 1 277 ? 12.171  15.838  5.133   1.00 37.93  ? 249 LYS A CD    1 
ATOM   1989 C  CE    . LYS A 1 277 ? 12.216  16.488  6.499   1.00 44.60  ? 249 LYS A CE    1 
ATOM   1990 N  NZ    . LYS A 1 277 ? 13.183  17.626  6.479   1.00 43.43  ? 249 LYS A NZ    1 
ATOM   1991 N  N     . GLY A 1 278 ? 7.561   13.084  6.544   1.00 34.66  ? 250 GLY A N     1 
ATOM   1992 C  CA    . GLY A 1 278 ? 6.120   13.124  6.702   1.00 36.05  ? 250 GLY A CA    1 
ATOM   1993 C  C     . GLY A 1 278 ? 5.727   14.187  7.702   1.00 38.08  ? 250 GLY A C     1 
ATOM   1994 O  O     . GLY A 1 278 ? 6.464   14.492  8.641   1.00 36.09  ? 250 GLY A O     1 
ATOM   1995 N  N     . LYS A 1 279 ? 4.560   14.774  7.477   1.00 44.34  ? 251 LYS A N     1 
ATOM   1996 C  CA    . LYS A 1 279 ? 3.998   15.709  8.438   1.00 36.98  ? 251 LYS A CA    1 
ATOM   1997 C  C     . LYS A 1 279 ? 3.171   14.873  9.397   1.00 33.05  ? 251 LYS A C     1 
ATOM   1998 O  O     . LYS A 1 279 ? 2.110   14.359  9.028   1.00 42.22  ? 251 LYS A O     1 
ATOM   1999 C  CB    . LYS A 1 279 ? 3.150   16.774  7.754   1.00 40.18  ? 251 LYS A CB    1 
ATOM   2000 C  CG    . LYS A 1 279 ? 2.339   17.614  8.753   1.00 52.17  ? 251 LYS A CG    1 
ATOM   2001 C  CD    . LYS A 1 279 ? 1.172   18.352  8.081   1.00 52.16  ? 251 LYS A CD    1 
ATOM   2002 C  CE    . LYS A 1 279 ? -0.171  17.900  8.651   1.00 44.41  ? 251 LYS A CE    1 
ATOM   2003 N  NZ    . LYS A 1 279 ? -0.513  16.460  8.321   1.00 49.64  ? 251 LYS A NZ    1 
ATOM   2004 N  N     . VAL A 1 280 ? 3.663   14.689  10.603  1.00 27.12  ? 252 VAL A N     1 
ATOM   2005 C  CA    . VAL A 1 280 ? 2.910   13.939  11.573  1.00 37.23  ? 252 VAL A CA    1 
ATOM   2006 C  C     . VAL A 1 280 ? 2.213   14.943  12.475  1.00 34.47  ? 252 VAL A C     1 
ATOM   2007 O  O     . VAL A 1 280 ? 2.572   16.122  12.539  1.00 31.71  ? 252 VAL A O     1 
ATOM   2008 C  CB    . VAL A 1 280 ? 3.777   12.937  12.368  1.00 37.36  ? 252 VAL A CB    1 
ATOM   2009 C  CG1   . VAL A 1 280 ? 5.041   12.632  11.601  1.00 38.93  ? 252 VAL A CG1   1 
ATOM   2010 C  CG2   . VAL A 1 280 ? 4.033   13.408  13.770  1.00 33.42  ? 252 VAL A CG2   1 
ATOM   2011 N  N     . ILE A 1 281 ? 1.158   14.483  13.126  1.00 33.43  ? 253 ILE A N     1 
ATOM   2012 C  CA    . ILE A 1 281 ? 0.423   15.292  14.083  1.00 32.92  ? 253 ILE A CA    1 
ATOM   2013 C  C     . ILE A 1 281 ? 0.587   14.628  15.436  1.00 34.86  ? 253 ILE A C     1 
ATOM   2014 O  O     . ILE A 1 281 ? 0.303   13.433  15.580  1.00 36.50  ? 253 ILE A O     1 
ATOM   2015 C  CB    . ILE A 1 281 ? -1.060  15.433  13.693  1.00 34.30  ? 253 ILE A CB    1 
ATOM   2016 C  CG1   . ILE A 1 281 ? -1.188  16.188  12.377  1.00 35.14  ? 253 ILE A CG1   1 
ATOM   2017 C  CG2   . ILE A 1 281 ? -1.827  16.168  14.777  1.00 35.62  ? 253 ILE A CG2   1 
ATOM   2018 C  CD1   . ILE A 1 281 ? -2.607  16.237  11.844  1.00 34.52  ? 253 ILE A CD1   1 
ATOM   2019 N  N     . GLU A 1 282 ? 1.103   15.382  16.406  1.00 39.31  ? 254 GLU A N     1 
ATOM   2020 C  CA    . GLU A 1 282 ? 1.137   14.961  17.798  1.00 36.81  ? 254 GLU A CA    1 
ATOM   2021 C  C     . GLU A 1 282 ? -0.112  15.489  18.523  1.00 42.11  ? 254 GLU A C     1 
ATOM   2022 O  O     . GLU A 1 282 ? -0.635  16.557  18.194  1.00 36.19  ? 254 GLU A O     1 
ATOM   2023 C  CB    . GLU A 1 282 ? 2.433   15.453  18.459  1.00 44.61  ? 254 GLU A CB    1 
ATOM   2024 C  CG    . GLU A 1 282 ? 3.711   14.901  17.772  1.00 43.87  ? 254 GLU A CG    1 
ATOM   2025 C  CD    . GLU A 1 282 ? 5.049   15.336  18.400  1.00 54.79  ? 254 GLU A CD    1 
ATOM   2026 O  OE1   . GLU A 1 282 ? 5.122   16.444  18.992  1.00 54.12  ? 254 GLU A OE1   1 
ATOM   2027 O  OE2   . GLU A 1 282 ? 6.032   14.549  18.300  1.00 48.00  ? 254 GLU A OE2   1 
ATOM   2028 N  N     . GLY A 1 283 ? -0.628  14.701  19.460  1.00 42.50  ? 255 GLY A N     1 
ATOM   2029 C  CA    . GLY A 1 283 ? -1.829  15.081  20.180  1.00 40.58  ? 255 GLY A CA    1 
ATOM   2030 C  C     . GLY A 1 283 ? -2.411  13.907  20.946  1.00 41.41  ? 255 GLY A C     1 
ATOM   2031 O  O     . GLY A 1 283 ? -1.805  12.838  21.035  1.00 43.29  ? 255 GLY A O     1 
ATOM   2032 N  N     . ASN A 1 284 ? -3.600  14.144  21.514  1.00 34.66  ? 256 ASN A N     1 
ATOM   2033 C  CA    . ASN A 1 284 ? -4.402  13.098  22.165  1.00 38.35  ? 256 ASN A CA    1 
ATOM   2034 C  C     . ASN A 1 284 ? -5.382  12.572  21.119  1.00 39.11  ? 256 ASN A C     1 
ATOM   2035 O  O     . ASN A 1 284 ? -6.470  13.117  20.922  1.00 35.48  ? 256 ASN A O     1 
ATOM   2036 C  CB    . ASN A 1 284 ? -5.119  13.632  23.406  1.00 45.38  ? 256 ASN A CB    1 
ATOM   2037 C  CG    . ASN A 1 284 ? -5.874  12.536  24.181  1.00 50.36  ? 256 ASN A CG    1 
ATOM   2038 O  OD1   . ASN A 1 284 ? -5.627  11.341  24.014  1.00 46.78  ? 256 ASN A OD1   1 
ATOM   2039 N  ND2   . ASN A 1 284 ? -6.791  12.954  25.041  1.00 58.28  ? 256 ASN A ND2   1 
ATOM   2040 N  N     . ILE A 1 285 ? -4.981  11.495  20.448  1.00 40.18  ? 257 ILE A N     1 
ATOM   2041 C  CA    . ILE A 1 285 ? -5.638  11.005  19.244  1.00 40.19  ? 257 ILE A CA    1 
ATOM   2042 C  C     . ILE A 1 285 ? -6.209  9.624   19.513  1.00 40.60  ? 257 ILE A C     1 
ATOM   2043 O  O     . ILE A 1 285 ? -5.552  8.785   20.134  1.00 35.44  ? 257 ILE A O     1 
ATOM   2044 C  CB    . ILE A 1 285 ? -4.655  10.962  18.053  1.00 41.28  ? 257 ILE A CB    1 
ATOM   2045 C  CG1   . ILE A 1 285 ? -4.129  12.369  17.729  1.00 36.90  ? 257 ILE A CG1   1 
ATOM   2046 C  CG2   . ILE A 1 285 ? -5.301  10.291  16.852  1.00 37.50  ? 257 ILE A CG2   1 
ATOM   2047 C  CD1   . ILE A 1 285 ? -2.642  12.406  17.388  1.00 33.35  ? 257 ILE A CD1   1 
ATOM   2048 N  N     . GLY A 1 286 ? -7.424  9.379   19.036  1.00 32.88  ? 258 GLY A N     1 
ATOM   2049 C  CA    . GLY A 1 286 ? -7.952  8.039   19.154  1.00 34.72  ? 258 GLY A CA    1 
ATOM   2050 C  C     . GLY A 1 286 ? -9.413  7.997   19.513  1.00 36.56  ? 258 GLY A C     1 
ATOM   2051 O  O     . GLY A 1 286 ? -10.148 8.956   19.255  1.00 44.72  ? 258 GLY A O     1 
ATOM   2052 N  N     . SER A 1 287 ? -9.843  6.906   20.141  1.00 44.98  ? 259 SER A N     1 
ATOM   2053 C  CA    . SER A 1 287 ? -11.259 6.582   20.249  1.00 44.85  ? 259 SER A CA    1 
ATOM   2054 C  C     . SER A 1 287 ? -11.804 6.689   21.668  1.00 53.86  ? 259 SER A C     1 
ATOM   2055 O  O     . SER A 1 287 ? -12.914 6.207   21.920  1.00 62.65  ? 259 SER A O     1 
ATOM   2056 C  CB    . SER A 1 287 ? -11.492 5.168   19.724  1.00 42.92  ? 259 SER A CB    1 
ATOM   2057 O  OG    . SER A 1 287 ? -10.756 4.231   20.497  1.00 45.04  ? 259 SER A OG    1 
ATOM   2058 N  N     . GLU A 1 288 ? -11.051 7.276   22.603  1.00 49.29  ? 260 GLU A N     1 
ATOM   2059 C  CA    . GLU A 1 288 ? -11.406 7.271   24.026  1.00 66.01  ? 260 GLU A CA    1 
ATOM   2060 C  C     . GLU A 1 288 ? -11.307 5.861   24.610  1.00 62.75  ? 260 GLU A C     1 
ATOM   2061 O  O     . GLU A 1 288 ? -10.825 5.690   25.736  1.00 66.36  ? 260 GLU A O     1 
ATOM   2062 C  CB    . GLU A 1 288 ? -12.803 7.865   24.269  1.00 69.71  ? 260 GLU A CB    1 
ATOM   2063 N  N     . LEU A 1 289 ? -11.753 4.846   23.866  1.00 55.87  ? 261 LEU A N     1 
ATOM   2064 C  CA    . LEU A 1 289 ? -11.326 3.476   24.131  1.00 60.51  ? 261 LEU A CA    1 
ATOM   2065 C  C     . LEU A 1 289 ? -9.803  3.406   23.998  1.00 62.67  ? 261 LEU A C     1 
ATOM   2066 O  O     . LEU A 1 289 ? -9.094  3.246   24.997  1.00 60.19  ? 261 LEU A O     1 
ATOM   2067 C  CB    . LEU A 1 289 ? -12.017 2.491   23.168  1.00 63.40  ? 261 LEU A CB    1 
ATOM   2068 C  CG    . LEU A 1 289 ? -11.763 0.967   23.250  1.00 68.44  ? 261 LEU A CG    1 
ATOM   2069 C  CD1   . LEU A 1 289 ? -13.054 0.144   23.054  1.00 57.19  ? 261 LEU A CD1   1 
ATOM   2070 C  CD2   . LEU A 1 289 ? -10.690 0.498   22.263  1.00 68.28  ? 261 LEU A CD2   1 
ATOM   2071 N  N     . LYS A 1 290 ? -9.290  3.572   22.779  1.00 57.76  ? 262 LYS A N     1 
ATOM   2072 C  CA    . LYS A 1 290 ? -7.866  3.463   22.481  1.00 47.99  ? 262 LYS A CA    1 
ATOM   2073 C  C     . LYS A 1 290 ? -7.288  4.799   22.037  1.00 50.43  ? 262 LYS A C     1 
ATOM   2074 O  O     . LYS A 1 290 ? -7.887  5.494   21.208  1.00 44.66  ? 262 LYS A O     1 
ATOM   2075 C  CB    . LYS A 1 290 ? -7.615  2.408   21.411  1.00 54.81  ? 262 LYS A CB    1 
ATOM   2076 C  CG    . LYS A 1 290 ? -6.161  2.325   20.984  1.00 54.77  ? 262 LYS A CG    1 
ATOM   2077 C  CD    . LYS A 1 290 ? -5.405  1.282   21.753  1.00 61.96  ? 262 LYS A CD    1 
ATOM   2078 C  CE    . LYS A 1 290 ? -4.078  1.846   22.208  1.00 54.77  ? 262 LYS A CE    1 
ATOM   2079 N  NZ    . LYS A 1 290 ? -3.498  2.748   21.173  1.00 48.96  ? 262 LYS A NZ    1 
ATOM   2080 N  N     . ARG A 1 291 ? -6.119  5.143   22.584  1.00 46.31  ? 263 ARG A N     1 
ATOM   2081 C  CA    . ARG A 1 291 ? -5.479  6.428   22.359  1.00 41.04  ? 263 ARG A CA    1 
ATOM   2082 C  C     . ARG A 1 291 ? -4.080  6.209   21.812  1.00 49.04  ? 263 ARG A C     1 
ATOM   2083 O  O     . ARG A 1 291 ? -3.507  5.120   21.923  1.00 45.68  ? 263 ARG A O     1 
ATOM   2084 C  CB    . ARG A 1 291 ? -5.395  7.265   23.654  1.00 44.59  ? 263 ARG A CB    1 
ATOM   2085 C  CG    . ARG A 1 291 ? -6.739  7.840   24.123  1.00 43.95  ? 263 ARG A CG    1 
ATOM   2086 C  CD    . ARG A 1 291 ? -7.240  8.891   23.145  1.00 50.08  ? 263 ARG A CD    1 
ATOM   2087 N  NE    . ARG A 1 291 ? -8.463  9.557   23.577  1.00 60.02  ? 263 ARG A NE    1 
ATOM   2088 C  CZ    . ARG A 1 291 ? -8.985  10.620  22.974  1.00 61.66  ? 263 ARG A CZ    1 
ATOM   2089 N  NH1   . ARG A 1 291 ? -8.401  11.175  21.920  1.00 55.94  ? 263 ARG A NH1   1 
ATOM   2090 N  NH2   . ARG A 1 291 ? -10.130 11.129  23.427  1.00 60.50  ? 263 ARG A NH2   1 
ATOM   2091 N  N     . ASP A 1 292 ? -3.543  7.270   21.211  1.00 38.50  ? 264 ASP A N     1 
ATOM   2092 C  CA    . ASP A 1 292 ? -2.141  7.338   20.830  1.00 43.25  ? 264 ASP A CA    1 
ATOM   2093 C  C     . ASP A 1 292 ? -1.741  8.802   20.810  1.00 40.55  ? 264 ASP A C     1 
ATOM   2094 O  O     . ASP A 1 292 ? -2.577  9.708   20.906  1.00 40.29  ? 264 ASP A O     1 
ATOM   2095 C  CB    . ASP A 1 292 ? -1.862  6.673   19.475  1.00 49.57  ? 264 ASP A CB    1 
ATOM   2096 C  CG    . ASP A 1 292 ? -0.389  6.264   19.307  1.00 52.88  ? 264 ASP A CG    1 
ATOM   2097 O  OD1   . ASP A 1 292 ? 0.522   6.988   19.782  1.00 54.83  ? 264 ASP A OD1   1 
ATOM   2098 O  OD2   . ASP A 1 292 ? -0.144  5.195   18.709  1.00 64.65  ? 264 ASP A OD2   1 
ATOM   2099 N  N     . TYR A 1 293 ? -0.440  9.018   20.701  1.00 45.29  ? 265 TYR A N     1 
ATOM   2100 C  CA    . TYR A 1 293 ? 0.160   10.335  20.814  1.00 45.99  ? 265 TYR A CA    1 
ATOM   2101 C  C     . TYR A 1 293 ? 0.484   10.923  19.432  1.00 36.83  ? 265 TYR A C     1 
ATOM   2102 O  O     . TYR A 1 293 ? 0.744   12.127  19.308  1.00 38.99  ? 265 TYR A O     1 
ATOM   2103 C  CB    . TYR A 1 293 ? 1.401   10.189  21.733  1.00 47.20  ? 265 TYR A CB    1 
ATOM   2104 C  CG    . TYR A 1 293 ? 2.581   11.103  21.536  1.00 47.89  ? 265 TYR A CG    1 
ATOM   2105 C  CD1   . TYR A 1 293 ? 2.430   12.487  21.572  1.00 59.18  ? 265 TYR A CD1   1 
ATOM   2106 C  CD2   . TYR A 1 293 ? 3.853   10.585  21.286  1.00 54.74  ? 265 TYR A CD2   1 
ATOM   2107 C  CE1   . TYR A 1 293 ? 3.526   13.336  21.399  1.00 57.27  ? 265 TYR A CE1   1 
ATOM   2108 C  CE2   . TYR A 1 293 ? 4.950   11.420  21.102  1.00 52.79  ? 265 TYR A CE2   1 
ATOM   2109 C  CZ    . TYR A 1 293 ? 4.777   12.798  21.162  1.00 59.10  ? 265 TYR A CZ    1 
ATOM   2110 O  OH    . TYR A 1 293 ? 5.847   13.651  20.977  1.00 71.92  ? 265 TYR A OH    1 
ATOM   2111 N  N     . THR A 1 294 ? 0.395   10.121  18.375  1.00 38.83  ? 266 THR A N     1 
ATOM   2112 C  CA    . THR A 1 294 ? 0.818   10.580  17.059  1.00 32.31  ? 266 THR A CA    1 
ATOM   2113 C  C     . THR A 1 294 ? -0.072  9.981   15.968  1.00 32.42  ? 266 THR A C     1 
ATOM   2114 O  O     . THR A 1 294 ? -0.676  8.921   16.142  1.00 31.70  ? 266 THR A O     1 
ATOM   2115 C  CB    . THR A 1 294 ? 2.293   10.222  16.861  1.00 30.28  ? 266 THR A CB    1 
ATOM   2116 O  OG1   . THR A 1 294 ? 2.790   10.860  15.683  1.00 52.05  ? 266 THR A OG1   1 
ATOM   2117 C  CG2   . THR A 1 294 ? 2.453   8.728   16.770  1.00 30.70  ? 266 THR A CG2   1 
ATOM   2118 N  N     . ILE A 1 295 ? -0.145  10.677  14.836  1.00 30.32  ? 267 ILE A N     1 
ATOM   2119 C  CA    . ILE A 1 295 ? -0.794  10.170  13.619  1.00 31.54  ? 267 ILE A CA    1 
ATOM   2120 C  C     . ILE A 1 295 ? -0.027  10.701  12.411  1.00 29.09  ? 267 ILE A C     1 
ATOM   2121 O  O     . ILE A 1 295 ? 0.296   11.891  12.341  1.00 34.16  ? 267 ILE A O     1 
ATOM   2122 C  CB    . ILE A 1 295 ? -2.296  10.549  13.523  1.00 28.44  ? 267 ILE A CB    1 
ATOM   2123 C  CG1   . ILE A 1 295 ? -2.939  9.937   12.272  1.00 32.41  ? 267 ILE A CG1   1 
ATOM   2124 C  CG2   . ILE A 1 295 ? -2.515  12.054  13.459  1.00 24.74  ? 267 ILE A CG2   1 
ATOM   2125 C  CD1   . ILE A 1 295 ? -4.469  9.916   12.339  1.00 34.51  ? 267 ILE A CD1   1 
ATOM   2126 N  N     . LEU A 1 296 ? 0.277   9.807   11.470  1.00 30.36  ? 268 LEU A N     1 
ATOM   2127 C  CA    . LEU A 1 296 ? 0.802   10.157  10.149  1.00 31.27  ? 268 LEU A CA    1 
ATOM   2128 C  C     . LEU A 1 296 ? -0.242  9.758   9.108   1.00 27.11  ? 268 LEU A C     1 
ATOM   2129 O  O     . LEU A 1 296 ? -0.394  8.571   8.798   1.00 26.02  ? 268 LEU A O     1 
ATOM   2130 C  CB    . LEU A 1 296 ? 2.131   9.451   9.881   1.00 28.48  ? 268 LEU A CB    1 
ATOM   2131 C  CG    . LEU A 1 296 ? 2.651   9.566   8.445   1.00 31.21  ? 268 LEU A CG    1 
ATOM   2132 C  CD1   . LEU A 1 296 ? 3.155   10.960  8.187   1.00 33.86  ? 268 LEU A CD1   1 
ATOM   2133 C  CD2   . LEU A 1 296 ? 3.797   8.553   8.185   1.00 29.81  ? 268 LEU A CD2   1 
ATOM   2134 N  N     . GLY A 1 297 ? -0.958  10.742  8.575   1.00 30.75  ? 269 GLY A N     1 
ATOM   2135 C  CA    . GLY A 1 297 ? -1.971  10.440  7.573   1.00 34.52  ? 269 GLY A CA    1 
ATOM   2136 C  C     . GLY A 1 297 ? -1.371  9.714   6.381   1.00 32.82  ? 269 GLY A C     1 
ATOM   2137 O  O     . GLY A 1 297 ? -0.274  10.039  5.920   1.00 36.66  ? 269 GLY A O     1 
ATOM   2138 N  N     . ASP A 1 298 ? -2.077  8.677   5.915   1.00 35.64  ? 270 ASP A N     1 
ATOM   2139 C  CA    . ASP A 1 298 ? -1.671  7.915   4.715   1.00 43.72  ? 270 ASP A CA    1 
ATOM   2140 C  C     . ASP A 1 298 ? -0.317  7.219   4.898   1.00 38.76  ? 270 ASP A C     1 
ATOM   2141 O  O     . ASP A 1 298 ? 0.440   7.024   3.934   1.00 32.59  ? 270 ASP A O     1 
ATOM   2142 C  CB    . ASP A 1 298 ? -1.642  8.804   3.465   1.00 45.99  ? 270 ASP A CB    1 
ATOM   2143 C  CG    . ASP A 1 298 ? -3.009  9.409   3.145   1.00 46.05  ? 270 ASP A CG    1 
ATOM   2144 O  OD1   . ASP A 1 298 ? -4.047  8.811   3.523   1.00 41.43  ? 270 ASP A OD1   1 
ATOM   2145 O  OD2   . ASP A 1 298 ? -3.036  10.495  2.529   1.00 43.67  ? 270 ASP A OD2   1 
ATOM   2146 N  N     . ALA A 1 299 ? -0.007  6.860   6.148   1.00 32.92  ? 271 ALA A N     1 
ATOM   2147 C  CA    . ALA A 1 299 ? 1.131   5.995   6.438   1.00 26.37  ? 271 ALA A CA    1 
ATOM   2148 C  C     . ALA A 1 299 ? 1.044   4.678   5.665   1.00 30.44  ? 271 ALA A C     1 
ATOM   2149 O  O     . ALA A 1 299 ? 2.062   4.168   5.170   1.00 29.32  ? 271 ALA A O     1 
ATOM   2150 C  CB    . ALA A 1 299 ? 1.193   5.724   7.948   1.00 30.19  ? 271 ALA A CB    1 
ATOM   2151 N  N     . VAL A 1 300 ? -0.168  4.115   5.565   1.00 28.27  ? 272 VAL A N     1 
ATOM   2152 C  CA    . VAL A 1 300 ? -0.418  2.895   4.789   1.00 30.01  ? 272 VAL A CA    1 
ATOM   2153 C  C     . VAL A 1 300 ? 0.165   3.014   3.387   1.00 34.87  ? 272 VAL A C     1 
ATOM   2154 O  O     . VAL A 1 300 ? 0.850   2.107   2.893   1.00 27.62  ? 272 VAL A O     1 
ATOM   2155 C  CB    . VAL A 1 300 ? -1.932  2.606   4.723   1.00 39.55  ? 272 VAL A CB    1 
ATOM   2156 C  CG1   . VAL A 1 300 ? -2.268  1.675   3.538   1.00 30.89  ? 272 VAL A CG1   1 
ATOM   2157 C  CG2   . VAL A 1 300 ? -2.403  2.006   6.010   1.00 34.50  ? 272 VAL A CG2   1 
ATOM   2158 N  N     . ASN A 1 301 ? -0.100  4.136   2.730   1.00 27.97  ? 273 ASN A N     1 
ATOM   2159 C  CA    . ASN A 1 301 ? 0.252   4.262   1.321   1.00 35.97  ? 273 ASN A CA    1 
ATOM   2160 C  C     . ASN A 1 301 ? 1.727   4.592   1.131   1.00 27.58  ? 273 ASN A C     1 
ATOM   2161 O  O     . ASN A 1 301 ? 2.343   4.121   0.172   1.00 28.43  ? 273 ASN A O     1 
ATOM   2162 C  CB    . ASN A 1 301 ? -0.644  5.318   0.679   1.00 34.54  ? 273 ASN A CB    1 
ATOM   2163 C  CG    . ASN A 1 301 ? -2.118  5.101   1.030   1.00 48.50  ? 273 ASN A CG    1 
ATOM   2164 O  OD1   . ASN A 1 301 ? -2.813  4.267   0.414   1.00 48.33  ? 273 ASN A OD1   1 
ATOM   2165 N  ND2   . ASN A 1 301 ? -2.582  5.807   2.071   1.00 39.85  ? 273 ASN A ND2   1 
ATOM   2166 N  N     . VAL A 1 302 ? 2.308   5.411   2.015   1.00 27.58  ? 274 VAL A N     1 
ATOM   2167 C  CA    . VAL A 1 302 ? 3.748   5.647   1.959   1.00 22.78  ? 274 VAL A CA    1 
ATOM   2168 C  C     . VAL A 1 302 ? 4.509   4.342   2.195   1.00 30.40  ? 274 VAL A C     1 
ATOM   2169 O  O     . VAL A 1 302 ? 5.474   4.030   1.479   1.00 30.26  ? 274 VAL A O     1 
ATOM   2170 C  CB    . VAL A 1 302 ? 4.157   6.745   2.957   1.00 29.01  ? 274 VAL A CB    1 
ATOM   2171 C  CG1   . VAL A 1 302 ? 5.672   6.853   3.052   1.00 29.05  ? 274 VAL A CG1   1 
ATOM   2172 C  CG2   . VAL A 1 302 ? 3.542   8.088   2.571   1.00 27.26  ? 274 VAL A CG2   1 
ATOM   2173 N  N     . ALA A 1 303 ? 4.077   3.542   3.174   1.00 22.75  ? 275 ALA A N     1 
ATOM   2174 C  CA    . ALA A 1 303 ? 4.741   2.252   3.404   1.00 29.42  ? 275 ALA A CA    1 
ATOM   2175 C  C     . ALA A 1 303 ? 4.620   1.351   2.180   1.00 30.64  ? 275 ALA A C     1 
ATOM   2176 O  O     . ALA A 1 303 ? 5.613   0.784   1.707   1.00 25.21  ? 275 ALA A O     1 
ATOM   2177 C  CB    . ALA A 1 303 ? 4.148   1.543   4.621   1.00 24.69  ? 275 ALA A CB    1 
ATOM   2178 N  N     . ALA A 1 304 ? 3.398   1.222   1.643   1.00 25.00  ? 276 ALA A N     1 
ATOM   2179 C  CA    . ALA A 1 304 ? 3.180   0.359   0.488   1.00 28.82  ? 276 ALA A CA    1 
ATOM   2180 C  C     . ALA A 1 304 ? 4.023   0.798   -0.704  1.00 23.97  ? 276 ALA A C     1 
ATOM   2181 O  O     . ALA A 1 304 ? 4.586   -0.040  -1.411  1.00 27.98  ? 276 ALA A O     1 
ATOM   2182 C  CB    . ALA A 1 304 ? 1.700   0.348   0.125   1.00 26.51  ? 276 ALA A CB    1 
ATOM   2183 N  N     . ARG A 1 305 ? 4.147   2.109   -0.927  1.00 26.14  ? 277 ARG A N     1 
ATOM   2184 C  CA    . ARG A 1 305 ? 4.924   2.592   -2.061  1.00 25.42  ? 277 ARG A CA    1 
ATOM   2185 C  C     . ARG A 1 305 ? 6.425   2.405   -1.857  1.00 32.03  ? 277 ARG A C     1 
ATOM   2186 O  O     . ARG A 1 305 ? 7.153   2.150   -2.822  1.00 25.05  ? 277 ARG A O     1 
ATOM   2187 C  CB    . ARG A 1 305 ? 4.600   4.056   -2.341  1.00 28.85  ? 277 ARG A CB    1 
ATOM   2188 C  CG    . ARG A 1 305 ? 3.356   4.209   -3.194  1.00 43.04  ? 277 ARG A CG    1 
ATOM   2189 C  CD    . ARG A 1 305 ? 2.547   5.426   -2.833  1.00 47.98  ? 277 ARG A CD    1 
ATOM   2190 N  NE    . ARG A 1 305 ? 1.132   5.217   -3.137  1.00 60.12  ? 277 ARG A NE    1 
ATOM   2191 C  CZ    . ARG A 1 305 ? 0.157   6.035   -2.763  1.00 58.65  ? 277 ARG A CZ    1 
ATOM   2192 N  NH1   . ARG A 1 305 ? 0.402   7.113   -2.036  1.00 53.09  ? 277 ARG A NH1   1 
ATOM   2193 N  NH2   . ARG A 1 305 ? -1.099  5.754   -3.113  1.00 67.71  ? 277 ARG A NH2   1 
ATOM   2194 N  N     . LEU A 1 306 ? 6.909   2.572   -0.627  1.00 23.53  ? 278 LEU A N     1 
ATOM   2195 C  CA    . LEU A 1 306 ? 8.310   2.299   -0.344  1.00 26.05  ? 278 LEU A CA    1 
ATOM   2196 C  C     . LEU A 1 306 ? 8.631   0.818   -0.520  1.00 25.99  ? 278 LEU A C     1 
ATOM   2197 O  O     . LEU A 1 306 ? 9.696   0.461   -1.039  1.00 26.23  ? 278 LEU A O     1 
ATOM   2198 C  CB    . LEU A 1 306 ? 8.659   2.776   1.075   1.00 24.73  ? 278 LEU A CB    1 
ATOM   2199 C  CG    . LEU A 1 306 ? 8.677   4.309   1.178   1.00 21.45  ? 278 LEU A CG    1 
ATOM   2200 C  CD1   . LEU A 1 306 ? 8.696   4.732   2.631   1.00 22.77  ? 278 LEU A CD1   1 
ATOM   2201 C  CD2   . LEU A 1 306 ? 9.881   4.879   0.404   1.00 25.56  ? 278 LEU A CD2   1 
ATOM   2202 N  N     . GLU A 1 307 ? 7.736   -0.059  -0.073  1.00 26.75  ? 279 GLU A N     1 
ATOM   2203 C  CA    . GLU A 1 307 ? 7.939   -1.486  -0.282  1.00 31.52  ? 279 GLU A CA    1 
ATOM   2204 C  C     . GLU A 1 307 ? 7.973   -1.828  -1.761  1.00 28.89  ? 279 GLU A C     1 
ATOM   2205 O  O     . GLU A 1 307 ? 8.762   -2.681  -2.180  1.00 30.42  ? 279 GLU A O     1 
ATOM   2206 C  CB    . GLU A 1 307 ? 6.846   -2.285  0.420   1.00 32.54  ? 279 GLU A CB    1 
ATOM   2207 C  CG    . GLU A 1 307 ? 7.014   -2.351  1.911   1.00 36.82  ? 279 GLU A CG    1 
ATOM   2208 C  CD    . GLU A 1 307 ? 6.057   -3.354  2.550   1.00 43.76  ? 279 GLU A CD    1 
ATOM   2209 O  OE1   . GLU A 1 307 ? 5.551   -4.234  1.810   1.00 42.93  ? 279 GLU A OE1   1 
ATOM   2210 O  OE2   . GLU A 1 307 ? 5.837   -3.275  3.794   1.00 35.35  ? 279 GLU A OE2   1 
ATOM   2211 N  N     . ALA A 1 308 ? 7.124   -1.184  -2.572  1.00 27.02  ? 280 ALA A N     1 
ATOM   2212 C  CA    . ALA A 1 308 ? 7.154   -1.465  -4.010  1.00 29.28  ? 280 ALA A CA    1 
ATOM   2213 C  C     . ALA A 1 308 ? 8.495   -1.079  -4.594  1.00 29.58  ? 280 ALA A C     1 
ATOM   2214 O  O     . ALA A 1 308 ? 9.017   -1.764  -5.484  1.00 32.31  ? 280 ALA A O     1 
ATOM   2215 C  CB    . ALA A 1 308 ? 6.028   -0.735  -4.753  1.00 28.90  ? 280 ALA A CB    1 
ATOM   2216 N  N     . LEU A 1 309 ? 9.096   -0.009  -4.078  1.00 28.48  ? 281 LEU A N     1 
ATOM   2217 C  CA    . LEU A 1 309 ? 10.363  0.447   -4.640  1.00 24.69  ? 281 LEU A CA    1 
ATOM   2218 C  C     . LEU A 1 309 ? 11.521  -0.467  -4.255  1.00 29.98  ? 281 LEU A C     1 
ATOM   2219 O  O     . LEU A 1 309 ? 12.403  -0.733  -5.079  1.00 26.96  ? 281 LEU A O     1 
ATOM   2220 C  CB    . LEU A 1 309 ? 10.630  1.877   -4.199  1.00 24.50  ? 281 LEU A CB    1 
ATOM   2221 C  CG    . LEU A 1 309 ? 9.933   2.972   -4.995  1.00 33.22  ? 281 LEU A CG    1 
ATOM   2222 C  CD1   . LEU A 1 309 ? 9.937   4.241   -4.174  1.00 30.92  ? 281 LEU A CD1   1 
ATOM   2223 C  CD2   . LEU A 1 309 ? 10.677  3.218   -6.311  1.00 30.70  ? 281 LEU A CD2   1 
ATOM   2224 N  N     . THR A 1 310 ? 11.571  -0.936  -3.008  1.00 28.40  ? 282 THR A N     1 
ATOM   2225 C  CA    . THR A 1 310 ? 12.687  -1.803  -2.648  1.00 31.75  ? 282 THR A CA    1 
ATOM   2226 C  C     . THR A 1 310 ? 12.624  -3.105  -3.436  1.00 32.25  ? 282 THR A C     1 
ATOM   2227 O  O     . THR A 1 310 ? 13.662  -3.629  -3.862  1.00 42.78  ? 282 THR A O     1 
ATOM   2228 C  CB    . THR A 1 310 ? 12.730  -2.090  -1.140  1.00 28.54  ? 282 THR A CB    1 
ATOM   2229 O  OG1   . THR A 1 310 ? 11.532  -2.760  -0.731  1.00 27.01  ? 282 THR A OG1   1 
ATOM   2230 C  CG2   . THR A 1 310 ? 12.922  -0.816  -0.309  1.00 24.90  ? 282 THR A CG2   1 
ATOM   2231 N  N     . ARG A 1 311 ? 11.414  -3.629  -3.659  1.00 29.35  ? 283 ARG A N     1 
ATOM   2232 C  CA    . ARG A 1 311 ? 11.250  -4.815  -4.506  1.00 30.22  ? 283 ARG A CA    1 
ATOM   2233 C  C     . ARG A 1 311 ? 11.646  -4.518  -5.946  1.00 34.87  ? 283 ARG A C     1 
ATOM   2234 O  O     . ARG A 1 311 ? 12.375  -5.287  -6.578  1.00 39.08  ? 283 ARG A O     1 
ATOM   2235 C  CB    . ARG A 1 311 ? 9.800   -5.298  -4.480  1.00 33.26  ? 283 ARG A CB    1 
ATOM   2236 C  CG    . ARG A 1 311 ? 9.248   -5.555  -3.100  1.00 44.52  ? 283 ARG A CG    1 
ATOM   2237 C  CD    . ARG A 1 311 ? 9.862   -6.792  -2.471  1.00 50.89  ? 283 ARG A CD    1 
ATOM   2238 N  NE    . ARG A 1 311 ? 10.030  -6.676  -1.022  1.00 56.37  ? 283 ARG A NE    1 
ATOM   2239 C  CZ    . ARG A 1 311 ? 9.085   -6.319  -0.154  1.00 45.93  ? 283 ARG A CZ    1 
ATOM   2240 N  NH1   . ARG A 1 311 ? 7.831   -6.105  -0.525  1.00 57.67  ? 283 ARG A NH1   1 
ATOM   2241 N  NH2   . ARG A 1 311 ? 9.402   -6.206  1.130   1.00 48.62  ? 283 ARG A NH2   1 
ATOM   2242 N  N     . GLN A 1 312 ? 11.173  -3.395  -6.477  1.00 35.19  ? 284 GLN A N     1 
ATOM   2243 C  CA    . GLN A 1 312 ? 11.361  -3.097  -7.892  1.00 40.07  ? 284 GLN A CA    1 
ATOM   2244 C  C     . GLN A 1 312 ? 12.809  -2.759  -8.214  1.00 46.35  ? 284 GLN A C     1 
ATOM   2245 O  O     . GLN A 1 312 ? 13.289  -3.089  -9.304  1.00 44.76  ? 284 GLN A O     1 
ATOM   2246 C  CB    . GLN A 1 312 ? 10.425  -1.956  -8.307  1.00 40.11  ? 284 GLN A CB    1 
ATOM   2247 C  CG    . GLN A 1 312 ? 10.445  -1.617  -9.791  1.00 40.84  ? 284 GLN A CG    1 
ATOM   2248 C  CD    . GLN A 1 312 ? 11.224  -0.358  -10.094 1.00 42.71  ? 284 GLN A CD    1 
ATOM   2249 O  OE1   . GLN A 1 312 ? 10.865  0.733   -9.631  1.00 40.75  ? 284 GLN A OE1   1 
ATOM   2250 N  NE2   . GLN A 1 312 ? 12.302  -0.494  -10.877 1.00 45.71  ? 284 GLN A NE2   1 
ATOM   2251 N  N     . LEU A 1 313 ? 13.514  -2.114  -7.291  1.00 38.35  ? 285 LEU A N     1 
ATOM   2252 C  CA    . LEU A 1 313 ? 14.844  -1.594  -7.563  1.00 42.95  ? 285 LEU A CA    1 
ATOM   2253 C  C     . LEU A 1 313 ? 15.954  -2.553  -7.194  1.00 44.90  ? 285 LEU A C     1 
ATOM   2254 O  O     . LEU A 1 313 ? 17.123  -2.256  -7.478  1.00 47.75  ? 285 LEU A O     1 
ATOM   2255 C  CB    . LEU A 1 313 ? 15.060  -0.280  -6.816  1.00 33.74  ? 285 LEU A CB    1 
ATOM   2256 C  CG    . LEU A 1 313 ? 14.272  0.875   -7.428  1.00 39.68  ? 285 LEU A CG    1 
ATOM   2257 C  CD1   . LEU A 1 313 ? 14.302  2.089   -6.496  1.00 30.69  ? 285 LEU A CD1   1 
ATOM   2258 C  CD2   . LEU A 1 313 ? 14.858  1.204   -8.798  1.00 41.33  ? 285 LEU A CD2   1 
ATOM   2259 N  N     . SER A 1 314 ? 15.628  -3.685  -6.578  1.00 46.08  ? 286 SER A N     1 
ATOM   2260 C  CA    . SER A 1 314 ? 16.651  -4.586  -6.061  1.00 55.84  ? 286 SER A CA    1 
ATOM   2261 C  C     . SER A 1 314 ? 17.628  -3.809  -5.187  1.00 50.79  ? 286 SER A C     1 
ATOM   2262 O  O     . SER A 1 314 ? 18.839  -4.022  -5.220  1.00 49.46  ? 286 SER A O     1 
ATOM   2263 C  CB    . SER A 1 314 ? 17.380  -5.305  -7.198  1.00 60.35  ? 286 SER A CB    1 
ATOM   2264 O  OG    . SER A 1 314 ? 16.467  -5.719  -8.206  1.00 58.58  ? 286 SER A OG    1 
ATOM   2265 N  N     . GLN A 1 315 ? 17.091  -2.863  -4.423  1.00 48.49  ? 287 GLN A N     1 
ATOM   2266 C  CA    . GLN A 1 315 ? 17.905  -2.013  -3.568  1.00 47.48  ? 287 GLN A CA    1 
ATOM   2267 C  C     . GLN A 1 315 ? 17.335  -2.077  -2.169  1.00 35.16  ? 287 GLN A C     1 
ATOM   2268 O  O     . GLN A 1 315 ? 16.141  -1.845  -1.976  1.00 43.61  ? 287 GLN A O     1 
ATOM   2269 C  CB    . GLN A 1 315 ? 17.933  -0.570  -4.061  1.00 43.85  ? 287 GLN A CB    1 
ATOM   2270 C  CG    . GLN A 1 315 ? 19.218  0.137   -3.685  1.00 48.31  ? 287 GLN A CG    1 
ATOM   2271 C  CD    . GLN A 1 315 ? 20.189  0.235   -4.827  1.00 46.20  ? 287 GLN A CD    1 
ATOM   2272 O  OE1   . GLN A 1 315 ? 19.853  -0.042  -6.000  1.00 39.14  ? 287 GLN A OE1   1 
ATOM   2273 N  NE2   . GLN A 1 315 ? 21.416  0.638   -4.502  1.00 53.62  ? 287 GLN A NE2   1 
ATOM   2274 N  N     . ALA A 1 316 ? 18.168  -2.434  -1.198  1.00 28.93  ? 288 ALA A N     1 
ATOM   2275 C  CA    . ALA A 1 316 ? 17.629  -2.676  0.132   1.00 28.96  ? 288 ALA A CA    1 
ATOM   2276 C  C     . ALA A 1 316 ? 17.238  -1.387  0.840   1.00 28.37  ? 288 ALA A C     1 
ATOM   2277 O  O     . ALA A 1 316 ? 16.488  -1.430  1.812   1.00 34.47  ? 288 ALA A O     1 
ATOM   2278 C  CB    . ALA A 1 316 ? 18.644  -3.452  0.976   1.00 26.64  ? 288 ALA A CB    1 
ATOM   2279 N  N     . LEU A 1 317 ? 17.763  -0.255  0.407   1.00 24.73  ? 289 LEU A N     1 
ATOM   2280 C  CA    . LEU A 1 317 ? 17.522  1.015   1.053   1.00 25.32  ? 289 LEU A CA    1 
ATOM   2281 C  C     . LEU A 1 317 ? 17.177  2.017   -0.026  1.00 29.06  ? 289 LEU A C     1 
ATOM   2282 O  O     . LEU A 1 317 ? 17.938  2.171   -0.989  1.00 24.50  ? 289 LEU A O     1 
ATOM   2283 C  CB    . LEU A 1 317 ? 18.750  1.476   1.834   1.00 25.38  ? 289 LEU A CB    1 
ATOM   2284 C  CG    . LEU A 1 317 ? 18.680  2.891   2.404   1.00 23.28  ? 289 LEU A CG    1 
ATOM   2285 C  CD1   . LEU A 1 317 ? 17.553  3.063   3.420   1.00 19.31  ? 289 LEU A CD1   1 
ATOM   2286 C  CD2   . LEU A 1 317 ? 20.035  3.211   3.039   1.00 23.66  ? 289 LEU A CD2   1 
ATOM   2287 N  N     . VAL A 1 318 ? 16.018  2.664   0.111   1.00 19.68  ? 290 VAL A N     1 
ATOM   2288 C  CA    . VAL A 1 318 ? 15.611  3.745   -0.777  1.00 23.42  ? 290 VAL A CA    1 
ATOM   2289 C  C     . VAL A 1 318 ? 15.130  4.903   0.086   1.00 23.40  ? 290 VAL A C     1 
ATOM   2290 O  O     . VAL A 1 318 ? 14.623  4.704   1.191   1.00 25.55  ? 290 VAL A O     1 
ATOM   2291 C  CB    . VAL A 1 318 ? 14.517  3.317   -1.796  1.00 21.54  ? 290 VAL A CB    1 
ATOM   2292 C  CG1   . VAL A 1 318 ? 14.984  2.098   -2.600  1.00 21.45  ? 290 VAL A CG1   1 
ATOM   2293 C  CG2   . VAL A 1 318 ? 13.151  3.058   -1.109  1.00 21.09  ? 290 VAL A CG2   1 
ATOM   2294 N  N     . PHE A 1 319 ? 15.331  6.131   -0.398  1.00 19.73  ? 291 PHE A N     1 
ATOM   2295 C  CA    . PHE A 1 319 ? 14.783  7.269   0.318   1.00 21.93  ? 291 PHE A CA    1 
ATOM   2296 C  C     . PHE A 1 319 ? 14.539  8.391   -0.668  1.00 22.63  ? 291 PHE A C     1 
ATOM   2297 O  O     . PHE A 1 319 ? 15.088  8.417   -1.774  1.00 22.37  ? 291 PHE A O     1 
ATOM   2298 C  CB    . PHE A 1 319 ? 15.667  7.740   1.497   1.00 19.45  ? 291 PHE A CB    1 
ATOM   2299 C  CG    . PHE A 1 319 ? 17.137  7.814   1.184   1.00 19.95  ? 291 PHE A CG    1 
ATOM   2300 C  CD1   . PHE A 1 319 ? 17.690  8.968   0.649   1.00 21.08  ? 291 PHE A CD1   1 
ATOM   2301 C  CD2   . PHE A 1 319 ? 17.975  6.743   1.476   1.00 19.06  ? 291 PHE A CD2   1 
ATOM   2302 C  CE1   . PHE A 1 319 ? 19.040  9.034   0.354   1.00 20.79  ? 291 PHE A CE1   1 
ATOM   2303 C  CE2   . PHE A 1 319 ? 19.333  6.792   1.176   1.00 21.57  ? 291 PHE A CE2   1 
ATOM   2304 C  CZ    . PHE A 1 319 ? 19.865  7.938   0.610   1.00 25.07  ? 291 PHE A CZ    1 
ATOM   2305 N  N     . SER A 1 320 ? 13.675  9.304   -0.256  1.00 24.65  ? 292 SER A N     1 
ATOM   2306 C  CA    . SER A 1 320 ? 13.220  10.387  -1.108  1.00 28.98  ? 292 SER A CA    1 
ATOM   2307 C  C     . SER A 1 320 ? 14.242  11.519  -1.161  1.00 27.07  ? 292 SER A C     1 
ATOM   2308 O  O     . SER A 1 320 ? 15.121  11.641  -0.317  1.00 23.79  ? 292 SER A O     1 
ATOM   2309 C  CB    . SER A 1 320 ? 11.906  10.939  -0.585  1.00 27.21  ? 292 SER A CB    1 
ATOM   2310 O  OG    . SER A 1 320 ? 12.124  11.477  0.704   1.00 25.77  ? 292 SER A OG    1 
ATOM   2311 N  N     . SER A 1 321 ? 14.060  12.374  -2.159  1.00 25.86  ? 293 SER A N     1 
ATOM   2312 C  CA    . SER A 1 321 ? 14.837  13.588  -2.323  1.00 27.57  ? 293 SER A CA    1 
ATOM   2313 C  C     . SER A 1 321 ? 14.838  14.439  -1.069  1.00 26.29  ? 293 SER A C     1 
ATOM   2314 O  O     . SER A 1 321 ? 15.881  14.980  -0.683  1.00 30.75  ? 293 SER A O     1 
ATOM   2315 C  CB    . SER A 1 321 ? 14.261  14.393  -3.493  1.00 27.06  ? 293 SER A CB    1 
ATOM   2316 O  OG    . SER A 1 321 ? 14.974  15.590  -3.655  1.00 33.46  ? 293 SER A OG    1 
ATOM   2317 N  N     . GLU A 1 322 ? 13.671  14.608  -0.442  1.00 24.21  ? 294 GLU A N     1 
ATOM   2318 C  CA    . GLU A 1 322 ? 13.598  15.409  0.776   1.00 29.84  ? 294 GLU A CA    1 
ATOM   2319 C  C     . GLU A 1 322 ? 14.523  14.863  1.860   1.00 29.98  ? 294 GLU A C     1 
ATOM   2320 O  O     . GLU A 1 322 ? 15.202  15.632  2.542   1.00 31.41  ? 294 GLU A O     1 
ATOM   2321 C  CB    . GLU A 1 322 ? 12.159  15.477  1.284   1.00 31.55  ? 294 GLU A CB    1 
ATOM   2322 C  CG    . GLU A 1 322 ? 11.303  16.521  0.584   1.00 39.18  ? 294 GLU A CG    1 
ATOM   2323 C  CD    . GLU A 1 322 ? 9.826   16.397  0.929   1.00 46.36  ? 294 GLU A CD    1 
ATOM   2324 O  OE1   . GLU A 1 322 ? 9.464   15.497  1.715   1.00 51.07  ? 294 GLU A OE1   1 
ATOM   2325 O  OE2   . GLU A 1 322 ? 9.020   17.199  0.408   1.00 56.57  ? 294 GLU A OE2   1 
ATOM   2326 N  N     . VAL A 1 323 ? 14.558  13.541  2.035   1.00 29.12  ? 295 VAL A N     1 
ATOM   2327 C  CA    . VAL A 1 323 ? 15.477  12.948  3.007   1.00 28.03  ? 295 VAL A CA    1 
ATOM   2328 C  C     . VAL A 1 323 ? 16.914  13.217  2.582   1.00 30.63  ? 295 VAL A C     1 
ATOM   2329 O  O     . VAL A 1 323 ? 17.736  13.723  3.362   1.00 31.14  ? 295 VAL A O     1 
ATOM   2330 C  CB    . VAL A 1 323 ? 15.207  11.438  3.159   1.00 20.72  ? 295 VAL A CB    1 
ATOM   2331 C  CG1   . VAL A 1 323 ? 16.317  10.767  3.990   1.00 22.47  ? 295 VAL A CG1   1 
ATOM   2332 C  CG2   . VAL A 1 323 ? 13.863  11.181  3.834   1.00 19.99  ? 295 VAL A CG2   1 
ATOM   2333 N  N     . LYS A 1 324 ? 17.221  12.896  1.325   1.00 24.01  ? 296 LYS A N     1 
ATOM   2334 C  CA    . LYS A 1 324 ? 18.573  13.015  0.791   1.00 29.49  ? 296 LYS A CA    1 
ATOM   2335 C  C     . LYS A 1 324 ? 19.112  14.422  0.980   1.00 32.71  ? 296 LYS A C     1 
ATOM   2336 O  O     . LYS A 1 324 ? 20.254  14.609  1.432   1.00 34.56  ? 296 LYS A O     1 
ATOM   2337 C  CB    . LYS A 1 324 ? 18.564  12.610  -0.698  1.00 23.35  ? 296 LYS A CB    1 
ATOM   2338 C  CG    . LYS A 1 324 ? 19.911  12.696  -1.416  1.00 31.87  ? 296 LYS A CG    1 
ATOM   2339 C  CD    . LYS A 1 324 ? 20.004  13.920  -2.270  1.00 28.28  ? 296 LYS A CD    1 
ATOM   2340 C  CE    . LYS A 1 324 ? 21.273  13.915  -3.129  1.00 32.71  ? 296 LYS A CE    1 
ATOM   2341 N  NZ    . LYS A 1 324 ? 21.434  15.265  -3.763  1.00 34.72  ? 296 LYS A NZ    1 
ATOM   2342 N  N     . ASN A 1 325 ? 18.290  15.428  0.686   1.00 31.99  ? 297 ASN A N     1 
ATOM   2343 C  CA    . ASN A 1 325 ? 18.743  16.802  0.828   1.00 33.46  ? 297 ASN A CA    1 
ATOM   2344 C  C     . ASN A 1 325 ? 18.628  17.337  2.254   1.00 39.96  ? 297 ASN A C     1 
ATOM   2345 O  O     . ASN A 1 325 ? 19.236  18.373  2.559   1.00 39.99  ? 297 ASN A O     1 
ATOM   2346 C  CB    . ASN A 1 325 ? 18.001  17.675  -0.190  1.00 37.71  ? 297 ASN A CB    1 
ATOM   2347 C  CG    . ASN A 1 325 ? 18.486  17.408  -1.615  1.00 41.17  ? 297 ASN A CG    1 
ATOM   2348 O  OD1   . ASN A 1 325 ? 19.615  17.760  -1.963  1.00 46.21  ? 297 ASN A OD1   1 
ATOM   2349 N  ND2   . ASN A 1 325 ? 17.652  16.760  -2.433  1.00 35.48  ? 297 ASN A ND2   1 
ATOM   2350 N  N     . SER A 1 326 ? 17.935  16.641  3.156   1.00 34.14  ? 298 SER A N     1 
ATOM   2351 C  CA    . SER A 1 326 ? 18.030  17.020  4.566   1.00 35.60  ? 298 SER A CA    1 
ATOM   2352 C  C     . SER A 1 326 ? 19.310  16.525  5.222   1.00 34.84  ? 298 SER A C     1 
ATOM   2353 O  O     . SER A 1 326 ? 19.757  17.105  6.220   1.00 33.80  ? 298 SER A O     1 
ATOM   2354 C  CB    . SER A 1 326 ? 16.850  16.477  5.357   1.00 32.48  ? 298 SER A CB    1 
ATOM   2355 O  OG    . SER A 1 326 ? 15.737  17.328  5.236   1.00 56.80  ? 298 SER A OG    1 
ATOM   2356 N  N     . ALA A 1 327 ? 19.903  15.458  4.699   1.00 33.90  ? 299 ALA A N     1 
ATOM   2357 C  CA    . ALA A 1 327 ? 21.150  14.948  5.248   1.00 29.84  ? 299 ALA A CA    1 
ATOM   2358 C  C     . ALA A 1 327 ? 22.232  16.016  5.179   1.00 40.19  ? 299 ALA A C     1 
ATOM   2359 O  O     . ALA A 1 327 ? 22.267  16.824  4.250   1.00 46.18  ? 299 ALA A O     1 
ATOM   2360 C  CB    . ALA A 1 327 ? 21.588  13.700  4.477   1.00 33.31  ? 299 ALA A CB    1 
ATOM   2361 N  N     . THR A 1 328 ? 23.126  16.026  6.176   1.00 37.48  ? 300 THR A N     1 
ATOM   2362 C  CA    . THR A 1 328 ? 24.289  16.914  6.129   1.00 42.61  ? 300 THR A CA    1 
ATOM   2363 C  C     . THR A 1 328 ? 25.600  16.204  5.837   1.00 42.20  ? 300 THR A C     1 
ATOM   2364 O  O     . THR A 1 328 ? 26.527  16.841  5.333   1.00 43.98  ? 300 THR A O     1 
ATOM   2365 C  CB    . THR A 1 328 ? 24.462  17.675  7.448   1.00 39.17  ? 300 THR A CB    1 
ATOM   2366 O  OG1   . THR A 1 328 ? 24.607  16.742  8.527   1.00 40.85  ? 300 THR A OG1   1 
ATOM   2367 C  CG2   . THR A 1 328 ? 23.267  18.538  7.708   1.00 35.36  ? 300 THR A CG2   1 
ATOM   2368 N  N     . LYS A 1 329 ? 25.721  14.922  6.159   1.00 37.17  ? 301 LYS A N     1 
ATOM   2369 C  CA    . LYS A 1 329 ? 27.003  14.269  5.970   1.00 35.21  ? 301 LYS A CA    1 
ATOM   2370 C  C     . LYS A 1 329 ? 27.190  13.900  4.508   1.00 37.04  ? 301 LYS A C     1 
ATOM   2371 O  O     . LYS A 1 329 ? 26.243  13.887  3.716   1.00 35.11  ? 301 LYS A O     1 
ATOM   2372 C  CB    . LYS A 1 329 ? 27.142  13.030  6.854   1.00 32.04  ? 301 LYS A CB    1 
ATOM   2373 C  CG    . LYS A 1 329 ? 26.909  13.265  8.349   1.00 41.74  ? 301 LYS A CG    1 
ATOM   2374 C  CD    . LYS A 1 329 ? 27.246  12.003  9.153   1.00 37.76  ? 301 LYS A CD    1 
ATOM   2375 C  CE    . LYS A 1 329 ? 26.908  12.142  10.635  1.00 52.36  ? 301 LYS A CE    1 
ATOM   2376 N  NZ    . LYS A 1 329 ? 27.579  13.301  11.262  1.00 58.52  ? 301 LYS A NZ    1 
ATOM   2377 N  N     . SER A 1 330 ? 28.436  13.599  4.147   1.00 40.56  ? 302 SER A N     1 
ATOM   2378 C  CA    . SER A 1 330 ? 28.772  13.357  2.745   1.00 35.98  ? 302 SER A CA    1 
ATOM   2379 C  C     . SER A 1 330 ? 28.558  11.886  2.391   1.00 35.21  ? 302 SER A C     1 
ATOM   2380 O  O     . SER A 1 330 ? 29.481  11.136  2.072   1.00 30.76  ? 302 SER A O     1 
ATOM   2381 C  CB    . SER A 1 330 ? 30.195  13.817  2.463   1.00 43.79  ? 302 SER A CB    1 
ATOM   2382 O  OG    . SER A 1 330 ? 30.261  15.220  2.623   1.00 51.61  ? 302 SER A OG    1 
ATOM   2383 N  N     . TRP A 1 331 ? 27.285  11.491  2.407   1.00 30.55  ? 303 TRP A N     1 
ATOM   2384 C  CA    . TRP A 1 331 ? 26.911  10.137  2.025   1.00 25.58  ? 303 TRP A CA    1 
ATOM   2385 C  C     . TRP A 1 331 ? 27.194  9.908   0.545   1.00 21.42  ? 303 TRP A C     1 
ATOM   2386 O  O     . TRP A 1 331 ? 27.112  10.827  -0.270  1.00 26.80  ? 303 TRP A O     1 
ATOM   2387 C  CB    . TRP A 1 331 ? 25.427  9.912   2.297   1.00 23.76  ? 303 TRP A CB    1 
ATOM   2388 C  CG    . TRP A 1 331 ? 25.066  10.030  3.751   1.00 28.20  ? 303 TRP A CG    1 
ATOM   2389 C  CD1   . TRP A 1 331 ? 24.468  11.092  4.372   1.00 29.21  ? 303 TRP A CD1   1 
ATOM   2390 C  CD2   . TRP A 1 331 ? 25.302  9.049   4.769   1.00 23.38  ? 303 TRP A CD2   1 
ATOM   2391 N  NE1   . TRP A 1 331 ? 24.288  10.815  5.713   1.00 28.32  ? 303 TRP A NE1   1 
ATOM   2392 C  CE2   . TRP A 1 331 ? 24.789  9.566   5.980   1.00 28.93  ? 303 TRP A CE2   1 
ATOM   2393 C  CE3   . TRP A 1 331 ? 25.887  7.778   4.771   1.00 25.26  ? 303 TRP A CE3   1 
ATOM   2394 C  CZ2   . TRP A 1 331 ? 24.850  8.855   7.182   1.00 29.79  ? 303 TRP A CZ2   1 
ATOM   2395 C  CZ3   . TRP A 1 331 ? 25.927  7.062   5.958   1.00 25.89  ? 303 TRP A CZ3   1 
ATOM   2396 C  CH2   . TRP A 1 331 ? 25.419  7.607   7.149   1.00 27.56  ? 303 TRP A CH2   1 
ATOM   2397 N  N     . ASN A 1 332 ? 27.494  8.657   0.193   1.00 23.18  ? 304 ASN A N     1 
ATOM   2398 C  CA    . ASN A 1 332 ? 27.735  8.287   -1.200  1.00 24.29  ? 304 ASN A CA    1 
ATOM   2399 C  C     . ASN A 1 332 ? 26.397  8.037   -1.903  1.00 27.03  ? 304 ASN A C     1 
ATOM   2400 O  O     . ASN A 1 332 ? 26.049  6.913   -2.271  1.00 25.55  ? 304 ASN A O     1 
ATOM   2401 C  CB    . ASN A 1 332 ? 28.652  7.075   -1.277  1.00 29.42  ? 304 ASN A CB    1 
ATOM   2402 C  CG    . ASN A 1 332 ? 29.960  7.281   -0.504  1.00 38.73  ? 304 ASN A CG    1 
ATOM   2403 O  OD1   . ASN A 1 332 ? 30.474  8.393   -0.425  1.00 35.25  ? 304 ASN A OD1   1 
ATOM   2404 N  ND2   . ASN A 1 332 ? 30.478  6.215   0.084   1.00 30.99  ? 304 ASN A ND2   1 
ATOM   2405 N  N     . PHE A 1 333 ? 25.653  9.135   -2.097  1.00 28.63  ? 305 PHE A N     1 
ATOM   2406 C  CA    . PHE A 1 333 ? 24.308  9.083   -2.673  1.00 23.34  ? 305 PHE A CA    1 
ATOM   2407 C  C     . PHE A 1 333 ? 24.354  8.609   -4.118  1.00 26.90  ? 305 PHE A C     1 
ATOM   2408 O  O     . PHE A 1 333 ? 25.263  8.963   -4.871  1.00 24.58  ? 305 PHE A O     1 
ATOM   2409 C  CB    . PHE A 1 333 ? 23.644  10.463  -2.651  1.00 22.70  ? 305 PHE A CB    1 
ATOM   2410 C  CG    . PHE A 1 333 ? 23.307  10.988  -1.280  1.00 24.34  ? 305 PHE A CG    1 
ATOM   2411 C  CD1   . PHE A 1 333 ? 22.474  10.276  -0.422  1.00 21.63  ? 305 PHE A CD1   1 
ATOM   2412 C  CD2   . PHE A 1 333 ? 23.789  12.227  -0.868  1.00 24.29  ? 305 PHE A CD2   1 
ATOM   2413 C  CE1   . PHE A 1 333 ? 22.151  10.778  0.832   1.00 25.84  ? 305 PHE A CE1   1 
ATOM   2414 C  CE2   . PHE A 1 333 ? 23.488  12.727  0.393   1.00 26.60  ? 305 PHE A CE2   1 
ATOM   2415 C  CZ    . PHE A 1 333 ? 22.665  12.022  1.238   1.00 24.07  ? 305 PHE A CZ    1 
ATOM   2416 N  N     . ILE A 1 334 ? 23.345  7.838   -4.521  1.00 24.68  ? 306 ILE A N     1 
ATOM   2417 C  CA    . ILE A 1 334 ? 23.153  7.496   -5.926  1.00 24.94  ? 306 ILE A CA    1 
ATOM   2418 C  C     . ILE A 1 334 ? 21.682  7.710   -6.286  1.00 24.63  ? 306 ILE A C     1 
ATOM   2419 O  O     . ILE A 1 334 ? 20.788  7.304   -5.534  1.00 25.33  ? 306 ILE A O     1 
ATOM   2420 C  CB    . ILE A 1 334 ? 23.599  6.049   -6.220  1.00 22.22  ? 306 ILE A CB    1 
ATOM   2421 C  CG1   . ILE A 1 334 ? 23.422  5.710   -7.717  1.00 24.23  ? 306 ILE A CG1   1 
ATOM   2422 C  CG2   . ILE A 1 334 ? 22.883  5.032   -5.296  1.00 22.46  ? 306 ILE A CG2   1 
ATOM   2423 C  CD1   . ILE A 1 334 ? 24.244  4.520   -8.157  1.00 27.31  ? 306 ILE A CD1   1 
ATOM   2424 N  N     . TRP A 1 335 ? 21.430  8.382   -7.413  1.00 24.42  ? 307 TRP A N     1 
ATOM   2425 C  CA    . TRP A 1 335 ? 20.072  8.527   -7.929  1.00 24.60  ? 307 TRP A CA    1 
ATOM   2426 C  C     . TRP A 1 335 ? 19.638  7.223   -8.596  1.00 27.44  ? 307 TRP A C     1 
ATOM   2427 O  O     . TRP A 1 335 ? 20.404  6.639   -9.375  1.00 24.73  ? 307 TRP A O     1 
ATOM   2428 C  CB    . TRP A 1 335 ? 19.990  9.693   -8.926  1.00 28.54  ? 307 TRP A CB    1 
ATOM   2429 C  CG    . TRP A 1 335 ? 18.596  9.872   -9.498  1.00 26.77  ? 307 TRP A CG    1 
ATOM   2430 C  CD1   . TRP A 1 335 ? 17.584  10.636  -8.986  1.00 28.08  ? 307 TRP A CD1   1 
ATOM   2431 C  CD2   . TRP A 1 335 ? 18.069  9.248   -10.681 1.00 25.02  ? 307 TRP A CD2   1 
ATOM   2432 N  NE1   . TRP A 1 335 ? 16.461  10.532  -9.781  1.00 25.73  ? 307 TRP A NE1   1 
ATOM   2433 C  CE2   . TRP A 1 335 ? 16.733  9.679   -10.822 1.00 28.67  ? 307 TRP A CE2   1 
ATOM   2434 C  CE3   . TRP A 1 335 ? 18.596  8.357   -11.626 1.00 26.24  ? 307 TRP A CE3   1 
ATOM   2435 C  CZ2   . TRP A 1 335 ? 15.914  9.256   -11.882 1.00 27.77  ? 307 TRP A CZ2   1 
ATOM   2436 C  CZ3   . TRP A 1 335 ? 17.780  7.935   -12.674 1.00 31.88  ? 307 TRP A CZ3   1 
ATOM   2437 C  CH2   . TRP A 1 335 ? 16.448  8.382   -12.786 1.00 22.56  ? 307 TRP A CH2   1 
ATOM   2438 N  N     . LEU A 1 336 ? 18.412  6.764   -8.299  1.00 19.98  ? 308 LEU A N     1 
ATOM   2439 C  CA    . LEU A 1 336 ? 17.903  5.500   -8.824  1.00 26.19  ? 308 LEU A CA    1 
ATOM   2440 C  C     . LEU A 1 336 ? 16.762  5.653   -9.824  1.00 28.62  ? 308 LEU A C     1 
ATOM   2441 O  O     . LEU A 1 336 ? 16.796  5.029   -10.886 1.00 28.21  ? 308 LEU A O     1 
ATOM   2442 C  CB    . LEU A 1 336 ? 17.450  4.593   -7.676  1.00 27.37  ? 308 LEU A CB    1 
ATOM   2443 C  CG    . LEU A 1 336 ? 18.548  4.229   -6.679  1.00 32.10  ? 308 LEU A CG    1 
ATOM   2444 C  CD1   . LEU A 1 336 ? 17.972  3.310   -5.637  1.00 29.92  ? 308 LEU A CD1   1 
ATOM   2445 C  CD2   . LEU A 1 336 ? 19.697  3.552   -7.414  1.00 25.61  ? 308 LEU A CD2   1 
ATOM   2446 N  N     . THR A 1 337 ? 15.743  6.446   -9.509  1.00 25.34  ? 309 THR A N     1 
ATOM   2447 C  CA    . THR A 1 337 ? 14.515  6.527   -10.296 1.00 25.21  ? 309 THR A CA    1 
ATOM   2448 C  C     . THR A 1 337 ? 13.666  7.651   -9.708  1.00 29.92  ? 309 THR A C     1 
ATOM   2449 O  O     . THR A 1 337 ? 13.989  8.207   -8.653  1.00 28.02  ? 309 THR A O     1 
ATOM   2450 C  CB    . THR A 1 337 ? 13.744  5.185   -10.286 1.00 31.13  ? 309 THR A CB    1 
ATOM   2451 O  OG1   . THR A 1 337 ? 12.720  5.190   -11.299 1.00 30.77  ? 309 THR A OG1   1 
ATOM   2452 C  CG2   . THR A 1 337 ? 13.083  4.960   -8.919  1.00 30.37  ? 309 THR A CG2   1 
ATOM   2453 N  N     . ASP A 1 338 ? 12.608  8.026   -10.441 1.00 31.39  ? 310 ASP A N     1 
ATOM   2454 C  CA    . ASP A 1 338 ? 11.451  8.740   -9.907  1.00 24.33  ? 310 ASP A CA    1 
ATOM   2455 C  C     . ASP A 1 338 ? 10.352  7.800   -9.455  1.00 25.77  ? 310 ASP A C     1 
ATOM   2456 O  O     . ASP A 1 338 ? 10.134  6.736   -10.037 1.00 30.62  ? 310 ASP A O     1 
ATOM   2457 C  CB    . ASP A 1 338 ? 10.854  9.727   -10.915 1.00 28.22  ? 310 ASP A CB    1 
ATOM   2458 C  CG    . ASP A 1 338 ? 11.703  10.942  -11.129 1.00 29.69  ? 310 ASP A CG    1 
ATOM   2459 O  OD1   . ASP A 1 338 ? 12.716  10.893  -11.838 1.00 26.00  ? 310 ASP A OD1   1 
ATOM   2460 O  OD2   . ASP A 1 338 ? 11.208  12.017  -10.696 1.00 31.13  ? 310 ASP A OD2   1 
ATOM   2461 N  N     . SER A 1 339 ? 9.627   8.236   -8.431  1.00 29.08  ? 311 SER A N     1 
ATOM   2462 C  CA    . SER A 1 339 ? 8.420   7.546   -8.016  1.00 30.29  ? 311 SER A CA    1 
ATOM   2463 C  C     . SER A 1 339 ? 7.461   8.581   -7.444  1.00 33.79  ? 311 SER A C     1 
ATOM   2464 O  O     . SER A 1 339 ? 7.720   9.790   -7.446  1.00 33.68  ? 311 SER A O     1 
ATOM   2465 C  CB    . SER A 1 339 ? 8.746   6.438   -7.010  1.00 33.38  ? 311 SER A CB    1 
ATOM   2466 O  OG    . SER A 1 339 ? 7.655   5.541   -6.865  1.00 42.06  ? 311 SER A OG    1 
ATOM   2467 N  N     . GLU A 1 340 ? 6.335   8.102   -6.957  1.00 30.96  ? 312 GLU A N     1 
ATOM   2468 C  CA    . GLU A 1 340 ? 5.423   8.957   -6.230  1.00 37.23  ? 312 GLU A CA    1 
ATOM   2469 C  C     . GLU A 1 340 ? 5.167   8.248   -4.911  1.00 38.96  ? 312 GLU A C     1 
ATOM   2470 O  O     . GLU A 1 340 ? 4.973   7.029   -4.896  1.00 43.44  ? 312 GLU A O     1 
ATOM   2471 C  CB    . GLU A 1 340 ? 4.151   9.190   -7.043  1.00 35.61  ? 312 GLU A CB    1 
ATOM   2472 C  CG    . GLU A 1 340 ? 3.420   10.451  -6.630  1.00 51.03  ? 312 GLU A CG    1 
ATOM   2473 C  CD    . GLU A 1 340 ? 2.660   10.270  -5.331  1.00 55.88  ? 312 GLU A CD    1 
ATOM   2474 O  OE1   . GLU A 1 340 ? 2.354   9.100   -4.997  1.00 54.51  ? 312 GLU A OE1   1 
ATOM   2475 O  OE2   . GLU A 1 340 ? 2.412   11.286  -4.629  1.00 51.10  ? 312 GLU A OE2   1 
ATOM   2476 N  N     . LEU A 1 341 ? 5.250   8.981   -3.804  1.00 33.68  ? 313 LEU A N     1 
ATOM   2477 C  CA    . LEU A 1 341 ? 5.060   8.357   -2.504  1.00 38.57  ? 313 LEU A CA    1 
ATOM   2478 C  C     . LEU A 1 341 ? 3.802   8.817   -1.782  1.00 47.25  ? 313 LEU A C     1 
ATOM   2479 O  O     . LEU A 1 341 ? 3.227   8.041   -1.011  1.00 45.05  ? 313 LEU A O     1 
ATOM   2480 C  CB    . LEU A 1 341 ? 6.279   8.608   -1.606  1.00 41.57  ? 313 LEU A CB    1 
ATOM   2481 C  CG    . LEU A 1 341 ? 7.611   7.985   -2.046  1.00 40.93  ? 313 LEU A CG    1 
ATOM   2482 C  CD1   . LEU A 1 341 ? 8.677   8.244   -0.995  1.00 37.17  ? 313 LEU A CD1   1 
ATOM   2483 C  CD2   . LEU A 1 341 ? 7.464   6.486   -2.310  1.00 32.47  ? 313 LEU A CD2   1 
ATOM   2484 N  N     . LYS A 1 342 ? 3.334   10.037  -2.040  1.00 43.18  ? 314 LYS A N     1 
ATOM   2485 C  CA    . LYS A 1 342 ? 2.306   10.664  -1.217  1.00 48.76  ? 314 LYS A CA    1 
ATOM   2486 C  C     . LYS A 1 342 ? 0.896   10.523  -1.789  1.00 56.55  ? 314 LYS A C     1 
ATOM   2487 O  O     . LYS A 1 342 ? -0.067  10.942  -1.137  1.00 54.13  ? 314 LYS A O     1 
ATOM   2488 C  CB    . LYS A 1 342 ? 2.648   12.145  -1.021  1.00 46.90  ? 314 LYS A CB    1 
ATOM   2489 C  CG    . LYS A 1 342 ? 4.012   12.384  -0.339  1.00 44.10  ? 314 LYS A CG    1 
ATOM   2490 C  CD    . LYS A 1 342 ? 4.101   11.741  1.040   1.00 52.60  ? 314 LYS A CD    1 
ATOM   2491 C  CE    . LYS A 1 342 ? 5.456   12.041  1.709   1.00 50.86  ? 314 LYS A CE    1 
ATOM   2492 N  NZ    . LYS A 1 342 ? 5.681   13.506  1.906   1.00 52.97  ? 314 LYS A NZ    1 
ATOM   2493 N  N     . GLY A 1 343 ? 0.745   9.928   -2.972  1.00 55.94  ? 315 GLY A N     1 
ATOM   2494 C  CA    . GLY A 1 343 ? -0.530  9.936   -3.662  1.00 61.47  ? 315 GLY A CA    1 
ATOM   2495 C  C     . GLY A 1 343 ? -0.847  11.237  -4.365  1.00 53.17  ? 315 GLY A C     1 
ATOM   2496 O  O     . GLY A 1 343 ? -1.935  11.364  -4.938  1.00 65.21  ? 315 GLY A O     1 
ATOM   2497 N  N     . LYS A 1 344 ? 0.051   12.215  -4.305  1.00 55.11  ? 316 LYS A N     1 
ATOM   2498 C  CA    . LYS A 1 344 ? -0.033  13.420  -5.117  1.00 61.41  ? 316 LYS A CA    1 
ATOM   2499 C  C     . LYS A 1 344 ? 0.330   13.061  -6.561  1.00 52.99  ? 316 LYS A C     1 
ATOM   2500 O  O     . LYS A 1 344 ? 0.532   11.896  -6.920  1.00 59.59  ? 316 LYS A O     1 
ATOM   2501 C  CB    . LYS A 1 344 ? 0.897   14.495  -4.556  1.00 65.42  ? 316 LYS A CB    1 
ATOM   2502 C  CG    . LYS A 1 344 ? 0.496   15.047  -3.191  1.00 63.82  ? 316 LYS A CG    1 
ATOM   2503 C  CD    . LYS A 1 344 ? -0.617  16.079  -3.326  1.00 69.52  ? 316 LYS A CD    1 
ATOM   2504 C  CE    . LYS A 1 344 ? -0.863  16.817  -2.021  1.00 68.84  ? 316 LYS A CE    1 
ATOM   2505 N  NZ    . LYS A 1 344 ? -1.167  15.877  -0.905  1.00 61.58  ? 316 LYS A NZ    1 
ATOM   2506 N  N     . SER A 1 345 ? 0.446   14.068  -7.412  1.00 48.10  ? 317 SER A N     1 
ATOM   2507 C  CA    . SER A 1 345 ? 0.988   13.845  -8.743  1.00 55.48  ? 317 SER A CA    1 
ATOM   2508 C  C     . SER A 1 345 ? 2.463   14.228  -8.833  1.00 54.43  ? 317 SER A C     1 
ATOM   2509 O  O     . SER A 1 345 ? 3.038   14.190  -9.926  1.00 49.16  ? 317 SER A O     1 
ATOM   2510 C  CB    . SER A 1 345 ? 0.170   14.614  -9.779  1.00 56.00  ? 317 SER A CB    1 
ATOM   2511 O  OG    . SER A 1 345 ? 0.031   15.969  -9.388  1.00 66.02  ? 317 SER A OG    1 
ATOM   2512 N  N     . GLU A 1 346 ? 3.086   14.589  -7.711  1.00 45.54  ? 318 GLU A N     1 
ATOM   2513 C  CA    . GLU A 1 346 ? 4.471   15.044  -7.717  1.00 51.17  ? 318 GLU A CA    1 
ATOM   2514 C  C     . GLU A 1 346 ? 5.411   13.855  -7.891  1.00 36.10  ? 318 GLU A C     1 
ATOM   2515 O  O     . GLU A 1 346 ? 5.379   12.908  -7.103  1.00 41.95  ? 318 GLU A O     1 
ATOM   2516 C  CB    . GLU A 1 346 ? 4.779   15.798  -6.427  1.00 53.08  ? 318 GLU A CB    1 
ATOM   2517 C  CG    . GLU A 1 346 ? 3.931   17.049  -6.242  1.00 60.10  ? 318 GLU A CG    1 
ATOM   2518 C  CD    . GLU A 1 346 ? 4.347   18.181  -7.167  1.00 71.42  ? 318 GLU A CD    1 
ATOM   2519 O  OE1   . GLU A 1 346 ? 3.824   18.250  -8.305  1.00 76.39  ? 318 GLU A OE1   1 
ATOM   2520 O  OE2   . GLU A 1 346 ? 5.195   19.005  -6.758  1.00 72.42  ? 318 GLU A OE2   1 
ATOM   2521 N  N     . SER A 1 347 ? 6.218   13.889  -8.940  1.00 31.30  ? 319 SER A N     1 
ATOM   2522 C  CA    . SER A 1 347 ? 7.243   12.879  -9.180  1.00 31.58  ? 319 SER A CA    1 
ATOM   2523 C  C     . SER A 1 347 ? 8.508   13.250  -8.420  1.00 32.42  ? 319 SER A C     1 
ATOM   2524 O  O     . SER A 1 347 ? 9.110   14.291  -8.698  1.00 30.22  ? 319 SER A O     1 
ATOM   2525 C  CB    . SER A 1 347 ? 7.552   12.785  -10.669 1.00 28.84  ? 319 SER A CB    1 
ATOM   2526 O  OG    . SER A 1 347 ? 8.445   11.721  -10.941 1.00 30.35  ? 319 SER A OG    1 
ATOM   2527 N  N     . ILE A 1 348 ? 8.932   12.402  -7.490  1.00 28.75  ? 320 ILE A N     1 
ATOM   2528 C  CA    . ILE A 1 348 ? 10.079  12.752  -6.655  1.00 28.57  ? 320 ILE A CA    1 
ATOM   2529 C  C     . ILE A 1 348 ? 11.245  11.823  -6.971  1.00 34.24  ? 320 ILE A C     1 
ATOM   2530 O  O     . ILE A 1 348 ? 11.059  10.662  -7.359  1.00 28.51  ? 320 ILE A O     1 
ATOM   2531 C  CB    . ILE A 1 348 ? 9.757   12.686  -5.152  1.00 35.23  ? 320 ILE A CB    1 
ATOM   2532 C  CG1   . ILE A 1 348 ? 9.428   11.252  -4.770  1.00 34.60  ? 320 ILE A CG1   1 
ATOM   2533 C  CG2   . ILE A 1 348 ? 8.592   13.633  -4.814  1.00 38.64  ? 320 ILE A CG2   1 
ATOM   2534 C  CD1   . ILE A 1 348 ? 9.425   11.022  -3.290  1.00 44.01  ? 320 ILE A CD1   1 
ATOM   2535 N  N     . ASP A 1 349 ? 12.461  12.339  -6.775  1.00 25.68  ? 321 ASP A N     1 
ATOM   2536 C  CA    . ASP A 1 349 ? 13.669  11.562  -7.005  1.00 24.56  ? 321 ASP A CA    1 
ATOM   2537 C  C     . ASP A 1 349 ? 13.852  10.580  -5.865  1.00 25.99  ? 321 ASP A C     1 
ATOM   2538 O  O     . ASP A 1 349 ? 13.716  10.955  -4.699  1.00 26.32  ? 321 ASP A O     1 
ATOM   2539 C  CB    . ASP A 1 349 ? 14.893  12.474  -7.096  1.00 28.11  ? 321 ASP A CB    1 
ATOM   2540 C  CG    . ASP A 1 349 ? 14.843  13.410  -8.303  1.00 34.16  ? 321 ASP A CG    1 
ATOM   2541 O  OD1   . ASP A 1 349 ? 14.590  12.924  -9.418  1.00 27.85  ? 321 ASP A OD1   1 
ATOM   2542 O  OD2   . ASP A 1 349 ? 15.052  14.636  -8.139  1.00 29.26  ? 321 ASP A OD2   1 
ATOM   2543 N  N     . ILE A 1 350 ? 14.144  9.323   -6.204  1.00 24.62  ? 322 ILE A N     1 
ATOM   2544 C  CA    . ILE A 1 350 ? 14.440  8.270   -5.236  1.00 25.67  ? 322 ILE A CA    1 
ATOM   2545 C  C     . ILE A 1 350 ? 15.939  8.007   -5.276  1.00 29.03  ? 322 ILE A C     1 
ATOM   2546 O  O     . ILE A 1 350 ? 16.513  7.814   -6.358  1.00 26.69  ? 322 ILE A O     1 
ATOM   2547 C  CB    . ILE A 1 350 ? 13.659  6.971   -5.521  1.00 24.18  ? 322 ILE A CB    1 
ATOM   2548 C  CG1   . ILE A 1 350 ? 12.148  7.195   -5.535  1.00 24.59  ? 322 ILE A CG1   1 
ATOM   2549 C  CG2   . ILE A 1 350 ? 13.974  5.908   -4.436  1.00 24.35  ? 322 ILE A CG2   1 
ATOM   2550 C  CD1   . ILE A 1 350 ? 11.625  7.894   -4.264  1.00 27.19  ? 322 ILE A CD1   1 
ATOM   2551 N  N     . TYR A 1 351 ? 16.571  8.009   -4.104  1.00 22.72  ? 323 TYR A N     1 
ATOM   2552 C  CA    . TYR A 1 351 ? 18.002  7.816   -3.966  1.00 23.19  ? 323 TYR A CA    1 
ATOM   2553 C  C     . TYR A 1 351 ? 18.285  6.596   -3.112  1.00 22.92  ? 323 TYR A C     1 
ATOM   2554 O  O     . TYR A 1 351 ? 17.419  6.115   -2.385  1.00 23.98  ? 323 TYR A O     1 
ATOM   2555 C  CB    . TYR A 1 351 ? 18.678  9.028   -3.310  1.00 21.98  ? 323 TYR A CB    1 
ATOM   2556 C  CG    . TYR A 1 351 ? 18.589  10.275  -4.143  1.00 26.87  ? 323 TYR A CG    1 
ATOM   2557 C  CD1   . TYR A 1 351 ? 17.472  11.082  -4.077  1.00 28.61  ? 323 TYR A CD1   1 
ATOM   2558 C  CD2   . TYR A 1 351 ? 19.626  10.648  -4.992  1.00 26.63  ? 323 TYR A CD2   1 
ATOM   2559 C  CE1   . TYR A 1 351 ? 17.374  12.232  -4.828  1.00 24.14  ? 323 TYR A CE1   1 
ATOM   2560 C  CE2   . TYR A 1 351 ? 19.543  11.799  -5.754  1.00 29.37  ? 323 TYR A CE2   1 
ATOM   2561 C  CZ    . TYR A 1 351 ? 18.405  12.584  -5.669  1.00 29.73  ? 323 TYR A CZ    1 
ATOM   2562 O  OH    . TYR A 1 351 ? 18.296  13.733  -6.406  1.00 30.25  ? 323 TYR A OH    1 
ATOM   2563 N  N     . SER A 1 352 ? 19.531  6.126   -3.172  1.00 25.35  ? 324 SER A N     1 
ATOM   2564 C  CA    . SER A 1 352 ? 20.038  5.198   -2.159  1.00 22.67  ? 324 SER A CA    1 
ATOM   2565 C  C     . SER A 1 352 ? 21.479  5.588   -1.819  1.00 26.04  ? 324 SER A C     1 
ATOM   2566 O  O     . SER A 1 352 ? 21.944  6.682   -2.149  1.00 25.77  ? 324 SER A O     1 
ATOM   2567 C  CB    . SER A 1 352 ? 19.928  3.751   -2.659  1.00 26.07  ? 324 SER A CB    1 
ATOM   2568 O  OG    . SER A 1 352 ? 20.317  2.827   -1.665  1.00 25.94  ? 324 SER A OG    1 
ATOM   2569 N  N     . ILE A 1 353 ? 22.174  4.693   -1.122  1.00 25.79  ? 325 ILE A N     1 
ATOM   2570 C  CA    . ILE A 1 353 ? 23.610  4.798   -0.858  1.00 28.55  ? 325 ILE A CA    1 
ATOM   2571 C  C     . ILE A 1 353 ? 24.284  3.760   -1.727  1.00 29.14  ? 325 ILE A C     1 
ATOM   2572 O  O     . ILE A 1 353 ? 23.847  2.606   -1.759  1.00 31.62  ? 325 ILE A O     1 
ATOM   2573 C  CB    . ILE A 1 353 ? 23.954  4.542   0.620   1.00 32.05  ? 325 ILE A CB    1 
ATOM   2574 C  CG1   . ILE A 1 353 ? 23.199  5.487   1.556   1.00 28.69  ? 325 ILE A CG1   1 
ATOM   2575 C  CG2   . ILE A 1 353 ? 25.459  4.614   0.853   1.00 30.83  ? 325 ILE A CG2   1 
ATOM   2576 C  CD1   . ILE A 1 353 ? 23.572  6.915   1.398   1.00 29.95  ? 325 ILE A CD1   1 
ATOM   2577 N  N     . ASP A 1 354 ? 25.348  4.153   -2.418  1.00 21.70  ? 326 ASP A N     1 
ATOM   2578 C  CA    . ASP A 1 354 ? 26.114  3.220   -3.243  1.00 29.73  ? 326 ASP A CA    1 
ATOM   2579 C  C     . ASP A 1 354 ? 27.308  2.774   -2.410  1.00 38.71  ? 326 ASP A C     1 
ATOM   2580 O  O     . ASP A 1 354 ? 28.244  3.543   -2.194  1.00 32.07  ? 326 ASP A O     1 
ATOM   2581 C  CB    . ASP A 1 354 ? 26.536  3.871   -4.559  1.00 31.12  ? 326 ASP A CB    1 
ATOM   2582 C  CG    . ASP A 1 354 ? 27.298  2.918   -5.477  1.00 35.57  ? 326 ASP A CG    1 
ATOM   2583 O  OD1   . ASP A 1 354 ? 27.052  1.698   -5.429  1.00 34.89  ? 326 ASP A OD1   1 
ATOM   2584 O  OD2   . ASP A 1 354 ? 28.134  3.397   -6.265  1.00 31.63  ? 326 ASP A OD2   1 
ATOM   2585 N  N     . ASN A 1 355 ? 27.237  1.553   -1.882  1.00 38.86  ? 327 ASN A N     1 
ATOM   2586 C  CA    . ASN A 1 355 ? 28.368  0.884   -1.251  1.00 38.65  ? 327 ASN A CA    1 
ATOM   2587 C  C     . ASN A 1 355 ? 28.247  -0.600  -1.566  1.00 44.06  ? 327 ASN A C     1 
ATOM   2588 O  O     . ASN A 1 355 ? 27.359  -1.020  -2.311  1.00 37.00  ? 327 ASN A O     1 
ATOM   2589 C  CB    . ASN A 1 355 ? 28.438  1.142   0.263   1.00 42.71  ? 327 ASN A CB    1 
ATOM   2590 C  CG    . ASN A 1 355 ? 27.153  0.773   0.999   1.00 45.80  ? 327 ASN A CG    1 
ATOM   2591 O  OD1   . ASN A 1 355 ? 26.376  -0.066  0.544   1.00 46.21  ? 327 ASN A OD1   1 
ATOM   2592 N  ND2   . ASN A 1 355 ? 26.927  1.414   2.155   1.00 40.05  ? 327 ASN A ND2   1 
ATOM   2593 N  N     . GLU A 1 356 ? 29.142  -1.404  -0.986  1.00 50.77  ? 328 GLU A N     1 
ATOM   2594 C  CA    . GLU A 1 356 ? 29.217  -2.814  -1.361  1.00 50.20  ? 328 GLU A CA    1 
ATOM   2595 C  C     . GLU A 1 356 ? 27.946  -3.549  -0.974  1.00 45.71  ? 328 GLU A C     1 
ATOM   2596 O  O     . GLU A 1 356 ? 27.495  -4.454  -1.686  1.00 52.27  ? 328 GLU A O     1 
ATOM   2597 C  CB    . GLU A 1 356 ? 30.437  -3.456  -0.694  1.00 59.58  ? 328 GLU A CB    1 
ATOM   2598 C  CG    . GLU A 1 356 ? 31.030  -4.676  -1.401  1.00 59.43  ? 328 GLU A CG    1 
ATOM   2599 C  CD    . GLU A 1 356 ? 32.366  -5.088  -0.782  1.00 62.51  ? 328 GLU A CD    1 
ATOM   2600 O  OE1   . GLU A 1 356 ? 32.545  -4.837  0.436   1.00 59.36  ? 328 GLU A OE1   1 
ATOM   2601 O  OE2   . GLU A 1 356 ? 33.228  -5.652  -1.506  1.00 59.91  ? 328 GLU A OE2   1 
ATOM   2602 N  N     . MET A 1 357 ? 27.337  -3.135  0.127   1.00 47.99  ? 329 MET A N     1 
ATOM   2603 C  CA    . MET A 1 357 ? 26.179  -3.828  0.666   1.00 47.80  ? 329 MET A CA    1 
ATOM   2604 C  C     . MET A 1 357 ? 24.959  -3.641  -0.224  1.00 56.31  ? 329 MET A C     1 
ATOM   2605 O  O     . MET A 1 357 ? 24.181  -4.581  -0.434  1.00 55.37  ? 329 MET A O     1 
ATOM   2606 C  CB    . MET A 1 357 ? 25.919  -3.287  2.059   1.00 45.69  ? 329 MET A CB    1 
ATOM   2607 C  CG    . MET A 1 357 ? 24.631  -3.692  2.714   1.00 49.56  ? 329 MET A CG    1 
ATOM   2608 S  SD    . MET A 1 357 ? 24.964  -3.503  4.484   1.00 59.10  ? 329 MET A SD    1 
ATOM   2609 C  CE    . MET A 1 357 ? 26.467  -2.516  4.439   1.00 51.57  ? 329 MET A CE    1 
ATOM   2610 N  N     . THR A 1 358 ? 24.769  -2.429  -0.745  1.00 50.52  ? 330 THR A N     1 
ATOM   2611 C  CA    . THR A 1 358 ? 23.615  -2.145  -1.585  1.00 51.34  ? 330 THR A CA    1 
ATOM   2612 C  C     . THR A 1 358 ? 23.842  -2.516  -3.047  1.00 53.63  ? 330 THR A C     1 
ATOM   2613 O  O     . THR A 1 358 ? 22.900  -2.415  -3.839  1.00 44.18  ? 330 THR A O     1 
ATOM   2614 C  CB    . THR A 1 358 ? 23.248  -0.659  -1.484  1.00 47.60  ? 330 THR A CB    1 
ATOM   2615 O  OG1   . THR A 1 358 ? 24.262  0.122   -2.134  1.00 48.32  ? 330 THR A OG1   1 
ATOM   2616 C  CG2   . THR A 1 358 ? 23.144  -0.212  -0.027  1.00 42.37  ? 330 THR A CG2   1 
ATOM   2617 N  N     . ARG A 1 359 ? 25.059  -2.933  -3.426  1.00 48.19  ? 331 ARG A N     1 
ATOM   2618 C  CA    . ARG A 1 359 ? 25.343  -3.331  -4.809  1.00 50.64  ? 331 ARG A CA    1 
ATOM   2619 C  C     . ARG A 1 359 ? 24.945  -4.793  -5.004  1.00 55.12  ? 331 ARG A C     1 
ATOM   2620 O  O     . ARG A 1 359 ? 25.774  -5.706  -5.011  1.00 64.78  ? 331 ARG A O     1 
ATOM   2621 C  CB    . ARG A 1 359 ? 26.810  -3.099  -5.156  1.00 47.27  ? 331 ARG A CB    1 
ATOM   2622 C  CG    . ARG A 1 359 ? 27.203  -1.625  -5.311  1.00 47.73  ? 331 ARG A CG    1 
ATOM   2623 C  CD    . ARG A 1 359 ? 28.696  -1.446  -5.679  1.00 44.37  ? 331 ARG A CD    1 
ATOM   2624 N  NE    . ARG A 1 359 ? 29.159  -0.086  -5.413  1.00 40.47  ? 331 ARG A NE    1 
ATOM   2625 C  CZ    . ARG A 1 359 ? 30.185  0.228   -4.627  1.00 48.70  ? 331 ARG A CZ    1 
ATOM   2626 N  NH1   . ARG A 1 359 ? 30.979  -0.700  -4.119  1.00 40.21  ? 331 ARG A NH1   1 
ATOM   2627 N  NH2   . ARG A 1 359 ? 30.429  1.510   -4.357  1.00 39.06  ? 331 ARG A NH2   1 
ATOM   2628 N  N     . LYS A 1 360 ? 23.643  -5.011  -5.190  1.00 68.61  ? 332 LYS A N     1 
ATOM   2629 C  CA    . LYS A 1 360 ? 23.061  -6.344  -5.273  1.00 62.24  ? 332 LYS A CA    1 
ATOM   2630 C  C     . LYS A 1 360 ? 22.392  -6.559  -6.627  1.00 63.75  ? 332 LYS A C     1 
ATOM   2631 O  O     . LYS A 1 360 ? 22.015  -5.609  -7.324  1.00 66.31  ? 332 LYS A O     1 
ATOM   2632 C  CB    . LYS A 1 360 ? 22.049  -6.576  -4.142  1.00 55.51  ? 332 LYS A CB    1 
ATOM   2633 C  CG    . LYS A 1 360 ? 22.694  -6.676  -2.762  1.00 58.66  ? 332 LYS A CG    1 
ATOM   2634 C  CD    . LYS A 1 360 ? 23.810  -7.713  -2.754  1.00 56.10  ? 332 LYS A CD    1 
ATOM   2635 C  CE    . LYS A 1 360 ? 24.715  -7.553  -1.539  1.00 56.71  ? 332 LYS A CE    1 
ATOM   2636 N  NZ    . LYS A 1 360 ? 26.139  -7.871  -1.890  1.00 59.02  ? 332 LYS A NZ    1 
ATOM   2637 N  N     . SER A 1 361 ? 22.253  -7.835  -6.994  1.00 69.12  ? 333 SER A N     1 
ATOM   2638 C  CA    . SER A 1 361 ? 21.634  -8.256  -8.251  1.00 72.31  ? 333 SER A CA    1 
ATOM   2639 C  C     . SER A 1 361 ? 20.290  -8.905  -7.951  1.00 74.90  ? 333 SER A C     1 
ATOM   2640 O  O     . SER A 1 361 ? 20.238  -9.953  -7.296  1.00 74.70  ? 333 SER A O     1 
ATOM   2641 C  CB    . SER A 1 361 ? 22.528  -9.235  -9.015  1.00 62.51  ? 333 SER A CB    1 
ATOM   2642 O  OG    . SER A 1 361 ? 23.613  -8.564  -9.625  1.00 63.62  ? 333 SER A OG    1 
ATOM   2643 N  N     . SER A 1 362 ? 19.215  -8.289  -8.438  1.00 84.11  ? 334 SER A N     1 
ATOM   2644 C  CA    . SER A 1 362 ? 17.854  -8.777  -8.210  1.00 74.82  ? 334 SER A CA    1 
ATOM   2645 C  C     . SER A 1 362 ? 17.588  -9.082  -6.735  1.00 73.89  ? 334 SER A C     1 
ATOM   2646 O  O     . SER A 1 362 ? 18.263  -8.563  -5.838  1.00 77.34  ? 334 SER A O     1 
ATOM   2647 C  CB    . SER A 1 362 ? 17.583  -10.024 -9.060  1.00 70.42  ? 334 SER A CB    1 
ATOM   2648 O  OG    . SER A 1 362 ? 16.254  -10.480 -8.871  1.00 84.03  ? 334 SER A OG    1 
ATOM   2649 N  N     . GLY A 1 364 ? 14.545  -9.077  -6.930  1.00 75.90  ? 336 GLY A N     1 
ATOM   2650 C  CA    . GLY A 1 364 ? 13.410  -9.362  -7.790  1.00 64.64  ? 336 GLY A CA    1 
ATOM   2651 C  C     . GLY A 1 364 ? 12.758  -10.691 -7.467  1.00 66.26  ? 336 GLY A C     1 
ATOM   2652 O  O     . GLY A 1 364 ? 12.659  -11.088 -6.304  1.00 64.30  ? 336 GLY A O     1 
ATOM   2653 N  N     . LEU A 1 365 ? 12.297  -11.393 -8.500  1.00 63.80  ? 337 LEU A N     1 
ATOM   2654 C  CA    . LEU A 1 365 ? 11.720  -12.709 -8.264  1.00 69.33  ? 337 LEU A CA    1 
ATOM   2655 C  C     . LEU A 1 365 ? 12.783  -13.742 -7.907  1.00 69.13  ? 337 LEU A C     1 
ATOM   2656 O  O     . LEU A 1 365 ? 12.439  -14.790 -7.349  1.00 55.92  ? 337 LEU A O     1 
ATOM   2657 C  CB    . LEU A 1 365 ? 10.906  -13.164 -9.486  1.00 71.43  ? 337 LEU A CB    1 
ATOM   2658 C  CG    . LEU A 1 365 ? 11.526  -13.148 -10.888 1.00 76.65  ? 337 LEU A CG    1 
ATOM   2659 C  CD1   . LEU A 1 365 ? 12.400  -14.375 -11.141 1.00 83.05  ? 337 LEU A CD1   1 
ATOM   2660 C  CD2   . LEU A 1 365 ? 10.448  -13.032 -11.958 1.00 69.62  ? 337 LEU A CD2   1 
ATOM   2661 N  N     . GLU A 1 366 ? 14.062  -13.469 -8.216  1.00 69.55  ? 338 GLU A N     1 
ATOM   2662 C  CA    . GLU A 1 366 ? 15.131  -14.387 -7.830  1.00 71.34  ? 338 GLU A CA    1 
ATOM   2663 C  C     . GLU A 1 366 ? 15.260  -14.467 -6.311  1.00 58.48  ? 338 GLU A C     1 
ATOM   2664 O  O     . GLU A 1 366 ? 15.459  -15.553 -5.756  1.00 56.16  ? 338 GLU A O     1 
ATOM   2665 C  CB    . GLU A 1 366 ? 16.469  -13.962 -8.452  1.00 68.97  ? 338 GLU A CB    1 
ATOM   2666 C  CG    . GLU A 1 366 ? 17.621  -14.954 -8.172  1.00 75.14  ? 338 GLU A CG    1 
ATOM   2667 C  CD    . GLU A 1 366 ? 18.969  -14.565 -8.812  1.00 77.93  ? 338 GLU A CD    1 
ATOM   2668 O  OE1   . GLU A 1 366 ? 19.236  -14.996 -9.957  1.00 77.80  ? 338 GLU A OE1   1 
ATOM   2669 O  OE2   . GLU A 1 366 ? 19.788  -13.882 -8.150  1.00 73.35  ? 338 GLU A OE2   1 
ATOM   2670 N  N     . ILE A 1 367 ? 15.144  -13.332 -5.620  1.00 52.40  ? 339 ILE A N     1 
ATOM   2671 C  CA    . ILE A 1 367 ? 15.191  -13.371 -4.161  1.00 58.33  ? 339 ILE A CA    1 
ATOM   2672 C  C     . ILE A 1 367 ? 14.022  -14.182 -3.620  1.00 51.58  ? 339 ILE A C     1 
ATOM   2673 O  O     . ILE A 1 367 ? 14.184  -15.003 -2.710  1.00 43.21  ? 339 ILE A O     1 
ATOM   2674 C  CB    . ILE A 1 367 ? 15.211  -11.947 -3.573  1.00 52.88  ? 339 ILE A CB    1 
ATOM   2675 C  CG1   . ILE A 1 367 ? 16.086  -11.030 -4.423  1.00 61.07  ? 339 ILE A CG1   1 
ATOM   2676 C  CG2   . ILE A 1 367 ? 15.706  -11.980 -2.139  1.00 50.00  ? 339 ILE A CG2   1 
ATOM   2677 C  CD1   . ILE A 1 367 ? 17.566  -11.254 -4.220  1.00 63.63  ? 339 ILE A CD1   1 
ATOM   2678 N  N     . ALA A 1 368 ? 12.830  -13.986 -4.186  1.00 56.01  ? 340 ALA A N     1 
ATOM   2679 C  CA    . ALA A 1 368 ? 11.658  -14.703 -3.696  1.00 46.35  ? 340 ALA A CA    1 
ATOM   2680 C  C     . ALA A 1 368 ? 11.843  -16.205 -3.835  1.00 47.17  ? 340 ALA A C     1 
ATOM   2681 O  O     . ALA A 1 368 ? 11.574  -16.962 -2.893  1.00 42.72  ? 340 ALA A O     1 
ATOM   2682 C  CB    . ALA A 1 368 ? 10.409  -14.249 -4.447  1.00 46.03  ? 340 ALA A CB    1 
ATOM   2683 N  N     . ARG A 1 369 ? 12.313  -16.649 -5.011  1.00 51.84  ? 341 ARG A N     1 
ATOM   2684 C  CA    . ARG A 1 369 ? 12.474  -18.077 -5.287  1.00 51.30  ? 341 ARG A CA    1 
ATOM   2685 C  C     . ARG A 1 369 ? 13.583  -18.694 -4.441  1.00 47.31  ? 341 ARG A C     1 
ATOM   2686 O  O     . ARG A 1 369 ? 13.479  -19.858 -4.031  1.00 41.42  ? 341 ARG A O     1 
ATOM   2687 C  CB    . ARG A 1 369 ? 12.771  -18.287 -6.773  1.00 56.79  ? 341 ARG A CB    1 
ATOM   2688 C  CG    . ARG A 1 369 ? 12.980  -19.737 -7.177  1.00 58.01  ? 341 ARG A CG    1 
ATOM   2689 C  CD    . ARG A 1 369 ? 13.014  -19.894 -8.701  1.00 70.28  ? 341 ARG A CD    1 
ATOM   2690 N  NE    . ARG A 1 369 ? 14.028  -19.043 -9.319  1.00 80.46  ? 341 ARG A NE    1 
ATOM   2691 C  CZ    . ARG A 1 369 ? 13.765  -17.973 -10.061 1.00 81.60  ? 341 ARG A CZ    1 
ATOM   2692 N  NH1   . ARG A 1 369 ? 12.522  -17.605 -10.330 1.00 80.72  ? 341 ARG A NH1   1 
ATOM   2693 N  NH2   . ARG A 1 369 ? 14.774  -17.254 -10.546 1.00 80.05  ? 341 ARG A NH2   1 
ATOM   2694 N  N     . ASN A 1 370 ? 14.665  -17.937 -4.203  1.00 35.53  ? 342 ASN A N     1 
ATOM   2695 C  CA    . ASN A 1 370 ? 15.740  -18.398 -3.326  1.00 44.51  ? 342 ASN A CA    1 
ATOM   2696 C  C     . ASN A 1 370 ? 15.226  -18.697 -1.922  1.00 38.34  ? 342 ASN A C     1 
ATOM   2697 O  O     . ASN A 1 370 ? 15.456  -19.786 -1.382  1.00 37.34  ? 342 ASN A O     1 
ATOM   2698 C  CB    . ASN A 1 370 ? 16.858  -17.347 -3.275  1.00 40.48  ? 342 ASN A CB    1 
ATOM   2699 C  CG    . ASN A 1 370 ? 17.976  -17.712 -2.290  1.00 59.00  ? 342 ASN A CG    1 
ATOM   2700 O  OD1   . ASN A 1 370 ? 18.385  -16.895 -1.447  1.00 52.73  ? 342 ASN A OD1   1 
ATOM   2701 N  ND2   . ASN A 1 370 ? 18.466  -18.948 -2.385  1.00 61.43  ? 342 ASN A ND2   1 
ATOM   2702 N  N     . ILE A 1 371 ? 14.528  -17.735 -1.311  1.00 44.17  ? 343 ILE A N     1 
ATOM   2703 C  CA    . ILE A 1 371 ? 14.017  -17.931 0.047   1.00 38.34  ? 343 ILE A CA    1 
ATOM   2704 C  C     . ILE A 1 371 ? 13.171  -19.191 0.124   1.00 36.52  ? 343 ILE A C     1 
ATOM   2705 O  O     . ILE A 1 371 ? 13.351  -20.027 1.018   1.00 34.14  ? 343 ILE A O     1 
ATOM   2706 C  CB    . ILE A 1 371 ? 13.231  -16.694 0.511   1.00 41.18  ? 343 ILE A CB    1 
ATOM   2707 C  CG1   . ILE A 1 371 ? 14.139  -15.468 0.492   1.00 35.91  ? 343 ILE A CG1   1 
ATOM   2708 C  CG2   . ILE A 1 371 ? 12.571  -16.934 1.873   1.00 30.88  ? 343 ILE A CG2   1 
ATOM   2709 C  CD1   . ILE A 1 371 ? 13.380  -14.155 0.491   1.00 44.77  ? 343 ILE A CD1   1 
ATOM   2710 N  N     . GLY A 1 372 ? 12.262  -19.368 -0.837  1.00 33.73  ? 344 GLY A N     1 
ATOM   2711 C  CA    . GLY A 1 372 ? 11.355  -20.505 -0.769  1.00 36.43  ? 344 GLY A CA    1 
ATOM   2712 C  C     . GLY A 1 372 ? 12.078  -21.828 -0.926  1.00 43.43  ? 344 GLY A C     1 
ATOM   2713 O  O     . GLY A 1 372 ? 11.817  -22.783 -0.184  1.00 37.61  ? 344 GLY A O     1 
ATOM   2714 N  N     . HIS A 1 373 ? 13.017  -21.892 -1.876  1.00 39.45  ? 345 HIS A N     1 
ATOM   2715 C  CA    . HIS A 1 373 ? 13.812  -23.098 -2.054  1.00 38.67  ? 345 HIS A CA    1 
ATOM   2716 C  C     . HIS A 1 373 ? 14.561  -23.448 -0.767  1.00 39.88  ? 345 HIS A C     1 
ATOM   2717 O  O     . HIS A 1 373 ? 14.566  -24.606 -0.334  1.00 39.52  ? 345 HIS A O     1 
ATOM   2718 C  CB    . HIS A 1 373 ? 14.783  -22.895 -3.219  1.00 41.29  ? 345 HIS A CB    1 
ATOM   2719 C  CG    . HIS A 1 373 ? 15.495  -24.139 -3.642  1.00 52.10  ? 345 HIS A CG    1 
ATOM   2720 N  ND1   . HIS A 1 373 ? 14.926  -25.074 -4.480  1.00 63.72  ? 345 HIS A ND1   1 
ATOM   2721 C  CD2   . HIS A 1 373 ? 16.723  -24.618 -3.322  1.00 63.58  ? 345 HIS A CD2   1 
ATOM   2722 C  CE1   . HIS A 1 373 ? 15.780  -26.066 -4.673  1.00 67.29  ? 345 HIS A CE1   1 
ATOM   2723 N  NE2   . HIS A 1 373 ? 16.875  -25.818 -3.976  1.00 62.83  ? 345 HIS A NE2   1 
ATOM   2724 N  N     . TYR A 1 374 ? 15.172  -22.452 -0.125  1.00 32.58  ? 346 TYR A N     1 
ATOM   2725 C  CA    . TYR A 1 374 ? 15.917  -22.713 1.104   1.00 33.17  ? 346 TYR A CA    1 
ATOM   2726 C  C     . TYR A 1 374 ? 14.992  -23.167 2.224   1.00 32.91  ? 346 TYR A C     1 
ATOM   2727 O  O     . TYR A 1 374 ? 15.301  -24.116 2.951   1.00 37.07  ? 346 TYR A O     1 
ATOM   2728 C  CB    . TYR A 1 374 ? 16.689  -21.457 1.517   1.00 31.68  ? 346 TYR A CB    1 
ATOM   2729 C  CG    . TYR A 1 374 ? 17.455  -21.589 2.808   1.00 27.57  ? 346 TYR A CG    1 
ATOM   2730 C  CD1   . TYR A 1 374 ? 16.860  -21.293 4.026   1.00 29.58  ? 346 TYR A CD1   1 
ATOM   2731 C  CD2   . TYR A 1 374 ? 18.796  -21.992 2.806   1.00 36.09  ? 346 TYR A CD2   1 
ATOM   2732 C  CE1   . TYR A 1 374 ? 17.563  -21.398 5.209   1.00 28.90  ? 346 TYR A CE1   1 
ATOM   2733 C  CE2   . TYR A 1 374 ? 19.512  -22.115 3.994   1.00 30.98  ? 346 TYR A CE2   1 
ATOM   2734 C  CZ    . TYR A 1 374 ? 18.887  -21.823 5.192   1.00 31.94  ? 346 TYR A CZ    1 
ATOM   2735 O  OH    . TYR A 1 374 ? 19.585  -21.920 6.377   1.00 27.19  ? 346 TYR A OH    1 
ATOM   2736 N  N     . LEU A 1 375 ? 13.866  -22.474 2.408   1.00 32.88  ? 347 LEU A N     1 
ATOM   2737 C  CA    . LEU A 1 375 ? 12.997  -22.803 3.535   1.00 38.67  ? 347 LEU A CA    1 
ATOM   2738 C  C     . LEU A 1 375 ? 12.293  -24.139 3.321   1.00 38.42  ? 347 LEU A C     1 
ATOM   2739 O  O     . LEU A 1 375 ? 11.998  -24.843 4.291   1.00 39.67  ? 347 LEU A O     1 
ATOM   2740 C  CB    . LEU A 1 375 ? 11.992  -21.672 3.762   1.00 37.69  ? 347 LEU A CB    1 
ATOM   2741 C  CG    . LEU A 1 375 ? 12.571  -20.330 4.220   1.00 27.23  ? 347 LEU A CG    1 
ATOM   2742 C  CD1   . LEU A 1 375 ? 11.465  -19.296 4.343   1.00 32.53  ? 347 LEU A CD1   1 
ATOM   2743 C  CD2   . LEU A 1 375 ? 13.254  -20.500 5.553   1.00 29.13  ? 347 LEU A CD2   1 
ATOM   2744 N  N     . GLU A 1 376 ? 12.057  -24.519 2.063   1.00 36.46  ? 348 GLU A N     1 
ATOM   2745 C  CA    . GLU A 1 376 ? 11.489  -25.831 1.775   1.00 46.25  ? 348 GLU A CA    1 
ATOM   2746 C  C     . GLU A 1 376 ? 12.349  -26.969 2.324   1.00 49.97  ? 348 GLU A C     1 
ATOM   2747 O  O     . GLU A 1 376 ? 11.818  -28.029 2.678   1.00 56.06  ? 348 GLU A O     1 
ATOM   2748 C  CB    . GLU A 1 376 ? 11.314  -25.986 0.266   1.00 47.61  ? 348 GLU A CB    1 
ATOM   2749 C  CG    . GLU A 1 376 ? 10.637  -27.277 -0.169  1.00 58.92  ? 348 GLU A CG    1 
ATOM   2750 C  CD    . GLU A 1 376 ? 9.206   -27.384 0.316   1.00 60.75  ? 348 GLU A CD    1 
ATOM   2751 O  OE1   . GLU A 1 376 ? 8.567   -26.328 0.508   1.00 64.08  ? 348 GLU A OE1   1 
ATOM   2752 O  OE2   . GLU A 1 376 ? 8.720   -28.523 0.517   1.00 65.98  ? 348 GLU A OE2   1 
ATOM   2753 N  N     . ARG A 1 377 ? 13.670  -26.779 2.411   1.00 46.87  ? 349 ARG A N     1 
ATOM   2754 C  CA    . ARG A 1 377 ? 14.592  -27.862 2.742   1.00 48.57  ? 349 ARG A CA    1 
ATOM   2755 C  C     . ARG A 1 377 ? 15.125  -27.803 4.170   1.00 49.51  ? 349 ARG A C     1 
ATOM   2756 O  O     . ARG A 1 377 ? 16.220  -28.313 4.431   1.00 56.29  ? 349 ARG A O     1 
ATOM   2757 C  CB    . ARG A 1 377 ? 15.757  -27.881 1.756   1.00 50.05  ? 349 ARG A CB    1 
ATOM   2758 C  CG    . ARG A 1 377 ? 15.428  -28.616 0.483   1.00 61.31  ? 349 ARG A CG    1 
ATOM   2759 C  CD    . ARG A 1 377 ? 15.930  -27.887 -0.744  1.00 66.94  ? 349 ARG A CD    1 
ATOM   2760 N  NE    . ARG A 1 377 ? 15.218  -28.348 -1.928  1.00 70.35  ? 349 ARG A NE    1 
ATOM   2761 C  CZ    . ARG A 1 377 ? 14.101  -27.796 -2.383  1.00 69.22  ? 349 ARG A CZ    1 
ATOM   2762 N  NH1   . ARG A 1 377 ? 13.563  -26.740 -1.792  1.00 60.16  ? 349 ARG A NH1   1 
ATOM   2763 N  NH2   . ARG A 1 377 ? 13.507  -28.316 -3.455  1.00 69.26  ? 349 ARG A NH2   1 
ATOM   2764 N  N     . VAL A 1 378 ? 14.385  -27.207 5.101   1.00 52.64  ? 350 VAL A N     1 
ATOM   2765 C  CA    . VAL A 1 378 ? 14.793  -27.187 6.514   1.00 56.36  ? 350 VAL A CA    1 
ATOM   2766 C  C     . VAL A 1 378 ? 13.606  -27.438 7.451   1.00 65.53  ? 350 VAL A C     1 
ATOM   2767 O  O     . VAL A 1 378 ? 13.720  -28.234 8.392   1.00 76.97  ? 350 VAL A O     1 
ATOM   2768 C  CB    . VAL A 1 378 ? 15.482  -25.857 6.902   1.00 50.95  ? 350 VAL A CB    1 
ATOM   2769 C  CG1   . VAL A 1 378 ? 16.769  -25.644 6.104   1.00 47.74  ? 350 VAL A CG1   1 
ATOM   2770 C  CG2   . VAL A 1 378 ? 14.526  -24.663 6.757   1.00 42.89  ? 350 VAL A CG2   1 
HETATM 2771 N  N1    . FAD B 2 .   ? 21.272  8.619   46.803  1.00 35.67  ? 401 FAD A N1    1 
HETATM 2772 C  C2    . FAD B 2 .   ? 20.865  9.855   47.254  1.00 39.03  ? 401 FAD A C2    1 
HETATM 2773 O  O2    . FAD B 2 .   ? 21.685  10.759  47.397  1.00 37.49  ? 401 FAD A O2    1 
HETATM 2774 N  N3    . FAD B 2 .   ? 19.525  10.094  47.532  1.00 36.26  ? 401 FAD A N3    1 
HETATM 2775 C  C4    . FAD B 2 .   ? 18.582  9.097   47.354  1.00 38.24  ? 401 FAD A C4    1 
HETATM 2776 O  O4    . FAD B 2 .   ? 17.386  9.289   47.606  1.00 32.55  ? 401 FAD A O4    1 
HETATM 2777 C  C4X   . FAD B 2 .   ? 18.997  7.857   46.907  1.00 35.99  ? 401 FAD A C4X   1 
HETATM 2778 N  N5    . FAD B 2 .   ? 18.056  6.876   46.734  1.00 35.35  ? 401 FAD A N5    1 
HETATM 2779 C  C5X   . FAD B 2 .   ? 18.456  5.635   46.286  1.00 37.72  ? 401 FAD A C5X   1 
HETATM 2780 C  C6    . FAD B 2 .   ? 17.517  4.641   46.106  1.00 34.12  ? 401 FAD A C6    1 
HETATM 2781 C  C7    . FAD B 2 .   ? 17.887  3.389   45.654  1.00 35.58  ? 401 FAD A C7    1 
HETATM 2782 C  C7M   . FAD B 2 .   ? 16.831  2.334   45.481  1.00 38.53  ? 401 FAD A C7M   1 
HETATM 2783 C  C8    . FAD B 2 .   ? 19.216  3.121   45.374  1.00 36.44  ? 401 FAD A C8    1 
HETATM 2784 C  C8M   . FAD B 2 .   ? 19.624  1.764   44.883  1.00 42.42  ? 401 FAD A C8M   1 
HETATM 2785 C  C9    . FAD B 2 .   ? 20.170  4.119   45.539  1.00 35.49  ? 401 FAD A C9    1 
HETATM 2786 C  C9A   . FAD B 2 .   ? 19.789  5.379   45.993  1.00 38.39  ? 401 FAD A C9A   1 
HETATM 2787 N  N10   . FAD B 2 .   ? 20.737  6.366   46.159  1.00 40.32  ? 401 FAD A N10   1 
HETATM 2788 C  C10   . FAD B 2 .   ? 20.345  7.613   46.620  1.00 39.87  ? 401 FAD A C10   1 
HETATM 2789 C  "C1'" . FAD B 2 .   ? 22.183  6.025   45.864  1.00 42.67  ? 401 FAD A "C1'" 1 
HETATM 2790 C  "C2'" . FAD B 2 .   ? 22.751  6.611   44.584  1.00 40.39  ? 401 FAD A "C2'" 1 
HETATM 2791 O  "O2'" . FAD B 2 .   ? 22.368  5.853   43.451  1.00 44.38  ? 401 FAD A "O2'" 1 
HETATM 2792 C  "C3'" . FAD B 2 .   ? 24.292  6.654   44.670  1.00 50.93  ? 401 FAD A "C3'" 1 
HETATM 2793 O  "O3'" . FAD B 2 .   ? 24.856  5.428   45.102  1.00 50.83  ? 401 FAD A "O3'" 1 
HETATM 2794 C  "C4'" . FAD B 2 .   ? 24.769  7.730   45.625  1.00 53.32  ? 401 FAD A "C4'" 1 
HETATM 2795 O  "O4'" . FAD B 2 .   ? 23.909  8.847   45.583  1.00 50.07  ? 401 FAD A "O4'" 1 
HETATM 2796 C  "C5'" . FAD B 2 .   ? 26.175  8.145   45.207  1.00 67.94  ? 401 FAD A "C5'" 1 
HETATM 2797 O  "O5'" . FAD B 2 .   ? 26.650  9.153   46.074  1.00 80.03  ? 401 FAD A "O5'" 1 
HETATM 2798 P  P     . FAD B 2 .   ? 27.906  10.096  45.675  1.00 101.99 ? 401 FAD A P     1 
HETATM 2799 O  O1P   . FAD B 2 .   ? 27.475  11.545  45.791  1.00 86.46  ? 401 FAD A O1P   1 
HETATM 2800 O  O2P   . FAD B 2 .   ? 29.048  9.833   46.639  1.00 94.32  ? 401 FAD A O2P   1 
HETATM 2801 O  O3P   . FAD B 2 .   ? 28.338  9.810   44.245  1.00 80.22  ? 401 FAD A O3P   1 
HETATM 2802 CA CA    . CA  C 3 .   ? 13.084  13.329  -11.208 1.00 26.86  ? 402 CA  A CA    1 
HETATM 2803 CA CA    . CA  D 3 .   ? 6.359   -7.487  3.887   1.00 45.13  ? 403 CA  A CA    1 
HETATM 2804 O  O     . HOH E 4 .   ? 27.196  8.125   54.866  1.00 39.01  ? 501 HOH A O     1 
HETATM 2805 O  O     . HOH E 4 .   ? -4.694  6.387   2.730   1.00 34.79  ? 502 HOH A O     1 
HETATM 2806 O  O     . HOH E 4 .   ? 16.119  15.212  -6.147  1.00 31.65  ? 503 HOH A O     1 
HETATM 2807 O  O     . HOH E 4 .   ? 18.002  2.279   61.021  1.00 38.26  ? 504 HOH A O     1 
HETATM 2808 O  O     . HOH E 4 .   ? 29.517  3.997   0.094   1.00 44.81  ? 505 HOH A O     1 
HETATM 2809 O  O     . HOH E 4 .   ? 28.486  -8.381  -2.196  1.00 43.97  ? 506 HOH A O     1 
HETATM 2810 O  O     . HOH E 4 .   ? 22.292  -2.558  -6.188  1.00 53.80  ? 507 HOH A O     1 
HETATM 2811 O  O     . HOH E 4 .   ? 3.223   -20.971 9.339   1.00 40.84  ? 508 HOH A O     1 
HETATM 2812 O  O     . HOH E 4 .   ? 17.981  -21.304 -1.890  1.00 40.78  ? 509 HOH A O     1 
HETATM 2813 O  O     . HOH E 4 .   ? 19.895  -12.453 -6.134  1.00 52.55  ? 510 HOH A O     1 
HETATM 2814 O  O     . HOH E 4 .   ? 7.719   -10.066 50.715  1.00 44.46  ? 511 HOH A O     1 
HETATM 2815 O  O     . HOH E 4 .   ? 11.989  -5.103  -0.064  1.00 33.92  ? 512 HOH A O     1 
HETATM 2816 O  O     . HOH E 4 .   ? 13.212  9.640   -13.920 1.00 26.77  ? 513 HOH A O     1 
HETATM 2817 O  O     . HOH E 4 .   ? 25.327  -2.208  14.857  1.00 52.03  ? 514 HOH A O     1 
HETATM 2818 O  O     . HOH E 4 .   ? 21.707  8.720   58.024  1.00 27.79  ? 515 HOH A O     1 
HETATM 2819 O  O     . HOH E 4 .   ? 20.490  18.692  -4.118  1.00 50.69  ? 516 HOH A O     1 
HETATM 2820 O  O     . HOH E 4 .   ? 3.891   9.820   44.159  1.00 34.04  ? 517 HOH A O     1 
HETATM 2821 O  O     . HOH E 4 .   ? 22.184  -1.650  57.674  1.00 38.93  ? 518 HOH A O     1 
HETATM 2822 O  O     . HOH E 4 .   ? 20.901  14.917  9.685   1.00 37.40  ? 519 HOH A O     1 
HETATM 2823 O  O     . HOH E 4 .   ? 15.580  15.529  57.820  1.00 42.62  ? 520 HOH A O     1 
HETATM 2824 O  O     . HOH E 4 .   ? 4.663   -5.341  4.636   1.00 33.66  ? 521 HOH A O     1 
HETATM 2825 O  O     . HOH E 4 .   ? 15.124  -16.669 15.667  1.00 36.43  ? 522 HOH A O     1 
HETATM 2826 O  O     . HOH E 4 .   ? -5.361  11.249  1.849   1.00 34.23  ? 523 HOH A O     1 
HETATM 2827 O  O     . HOH E 4 .   ? 27.694  13.287  -0.589  1.00 26.50  ? 524 HOH A O     1 
HETATM 2828 O  O     . HOH E 4 .   ? -1.720  5.031   16.697  1.00 47.48  ? 525 HOH A O     1 
HETATM 2829 O  O     . HOH E 4 .   ? 1.291   0.044   60.539  1.00 37.16  ? 526 HOH A O     1 
HETATM 2830 O  O     . HOH E 4 .   ? 18.076  -13.614 16.619  1.00 39.02  ? 527 HOH A O     1 
HETATM 2831 O  O     . HOH E 4 .   ? -4.458  16.567  21.392  1.00 43.48  ? 528 HOH A O     1 
HETATM 2832 O  O     . HOH E 4 .   ? 24.051  -7.859  54.321  1.00 44.84  ? 529 HOH A O     1 
HETATM 2833 O  O     . HOH E 4 .   ? 27.419  11.903  51.903  1.00 52.32  ? 530 HOH A O     1 
HETATM 2834 O  O     . HOH E 4 .   ? 1.435   -11.201 23.671  1.00 47.37  ? 531 HOH A O     1 
HETATM 2835 O  O     . HOH E 4 .   ? 7.049   -9.260  2.537   1.00 33.86  ? 532 HOH A O     1 
HETATM 2836 O  O     . HOH E 4 .   ? 16.146  16.864  54.093  1.00 32.98  ? 533 HOH A O     1 
HETATM 2837 O  O     . HOH E 4 .   ? 13.688  4.986   -13.701 1.00 34.57  ? 534 HOH A O     1 
HETATM 2838 O  O     . HOH E 4 .   ? 21.063  19.045  -0.228  1.00 53.56  ? 535 HOH A O     1 
HETATM 2839 O  O     . HOH E 4 .   ? 23.665  -0.755  51.121  1.00 38.63  ? 536 HOH A O     1 
HETATM 2840 O  O     . HOH E 4 .   ? 26.932  3.223   13.469  1.00 42.90  ? 537 HOH A O     1 
HETATM 2841 O  O     . HOH E 4 .   ? 9.343   -3.289  58.298  1.00 43.10  ? 538 HOH A O     1 
HETATM 2842 O  O     . HOH E 4 .   ? 6.102   -10.337 53.523  1.00 44.54  ? 539 HOH A O     1 
HETATM 2843 O  O     . HOH E 4 .   ? 3.693   -2.451  -1.900  1.00 38.84  ? 540 HOH A O     1 
HETATM 2844 O  O     . HOH E 4 .   ? 23.821  15.916  49.207  1.00 31.94  ? 541 HOH A O     1 
HETATM 2845 O  O     . HOH E 4 .   ? 7.710   -2.174  59.643  1.00 39.92  ? 542 HOH A O     1 
HETATM 2846 O  O     . HOH E 4 .   ? 25.061  15.697  2.225   1.00 41.85  ? 543 HOH A O     1 
HETATM 2847 O  O     . HOH E 4 .   ? 16.266  4.656   -13.435 1.00 32.25  ? 544 HOH A O     1 
HETATM 2848 O  O     . HOH E 4 .   ? 2.352   7.080   14.228  1.00 42.56  ? 545 HOH A O     1 
HETATM 2849 O  O     . HOH E 4 .   ? 17.925  -20.135 14.024  1.00 34.47  ? 546 HOH A O     1 
HETATM 2850 O  O     . HOH E 4 .   ? 12.479  17.840  60.073  1.00 46.52  ? 547 HOH A O     1 
HETATM 2851 O  O     . HOH E 4 .   ? 10.517  -2.348  1.992   1.00 28.37  ? 548 HOH A O     1 
HETATM 2852 O  O     . HOH E 4 .   ? 18.035  -6.885  2.209   1.00 37.73  ? 549 HOH A O     1 
HETATM 2853 O  O     . HOH E 4 .   ? 19.944  -3.231  -7.492  1.00 43.19  ? 550 HOH A O     1 
HETATM 2854 O  O     . HOH E 4 .   ? 20.363  -9.320  -4.410  1.00 67.08  ? 551 HOH A O     1 
HETATM 2855 O  O     . HOH E 4 .   ? 20.981  -16.121 2.375   1.00 37.73  ? 552 HOH A O     1 
HETATM 2856 O  O     . HOH E 4 .   ? 25.524  -24.694 12.268  1.00 43.49  ? 553 HOH A O     1 
HETATM 2857 O  O     . HOH E 4 .   ? 16.331  5.891   55.896  1.00 32.75  ? 554 HOH A O     1 
HETATM 2858 O  O     . HOH E 4 .   ? 18.637  -7.244  -3.554  1.00 62.79  ? 555 HOH A O     1 
HETATM 2859 O  O     . HOH E 4 .   ? 19.482  0.535   21.470  1.00 38.56  ? 556 HOH A O     1 
HETATM 2860 O  O     . HOH E 4 .   ? 20.953  -2.295  61.886  1.00 55.32  ? 557 HOH A O     1 
HETATM 2861 O  O     . HOH E 4 .   ? 9.015   16.816  -7.823  1.00 43.69  ? 558 HOH A O     1 
HETATM 2862 O  O     . HOH E 4 .   ? 6.739   -8.893  41.599  1.00 60.41  ? 559 HOH A O     1 
HETATM 2863 O  O     . HOH E 4 .   ? 15.737  21.162  47.749  1.00 37.21  ? 560 HOH A O     1 
HETATM 2864 O  O     . HOH E 4 .   ? 0.707   12.466  6.524   1.00 38.23  ? 561 HOH A O     1 
HETATM 2865 O  O     . HOH E 4 .   ? 25.465  -19.614 15.153  1.00 34.53  ? 562 HOH A O     1 
HETATM 2866 O  O     . HOH E 4 .   ? 28.358  -5.539  14.317  1.00 34.32  ? 563 HOH A O     1 
HETATM 2867 O  O     . HOH E 4 .   ? 26.121  21.773  54.850  1.00 45.70  ? 564 HOH A O     1 
HETATM 2868 O  O     . HOH E 4 .   ? -3.381  -9.348  58.100  1.00 34.44  ? 565 HOH A O     1 
HETATM 2869 O  O     . HOH E 4 .   ? 2.586   -8.739  55.551  1.00 40.89  ? 566 HOH A O     1 
HETATM 2870 O  O     . HOH E 4 .   ? 8.743   -18.975 18.918  1.00 31.28  ? 567 HOH A O     1 
HETATM 2871 O  O     . HOH E 4 .   ? 5.691   12.415  41.660  1.00 43.32  ? 568 HOH A O     1 
HETATM 2872 O  O     . HOH E 4 .   ? 13.472  -12.400 4.068   1.00 27.67  ? 569 HOH A O     1 
HETATM 2873 O  O     . HOH E 4 .   ? -0.107  20.366  25.512  1.00 56.68  ? 570 HOH A O     1 
HETATM 2874 O  O     . HOH E 4 .   ? 27.960  6.891   2.211   1.00 30.06  ? 571 HOH A O     1 
HETATM 2875 O  O     . HOH E 4 .   ? 15.441  10.930  57.035  1.00 30.85  ? 572 HOH A O     1 
HETATM 2876 O  O     . HOH E 4 .   ? 10.006  2.684   58.493  1.00 36.49  ? 573 HOH A O     1 
HETATM 2877 O  O     . HOH E 4 .   ? 17.746  19.333  54.815  1.00 47.96  ? 574 HOH A O     1 
HETATM 2878 O  O     . HOH E 4 .   ? 22.479  -4.159  -9.588  1.00 66.28  ? 575 HOH A O     1 
HETATM 2879 O  O     . HOH E 4 .   ? 12.509  14.968  -6.004  1.00 29.77  ? 576 HOH A O     1 
HETATM 2880 O  O     . HOH E 4 .   ? 24.443  8.757   13.415  1.00 40.37  ? 577 HOH A O     1 
HETATM 2881 O  O     . HOH E 4 .   ? 15.646  11.492  16.112  1.00 29.95  ? 578 HOH A O     1 
HETATM 2882 O  O     . HOH E 4 .   ? 15.647  -3.285  55.631  1.00 36.17  ? 579 HOH A O     1 
HETATM 2883 O  O     . HOH E 4 .   ? 20.031  -8.196  56.385  1.00 51.10  ? 580 HOH A O     1 
HETATM 2884 O  O     . HOH E 4 .   ? 17.947  19.685  57.204  1.00 49.12  ? 581 HOH A O     1 
HETATM 2885 O  O     . HOH E 4 .   ? 4.273   12.673  35.012  1.00 49.34  ? 582 HOH A O     1 
HETATM 2886 O  O     . HOH E 4 .   ? -0.676  13.153  9.882   1.00 44.19  ? 583 HOH A O     1 
HETATM 2887 O  O     . HOH E 4 .   ? 14.037  -7.152  52.747  1.00 37.88  ? 584 HOH A O     1 
HETATM 2888 O  O     . HOH E 4 .   ? 21.390  -6.744  4.631   1.00 24.91  ? 585 HOH A O     1 
HETATM 2889 O  O     . HOH E 4 .   ? 5.521   -5.139  61.478  1.00 37.06  ? 586 HOH A O     1 
HETATM 2890 O  O     . HOH E 4 .   ? 18.157  -5.526  33.541  1.00 61.05  ? 587 HOH A O     1 
HETATM 2891 O  O     . HOH E 4 .   ? 22.565  16.053  0.907   1.00 41.28  ? 588 HOH A O     1 
HETATM 2892 O  O     . HOH E 4 .   ? 9.606   12.765  1.231   1.00 24.73  ? 589 HOH A O     1 
HETATM 2893 O  O     . HOH E 4 .   ? 23.628  -9.543  13.694  1.00 30.06  ? 590 HOH A O     1 
HETATM 2894 O  O     . HOH E 4 .   ? 28.394  3.742   2.560   1.00 42.51  ? 591 HOH A O     1 
HETATM 2895 O  O     . HOH E 4 .   ? 10.547  3.217   -10.845 1.00 40.80  ? 592 HOH A O     1 
HETATM 2896 O  O     . HOH E 4 .   ? 2.712   -6.316  13.497  1.00 32.21  ? 593 HOH A O     1 
HETATM 2897 O  O     . HOH E 4 .   ? 20.277  11.086  58.184  1.00 38.48  ? 594 HOH A O     1 
HETATM 2898 O  O     . HOH E 4 .   ? 23.012  15.381  46.384  1.00 41.94  ? 595 HOH A O     1 
HETATM 2899 O  O     . HOH E 4 .   ? 13.682  17.604  57.094  1.00 38.72  ? 596 HOH A O     1 
HETATM 2900 O  O     . HOH E 4 .   ? -0.239  -12.233 52.670  1.00 44.06  ? 597 HOH A O     1 
HETATM 2901 O  O     . HOH E 4 .   ? 24.506  4.730   57.344  1.00 41.86  ? 598 HOH A O     1 
HETATM 2902 O  O     . HOH E 4 .   ? 18.364  -3.218  61.576  1.00 50.90  ? 599 HOH A O     1 
HETATM 2903 O  O     . HOH E 4 .   ? 18.959  -0.505  -8.666  1.00 54.97  ? 600 HOH A O     1 
HETATM 2904 O  O     . HOH E 4 .   ? 31.765  -3.387  -4.293  1.00 51.42  ? 601 HOH A O     1 
HETATM 2905 O  O     . HOH E 4 .   ? 16.288  11.574  19.802  1.00 48.57  ? 602 HOH A O     1 
HETATM 2906 O  O     . HOH E 4 .   ? 2.175   -6.233  56.944  1.00 34.29  ? 603 HOH A O     1 
HETATM 2907 O  O     . HOH E 4 .   ? 2.587   -5.550  6.679   1.00 29.09  ? 604 HOH A O     1 
HETATM 2908 O  O     . HOH E 4 .   ? 13.704  -14.685 18.159  1.00 34.41  ? 605 HOH A O     1 
HETATM 2909 O  O     . HOH E 4 .   ? 11.799  14.618  -9.729  1.00 25.71  ? 606 HOH A O     1 
HETATM 2910 O  O     . HOH E 4 .   ? 18.008  10.793  15.862  1.00 34.36  ? 607 HOH A O     1 
HETATM 2911 O  O     . HOH E 4 .   ? 7.052   -13.517 -2.166  1.00 51.44  ? 608 HOH A O     1 
HETATM 2912 O  O     . HOH E 4 .   ? 15.142  18.434  2.067   1.00 45.82  ? 609 HOH A O     1 
HETATM 2913 O  O     . HOH E 4 .   ? 17.400  23.042  47.417  1.00 49.57  ? 610 HOH A O     1 
HETATM 2914 O  O     . HOH E 4 .   ? 13.496  7.111   34.091  1.00 51.52  ? 611 HOH A O     1 
HETATM 2915 O  O     . HOH E 4 .   ? 23.727  -12.906 3.093   1.00 29.16  ? 612 HOH A O     1 
HETATM 2916 O  O     . HOH E 4 .   ? 2.888   -2.086  17.137  1.00 37.86  ? 613 HOH A O     1 
HETATM 2917 O  O     . HOH E 4 .   ? 29.083  9.742   56.639  1.00 32.69  ? 614 HOH A O     1 
HETATM 2918 O  O     . HOH E 4 .   ? 24.290  1.007   -5.072  1.00 42.92  ? 615 HOH A O     1 
HETATM 2919 O  O     . HOH E 4 .   ? 26.841  11.234  -4.104  1.00 33.98  ? 616 HOH A O     1 
HETATM 2920 O  O     . HOH E 4 .   ? 17.838  -10.516 16.716  1.00 40.87  ? 617 HOH A O     1 
HETATM 2921 O  O     . HOH E 4 .   ? 1.414   22.859  14.868  1.00 41.12  ? 618 HOH A O     1 
HETATM 2922 O  O     . HOH E 4 .   ? 23.236  14.841  56.690  1.00 26.13  ? 619 HOH A O     1 
HETATM 2923 O  O     . HOH E 4 .   ? 2.112   13.671  -12.605 1.00 51.42  ? 620 HOH A O     1 
HETATM 2924 O  O     . HOH E 4 .   ? 17.356  15.849  8.479   1.00 46.89  ? 621 HOH A O     1 
HETATM 2925 O  O     . HOH E 4 .   ? 11.174  14.072  -1.792  1.00 31.34  ? 622 HOH A O     1 
HETATM 2926 O  O     . HOH E 4 .   ? 27.535  -6.587  7.332   1.00 29.95  ? 623 HOH A O     1 
HETATM 2927 O  O     . HOH E 4 .   ? 15.936  6.891   20.838  1.00 39.90  ? 624 HOH A O     1 
HETATM 2928 O  O     . HOH E 4 .   ? 2.654   -24.535 12.390  1.00 41.55  ? 625 HOH A O     1 
HETATM 2929 O  O     . HOH E 4 .   ? 30.033  -12.422 8.119   1.00 36.16  ? 626 HOH A O     1 
HETATM 2930 O  O     . HOH E 4 .   ? 27.076  0.058   8.795   1.00 40.66  ? 627 HOH A O     1 
HETATM 2931 O  O     . HOH E 4 .   ? 12.070  -0.564  57.522  1.00 39.47  ? 628 HOH A O     1 
HETATM 2932 O  O     . HOH E 4 .   ? -0.391  -5.911  63.532  1.00 39.46  ? 629 HOH A O     1 
HETATM 2933 O  O     . HOH E 4 .   ? 26.504  6.260   14.555  1.00 41.21  ? 630 HOH A O     1 
HETATM 2934 O  O     . HOH E 4 .   ? 21.922  -26.605 12.925  1.00 45.14  ? 631 HOH A O     1 
HETATM 2935 O  O     . HOH E 4 .   ? 5.302   -7.094  1.011   1.00 38.13  ? 632 HOH A O     1 
HETATM 2936 O  O     . HOH E 4 .   ? 18.753  -7.272  4.224   1.00 25.18  ? 633 HOH A O     1 
HETATM 2937 O  O     . HOH E 4 .   ? 15.335  -4.717  20.593  1.00 39.48  ? 634 HOH A O     1 
HETATM 2938 O  O     . HOH E 4 .   ? 22.542  -1.562  18.513  1.00 47.29  ? 635 HOH A O     1 
HETATM 2939 O  O     . HOH E 4 .   ? 1.333   -9.815  51.999  1.00 38.27  ? 636 HOH A O     1 
HETATM 2940 O  O     . HOH E 4 .   ? 13.021  -19.739 13.431  1.00 42.45  ? 637 HOH A O     1 
HETATM 2941 O  O     . HOH E 4 .   ? 8.417   -9.210  -0.871  1.00 41.42  ? 638 HOH A O     1 
HETATM 2942 O  O     . HOH E 4 .   ? 22.244  -5.622  15.550  1.00 43.71  ? 639 HOH A O     1 
HETATM 2943 O  O     . HOH E 4 .   ? 9.637   -0.350  3.199   1.00 33.71  ? 640 HOH A O     1 
HETATM 2944 O  O     . HOH E 4 .   ? -0.097  -6.663  12.494  1.00 20.43  ? 641 HOH A O     1 
HETATM 2945 O  O     . HOH E 4 .   ? 7.539   13.859  56.627  1.00 36.15  ? 642 HOH A O     1 
HETATM 2946 O  O     . HOH E 4 .   ? -4.951  -11.886 58.597  1.00 38.37  ? 643 HOH A O     1 
HETATM 2947 O  O     . HOH E 4 .   ? 1.817   10.687  -9.510  1.00 49.39  ? 644 HOH A O     1 
HETATM 2948 O  O     . HOH E 4 .   ? -2.308  -2.611  61.267  1.00 31.49  ? 645 HOH A O     1 
HETATM 2949 O  O     . HOH E 4 .   ? 6.255   2.817   -5.751  1.00 41.45  ? 646 HOH A O     1 
HETATM 2950 O  O     . HOH E 4 .   ? 15.032  12.893  59.099  1.00 29.01  ? 647 HOH A O     1 
HETATM 2951 O  O     . HOH E 4 .   ? 14.197  15.429  -11.298 1.00 31.54  ? 648 HOH A O     1 
HETATM 2952 O  O     . HOH E 4 .   ? 9.031   -8.780  42.063  1.00 60.80  ? 649 HOH A O     1 
HETATM 2953 O  O     . HOH E 4 .   ? 24.929  9.665   11.112  1.00 41.67  ? 650 HOH A O     1 
HETATM 2954 O  O     . HOH E 4 .   ? -12.143 10.999  20.652  1.00 51.33  ? 651 HOH A O     1 
HETATM 2955 O  O     . HOH E 4 .   ? 19.908  26.621  46.940  1.00 59.47  ? 652 HOH A O     1 
HETATM 2956 O  O     . HOH E 4 .   ? 17.102  24.468  48.758  1.00 50.14  ? 653 HOH A O     1 
HETATM 2957 O  O     . HOH E 4 .   ? 28.776  18.290  56.029  1.00 36.05  ? 654 HOH A O     1 
HETATM 2958 O  O     . HOH E 4 .   ? 11.971  -14.999 20.004  1.00 50.17  ? 655 HOH A O     1 
HETATM 2959 O  O     . HOH E 4 .   ? 17.590  13.152  -11.553 1.00 45.35  ? 656 HOH A O     1 
HETATM 2960 O  O     . HOH E 4 .   ? 19.148  12.490  59.134  1.00 40.05  ? 657 HOH A O     1 
HETATM 2961 O  O     . HOH E 4 .   ? 0.417   -10.760 45.114  1.00 48.48  ? 658 HOH A O     1 
HETATM 2962 O  O     . HOH E 4 .   ? 0.739   11.072  2.838   1.00 51.63  ? 659 HOH A O     1 
HETATM 2963 O  O     . HOH E 4 .   ? 20.046  2.710   22.610  1.00 40.09  ? 660 HOH A O     1 
HETATM 2964 O  O     . HOH E 4 .   ? 8.037   0.886   -7.673  1.00 55.34  ? 661 HOH A O     1 
HETATM 2965 O  O     . HOH E 4 .   ? -0.930  -3.459  63.146  1.00 49.08  ? 662 HOH A O     1 
HETATM 2966 O  O     . HOH E 4 .   ? 1.825   -10.977 46.929  1.00 52.00  ? 663 HOH A O     1 
HETATM 2967 O  O     . HOH E 4 .   ? 15.983  -2.497  21.769  1.00 45.18  ? 664 HOH A O     1 
HETATM 2968 O  O     . HOH E 4 .   ? 14.473  -12.518 19.218  1.00 41.43  ? 665 HOH A O     1 
HETATM 2969 O  O     . HOH E 4 .   ? 5.535   14.731  58.366  1.00 45.60  ? 666 HOH A O     1 
HETATM 2970 O  O     . HOH E 4 .   ? 25.812  14.961  57.055  1.00 33.91  ? 667 HOH A O     1 
HETATM 2971 O  O     . HOH E 4 .   ? 24.292  18.496  48.546  1.00 41.99  ? 668 HOH A O     1 
HETATM 2972 O  O     . HOH E 4 .   ? 7.744   12.689  -0.843  1.00 44.18  ? 669 HOH A O     1 
HETATM 2973 O  O     . HOH E 4 .   ? 18.337  -23.957 -0.795  1.00 48.89  ? 670 HOH A O     1 
HETATM 2974 O  O     . HOH E 4 .   ? 21.952  -5.652  2.287   1.00 43.21  ? 671 HOH A O     1 
HETATM 2975 O  O     . HOH E 4 .   ? 23.368  8.921   18.305  1.00 52.07  ? 672 HOH A O     1 
HETATM 2976 O  O     . HOH E 4 .   ? 3.084   13.024  4.567   1.00 45.23  ? 673 HOH A O     1 
HETATM 2977 O  O     . HOH E 4 .   ? 30.172  11.580  55.064  1.00 38.69  ? 674 HOH A O     1 
HETATM 2978 O  O     . HOH E 4 .   ? 20.878  15.423  15.547  1.00 59.98  ? 675 HOH A O     1 
HETATM 2979 O  O     . HOH E 4 .   ? 0.376   -19.117 5.410   1.00 54.12  ? 676 HOH A O     1 
HETATM 2980 O  O     . HOH E 4 .   ? 15.295  -18.794 13.685  1.00 38.87  ? 677 HOH A O     1 
HETATM 2981 O  O     . HOH E 4 .   ? 31.853  1.191   -0.270  1.00 36.68  ? 678 HOH A O     1 
HETATM 2982 O  O     . HOH E 4 .   ? 11.194  16.178  -3.575  1.00 36.04  ? 679 HOH A O     1 
HETATM 2983 O  O     . HOH E 4 .   ? -0.746  -10.618 59.695  1.00 51.70  ? 680 HOH A O     1 
HETATM 2984 O  O     . HOH E 4 .   ? 18.373  -23.054 13.582  1.00 44.10  ? 681 HOH A O     1 
HETATM 2985 O  O     . HOH E 4 .   ? 29.282  -13.239 13.468  1.00 29.25  ? 682 HOH A O     1 
HETATM 2986 O  O     . HOH E 4 .   ? 15.720  0.371   57.037  1.00 44.24  ? 683 HOH A O     1 
HETATM 2987 O  O     . HOH E 4 .   ? 1.737   -10.686 57.931  1.00 57.21  ? 684 HOH A O     1 
HETATM 2988 O  O     . HOH E 4 .   ? 17.281  -17.388 17.120  1.00 35.94  ? 685 HOH A O     1 
HETATM 2989 O  O     . HOH E 4 .   ? 7.206   -1.180  -9.186  1.00 41.69  ? 686 HOH A O     1 
HETATM 2990 O  O     . HOH E 4 .   ? 25.169  7.723   17.770  1.00 55.85  ? 687 HOH A O     1 
HETATM 2991 O  O     . HOH E 4 .   ? 0.658   -21.177 10.005  1.00 41.50  ? 688 HOH A O     1 
HETATM 2992 O  O     . HOH E 4 .   ? 19.514  -18.957 15.571  1.00 39.41  ? 689 HOH A O     1 
HETATM 2993 O  O     . HOH E 4 .   ? 23.132  20.250  47.041  1.00 53.49  ? 690 HOH A O     1 
HETATM 2994 O  O     . HOH E 4 .   ? 16.994  17.046  59.332  1.00 36.67  ? 691 HOH A O     1 
HETATM 2995 O  O     . HOH E 4 .   ? 36.397  -7.749  0.481   1.00 43.72  ? 692 HOH A O     1 
HETATM 2996 O  O     . HOH E 4 .   ? 25.489  -2.419  53.445  1.00 54.02  ? 693 HOH A O     1 
HETATM 2997 O  O     . HOH E 4 .   ? 21.960  -17.342 -6.340  1.00 42.06  ? 694 HOH A O     1 
HETATM 2998 O  O     . HOH E 4 .   ? 29.042  6.662   53.863  1.00 37.63  ? 695 HOH A O     1 
HETATM 2999 O  O     . HOH E 4 .   ? 30.085  -13.239 10.924  1.00 39.83  ? 696 HOH A O     1 
HETATM 3000 O  O     . HOH E 4 .   ? 3.957   2.468   -6.251  1.00 44.77  ? 697 HOH A O     1 
HETATM 3001 O  O     . HOH E 4 .   ? -4.583  -2.197  62.691  1.00 38.43  ? 698 HOH A O     1 
HETATM 3002 O  O     . HOH E 4 .   ? 14.783  3.608   29.403  1.00 56.36  ? 699 HOH A O     1 
# 
