data_9F1X
# 
_entry.id   9F1X 
# 
_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   9F1X         pdb_00009f1x 10.2210/pdb9f1x/pdb 
WWPDB D_1292138020 ?            ?                   
# 
_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                        9F1X 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-20 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              sofia.kapetanaki@aok.pte.hu 
_pdbx_contact_author.name_first         Sofia 
_pdbx_contact_author.name_last          Kapetanaki 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-1286-9929 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Kapetanaki, S.' 1 ? 
'Coquelle, N.'   2 ? 
'Weik, M.'       3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To be published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'SSX room temperature structure of Oscillatoria acuminata adenylyate cyclase.' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kapetanaki, S.' 1 ? 
primary 'Coquelle, N.'   2 ? 
primary 'Weik, M.'       3 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Family 3 adenylate cyclase' 44173.285 1  ? ? ? ? 
2 non-polymer syn 'FLAVIN MONONUCLEOTIDE'      456.344   1  ? ? ? ? 
3 non-polymer syn 'CALCIUM ION'                40.078    2  ? ? ? ? 
4 water       nat water                        18.015    92 ? ? ? ? 
# 
_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 MONONUCLEOTIDE' FMN 
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 
FMN non-polymer         . 'FLAVIN MONONUCLEOTIDE' 'RIBOFLAVIN MONOPHOSPHATE' 'C17 H21 N4 O9 P' 456.344 
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 365 337 337 LEU LEU A . n 
A 1 366 GLU 366 338 338 GLU GLU A . n 
A 1 367 ILE 367 339 339 ILE ILE A . n 
A 1 368 ALA 368 340 340 ALA ALA A . n 
A 1 369 ARG 369 341 341 ARG ARG A . n 
A 1 370 ASN 370 342 342 ASN ASN A . n 
A 1 371 ILE 371 343 343 ILE ILE A . n 
A 1 372 GLY 372 344 344 GLY GLY A . n 
A 1 373 HIS 373 345 345 HIS HIS A . n 
A 1 374 TYR 374 346 346 TYR TYR A . n 
A 1 375 LEU 375 347 347 LEU LEU A . n 
A 1 376 GLU 376 348 348 GLU GLU A . n 
A 1 377 ARG 377 349 349 ARG ARG A . n 
A 1 378 VAL 378 350 350 VAL VAL A . n 
A 1 379 GLY 379 351 ?   ?   ?   A . n 
A 1 380 ASP 380 352 ?   ?   ?   A . n 
A 1 381 ARG 381 353 ?   ?   ?   A . n 
A 1 382 GLN 382 354 ?   ?   ?   A . n 
A 1 383 PRO 383 355 ?   ?   ?   A . n 
A 1 384 SER 384 356 ?   ?   ?   A . n 
A 1 385 GLN 385 357 ?   ?   ?   A . n 
A 1 386 ILE 386 358 ?   ?   ?   A . n 
A 1 387 PHE 387 359 ?   ?   ?   A . n 
A 1 388 GLY 388 360 ?   ?   ?   A . n 
A 1 389 VAL 389 361 ?   ?   ?   A . n 
A 1 390 LYS 390 362 ?   ?   ?   A . n 
A 1 391 SER 391 363 ?   ?   ?   A . n 
A 1 392 LEU 392 364 ?   ?   ?   A . n 
A 1 393 PRO 393 365 ?   ?   ?   A . n 
A 1 394 LEU 394 366 ?   ?   ?   A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 FMN 1  401 401 FMN FMN A . 
C 3 CA  1  402 2   CA  CA  A . 
D 3 CA  1  403 3   CA  CA  A . 
E 4 HOH 1  501 68  HOH HOH A . 
E 4 HOH 2  502 90  HOH HOH A . 
E 4 HOH 3  503 82  HOH HOH A . 
E 4 HOH 4  504 85  HOH HOH A . 
E 4 HOH 5  505 25  HOH HOH A . 
E 4 HOH 6  506 21  HOH HOH A . 
E 4 HOH 7  507 43  HOH HOH A . 
E 4 HOH 8  508 71  HOH HOH A . 
E 4 HOH 9  509 64  HOH HOH A . 
E 4 HOH 10 510 44  HOH HOH A . 
E 4 HOH 11 511 45  HOH HOH A . 
E 4 HOH 12 512 59  HOH HOH A . 
E 4 HOH 13 513 50  HOH HOH A . 
E 4 HOH 14 514 61  HOH HOH A . 
E 4 HOH 15 515 3   HOH HOH A . 
E 4 HOH 16 516 77  HOH HOH A . 
E 4 HOH 17 517 8   HOH HOH A . 
E 4 HOH 18 518 53  HOH HOH A . 
E 4 HOH 19 519 13  HOH HOH A . 
E 4 HOH 20 520 19  HOH HOH A . 
E 4 HOH 21 521 4   HOH HOH A . 
E 4 HOH 22 522 69  HOH HOH A . 
E 4 HOH 23 523 10  HOH HOH A . 
E 4 HOH 24 524 27  HOH HOH A . 
E 4 HOH 25 525 26  HOH HOH A . 
E 4 HOH 26 526 38  HOH HOH A . 
E 4 HOH 27 527 5   HOH HOH A . 
E 4 HOH 28 528 11  HOH HOH A . 
E 4 HOH 29 529 54  HOH HOH A . 
E 4 HOH 30 530 34  HOH HOH A . 
E 4 HOH 31 531 7   HOH HOH A . 
E 4 HOH 32 532 32  HOH HOH A . 
E 4 HOH 33 533 42  HOH HOH A . 
E 4 HOH 34 534 6   HOH HOH A . 
E 4 HOH 35 535 74  HOH HOH A . 
E 4 HOH 36 536 24  HOH HOH A . 
E 4 HOH 37 537 75  HOH HOH A . 
E 4 HOH 38 538 18  HOH HOH A . 
E 4 HOH 39 539 16  HOH HOH A . 
E 4 HOH 40 540 37  HOH HOH A . 
E 4 HOH 41 541 30  HOH HOH A . 
E 4 HOH 42 542 84  HOH HOH A . 
E 4 HOH 43 543 88  HOH HOH A . 
E 4 HOH 44 544 41  HOH HOH A . 
E 4 HOH 45 545 55  HOH HOH A . 
E 4 HOH 46 546 12  HOH HOH A . 
E 4 HOH 47 547 15  HOH HOH A . 
E 4 HOH 48 548 36  HOH HOH A . 
E 4 HOH 49 549 49  HOH HOH A . 
E 4 HOH 50 550 31  HOH HOH A . 
E 4 HOH 51 551 33  HOH HOH A . 
E 4 HOH 52 552 76  HOH HOH A . 
E 4 HOH 53 553 35  HOH HOH A . 
E 4 HOH 54 554 67  HOH HOH A . 
E 4 HOH 55 555 23  HOH HOH A . 
E 4 HOH 56 556 51  HOH HOH A . 
E 4 HOH 57 557 9   HOH HOH A . 
E 4 HOH 58 558 63  HOH HOH A . 
E 4 HOH 59 559 58  HOH HOH A . 
E 4 HOH 60 560 73  HOH HOH A . 
E 4 HOH 61 561 39  HOH HOH A . 
E 4 HOH 62 562 20  HOH HOH A . 
E 4 HOH 63 563 48  HOH HOH A . 
E 4 HOH 64 564 78  HOH HOH A . 
E 4 HOH 65 565 83  HOH HOH A . 
E 4 HOH 66 566 17  HOH HOH A . 
E 4 HOH 67 567 28  HOH HOH A . 
E 4 HOH 68 568 46  HOH HOH A . 
E 4 HOH 69 569 72  HOH HOH A . 
E 4 HOH 70 570 1   HOH HOH A . 
E 4 HOH 71 571 14  HOH HOH A . 
E 4 HOH 72 572 91  HOH HOH A . 
E 4 HOH 73 573 22  HOH HOH A . 
E 4 HOH 74 574 60  HOH HOH A . 
E 4 HOH 75 575 40  HOH HOH A . 
E 4 HOH 76 576 29  HOH HOH A . 
E 4 HOH 77 577 62  HOH HOH A . 
E 4 HOH 78 578 70  HOH HOH A . 
E 4 HOH 79 579 89  HOH HOH A . 
E 4 HOH 80 580 57  HOH HOH A . 
E 4 HOH 81 581 81  HOH HOH A . 
E 4 HOH 82 582 2   HOH HOH A . 
E 4 HOH 83 583 56  HOH HOH A . 
E 4 HOH 84 584 92  HOH HOH A . 
E 4 HOH 85 585 52  HOH HOH A . 
E 4 HOH 86 586 79  HOH HOH A . 
E 4 HOH 87 587 87  HOH HOH A . 
E 4 HOH 88 588 80  HOH HOH A . 
E 4 HOH 89 589 65  HOH HOH A . 
E 4 HOH 90 590 66  HOH HOH A . 
E 4 HOH 91 591 47  HOH HOH A . 
E 4 HOH 92 592 86  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 260 ? CG  ? A GLU 288 CG  
2 1 Y 1 A GLU 260 ? CD  ? A GLU 288 CD  
3 1 Y 1 A GLU 260 ? OE1 ? A GLU 288 OE1 
4 1 Y 1 A GLU 260 ? OE2 ? A GLU 288 OE2 
5 1 Y 1 A LEU 261 ? CG  ? A LEU 289 CG  
6 1 Y 1 A LEU 261 ? CD1 ? A LEU 289 CD1 
7 1 Y 1 A LEU 261 ? CD2 ? A LEU 289 CD2 
8 1 Y 1 A VAL 350 ? CG1 ? A VAL 378 CG1 
9 1 Y 1 A VAL 350 ? CG2 ? A VAL 378 CG2 
# 
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'   ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? .                    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                     9F1X 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     101.510 
_cell.length_a_esd                 ? 
_cell.length_b                     53.930 
_cell.length_b_esd                 ? 
_cell.length_c                     72.050 
_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                         9F1X 
_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                   9F1X 
_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              8.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.06 M divalents, 0.1 M Tris-Bicine, 30% v/v PEG550 MME-PEG20000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     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   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 4M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-10-29 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.978 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.978 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P14 (MX2)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9F1X 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.80 
_reflns.d_resolution_low                               59 
_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                                     36950 
_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                                595 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.8 
_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                                   0.9989 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   0.074 
_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                                    1.80 
_reflns_shell.d_res_low                                     1.86 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3615 
_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                                  0.5667 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  1.907 
_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                                 9F1X 
_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                            1.80 
_refine.ls_d_res_low                             58.75 
_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                     36864 
_refine.ls_number_reflns_R_free                  1820 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.28 
_refine.ls_percent_reflns_R_free                 4.94 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1856 
_refine.ls_R_factor_R_free                       0.2122 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1843 
_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                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 23.23 
_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                            0.26 
_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.pdbx_number_atoms_protein        2724 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         33 
_refine_hist.number_atoms_solvent             92 
_refine_hist.number_atoms_total               2849 
_refine_hist.d_res_high                       1.80 
_refine_hist.d_res_low                        58.75 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008  ? 2929 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.970  ? 3992 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 10.328 ? 420  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.062  ? 466  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.010  ? 508  ? 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' 1.80 1.85  . . 120 2449 91.00  . . . . 0.3843 . . . . . . . . . . . 0.3878 
'X-RAY DIFFRACTION' 1.85 1.91  . . 147 2628 100.00 . . . . 0.3321 . . . . . . . . . . . 0.3605 
'X-RAY DIFFRACTION' 1.91 1.97  . . 150 2672 100.00 . . . . 0.2938 . . . . . . . . . . . 0.3251 
'X-RAY DIFFRACTION' 1.97 2.04  . . 132 2672 100.00 . . . . 0.2748 . . . . . . . . . . . 0.2845 
'X-RAY DIFFRACTION' 2.04 2.12  . . 152 2693 100.00 . . . . 0.2340 . . . . . . . . . . . 0.2838 
'X-RAY DIFFRACTION' 2.12 2.22  . . 121 2698 100.00 . . . . 0.2062 . . . . . . . . . . . 0.2457 
'X-RAY DIFFRACTION' 2.22 2.33  . . 145 2690 100.00 . . . . 0.1992 . . . . . . . . . . . 0.2444 
'X-RAY DIFFRACTION' 2.33 2.48  . . 114 2719 100.00 . . . . 0.2041 . . . . . . . . . . . 0.2426 
'X-RAY DIFFRACTION' 2.48 2.67  . . 157 2694 100.00 . . . . 0.2017 . . . . . . . . . . . 0.2120 
'X-RAY DIFFRACTION' 2.67 2.94  . . 143 2710 100.00 . . . . 0.1884 . . . . . . . . . . . 0.2222 
'X-RAY DIFFRACTION' 2.94 3.37  . . 157 2744 100.00 . . . . 0.1844 . . . . . . . . . . . 0.2303 
'X-RAY DIFFRACTION' 3.37 4.24  . . 128 2785 100.00 . . . . 0.1517 . . . . . . . . . . . 0.1661 
'X-RAY DIFFRACTION' 4.24 58.75 . . 154 2890 100.00 . . . . 0.1521 . . . . . . . . . . . 0.1756 
# 
_struct.entry_id                     9F1X 
_struct.title                        'SSX 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        9F1X 
_struct_keywords.text            'FAD, SSX, TREXX, 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              9F1X 
_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 9F1X MET A 1  ? UNP K9TLZ5 ? ? 'initiating methionine' -27 1  
1 9F1X GLY A 2  ? UNP K9TLZ5 ? ? 'expression tag'        -26 2  
1 9F1X SER A 3  ? UNP K9TLZ5 ? ? 'expression tag'        -25 3  
1 9F1X SER A 4  ? UNP K9TLZ5 ? ? 'expression tag'        -24 4  
1 9F1X HIS A 5  ? UNP K9TLZ5 ? ? 'expression tag'        -23 5  
1 9F1X HIS A 6  ? UNP K9TLZ5 ? ? 'expression tag'        -22 6  
1 9F1X HIS A 7  ? UNP K9TLZ5 ? ? 'expression tag'        -21 7  
1 9F1X HIS A 8  ? UNP K9TLZ5 ? ? 'expression tag'        -20 8  
1 9F1X HIS A 9  ? UNP K9TLZ5 ? ? 'expression tag'        -19 9  
1 9F1X HIS A 10 ? UNP K9TLZ5 ? ? 'expression tag'        -18 10 
1 9F1X SER A 11 ? UNP K9TLZ5 ? ? 'expression tag'        -17 11 
1 9F1X SER A 12 ? UNP K9TLZ5 ? ? 'expression tag'        -16 12 
1 9F1X GLY A 13 ? UNP K9TLZ5 ? ? 'expression tag'        -15 13 
1 9F1X LEU A 14 ? UNP K9TLZ5 ? ? 'expression tag'        -14 14 
1 9F1X VAL A 15 ? UNP K9TLZ5 ? ? 'expression tag'        -13 15 
1 9F1X PRO A 16 ? UNP K9TLZ5 ? ? 'expression tag'        -12 16 
1 9F1X ARG A 17 ? UNP K9TLZ5 ? ? 'expression tag'        -11 17 
1 9F1X GLY A 18 ? UNP K9TLZ5 ? ? 'expression tag'        -10 18 
1 9F1X SER A 19 ? UNP K9TLZ5 ? ? 'expression tag'        -9  19 
1 9F1X HIS A 20 ? UNP K9TLZ5 ? ? 'expression tag'        -8  20 
1 9F1X MET A 21 ? UNP K9TLZ5 ? ? 'expression tag'        -7  21 
1 9F1X GLU A 22 ? UNP K9TLZ5 ? ? 'expression tag'        -6  22 
1 9F1X ASN A 23 ? UNP K9TLZ5 ? ? 'expression tag'        -5  23 
1 9F1X LEU A 24 ? UNP K9TLZ5 ? ? 'expression tag'        -4  24 
1 9F1X TYR A 25 ? UNP K9TLZ5 ? ? 'expression tag'        -3  25 
1 9F1X PHE A 26 ? UNP K9TLZ5 ? ? 'expression tag'        -2  26 
1 9F1X GLN A 27 ? UNP K9TLZ5 ? ? 'expression tag'        -1  27 
1 9F1X GLY A 28 ? UNP K9TLZ5 ? ? 'expression tag'        0   28 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_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)' 10070 ? 
1 MORE         -126  ? 
1 'SSA (A^2)'  29180 ? 
# 
_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 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z   1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
2 'crystal symmetry operation' 2_555 -x,-y,z -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 43  ? ASN A 62  ? SER A 15  ASN A 34  1 ? 20 
HELX_P HELX_P2  AA2 ALA A 82  ? ASP A 95  ? ALA A 54  ASP A 67  1 ? 14 
HELX_P HELX_P3  AA3 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 GLN A 155 ? GLN A 164 ? GLN A 127 GLN A 136 1 ? 10 
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 GLU A 366 ? ARG A 377 ? GLU A 338 ARG A 349 1 ? 12 
# 
_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 ? ? ? ? ? ? ? 2.424 ? ? 
metalc2  metalc ? ? A ASP 184 OD2 ? ? ? 1_555 D CA  . CA ? ? A ASP 156 A CA  403 1_555 ? ? ? ? ? ? ? 2.667 ? ? 
metalc3  metalc ? ? A ASP 228 OD2 ? ? ? 1_555 D CA  . CA ? ? A ASP 200 A CA  403 1_555 ? ? ? ? ? ? ? 2.395 ? ? 
metalc4  metalc ? ? A ASP 298 OD1 ? ? ? 1_555 D CA  . CA ? ? A ASP 270 A CA  403 2_555 ? ? ? ? ? ? ? 2.650 ? ? 
metalc5  metalc ? ? A ASP 338 OD1 ? ? ? 1_555 C CA  . CA ? ? A ASP 310 A CA  402 1_555 ? ? ? ? ? ? ? 2.511 ? ? 
metalc6  metalc ? ? A ASP 338 OD2 ? ? ? 1_555 C CA  . CA ? ? A ASP 310 A CA  402 1_555 ? ? ? ? ? ? ? 2.399 ? ? 
metalc7  metalc ? ? A ASP 349 OD1 ? ? ? 1_555 C CA  . CA ? ? A ASP 321 A CA  402 1_555 ? ? ? ? ? ? ? 2.321 ? ? 
metalc8  metalc ? ? C CA  .   CA  ? ? ? 1_555 E HOH . O  ? ? A CA  402 A HOH 564 1_555 ? ? ? ? ? ? ? 2.442 ? ? 
metalc9  metalc ? ? C CA  .   CA  ? ? ? 1_555 E HOH . O  ? ? A CA  402 A HOH 580 1_555 ? ? ? ? ? ? ? 2.431 ? ? 
metalc10 metalc ? ? C CA  .   CA  ? ? ? 1_555 E HOH . O  ? ? A CA  402 A HOH 586 1_554 ? ? ? ? ? ? ? 2.402 ? ? 
metalc11 metalc ? ? D CA  .   CA  ? ? ? 1_555 E HOH . O  ? ? A CA  403 A HOH 502 2_555 ? ? ? ? ? ? ? 2.302 ? ? 
metalc12 metalc ? ? D CA  .   CA  ? ? ? 1_555 E HOH . O  ? ? A CA  403 A HOH 516 1_555 ? ? ? ? ? ? ? 2.739 ? ? 
metalc13 metalc ? ? D CA  .   CA  ? ? ? 1_555 E HOH . O  ? ? A CA  403 A HOH 552 1_555 ? ? ? ? ? ? ? 2.442 ? ? 
# 
_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 31.9  ? 
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 30.4  ? 
3  OD1 ? A ASP 338 ? A ASP 310 ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 OD2 ? A ASP 338 ? A ASP 310 ? 1_555 1.5   ? 
4  O   ? A ASP 117 ? A ASP 89  ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 OD1 ? A ASP 349 ? A ASP 321 ? 1_555 32.4  ? 
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 2.7   ? 
7  O   ? A ASP 117 ? A ASP 89  ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 564 ? 1_555 29.8  ? 
8  OD1 ? A ASP 338 ? A ASP 310 ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 564 ? 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 564 ? 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 564 ? 1_555 2.7   ? 
11 O   ? A ASP 117 ? A ASP 89  ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 580 ? 1_555 32.7  ? 
12 OD1 ? A ASP 338 ? A ASP 310 ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 580 ? 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 580 ? 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 580 ? 1_555 0.4   ? 
15 O   ? E HOH .   ? A HOH 564 ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 580 ? 1_555 3.0   ? 
16 O   ? A ASP 117 ? A ASP 89  ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 586 ? 1_554 31.4  ? 
17 OD1 ? A ASP 338 ? A ASP 310 ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 586 ? 1_554 3.7   ? 
18 OD2 ? A ASP 338 ? A ASP 310 ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 586 ? 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 586 ? 1_554 2.2   ? 
20 O   ? E HOH .   ? A HOH 564 ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 586 ? 1_554 2.1   ? 
21 O   ? E HOH .   ? A HOH 580 ? 1_555 CA ? C CA . ? A CA 402 ? 1_556 O   ? E HOH .   ? A HOH 586 ? 1_554 2.1   ? 
22 OD2 ? A ASP 184 ? A ASP 156 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 OD2 ? A ASP 228 ? A ASP 200 ? 1_555 106.5 ? 
23 OD2 ? A ASP 184 ? A ASP 156 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 OD1 ? A ASP 298 ? A ASP 270 ? 1_555 82.3  ? 
24 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_555 110.6 ? 
25 OD2 ? A ASP 184 ? A ASP 156 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 502 ? 2_555 95.0  ? 
26 OD2 ? A ASP 228 ? A ASP 200 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 502 ? 2_555 141.1 ? 
27 OD1 ? A ASP 298 ? A ASP 270 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 502 ? 2_555 39.9  ? 
28 OD2 ? A ASP 184 ? A ASP 156 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 516 ? 1_555 98.8  ? 
29 OD2 ? A ASP 228 ? A ASP 200 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 516 ? 1_555 94.3  ? 
30 OD1 ? A ASP 298 ? A ASP 270 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 516 ? 1_555 20.4  ? 
31 O   ? E HOH .   ? A HOH 502 ? 2_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 516 ? 1_555 49.7  ? 
32 OD2 ? A ASP 184 ? A ASP 156 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 552 ? 1_555 107.7 ? 
33 OD2 ? A ASP 228 ? A ASP 200 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 552 ? 1_555 101.3 ? 
34 OD1 ? A ASP 298 ? A ASP 270 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 552 ? 1_555 142.4 ? 
35 O   ? E HOH .   ? A HOH 502 ? 2_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 552 ? 1_555 102.5 ? 
36 O   ? E HOH .   ? A HOH 516 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .   ? A HOH 552 ? 1_555 143.6 ? 
# 
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 VAL A 180 ? N VAL A 152 O ALA A 276 ? O ALA A 248 
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 VAL A 180 ? N VAL A 152 O ALA A 276 ? O ALA A 248 
AA3 4 5 N ILE A 273 ? N ILE A 245 O VAL A 318 ? O VAL A 290 
AA3 5 6 N PHE A 319 ? N PHE A 291 O TYR A 351 ? O TYR A 323 
AA3 6 7 O ILE A 350 ? O ILE A 322 N THR A 337 ? N THR A 309 
# 
_pdbx_entry_details.entry_id                   9F1X 
_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 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OE1 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   GLN 
_pdbx_validate_close_contact.auth_seq_id_1    31 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   B 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    501 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.95 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     502 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     516 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_555 
_pdbx_validate_symm_contact.dist              2.15 
# 
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 SER A 317 ? ? -79.88 36.61  
2 1 GLU A 338 ? ? 36.27  -85.09 
# 
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 GLY 351 ? A GLY 379 
34 1 Y 1 A ASP 352 ? A ASP 380 
35 1 Y 1 A ARG 353 ? A ARG 381 
36 1 Y 1 A GLN 354 ? A GLN 382 
37 1 Y 1 A PRO 355 ? A PRO 383 
38 1 Y 1 A SER 356 ? A SER 384 
39 1 Y 1 A GLN 357 ? A GLN 385 
40 1 Y 1 A ILE 358 ? A ILE 386 
41 1 Y 1 A PHE 359 ? A PHE 387 
42 1 Y 1 A GLY 360 ? A GLY 388 
43 1 Y 1 A VAL 361 ? A VAL 389 
44 1 Y 1 A LYS 362 ? A LYS 390 
45 1 Y 1 A SER 363 ? A SER 391 
46 1 Y 1 A LEU 364 ? A LEU 392 
47 1 Y 1 A PRO 365 ? A PRO 393 
48 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  
FMN N1     N  N N 89  
FMN C2     C  N N 90  
FMN O2     O  N N 91  
FMN N3     N  N N 92  
FMN C4     C  N N 93  
FMN O4     O  N N 94  
FMN C4A    C  N N 95  
FMN N5     N  N N 96  
FMN C5A    C  Y N 97  
FMN C6     C  Y N 98  
FMN C7     C  Y N 99  
FMN C7M    C  N N 100 
FMN C8     C  Y N 101 
FMN C8M    C  N N 102 
FMN C9     C  Y N 103 
FMN C9A    C  Y N 104 
FMN N10    N  N N 105 
FMN C10    C  N N 106 
FMN "C1'"  C  N N 107 
FMN "C2'"  C  N S 108 
FMN "O2'"  O  N N 109 
FMN "C3'"  C  N S 110 
FMN "O3'"  O  N N 111 
FMN "C4'"  C  N R 112 
FMN "O4'"  O  N N 113 
FMN "C5'"  C  N N 114 
FMN "O5'"  O  N N 115 
FMN P      P  N N 116 
FMN O1P    O  N N 117 
FMN O2P    O  N N 118 
FMN O3P    O  N N 119 
FMN HN3    H  N N 120 
FMN H6     H  N N 121 
FMN HM71   H  N N 122 
FMN HM72   H  N N 123 
FMN HM73   H  N N 124 
FMN HM81   H  N N 125 
FMN HM82   H  N N 126 
FMN HM83   H  N N 127 
FMN H9     H  N N 128 
FMN "H1'1" H  N N 129 
FMN "H1'2" H  N N 130 
FMN "H2'"  H  N N 131 
FMN "HO2'" H  N N 132 
FMN "H3'"  H  N N 133 
FMN "HO3'" H  N N 134 
FMN "H4'"  H  N N 135 
FMN "HO4'" H  N N 136 
FMN "H5'1" H  N N 137 
FMN "H5'2" H  N N 138 
FMN HOP2   H  N N 139 
FMN HOP3   H  N N 140 
GLN N      N  N N 141 
GLN CA     C  N S 142 
GLN C      C  N N 143 
GLN O      O  N N 144 
GLN CB     C  N N 145 
GLN CG     C  N N 146 
GLN CD     C  N N 147 
GLN OE1    O  N N 148 
GLN NE2    N  N N 149 
GLN OXT    O  N N 150 
GLN H      H  N N 151 
GLN H2     H  N N 152 
GLN HA     H  N N 153 
GLN HB2    H  N N 154 
GLN HB3    H  N N 155 
GLN HG2    H  N N 156 
GLN HG3    H  N N 157 
GLN HE21   H  N N 158 
GLN HE22   H  N N 159 
GLN HXT    H  N N 160 
GLU N      N  N N 161 
GLU CA     C  N S 162 
GLU C      C  N N 163 
GLU O      O  N N 164 
GLU CB     C  N N 165 
GLU CG     C  N N 166 
GLU CD     C  N N 167 
GLU OE1    O  N N 168 
GLU OE2    O  N N 169 
GLU OXT    O  N N 170 
GLU H      H  N N 171 
GLU H2     H  N N 172 
GLU HA     H  N N 173 
GLU HB2    H  N N 174 
GLU HB3    H  N N 175 
GLU HG2    H  N N 176 
GLU HG3    H  N N 177 
GLU HE2    H  N N 178 
GLU HXT    H  N N 179 
GLY N      N  N N 180 
GLY CA     C  N N 181 
GLY C      C  N N 182 
GLY O      O  N N 183 
GLY OXT    O  N N 184 
GLY H      H  N N 185 
GLY H2     H  N N 186 
GLY HA2    H  N N 187 
GLY HA3    H  N N 188 
GLY HXT    H  N N 189 
HIS N      N  N N 190 
HIS CA     C  N S 191 
HIS C      C  N N 192 
HIS O      O  N N 193 
HIS CB     C  N N 194 
HIS CG     C  Y N 195 
HIS ND1    N  Y N 196 
HIS CD2    C  Y N 197 
HIS CE1    C  Y N 198 
HIS NE2    N  Y N 199 
HIS OXT    O  N N 200 
HIS H      H  N N 201 
HIS H2     H  N N 202 
HIS HA     H  N N 203 
HIS HB2    H  N N 204 
HIS HB3    H  N N 205 
HIS HD1    H  N N 206 
HIS HD2    H  N N 207 
HIS HE1    H  N N 208 
HIS HE2    H  N N 209 
HIS HXT    H  N N 210 
HOH O      O  N N 211 
HOH H1     H  N N 212 
HOH H2     H  N N 213 
ILE N      N  N N 214 
ILE CA     C  N S 215 
ILE C      C  N N 216 
ILE O      O  N N 217 
ILE CB     C  N S 218 
ILE CG1    C  N N 219 
ILE CG2    C  N N 220 
ILE CD1    C  N N 221 
ILE OXT    O  N N 222 
ILE H      H  N N 223 
ILE H2     H  N N 224 
ILE HA     H  N N 225 
ILE HB     H  N N 226 
ILE HG12   H  N N 227 
ILE HG13   H  N N 228 
ILE HG21   H  N N 229 
ILE HG22   H  N N 230 
ILE HG23   H  N N 231 
ILE HD11   H  N N 232 
ILE HD12   H  N N 233 
ILE HD13   H  N N 234 
ILE HXT    H  N N 235 
LEU N      N  N N 236 
LEU CA     C  N S 237 
LEU C      C  N N 238 
LEU O      O  N N 239 
LEU CB     C  N N 240 
LEU CG     C  N N 241 
LEU CD1    C  N N 242 
LEU CD2    C  N N 243 
LEU OXT    O  N N 244 
LEU H      H  N N 245 
LEU H2     H  N N 246 
LEU HA     H  N N 247 
LEU HB2    H  N N 248 
LEU HB3    H  N N 249 
LEU HG     H  N N 250 
LEU HD11   H  N N 251 
LEU HD12   H  N N 252 
LEU HD13   H  N N 253 
LEU HD21   H  N N 254 
LEU HD22   H  N N 255 
LEU HD23   H  N N 256 
LEU HXT    H  N N 257 
LYS N      N  N N 258 
LYS CA     C  N S 259 
LYS C      C  N N 260 
LYS O      O  N N 261 
LYS CB     C  N N 262 
LYS CG     C  N N 263 
LYS CD     C  N N 264 
LYS CE     C  N N 265 
LYS NZ     N  N N 266 
LYS OXT    O  N N 267 
LYS H      H  N N 268 
LYS H2     H  N N 269 
LYS HA     H  N N 270 
LYS HB2    H  N N 271 
LYS HB3    H  N N 272 
LYS HG2    H  N N 273 
LYS HG3    H  N N 274 
LYS HD2    H  N N 275 
LYS HD3    H  N N 276 
LYS HE2    H  N N 277 
LYS HE3    H  N N 278 
LYS HZ1    H  N N 279 
LYS HZ2    H  N N 280 
LYS HZ3    H  N N 281 
LYS HXT    H  N N 282 
MET N      N  N N 283 
MET CA     C  N S 284 
MET C      C  N N 285 
MET O      O  N N 286 
MET CB     C  N N 287 
MET CG     C  N N 288 
MET SD     S  N N 289 
MET CE     C  N N 290 
MET OXT    O  N N 291 
MET H      H  N N 292 
MET H2     H  N N 293 
MET HA     H  N N 294 
MET HB2    H  N N 295 
MET HB3    H  N N 296 
MET HG2    H  N N 297 
MET HG3    H  N N 298 
MET HE1    H  N N 299 
MET HE2    H  N N 300 
MET HE3    H  N N 301 
MET HXT    H  N N 302 
PHE N      N  N N 303 
PHE CA     C  N S 304 
PHE C      C  N N 305 
PHE O      O  N N 306 
PHE CB     C  N N 307 
PHE CG     C  Y N 308 
PHE CD1    C  Y N 309 
PHE CD2    C  Y N 310 
PHE CE1    C  Y N 311 
PHE CE2    C  Y N 312 
PHE CZ     C  Y N 313 
PHE OXT    O  N N 314 
PHE H      H  N N 315 
PHE H2     H  N N 316 
PHE HA     H  N N 317 
PHE HB2    H  N N 318 
PHE HB3    H  N N 319 
PHE HD1    H  N N 320 
PHE HD2    H  N N 321 
PHE HE1    H  N N 322 
PHE HE2    H  N N 323 
PHE HZ     H  N N 324 
PHE HXT    H  N N 325 
PRO N      N  N N 326 
PRO CA     C  N S 327 
PRO C      C  N N 328 
PRO O      O  N N 329 
PRO CB     C  N N 330 
PRO CG     C  N N 331 
PRO CD     C  N N 332 
PRO OXT    O  N N 333 
PRO H      H  N N 334 
PRO HA     H  N N 335 
PRO HB2    H  N N 336 
PRO HB3    H  N N 337 
PRO HG2    H  N N 338 
PRO HG3    H  N N 339 
PRO HD2    H  N N 340 
PRO HD3    H  N N 341 
PRO HXT    H  N N 342 
SER N      N  N N 343 
SER CA     C  N S 344 
SER C      C  N N 345 
SER O      O  N N 346 
SER CB     C  N N 347 
SER OG     O  N N 348 
SER OXT    O  N N 349 
SER H      H  N N 350 
SER H2     H  N N 351 
SER HA     H  N N 352 
SER HB2    H  N N 353 
SER HB3    H  N N 354 
SER HG     H  N N 355 
SER HXT    H  N N 356 
THR N      N  N N 357 
THR CA     C  N S 358 
THR C      C  N N 359 
THR O      O  N N 360 
THR CB     C  N R 361 
THR OG1    O  N N 362 
THR CG2    C  N N 363 
THR OXT    O  N N 364 
THR H      H  N N 365 
THR H2     H  N N 366 
THR HA     H  N N 367 
THR HB     H  N N 368 
THR HG1    H  N N 369 
THR HG21   H  N N 370 
THR HG22   H  N N 371 
THR HG23   H  N N 372 
THR HXT    H  N N 373 
TRP N      N  N N 374 
TRP CA     C  N S 375 
TRP C      C  N N 376 
TRP O      O  N N 377 
TRP CB     C  N N 378 
TRP CG     C  Y N 379 
TRP CD1    C  Y N 380 
TRP CD2    C  Y N 381 
TRP NE1    N  Y N 382 
TRP CE2    C  Y N 383 
TRP CE3    C  Y N 384 
TRP CZ2    C  Y N 385 
TRP CZ3    C  Y N 386 
TRP CH2    C  Y N 387 
TRP OXT    O  N N 388 
TRP H      H  N N 389 
TRP H2     H  N N 390 
TRP HA     H  N N 391 
TRP HB2    H  N N 392 
TRP HB3    H  N N 393 
TRP HD1    H  N N 394 
TRP HE1    H  N N 395 
TRP HE3    H  N N 396 
TRP HZ2    H  N N 397 
TRP HZ3    H  N N 398 
TRP HH2    H  N N 399 
TRP HXT    H  N N 400 
TYR N      N  N N 401 
TYR CA     C  N S 402 
TYR C      C  N N 403 
TYR O      O  N N 404 
TYR CB     C  N N 405 
TYR CG     C  Y N 406 
TYR CD1    C  Y N 407 
TYR CD2    C  Y N 408 
TYR CE1    C  Y N 409 
TYR CE2    C  Y N 410 
TYR CZ     C  Y N 411 
TYR OH     O  N N 412 
TYR OXT    O  N N 413 
TYR H      H  N N 414 
TYR H2     H  N N 415 
TYR HA     H  N N 416 
TYR HB2    H  N N 417 
TYR HB3    H  N N 418 
TYR HD1    H  N N 419 
TYR HD2    H  N N 420 
TYR HE1    H  N N 421 
TYR HE2    H  N N 422 
TYR HH     H  N N 423 
TYR HXT    H  N N 424 
VAL N      N  N N 425 
VAL CA     C  N S 426 
VAL C      C  N N 427 
VAL O      O  N N 428 
VAL CB     C  N N 429 
VAL CG1    C  N N 430 
VAL CG2    C  N N 431 
VAL OXT    O  N N 432 
VAL H      H  N N 433 
VAL H2     H  N N 434 
VAL HA     H  N N 435 
VAL HB     H  N N 436 
VAL HG11   H  N N 437 
VAL HG12   H  N N 438 
VAL HG13   H  N N 439 
VAL HG21   H  N N 440 
VAL HG22   H  N N 441 
VAL HG23   H  N N 442 
VAL HXT    H  N N 443 
# 
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  
FMN N1    C2     sing N N 83  
FMN N1    C10    doub N N 84  
FMN C2    O2     doub N N 85  
FMN C2    N3     sing N N 86  
FMN N3    C4     sing N N 87  
FMN N3    HN3    sing N N 88  
FMN C4    O4     doub N N 89  
FMN C4    C4A    sing N N 90  
FMN C4A   N5     doub N N 91  
FMN C4A   C10    sing N N 92  
FMN N5    C5A    sing N N 93  
FMN C5A   C6     doub Y N 94  
FMN C5A   C9A    sing Y N 95  
FMN C6    C7     sing Y N 96  
FMN C6    H6     sing N N 97  
FMN C7    C7M    sing N N 98  
FMN C7    C8     doub Y N 99  
FMN C7M   HM71   sing N N 100 
FMN C7M   HM72   sing N N 101 
FMN C7M   HM73   sing N N 102 
FMN C8    C8M    sing N N 103 
FMN C8    C9     sing Y N 104 
FMN C8M   HM81   sing N N 105 
FMN C8M   HM82   sing N N 106 
FMN C8M   HM83   sing N N 107 
FMN C9    C9A    doub Y N 108 
FMN C9    H9     sing N N 109 
FMN C9A   N10    sing N N 110 
FMN N10   C10    sing N N 111 
FMN N10   "C1'"  sing N N 112 
FMN "C1'" "C2'"  sing N N 113 
FMN "C1'" "H1'1" sing N N 114 
FMN "C1'" "H1'2" sing N N 115 
FMN "C2'" "O2'"  sing N N 116 
FMN "C2'" "C3'"  sing N N 117 
FMN "C2'" "H2'"  sing N N 118 
FMN "O2'" "HO2'" sing N N 119 
FMN "C3'" "O3'"  sing N N 120 
FMN "C3'" "C4'"  sing N N 121 
FMN "C3'" "H3'"  sing N N 122 
FMN "O3'" "HO3'" sing N N 123 
FMN "C4'" "O4'"  sing N N 124 
FMN "C4'" "C5'"  sing N N 125 
FMN "C4'" "H4'"  sing N N 126 
FMN "O4'" "HO4'" sing N N 127 
FMN "C5'" "O5'"  sing N N 128 
FMN "C5'" "H5'1" sing N N 129 
FMN "C5'" "H5'2" sing N N 130 
FMN "O5'" P      sing N N 131 
FMN P     O1P    doub N N 132 
FMN P     O2P    sing N N 133 
FMN P     O3P    sing N N 134 
FMN O2P   HOP2   sing N N 135 
FMN O3P   HOP3   sing N N 136 
GLN N     CA     sing N N 137 
GLN N     H      sing N N 138 
GLN N     H2     sing N N 139 
GLN CA    C      sing N N 140 
GLN CA    CB     sing N N 141 
GLN CA    HA     sing N N 142 
GLN C     O      doub N N 143 
GLN C     OXT    sing N N 144 
GLN CB    CG     sing N N 145 
GLN CB    HB2    sing N N 146 
GLN CB    HB3    sing N N 147 
GLN CG    CD     sing N N 148 
GLN CG    HG2    sing N N 149 
GLN CG    HG3    sing N N 150 
GLN CD    OE1    doub N N 151 
GLN CD    NE2    sing N N 152 
GLN NE2   HE21   sing N N 153 
GLN NE2   HE22   sing N N 154 
GLN OXT   HXT    sing N N 155 
GLU N     CA     sing N N 156 
GLU N     H      sing N N 157 
GLU N     H2     sing N N 158 
GLU CA    C      sing N N 159 
GLU CA    CB     sing N N 160 
GLU CA    HA     sing N N 161 
GLU C     O      doub N N 162 
GLU C     OXT    sing N N 163 
GLU CB    CG     sing N N 164 
GLU CB    HB2    sing N N 165 
GLU CB    HB3    sing N N 166 
GLU CG    CD     sing N N 167 
GLU CG    HG2    sing N N 168 
GLU CG    HG3    sing N N 169 
GLU CD    OE1    doub N N 170 
GLU CD    OE2    sing N N 171 
GLU OE2   HE2    sing N N 172 
GLU OXT   HXT    sing N N 173 
GLY N     CA     sing N N 174 
GLY N     H      sing N N 175 
GLY N     H2     sing N N 176 
GLY CA    C      sing N N 177 
GLY CA    HA2    sing N N 178 
GLY CA    HA3    sing N N 179 
GLY C     O      doub N N 180 
GLY C     OXT    sing N N 181 
GLY OXT   HXT    sing N N 182 
HIS N     CA     sing N N 183 
HIS N     H      sing N N 184 
HIS N     H2     sing N N 185 
HIS CA    C      sing N N 186 
HIS CA    CB     sing N N 187 
HIS CA    HA     sing N N 188 
HIS C     O      doub N N 189 
HIS C     OXT    sing N N 190 
HIS CB    CG     sing N N 191 
HIS CB    HB2    sing N N 192 
HIS CB    HB3    sing N N 193 
HIS CG    ND1    sing Y N 194 
HIS CG    CD2    doub Y N 195 
HIS ND1   CE1    doub Y N 196 
HIS ND1   HD1    sing N N 197 
HIS CD2   NE2    sing Y N 198 
HIS CD2   HD2    sing N N 199 
HIS CE1   NE2    sing Y N 200 
HIS CE1   HE1    sing N N 201 
HIS NE2   HE2    sing N N 202 
HIS OXT   HXT    sing N N 203 
HOH O     H1     sing N N 204 
HOH O     H2     sing N N 205 
ILE N     CA     sing N N 206 
ILE N     H      sing N N 207 
ILE N     H2     sing N N 208 
ILE CA    C      sing N N 209 
ILE CA    CB     sing N N 210 
ILE CA    HA     sing N N 211 
ILE C     O      doub N N 212 
ILE C     OXT    sing N N 213 
ILE CB    CG1    sing N N 214 
ILE CB    CG2    sing N N 215 
ILE CB    HB     sing N N 216 
ILE CG1   CD1    sing N N 217 
ILE CG1   HG12   sing N N 218 
ILE CG1   HG13   sing N N 219 
ILE CG2   HG21   sing N N 220 
ILE CG2   HG22   sing N N 221 
ILE CG2   HG23   sing N N 222 
ILE CD1   HD11   sing N N 223 
ILE CD1   HD12   sing N N 224 
ILE CD1   HD13   sing N N 225 
ILE OXT   HXT    sing N N 226 
LEU N     CA     sing N N 227 
LEU N     H      sing N N 228 
LEU N     H2     sing N N 229 
LEU CA    C      sing N N 230 
LEU CA    CB     sing N N 231 
LEU CA    HA     sing N N 232 
LEU C     O      doub N N 233 
LEU C     OXT    sing N N 234 
LEU CB    CG     sing N N 235 
LEU CB    HB2    sing N N 236 
LEU CB    HB3    sing N N 237 
LEU CG    CD1    sing N N 238 
LEU CG    CD2    sing N N 239 
LEU CG    HG     sing N N 240 
LEU CD1   HD11   sing N N 241 
LEU CD1   HD12   sing N N 242 
LEU CD1   HD13   sing N N 243 
LEU CD2   HD21   sing N N 244 
LEU CD2   HD22   sing N N 245 
LEU CD2   HD23   sing N N 246 
LEU OXT   HXT    sing N N 247 
LYS N     CA     sing N N 248 
LYS N     H      sing N N 249 
LYS N     H2     sing N N 250 
LYS CA    C      sing N N 251 
LYS CA    CB     sing N N 252 
LYS CA    HA     sing N N 253 
LYS C     O      doub N N 254 
LYS C     OXT    sing N N 255 
LYS CB    CG     sing N N 256 
LYS CB    HB2    sing N N 257 
LYS CB    HB3    sing N N 258 
LYS CG    CD     sing N N 259 
LYS CG    HG2    sing N N 260 
LYS CG    HG3    sing N N 261 
LYS CD    CE     sing N N 262 
LYS CD    HD2    sing N N 263 
LYS CD    HD3    sing N N 264 
LYS CE    NZ     sing N N 265 
LYS CE    HE2    sing N N 266 
LYS CE    HE3    sing N N 267 
LYS NZ    HZ1    sing N N 268 
LYS NZ    HZ2    sing N N 269 
LYS NZ    HZ3    sing N N 270 
LYS OXT   HXT    sing N N 271 
MET N     CA     sing N N 272 
MET N     H      sing N N 273 
MET N     H2     sing N N 274 
MET CA    C      sing N N 275 
MET CA    CB     sing N N 276 
MET CA    HA     sing N N 277 
MET C     O      doub N N 278 
MET C     OXT    sing N N 279 
MET CB    CG     sing N N 280 
MET CB    HB2    sing N N 281 
MET CB    HB3    sing N N 282 
MET CG    SD     sing N N 283 
MET CG    HG2    sing N N 284 
MET CG    HG3    sing N N 285 
MET SD    CE     sing N N 286 
MET CE    HE1    sing N N 287 
MET CE    HE2    sing N N 288 
MET CE    HE3    sing N N 289 
MET OXT   HXT    sing N N 290 
PHE N     CA     sing N N 291 
PHE N     H      sing N N 292 
PHE N     H2     sing N N 293 
PHE CA    C      sing N N 294 
PHE CA    CB     sing N N 295 
PHE CA    HA     sing N N 296 
PHE C     O      doub N N 297 
PHE C     OXT    sing N N 298 
PHE CB    CG     sing N N 299 
PHE CB    HB2    sing N N 300 
PHE CB    HB3    sing N N 301 
PHE CG    CD1    doub Y N 302 
PHE CG    CD2    sing Y N 303 
PHE CD1   CE1    sing Y N 304 
PHE CD1   HD1    sing N N 305 
PHE CD2   CE2    doub Y N 306 
PHE CD2   HD2    sing N N 307 
PHE CE1   CZ     doub Y N 308 
PHE CE1   HE1    sing N N 309 
PHE CE2   CZ     sing Y N 310 
PHE CE2   HE2    sing N N 311 
PHE CZ    HZ     sing N N 312 
PHE OXT   HXT    sing N N 313 
PRO N     CA     sing N N 314 
PRO N     CD     sing N N 315 
PRO N     H      sing N N 316 
PRO CA    C      sing N N 317 
PRO CA    CB     sing N N 318 
PRO CA    HA     sing N N 319 
PRO C     O      doub N N 320 
PRO C     OXT    sing N N 321 
PRO CB    CG     sing N N 322 
PRO CB    HB2    sing N N 323 
PRO CB    HB3    sing N N 324 
PRO CG    CD     sing N N 325 
PRO CG    HG2    sing N N 326 
PRO CG    HG3    sing N N 327 
PRO CD    HD2    sing N N 328 
PRO CD    HD3    sing N N 329 
PRO OXT   HXT    sing N N 330 
SER N     CA     sing N N 331 
SER N     H      sing N N 332 
SER N     H2     sing N N 333 
SER CA    C      sing N N 334 
SER CA    CB     sing N N 335 
SER CA    HA     sing N N 336 
SER C     O      doub N N 337 
SER C     OXT    sing N N 338 
SER CB    OG     sing N N 339 
SER CB    HB2    sing N N 340 
SER CB    HB3    sing N N 341 
SER OG    HG     sing N N 342 
SER OXT   HXT    sing N N 343 
THR N     CA     sing N N 344 
THR N     H      sing N N 345 
THR N     H2     sing N N 346 
THR CA    C      sing N N 347 
THR CA    CB     sing N N 348 
THR CA    HA     sing N N 349 
THR C     O      doub N N 350 
THR C     OXT    sing N N 351 
THR CB    OG1    sing N N 352 
THR CB    CG2    sing N N 353 
THR CB    HB     sing N N 354 
THR OG1   HG1    sing N N 355 
THR CG2   HG21   sing N N 356 
THR CG2   HG22   sing N N 357 
THR CG2   HG23   sing N N 358 
THR OXT   HXT    sing N N 359 
TRP N     CA     sing N N 360 
TRP N     H      sing N N 361 
TRP N     H2     sing N N 362 
TRP CA    C      sing N N 363 
TRP CA    CB     sing N N 364 
TRP CA    HA     sing N N 365 
TRP C     O      doub N N 366 
TRP C     OXT    sing N N 367 
TRP CB    CG     sing N N 368 
TRP CB    HB2    sing N N 369 
TRP CB    HB3    sing N N 370 
TRP CG    CD1    doub Y N 371 
TRP CG    CD2    sing Y N 372 
TRP CD1   NE1    sing Y N 373 
TRP CD1   HD1    sing N N 374 
TRP CD2   CE2    doub Y N 375 
TRP CD2   CE3    sing Y N 376 
TRP NE1   CE2    sing Y N 377 
TRP NE1   HE1    sing N N 378 
TRP CE2   CZ2    sing Y N 379 
TRP CE3   CZ3    doub Y N 380 
TRP CE3   HE3    sing N N 381 
TRP CZ2   CH2    doub Y N 382 
TRP CZ2   HZ2    sing N N 383 
TRP CZ3   CH2    sing Y N 384 
TRP CZ3   HZ3    sing N N 385 
TRP CH2   HH2    sing N N 386 
TRP OXT   HXT    sing N N 387 
TYR N     CA     sing N N 388 
TYR N     H      sing N N 389 
TYR N     H2     sing N N 390 
TYR CA    C      sing N N 391 
TYR CA    CB     sing N N 392 
TYR CA    HA     sing N N 393 
TYR C     O      doub N N 394 
TYR C     OXT    sing N N 395 
TYR CB    CG     sing N N 396 
TYR CB    HB2    sing N N 397 
TYR CB    HB3    sing N N 398 
TYR CG    CD1    doub Y N 399 
TYR CG    CD2    sing Y N 400 
TYR CD1   CE1    sing Y N 401 
TYR CD1   HD1    sing N N 402 
TYR CD2   CE2    doub Y N 403 
TYR CD2   HD2    sing N N 404 
TYR CE1   CZ     doub Y N 405 
TYR CE1   HE1    sing N N 406 
TYR CE2   CZ     sing Y N 407 
TYR CE2   HE2    sing N N 408 
TYR CZ    OH     sing N N 409 
TYR OH    HH     sing N N 410 
TYR OXT   HXT    sing N N 411 
VAL N     CA     sing N N 412 
VAL N     H      sing N N 413 
VAL N     H2     sing N N 414 
VAL CA    C      sing N N 415 
VAL CA    CB     sing N N 416 
VAL CA    HA     sing N N 417 
VAL C     O      doub N N 418 
VAL C     OXT    sing N N 419 
VAL CB    CG1    sing N N 420 
VAL CB    CG2    sing N N 421 
VAL CB    HB     sing N N 422 
VAL CG1   HG11   sing N N 423 
VAL CG1   HG12   sing N N 424 
VAL CG1   HG13   sing N N 425 
VAL CG2   HG21   sing N N 426 
VAL CG2   HG22   sing N N 427 
VAL CG2   HG23   sing N N 428 
VAL OXT   HXT    sing N N 429 
# 
_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   1 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4YUT 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9F1X 
_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]   0.009851 
_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]   0.018543 
_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]   0.013879 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CA 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . GLY A 1 28  ? 11.880  26.407  41.354  1.00 86.27  ? 0   GLY A N     1 
ATOM   2    C  CA    . GLY A 1 28  ? 10.670  25.848  41.951  1.00 79.86  ? 0   GLY A CA    1 
ATOM   3    C  C     . GLY A 1 28  ? 10.769  24.351  42.263  1.00 73.61  ? 0   GLY A C     1 
ATOM   4    O  O     . GLY A 1 28  ? 11.733  23.684  41.874  1.00 67.89  ? 0   GLY A O     1 
ATOM   5    N  N     . MET A 1 29  ? 9.749   23.826  42.944  1.00 69.92  ? 1   MET A N     1 
ATOM   6    C  CA    . MET A 1 29  ? 9.813   22.490  43.518  1.00 63.75  ? 1   MET A CA    1 
ATOM   7    C  C     . MET A 1 29  ? 9.261   21.436  42.570  1.00 54.72  ? 1   MET A C     1 
ATOM   8    O  O     . MET A 1 29  ? 8.262   21.651  41.875  1.00 61.40  ? 1   MET A O     1 
ATOM   9    C  CB    . MET A 1 29  ? 9.061   22.429  44.847  1.00 61.76  ? 1   MET A CB    1 
ATOM   10   C  CG    . MET A 1 29  ? 9.914   22.882  46.030  1.00 62.82  ? 1   MET A CG    1 
ATOM   11   S  SD    . MET A 1 29  ? 9.490   22.070  47.585  1.00 72.47  ? 1   MET A SD    1 
ATOM   12   C  CE    . MET A 1 29  ? 8.015   22.968  48.069  1.00 66.54  ? 1   MET A CE    1 
ATOM   13   N  N     . LYS A 1 30  ? 9.918   20.284  42.576  1.00 50.84  ? 2   LYS A N     1 
ATOM   14   C  CA    . LYS A 1 30  ? 9.605   19.146  41.734  1.00 46.65  ? 2   LYS A CA    1 
ATOM   15   C  C     . LYS A 1 30  ? 9.489   17.919  42.628  1.00 55.47  ? 2   LYS A C     1 
ATOM   16   O  O     . LYS A 1 30  ? 10.198  17.809  43.633  1.00 49.16  ? 2   LYS A O     1 
ATOM   17   C  CB    . LYS A 1 30  ? 10.704  18.951  40.675  1.00 51.01  ? 2   LYS A CB    1 
ATOM   18   C  CG    . LYS A 1 30  ? 10.484  17.854  39.643  1.00 56.88  ? 2   LYS A CG    1 
ATOM   19   C  CD    . LYS A 1 30  ? 11.693  17.801  38.707  1.00 62.96  ? 2   LYS A CD    1 
ATOM   20   C  CE    . LYS A 1 30  ? 11.340  17.313  37.304  1.00 66.80  ? 2   LYS A CE    1 
ATOM   21   N  NZ    . LYS A 1 30  ? 12.468  16.547  36.679  1.00 69.43  ? 2   LYS A NZ    1 
ATOM   22   N  N     . ARG A 1 31  ? 8.588   17.007  42.267  1.00 50.93  ? 3   ARG A N     1 
ATOM   23   C  CA    . ARG A 1 31  ? 8.418   15.736  42.965  1.00 43.04  ? 3   ARG A CA    1 
ATOM   24   C  C     . ARG A 1 31  ? 8.373   14.616  41.937  1.00 46.81  ? 3   ARG A C     1 
ATOM   25   O  O     . ARG A 1 31  ? 7.501   14.614  41.056  1.00 49.73  ? 3   ARG A O     1 
ATOM   26   C  CB    . ARG A 1 31  ? 7.146   15.741  43.825  1.00 41.73  ? 3   ARG A CB    1 
ATOM   27   C  CG    . ARG A 1 31  ? 7.003   14.524  44.709  1.00 39.45  ? 3   ARG A CG    1 
ATOM   28   C  CD    . ARG A 1 31  ? 5.980   14.716  45.819  1.00 36.08  ? 3   ARG A CD    1 
ATOM   29   N  NE    . ARG A 1 31  ? 4.784   15.414  45.377  1.00 43.86  ? 3   ARG A NE    1 
ATOM   30   C  CZ    . ARG A 1 31  ? 4.318   16.521  45.935  1.00 43.80  ? 3   ARG A CZ    1 
ATOM   31   N  NH1   . ARG A 1 31  ? 4.923   17.084  46.971  1.00 43.32  ? 3   ARG A NH1   1 
ATOM   32   N  NH2   . ARG A 1 31  ? 3.226   17.085  45.434  1.00 47.61  ? 3   ARG A NH2   1 
ATOM   33   N  N     . LEU A 1 32  ? 9.318   13.681  42.030  1.00 38.58  ? 4   LEU A N     1 
ATOM   34   C  CA    . LEU A 1 32  ? 9.309   12.487  41.203  1.00 37.95  ? 4   LEU A CA    1 
ATOM   35   C  C     . LEU A 1 32  ? 8.921   11.274  42.027  1.00 40.44  ? 4   LEU A C     1 
ATOM   36   O  O     . LEU A 1 32  ? 9.272   11.160  43.209  1.00 36.14  ? 4   LEU A O     1 
ATOM   37   C  CB    . LEU A 1 32  ? 10.665  12.199  40.547  1.00 38.74  ? 4   LEU A CB    1 
ATOM   38   C  CG    . LEU A 1 32  ? 11.517  13.307  39.959  1.00 53.47  ? 4   LEU A CG    1 
ATOM   39   C  CD1   . LEU A 1 32  ? 12.753  12.673  39.349  1.00 51.63  ? 4   LEU A CD1   1 
ATOM   40   C  CD2   . LEU A 1 32  ? 10.716  14.012  38.887  1.00 58.35  ? 4   LEU A CD2   1 
ATOM   41   N  N     . THR A 1 33  ? 8.214   10.364  41.366  1.00 34.19  ? 5   THR A N     1 
ATOM   42   C  CA    . THR A 1 33  ? 7.918   9.037   41.880  1.00 34.01  ? 5   THR A CA    1 
ATOM   43   C  C     . THR A 1 33  ? 8.391   8.009   40.864  1.00 37.49  ? 5   THR A C     1 
ATOM   44   O  O     . THR A 1 33  ? 8.043   8.101   39.682  1.00 41.34  ? 5   THR A O     1 
ATOM   45   C  CB    . THR A 1 33  ? 6.423   8.862   42.129  1.00 37.82  ? 5   THR A CB    1 
ATOM   46   O  OG1   . THR A 1 33  ? 5.943   9.933   42.944  1.00 36.32  ? 5   THR A OG1   1 
ATOM   47   C  CG2   . THR A 1 33  ? 6.148   7.511   42.798  1.00 36.26  ? 5   THR A CG2   1 
ATOM   48   N  N     . TYR A 1 34  ? 9.158   7.019   41.316  1.00 32.20  ? 6   TYR A N     1 
ATOM   49   C  CA    . TYR A 1 34  ? 9.604   5.973   40.412  1.00 38.73  ? 6   TYR A CA    1 
ATOM   50   C  C     . TYR A 1 34  ? 9.583   4.628   41.117  1.00 41.67  ? 6   TYR A C     1 
ATOM   51   O  O     . TYR A 1 34  ? 9.549   4.528   42.350  1.00 37.92  ? 6   TYR A O     1 
ATOM   52   C  CB    . TYR A 1 34  ? 11.010  6.262   39.827  1.00 41.73  ? 6   TYR A CB    1 
ATOM   53   C  CG    . TYR A 1 34  ? 12.154  6.046   40.808  1.00 34.94  ? 6   TYR A CG    1 
ATOM   54   C  CD1   . TYR A 1 34  ? 12.711  4.787   41.002  1.00 36.84  ? 6   TYR A CD1   1 
ATOM   55   C  CD2   . TYR A 1 34  ? 12.640  7.098   41.561  1.00 35.31  ? 6   TYR A CD2   1 
ATOM   56   C  CE1   . TYR A 1 34  ? 13.731  4.589   41.910  1.00 37.28  ? 6   TYR A CE1   1 
ATOM   57   C  CE2   . TYR A 1 34  ? 13.670  6.914   42.456  1.00 35.11  ? 6   TYR A CE2   1 
ATOM   58   C  CZ    . TYR A 1 34  ? 14.206  5.658   42.632  1.00 37.03  ? 6   TYR A CZ    1 
ATOM   59   O  OH    . TYR A 1 34  ? 15.227  5.480   43.551  1.00 38.55  ? 6   TYR A OH    1 
ATOM   60   N  N     . ILE A 1 35  ? 9.601   3.589   40.297  1.00 32.07  ? 7   ILE A N     1 
ATOM   61   C  CA    . ILE A 1 35  ? 9.775   2.220   40.739  1.00 32.82  ? 7   ILE A CA    1 
ATOM   62   C  C     . ILE A 1 35  ? 11.006  1.674   40.032  1.00 37.54  ? 7   ILE A C     1 
ATOM   63   O  O     . ILE A 1 35  ? 11.392  2.139   38.962  1.00 40.68  ? 7   ILE A O     1 
ATOM   64   C  CB    . ILE A 1 35  ? 8.544   1.348   40.444  1.00 40.74  ? 7   ILE A CB    1 
ATOM   65   C  CG1   . ILE A 1 35  ? 8.199   1.445   38.961  1.00 36.98  ? 7   ILE A CG1   1 
ATOM   66   C  CG2   . ILE A 1 35  ? 7.354   1.784   41.297  1.00 39.34  ? 7   ILE A CG2   1 
ATOM   67   C  CD1   . ILE A 1 35  ? 7.078   0.523   38.553  1.00 42.06  ? 7   ILE A CD1   1 
ATOM   68   N  N     . SER A 1 36  ? 11.618  0.674   40.648  1.00 39.02  ? 8   SER A N     1 
ATOM   69   C  CA    . SER A 1 36  ? 12.778  0.023   40.072  1.00 44.89  ? 8   SER A CA    1 
ATOM   70   C  C     . SER A 1 36  ? 12.846  -1.393  40.604  1.00 42.25  ? 8   SER A C     1 
ATOM   71   O  O     . SER A 1 36  ? 12.086  -1.785  41.489  1.00 41.98  ? 8   SER A O     1 
ATOM   72   C  CB    . SER A 1 36  ? 14.064  0.782   40.394  1.00 41.95  ? 8   SER A CB    1 
ATOM   73   O  OG    . SER A 1 36  ? 14.365  0.697   41.773  1.00 40.53  ? 8   SER A OG    1 
ATOM   74   N  N     . LYS A 1 37  ? 13.789  -2.155  40.061  1.00 45.58  ? 9   LYS A N     1 
ATOM   75   C  CA    . LYS A 1 37  ? 13.976  -3.558  40.387  1.00 39.86  ? 9   LYS A CA    1 
ATOM   76   C  C     . LYS A 1 37  ? 15.369  -3.737  40.966  1.00 40.48  ? 9   LYS A C     1 
ATOM   77   O  O     . LYS A 1 37  ? 16.331  -3.165  40.445  1.00 45.89  ? 9   LYS A O     1 
ATOM   78   C  CB    . LYS A 1 37  ? 13.796  -4.419  39.116  1.00 46.50  ? 9   LYS A CB    1 
ATOM   79   C  CG    . LYS A 1 37  ? 13.234  -5.818  39.301  1.00 62.90  ? 9   LYS A CG    1 
ATOM   80   C  CD    . LYS A 1 37  ? 12.991  -6.457  37.925  1.00 68.14  ? 9   LYS A CD    1 
ATOM   81   C  CE    . LYS A 1 37  ? 13.648  -7.822  37.775  1.00 76.91  ? 9   LYS A CE    1 
ATOM   82   N  NZ    . LYS A 1 37  ? 12.801  -8.777  36.976  1.00 77.56  ? 9   LYS A NZ    1 
ATOM   83   N  N     . PHE A 1 38  ? 15.476  -4.517  42.046  1.00 40.55  ? 10  PHE A N     1 
ATOM   84   C  CA    . PHE A 1 38  ? 16.788  -4.918  42.547  1.00 42.43  ? 10  PHE A CA    1 
ATOM   85   C  C     . PHE A 1 38  ? 17.575  -5.541  41.405  1.00 49.06  ? 10  PHE A C     1 
ATOM   86   O  O     . PHE A 1 38  ? 17.100  -6.474  40.756  1.00 49.08  ? 10  PHE A O     1 
ATOM   87   C  CB    . PHE A 1 38  ? 16.670  -5.952  43.674  1.00 43.74  ? 10  PHE A CB    1 
ATOM   88   C  CG    . PHE A 1 38  ? 16.179  -5.412  44.998  1.00 46.73  ? 10  PHE A CG    1 
ATOM   89   C  CD1   . PHE A 1 38  ? 15.435  -4.244  45.084  1.00 40.78  ? 10  PHE A CD1   1 
ATOM   90   C  CD2   . PHE A 1 38  ? 16.410  -6.140  46.159  1.00 46.94  ? 10  PHE A CD2   1 
ATOM   91   C  CE1   . PHE A 1 38  ? 14.964  -3.790  46.312  1.00 41.13  ? 10  PHE A CE1   1 
ATOM   92   C  CE2   . PHE A 1 38  ? 15.949  -5.696  47.391  1.00 45.85  ? 10  PHE A CE2   1 
ATOM   93   C  CZ    . PHE A 1 38  ? 15.219  -4.529  47.471  1.00 41.20  ? 10  PHE A CZ    1 
ATOM   94   N  N     . SER A 1 39  ? 18.773  -5.023  41.149  1.00 52.41  ? 11  SER A N     1 
ATOM   95   C  CA    . SER A 1 39  ? 19.613  -5.674  40.154  1.00 53.70  ? 11  SER A CA    1 
ATOM   96   C  C     . SER A 1 39  ? 20.270  -6.918  40.719  1.00 58.02  ? 11  SER A C     1 
ATOM   97   O  O     . SER A 1 39  ? 20.672  -7.802  39.957  1.00 66.20  ? 11  SER A O     1 
ATOM   98   C  CB    . SER A 1 39  ? 20.679  -4.710  39.645  1.00 54.04  ? 11  SER A CB    1 
ATOM   99   O  OG    . SER A 1 39  ? 21.576  -4.392  40.687  1.00 59.07  ? 11  SER A OG    1 
ATOM   100  N  N     . ARG A 1 40  ? 20.365  -6.993  42.038  1.00 55.09  ? 12  ARG A N     1 
ATOM   101  C  CA    A ARG A 1 40  ? 20.953  -8.118  42.747  0.68 58.35  ? 12  ARG A CA    1 
ATOM   102  C  CA    B ARG A 1 40  ? 20.962  -8.112  42.748  0.32 58.36  ? 12  ARG A CA    1 
ATOM   103  C  C     . ARG A 1 40  ? 20.262  -8.206  44.099  1.00 58.25  ? 12  ARG A C     1 
ATOM   104  O  O     . ARG A 1 40  ? 19.695  -7.219  44.571  1.00 57.01  ? 12  ARG A O     1 
ATOM   105  C  CB    A ARG A 1 40  ? 22.469  -7.940  42.934  0.68 59.94  ? 12  ARG A CB    1 
ATOM   106  C  CB    B ARG A 1 40  ? 22.475  -7.904  42.919  0.32 59.91  ? 12  ARG A CB    1 
ATOM   107  C  CG    A ARG A 1 40  ? 22.859  -6.718  43.741  0.68 56.41  ? 12  ARG A CG    1 
ATOM   108  C  CG    B ARG A 1 40  ? 23.287  -8.339  41.703  0.32 60.24  ? 12  ARG A CG    1 
ATOM   109  C  CD    A ARG A 1 40  ? 24.368  -6.514  43.750  0.68 58.37  ? 12  ARG A CD    1 
ATOM   110  C  CD    B ARG A 1 40  ? 23.896  -7.131  40.990  0.32 59.72  ? 12  ARG A CD    1 
ATOM   111  N  NE    A ARG A 1 40  ? 24.768  -5.421  44.628  0.68 59.46  ? 12  ARG A NE    1 
ATOM   112  N  NE    B ARG A 1 40  ? 23.965  -5.968  41.867  0.32 58.35  ? 12  ARG A NE    1 
ATOM   113  C  CZ    A ARG A 1 40  ? 24.733  -5.460  45.953  0.68 59.17  ? 12  ARG A CZ    1 
ATOM   114  C  CZ    B ARG A 1 40  ? 24.774  -4.934  41.683  0.32 60.73  ? 12  ARG A CZ    1 
ATOM   115  N  NH1   A ARG A 1 40  ? 24.382  -6.555  46.605  0.68 52.42  ? 12  ARG A NH1   1 
ATOM   116  N  NH1   B ARG A 1 40  ? 25.479  -4.797  40.572  0.32 60.42  ? 12  ARG A NH1   1 
ATOM   117  N  NH2   A ARG A 1 40  ? 25.052  -4.368  46.643  0.68 58.40  ? 12  ARG A NH2   1 
ATOM   118  N  NH2   B ARG A 1 40  ? 24.880  -4.015  42.638  0.32 60.99  ? 12  ARG A NH2   1 
ATOM   119  N  N     . PRO A 1 41  ? 20.283  -9.374  44.742  1.00 60.40  ? 13  PRO A N     1 
ATOM   120  C  CA    . PRO A 1 41  ? 19.679  -9.429  46.082  1.00 59.74  ? 13  PRO A CA    1 
ATOM   121  C  C     . PRO A 1 41  ? 20.396  -8.494  47.046  1.00 61.49  ? 13  PRO A C     1 
ATOM   122  O  O     . PRO A 1 41  ? 21.621  -8.358  47.021  1.00 64.15  ? 13  PRO A O     1 
ATOM   123  C  CB    . PRO A 1 41  ? 19.807  -10.903 46.489  1.00 55.76  ? 13  PRO A CB    1 
ATOM   124  C  CG    . PRO A 1 41  ? 20.722  -11.542 45.523  1.00 59.48  ? 13  PRO A CG    1 
ATOM   125  C  CD    . PRO A 1 41  ? 21.115  -10.559 44.464  1.00 63.97  ? 13  PRO A CD    1 
ATOM   126  N  N     . LEU A 1 42  ? 19.606  -7.805  47.865  1.00 53.95  ? 14  LEU A N     1 
ATOM   127  C  CA    . LEU A 1 42  ? 20.097  -6.826  48.823  1.00 50.76  ? 14  LEU A CA    1 
ATOM   128  C  C     . LEU A 1 42  ? 19.601  -7.226  50.199  1.00 46.63  ? 14  LEU A C     1 
ATOM   129  O  O     . LEU A 1 42  ? 18.406  -7.484  50.374  1.00 56.21  ? 14  LEU A O     1 
ATOM   130  C  CB    . LEU A 1 42  ? 19.593  -5.425  48.472  1.00 46.42  ? 14  LEU A CB    1 
ATOM   131  C  CG    . LEU A 1 42  ? 19.973  -4.915  47.091  1.00 53.85  ? 14  LEU A CG    1 
ATOM   132  C  CD1   . LEU A 1 42  ? 19.311  -3.571  46.821  1.00 44.61  ? 14  LEU A CD1   1 
ATOM   133  C  CD2   . LEU A 1 42  ? 21.491  -4.811  46.995  1.00 55.58  ? 14  LEU A CD2   1 
ATOM   134  N  N     . SER A 1 43  ? 20.505  -7.289  51.168  1.00 50.08  ? 15  SER A N     1 
ATOM   135  C  CA    . SER A 1 43  ? 20.088  -7.604  52.527  1.00 47.19  ? 15  SER A CA    1 
ATOM   136  C  C     . SER A 1 43  ? 19.363  -6.414  53.155  1.00 51.53  ? 15  SER A C     1 
ATOM   137  O  O     . SER A 1 43  ? 19.486  -5.264  52.713  1.00 46.03  ? 15  SER A O     1 
ATOM   138  C  CB    . SER A 1 43  ? 21.294  -7.981  53.393  1.00 54.07  ? 15  SER A CB    1 
ATOM   139  O  OG    . SER A 1 43  ? 22.131  -6.859  53.609  1.00 57.53  ? 15  SER A OG    1 
ATOM   140  N  N     . GLY A 1 44  ? 18.619  -6.704  54.222  1.00 44.23  ? 16  GLY A N     1 
ATOM   141  C  CA    . GLY A 1 44  ? 17.939  -5.646  54.946  1.00 47.04  ? 16  GLY A CA    1 
ATOM   142  C  C     . GLY A 1 44  ? 18.897  -4.605  55.489  1.00 50.45  ? 16  GLY A C     1 
ATOM   143  O  O     . GLY A 1 44  ? 18.554  -3.423  55.574  1.00 44.57  ? 16  GLY A O     1 
ATOM   144  N  N     . ASP A 1 45  ? 20.118  -5.020  55.843  1.00 51.34  ? 17  ASP A N     1 
ATOM   145  C  CA    . ASP A 1 45  ? 21.110  -4.056  56.305  1.00 50.70  ? 17  ASP A CA    1 
ATOM   146  C  C     . ASP A 1 45  ? 21.617  -3.183  55.166  1.00 45.69  ? 17  ASP A C     1 
ATOM   147  O  O     . ASP A 1 45  ? 21.890  -1.993  55.375  1.00 48.41  ? 17  ASP A O     1 
ATOM   148  C  CB    . ASP A 1 45  ? 22.265  -4.779  56.996  1.00 52.57  ? 17  ASP A CB    1 
ATOM   149  C  CG    . ASP A 1 45  ? 21.853  -5.366  58.334  1.00 68.83  ? 17  ASP A CG    1 
ATOM   150  O  OD1   . ASP A 1 45  ? 21.644  -4.595  59.297  1.00 73.25  ? 17  ASP A OD1   1 
ATOM   151  O  OD2   . ASP A 1 45  ? 21.724  -6.604  58.421  1.00 78.62  ? 17  ASP A OD2   1 
ATOM   152  N  N     . GLU A 1 46  ? 21.740  -3.730  53.952  1.00 39.03  ? 18  GLU A N     1 
ATOM   153  C  CA    . GLU A 1 46  ? 22.164  -2.882  52.836  1.00 43.22  ? 18  GLU A CA    1 
ATOM   154  C  C     . GLU A 1 46  ? 21.093  -1.850  52.502  1.00 36.71  ? 18  GLU A C     1 
ATOM   155  O  O     . GLU A 1 46  ? 21.406  -0.714  52.118  1.00 39.25  ? 18  GLU A O     1 
ATOM   156  C  CB    . GLU A 1 46  ? 22.466  -3.719  51.596  1.00 45.99  ? 18  GLU A CB    1 
ATOM   157  C  CG    . GLU A 1 46  ? 23.865  -4.294  51.512  1.00 62.94  ? 18  GLU A CG    1 
ATOM   158  C  CD    . GLU A 1 46  ? 23.910  -5.498  50.584  1.00 64.85  ? 18  GLU A CD    1 
ATOM   159  O  OE1   . GLU A 1 46  ? 23.447  -6.586  51.007  1.00 66.89  ? 18  GLU A OE1   1 
ATOM   160  O  OE2   . GLU A 1 46  ? 24.415  -5.354  49.442  1.00 66.78  ? 18  GLU A OE2   1 
ATOM   161  N  N     . ILE A 1 47  ? 19.822  -2.235  52.622  1.00 45.28  ? 19  ILE A N     1 
ATOM   162  C  CA    . ILE A 1 47  ? 18.740  -1.294  52.353  1.00 41.69  ? 19  ILE A CA    1 
ATOM   163  C  C     . ILE A 1 47  ? 18.711  -0.206  53.422  1.00 37.28  ? 19  ILE A C     1 
ATOM   164  O  O     . ILE A 1 47  ? 18.510  0.976   53.122  1.00 37.34  ? 19  ILE A O     1 
ATOM   165  C  CB    . ILE A 1 47  ? 17.400  -2.047  52.257  1.00 39.94  ? 19  ILE A CB    1 
ATOM   166  C  CG1   . ILE A 1 47  ? 17.369  -2.886  50.977  1.00 43.08  ? 19  ILE A CG1   1 
ATOM   167  C  CG2   . ILE A 1 47  ? 16.240  -1.068  52.226  1.00 35.20  ? 19  ILE A CG2   1 
ATOM   168  C  CD1   . ILE A 1 47  ? 16.559  -4.139  51.110  1.00 47.22  ? 19  ILE A CD1   1 
ATOM   169  N  N     . GLU A 1 48  ? 18.910  -0.592  54.682  1.00 36.08  ? 20  GLU A N     1 
ATOM   170  C  CA    . GLU A 1 48  ? 19.044  0.384   55.759  1.00 41.85  ? 20  GLU A CA    1 
ATOM   171  C  C     . GLU A 1 48  ? 20.168  1.375   55.471  1.00 41.27  ? 20  GLU A C     1 
ATOM   172  O  O     . GLU A 1 48  ? 20.004  2.584   55.671  1.00 37.67  ? 20  GLU A O     1 
ATOM   173  C  CB    . GLU A 1 48  ? 19.274  -0.357  57.074  1.00 45.14  ? 20  GLU A CB    1 
ATOM   174  C  CG    . GLU A 1 48  ? 19.229  0.491   58.332  1.00 60.89  ? 20  GLU A CG    1 
ATOM   175  C  CD    . GLU A 1 48  ? 19.313  -0.357  59.599  1.00 67.98  ? 20  GLU A CD    1 
ATOM   176  O  OE1   . GLU A 1 48  ? 20.028  -1.384  59.588  1.00 70.93  ? 20  GLU A OE1   1 
ATOM   177  O  OE2   . GLU A 1 48  ? 18.667  0.005   60.607  1.00 80.98  ? 20  GLU A OE2   1 
ATOM   178  N  N     . ALA A 1 49  ? 21.301  0.890   54.945  1.00 41.76  ? 21  ALA A N     1 
ATOM   179  C  CA    . ALA A 1 49  ? 22.422  1.782   54.665  1.00 41.28  ? 21  ALA A CA    1 
ATOM   180  C  C     . ALA A 1 49  ? 22.093  2.740   53.534  1.00 39.55  ? 21  ALA A C     1 
ATOM   181  O  O     . ALA A 1 49  ? 22.459  3.922   53.585  1.00 38.46  ? 21  ALA A O     1 
ATOM   182  C  CB    . ALA A 1 49  ? 23.681  0.974   54.327  1.00 43.36  ? 21  ALA A CB    1 
ATOM   183  N  N     . ILE A 1 50  ? 21.404  2.247   52.504  1.00 36.72  ? 22  ILE A N     1 
ATOM   184  C  CA    . ILE A 1 50  ? 20.993  3.112   51.408  1.00 33.51  ? 22  ILE A CA    1 
ATOM   185  C  C     . ILE A 1 50  ? 20.115  4.231   51.945  1.00 37.32  ? 22  ILE A C     1 
ATOM   186  O  O     . ILE A 1 50  ? 20.284  5.411   51.603  1.00 39.90  ? 22  ILE A O     1 
ATOM   187  C  CB    . ILE A 1 50  ? 20.269  2.285   50.333  1.00 39.88  ? 22  ILE A CB    1 
ATOM   188  C  CG1   . ILE A 1 50  ? 21.272  1.377   49.607  1.00 47.09  ? 22  ILE A CG1   1 
ATOM   189  C  CG2   . ILE A 1 50  ? 19.582  3.204   49.327  1.00 44.74  ? 22  ILE A CG2   1 
ATOM   190  C  CD1   . ILE A 1 50  ? 20.635  0.494   48.554  1.00 49.80  ? 22  ILE A CD1   1 
ATOM   191  N  N     . GLY A 1 51  ? 19.168  3.870   52.813  1.00 34.90  ? 23  GLY A N     1 
ATOM   192  C  CA    . GLY A 1 51  ? 18.279  4.869   53.371  1.00 32.76  ? 23  GLY A CA    1 
ATOM   193  C  C     . GLY A 1 51  ? 19.021  5.871   54.235  1.00 39.97  ? 23  GLY A C     1 
ATOM   194  O  O     . GLY A 1 51  ? 18.736  7.069   54.198  1.00 34.29  ? 23  GLY A O     1 
ATOM   195  N  N     . ARG A 1 52  ? 19.999  5.399   55.009  1.00 34.74  ? 24  ARG A N     1 
ATOM   196  C  CA    A ARG A 1 52  ? 20.686  6.311   55.914  0.70 34.68  ? 24  ARG A CA    1 
ATOM   197  C  CA    B ARG A 1 52  ? 20.731  6.283   55.916  0.30 34.78  ? 24  ARG A CA    1 
ATOM   198  C  C     . ARG A 1 52  ? 21.624  7.252   55.162  1.00 33.80  ? 24  ARG A C     1 
ATOM   199  O  O     . ARG A 1 52  ? 21.690  8.442   55.495  1.00 37.13  ? 24  ARG A O     1 
ATOM   200  C  CB    A ARG A 1 52  ? 21.399  5.510   56.999  0.70 37.90  ? 24  ARG A CB    1 
ATOM   201  C  CB    B ARG A 1 52  ? 21.547  5.459   56.908  0.30 37.71  ? 24  ARG A CB    1 
ATOM   202  C  CG    A ARG A 1 52  ? 20.390  4.988   58.059  0.70 36.53  ? 24  ARG A CG    1 
ATOM   203  C  CG    B ARG A 1 52  ? 22.271  6.313   57.922  0.30 38.09  ? 24  ARG A CG    1 
ATOM   204  C  CD    A ARG A 1 52  ? 21.076  4.627   59.373  0.70 45.40  ? 24  ARG A CD    1 
ATOM   205  C  CD    B ARG A 1 52  ? 23.068  5.507   58.912  0.30 35.82  ? 24  ARG A CD    1 
ATOM   206  N  NE    A ARG A 1 52  ? 21.313  5.797   60.213  0.70 42.32  ? 24  ARG A NE    1 
ATOM   207  N  NE    B ARG A 1 52  ? 22.153  4.715   59.723  0.30 42.64  ? 24  ARG A NE    1 
ATOM   208  C  CZ    A ARG A 1 52  ? 22.515  6.325   60.424  0.70 36.71  ? 24  ARG A CZ    1 
ATOM   209  C  CZ    B ARG A 1 52  ? 21.511  5.186   60.785  0.30 39.18  ? 24  ARG A CZ    1 
ATOM   210  N  NH1   A ARG A 1 52  ? 23.598  5.819   59.863  0.70 36.27  ? 24  ARG A NH1   1 
ATOM   211  N  NH1   B ARG A 1 52  ? 21.597  6.459   61.134  0.30 38.29  ? 24  ARG A NH1   1 
ATOM   212  N  NH2   A ARG A 1 52  ? 22.623  7.406   61.187  0.70 32.38  ? 24  ARG A NH2   1 
ATOM   213  N  NH2   B ARG A 1 52  ? 20.730  4.370   61.487  0.30 39.80  ? 24  ARG A NH2   1 
ATOM   214  N  N     . ILE A 1 53  ? 22.326  6.761   54.138  1.00 37.79  ? 25  ILE A N     1 
ATOM   215  C  CA    . ILE A 1 53  ? 23.129  7.652   53.307  1.00 36.90  ? 25  ILE A CA    1 
ATOM   216  C  C     . ILE A 1 53  ? 22.233  8.626   52.562  1.00 39.60  ? 25  ILE A C     1 
ATOM   217  O  O     . ILE A 1 53  ? 22.543  9.817   52.454  1.00 37.49  ? 25  ILE A O     1 
ATOM   218  C  CB    . ILE A 1 53  ? 24.016  6.848   52.333  1.00 45.23  ? 25  ILE A CB    1 
ATOM   219  C  CG1   . ILE A 1 53  ? 24.891  5.840   53.088  1.00 50.56  ? 25  ILE A CG1   1 
ATOM   220  C  CG2   . ILE A 1 53  ? 24.882  7.790   51.476  1.00 47.68  ? 25  ILE A CG2   1 
ATOM   221  C  CD1   . ILE A 1 53  ? 25.745  6.445   54.184  1.00 63.36  ? 25  ILE A CD1   1 
ATOM   222  N  N     . SER A 1 54  ? 21.087  8.149   52.055  1.00 38.15  ? 26  SER A N     1 
ATOM   223  C  CA    . SER A 1 54  ? 20.201  9.053   51.326  1.00 32.26  ? 26  SER A CA    1 
ATOM   224  C  C     . SER A 1 54  ? 19.687  10.150  52.235  1.00 34.29  ? 26  SER A C     1 
ATOM   225  O  O     . SER A 1 54  ? 19.570  11.310  51.821  1.00 35.14  ? 26  SER A O     1 
ATOM   226  C  CB    . SER A 1 54  ? 19.025  8.287   50.711  1.00 33.84  ? 26  SER A CB    1 
ATOM   227  O  OG    . SER A 1 54  ? 19.505  7.204   49.932  1.00 37.54  ? 26  SER A OG    1 
ATOM   228  N  N     . SER A 1 55  ? 19.359  9.799   53.478  1.00 31.67  ? 27  SER A N     1 
ATOM   229  C  CA    . SER A 1 55  ? 18.841  10.801  54.393  1.00 30.12  ? 27  SER A CA    1 
ATOM   230  C  C     . SER A 1 55  ? 19.897  11.863  54.657  1.00 32.96  ? 27  SER A C     1 
ATOM   231  O  O     . SER A 1 55  ? 19.606  13.063  54.634  1.00 35.74  ? 27  SER A O     1 
ATOM   232  C  CB    . SER A 1 55  ? 18.387  10.133  55.694  1.00 31.67  ? 27  SER A CB    1 
ATOM   233  O  OG    . SER A 1 55  ? 17.899  11.099  56.610  1.00 33.11  ? 27  SER A OG    1 
ATOM   234  N  N     . GLN A 1 56  ? 21.141  11.434  54.861  1.00 34.04  ? 28  GLN A N     1 
ATOM   235  C  CA    . GLN A 1 56  ? 22.226  12.376  55.110  1.00 35.60  ? 28  GLN A CA    1 
ATOM   236  C  C     . GLN A 1 56  ? 22.453  13.295  53.906  1.00 36.64  ? 28  GLN A C     1 
ATOM   237  O  O     . GLN A 1 56  ? 22.467  14.525  54.043  1.00 39.61  ? 28  GLN A O     1 
ATOM   238  C  CB    . GLN A 1 56  ? 23.493  11.599  55.463  1.00 33.67  ? 28  GLN A CB    1 
ATOM   239  C  CG    . GLN A 1 56  ? 24.670  12.494  55.878  1.00 38.58  ? 28  GLN A CG    1 
ATOM   240  C  CD    . GLN A 1 56  ? 25.992  11.728  56.030  1.00 49.29  ? 28  GLN A CD    1 
ATOM   241  O  OE1   . GLN A 1 56  ? 26.190  10.662  55.445  1.00 54.31  ? 28  GLN A OE1   1 
ATOM   242  N  NE2   . GLN A 1 56  ? 26.895  12.276  56.836  1.00 55.85  ? 28  GLN A NE2   1 
ATOM   243  N  N     . LYS A 1 57  ? 22.589  12.712  52.712  1.00 32.22  ? 29  LYS A N     1 
ATOM   244  C  CA    . LYS A 1 57  ? 22.778  13.510  51.499  1.00 36.52  ? 29  LYS A CA    1 
ATOM   245  C  C     . LYS A 1 57  ? 21.578  14.417  51.224  1.00 42.07  ? 29  LYS A C     1 
ATOM   246  O  O     . LYS A 1 57  ? 21.739  15.603  50.920  1.00 37.62  ? 29  LYS A O     1 
ATOM   247  C  CB    . LYS A 1 57  ? 23.031  12.578  50.314  1.00 42.48  ? 29  LYS A CB    1 
ATOM   248  C  CG    . LYS A 1 57  ? 24.328  11.773  50.415  1.00 52.64  ? 29  LYS A CG    1 
ATOM   249  C  CD    . LYS A 1 57  ? 25.056  11.720  49.075  1.00 67.16  ? 29  LYS A CD    1 
ATOM   250  C  CE    . LYS A 1 57  ? 25.320  13.115  48.508  1.00 75.13  ? 29  LYS A CE    1 
ATOM   251  N  NZ    . LYS A 1 57  ? 26.654  13.684  48.873  1.00 75.65  ? 29  LYS A NZ    1 
ATOM   252  N  N     . ASN A 1 58  ? 20.359  13.884  51.337  1.00 36.78  ? 30  ASN A N     1 
ATOM   253  C  CA    . ASN A 1 58  ? 19.187  14.707  51.043  1.00 35.92  ? 30  ASN A CA    1 
ATOM   254  C  C     . ASN A 1 58  ? 19.061  15.861  52.016  1.00 39.27  ? 30  ASN A C     1 
ATOM   255  O  O     . ASN A 1 58  ? 18.636  16.951  51.625  1.00 36.93  ? 30  ASN A O     1 
ATOM   256  C  CB    . ASN A 1 58  ? 17.919  13.854  51.050  1.00 32.69  ? 30  ASN A CB    1 
ATOM   257  C  CG    . ASN A 1 58  ? 17.811  12.994  49.817  1.00 37.78  ? 30  ASN A CG    1 
ATOM   258  O  OD1   . ASN A 1 58  ? 18.666  13.068  48.928  1.00 38.58  ? 30  ASN A OD1   1 
ATOM   259  N  ND2   . ASN A 1 58  ? 16.785  12.140  49.763  1.00 35.32  ? 30  ASN A ND2   1 
ATOM   260  N  N     . GLN A 1 59  ? 19.401  15.641  53.293  1.00 31.38  ? 31  GLN A N     1 
ATOM   261  C  CA    A GLN A 1 59  ? 19.348  16.728  54.268  0.62 38.40  ? 31  GLN A CA    1 
ATOM   262  C  CA    B GLN A 1 59  ? 19.339  16.732  54.261  0.38 38.38  ? 31  GLN A CA    1 
ATOM   263  C  C     . GLN A 1 59  ? 20.229  17.898  53.842  1.00 41.76  ? 31  GLN A C     1 
ATOM   264  O  O     . GLN A 1 59  ? 19.841  19.065  53.987  1.00 37.13  ? 31  GLN A O     1 
ATOM   265  C  CB    A GLN A 1 59  ? 19.806  16.241  55.638  0.62 36.75  ? 31  GLN A CB    1 
ATOM   266  C  CB    B GLN A 1 59  ? 19.737  16.235  55.648  0.38 36.82  ? 31  GLN A CB    1 
ATOM   267  C  CG    A GLN A 1 59  ? 19.495  17.227  56.738  0.62 40.51  ? 31  GLN A CG    1 
ATOM   268  C  CG    B GLN A 1 59  ? 19.567  17.287  56.725  0.38 40.52  ? 31  GLN A CG    1 
ATOM   269  C  CD    A GLN A 1 59  ? 20.607  18.242  56.934  0.62 42.56  ? 31  GLN A CD    1 
ATOM   270  C  CD    B GLN A 1 59  ? 19.804  16.761  58.129  0.38 45.86  ? 31  GLN A CD    1 
ATOM   271  O  OE1   A GLN A 1 59  ? 21.763  17.992  56.589  0.62 41.94  ? 31  GLN A OE1   1 
ATOM   272  O  OE1   B GLN A 1 59  ? 20.013  15.567  58.338  0.38 46.67  ? 31  GLN A OE1   1 
ATOM   273  N  NE2   A GLN A 1 59  ? 20.261  19.393  57.499  0.62 44.07  ? 31  GLN A NE2   1 
ATOM   274  N  NE2   B GLN A 1 59  ? 19.798  17.664  59.099  0.38 45.42  ? 31  GLN A NE2   1 
ATOM   275  N  N     . GLN A 1 60  ? 21.429  17.597  53.339  1.00 38.78  ? 32  GLN A N     1 
ATOM   276  C  CA    . GLN A 1 60  ? 22.357  18.604  52.830  1.00 44.01  ? 32  GLN A CA    1 
ATOM   277  C  C     . GLN A 1 60  ? 21.819  19.296  51.581  1.00 48.06  ? 32  GLN A C     1 
ATOM   278  O  O     . GLN A 1 60  ? 22.236  20.416  51.276  1.00 48.70  ? 32  GLN A O     1 
ATOM   279  C  CB    . GLN A 1 60  ? 23.700  17.942  52.498  1.00 38.90  ? 32  GLN A CB    1 
ATOM   280  C  CG    . GLN A 1 60  ? 24.567  17.575  53.714  1.00 47.02  ? 32  GLN A CG    1 
ATOM   281  C  CD    . GLN A 1 60  ? 24.900  18.759  54.625  1.00 62.34  ? 32  GLN A CD    1 
ATOM   282  O  OE1   . GLN A 1 60  ? 24.413  18.849  55.768  1.00 53.04  ? 32  GLN A OE1   1 
ATOM   283  N  NE2   . GLN A 1 60  ? 25.771  19.649  54.141  1.00 60.33  ? 32  GLN A NE2   1 
ATOM   284  N  N     . ALA A 1 61  ? 20.906  18.656  50.852  1.00 44.34  ? 33  ALA A N     1 
ATOM   285  C  CA    . ALA A 1 61  ? 20.352  19.213  49.625  1.00 36.45  ? 33  ALA A CA    1 
ATOM   286  C  C     . ALA A 1 61  ? 18.956  19.799  49.805  1.00 45.07  ? 33  ALA A C     1 
ATOM   287  O  O     . ALA A 1 61  ? 18.388  20.328  48.841  1.00 51.82  ? 33  ALA A O     1 
ATOM   288  C  CB    . ALA A 1 61  ? 20.346  18.140  48.528  1.00 45.58  ? 33  ALA A CB    1 
ATOM   289  N  N     . ASN A 1 62  ? 18.401  19.741  51.017  1.00 45.47  ? 34  ASN A N     1 
ATOM   290  C  CA    . ASN A 1 62  ? 17.039  20.198  51.285  1.00 46.10  ? 34  ASN A CA    1 
ATOM   291  C  C     . ASN A 1 62  ? 16.013  19.407  50.473  1.00 44.28  ? 34  ASN A C     1 
ATOM   292  O  O     . ASN A 1 62  ? 14.992  19.943  50.032  1.00 44.53  ? 34  ASN A O     1 
ATOM   293  C  CB    . ASN A 1 62  ? 16.885  21.699  51.032  1.00 51.05  ? 34  ASN A CB    1 
ATOM   294  C  CG    . ASN A 1 62  ? 15.730  22.297  51.808  1.00 55.90  ? 34  ASN A CG    1 
ATOM   295  O  OD1   . ASN A 1 62  ? 15.433  21.880  52.929  1.00 65.18  ? 34  ASN A OD1   1 
ATOM   296  N  ND2   . ASN A 1 62  ? 15.051  23.265  51.203  1.00 56.34  ? 34  ASN A ND2   1 
ATOM   297  N  N     . VAL A 1 63  ? 16.289  18.122  50.271  1.00 43.04  ? 35  VAL A N     1 
ATOM   298  C  CA    . VAL A 1 63  ? 15.381  17.208  49.588  1.00 38.12  ? 35  VAL A CA    1 
ATOM   299  C  C     . VAL A 1 63  ? 14.728  16.314  50.636  1.00 41.10  ? 35  VAL A C     1 
ATOM   300  O  O     . VAL A 1 63  ? 15.354  15.983  51.650  1.00 31.17  ? 35  VAL A O     1 
ATOM   301  C  CB    . VAL A 1 63  ? 16.148  16.400  48.523  1.00 39.99  ? 35  VAL A CB    1 
ATOM   302  C  CG1   . VAL A 1 63  ? 15.417  15.121  48.122  1.00 39.60  ? 35  VAL A CG1   1 
ATOM   303  C  CG2   . VAL A 1 63  ? 16.409  17.291  47.300  1.00 45.03  ? 35  VAL A CG2   1 
ATOM   304  N  N     . THR A 1 64  ? 13.460  15.962  50.419  1.00 30.89  ? 36  THR A N     1 
ATOM   305  C  CA    . THR A 1 64  ? 12.733  15.080  51.333  1.00 34.11  ? 36  THR A CA    1 
ATOM   306  C  C     . THR A 1 64  ? 12.085  13.955  50.530  1.00 35.32  ? 36  THR A C     1 
ATOM   307  O  O     . THR A 1 64  ? 12.032  13.998  49.300  1.00 34.40  ? 36  THR A O     1 
ATOM   308  C  CB    . THR A 1 64  ? 11.659  15.831  52.152  1.00 34.84  ? 36  THR A CB    1 
ATOM   309  O  OG1   . THR A 1 64  ? 10.825  16.623  51.289  1.00 36.57  ? 36  THR A OG1   1 
ATOM   310  C  CG2   . THR A 1 64  ? 12.270  16.722  53.250  1.00 39.11  ? 36  THR A CG2   1 
ATOM   311  N  N     . GLY A 1 65  ? 11.594  12.938  51.225  1.00 29.05  ? 37  GLY A N     1 
ATOM   312  C  CA    . GLY A 1 65  ? 10.847  11.906  50.534  1.00 30.75  ? 37  GLY A CA    1 
ATOM   313  C  C     . GLY A 1 65  ? 10.822  10.608  51.323  1.00 34.85  ? 37  GLY A C     1 
ATOM   314  O  O     . GLY A 1 65  ? 11.069  10.588  52.538  1.00 31.88  ? 37  GLY A O     1 
ATOM   315  N  N     . VAL A 1 66  ? 10.527  9.532   50.599  1.00 30.18  ? 38  VAL A N     1 
ATOM   316  C  CA    . VAL A 1 66  ? 10.319  8.226   51.221  1.00 28.45  ? 38  VAL A CA    1 
ATOM   317  C  C     . VAL A 1 66  ? 10.804  7.155   50.258  1.00 29.96  ? 38  VAL A C     1 
ATOM   318  O  O     . VAL A 1 66  ? 10.684  7.281   49.030  1.00 30.11  ? 38  VAL A O     1 
ATOM   319  C  CB    . VAL A 1 66  ? 8.839   8.013   51.613  1.00 31.00  ? 38  VAL A CB    1 
ATOM   320  C  CG1   . VAL A 1 66  ? 7.926   8.077   50.396  1.00 33.93  ? 38  VAL A CG1   1 
ATOM   321  C  CG2   . VAL A 1 66  ? 8.649   6.681   52.387  1.00 28.83  ? 38  VAL A CG2   1 
ATOM   322  N  N     . LEU A 1 67  ? 11.362  6.100   50.821  1.00 29.34  ? 39  LEU A N     1 
ATOM   323  C  CA    . LEU A 1 67  ? 11.831  4.958   50.048  1.00 29.72  ? 39  LEU A CA    1 
ATOM   324  C  C     . LEU A 1 67  ? 11.215  3.709   50.643  1.00 31.72  ? 39  LEU A C     1 
ATOM   325  O  O     . LEU A 1 67  ? 11.354  3.467   51.847  1.00 33.76  ? 39  LEU A O     1 
ATOM   326  C  CB    . LEU A 1 67  ? 13.366  4.867   50.078  1.00 31.45  ? 39  LEU A CB    1 
ATOM   327  C  CG    . LEU A 1 67  ? 14.017  3.621   49.452  1.00 37.30  ? 39  LEU A CG    1 
ATOM   328  C  CD1   . LEU A 1 67  ? 13.894  3.649   47.947  1.00 38.75  ? 39  LEU A CD1   1 
ATOM   329  C  CD2   . LEU A 1 67  ? 15.496  3.519   49.865  1.00 39.06  ? 39  LEU A CD2   1 
ATOM   330  N  N     . LEU A 1 68  ? 10.534  2.926   49.808  1.00 32.80  ? 40  LEU A N     1 
ATOM   331  C  CA    . LEU A 1 68  ? 9.937   1.663   50.220  1.00 30.96  ? 40  LEU A CA    1 
ATOM   332  C  C     . LEU A 1 68  ? 10.494  0.532   49.375  1.00 35.00  ? 40  LEU A C     1 
ATOM   333  O  O     . LEU A 1 68  ? 10.789  0.708   48.191  1.00 34.75  ? 40  LEU A O     1 
ATOM   334  C  CB    . LEU A 1 68  ? 8.412   1.695   50.095  1.00 33.38  ? 40  LEU A CB    1 
ATOM   335  C  CG    . LEU A 1 68  ? 7.751   2.816   50.877  1.00 37.26  ? 40  LEU A CG    1 
ATOM   336  C  CD1   . LEU A 1 68  ? 7.463   3.990   49.973  1.00 42.90  ? 40  LEU A CD1   1 
ATOM   337  C  CD2   . LEU A 1 68  ? 6.476   2.290   51.515  1.00 41.94  ? 40  LEU A CD2   1 
ATOM   338  N  N     . CYS A 1 69  ? 10.656  -0.630  49.994  1.00 33.09  ? 41  CYS A N     1 
ATOM   339  C  CA    . CYS A 1 69  ? 11.041  -1.817  49.247  1.00 34.30  ? 41  CYS A CA    1 
ATOM   340  C  C     . CYS A 1 69  ? 10.099  -2.955  49.597  1.00 32.65  ? 41  CYS A C     1 
ATOM   341  O  O     . CYS A 1 69  ? 9.542   -3.019  50.697  1.00 30.63  ? 41  CYS A O     1 
ATOM   342  C  CB    . CYS A 1 69  ? 12.517  -2.223  49.488  1.00 35.97  ? 41  CYS A CB    1 
ATOM   343  S  SG    . CYS A 1 69  ? 12.831  -2.888  51.090  1.00 44.50  ? 41  CYS A SG    1 
ATOM   344  N  N     . LEU A 1 70  ? 9.882   -3.821  48.613  1.00 33.45  ? 42  LEU A N     1 
ATOM   345  C  CA    . LEU A 1 70  ? 8.987   -4.960  48.762  1.00 36.08  ? 42  LEU A CA    1 
ATOM   346  C  C     . LEU A 1 70  ? 9.376   -5.968  47.698  1.00 38.14  ? 42  LEU A C     1 
ATOM   347  O  O     . LEU A 1 70  ? 9.305   -5.654  46.504  1.00 37.55  ? 42  LEU A O     1 
ATOM   348  C  CB    . LEU A 1 70  ? 7.518   -4.537  48.615  1.00 36.57  ? 42  LEU A CB    1 
ATOM   349  C  CG    . LEU A 1 70  ? 6.501   -5.671  48.574  1.00 34.06  ? 42  LEU A CG    1 
ATOM   350  C  CD1   . LEU A 1 70  ? 6.430   -6.326  49.939  1.00 38.39  ? 42  LEU A CD1   1 
ATOM   351  C  CD2   . LEU A 1 70  ? 5.138   -5.114  48.182  1.00 38.84  ? 42  LEU A CD2   1 
ATOM   352  N  N     . ASP A 1 71  ? 9.846   -7.136  48.136  1.00 40.17  ? 43  ASP A N     1 
ATOM   353  C  CA    . ASP A 1 71  ? 10.082  -8.290  47.270  1.00 50.26  ? 43  ASP A CA    1 
ATOM   354  C  C     . ASP A 1 71  ? 10.875  -7.911  46.014  1.00 47.92  ? 43  ASP A C     1 
ATOM   355  O  O     . ASP A 1 71  ? 10.502  -8.242  44.886  1.00 49.41  ? 43  ASP A O     1 
ATOM   356  C  CB    . ASP A 1 71  ? 8.755   -8.956  46.905  1.00 56.45  ? 43  ASP A CB    1 
ATOM   357  C  CG    . ASP A 1 71  ? 8.930   -10.393 46.463  1.00 65.57  ? 43  ASP A CG    1 
ATOM   358  O  OD1   . ASP A 1 71  ? 9.456   -11.192 47.264  1.00 61.45  ? 43  ASP A OD1   1 
ATOM   359  O  OD2   . ASP A 1 71  ? 8.560   -10.716 45.314  1.00 64.48  ? 43  ASP A OD2   1 
ATOM   360  N  N     . GLY A 1 72  ? 11.976  -7.185  46.213  1.00 42.23  ? 44  GLY A N     1 
ATOM   361  C  CA    . GLY A 1 72  ? 12.843  -6.843  45.097  1.00 38.83  ? 44  GLY A CA    1 
ATOM   362  C  C     . GLY A 1 72  ? 12.428  -5.640  44.285  1.00 41.89  ? 44  GLY A C     1 
ATOM   363  O  O     . GLY A 1 72  ? 12.977  -5.431  43.196  1.00 44.63  ? 44  GLY A O     1 
ATOM   364  N  N     . ILE A 1 73  ? 11.493  -4.834  44.774  1.00 36.60  ? 45  ILE A N     1 
ATOM   365  C  CA    . ILE A 1 73  ? 11.049  -3.611  44.116  1.00 35.63  ? 45  ILE A CA    1 
ATOM   366  C  C     . ILE A 1 73  ? 11.394  -2.444  45.026  1.00 36.10  ? 45  ILE A C     1 
ATOM   367  O  O     . ILE A 1 73  ? 11.156  -2.514  46.238  1.00 33.46  ? 45  ILE A O     1 
ATOM   368  C  CB    . ILE A 1 73  ? 9.524   -3.635  43.857  1.00 38.74  ? 45  ILE A CB    1 
ATOM   369  C  CG1   . ILE A 1 73  ? 9.105   -4.918  43.136  1.00 44.41  ? 45  ILE A CG1   1 
ATOM   370  C  CG2   . ILE A 1 73  ? 9.054   -2.349  43.134  1.00 34.47  ? 45  ILE A CG2   1 
ATOM   371  C  CD1   . ILE A 1 73  ? 7.700   -5.412  43.576  1.00 48.14  ? 45  ILE A CD1   1 
ATOM   372  N  N     . PHE A 1 74  ? 11.942  -1.377  44.453  1.00 36.82  ? 46  PHE A N     1 
ATOM   373  C  CA    . PHE A 1 74  ? 12.017  -0.099  45.146  1.00 38.46  ? 46  PHE A CA    1 
ATOM   374  C  C     . PHE A 1 74  ? 10.880  0.788   44.667  1.00 38.95  ? 46  PHE A C     1 
ATOM   375  O  O     . PHE A 1 74  ? 10.534  0.784   43.480  1.00 37.56  ? 46  PHE A O     1 
ATOM   376  C  CB    . PHE A 1 74  ? 13.335  0.634   44.879  1.00 31.47  ? 46  PHE A CB    1 
ATOM   377  C  CG    . PHE A 1 74  ? 14.512  0.090   45.642  1.00 39.85  ? 46  PHE A CG    1 
ATOM   378  C  CD1   . PHE A 1 74  ? 14.560  0.152   47.029  1.00 39.12  ? 46  PHE A CD1   1 
ATOM   379  C  CD2   . PHE A 1 74  ? 15.593  -0.453  44.954  1.00 37.84  ? 46  PHE A CD2   1 
ATOM   380  C  CE1   . PHE A 1 74  ? 15.654  -0.331  47.721  1.00 36.49  ? 46  PHE A CE1   1 
ATOM   381  C  CE2   . PHE A 1 74  ? 16.705  -0.940  45.640  1.00 42.23  ? 46  PHE A CE2   1 
ATOM   382  C  CZ    . PHE A 1 74  ? 16.734  -0.886  47.025  1.00 43.71  ? 46  PHE A CZ    1 
ATOM   383  N  N     . PHE A 1 75  ? 10.308  1.546   45.597  1.00 32.70  ? 47  PHE A N     1 
ATOM   384  C  CA    . PHE A 1 75  ? 9.439   2.673   45.303  1.00 30.31  ? 47  PHE A CA    1 
ATOM   385  C  C     . PHE A 1 75  ? 10.052  3.898   45.961  1.00 31.33  ? 47  PHE A C     1 
ATOM   386  O  O     . PHE A 1 75  ? 10.366  3.861   47.155  1.00 33.81  ? 47  PHE A O     1 
ATOM   387  C  CB    . PHE A 1 75  ? 8.026   2.463   45.867  1.00 31.47  ? 47  PHE A CB    1 
ATOM   388  C  CG    . PHE A 1 75  ? 7.432   1.117   45.583  1.00 34.84  ? 47  PHE A CG    1 
ATOM   389  C  CD1   . PHE A 1 75  ? 7.751   0.013   46.364  1.00 36.41  ? 47  PHE A CD1   1 
ATOM   390  C  CD2   . PHE A 1 75  ? 6.499   0.974   44.573  1.00 38.72  ? 47  PHE A CD2   1 
ATOM   391  C  CE1   . PHE A 1 75  ? 7.179   -1.235  46.112  1.00 38.22  ? 47  PHE A CE1   1 
ATOM   392  C  CE2   . PHE A 1 75  ? 5.923   -0.260  44.312  1.00 42.31  ? 47  PHE A CE2   1 
ATOM   393  C  CZ    . PHE A 1 75  ? 6.262   -1.364  45.079  1.00 42.22  ? 47  PHE A CZ    1 
ATOM   394  N  N     . GLN A 1 76  ? 10.177  4.997   45.230  1.00 30.19  ? 48  GLN A N     1 
ATOM   395  C  CA    . GLN A 1 76  ? 10.697  6.187   45.890  1.00 31.31  ? 48  GLN A CA    1 
ATOM   396  C  C     . GLN A 1 76  ? 9.988   7.449   45.429  1.00 33.38  ? 48  GLN A C     1 
ATOM   397  O  O     . GLN A 1 76  ? 9.660   7.610   44.250  1.00 32.70  ? 48  GLN A O     1 
ATOM   398  C  CB    . GLN A 1 76  ? 12.213  6.357   45.665  1.00 29.98  ? 48  GLN A CB    1 
ATOM   399  C  CG    . GLN A 1 76  ? 12.802  7.480   46.481  1.00 31.84  ? 48  GLN A CG    1 
ATOM   400  C  CD    . GLN A 1 76  ? 14.303  7.488   46.419  1.00 39.82  ? 48  GLN A CD    1 
ATOM   401  O  OE1   . GLN A 1 76  ? 14.889  7.205   45.370  1.00 37.36  ? 48  GLN A OE1   1 
ATOM   402  N  NE2   . GLN A 1 76  ? 14.939  7.762   47.544  1.00 35.04  ? 48  GLN A NE2   1 
ATOM   403  N  N     . ILE A 1 77  ? 9.767   8.342   46.383  1.00 30.27  ? 49  ILE A N     1 
ATOM   404  C  CA    . ILE A 1 77  ? 9.284   9.686   46.129  1.00 33.44  ? 49  ILE A CA    1 
ATOM   405  C  C     . ILE A 1 77  ? 10.351  10.648  46.613  1.00 36.53  ? 49  ILE A C     1 
ATOM   406  O  O     . ILE A 1 77  ? 10.821  10.536  47.752  1.00 35.60  ? 49  ILE A O     1 
ATOM   407  C  CB    . ILE A 1 77  ? 7.949   9.962   46.841  1.00 29.66  ? 49  ILE A CB    1 
ATOM   408  C  CG1   . ILE A 1 77  ? 6.880   8.954   46.415  1.00 33.58  ? 49  ILE A CG1   1 
ATOM   409  C  CG2   . ILE A 1 77  ? 7.486   11.382  46.564  1.00 33.28  ? 49  ILE A CG2   1 
ATOM   410  C  CD1   . ILE A 1 77  ? 5.630   9.020   47.294  1.00 36.47  ? 49  ILE A CD1   1 
ATOM   411  N  N     . LEU A 1 78  ? 10.738  11.577  45.748  1.00 34.16  ? 50  LEU A N     1 
ATOM   412  C  CA    . LEU A 1 78  ? 11.708  12.624  46.047  1.00 36.41  ? 50  LEU A CA    1 
ATOM   413  C  C     . LEU A 1 78  ? 11.074  13.970  45.756  1.00 39.41  ? 50  LEU A C     1 
ATOM   414  O  O     . LEU A 1 78  ? 10.402  14.127  44.735  1.00 46.48  ? 50  LEU A O     1 
ATOM   415  C  CB    . LEU A 1 78  ? 12.964  12.472  45.191  1.00 38.09  ? 50  LEU A CB    1 
ATOM   416  C  CG    . LEU A 1 78  ? 13.695  11.152  45.343  1.00 43.67  ? 50  LEU A CG    1 
ATOM   417  C  CD1   . LEU A 1 78  ? 14.376  10.770  44.031  1.00 53.43  ? 50  LEU A CD1   1 
ATOM   418  C  CD2   . LEU A 1 78  ? 14.718  11.298  46.471  1.00 40.95  ? 50  LEU A CD2   1 
ATOM   419  N  N     . GLU A 1 79  ? 11.287  14.943  46.642  1.00 38.77  ? 51  GLU A N     1 
ATOM   420  C  CA    . GLU A 1 79  ? 10.732  16.274  46.448  1.00 37.76  ? 51  GLU A CA    1 
ATOM   421  C  C     . GLU A 1 79  ? 11.737  17.331  46.879  1.00 45.31  ? 51  GLU A C     1 
ATOM   422  O  O     . GLU A 1 79  ? 12.438  17.175  47.884  1.00 40.96  ? 51  GLU A O     1 
ATOM   423  C  CB    . GLU A 1 79  ? 9.415   16.462  47.208  1.00 38.59  ? 51  GLU A CB    1 
ATOM   424  C  CG    . GLU A 1 79  ? 9.509   16.134  48.667  1.00 45.12  ? 51  GLU A CG    1 
ATOM   425  C  CD    . GLU A 1 79  ? 8.156   16.108  49.371  1.00 39.11  ? 51  GLU A CD    1 
ATOM   426  O  OE1   . GLU A 1 79  ? 7.103   16.182  48.700  1.00 41.77  ? 51  GLU A OE1   1 
ATOM   427  O  OE2   . GLU A 1 79  ? 8.147   16.034  50.620  1.00 42.90  ? 51  GLU A OE2   1 
ATOM   428  N  N     . GLY A 1 80  ? 11.791  18.408  46.112  1.00 41.31  ? 52  GLY A N     1 
ATOM   429  C  CA    . GLY A 1 80  ? 12.700  19.499  46.385  1.00 51.57  ? 52  GLY A CA    1 
ATOM   430  C  C     . GLY A 1 80  ? 12.872  20.364  45.148  1.00 58.03  ? 52  GLY A C     1 
ATOM   431  O  O     . GLY A 1 80  ? 12.126  20.247  44.172  1.00 51.09  ? 52  GLY A O     1 
ATOM   432  N  N     . GLU A 1 81  ? 13.881  21.235  45.218  1.00 58.65  ? 53  GLU A N     1 
ATOM   433  C  CA    A GLU A 1 81  ? 14.214  22.110  44.097  0.49 59.90  ? 53  GLU A CA    1 
ATOM   434  C  CA    B GLU A 1 81  ? 14.184  22.112  44.098  0.51 59.90  ? 53  GLU A CA    1 
ATOM   435  C  C     . GLU A 1 81  ? 14.465  21.291  42.847  1.00 52.02  ? 53  GLU A C     1 
ATOM   436  O  O     . GLU A 1 81  ? 15.215  20.312  42.884  1.00 49.43  ? 53  GLU A O     1 
ATOM   437  C  CB    A GLU A 1 81  ? 15.454  22.948  44.421  0.49 62.30  ? 53  GLU A CB    1 
ATOM   438  C  CB    B GLU A 1 81  ? 15.372  23.009  44.442  0.51 62.30  ? 53  GLU A CB    1 
ATOM   439  C  CG    A GLU A 1 81  ? 15.272  23.919  45.559  0.49 59.72  ? 53  GLU A CG    1 
ATOM   440  C  CG    B GLU A 1 81  ? 16.108  23.590  43.251  0.51 64.52  ? 53  GLU A CG    1 
ATOM   441  C  CD    A GLU A 1 81  ? 13.992  24.708  45.417  0.49 69.18  ? 53  GLU A CD    1 
ATOM   442  C  CD    B GLU A 1 81  ? 17.218  24.523  43.677  0.51 70.25  ? 53  GLU A CD    1 
ATOM   443  O  OE1   A GLU A 1 81  ? 13.887  25.480  44.436  0.49 74.30  ? 53  GLU A OE1   1 
ATOM   444  O  OE1   B GLU A 1 81  ? 16.916  25.518  44.370  0.51 70.25  ? 53  GLU A OE1   1 
ATOM   445  O  OE2   A GLU A 1 81  ? 13.092  24.563  46.276  0.49 66.78  ? 53  GLU A OE2   1 
ATOM   446  O  OE2   B GLU A 1 81  ? 18.389  24.270  43.322  0.51 73.36  ? 53  GLU A OE2   1 
ATOM   447  N  N     . ALA A 1 82  ? 13.835  21.696  41.739  1.00 54.66  ? 54  ALA A N     1 
ATOM   448  C  CA    . ALA A 1 82  ? 13.972  20.966  40.484  1.00 56.78  ? 54  ALA A CA    1 
ATOM   449  C  C     . ALA A 1 82  ? 15.434  20.691  40.163  1.00 57.99  ? 54  ALA A C     1 
ATOM   450  O  O     . ALA A 1 82  ? 15.797  19.576  39.764  1.00 59.32  ? 54  ALA A O     1 
ATOM   451  C  CB    . ALA A 1 82  ? 13.305  21.752  39.352  1.00 60.18  ? 54  ALA A CB    1 
ATOM   452  N  N     . GLU A 1 83  ? 16.288  21.697  40.370  1.00 57.36  ? 55  GLU A N     1 
ATOM   453  C  CA    . GLU A 1 83  ? 17.713  21.569  40.087  1.00 64.53  ? 55  GLU A CA    1 
ATOM   454  C  C     . GLU A 1 83  ? 18.338  20.426  40.883  1.00 56.68  ? 55  GLU A C     1 
ATOM   455  O  O     . GLU A 1 83  ? 19.017  19.558  40.322  1.00 62.31  ? 55  GLU A O     1 
ATOM   456  C  CB    . GLU A 1 83  ? 18.400  22.899  40.405  1.00 72.25  ? 55  GLU A CB    1 
ATOM   457  C  CG    . GLU A 1 83  ? 19.915  22.888  40.344  1.00 87.51  ? 55  GLU A CG    1 
ATOM   458  C  CD    . GLU A 1 83  ? 20.490  24.253  39.987  1.00 99.52  ? 55  GLU A CD    1 
ATOM   459  O  OE1   . GLU A 1 83  ? 19.762  25.077  39.387  1.00 96.62  ? 55  GLU A OE1   1 
ATOM   460  O  OE2   . GLU A 1 83  ? 21.673  24.499  40.314  1.00 103.90 ? 55  GLU A OE2   1 
ATOM   461  N  N     . LYS A 1 84  ? 18.114  20.409  42.199  1.00 60.35  ? 56  LYS A N     1 
ATOM   462  C  CA    . LYS A 1 84  ? 18.690  19.362  43.041  1.00 59.35  ? 56  LYS A CA    1 
ATOM   463  C  C     . LYS A 1 84  ? 18.070  18.002  42.743  1.00 49.98  ? 56  LYS A C     1 
ATOM   464  O  O     . LYS A 1 84  ? 18.763  16.977  42.748  1.00 51.68  ? 56  LYS A O     1 
ATOM   465  C  CB    . LYS A 1 84  ? 18.498  19.718  44.509  1.00 54.30  ? 56  LYS A CB    1 
ATOM   466  C  CG    . LYS A 1 84  ? 18.947  21.112  44.870  1.00 63.84  ? 56  LYS A CG    1 
ATOM   467  C  CD    . LYS A 1 84  ? 20.256  21.089  45.639  1.00 67.13  ? 56  LYS A CD    1 
ATOM   468  C  CE    . LYS A 1 84  ? 20.452  22.398  46.402  1.00 73.38  ? 56  LYS A CE    1 
ATOM   469  N  NZ    . LYS A 1 84  ? 19.141  22.965  46.859  1.00 67.79  ? 56  LYS A NZ    1 
ATOM   470  N  N     . ILE A 1 85  ? 16.765  17.976  42.478  1.00 49.94  ? 57  ILE A N     1 
ATOM   471  C  CA    . ILE A 1 85  ? 16.087  16.712  42.216  1.00 51.10  ? 57  ILE A CA    1 
ATOM   472  C  C     . ILE A 1 85  ? 16.697  16.039  40.994  1.00 49.70  ? 57  ILE A C     1 
ATOM   473  O  O     . ILE A 1 85  ? 17.072  14.861  41.029  1.00 51.74  ? 57  ILE A O     1 
ATOM   474  C  CB    . ILE A 1 85  ? 14.575  16.950  42.046  1.00 51.95  ? 57  ILE A CB    1 
ATOM   475  C  CG1   . ILE A 1 85  ? 13.930  17.199  43.414  1.00 50.19  ? 57  ILE A CG1   1 
ATOM   476  C  CG2   . ILE A 1 85  ? 13.925  15.785  41.339  1.00 48.43  ? 57  ILE A CG2   1 
ATOM   477  C  CD1   . ILE A 1 85  ? 14.163  16.074  44.420  1.00 46.66  ? 57  ILE A CD1   1 
ATOM   478  N  N     . ASP A 1 86  ? 16.870  16.805  39.913  1.00 59.48  ? 58  ASP A N     1 
ATOM   479  C  CA    . ASP A 1 86  ? 17.356  16.220  38.667  1.00 57.27  ? 58  ASP A CA    1 
ATOM   480  C  C     . ASP A 1 86  ? 18.771  15.682  38.810  1.00 53.57  ? 58  ASP A C     1 
ATOM   481  O  O     . ASP A 1 86  ? 19.111  14.657  38.207  1.00 62.64  ? 58  ASP A O     1 
ATOM   482  C  CB    . ASP A 1 86  ? 17.271  17.249  37.539  1.00 59.16  ? 58  ASP A CB    1 
ATOM   483  C  CG    . ASP A 1 86  ? 15.833  17.598  37.176  1.00 66.88  ? 58  ASP A CG    1 
ATOM   484  O  OD1   . ASP A 1 86  ? 14.926  16.776  37.441  1.00 64.86  ? 58  ASP A OD1   1 
ATOM   485  O  OD2   . ASP A 1 86  ? 15.608  18.684  36.606  1.00 68.32  ? 58  ASP A OD2   1 
ATOM   486  N  N     . ARG A 1 87  ? 19.598  16.336  39.626  1.00 56.44  ? 59  ARG A N     1 
ATOM   487  C  CA    . ARG A 1 87  ? 20.968  15.874  39.828  1.00 59.28  ? 59  ARG A CA    1 
ATOM   488  C  C     . ARG A 1 87  ? 21.009  14.605  40.663  1.00 56.10  ? 59  ARG A C     1 
ATOM   489  O  O     . ARG A 1 87  ? 21.777  13.681  40.360  1.00 51.78  ? 59  ARG A O     1 
ATOM   490  C  CB    . ARG A 1 87  ? 21.785  16.977  40.493  1.00 59.74  ? 59  ARG A CB    1 
ATOM   491  C  CG    . ARG A 1 87  ? 22.038  18.174  39.588  1.00 75.37  ? 59  ARG A CG    1 
ATOM   492  C  CD    . ARG A 1 87  ? 23.334  18.857  39.958  1.00 86.37  ? 59  ARG A CD    1 
ATOM   493  N  NE    . ARG A 1 87  ? 23.446  18.971  41.409  1.00 92.51  ? 59  ARG A NE    1 
ATOM   494  C  CZ    . ARG A 1 87  ? 23.349  20.110  42.082  1.00 94.25  ? 59  ARG A CZ    1 
ATOM   495  N  NH1   . ARG A 1 87  ? 23.125  21.261  41.466  1.00 92.91  ? 59  ARG A NH1   1 
ATOM   496  N  NH2   . ARG A 1 87  ? 23.460  20.092  43.409  1.00 87.99  ? 59  ARG A NH2   1 
ATOM   497  N  N     . ILE A 1 88  ? 20.204  14.551  41.730  1.00 53.66  ? 60  ILE A N     1 
ATOM   498  C  CA    . ILE A 1 88  ? 20.126  13.335  42.535  1.00 52.33  ? 60  ILE A CA    1 
ATOM   499  C  C     . ILE A 1 88  ? 19.586  12.187  41.699  1.00 44.46  ? 60  ILE A C     1 
ATOM   500  O  O     . ILE A 1 88  ? 20.106  11.064  41.748  1.00 45.77  ? 60  ILE A O     1 
ATOM   501  C  CB    . ILE A 1 88  ? 19.266  13.570  43.793  1.00 55.76  ? 60  ILE A CB    1 
ATOM   502  C  CG1   . ILE A 1 88  ? 19.993  14.482  44.780  1.00 50.28  ? 60  ILE A CG1   1 
ATOM   503  C  CG2   . ILE A 1 88  ? 18.991  12.254  44.488  1.00 49.64  ? 60  ILE A CG2   1 
ATOM   504  C  CD1   . ILE A 1 88  ? 19.068  15.303  45.636  1.00 58.20  ? 60  ILE A CD1   1 
ATOM   505  N  N     . TYR A 1 89  ? 18.543  12.452  40.907  1.00 49.14  ? 61  TYR A N     1 
ATOM   506  C  CA    . TYR A 1 89  ? 17.928  11.385  40.117  1.00 52.22  ? 61  TYR A CA    1 
ATOM   507  C  C     . TYR A 1 89  ? 18.901  10.832  39.081  1.00 52.73  ? 61  TYR A C     1 
ATOM   508  O  O     . TYR A 1 89  ? 18.916  9.624   38.818  1.00 48.90  ? 61  TYR A O     1 
ATOM   509  C  CB    . TYR A 1 89  ? 16.632  11.897  39.471  1.00 52.55  ? 61  TYR A CB    1 
ATOM   510  C  CG    . TYR A 1 89  ? 15.827  10.853  38.708  1.00 56.30  ? 61  TYR A CG    1 
ATOM   511  C  CD1   . TYR A 1 89  ? 15.047  9.911   39.386  1.00 56.42  ? 61  TYR A CD1   1 
ATOM   512  C  CD2   . TYR A 1 89  ? 15.772  10.863  37.318  1.00 53.80  ? 61  TYR A CD2   1 
ATOM   513  C  CE1   . TYR A 1 89  ? 14.293  8.964   38.693  1.00 53.38  ? 61  TYR A CE1   1 
ATOM   514  C  CE2   . TYR A 1 89  ? 15.022  9.923   36.622  1.00 58.69  ? 61  TYR A CE2   1 
ATOM   515  C  CZ    . TYR A 1 89  ? 14.278  8.983   37.313  1.00 57.88  ? 61  TYR A CZ    1 
ATOM   516  O  OH    . TYR A 1 89  ? 13.530  8.058   36.620  1.00 63.17  ? 61  TYR A OH    1 
ATOM   517  N  N     . GLU A 1 90  ? 19.745  11.694  38.504  1.00 57.00  ? 62  GLU A N     1 
ATOM   518  C  CA    . GLU A 1 90  ? 20.784  11.211  37.595  1.00 57.03  ? 62  GLU A CA    1 
ATOM   519  C  C     . GLU A 1 90  ? 21.700  10.225  38.302  1.00 48.95  ? 62  GLU A C     1 
ATOM   520  O  O     . GLU A 1 90  ? 22.022  9.155   37.770  1.00 52.28  ? 62  GLU A O     1 
ATOM   521  C  CB    . GLU A 1 90  ? 21.599  12.385  37.058  1.00 63.24  ? 62  GLU A CB    1 
ATOM   522  C  CG    . GLU A 1 90  ? 21.182  12.875  35.689  1.00 73.34  ? 62  GLU A CG    1 
ATOM   523  C  CD    . GLU A 1 90  ? 21.978  14.093  35.259  1.00 79.82  ? 62  GLU A CD    1 
ATOM   524  O  OE1   . GLU A 1 90  ? 22.091  15.041  36.063  1.00 82.32  ? 62  GLU A OE1   1 
ATOM   525  O  OE2   . GLU A 1 90  ? 22.489  14.104  34.121  1.00 85.24  ? 62  GLU A OE2   1 
ATOM   526  N  N     . ARG A 1 91  ? 22.126  10.577  39.515  1.00 46.50  ? 63  ARG A N     1 
ATOM   527  C  CA    . ARG A 1 91  ? 22.971  9.692   40.303  1.00 44.06  ? 63  ARG A CA    1 
ATOM   528  C  C     . ARG A 1 91  ? 22.253  8.386   40.612  1.00 50.12  ? 63  ARG A C     1 
ATOM   529  O  O     . ARG A 1 91  ? 22.841  7.299   40.511  1.00 42.49  ? 63  ARG A O     1 
ATOM   530  C  CB    . ARG A 1 91  ? 23.385  10.415  41.583  1.00 50.26  ? 63  ARG A CB    1 
ATOM   531  C  CG    . ARG A 1 91  ? 24.767  10.084  42.086  1.00 66.17  ? 63  ARG A CG    1 
ATOM   532  C  CD    . ARG A 1 91  ? 25.308  11.264  42.883  1.00 75.83  ? 63  ARG A CD    1 
ATOM   533  N  NE    . ARG A 1 91  ? 24.532  11.517  44.092  1.00 73.33  ? 63  ARG A NE    1 
ATOM   534  C  CZ    . ARG A 1 91  ? 24.047  12.702  44.438  1.00 72.58  ? 63  ARG A CZ    1 
ATOM   535  N  NH1   . ARG A 1 91  ? 24.197  13.763  43.663  1.00 67.76  ? 63  ARG A NH1   1 
ATOM   536  N  NH2   . ARG A 1 91  ? 23.384  12.822  45.585  1.00 60.29  ? 63  ARG A NH2   1 
ATOM   537  N  N     . ILE A 1 92  ? 20.965  8.472   40.967  1.00 45.30  ? 64  ILE A N     1 
ATOM   538  C  CA    . ILE A 1 92  ? 20.182  7.272   41.248  1.00 46.43  ? 64  ILE A CA    1 
ATOM   539  C  C     . ILE A 1 92  ? 20.084  6.387   40.008  1.00 42.66  ? 64  ILE A C     1 
ATOM   540  O  O     . ILE A 1 92  ? 20.138  5.153   40.101  1.00 49.26  ? 64  ILE A O     1 
ATOM   541  C  CB    . ILE A 1 92  ? 18.792  7.673   41.777  1.00 46.66  ? 64  ILE A CB    1 
ATOM   542  C  CG1   . ILE A 1 92  ? 18.910  8.188   43.214  1.00 42.75  ? 64  ILE A CG1   1 
ATOM   543  C  CG2   . ILE A 1 92  ? 17.814  6.508   41.666  1.00 42.23  ? 64  ILE A CG2   1 
ATOM   544  C  CD1   . ILE A 1 92  ? 17.684  8.976   43.699  1.00 43.99  ? 64  ILE A CD1   1 
ATOM   545  N  N     . LEU A 1 93  ? 19.940  7.000   38.830  1.00 47.05  ? 65  LEU A N     1 
ATOM   546  C  CA    . LEU A 1 93  ? 19.848  6.224   37.592  1.00 50.77  ? 65  LEU A CA    1 
ATOM   547  C  C     . LEU A 1 93  ? 21.104  5.399   37.354  1.00 52.30  ? 65  LEU A C     1 
ATOM   548  O  O     . LEU A 1 93  ? 21.035  4.282   36.826  1.00 59.95  ? 65  LEU A O     1 
ATOM   549  C  CB    . LEU A 1 93  ? 19.606  7.158   36.411  1.00 48.40  ? 65  LEU A CB    1 
ATOM   550  C  CG    . LEU A 1 93  ? 18.172  7.630   36.221  1.00 56.52  ? 65  LEU A CG    1 
ATOM   551  C  CD1   . LEU A 1 93  ? 18.093  8.646   35.098  1.00 61.44  ? 65  LEU A CD1   1 
ATOM   552  C  CD2   . LEU A 1 93  ? 17.289  6.437   35.924  1.00 49.20  ? 65  LEU A CD2   1 
ATOM   553  N  N     . ALA A 1 94  ? 22.261  5.932   37.737  1.00 49.95  ? 66  ALA A N     1 
ATOM   554  C  CA    . ALA A 1 94  ? 23.526  5.242   37.537  1.00 58.09  ? 66  ALA A CA    1 
ATOM   555  C  C     . ALA A 1 94  ? 23.849  4.244   38.639  1.00 57.85  ? 66  ALA A C     1 
ATOM   556  O  O     . ALA A 1 94  ? 24.805  3.478   38.487  1.00 56.11  ? 66  ALA A O     1 
ATOM   557  C  CB    . ALA A 1 94  ? 24.663  6.260   37.424  1.00 59.68  ? 66  ALA A CB    1 
ATOM   558  N  N     . ASP A 1 95  ? 23.099  4.235   39.741  1.00 48.40  ? 67  ASP A N     1 
ATOM   559  C  CA    . ASP A 1 95  ? 23.377  3.297   40.823  1.00 49.90  ? 67  ASP A CA    1 
ATOM   560  C  C     . ASP A 1 95  ? 23.143  1.867   40.339  1.00 55.19  ? 67  ASP A C     1 
ATOM   561  O  O     . ASP A 1 95  ? 22.043  1.524   39.894  1.00 55.04  ? 67  ASP A O     1 
ATOM   562  C  CB    . ASP A 1 95  ? 22.497  3.615   42.033  1.00 48.75  ? 67  ASP A CB    1 
ATOM   563  C  CG    . ASP A 1 95  ? 22.949  2.905   43.288  1.00 51.15  ? 67  ASP A CG    1 
ATOM   564  O  OD1   . ASP A 1 95  ? 23.093  1.660   43.263  1.00 45.90  ? 67  ASP A OD1   1 
ATOM   565  O  OD2   . ASP A 1 95  ? 23.138  3.600   44.314  1.00 48.29  ? 67  ASP A OD2   1 
ATOM   566  N  N     . GLU A 1 96  ? 24.178  1.030   40.429  1.00 59.71  ? 68  GLU A N     1 
ATOM   567  C  CA    . GLU A 1 96  ? 24.111  -0.320  39.880  1.00 58.84  ? 68  GLU A CA    1 
ATOM   568  C  C     . GLU A 1 96  ? 23.208  -1.245  40.680  1.00 59.41  ? 68  GLU A C     1 
ATOM   569  O  O     . GLU A 1 96  ? 22.926  -2.354  40.214  1.00 58.18  ? 68  GLU A O     1 
ATOM   570  C  CB    . GLU A 1 96  ? 25.496  -0.965  39.840  1.00 63.39  ? 68  GLU A CB    1 
ATOM   571  C  CG    . GLU A 1 96  ? 25.971  -1.368  41.225  1.00 68.23  ? 68  GLU A CG    1 
ATOM   572  C  CD    . GLU A 1 96  ? 27.407  -1.837  41.256  1.00 93.31  ? 68  GLU A CD    1 
ATOM   573  O  OE1   . GLU A 1 96  ? 28.072  -1.817  40.193  1.00 95.60  ? 68  GLU A OE1   1 
ATOM   574  O  OE2   . GLU A 1 96  ? 27.862  -2.246  42.349  1.00 104.05 ? 68  GLU A OE2   1 
ATOM   575  N  N     . ARG A 1 97  ? 22.780  -0.841  41.876  1.00 55.58  ? 69  ARG A N     1 
ATOM   576  C  CA    . ARG A 1 97  ? 22.058  -1.756  42.747  1.00 51.60  ? 69  ARG A CA    1 
ATOM   577  C  C     . ARG A 1 97  ? 20.592  -1.902  42.362  1.00 43.53  ? 69  ARG A C     1 
ATOM   578  O  O     . ARG A 1 97  ? 19.899  -2.761  42.916  1.00 46.17  ? 69  ARG A O     1 
ATOM   579  C  CB    . ARG A 1 97  ? 22.184  -1.303  44.203  1.00 48.46  ? 69  ARG A CB    1 
ATOM   580  C  CG    . ARG A 1 97  ? 23.525  -1.661  44.836  1.00 50.96  ? 69  ARG A CG    1 
ATOM   581  C  CD    . ARG A 1 97  ? 23.684  -0.940  46.147  1.00 49.04  ? 69  ARG A CD    1 
ATOM   582  N  NE    . ARG A 1 97  ? 23.633  0.502   45.954  1.00 46.55  ? 69  ARG A NE    1 
ATOM   583  C  CZ    . ARG A 1 97  ? 23.966  1.386   46.883  1.00 46.92  ? 69  ARG A CZ    1 
ATOM   584  N  NH1   . ARG A 1 97  ? 24.383  1.006   48.079  1.00 43.84  ? 69  ARG A NH1   1 
ATOM   585  N  NH2   . ARG A 1 97  ? 23.861  2.684   46.610  1.00 48.43  ? 69  ARG A NH2   1 
ATOM   586  N  N     . HIS A 1 98  ? 20.103  -1.099  41.431  1.00 46.64  ? 70  HIS A N     1 
ATOM   587  C  CA    . HIS A 1 98  ? 18.777  -1.336  40.884  1.00 52.47  ? 70  HIS A CA    1 
ATOM   588  C  C     . HIS A 1 98  ? 18.804  -1.055  39.388  1.00 55.44  ? 70  HIS A C     1 
ATOM   589  O  O     . HIS A 1 98  ? 19.758  -0.475  38.851  1.00 45.47  ? 70  HIS A O     1 
ATOM   590  C  CB    . HIS A 1 98  ? 17.693  -0.504  41.606  1.00 42.54  ? 70  HIS A CB    1 
ATOM   591  C  CG    . HIS A 1 98  ? 17.859  0.978   41.462  1.00 42.06  ? 70  HIS A CG    1 
ATOM   592  N  ND1   . HIS A 1 98  ? 16.844  1.867   41.745  1.00 39.65  ? 70  HIS A ND1   1 
ATOM   593  C  CD2   . HIS A 1 98  ? 18.925  1.729   41.095  1.00 43.47  ? 70  HIS A CD2   1 
ATOM   594  C  CE1   . HIS A 1 98  ? 17.271  3.101   41.540  1.00 42.05  ? 70  HIS A CE1   1 
ATOM   595  N  NE2   . HIS A 1 98  ? 18.529  3.046   41.142  1.00 45.66  ? 70  HIS A NE2   1 
ATOM   596  N  N     . THR A 1 99  ? 17.744  -1.495  38.715  1.00 44.70  ? 71  THR A N     1 
ATOM   597  C  CA    . THR A 1 99  ? 17.619  -1.343  37.277  1.00 50.49  ? 71  THR A CA    1 
ATOM   598  C  C     . THR A 1 99  ? 16.138  -1.249  36.929  1.00 57.56  ? 71  THR A C     1 
ATOM   599  O  O     . THR A 1 99  ? 15.268  -1.350  37.802  1.00 47.68  ? 71  THR A O     1 
ATOM   600  C  CB    . THR A 1 99  ? 18.310  -2.501  36.555  1.00 58.50  ? 71  THR A CB    1 
ATOM   601  O  OG1   . THR A 1 99  ? 18.527  -2.151  35.182  1.00 60.40  ? 71  THR A OG1   1 
ATOM   602  C  CG2   . THR A 1 99  ? 17.476  -3.767  36.654  1.00 49.86  ? 71  THR A CG2   1 
ATOM   603  N  N     . ASP A 1 100 ? 15.860  -1.038  35.638  1.00 52.63  ? 72  ASP A N     1 
ATOM   604  C  CA    . ASP A 1 100 ? 14.492  -0.922  35.131  1.00 54.52  ? 72  ASP A CA    1 
ATOM   605  C  C     . ASP A 1 100 ? 13.759  0.234   35.808  1.00 52.99  ? 72  ASP A C     1 
ATOM   606  O  O     . ASP A 1 100 ? 12.601  0.109   36.209  1.00 54.14  ? 72  ASP A O     1 
ATOM   607  C  CB    . ASP A 1 100 ? 13.728  -2.235  35.312  1.00 56.17  ? 72  ASP A CB    1 
ATOM   608  C  CG    . ASP A 1 100 ? 14.263  -3.340  34.425  1.00 65.15  ? 72  ASP A CG    1 
ATOM   609  O  OD1   . ASP A 1 100 ? 14.926  -3.015  33.418  1.00 69.18  ? 72  ASP A OD1   1 
ATOM   610  O  OD2   . ASP A 1 100 ? 14.059  -4.529  34.758  1.00 67.47  ? 72  ASP A OD2   1 
ATOM   611  N  N     . ILE A 1 101 ? 14.456  1.362   35.947  1.00 52.00  ? 73  ILE A N     1 
ATOM   612  C  CA    . ILE A 1 101 ? 13.896  2.550   36.580  1.00 53.38  ? 73  ILE A CA    1 
ATOM   613  C  C     . ILE A 1 101 ? 12.757  3.051   35.708  1.00 56.45  ? 73  ILE A C     1 
ATOM   614  O  O     . ILE A 1 101 ? 12.959  3.372   34.533  1.00 61.52  ? 73  ILE A O     1 
ATOM   615  C  CB    . ILE A 1 101 ? 14.950  3.659   36.749  1.00 48.61  ? 73  ILE A CB    1 
ATOM   616  C  CG1   . ILE A 1 101 ? 16.293  3.176   37.317  1.00 57.55  ? 73  ILE A CG1   1 
ATOM   617  C  CG2   . ILE A 1 101 ? 14.380  4.816   37.576  1.00 47.94  ? 73  ILE A CG2   1 
ATOM   618  C  CD1   . ILE A 1 101 ? 16.234  2.117   38.321  1.00 51.09  ? 73  ILE A CD1   1 
ATOM   619  N  N     . LEU A 1 102 ? 11.562  3.144   36.277  1.00 45.00  ? 74  LEU A N     1 
ATOM   620  C  CA    . LEU A 1 102 ? 10.444  3.745   35.567  1.00 41.95  ? 74  LEU A CA    1 
ATOM   621  C  C     . LEU A 1 102 ? 9.849   4.856   36.418  1.00 42.16  ? 74  LEU A C     1 
ATOM   622  O  O     . LEU A 1 102 ? 9.339   4.602   37.517  1.00 35.81  ? 74  LEU A O     1 
ATOM   623  C  CB    . LEU A 1 102 ? 9.380   2.700   35.217  1.00 42.86  ? 74  LEU A CB    1 
ATOM   624  C  CG    . LEU A 1 102 ? 8.301   3.347   34.346  1.00 53.83  ? 74  LEU A CG    1 
ATOM   625  C  CD1   . LEU A 1 102 ? 8.956   4.042   33.126  1.00 50.85  ? 74  LEU A CD1   1 
ATOM   626  C  CD2   . LEU A 1 102 ? 7.257   2.333   33.931  1.00 49.02  ? 74  LEU A CD2   1 
ATOM   627  N  N     . CYS A 1 103 ? 9.910   6.077   35.903  1.00 36.00  ? 75  CYS A N     1 
ATOM   628  C  CA    . CYS A 1 103 ? 9.264   7.221   36.530  1.00 36.33  ? 75  CYS A CA    1 
ATOM   629  C  C     . CYS A 1 103 ? 7.760   7.157   36.272  1.00 45.65  ? 75  CYS A C     1 
ATOM   630  O  O     . CYS A 1 103 ? 7.311   7.328   35.134  1.00 43.08  ? 75  CYS A O     1 
ATOM   631  C  CB    . CYS A 1 103 ? 9.856   8.513   35.986  1.00 38.15  ? 75  CYS A CB    1 
ATOM   632  S  SG    . CYS A 1 103 ? 9.015   9.994   36.559  1.00 49.31  ? 75  CYS A SG    1 
ATOM   633  N  N     . LEU A 1 104 ? 6.975   6.940   37.331  1.00 43.94  ? 76  LEU A N     1 
ATOM   634  C  CA    . LEU A 1 104 ? 5.524   6.856   37.199  1.00 42.51  ? 76  LEU A CA    1 
ATOM   635  C  C     . LEU A 1 104 ? 4.876   8.221   37.154  1.00 39.97  ? 76  LEU A C     1 
ATOM   636  O  O     . LEU A 1 104 ? 3.754   8.367   36.656  1.00 45.09  ? 76  LEU A O     1 
ATOM   637  C  CB    . LEU A 1 104 ? 4.923   6.073   38.371  1.00 37.38  ? 76  LEU A CB    1 
ATOM   638  C  CG    . LEU A 1 104 ? 5.516   4.705   38.634  1.00 47.83  ? 76  LEU A CG    1 
ATOM   639  C  CD1   . LEU A 1 104 ? 4.975   4.199   39.954  1.00 47.98  ? 76  LEU A CD1   1 
ATOM   640  C  CD2   . LEU A 1 104 ? 5.169   3.764   37.481  1.00 45.11  ? 76  LEU A CD2   1 
ATOM   641  N  N     . LYS A 1 105 ? 5.532   9.224   37.708  1.00 40.91  ? 77  LYS A N     1 
ATOM   642  C  CA    . LYS A 1 105 ? 4.912   10.530  37.834  1.00 36.61  ? 77  LYS A CA    1 
ATOM   643  C  C     . LYS A 1 105 ? 5.981   11.554  38.136  1.00 44.95  ? 77  LYS A C     1 
ATOM   644  O  O     . LYS A 1 105 ? 6.824   11.333  39.009  1.00 43.38  ? 77  LYS A O     1 
ATOM   645  C  CB    . LYS A 1 105 ? 3.868   10.571  38.947  1.00 43.88  ? 77  LYS A CB    1 
ATOM   646  C  CG    . LYS A 1 105 ? 3.348   11.980  39.135  1.00 44.72  ? 77  LYS A CG    1 
ATOM   647  C  CD    . LYS A 1 105 ? 2.473   12.112  40.365  1.00 47.01  ? 77  LYS A CD    1 
ATOM   648  C  CE    . LYS A 1 105 ? 1.065   11.877  40.047  1.00 52.85  ? 77  LYS A CE    1 
ATOM   649  N  NZ    . LYS A 1 105 ? 0.129   12.924  40.562  1.00 61.78  ? 77  LYS A NZ    1 
ATOM   650  N  N     . SER A 1 106 ? 5.925   12.671  37.426  1.00 42.67  ? 78  SER A N     1 
ATOM   651  C  CA    . SER A 1 106 ? 6.803   13.804  37.668  1.00 43.78  ? 78  SER A CA    1 
ATOM   652  C  C     . SER A 1 106 ? 5.927   15.038  37.805  1.00 46.87  ? 78  SER A C     1 
ATOM   653  O  O     . SER A 1 106 ? 5.185   15.376  36.878  1.00 55.73  ? 78  SER A O     1 
ATOM   654  C  CB    . SER A 1 106 ? 7.814   13.964  36.530  1.00 47.82  ? 78  SER A CB    1 
ATOM   655  O  OG    . SER A 1 106 ? 8.537   15.168  36.675  1.00 59.65  ? 78  SER A OG    1 
ATOM   656  N  N     . GLU A 1 107 ? 5.973   15.684  38.966  1.00 41.50  ? 79  GLU A N     1 
ATOM   657  C  CA    . GLU A 1 107 ? 5.168   16.870  39.239  1.00 43.94  ? 79  GLU A CA    1 
ATOM   658  C  C     . GLU A 1 107 ? 6.094   18.074  39.232  1.00 56.40  ? 79  GLU A C     1 
ATOM   659  O  O     . GLU A 1 107 ? 6.958   18.198  40.103  1.00 56.71  ? 79  GLU A O     1 
ATOM   660  C  CB    . GLU A 1 107 ? 4.436   16.770  40.579  1.00 45.71  ? 79  GLU A CB    1 
ATOM   661  C  CG    . GLU A 1 107 ? 3.621   15.497  40.783  1.00 47.26  ? 79  GLU A CG    1 
ATOM   662  C  CD    . GLU A 1 107 ? 3.199   15.322  42.231  1.00 48.93  ? 79  GLU A CD    1 
ATOM   663  O  OE1   . GLU A 1 107 ? 2.406   16.153  42.719  1.00 43.44  ? 79  GLU A OE1   1 
ATOM   664  O  OE2   . GLU A 1 107 ? 3.676   14.371  42.888  1.00 47.61  ? 79  GLU A OE2   1 
ATOM   665  N  N     . VAL A 1 108 ? 5.924   18.950  38.254  1.00 59.36  ? 80  VAL A N     1 
ATOM   666  C  CA    . VAL A 1 108 ? 6.602   20.237  38.265  1.00 59.28  ? 80  VAL A CA    1 
ATOM   667  C  C     . VAL A 1 108 ? 5.678   21.248  38.927  1.00 56.48  ? 80  VAL A C     1 
ATOM   668  O  O     . VAL A 1 108 ? 4.468   21.035  39.029  1.00 64.20  ? 80  VAL A O     1 
ATOM   669  C  CB    . VAL A 1 108 ? 7.007   20.672  36.844  1.00 56.38  ? 80  VAL A CB    1 
ATOM   670  C  CG1   . VAL A 1 108 ? 7.677   19.517  36.124  1.00 55.89  ? 80  VAL A CG1   1 
ATOM   671  C  CG2   . VAL A 1 108 ? 5.794   21.109  36.071  1.00 57.29  ? 80  VAL A CG2   1 
ATOM   672  N  N     . GLU A 1 109 ? 6.251   22.345  39.423  1.00 63.57  ? 81  GLU A N     1 
ATOM   673  C  CA    . GLU A 1 109 ? 5.456   23.396  40.063  1.00 73.29  ? 81  GLU A CA    1 
ATOM   674  C  C     . GLU A 1 109 ? 4.707   22.845  41.280  1.00 74.26  ? 81  GLU A C     1 
ATOM   675  O  O     . GLU A 1 109 ? 3.504   23.062  41.465  1.00 71.62  ? 81  GLU A O     1 
ATOM   676  C  CB    . GLU A 1 109 ? 4.496   24.028  39.044  1.00 79.04  ? 81  GLU A CB    1 
ATOM   677  C  CG    . GLU A 1 109 ? 4.301   25.548  39.106  1.00 91.20  ? 81  GLU A CG    1 
ATOM   678  C  CD    . GLU A 1 109 ? 3.504   26.012  40.321  1.00 99.52  ? 81  GLU A CD    1 
ATOM   679  O  OE1   . GLU A 1 109 ? 4.109   26.540  41.279  1.00 97.75  ? 81  GLU A OE1   1 
ATOM   680  O  OE2   . GLU A 1 109 ? 2.260   25.861  40.307  1.00 100.64 ? 81  GLU A OE2   1 
ATOM   681  N  N     . VAL A 1 110 ? 5.431   22.110  42.116  1.00 68.98  ? 82  VAL A N     1 
ATOM   682  C  CA    . VAL A 1 110 ? 4.839   21.541  43.320  1.00 66.81  ? 82  VAL A CA    1 
ATOM   683  C  C     . VAL A 1 110 ? 4.695   22.637  44.367  1.00 63.81  ? 82  VAL A C     1 
ATOM   684  O  O     . VAL A 1 110 ? 5.600   23.459  44.557  1.00 67.54  ? 82  VAL A O     1 
ATOM   685  C  CB    . VAL A 1 110 ? 5.693   20.368  43.831  1.00 58.81  ? 82  VAL A CB    1 
ATOM   686  C  CG1   . VAL A 1 110 ? 5.554   20.216  45.335  1.00 62.65  ? 82  VAL A CG1   1 
ATOM   687  C  CG2   . VAL A 1 110 ? 5.302   19.094  43.113  1.00 56.89  ? 82  VAL A CG2   1 
ATOM   688  N  N     . GLN A 1 111 ? 3.556   22.658  45.057  1.00 57.04  ? 83  GLN A N     1 
ATOM   689  C  CA    . GLN A 1 111 ? 3.281   23.790  45.935  1.00 64.48  ? 83  GLN A CA    1 
ATOM   690  C  C     . GLN A 1 111 ? 3.771   23.564  47.363  1.00 70.55  ? 83  GLN A C     1 
ATOM   691  O  O     . GLN A 1 111 ? 4.344   24.476  47.970  1.00 61.22  ? 83  GLN A O     1 
ATOM   692  C  CB    . GLN A 1 111 ? 1.785   24.104  45.938  1.00 73.94  ? 83  GLN A CB    1 
ATOM   693  C  CG    . GLN A 1 111 ? 1.338   24.852  44.678  1.00 85.99  ? 83  GLN A CG    1 
ATOM   694  C  CD    . GLN A 1 111 ? 1.944   26.244  44.562  1.00 88.41  ? 83  GLN A CD    1 
ATOM   695  O  OE1   . GLN A 1 111 ? 2.963   26.428  43.890  1.00 88.06  ? 83  GLN A OE1   1 
ATOM   696  N  NE2   . GLN A 1 111 ? 1.338   27.221  45.223  1.00 86.42  ? 83  GLN A NE2   1 
ATOM   697  N  N     . GLU A 1 112 ? 3.564   22.376  47.930  1.00 62.58  ? 84  GLU A N     1 
ATOM   698  C  CA    . GLU A 1 112 ? 4.098   22.089  49.255  1.00 59.18  ? 84  GLU A CA    1 
ATOM   699  C  C     . GLU A 1 112 ? 4.627   20.663  49.311  1.00 52.79  ? 84  GLU A C     1 
ATOM   700  O  O     . GLU A 1 112 ? 4.307   19.821  48.466  1.00 47.84  ? 84  GLU A O     1 
ATOM   701  C  CB    . GLU A 1 112 ? 3.055   22.293  50.353  1.00 65.15  ? 84  GLU A CB    1 
ATOM   702  C  CG    . GLU A 1 112 ? 1.987   21.221  50.408  1.00 73.95  ? 84  GLU A CG    1 
ATOM   703  C  CD    . GLU A 1 112 ? 0.772   21.655  51.220  1.00 91.81  ? 84  GLU A CD    1 
ATOM   704  O  OE1   . GLU A 1 112 ? -0.348  21.665  50.659  1.00 94.74  ? 84  GLU A OE1   1 
ATOM   705  O  OE2   . GLU A 1 112 ? 0.941   21.993  52.414  1.00 93.96  ? 84  GLU A OE2   1 
ATOM   706  N  N     . ARG A 1 113 ? 5.446   20.404  50.330  1.00 52.17  ? 85  ARG A N     1 
ATOM   707  C  CA    . ARG A 1 113 ? 6.036   19.088  50.502  1.00 41.01  ? 85  ARG A CA    1 
ATOM   708  C  C     . ARG A 1 113 ? 5.043   18.114  51.108  1.00 39.78  ? 85  ARG A C     1 
ATOM   709  O  O     . ARG A 1 113 ? 4.248   18.460  51.991  1.00 42.12  ? 85  ARG A O     1 
ATOM   710  C  CB    . ARG A 1 113 ? 7.290   19.146  51.377  1.00 39.98  ? 85  ARG A CB    1 
ATOM   711  C  CG    . ARG A 1 113 ? 8.526   19.784  50.711  1.00 44.76  ? 85  ARG A CG    1 
ATOM   712  C  CD    . ARG A 1 113 ? 9.631   20.024  51.727  1.00 40.95  ? 85  ARG A CD    1 
ATOM   713  N  NE    . ARG A 1 113 ? 10.719  20.832  51.183  1.00 43.42  ? 85  ARG A NE    1 
ATOM   714  C  CZ    . ARG A 1 113 ? 11.801  20.348  50.594  1.00 44.45  ? 85  ARG A CZ    1 
ATOM   715  N  NH1   . ARG A 1 113 ? 11.958  19.050  50.390  1.00 46.04  ? 85  ARG A NH1   1 
ATOM   716  N  NH2   . ARG A 1 113 ? 12.756  21.187  50.200  1.00 49.48  ? 85  ARG A NH2   1 
ATOM   717  N  N     . MET A 1 114 ? 5.105   16.880  50.630  1.00 39.41  ? 86  MET A N     1 
ATOM   718  C  CA    . MET A 1 114 ? 4.328   15.800  51.220  1.00 43.27  ? 86  MET A CA    1 
ATOM   719  C  C     . MET A 1 114 ? 5.016   15.208  52.450  1.00 41.45  ? 86  MET A C     1 
ATOM   720  O  O     . MET A 1 114 ? 4.345   14.675  53.342  1.00 41.04  ? 86  MET A O     1 
ATOM   721  C  CB    . MET A 1 114 ? 4.138   14.745  50.147  1.00 41.24  ? 86  MET A CB    1 
ATOM   722  C  CG    . MET A 1 114 ? 3.213   15.239  49.075  1.00 55.91  ? 86  MET A CG    1 
ATOM   723  S  SD    . MET A 1 114 ? 2.006   13.989  48.746  1.00 73.38  ? 86  MET A SD    1 
ATOM   724  C  CE    . MET A 1 114 ? 3.203   12.804  48.163  1.00 47.46  ? 86  MET A CE    1 
ATOM   725  N  N     . PHE A 1 115 ? 6.344   15.277  52.511  1.00 36.41  ? 87  PHE A N     1 
ATOM   726  C  CA    . PHE A 1 115 ? 7.119   14.620  53.565  1.00 34.19  ? 87  PHE A CA    1 
ATOM   727  C  C     . PHE A 1 115 ? 8.119   15.599  54.169  1.00 34.50  ? 87  PHE A C     1 
ATOM   728  O  O     . PHE A 1 115 ? 9.319   15.338  54.195  1.00 32.15  ? 87  PHE A O     1 
ATOM   729  C  CB    . PHE A 1 115 ? 7.807   13.387  52.986  1.00 31.21  ? 87  PHE A CB    1 
ATOM   730  C  CG    . PHE A 1 115 ? 6.844   12.471  52.280  1.00 40.51  ? 87  PHE A CG    1 
ATOM   731  C  CD1   . PHE A 1 115 ? 5.854   11.814  52.994  1.00 36.53  ? 87  PHE A CD1   1 
ATOM   732  C  CD2   . PHE A 1 115 ? 6.884   12.321  50.907  1.00 41.52  ? 87  PHE A CD2   1 
ATOM   733  C  CE1   . PHE A 1 115 ? 4.949   10.979  52.356  1.00 42.24  ? 87  PHE A CE1   1 
ATOM   734  C  CE2   . PHE A 1 115 ? 5.974   11.489  50.246  1.00 34.33  ? 87  PHE A CE2   1 
ATOM   735  C  CZ    . PHE A 1 115 ? 5.005   10.817  50.976  1.00 38.51  ? 87  PHE A CZ    1 
ATOM   736  N  N     . PRO A 1 116 ? 7.640   16.722  54.723  1.00 40.42  ? 88  PRO A N     1 
ATOM   737  C  CA    . PRO A 1 116 ? 8.571   17.786  55.145  1.00 35.38  ? 88  PRO A CA    1 
ATOM   738  C  C     . PRO A 1 116 ? 9.582   17.363  56.200  1.00 41.31  ? 88  PRO A C     1 
ATOM   739  O  O     . PRO A 1 116 ? 10.674  17.946  56.279  1.00 39.26  ? 88  PRO A O     1 
ATOM   740  C  CB    . PRO A 1 116 ? 7.631   18.875  55.685  1.00 38.99  ? 88  PRO A CB    1 
ATOM   741  C  CG    . PRO A 1 116 ? 6.344   18.163  56.010  1.00 38.87  ? 88  PRO A CG    1 
ATOM   742  C  CD    . PRO A 1 116 ? 6.235   17.051  55.022  1.00 37.00  ? 88  PRO A CD    1 
ATOM   743  N  N     . ASP A 1 117 ? 9.266   16.364  57.016  1.00 36.73  ? 89  ASP A N     1 
ATOM   744  C  CA    . ASP A 1 117 ? 10.140  15.972  58.110  1.00 34.98  ? 89  ASP A CA    1 
ATOM   745  C  C     . ASP A 1 117 ? 11.017  14.779  57.775  1.00 34.69  ? 89  ASP A C     1 
ATOM   746  O  O     . ASP A 1 117 ? 11.748  14.307  58.648  1.00 35.12  ? 89  ASP A O     1 
ATOM   747  C  CB    . ASP A 1 117 ? 9.301   15.652  59.348  1.00 39.61  ? 89  ASP A CB    1 
ATOM   748  C  CG    . ASP A 1 117 ? 8.571   16.885  59.877  1.00 48.88  ? 89  ASP A CG    1 
ATOM   749  O  OD1   . ASP A 1 117 ? 9.241   17.908  60.121  1.00 51.28  ? 89  ASP A OD1   1 
ATOM   750  O  OD2   . ASP A 1 117 ? 7.331   16.831  60.013  1.00 45.65  ? 89  ASP A OD2   1 
ATOM   751  N  N     . TRP A 1 118 ? 10.972  14.278  56.551  1.00 29.22  ? 90  TRP A N     1 
ATOM   752  C  CA    . TRP A 1 118 ? 11.716  13.074  56.180  1.00 28.90  ? 90  TRP A CA    1 
ATOM   753  C  C     . TRP A 1 118 ? 12.713  13.417  55.085  1.00 34.29  ? 90  TRP A C     1 
ATOM   754  O  O     . TRP A 1 118 ? 12.330  13.505  53.917  1.00 31.81  ? 90  TRP A O     1 
ATOM   755  C  CB    . TRP A 1 118 ? 10.791  11.969  55.696  1.00 28.75  ? 90  TRP A CB    1 
ATOM   756  C  CG    . TRP A 1 118 ? 9.714   11.549  56.607  1.00 27.81  ? 90  TRP A CG    1 
ATOM   757  C  CD1   . TRP A 1 118 ? 9.563   11.839  57.938  1.00 32.49  ? 90  TRP A CD1   1 
ATOM   758  C  CD2   . TRP A 1 118 ? 8.626   10.688  56.256  1.00 28.94  ? 90  TRP A CD2   1 
ATOM   759  N  NE1   . TRP A 1 118 ? 8.430   11.220  58.423  1.00 30.14  ? 90  TRP A NE1   1 
ATOM   760  C  CE2   . TRP A 1 118 ? 7.844   10.506  57.406  1.00 32.84  ? 90  TRP A CE2   1 
ATOM   761  C  CE3   . TRP A 1 118 ? 8.241   10.058  55.064  1.00 32.05  ? 90  TRP A CE3   1 
ATOM   762  C  CZ2   . TRP A 1 118 ? 6.689   9.723   57.404  1.00 35.59  ? 90  TRP A CZ2   1 
ATOM   763  C  CZ3   . TRP A 1 118 ? 7.093   9.271   55.066  1.00 31.39  ? 90  TRP A CZ3   1 
ATOM   764  C  CH2   . TRP A 1 118 ? 6.333   9.117   56.221  1.00 31.15  ? 90  TRP A CH2   1 
ATOM   765  N  N     . SER A 1 119 ? 13.984  13.608  55.447  1.00 30.38  ? 91  SER A N     1 
ATOM   766  C  CA    . SER A 1 119 ? 15.013  13.738  54.422  1.00 30.00  ? 91  SER A CA    1 
ATOM   767  C  C     . SER A 1 119 ? 15.007  12.517  53.520  1.00 33.48  ? 91  SER A C     1 
ATOM   768  O  O     . SER A 1 119 ? 15.018  12.632  52.292  1.00 32.12  ? 91  SER A O     1 
ATOM   769  C  CB    . SER A 1 119 ? 16.387  13.912  55.076  1.00 34.12  ? 91  SER A CB    1 
ATOM   770  O  OG    . SER A 1 119 ? 16.440  15.153  55.751  1.00 35.76  ? 91  SER A OG    1 
ATOM   771  N  N     . MET A 1 120 ? 15.028  11.331  54.121  1.00 30.36  ? 92  MET A N     1 
ATOM   772  C  CA    . MET A 1 120 ? 14.652  10.105  53.418  1.00 33.32  ? 92  MET A CA    1 
ATOM   773  C  C     . MET A 1 120 ? 14.228  9.082   54.458  1.00 36.13  ? 92  MET A C     1 
ATOM   774  O  O     . MET A 1 120 ? 15.056  8.581   55.225  1.00 31.74  ? 92  MET A O     1 
ATOM   775  C  CB    . MET A 1 120 ? 15.775  9.565   52.524  1.00 33.77  ? 92  MET A CB    1 
ATOM   776  C  CG    . MET A 1 120 ? 15.294  8.345   51.737  1.00 37.61  ? 92  MET A CG    1 
ATOM   777  S  SD    . MET A 1 120 ? 13.834  8.524   50.674  1.00 33.27  ? 92  MET A SD    1 
ATOM   778  C  CE    . MET A 1 120 ? 13.985  10.163  49.995  1.00 29.14  ? 92  MET A CE    1 
ATOM   779  N  N     . GLN A 1 121 ? 12.947  8.790   54.475  1.00 30.73  ? 93  GLN A N     1 
ATOM   780  C  CA    . GLN A 1 121 ? 12.397  7.778   55.357  1.00 30.10  ? 93  GLN A CA    1 
ATOM   781  C  C     . GLN A 1 121 ? 12.399  6.446   54.614  1.00 33.20  ? 93  GLN A C     1 
ATOM   782  O  O     . GLN A 1 121 ? 11.952  6.367   53.469  1.00 36.55  ? 93  GLN A O     1 
ATOM   783  C  CB    . GLN A 1 121 ? 10.984  8.166   55.767  1.00 28.32  ? 93  GLN A CB    1 
ATOM   784  C  CG    . GLN A 1 121 ? 10.235  7.082   56.516  1.00 30.08  ? 93  GLN A CG    1 
ATOM   785  C  CD    . GLN A 1 121 ? 10.589  7.083   57.998  1.00 38.56  ? 93  GLN A CD    1 
ATOM   786  O  OE1   . GLN A 1 121 ? 11.444  7.849   58.445  1.00 34.25  ? 93  GLN A OE1   1 
ATOM   787  N  NE2   . GLN A 1 121 ? 9.910   6.248   58.768  1.00 39.09  ? 93  GLN A NE2   1 
ATOM   788  N  N     . THR A 1 122 ? 12.902  5.408   55.256  1.00 27.36  ? 94  THR A N     1 
ATOM   789  C  CA    . THR A 1 122 ? 13.023  4.096   54.635  1.00 30.28  ? 94  THR A CA    1 
ATOM   790  C  C     . THR A 1 122 ? 12.029  3.150   55.290  1.00 33.62  ? 94  THR A C     1 
ATOM   791  O  O     . THR A 1 122 ? 12.022  3.008   56.516  1.00 32.97  ? 94  THR A O     1 
ATOM   792  C  CB    . THR A 1 122 ? 14.452  3.581   54.771  1.00 32.13  ? 94  THR A CB    1 
ATOM   793  O  OG1   . THR A 1 122 ? 15.326  4.562   54.194  1.00 40.08  ? 94  THR A OG1   1 
ATOM   794  C  CG2   . THR A 1 122 ? 14.610  2.279   54.009  1.00 39.17  ? 94  THR A CG2   1 
ATOM   795  N  N     . ILE A 1 123 ? 11.181  2.530   54.475  1.00 32.32  ? 95  ILE A N     1 
ATOM   796  C  CA    . ILE A 1 123 ? 10.150  1.615   54.941  1.00 31.76  ? 95  ILE A CA    1 
ATOM   797  C  C     . ILE A 1 123 ? 10.386  0.284   54.235  1.00 35.64  ? 95  ILE A C     1 
ATOM   798  O  O     . ILE A 1 123 ? 10.069  0.135   53.049  1.00 33.08  ? 95  ILE A O     1 
ATOM   799  C  CB    . ILE A 1 123 ? 8.746   2.148   54.659  1.00 35.71  ? 95  ILE A CB    1 
ATOM   800  C  CG1   . ILE A 1 123 ? 8.546   3.506   55.348  1.00 35.86  ? 95  ILE A CG1   1 
ATOM   801  C  CG2   . ILE A 1 123 ? 7.716   1.147   55.133  1.00 31.95  ? 95  ILE A CG2   1 
ATOM   802  C  CD1   . ILE A 1 123 ? 7.233   4.216   54.935  1.00 38.13  ? 95  ILE A CD1   1 
ATOM   803  N  N     . ASN A 1 124 ? 10.934  -0.692  54.955  1.00 32.77  ? 96  ASN A N     1 
ATOM   804  C  CA    . ASN A 1 124 ? 11.196  -2.013  54.388  1.00 36.64  ? 96  ASN A CA    1 
ATOM   805  C  C     . ASN A 1 124 ? 9.938   -2.861  54.585  1.00 35.20  ? 96  ASN A C     1 
ATOM   806  O  O     . ASN A 1 124 ? 9.687   -3.383  55.673  1.00 34.04  ? 96  ASN A O     1 
ATOM   807  C  CB    . ASN A 1 124 ? 12.409  -2.653  55.051  1.00 38.89  ? 96  ASN A CB    1 
ATOM   808  C  CG    . ASN A 1 124 ? 12.826  -3.943  54.374  1.00 45.27  ? 96  ASN A CG    1 
ATOM   809  O  OD1   . ASN A 1 124 ? 11.992  -4.660  53.847  1.00 42.77  ? 96  ASN A OD1   1 
ATOM   810  N  ND2   . ASN A 1 124 ? 14.123  -4.248  54.398  1.00 43.60  ? 96  ASN A ND2   1 
ATOM   811  N  N     . LEU A 1 125 ? 9.156   -3.031  53.524  1.00 31.78  ? 97  LEU A N     1 
ATOM   812  C  CA    . LEU A 1 125 ? 7.898   -3.754  53.683  1.00 34.52  ? 97  LEU A CA    1 
ATOM   813  C  C     . LEU A 1 125 ? 8.090   -5.257  53.836  1.00 37.61  ? 97  LEU A C     1 
ATOM   814  O  O     . LEU A 1 125 ? 7.202   -5.925  54.380  1.00 34.47  ? 97  LEU A O     1 
ATOM   815  C  CB    . LEU A 1 125 ? 6.963   -3.474  52.507  1.00 36.03  ? 97  LEU A CB    1 
ATOM   816  C  CG    . LEU A 1 125 ? 6.381   -2.068  52.610  1.00 36.71  ? 97  LEU A CG    1 
ATOM   817  C  CD1   . LEU A 1 125 ? 5.515   -1.749  51.381  1.00 41.26  ? 97  LEU A CD1   1 
ATOM   818  C  CD2   . LEU A 1 125 ? 5.629   -1.887  53.934  1.00 35.62  ? 97  LEU A CD2   1 
ATOM   819  N  N     . ASP A 1 126 ? 9.211   -5.808  53.359  1.00 33.37  ? 98  ASP A N     1 
ATOM   820  C  CA    . ASP A 1 126 ? 9.459   -7.235  53.549  1.00 34.79  ? 98  ASP A CA    1 
ATOM   821  C  C     . ASP A 1 126 ? 9.507   -7.589  55.026  1.00 43.70  ? 98  ASP A C     1 
ATOM   822  O  O     . ASP A 1 126 ? 9.193   -8.720  55.411  1.00 45.97  ? 98  ASP A O     1 
ATOM   823  C  CB    . ASP A 1 126 ? 10.787  -7.645  52.908  1.00 37.81  ? 98  ASP A CB    1 
ATOM   824  C  CG    . ASP A 1 126 ? 10.806  -7.456  51.413  1.00 43.10  ? 98  ASP A CG    1 
ATOM   825  O  OD1   . ASP A 1 126 ? 9.814   -7.809  50.756  1.00 43.91  ? 98  ASP A OD1   1 
ATOM   826  O  OD2   . ASP A 1 126 ? 11.821  -6.950  50.891  1.00 50.85  ? 98  ASP A OD2   1 
ATOM   827  N  N     . GLU A 1 127 ? 9.938   -6.651  55.861  1.00 37.05  ? 99  GLU A N     1 
ATOM   828  C  CA    . GLU A 1 127 ? 10.136  -6.912  57.271  1.00 40.01  ? 99  GLU A CA    1 
ATOM   829  C  C     . GLU A 1 127 ? 8.897   -6.582  58.083  1.00 46.78  ? 99  GLU A C     1 
ATOM   830  O  O     . GLU A 1 127 ? 8.852   -6.889  59.275  1.00 43.53  ? 99  GLU A O     1 
ATOM   831  C  CB    . GLU A 1 127 ? 11.334  -6.091  57.775  1.00 38.40  ? 99  GLU A CB    1 
ATOM   832  C  CG    . GLU A 1 127 ? 12.649  -6.848  57.682  1.00 49.69  ? 99  GLU A CG    1 
ATOM   833  C  CD    . GLU A 1 127 ? 13.860  -5.940  57.868  1.00 62.77  ? 99  GLU A CD    1 
ATOM   834  O  OE1   . GLU A 1 127 ? 13.668  -4.747  58.215  1.00 54.81  ? 99  GLU A OE1   1 
ATOM   835  O  OE2   . GLU A 1 127 ? 14.993  -6.405  57.615  1.00 62.18  ? 99  GLU A OE2   1 
ATOM   836  N  N     . ASN A 1 128 ? 7.889   -5.976  57.468  1.00 38.07  ? 100 ASN A N     1 
ATOM   837  C  CA    . ASN A 1 128 ? 6.741   -5.489  58.215  1.00 43.02  ? 100 ASN A CA    1 
ATOM   838  C  C     . ASN A 1 128 ? 5.689   -6.589  58.307  1.00 40.57  ? 100 ASN A C     1 
ATOM   839  O  O     . ASN A 1 128 ? 5.289   -7.161  57.288  1.00 39.76  ? 100 ASN A O     1 
ATOM   840  C  CB    . ASN A 1 128 ? 6.168   -4.233  57.559  1.00 36.17  ? 100 ASN A CB    1 
ATOM   841  C  CG    . ASN A 1 128 ? 4.957   -3.709  58.280  1.00 39.81  ? 100 ASN A CG    1 
ATOM   842  O  OD1   . ASN A 1 128 ? 3.944   -4.388  58.358  1.00 42.74  ? 100 ASN A OD1   1 
ATOM   843  N  ND2   . ASN A 1 128 ? 5.053   -2.494  58.817  1.00 38.28  ? 100 ASN A ND2   1 
ATOM   844  N  N     . THR A 1 129 ? 5.252   -6.877  59.532  1.00 40.84  ? 101 THR A N     1 
ATOM   845  C  CA    . THR A 1 129 ? 4.274   -7.921  59.810  1.00 50.89  ? 101 THR A CA    1 
ATOM   846  C  C     . THR A 1 129 ? 2.944   -7.352  60.291  1.00 44.12  ? 101 THR A C     1 
ATOM   847  O  O     . THR A 1 129 ? 2.127   -8.099  60.834  1.00 48.75  ? 101 THR A O     1 
ATOM   848  C  CB    . THR A 1 129 ? 4.815   -8.902  60.862  1.00 51.68  ? 101 THR A CB    1 
ATOM   849  O  OG1   . THR A 1 129 ? 5.221   -8.177  62.032  1.00 58.16  ? 101 THR A OG1   1 
ATOM   850  C  CG2   . THR A 1 129 ? 6.026   -9.663  60.327  1.00 49.34  ? 101 THR A CG2   1 
ATOM   851  N  N     . ASP A 1 130 ? 2.707   -6.057  60.109  1.00 42.08  ? 102 ASP A N     1 
ATOM   852  C  CA    . ASP A 1 130 ? 1.505   -5.436  60.648  1.00 37.34  ? 102 ASP A CA    1 
ATOM   853  C  C     . ASP A 1 130 ? 0.273   -6.036  59.979  1.00 37.22  ? 102 ASP A C     1 
ATOM   854  O  O     . ASP A 1 130 ? 0.293   -6.399  58.800  1.00 40.03  ? 102 ASP A O     1 
ATOM   855  C  CB    . ASP A 1 130 ? 1.541   -3.929  60.411  1.00 40.29  ? 102 ASP A CB    1 
ATOM   856  C  CG    . ASP A 1 130 ? 2.482   -3.219  61.370  1.00 54.34  ? 102 ASP A CG    1 
ATOM   857  O  OD1   . ASP A 1 130 ? 3.034   -3.915  62.244  1.00 49.48  ? 102 ASP A OD1   1 
ATOM   858  O  OD2   . ASP A 1 130 ? 2.746   -2.004  61.188  1.00 54.22  ? 102 ASP A OD2   1 
ATOM   859  N  N     . PHE A 1 131 ? -0.811  -6.105  60.750  1.00 41.96  ? 103 PHE A N     1 
ATOM   860  C  CA    . PHE A 1 131 ? -2.010  -6.826  60.334  1.00 40.03  ? 103 PHE A CA    1 
ATOM   861  C  C     . PHE A 1 131 ? -2.627  -6.211  59.082  1.00 37.46  ? 103 PHE A C     1 
ATOM   862  O  O     . PHE A 1 131 ? -2.957  -6.922  58.125  1.00 38.82  ? 103 PHE A O     1 
ATOM   863  C  CB    . PHE A 1 131 ? -2.997  -6.824  61.503  1.00 40.35  ? 103 PHE A CB    1 
ATOM   864  C  CG    . PHE A 1 131 ? -4.337  -7.458  61.204  1.00 40.04  ? 103 PHE A CG    1 
ATOM   865  C  CD1   . PHE A 1 131 ? -4.484  -8.839  61.222  1.00 40.28  ? 103 PHE A CD1   1 
ATOM   866  C  CD2   . PHE A 1 131 ? -5.448  -6.672  60.953  1.00 37.72  ? 103 PHE A CD2   1 
ATOM   867  C  CE1   . PHE A 1 131 ? -5.709  -9.425  60.975  1.00 33.99  ? 103 PHE A CE1   1 
ATOM   868  C  CE2   . PHE A 1 131 ? -6.674  -7.239  60.702  1.00 43.90  ? 103 PHE A CE2   1 
ATOM   869  C  CZ    . PHE A 1 131 ? -6.811  -8.623  60.720  1.00 41.90  ? 103 PHE A CZ    1 
ATOM   870  N  N     . LEU A 1 132 ? -2.803  -4.887  59.075  1.00 37.81  ? 104 LEU A N     1 
ATOM   871  C  CA    . LEU A 1 132 ? -3.430  -4.210  57.951  1.00 38.11  ? 104 LEU A CA    1 
ATOM   872  C  C     . LEU A 1 132 ? -2.500  -4.076  56.755  1.00 39.91  ? 104 LEU A C     1 
ATOM   873  O  O     . LEU A 1 132 ? -2.975  -3.969  55.620  1.00 39.05  ? 104 LEU A O     1 
ATOM   874  C  CB    . LEU A 1 132 ? -3.913  -2.817  58.355  1.00 37.90  ? 104 LEU A CB    1 
ATOM   875  C  CG    . LEU A 1 132 ? -5.179  -2.716  59.228  1.00 52.10  ? 104 LEU A CG    1 
ATOM   876  C  CD1   . LEU A 1 132 ? -5.365  -1.299  59.745  1.00 53.45  ? 104 LEU A CD1   1 
ATOM   877  C  CD2   . LEU A 1 132 ? -6.456  -3.197  58.527  1.00 47.87  ? 104 LEU A CD2   1 
ATOM   878  N  N     . ILE A 1 133 ? -1.187  -4.082  56.978  1.00 34.15  ? 105 ILE A N     1 
ATOM   879  C  CA    . ILE A 1 133 ? -0.278  -3.912  55.859  1.00 26.70  ? 105 ILE A CA    1 
ATOM   880  C  C     . ILE A 1 133 ? -0.146  -5.192  55.027  1.00 37.07  ? 105 ILE A C     1 
ATOM   881  O  O     . ILE A 1 133 ? 0.192   -5.113  53.837  1.00 37.09  ? 105 ILE A O     1 
ATOM   882  C  CB    . ILE A 1 133 ? 1.057   -3.382  56.407  1.00 34.60  ? 105 ILE A CB    1 
ATOM   883  C  CG1   . ILE A 1 133 ? 0.855   -1.920  56.830  1.00 41.27  ? 105 ILE A CG1   1 
ATOM   884  C  CG2   . ILE A 1 133 ? 2.150   -3.429  55.360  1.00 33.26  ? 105 ILE A CG2   1 
ATOM   885  C  CD1   . ILE A 1 133 ? 2.148   -1.162  57.143  1.00 40.91  ? 105 ILE A CD1   1 
ATOM   886  N  N     . ARG A 1 134 ? -0.451  -6.370  55.590  1.00 29.07  ? 106 ARG A N     1 
ATOM   887  C  CA    . ARG A 1 134 ? -0.321  -7.590  54.791  1.00 34.42  ? 106 ARG A CA    1 
ATOM   888  C  C     . ARG A 1 134 ? -1.141  -7.576  53.506  1.00 31.26  ? 106 ARG A C     1 
ATOM   889  O  O     . ARG A 1 134 ? -0.566  -7.860  52.440  1.00 37.05  ? 106 ARG A O     1 
ATOM   890  C  CB    . ARG A 1 134 ? -0.650  -8.829  55.629  1.00 37.04  ? 106 ARG A CB    1 
ATOM   891  C  CG    . ARG A 1 134 ? -0.225  -10.107 54.917  1.00 44.44  ? 106 ARG A CG    1 
ATOM   892  C  CD    . ARG A 1 134 ? -0.299  -11.321 55.815  1.00 56.16  ? 106 ARG A CD    1 
ATOM   893  N  NE    . ARG A 1 134 ? -1.689  -11.552 56.189  1.00 58.33  ? 106 ARG A NE    1 
ATOM   894  C  CZ    . ARG A 1 134 ? -2.543  -12.316 55.519  1.00 57.34  ? 106 ARG A CZ    1 
ATOM   895  N  NH1   . ARG A 1 134 ? -2.179  -12.974 54.425  1.00 40.67  ? 106 ARG A NH1   1 
ATOM   896  N  NH2   . ARG A 1 134 ? -3.798  -12.410 55.951  1.00 58.85  ? 106 ARG A NH2   1 
ATOM   897  N  N     . PRO A 1 135 ? -2.451  -7.292  53.508  1.00 34.05  ? 107 PRO A N     1 
ATOM   898  C  CA    . PRO A 1 135 ? -3.154  -7.239  52.212  1.00 35.78  ? 107 PRO A CA    1 
ATOM   899  C  C     . PRO A 1 135 ? -2.639  -6.125  51.326  1.00 34.88  ? 107 PRO A C     1 
ATOM   900  O  O     . PRO A 1 135 ? -2.689  -6.249  50.101  1.00 33.42  ? 107 PRO A O     1 
ATOM   901  C  CB    . PRO A 1 135 ? -4.624  -7.014  52.597  1.00 32.35  ? 107 PRO A CB    1 
ATOM   902  C  CG    . PRO A 1 135 ? -4.579  -6.396  53.976  1.00 33.81  ? 107 PRO A CG    1 
ATOM   903  C  CD    . PRO A 1 135 ? -3.359  -7.021  54.636  1.00 35.02  ? 107 PRO A CD    1 
ATOM   904  N  N     . ILE A 1 136 ? -2.145  -5.028  51.907  1.00 31.43  ? 108 ILE A N     1 
ATOM   905  C  CA    . ILE A 1 136 ? -1.652  -3.934  51.077  1.00 31.28  ? 108 ILE A CA    1 
ATOM   906  C  C     . ILE A 1 136 ? -0.404  -4.349  50.302  1.00 33.12  ? 108 ILE A C     1 
ATOM   907  O  O     . ILE A 1 136 ? -0.229  -3.962  49.141  1.00 36.04  ? 108 ILE A O     1 
ATOM   908  C  CB    . ILE A 1 136 ? -1.399  -2.679  51.924  1.00 36.45  ? 108 ILE A CB    1 
ATOM   909  C  CG1   . ILE A 1 136 ? -2.692  -2.231  52.609  1.00 37.37  ? 108 ILE A CG1   1 
ATOM   910  C  CG2   . ILE A 1 136 ? -0.853  -1.571  51.050  1.00 41.19  ? 108 ILE A CG2   1 
ATOM   911  C  CD1   . ILE A 1 136 ? -2.459  -1.265  53.738  1.00 42.62  ? 108 ILE A CD1   1 
ATOM   912  N  N     . LYS A 1 137 ? 0.491   -5.131  50.928  1.00 32.75  ? 109 LYS A N     1 
ATOM   913  C  CA    . LYS A 1 137 ? 1.667   -5.632  50.213  1.00 35.81  ? 109 LYS A CA    1 
ATOM   914  C  C     . LYS A 1 137 ? 1.263   -6.491  49.018  1.00 37.84  ? 109 LYS A C     1 
ATOM   915  O  O     . LYS A 1 137 ? 1.894   -6.432  47.957  1.00 36.97  ? 109 LYS A O     1 
ATOM   916  C  CB    . LYS A 1 137 ? 2.550   -6.453  51.157  1.00 32.22  ? 109 LYS A CB    1 
ATOM   917  C  CG    . LYS A 1 137 ? 3.325   -5.632  52.190  1.00 37.22  ? 109 LYS A CG    1 
ATOM   918  C  CD    . LYS A 1 137 ? 3.701   -6.514  53.408  1.00 38.67  ? 109 LYS A CD    1 
ATOM   919  C  CE    . LYS A 1 137 ? 4.754   -7.562  53.097  1.00 36.26  ? 109 LYS A CE    1 
ATOM   920  N  NZ    . LYS A 1 137 ? 5.262   -8.128  54.387  1.00 35.81  ? 109 LYS A NZ    1 
ATOM   921  N  N     . VAL A 1 138 ? 0.231   -7.317  49.184  1.00 35.70  ? 110 VAL A N     1 
ATOM   922  C  CA    . VAL A 1 138 ? -0.235  -8.135  48.067  1.00 38.21  ? 110 VAL A CA    1 
ATOM   923  C  C     . VAL A 1 138 ? -0.698  -7.235  46.934  1.00 40.11  ? 110 VAL A C     1 
ATOM   924  O  O     . VAL A 1 138 ? -0.306  -7.401  45.775  1.00 38.72  ? 110 VAL A O     1 
ATOM   925  C  CB    . VAL A 1 138 ? -1.361  -9.078  48.519  1.00 43.91  ? 110 VAL A CB    1 
ATOM   926  C  CG1   . VAL A 1 138 ? -1.980  -9.784  47.288  1.00 38.22  ? 110 VAL A CG1   1 
ATOM   927  C  CG2   . VAL A 1 138 ? -0.863  -10.059 49.575  1.00 43.34  ? 110 VAL A CG2   1 
ATOM   928  N  N     . LEU A 1 139 ? -1.514  -6.240  47.271  1.00 37.90  ? 111 LEU A N     1 
ATOM   929  C  CA    . LEU A 1 139 ? -2.005  -5.294  46.278  1.00 36.76  ? 111 LEU A CA    1 
ATOM   930  C  C     . LEU A 1 139 ? -0.871  -4.554  45.577  1.00 41.49  ? 111 LEU A C     1 
ATOM   931  O  O     . LEU A 1 139 ? -0.867  -4.433  44.345  1.00 37.36  ? 111 LEU A O     1 
ATOM   932  C  CB    . LEU A 1 139 ? -2.956  -4.316  46.959  1.00 40.73  ? 111 LEU A CB    1 
ATOM   933  C  CG    . LEU A 1 139 ? -4.059  -3.694  46.141  1.00 50.40  ? 111 LEU A CG    1 
ATOM   934  C  CD1   . LEU A 1 139 ? -5.028  -4.773  45.660  1.00 44.10  ? 111 LEU A CD1   1 
ATOM   935  C  CD2   . LEU A 1 139 ? -4.733  -2.707  47.073  1.00 48.85  ? 111 LEU A CD2   1 
ATOM   936  N  N     . LEU A 1 140 ? 0.085   -4.021  46.344  1.00 42.57  ? 112 LEU A N     1 
ATOM   937  C  CA    . LEU A 1 140 ? 1.219   -3.319  45.744  1.00 39.93  ? 112 LEU A CA    1 
ATOM   938  C  C     . LEU A 1 140 ? 1.979   -4.219  44.781  1.00 39.78  ? 112 LEU A C     1 
ATOM   939  O  O     . LEU A 1 140 ? 2.376   -3.793  43.692  1.00 40.68  ? 112 LEU A O     1 
ATOM   940  C  CB    . LEU A 1 140 ? 2.170   -2.820  46.835  1.00 38.22  ? 112 LEU A CB    1 
ATOM   941  C  CG    . LEU A 1 140 ? 1.845   -1.506  47.529  1.00 40.74  ? 112 LEU A CG    1 
ATOM   942  C  CD1   . LEU A 1 140 ? 2.843   -1.304  48.658  1.00 46.82  ? 112 LEU A CD1   1 
ATOM   943  C  CD2   . LEU A 1 140 ? 1.867   -0.340  46.547  1.00 43.49  ? 112 LEU A CD2   1 
ATOM   944  N  N     . GLN A 1 141 ? 2.229   -5.461  45.188  1.00 38.77  ? 113 GLN A N     1 
ATOM   945  C  CA    . GLN A 1 141 ? 2.913   -6.400  44.315  1.00 41.70  ? 113 GLN A CA    1 
ATOM   946  C  C     . GLN A 1 141 ? 2.128   -6.605  43.026  1.00 43.78  ? 113 GLN A C     1 
ATOM   947  O  O     . GLN A 1 141 ? 2.689   -6.568  41.928  1.00 36.50  ? 113 GLN A O     1 
ATOM   948  C  CB    . GLN A 1 141 ? 3.112   -7.725  45.048  1.00 43.96  ? 113 GLN A CB    1 
ATOM   949  C  CG    . GLN A 1 141 ? 3.996   -8.717  44.328  1.00 58.23  ? 113 GLN A CG    1 
ATOM   950  C  CD    . GLN A 1 141 ? 5.103   -9.220  45.215  1.00 64.48  ? 113 GLN A CD    1 
ATOM   951  O  OE1   . GLN A 1 141 ? 4.891   -9.462  46.405  1.00 68.56  ? 113 GLN A OE1   1 
ATOM   952  N  NE2   . GLN A 1 141 ? 6.302   -9.363  44.651  1.00 67.68  ? 113 GLN A NE2   1 
ATOM   953  N  N     . THR A 1 142 ? 0.812   -6.800  43.145  1.00 41.97  ? 114 THR A N     1 
ATOM   954  C  CA    . THR A 1 142 ? -0.002  -7.062  41.967  1.00 38.11  ? 114 THR A CA    1 
ATOM   955  C  C     . THR A 1 142 ? -0.067  -5.850  41.046  1.00 42.03  ? 114 THR A C     1 
ATOM   956  O  O     . THR A 1 142 ? 0.064   -5.999  39.824  1.00 43.79  ? 114 THR A O     1 
ATOM   957  C  CB    . THR A 1 142 ? -1.395  -7.501  42.404  1.00 38.64  ? 114 THR A CB    1 
ATOM   958  O  OG1   . THR A 1 142 ? -1.277  -8.748  43.093  1.00 38.50  ? 114 THR A OG1   1 
ATOM   959  C  CG2   . THR A 1 142 ? -2.303  -7.672  41.203  1.00 42.43  ? 114 THR A CG2   1 
ATOM   960  N  N     . LEU A 1 143 ? -0.264  -4.644  41.606  1.00 38.86  ? 115 LEU A N     1 
ATOM   961  C  CA    . LEU A 1 143 ? -0.268  -3.434  40.781  1.00 40.49  ? 115 LEU A CA    1 
ATOM   962  C  C     . LEU A 1 143 ? 1.047   -3.238  40.051  1.00 41.86  ? 115 LEU A C     1 
ATOM   963  O  O     . LEU A 1 143 ? 1.054   -2.844  38.878  1.00 39.28  ? 115 LEU A O     1 
ATOM   964  C  CB    . LEU A 1 143 ? -0.576  -2.179  41.606  1.00 39.37  ? 115 LEU A CB    1 
ATOM   965  C  CG    . LEU A 1 143 ? -2.023  -1.733  41.829  1.00 50.76  ? 115 LEU A CG    1 
ATOM   966  C  CD1   . LEU A 1 143 ? -2.071  -0.558  42.792  1.00 46.96  ? 115 LEU A CD1   1 
ATOM   967  C  CD2   . LEU A 1 143 ? -2.636  -1.317  40.504  1.00 52.13  ? 115 LEU A CD2   1 
ATOM   968  N  N     . THR A 1 144 ? 2.171   -3.471  40.732  1.00 38.24  ? 116 THR A N     1 
ATOM   969  C  CA    . THR A 1 144 ? 3.475   -3.276  40.107  1.00 37.84  ? 116 THR A CA    1 
ATOM   970  C  C     . THR A 1 144 ? 3.708   -4.279  38.987  1.00 39.75  ? 116 THR A C     1 
ATOM   971  O  O     . THR A 1 144 ? 4.230   -3.934  37.920  1.00 46.33  ? 116 THR A O     1 
ATOM   972  C  CB    . THR A 1 144 ? 4.580   -3.393  41.166  1.00 41.30  ? 116 THR A CB    1 
ATOM   973  O  OG1   . THR A 1 144 ? 4.324   -2.451  42.214  1.00 46.10  ? 116 THR A OG1   1 
ATOM   974  C  CG2   . THR A 1 144 ? 5.946   -3.099  40.565  1.00 46.28  ? 116 THR A CG2   1 
ATOM   975  N  N     . GLU A 1 145 ? 3.334   -5.528  39.220  1.00 37.15  ? 117 GLU A N     1 
ATOM   976  C  CA    A GLU A 1 145 ? 3.526   -6.583  38.226  0.60 46.64  ? 117 GLU A CA    1 
ATOM   977  C  CA    B GLU A 1 145 ? 3.574   -6.538  38.205  0.40 46.64  ? 117 GLU A CA    1 
ATOM   978  C  C     . GLU A 1 145 ? 2.641   -6.359  37.007  1.00 51.54  ? 117 GLU A C     1 
ATOM   979  O  O     . GLU A 1 145 ? 3.080   -6.501  35.861  1.00 45.85  ? 117 GLU A O     1 
ATOM   980  C  CB    A GLU A 1 145 ? 3.207   -7.946  38.840  0.60 47.39  ? 117 GLU A CB    1 
ATOM   981  C  CB    B GLU A 1 145 ? 3.466   -7.902  38.861  0.40 47.55  ? 117 GLU A CB    1 
ATOM   982  C  CG    A GLU A 1 145 ? 4.296   -8.535  39.713  0.60 53.23  ? 117 GLU A CG    1 
ATOM   983  C  CG    B GLU A 1 145 ? 2.102   -8.453  38.886  0.40 51.08  ? 117 GLU A CG    1 
ATOM   984  C  CD    A GLU A 1 145 ? 3.839   -9.811  40.402  0.60 58.85  ? 117 GLU A CD    1 
ATOM   985  C  CD    B GLU A 1 145 ? 1.992   -9.494  39.937  0.40 56.09  ? 117 GLU A CD    1 
ATOM   986  O  OE1   A GLU A 1 145 ? 2.766   -10.342 40.030  0.60 61.83  ? 117 GLU A OE1   1 
ATOM   987  O  OE1   B GLU A 1 145 ? 2.939   -9.666  40.731  0.40 59.68  ? 117 GLU A OE1   1 
ATOM   988  O  OE2   A GLU A 1 145 ? 4.534   -10.261 41.338  0.60 64.46  ? 117 GLU A OE2   1 
ATOM   989  O  OE2   B GLU A 1 145 ? 0.920   -10.069 40.042  0.40 58.96  ? 117 GLU A OE2   1 
ATOM   990  N  N     . SER A 1 146 ? 1.372   -6.010  37.235  1.00 44.80  ? 118 SER A N     1 
ATOM   991  C  CA    . SER A 1 146 ? 0.512   -5.683  36.101  1.00 45.12  ? 118 SER A CA    1 
ATOM   992  C  C     . SER A 1 146 ? 1.068   -4.476  35.359  1.00 43.25  ? 118 SER A C     1 
ATOM   993  O  O     . SER A 1 146 ? 1.078   -4.435  34.121  1.00 47.10  ? 118 SER A O     1 
ATOM   994  C  CB    . SER A 1 146 ? -0.926  -5.434  36.583  1.00 45.02  ? 118 SER A CB    1 
ATOM   995  O  OG    . SER A 1 146 ? -1.607  -4.551  35.707  1.00 49.28  ? 118 SER A OG    1 
ATOM   996  N  N     . HIS A 1 147 ? 1.587   -3.503  36.105  1.00 43.95  ? 119 HIS A N     1 
ATOM   997  C  CA    . HIS A 1 147 ? 2.201   -2.330  35.495  1.00 36.94  ? 119 HIS A CA    1 
ATOM   998  C  C     . HIS A 1 147 ? 3.377   -2.701  34.597  1.00 45.01  ? 119 HIS A C     1 
ATOM   999  O  O     . HIS A 1 147 ? 3.573   -2.102  33.528  1.00 45.47  ? 119 HIS A O     1 
ATOM   1000 C  CB    . HIS A 1 147 ? 2.669   -1.376  36.583  1.00 45.62  ? 119 HIS A CB    1 
ATOM   1001 C  CG    . HIS A 1 147 ? 2.649   0.049   36.161  1.00 40.86  ? 119 HIS A CG    1 
ATOM   1002 N  ND1   . HIS A 1 147 ? 3.596   0.583   35.319  1.00 49.22  ? 119 HIS A ND1   1 
ATOM   1003 C  CD2   . HIS A 1 147 ? 1.783   1.048   36.444  1.00 45.31  ? 119 HIS A CD2   1 
ATOM   1004 C  CE1   . HIS A 1 147 ? 3.319   1.857   35.106  1.00 50.35  ? 119 HIS A CE1   1 
ATOM   1005 N  NE2   . HIS A 1 147 ? 2.221   2.162   35.774  1.00 51.87  ? 119 HIS A NE2   1 
ATOM   1006 N  N     . ARG A 1 148 ? 4.190   -3.666  35.028  1.00 41.15  ? 120 ARG A N     1 
ATOM   1007 C  CA    . ARG A 1 148 ? 5.340   -4.067  34.230  1.00 42.97  ? 120 ARG A CA    1 
ATOM   1008 C  C     . ARG A 1 148 ? 4.912   -4.788  32.953  1.00 50.40  ? 120 ARG A C     1 
ATOM   1009 O  O     . ARG A 1 148 ? 5.580   -4.666  31.924  1.00 49.34  ? 120 ARG A O     1 
ATOM   1010 C  CB    . ARG A 1 148 ? 6.269   -4.939  35.070  1.00 42.76  ? 120 ARG A CB    1 
ATOM   1011 C  CG    . ARG A 1 148 ? 6.905   -4.196  36.257  1.00 48.31  ? 120 ARG A CG    1 
ATOM   1012 C  CD    . ARG A 1 148 ? 7.642   -2.939  35.818  1.00 48.25  ? 120 ARG A CD    1 
ATOM   1013 N  NE    . ARG A 1 148 ? 8.759   -2.613  36.695  1.00 53.95  ? 120 ARG A NE    1 
ATOM   1014 C  CZ    . ARG A 1 148 ? 9.724   -1.749  36.402  1.00 56.52  ? 120 ARG A CZ    1 
ATOM   1015 N  NH1   . ARG A 1 148 ? 9.784   -1.149  35.223  1.00 52.15  ? 120 ARG A NH1   1 
ATOM   1016 N  NH2   . ARG A 1 148 ? 10.655  -1.481  37.314  1.00 55.53  ? 120 ARG A NH2   1 
ATOM   1017 N  N     . ILE A 1 149 ? 3.803   -5.528  32.984  1.00 46.62  ? 121 ILE A N     1 
ATOM   1018 C  CA    . ILE A 1 149 ? 3.307   -6.139  31.754  1.00 49.49  ? 121 ILE A CA    1 
ATOM   1019 C  C     . ILE A 1 149 ? 2.873   -5.068  30.763  1.00 51.70  ? 121 ILE A C     1 
ATOM   1020 O  O     . ILE A 1 149 ? 3.286   -5.071  29.596  1.00 48.79  ? 121 ILE A O     1 
ATOM   1021 C  CB    . ILE A 1 149 ? 2.167   -7.118  32.061  1.00 48.36  ? 121 ILE A CB    1 
ATOM   1022 C  CG1   . ILE A 1 149 ? 2.704   -8.285  32.882  1.00 48.02  ? 121 ILE A CG1   1 
ATOM   1023 C  CG2   . ILE A 1 149 ? 1.511   -7.572  30.768  1.00 51.84  ? 121 ILE A CG2   1 
ATOM   1024 C  CD1   . ILE A 1 149 ? 1.638   -9.266  33.314  1.00 56.43  ? 121 ILE A CD1   1 
ATOM   1025 N  N     . LEU A 1 150 ? 2.039   -4.132  31.220  1.00 43.03  ? 122 LEU A N     1 
ATOM   1026 C  CA    . LEU A 1 150 ? 1.550   -3.048  30.372  1.00 48.27  ? 122 LEU A CA    1 
ATOM   1027 C  C     . LEU A 1 150 ? 2.678   -2.207  29.801  1.00 53.16  ? 122 LEU A C     1 
ATOM   1028 O  O     . LEU A 1 150 ? 2.548   -1.655  28.702  1.00 48.27  ? 122 LEU A O     1 
ATOM   1029 C  CB    . LEU A 1 150 ? 0.612   -2.145  31.171  1.00 46.24  ? 122 LEU A CB    1 
ATOM   1030 C  CG    . LEU A 1 150 ? -0.883  -2.412  31.064  1.00 57.37  ? 122 LEU A CG    1 
ATOM   1031 C  CD1   . LEU A 1 150 ? -1.235  -3.825  31.538  1.00 54.04  ? 122 LEU A CD1   1 
ATOM   1032 C  CD2   . LEU A 1 150 ? -1.620  -1.354  31.865  1.00 57.90  ? 122 LEU A CD2   1 
ATOM   1033 N  N     . GLU A 1 151 ? 3.772   -2.061  30.549  1.00 46.72  ? 123 GLU A N     1 
ATOM   1034 C  CA    . GLU A 1 151 ? 4.905   -1.273  30.082  1.00 49.97  ? 123 GLU A CA    1 
ATOM   1035 C  C     . GLU A 1 151 ? 5.464   -1.829  28.775  1.00 50.49  ? 123 GLU A C     1 
ATOM   1036 O  O     . GLU A 1 151 ? 5.919   -1.067  27.915  1.00 52.31  ? 123 GLU A O     1 
ATOM   1037 C  CB    . GLU A 1 151 ? 5.982   -1.269  31.171  1.00 48.20  ? 123 GLU A CB    1 
ATOM   1038 C  CG    . GLU A 1 151 ? 7.129   -0.287  30.984  1.00 63.36  ? 123 GLU A CG    1 
ATOM   1039 C  CD    . GLU A 1 151 ? 8.333   -0.619  31.867  1.00 66.62  ? 123 GLU A CD    1 
ATOM   1040 O  OE1   . GLU A 1 151 ? 8.150   -1.274  32.918  1.00 61.37  ? 123 GLU A OE1   1 
ATOM   1041 O  OE2   . GLU A 1 151 ? 9.456   -0.180  31.537  1.00 59.03  ? 123 GLU A OE2   1 
ATOM   1042 N  N     . LYS A 1 152 ? 5.440   -3.155  28.616  1.00 43.81  ? 124 LYS A N     1 
ATOM   1043 C  CA    . LYS A 1 152 ? 5.968   -3.786  27.408  1.00 50.44  ? 124 LYS A CA    1 
ATOM   1044 C  C     . LYS A 1 152 ? 5.121   -3.488  26.176  1.00 53.44  ? 124 LYS A C     1 
ATOM   1045 O  O     . LYS A 1 152 ? 5.661   -3.403  25.064  1.00 49.58  ? 124 LYS A O     1 
ATOM   1046 C  CB    . LYS A 1 152 ? 6.082   -5.294  27.628  1.00 47.08  ? 124 LYS A CB    1 
ATOM   1047 C  CG    . LYS A 1 152 ? 7.187   -5.679  28.598  1.00 60.45  ? 124 LYS A CG    1 
ATOM   1048 C  CD    . LYS A 1 152 ? 8.444   -4.850  28.288  1.00 61.29  ? 124 LYS A CD    1 
ATOM   1049 C  CE    . LYS A 1 152 ? 9.618   -5.190  29.201  1.00 70.54  ? 124 LYS A CE    1 
ATOM   1050 N  NZ    . LYS A 1 152 ? 9.735   -6.657  29.441  1.00 73.79  ? 124 LYS A NZ    1 
ATOM   1051 N  N     . TYR A 1 153 ? 3.810   -3.321  26.345  1.00 47.80  ? 125 TYR A N     1 
ATOM   1052 C  CA    . TYR A 1 153 ? 2.889   -3.176  25.228  1.00 45.47  ? 125 TYR A CA    1 
ATOM   1053 C  C     . TYR A 1 153 ? 2.564   -1.729  24.901  1.00 50.70  ? 125 TYR A C     1 
ATOM   1054 O  O     . TYR A 1 153 ? 1.654   -1.479  24.106  1.00 57.32  ? 125 TYR A O     1 
ATOM   1055 C  CB    . TYR A 1 153 ? 1.595   -3.931  25.519  1.00 40.58  ? 125 TYR A CB    1 
ATOM   1056 C  CG    . TYR A 1 153 ? 1.793   -5.406  25.603  1.00 45.52  ? 125 TYR A CG    1 
ATOM   1057 C  CD1   . TYR A 1 153 ? 1.779   -6.188  24.458  1.00 39.17  ? 125 TYR A CD1   1 
ATOM   1058 C  CD2   . TYR A 1 153 ? 2.009   -6.027  26.824  1.00 49.15  ? 125 TYR A CD2   1 
ATOM   1059 C  CE1   . TYR A 1 153 ? 1.968   -7.547  24.523  1.00 45.36  ? 125 TYR A CE1   1 
ATOM   1060 C  CE2   . TYR A 1 153 ? 2.199   -7.395  26.903  1.00 44.24  ? 125 TYR A CE2   1 
ATOM   1061 C  CZ    . TYR A 1 153 ? 2.182   -8.150  25.740  1.00 44.60  ? 125 TYR A CZ    1 
ATOM   1062 O  OH    . TYR A 1 153 ? 2.367   -9.509  25.790  1.00 58.23  ? 125 TYR A OH    1 
ATOM   1063 N  N     . THR A 1 154 ? 3.262   -0.764  25.489  1.00 52.05  ? 126 THR A N     1 
ATOM   1064 C  CA    A THR A 1 154 ? 2.956   0.647   25.301  0.68 57.54  ? 126 THR A CA    1 
ATOM   1065 C  CA    B THR A 1 154 ? 2.934   0.628   25.245  0.32 57.56  ? 126 THR A CA    1 
ATOM   1066 C  C     . THR A 1 154 ? 4.098   1.349   24.581  1.00 64.18  ? 126 THR A C     1 
ATOM   1067 O  O     . THR A 1 154 ? 5.270   0.989   24.754  1.00 61.89  ? 126 THR A O     1 
ATOM   1068 C  CB    A THR A 1 154 ? 2.687   1.355   26.641  0.68 60.72  ? 126 THR A CB    1 
ATOM   1069 C  CB    B THR A 1 154 ? 2.519   1.343   26.541  0.32 60.64  ? 126 THR A CB    1 
ATOM   1070 O  OG1   A THR A 1 154 ? 3.493   0.775   27.671  0.68 61.11  ? 126 THR A OG1   1 
ATOM   1071 O  OG1   B THR A 1 154 ? 2.312   2.740   26.287  0.32 60.87  ? 126 THR A OG1   1 
ATOM   1072 C  CG2   A THR A 1 154 ? 1.221   1.244   27.026  0.68 58.30  ? 126 THR A CG2   1 
ATOM   1073 C  CG2   B THR A 1 154 ? 3.559   1.165   27.594  0.32 59.41  ? 126 THR A CG2   1 
ATOM   1074 N  N     . GLN A 1 155 ? 3.739   2.354   23.788  1.00 63.45  ? 127 GLN A N     1 
ATOM   1075 C  CA    . GLN A 1 155 ? 4.713   3.156   23.069  1.00 68.68  ? 127 GLN A CA    1 
ATOM   1076 C  C     . GLN A 1 155 ? 5.721   3.731   24.053  1.00 69.46  ? 127 GLN A C     1 
ATOM   1077 O  O     . GLN A 1 155 ? 5.322   4.378   25.033  1.00 62.03  ? 127 GLN A O     1 
ATOM   1078 C  CB    . GLN A 1 155 ? 4.015   4.291   22.328  1.00 74.21  ? 127 GLN A CB    1 
ATOM   1079 C  CG    . GLN A 1 155 ? 4.864   5.097   21.361  1.00 75.74  ? 127 GLN A CG    1 
ATOM   1080 C  CD    . GLN A 1 155 ? 4.010   5.829   20.342  1.00 76.75  ? 127 GLN A CD    1 
ATOM   1081 O  OE1   . GLN A 1 155 ? 4.083   7.061   20.218  1.00 71.30  ? 127 GLN A OE1   1 
ATOM   1082 N  NE2   . GLN A 1 155 ? 3.161   5.082   19.634  1.00 78.55  ? 127 GLN A NE2   1 
ATOM   1083 N  N     . PRO A 1 156 ? 7.025   3.520   23.833  1.00 74.73  ? 128 PRO A N     1 
ATOM   1084 C  CA    . PRO A 1 156 ? 8.051   4.137   24.690  1.00 65.43  ? 128 PRO A CA    1 
ATOM   1085 C  C     . PRO A 1 156 ? 7.884   5.639   24.884  1.00 60.11  ? 128 PRO A C     1 
ATOM   1086 O  O     . PRO A 1 156 ? 8.365   6.198   25.876  1.00 57.95  ? 128 PRO A O     1 
ATOM   1087 C  CB    . PRO A 1 156 ? 9.359   3.830   23.945  1.00 74.15  ? 128 PRO A CB    1 
ATOM   1088 C  CG    . PRO A 1 156 ? 8.955   3.192   22.615  1.00 68.76  ? 128 PRO A CG    1 
ATOM   1089 C  CD    . PRO A 1 156 ? 7.603   2.608   22.834  1.00 71.68  ? 128 PRO A CD    1 
ATOM   1090 N  N     . SER A 1 157 ? 7.196   6.303   23.950  1.00 63.81  ? 129 SER A N     1 
ATOM   1091 C  CA    . SER A 1 157 ? 7.116   7.760   23.967  1.00 51.51  ? 129 SER A CA    1 
ATOM   1092 C  C     . SER A 1 157 ? 6.138   8.292   25.014  1.00 59.63  ? 129 SER A C     1 
ATOM   1093 O  O     . SER A 1 157 ? 6.318   9.420   25.486  1.00 53.61  ? 129 SER A O     1 
ATOM   1094 C  CB    . SER A 1 157 ? 6.737   8.282   22.578  1.00 58.33  ? 129 SER A CB    1 
ATOM   1095 O  OG    . SER A 1 157 ? 7.497   7.646   21.553  1.00 66.46  ? 129 SER A OG    1 
ATOM   1096 N  N     . ILE A 1 158 ? 5.091   7.533   25.377  1.00 57.13  ? 130 ILE A N     1 
ATOM   1097 C  CA    . ILE A 1 158 ? 4.237   7.959   26.491  1.00 49.46  ? 130 ILE A CA    1 
ATOM   1098 C  C     . ILE A 1 158 ? 5.042   8.101   27.779  1.00 49.51  ? 130 ILE A C     1 
ATOM   1099 O  O     . ILE A 1 158 ? 4.875   9.076   28.522  1.00 48.82  ? 130 ILE A O     1 
ATOM   1100 C  CB    . ILE A 1 158 ? 3.023   7.022   26.675  1.00 56.92  ? 130 ILE A CB    1 
ATOM   1101 C  CG1   . ILE A 1 158 ? 2.062   7.120   25.481  1.00 54.78  ? 130 ILE A CG1   1 
ATOM   1102 C  CG2   . ILE A 1 158 ? 2.321   7.282   27.991  1.00 53.02  ? 130 ILE A CG2   1 
ATOM   1103 C  CD1   . ILE A 1 158 ? 2.265   6.129   24.434  1.00 62.24  ? 130 ILE A CD1   1 
ATOM   1104 N  N     . PHE A 1 159 ? 5.941   7.157   28.055  1.00 51.11  ? 131 PHE A N     1 
ATOM   1105 C  CA    . PHE A 1 159 ? 6.728   7.273   29.278  1.00 51.94  ? 131 PHE A CA    1 
ATOM   1106 C  C     . PHE A 1 159 ? 7.581   8.531   29.282  1.00 52.90  ? 131 PHE A C     1 
ATOM   1107 O  O     . PHE A 1 159 ? 7.774   9.141   30.340  1.00 49.52  ? 131 PHE A O     1 
ATOM   1108 C  CB    . PHE A 1 159 ? 7.591   6.037   29.472  1.00 52.16  ? 131 PHE A CB    1 
ATOM   1109 C  CG    . PHE A 1 159 ? 6.798   4.797   29.687  1.00 52.98  ? 131 PHE A CG    1 
ATOM   1110 C  CD1   . PHE A 1 159 ? 5.921   4.704   30.759  1.00 51.97  ? 131 PHE A CD1   1 
ATOM   1111 C  CD2   . PHE A 1 159 ? 6.932   3.715   28.833  1.00 60.94  ? 131 PHE A CD2   1 
ATOM   1112 C  CE1   . PHE A 1 159 ? 5.182   3.564   30.964  1.00 52.66  ? 131 PHE A CE1   1 
ATOM   1113 C  CE2   . PHE A 1 159 ? 6.199   2.568   29.041  1.00 58.63  ? 131 PHE A CE2   1 
ATOM   1114 C  CZ    . PHE A 1 159 ? 5.321   2.496   30.109  1.00 53.24  ? 131 PHE A CZ    1 
ATOM   1115 N  N     . LYS A 1 160 ? 8.077   8.954   28.114  1.00 57.54  ? 132 LYS A N     1 
ATOM   1116 C  CA    . LYS A 1 160 ? 8.881   10.173  28.055  1.00 55.68  ? 132 LYS A CA    1 
ATOM   1117 C  C     . LYS A 1 160 ? 8.040   11.409  28.359  1.00 53.07  ? 132 LYS A C     1 
ATOM   1118 O  O     . LYS A 1 160 ? 8.510   12.342  29.019  1.00 55.16  ? 132 LYS A O     1 
ATOM   1119 C  CB    . LYS A 1 160 ? 9.545   10.300  26.682  1.00 62.73  ? 132 LYS A CB    1 
ATOM   1120 C  CG    . LYS A 1 160 ? 10.425  9.111   26.309  1.00 71.89  ? 132 LYS A CG    1 
ATOM   1121 C  CD    . LYS A 1 160 ? 11.400  8.752   27.428  1.00 80.94  ? 132 LYS A CD    1 
ATOM   1122 C  CE    . LYS A 1 160 ? 12.810  8.523   26.901  1.00 82.94  ? 132 LYS A CE    1 
ATOM   1123 N  NZ    . LYS A 1 160 ? 13.612  7.671   27.828  1.00 88.56  ? 132 LYS A NZ    1 
ATOM   1124 N  N     . ILE A 1 161 ? 6.794   11.440  27.887  1.00 51.36  ? 133 ILE A N     1 
ATOM   1125 C  CA    . ILE A 1 161 ? 5.918   12.569  28.187  1.00 46.43  ? 133 ILE A CA    1 
ATOM   1126 C  C     . ILE A 1 161 ? 5.622   12.628  29.680  1.00 51.13  ? 133 ILE A C     1 
ATOM   1127 O  O     . ILE A 1 161 ? 5.588   13.707  30.287  1.00 50.01  ? 133 ILE A O     1 
ATOM   1128 C  CB    . ILE A 1 161 ? 4.620   12.458  27.367  1.00 49.12  ? 133 ILE A CB    1 
ATOM   1129 C  CG1   . ILE A 1 161 ? 4.930   12.466  25.866  1.00 51.32  ? 133 ILE A CG1   1 
ATOM   1130 C  CG2   . ILE A 1 161 ? 3.671   13.573  27.743  1.00 47.55  ? 133 ILE A CG2   1 
ATOM   1131 C  CD1   . ILE A 1 161 ? 3.958   11.615  25.045  1.00 51.36  ? 133 ILE A CD1   1 
ATOM   1132 N  N     . ILE A 1 162 ? 5.381   11.465  30.286  1.00 48.65  ? 134 ILE A N     1 
ATOM   1133 C  CA    . ILE A 1 162 ? 5.161   11.390  31.726  1.00 50.96  ? 134 ILE A CA    1 
ATOM   1134 C  C     . ILE A 1 162 ? 6.358   11.957  32.479  1.00 44.74  ? 134 ILE A C     1 
ATOM   1135 O  O     . ILE A 1 162 ? 6.201   12.790  33.380  1.00 48.78  ? 134 ILE A O     1 
ATOM   1136 C  CB    . ILE A 1 162 ? 4.869   9.938   32.141  1.00 47.81  ? 134 ILE A CB    1 
ATOM   1137 C  CG1   . ILE A 1 162 ? 3.439   9.553   31.741  1.00 43.89  ? 134 ILE A CG1   1 
ATOM   1138 C  CG2   . ILE A 1 162 ? 5.122   9.738   33.639  1.00 52.27  ? 134 ILE A CG2   1 
ATOM   1139 C  CD1   . ILE A 1 162 ? 3.278   8.097   31.411  1.00 48.01  ? 134 ILE A CD1   1 
ATOM   1140 N  N     . SER A 1 163 ? 7.574   11.534  32.099  1.00 52.01  ? 135 SER A N     1 
ATOM   1141 C  CA    . SER A 1 163 ? 8.778   11.967  32.810  1.00 55.23  ? 135 SER A CA    1 
ATOM   1142 C  C     . SER A 1 163 ? 8.962   13.470  32.731  1.00 56.44  ? 135 SER A C     1 
ATOM   1143 O  O     . SER A 1 163 ? 9.522   14.079  33.649  1.00 61.54  ? 135 SER A O     1 
ATOM   1144 C  CB    . SER A 1 163 ? 10.012  11.271  32.244  1.00 54.67  ? 135 SER A CB    1 
ATOM   1145 O  OG    . SER A 1 163 ? 9.806   9.873   32.172  1.00 63.11  ? 135 SER A OG    1 
ATOM   1146 N  N     . GLN A 1 164 ? 8.495   14.085  31.653  1.00 60.84  ? 136 GLN A N     1 
ATOM   1147 C  CA    . GLN A 1 164 ? 8.547   15.531  31.500  1.00 53.61  ? 136 GLN A CA    1 
ATOM   1148 C  C     . GLN A 1 164 ? 7.456   16.245  32.284  1.00 54.81  ? 136 GLN A C     1 
ATOM   1149 O  O     . GLN A 1 164 ? 7.371   17.474  32.228  1.00 60.77  ? 136 GLN A O     1 
ATOM   1150 C  CB    . GLN A 1 164 ? 8.474   15.872  30.011  1.00 63.20  ? 136 GLN A CB    1 
ATOM   1151 C  CG    . GLN A 1 164 ? 9.775   15.511  29.290  1.00 73.08  ? 136 GLN A CG    1 
ATOM   1152 C  CD    . GLN A 1 164 ? 9.614   15.333  27.785  1.00 84.04  ? 136 GLN A CD    1 
ATOM   1153 O  OE1   . GLN A 1 164 ? 10.522  14.833  27.110  1.00 77.34  ? 136 GLN A OE1   1 
ATOM   1154 N  NE2   . GLN A 1 164 ? 8.449   15.709  27.259  1.00 73.09  ? 136 GLN A NE2   1 
ATOM   1155 N  N     . GLY A 1 165 ? 6.630   15.514  33.019  1.00 57.89  ? 137 GLY A N     1 
ATOM   1156 C  CA    . GLY A 1 165 ? 5.668   16.134  33.903  1.00 50.86  ? 137 GLY A CA    1 
ATOM   1157 C  C     . GLY A 1 165 ? 4.315   16.434  33.307  1.00 54.80  ? 137 GLY A C     1 
ATOM   1158 O  O     . GLY A 1 165 ? 3.583   17.258  33.866  1.00 52.04  ? 137 GLY A O     1 
ATOM   1159 N  N     . THR A 1 166 ? 3.950   15.808  32.193  1.00 55.25  ? 138 THR A N     1 
ATOM   1160 C  CA    . THR A 1 166 ? 2.650   16.070  31.589  1.00 51.99  ? 138 THR A CA    1 
ATOM   1161 C  C     . THR A 1 166 ? 1.873   14.771  31.438  1.00 55.42  ? 138 THR A C     1 
ATOM   1162 O  O     . THR A 1 166 ? 2.448   13.720  31.142  1.00 50.43  ? 138 THR A O     1 
ATOM   1163 C  CB    . THR A 1 166 ? 2.783   16.766  30.224  1.00 65.54  ? 138 THR A CB    1 
ATOM   1164 O  OG1   . THR A 1 166 ? 3.812   16.132  29.460  1.00 65.53  ? 138 THR A OG1   1 
ATOM   1165 C  CG2   . THR A 1 166 ? 3.135   18.235  30.408  1.00 59.72  ? 138 THR A CG2   1 
ATOM   1166 N  N     . ASN A 1 167 ? 0.571   14.853  31.677  1.00 57.00  ? 139 ASN A N     1 
ATOM   1167 C  CA    . ASN A 1 167 ? -0.317  13.738  31.404  1.00 55.37  ? 139 ASN A CA    1 
ATOM   1168 C  C     . ASN A 1 167 ? -0.454  13.573  29.897  1.00 54.08  ? 139 ASN A C     1 
ATOM   1169 O  O     . ASN A 1 167 ? -0.876  14.521  29.217  1.00 60.60  ? 139 ASN A O     1 
ATOM   1170 C  CB    . ASN A 1 167 ? -1.689  13.971  32.029  1.00 47.04  ? 139 ASN A CB    1 
ATOM   1171 C  CG    . ASN A 1 167 ? -2.577  12.755  31.927  1.00 56.53  ? 139 ASN A CG    1 
ATOM   1172 O  OD1   . ASN A 1 167 ? -2.651  12.108  30.880  1.00 52.44  ? 139 ASN A OD1   1 
ATOM   1173 N  ND2   . ASN A 1 167 ? -3.278  12.444  33.009  1.00 67.25  ? 139 ASN A ND2   1 
ATOM   1174 N  N     . PRO A 1 168 ? -0.136  12.404  29.337  1.00 56.65  ? 140 PRO A N     1 
ATOM   1175 C  CA    . PRO A 1 168 ? -0.276  12.229  27.878  1.00 57.08  ? 140 PRO A CA    1 
ATOM   1176 C  C     . PRO A 1 168 ? -1.695  12.467  27.379  1.00 56.18  ? 140 PRO A C     1 
ATOM   1177 O  O     . PRO A 1 168 ? -1.877  12.928  26.246  1.00 58.59  ? 140 PRO A O     1 
ATOM   1178 C  CB    . PRO A 1 168 ? 0.157   10.775  27.643  1.00 56.84  ? 140 PRO A CB    1 
ATOM   1179 C  CG    . PRO A 1 168 ? 0.684   10.266  28.933  1.00 58.53  ? 140 PRO A CG    1 
ATOM   1180 C  CD    . PRO A 1 168 ? 0.314   11.188  30.033  1.00 55.69  ? 140 PRO A CD    1 
ATOM   1181 N  N     . LEU A 1 169 ? -2.712  12.176  28.188  1.00 50.98  ? 141 LEU A N     1 
ATOM   1182 C  CA    . LEU A 1 169 ? -4.079  12.407  27.740  1.00 53.52  ? 141 LEU A CA    1 
ATOM   1183 C  C     . LEU A 1 169 ? -4.443  13.880  27.666  1.00 58.08  ? 141 LEU A C     1 
ATOM   1184 O  O     . LEU A 1 169 ? -5.548  14.198  27.216  1.00 58.06  ? 141 LEU A O     1 
ATOM   1185 C  CB    . LEU A 1 169 ? -5.071  11.685  28.656  1.00 57.67  ? 141 LEU A CB    1 
ATOM   1186 C  CG    . LEU A 1 169 ? -4.714  10.241  28.998  1.00 53.15  ? 141 LEU A CG    1 
ATOM   1187 C  CD1   . LEU A 1 169 ? -5.484  9.783   30.226  1.00 56.82  ? 141 LEU A CD1   1 
ATOM   1188 C  CD2   . LEU A 1 169 ? -5.000  9.335   27.802  1.00 57.61  ? 141 LEU A CD2   1 
ATOM   1189 N  N     . ASN A 1 170 ? -3.563  14.787  28.083  1.00 56.61  ? 142 ASN A N     1 
ATOM   1190 C  CA    . ASN A 1 170 ? -3.904  16.202  28.149  1.00 59.82  ? 142 ASN A CA    1 
ATOM   1191 C  C     . ASN A 1 170 ? -3.056  17.050  27.215  1.00 61.33  ? 142 ASN A C     1 
ATOM   1192 O  O     . ASN A 1 170 ? -3.136  18.282  27.261  1.00 66.25  ? 142 ASN A O     1 
ATOM   1193 C  CB    . ASN A 1 170 ? -3.763  16.709  29.583  1.00 67.42  ? 142 ASN A CB    1 
ATOM   1194 C  CG    . ASN A 1 170 ? -5.077  16.724  30.313  1.00 74.65  ? 142 ASN A CG    1 
ATOM   1195 O  OD1   . ASN A 1 170 ? -5.437  15.751  30.978  1.00 77.55  ? 142 ASN A OD1   1 
ATOM   1196 N  ND2   . ASN A 1 170 ? -5.821  17.816  30.174  1.00 82.89  ? 142 ASN A ND2   1 
ATOM   1197 N  N     . ILE A 1 171 ? -2.236  16.420  26.382  1.00 59.22  ? 143 ILE A N     1 
ATOM   1198 C  CA    A ILE A 1 171 ? -1.411  17.142  25.423  0.56 60.17  ? 143 ILE A CA    1 
ATOM   1199 C  CA    B ILE A 1 171 ? -1.417  17.173  25.447  0.44 60.17  ? 143 ILE A CA    1 
ATOM   1200 C  C     . ILE A 1 171 ? -2.307  17.857  24.418  1.00 65.16  ? 143 ILE A C     1 
ATOM   1201 O  O     . ILE A 1 171 ? -3.337  17.316  23.983  1.00 55.96  ? 143 ILE A O     1 
ATOM   1202 C  CB    A ILE A 1 171 ? -0.454  16.156  24.729  0.56 58.33  ? 143 ILE A CB    1 
ATOM   1203 C  CB    B ILE A 1 171 ? -0.396  16.246  24.775  0.44 58.36  ? 143 ILE A CB    1 
ATOM   1204 C  CG1   A ILE A 1 171 ? 0.629   15.680  25.700  0.56 60.43  ? 143 ILE A CG1   1 
ATOM   1205 C  CG1   B ILE A 1 171 ? -1.123  15.061  24.150  0.44 53.66  ? 143 ILE A CG1   1 
ATOM   1206 C  CG2   A ILE A 1 171 ? 0.194   16.768  23.495  0.56 60.06  ? 143 ILE A CG2   1 
ATOM   1207 C  CG2   B ILE A 1 171 ? 0.644   15.780  25.786  0.44 60.35  ? 143 ILE A CG2   1 
ATOM   1208 C  CD1   A ILE A 1 171 ? 1.466   14.542  25.144  0.56 61.54  ? 143 ILE A CD1   1 
ATOM   1209 C  CD1   B ILE A 1 171 ? -0.220  14.117  23.458  0.44 57.74  ? 143 ILE A CD1   1 
ATOM   1210 N  N     . ARG A 1 172 ? -1.931  19.080  24.052  1.00 61.81  ? 144 ARG A N     1 
ATOM   1211 C  CA    . ARG A 1 172 ? -2.604  19.783  22.971  1.00 60.44  ? 144 ARG A CA    1 
ATOM   1212 C  C     . ARG A 1 172 ? -2.074  19.281  21.630  1.00 52.35  ? 144 ARG A C     1 
ATOM   1213 O  O     . ARG A 1 172 ? -0.891  18.960  21.515  1.00 50.74  ? 144 ARG A O     1 
ATOM   1214 C  CB    . ARG A 1 172 ? -2.372  21.282  23.079  1.00 73.24  ? 144 ARG A CB    1 
ATOM   1215 C  CG    . ARG A 1 172 ? -3.106  21.965  24.219  1.00 90.19  ? 144 ARG A CG    1 
ATOM   1216 C  CD    . ARG A 1 172 ? -2.772  23.454  24.218  1.00 99.90  ? 144 ARG A CD    1 
ATOM   1217 N  NE    . ARG A 1 172 ? -3.731  24.253  23.465  1.00 107.69 ? 144 ARG A NE    1 
ATOM   1218 C  CZ    . ARG A 1 172 ? -3.437  24.914  22.352  1.00 112.26 ? 144 ARG A CZ    1 
ATOM   1219 N  NH1   . ARG A 1 172 ? -2.224  24.870  21.820  1.00 107.58 ? 144 ARG A NH1   1 
ATOM   1220 N  NH2   . ARG A 1 172 ? -4.383  25.638  21.758  1.00 105.54 ? 144 ARG A NH2   1 
ATOM   1221 N  N     . PRO A 1 173 ? -2.911  19.218  20.604  1.00 45.70  ? 145 PRO A N     1 
ATOM   1222 C  CA    . PRO A 1 173 ? -2.449  18.663  19.327  1.00 46.01  ? 145 PRO A CA    1 
ATOM   1223 C  C     . PRO A 1 173 ? -1.414  19.564  18.674  1.00 39.58  ? 145 PRO A C     1 
ATOM   1224 O  O     . PRO A 1 173 ? -1.502  20.787  18.733  1.00 37.43  ? 145 PRO A O     1 
ATOM   1225 C  CB    . PRO A 1 173 ? -3.723  18.575  18.474  1.00 41.64  ? 145 PRO A CB    1 
ATOM   1226 C  CG    . PRO A 1 173 ? -4.809  19.224  19.243  1.00 52.31  ? 145 PRO A CG    1 
ATOM   1227 C  CD    . PRO A 1 173 ? -4.343  19.565  20.615  1.00 46.37  ? 145 PRO A CD    1 
ATOM   1228 N  N     . LYS A 1 174 ? -0.443  18.941  18.014  1.00 37.71  ? 146 LYS A N     1 
ATOM   1229 C  CA    . LYS A 1 174 ? 0.627   19.654  17.343  1.00 38.88  ? 146 LYS A CA    1 
ATOM   1230 C  C     . LYS A 1 174 ? 0.970   18.901  16.070  1.00 39.47  ? 146 LYS A C     1 
ATOM   1231 O  O     . LYS A 1 174 ? 0.849   17.680  16.020  1.00 38.14  ? 146 LYS A O     1 
ATOM   1232 C  CB    . LYS A 1 174 ? 1.835   19.767  18.280  1.00 44.05  ? 146 LYS A CB    1 
ATOM   1233 C  CG    . LYS A 1 174 ? 2.945   20.665  17.848  1.00 53.09  ? 146 LYS A CG    1 
ATOM   1234 C  CD    . LYS A 1 174 ? 3.861   20.913  19.057  1.00 65.01  ? 146 LYS A CD    1 
ATOM   1235 C  CE    . LYS A 1 174 ? 4.701   19.676  19.407  1.00 76.77  ? 146 LYS A CE    1 
ATOM   1236 N  NZ    . LYS A 1 174 ? 6.155   19.968  19.643  1.00 74.65  ? 146 LYS A NZ    1 
ATOM   1237 N  N     . ALA A 1 175 ? 1.325   19.636  15.025  1.00 32.49  ? 147 ALA A N     1 
ATOM   1238 C  CA    . ALA A 1 175 ? 1.778   19.042  13.777  1.00 38.16  ? 147 ALA A CA    1 
ATOM   1239 C  C     . ALA A 1 175 ? 3.271   19.287  13.663  1.00 39.96  ? 147 ALA A C     1 
ATOM   1240 O  O     . ALA A 1 175 ? 3.734   20.406  13.881  1.00 35.57  ? 147 ALA A O     1 
ATOM   1241 C  CB    . ALA A 1 175 ? 1.042   19.624  12.569  1.00 41.33  ? 147 ALA A CB    1 
ATOM   1242 N  N     . VAL A 1 176 ? 4.034   18.243  13.368  1.00 34.81  ? 148 VAL A N     1 
ATOM   1243 C  CA    . VAL A 1 176 ? 5.489   18.369  13.338  1.00 34.84  ? 148 VAL A CA    1 
ATOM   1244 C  C     . VAL A 1 176 ? 6.032   17.541  12.181  1.00 40.72  ? 148 VAL A C     1 
ATOM   1245 O  O     . VAL A 1 176 ? 5.555   16.435  11.920  1.00 40.15  ? 148 VAL A O     1 
ATOM   1246 C  CB    . VAL A 1 176 ? 6.112   17.941  14.686  1.00 39.33  ? 148 VAL A CB    1 
ATOM   1247 C  CG1   . VAL A 1 176 ? 5.521   16.653  15.153  1.00 46.94  ? 148 VAL A CG1   1 
ATOM   1248 C  CG2   . VAL A 1 176 ? 7.607   17.762  14.554  1.00 50.38  ? 148 VAL A CG2   1 
ATOM   1249 N  N     . GLU A 1 177 ? 7.017   18.087  11.477  1.00 38.75  ? 149 GLU A N     1 
ATOM   1250 C  CA    . GLU A 1 177 ? 7.669   17.360  10.397  1.00 41.97  ? 149 GLU A CA    1 
ATOM   1251 C  C     . GLU A 1 177 ? 8.623   16.322  10.968  1.00 38.12  ? 149 GLU A C     1 
ATOM   1252 O  O     . GLU A 1 177 ? 9.448   16.628  11.832  1.00 38.73  ? 149 GLU A O     1 
ATOM   1253 C  CB    . GLU A 1 177 ? 8.433   18.299  9.470   1.00 48.92  ? 149 GLU A CB    1 
ATOM   1254 C  CG    . GLU A 1 177 ? 7.724   18.672  8.193   1.00 61.58  ? 149 GLU A CG    1 
ATOM   1255 C  CD    . GLU A 1 177 ? 8.735   18.955  7.080   1.00 69.45  ? 149 GLU A CD    1 
ATOM   1256 O  OE1   . GLU A 1 177 ? 9.927   19.161  7.404   1.00 68.33  ? 149 GLU A OE1   1 
ATOM   1257 O  OE2   . GLU A 1 177 ? 8.357   18.935  5.890   1.00 71.29  ? 149 GLU A OE2   1 
ATOM   1258 N  N     . LYS A 1 178 ? 8.485   15.090  10.502  1.00 36.91  ? 150 LYS A N     1 
ATOM   1259 C  CA    . LYS A 1 178 ? 9.370   14.010  10.889  1.00 29.42  ? 150 LYS A CA    1 
ATOM   1260 C  C     . LYS A 1 178 ? 9.955   13.351  9.652   1.00 30.76  ? 150 LYS A C     1 
ATOM   1261 O  O     . LYS A 1 178 ? 9.404   13.416  8.552   1.00 32.37  ? 150 LYS A O     1 
ATOM   1262 C  CB    . LYS A 1 178 ? 8.634   12.915  11.687  1.00 29.96  ? 150 LYS A CB    1 
ATOM   1263 C  CG    . LYS A 1 178 ? 7.931   13.387  12.958  1.00 31.13  ? 150 LYS A CG    1 
ATOM   1264 C  CD    . LYS A 1 178 ? 8.921   13.509  14.080  1.00 37.12  ? 150 LYS A CD    1 
ATOM   1265 C  CE    . LYS A 1 178 ? 8.201   13.631  15.414  1.00 46.09  ? 150 LYS A CE    1 
ATOM   1266 N  NZ    . LYS A 1 178 ? 9.174   14.046  16.448  1.00 46.49  ? 150 LYS A NZ    1 
ATOM   1267 N  N     . ILE A 1 179 ? 11.076  12.694  9.867   1.00 29.18  ? 151 ILE A N     1 
ATOM   1268 C  CA    A ILE A 1 179 ? 11.561  11.657  8.967   0.62 29.40  ? 151 ILE A CA    1 
ATOM   1269 C  CA    B ILE A 1 179 ? 11.538  11.665  8.958   0.38 29.41  ? 151 ILE A CA    1 
ATOM   1270 C  C     . ILE A 1 179 ? 10.896  10.362  9.388   1.00 29.14  ? 151 ILE A C     1 
ATOM   1271 O  O     . ILE A 1 179 ? 11.042  9.937   10.537  1.00 33.08  ? 151 ILE A O     1 
ATOM   1272 C  CB    A ILE A 1 179 ? 13.094  11.527  9.018   0.62 31.39  ? 151 ILE A CB    1 
ATOM   1273 C  CB    B ILE A 1 179 ? 13.063  11.572  8.968   0.38 31.35  ? 151 ILE A CB    1 
ATOM   1274 C  CG1   A ILE A 1 179 ? 13.758  12.846  8.646   0.62 33.23  ? 151 ILE A CG1   1 
ATOM   1275 C  CG1   B ILE A 1 179 ? 13.591  12.876  8.404   0.38 33.06  ? 151 ILE A CG1   1 
ATOM   1276 C  CG2   A ILE A 1 179 ? 13.579  10.415  8.081   0.62 29.62  ? 151 ILE A CG2   1 
ATOM   1277 C  CG2   B ILE A 1 179 ? 13.541  10.362  8.165   0.38 29.62  ? 151 ILE A CG2   1 
ATOM   1278 C  CD1   A ILE A 1 179 ? 13.367  13.279  7.263   0.62 29.51  ? 151 ILE A CD1   1 
ATOM   1279 C  CD1   B ILE A 1 179 ? 14.975  13.030  8.590   0.38 30.26  ? 151 ILE A CD1   1 
ATOM   1280 N  N     . VAL A 1 180 ? 10.187  9.737   8.465   1.00 27.27  ? 152 VAL A N     1 
ATOM   1281 C  CA    . VAL A 1 180 ? 9.493   8.499   8.732   1.00 27.10  ? 152 VAL A CA    1 
ATOM   1282 C  C     . VAL A 1 180 ? 10.298  7.352   8.135   1.00 25.89  ? 152 VAL A C     1 
ATOM   1283 O  O     . VAL A 1 180 ? 10.722  7.417   6.979   1.00 27.69  ? 152 VAL A O     1 
ATOM   1284 C  CB    . VAL A 1 180 ? 8.070   8.533   8.155   1.00 30.97  ? 152 VAL A CB    1 
ATOM   1285 C  CG1   . VAL A 1 180 ? 7.319   7.316   8.632   1.00 31.50  ? 152 VAL A CG1   1 
ATOM   1286 C  CG2   . VAL A 1 180 ? 7.379   9.814   8.584   1.00 35.80  ? 152 VAL A CG2   1 
ATOM   1287 N  N     . PHE A 1 181 ? 10.489  6.303   8.934   1.00 29.15  ? 153 PHE A N     1 
ATOM   1288 C  CA    . PHE A 1 181 ? 11.251  5.108   8.591   1.00 24.74  ? 153 PHE A CA    1 
ATOM   1289 C  C     . PHE A 1 181 ? 10.258  3.956   8.466   1.00 27.57  ? 153 PHE A C     1 
ATOM   1290 O  O     . PHE A 1 181 ? 9.425   3.760   9.357   1.00 26.64  ? 153 PHE A O     1 
ATOM   1291 C  CB    . PHE A 1 181 ? 12.292  4.856   9.695   1.00 27.32  ? 153 PHE A CB    1 
ATOM   1292 C  CG    . PHE A 1 181 ? 12.992  3.514   9.642   1.00 27.83  ? 153 PHE A CG    1 
ATOM   1293 C  CD1   . PHE A 1 181 ? 12.323  2.347   10.002  1.00 25.09  ? 153 PHE A CD1   1 
ATOM   1294 C  CD2   . PHE A 1 181 ? 14.357  3.441   9.347   1.00 27.90  ? 153 PHE A CD2   1 
ATOM   1295 C  CE1   . PHE A 1 181 ? 12.984  1.109   9.990   1.00 33.23  ? 153 PHE A CE1   1 
ATOM   1296 C  CE2   . PHE A 1 181 ? 15.020  2.220   9.332   1.00 28.35  ? 153 PHE A CE2   1 
ATOM   1297 C  CZ    . PHE A 1 181 ? 14.332  1.048   9.663   1.00 30.37  ? 153 PHE A CZ    1 
ATOM   1298 N  N     . PHE A 1 182 ? 10.340  3.197   7.368   1.00 23.89  ? 154 PHE A N     1 
ATOM   1299 C  CA    . PHE A 1 182 ? 9.568   1.961   7.219   1.00 25.34  ? 154 PHE A CA    1 
ATOM   1300 C  C     . PHE A 1 182 ? 10.523  0.874   6.774   1.00 27.63  ? 154 PHE A C     1 
ATOM   1301 O  O     . PHE A 1 182 ? 11.269  1.062   5.819   1.00 27.97  ? 154 PHE A O     1 
ATOM   1302 C  CB    . PHE A 1 182 ? 8.455   2.054   6.165   1.00 26.54  ? 154 PHE A CB    1 
ATOM   1303 C  CG    . PHE A 1 182 ? 7.339   2.992   6.518   1.00 28.75  ? 154 PHE A CG    1 
ATOM   1304 C  CD1   . PHE A 1 182 ? 6.334   2.600   7.359   1.00 27.94  ? 154 PHE A CD1   1 
ATOM   1305 C  CD2   . PHE A 1 182 ? 7.299   4.262   5.965   1.00 34.74  ? 154 PHE A CD2   1 
ATOM   1306 C  CE1   . PHE A 1 182 ? 5.292   3.467   7.662   1.00 35.25  ? 154 PHE A CE1   1 
ATOM   1307 C  CE2   . PHE A 1 182 ? 6.250   5.123   6.256   1.00 36.13  ? 154 PHE A CE2   1 
ATOM   1308 C  CZ    . PHE A 1 182 ? 5.262   4.730   7.085   1.00 28.26  ? 154 PHE A CZ    1 
ATOM   1309 N  N     . SER A 1 183 ? 10.512  -0.250  7.453   1.00 26.80  ? 155 SER A N     1 
ATOM   1310 C  CA    . SER A 1 183 ? 11.283  -1.380  6.977   1.00 23.93  ? 155 SER A CA    1 
ATOM   1311 C  C     . SER A 1 183 ? 10.398  -2.606  7.005   1.00 30.04  ? 155 SER A C     1 
ATOM   1312 O  O     . SER A 1 183 ? 9.466   -2.693  7.805   1.00 34.10  ? 155 SER A O     1 
ATOM   1313 C  CB    . SER A 1 183 ? 12.543  -1.614  7.810   1.00 28.84  ? 155 SER A CB    1 
ATOM   1314 O  OG    . SER A 1 183 ? 12.196  -2.022  9.124   1.00 38.15  ? 155 SER A OG    1 
ATOM   1315 N  N     . ASP A 1 184 ? 10.680  -3.551  6.121   1.00 25.60  ? 156 ASP A N     1 
ATOM   1316 C  CA    . ASP A 1 184 ? 9.865   -4.751  6.089   1.00 25.99  ? 156 ASP A CA    1 
ATOM   1317 C  C     . ASP A 1 184 ? 10.764  -5.954  5.823   1.00 28.14  ? 156 ASP A C     1 
ATOM   1318 O  O     . ASP A 1 184 ? 11.981  -5.824  5.610   1.00 30.46  ? 156 ASP A O     1 
ATOM   1319 C  CB    . ASP A 1 184 ? 8.740   -4.612  5.054   1.00 29.97  ? 156 ASP A CB    1 
ATOM   1320 C  CG    . ASP A 1 184 ? 9.210   -4.870  3.627   1.00 33.74  ? 156 ASP A CG    1 
ATOM   1321 O  OD1   . ASP A 1 184 ? 10.352  -4.482  3.278   1.00 42.19  ? 156 ASP A OD1   1 
ATOM   1322 O  OD2   . ASP A 1 184 ? 8.424   -5.463  2.867   1.00 40.34  ? 156 ASP A OD2   1 
ATOM   1323 N  N     . ILE A 1 185 ? 10.155  -7.129  5.876   1.00 28.11  ? 157 ILE A N     1 
ATOM   1324 C  CA    . ILE A 1 185 ? 10.843  -8.397  5.671   1.00 29.16  ? 157 ILE A CA    1 
ATOM   1325 C  C     . ILE A 1 185 ? 10.560  -8.853  4.250   1.00 30.93  ? 157 ILE A C     1 
ATOM   1326 O  O     . ILE A 1 185 ? 9.400   -8.944  3.846   1.00 31.21  ? 157 ILE A O     1 
ATOM   1327 C  CB    . ILE A 1 185 ? 10.373  -9.444  6.692   1.00 30.80  ? 157 ILE A CB    1 
ATOM   1328 C  CG1   . ILE A 1 185 ? 10.810  -9.055  8.105   1.00 26.29  ? 157 ILE A CG1   1 
ATOM   1329 C  CG2   . ILE A 1 185 ? 10.939  -10.825 6.334   1.00 31.68  ? 157 ILE A CG2   1 
ATOM   1330 C  CD1   . ILE A 1 185 ? 10.271  -9.998  9.177   1.00 30.76  ? 157 ILE A CD1   1 
ATOM   1331 N  N     . VAL A 1 186 ? 11.615  -9.127  3.482   1.00 27.27  ? 158 VAL A N     1 
ATOM   1332 C  CA    . VAL A 1 186 ? 11.434  -9.561  2.102   1.00 28.23  ? 158 VAL A CA    1 
ATOM   1333 C  C     . VAL A 1 186 ? 10.790  -10.937 2.093   1.00 31.36  ? 158 VAL A C     1 
ATOM   1334 O  O     . VAL A 1 186 ? 11.232  -11.852 2.799   1.00 28.76  ? 158 VAL A O     1 
ATOM   1335 C  CB    . VAL A 1 186 ? 12.771  -9.567  1.347   1.00 34.32  ? 158 VAL A CB    1 
ATOM   1336 C  CG1   . VAL A 1 186 ? 12.582  -10.174 -0.047  1.00 35.54  ? 158 VAL A CG1   1 
ATOM   1337 C  CG2   . VAL A 1 186 ? 13.313  -8.154  1.269   1.00 37.02  ? 158 VAL A CG2   1 
ATOM   1338 N  N     . SER A 1 187 ? 9.696   -11.063 1.346   1.00 31.15  ? 159 SER A N     1 
ATOM   1339 C  CA    . SER A 1 187 ? 9.026   -12.346 1.138   1.00 37.45  ? 159 SER A CA    1 
ATOM   1340 C  C     . SER A 1 187 ? 8.567   -12.964 2.456   1.00 32.76  ? 159 SER A C     1 
ATOM   1341 O  O     . SER A 1 187 ? 8.640   -14.178 2.657   1.00 34.72  ? 159 SER A O     1 
ATOM   1342 C  CB    . SER A 1 187 ? 9.938   -13.303 0.357   1.00 38.27  ? 159 SER A CB    1 
ATOM   1343 O  OG    . SER A 1 187 ? 9.166   -14.225 -0.388  1.00 55.20  ? 159 SER A OG    1 
ATOM   1344 N  N     . PHE A 1 188 ? 8.069   -12.123 3.365   1.00 31.34  ? 160 PHE A N     1 
ATOM   1345 C  CA    . PHE A 1 188 ? 7.594   -12.625 4.644   1.00 29.79  ? 160 PHE A CA    1 
ATOM   1346 C  C     . PHE A 1 188 ? 6.606   -13.778 4.482   1.00 33.39  ? 160 PHE A C     1 
ATOM   1347 O  O     . PHE A 1 188 ? 6.565   -14.690 5.312   1.00 30.99  ? 160 PHE A O     1 
ATOM   1348 C  CB    . PHE A 1 188 ? 6.918   -11.513 5.438   1.00 33.23  ? 160 PHE A CB    1 
ATOM   1349 C  CG    . PHE A 1 188 ? 6.263   -12.009 6.682   1.00 37.17  ? 160 PHE A CG    1 
ATOM   1350 C  CD1   . PHE A 1 188 ? 7.022   -12.252 7.814   1.00 39.98  ? 160 PHE A CD1   1 
ATOM   1351 C  CD2   . PHE A 1 188 ? 4.910   -12.320 6.697   1.00 39.38  ? 160 PHE A CD2   1 
ATOM   1352 C  CE1   . PHE A 1 188 ? 6.426   -12.733 8.957   1.00 44.82  ? 160 PHE A CE1   1 
ATOM   1353 C  CE2   . PHE A 1 188 ? 4.314   -12.821 7.835   1.00 36.88  ? 160 PHE A CE2   1 
ATOM   1354 C  CZ    . PHE A 1 188 ? 5.074   -13.009 8.967   1.00 39.93  ? 160 PHE A CZ    1 
ATOM   1355 N  N     . SER A 1 189 ? 5.755   -13.725 3.455   1.00 31.03  ? 161 SER A N     1 
ATOM   1356 C  CA    . SER A 1 189 ? 4.744   -14.769 3.309   1.00 37.75  ? 161 SER A CA    1 
ATOM   1357 C  C     . SER A 1 189 ? 5.373   -16.149 3.146   1.00 39.19  ? 161 SER A C     1 
ATOM   1358 O  O     . SER A 1 189 ? 4.796   -17.147 3.586   1.00 38.37  ? 161 SER A O     1 
ATOM   1359 C  CB    . SER A 1 189 ? 3.829   -14.446 2.123   1.00 40.71  ? 161 SER A CB    1 
ATOM   1360 O  OG    . SER A 1 189 ? 4.609   -14.179 0.970   1.00 53.76  ? 161 SER A OG    1 
ATOM   1361 N  N     . THR A 1 190 ? 6.549   -16.229 2.522   1.00 36.93  ? 162 THR A N     1 
ATOM   1362 C  CA    . THR A 1 190 ? 7.194   -17.523 2.331   1.00 34.74  ? 162 THR A CA    1 
ATOM   1363 C  C     . THR A 1 190 ? 7.582   -18.144 3.664   1.00 35.35  ? 162 THR A C     1 
ATOM   1364 O  O     . THR A 1 190 ? 7.470   -19.362 3.847   1.00 39.86  ? 162 THR A O     1 
ATOM   1365 C  CB    . THR A 1 190 ? 8.422   -17.371 1.438   1.00 38.98  ? 162 THR A CB    1 
ATOM   1366 O  OG1   . THR A 1 190 ? 8.043   -16.728 0.222   1.00 45.02  ? 162 THR A OG1   1 
ATOM   1367 C  CG2   . THR A 1 190 ? 9.012   -18.739 1.114   1.00 45.14  ? 162 THR A CG2   1 
ATOM   1368 N  N     . PHE A 1 191 ? 8.041   -17.326 4.615   1.00 33.98  ? 163 PHE A N     1 
ATOM   1369 C  CA    . PHE A 1 191 ? 8.315   -17.841 5.955   1.00 33.82  ? 163 PHE A CA    1 
ATOM   1370 C  C     . PHE A 1 191 ? 7.057   -18.432 6.569   1.00 41.33  ? 163 PHE A C     1 
ATOM   1371 O  O     . PHE A 1 191 ? 7.073   -19.541 7.115   1.00 36.13  ? 163 PHE A O     1 
ATOM   1372 C  CB    . PHE A 1 191 ? 8.834   -16.727 6.863   1.00 31.93  ? 163 PHE A CB    1 
ATOM   1373 C  CG    . PHE A 1 191 ? 10.227  -16.283 6.553   1.00 33.92  ? 163 PHE A CG    1 
ATOM   1374 C  CD1   . PHE A 1 191 ? 10.446  -15.259 5.658   1.00 31.67  ? 163 PHE A CD1   1 
ATOM   1375 C  CD2   . PHE A 1 191 ? 11.322  -16.863 7.200   1.00 34.33  ? 163 PHE A CD2   1 
ATOM   1376 C  CE1   . PHE A 1 191 ? 11.737  -14.821 5.386   1.00 38.88  ? 163 PHE A CE1   1 
ATOM   1377 C  CE2   . PHE A 1 191 ? 12.601  -16.429 6.936   1.00 33.13  ? 163 PHE A CE2   1 
ATOM   1378 C  CZ    . PHE A 1 191 ? 12.812  -15.410 6.025   1.00 38.55  ? 163 PHE A CZ    1 
ATOM   1379 N  N     . ALA A 1 192 ? 5.960   -17.673 6.522   1.00 36.37  ? 164 ALA A N     1 
ATOM   1380 C  CA    . ALA A 1 192 ? 4.728   -18.109 7.167   1.00 42.94  ? 164 ALA A CA    1 
ATOM   1381 C  C     . ALA A 1 192 ? 4.166   -19.360 6.502   1.00 38.31  ? 164 ALA A C     1 
ATOM   1382 O  O     . ALA A 1 192 ? 3.503   -20.172 7.154   1.00 45.51  ? 164 ALA A O     1 
ATOM   1383 C  CB    . ALA A 1 192 ? 3.708   -16.962 7.152   1.00 40.21  ? 164 ALA A CB    1 
ATOM   1384 N  N     . GLU A 1 193 ? 4.443   -19.537 5.212   1.00 43.89  ? 165 GLU A N     1 
ATOM   1385 C  CA    . GLU A 1 193 ? 3.952   -20.688 4.471   1.00 41.28  ? 165 GLU A CA    1 
ATOM   1386 C  C     . GLU A 1 193 ? 4.774   -21.937 4.741   1.00 44.41  ? 165 GLU A C     1 
ATOM   1387 O  O     . GLU A 1 193 ? 4.228   -23.043 4.736   1.00 49.14  ? 165 GLU A O     1 
ATOM   1388 C  CB    . GLU A 1 193 ? 3.970   -20.398 2.968   1.00 53.74  ? 165 GLU A CB    1 
ATOM   1389 C  CG    . GLU A 1 193 ? 2.653   -19.882 2.392   1.00 62.19  ? 165 GLU A CG    1 
ATOM   1390 C  CD    . GLU A 1 193 ? 2.856   -18.936 1.214   1.00 72.25  ? 165 GLU A CD    1 
ATOM   1391 O  OE1   . GLU A 1 193 ? 1.992   -18.053 1.008   1.00 83.62  ? 165 GLU A OE1   1 
ATOM   1392 O  OE2   . GLU A 1 193 ? 3.873   -19.081 0.494   1.00 68.35  ? 165 GLU A OE2   1 
ATOM   1393 N  N     . LYS A 1 194 ? 6.072   -21.789 4.981   1.00 38.81  ? 166 LYS A N     1 
ATOM   1394 C  CA    . LYS A 1 194 ? 6.984   -22.917 4.957   1.00 41.47  ? 166 LYS A CA    1 
ATOM   1395 C  C     . LYS A 1 194 ? 7.490   -23.335 6.328   1.00 37.88  ? 166 LYS A C     1 
ATOM   1396 O  O     . LYS A 1 194 ? 8.080   -24.414 6.447   1.00 47.46  ? 166 LYS A O     1 
ATOM   1397 C  CB    . LYS A 1 194 ? 8.173   -22.592 4.043   1.00 41.05  ? 166 LYS A CB    1 
ATOM   1398 C  CG    . LYS A 1 194 ? 7.748   -22.426 2.589   1.00 46.42  ? 166 LYS A CG    1 
ATOM   1399 C  CD    . LYS A 1 194 ? 8.666   -23.189 1.655   1.00 56.75  ? 166 LYS A CD    1 
ATOM   1400 C  CE    . LYS A 1 194 ? 8.370   -22.889 0.182   1.00 62.71  ? 166 LYS A CE    1 
ATOM   1401 N  NZ    . LYS A 1 194 ? 6.975   -23.269 -0.203  1.00 67.68  ? 166 LYS A NZ    1 
ATOM   1402 N  N     . LEU A 1 195 ? 7.288   -22.526 7.358   1.00 39.00  ? 167 LEU A N     1 
ATOM   1403 C  CA    . LEU A 1 195 ? 7.849   -22.845 8.666   1.00 34.50  ? 167 LEU A CA    1 
ATOM   1404 C  C     . LEU A 1 195 ? 6.749   -22.963 9.705   1.00 36.70  ? 167 LEU A C     1 
ATOM   1405 O  O     . LEU A 1 195 ? 5.697   -22.338 9.569   1.00 38.10  ? 167 LEU A O     1 
ATOM   1406 C  CB    . LEU A 1 195 ? 8.845   -21.778 9.138   1.00 40.11  ? 167 LEU A CB    1 
ATOM   1407 C  CG    . LEU A 1 195 ? 10.085  -21.444 8.310   1.00 40.84  ? 167 LEU A CG    1 
ATOM   1408 C  CD1   . LEU A 1 195 ? 10.814  -20.301 8.948   1.00 36.28  ? 167 LEU A CD1   1 
ATOM   1409 C  CD2   . LEU A 1 195 ? 10.993  -22.655 8.250   1.00 39.00  ? 167 LEU A CD2   1 
ATOM   1410 N  N     . PRO A 1 196 ? 6.981   -23.731 10.768  1.00 38.16  ? 168 PRO A N     1 
ATOM   1411 C  CA    . PRO A 1 196 ? 6.040   -23.741 11.893  1.00 42.85  ? 168 PRO A CA    1 
ATOM   1412 C  C     . PRO A 1 196 ? 5.954   -22.362 12.533  1.00 47.28  ? 168 PRO A C     1 
ATOM   1413 O  O     . PRO A 1 196 ? 6.908   -21.577 12.499  1.00 39.57  ? 168 PRO A O     1 
ATOM   1414 C  CB    . PRO A 1 196 ? 6.647   -24.755 12.869  1.00 44.35  ? 168 PRO A CB    1 
ATOM   1415 C  CG    . PRO A 1 196 ? 7.960   -25.115 12.348  1.00 43.90  ? 168 PRO A CG    1 
ATOM   1416 C  CD    . PRO A 1 196 ? 8.116   -24.646 10.954  1.00 40.05  ? 168 PRO A CD    1 
ATOM   1417 N  N     . VAL A 1 197 ? 4.806   -22.085 13.162  1.00 39.00  ? 169 VAL A N     1 
ATOM   1418 C  CA    . VAL A 1 197 ? 4.558   -20.728 13.644  1.00 43.78  ? 169 VAL A CA    1 
ATOM   1419 C  C     . VAL A 1 197 ? 5.624   -20.291 14.653  1.00 39.16  ? 169 VAL A C     1 
ATOM   1420 O  O     . VAL A 1 197 ? 6.050   -19.128 14.649  1.00 36.71  ? 169 VAL A O     1 
ATOM   1421 C  CB    . VAL A 1 197 ? 3.126   -20.599 14.205  1.00 44.90  ? 169 VAL A CB    1 
ATOM   1422 C  CG1   . VAL A 1 197 ? 2.903   -21.508 15.385  1.00 42.73  ? 169 VAL A CG1   1 
ATOM   1423 C  CG2   . VAL A 1 197 ? 2.845   -19.155 14.587  1.00 43.10  ? 169 VAL A CG2   1 
ATOM   1424 N  N     . GLU A 1 198 ? 6.105   -21.208 15.508  1.00 37.30  ? 170 GLU A N     1 
ATOM   1425 C  CA    . GLU A 1 198 ? 7.113   -20.812 16.496  1.00 41.05  ? 170 GLU A CA    1 
ATOM   1426 C  C     . GLU A 1 198 ? 8.384   -20.314 15.824  1.00 39.29  ? 170 GLU A C     1 
ATOM   1427 O  O     . GLU A 1 198 ? 9.046   -19.398 16.331  1.00 40.25  ? 170 GLU A O     1 
ATOM   1428 C  CB    . GLU A 1 198 ? 7.463   -21.953 17.454  1.00 45.78  ? 170 GLU A CB    1 
ATOM   1429 C  CG    . GLU A 1 198 ? 6.338   -22.878 17.829  1.00 55.96  ? 170 GLU A CG    1 
ATOM   1430 C  CD    . GLU A 1 198 ? 6.078   -23.914 16.762  1.00 57.72  ? 170 GLU A CD    1 
ATOM   1431 O  OE1   . GLU A 1 198 ? 4.950   -23.941 16.227  1.00 58.01  ? 170 GLU A OE1   1 
ATOM   1432 O  OE2   . GLU A 1 198 ? 7.015   -24.679 16.439  1.00 69.16  ? 170 GLU A OE2   1 
ATOM   1433 N  N     . GLU A 1 199 ? 8.746   -20.912 14.689  1.00 39.52  ? 171 GLU A N     1 
ATOM   1434 C  CA    . GLU A 1 199 ? 9.932   -20.472 13.964  1.00 40.95  ? 171 GLU A CA    1 
ATOM   1435 C  C     . GLU A 1 199 ? 9.692   -19.141 13.260  1.00 39.24  ? 171 GLU A C     1 
ATOM   1436 O  O     . GLU A 1 199 ? 10.610  -18.319 13.157  1.00 37.22  ? 171 GLU A O     1 
ATOM   1437 C  CB    . GLU A 1 199 ? 10.350  -21.541 12.952  1.00 41.97  ? 171 GLU A CB    1 
ATOM   1438 C  CG    . GLU A 1 199 ? 10.871  -22.835 13.586  1.00 52.87  ? 171 GLU A CG    1 
ATOM   1439 C  CD    . GLU A 1 199 ? 12.163  -22.618 14.366  1.00 70.01  ? 171 GLU A CD    1 
ATOM   1440 O  OE1   . GLU A 1 199 ? 13.125  -22.045 13.793  1.00 69.18  ? 171 GLU A OE1   1 
ATOM   1441 O  OE2   . GLU A 1 199 ? 12.214  -23.001 15.554  1.00 82.61  ? 171 GLU A OE2   1 
ATOM   1442 N  N     . VAL A 1 200 ? 8.480   -18.927 12.731  1.00 32.69  ? 172 VAL A N     1 
ATOM   1443 C  CA    . VAL A 1 200 ? 8.162   -17.627 12.146  1.00 33.69  ? 172 VAL A CA    1 
ATOM   1444 C  C     . VAL A 1 200 ? 8.306   -16.538 13.198  1.00 32.88  ? 172 VAL A C     1 
ATOM   1445 O  O     . VAL A 1 200 ? 8.873   -15.471 12.941  1.00 29.29  ? 172 VAL A O     1 
ATOM   1446 C  CB    . VAL A 1 200 ? 6.744   -17.634 11.533  1.00 34.86  ? 172 VAL A CB    1 
ATOM   1447 C  CG1   . VAL A 1 200 ? 6.417   -16.261 10.949  1.00 36.25  ? 172 VAL A CG1   1 
ATOM   1448 C  CG2   . VAL A 1 200 ? 6.633   -18.687 10.453  1.00 33.19  ? 172 VAL A CG2   1 
ATOM   1449 N  N     . VAL A 1 201 ? 7.801   -16.797 14.404  1.00 29.60  ? 173 VAL A N     1 
ATOM   1450 C  CA    . VAL A 1 201 ? 7.856   -15.812 15.474  1.00 34.03  ? 173 VAL A CA    1 
ATOM   1451 C  C     . VAL A 1 201 ? 9.298   -15.574 15.894  1.00 34.51  ? 173 VAL A C     1 
ATOM   1452 O  O     . VAL A 1 201 ? 9.692   -14.446 16.204  1.00 33.28  ? 173 VAL A O     1 
ATOM   1453 C  CB    . VAL A 1 201 ? 6.980   -16.274 16.656  1.00 34.35  ? 173 VAL A CB    1 
ATOM   1454 C  CG1   . VAL A 1 201 ? 7.295   -15.484 17.931  1.00 34.09  ? 173 VAL A CG1   1 
ATOM   1455 C  CG2   . VAL A 1 201 ? 5.508   -16.159 16.303  1.00 38.34  ? 173 VAL A CG2   1 
ATOM   1456 N  N     . SER A 1 202 ? 10.113  -16.630 15.914  1.00 34.08  ? 174 SER A N     1 
ATOM   1457 C  CA    . SER A 1 202 ? 11.519  -16.442 16.233  1.00 34.16  ? 174 SER A CA    1 
ATOM   1458 C  C     . SER A 1 202 ? 12.186  -15.554 15.188  1.00 37.53  ? 174 SER A C     1 
ATOM   1459 O  O     . SER A 1 202 ? 12.970  -14.660 15.530  1.00 33.83  ? 174 SER A O     1 
ATOM   1460 C  CB    . SER A 1 202 ? 12.215  -17.803 16.338  1.00 35.04  ? 174 SER A CB    1 
ATOM   1461 O  OG    . SER A 1 202 ? 13.430  -17.670 17.022  1.00 53.11  ? 174 SER A OG    1 
ATOM   1462 N  N     . VAL A 1 203 ? 11.847  -15.749 13.910  1.00 30.73  ? 175 VAL A N     1 
ATOM   1463 C  CA    . VAL A 1 203 ? 12.434  -14.912 12.870  1.00 32.01  ? 175 VAL A CA    1 
ATOM   1464 C  C     . VAL A 1 203 ? 11.977  -13.464 13.020  1.00 31.98  ? 175 VAL A C     1 
ATOM   1465 O  O     . VAL A 1 203 ? 12.798  -12.541 12.995  1.00 30.11  ? 175 VAL A O     1 
ATOM   1466 C  CB    . VAL A 1 203 ? 12.098  -15.466 11.478  1.00 34.08  ? 175 VAL A CB    1 
ATOM   1467 C  CG1   . VAL A 1 203 ? 12.482  -14.461 10.398  1.00 36.53  ? 175 VAL A CG1   1 
ATOM   1468 C  CG2   . VAL A 1 203 ? 12.804  -16.796 11.269  1.00 35.01  ? 175 VAL A CG2   1 
ATOM   1469 N  N     . VAL A 1 204 ? 10.665  -13.235 13.178  1.00 28.04  ? 176 VAL A N     1 
ATOM   1470 C  CA    . VAL A 1 204 ? 10.190  -11.851 13.225  1.00 30.74  ? 176 VAL A CA    1 
ATOM   1471 C  C     . VAL A 1 204 ? 10.726  -11.152 14.465  1.00 26.04  ? 176 VAL A C     1 
ATOM   1472 O  O     . VAL A 1 204 ? 11.080  -9.968  14.419  1.00 31.59  ? 176 VAL A O     1 
ATOM   1473 C  CB    . VAL A 1 204 ? 8.644   -11.770 13.154  1.00 34.30  ? 176 VAL A CB    1 
ATOM   1474 C  CG1   . VAL A 1 204 ? 8.128   -12.493 11.945  1.00 36.09  ? 176 VAL A CG1   1 
ATOM   1475 C  CG2   . VAL A 1 204 ? 7.973   -12.271 14.417  1.00 40.14  ? 176 VAL A CG2   1 
ATOM   1476 N  N     . ASN A 1 205 ? 10.827  -11.873 15.584  1.00 28.26  ? 177 ASN A N     1 
ATOM   1477 C  CA    . ASN A 1 205 ? 11.357  -11.268 16.808  1.00 29.76  ? 177 ASN A CA    1 
ATOM   1478 C  C     . ASN A 1 205 ? 12.836  -10.892 16.674  1.00 27.75  ? 177 ASN A C     1 
ATOM   1479 O  O     . ASN A 1 205 ? 13.259  -9.851  17.185  1.00 30.42  ? 177 ASN A O     1 
ATOM   1480 C  CB    . ASN A 1 205 ? 11.141  -12.219 17.984  1.00 32.19  ? 177 ASN A CB    1 
ATOM   1481 C  CG    . ASN A 1 205 ? 9.711   -12.141 18.539  1.00 38.25  ? 177 ASN A CG    1 
ATOM   1482 O  OD1   . ASN A 1 205 ? 8.850   -11.438 17.995  1.00 34.05  ? 177 ASN A OD1   1 
ATOM   1483 N  ND2   . ASN A 1 205 ? 9.450   -12.890 19.603  1.00 35.06  ? 177 ASN A ND2   1 
ATOM   1484 N  N     . SER A 1 206 ? 13.652  -11.740 16.041  1.00 30.22  ? 178 SER A N     1 
ATOM   1485 C  CA    . SER A 1 206 ? 15.026  -11.328 15.746  1.00 29.57  ? 178 SER A CA    1 
ATOM   1486 C  C     . SER A 1 206 ? 15.040  -10.049 14.920  1.00 28.03  ? 178 SER A C     1 
ATOM   1487 O  O     . SER A 1 206 ? 15.788  -9.112  15.207  1.00 28.42  ? 178 SER A O     1 
ATOM   1488 C  CB    . SER A 1 206 ? 15.774  -12.437 14.999  1.00 32.96  ? 178 SER A CB    1 
ATOM   1489 O  OG    . SER A 1 206 ? 15.817  -13.618 15.773  1.00 33.88  ? 178 SER A OG    1 
ATOM   1490 N  N     . TYR A 1 207 ? 14.229  -10.014 13.868  1.00 26.80  ? 179 TYR A N     1 
ATOM   1491 C  CA    . TYR A 1 207 ? 14.129  -8.825  13.026  1.00 26.74  ? 179 TYR A CA    1 
ATOM   1492 C  C     . TYR A 1 207 ? 13.744  -7.595  13.840  1.00 30.57  ? 179 TYR A C     1 
ATOM   1493 O  O     . TYR A 1 207 ? 14.419  -6.561  13.804  1.00 25.68  ? 179 TYR A O     1 
ATOM   1494 C  CB    . TYR A 1 207 ? 13.095  -9.079  11.944  1.00 31.37  ? 179 TYR A CB    1 
ATOM   1495 C  CG    . TYR A 1 207 ? 12.931  -7.907  11.059  1.00 31.92  ? 179 TYR A CG    1 
ATOM   1496 C  CD1   . TYR A 1 207 ? 14.012  -7.432  10.344  1.00 34.14  ? 179 TYR A CD1   1 
ATOM   1497 C  CD2   . TYR A 1 207 ? 11.707  -7.245  10.961  1.00 34.25  ? 179 TYR A CD2   1 
ATOM   1498 C  CE1   . TYR A 1 207 ? 13.891  -6.351  9.517   1.00 41.74  ? 179 TYR A CE1   1 
ATOM   1499 C  CE2   . TYR A 1 207 ? 11.579  -6.134  10.126  1.00 35.81  ? 179 TYR A CE2   1 
ATOM   1500 C  CZ    . TYR A 1 207 ? 12.688  -5.704  9.419   1.00 29.11  ? 179 TYR A CZ    1 
ATOM   1501 O  OH    . TYR A 1 207 ? 12.626  -4.615  8.567   1.00 41.26  ? 179 TYR A OH    1 
ATOM   1502 N  N     . PHE A 1 208 ? 12.634  -7.685  14.569  1.00 24.77  ? 180 PHE A N     1 
ATOM   1503 C  CA    . PHE A 1 208 ? 12.165  -6.528  15.326  1.00 29.48  ? 180 PHE A CA    1 
ATOM   1504 C  C     . PHE A 1 208 ? 13.200  -6.103  16.368  1.00 30.25  ? 180 PHE A C     1 
ATOM   1505 O  O     . PHE A 1 208 ? 13.392  -4.904  16.614  1.00 29.56  ? 180 PHE A O     1 
ATOM   1506 C  CB    . PHE A 1 208 ? 10.821  -6.875  15.979  1.00 27.88  ? 180 PHE A CB    1 
ATOM   1507 C  CG    . PHE A 1 208 ? 9.628   -6.840  15.030  1.00 28.12  ? 180 PHE A CG    1 
ATOM   1508 C  CD1   . PHE A 1 208 ? 9.681   -6.157  13.829  1.00 31.26  ? 180 PHE A CD1   1 
ATOM   1509 C  CD2   . PHE A 1 208 ? 8.477   -7.538  15.330  1.00 31.58  ? 180 PHE A CD2   1 
ATOM   1510 C  CE1   . PHE A 1 208 ? 8.592   -6.116  12.974  1.00 35.74  ? 180 PHE A CE1   1 
ATOM   1511 C  CE2   . PHE A 1 208 ? 7.373   -7.504  14.476  1.00 32.35  ? 180 PHE A CE2   1 
ATOM   1512 C  CZ    . PHE A 1 208 ? 7.425   -6.793  13.302  1.00 29.05  ? 180 PHE A CZ    1 
ATOM   1513 N  N     . SER A 1 209 ? 13.886  -7.068  16.986  1.00 28.12  ? 181 SER A N     1 
ATOM   1514 C  CA    . SER A 1 209 ? 14.891  -6.714  17.988  1.00 28.32  ? 181 SER A CA    1 
ATOM   1515 C  C     . SER A 1 209 ? 16.036  -5.927  17.368  1.00 31.53  ? 181 SER A C     1 
ATOM   1516 O  O     . SER A 1 209 ? 16.509  -4.950  17.955  1.00 30.98  ? 181 SER A O     1 
ATOM   1517 C  CB    . SER A 1 209 ? 15.439  -7.969  18.669  1.00 34.10  ? 181 SER A CB    1 
ATOM   1518 O  OG    . SER A 1 209 ? 14.396  -8.711  19.270  1.00 50.13  ? 181 SER A OG    1 
ATOM   1519 N  N     . VAL A 1 210 ? 16.513  -6.355  16.195  1.00 26.80  ? 182 VAL A N     1 
ATOM   1520 C  CA    . VAL A 1 210 ? 17.623  -5.654  15.530  1.00 26.23  ? 182 VAL A CA    1 
ATOM   1521 C  C     . VAL A 1 210 ? 17.206  -4.231  15.178  1.00 29.85  ? 182 VAL A C     1 
ATOM   1522 O  O     . VAL A 1 210 ? 17.931  -3.256  15.433  1.00 29.71  ? 182 VAL A O     1 
ATOM   1523 C  CB    . VAL A 1 210 ? 18.066  -6.425  14.270  1.00 28.98  ? 182 VAL A CB    1 
ATOM   1524 C  CG1   . VAL A 1 210 ? 18.992  -5.564  13.400  1.00 36.85  ? 182 VAL A CG1   1 
ATOM   1525 C  CG2   . VAL A 1 210 ? 18.796  -7.683  14.625  1.00 32.37  ? 182 VAL A CG2   1 
ATOM   1526 N  N     . CYS A 1 211 ? 16.028  -4.101  14.568  1.00 27.64  ? 183 CYS A N     1 
ATOM   1527 C  CA    . CYS A 1 211 ? 15.566  -2.803  14.106  1.00 28.59  ? 183 CYS A CA    1 
ATOM   1528 C  C     . CYS A 1 211 ? 15.363  -1.854  15.273  1.00 27.92  ? 183 CYS A C     1 
ATOM   1529 O  O     . CYS A 1 211 ? 15.812  -0.705  15.238  1.00 31.12  ? 183 CYS A O     1 
ATOM   1530 C  CB    . CYS A 1 211 ? 14.258  -2.968  13.312  1.00 30.05  ? 183 CYS A CB    1 
ATOM   1531 S  SG    . CYS A 1 211 ? 14.498  -3.738  11.685  1.00 33.15  ? 183 CYS A SG    1 
ATOM   1532 N  N     . THR A 1 212 ? 14.683  -2.314  16.320  1.00 27.96  ? 184 THR A N     1 
ATOM   1533 C  CA    A THR A 1 212 ? 14.337  -1.386  17.389  0.30 35.36  ? 184 THR A CA    1 
ATOM   1534 C  CA    B THR A 1 212 ? 14.331  -1.425  17.422  0.70 35.48  ? 184 THR A CA    1 
ATOM   1535 C  C     . THR A 1 212 ? 15.572  -0.951  18.168  1.00 35.04  ? 184 THR A C     1 
ATOM   1536 O  O     . THR A 1 212 ? 15.689  0.228   18.519  1.00 31.53  ? 184 THR A O     1 
ATOM   1537 C  CB    A THR A 1 212 ? 13.288  -1.992  18.321  0.30 35.36  ? 184 THR A CB    1 
ATOM   1538 C  CB    B THR A 1 212 ? 13.367  -2.146  18.371  0.70 35.28  ? 184 THR A CB    1 
ATOM   1539 O  OG1   A THR A 1 212 ? 12.811  -0.976  19.212  0.30 43.56  ? 184 THR A OG1   1 
ATOM   1540 O  OG1   B THR A 1 212 ? 12.157  -2.486  17.667  0.70 29.99  ? 184 THR A OG1   1 
ATOM   1541 C  CG2   A THR A 1 212 ? 13.877  -3.099  19.132  0.30 28.78  ? 184 THR A CG2   1 
ATOM   1542 C  CG2   B THR A 1 212 ? 13.034  -1.255  19.549  0.70 44.24  ? 184 THR A CG2   1 
ATOM   1543 N  N     . ALA A 1 213 ? 16.521  -1.866  18.411  1.00 30.60  ? 185 ALA A N     1 
ATOM   1544 C  CA    . ALA A 1 213 ? 17.754  -1.494  19.104  1.00 33.44  ? 185 ALA A CA    1 
ATOM   1545 C  C     . ALA A 1 213 ? 18.519  -0.432  18.337  1.00 36.32  ? 185 ALA A C     1 
ATOM   1546 O  O     . ALA A 1 213 ? 19.023  0.540   18.917  1.00 36.79  ? 185 ALA A O     1 
ATOM   1547 C  CB    . ALA A 1 213 ? 18.650  -2.718  19.305  1.00 33.81  ? 185 ALA A CB    1 
ATOM   1548 N  N     . ILE A 1 214 ? 18.623  -0.593  17.028  1.00 29.59  ? 186 ILE A N     1 
ATOM   1549 C  CA    . ILE A 1 214 ? 19.452  0.338   16.286  1.00 28.29  ? 186 ILE A CA    1 
ATOM   1550 C  C     . ILE A 1 214 ? 18.742  1.671   16.104  1.00 28.16  ? 186 ILE A C     1 
ATOM   1551 O  O     . ILE A 1 214 ? 19.363  2.731   16.225  1.00 29.61  ? 186 ILE A O     1 
ATOM   1552 C  CB    . ILE A 1 214 ? 19.869  -0.286  14.951  1.00 30.49  ? 186 ILE A CB    1 
ATOM   1553 C  CG1   . ILE A 1 214 ? 20.895  -1.408  15.185  1.00 32.23  ? 186 ILE A CG1   1 
ATOM   1554 C  CG2   . ILE A 1 214 ? 20.423  0.767   14.044  1.00 28.10  ? 186 ILE A CG2   1 
ATOM   1555 C  CD1   . ILE A 1 214 ? 21.063  -2.320  14.017  1.00 35.35  ? 186 ILE A CD1   1 
ATOM   1556 N  N     . ILE A 1 215 ? 17.442  1.650   15.806  1.00 27.50  ? 187 ILE A N     1 
ATOM   1557 C  CA    . ILE A 1 215 ? 16.701  2.907   15.680  1.00 29.84  ? 187 ILE A CA    1 
ATOM   1558 C  C     . ILE A 1 215 ? 16.773  3.709   16.982  1.00 30.88  ? 187 ILE A C     1 
ATOM   1559 O  O     . ILE A 1 215 ? 17.036  4.919   16.973  1.00 31.73  ? 187 ILE A O     1 
ATOM   1560 C  CB    . ILE A 1 215 ? 15.251  2.619   15.257  1.00 26.86  ? 187 ILE A CB    1 
ATOM   1561 C  CG1   . ILE A 1 215 ? 15.223  2.131   13.794  1.00 25.11  ? 187 ILE A CG1   1 
ATOM   1562 C  CG2   . ILE A 1 215 ? 14.363  3.882   15.415  1.00 28.91  ? 187 ILE A CG2   1 
ATOM   1563 C  CD1   . ILE A 1 215 ? 13.819  1.572   13.398  1.00 28.01  ? 187 ILE A CD1   1 
ATOM   1564 N  N     . THR A 1 216 ? 16.579  3.041   18.118  1.00 29.19  ? 188 THR A N     1 
ATOM   1565 C  CA    . THR A 1 216 ? 16.599  3.725   19.412  1.00 32.79  ? 188 THR A CA    1 
ATOM   1566 C  C     . THR A 1 216 ? 17.973  4.316   19.713  1.00 37.56  ? 188 THR A C     1 
ATOM   1567 O  O     . THR A 1 216 ? 18.086  5.476   20.129  1.00 38.82  ? 188 THR A O     1 
ATOM   1568 C  CB    . THR A 1 216 ? 16.169  2.746   20.502  1.00 35.31  ? 188 THR A CB    1 
ATOM   1569 O  OG1   . THR A 1 216 ? 14.855  2.282   20.204  1.00 37.46  ? 188 THR A OG1   1 
ATOM   1570 C  CG2   . THR A 1 216 ? 16.140  3.421   21.858  1.00 44.89  ? 188 THR A CG2   1 
ATOM   1571 N  N     . ARG A 1 217 ? 19.027  3.546   19.474  1.00 33.83  ? 189 ARG A N     1 
ATOM   1572 C  CA    . ARG A 1 217 ? 20.387  4.021   19.685  1.00 36.94  ? 189 ARG A CA    1 
ATOM   1573 C  C     . ARG A 1 217 ? 20.704  5.235   18.821  1.00 38.64  ? 189 ARG A C     1 
ATOM   1574 O  O     . ARG A 1 217 ? 21.493  6.097   19.227  1.00 37.06  ? 189 ARG A O     1 
ATOM   1575 C  CB    . ARG A 1 217 ? 21.334  2.856   19.402  1.00 38.13  ? 189 ARG A CB    1 
ATOM   1576 C  CG    . ARG A 1 217 ? 22.815  3.104   19.363  1.00 58.18  ? 189 ARG A CG    1 
ATOM   1577 C  CD    . ARG A 1 217 ? 23.472  1.725   19.350  1.00 61.92  ? 189 ARG A CD    1 
ATOM   1578 N  NE    . ARG A 1 217 ? 23.892  1.320   18.013  1.00 71.93  ? 189 ARG A NE    1 
ATOM   1579 C  CZ    . ARG A 1 217 ? 23.928  0.063   17.588  1.00 69.13  ? 189 ARG A CZ    1 
ATOM   1580 N  NH1   . ARG A 1 217 ? 23.497  -0.937  18.345  1.00 64.30  ? 189 ARG A NH1   1 
ATOM   1581 N  NH2   . ARG A 1 217 ? 24.404  -0.195  16.371  1.00 63.44  ? 189 ARG A NH2   1 
ATOM   1582 N  N     . GLN A 1 218 ? 20.106  5.336   17.632  1.00 30.42  ? 190 GLN A N     1 
ATOM   1583 C  CA    . GLN A 1 218 ? 20.323  6.505   16.798  1.00 28.82  ? 190 GLN A CA    1 
ATOM   1584 C  C     . GLN A 1 218 ? 19.340  7.630   17.088  1.00 32.50  ? 190 GLN A C     1 
ATOM   1585 O  O     . GLN A 1 218 ? 19.287  8.598   16.323  1.00 35.55  ? 190 GLN A O     1 
ATOM   1586 C  CB    . GLN A 1 218 ? 20.258  6.129   15.316  1.00 32.11  ? 190 GLN A CB    1 
ATOM   1587 C  CG    . GLN A 1 218 ? 21.397  5.251   14.909  1.00 36.48  ? 190 GLN A CG    1 
ATOM   1588 C  CD    . GLN A 1 218 ? 22.686  6.022   14.865  1.00 37.59  ? 190 GLN A CD    1 
ATOM   1589 O  OE1   . GLN A 1 218 ? 22.687  7.231   14.643  1.00 45.67  ? 190 GLN A OE1   1 
ATOM   1590 N  NE2   . GLN A 1 218 ? 23.787  5.340   15.101  1.00 39.24  ? 190 GLN A NE2   1 
ATOM   1591 N  N     . GLY A 1 219 ? 18.569  7.531   18.167  1.00 32.92  ? 191 GLY A N     1 
ATOM   1592 C  CA    . GLY A 1 219 ? 17.669  8.601   18.539  1.00 33.26  ? 191 GLY A CA    1 
ATOM   1593 C  C     . GLY A 1 219 ? 16.299  8.571   17.901  1.00 39.91  ? 191 GLY A C     1 
ATOM   1594 O  O     . GLY A 1 219 ? 15.541  9.528   18.072  1.00 37.05  ? 191 GLY A O     1 
ATOM   1595 N  N     . GLY A 1 220 ? 15.948  7.513   17.166  1.00 35.73  ? 192 GLY A N     1 
ATOM   1596 C  CA    . GLY A 1 220 ? 14.607  7.399   16.633  1.00 34.08  ? 192 GLY A CA    1 
ATOM   1597 C  C     . GLY A 1 220 ? 13.651  6.791   17.642  1.00 34.43  ? 192 GLY A C     1 
ATOM   1598 O  O     . GLY A 1 220 ? 14.045  6.277   18.683  1.00 34.13  ? 192 GLY A O     1 
ATOM   1599 N  N     . GLU A 1 221 ? 12.359  6.873   17.335  1.00 30.97  ? 193 GLU A N     1 
ATOM   1600 C  CA    . GLU A 1 221 ? 11.347  6.181   18.119  1.00 35.53  ? 193 GLU A CA    1 
ATOM   1601 C  C     . GLU A 1 221 ? 10.539  5.265   17.226  1.00 33.62  ? 193 GLU A C     1 
ATOM   1602 O  O     . GLU A 1 221 ? 9.936   5.705   16.242  1.00 33.51  ? 193 GLU A O     1 
ATOM   1603 C  CB    . GLU A 1 221 ? 10.401  7.126   18.862  1.00 40.71  ? 193 GLU A CB    1 
ATOM   1604 C  CG    . GLU A 1 221 ? 10.055  8.423   18.197  0.48 42.68  ? 193 GLU A CG    1 
ATOM   1605 C  CD    . GLU A 1 221 ? 9.522   9.425   19.206  0.55 55.50  ? 193 GLU A CD    1 
ATOM   1606 O  OE1   . GLU A 1 221 ? 9.148   8.993   20.321  0.69 60.26  ? 193 GLU A OE1   1 
ATOM   1607 O  OE2   . GLU A 1 221 ? 9.487   10.632  18.891  0.60 56.35  ? 193 GLU A OE2   1 
ATOM   1608 N  N     . VAL A 1 222 ? 10.502  3.998   17.593  1.00 30.91  ? 194 VAL A N     1 
ATOM   1609 C  CA    . VAL A 1 222 ? 9.624   3.051   16.935  1.00 35.71  ? 194 VAL A CA    1 
ATOM   1610 C  C     . VAL A 1 222 ? 8.231   3.339   17.464  1.00 40.51  ? 194 VAL A C     1 
ATOM   1611 O  O     . VAL A 1 222 ? 8.029   3.383   18.680  1.00 37.78  ? 194 VAL A O     1 
ATOM   1612 C  CB    . VAL A 1 222 ? 10.057  1.609   17.227  1.00 37.95  ? 194 VAL A CB    1 
ATOM   1613 C  CG1   . VAL A 1 222 ? 9.016   0.608   16.693  1.00 33.07  ? 194 VAL A CG1   1 
ATOM   1614 C  CG2   . VAL A 1 222 ? 11.481  1.350   16.641  1.00 41.03  ? 194 VAL A CG2   1 
ATOM   1615 N  N     . THR A 1 223 ? 7.292   3.606   16.564  1.00 34.72  ? 195 THR A N     1 
ATOM   1616 C  CA    . THR A 1 223 ? 5.922   3.880   16.984  1.00 35.96  ? 195 THR A CA    1 
ATOM   1617 C  C     . THR A 1 223 ? 5.005   2.688   16.817  1.00 36.47  ? 195 THR A C     1 
ATOM   1618 O  O     . THR A 1 223 ? 4.113   2.490   17.644  1.00 41.20  ? 195 THR A O     1 
ATOM   1619 C  CB    . THR A 1 223 ? 5.327   5.080   16.233  1.00 44.52  ? 195 THR A CB    1 
ATOM   1620 O  OG1   . THR A 1 223 ? 5.377   4.860   14.818  1.00 45.63  ? 195 THR A OG1   1 
ATOM   1621 C  CG2   . THR A 1 223 ? 6.081   6.318   16.584  1.00 48.68  ? 195 THR A CG2   1 
ATOM   1622 N  N     . LYS A 1 224 ? 5.169   1.884   15.772  1.00 34.11  ? 196 LYS A N     1 
ATOM   1623 C  CA    . LYS A 1 224 ? 4.349   0.686   15.744  1.00 35.90  ? 196 LYS A CA    1 
ATOM   1624 C  C     . LYS A 1 224 ? 4.921   -0.349  14.798  1.00 33.64  ? 196 LYS A C     1 
ATOM   1625 O  O     . LYS A 1 224 ? 5.735   -0.052  13.921  1.00 32.77  ? 196 LYS A O     1 
ATOM   1626 C  CB    . LYS A 1 224 ? 2.898   0.983   15.359  1.00 44.99  ? 196 LYS A CB    1 
ATOM   1627 C  CG    . LYS A 1 224 ? 2.691   1.614   14.032  1.00 42.24  ? 196 LYS A CG    1 
ATOM   1628 C  CD    . LYS A 1 224 ? 1.254   2.194   13.960  1.00 46.76  ? 196 LYS A CD    1 
ATOM   1629 C  CE    . LYS A 1 224 ? 1.036   3.342   14.934  1.00 44.81  ? 196 LYS A CE    1 
ATOM   1630 N  NZ    . LYS A 1 224 ? -0.349  3.396   15.480  1.00 44.45  ? 196 LYS A NZ    1 
ATOM   1631 N  N     . PHE A 1 225 ? 4.485   -1.578  15.010  1.00 28.32  ? 197 PHE A N     1 
ATOM   1632 C  CA    . PHE A 1 225 ? 4.660   -2.657  14.048  1.00 31.12  ? 197 PHE A CA    1 
ATOM   1633 C  C     . PHE A 1 225 ? 3.374   -2.757  13.242  1.00 36.91  ? 197 PHE A C     1 
ATOM   1634 O  O     . PHE A 1 225 ? 2.287   -2.764  13.823  1.00 39.62  ? 197 PHE A O     1 
ATOM   1635 C  CB    . PHE A 1 225 ? 4.943   -3.975  14.771  1.00 30.73  ? 197 PHE A CB    1 
ATOM   1636 C  CG    . PHE A 1 225 ? 6.123   -3.913  15.691  1.00 33.71  ? 197 PHE A CG    1 
ATOM   1637 C  CD1   . PHE A 1 225 ? 7.326   -3.348  15.263  1.00 32.67  ? 197 PHE A CD1   1 
ATOM   1638 C  CD2   . PHE A 1 225 ? 6.056   -4.441  16.965  1.00 33.91  ? 197 PHE A CD2   1 
ATOM   1639 C  CE1   . PHE A 1 225 ? 8.434   -3.288  16.106  1.00 32.24  ? 197 PHE A CE1   1 
ATOM   1640 C  CE2   . PHE A 1 225 ? 7.164   -4.387  17.814  1.00 35.40  ? 197 PHE A CE2   1 
ATOM   1641 C  CZ    . PHE A 1 225 ? 8.350   -3.806  17.386  1.00 34.26  ? 197 PHE A CZ    1 
ATOM   1642 N  N     . ILE A 1 226 ? 3.483   -2.785  11.918  1.00 29.75  ? 198 ILE A N     1 
ATOM   1643 C  CA    . ILE A 1 226 ? 2.324   -3.007  11.059  1.00 27.90  ? 198 ILE A CA    1 
ATOM   1644 C  C     . ILE A 1 226 ? 2.597   -4.292  10.301  1.00 29.71  ? 198 ILE A C     1 
ATOM   1645 O  O     . ILE A 1 226 ? 3.255   -4.275  9.260   1.00 29.14  ? 198 ILE A O     1 
ATOM   1646 C  CB    . ILE A 1 226 ? 2.076   -1.852  10.091  1.00 37.97  ? 198 ILE A CB    1 
ATOM   1647 C  CG1   . ILE A 1 226 ? 2.078   -0.521  10.835  1.00 38.53  ? 198 ILE A CG1   1 
ATOM   1648 C  CG2   . ILE A 1 226 ? 0.778   -2.086  9.311   1.00 34.39  ? 198 ILE A CG2   1 
ATOM   1649 C  CD1   . ILE A 1 226 ? 2.578   0.630   9.990   1.00 46.45  ? 198 ILE A CD1   1 
ATOM   1650 N  N     . GLY A 1 227 ? 2.087   -5.401  10.807  1.00 29.90  ? 199 GLY A N     1 
ATOM   1651 C  CA    . GLY A 1 227 ? 2.515   -6.674  10.275  1.00 33.12  ? 199 GLY A CA    1 
ATOM   1652 C  C     . GLY A 1 227 ? 4.023   -6.777  10.404  1.00 28.96  ? 199 GLY A C     1 
ATOM   1653 O  O     . GLY A 1 227 ? 4.596   -6.489  11.455  1.00 27.90  ? 199 GLY A O     1 
ATOM   1654 N  N     . ASP A 1 228 ? 4.681   -7.174  9.324   1.00 28.33  ? 200 ASP A N     1 
ATOM   1655 C  CA    . ASP A 1 228 ? 6.136   -7.312  9.315   1.00 25.54  ? 200 ASP A CA    1 
ATOM   1656 C  C     . ASP A 1 228 ? 6.867   -5.989  9.136   1.00 30.10  ? 200 ASP A C     1 
ATOM   1657 O  O     . ASP A 1 228 ? 8.105   -5.980  9.054   1.00 32.26  ? 200 ASP A O     1 
ATOM   1658 C  CB    . ASP A 1 228 ? 6.535   -8.291  8.204   1.00 32.55  ? 200 ASP A CB    1 
ATOM   1659 C  CG    . ASP A 1 228 ? 6.220   -7.749  6.808   1.00 38.13  ? 200 ASP A CG    1 
ATOM   1660 O  OD1   . ASP A 1 228 ? 5.041   -7.414  6.538   1.00 33.68  ? 200 ASP A OD1   1 
ATOM   1661 O  OD2   . ASP A 1 228 ? 7.121   -7.752  5.954   1.00 31.39  ? 200 ASP A OD2   1 
ATOM   1662 N  N     . CYS A 1 229 ? 6.149   -4.880  9.115   1.00 29.29  ? 201 CYS A N     1 
ATOM   1663 C  CA    . CYS A 1 229 ? 6.720   -3.569  8.858   1.00 27.35  ? 201 CYS A CA    1 
ATOM   1664 C  C     . CYS A 1 229 ? 6.968   -2.826  10.166  1.00 31.24  ? 201 CYS A C     1 
ATOM   1665 O  O     . CYS A 1 229 ? 6.084   -2.757  11.030  1.00 30.85  ? 201 CYS A O     1 
ATOM   1666 C  CB    . CYS A 1 229 ? 5.780   -2.771  7.951   1.00 32.11  ? 201 CYS A CB    1 
ATOM   1667 S  SG    . CYS A 1 229 ? 6.305   -1.086  7.714   1.00 42.25  ? 201 CYS A SG    1 
ATOM   1668 N  N     . VAL A 1 230 ? 8.181   -2.304  10.326  1.00 25.96  ? 202 VAL A N     1 
ATOM   1669 C  CA    . VAL A 1 230 ? 8.523   -1.441  11.452  1.00 25.32  ? 202 VAL A CA    1 
ATOM   1670 C  C     . VAL A 1 230 ? 8.329   0.003   11.003  1.00 29.03  ? 202 VAL A C     1 
ATOM   1671 O  O     . VAL A 1 230 ? 8.909   0.424   9.995   1.00 28.86  ? 202 VAL A O     1 
ATOM   1672 C  CB    . VAL A 1 230 ? 9.988   -1.656  11.899  1.00 31.61  ? 202 VAL A CB    1 
ATOM   1673 C  CG1   . VAL A 1 230 ? 10.362  -0.672  13.001  1.00 32.04  ? 202 VAL A CG1   1 
ATOM   1674 C  CG2   . VAL A 1 230 ? 10.262  -3.109  12.325  1.00 30.12  ? 202 VAL A CG2   1 
ATOM   1675 N  N     . MET A 1 231 ? 7.562   0.772   11.769  1.00 25.51  ? 203 MET A N     1 
ATOM   1676 C  CA    . MET A 1 231 ? 7.377   2.195   11.520  1.00 26.91  ? 203 MET A CA    1 
ATOM   1677 C  C     . MET A 1 231 ? 8.032   2.988   12.638  1.00 25.98  ? 203 MET A C     1 
ATOM   1678 O  O     . MET A 1 231 ? 7.766   2.726   13.820  1.00 31.96  ? 203 MET A O     1 
ATOM   1679 C  CB    . MET A 1 231 ? 5.894   2.540   11.443  1.00 29.95  ? 203 MET A CB    1 
ATOM   1680 C  CG    . MET A 1 231 ? 5.616   3.999   11.372  1.00 33.54  ? 203 MET A CG    1 
ATOM   1681 S  SD    . MET A 1 231 ? 3.868   4.296   11.068  1.00 36.51  ? 203 MET A SD    1 
ATOM   1682 C  CE    . MET A 1 231 ? 3.868   6.009   10.628  1.00 33.89  ? 203 MET A CE    1 
ATOM   1683 N  N     . ALA A 1 232 ? 8.861   3.968   12.276  1.00 25.45  ? 204 ALA A N     1 
ATOM   1684 C  CA    . ALA A 1 232 ? 9.595   4.745   13.262  1.00 31.40  ? 204 ALA A CA    1 
ATOM   1685 C  C     . ALA A 1 232 ? 9.706   6.189   12.813  1.00 30.64  ? 204 ALA A C     1 
ATOM   1686 O  O     . ALA A 1 232 ? 9.613   6.498   11.626  1.00 27.29  ? 204 ALA A O     1 
ATOM   1687 C  CB    . ALA A 1 232 ? 11.018  4.190   13.487  1.00 26.47  ? 204 ALA A CB    1 
ATOM   1688 N  N     . TYR A 1 233 ? 9.956   7.073   13.778  1.00 27.87  ? 205 TYR A N     1 
ATOM   1689 C  CA    . TYR A 1 233 ? 10.160  8.488   13.504  1.00 26.71  ? 205 TYR A CA    1 
ATOM   1690 C  C     . TYR A 1 233 ? 11.535  8.933   13.934  1.00 29.55  ? 205 TYR A C     1 
ATOM   1691 O  O     . TYR A 1 233 ? 12.024  8.518   14.980  1.00 34.53  ? 205 TYR A O     1 
ATOM   1692 C  CB    . TYR A 1 233 ? 9.187   9.391   14.271  1.00 32.64  ? 205 TYR A CB    1 
ATOM   1693 C  CG    . TYR A 1 233 ? 7.756   9.160   13.947  1.00 31.98  ? 205 TYR A CG    1 
ATOM   1694 C  CD1   . TYR A 1 233 ? 7.335   9.021   12.637  1.00 32.92  ? 205 TYR A CD1   1 
ATOM   1695 C  CD2   . TYR A 1 233 ? 6.806   9.156   14.952  1.00 39.06  ? 205 TYR A CD2   1 
ATOM   1696 C  CE1   . TYR A 1 233 ? 5.991   8.824   12.343  1.00 31.91  ? 205 TYR A CE1   1 
ATOM   1697 C  CE2   . TYR A 1 233 ? 5.480   8.958   14.673  1.00 42.23  ? 205 TYR A CE2   1 
ATOM   1698 C  CZ    . TYR A 1 233 ? 5.069   8.801   13.373  1.00 39.06  ? 205 TYR A CZ    1 
ATOM   1699 O  OH    . TYR A 1 233 ? 3.733   8.603   13.092  1.00 44.90  ? 205 TYR A OH    1 
ATOM   1700 N  N     . PHE A 1 234 ? 12.099  9.849   13.159  1.00 30.37  ? 206 PHE A N     1 
ATOM   1701 C  CA    . PHE A 1 234 ? 13.250  10.646  13.549  1.00 31.80  ? 206 PHE A CA    1 
ATOM   1702 C  C     . PHE A 1 234 ? 12.842  12.108  13.438  1.00 36.91  ? 206 PHE A C     1 
ATOM   1703 O  O     . PHE A 1 234 ? 11.968  12.442  12.637  1.00 31.99  ? 206 PHE A O     1 
ATOM   1704 C  CB    . PHE A 1 234 ? 14.461  10.368  12.636  1.00 28.81  ? 206 PHE A CB    1 
ATOM   1705 C  CG    . PHE A 1 234 ? 15.044  8.990   12.803  1.00 28.66  ? 206 PHE A CG    1 
ATOM   1706 C  CD1   . PHE A 1 234 ? 14.480  7.912   12.159  1.00 30.00  ? 206 PHE A CD1   1 
ATOM   1707 C  CD2   . PHE A 1 234 ? 16.181  8.786   13.586  1.00 31.59  ? 206 PHE A CD2   1 
ATOM   1708 C  CE1   . PHE A 1 234 ? 15.009  6.629   12.299  1.00 30.82  ? 206 PHE A CE1   1 
ATOM   1709 C  CE2   . PHE A 1 234 ? 16.726  7.509   13.737  1.00 29.01  ? 206 PHE A CE2   1 
ATOM   1710 C  CZ    . PHE A 1 234 ? 16.129  6.425   13.098  1.00 28.92  ? 206 PHE A CZ    1 
ATOM   1711 N  N     . ASP A 1 235 ? 13.465  12.980  14.234  1.00 36.87  ? 207 ASP A N     1 
ATOM   1712 C  CA    . ASP A 1 235 ? 13.200  14.410  14.093  1.00 39.74  ? 207 ASP A CA    1 
ATOM   1713 C  C     . ASP A 1 235 ? 13.493  14.855  12.672  1.00 34.92  ? 207 ASP A C     1 
ATOM   1714 O  O     . ASP A 1 235 ? 14.341  14.284  11.988  1.00 33.22  ? 207 ASP A O     1 
ATOM   1715 C  CB    . ASP A 1 235 ? 14.037  15.220  15.077  1.00 40.95  ? 207 ASP A CB    1 
ATOM   1716 C  CG    . ASP A 1 235 ? 13.510  15.119  16.501  1.00 43.85  ? 207 ASP A CG    1 
ATOM   1717 O  OD1   . ASP A 1 235 ? 12.383  14.607  16.688  1.00 53.48  ? 207 ASP A OD1   1 
ATOM   1718 O  OD2   . ASP A 1 235 ? 14.237  15.515  17.436  1.00 60.93  ? 207 ASP A OD2   1 
ATOM   1719 N  N     . GLY A 1 236 ? 12.770  15.886  12.220  1.00 35.05  ? 208 GLY A N     1 
ATOM   1720 C  CA    . GLY A 1 236 ? 12.835  16.293  10.822  1.00 34.71  ? 208 GLY A CA    1 
ATOM   1721 C  C     . GLY A 1 236 ? 14.203  16.749  10.355  1.00 37.42  ? 208 GLY A C     1 
ATOM   1722 O  O     . GLY A 1 236 ? 14.489  16.703  9.156   1.00 42.80  ? 208 GLY A O     1 
ATOM   1723 N  N     . ASP A 1 237 ? 15.066  17.172  11.267  1.00 37.37  ? 209 ASP A N     1 
ATOM   1724 C  CA    . ASP A 1 237 ? 16.419  17.557  10.892  1.00 44.54  ? 209 ASP A CA    1 
ATOM   1725 C  C     . ASP A 1 237 ? 17.448  16.486  11.242  1.00 43.64  ? 209 ASP A C     1 
ATOM   1726 O  O     . ASP A 1 237 ? 18.653  16.770  11.264  1.00 45.99  ? 209 ASP A O     1 
ATOM   1727 C  CB    . ASP A 1 237 ? 16.779  18.892  11.548  1.00 45.90  ? 209 ASP A CB    1 
ATOM   1728 C  CG    . ASP A 1 237 ? 16.744  18.832  13.063  1.00 54.83  ? 209 ASP A CG    1 
ATOM   1729 O  OD1   . ASP A 1 237 ? 16.297  17.811  13.629  1.00 56.87  ? 209 ASP A OD1   1 
ATOM   1730 O  OD2   . ASP A 1 237 ? 17.149  19.830  13.699  1.00 70.25  ? 209 ASP A OD2   1 
ATOM   1731 N  N     . CYS A 1 238 ? 17.002  15.260  11.507  1.00 37.93  ? 210 CYS A N     1 
ATOM   1732 C  CA    . CYS A 1 238 ? 17.889  14.158  11.871  1.00 34.84  ? 210 CYS A CA    1 
ATOM   1733 C  C     . CYS A 1 238 ? 17.957  13.116  10.759  1.00 33.29  ? 210 CYS A C     1 
ATOM   1734 O  O     . CYS A 1 238 ? 17.948  11.915  11.018  1.00 29.95  ? 210 CYS A O     1 
ATOM   1735 C  CB    . CYS A 1 238 ? 17.437  13.517  13.176  1.00 36.88  ? 210 CYS A CB    1 
ATOM   1736 S  SG    . CYS A 1 238 ? 17.840  14.524  14.609  1.00 43.65  ? 210 CYS A SG    1 
ATOM   1737 N  N     . ALA A 1 239 ? 18.025  13.578  9.510   1.00 30.62  ? 211 ALA A N     1 
ATOM   1738 C  CA    . ALA A 1 239 ? 18.181  12.667  8.378   1.00 36.87  ? 211 ALA A CA    1 
ATOM   1739 C  C     . ALA A 1 239 ? 19.444  11.824  8.482   1.00 34.62  ? 211 ALA A C     1 
ATOM   1740 O  O     . ALA A 1 239 ? 19.429  10.644  8.119   1.00 30.42  ? 211 ALA A O     1 
ATOM   1741 C  CB    . ALA A 1 239 ? 18.185  13.453  7.069   1.00 32.54  ? 211 ALA A CB    1 
ATOM   1742 N  N     . ASP A 1 240 ? 20.563  12.421  8.917   1.00 31.25  ? 212 ASP A N     1 
ATOM   1743 C  CA    . ASP A 1 240 ? 21.809  11.659  8.990   1.00 34.32  ? 212 ASP A CA    1 
ATOM   1744 C  C     . ASP A 1 240 ? 21.668  10.471  9.924   1.00 27.13  ? 212 ASP A C     1 
ATOM   1745 O  O     . ASP A 1 240 ? 22.208  9.391   9.651   1.00 30.91  ? 212 ASP A O     1 
ATOM   1746 C  CB    . ASP A 1 240 ? 22.971  12.549  9.446   1.00 34.59  ? 212 ASP A CB    1 
ATOM   1747 C  CG    . ASP A 1 240 ? 23.223  13.697  8.498   1.00 40.62  ? 212 ASP A CG    1 
ATOM   1748 O  OD1   . ASP A 1 240 ? 23.487  13.435  7.305   1.00 36.16  ? 212 ASP A OD1   1 
ATOM   1749 O  OD2   . ASP A 1 240 ? 23.129  14.863  8.924   1.00 46.96  ? 212 ASP A OD2   1 
ATOM   1750 N  N     . GLN A 1 241 ? 20.987  10.674  11.053  1.00 27.14  ? 213 GLN A N     1 
ATOM   1751 C  CA    . GLN A 1 241 ? 20.753  9.603   12.015  1.00 31.53  ? 213 GLN A CA    1 
ATOM   1752 C  C     . GLN A 1 241 ? 19.849  8.522   11.422  1.00 30.18  ? 213 GLN A C     1 
ATOM   1753 O  O     . GLN A 1 241 ? 20.078  7.322   11.637  1.00 30.32  ? 213 GLN A O     1 
ATOM   1754 C  CB    . GLN A 1 241 ? 20.140  10.205  13.275  1.00 31.28  ? 213 GLN A CB    1 
ATOM   1755 C  CG    . GLN A 1 241 ? 21.162  10.957  14.143  0.87 30.42  ? 213 GLN A CG    1 
ATOM   1756 C  CD    . GLN A 1 241 ? 21.616  12.266  13.518  0.79 38.67  ? 213 GLN A CD    1 
ATOM   1757 O  OE1   . GLN A 1 241 ? 20.827  13.021  12.941  0.85 37.93  ? 213 GLN A OE1   1 
ATOM   1758 N  NE2   . GLN A 1 241 ? 22.915  12.523  13.606  0.64 40.53  ? 213 GLN A NE2   1 
ATOM   1759 N  N     . ALA A 1 242 ? 18.819  8.926   10.668  1.00 28.71  ? 214 ALA A N     1 
ATOM   1760 C  CA    . ALA A 1 242 ? 17.948  7.938   10.027  1.00 28.03  ? 214 ALA A CA    1 
ATOM   1761 C  C     . ALA A 1 242 ? 18.701  7.124   8.974   1.00 28.75  ? 214 ALA A C     1 
ATOM   1762 O  O     . ALA A 1 242 ? 18.515  5.903   8.865   1.00 29.47  ? 214 ALA A O     1 
ATOM   1763 C  CB    . ALA A 1 242 ? 16.745  8.640   9.388   1.00 26.90  ? 214 ALA A CB    1 
ATOM   1764 N  N     . ILE A 1 243 ? 19.524  7.790   8.165   1.00 26.85  ? 215 ILE A N     1 
ATOM   1765 C  CA    . ILE A 1 243 ? 20.341  7.080   7.182   1.00 25.28  ? 215 ILE A CA    1 
ATOM   1766 C  C     . ILE A 1 243 ? 21.361  6.174   7.860   1.00 27.61  ? 215 ILE A C     1 
ATOM   1767 O  O     . ILE A 1 243 ? 21.545  5.023   7.451   1.00 26.29  ? 215 ILE A O     1 
ATOM   1768 C  CB    . ILE A 1 243 ? 21.016  8.085   6.240   1.00 29.04  ? 215 ILE A CB    1 
ATOM   1769 C  CG1   . ILE A 1 243 ? 19.944  8.795   5.403   1.00 32.30  ? 215 ILE A CG1   1 
ATOM   1770 C  CG2   . ILE A 1 243 ? 22.038  7.383   5.341   1.00 28.41  ? 215 ILE A CG2   1 
ATOM   1771 C  CD1   . ILE A 1 243 ? 20.504  9.972   4.631   1.00 33.89  ? 215 ILE A CD1   1 
ATOM   1772 N  N     . GLN A 1 244 ? 22.044  6.667   8.907   1.00 28.04  ? 216 GLN A N     1 
ATOM   1773 C  CA    . GLN A 1 244 ? 22.994  5.811   9.606   1.00 29.53  ? 216 GLN A CA    1 
ATOM   1774 C  C     . GLN A 1 244 ? 22.295  4.593   10.189  1.00 28.23  ? 216 GLN A C     1 
ATOM   1775 O  O     . GLN A 1 244 ? 22.815  3.472   10.104  1.00 28.45  ? 216 GLN A O     1 
ATOM   1776 C  CB    . GLN A 1 244 ? 23.705  6.570   10.729  1.00 32.32  ? 216 GLN A CB    1 
ATOM   1777 C  CG    . GLN A 1 244 ? 24.761  5.713   11.410  1.00 32.38  ? 216 GLN A CG    1 
ATOM   1778 C  CD    . GLN A 1 244 ? 25.925  5.401   10.457  1.00 35.88  ? 216 GLN A CD    1 
ATOM   1779 O  OE1   . GLN A 1 244 ? 26.542  6.308   9.901   1.00 39.08  ? 216 GLN A OE1   1 
ATOM   1780 N  NE2   . GLN A 1 244 ? 26.202  4.124   10.246  1.00 41.15  ? 216 GLN A NE2   1 
ATOM   1781 N  N     . ALA A 1 245 ? 21.115  4.794   10.792  1.00 28.49  ? 217 ALA A N     1 
ATOM   1782 C  CA    . ALA A 1 245 ? 20.371  3.676   11.369  1.00 29.97  ? 217 ALA A CA    1 
ATOM   1783 C  C     . ALA A 1 245 ? 20.026  2.640   10.309  1.00 24.09  ? 217 ALA A C     1 
ATOM   1784 O  O     . ALA A 1 245 ? 20.152  1.432   10.548  1.00 26.50  ? 217 ALA A O     1 
ATOM   1785 C  CB    . ALA A 1 245 ? 19.092  4.177   12.048  1.00 29.61  ? 217 ALA A CB    1 
ATOM   1786 N  N     . SER A 1 246 ? 19.571  3.102   9.141   1.00 23.12  ? 218 SER A N     1 
ATOM   1787 C  CA    . SER A 1 246 ? 19.296  2.205   8.019   1.00 26.71  ? 218 SER A CA    1 
ATOM   1788 C  C     . SER A 1 246 ? 20.532  1.399   7.622   1.00 30.30  ? 218 SER A C     1 
ATOM   1789 O  O     . SER A 1 246 ? 20.456  0.177   7.435   1.00 25.96  ? 218 SER A O     1 
ATOM   1790 C  CB    . SER A 1 246 ? 18.778  3.020   6.834   1.00 24.98  ? 218 SER A CB    1 
ATOM   1791 O  OG    . SER A 1 246 ? 17.612  3.782   7.204   1.00 27.65  ? 218 SER A OG    1 
ATOM   1792 N  N     . LEU A 1 247 ? 21.671  2.069   7.421   1.00 27.67  ? 219 LEU A N     1 
ATOM   1793 C  CA    . LEU A 1 247 ? 22.890  1.335   7.053   1.00 27.72  ? 219 LEU A CA    1 
ATOM   1794 C  C     . LEU A 1 247 ? 23.293  0.344   8.134   1.00 25.70  ? 219 LEU A C     1 
ATOM   1795 O  O     . LEU A 1 247 ? 23.707  -0.785  7.830   1.00 29.60  ? 219 LEU A O     1 
ATOM   1796 C  CB    . LEU A 1 247 ? 24.041  2.309   6.780   1.00 29.67  ? 219 LEU A CB    1 
ATOM   1797 C  CG    . LEU A 1 247 ? 23.777  3.249   5.620   1.00 33.69  ? 219 LEU A CG    1 
ATOM   1798 C  CD1   . LEU A 1 247 ? 24.847  4.340   5.540   1.00 34.47  ? 219 LEU A CD1   1 
ATOM   1799 C  CD2   . LEU A 1 247 ? 23.697  2.458   4.329   1.00 31.72  ? 219 LEU A CD2   1 
ATOM   1800 N  N     . ASP A 1 248 ? 23.185  0.734   9.404   1.00 27.15  ? 220 ASP A N     1 
ATOM   1801 C  CA    . ASP A 1 248 ? 23.544  -0.186  10.481  1.00 28.46  ? 220 ASP A CA    1 
ATOM   1802 C  C     . ASP A 1 248 ? 22.630  -1.405  10.515  1.00 27.94  ? 220 ASP A C     1 
ATOM   1803 O  O     . ASP A 1 248 ? 23.087  -2.524  10.773  1.00 25.53  ? 220 ASP A O     1 
ATOM   1804 C  CB    . ASP A 1 248 ? 23.501  0.525   11.823  1.00 28.56  ? 220 ASP A CB    1 
ATOM   1805 C  CG    . ASP A 1 248 ? 24.676  1.475   12.003  1.00 39.88  ? 220 ASP A CG    1 
ATOM   1806 O  OD1   . ASP A 1 248 ? 25.594  1.447   11.164  1.00 34.52  ? 220 ASP A OD1   1 
ATOM   1807 O  OD2   . ASP A 1 248 ? 24.680  2.228   12.983  1.00 38.49  ? 220 ASP A OD2   1 
ATOM   1808 N  N     . ILE A 1 249 ? 21.326  -1.211  10.303  1.00 27.50  ? 221 ILE A N     1 
ATOM   1809 C  CA    . ILE A 1 249 ? 20.431  -2.366  10.235  1.00 23.57  ? 221 ILE A CA    1 
ATOM   1810 C  C     . ILE A 1 249 ? 20.860  -3.304  9.117   1.00 24.27  ? 221 ILE A C     1 
ATOM   1811 O  O     . ILE A 1 249 ? 20.922  -4.528  9.298   1.00 25.62  ? 221 ILE A O     1 
ATOM   1812 C  CB    . ILE A 1 249 ? 18.963  -1.894  10.062  1.00 23.55  ? 221 ILE A CB    1 
ATOM   1813 C  CG1   . ILE A 1 249 ? 18.498  -1.232  11.359  1.00 29.07  ? 221 ILE A CG1   1 
ATOM   1814 C  CG2   . ILE A 1 249 ? 18.056  -3.062  9.709   1.00 26.55  ? 221 ILE A CG2   1 
ATOM   1815 C  CD1   . ILE A 1 249 ? 17.144  -0.492  11.224  1.00 27.61  ? 221 ILE A CD1   1 
ATOM   1816 N  N     . LEU A 1 250 ? 21.170  -2.755  7.938   1.00 25.15  ? 222 LEU A N     1 
ATOM   1817 C  CA    . LEU A 1 250 ? 21.558  -3.632  6.840   1.00 29.51  ? 222 LEU A CA    1 
ATOM   1818 C  C     . LEU A 1 250 ? 22.836  -4.389  7.183   1.00 30.16  ? 222 LEU A C     1 
ATOM   1819 O  O     . LEU A 1 250 ? 22.961  -5.580  6.892   1.00 28.25  ? 222 LEU A O     1 
ATOM   1820 C  CB    . LEU A 1 250 ? 21.724  -2.830  5.555   1.00 31.44  ? 222 LEU A CB    1 
ATOM   1821 C  CG    . LEU A 1 250 ? 20.414  -2.218  5.055   1.00 33.00  ? 222 LEU A CG    1 
ATOM   1822 C  CD1   . LEU A 1 250 ? 20.708  -1.331  3.863   1.00 33.02  ? 222 LEU A CD1   1 
ATOM   1823 C  CD2   . LEU A 1 250 ? 19.367  -3.299  4.708   1.00 32.00  ? 222 LEU A CD2   1 
ATOM   1824 N  N     . MET A 1 251 ? 23.784  -3.714  7.824   1.00 27.97  ? 223 MET A N     1 
ATOM   1825 C  CA    A MET A 1 251 ? 25.034  -4.369  8.198   0.39 32.85  ? 223 MET A CA    1 
ATOM   1826 C  CA    B MET A 1 251 ? 25.032  -4.373  8.191   0.61 32.85  ? 223 MET A CA    1 
ATOM   1827 C  C     . MET A 1 251 ? 24.795  -5.469  9.225   1.00 31.73  ? 223 MET A C     1 
ATOM   1828 O  O     . MET A 1 251 ? 25.338  -6.570  9.098   1.00 31.99  ? 223 MET A O     1 
ATOM   1829 C  CB    A MET A 1 251 ? 26.027  -3.327  8.722   0.39 32.67  ? 223 MET A CB    1 
ATOM   1830 C  CB    B MET A 1 251 ? 26.031  -3.342  8.714   0.61 32.62  ? 223 MET A CB    1 
ATOM   1831 C  CG    A MET A 1 251 ? 27.237  -3.901  9.446   0.39 41.53  ? 223 MET A CG    1 
ATOM   1832 C  CG    B MET A 1 251 ? 27.080  -3.916  9.644   0.61 41.34  ? 223 MET A CG    1 
ATOM   1833 S  SD    A MET A 1 251 ? 27.996  -2.664  10.530  0.39 60.63  ? 223 MET A SD    1 
ATOM   1834 S  SD    B MET A 1 251 ? 28.335  -2.665  9.979   0.61 59.05  ? 223 MET A SD    1 
ATOM   1835 C  CE    A MET A 1 251 ? 28.284  -3.618  12.017  0.39 50.12  ? 223 MET A CE    1 
ATOM   1836 C  CE    B MET A 1 251 ? 28.753  -2.174  8.316   0.61 46.22  ? 223 MET A CE    1 
ATOM   1837 N  N     . GLU A 1 252 ? 23.971  -5.198  10.246  1.00 25.92  ? 224 GLU A N     1 
ATOM   1838 C  CA    . GLU A 1 252 ? 23.672  -6.213  11.264  1.00 24.35  ? 224 GLU A CA    1 
ATOM   1839 C  C     . GLU A 1 252 ? 22.940  -7.416  10.673  1.00 30.75  ? 224 GLU A C     1 
ATOM   1840 O  O     . GLU A 1 252 ? 23.170  -8.556  11.093  1.00 30.47  ? 224 GLU A O     1 
ATOM   1841 C  CB    . GLU A 1 252 ? 22.833  -5.609  12.396  1.00 27.77  ? 224 GLU A CB    1 
ATOM   1842 C  CG    . GLU A 1 252 ? 23.594  -4.699  13.288  1.00 41.40  ? 224 GLU A CG    1 
ATOM   1843 C  CD    . GLU A 1 252 ? 24.728  -5.400  13.998  1.00 43.81  ? 224 GLU A CD    1 
ATOM   1844 O  OE1   . GLU A 1 252 ? 24.540  -6.553  14.427  1.00 46.73  ? 224 GLU A OE1   1 
ATOM   1845 O  OE2   . GLU A 1 252 ? 25.811  -4.792  14.106  1.00 50.57  ? 224 GLU A OE2   1 
ATOM   1846 N  N     . LEU A 1 253 ? 22.014  -7.188  9.729   1.00 25.84  ? 225 LEU A N     1 
ATOM   1847 C  CA    . LEU A 1 253 ? 21.323  -8.322  9.124   1.00 25.91  ? 225 LEU A CA    1 
ATOM   1848 C  C     . LEU A 1 253 ? 22.296  -9.168  8.313   1.00 25.64  ? 225 LEU A C     1 
ATOM   1849 O  O     . LEU A 1 253 ? 22.179  -10.395 8.284   1.00 28.12  ? 225 LEU A O     1 
ATOM   1850 C  CB    . LEU A 1 253 ? 20.165  -7.838  8.240   1.00 24.81  ? 225 LEU A CB    1 
ATOM   1851 C  CG    . LEU A 1 253 ? 18.964  -7.316  9.043   1.00 30.31  ? 225 LEU A CG    1 
ATOM   1852 C  CD1   . LEU A 1 253 ? 17.816  -6.903  8.099   1.00 30.38  ? 225 LEU A CD1   1 
ATOM   1853 C  CD2   . LEU A 1 253 ? 18.467  -8.358  10.034  1.00 36.04  ? 225 LEU A CD2   1 
ATOM   1854 N  N     . GLU A 1 254 ? 23.250  -8.529  7.639   1.00 29.20  ? 226 GLU A N     1 
ATOM   1855 C  CA    . GLU A 1 254 ? 24.240  -9.304  6.894   1.00 30.59  ? 226 GLU A CA    1 
ATOM   1856 C  C     . GLU A 1 254 ? 25.065  -10.172 7.838   1.00 28.03  ? 226 GLU A C     1 
ATOM   1857 O  O     . GLU A 1 254 ? 25.259  -11.363 7.581   1.00 29.73  ? 226 GLU A O     1 
ATOM   1858 C  CB    . GLU A 1 254 ? 25.138  -8.375  6.076   1.00 30.69  ? 226 GLU A CB    1 
ATOM   1859 C  CG    . GLU A 1 254 ? 26.380  -9.043  5.522   1.00 34.78  ? 226 GLU A CG    1 
ATOM   1860 C  CD    . GLU A 1 254 ? 26.101  -9.838  4.267   1.00 40.99  ? 226 GLU A CD    1 
ATOM   1861 O  OE1   . GLU A 1 254 ? 25.073  -9.576  3.593   1.00 39.44  ? 226 GLU A OE1   1 
ATOM   1862 O  OE2   . GLU A 1 254 ? 26.936  -10.700 3.919   1.00 50.02  ? 226 GLU A OE2   1 
ATOM   1863 N  N     . ILE A 1 255 ? 25.503  -9.603  8.959   1.00 27.17  ? 227 ILE A N     1 
ATOM   1864 C  CA    . ILE A 1 255 ? 26.218  -10.366 9.983   1.00 30.59  ? 227 ILE A CA    1 
ATOM   1865 C  C     . ILE A 1 255 ? 25.360  -11.508 10.496  1.00 31.02  ? 227 ILE A C     1 
ATOM   1866 O  O     . ILE A 1 255 ? 25.828  -12.638 10.659  1.00 29.11  ? 227 ILE A O     1 
ATOM   1867 C  CB    . ILE A 1 255 ? 26.656  -9.432  11.128  1.00 34.37  ? 227 ILE A CB    1 
ATOM   1868 C  CG1   . ILE A 1 255 ? 27.735  -8.456  10.638  1.00 34.01  ? 227 ILE A CG1   1 
ATOM   1869 C  CG2   . ILE A 1 255 ? 27.168  -10.230 12.352  1.00 35.27  ? 227 ILE A CG2   1 
ATOM   1870 C  CD1   . ILE A 1 255 ? 27.982  -7.329  11.608  1.00 43.16  ? 227 ILE A CD1   1 
ATOM   1871 N  N     . LEU A 1 256 ? 24.086  -11.228 10.758  1.00 27.76  ? 228 LEU A N     1 
ATOM   1872 C  CA    . LEU A 1 256 ? 23.171  -12.242 11.254  1.00 29.13  ? 228 LEU A CA    1 
ATOM   1873 C  C     . LEU A 1 256 ? 23.016  -13.404 10.273  1.00 30.63  ? 228 LEU A C     1 
ATOM   1874 O  O     . LEU A 1 256 ? 23.073  -14.576 10.675  1.00 27.83  ? 228 LEU A O     1 
ATOM   1875 C  CB    . LEU A 1 256 ? 21.817  -11.586 11.535  1.00 29.47  ? 228 LEU A CB    1 
ATOM   1876 C  CG    . LEU A 1 256 ? 20.800  -12.457 12.233  1.00 36.76  ? 228 LEU A CG    1 
ATOM   1877 C  CD1   . LEU A 1 256 ? 21.322  -12.814 13.613  1.00 40.63  ? 228 LEU A CD1   1 
ATOM   1878 C  CD2   . LEU A 1 256 ? 19.479  -11.693 12.316  1.00 38.83  ? 228 LEU A CD2   1 
ATOM   1879 N  N     . ARG A 1 257 ? 22.771  -13.099 8.989   1.00 25.54  ? 229 ARG A N     1 
ATOM   1880 C  CA    . ARG A 1 257 ? 22.640  -14.150 7.976   1.00 28.05  ? 229 ARG A CA    1 
ATOM   1881 C  C     . ARG A 1 257 ? 23.903  -15.012 7.889   1.00 27.95  ? 229 ARG A C     1 
ATOM   1882 O  O     . ARG A 1 257 ? 23.814  -16.236 7.730   1.00 31.42  ? 229 ARG A O     1 
ATOM   1883 C  CB    . ARG A 1 257 ? 22.352  -13.549 6.592   1.00 26.23  ? 229 ARG A CB    1 
ATOM   1884 C  CG    . ARG A 1 257 ? 20.988  -12.854 6.413   1.00 25.57  ? 229 ARG A CG    1 
ATOM   1885 C  CD    . ARG A 1 257 ? 20.758  -12.553 4.933   1.00 28.79  ? 229 ARG A CD    1 
ATOM   1886 N  NE    . ARG A 1 257 ? 21.636  -11.483 4.462   1.00 26.71  ? 229 ARG A NE    1 
ATOM   1887 C  CZ    . ARG A 1 257 ? 21.345  -10.190 4.560   1.00 32.38  ? 229 ARG A CZ    1 
ATOM   1888 N  NH1   . ARG A 1 257 ? 20.235  -9.775  5.157   1.00 27.33  ? 229 ARG A NH1   1 
ATOM   1889 N  NH2   . ARG A 1 257 ? 22.192  -9.293  4.059   1.00 28.58  ? 229 ARG A NH2   1 
ATOM   1890 N  N     . ASN A 1 258 ? 25.080  -14.383 7.947   1.00 29.66  ? 230 ASN A N     1 
ATOM   1891 C  CA    . ASN A 1 258 ? 26.340  -15.117 7.805   1.00 29.42  ? 230 ASN A CA    1 
ATOM   1892 C  C     . ASN A 1 258 ? 26.658  -15.977 9.020   1.00 32.98  ? 230 ASN A C     1 
ATOM   1893 O  O     . ASN A 1 258 ? 27.329  -17.016 8.895   1.00 31.32  ? 230 ASN A O     1 
ATOM   1894 C  CB    . ASN A 1 258 ? 27.509  -14.153 7.586   1.00 27.19  ? 230 ASN A CB    1 
ATOM   1895 C  CG    . ASN A 1 258 ? 27.391  -13.344 6.307   1.00 33.06  ? 230 ASN A CG    1 
ATOM   1896 O  OD1   . ASN A 1 258 ? 26.630  -13.680 5.402   1.00 40.88  ? 230 ASN A OD1   1 
ATOM   1897 N  ND2   . ASN A 1 258 ? 28.160  -12.272 6.228   1.00 41.82  ? 230 ASN A ND2   1 
ATOM   1898 N  N     . SER A 1 259 ? 26.252  -15.536 10.204  1.00 28.78  ? 231 SER A N     1 
ATOM   1899 C  CA    A SER A 1 259 ? 26.720  -16.156 11.431  0.52 30.81  ? 231 SER A CA    1 
ATOM   1900 C  CA    B SER A 1 259 ? 26.707  -16.139 11.447  0.48 30.81  ? 231 SER A CA    1 
ATOM   1901 C  C     . SER A 1 259 ? 25.728  -17.143 12.026  1.00 34.13  ? 231 SER A C     1 
ATOM   1902 O  O     . SER A 1 259 ? 26.073  -17.816 12.999  1.00 35.17  ? 231 SER A O     1 
ATOM   1903 C  CB    A SER A 1 259 ? 27.070  -15.078 12.459  0.52 30.56  ? 231 SER A CB    1 
ATOM   1904 C  CB    B SER A 1 259 ? 26.993  -15.051 12.487  0.48 30.62  ? 231 SER A CB    1 
ATOM   1905 O  OG    A SER A 1 259 ? 25.942  -14.291 12.760  0.52 33.82  ? 231 SER A OG    1 
ATOM   1906 O  OG    B SER A 1 259 ? 27.570  -13.919 11.874  0.48 32.58  ? 231 SER A OG    1 
ATOM   1907 N  N     . ALA A 1 260 ? 24.530  -17.277 11.438  1.00 28.77  ? 232 ALA A N     1 
ATOM   1908 C  CA    . ALA A 1 260 ? 23.531  -18.190 11.962  1.00 32.84  ? 232 ALA A CA    1 
ATOM   1909 C  C     . ALA A 1 260 ? 23.951  -19.642 11.763  1.00 32.53  ? 232 ALA A C     1 
ATOM   1910 O  O     . ALA A 1 260 ? 24.736  -19.962 10.863  1.00 34.45  ? 232 ALA A O     1 
ATOM   1911 C  CB    . ALA A 1 260 ? 22.175  -17.953 11.284  1.00 33.41  ? 232 ALA A CB    1 
ATOM   1912 N  N     . PRO A 1 261 ? 23.417  -20.539 12.588  1.00 37.51  ? 233 PRO A N     1 
ATOM   1913 C  CA    . PRO A 1 261 ? 23.655  -21.978 12.401  1.00 35.90  ? 233 PRO A CA    1 
ATOM   1914 C  C     . PRO A 1 261 ? 23.324  -22.434 10.990  1.00 39.87  ? 233 PRO A C     1 
ATOM   1915 O  O     . PRO A 1 261 ? 22.522  -21.816 10.283  1.00 34.16  ? 233 PRO A O     1 
ATOM   1916 C  CB    . PRO A 1 261 ? 22.703  -22.618 13.421  1.00 40.50  ? 233 PRO A CB    1 
ATOM   1917 C  CG    . PRO A 1 261 ? 22.552  -21.591 14.472  1.00 40.84  ? 233 PRO A CG    1 
ATOM   1918 C  CD    . PRO A 1 261 ? 22.599  -20.261 13.783  1.00 35.14  ? 233 PRO A CD    1 
ATOM   1919 N  N     . GLU A 1 262 ? 23.937  -23.539 10.574  1.00 34.18  ? 234 GLU A N     1 
ATOM   1920 C  CA    A GLU A 1 262 ? 23.561  -24.157 9.310   0.56 40.40  ? 234 GLU A CA    1 
ATOM   1921 C  CA    B GLU A 1 262 ? 23.552  -24.108 9.296   0.44 40.39  ? 234 GLU A CA    1 
ATOM   1922 C  C     . GLU A 1 262 ? 22.079  -24.504 9.347   1.00 41.31  ? 234 GLU A C     1 
ATOM   1923 O  O     . GLU A 1 262 ? 21.563  -24.945 10.378  1.00 34.92  ? 234 GLU A O     1 
ATOM   1924 C  CB    A GLU A 1 262 ? 24.390  -25.421 9.043   0.56 44.83  ? 234 GLU A CB    1 
ATOM   1925 C  CB    B GLU A 1 262 ? 24.446  -25.298 8.939   0.44 44.92  ? 234 GLU A CB    1 
ATOM   1926 C  CG    A GLU A 1 262 ? 25.880  -25.261 9.300   0.56 48.46  ? 234 GLU A CG    1 
ATOM   1927 C  CG    B GLU A 1 262 ? 24.129  -26.591 9.643   0.44 45.79  ? 234 GLU A CG    1 
ATOM   1928 C  CD    A GLU A 1 262 ? 26.707  -26.410 8.737   0.56 54.51  ? 234 GLU A CD    1 
ATOM   1929 C  CD    B GLU A 1 262 ? 24.936  -27.751 9.086   0.44 53.07  ? 234 GLU A CD    1 
ATOM   1930 O  OE1   A GLU A 1 262 ? 26.139  -27.505 8.527   0.56 51.95  ? 234 GLU A OE1   1 
ATOM   1931 O  OE1   B GLU A 1 262 ? 26.116  -27.535 8.733   0.44 55.55  ? 234 GLU A OE1   1 
ATOM   1932 O  OE2   A GLU A 1 262 ? 27.923  -26.206 8.491   0.56 55.55  ? 234 GLU A OE2   1 
ATOM   1933 O  OE2   B GLU A 1 262 ? 24.393  -28.872 8.995   0.44 46.05  ? 234 GLU A OE2   1 
ATOM   1934 N  N     . GLY A 1 263 ? 21.397  -24.295 8.230   1.00 34.68  ? 235 GLY A N     1 
ATOM   1935 C  CA    . GLY A 1 263 ? 19.976  -24.534 8.123   1.00 37.92  ? 235 GLY A CA    1 
ATOM   1936 C  C     . GLY A 1 263 ? 19.077  -23.527 8.827   1.00 37.39  ? 235 GLY A C     1 
ATOM   1937 O  O     . GLY A 1 263 ? 17.865  -23.716 8.816   1.00 35.12  ? 235 GLY A O     1 
ATOM   1938 N  N     . SER A 1 264 ? 19.620  -22.463 9.418   1.00 34.31  ? 236 SER A N     1 
ATOM   1939 C  CA    . SER A 1 264 ? 18.777  -21.507 10.138  1.00 30.10  ? 236 SER A CA    1 
ATOM   1940 C  C     . SER A 1 264 ? 17.933  -20.692 9.160   1.00 31.69  ? 236 SER A C     1 
ATOM   1941 O  O     . SER A 1 264 ? 18.454  -20.199 8.151   1.00 30.23  ? 236 SER A O     1 
ATOM   1942 C  CB    . SER A 1 264 ? 19.633  -20.560 10.977  1.00 31.28  ? 236 SER A CB    1 
ATOM   1943 O  OG    . SER A 1 264 ? 18.836  -19.527 11.565  1.00 33.49  ? 236 SER A OG    1 
ATOM   1944 N  N     . PRO A 1 265 ? 16.636  -20.507 9.443   1.00 31.38  ? 237 PRO A N     1 
ATOM   1945 C  CA    . PRO A 1 265 ? 15.840  -19.551 8.652   1.00 31.70  ? 237 PRO A CA    1 
ATOM   1946 C  C     . PRO A 1 265 ? 16.401  -18.134 8.696   1.00 30.71  ? 237 PRO A C     1 
ATOM   1947 O  O     . PRO A 1 265 ? 16.141  -17.343 7.774   1.00 31.86  ? 237 PRO A O     1 
ATOM   1948 C  CB    . PRO A 1 265 ? 14.443  -19.617 9.305   1.00 31.87  ? 237 PRO A CB    1 
ATOM   1949 C  CG    . PRO A 1 265 ? 14.459  -20.837 10.182  1.00 39.56  ? 237 PRO A CG    1 
ATOM   1950 C  CD    . PRO A 1 265 ? 15.887  -21.033 10.596  1.00 35.07  ? 237 PRO A CD    1 
ATOM   1951 N  N     . LEU A 1 266 ? 17.182  -17.788 9.723   1.00 29.92  ? 238 LEU A N     1 
ATOM   1952 C  CA    . LEU A 1 266 ? 17.780  -16.454 9.753   1.00 30.12  ? 238 LEU A CA    1 
ATOM   1953 C  C     . LEU A 1 266 ? 18.721  -16.201 8.575   1.00 32.83  ? 238 LEU A C     1 
ATOM   1954 O  O     . LEU A 1 266 ? 18.944  -15.037 8.222   1.00 29.18  ? 238 LEU A O     1 
ATOM   1955 C  CB    . LEU A 1 266 ? 18.513  -16.225 11.076  1.00 26.91  ? 238 LEU A CB    1 
ATOM   1956 C  CG    . LEU A 1 266 ? 17.625  -16.281 12.326  1.00 33.56  ? 238 LEU A CG    1 
ATOM   1957 C  CD1   . LEU A 1 266 ? 18.418  -16.133 13.607  1.00 37.12  ? 238 LEU A CD1   1 
ATOM   1958 C  CD2   . LEU A 1 266 ? 16.546  -15.192 12.239  1.00 35.89  ? 238 LEU A CD2   1 
ATOM   1959 N  N     . ARG A 1 267 ? 19.244  -17.253 7.937   1.00 27.63  ? 239 ARG A N     1 
ATOM   1960 C  CA    . ARG A 1 267 ? 20.140  -17.057 6.800   1.00 31.20  ? 239 ARG A CA    1 
ATOM   1961 C  C     . ARG A 1 267 ? 19.441  -16.359 5.644   1.00 28.95  ? 239 ARG A C     1 
ATOM   1962 O  O     . ARG A 1 267 ? 20.123  -15.725 4.814   1.00 32.12  ? 239 ARG A O     1 
ATOM   1963 C  CB    . ARG A 1 267 ? 20.715  -18.416 6.343   1.00 31.65  ? 239 ARG A CB    1 
ATOM   1964 C  CG    . ARG A 1 267 ? 21.598  -18.406 5.070   1.00 30.36  ? 239 ARG A CG    1 
ATOM   1965 C  CD    . ARG A 1 267 ? 22.649  -19.552 5.181   1.00 28.25  ? 239 ARG A CD    1 
ATOM   1966 N  NE    . ARG A 1 267 ? 23.645  -19.136 6.148   1.00 26.94  ? 239 ARG A NE    1 
ATOM   1967 C  CZ    . ARG A 1 267 ? 23.755  -19.606 7.376   1.00 29.27  ? 239 ARG A CZ    1 
ATOM   1968 N  NH1   . ARG A 1 267 ? 23.104  -20.701 7.756   1.00 29.25  ? 239 ARG A NH1   1 
ATOM   1969 N  NH2   . ARG A 1 267 ? 24.484  -18.925 8.257   1.00 28.14  ? 239 ARG A NH2   1 
ATOM   1970 N  N     . VAL A 1 268 ? 18.103  -16.418 5.575   1.00 27.92  ? 240 VAL A N     1 
ATOM   1971 C  CA    . VAL A 1 268 ? 17.451  -15.785 4.434   1.00 29.93  ? 240 VAL A CA    1 
ATOM   1972 C  C     . VAL A 1 268 ? 16.559  -14.626 4.875   1.00 33.91  ? 240 VAL A C     1 
ATOM   1973 O  O     . VAL A 1 268 ? 15.606  -14.271 4.181   1.00 32.52  ? 240 VAL A O     1 
ATOM   1974 C  CB    . VAL A 1 268 ? 16.669  -16.813 3.593   1.00 30.41  ? 240 VAL A CB    1 
ATOM   1975 C  CG1   . VAL A 1 268 ? 17.674  -17.670 2.742   1.00 33.47  ? 240 VAL A CG1   1 
ATOM   1976 C  CG2   . VAL A 1 268 ? 15.690  -17.659 4.436   1.00 31.43  ? 240 VAL A CG2   1 
ATOM   1977 N  N     . LEU A 1 269 ? 16.905  -13.990 5.985   1.00 30.31  ? 241 LEU A N     1 
ATOM   1978 C  CA    . LEU A 1 269 ? 16.208  -12.796 6.471   1.00 29.07  ? 241 LEU A CA    1 
ATOM   1979 C  C     . LEU A 1 269 ? 16.823  -11.562 5.826   1.00 26.54  ? 241 LEU A C     1 
ATOM   1980 O  O     . LEU A 1 269 ? 17.965  -11.195 6.125   1.00 28.48  ? 241 LEU A O     1 
ATOM   1981 C  CB    . LEU A 1 269 ? 16.299  -12.689 7.995   1.00 28.96  ? 241 LEU A CB    1 
ATOM   1982 C  CG    . LEU A 1 269 ? 15.720  -11.438 8.669   1.00 31.27  ? 241 LEU A CG    1 
ATOM   1983 C  CD1   . LEU A 1 269 ? 14.222  -11.277 8.296   1.00 28.85  ? 241 LEU A CD1   1 
ATOM   1984 C  CD2   . LEU A 1 269 ? 15.865  -11.486 10.220  1.00 28.87  ? 241 LEU A CD2   1 
ATOM   1985 N  N     . TYR A 1 270 ? 16.052  -10.905 4.974   1.00 28.20  ? 242 TYR A N     1 
ATOM   1986 C  CA    . TYR A 1 270 ? 16.439  -9.689  4.278   1.00 27.42  ? 242 TYR A CA    1 
ATOM   1987 C  C     . TYR A 1 270 ? 15.390  -8.620  4.530   1.00 26.74  ? 242 TYR A C     1 
ATOM   1988 O  O     . TYR A 1 270 ? 14.217  -8.926  4.733   1.00 26.41  ? 242 TYR A O     1 
ATOM   1989 C  CB    . TYR A 1 270 ? 16.536  -9.910  2.765   1.00 26.87  ? 242 TYR A CB    1 
ATOM   1990 C  CG    . TYR A 1 270 ? 17.681  -10.832 2.374   1.00 28.11  ? 242 TYR A CG    1 
ATOM   1991 C  CD1   . TYR A 1 270 ? 17.491  -12.215 2.307   1.00 33.07  ? 242 TYR A CD1   1 
ATOM   1992 C  CD2   . TYR A 1 270 ? 18.917  -10.318 2.028   1.00 30.16  ? 242 TYR A CD2   1 
ATOM   1993 C  CE1   . TYR A 1 270 ? 18.512  -13.052 1.938   1.00 31.55  ? 242 TYR A CE1   1 
ATOM   1994 C  CE2   . TYR A 1 270 ? 19.969  -11.174 1.640   1.00 34.37  ? 242 TYR A CE2   1 
ATOM   1995 C  CZ    . TYR A 1 270 ? 19.743  -12.528 1.611   1.00 36.06  ? 242 TYR A CZ    1 
ATOM   1996 O  OH    . TYR A 1 270 ? 20.737  -13.395 1.250   1.00 37.83  ? 242 TYR A OH    1 
ATOM   1997 N  N     . SER A 1 271 ? 15.814  -7.369  4.443   1.00 30.48  ? 243 SER A N     1 
ATOM   1998 C  CA    . SER A 1 271 ? 14.927  -6.259  4.722   1.00 28.92  ? 243 SER A CA    1 
ATOM   1999 C  C     . SER A 1 271 ? 15.045  -5.203  3.637   1.00 30.17  ? 243 SER A C     1 
ATOM   2000 O  O     . SER A 1 271 ? 16.113  -5.003  3.049   1.00 30.76  ? 243 SER A O     1 
ATOM   2001 C  CB    . SER A 1 271 ? 15.241  -5.661  6.084   1.00 30.93  ? 243 SER A CB    1 
ATOM   2002 O  OG    . SER A 1 271 ? 14.308  -4.649  6.401   1.00 37.18  ? 243 SER A OG    1 
ATOM   2003 N  N     . GLY A 1 272 ? 13.920  -4.567  3.341   1.00 24.77  ? 244 GLY A N     1 
ATOM   2004 C  CA    . GLY A 1 272 ? 13.890  -3.343  2.553   1.00 26.10  ? 244 GLY A CA    1 
ATOM   2005 C  C     . GLY A 1 272 ? 13.600  -2.193  3.504   1.00 30.42  ? 244 GLY A C     1 
ATOM   2006 O  O     . GLY A 1 272 ? 12.832  -2.352  4.454   1.00 30.56  ? 244 GLY A O     1 
ATOM   2007 N  N     . ILE A 1 273 ? 14.207  -1.037  3.260   1.00 21.65  ? 245 ILE A N     1 
ATOM   2008 C  CA    . ILE A 1 273 ? 14.008  0.130   4.121   1.00 24.13  ? 245 ILE A CA    1 
ATOM   2009 C  C     . ILE A 1 273 ? 13.687  1.341   3.259   1.00 26.06  ? 245 ILE A C     1 
ATOM   2010 O  O     . ILE A 1 273 ? 14.373  1.588   2.266   1.00 24.23  ? 245 ILE A O     1 
ATOM   2011 C  CB    . ILE A 1 273 ? 15.254  0.414   4.971   1.00 25.82  ? 245 ILE A CB    1 
ATOM   2012 C  CG1   . ILE A 1 273 ? 15.629  -0.814  5.805   1.00 26.58  ? 245 ILE A CG1   1 
ATOM   2013 C  CG2   . ILE A 1 273 ? 15.048  1.661   5.817   1.00 25.92  ? 245 ILE A CG2   1 
ATOM   2014 C  CD1   . ILE A 1 273 ? 16.940  -0.645  6.523   1.00 32.87  ? 245 ILE A CD1   1 
ATOM   2015 N  N     . GLY A 1 274 ? 12.668  2.097   3.638   1.00 23.18  ? 246 GLY A N     1 
ATOM   2016 C  CA    . GLY A 1 274 ? 12.363  3.349   2.961   1.00 24.64  ? 246 GLY A CA    1 
ATOM   2017 C  C     . GLY A 1 274 ? 12.256  4.468   3.971   1.00 24.35  ? 246 GLY A C     1 
ATOM   2018 O  O     . GLY A 1 274 ? 11.814  4.257   5.100   1.00 25.98  ? 246 GLY A O     1 
ATOM   2019 N  N     . LEU A 1 275 ? 12.706  5.655   3.568   1.00 25.45  ? 247 LEU A N     1 
ATOM   2020 C  CA    . LEU A 1 275 ? 12.608  6.841   4.410   1.00 22.82  ? 247 LEU A CA    1 
ATOM   2021 C  C     . LEU A 1 275 ? 11.885  7.924   3.641   1.00 27.97  ? 247 LEU A C     1 
ATOM   2022 O  O     . LEU A 1 275 ? 12.140  8.141   2.450   1.00 27.42  ? 247 LEU A O     1 
ATOM   2023 C  CB    . LEU A 1 275 ? 13.982  7.415   4.850   1.00 22.45  ? 247 LEU A CB    1 
ATOM   2024 C  CG    . LEU A 1 275 ? 15.002  6.417   5.420   1.00 26.90  ? 247 LEU A CG    1 
ATOM   2025 C  CD1   . LEU A 1 275 ? 16.335  7.155   5.584   1.00 30.25  ? 247 LEU A CD1   1 
ATOM   2026 C  CD2   . LEU A 1 275 ? 14.501  5.864   6.737   1.00 29.68  ? 247 LEU A CD2   1 
ATOM   2027 N  N     . ALA A 1 276 ? 10.996  8.609   4.323   1.00 23.53  ? 248 ALA A N     1 
ATOM   2028 C  CA    . ALA A 1 276 ? 10.323  9.741   3.720   1.00 28.22  ? 248 ALA A CA    1 
ATOM   2029 C  C     . ALA A 1 276 ? 10.172  10.804  4.791   1.00 31.85  ? 248 ALA A C     1 
ATOM   2030 O  O     . ALA A 1 276 ? 10.468  10.581  5.967   1.00 32.23  ? 248 ALA A O     1 
ATOM   2031 C  CB    . ALA A 1 276 ? 8.956   9.346   3.128   1.00 28.83  ? 248 ALA A CB    1 
ATOM   2032 N  N     . LYS A 1 277 ? 9.741   11.979  4.364   1.00 28.30  ? 249 LYS A N     1 
ATOM   2033 C  CA    . LYS A 1 277 ? 9.420   13.062  5.264   1.00 31.05  ? 249 LYS A CA    1 
ATOM   2034 C  C     . LYS A 1 277 ? 7.907   13.176  5.312   1.00 37.65  ? 249 LYS A C     1 
ATOM   2035 O  O     . LYS A 1 277 ? 7.226   13.009  4.292   1.00 34.94  ? 249 LYS A O     1 
ATOM   2036 C  CB    . LYS A 1 277 ? 10.045  14.373  4.796   1.00 31.94  ? 249 LYS A CB    1 
ATOM   2037 C  CG    . LYS A 1 277 ? 10.599  15.188  5.921   1.00 45.76  ? 249 LYS A CG    1 
ATOM   2038 C  CD    . LYS A 1 277 ? 11.704  16.100  5.471   1.00 42.29  ? 249 LYS A CD    1 
ATOM   2039 C  CE    . LYS A 1 277 ? 12.185  16.932  6.651   1.00 49.61  ? 249 LYS A CE    1 
ATOM   2040 N  NZ    . LYS A 1 277 ? 13.150  17.969  6.235   1.00 49.30  ? 249 LYS A NZ    1 
ATOM   2041 N  N     . GLY A 1 278 ? 7.377   13.388  6.504   1.00 32.56  ? 250 GLY A N     1 
ATOM   2042 C  CA    . GLY A 1 278 ? 5.941   13.516  6.634   1.00 37.57  ? 250 GLY A CA    1 
ATOM   2043 C  C     . GLY A 1 278 ? 5.595   14.474  7.748   1.00 39.44  ? 250 GLY A C     1 
ATOM   2044 O  O     . GLY A 1 278 ? 6.410   14.778  8.626   1.00 41.57  ? 250 GLY A O     1 
ATOM   2045 N  N     . LYS A 1 279 ? 4.355   14.923  7.713   1.00 39.91  ? 251 LYS A N     1 
ATOM   2046 C  CA    . LYS A 1 279 ? 3.819   15.806  8.728   1.00 40.86  ? 251 LYS A CA    1 
ATOM   2047 C  C     . LYS A 1 279 ? 3.019   14.920  9.665   1.00 35.07  ? 251 LYS A C     1 
ATOM   2048 O  O     . LYS A 1 279 ? 1.989   14.361  9.281   1.00 36.94  ? 251 LYS A O     1 
ATOM   2049 C  CB    . LYS A 1 279 ? 2.960   16.905  8.104   1.00 41.78  ? 251 LYS A CB    1 
ATOM   2050 C  CG    . LYS A 1 279 ? 2.903   18.117  9.005   1.00 58.37  ? 251 LYS A CG    1 
ATOM   2051 C  CD    . LYS A 1 279 ? 2.179   19.299  8.379   1.00 68.83  ? 251 LYS A CD    1 
ATOM   2052 C  CE    . LYS A 1 279 ? 3.170   20.458  8.188   1.00 72.99  ? 251 LYS A CE    1 
ATOM   2053 N  NZ    . LYS A 1 279 ? 4.013   20.728  9.402   1.00 64.66  ? 251 LYS A NZ    1 
ATOM   2054 N  N     . VAL A 1 280 ? 3.526   14.732  10.856  1.00 31.44  ? 252 VAL A N     1 
ATOM   2055 C  CA    A VAL A 1 280 ? 2.832   13.884  11.811  0.29 33.21  ? 252 VAL A CA    1 
ATOM   2056 C  CA    B VAL A 1 280 ? 2.910   13.887  11.864  0.71 33.11  ? 252 VAL A CA    1 
ATOM   2057 C  C     . VAL A 1 280 ? 2.106   14.774  12.805  1.00 35.86  ? 252 VAL A C     1 
ATOM   2058 O  O     . VAL A 1 280 ? 2.520   15.900  13.101  1.00 38.08  ? 252 VAL A O     1 
ATOM   2059 C  CB    A VAL A 1 280 ? 3.783   12.891  12.511  0.29 37.44  ? 252 VAL A CB    1 
ATOM   2060 C  CB    B VAL A 1 280 ? 4.008   13.102  12.604  0.71 37.88  ? 252 VAL A CB    1 
ATOM   2061 C  CG1   A VAL A 1 280 ? 4.780   12.327  11.503  0.29 33.42  ? 252 VAL A CG1   1 
ATOM   2062 C  CG1   B VAL A 1 280 ? 3.470   12.444  13.824  0.71 32.40  ? 252 VAL A CG1   1 
ATOM   2063 C  CG2   A VAL A 1 280 ? 4.487   13.539  13.684  0.29 35.20  ? 252 VAL A CG2   1 
ATOM   2064 C  CG2   B VAL A 1 280 ? 4.614   12.068  11.662  0.71 33.19  ? 252 VAL A CG2   1 
ATOM   2065 N  N     . ILE A 1 281 ? 0.967   14.282  13.276  1.00 31.11  ? 253 ILE A N     1 
ATOM   2066 C  CA    . ILE A 1 281 ? 0.170   14.982  14.274  1.00 34.23  ? 253 ILE A CA    1 
ATOM   2067 C  C     . ILE A 1 281 ? 0.358   14.263  15.602  1.00 37.83  ? 253 ILE A C     1 
ATOM   2068 O  O     . ILE A 1 281 ? 0.156   13.044  15.692  1.00 39.69  ? 253 ILE A O     1 
ATOM   2069 C  CB    . ILE A 1 281 ? -1.316  15.053  13.878  1.00 43.90  ? 253 ILE A CB    1 
ATOM   2070 C  CG1   . ILE A 1 281 ? -1.504  15.986  12.683  1.00 33.79  ? 253 ILE A CG1   1 
ATOM   2071 C  CG2   . ILE A 1 281 ? -2.160  15.544  15.057  1.00 44.24  ? 253 ILE A CG2   1 
ATOM   2072 C  CD1   . ILE A 1 281 ? -2.915  15.967  12.140  1.00 43.66  ? 253 ILE A CD1   1 
ATOM   2073 N  N     . GLU A 1 282 ? 0.774   15.008  16.621  1.00 35.56  ? 254 GLU A N     1 
ATOM   2074 C  CA    . GLU A 1 282 ? 0.891   14.492  17.973  1.00 34.68  ? 254 GLU A CA    1 
ATOM   2075 C  C     . GLU A 1 282 ? -0.250  15.061  18.799  1.00 43.29  ? 254 GLU A C     1 
ATOM   2076 O  O     . GLU A 1 282 ? -0.563  16.249  18.686  1.00 40.27  ? 254 GLU A O     1 
ATOM   2077 C  CB    . GLU A 1 282 ? 2.225   14.876  18.605  1.00 38.63  ? 254 GLU A CB    1 
ATOM   2078 C  CG    . GLU A 1 282 ? 3.443   14.503  17.772  1.00 46.26  ? 254 GLU A CG    1 
ATOM   2079 C  CD    . GLU A 1 282 ? 4.745   14.970  18.409  1.00 52.56  ? 254 GLU A CD    1 
ATOM   2080 O  OE1   . GLU A 1 282 ? 4.712   15.969  19.160  1.00 55.08  ? 254 GLU A OE1   1 
ATOM   2081 O  OE2   . GLU A 1 282 ? 5.799   14.350  18.137  1.00 50.53  ? 254 GLU A OE2   1 
ATOM   2082 N  N     . GLY A 1 283 ? -0.881  14.212  19.602  1.00 38.26  ? 255 GLY A N     1 
ATOM   2083 C  CA    . GLY A 1 283 ? -2.008  14.645  20.406  1.00 42.10  ? 255 GLY A CA    1 
ATOM   2084 C  C     . GLY A 1 283 ? -2.686  13.452  21.049  1.00 35.87  ? 255 GLY A C     1 
ATOM   2085 O  O     . GLY A 1 283 ? -2.172  12.334  21.016  1.00 41.97  ? 255 GLY A O     1 
ATOM   2086 N  N     . ASN A 1 284 ? -3.858  13.716  21.635  1.00 39.37  ? 256 ASN A N     1 
ATOM   2087 C  CA    . ASN A 1 284 ? -4.698  12.673  22.228  1.00 39.80  ? 256 ASN A CA    1 
ATOM   2088 C  C     . ASN A 1 284 ? -5.626  12.135  21.146  1.00 41.53  ? 256 ASN A C     1 
ATOM   2089 O  O     . ASN A 1 284 ? -6.725  12.650  20.931  1.00 40.48  ? 256 ASN A O     1 
ATOM   2090 C  CB    . ASN A 1 284 ? -5.491  13.223  23.407  1.00 41.75  ? 256 ASN A CB    1 
ATOM   2091 C  CG    . ASN A 1 284 ? -6.176  12.134  24.198  1.00 53.86  ? 256 ASN A CG    1 
ATOM   2092 O  OD1   . ASN A 1 284 ? -5.823  10.964  24.088  1.00 57.67  ? 256 ASN A OD1   1 
ATOM   2093 N  ND2   . ASN A 1 284 ? -7.173  12.508  24.987  1.00 55.11  ? 256 ASN A ND2   1 
ATOM   2094 N  N     . ILE A 1 285 ? -5.197  11.076  20.471  1.00 35.89  ? 257 ILE A N     1 
ATOM   2095 C  CA    . ILE A 1 285 ? -5.876  10.594  19.275  1.00 38.86  ? 257 ILE A CA    1 
ATOM   2096 C  C     . ILE A 1 285 ? -6.542  9.255   19.561  1.00 39.50  ? 257 ILE A C     1 
ATOM   2097 O  O     . ILE A 1 285 ? -5.945  8.365   20.173  1.00 38.62  ? 257 ILE A O     1 
ATOM   2098 C  CB    . ILE A 1 285 ? -4.912  10.473  18.078  1.00 41.57  ? 257 ILE A CB    1 
ATOM   2099 C  CG1   . ILE A 1 285 ? -4.468  11.866  17.611  1.00 41.02  ? 257 ILE A CG1   1 
ATOM   2100 C  CG2   . ILE A 1 285 ? -5.580  9.736   16.933  1.00 40.74  ? 257 ILE A CG2   1 
ATOM   2101 C  CD1   . ILE A 1 285 ? -3.019  11.968  17.336  1.00 48.93  ? 257 ILE A CD1   1 
ATOM   2102 N  N     . GLY A 1 286 ? -7.775  9.107   19.081  1.00 35.05  ? 258 GLY A N     1 
ATOM   2103 C  CA    . GLY A 1 286 ? -8.451  7.833   19.156  1.00 31.96  ? 258 GLY A CA    1 
ATOM   2104 C  C     . GLY A 1 286 ? -9.806  7.941   19.814  1.00 47.91  ? 258 GLY A C     1 
ATOM   2105 O  O     . GLY A 1 286 ? -10.506 8.948   19.661  1.00 44.05  ? 258 GLY A O     1 
ATOM   2106 N  N     . SER A 1 287 ? -10.181 6.911   20.567  1.00 46.98  ? 259 SER A N     1 
ATOM   2107 C  CA    . SER A 1 287 ? -11.505 6.810   21.159  1.00 47.81  ? 259 SER A CA    1 
ATOM   2108 C  C     . SER A 1 287 ? -11.384 6.481   22.635  1.00 45.87  ? 259 SER A C     1 
ATOM   2109 O  O     . SER A 1 287 ? -10.291 6.273   23.160  1.00 44.07  ? 259 SER A O     1 
ATOM   2110 C  CB    . SER A 1 287 ? -12.308 5.718   20.469  1.00 41.90  ? 259 SER A CB    1 
ATOM   2111 O  OG    . SER A 1 287 ? -11.534 4.525   20.464  1.00 47.79  ? 259 SER A OG    1 
ATOM   2112 N  N     . GLU A 1 288 ? -12.542 6.374   23.289  1.00 55.09  ? 260 GLU A N     1 
ATOM   2113 C  CA    . GLU A 1 288 ? -12.572 5.909   24.671  1.00 51.41  ? 260 GLU A CA    1 
ATOM   2114 C  C     . GLU A 1 288 ? -11.932 4.533   24.812  1.00 50.60  ? 260 GLU A C     1 
ATOM   2115 O  O     . GLU A 1 288 ? -11.316 4.237   25.841  1.00 56.53  ? 260 GLU A O     1 
ATOM   2116 C  CB    . GLU A 1 288 ? -14.018 5.877   25.187  1.00 55.97  ? 260 GLU A CB    1 
ATOM   2117 N  N     . LEU A 1 289 ? -12.042 3.689   23.787  1.00 47.81  ? 261 LEU A N     1 
ATOM   2118 C  CA    . LEU A 1 289 ? -11.549 2.323   23.905  1.00 49.27  ? 261 LEU A CA    1 
ATOM   2119 C  C     . LEU A 1 289 ? -10.056 2.202   23.613  1.00 48.79  ? 261 LEU A C     1 
ATOM   2120 O  O     . LEU A 1 289 ? -9.402  1.305   24.154  1.00 51.68  ? 261 LEU A O     1 
ATOM   2121 C  CB    . LEU A 1 289 ? -12.342 1.396   22.976  1.00 51.98  ? 261 LEU A CB    1 
ATOM   2122 N  N     . LYS A 1 290 ? -9.490  3.072   22.778  1.00 45.12  ? 262 LYS A N     1 
ATOM   2123 C  CA    A LYS A 1 290 ? -8.095  2.924   22.384  0.63 42.05  ? 262 LYS A CA    1 
ATOM   2124 C  CA    B LYS A 1 290 ? -8.097  2.922   22.377  0.37 42.13  ? 262 LYS A CA    1 
ATOM   2125 C  C     . LYS A 1 290 ? -7.531  4.283   22.007  1.00 39.14  ? 262 LYS A C     1 
ATOM   2126 O  O     . LYS A 1 290 ? -8.129  5.012   21.211  1.00 35.98  ? 262 LYS A O     1 
ATOM   2127 C  CB    A LYS A 1 290 ? -7.957  1.941   21.213  0.63 45.50  ? 262 LYS A CB    1 
ATOM   2128 C  CB    B LYS A 1 290 ? -7.977  1.949   21.197  0.37 45.48  ? 262 LYS A CB    1 
ATOM   2129 C  CG    A LYS A 1 290 ? -6.559  1.836   20.625  0.63 47.22  ? 262 LYS A CG    1 
ATOM   2130 C  CG    B LYS A 1 290 ? -6.559  1.666   20.747  0.37 46.98  ? 262 LYS A CG    1 
ATOM   2131 C  CD    A LYS A 1 290 ? -5.540  1.406   21.671  0.63 49.66  ? 262 LYS A CD    1 
ATOM   2132 C  CD    B LYS A 1 290 ? -6.549  0.898   19.436  0.37 42.18  ? 262 LYS A CD    1 
ATOM   2133 C  CE    A LYS A 1 290 ? -4.219  1.002   21.026  0.63 47.53  ? 262 LYS A CE    1 
ATOM   2134 C  CE    B LYS A 1 290 ? -5.126  0.552   19.023  0.37 39.95  ? 262 LYS A CE    1 
ATOM   2135 N  NZ    A LYS A 1 290 ? -3.309  2.164   20.860  0.63 46.35  ? 262 LYS A NZ    1 
ATOM   2136 N  NZ    B LYS A 1 290 ? -4.523  -0.464  19.923  0.37 53.08  ? 262 LYS A NZ    1 
ATOM   2137 N  N     . ARG A 1 291 ? -6.392  4.619   22.585  1.00 35.62  ? 263 ARG A N     1 
ATOM   2138 C  CA    . ARG A 1 291 ? -5.734  5.882   22.326  1.00 41.93  ? 263 ARG A CA    1 
ATOM   2139 C  C     . ARG A 1 291 ? -4.373  5.655   21.694  1.00 39.98  ? 263 ARG A C     1 
ATOM   2140 O  O     . ARG A 1 291 ? -3.734  4.614   21.873  1.00 41.49  ? 263 ARG A O     1 
ATOM   2141 C  CB    . ARG A 1 291 ? -5.565  6.709   23.605  1.00 43.73  ? 263 ARG A CB    1 
ATOM   2142 C  CG    . ARG A 1 291 ? -6.898  7.090   24.230  1.00 47.52  ? 263 ARG A CG    1 
ATOM   2143 C  CD    . ARG A 1 291 ? -7.308  8.455   23.770  1.00 48.04  ? 263 ARG A CD    1 
ATOM   2144 N  NE    . ARG A 1 291 ? -8.568  8.904   24.351  1.00 58.64  ? 263 ARG A NE    1 
ATOM   2145 C  CZ    . ARG A 1 291 ? -9.415  9.731   23.749  1.00 65.02  ? 263 ARG A CZ    1 
ATOM   2146 N  NH1   . ARG A 1 291 ? -9.115  10.315  22.598  1.00 56.90  ? 263 ARG A NH1   1 
ATOM   2147 N  NH2   . ARG A 1 291 ? -10.581 10.001  24.329  1.00 72.31  ? 263 ARG A NH2   1 
ATOM   2148 N  N     . ASP A 1 292 ? -3.951  6.665   20.958  1.00 39.05  ? 264 ASP A N     1 
ATOM   2149 C  CA    A ASP A 1 292 ? -2.627  6.723   20.375  0.62 40.11  ? 264 ASP A CA    1 
ATOM   2150 C  CA    B ASP A 1 292 ? -2.627  6.729   20.367  0.38 40.13  ? 264 ASP A CA    1 
ATOM   2151 C  C     . ASP A 1 292 ? -2.090  8.128   20.599  1.00 37.82  ? 264 ASP A C     1 
ATOM   2152 O  O     . ASP A 1 292 ? -2.847  9.066   20.868  1.00 34.91  ? 264 ASP A O     1 
ATOM   2153 C  CB    A ASP A 1 292 ? -2.671  6.378   18.879  0.62 42.31  ? 264 ASP A CB    1 
ATOM   2154 C  CB    B ASP A 1 292 ? -2.645  6.410   18.862  0.38 42.31  ? 264 ASP A CB    1 
ATOM   2155 C  CG    A ASP A 1 292 ? -1.392  5.740   18.379  0.62 44.05  ? 264 ASP A CG    1 
ATOM   2156 C  CG    B ASP A 1 292 ? -2.472  4.933   18.569  0.38 43.74  ? 264 ASP A CG    1 
ATOM   2157 O  OD1   A ASP A 1 292 ? -0.291  6.130   18.838  0.62 47.15  ? 264 ASP A OD1   1 
ATOM   2158 O  OD1   B ASP A 1 292 ? -2.103  4.179   19.494  0.38 46.03  ? 264 ASP A OD1   1 
ATOM   2159 O  OD2   A ASP A 1 292 ? -1.498  4.858   17.495  0.62 41.74  ? 264 ASP A OD2   1 
ATOM   2160 O  OD2   B ASP A 1 292 ? -2.699  4.528   17.408  0.38 44.86  ? 264 ASP A OD2   1 
ATOM   2161 N  N     . TYR A 1 293 ? -0.773  8.254   20.514  1.00 38.16  ? 265 TYR A N     1 
ATOM   2162 C  CA    . TYR A 1 293 ? -0.104  9.529   20.715  1.00 40.92  ? 265 TYR A CA    1 
ATOM   2163 C  C     . TYR A 1 293 ? 0.140   10.291  19.409  1.00 38.03  ? 265 TYR A C     1 
ATOM   2164 O  O     . TYR A 1 293 ? 0.229   11.523  19.414  1.00 39.04  ? 265 TYR A O     1 
ATOM   2165 C  CB    . TYR A 1 293 ? 1.220   9.275   21.461  1.00 38.31  ? 265 TYR A CB    1 
ATOM   2166 C  CG    . TYR A 1 293 ? 2.124   10.471  21.533  1.00 51.93  ? 265 TYR A CG    1 
ATOM   2167 C  CD1   . TYR A 1 293 ? 1.664   11.697  21.988  1.00 55.70  ? 265 TYR A CD1   1 
ATOM   2168 C  CD2   . TYR A 1 293 ? 3.434   10.390  21.076  1.00 52.43  ? 265 TYR A CD2   1 
ATOM   2169 C  CE1   . TYR A 1 293 ? 2.497   12.805  22.020  1.00 54.11  ? 265 TYR A CE1   1 
ATOM   2170 C  CE2   . TYR A 1 293 ? 4.268   11.487  21.107  1.00 56.74  ? 265 TYR A CE2   1 
ATOM   2171 C  CZ    . TYR A 1 293 ? 3.794   12.694  21.581  1.00 53.81  ? 265 TYR A CZ    1 
ATOM   2172 O  OH    . TYR A 1 293 ? 4.625   13.793  21.612  1.00 64.25  ? 265 TYR A OH    1 
ATOM   2173 N  N     . THR A 1 294 ? 0.168   9.601   18.283  1.00 33.81  ? 266 THR A N     1 
ATOM   2174 C  CA    A THR A 1 294 ? 0.568   10.227  17.040  0.54 33.76  ? 266 THR A CA    1 
ATOM   2175 C  CA    B THR A 1 294 ? 0.645   10.163  17.036  0.46 33.87  ? 266 THR A CA    1 
ATOM   2176 C  C     . THR A 1 294 ? -0.164  9.578   15.881  1.00 36.98  ? 266 THR A C     1 
ATOM   2177 O  O     . THR A 1 294 ? -0.536  8.405   15.933  1.00 42.91  ? 266 THR A O     1 
ATOM   2178 C  CB    A THR A 1 294 ? 2.075   10.114  16.824  0.54 36.52  ? 266 THR A CB    1 
ATOM   2179 C  CB    B THR A 1 294 ? 2.128   9.813   16.902  0.46 36.47  ? 266 THR A CB    1 
ATOM   2180 O  OG1   A THR A 1 294 ? 2.412   10.726  15.581  0.54 37.67  ? 266 THR A OG1   1 
ATOM   2181 O  OG1   B THR A 1 294 ? 2.948   10.773  17.597  0.46 32.82  ? 266 THR A OG1   1 
ATOM   2182 C  CG2   A THR A 1 294 ? 2.501   8.655   16.809  0.54 32.21  ? 266 THR A CG2   1 
ATOM   2183 C  CG2   B THR A 1 294 ? 2.487   9.723   15.500  0.46 37.56  ? 266 THR A CG2   1 
ATOM   2184 N  N     . ILE A 1 295 ? -0.392  10.377  14.834  1.00 31.79  ? 267 ILE A N     1 
ATOM   2185 C  CA    . ILE A 1 295 ? -1.011  9.917   13.588  1.00 40.47  ? 267 ILE A CA    1 
ATOM   2186 C  C     . ILE A 1 295 ? -0.231  10.480  12.396  1.00 36.72  ? 267 ILE A C     1 
ATOM   2187 O  O     . ILE A 1 295 ? 0.014   11.692  12.309  1.00 33.08  ? 267 ILE A O     1 
ATOM   2188 C  CB    . ILE A 1 295 ? -2.512  10.312  13.510  1.00 32.86  ? 267 ILE A CB    1 
ATOM   2189 C  CG1   . ILE A 1 295 ? -3.152  9.881   12.203  1.00 38.92  ? 267 ILE A CG1   1 
ATOM   2190 C  CG2   . ILE A 1 295 ? -2.730  11.801  13.655  1.00 39.69  ? 267 ILE A CG2   1 
ATOM   2191 C  CD1   . ILE A 1 295 ? -4.576  9.442   12.405  1.00 45.77  ? 267 ILE A CD1   1 
ATOM   2192 N  N     . LEU A 1 296 ? 0.154   9.594   11.466  1.00 34.89  ? 268 LEU A N     1 
ATOM   2193 C  CA    . LEU A 1 296 ? 0.665   9.974   10.149  1.00 32.19  ? 268 LEU A CA    1 
ATOM   2194 C  C     . LEU A 1 296 ? -0.397  9.568   9.123   1.00 30.00  ? 268 LEU A C     1 
ATOM   2195 O  O     . LEU A 1 296 ? -0.570  8.385   8.829   1.00 29.74  ? 268 LEU A O     1 
ATOM   2196 C  CB    . LEU A 1 296 ? 2.005   9.301   9.852   1.00 33.81  ? 268 LEU A CB    1 
ATOM   2197 C  CG    . LEU A 1 296 ? 2.449   9.498   8.408   1.00 32.80  ? 268 LEU A CG    1 
ATOM   2198 C  CD1   . LEU A 1 296 ? 2.790   10.970  8.143   1.00 31.97  ? 268 LEU A CD1   1 
ATOM   2199 C  CD2   . LEU A 1 296 ? 3.623   8.583   8.046   1.00 33.86  ? 268 LEU A CD2   1 
ATOM   2200 N  N     . GLY A 1 297 ? -1.132  10.545  8.609   1.00 30.81  ? 269 GLY A N     1 
ATOM   2201 C  CA    . GLY A 1 297 ? -2.163  10.234  7.633   1.00 35.18  ? 269 GLY A CA    1 
ATOM   2202 C  C     . GLY A 1 297 ? -1.589  9.518   6.423   1.00 32.34  ? 269 GLY A C     1 
ATOM   2203 O  O     . GLY A 1 297 ? -0.482  9.815   5.969   1.00 32.29  ? 269 GLY A O     1 
ATOM   2204 N  N     . ASP A 1 298 ? -2.339  8.535   5.919   1.00 30.95  ? 270 ASP A N     1 
ATOM   2205 C  CA    . ASP A 1 298 ? -1.940  7.770   4.725   1.00 33.02  ? 270 ASP A CA    1 
ATOM   2206 C  C     . ASP A 1 298 ? -0.609  7.046   4.922   1.00 31.73  ? 270 ASP A C     1 
ATOM   2207 O  O     . ASP A 1 298 ? 0.154   6.849   3.970   1.00 32.14  ? 270 ASP A O     1 
ATOM   2208 C  CB    . ASP A 1 298 ? -1.897  8.667   3.485   1.00 38.21  ? 270 ASP A CB    1 
ATOM   2209 C  CG    . ASP A 1 298 ? -3.280  9.179   3.120   1.00 37.72  ? 270 ASP A CG    1 
ATOM   2210 O  OD1   . ASP A 1 298 ? -4.242  8.410   3.323   1.00 36.22  ? 270 ASP A OD1   1 
ATOM   2211 O  OD2   . ASP A 1 298 ? -3.415  10.327  2.666   1.00 42.32  ? 270 ASP A OD2   1 
ATOM   2212 N  N     . ALA A 1 299 ? -0.322  6.673   6.177   1.00 34.04  ? 271 ALA A N     1 
ATOM   2213 C  CA    . ALA A 1 299 ? 0.872   5.883   6.482   1.00 31.33  ? 271 ALA A CA    1 
ATOM   2214 C  C     . ALA A 1 299 ? 0.882   4.594   5.673   1.00 26.25  ? 271 ALA A C     1 
ATOM   2215 O  O     . ALA A 1 299 ? 1.926   4.179   5.138   1.00 27.95  ? 271 ALA A O     1 
ATOM   2216 C  CB    . ALA A 1 299 ? 0.910   5.572   7.982   1.00 28.25  ? 271 ALA A CB    1 
ATOM   2217 N  N     . VAL A 1 300 ? -0.295  3.957   5.579   1.00 24.40  ? 272 VAL A N     1 
ATOM   2218 C  CA    . VAL A 1 300 ? -0.491  2.748   4.783   1.00 27.50  ? 272 VAL A CA    1 
ATOM   2219 C  C     . VAL A 1 300 ? 0.053   2.937   3.373   1.00 30.56  ? 272 VAL A C     1 
ATOM   2220 O  O     . VAL A 1 300 ? 0.764   2.077   2.834   1.00 27.15  ? 272 VAL A O     1 
ATOM   2221 C  CB    . VAL A 1 300 ? -1.996  2.385   4.765   1.00 29.67  ? 272 VAL A CB    1 
ATOM   2222 C  CG1   . VAL A 1 300 ? -2.363  1.642   3.529   1.00 34.07  ? 272 VAL A CG1   1 
ATOM   2223 C  CG2   . VAL A 1 300 ? -2.345  1.593   6.013   1.00 41.28  ? 272 VAL A CG2   1 
ATOM   2224 N  N     . ASN A 1 301 ? -0.300  4.053   2.743   1.00 26.08  ? 273 ASN A N     1 
ATOM   2225 C  CA    . ASN A 1 301 ? 0.042   4.245   1.333   1.00 29.52  ? 273 ASN A CA    1 
ATOM   2226 C  C     . ASN A 1 301 ? 1.518   4.570   1.145   1.00 30.54  ? 273 ASN A C     1 
ATOM   2227 O  O     . ASN A 1 301 ? 2.138   4.109   0.179   1.00 30.04  ? 273 ASN A O     1 
ATOM   2228 C  CB    . ASN A 1 301 ? -0.843  5.338   0.752   1.00 31.79  ? 273 ASN A CB    1 
ATOM   2229 C  CG    . ASN A 1 301 ? -2.295  5.134   1.147   1.00 42.31  ? 273 ASN A CG    1 
ATOM   2230 O  OD1   . ASN A 1 301 ? -2.754  5.650   2.184   1.00 33.30  ? 273 ASN A OD1   1 
ATOM   2231 N  ND2   . ASN A 1 301 ? -2.995  4.305   0.383   1.00 34.03  ? 273 ASN A ND2   1 
ATOM   2232 N  N     . VAL A 1 302 ? 2.103   5.377   2.040   1.00 28.69  ? 274 VAL A N     1 
ATOM   2233 C  CA    . VAL A 1 302 ? 3.529   5.657   1.917   1.00 25.55  ? 274 VAL A CA    1 
ATOM   2234 C  C     . VAL A 1 302 ? 4.340   4.375   2.096   1.00 26.96  ? 274 VAL A C     1 
ATOM   2235 O  O     . VAL A 1 302 ? 5.293   4.116   1.345   1.00 26.98  ? 274 VAL A O     1 
ATOM   2236 C  CB    . VAL A 1 302 ? 3.956   6.751   2.920   1.00 30.88  ? 274 VAL A CB    1 
ATOM   2237 C  CG1   . VAL A 1 302 ? 5.461   6.979   2.851   1.00 33.33  ? 274 VAL A CG1   1 
ATOM   2238 C  CG2   . VAL A 1 302 ? 3.205   8.075   2.644   1.00 29.21  ? 274 VAL A CG2   1 
ATOM   2239 N  N     . ALA A 1 303 ? 3.965   3.545   3.074   1.00 26.94  ? 275 ALA A N     1 
ATOM   2240 C  CA    . ALA A 1 303 ? 4.737   2.336   3.331   1.00 24.06  ? 275 ALA A CA    1 
ATOM   2241 C  C     . ALA A 1 303 ? 4.628   1.364   2.165   1.00 28.15  ? 275 ALA A C     1 
ATOM   2242 O  O     . ALA A 1 303 ? 5.614   0.738   1.771   1.00 26.56  ? 275 ALA A O     1 
ATOM   2243 C  CB    . ALA A 1 303 ? 4.262   1.673   4.617   1.00 23.49  ? 275 ALA A CB    1 
ATOM   2244 N  N     . ALA A 1 304 ? 3.425   1.203   1.622   1.00 27.70  ? 276 ALA A N     1 
ATOM   2245 C  CA    . ALA A 1 304 ? 3.240   0.292   0.495   1.00 27.13  ? 276 ALA A CA    1 
ATOM   2246 C  C     . ALA A 1 304 ? 4.019   0.760   -0.725  1.00 28.58  ? 276 ALA A C     1 
ATOM   2247 O  O     . ALA A 1 304 ? 4.613   -0.054  -1.447  1.00 30.99  ? 276 ALA A O     1 
ATOM   2248 C  CB    . ALA A 1 304 ? 1.745   0.158   0.178   1.00 30.12  ? 276 ALA A CB    1 
ATOM   2249 N  N     . ARG A 1 305 ? 4.073   2.076   -0.947  1.00 27.80  ? 277 ARG A N     1 
ATOM   2250 C  CA    . ARG A 1 305 ? 4.819   2.591   -2.090  1.00 28.71  ? 277 ARG A CA    1 
ATOM   2251 C  C     . ARG A 1 305 ? 6.319   2.443   -1.890  1.00 29.96  ? 277 ARG A C     1 
ATOM   2252 O  O     . ARG A 1 305 ? 7.046   2.149   -2.849  1.00 29.29  ? 277 ARG A O     1 
ATOM   2253 C  CB    . ARG A 1 305 ? 4.449   4.045   -2.353  1.00 30.98  ? 277 ARG A CB    1 
ATOM   2254 C  CG    . ARG A 1 305 ? 3.143   4.176   -3.151  1.00 37.45  ? 277 ARG A CG    1 
ATOM   2255 C  CD    . ARG A 1 305 ? 2.645   5.624   -3.142  1.00 49.28  ? 277 ARG A CD    1 
ATOM   2256 N  NE    . ARG A 1 305 ? 1.267   5.750   -3.606  1.00 59.15  ? 277 ARG A NE    1 
ATOM   2257 C  CZ    . ARG A 1 305 ? 0.340   6.493   -3.013  1.00 70.65  ? 277 ARG A CZ    1 
ATOM   2258 N  NH1   . ARG A 1 305 ? 0.615   7.222   -1.941  1.00 61.25  ? 277 ARG A NH1   1 
ATOM   2259 N  NH2   . ARG A 1 305 ? -0.894  6.512   -3.512  1.00 85.37  ? 277 ARG A NH2   1 
ATOM   2260 N  N     . LEU A 1 306 ? 6.805   2.608   -0.653  1.00 27.34  ? 278 LEU A N     1 
ATOM   2261 C  CA    . LEU A 1 306 ? 8.231   2.385   -0.415  1.00 27.37  ? 278 LEU A CA    1 
ATOM   2262 C  C     . LEU A 1 306 ? 8.591   0.900   -0.534  1.00 28.17  ? 278 LEU A C     1 
ATOM   2263 O  O     . LEU A 1 306 ? 9.633   0.566   -1.102  1.00 29.71  ? 278 LEU A O     1 
ATOM   2264 C  CB    . LEU A 1 306 ? 8.650   2.935   0.948   1.00 29.35  ? 278 LEU A CB    1 
ATOM   2265 C  CG    . LEU A 1 306 ? 8.641   4.463   1.090   1.00 30.99  ? 278 LEU A CG    1 
ATOM   2266 C  CD1   . LEU A 1 306 ? 8.703   4.880   2.553   1.00 28.85  ? 278 LEU A CD1   1 
ATOM   2267 C  CD2   . LEU A 1 306 ? 9.807   5.088   0.309   1.00 31.59  ? 278 LEU A CD2   1 
ATOM   2268 N  N     . GLU A 1 307 ? 7.751   -0.016  -0.028  1.00 27.03  ? 279 GLU A N     1 
ATOM   2269 C  CA    A GLU A 1 307 ? 8.082   -1.423  -0.250  0.63 34.14  ? 279 GLU A CA    1 
ATOM   2270 C  CA    B GLU A 1 307 ? 7.999   -1.439  -0.237  0.37 34.09  ? 279 GLU A CA    1 
ATOM   2271 C  C     . GLU A 1 307 ? 8.085   -1.757  -1.723  1.00 31.69  ? 279 GLU A C     1 
ATOM   2272 O  O     . GLU A 1 307 ? 8.871   -2.604  -2.144  1.00 31.79  ? 279 GLU A O     1 
ATOM   2273 C  CB    A GLU A 1 307 ? 7.160   -2.418  0.470   0.63 31.70  ? 279 GLU A CB    1 
ATOM   2274 C  CB    B GLU A 1 307 ? 6.886   -2.262  0.426   0.37 31.53  ? 279 GLU A CB    1 
ATOM   2275 C  CG    A GLU A 1 307 ? 6.731   -2.086  1.863   0.63 34.28  ? 279 GLU A CG    1 
ATOM   2276 C  CG    B GLU A 1 307 ? 7.084   -3.773  0.416   0.37 35.35  ? 279 GLU A CG    1 
ATOM   2277 C  CD    A GLU A 1 307 ? 6.011   -3.258  2.545   0.63 35.53  ? 279 GLU A CD    1 
ATOM   2278 C  CD    B GLU A 1 307 ? 6.397   -4.490  -0.733  0.37 40.41  ? 279 GLU A CD    1 
ATOM   2279 O  OE1   A GLU A 1 307 ? 5.607   -4.205  1.831   0.63 26.84  ? 279 GLU A OE1   1 
ATOM   2280 O  OE1   B GLU A 1 307 ? 5.700   -3.835  -1.537  0.37 44.80  ? 279 GLU A OE1   1 
ATOM   2281 O  OE2   A GLU A 1 307 ? 5.836   -3.215  3.789   0.63 29.25  ? 279 GLU A OE2   1 
ATOM   2282 O  OE2   B GLU A 1 307 ? 6.541   -5.724  -0.823  0.37 40.99  ? 279 GLU A OE2   1 
ATOM   2283 N  N     . ALA A 1 308 ? 7.245   -1.103  -2.521  1.00 32.12  ? 280 ALA A N     1 
ATOM   2284 C  CA    . ALA A 1 308 ? 7.218   -1.411  -3.941  1.00 31.98  ? 280 ALA A CA    1 
ATOM   2285 C  C     . ALA A 1 308 ? 8.494   -0.944  -4.600  1.00 32.89  ? 280 ALA A C     1 
ATOM   2286 O  O     . ALA A 1 308 ? 9.030   -1.638  -5.475  1.00 32.37  ? 280 ALA A O     1 
ATOM   2287 C  CB    . ALA A 1 308 ? 6.001   -0.770  -4.609  1.00 30.18  ? 280 ALA A CB    1 
ATOM   2288 N  N     . LEU A 1 309 ? 9.005   0.221   -4.166  1.00 27.77  ? 281 LEU A N     1 
ATOM   2289 C  CA    . LEU A 1 309 ? 10.258  0.743   -4.700  1.00 30.89  ? 281 LEU A CA    1 
ATOM   2290 C  C     . LEU A 1 309 ? 11.435  -0.180  -4.409  1.00 30.92  ? 281 LEU A C     1 
ATOM   2291 O  O     . LEU A 1 309 ? 12.278  -0.421  -5.281  1.00 34.32  ? 281 LEU A O     1 
ATOM   2292 C  CB    . LEU A 1 309 ? 10.524  2.128   -4.112  1.00 28.21  ? 281 LEU A CB    1 
ATOM   2293 C  CG    . LEU A 1 309 ? 9.805   3.224   -4.881  1.00 37.81  ? 281 LEU A CG    1 
ATOM   2294 C  CD1   . LEU A 1 309 ? 9.898   4.573   -4.131  1.00 34.06  ? 281 LEU A CD1   1 
ATOM   2295 C  CD2   . LEU A 1 309 ? 10.375  3.302   -6.294  1.00 39.88  ? 281 LEU A CD2   1 
ATOM   2296 N  N     . THR A 1 310 ? 11.543  -0.678  -3.177  1.00 29.85  ? 282 THR A N     1 
ATOM   2297 C  CA    . THR A 1 310 ? 12.709  -1.494  -2.845  1.00 29.62  ? 282 THR A CA    1 
ATOM   2298 C  C     . THR A 1 310 ? 12.722  -2.770  -3.672  1.00 39.57  ? 282 THR A C     1 
ATOM   2299 O  O     . THR A 1 310 ? 13.790  -3.231  -4.102  1.00 36.49  ? 282 THR A O     1 
ATOM   2300 C  CB    . THR A 1 310 ? 12.745  -1.831  -1.355  1.00 31.53  ? 282 THR A CB    1 
ATOM   2301 O  OG1   . THR A 1 310 ? 11.565  -2.561  -0.983  1.00 31.59  ? 282 THR A OG1   1 
ATOM   2302 C  CG2   . THR A 1 310 ? 12.840  -0.530  -0.492  1.00 28.97  ? 282 THR A CG2   1 
ATOM   2303 N  N     . ARG A 1 311 ? 11.546  -3.338  -3.937  1.00 32.17  ? 283 ARG A N     1 
ATOM   2304 C  CA    . ARG A 1 311 ? 11.487  -4.512  -4.808  1.00 35.92  ? 283 ARG A CA    1 
ATOM   2305 C  C     . ARG A 1 311 ? 11.733  -4.141  -6.264  1.00 36.76  ? 283 ARG A C     1 
ATOM   2306 O  O     . ARG A 1 311 ? 12.463  -4.839  -6.969  1.00 44.05  ? 283 ARG A O     1 
ATOM   2307 C  CB    . ARG A 1 311 ? 10.133  -5.223  -4.687  1.00 36.21  ? 283 ARG A CB    1 
ATOM   2308 C  CG    . ARG A 1 311 ? 9.585   -5.299  -3.301  1.00 43.96  ? 283 ARG A CG    1 
ATOM   2309 C  CD    . ARG A 1 311 ? 10.434  -6.158  -2.402  1.00 46.49  ? 283 ARG A CD    1 
ATOM   2310 N  NE    . ARG A 1 311 ? 9.607   -6.759  -1.360  1.00 52.36  ? 283 ARG A NE    1 
ATOM   2311 C  CZ    . ARG A 1 311 ? 9.537   -6.347  -0.102  1.00 47.20  ? 283 ARG A CZ    1 
ATOM   2312 N  NH1   . ARG A 1 311 ? 10.259  -5.326  0.334   1.00 51.08  ? 283 ARG A NH1   1 
ATOM   2313 N  NH2   . ARG A 1 311 ? 8.730   -6.987  0.743   1.00 38.08  ? 283 ARG A NH2   1 
ATOM   2314 N  N     . GLN A 1 312 ? 11.121  -3.060  -6.736  1.00 35.61  ? 284 GLN A N     1 
ATOM   2315 C  CA    . GLN A 1 312 ? 11.240  -2.679  -8.141  1.00 41.86  ? 284 GLN A CA    1 
ATOM   2316 C  C     . GLN A 1 312 ? 12.666  -2.295  -8.506  1.00 41.94  ? 284 GLN A C     1 
ATOM   2317 O  O     . GLN A 1 312 ? 13.140  -2.614  -9.605  1.00 37.94  ? 284 GLN A O     1 
ATOM   2318 C  CB    . GLN A 1 312 ? 10.259  -1.545  -8.442  1.00 43.75  ? 284 GLN A CB    1 
ATOM   2319 C  CG    . GLN A 1 312 ? 10.416  -0.863  -9.796  1.00 51.10  ? 284 GLN A CG    1 
ATOM   2320 C  CD    . GLN A 1 312 ? 10.096  0.632   -9.722  1.00 51.65  ? 284 GLN A CD    1 
ATOM   2321 O  OE1   . GLN A 1 312 ? 10.803  1.466   -10.297 1.00 50.83  ? 284 GLN A OE1   1 
ATOM   2322 N  NE2   . GLN A 1 312 ? 8.989   0.969   -9.053  1.00 54.27  ? 284 GLN A NE2   1 
ATOM   2323 N  N     . LEU A 1 313 ? 13.374  -1.637  -7.600  1.00 36.91  ? 285 LEU A N     1 
ATOM   2324 C  CA    . LEU A 1 313 ? 14.731  -1.197  -7.859  1.00 41.51  ? 285 LEU A CA    1 
ATOM   2325 C  C     . LEU A 1 313 ? 15.769  -2.199  -7.404  1.00 33.87  ? 285 LEU A C     1 
ATOM   2326 O  O     . LEU A 1 313 ? 16.956  -1.999  -7.675  1.00 35.86  ? 285 LEU A O     1 
ATOM   2327 C  CB    . LEU A 1 313 ? 15.006  0.140   -7.168  1.00 34.89  ? 285 LEU A CB    1 
ATOM   2328 C  CG    . LEU A 1 313 ? 14.072  1.264   -7.581  1.00 37.19  ? 285 LEU A CG    1 
ATOM   2329 C  CD1   . LEU A 1 313 ? 14.236  2.394   -6.584  1.00 35.15  ? 285 LEU A CD1   1 
ATOM   2330 C  CD2   . LEU A 1 313 ? 14.329  1.721   -9.005  1.00 41.74  ? 285 LEU A CD2   1 
ATOM   2331 N  N     . SER A 1 314 ? 15.364  -3.281  -6.742  1.00 33.50  ? 286 SER A N     1 
ATOM   2332 C  CA    . SER A 1 314 ? 16.324  -4.195  -6.126  1.00 43.27  ? 286 SER A CA    1 
ATOM   2333 C  C     . SER A 1 314 ? 17.340  -3.416  -5.292  1.00 43.22  ? 286 SER A C     1 
ATOM   2334 O  O     . SER A 1 314 ? 18.545  -3.658  -5.353  1.00 35.30  ? 286 SER A O     1 
ATOM   2335 C  CB    . SER A 1 314 ? 17.040  -5.060  -7.178  1.00 52.80  ? 286 SER A CB    1 
ATOM   2336 O  OG    . SER A 1 314 ? 16.122  -5.695  -8.055  1.00 53.56  ? 286 SER A OG    1 
ATOM   2337 N  N     . GLN A 1 315 ? 16.849  -2.454  -4.513  1.00 38.11  ? 287 GLN A N     1 
ATOM   2338 C  CA    . GLN A 1 315 ? 17.704  -1.637  -3.659  1.00 35.62  ? 287 GLN A CA    1 
ATOM   2339 C  C     . GLN A 1 315 ? 17.190  -1.736  -2.239  1.00 30.18  ? 287 GLN A C     1 
ATOM   2340 O  O     . GLN A 1 315 ? 16.009  -1.494  -2.005  1.00 36.74  ? 287 GLN A O     1 
ATOM   2341 C  CB    . GLN A 1 315 ? 17.704  -0.177  -4.111  1.00 37.91  ? 287 GLN A CB    1 
ATOM   2342 C  CG    . GLN A 1 315 ? 18.887  0.580   -3.580  1.00 50.02  ? 287 GLN A CG    1 
ATOM   2343 C  CD    . GLN A 1 315 ? 20.043  0.543   -4.518  1.00 37.36  ? 287 GLN A CD    1 
ATOM   2344 O  OE1   . GLN A 1 315 ? 19.879  0.226   -5.708  1.00 46.58  ? 287 GLN A OE1   1 
ATOM   2345 N  NE2   . GLN A 1 315 ? 21.227  0.869   -4.011  1.00 52.00  ? 287 GLN A NE2   1 
ATOM   2346 N  N     . ALA A 1 316 ? 18.058  -2.095  -1.295  1.00 30.28  ? 288 ALA A N     1 
ATOM   2347 C  CA    . ALA A 1 316 ? 17.581  -2.327  0.062   1.00 30.91  ? 288 ALA A CA    1 
ATOM   2348 C  C     . ALA A 1 316 ? 17.232  -1.039  0.800   1.00 27.87  ? 288 ALA A C     1 
ATOM   2349 O  O     . ALA A 1 316 ? 16.594  -1.106  1.853   1.00 34.62  ? 288 ALA A O     1 
ATOM   2350 C  CB    . ALA A 1 316 ? 18.633  -3.126  0.871   1.00 30.57  ? 288 ALA A CB    1 
ATOM   2351 N  N     . LEU A 1 317 ? 17.625  0.119   0.287   1.00 24.23  ? 289 LEU A N     1 
ATOM   2352 C  CA    . LEU A 1 317 ? 17.419  1.393   0.965   1.00 24.82  ? 289 LEU A CA    1 
ATOM   2353 C  C     . LEU A 1 317 ? 17.045  2.433   -0.076  1.00 26.06  ? 289 LEU A C     1 
ATOM   2354 O  O     . LEU A 1 317 ? 17.817  2.664   -1.010  1.00 27.99  ? 289 LEU A O     1 
ATOM   2355 C  CB    . LEU A 1 317 ? 18.699  1.853   1.698   1.00 26.86  ? 289 LEU A CB    1 
ATOM   2356 C  CG    . LEU A 1 317 ? 18.621  3.246   2.337   1.00 28.97  ? 289 LEU A CG    1 
ATOM   2357 C  CD1   . LEU A 1 317 ? 17.544  3.324   3.405   1.00 27.60  ? 289 LEU A CD1   1 
ATOM   2358 C  CD2   . LEU A 1 317 ? 19.964  3.632   2.926   1.00 31.03  ? 289 LEU A CD2   1 
ATOM   2359 N  N     . VAL A 1 318 ? 15.880  3.062   0.075   1.00 23.69  ? 290 VAL A N     1 
ATOM   2360 C  CA    . VAL A 1 318 ? 15.473  4.125   -0.828  1.00 23.17  ? 290 VAL A CA    1 
ATOM   2361 C  C     . VAL A 1 318 ? 14.939  5.257   0.028   1.00 29.16  ? 290 VAL A C     1 
ATOM   2362 O  O     . VAL A 1 318 ? 14.395  5.035   1.111   1.00 27.10  ? 290 VAL A O     1 
ATOM   2363 C  CB    . VAL A 1 318 ? 14.410  3.662   -1.868  1.00 26.92  ? 290 VAL A CB    1 
ATOM   2364 C  CG1   . VAL A 1 318 ? 14.969  2.493   -2.694  1.00 30.64  ? 290 VAL A CG1   1 
ATOM   2365 C  CG2   . VAL A 1 318 ? 13.098  3.279   -1.206  1.00 28.22  ? 290 VAL A CG2   1 
ATOM   2366 N  N     . PHE A 1 319 ? 15.098  6.477   -0.456  1.00 28.84  ? 291 PHE A N     1 
ATOM   2367 C  CA    . PHE A 1 319 ? 14.519  7.588   0.271   1.00 25.52  ? 291 PHE A CA    1 
ATOM   2368 C  C     . PHE A 1 319 ? 14.314  8.737   -0.698  1.00 28.14  ? 291 PHE A C     1 
ATOM   2369 O  O     . PHE A 1 319 ? 14.897  8.776   -1.785  1.00 30.16  ? 291 PHE A O     1 
ATOM   2370 C  CB    . PHE A 1 319 ? 15.373  8.010   1.485   1.00 24.72  ? 291 PHE A CB    1 
ATOM   2371 C  CG    . PHE A 1 319 ? 16.835  8.111   1.207   1.00 24.21  ? 291 PHE A CG    1 
ATOM   2372 C  CD1   . PHE A 1 319 ? 17.365  9.272   0.654   1.00 26.75  ? 291 PHE A CD1   1 
ATOM   2373 C  CD2   . PHE A 1 319 ? 17.682  7.061   1.528   1.00 24.71  ? 291 PHE A CD2   1 
ATOM   2374 C  CE1   . PHE A 1 319 ? 18.722  9.381   0.402   1.00 25.32  ? 291 PHE A CE1   1 
ATOM   2375 C  CE2   . PHE A 1 319 ? 19.069  7.153   1.293   1.00 27.95  ? 291 PHE A CE2   1 
ATOM   2376 C  CZ    . PHE A 1 319 ? 19.576  8.321   0.716   1.00 28.26  ? 291 PHE A CZ    1 
ATOM   2377 N  N     . SER A 1 320 ? 13.433  9.641   -0.305  1.00 29.50  ? 292 SER A N     1 
ATOM   2378 C  CA    . SER A 1 320 ? 13.049  10.747  -1.163  1.00 30.23  ? 292 SER A CA    1 
ATOM   2379 C  C     . SER A 1 320 ? 14.104  11.855  -1.148  1.00 29.96  ? 292 SER A C     1 
ATOM   2380 O  O     . SER A 1 320 ? 14.956  11.936  -0.252  1.00 29.45  ? 292 SER A O     1 
ATOM   2381 C  CB    . SER A 1 320 ? 11.724  11.321  -0.690  1.00 32.99  ? 292 SER A CB    1 
ATOM   2382 O  OG    . SER A 1 320 ? 11.924  11.866  0.604   1.00 31.99  ? 292 SER A OG    1 
ATOM   2383 N  N     . SER A 1 321 ? 13.980  12.763  -2.128  1.00 29.06  ? 293 SER A N     1 
ATOM   2384 C  CA    . SER A 1 321 ? 14.833  13.950  -2.196  1.00 31.07  ? 293 SER A CA    1 
ATOM   2385 C  C     . SER A 1 321 ? 14.729  14.797  -0.935  1.00 31.44  ? 293 SER A C     1 
ATOM   2386 O  O     . SER A 1 321 ? 15.731  15.392  -0.514  1.00 32.16  ? 293 SER A O     1 
ATOM   2387 C  CB    . SER A 1 321 ? 14.465  14.823  -3.409  1.00 30.61  ? 293 SER A CB    1 
ATOM   2388 O  OG    . SER A 1 321 ? 13.066  14.967  -3.495  1.00 40.83  ? 293 SER A OG    1 
ATOM   2389 N  N     . GLU A 1 322 ? 13.536  14.880  -0.330  1.00 27.67  ? 294 GLU A N     1 
ATOM   2390 C  CA    . GLU A 1 322 ? 13.387  15.645  0.911   1.00 36.68  ? 294 GLU A CA    1 
ATOM   2391 C  C     . GLU A 1 322 ? 14.269  15.090  2.013   1.00 33.55  ? 294 GLU A C     1 
ATOM   2392 O  O     . GLU A 1 322 ? 14.884  15.854  2.764   1.00 33.39  ? 294 GLU A O     1 
ATOM   2393 C  CB    . GLU A 1 322 ? 11.925  15.691  1.380   1.00 36.98  ? 294 GLU A CB    1 
ATOM   2394 C  CG    . GLU A 1 322 ? 10.944  16.254  0.361   1.00 46.07  ? 294 GLU A CG    1 
ATOM   2395 C  CD    . GLU A 1 322 ? 9.519   16.382  0.916   1.00 61.30  ? 294 GLU A CD    1 
ATOM   2396 O  OE1   . GLU A 1 322 ? 8.895   15.346  1.247   1.00 65.15  ? 294 GLU A OE1   1 
ATOM   2397 O  OE2   . GLU A 1 322 ? 9.030   17.524  1.039   1.00 77.90  ? 294 GLU A OE2   1 
ATOM   2398 N  N     . VAL A 1 323 ? 14.365  13.763  2.120   1.00 32.82  ? 295 VAL A N     1 
ATOM   2399 C  CA    . VAL A 1 323 ? 15.279  13.190  3.100   1.00 30.37  ? 295 VAL A CA    1 
ATOM   2400 C  C     . VAL A 1 323 ? 16.714  13.515  2.723   1.00 31.18  ? 295 VAL A C     1 
ATOM   2401 O  O     . VAL A 1 323 ? 17.518  13.951  3.558   1.00 33.18  ? 295 VAL A O     1 
ATOM   2402 C  CB    . VAL A 1 323 ? 15.059  11.671  3.230   1.00 26.82  ? 295 VAL A CB    1 
ATOM   2403 C  CG1   . VAL A 1 323 ? 16.183  11.062  4.060   1.00 28.20  ? 295 VAL A CG1   1 
ATOM   2404 C  CG2   . VAL A 1 323 ? 13.663  11.396  3.870   1.00 28.54  ? 295 VAL A CG2   1 
ATOM   2405 N  N     . LYS A 1 324 ? 17.045  13.319  1.449   1.00 29.23  ? 296 LYS A N     1 
ATOM   2406 C  CA    . LYS A 1 324 ? 18.388  13.580  0.964   1.00 30.24  ? 296 LYS A CA    1 
ATOM   2407 C  C     . LYS A 1 324 ? 18.801  15.020  1.250   1.00 38.24  ? 296 LYS A C     1 
ATOM   2408 O  O     . LYS A 1 324 ? 19.925  15.275  1.701   1.00 40.00  ? 296 LYS A O     1 
ATOM   2409 C  CB    . LYS A 1 324 ? 18.439  13.275  -0.533  1.00 29.27  ? 296 LYS A CB    1 
ATOM   2410 C  CG    . LYS A 1 324 ? 19.811  13.416  -1.165  1.00 35.99  ? 296 LYS A CG    1 
ATOM   2411 C  CD    . LYS A 1 324 ? 19.802  14.465  -2.238  1.00 38.16  ? 296 LYS A CD    1 
ATOM   2412 C  CE    . LYS A 1 324 ? 21.182  14.666  -2.822  1.00 42.28  ? 296 LYS A CE    1 
ATOM   2413 N  NZ    . LYS A 1 324 ? 21.241  16.032  -3.367  1.00 40.85  ? 296 LYS A NZ    1 
ATOM   2414 N  N     . ASN A 1 325 ? 17.882  15.967  1.053   1.00 36.61  ? 297 ASN A N     1 
ATOM   2415 C  CA    . ASN A 1 325 ? 18.180  17.378  1.241   1.00 34.07  ? 297 ASN A CA    1 
ATOM   2416 C  C     . ASN A 1 325 ? 18.213  17.791  2.705   1.00 39.71  ? 297 ASN A C     1 
ATOM   2417 O  O     . ASN A 1 325 ? 18.792  18.834  3.025   1.00 50.67  ? 297 ASN A O     1 
ATOM   2418 C  CB    . ASN A 1 325 ? 17.161  18.223  0.479   1.00 41.20  ? 297 ASN A CB    1 
ATOM   2419 C  CG    . ASN A 1 325 ? 17.345  18.123  -1.022  1.00 43.77  ? 297 ASN A CG    1 
ATOM   2420 O  OD1   . ASN A 1 325 ? 18.465  17.941  -1.512  1.00 49.18  ? 297 ASN A OD1   1 
ATOM   2421 N  ND2   . ASN A 1 325 ? 16.251  18.245  -1.761  1.00 47.60  ? 297 ASN A ND2   1 
ATOM   2422 N  N     . SER A 1 326 ? 17.622  17.003  3.599   1.00 36.94  ? 298 SER A N     1 
ATOM   2423 C  CA    . SER A 1 326 ? 17.719  17.293  5.021   1.00 37.88  ? 298 SER A CA    1 
ATOM   2424 C  C     . SER A 1 326 ? 19.000  16.768  5.644   1.00 41.02  ? 298 SER A C     1 
ATOM   2425 O  O     . SER A 1 326 ? 19.265  17.059  6.811   1.00 42.75  ? 298 SER A O     1 
ATOM   2426 C  CB    . SER A 1 326 ? 16.531  16.698  5.758   1.00 37.27  ? 298 SER A CB    1 
ATOM   2427 O  OG    . SER A 1 326 ? 15.325  17.180  5.213   1.00 49.05  ? 298 SER A OG    1 
ATOM   2428 N  N     . ALA A 1 327 ? 19.782  15.984  4.918   1.00 33.29  ? 299 ALA A N     1 
ATOM   2429 C  CA    . ALA A 1 327 ? 21.011  15.444  5.465   1.00 37.10  ? 299 ALA A CA    1 
ATOM   2430 C  C     . ALA A 1 327 ? 22.088  16.516  5.465   1.00 40.77  ? 299 ALA A C     1 
ATOM   2431 O  O     . ALA A 1 327 ? 22.109  17.382  4.592   1.00 44.00  ? 299 ALA A O     1 
ATOM   2432 C  CB    . ALA A 1 327 ? 21.474  14.243  4.637   1.00 36.88  ? 299 ALA A CB    1 
ATOM   2433 N  N     . THR A 1 328 ? 22.993  16.443  6.441   1.00 36.04  ? 300 THR A N     1 
ATOM   2434 C  CA    . THR A 1 328 ? 24.153  17.334  6.475   1.00 39.46  ? 300 THR A CA    1 
ATOM   2435 C  C     . THR A 1 328 ? 25.465  16.651  6.119   1.00 43.83  ? 300 THR A C     1 
ATOM   2436 O  O     . THR A 1 328 ? 26.359  17.311  5.590   1.00 51.79  ? 300 THR A O     1 
ATOM   2437 C  CB    . THR A 1 328 ? 24.311  18.002  7.853   1.00 41.06  ? 300 THR A CB    1 
ATOM   2438 O  OG1   . THR A 1 328 ? 24.663  17.025  8.837   1.00 49.79  ? 300 THR A OG1   1 
ATOM   2439 C  CG2   . THR A 1 328 ? 23.057  18.681  8.277   1.00 37.53  ? 300 THR A CG2   1 
ATOM   2440 N  N     . LYS A 1 329 ? 25.621  15.360  6.379   1.00 42.15  ? 301 LYS A N     1 
ATOM   2441 C  CA    A LYS A 1 329 ? 26.877  14.693  6.071   0.49 39.83  ? 301 LYS A CA    1 
ATOM   2442 C  CA    B LYS A 1 329 ? 26.897  14.741  6.066   0.51 39.80  ? 301 LYS A CA    1 
ATOM   2443 C  C     . LYS A 1 329 ? 27.010  14.479  4.565   1.00 38.71  ? 301 LYS A C     1 
ATOM   2444 O  O     . LYS A 1 329 ? 26.030  14.533  3.815   1.00 40.98  ? 301 LYS A O     1 
ATOM   2445 C  CB    A LYS A 1 329 ? 26.966  13.351  6.803   0.49 43.53  ? 301 LYS A CB    1 
ATOM   2446 C  CB    B LYS A 1 329 ? 27.090  13.442  6.859   0.51 43.54  ? 301 LYS A CB    1 
ATOM   2447 C  CG    A LYS A 1 329 ? 27.005  13.448  8.323   0.49 47.41  ? 301 LYS A CG    1 
ATOM   2448 C  CG    B LYS A 1 329 ? 26.989  13.599  8.380   0.51 47.35  ? 301 LYS A CG    1 
ATOM   2449 C  CD    A LYS A 1 329 ? 27.926  14.552  8.806   0.49 45.58  ? 301 LYS A CD    1 
ATOM   2450 C  CD    B LYS A 1 329 ? 26.926  12.237  9.076   0.51 48.91  ? 301 LYS A CD    1 
ATOM   2451 C  CE    A LYS A 1 329 ? 28.537  14.188  10.157  0.49 56.83  ? 301 LYS A CE    1 
ATOM   2452 C  CE    B LYS A 1 329 ? 26.658  12.363  10.571  0.51 54.54  ? 301 LYS A CE    1 
ATOM   2453 N  NZ    A LYS A 1 329 ? 29.660  15.094  10.540  0.49 58.05  ? 301 LYS A NZ    1 
ATOM   2454 N  NZ    B LYS A 1 329 ? 27.812  11.896  11.391  0.51 62.38  ? 301 LYS A NZ    1 
ATOM   2455 N  N     . SER A 1 330 ? 28.238  14.218  4.129   1.00 37.27  ? 302 SER A N     1 
ATOM   2456 C  CA    A SER A 1 330 ? 28.528  14.024  2.709   0.49 41.20  ? 302 SER A CA    1 
ATOM   2457 C  CA    B SER A 1 330 ? 28.545  14.019  2.712   0.51 41.20  ? 302 SER A CA    1 
ATOM   2458 C  C     . SER A 1 330 ? 28.375  12.544  2.350   1.00 40.35  ? 302 SER A C     1 
ATOM   2459 O  O     . SER A 1 330 ? 29.324  11.844  1.999   1.00 41.11  ? 302 SER A O     1 
ATOM   2460 C  CB    A SER A 1 330 ? 29.916  14.551  2.374   0.49 43.64  ? 302 SER A CB    1 
ATOM   2461 C  CB    B SER A 1 330 ? 29.957  14.492  2.398   0.51 43.63  ? 302 SER A CB    1 
ATOM   2462 O  OG    A SER A 1 330 ? 29.913  15.968  2.394   0.49 44.08  ? 302 SER A OG    1 
ATOM   2463 O  OG    B SER A 1 330 ? 30.912  13.674  3.055   0.51 47.71  ? 302 SER A OG    1 
ATOM   2464 N  N     . TRP A 1 331 ? 27.127  12.083  2.430   1.00 33.36  ? 303 TRP A N     1 
ATOM   2465 C  CA    . TRP A 1 331 ? 26.818  10.702  2.078   1.00 33.10  ? 303 TRP A CA    1 
ATOM   2466 C  C     . TRP A 1 331 ? 27.081  10.440  0.598   1.00 29.34  ? 303 TRP A C     1 
ATOM   2467 O  O     . TRP A 1 331 ? 26.967  11.331  -0.243  1.00 30.61  ? 303 TRP A O     1 
ATOM   2468 C  CB    . TRP A 1 331 ? 25.353  10.397  2.382   1.00 28.79  ? 303 TRP A CB    1 
ATOM   2469 C  CG    . TRP A 1 331 ? 24.967  10.514  3.837   1.00 25.61  ? 303 TRP A CG    1 
ATOM   2470 C  CD1   . TRP A 1 331 ? 24.301  11.553  4.416   1.00 32.81  ? 303 TRP A CD1   1 
ATOM   2471 C  CD2   . TRP A 1 331 ? 25.223  9.563   4.883   1.00 30.69  ? 303 TRP A CD2   1 
ATOM   2472 N  NE1   . TRP A 1 331 ? 24.116  11.305  5.758   1.00 31.74  ? 303 TRP A NE1   1 
ATOM   2473 C  CE2   . TRP A 1 331 ? 24.670  10.086  6.067   1.00 32.88  ? 303 TRP A CE2   1 
ATOM   2474 C  CE3   . TRP A 1 331 ? 25.869  8.319   4.930   1.00 30.27  ? 303 TRP A CE3   1 
ATOM   2475 C  CZ2   . TRP A 1 331 ? 24.729  9.408   7.284   1.00 32.71  ? 303 TRP A CZ2   1 
ATOM   2476 C  CZ3   . TRP A 1 331 ? 25.919  7.644   6.126   1.00 34.15  ? 303 TRP A CZ3   1 
ATOM   2477 C  CH2   . TRP A 1 331 ? 25.361  8.193   7.296   1.00 35.99  ? 303 TRP A CH2   1 
ATOM   2478 N  N     . ASN A 1 332 ? 27.363  9.182   0.264   1.00 31.61  ? 304 ASN A N     1 
ATOM   2479 C  CA    . ASN A 1 332 ? 27.527  8.804   -1.139  1.00 26.46  ? 304 ASN A CA    1 
ATOM   2480 C  C     . ASN A 1 332 ? 26.162  8.551   -1.790  1.00 27.12  ? 304 ASN A C     1 
ATOM   2481 O  O     . ASN A 1 332 ? 25.784  7.426   -2.118  1.00 32.63  ? 304 ASN A O     1 
ATOM   2482 C  CB    . ASN A 1 332 ? 28.436  7.596   -1.258  1.00 32.62  ? 304 ASN A CB    1 
ATOM   2483 C  CG    . ASN A 1 332 ? 29.786  7.842   -0.621  1.00 41.04  ? 304 ASN A CG    1 
ATOM   2484 O  OD1   . ASN A 1 332 ? 30.330  8.943   -0.713  1.00 41.00  ? 304 ASN A OD1   1 
ATOM   2485 N  ND2   . ASN A 1 332 ? 30.289  6.853   0.100   1.00 38.71  ? 304 ASN A ND2   1 
ATOM   2486 N  N     . PHE A 1 333 ? 25.444  9.647   -2.028  1.00 28.66  ? 305 PHE A N     1 
ATOM   2487 C  CA    . PHE A 1 333 ? 24.117  9.591   -2.634  1.00 27.09  ? 305 PHE A CA    1 
ATOM   2488 C  C     . PHE A 1 333 ? 24.171  9.099   -4.071  1.00 32.08  ? 305 PHE A C     1 
ATOM   2489 O  O     . PHE A 1 333 ? 25.061  9.467   -4.841  1.00 29.53  ? 305 PHE A O     1 
ATOM   2490 C  CB    . PHE A 1 333 ? 23.490  10.977  -2.636  1.00 27.85  ? 305 PHE A CB    1 
ATOM   2491 C  CG    . PHE A 1 333 ? 23.171  11.494  -1.283  1.00 28.08  ? 305 PHE A CG    1 
ATOM   2492 C  CD1   . PHE A 1 333 ? 22.276  10.832  -0.458  1.00 27.95  ? 305 PHE A CD1   1 
ATOM   2493 C  CD2   . PHE A 1 333 ? 23.791  12.641  -0.820  1.00 29.92  ? 305 PHE A CD2   1 
ATOM   2494 C  CE1   . PHE A 1 333 ? 21.977  11.331  0.805   1.00 33.35  ? 305 PHE A CE1   1 
ATOM   2495 C  CE2   . PHE A 1 333 ? 23.495  13.148  0.440   1.00 31.19  ? 305 PHE A CE2   1 
ATOM   2496 C  CZ    . PHE A 1 333 ? 22.591  12.502  1.245   1.00 30.15  ? 305 PHE A CZ    1 
ATOM   2497 N  N     . ILE A 1 334 ? 23.165  8.313   -4.464  1.00 26.74  ? 306 ILE A N     1 
ATOM   2498 C  CA    . ILE A 1 334 ? 22.984  7.969   -5.867  1.00 22.36  ? 306 ILE A CA    1 
ATOM   2499 C  C     . ILE A 1 334 ? 21.522  8.166   -6.234  1.00 30.13  ? 306 ILE A C     1 
ATOM   2500 O  O     . ILE A 1 334 ? 20.630  7.688   -5.526  1.00 29.42  ? 306 ILE A O     1 
ATOM   2501 C  CB    . ILE A 1 334 ? 23.457  6.534   -6.200  1.00 28.29  ? 306 ILE A CB    1 
ATOM   2502 C  CG1   . ILE A 1 334 ? 23.244  6.261   -7.692  1.00 29.65  ? 306 ILE A CG1   1 
ATOM   2503 C  CG2   . ILE A 1 334 ? 22.829  5.458   -5.278  1.00 25.55  ? 306 ILE A CG2   1 
ATOM   2504 C  CD1   . ILE A 1 334 ? 23.862  4.958   -8.170  1.00 36.90  ? 306 ILE A CD1   1 
ATOM   2505 N  N     . TRP A 1 335 ? 21.276  8.893   -7.321  1.00 25.67  ? 307 TRP A N     1 
ATOM   2506 C  CA    . TRP A 1 335 ? 19.924  9.061   -7.847  1.00 27.34  ? 307 TRP A CA    1 
ATOM   2507 C  C     . TRP A 1 335 ? 19.480  7.783   -8.555  1.00 32.94  ? 307 TRP A C     1 
ATOM   2508 O  O     . TRP A 1 335 ? 20.243  7.215   -9.339  1.00 31.36  ? 307 TRP A O     1 
ATOM   2509 C  CB    . TRP A 1 335 ? 19.873  10.230  -8.831  1.00 27.50  ? 307 TRP A CB    1 
ATOM   2510 C  CG    . TRP A 1 335 ? 18.506  10.399  -9.436  1.00 31.68  ? 307 TRP A CG    1 
ATOM   2511 C  CD1   . TRP A 1 335 ? 17.491  11.133  -8.937  1.00 27.13  ? 307 TRP A CD1   1 
ATOM   2512 C  CD2   . TRP A 1 335 ? 18.017  9.810   -10.656 1.00 29.39  ? 307 TRP A CD2   1 
ATOM   2513 N  NE1   . TRP A 1 335 ? 16.395  11.056  -9.765  1.00 32.10  ? 307 TRP A NE1   1 
ATOM   2514 C  CE2   . TRP A 1 335 ? 16.692  10.239  -10.822 1.00 29.90  ? 307 TRP A CE2   1 
ATOM   2515 C  CE3   . TRP A 1 335 ? 18.580  8.964   -11.621 1.00 31.57  ? 307 TRP A CE3   1 
ATOM   2516 C  CZ2   . TRP A 1 335 ? 15.908  9.857   -11.917 1.00 35.27  ? 307 TRP A CZ2   1 
ATOM   2517 C  CZ3   . TRP A 1 335 ? 17.804  8.569   -12.692 1.00 32.78  ? 307 TRP A CZ3   1 
ATOM   2518 C  CH2   . TRP A 1 335 ? 16.476  9.014   -12.835 1.00 28.88  ? 307 TRP A CH2   1 
ATOM   2519 N  N     . LEU A 1 336 ? 18.258  7.323   -8.284  1.00 27.59  ? 308 LEU A N     1 
ATOM   2520 C  CA    . LEU A 1 336 ? 17.784  6.073   -8.877  1.00 27.72  ? 308 LEU A CA    1 
ATOM   2521 C  C     . LEU A 1 336 ? 16.680  6.259   -9.905  1.00 29.69  ? 308 LEU A C     1 
ATOM   2522 O  O     . LEU A 1 336 ? 16.780  5.701   -10.998 1.00 29.15  ? 308 LEU A O     1 
ATOM   2523 C  CB    . LEU A 1 336 ? 17.293  5.094   -7.799  1.00 32.80  ? 308 LEU A CB    1 
ATOM   2524 C  CG    . LEU A 1 336 ? 18.365  4.669   -6.793  1.00 33.13  ? 308 LEU A CG    1 
ATOM   2525 C  CD1   . LEU A 1 336 ? 17.788  3.775   -5.702  1.00 34.13  ? 308 LEU A CD1   1 
ATOM   2526 C  CD2   . LEU A 1 336 ? 19.536  3.979   -7.521  1.00 32.55  ? 308 LEU A CD2   1 
ATOM   2527 N  N     . THR A 1 337 ? 15.616  6.992   -9.575  1.00 27.21  ? 309 THR A N     1 
ATOM   2528 C  CA    . THR A 1 337 ? 14.404  7.001   -10.384 1.00 28.42  ? 309 THR A CA    1 
ATOM   2529 C  C     . THR A 1 337 ? 13.496  8.095   -9.837  1.00 33.69  ? 309 THR A C     1 
ATOM   2530 O  O     . THR A 1 337 ? 13.784  8.710   -8.807  1.00 30.12  ? 309 THR A O     1 
ATOM   2531 C  CB    . THR A 1 337 ? 13.682  5.639   -10.354 1.00 32.47  ? 309 THR A CB    1 
ATOM   2532 O  OG1   . THR A 1 337 ? 12.686  5.594   -11.381 1.00 30.97  ? 309 THR A OG1   1 
ATOM   2533 C  CG2   . THR A 1 337 ? 12.982  5.430   -8.994  1.00 30.42  ? 309 THR A CG2   1 
ATOM   2534 N  N     . ASP A 1 338 ? 12.398  8.335   -10.549 1.00 29.98  ? 310 ASP A N     1 
ATOM   2535 C  CA    . ASP A 1 338 ? 11.305  9.150   -10.059 1.00 27.48  ? 310 ASP A CA    1 
ATOM   2536 C  C     . ASP A 1 338 ? 10.188  8.237   -9.577  1.00 34.08  ? 310 ASP A C     1 
ATOM   2537 O  O     . ASP A 1 338 ? 9.972   7.157   -10.125 1.00 31.22  ? 310 ASP A O     1 
ATOM   2538 C  CB    . ASP A 1 338 ? 10.742  10.072  -11.135 1.00 29.86  ? 310 ASP A CB    1 
ATOM   2539 C  CG    . ASP A 1 338 ? 11.516  11.360  -11.264 1.00 31.60  ? 310 ASP A CG    1 
ATOM   2540 O  OD1   . ASP A 1 338 ? 12.618  11.331  -11.858 1.00 30.65  ? 310 ASP A OD1   1 
ATOM   2541 O  OD2   . ASP A 1 338 ? 10.997  12.394  -10.782 1.00 32.45  ? 310 ASP A OD2   1 
ATOM   2542 N  N     . SER A 1 339 ? 9.479   8.675   -8.550  1.00 32.06  ? 311 SER A N     1 
ATOM   2543 C  CA    . SER A 1 339 ? 8.344   7.906   -8.074  1.00 29.40  ? 311 SER A CA    1 
ATOM   2544 C  C     . SER A 1 339 ? 7.330   8.856   -7.454  1.00 33.66  ? 311 SER A C     1 
ATOM   2545 O  O     . SER A 1 339 ? 7.536   10.067  -7.387  1.00 36.70  ? 311 SER A O     1 
ATOM   2546 C  CB    . SER A 1 339 ? 8.766   6.820   -7.078  1.00 38.55  ? 311 SER A CB    1 
ATOM   2547 O  OG    . SER A 1 339 ? 7.701   5.883   -6.891  1.00 36.39  ? 311 SER A OG    1 
ATOM   2548 N  N     . GLU A 1 340 ? 6.203   8.287   -7.053  1.00 35.51  ? 312 GLU A N     1 
ATOM   2549 C  CA    . GLU A 1 340 ? 5.134   9.006   -6.378  1.00 39.80  ? 312 GLU A CA    1 
ATOM   2550 C  C     . GLU A 1 340 ? 4.982   8.354   -5.015  1.00 36.26  ? 312 GLU A C     1 
ATOM   2551 O  O     . GLU A 1 340 ? 4.816   7.138   -4.933  1.00 41.50  ? 312 GLU A O     1 
ATOM   2552 C  CB    . GLU A 1 340 ? 3.838   8.911   -7.186  1.00 42.88  ? 312 GLU A CB    1 
ATOM   2553 C  CG    . GLU A 1 340 ? 2.586   9.457   -6.505  1.00 64.87  ? 312 GLU A CG    1 
ATOM   2554 C  CD    . GLU A 1 340 ? 1.321   9.146   -7.308  1.00 73.58  ? 312 GLU A CD    1 
ATOM   2555 O  OE1   . GLU A 1 340 ? 0.792   8.021   -7.173  1.00 72.41  ? 312 GLU A OE1   1 
ATOM   2556 O  OE2   . GLU A 1 340 ? 0.860   10.016  -8.080  1.00 76.68  ? 312 GLU A OE2   1 
ATOM   2557 N  N     . LEU A 1 341 ? 5.089   9.136   -3.952  1.00 36.09  ? 313 LEU A N     1 
ATOM   2558 C  CA    . LEU A 1 341 ? 4.992   8.558   -2.617  1.00 44.51  ? 313 LEU A CA    1 
ATOM   2559 C  C     . LEU A 1 341 ? 3.720   8.950   -1.893  1.00 53.43  ? 313 LEU A C     1 
ATOM   2560 O  O     . LEU A 1 341 ? 3.117   8.117   -1.210  1.00 46.03  ? 313 LEU A O     1 
ATOM   2561 C  CB    . LEU A 1 341 ? 6.193   8.952   -1.753  1.00 43.87  ? 313 LEU A CB    1 
ATOM   2562 C  CG    . LEU A 1 341 ? 7.536   8.346   -2.123  1.00 42.03  ? 313 LEU A CG    1 
ATOM   2563 C  CD1   . LEU A 1 341 ? 8.563   8.700   -1.055  1.00 42.02  ? 313 LEU A CD1   1 
ATOM   2564 C  CD2   . LEU A 1 341 ? 7.421   6.839   -2.315  1.00 41.35  ? 313 LEU A CD2   1 
ATOM   2565 N  N     . LYS A 1 342 ? 3.307   10.196  -2.018  1.00 53.23  ? 314 LYS A N     1 
ATOM   2566 C  CA    . LYS A 1 342 ? 2.016   10.617  -1.510  1.00 65.24  ? 314 LYS A CA    1 
ATOM   2567 C  C     . LYS A 1 342 ? 1.011   10.522  -2.650  1.00 79.66  ? 314 LYS A C     1 
ATOM   2568 O  O     . LYS A 1 342 ? 1.374   10.632  -3.828  1.00 81.98  ? 314 LYS A O     1 
ATOM   2569 C  CB    . LYS A 1 342 ? 2.105   12.040  -0.967  1.00 69.38  ? 314 LYS A CB    1 
ATOM   2570 C  CG    . LYS A 1 342 ? 3.446   12.324  -0.275  1.00 69.62  ? 314 LYS A CG    1 
ATOM   2571 C  CD    . LYS A 1 342 ? 3.411   11.990  1.209   1.00 74.89  ? 314 LYS A CD    1 
ATOM   2572 C  CE    . LYS A 1 342 ? 4.026   13.096  2.075   1.00 78.50  ? 314 LYS A CE    1 
ATOM   2573 N  NZ    . LYS A 1 342 ? 5.444   13.425  1.715   1.00 67.89  ? 314 LYS A NZ    1 
ATOM   2574 N  N     . GLY A 1 343 ? -0.256  10.302  -2.297  1.00 78.85  ? 315 GLY A N     1 
ATOM   2575 C  CA    . GLY A 1 343 ? -1.297  10.171  -3.312  1.00 90.23  ? 315 GLY A CA    1 
ATOM   2576 C  C     . GLY A 1 343 ? -1.361  11.316  -4.309  1.00 85.44  ? 315 GLY A C     1 
ATOM   2577 O  O     . GLY A 1 343 ? -2.008  11.174  -5.355  1.00 83.28  ? 315 GLY A O     1 
ATOM   2578 N  N     . LYS A 1 344 ? -0.715  12.437  -4.007  1.00 82.98  ? 316 LYS A N     1 
ATOM   2579 C  CA    . LYS A 1 344 ? -0.622  13.552  -4.936  1.00 82.65  ? 316 LYS A CA    1 
ATOM   2580 C  C     . LYS A 1 344 ? 0.258   13.175  -6.123  1.00 82.23  ? 316 LYS A C     1 
ATOM   2581 O  O     . LYS A 1 344 ? 1.223   12.417  -5.992  1.00 83.76  ? 316 LYS A O     1 
ATOM   2582 C  CB    . LYS A 1 344 ? -0.058  14.775  -4.212  1.00 87.73  ? 316 LYS A CB    1 
ATOM   2583 C  CG    . LYS A 1 344 ? -0.684  14.970  -2.827  1.00 89.90  ? 316 LYS A CG    1 
ATOM   2584 C  CD    . LYS A 1 344 ? 0.370   15.063  -1.735  1.00 86.18  ? 316 LYS A CD    1 
ATOM   2585 C  CE    . LYS A 1 344 ? -0.197  15.649  -0.441  1.00 92.17  ? 316 LYS A CE    1 
ATOM   2586 N  NZ    . LYS A 1 344 ? 0.796   15.578  0.691   1.00 87.63  ? 316 LYS A NZ    1 
ATOM   2587 N  N     . SER A 1 345 ? -0.079  13.720  -7.291  1.00 74.09  ? 317 SER A N     1 
ATOM   2588 C  CA    . SER A 1 345 ? 0.595   13.345  -8.528  1.00 75.33  ? 317 SER A CA    1 
ATOM   2589 C  C     . SER A 1 345 ? 1.936   14.050  -8.685  1.00 75.44  ? 317 SER A C     1 
ATOM   2590 O  O     . SER A 1 345 ? 2.318   14.420  -9.801  1.00 73.25  ? 317 SER A O     1 
ATOM   2591 C  CB    . SER A 1 345 ? -0.287  13.665  -9.730  1.00 76.20  ? 317 SER A CB    1 
ATOM   2592 O  OG    . SER A 1 345 ? -0.546  15.057  -9.778  1.00 79.03  ? 317 SER A OG    1 
ATOM   2593 N  N     . GLU A 1 346 ? 2.659   14.243  -7.586  1.00 68.46  ? 318 GLU A N     1 
ATOM   2594 C  CA    . GLU A 1 346 ? 3.950   14.912  -7.625  1.00 66.77  ? 318 GLU A CA    1 
ATOM   2595 C  C     . GLU A 1 346 ? 5.057   13.874  -7.796  1.00 58.67  ? 318 GLU A C     1 
ATOM   2596 O  O     . GLU A 1 346 ? 5.103   12.882  -7.060  1.00 57.98  ? 318 GLU A O     1 
ATOM   2597 C  CB    . GLU A 1 346 ? 4.163   15.731  -6.352  1.00 68.07  ? 318 GLU A CB    1 
ATOM   2598 C  CG    . GLU A 1 346 ? 5.207   16.845  -6.459  1.00 79.43  ? 318 GLU A CG    1 
ATOM   2599 C  CD    . GLU A 1 346 ? 5.258   17.515  -7.836  1.00 90.56  ? 318 GLU A CD    1 
ATOM   2600 O  OE1   . GLU A 1 346 ? 5.800   16.913  -8.799  1.00 82.11  ? 318 GLU A OE1   1 
ATOM   2601 O  OE2   . GLU A 1 346 ? 4.746   18.655  -7.951  1.00 95.10  ? 318 GLU A OE2   1 
ATOM   2602 N  N     . SER A 1 347 ? 5.944   14.100  -8.766  1.00 40.77  ? 319 SER A N     1 
ATOM   2603 C  CA    . SER A 1 347 ? 6.966   13.121  -9.116  1.00 42.46  ? 319 SER A CA    1 
ATOM   2604 C  C     . SER A 1 347 ? 8.247   13.476  -8.369  1.00 37.33  ? 319 SER A C     1 
ATOM   2605 O  O     . SER A 1 347 ? 8.825   14.545  -8.593  1.00 42.15  ? 319 SER A O     1 
ATOM   2606 C  CB    . SER A 1 347 ? 7.178   13.096  -10.630 1.00 38.90  ? 319 SER A CB    1 
ATOM   2607 O  OG    . SER A 1 347 ? 8.202   12.195  -10.997 1.00 32.69  ? 319 SER A OG    1 
ATOM   2608 N  N     . ILE A 1 348 ? 8.686   12.607  -7.468  1.00 33.91  ? 320 ILE A N     1 
ATOM   2609 C  CA    A ILE A 1 348 ? 9.821   12.953  -6.619  0.44 31.56  ? 320 ILE A CA    1 
ATOM   2610 C  CA    B ILE A 1 348 ? 9.793   12.899  -6.560  0.56 31.52  ? 320 ILE A CA    1 
ATOM   2611 C  C     . ILE A 1 348 ? 10.998  12.049  -6.943  1.00 35.06  ? 320 ILE A C     1 
ATOM   2612 O  O     . ILE A 1 348 ? 10.850  10.873  -7.289  1.00 32.39  ? 320 ILE A O     1 
ATOM   2613 C  CB    A ILE A 1 348 ? 9.517   12.864  -5.117  0.44 34.33  ? 320 ILE A CB    1 
ATOM   2614 C  CB    B ILE A 1 348 ? 9.384   12.647  -5.095  0.56 34.00  ? 320 ILE A CB    1 
ATOM   2615 C  CG1   A ILE A 1 348 ? 9.168   11.447  -4.721  0.44 33.40  ? 320 ILE A CG1   1 
ATOM   2616 C  CG1   B ILE A 1 348 ? 8.308   13.649  -4.664  0.56 43.80  ? 320 ILE A CG1   1 
ATOM   2617 C  CG2   A ILE A 1 348 ? 8.347   13.776  -4.761  0.44 43.73  ? 320 ILE A CG2   1 
ATOM   2618 C  CG2   B ILE A 1 348 ? 10.564  12.754  -4.149  0.56 35.02  ? 320 ILE A CG2   1 
ATOM   2619 C  CD1   A ILE A 1 348 ? 9.098   11.306  -3.253  0.44 40.17  ? 320 ILE A CD1   1 
ATOM   2620 C  CD1   B ILE A 1 348 ? 7.681   13.320  -3.326  0.56 43.91  ? 320 ILE A CD1   1 
ATOM   2621 N  N     . ASP A 1 349 ? 12.188  12.630  -6.843  1.00 28.34  ? 321 ASP A N     1 
ATOM   2622 C  CA    . ASP A 1 349 ? 13.412  11.876  -7.079  1.00 27.64  ? 321 ASP A CA    1 
ATOM   2623 C  C     . ASP A 1 349 ? 13.677  10.947  -5.915  1.00 31.15  ? 321 ASP A C     1 
ATOM   2624 O  O     . ASP A 1 349 ? 13.575  11.343  -4.747  1.00 29.30  ? 321 ASP A O     1 
ATOM   2625 C  CB    . ASP A 1 349 ? 14.607  12.809  -7.223  1.00 29.46  ? 321 ASP A CB    1 
ATOM   2626 C  CG    . ASP A 1 349 ? 14.547  13.640  -8.476  1.00 37.72  ? 321 ASP A CG    1 
ATOM   2627 O  OD1   . ASP A 1 349 ? 14.217  13.108  -9.549  1.00 32.38  ? 321 ASP A OD1   1 
ATOM   2628 O  OD2   . ASP A 1 349 ? 14.866  14.830  -8.384  1.00 38.60  ? 321 ASP A OD2   1 
ATOM   2629 N  N     . ILE A 1 350 ? 14.050  9.717   -6.241  1.00 26.29  ? 322 ILE A N     1 
ATOM   2630 C  CA    . ILE A 1 350 ? 14.327  8.681   -5.262  1.00 24.75  ? 322 ILE A CA    1 
ATOM   2631 C  C     . ILE A 1 350 ? 15.825  8.439   -5.274  1.00 26.05  ? 322 ILE A C     1 
ATOM   2632 O  O     . ILE A 1 350 ? 16.422  8.272   -6.342  1.00 29.75  ? 322 ILE A O     1 
ATOM   2633 C  CB    . ILE A 1 350 ? 13.560  7.383   -5.576  1.00 28.54  ? 322 ILE A CB    1 
ATOM   2634 C  CG1   . ILE A 1 350 ? 12.039  7.633   -5.579  1.00 26.18  ? 322 ILE A CG1   1 
ATOM   2635 C  CG2   . ILE A 1 350 ? 13.951  6.299   -4.574  1.00 33.26  ? 322 ILE A CG2   1 
ATOM   2636 C  CD1   . ILE A 1 350 ? 11.502  8.100   -4.238  1.00 29.99  ? 322 ILE A CD1   1 
ATOM   2637 N  N     . TYR A 1 351 ? 16.431  8.434   -4.095  1.00 24.84  ? 323 TYR A N     1 
ATOM   2638 C  CA    . TYR A 1 351 ? 17.865  8.236   -3.958  1.00 25.87  ? 323 TYR A CA    1 
ATOM   2639 C  C     . TYR A 1 351 ? 18.145  6.996   -3.134  1.00 28.12  ? 323 TYR A C     1 
ATOM   2640 O  O     . TYR A 1 351 ? 17.286  6.493   -2.420  1.00 24.64  ? 323 TYR A O     1 
ATOM   2641 C  CB    . TYR A 1 351 ? 18.522  9.417   -3.240  1.00 27.86  ? 323 TYR A CB    1 
ATOM   2642 C  CG    . TYR A 1 351 ? 18.530  10.652  -4.059  1.00 30.80  ? 323 TYR A CG    1 
ATOM   2643 C  CD1   . TYR A 1 351 ? 17.397  11.453  -4.124  1.00 29.03  ? 323 TYR A CD1   1 
ATOM   2644 C  CD2   . TYR A 1 351 ? 19.662  11.033  -4.780  1.00 29.82  ? 323 TYR A CD2   1 
ATOM   2645 C  CE1   . TYR A 1 351 ? 17.385  12.601  -4.880  1.00 34.38  ? 323 TYR A CE1   1 
ATOM   2646 C  CE2   . TYR A 1 351 ? 19.647  12.183  -5.547  1.00 33.19  ? 323 TYR A CE2   1 
ATOM   2647 C  CZ    . TYR A 1 351 ? 18.518  12.951  -5.590  1.00 35.87  ? 323 TYR A CZ    1 
ATOM   2648 O  OH    . TYR A 1 351 ? 18.499  14.095  -6.332  1.00 35.72  ? 323 TYR A OH    1 
ATOM   2649 N  N     . SER A 1 352 ? 19.400  6.561   -3.173  1.00 28.87  ? 324 SER A N     1 
ATOM   2650 C  CA    . SER A 1 352 ? 19.908  5.604   -2.219  1.00 29.93  ? 324 SER A CA    1 
ATOM   2651 C  C     . SER A 1 352 ? 21.315  6.059   -1.846  1.00 30.59  ? 324 SER A C     1 
ATOM   2652 O  O     . SER A 1 352 ? 21.723  7.184   -2.161  1.00 24.85  ? 324 SER A O     1 
ATOM   2653 C  CB    . SER A 1 352 ? 19.853  4.177   -2.792  1.00 25.39  ? 324 SER A CB    1 
ATOM   2654 O  OG    . SER A 1 352 ? 20.161  3.215   -1.787  1.00 27.35  ? 324 SER A OG    1 
ATOM   2655 N  N     . ILE A 1 353 ? 22.022  5.200   -1.121  1.00 29.37  ? 325 ILE A N     1 
ATOM   2656 C  CA    . ILE A 1 353 ? 23.451  5.335   -0.831  1.00 28.05  ? 325 ILE A CA    1 
ATOM   2657 C  C     . ILE A 1 353 ? 24.158  4.290   -1.662  1.00 34.71  ? 325 ILE A C     1 
ATOM   2658 O  O     . ILE A 1 353 ? 23.735  3.128   -1.689  1.00 30.34  ? 325 ILE A O     1 
ATOM   2659 C  CB    . ILE A 1 353 ? 23.754  5.102   0.656   1.00 29.10  ? 325 ILE A CB    1 
ATOM   2660 C  CG1   . ILE A 1 353 ? 23.017  6.095   1.543   1.00 37.57  ? 325 ILE A CG1   1 
ATOM   2661 C  CG2   . ILE A 1 353 ? 25.275  5.151   0.948   1.00 34.58  ? 325 ILE A CG2   1 
ATOM   2662 C  CD1   . ILE A 1 353 ? 23.396  7.506   1.294   1.00 34.31  ? 325 ILE A CD1   1 
ATOM   2663 N  N     . ASP A 1 354 ? 25.228  4.687   -2.326  1.00 27.37  ? 326 ASP A N     1 
ATOM   2664 C  CA    . ASP A 1 354 ? 25.985  3.779   -3.177  1.00 30.93  ? 326 ASP A CA    1 
ATOM   2665 C  C     . ASP A 1 354 ? 27.166  3.307   -2.355  1.00 40.28  ? 326 ASP A C     1 
ATOM   2666 O  O     . ASP A 1 354 ? 28.180  3.987   -2.256  1.00 39.50  ? 326 ASP A O     1 
ATOM   2667 C  CB    . ASP A 1 354 ? 26.433  4.458   -4.470  1.00 32.62  ? 326 ASP A CB    1 
ATOM   2668 C  CG    . ASP A 1 354 ? 27.280  3.544   -5.349  1.00 37.72  ? 326 ASP A CG    1 
ATOM   2669 O  OD1   . ASP A 1 354 ? 27.174  2.313   -5.186  1.00 37.66  ? 326 ASP A OD1   1 
ATOM   2670 O  OD2   . ASP A 1 354 ? 27.997  4.043   -6.231  1.00 37.43  ? 326 ASP A OD2   1 
ATOM   2671 N  N     . ASN A 1 355 ? 27.020  2.144   -1.732  1.00 39.74  ? 327 ASN A N     1 
ATOM   2672 C  CA    . ASN A 1 355 ? 28.150  1.520   -1.063  1.00 47.70  ? 327 ASN A CA    1 
ATOM   2673 C  C     . ASN A 1 355 ? 28.022  0.010   -1.217  1.00 47.98  ? 327 ASN A C     1 
ATOM   2674 O  O     . ASN A 1 355 ? 27.063  -0.499  -1.799  1.00 49.62  ? 327 ASN A O     1 
ATOM   2675 C  CB    . ASN A 1 355 ? 28.267  1.994   0.398   1.00 49.68  ? 327 ASN A CB    1 
ATOM   2676 C  CG    . ASN A 1 355 ? 27.207  1.389   1.328   1.00 51.09  ? 327 ASN A CG    1 
ATOM   2677 O  OD1   . ASN A 1 355 ? 26.390  0.563   0.939   1.00 59.34  ? 327 ASN A OD1   1 
ATOM   2678 N  ND2   . ASN A 1 355 ? 27.221  1.837   2.580   1.00 55.93  ? 327 ASN A ND2   1 
ATOM   2679 N  N     . GLU A 1 356 ? 29.032  -0.697  -0.704  1.00 59.76  ? 328 GLU A N     1 
ATOM   2680 C  CA    . GLU A 1 356 ? 29.118  -2.154  -0.824  1.00 64.89  ? 328 GLU A CA    1 
ATOM   2681 C  C     . GLU A 1 356 ? 27.822  -2.844  -0.391  1.00 58.74  ? 328 GLU A C     1 
ATOM   2682 O  O     . GLU A 1 356 ? 27.369  -3.804  -1.030  1.00 69.65  ? 328 GLU A O     1 
ATOM   2683 C  CB    . GLU A 1 356 ? 30.322  -2.629  -0.015  1.00 71.08  ? 328 GLU A CB    1 
ATOM   2684 C  CG    . GLU A 1 356 ? 30.081  -2.474  1.475   1.00 75.28  ? 328 GLU A CG    1 
ATOM   2685 C  CD    . GLU A 1 356 ? 30.682  -1.189  2.003   1.00 82.36  ? 328 GLU A CD    1 
ATOM   2686 O  OE1   . GLU A 1 356 ? 31.054  -1.131  3.190   1.00 82.18  ? 328 GLU A OE1   1 
ATOM   2687 O  OE2   . GLU A 1 356 ? 30.767  -0.218  1.225   1.00 80.26  ? 328 GLU A OE2   1 
ATOM   2688 N  N     . MET A 1 357 ? 27.184  -2.330  0.660   1.00 69.86  ? 329 MET A N     1 
ATOM   2689 C  CA    . MET A 1 357 ? 25.978  -2.904  1.252   1.00 64.23  ? 329 MET A CA    1 
ATOM   2690 C  C     . MET A 1 357 ? 24.822  -2.928  0.266   1.00 73.43  ? 329 MET A C     1 
ATOM   2691 O  O     . MET A 1 357 ? 24.392  -3.990  -0.197  1.00 83.18  ? 329 MET A O     1 
ATOM   2692 C  CB    . MET A 1 357 ? 25.581  -2.089  2.475   1.00 62.33  ? 329 MET A CB    1 
ATOM   2693 C  CG    . MET A 1 357 ? 26.449  -2.345  3.668   1.00 70.96  ? 329 MET A CG    1 
ATOM   2694 S  SD    . MET A 1 357 ? 25.665  -3.569  4.707   1.00 74.47  ? 329 MET A SD    1 
ATOM   2695 C  CE    . MET A 1 357 ? 26.259  -5.086  3.970   1.00 62.97  ? 329 MET A CE    1 
ATOM   2696 N  N     . THR A 1 358 ? 24.314  -1.739  -0.040  1.00 66.38  ? 330 THR A N     1 
ATOM   2697 C  CA    . THR A 1 358 ? 23.215  -1.599  -0.972  1.00 62.68  ? 330 THR A CA    1 
ATOM   2698 C  C     . THR A 1 358 ? 23.567  -2.104  -2.368  1.00 66.38  ? 330 THR A C     1 
ATOM   2699 O  O     . THR A 1 358 ? 22.658  -2.410  -3.150  1.00 69.00  ? 330 THR A O     1 
ATOM   2700 C  CB    . THR A 1 358 ? 22.801  -0.128  -1.016  1.00 47.71  ? 330 THR A CB    1 
ATOM   2701 O  OG1   . THR A 1 358 ? 23.834  0.620   -1.666  1.00 51.42  ? 330 THR A OG1   1 
ATOM   2702 C  CG2   . THR A 1 358 ? 22.629  0.411   0.391   1.00 45.66  ? 330 THR A CG2   1 
ATOM   2703 N  N     . ARG A 1 359 ? 24.857  -2.200  -2.703  1.00 63.71  ? 331 ARG A N     1 
ATOM   2704 C  CA    . ARG A 1 359 ? 25.259  -2.634  -4.048  1.00 58.71  ? 331 ARG A CA    1 
ATOM   2705 C  C     . ARG A 1 359 ? 24.932  -4.104  -4.293  1.00 70.17  ? 331 ARG A C     1 
ATOM   2706 O  O     . ARG A 1 359 ? 25.241  -4.642  -5.363  1.00 68.28  ? 331 ARG A O     1 
ATOM   2707 C  CB    . ARG A 1 359 ? 26.757  -2.406  -4.297  1.00 66.23  ? 331 ARG A CB    1 
ATOM   2708 C  CG    . ARG A 1 359 ? 27.084  -1.276  -5.294  1.00 62.52  ? 331 ARG A CG    1 
ATOM   2709 C  CD    . ARG A 1 359 ? 28.603  -1.059  -5.433  1.00 55.49  ? 331 ARG A CD    1 
ATOM   2710 N  NE    . ARG A 1 359 ? 29.015  0.318   -5.176  1.00 56.61  ? 331 ARG A NE    1 
ATOM   2711 C  CZ    . ARG A 1 359 ? 30.046  0.662   -4.410  1.00 60.80  ? 331 ARG A CZ    1 
ATOM   2712 N  NH1   . ARG A 1 359 ? 30.827  -0.249  -3.848  1.00 63.26  ? 331 ARG A NH1   1 
ATOM   2713 N  NH2   . ARG A 1 359 ? 30.298  1.950   -4.197  1.00 55.29  ? 331 ARG A NH2   1 
ATOM   2714 N  N     . LEU A 1 365 ? 10.699  -12.225 -7.339  1.00 96.26  ? 337 LEU A N     1 
ATOM   2715 C  CA    . LEU A 1 365 ? 11.641  -11.116 -7.425  1.00 89.37  ? 337 LEU A CA    1 
ATOM   2716 C  C     . LEU A 1 365 ? 12.956  -11.497 -6.777  1.00 93.04  ? 337 LEU A C     1 
ATOM   2717 O  O     . LEU A 1 365 ? 13.053  -11.490 -5.548  1.00 95.97  ? 337 LEU A O     1 
ATOM   2718 C  CB    . LEU A 1 365 ? 11.085  -9.861  -6.740  1.00 97.31  ? 337 LEU A CB    1 
ATOM   2719 C  CG    . LEU A 1 365 ? 10.180  -10.054 -5.513  1.00 93.15  ? 337 LEU A CG    1 
ATOM   2720 C  CD1   . LEU A 1 365 ? 10.734  -9.287  -4.313  1.00 83.22  ? 337 LEU A CD1   1 
ATOM   2721 C  CD2   . LEU A 1 365 ? 8.738   -9.634  -5.800  1.00 87.09  ? 337 LEU A CD2   1 
ATOM   2722 N  N     . GLU A 1 366 ? 13.964  -11.799 -7.603  1.00 92.19  ? 338 GLU A N     1 
ATOM   2723 C  CA    . GLU A 1 366 ? 15.329  -12.111 -7.168  1.00 91.40  ? 338 GLU A CA    1 
ATOM   2724 C  C     . GLU A 1 366 ? 15.387  -12.901 -5.858  1.00 86.16  ? 338 GLU A C     1 
ATOM   2725 O  O     . GLU A 1 366 ? 15.459  -14.136 -5.864  1.00 83.94  ? 338 GLU A O     1 
ATOM   2726 C  CB    . GLU A 1 366 ? 16.167  -10.825 -7.044  1.00 91.18  ? 338 GLU A CB    1 
ATOM   2727 C  CG    . GLU A 1 366 ? 15.474  -9.620  -6.397  1.00 85.12  ? 338 GLU A CG    1 
ATOM   2728 C  CD    . GLU A 1 366 ? 16.442  -8.715  -5.669  1.00 94.23  ? 338 GLU A CD    1 
ATOM   2729 O  OE1   . GLU A 1 366 ? 17.661  -8.794  -5.958  1.00 96.74  ? 338 GLU A OE1   1 
ATOM   2730 O  OE2   . GLU A 1 366 ? 15.985  -7.941  -4.795  1.00 94.08  ? 338 GLU A OE2   1 
ATOM   2731 N  N     . ILE A 1 367 ? 15.345  -12.186 -4.731  1.00 80.35  ? 339 ILE A N     1 
ATOM   2732 C  CA    . ILE A 1 367 ? 15.476  -12.812 -3.417  1.00 78.62  ? 339 ILE A CA    1 
ATOM   2733 C  C     . ILE A 1 367 ? 14.312  -13.767 -3.151  1.00 73.09  ? 339 ILE A C     1 
ATOM   2734 O  O     . ILE A 1 367 ? 14.491  -14.832 -2.550  1.00 67.91  ? 339 ILE A O     1 
ATOM   2735 C  CB    . ILE A 1 367 ? 15.584  -11.718 -2.334  1.00 76.75  ? 339 ILE A CB    1 
ATOM   2736 C  CG1   . ILE A 1 367 ? 16.702  -10.724 -2.679  1.00 73.11  ? 339 ILE A CG1   1 
ATOM   2737 C  CG2   . ILE A 1 367 ? 15.820  -12.327 -0.958  1.00 61.58  ? 339 ILE A CG2   1 
ATOM   2738 C  CD1   . ILE A 1 367 ? 16.701  -9.461  -1.828  1.00 65.09  ? 339 ILE A CD1   1 
ATOM   2739 N  N     . ALA A 1 368 ? 13.110  -13.415 -3.619  1.00 74.49  ? 340 ALA A N     1 
ATOM   2740 C  CA    . ALA A 1 368 ? 11.909  -14.167 -3.259  1.00 65.56  ? 340 ALA A CA    1 
ATOM   2741 C  C     . ALA A 1 368 ? 12.017  -15.642 -3.636  1.00 67.60  ? 340 ALA A C     1 
ATOM   2742 O  O     . ALA A 1 368 ? 11.669  -16.520 -2.837  1.00 64.00  ? 340 ALA A O     1 
ATOM   2743 C  CB    . ALA A 1 368 ? 10.684  -13.535 -3.919  1.00 69.99  ? 340 ALA A CB    1 
ATOM   2744 N  N     . ARG A 1 369 ? 12.491  -15.938 -4.851  1.00 75.22  ? 341 ARG A N     1 
ATOM   2745 C  CA    . ARG A 1 369 ? 12.607  -17.334 -5.272  1.00 72.95  ? 341 ARG A CA    1 
ATOM   2746 C  C     . ARG A 1 369 ? 13.693  -18.077 -4.495  1.00 71.65  ? 341 ARG A C     1 
ATOM   2747 O  O     . ARG A 1 369 ? 13.546  -19.276 -4.218  1.00 64.07  ? 341 ARG A O     1 
ATOM   2748 C  CB    . ARG A 1 369 ? 12.868  -17.416 -6.780  1.00 75.90  ? 341 ARG A CB    1 
ATOM   2749 C  CG    . ARG A 1 369 ? 14.101  -16.647 -7.255  1.00 88.38  ? 341 ARG A CG    1 
ATOM   2750 C  CD    . ARG A 1 369 ? 13.786  -15.680 -8.406  1.00 98.31  ? 341 ARG A CD    1 
ATOM   2751 N  NE    . ARG A 1 369 ? 14.927  -14.823 -8.719  1.00 101.72 ? 341 ARG A NE    1 
ATOM   2752 C  CZ    . ARG A 1 369 ? 15.653  -14.894 -9.828  1.00 104.84 ? 341 ARG A CZ    1 
ATOM   2753 N  NH1   . ARG A 1 369 ? 15.380  -15.773 -10.779 1.00 102.24 ? 341 ARG A NH1   1 
ATOM   2754 N  NH2   . ARG A 1 369 ? 16.682  -14.062 -9.984  1.00 101.11 ? 341 ARG A NH2   1 
ATOM   2755 N  N     . ASN A 1 370 ? 14.784  -17.390 -4.142  1.00 63.47  ? 342 ASN A N     1 
ATOM   2756 C  CA    . ASN A 1 370 ? 15.818  -18.000 -3.310  1.00 63.86  ? 342 ASN A CA    1 
ATOM   2757 C  C     . ASN A 1 370 ? 15.263  -18.368 -1.939  1.00 59.94  ? 342 ASN A C     1 
ATOM   2758 O  O     . ASN A 1 370 ? 15.573  -19.442 -1.402  1.00 53.90  ? 342 ASN A O     1 
ATOM   2759 C  CB    . ASN A 1 370 ? 17.003  -17.035 -3.177  1.00 65.47  ? 342 ASN A CB    1 
ATOM   2760 C  CG    . ASN A 1 370 ? 18.000  -17.445 -2.080  1.00 75.14  ? 342 ASN A CG    1 
ATOM   2761 O  OD1   . ASN A 1 370 ? 18.236  -18.636 -1.833  1.00 72.76  ? 342 ASN A OD1   1 
ATOM   2762 N  ND2   . ASN A 1 370 ? 18.586  -16.445 -1.417  1.00 65.59  ? 342 ASN A ND2   1 
ATOM   2763 N  N     . ILE A 1 371 ? 14.427  -17.488 -1.372  1.00 56.23  ? 343 ILE A N     1 
ATOM   2764 C  CA    . ILE A 1 371 ? 13.894  -17.686 -0.027  1.00 56.21  ? 343 ILE A CA    1 
ATOM   2765 C  C     . ILE A 1 371 ? 13.185  -19.028 0.033   1.00 47.59  ? 343 ILE A C     1 
ATOM   2766 O  O     . ILE A 1 371 ? 13.461  -19.876 0.892   1.00 47.53  ? 343 ILE A O     1 
ATOM   2767 C  CB    . ILE A 1 371 ? 12.891  -16.574 0.319   1.00 56.68  ? 343 ILE A CB    1 
ATOM   2768 C  CG1   . ILE A 1 371 ? 13.563  -15.245 0.568   1.00 58.56  ? 343 ILE A CG1   1 
ATOM   2769 C  CG2   . ILE A 1 371 ? 12.259  -16.901 1.657   1.00 47.43  ? 343 ILE A CG2   1 
ATOM   2770 C  CD1   . ILE A 1 371 ? 14.186  -15.111 1.862   1.00 62.41  ? 343 ILE A CD1   1 
ATOM   2771 N  N     . GLY A 1 372 ? 12.259  -19.230 -0.912  1.00 51.32  ? 344 GLY A N     1 
ATOM   2772 C  CA    . GLY A 1 372 ? 11.407  -20.405 -0.889  1.00 55.40  ? 344 GLY A CA    1 
ATOM   2773 C  C     . GLY A 1 372 ? 12.184  -21.700 -1.013  1.00 52.98  ? 344 GLY A C     1 
ATOM   2774 O  O     . GLY A 1 372 ? 11.925  -22.663 -0.285  1.00 56.18  ? 344 GLY A O     1 
ATOM   2775 N  N     . HIS A 1 373 ? 13.150  -21.743 -1.939  1.00 53.93  ? 345 HIS A N     1 
ATOM   2776 C  CA    . HIS A 1 373 ? 13.975  -22.941 -2.083  1.00 55.99  ? 345 HIS A CA    1 
ATOM   2777 C  C     . HIS A 1 373 ? 14.709  -23.281 -0.786  1.00 56.03  ? 345 HIS A C     1 
ATOM   2778 O  O     . HIS A 1 373 ? 14.664  -24.425 -0.316  1.00 62.25  ? 345 HIS A O     1 
ATOM   2779 C  CB    . HIS A 1 373 ? 14.972  -22.768 -3.229  1.00 61.29  ? 345 HIS A CB    1 
ATOM   2780 C  CG    . HIS A 1 373 ? 15.698  -24.030 -3.578  1.00 72.76  ? 345 HIS A CG    1 
ATOM   2781 N  ND1   . HIS A 1 373 ? 15.054  -25.202 -3.915  1.00 78.79  ? 345 HIS A ND1   1 
ATOM   2782 C  CD2   . HIS A 1 373 ? 17.022  -24.319 -3.574  1.00 77.20  ? 345 HIS A CD2   1 
ATOM   2783 C  CE1   . HIS A 1 373 ? 15.951  -26.147 -4.139  1.00 78.00  ? 345 HIS A CE1   1 
ATOM   2784 N  NE2   . HIS A 1 373 ? 17.153  -25.636 -3.940  1.00 75.62  ? 345 HIS A NE2   1 
ATOM   2785 N  N     . TYR A 1 374 ? 15.407  -22.302 -0.201  1.00 52.79  ? 346 TYR A N     1 
ATOM   2786 C  CA    . TYR A 1 374 ? 16.145  -22.546 1.037   1.00 49.09  ? 346 TYR A CA    1 
ATOM   2787 C  C     . TYR A 1 374 ? 15.224  -23.024 2.155   1.00 53.66  ? 346 TYR A C     1 
ATOM   2788 O  O     . TYR A 1 374 ? 15.515  -24.018 2.831   1.00 50.22  ? 346 TYR A O     1 
ATOM   2789 C  CB    . TYR A 1 374 ? 16.886  -21.275 1.463   1.00 44.95  ? 346 TYR A CB    1 
ATOM   2790 C  CG    . TYR A 1 374 ? 17.661  -21.412 2.757   1.00 43.15  ? 346 TYR A CG    1 
ATOM   2791 C  CD1   . TYR A 1 374 ? 17.043  -21.214 3.998   1.00 37.21  ? 346 TYR A CD1   1 
ATOM   2792 C  CD2   . TYR A 1 374 ? 19.013  -21.743 2.737   1.00 44.97  ? 346 TYR A CD2   1 
ATOM   2793 C  CE1   . TYR A 1 374 ? 17.759  -21.338 5.182   1.00 38.55  ? 346 TYR A CE1   1 
ATOM   2794 C  CE2   . TYR A 1 374 ? 19.743  -21.869 3.916   1.00 41.89  ? 346 TYR A CE2   1 
ATOM   2795 C  CZ    . TYR A 1 374 ? 19.116  -21.662 5.128   1.00 39.06  ? 346 TYR A CZ    1 
ATOM   2796 O  OH    . TYR A 1 374 ? 19.858  -21.794 6.276   1.00 33.26  ? 346 TYR A OH    1 
ATOM   2797 N  N     . LEU A 1 375 ? 14.118  -22.308 2.383   1.00 43.16  ? 347 LEU A N     1 
ATOM   2798 C  CA    . LEU A 1 375 ? 13.203  -22.667 3.460   1.00 56.63  ? 347 LEU A CA    1 
ATOM   2799 C  C     . LEU A 1 375 ? 12.552  -24.019 3.206   1.00 61.82  ? 347 LEU A C     1 
ATOM   2800 O  O     . LEU A 1 375 ? 12.187  -24.721 4.156   1.00 63.05  ? 347 LEU A O     1 
ATOM   2801 C  CB    . LEU A 1 375 ? 12.129  -21.588 3.612   1.00 46.58  ? 347 LEU A CB    1 
ATOM   2802 C  CG    . LEU A 1 375 ? 12.632  -20.281 4.209   1.00 47.96  ? 347 LEU A CG    1 
ATOM   2803 C  CD1   . LEU A 1 375 ? 11.458  -19.343 4.437   1.00 45.99  ? 347 LEU A CD1   1 
ATOM   2804 C  CD2   . LEU A 1 375 ? 13.387  -20.547 5.517   1.00 46.83  ? 347 LEU A CD2   1 
ATOM   2805 N  N     . GLU A 1 376 ? 12.401  -24.392 1.934   1.00 58.51  ? 348 GLU A N     1 
ATOM   2806 C  CA    . GLU A 1 376 ? 11.785  -25.669 1.596   1.00 65.92  ? 348 GLU A CA    1 
ATOM   2807 C  C     . GLU A 1 376 ? 12.539  -26.841 2.210   1.00 75.48  ? 348 GLU A C     1 
ATOM   2808 O  O     . GLU A 1 376 ? 11.922  -27.818 2.647   1.00 78.84  ? 348 GLU A O     1 
ATOM   2809 C  CB    . GLU A 1 376 ? 11.702  -25.817 0.077   1.00 64.69  ? 348 GLU A CB    1 
ATOM   2810 C  CG    . GLU A 1 376 ? 10.768  -26.917 -0.386  1.00 73.53  ? 348 GLU A CG    1 
ATOM   2811 C  CD    . GLU A 1 376 ? 9.312   -26.561 -0.156  1.00 81.09  ? 348 GLU A CD    1 
ATOM   2812 O  OE1   . GLU A 1 376 ? 8.838   -26.716 0.994   1.00 80.32  ? 348 GLU A OE1   1 
ATOM   2813 O  OE2   . GLU A 1 376 ? 8.649   -26.106 -1.113  1.00 86.48  ? 348 GLU A OE2   1 
ATOM   2814 N  N     . ARG A 1 377 ? 13.867  -26.763 2.274   1.00 67.10  ? 349 ARG A N     1 
ATOM   2815 C  CA    . ARG A 1 377 ? 14.688  -27.887 2.715   1.00 73.76  ? 349 ARG A CA    1 
ATOM   2816 C  C     . ARG A 1 377 ? 15.439  -27.629 4.020   1.00 78.02  ? 349 ARG A C     1 
ATOM   2817 O  O     . ARG A 1 377 ? 16.590  -28.047 4.172   1.00 86.65  ? 349 ARG A O     1 
ATOM   2818 C  CB    . ARG A 1 377 ? 15.669  -28.292 1.617   1.00 77.67  ? 349 ARG A CB    1 
ATOM   2819 C  CG    . ARG A 1 377 ? 15.022  -28.452 0.248   1.00 83.74  ? 349 ARG A CG    1 
ATOM   2820 C  CD    . ARG A 1 377 ? 16.059  -28.594 -0.835  1.00 86.42  ? 349 ARG A CD    1 
ATOM   2821 N  NE    . ARG A 1 377 ? 16.360  -30.014 -1.022  1.00 98.22  ? 349 ARG A NE    1 
ATOM   2822 C  CZ    . ARG A 1 377 ? 17.231  -30.514 -1.889  1.00 98.89  ? 349 ARG A CZ    1 
ATOM   2823 N  NH1   . ARG A 1 377 ? 17.821  -29.745 -2.811  1.00 97.53  ? 349 ARG A NH1   1 
ATOM   2824 N  NH2   . ARG A 1 377 ? 17.511  -31.817 -1.831  1.00 91.53  ? 349 ARG A NH2   1 
ATOM   2825 N  N     . VAL A 1 378 ? 14.798  -26.973 4.986   1.00 74.86  ? 350 VAL A N     1 
ATOM   2826 C  CA    . VAL A 1 378 ? 15.418  -26.758 6.296   1.00 78.55  ? 350 VAL A CA    1 
ATOM   2827 C  C     . VAL A 1 378 ? 14.496  -27.222 7.426   1.00 81.61  ? 350 VAL A C     1 
ATOM   2828 O  O     . VAL A 1 378 ? 13.643  -26.467 7.903   1.00 84.89  ? 350 VAL A O     1 
ATOM   2829 C  CB    . VAL A 1 378 ? 15.820  -25.277 6.495   1.00 68.37  ? 350 VAL A CB    1 
HETATM 2830 N  N1    . FMN B 2 .   ? 21.152  9.068   47.181  1.00 46.46  ? 401 FMN A N1    1 
HETATM 2831 C  C2    . FMN B 2 .   ? 20.743  10.314  47.631  1.00 45.40  ? 401 FMN A C2    1 
HETATM 2832 O  O2    . FMN B 2 .   ? 21.563  11.197  47.846  1.00 46.85  ? 401 FMN A O2    1 
HETATM 2833 N  N3    . FMN B 2 .   ? 19.407  10.591  47.846  1.00 37.90  ? 401 FMN A N3    1 
HETATM 2834 C  C4    . FMN B 2 .   ? 18.455  9.609   47.605  1.00 40.85  ? 401 FMN A C4    1 
HETATM 2835 O  O4    . FMN B 2 .   ? 17.262  9.862   47.820  1.00 39.91  ? 401 FMN A O4    1 
HETATM 2836 C  C4A   . FMN B 2 .   ? 18.863  8.357   47.147  1.00 38.55  ? 401 FMN A C4A   1 
HETATM 2837 N  N5    . FMN B 2 .   ? 17.935  7.379   46.898  1.00 35.38  ? 401 FMN A N5    1 
HETATM 2838 C  C5A   . FMN B 2 .   ? 18.336  6.133   46.435  1.00 38.22  ? 401 FMN A C5A   1 
HETATM 2839 C  C6    . FMN B 2 .   ? 17.393  5.155   46.180  1.00 36.94  ? 401 FMN A C6    1 
HETATM 2840 C  C7    . FMN B 2 .   ? 17.772  3.898   45.724  1.00 40.59  ? 401 FMN A C7    1 
HETATM 2841 C  C7M   . FMN B 2 .   ? 16.699  2.879   45.471  1.00 36.44  ? 401 FMN A C7M   1 
HETATM 2842 C  C8    . FMN B 2 .   ? 19.114  3.612   45.507  1.00 44.98  ? 401 FMN A C8    1 
HETATM 2843 C  C8M   . FMN B 2 .   ? 19.537  2.256   45.017  1.00 44.96  ? 401 FMN A C8M   1 
HETATM 2844 C  C9    . FMN B 2 .   ? 20.069  4.593   45.761  1.00 43.02  ? 401 FMN A C9    1 
HETATM 2845 C  C9A   . FMN B 2 .   ? 19.677  5.850   46.219  1.00 42.51  ? 401 FMN A C9A   1 
HETATM 2846 N  N10   . FMN B 2 .   ? 20.615  6.830   46.470  1.00 42.85  ? 401 FMN A N10   1 
HETATM 2847 C  C10   . FMN B 2 .   ? 20.221  8.078   46.932  1.00 39.75  ? 401 FMN A C10   1 
HETATM 2848 C  "C1'" . FMN B 2 .   ? 22.062  6.479   46.261  1.00 45.68  ? 401 FMN A "C1'" 1 
HETATM 2849 C  "C2'" . FMN B 2 .   ? 22.690  7.091   45.036  1.00 47.78  ? 401 FMN A "C2'" 1 
HETATM 2850 O  "O2'" . FMN B 2 .   ? 22.381  6.257   43.940  1.00 47.78  ? 401 FMN A "O2'" 1 
HETATM 2851 C  "C3'" . FMN B 2 .   ? 24.194  7.157   45.308  1.00 60.17  ? 401 FMN A "C3'" 1 
HETATM 2852 O  "O3'" . FMN B 2 .   ? 24.708  5.862   45.525  1.00 53.97  ? 401 FMN A "O3'" 1 
HETATM 2853 C  "C4'" . FMN B 2 .   ? 24.503  7.984   46.553  1.00 62.40  ? 401 FMN A "C4'" 1 
HETATM 2854 O  "O4'" . FMN B 2 .   ? 23.837  9.236   46.518  1.00 62.82  ? 401 FMN A "O4'" 1 
HETATM 2855 C  "C5'" . FMN B 2 .   ? 25.998  8.241   46.625  1.00 76.06  ? 401 FMN A "C5'" 1 
HETATM 2856 O  "O5'" . FMN B 2 .   ? 26.264  9.344   45.784  1.00 101.03 ? 401 FMN A "O5'" 1 
HETATM 2857 P  P     . FMN B 2 .   ? 27.761  9.917   45.583  1.00 132.88 ? 401 FMN A P     1 
HETATM 2858 O  O1P   . FMN B 2 .   ? 28.295  9.375   44.273  1.00 113.64 ? 401 FMN A O1P   1 
HETATM 2859 O  O2P   . FMN B 2 .   ? 27.745  11.434  45.543  1.00 103.77 ? 401 FMN A O2P   1 
HETATM 2860 O  O3P   . FMN B 2 .   ? 28.628  9.444   46.733  1.00 115.82 ? 401 FMN A O3P   1 
HETATM 2861 CA CA    . CA  C 3 .   ? 12.884  13.771  -11.329 1.00 32.84  ? 402 CA  A CA    1 
HETATM 2862 CA CA    . CA  D 3 .   ? 6.556   -7.174  3.700   1.00 50.65  ? 403 CA  A CA    1 
HETATM 2863 O  O     . HOH E 4 .   ? 21.361  14.159  58.328  1.00 46.71  ? 501 HOH A O     1 
HETATM 2864 O  O     . HOH E 4 .   ? -4.857  6.233   2.465   1.00 34.61  ? 502 HOH A O     1 
HETATM 2865 O  O     . HOH E 4 .   ? 28.720  -25.181 10.284  1.00 59.35  ? 503 HOH A O     1 
HETATM 2866 O  O     . HOH E 4 .   ? 25.805  4.319   44.156  1.00 59.91  ? 504 HOH A O     1 
HETATM 2867 O  O     . HOH E 4 .   ? 0.325   6.057   -8.381  1.00 59.20  ? 505 HOH A O     1 
HETATM 2868 O  O     . HOH E 4 .   ? -5.323  11.300  1.590   1.00 38.15  ? 506 HOH A O     1 
HETATM 2869 O  O     . HOH E 4 .   ? 26.860  0.534   9.345   1.00 50.56  ? 507 HOH A O     1 
HETATM 2870 O  O     . HOH E 4 .   ? 5.566   15.623  58.909  1.00 58.99  ? 508 HOH A O     1 
HETATM 2871 O  O     . HOH E 4 .   ? 31.859  1.685   0.229   1.00 55.82  ? 509 HOH A O     1 
HETATM 2872 O  O     . HOH E 4 .   ? 13.261  8.085   34.166  1.00 59.49  ? 510 HOH A O     1 
HETATM 2873 O  O     . HOH E 4 .   ? 3.573   -2.628  -2.054  1.00 43.54  ? 511 HOH A O     1 
HETATM 2874 O  O     . HOH E 4 .   ? 6.242   -0.218  34.162  1.00 56.36  ? 512 HOH A O     1 
HETATM 2875 O  O     . HOH E 4 .   ? 2.347   6.939   14.365  1.00 48.84  ? 513 HOH A O     1 
HETATM 2876 O  O     . HOH E 4 .   ? 24.711  16.118  2.373   1.00 47.81  ? 514 HOH A O     1 
HETATM 2877 O  O     . HOH E 4 .   ? 13.095  9.955   -13.926 1.00 31.35  ? 515 HOH A O     1 
HETATM 2878 O  O     . HOH E 4 .   ? 4.627   -5.370  4.426   1.00 34.99  ? 516 HOH A O     1 
HETATM 2879 O  O     . HOH E 4 .   ? 10.654  -2.367  1.840   1.00 36.71  ? 517 HOH A O     1 
HETATM 2880 O  O     . HOH E 4 .   ? 8.339   7.848   32.795  1.00 52.92  ? 518 HOH A O     1 
HETATM 2881 O  O     . HOH E 4 .   ? 23.886  -8.999  13.945  1.00 37.73  ? 519 HOH A O     1 
HETATM 2882 O  O     . HOH E 4 .   ? 21.186  -15.775 2.460   1.00 42.22  ? 520 HOH A O     1 
HETATM 2883 O  O     . HOH E 4 .   ? 21.779  -6.489  4.778   1.00 32.32  ? 521 HOH A O     1 
HETATM 2884 O  O     . HOH E 4 .   ? 1.830   -11.291 23.988  1.00 55.50  ? 522 HOH A O     1 
HETATM 2885 O  O     . HOH E 4 .   ? 27.454  13.851  -0.613  1.00 36.62  ? 523 HOH A O     1 
HETATM 2886 O  O     . HOH E 4 .   ? 20.648  15.275  9.563   1.00 46.92  ? 524 HOH A O     1 
HETATM 2887 O  O     . HOH E 4 .   ? 20.309  14.828  -8.104  1.00 43.96  ? 525 HOH A O     1 
HETATM 2888 O  O     . HOH E 4 .   ? 18.121  -20.199 14.028  1.00 47.57  ? 526 HOH A O     1 
HETATM 2889 O  O     . HOH E 4 .   ? 16.077  6.294   56.135  1.00 37.50  ? 527 HOH A O     1 
HETATM 2890 O  O     . HOH E 4 .   ? 16.260  15.694  -6.259  1.00 42.77  ? 528 HOH A O     1 
HETATM 2891 O  O     . HOH E 4 .   ? -2.510  1.851   17.317  1.00 42.62  ? 529 HOH A O     1 
HETATM 2892 O  O     . HOH E 4 .   ? 15.775  17.178  54.031  1.00 37.68  ? 530 HOH A O     1 
HETATM 2893 O  O     . HOH E 4 .   ? 13.666  -12.155 3.931   1.00 34.12  ? 531 HOH A O     1 
HETATM 2894 O  O     . HOH E 4 .   ? -0.440  13.218  9.593   1.00 47.04  ? 532 HOH A O     1 
HETATM 2895 O  O     . HOH E 4 .   ? 5.940   -5.090  61.455  1.00 48.48  ? 533 HOH A O     1 
HETATM 2896 O  O     . HOH E 4 .   ? 9.294   12.661  1.301   1.00 29.53  ? 534 HOH A O     1 
HETATM 2897 O  O     . HOH E 4 .   ? 23.823  2.467   15.550  1.00 56.71  ? 535 HOH A O     1 
HETATM 2898 O  O     . HOH E 4 .   ? 21.695  9.337   58.064  1.00 38.71  ? 536 HOH A O     1 
HETATM 2899 O  O     . HOH E 4 .   ? 7.349   -1.022  4.425   1.00 49.25  ? 537 HOH A O     1 
HETATM 2900 O  O     . HOH E 4 .   ? -3.464  -10.015 44.152  1.00 43.31  ? 538 HOH A O     1 
HETATM 2901 O  O     . HOH E 4 .   ? 12.285  15.457  -6.078  1.00 35.47  ? 539 HOH A O     1 
HETATM 2902 O  O     . HOH E 4 .   ? 23.758  16.371  49.218  1.00 57.08  ? 540 HOH A O     1 
HETATM 2903 O  O     . HOH E 4 .   ? 26.947  3.639   13.688  1.00 45.13  ? 541 HOH A O     1 
HETATM 2904 O  O     . HOH E 4 .   ? 10.852  17.187  14.146  1.00 56.21  ? 542 HOH A O     1 
HETATM 2905 O  O     . HOH E 4 .   ? 24.751  9.032   14.226  1.00 50.50  ? 543 HOH A O     1 
HETATM 2906 O  O     . HOH E 4 .   ? 19.996  11.651  58.342  1.00 41.69  ? 544 HOH A O     1 
HETATM 2907 O  O     . HOH E 4 .   ? 11.151  11.432  16.816  1.00 51.93  ? 545 HOH A O     1 
HETATM 2908 O  O     . HOH E 4 .   ? 2.540   -6.932  56.958  1.00 42.48  ? 546 HOH A O     1 
HETATM 2909 O  O     . HOH E 4 .   ? 23.258  15.613  56.483  1.00 40.60  ? 547 HOH A O     1 
HETATM 2910 O  O     . HOH E 4 .   ? 18.234  -6.460  1.944   1.00 46.49  ? 548 HOH A O     1 
HETATM 2911 O  O     . HOH E 4 .   ? -3.074  -9.721  58.094  1.00 45.44  ? 549 HOH A O     1 
HETATM 2912 O  O     . HOH E 4 .   ? 15.751  -2.659  56.035  1.00 47.68  ? 550 HOH A O     1 
HETATM 2913 O  O     . HOH E 4 .   ? 5.578   12.611  41.807  1.00 37.99  ? 551 HOH A O     1 
HETATM 2914 O  O     . HOH E 4 .   ? 6.930   -9.297  2.552   1.00 37.67  ? 552 HOH A O     1 
HETATM 2915 O  O     . HOH E 4 .   ? -4.833  16.483  21.753  1.00 48.29  ? 553 HOH A O     1 
HETATM 2916 O  O     . HOH E 4 .   ? 16.297  4.933   -13.669 1.00 45.91  ? 554 HOH A O     1 
HETATM 2917 O  O     . HOH E 4 .   ? 28.542  -5.221  14.742  1.00 58.45  ? 555 HOH A O     1 
HETATM 2918 O  O     . HOH E 4 .   ? 4.015   12.995  35.339  1.00 45.63  ? 556 HOH A O     1 
HETATM 2919 O  O     . HOH E 4 .   ? 2.826   -5.360  6.659   1.00 33.98  ? 557 HOH A O     1 
HETATM 2920 O  O     . HOH E 4 .   ? 15.570  21.425  47.520  1.00 53.76  ? 558 HOH A O     1 
HETATM 2921 O  O     . HOH E 4 .   ? 7.225   3.877   -8.907  1.00 53.74  ? 559 HOH A O     1 
HETATM 2922 O  O     . HOH E 4 .   ? 26.771  11.623  -3.962  1.00 40.98  ? 560 HOH A O     1 
HETATM 2923 O  O     . HOH E 4 .   ? 13.928  5.476   -13.999 1.00 45.05  ? 561 HOH A O     1 
HETATM 2924 O  O     . HOH E 4 .   ? 15.034  11.315  57.154  1.00 33.79  ? 562 HOH A O     1 
HETATM 2925 O  O     . HOH E 4 .   ? 7.317   14.194  56.775  1.00 39.42  ? 563 HOH A O     1 
HETATM 2926 O  O     . HOH E 4 .   ? 11.531  15.101  -9.791  1.00 31.96  ? 564 HOH A O     1 
HETATM 2927 O  O     . HOH E 4 .   ? 2.382   12.183  44.377  1.00 55.76  ? 565 HOH A O     1 
HETATM 2928 O  O     . HOH E 4 .   ? 15.488  11.769  16.014  1.00 38.97  ? 566 HOH A O     1 
HETATM 2929 O  O     . HOH E 4 .   ? -2.209  -3.241  61.461  1.00 45.19  ? 567 HOH A O     1 
HETATM 2930 O  O     . HOH E 4 .   ? 11.825  -0.304  57.750  1.00 46.62  ? 568 HOH A O     1 
HETATM 2931 O  O     . HOH E 4 .   ? 9.159   4.312   -10.290 1.00 55.03  ? 569 HOH A O     1 
HETATM 2932 O  O     . HOH E 4 .   ? -0.197  -6.424  12.397  1.00 28.76  ? 570 HOH A O     1 
HETATM 2933 O  O     . HOH E 4 .   ? 24.059  -12.653 3.212   1.00 34.61  ? 571 HOH A O     1 
HETATM 2934 O  O     . HOH E 4 .   ? 20.477  -3.214  -7.564  1.00 55.60  ? 572 HOH A O     1 
HETATM 2935 O  O     . HOH E 4 .   ? 18.060  11.266  15.867  1.00 44.28  ? 573 HOH A O     1 
HETATM 2936 O  O     . HOH E 4 .   ? 8.262   -9.404  -0.925  1.00 50.82  ? 574 HOH A O     1 
HETATM 2937 O  O     . HOH E 4 .   ? 14.192  -6.912  52.721  1.00 55.65  ? 575 HOH A O     1 
HETATM 2938 O  O     . HOH E 4 .   ? 28.092  7.100   2.306   1.00 35.56  ? 576 HOH A O     1 
HETATM 2939 O  O     . HOH E 4 .   ? 7.287   -3.654  -6.895  1.00 48.93  ? 577 HOH A O     1 
HETATM 2940 O  O     . HOH E 4 .   ? 28.651  4.494   2.741   1.00 54.42  ? 578 HOH A O     1 
HETATM 2941 O  O     . HOH E 4 .   ? 22.075  17.122  0.547   1.00 50.38  ? 579 HOH A O     1 
HETATM 2942 O  O     . HOH E 4 .   ? 14.811  13.292  -12.732 1.00 32.38  ? 580 HOH A O     1 
HETATM 2943 O  O     . HOH E 4 .   ? 9.760   2.960   58.609  1.00 46.58  ? 581 HOH A O     1 
HETATM 2944 O  O     . HOH E 4 .   ? 18.880  -7.079  4.299   1.00 33.32  ? 582 HOH A O     1 
HETATM 2945 O  O     . HOH E 4 .   ? 14.127  -14.584 18.417  1.00 46.63  ? 583 HOH A O     1 
HETATM 2946 O  O     . HOH E 4 .   ? 2.781   -24.522 12.886  1.00 49.19  ? 584 HOH A O     1 
HETATM 2947 O  O     . HOH E 4 .   ? 9.908   -0.449  3.269   1.00 43.14  ? 585 HOH A O     1 
HETATM 2948 O  O     . HOH E 4 .   ? 14.058  15.848  60.443  1.00 41.13  ? 586 HOH A O     1 
HETATM 2949 O  O     . HOH E 4 .   ? 20.920  -5.138  -2.129  1.00 57.08  ? 587 HOH A O     1 
HETATM 2950 O  O     . HOH E 4 .   ? 22.190  -5.314  2.036   1.00 52.10  ? 588 HOH A O     1 
HETATM 2951 O  O     . HOH E 4 .   ? 18.506  13.103  60.297  1.00 51.72  ? 589 HOH A O     1 
HETATM 2952 O  O     . HOH E 4 .   ? 25.678  15.551  57.115  1.00 43.61  ? 590 HOH A O     1 
HETATM 2953 O  O     . HOH E 4 .   ? 0.949   -21.610 10.168  1.00 57.69  ? 591 HOH A O     1 
HETATM 2954 O  O     . HOH E 4 .   ? 30.725  20.359  0.656   1.00 57.27  ? 592 HOH A O     1 
# 
