data_9F1W
# 
_entry.id   9F1W 
# 
_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   9F1W         pdb_00009f1w 10.2210/pdb9f1w/pdb 
WWPDB D_1292138014 ?            ?                   
# 
_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                        9F1W 
_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                     'SFX 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    113 ? ? ? ? 
# 
_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 ?   ?   ?   A . n 
A 1 361 SER 361 333 ?   ?   ?   A . n 
A 1 362 SER 362 334 ?   ?   ?   A . n 
A 1 363 GLY 363 335 ?   ?   ?   A . n 
A 1 364 GLY 364 336 ?   ?   ?   A . n 
A 1 365 LEU 365 337 ?   ?   ?   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   401 401 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   501 446 HOH HOH A . 
E 4 HOH 2   502 416 HOH HOH A . 
E 4 HOH 3   503 453 HOH HOH A . 
E 4 HOH 4   504 363 HOH HOH A . 
E 4 HOH 5   505 460 HOH HOH A . 
E 4 HOH 6   506 278 HOH HOH A . 
E 4 HOH 7   507 340 HOH HOH A . 
E 4 HOH 8   508 457 HOH HOH A . 
E 4 HOH 9   509 136 HOH HOH A . 
E 4 HOH 10  510 67  HOH HOH A . 
E 4 HOH 11  511 312 HOH HOH A . 
E 4 HOH 12  512 310 HOH HOH A . 
E 4 HOH 13  513 239 HOH HOH A . 
E 4 HOH 14  514 444 HOH HOH A . 
E 4 HOH 15  515 337 HOH HOH A . 
E 4 HOH 16  516 41  HOH HOH A . 
E 4 HOH 17  517 394 HOH HOH A . 
E 4 HOH 18  518 454 HOH HOH A . 
E 4 HOH 19  519 8   HOH HOH A . 
E 4 HOH 20  520 52  HOH HOH A . 
E 4 HOH 21  521 459 HOH HOH A . 
E 4 HOH 22  522 411 HOH HOH A . 
E 4 HOH 23  523 277 HOH HOH A . 
E 4 HOH 24  524 447 HOH HOH A . 
E 4 HOH 25  525 77  HOH HOH A . 
E 4 HOH 26  526 10  HOH HOH A . 
E 4 HOH 27  527 374 HOH HOH A . 
E 4 HOH 28  528 157 HOH HOH A . 
E 4 HOH 29  529 390 HOH HOH A . 
E 4 HOH 30  530 448 HOH HOH A . 
E 4 HOH 31  531 18  HOH HOH A . 
E 4 HOH 32  532 34  HOH HOH A . 
E 4 HOH 33  533 3   HOH HOH A . 
E 4 HOH 34  534 93  HOH HOH A . 
E 4 HOH 35  535 19  HOH HOH A . 
E 4 HOH 36  536 404 HOH HOH A . 
E 4 HOH 37  537 11  HOH HOH A . 
E 4 HOH 38  538 314 HOH HOH A . 
E 4 HOH 39  539 15  HOH HOH A . 
E 4 HOH 40  540 4   HOH HOH A . 
E 4 HOH 41  541 5   HOH HOH A . 
E 4 HOH 42  542 458 HOH HOH A . 
E 4 HOH 43  543 45  HOH HOH A . 
E 4 HOH 44  544 9   HOH HOH A . 
E 4 HOH 45  545 38  HOH HOH A . 
E 4 HOH 46  546 438 HOH HOH A . 
E 4 HOH 47  547 328 HOH HOH A . 
E 4 HOH 48  548 36  HOH HOH A . 
E 4 HOH 49  549 13  HOH HOH A . 
E 4 HOH 50  550 6   HOH HOH A . 
E 4 HOH 51  551 7   HOH HOH A . 
E 4 HOH 52  552 380 HOH HOH A . 
E 4 HOH 53  553 20  HOH HOH A . 
E 4 HOH 54  554 35  HOH HOH A . 
E 4 HOH 55  555 433 HOH HOH A . 
E 4 HOH 56  556 129 HOH HOH A . 
E 4 HOH 57  557 28  HOH HOH A . 
E 4 HOH 58  558 59  HOH HOH A . 
E 4 HOH 59  559 243 HOH HOH A . 
E 4 HOH 60  560 12  HOH HOH A . 
E 4 HOH 61  561 22  HOH HOH A . 
E 4 HOH 62  562 407 HOH HOH A . 
E 4 HOH 63  563 42  HOH HOH A . 
E 4 HOH 64  564 47  HOH HOH A . 
E 4 HOH 65  565 101 HOH HOH A . 
E 4 HOH 66  566 43  HOH HOH A . 
E 4 HOH 67  567 25  HOH HOH A . 
E 4 HOH 68  568 32  HOH HOH A . 
E 4 HOH 69  569 452 HOH HOH A . 
E 4 HOH 70  570 449 HOH HOH A . 
E 4 HOH 71  571 451 HOH HOH A . 
E 4 HOH 72  572 381 HOH HOH A . 
E 4 HOH 73  573 78  HOH HOH A . 
E 4 HOH 74  574 392 HOH HOH A . 
E 4 HOH 75  575 327 HOH HOH A . 
E 4 HOH 76  576 30  HOH HOH A . 
E 4 HOH 77  577 14  HOH HOH A . 
E 4 HOH 78  578 403 HOH HOH A . 
E 4 HOH 79  579 16  HOH HOH A . 
E 4 HOH 80  580 55  HOH HOH A . 
E 4 HOH 81  581 61  HOH HOH A . 
E 4 HOH 82  582 384 HOH HOH A . 
E 4 HOH 83  583 139 HOH HOH A . 
E 4 HOH 84  584 57  HOH HOH A . 
E 4 HOH 85  585 17  HOH HOH A . 
E 4 HOH 86  586 396 HOH HOH A . 
E 4 HOH 87  587 326 HOH HOH A . 
E 4 HOH 88  588 29  HOH HOH A . 
E 4 HOH 89  589 2   HOH HOH A . 
E 4 HOH 90  590 386 HOH HOH A . 
E 4 HOH 91  591 44  HOH HOH A . 
E 4 HOH 92  592 455 HOH HOH A . 
E 4 HOH 93  593 33  HOH HOH A . 
E 4 HOH 94  594 69  HOH HOH A . 
E 4 HOH 95  595 216 HOH HOH A . 
E 4 HOH 96  596 434 HOH HOH A . 
E 4 HOH 97  597 107 HOH HOH A . 
E 4 HOH 98  598 1   HOH HOH A . 
E 4 HOH 99  599 313 HOH HOH A . 
E 4 HOH 100 600 219 HOH HOH A . 
E 4 HOH 101 601 62  HOH HOH A . 
E 4 HOH 102 602 218 HOH HOH A . 
E 4 HOH 103 603 271 HOH HOH A . 
E 4 HOH 104 604 156 HOH HOH A . 
E 4 HOH 105 605 379 HOH HOH A . 
E 4 HOH 106 606 408 HOH HOH A . 
E 4 HOH 107 607 409 HOH HOH A . 
E 4 HOH 108 608 450 HOH HOH A . 
E 4 HOH 109 609 410 HOH HOH A . 
E 4 HOH 110 610 300 HOH HOH A . 
E 4 HOH 111 611 406 HOH HOH A . 
E 4 HOH 112 612 355 HOH HOH A . 
E 4 HOH 113 613 432 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 GLU 117 ? CG  ? A GLU 145 CG  
2  1 Y 1 A GLU 117 ? CD  ? A GLU 145 CD  
3  1 Y 1 A GLU 117 ? OE1 ? A GLU 145 OE1 
4  1 Y 1 A GLU 117 ? OE2 ? A GLU 145 OE2 
5  1 Y 1 A GLU 260 ? CG  ? A GLU 288 CG  
6  1 Y 1 A GLU 260 ? CD  ? A GLU 288 CD  
7  1 Y 1 A GLU 260 ? OE1 ? A GLU 288 OE1 
8  1 Y 1 A GLU 260 ? OE2 ? A GLU 288 OE2 
9  1 Y 1 A LEU 261 ? CG  ? A LEU 289 CG  
10 1 Y 1 A LEU 261 ? CD1 ? A LEU 289 CD1 
11 1 Y 1 A LEU 261 ? CD2 ? A LEU 289 CD2 
12 1 Y 1 A LYS 314 ? CG  ? A LYS 342 CG  
13 1 Y 1 A LYS 314 ? CD  ? A LYS 342 CD  
14 1 Y 1 A LYS 314 ? CE  ? A LYS 342 CE  
15 1 Y 1 A LYS 314 ? NZ  ? A LYS 342 NZ  
16 1 Y 1 A LYS 316 ? CG  ? A LYS 344 CG  
17 1 Y 1 A LYS 316 ? CD  ? A LYS 344 CD  
18 1 Y 1 A LYS 316 ? CE  ? A LYS 344 CE  
19 1 Y 1 A LYS 316 ? NZ  ? A LYS 344 NZ  
20 1 Y 1 A ARG 349 ? CG  ? A ARG 377 CG  
21 1 Y 1 A ARG 349 ? CD  ? A ARG 377 CD  
22 1 Y 1 A ARG 349 ? NE  ? A ARG 377 NE  
23 1 Y 1 A ARG 349 ? CZ  ? A ARG 377 CZ  
24 1 Y 1 A ARG 349 ? NH1 ? A ARG 377 NH1 
25 1 Y 1 A ARG 349 ? NH2 ? A ARG 377 NH2 
26 1 Y 1 A VAL 350 ? CG1 ? A VAL 378 CG1 
27 1 Y 1 A VAL 350 ? CG2 ? A VAL 378 CG2 
28 1 N 1 A FAD 401 ? PA  ? B FAD 1   PA  
29 1 N 1 A FAD 401 ? O1A ? B FAD 1   O1A 
30 1 N 1 A FAD 401 ? O2A ? B FAD 1   O2A 
31 1 N 1 A FAD 401 ? O5B ? B FAD 1   O5B 
32 1 N 1 A FAD 401 ? C5B ? B FAD 1   C5B 
33 1 N 1 A FAD 401 ? C4B ? B FAD 1   C4B 
34 1 N 1 A FAD 401 ? O4B ? B FAD 1   O4B 
35 1 N 1 A FAD 401 ? C3B ? B FAD 1   C3B 
36 1 N 1 A FAD 401 ? O3B ? B FAD 1   O3B 
37 1 N 1 A FAD 401 ? C2B ? B FAD 1   C2B 
38 1 N 1 A FAD 401 ? O2B ? B FAD 1   O2B 
39 1 N 1 A FAD 401 ? C1B ? B FAD 1   C1B 
40 1 N 1 A FAD 401 ? N9A ? B FAD 1   N9A 
41 1 N 1 A FAD 401 ? C8A ? B FAD 1   C8A 
42 1 N 1 A FAD 401 ? N7A ? B FAD 1   N7A 
43 1 N 1 A FAD 401 ? C5A ? B FAD 1   C5A 
44 1 N 1 A FAD 401 ? C6A ? B FAD 1   C6A 
45 1 N 1 A FAD 401 ? N6A ? B FAD 1   N6A 
46 1 N 1 A FAD 401 ? N1A ? B FAD 1   N1A 
47 1 N 1 A FAD 401 ? C2A ? B FAD 1   C2A 
48 1 N 1 A FAD 401 ? N3A ? B FAD 1   N3A 
49 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 reduction' ? ? ? ? ? ? ? ? ? ? ? CrystFEL ? ? ? .               2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? CrystFEL ? ? ? .               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                     9F1W 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     102.900 
_cell.length_a_esd                 ? 
_cell.length_b                     54.910 
_cell.length_b_esd                 ? 
_cell.length_c                     72.980 
_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                         9F1W 
_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                   9F1W 
_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          'BATCH MODE' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.06 M divalents, 0.1 M Tris-Bicine 8.5, 30% v/v PEG550 MME-PEG20000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     293 
_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   Y 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         AGIPD 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-10-26 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.33 
_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                      'FREE ELECTRON LASER' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'EUROPEAN XFEL BEAMLINE SPB/SFX' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.33 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   SPB/SFX 
_diffrn_source.pdbx_synchrotron_site       'European XFEL' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9F1W 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.75 
_reflns.d_resolution_low                               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                                     42444 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                453 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.9905 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   0.085 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.75 
_reflns_shell.d_res_low                                     1.78 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.1 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2694 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.5868 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  0.908 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9F1W 
_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                            1.75 
_refine.ls_d_res_low                             26.53 
_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                     42444 
_refine.ls_number_reflns_R_free                  2046 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.95 
_refine.ls_percent_reflns_R_free                 4.82 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1949 
_refine.ls_R_factor_R_free                       0.2191 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1937 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               NONE 
_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                 23.94 
_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                       1.75 
_refine_hist.d_res_low                        26.53 
_refine_hist.number_atoms_solvent             113 
_refine_hist.number_atoms_total               2844 
_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        2698 
_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' ? 0.009  ? 2868 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.879  ? 3912 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 10.308 ? 409  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.065  ? 460  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009  ? 499  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.75 1.79  . . 123 2661 100.00 . . . . 0.3142 . . . . . . . . . . . 0.3406 
'X-RAY DIFFRACTION' 1.79 1.84  . . 132 2688 100.00 . . . . 0.2934 . . . . . . . . . . . 0.3062 
'X-RAY DIFFRACTION' 1.84 1.89  . . 135 2636 100.00 . . . . 0.3656 . . . . . . . . . . . 0.4145 
'X-RAY DIFFRACTION' 1.89 1.94  . . 144 2664 100.00 . . . . 0.3643 . . . . . . . . . . . 0.4341 
'X-RAY DIFFRACTION' 1.94 2.00  . . 152 2610 100.00 . . . . 0.2451 . . . . . . . . . . . 0.3034 
'X-RAY DIFFRACTION' 2.00 2.07  . . 152 2653 100.00 . . . . 0.2034 . . . . . . . . . . . 0.2640 
'X-RAY DIFFRACTION' 2.07 2.16  . . 123 2673 100.00 . . . . 0.2035 . . . . . . . . . . . 0.2194 
'X-RAY DIFFRACTION' 2.16 2.26  . . 136 2675 100.00 . . . . 0.2110 . . . . . . . . . . . 0.2383 
'X-RAY DIFFRACTION' 2.26 2.37  . . 123 2681 100.00 . . . . 0.2224 . . . . . . . . . . . 0.2339 
'X-RAY DIFFRACTION' 2.37 2.52  . . 131 2703 100.00 . . . . 0.2104 . . . . . . . . . . . 0.2831 
'X-RAY DIFFRACTION' 2.52 2.72  . . 134 2684 100.00 . . . . 0.2027 . . . . . . . . . . . 0.2521 
'X-RAY DIFFRACTION' 2.72 2.99  . . 145 2712 100.00 . . . . 0.2028 . . . . . . . . . . . 0.2007 
'X-RAY DIFFRACTION' 2.99 3.42  . . 125 2732 100.00 . . . . 0.1811 . . . . . . . . . . . 0.1996 
'X-RAY DIFFRACTION' 3.42 4.31  . . 150 2744 100.00 . . . . 0.1579 . . . . . . . . . . . 0.1791 
'X-RAY DIFFRACTION' 4.31 26.53 . . 141 2882 100.00 . . . . 0.1762 . . . . . . . . . . . 0.1956 
# 
_struct.entry_id                     9F1W 
_struct.title                        'SFX room temperature structure of Oscillatoria acuminata adenylyate cyclase.' 
_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        9F1W 
_struct_keywords.text            'FAD, SFX, EuXFEL, room temperature, 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              9F1W 
_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 9F1W MET A 1  ? UNP K9TLZ5 ? ? 'initiating methionine' -27 1  
1 9F1W GLY A 2  ? UNP K9TLZ5 ? ? 'expression tag'        -26 2  
1 9F1W SER A 3  ? UNP K9TLZ5 ? ? 'expression tag'        -25 3  
1 9F1W SER A 4  ? UNP K9TLZ5 ? ? 'expression tag'        -24 4  
1 9F1W HIS A 5  ? UNP K9TLZ5 ? ? 'expression tag'        -23 5  
1 9F1W HIS A 6  ? UNP K9TLZ5 ? ? 'expression tag'        -22 6  
1 9F1W HIS A 7  ? UNP K9TLZ5 ? ? 'expression tag'        -21 7  
1 9F1W HIS A 8  ? UNP K9TLZ5 ? ? 'expression tag'        -20 8  
1 9F1W HIS A 9  ? UNP K9TLZ5 ? ? 'expression tag'        -19 9  
1 9F1W HIS A 10 ? UNP K9TLZ5 ? ? 'expression tag'        -18 10 
1 9F1W SER A 11 ? UNP K9TLZ5 ? ? 'expression tag'        -17 11 
1 9F1W SER A 12 ? UNP K9TLZ5 ? ? 'expression tag'        -16 12 
1 9F1W GLY A 13 ? UNP K9TLZ5 ? ? 'expression tag'        -15 13 
1 9F1W LEU A 14 ? UNP K9TLZ5 ? ? 'expression tag'        -14 14 
1 9F1W VAL A 15 ? UNP K9TLZ5 ? ? 'expression tag'        -13 15 
1 9F1W PRO A 16 ? UNP K9TLZ5 ? ? 'expression tag'        -12 16 
1 9F1W ARG A 17 ? UNP K9TLZ5 ? ? 'expression tag'        -11 17 
1 9F1W GLY A 18 ? UNP K9TLZ5 ? ? 'expression tag'        -10 18 
1 9F1W SER A 19 ? UNP K9TLZ5 ? ? 'expression tag'        -9  19 
1 9F1W HIS A 20 ? UNP K9TLZ5 ? ? 'expression tag'        -8  20 
1 9F1W MET A 21 ? UNP K9TLZ5 ? ? 'expression tag'        -7  21 
1 9F1W GLU A 22 ? UNP K9TLZ5 ? ? 'expression tag'        -6  22 
1 9F1W ASN A 23 ? UNP K9TLZ5 ? ? 'expression tag'        -5  23 
1 9F1W LEU A 24 ? UNP K9TLZ5 ? ? 'expression tag'        -4  24 
1 9F1W TYR A 25 ? UNP K9TLZ5 ? ? 'expression tag'        -3  25 
1 9F1W PHE A 26 ? UNP K9TLZ5 ? ? 'expression tag'        -2  26 
1 9F1W GLN A 27 ? UNP K9TLZ5 ? ? 'expression tag'        -1  27 
1 9F1W 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)' 9830  ? 
1 MORE         -128  ? 
1 'SSA (A^2)'  30600 ? 
# 
_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  ? ALA A 61  ? SER A 15  ALA A 33  1 ? 19 
HELX_P HELX_P2  AA2 ALA A 82  ? ALA A 94  ? ALA A 54  ALA A 66  1 ? 13 
HELX_P HELX_P3  AA3 ASP A 126 ? ASN A 128 ? ASP A 98  ASN A 100 5 ? 3  
HELX_P HELX_P4  AA4 LEU A 132 ? TYR A 153 ? LEU A 104 TYR A 125 1 ? 22 
HELX_P HELX_P5  AA5 PRO A 156 ? GLN A 164 ? PRO A 128 GLN A 136 1 ? 9  
HELX_P HELX_P6  AA6 ASN A 167 ? ILE A 171 ? ASN A 139 ILE A 143 5 ? 5  
HELX_P HELX_P7  AA7 SER A 187 ? LEU A 195 ? SER A 159 LEU A 167 1 ? 9  
HELX_P HELX_P8  AA8 PRO A 196 ? GLN A 218 ? PRO A 168 GLN A 190 1 ? 23 
HELX_P HELX_P9  AA9 CYS A 238 ? ALA A 260 ? CYS A 210 ALA A 232 1 ? 23 
HELX_P HELX_P10 AB1 SER A 264 ? LEU A 269 ? SER A 236 LEU A 241 5 ? 6  
HELX_P HELX_P11 AB2 ASP A 298 ? SER A 314 ? ASP A 270 SER A 286 1 ? 17 
HELX_P HELX_P12 AB3 SER A 321 ? ALA A 327 ? SER A 293 ALA A 299 1 ? 7  
HELX_P HELX_P13 AB4 ILE A 367 ? ARG A 377 ? ILE A 339 ARG A 349 1 ? 11 
# 
_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 ? ? ? ? ? ? ? 2.450 ? ? 
metalc2  metalc ? ? A ASP 184 OD1 B ? ? 1_555 D CA  . CA ? ? A ASP 156 A CA  403 1_555 ? ? ? ? ? ? ? 2.469 ? ? 
metalc3  metalc ? ? A ASP 184 OD2 B ? ? 1_555 D CA  . CA ? ? A ASP 156 A CA  403 1_555 ? ? ? ? ? ? ? 2.242 ? ? 
metalc4  metalc ? ? A ASP 228 OD1 ? ? ? 1_555 D CA  . CA ? ? A ASP 200 A CA  403 1_555 ? ? ? ? ? ? ? 2.923 ? ? 
metalc5  metalc ? ? A ASP 228 OD2 ? ? ? 1_555 D CA  . CA ? ? A ASP 200 A CA  403 1_555 ? ? ? ? ? ? ? 2.388 ? ? 
metalc6  metalc ? ? A ASP 298 OD1 ? ? ? 1_555 D CA  . CA ? ? A ASP 270 A CA  403 2_555 ? ? ? ? ? ? ? 2.464 ? ? 
metalc7  metalc ? ? A ASP 338 OD1 ? ? ? 1_555 C CA  . CA ? ? A ASP 310 A CA  402 1_555 ? ? ? ? ? ? ? 2.525 ? ? 
metalc8  metalc ? ? A ASP 338 OD2 ? ? ? 1_555 C CA  . CA ? ? A ASP 310 A CA  402 1_555 ? ? ? ? ? ? ? 2.435 ? ? 
metalc9  metalc ? ? A ASP 349 OD1 ? ? ? 1_555 C CA  . CA ? ? A ASP 321 A CA  402 1_555 ? ? ? ? ? ? ? 2.371 ? ? 
metalc10 metalc ? ? C CA  .   CA  ? ? ? 1_555 E HOH . O  ? ? A CA  402 A HOH 571 1_555 ? ? ? ? ? ? ? 2.340 ? ? 
metalc11 metalc ? ? C CA  .   CA  ? ? ? 1_555 E HOH . O  ? ? A CA  402 A HOH 600 1_555 ? ? ? ? ? ? ? 2.518 ? ? 
metalc12 metalc ? ? C CA  .   CA  ? ? ? 1_555 E HOH . O  ? ? A CA  402 A HOH 602 1_554 ? ? ? ? ? ? ? 2.460 ? ? 
metalc13 metalc ? ? D CA  .   CA  ? ? ? 1_555 E HOH . O  ? ? A CA  403 A HOH 506 2_555 ? ? ? ? ? ? ? 2.264 ? ? 
metalc14 metalc ? ? D CA  .   CA  ? ? ? 1_555 E HOH . O  ? ? A CA  403 A HOH 523 1_555 ? ? ? ? ? ? ? 2.553 ? ? 
metalc15 metalc ? ? D CA  .   CA  ? ? ? 1_555 E HOH . O  ? ? A CA  403 A HOH 525 1_555 ? ? ? ? ? ? ? 2.360 ? ? 
metalc16 metalc ? ? D CA  .   CA  ? ? ? 1_555 E HOH . O  ? ? A CA  403 A HOH 547 1_555 ? ? ? ? ? ? ? 3.194 ? ? 
# 
_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 32.2  ? 
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 30.6  ? 
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 1.6   ? 
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 32.6  ? 
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 1.9   ? 
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 2.6   ? 
7  O   ? A ASP 117 ? A ASP 89  ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 571 ? 1_555 30.1  ? 
8  OD1 ? A ASP 338 ? A ASP 310 ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 571 ? 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 571 ? 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 571 ? 1_555 2.6   ? 
11 O   ? A ASP 117 ? A ASP 89  ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 600 ? 1_555 33.0  ? 
12 OD1 ? A ASP 338 ? A ASP 310 ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 600 ? 1_555 2.3   ? 
13 OD2 ? A ASP 338 ? A ASP 310 ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 600 ? 1_555 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 600 ? 1_555 0.5   ? 
15 O   ? E HOH .   ? A HOH 571 ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 600 ? 1_555 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 602 ? 1_554 31.6  ? 
17 OD1 ? A ASP 338 ? A ASP 310 ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 602 ? 1_554 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 602 ? 1_554 3.7   ? 
19 OD1 ? A ASP 349 ? A ASP 321 ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 602 ? 1_554 2.2   ? 
20 O   ? E HOH .   ? A HOH 571 ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 602 ? 1_554 2.0   ? 
21 O   ? E HOH .   ? A HOH 600 ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 602 ? 1_554 2.1   ? 
22 OD1 B A ASP 184 ? A ASP 156 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 OD2 B A ASP 184 ? A ASP 156 ? 1_555 55.1  ? 
23 OD1 B 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 70.0  ? 
24 OD2 B A ASP 184 ? A ASP 156 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 OD1 ? A ASP 228 ? A ASP 200 ? 1_555 125.1 ? 
25 OD1 B 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 59.1  ? 
26 OD2 B 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 97.3  ? 
27 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 47.1  ? 
28 OD1 B 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 74.4  ? 
29 OD2 B 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 83.4  ? 
30 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 84.0  ? 
31 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_555 119.9 ? 
32 OD1 B A ASP 184 ? A ASP 156 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 506 ? 2_555 109.4 ? 
33 OD2 B A ASP 184 ? A ASP 156 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 506 ? 2_555 90.9  ? 
34 OD1 ? A ASP 228 ? A ASP 200 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 506 ? 2_555 110.2 ? 
35 OD2 ? A ASP 228 ? A ASP 200 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 506 ? 2_555 155.8 ? 
36 OD1 ? A ASP 298 ? A ASP 270 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 506 ? 2_555 38.4  ? 
37 OD1 B A ASP 184 ? A ASP 156 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 523 ? 1_555 68.1  ? 
38 OD2 B A ASP 184 ? A ASP 156 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 523 ? 1_555 92.1  ? 
39 OD1 ? A ASP 228 ? A ASP 200 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 523 ? 1_555 67.4  ? 
40 OD2 ? A ASP 228 ? A ASP 200 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 523 ? 1_555 104.7 ? 
41 OD1 ? A ASP 298 ? A ASP 270 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 523 ? 1_555 16.7  ? 
42 O   ? E HOH .   ? A HOH 506 ? 2_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 523 ? 1_555 52.0  ? 
43 OD1 B A ASP 184 ? A ASP 156 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 525 ? 1_555 131.8 ? 
44 OD2 B A ASP 184 ? A ASP 156 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 525 ? 1_555 95.7  ? 
45 OD1 ? A ASP 228 ? A ASP 200 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 525 ? 1_555 122.0 ? 
46 OD2 ? A ASP 228 ? A ASP 200 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 525 ? 1_555 93.7  ? 
47 OD1 ? A ASP 298 ? A ASP 270 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 525 ? 1_555 146.3 ? 
48 O   ? E HOH .   ? A HOH 506 ? 2_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 525 ? 1_555 108.2 ? 
49 O   ? E HOH .   ? A HOH 523 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 525 ? 1_555 158.9 ? 
50 OD1 B A ASP 184 ? A ASP 156 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 547 ? 1_555 131.1 ? 
51 OD2 B A ASP 184 ? A ASP 156 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 547 ? 1_555 85.7  ? 
52 OD1 ? A ASP 228 ? A ASP 200 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 547 ? 1_555 139.3 ? 
53 OD2 ? A ASP 228 ? A ASP 200 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 547 ? 1_555 167.0 ? 
54 OD1 ? A ASP 298 ? A ASP 270 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 547 ? 1_555 73.0  ? 
55 O   ? E HOH .   ? A HOH 506 ? 2_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 547 ? 1_555 36.0  ? 
56 O   ? E HOH .   ? A HOH 523 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 547 ? 1_555 87.8  ? 
57 O   ? E HOH .   ? A HOH 525 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 547 ? 1_555 73.3  ? 
# 
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 THR A 99  ? O THR A 71  N LYS A 37  ? N LYS A 9   
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 LYS A 174 ? N LYS A 146 O GLU A 282 ? O GLU A 254 
AA2 4 5 N ILE A 285 ? N ILE A 257 O ASP A 292 ? O ASP A 264 
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 LYS A 174 ? N LYS A 146 O GLU A 282 ? O GLU A 254 
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 348 ? O ILE A 320 N SER A 339 ? N SER A 311 
# 
_pdbx_entry_details.entry_id                   9F1W 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_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 503 ? ? O   A HOH 518 ? ? 2.00 
2 1 N   A ILE 130 ? ? O   A HOH 502 ? ? 2.10 
3 1 O   A ASP 326 ? ? O   A HOH 503 ? ? 2.11 
4 1 OG  A SER 129 ? ? OE2 A GLU 193 ? ? 2.12 
5 1 OE1 A GLU 338 ? ? O   A HOH 504 ? ? 2.13 
6 1 O   A HOH 508 ? ? O   A HOH 604 ? ? 2.17 
7 1 NZ  A LYS 262 ? ? O   A HOH 505 ? ? 2.17 
8 1 OD1 A ASN 273 ? ? O   A HOH 506 ? ? 2.17 
9 1 O   A HOH 611 ? ? O   A HOH 612 ? ? 2.18 
# 
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 506 ? ? 1_555 O A HOH 547 ? ? 2_555 1.90 
2 1 O A HOH 506 ? ? 1_555 O A HOH 523 ? ? 2_555 2.13 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 MET A 92  ? ? -160.05 110.67 
2 1 ARG A 349 ? ? -103.30 73.31  
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     239 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.079 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 608 ? E HOH . 
2 1 A HOH 613 ? E HOH . 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 611 ? 8.27 . 
2 1 O ? A HOH 612 ? 8.42 . 
3 1 O ? A HOH 613 ? 8.56 . 
# 
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 LYS 332 ? A LYS 360 
29 1 Y 1 A SER 333 ? A SER 361 
30 1 Y 1 A SER 334 ? A SER 362 
31 1 Y 1 A GLY 335 ? A GLY 363 
32 1 Y 1 A GLY 336 ? A GLY 364 
33 1 Y 1 A LEU 337 ? A LEU 365 
34 1 Y 1 A GLY 351 ? A GLY 379 
35 1 Y 1 A ASP 352 ? A ASP 380 
36 1 Y 1 A ARG 353 ? A ARG 381 
37 1 Y 1 A GLN 354 ? A GLN 382 
38 1 Y 1 A PRO 355 ? A PRO 383 
39 1 Y 1 A SER 356 ? A SER 384 
40 1 Y 1 A GLN 357 ? A GLN 385 
41 1 Y 1 A ILE 358 ? A ILE 386 
42 1 Y 1 A PHE 359 ? A PHE 387 
43 1 Y 1 A GLY 360 ? A GLY 388 
44 1 Y 1 A VAL 361 ? A VAL 389 
45 1 Y 1 A LYS 362 ? A LYS 390 
46 1 Y 1 A SER 363 ? A SER 391 
47 1 Y 1 A LEU 364 ? A LEU 392 
48 1 Y 1 A PRO 365 ? A PRO 393 
49 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          ? 
# 
_pdbx_serial_crystallography_measurement.diffrn_id                    1 
_pdbx_serial_crystallography_measurement.pulse_energy                 ? 
_pdbx_serial_crystallography_measurement.pulse_duration               50 
_pdbx_serial_crystallography_measurement.xfel_pulse_repetition_rate   564000 
_pdbx_serial_crystallography_measurement.pulse_photon_energy          9.3 
_pdbx_serial_crystallography_measurement.photons_per_pulse            ? 
_pdbx_serial_crystallography_measurement.source_size                  ? 
_pdbx_serial_crystallography_measurement.source_distance              ? 
_pdbx_serial_crystallography_measurement.focal_spot_size              3 
_pdbx_serial_crystallography_measurement.collimation                  ? 
_pdbx_serial_crystallography_measurement.collection_time_total        ? 
# 
_pdbx_serial_crystallography_sample_delivery.diffrn_id     1 
_pdbx_serial_crystallography_sample_delivery.description   GDVN 
_pdbx_serial_crystallography_sample_delivery.method        injection 
# 
_atom_sites.entry_id                    9F1W 
_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]   0.009718 
_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]   0.018212 
_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]   0.013702 
_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  ? 8.582   26.629  43.213  1.00 89.68  ? 0   GLY A N     1 
ATOM   2    C  CA    . GLY A 1 28  ? 9.888   26.311  42.644  1.00 93.37  ? 0   GLY A CA    1 
ATOM   3    C  C     . GLY A 1 28  ? 10.329  24.902  43.044  1.00 82.51  ? 0   GLY A C     1 
ATOM   4    O  O     . GLY A 1 28  ? 11.479  24.513  42.827  1.00 76.74  ? 0   GLY A O     1 
ATOM   5    N  N     . MET A 1 29  ? 9.406   24.136  43.616  1.00 76.31  ? 1   MET A N     1 
ATOM   6    C  CA    . MET A 1 29  ? 9.709   22.810  44.127  1.00 65.26  ? 1   MET A CA    1 
ATOM   7    C  C     . MET A 1 29  ? 9.290   21.727  43.142  1.00 56.42  ? 1   MET A C     1 
ATOM   8    O  O     . MET A 1 29  ? 8.312   21.875  42.402  1.00 57.12  ? 1   MET A O     1 
ATOM   9    C  CB    . MET A 1 29  ? 9.014   22.572  45.467  1.00 60.80  ? 1   MET A CB    1 
ATOM   10   C  CG    . MET A 1 29  ? 9.673   23.291  46.621  1.00 69.63  ? 1   MET A CG    1 
ATOM   11   S  SD    . MET A 1 29  ? 9.421   22.448  48.190  1.00 72.63  ? 1   MET A SD    1 
ATOM   12   C  CE    . MET A 1 29  ? 11.116  22.401  48.693  1.00 65.65  ? 1   MET A CE    1 
ATOM   13   N  N     . LYS A 1 30  ? 10.043  20.629  43.157  1.00 45.56  ? 2   LYS A N     1 
ATOM   14   C  CA    . LYS A 1 30  ? 9.761   19.430  42.386  1.00 47.59  ? 2   LYS A CA    1 
ATOM   15   C  C     . LYS A 1 30  ? 9.526   18.251  43.324  1.00 56.32  ? 2   LYS A C     1 
ATOM   16   O  O     . LYS A 1 30  ? 10.089  18.198  44.422  1.00 52.27  ? 2   LYS A O     1 
ATOM   17   C  CB    . LYS A 1 30  ? 10.923  19.084  41.448  1.00 52.66  ? 2   LYS A CB    1 
ATOM   18   C  CG    . LYS A 1 30  ? 10.520  18.442  40.148  1.00 59.57  ? 2   LYS A CG    1 
ATOM   19   C  CD    . LYS A 1 30  ? 11.447  18.880  39.030  1.00 64.90  ? 2   LYS A CD    1 
ATOM   20   C  CE    . LYS A 1 30  ? 11.770  17.716  38.103  1.00 69.36  ? 2   LYS A CE    1 
ATOM   21   N  NZ    . LYS A 1 30  ? 12.438  18.175  36.850  1.00 81.86  ? 2   LYS A NZ    1 
ATOM   22   N  N     . ARG A 1 31  ? 8.717   17.290  42.871  1.00 52.65  ? 3   ARG A N     1 
ATOM   23   C  CA    . ARG A 1 31  ? 8.515   16.028  43.585  1.00 45.80  ? 3   ARG A CA    1 
ATOM   24   C  C     . ARG A 1 31  ? 8.431   14.898  42.568  1.00 48.79  ? 3   ARG A C     1 
ATOM   25   O  O     . ARG A 1 31  ? 7.601   14.954  41.652  1.00 50.22  ? 3   ARG A O     1 
ATOM   26   C  CB    . ARG A 1 31  ? 7.246   16.079  44.452  1.00 42.16  ? 3   ARG A CB    1 
ATOM   27   C  CG    . ARG A 1 31  ? 6.966   14.788  45.233  1.00 42.33  ? 3   ARG A CG    1 
ATOM   28   C  CD    . ARG A 1 31  ? 6.074   15.025  46.442  1.00 40.00  ? 3   ARG A CD    1 
ATOM   29   N  NE    . ARG A 1 31  ? 4.824   15.684  46.080  1.00 46.28  ? 3   ARG A NE    1 
ATOM   30   C  CZ    . ARG A 1 31  ? 4.346   16.774  46.667  1.00 45.49  ? 3   ARG A CZ    1 
ATOM   31   N  NH1   . ARG A 1 31  ? 4.992   17.373  47.654  1.00 46.32  ? 3   ARG A NH1   1 
ATOM   32   N  NH2   . ARG A 1 31  ? 3.195   17.284  46.241  1.00 50.80  ? 3   ARG A NH2   1 
ATOM   33   N  N     . LEU A 1 32  ? 9.289   13.883  42.710  1.00 43.12  ? 4   LEU A N     1 
ATOM   34   C  CA    . LEU A 1 32  ? 9.286   12.726  41.820  1.00 41.87  ? 4   LEU A CA    1 
ATOM   35   C  C     . LEU A 1 32  ? 8.982   11.453  42.594  1.00 42.92  ? 4   LEU A C     1 
ATOM   36   O  O     . LEU A 1 32  ? 9.390   11.306  43.754  1.00 41.38  ? 4   LEU A O     1 
ATOM   37   C  CB    . LEU A 1 32  ? 10.625  12.531  41.092  1.00 47.52  ? 4   LEU A CB    1 
ATOM   38   C  CG    . LEU A 1 32  ? 11.427  13.659  40.455  1.00 57.52  ? 4   LEU A CG    1 
ATOM   39   C  CD1   . LEU A 1 32  ? 12.825  13.135  40.150  1.00 57.33  ? 4   LEU A CD1   1 
ATOM   40   C  CD2   . LEU A 1 32  ? 10.744  14.123  39.181  1.00 60.46  ? 4   LEU A CD2   1 
ATOM   41   N  N     . THR A 1 33  ? 8.268   10.531  41.931  1.00 38.56  ? 5   THR A N     1 
ATOM   42   C  CA    . THR A 1 33  ? 7.970   9.195   42.446  1.00 33.39  ? 5   THR A CA    1 
ATOM   43   C  C     . THR A 1 33  ? 8.437   8.151   41.440  1.00 40.01  ? 5   THR A C     1 
ATOM   44   O  O     . THR A 1 33  ? 8.071   8.227   40.262  1.00 43.31  ? 5   THR A O     1 
ATOM   45   C  CB    . THR A 1 33  ? 6.462   9.017   42.704  1.00 36.10  ? 5   THR A CB    1 
ATOM   46   O  OG1   . THR A 1 33  ? 5.977   10.085  43.525  1.00 40.14  ? 5   THR A OG1   1 
ATOM   47   C  CG2   . THR A 1 33  ? 6.183   7.683   43.388  1.00 38.21  ? 5   THR A CG2   1 
ATOM   48   N  N     . TYR A 1 34  ? 9.206   7.156   41.890  1.00 35.50  ? 6   TYR A N     1 
ATOM   49   C  CA    . TYR A 1 34  ? 9.662   6.118   40.965  1.00 34.32  ? 6   TYR A CA    1 
ATOM   50   C  C     . TYR A 1 34  ? 9.662   4.752   41.640  1.00 42.63  ? 6   TYR A C     1 
ATOM   51   O  O     . TYR A 1 34  ? 9.653   4.637   42.870  1.00 40.28  ? 6   TYR A O     1 
ATOM   52   C  CB    . TYR A 1 34  ? 11.065  6.439   40.385  1.00 41.56  ? 6   TYR A CB    1 
ATOM   53   C  CG    . TYR A 1 34  ? 12.222  6.236   41.350  1.00 40.77  ? 6   TYR A CG    1 
ATOM   54   C  CD1   . TYR A 1 34  ? 12.818  4.986   41.493  1.00 38.19  ? 6   TYR A CD1   1 
ATOM   55   C  CD2   . TYR A 1 34  ? 12.718  7.294   42.108  1.00 38.57  ? 6   TYR A CD2   1 
ATOM   56   C  CE1   . TYR A 1 34  ? 13.867  4.787   42.391  1.00 40.73  ? 6   TYR A CE1   1 
ATOM   57   C  CE2   . TYR A 1 34  ? 13.784  7.103   43.001  1.00 37.81  ? 6   TYR A CE2   1 
ATOM   58   C  CZ    . TYR A 1 34  ? 14.339  5.849   43.135  1.00 37.46  ? 6   TYR A CZ    1 
ATOM   59   O  OH    . TYR A 1 34  ? 15.386  5.633   44.021  1.00 42.01  ? 6   TYR A OH    1 
ATOM   60   N  N     . ILE A 1 35  ? 9.663   3.703   40.807  1.00 35.66  ? 7   ILE A N     1 
ATOM   61   C  CA    . ILE A 1 35  ? 9.850   2.328   41.253  1.00 31.58  ? 7   ILE A CA    1 
ATOM   62   C  C     . ILE A 1 35  ? 11.085  1.757   40.556  1.00 40.79  ? 7   ILE A C     1 
ATOM   63   O  O     . ILE A 1 35  ? 11.495  2.225   39.493  1.00 43.07  ? 7   ILE A O     1 
ATOM   64   C  CB    . ILE A 1 35  ? 8.617   1.436   40.987  1.00 42.81  ? 7   ILE A CB    1 
ATOM   65   C  CG1   . ILE A 1 35  ? 8.247   1.459   39.502  1.00 42.54  ? 7   ILE A CG1   1 
ATOM   66   C  CG2   . ILE A 1 35  ? 7.418   1.893   41.836  1.00 40.18  ? 7   ILE A CG2   1 
ATOM   67   C  CD1   . ILE A 1 35  ? 7.181   0.422   39.133  1.00 42.66  ? 7   ILE A CD1   1 
ATOM   68   N  N     . SER A 1 36  ? 11.678  0.733   41.174  1.00 38.34  ? 8   SER A N     1 
ATOM   69   C  CA    . SER A 1 36  ? 12.860  0.076   40.615  1.00 40.18  ? 8   SER A CA    1 
ATOM   70   C  C     . SER A 1 36  ? 12.986  -1.333  41.180  1.00 39.04  ? 8   SER A C     1 
ATOM   71   O  O     . SER A 1 36  ? 12.282  -1.711  42.115  1.00 42.95  ? 8   SER A O     1 
ATOM   72   C  CB    . SER A 1 36  ? 14.132  0.887   40.896  1.00 41.43  ? 8   SER A CB    1 
ATOM   73   O  OG    . SER A 1 36  ? 14.526  0.756   42.255  1.00 42.46  ? 8   SER A OG    1 
ATOM   74   N  N     . LYS A 1 37  ? 13.916  -2.113  40.607  1.00 42.14  ? 9   LYS A N     1 
ATOM   75   C  CA    . LYS A 1 37  ? 14.129  -3.508  40.977  1.00 41.75  ? 9   LYS A CA    1 
ATOM   76   C  C     . LYS A 1 37  ? 15.532  -3.693  41.545  1.00 42.27  ? 9   LYS A C     1 
ATOM   77   O  O     . LYS A 1 37  ? 16.494  -3.119  41.023  1.00 48.52  ? 9   LYS A O     1 
ATOM   78   C  CB    . LYS A 1 37  ? 13.966  -4.444  39.762  1.00 48.26  ? 9   LYS A CB    1 
ATOM   79   C  CG    . LYS A 1 37  ? 12.627  -4.325  39.049  1.00 63.26  ? 9   LYS A CG    1 
ATOM   80   C  CD    . LYS A 1 37  ? 11.704  -5.496  39.338  1.00 70.51  ? 9   LYS A CD    1 
ATOM   81   C  CE    . LYS A 1 37  ? 10.283  -5.005  39.616  1.00 71.50  ? 9   LYS A CE    1 
ATOM   82   N  NZ    . LYS A 1 37  ? 9.310   -6.129  39.729  1.00 69.95  ? 9   LYS A NZ    1 
ATOM   83   N  N     . PHE A 1 38  ? 15.650  -4.516  42.593  1.00 44.11  ? 10  PHE A N     1 
ATOM   84   C  CA    . PHE A 1 38  ? 16.966  -4.907  43.105  1.00 40.91  ? 10  PHE A CA    1 
ATOM   85   C  C     . PHE A 1 38  ? 17.751  -5.557  41.971  1.00 50.49  ? 10  PHE A C     1 
ATOM   86   O  O     . PHE A 1 38  ? 17.221  -6.412  41.259  1.00 49.91  ? 10  PHE A O     1 
ATOM   87   C  CB    . PHE A 1 38  ? 16.857  -5.918  44.253  1.00 43.54  ? 10  PHE A CB    1 
ATOM   88   C  CG    . PHE A 1 38  ? 16.326  -5.367  45.574  1.00 48.62  ? 10  PHE A CG    1 
ATOM   89   C  CD1   . PHE A 1 38  ? 15.614  -4.180  45.641  1.00 41.03  ? 10  PHE A CD1   1 
ATOM   90   C  CD2   . PHE A 1 38  ? 16.504  -6.099  46.742  1.00 49.79  ? 10  PHE A CD2   1 
ATOM   91   C  CE1   . PHE A 1 38  ? 15.119  -3.709  46.868  1.00 45.49  ? 10  PHE A CE1   1 
ATOM   92   C  CE2   . PHE A 1 38  ? 16.012  -5.646  47.973  1.00 49.87  ? 10  PHE A CE2   1 
ATOM   93   C  CZ    . PHE A 1 38  ? 15.313  -4.453  48.036  1.00 41.71  ? 10  PHE A CZ    1 
ATOM   94   N  N     . SER A 1 39  ? 19.016  -5.173  41.809  1.00 53.15  ? 11  SER A N     1 
ATOM   95   C  CA    . SER A 1 39  ? 19.854  -5.830  40.811  1.00 58.66  ? 11  SER A CA    1 
ATOM   96   C  C     . SER A 1 39  ? 20.553  -7.064  41.357  1.00 63.52  ? 11  SER A C     1 
ATOM   97   O  O     . SER A 1 39  ? 21.146  -7.818  40.579  1.00 71.50  ? 11  SER A O     1 
ATOM   98   C  CB    . SER A 1 39  ? 20.903  -4.861  40.265  1.00 54.08  ? 11  SER A CB    1 
ATOM   99   O  OG    . SER A 1 39  ? 21.783  -4.446  41.293  1.00 62.10  ? 11  SER A OG    1 
ATOM   100  N  N     . ARG A 1 40  ? 20.497  -7.272  42.667  1.00 53.73  ? 12  ARG A N     1 
ATOM   101  C  CA    . ARG A 1 40  ? 21.095  -8.405  43.355  1.00 61.22  ? 12  ARG A CA    1 
ATOM   102  C  C     . ARG A 1 40  ? 20.466  -8.483  44.736  1.00 60.41  ? 12  ARG A C     1 
ATOM   103  O  O     . ARG A 1 40  ? 19.910  -7.489  45.221  1.00 58.95  ? 12  ARG A O     1 
ATOM   104  C  CB    . ARG A 1 40  ? 22.621  -8.246  43.475  1.00 65.58  ? 12  ARG A CB    1 
ATOM   105  C  CG    . ARG A 1 40  ? 23.024  -7.101  44.394  1.00 64.79  ? 12  ARG A CG    1 
ATOM   106  C  CD    . ARG A 1 40  ? 24.295  -7.391  45.184  1.00 77.57  ? 12  ARG A CD    1 
ATOM   107  N  NE    . ARG A 1 40  ? 24.860  -6.169  45.747  1.00 69.81  ? 12  ARG A NE    1 
ATOM   108  C  CZ    . ARG A 1 40  ? 25.003  -5.945  47.046  1.00 72.69  ? 12  ARG A CZ    1 
ATOM   109  N  NH1   . ARG A 1 40  ? 24.625  -6.839  47.949  1.00 65.75  ? 12  ARG A NH1   1 
ATOM   110  N  NH2   . ARG A 1 40  ? 25.521  -4.788  47.451  1.00 74.24  ? 12  ARG A NH2   1 
ATOM   111  N  N     . PRO A 1 41  ? 20.533  -9.635  45.396  1.00 65.81  ? 13  PRO A N     1 
ATOM   112  C  CA    . PRO A 1 41  ? 20.018  -9.708  46.772  1.00 68.03  ? 13  PRO A CA    1 
ATOM   113  C  C     . PRO A 1 41  ? 20.690  -8.669  47.662  1.00 69.04  ? 13  PRO A C     1 
ATOM   114  O  O     . PRO A 1 41  ? 21.916  -8.549  47.691  1.00 66.87  ? 13  PRO A O     1 
ATOM   115  C  CB    . PRO A 1 41  ? 20.356  -11.138 47.212  1.00 64.97  ? 13  PRO A CB    1 
ATOM   116  C  CG    . PRO A 1 41  ? 20.608  -11.900 45.963  1.00 65.70  ? 13  PRO A CG    1 
ATOM   117  C  CD    . PRO A 1 41  ? 21.026  -10.931 44.899  1.00 66.31  ? 13  PRO A CD    1 
ATOM   118  N  N     . LEU A 1 42  ? 19.867  -7.889  48.363  1.00 56.36  ? 14  LEU A N     1 
ATOM   119  C  CA    . LEU A 1 42  ? 20.330  -6.900  49.329  1.00 53.03  ? 14  LEU A CA    1 
ATOM   120  C  C     . LEU A 1 42  ? 19.786  -7.284  50.696  1.00 54.64  ? 14  LEU A C     1 
ATOM   121  O  O     . LEU A 1 42  ? 18.586  -7.553  50.835  1.00 57.46  ? 14  LEU A O     1 
ATOM   122  C  CB    . LEU A 1 42  ? 19.864  -5.490  48.950  1.00 50.74  ? 14  LEU A CB    1 
ATOM   123  C  CG    . LEU A 1 42  ? 20.298  -4.911  47.603  1.00 56.91  ? 14  LEU A CG    1 
ATOM   124  C  CD1   . LEU A 1 42  ? 19.669  -3.537  47.374  1.00 52.76  ? 14  LEU A CD1   1 
ATOM   125  C  CD2   . LEU A 1 42  ? 21.813  -4.832  47.496  1.00 60.92  ? 14  LEU A CD2   1 
ATOM   126  N  N     . SER A 1 43  ? 20.660  -7.319  51.697  1.00 49.09  ? 15  SER A N     1 
ATOM   127  C  CA    . SER A 1 43  ? 20.241  -7.668  53.044  1.00 52.77  ? 15  SER A CA    1 
ATOM   128  C  C     . SER A 1 43  ? 19.610  -6.461  53.743  1.00 53.47  ? 15  SER A C     1 
ATOM   129  O  O     . SER A 1 43  ? 19.748  -5.310  53.313  1.00 50.13  ? 15  SER A O     1 
ATOM   130  C  CB    . SER A 1 43  ? 21.425  -8.195  53.854  1.00 55.24  ? 15  SER A CB    1 
ATOM   131  O  OG    . SER A 1 43  ? 22.205  -7.127  54.371  1.00 60.86  ? 15  SER A OG    1 
ATOM   132  N  N     . GLY A 1 44  ? 18.923  -6.741  54.857  1.00 49.40  ? 16  GLY A N     1 
ATOM   133  C  CA    . GLY A 1 44  ? 18.259  -5.680  55.596  1.00 53.60  ? 16  GLY A CA    1 
ATOM   134  C  C     . GLY A 1 44  ? 19.212  -4.618  56.107  1.00 53.66  ? 16  GLY A C     1 
ATOM   135  O  O     . GLY A 1 44  ? 18.842  -3.444  56.205  1.00 49.07  ? 16  GLY A O     1 
ATOM   136  N  N     . ASP A 1 45  ? 20.448  -5.007  56.442  1.00 56.24  ? 17  ASP A N     1 
ATOM   137  C  CA    . ASP A 1 45  ? 21.412  -4.024  56.929  1.00 56.31  ? 17  ASP A CA    1 
ATOM   138  C  C     . ASP A 1 45  ? 21.915  -3.129  55.806  1.00 52.45  ? 17  ASP A C     1 
ATOM   139  O  O     . ASP A 1 45  ? 22.171  -1.938  56.032  1.00 52.16  ? 17  ASP A O     1 
ATOM   140  C  CB    . ASP A 1 45  ? 22.584  -4.719  57.624  1.00 60.05  ? 17  ASP A CB    1 
ATOM   141  C  CG    . ASP A 1 45  ? 22.271  -5.087  59.061  1.00 71.49  ? 17  ASP A CG    1 
ATOM   142  O  OD1   . ASP A 1 45  ? 21.149  -4.780  59.524  1.00 78.99  ? 17  ASP A OD1   1 
ATOM   143  O  OD2   . ASP A 1 45  ? 23.147  -5.671  59.733  1.00 85.56  ? 17  ASP A OD2   1 
ATOM   144  N  N     . GLU A 1 46  ? 22.071  -3.671  54.594  1.00 42.56  ? 18  GLU A N     1 
ATOM   145  C  CA    . GLU A 1 46  ? 22.455  -2.822  53.474  1.00 42.02  ? 18  GLU A CA    1 
ATOM   146  C  C     . GLU A 1 46  ? 21.356  -1.824  53.131  1.00 38.16  ? 18  GLU A C     1 
ATOM   147  O  O     . GLU A 1 46  ? 21.648  -0.705  52.696  1.00 42.22  ? 18  GLU A O     1 
ATOM   148  C  CB    . GLU A 1 46  ? 22.784  -3.672  52.245  1.00 51.58  ? 18  GLU A CB    1 
ATOM   149  C  CG    . GLU A 1 46  ? 24.044  -4.516  52.367  1.00 56.52  ? 18  GLU A CG    1 
ATOM   150  C  CD    . GLU A 1 46  ? 24.172  -5.500  51.221  1.00 64.89  ? 18  GLU A CD    1 
ATOM   151  O  OE1   . GLU A 1 46  ? 23.454  -6.522  51.245  1.00 62.24  ? 18  GLU A OE1   1 
ATOM   152  O  OE2   . GLU A 1 46  ? 24.974  -5.244  50.294  1.00 70.71  ? 18  GLU A OE2   1 
ATOM   153  N  N     . ILE A 1 47  ? 20.091  -2.223  53.286  1.00 45.51  ? 19  ILE A N     1 
ATOM   154  C  CA    . ILE A 1 47  ? 18.990  -1.298  53.030  1.00 40.67  ? 19  ILE A CA    1 
ATOM   155  C  C     . ILE A 1 47  ? 18.962  -0.207  54.098  1.00 41.80  ? 19  ILE A C     1 
ATOM   156  O  O     . ILE A 1 47  ? 18.782  0.978   53.797  1.00 39.51  ? 19  ILE A O     1 
ATOM   157  C  CB    . ILE A 1 47  ? 17.661  -2.071  52.958  1.00 42.08  ? 19  ILE A CB    1 
ATOM   158  C  CG1   . ILE A 1 47  ? 17.576  -2.857  51.646  1.00 45.70  ? 19  ILE A CG1   1 
ATOM   159  C  CG2   . ILE A 1 47  ? 16.473  -1.133  53.071  1.00 38.64  ? 19  ILE A CG2   1 
ATOM   160  C  CD1   . ILE A 1 47  ? 16.706  -4.081  51.766  1.00 51.32  ? 19  ILE A CD1   1 
ATOM   161  N  N     . GLU A 1 48  ? 19.177  -0.587  55.358  1.00 41.05  ? 20  GLU A N     1 
ATOM   162  C  CA    . GLU A 1 48  ? 19.237  0.399   56.431  1.00 41.90  ? 20  GLU A CA    1 
ATOM   163  C  C     . GLU A 1 48  ? 20.376  1.392   56.196  1.00 46.70  ? 20  GLU A C     1 
ATOM   164  O  O     . GLU A 1 48  ? 20.227  2.596   56.449  1.00 43.42  ? 20  GLU A O     1 
ATOM   165  C  CB    . GLU A 1 48  ? 19.380  -0.344  57.761  1.00 49.37  ? 20  GLU A CB    1 
ATOM   166  C  CG    . GLU A 1 48  ? 19.771  0.481   58.965  1.00 60.08  ? 20  GLU A CG    1 
ATOM   167  C  CD    . GLU A 1 48  ? 20.211  -0.405  60.122  1.00 67.04  ? 20  GLU A CD    1 
ATOM   168  O  OE1   . GLU A 1 48  ? 21.270  -1.060  60.005  1.00 74.66  ? 20  GLU A OE1   1 
ATOM   169  O  OE2   . GLU A 1 48  ? 19.481  -0.475  61.131  1.00 74.11  ? 20  GLU A OE2   1 
ATOM   170  N  N     . ALA A 1 49  ? 21.495  0.914   55.643  1.00 43.83  ? 21  ALA A N     1 
ATOM   171  C  CA    . ALA A 1 49  ? 22.638  1.782   55.369  1.00 46.11  ? 21  ALA A CA    1 
ATOM   172  C  C     . ALA A 1 49  ? 22.347  2.764   54.238  1.00 41.05  ? 21  ALA A C     1 
ATOM   173  O  O     . ALA A 1 49  ? 22.756  3.929   54.309  1.00 44.08  ? 21  ALA A O     1 
ATOM   174  C  CB    . ALA A 1 49  ? 23.872  0.934   55.044  1.00 47.95  ? 21  ALA A CB    1 
ATOM   175  N  N     . ILE A 1 50  ? 21.666  2.309   53.174  1.00 39.69  ? 22  ILE A N     1 
ATOM   176  C  CA    . ILE A 1 50  ? 21.280  3.210   52.084  1.00 39.08  ? 22  ILE A CA    1 
ATOM   177  C  C     . ILE A 1 50  ? 20.386  4.321   52.615  1.00 39.73  ? 22  ILE A C     1 
ATOM   178  O  O     . ILE A 1 50  ? 20.506  5.491   52.220  1.00 42.11  ? 22  ILE A O     1 
ATOM   179  C  CB    . ILE A 1 50  ? 20.577  2.424   50.955  1.00 42.48  ? 22  ILE A CB    1 
ATOM   180  C  CG1   . ILE A 1 50  ? 21.560  1.498   50.226  1.00 46.53  ? 22  ILE A CG1   1 
ATOM   181  C  CG2   . ILE A 1 50  ? 19.870  3.377   49.958  1.00 42.09  ? 22  ILE A CG2   1 
ATOM   182  C  CD1   . ILE A 1 50  ? 20.907  0.611   49.198  1.00 51.97  ? 22  ILE A CD1   1 
ATOM   183  N  N     . GLY A 1 51  ? 19.455  3.968   53.501  1.00 40.61  ? 23  GLY A N     1 
ATOM   184  C  CA    . GLY A 1 51  ? 18.562  4.972   54.043  1.00 37.17  ? 23  GLY A CA    1 
ATOM   185  C  C     . GLY A 1 51  ? 19.293  5.975   54.915  1.00 38.52  ? 23  GLY A C     1 
ATOM   186  O  O     . GLY A 1 51  ? 19.019  7.178   54.854  1.00 38.24  ? 23  GLY A O     1 
ATOM   187  N  N     . ARG A 1 52  ? 20.238  5.501   55.733  1.00 38.14  ? 24  ARG A N     1 
ATOM   188  C  CA    . ARG A 1 52  ? 20.905  6.425   56.653  1.00 36.04  ? 24  ARG A CA    1 
ATOM   189  C  C     . ARG A 1 52  ? 21.843  7.369   55.906  1.00 35.35  ? 24  ARG A C     1 
ATOM   190  O  O     . ARG A 1 52  ? 21.905  8.561   56.222  1.00 39.33  ? 24  ARG A O     1 
ATOM   191  C  CB    . ARG A 1 52  ? 21.636  5.659   57.768  1.00 46.02  ? 24  ARG A CB    1 
ATOM   192  C  CG    . ARG A 1 52  ? 20.669  5.058   58.836  1.00 49.70  ? 24  ARG A CG    1 
ATOM   193  C  CD    . ARG A 1 52  ? 21.349  4.660   60.186  1.00 65.14  ? 24  ARG A CD    1 
ATOM   194  N  NE    . ARG A 1 52  ? 21.569  5.794   61.088  1.00 51.42  ? 24  ARG A NE    1 
ATOM   195  C  CZ    . ARG A 1 52  ? 22.734  6.418   61.233  1.00 50.67  ? 24  ARG A CZ    1 
ATOM   196  N  NH1   . ARG A 1 52  ? 23.832  5.981   60.634  1.00 48.05  ? 24  ARG A NH1   1 
ATOM   197  N  NH2   . ARG A 1 52  ? 22.794  7.524   61.974  1.00 41.09  ? 24  ARG A NH2   1 
ATOM   198  N  N     . ILE A 1 53  ? 22.561  6.871   54.901  1.00 35.55  ? 25  ILE A N     1 
ATOM   199  C  CA    . ILE A 1 53  ? 23.386  7.751   54.081  1.00 41.03  ? 25  ILE A CA    1 
ATOM   200  C  C     . ILE A 1 53  ? 22.515  8.719   53.287  1.00 44.93  ? 25  ILE A C     1 
ATOM   201  O  O     . ILE A 1 53  ? 22.852  9.899   53.145  1.00 38.82  ? 25  ILE A O     1 
ATOM   202  C  CB    . ILE A 1 53  ? 24.314  6.922   53.171  1.00 47.76  ? 25  ILE A CB    1 
ATOM   203  C  CG1   . ILE A 1 53  ? 25.336  6.175   54.022  1.00 56.55  ? 25  ILE A CG1   1 
ATOM   204  C  CG2   . ILE A 1 53  ? 25.057  7.821   52.188  1.00 51.62  ? 25  ILE A CG2   1 
ATOM   205  C  CD1   . ILE A 1 53  ? 26.055  5.079   53.294  1.00 57.45  ? 25  ILE A CD1   1 
ATOM   206  N  N     . SER A 1 54  ? 21.361  8.257   52.786  1.00 36.54  ? 26  SER A N     1 
ATOM   207  C  CA    . SER A 1 54  ? 20.487  9.173   52.046  1.00 32.31  ? 26  SER A CA    1 
ATOM   208  C  C     . SER A 1 54  ? 19.948  10.270  52.948  1.00 33.71  ? 26  SER A C     1 
ATOM   209  O  O     . SER A 1 54  ? 19.789  11.417  52.514  1.00 40.03  ? 26  SER A O     1 
ATOM   210  C  CB    . SER A 1 54  ? 19.319  8.418   51.407  1.00 35.62  ? 26  SER A CB    1 
ATOM   211  O  OG    . SER A 1 54  ? 19.798  7.397   50.544  1.00 37.84  ? 26  SER A OG    1 
ATOM   212  N  N     . SER A 1 55  ? 19.627  9.929   54.201  1.00 34.88  ? 27  SER A N     1 
ATOM   213  C  CA    . SER A 1 55  ? 19.122  10.947  55.113  1.00 34.32  ? 27  SER A CA    1 
ATOM   214  C  C     . SER A 1 55  ? 20.171  12.031  55.356  1.00 36.40  ? 27  SER A C     1 
ATOM   215  O  O     . SER A 1 55  ? 19.848  13.227  55.369  1.00 37.37  ? 27  SER A O     1 
ATOM   216  C  CB    . SER A 1 55  ? 18.686  10.307  56.434  1.00 33.98  ? 27  SER A CB    1 
ATOM   217  O  OG    . SER A 1 55  ? 18.161  11.298  57.309  1.00 35.30  ? 27  SER A OG    1 
ATOM   218  N  N     . GLN A 1 56  ? 21.437  11.632  55.510  1.00 36.55  ? 28  GLN A N     1 
ATOM   219  C  CA    . GLN A 1 56  ? 22.498  12.601  55.797  1.00 34.34  ? 28  GLN A CA    1 
ATOM   220  C  C     . GLN A 1 56  ? 22.717  13.544  54.614  1.00 40.35  ? 28  GLN A C     1 
ATOM   221  O  O     . GLN A 1 56  ? 22.749  14.770  54.779  1.00 41.17  ? 28  GLN A O     1 
ATOM   222  C  CB    . GLN A 1 56  ? 23.785  11.851  56.156  1.00 37.45  ? 28  GLN A CB    1 
ATOM   223  C  CG    . GLN A 1 56  ? 25.024  12.722  56.360  1.00 37.79  ? 28  GLN A CG    1 
ATOM   224  C  CD    . GLN A 1 56  ? 26.277  11.880  56.518  1.00 51.35  ? 28  GLN A CD    1 
ATOM   225  O  OE1   . GLN A 1 56  ? 26.654  11.132  55.615  1.00 54.53  ? 28  GLN A OE1   1 
ATOM   226  N  NE2   . GLN A 1 56  ? 26.912  11.976  57.683  1.00 52.81  ? 28  GLN A NE2   1 
ATOM   227  N  N     . LYS A 1 57  ? 22.834  12.987  53.403  1.00 38.21  ? 29  LYS A N     1 
ATOM   228  C  CA    . LYS A 1 57  ? 23.069  13.815  52.220  1.00 38.09  ? 29  LYS A CA    1 
ATOM   229  C  C     . LYS A 1 57  ? 21.864  14.688  51.896  1.00 45.30  ? 29  LYS A C     1 
ATOM   230  O  O     . LYS A 1 57  ? 22.023  15.846  51.490  1.00 40.91  ? 29  LYS A O     1 
ATOM   231  C  CB    . LYS A 1 57  ? 23.428  12.923  51.028  1.00 42.31  ? 29  LYS A CB    1 
ATOM   232  C  CG    . LYS A 1 57  ? 24.814  12.319  51.129  1.00 51.47  ? 29  LYS A CG    1 
ATOM   233  C  CD    . LYS A 1 57  ? 24.927  11.040  50.332  1.00 55.95  ? 29  LYS A CD    1 
ATOM   234  C  CE    . LYS A 1 57  ? 26.106  11.115  49.391  1.00 73.04  ? 29  LYS A CE    1 
ATOM   235  N  NZ    . LYS A 1 57  ? 25.977  12.255  48.445  1.00 78.66  ? 29  LYS A NZ    1 
ATOM   236  N  N     . ASN A 1 58  ? 20.646  14.161  52.074  1.00 37.34  ? 30  ASN A N     1 
ATOM   237  C  CA    . ASN A 1 58  ? 19.478  14.965  51.757  1.00 33.34  ? 30  ASN A CA    1 
ATOM   238  C  C     . ASN A 1 58  ? 19.361  16.161  52.687  1.00 39.87  ? 30  ASN A C     1 
ATOM   239  O  O     . ASN A 1 58  ? 18.987  17.250  52.242  1.00 38.95  ? 30  ASN A O     1 
ATOM   240  C  CB    . ASN A 1 58  ? 18.204  14.115  51.798  1.00 34.25  ? 30  ASN A CB    1 
ATOM   241  C  CG    . ASN A 1 58  ? 18.070  13.218  50.576  1.00 37.51  ? 30  ASN A CG    1 
ATOM   242  O  OD1   . ASN A 1 58  ? 18.920  13.247  49.691  1.00 42.52  ? 30  ASN A OD1   1 
ATOM   243  N  ND2   . ASN A 1 58  ? 16.997  12.398  50.529  1.00 35.82  ? 30  ASN A ND2   1 
ATOM   244  N  N     . GLN A 1 59  ? 19.653  15.977  53.982  1.00 34.83  ? 31  GLN A N     1 
ATOM   245  C  CA    . GLN A 1 59  ? 19.576  17.091  54.929  1.00 40.87  ? 31  GLN A CA    1 
ATOM   246  C  C     . GLN A 1 59  ? 20.475  18.249  54.506  1.00 43.12  ? 31  GLN A C     1 
ATOM   247  O  O     . GLN A 1 59  ? 20.100  19.416  54.664  1.00 44.08  ? 31  GLN A O     1 
ATOM   248  C  CB    . GLN A 1 59  ? 19.947  16.620  56.339  1.00 37.76  ? 31  GLN A CB    1 
ATOM   249  C  CG    . GLN A 1 59  ? 19.771  17.660  57.477  1.00 46.17  ? 31  GLN A CG    1 
ATOM   250  C  CD    . GLN A 1 59  ? 20.897  18.696  57.555  1.00 56.52  ? 31  GLN A CD    1 
ATOM   251  O  OE1   . GLN A 1 59  ? 22.053  18.386  57.259  1.00 49.54  ? 31  GLN A OE1   1 
ATOM   252  N  NE2   . GLN A 1 59  ? 20.563  19.924  57.966  1.00 56.78  ? 31  GLN A NE2   1 
ATOM   253  N  N     . GLN A 1 60  ? 21.670  17.948  53.990  1.00 44.30  ? 32  GLN A N     1 
ATOM   254  C  CA    . GLN A 1 60  ? 22.571  19.010  53.537  1.00 47.55  ? 32  GLN A CA    1 
ATOM   255  C  C     . GLN A 1 60  ? 22.074  19.681  52.259  1.00 57.20  ? 32  GLN A C     1 
ATOM   256  O  O     . GLN A 1 60  ? 22.531  20.781  51.936  1.00 54.74  ? 32  GLN A O     1 
ATOM   257  C  CB    . GLN A 1 60  ? 23.986  18.466  53.295  1.00 42.85  ? 32  GLN A CB    1 
ATOM   258  C  CG    . GLN A 1 60  ? 24.681  17.906  54.550  1.00 50.90  ? 32  GLN A CG    1 
ATOM   259  C  CD    . GLN A 1 60  ? 25.312  18.976  55.444  1.00 61.79  ? 32  GLN A CD    1 
ATOM   260  O  OE1   . GLN A 1 60  ? 24.772  19.305  56.512  1.00 63.37  ? 32  GLN A OE1   1 
ATOM   261  N  NE2   . GLN A 1 60  ? 26.458  19.508  55.027  1.00 60.68  ? 32  GLN A NE2   1 
ATOM   262  N  N     . ALA A 1 61  ? 21.159  19.046  51.526  1.00 44.12  ? 33  ALA A N     1 
ATOM   263  C  CA    . ALA A 1 61  ? 20.632  19.584  50.277  1.00 43.36  ? 33  ALA A CA    1 
ATOM   264  C  C     . ALA A 1 61  ? 19.220  20.148  50.406  1.00 48.05  ? 33  ALA A C     1 
ATOM   265  O  O     . ALA A 1 61  ? 18.681  20.647  49.411  1.00 50.41  ? 33  ALA A O     1 
ATOM   266  C  CB    . ALA A 1 61  ? 20.655  18.502  49.194  1.00 49.25  ? 33  ALA A CB    1 
ATOM   267  N  N     . ASN A 1 62  ? 18.609  20.085  51.600  1.00 43.86  ? 34  ASN A N     1 
ATOM   268  C  CA    . ASN A 1 62  ? 17.228  20.542  51.829  1.00 45.47  ? 34  ASN A CA    1 
ATOM   269  C  C     . ASN A 1 62  ? 16.196  19.709  51.068  1.00 44.94  ? 34  ASN A C     1 
ATOM   270  O  O     . ASN A 1 62  ? 15.179  20.240  50.616  1.00 46.33  ? 34  ASN A O     1 
ATOM   271  C  CB    . ASN A 1 62  ? 17.049  22.021  51.485  1.00 54.73  ? 34  ASN A CB    1 
ATOM   272  C  CG    . ASN A 1 62  ? 16.004  22.691  52.341  1.00 58.11  ? 34  ASN A CG    1 
ATOM   273  O  OD1   . ASN A 1 62  ? 15.797  22.322  53.492  1.00 69.00  ? 34  ASN A OD1   1 
ATOM   274  N  ND2   . ASN A 1 62  ? 15.317  23.674  51.770  1.00 65.55  ? 34  ASN A ND2   1 
ATOM   275  N  N     . VAL A 1 63  ? 16.446  18.406  50.943  1.00 42.75  ? 35  VAL A N     1 
ATOM   276  C  CA    . VAL A 1 63  ? 15.562  17.472  50.245  1.00 38.83  ? 35  VAL A CA    1 
ATOM   277  C  C     . VAL A 1 63  ? 14.907  16.556  51.275  1.00 43.00  ? 35  VAL A C     1 
ATOM   278  O  O     . VAL A 1 63  ? 15.547  16.186  52.265  1.00 36.20  ? 35  VAL A O     1 
ATOM   279  C  CB    . VAL A 1 63  ? 16.371  16.676  49.201  1.00 42.53  ? 35  VAL A CB    1 
ATOM   280  C  CG1   . VAL A 1 63  ? 15.685  15.361  48.803  1.00 40.78  ? 35  VAL A CG1   1 
ATOM   281  C  CG2   . VAL A 1 63  ? 16.627  17.546  47.963  1.00 48.74  ? 35  VAL A CG2   1 
ATOM   282  N  N     . THR A 1 64  ? 13.631  16.203  51.056  1.00 35.14  ? 36  THR A N     1 
ATOM   283  C  CA    . THR A 1 64  ? 12.889  15.324  51.973  1.00 34.29  ? 36  THR A CA    1 
ATOM   284  C  C     . THR A 1 64  ? 12.245  14.185  51.175  1.00 36.88  ? 36  THR A C     1 
ATOM   285  O  O     . THR A 1 64  ? 12.271  14.185  49.942  1.00 37.20  ? 36  THR A O     1 
ATOM   286  C  CB    . THR A 1 64  ? 11.832  16.101  52.781  1.00 35.05  ? 36  THR A CB    1 
ATOM   287  O  OG1   . THR A 1 64  ? 10.991  16.886  51.911  1.00 37.20  ? 36  THR A OG1   1 
ATOM   288  C  CG2   . THR A 1 64  ? 12.510  17.033  53.827  1.00 35.38  ? 36  THR A CG2   1 
ATOM   289  N  N     . GLY A 1 65  ? 11.689  13.178  51.860  1.00 33.73  ? 37  GLY A N     1 
ATOM   290  C  CA    . GLY A 1 65  ? 11.000  12.104  51.138  1.00 33.97  ? 37  GLY A CA    1 
ATOM   291  C  C     . GLY A 1 65  ? 10.977  10.797  51.927  1.00 38.05  ? 37  GLY A C     1 
ATOM   292  O  O     . GLY A 1 65  ? 11.261  10.771  53.126  1.00 36.21  ? 37  GLY A O     1 
ATOM   293  N  N     . VAL A 1 66  ? 10.645  9.706   51.223  1.00 31.43  ? 38  VAL A N     1 
ATOM   294  C  CA    . VAL A 1 66  ? 10.459  8.395   51.849  1.00 30.17  ? 38  VAL A CA    1 
ATOM   295  C  C     . VAL A 1 66  ? 10.937  7.303   50.895  1.00 37.82  ? 38  VAL A C     1 
ATOM   296  O  O     . VAL A 1 66  ? 10.822  7.432   49.675  1.00 34.49  ? 38  VAL A O     1 
ATOM   297  C  CB    . VAL A 1 66  ? 8.979   8.175   52.276  1.00 32.82  ? 38  VAL A CB    1 
ATOM   298  C  CG1   . VAL A 1 66  ? 8.013   8.146   51.072  1.00 36.41  ? 38  VAL A CG1   1 
ATOM   299  C  CG2   . VAL A 1 66  ? 8.807   6.897   53.131  1.00 31.48  ? 38  VAL A CG2   1 
ATOM   300  N  N     . LEU A 1 67  ? 11.467  6.214   51.466  1.00 31.67  ? 39  LEU A N     1 
ATOM   301  C  CA    . LEU A 1 67  ? 11.966  5.060   50.706  1.00 32.67  ? 39  LEU A CA    1 
ATOM   302  C  C     . LEU A 1 67  ? 11.342  3.796   51.288  1.00 34.04  ? 39  LEU A C     1 
ATOM   303  O  O     . LEU A 1 67  ? 11.397  3.584   52.505  1.00 34.07  ? 39  LEU A O     1 
ATOM   304  C  CB    . LEU A 1 67  ? 13.505  4.988   50.755  1.00 35.35  ? 39  LEU A CB    1 
ATOM   305  C  CG    . LEU A 1 67  ? 14.219  3.738   50.206  1.00 37.35  ? 39  LEU A CG    1 
ATOM   306  C  CD1   . LEU A 1 67  ? 14.082  3.718   48.696  1.00 40.46  ? 39  LEU A CD1   1 
ATOM   307  C  CD2   . LEU A 1 67  ? 15.716  3.678   50.629  1.00 34.47  ? 39  LEU A CD2   1 
ATOM   308  N  N     . LEU A 1 68  ? 10.723  2.966   50.429  1.00 33.74  ? 40  LEU A N     1 
ATOM   309  C  CA    . LEU A 1 68  ? 10.100  1.716   50.868  1.00 31.80  ? 40  LEU A CA    1 
ATOM   310  C  C     . LEU A 1 68  ? 10.641  0.557   50.045  1.00 35.78  ? 40  LEU A C     1 
ATOM   311  O  O     . LEU A 1 68  ? 10.983  0.722   48.872  1.00 37.97  ? 40  LEU A O     1 
ATOM   312  C  CB    . LEU A 1 68  ? 8.574   1.758   50.719  1.00 33.79  ? 40  LEU A CB    1 
ATOM   313  C  CG    . LEU A 1 68  ? 7.877   2.874   51.494  1.00 41.65  ? 40  LEU A CG    1 
ATOM   314  C  CD1   . LEU A 1 68  ? 7.710   4.065   50.591  1.00 43.87  ? 40  LEU A CD1   1 
ATOM   315  C  CD2   . LEU A 1 68  ? 6.525   2.391   52.007  1.00 48.61  ? 40  LEU A CD2   1 
ATOM   316  N  N     . CYS A 1 69  ? 10.720  -0.620  50.659  1.00 36.94  ? 41  CYS A N     1 
ATOM   317  C  CA    . CYS A 1 69  ? 11.083  -1.817  49.907  1.00 38.25  ? 41  CYS A CA    1 
ATOM   318  C  C     . CYS A 1 69  ? 10.160  -2.978  50.257  1.00 37.33  ? 41  CYS A C     1 
ATOM   319  O  O     . CYS A 1 69  ? 9.633   -3.073  51.372  1.00 34.15  ? 41  CYS A O     1 
ATOM   320  C  CB    . CYS A 1 69  ? 12.573  -2.199  50.118  1.00 39.83  ? 41  CYS A CB    1 
ATOM   321  S  SG    . CYS A 1 69  ? 13.011  -2.807  51.743  1.00 44.34  ? 41  CYS A SG    1 
ATOM   322  N  N     . LEU A 1 70  ? 9.932   -3.836  49.264  1.00 35.21  ? 42  LEU A N     1 
ATOM   323  C  CA    . LEU A 1 70  ? 9.065   -5.006  49.418  1.00 36.41  ? 42  LEU A CA    1 
ATOM   324  C  C     . LEU A 1 70  ? 9.484   -6.016  48.359  1.00 40.56  ? 42  LEU A C     1 
ATOM   325  O  O     . LEU A 1 70  ? 9.459   -5.688  47.173  1.00 40.32  ? 42  LEU A O     1 
ATOM   326  C  CB    . LEU A 1 70  ? 7.584   -4.623  49.256  1.00 39.11  ? 42  LEU A CB    1 
ATOM   327  C  CG    . LEU A 1 70  ? 6.565   -5.768  49.271  1.00 40.97  ? 42  LEU A CG    1 
ATOM   328  C  CD1   . LEU A 1 70  ? 6.523   -6.393  50.648  1.00 43.23  ? 42  LEU A CD1   1 
ATOM   329  C  CD2   . LEU A 1 70  ? 5.207   -5.219  48.888  1.00 40.66  ? 42  LEU A CD2   1 
ATOM   330  N  N     . ASP A 1 71  ? 9.930   -7.198  48.787  1.00 40.76  ? 43  ASP A N     1 
ATOM   331  C  CA    . ASP A 1 71  ? 10.171  -8.334  47.888  1.00 52.33  ? 43  ASP A CA    1 
ATOM   332  C  C     . ASP A 1 71  ? 11.005  -7.946  46.657  1.00 49.24  ? 43  ASP A C     1 
ATOM   333  O  O     . ASP A 1 71  ? 10.668  -8.273  45.515  1.00 51.98  ? 43  ASP A O     1 
ATOM   334  C  CB    . ASP A 1 71  ? 8.833   -8.958  47.471  1.00 53.87  ? 43  ASP A CB    1 
ATOM   335  C  CG    . ASP A 1 71  ? 8.968   -10.406 47.025  1.00 67.60  ? 43  ASP A CG    1 
ATOM   336  O  OD1   . ASP A 1 71  ? 9.457   -11.240 47.821  1.00 68.33  ? 43  ASP A OD1   1 
ATOM   337  O  OD2   . ASP A 1 71  ? 8.584   -10.705 45.872  1.00 76.15  ? 43  ASP A OD2   1 
ATOM   338  N  N     . GLY A 1 72  ? 12.112  -7.236  46.889  1.00 44.70  ? 44  GLY A N     1 
ATOM   339  C  CA    . GLY A 1 72  ? 13.008  -6.898  45.793  1.00 42.76  ? 44  GLY A CA    1 
ATOM   340  C  C     . GLY A 1 72  ? 12.590  -5.735  44.920  1.00 46.31  ? 44  GLY A C     1 
ATOM   341  O  O     . GLY A 1 72  ? 13.145  -5.574  43.825  1.00 44.28  ? 44  GLY A O     1 
ATOM   342  N  N     . ILE A 1 73  ? 11.644  -4.905  45.377  1.00 43.33  ? 45  ILE A N     1 
ATOM   343  C  CA    . ILE A 1 73  ? 11.197  -3.689  44.695  1.00 37.00  ? 45  ILE A CA    1 
ATOM   344  C  C     . ILE A 1 73  ? 11.488  -2.491  45.591  1.00 38.09  ? 45  ILE A C     1 
ATOM   345  O  O     . ILE A 1 73  ? 11.238  -2.549  46.800  1.00 37.49  ? 45  ILE A O     1 
ATOM   346  C  CB    . ILE A 1 73  ? 9.678   -3.743  44.393  1.00 45.12  ? 45  ILE A CB    1 
ATOM   347  C  CG1   . ILE A 1 73  ? 9.301   -5.010  43.621  1.00 51.66  ? 45  ILE A CG1   1 
ATOM   348  C  CG2   . ILE A 1 73  ? 9.164   -2.441  43.744  1.00 39.49  ? 45  ILE A CG2   1 
ATOM   349  C  CD1   . ILE A 1 73  ? 8.013   -5.640  44.134  1.00 53.91  ? 45  ILE A CD1   1 
ATOM   350  N  N     . PHE A 1 74  ? 11.999  -1.407  45.007  1.00 36.33  ? 46  PHE A N     1 
ATOM   351  C  CA    . PHE A 1 74  ? 12.124  -0.128  45.702  1.00 39.64  ? 46  PHE A CA    1 
ATOM   352  C  C     . PHE A 1 74  ? 11.001  0.791   45.236  1.00 43.21  ? 46  PHE A C     1 
ATOM   353  O  O     . PHE A 1 74  ? 10.652  0.798   44.049  1.00 37.65  ? 46  PHE A O     1 
ATOM   354  C  CB    . PHE A 1 74  ? 13.451  0.580   45.398  1.00 36.26  ? 46  PHE A CB    1 
ATOM   355  C  CG    . PHE A 1 74  ? 14.655  0.070   46.180  1.00 42.95  ? 46  PHE A CG    1 
ATOM   356  C  CD1   . PHE A 1 74  ? 14.699  0.126   47.563  1.00 39.52  ? 46  PHE A CD1   1 
ATOM   357  C  CD2   . PHE A 1 74  ? 15.771  -0.404  45.498  1.00 41.85  ? 46  PHE A CD2   1 
ATOM   358  C  CE1   . PHE A 1 74  ? 15.830  -0.310  48.262  1.00 47.59  ? 46  PHE A CE1   1 
ATOM   359  C  CE2   . PHE A 1 74  ? 16.908  -0.839  46.186  1.00 44.65  ? 46  PHE A CE2   1 
ATOM   360  C  CZ    . PHE A 1 74  ? 16.932  -0.796  47.570  1.00 45.62  ? 46  PHE A CZ    1 
ATOM   361  N  N     . PHE A 1 75  ? 10.457  1.582   46.170  1.00 35.87  ? 47  PHE A N     1 
ATOM   362  C  CA    . PHE A 1 75  ? 9.585   2.717   45.870  1.00 35.58  ? 47  PHE A CA    1 
ATOM   363  C  C     . PHE A 1 75  ? 10.167  3.950   46.556  1.00 37.07  ? 47  PHE A C     1 
ATOM   364  O  O     . PHE A 1 75  ? 10.449  3.893   47.757  1.00 35.47  ? 47  PHE A O     1 
ATOM   365  C  CB    . PHE A 1 75  ? 8.142   2.529   46.408  1.00 34.77  ? 47  PHE A CB    1 
ATOM   366  C  CG    . PHE A 1 75  ? 7.521   1.149   46.175  1.00 35.07  ? 47  PHE A CG    1 
ATOM   367  C  CD1   . PHE A 1 75  ? 7.858   0.060   46.969  1.00 36.32  ? 47  PHE A CD1   1 
ATOM   368  C  CD2   . PHE A 1 75  ? 6.551   0.980   45.201  1.00 39.72  ? 47  PHE A CD2   1 
ATOM   369  C  CE1   . PHE A 1 75  ? 7.265   -1.190  46.766  1.00 42.77  ? 47  PHE A CE1   1 
ATOM   370  C  CE2   . PHE A 1 75  ? 5.951   -0.258  44.995  1.00 40.46  ? 47  PHE A CE2   1 
ATOM   371  C  CZ    . PHE A 1 75  ? 6.307   -1.342  45.783  1.00 42.12  ? 47  PHE A CZ    1 
ATOM   372  N  N     . GLN A 1 76  ? 10.293  5.077   45.841  1.00 32.36  ? 48  GLN A N     1 
ATOM   373  C  CA    . GLN A 1 76  ? 10.791  6.294   46.492  1.00 32.66  ? 48  GLN A CA    1 
ATOM   374  C  C     . GLN A 1 76  ? 10.066  7.555   46.028  1.00 35.75  ? 48  GLN A C     1 
ATOM   375  O  O     . GLN A 1 76  ? 9.716   7.689   44.851  1.00 37.45  ? 48  GLN A O     1 
ATOM   376  C  CB    . GLN A 1 76  ? 12.313  6.475   46.265  1.00 35.60  ? 48  GLN A CB    1 
ATOM   377  C  CG    . GLN A 1 76  ? 12.916  7.609   47.114  1.00 32.88  ? 48  GLN A CG    1 
ATOM   378  C  CD    . GLN A 1 76  ? 14.439  7.629   47.061  1.00 39.08  ? 48  GLN A CD    1 
ATOM   379  O  OE1   . GLN A 1 76  ? 15.036  7.450   45.994  1.00 41.82  ? 48  GLN A OE1   1 
ATOM   380  N  NE2   . GLN A 1 76  ? 15.074  7.841   48.211  1.00 38.19  ? 48  GLN A NE2   1 
ATOM   381  N  N     . ILE A 1 77  ? 9.876   8.493   46.964  1.00 33.74  ? 49  ILE A N     1 
ATOM   382  C  CA    . ILE A 1 77  ? 9.363   9.832   46.690  1.00 34.88  ? 49  ILE A CA    1 
ATOM   383  C  C     . ILE A 1 77  ? 10.402  10.837  47.171  1.00 44.14  ? 49  ILE A C     1 
ATOM   384  O  O     . ILE A 1 77  ? 10.840  10.759  48.323  1.00 37.30  ? 49  ILE A O     1 
ATOM   385  C  CB    . ILE A 1 77  ? 8.014   10.067  47.401  1.00 37.29  ? 49  ILE A CB    1 
ATOM   386  C  CG1   . ILE A 1 77  ? 6.960   9.069   46.901  1.00 38.33  ? 49  ILE A CG1   1 
ATOM   387  C  CG2   . ILE A 1 77  ? 7.565   11.496  47.219  1.00 38.23  ? 49  ILE A CG2   1 
ATOM   388  C  CD1   . ILE A 1 77  ? 5.676   9.015   47.757  1.00 43.20  ? 49  ILE A CD1   1 
ATOM   389  N  N     . LEU A 1 78  ? 10.816  11.763  46.289  1.00 37.69  ? 50  LEU A N     1 
ATOM   390  C  CA    . LEU A 1 78  ? 11.758  12.839  46.623  1.00 40.30  ? 50  LEU A CA    1 
ATOM   391  C  C     . LEU A 1 78  ? 11.152  14.206  46.334  1.00 44.39  ? 50  LEU A C     1 
ATOM   392  O  O     . LEU A 1 78  ? 10.496  14.390  45.303  1.00 42.91  ? 50  LEU A O     1 
ATOM   393  C  CB    . LEU A 1 78  ? 13.088  12.707  45.833  1.00 40.97  ? 50  LEU A CB    1 
ATOM   394  C  CG    . LEU A 1 78  ? 13.883  11.412  45.860  1.00 47.71  ? 50  LEU A CG    1 
ATOM   395  C  CD1   . LEU A 1 78  ? 14.620  11.160  44.549  1.00 55.64  ? 50  LEU A CD1   1 
ATOM   396  C  CD2   . LEU A 1 78  ? 14.901  11.531  46.984  1.00 45.48  ? 50  LEU A CD2   1 
ATOM   397  N  N     . GLU A 1 79  ? 11.395  15.180  47.226  1.00 40.20  ? 51  GLU A N     1 
ATOM   398  C  CA    . GLU A 1 79  ? 10.869  16.533  47.046  1.00 40.33  ? 51  GLU A CA    1 
ATOM   399  C  C     . GLU A 1 79  ? 11.900  17.580  47.445  1.00 46.19  ? 51  GLU A C     1 
ATOM   400  O  O     . GLU A 1 79  ? 12.617  17.433  48.444  1.00 42.55  ? 51  GLU A O     1 
ATOM   401  C  CB    . GLU A 1 79  ? 9.582   16.797  47.849  1.00 45.54  ? 51  GLU A CB    1 
ATOM   402  C  CG    . GLU A 1 79  ? 9.548   16.112  49.180  1.00 51.27  ? 51  GLU A CG    1 
ATOM   403  C  CD    . GLU A 1 79  ? 8.243   16.312  49.941  1.00 46.80  ? 51  GLU A CD    1 
ATOM   404  O  OE1   . GLU A 1 79  ? 7.163   16.455  49.318  1.00 40.91  ? 51  GLU A OE1   1 
ATOM   405  O  OE2   . GLU A 1 79  ? 8.299   16.286  51.188  1.00 40.93  ? 51  GLU A OE2   1 
ATOM   406  N  N     . GLY A 1 80  ? 11.953  18.650  46.663  1.00 44.23  ? 52  GLY A N     1 
ATOM   407  C  CA    . GLY A 1 80  ? 12.813  19.761  47.000  1.00 42.31  ? 52  GLY A CA    1 
ATOM   408  C  C     . GLY A 1 80  ? 12.937  20.723  45.834  1.00 55.70  ? 52  GLY A C     1 
ATOM   409  O  O     . GLY A 1 80  ? 12.160  20.685  44.875  1.00 48.82  ? 52  GLY A O     1 
ATOM   410  N  N     . GLU A 1 81  ? 13.940  21.586  45.949  1.00 51.84  ? 53  GLU A N     1 
ATOM   411  C  CA    . GLU A 1 81  ? 14.260  22.532  44.890  1.00 60.09  ? 53  GLU A CA    1 
ATOM   412  C  C     . GLU A 1 81  ? 14.630  21.791  43.610  1.00 48.82  ? 53  GLU A C     1 
ATOM   413  O  O     . GLU A 1 81  ? 15.347  20.786  43.634  1.00 55.32  ? 53  GLU A O     1 
ATOM   414  C  CB    . GLU A 1 81  ? 15.392  23.444  45.370  1.00 62.18  ? 53  GLU A CB    1 
ATOM   415  C  CG    . GLU A 1 81  ? 16.238  24.127  44.325  1.00 72.52  ? 53  GLU A CG    1 
ATOM   416  C  CD    . GLU A 1 81  ? 17.189  25.126  44.970  1.00 85.42  ? 53  GLU A CD    1 
ATOM   417  O  OE1   . GLU A 1 81  ? 16.733  25.910  45.831  1.00 85.23  ? 53  GLU A OE1   1 
ATOM   418  O  OE2   . GLU A 1 81  ? 18.396  25.104  44.652  1.00 87.31  ? 53  GLU A OE2   1 
ATOM   419  N  N     . ALA A 1 82  ? 14.123  22.298  42.481  1.00 55.83  ? 54  ALA A N     1 
ATOM   420  C  CA    . ALA A 1 82  ? 14.198  21.561  41.223  1.00 50.37  ? 54  ALA A CA    1 
ATOM   421  C  C     . ALA A 1 82  ? 15.630  21.179  40.853  1.00 54.15  ? 54  ALA A C     1 
ATOM   422  O  O     . ALA A 1 82  ? 15.880  20.038  40.444  1.00 54.93  ? 54  ALA A O     1 
ATOM   423  C  CB    . ALA A 1 82  ? 13.550  22.378  40.103  1.00 59.57  ? 54  ALA A CB    1 
ATOM   424  N  N     . GLU A 1 83  ? 16.592  22.104  40.987  1.00 61.72  ? 55  GLU A N     1 
ATOM   425  C  CA    . GLU A 1 83  ? 17.947  21.781  40.535  1.00 60.48  ? 55  GLU A CA    1 
ATOM   426  C  C     . GLU A 1 83  ? 18.579  20.706  41.414  1.00 60.71  ? 55  GLU A C     1 
ATOM   427  O  O     . GLU A 1 83  ? 19.318  19.846  40.919  1.00 65.49  ? 55  GLU A O     1 
ATOM   428  C  CB    . GLU A 1 83  ? 18.860  23.014  40.511  1.00 69.58  ? 55  GLU A CB    1 
ATOM   429  C  CG    . GLU A 1 83  ? 19.165  23.657  41.867  1.00 84.70  ? 55  GLU A CG    1 
ATOM   430  C  CD    . GLU A 1 83  ? 20.020  24.917  41.746  1.00 100.66 ? 55  GLU A CD    1 
ATOM   431  O  OE1   . GLU A 1 83  ? 20.649  25.108  40.681  1.00 100.79 ? 55  GLU A OE1   1 
ATOM   432  O  OE2   . GLU A 1 83  ? 20.105  25.694  42.725  1.00 98.03  ? 55  GLU A OE2   1 
ATOM   433  N  N     . LYS A 1 84  ? 18.320  20.752  42.722  1.00 61.14  ? 56  LYS A N     1 
ATOM   434  C  CA    . LYS A 1 84  ? 18.877  19.743  43.617  1.00 60.16  ? 56  LYS A CA    1 
ATOM   435  C  C     . LYS A 1 84  ? 18.283  18.370  43.331  1.00 53.84  ? 56  LYS A C     1 
ATOM   436  O  O     . LYS A 1 84  ? 19.011  17.370  43.271  1.00 53.50  ? 56  LYS A O     1 
ATOM   437  C  CB    . LYS A 1 84  ? 18.635  20.147  45.071  1.00 61.54  ? 56  LYS A CB    1 
ATOM   438  C  CG    . LYS A 1 84  ? 18.909  21.613  45.353  1.00 68.98  ? 56  LYS A CG    1 
ATOM   439  C  CD    . LYS A 1 84  ? 19.881  21.781  46.512  1.00 71.64  ? 56  LYS A CD    1 
ATOM   440  C  CE    . LYS A 1 84  ? 20.040  23.249  46.903  1.00 72.32  ? 56  LYS A CE    1 
ATOM   441  N  NZ    . LYS A 1 84  ? 19.092  23.646  47.985  1.00 72.17  ? 56  LYS A NZ    1 
ATOM   442  N  N     . ILE A 1 85  ? 16.964  18.309  43.138  1.00 49.61  ? 57  ILE A N     1 
ATOM   443  C  CA    . ILE A 1 85  ? 16.313  17.039  42.834  1.00 52.55  ? 57  ILE A CA    1 
ATOM   444  C  C     . ILE A 1 85  ? 16.891  16.429  41.564  1.00 54.46  ? 57  ILE A C     1 
ATOM   445  O  O     . ILE A 1 85  ? 17.167  15.223  41.502  1.00 54.48  ? 57  ILE A O     1 
ATOM   446  C  CB    . ILE A 1 85  ? 14.792  17.242  42.729  1.00 50.84  ? 57  ILE A CB    1 
ATOM   447  C  CG1   . ILE A 1 85  ? 14.218  17.530  44.116  1.00 58.02  ? 57  ILE A CG1   1 
ATOM   448  C  CG2   . ILE A 1 85  ? 14.124  16.034  42.112  1.00 55.26  ? 57  ILE A CG2   1 
ATOM   449  C  CD1   . ILE A 1 85  ? 14.555  16.454  45.153  1.00 49.15  ? 57  ILE A CD1   1 
ATOM   450  N  N     . ASP A 1 86  ? 17.113  17.256  40.540  1.00 57.31  ? 58  ASP A N     1 
ATOM   451  C  CA    . ASP A 1 86  ? 17.589  16.727  39.267  1.00 58.92  ? 58  ASP A CA    1 
ATOM   452  C  C     . ASP A 1 86  ? 18.975  16.116  39.416  1.00 56.33  ? 58  ASP A C     1 
ATOM   453  O  O     . ASP A 1 86  ? 19.275  15.076  38.817  1.00 62.59  ? 58  ASP A O     1 
ATOM   454  C  CB    . ASP A 1 86  ? 17.602  17.834  38.216  1.00 57.92  ? 58  ASP A CB    1 
ATOM   455  C  CG    . ASP A 1 86  ? 16.322  17.887  37.411  1.00 69.20  ? 58  ASP A CG    1 
ATOM   456  O  OD1   . ASP A 1 86  ? 15.378  17.128  37.722  1.00 72.12  ? 58  ASP A OD1   1 
ATOM   457  O  OD2   . ASP A 1 86  ? 16.256  18.697  36.466  1.00 80.47  ? 58  ASP A OD2   1 
ATOM   458  N  N     . ARG A 1 87  ? 19.828  16.736  40.232  1.00 59.92  ? 59  ARG A N     1 
ATOM   459  C  CA    . ARG A 1 87  ? 21.198  16.259  40.383  1.00 61.84  ? 59  ARG A CA    1 
ATOM   460  C  C     . ARG A 1 87  ? 21.261  14.998  41.237  1.00 59.67  ? 59  ARG A C     1 
ATOM   461  O  O     . ARG A 1 87  ? 22.083  14.107  40.978  1.00 55.25  ? 59  ARG A O     1 
ATOM   462  C  CB    . ARG A 1 87  ? 22.068  17.370  40.981  1.00 63.26  ? 59  ARG A CB    1 
ATOM   463  C  CG    . ARG A 1 87  ? 22.855  18.172  39.939  1.00 78.13  ? 59  ARG A CG    1 
ATOM   464  C  CD    . ARG A 1 87  ? 21.926  18.954  39.010  1.00 82.87  ? 59  ARG A CD    1 
ATOM   465  N  NE    . ARG A 1 87  ? 22.586  19.340  37.767  1.00 90.64  ? 59  ARG A NE    1 
ATOM   466  C  CZ    . ARG A 1 87  ? 22.758  20.591  37.360  1.00 96.36  ? 59  ARG A CZ    1 
ATOM   467  N  NH1   . ARG A 1 87  ? 22.297  21.617  38.059  1.00 88.19  ? 59  ARG A NH1   1 
ATOM   468  N  NH2   . ARG A 1 87  ? 23.407  20.819  36.221  1.00 94.33  ? 59  ARG A NH2   1 
ATOM   469  N  N     . ILE A 1 88  ? 20.407  14.908  42.262  1.00 51.81  ? 60  ILE A N     1 
ATOM   470  C  CA    . ILE A 1 88  ? 20.323  13.687  43.062  1.00 51.92  ? 60  ILE A CA    1 
ATOM   471  C  C     . ILE A 1 88  ? 19.805  12.528  42.218  1.00 46.29  ? 60  ILE A C     1 
ATOM   472  O  O     . ILE A 1 88  ? 20.305  11.400  42.309  1.00 50.36  ? 60  ILE A O     1 
ATOM   473  C  CB    . ILE A 1 88  ? 19.433  13.925  44.297  1.00 49.83  ? 60  ILE A CB    1 
ATOM   474  C  CG1   . ILE A 1 88  ? 20.092  14.916  45.261  1.00 54.24  ? 60  ILE A CG1   1 
ATOM   475  C  CG2   . ILE A 1 88  ? 19.163  12.614  45.022  1.00 47.05  ? 60  ILE A CG2   1 
ATOM   476  C  CD1   . ILE A 1 88  ? 19.271  15.178  46.506  1.00 55.31  ? 60  ILE A CD1   1 
ATOM   477  N  N     . TYR A 1 89  ? 18.782  12.780  41.394  1.00 47.96  ? 61  TYR A N     1 
ATOM   478  C  CA    . TYR A 1 89  ? 18.167  11.700  40.627  1.00 46.30  ? 61  TYR A CA    1 
ATOM   479  C  C     . TYR A 1 89  ? 19.145  11.113  39.616  1.00 55.56  ? 61  TYR A C     1 
ATOM   480  O  O     . TYR A 1 89  ? 19.170  9.894   39.400  1.00 50.27  ? 61  TYR A O     1 
ATOM   481  C  CB    . TYR A 1 89  ? 16.896  12.215  39.947  1.00 54.32  ? 61  TYR A CB    1 
ATOM   482  C  CG    . TYR A 1 89  ? 16.057  11.159  39.252  1.00 55.50  ? 61  TYR A CG    1 
ATOM   483  C  CD1   . TYR A 1 89  ? 15.427  10.146  39.976  1.00 52.04  ? 61  TYR A CD1   1 
ATOM   484  C  CD2   . TYR A 1 89  ? 15.853  11.207  37.876  1.00 50.64  ? 61  TYR A CD2   1 
ATOM   485  C  CE1   . TYR A 1 89  ? 14.641  9.183   39.333  1.00 57.65  ? 61  TYR A CE1   1 
ATOM   486  C  CE2   . TYR A 1 89  ? 15.079  10.254  37.230  1.00 57.92  ? 61  TYR A CE2   1 
ATOM   487  C  CZ    . TYR A 1 89  ? 14.474  9.248   37.956  1.00 62.11  ? 61  TYR A CZ    1 
ATOM   488  O  OH    . TYR A 1 89  ? 13.703  8.316   37.293  1.00 56.81  ? 61  TYR A OH    1 
ATOM   489  N  N     . GLU A 1 90  ? 19.986  11.957  39.012  1.00 59.57  ? 62  GLU A N     1 
ATOM   490  C  CA    . GLU A 1 90  ? 20.969  11.456  38.054  1.00 62.42  ? 62  GLU A CA    1 
ATOM   491  C  C     . GLU A 1 90  ? 21.944  10.499  38.730  1.00 51.40  ? 62  GLU A C     1 
ATOM   492  O  O     . GLU A 1 90  ? 22.282  9.447   38.174  1.00 53.79  ? 62  GLU A O     1 
ATOM   493  C  CB    . GLU A 1 90  ? 21.705  12.630  37.403  1.00 64.16  ? 62  GLU A CB    1 
ATOM   494  C  CG    . GLU A 1 90  ? 20.894  13.327  36.311  1.00 72.12  ? 62  GLU A CG    1 
ATOM   495  C  CD    . GLU A 1 90  ? 21.653  14.461  35.623  1.00 89.67  ? 62  GLU A CD    1 
ATOM   496  O  OE1   . GLU A 1 90  ? 22.683  14.918  36.168  1.00 85.78  ? 62  GLU A OE1   1 
ATOM   497  O  OE2   . GLU A 1 90  ? 21.208  14.900  34.538  1.00 89.81  ? 62  GLU A OE2   1 
ATOM   498  N  N     . ARG A 1 91  ? 22.376  10.833  39.951  1.00 53.55  ? 63  ARG A N     1 
ATOM   499  C  CA    . ARG A 1 91  ? 23.212  9.926   40.736  1.00 48.55  ? 63  ARG A CA    1 
ATOM   500  C  C     . ARG A 1 91  ? 22.492  8.618   41.036  1.00 54.19  ? 63  ARG A C     1 
ATOM   501  O  O     . ARG A 1 91  ? 23.085  7.536   40.938  1.00 48.88  ? 63  ARG A O     1 
ATOM   502  C  CB    . ARG A 1 91  ? 23.637  10.609  42.036  1.00 54.85  ? 63  ARG A CB    1 
ATOM   503  C  CG    . ARG A 1 91  ? 25.121  10.501  42.343  1.00 71.30  ? 63  ARG A CG    1 
ATOM   504  C  CD    . ARG A 1 91  ? 25.459  11.053  43.727  1.00 77.69  ? 63  ARG A CD    1 
ATOM   505  N  NE    . ARG A 1 91  ? 25.093  12.458  43.868  1.00 73.38  ? 63  ARG A NE    1 
ATOM   506  C  CZ    . ARG A 1 91  ? 24.477  12.969  44.926  1.00 74.64  ? 63  ARG A CZ    1 
ATOM   507  N  NH1   . ARG A 1 91  ? 24.144  12.217  45.963  1.00 70.63  ? 63  ARG A NH1   1 
ATOM   508  N  NH2   . ARG A 1 91  ? 24.188  14.267  44.944  1.00 69.28  ? 63  ARG A NH2   1 
ATOM   509  N  N     . ILE A 1 92  ? 21.213  8.696   41.423  1.00 51.85  ? 64  ILE A N     1 
ATOM   510  C  CA    . ILE A 1 92  ? 20.447  7.487   41.713  1.00 50.74  ? 64  ILE A CA    1 
ATOM   511  C  C     . ILE A 1 92  ? 20.363  6.587   40.481  1.00 42.93  ? 64  ILE A C     1 
ATOM   512  O  O     . ILE A 1 92  ? 20.431  5.356   40.591  1.00 45.62  ? 64  ILE A O     1 
ATOM   513  C  CB    . ILE A 1 92  ? 19.045  7.857   42.247  1.00 48.71  ? 64  ILE A CB    1 
ATOM   514  C  CG1   . ILE A 1 92  ? 19.140  8.412   43.671  1.00 49.16  ? 64  ILE A CG1   1 
ATOM   515  C  CG2   . ILE A 1 92  ? 18.112  6.647   42.207  1.00 48.66  ? 64  ILE A CG2   1 
ATOM   516  C  CD1   . ILE A 1 92  ? 17.928  9.272   44.100  1.00 50.28  ? 64  ILE A CD1   1 
ATOM   517  N  N     . LEU A 1 93  ? 20.204  7.178   39.292  1.00 49.73  ? 65  LEU A N     1 
ATOM   518  C  CA    . LEU A 1 93  ? 20.127  6.365   38.076  1.00 54.72  ? 65  LEU A CA    1 
ATOM   519  C  C     . LEU A 1 93  ? 21.400  5.572   37.801  1.00 57.52  ? 65  LEU A C     1 
ATOM   520  O  O     . LEU A 1 93  ? 21.339  4.547   37.111  1.00 59.78  ? 65  LEU A O     1 
ATOM   521  C  CB    . LEU A 1 93  ? 19.815  7.234   36.856  1.00 52.20  ? 65  LEU A CB    1 
ATOM   522  C  CG    . LEU A 1 93  ? 18.451  7.902   36.823  1.00 59.90  ? 65  LEU A CG    1 
ATOM   523  C  CD1   . LEU A 1 93  ? 18.323  8.805   35.607  1.00 61.85  ? 65  LEU A CD1   1 
ATOM   524  C  CD2   . LEU A 1 93  ? 17.382  6.824   36.815  1.00 55.06  ? 65  LEU A CD2   1 
ATOM   525  N  N     . ALA A 1 94  ? 22.539  6.006   38.326  1.00 54.40  ? 66  ALA A N     1 
ATOM   526  C  CA    . ALA A 1 94  ? 23.807  5.328   38.087  1.00 61.97  ? 66  ALA A CA    1 
ATOM   527  C  C     . ALA A 1 94  ? 24.162  4.325   39.174  1.00 64.08  ? 66  ALA A C     1 
ATOM   528  O  O     . ALA A 1 94  ? 25.190  3.650   39.060  1.00 58.54  ? 66  ALA A O     1 
ATOM   529  C  CB    . ALA A 1 94  ? 24.939  6.352   37.956  1.00 61.45  ? 66  ALA A CB    1 
ATOM   530  N  N     . ASP A 1 95  ? 23.347  4.217   40.223  1.00 57.21  ? 67  ASP A N     1 
ATOM   531  C  CA    . ASP A 1 95  ? 23.646  3.309   41.321  1.00 52.22  ? 67  ASP A CA    1 
ATOM   532  C  C     . ASP A 1 95  ? 23.477  1.868   40.852  1.00 58.37  ? 67  ASP A C     1 
ATOM   533  O  O     . ASP A 1 95  ? 22.405  1.480   40.377  1.00 56.60  ? 67  ASP A O     1 
ATOM   534  C  CB    . ASP A 1 95  ? 22.736  3.621   42.506  1.00 48.40  ? 67  ASP A CB    1 
ATOM   535  C  CG    . ASP A 1 95  ? 23.183  2.947   43.786  1.00 47.97  ? 67  ASP A CG    1 
ATOM   536  O  OD1   . ASP A 1 95  ? 23.381  1.712   43.795  1.00 50.12  ? 67  ASP A OD1   1 
ATOM   537  O  OD2   . ASP A 1 95  ? 23.319  3.666   44.800  1.00 52.08  ? 67  ASP A OD2   1 
ATOM   538  N  N     . GLU A 1 96  ? 24.546  1.078   40.974  1.00 57.08  ? 68  GLU A N     1 
ATOM   539  C  CA    . GLU A 1 96  ? 24.552  -0.294  40.477  1.00 53.43  ? 68  GLU A CA    1 
ATOM   540  C  C     . GLU A 1 96  ? 23.567  -1.191  41.211  1.00 56.45  ? 68  GLU A C     1 
ATOM   541  O  O     . GLU A 1 96  ? 23.285  -2.296  40.737  1.00 55.52  ? 68  GLU A O     1 
ATOM   542  C  CB    . GLU A 1 96  ? 25.945  -0.906  40.631  1.00 63.23  ? 68  GLU A CB    1 
ATOM   543  C  CG    . GLU A 1 96  ? 26.503  -0.700  42.036  1.00 68.13  ? 68  GLU A CG    1 
ATOM   544  C  CD    . GLU A 1 96  ? 27.463  -1.786  42.465  1.00 87.83  ? 68  GLU A CD    1 
ATOM   545  O  OE1   . GLU A 1 96  ? 27.046  -2.654  43.263  1.00 86.05  ? 68  GLU A OE1   1 
ATOM   546  O  OE2   . GLU A 1 96  ? 28.630  -1.772  42.012  1.00 100.07 ? 68  GLU A OE2   1 
ATOM   547  N  N     . ARG A 1 97  ? 23.059  -0.758  42.362  1.00 48.17  ? 69  ARG A N     1 
ATOM   548  C  CA    . ARG A 1 97  ? 22.342  -1.672  43.239  1.00 48.13  ? 69  ARG A CA    1 
ATOM   549  C  C     . ARG A 1 97  ? 20.884  -1.860  42.846  1.00 46.71  ? 69  ARG A C     1 
ATOM   550  O  O     . ARG A 1 97  ? 20.218  -2.721  43.430  1.00 46.80  ? 69  ARG A O     1 
ATOM   551  C  CB    . ARG A 1 97  ? 22.433  -1.192  44.690  1.00 53.27  ? 69  ARG A CB    1 
ATOM   552  C  CG    . ARG A 1 97  ? 23.692  -1.679  45.419  1.00 56.55  ? 69  ARG A CG    1 
ATOM   553  C  CD    . ARG A 1 97  ? 23.898  -0.940  46.732  1.00 52.83  ? 69  ARG A CD    1 
ATOM   554  N  NE    . ARG A 1 97  ? 23.944  0.509   46.565  1.00 48.08  ? 69  ARG A NE    1 
ATOM   555  C  CZ    . ARG A 1 97  ? 24.306  1.350   47.527  1.00 45.72  ? 69  ARG A CZ    1 
ATOM   556  N  NH1   . ARG A 1 97  ? 24.666  0.913   48.722  1.00 49.17  ? 69  ARG A NH1   1 
ATOM   557  N  NH2   . ARG A 1 97  ? 24.290  2.659   47.288  1.00 50.50  ? 69  ARG A NH2   1 
ATOM   558  N  N     . HIS A 1 98  ? 20.378  -1.103  41.875  1.00 43.09  ? 70  HIS A N     1 
ATOM   559  C  CA    . HIS A 1 98  ? 19.035  -1.354  41.357  1.00 48.05  ? 70  HIS A CA    1 
ATOM   560  C  C     . HIS A 1 98  ? 18.984  -1.066  39.859  1.00 53.31  ? 70  HIS A C     1 
ATOM   561  O  O     . HIS A 1 98  ? 19.894  -0.463  39.278  1.00 50.21  ? 70  HIS A O     1 
ATOM   562  C  CB    . HIS A 1 98  ? 17.962  -0.543  42.112  1.00 41.85  ? 70  HIS A CB    1 
ATOM   563  C  CG    . HIS A 1 98  ? 18.101  0.943   41.993  1.00 42.34  ? 70  HIS A CG    1 
ATOM   564  N  ND1   . HIS A 1 98  ? 17.084  1.805   42.348  1.00 41.03  ? 70  HIS A ND1   1 
ATOM   565  C  CD2   . HIS A 1 98  ? 19.126  1.726   41.578  1.00 46.79  ? 70  HIS A CD2   1 
ATOM   566  C  CE1   . HIS A 1 98  ? 17.469  3.052   42.150  1.00 38.19  ? 70  HIS A CE1   1 
ATOM   567  N  NE2   . HIS A 1 98  ? 18.707  3.033   41.680  1.00 42.42  ? 70  HIS A NE2   1 
ATOM   568  N  N     . THR A 1 99  ? 17.901  -1.515  39.227  1.00 45.53  ? 71  THR A N     1 
ATOM   569  C  CA    . THR A 1 99  ? 17.768  -1.381  37.786  1.00 49.37  ? 71  THR A CA    1 
ATOM   570  C  C     . THR A 1 99  ? 16.291  -1.241  37.434  1.00 62.13  ? 71  THR A C     1 
ATOM   571  O  O     . THR A 1 99  ? 15.411  -1.309  38.305  1.00 45.71  ? 71  THR A O     1 
ATOM   572  C  CB    . THR A 1 99  ? 18.437  -2.571  37.079  1.00 56.88  ? 71  THR A CB    1 
ATOM   573  O  OG1   . THR A 1 99  ? 18.596  -2.286  35.684  1.00 61.71  ? 71  THR A OG1   1 
ATOM   574  C  CG2   . THR A 1 99  ? 17.627  -3.842  37.258  1.00 55.27  ? 71  THR A CG2   1 
ATOM   575  N  N     . ASP A 1 100 ? 16.032  -1.026  36.138  1.00 56.36  ? 72  ASP A N     1 
ATOM   576  C  CA    . ASP A 1 100 ? 14.681  -0.886  35.599  1.00 55.51  ? 72  ASP A CA    1 
ATOM   577  C  C     . ASP A 1 100 ? 13.935  0.259   36.285  1.00 50.62  ? 72  ASP A C     1 
ATOM   578  O  O     . ASP A 1 100 ? 12.806  0.101   36.753  1.00 52.46  ? 72  ASP A O     1 
ATOM   579  C  CB    . ASP A 1 100 ? 13.903  -2.199  35.715  1.00 56.48  ? 72  ASP A CB    1 
ATOM   580  C  CG    . ASP A 1 100 ? 14.507  -3.310  34.876  1.00 66.74  ? 72  ASP A CG    1 
ATOM   581  O  OD1   . ASP A 1 100 ? 15.155  -2.999  33.858  1.00 62.15  ? 72  ASP A OD1   1 
ATOM   582  O  OD2   . ASP A 1 100 ? 14.326  -4.495  35.231  1.00 70.84  ? 72  ASP A OD2   1 
ATOM   583  N  N     . ILE A 1 101 ? 14.592  1.419   36.347  1.00 51.75  ? 73  ILE A N     1 
ATOM   584  C  CA    . ILE A 1 101 ? 14.002  2.606   36.952  1.00 51.29  ? 73  ILE A CA    1 
ATOM   585  C  C     . ILE A 1 101 ? 12.837  3.078   36.100  1.00 58.43  ? 73  ILE A C     1 
ATOM   586  O  O     . ILE A 1 101 ? 12.970  3.247   34.881  1.00 59.14  ? 73  ILE A O     1 
ATOM   587  C  CB    . ILE A 1 101 ? 15.038  3.734   37.097  1.00 50.17  ? 73  ILE A CB    1 
ATOM   588  C  CG1   . ILE A 1 101 ? 16.409  3.217   37.545  1.00 65.06  ? 73  ILE A CG1   1 
ATOM   589  C  CG2   . ILE A 1 101 ? 14.498  4.862   37.996  1.00 49.70  ? 73  ILE A CG2   1 
ATOM   590  C  CD1   . ILE A 1 101 ? 16.388  2.297   38.711  1.00 51.65  ? 73  ILE A CD1   1 
ATOM   591  N  N     . LEU A 1 102 ? 11.692  3.317   36.739  1.00 48.14  ? 74  LEU A N     1 
ATOM   592  C  CA    . LEU A 1 102 ? 10.522  3.859   36.056  1.00 46.89  ? 74  LEU A CA    1 
ATOM   593  C  C     . LEU A 1 102 ? 9.950   4.996   36.892  1.00 43.10  ? 74  LEU A C     1 
ATOM   594  O  O     . LEU A 1 102 ? 9.462   4.764   38.004  1.00 41.63  ? 74  LEU A O     1 
ATOM   595  C  CB    . LEU A 1 102 ? 9.472   2.769   35.826  1.00 47.85  ? 74  LEU A CB    1 
ATOM   596  C  CG    . LEU A 1 102 ? 8.304   3.180   34.928  1.00 57.46  ? 74  LEU A CG    1 
ATOM   597  C  CD1   . LEU A 1 102 ? 8.822   3.900   33.683  1.00 63.06  ? 74  LEU A CD1   1 
ATOM   598  C  CD2   . LEU A 1 102 ? 7.466   1.970   34.560  1.00 57.77  ? 74  LEU A CD2   1 
ATOM   599  N  N     . CYS A 1 103 ? 9.992   6.216   36.357  1.00 38.85  ? 75  CYS A N     1 
ATOM   600  C  CA    . CYS A 1 103 ? 9.359   7.363   37.000  1.00 42.08  ? 75  CYS A CA    1 
ATOM   601  C  C     . CYS A 1 103 ? 7.853   7.334   36.747  1.00 49.03  ? 75  CYS A C     1 
ATOM   602  O  O     . CYS A 1 103 ? 7.416   7.453   35.598  1.00 44.88  ? 75  CYS A O     1 
ATOM   603  C  CB    . CYS A 1 103 ? 9.970   8.660   36.471  1.00 43.67  ? 75  CYS A CB    1 
ATOM   604  S  SG    . CYS A 1 103 ? 9.114   10.174  36.967  1.00 50.06  ? 75  CYS A SG    1 
ATOM   605  N  N     . LEU A 1 104 ? 7.057   7.192   37.816  1.00 41.26  ? 76  LEU A N     1 
ATOM   606  C  CA    . LEU A 1 104 ? 5.599   7.130   37.697  1.00 39.94  ? 76  LEU A CA    1 
ATOM   607  C  C     . LEU A 1 104 ? 4.927   8.494   37.672  1.00 46.66  ? 76  LEU A C     1 
ATOM   608  O  O     . LEU A 1 104 ? 3.813   8.618   37.147  1.00 48.62  ? 76  LEU A O     1 
ATOM   609  C  CB    . LEU A 1 104 ? 4.998   6.336   38.863  1.00 45.17  ? 76  LEU A CB    1 
ATOM   610  C  CG    . LEU A 1 104 ? 5.569   4.951   39.111  1.00 47.38  ? 76  LEU A CG    1 
ATOM   611  C  CD1   . LEU A 1 104 ? 5.121   4.435   40.479  1.00 50.56  ? 76  LEU A CD1   1 
ATOM   612  C  CD2   . LEU A 1 104 ? 5.159   4.007   38.002  1.00 49.52  ? 76  LEU A CD2   1 
ATOM   613  N  N     . LYS A 1 105 ? 5.551   9.509   38.259  1.00 41.75  ? 77  LYS A N     1 
ATOM   614  C  CA    . LYS A 1 105 ? 4.916   10.803  38.462  1.00 42.43  ? 77  LYS A CA    1 
ATOM   615  C  C     . LYS A 1 105 ? 5.992   11.847  38.682  1.00 47.66  ? 77  LYS A C     1 
ATOM   616  O  O     . LYS A 1 105 ? 6.892   11.634  39.497  1.00 41.68  ? 77  LYS A O     1 
ATOM   617  C  CB    . LYS A 1 105 ? 3.991   10.798  39.680  1.00 50.06  ? 77  LYS A CB    1 
ATOM   618  C  CG    . LYS A 1 105 ? 3.001   11.952  39.725  1.00 50.67  ? 77  LYS A CG    1 
ATOM   619  C  CD    . LYS A 1 105 ? 1.732   11.536  40.458  1.00 56.98  ? 77  LYS A CD    1 
ATOM   620  C  CE    . LYS A 1 105 ? 0.918   12.741  40.882  1.00 65.25  ? 77  LYS A CE    1 
ATOM   621  N  NZ    . LYS A 1 105 ? 0.069   13.228  39.758  1.00 76.35  ? 77  LYS A NZ    1 
ATOM   622  N  N     . SER A 1 106 ? 5.867   12.981  37.999  1.00 44.35  ? 78  SER A N     1 
ATOM   623  C  CA    . SER A 1 106 ? 6.732   14.134  38.222  1.00 43.75  ? 78  SER A CA    1 
ATOM   624  C  C     . SER A 1 106 ? 5.852   15.365  38.379  1.00 54.08  ? 78  SER A C     1 
ATOM   625  O  O     . SER A 1 106 ? 5.072   15.693  37.479  1.00 57.58  ? 78  SER A O     1 
ATOM   626  C  CB    . SER A 1 106 ? 7.726   14.310  37.071  1.00 48.46  ? 78  SER A CB    1 
ATOM   627  O  OG    . SER A 1 106 ? 8.428   15.530  37.203  1.00 58.15  ? 78  SER A OG    1 
ATOM   628  N  N     . GLU A 1 107 ? 5.952   16.030  39.524  1.00 41.15  ? 79  GLU A N     1 
ATOM   629  C  CA    . GLU A 1 107 ? 5.144   17.205  39.827  1.00 49.97  ? 79  GLU A CA    1 
ATOM   630  C  C     . GLU A 1 107 ? 6.048   18.427  39.836  1.00 59.09  ? 79  GLU A C     1 
ATOM   631  O  O     . GLU A 1 107 ? 6.976   18.509  40.645  1.00 53.20  ? 79  GLU A O     1 
ATOM   632  C  CB    . GLU A 1 107 ? 4.434   17.062  41.178  1.00 52.01  ? 79  GLU A CB    1 
ATOM   633  C  CG    . GLU A 1 107 ? 3.720   15.739  41.384  1.00 49.21  ? 79  GLU A CG    1 
ATOM   634  C  CD    . GLU A 1 107 ? 3.210   15.579  42.803  1.00 55.84  ? 79  GLU A CD    1 
ATOM   635  O  OE1   . GLU A 1 107 ? 2.353   16.383  43.246  1.00 47.62  ? 79  GLU A OE1   1 
ATOM   636  O  OE2   . GLU A 1 107 ? 3.709   14.659  43.490  1.00 50.43  ? 79  GLU A OE2   1 
ATOM   637  N  N     . VAL A 1 108 ? 5.778   19.371  38.944  1.00 56.94  ? 80  VAL A N     1 
ATOM   638  C  CA    . VAL A 1 108 ? 6.535   20.604  38.878  1.00 58.90  ? 80  VAL A CA    1 
ATOM   639  C  C     . VAL A 1 108 ? 5.725   21.696  39.562  1.00 61.14  ? 80  VAL A C     1 
ATOM   640  O  O     . VAL A 1 108 ? 4.502   21.608  39.696  1.00 59.25  ? 80  VAL A O     1 
ATOM   641  C  CB    . VAL A 1 108 ? 6.886   20.976  37.422  1.00 56.59  ? 80  VAL A CB    1 
ATOM   642  C  CG1   . VAL A 1 108 ? 7.877   19.963  36.863  1.00 58.19  ? 80  VAL A CG1   1 
ATOM   643  C  CG2   . VAL A 1 108 ? 5.635   21.006  36.573  1.00 60.34  ? 80  VAL A CG2   1 
ATOM   644  N  N     . GLU A 1 109 ? 6.421   22.727  40.036  1.00 68.21  ? 81  GLU A N     1 
ATOM   645  C  CA    . GLU A 1 109 ? 5.806   23.840  40.763  1.00 73.74  ? 81  GLU A CA    1 
ATOM   646  C  C     . GLU A 1 109 ? 4.941   23.312  41.916  1.00 74.47  ? 81  GLU A C     1 
ATOM   647  O  O     . GLU A 1 109 ? 3.715   23.430  41.941  1.00 70.97  ? 81  GLU A O     1 
ATOM   648  C  CB    . GLU A 1 109 ? 5.008   24.725  39.793  1.00 81.10  ? 81  GLU A CB    1 
ATOM   649  C  CG    . GLU A 1 109 ? 4.346   25.954  40.416  1.00 93.51  ? 81  GLU A CG    1 
ATOM   650  C  CD    . GLU A 1 109 ? 3.367   26.635  39.473  1.00 102.55 ? 81  GLU A CD    1 
ATOM   651  O  OE1   . GLU A 1 109 ? 2.225   26.915  39.899  1.00 107.04 ? 81  GLU A OE1   1 
ATOM   652  O  OE2   . GLU A 1 109 ? 3.737   26.887  38.306  1.00 102.31 ? 81  GLU A OE2   1 
ATOM   653  N  N     . VAL A 1 110 ? 5.625   22.699  42.871  1.00 72.60  ? 82  VAL A N     1 
ATOM   654  C  CA    . VAL A 1 110 ? 4.966   22.068  44.011  1.00 69.74  ? 82  VAL A CA    1 
ATOM   655  C  C     . VAL A 1 110 ? 4.734   23.108  45.100  1.00 57.57  ? 82  VAL A C     1 
ATOM   656  O  O     . VAL A 1 110 ? 5.588   23.961  45.363  1.00 68.59  ? 82  VAL A O     1 
ATOM   657  C  CB    . VAL A 1 110 ? 5.796   20.874  44.527  1.00 64.63  ? 82  VAL A CB    1 
ATOM   658  C  CG1   . VAL A 1 110 ? 5.566   20.645  46.011  1.00 61.83  ? 82  VAL A CG1   1 
ATOM   659  C  CG2   . VAL A 1 110 ? 5.449   19.624  43.741  1.00 59.18  ? 82  VAL A CG2   1 
ATOM   660  N  N     . GLN A 1 111 ? 3.567   23.027  45.737  1.00 64.21  ? 83  GLN A N     1 
ATOM   661  C  CA    . GLN A 1 111 ? 3.158   23.999  46.750  1.00 72.30  ? 83  GLN A CA    1 
ATOM   662  C  C     . GLN A 1 111 ? 3.776   23.693  48.114  1.00 74.31  ? 83  GLN A C     1 
ATOM   663  O  O     . GLN A 1 111 ? 4.624   24.441  48.607  1.00 69.22  ? 83  GLN A O     1 
ATOM   664  C  CB    . GLN A 1 111 ? 1.628   24.020  46.826  1.00 84.32  ? 83  GLN A CB    1 
ATOM   665  C  CG    . GLN A 1 111 ? 1.006   25.402  46.948  1.00 97.25  ? 83  GLN A CG    1 
ATOM   666  C  CD    . GLN A 1 111 ? -0.479  25.391  46.623  1.00 100.48 ? 83  GLN A CD    1 
ATOM   667  O  OE1   . GLN A 1 111 ? -1.298  24.923  47.415  1.00 103.15 ? 83  GLN A OE1   1 
ATOM   668  N  NE2   . GLN A 1 111 ? -0.831  25.910  45.451  1.00 96.13  ? 83  GLN A NE2   1 
ATOM   669  N  N     . GLU A 1 112 ? 3.350   22.600  48.746  1.00 66.91  ? 84  GLU A N     1 
ATOM   670  C  CA    . GLU A 1 112 ? 3.803   22.231  50.079  1.00 61.89  ? 84  GLU A CA    1 
ATOM   671  C  C     . GLU A 1 112 ? 4.562   20.909  50.041  1.00 55.70  ? 84  GLU A C     1 
ATOM   672  O  O     . GLU A 1 112 ? 4.372   20.081  49.148  1.00 54.15  ? 84  GLU A O     1 
ATOM   673  C  CB    . GLU A 1 112 ? 2.628   22.108  51.063  1.00 69.12  ? 84  GLU A CB    1 
ATOM   674  C  CG    . GLU A 1 112 ? 1.514   23.130  50.888  1.00 84.94  ? 84  GLU A CG    1 
ATOM   675  C  CD    . GLU A 1 112 ? 1.472   24.145  52.021  1.00 91.80  ? 84  GLU A CD    1 
ATOM   676  O  OE1   . GLU A 1 112 ? 0.780   25.177  51.878  1.00 92.84  ? 84  GLU A OE1   1 
ATOM   677  O  OE2   . GLU A 1 112 ? 2.123   23.902  53.063  1.00 93.67  ? 84  GLU A OE2   1 
ATOM   678  N  N     . ARG A 1 113 ? 5.436   20.721  51.024  1.00 53.85  ? 85  ARG A N     1 
ATOM   679  C  CA    . ARG A 1 113 ? 6.098   19.440  51.196  1.00 43.00  ? 85  ARG A CA    1 
ATOM   680  C  C     . ARG A 1 113 ? 5.122   18.458  51.832  1.00 43.64  ? 85  ARG A C     1 
ATOM   681  O  O     . ARG A 1 113 ? 4.315   18.830  52.687  1.00 44.39  ? 85  ARG A O     1 
ATOM   682  C  CB    . ARG A 1 113 ? 7.340   19.595  52.084  1.00 44.43  ? 85  ARG A CB    1 
ATOM   683  C  CG    . ARG A 1 113 ? 8.591   20.148  51.399  1.00 51.59  ? 85  ARG A CG    1 
ATOM   684  C  CD    . ARG A 1 113 ? 9.737   20.203  52.405  1.00 44.20  ? 85  ARG A CD    1 
ATOM   685  N  NE    . ARG A 1 113 ? 10.849  21.054  51.991  1.00 48.56  ? 85  ARG A NE    1 
ATOM   686  C  CZ    . ARG A 1 113 ? 11.925  20.635  51.340  1.00 47.88  ? 85  ARG A CZ    1 
ATOM   687  N  NH1   . ARG A 1 113 ? 12.071  19.370  50.981  1.00 45.64  ? 85  ARG A NH1   1 
ATOM   688  N  NH2   . ARG A 1 113 ? 12.884  21.510  51.039  1.00 54.88  ? 85  ARG A NH2   1 
ATOM   689  N  N     . MET A 1 114 ? 5.195   17.198  51.417  1.00 40.94  ? 86  MET A N     1 
ATOM   690  C  CA    . MET A 1 114 ? 4.381   16.158  52.041  1.00 37.76  ? 86  MET A CA    1 
ATOM   691  C  C     . MET A 1 114 ? 5.083   15.483  53.215  1.00 41.84  ? 86  MET A C     1 
ATOM   692  O  O     . MET A 1 114 ? 4.405   14.925  54.091  1.00 44.15  ? 86  MET A O     1 
ATOM   693  C  CB    . MET A 1 114 ? 4.033   15.087  51.011  1.00 42.74  ? 86  MET A CB    1 
ATOM   694  C  CG    . MET A 1 114 ? 2.971   15.508  50.024  1.00 59.97  ? 86  MET A CG    1 
ATOM   695  S  SD    . MET A 1 114 ? 2.080   14.085  49.394  1.00 78.17  ? 86  MET A SD    1 
ATOM   696  C  CE    . MET A 1 114 ? 3.425   13.186  48.642  1.00 53.56  ? 86  MET A CE    1 
ATOM   697  N  N     . PHE A 1 115 ? 6.415   15.501  53.241  1.00 37.68  ? 87  PHE A N     1 
ATOM   698  C  CA    . PHE A 1 115 ? 7.205   14.829  54.280  1.00 34.63  ? 87  PHE A CA    1 
ATOM   699  C  C     . PHE A 1 115 ? 8.232   15.798  54.867  1.00 35.52  ? 87  PHE A C     1 
ATOM   700  O  O     . PHE A 1 115 ? 9.436   15.531  54.848  1.00 36.13  ? 87  PHE A O     1 
ATOM   701  C  CB    . PHE A 1 115 ? 7.880   13.589  53.688  1.00 36.22  ? 87  PHE A CB    1 
ATOM   702  C  CG    . PHE A 1 115 ? 6.908   12.675  52.955  1.00 41.20  ? 87  PHE A CG    1 
ATOM   703  C  CD1   . PHE A 1 115 ? 5.930   11.988  53.654  1.00 37.27  ? 87  PHE A CD1   1 
ATOM   704  C  CD2   . PHE A 1 115 ? 6.971   12.526  51.574  1.00 41.52  ? 87  PHE A CD2   1 
ATOM   705  C  CE1   . PHE A 1 115 ? 5.040   11.157  53.002  1.00 41.81  ? 87  PHE A CE1   1 
ATOM   706  C  CE2   . PHE A 1 115 ? 6.075   11.688  50.900  1.00 42.39  ? 87  PHE A CE2   1 
ATOM   707  C  CZ    . PHE A 1 115 ? 5.111   11.004  51.618  1.00 41.04  ? 87  PHE A CZ    1 
ATOM   708  N  N     . PRO A 1 116 ? 7.776   16.915  55.458  1.00 39.41  ? 88  PRO A N     1 
ATOM   709  C  CA    . PRO A 1 116 ? 8.714   17.985  55.854  1.00 37.75  ? 88  PRO A CA    1 
ATOM   710  C  C     . PRO A 1 116 ? 9.711   17.604  56.938  1.00 40.19  ? 88  PRO A C     1 
ATOM   711  O  O     . PRO A 1 116 ? 10.768  18.244  57.031  1.00 41.80  ? 88  PRO A O     1 
ATOM   712  C  CB    . PRO A 1 116 ? 7.779   19.100  56.348  1.00 40.90  ? 88  PRO A CB    1 
ATOM   713  C  CG    . PRO A 1 116 ? 6.530   18.390  56.771  1.00 41.73  ? 88  PRO A CG    1 
ATOM   714  C  CD    . PRO A 1 116 ? 6.380   17.273  55.771  1.00 41.35  ? 88  PRO A CD    1 
ATOM   715  N  N     . ASP A 1 117 ? 9.426   16.601  57.758  1.00 38.95  ? 89  ASP A N     1 
ATOM   716  C  CA    . ASP A 1 117 ? 10.315  16.230  58.851  1.00 38.64  ? 89  ASP A CA    1 
ATOM   717  C  C     . ASP A 1 117 ? 11.195  15.025  58.535  1.00 38.24  ? 89  ASP A C     1 
ATOM   718  O  O     . ASP A 1 117 ? 11.911  14.555  59.428  1.00 34.81  ? 89  ASP A O     1 
ATOM   719  C  CB    . ASP A 1 117 ? 9.488   15.952  60.108  1.00 38.73  ? 89  ASP A CB    1 
ATOM   720  C  CG    . ASP A 1 117 ? 8.699   17.191  60.577  1.00 53.38  ? 89  ASP A CG    1 
ATOM   721  O  OD1   . ASP A 1 117 ? 9.325   18.255  60.782  1.00 51.26  ? 89  ASP A OD1   1 
ATOM   722  O  OD2   . ASP A 1 117 ? 7.462   17.098  60.722  1.00 50.25  ? 89  ASP A OD2   1 
ATOM   723  N  N     . TRP A 1 118 ? 11.184  14.530  57.295  1.00 31.99  ? 90  TRP A N     1 
ATOM   724  C  CA    . TRP A 1 118 ? 11.879  13.297  56.911  1.00 32.01  ? 90  TRP A CA    1 
ATOM   725  C  C     . TRP A 1 118 ? 12.894  13.622  55.818  1.00 34.29  ? 90  TRP A C     1 
ATOM   726  O  O     . TRP A 1 118 ? 12.515  13.742  54.646  1.00 32.95  ? 90  TRP A O     1 
ATOM   727  C  CB    . TRP A 1 118 ? 10.895  12.262  56.370  1.00 34.51  ? 90  TRP A CB    1 
ATOM   728  C  CG    . TRP A 1 118 ? 9.876   11.724  57.331  1.00 33.59  ? 90  TRP A CG    1 
ATOM   729  C  CD1   . TRP A 1 118 ? 9.748   11.998  58.671  1.00 36.01  ? 90  TRP A CD1   1 
ATOM   730  C  CD2   . TRP A 1 118 ? 8.764   10.891  56.982  1.00 31.69  ? 90  TRP A CD2   1 
ATOM   731  N  NE1   . TRP A 1 118 ? 8.638   11.343  59.184  1.00 34.32  ? 90  TRP A NE1   1 
ATOM   732  C  CE2   . TRP A 1 118 ? 8.026   10.653  58.165  1.00 34.96  ? 90  TRP A CE2   1 
ATOM   733  C  CE3   . TRP A 1 118 ? 8.340   10.299  55.786  1.00 35.36  ? 90  TRP A CE3   1 
ATOM   734  C  CZ2   . TRP A 1 118 ? 6.882   9.857   58.180  1.00 36.96  ? 90  TRP A CZ2   1 
ATOM   735  C  CZ3   . TRP A 1 118 ? 7.203   9.504   55.803  1.00 32.86  ? 90  TRP A CZ3   1 
ATOM   736  C  CH2   . TRP A 1 118 ? 6.487   9.291   56.995  1.00 37.25  ? 90  TRP A CH2   1 
ATOM   737  N  N     . SER A 1 119 ? 14.173  13.784  56.177  1.00 32.30  ? 91  SER A N     1 
ATOM   738  C  CA    . SER A 1 119 ? 15.195  13.917  55.136  1.00 32.88  ? 91  SER A CA    1 
ATOM   739  C  C     . SER A 1 119 ? 15.206  12.687  54.239  1.00 37.36  ? 91  SER A C     1 
ATOM   740  O  O     . SER A 1 119 ? 15.255  12.801  53.008  1.00 34.66  ? 91  SER A O     1 
ATOM   741  C  CB    . SER A 1 119 ? 16.575  14.154  55.760  1.00 36.22  ? 91  SER A CB    1 
ATOM   742  O  OG    . SER A 1 119 ? 16.562  15.378  56.478  1.00 40.75  ? 91  SER A OG    1 
ATOM   743  N  N     . MET A 1 120 ? 15.164  11.497  54.845  1.00 32.66  ? 92  MET A N     1 
ATOM   744  C  CA    . MET A 1 120 ? 14.804  10.262  54.135  1.00 32.63  ? 92  MET A CA    1 
ATOM   745  C  C     . MET A 1 120 ? 14.376  9.236   55.174  1.00 38.52  ? 92  MET A C     1 
ATOM   746  O  O     . MET A 1 120 ? 15.209  8.741   55.937  1.00 35.02  ? 92  MET A O     1 
ATOM   747  C  CB    . MET A 1 120 ? 15.955  9.720   53.299  1.00 34.26  ? 92  MET A CB    1 
ATOM   748  C  CG    . MET A 1 120 ? 15.583  8.639   52.278  1.00 33.73  ? 92  MET A CG    1 
ATOM   749  S  SD    . MET A 1 120 ? 14.004  8.746   51.420  1.00 35.65  ? 92  MET A SD    1 
ATOM   750  C  CE    . MET A 1 120 ? 14.185  10.334  50.608  1.00 33.13  ? 92  MET A CE    1 
ATOM   751  N  N     . GLN A 1 121 ? 13.095  8.913   55.190  1.00 31.85  ? 93  GLN A N     1 
ATOM   752  C  CA    . GLN A 1 121 ? 12.557  7.893   56.089  1.00 32.48  ? 93  GLN A CA    1 
ATOM   753  C  C     . GLN A 1 121 ? 12.569  6.567   55.340  1.00 38.10  ? 93  GLN A C     1 
ATOM   754  O  O     . GLN A 1 121 ? 12.129  6.507   54.196  1.00 36.43  ? 93  GLN A O     1 
ATOM   755  C  CB    . GLN A 1 121 ? 11.139  8.269   56.520  1.00 30.55  ? 93  GLN A CB    1 
ATOM   756  C  CG    . GLN A 1 121 ? 10.395  7.172   57.321  1.00 33.12  ? 93  GLN A CG    1 
ATOM   757  C  CD    . GLN A 1 121 ? 10.710  7.250   58.802  1.00 43.23  ? 93  GLN A CD    1 
ATOM   758  O  OE1   . GLN A 1 121 ? 11.563  8.023   59.218  1.00 36.00  ? 93  GLN A OE1   1 
ATOM   759  N  NE2   . GLN A 1 121 ? 10.001  6.473   59.605  1.00 41.43  ? 93  GLN A NE2   1 
ATOM   760  N  N     . THR A 1 122 ? 13.057  5.508   55.978  1.00 31.77  ? 94  THR A N     1 
ATOM   761  C  CA    . THR A 1 122 ? 13.160  4.199   55.336  1.00 30.35  ? 94  THR A CA    1 
ATOM   762  C  C     . THR A 1 122 ? 12.166  3.242   55.984  1.00 36.08  ? 94  THR A C     1 
ATOM   763  O  O     . THR A 1 122 ? 12.157  3.102   57.213  1.00 34.43  ? 94  THR A O     1 
ATOM   764  C  CB    . THR A 1 122 ? 14.587  3.655   55.458  1.00 37.68  ? 94  THR A CB    1 
ATOM   765  O  OG1   . THR A 1 122 ? 15.500  4.624   54.914  1.00 40.13  ? 94  THR A OG1   1 
ATOM   766  C  CG2   . THR A 1 122 ? 14.724  2.336   54.702  1.00 40.77  ? 94  THR A CG2   1 
ATOM   767  N  N     . ILE A 1 123 ? 11.320  2.603   55.165  1.00 33.31  ? 95  ILE A N     1 
ATOM   768  C  CA    . ILE A 1 123 ? 10.300  1.656   55.633  1.00 35.12  ? 95  ILE A CA    1 
ATOM   769  C  C     . ILE A 1 123 ? 10.533  0.316   54.932  1.00 38.75  ? 95  ILE A C     1 
ATOM   770  O  O     . ILE A 1 123 ? 10.210  0.175   53.745  1.00 35.86  ? 95  ILE A O     1 
ATOM   771  C  CB    . ILE A 1 123 ? 8.869   2.150   55.365  1.00 39.46  ? 95  ILE A CB    1 
ATOM   772  C  CG1   . ILE A 1 123 ? 8.608   3.511   56.025  1.00 38.73  ? 95  ILE A CG1   1 
ATOM   773  C  CG2   . ILE A 1 123 ? 7.878   1.120   55.881  1.00 39.61  ? 95  ILE A CG2   1 
ATOM   774  C  CD1   . ILE A 1 123 ? 7.275   4.173   55.601  1.00 39.58  ? 95  ILE A CD1   1 
ATOM   775  N  N     . ASN A 1 124 ? 11.036  -0.680  55.669  1.00 34.70  ? 96  ASN A N     1 
ATOM   776  C  CA    . ASN A 1 124 ? 11.274  -2.018  55.108  1.00 37.88  ? 96  ASN A CA    1 
ATOM   777  C  C     . ASN A 1 124 ? 10.044  -2.896  55.357  1.00 37.68  ? 96  ASN A C     1 
ATOM   778  O  O     . ASN A 1 124 ? 9.837   -3.408  56.461  1.00 41.67  ? 96  ASN A O     1 
ATOM   779  C  CB    . ASN A 1 124 ? 12.532  -2.641  55.703  1.00 38.97  ? 96  ASN A CB    1 
ATOM   780  C  CG    . ASN A 1 124 ? 12.880  -3.992  55.066  1.00 46.48  ? 96  ASN A CG    1 
ATOM   781  O  OD1   . ASN A 1 124 ? 12.027  -4.653  54.467  1.00 44.20  ? 96  ASN A OD1   1 
ATOM   782  N  ND2   . ASN A 1 124 ? 14.138  -4.394  55.181  1.00 44.16  ? 96  ASN A ND2   1 
ATOM   783  N  N     . LEU A 1 125 ? 9.244   -3.111  54.310  1.00 33.67  ? 97  LEU A N     1 
ATOM   784  C  CA    . LEU A 1 125 ? 7.991   -3.845  54.476  1.00 38.41  ? 97  LEU A CA    1 
ATOM   785  C  C     . LEU A 1 125 ? 8.192   -5.355  54.595  1.00 39.39  ? 97  LEU A C     1 
ATOM   786  O  O     . LEU A 1 125 ? 7.299   -6.039  55.109  1.00 38.10  ? 97  LEU A O     1 
ATOM   787  C  CB    . LEU A 1 125 ? 7.053   -3.530  53.304  1.00 32.91  ? 97  LEU A CB    1 
ATOM   788  C  CG    . LEU A 1 125 ? 6.477   -2.117  53.333  1.00 43.56  ? 97  LEU A CG    1 
ATOM   789  C  CD1   . LEU A 1 125 ? 5.720   -1.810  52.035  1.00 41.63  ? 97  LEU A CD1   1 
ATOM   790  C  CD2   . LEU A 1 125 ? 5.609   -1.911  54.579  1.00 37.48  ? 97  LEU A CD2   1 
ATOM   791  N  N     . ASP A 1 126 ? 9.330   -5.890  54.121  1.00 37.35  ? 98  ASP A N     1 
ATOM   792  C  CA    . ASP A 1 126 ? 9.646   -7.302  54.340  1.00 41.77  ? 98  ASP A CA    1 
ATOM   793  C  C     . ASP A 1 126 ? 9.649   -7.661  55.826  1.00 47.96  ? 98  ASP A C     1 
ATOM   794  O  O     . ASP A 1 126 ? 9.281   -8.780  56.202  1.00 49.44  ? 98  ASP A O     1 
ATOM   795  C  CB    . ASP A 1 126 ? 11.015  -7.651  53.748  1.00 38.81  ? 98  ASP A CB    1 
ATOM   796  C  CG    . ASP A 1 126 ? 11.064  -7.558  52.235  1.00 45.92  ? 98  ASP A CG    1 
ATOM   797  O  OD1   . ASP A 1 126 ? 10.070  -7.892  51.571  1.00 46.46  ? 98  ASP A OD1   1 
ATOM   798  O  OD2   . ASP A 1 126 ? 12.128  -7.169  51.705  1.00 51.54  ? 98  ASP A OD2   1 
ATOM   799  N  N     . GLU A 1 127 ? 10.103  -6.744  56.686  1.00 40.78  ? 99  GLU A N     1 
ATOM   800  C  CA    . GLU A 1 127 ? 10.228  -7.023  58.113  1.00 42.15  ? 99  GLU A CA    1 
ATOM   801  C  C     . GLU A 1 127 ? 8.995   -6.631  58.918  1.00 48.88  ? 99  GLU A C     1 
ATOM   802  O  O     . GLU A 1 127 ? 8.946   -6.913  60.118  1.00 48.92  ? 99  GLU A O     1 
ATOM   803  C  CB    . GLU A 1 127 ? 11.471  -6.317  58.700  1.00 45.64  ? 99  GLU A CB    1 
ATOM   804  C  CG    . GLU A 1 127 ? 12.806  -6.751  58.046  1.00 55.09  ? 99  GLU A CG    1 
ATOM   805  C  CD    . GLU A 1 127 ? 14.004  -5.892  58.446  1.00 64.16  ? 99  GLU A CD    1 
ATOM   806  O  OE1   . GLU A 1 127 ? 13.828  -4.916  59.212  1.00 55.69  ? 99  GLU A OE1   1 
ATOM   807  O  OE2   . GLU A 1 127 ? 15.134  -6.214  58.012  1.00 55.67  ? 99  GLU A OE2   1 
ATOM   808  N  N     . ASN A 1 128 ? 7.998   -6.008  58.300  1.00 41.98  ? 100 ASN A N     1 
ATOM   809  C  CA    . ASN A 1 128 ? 6.821   -5.557  59.031  1.00 41.66  ? 100 ASN A CA    1 
ATOM   810  C  C     . ASN A 1 128 ? 5.807   -6.690  59.105  1.00 42.40  ? 100 ASN A C     1 
ATOM   811  O  O     . ASN A 1 128 ? 5.486   -7.311  58.088  1.00 44.29  ? 100 ASN A O     1 
ATOM   812  C  CB    . ASN A 1 128 ? 6.212   -4.321  58.360  1.00 39.45  ? 100 ASN A CB    1 
ATOM   813  C  CG    . ASN A 1 128 ? 5.024   -3.765  59.116  1.00 45.77  ? 100 ASN A CG    1 
ATOM   814  O  OD1   . ASN A 1 128 ? 3.989   -4.422  59.231  1.00 46.34  ? 100 ASN A OD1   1 
ATOM   815  N  ND2   . ASN A 1 128 ? 5.162   -2.539  59.628  1.00 42.08  ? 100 ASN A ND2   1 
ATOM   816  N  N     . THR A 1 129 ? 5.303   -6.947  60.312  1.00 44.03  ? 101 THR A N     1 
ATOM   817  C  CA    . THR A 1 129 ? 4.345   -8.017  60.558  1.00 48.82  ? 101 THR A CA    1 
ATOM   818  C  C     . THR A 1 129 ? 2.993   -7.498  61.032  1.00 45.88  ? 101 THR A C     1 
ATOM   819  O  O     . THR A 1 129 ? 2.168   -8.295  61.493  1.00 51.80  ? 101 THR A O     1 
ATOM   820  C  CB    . THR A 1 129 ? 4.907   -9.007  61.590  1.00 61.62  ? 101 THR A CB    1 
ATOM   821  O  OG1   . THR A 1 129 ? 5.309   -8.292  62.767  1.00 57.93  ? 101 THR A OG1   1 
ATOM   822  C  CG2   . THR A 1 129 ? 6.112   -9.752  61.026  1.00 55.16  ? 101 THR A CG2   1 
ATOM   823  N  N     . ASP A 1 130 ? 2.743   -6.193  60.938  1.00 44.58  ? 102 ASP A N     1 
ATOM   824  C  CA    . ASP A 1 130 ? 1.508   -5.623  61.466  1.00 39.73  ? 102 ASP A CA    1 
ATOM   825  C  C     . ASP A 1 130 ? 0.291   -6.217  60.763  1.00 43.09  ? 102 ASP A C     1 
ATOM   826  O  O     . ASP A 1 130 ? 0.319   -6.503  59.564  1.00 43.78  ? 102 ASP A O     1 
ATOM   827  C  CB    . ASP A 1 130 ? 1.501   -4.099  61.300  1.00 44.54  ? 102 ASP A CB    1 
ATOM   828  C  CG    . ASP A 1 130 ? 2.546   -3.409  62.172  1.00 57.28  ? 102 ASP A CG    1 
ATOM   829  O  OD1   . ASP A 1 130 ? 3.100   -4.083  63.065  1.00 55.15  ? 102 ASP A OD1   1 
ATOM   830  O  OD2   . ASP A 1 130 ? 2.815   -2.200  61.956  1.00 58.26  ? 102 ASP A OD2   1 
ATOM   831  N  N     . PHE A 1 131 ? -0.799  -6.338  61.531  1.00 37.57  ? 103 PHE A N     1 
ATOM   832  C  CA    . PHE A 1 131 ? -2.023  -7.003  61.086  1.00 41.93  ? 103 PHE A CA    1 
ATOM   833  C  C     . PHE A 1 131 ? -2.629  -6.332  59.853  1.00 38.97  ? 103 PHE A C     1 
ATOM   834  O  O     . PHE A 1 131 ? -2.921  -6.998  58.854  1.00 39.62  ? 103 PHE A O     1 
ATOM   835  C  CB    . PHE A 1 131 ? -3.007  -7.016  62.266  1.00 40.53  ? 103 PHE A CB    1 
ATOM   836  C  CG    . PHE A 1 131 ? -4.372  -7.601  61.957  1.00 40.45  ? 103 PHE A CG    1 
ATOM   837  C  CD1   . PHE A 1 131 ? -4.598  -8.969  62.072  1.00 41.16  ? 103 PHE A CD1   1 
ATOM   838  C  CD2   . PHE A 1 131 ? -5.426  -6.778  61.601  1.00 39.90  ? 103 PHE A CD2   1 
ATOM   839  C  CE1   . PHE A 1 131 ? -5.853  -9.504  61.818  1.00 39.56  ? 103 PHE A CE1   1 
ATOM   840  C  CE2   . PHE A 1 131 ? -6.687  -7.302  61.347  1.00 47.38  ? 103 PHE A CE2   1 
ATOM   841  C  CZ    . PHE A 1 131 ? -6.901  -8.671  61.456  1.00 44.83  ? 103 PHE A CZ    1 
ATOM   842  N  N     . LEU A 1 132 ? -2.829  -5.008  59.899  1.00 39.66  ? 104 LEU A N     1 
ATOM   843  C  CA    . LEU A 1 132 ? -3.470  -4.339  58.773  1.00 42.00  ? 104 LEU A CA    1 
ATOM   844  C  C     . LEU A 1 132 ? -2.547  -4.205  57.570  1.00 39.24  ? 104 LEU A C     1 
ATOM   845  O  O     . LEU A 1 132 ? -3.034  -4.080  56.435  1.00 40.73  ? 104 LEU A O     1 
ATOM   846  C  CB    . LEU A 1 132 ? -3.973  -2.950  59.171  1.00 49.02  ? 104 LEU A CB    1 
ATOM   847  C  CG    . LEU A 1 132 ? -5.265  -2.847  59.992  1.00 57.31  ? 104 LEU A CG    1 
ATOM   848  C  CD1   . LEU A 1 132 ? -5.682  -1.389  60.114  1.00 53.77  ? 104 LEU A CD1   1 
ATOM   849  C  CD2   . LEU A 1 132 ? -6.400  -3.690  59.408  1.00 53.35  ? 104 LEU A CD2   1 
ATOM   850  N  N     . ILE A 1 133 ? -1.231  -4.221  57.781  1.00 35.26  ? 105 ILE A N     1 
ATOM   851  C  CA    . ILE A 1 133 ? -0.319  -4.031  56.662  1.00 35.62  ? 105 ILE A CA    1 
ATOM   852  C  C     . ILE A 1 133 ? -0.206  -5.285  55.787  1.00 36.83  ? 105 ILE A C     1 
ATOM   853  O  O     . ILE A 1 133 ? 0.100   -5.161  54.589  1.00 36.66  ? 105 ILE A O     1 
ATOM   854  C  CB    . ILE A 1 133 ? 1.040   -3.542  57.205  1.00 40.85  ? 105 ILE A CB    1 
ATOM   855  C  CG1   . ILE A 1 133 ? 0.852   -2.143  57.820  1.00 47.35  ? 105 ILE A CG1   1 
ATOM   856  C  CG2   . ILE A 1 133 ? 2.100   -3.484  56.119  1.00 41.52  ? 105 ILE A CG2   1 
ATOM   857  C  CD1   . ILE A 1 133 ? 2.117   -1.315  57.924  1.00 50.72  ? 105 ILE A CD1   1 
ATOM   858  N  N     . ARG A 1 134 ? -0.500  -6.481  56.324  1.00 33.75  ? 106 ARG A N     1 
ATOM   859  C  CA    . ARG A 1 134 ? -0.342  -7.695  55.518  1.00 34.02  ? 106 ARG A CA    1 
ATOM   860  C  C     . ARG A 1 134 ? -1.136  -7.668  54.210  1.00 34.47  ? 106 ARG A C     1 
ATOM   861  O  O     . ARG A 1 134 ? -0.541  -7.937  53.151  1.00 35.07  ? 106 ARG A O     1 
ATOM   862  C  CB    . ARG A 1 134 ? -0.701  -8.938  56.344  1.00 36.82  ? 106 ARG A CB    1 
ATOM   863  C  CG    . ARG A 1 134 ? -0.456  -10.253 55.580  1.00 44.51  ? 106 ARG A CG    1 
ATOM   864  C  CD    . ARG A 1 134 ? -0.576  -11.501 56.462  1.00 51.78  ? 106 ARG A CD    1 
ATOM   865  N  NE    . ARG A 1 134 ? -1.959  -11.799 56.823  1.00 57.61  ? 106 ARG A NE    1 
ATOM   866  C  CZ    . ARG A 1 134 ? -2.760  -12.614 56.147  1.00 57.13  ? 106 ARG A CZ    1 
ATOM   867  N  NH1   . ARG A 1 134 ? -2.352  -13.235 55.053  1.00 47.71  ? 106 ARG A NH1   1 
ATOM   868  N  NH2   . ARG A 1 134 ? -3.996  -12.826 56.592  1.00 57.94  ? 106 ARG A NH2   1 
ATOM   869  N  N     . PRO A 1 135 ? -2.440  -7.384  54.187  1.00 36.23  ? 107 PRO A N     1 
ATOM   870  C  CA    . PRO A 1 135 ? -3.121  -7.345  52.882  1.00 37.87  ? 107 PRO A CA    1 
ATOM   871  C  C     . PRO A 1 135 ? -2.647  -6.202  51.999  1.00 38.67  ? 107 PRO A C     1 
ATOM   872  O  O     . PRO A 1 135 ? -2.709  -6.310  50.768  1.00 36.26  ? 107 PRO A O     1 
ATOM   873  C  CB    . PRO A 1 135 ? -4.605  -7.206  53.258  1.00 40.30  ? 107 PRO A CB    1 
ATOM   874  C  CG    . PRO A 1 135 ? -4.597  -6.606  54.627  1.00 38.04  ? 107 PRO A CG    1 
ATOM   875  C  CD    . PRO A 1 135 ? -3.396  -7.193  55.300  1.00 36.94  ? 107 PRO A CD    1 
ATOM   876  N  N     . ILE A 1 136 ? -2.169  -5.103  52.591  1.00 34.04  ? 108 ILE A N     1 
ATOM   877  C  CA    . ILE A 1 136 ? -1.632  -3.999  51.795  1.00 36.51  ? 108 ILE A CA    1 
ATOM   878  C  C     . ILE A 1 136 ? -0.376  -4.433  51.030  1.00 35.81  ? 108 ILE A C     1 
ATOM   879  O  O     . ILE A 1 136 ? -0.185  -4.059  49.861  1.00 37.87  ? 108 ILE A O     1 
ATOM   880  C  CB    . ILE A 1 136 ? -1.363  -2.776  52.695  1.00 40.36  ? 108 ILE A CB    1 
ATOM   881  C  CG1   . ILE A 1 136 ? -2.670  -2.259  53.310  1.00 40.96  ? 108 ILE A CG1   1 
ATOM   882  C  CG2   . ILE A 1 136 ? -0.660  -1.669  51.893  1.00 41.19  ? 108 ILE A CG2   1 
ATOM   883  C  CD1   . ILE A 1 136 ? -2.474  -1.103  54.322  1.00 43.83  ? 108 ILE A CD1   1 
ATOM   884  N  N     . LYS A 1 137 ? 0.505   -5.222  51.666  1.00 33.57  ? 109 LYS A N     1 
ATOM   885  C  CA    . LYS A 1 137 ? 1.678   -5.730  50.945  1.00 35.32  ? 109 LYS A CA    1 
ATOM   886  C  C     . LYS A 1 137 ? 1.267   -6.576  49.740  1.00 39.13  ? 109 LYS A C     1 
ATOM   887  O  O     . LYS A 1 137 ? 1.890   -6.500  48.673  1.00 40.26  ? 109 LYS A O     1 
ATOM   888  C  CB    . LYS A 1 137 ? 2.577   -6.549  51.882  1.00 36.45  ? 109 LYS A CB    1 
ATOM   889  C  CG    . LYS A 1 137 ? 3.364   -5.696  52.883  1.00 35.86  ? 109 LYS A CG    1 
ATOM   890  C  CD    . LYS A 1 137 ? 3.783   -6.506  54.115  1.00 39.94  ? 109 LYS A CD    1 
ATOM   891  C  CE    . LYS A 1 137 ? 4.791   -7.588  53.760  1.00 42.91  ? 109 LYS A CE    1 
ATOM   892  N  NZ    . LYS A 1 137 ? 5.452   -8.136  55.008  1.00 45.02  ? 109 LYS A NZ    1 
ATOM   893  N  N     . VAL A 1 138 ? 0.242   -7.414  49.900  1.00 39.61  ? 110 VAL A N     1 
ATOM   894  C  CA    . VAL A 1 138 ? -0.213  -8.224  48.769  1.00 38.66  ? 110 VAL A CA    1 
ATOM   895  C  C     . VAL A 1 138 ? -0.696  -7.328  47.638  1.00 45.32  ? 110 VAL A C     1 
ATOM   896  O  O     . VAL A 1 138 ? -0.373  -7.545  46.464  1.00 40.33  ? 110 VAL A O     1 
ATOM   897  C  CB    . VAL A 1 138 ? -1.322  -9.194  49.217  1.00 38.88  ? 110 VAL A CB    1 
ATOM   898  C  CG1   . VAL A 1 138 ? -1.836  -10.005 48.012  1.00 44.90  ? 110 VAL A CG1   1 
ATOM   899  C  CG2   . VAL A 1 138 ? -0.836  -10.104 50.330  1.00 42.90  ? 110 VAL A CG2   1 
ATOM   900  N  N     . LEU A 1 139 ? -1.483  -6.306  47.978  1.00 39.88  ? 111 LEU A N     1 
ATOM   901  C  CA    . LEU A 1 139 ? -2.011  -5.391  46.973  1.00 38.42  ? 111 LEU A CA    1 
ATOM   902  C  C     . LEU A 1 139 ? -0.904  -4.619  46.265  1.00 43.78  ? 111 LEU A C     1 
ATOM   903  O  O     . LEU A 1 139 ? -0.940  -4.457  45.039  1.00 41.80  ? 111 LEU A O     1 
ATOM   904  C  CB    . LEU A 1 139 ? -2.992  -4.426  47.638  1.00 45.29  ? 111 LEU A CB    1 
ATOM   905  C  CG    . LEU A 1 139 ? -4.175  -3.898  46.848  1.00 58.31  ? 111 LEU A CG    1 
ATOM   906  C  CD1   . LEU A 1 139 ? -5.091  -5.043  46.432  1.00 49.97  ? 111 LEU A CD1   1 
ATOM   907  C  CD2   . LEU A 1 139 ? -4.901  -2.889  47.725  1.00 50.47  ? 111 LEU A CD2   1 
ATOM   908  N  N     . LEU A 1 140 ? 0.076   -4.103  47.018  1.00 42.24  ? 112 LEU A N     1 
ATOM   909  C  CA    . LEU A 1 140 ? 1.182   -3.370  46.395  1.00 38.50  ? 112 LEU A CA    1 
ATOM   910  C  C     . LEU A 1 140 ? 1.953   -4.247  45.409  1.00 44.12  ? 112 LEU A C     1 
ATOM   911  O  O     . LEU A 1 140 ? 2.343   -3.793  44.327  1.00 43.15  ? 112 LEU A O     1 
ATOM   912  C  CB    . LEU A 1 140 ? 2.143   -2.852  47.474  1.00 44.62  ? 112 LEU A CB    1 
ATOM   913  C  CG    . LEU A 1 140 ? 1.884   -1.470  48.066  1.00 44.98  ? 112 LEU A CG    1 
ATOM   914  C  CD1   . LEU A 1 140 ? 2.853   -1.232  49.217  1.00 48.96  ? 112 LEU A CD1   1 
ATOM   915  C  CD2   . LEU A 1 140 ? 2.006   -0.370  47.014  1.00 47.59  ? 112 LEU A CD2   1 
ATOM   916  N  N     . GLN A 1 141 ? 2.220   -5.494  45.788  1.00 37.55  ? 113 GLN A N     1 
ATOM   917  C  CA    . GLN A 1 141 ? 2.962   -6.388  44.913  1.00 38.25  ? 113 GLN A CA    1 
ATOM   918  C  C     . GLN A 1 141 ? 2.175   -6.676  43.634  1.00 42.65  ? 113 GLN A C     1 
ATOM   919  O  O     . GLN A 1 141 ? 2.743   -6.697  42.535  1.00 40.07  ? 113 GLN A O     1 
ATOM   920  C  CB    . GLN A 1 141 ? 3.282   -7.674  45.676  1.00 46.62  ? 113 GLN A CB    1 
ATOM   921  C  CG    . GLN A 1 141 ? 4.044   -8.726  44.889  1.00 60.00  ? 113 GLN A CG    1 
ATOM   922  C  CD    . GLN A 1 141 ? 5.175   -9.330  45.703  1.00 62.88  ? 113 GLN A CD    1 
ATOM   923  O  OE1   . GLN A 1 141 ? 4.973   -9.743  46.847  1.00 69.00  ? 113 GLN A OE1   1 
ATOM   924  N  NE2   . GLN A 1 141 ? 6.368   -9.395  45.117  1.00 68.68  ? 113 GLN A NE2   1 
ATOM   925  N  N     . THR A 1 142 ? 0.857   -6.875  43.754  1.00 46.60  ? 114 THR A N     1 
ATOM   926  C  CA    . THR A 1 142 ? 0.050   -7.189  42.574  1.00 40.51  ? 114 THR A CA    1 
ATOM   927  C  C     . THR A 1 142 ? -0.041  -5.996  41.624  1.00 45.34  ? 114 THR A C     1 
ATOM   928  O  O     . THR A 1 142 ? 0.059   -6.164  40.402  1.00 43.54  ? 114 THR A O     1 
ATOM   929  C  CB    . THR A 1 142 ? -1.348  -7.653  42.996  1.00 37.57  ? 114 THR A CB    1 
ATOM   930  O  OG1   . THR A 1 142 ? -1.245  -8.875  43.726  1.00 45.25  ? 114 THR A OG1   1 
ATOM   931  C  CG2   . THR A 1 142 ? -2.223  -7.913  41.743  1.00 41.80  ? 114 THR A CG2   1 
ATOM   932  N  N     . LEU A 1 143 ? -0.222  -4.779  42.160  1.00 38.00  ? 115 LEU A N     1 
ATOM   933  C  CA    . LEU A 1 143 ? -0.267  -3.594  41.301  1.00 39.78  ? 115 LEU A CA    1 
ATOM   934  C  C     . LEU A 1 143 ? 1.050   -3.362  40.563  1.00 46.66  ? 115 LEU A C     1 
ATOM   935  O  O     . LEU A 1 143 ? 1.045   -2.993  39.382  1.00 44.36  ? 115 LEU A O     1 
ATOM   936  C  CB    . LEU A 1 143 ? -0.617  -2.344  42.107  1.00 43.68  ? 115 LEU A CB    1 
ATOM   937  C  CG    . LEU A 1 143 ? -2.082  -1.953  42.292  1.00 51.39  ? 115 LEU A CG    1 
ATOM   938  C  CD1   . LEU A 1 143 ? -2.201  -0.978  43.464  1.00 57.44  ? 115 LEU A CD1   1 
ATOM   939  C  CD2   . LEU A 1 143 ? -2.628  -1.341  41.014  1.00 48.30  ? 115 LEU A CD2   1 
ATOM   940  N  N     . THR A 1 144 ? 2.192   -3.519  41.242  1.00 41.37  ? 116 THR A N     1 
ATOM   941  C  CA    A THR A 1 144 ? 3.472   -3.273  40.581  0.61 40.24  ? 116 THR A CA    1 
ATOM   942  C  CA    B THR A 1 144 ? 3.461   -3.262  40.568  0.39 40.31  ? 116 THR A CA    1 
ATOM   943  C  C     . THR A 1 144 ? 3.751   -4.308  39.497  1.00 41.47  ? 116 THR A C     1 
ATOM   944  O  O     . THR A 1 144 ? 4.328   -3.978  38.457  1.00 45.98  ? 116 THR A O     1 
ATOM   945  C  CB    A THR A 1 144 ? 4.610   -3.254  41.605  0.61 47.24  ? 116 THR A CB    1 
ATOM   946  C  CB    B THR A 1 144 ? 4.611   -3.174  41.585  0.39 47.19  ? 116 THR A CB    1 
ATOM   947  O  OG1   A THR A 1 144 ? 4.723   -4.538  42.225  0.61 51.99  ? 116 THR A OG1   1 
ATOM   948  O  OG1   B THR A 1 144 ? 5.800   -2.720  40.929  0.39 42.02  ? 116 THR A OG1   1 
ATOM   949  C  CG2   A THR A 1 144 ? 4.343   -2.216  42.659  0.61 33.56  ? 116 THR A CG2   1 
ATOM   950  C  CG2   B THR A 1 144 ? 4.890   -4.509  42.243  0.39 51.52  ? 116 THR A CG2   1 
ATOM   951  N  N     . GLU A 1 145 ? 3.346   -5.561  39.719  1.00 42.95  ? 117 GLU A N     1 
ATOM   952  C  CA    . GLU A 1 145 ? 3.562   -6.594  38.709  1.00 47.79  ? 117 GLU A CA    1 
ATOM   953  C  C     . GLU A 1 145 ? 2.690   -6.352  37.479  1.00 55.63  ? 117 GLU A C     1 
ATOM   954  O  O     . GLU A 1 145 ? 3.171   -6.460  36.343  1.00 45.48  ? 117 GLU A O     1 
ATOM   955  C  CB    . GLU A 1 145 ? 3.306   -7.977  39.305  1.00 47.37  ? 117 GLU A CB    1 
ATOM   956  N  N     . SER A 1 146 ? 1.413   -5.999  37.678  1.00 46.98  ? 118 SER A N     1 
ATOM   957  C  CA    A SER A 1 146 ? 0.565   -5.638  36.542  0.65 46.58  ? 118 SER A CA    1 
ATOM   958  C  CA    B SER A 1 146 ? 0.568   -5.641  36.541  0.35 46.60  ? 118 SER A CA    1 
ATOM   959  C  C     . SER A 1 146 ? 1.147   -4.454  35.784  1.00 46.77  ? 118 SER A C     1 
ATOM   960  O  O     . SER A 1 146 ? 1.154   -4.438  34.544  1.00 46.89  ? 118 SER A O     1 
ATOM   961  C  CB    A SER A 1 146 ? -0.860  -5.329  37.019  0.65 48.56  ? 118 SER A CB    1 
ATOM   962  C  CB    B SER A 1 146 ? -0.855  -5.330  37.011  0.35 48.52  ? 118 SER A CB    1 
ATOM   963  O  OG    A SER A 1 146 ? -1.601  -4.642  36.022  0.65 48.68  ? 118 SER A OG    1 
ATOM   964  O  OG    B SER A 1 146 ? -1.160  -6.010  38.211  0.35 45.39  ? 118 SER A OG    1 
ATOM   965  N  N     . HIS A 1 147 ? 1.646   -3.455  36.515  1.00 47.27  ? 119 HIS A N     1 
ATOM   966  C  CA    . HIS A 1 147 ? 2.289   -2.305  35.890  1.00 42.06  ? 119 HIS A CA    1 
ATOM   967  C  C     . HIS A 1 147 ? 3.460   -2.717  35.002  1.00 47.33  ? 119 HIS A C     1 
ATOM   968  O  O     . HIS A 1 147 ? 3.639   -2.176  33.903  1.00 50.17  ? 119 HIS A O     1 
ATOM   969  C  CB    . HIS A 1 147 ? 2.772   -1.341  36.968  1.00 47.45  ? 119 HIS A CB    1 
ATOM   970  C  CG    . HIS A 1 147 ? 2.754   0.089   36.548  1.00 47.45  ? 119 HIS A CG    1 
ATOM   971  N  ND1   . HIS A 1 147 ? 3.793   0.671   35.855  1.00 49.60  ? 119 HIS A ND1   1 
ATOM   972  C  CD2   . HIS A 1 147 ? 1.830   1.058   36.729  1.00 45.75  ? 119 HIS A CD2   1 
ATOM   973  C  CE1   . HIS A 1 147 ? 3.504   1.939   35.622  1.00 49.03  ? 119 HIS A CE1   1 
ATOM   974  N  NE2   . HIS A 1 147 ? 2.315   2.196   36.137  1.00 50.28  ? 119 HIS A NE2   1 
ATOM   975  N  N     . ARG A 1 148 ? 4.294   -3.642  35.477  1.00 45.63  ? 120 ARG A N     1 
ATOM   976  C  CA    . ARG A 1 148 ? 5.462   -4.046  34.695  1.00 49.95  ? 120 ARG A CA    1 
ATOM   977  C  C     . ARG A 1 148 ? 5.057   -4.767  33.409  1.00 52.29  ? 120 ARG A C     1 
ATOM   978  O  O     . ARG A 1 148 ? 5.770   -4.680  32.403  1.00 52.89  ? 120 ARG A O     1 
ATOM   979  C  CB    . ARG A 1 148 ? 6.386   -4.921  35.549  1.00 49.17  ? 120 ARG A CB    1 
ATOM   980  C  CG    . ARG A 1 148 ? 7.068   -4.186  36.726  1.00 53.32  ? 120 ARG A CG    1 
ATOM   981  C  CD    . ARG A 1 148 ? 7.769   -2.898  36.276  1.00 59.76  ? 120 ARG A CD    1 
ATOM   982  N  NE    . ARG A 1 148 ? 8.854   -2.490  37.166  1.00 52.69  ? 120 ARG A NE    1 
ATOM   983  C  CZ    . ARG A 1 148 ? 9.782   -1.587  36.864  1.00 55.83  ? 120 ARG A CZ    1 
ATOM   984  N  NH1   . ARG A 1 148 ? 9.815   -0.992  35.683  1.00 50.70  ? 120 ARG A NH1   1 
ATOM   985  N  NH2   . ARG A 1 148 ? 10.701  -1.269  37.773  1.00 52.15  ? 120 ARG A NH2   1 
ATOM   986  N  N     . ILE A 1 149 ? 3.924   -5.474  33.415  1.00 46.97  ? 121 ILE A N     1 
ATOM   987  C  CA    . ILE A 1 149 ? 3.422   -6.085  32.183  1.00 47.89  ? 121 ILE A CA    1 
ATOM   988  C  C     . ILE A 1 149 ? 2.967   -5.011  31.203  1.00 54.94  ? 121 ILE A C     1 
ATOM   989  O  O     . ILE A 1 149 ? 3.358   -5.009  30.029  1.00 53.08  ? 121 ILE A O     1 
ATOM   990  C  CB    . ILE A 1 149 ? 2.285   -7.072  32.497  1.00 54.51  ? 121 ILE A CB    1 
ATOM   991  C  CG1   . ILE A 1 149 ? 2.816   -8.278  33.272  1.00 51.68  ? 121 ILE A CG1   1 
ATOM   992  C  CG2   . ILE A 1 149 ? 1.590   -7.511  31.213  1.00 58.81  ? 121 ILE A CG2   1 
ATOM   993  C  CD1   . ILE A 1 149 ? 1.739   -9.058  33.979  1.00 60.81  ? 121 ILE A CD1   1 
ATOM   994  N  N     . LEU A 1 150 ? 2.114   -4.095  31.669  1.00 47.79  ? 122 LEU A N     1 
ATOM   995  C  CA    . LEU A 1 150 ? 1.648   -2.980  30.846  1.00 52.00  ? 122 LEU A CA    1 
ATOM   996  C  C     . LEU A 1 150 ? 2.800   -2.176  30.258  1.00 59.47  ? 122 LEU A C     1 
ATOM   997  O  O     . LEU A 1 150 ? 2.683   -1.640  29.148  1.00 50.56  ? 122 LEU A O     1 
ATOM   998  C  CB    . LEU A 1 150 ? 0.760   -2.048  31.679  1.00 50.94  ? 122 LEU A CB    1 
ATOM   999  C  CG    . LEU A 1 150 ? -0.734  -2.292  31.888  1.00 57.30  ? 122 LEU A CG    1 
ATOM   1000 C  CD1   . LEU A 1 150 ? -1.505  -1.693  30.745  1.00 66.67  ? 122 LEU A CD1   1 
ATOM   1001 C  CD2   . LEU A 1 150 ? -1.064  -3.770  32.032  1.00 63.42  ? 122 LEU A CD2   1 
ATOM   1002 N  N     . GLU A 1 151 ? 3.909   -2.059  30.995  1.00 46.09  ? 123 GLU A N     1 
ATOM   1003 C  CA    . GLU A 1 151 ? 5.058   -1.309  30.500  1.00 45.20  ? 123 GLU A CA    1 
ATOM   1004 C  C     . GLU A 1 151 ? 5.545   -1.853  29.158  1.00 48.26  ? 123 GLU A C     1 
ATOM   1005 O  O     . GLU A 1 151 ? 5.955   -1.084  28.285  1.00 46.27  ? 123 GLU A O     1 
ATOM   1006 C  CB    . GLU A 1 151 ? 6.187   -1.351  31.538  1.00 49.85  ? 123 GLU A CB    1 
ATOM   1007 C  CG    . GLU A 1 151 ? 7.419   -0.525  31.187  1.00 61.62  ? 123 GLU A CG    1 
ATOM   1008 C  CD    . GLU A 1 151 ? 8.561   -0.694  32.200  1.00 69.92  ? 123 GLU A CD    1 
ATOM   1009 O  OE1   . GLU A 1 151 ? 8.361   -1.345  33.256  1.00 60.76  ? 123 GLU A OE1   1 
ATOM   1010 O  OE2   . GLU A 1 151 ? 9.665   -0.178  31.933  1.00 63.88  ? 123 GLU A OE2   1 
ATOM   1011 N  N     . LYS A 1 152 ? 5.497   -3.171  28.974  1.00 43.62  ? 124 LYS A N     1 
ATOM   1012 C  CA    . LYS A 1 152 ? 6.081   -3.768  27.773  1.00 48.36  ? 124 LYS A CA    1 
ATOM   1013 C  C     . LYS A 1 152 ? 5.232   -3.522  26.532  1.00 53.48  ? 124 LYS A C     1 
ATOM   1014 O  O     . LYS A 1 152 ? 5.764   -3.508  25.414  1.00 53.16  ? 124 LYS A O     1 
ATOM   1015 C  CB    . LYS A 1 152 ? 6.279   -5.271  27.974  1.00 46.26  ? 124 LYS A CB    1 
ATOM   1016 C  CG    . LYS A 1 152 ? 7.321   -5.631  29.006  1.00 53.23  ? 124 LYS A CG    1 
ATOM   1017 C  CD    . LYS A 1 152 ? 8.600   -4.842  28.771  1.00 61.21  ? 124 LYS A CD    1 
ATOM   1018 C  CE    . LYS A 1 152 ? 9.737   -5.386  29.617  1.00 67.37  ? 124 LYS A CE    1 
ATOM   1019 N  NZ    . LYS A 1 152 ? 9.497   -6.816  29.966  1.00 74.56  ? 124 LYS A NZ    1 
ATOM   1020 N  N     . TYR A 1 153 ? 3.922   -3.338  26.700  1.00 53.62  ? 125 TYR A N     1 
ATOM   1021 C  CA    . TYR A 1 153 ? 2.990   -3.157  25.592  1.00 55.09  ? 125 TYR A CA    1 
ATOM   1022 C  C     . TYR A 1 153 ? 2.685   -1.698  25.286  1.00 57.87  ? 125 TYR A C     1 
ATOM   1023 O  O     . TYR A 1 153 ? 1.770   -1.429  24.503  1.00 63.52  ? 125 TYR A O     1 
ATOM   1024 C  CB    . TYR A 1 153 ? 1.679   -3.895  25.873  1.00 44.87  ? 125 TYR A CB    1 
ATOM   1025 C  CG    . TYR A 1 153 ? 1.828   -5.386  25.943  1.00 52.27  ? 125 TYR A CG    1 
ATOM   1026 C  CD1   . TYR A 1 153 ? 1.819   -6.155  24.787  1.00 42.30  ? 125 TYR A CD1   1 
ATOM   1027 C  CD2   . TYR A 1 153 ? 1.994   -6.028  27.158  1.00 48.27  ? 125 TYR A CD2   1 
ATOM   1028 C  CE1   . TYR A 1 153 ? 1.971   -7.522  24.842  1.00 42.88  ? 125 TYR A CE1   1 
ATOM   1029 C  CE2   . TYR A 1 153 ? 2.150   -7.400  27.226  1.00 56.62  ? 125 TYR A CE2   1 
ATOM   1030 C  CZ    . TYR A 1 153 ? 2.137   -8.141  26.063  1.00 50.75  ? 125 TYR A CZ    1 
ATOM   1031 O  OH    . TYR A 1 153 ? 2.284   -9.501  26.123  1.00 63.63  ? 125 TYR A OH    1 
ATOM   1032 N  N     . THR A 1 154 ? 3.405   -0.749  25.882  1.00 53.26  ? 126 THR A N     1 
ATOM   1033 C  CA    A THR A 1 154 ? 3.178   0.668   25.634  0.73 62.80  ? 126 THR A CA    1 
ATOM   1034 C  CA    B THR A 1 154 ? 3.177   0.667   25.631  0.27 62.80  ? 126 THR A CA    1 
ATOM   1035 C  C     . THR A 1 154 ? 4.423   1.310   25.036  1.00 64.38  ? 126 THR A C     1 
ATOM   1036 O  O     . THR A 1 154 ? 5.553   0.901   25.319  1.00 65.05  ? 126 THR A O     1 
ATOM   1037 C  CB    A THR A 1 154 ? 2.775   1.416   26.922  0.73 66.52  ? 126 THR A CB    1 
ATOM   1038 C  CB    B THR A 1 154 ? 2.770   1.407   26.915  0.27 66.38  ? 126 THR A CB    1 
ATOM   1039 O  OG1   A THR A 1 154 ? 3.624   1.016   28.002  0.73 66.88  ? 126 THR A OG1   1 
ATOM   1040 O  OG1   B THR A 1 154 ? 2.679   2.813   26.654  0.27 65.25  ? 126 THR A OG1   1 
ATOM   1041 C  CG2   A THR A 1 154 ? 1.330   1.131   27.282  0.73 60.23  ? 126 THR A CG2   1 
ATOM   1042 C  CG2   B THR A 1 154 ? 3.782   1.168   28.006  0.27 66.07  ? 126 THR A CG2   1 
ATOM   1043 N  N     . GLN A 1 155 ? 4.199   2.328   24.203  1.00 71.76  ? 127 GLN A N     1 
ATOM   1044 C  CA    . GLN A 1 155 ? 5.238   3.093   23.516  1.00 77.31  ? 127 GLN A CA    1 
ATOM   1045 C  C     . GLN A 1 155 ? 6.222   3.669   24.526  1.00 80.18  ? 127 GLN A C     1 
ATOM   1046 O  O     . GLN A 1 155 ? 5.912   3.701   25.725  1.00 77.84  ? 127 GLN A O     1 
ATOM   1047 C  CB    . GLN A 1 155 ? 4.592   4.221   22.710  1.00 78.32  ? 127 GLN A CB    1 
ATOM   1048 C  CG    . GLN A 1 155 ? 4.701   4.098   21.207  1.00 77.27  ? 127 GLN A CG    1 
ATOM   1049 C  CD    . GLN A 1 155 ? 4.268   5.376   20.509  1.00 79.49  ? 127 GLN A CD    1 
ATOM   1050 O  OE1   . GLN A 1 155 ? 4.672   6.474   20.888  1.00 80.64  ? 127 GLN A OE1   1 
ATOM   1051 N  NE2   . GLN A 1 155 ? 3.400   5.238   19.510  1.00 73.44  ? 127 GLN A NE2   1 
ATOM   1052 N  N     . PRO A 1 156 ? 7.387   4.194   24.100  1.00 78.85  ? 128 PRO A N     1 
ATOM   1053 C  CA    . PRO A 1 156 ? 8.243   4.913   25.057  1.00 64.54  ? 128 PRO A CA    1 
ATOM   1054 C  C     . PRO A 1 156 ? 7.939   6.406   25.175  1.00 65.35  ? 128 PRO A C     1 
ATOM   1055 O  O     . PRO A 1 156 ? 8.366   7.034   26.148  1.00 63.78  ? 128 PRO A O     1 
ATOM   1056 C  CB    . PRO A 1 156 ? 9.656   4.664   24.512  1.00 73.31  ? 128 PRO A CB    1 
ATOM   1057 C  CG    . PRO A 1 156 ? 9.463   4.528   23.041  1.00 73.93  ? 128 PRO A CG    1 
ATOM   1058 C  CD    . PRO A 1 156 ? 8.082   3.930   22.825  1.00 78.98  ? 128 PRO A CD    1 
ATOM   1059 N  N     . SER A 1 157 ? 7.198   6.987   24.220  1.00 64.11  ? 129 SER A N     1 
ATOM   1060 C  CA    . SER A 1 157 ? 6.862   8.412   24.299  1.00 66.97  ? 129 SER A CA    1 
ATOM   1061 C  C     . SER A 1 157 ? 6.060   8.746   25.548  1.00 52.07  ? 129 SER A C     1 
ATOM   1062 O  O     . SER A 1 157 ? 6.288   9.788   26.168  1.00 57.36  ? 129 SER A O     1 
ATOM   1063 C  CB    . SER A 1 157 ? 6.058   8.871   23.078  1.00 66.11  ? 129 SER A CB    1 
ATOM   1064 O  OG    . SER A 1 157 ? 6.787   8.769   21.883  1.00 76.50  ? 129 SER A OG    1 
ATOM   1065 N  N     . ILE A 1 158 ? 5.063   7.918   25.881  1.00 59.83  ? 130 ILE A N     1 
ATOM   1066 C  CA    . ILE A 1 158 ? 4.183   8.206   27.013  1.00 55.92  ? 130 ILE A CA    1 
ATOM   1067 C  C     . ILE A 1 158 ? 5.005   8.384   28.281  1.00 48.39  ? 130 ILE A C     1 
ATOM   1068 O  O     . ILE A 1 158 ? 4.784   9.321   29.057  1.00 53.39  ? 130 ILE A O     1 
ATOM   1069 C  CB    . ILE A 1 158 ? 3.127   7.090   27.176  1.00 58.11  ? 130 ILE A CB    1 
ATOM   1070 C  CG1   . ILE A 1 158 ? 2.259   6.953   25.913  1.00 60.68  ? 130 ILE A CG1   1 
ATOM   1071 C  CG2   . ILE A 1 158 ? 2.261   7.326   28.409  1.00 55.27  ? 130 ILE A CG2   1 
ATOM   1072 C  CD1   . ILE A 1 158 ? 1.930   8.261   25.247  1.00 51.41  ? 130 ILE A CD1   1 
ATOM   1073 N  N     . PHE A 1 159 ? 5.983   7.502   28.496  1.00 53.23  ? 131 PHE A N     1 
ATOM   1074 C  CA    . PHE A 1 159 ? 6.797   7.592   29.705  1.00 52.20  ? 131 PHE A CA    1 
ATOM   1075 C  C     . PHE A 1 159 ? 7.677   8.832   29.691  1.00 58.13  ? 131 PHE A C     1 
ATOM   1076 O  O     . PHE A 1 159 ? 7.889   9.457   30.738  1.00 52.07  ? 131 PHE A O     1 
ATOM   1077 C  CB    . PHE A 1 159 ? 7.637   6.333   29.864  1.00 50.35  ? 131 PHE A CB    1 
ATOM   1078 C  CG    . PHE A 1 159 ? 6.826   5.115   30.173  1.00 58.78  ? 131 PHE A CG    1 
ATOM   1079 C  CD1   . PHE A 1 159 ? 5.895   5.138   31.202  1.00 54.01  ? 131 PHE A CD1   1 
ATOM   1080 C  CD2   . PHE A 1 159 ? 6.993   3.948   29.449  1.00 59.97  ? 131 PHE A CD2   1 
ATOM   1081 C  CE1   . PHE A 1 159 ? 5.140   4.024   31.496  1.00 56.14  ? 131 PHE A CE1   1 
ATOM   1082 C  CE2   . PHE A 1 159 ? 6.242   2.826   29.744  1.00 60.61  ? 131 PHE A CE2   1 
ATOM   1083 C  CZ    . PHE A 1 159 ? 5.312   2.868   30.771  1.00 57.02  ? 131 PHE A CZ    1 
ATOM   1084 N  N     . LYS A 1 160 ? 8.189   9.209   28.512  1.00 58.04  ? 132 LYS A N     1 
ATOM   1085 C  CA    . LYS A 1 160 ? 8.946   10.452  28.390  1.00 55.68  ? 132 LYS A CA    1 
ATOM   1086 C  C     . LYS A 1 160 ? 8.094   11.655  28.763  1.00 55.17  ? 132 LYS A C     1 
ATOM   1087 O  O     . LYS A 1 160 ? 8.540   12.533  29.504  1.00 52.51  ? 132 LYS A O     1 
ATOM   1088 C  CB    . LYS A 1 160 ? 9.494   10.610  26.969  1.00 61.47  ? 132 LYS A CB    1 
ATOM   1089 C  CG    . LYS A 1 160 ? 10.823  9.930   26.728  1.00 74.12  ? 132 LYS A CG    1 
ATOM   1090 C  CD    . LYS A 1 160 ? 11.418  10.350  25.384  1.00 79.26  ? 132 LYS A CD    1 
ATOM   1091 C  CE    . LYS A 1 160 ? 11.529  9.170   24.432  1.00 81.50  ? 132 LYS A CE    1 
ATOM   1092 N  NZ    . LYS A 1 160 ? 11.908  7.916   25.147  1.00 80.01  ? 132 LYS A NZ    1 
ATOM   1093 N  N     . ILE A 1 161 ? 6.857   11.717  28.265  1.00 52.21  ? 133 ILE A N     1 
ATOM   1094 C  CA    . ILE A 1 161 ? 5.988   12.837  28.616  1.00 48.91  ? 133 ILE A CA    1 
ATOM   1095 C  C     . ILE A 1 161 ? 5.690   12.842  30.111  1.00 50.45  ? 133 ILE A C     1 
ATOM   1096 O  O     . ILE A 1 161 ? 5.569   13.903  30.732  1.00 49.61  ? 133 ILE A O     1 
ATOM   1097 C  CB    . ILE A 1 161 ? 4.692   12.801  27.784  1.00 58.32  ? 133 ILE A CB    1 
ATOM   1098 C  CG1   . ILE A 1 161 ? 5.007   12.619  26.299  1.00 59.69  ? 133 ILE A CG1   1 
ATOM   1099 C  CG2   . ILE A 1 161 ? 3.885   14.061  28.013  1.00 61.93  ? 133 ILE A CG2   1 
ATOM   1100 C  CD1   . ILE A 1 161 ? 3.899   11.929  25.515  1.00 63.14  ? 133 ILE A CD1   1 
ATOM   1101 N  N     . ILE A 1 162 ? 5.556   11.659  30.711  1.00 52.94  ? 134 ILE A N     1 
ATOM   1102 C  CA    . ILE A 1 162 ? 5.253   11.590  32.140  1.00 48.68  ? 134 ILE A CA    1 
ATOM   1103 C  C     . ILE A 1 162 ? 6.397   12.181  32.962  1.00 44.78  ? 134 ILE A C     1 
ATOM   1104 O  O     . ILE A 1 162 ? 6.164   12.948  33.904  1.00 46.64  ? 134 ILE A O     1 
ATOM   1105 C  CB    . ILE A 1 162 ? 4.930   10.139  32.546  1.00 48.06  ? 134 ILE A CB    1 
ATOM   1106 C  CG1   . ILE A 1 162 ? 3.531   9.752   32.040  1.00 44.51  ? 134 ILE A CG1   1 
ATOM   1107 C  CG2   . ILE A 1 162 ? 5.030   9.963   34.068  1.00 48.83  ? 134 ILE A CG2   1 
ATOM   1108 C  CD1   . ILE A 1 162 ? 3.251   8.269   32.074  1.00 51.87  ? 134 ILE A CD1   1 
ATOM   1109 N  N     . SER A 1 163 ? 7.649   11.876  32.595  1.00 52.55  ? 135 SER A N     1 
ATOM   1110 C  CA    . SER A 1 163 ? 8.785   12.388  33.364  1.00 53.61  ? 135 SER A CA    1 
ATOM   1111 C  C     . SER A 1 163 ? 8.936   13.903  33.271  1.00 60.23  ? 135 SER A C     1 
ATOM   1112 O  O     . SER A 1 163 ? 9.599   14.496  34.128  1.00 62.06  ? 135 SER A O     1 
ATOM   1113 C  CB    . SER A 1 163 ? 10.089  11.729  32.916  1.00 57.26  ? 135 SER A CB    1 
ATOM   1114 O  OG    . SER A 1 163 ? 9.897   10.368  32.586  1.00 67.20  ? 135 SER A OG    1 
ATOM   1115 N  N     . GLN A 1 164 ? 8.348   14.543  32.262  1.00 57.95  ? 136 GLN A N     1 
ATOM   1116 C  CA    . GLN A 1 164 ? 8.405   15.996  32.131  1.00 56.73  ? 136 GLN A CA    1 
ATOM   1117 C  C     . GLN A 1 164 ? 7.327   16.708  32.938  1.00 61.26  ? 136 GLN A C     1 
ATOM   1118 O  O     . GLN A 1 164 ? 7.233   17.938  32.877  1.00 64.74  ? 136 GLN A O     1 
ATOM   1119 C  CB    . GLN A 1 164 ? 8.308   16.391  30.648  1.00 60.03  ? 136 GLN A CB    1 
ATOM   1120 C  CG    . GLN A 1 164 ? 9.005   15.391  29.739  1.00 66.78  ? 136 GLN A CG    1 
ATOM   1121 C  CD    . GLN A 1 164 ? 9.042   15.783  28.265  1.00 78.38  ? 136 GLN A CD    1 
ATOM   1122 O  OE1   . GLN A 1 164 ? 8.004   16.017  27.640  1.00 73.22  ? 136 GLN A OE1   1 
ATOM   1123 N  NE2   . GLN A 1 164 ? 10.244  15.808  27.693  1.00 76.59  ? 136 GLN A NE2   1 
ATOM   1124 N  N     . GLY A 1 165 ? 6.518   15.977  33.697  1.00 53.06  ? 137 GLY A N     1 
ATOM   1125 C  CA    . GLY A 1 165 ? 5.497   16.600  34.512  1.00 55.34  ? 137 GLY A CA    1 
ATOM   1126 C  C     . GLY A 1 165 ? 4.154   16.777  33.846  1.00 55.33  ? 137 GLY A C     1 
ATOM   1127 O  O     . GLY A 1 165 ? 3.328   17.545  34.351  1.00 58.51  ? 137 GLY A O     1 
ATOM   1128 N  N     . THR A 1 166 ? 3.903   16.085  32.739  1.00 55.38  ? 138 THR A N     1 
ATOM   1129 C  CA    . THR A 1 166 ? 2.701   16.272  31.937  1.00 55.36  ? 138 THR A CA    1 
ATOM   1130 C  C     . THR A 1 166 ? 1.905   14.975  31.882  1.00 53.40  ? 138 THR A C     1 
ATOM   1131 O  O     . THR A 1 166 ? 2.472   13.894  31.703  1.00 51.20  ? 138 THR A O     1 
ATOM   1132 C  CB    . THR A 1 166 ? 3.064   16.727  30.509  1.00 57.97  ? 138 THR A CB    1 
ATOM   1133 O  OG1   . THR A 1 166 ? 3.597   18.056  30.553  1.00 70.23  ? 138 THR A OG1   1 
ATOM   1134 C  CG2   . THR A 1 166 ? 1.844   16.709  29.597  1.00 60.58  ? 138 THR A CG2   1 
ATOM   1135 N  N     . ASN A 1 167 ? 0.589   15.086  32.028  1.00 61.39  ? 139 ASN A N     1 
ATOM   1136 C  CA    . ASN A 1 167 ? -0.277  13.930  31.858  1.00 56.42  ? 139 ASN A CA    1 
ATOM   1137 C  C     . ASN A 1 167 ? -0.535  13.759  30.364  1.00 52.18  ? 139 ASN A C     1 
ATOM   1138 O  O     . ASN A 1 167 ? -1.049  14.687  29.729  1.00 57.76  ? 139 ASN A O     1 
ATOM   1139 C  CB    . ASN A 1 167 ? -1.584  14.131  32.621  1.00 53.62  ? 139 ASN A CB    1 
ATOM   1140 C  CG    . ASN A 1 167 ? -2.580  12.989  32.424  1.00 63.85  ? 139 ASN A CG    1 
ATOM   1141 O  OD1   . ASN A 1 167 ? -2.576  12.283  31.416  1.00 60.50  ? 139 ASN A OD1   1 
ATOM   1142 N  ND2   . ASN A 1 167 ? -3.451  12.808  33.413  1.00 69.84  ? 139 ASN A ND2   1 
ATOM   1143 N  N     . PRO A 1 168 ? -0.196  12.612  29.768  1.00 52.24  ? 140 PRO A N     1 
ATOM   1144 C  CA    . PRO A 1 168 ? -0.327  12.472  28.303  1.00 59.78  ? 140 PRO A CA    1 
ATOM   1145 C  C     . PRO A 1 168 ? -1.739  12.660  27.777  1.00 57.28  ? 140 PRO A C     1 
ATOM   1146 O  O     . PRO A 1 168 ? -1.891  12.993  26.598  1.00 58.88  ? 140 PRO A O     1 
ATOM   1147 C  CB    . PRO A 1 168 ? 0.172   11.047  28.026  1.00 61.52  ? 140 PRO A CB    1 
ATOM   1148 C  CG    . PRO A 1 168 ? 0.336   10.387  29.341  1.00 63.73  ? 140 PRO A CG    1 
ATOM   1149 C  CD    . PRO A 1 168 ? 0.381   11.421  30.409  1.00 55.28  ? 140 PRO A CD    1 
ATOM   1150 N  N     . LEU A 1 169 ? -2.777  12.444  28.590  1.00 48.92  ? 141 LEU A N     1 
ATOM   1151 C  CA    . LEU A 1 169 ? -4.139  12.697  28.128  1.00 55.50  ? 141 LEU A CA    1 
ATOM   1152 C  C     . LEU A 1 169 ? -4.507  14.174  28.080  1.00 63.74  ? 141 LEU A C     1 
ATOM   1153 O  O     . LEU A 1 169 ? -5.596  14.502  27.597  1.00 65.28  ? 141 LEU A O     1 
ATOM   1154 C  CB    . LEU A 1 169 ? -5.157  11.966  29.007  1.00 60.01  ? 141 LEU A CB    1 
ATOM   1155 C  CG    . LEU A 1 169 ? -4.768  10.579  29.500  1.00 57.33  ? 141 LEU A CG    1 
ATOM   1156 C  CD1   . LEU A 1 169 ? -5.755  10.093  30.544  1.00 63.09  ? 141 LEU A CD1   1 
ATOM   1157 C  CD2   . LEU A 1 169 ? -4.743  9.637   28.311  1.00 60.69  ? 141 LEU A CD2   1 
ATOM   1158 N  N     . ASN A 1 170 ? -3.646  15.070  28.559  1.00 63.15  ? 142 ASN A N     1 
ATOM   1159 C  CA    . ASN A 1 170 ? -3.964  16.492  28.627  1.00 64.40  ? 142 ASN A CA    1 
ATOM   1160 C  C     . ASN A 1 170 ? -3.158  17.324  27.636  1.00 62.03  ? 142 ASN A C     1 
ATOM   1161 O  O     . ASN A 1 170 ? -3.258  18.555  27.647  1.00 64.89  ? 142 ASN A O     1 
ATOM   1162 C  CB    . ASN A 1 170 ? -3.739  17.013  30.051  1.00 69.05  ? 142 ASN A CB    1 
ATOM   1163 C  CG    . ASN A 1 170 ? -4.795  16.521  31.031  1.00 73.86  ? 142 ASN A CG    1 
ATOM   1164 O  OD1   . ASN A 1 170 ? -5.795  15.913  30.639  1.00 78.89  ? 142 ASN A OD1   1 
ATOM   1165 N  ND2   . ASN A 1 170 ? -4.557  16.754  32.317  1.00 75.97  ? 142 ASN A ND2   1 
ATOM   1166 N  N     . ILE A 1 171 ? -2.357  16.683  26.786  1.00 59.70  ? 143 ILE A N     1 
ATOM   1167 C  CA    A ILE A 1 171 ? -1.550  17.403  25.809  0.45 58.78  ? 143 ILE A CA    1 
ATOM   1168 C  CA    B ILE A 1 171 ? -1.554  17.421  25.822  0.55 58.77  ? 143 ILE A CA    1 
ATOM   1169 C  C     . ILE A 1 171 ? -2.456  18.062  24.775  1.00 59.25  ? 143 ILE A C     1 
ATOM   1170 O  O     . ILE A 1 171 ? -3.452  17.475  24.330  1.00 61.05  ? 143 ILE A O     1 
ATOM   1171 C  CB    A ILE A 1 171 ? -0.548  16.440  25.147  0.45 59.08  ? 143 ILE A CB    1 
ATOM   1172 C  CB    B ILE A 1 171 ? -0.509  16.501  25.167  0.55 59.08  ? 143 ILE A CB    1 
ATOM   1173 C  CG1   A ILE A 1 171 ? 0.489   15.957  26.162  0.45 60.29  ? 143 ILE A CG1   1 
ATOM   1174 C  CG1   B ILE A 1 171 ? -1.202  15.449  24.295  0.55 53.08  ? 143 ILE A CG1   1 
ATOM   1175 C  CG2   A ILE A 1 171 ? 0.154   17.091  23.969  0.45 59.09  ? 143 ILE A CG2   1 
ATOM   1176 C  CG2   B ILE A 1 171 ? 0.391   15.874  26.227  0.55 60.34  ? 143 ILE A CG2   1 
ATOM   1177 C  CD1   A ILE A 1 171 ? 1.311   14.784  25.671  0.45 58.01  ? 143 ILE A CD1   1 
ATOM   1178 C  CD1   B ILE A 1 171 ? -0.402  14.204  24.074  0.55 57.55  ? 143 ILE A CD1   1 
ATOM   1179 N  N     . ARG A 1 172 ? -2.122  19.289  24.399  1.00 58.23  ? 144 ARG A N     1 
ATOM   1180 C  CA    . ARG A 1 172 ? -2.776  19.982  23.302  1.00 57.69  ? 144 ARG A CA    1 
ATOM   1181 C  C     . ARG A 1 172 ? -2.140  19.538  21.984  1.00 50.79  ? 144 ARG A C     1 
ATOM   1182 O  O     . ARG A 1 172 ? -0.939  19.258  21.936  1.00 51.04  ? 144 ARG A O     1 
ATOM   1183 C  CB    . ARG A 1 172 ? -2.636  21.496  23.462  1.00 65.94  ? 144 ARG A CB    1 
ATOM   1184 C  CG    . ARG A 1 172 ? -1.194  22.025  23.345  1.00 75.01  ? 144 ARG A CG    1 
ATOM   1185 C  CD    . ARG A 1 172 ? -0.319  21.709  24.565  1.00 83.41  ? 144 ARG A CD    1 
ATOM   1186 N  NE    . ARG A 1 172 ? 1.009   22.302  24.459  1.00 92.45  ? 144 ARG A NE    1 
ATOM   1187 C  CZ    . ARG A 1 172 ? 1.779   22.614  25.492  1.00 101.46 ? 144 ARG A CZ    1 
ATOM   1188 N  NH1   . ARG A 1 172 ? 1.386   22.398  26.737  1.00 107.13 ? 144 ARG A NH1   1 
ATOM   1189 N  NH2   . ARG A 1 172 ? 2.976   23.151  25.271  1.00 99.84  ? 144 ARG A NH2   1 
ATOM   1190 N  N     . PRO A 1 173 ? -2.916  19.450  20.908  1.00 46.88  ? 145 PRO A N     1 
ATOM   1191 C  CA    . PRO A 1 173 ? -2.378  18.882  19.662  1.00 43.89  ? 145 PRO A CA    1 
ATOM   1192 C  C     . PRO A 1 173 ? -1.386  19.808  18.967  1.00 43.31  ? 145 PRO A C     1 
ATOM   1193 O  O     . PRO A 1 173 ? -1.489  21.032  19.031  1.00 45.18  ? 145 PRO A O     1 
ATOM   1194 C  CB    . PRO A 1 173 ? -3.631  18.664  18.803  1.00 46.92  ? 145 PRO A CB    1 
ATOM   1195 C  CG    . PRO A 1 173 ? -4.617  19.652  19.325  1.00 51.01  ? 145 PRO A CG    1 
ATOM   1196 C  CD    . PRO A 1 173 ? -4.352  19.771  20.799  1.00 43.06  ? 145 PRO A CD    1 
ATOM   1197 N  N     . LYS A 1 174 ? -0.420  19.201  18.273  1.00 36.62  ? 146 LYS A N     1 
ATOM   1198 C  CA    . LYS A 1 174 ? 0.624   19.941  17.576  1.00 37.62  ? 146 LYS A CA    1 
ATOM   1199 C  C     . LYS A 1 174 ? 0.991   19.194  16.294  1.00 40.49  ? 146 LYS A C     1 
ATOM   1200 O  O     . LYS A 1 174 ? 0.922   17.970  16.251  1.00 42.24  ? 146 LYS A O     1 
ATOM   1201 C  CB    . LYS A 1 174 ? 1.849   20.091  18.488  1.00 44.88  ? 146 LYS A CB    1 
ATOM   1202 C  CG    . LYS A 1 174 ? 2.926   21.013  17.994  1.00 54.64  ? 146 LYS A CG    1 
ATOM   1203 C  CD    . LYS A 1 174 ? 3.811   21.466  19.155  1.00 68.89  ? 146 LYS A CD    1 
ATOM   1204 C  CE    . LYS A 1 174 ? 5.192   20.829  19.075  1.00 76.73  ? 146 LYS A CE    1 
ATOM   1205 N  NZ    . LYS A 1 174 ? 6.203   21.536  19.914  1.00 88.39  ? 146 LYS A NZ    1 
ATOM   1206 N  N     . ALA A 1 175 ? 1.346   19.930  15.242  1.00 39.13  ? 147 ALA A N     1 
ATOM   1207 C  CA    . ALA A 1 175 ? 1.862   19.320  14.017  1.00 39.48  ? 147 ALA A CA    1 
ATOM   1208 C  C     . ALA A 1 175 ? 3.368   19.535  13.949  1.00 43.44  ? 147 ALA A C     1 
ATOM   1209 O  O     . ALA A 1 175 ? 3.851   20.643  14.203  1.00 40.94  ? 147 ALA A O     1 
ATOM   1210 C  CB    . ALA A 1 175 ? 1.188   19.896  12.767  1.00 46.25  ? 147 ALA A CB    1 
ATOM   1211 N  N     . VAL A 1 176 ? 4.112   18.481  13.607  1.00 37.22  ? 148 VAL A N     1 
ATOM   1212 C  CA    . VAL A 1 176 ? 5.573   18.504  13.670  1.00 37.35  ? 148 VAL A CA    1 
ATOM   1213 C  C     . VAL A 1 176 ? 6.131   17.748  12.468  1.00 42.52  ? 148 VAL A C     1 
ATOM   1214 O  O     . VAL A 1 176 ? 5.612   16.693  12.104  1.00 40.49  ? 148 VAL A O     1 
ATOM   1215 C  CB    . VAL A 1 176 ? 6.081   17.857  14.982  1.00 41.65  ? 148 VAL A CB    1 
ATOM   1216 C  CG1   . VAL A 1 176 ? 7.593   17.751  14.983  1.00 51.72  ? 148 VAL A CG1   1 
ATOM   1217 C  CG2   . VAL A 1 176 ? 5.592   18.632  16.211  1.00 50.08  ? 148 VAL A CG2   1 
ATOM   1218 N  N     . GLU A 1 177 ? 7.201   18.269  11.871  1.00 40.09  ? 149 GLU A N     1 
ATOM   1219 C  CA    . GLU A 1 177 ? 7.883   17.587  10.772  1.00 44.93  ? 149 GLU A CA    1 
ATOM   1220 C  C     . GLU A 1 177 ? 8.796   16.490  11.311  1.00 42.92  ? 149 GLU A C     1 
ATOM   1221 O  O     . GLU A 1 177 ? 9.574   16.724  12.243  1.00 41.25  ? 149 GLU A O     1 
ATOM   1222 C  CB    . GLU A 1 177 ? 8.713   18.581  9.958   1.00 54.81  ? 149 GLU A CB    1 
ATOM   1223 C  CG    . GLU A 1 177 ? 8.040   19.000  8.693   1.00 61.88  ? 149 GLU A CG    1 
ATOM   1224 C  CD    . GLU A 1 177 ? 8.987   19.346  7.567   1.00 73.03  ? 149 GLU A CD    1 
ATOM   1225 O  OE1   . GLU A 1 177 ? 10.060  19.933  7.829   1.00 74.71  ? 149 GLU A OE1   1 
ATOM   1226 O  OE2   . GLU A 1 177 ? 8.641   19.022  6.408   1.00 71.18  ? 149 GLU A OE2   1 
ATOM   1227 N  N     . LYS A 1 178 ? 8.701   15.285  10.729  1.00 36.25  ? 150 LYS A N     1 
ATOM   1228 C  CA    . LYS A 1 178 ? 9.547   14.166  11.119  1.00 33.27  ? 150 LYS A CA    1 
ATOM   1229 C  C     . LYS A 1 178 ? 10.125  13.500  9.878   1.00 31.24  ? 150 LYS A C     1 
ATOM   1230 O  O     . LYS A 1 178 ? 9.538   13.564  8.800   1.00 36.37  ? 150 LYS A O     1 
ATOM   1231 C  CB    . LYS A 1 178 ? 8.778   13.096  11.918  1.00 34.60  ? 150 LYS A CB    1 
ATOM   1232 C  CG    . LYS A 1 178 ? 8.067   13.613  13.152  1.00 40.78  ? 150 LYS A CG    1 
ATOM   1233 C  CD    . LYS A 1 178 ? 8.911   13.416  14.398  1.00 43.70  ? 150 LYS A CD    1 
ATOM   1234 C  CE    . LYS A 1 178 ? 8.029   13.500  15.657  1.00 50.14  ? 150 LYS A CE    1 
ATOM   1235 N  NZ    . LYS A 1 178 ? 8.851   14.025  16.781  1.00 52.40  ? 150 LYS A NZ    1 
ATOM   1236 N  N     . ILE A 1 179 ? 11.264  12.822  10.064  1.00 28.01  ? 151 ILE A N     1 
ATOM   1237 C  CA    . ILE A 1 179 ? 11.730  11.822  9.112   1.00 29.46  ? 151 ILE A CA    1 
ATOM   1238 C  C     . ILE A 1 179 ? 11.084  10.508  9.525   1.00 32.53  ? 151 ILE A C     1 
ATOM   1239 O  O     . ILE A 1 179 ? 11.235  10.080  10.672  1.00 36.78  ? 151 ILE A O     1 
ATOM   1240 C  CB    . ILE A 1 179 ? 13.264  11.700  9.123   1.00 32.80  ? 151 ILE A CB    1 
ATOM   1241 C  CG1   . ILE A 1 179 ? 13.940  13.043  8.826   1.00 40.80  ? 151 ILE A CG1   1 
ATOM   1242 C  CG2   . ILE A 1 179 ? 13.734  10.645  8.125   1.00 34.18  ? 151 ILE A CG2   1 
ATOM   1243 C  CD1   . ILE A 1 179 ? 13.627  13.571  7.485   1.00 41.33  ? 151 ILE A CD1   1 
ATOM   1244 N  N     . VAL A 1 180 ? 10.364  9.863   8.609   1.00 28.19  ? 152 VAL A N     1 
ATOM   1245 C  CA    A VAL A 1 180 ? 9.641   8.628   8.900   0.68 28.03  ? 152 VAL A CA    1 
ATOM   1246 C  CA    B VAL A 1 180 ? 9.660   8.626   8.923   0.32 28.13  ? 152 VAL A CA    1 
ATOM   1247 C  C     . VAL A 1 180 ? 10.422  7.460   8.305   1.00 30.70  ? 152 VAL A C     1 
ATOM   1248 O  O     . VAL A 1 180 ? 10.858  7.530   7.153   1.00 31.16  ? 152 VAL A O     1 
ATOM   1249 C  CB    A VAL A 1 180 ? 8.210   8.675   8.337   0.68 31.86  ? 152 VAL A CB    1 
ATOM   1250 C  CB    B VAL A 1 180 ? 8.189   8.653   8.455   0.32 31.92  ? 152 VAL A CB    1 
ATOM   1251 C  CG1   A VAL A 1 180 ? 7.397   7.489   8.861   0.68 35.23  ? 152 VAL A CG1   1 
ATOM   1252 C  CG1   B VAL A 1 180 ? 8.076   8.800   6.947   0.32 30.11  ? 152 VAL A CG1   1 
ATOM   1253 C  CG2   A VAL A 1 180 ? 7.523   9.998   8.693   0.68 33.00  ? 152 VAL A CG2   1 
ATOM   1254 C  CG2   B VAL A 1 180 ? 7.454   7.401   8.935   0.32 35.02  ? 152 VAL A CG2   1 
ATOM   1255 N  N     . PHE A 1 181 ? 10.587  6.393   9.092   1.00 30.65  ? 153 PHE A N     1 
ATOM   1256 C  CA    . PHE A 1 181 ? 11.352  5.190   8.750   1.00 28.03  ? 153 PHE A CA    1 
ATOM   1257 C  C     . PHE A 1 181 ? 10.381  4.015   8.625   1.00 27.48  ? 153 PHE A C     1 
ATOM   1258 O  O     . PHE A 1 181 ? 9.575   3.781   9.532   1.00 28.33  ? 153 PHE A O     1 
ATOM   1259 C  CB    . PHE A 1 181 ? 12.400  4.954   9.860   1.00 29.25  ? 153 PHE A CB    1 
ATOM   1260 C  CG    . PHE A 1 181 ? 13.139  3.616   9.816   1.00 29.83  ? 153 PHE A CG    1 
ATOM   1261 C  CD1   . PHE A 1 181 ? 12.510  2.433   10.178  1.00 32.88  ? 153 PHE A CD1   1 
ATOM   1262 C  CD2   . PHE A 1 181 ? 14.505  3.583   9.508   1.00 32.59  ? 153 PHE A CD2   1 
ATOM   1263 C  CE1   . PHE A 1 181 ? 13.194  1.215   10.155  1.00 34.21  ? 153 PHE A CE1   1 
ATOM   1264 C  CE2   . PHE A 1 181 ? 15.211  2.363   9.495   1.00 33.18  ? 153 PHE A CE2   1 
ATOM   1265 C  CZ    . PHE A 1 181 ? 14.553  1.187   9.823   1.00 33.15  ? 153 PHE A CZ    1 
ATOM   1266 N  N     . PHE A 1 182 ? 10.477  3.250   7.526   1.00 26.84  ? 154 PHE A N     1 
ATOM   1267 C  CA    . PHE A 1 182 ? 9.715   2.011   7.349   1.00 28.66  ? 154 PHE A CA    1 
ATOM   1268 C  C     . PHE A 1 182 ? 10.671  0.906   6.898   1.00 31.86  ? 154 PHE A C     1 
ATOM   1269 O  O     . PHE A 1 182 ? 11.408  1.105   5.931   1.00 29.85  ? 154 PHE A O     1 
ATOM   1270 C  CB    . PHE A 1 182 ? 8.612   2.153   6.277   1.00 25.77  ? 154 PHE A CB    1 
ATOM   1271 C  CG    . PHE A 1 182 ? 7.475   3.089   6.643   1.00 28.85  ? 154 PHE A CG    1 
ATOM   1272 C  CD1   . PHE A 1 182 ? 6.471   2.669   7.495   1.00 33.35  ? 154 PHE A CD1   1 
ATOM   1273 C  CD2   . PHE A 1 182 ? 7.401   4.358   6.092   1.00 39.26  ? 154 PHE A CD2   1 
ATOM   1274 C  CE1   . PHE A 1 182 ? 5.400   3.516   7.804   1.00 34.69  ? 154 PHE A CE1   1 
ATOM   1275 C  CE2   . PHE A 1 182 ? 6.327   5.209   6.413   1.00 35.49  ? 154 PHE A CE2   1 
ATOM   1276 C  CZ    . PHE A 1 182 ? 5.352   4.780   7.245   1.00 33.40  ? 154 PHE A CZ    1 
ATOM   1277 N  N     . SER A 1 183 ? 10.668  -0.251  7.583   1.00 29.45  ? 155 SER A N     1 
ATOM   1278 C  CA    . SER A 1 183 ? 11.474  -1.407  7.166   1.00 31.07  ? 155 SER A CA    1 
ATOM   1279 C  C     . SER A 1 183 ? 10.596  -2.651  7.170   1.00 35.56  ? 155 SER A C     1 
ATOM   1280 O  O     . SER A 1 183 ? 9.661   -2.746  7.962   1.00 36.04  ? 155 SER A O     1 
ATOM   1281 C  CB    . SER A 1 183 ? 12.709  -1.628  8.074   1.00 32.94  ? 155 SER A CB    1 
ATOM   1282 O  OG    . SER A 1 183 ? 12.341  -2.049  9.393   1.00 36.47  ? 155 SER A OG    1 
ATOM   1283 N  N     . ASP A 1 184 ? 10.899  -3.613  6.290   1.00 27.99  ? 156 ASP A N     1 
ATOM   1284 C  CA    A ASP A 1 184 ? 10.032  -4.778  6.154   0.65 30.12  ? 156 ASP A CA    1 
ATOM   1285 C  CA    B ASP A 1 184 ? 10.017  -4.742  6.063   0.35 30.33  ? 156 ASP A CA    1 
ATOM   1286 C  C     . ASP A 1 184 ? 10.888  -5.997  5.868   1.00 32.52  ? 156 ASP A C     1 
ATOM   1287 O  O     . ASP A 1 184 ? 12.080  -5.894  5.559   1.00 33.87  ? 156 ASP A O     1 
ATOM   1288 C  CB    A ASP A 1 184 ? 8.999   -4.601  5.028   0.65 36.38  ? 156 ASP A CB    1 
ATOM   1289 C  CB    B ASP A 1 184 ? 9.143   -4.411  4.837   0.35 36.97  ? 156 ASP A CB    1 
ATOM   1290 C  CG    A ASP A 1 184 ? 9.605   -4.839  3.638   0.65 29.52  ? 156 ASP A CG    1 
ATOM   1291 C  CG    B ASP A 1 184 ? 8.123   -5.446  4.555   0.35 35.72  ? 156 ASP A CG    1 
ATOM   1292 O  OD1   A ASP A 1 184 ? 10.747  -4.404  3.385   0.65 36.18  ? 156 ASP A OD1   1 
ATOM   1293 O  OD1   B ASP A 1 184 ? 7.419   -5.744  5.525   0.35 42.86  ? 156 ASP A OD1   1 
ATOM   1294 O  OD2   A ASP A 1 184 ? 8.959   -5.472  2.801   0.65 37.51  ? 156 ASP A OD2   1 
ATOM   1295 O  OD2   B ASP A 1 184 ? 7.991   -5.941  3.421   0.35 35.41  ? 156 ASP A OD2   1 
ATOM   1296 N  N     . ILE A 1 185 ? 10.287  -7.178  6.020   1.00 28.44  ? 157 ILE A N     1 
ATOM   1297 C  CA    . ILE A 1 185 ? 10.985  -8.448  5.747   1.00 28.04  ? 157 ILE A CA    1 
ATOM   1298 C  C     . ILE A 1 185 ? 10.694  -8.927  4.324   1.00 34.94  ? 157 ILE A C     1 
ATOM   1299 O  O     . ILE A 1 185 ? 9.534   -9.119  3.950   1.00 35.61  ? 157 ILE A O     1 
ATOM   1300 C  CB    . ILE A 1 185 ? 10.565  -9.527  6.765   1.00 31.16  ? 157 ILE A CB    1 
ATOM   1301 C  CG1   . ILE A 1 185 ? 11.000  -9.153  8.178   1.00 30.79  ? 157 ILE A CG1   1 
ATOM   1302 C  CG2   . ILE A 1 185 ? 11.151  -10.888 6.368   1.00 35.40  ? 157 ILE A CG2   1 
ATOM   1303 C  CD1   . ILE A 1 185 ? 10.426  -10.111 9.253   1.00 34.93  ? 157 ILE A CD1   1 
ATOM   1304 N  N     . VAL A 1 186 ? 11.749  -9.191  3.550   1.00 30.59  ? 158 VAL A N     1 
ATOM   1305 C  CA    . VAL A 1 186 ? 11.579  -9.653  2.171   1.00 31.59  ? 158 VAL A CA    1 
ATOM   1306 C  C     . VAL A 1 186 ? 10.949  -11.041 2.146   1.00 33.08  ? 158 VAL A C     1 
ATOM   1307 O  O     . VAL A 1 186 ? 11.409  -11.966 2.834   1.00 35.39  ? 158 VAL A O     1 
ATOM   1308 C  CB    . VAL A 1 186 ? 12.927  -9.656  1.436   1.00 32.96  ? 158 VAL A CB    1 
ATOM   1309 C  CG1   . VAL A 1 186 ? 12.761  -10.247 0.020   1.00 41.22  ? 158 VAL A CG1   1 
ATOM   1310 C  CG2   . VAL A 1 186 ? 13.492  -8.244  1.377   1.00 37.40  ? 158 VAL A CG2   1 
ATOM   1311 N  N     . SER A 1 187 ? 9.889   -11.190 1.343   1.00 34.01  ? 159 SER A N     1 
ATOM   1312 C  CA    . SER A 1 187 ? 9.208   -12.473 1.140   1.00 40.87  ? 159 SER A CA    1 
ATOM   1313 C  C     . SER A 1 187 ? 8.752   -13.107 2.452   1.00 39.21  ? 159 SER A C     1 
ATOM   1314 O  O     . SER A 1 187 ? 8.877   -14.319 2.663   1.00 35.46  ? 159 SER A O     1 
ATOM   1315 C  CB    . SER A 1 187 ? 10.106  -13.439 0.360   1.00 43.16  ? 159 SER A CB    1 
ATOM   1316 O  OG    . SER A 1 187 ? 9.312   -14.328 -0.411  1.00 55.04  ? 159 SER A OG    1 
ATOM   1317 N  N     . PHE A 1 188 ? 8.186   -12.287 3.342   1.00 33.88  ? 160 PHE A N     1 
ATOM   1318 C  CA    . PHE A 1 188 ? 7.727   -12.818 4.619   1.00 32.22  ? 160 PHE A CA    1 
ATOM   1319 C  C     . PHE A 1 188 ? 6.725   -13.964 4.453   1.00 34.75  ? 160 PHE A C     1 
ATOM   1320 O  O     . PHE A 1 188 ? 6.699   -14.882 5.281   1.00 37.11  ? 160 PHE A O     1 
ATOM   1321 C  CB    . PHE A 1 188 ? 7.085   -11.698 5.455   1.00 37.36  ? 160 PHE A CB    1 
ATOM   1322 C  CG    . PHE A 1 188 ? 6.463   -12.184 6.722   1.00 40.47  ? 160 PHE A CG    1 
ATOM   1323 C  CD1   . PHE A 1 188 ? 7.246   -12.416 7.841   1.00 44.86  ? 160 PHE A CD1   1 
ATOM   1324 C  CD2   . PHE A 1 188 ? 5.112   -12.453 6.788   1.00 40.93  ? 160 PHE A CD2   1 
ATOM   1325 C  CE1   . PHE A 1 188 ? 6.667   -12.873 9.013   1.00 48.09  ? 160 PHE A CE1   1 
ATOM   1326 C  CE2   . PHE A 1 188 ? 4.538   -12.929 7.958   1.00 45.49  ? 160 PHE A CE2   1 
ATOM   1327 C  CZ    . PHE A 1 188 ? 5.315   -13.129 9.062   1.00 45.28  ? 160 PHE A CZ    1 
ATOM   1328 N  N     . SER A 1 189 ? 5.867   -13.931 3.421   1.00 38.94  ? 161 SER A N     1 
ATOM   1329 C  CA    . SER A 1 189 ? 4.843   -14.974 3.337   1.00 45.42  ? 161 SER A CA    1 
ATOM   1330 C  C     . SER A 1 189 ? 5.457   -16.358 3.154   1.00 45.31  ? 161 SER A C     1 
ATOM   1331 O  O     . SER A 1 189 ? 4.863   -17.363 3.566   1.00 43.93  ? 161 SER A O     1 
ATOM   1332 C  CB    . SER A 1 189 ? 3.854   -14.689 2.205   1.00 47.03  ? 161 SER A CB    1 
ATOM   1333 O  OG    . SER A 1 189 ? 4.498   -14.073 1.109   1.00 50.92  ? 161 SER A OG    1 
ATOM   1334 N  N     . THR A 1 190 ? 6.643   -16.430 2.550   1.00 37.45  ? 162 THR A N     1 
ATOM   1335 C  CA    . THR A 1 190 ? 7.324   -17.714 2.383   1.00 38.15  ? 162 THR A CA    1 
ATOM   1336 C  C     . THR A 1 190 ? 7.700   -18.329 3.727   1.00 43.67  ? 162 THR A C     1 
ATOM   1337 O  O     . THR A 1 190 ? 7.591   -19.551 3.909   1.00 42.14  ? 162 THR A O     1 
ATOM   1338 C  CB    . THR A 1 190 ? 8.558   -17.530 1.502   1.00 48.65  ? 162 THR A CB    1 
ATOM   1339 O  OG1   . THR A 1 190 ? 8.173   -16.881 0.283   1.00 47.74  ? 162 THR A OG1   1 
ATOM   1340 C  CG2   . THR A 1 190 ? 9.193   -18.883 1.168   1.00 52.01  ? 162 THR A CG2   1 
ATOM   1341 N  N     . PHE A 1 191 ? 8.141   -17.505 4.688   1.00 37.47  ? 163 PHE A N     1 
ATOM   1342 C  CA    . PHE A 1 191 ? 8.434   -18.030 6.021   1.00 35.65  ? 163 PHE A CA    1 
ATOM   1343 C  C     . PHE A 1 191 ? 7.177   -18.620 6.653   1.00 43.88  ? 163 PHE A C     1 
ATOM   1344 O  O     . PHE A 1 191 ? 7.218   -19.702 7.256   1.00 41.48  ? 163 PHE A O     1 
ATOM   1345 C  CB    . PHE A 1 191 ? 8.983   -16.929 6.943   1.00 35.07  ? 163 PHE A CB    1 
ATOM   1346 C  CG    . PHE A 1 191 ? 10.383  -16.467 6.611   1.00 36.79  ? 163 PHE A CG    1 
ATOM   1347 C  CD1   . PHE A 1 191 ? 10.576  -15.498 5.641   1.00 36.37  ? 163 PHE A CD1   1 
ATOM   1348 C  CD2   . PHE A 1 191 ? 11.494  -16.964 7.298   1.00 34.12  ? 163 PHE A CD2   1 
ATOM   1349 C  CE1   . PHE A 1 191 ? 11.847  -15.046 5.326   1.00 39.83  ? 163 PHE A CE1   1 
ATOM   1350 C  CE2   . PHE A 1 191 ? 12.786  -16.507 7.006   1.00 37.34  ? 163 PHE A CE2   1 
ATOM   1351 C  CZ    . PHE A 1 191 ? 12.963  -15.554 6.012   1.00 36.53  ? 163 PHE A CZ    1 
ATOM   1352 N  N     . ALA A 1 192 ? 6.055   -17.898 6.549   1.00 37.59  ? 164 ALA A N     1 
ATOM   1353 C  CA    . ALA A 1 192 ? 4.817   -18.330 7.197   1.00 43.50  ? 164 ALA A CA    1 
ATOM   1354 C  C     . ALA A 1 192 ? 4.257   -19.593 6.556   1.00 42.75  ? 164 ALA A C     1 
ATOM   1355 O  O     . ALA A 1 192 ? 3.558   -20.367 7.219   1.00 50.09  ? 164 ALA A O     1 
ATOM   1356 C  CB    . ALA A 1 192 ? 3.780   -17.204 7.146   1.00 48.29  ? 164 ALA A CB    1 
ATOM   1357 N  N     . GLU A 1 193 ? 4.570   -19.824 5.281   1.00 47.19  ? 165 GLU A N     1 
ATOM   1358 C  CA    . GLU A 1 193 ? 4.031   -20.968 4.557   1.00 47.29  ? 165 GLU A CA    1 
ATOM   1359 C  C     . GLU A 1 193 ? 4.851   -22.236 4.766   1.00 48.38  ? 165 GLU A C     1 
ATOM   1360 O  O     . GLU A 1 193 ? 4.315   -23.342 4.643   1.00 54.82  ? 165 GLU A O     1 
ATOM   1361 C  CB    . GLU A 1 193 ? 3.957   -20.641 3.066   1.00 47.15  ? 165 GLU A CB    1 
ATOM   1362 C  CG    . GLU A 1 193 ? 2.773   -19.767 2.698   1.00 63.93  ? 165 GLU A CG    1 
ATOM   1363 C  CD    . GLU A 1 193 ? 2.833   -19.296 1.262   1.00 63.58  ? 165 GLU A CD    1 
ATOM   1364 O  OE1   . GLU A 1 193 ? 3.772   -19.704 0.545   1.00 66.52  ? 165 GLU A OE1   1 
ATOM   1365 O  OE2   . GLU A 1 193 ? 1.949   -18.510 0.855   1.00 74.65  ? 165 GLU A OE2   1 
ATOM   1366 N  N     . LYS A 1 194 ? 6.140   -22.107 5.080   1.00 43.39  ? 166 LYS A N     1 
ATOM   1367 C  CA    . LYS A 1 194 ? 7.044   -23.250 5.084   1.00 43.85  ? 166 LYS A CA    1 
ATOM   1368 C  C     . LYS A 1 194 ? 7.573   -23.654 6.457   1.00 45.27  ? 166 LYS A C     1 
ATOM   1369 O  O     . LYS A 1 194 ? 8.153   -24.740 6.571   1.00 51.13  ? 166 LYS A O     1 
ATOM   1370 C  CB    . LYS A 1 194 ? 8.231   -22.966 4.148   1.00 49.12  ? 166 LYS A CB    1 
ATOM   1371 C  CG    . LYS A 1 194 ? 7.812   -22.805 2.690   1.00 57.06  ? 166 LYS A CG    1 
ATOM   1372 C  CD    . LYS A 1 194 ? 8.832   -23.390 1.745   1.00 64.90  ? 166 LYS A CD    1 
ATOM   1373 C  CE    . LYS A 1 194 ? 8.636   -22.870 0.329   1.00 63.66  ? 166 LYS A CE    1 
ATOM   1374 N  NZ    . LYS A 1 194 ? 7.457   -23.485 -0.338  1.00 65.62  ? 166 LYS A NZ    1 
ATOM   1375 N  N     . LEU A 1 195 ? 7.424   -22.829 7.492   1.00 40.91  ? 167 LEU A N     1 
ATOM   1376 C  CA    . LEU A 1 195 ? 7.966   -23.137 8.809   1.00 36.77  ? 167 LEU A CA    1 
ATOM   1377 C  C     . LEU A 1 195 ? 6.852   -23.302 9.835   1.00 39.30  ? 167 LEU A C     1 
ATOM   1378 O  O     . LEU A 1 195 ? 5.772   -22.728 9.679   1.00 38.61  ? 167 LEU A O     1 
ATOM   1379 C  CB    . LEU A 1 195 ? 8.907   -22.023 9.289   1.00 41.63  ? 167 LEU A CB    1 
ATOM   1380 C  CG    . LEU A 1 195 ? 10.193  -21.745 8.516   1.00 50.83  ? 167 LEU A CG    1 
ATOM   1381 C  CD1   . LEU A 1 195 ? 10.845  -20.498 9.073   1.00 43.98  ? 167 LEU A CD1   1 
ATOM   1382 C  CD2   . LEU A 1 195 ? 11.154  -22.928 8.604   1.00 49.97  ? 167 LEU A CD2   1 
ATOM   1383 N  N     . PRO A 1 196 ? 7.096   -24.043 10.920  1.00 41.17  ? 168 PRO A N     1 
ATOM   1384 C  CA    . PRO A 1 196 ? 6.152   -24.042 12.050  1.00 42.57  ? 168 PRO A CA    1 
ATOM   1385 C  C     . PRO A 1 196 ? 6.043   -22.655 12.670  1.00 47.38  ? 168 PRO A C     1 
ATOM   1386 O  O     . PRO A 1 196 ? 6.974   -21.846 12.611  1.00 40.13  ? 168 PRO A O     1 
ATOM   1387 C  CB    . PRO A 1 196 ? 6.780   -25.033 13.047  1.00 45.58  ? 168 PRO A CB    1 
ATOM   1388 C  CG    . PRO A 1 196 ? 7.747   -25.844 12.236  1.00 49.45  ? 168 PRO A CG    1 
ATOM   1389 C  CD    . PRO A 1 196 ? 8.249   -24.928 11.167  1.00 47.13  ? 168 PRO A CD    1 
ATOM   1390 N  N     . VAL A 1 197 ? 4.910   -22.408 13.337  1.00 45.08  ? 169 VAL A N     1 
ATOM   1391 C  CA    A VAL A 1 197 ? 4.622   -21.058 13.815  0.51 44.35  ? 169 VAL A CA    1 
ATOM   1392 C  CA    B VAL A 1 197 ? 4.614   -21.064 13.829  0.49 44.35  ? 169 VAL A CA    1 
ATOM   1393 C  C     . VAL A 1 197 ? 5.660   -20.608 14.842  1.00 42.06  ? 169 VAL A C     1 
ATOM   1394 O  O     . VAL A 1 197 ? 6.073   -19.441 14.853  1.00 38.77  ? 169 VAL A O     1 
ATOM   1395 C  CB    A VAL A 1 197 ? 3.181   -20.975 14.362  0.51 46.82  ? 169 VAL A CB    1 
ATOM   1396 C  CB    B VAL A 1 197 ? 3.189   -21.013 14.415  0.49 46.85  ? 169 VAL A CB    1 
ATOM   1397 C  CG1   A VAL A 1 197 ? 2.981   -21.907 15.558  0.51 49.06  ? 169 VAL A CG1   1 
ATOM   1398 C  CG1   B VAL A 1 197 ? 2.172   -21.248 13.328  0.49 43.62  ? 169 VAL A CG1   1 
ATOM   1399 C  CG2   A VAL A 1 197 ? 2.813   -19.533 14.715  0.51 41.93  ? 169 VAL A CG2   1 
ATOM   1400 C  CG2   B VAL A 1 197 ? 3.015   -22.032 15.541  0.49 49.08  ? 169 VAL A CG2   1 
ATOM   1401 N  N     . GLU A 1 198 ? 6.124   -21.517 15.704  1.00 41.42  ? 170 GLU A N     1 
ATOM   1402 C  CA    . GLU A 1 198 ? 7.108   -21.108 16.709  1.00 43.81  ? 170 GLU A CA    1 
ATOM   1403 C  C     . GLU A 1 198 ? 8.416   -20.638 16.069  1.00 41.60  ? 170 GLU A C     1 
ATOM   1404 O  O     . GLU A 1 198 ? 9.087   -19.742 16.603  1.00 43.42  ? 170 GLU A O     1 
ATOM   1405 C  CB    . GLU A 1 198 ? 7.353   -22.251 17.701  1.00 48.75  ? 170 GLU A CB    1 
ATOM   1406 C  CG    . GLU A 1 198 ? 7.958   -23.491 17.083  0.51 48.37  ? 170 GLU A CG    1 
ATOM   1407 C  CD    . GLU A 1 198 ? 6.915   -24.523 16.694  0.30 51.71  ? 170 GLU A CD    1 
ATOM   1408 O  OE1   . GLU A 1 198 ? 5.705   -24.187 16.669  0.98 51.92  ? 170 GLU A OE1   1 
ATOM   1409 O  OE2   . GLU A 1 198 ? 7.313   -25.674 16.409  0.50 55.02  ? 170 GLU A OE2   1 
ATOM   1410 N  N     A GLU A 1 199 ? 8.795   -21.239 14.937  0.58 41.57  ? 171 GLU A N     1 
ATOM   1411 N  N     B GLU A 1 199 ? 8.780   -21.202 14.917  0.42 41.64  ? 171 GLU A N     1 
ATOM   1412 C  CA    A GLU A 1 199 ? 9.973   -20.799 14.199  0.58 42.33  ? 171 GLU A CA    1 
ATOM   1413 C  CA    B GLU A 1 199 ? 9.988   -20.770 14.227  0.42 42.35  ? 171 GLU A CA    1 
ATOM   1414 C  C     A GLU A 1 199 ? 9.748   -19.443 13.540  0.58 40.97  ? 171 GLU A C     1 
ATOM   1415 C  C     B GLU A 1 199 ? 9.778   -19.480 13.441  0.42 40.98  ? 171 GLU A C     1 
ATOM   1416 O  O     A GLU A 1 199 ? 10.669  -18.617 13.488  0.58 39.40  ? 171 GLU A O     1 
ATOM   1417 O  O     B GLU A 1 199 ? 10.739  -18.730 13.229  0.42 39.06  ? 171 GLU A O     1 
ATOM   1418 C  CB    A GLU A 1 199 ? 10.339  -21.838 13.141  0.58 48.05  ? 171 GLU A CB    1 
ATOM   1419 C  CB    B GLU A 1 199 ? 10.484  -21.885 13.307  0.42 48.00  ? 171 GLU A CB    1 
ATOM   1420 C  CG    A GLU A 1 199 ? 10.194  -23.284 13.587  0.58 52.50  ? 171 GLU A CG    1 
ATOM   1421 C  CG    B GLU A 1 199 ? 10.987  -23.092 14.074  0.42 47.04  ? 171 GLU A CG    1 
ATOM   1422 C  CD    A GLU A 1 199 ? 11.510  -24.024 13.609  0.58 56.80  ? 171 GLU A CD    1 
ATOM   1423 C  CD    B GLU A 1 199 ? 12.146  -22.733 14.977  0.42 54.98  ? 171 GLU A CD    1 
ATOM   1424 O  OE1   A GLU A 1 199 ? 12.454  -23.567 14.287  0.58 61.68  ? 171 GLU A OE1   1 
ATOM   1425 O  OE1   B GLU A 1 199 ? 13.047  -22.005 14.511  0.42 51.16  ? 171 GLU A OE1   1 
ATOM   1426 O  OE2   A GLU A 1 199 ? 11.613  -25.050 12.902  0.58 59.16  ? 171 GLU A OE2   1 
ATOM   1427 O  OE2   B GLU A 1 199 ? 12.149  -23.157 16.152  0.42 56.42  ? 171 GLU A OE2   1 
ATOM   1428 N  N     . VAL A 1 200 ? 8.549   -19.212 12.992  1.00 33.49  ? 172 VAL A N     1 
ATOM   1429 C  CA    . VAL A 1 200 ? 8.253   -17.912 12.378  1.00 38.03  ? 172 VAL A CA    1 
ATOM   1430 C  C     . VAL A 1 200 ? 8.388   -16.801 13.415  1.00 37.74  ? 172 VAL A C     1 
ATOM   1431 O  O     . VAL A 1 200 ? 8.971   -15.747 13.143  1.00 35.42  ? 172 VAL A O     1 
ATOM   1432 C  CB    . VAL A 1 200 ? 6.849   -17.910 11.727  1.00 43.62  ? 172 VAL A CB    1 
ATOM   1433 C  CG1   . VAL A 1 200 ? 6.484   -16.500 11.203  1.00 38.70  ? 172 VAL A CG1   1 
ATOM   1434 C  CG2   . VAL A 1 200 ? 6.776   -18.916 10.579  1.00 42.51  ? 172 VAL A CG2   1 
ATOM   1435 N  N     . VAL A 1 201 ? 7.877   -17.033 14.628  1.00 35.76  ? 173 VAL A N     1 
ATOM   1436 C  CA    . VAL A 1 201 ? 7.965   -16.035 15.692  1.00 33.94  ? 173 VAL A CA    1 
ATOM   1437 C  C     . VAL A 1 201 ? 9.425   -15.785 16.081  1.00 35.50  ? 173 VAL A C     1 
ATOM   1438 O  O     . VAL A 1 201 ? 9.835   -14.643 16.330  1.00 36.55  ? 173 VAL A O     1 
ATOM   1439 C  CB    . VAL A 1 201 ? 7.108   -16.477 16.898  1.00 38.96  ? 173 VAL A CB    1 
ATOM   1440 C  CG1   . VAL A 1 201 ? 7.417   -15.644 18.138  1.00 42.42  ? 173 VAL A CG1   1 
ATOM   1441 C  CG2   . VAL A 1 201 ? 5.617   -16.402 16.558  1.00 39.33  ? 173 VAL A CG2   1 
ATOM   1442 N  N     . SER A 1 202 ? 10.239  -16.841 16.116  1.00 36.88  ? 174 SER A N     1 
ATOM   1443 C  CA    . SER A 1 202 ? 11.660  -16.671 16.409  1.00 37.91  ? 174 SER A CA    1 
ATOM   1444 C  C     . SER A 1 202 ? 12.333  -15.747 15.390  1.00 39.18  ? 174 SER A C     1 
ATOM   1445 O  O     . SER A 1 202 ? 13.098  -14.849 15.762  1.00 38.12  ? 174 SER A O     1 
ATOM   1446 C  CB    . SER A 1 202 ? 12.336  -18.048 16.445  1.00 39.00  ? 174 SER A CB    1 
ATOM   1447 O  OG    . SER A 1 202 ? 13.640  -17.958 16.959  1.00 50.99  ? 174 SER A OG    1 
ATOM   1448 N  N     . VAL A 1 203 ? 12.020  -15.923 14.103  1.00 34.42  ? 175 VAL A N     1 
ATOM   1449 C  CA    . VAL A 1 203 ? 12.611  -15.089 13.058  1.00 35.34  ? 175 VAL A CA    1 
ATOM   1450 C  C     . VAL A 1 203 ? 12.165  -13.636 13.215  1.00 36.25  ? 175 VAL A C     1 
ATOM   1451 O  O     . VAL A 1 203 ? 12.993  -12.712 13.190  1.00 33.90  ? 175 VAL A O     1 
ATOM   1452 C  CB    . VAL A 1 203 ? 12.245  -15.637 11.668  1.00 36.53  ? 175 VAL A CB    1 
ATOM   1453 C  CG1   . VAL A 1 203 ? 12.566  -14.618 10.578  1.00 38.36  ? 175 VAL A CG1   1 
ATOM   1454 C  CG2   . VAL A 1 203 ? 12.973  -16.957 11.408  1.00 38.76  ? 175 VAL A CG2   1 
ATOM   1455 N  N     . VAL A 1 204 ? 10.851  -13.409 13.370  1.00 31.52  ? 176 VAL A N     1 
ATOM   1456 C  CA    . VAL A 1 204 ? 10.355  -12.029 13.432  1.00 32.89  ? 176 VAL A CA    1 
ATOM   1457 C  C     . VAL A 1 204 ? 10.892  -11.324 14.676  1.00 30.50  ? 176 VAL A C     1 
ATOM   1458 O  O     . VAL A 1 204 ? 11.254  -10.139 14.625  1.00 31.93  ? 176 VAL A O     1 
ATOM   1459 C  CB    . VAL A 1 204 ? 8.807   -11.955 13.354  1.00 38.05  ? 176 VAL A CB    1 
ATOM   1460 C  CG1   . VAL A 1 204 ? 8.258   -12.631 12.095  1.00 39.15  ? 176 VAL A CG1   1 
ATOM   1461 C  CG2   . VAL A 1 204 ? 8.137   -12.539 14.582  1.00 47.05  ? 176 VAL A CG2   1 
ATOM   1462 N  N     . ASN A 1 205 ? 11.001  -12.040 15.798  1.00 31.89  ? 177 ASN A N     1 
ATOM   1463 C  CA    . ASN A 1 205 ? 11.534  -11.416 17.011  1.00 32.86  ? 177 ASN A CA    1 
ATOM   1464 C  C     . ASN A 1 205 ? 13.017  -11.047 16.861  1.00 31.60  ? 177 ASN A C     1 
ATOM   1465 O  O     . ASN A 1 205 ? 13.458  -10.017 17.387  1.00 34.11  ? 177 ASN A O     1 
ATOM   1466 C  CB    . ASN A 1 205 ? 11.312  -12.342 18.218  1.00 36.06  ? 177 ASN A CB    1 
ATOM   1467 C  CG    . ASN A 1 205 ? 9.852   -12.314 18.725  1.00 36.71  ? 177 ASN A CG    1 
ATOM   1468 O  OD1   . ASN A 1 205 ? 8.999   -11.615 18.176  1.00 37.14  ? 177 ASN A OD1   1 
ATOM   1469 N  ND2   . ASN A 1 205 ? 9.581   -13.057 19.794  1.00 40.46  ? 177 ASN A ND2   1 
ATOM   1470 N  N     . SER A 1 206 ? 13.812  -11.885 16.183  1.00 32.54  ? 178 SER A N     1 
ATOM   1471 C  CA    . SER A 1 206 ? 15.212  -11.532 15.921  1.00 32.50  ? 178 SER A CA    1 
ATOM   1472 C  C     . SER A 1 206 ? 15.305  -10.256 15.095  1.00 33.07  ? 178 SER A C     1 
ATOM   1473 O  O     . SER A 1 206 ? 16.117  -9.370  15.389  1.00 32.77  ? 178 SER A O     1 
ATOM   1474 C  CB    . SER A 1 206 ? 15.931  -12.675 15.184  1.00 36.34  ? 178 SER A CB    1 
ATOM   1475 O  OG    . SER A 1 206 ? 16.020  -13.854 15.992  1.00 38.34  ? 178 SER A OG    1 
ATOM   1476 N  N     . TYR A 1 207 ? 14.456  -10.149 14.069  1.00 30.11  ? 179 TYR A N     1 
ATOM   1477 C  CA    . TYR A 1 207 ? 14.402  -8.960  13.220  1.00 28.47  ? 179 TYR A CA    1 
ATOM   1478 C  C     . TYR A 1 207 ? 13.984  -7.725  14.011  1.00 30.23  ? 179 TYR A C     1 
ATOM   1479 O  O     . TYR A 1 207 ? 14.636  -6.676  13.945  1.00 28.35  ? 179 TYR A O     1 
ATOM   1480 C  CB    . TYR A 1 207 ? 13.430  -9.208  12.079  1.00 29.77  ? 179 TYR A CB    1 
ATOM   1481 C  CG    . TYR A 1 207 ? 13.228  -8.013  11.165  1.00 30.94  ? 179 TYR A CG    1 
ATOM   1482 C  CD1   . TYR A 1 207 ? 14.273  -7.550  10.384  1.00 36.92  ? 179 TYR A CD1   1 
ATOM   1483 C  CD2   . TYR A 1 207 ? 12.002  -7.356  11.091  1.00 39.69  ? 179 TYR A CD2   1 
ATOM   1484 C  CE1   . TYR A 1 207 ? 14.121  -6.472  9.545   1.00 40.50  ? 179 TYR A CE1   1 
ATOM   1485 C  CE2   . TYR A 1 207 ? 11.844  -6.246  10.234  1.00 39.63  ? 179 TYR A CE2   1 
ATOM   1486 C  CZ    . TYR A 1 207 ? 12.913  -5.832  9.472   1.00 33.76  ? 179 TYR A CZ    1 
ATOM   1487 O  OH    . TYR A 1 207 ? 12.838  -4.750  8.597   1.00 43.76  ? 179 TYR A OH    1 
ATOM   1488 N  N     . PHE A 1 208 ? 12.879  -7.824  14.752  1.00 28.65  ? 180 PHE A N     1 
ATOM   1489 C  CA    . PHE A 1 208 ? 12.411  -6.667  15.505  1.00 33.09  ? 180 PHE A CA    1 
ATOM   1490 C  C     . PHE A 1 208 ? 13.436  -6.228  16.555  1.00 35.24  ? 180 PHE A C     1 
ATOM   1491 O  O     . PHE A 1 208 ? 13.571  -5.027  16.830  1.00 32.35  ? 180 PHE A O     1 
ATOM   1492 C  CB    . PHE A 1 208 ? 11.060  -6.994  16.171  1.00 31.81  ? 180 PHE A CB    1 
ATOM   1493 C  CG    . PHE A 1 208 ? 9.861   -6.959  15.226  1.00 32.27  ? 180 PHE A CG    1 
ATOM   1494 C  CD1   . PHE A 1 208 ? 9.885   -6.246  14.034  1.00 36.73  ? 180 PHE A CD1   1 
ATOM   1495 C  CD2   . PHE A 1 208 ? 8.708   -7.638  15.553  1.00 33.81  ? 180 PHE A CD2   1 
ATOM   1496 C  CE1   . PHE A 1 208 ? 8.769   -6.226  13.195  1.00 37.18  ? 180 PHE A CE1   1 
ATOM   1497 C  CE2   . PHE A 1 208 ? 7.591   -7.604  14.724  1.00 35.44  ? 180 PHE A CE2   1 
ATOM   1498 C  CZ    . PHE A 1 208 ? 7.624   -6.907  13.553  1.00 32.95  ? 180 PHE A CZ    1 
ATOM   1499 N  N     . SER A 1 209 ? 14.169  -7.179  17.160  1.00 30.44  ? 181 SER A N     1 
ATOM   1500 C  CA    . SER A 1 209 ? 15.148  -6.797  18.181  1.00 31.71  ? 181 SER A CA    1 
ATOM   1501 C  C     . SER A 1 209 ? 16.303  -6.005  17.579  1.00 35.29  ? 181 SER A C     1 
ATOM   1502 O  O     . SER A 1 209 ? 16.752  -5.018  18.173  1.00 35.37  ? 181 SER A O     1 
ATOM   1503 C  CB    . SER A 1 209 ? 15.699  -8.028  18.914  1.00 38.78  ? 181 SER A CB    1 
ATOM   1504 O  OG    . SER A 1 209 ? 14.666  -8.742  19.562  1.00 46.79  ? 181 SER A OG    1 
ATOM   1505 N  N     . VAL A 1 210 ? 16.805  -6.445  16.417  1.00 29.91  ? 182 VAL A N     1 
ATOM   1506 C  CA    . VAL A 1 210 ? 17.876  -5.723  15.720  1.00 28.48  ? 182 VAL A CA    1 
ATOM   1507 C  C     . VAL A 1 210 ? 17.432  -4.301  15.379  1.00 33.72  ? 182 VAL A C     1 
ATOM   1508 O  O     . VAL A 1 210 ? 18.139  -3.326  15.659  1.00 31.98  ? 182 VAL A O     1 
ATOM   1509 C  CB    . VAL A 1 210 ? 18.307  -6.489  14.456  1.00 30.16  ? 182 VAL A CB    1 
ATOM   1510 C  CG1   . VAL A 1 210 ? 19.219  -5.615  13.569  1.00 34.56  ? 182 VAL A CG1   1 
ATOM   1511 C  CG2   . VAL A 1 210 ? 19.055  -7.764  14.845  1.00 37.69  ? 182 VAL A CG2   1 
ATOM   1512 N  N     . CYS A 1 211 ? 16.255  -4.165  14.766  1.00 28.92  ? 183 CYS A N     1 
ATOM   1513 C  CA    . CYS A 1 211 ? 15.811  -2.852  14.313  1.00 31.69  ? 183 CYS A CA    1 
ATOM   1514 C  C     . CYS A 1 211 ? 15.610  -1.904  15.491  1.00 29.41  ? 183 CYS A C     1 
ATOM   1515 O  O     . CYS A 1 211 ? 16.034  -0.747  15.439  1.00 34.42  ? 183 CYS A O     1 
ATOM   1516 C  CB    . CYS A 1 211 ? 14.505  -2.967  13.502  1.00 31.70  ? 183 CYS A CB    1 
ATOM   1517 S  SG    . CYS A 1 211 ? 14.712  -3.774  11.888  1.00 35.22  ? 183 CYS A SG    1 
ATOM   1518 N  N     . THR A 1 212 ? 14.944  -2.370  16.549  1.00 31.79  ? 184 THR A N     1 
ATOM   1519 C  CA    . THR A 1 212 ? 14.608  -1.468  17.651  1.00 37.66  ? 184 THR A CA    1 
ATOM   1520 C  C     . THR A 1 212 ? 15.851  -1.028  18.412  1.00 33.94  ? 184 THR A C     1 
ATOM   1521 O  O     . THR A 1 212 ? 15.941  0.131   18.826  1.00 34.84  ? 184 THR A O     1 
ATOM   1522 C  CB    . THR A 1 212 ? 13.569  -2.094  18.606  1.00 38.74  ? 184 THR A CB    1 
ATOM   1523 O  OG1   . THR A 1 212 ? 12.406  -2.573  17.893  1.00 39.22  ? 184 THR A OG1   1 
ATOM   1524 C  CG2   . THR A 1 212 ? 13.144  -1.092  19.695  1.00 47.31  ? 184 THR A CG2   1 
ATOM   1525 N  N     . ALA A 1 213 ? 16.828  -1.925  18.579  1.00 32.99  ? 185 ALA A N     1 
ATOM   1526 C  CA    . ALA A 1 213 ? 18.057  -1.568  19.296  1.00 35.79  ? 185 ALA A CA    1 
ATOM   1527 C  C     . ALA A 1 213 ? 18.828  -0.463  18.581  1.00 38.07  ? 185 ALA A C     1 
ATOM   1528 O  O     . ALA A 1 213 ? 19.301  0.492   19.212  1.00 38.97  ? 185 ALA A O     1 
ATOM   1529 C  CB    . ALA A 1 213 ? 18.947  -2.801  19.474  1.00 36.26  ? 185 ALA A CB    1 
ATOM   1530 N  N     . ILE A 1 214 ? 18.961  -0.572  17.256  1.00 30.19  ? 186 ILE A N     1 
ATOM   1531 C  CA    . ILE A 1 214 ? 19.765  0.375   16.493  1.00 30.87  ? 186 ILE A CA    1 
ATOM   1532 C  C     . ILE A 1 214 ? 19.037  1.705   16.328  1.00 33.64  ? 186 ILE A C     1 
ATOM   1533 O  O     . ILE A 1 214 ? 19.649  2.777   16.433  1.00 35.12  ? 186 ILE A O     1 
ATOM   1534 C  CB    . ILE A 1 214 ? 20.148  -0.241  15.132  1.00 32.81  ? 186 ILE A CB    1 
ATOM   1535 C  CG1   . ILE A 1 214 ? 21.206  -1.336  15.337  1.00 38.22  ? 186 ILE A CG1   1 
ATOM   1536 C  CG2   . ILE A 1 214 ? 20.690  0.824   14.183  1.00 30.80  ? 186 ILE A CG2   1 
ATOM   1537 C  CD1   . ILE A 1 214 ? 21.369  -2.282  14.172  1.00 39.53  ? 186 ILE A CD1   1 
ATOM   1538 N  N     . ILE A 1 215 ? 17.732  1.666   16.047  1.00 29.84  ? 187 ILE A N     1 
ATOM   1539 C  CA    . ILE A 1 215 ? 16.966  2.910   15.932  1.00 30.36  ? 187 ILE A CA    1 
ATOM   1540 C  C     . ILE A 1 215 ? 17.058  3.707   17.234  1.00 33.72  ? 187 ILE A C     1 
ATOM   1541 O  O     . ILE A 1 215 ? 17.332  4.913   17.230  1.00 34.60  ? 187 ILE A O     1 
ATOM   1542 C  CB    . ILE A 1 215 ? 15.508  2.603   15.542  1.00 31.04  ? 187 ILE A CB    1 
ATOM   1543 C  CG1   . ILE A 1 215 ? 15.453  2.165   14.063  1.00 30.27  ? 187 ILE A CG1   1 
ATOM   1544 C  CG2   . ILE A 1 215 ? 14.582  3.833   15.769  1.00 32.92  ? 187 ILE A CG2   1 
ATOM   1545 C  CD1   . ILE A 1 215 ? 14.074  1.499   13.672  1.00 34.20  ? 187 ILE A CD1   1 
ATOM   1546 N  N     . THR A 1 216 ? 16.894  3.026   18.372  1.00 33.53  ? 188 THR A N     1 
ATOM   1547 C  CA    . THR A 1 216 ? 16.900  3.725   19.661  1.00 37.98  ? 188 THR A CA    1 
ATOM   1548 C  C     . THR A 1 216 ? 18.285  4.289   19.978  1.00 36.31  ? 188 THR A C     1 
ATOM   1549 O  O     . THR A 1 216 ? 18.411  5.421   20.469  1.00 39.44  ? 188 THR A O     1 
ATOM   1550 C  CB    . THR A 1 216 ? 16.421  2.775   20.767  1.00 36.11  ? 188 THR A CB    1 
ATOM   1551 O  OG1   . THR A 1 216 ? 15.065  2.411   20.511  1.00 42.43  ? 188 THR A OG1   1 
ATOM   1552 C  CG2   . THR A 1 216 ? 16.490  3.450   22.148  1.00 48.41  ? 188 THR A CG2   1 
ATOM   1553 N  N     . ARG A 1 217 ? 19.334  3.537   19.662  1.00 37.59  ? 189 ARG A N     1 
ATOM   1554 C  CA    . ARG A 1 217 ? 20.693  4.028   19.861  1.00 39.79  ? 189 ARG A CA    1 
ATOM   1555 C  C     . ARG A 1 217 ? 20.970  5.317   19.075  1.00 44.31  ? 189 ARG A C     1 
ATOM   1556 O  O     . ARG A 1 217 ? 21.716  6.182   19.552  1.00 41.38  ? 189 ARG A O     1 
ATOM   1557 C  CB    . ARG A 1 217 ? 21.680  2.914   19.481  1.00 39.23  ? 189 ARG A CB    1 
ATOM   1558 C  CG    . ARG A 1 217 ? 23.143  3.307   19.455  1.00 63.56  ? 189 ARG A CG    1 
ATOM   1559 C  CD    . ARG A 1 217 ? 24.054  2.079   19.595  1.00 63.39  ? 189 ARG A CD    1 
ATOM   1560 N  NE    . ARG A 1 217 ? 24.408  1.498   18.304  1.00 75.79  ? 189 ARG A NE    1 
ATOM   1561 C  CZ    . ARG A 1 217 ? 24.137  0.251   17.940  1.00 73.29  ? 189 ARG A CZ    1 
ATOM   1562 N  NH1   . ARG A 1 217 ? 23.526  -0.593  18.759  1.00 67.49  ? 189 ARG A NH1   1 
ATOM   1563 N  NH2   . ARG A 1 217 ? 24.500  -0.165  16.726  1.00 65.68  ? 189 ARG A NH2   1 
ATOM   1564 N  N     . GLN A 1 218 ? 20.380  5.479   17.881  1.00 36.03  ? 190 GLN A N     1 
ATOM   1565 C  CA    . GLN A 1 218 ? 20.603  6.656   17.048  1.00 32.88  ? 190 GLN A CA    1 
ATOM   1566 C  C     . GLN A 1 218 ? 19.612  7.792   17.320  1.00 34.35  ? 190 GLN A C     1 
ATOM   1567 O  O     . GLN A 1 218 ? 19.547  8.742   16.529  1.00 40.27  ? 190 GLN A O     1 
ATOM   1568 C  CB    . GLN A 1 218 ? 20.563  6.272   15.560  1.00 35.94  ? 190 GLN A CB    1 
ATOM   1569 C  CG    . GLN A 1 218 ? 21.671  5.309   15.149  1.00 36.12  ? 190 GLN A CG    1 
ATOM   1570 C  CD    . GLN A 1 218 ? 23.004  6.014   14.957  1.00 46.08  ? 190 GLN A CD    1 
ATOM   1571 O  OE1   . GLN A 1 218 ? 23.061  7.238   14.856  1.00 50.86  ? 190 GLN A OE1   1 
ATOM   1572 N  NE2   . GLN A 1 218 ? 24.077  5.246   14.920  1.00 52.96  ? 190 GLN A NE2   1 
ATOM   1573 N  N     . GLY A 1 219 ? 18.839  7.714   18.401  1.00 36.02  ? 191 GLY A N     1 
ATOM   1574 C  CA    . GLY A 1 219 ? 17.918  8.773   18.790  1.00 38.21  ? 191 GLY A CA    1 
ATOM   1575 C  C     . GLY A 1 219 ? 16.524  8.715   18.198  1.00 41.62  ? 191 GLY A C     1 
ATOM   1576 O  O     . GLY A 1 219 ? 15.731  9.645   18.423  1.00 37.83  ? 191 GLY A O     1 
ATOM   1577 N  N     . GLY A 1 220 ? 16.187  7.657   17.461  1.00 36.35  ? 192 GLY A N     1 
ATOM   1578 C  CA    . GLY A 1 220 ? 14.854  7.515   16.911  1.00 32.35  ? 192 GLY A CA    1 
ATOM   1579 C  C     . GLY A 1 220 ? 13.899  6.881   17.896  1.00 35.77  ? 192 GLY A C     1 
ATOM   1580 O  O     . GLY A 1 220 ? 14.270  6.427   18.973  1.00 37.58  ? 192 GLY A O     1 
ATOM   1581 N  N     . GLU A 1 221 ? 12.628  6.845   17.515  1.00 34.76  ? 193 GLU A N     1 
ATOM   1582 C  CA    . GLU A 1 221 ? 11.609  6.202   18.338  1.00 37.75  ? 193 GLU A CA    1 
ATOM   1583 C  C     . GLU A 1 221 ? 10.755  5.263   17.500  1.00 40.20  ? 193 GLU A C     1 
ATOM   1584 O  O     . GLU A 1 221 ? 10.107  5.701   16.545  1.00 38.46  ? 193 GLU A O     1 
ATOM   1585 C  CB    . GLU A 1 221 ? 10.711  7.233   19.016  1.00 42.43  ? 193 GLU A CB    1 
ATOM   1586 C  CG    . GLU A 1 221 ? 9.666   6.540   19.854  1.00 59.00  ? 193 GLU A CG    1 
ATOM   1587 C  CD    . GLU A 1 221 ? 8.862   7.499   20.670  1.00 72.62  ? 193 GLU A CD    1 
ATOM   1588 O  OE1   . GLU A 1 221 ? 9.197   8.706   20.681  1.00 75.47  ? 193 GLU A OE1   1 
ATOM   1589 O  OE2   . GLU A 1 221 ? 7.888   7.048   21.307  1.00 63.26  ? 193 GLU A OE2   1 
ATOM   1590 N  N     . VAL A 1 222 ? 10.712  3.987   17.887  1.00 37.05  ? 194 VAL A N     1 
ATOM   1591 C  CA    . VAL A 1 222 ? 9.789   3.051   17.253  1.00 35.78  ? 194 VAL A CA    1 
ATOM   1592 C  C     . VAL A 1 222 ? 8.373   3.354   17.727  1.00 41.81  ? 194 VAL A C     1 
ATOM   1593 O  O     . VAL A 1 222 ? 8.109   3.412   18.934  1.00 40.03  ? 194 VAL A O     1 
ATOM   1594 C  CB    . VAL A 1 222 ? 10.191  1.600   17.567  1.00 37.95  ? 194 VAL A CB    1 
ATOM   1595 C  CG1   . VAL A 1 222 ? 9.232   0.604   16.877  1.00 39.81  ? 194 VAL A CG1   1 
ATOM   1596 C  CG2   . VAL A 1 222 ? 11.643  1.358   17.136  1.00 43.80  ? 194 VAL A CG2   1 
ATOM   1597 N  N     . THR A 1 223 ? 7.453   3.558   16.783  1.00 36.26  ? 195 THR A N     1 
ATOM   1598 C  CA    A THR A 1 223 ? 6.081   3.901   17.144  0.77 38.20  ? 195 THR A CA    1 
ATOM   1599 C  CA    B THR A 1 223 ? 6.072   3.916   17.097  0.23 38.45  ? 195 THR A CA    1 
ATOM   1600 C  C     . THR A 1 223 ? 5.119   2.730   17.025  1.00 41.20  ? 195 THR A C     1 
ATOM   1601 O  O     . THR A 1 223 ? 4.258   2.568   17.897  1.00 42.52  ? 195 THR A O     1 
ATOM   1602 C  CB    A THR A 1 223 ? 5.592   5.092   16.304  0.77 44.72  ? 195 THR A CB    1 
ATOM   1603 C  CB    B THR A 1 223 ? 5.585   5.021   16.147  0.23 44.53  ? 195 THR A CB    1 
ATOM   1604 O  OG1   A THR A 1 223 ? 5.318   4.681   14.956  0.77 40.84  ? 195 THR A OG1   1 
ATOM   1605 O  OG1   B THR A 1 223 ? 6.393   6.192   16.317  0.23 51.73  ? 195 THR A OG1   1 
ATOM   1606 C  CG2   A THR A 1 223 ? 6.675   6.139   16.271  0.77 52.79  ? 195 THR A CG2   1 
ATOM   1607 C  CG2   B THR A 1 223 ? 4.138   5.379   16.426  0.23 40.95  ? 195 THR A CG2   1 
ATOM   1608 N  N     . LYS A 1 224 ? 5.242   1.884   16.000  1.00 34.15  ? 196 LYS A N     1 
ATOM   1609 C  CA    . LYS A 1 224 ? 4.386   0.706   15.951  1.00 35.73  ? 196 LYS A CA    1 
ATOM   1610 C  C     . LYS A 1 224 ? 4.984   -0.348  15.031  1.00 36.65  ? 196 LYS A C     1 
ATOM   1611 O  O     . LYS A 1 224 ? 5.874   -0.069  14.223  1.00 36.14  ? 196 LYS A O     1 
ATOM   1612 C  CB    . LYS A 1 224 ? 2.960   1.048   15.502  1.00 52.31  ? 196 LYS A CB    1 
ATOM   1613 C  CG    . LYS A 1 224 ? 2.843   1.825   14.229  1.00 45.34  ? 196 LYS A CG    1 
ATOM   1614 C  CD    . LYS A 1 224 ? 1.481   2.583   14.149  1.00 43.75  ? 196 LYS A CD    1 
ATOM   1615 C  CE    . LYS A 1 224 ? 0.685   2.517   15.445  1.00 53.70  ? 196 LYS A CE    1 
ATOM   1616 N  NZ    . LYS A 1 224 ? -0.284  3.657   15.581  1.00 47.77  ? 196 LYS A NZ    1 
ATOM   1617 N  N     . PHE A 1 225 ? 4.518   -1.578  15.210  1.00 31.83  ? 197 PHE A N     1 
ATOM   1618 C  CA    . PHE A 1 225 ? 4.739   -2.650  14.245  1.00 32.87  ? 197 PHE A CA    1 
ATOM   1619 C  C     . PHE A 1 225 ? 3.459   -2.772  13.419  1.00 39.18  ? 197 PHE A C     1 
ATOM   1620 O  O     . PHE A 1 225 ? 2.370   -2.812  13.993  1.00 40.33  ? 197 PHE A O     1 
ATOM   1621 C  CB    . PHE A 1 225 ? 5.002   -3.992  14.939  1.00 35.41  ? 197 PHE A CB    1 
ATOM   1622 C  CG    . PHE A 1 225 ? 6.198   -4.012  15.863  1.00 33.73  ? 197 PHE A CG    1 
ATOM   1623 C  CD1   . PHE A 1 225 ? 7.442   -3.499  15.481  1.00 36.39  ? 197 PHE A CD1   1 
ATOM   1624 C  CD2   . PHE A 1 225 ? 6.060   -4.499  17.153  1.00 38.21  ? 197 PHE A CD2   1 
ATOM   1625 C  CE1   . PHE A 1 225 ? 8.528   -3.529  16.366  1.00 35.26  ? 197 PHE A CE1   1 
ATOM   1626 C  CE2   . PHE A 1 225 ? 7.143   -4.538  18.026  1.00 38.58  ? 197 PHE A CE2   1 
ATOM   1627 C  CZ    . PHE A 1 225 ? 8.362   -4.043  17.638  1.00 37.64  ? 197 PHE A CZ    1 
ATOM   1628 N  N     . ILE A 1 226 ? 3.576   -2.837  12.088  1.00 30.67  ? 198 ILE A N     1 
ATOM   1629 C  CA    . ILE A 1 226 ? 2.424   -3.025  11.202  1.00 33.59  ? 198 ILE A CA    1 
ATOM   1630 C  C     . ILE A 1 226 ? 2.691   -4.287  10.392  1.00 36.62  ? 198 ILE A C     1 
ATOM   1631 O  O     . ILE A 1 226 ? 3.374   -4.239  9.363   1.00 33.93  ? 198 ILE A O     1 
ATOM   1632 C  CB    . ILE A 1 226 ? 2.181   -1.827  10.276  1.00 36.78  ? 198 ILE A CB    1 
ATOM   1633 C  CG1   . ILE A 1 226 ? 2.039   -0.526  11.071  1.00 41.27  ? 198 ILE A CG1   1 
ATOM   1634 C  CG2   . ILE A 1 226 ? 0.941   -2.080  9.398   1.00 39.84  ? 198 ILE A CG2   1 
ATOM   1635 C  CD1   . ILE A 1 226 ? 2.762   0.627   10.436  1.00 51.46  ? 198 ILE A CD1   1 
ATOM   1636 N  N     . GLY A 1 227 ? 2.144   -5.414  10.832  1.00 35.87  ? 199 GLY A N     1 
ATOM   1637 C  CA    . GLY A 1 227 ? 2.593   -6.689  10.284  1.00 35.02  ? 199 GLY A CA    1 
ATOM   1638 C  C     . GLY A 1 227 ? 4.102   -6.847  10.472  1.00 30.99  ? 199 GLY A C     1 
ATOM   1639 O  O     . GLY A 1 227 ? 4.635   -6.633  11.561  1.00 33.45  ? 199 GLY A O     1 
ATOM   1640 N  N     . ASP A 1 228 ? 4.792   -7.234  9.402   1.00 33.21  ? 200 ASP A N     1 
ATOM   1641 C  CA    . ASP A 1 228 ? 6.239   -7.410  9.437   1.00 30.03  ? 200 ASP A CA    1 
ATOM   1642 C  C     . ASP A 1 228 ? 6.991   -6.098  9.258   1.00 33.05  ? 200 ASP A C     1 
ATOM   1643 O  O     . ASP A 1 228 ? 8.219   -6.116  9.121   1.00 36.13  ? 200 ASP A O     1 
ATOM   1644 C  CB    . ASP A 1 228 ? 6.699   -8.426  8.364   1.00 35.77  ? 200 ASP A CB    1 
ATOM   1645 C  CG    . ASP A 1 228 ? 6.350   -8.004  6.937   1.00 40.90  ? 200 ASP A CG    1 
ATOM   1646 O  OD1   . ASP A 1 228 ? 5.201   -7.610  6.666   1.00 35.54  ? 200 ASP A OD1   1 
ATOM   1647 O  OD2   . ASP A 1 228 ? 7.244   -8.072  6.064   1.00 35.64  ? 200 ASP A OD2   1 
ATOM   1648 N  N     . CYS A 1 229 ? 6.297   -4.959  9.275   1.00 30.05  ? 201 CYS A N     1 
ATOM   1649 C  CA    . CYS A 1 229 ? 6.906   -3.661  9.003   1.00 29.12  ? 201 CYS A CA    1 
ATOM   1650 C  C     . CYS A 1 229 ? 7.146   -2.896  10.307  1.00 34.71  ? 201 CYS A C     1 
ATOM   1651 O  O     . CYS A 1 229 ? 6.256   -2.835  11.164  1.00 37.09  ? 201 CYS A O     1 
ATOM   1652 C  CB    . CYS A 1 229 ? 5.980   -2.865  8.077   1.00 33.94  ? 201 CYS A CB    1 
ATOM   1653 S  SG    . CYS A 1 229 ? 6.437   -1.130  7.831   1.00 42.28  ? 201 CYS A SG    1 
ATOM   1654 N  N     . VAL A 1 230 ? 8.346   -2.323  10.462  1.00 29.09  ? 202 VAL A N     1 
ATOM   1655 C  CA    . VAL A 1 230 ? 8.675   -1.451  11.599  1.00 31.89  ? 202 VAL A CA    1 
ATOM   1656 C  C     . VAL A 1 230 ? 8.486   0.004   11.177  1.00 31.05  ? 202 VAL A C     1 
ATOM   1657 O  O     . VAL A 1 230 ? 9.080   0.440   10.184  1.00 30.67  ? 202 VAL A O     1 
ATOM   1658 C  CB    . VAL A 1 230 ? 10.126  -1.673  12.069  1.00 32.38  ? 202 VAL A CB    1 
ATOM   1659 C  CG1   . VAL A 1 230 ? 10.479  -0.707  13.188  1.00 32.52  ? 202 VAL A CG1   1 
ATOM   1660 C  CG2   . VAL A 1 230 ? 10.349  -3.108  12.538  1.00 35.66  ? 202 VAL A CG2   1 
ATOM   1661 N  N     . MET A 1 231 ? 7.692   0.767   11.937  1.00 31.54  ? 203 MET A N     1 
ATOM   1662 C  CA    . MET A 1 231 ? 7.515   2.195   11.689  1.00 27.96  ? 203 MET A CA    1 
ATOM   1663 C  C     . MET A 1 231 ? 8.153   3.003   12.818  1.00 32.97  ? 203 MET A C     1 
ATOM   1664 O  O     . MET A 1 231 ? 7.911   2.718   13.998  1.00 33.06  ? 203 MET A O     1 
ATOM   1665 C  CB    . MET A 1 231 ? 6.018   2.538   11.517  1.00 30.31  ? 203 MET A CB    1 
ATOM   1666 C  CG    . MET A 1 231 ? 5.766   4.006   11.354  1.00 32.49  ? 203 MET A CG    1 
ATOM   1667 S  SD    . MET A 1 231 ? 3.977   4.307   11.349  1.00 39.21  ? 203 MET A SD    1 
ATOM   1668 C  CE    . MET A 1 231 ? 3.977   5.907   10.557  1.00 39.68  ? 203 MET A CE    1 
ATOM   1669 N  N     . ALA A 1 232 ? 9.001   3.976   12.459  1.00 29.64  ? 204 ALA A N     1 
ATOM   1670 C  CA    . ALA A 1 232 ? 9.758   4.761   13.436  1.00 28.90  ? 204 ALA A CA    1 
ATOM   1671 C  C     . ALA A 1 232 ? 9.866   6.230   13.001  1.00 31.68  ? 204 ALA A C     1 
ATOM   1672 O  O     . ALA A 1 232 ? 9.758   6.555   11.821  1.00 30.71  ? 204 ALA A O     1 
ATOM   1673 C  CB    . ALA A 1 232 ? 11.178  4.168   13.648  1.00 29.53  ? 204 ALA A CB    1 
ATOM   1674 N  N     . TYR A 1 233 ? 10.084  7.129   13.976  1.00 33.76  ? 205 TYR A N     1 
ATOM   1675 C  CA    . TYR A 1 233 ? 10.282  8.555   13.710  1.00 30.69  ? 205 TYR A CA    1 
ATOM   1676 C  C     . TYR A 1 233 ? 11.662  8.999   14.150  1.00 32.08  ? 205 TYR A C     1 
ATOM   1677 O  O     . TYR A 1 233 ? 12.153  8.558   15.192  1.00 35.35  ? 205 TYR A O     1 
ATOM   1678 C  CB    . TYR A 1 233 ? 9.298   9.449   14.491  1.00 33.36  ? 205 TYR A CB    1 
ATOM   1679 C  CG    . TYR A 1 233 ? 7.837   9.239   14.200  1.00 33.89  ? 205 TYR A CG    1 
ATOM   1680 C  CD1   . TYR A 1 233 ? 7.381   9.084   12.902  1.00 34.40  ? 205 TYR A CD1   1 
ATOM   1681 C  CD2   . TYR A 1 233 ? 6.912   9.256   15.226  1.00 42.31  ? 205 TYR A CD2   1 
ATOM   1682 C  CE1   . TYR A 1 233 ? 6.039   8.912   12.637  1.00 34.19  ? 205 TYR A CE1   1 
ATOM   1683 C  CE2   . TYR A 1 233 ? 5.575   9.072   14.970  1.00 43.17  ? 205 TYR A CE2   1 
ATOM   1684 C  CZ    . TYR A 1 233 ? 5.146   8.904   13.676  1.00 39.19  ? 205 TYR A CZ    1 
ATOM   1685 O  OH    . TYR A 1 233 ? 3.800   8.728   13.400  1.00 46.90  ? 205 TYR A OH    1 
ATOM   1686 N  N     . PHE A 1 234 ? 12.250  9.924   13.380  1.00 31.60  ? 206 PHE A N     1 
ATOM   1687 C  CA    . PHE A 1 234 ? 13.403  10.737  13.764  1.00 33.97  ? 206 PHE A CA    1 
ATOM   1688 C  C     . PHE A 1 234 ? 13.027  12.212  13.640  1.00 37.43  ? 206 PHE A C     1 
ATOM   1689 O  O     . PHE A 1 234 ? 12.186  12.575  12.818  1.00 34.64  ? 206 PHE A O     1 
ATOM   1690 C  CB    . PHE A 1 234 ? 14.639  10.457  12.856  1.00 31.70  ? 206 PHE A CB    1 
ATOM   1691 C  CG    . PHE A 1 234 ? 15.233  9.072   13.027  1.00 31.09  ? 206 PHE A CG    1 
ATOM   1692 C  CD1   . PHE A 1 234 ? 14.654  7.970   12.401  1.00 36.07  ? 206 PHE A CD1   1 
ATOM   1693 C  CD2   . PHE A 1 234 ? 16.390  8.885   13.773  1.00 34.90  ? 206 PHE A CD2   1 
ATOM   1694 C  CE1   . PHE A 1 234 ? 15.199  6.681   12.549  1.00 33.43  ? 206 PHE A CE1   1 
ATOM   1695 C  CE2   . PHE A 1 234 ? 16.952  7.608   13.928  1.00 36.35  ? 206 PHE A CE2   1 
ATOM   1696 C  CZ    . PHE A 1 234 ? 16.364  6.506   13.318  1.00 32.55  ? 206 PHE A CZ    1 
ATOM   1697 N  N     . ASP A 1 235 ? 13.666  13.076  14.436  1.00 38.99  ? 207 ASP A N     1 
ATOM   1698 C  CA    . ASP A 1 235 ? 13.420  14.514  14.302  1.00 40.04  ? 207 ASP A CA    1 
ATOM   1699 C  C     . ASP A 1 235 ? 13.700  14.980  12.876  1.00 37.29  ? 207 ASP A C     1 
ATOM   1700 O  O     . ASP A 1 235 ? 14.524  14.402  12.159  1.00 36.11  ? 207 ASP A O     1 
ATOM   1701 C  CB    . ASP A 1 235 ? 14.296  15.306  15.276  1.00 44.26  ? 207 ASP A CB    1 
ATOM   1702 C  CG    . ASP A 1 235 ? 13.725  15.346  16.687  1.00 50.91  ? 207 ASP A CG    1 
ATOM   1703 O  OD1   . ASP A 1 235 ? 12.640  14.785  16.920  1.00 50.45  ? 207 ASP A OD1   1 
ATOM   1704 O  OD2   . ASP A 1 235 ? 14.373  15.931  17.574  1.00 58.32  ? 207 ASP A OD2   1 
ATOM   1705 N  N     . GLY A 1 236 ? 13.007  16.052  12.466  1.00 38.46  ? 208 GLY A N     1 
ATOM   1706 C  CA    . GLY A 1 236 ? 13.038  16.501  11.079  1.00 38.93  ? 208 GLY A CA    1 
ATOM   1707 C  C     . GLY A 1 236 ? 14.387  16.994  10.604  1.00 44.68  ? 208 GLY A C     1 
ATOM   1708 O  O     . GLY A 1 236 ? 14.635  17.038  9.394   1.00 50.53  ? 208 GLY A O     1 
ATOM   1709 N  N     . ASP A 1 237 ? 15.267  17.363  11.522  1.00 40.15  ? 209 ASP A N     1 
ATOM   1710 C  CA    . ASP A 1 237 ? 16.623  17.755  11.166  1.00 48.70  ? 209 ASP A CA    1 
ATOM   1711 C  C     . ASP A 1 237 ? 17.657  16.699  11.552  1.00 48.53  ? 209 ASP A C     1 
ATOM   1712 O  O     . ASP A 1 237 ? 18.839  17.019  11.720  1.00 50.09  ? 209 ASP A O     1 
ATOM   1713 C  CB    . ASP A 1 237 ? 16.952  19.120  11.781  1.00 51.08  ? 209 ASP A CB    1 
ATOM   1714 C  CG    . ASP A 1 237 ? 17.035  19.094  13.294  1.00 58.81  ? 209 ASP A CG    1 
ATOM   1715 O  OD1   . ASP A 1 237 ? 16.610  18.107  13.931  1.00 59.14  ? 209 ASP A OD1   1 
ATOM   1716 O  OD2   . ASP A 1 237 ? 17.546  20.085  13.861  1.00 79.37  ? 209 ASP A OD2   1 
ATOM   1717 N  N     . CYS A 1 238 ? 17.239  15.440  11.685  1.00 38.44  ? 210 CYS A N     1 
ATOM   1718 C  CA    . CYS A 1 238 ? 18.127  14.334  12.030  1.00 34.79  ? 210 CYS A CA    1 
ATOM   1719 C  C     . CYS A 1 238 ? 18.210  13.293  10.917  1.00 35.31  ? 210 CYS A C     1 
ATOM   1720 O  O     . CYS A 1 238 ? 18.234  12.092  11.184  1.00 35.14  ? 210 CYS A O     1 
ATOM   1721 C  CB    . CYS A 1 238 ? 17.681  13.665  13.323  1.00 30.93  ? 210 CYS A CB    1 
ATOM   1722 S  SG    . CYS A 1 238 ? 18.022  14.692  14.804  1.00 43.67  ? 210 CYS A SG    1 
ATOM   1723 N  N     . ALA A 1 239 ? 18.259  13.737  9.660   1.00 35.64  ? 211 ALA A N     1 
ATOM   1724 C  CA    . ALA A 1 239 ? 18.386  12.787  8.550   1.00 37.43  ? 211 ALA A CA    1 
ATOM   1725 C  C     . ALA A 1 239 ? 19.693  11.998  8.619   1.00 38.73  ? 211 ALA A C     1 
ATOM   1726 O  O     . ALA A 1 239 ? 19.728  10.821  8.232   1.00 32.08  ? 211 ALA A O     1 
ATOM   1727 C  CB    . ALA A 1 239 ? 18.281  13.510  7.205   1.00 36.26  ? 211 ALA A CB    1 
ATOM   1728 N  N     . ASP A 1 240 ? 20.790  12.627  9.076   1.00 33.19  ? 212 ASP A N     1 
ATOM   1729 C  CA    . ASP A 1 240 ? 22.060  11.901  9.167   1.00 36.01  ? 212 ASP A CA    1 
ATOM   1730 C  C     . ASP A 1 240 ? 21.923  10.678  10.068  1.00 31.39  ? 212 ASP A C     1 
ATOM   1731 O  O     . ASP A 1 240 ? 22.466  9.607   9.767   1.00 34.29  ? 212 ASP A O     1 
ATOM   1732 C  CB    . ASP A 1 240 ? 23.179  12.808  9.701   1.00 36.50  ? 212 ASP A CB    1 
ATOM   1733 C  CG    . ASP A 1 240 ? 23.544  13.929  8.737   1.00 42.89  ? 212 ASP A CG    1 
ATOM   1734 O  OD1   . ASP A 1 240 ? 23.731  13.669  7.527   1.00 38.30  ? 212 ASP A OD1   1 
ATOM   1735 O  OD2   . ASP A 1 240 ? 23.632  15.090  9.197   1.00 49.82  ? 212 ASP A OD2   1 
ATOM   1736 N  N     . GLN A 1 241 ? 21.212  10.830  11.181  1.00 30.37  ? 213 GLN A N     1 
ATOM   1737 C  CA    . GLN A 1 241 ? 21.020  9.731   12.122  1.00 33.58  ? 213 GLN A CA    1 
ATOM   1738 C  C     . GLN A 1 241 ? 20.112  8.648   11.549  1.00 34.33  ? 213 GLN A C     1 
ATOM   1739 O  O     . GLN A 1 241 ? 20.330  7.455   11.809  1.00 33.02  ? 213 GLN A O     1 
ATOM   1740 C  CB    . GLN A 1 241 ? 20.483  10.301  13.436  1.00 35.79  ? 213 GLN A CB    1 
ATOM   1741 C  CG    . GLN A 1 241 ? 21.590  11.095  14.149  1.00 39.45  ? 213 GLN A CG    1 
ATOM   1742 C  CD    . GLN A 1 241 ? 21.443  12.601  14.027  1.00 52.31  ? 213 GLN A CD    1 
ATOM   1743 O  OE1   . GLN A 1 241 ? 21.068  13.126  12.969  1.00 44.42  ? 213 GLN A OE1   1 
ATOM   1744 N  NE2   . GLN A 1 241 ? 21.780  13.312  15.099  1.00 67.22  ? 213 GLN A NE2   1 
ATOM   1745 N  N     . ALA A 1 242 ? 19.097  9.041   10.770  1.00 33.02  ? 214 ALA A N     1 
ATOM   1746 C  CA    . ALA A 1 242 ? 18.217  8.055   10.128  1.00 29.34  ? 214 ALA A CA    1 
ATOM   1747 C  C     . ALA A 1 242 ? 18.966  7.259   9.055   1.00 32.43  ? 214 ALA A C     1 
ATOM   1748 O  O     . ALA A 1 242 ? 18.776  6.040   8.927   1.00 29.98  ? 214 ALA A O     1 
ATOM   1749 C  CB    . ALA A 1 242 ? 17.000  8.756   9.517   1.00 31.63  ? 214 ALA A CB    1 
ATOM   1750 N  N     . ILE A 1 243 ? 19.805  7.930   8.261   1.00 29.38  ? 215 ILE A N     1 
ATOM   1751 C  CA    . ILE A 1 243 ? 20.601  7.204   7.266   1.00 27.21  ? 215 ILE A CA    1 
ATOM   1752 C  C     . ILE A 1 243 ? 21.601  6.267   7.943   1.00 34.91  ? 215 ILE A C     1 
ATOM   1753 O  O     . ILE A 1 243 ? 21.768  5.116   7.522   1.00 32.32  ? 215 ILE A O     1 
ATOM   1754 C  CB    . ILE A 1 243 ? 21.296  8.194   6.311   1.00 26.29  ? 215 ILE A CB    1 
ATOM   1755 C  CG1   . ILE A 1 243 ? 20.251  8.927   5.450   1.00 30.91  ? 215 ILE A CG1   1 
ATOM   1756 C  CG2   . ILE A 1 243 ? 22.349  7.480   5.418   1.00 32.14  ? 215 ILE A CG2   1 
ATOM   1757 C  CD1   . ILE A 1 243 ? 20.825  10.144  4.699   1.00 35.34  ? 215 ILE A CD1   1 
ATOM   1758 N  N     . GLN A 1 244 ? 22.269  6.724   9.013   1.00 28.98  ? 216 GLN A N     1 
ATOM   1759 C  CA    . GLN A 1 244 ? 23.238  5.862   9.692   1.00 31.71  ? 216 GLN A CA    1 
ATOM   1760 C  C     . GLN A 1 244 ? 22.559  4.657   10.328  1.00 30.38  ? 216 GLN A C     1 
ATOM   1761 O  O     . GLN A 1 244 ? 23.093  3.541   10.280  1.00 31.63  ? 216 GLN A O     1 
ATOM   1762 C  CB    . GLN A 1 244 ? 24.015  6.641   10.762  1.00 31.70  ? 216 GLN A CB    1 
ATOM   1763 C  CG    . GLN A 1 244 ? 25.124  5.821   11.444  1.00 33.68  ? 216 GLN A CG    1 
ATOM   1764 C  CD    . GLN A 1 244 ? 26.266  5.494   10.487  1.00 42.03  ? 216 GLN A CD    1 
ATOM   1765 O  OE1   . GLN A 1 244 ? 26.920  6.393   9.965   1.00 43.66  ? 216 GLN A OE1   1 
ATOM   1766 N  NE2   . GLN A 1 244 ? 26.491  4.212   10.233  1.00 45.48  ? 216 GLN A NE2   1 
ATOM   1767 N  N     . ALA A 1 245 ? 21.373  4.851   10.926  1.00 27.79  ? 217 ALA A N     1 
ATOM   1768 C  CA    . ALA A 1 245 ? 20.664  3.710   11.502  1.00 27.98  ? 217 ALA A CA    1 
ATOM   1769 C  C     . ALA A 1 245 ? 20.341  2.670   10.432  1.00 30.94  ? 217 ALA A C     1 
ATOM   1770 O  O     . ALA A 1 245 ? 20.433  1.458   10.683  1.00 29.06  ? 217 ALA A O     1 
ATOM   1771 C  CB    . ALA A 1 245 ? 19.369  4.180   12.180  1.00 28.58  ? 217 ALA A CB    1 
ATOM   1772 N  N     . SER A 1 246 ? 19.921  3.130   9.246   1.00 27.60  ? 218 SER A N     1 
ATOM   1773 C  CA    . SER A 1 246 ? 19.593  2.218   8.150   1.00 28.42  ? 218 SER A CA    1 
ATOM   1774 C  C     . SER A 1 246 ? 20.813  1.407   7.720   1.00 29.82  ? 218 SER A C     1 
ATOM   1775 O  O     . SER A 1 246 ? 20.726  0.188   7.516   1.00 30.02  ? 218 SER A O     1 
ATOM   1776 C  CB    . SER A 1 246 ? 19.029  3.012   6.961   1.00 30.42  ? 218 SER A CB    1 
ATOM   1777 O  OG    . SER A 1 246 ? 17.859  3.725   7.359   1.00 30.47  ? 218 SER A OG    1 
ATOM   1778 N  N     . LEU A 1 247 ? 21.966  2.071   7.570   1.00 28.55  ? 219 LEU A N     1 
ATOM   1779 C  CA    . LEU A 1 247 ? 23.176  1.351   7.166   1.00 28.44  ? 219 LEU A CA    1 
ATOM   1780 C  C     . LEU A 1 247 ? 23.616  0.357   8.241   1.00 33.32  ? 219 LEU A C     1 
ATOM   1781 O  O     . LEU A 1 247 ? 24.040  -0.763  7.926   1.00 31.81  ? 219 LEU A O     1 
ATOM   1782 C  CB    . LEU A 1 247 ? 24.302  2.346   6.853   1.00 31.58  ? 219 LEU A CB    1 
ATOM   1783 C  CG    . LEU A 1 247 ? 24.084  3.237   5.631   1.00 33.39  ? 219 LEU A CG    1 
ATOM   1784 C  CD1   . LEU A 1 247 ? 25.127  4.371   5.530   1.00 37.35  ? 219 LEU A CD1   1 
ATOM   1785 C  CD2   . LEU A 1 247 ? 24.066  2.390   4.368   1.00 36.81  ? 219 LEU A CD2   1 
ATOM   1786 N  N     . ASP A 1 248 ? 23.504  0.739   9.517   1.00 27.62  ? 220 ASP A N     1 
ATOM   1787 C  CA    . ASP A 1 248 ? 23.867  -0.176  10.603  1.00 31.63  ? 220 ASP A CA    1 
ATOM   1788 C  C     . ASP A 1 248 ? 22.950  -1.403  10.656  1.00 36.31  ? 220 ASP A C     1 
ATOM   1789 O  O     . ASP A 1 248 ? 23.410  -2.517  10.951  1.00 30.95  ? 220 ASP A O     1 
ATOM   1790 C  CB    . ASP A 1 248 ? 23.837  0.551   11.949  1.00 31.22  ? 220 ASP A CB    1 
ATOM   1791 C  CG    . ASP A 1 248 ? 24.983  1.545   12.115  1.00 41.60  ? 220 ASP A CG    1 
ATOM   1792 O  OD1   . ASP A 1 248 ? 25.919  1.545   11.297  1.00 39.16  ? 220 ASP A OD1   1 
ATOM   1793 O  OD2   . ASP A 1 248 ? 24.940  2.311   13.095  1.00 44.49  ? 220 ASP A OD2   1 
ATOM   1794 N  N     . ILE A 1 249 ? 21.647  -1.227  10.410  1.00 29.35  ? 221 ILE A N     1 
ATOM   1795 C  CA    . ILE A 1 249 ? 20.761  -2.393  10.357  1.00 29.66  ? 221 ILE A CA    1 
ATOM   1796 C  C     . ILE A 1 249 ? 21.178  -3.332  9.227   1.00 29.41  ? 221 ILE A C     1 
ATOM   1797 O  O     . ILE A 1 249 ? 21.236  -4.558  9.415   1.00 30.95  ? 221 ILE A O     1 
ATOM   1798 C  CB    . ILE A 1 249 ? 19.284  -1.953  10.220  1.00 28.88  ? 221 ILE A CB    1 
ATOM   1799 C  CG1   . ILE A 1 249 ? 18.828  -1.328  11.531  1.00 27.42  ? 221 ILE A CG1   1 
ATOM   1800 C  CG2   . ILE A 1 249 ? 18.366  -3.141  9.835   1.00 32.27  ? 221 ILE A CG2   1 
ATOM   1801 C  CD1   . ILE A 1 249 ? 17.406  -0.617  11.439  1.00 32.56  ? 221 ILE A CD1   1 
ATOM   1802 N  N     . LEU A 1 250 ? 21.485  -2.784  8.041   1.00 27.76  ? 222 LEU A N     1 
ATOM   1803 C  CA    . LEU A 1 250 ? 21.892  -3.660  6.938   1.00 31.66  ? 222 LEU A CA    1 
ATOM   1804 C  C     . LEU A 1 250 ? 23.166  -4.433  7.291   1.00 33.10  ? 222 LEU A C     1 
ATOM   1805 O  O     . LEU A 1 250 ? 23.287  -5.626  6.975   1.00 33.53  ? 222 LEU A O     1 
ATOM   1806 C  CB    . LEU A 1 250 ? 22.093  -2.854  5.650   1.00 31.72  ? 222 LEU A CB    1 
ATOM   1807 C  CG    . LEU A 1 250 ? 20.792  -2.278  5.065   1.00 32.62  ? 222 LEU A CG    1 
ATOM   1808 C  CD1   . LEU A 1 250 ? 21.089  -1.508  3.778   1.00 40.39  ? 222 LEU A CD1   1 
ATOM   1809 C  CD2   . LEU A 1 250 ? 19.715  -3.359  4.829   1.00 35.62  ? 222 LEU A CD2   1 
ATOM   1810 N  N     . MET A 1 251 ? 24.118  -3.768  7.952   1.00 29.54  ? 223 MET A N     1 
ATOM   1811 C  CA    A MET A 1 251 ? 25.375  -4.418  8.330   0.57 37.13  ? 223 MET A CA    1 
ATOM   1812 C  CA    B MET A 1 251 ? 25.369  -4.432  8.314   0.43 37.12  ? 223 MET A CA    1 
ATOM   1813 C  C     . MET A 1 251 ? 25.140  -5.536  9.342   1.00 36.98  ? 223 MET A C     1 
ATOM   1814 O  O     . MET A 1 251 ? 25.706  -6.630  9.216   1.00 33.94  ? 223 MET A O     1 
ATOM   1815 C  CB    A MET A 1 251 ? 26.347  -3.379  8.898   0.57 34.49  ? 223 MET A CB    1 
ATOM   1816 C  CB    B MET A 1 251 ? 26.383  -3.403  8.823   0.43 34.55  ? 223 MET A CB    1 
ATOM   1817 C  CG    A MET A 1 251 ? 27.482  -3.969  9.755   0.57 35.07  ? 223 MET A CG    1 
ATOM   1818 C  CG    B MET A 1 251 ? 27.808  -3.595  8.289   0.43 47.51  ? 223 MET A CG    1 
ATOM   1819 S  SD    A MET A 1 251 ? 28.719  -2.719  10.167  0.57 49.73  ? 223 MET A SD    1 
ATOM   1820 S  SD    B MET A 1 251 ? 28.583  -5.160  8.742   0.43 57.30  ? 223 MET A SD    1 
ATOM   1821 C  CE    A MET A 1 251 ? 29.099  -2.059  8.547   0.57 49.29  ? 223 MET A CE    1 
ATOM   1822 C  CE    B MET A 1 251 ? 28.335  -6.210  7.317   0.43 32.88  ? 223 MET A CE    1 
ATOM   1823 N  N     . GLU A 1 252 ? 24.311  -5.281  10.362  1.00 28.68  ? 224 GLU A N     1 
ATOM   1824 C  CA    . GLU A 1 252 ? 24.057  -6.302  11.386  1.00 28.76  ? 224 GLU A CA    1 
ATOM   1825 C  C     . GLU A 1 252 ? 23.319  -7.514  10.816  1.00 33.23  ? 224 GLU A C     1 
ATOM   1826 O  O     . GLU A 1 252 ? 23.537  -8.652  11.266  1.00 31.02  ? 224 GLU A O     1 
ATOM   1827 C  CB    . GLU A 1 252 ? 23.238  -5.718  12.538  1.00 33.69  ? 224 GLU A CB    1 
ATOM   1828 C  CG    . GLU A 1 252 ? 24.027  -4.817  13.446  1.00 44.31  ? 224 GLU A CG    1 
ATOM   1829 C  CD    . GLU A 1 252 ? 25.157  -5.544  14.165  1.00 50.30  ? 224 GLU A CD    1 
ATOM   1830 O  OE1   . GLU A 1 252 ? 24.911  -6.630  14.733  1.00 50.43  ? 224 GLU A OE1   1 
ATOM   1831 O  OE2   . GLU A 1 252 ? 26.283  -5.014  14.178  1.00 58.98  ? 224 GLU A OE2   1 
ATOM   1832 N  N     . LEU A 1 253 ? 22.425  -7.294  9.846   1.00 29.76  ? 225 LEU A N     1 
ATOM   1833 C  CA    . LEU A 1 253 ? 21.708  -8.428  9.263   1.00 28.11  ? 225 LEU A CA    1 
ATOM   1834 C  C     . LEU A 1 253 ? 22.649  -9.293  8.422   1.00 29.69  ? 225 LEU A C     1 
ATOM   1835 O  O     . LEU A 1 253 ? 22.491  -10.516 8.376   1.00 31.05  ? 225 LEU A O     1 
ATOM   1836 C  CB    . LEU A 1 253 ? 20.520  -7.947  8.416   1.00 27.74  ? 225 LEU A CB    1 
ATOM   1837 C  CG    . LEU A 1 253 ? 19.353  -7.280  9.209   1.00 31.84  ? 225 LEU A CG    1 
ATOM   1838 C  CD1   . LEU A 1 253 ? 18.200  -6.872  8.259   1.00 37.63  ? 225 LEU A CD1   1 
ATOM   1839 C  CD2   . LEU A 1 253 ? 18.844  -8.142  10.337  1.00 34.46  ? 225 LEU A CD2   1 
ATOM   1840 N  N     . GLU A 1 254 ? 23.623  -8.681  7.741   1.00 30.29  ? 226 GLU A N     1 
ATOM   1841 C  CA    . GLU A 1 254 ? 24.600  -9.492  6.998   1.00 29.43  ? 226 GLU A CA    1 
ATOM   1842 C  C     . GLU A 1 254 ? 25.425  -10.357 7.951   1.00 31.67  ? 226 GLU A C     1 
ATOM   1843 O  O     . GLU A 1 254 ? 25.690  -11.535 7.669   1.00 32.96  ? 226 GLU A O     1 
ATOM   1844 C  CB    . GLU A 1 254 ? 25.501  -8.583  6.155   1.00 31.66  ? 226 GLU A CB    1 
ATOM   1845 C  CG    . GLU A 1 254 ? 26.723  -9.289  5.531   1.00 37.01  ? 226 GLU A CG    1 
ATOM   1846 C  CD    . GLU A 1 254 ? 26.391  -10.060 4.265   1.00 45.00  ? 226 GLU A CD    1 
ATOM   1847 O  OE1   . GLU A 1 254 ? 25.342  -9.776  3.648   1.00 46.96  ? 226 GLU A OE1   1 
ATOM   1848 O  OE2   . GLU A 1 254 ? 27.184  -10.958 3.878   1.00 49.02  ? 226 GLU A OE2   1 
ATOM   1849 N  N     . ILE A 1 255 ? 25.823  -9.793  9.095   1.00 31.31  ? 227 ILE A N     1 
ATOM   1850 C  CA    . ILE A 1 255 ? 26.569  -10.556 10.100  1.00 34.85  ? 227 ILE A CA    1 
ATOM   1851 C  C     . ILE A 1 255 ? 25.720  -11.699 10.641  1.00 36.86  ? 227 ILE A C     1 
ATOM   1852 O  O     . ILE A 1 255 ? 26.191  -12.840 10.792  1.00 34.16  ? 227 ILE A O     1 
ATOM   1853 C  CB    . ILE A 1 255 ? 27.060  -9.618  11.224  1.00 34.33  ? 227 ILE A CB    1 
ATOM   1854 C  CG1   . ILE A 1 255 ? 28.177  -8.690  10.718  1.00 33.53  ? 227 ILE A CG1   1 
ATOM   1855 C  CG2   . ILE A 1 255 ? 27.547  -10.427 12.459  1.00 44.72  ? 227 ILE A CG2   1 
ATOM   1856 C  CD1   . ILE A 1 255 ? 28.383  -7.461  11.600  1.00 38.68  ? 227 ILE A CD1   1 
ATOM   1857 N  N     . LEU A 1 256 ? 24.443  -11.424 10.901  1.00 31.69  ? 228 LEU A N     1 
ATOM   1858 C  CA    . LEU A 1 256 ? 23.545  -12.446 11.413  1.00 29.54  ? 228 LEU A CA    1 
ATOM   1859 C  C     . LEU A 1 256 ? 23.390  -13.605 10.425  1.00 33.41  ? 228 LEU A C     1 
ATOM   1860 O  O     . LEU A 1 256 ? 23.446  -14.777 10.825  1.00 30.34  ? 228 LEU A O     1 
ATOM   1861 C  CB    . LEU A 1 256 ? 22.188  -11.802 11.729  1.00 30.49  ? 228 LEU A CB    1 
ATOM   1862 C  CG    . LEU A 1 256 ? 21.085  -12.660 12.330  1.00 42.50  ? 228 LEU A CG    1 
ATOM   1863 C  CD1   . LEU A 1 256 ? 21.540  -13.194 13.669  1.00 44.76  ? 228 LEU A CD1   1 
ATOM   1864 C  CD2   . LEU A 1 256 ? 19.819  -11.794 12.519  1.00 45.04  ? 228 LEU A CD2   1 
ATOM   1865 N  N     . ARG A 1 257 ? 23.208  -13.289 9.133   1.00 28.86  ? 229 ARG A N     1 
ATOM   1866 C  CA    . ARG A 1 257 ? 23.031  -14.308 8.092   1.00 29.92  ? 229 ARG A CA    1 
ATOM   1867 C  C     . ARG A 1 257 ? 24.259  -15.211 8.005   1.00 33.74  ? 229 ARG A C     1 
ATOM   1868 O  O     . ARG A 1 257 ? 24.134  -16.437 7.881   1.00 33.71  ? 229 ARG A O     1 
ATOM   1869 C  CB    . ARG A 1 257 ? 22.810  -13.642 6.719   1.00 31.49  ? 229 ARG A CB    1 
ATOM   1870 C  CG    . ARG A 1 257 ? 21.359  -13.248 6.427   1.00 29.40  ? 229 ARG A CG    1 
ATOM   1871 C  CD    . ARG A 1 257 ? 21.102  -12.659 5.017   1.00 28.45  ? 229 ARG A CD    1 
ATOM   1872 N  NE    . ARG A 1 257 ? 22.032  -11.610 4.600   1.00 31.11  ? 229 ARG A NE    1 
ATOM   1873 C  CZ    . ARG A 1 257 ? 21.703  -10.320 4.628   1.00 33.60  ? 229 ARG A CZ    1 
ATOM   1874 N  NH1   . ARG A 1 257 ? 20.563  -9.911  5.170   1.00 31.97  ? 229 ARG A NH1   1 
ATOM   1875 N  NH2   . ARG A 1 257 ? 22.545  -9.417  4.130   1.00 32.03  ? 229 ARG A NH2   1 
ATOM   1876 N  N     . ASN A 1 258 ? 25.441  -14.609 8.054   1.00 30.83  ? 230 ASN A N     1 
ATOM   1877 C  CA    . ASN A 1 258 ? 26.695  -15.365 7.897   1.00 29.27  ? 230 ASN A CA    1 
ATOM   1878 C  C     . ASN A 1 258 ? 27.029  -16.224 9.123   1.00 36.28  ? 230 ASN A C     1 
ATOM   1879 O  O     . ASN A 1 258 ? 27.714  -17.261 9.000   1.00 35.62  ? 230 ASN A O     1 
ATOM   1880 C  CB    . ASN A 1 258 ? 27.861  -14.401 7.655   1.00 33.83  ? 230 ASN A CB    1 
ATOM   1881 C  CG    . ASN A 1 258 ? 27.738  -13.591 6.361   1.00 40.65  ? 230 ASN A CG    1 
ATOM   1882 O  OD1   . ASN A 1 258 ? 27.000  -13.942 5.453   1.00 48.04  ? 230 ASN A OD1   1 
ATOM   1883 N  ND2   . ASN A 1 258 ? 28.487  -12.507 6.287   1.00 41.60  ? 230 ASN A ND2   1 
ATOM   1884 N  N     . SER A 1 259 ? 26.609  -15.796 10.313  1.00 29.50  ? 231 SER A N     1 
ATOM   1885 C  CA    A SER A 1 259 ? 27.074  -16.431 11.538  0.57 32.56  ? 231 SER A CA    1 
ATOM   1886 C  CA    B SER A 1 259 ? 27.047  -16.389 11.571  0.43 32.62  ? 231 SER A CA    1 
ATOM   1887 C  C     . SER A 1 259 ? 26.080  -17.419 12.135  1.00 35.14  ? 231 SER A C     1 
ATOM   1888 O  O     . SER A 1 259 ? 26.431  -18.097 13.111  1.00 34.29  ? 231 SER A O     1 
ATOM   1889 C  CB    A SER A 1 259 ? 27.431  -15.369 12.591  0.57 36.80  ? 231 SER A CB    1 
ATOM   1890 C  CB    B SER A 1 259 ? 27.265  -15.297 12.628  0.43 36.63  ? 231 SER A CB    1 
ATOM   1891 O  OG    A SER A 1 259 ? 26.350  -14.491 12.834  0.57 35.72  ? 231 SER A OG    1 
ATOM   1892 O  OG    B SER A 1 259 ? 28.021  -14.220 12.118  0.43 37.44  ? 231 SER A OG    1 
ATOM   1893 N  N     . ALA A 1 260 ? 24.872  -17.542 11.568  1.00 31.48  ? 232 ALA A N     1 
ATOM   1894 C  CA    . ALA A 1 260 ? 23.864  -18.449 12.102  1.00 36.01  ? 232 ALA A CA    1 
ATOM   1895 C  C     . ALA A 1 260 ? 24.266  -19.917 11.922  1.00 35.48  ? 232 ALA A C     1 
ATOM   1896 O  O     . ALA A 1 260 ? 25.085  -20.255 11.061  1.00 34.66  ? 232 ALA A O     1 
ATOM   1897 C  CB    . ALA A 1 260 ? 22.514  -18.195 11.421  1.00 35.83  ? 232 ALA A CB    1 
ATOM   1898 N  N     . PRO A 1 261 ? 23.688  -20.814 12.720  1.00 36.69  ? 233 PRO A N     1 
ATOM   1899 C  CA    . PRO A 1 261 ? 23.955  -22.246 12.540  1.00 39.32  ? 233 PRO A CA    1 
ATOM   1900 C  C     . PRO A 1 261 ? 23.597  -22.743 11.147  1.00 42.43  ? 233 PRO A C     1 
ATOM   1901 O  O     . PRO A 1 261 ? 22.791  -22.158 10.420  1.00 33.94  ? 233 PRO A O     1 
ATOM   1902 C  CB    . PRO A 1 261 ? 23.061  -22.907 13.605  1.00 38.62  ? 233 PRO A CB    1 
ATOM   1903 C  CG    . PRO A 1 261 ? 22.838  -21.858 14.611  1.00 40.16  ? 233 PRO A CG    1 
ATOM   1904 C  CD    . PRO A 1 261 ? 22.815  -20.563 13.882  1.00 40.91  ? 233 PRO A CD    1 
ATOM   1905 N  N     . GLU A 1 262 ? 24.216  -23.865 10.785  1.00 36.19  ? 234 GLU A N     1 
ATOM   1906 C  CA    . GLU A 1 262 ? 23.837  -24.629 9.605   1.00 39.01  ? 234 GLU A CA    1 
ATOM   1907 C  C     . GLU A 1 262 ? 22.335  -24.911 9.571   1.00 36.31  ? 234 GLU A C     1 
ATOM   1908 O  O     . GLU A 1 262 ? 21.763  -25.381 10.551  1.00 40.27  ? 234 GLU A O     1 
ATOM   1909 C  CB    . GLU A 1 262 ? 24.606  -25.949 9.625   1.00 44.83  ? 234 GLU A CB    1 
ATOM   1910 C  CG    . GLU A 1 262 ? 25.286  -26.322 8.371   1.00 49.61  ? 234 GLU A CG    1 
ATOM   1911 C  CD    . GLU A 1 262 ? 25.973  -27.664 8.527   1.00 66.47  ? 234 GLU A CD    1 
ATOM   1912 O  OE1   . GLU A 1 262 ? 26.994  -27.713 9.235   1.00 62.57  ? 234 GLU A OE1   1 
ATOM   1913 O  OE2   . GLU A 1 262 ? 25.469  -28.667 7.981   1.00 73.05  ? 234 GLU A OE2   1 
ATOM   1914 N  N     . GLY A 1 263 ? 21.702  -24.609 8.439   1.00 37.13  ? 235 GLY A N     1 
ATOM   1915 C  CA    . GLY A 1 263 ? 20.274  -24.842 8.256   1.00 39.12  ? 235 GLY A CA    1 
ATOM   1916 C  C     . GLY A 1 263 ? 19.336  -23.844 8.919   1.00 37.83  ? 235 GLY A C     1 
ATOM   1917 O  O     . GLY A 1 263 ? 18.118  -24.044 8.872   1.00 38.72  ? 235 GLY A O     1 
ATOM   1918 N  N     . SER A 1 264 ? 19.855  -22.770 9.511   1.00 37.24  ? 236 SER A N     1 
ATOM   1919 C  CA    . SER A 1 264 ? 19.005  -21.826 10.238  1.00 34.60  ? 236 SER A CA    1 
ATOM   1920 C  C     . SER A 1 264 ? 18.189  -20.976 9.265   1.00 34.18  ? 236 SER A C     1 
ATOM   1921 O  O     . SER A 1 264 ? 18.719  -20.507 8.259   1.00 32.71  ? 236 SER A O     1 
ATOM   1922 C  CB    . SER A 1 264 ? 19.871  -20.916 11.118  1.00 34.17  ? 236 SER A CB    1 
ATOM   1923 O  OG    . SER A 1 264 ? 19.130  -19.835 11.683  1.00 35.56  ? 236 SER A OG    1 
ATOM   1924 N  N     . PRO A 1 265 ? 16.901  -20.747 9.542   1.00 34.20  ? 237 PRO A N     1 
ATOM   1925 C  CA    . PRO A 1 265 ? 16.137  -19.803 8.712   1.00 34.68  ? 237 PRO A CA    1 
ATOM   1926 C  C     . PRO A 1 265 ? 16.686  -18.386 8.763   1.00 32.07  ? 237 PRO A C     1 
ATOM   1927 O  O     . PRO A 1 265 ? 16.407  -17.612 7.840   1.00 33.51  ? 237 PRO A O     1 
ATOM   1928 C  CB    . PRO A 1 265 ? 14.712  -19.873 9.299   1.00 37.62  ? 237 PRO A CB    1 
ATOM   1929 C  CG    . PRO A 1 265 ? 14.703  -21.082 10.173  1.00 46.94  ? 237 PRO A CG    1 
ATOM   1930 C  CD    . PRO A 1 265 ? 16.104  -21.264 10.666  1.00 36.19  ? 237 PRO A CD    1 
ATOM   1931 N  N     . LEU A 1 266 ? 17.472  -18.024 9.786   1.00 31.71  ? 238 LEU A N     1 
ATOM   1932 C  CA    . LEU A 1 266 ? 18.037  -16.681 9.833   1.00 32.00  ? 238 LEU A CA    1 
ATOM   1933 C  C     . LEU A 1 266 ? 18.983  -16.410 8.669   1.00 34.55  ? 238 LEU A C     1 
ATOM   1934 O  O     . LEU A 1 266 ? 19.251  -15.243 8.376   1.00 32.64  ? 238 LEU A O     1 
ATOM   1935 C  CB    . LEU A 1 266 ? 18.785  -16.445 11.146  1.00 28.97  ? 238 LEU A CB    1 
ATOM   1936 C  CG    . LEU A 1 266 ? 17.935  -16.483 12.433  1.00 37.96  ? 238 LEU A CG    1 
ATOM   1937 C  CD1   . LEU A 1 266 ? 18.783  -16.334 13.672  1.00 42.25  ? 238 LEU A CD1   1 
ATOM   1938 C  CD2   . LEU A 1 266 ? 16.873  -15.381 12.384  1.00 39.21  ? 238 LEU A CD2   1 
ATOM   1939 N  N     . ARG A 1 267 ? 19.496  -17.454 7.996   1.00 29.60  ? 239 ARG A N     1 
ATOM   1940 C  CA    . ARG A 1 267 ? 20.387  -17.244 6.849   1.00 31.88  ? 239 ARG A CA    1 
ATOM   1941 C  C     . ARG A 1 267 ? 19.691  -16.562 5.662   1.00 30.70  ? 239 ARG A C     1 
ATOM   1942 O  O     . ARG A 1 267 ? 20.380  -15.959 4.813   1.00 32.51  ? 239 ARG A O     1 
ATOM   1943 C  CB    . ARG A 1 267 ? 20.998  -18.602 6.412   1.00 34.04  ? 239 ARG A CB    1 
ATOM   1944 C  CG    . ARG A 1 267 ? 21.926  -18.574 5.174   1.00 31.41  ? 239 ARG A CG    1 
ATOM   1945 C  CD    . ARG A 1 267 ? 23.027  -19.716 5.295   1.00 28.40  ? 239 ARG A CD    1 
ATOM   1946 N  NE    . ARG A 1 267 ? 23.998  -19.336 6.307   1.00 30.92  ? 239 ARG A NE    1 
ATOM   1947 C  CZ    . ARG A 1 267 ? 24.076  -19.856 7.525   1.00 33.02  ? 239 ARG A CZ    1 
ATOM   1948 N  NH1   . ARG A 1 267 ? 23.440  -20.979 7.849   1.00 34.47  ? 239 ARG A NH1   1 
ATOM   1949 N  NH2   . ARG A 1 267 ? 24.766  -19.210 8.450   1.00 31.62  ? 239 ARG A NH2   1 
ATOM   1950 N  N     . VAL A 1 268 ? 18.355  -16.596 5.592   1.00 29.36  ? 240 VAL A N     1 
ATOM   1951 C  CA    . VAL A 1 268 ? 17.672  -15.962 4.468   1.00 31.16  ? 240 VAL A CA    1 
ATOM   1952 C  C     . VAL A 1 268 ? 16.762  -14.816 4.931   1.00 32.81  ? 240 VAL A C     1 
ATOM   1953 O  O     . VAL A 1 268 ? 15.753  -14.516 4.275   1.00 35.45  ? 240 VAL A O     1 
ATOM   1954 C  CB    . VAL A 1 268 ? 16.881  -16.993 3.626   1.00 31.61  ? 240 VAL A CB    1 
ATOM   1955 C  CG1   . VAL A 1 268 ? 17.851  -17.905 2.859   1.00 35.77  ? 240 VAL A CG1   1 
ATOM   1956 C  CG2   . VAL A 1 268 ? 15.857  -17.790 4.473   1.00 33.04  ? 240 VAL A CG2   1 
ATOM   1957 N  N     . LEU A 1 269 ? 17.138  -14.143 6.031   1.00 31.00  ? 241 LEU A N     1 
ATOM   1958 C  CA    . LEU A 1 269 ? 16.431  -12.947 6.515   1.00 33.48  ? 241 LEU A CA    1 
ATOM   1959 C  C     . LEU A 1 269 ? 17.042  -11.710 5.857   1.00 31.65  ? 241 LEU A C     1 
ATOM   1960 O  O     . LEU A 1 269 ? 18.193  -11.370 6.115   1.00 30.26  ? 241 LEU A O     1 
ATOM   1961 C  CB    . LEU A 1 269 ? 16.520  -12.843 8.041   1.00 32.65  ? 241 LEU A CB    1 
ATOM   1962 C  CG    . LEU A 1 269 ? 15.988  -11.576 8.734   1.00 36.74  ? 241 LEU A CG    1 
ATOM   1963 C  CD1   . LEU A 1 269 ? 14.502  -11.347 8.410   1.00 34.94  ? 241 LEU A CD1   1 
ATOM   1964 C  CD2   . LEU A 1 269 ? 16.203  -11.649 10.261  1.00 34.95  ? 241 LEU A CD2   1 
ATOM   1965 N  N     . TYR A 1 270 ? 16.266  -11.039 5.002   1.00 30.50  ? 242 TYR A N     1 
ATOM   1966 C  CA    . TYR A 1 270 ? 16.669  -9.823  4.311   1.00 29.17  ? 242 TYR A CA    1 
ATOM   1967 C  C     . TYR A 1 270 ? 15.623  -8.743  4.583   1.00 26.04  ? 242 TYR A C     1 
ATOM   1968 O  O     . TYR A 1 270 ? 14.451  -9.050  4.828   1.00 31.77  ? 242 TYR A O     1 
ATOM   1969 C  CB    . TYR A 1 270 ? 16.776  -10.031 2.790   1.00 28.58  ? 242 TYR A CB    1 
ATOM   1970 C  CG    . TYR A 1 270 ? 17.917  -10.974 2.365   1.00 28.83  ? 242 TYR A CG    1 
ATOM   1971 C  CD1   . TYR A 1 270 ? 17.717  -12.345 2.304   1.00 35.85  ? 242 TYR A CD1   1 
ATOM   1972 C  CD2   . TYR A 1 270 ? 19.161  -10.469 2.003   1.00 35.29  ? 242 TYR A CD2   1 
ATOM   1973 C  CE1   . TYR A 1 270 ? 18.758  -13.203 1.926   1.00 32.10  ? 242 TYR A CE1   1 
ATOM   1974 C  CE2   . TYR A 1 270 ? 20.216  -11.326 1.612   1.00 33.37  ? 242 TYR A CE2   1 
ATOM   1975 C  CZ    . TYR A 1 270 ? 19.982  -12.685 1.569   1.00 35.28  ? 242 TYR A CZ    1 
ATOM   1976 O  OH    . TYR A 1 270 ? 21.001  -13.546 1.198   1.00 40.39  ? 242 TYR A OH    1 
ATOM   1977 N  N     . SER A 1 271 ? 16.046  -7.476  4.490   1.00 33.91  ? 243 SER A N     1 
ATOM   1978 C  CA    . SER A 1 271 ? 15.147  -6.339  4.738   1.00 29.51  ? 243 SER A CA    1 
ATOM   1979 C  C     . SER A 1 271 ? 15.260  -5.273  3.653   1.00 33.25  ? 243 SER A C     1 
ATOM   1980 O  O     . SER A 1 271 ? 16.322  -5.095  3.040   1.00 30.89  ? 243 SER A O     1 
ATOM   1981 C  CB    . SER A 1 271 ? 15.448  -5.689  6.100   1.00 33.17  ? 243 SER A CB    1 
ATOM   1982 O  OG    . SER A 1 271 ? 14.449  -4.761  6.494   1.00 37.95  ? 243 SER A OG    1 
ATOM   1983 N  N     . GLY A 1 272 ? 14.144  -4.561  3.428   1.00 28.21  ? 244 GLY A N     1 
ATOM   1984 C  CA    . GLY A 1 272 ? 14.135  -3.338  2.632   1.00 27.03  ? 244 GLY A CA    1 
ATOM   1985 C  C     . GLY A 1 272 ? 13.811  -2.176  3.563   1.00 32.07  ? 244 GLY A C     1 
ATOM   1986 O  O     . GLY A 1 272 ? 13.065  -2.340  4.526   1.00 31.24  ? 244 GLY A O     1 
ATOM   1987 N  N     . ILE A 1 273 ? 14.398  -1.005  3.311   1.00 26.16  ? 245 ILE A N     1 
ATOM   1988 C  CA    . ILE A 1 273 ? 14.198  0.167   4.176   1.00 25.31  ? 245 ILE A CA    1 
ATOM   1989 C  C     . ILE A 1 273 ? 13.894  1.379   3.309   1.00 25.75  ? 245 ILE A C     1 
ATOM   1990 O  O     . ILE A 1 273 ? 14.625  1.648   2.351   1.00 28.17  ? 245 ILE A O     1 
ATOM   1991 C  CB    . ILE A 1 273 ? 15.452  0.454   5.025   1.00 28.19  ? 245 ILE A CB    1 
ATOM   1992 C  CG1   . ILE A 1 273 ? 15.880  -0.785  5.821   1.00 30.07  ? 245 ILE A CG1   1 
ATOM   1993 C  CG2   . ILE A 1 273 ? 15.244  1.686   5.945   1.00 31.90  ? 245 ILE A CG2   1 
ATOM   1994 C  CD1   . ILE A 1 273 ? 17.210  -0.598  6.525   1.00 38.20  ? 245 ILE A CD1   1 
ATOM   1995 N  N     . GLY A 1 274 ? 12.887  2.160   3.689   1.00 26.02  ? 246 GLY A N     1 
ATOM   1996 C  CA    . GLY A 1 274 ? 12.610  3.423   3.006   1.00 25.73  ? 246 GLY A CA    1 
ATOM   1997 C  C     . GLY A 1 274 ? 12.428  4.553   3.999   1.00 28.79  ? 246 GLY A C     1 
ATOM   1998 O  O     . GLY A 1 274 ? 11.906  4.347   5.091   1.00 30.10  ? 246 GLY A O     1 
ATOM   1999 N  N     . LEU A 1 275 ? 12.910  5.750   3.626   1.00 28.71  ? 247 LEU A N     1 
ATOM   2000 C  CA    . LEU A 1 275 ? 12.774  6.944   4.470   1.00 24.93  ? 247 LEU A CA    1 
ATOM   2001 C  C     . LEU A 1 275 ? 12.072  8.045   3.694   1.00 29.24  ? 247 LEU A C     1 
ATOM   2002 O  O     . LEU A 1 275 ? 12.353  8.253   2.507   1.00 28.07  ? 247 LEU A O     1 
ATOM   2003 C  CB    . LEU A 1 275 ? 14.145  7.491   4.938   1.00 26.43  ? 247 LEU A CB    1 
ATOM   2004 C  CG    . LEU A 1 275 ? 15.183  6.503   5.464   1.00 31.74  ? 247 LEU A CG    1 
ATOM   2005 C  CD1   . LEU A 1 275 ? 16.537  7.214   5.647   1.00 34.90  ? 247 LEU A CD1   1 
ATOM   2006 C  CD2   . LEU A 1 275 ? 14.682  5.984   6.789   1.00 35.01  ? 247 LEU A CD2   1 
ATOM   2007 N  N     . ALA A 1 276 ? 11.193  8.784   4.382   1.00 27.48  ? 248 ALA A N     1 
ATOM   2008 C  CA    . ALA A 1 276 ? 10.496  9.911   3.774   1.00 29.69  ? 248 ALA A CA    1 
ATOM   2009 C  C     . ALA A 1 276 ? 10.329  10.989  4.839   1.00 34.86  ? 248 ALA A C     1 
ATOM   2010 O  O     . ALA A 1 276 ? 10.666  10.790  6.008   1.00 36.64  ? 248 ALA A O     1 
ATOM   2011 C  CB    . ALA A 1 276 ? 9.129   9.484   3.214   1.00 30.71  ? 248 ALA A CB    1 
ATOM   2012 N  N     . LYS A 1 277 ? 9.819   12.145  4.433   1.00 31.86  ? 249 LYS A N     1 
ATOM   2013 C  CA    . LYS A 1 277 ? 9.515   13.208  5.378   1.00 31.60  ? 249 LYS A CA    1 
ATOM   2014 C  C     . LYS A 1 277 ? 7.999   13.360  5.443   1.00 36.16  ? 249 LYS A C     1 
ATOM   2015 O  O     . LYS A 1 277 ? 7.308   13.200  4.431   1.00 39.15  ? 249 LYS A O     1 
ATOM   2016 C  CB    . LYS A 1 277 ? 10.184  14.519  4.952   1.00 38.24  ? 249 LYS A CB    1 
ATOM   2017 C  CG    . LYS A 1 277 ? 10.745  15.342  6.096   1.00 53.22  ? 249 LYS A CG    1 
ATOM   2018 C  CD    . LYS A 1 277 ? 11.826  16.309  5.636   1.00 51.77  ? 249 LYS A CD    1 
ATOM   2019 C  CE    . LYS A 1 277 ? 12.327  17.140  6.810   1.00 57.71  ? 249 LYS A CE    1 
ATOM   2020 N  NZ    . LYS A 1 277 ? 13.180  18.280  6.395   1.00 55.00  ? 249 LYS A NZ    1 
ATOM   2021 N  N     . GLY A 1 278 ? 7.468   13.622  6.635   1.00 33.34  ? 250 GLY A N     1 
ATOM   2022 C  CA    . GLY A 1 278 ? 6.027   13.738  6.764   1.00 38.48  ? 250 GLY A CA    1 
ATOM   2023 C  C     . GLY A 1 278 ? 5.641   14.652  7.908   1.00 38.10  ? 250 GLY A C     1 
ATOM   2024 O  O     . GLY A 1 278 ? 6.431   14.904  8.825   1.00 40.92  ? 250 GLY A O     1 
ATOM   2025 N  N     . LYS A 1 279 ? 4.400   15.137  7.834   1.00 40.75  ? 251 LYS A N     1 
ATOM   2026 C  CA    . LYS A 1 279 ? 3.791   15.966  8.872   1.00 38.23  ? 251 LYS A CA    1 
ATOM   2027 C  C     . LYS A 1 279 ? 3.033   15.049  9.822   1.00 36.28  ? 251 LYS A C     1 
ATOM   2028 O  O     . LYS A 1 279 ? 2.030   14.441  9.441   1.00 43.01  ? 251 LYS A O     1 
ATOM   2029 C  CB    . LYS A 1 279 ? 2.817   16.975  8.265   1.00 48.38  ? 251 LYS A CB    1 
ATOM   2030 C  CG    . LYS A 1 279 ? 2.809   18.357  8.902   1.00 61.66  ? 251 LYS A CG    1 
ATOM   2031 C  CD    . LYS A 1 279 ? 4.199   18.907  9.102   1.00 65.51  ? 251 LYS A CD    1 
ATOM   2032 C  CE    . LYS A 1 279 ? 4.925   18.903  7.768   1.00 67.68  ? 251 LYS A CE    1 
ATOM   2033 N  NZ    . LYS A 1 279 ? 4.418   19.961  6.854   1.00 75.83  ? 251 LYS A NZ    1 
ATOM   2034 N  N     . VAL A 1 280 ? 3.481   14.980  11.062  1.00 36.13  ? 252 VAL A N     1 
ATOM   2035 C  CA    . VAL A 1 280 ? 2.884   14.113  12.068  1.00 30.59  ? 252 VAL A CA    1 
ATOM   2036 C  C     . VAL A 1 280 ? 2.079   14.979  13.038  1.00 34.65  ? 252 VAL A C     1 
ATOM   2037 O  O     . VAL A 1 280 ? 2.501   16.088  13.373  1.00 37.93  ? 252 VAL A O     1 
ATOM   2038 C  CB    . VAL A 1 280 ? 4.020   13.357  12.786  1.00 42.03  ? 252 VAL A CB    1 
ATOM   2039 C  CG1   . VAL A 1 280 ? 3.516   12.672  13.981  1.00 42.02  ? 252 VAL A CG1   1 
ATOM   2040 C  CG2   . VAL A 1 280 ? 4.719   12.374  11.820  1.00 36.97  ? 252 VAL A CG2   1 
ATOM   2041 N  N     . ILE A 1 281 ? 0.940   14.480  13.507  1.00 33.00  ? 253 ILE A N     1 
ATOM   2042 C  CA    . ILE A 1 281 ? 0.162   15.189  14.522  1.00 35.81  ? 253 ILE A CA    1 
ATOM   2043 C  C     . ILE A 1 281 ? 0.358   14.489  15.863  1.00 43.20  ? 253 ILE A C     1 
ATOM   2044 O  O     . ILE A 1 281 ? 0.145   13.278  15.977  1.00 39.08  ? 253 ILE A O     1 
ATOM   2045 C  CB    . ILE A 1 281 ? -1.321  15.271  14.130  1.00 39.40  ? 253 ILE A CB    1 
ATOM   2046 C  CG1   . ILE A 1 281 ? -1.472  16.183  12.902  1.00 37.28  ? 253 ILE A CG1   1 
ATOM   2047 C  CG2   . ILE A 1 281 ? -2.172  15.754  15.325  1.00 43.99  ? 253 ILE A CG2   1 
ATOM   2048 C  CD1   . ILE A 1 281 ? -2.907  16.246  12.339  1.00 49.15  ? 253 ILE A CD1   1 
ATOM   2049 N  N     . GLU A 1 282 ? 0.803   15.236  16.872  1.00 38.94  ? 254 GLU A N     1 
ATOM   2050 C  CA    . GLU A 1 282 ? 0.922   14.729  18.238  1.00 36.64  ? 254 GLU A CA    1 
ATOM   2051 C  C     . GLU A 1 282 ? -0.262  15.228  19.055  1.00 44.41  ? 254 GLU A C     1 
ATOM   2052 O  O     . GLU A 1 282 ? -0.628  16.406  18.960  1.00 45.40  ? 254 GLU A O     1 
ATOM   2053 C  CB    . GLU A 1 282 ? 2.238   15.180  18.884  1.00 46.79  ? 254 GLU A CB    1 
ATOM   2054 C  CG    . GLU A 1 282 ? 3.498   14.756  18.130  1.00 51.25  ? 254 GLU A CG    1 
ATOM   2055 C  CD    . GLU A 1 282 ? 4.774   15.276  18.771  1.00 58.48  ? 254 GLU A CD    1 
ATOM   2056 O  OE1   . GLU A 1 282 ? 4.703   16.258  19.541  1.00 64.66  ? 254 GLU A OE1   1 
ATOM   2057 O  OE2   . GLU A 1 282 ? 5.848   14.709  18.494  1.00 56.66  ? 254 GLU A OE2   1 
ATOM   2058 N  N     . GLY A 1 283 ? -0.876  14.336  19.828  1.00 40.71  ? 255 GLY A N     1 
ATOM   2059 C  CA    . GLY A 1 283 ? -1.993  14.737  20.664  1.00 45.02  ? 255 GLY A CA    1 
ATOM   2060 C  C     . GLY A 1 283 ? -2.677  13.546  21.313  1.00 40.38  ? 255 GLY A C     1 
ATOM   2061 O  O     . GLY A 1 283 ? -2.162  12.424  21.307  1.00 47.85  ? 255 GLY A O     1 
ATOM   2062 N  N     . ASN A 1 284 ? -3.854  13.826  21.884  1.00 42.24  ? 256 ASN A N     1 
ATOM   2063 C  CA    . ASN A 1 284 ? -4.709  12.816  22.509  1.00 39.31  ? 256 ASN A CA    1 
ATOM   2064 C  C     . ASN A 1 284 ? -5.673  12.293  21.445  1.00 39.28  ? 256 ASN A C     1 
ATOM   2065 O  O     . ASN A 1 284 ? -6.764  12.833  21.258  1.00 42.62  ? 256 ASN A O     1 
ATOM   2066 C  CB    . ASN A 1 284 ? -5.457  13.414  23.696  1.00 49.36  ? 256 ASN A CB    1 
ATOM   2067 C  CG    . ASN A 1 284 ? -6.284  12.389  24.449  1.00 55.36  ? 256 ASN A CG    1 
ATOM   2068 O  OD1   . ASN A 1 284 ? -6.002  11.192  24.406  1.00 58.48  ? 256 ASN A OD1   1 
ATOM   2069 N  ND2   . ASN A 1 284 ? -7.301  12.858  25.158  1.00 60.51  ? 256 ASN A ND2   1 
ATOM   2070 N  N     . ILE A 1 285 ? -5.260  11.228  20.746  1.00 39.25  ? 257 ILE A N     1 
ATOM   2071 C  CA    . ILE A 1 285 ? -5.967  10.695  19.577  1.00 37.16  ? 257 ILE A CA    1 
ATOM   2072 C  C     . ILE A 1 285 ? -6.708  9.414   19.935  1.00 38.55  ? 257 ILE A C     1 
ATOM   2073 O  O     . ILE A 1 285 ? -6.148  8.525   20.588  1.00 42.69  ? 257 ILE A O     1 
ATOM   2074 C  CB    . ILE A 1 285 ? -4.984  10.419  18.418  1.00 38.95  ? 257 ILE A CB    1 
ATOM   2075 C  CG1   . ILE A 1 285 ? -4.078  11.638  18.154  1.00 46.13  ? 257 ILE A CG1   1 
ATOM   2076 C  CG2   . ILE A 1 285 ? -5.743  10.011  17.171  1.00 41.17  ? 257 ILE A CG2   1 
ATOM   2077 C  CD1   . ILE A 1 285 ? -4.779  12.792  17.552  1.00 50.26  ? 257 ILE A CD1   1 
ATOM   2078 N  N     . GLY A 1 286 ? -7.956  9.290   19.464  1.00 38.99  ? 258 GLY A N     1 
ATOM   2079 C  CA    . GLY A 1 286 ? -8.664  8.029   19.594  1.00 37.13  ? 258 GLY A CA    1 
ATOM   2080 C  C     . GLY A 1 286 ? -10.063 8.110   20.168  1.00 45.06  ? 258 GLY A C     1 
ATOM   2081 O  O     . GLY A 1 286 ? -10.761 9.117   19.997  1.00 42.51  ? 258 GLY A O     1 
ATOM   2082 N  N     . SER A 1 287 ? -10.487 7.045   20.855  1.00 46.81  ? 259 SER A N     1 
ATOM   2083 C  CA    . SER A 1 287 ? -11.807 6.969   21.469  1.00 51.85  ? 259 SER A CA    1 
ATOM   2084 C  C     . SER A 1 287 ? -11.668 6.644   22.950  1.00 50.67  ? 259 SER A C     1 
ATOM   2085 O  O     . SER A 1 287 ? -10.570 6.424   23.465  1.00 45.13  ? 259 SER A O     1 
ATOM   2086 C  CB    . SER A 1 287 ? -12.673 5.899   20.793  1.00 48.21  ? 259 SER A CB    1 
ATOM   2087 O  OG    . SER A 1 287 ? -12.035 4.629   20.864  1.00 55.63  ? 259 SER A OG    1 
ATOM   2088 N  N     . GLU A 1 288 ? -12.812 6.559   23.635  1.00 57.97  ? 260 GLU A N     1 
ATOM   2089 C  CA    . GLU A 1 288 ? -12.790 6.113   25.025  1.00 55.09  ? 260 GLU A CA    1 
ATOM   2090 C  C     . GLU A 1 288 ? -12.212 4.707   25.145  1.00 54.63  ? 260 GLU A C     1 
ATOM   2091 O  O     . GLU A 1 288 ? -11.650 4.353   26.187  1.00 55.97  ? 260 GLU A O     1 
ATOM   2092 C  CB    . GLU A 1 288 ? -14.202 6.165   25.618  1.00 65.64  ? 260 GLU A CB    1 
ATOM   2093 N  N     . LEU A 1 289 ? -12.310 3.906   24.084  1.00 48.63  ? 261 LEU A N     1 
ATOM   2094 C  CA    . LEU A 1 289 ? -11.836 2.528   24.149  1.00 47.85  ? 261 LEU A CA    1 
ATOM   2095 C  C     . LEU A 1 289 ? -10.326 2.415   23.945  1.00 51.57  ? 261 LEU A C     1 
ATOM   2096 O  O     . LEU A 1 289 ? -9.687  1.548   24.547  1.00 53.88  ? 261 LEU A O     1 
ATOM   2097 C  CB    . LEU A 1 289 ? -12.575 1.676   23.116  1.00 57.49  ? 261 LEU A CB    1 
ATOM   2098 N  N     . LYS A 1 290 ? -9.729  3.264   23.111  1.00 42.50  ? 262 LYS A N     1 
ATOM   2099 C  CA    . LYS A 1 290 ? -8.326  3.089   22.756  1.00 42.22  ? 262 LYS A CA    1 
ATOM   2100 C  C     . LYS A 1 290 ? -7.726  4.428   22.356  1.00 39.45  ? 262 LYS A C     1 
ATOM   2101 O  O     . LYS A 1 290 ? -8.328  5.150   21.559  1.00 38.93  ? 262 LYS A O     1 
ATOM   2102 C  CB    . LYS A 1 290 ? -8.175  2.097   21.597  1.00 48.28  ? 262 LYS A CB    1 
ATOM   2103 C  CG    . LYS A 1 290 ? -6.735  1.750   21.319  1.00 56.45  ? 262 LYS A CG    1 
ATOM   2104 C  CD    . LYS A 1 290 ? -6.549  0.914   20.067  1.00 63.53  ? 262 LYS A CD    1 
ATOM   2105 C  CE    . LYS A 1 290 ? -5.081  0.490   19.975  1.00 67.95  ? 262 LYS A CE    1 
ATOM   2106 N  NZ    . LYS A 1 290 ? -4.304  0.962   21.179  1.00 70.14  ? 262 LYS A NZ    1 
ATOM   2107 N  N     . ARG A 1 291 ? -6.553  4.749   22.896  1.00 37.61  ? 263 ARG A N     1 
ATOM   2108 C  CA    . ARG A 1 291 ? -5.885  6.010   22.605  1.00 42.20  ? 263 ARG A CA    1 
ATOM   2109 C  C     . ARG A 1 291 ? -4.524  5.767   21.961  1.00 40.49  ? 263 ARG A C     1 
ATOM   2110 O  O     . ARG A 1 291 ? -3.923  4.707   22.107  1.00 43.70  ? 263 ARG A O     1 
ATOM   2111 C  CB    . ARG A 1 291 ? -5.699  6.864   23.876  1.00 46.76  ? 263 ARG A CB    1 
ATOM   2112 C  CG    . ARG A 1 291 ? -7.006  7.275   24.543  1.00 47.59  ? 263 ARG A CG    1 
ATOM   2113 C  CD    . ARG A 1 291 ? -7.650  8.448   23.819  1.00 49.05  ? 263 ARG A CD    1 
ATOM   2114 N  NE    . ARG A 1 291 ? -8.886  8.883   24.460  1.00 59.86  ? 263 ARG A NE    1 
ATOM   2115 C  CZ    . ARG A 1 291 ? -9.649  9.877   24.022  1.00 61.97  ? 263 ARG A CZ    1 
ATOM   2116 N  NH1   . ARG A 1 291 ? -9.330  10.573  22.940  1.00 58.00  ? 263 ARG A NH1   1 
ATOM   2117 N  NH2   . ARG A 1 291 ? -10.765 10.179  24.681  1.00 65.79  ? 263 ARG A NH2   1 
ATOM   2118 N  N     . ASP A 1 292 ? -4.059  6.785   21.239  1.00 37.30  ? 264 ASP A N     1 
ATOM   2119 C  CA    A ASP A 1 292 ? -2.745  6.828   20.607  0.64 41.46  ? 264 ASP A CA    1 
ATOM   2120 C  CA    B ASP A 1 292 ? -2.721  6.810   20.675  0.36 41.45  ? 264 ASP A CA    1 
ATOM   2121 C  C     . ASP A 1 292 ? -2.166  8.215   20.846  1.00 37.90  ? 264 ASP A C     1 
ATOM   2122 O  O     . ASP A 1 292 ? -2.894  9.165   21.129  1.00 39.49  ? 264 ASP A O     1 
ATOM   2123 C  CB    A ASP A 1 292 ? -2.822  6.552   19.092  0.64 43.78  ? 264 ASP A CB    1 
ATOM   2124 C  CB    B ASP A 1 292 ? -2.713  6.397   19.197  0.36 43.59  ? 264 ASP A CB    1 
ATOM   2125 C  CG    A ASP A 1 292 ? -1.634  5.768   18.564  0.64 44.33  ? 264 ASP A CG    1 
ATOM   2126 C  CG    B ASP A 1 292 ? -2.553  4.906   19.015  0.36 42.19  ? 264 ASP A CG    1 
ATOM   2127 O  OD1   A ASP A 1 292 ? -0.520  5.901   19.113  0.64 46.21  ? 264 ASP A OD1   1 
ATOM   2128 O  OD1   B ASP A 1 292 ? -1.994  4.257   19.921  0.36 54.52  ? 264 ASP A OD1   1 
ATOM   2129 O  OD2   A ASP A 1 292 ? -1.804  5.040   17.559  0.64 43.23  ? 264 ASP A OD2   1 
ATOM   2130 O  OD2   B ASP A 1 292 ? -2.987  4.379   17.970  0.36 49.13  ? 264 ASP A OD2   1 
ATOM   2131 N  N     . TYR A 1 293 ? -0.853  8.334   20.719  1.00 37.58  ? 265 TYR A N     1 
ATOM   2132 C  CA    . TYR A 1 293 ? -0.218  9.627   20.946  1.00 40.91  ? 265 TYR A CA    1 
ATOM   2133 C  C     . TYR A 1 293 ? 0.090   10.385  19.657  1.00 45.45  ? 265 TYR A C     1 
ATOM   2134 O  O     . TYR A 1 293 ? 0.232   11.611  19.687  1.00 42.14  ? 265 TYR A O     1 
ATOM   2135 C  CB    . TYR A 1 293 ? 1.072   9.421   21.768  1.00 41.19  ? 265 TYR A CB    1 
ATOM   2136 C  CG    . TYR A 1 293 ? 1.966   10.627  21.864  1.00 52.59  ? 265 TYR A CG    1 
ATOM   2137 C  CD1   . TYR A 1 293 ? 1.517   11.820  22.417  1.00 54.75  ? 265 TYR A CD1   1 
ATOM   2138 C  CD2   . TYR A 1 293 ? 3.266   10.578  21.375  1.00 53.71  ? 265 TYR A CD2   1 
ATOM   2139 C  CE1   . TYR A 1 293 ? 2.349   12.935  22.485  1.00 64.96  ? 265 TYR A CE1   1 
ATOM   2140 C  CE2   . TYR A 1 293 ? 4.100   11.680  21.445  1.00 59.66  ? 265 TYR A CE2   1 
ATOM   2141 C  CZ    . TYR A 1 293 ? 3.638   12.857  21.997  1.00 58.47  ? 265 TYR A CZ    1 
ATOM   2142 O  OH    . TYR A 1 293 ? 4.470   13.957  22.060  1.00 65.24  ? 265 TYR A OH    1 
ATOM   2143 N  N     . THR A 1 294 ? 0.121   9.703   18.519  1.00 36.90  ? 266 THR A N     1 
ATOM   2144 C  CA    A THR A 1 294 ? 0.553   10.338  17.288  0.50 35.74  ? 266 THR A CA    1 
ATOM   2145 C  CA    B THR A 1 294 ? 0.621   10.284  17.282  0.50 35.78  ? 266 THR A CA    1 
ATOM   2146 C  C     . THR A 1 294 ? -0.189  9.727   16.111  1.00 40.76  ? 266 THR A C     1 
ATOM   2147 O  O     . THR A 1 294 ? -0.605  8.566   16.148  1.00 44.44  ? 266 THR A O     1 
ATOM   2148 C  CB    A THR A 1 294 ? 2.064   10.188  17.103  0.50 39.41  ? 266 THR A CB    1 
ATOM   2149 C  CB    B THR A 1 294 ? 2.117   9.935   17.144  0.50 39.16  ? 266 THR A CB    1 
ATOM   2150 O  OG1   A THR A 1 294 ? 2.478   11.016  16.027  0.50 43.24  ? 266 THR A OG1   1 
ATOM   2151 O  OG1   B THR A 1 294 ? 2.944   10.923  17.793  0.50 38.53  ? 266 THR A OG1   1 
ATOM   2152 C  CG2   A THR A 1 294 ? 2.437   8.754   16.802  0.50 30.81  ? 266 THR A CG2   1 
ATOM   2153 C  CG2   B THR A 1 294 ? 2.480   9.816   15.737  0.50 42.75  ? 266 THR A CG2   1 
ATOM   2154 N  N     . ILE A 1 295 ? -0.382  10.532  15.056  1.00 35.31  ? 267 ILE A N     1 
ATOM   2155 C  CA    . ILE A 1 295 ? -0.964  10.010  13.812  1.00 38.53  ? 267 ILE A CA    1 
ATOM   2156 C  C     . ILE A 1 295 ? -0.239  10.580  12.591  1.00 37.97  ? 267 ILE A C     1 
ATOM   2157 O  O     . ILE A 1 295 ? 0.022   11.786  12.513  1.00 35.37  ? 267 ILE A O     1 
ATOM   2158 C  CB    . ILE A 1 295 ? -2.489  10.278  13.741  1.00 39.06  ? 267 ILE A CB    1 
ATOM   2159 C  CG1   . ILE A 1 295 ? -3.079  9.715   12.452  1.00 44.16  ? 267 ILE A CG1   1 
ATOM   2160 C  CG2   . ILE A 1 295 ? -2.834  11.758  13.868  1.00 39.98  ? 267 ILE A CG2   1 
ATOM   2161 C  CD1   . ILE A 1 295 ? -4.508  10.122  12.257  1.00 48.45  ? 267 ILE A CD1   1 
ATOM   2162 N  N     . LEU A 1 296 ? 0.091   9.702   11.625  1.00 33.23  ? 268 LEU A N     1 
ATOM   2163 C  CA    . LEU A 1 296 ? 0.628   10.104  10.316  1.00 32.08  ? 268 LEU A CA    1 
ATOM   2164 C  C     . LEU A 1 296 ? -0.415  9.725   9.272   1.00 36.71  ? 268 LEU A C     1 
ATOM   2165 O  O     . LEU A 1 296 ? -0.593  8.541   8.984   1.00 31.38  ? 268 LEU A O     1 
ATOM   2166 C  CB    . LEU A 1 296 ? 1.959   9.410   10.004  1.00 31.56  ? 268 LEU A CB    1 
ATOM   2167 C  CG    . LEU A 1 296 ? 2.468   9.612   8.578   1.00 31.75  ? 268 LEU A CG    1 
ATOM   2168 C  CD1   . LEU A 1 296 ? 2.915   11.070  8.364   1.00 36.26  ? 268 LEU A CD1   1 
ATOM   2169 C  CD2   . LEU A 1 296 ? 3.646   8.663   8.278   1.00 37.40  ? 268 LEU A CD2   1 
ATOM   2170 N  N     . GLY A 1 297 ? -1.104  10.715  8.708   1.00 34.25  ? 269 GLY A N     1 
ATOM   2171 C  CA    . GLY A 1 297 ? -2.163  10.401  7.757   1.00 37.90  ? 269 GLY A CA    1 
ATOM   2172 C  C     . GLY A 1 297 ? -1.613  9.686   6.532   1.00 33.63  ? 269 GLY A C     1 
ATOM   2173 O  O     . GLY A 1 297 ? -0.510  9.968   6.072   1.00 32.07  ? 269 GLY A O     1 
ATOM   2174 N  N     . ASP A 1 298 ? -2.375  8.713   6.027   1.00 33.21  ? 270 ASP A N     1 
ATOM   2175 C  CA    . ASP A 1 298 ? -1.962  7.905   4.862   1.00 32.87  ? 270 ASP A CA    1 
ATOM   2176 C  C     . ASP A 1 298 ? -0.627  7.177   5.060   1.00 33.97  ? 270 ASP A C     1 
ATOM   2177 O  O     . ASP A 1 298 ? 0.098   6.932   4.085   1.00 35.04  ? 270 ASP A O     1 
ATOM   2178 C  CB    . ASP A 1 298 ? -1.898  8.755   3.589   1.00 35.44  ? 270 ASP A CB    1 
ATOM   2179 C  CG    . ASP A 1 298 ? -3.268  9.232   3.158   1.00 48.47  ? 270 ASP A CG    1 
ATOM   2180 O  OD1   . ASP A 1 298 ? -4.240  8.463   3.325   1.00 45.58  ? 270 ASP A OD1   1 
ATOM   2181 O  OD2   . ASP A 1 298 ? -3.369  10.362  2.657   1.00 43.54  ? 270 ASP A OD2   1 
ATOM   2182 N  N     . ALA A 1 299 ? -0.300  6.790   6.305   1.00 30.30  ? 271 ALA A N     1 
ATOM   2183 C  CA    . ALA A 1 299 ? 0.916   6.010   6.546   1.00 33.51  ? 271 ALA A CA    1 
ATOM   2184 C  C     . ALA A 1 299 ? 0.905   4.710   5.745   1.00 28.51  ? 271 ALA A C     1 
ATOM   2185 O  O     . ALA A 1 299 ? 1.953   4.260   5.261   1.00 31.15  ? 271 ALA A O     1 
ATOM   2186 C  CB    . ALA A 1 299 ? 1.062   5.716   8.048   1.00 31.58  ? 271 ALA A CB    1 
ATOM   2187 N  N     . VAL A 1 300 ? -0.277  4.103   5.593   1.00 28.42  ? 272 VAL A N     1 
ATOM   2188 C  CA    . VAL A 1 300 ? -0.418  2.839   4.858   1.00 29.47  ? 272 VAL A CA    1 
ATOM   2189 C  C     . VAL A 1 300 ? 0.078   3.002   3.430   1.00 33.14  ? 272 VAL A C     1 
ATOM   2190 O  O     . VAL A 1 300 ? 0.787   2.140   2.887   1.00 32.40  ? 272 VAL A O     1 
ATOM   2191 C  CB    . VAL A 1 300 ? -1.903  2.399   4.895   1.00 36.45  ? 272 VAL A CB    1 
ATOM   2192 C  CG1   . VAL A 1 300 ? -2.284  1.566   3.688   1.00 44.64  ? 272 VAL A CG1   1 
ATOM   2193 C  CG2   . VAL A 1 300 ? -2.192  1.665   6.187   1.00 50.75  ? 272 VAL A CG2   1 
ATOM   2194 N  N     . ASN A 1 301 ? -0.295  4.112   2.800   1.00 30.65  ? 273 ASN A N     1 
ATOM   2195 C  CA    . ASN A 1 301 ? 0.050   4.334   1.400   1.00 35.34  ? 273 ASN A CA    1 
ATOM   2196 C  C     . ASN A 1 301 ? 1.533   4.643   1.216   1.00 34.10  ? 273 ASN A C     1 
ATOM   2197 O  O     . ASN A 1 301 ? 2.143   4.199   0.236   1.00 33.75  ? 273 ASN A O     1 
ATOM   2198 C  CB    . ASN A 1 301 ? -0.820  5.461   0.857   1.00 35.60  ? 273 ASN A CB    1 
ATOM   2199 C  CG    . ASN A 1 301 ? -2.295  5.272   1.229   1.00 46.52  ? 273 ASN A CG    1 
ATOM   2200 O  OD1   . ASN A 1 301 ? -2.791  5.842   2.213   1.00 39.43  ? 273 ASN A OD1   1 
ATOM   2201 N  ND2   . ASN A 1 301 ? -2.990  4.441   0.457   1.00 42.75  ? 273 ASN A ND2   1 
ATOM   2202 N  N     . VAL A 1 302 ? 2.129   5.429   2.119   1.00 29.14  ? 274 VAL A N     1 
ATOM   2203 C  CA    . VAL A 1 302 ? 3.563   5.725   1.997   1.00 26.49  ? 274 VAL A CA    1 
ATOM   2204 C  C     . VAL A 1 302 ? 4.374   4.449   2.182   1.00 30.96  ? 274 VAL A C     1 
ATOM   2205 O  O     . VAL A 1 302 ? 5.330   4.179   1.439   1.00 33.22  ? 274 VAL A O     1 
ATOM   2206 C  CB    . VAL A 1 302 ? 3.974   6.811   3.014   1.00 31.43  ? 274 VAL A CB    1 
ATOM   2207 C  CG1   . VAL A 1 302 ? 5.471   7.103   2.923   1.00 35.76  ? 274 VAL A CG1   1 
ATOM   2208 C  CG2   . VAL A 1 302 ? 3.168   8.109   2.812   1.00 36.60  ? 274 VAL A CG2   1 
ATOM   2209 N  N     . ALA A 1 303 ? 3.981   3.617   3.147   1.00 28.23  ? 275 ALA A N     1 
ATOM   2210 C  CA    . ALA A 1 303 ? 4.746   2.397   3.405   1.00 29.44  ? 275 ALA A CA    1 
ATOM   2211 C  C     . ALA A 1 303 ? 4.670   1.440   2.220   1.00 31.11  ? 275 ALA A C     1 
ATOM   2212 O  O     . ALA A 1 303 ? 5.675   0.829   1.835   1.00 30.76  ? 275 ALA A O     1 
ATOM   2213 C  CB    . ALA A 1 303 ? 4.220   1.705   4.674   1.00 29.32  ? 275 ALA A CB    1 
ATOM   2214 N  N     . ALA A 1 304 ? 3.476   1.286   1.636   1.00 30.26  ? 276 ALA A N     1 
ATOM   2215 C  CA    . ALA A 1 304 ? 3.317   0.381   0.495   1.00 30.23  ? 276 ALA A CA    1 
ATOM   2216 C  C     . ALA A 1 304 ? 4.102   0.868   -0.721  1.00 31.58  ? 276 ALA A C     1 
ATOM   2217 O  O     . ALA A 1 304 ? 4.634   0.056   -1.488  1.00 33.54  ? 276 ALA A O     1 
ATOM   2218 C  CB    . ALA A 1 304 ? 1.826   0.236   0.161   1.00 32.46  ? 276 ALA A CB    1 
ATOM   2219 N  N     . ARG A 1 305 ? 4.167   2.183   -0.936  1.00 29.29  ? 277 ARG A N     1 
ATOM   2220 C  CA    . ARG A 1 305 ? 4.921   2.695   -2.082  1.00 28.91  ? 277 ARG A CA    1 
ATOM   2221 C  C     . ARG A 1 305 ? 6.426   2.511   -1.899  1.00 32.98  ? 277 ARG A C     1 
ATOM   2222 O  O     . ARG A 1 305 ? 7.136   2.219   -2.872  1.00 33.13  ? 277 ARG A O     1 
ATOM   2223 C  CB    . ARG A 1 305 ? 4.580   4.164   -2.328  1.00 34.74  ? 277 ARG A CB    1 
ATOM   2224 C  CG    . ARG A 1 305 ? 3.120   4.343   -2.685  1.00 40.20  ? 277 ARG A CG    1 
ATOM   2225 C  CD    . ARG A 1 305 ? 2.807   5.733   -3.196  1.00 60.87  ? 277 ARG A CD    1 
ATOM   2226 N  NE    . ARG A 1 305 ? 1.597   5.730   -4.010  1.00 64.59  ? 277 ARG A NE    1 
ATOM   2227 C  CZ    . ARG A 1 305 ? 0.448   6.279   -3.643  1.00 73.89  ? 277 ARG A CZ    1 
ATOM   2228 N  NH1   . ARG A 1 305 ? 0.324   6.925   -2.491  1.00 64.91  ? 277 ARG A NH1   1 
ATOM   2229 N  NH2   . ARG A 1 305 ? -0.605  6.181   -4.452  1.00 80.70  ? 277 ARG A NH2   1 
ATOM   2230 N  N     . LEU A 1 306 ? 6.936   2.683   -0.672  1.00 30.65  ? 278 LEU A N     1 
ATOM   2231 C  CA    . LEU A 1 306 ? 8.371   2.457   -0.448  1.00 29.94  ? 278 LEU A CA    1 
ATOM   2232 C  C     . LEU A 1 306 ? 8.729   0.973   -0.583  1.00 33.99  ? 278 LEU A C     1 
ATOM   2233 O  O     . LEU A 1 306 ? 9.783   0.635   -1.140  1.00 33.33  ? 278 LEU A O     1 
ATOM   2234 C  CB    . LEU A 1 306 ? 8.790   2.999   0.929   1.00 28.69  ? 278 LEU A CB    1 
ATOM   2235 C  CG    . LEU A 1 306 ? 8.739   4.529   1.099   1.00 36.29  ? 278 LEU A CG    1 
ATOM   2236 C  CD1   . LEU A 1 306 ? 8.811   4.918   2.583   1.00 33.07  ? 278 LEU A CD1   1 
ATOM   2237 C  CD2   . LEU A 1 306 ? 9.861   5.218   0.320   1.00 37.67  ? 278 LEU A CD2   1 
ATOM   2238 N  N     A GLU A 1 307 ? 7.876   0.079   -0.067  0.65 31.61  ? 279 GLU A N     1 
ATOM   2239 N  N     B GLU A 1 307 ? 7.862   0.079   -0.103  0.35 31.69  ? 279 GLU A N     1 
ATOM   2240 C  CA    A GLU A 1 307 ? 8.096   -1.357  -0.245  0.65 34.15  ? 279 GLU A CA    1 
ATOM   2241 C  CA    B GLU A 1 307 ? 8.108   -1.355  -0.247  0.35 34.19  ? 279 GLU A CA    1 
ATOM   2242 C  C     A GLU A 1 307 ? 8.199   -1.711  -1.725  0.65 36.79  ? 279 GLU A C     1 
ATOM   2243 C  C     B GLU A 1 307 ? 8.137   -1.776  -1.712  0.35 36.71  ? 279 GLU A C     1 
ATOM   2244 O  O     A GLU A 1 307 ? 9.077   -2.481  -2.128  0.65 37.47  ? 279 GLU A O     1 
ATOM   2245 O  O     B GLU A 1 307 ? 8.878   -2.693  -2.081  0.35 37.05  ? 279 GLU A O     1 
ATOM   2246 C  CB    A GLU A 1 307 ? 6.969   -2.179  0.414   0.65 35.13  ? 279 GLU A CB    1 
ATOM   2247 C  CB    B GLU A 1 307 ? 7.033   -2.146  0.505   0.35 35.25  ? 279 GLU A CB    1 
ATOM   2248 C  CG    A GLU A 1 307 ? 6.986   -2.181  1.945   0.65 35.97  ? 279 GLU A CG    1 
ATOM   2249 C  CG    B GLU A 1 307 ? 7.209   -3.663  0.536   0.35 36.24  ? 279 GLU A CG    1 
ATOM   2250 C  CD    A GLU A 1 307 ? 6.095   -3.251  2.610   0.65 41.83  ? 279 GLU A CD    1 
ATOM   2251 C  CD    B GLU A 1 307 ? 6.643   -4.376  -0.685  0.35 42.92  ? 279 GLU A CD    1 
ATOM   2252 O  OE1   A GLU A 1 307 ? 5.642   -4.194  1.920   0.65 31.71  ? 279 GLU A OE1   1 
ATOM   2253 O  OE1   B GLU A 1 307 ? 5.864   -3.759  -1.441  0.35 42.80  ? 279 GLU A OE1   1 
ATOM   2254 O  OE2   A GLU A 1 307 ? 5.850   -3.140  3.840   0.65 35.41  ? 279 GLU A OE2   1 
ATOM   2255 O  OE2   B GLU A 1 307 ? 6.929   -5.579  -0.856  0.35 43.46  ? 279 GLU A OE2   1 
ATOM   2256 N  N     . ALA A 1 308 ? 7.327   -1.136  -2.553  1.00 32.66  ? 280 ALA A N     1 
ATOM   2257 C  CA    . ALA A 1 308 ? 7.353   -1.453  -3.978  1.00 33.51  ? 280 ALA A CA    1 
ATOM   2258 C  C     . ALA A 1 308 ? 8.643   -0.971  -4.618  1.00 34.08  ? 280 ALA A C     1 
ATOM   2259 O  O     . ALA A 1 308 ? 9.159   -1.617  -5.547  1.00 35.68  ? 280 ALA A O     1 
ATOM   2260 C  CB    . ALA A 1 308 ? 6.153   -0.816  -4.674  1.00 33.71  ? 280 ALA A CB    1 
ATOM   2261 N  N     . LEU A 1 309 ? 9.176   0.155   -4.133  1.00 31.42  ? 281 LEU A N     1 
ATOM   2262 C  CA    . LEU A 1 309 ? 10.393  0.713   -4.706  1.00 32.90  ? 281 LEU A CA    1 
ATOM   2263 C  C     . LEU A 1 309 ? 11.603  -0.150  -4.396  1.00 35.55  ? 281 LEU A C     1 
ATOM   2264 O  O     . LEU A 1 309 ? 12.457  -0.356  -5.263  1.00 39.15  ? 281 LEU A O     1 
ATOM   2265 C  CB    . LEU A 1 309 ? 10.614  2.141   -4.191  1.00 33.83  ? 281 LEU A CB    1 
ATOM   2266 C  CG    . LEU A 1 309 ? 9.874   3.228   -4.975  1.00 38.20  ? 281 LEU A CG    1 
ATOM   2267 C  CD1   . LEU A 1 309 ? 9.986   4.566   -4.246  1.00 40.76  ? 281 LEU A CD1   1 
ATOM   2268 C  CD2   . LEU A 1 309 ? 10.469  3.339   -6.384  1.00 37.55  ? 281 LEU A CD2   1 
ATOM   2269 N  N     . THR A 1 310 ? 11.715  -0.658  -3.164  1.00 30.24  ? 282 THR A N     1 
ATOM   2270 C  CA    . THR A 1 310 ? 12.885  -1.481  -2.867  1.00 31.95  ? 282 THR A CA    1 
ATOM   2271 C  C     . THR A 1 310 ? 12.877  -2.741  -3.729  1.00 39.88  ? 282 THR A C     1 
ATOM   2272 O  O     . THR A 1 310 ? 13.935  -3.206  -4.187  1.00 37.94  ? 282 THR A O     1 
ATOM   2273 C  CB    . THR A 1 310 ? 12.934  -1.830  -1.379  1.00 34.89  ? 282 THR A CB    1 
ATOM   2274 O  OG1   . THR A 1 310 ? 11.779  -2.593  -1.012  1.00 34.79  ? 282 THR A OG1   1 
ATOM   2275 C  CG2   . THR A 1 310 ? 13.012  -0.535  -0.487  1.00 33.96  ? 282 THR A CG2   1 
ATOM   2276 N  N     . ARG A 1 311 ? 11.684  -3.273  -4.007  1.00 35.83  ? 283 ARG A N     1 
ATOM   2277 C  CA    . ARG A 1 311 ? 11.570  -4.455  -4.863  1.00 35.46  ? 283 ARG A CA    1 
ATOM   2278 C  C     . ARG A 1 311 ? 11.859  -4.116  -6.330  1.00 40.60  ? 283 ARG A C     1 
ATOM   2279 O  O     . ARG A 1 311 ? 12.596  -4.839  -7.015  1.00 46.52  ? 283 ARG A O     1 
ATOM   2280 C  CB    . ARG A 1 311 ? 10.162  -5.055  -4.726  1.00 36.09  ? 283 ARG A CB    1 
ATOM   2281 C  CG    . ARG A 1 311 ? 10.014  -6.210  -3.743  1.00 51.40  ? 283 ARG A CG    1 
ATOM   2282 C  CD    . ARG A 1 311 ? 10.609  -5.964  -2.360  1.00 53.25  ? 283 ARG A CD    1 
ATOM   2283 N  NE    . ARG A 1 311 ? 9.800   -6.620  -1.329  1.00 58.43  ? 283 ARG A NE    1 
ATOM   2284 C  CZ    . ARG A 1 311 ? 9.797   -6.309  -0.036  1.00 54.43  ? 283 ARG A CZ    1 
ATOM   2285 N  NH1   . ARG A 1 311 ? 10.593  -5.372  0.457   1.00 55.96  ? 283 ARG A NH1   1 
ATOM   2286 N  NH2   . ARG A 1 311 ? 8.988   -6.973  0.789   1.00 48.77  ? 283 ARG A NH2   1 
ATOM   2287 N  N     . GLN A 1 312 ? 11.272  -3.026  -6.838  1.00 39.02  ? 284 GLN A N     1 
ATOM   2288 C  CA    . GLN A 1 312 ? 11.390  -2.688  -8.259  1.00 44.62  ? 284 GLN A CA    1 
ATOM   2289 C  C     . GLN A 1 312 ? 12.812  -2.281  -8.637  1.00 44.45  ? 284 GLN A C     1 
ATOM   2290 O  O     . GLN A 1 312 ? 13.261  -2.548  -9.763  1.00 44.21  ? 284 GLN A O     1 
ATOM   2291 C  CB    . GLN A 1 312 ? 10.406  -1.568  -8.607  1.00 49.13  ? 284 GLN A CB    1 
ATOM   2292 C  CG    . GLN A 1 312 ? 10.758  -0.724  -9.850  1.00 49.23  ? 284 GLN A CG    1 
ATOM   2293 C  CD    . GLN A 1 312 ? 10.226  0.703   -9.782  1.00 58.05  ? 284 GLN A CD    1 
ATOM   2294 O  OE1   . GLN A 1 312 ? 10.910  1.655   -10.181 1.00 64.42  ? 284 GLN A OE1   1 
ATOM   2295 N  NE2   . GLN A 1 312 ? 9.003   0.861   -9.275  1.00 56.73  ? 284 GLN A NE2   1 
ATOM   2296 N  N     . LEU A 1 313 ? 13.532  -1.633  -7.723  1.00 39.94  ? 285 LEU A N     1 
ATOM   2297 C  CA    . LEU A 1 313 ? 14.883  -1.152  -7.985  1.00 38.95  ? 285 LEU A CA    1 
ATOM   2298 C  C     . LEU A 1 313 ? 15.952  -2.153  -7.573  1.00 35.71  ? 285 LEU A C     1 
ATOM   2299 O  O     . LEU A 1 313 ? 17.124  -1.960  -7.915  1.00 40.44  ? 285 LEU A O     1 
ATOM   2300 C  CB    . LEU A 1 313 ? 15.130  0.188   -7.260  1.00 34.37  ? 285 LEU A CB    1 
ATOM   2301 C  CG    . LEU A 1 313 ? 14.274  1.375   -7.705  1.00 41.48  ? 285 LEU A CG    1 
ATOM   2302 C  CD1   . LEU A 1 313 ? 14.445  2.583   -6.788  1.00 40.65  ? 285 LEU A CD1   1 
ATOM   2303 C  CD2   . LEU A 1 313 ? 14.620  1.748   -9.128  1.00 46.40  ? 285 LEU A CD2   1 
ATOM   2304 N  N     . SER A 1 314 ? 15.575  -3.219  -6.872  1.00 35.15  ? 286 SER A N     1 
ATOM   2305 C  CA    . SER A 1 314 ? 16.526  -4.147  -6.264  1.00 41.66  ? 286 SER A CA    1 
ATOM   2306 C  C     . SER A 1 314 ? 17.548  -3.397  -5.412  1.00 44.35  ? 286 SER A C     1 
ATOM   2307 O  O     . SER A 1 314 ? 18.756  -3.623  -5.497  1.00 42.01  ? 286 SER A O     1 
ATOM   2308 C  CB    . SER A 1 314 ? 17.227  -5.003  -7.328  1.00 53.55  ? 286 SER A CB    1 
ATOM   2309 O  OG    . SER A 1 314 ? 16.275  -5.699  -8.126  1.00 53.04  ? 286 SER A OG    1 
ATOM   2310 N  N     . GLN A 1 315 ? 17.047  -2.492  -4.570  1.00 39.07  ? 287 GLN A N     1 
ATOM   2311 C  CA    . GLN A 1 315 ? 17.891  -1.660  -3.718  1.00 39.02  ? 287 GLN A CA    1 
ATOM   2312 C  C     . GLN A 1 315 ? 17.372  -1.778  -2.300  1.00 38.33  ? 287 GLN A C     1 
ATOM   2313 O  O     . GLN A 1 315 ? 16.177  -1.580  -2.065  1.00 39.66  ? 287 GLN A O     1 
ATOM   2314 C  CB    . GLN A 1 315 ? 17.849  -0.183  -4.159  1.00 45.77  ? 287 GLN A CB    1 
ATOM   2315 C  CG    . GLN A 1 315 ? 18.440  0.082   -5.526  1.00 54.16  ? 287 GLN A CG    1 
ATOM   2316 C  CD    . GLN A 1 315 ? 19.934  0.354   -5.480  1.00 44.55  ? 287 GLN A CD    1 
ATOM   2317 O  OE1   . GLN A 1 315 ? 20.533  0.477   -4.404  1.00 48.64  ? 287 GLN A OE1   1 
ATOM   2318 N  NE2   . GLN A 1 315 ? 20.542  0.429   -6.647  1.00 55.15  ? 287 GLN A NE2   1 
ATOM   2319 N  N     . ALA A 1 316 ? 18.251  -2.083  -1.353  1.00 32.01  ? 288 ALA A N     1 
ATOM   2320 C  CA    . ALA A 1 316 ? 17.751  -2.320  -0.003  1.00 27.98  ? 288 ALA A CA    1 
ATOM   2321 C  C     . ALA A 1 316 ? 17.461  -1.044  0.768   1.00 33.05  ? 288 ALA A C     1 
ATOM   2322 O  O     . ALA A 1 316 ? 16.841  -1.126  1.831   1.00 35.01  ? 288 ALA A O     1 
ATOM   2323 C  CB    . ALA A 1 316 ? 18.752  -3.162  0.798   1.00 35.10  ? 288 ALA A CB    1 
ATOM   2324 N  N     . LEU A 1 317 ? 17.923  0.119   0.298   1.00 30.46  ? 289 LEU A N     1 
ATOM   2325 C  CA    . LEU A 1 317 ? 17.688  1.398   0.982   1.00 27.56  ? 289 LEU A CA    1 
ATOM   2326 C  C     . LEU A 1 317 ? 17.301  2.448   -0.050  1.00 30.57  ? 289 LEU A C     1 
ATOM   2327 O  O     . LEU A 1 317 ? 18.093  2.695   -0.969  1.00 31.18  ? 289 LEU A O     1 
ATOM   2328 C  CB    . LEU A 1 317 ? 18.961  1.866   1.726   1.00 28.30  ? 289 LEU A CB    1 
ATOM   2329 C  CG    . LEU A 1 317 ? 18.916  3.297   2.296   1.00 31.86  ? 289 LEU A CG    1 
ATOM   2330 C  CD1   . LEU A 1 317 ? 17.869  3.423   3.396   1.00 35.50  ? 289 LEU A CD1   1 
ATOM   2331 C  CD2   . LEU A 1 317 ? 20.301  3.685   2.872   1.00 36.01  ? 289 LEU A CD2   1 
ATOM   2332 N  N     . VAL A 1 318 ? 16.121  3.083   0.101   1.00 26.13  ? 290 VAL A N     1 
ATOM   2333 C  CA    . VAL A 1 318 ? 15.698  4.169   -0.797  1.00 24.65  ? 290 VAL A CA    1 
ATOM   2334 C  C     . VAL A 1 318 ? 15.197  5.336   0.056   1.00 31.88  ? 290 VAL A C     1 
ATOM   2335 O  O     . VAL A 1 318 ? 14.648  5.132   1.141   1.00 29.85  ? 290 VAL A O     1 
ATOM   2336 C  CB    . VAL A 1 318 ? 14.591  3.726   -1.805  1.00 32.27  ? 290 VAL A CB    1 
ATOM   2337 C  CG1   . VAL A 1 318 ? 15.100  2.578   -2.700  1.00 33.96  ? 290 VAL A CG1   1 
ATOM   2338 C  CG2   . VAL A 1 318 ? 13.303  3.306   -1.095  1.00 32.95  ? 290 VAL A CG2   1 
ATOM   2339 N  N     . PHE A 1 319 ? 15.339  6.566   -0.456  1.00 29.60  ? 291 PHE A N     1 
ATOM   2340 C  CA    . PHE A 1 319 ? 14.735  7.689   0.256   1.00 25.12  ? 291 PHE A CA    1 
ATOM   2341 C  C     . PHE A 1 319 ? 14.503  8.843   -0.710  1.00 30.68  ? 291 PHE A C     1 
ATOM   2342 O  O     . PHE A 1 319 ? 15.096  8.911   -1.786  1.00 31.08  ? 291 PHE A O     1 
ATOM   2343 C  CB    . PHE A 1 319 ? 15.580  8.153   1.455   1.00 30.96  ? 291 PHE A CB    1 
ATOM   2344 C  CG    . PHE A 1 319 ? 17.044  8.238   1.178   1.00 30.34  ? 291 PHE A CG    1 
ATOM   2345 C  CD1   . PHE A 1 319 ? 17.611  9.423   0.686   1.00 26.88  ? 291 PHE A CD1   1 
ATOM   2346 C  CD2   . PHE A 1 319 ? 17.874  7.166   1.477   1.00 29.27  ? 291 PHE A CD2   1 
ATOM   2347 C  CE1   . PHE A 1 319 ? 18.979  9.533   0.457   1.00 28.88  ? 291 PHE A CE1   1 
ATOM   2348 C  CE2   . PHE A 1 319 ? 19.267  7.267   1.261   1.00 31.71  ? 291 PHE A CE2   1 
ATOM   2349 C  CZ    . PHE A 1 319 ? 19.812  8.449   0.735   1.00 33.66  ? 291 PHE A CZ    1 
ATOM   2350 N  N     . SER A 1 320 ? 13.629  9.750   -0.299  1.00 29.62  ? 292 SER A N     1 
ATOM   2351 C  CA    . SER A 1 320 ? 13.225  10.855  -1.156  1.00 29.51  ? 292 SER A CA    1 
ATOM   2352 C  C     . SER A 1 320 ? 14.225  12.016  -1.115  1.00 31.83  ? 292 SER A C     1 
ATOM   2353 O  O     . SER A 1 320 ? 15.064  12.144  -0.213  1.00 32.36  ? 292 SER A O     1 
ATOM   2354 C  CB    . SER A 1 320 ? 11.858  11.376  -0.730  1.00 34.96  ? 292 SER A CB    1 
ATOM   2355 O  OG    . SER A 1 320 ? 11.989  12.010  0.533   1.00 35.52  ? 292 SER A OG    1 
ATOM   2356 N  N     . SER A 1 321 ? 14.061  12.917  -2.094  1.00 30.46  ? 293 SER A N     1 
ATOM   2357 C  CA    A SER A 1 321 ? 14.921  14.092  -2.173  0.74 33.14  ? 293 SER A CA    1 
ATOM   2358 C  CA    B SER A 1 321 ? 14.887  14.117  -2.188  0.26 33.22  ? 293 SER A CA    1 
ATOM   2359 C  C     . SER A 1 321 ? 14.813  14.956  -0.920  1.00 31.83  ? 293 SER A C     1 
ATOM   2360 O  O     . SER A 1 321 ? 15.802  15.595  -0.529  1.00 37.41  ? 293 SER A O     1 
ATOM   2361 C  CB    A SER A 1 321 ? 14.569  14.920  -3.424  0.74 32.79  ? 293 SER A CB    1 
ATOM   2362 C  CB    B SER A 1 321 ? 14.438  14.945  -3.398  0.26 32.78  ? 293 SER A CB    1 
ATOM   2363 O  OG    A SER A 1 321 ? 13.225  15.350  -3.392  0.74 36.98  ? 293 SER A OG    1 
ATOM   2364 O  OG    B SER A 1 321 ? 15.165  16.154  -3.501  0.26 34.87  ? 293 SER A OG    1 
ATOM   2365 N  N     . GLU A 1 322 ? 13.647  14.970  -0.269  1.00 32.60  ? 294 GLU A N     1 
ATOM   2366 C  CA    . GLU A 1 322 ? 13.479  15.774  0.943   1.00 37.41  ? 294 GLU A CA    1 
ATOM   2367 C  C     . GLU A 1 322 ? 14.399  15.284  2.051   1.00 39.75  ? 294 GLU A C     1 
ATOM   2368 O  O     . GLU A 1 322 ? 14.993  16.087  2.789   1.00 36.65  ? 294 GLU A O     1 
ATOM   2369 C  CB    . GLU A 1 322 ? 12.009  15.729  1.382   1.00 36.60  ? 294 GLU A CB    1 
ATOM   2370 C  CG    . GLU A 1 322 ? 11.180  16.873  0.784   1.00 47.00  ? 294 GLU A CG    1 
ATOM   2371 C  CD    . GLU A 1 322 ? 9.676   16.608  0.787   1.00 66.01  ? 294 GLU A CD    1 
ATOM   2372 O  OE1   . GLU A 1 322 ? 9.194   15.782  1.590   1.00 60.40  ? 294 GLU A OE1   1 
ATOM   2373 O  OE2   . GLU A 1 322 ? 8.964   17.241  -0.021  1.00 77.66  ? 294 GLU A OE2   1 
ATOM   2374 N  N     . VAL A 1 323 ? 14.547  13.964  2.171   1.00 33.35  ? 295 VAL A N     1 
ATOM   2375 C  CA    . VAL A 1 323 ? 15.473  13.405  3.150   1.00 31.21  ? 295 VAL A CA    1 
ATOM   2376 C  C     . VAL A 1 323 ? 16.902  13.730  2.760   1.00 30.52  ? 295 VAL A C     1 
ATOM   2377 O  O     . VAL A 1 323 ? 17.718  14.143  3.595   1.00 36.45  ? 295 VAL A O     1 
ATOM   2378 C  CB    . VAL A 1 323 ? 15.261  11.883  3.284   1.00 32.03  ? 295 VAL A CB    1 
ATOM   2379 C  CG1   . VAL A 1 323 ? 16.363  11.252  4.165   1.00 30.26  ? 295 VAL A CG1   1 
ATOM   2380 C  CG2   . VAL A 1 323 ? 13.853  11.578  3.835   1.00 35.02  ? 295 VAL A CG2   1 
ATOM   2381 N  N     . LYS A 1 324 ? 17.230  13.545  1.477   1.00 30.32  ? 296 LYS A N     1 
ATOM   2382 C  CA    . LYS A 1 324 ? 18.577  13.846  1.005   1.00 33.93  ? 296 LYS A CA    1 
ATOM   2383 C  C     . LYS A 1 324 ? 18.968  15.286  1.339   1.00 42.28  ? 296 LYS A C     1 
ATOM   2384 O  O     . LYS A 1 324 ? 20.073  15.545  1.850   1.00 36.59  ? 296 LYS A O     1 
ATOM   2385 C  CB    . LYS A 1 324 ? 18.643  13.576  -0.500  1.00 34.21  ? 296 LYS A CB    1 
ATOM   2386 C  CG    . LYS A 1 324 ? 20.036  13.752  -1.149  1.00 38.18  ? 296 LYS A CG    1 
ATOM   2387 C  CD    . LYS A 1 324 ? 20.028  14.854  -2.183  1.00 42.33  ? 296 LYS A CD    1 
ATOM   2388 C  CE    . LYS A 1 324 ? 21.363  14.957  -2.894  1.00 47.14  ? 296 LYS A CE    1 
ATOM   2389 N  NZ    . LYS A 1 324 ? 21.592  16.369  -3.258  1.00 45.90  ? 296 LYS A NZ    1 
ATOM   2390 N  N     . ASN A 1 325 ? 18.046  16.230  1.117   1.00 39.07  ? 297 ASN A N     1 
ATOM   2391 C  CA    . ASN A 1 325 ? 18.340  17.650  1.316   1.00 38.83  ? 297 ASN A CA    1 
ATOM   2392 C  C     . ASN A 1 325 ? 18.403  18.067  2.785   1.00 43.43  ? 297 ASN A C     1 
ATOM   2393 O  O     . ASN A 1 325 ? 18.967  19.127  3.082   1.00 48.24  ? 297 ASN A O     1 
ATOM   2394 C  CB    . ASN A 1 325 ? 17.299  18.504  0.586   1.00 41.75  ? 297 ASN A CB    1 
ATOM   2395 C  CG    . ASN A 1 325 ? 17.451  18.445  -0.922  1.00 45.84  ? 297 ASN A CG    1 
ATOM   2396 O  OD1   . ASN A 1 325 ? 18.542  18.216  -1.442  1.00 55.93  ? 297 ASN A OD1   1 
ATOM   2397 N  ND2   . ASN A 1 325 ? 16.350  18.657  -1.636  1.00 55.16  ? 297 ASN A ND2   1 
ATOM   2398 N  N     . SER A 1 326 ? 17.836  17.287  3.710   1.00 41.25  ? 298 SER A N     1 
ATOM   2399 C  CA    . SER A 1 326 ? 17.959  17.582  5.137   1.00 38.76  ? 298 SER A CA    1 
ATOM   2400 C  C     . SER A 1 326 ? 19.239  17.044  5.771   1.00 44.68  ? 298 SER A C     1 
ATOM   2401 O  O     . SER A 1 326 ? 19.482  17.299  6.956   1.00 44.10  ? 298 SER A O     1 
ATOM   2402 C  CB    . SER A 1 326 ? 16.770  16.996  5.905   1.00 40.93  ? 298 SER A CB    1 
ATOM   2403 O  OG    . SER A 1 326 ? 15.531  17.363  5.325   1.00 51.67  ? 298 SER A OG    1 
ATOM   2404 N  N     . ALA A 1 327 ? 20.046  16.282  5.049   1.00 33.44  ? 299 ALA A N     1 
ATOM   2405 C  CA    . ALA A 1 327 ? 21.255  15.711  5.633   1.00 38.55  ? 299 ALA A CA    1 
ATOM   2406 C  C     . ALA A 1 327 ? 22.388  16.735  5.609   1.00 46.81  ? 299 ALA A C     1 
ATOM   2407 O  O     . ALA A 1 327 ? 22.484  17.546  4.692   1.00 47.85  ? 299 ALA A O     1 
ATOM   2408 C  CB    . ALA A 1 327 ? 21.671  14.448  4.870   1.00 43.03  ? 299 ALA A CB    1 
ATOM   2409 N  N     . THR A 1 328 ? 23.253  16.698  6.629   1.00 39.19  ? 300 THR A N     1 
ATOM   2410 C  CA    . THR A 1 328 ? 24.393  17.621  6.661   1.00 45.06  ? 300 THR A CA    1 
ATOM   2411 C  C     . THR A 1 328 ? 25.729  16.983  6.275   1.00 48.03  ? 300 THR A C     1 
ATOM   2412 O  O     . THR A 1 328 ? 26.624  17.695  5.801   1.00 54.63  ? 300 THR A O     1 
ATOM   2413 C  CB    . THR A 1 328 ? 24.520  18.281  8.049   1.00 42.64  ? 300 THR A CB    1 
ATOM   2414 O  OG1   . THR A 1 328 ? 24.889  17.309  9.042   1.00 50.49  ? 300 THR A OG1   1 
ATOM   2415 C  CG2   . THR A 1 328 ? 23.221  18.914  8.461   1.00 48.67  ? 300 THR A CG2   1 
ATOM   2416 N  N     . LYS A 1 329 ? 25.888  15.674  6.423   1.00 42.19  ? 301 LYS A N     1 
ATOM   2417 C  CA    . LYS A 1 329 ? 27.161  15.054  6.098   1.00 41.62  ? 301 LYS A CA    1 
ATOM   2418 C  C     . LYS A 1 329 ? 27.275  14.767  4.595   1.00 39.19  ? 301 LYS A C     1 
ATOM   2419 O  O     . LYS A 1 329 ? 26.287  14.771  3.852   1.00 42.69  ? 301 LYS A O     1 
ATOM   2420 C  CB    . LYS A 1 329 ? 27.356  13.778  6.926   1.00 42.78  ? 301 LYS A CB    1 
ATOM   2421 C  CG    . LYS A 1 329 ? 27.085  13.990  8.418   1.00 46.62  ? 301 LYS A CG    1 
ATOM   2422 C  CD    . LYS A 1 329 ? 27.515  12.783  9.265   1.00 57.72  ? 301 LYS A CD    1 
ATOM   2423 C  CE    . LYS A 1 329 ? 27.712  13.192  10.727  1.00 71.59  ? 301 LYS A CE    1 
ATOM   2424 N  NZ    . LYS A 1 329 ? 29.029  13.861  10.967  1.00 73.65  ? 301 LYS A NZ    1 
ATOM   2425 N  N     . SER A 1 330 ? 28.509  14.517  4.152   1.00 40.61  ? 302 SER A N     1 
ATOM   2426 C  CA    A SER A 1 330 ? 28.783  14.310  2.726   0.46 43.32  ? 302 SER A CA    1 
ATOM   2427 C  CA    B SER A 1 330 ? 28.807  14.304  2.732   0.54 43.33  ? 302 SER A CA    1 
ATOM   2428 C  C     . SER A 1 330 ? 28.683  12.820  2.382   1.00 43.15  ? 302 SER A C     1 
ATOM   2429 O  O     . SER A 1 330 ? 29.654  12.135  2.062   1.00 42.62  ? 302 SER A O     1 
ATOM   2430 C  CB    A SER A 1 330 ? 30.140  14.894  2.353   0.46 45.54  ? 302 SER A CB    1 
ATOM   2431 C  CB    B SER A 1 330 ? 30.199  14.823  2.400   0.54 45.56  ? 302 SER A CB    1 
ATOM   2432 O  OG    A SER A 1 330 ? 30.111  16.312  2.429   0.46 37.11  ? 302 SER A OG    1 
ATOM   2433 O  OG    B SER A 1 330 ? 31.188  13.976  2.963   0.54 49.58  ? 302 SER A OG    1 
ATOM   2434 N  N     . TRP A 1 331 ? 27.452  12.326  2.442   1.00 38.55  ? 303 TRP A N     1 
ATOM   2435 C  CA    . TRP A 1 331 ? 27.168  10.943  2.086   1.00 35.55  ? 303 TRP A CA    1 
ATOM   2436 C  C     . TRP A 1 331 ? 27.435  10.679  0.592   1.00 30.72  ? 303 TRP A C     1 
ATOM   2437 O  O     . TRP A 1 331 ? 27.370  11.576  -0.263  1.00 32.19  ? 303 TRP A O     1 
ATOM   2438 C  CB    . TRP A 1 331 ? 25.701  10.624  2.416   1.00 32.82  ? 303 TRP A CB    1 
ATOM   2439 C  CG    . TRP A 1 331 ? 25.318  10.739  3.883   1.00 31.47  ? 303 TRP A CG    1 
ATOM   2440 C  CD1   . TRP A 1 331 ? 24.645  11.772  4.492   1.00 32.69  ? 303 TRP A CD1   1 
ATOM   2441 C  CD2   . TRP A 1 331 ? 25.560  9.767   4.909   1.00 31.35  ? 303 TRP A CD2   1 
ATOM   2442 N  NE1   . TRP A 1 331 ? 24.472  11.503  5.838   1.00 36.05  ? 303 TRP A NE1   1 
ATOM   2443 C  CE2   . TRP A 1 331 ? 25.012  10.272  6.112   1.00 33.67  ? 303 TRP A CE2   1 
ATOM   2444 C  CE3   . TRP A 1 331 ? 26.193  8.520   4.926   1.00 35.48  ? 303 TRP A CE3   1 
ATOM   2445 C  CZ2   . TRP A 1 331 ? 25.087  9.574   7.312   1.00 35.27  ? 303 TRP A CZ2   1 
ATOM   2446 C  CZ3   . TRP A 1 331 ? 26.263  7.826   6.108   1.00 34.87  ? 303 TRP A CZ3   1 
ATOM   2447 C  CH2   . TRP A 1 331 ? 25.721  8.352   7.290   1.00 36.60  ? 303 TRP A CH2   1 
ATOM   2448 N  N     . ASN A 1 332 ? 27.692  9.408   0.262   1.00 32.81  ? 304 ASN A N     1 
ATOM   2449 C  CA    . ASN A 1 332 ? 27.883  9.005   -1.138  1.00 31.07  ? 304 ASN A CA    1 
ATOM   2450 C  C     . ASN A 1 332 ? 26.529  8.740   -1.811  1.00 33.51  ? 304 ASN A C     1 
ATOM   2451 O  O     . ASN A 1 332 ? 26.176  7.605   -2.129  1.00 32.83  ? 304 ASN A O     1 
ATOM   2452 C  CB    . ASN A 1 332 ? 28.773  7.770   -1.228  1.00 32.34  ? 304 ASN A CB    1 
ATOM   2453 C  CG    . ASN A 1 332 ? 30.134  7.973   -0.559  1.00 46.66  ? 304 ASN A CG    1 
ATOM   2454 O  OD1   . ASN A 1 332 ? 30.658  7.069   0.098   1.00 45.35  ? 304 ASN A OD1   1 
ATOM   2455 N  ND2   . ASN A 1 332 ? 30.689  9.175   -0.695  1.00 38.29  ? 304 ASN A ND2   1 
ATOM   2456 N  N     . PHE A 1 333 ? 25.798  9.825   -2.086  1.00 28.69  ? 305 PHE A N     1 
ATOM   2457 C  CA    . PHE A 1 333 ? 24.454  9.751   -2.686  1.00 27.83  ? 305 PHE A CA    1 
ATOM   2458 C  C     . PHE A 1 333 ? 24.491  9.296   -4.141  1.00 31.35  ? 305 PHE A C     1 
ATOM   2459 O  O     . PHE A 1 333 ? 25.388  9.664   -4.905  1.00 32.50  ? 305 PHE A O     1 
ATOM   2460 C  CB    . PHE A 1 333 ? 23.756  11.119  -2.669  1.00 33.11  ? 305 PHE A CB    1 
ATOM   2461 C  CG    . PHE A 1 333 ? 23.462  11.674  -1.292  1.00 31.88  ? 305 PHE A CG    1 
ATOM   2462 C  CD1   . PHE A 1 333 ? 22.587  11.024  -0.431  1.00 34.08  ? 305 PHE A CD1   1 
ATOM   2463 C  CD2   . PHE A 1 333 ? 24.046  12.864  -0.883  1.00 35.88  ? 305 PHE A CD2   1 
ATOM   2464 C  CE1   . PHE A 1 333 ? 22.308  11.541  0.839   1.00 40.44  ? 305 PHE A CE1   1 
ATOM   2465 C  CE2   . PHE A 1 333 ? 23.767  13.389  0.387   1.00 35.25  ? 305 PHE A CE2   1 
ATOM   2466 C  CZ    . PHE A 1 333 ? 22.900  12.732  1.234   1.00 33.69  ? 305 PHE A CZ    1 
ATOM   2467 N  N     . ILE A 1 334 ? 23.458  8.545   -4.553  1.00 28.03  ? 306 ILE A N     1 
ATOM   2468 C  CA    . ILE A 1 334 ? 23.273  8.179   -5.960  1.00 27.59  ? 306 ILE A CA    1 
ATOM   2469 C  C     . ILE A 1 334 ? 21.800  8.352   -6.328  1.00 32.32  ? 306 ILE A C     1 
ATOM   2470 O  O     . ILE A 1 334 ? 20.914  7.876   -5.607  1.00 29.54  ? 306 ILE A O     1 
ATOM   2471 C  CB    . ILE A 1 334 ? 23.777  6.742   -6.271  1.00 30.70  ? 306 ILE A CB    1 
ATOM   2472 C  CG1   . ILE A 1 334 ? 23.544  6.402   -7.746  1.00 29.75  ? 306 ILE A CG1   1 
ATOM   2473 C  CG2   . ILE A 1 334 ? 23.143  5.670   -5.340  1.00 30.80  ? 306 ILE A CG2   1 
ATOM   2474 C  CD1   . ILE A 1 334 ? 24.261  5.105   -8.196  1.00 34.96  ? 306 ILE A CD1   1 
ATOM   2475 N  N     . TRP A 1 335 ? 21.532  9.052   -7.441  1.00 27.97  ? 307 TRP A N     1 
ATOM   2476 C  CA    . TRP A 1 335 ? 20.163  9.207   -7.958  1.00 30.96  ? 307 TRP A CA    1 
ATOM   2477 C  C     . TRP A 1 335 ? 19.723  7.921   -8.656  1.00 31.51  ? 307 TRP A C     1 
ATOM   2478 O  O     . TRP A 1 335 ? 20.506  7.317   -9.394  1.00 33.26  ? 307 TRP A O     1 
ATOM   2479 C  CB    . TRP A 1 335 ? 20.099  10.398  -8.939  1.00 30.64  ? 307 TRP A CB    1 
ATOM   2480 C  CG    . TRP A 1 335 ? 18.734  10.577  -9.575  1.00 29.75  ? 307 TRP A CG    1 
ATOM   2481 C  CD1   . TRP A 1 335 ? 17.701  11.334  -9.090  1.00 31.36  ? 307 TRP A CD1   1 
ATOM   2482 C  CD2   . TRP A 1 335 ? 18.241  9.976   -10.793 1.00 31.49  ? 307 TRP A CD2   1 
ATOM   2483 N  NE1   . TRP A 1 335 ? 16.615  11.235  -9.913  1.00 32.84  ? 307 TRP A NE1   1 
ATOM   2484 C  CE2   . TRP A 1 335 ? 16.917  10.412  -10.965 1.00 31.55  ? 307 TRP A CE2   1 
ATOM   2485 C  CE3   . TRP A 1 335 ? 18.793  9.107   -11.741 1.00 32.62  ? 307 TRP A CE3   1 
ATOM   2486 C  CZ2   . TRP A 1 335 ? 16.121  10.012  -12.050 1.00 33.82  ? 307 TRP A CZ2   1 
ATOM   2487 C  CZ3   . TRP A 1 335 ? 17.991  8.715   -12.833 1.00 33.50  ? 307 TRP A CZ3   1 
ATOM   2488 C  CH2   . TRP A 1 335 ? 16.685  9.165   -12.973 1.00 32.96  ? 307 TRP A CH2   1 
ATOM   2489 N  N     . LEU A 1 336 ? 18.483  7.471   -8.398  1.00 28.21  ? 308 LEU A N     1 
ATOM   2490 C  CA    . LEU A 1 336 ? 17.997  6.204   -8.963  1.00 32.00  ? 308 LEU A CA    1 
ATOM   2491 C  C     . LEU A 1 336 ? 16.861  6.344   -9.976  1.00 32.05  ? 308 LEU A C     1 
ATOM   2492 O  O     . LEU A 1 336 ? 16.911  5.698   -11.037 1.00 33.98  ? 308 LEU A O     1 
ATOM   2493 C  CB    . LEU A 1 336 ? 17.544  5.263   -7.823  1.00 31.28  ? 308 LEU A CB    1 
ATOM   2494 C  CG    . LEU A 1 336 ? 18.629  4.723   -6.878  1.00 35.63  ? 308 LEU A CG    1 
ATOM   2495 C  CD1   . LEU A 1 336 ? 17.979  3.819   -5.793  1.00 39.55  ? 308 LEU A CD1   1 
ATOM   2496 C  CD2   . LEU A 1 336 ? 19.796  4.014   -7.591  1.00 36.72  ? 308 LEU A CD2   1 
ATOM   2497 N  N     . THR A 1 337 ? 15.812  7.124   -9.681  1.00 29.77  ? 309 THR A N     1 
ATOM   2498 C  CA    . THR A 1 337 ? 14.584  7.163   -10.485 1.00 31.01  ? 309 THR A CA    1 
ATOM   2499 C  C     . THR A 1 337 ? 13.671  8.269   -9.953  1.00 33.67  ? 309 THR A C     1 
ATOM   2500 O  O     . THR A 1 337 ? 13.962  8.901   -8.930  1.00 32.47  ? 309 THR A O     1 
ATOM   2501 C  CB    . THR A 1 337 ? 13.857  5.798   -10.443 1.00 33.88  ? 309 THR A CB    1 
ATOM   2502 O  OG1   . THR A 1 337 ? 12.880  5.713   -11.488 1.00 35.23  ? 309 THR A OG1   1 
ATOM   2503 C  CG2   . THR A 1 337 ? 13.136  5.619   -9.081  1.00 32.19  ? 309 THR A CG2   1 
ATOM   2504 N  N     . ASP A 1 338 ? 12.553  8.498   -10.655 1.00 31.86  ? 310 ASP A N     1 
ATOM   2505 C  CA    . ASP A 1 338 ? 11.466  9.318   -10.137 1.00 29.00  ? 310 ASP A CA    1 
ATOM   2506 C  C     . ASP A 1 338 ? 10.333  8.413   -9.662  1.00 36.03  ? 310 ASP A C     1 
ATOM   2507 O  O     . ASP A 1 338 ? 10.096  7.344   -10.230 1.00 33.70  ? 310 ASP A O     1 
ATOM   2508 C  CB    . ASP A 1 338 ? 10.881  10.288  -11.172 1.00 31.75  ? 310 ASP A CB    1 
ATOM   2509 C  CG    . ASP A 1 338 ? 11.684  11.566  -11.330 1.00 31.39  ? 310 ASP A CG    1 
ATOM   2510 O  OD1   . ASP A 1 338 ? 12.821  11.524  -11.817 1.00 33.02  ? 310 ASP A OD1   1 
ATOM   2511 O  OD2   . ASP A 1 338 ? 11.145  12.620  -10.925 1.00 35.88  ? 310 ASP A OD2   1 
ATOM   2512 N  N     . SER A 1 339 ? 9.621   8.857   -8.633  1.00 33.19  ? 311 SER A N     1 
ATOM   2513 C  CA    . SER A 1 339 ? 8.438   8.130   -8.174  1.00 33.67  ? 311 SER A CA    1 
ATOM   2514 C  C     . SER A 1 339 ? 7.425   9.099   -7.569  1.00 39.16  ? 311 SER A C     1 
ATOM   2515 O  O     . SER A 1 339 ? 7.590   10.325  -7.593  1.00 38.52  ? 311 SER A O     1 
ATOM   2516 C  CB    . SER A 1 339 ? 8.820   7.034   -7.167  1.00 40.89  ? 311 SER A CB    1 
ATOM   2517 O  OG    . SER A 1 339 ? 7.789   6.050   -7.070  1.00 40.26  ? 311 SER A OG    1 
ATOM   2518 N  N     . GLU A 1 340 ? 6.343   8.518   -7.058  1.00 38.28  ? 312 GLU A N     1 
ATOM   2519 C  CA    . GLU A 1 340 ? 5.248   9.229   -6.412  1.00 45.90  ? 312 GLU A CA    1 
ATOM   2520 C  C     . GLU A 1 340 ? 5.073   8.575   -5.052  1.00 42.44  ? 312 GLU A C     1 
ATOM   2521 O  O     . GLU A 1 340 ? 4.910   7.357   -4.981  1.00 44.43  ? 312 GLU A O     1 
ATOM   2522 C  CB    . GLU A 1 340 ? 3.981   9.121   -7.270  1.00 47.47  ? 312 GLU A CB    1 
ATOM   2523 C  CG    . GLU A 1 340 ? 2.679   9.663   -6.695  1.00 61.99  ? 312 GLU A CG    1 
ATOM   2524 C  CD    . GLU A 1 340 ? 1.524   9.532   -7.697  1.00 74.45  ? 312 GLU A CD    1 
ATOM   2525 O  OE1   . GLU A 1 340 ? 1.299   10.474  -8.488  1.00 74.70  ? 312 GLU A OE1   1 
ATOM   2526 O  OE2   . GLU A 1 340 ? 0.857   8.472   -7.715  1.00 69.22  ? 312 GLU A OE2   1 
ATOM   2527 N  N     . LEU A 1 341 ? 5.173   9.360   -3.976  1.00 38.93  ? 313 LEU A N     1 
ATOM   2528 C  CA    . LEU A 1 341 ? 5.087   8.815   -2.626  1.00 47.30  ? 313 LEU A CA    1 
ATOM   2529 C  C     . LEU A 1 341 ? 3.806   9.220   -1.912  1.00 57.82  ? 313 LEU A C     1 
ATOM   2530 O  O     . LEU A 1 341 ? 3.167   8.384   -1.263  1.00 51.63  ? 313 LEU A O     1 
ATOM   2531 C  CB    . LEU A 1 341 ? 6.302   9.250   -1.788  1.00 44.25  ? 313 LEU A CB    1 
ATOM   2532 C  CG    . LEU A 1 341 ? 7.676   8.704   -2.182  1.00 43.47  ? 313 LEU A CG    1 
ATOM   2533 C  CD1   . LEU A 1 341 ? 8.748   9.033   -1.119  1.00 43.94  ? 313 LEU A CD1   1 
ATOM   2534 C  CD2   . LEU A 1 341 ? 7.615   7.208   -2.428  1.00 46.98  ? 313 LEU A CD2   1 
ATOM   2535 N  N     . LYS A 1 342 ? 3.421   10.488  -2.009  1.00 53.89  ? 314 LYS A N     1 
ATOM   2536 C  CA    . LYS A 1 342 ? 2.178   10.945  -1.415  1.00 69.46  ? 314 LYS A CA    1 
ATOM   2537 C  C     . LYS A 1 342 ? 1.008   10.595  -2.331  1.00 78.70  ? 314 LYS A C     1 
ATOM   2538 O  O     . LYS A 1 342 ? 1.184   10.141  -3.465  1.00 84.23  ? 314 LYS A O     1 
ATOM   2539 C  CB    . LYS A 1 342 ? 2.229   12.450  -1.158  1.00 63.30  ? 314 LYS A CB    1 
ATOM   2540 N  N     . GLY A 1 343 ? -0.207  10.806  -1.827  1.00 74.86  ? 315 GLY A N     1 
ATOM   2541 C  CA    . GLY A 1 343 ? -1.367  10.636  -2.682  1.00 91.91  ? 315 GLY A CA    1 
ATOM   2542 C  C     . GLY A 1 343 ? -1.381  11.577  -3.870  1.00 93.34  ? 315 GLY A C     1 
ATOM   2543 O  O     . GLY A 1 343 ? -2.044  11.290  -4.874  1.00 91.26  ? 315 GLY A O     1 
ATOM   2544 N  N     . LYS A 1 344 ? -0.649  12.688  -3.784  1.00 88.94  ? 316 LYS A N     1 
ATOM   2545 C  CA    . LYS A 1 344 ? -0.643  13.705  -4.824  1.00 85.71  ? 316 LYS A CA    1 
ATOM   2546 C  C     . LYS A 1 344 ? 0.090   13.194  -6.063  1.00 85.17  ? 316 LYS A C     1 
ATOM   2547 O  O     . LYS A 1 344 ? 0.568   12.058  -6.118  1.00 89.94  ? 316 LYS A O     1 
ATOM   2548 C  CB    . LYS A 1 344 ? -0.005  14.989  -4.299  1.00 88.01  ? 316 LYS A CB    1 
ATOM   2549 N  N     . SER A 1 345 ? 0.195   14.061  -7.071  1.00 76.98  ? 317 SER A N     1 
ATOM   2550 C  CA    . SER A 1 345 ? 0.723   13.681  -8.375  1.00 77.86  ? 317 SER A CA    1 
ATOM   2551 C  C     . SER A 1 345 ? 2.077   14.317  -8.686  1.00 72.44  ? 317 SER A C     1 
ATOM   2552 O  O     . SER A 1 345 ? 2.475   14.361  -9.854  1.00 76.22  ? 317 SER A O     1 
ATOM   2553 C  CB    . SER A 1 345 ? -0.286  14.031  -9.467  1.00 75.15  ? 317 SER A CB    1 
ATOM   2554 O  OG    . SER A 1 345 ? -0.011  15.309  -10.012 1.00 82.86  ? 317 SER A OG    1 
ATOM   2555 N  N     . GLU A 1 346 ? 2.796   14.809  -7.678  1.00 66.78  ? 318 GLU A N     1 
ATOM   2556 C  CA    . GLU A 1 346 ? 4.130   15.353  -7.902  1.00 69.14  ? 318 GLU A CA    1 
ATOM   2557 C  C     . GLU A 1 346 ? 5.156   14.235  -8.047  1.00 57.98  ? 318 GLU A C     1 
ATOM   2558 O  O     . GLU A 1 346 ? 5.069   13.202  -7.379  1.00 60.14  ? 318 GLU A O     1 
ATOM   2559 C  CB    . GLU A 1 346 ? 4.540   16.297  -6.770  1.00 69.35  ? 318 GLU A CB    1 
ATOM   2560 C  CG    . GLU A 1 346 ? 4.263   17.772  -7.055  1.00 80.89  ? 318 GLU A CG    1 
ATOM   2561 C  CD    . GLU A 1 346 ? 2.935   18.259  -6.506  1.00 95.66  ? 318 GLU A CD    1 
ATOM   2562 O  OE1   . GLU A 1 346 ? 2.650   18.013  -5.313  1.00 93.97  ? 318 GLU A OE1   1 
ATOM   2563 O  OE2   . GLU A 1 346 ? 2.176   18.893  -7.271  1.00 103.48 ? 318 GLU A OE2   1 
ATOM   2564 N  N     . SER A 1 347 ? 6.125   14.448  -8.932  1.00 41.05  ? 319 SER A N     1 
ATOM   2565 C  CA    . SER A 1 347 ? 7.128   13.439  -9.256  1.00 39.79  ? 319 SER A CA    1 
ATOM   2566 C  C     . SER A 1 347 ? 8.385   13.764  -8.462  1.00 42.25  ? 319 SER A C     1 
ATOM   2567 O  O     . SER A 1 347 ? 8.963   14.844  -8.631  1.00 40.74  ? 319 SER A O     1 
ATOM   2568 C  CB    . SER A 1 347 ? 7.407   13.419  -10.762 1.00 41.66  ? 319 SER A CB    1 
ATOM   2569 O  OG    . SER A 1 347 ? 8.299   12.373  -11.123 1.00 37.11  ? 319 SER A OG    1 
ATOM   2570 N  N     . ILE A 1 348 ? 8.799   12.837  -7.596  1.00 32.77  ? 320 ILE A N     1 
ATOM   2571 C  CA    . ILE A 1 348 ? 9.875   13.062  -6.631  1.00 34.14  ? 320 ILE A CA    1 
ATOM   2572 C  C     . ILE A 1 348 ? 11.100  12.242  -7.015  1.00 32.72  ? 320 ILE A C     1 
ATOM   2573 O  O     . ILE A 1 348 ? 10.983  11.063  -7.370  1.00 33.65  ? 320 ILE A O     1 
ATOM   2574 C  CB    . ILE A 1 348 ? 9.414   12.669  -5.214  1.00 39.40  ? 320 ILE A CB    1 
ATOM   2575 C  CG1   . ILE A 1 348 ? 8.053   13.305  -4.919  1.00 54.34  ? 320 ILE A CG1   1 
ATOM   2576 C  CG2   . ILE A 1 348 ? 10.454  13.077  -4.183  1.00 46.66  ? 320 ILE A CG2   1 
ATOM   2577 C  CD1   . ILE A 1 348 ? 8.139   14.771  -4.542  1.00 51.61  ? 320 ILE A CD1   1 
ATOM   2578 N  N     . ASP A 1 349 ? 12.283  12.846  -6.878  1.00 31.45  ? 321 ASP A N     1 
ATOM   2579 C  CA    . ASP A 1 349 ? 13.521  12.120  -7.112  1.00 30.24  ? 321 ASP A CA    1 
ATOM   2580 C  C     . ASP A 1 349 ? 13.799  11.149  -5.962  1.00 30.86  ? 321 ASP A C     1 
ATOM   2581 O  O     . ASP A 1 349 ? 13.671  11.511  -4.786  1.00 31.35  ? 321 ASP A O     1 
ATOM   2582 C  CB    . ASP A 1 349 ? 14.690  13.097  -7.227  1.00 30.88  ? 321 ASP A CB    1 
ATOM   2583 C  CG    . ASP A 1 349 ? 14.643  13.915  -8.512  1.00 38.36  ? 321 ASP A CG    1 
ATOM   2584 O  OD1   . ASP A 1 349 ? 14.343  13.342  -9.578  1.00 34.09  ? 321 ASP A OD1   1 
ATOM   2585 O  OD2   . ASP A 1 349 ? 14.930  15.125  -8.450  1.00 43.22  ? 321 ASP A OD2   1 
ATOM   2586 N  N     . ILE A 1 350 ? 14.215  9.926   -6.306  1.00 27.23  ? 322 ILE A N     1 
ATOM   2587 C  CA    . ILE A 1 350 ? 14.519  8.872   -5.329  1.00 27.09  ? 322 ILE A CA    1 
ATOM   2588 C  C     . ILE A 1 350 ? 16.026  8.603   -5.345  1.00 32.58  ? 322 ILE A C     1 
ATOM   2589 O  O     . ILE A 1 350 ? 16.612  8.427   -6.421  1.00 31.51  ? 322 ILE A O     1 
ATOM   2590 C  CB    . ILE A 1 350 ? 13.740  7.571   -5.634  1.00 29.13  ? 322 ILE A CB    1 
ATOM   2591 C  CG1   . ILE A 1 350 ? 12.212  7.797   -5.643  1.00 31.41  ? 322 ILE A CG1   1 
ATOM   2592 C  CG2   . ILE A 1 350 ? 14.148  6.453   -4.633  1.00 33.39  ? 322 ILE A CG2   1 
ATOM   2593 C  CD1   . ILE A 1 350 ? 11.620  8.345   -4.310  1.00 35.10  ? 322 ILE A CD1   1 
ATOM   2594 N  N     . TYR A 1 351 ? 16.649  8.539   -4.155  1.00 28.13  ? 323 TYR A N     1 
ATOM   2595 C  CA    . TYR A 1 351 ? 18.090  8.354   -3.986  1.00 26.42  ? 323 TYR A CA    1 
ATOM   2596 C  C     . TYR A 1 351 ? 18.395  7.114   -3.146  1.00 30.48  ? 323 TYR A C     1 
ATOM   2597 O  O     . TYR A 1 351 ? 17.530  6.602   -2.432  1.00 28.43  ? 323 TYR A O     1 
ATOM   2598 C  CB    . TYR A 1 351 ? 18.719  9.564   -3.262  1.00 29.19  ? 323 TYR A CB    1 
ATOM   2599 C  CG    . TYR A 1 351 ? 18.690  10.827  -4.089  1.00 28.38  ? 323 TYR A CG    1 
ATOM   2600 C  CD1   . TYR A 1 351 ? 17.544  11.626  -4.133  1.00 30.43  ? 323 TYR A CD1   1 
ATOM   2601 C  CD2   . TYR A 1 351 ? 19.807  11.224  -4.825  1.00 36.66  ? 323 TYR A CD2   1 
ATOM   2602 C  CE1   . TYR A 1 351 ? 17.503  12.774  -4.904  1.00 35.04  ? 323 TYR A CE1   1 
ATOM   2603 C  CE2   . TYR A 1 351 ? 19.768  12.370  -5.602  1.00 35.90  ? 323 TYR A CE2   1 
ATOM   2604 C  CZ    . TYR A 1 351 ? 18.625  13.136  -5.635  1.00 42.42  ? 323 TYR A CZ    1 
ATOM   2605 O  OH    . TYR A 1 351 ? 18.612  14.279  -6.408  1.00 39.46  ? 323 TYR A OH    1 
ATOM   2606 N  N     . SER A 1 352 ? 19.657  6.678   -3.181  1.00 30.07  ? 324 SER A N     1 
ATOM   2607 C  CA    . SER A 1 352 ? 20.183  5.728   -2.189  1.00 27.22  ? 324 SER A CA    1 
ATOM   2608 C  C     . SER A 1 352 ? 21.605  6.162   -1.836  1.00 32.74  ? 324 SER A C     1 
ATOM   2609 O  O     . SER A 1 352 ? 22.024  7.287   -2.144  1.00 30.25  ? 324 SER A O     1 
ATOM   2610 C  CB    . SER A 1 352 ? 20.116  4.280   -2.708  1.00 29.99  ? 324 SER A CB    1 
ATOM   2611 O  OG    . SER A 1 352 ? 20.539  3.341   -1.694  1.00 30.78  ? 324 SER A OG    1 
ATOM   2612 N  N     . ILE A 1 353 ? 22.319  5.286   -1.126  1.00 30.56  ? 325 ILE A N     1 
ATOM   2613 C  CA    . ILE A 1 353 ? 23.752  5.415   -0.848  1.00 31.69  ? 325 ILE A CA    1 
ATOM   2614 C  C     . ILE A 1 353 ? 24.480  4.364   -1.667  1.00 38.59  ? 325 ILE A C     1 
ATOM   2615 O  O     . ILE A 1 353 ? 24.099  3.186   -1.645  1.00 36.21  ? 325 ILE A O     1 
ATOM   2616 C  CB    . ILE A 1 353 ? 24.061  5.216   0.650   1.00 29.87  ? 325 ILE A CB    1 
ATOM   2617 C  CG1   . ILE A 1 353 ? 23.312  6.236   1.516   1.00 41.10  ? 325 ILE A CG1   1 
ATOM   2618 C  CG2   . ILE A 1 353 ? 25.578  5.291   0.914   1.00 38.97  ? 325 ILE A CG2   1 
ATOM   2619 C  CD1   . ILE A 1 353 ? 23.827  7.633   1.343   1.00 39.84  ? 325 ILE A CD1   1 
ATOM   2620 N  N     . ASP A 1 354 ? 25.544  4.772   -2.363  1.00 30.69  ? 326 ASP A N     1 
ATOM   2621 C  CA    . ASP A 1 354 ? 26.327  3.847   -3.181  1.00 30.54  ? 326 ASP A CA    1 
ATOM   2622 C  C     . ASP A 1 354 ? 27.489  3.347   -2.338  1.00 40.15  ? 326 ASP A C     1 
ATOM   2623 O  O     . ASP A 1 354 ? 28.481  4.052   -2.148  1.00 37.67  ? 326 ASP A O     1 
ATOM   2624 C  CB    . ASP A 1 354 ? 26.815  4.550   -4.445  1.00 35.23  ? 326 ASP A CB    1 
ATOM   2625 C  CG    . ASP A 1 354 ? 27.643  3.644   -5.345  1.00 43.38  ? 326 ASP A CG    1 
ATOM   2626 O  OD1   . ASP A 1 354 ? 27.543  2.411   -5.232  1.00 41.28  ? 326 ASP A OD1   1 
ATOM   2627 O  OD2   . ASP A 1 354 ? 28.379  4.181   -6.184  1.00 36.61  ? 326 ASP A OD2   1 
ATOM   2628 N  N     . ASN A 1 355 ? 27.374  2.138   -1.804  1.00 40.94  ? 327 ASN A N     1 
ATOM   2629 C  CA    . ASN A 1 355 ? 28.527  1.547   -1.139  1.00 48.91  ? 327 ASN A CA    1 
ATOM   2630 C  C     . ASN A 1 355 ? 28.462  0.038   -1.322  1.00 46.95  ? 327 ASN A C     1 
ATOM   2631 O  O     . ASN A 1 355 ? 27.536  -0.492  -1.945  1.00 48.13  ? 327 ASN A O     1 
ATOM   2632 C  CB    . ASN A 1 355 ? 28.635  1.993   0.330   1.00 50.43  ? 327 ASN A CB    1 
ATOM   2633 C  CG    . ASN A 1 355 ? 27.549  1.405   1.240   1.00 48.19  ? 327 ASN A CG    1 
ATOM   2634 O  OD1   . ASN A 1 355 ? 26.831  0.474   0.883   1.00 53.88  ? 327 ASN A OD1   1 
ATOM   2635 N  ND2   . ASN A 1 355 ? 27.448  1.959   2.437   1.00 55.23  ? 327 ASN A ND2   1 
ATOM   2636 N  N     . GLU A 1 356 ? 29.491  -0.648  -0.817  1.00 61.15  ? 328 GLU A N     1 
ATOM   2637 C  CA    . GLU A 1 356 ? 29.577  -2.090  -1.016  1.00 66.80  ? 328 GLU A CA    1 
ATOM   2638 C  C     . GLU A 1 356 ? 28.371  -2.801  -0.413  1.00 60.45  ? 328 GLU A C     1 
ATOM   2639 O  O     . GLU A 1 356 ? 27.894  -3.796  -0.970  1.00 68.25  ? 328 GLU A O     1 
ATOM   2640 C  CB    . GLU A 1 356 ? 30.892  -2.608  -0.429  1.00 63.29  ? 328 GLU A CB    1 
ATOM   2641 C  CG    . GLU A 1 356 ? 30.853  -2.866  1.065   1.00 65.50  ? 328 GLU A CG    1 
ATOM   2642 C  CD    . GLU A 1 356 ? 31.275  -1.649  1.882   1.00 80.34  ? 328 GLU A CD    1 
ATOM   2643 O  OE1   . GLU A 1 356 ? 31.534  -0.574  1.289   1.00 72.26  ? 328 GLU A OE1   1 
ATOM   2644 O  OE2   . GLU A 1 356 ? 31.336  -1.766  3.125   1.00 83.96  ? 328 GLU A OE2   1 
ATOM   2645 N  N     . MET A 1 357 ? 27.833  -2.267  0.686   1.00 69.52  ? 329 MET A N     1 
ATOM   2646 C  CA    . MET A 1 357 ? 26.657  -2.847  1.327   1.00 64.80  ? 329 MET A CA    1 
ATOM   2647 C  C     . MET A 1 357 ? 25.455  -2.831  0.390   1.00 77.18  ? 329 MET A C     1 
ATOM   2648 O  O     . MET A 1 357 ? 24.888  -3.882  0.068   1.00 81.68  ? 329 MET A O     1 
ATOM   2649 C  CB    . MET A 1 357 ? 26.361  -2.081  2.619   1.00 70.44  ? 329 MET A CB    1 
ATOM   2650 C  CG    . MET A 1 357 ? 25.393  -2.738  3.587   1.00 68.50  ? 329 MET A CG    1 
ATOM   2651 S  SD    . MET A 1 357 ? 26.177  -4.102  4.464   1.00 83.26  ? 329 MET A SD    1 
ATOM   2652 C  CE    . MET A 1 357 ? 27.777  -3.365  4.798   1.00 69.92  ? 329 MET A CE    1 
ATOM   2653 N  N     . THR A 1 358 ? 25.040  -1.642  -0.058  1.00 71.77  ? 330 THR A N     1 
ATOM   2654 C  CA    . THR A 1 358 ? 23.873  -1.557  -0.931  1.00 67.25  ? 330 THR A CA    1 
ATOM   2655 C  C     . THR A 1 358 ? 24.156  -2.092  -2.327  1.00 66.29  ? 330 THR A C     1 
ATOM   2656 O  O     . THR A 1 358 ? 23.213  -2.345  -3.083  1.00 74.44  ? 330 THR A O     1 
ATOM   2657 C  CB    . THR A 1 358 ? 23.380  -0.111  -1.049  1.00 54.05  ? 330 THR A CB    1 
ATOM   2658 O  OG1   . THR A 1 358 ? 24.405  0.682   -1.657  1.00 50.45  ? 330 THR A OG1   1 
ATOM   2659 C  CG2   . THR A 1 358 ? 23.066  0.462   0.307   1.00 51.67  ? 330 THR A CG2   1 
ATOM   2660 N  N     . ARG A 1 359 ? 25.424  -2.240  -2.702  1.00 66.61  ? 331 ARG A N     1 
ATOM   2661 C  CA    . ARG A 1 359 ? 25.758  -2.823  -3.997  1.00 68.80  ? 331 ARG A CA    1 
ATOM   2662 C  C     . ARG A 1 359 ? 25.501  -4.328  -3.972  1.00 73.19  ? 331 ARG A C     1 
ATOM   2663 O  O     . ARG A 1 359 ? 25.766  -5.028  -4.950  1.00 81.41  ? 331 ARG A O     1 
ATOM   2664 C  CB    . ARG A 1 359 ? 27.219  -2.534  -4.377  1.00 71.87  ? 331 ARG A CB    1 
ATOM   2665 C  CG    . ARG A 1 359 ? 27.443  -1.206  -5.110  1.00 65.95  ? 331 ARG A CG    1 
ATOM   2666 C  CD    . ARG A 1 359 ? 28.930  -0.967  -5.412  1.00 59.65  ? 331 ARG A CD    1 
ATOM   2667 N  NE    . ARG A 1 359 ? 29.326  0.422   -5.188  1.00 55.23  ? 331 ARG A NE    1 
ATOM   2668 C  CZ    . ARG A 1 359 ? 30.417  0.805   -4.533  1.00 62.90  ? 331 ARG A CZ    1 
ATOM   2669 N  NH1   . ARG A 1 359 ? 31.274  -0.075  -4.037  1.00 61.61  ? 331 ARG A NH1   1 
ATOM   2670 N  NH2   . ARG A 1 359 ? 30.656  2.105   -4.369  1.00 56.01  ? 331 ARG A NH2   1 
ATOM   2671 N  N     . GLU A 1 366 ? 16.075  -13.538 -8.371  1.00 93.35  ? 338 GLU A N     1 
ATOM   2672 C  CA    . GLU A 1 366 ? 15.075  -13.148 -7.383  1.00 91.25  ? 338 GLU A CA    1 
ATOM   2673 C  C     . GLU A 1 366 ? 15.382  -13.745 -6.010  1.00 87.33  ? 338 GLU A C     1 
ATOM   2674 O  O     . GLU A 1 366 ? 15.541  -14.963 -5.870  1.00 83.51  ? 338 GLU A O     1 
ATOM   2675 C  CB    . GLU A 1 366 ? 13.676  -13.573 -7.842  1.00 90.88  ? 338 GLU A CB    1 
ATOM   2676 C  CG    . GLU A 1 366 ? 12.600  -13.445 -6.776  1.00 86.37  ? 338 GLU A CG    1 
ATOM   2677 C  CD    . GLU A 1 366 ? 11.967  -12.065 -6.749  1.00 97.05  ? 338 GLU A CD    1 
ATOM   2678 O  OE1   . GLU A 1 366 ? 12.342  -11.223 -7.592  1.00 94.41  ? 338 GLU A OE1   1 
ATOM   2679 O  OE2   . GLU A 1 366 ? 11.093  -11.820 -5.886  1.00 95.67  ? 338 GLU A OE2   1 
ATOM   2680 N  N     . ILE A 1 367 ? 15.470  -12.873 -5.001  1.00 82.42  ? 339 ILE A N     1 
ATOM   2681 C  CA    . ILE A 1 367 ? 15.688  -13.337 -3.633  1.00 75.35  ? 339 ILE A CA    1 
ATOM   2682 C  C     . ILE A 1 367 ? 14.566  -14.275 -3.202  1.00 73.20  ? 339 ILE A C     1 
ATOM   2683 O  O     . ILE A 1 367 ? 14.812  -15.313 -2.579  1.00 66.73  ? 339 ILE A O     1 
ATOM   2684 C  CB    . ILE A 1 367 ? 15.825  -12.139 -2.672  1.00 77.61  ? 339 ILE A CB    1 
ATOM   2685 C  CG1   . ILE A 1 367 ? 16.728  -11.060 -3.274  1.00 81.29  ? 339 ILE A CG1   1 
ATOM   2686 C  CG2   . ILE A 1 367 ? 16.365  -12.596 -1.324  1.00 72.31  ? 339 ILE A CG2   1 
ATOM   2687 C  CD1   . ILE A 1 367 ? 17.176  -9.995  -2.274  1.00 74.13  ? 339 ILE A CD1   1 
ATOM   2688 N  N     . ALA A 1 368 ? 13.317  -13.936 -3.542  1.00 73.79  ? 340 ALA A N     1 
ATOM   2689 C  CA    . ALA A 1 368 ? 12.184  -14.745 -3.100  1.00 68.33  ? 340 ALA A CA    1 
ATOM   2690 C  C     . ALA A 1 368 ? 12.269  -16.174 -3.619  1.00 68.78  ? 340 ALA A C     1 
ATOM   2691 O  O     . ALA A 1 368 ? 11.820  -17.108 -2.942  1.00 63.47  ? 340 ALA A O     1 
ATOM   2692 C  CB    . ALA A 1 368 ? 10.869  -14.097 -3.540  1.00 73.67  ? 340 ALA A CB    1 
ATOM   2693 N  N     . ARG A 1 369 ? 12.840  -16.370 -4.810  1.00 73.32  ? 341 ARG A N     1 
ATOM   2694 C  CA    . ARG A 1 369 ? 13.021  -17.725 -5.317  1.00 76.20  ? 341 ARG A CA    1 
ATOM   2695 C  C     . ARG A 1 369 ? 14.065  -18.478 -4.497  1.00 72.10  ? 341 ARG A C     1 
ATOM   2696 O  O     . ARG A 1 369 ? 13.874  -19.657 -4.166  1.00 66.81  ? 341 ARG A O     1 
ATOM   2697 C  CB    . ARG A 1 369 ? 13.412  -17.680 -6.795  1.00 79.73  ? 341 ARG A CB    1 
ATOM   2698 C  CG    . ARG A 1 369 ? 12.725  -18.733 -7.649  1.00 85.33  ? 341 ARG A CG    1 
ATOM   2699 C  CD    . ARG A 1 369 ? 13.697  -19.799 -8.131  1.00 92.71  ? 341 ARG A CD    1 
ATOM   2700 N  NE    . ARG A 1 369 ? 13.034  -20.782 -8.979  1.00 105.04 ? 341 ARG A NE    1 
ATOM   2701 C  CZ    . ARG A 1 369 ? 13.633  -21.831 -9.529  1.00 108.47 ? 341 ARG A CZ    1 
ATOM   2702 N  NH1   . ARG A 1 369 ? 14.918  -22.075 -9.332  1.00 109.53 ? 341 ARG A NH1   1 
ATOM   2703 N  NH2   . ARG A 1 369 ? 12.923  -22.656 -10.294 1.00 110.11 ? 341 ARG A NH2   1 
ATOM   2704 N  N     . ASN A 1 370 ? 15.165  -17.803 -4.143  1.00 67.21  ? 342 ASN A N     1 
ATOM   2705 C  CA    . ASN A 1 370 ? 16.192  -18.412 -3.300  1.00 66.57  ? 342 ASN A CA    1 
ATOM   2706 C  C     . ASN A 1 370 ? 15.644  -18.757 -1.918  1.00 66.69  ? 342 ASN A C     1 
ATOM   2707 O  O     . ASN A 1 370 ? 15.977  -19.809 -1.354  1.00 61.11  ? 342 ASN A O     1 
ATOM   2708 C  CB    . ASN A 1 370 ? 17.390  -17.461 -3.180  1.00 68.04  ? 342 ASN A CB    1 
ATOM   2709 C  CG    . ASN A 1 370 ? 18.269  -17.759 -1.963  1.00 75.96  ? 342 ASN A CG    1 
ATOM   2710 O  OD1   . ASN A 1 370 ? 18.604  -18.915 -1.688  1.00 75.19  ? 342 ASN A OD1   1 
ATOM   2711 N  ND2   . ASN A 1 370 ? 18.643  -16.709 -1.229  1.00 65.19  ? 342 ASN A ND2   1 
ATOM   2712 N  N     . ILE A 1 371 ? 14.813  -17.877 -1.351  1.00 61.08  ? 343 ILE A N     1 
ATOM   2713 C  CA    . ILE A 1 371 ? 14.286  -18.108 -0.007  1.00 54.52  ? 343 ILE A CA    1 
ATOM   2714 C  C     . ILE A 1 371 ? 13.440  -19.372 0.019   1.00 50.81  ? 343 ILE A C     1 
ATOM   2715 O  O     . ILE A 1 371 ? 13.616  -20.242 0.882   1.00 55.05  ? 343 ILE A O     1 
ATOM   2716 C  CB    . ILE A 1 371 ? 13.483  -16.885 0.477   1.00 54.27  ? 343 ILE A CB    1 
ATOM   2717 C  CG1   . ILE A 1 371 ? 14.404  -15.670 0.635   1.00 55.42  ? 343 ILE A CG1   1 
ATOM   2718 C  CG2   . ILE A 1 371 ? 12.752  -17.213 1.775   1.00 45.82  ? 343 ILE A CG2   1 
ATOM   2719 C  CD1   . ILE A 1 371 ? 13.693  -14.408 1.078   1.00 59.86  ? 343 ILE A CD1   1 
ATOM   2720 N  N     . GLY A 1 372 ? 12.517  -19.498 -0.940  1.00 58.42  ? 344 GLY A N     1 
ATOM   2721 C  CA    . GLY A 1 372 ? 11.640  -20.657 -0.960  1.00 58.22  ? 344 GLY A CA    1 
ATOM   2722 C  C     . GLY A 1 372 ? 12.390  -21.971 -1.070  1.00 60.34  ? 344 GLY A C     1 
ATOM   2723 O  O     . GLY A 1 372 ? 12.054  -22.946 -0.390  1.00 57.05  ? 344 GLY A O     1 
ATOM   2724 N  N     . HIS A 1 373 ? 13.425  -22.015 -1.919  1.00 56.01  ? 345 HIS A N     1 
ATOM   2725 C  CA    . HIS A 1 373 ? 14.181  -23.254 -2.090  1.00 57.89  ? 345 HIS A CA    1 
ATOM   2726 C  C     . HIS A 1 373 ? 14.967  -23.614 -0.835  1.00 60.68  ? 345 HIS A C     1 
ATOM   2727 O  O     . HIS A 1 373 ? 14.982  -24.779 -0.423  1.00 60.93  ? 345 HIS A O     1 
ATOM   2728 C  CB    . HIS A 1 373 ? 15.133  -23.150 -3.277  1.00 61.05  ? 345 HIS A CB    1 
ATOM   2729 C  CG    . HIS A 1 373 ? 15.858  -24.429 -3.562  1.00 81.84  ? 345 HIS A CG    1 
ATOM   2730 N  ND1   . HIS A 1 373 ? 17.210  -24.581 -3.342  1.00 79.02  ? 345 HIS A ND1   1 
ATOM   2731 C  CD2   . HIS A 1 373 ? 15.415  -25.622 -4.026  1.00 85.12  ? 345 HIS A CD2   1 
ATOM   2732 C  CE1   . HIS A 1 373 ? 17.570  -25.811 -3.665  1.00 84.77  ? 345 HIS A CE1   1 
ATOM   2733 N  NE2   . HIS A 1 373 ? 16.500  -26.463 -4.083  1.00 81.71  ? 345 HIS A NE2   1 
ATOM   2734 N  N     . TYR A 1 374 ? 15.636  -22.632 -0.222  1.00 53.85  ? 346 TYR A N     1 
ATOM   2735 C  CA    . TYR A 1 374 ? 16.388  -22.893 1.003   1.00 52.96  ? 346 TYR A CA    1 
ATOM   2736 C  C     . TYR A 1 374 ? 15.466  -23.350 2.129   1.00 55.89  ? 346 TYR A C     1 
ATOM   2737 O  O     . TYR A 1 374 ? 15.756  -24.328 2.829   1.00 54.73  ? 346 TYR A O     1 
ATOM   2738 C  CB    . TYR A 1 374 ? 17.175  -21.638 1.405   1.00 48.65  ? 346 TYR A CB    1 
ATOM   2739 C  CG    . TYR A 1 374 ? 17.950  -21.736 2.717   1.00 41.66  ? 346 TYR A CG    1 
ATOM   2740 C  CD1   . TYR A 1 374 ? 17.333  -21.477 3.936   1.00 44.51  ? 346 TYR A CD1   1 
ATOM   2741 C  CD2   . TYR A 1 374 ? 19.296  -22.088 2.728   1.00 42.39  ? 346 TYR A CD2   1 
ATOM   2742 C  CE1   . TYR A 1 374 ? 18.036  -21.558 5.130   1.00 39.56  ? 346 TYR A CE1   1 
ATOM   2743 C  CE2   . TYR A 1 374 ? 20.014  -22.174 3.909   1.00 40.77  ? 346 TYR A CE2   1 
ATOM   2744 C  CZ    . TYR A 1 374 ? 19.379  -21.908 5.112   1.00 39.48  ? 346 TYR A CZ    1 
ATOM   2745 O  OH    . TYR A 1 374 ? 20.097  -21.995 6.286   1.00 37.85  ? 346 TYR A OH    1 
ATOM   2746 N  N     . LEU A 1 375 ? 14.348  -22.643 2.326   1.00 52.50  ? 347 LEU A N     1 
ATOM   2747 C  CA    . LEU A 1 375 ? 13.421  -23.011 3.389   1.00 53.90  ? 347 LEU A CA    1 
ATOM   2748 C  C     . LEU A 1 375 ? 12.764  -24.358 3.121   1.00 66.44  ? 347 LEU A C     1 
ATOM   2749 O  O     . LEU A 1 375 ? 12.421  -25.081 4.065   1.00 61.97  ? 347 LEU A O     1 
ATOM   2750 C  CB    . LEU A 1 375 ? 12.354  -21.929 3.548   1.00 53.93  ? 347 LEU A CB    1 
ATOM   2751 C  CG    . LEU A 1 375 ? 12.831  -20.664 4.250   1.00 49.88  ? 347 LEU A CG    1 
ATOM   2752 C  CD1   . LEU A 1 375 ? 11.633  -19.814 4.588   1.00 43.13  ? 347 LEU A CD1   1 
ATOM   2753 C  CD2   . LEU A 1 375 ? 13.603  -21.017 5.512   1.00 48.94  ? 347 LEU A CD2   1 
ATOM   2754 N  N     . GLU A 1 376 ? 12.574  -24.703 1.847   1.00 66.06  ? 348 GLU A N     1 
ATOM   2755 C  CA    . GLU A 1 376 ? 11.964  -25.983 1.504   1.00 71.84  ? 348 GLU A CA    1 
ATOM   2756 C  C     . GLU A 1 376 ? 12.810  -27.146 2.010   1.00 80.81  ? 348 GLU A C     1 
ATOM   2757 O  O     . GLU A 1 376 ? 12.296  -28.077 2.644   1.00 81.00  ? 348 GLU A O     1 
ATOM   2758 C  CB    . GLU A 1 376 ? 11.770  -26.071 -0.009  1.00 69.32  ? 348 GLU A CB    1 
ATOM   2759 C  CG    . GLU A 1 376 ? 10.990  -27.285 -0.459  1.00 80.27  ? 348 GLU A CG    1 
ATOM   2760 C  CD    . GLU A 1 376 ? 9.657   -27.399 0.251   1.00 88.54  ? 348 GLU A CD    1 
ATOM   2761 O  OE1   . GLU A 1 376 ? 8.955   -26.370 0.361   1.00 87.96  ? 348 GLU A OE1   1 
ATOM   2762 O  OE2   . GLU A 1 376 ? 9.315   -28.513 0.704   1.00 98.00  ? 348 GLU A OE2   1 
ATOM   2763 N  N     . ARG A 1 377 ? 14.119  -27.095 1.763   1.00 76.95  ? 349 ARG A N     1 
ATOM   2764 C  CA    . ARG A 1 377 ? 15.009  -28.215 2.062   1.00 80.91  ? 349 ARG A CA    1 
ATOM   2765 C  C     . ARG A 1 377 ? 15.808  -27.929 3.334   1.00 83.64  ? 349 ARG A C     1 
ATOM   2766 O  O     . ARG A 1 377 ? 17.010  -27.658 3.310   1.00 86.76  ? 349 ARG A O     1 
ATOM   2767 C  CB    . ARG A 1 377 ? 15.927  -28.487 0.873   1.00 77.40  ? 349 ARG A CB    1 
ATOM   2768 N  N     . VAL A 1 378 ? 15.112  -28.009 4.466   1.00 84.20  ? 350 VAL A N     1 
ATOM   2769 C  CA    . VAL A 1 378 ? 15.755  -27.823 5.765   1.00 85.90  ? 350 VAL A CA    1 
ATOM   2770 C  C     . VAL A 1 378 ? 15.118  -28.716 6.822   1.00 96.07  ? 350 VAL A C     1 
ATOM   2771 O  O     . VAL A 1 378 ? 15.681  -28.914 7.900   1.00 97.81  ? 350 VAL A O     1 
ATOM   2772 C  CB    . VAL A 1 378 ? 15.707  -26.349 6.207   1.00 83.13  ? 350 VAL A CB    1 
HETATM 2773 N  N1    . FAD B 2 .   ? 21.407  9.255   47.755  1.00 44.18  ? 401 FAD A N1    1 
HETATM 2774 C  C2    . FAD B 2 .   ? 21.004  10.481  48.234  1.00 50.54  ? 401 FAD A C2    1 
HETATM 2775 O  O2    . FAD B 2 .   ? 21.832  11.363  48.446  1.00 46.52  ? 401 FAD A O2    1 
HETATM 2776 N  N3    . FAD B 2 .   ? 19.667  10.740  48.481  1.00 39.55  ? 401 FAD A N3    1 
HETATM 2777 C  C4    . FAD B 2 .   ? 18.717  9.777   48.246  1.00 43.50  ? 401 FAD A C4    1 
HETATM 2778 O  O4    . FAD B 2 .   ? 17.540  10.051  48.501  1.00 38.31  ? 401 FAD A O4    1 
HETATM 2779 C  C4X   . FAD B 2 .   ? 19.116  8.533   47.754  1.00 39.61  ? 401 FAD A C4X   1 
HETATM 2780 N  N5    . FAD B 2 .   ? 18.199  7.544   47.523  1.00 37.76  ? 401 FAD A N5    1 
HETATM 2781 C  C5X   . FAD B 2 .   ? 18.595  6.315   47.030  1.00 38.05  ? 401 FAD A C5X   1 
HETATM 2782 C  C6    . FAD B 2 .   ? 17.638  5.335   46.777  1.00 40.48  ? 401 FAD A C6    1 
HETATM 2783 C  C7    . FAD B 2 .   ? 18.029  4.093   46.297  1.00 44.15  ? 401 FAD A C7    1 
HETATM 2784 C  C7M   . FAD B 2 .   ? 17.015  3.018   46.022  1.00 40.70  ? 401 FAD A C7M   1 
HETATM 2785 C  C8    . FAD B 2 .   ? 19.374  3.833   46.059  1.00 47.05  ? 401 FAD A C8    1 
HETATM 2786 C  C8M   . FAD B 2 .   ? 19.773  2.485   45.537  1.00 48.72  ? 401 FAD A C8M   1 
HETATM 2787 C  C9    . FAD B 2 .   ? 20.334  4.813   46.306  1.00 41.93  ? 401 FAD A C9    1 
HETATM 2788 C  C9A   . FAD B 2 .   ? 19.944  6.055   46.786  1.00 46.00  ? 401 FAD A C9A   1 
HETATM 2789 N  N10   . FAD B 2 .   ? 20.880  7.042   47.023  1.00 43.56  ? 401 FAD A N10   1 
HETATM 2790 C  C10   . FAD B 2 .   ? 20.473  8.271   47.517  1.00 40.61  ? 401 FAD A C10   1 
HETATM 2791 C  "C1'" . FAD B 2 .   ? 22.347  6.755   46.801  1.00 52.06  ? 401 FAD A "C1'" 1 
HETATM 2792 C  "C2'" . FAD B 2 .   ? 22.958  7.414   45.586  1.00 51.60  ? 401 FAD A "C2'" 1 
HETATM 2793 O  "O2'" . FAD B 2 .   ? 22.653  6.606   44.476  1.00 52.09  ? 401 FAD A "O2'" 1 
HETATM 2794 C  "C3'" . FAD B 2 .   ? 24.469  7.501   45.804  1.00 59.38  ? 401 FAD A "C3'" 1 
HETATM 2795 O  "O3'" . FAD B 2 .   ? 25.016  6.237   46.118  1.00 54.09  ? 401 FAD A "O3'" 1 
HETATM 2796 C  "C4'" . FAD B 2 .   ? 24.790  8.410   46.983  1.00 60.88  ? 401 FAD A "C4'" 1 
HETATM 2797 O  "O4'" . FAD B 2 .   ? 24.254  9.705   46.769  1.00 57.20  ? 401 FAD A "O4'" 1 
HETATM 2798 C  "C5'" . FAD B 2 .   ? 26.305  8.474   47.147  1.00 74.09  ? 401 FAD A "C5'" 1 
HETATM 2799 O  "O5'" . FAD B 2 .   ? 26.820  9.394   46.213  1.00 73.81  ? 401 FAD A "O5'" 1 
HETATM 2800 P  P     . FAD B 2 .   ? 28.392  9.760   46.182  1.00 108.28 ? 401 FAD A P     1 
HETATM 2801 O  O1P   . FAD B 2 .   ? 28.995  9.171   44.925  1.00 93.97  ? 401 FAD A O1P   1 
HETATM 2802 O  O2P   . FAD B 2 .   ? 28.533  11.266  46.180  1.00 95.40  ? 401 FAD A O2P   1 
HETATM 2803 O  O3P   . FAD B 2 .   ? 29.093  9.180   47.393  1.00 81.74  ? 401 FAD A O3P   1 
HETATM 2804 CA CA    . CA  C 3 .   ? 13.069  14.012  -11.462 1.00 33.85  ? 402 CA  A CA    1 
HETATM 2805 CA CA    . CA  D 3 .   ? 6.330   -7.337  3.984   1.00 52.89  ? 403 CA  A CA    1 
HETATM 2806 O  O     . HOH E 4 .   ? 14.588  -22.375 13.234  0.78 64.79  ? 501 HOH A O     1 
HETATM 2807 O  O     . HOH E 4 .   ? 5.151   5.897   25.332  1.00 68.91  ? 502 HOH A O     1 
HETATM 2808 O  O     . HOH E 4 .   ? 29.909  4.863   -0.831  1.00 65.79  ? 503 HOH A O     1 
HETATM 2809 O  O     . HOH E 4 .   ? 13.448  -9.490  -8.136  1.00 98.58  ? 504 HOH A O     1 
HETATM 2810 O  O     . HOH E 4 .   ? -2.781  2.513   21.190  1.00 66.19  ? 505 HOH A O     1 
HETATM 2811 O  O     . HOH E 4 .   ? -4.889  6.220   2.641   1.00 34.47  ? 506 HOH A O     1 
HETATM 2812 O  O     . HOH E 4 .   ? 18.460  -21.086 -2.075  1.00 59.99  ? 507 HOH A O     1 
HETATM 2813 O  O     . HOH E 4 .   ? 22.966  -3.729  1.363   1.00 68.95  ? 508 HOH A O     1 
HETATM 2814 O  O     . HOH E 4 .   ? 10.953  17.311  14.079  1.00 56.78  ? 509 HOH A O     1 
HETATM 2815 O  O     . HOH E 4 .   ? -2.676  2.051   17.595  1.00 46.85  ? 510 HOH A O     1 
HETATM 2816 O  O     . HOH E 4 .   ? 27.226  0.459   9.583   1.00 57.02  ? 511 HOH A O     1 
HETATM 2817 O  O     . HOH E 4 .   ? -0.056  6.365   -8.519  1.00 63.10  ? 512 HOH A O     1 
HETATM 2818 O  O     . HOH E 4 .   ? -5.367  11.445  1.676   1.00 44.42  ? 513 HOH A O     1 
HETATM 2819 O  O     . HOH E 4 .   ? 21.462  13.836  48.506  1.00 57.33  ? 514 HOH A O     1 
HETATM 2820 O  O     . HOH E 4 .   ? 24.957  16.391  2.468   1.00 52.93  ? 515 HOH A O     1 
HETATM 2821 O  O     . HOH E 4 .   ? 18.218  -20.454 13.944  1.00 50.07  ? 516 HOH A O     1 
HETATM 2822 O  O     . HOH E 4 .   ? 24.252  2.330   15.526  1.00 59.76  ? 517 HOH A O     1 
HETATM 2823 O  O     . HOH E 4 .   ? 30.115  4.835   1.157   1.00 65.83  ? 518 HOH A O     1 
HETATM 2824 O  O     . HOH E 4 .   ? 10.894  -2.389  1.839   1.00 42.32  ? 519 HOH A O     1 
HETATM 2825 O  O     . HOH E 4 .   ? 3.736   -2.464  -1.994  1.00 46.20  ? 520 HOH A O     1 
HETATM 2826 O  O     . HOH E 4 .   ? -7.864  15.044  21.924  1.00 59.34  ? 521 HOH A O     1 
HETATM 2827 O  O     . HOH E 4 .   ? 27.952  13.439  44.882  1.00 83.72  ? 522 HOH A O     1 
HETATM 2828 O  O     . HOH E 4 .   ? 4.786   -5.400  4.602   1.00 36.24  ? 523 HOH A O     1 
HETATM 2829 O  O     . HOH E 4 .   ? 13.448  -23.805 11.490  0.68 65.63  ? 524 HOH A O     1 
HETATM 2830 O  O     . HOH E 4 .   ? 7.167   -9.190  2.785   1.00 40.17  ? 525 HOH A O     1 
HETATM 2831 O  O     . HOH E 4 .   ? 27.724  14.172  -0.587  1.00 44.08  ? 526 HOH A O     1 
HETATM 2832 O  O     . HOH E 4 .   ? 23.942  16.665  49.851  1.00 57.85  ? 527 HOH A O     1 
HETATM 2833 O  O     . HOH E 4 .   ? 16.171  17.848  16.542  1.00 73.22  ? 528 HOH A O     1 
HETATM 2834 O  O     . HOH E 4 .   ? 8.569   8.128   33.154  1.00 54.04  ? 529 HOH A O     1 
HETATM 2835 O  O     . HOH E 4 .   ? 15.272  -7.713  55.788  1.00 63.20  ? 530 HOH A O     1 
HETATM 2836 O  O     . HOH E 4 .   ? -3.419  -10.131 44.709  1.00 47.15  ? 531 HOH A O     1 
HETATM 2837 O  O     . HOH E 4 .   ? -0.442  13.413  9.779   1.00 53.62  ? 532 HOH A O     1 
HETATM 2838 O  O     . HOH E 4 .   ? 13.257  10.257  -14.171 1.00 33.49  ? 533 HOH A O     1 
HETATM 2839 O  O     . HOH E 4 .   ? 29.632  -12.996 13.924  1.00 46.93  ? 534 HOH A O     1 
HETATM 2840 O  O     . HOH E 4 .   ? 21.587  -15.956 2.301   1.00 43.79  ? 535 HOH A O     1 
HETATM 2841 O  O     . HOH E 4 .   ? 6.069   17.001  -9.876  1.00 63.56  ? 536 HOH A O     1 
HETATM 2842 O  O     . HOH E 4 .   ? 16.525  16.030  -6.341  1.00 47.88  ? 537 HOH A O     1 
HETATM 2843 O  O     . HOH E 4 .   ? 32.697  2.151   -2.556  1.00 61.34  ? 538 HOH A O     1 
HETATM 2844 O  O     . HOH E 4 .   ? 23.458  15.860  57.188  1.00 41.14  ? 539 HOH A O     1 
HETATM 2845 O  O     . HOH E 4 .   ? 21.972  -6.666  4.780   1.00 36.76  ? 540 HOH A O     1 
HETATM 2846 O  O     . HOH E 4 .   ? 16.325  6.401   56.896  1.00 41.73  ? 541 HOH A O     1 
HETATM 2847 O  O     . HOH E 4 .   ? 8.483   -4.122  32.526  1.00 67.04  ? 542 HOH A O     1 
HETATM 2848 O  O     . HOH E 4 .   ? 20.245  11.756  59.084  1.00 42.83  ? 543 HOH A O     1 
HETATM 2849 O  O     . HOH E 4 .   ? 2.889   -5.254  6.821   1.00 38.33  ? 544 HOH A O     1 
HETATM 2850 O  O     . HOH E 4 .   ? -4.855  16.662  22.072  1.00 51.69  ? 545 HOH A O     1 
HETATM 2851 O  O     . HOH E 4 .   ? 15.809  21.663  48.013  1.00 55.36  ? 546 HOH A O     1 
HETATM 2852 O  O     . HOH E 4 .   ? 5.344   -6.998  0.965   1.00 48.54  ? 547 HOH A O     1 
HETATM 2853 O  O     . HOH E 4 .   ? 16.067  17.557  54.653  1.00 41.50  ? 548 HOH A O     1 
HETATM 2854 O  O     . HOH E 4 .   ? 24.191  -9.285  14.153  1.00 40.64  ? 549 HOH A O     1 
HETATM 2855 O  O     . HOH E 4 .   ? 9.462   12.931  1.355   1.00 34.12  ? 550 HOH A O     1 
HETATM 2856 O  O     . HOH E 4 .   ? 13.899  -12.313 4.157   1.00 35.05  ? 551 HOH A O     1 
HETATM 2857 O  O     . HOH E 4 .   ? 8.536   17.628  -8.903  1.00 69.50  ? 552 HOH A O     1 
HETATM 2858 O  O     . HOH E 4 .   ? 15.387  11.541  57.831  1.00 35.59  ? 553 HOH A O     1 
HETATM 2859 O  O     . HOH E 4 .   ? 5.639   12.860  42.447  1.00 43.24  ? 554 HOH A O     1 
HETATM 2860 O  O     . HOH E 4 .   ? 18.470  -6.624  1.983   1.00 47.70  ? 555 HOH A O     1 
HETATM 2861 O  O     . HOH E 4 .   ? 9.883   -4.793  61.764  1.00 63.43  ? 556 HOH A O     1 
HETATM 2862 O  O     . HOH E 4 .   ? 20.840  15.561  9.478   1.00 48.78  ? 557 HOH A O     1 
HETATM 2863 O  O     . HOH E 4 .   ? -3.221  -9.829  58.912  1.00 49.67  ? 558 HOH A O     1 
HETATM 2864 O  O     . HOH E 4 .   ? 6.122   2.752   -5.497  1.00 52.26  ? 559 HOH A O     1 
HETATM 2865 O  O     . HOH E 4 .   ? 2.419   -6.994  57.671  1.00 45.34  ? 560 HOH A O     1 
HETATM 2866 O  O     . HOH E 4 .   ? 18.404  11.336  16.065  1.00 42.12  ? 561 HOH A O     1 
HETATM 2867 O  O     . HOH E 4 .   ? 29.265  10.323  57.449  1.00 57.35  ? 562 HOH A O     1 
HETATM 2868 O  O     . HOH E 4 .   ? 13.976  5.523   -14.153 1.00 44.98  ? 563 HOH A O     1 
HETATM 2869 O  O     . HOH E 4 .   ? 6.074   -5.099  62.393  1.00 51.64  ? 564 HOH A O     1 
HETATM 2870 O  O     . HOH E 4 .   ? 26.990  11.916  -4.060  1.00 42.43  ? 565 HOH A O     1 
HETATM 2871 O  O     . HOH E 4 .   ? 14.452  -6.884  53.404  1.00 58.10  ? 566 HOH A O     1 
HETATM 2872 O  O     . HOH E 4 .   ? 22.003  9.501   58.957  1.00 40.27  ? 567 HOH A O     1 
HETATM 2873 O  O     . HOH E 4 .   ? 16.062  -2.759  56.688  1.00 46.57  ? 568 HOH A O     1 
HETATM 2874 O  O     . HOH E 4 .   ? 8.437   -9.445  -0.638  1.00 57.53  ? 569 HOH A O     1 
HETATM 2875 O  O     . HOH E 4 .   ? 7.444   -0.812  4.541   1.00 52.79  ? 570 HOH A O     1 
HETATM 2876 O  O     . HOH E 4 .   ? 11.774  15.315  -10.012 1.00 37.86  ? 571 HOH A O     1 
HETATM 2877 O  O     . HOH E 4 .   ? 2.444   12.498  45.015  1.00 61.18  ? 572 HOH A O     1 
HETATM 2878 O  O     . HOH E 4 .   ? 15.885  -4.838  20.968  1.00 49.03  ? 573 HOH A O     1 
HETATM 2879 O  O     . HOH E 4 .   ? 3.470   -20.956 10.113  1.00 57.05  ? 574 HOH A O     1 
HETATM 2880 O  O     . HOH E 4 .   ? 27.215  9.208   10.752  1.00 61.22  ? 575 HOH A O     1 
HETATM 2881 O  O     . HOH E 4 .   ? 28.384  7.418   2.315   1.00 40.85  ? 576 HOH A O     1 
HETATM 2882 O  O     . HOH E 4 .   ? 24.417  -12.676 3.242   1.00 40.32  ? 577 HOH A O     1 
HETATM 2883 O  O     . HOH E 4 .   ? 5.364   -17.289 -0.580  1.00 60.54  ? 578 HOH A O     1 
HETATM 2884 O  O     . HOH E 4 .   ? 12.383  15.781  -6.205  1.00 41.12  ? 579 HOH A O     1 
HETATM 2885 O  O     . HOH E 4 .   ? 11.867  -0.259  58.494  1.00 49.39  ? 580 HOH A O     1 
HETATM 2886 O  O     . HOH E 4 .   ? 3.864   13.308  35.756  1.00 49.04  ? 581 HOH A O     1 
HETATM 2887 O  O     . HOH E 4 .   ? 3.259   18.904  37.430  1.00 62.02  ? 582 HOH A O     1 
HETATM 2888 O  O     . HOH E 4 .   ? 12.081  3.434   20.475  1.00 52.45  ? 583 HOH A O     1 
HETATM 2889 O  O     . HOH E 4 .   ? 7.441   14.371  57.516  1.00 42.09  ? 584 HOH A O     1 
HETATM 2890 O  O     . HOH E 4 .   ? 15.592  11.829  16.370  1.00 43.74  ? 585 HOH A O     1 
HETATM 2891 O  O     . HOH E 4 .   ? 17.714  -9.434  55.441  1.00 62.07  ? 586 HOH A O     1 
HETATM 2892 O  O     . HOH E 4 .   ? 27.492  3.807   13.737  1.00 59.94  ? 587 HOH A O     1 
HETATM 2893 O  O     . HOH E 4 .   ? -2.356  -3.245  62.342  1.00 47.17  ? 588 HOH A O     1 
HETATM 2894 O  O     . HOH E 4 .   ? 19.090  -7.270  4.238   1.00 36.68  ? 589 HOH A O     1 
HETATM 2895 O  O     . HOH E 4 .   ? 10.695  24.059  52.583  1.00 72.56  ? 590 HOH A O     1 
HETATM 2896 O  O     . HOH E 4 .   ? 0.914   22.969  15.374  1.00 52.78  ? 591 HOH A O     1 
HETATM 2897 O  O     . HOH E 4 .   ? 22.510  17.054  0.657   1.00 58.29  ? 592 HOH A O     1 
HETATM 2898 O  O     . HOH E 4 .   ? 10.021  2.914   59.462  1.00 45.96  ? 593 HOH A O     1 
HETATM 2899 O  O     . HOH E 4 .   ? 14.279  -14.618 18.638  1.00 48.79  ? 594 HOH A O     1 
HETATM 2900 O  O     . HOH E 4 .   ? 2.755   -24.663 13.184  1.00 53.60  ? 595 HOH A O     1 
HETATM 2901 O  O     . HOH E 4 .   ? 28.914  4.645   3.073   1.00 56.56  ? 596 HOH A O     1 
HETATM 2902 O  O     . HOH E 4 .   ? 10.952  7.016   33.486  1.00 55.02  ? 597 HOH A O     1 
HETATM 2903 O  O     . HOH E 4 .   ? -0.237  -6.489  12.572  1.00 34.03  ? 598 HOH A O     1 
HETATM 2904 O  O     . HOH E 4 .   ? 32.185  2.449   0.432   1.00 63.69  ? 599 HOH A O     1 
HETATM 2905 O  O     . HOH E 4 .   ? 15.042  13.580  -12.965 1.00 39.96  ? 600 HOH A O     1 
HETATM 2906 O  O     . HOH E 4 .   ? 9.998   -0.409  3.427   1.00 47.12  ? 601 HOH A O     1 
HETATM 2907 O  O     . HOH E 4 .   ? 14.176  16.176  61.139  1.00 39.60  ? 602 HOH A O     1 
HETATM 2908 O  O     . HOH E 4 .   ? 13.064  -10.883 44.456  1.00 76.06  ? 603 HOH A O     1 
HETATM 2909 O  O     . HOH E 4 .   ? 22.561  -5.598  2.386   1.00 52.67  ? 604 HOH A O     1 
HETATM 2910 O  O     . HOH E 4 .   ? 25.202  -11.635 14.998  1.00 46.33  ? 605 HOH A O     1 
HETATM 2911 O  O     . HOH E 4 .   ? 30.416  12.230  55.804  1.00 62.69  ? 606 HOH A O     1 
HETATM 2912 O  O     . HOH E 4 .   ? -0.125  23.768  38.216  1.00 86.15  ? 607 HOH A O     1 
HETATM 2913 O  O     . HOH E 4 .   ? 0.000   -0.000  17.860  0.50 60.46  ? 608 HOH A O     1 
HETATM 2914 O  O     . HOH E 4 .   ? 0.938   -21.796 10.475  1.00 59.91  ? 609 HOH A O     1 
HETATM 2915 O  O     . HOH E 4 .   ? 3.695   1.823   -6.149  1.00 60.06  ? 610 HOH A O     1 
HETATM 2916 O  O     . HOH E 4 .   ? 18.653  -15.538 53.005  1.00 83.60  ? 611 HOH A O     1 
HETATM 2917 O  O     . HOH E 4 .   ? 17.481  -15.039 54.768  1.00 76.30  ? 612 HOH A O     1 
HETATM 2918 O  O     . HOH E 4 .   ? -0.000  -27.455 -1.701  0.50 82.86  ? 613 HOH A O     1 
# 
