data_8RQW
# 
_entry.id   8RQW 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   8RQW         pdb_00008rqw 10.2210/pdb8rqw/pdb 
WWPDB D_1292136066 ?            ?                   
# 
_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       2025-01-29 
# 
_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                        8RQW 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-20 
_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 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 8RQV unspecified 
PDB . 8RM2 unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              daniel.gutman@mail.huji.ac.il 
_pdbx_contact_author.name_first         Daniel 
_pdbx_contact_author.name_last          Gutman 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0009-0009-3240-752X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Livnah, O.' 1 ? 
'Gutman, D.' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_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                     'Erk2 MAP kinase (T188A) ANP-PNP complex' 
_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 'Livnah, O.' 1 ? 
primary 'Gutman, D.' 2 ? 
# 
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 'Mitogen-activated protein kinase 1'          42258.520 1   2.7.11.24 ? ? ? 
2 non-polymer syn 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' 506.196   1   ?         ? ? ? 
3 water       nat water                                         18.015    117 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;MAP kinase 1,MAPK 1,ERT1,Extracellular signal-regulated kinase 2,ERK-2,MAP kinase isoform p42,p42-MAPK,Mitogen-activated protein kinase 2,MAP kinase 2,MAPK 2
;
# 
_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       
;AHHHHHHMAAAAAAGPEMVRGQVFDVGPRYTNLSYIGEGAYGMVCSAYDNLNKVRVAIKKISPFEHQTYCQRTLREIKIL
LRFRHENIIGINDIIRAPTIEQMKDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNL
LLNTTCDLKICDFGLARVADPDHDHTGFLTEYVAERWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLD
QLNHILGILGSPSQEDLNCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQ
YYDPSDEPIAEAPFKFDMELDDLPKEKLKELIFEETARFQPGYRS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;AHHHHHHMAAAAAAGPEMVRGQVFDVGPRYTNLSYIGEGAYGMVCSAYDNLNKVRVAIKKISPFEHQTYCQRTLREIKIL
LRFRHENIIGINDIIRAPTIEQMKDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNL
LLNTTCDLKICDFGLARVADPDHDHTGFLTEYVAERWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLD
QLNHILGILGSPSQEDLNCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQ
YYDPSDEPIAEAPFKFDMELDDLPKEKLKELIFEETARFQPGYRS
;
_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 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' ANP 
3 water                                         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   HIS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   MET n 
1 9   ALA n 
1 10  ALA n 
1 11  ALA n 
1 12  ALA n 
1 13  ALA n 
1 14  ALA n 
1 15  GLY n 
1 16  PRO n 
1 17  GLU n 
1 18  MET n 
1 19  VAL n 
1 20  ARG n 
1 21  GLY n 
1 22  GLN n 
1 23  VAL n 
1 24  PHE n 
1 25  ASP n 
1 26  VAL n 
1 27  GLY n 
1 28  PRO n 
1 29  ARG n 
1 30  TYR n 
1 31  THR n 
1 32  ASN n 
1 33  LEU n 
1 34  SER n 
1 35  TYR n 
1 36  ILE n 
1 37  GLY n 
1 38  GLU n 
1 39  GLY n 
1 40  ALA n 
1 41  TYR n 
1 42  GLY n 
1 43  MET n 
1 44  VAL n 
1 45  CYS n 
1 46  SER n 
1 47  ALA n 
1 48  TYR n 
1 49  ASP n 
1 50  ASN n 
1 51  LEU n 
1 52  ASN n 
1 53  LYS n 
1 54  VAL n 
1 55  ARG n 
1 56  VAL n 
1 57  ALA n 
1 58  ILE n 
1 59  LYS n 
1 60  LYS n 
1 61  ILE n 
1 62  SER n 
1 63  PRO n 
1 64  PHE n 
1 65  GLU n 
1 66  HIS n 
1 67  GLN n 
1 68  THR n 
1 69  TYR n 
1 70  CYS n 
1 71  GLN n 
1 72  ARG n 
1 73  THR n 
1 74  LEU n 
1 75  ARG n 
1 76  GLU n 
1 77  ILE n 
1 78  LYS n 
1 79  ILE n 
1 80  LEU n 
1 81  LEU n 
1 82  ARG n 
1 83  PHE n 
1 84  ARG n 
1 85  HIS n 
1 86  GLU n 
1 87  ASN n 
1 88  ILE n 
1 89  ILE n 
1 90  GLY n 
1 91  ILE n 
1 92  ASN n 
1 93  ASP n 
1 94  ILE n 
1 95  ILE n 
1 96  ARG n 
1 97  ALA n 
1 98  PRO n 
1 99  THR n 
1 100 ILE n 
1 101 GLU n 
1 102 GLN n 
1 103 MET n 
1 104 LYS n 
1 105 ASP n 
1 106 VAL n 
1 107 TYR n 
1 108 ILE n 
1 109 VAL n 
1 110 GLN n 
1 111 ASP n 
1 112 LEU n 
1 113 MET n 
1 114 GLU n 
1 115 THR n 
1 116 ASP n 
1 117 LEU n 
1 118 TYR n 
1 119 LYS n 
1 120 LEU n 
1 121 LEU n 
1 122 LYS n 
1 123 THR n 
1 124 GLN n 
1 125 HIS n 
1 126 LEU n 
1 127 SER n 
1 128 ASN n 
1 129 ASP n 
1 130 HIS n 
1 131 ILE n 
1 132 CYS n 
1 133 TYR n 
1 134 PHE n 
1 135 LEU n 
1 136 TYR n 
1 137 GLN n 
1 138 ILE n 
1 139 LEU n 
1 140 ARG n 
1 141 GLY n 
1 142 LEU n 
1 143 LYS n 
1 144 TYR n 
1 145 ILE n 
1 146 HIS n 
1 147 SER n 
1 148 ALA n 
1 149 ASN n 
1 150 VAL n 
1 151 LEU n 
1 152 HIS n 
1 153 ARG n 
1 154 ASP n 
1 155 LEU n 
1 156 LYS n 
1 157 PRO n 
1 158 SER n 
1 159 ASN n 
1 160 LEU n 
1 161 LEU n 
1 162 LEU n 
1 163 ASN n 
1 164 THR n 
1 165 THR n 
1 166 CYS n 
1 167 ASP n 
1 168 LEU n 
1 169 LYS n 
1 170 ILE n 
1 171 CYS n 
1 172 ASP n 
1 173 PHE n 
1 174 GLY n 
1 175 LEU n 
1 176 ALA n 
1 177 ARG n 
1 178 VAL n 
1 179 ALA n 
1 180 ASP n 
1 181 PRO n 
1 182 ASP n 
1 183 HIS n 
1 184 ASP n 
1 185 HIS n 
1 186 THR n 
1 187 GLY n 
1 188 PHE n 
1 189 LEU n 
1 190 THR n 
1 191 GLU n 
1 192 TYR n 
1 193 VAL n 
1 194 ALA n 
1 195 GLU n 
1 196 ARG n 
1 197 TRP n 
1 198 TYR n 
1 199 ARG n 
1 200 ALA n 
1 201 PRO n 
1 202 GLU n 
1 203 ILE n 
1 204 MET n 
1 205 LEU n 
1 206 ASN n 
1 207 SER n 
1 208 LYS n 
1 209 GLY n 
1 210 TYR n 
1 211 THR n 
1 212 LYS n 
1 213 SER n 
1 214 ILE n 
1 215 ASP n 
1 216 ILE n 
1 217 TRP n 
1 218 SER n 
1 219 VAL n 
1 220 GLY n 
1 221 CYS n 
1 222 ILE n 
1 223 LEU n 
1 224 ALA n 
1 225 GLU n 
1 226 MET n 
1 227 LEU n 
1 228 SER n 
1 229 ASN n 
1 230 ARG n 
1 231 PRO n 
1 232 ILE n 
1 233 PHE n 
1 234 PRO n 
1 235 GLY n 
1 236 LYS n 
1 237 HIS n 
1 238 TYR n 
1 239 LEU n 
1 240 ASP n 
1 241 GLN n 
1 242 LEU n 
1 243 ASN n 
1 244 HIS n 
1 245 ILE n 
1 246 LEU n 
1 247 GLY n 
1 248 ILE n 
1 249 LEU n 
1 250 GLY n 
1 251 SER n 
1 252 PRO n 
1 253 SER n 
1 254 GLN n 
1 255 GLU n 
1 256 ASP n 
1 257 LEU n 
1 258 ASN n 
1 259 CYS n 
1 260 ILE n 
1 261 ILE n 
1 262 ASN n 
1 263 LEU n 
1 264 LYS n 
1 265 ALA n 
1 266 ARG n 
1 267 ASN n 
1 268 TYR n 
1 269 LEU n 
1 270 LEU n 
1 271 SER n 
1 272 LEU n 
1 273 PRO n 
1 274 HIS n 
1 275 LYS n 
1 276 ASN n 
1 277 LYS n 
1 278 VAL n 
1 279 PRO n 
1 280 TRP n 
1 281 ASN n 
1 282 ARG n 
1 283 LEU n 
1 284 PHE n 
1 285 PRO n 
1 286 ASN n 
1 287 ALA n 
1 288 ASP n 
1 289 SER n 
1 290 LYS n 
1 291 ALA n 
1 292 LEU n 
1 293 ASP n 
1 294 LEU n 
1 295 LEU n 
1 296 ASP n 
1 297 LYS n 
1 298 MET n 
1 299 LEU n 
1 300 THR n 
1 301 PHE n 
1 302 ASN n 
1 303 PRO n 
1 304 HIS n 
1 305 LYS n 
1 306 ARG n 
1 307 ILE n 
1 308 GLU n 
1 309 VAL n 
1 310 GLU n 
1 311 GLN n 
1 312 ALA n 
1 313 LEU n 
1 314 ALA n 
1 315 HIS n 
1 316 PRO n 
1 317 TYR n 
1 318 LEU n 
1 319 GLU n 
1 320 GLN n 
1 321 TYR n 
1 322 TYR n 
1 323 ASP n 
1 324 PRO n 
1 325 SER n 
1 326 ASP n 
1 327 GLU n 
1 328 PRO n 
1 329 ILE n 
1 330 ALA n 
1 331 GLU n 
1 332 ALA n 
1 333 PRO n 
1 334 PHE n 
1 335 LYS n 
1 336 PHE n 
1 337 ASP n 
1 338 MET n 
1 339 GLU n 
1 340 LEU n 
1 341 ASP n 
1 342 ASP n 
1 343 LEU n 
1 344 PRO n 
1 345 LYS n 
1 346 GLU n 
1 347 LYS n 
1 348 LEU n 
1 349 LYS n 
1 350 GLU n 
1 351 LEU n 
1 352 ILE n 
1 353 PHE n 
1 354 GLU n 
1 355 GLU n 
1 356 THR n 
1 357 ALA n 
1 358 ARG n 
1 359 PHE n 
1 360 GLN n 
1 361 PRO n 
1 362 GLY n 
1 363 TYR n 
1 364 ARG n 
1 365 SER 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                   365 
_entity_src_gen.gene_src_common_name               'Norway rat' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'Mapk1, Erk2, Mapk, Prkm1' 
_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      'Rattus norvegicus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     10116 
_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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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  
ANP non-polymer         . 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' ? 'C10 H17 N6 O12 P3' 506.196 
ARG 'L-peptide linking' y ARGININE                                      ? 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                                    ? 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                               ? 'C4 H7 N O4'        133.103 
CYS 'L-peptide linking' y CYSTEINE                                      ? 'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE                                     ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                               ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                                       ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                                     ? 'C6 H10 N3 O2 1'    156.162 
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   ALA 1   -6  ?   ?   ?   A . n 
A 1 2   HIS 2   -5  ?   ?   ?   A . n 
A 1 3   HIS 3   -4  ?   ?   ?   A . n 
A 1 4   HIS 4   -3  ?   ?   ?   A . n 
A 1 5   HIS 5   -2  ?   ?   ?   A . n 
A 1 6   HIS 6   -1  ?   ?   ?   A . n 
A 1 7   HIS 7   0   ?   ?   ?   A . n 
A 1 8   MET 8   1   ?   ?   ?   A . n 
A 1 9   ALA 9   2   ?   ?   ?   A . n 
A 1 10  ALA 10  3   ?   ?   ?   A . n 
A 1 11  ALA 11  4   4   ALA ALA A . n 
A 1 12  ALA 12  5   5   ALA ALA A . n 
A 1 13  ALA 13  6   6   ALA ALA A . n 
A 1 14  ALA 14  7   7   ALA ALA A . n 
A 1 15  GLY 15  8   ?   ?   ?   A . n 
A 1 16  PRO 16  9   ?   ?   ?   A . n 
A 1 17  GLU 17  10  ?   ?   ?   A . n 
A 1 18  MET 18  11  ?   ?   ?   A . n 
A 1 19  VAL 19  12  ?   ?   ?   A . n 
A 1 20  ARG 20  13  ?   ?   ?   A . n 
A 1 21  GLY 21  14  ?   ?   ?   A . n 
A 1 22  GLN 22  15  15  GLN GLN A . n 
A 1 23  VAL 23  16  16  VAL VAL A . n 
A 1 24  PHE 24  17  17  PHE PHE A . n 
A 1 25  ASP 25  18  18  ASP ASP A . n 
A 1 26  VAL 26  19  19  VAL VAL A . n 
A 1 27  GLY 27  20  20  GLY GLY A . n 
A 1 28  PRO 28  21  21  PRO PRO A . n 
A 1 29  ARG 29  22  22  ARG ARG A . n 
A 1 30  TYR 30  23  23  TYR TYR A . n 
A 1 31  THR 31  24  24  THR THR A . n 
A 1 32  ASN 32  25  25  ASN ASN A . n 
A 1 33  LEU 33  26  26  LEU LEU A . n 
A 1 34  SER 34  27  27  SER SER A . n 
A 1 35  TYR 35  28  28  TYR TYR A . n 
A 1 36  ILE 36  29  29  ILE ILE A . n 
A 1 37  GLY 37  30  30  GLY GLY A . n 
A 1 38  GLU 38  31  31  GLU GLU A . n 
A 1 39  GLY 39  32  32  GLY GLY A . n 
A 1 40  ALA 40  33  33  ALA ALA A . n 
A 1 41  TYR 41  34  34  TYR TYR A . n 
A 1 42  GLY 42  35  35  GLY GLY A . n 
A 1 43  MET 43  36  36  MET MET A . n 
A 1 44  VAL 44  37  37  VAL VAL A . n 
A 1 45  CYS 45  38  38  CYS CYS A . n 
A 1 46  SER 46  39  39  SER SER A . n 
A 1 47  ALA 47  40  40  ALA ALA A . n 
A 1 48  TYR 48  41  41  TYR TYR A . n 
A 1 49  ASP 49  42  42  ASP ASP A . n 
A 1 50  ASN 50  43  43  ASN ASN A . n 
A 1 51  LEU 51  44  44  LEU LEU A . n 
A 1 52  ASN 52  45  45  ASN ASN A . n 
A 1 53  LYS 53  46  46  LYS LYS A . n 
A 1 54  VAL 54  47  47  VAL VAL A . n 
A 1 55  ARG 55  48  48  ARG ARG A . n 
A 1 56  VAL 56  49  49  VAL VAL A . n 
A 1 57  ALA 57  50  50  ALA ALA A . n 
A 1 58  ILE 58  51  51  ILE ILE A . n 
A 1 59  LYS 59  52  52  LYS LYS A . n 
A 1 60  LYS 60  53  53  LYS LYS A . n 
A 1 61  ILE 61  54  54  ILE ILE A . n 
A 1 62  SER 62  55  55  SER SER A . n 
A 1 63  PRO 63  56  56  PRO PRO A . n 
A 1 64  PHE 64  57  57  PHE PHE A . n 
A 1 65  GLU 65  58  58  GLU GLU A . n 
A 1 66  HIS 66  59  59  HIS HIS A . n 
A 1 67  GLN 67  60  60  GLN GLN A . n 
A 1 68  THR 68  61  61  THR THR A . n 
A 1 69  TYR 69  62  62  TYR TYR A . n 
A 1 70  CYS 70  63  63  CYS CYS A . n 
A 1 71  GLN 71  64  64  GLN GLN A . n 
A 1 72  ARG 72  65  65  ARG ARG A . n 
A 1 73  THR 73  66  66  THR THR A . n 
A 1 74  LEU 74  67  67  LEU LEU A . n 
A 1 75  ARG 75  68  68  ARG ARG A . n 
A 1 76  GLU 76  69  69  GLU GLU A . n 
A 1 77  ILE 77  70  70  ILE ILE A . n 
A 1 78  LYS 78  71  71  LYS LYS A . n 
A 1 79  ILE 79  72  72  ILE ILE A . n 
A 1 80  LEU 80  73  73  LEU LEU A . n 
A 1 81  LEU 81  74  74  LEU LEU A . n 
A 1 82  ARG 82  75  75  ARG ARG A . n 
A 1 83  PHE 83  76  76  PHE PHE A . n 
A 1 84  ARG 84  77  77  ARG ARG A . n 
A 1 85  HIS 85  78  78  HIS HIS A . n 
A 1 86  GLU 86  79  79  GLU GLU A . n 
A 1 87  ASN 87  80  80  ASN ASN A . n 
A 1 88  ILE 88  81  81  ILE ILE A . n 
A 1 89  ILE 89  82  82  ILE ILE A . n 
A 1 90  GLY 90  83  83  GLY GLY A . n 
A 1 91  ILE 91  84  84  ILE ILE A . n 
A 1 92  ASN 92  85  85  ASN ASN A . n 
A 1 93  ASP 93  86  86  ASP ASP A . n 
A 1 94  ILE 94  87  87  ILE ILE A . n 
A 1 95  ILE 95  88  88  ILE ILE A . n 
A 1 96  ARG 96  89  89  ARG ARG A . n 
A 1 97  ALA 97  90  90  ALA ALA A . n 
A 1 98  PRO 98  91  91  PRO PRO A . n 
A 1 99  THR 99  92  92  THR THR A . n 
A 1 100 ILE 100 93  93  ILE ILE A . n 
A 1 101 GLU 101 94  94  GLU GLU A . n 
A 1 102 GLN 102 95  95  GLN GLN A . n 
A 1 103 MET 103 96  96  MET MET A . n 
A 1 104 LYS 104 97  97  LYS LYS A . n 
A 1 105 ASP 105 98  98  ASP ASP A . n 
A 1 106 VAL 106 99  99  VAL VAL A . n 
A 1 107 TYR 107 100 100 TYR TYR A . n 
A 1 108 ILE 108 101 101 ILE ILE A . n 
A 1 109 VAL 109 102 102 VAL VAL A . n 
A 1 110 GLN 110 103 103 GLN GLN A . n 
A 1 111 ASP 111 104 104 ASP ASP A . n 
A 1 112 LEU 112 105 105 LEU LEU A . n 
A 1 113 MET 113 106 106 MET MET A . n 
A 1 114 GLU 114 107 107 GLU GLU A . n 
A 1 115 THR 115 108 108 THR THR A . n 
A 1 116 ASP 116 109 109 ASP ASP A . n 
A 1 117 LEU 117 110 110 LEU LEU A . n 
A 1 118 TYR 118 111 111 TYR TYR A . n 
A 1 119 LYS 119 112 112 LYS LYS A . n 
A 1 120 LEU 120 113 113 LEU LEU A . n 
A 1 121 LEU 121 114 114 LEU LEU A . n 
A 1 122 LYS 122 115 115 LYS LYS A . n 
A 1 123 THR 123 116 116 THR THR A . n 
A 1 124 GLN 124 117 117 GLN GLN A . n 
A 1 125 HIS 125 118 118 HIS HIS A . n 
A 1 126 LEU 126 119 119 LEU LEU A . n 
A 1 127 SER 127 120 120 SER SER A . n 
A 1 128 ASN 128 121 121 ASN ASN A . n 
A 1 129 ASP 129 122 122 ASP ASP A . n 
A 1 130 HIS 130 123 123 HIS HIS A . n 
A 1 131 ILE 131 124 124 ILE ILE A . n 
A 1 132 CYS 132 125 125 CYS CYS A . n 
A 1 133 TYR 133 126 126 TYR TYR A . n 
A 1 134 PHE 134 127 127 PHE PHE A . n 
A 1 135 LEU 135 128 128 LEU LEU A . n 
A 1 136 TYR 136 129 129 TYR TYR A . n 
A 1 137 GLN 137 130 130 GLN GLN A . n 
A 1 138 ILE 138 131 131 ILE ILE A . n 
A 1 139 LEU 139 132 132 LEU LEU A . n 
A 1 140 ARG 140 133 133 ARG ARG A . n 
A 1 141 GLY 141 134 134 GLY GLY A . n 
A 1 142 LEU 142 135 135 LEU LEU A . n 
A 1 143 LYS 143 136 136 LYS LYS A . n 
A 1 144 TYR 144 137 137 TYR TYR A . n 
A 1 145 ILE 145 138 138 ILE ILE A . n 
A 1 146 HIS 146 139 139 HIS HIS A . n 
A 1 147 SER 147 140 140 SER SER A . n 
A 1 148 ALA 148 141 141 ALA ALA A . n 
A 1 149 ASN 149 142 142 ASN ASN A . n 
A 1 150 VAL 150 143 143 VAL VAL A . n 
A 1 151 LEU 151 144 144 LEU LEU A . n 
A 1 152 HIS 152 145 145 HIS HIS A . n 
A 1 153 ARG 153 146 146 ARG ARG A . n 
A 1 154 ASP 154 147 147 ASP ASP A . n 
A 1 155 LEU 155 148 148 LEU LEU A . n 
A 1 156 LYS 156 149 149 LYS LYS A . n 
A 1 157 PRO 157 150 150 PRO PRO A . n 
A 1 158 SER 158 151 151 SER SER A . n 
A 1 159 ASN 159 152 152 ASN ASN A . n 
A 1 160 LEU 160 153 153 LEU LEU A . n 
A 1 161 LEU 161 154 154 LEU LEU A . n 
A 1 162 LEU 162 155 155 LEU LEU A . n 
A 1 163 ASN 163 156 156 ASN ASN A . n 
A 1 164 THR 164 157 157 THR THR A . n 
A 1 165 THR 165 158 158 THR THR A . n 
A 1 166 CYS 166 159 159 CYS CYS A . n 
A 1 167 ASP 167 160 160 ASP ASP A . n 
A 1 168 LEU 168 161 161 LEU LEU A . n 
A 1 169 LYS 169 162 162 LYS LYS A . n 
A 1 170 ILE 170 163 163 ILE ILE A . n 
A 1 171 CYS 171 164 164 CYS CYS A . n 
A 1 172 ASP 172 165 165 ASP ASP A . n 
A 1 173 PHE 173 166 166 PHE PHE A . n 
A 1 174 GLY 174 167 167 GLY GLY A . n 
A 1 175 LEU 175 168 168 LEU LEU A . n 
A 1 176 ALA 176 169 169 ALA ALA A . n 
A 1 177 ARG 177 170 170 ARG ARG A . n 
A 1 178 VAL 178 171 171 VAL VAL A . n 
A 1 179 ALA 179 172 172 ALA ALA A . n 
A 1 180 ASP 180 173 173 ASP ASP A . n 
A 1 181 PRO 181 174 174 PRO PRO A . n 
A 1 182 ASP 182 175 175 ASP ASP A . n 
A 1 183 HIS 183 176 176 HIS HIS A . n 
A 1 184 ASP 184 177 177 ASP ASP A . n 
A 1 185 HIS 185 178 178 HIS HIS A . n 
A 1 186 THR 186 179 179 THR THR A . n 
A 1 187 GLY 187 180 180 GLY GLY A . n 
A 1 188 PHE 188 181 181 PHE PHE A . n 
A 1 189 LEU 189 182 182 LEU LEU A . n 
A 1 190 THR 190 183 183 THR THR A . n 
A 1 191 GLU 191 184 184 GLU GLU A . n 
A 1 192 TYR 192 185 185 TYR TYR A . n 
A 1 193 VAL 193 186 186 VAL VAL A . n 
A 1 194 ALA 194 187 187 ALA ALA A . n 
A 1 195 GLU 195 188 188 GLU GLU A . n 
A 1 196 ARG 196 189 189 ARG ARG A . n 
A 1 197 TRP 197 190 190 TRP TRP A . n 
A 1 198 TYR 198 191 191 TYR TYR A . n 
A 1 199 ARG 199 192 192 ARG ARG A . n 
A 1 200 ALA 200 193 193 ALA ALA A . n 
A 1 201 PRO 201 194 194 PRO PRO A . n 
A 1 202 GLU 202 195 195 GLU GLU A . n 
A 1 203 ILE 203 196 196 ILE ILE A . n 
A 1 204 MET 204 197 197 MET MET A . n 
A 1 205 LEU 205 198 198 LEU LEU A . n 
A 1 206 ASN 206 199 199 ASN ASN A . n 
A 1 207 SER 207 200 200 SER SER A . n 
A 1 208 LYS 208 201 201 LYS LYS A . n 
A 1 209 GLY 209 202 202 GLY GLY A . n 
A 1 210 TYR 210 203 203 TYR TYR A . n 
A 1 211 THR 211 204 204 THR THR A . n 
A 1 212 LYS 212 205 205 LYS LYS A . n 
A 1 213 SER 213 206 206 SER SER A . n 
A 1 214 ILE 214 207 207 ILE ILE A . n 
A 1 215 ASP 215 208 208 ASP ASP A . n 
A 1 216 ILE 216 209 209 ILE ILE A . n 
A 1 217 TRP 217 210 210 TRP TRP A . n 
A 1 218 SER 218 211 211 SER SER A . n 
A 1 219 VAL 219 212 212 VAL VAL A . n 
A 1 220 GLY 220 213 213 GLY GLY A . n 
A 1 221 CYS 221 214 214 CYS CYS A . n 
A 1 222 ILE 222 215 215 ILE ILE A . n 
A 1 223 LEU 223 216 216 LEU LEU A . n 
A 1 224 ALA 224 217 217 ALA ALA A . n 
A 1 225 GLU 225 218 218 GLU GLU A . n 
A 1 226 MET 226 219 219 MET MET A . n 
A 1 227 LEU 227 220 220 LEU LEU A . n 
A 1 228 SER 228 221 221 SER SER A . n 
A 1 229 ASN 229 222 222 ASN ASN A . n 
A 1 230 ARG 230 223 223 ARG ARG A . n 
A 1 231 PRO 231 224 224 PRO PRO A . n 
A 1 232 ILE 232 225 225 ILE ILE A . n 
A 1 233 PHE 233 226 226 PHE PHE A . n 
A 1 234 PRO 234 227 227 PRO PRO A . n 
A 1 235 GLY 235 228 228 GLY GLY A . n 
A 1 236 LYS 236 229 229 LYS LYS A . n 
A 1 237 HIS 237 230 230 HIS HIS A . n 
A 1 238 TYR 238 231 231 TYR TYR A . n 
A 1 239 LEU 239 232 232 LEU LEU A . n 
A 1 240 ASP 240 233 233 ASP ASP A . n 
A 1 241 GLN 241 234 234 GLN GLN A . n 
A 1 242 LEU 242 235 235 LEU LEU A . n 
A 1 243 ASN 243 236 236 ASN ASN A . n 
A 1 244 HIS 244 237 237 HIS HIS A . n 
A 1 245 ILE 245 238 238 ILE ILE A . n 
A 1 246 LEU 246 239 239 LEU LEU A . n 
A 1 247 GLY 247 240 240 GLY GLY A . n 
A 1 248 ILE 248 241 241 ILE ILE A . n 
A 1 249 LEU 249 242 242 LEU LEU A . n 
A 1 250 GLY 250 243 243 GLY GLY A . n 
A 1 251 SER 251 244 244 SER SER A . n 
A 1 252 PRO 252 245 245 PRO PRO A . n 
A 1 253 SER 253 246 246 SER SER A . n 
A 1 254 GLN 254 247 247 GLN GLN A . n 
A 1 255 GLU 255 248 248 GLU GLU A . n 
A 1 256 ASP 256 249 249 ASP ASP A . n 
A 1 257 LEU 257 250 250 LEU LEU A . n 
A 1 258 ASN 258 251 251 ASN ASN A . n 
A 1 259 CYS 259 252 252 CYS CYS A . n 
A 1 260 ILE 260 253 253 ILE ILE A . n 
A 1 261 ILE 261 254 254 ILE ILE A . n 
A 1 262 ASN 262 255 255 ASN ASN A . n 
A 1 263 LEU 263 256 256 LEU LEU A . n 
A 1 264 LYS 264 257 257 LYS LYS A . n 
A 1 265 ALA 265 258 258 ALA ALA A . n 
A 1 266 ARG 266 259 259 ARG ARG A . n 
A 1 267 ASN 267 260 260 ASN ASN A . n 
A 1 268 TYR 268 261 261 TYR TYR A . n 
A 1 269 LEU 269 262 262 LEU LEU A . n 
A 1 270 LEU 270 263 263 LEU LEU A . n 
A 1 271 SER 271 264 264 SER SER A . n 
A 1 272 LEU 272 265 265 LEU LEU A . n 
A 1 273 PRO 273 266 266 PRO PRO A . n 
A 1 274 HIS 274 267 267 HIS HIS A . n 
A 1 275 LYS 275 268 268 LYS LYS A . n 
A 1 276 ASN 276 269 269 ASN ASN A . n 
A 1 277 LYS 277 270 270 LYS LYS A . n 
A 1 278 VAL 278 271 271 VAL VAL A . n 
A 1 279 PRO 279 272 272 PRO PRO A . n 
A 1 280 TRP 280 273 273 TRP TRP A . n 
A 1 281 ASN 281 274 274 ASN ASN A . n 
A 1 282 ARG 282 275 275 ARG ARG A . n 
A 1 283 LEU 283 276 276 LEU LEU A . n 
A 1 284 PHE 284 277 277 PHE PHE A . n 
A 1 285 PRO 285 278 278 PRO PRO A . n 
A 1 286 ASN 286 279 279 ASN ASN A . n 
A 1 287 ALA 287 280 280 ALA ALA A . n 
A 1 288 ASP 288 281 281 ASP ASP A . n 
A 1 289 SER 289 282 282 SER SER A . n 
A 1 290 LYS 290 283 283 LYS LYS A . n 
A 1 291 ALA 291 284 284 ALA ALA A . n 
A 1 292 LEU 292 285 285 LEU LEU A . n 
A 1 293 ASP 293 286 286 ASP ASP A . n 
A 1 294 LEU 294 287 287 LEU LEU A . n 
A 1 295 LEU 295 288 288 LEU LEU A . n 
A 1 296 ASP 296 289 289 ASP ASP A . n 
A 1 297 LYS 297 290 290 LYS LYS A . n 
A 1 298 MET 298 291 291 MET MET A . n 
A 1 299 LEU 299 292 292 LEU LEU A . n 
A 1 300 THR 300 293 293 THR THR A . n 
A 1 301 PHE 301 294 294 PHE PHE A . n 
A 1 302 ASN 302 295 295 ASN ASN A . n 
A 1 303 PRO 303 296 296 PRO PRO A . n 
A 1 304 HIS 304 297 297 HIS HIS A . n 
A 1 305 LYS 305 298 298 LYS LYS A . n 
A 1 306 ARG 306 299 299 ARG ARG A . n 
A 1 307 ILE 307 300 300 ILE ILE A . n 
A 1 308 GLU 308 301 301 GLU GLU A . n 
A 1 309 VAL 309 302 302 VAL VAL A . n 
A 1 310 GLU 310 303 303 GLU GLU A . n 
A 1 311 GLN 311 304 304 GLN GLN A . n 
A 1 312 ALA 312 305 305 ALA ALA A . n 
A 1 313 LEU 313 306 306 LEU LEU A . n 
A 1 314 ALA 314 307 307 ALA ALA A . n 
A 1 315 HIS 315 308 308 HIS HIS A . n 
A 1 316 PRO 316 309 309 PRO PRO A . n 
A 1 317 TYR 317 310 310 TYR TYR A . n 
A 1 318 LEU 318 311 311 LEU LEU A . n 
A 1 319 GLU 319 312 312 GLU GLU A . n 
A 1 320 GLN 320 313 313 GLN GLN A . n 
A 1 321 TYR 321 314 314 TYR TYR A . n 
A 1 322 TYR 322 315 315 TYR TYR A . n 
A 1 323 ASP 323 316 316 ASP ASP A . n 
A 1 324 PRO 324 317 317 PRO PRO A . n 
A 1 325 SER 325 318 318 SER SER A . n 
A 1 326 ASP 326 319 319 ASP ASP A . n 
A 1 327 GLU 327 320 320 GLU GLU A . n 
A 1 328 PRO 328 321 321 PRO PRO A . n 
A 1 329 ILE 329 322 322 ILE ILE A . n 
A 1 330 ALA 330 323 323 ALA ALA A . n 
A 1 331 GLU 331 324 324 GLU GLU A . n 
A 1 332 ALA 332 325 325 ALA ALA A . n 
A 1 333 PRO 333 326 326 PRO PRO A . n 
A 1 334 PHE 334 327 327 PHE PHE A . n 
A 1 335 LYS 335 328 328 LYS LYS A . n 
A 1 336 PHE 336 329 329 PHE PHE A . n 
A 1 337 ASP 337 330 330 ASP ASP A . n 
A 1 338 MET 338 331 331 MET MET A . n 
A 1 339 GLU 339 332 332 GLU GLU A . n 
A 1 340 LEU 340 333 333 LEU LEU A . n 
A 1 341 ASP 341 334 334 ASP ASP A . n 
A 1 342 ASP 342 335 335 ASP ASP A . n 
A 1 343 LEU 343 336 336 LEU LEU A . n 
A 1 344 PRO 344 337 337 PRO PRO A . n 
A 1 345 LYS 345 338 338 LYS LYS A . n 
A 1 346 GLU 346 339 339 GLU GLU A . n 
A 1 347 LYS 347 340 340 LYS LYS A . n 
A 1 348 LEU 348 341 341 LEU LEU A . n 
A 1 349 LYS 349 342 342 LYS LYS A . n 
A 1 350 GLU 350 343 343 GLU GLU A . n 
A 1 351 LEU 351 344 344 LEU LEU A . n 
A 1 352 ILE 352 345 345 ILE ILE A . n 
A 1 353 PHE 353 346 346 PHE PHE A . n 
A 1 354 GLU 354 347 347 GLU GLU A . n 
A 1 355 GLU 355 348 348 GLU GLU A . n 
A 1 356 THR 356 349 349 THR THR A . n 
A 1 357 ALA 357 350 350 ALA ALA A . n 
A 1 358 ARG 358 351 351 ARG ARG A . n 
A 1 359 PHE 359 352 352 PHE PHE A . n 
A 1 360 GLN 360 353 353 GLN GLN A . n 
A 1 361 PRO 361 354 354 PRO PRO A . n 
A 1 362 GLY 362 355 ?   ?   ?   A . n 
A 1 363 TYR 363 356 ?   ?   ?   A . n 
A 1 364 ARG 364 357 ?   ?   ?   A . n 
A 1 365 SER 365 358 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        ANP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   ANP 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 ANP 1   501 501 ANP ANP A . 
C 3 HOH 1   601 92  HOH HOH A . 
C 3 HOH 2   602 46  HOH HOH A . 
C 3 HOH 3   603 53  HOH HOH A . 
C 3 HOH 4   604 60  HOH HOH A . 
C 3 HOH 5   605 54  HOH HOH A . 
C 3 HOH 6   606 111 HOH HOH A . 
C 3 HOH 7   607 33  HOH HOH A . 
C 3 HOH 8   608 105 HOH HOH A . 
C 3 HOH 9   609 109 HOH HOH A . 
C 3 HOH 10  610 20  HOH HOH A . 
C 3 HOH 11  611 11  HOH HOH A . 
C 3 HOH 12  612 9   HOH HOH A . 
C 3 HOH 13  613 49  HOH HOH A . 
C 3 HOH 14  614 87  HOH HOH A . 
C 3 HOH 15  615 68  HOH HOH A . 
C 3 HOH 16  616 39  HOH HOH A . 
C 3 HOH 17  617 57  HOH HOH A . 
C 3 HOH 18  618 118 HOH HOH A . 
C 3 HOH 19  619 78  HOH HOH A . 
C 3 HOH 20  620 104 HOH HOH A . 
C 3 HOH 21  621 73  HOH HOH A . 
C 3 HOH 22  622 95  HOH HOH A . 
C 3 HOH 23  623 133 HOH HOH A . 
C 3 HOH 24  624 93  HOH HOH A . 
C 3 HOH 25  625 3   HOH HOH A . 
C 3 HOH 26  626 108 HOH HOH A . 
C 3 HOH 27  627 76  HOH HOH A . 
C 3 HOH 28  628 69  HOH HOH A . 
C 3 HOH 29  629 52  HOH HOH A . 
C 3 HOH 30  630 4   HOH HOH A . 
C 3 HOH 31  631 99  HOH HOH A . 
C 3 HOH 32  632 114 HOH HOH A . 
C 3 HOH 33  633 47  HOH HOH A . 
C 3 HOH 34  634 63  HOH HOH A . 
C 3 HOH 35  635 8   HOH HOH A . 
C 3 HOH 36  636 16  HOH HOH A . 
C 3 HOH 37  637 31  HOH HOH A . 
C 3 HOH 38  638 6   HOH HOH A . 
C 3 HOH 39  639 59  HOH HOH A . 
C 3 HOH 40  640 56  HOH HOH A . 
C 3 HOH 41  641 86  HOH HOH A . 
C 3 HOH 42  642 123 HOH HOH A . 
C 3 HOH 43  643 61  HOH HOH A . 
C 3 HOH 44  644 42  HOH HOH A . 
C 3 HOH 45  645 12  HOH HOH A . 
C 3 HOH 46  646 17  HOH HOH A . 
C 3 HOH 47  647 25  HOH HOH A . 
C 3 HOH 48  648 64  HOH HOH A . 
C 3 HOH 49  649 128 HOH HOH A . 
C 3 HOH 50  650 103 HOH HOH A . 
C 3 HOH 51  651 37  HOH HOH A . 
C 3 HOH 52  652 94  HOH HOH A . 
C 3 HOH 53  653 1   HOH HOH A . 
C 3 HOH 54  654 26  HOH HOH A . 
C 3 HOH 55  655 55  HOH HOH A . 
C 3 HOH 56  656 75  HOH HOH A . 
C 3 HOH 57  657 88  HOH HOH A . 
C 3 HOH 58  658 2   HOH HOH A . 
C 3 HOH 59  659 66  HOH HOH A . 
C 3 HOH 60  660 58  HOH HOH A . 
C 3 HOH 61  661 30  HOH HOH A . 
C 3 HOH 62  662 40  HOH HOH A . 
C 3 HOH 63  663 32  HOH HOH A . 
C 3 HOH 64  664 107 HOH HOH A . 
C 3 HOH 65  665 48  HOH HOH A . 
C 3 HOH 66  666 24  HOH HOH A . 
C 3 HOH 67  667 13  HOH HOH A . 
C 3 HOH 68  668 19  HOH HOH A . 
C 3 HOH 69  669 81  HOH HOH A . 
C 3 HOH 70  670 43  HOH HOH A . 
C 3 HOH 71  671 97  HOH HOH A . 
C 3 HOH 72  672 121 HOH HOH A . 
C 3 HOH 73  673 22  HOH HOH A . 
C 3 HOH 74  674 5   HOH HOH A . 
C 3 HOH 75  675 7   HOH HOH A . 
C 3 HOH 76  676 117 HOH HOH A . 
C 3 HOH 77  677 51  HOH HOH A . 
C 3 HOH 78  678 14  HOH HOH A . 
C 3 HOH 79  679 91  HOH HOH A . 
C 3 HOH 80  680 110 HOH HOH A . 
C 3 HOH 81  681 79  HOH HOH A . 
C 3 HOH 82  682 45  HOH HOH A . 
C 3 HOH 83  683 34  HOH HOH A . 
C 3 HOH 84  684 84  HOH HOH A . 
C 3 HOH 85  685 65  HOH HOH A . 
C 3 HOH 86  686 77  HOH HOH A . 
C 3 HOH 87  687 102 HOH HOH A . 
C 3 HOH 88  688 10  HOH HOH A . 
C 3 HOH 89  689 15  HOH HOH A . 
C 3 HOH 90  690 29  HOH HOH A . 
C 3 HOH 91  691 112 HOH HOH A . 
C 3 HOH 92  692 106 HOH HOH A . 
C 3 HOH 93  693 116 HOH HOH A . 
C 3 HOH 94  694 23  HOH HOH A . 
C 3 HOH 95  695 127 HOH HOH A . 
C 3 HOH 96  696 62  HOH HOH A . 
C 3 HOH 97  697 21  HOH HOH A . 
C 3 HOH 98  698 74  HOH HOH A . 
C 3 HOH 99  699 38  HOH HOH A . 
C 3 HOH 100 700 27  HOH HOH A . 
C 3 HOH 101 701 80  HOH HOH A . 
C 3 HOH 102 702 28  HOH HOH A . 
C 3 HOH 103 703 72  HOH HOH A . 
C 3 HOH 104 704 71  HOH HOH A . 
C 3 HOH 105 705 35  HOH HOH A . 
C 3 HOH 106 706 126 HOH HOH A . 
C 3 HOH 107 707 41  HOH HOH A . 
C 3 HOH 108 708 131 HOH HOH A . 
C 3 HOH 109 709 70  HOH HOH A . 
C 3 HOH 110 710 36  HOH HOH A . 
C 3 HOH 111 711 67  HOH HOH A . 
C 3 HOH 112 712 115 HOH HOH A . 
C 3 HOH 113 713 89  HOH HOH A . 
C 3 HOH 114 714 85  HOH HOH A . 
C 3 HOH 115 715 96  HOH HOH A . 
C 3 HOH 116 716 90  HOH HOH A . 
C 3 HOH 117 717 124 HOH HOH A . 
# 
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       ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? 5.8.0258 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? MOSFLM   ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP   ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   109.61 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8RQW 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     48.913 
_cell.length_a_esd                 ? 
_cell.length_b                     70.601 
_cell.length_b_esd                 ? 
_cell.length_c                     60.409 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_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                         8RQW 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8RQW 
_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             2.33 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.10 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1M sodium hepes pH=7, 4% v/v PEG 400 and 2M ammonium sulfate.' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 2M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-02-25 
_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   0.9655 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ESRF BEAMLINE MASSIF-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9655 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MASSIF-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8RQW 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.8 
_reflns.d_resolution_low                               44.3 
_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                                     35528 
_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                           89.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.0 
_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                                   0.979 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.8 
_reflns_shell.d_res_low                                     1.83 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.9 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2110 
_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                                  0.587 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.00 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            0.00 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               33.308 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.956 
_refine.correlation_coeff_Fo_to_Fc_free          0.942 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 8RQW 
_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                             44.30 
_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                     33681 
_refine.ls_number_reflns_R_free                  1828 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.76 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.19777 
_refine.ls_R_factor_R_free                       0.23058 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.19594 
_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                    MASK 
_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       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.133 
_refine.pdbx_overall_ESU_R_Free                  0.126 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                 ? 
_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                             3.444 
_refine.overall_SU_ML                            0.102 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.80 
_refine_hist.d_res_low                        44.30 
_refine_hist.number_atoms_solvent             117 
_refine_hist.number_atoms_total               2955 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2807 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         31 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.010  0.013  2911 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.017  2695 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.643  1.648  3954 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.338  1.576  6270 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.067  5.000  344  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 34.938 22.675 157  ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 16.190 15.000 513  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 23.324 15.000 17   ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.079  0.200  379  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  3186 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  592  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 3.013  3.285  1376 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.005  3.283  1375 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 4.327  4.910  1717 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.326  4.913  1718 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.778  3.830  1535 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.778  3.830  1535 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.826  5.599  2237 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 7.954  38.744 3255 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 7.988  38.721 3243 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.800 
_refine_ls_shell.d_res_low                        1.847 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             123 
_refine_ls_shell.number_reflns_R_work             2485 
_refine_ls_shell.percent_reflns_obs               99.62 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.306 
_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   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.304 
# 
_struct.entry_id                     8RQW 
_struct.title                        'Erk2 MAP kinase (T188E) AMP-PNP complex' 
_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        8RQW 
_struct_keywords.text            'MAP kinases, SIGNAL TRANSDUCTION, PHOSPHORYLATION, erk, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    MK01_RAT 
_struct_ref.pdbx_db_accession          P63086 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MAAAAAAGPEMVRGQVFDVGPRYTNLSYIGEGAYGMVCSAYDNLNKVRVAIKKISPFEHQTYCQRTLREIKILLRFRHEN
IIGINDIIRAPTIEQMKDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCD
LKICDFGLARVADPDHDHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILG
ILGSPSQEDLNCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQYYDPSDE
PIAEAPFKFDMELDDLPKEKLKELIFEETARFQPGYRS
;
_struct_ref.pdbx_align_begin           0 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8RQW 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 8 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 365 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P63086 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  358 
_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       358 
# 
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 8RQW ALA A 1   ? UNP P63086 ?   ?   'expression tag'      -6  1 
1 8RQW HIS A 2   ? UNP P63086 ?   ?   'expression tag'      -5  2 
1 8RQW HIS A 3   ? UNP P63086 ?   ?   'expression tag'      -4  3 
1 8RQW HIS A 4   ? UNP P63086 ?   ?   'expression tag'      -3  4 
1 8RQW HIS A 5   ? UNP P63086 ?   ?   'expression tag'      -2  5 
1 8RQW HIS A 6   ? UNP P63086 ?   ?   'expression tag'      -1  6 
1 8RQW HIS A 7   ? UNP P63086 ?   ?   'expression tag'      0   7 
1 8RQW GLU A 195 ? UNP P63086 THR 188 'engineered mutation' 188 8 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
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)' 800   ? 
1 MORE         -5    ? 
1 'SSA (A^2)'  16160 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 66  ? PHE A 83  ? HIS A 59  PHE A 76  1 ? 18 
HELX_P HELX_P2  AA2 LEU A 117 ? GLN A 124 ? LEU A 110 GLN A 117 1 ? 8  
HELX_P HELX_P3  AA3 SER A 127 ? ALA A 148 ? SER A 120 ALA A 141 1 ? 22 
HELX_P HELX_P4  AA4 LYS A 156 ? SER A 158 ? LYS A 149 SER A 151 5 ? 3  
HELX_P HELX_P5  AA5 ASP A 180 ? ASP A 184 ? ASP A 173 ASP A 177 5 ? 5  
HELX_P HELX_P6  AA6 GLU A 195 ? ARG A 199 ? GLU A 188 ARG A 192 5 ? 5  
HELX_P HELX_P7  AA7 ALA A 200 ? ASN A 206 ? ALA A 193 ASN A 199 1 ? 7  
HELX_P HELX_P8  AA8 LYS A 212 ? ASN A 229 ? LYS A 205 ASN A 222 1 ? 18 
HELX_P HELX_P9  AA9 HIS A 237 ? GLY A 250 ? HIS A 230 GLY A 243 1 ? 14 
HELX_P HELX_P10 AB1 SER A 253 ? CYS A 259 ? SER A 246 CYS A 252 1 ? 7  
HELX_P HELX_P11 AB2 ASN A 262 ? LEU A 272 ? ASN A 255 LEU A 265 1 ? 11 
HELX_P HELX_P12 AB3 PRO A 279 ? PHE A 284 ? PRO A 272 PHE A 277 1 ? 6  
HELX_P HELX_P13 AB4 ASP A 288 ? LEU A 299 ? ASP A 281 LEU A 292 1 ? 12 
HELX_P HELX_P14 AB5 GLU A 308 ? ALA A 314 ? GLU A 301 ALA A 307 1 ? 7  
HELX_P HELX_P15 AB6 HIS A 315 ? GLU A 319 ? HIS A 308 GLU A 312 5 ? 5  
HELX_P HELX_P16 AB7 ASP A 323 ? GLU A 327 ? ASP A 316 GLU A 320 5 ? 5  
HELX_P HELX_P17 AB8 PRO A 344 ? THR A 356 ? PRO A 337 THR A 349 1 ? 13 
HELX_P HELX_P18 AB9 ALA A 357 ? GLN A 360 ? ALA A 350 GLN A 353 5 ? 4  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TYR A 30  ? GLU A 38  ? TYR A 23  GLU A 31  
AA1 2 MET A 43  ? ASP A 49  ? MET A 36  ASP A 42  
AA1 3 VAL A 54  ? ILE A 61  ? VAL A 47  ILE A 54  
AA1 4 VAL A 106 ? ASP A 111 ? VAL A 99  ASP A 104 
AA1 5 ASP A 93  ? ILE A 95  ? ASP A 86  ILE A 88  
AA2 1 THR A 115 ? ASP A 116 ? THR A 108 ASP A 109 
AA2 2 LEU A 160 ? LEU A 162 ? LEU A 153 LEU A 155 
AA2 3 LEU A 168 ? ILE A 170 ? LEU A 161 ILE A 163 
AA3 1 VAL A 150 ? LEU A 151 ? VAL A 143 LEU A 144 
AA3 2 ARG A 177 ? VAL A 178 ? ARG A 170 VAL A 171 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N THR A 31  ? N THR A 24  O TYR A 48  ? O TYR A 41  
AA1 2 3 N CYS A 45  ? N CYS A 38  O ILE A 58  ? O ILE A 51  
AA1 3 4 N ILE A 61  ? N ILE A 54  O VAL A 106 ? O VAL A 99  
AA1 4 5 O VAL A 109 ? O VAL A 102 N ASP A 93  ? N ASP A 86  
AA2 1 2 N THR A 115 ? N THR A 108 O LEU A 162 ? O LEU A 155 
AA2 2 3 N LEU A 161 ? N LEU A 154 O LYS A 169 ? O LYS A 162 
AA3 1 2 N LEU A 151 ? N LEU A 144 O ARG A 177 ? O ARG A 170 
# 
_pdbx_entry_details.entry_id                   8RQW 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 89 ? ? CZ A ARG 89 ? ? NH1 A ARG 89 ? ? 126.14 120.30 5.84  0.50 N 
2 1 NE A ARG 89 ? ? CZ A ARG 89 ? ? NH2 A ARG 89 ? ? 114.59 120.30 -5.71 0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ALA A 33  ? ? -66.09  -70.57 
2 1 ASP A 147 ? ? -144.40 40.95  
3 1 ASP A 165 ? ? 67.86   79.37  
4 1 ASP A 173 ? ? -153.99 72.08  
5 1 ASN A 199 ? ? -161.54 15.21  
6 1 TYR A 231 ? ? -29.79  -61.70 
7 1 LEU A 292 ? ? -102.74 53.29  
# 
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 ALA -6  ? A ALA 1   
2  1 Y 1 A HIS -5  ? A HIS 2   
3  1 Y 1 A HIS -4  ? A HIS 3   
4  1 Y 1 A HIS -3  ? A HIS 4   
5  1 Y 1 A HIS -2  ? A HIS 5   
6  1 Y 1 A HIS -1  ? A HIS 6   
7  1 Y 1 A HIS 0   ? A HIS 7   
8  1 Y 1 A MET 1   ? A MET 8   
9  1 Y 1 A ALA 2   ? A ALA 9   
10 1 Y 1 A ALA 3   ? A ALA 10  
11 1 Y 1 A GLY 8   ? A GLY 15  
12 1 Y 1 A PRO 9   ? A PRO 16  
13 1 Y 1 A GLU 10  ? A GLU 17  
14 1 Y 1 A MET 11  ? A MET 18  
15 1 Y 1 A VAL 12  ? A VAL 19  
16 1 Y 1 A ARG 13  ? A ARG 20  
17 1 Y 1 A GLY 14  ? A GLY 21  
18 1 Y 1 A GLY 355 ? A GLY 362 
19 1 Y 1 A TYR 356 ? A TYR 363 
20 1 Y 1 A ARG 357 ? A ARG 364 
21 1 Y 1 A SER 358 ? A SER 365 
# 
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  
ANP PG     P N N 14  
ANP O1G    O N N 15  
ANP O2G    O N N 16  
ANP O3G    O N N 17  
ANP PB     P N N 18  
ANP O1B    O N N 19  
ANP O2B    O N N 20  
ANP N3B    N N N 21  
ANP PA     P N N 22  
ANP O1A    O N N 23  
ANP O2A    O N N 24  
ANP O3A    O N N 25  
ANP "O5'"  O N N 26  
ANP "C5'"  C N N 27  
ANP "C4'"  C N R 28  
ANP "O4'"  O N N 29  
ANP "C3'"  C N S 30  
ANP "O3'"  O N N 31  
ANP "C2'"  C N R 32  
ANP "O2'"  O N N 33  
ANP "C1'"  C N R 34  
ANP N9     N Y N 35  
ANP C8     C Y N 36  
ANP N7     N Y N 37  
ANP C5     C Y N 38  
ANP C6     C Y N 39  
ANP N6     N N N 40  
ANP N1     N Y N 41  
ANP C2     C Y N 42  
ANP N3     N Y N 43  
ANP C4     C Y N 44  
ANP HOG2   H N N 45  
ANP HOG3   H N N 46  
ANP HOB2   H N N 47  
ANP HNB1   H N N 48  
ANP HOA2   H N N 49  
ANP "H5'1" H N N 50  
ANP "H5'2" H N N 51  
ANP "H4'"  H N N 52  
ANP "H3'"  H N N 53  
ANP "HO3'" H N N 54  
ANP "H2'"  H N N 55  
ANP "HO2'" H N N 56  
ANP "H1'"  H N N 57  
ANP H8     H N N 58  
ANP HN61   H N N 59  
ANP HN62   H N N 60  
ANP H2     H N N 61  
ARG N      N N N 62  
ARG CA     C N S 63  
ARG C      C N N 64  
ARG O      O N N 65  
ARG CB     C N N 66  
ARG CG     C N N 67  
ARG CD     C N N 68  
ARG NE     N N N 69  
ARG CZ     C N N 70  
ARG NH1    N N N 71  
ARG NH2    N N N 72  
ARG OXT    O N N 73  
ARG H      H N N 74  
ARG H2     H N N 75  
ARG HA     H N N 76  
ARG HB2    H N N 77  
ARG HB3    H N N 78  
ARG HG2    H N N 79  
ARG HG3    H N N 80  
ARG HD2    H N N 81  
ARG HD3    H N N 82  
ARG HE     H N N 83  
ARG HH11   H N N 84  
ARG HH12   H N N 85  
ARG HH21   H N N 86  
ARG HH22   H N N 87  
ARG HXT    H N N 88  
ASN N      N N N 89  
ASN CA     C N S 90  
ASN C      C N N 91  
ASN O      O N N 92  
ASN CB     C N N 93  
ASN CG     C N N 94  
ASN OD1    O N N 95  
ASN ND2    N N N 96  
ASN OXT    O N N 97  
ASN H      H N N 98  
ASN H2     H N N 99  
ASN HA     H N N 100 
ASN HB2    H N N 101 
ASN HB3    H N N 102 
ASN HD21   H N N 103 
ASN HD22   H N N 104 
ASN HXT    H N N 105 
ASP N      N N N 106 
ASP CA     C N S 107 
ASP C      C N N 108 
ASP O      O N N 109 
ASP CB     C N N 110 
ASP CG     C N N 111 
ASP OD1    O N N 112 
ASP OD2    O N N 113 
ASP OXT    O N N 114 
ASP H      H N N 115 
ASP H2     H N N 116 
ASP HA     H N N 117 
ASP HB2    H N N 118 
ASP HB3    H N N 119 
ASP HD2    H N N 120 
ASP HXT    H N N 121 
CYS N      N N N 122 
CYS CA     C N R 123 
CYS C      C N N 124 
CYS O      O N N 125 
CYS CB     C N N 126 
CYS SG     S N N 127 
CYS OXT    O N N 128 
CYS H      H N N 129 
CYS H2     H N N 130 
CYS HA     H N N 131 
CYS HB2    H N N 132 
CYS HB3    H N N 133 
CYS HG     H N N 134 
CYS HXT    H N N 135 
GLN N      N N N 136 
GLN CA     C N S 137 
GLN C      C N N 138 
GLN O      O N N 139 
GLN CB     C N N 140 
GLN CG     C N N 141 
GLN CD     C N N 142 
GLN OE1    O N N 143 
GLN NE2    N N N 144 
GLN OXT    O N N 145 
GLN H      H N N 146 
GLN H2     H N N 147 
GLN HA     H N N 148 
GLN HB2    H N N 149 
GLN HB3    H N N 150 
GLN HG2    H N N 151 
GLN HG3    H N N 152 
GLN HE21   H N N 153 
GLN HE22   H N N 154 
GLN HXT    H N N 155 
GLU N      N N N 156 
GLU CA     C N S 157 
GLU C      C N N 158 
GLU O      O N N 159 
GLU CB     C N N 160 
GLU CG     C N N 161 
GLU CD     C N N 162 
GLU OE1    O N N 163 
GLU OE2    O N N 164 
GLU OXT    O N N 165 
GLU H      H N N 166 
GLU H2     H N N 167 
GLU HA     H N N 168 
GLU HB2    H N N 169 
GLU HB3    H N N 170 
GLU HG2    H N N 171 
GLU HG3    H N N 172 
GLU HE2    H N N 173 
GLU HXT    H N N 174 
GLY N      N N N 175 
GLY CA     C N N 176 
GLY C      C N N 177 
GLY O      O N N 178 
GLY OXT    O N N 179 
GLY H      H N N 180 
GLY H2     H N N 181 
GLY HA2    H N N 182 
GLY HA3    H N N 183 
GLY HXT    H N N 184 
HIS N      N N N 185 
HIS CA     C N S 186 
HIS C      C N N 187 
HIS O      O N N 188 
HIS CB     C N N 189 
HIS CG     C Y N 190 
HIS ND1    N Y N 191 
HIS CD2    C Y N 192 
HIS CE1    C Y N 193 
HIS NE2    N Y N 194 
HIS OXT    O N N 195 
HIS H      H N N 196 
HIS H2     H N N 197 
HIS HA     H N N 198 
HIS HB2    H N N 199 
HIS HB3    H N N 200 
HIS HD1    H N N 201 
HIS HD2    H N N 202 
HIS HE1    H N N 203 
HIS HE2    H N N 204 
HIS HXT    H N N 205 
HOH O      O N N 206 
HOH H1     H N N 207 
HOH H2     H N N 208 
ILE N      N N N 209 
ILE CA     C N S 210 
ILE C      C N N 211 
ILE O      O N N 212 
ILE CB     C N S 213 
ILE CG1    C N N 214 
ILE CG2    C N N 215 
ILE CD1    C N N 216 
ILE OXT    O N N 217 
ILE H      H N N 218 
ILE H2     H N N 219 
ILE HA     H N N 220 
ILE HB     H N N 221 
ILE HG12   H N N 222 
ILE HG13   H N N 223 
ILE HG21   H N N 224 
ILE HG22   H N N 225 
ILE HG23   H N N 226 
ILE HD11   H N N 227 
ILE HD12   H N N 228 
ILE HD13   H N N 229 
ILE HXT    H N N 230 
LEU N      N N N 231 
LEU CA     C N S 232 
LEU C      C N N 233 
LEU O      O N N 234 
LEU CB     C N N 235 
LEU CG     C N N 236 
LEU CD1    C N N 237 
LEU CD2    C N N 238 
LEU OXT    O N N 239 
LEU H      H N N 240 
LEU H2     H N N 241 
LEU HA     H N N 242 
LEU HB2    H N N 243 
LEU HB3    H N N 244 
LEU HG     H N N 245 
LEU HD11   H N N 246 
LEU HD12   H N N 247 
LEU HD13   H N N 248 
LEU HD21   H N N 249 
LEU HD22   H N N 250 
LEU HD23   H N N 251 
LEU HXT    H N N 252 
LYS N      N N N 253 
LYS CA     C N S 254 
LYS C      C N N 255 
LYS O      O N N 256 
LYS CB     C N N 257 
LYS CG     C N N 258 
LYS CD     C N N 259 
LYS CE     C N N 260 
LYS NZ     N N N 261 
LYS OXT    O N N 262 
LYS H      H N N 263 
LYS H2     H N N 264 
LYS HA     H N N 265 
LYS HB2    H N N 266 
LYS HB3    H N N 267 
LYS HG2    H N N 268 
LYS HG3    H N N 269 
LYS HD2    H N N 270 
LYS HD3    H N N 271 
LYS HE2    H N N 272 
LYS HE3    H N N 273 
LYS HZ1    H N N 274 
LYS HZ2    H N N 275 
LYS HZ3    H N N 276 
LYS HXT    H N N 277 
MET N      N N N 278 
MET CA     C N S 279 
MET C      C N N 280 
MET O      O N N 281 
MET CB     C N N 282 
MET CG     C N N 283 
MET SD     S N N 284 
MET CE     C N N 285 
MET OXT    O N N 286 
MET H      H N N 287 
MET H2     H N N 288 
MET HA     H N N 289 
MET HB2    H N N 290 
MET HB3    H N N 291 
MET HG2    H N N 292 
MET HG3    H N N 293 
MET HE1    H N N 294 
MET HE2    H N N 295 
MET HE3    H N N 296 
MET HXT    H N N 297 
PHE N      N N N 298 
PHE CA     C N S 299 
PHE C      C N N 300 
PHE O      O N N 301 
PHE CB     C N N 302 
PHE CG     C Y N 303 
PHE CD1    C Y N 304 
PHE CD2    C Y N 305 
PHE CE1    C Y N 306 
PHE CE2    C Y N 307 
PHE CZ     C Y N 308 
PHE OXT    O N N 309 
PHE H      H N N 310 
PHE H2     H N N 311 
PHE HA     H N N 312 
PHE HB2    H N N 313 
PHE HB3    H N N 314 
PHE HD1    H N N 315 
PHE HD2    H N N 316 
PHE HE1    H N N 317 
PHE HE2    H N N 318 
PHE HZ     H N N 319 
PHE HXT    H N N 320 
PRO N      N N N 321 
PRO CA     C N S 322 
PRO C      C N N 323 
PRO O      O N N 324 
PRO CB     C N N 325 
PRO CG     C N N 326 
PRO CD     C N N 327 
PRO OXT    O N N 328 
PRO H      H N N 329 
PRO HA     H N N 330 
PRO HB2    H N N 331 
PRO HB3    H N N 332 
PRO HG2    H N N 333 
PRO HG3    H N N 334 
PRO HD2    H N N 335 
PRO HD3    H N N 336 
PRO HXT    H N N 337 
SER N      N N N 338 
SER CA     C N S 339 
SER C      C N N 340 
SER O      O N N 341 
SER CB     C N N 342 
SER OG     O N N 343 
SER OXT    O N N 344 
SER H      H N N 345 
SER H2     H N N 346 
SER HA     H N N 347 
SER HB2    H N N 348 
SER HB3    H N N 349 
SER HG     H N N 350 
SER HXT    H N N 351 
THR N      N N N 352 
THR CA     C N S 353 
THR C      C N N 354 
THR O      O N N 355 
THR CB     C N R 356 
THR OG1    O N N 357 
THR CG2    C N N 358 
THR OXT    O N N 359 
THR H      H N N 360 
THR H2     H N N 361 
THR HA     H N N 362 
THR HB     H N N 363 
THR HG1    H N N 364 
THR HG21   H N N 365 
THR HG22   H N N 366 
THR HG23   H N N 367 
THR HXT    H N N 368 
TRP N      N N N 369 
TRP CA     C N S 370 
TRP C      C N N 371 
TRP O      O N N 372 
TRP CB     C N N 373 
TRP CG     C Y N 374 
TRP CD1    C Y N 375 
TRP CD2    C Y N 376 
TRP NE1    N Y N 377 
TRP CE2    C Y N 378 
TRP CE3    C Y N 379 
TRP CZ2    C Y N 380 
TRP CZ3    C Y N 381 
TRP CH2    C Y N 382 
TRP OXT    O N N 383 
TRP H      H N N 384 
TRP H2     H N N 385 
TRP HA     H N N 386 
TRP HB2    H N N 387 
TRP HB3    H N N 388 
TRP HD1    H N N 389 
TRP HE1    H N N 390 
TRP HE3    H N N 391 
TRP HZ2    H N N 392 
TRP HZ3    H N N 393 
TRP HH2    H N N 394 
TRP HXT    H N N 395 
TYR N      N N N 396 
TYR CA     C N S 397 
TYR C      C N N 398 
TYR O      O N N 399 
TYR CB     C N N 400 
TYR CG     C Y N 401 
TYR CD1    C Y N 402 
TYR CD2    C Y N 403 
TYR CE1    C Y N 404 
TYR CE2    C Y N 405 
TYR CZ     C Y N 406 
TYR OH     O N N 407 
TYR OXT    O N N 408 
TYR H      H N N 409 
TYR H2     H N N 410 
TYR HA     H N N 411 
TYR HB2    H N N 412 
TYR HB3    H N N 413 
TYR HD1    H N N 414 
TYR HD2    H N N 415 
TYR HE1    H N N 416 
TYR HE2    H N N 417 
TYR HH     H N N 418 
TYR HXT    H N N 419 
VAL N      N N N 420 
VAL CA     C N S 421 
VAL C      C N N 422 
VAL O      O N N 423 
VAL CB     C N N 424 
VAL CG1    C N N 425 
VAL CG2    C N N 426 
VAL OXT    O N N 427 
VAL H      H N N 428 
VAL H2     H N N 429 
VAL HA     H N N 430 
VAL HB     H N N 431 
VAL HG11   H N N 432 
VAL HG12   H N N 433 
VAL HG13   H N N 434 
VAL HG21   H N N 435 
VAL HG22   H N N 436 
VAL HG23   H N N 437 
VAL HXT    H N N 438 
# 
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  
ANP PG    O1G    doub N N 13  
ANP PG    O2G    sing N N 14  
ANP PG    O3G    sing N N 15  
ANP PG    N3B    sing N N 16  
ANP O2G   HOG2   sing N N 17  
ANP O3G   HOG3   sing N N 18  
ANP PB    O1B    doub N N 19  
ANP PB    O2B    sing N N 20  
ANP PB    N3B    sing N N 21  
ANP PB    O3A    sing N N 22  
ANP O2B   HOB2   sing N N 23  
ANP N3B   HNB1   sing N N 24  
ANP PA    O1A    doub N N 25  
ANP PA    O2A    sing N N 26  
ANP PA    O3A    sing N N 27  
ANP PA    "O5'"  sing N N 28  
ANP O2A   HOA2   sing N N 29  
ANP "O5'" "C5'"  sing N N 30  
ANP "C5'" "C4'"  sing N N 31  
ANP "C5'" "H5'1" sing N N 32  
ANP "C5'" "H5'2" sing N N 33  
ANP "C4'" "O4'"  sing N N 34  
ANP "C4'" "C3'"  sing N N 35  
ANP "C4'" "H4'"  sing N N 36  
ANP "O4'" "C1'"  sing N N 37  
ANP "C3'" "O3'"  sing N N 38  
ANP "C3'" "C2'"  sing N N 39  
ANP "C3'" "H3'"  sing N N 40  
ANP "O3'" "HO3'" sing N N 41  
ANP "C2'" "O2'"  sing N N 42  
ANP "C2'" "C1'"  sing N N 43  
ANP "C2'" "H2'"  sing N N 44  
ANP "O2'" "HO2'" sing N N 45  
ANP "C1'" N9     sing N N 46  
ANP "C1'" "H1'"  sing N N 47  
ANP N9    C8     sing Y N 48  
ANP N9    C4     sing Y N 49  
ANP C8    N7     doub Y N 50  
ANP C8    H8     sing N N 51  
ANP N7    C5     sing Y N 52  
ANP C5    C6     sing Y N 53  
ANP C5    C4     doub Y N 54  
ANP C6    N6     sing N N 55  
ANP C6    N1     doub Y N 56  
ANP N6    HN61   sing N N 57  
ANP N6    HN62   sing N N 58  
ANP N1    C2     sing Y N 59  
ANP C2    N3     doub Y N 60  
ANP C2    H2     sing N N 61  
ANP N3    C4     sing Y N 62  
ARG N     CA     sing N N 63  
ARG N     H      sing N N 64  
ARG N     H2     sing N N 65  
ARG CA    C      sing N N 66  
ARG CA    CB     sing N N 67  
ARG CA    HA     sing N N 68  
ARG C     O      doub N N 69  
ARG C     OXT    sing N N 70  
ARG CB    CG     sing N N 71  
ARG CB    HB2    sing N N 72  
ARG CB    HB3    sing N N 73  
ARG CG    CD     sing N N 74  
ARG CG    HG2    sing N N 75  
ARG CG    HG3    sing N N 76  
ARG CD    NE     sing N N 77  
ARG CD    HD2    sing N N 78  
ARG CD    HD3    sing N N 79  
ARG NE    CZ     sing N N 80  
ARG NE    HE     sing N N 81  
ARG CZ    NH1    sing N N 82  
ARG CZ    NH2    doub N N 83  
ARG NH1   HH11   sing N N 84  
ARG NH1   HH12   sing N N 85  
ARG NH2   HH21   sing N N 86  
ARG NH2   HH22   sing N N 87  
ARG OXT   HXT    sing N N 88  
ASN N     CA     sing N N 89  
ASN N     H      sing N N 90  
ASN N     H2     sing N N 91  
ASN CA    C      sing N N 92  
ASN CA    CB     sing N N 93  
ASN CA    HA     sing N N 94  
ASN C     O      doub N N 95  
ASN C     OXT    sing N N 96  
ASN CB    CG     sing N N 97  
ASN CB    HB2    sing N N 98  
ASN CB    HB3    sing N N 99  
ASN CG    OD1    doub N N 100 
ASN CG    ND2    sing N N 101 
ASN ND2   HD21   sing N N 102 
ASN ND2   HD22   sing N N 103 
ASN OXT   HXT    sing N N 104 
ASP N     CA     sing N N 105 
ASP N     H      sing N N 106 
ASP N     H2     sing N N 107 
ASP CA    C      sing N N 108 
ASP CA    CB     sing N N 109 
ASP CA    HA     sing N N 110 
ASP C     O      doub N N 111 
ASP C     OXT    sing N N 112 
ASP CB    CG     sing N N 113 
ASP CB    HB2    sing N N 114 
ASP CB    HB3    sing N N 115 
ASP CG    OD1    doub N N 116 
ASP CG    OD2    sing N N 117 
ASP OD2   HD2    sing N N 118 
ASP OXT   HXT    sing N N 119 
CYS N     CA     sing N N 120 
CYS N     H      sing N N 121 
CYS N     H2     sing N N 122 
CYS CA    C      sing N N 123 
CYS CA    CB     sing N N 124 
CYS CA    HA     sing N N 125 
CYS C     O      doub N N 126 
CYS C     OXT    sing N N 127 
CYS CB    SG     sing N N 128 
CYS CB    HB2    sing N N 129 
CYS CB    HB3    sing N N 130 
CYS SG    HG     sing N N 131 
CYS OXT   HXT    sing N N 132 
GLN N     CA     sing N N 133 
GLN N     H      sing N N 134 
GLN N     H2     sing N N 135 
GLN CA    C      sing N N 136 
GLN CA    CB     sing N N 137 
GLN CA    HA     sing N N 138 
GLN C     O      doub N N 139 
GLN C     OXT    sing N N 140 
GLN CB    CG     sing N N 141 
GLN CB    HB2    sing N N 142 
GLN CB    HB3    sing N N 143 
GLN CG    CD     sing N N 144 
GLN CG    HG2    sing N N 145 
GLN CG    HG3    sing N N 146 
GLN CD    OE1    doub N N 147 
GLN CD    NE2    sing N N 148 
GLN NE2   HE21   sing N N 149 
GLN NE2   HE22   sing N N 150 
GLN OXT   HXT    sing N N 151 
GLU N     CA     sing N N 152 
GLU N     H      sing N N 153 
GLU N     H2     sing N N 154 
GLU CA    C      sing N N 155 
GLU CA    CB     sing N N 156 
GLU CA    HA     sing N N 157 
GLU C     O      doub N N 158 
GLU C     OXT    sing N N 159 
GLU CB    CG     sing N N 160 
GLU CB    HB2    sing N N 161 
GLU CB    HB3    sing N N 162 
GLU CG    CD     sing N N 163 
GLU CG    HG2    sing N N 164 
GLU CG    HG3    sing N N 165 
GLU CD    OE1    doub N N 166 
GLU CD    OE2    sing N N 167 
GLU OE2   HE2    sing N N 168 
GLU OXT   HXT    sing N N 169 
GLY N     CA     sing N N 170 
GLY N     H      sing N N 171 
GLY N     H2     sing N N 172 
GLY CA    C      sing N N 173 
GLY CA    HA2    sing N N 174 
GLY CA    HA3    sing N N 175 
GLY C     O      doub N N 176 
GLY C     OXT    sing N N 177 
GLY OXT   HXT    sing N N 178 
HIS N     CA     sing N N 179 
HIS N     H      sing N N 180 
HIS N     H2     sing N N 181 
HIS CA    C      sing N N 182 
HIS CA    CB     sing N N 183 
HIS CA    HA     sing N N 184 
HIS C     O      doub N N 185 
HIS C     OXT    sing N N 186 
HIS CB    CG     sing N N 187 
HIS CB    HB2    sing N N 188 
HIS CB    HB3    sing N N 189 
HIS CG    ND1    sing Y N 190 
HIS CG    CD2    doub Y N 191 
HIS ND1   CE1    doub Y N 192 
HIS ND1   HD1    sing N N 193 
HIS CD2   NE2    sing Y N 194 
HIS CD2   HD2    sing N N 195 
HIS CE1   NE2    sing Y N 196 
HIS CE1   HE1    sing N N 197 
HIS NE2   HE2    sing N N 198 
HIS OXT   HXT    sing N N 199 
HOH O     H1     sing N N 200 
HOH O     H2     sing N N 201 
ILE N     CA     sing N N 202 
ILE N     H      sing N N 203 
ILE N     H2     sing N N 204 
ILE CA    C      sing N N 205 
ILE CA    CB     sing N N 206 
ILE CA    HA     sing N N 207 
ILE C     O      doub N N 208 
ILE C     OXT    sing N N 209 
ILE CB    CG1    sing N N 210 
ILE CB    CG2    sing N N 211 
ILE CB    HB     sing N N 212 
ILE CG1   CD1    sing N N 213 
ILE CG1   HG12   sing N N 214 
ILE CG1   HG13   sing N N 215 
ILE CG2   HG21   sing N N 216 
ILE CG2   HG22   sing N N 217 
ILE CG2   HG23   sing N N 218 
ILE CD1   HD11   sing N N 219 
ILE CD1   HD12   sing N N 220 
ILE CD1   HD13   sing N N 221 
ILE OXT   HXT    sing N N 222 
LEU N     CA     sing N N 223 
LEU N     H      sing N N 224 
LEU N     H2     sing N N 225 
LEU CA    C      sing N N 226 
LEU CA    CB     sing N N 227 
LEU CA    HA     sing N N 228 
LEU C     O      doub N N 229 
LEU C     OXT    sing N N 230 
LEU CB    CG     sing N N 231 
LEU CB    HB2    sing N N 232 
LEU CB    HB3    sing N N 233 
LEU CG    CD1    sing N N 234 
LEU CG    CD2    sing N N 235 
LEU CG    HG     sing N N 236 
LEU CD1   HD11   sing N N 237 
LEU CD1   HD12   sing N N 238 
LEU CD1   HD13   sing N N 239 
LEU CD2   HD21   sing N N 240 
LEU CD2   HD22   sing N N 241 
LEU CD2   HD23   sing N N 242 
LEU OXT   HXT    sing N N 243 
LYS N     CA     sing N N 244 
LYS N     H      sing N N 245 
LYS N     H2     sing N N 246 
LYS CA    C      sing N N 247 
LYS CA    CB     sing N N 248 
LYS CA    HA     sing N N 249 
LYS C     O      doub N N 250 
LYS C     OXT    sing N N 251 
LYS CB    CG     sing N N 252 
LYS CB    HB2    sing N N 253 
LYS CB    HB3    sing N N 254 
LYS CG    CD     sing N N 255 
LYS CG    HG2    sing N N 256 
LYS CG    HG3    sing N N 257 
LYS CD    CE     sing N N 258 
LYS CD    HD2    sing N N 259 
LYS CD    HD3    sing N N 260 
LYS CE    NZ     sing N N 261 
LYS CE    HE2    sing N N 262 
LYS CE    HE3    sing N N 263 
LYS NZ    HZ1    sing N N 264 
LYS NZ    HZ2    sing N N 265 
LYS NZ    HZ3    sing N N 266 
LYS OXT   HXT    sing N N 267 
MET N     CA     sing N N 268 
MET N     H      sing N N 269 
MET N     H2     sing N N 270 
MET CA    C      sing N N 271 
MET CA    CB     sing N N 272 
MET CA    HA     sing N N 273 
MET C     O      doub N N 274 
MET C     OXT    sing N N 275 
MET CB    CG     sing N N 276 
MET CB    HB2    sing N N 277 
MET CB    HB3    sing N N 278 
MET CG    SD     sing N N 279 
MET CG    HG2    sing N N 280 
MET CG    HG3    sing N N 281 
MET SD    CE     sing N N 282 
MET CE    HE1    sing N N 283 
MET CE    HE2    sing N N 284 
MET CE    HE3    sing N N 285 
MET OXT   HXT    sing N N 286 
PHE N     CA     sing N N 287 
PHE N     H      sing N N 288 
PHE N     H2     sing N N 289 
PHE CA    C      sing N N 290 
PHE CA    CB     sing N N 291 
PHE CA    HA     sing N N 292 
PHE C     O      doub N N 293 
PHE C     OXT    sing N N 294 
PHE CB    CG     sing N N 295 
PHE CB    HB2    sing N N 296 
PHE CB    HB3    sing N N 297 
PHE CG    CD1    doub Y N 298 
PHE CG    CD2    sing Y N 299 
PHE CD1   CE1    sing Y N 300 
PHE CD1   HD1    sing N N 301 
PHE CD2   CE2    doub Y N 302 
PHE CD2   HD2    sing N N 303 
PHE CE1   CZ     doub Y N 304 
PHE CE1   HE1    sing N N 305 
PHE CE2   CZ     sing Y N 306 
PHE CE2   HE2    sing N N 307 
PHE CZ    HZ     sing N N 308 
PHE OXT   HXT    sing N N 309 
PRO N     CA     sing N N 310 
PRO N     CD     sing N N 311 
PRO N     H      sing N N 312 
PRO CA    C      sing N N 313 
PRO CA    CB     sing N N 314 
PRO CA    HA     sing N N 315 
PRO C     O      doub N N 316 
PRO C     OXT    sing N N 317 
PRO CB    CG     sing N N 318 
PRO CB    HB2    sing N N 319 
PRO CB    HB3    sing N N 320 
PRO CG    CD     sing N N 321 
PRO CG    HG2    sing N N 322 
PRO CG    HG3    sing N N 323 
PRO CD    HD2    sing N N 324 
PRO CD    HD3    sing N N 325 
PRO OXT   HXT    sing N N 326 
SER N     CA     sing N N 327 
SER N     H      sing N N 328 
SER N     H2     sing N N 329 
SER CA    C      sing N N 330 
SER CA    CB     sing N N 331 
SER CA    HA     sing N N 332 
SER C     O      doub N N 333 
SER C     OXT    sing N N 334 
SER CB    OG     sing N N 335 
SER CB    HB2    sing N N 336 
SER CB    HB3    sing N N 337 
SER OG    HG     sing N N 338 
SER OXT   HXT    sing N N 339 
THR N     CA     sing N N 340 
THR N     H      sing N N 341 
THR N     H2     sing N N 342 
THR CA    C      sing N N 343 
THR CA    CB     sing N N 344 
THR CA    HA     sing N N 345 
THR C     O      doub N N 346 
THR C     OXT    sing N N 347 
THR CB    OG1    sing N N 348 
THR CB    CG2    sing N N 349 
THR CB    HB     sing N N 350 
THR OG1   HG1    sing N N 351 
THR CG2   HG21   sing N N 352 
THR CG2   HG22   sing N N 353 
THR CG2   HG23   sing N N 354 
THR OXT   HXT    sing N N 355 
TRP N     CA     sing N N 356 
TRP N     H      sing N N 357 
TRP N     H2     sing N N 358 
TRP CA    C      sing N N 359 
TRP CA    CB     sing N N 360 
TRP CA    HA     sing N N 361 
TRP C     O      doub N N 362 
TRP C     OXT    sing N N 363 
TRP CB    CG     sing N N 364 
TRP CB    HB2    sing N N 365 
TRP CB    HB3    sing N N 366 
TRP CG    CD1    doub Y N 367 
TRP CG    CD2    sing Y N 368 
TRP CD1   NE1    sing Y N 369 
TRP CD1   HD1    sing N N 370 
TRP CD2   CE2    doub Y N 371 
TRP CD2   CE3    sing Y N 372 
TRP NE1   CE2    sing Y N 373 
TRP NE1   HE1    sing N N 374 
TRP CE2   CZ2    sing Y N 375 
TRP CE3   CZ3    doub Y N 376 
TRP CE3   HE3    sing N N 377 
TRP CZ2   CH2    doub Y N 378 
TRP CZ2   HZ2    sing N N 379 
TRP CZ3   CH2    sing Y N 380 
TRP CZ3   HZ3    sing N N 381 
TRP CH2   HH2    sing N N 382 
TRP OXT   HXT    sing N N 383 
TYR N     CA     sing N N 384 
TYR N     H      sing N N 385 
TYR N     H2     sing N N 386 
TYR CA    C      sing N N 387 
TYR CA    CB     sing N N 388 
TYR CA    HA     sing N N 389 
TYR C     O      doub N N 390 
TYR C     OXT    sing N N 391 
TYR CB    CG     sing N N 392 
TYR CB    HB2    sing N N 393 
TYR CB    HB3    sing N N 394 
TYR CG    CD1    doub Y N 395 
TYR CG    CD2    sing Y N 396 
TYR CD1   CE1    sing Y N 397 
TYR CD1   HD1    sing N N 398 
TYR CD2   CE2    doub Y N 399 
TYR CD2   HD2    sing N N 400 
TYR CE1   CZ     doub Y N 401 
TYR CE1   HE1    sing N N 402 
TYR CE2   CZ     sing Y N 403 
TYR CE2   HE2    sing N N 404 
TYR CZ    OH     sing N N 405 
TYR OH    HH     sing N N 406 
TYR OXT   HXT    sing N N 407 
VAL N     CA     sing N N 408 
VAL N     H      sing N N 409 
VAL N     H2     sing N N 410 
VAL CA    C      sing N N 411 
VAL CA    CB     sing N N 412 
VAL CA    HA     sing N N 413 
VAL C     O      doub N N 414 
VAL C     OXT    sing N N 415 
VAL CB    CG1    sing N N 416 
VAL CB    CG2    sing N N 417 
VAL CB    HB     sing N N 418 
VAL CG1   HG11   sing N N 419 
VAL CG1   HG12   sing N N 420 
VAL CG1   HG13   sing N N 421 
VAL CG2   HG21   sing N N 422 
VAL CG2   HG22   sing N N 423 
VAL CG2   HG23   sing N N 424 
VAL OXT   HXT    sing N N 425 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4S32 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8RQW 
_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]   0.020444 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.007285 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014164 
_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]   0.017573 
_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 
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     . ALA A 1 11  ? -11.655 21.928  -8.532  1.00 52.68  ? 4   ALA A N     1 
ATOM   2    C CA    . ALA A 1 11  ? -10.962 21.396  -7.332  1.00 52.96  ? 4   ALA A CA    1 
ATOM   3    C C     . ALA A 1 11  ? -11.576 22.023  -6.071  1.00 58.27  ? 4   ALA A C     1 
ATOM   4    O O     . ALA A 1 11  ? -11.437 23.255  -5.909  1.00 55.97  ? 4   ALA A O     1 
ATOM   5    C CB    . ALA A 1 11  ? -9.485  21.688  -7.436  1.00 56.24  ? 4   ALA A CB    1 
ATOM   6    N N     . ALA A 1 12  ? -12.240 21.223  -5.222  1.00 61.59  ? 5   ALA A N     1 
ATOM   7    C CA    . ALA A 1 12  ? -12.735 21.625  -3.880  1.00 62.96  ? 5   ALA A CA    1 
ATOM   8    C C     . ALA A 1 12  ? -11.607 22.342  -3.117  1.00 61.09  ? 5   ALA A C     1 
ATOM   9    O O     . ALA A 1 12  ? -10.448 21.914  -3.223  1.00 57.30  ? 5   ALA A O     1 
ATOM   10   C CB    . ALA A 1 12  ? -13.239 20.412  -3.128  1.00 62.82  ? 5   ALA A CB    1 
ATOM   11   N N     . ALA A 1 13  ? -11.918 23.431  -2.413  1.00 63.18  ? 6   ALA A N     1 
ATOM   12   C CA    . ALA A 1 13  ? -10.923 24.292  -1.730  1.00 61.80  ? 6   ALA A CA    1 
ATOM   13   C C     . ALA A 1 13  ? -11.328 24.442  -0.262  1.00 59.83  ? 6   ALA A C     1 
ATOM   14   O O     . ALA A 1 13  ? -12.524 24.251  0.019   1.00 58.88  ? 6   ALA A O     1 
ATOM   15   C CB    . ALA A 1 13  ? -10.830 25.628  -2.429  1.00 62.22  ? 6   ALA A CB    1 
ATOM   16   N N     . ALA A 1 14  ? -10.376 24.768  0.624   1.00 60.26  ? 7   ALA A N     1 
ATOM   17   C CA    . ALA A 1 14  ? -10.590 24.903  2.087   1.00 58.55  ? 7   ALA A CA    1 
ATOM   18   C C     . ALA A 1 14  ? -9.655  25.965  2.686   1.00 58.71  ? 7   ALA A C     1 
ATOM   19   O O     . ALA A 1 14  ? -8.429  25.866  2.453   1.00 55.45  ? 7   ALA A O     1 
ATOM   20   C CB    . ALA A 1 14  ? -10.401 23.559  2.744   1.00 61.96  ? 7   ALA A CB    1 
ATOM   21   N N     . GLN A 1 22  ? -6.322  25.810  0.930   1.00 65.95  ? 15  GLN A N     1 
ATOM   22   C CA    . GLN A 1 22  ? -6.073  26.025  -0.521  1.00 63.65  ? 15  GLN A CA    1 
ATOM   23   C C     . GLN A 1 22  ? -6.846  24.957  -1.311  1.00 56.59  ? 15  GLN A C     1 
ATOM   24   O O     . GLN A 1 22  ? -8.023  24.682  -0.988  1.00 53.78  ? 15  GLN A O     1 
ATOM   25   C CB    . GLN A 1 22  ? -4.563  25.990  -0.811  1.00 66.77  ? 15  GLN A CB    1 
ATOM   26   C CG    . GLN A 1 22  ? -4.162  26.694  -2.116  1.00 73.20  ? 15  GLN A CG    1 
ATOM   27   C CD    . GLN A 1 22  ? -3.234  25.934  -3.047  1.00 74.98  ? 15  GLN A CD    1 
ATOM   28   O OE1   . GLN A 1 22  ? -2.901  26.396  -4.141  1.00 70.06  ? 15  GLN A OE1   1 
ATOM   29   N NE2   . GLN A 1 22  ? -2.814  24.749  -2.638  1.00 74.49  ? 15  GLN A NE2   1 
ATOM   30   N N     . VAL A 1 23  ? -6.213  24.375  -2.325  1.00 51.04  ? 16  VAL A N     1 
ATOM   31   C CA    . VAL A 1 23  ? -6.733  23.188  -3.050  1.00 49.81  ? 16  VAL A CA    1 
ATOM   32   C C     . VAL A 1 23  ? -6.731  22.030  -2.049  1.00 46.44  ? 16  VAL A C     1 
ATOM   33   O O     . VAL A 1 23  ? -5.692  21.787  -1.439  1.00 49.30  ? 16  VAL A O     1 
ATOM   34   C CB    . VAL A 1 23  ? -5.886  22.881  -4.299  1.00 51.04  ? 16  VAL A CB    1 
ATOM   35   C CG1   . VAL A 1 23  ? -6.307  21.588  -4.973  1.00 52.53  ? 16  VAL A CG1   1 
ATOM   36   C CG2   . VAL A 1 23  ? -5.921  24.034  -5.291  1.00 55.32  ? 16  VAL A CG2   1 
ATOM   37   N N     . PHE A 1 24  ? -7.875  21.385  -1.878  1.00 44.73  ? 17  PHE A N     1 
ATOM   38   C CA    . PHE A 1 24  ? -8.048  20.126  -1.121  1.00 46.21  ? 17  PHE A CA    1 
ATOM   39   C C     . PHE A 1 24  ? -8.850  19.184  -2.017  1.00 39.53  ? 17  PHE A C     1 
ATOM   40   O O     . PHE A 1 24  ? -10.057 19.027  -1.855  1.00 45.68  ? 17  PHE A O     1 
ATOM   41   C CB    . PHE A 1 24  ? -8.674  20.404  0.244   1.00 47.31  ? 17  PHE A CB    1 
ATOM   42   C CG    . PHE A 1 24  ? -8.242  19.407  1.285   1.00 45.36  ? 17  PHE A CG    1 
ATOM   43   C CD1   . PHE A 1 24  ? -8.865  18.173  1.374   1.00 48.21  ? 17  PHE A CD1   1 
ATOM   44   C CD2   . PHE A 1 24  ? -7.196  19.691  2.144   1.00 46.29  ? 17  PHE A CD2   1 
ATOM   45   C CE1   . PHE A 1 24  ? -8.450  17.233  2.306   1.00 45.53  ? 17  PHE A CE1   1 
ATOM   46   C CE2   . PHE A 1 24  ? -6.793  18.760  3.092   1.00 48.62  ? 17  PHE A CE2   1 
ATOM   47   C CZ    . PHE A 1 24  ? -7.420  17.532  3.167   1.00 46.97  ? 17  PHE A CZ    1 
ATOM   48   N N     . ASP A 1 25  ? -8.134  18.584  -2.959  1.00 40.02  ? 18  ASP A N     1 
ATOM   49   C CA    . ASP A 1 25  ? -8.672  18.008  -4.208  1.00 40.12  ? 18  ASP A CA    1 
ATOM   50   C C     . ASP A 1 25  ? -8.851  16.506  -4.003  1.00 37.90  ? 18  ASP A C     1 
ATOM   51   O O     . ASP A 1 25  ? -8.062  15.702  -4.514  1.00 35.76  ? 18  ASP A O     1 
ATOM   52   C CB    . ASP A 1 25  ? -7.732  18.357  -5.361  1.00 41.89  ? 18  ASP A CB    1 
ATOM   53   C CG    . ASP A 1 25  ? -8.229  17.855  -6.700  1.00 42.74  ? 18  ASP A CG    1 
ATOM   54   O OD1   . ASP A 1 25  ? -9.462  17.627  -6.817  1.00 37.17  ? 18  ASP A OD1   1 
ATOM   55   O OD2   . ASP A 1 25  ? -7.371  17.689  -7.598  1.00 47.17  ? 18  ASP A OD2   1 
ATOM   56   N N     . VAL A 1 26  ? -9.849  16.136  -3.227  1.00 38.62  ? 19  VAL A N     1 
ATOM   57   C CA    . VAL A 1 26  ? -10.033 14.723  -2.799  1.00 45.71  ? 19  VAL A CA    1 
ATOM   58   C C     . VAL A 1 26  ? -11.247 14.221  -3.567  1.00 52.99  ? 19  VAL A C     1 
ATOM   59   O O     . VAL A 1 26  ? -12.021 13.401  -3.025  1.00 52.32  ? 19  VAL A O     1 
ATOM   60   C CB    . VAL A 1 26  ? -10.100 14.614  -1.265  1.00 40.89  ? 19  VAL A CB    1 
ATOM   61   C CG1   . VAL A 1 26  ? -8.789  15.068  -0.670  1.00 39.04  ? 19  VAL A CG1   1 
ATOM   62   C CG2   . VAL A 1 26  ? -11.235 15.429  -0.661  1.00 45.98  ? 19  VAL A CG2   1 
ATOM   63   N N     . GLY A 1 27  ? -11.352 14.763  -4.792  1.00 64.90  ? 20  GLY A N     1 
ATOM   64   C CA    . GLY A 1 27  ? -12.134 14.264  -5.934  1.00 57.87  ? 20  GLY A CA    1 
ATOM   65   C C     . GLY A 1 27  ? -13.599 14.225  -5.566  1.00 62.63  ? 20  GLY A C     1 
ATOM   66   O O     . GLY A 1 27  ? -14.029 14.986  -4.704  1.00 64.57  ? 20  GLY A O     1 
ATOM   67   N N     . PRO A 1 28  ? -14.373 13.289  -6.145  1.00 63.50  ? 21  PRO A N     1 
ATOM   68   C CA    . PRO A 1 28  ? -15.804 13.224  -5.876  1.00 62.61  ? 21  PRO A CA    1 
ATOM   69   C C     . PRO A 1 28  ? -16.124 12.438  -4.598  1.00 52.62  ? 21  PRO A C     1 
ATOM   70   O O     . PRO A 1 28  ? -17.126 12.730  -3.974  1.00 44.61  ? 21  PRO A O     1 
ATOM   71   C CB    . PRO A 1 28  ? -16.297 12.465  -7.115  1.00 66.43  ? 21  PRO A CB    1 
ATOM   72   C CG    . PRO A 1 28  ? -15.183 11.455  -7.375  1.00 68.84  ? 21  PRO A CG    1 
ATOM   73   C CD    . PRO A 1 28  ? -13.912 12.211  -7.040  1.00 66.71  ? 21  PRO A CD    1 
ATOM   74   N N     . ARG A 1 29  ? -15.289 11.446  -4.268  1.00 48.21  ? 22  ARG A N     1 
ATOM   75   C CA    . ARG A 1 29  ? -15.590 10.432  -3.223  1.00 48.84  ? 22  ARG A CA    1 
ATOM   76   C C     . ARG A 1 29  ? -15.718 11.137  -1.858  1.00 41.27  ? 22  ARG A C     1 
ATOM   77   O O     . ARG A 1 29  ? -16.647 10.812  -1.111  1.00 46.39  ? 22  ARG A O     1 
ATOM   78   C CB    . ARG A 1 29  ? -14.542 9.322   -3.257  1.00 44.13  ? 22  ARG A CB    1 
ATOM   79   C CG    . ARG A 1 29  ? -14.246 8.712   -1.901  1.00 50.06  ? 22  ARG A CG    1 
ATOM   80   C CD    . ARG A 1 29  ? -14.705 7.294   -1.703  1.00 52.99  ? 22  ARG A CD    1 
ATOM   81   N NE    . ARG A 1 29  ? -13.634 6.355   -1.985  1.00 54.54  ? 22  ARG A NE    1 
ATOM   82   C CZ    . ARG A 1 29  ? -13.256 5.338   -1.211  1.00 51.16  ? 22  ARG A CZ    1 
ATOM   83   N NH1   . ARG A 1 29  ? -13.841 5.093   -0.057  1.00 53.67  ? 22  ARG A NH1   1 
ATOM   84   N NH2   . ARG A 1 29  ? -12.276 4.555   -1.602  1.00 53.82  ? 22  ARG A NH2   1 
ATOM   85   N N     . TYR A 1 30  ? -14.864 12.113  -1.579  1.00 40.07  ? 23  TYR A N     1 
ATOM   86   C CA    . TYR A 1 30  ? -14.722 12.714  -0.231  1.00 42.86  ? 23  TYR A CA    1 
ATOM   87   C C     . TYR A 1 30  ? -15.190 14.170  -0.336  1.00 44.02  ? 23  TYR A C     1 
ATOM   88   O O     . TYR A 1 30  ? -14.566 14.961  -1.075  1.00 41.55  ? 23  TYR A O     1 
ATOM   89   C CB    . TYR A 1 30  ? -13.298 12.491  0.294   1.00 38.69  ? 23  TYR A CB    1 
ATOM   90   C CG    . TYR A 1 30  ? -12.796 11.058  0.295   1.00 38.65  ? 23  TYR A CG    1 
ATOM   91   C CD1   . TYR A 1 30  ? -13.161 10.158  1.291   1.00 36.56  ? 23  TYR A CD1   1 
ATOM   92   C CD2   . TYR A 1 30  ? -11.857 10.618  -0.639  1.00 36.41  ? 23  TYR A CD2   1 
ATOM   93   C CE1   . TYR A 1 30  ? -12.689 8.848   1.314   1.00 34.95  ? 23  TYR A CE1   1 
ATOM   94   C CE2   . TYR A 1 30  ? -11.384 9.309   -0.638  1.00 34.36  ? 23  TYR A CE2   1 
ATOM   95   C CZ    . TYR A 1 30  ? -11.778 8.426   0.359   1.00 36.67  ? 23  TYR A CZ    1 
ATOM   96   O OH    . TYR A 1 30  ? -11.298 7.151   0.390   1.00 32.22  ? 23  TYR A OH    1 
ATOM   97   N N     . THR A 1 31  ? -16.274 14.492  0.380   1.00 49.89  ? 24  THR A N     1 
ATOM   98   C CA    . THR A 1 31  ? -17.021 15.785  0.321   1.00 52.76  ? 24  THR A CA    1 
ATOM   99   C C     . THR A 1 31  ? -17.199 16.358  1.741   1.00 52.79  ? 24  THR A C     1 
ATOM   100  O O     . THR A 1 31  ? -16.700 15.738  2.690   1.00 51.19  ? 24  THR A O     1 
ATOM   101  C CB    . THR A 1 31  ? -18.366 15.561  -0.387  1.00 48.86  ? 24  THR A CB    1 
ATOM   102  O OG1   . THR A 1 31  ? -19.084 14.553  0.320   1.00 46.13  ? 24  THR A OG1   1 
ATOM   103  C CG2   . THR A 1 31  ? -18.209 15.129  -1.830  1.00 46.75  ? 24  THR A CG2   1 
ATOM   104  N N     . ASN A 1 32  ? -17.868 17.505  1.875   1.00 52.44  ? 25  ASN A N     1 
ATOM   105  C CA    . ASN A 1 32  ? -18.227 18.104  3.188   1.00 54.47  ? 25  ASN A CA    1 
ATOM   106  C C     . ASN A 1 32  ? -16.953 18.278  4.026   1.00 56.78  ? 25  ASN A C     1 
ATOM   107  O O     . ASN A 1 32  ? -16.947 17.882  5.208   1.00 60.41  ? 25  ASN A O     1 
ATOM   108  C CB    . ASN A 1 32  ? -19.260 17.238  3.919   1.00 59.01  ? 25  ASN A CB    1 
ATOM   109  C CG    . ASN A 1 32  ? -20.317 16.679  2.991   1.00 68.78  ? 25  ASN A CG    1 
ATOM   110  O OD1   . ASN A 1 32  ? -20.669 17.301  1.991   1.00 69.80  ? 25  ASN A OD1   1 
ATOM   111  N ND2   . ASN A 1 32  ? -20.809 15.490  3.298   1.00 77.56  ? 25  ASN A ND2   1 
ATOM   112  N N     . LEU A 1 33  ? -15.909 18.851  3.434   1.00 50.40  ? 26  LEU A N     1 
ATOM   113  C CA    . LEU A 1 33  ? -14.605 19.063  4.104   1.00 53.94  ? 26  LEU A CA    1 
ATOM   114  C C     . LEU A 1 33  ? -14.820 20.011  5.291   1.00 56.04  ? 26  LEU A C     1 
ATOM   115  O O     . LEU A 1 33  ? -15.652 20.938  5.166   1.00 55.88  ? 26  LEU A O     1 
ATOM   116  C CB    . LEU A 1 33  ? -13.605 19.644  3.100   1.00 55.02  ? 26  LEU A CB    1 
ATOM   117  C CG    . LEU A 1 33  ? -12.960 18.690  2.085   1.00 54.56  ? 26  LEU A CG    1 
ATOM   118  C CD1   . LEU A 1 33  ? -13.814 17.466  1.771   1.00 55.23  ? 26  LEU A CD1   1 
ATOM   119  C CD2   . LEU A 1 33  ? -12.636 19.443  0.800   1.00 51.20  ? 26  LEU A CD2   1 
ATOM   120  N N     . SER A 1 34  ? -14.117 19.774  6.398   1.00 49.68  ? 27  SER A N     1 
ATOM   121  C CA    . SER A 1 34  ? -14.069 20.673  7.579   1.00 54.50  ? 27  SER A CA    1 
ATOM   122  C C     . SER A 1 34  ? -12.639 20.713  8.115   1.00 52.55  ? 27  SER A C     1 
ATOM   123  O O     . SER A 1 34  ? -12.114 19.656  8.471   1.00 54.43  ? 27  SER A O     1 
ATOM   124  C CB    . SER A 1 34  ? -15.048 20.261  8.646   1.00 55.97  ? 27  SER A CB    1 
ATOM   125  O OG    . SER A 1 34  ? -15.248 21.324  9.559   1.00 59.12  ? 27  SER A OG    1 
ATOM   126  N N     . TYR A 1 35  ? -12.046 21.904  8.121   1.00 56.65  ? 28  TYR A N     1 
ATOM   127  C CA    . TYR A 1 35  ? -10.660 22.178  8.553   1.00 58.03  ? 28  TYR A CA    1 
ATOM   128  C C     . TYR A 1 35  ? -10.500 21.732  10.009  1.00 64.30  ? 28  TYR A C     1 
ATOM   129  O O     . TYR A 1 35  ? -11.104 22.373  10.888  1.00 69.86  ? 28  TYR A O     1 
ATOM   130  C CB    . TYR A 1 35  ? -10.350 23.664  8.374   1.00 58.30  ? 28  TYR A CB    1 
ATOM   131  C CG    . TYR A 1 35  ? -8.980  24.070  8.849   1.00 61.44  ? 28  TYR A CG    1 
ATOM   132  C CD1   . TYR A 1 35  ? -8.748  24.412  10.174  1.00 61.59  ? 28  TYR A CD1   1 
ATOM   133  C CD2   . TYR A 1 35  ? -7.911  24.121  7.971   1.00 61.75  ? 28  TYR A CD2   1 
ATOM   134  C CE1   . TYR A 1 35  ? -7.490  24.790  10.613  1.00 59.96  ? 28  TYR A CE1   1 
ATOM   135  C CE2   . TYR A 1 35  ? -6.646  24.499  8.392   1.00 61.23  ? 28  TYR A CE2   1 
ATOM   136  C CZ    . TYR A 1 35  ? -6.436  24.833  9.718   1.00 62.27  ? 28  TYR A CZ    1 
ATOM   137  O OH    . TYR A 1 35  ? -5.190  25.194  10.132  1.00 67.34  ? 28  TYR A OH    1 
ATOM   138  N N     . ILE A 1 36  ? -9.737  20.660  10.243  1.00 59.93  ? 29  ILE A N     1 
ATOM   139  C CA    . ILE A 1 36  ? -9.425  20.134  11.604  1.00 63.14  ? 29  ILE A CA    1 
ATOM   140  C C     . ILE A 1 36  ? -7.902  20.136  11.781  1.00 68.54  ? 29  ILE A C     1 
ATOM   141  O O     . ILE A 1 36  ? -7.343  19.106  12.237  1.00 78.19  ? 29  ILE A O     1 
ATOM   142  C CB    . ILE A 1 36  ? -10.079 18.753  11.856  1.00 62.35  ? 29  ILE A CB    1 
ATOM   143  C CG1   . ILE A 1 36  ? -9.652  17.689  10.848  1.00 64.70  ? 29  ILE A CG1   1 
ATOM   144  C CG2   . ILE A 1 36  ? -11.598 18.869  11.902  1.00 66.36  ? 29  ILE A CG2   1 
ATOM   145  C CD1   . ILE A 1 36  ? -9.932  16.279  11.307  1.00 66.16  ? 29  ILE A CD1   1 
ATOM   146  N N     . GLY A 1 37  ? -7.260  21.257  11.429  1.00 64.78  ? 30  GLY A N     1 
ATOM   147  C CA    . GLY A 1 37  ? -5.882  21.591  11.838  1.00 70.48  ? 30  GLY A CA    1 
ATOM   148  C C     . GLY A 1 37  ? -4.902  21.690  10.677  1.00 71.35  ? 30  GLY A C     1 
ATOM   149  O O     . GLY A 1 37  ? -5.257  21.289  9.543   1.00 70.29  ? 30  GLY A O     1 
ATOM   150  N N     . GLU A 1 38  ? -3.711  22.234  10.961  1.00 74.84  ? 31  GLU A N     1 
ATOM   151  C CA    . GLU A 1 38  ? -2.517  22.228  10.071  1.00 78.55  ? 31  GLU A CA    1 
ATOM   152  C C     . GLU A 1 38  ? -1.638  21.042  10.474  1.00 80.07  ? 31  GLU A C     1 
ATOM   153  O O     . GLU A 1 38  ? -1.768  20.578  11.617  1.00 84.60  ? 31  GLU A O     1 
ATOM   154  C CB    . GLU A 1 38  ? -1.736  23.539  10.170  1.00 82.07  ? 31  GLU A CB    1 
ATOM   155  C CG    . GLU A 1 38  ? -0.928  23.868  8.923   1.00 86.23  ? 31  GLU A CG    1 
ATOM   156  C CD    . GLU A 1 38  ? -1.746  24.335  7.729   1.00 91.96  ? 31  GLU A CD    1 
ATOM   157  O OE1   . GLU A 1 38  ? -2.871  24.837  7.933   1.00 91.51  ? 31  GLU A OE1   1 
ATOM   158  O OE2   . GLU A 1 38  ? -1.255  24.197  6.592   1.00 100.41 ? 31  GLU A OE2   1 
ATOM   159  N N     . GLY A 1 39  ? -0.806  20.555  9.553   1.00 88.78  ? 32  GLY A N     1 
ATOM   160  C CA    . GLY A 1 39  ? 0.047   19.365  9.747   1.00 85.37  ? 32  GLY A CA    1 
ATOM   161  C C     . GLY A 1 39  ? 1.512   19.696  9.534   1.00 85.64  ? 32  GLY A C     1 
ATOM   162  O O     . GLY A 1 39  ? 1.887   20.890  9.658   1.00 77.09  ? 32  GLY A O     1 
ATOM   163  N N     . ALA A 1 40  ? 2.314   18.674  9.220   1.00 85.89  ? 33  ALA A N     1 
ATOM   164  C CA    . ALA A 1 40  ? 3.756   18.802  8.910   1.00 83.48  ? 33  ALA A CA    1 
ATOM   165  C C     . ALA A 1 40  ? 3.910   19.593  7.605   1.00 82.80  ? 33  ALA A C     1 
ATOM   166  O O     . ALA A 1 40  ? 4.320   20.771  7.672   1.00 82.30  ? 33  ALA A O     1 
ATOM   167  C CB    . ALA A 1 40  ? 4.392   17.433  8.826   1.00 81.90  ? 33  ALA A CB    1 
ATOM   168  N N     . TYR A 1 41  ? 3.534   18.975  6.479   1.00 82.74  ? 34  TYR A N     1 
ATOM   169  C CA    . TYR A 1 41  ? 3.727   19.483  5.092   1.00 77.40  ? 34  TYR A CA    1 
ATOM   170  C C     . TYR A 1 41  ? 2.363   19.682  4.432   1.00 62.81  ? 34  TYR A C     1 
ATOM   171  O O     . TYR A 1 41  ? 2.283   19.548  3.214   1.00 55.56  ? 34  TYR A O     1 
ATOM   172  C CB    . TYR A 1 41  ? 4.588   18.511  4.276   1.00 77.84  ? 34  TYR A CB    1 
ATOM   173  C CG    . TYR A 1 41  ? 5.575   17.773  5.135   1.00 78.53  ? 34  TYR A CG    1 
ATOM   174  C CD1   . TYR A 1 41  ? 6.577   18.460  5.798   1.00 81.88  ? 34  TYR A CD1   1 
ATOM   175  C CD2   . TYR A 1 41  ? 5.442   16.418  5.376   1.00 78.44  ? 34  TYR A CD2   1 
ATOM   176  C CE1   . TYR A 1 41  ? 7.465   17.803  6.635   1.00 84.74  ? 34  TYR A CE1   1 
ATOM   177  C CE2   . TYR A 1 41  ? 6.314   15.746  6.216   1.00 81.35  ? 34  TYR A CE2   1 
ATOM   178  C CZ    . TYR A 1 41  ? 7.332   16.442  6.840   1.00 81.28  ? 34  TYR A CZ    1 
ATOM   179  O OH    . TYR A 1 41  ? 8.192   15.785  7.663   1.00 91.48  ? 34  TYR A OH    1 
ATOM   180  N N     . GLY A 1 42  ? 1.329   19.972  5.222   1.00 60.21  ? 35  GLY A N     1 
ATOM   181  C CA    . GLY A 1 42  ? 0.015   20.396  4.704   1.00 59.33  ? 35  GLY A CA    1 
ATOM   182  C C     . GLY A 1 42  ? -1.024  20.522  5.798   1.00 57.69  ? 35  GLY A C     1 
ATOM   183  O O     . GLY A 1 42  ? -0.637  20.716  6.965   1.00 66.17  ? 35  GLY A O     1 
ATOM   184  N N     . MET A 1 43  ? -2.301  20.449  5.422   1.00 58.22  ? 36  MET A N     1 
ATOM   185  C CA    . MET A 1 43  ? -3.450  20.641  6.334   1.00 59.73  ? 36  MET A CA    1 
ATOM   186  C C     . MET A 1 43  ? -4.293  19.365  6.380   1.00 59.17  ? 36  MET A C     1 
ATOM   187  O O     . MET A 1 43  ? -4.169  18.504  5.466   1.00 50.80  ? 36  MET A O     1 
ATOM   188  C CB    . MET A 1 43  ? -4.317  21.827  5.905   1.00 63.21  ? 36  MET A CB    1 
ATOM   189  C CG    . MET A 1 43  ? -5.226  21.551  4.735   1.00 64.67  ? 36  MET A CG    1 
ATOM   190  S SD    . MET A 1 43  ? -6.316  22.956  4.451   1.00 76.50  ? 36  MET A SD    1 
ATOM   191  C CE    . MET A 1 43  ? -5.179  24.057  3.609   1.00 73.59  ? 36  MET A CE    1 
ATOM   192  N N     . VAL A 1 44  ? -5.104  19.260  7.432   1.00 53.80  ? 37  VAL A N     1 
ATOM   193  C CA    . VAL A 1 44  ? -5.918  18.062  7.763   1.00 52.50  ? 37  VAL A CA    1 
ATOM   194  C C     . VAL A 1 44  ? -7.378  18.494  7.760   1.00 54.68  ? 37  VAL A C     1 
ATOM   195  O O     . VAL A 1 44  ? -7.687  19.591  8.299   1.00 51.03  ? 37  VAL A O     1 
ATOM   196  C CB    . VAL A 1 44  ? -5.506  17.456  9.111   1.00 52.23  ? 37  VAL A CB    1 
ATOM   197  C CG1   . VAL A 1 44  ? -6.254  16.163  9.389   1.00 54.87  ? 37  VAL A CG1   1 
ATOM   198  C CG2   . VAL A 1 44  ? -4.003  17.240  9.179   1.00 49.01  ? 37  VAL A CG2   1 
ATOM   199  N N     . CYS A 1 45  ? -8.224  17.682  7.135   1.00 48.02  ? 38  CYS A N     1 
ATOM   200  C CA    . CYS A 1 45  ? -9.680  17.899  7.068   1.00 47.94  ? 38  CYS A CA    1 
ATOM   201  C C     . CYS A 1 45  ? -10.390 16.600  7.410   1.00 48.19  ? 38  CYS A C     1 
ATOM   202  O O     . CYS A 1 45  ? -9.849  15.528  7.082   1.00 50.36  ? 38  CYS A O     1 
ATOM   203  C CB    . CYS A 1 45  ? -10.095 18.365  5.683   1.00 53.83  ? 38  CYS A CB    1 
ATOM   204  S SG    . CYS A 1 45  ? -9.460  20.016  5.319   1.00 53.32  ? 38  CYS A SG    1 
ATOM   205  N N     . SER A 1 46  ? -11.548 16.721  8.059   1.00 45.17  ? 39  SER A N     1 
ATOM   206  C CA    . SER A 1 46  ? -12.589 15.674  8.079   1.00 43.46  ? 39  SER A CA    1 
ATOM   207  C C     . SER A 1 46  ? -13.327 15.808  6.757   1.00 40.07  ? 39  SER A C     1 
ATOM   208  O O     . SER A 1 46  ? -13.311 16.907  6.177   1.00 39.51  ? 39  SER A O     1 
ATOM   209  C CB    . SER A 1 46  ? -13.526 15.789  9.253   1.00 44.40  ? 39  SER A CB    1 
ATOM   210  O OG    . SER A 1 46  ? -14.179 17.043  9.250   1.00 42.74  ? 39  SER A OG    1 
ATOM   211  N N     . ALA A 1 47  ? -13.918 14.720  6.301   1.00 40.43  ? 40  ALA A N     1 
ATOM   212  C CA    . ALA A 1 47  ? -14.577 14.647  4.987   1.00 40.04  ? 40  ALA A CA    1 
ATOM   213  C C     . ALA A 1 47  ? -15.520 13.471  5.043   1.00 43.03  ? 40  ALA A C     1 
ATOM   214  O O     . ALA A 1 47  ? -15.253 12.543  5.820   1.00 41.92  ? 40  ALA A O     1 
ATOM   215  C CB    . ALA A 1 47  ? -13.557 14.486  3.890   1.00 41.72  ? 40  ALA A CB    1 
ATOM   216  N N     . TYR A 1 48  ? -16.611 13.549  4.296   1.00 44.19  ? 41  TYR A N     1 
ATOM   217  C CA    . TYR A 1 48  ? -17.570 12.435  4.165   1.00 43.46  ? 41  TYR A CA    1 
ATOM   218  C C     . TYR A 1 48  ? -17.115 11.545  3.010   1.00 42.20  ? 41  TYR A C     1 
ATOM   219  O O     . TYR A 1 48  ? -16.902 12.071  1.891   1.00 41.33  ? 41  TYR A O     1 
ATOM   220  C CB    . TYR A 1 48  ? -18.985 12.974  3.955   1.00 46.13  ? 41  TYR A CB    1 
ATOM   221  C CG    . TYR A 1 48  ? -20.029 11.892  3.901   1.00 51.51  ? 41  TYR A CG    1 
ATOM   222  C CD1   . TYR A 1 48  ? -20.397 11.215  5.052   1.00 54.04  ? 41  TYR A CD1   1 
ATOM   223  C CD2   . TYR A 1 48  ? -20.639 11.539  2.705   1.00 57.06  ? 41  TYR A CD2   1 
ATOM   224  C CE1   . TYR A 1 48  ? -21.345 10.211  5.021   1.00 52.97  ? 41  TYR A CE1   1 
ATOM   225  C CE2   . TYR A 1 48  ? -21.603 10.548  2.660   1.00 56.00  ? 41  TYR A CE2   1 
ATOM   226  C CZ    . TYR A 1 48  ? -21.956 9.888   3.825   1.00 54.79  ? 41  TYR A CZ    1 
ATOM   227  O OH    . TYR A 1 48  ? -22.893 8.906   3.817   1.00 59.21  ? 41  TYR A OH    1 
ATOM   228  N N     . ASP A 1 49  ? -16.970 10.254  3.301   1.00 39.92  ? 42  ASP A N     1 
ATOM   229  C CA    . ASP A 1 49  ? -16.631 9.179   2.343   1.00 44.85  ? 42  ASP A CA    1 
ATOM   230  C C     . ASP A 1 49  ? -17.959 8.742   1.713   1.00 53.09  ? 42  ASP A C     1 
ATOM   231  O O     . ASP A 1 49  ? -18.683 7.930   2.349   1.00 53.63  ? 42  ASP A O     1 
ATOM   232  C CB    . ASP A 1 49  ? -15.851 8.067   3.057   1.00 47.07  ? 42  ASP A CB    1 
ATOM   233  C CG    . ASP A 1 49  ? -15.541 6.850   2.201   1.00 45.88  ? 42  ASP A CG    1 
ATOM   234  O OD1   . ASP A 1 49  ? -16.170 6.713   1.155   1.00 48.99  ? 42  ASP A OD1   1 
ATOM   235  O OD2   . ASP A 1 49  ? -14.689 6.035   2.606   1.00 47.52  ? 42  ASP A OD2   1 
ATOM   236  N N     . ASN A 1 50  ? -18.276 9.305   0.538   1.00 54.03  ? 43  ASN A N     1 
ATOM   237  C CA    . ASN A 1 50  ? -19.521 9.049   -0.241  1.00 53.61  ? 43  ASN A CA    1 
ATOM   238  C C     . ASN A 1 50  ? -19.632 7.573   -0.645  1.00 56.88  ? 43  ASN A C     1 
ATOM   239  O O     . ASN A 1 50  ? -20.740 7.174   -1.044  1.00 63.91  ? 43  ASN A O     1 
ATOM   240  C CB    . ASN A 1 50  ? -19.613 9.971   -1.454  1.00 52.33  ? 43  ASN A CB    1 
ATOM   241  C CG    . ASN A 1 50  ? -19.919 11.388  -1.035  1.00 52.45  ? 43  ASN A CG    1 
ATOM   242  O OD1   . ASN A 1 50  ? -21.011 11.658  -0.553  1.00 55.66  ? 43  ASN A OD1   1 
ATOM   243  N ND2   . ASN A 1 50  ? -18.981 12.297  -1.225  1.00 55.31  ? 43  ASN A ND2   1 
ATOM   244  N N     . LEU A 1 51  ? -18.548 6.798   -0.538  1.00 59.48  ? 44  LEU A N     1 
ATOM   245  C CA    . LEU A 1 51  ? -18.573 5.317   -0.650  1.00 63.96  ? 44  LEU A CA    1 
ATOM   246  C C     . LEU A 1 51  ? -19.032 4.735   0.689   1.00 72.30  ? 44  LEU A C     1 
ATOM   247  O O     . LEU A 1 51  ? -20.153 4.217   0.729   1.00 79.20  ? 44  LEU A O     1 
ATOM   248  C CB    . LEU A 1 51  ? -17.189 4.785   -1.043  1.00 69.77  ? 44  LEU A CB    1 
ATOM   249  C CG    . LEU A 1 51  ? -17.167 3.433   -1.759  1.00 68.14  ? 44  LEU A CG    1 
ATOM   250  C CD1   . LEU A 1 51  ? -15.823 3.209   -2.438  1.00 67.44  ? 44  LEU A CD1   1 
ATOM   251  C CD2   . LEU A 1 51  ? -17.471 2.285   -0.808  1.00 66.67  ? 44  LEU A CD2   1 
ATOM   252  N N     . ASN A 1 52  ? -18.220 4.833   1.750   1.00 67.15  ? 45  ASN A N     1 
ATOM   253  C CA    . ASN A 1 52  ? -18.404 4.010   2.980   1.00 63.99  ? 45  ASN A CA    1 
ATOM   254  C C     . ASN A 1 52  ? -19.374 4.682   3.953   1.00 59.80  ? 45  ASN A C     1 
ATOM   255  O O     . ASN A 1 52  ? -19.619 4.095   5.029   1.00 58.68  ? 45  ASN A O     1 
ATOM   256  C CB    . ASN A 1 52  ? -17.075 3.682   3.663   1.00 66.19  ? 45  ASN A CB    1 
ATOM   257  C CG    . ASN A 1 52  ? -16.342 2.554   2.975   1.00 65.44  ? 45  ASN A CG    1 
ATOM   258  O OD1   . ASN A 1 52  ? -15.143 2.382   3.162   1.00 68.70  ? 45  ASN A OD1   1 
ATOM   259  N ND2   . ASN A 1 52  ? -17.058 1.779   2.177   1.00 69.86  ? 45  ASN A ND2   1 
ATOM   260  N N     . LYS A 1 53  ? -19.895 5.860   3.605   1.00 59.98  ? 46  LYS A N     1 
ATOM   261  C CA    . LYS A 1 53  ? -20.951 6.547   4.391   1.00 61.18  ? 46  LYS A CA    1 
ATOM   262  C C     . LYS A 1 53  ? -20.489 6.670   5.851   1.00 62.89  ? 46  LYS A C     1 
ATOM   263  O O     . LYS A 1 53  ? -21.278 6.381   6.767   1.00 65.28  ? 46  LYS A O     1 
ATOM   264  C CB    . LYS A 1 53  ? -22.253 5.750   4.274   1.00 62.10  ? 46  LYS A CB    1 
ATOM   265  C CG    . LYS A 1 53  ? -22.641 5.337   2.863   1.00 60.76  ? 46  LYS A CG    1 
ATOM   266  C CD    . LYS A 1 53  ? -22.957 6.515   1.954   1.00 65.05  ? 46  LYS A CD    1 
ATOM   267  C CE    . LYS A 1 53  ? -23.469 6.106   0.588   1.00 65.61  ? 46  LYS A CE    1 
ATOM   268  N NZ    . LYS A 1 53  ? -24.618 5.174   0.703   1.00 69.29  ? 46  LYS A NZ    1 
ATOM   269  N N     . VAL A 1 54  ? -19.221 7.023   6.046   1.00 60.47  ? 47  VAL A N     1 
ATOM   270  C CA    . VAL A 1 54  ? -18.633 7.397   7.360   1.00 57.10  ? 47  VAL A CA    1 
ATOM   271  C C     . VAL A 1 54  ? -17.753 8.617   7.103   1.00 50.35  ? 47  VAL A C     1 
ATOM   272  O O     . VAL A 1 54  ? -17.286 8.772   5.963   1.00 44.59  ? 47  VAL A O     1 
ATOM   273  C CB    . VAL A 1 54  ? -17.850 6.228   7.984   1.00 63.78  ? 47  VAL A CB    1 
ATOM   274  C CG1   . VAL A 1 54  ? -18.789 5.134   8.465   1.00 63.97  ? 47  VAL A CG1   1 
ATOM   275  C CG2   . VAL A 1 54  ? -16.816 5.655   7.025   1.00 64.26  ? 47  VAL A CG2   1 
ATOM   276  N N     . ARG A 1 55  ? -17.595 9.479   8.102   1.00 46.20  ? 48  ARG A N     1 
ATOM   277  C CA    . ARG A 1 55  ? -16.665 10.627  8.025   1.00 49.05  ? 48  ARG A CA    1 
ATOM   278  C C     . ARG A 1 55  ? -15.261 10.050  8.232   1.00 47.26  ? 48  ARG A C     1 
ATOM   279  O O     . ARG A 1 55  ? -15.137 8.930   8.808   1.00 44.02  ? 48  ARG A O     1 
ATOM   280  C CB    . ARG A 1 55  ? -17.080 11.753  8.982   1.00 52.35  ? 48  ARG A CB    1 
ATOM   281  C CG    . ARG A 1 55  ? -18.126 12.685  8.380   1.00 52.97  ? 48  ARG A CG    1 
ATOM   282  C CD    . ARG A 1 55  ? -18.392 13.976  9.139   1.00 49.91  ? 48  ARG A CD    1 
ATOM   283  N NE    . ARG A 1 55  ? -17.419 15.046  8.937   1.00 46.62  ? 48  ARG A NE    1 
ATOM   284  C CZ    . ARG A 1 55  ? -17.246 15.744  7.808   1.00 48.32  ? 48  ARG A CZ    1 
ATOM   285  N NH1   . ARG A 1 55  ? -17.963 15.463  6.734   1.00 49.36  ? 48  ARG A NH1   1 
ATOM   286  N NH2   . ARG A 1 55  ? -16.341 16.716  7.755   1.00 45.77  ? 48  ARG A NH2   1 
ATOM   287  N N     . VAL A 1 56  ? -14.268 10.720  7.654   1.00 42.84  ? 49  VAL A N     1 
ATOM   288  C CA    . VAL A 1 56  ? -12.856 10.254  7.625   1.00 39.19  ? 49  VAL A CA    1 
ATOM   289  C C     . VAL A 1 56  ? -12.009 11.492  7.832   1.00 37.88  ? 49  VAL A C     1 
ATOM   290  O O     . VAL A 1 56  ? -12.550 12.616  7.683   1.00 36.69  ? 49  VAL A O     1 
ATOM   291  C CB    . VAL A 1 56  ? -12.465 9.508   6.334   1.00 40.44  ? 49  VAL A CB    1 
ATOM   292  C CG1   . VAL A 1 56  ? -13.239 8.224   6.165   1.00 42.91  ? 49  VAL A CG1   1 
ATOM   293  C CG2   . VAL A 1 56  ? -12.582 10.369  5.086   1.00 41.91  ? 49  VAL A CG2   1 
ATOM   294  N N     . ALA A 1 57  ? -10.750 11.269  8.197   1.00 33.29  ? 50  ALA A N     1 
ATOM   295  C CA    . ALA A 1 57  ? -9.694  12.299  8.240   1.00 35.16  ? 50  ALA A CA    1 
ATOM   296  C C     . ALA A 1 57  ? -8.924  12.207  6.921   1.00 34.26  ? 50  ALA A C     1 
ATOM   297  O O     . ALA A 1 57  ? -8.707  11.099  6.443   1.00 35.28  ? 50  ALA A O     1 
ATOM   298  C CB    . ALA A 1 57  ? -8.776  12.091  9.422   1.00 32.91  ? 50  ALA A CB    1 
ATOM   299  N N     . ILE A 1 58  ? -8.555  13.341  6.356   1.00 35.31  ? 51  ILE A N     1 
ATOM   300  C CA    . ILE A 1 58  ? -7.634  13.386  5.189   1.00 34.09  ? 51  ILE A CA    1 
ATOM   301  C C     . ILE A 1 58  ? -6.553  14.386  5.527   1.00 33.64  ? 51  ILE A C     1 
ATOM   302  O O     . ILE A 1 58  ? -6.896  15.530  5.917   1.00 36.49  ? 51  ILE A O     1 
ATOM   303  C CB    . ILE A 1 58  ? -8.343  13.727  3.860   1.00 32.93  ? 51  ILE A CB    1 
ATOM   304  C CG1   . ILE A 1 58  ? -9.633  12.928  3.704   1.00 33.83  ? 51  ILE A CG1   1 
ATOM   305  C CG2   . ILE A 1 58  ? -7.388  13.480  2.702   1.00 32.07  ? 51  ILE A CG2   1 
ATOM   306  C CD1   . ILE A 1 58  ? -10.317 13.068  2.353   1.00 38.50  ? 51  ILE A CD1   1 
ATOM   307  N N     . LYS A 1 59  ? -5.312  13.926  5.394   1.00 33.80  ? 52  LYS A N     1 
ATOM   308  C CA    . LYS A 1 59  ? -4.072  14.728  5.504   1.00 39.94  ? 52  LYS A CA    1 
ATOM   309  C C     . LYS A 1 59  ? -3.563  14.973  4.082   1.00 37.35  ? 52  LYS A C     1 
ATOM   310  O O     . LYS A 1 59  ? -3.155  14.001  3.437   1.00 37.89  ? 52  LYS A O     1 
ATOM   311  C CB    . LYS A 1 59  ? -2.993  14.000  6.318   1.00 45.36  ? 52  LYS A CB    1 
ATOM   312  C CG    . LYS A 1 59  ? -3.315  13.756  7.790   1.00 55.46  ? 52  LYS A CG    1 
ATOM   313  C CD    . LYS A 1 59  ? -2.101  13.348  8.633   1.00 57.78  ? 52  LYS A CD    1 
ATOM   314  C CE    . LYS A 1 59  ? -1.620  11.931  8.354   1.00 61.45  ? 52  LYS A CE    1 
ATOM   315  N NZ    . LYS A 1 59  ? -0.158  11.768  8.571   1.00 60.31  ? 52  LYS A NZ    1 
ATOM   316  N N     . LYS A 1 60  ? -3.630  16.218  3.621   1.00 38.44  ? 53  LYS A N     1 
ATOM   317  C CA    . LYS A 1 60  ? -2.905  16.712  2.424   1.00 40.01  ? 53  LYS A CA    1 
ATOM   318  C C     . LYS A 1 60  ? -1.439  16.905  2.784   1.00 35.83  ? 53  LYS A C     1 
ATOM   319  O O     . LYS A 1 60  ? -1.155  17.681  3.710   1.00 40.52  ? 53  LYS A O     1 
ATOM   320  C CB    . LYS A 1 60  ? -3.477  18.043  1.931   1.00 42.95  ? 53  LYS A CB    1 
ATOM   321  C CG    . LYS A 1 60  ? -2.652  18.729  0.850   1.00 43.12  ? 53  LYS A CG    1 
ATOM   322  C CD    . LYS A 1 60  ? -3.295  20.008  0.326   1.00 46.43  ? 53  LYS A CD    1 
ATOM   323  C CE    . LYS A 1 60  ? -2.709  20.463  -0.993  1.00 50.74  ? 53  LYS A CE    1 
ATOM   324  N NZ    . LYS A 1 60  ? -3.465  21.595  -1.586  1.00 53.90  ? 53  LYS A NZ    1 
ATOM   325  N N     . ILE A 1 61  ? -0.551  16.224  2.080   1.00 36.44  ? 54  ILE A N     1 
ATOM   326  C CA    . ILE A 1 61  ? 0.926   16.309  2.233   1.00 37.30  ? 54  ILE A CA    1 
ATOM   327  C C     . ILE A 1 61  ? 1.504   16.867  0.938   1.00 40.34  ? 54  ILE A C     1 
ATOM   328  O O     . ILE A 1 61  ? 1.211   16.284  -0.133  1.00 39.06  ? 54  ILE A O     1 
ATOM   329  C CB    . ILE A 1 61  ? 1.507   14.923  2.552   1.00 39.62  ? 54  ILE A CB    1 
ATOM   330  C CG1   . ILE A 1 61  ? 0.727   14.262  3.689   1.00 42.56  ? 54  ILE A CG1   1 
ATOM   331  C CG2   . ILE A 1 61  ? 2.989   15.023  2.856   1.00 41.81  ? 54  ILE A CG2   1 
ATOM   332  C CD1   . ILE A 1 61  ? 1.356   12.998  4.206   1.00 43.65  ? 54  ILE A CD1   1 
ATOM   333  N N     . SER A 1 62  ? 2.293   17.939  1.047   1.00 38.98  ? 55  SER A N     1 
ATOM   334  C CA    . SER A 1 62  ? 2.913   18.678  -0.081  1.00 41.49  ? 55  SER A CA    1 
ATOM   335  C C     . SER A 1 62  ? 4.416   18.764  0.157   1.00 42.43  ? 55  SER A C     1 
ATOM   336  O O     . SER A 1 62  ? 4.903   19.823  0.524   1.00 40.62  ? 55  SER A O     1 
ATOM   337  C CB    . SER A 1 62  ? 2.311   20.047  -0.211  1.00 40.49  ? 55  SER A CB    1 
ATOM   338  O OG    . SER A 1 62  ? 0.898   19.978  -0.290  1.00 44.55  ? 55  SER A OG    1 
ATOM   339  N N     . PRO A 1 63  ? 5.167   17.645  0.034   1.00 40.24  ? 56  PRO A N     1 
ATOM   340  C CA    . PRO A 1 63  ? 6.554   17.589  0.480   1.00 38.96  ? 56  PRO A CA    1 
ATOM   341  C C     . PRO A 1 63  ? 7.672   17.564  -0.564  1.00 37.97  ? 56  PRO A C     1 
ATOM   342  O O     . PRO A 1 63  ? 8.793   17.404  -0.165  1.00 40.12  ? 56  PRO A O     1 
ATOM   343  C CB    . PRO A 1 63  ? 6.570   16.172  1.062   1.00 39.01  ? 56  PRO A CB    1 
ATOM   344  C CG    . PRO A 1 63  ? 5.793   15.377  0.013   1.00 41.04  ? 56  PRO A CG    1 
ATOM   345  C CD    . PRO A 1 63  ? 4.686   16.321  -0.417  1.00 39.40  ? 56  PRO A CD    1 
ATOM   346  N N     . PHE A 1 64  ? 7.361   17.667  -1.859  1.00 36.32  ? 57  PHE A N     1 
ATOM   347  C CA    . PHE A 1 64  ? 8.308   17.237  -2.918  1.00 39.74  ? 57  PHE A CA    1 
ATOM   348  C C     . PHE A 1 64  ? 9.396   18.303  -3.091  1.00 42.98  ? 57  PHE A C     1 
ATOM   349  O O     . PHE A 1 64  ? 10.426  17.979  -3.716  1.00 45.54  ? 57  PHE A O     1 
ATOM   350  C CB    . PHE A 1 64  ? 7.566   16.864  -4.208  1.00 42.18  ? 57  PHE A CB    1 
ATOM   351  C CG    . PHE A 1 64  ? 6.652   15.673  -4.046  1.00 41.88  ? 57  PHE A CG    1 
ATOM   352  C CD1   . PHE A 1 64  ? 7.151   14.453  -3.620  1.00 38.36  ? 57  PHE A CD1   1 
ATOM   353  C CD2   . PHE A 1 64  ? 5.289   15.789  -4.275  1.00 40.88  ? 57  PHE A CD2   1 
ATOM   354  C CE1   . PHE A 1 64  ? 6.301   13.370  -3.441  1.00 41.59  ? 57  PHE A CE1   1 
ATOM   355  C CE2   . PHE A 1 64  ? 4.445   14.707  -4.090  1.00 41.64  ? 57  PHE A CE2   1 
ATOM   356  C CZ    . PHE A 1 64  ? 4.951   13.501  -3.689  1.00 38.42  ? 57  PHE A CZ    1 
ATOM   357  N N     . GLU A 1 65  ? 9.190   19.495  -2.525  1.00 48.57  ? 58  GLU A N     1 
ATOM   358  C CA    . GLU A 1 65  ? 10.173  20.614  -2.580  1.00 61.47  ? 58  GLU A CA    1 
ATOM   359  C C     . GLU A 1 65  ? 11.433  20.212  -1.806  1.00 65.17  ? 58  GLU A C     1 
ATOM   360  O O     . GLU A 1 65  ? 12.555  20.448  -2.325  1.00 61.34  ? 58  GLU A O     1 
ATOM   361  C CB    . GLU A 1 65  ? 9.602   21.900  -1.969  1.00 64.47  ? 58  GLU A CB    1 
ATOM   362  C CG    . GLU A 1 65  ? 8.312   22.388  -2.605  1.00 70.29  ? 58  GLU A CG    1 
ATOM   363  C CD    . GLU A 1 65  ? 8.443   22.910  -4.026  1.00 77.89  ? 58  GLU A CD    1 
ATOM   364  O OE1   . GLU A 1 65  ? 9.144   22.265  -4.833  1.00 81.13  ? 58  GLU A OE1   1 
ATOM   365  O OE2   . GLU A 1 65  ? 7.837   23.964  -4.326  1.00 83.28  ? 58  GLU A OE2   1 
ATOM   366  N N     . HIS A 1 66  ? 11.239  19.607  -0.625  1.00 64.73  ? 59  HIS A N     1 
ATOM   367  C CA    . HIS A 1 66  ? 12.269  19.418  0.432   1.00 61.79  ? 59  HIS A CA    1 
ATOM   368  C C     . HIS A 1 66  ? 12.574  17.928  0.637   1.00 56.53  ? 59  HIS A C     1 
ATOM   369  O O     . HIS A 1 66  ? 11.627  17.108  0.873   1.00 45.83  ? 59  HIS A O     1 
ATOM   370  C CB    . HIS A 1 66  ? 11.810  20.109  1.723   1.00 70.39  ? 59  HIS A CB    1 
ATOM   371  C CG    . HIS A 1 66  ? 11.474  21.555  1.548   1.00 77.99  ? 59  HIS A CG    1 
ATOM   372  N ND1   . HIS A 1 66  ? 10.221  22.072  1.865   1.00 82.21  ? 59  HIS A ND1   1 
ATOM   373  C CD2   . HIS A 1 66  ? 12.213  22.594  1.097   1.00 76.46  ? 59  HIS A CD2   1 
ATOM   374  C CE1   . HIS A 1 66  ? 10.205  23.368  1.619   1.00 79.87  ? 59  HIS A CE1   1 
ATOM   375  N NE2   . HIS A 1 66  ? 11.417  23.712  1.149   1.00 82.02  ? 59  HIS A NE2   1 
ATOM   376  N N     . GLN A 1 67  ? 13.862  17.599  0.613   1.00 49.41  ? 60  GLN A N     1 
ATOM   377  C CA    . GLN A 1 67  ? 14.382  16.211  0.693   1.00 53.54  ? 60  GLN A CA    1 
ATOM   378  C C     . GLN A 1 67  ? 13.998  15.605  2.058   1.00 54.07  ? 60  GLN A C     1 
ATOM   379  O O     . GLN A 1 67  ? 13.674  14.382  2.096   1.00 49.88  ? 60  GLN A O     1 
ATOM   380  C CB    . GLN A 1 67  ? 15.888  16.234  0.407   1.00 51.45  ? 60  GLN A CB    1 
ATOM   381  C CG    . GLN A 1 67  ? 16.435  14.903  -0.092  1.00 52.16  ? 60  GLN A CG    1 
ATOM   382  C CD    . GLN A 1 67  ? 16.882  14.007  1.040   1.00 55.45  ? 60  GLN A CD    1 
ATOM   383  O OE1   . GLN A 1 67  ? 17.222  12.839  0.857   1.00 60.12  ? 60  GLN A OE1   1 
ATOM   384  N NE2   . GLN A 1 67  ? 16.874  14.557  2.237   1.00 45.90  ? 60  GLN A NE2   1 
ATOM   385  N N     . THR A 1 68  ? 13.997  16.426  3.118   1.00 52.72  ? 61  THR A N     1 
ATOM   386  C CA    . THR A 1 68  ? 13.631  16.053  4.518   1.00 54.53  ? 61  THR A CA    1 
ATOM   387  C C     . THR A 1 68  ? 12.153  15.645  4.594   1.00 51.25  ? 61  THR A C     1 
ATOM   388  O O     . THR A 1 68  ? 11.854  14.631  5.252   1.00 40.58  ? 61  THR A O     1 
ATOM   389  C CB    . THR A 1 68  ? 13.918  17.198  5.503   1.00 54.76  ? 61  THR A CB    1 
ATOM   390  O OG1   . THR A 1 68  ? 15.326  17.195  5.720   1.00 56.73  ? 61  THR A OG1   1 
ATOM   391  C CG2   . THR A 1 68  ? 13.244  17.047  6.848   1.00 58.56  ? 61  THR A CG2   1 
ATOM   392  N N     . TYR A 1 69  ? 11.285  16.429  3.956   1.00 50.13  ? 62  TYR A N     1 
ATOM   393  C CA    . TYR A 1 69  ? 9.814   16.239  3.903   1.00 49.09  ? 62  TYR A CA    1 
ATOM   394  C C     . TYR A 1 69  ? 9.502   14.942  3.147   1.00 45.33  ? 62  TYR A C     1 
ATOM   395  O O     . TYR A 1 69  ? 8.568   14.230  3.580   1.00 42.23  ? 62  TYR A O     1 
ATOM   396  C CB    . TYR A 1 69  ? 9.146   17.468  3.280   1.00 55.69  ? 62  TYR A CB    1 
ATOM   397  C CG    . TYR A 1 69  ? 9.282   18.749  4.069   1.00 64.05  ? 62  TYR A CG    1 
ATOM   398  C CD1   . TYR A 1 69  ? 10.163  18.861  5.139   1.00 68.13  ? 62  TYR A CD1   1 
ATOM   399  C CD2   . TYR A 1 69  ? 8.538   19.869  3.729   1.00 66.03  ? 62  TYR A CD2   1 
ATOM   400  C CE1   . TYR A 1 69  ? 10.283  20.038  5.859   1.00 68.67  ? 62  TYR A CE1   1 
ATOM   401  C CE2   . TYR A 1 69  ? 8.643   21.051  4.442   1.00 67.65  ? 62  TYR A CE2   1 
ATOM   402  C CZ    . TYR A 1 69  ? 9.519   21.135  5.508   1.00 69.11  ? 62  TYR A CZ    1 
ATOM   403  O OH    . TYR A 1 69  ? 9.636   22.295  6.211   1.00 78.67  ? 62  TYR A OH    1 
ATOM   404  N N     . CYS A 1 70  ? 10.246  14.644  2.070   1.00 37.46  ? 63  CYS A N     1 
ATOM   405  C CA    . CYS A 1 70  ? 10.062  13.422  1.247   1.00 38.78  ? 63  CYS A CA    1 
ATOM   406  C C     . CYS A 1 70  ? 10.516  12.203  2.052   1.00 40.86  ? 63  CYS A C     1 
ATOM   407  O O     . CYS A 1 70  ? 9.894   11.127  1.919   1.00 32.01  ? 63  CYS A O     1 
ATOM   408  C CB    . CYS A 1 70  ? 10.809  13.485  -0.078  1.00 40.98  ? 63  CYS A CB    1 
ATOM   409  S SG    . CYS A 1 70  ? 10.146  14.746  -1.202  1.00 41.33  ? 63  CYS A SG    1 
ATOM   410  N N     . GLN A 1 71  ? 11.608  12.343  2.803   1.00 36.16  ? 64  GLN A N     1 
ATOM   411  C CA    . GLN A 1 71  ? 12.113  11.264  3.671   1.00 37.15  ? 64  GLN A CA    1 
ATOM   412  C C     . GLN A 1 71  ? 11.020  10.889  4.664   1.00 31.38  ? 64  GLN A C     1 
ATOM   413  O O     . GLN A 1 71  ? 10.693  9.732   4.713   1.00 32.52  ? 64  GLN A O     1 
ATOM   414  C CB    . GLN A 1 71  ? 13.384  11.696  4.393   1.00 41.09  ? 64  GLN A CB    1 
ATOM   415  C CG    . GLN A 1 71  ? 14.639  11.284  3.657   1.00 47.35  ? 64  GLN A CG    1 
ATOM   416  C CD    . GLN A 1 71  ? 15.824  11.489  4.560   1.00 52.10  ? 64  GLN A CD    1 
ATOM   417  O OE1   . GLN A 1 71  ? 16.225  10.579  5.281   1.00 55.95  ? 64  GLN A OE1   1 
ATOM   418  N NE2   . GLN A 1 71  ? 16.329  12.714  4.566   1.00 52.44  ? 64  GLN A NE2   1 
ATOM   419  N N     . ARG A 1 72  ? 10.484  11.852  5.410   1.00 32.98  ? 65  ARG A N     1 
ATOM   420  C CA    . ARG A 1 72  ? 9.537   11.589  6.525   1.00 35.71  ? 65  ARG A CA    1 
ATOM   421  C C     . ARG A 1 72  ? 8.228   11.016  5.967   1.00 34.51  ? 65  ARG A C     1 
ATOM   422  O O     . ARG A 1 72  ? 7.623   10.123  6.599   1.00 28.77  ? 65  ARG A O     1 
ATOM   423  C CB    . ARG A 1 72  ? 9.300   12.886  7.304   1.00 38.51  ? 65  ARG A CB    1 
ATOM   424  C CG    . ARG A 1 72  ? 10.529  13.327  8.088   1.00 39.95  ? 65  ARG A CG    1 
ATOM   425  C CD    . ARG A 1 72  ? 10.290  14.464  9.052   1.00 45.96  ? 65  ARG A CD    1 
ATOM   426  N NE    . ARG A 1 72  ? 11.575  14.922  9.587   1.00 53.39  ? 65  ARG A NE    1 
ATOM   427  C CZ    . ARG A 1 72  ? 11.753  16.050  10.271  1.00 57.82  ? 65  ARG A CZ    1 
ATOM   428  N NH1   . ARG A 1 72  ? 10.727  16.851  10.510  1.00 60.25  ? 65  ARG A NH1   1 
ATOM   429  N NH2   . ARG A 1 72  ? 12.960  16.376  10.709  1.00 62.06  ? 65  ARG A NH2   1 
ATOM   430  N N     . THR A 1 73  ? 7.776   11.569  4.837   1.00 32.20  ? 66  THR A N     1 
ATOM   431  C CA    . THR A 1 73  ? 6.572   11.111  4.101   1.00 29.16  ? 66  THR A CA    1 
ATOM   432  C C     . THR A 1 73  ? 6.763   9.663   3.653   1.00 28.70  ? 66  THR A C     1 
ATOM   433  O O     . THR A 1 73  ? 5.825   8.861   3.851   1.00 30.98  ? 66  THR A O     1 
ATOM   434  C CB    . THR A 1 73  ? 6.252   12.011  2.899   1.00 30.24  ? 66  THR A CB    1 
ATOM   435  O OG1   . THR A 1 73  ? 6.058   13.324  3.410   1.00 27.84  ? 66  THR A OG1   1 
ATOM   436  C CG2   . THR A 1 73  ? 5.031   11.530  2.144   1.00 27.42  ? 66  THR A CG2   1 
ATOM   437  N N     . LEU A 1 74  ? 7.898   9.315   3.052   1.00 28.20  ? 67  LEU A N     1 
ATOM   438  C CA    . LEU A 1 74  ? 8.092   7.942   2.561   1.00 28.29  ? 67  LEU A CA    1 
ATOM   439  C C     . LEU A 1 74  ? 8.125   6.994   3.764   1.00 29.54  ? 67  LEU A C     1 
ATOM   440  O O     . LEU A 1 74  ? 7.503   5.938   3.698   1.00 25.50  ? 67  LEU A O     1 
ATOM   441  C CB    . LEU A 1 74  ? 9.373   7.832   1.726   1.00 30.95  ? 67  LEU A CB    1 
ATOM   442  C CG    . LEU A 1 74  ? 9.725   6.413   1.277   1.00 29.79  ? 67  LEU A CG    1 
ATOM   443  C CD1   . LEU A 1 74  ? 8.589   5.795   0.487   1.00 28.56  ? 67  LEU A CD1   1 
ATOM   444  C CD2   . LEU A 1 74  ? 11.004  6.380   0.451   1.00 34.23  ? 67  LEU A CD2   1 
ATOM   445  N N     . ARG A 1 75  ? 8.869   7.361   4.815   1.00 32.04  ? 68  ARG A N     1 
ATOM   446  C CA    . ARG A 1 75  ? 9.084   6.494   6.004   1.00 33.32  ? 68  ARG A CA    1 
ATOM   447  C C     . ARG A 1 75  ? 7.714   6.176   6.620   1.00 29.88  ? 68  ARG A C     1 
ATOM   448  O O     . ARG A 1 75  ? 7.423   4.971   6.927   1.00 31.42  ? 68  ARG A O     1 
ATOM   449  C CB    . ARG A 1 75  ? 10.066  7.252   6.909   1.00 38.62  ? 68  ARG A CB    1 
ATOM   450  C CG    . ARG A 1 75  ? 10.638  6.434   8.042   1.00 46.29  ? 68  ARG A CG    1 
ATOM   451  C CD    . ARG A 1 75  ? 11.234  7.363   9.082   1.00 49.55  ? 68  ARG A CD    1 
ATOM   452  N NE    . ARG A 1 75  ? 12.207  8.301   8.559   1.00 49.09  ? 68  ARG A NE    1 
ATOM   453  C CZ    . ARG A 1 75  ? 13.397  7.980   8.071   1.00 50.88  ? 68  ARG A CZ    1 
ATOM   454  N NH1   . ARG A 1 75  ? 13.796  6.718   7.991   1.00 54.07  ? 68  ARG A NH1   1 
ATOM   455  N NH2   . ARG A 1 75  ? 14.187  8.942   7.637   1.00 55.44  ? 68  ARG A NH2   1 
ATOM   456  N N     . GLU A 1 76  ? 6.875   7.199   6.733   1.00 28.79  ? 69  GLU A N     1 
ATOM   457  C CA    . GLU A 1 76  ? 5.551   7.140   7.369   1.00 32.89  ? 69  GLU A CA    1 
ATOM   458  C C     . GLU A 1 76  ? 4.610   6.272   6.540   1.00 33.16  ? 69  GLU A C     1 
ATOM   459  O O     . GLU A 1 76  ? 3.981   5.359   7.100   1.00 30.38  ? 69  GLU A O     1 
ATOM   460  C CB    . GLU A 1 76  ? 5.030   8.551   7.507   1.00 35.63  ? 69  GLU A CB    1 
ATOM   461  C CG    . GLU A 1 76  ? 3.599   8.600   7.943   1.00 41.73  ? 69  GLU A CG    1 
ATOM   462  C CD    . GLU A 1 76  ? 3.364   9.520   9.119   1.00 46.22  ? 69  GLU A CD    1 
ATOM   463  O OE1   . GLU A 1 76  ? 3.994   10.609  9.170   1.00 55.44  ? 69  GLU A OE1   1 
ATOM   464  O OE2   . GLU A 1 76  ? 2.588   9.130   9.995   1.00 43.70  ? 69  GLU A OE2   1 
ATOM   465  N N     . ILE A 1 77  ? 4.541   6.523   5.234   1.00 28.91  ? 70  ILE A N     1 
ATOM   466  C CA    . ILE A 1 77  ? 3.715   5.695   4.320   1.00 27.43  ? 70  ILE A CA    1 
ATOM   467  C C     . ILE A 1 77  ? 4.182   4.238   4.385   1.00 24.22  ? 70  ILE A C     1 
ATOM   468  O O     . ILE A 1 77  ? 3.303   3.408   4.589   1.00 27.51  ? 70  ILE A O     1 
ATOM   469  C CB    . ILE A 1 77  ? 3.683   6.250   2.878   1.00 27.73  ? 70  ILE A CB    1 
ATOM   470  C CG1   . ILE A 1 77  ? 2.941   7.588   2.818   1.00 28.74  ? 70  ILE A CG1   1 
ATOM   471  C CG2   . ILE A 1 77  ? 3.043   5.204   1.974   1.00 27.45  ? 70  ILE A CG2   1 
ATOM   472  C CD1   . ILE A 1 77  ? 3.083   8.317   1.504   1.00 31.79  ? 70  ILE A CD1   1 
ATOM   473  N N     . LYS A 1 78  ? 5.478   3.924   4.247   1.00 27.72  ? 71  LYS A N     1 
ATOM   474  C CA    . LYS A 1 78  ? 5.993   2.526   4.234   1.00 28.16  ? 71  LYS A CA    1 
ATOM   475  C C     . LYS A 1 78  ? 5.622   1.810   5.542   1.00 26.13  ? 71  LYS A C     1 
ATOM   476  O O     . LYS A 1 78  ? 5.114   0.660   5.488   1.00 26.34  ? 71  LYS A O     1 
ATOM   477  C CB    . LYS A 1 78  ? 7.510   2.430   4.052   1.00 31.99  ? 71  LYS A CB    1 
ATOM   478  C CG    . LYS A 1 78  ? 8.017   2.792   2.668   1.00 43.81  ? 71  LYS A CG    1 
ATOM   479  C CD    . LYS A 1 78  ? 9.530   2.917   2.611   1.00 47.63  ? 71  LYS A CD    1 
ATOM   480  C CE    . LYS A 1 78  ? 10.243  1.591   2.489   1.00 50.88  ? 71  LYS A CE    1 
ATOM   481  N NZ    . LYS A 1 78  ? 10.009  0.971   1.162   1.00 57.07  ? 71  LYS A NZ    1 
ATOM   482  N N     . ILE A 1 79  ? 5.854   2.461   6.676   1.00 25.84  ? 72  ILE A N     1 
ATOM   483  C CA    . ILE A 1 79  ? 5.517   1.880   8.008   1.00 23.42  ? 72  ILE A CA    1 
ATOM   484  C C     . ILE A 1 79  ? 4.006   1.647   8.135   1.00 23.10  ? 72  ILE A C     1 
ATOM   485  O O     . ILE A 1 79  ? 3.599   0.519   8.426   1.00 24.98  ? 72  ILE A O     1 
ATOM   486  C CB    . ILE A 1 79  ? 6.107   2.745   9.138   1.00 25.35  ? 72  ILE A CB    1 
ATOM   487  C CG1   . ILE A 1 79  ? 7.642   2.742   9.123   1.00 27.93  ? 72  ILE A CG1   1 
ATOM   488  C CG2   . ILE A 1 79  ? 5.542   2.256   10.465  1.00 28.08  ? 72  ILE A CG2   1 
ATOM   489  C CD1   . ILE A 1 79  ? 8.277   3.889   9.875   1.00 29.98  ? 72  ILE A CD1   1 
ATOM   490  N N     . LEU A 1 80  ? 3.174   2.663   7.903   1.00 23.62  ? 73  LEU A N     1 
ATOM   491  C CA    . LEU A 1 80  ? 1.731   2.569   8.182   1.00 24.68  ? 73  LEU A CA    1 
ATOM   492  C C     . LEU A 1 80  ? 1.040   1.598   7.230   1.00 27.09  ? 73  LEU A C     1 
ATOM   493  O O     . LEU A 1 80  ? 0.046   1.033   7.644   1.00 28.99  ? 73  LEU A O     1 
ATOM   494  C CB    . LEU A 1 80  ? 1.125   3.958   8.127   1.00 27.40  ? 73  LEU A CB    1 
ATOM   495  C CG    . LEU A 1 80  ? 1.485   4.861   9.302   1.00 30.85  ? 73  LEU A CG    1 
ATOM   496  C CD1   . LEU A 1 80  ? 0.752   6.172   9.176   1.00 31.76  ? 73  LEU A CD1   1 
ATOM   497  C CD2   . LEU A 1 80  ? 1.194   4.199   10.650  1.00 29.03  ? 73  LEU A CD2   1 
ATOM   498  N N     . LEU A 1 81  ? 1.554   1.389   6.023   1.00 27.48  ? 74  LEU A N     1 
ATOM   499  C CA    . LEU A 1 81  ? 1.016   0.364   5.092   1.00 28.56  ? 74  LEU A CA    1 
ATOM   500  C C     . LEU A 1 81  ? 1.426   -1.040  5.542   1.00 29.87  ? 74  LEU A C     1 
ATOM   501  O O     . LEU A 1 81  ? 0.677   -1.971  5.264   1.00 31.53  ? 74  LEU A O     1 
ATOM   502  C CB    . LEU A 1 81  ? 1.530   0.638   3.677   1.00 28.65  ? 74  LEU A CB    1 
ATOM   503  C CG    . LEU A 1 81  ? 0.992   1.910   3.042   1.00 31.44  ? 74  LEU A CG    1 
ATOM   504  C CD1   . LEU A 1 81  ? 1.545   2.041   1.628   1.00 36.02  ? 74  LEU A CD1   1 
ATOM   505  C CD2   . LEU A 1 81  ? -0.543  1.941   3.018   1.00 33.26  ? 74  LEU A CD2   1 
ATOM   506  N N     . ARG A 1 82  ? 2.567   -1.189  6.202   1.00 31.19  ? 75  ARG A N     1 
ATOM   507  C CA    . ARG A 1 82  ? 3.072   -2.515  6.637   1.00 35.23  ? 75  ARG A CA    1 
ATOM   508  C C     . ARG A 1 82  ? 2.396   -2.899  7.957   1.00 33.32  ? 75  ARG A C     1 
ATOM   509  O O     . ARG A 1 82  ? 2.108   -4.067  8.140   1.00 33.82  ? 75  ARG A O     1 
ATOM   510  C CB    . ARG A 1 82  ? 4.601   -2.492  6.747   1.00 38.79  ? 75  ARG A CB    1 
ATOM   511  C CG    . ARG A 1 82  ? 5.240   -3.803  7.180   1.00 46.08  ? 75  ARG A CG    1 
ATOM   512  C CD    . ARG A 1 82  ? 5.887   -4.629  6.079   1.00 50.26  ? 75  ARG A CD    1 
ATOM   513  N NE    . ARG A 1 82  ? 7.147   -5.155  6.589   1.00 54.03  ? 75  ARG A NE    1 
ATOM   514  C CZ    . ARG A 1 82  ? 8.362   -4.913  6.090   1.00 53.01  ? 75  ARG A CZ    1 
ATOM   515  N NH1   . ARG A 1 82  ? 8.535   -4.210  4.982   1.00 51.67  ? 75  ARG A NH1   1 
ATOM   516  N NH2   . ARG A 1 82  ? 9.419   -5.429  6.689   1.00 57.01  ? 75  ARG A NH2   1 
ATOM   517  N N     . PHE A 1 83  ? 2.122   -1.942  8.832   1.00 26.48  ? 76  PHE A N     1 
ATOM   518  C CA    . PHE A 1 83  ? 1.535   -2.206  10.159  1.00 26.08  ? 76  PHE A CA    1 
ATOM   519  C C     . PHE A 1 83  ? 0.042   -2.478  10.027  1.00 29.05  ? 76  PHE A C     1 
ATOM   520  O O     . PHE A 1 83  ? -0.669  -1.795  9.244   1.00 25.98  ? 76  PHE A O     1 
ATOM   521  C CB    . PHE A 1 83  ? 1.793   -1.012  11.064  1.00 27.36  ? 76  PHE A CB    1 
ATOM   522  C CG    . PHE A 1 83  ? 3.211   -0.926  11.569  1.00 23.68  ? 76  PHE A CG    1 
ATOM   523  C CD1   . PHE A 1 83  ? 4.188   -1.802  11.151  1.00 24.86  ? 76  PHE A CD1   1 
ATOM   524  C CD2   . PHE A 1 83  ? 3.556   0.052   12.489  1.00 26.14  ? 76  PHE A CD2   1 
ATOM   525  C CE1   . PHE A 1 83  ? 5.488   -1.704  11.630  1.00 25.94  ? 76  PHE A CE1   1 
ATOM   526  C CE2   . PHE A 1 83  ? 4.842   0.122   13.005  1.00 25.13  ? 76  PHE A CE2   1 
ATOM   527  C CZ    . PHE A 1 83  ? 5.801   -0.757  12.578  1.00 25.40  ? 76  PHE A CZ    1 
ATOM   528  N N     . ARG A 1 84  ? -0.446  -3.417  10.825  1.00 27.52  ? 77  ARG A N     1 
ATOM   529  C CA    . ARG A 1 84  ? -1.901  -3.639  10.960  1.00 28.57  ? 77  ARG A CA    1 
ATOM   530  C C     . ARG A 1 84  ? -2.196  -3.921  12.431  1.00 26.01  ? 77  ARG A C     1 
ATOM   531  O O     . ARG A 1 84  ? -1.908  -5.044  12.885  1.00 26.86  ? 77  ARG A O     1 
ATOM   532  C CB    . ARG A 1 84  ? -2.319  -4.797  10.043  1.00 33.86  ? 77  ARG A CB    1 
ATOM   533  C CG    . ARG A 1 84  ? -3.824  -5.042  10.031  1.00 43.84  ? 77  ARG A CG    1 
ATOM   534  C CD    . ARG A 1 84  ? -4.256  -6.088  9.005   1.00 53.83  ? 77  ARG A CD    1 
ATOM   535  N NE    . ARG A 1 84  ? -5.681  -6.433  9.082   1.00 61.72  ? 77  ARG A NE    1 
ATOM   536  C CZ    . ARG A 1 84  ? -6.649  -5.974  8.277   1.00 68.27  ? 77  ARG A CZ    1 
ATOM   537  N NH1   . ARG A 1 84  ? -6.385  -5.122  7.295   1.00 71.38  ? 77  ARG A NH1   1 
ATOM   538  N NH2   . ARG A 1 84  ? -7.895  -6.386  8.457   1.00 71.45  ? 77  ARG A NH2   1 
ATOM   539  N N     . HIS A 1 85  ? -2.698  -2.946  13.169  1.00 23.86  ? 78  HIS A N     1 
ATOM   540  C CA    . HIS A 1 85  ? -2.884  -3.079  14.642  1.00 22.72  ? 78  HIS A CA    1 
ATOM   541  C C     . HIS A 1 85  ? -3.964  -2.111  15.140  1.00 23.26  ? 78  HIS A C     1 
ATOM   542  O O     . HIS A 1 85  ? -3.996  -0.972  14.691  1.00 24.66  ? 78  HIS A O     1 
ATOM   543  C CB    . HIS A 1 85  ? -1.505  -2.961  15.334  1.00 21.49  ? 78  HIS A CB    1 
ATOM   544  C CG    . HIS A 1 85  ? -1.577  -3.160  16.791  1.00 20.45  ? 78  HIS A CG    1 
ATOM   545  N ND1   . HIS A 1 85  ? -1.101  -4.304  17.409  1.00 21.80  ? 78  HIS A ND1   1 
ATOM   546  C CD2   . HIS A 1 85  ? -2.085  -2.379  17.751  1.00 20.13  ? 78  HIS A CD2   1 
ATOM   547  C CE1   . HIS A 1 85  ? -1.341  -4.215  18.708  1.00 19.49  ? 78  HIS A CE1   1 
ATOM   548  N NE2   . HIS A 1 85  ? -1.945  -3.045  18.938  1.00 22.63  ? 78  HIS A NE2   1 
ATOM   549  N N     . GLU A 1 86  ? -4.826  -2.547  16.044  1.00 23.06  ? 79  GLU A N     1 
ATOM   550  C CA    . GLU A 1 86  ? -5.990  -1.745  16.533  1.00 25.32  ? 79  GLU A CA    1 
ATOM   551  C C     . GLU A 1 86  ? -5.538  -0.425  17.180  1.00 20.73  ? 79  GLU A C     1 
ATOM   552  O O     . GLU A 1 86  ? -6.324  0.542   17.158  1.00 21.14  ? 79  GLU A O     1 
ATOM   553  C CB    . GLU A 1 86  ? -6.794  -2.544  17.544  1.00 30.56  ? 79  GLU A CB    1 
ATOM   554  C CG    . GLU A 1 86  ? -7.521  -3.727  16.950  1.00 38.72  ? 79  GLU A CG    1 
ATOM   555  C CD    . GLU A 1 86  ? -8.111  -4.674  17.986  1.00 45.80  ? 79  GLU A CD    1 
ATOM   556  O OE1   . GLU A 1 86  ? -7.869  -4.450  19.203  1.00 41.87  ? 79  GLU A OE1   1 
ATOM   557  O OE2   . GLU A 1 86  ? -8.811  -5.638  17.573  1.00 53.69  ? 79  GLU A OE2   1 
ATOM   558  N N     . ASN A 1 87  ? -4.294  -0.364  17.707  1.00 21.54  ? 80  ASN A N     1 
ATOM   559  C CA    . ASN A 1 87  ? -3.789  0.803   18.463  1.00 18.58  ? 80  ASN A CA    1 
ATOM   560  C C     . ASN A 1 87  ? -2.790  1.594   17.616  1.00 19.21  ? 80  ASN A C     1 
ATOM   561  O O     . ASN A 1 87  ? -2.050  2.410   18.158  1.00 18.58  ? 80  ASN A O     1 
ATOM   562  C CB    . ASN A 1 87  ? -3.220  0.382   19.821  1.00 17.28  ? 80  ASN A CB    1 
ATOM   563  C CG    . ASN A 1 87  ? -4.207  -0.333  20.707  1.00 19.06  ? 80  ASN A CG    1 
ATOM   564  O OD1   . ASN A 1 87  ? -3.962  -1.494  21.032  1.00 19.27  ? 80  ASN A OD1   1 
ATOM   565  N ND2   . ASN A 1 87  ? -5.315  0.324   21.080  1.00 18.45  ? 80  ASN A ND2   1 
ATOM   566  N N     . ILE A 1 88  ? -2.795  1.413   16.303  1.00 19.66  ? 81  ILE A N     1 
ATOM   567  C CA    . ILE A 1 88  ? -1.940  2.192   15.380  1.00 21.52  ? 81  ILE A CA    1 
ATOM   568  C C     . ILE A 1 88  ? -2.813  2.674   14.228  1.00 24.32  ? 81  ILE A C     1 
ATOM   569  O O     . ILE A 1 88  ? -3.522  1.807   13.635  1.00 23.98  ? 81  ILE A O     1 
ATOM   570  C CB    . ILE A 1 88  ? -0.768  1.327   14.882  1.00 20.80  ? 81  ILE A CB    1 
ATOM   571  C CG1   . ILE A 1 88  ? 0.084   0.830   16.059  1.00 21.07  ? 81  ILE A CG1   1 
ATOM   572  C CG2   . ILE A 1 88  ? 0.060   2.096   13.860  1.00 21.48  ? 81  ILE A CG2   1 
ATOM   573  C CD1   . ILE A 1 88  ? 1.196   -0.087  15.670  1.00 22.64  ? 81  ILE A CD1   1 
ATOM   574  N N     . ILE A 1 89  ? -2.802  3.976   13.948  1.00 24.15  ? 82  ILE A N     1 
ATOM   575  C CA    . ILE A 1 89  ? -3.606  4.543   12.831  1.00 23.94  ? 82  ILE A CA    1 
ATOM   576  C C     . ILE A 1 89  ? -3.259  3.800   11.527  1.00 26.10  ? 82  ILE A C     1 
ATOM   577  O O     . ILE A 1 89  ? -2.063  3.476   11.269  1.00 26.38  ? 82  ILE A O     1 
ATOM   578  C CB    . ILE A 1 89  ? -3.421  6.074   12.742  1.00 25.30  ? 82  ILE A CB    1 
ATOM   579  C CG1   . ILE A 1 89  ? -4.549  6.678   11.905  1.00 24.98  ? 82  ILE A CG1   1 
ATOM   580  C CG2   . ILE A 1 89  ? -2.022  6.443   12.281  1.00 24.91  ? 82  ILE A CG2   1 
ATOM   581  C CD1   . ILE A 1 89  ? -5.912  6.562   12.531  1.00 25.66  ? 82  ILE A CD1   1 
ATOM   582  N N     . GLY A 1 90  ? -4.279  3.442   10.765  1.00 26.76  ? 83  GLY A N     1 
ATOM   583  C CA    . GLY A 1 90  ? -4.103  2.798   9.455   1.00 29.16  ? 83  GLY A CA    1 
ATOM   584  C C     . GLY A 1 90  ? -4.246  3.825   8.337   1.00 29.89  ? 83  GLY A C     1 
ATOM   585  O O     . GLY A 1 90  ? -4.719  4.956   8.596   1.00 37.34  ? 83  GLY A O     1 
ATOM   586  N N     . ILE A 1 91  ? -3.802  3.475   7.147   1.00 31.81  ? 84  ILE A N     1 
ATOM   587  C CA    . ILE A 1 91  ? -4.145  4.211   5.895   1.00 29.28  ? 84  ILE A CA    1 
ATOM   588  C C     . ILE A 1 91  ? -5.286  3.454   5.231   1.00 27.45  ? 84  ILE A C     1 
ATOM   589  O O     . ILE A 1 91  ? -5.093  2.295   4.946   1.00 31.89  ? 84  ILE A O     1 
ATOM   590  C CB    . ILE A 1 91  ? -2.907  4.387   5.004   1.00 32.00  ? 84  ILE A CB    1 
ATOM   591  C CG1   . ILE A 1 91  ? -1.799  5.128   5.765   1.00 30.72  ? 84  ILE A CG1   1 
ATOM   592  C CG2   . ILE A 1 91  ? -3.273  5.126   3.721   1.00 31.89  ? 84  ILE A CG2   1 
ATOM   593  C CD1   . ILE A 1 91  ? -0.452  5.126   5.102   1.00 30.81  ? 84  ILE A CD1   1 
ATOM   594  N N     . ASN A 1 92  ? -6.445  4.088   5.046   1.00 29.81  ? 85  ASN A N     1 
ATOM   595  C CA    . ASN A 1 92  ? -7.614  3.500   4.336   1.00 31.89  ? 85  ASN A CA    1 
ATOM   596  C C     . ASN A 1 92  ? -7.489  3.754   2.839   1.00 35.90  ? 85  ASN A C     1 
ATOM   597  O O     . ASN A 1 92  ? -7.932  2.899   2.080   1.00 33.83  ? 85  ASN A O     1 
ATOM   598  C CB    . ASN A 1 92  ? -8.940  4.058   4.852   1.00 36.21  ? 85  ASN A CB    1 
ATOM   599  C CG    . ASN A 1 92  ? -9.059  3.878   6.350   1.00 38.87  ? 85  ASN A CG    1 
ATOM   600  O OD1   . ASN A 1 92  ? -9.788  4.605   7.004   1.00 43.22  ? 85  ASN A OD1   1 
ATOM   601  N ND2   . ASN A 1 92  ? -8.316  2.933   6.894   1.00 43.00  ? 85  ASN A ND2   1 
ATOM   602  N N     . ASP A 1 93  ? -6.909  4.893   2.458   1.00 34.57  ? 86  ASP A N     1 
ATOM   603  C CA    . ASP A 1 93  ? -6.800  5.314   1.038   1.00 30.89  ? 86  ASP A CA    1 
ATOM   604  C C     . ASP A 1 93  ? -5.630  6.289   0.868   1.00 29.15  ? 86  ASP A C     1 
ATOM   605  O O     . ASP A 1 93  ? -5.271  7.016   1.856   1.00 27.44  ? 86  ASP A O     1 
ATOM   606  C CB    . ASP A 1 93  ? -8.115  5.949   0.591   1.00 28.01  ? 86  ASP A CB    1 
ATOM   607  C CG    . ASP A 1 93  ? -8.308  5.977   -0.925  1.00 32.71  ? 86  ASP A CG    1 
ATOM   608  O OD1   . ASP A 1 93  ? -7.469  5.397   -1.679  1.00 31.48  ? 86  ASP A OD1   1 
ATOM   609  O OD2   . ASP A 1 93  ? -9.305  6.590   -1.336  1.00 39.09  ? 86  ASP A OD2   1 
ATOM   610  N N     . ILE A 1 94  ? -5.063  6.336   -0.341  1.00 28.37  ? 87  ILE A N     1 
ATOM   611  C CA    . ILE A 1 94  ? -4.143  7.437   -0.742  1.00 27.43  ? 87  ILE A CA    1 
ATOM   612  C C     . ILE A 1 94  ? -4.556  7.986   -2.108  1.00 29.23  ? 87  ILE A C     1 
ATOM   613  O O     . ILE A 1 94  ? -4.665  7.213   -3.037  1.00 30.22  ? 87  ILE A O     1 
ATOM   614  C CB    . ILE A 1 94  ? -2.661  7.016   -0.719  1.00 28.13  ? 87  ILE A CB    1 
ATOM   615  C CG1   . ILE A 1 94  ? -2.239  6.406   0.623   1.00 29.92  ? 87  ILE A CG1   1 
ATOM   616  C CG2   . ILE A 1 94  ? -1.796  8.225   -1.051  1.00 29.49  ? 87  ILE A CG2   1 
ATOM   617  C CD1   . ILE A 1 94  ? -0.828  5.875   0.623   1.00 30.84  ? 87  ILE A CD1   1 
ATOM   618  N N     . ILE A 1 95  ? -4.783  9.291   -2.168  1.00 32.23  ? 88  ILE A N     1 
ATOM   619  C CA    . ILE A 1 95  ? -5.169  10.032  -3.398  1.00 32.54  ? 88  ILE A CA    1 
ATOM   620  C C     . ILE A 1 95  ? -3.930  10.787  -3.898  1.00 30.39  ? 88  ILE A C     1 
ATOM   621  O O     . ILE A 1 95  ? -3.381  11.619  -3.140  1.00 29.14  ? 88  ILE A O     1 
ATOM   622  C CB    . ILE A 1 95  ? -6.340  10.982  -3.100  1.00 36.14  ? 88  ILE A CB    1 
ATOM   623  C CG1   . ILE A 1 95  ? -7.517  10.274  -2.429  1.00 40.84  ? 88  ILE A CG1   1 
ATOM   624  C CG2   . ILE A 1 95  ? -6.792  11.691  -4.364  1.00 37.35  ? 88  ILE A CG2   1 
ATOM   625  C CD1   . ILE A 1 95  ? -8.471  11.225  -1.735  1.00 41.26  ? 88  ILE A CD1   1 
ATOM   626  N N     . ARG A 1 96  ? -3.510  10.512  -5.129  1.00 26.43  ? 89  ARG A N     1 
ATOM   627  C CA    . ARG A 1 96  ? -2.453  11.284  -5.820  1.00 28.72  ? 89  ARG A CA    1 
ATOM   628  C C     . ARG A 1 96  ? -2.739  11.181  -7.314  1.00 29.02  ? 89  ARG A C     1 
ATOM   629  O O     . ARG A 1 96  ? -3.599  10.367  -7.705  1.00 26.64  ? 89  ARG A O     1 
ATOM   630  C CB    . ARG A 1 96  ? -1.067  10.769  -5.438  1.00 29.66  ? 89  ARG A CB    1 
ATOM   631  C CG    . ARG A 1 96  ? -1.000  9.256   -5.381  1.00 33.18  ? 89  ARG A CG    1 
ATOM   632  C CD    . ARG A 1 96  ? 0.233   8.540   -5.913  1.00 38.43  ? 89  ARG A CD    1 
ATOM   633  N NE    . ARG A 1 96  ? -0.089  8.241   -7.250  1.00 38.19  ? 89  ARG A NE    1 
ATOM   634  C CZ    . ARG A 1 96  ? 0.152   7.150   -7.960  1.00 32.54  ? 89  ARG A CZ    1 
ATOM   635  N NH1   . ARG A 1 96  ? 0.812   6.080   -7.547  1.00 31.04  ? 89  ARG A NH1   1 
ATOM   636  N NH2   . ARG A 1 96  ? -0.299  7.189   -9.189  1.00 31.72  ? 89  ARG A NH2   1 
ATOM   637  N N     . ALA A 1 97  ? -2.091  12.027  -8.100  1.00 29.53  ? 90  ALA A N     1 
ATOM   638  C CA    . ALA A 1 97  ? -2.237  12.051  -9.572  1.00 26.01  ? 90  ALA A CA    1 
ATOM   639  C C     . ALA A 1 97  ? -1.758  10.733  -10.167 1.00 25.44  ? 90  ALA A C     1 
ATOM   640  O O     . ALA A 1 97  ? -0.916  10.026  -9.607  1.00 25.61  ? 90  ALA A O     1 
ATOM   641  C CB    . ALA A 1 97  ? -1.457  13.205  -10.149 1.00 25.80  ? 90  ALA A CB    1 
ATOM   642  N N     . PRO A 1 98  ? -2.239  10.354  -11.369 1.00 26.84  ? 91  PRO A N     1 
ATOM   643  C CA    . PRO A 1 98  ? -1.808  9.086   -11.972 1.00 27.20  ? 91  PRO A CA    1 
ATOM   644  C C     . PRO A 1 98  ? -0.387  9.035   -12.529 1.00 24.85  ? 91  PRO A C     1 
ATOM   645  O O     . PRO A 1 98  ? 0.079   7.964   -12.849 1.00 30.17  ? 91  PRO A O     1 
ATOM   646  C CB    . PRO A 1 98  ? -2.840  8.857   -13.089 1.00 30.43  ? 91  PRO A CB    1 
ATOM   647  C CG    . PRO A 1 98  ? -3.355  10.244  -13.423 1.00 27.77  ? 91  PRO A CG    1 
ATOM   648  C CD    . PRO A 1 98  ? -3.369  10.975  -12.088 1.00 26.60  ? 91  PRO A CD    1 
ATOM   649  N N     . THR A 1 99  ? 0.281   10.168  -12.632 1.00 25.47  ? 92  THR A N     1 
ATOM   650  C CA    . THR A 1 99  ? 1.660   10.288  -13.134 1.00 27.31  ? 92  THR A CA    1 
ATOM   651  C C     . THR A 1 99  ? 2.512   11.068  -12.153 1.00 26.39  ? 92  THR A C     1 
ATOM   652  O O     . THR A 1 99  ? 1.970   11.972  -11.486 1.00 28.40  ? 92  THR A O     1 
ATOM   653  C CB    . THR A 1 99  ? 1.649   11.002  -14.486 1.00 30.22  ? 92  THR A CB    1 
ATOM   654  O OG1   . THR A 1 99  ? 1.160   12.335  -14.295 1.00 30.64  ? 92  THR A OG1   1 
ATOM   655  C CG2   . THR A 1 99  ? 0.744   10.286  -15.459 1.00 31.20  ? 92  THR A CG2   1 
ATOM   656  N N     . ILE A 1 100 ? 3.816   10.786  -12.158 1.00 31.40  ? 93  ILE A N     1 
ATOM   657  C CA    . ILE A 1 100 ? 4.810   11.473  -11.289 1.00 37.65  ? 93  ILE A CA    1 
ATOM   658  C C     . ILE A 1 100 ? 4.788   12.950  -11.656 1.00 36.43  ? 93  ILE A C     1 
ATOM   659  O O     . ILE A 1 100 ? 4.780   13.769  -10.730 1.00 35.30  ? 93  ILE A O     1 
ATOM   660  C CB    . ILE A 1 100 ? 6.221   10.851  -11.397 1.00 42.42  ? 93  ILE A CB    1 
ATOM   661  C CG1   . ILE A 1 100 ? 6.259   9.481   -10.722 1.00 46.08  ? 93  ILE A CG1   1 
ATOM   662  C CG2   . ILE A 1 100 ? 7.261   11.787  -10.795 1.00 49.85  ? 93  ILE A CG2   1 
ATOM   663  C CD1   . ILE A 1 100 ? 7.479   8.644   -11.055 1.00 46.47  ? 93  ILE A CD1   1 
ATOM   664  N N     . GLU A 1 101 ? 4.678   13.254  -12.955 1.00 33.00  ? 94  GLU A N     1 
ATOM   665  C CA    . GLU A 1 101 ? 4.768   14.641  -13.463 1.00 34.43  ? 94  GLU A CA    1 
ATOM   666  C C     . GLU A 1 101 ? 3.625   15.465  -12.879 1.00 30.51  ? 94  GLU A C     1 
ATOM   667  O O     . GLU A 1 101 ? 3.863   16.647  -12.550 1.00 38.39  ? 94  GLU A O     1 
ATOM   668  C CB    . GLU A 1 101 ? 4.759   14.640  -14.990 1.00 37.15  ? 94  GLU A CB    1 
ATOM   669  C CG    . GLU A 1 101 ? 5.981   13.962  -15.574 1.00 40.92  ? 94  GLU A CG    1 
ATOM   670  C CD    . GLU A 1 101 ? 5.917   12.453  -15.724 1.00 43.78  ? 94  GLU A CD    1 
ATOM   671  O OE1   . GLU A 1 101 ? 4.951   11.808  -15.212 1.00 43.47  ? 94  GLU A OE1   1 
ATOM   672  O OE2   . GLU A 1 101 ? 6.832   11.926  -16.362 1.00 51.49  ? 94  GLU A OE2   1 
ATOM   673  N N     . GLN A 1 102 ? 2.420   14.901  -12.787 1.00 27.59  ? 95  GLN A N     1 
ATOM   674  C CA    . GLN A 1 102 ? 1.218   15.629  -12.328 1.00 27.17  ? 95  GLN A CA    1 
ATOM   675  C C     . GLN A 1 102 ? 1.109   15.582  -10.797 1.00 29.05  ? 95  GLN A C     1 
ATOM   676  O O     . GLN A 1 102 ? 0.258   16.279  -10.263 1.00 28.81  ? 95  GLN A O     1 
ATOM   677  C CB    . GLN A 1 102 ? -0.027  15.038  -12.991 1.00 30.08  ? 95  GLN A CB    1 
ATOM   678  C CG    . GLN A 1 102 ? -0.037  15.224  -14.521 1.00 28.12  ? 95  GLN A CG    1 
ATOM   679  C CD    . GLN A 1 102 ? -1.166  14.442  -15.158 1.00 29.57  ? 95  GLN A CD    1 
ATOM   680  O OE1   . GLN A 1 102 ? -1.191  13.201  -15.138 1.00 27.08  ? 95  GLN A OE1   1 
ATOM   681  N NE2   . GLN A 1 102 ? -2.132  15.169  -15.706 1.00 29.60  ? 95  GLN A NE2   1 
ATOM   682  N N     . MET A 1 103 ? 1.906   14.748  -10.128 1.00 32.01  ? 96  MET A N     1 
ATOM   683  C CA    . MET A 1 103 ? 1.770   14.512  -8.656  1.00 29.31  ? 96  MET A CA    1 
ATOM   684  C C     . MET A 1 103 ? 2.507   15.629  -7.917  1.00 29.50  ? 96  MET A C     1 
ATOM   685  O O     . MET A 1 103 ? 3.749   15.632  -8.001  1.00 29.62  ? 96  MET A O     1 
ATOM   686  C CB    . MET A 1 103 ? 2.352   13.170  -8.208  1.00 29.19  ? 96  MET A CB    1 
ATOM   687  C CG    . MET A 1 103 ? 2.238   12.987  -6.696  1.00 30.47  ? 96  MET A CG    1 
ATOM   688  S SD    . MET A 1 103 ? 2.735   11.336  -6.142  1.00 32.04  ? 96  MET A SD    1 
ATOM   689  C CE    . MET A 1 103 ? 4.498   11.414  -6.446  1.00 29.12  ? 96  MET A CE    1 
ATOM   690  N N     . LYS A 1 104 ? 1.758   16.504  -7.244  1.00 33.09  ? 97  LYS A N     1 
ATOM   691  C CA    . LYS A 1 104 ? 2.286   17.613  -6.404  1.00 37.78  ? 97  LYS A CA    1 
ATOM   692  C C     . LYS A 1 104 ? 1.970   17.356  -4.935  1.00 36.49  ? 97  LYS A C     1 
ATOM   693  O O     . LYS A 1 104 ? 2.836   17.622  -4.113  1.00 40.05  ? 97  LYS A O     1 
ATOM   694  C CB    . LYS A 1 104 ? 1.680   18.948  -6.842  1.00 43.07  ? 97  LYS A CB    1 
ATOM   695  C CG    . LYS A 1 104 ? 2.059   19.387  -8.254  1.00 53.39  ? 97  LYS A CG    1 
ATOM   696  C CD    . LYS A 1 104 ? 3.496   19.051  -8.663  1.00 58.75  ? 97  LYS A CD    1 
ATOM   697  C CE    . LYS A 1 104 ? 3.643   18.758  -10.142 1.00 63.10  ? 97  LYS A CE    1 
ATOM   698  N NZ    . LYS A 1 104 ? 3.221   19.919  -10.959 1.00 60.42  ? 97  LYS A NZ    1 
ATOM   699  N N     . ASP A 1 105 ? 0.746   16.919  -4.658  1.00 36.57  ? 98  ASP A N     1 
ATOM   700  C CA    . ASP A 1 105 ? 0.203   16.620  -3.308  1.00 33.77  ? 98  ASP A CA    1 
ATOM   701  C C     . ASP A 1 105 ? -0.118  15.129  -3.221  1.00 34.41  ? 98  ASP A C     1 
ATOM   702  O O     . ASP A 1 105 ? -0.408  14.492  -4.293  1.00 29.25  ? 98  ASP A O     1 
ATOM   703  C CB    . ASP A 1 105 ? -1.045  17.454  -3.044  1.00 32.43  ? 98  ASP A CB    1 
ATOM   704  C CG    . ASP A 1 105 ? -0.836  18.914  -3.408  1.00 37.68  ? 98  ASP A CG    1 
ATOM   705  O OD1   . ASP A 1 105 ? 0.092   19.542  -2.845  1.00 39.34  ? 98  ASP A OD1   1 
ATOM   706  O OD2   . ASP A 1 105 ? -1.571  19.395  -4.255  1.00 42.77  ? 98  ASP A OD2   1 
ATOM   707  N N     . VAL A 1 106 ? -0.068  14.591  -2.004  1.00 28.15  ? 99  VAL A N     1 
ATOM   708  C CA    . VAL A 1 106 ? -0.592  13.238  -1.670  1.00 30.74  ? 99  VAL A CA    1 
ATOM   709  C C     . VAL A 1 106 ? -1.615  13.421  -0.559  1.00 32.22  ? 99  VAL A C     1 
ATOM   710  O O     . VAL A 1 106 ? -1.331  14.159  0.385   1.00 34.97  ? 99  VAL A O     1 
ATOM   711  C CB    . VAL A 1 106 ? 0.554   12.318  -1.231  1.00 36.31  ? 99  VAL A CB    1 
ATOM   712  C CG1   . VAL A 1 106 ? 0.118   10.892  -1.010  1.00 37.34  ? 99  VAL A CG1   1 
ATOM   713  C CG2   . VAL A 1 106 ? 1.701   12.380  -2.214  1.00 43.09  ? 99  VAL A CG2   1 
ATOM   714  N N     . TYR A 1 107 ? -2.745  12.742  -0.646  1.00 30.18  ? 100 TYR A N     1 
ATOM   715  C CA    . TYR A 1 107 ? -3.804  12.798  0.383   1.00 28.74  ? 100 TYR A CA    1 
ATOM   716  C C     . TYR A 1 107 ? -3.881  11.425  1.040   1.00 28.39  ? 100 TYR A C     1 
ATOM   717  O O     . TYR A 1 107 ? -4.062  10.394  0.366   1.00 26.11  ? 100 TYR A O     1 
ATOM   718  C CB    . TYR A 1 107 ? -5.138  13.247  -0.215  1.00 31.70  ? 100 TYR A CB    1 
ATOM   719  C CG    . TYR A 1 107 ? -5.117  14.594  -0.890  1.00 33.22  ? 100 TYR A CG    1 
ATOM   720  C CD1   . TYR A 1 107 ? -4.721  14.736  -2.217  1.00 35.41  ? 100 TYR A CD1   1 
ATOM   721  C CD2   . TYR A 1 107 ? -5.519  15.728  -0.211  1.00 33.06  ? 100 TYR A CD2   1 
ATOM   722  C CE1   . TYR A 1 107 ? -4.716  15.973  -2.844  1.00 36.52  ? 100 TYR A CE1   1 
ATOM   723  C CE2   . TYR A 1 107 ? -5.497  16.976  -0.818  1.00 37.34  ? 100 TYR A CE2   1 
ATOM   724  C CZ    . TYR A 1 107 ? -5.119  17.099  -2.143  1.00 38.32  ? 100 TYR A CZ    1 
ATOM   725  O OH    . TYR A 1 107 ? -5.125  18.337  -2.725  1.00 42.66  ? 100 TYR A OH    1 
ATOM   726  N N     . ILE A 1 108 ? -3.697  11.415  2.351   1.00 27.95  ? 101 ILE A N     1 
ATOM   727  C CA    . ILE A 1 108 ? -3.741  10.171  3.159   1.00 29.76  ? 101 ILE A CA    1 
ATOM   728  C C     . ILE A 1 108 ? -5.081  10.153  3.894   1.00 24.28  ? 101 ILE A C     1 
ATOM   729  O O     . ILE A 1 108 ? -5.379  11.068  4.696   1.00 28.00  ? 101 ILE A O     1 
ATOM   730  C CB    . ILE A 1 108 ? -2.541  10.106  4.120   1.00 34.47  ? 101 ILE A CB    1 
ATOM   731  C CG1   . ILE A 1 108 ? -1.233  10.229  3.322   1.00 37.70  ? 101 ILE A CG1   1 
ATOM   732  C CG2   . ILE A 1 108 ? -2.619  8.836   4.955   1.00 34.73  ? 101 ILE A CG2   1 
ATOM   733  C CD1   . ILE A 1 108 ? 0.017   10.075  4.125   1.00 43.03  ? 101 ILE A CD1   1 
ATOM   734  N N     . VAL A 1 109 ? -5.832  9.105   3.660   1.00 27.33  ? 102 VAL A N     1 
ATOM   735  C CA    . VAL A 1 109 ? -7.168  8.937   4.263   1.00 26.99  ? 102 VAL A CA    1 
ATOM   736  C C     . VAL A 1 109 ? -7.031  7.947   5.410   1.00 26.74  ? 102 VAL A C     1 
ATOM   737  O O     . VAL A 1 109 ? -6.490  6.848   5.172   1.00 26.87  ? 102 VAL A O     1 
ATOM   738  C CB    . VAL A 1 109 ? -8.164  8.452   3.213   1.00 27.44  ? 102 VAL A CB    1 
ATOM   739  C CG1   . VAL A 1 109 ? -9.545  8.273   3.816   1.00 31.26  ? 102 VAL A CG1   1 
ATOM   740  C CG2   . VAL A 1 109 ? -8.173  9.420   2.037   1.00 28.66  ? 102 VAL A CG2   1 
ATOM   741  N N     . GLN A 1 110 ? -7.530  8.359   6.572   1.00 29.65  ? 103 GLN A N     1 
ATOM   742  C CA    . GLN A 1 110 ? -7.503  7.577   7.831   1.00 32.76  ? 103 GLN A CA    1 
ATOM   743  C C     . GLN A 1 110 ? -8.893  7.575   8.469   1.00 35.71  ? 103 GLN A C     1 
ATOM   744  O O     . GLN A 1 110 ? -9.710  8.474   8.165   1.00 35.65  ? 103 GLN A O     1 
ATOM   745  C CB    . GLN A 1 110 ? -6.482  8.227   8.765   1.00 33.37  ? 103 GLN A CB    1 
ATOM   746  C CG    . GLN A 1 110 ? -5.098  8.294   8.147   1.00 35.33  ? 103 GLN A CG    1 
ATOM   747  C CD    . GLN A 1 110 ? -4.094  8.892   9.102   1.00 36.55  ? 103 GLN A CD    1 
ATOM   748  O OE1   . GLN A 1 110 ? -4.441  9.669   9.982   1.00 34.75  ? 103 GLN A OE1   1 
ATOM   749  N NE2   . GLN A 1 110 ? -2.848  8.472   8.963   1.00 38.27  ? 103 GLN A NE2   1 
ATOM   750  N N     . ASP A 1 111 ? -9.142  6.625   9.370   1.00 37.89  ? 104 ASP A N     1 
ATOM   751  C CA    . ASP A 1 111 ? -10.265 6.731   10.340  1.00 36.43  ? 104 ASP A CA    1 
ATOM   752  C C     . ASP A 1 111 ? -10.254 8.122   10.989  1.00 36.26  ? 104 ASP A C     1 
ATOM   753  O O     . ASP A 1 111 ? -9.157  8.626   11.447  1.00 34.00  ? 104 ASP A O     1 
ATOM   754  C CB    . ASP A 1 111 ? -10.164 5.665   11.429  1.00 40.09  ? 104 ASP A CB    1 
ATOM   755  C CG    . ASP A 1 111 ? -10.229 4.237   10.933  1.00 41.31  ? 104 ASP A CG    1 
ATOM   756  O OD1   . ASP A 1 111 ? -10.588 4.032   9.774   1.00 48.96  ? 104 ASP A OD1   1 
ATOM   757  O OD2   . ASP A 1 111 ? -9.883  3.343   11.715  1.00 49.24  ? 104 ASP A OD2   1 
ATOM   758  N N     . LEU A 1 112 ? -11.433 8.726   11.114  1.00 30.16  ? 105 LEU A N     1 
ATOM   759  C CA    . LEU A 1 112 ? -11.581 10.013  11.819  1.00 33.59  ? 105 LEU A CA    1 
ATOM   760  C C     . LEU A 1 112 ? -11.528 9.725   13.324  1.00 35.42  ? 105 LEU A C     1 
ATOM   761  O O     . LEU A 1 112 ? -12.268 8.847   13.831  1.00 35.76  ? 105 LEU A O     1 
ATOM   762  C CB    . LEU A 1 112 ? -12.890 10.705  11.419  1.00 34.89  ? 105 LEU A CB    1 
ATOM   763  C CG    . LEU A 1 112 ? -13.152 12.058  12.080  1.00 34.71  ? 105 LEU A CG    1 
ATOM   764  C CD1   . LEU A 1 112 ? -12.158 13.114  11.648  1.00 35.29  ? 105 LEU A CD1   1 
ATOM   765  C CD2   . LEU A 1 112 ? -14.577 12.516  11.787  1.00 42.50  ? 105 LEU A CD2   1 
ATOM   766  N N     . MET A 1 113 ? -10.674 10.446  14.026  1.00 33.14  ? 106 MET A N     1 
ATOM   767  C CA    . MET A 1 113 ? -10.585 10.326  15.497  1.00 34.57  ? 106 MET A CA    1 
ATOM   768  C C     . MET A 1 113 ? -11.021 11.662  16.088  1.00 35.05  ? 106 MET A C     1 
ATOM   769  O O     . MET A 1 113 ? -10.486 12.695  15.663  1.00 46.12  ? 106 MET A O     1 
ATOM   770  C CB    . MET A 1 113 ? -9.144  9.954   15.874  1.00 30.45  ? 106 MET A CB    1 
ATOM   771  C CG    . MET A 1 113 ? -8.701  8.634   15.251  1.00 29.84  ? 106 MET A CG    1 
ATOM   772  S SD    . MET A 1 113 ? -9.519  7.150   15.900  1.00 32.48  ? 106 MET A SD    1 
ATOM   773  C CE    . MET A 1 113 ? -8.625  7.003   17.457  1.00 29.78  ? 106 MET A CE    1 
ATOM   774  N N     . GLU A 1 114 ? -11.909 11.658  17.073  1.00 36.54  ? 107 GLU A N     1 
ATOM   775  C CA    . GLU A 1 114 ? -12.503 12.927  17.572  1.00 39.54  ? 107 GLU A CA    1 
ATOM   776  C C     . GLU A 1 114 ? -11.465 13.816  18.261  1.00 36.39  ? 107 GLU A C     1 
ATOM   777  O O     . GLU A 1 114 ? -11.670 14.997  18.262  1.00 33.22  ? 107 GLU A O     1 
ATOM   778  C CB    . GLU A 1 114 ? -13.708 12.646  18.474  1.00 48.19  ? 107 GLU A CB    1 
ATOM   779  C CG    . GLU A 1 114 ? -14.985 12.449  17.666  1.00 54.69  ? 107 GLU A CG    1 
ATOM   780  C CD    . GLU A 1 114 ? -14.941 11.281  16.686  1.00 64.22  ? 107 GLU A CD    1 
ATOM   781  O OE1   . GLU A 1 114 ? -15.576 11.403  15.617  1.00 66.27  ? 107 GLU A OE1   1 
ATOM   782  O OE2   . GLU A 1 114 ? -14.258 10.245  16.986  1.00 61.31  ? 107 GLU A OE2   1 
ATOM   783  N N     . THR A 1 115 ? -10.378 13.304  18.850  1.00 29.61  ? 108 THR A N     1 
ATOM   784  C CA    . THR A 1 115 ? -9.474  14.176  19.620  1.00 25.42  ? 108 THR A CA    1 
ATOM   785  C C     . THR A 1 115 ? -8.098  13.512  19.764  1.00 23.18  ? 108 THR A C     1 
ATOM   786  O O     . THR A 1 115 ? -7.814  12.538  19.060  1.00 21.32  ? 108 THR A O     1 
ATOM   787  C CB    . THR A 1 115 ? -10.069 14.570  20.983  1.00 26.89  ? 108 THR A CB    1 
ATOM   788  O OG1   . THR A 1 115 ? -9.244  15.544  21.621  1.00 33.12  ? 108 THR A OG1   1 
ATOM   789  C CG2   . THR A 1 115 ? -10.212 13.446  21.986  1.00 27.59  ? 108 THR A CG2   1 
ATOM   790  N N     . ASP A 1 116 ? -7.249  14.126  20.556  1.00 25.15  ? 109 ASP A N     1 
ATOM   791  C CA    . ASP A 1 116 ? -5.895  13.563  20.815  1.00 26.44  ? 109 ASP A CA    1 
ATOM   792  C C     . ASP A 1 116 ? -5.633  13.800  22.286  1.00 26.51  ? 109 ASP A C     1 
ATOM   793  O O     . ASP A 1 116 ? -6.436  14.524  22.962  1.00 24.50  ? 109 ASP A O     1 
ATOM   794  C CB    . ASP A 1 116 ? -4.869  14.058  19.785  1.00 28.92  ? 109 ASP A CB    1 
ATOM   795  C CG    . ASP A 1 116 ? -4.530  15.530  19.911  1.00 32.01  ? 109 ASP A CG    1 
ATOM   796  O OD1   . ASP A 1 116 ? -4.263  15.952  21.038  1.00 28.52  ? 109 ASP A OD1   1 
ATOM   797  O OD2   . ASP A 1 116 ? -4.561  16.230  18.873  1.00 33.58  ? 109 ASP A OD2   1 
ATOM   798  N N     . LEU A 1 117 ? -4.617  13.135  22.820  1.00 24.83  ? 110 LEU A N     1 
ATOM   799  C CA    . LEU A 1 117 ? -4.423  13.152  24.278  1.00 22.90  ? 110 LEU A CA    1 
ATOM   800  C C     . LEU A 1 117 ? -3.971  14.553  24.707  1.00 20.07  ? 110 LEU A C     1 
ATOM   801  O O     . LEU A 1 117 ? -4.140  14.915  25.875  1.00 20.79  ? 110 LEU A O     1 
ATOM   802  C CB    . LEU A 1 117 ? -3.424  12.060  24.666  1.00 22.01  ? 110 LEU A CB    1 
ATOM   803  C CG    . LEU A 1 117 ? -3.208  11.891  26.168  1.00 23.58  ? 110 LEU A CG    1 
ATOM   804  C CD1   . LEU A 1 117 ? -4.488  11.519  26.878  1.00 24.58  ? 110 LEU A CD1   1 
ATOM   805  C CD2   . LEU A 1 117 ? -2.154  10.818  26.426  1.00 25.45  ? 110 LEU A CD2   1 
ATOM   806  N N     . TYR A 1 118 ? -3.304  15.283  23.836  1.00 21.54  ? 111 TYR A N     1 
ATOM   807  C CA    . TYR A 1 118 ? -2.829  16.651  24.182  1.00 23.93  ? 111 TYR A CA    1 
ATOM   808  C C     . TYR A 1 118 ? -4.067  17.547  24.411  1.00 22.87  ? 111 TYR A C     1 
ATOM   809  O O     . TYR A 1 118 ? -4.129  18.198  25.428  1.00 23.26  ? 111 TYR A O     1 
ATOM   810  C CB    . TYR A 1 118 ? -1.925  17.176  23.070  1.00 27.24  ? 111 TYR A CB    1 
ATOM   811  C CG    . TYR A 1 118 ? -1.602  18.645  23.170  1.00 30.86  ? 111 TYR A CG    1 
ATOM   812  C CD1   . TYR A 1 118 ? -0.549  19.084  23.951  1.00 36.36  ? 111 TYR A CD1   1 
ATOM   813  C CD2   . TYR A 1 118 ? -2.368  19.591  22.495  1.00 35.71  ? 111 TYR A CD2   1 
ATOM   814  C CE1   . TYR A 1 118 ? -0.253  20.430  24.073  1.00 38.24  ? 111 TYR A CE1   1 
ATOM   815  C CE2   . TYR A 1 118 ? -2.080  20.945  22.596  1.00 41.10  ? 111 TYR A CE2   1 
ATOM   816  C CZ    . TYR A 1 118 ? -1.016  21.361  23.387  1.00 43.14  ? 111 TYR A CZ    1 
ATOM   817  O OH    . TYR A 1 118 ? -0.712  22.683  23.523  1.00 44.81  ? 111 TYR A OH    1 
ATOM   818  N N     . LYS A 1 119 ? -4.981  17.598  23.446  1.00 28.89  ? 112 LYS A N     1 
ATOM   819  C CA    . LYS A 1 119 ? -6.285  18.337  23.549  1.00 30.08  ? 112 LYS A CA    1 
ATOM   820  C C     . LYS A 1 119 ? -7.064  17.867  24.768  1.00 31.50  ? 112 LYS A C     1 
ATOM   821  O O     . LYS A 1 119 ? -7.534  18.705  25.546  1.00 35.45  ? 112 LYS A O     1 
ATOM   822  C CB    . LYS A 1 119 ? -7.127  18.129  22.292  1.00 33.55  ? 112 LYS A CB    1 
ATOM   823  C CG    . LYS A 1 119 ? -6.538  18.772  21.056  1.00 39.53  ? 112 LYS A CG    1 
ATOM   824  C CD    . LYS A 1 119 ? -7.486  18.685  19.877  1.00 46.24  ? 112 LYS A CD    1 
ATOM   825  C CE    . LYS A 1 119 ? -6.824  19.043  18.560  1.00 53.59  ? 112 LYS A CE    1 
ATOM   826  N NZ    . LYS A 1 119 ? -7.118  18.010  17.535  1.00 62.61  ? 112 LYS A NZ    1 
ATOM   827  N N     . LEU A 1 120 ? -7.113  16.558  25.013  1.00 30.31  ? 113 LEU A N     1 
ATOM   828  C CA    . LEU A 1 120 ? -7.806  15.992  26.195  1.00 28.81  ? 113 LEU A CA    1 
ATOM   829  C C     . LEU A 1 120 ? -7.146  16.477  27.485  1.00 27.52  ? 113 LEU A C     1 
ATOM   830  O O     . LEU A 1 120 ? -7.861  16.846  28.415  1.00 28.20  ? 113 LEU A O     1 
ATOM   831  C CB    . LEU A 1 120 ? -7.758  14.464  26.048  1.00 32.48  ? 113 LEU A CB    1 
ATOM   832  C CG    . LEU A 1 120 ? -8.936  13.644  26.521  1.00 36.84  ? 113 LEU A CG    1 
ATOM   833  C CD1   . LEU A 1 120 ? -10.258 14.222  26.068  1.00 34.50  ? 113 LEU A CD1   1 
ATOM   834  C CD2   . LEU A 1 120 ? -8.766  12.213  26.027  1.00 37.25  ? 113 LEU A CD2   1 
ATOM   835  N N     . LEU A 1 121 ? -5.814  16.444  27.598  1.00 25.55  ? 114 LEU A N     1 
ATOM   836  C CA    . LEU A 1 121 ? -5.131  16.805  28.876  1.00 27.75  ? 114 LEU A CA    1 
ATOM   837  C C     . LEU A 1 121 ? -5.274  18.304  29.180  1.00 27.26  ? 114 LEU A C     1 
ATOM   838  O O     . LEU A 1 121 ? -5.179  18.675  30.372  1.00 30.15  ? 114 LEU A O     1 
ATOM   839  C CB    . LEU A 1 121 ? -3.660  16.416  28.793  1.00 28.80  ? 114 LEU A CB    1 
ATOM   840  C CG    . LEU A 1 121 ? -3.453  14.908  28.861  1.00 33.64  ? 114 LEU A CG    1 
ATOM   841  C CD1   . LEU A 1 121 ? -2.029  14.555  28.525  1.00 30.07  ? 114 LEU A CD1   1 
ATOM   842  C CD2   . LEU A 1 121 ? -3.857  14.380  30.243  1.00 36.91  ? 114 LEU A CD2   1 
ATOM   843  N N     . LYS A 1 122 ? -5.427  19.114  28.146  1.00 30.63  ? 115 LYS A N     1 
ATOM   844  C CA    . LYS A 1 122 ? -5.635  20.580  28.305  1.00 37.19  ? 115 LYS A CA    1 
ATOM   845  C C     . LYS A 1 122 ? -6.986  20.860  28.981  1.00 35.29  ? 115 LYS A C     1 
ATOM   846  O O     . LYS A 1 122 ? -7.071  21.891  29.642  1.00 34.79  ? 115 LYS A O     1 
ATOM   847  C CB    . LYS A 1 122 ? -5.614  21.281  26.943  1.00 40.23  ? 115 LYS A CB    1 
ATOM   848  C CG    . LYS A 1 122 ? -4.242  21.439  26.313  1.00 45.17  ? 115 LYS A CG    1 
ATOM   849  C CD    . LYS A 1 122 ? -4.290  21.765  24.834  1.00 55.69  ? 115 LYS A CD    1 
ATOM   850  C CE    . LYS A 1 122 ? -5.198  22.917  24.436  1.00 57.95  ? 115 LYS A CE    1 
ATOM   851  N NZ    . LYS A 1 122 ? -5.813  22.681  23.105  1.00 61.29  ? 115 LYS A NZ    1 
ATOM   852  N N     . THR A 1 123 ? -7.995  19.979  28.834  1.00 35.40  ? 116 THR A N     1 
ATOM   853  C CA    . THR A 1 123 ? -9.421  20.282  29.163  1.00 37.49  ? 116 THR A CA    1 
ATOM   854  C C     . THR A 1 123 ? -10.029 19.288  30.168  1.00 35.26  ? 116 THR A C     1 
ATOM   855  O O     . THR A 1 123 ? -11.048 19.636  30.759  1.00 36.80  ? 116 THR A O     1 
ATOM   856  C CB    . THR A 1 123 ? -10.292 20.302  27.895  1.00 38.30  ? 116 THR A CB    1 
ATOM   857  O OG1   . THR A 1 123 ? -10.176 19.058  27.214  1.00 40.88  ? 116 THR A OG1   1 
ATOM   858  C CG2   . THR A 1 123 ? -9.898  21.383  26.912  1.00 43.00  ? 116 THR A CG2   1 
ATOM   859  N N     . GLN A 1 124 ? -9.494  18.071  30.358  1.00 27.17  ? 117 GLN A N     1 
ATOM   860  C CA    . GLN A 1 124 ? -10.251 17.027  31.092  1.00 26.45  ? 117 GLN A CA    1 
ATOM   861  C C     . GLN A 1 124 ? -9.393  16.437  32.212  1.00 26.22  ? 117 GLN A C     1 
ATOM   862  O O     . GLN A 1 124 ? -8.244  16.064  31.976  1.00 30.93  ? 117 GLN A O     1 
ATOM   863  C CB    . GLN A 1 124 ? -10.731 15.946  30.115  1.00 26.88  ? 117 GLN A CB    1 
ATOM   864  C CG    . GLN A 1 124 ? -11.560 16.438  28.939  1.00 28.94  ? 117 GLN A CG    1 
ATOM   865  C CD    . GLN A 1 124 ? -12.876 17.074  29.314  1.00 28.84  ? 117 GLN A CD    1 
ATOM   866  O OE1   . GLN A 1 124 ? -13.481 16.724  30.311  1.00 30.46  ? 117 GLN A OE1   1 
ATOM   867  N NE2   . GLN A 1 124 ? -13.253 18.107  28.590  1.00 30.15  ? 117 GLN A NE2   1 
ATOM   868  N N     . HIS A 1 125 ? -9.964  16.281  33.388  1.00 25.94  ? 118 HIS A N     1 
ATOM   869  C CA    . HIS A 1 125 ? -9.463  15.356  34.433  1.00 29.32  ? 118 HIS A CA    1 
ATOM   870  C C     . HIS A 1 125 ? -9.654  13.906  33.959  1.00 28.94  ? 118 HIS A C     1 
ATOM   871  O O     . HIS A 1 125 ? -10.790 13.520  33.553  1.00 24.26  ? 118 HIS A O     1 
ATOM   872  C CB    . HIS A 1 125 ? -10.200 15.606  35.742  1.00 37.11  ? 118 HIS A CB    1 
ATOM   873  C CG    . HIS A 1 125 ? -9.787  14.683  36.839  1.00 43.82  ? 118 HIS A CG    1 
ATOM   874  N ND1   . HIS A 1 125 ? -10.561 13.593  37.217  1.00 44.97  ? 118 HIS A ND1   1 
ATOM   875  C CD2   . HIS A 1 125 ? -8.704  14.695  37.653  1.00 47.17  ? 118 HIS A CD2   1 
ATOM   876  C CE1   . HIS A 1 125 ? -9.962  12.955  38.203  1.00 45.66  ? 118 HIS A CE1   1 
ATOM   877  N NE2   . HIS A 1 125 ? -8.820  13.616  38.495  1.00 52.26  ? 118 HIS A NE2   1 
ATOM   878  N N     . LEU A 1 126 ? -8.599  13.095  33.990  1.00 26.05  ? 119 LEU A N     1 
ATOM   879  C CA    . LEU A 1 126 ? -8.728  11.652  33.638  1.00 26.16  ? 119 LEU A CA    1 
ATOM   880  C C     . LEU A 1 126 ? -8.987  10.873  34.919  1.00 24.57  ? 119 LEU A C     1 
ATOM   881  O O     . LEU A 1 126 ? -8.234  11.087  35.850  1.00 28.14  ? 119 LEU A O     1 
ATOM   882  C CB    . LEU A 1 126 ? -7.435  11.181  32.962  1.00 28.54  ? 119 LEU A CB    1 
ATOM   883  C CG    . LEU A 1 126 ? -7.352  11.244  31.432  1.00 33.95  ? 119 LEU A CG    1 
ATOM   884  C CD1   . LEU A 1 126 ? -7.822  12.554  30.854  1.00 32.73  ? 119 LEU A CD1   1 
ATOM   885  C CD2   . LEU A 1 126 ? -5.912  10.968  30.967  1.00 38.16  ? 119 LEU A CD2   1 
ATOM   886  N N     . SER A 1 127 ? -9.957  9.956   34.956  1.00 25.01  ? 120 SER A N     1 
ATOM   887  C CA    . SER A 1 127 ? -10.114 8.998   36.081  1.00 24.89  ? 120 SER A CA    1 
ATOM   888  C C     . SER A 1 127 ? -8.891  8.067   36.065  1.00 26.40  ? 120 SER A C     1 
ATOM   889  O O     . SER A 1 127 ? -8.314  7.878   34.962  1.00 25.34  ? 120 SER A O     1 
ATOM   890  C CB    . SER A 1 127 ? -11.402 8.177   35.988  1.00 27.44  ? 120 SER A CB    1 
ATOM   891  O OG    . SER A 1 127 ? -11.351 7.191   34.942  1.00 26.67  ? 120 SER A OG    1 
ATOM   892  N N     . ASN A 1 128 ? -8.589  7.430   37.196  1.00 27.77  ? 121 ASN A N     1 
ATOM   893  C CA    . ASN A 1 128 ? -7.623  6.296   37.271  1.00 28.48  ? 121 ASN A CA    1 
ATOM   894  C C     . ASN A 1 128 ? -7.976  5.218   36.221  1.00 25.36  ? 121 ASN A C     1 
ATOM   895  O O     . ASN A 1 128 ? -7.052  4.658   35.618  1.00 22.14  ? 121 ASN A O     1 
ATOM   896  C CB    . ASN A 1 128 ? -7.497  5.693   38.672  1.00 28.61  ? 121 ASN A CB    1 
ATOM   897  C CG    . ASN A 1 128 ? -6.298  4.765   38.816  1.00 33.16  ? 121 ASN A CG    1 
ATOM   898  O OD1   . ASN A 1 128 ? -6.386  3.738   39.510  1.00 38.88  ? 121 ASN A OD1   1 
ATOM   899  N ND2   . ASN A 1 128 ? -5.182  5.074   38.160  1.00 25.71  ? 121 ASN A ND2   1 
ATOM   900  N N     . ASP A 1 129 ? -9.253  4.933   35.957  1.00 22.97  ? 122 ASP A N     1 
ATOM   901  C CA    . ASP A 1 129 ? -9.612  3.898   34.960  1.00 25.30  ? 122 ASP A CA    1 
ATOM   902  C C     . ASP A 1 129 ? -9.218  4.354   33.549  1.00 21.77  ? 122 ASP A C     1 
ATOM   903  O O     . ASP A 1 129 ? -8.789  3.505   32.783  1.00 21.27  ? 122 ASP A O     1 
ATOM   904  C CB    . ASP A 1 129 ? -11.098 3.504   35.022  1.00 26.94  ? 122 ASP A CB    1 
ATOM   905  C CG    . ASP A 1 129 ? -11.470 2.796   36.320  1.00 34.11  ? 122 ASP A CG    1 
ATOM   906  O OD1   . ASP A 1 129 ? -10.709 1.929   36.761  1.00 35.61  ? 122 ASP A OD1   1 
ATOM   907  O OD2   . ASP A 1 129 ? -12.491 3.128   36.878  1.00 37.20  ? 122 ASP A OD2   1 
ATOM   908  N N     . HIS A 1 130 ? -9.397  5.620   33.195  1.00 21.57  ? 123 HIS A N     1 
ATOM   909  C CA    . HIS A 1 130 ? -9.005  6.141   31.868  1.00 21.05  ? 123 HIS A CA    1 
ATOM   910  C C     . HIS A 1 130 ? -7.479  6.096   31.710  1.00 18.13  ? 123 HIS A C     1 
ATOM   911  O O     . HIS A 1 130 ? -7.082  5.744   30.645  1.00 20.22  ? 123 HIS A O     1 
ATOM   912  C CB    . HIS A 1 130 ? -9.494  7.569   31.609  1.00 23.39  ? 123 HIS A CB    1 
ATOM   913  C CG    . HIS A 1 130 ? -10.961 7.647   31.375  1.00 24.69  ? 123 HIS A CG    1 
ATOM   914  N ND1   . HIS A 1 130 ? -11.860 7.681   32.417  1.00 29.24  ? 123 HIS A ND1   1 
ATOM   915  C CD2   . HIS A 1 130 ? -11.686 7.642   30.235  1.00 28.58  ? 123 HIS A CD2   1 
ATOM   916  C CE1   . HIS A 1 130 ? -13.076 7.724   31.927  1.00 27.32  ? 123 HIS A CE1   1 
ATOM   917  N NE2   . HIS A 1 130 ? -12.998 7.695   30.593  1.00 27.70  ? 123 HIS A NE2   1 
ATOM   918  N N     . ILE A 1 131 ? -6.732  6.488   32.724  1.00 20.77  ? 124 ILE A N     1 
ATOM   919  C CA    . ILE A 1 131 ? -5.232  6.522   32.725  1.00 20.46  ? 124 ILE A CA    1 
ATOM   920  C C     . ILE A 1 131 ? -4.749  5.097   32.470  1.00 21.00  ? 124 ILE A C     1 
ATOM   921  O O     . ILE A 1 131 ? -3.936  4.868   31.558  1.00 22.23  ? 124 ILE A O     1 
ATOM   922  C CB    . ILE A 1 131 ? -4.662  7.111   34.029  1.00 22.47  ? 124 ILE A CB    1 
ATOM   923  C CG1   . ILE A 1 131 ? -5.078  8.570   34.202  1.00 22.59  ? 124 ILE A CG1   1 
ATOM   924  C CG2   . ILE A 1 131 ? -3.136  6.926   34.081  1.00 22.51  ? 124 ILE A CG2   1 
ATOM   925  C CD1   . ILE A 1 131 ? -4.676  9.193   35.523  1.00 24.65  ? 124 ILE A CD1   1 
ATOM   926  N N     . CYS A 1 132 ? -5.325  4.157   33.194  1.00 19.94  ? 125 CYS A N     1 
ATOM   927  C CA    . CYS A 1 132 ? -4.992  2.728   33.102  1.00 20.05  ? 125 CYS A CA    1 
ATOM   928  C C     . CYS A 1 132 ? -5.233  2.245   31.661  1.00 20.05  ? 125 CYS A C     1 
ATOM   929  O O     . CYS A 1 132 ? -4.351  1.622   31.077  1.00 21.46  ? 125 CYS A O     1 
ATOM   930  C CB    . CYS A 1 132 ? -5.795  1.970   34.148  1.00 21.82  ? 125 CYS A CB    1 
ATOM   931  S SG    . CYS A 1 132 ? -5.078  0.340   34.409  1.00 26.11  ? 125 CYS A SG    1 
ATOM   932  N N     . TYR A 1 133 ? -6.425  2.475   31.129  1.00 21.40  ? 126 TYR A N     1 
ATOM   933  C CA    . TYR A 1 133 ? -6.868  2.031   29.789  1.00 21.15  ? 126 TYR A CA    1 
ATOM   934  C C     . TYR A 1 133 ? -6.042  2.706   28.686  1.00 18.18  ? 126 TYR A C     1 
ATOM   935  O O     . TYR A 1 133 ? -5.629  2.015   27.733  1.00 17.52  ? 126 TYR A O     1 
ATOM   936  C CB    . TYR A 1 133 ? -8.363  2.298   29.646  1.00 23.85  ? 126 TYR A CB    1 
ATOM   937  C CG    . TYR A 1 133 ? -8.963  1.793   28.367  1.00 23.59  ? 126 TYR A CG    1 
ATOM   938  C CD1   . TYR A 1 133 ? -8.651  0.539   27.872  1.00 25.95  ? 126 TYR A CD1   1 
ATOM   939  C CD2   . TYR A 1 133 ? -9.867  2.567   27.660  1.00 25.23  ? 126 TYR A CD2   1 
ATOM   940  C CE1   . TYR A 1 133 ? -9.218  0.064   26.709  1.00 29.44  ? 126 TYR A CE1   1 
ATOM   941  C CE2   . TYR A 1 133 ? -10.457 2.109   26.501  1.00 27.56  ? 126 TYR A CE2   1 
ATOM   942  C CZ    . TYR A 1 133 ? -10.130 0.856   26.032  1.00 29.04  ? 126 TYR A CZ    1 
ATOM   943  O OH    . TYR A 1 133 ? -10.675 0.414   24.878  1.00 32.44  ? 126 TYR A OH    1 
ATOM   944  N N     . PHE A 1 134 ? -5.780  4.007   28.800  1.00 17.55  ? 127 PHE A N     1 
ATOM   945  C CA    . PHE A 1 134 ? -4.948  4.722   27.793  1.00 18.88  ? 127 PHE A CA    1 
ATOM   946  C C     . PHE A 1 134 ? -3.532  4.127   27.777  1.00 18.50  ? 127 PHE A C     1 
ATOM   947  O O     . PHE A 1 134 ? -3.006  3.781   26.703  1.00 17.78  ? 127 PHE A O     1 
ATOM   948  C CB    . PHE A 1 134 ? -4.871  6.226   28.086  1.00 20.66  ? 127 PHE A CB    1 
ATOM   949  C CG    . PHE A 1 134 ? -6.172  6.957   27.885  1.00 23.65  ? 127 PHE A CG    1 
ATOM   950  C CD1   . PHE A 1 134 ? -7.240  6.349   27.254  1.00 27.41  ? 127 PHE A CD1   1 
ATOM   951  C CD2   . PHE A 1 134 ? -6.318  8.272   28.307  1.00 26.64  ? 127 PHE A CD2   1 
ATOM   952  C CE1   . PHE A 1 134 ? -8.443  7.024   27.088  1.00 29.17  ? 127 PHE A CE1   1 
ATOM   953  C CE2   . PHE A 1 134 ? -7.518  8.950   28.119  1.00 27.52  ? 127 PHE A CE2   1 
ATOM   954  C CZ    . PHE A 1 134 ? -8.570  8.323   27.508  1.00 25.91  ? 127 PHE A CZ    1 
ATOM   955  N N     . LEU A 1 135 ? -2.917  4.024   28.947  1.00 17.34  ? 128 LEU A N     1 
ATOM   956  C CA    . LEU A 1 135 ? -1.542  3.476   29.077  1.00 16.49  ? 128 LEU A CA    1 
ATOM   957  C C     . LEU A 1 135 ? -1.506  2.049   28.506  1.00 18.16  ? 128 LEU A C     1 
ATOM   958  O O     . LEU A 1 135 ? -0.587  1.716   27.732  1.00 16.58  ? 128 LEU A O     1 
ATOM   959  C CB    . LEU A 1 135 ? -1.110  3.493   30.545  1.00 19.33  ? 128 LEU A CB    1 
ATOM   960  C CG    . LEU A 1 135 ? 0.302   2.946   30.760  1.00 18.31  ? 128 LEU A CG    1 
ATOM   961  C CD1   . LEU A 1 135 ? 1.330   3.867   30.116  1.00 20.88  ? 128 LEU A CD1   1 
ATOM   962  C CD2   . LEU A 1 135 ? 0.592   2.725   32.210  1.00 20.44  ? 128 LEU A CD2   1 
ATOM   963  N N     . TYR A 1 136 ? -2.503  1.212   28.850  1.00 18.95  ? 129 TYR A N     1 
ATOM   964  C CA    . TYR A 1 136 ? -2.581  -0.152  28.299  1.00 18.91  ? 129 TYR A CA    1 
ATOM   965  C C     . TYR A 1 136 ? -2.486  -0.070  26.768  1.00 19.56  ? 129 TYR A C     1 
ATOM   966  O O     . TYR A 1 136 ? -1.718  -0.810  26.158  1.00 18.83  ? 129 TYR A O     1 
ATOM   967  C CB    . TYR A 1 136 ? -3.867  -0.862  28.727  1.00 21.09  ? 129 TYR A CB    1 
ATOM   968  C CG    . TYR A 1 136 ? -3.953  -2.218  28.096  1.00 21.51  ? 129 TYR A CG    1 
ATOM   969  C CD1   . TYR A 1 136 ? -3.040  -3.193  28.445  1.00 20.83  ? 129 TYR A CD1   1 
ATOM   970  C CD2   . TYR A 1 136 ? -4.861  -2.499  27.095  1.00 21.89  ? 129 TYR A CD2   1 
ATOM   971  C CE1   . TYR A 1 136 ? -3.081  -4.451  27.864  1.00 20.84  ? 129 TYR A CE1   1 
ATOM   972  C CE2   . TYR A 1 136 ? -4.914  -3.756  26.502  1.00 23.40  ? 129 TYR A CE2   1 
ATOM   973  C CZ    . TYR A 1 136 ? -3.979  -4.708  26.849  1.00 22.02  ? 129 TYR A CZ    1 
ATOM   974  O OH    . TYR A 1 136 ? -3.977  -5.937  26.264  1.00 21.37  ? 129 TYR A OH    1 
ATOM   975  N N     . GLN A 1 137 ? -3.306  0.764   26.150  1.00 17.87  ? 130 GLN A N     1 
ATOM   976  C CA    . GLN A 1 137 ? -3.433  0.791   24.666  1.00 18.63  ? 130 GLN A CA    1 
ATOM   977  C C     . GLN A 1 137 ? -2.153  1.364   24.034  1.00 17.19  ? 130 GLN A C     1 
ATOM   978  O O     . GLN A 1 137 ? -1.739  0.874   22.988  1.00 17.96  ? 130 GLN A O     1 
ATOM   979  C CB    . GLN A 1 137 ? -4.616  1.633   24.222  1.00 18.02  ? 130 GLN A CB    1 
ATOM   980  C CG    . GLN A 1 137 ? -5.948  1.032   24.626  1.00 20.19  ? 130 GLN A CG    1 
ATOM   981  C CD    . GLN A 1 137 ? -7.084  1.887   24.140  1.00 20.31  ? 130 GLN A CD    1 
ATOM   982  O OE1   . GLN A 1 137 ? -7.438  1.818   22.950  1.00 21.34  ? 130 GLN A OE1   1 
ATOM   983  N NE2   . GLN A 1 137 ? -7.598  2.747   25.027  1.00 20.38  ? 130 GLN A NE2   1 
ATOM   984  N N     . ILE A 1 138 ? -1.535  2.350   24.677  1.00 17.34  ? 131 ILE A N     1 
ATOM   985  C CA    . ILE A 1 138 ? -0.214  2.885   24.232  1.00 15.66  ? 131 ILE A CA    1 
ATOM   986  C C     . ILE A 1 138 ? 0.816   1.734   24.227  1.00 16.21  ? 131 ILE A C     1 
ATOM   987  O O     . ILE A 1 138 ? 1.452   1.531   23.221  1.00 16.25  ? 131 ILE A O     1 
ATOM   988  C CB    . ILE A 1 138 ? 0.281   4.052   25.101  1.00 16.25  ? 131 ILE A CB    1 
ATOM   989  C CG1   . ILE A 1 138 ? -0.631  5.279   25.049  1.00 17.57  ? 131 ILE A CG1   1 
ATOM   990  C CG2   . ILE A 1 138 ? 1.712   4.381   24.718  1.00 17.41  ? 131 ILE A CG2   1 
ATOM   991  C CD1   . ILE A 1 138 ? -0.419  6.275   26.179  1.00 18.30  ? 131 ILE A CD1   1 
ATOM   992  N N     . LEU A 1 139 ? 0.943   0.985   25.305  1.00 15.92  ? 132 LEU A N     1 
ATOM   993  C CA    . LEU A 1 139 ? 1.957   -0.099  25.412  1.00 15.53  ? 132 LEU A CA    1 
ATOM   994  C C     . LEU A 1 139 ? 1.612   -1.241  24.472  1.00 16.31  ? 132 LEU A C     1 
ATOM   995  O O     . LEU A 1 139 ? 2.508   -1.871  23.907  1.00 17.00  ? 132 LEU A O     1 
ATOM   996  C CB    . LEU A 1 139 ? 2.015   -0.515  26.857  1.00 15.65  ? 132 LEU A CB    1 
ATOM   997  C CG    . LEU A 1 139 ? 2.634   0.527   27.772  1.00 17.61  ? 132 LEU A CG    1 
ATOM   998  C CD1   . LEU A 1 139 ? 2.374   0.073   29.188  1.00 19.71  ? 132 LEU A CD1   1 
ATOM   999  C CD2   . LEU A 1 139 ? 4.110   0.684   27.539  1.00 19.09  ? 132 LEU A CD2   1 
ATOM   1000 N N     . ARG A 1 140 ? 0.318   -1.511  24.280  1.00 17.33  ? 133 ARG A N     1 
ATOM   1001 C CA    . ARG A 1 140 ? -0.072  -2.616  23.378  1.00 16.68  ? 133 ARG A CA    1 
ATOM   1002 C C     . ARG A 1 140 ? 0.331   -2.271  21.939  1.00 17.42  ? 133 ARG A C     1 
ATOM   1003 O O     . ARG A 1 140 ? 0.923   -3.095  21.237  1.00 16.53  ? 133 ARG A O     1 
ATOM   1004 C CB    . ARG A 1 140 ? -1.571  -2.852  23.498  1.00 16.85  ? 133 ARG A CB    1 
ATOM   1005 C CG    . ARG A 1 140 ? -2.089  -4.007  22.677  1.00 16.70  ? 133 ARG A CG    1 
ATOM   1006 C CD    . ARG A 1 140 ? -3.552  -4.177  22.974  1.00 19.71  ? 133 ARG A CD    1 
ATOM   1007 N NE    . ARG A 1 140 ? -4.145  -5.275  22.213  1.00 20.04  ? 133 ARG A NE    1 
ATOM   1008 C CZ    . ARG A 1 140 ? -4.950  -5.178  21.164  1.00 26.08  ? 133 ARG A CZ    1 
ATOM   1009 N NH1   . ARG A 1 140 ? -5.294  -4.001  20.667  1.00 27.47  ? 133 ARG A NH1   1 
ATOM   1010 N NH2   . ARG A 1 140 ? -5.443  -6.286  20.617  1.00 26.80  ? 133 ARG A NH2   1 
ATOM   1011 N N     . GLY A 1 141 ? 0.109   -1.032  21.527  1.00 17.80  ? 134 GLY A N     1 
ATOM   1012 C CA    . GLY A 1 141 ? 0.554   -0.597  20.214  1.00 16.79  ? 134 GLY A CA    1 
ATOM   1013 C C     . GLY A 1 141 ? 2.068   -0.593  20.184  1.00 16.37  ? 134 GLY A C     1 
ATOM   1014 O O     . GLY A 1 141 ? 2.626   -0.994  19.159  1.00 15.19  ? 134 GLY A O     1 
ATOM   1015 N N     . LEU A 1 142 ? 2.710   -0.091  21.252  1.00 15.84  ? 135 LEU A N     1 
ATOM   1016 C CA    . LEU A 1 142 ? 4.189   0.017   21.227  1.00 16.10  ? 135 LEU A CA    1 
ATOM   1017 C C     . LEU A 1 142 ? 4.818   -1.383  21.171  1.00 16.26  ? 135 LEU A C     1 
ATOM   1018 O O     . LEU A 1 142 ? 5.879   -1.526  20.566  1.00 17.38  ? 135 LEU A O     1 
ATOM   1019 C CB    . LEU A 1 142 ? 4.688   0.793   22.436  1.00 17.21  ? 135 LEU A CB    1 
ATOM   1020 C CG    . LEU A 1 142 ? 6.170   1.158   22.377  1.00 18.07  ? 135 LEU A CG    1 
ATOM   1021 C CD1   . LEU A 1 142 ? 6.456   2.047   21.205  1.00 18.70  ? 135 LEU A CD1   1 
ATOM   1022 C CD2   . LEU A 1 142 ? 6.593   1.822   23.684  1.00 20.15  ? 135 LEU A CD2   1 
ATOM   1023 N N     . LYS A 1 143 ? 4.194   -2.388  21.791  1.00 16.57  ? 136 LYS A N     1 
ATOM   1024 C CA    . LYS A 1 143 ? 4.714   -3.776  21.742  1.00 16.04  ? 136 LYS A CA    1 
ATOM   1025 C C     . LYS A 1 143 ? 4.824   -4.189  20.264  1.00 18.20  ? 136 LYS A C     1 
ATOM   1026 O O     . LYS A 1 143 ? 5.847   -4.758  19.871  1.00 16.39  ? 136 LYS A O     1 
ATOM   1027 C CB    . LYS A 1 143 ? 3.858   -4.719  22.582  1.00 15.13  ? 136 LYS A CB    1 
ATOM   1028 C CG    . LYS A 1 143 ? 4.248   -6.167  22.414  1.00 16.55  ? 136 LYS A CG    1 
ATOM   1029 C CD    . LYS A 1 143 ? 3.330   -7.169  23.067  1.00 16.98  ? 136 LYS A CD    1 
ATOM   1030 C CE    . LYS A 1 143 ? 3.831   -8.603  22.908  1.00 18.78  ? 136 LYS A CE    1 
ATOM   1031 N NZ    . LYS A 1 143 ? 2.855   -9.578  23.470  1.00 19.04  ? 136 LYS A NZ    1 
ATOM   1032 N N     . TYR A 1 144 ? 3.794   -3.905  19.483  1.00 17.96  ? 137 TYR A N     1 
ATOM   1033 C CA    . TYR A 1 144 ? 3.750   -4.256  18.045  1.00 17.09  ? 137 TYR A CA    1 
ATOM   1034 C C     . TYR A 1 144 ? 4.836   -3.508  17.272  1.00 16.14  ? 137 TYR A C     1 
ATOM   1035 O O     . TYR A 1 144 ? 5.668   -4.134  16.585  1.00 17.51  ? 137 TYR A O     1 
ATOM   1036 C CB    . TYR A 1 144 ? 2.320   -4.069  17.560  1.00 17.39  ? 137 TYR A CB    1 
ATOM   1037 C CG    . TYR A 1 144 ? 2.145   -4.422  16.117  1.00 19.84  ? 137 TYR A CG    1 
ATOM   1038 C CD1   . TYR A 1 144 ? 2.423   -3.494  15.126  1.00 21.81  ? 137 TYR A CD1   1 
ATOM   1039 C CD2   . TYR A 1 144 ? 1.714   -5.667  15.716  1.00 22.86  ? 137 TYR A CD2   1 
ATOM   1040 C CE1   . TYR A 1 144 ? 2.235   -3.798  13.779  1.00 22.69  ? 137 TYR A CE1   1 
ATOM   1041 C CE2   . TYR A 1 144 ? 1.509   -5.978  14.381  1.00 23.67  ? 137 TYR A CE2   1 
ATOM   1042 C CZ    . TYR A 1 144 ? 1.777   -5.038  13.403  1.00 24.91  ? 137 TYR A CZ    1 
ATOM   1043 O OH    . TYR A 1 144 ? 1.548   -5.303  12.074  1.00 25.08  ? 137 TYR A OH    1 
ATOM   1044 N N     . ILE A 1 145 ? 4.941   -2.208  17.495  1.00 16.22  ? 138 ILE A N     1 
ATOM   1045 C CA    . ILE A 1 145 ? 5.970   -1.359  16.847  1.00 17.28  ? 138 ILE A CA    1 
ATOM   1046 C C     . ILE A 1 145 ? 7.367   -1.932  17.139  1.00 17.30  ? 138 ILE A C     1 
ATOM   1047 O O     . ILE A 1 145 ? 8.105   -2.177  16.203  1.00 18.95  ? 138 ILE A O     1 
ATOM   1048 C CB    . ILE A 1 145 ? 5.832   0.092   17.303  1.00 17.70  ? 138 ILE A CB    1 
ATOM   1049 C CG1   . ILE A 1 145 ? 4.483   0.704   16.914  1.00 19.20  ? 138 ILE A CG1   1 
ATOM   1050 C CG2   . ILE A 1 145 ? 6.963   0.897   16.737  1.00 17.93  ? 138 ILE A CG2   1 
ATOM   1051 C CD1   . ILE A 1 145 ? 4.181   1.990   17.679  1.00 19.51  ? 138 ILE A CD1   1 
ATOM   1052 N N     . HIS A 1 146 ? 7.695   -2.194  18.416  1.00 17.47  ? 139 HIS A N     1 
ATOM   1053 C CA    . HIS A 1 146 ? 9.039   -2.650  18.840  1.00 19.04  ? 139 HIS A CA    1 
ATOM   1054 C C     . HIS A 1 146 ? 9.272   -4.050  18.275  1.00 18.55  ? 139 HIS A C     1 
ATOM   1055 O O     . HIS A 1 146 ? 10.405  -4.339  17.920  1.00 17.76  ? 139 HIS A O     1 
ATOM   1056 C CB    . HIS A 1 146 ? 9.184   -2.577  20.372  1.00 17.25  ? 139 HIS A CB    1 
ATOM   1057 C CG    . HIS A 1 146 ? 9.416   -1.176  20.826  1.00 18.82  ? 139 HIS A CG    1 
ATOM   1058 N ND1   . HIS A 1 146 ? 9.614   -0.855  22.180  1.00 16.47  ? 139 HIS A ND1   1 
ATOM   1059 C CD2   . HIS A 1 146 ? 9.503   -0.020  20.108  1.00 18.36  ? 139 HIS A CD2   1 
ATOM   1060 C CE1   . HIS A 1 146 ? 9.801   0.443   22.238  1.00 18.03  ? 139 HIS A CE1   1 
ATOM   1061 N NE2   . HIS A 1 146 ? 9.752   0.972   20.997  1.00 19.17  ? 139 HIS A NE2   1 
ATOM   1062 N N     . SER A 1 147 ? 8.221   -4.863  18.207  1.00 18.71  ? 140 SER A N     1 
ATOM   1063 C CA    . SER A 1 147 ? 8.256   -6.245  17.672  1.00 21.06  ? 140 SER A CA    1 
ATOM   1064 C C     . SER A 1 147 ? 8.660   -6.206  16.188  1.00 22.17  ? 140 SER A C     1 
ATOM   1065 O O     . SER A 1 147 ? 9.239   -7.192  15.702  1.00 22.01  ? 140 SER A O     1 
ATOM   1066 C CB    . SER A 1 147 ? 6.953   -6.994  17.883  1.00 19.63  ? 140 SER A CB    1 
ATOM   1067 O OG    . SER A 1 147 ? 5.966   -6.678  16.903  1.00 21.15  ? 140 SER A OG    1 
ATOM   1068 N N     . ALA A 1 148 ? 8.424   -5.096  15.508  1.00 22.56  ? 141 ALA A N     1 
ATOM   1069 C CA    . ALA A 1 148 ? 8.726   -4.925  14.070  1.00 22.64  ? 141 ALA A CA    1 
ATOM   1070 C C     . ALA A 1 148 ? 10.138  -4.323  13.905  1.00 23.30  ? 141 ALA A C     1 
ATOM   1071 O O     . ALA A 1 148 ? 10.510  -3.989  12.774  1.00 25.01  ? 141 ALA A O     1 
ATOM   1072 C CB    . ALA A 1 148 ? 7.664   -4.078  13.445  1.00 21.95  ? 141 ALA A CB    1 
ATOM   1073 N N     . ASN A 1 149 ? 10.868  -4.221  15.003  1.00 21.60  ? 142 ASN A N     1 
ATOM   1074 C CA    . ASN A 1 149 ? 12.244  -3.660  15.079  1.00 24.19  ? 142 ASN A CA    1 
ATOM   1075 C C     . ASN A 1 149 ? 12.204  -2.169  14.745  1.00 24.39  ? 142 ASN A C     1 
ATOM   1076 O O     . ASN A 1 149 ? 13.216  -1.651  14.221  1.00 24.23  ? 142 ASN A O     1 
ATOM   1077 C CB    . ASN A 1 149 ? 13.223  -4.424  14.176  1.00 28.54  ? 142 ASN A CB    1 
ATOM   1078 C CG    . ASN A 1 149 ? 14.657  -4.199  14.602  1.00 33.03  ? 142 ASN A CG    1 
ATOM   1079 O OD1   . ASN A 1 149 ? 14.939  -4.162  15.797  1.00 35.66  ? 142 ASN A OD1   1 
ATOM   1080 N ND2   . ASN A 1 149 ? 15.552  -4.018  13.649  1.00 38.01  ? 142 ASN A ND2   1 
ATOM   1081 N N     . VAL A 1 150 ? 11.048  -1.521  14.980  1.00 22.80  ? 143 VAL A N     1 
ATOM   1082 C CA    . VAL A 1 150 ? 10.843  -0.078  14.697  1.00 22.77  ? 143 VAL A CA    1 
ATOM   1083 C C     . VAL A 1 150 ? 10.788  0.697   16.020  1.00 21.80  ? 143 VAL A C     1 
ATOM   1084 O O     . VAL A 1 150 ? 10.216  0.176   17.000  1.00 23.55  ? 143 VAL A O     1 
ATOM   1085 C CB    . VAL A 1 150 ? 9.594   0.163   13.848  1.00 21.65  ? 143 VAL A CB    1 
ATOM   1086 C CG1   . VAL A 1 150 ? 9.266   1.647   13.712  1.00 22.82  ? 143 VAL A CG1   1 
ATOM   1087 C CG2   . VAL A 1 150 ? 9.780   -0.477  12.484  1.00 24.15  ? 143 VAL A CG2   1 
ATOM   1088 N N     . LEU A 1 151 ? 11.405  1.875   16.018  1.00 19.18  ? 144 LEU A N     1 
ATOM   1089 C CA    . LEU A 1 151 ? 11.342  2.899   17.104  1.00 21.84  ? 144 LEU A CA    1 
ATOM   1090 C C     . LEU A 1 151 ? 10.469  4.045   16.604  1.00 21.44  ? 144 LEU A C     1 
ATOM   1091 O O     . LEU A 1 151 ? 10.722  4.540   15.475  1.00 24.56  ? 144 LEU A O     1 
ATOM   1092 C CB    . LEU A 1 151 ? 12.746  3.431   17.373  1.00 22.31  ? 144 LEU A CB    1 
ATOM   1093 C CG    . LEU A 1 151 ? 13.802  2.369   17.645  1.00 22.89  ? 144 LEU A CG    1 
ATOM   1094 C CD1   . LEU A 1 151 ? 15.152  2.996   17.837  1.00 25.52  ? 144 LEU A CD1   1 
ATOM   1095 C CD2   . LEU A 1 151 ? 13.446  1.558   18.870  1.00 26.89  ? 144 LEU A CD2   1 
ATOM   1096 N N     . HIS A 1 152 ? 9.491   4.462   17.383  1.00 19.15  ? 145 HIS A N     1 
ATOM   1097 C CA    . HIS A 1 152 ? 8.626   5.603   17.017  1.00 19.59  ? 145 HIS A CA    1 
ATOM   1098 C C     . HIS A 1 152 ? 9.429   6.917   17.076  1.00 20.90  ? 145 HIS A C     1 
ATOM   1099 O O     . HIS A 1 152 ? 9.421   7.677   16.080  1.00 20.12  ? 145 HIS A O     1 
ATOM   1100 C CB    . HIS A 1 152 ? 7.382   5.632   17.899  1.00 20.27  ? 145 HIS A CB    1 
ATOM   1101 C CG    . HIS A 1 152 ? 6.400   6.664   17.473  1.00 20.81  ? 145 HIS A CG    1 
ATOM   1102 N ND1   . HIS A 1 152 ? 6.624   8.010   17.694  1.00 18.39  ? 145 HIS A ND1   1 
ATOM   1103 C CD2   . HIS A 1 152 ? 5.205   6.556   16.872  1.00 21.27  ? 145 HIS A CD2   1 
ATOM   1104 C CE1   . HIS A 1 152 ? 5.567   8.664   17.269  1.00 19.70  ? 145 HIS A CE1   1 
ATOM   1105 N NE2   . HIS A 1 152 ? 4.695   7.796   16.753  1.00 19.50  ? 145 HIS A NE2   1 
ATOM   1106 N N     . ARG A 1 153 ? 10.086  7.155   18.225  1.00 19.83  ? 146 ARG A N     1 
ATOM   1107 C CA    . ARG A 1 153 ? 11.009  8.266   18.512  1.00 22.20  ? 146 ARG A CA    1 
ATOM   1108 C C     . ARG A 1 153 ? 10.287  9.609   18.615  1.00 23.03  ? 146 ARG A C     1 
ATOM   1109 O O     . ARG A 1 153 ? 11.007  10.613  18.816  1.00 23.44  ? 146 ARG A O     1 
ATOM   1110 C CB    . ARG A 1 153 ? 12.118  8.336   17.462  1.00 21.80  ? 146 ARG A CB    1 
ATOM   1111 C CG    . ARG A 1 153 ? 12.859  7.018   17.337  1.00 24.10  ? 146 ARG A CG    1 
ATOM   1112 C CD    . ARG A 1 153 ? 13.903  7.012   16.287  1.00 24.55  ? 146 ARG A CD    1 
ATOM   1113 N NE    . ARG A 1 153 ? 15.060  7.811   16.518  1.00 31.84  ? 146 ARG A NE    1 
ATOM   1114 C CZ    . ARG A 1 153 ? 15.445  8.861   15.803  1.00 34.63  ? 146 ARG A CZ    1 
ATOM   1115 N NH1   . ARG A 1 153 ? 14.681  9.348   14.849  1.00 36.91  ? 146 ARG A NH1   1 
ATOM   1116 N NH2   . ARG A 1 153 ? 16.611  9.427   16.062  1.00 35.61  ? 146 ARG A NH2   1 
ATOM   1117 N N     . ASP A 1 154 ? 8.959   9.667   18.574  1.00 21.36  ? 147 ASP A N     1 
ATOM   1118 C CA    . ASP A 1 154 ? 8.262   10.963  18.787  1.00 24.56  ? 147 ASP A CA    1 
ATOM   1119 C C     . ASP A 1 154 ? 6.953   10.760  19.542  1.00 21.30  ? 147 ASP A C     1 
ATOM   1120 O O     . ASP A 1 154 ? 5.983   11.456  19.259  1.00 22.34  ? 147 ASP A O     1 
ATOM   1121 C CB    . ASP A 1 154 ? 8.055   11.708  17.471  1.00 26.99  ? 147 ASP A CB    1 
ATOM   1122 C CG    . ASP A 1 154 ? 7.816   13.197  17.693  1.00 28.77  ? 147 ASP A CG    1 
ATOM   1123 O OD1   . ASP A 1 154 ? 8.217   13.746  18.765  1.00 31.75  ? 147 ASP A OD1   1 
ATOM   1124 O OD2   . ASP A 1 154 ? 7.168   13.760  16.836  1.00 32.07  ? 147 ASP A OD2   1 
ATOM   1125 N N     . LEU A 1 155 ? 6.951   9.891   20.551  1.00 22.09  ? 148 LEU A N     1 
ATOM   1126 C CA    . LEU A 1 155 ? 5.725   9.651   21.337  1.00 19.88  ? 148 LEU A CA    1 
ATOM   1127 C C     . LEU A 1 155 ? 5.519   10.865  22.246  1.00 19.82  ? 148 LEU A C     1 
ATOM   1128 O O     . LEU A 1 155 ? 6.441   11.280  22.950  1.00 19.67  ? 148 LEU A O     1 
ATOM   1129 C CB    . LEU A 1 155 ? 5.831   8.346   22.106  1.00 21.47  ? 148 LEU A CB    1 
ATOM   1130 C CG    . LEU A 1 155 ? 5.894   7.078   21.246  1.00 21.33  ? 148 LEU A CG    1 
ATOM   1131 C CD1   . LEU A 1 155 ? 6.259   5.890   22.112  1.00 21.68  ? 148 LEU A CD1   1 
ATOM   1132 C CD2   . LEU A 1 155 ? 4.575   6.798   20.541  1.00 23.50  ? 148 LEU A CD2   1 
ATOM   1133 N N     . LYS A 1 156 ? 4.339   11.453  22.145  1.00 19.75  ? 149 LYS A N     1 
ATOM   1134 C CA    . LYS A 1 156 ? 3.917   12.615  22.945  1.00 18.94  ? 149 LYS A CA    1 
ATOM   1135 C C     . LYS A 1 156 ? 2.402   12.664  22.817  1.00 18.25  ? 149 LYS A C     1 
ATOM   1136 O O     . LYS A 1 156 ? 1.822   12.009  21.928  1.00 20.58  ? 149 LYS A O     1 
ATOM   1137 C CB    . LYS A 1 156 ? 4.609   13.873  22.423  1.00 20.24  ? 149 LYS A CB    1 
ATOM   1138 C CG    . LYS A 1 156 ? 4.171   14.301  21.049  1.00 23.80  ? 149 LYS A CG    1 
ATOM   1139 C CD    . LYS A 1 156 ? 5.121   15.293  20.384  1.00 28.98  ? 149 LYS A CD    1 
ATOM   1140 C CE    . LYS A 1 156 ? 4.641   15.622  18.992  1.00 34.35  ? 149 LYS A CE    1 
ATOM   1141 N NZ    . LYS A 1 156 ? 5.760   16.026  18.111  1.00 43.50  ? 149 LYS A NZ    1 
ATOM   1142 N N     . PRO A 1 157 ? 1.710   13.397  23.712  1.00 19.71  ? 150 PRO A N     1 
ATOM   1143 C CA    . PRO A 1 157 ? 0.247   13.381  23.740  1.00 19.71  ? 150 PRO A CA    1 
ATOM   1144 C C     . PRO A 1 157 ? -0.403  13.682  22.390  1.00 20.41  ? 150 PRO A C     1 
ATOM   1145 O O     . PRO A 1 157 ? -1.415  13.010  22.019  1.00 19.95  ? 150 PRO A O     1 
ATOM   1146 C CB    . PRO A 1 157 ? -0.081  14.393  24.859  1.00 20.84  ? 150 PRO A CB    1 
ATOM   1147 C CG    . PRO A 1 157 ? 1.094   14.289  25.784  1.00 20.46  ? 150 PRO A CG    1 
ATOM   1148 C CD    . PRO A 1 157 ? 2.270   14.156  24.837  1.00 21.27  ? 150 PRO A CD    1 
ATOM   1149 N N     . SER A 1 158 ? 0.165   14.619  21.608  1.00 22.65  ? 151 SER A N     1 
ATOM   1150 C CA    . SER A 1 158 ? -0.431  15.033  20.305  1.00 24.32  ? 151 SER A CA    1 
ATOM   1151 C C     . SER A 1 158 ? -0.349  13.904  19.262  1.00 25.80  ? 151 SER A C     1 
ATOM   1152 O O     . SER A 1 158 ? -1.150  13.940  18.290  1.00 22.71  ? 151 SER A O     1 
ATOM   1153 C CB    . SER A 1 158 ? 0.159   16.339  19.798  1.00 27.70  ? 151 SER A CB    1 
ATOM   1154 O OG    . SER A 1 158 ? 1.503   16.162  19.432  1.00 33.67  ? 151 SER A OG    1 
ATOM   1155 N N     . ASN A 1 159 ? 0.484   12.874  19.461  1.00 19.66  ? 152 ASN A N     1 
ATOM   1156 C CA    . ASN A 1 159 ? 0.590   11.770  18.487  1.00 20.28  ? 152 ASN A CA    1 
ATOM   1157 C C     . ASN A 1 159 ? -0.231  10.563  18.977  1.00 21.07  ? 152 ASN A C     1 
ATOM   1158 O O     . ASN A 1 159 ? 0.046   9.475   18.511  1.00 21.98  ? 152 ASN A O     1 
ATOM   1159 C CB    . ASN A 1 159 ? 2.067   11.437  18.230  1.00 22.69  ? 152 ASN A CB    1 
ATOM   1160 C CG    . ASN A 1 159 ? 2.767   12.501  17.392  1.00 24.65  ? 152 ASN A CG    1 
ATOM   1161 O OD1   . ASN A 1 159 ? 4.001   12.644  17.416  1.00 27.48  ? 152 ASN A OD1   1 
ATOM   1162 N ND2   . ASN A 1 159 ? 2.006   13.153  16.549  1.00 22.61  ? 152 ASN A ND2   1 
ATOM   1163 N N     . LEU A 1 160 ? -1.143  10.738  19.941  1.00 19.90  ? 153 LEU A N     1 
ATOM   1164 C CA    . LEU A 1 160 ? -2.038  9.643   20.405  1.00 19.24  ? 153 LEU A CA    1 
ATOM   1165 C C     . LEU A 1 160 ? -3.470  10.101  20.168  1.00 20.13  ? 153 LEU A C     1 
ATOM   1166 O O     . LEU A 1 160 ? -3.929  11.028  20.845  1.00 23.09  ? 153 LEU A O     1 
ATOM   1167 C CB    . LEU A 1 160 ? -1.765  9.326   21.872  1.00 18.79  ? 153 LEU A CB    1 
ATOM   1168 C CG    . LEU A 1 160 ? -0.298  9.068   22.224  1.00 19.52  ? 153 LEU A CG    1 
ATOM   1169 C CD1   . LEU A 1 160 ? -0.155  8.916   23.731  1.00 19.87  ? 153 LEU A CD1   1 
ATOM   1170 C CD2   . LEU A 1 160 ? 0.241   7.833   21.497  1.00 20.13  ? 153 LEU A CD2   1 
ATOM   1171 N N     . LEU A 1 161 ? -4.091  9.534   19.165  1.00 20.29  ? 154 LEU A N     1 
ATOM   1172 C CA    . LEU A 1 161 ? -5.464  9.915   18.800  1.00 21.74  ? 154 LEU A CA    1 
ATOM   1173 C C     . LEU A 1 161 ? -6.455  9.089   19.583  1.00 22.11  ? 154 LEU A C     1 
ATOM   1174 O O     . LEU A 1 161 ? -6.156  7.929   19.851  1.00 20.20  ? 154 LEU A O     1 
ATOM   1175 C CB    . LEU A 1 161 ? -5.682  9.664   17.313  1.00 22.98  ? 154 LEU A CB    1 
ATOM   1176 C CG    . LEU A 1 161 ? -4.621  10.265  16.409  1.00 23.83  ? 154 LEU A CG    1 
ATOM   1177 C CD1   . LEU A 1 161 ? -4.777  9.708   15.010  1.00 26.31  ? 154 LEU A CD1   1 
ATOM   1178 C CD2   . LEU A 1 161 ? -4.724  11.780  16.455  1.00 28.09  ? 154 LEU A CD2   1 
ATOM   1179 N N     . LEU A 1 162 ? -7.625  9.680   19.871  1.00 19.64  ? 155 LEU A N     1 
ATOM   1180 C CA    . LEU A 1 162 ? -8.729  9.001   20.565  1.00 22.42  ? 155 LEU A CA    1 
ATOM   1181 C C     . LEU A 1 162 ? -10.056 9.361   19.898  1.00 24.50  ? 155 LEU A C     1 
ATOM   1182 O O     . LEU A 1 162 ? -10.179 10.441  19.299  1.00 26.19  ? 155 LEU A O     1 
ATOM   1183 C CB    . LEU A 1 162 ? -8.763  9.389   22.035  1.00 26.06  ? 155 LEU A CB    1 
ATOM   1184 C CG    . LEU A 1 162 ? -7.482  9.052   22.773  1.00 28.30  ? 155 LEU A CG    1 
ATOM   1185 C CD1   . LEU A 1 162 ? -6.844  10.310  23.304  1.00 29.37  ? 155 LEU A CD1   1 
ATOM   1186 C CD2   . LEU A 1 162 ? -7.754  8.057   23.858  1.00 29.74  ? 155 LEU A CD2   1 
ATOM   1187 N N     . ASN A 1 163 ? -10.973 8.419   19.977  1.00 27.92  ? 156 ASN A N     1 
ATOM   1188 C CA    . ASN A 1 163 ? -12.356 8.542   19.446  1.00 30.55  ? 156 ASN A CA    1 
ATOM   1189 C C     . ASN A 1 163 ? -13.293 8.630   20.658  1.00 29.69  ? 156 ASN A C     1 
ATOM   1190 O O     . ASN A 1 163 ? -12.788 8.704   21.766  1.00 28.30  ? 156 ASN A O     1 
ATOM   1191 C CB    . ASN A 1 163 ? -12.611 7.401   18.465  1.00 29.70  ? 156 ASN A CB    1 
ATOM   1192 C CG    . ASN A 1 163 ? -12.721 6.077   19.178  1.00 31.34  ? 156 ASN A CG    1 
ATOM   1193 O OD1   . ASN A 1 163 ? -12.760 6.014   20.416  1.00 29.82  ? 156 ASN A OD1   1 
ATOM   1194 N ND2   . ASN A 1 163 ? -12.806 5.017   18.404  1.00 32.07  ? 156 ASN A ND2   1 
ATOM   1195 N N     . THR A 1 164 ? -14.620 8.702   20.470  1.00 33.45  ? 157 THR A N     1 
ATOM   1196 C CA    . THR A 1 164 ? -15.565 9.117   21.546  1.00 33.95  ? 157 THR A CA    1 
ATOM   1197 C C     . THR A 1 164 ? -15.750 7.962   22.528  1.00 34.73  ? 157 THR A C     1 
ATOM   1198 O O     . THR A 1 164 ? -16.317 8.196   23.626  1.00 37.18  ? 157 THR A O     1 
ATOM   1199 C CB    . THR A 1 164 ? -16.921 9.572   20.984  1.00 39.14  ? 157 THR A CB    1 
ATOM   1200 O OG1   . THR A 1 164 ? -17.417 8.514   20.168  1.00 45.08  ? 157 THR A OG1   1 
ATOM   1201 C CG2   . THR A 1 164 ? -16.818 10.840  20.175  1.00 40.17  ? 157 THR A CG2   1 
ATOM   1202 N N     . THR A 1 165 ? -15.291 6.759   22.171  1.00 30.93  ? 158 THR A N     1 
ATOM   1203 C CA    . THR A 1 165 ? -15.347 5.592   23.082  1.00 33.29  ? 158 THR A CA    1 
ATOM   1204 C C     . THR A 1 165 ? -13.940 5.279   23.620  1.00 32.19  ? 158 THR A C     1 
ATOM   1205 O O     . THR A 1 165 ? -13.741 4.153   24.084  1.00 33.99  ? 158 THR A O     1 
ATOM   1206 C CB    . THR A 1 165 ? -15.996 4.394   22.392  1.00 35.59  ? 158 THR A CB    1 
ATOM   1207 O OG1   . THR A 1 165 ? -15.258 4.192   21.205  1.00 34.84  ? 158 THR A OG1   1 
ATOM   1208 C CG2   . THR A 1 165 ? -17.441 4.629   22.021  1.00 39.28  ? 158 THR A CG2   1 
ATOM   1209 N N     . CYS A 1 166 ? -13.032 6.255   23.628  1.00 29.63  ? 159 CYS A N     1 
ATOM   1210 C CA    . CYS A 1 166 ? -11.705 6.127   24.291  1.00 28.79  ? 159 CYS A CA    1 
ATOM   1211 C C     . CYS A 1 166 ? -10.816 5.032   23.658  1.00 26.28  ? 159 CYS A C     1 
ATOM   1212 O O     . CYS A 1 166 ? -9.844  4.600   24.312  1.00 24.71  ? 159 CYS A O     1 
ATOM   1213 C CB    . CYS A 1 166 ? -11.933 5.939   25.785  1.00 32.68  ? 159 CYS A CB    1 
ATOM   1214 S SG    . CYS A 1 166 ? -12.813 7.364   26.476  1.00 39.92  ? 159 CYS A SG    1 
ATOM   1215 N N     . ASP A 1 167 ? -11.015 4.696   22.390  1.00 25.44  ? 160 ASP A N     1 
ATOM   1216 C CA    . ASP A 1 167 ? -10.048 3.874   21.612  1.00 27.79  ? 160 ASP A CA    1 
ATOM   1217 C C     . ASP A 1 167 ? -8.858  4.771   21.262  1.00 24.45  ? 160 ASP A C     1 
ATOM   1218 O O     . ASP A 1 167 ? -9.061  5.887   20.783  1.00 24.02  ? 160 ASP A O     1 
ATOM   1219 C CB    . ASP A 1 167 ? -10.674 3.284   20.337  1.00 28.79  ? 160 ASP A CB    1 
ATOM   1220 C CG    . ASP A 1 167 ? -11.874 2.399   20.656  1.00 34.04  ? 160 ASP A CG    1 
ATOM   1221 O OD1   . ASP A 1 167 ? -11.679 1.372   21.303  1.00 31.35  ? 160 ASP A OD1   1 
ATOM   1222 O OD2   . ASP A 1 167 ? -13.003 2.779   20.303  1.00 37.67  ? 160 ASP A OD2   1 
ATOM   1223 N N     . LEU A 1 168 ? -7.640  4.267   21.443  1.00 22.55  ? 161 LEU A N     1 
ATOM   1224 C CA    . LEU A 1 168 ? -6.394  5.046   21.288  1.00 20.10  ? 161 LEU A CA    1 
ATOM   1225 C C     . LEU A 1 168 ? -5.578  4.425   20.171  1.00 22.02  ? 161 LEU A C     1 
ATOM   1226 O O     . LEU A 1 168 ? -5.501  3.182   20.118  1.00 21.49  ? 161 LEU A O     1 
ATOM   1227 C CB    . LEU A 1 168 ? -5.634  5.037   22.620  1.00 19.94  ? 161 LEU A CB    1 
ATOM   1228 C CG    . LEU A 1 168 ? -4.344  5.866   22.694  1.00 18.72  ? 161 LEU A CG    1 
ATOM   1229 C CD1   . LEU A 1 168 ? -4.086  6.313   24.126  1.00 19.77  ? 161 LEU A CD1   1 
ATOM   1230 C CD2   . LEU A 1 168 ? -3.168  5.057   22.147  1.00 20.98  ? 161 LEU A CD2   1 
ATOM   1231 N N     . LYS A 1 169 ? -5.081  5.284   19.272  1.00 21.12  ? 162 LYS A N     1 
ATOM   1232 C CA    . LYS A 1 169 ? -4.265  4.909   18.108  1.00 20.98  ? 162 LYS A CA    1 
ATOM   1233 C C     . LYS A 1 169 ? -3.030  5.789   18.059  1.00 20.44  ? 162 LYS A C     1 
ATOM   1234 O O     . LYS A 1 169 ? -3.161  7.039   18.073  1.00 21.73  ? 162 LYS A O     1 
ATOM   1235 C CB    . LYS A 1 169 ? -5.054  5.051   16.814  1.00 21.61  ? 162 LYS A CB    1 
ATOM   1236 C CG    . LYS A 1 169 ? -6.283  4.140   16.755  1.00 23.52  ? 162 LYS A CG    1 
ATOM   1237 C CD    . LYS A 1 169 ? -6.877  4.098   15.384  1.00 24.51  ? 162 LYS A CD    1 
ATOM   1238 C CE    . LYS A 1 169 ? -8.191  3.342   15.294  1.00 29.13  ? 162 LYS A CE    1 
ATOM   1239 N NZ    . LYS A 1 169 ? -7.967  1.886   15.409  1.00 30.39  ? 162 LYS A NZ    1 
ATOM   1240 N N     . ILE A 1 170 ? -1.872  5.135   17.967  1.00 20.21  ? 163 ILE A N     1 
ATOM   1241 C CA    . ILE A 1 170 ? -0.594  5.853   17.805  1.00 18.50  ? 163 ILE A CA    1 
ATOM   1242 C C     . ILE A 1 170 ? -0.508  6.352   16.364  1.00 17.80  ? 163 ILE A C     1 
ATOM   1243 O O     . ILE A 1 170 ? -0.763  5.565   15.444  1.00 21.00  ? 163 ILE A O     1 
ATOM   1244 C CB    . ILE A 1 170 ? 0.589   4.957   18.198  1.00 17.70  ? 163 ILE A CB    1 
ATOM   1245 C CG1   . ILE A 1 170 ? 0.469   4.454   19.642  1.00 17.51  ? 163 ILE A CG1   1 
ATOM   1246 C CG2   . ILE A 1 170 ? 1.909   5.685   17.937  1.00 17.06  ? 163 ILE A CG2   1 
ATOM   1247 C CD1   . ILE A 1 170 ? 1.407   3.298   19.953  1.00 19.02  ? 163 ILE A CD1   1 
ATOM   1248 N N     . CYS A 1 171 ? -0.132  7.607   16.169  1.00 21.62  ? 164 CYS A N     1 
ATOM   1249 C CA    . CYS A 1 171 ? 0.089   8.162   14.803  1.00 23.89  ? 164 CYS A CA    1 
ATOM   1250 C C     . CYS A 1 171 ? 1.453   8.857   14.738  1.00 23.80  ? 164 CYS A C     1 
ATOM   1251 O O     . CYS A 1 171 ? 2.176   8.832   15.731  1.00 23.18  ? 164 CYS A O     1 
ATOM   1252 C CB    . CYS A 1 171 ? -1.023  9.136   14.430  1.00 25.24  ? 164 CYS A CB    1 
ATOM   1253 S SG    . CYS A 1 171 ? -0.948  10.698  15.341  1.00 30.46  ? 164 CYS A SG    1 
ATOM   1254 N N     . ASP A 1 172 ? 1.780   9.375   13.559  1.00 27.19  ? 165 ASP A N     1 
ATOM   1255 C CA    . ASP A 1 172 ? 2.968   10.213  13.241  1.00 26.37  ? 165 ASP A CA    1 
ATOM   1256 C C     . ASP A 1 172 ? 4.268   9.401   13.348  1.00 27.54  ? 165 ASP A C     1 
ATOM   1257 O O     . ASP A 1 172 ? 5.016   9.614   14.296  1.00 25.69  ? 165 ASP A O     1 
ATOM   1258 C CB    . ASP A 1 172 ? 2.998   11.436  14.134  1.00 32.44  ? 165 ASP A CB    1 
ATOM   1259 C CG    . ASP A 1 172 ? 3.909   12.522  13.600  1.00 39.48  ? 165 ASP A CG    1 
ATOM   1260 O OD1   . ASP A 1 172 ? 4.782   12.212  12.735  1.00 41.35  ? 165 ASP A OD1   1 
ATOM   1261 O OD2   . ASP A 1 172 ? 3.729   13.656  14.044  1.00 48.30  ? 165 ASP A OD2   1 
ATOM   1262 N N     . PHE A 1 173 ? 4.575   8.605   12.320  1.00 25.66  ? 166 PHE A N     1 
ATOM   1263 C CA    . PHE A 1 173 ? 5.797   7.773   12.217  1.00 24.39  ? 166 PHE A CA    1 
ATOM   1264 C C     . PHE A 1 173 ? 6.873   8.483   11.376  1.00 25.07  ? 166 PHE A C     1 
ATOM   1265 O O     . PHE A 1 173 ? 7.807   7.825   10.891  1.00 25.43  ? 166 PHE A O     1 
ATOM   1266 C CB    . PHE A 1 173 ? 5.402   6.403   11.690  1.00 23.18  ? 166 PHE A CB    1 
ATOM   1267 C CG    . PHE A 1 173 ? 4.713   5.554   12.730  1.00 25.80  ? 166 PHE A CG    1 
ATOM   1268 C CD1   . PHE A 1 173 ? 3.373   5.742   13.053  1.00 26.29  ? 166 PHE A CD1   1 
ATOM   1269 C CD2   . PHE A 1 173 ? 5.417   4.590   13.428  1.00 23.51  ? 166 PHE A CD2   1 
ATOM   1270 C CE1   . PHE A 1 173 ? 2.753   4.959   14.024  1.00 24.99  ? 166 PHE A CE1   1 
ATOM   1271 C CE2   . PHE A 1 173 ? 4.792   3.790   14.375  1.00 23.68  ? 166 PHE A CE2   1 
ATOM   1272 C CZ    . PHE A 1 173 ? 3.456   3.960   14.663  1.00 22.89  ? 166 PHE A CZ    1 
ATOM   1273 N N     . GLY A 1 174 ? 6.757   9.802   11.244  1.00 26.02  ? 167 GLY A N     1 
ATOM   1274 C CA    . GLY A 1 174 ? 7.691   10.645  10.466  1.00 30.71  ? 167 GLY A CA    1 
ATOM   1275 C C     . GLY A 1 174 ? 9.125   10.601  10.962  1.00 30.14  ? 167 GLY A C     1 
ATOM   1276 O O     . GLY A 1 174 ? 10.035  10.746  10.115  1.00 30.55  ? 167 GLY A O     1 
ATOM   1277 N N     . LEU A 1 175 ? 9.360   10.403  12.265  1.00 27.77  ? 168 LEU A N     1 
ATOM   1278 C CA    . LEU A 1 175 ? 10.727  10.348  12.837  1.00 28.03  ? 168 LEU A CA    1 
ATOM   1279 C C     . LEU A 1 175 ? 11.111  8.922   13.223  1.00 25.94  ? 168 LEU A C     1 
ATOM   1280 O O     . LEU A 1 175 ? 12.181  8.744   13.806  1.00 25.44  ? 168 LEU A O     1 
ATOM   1281 C CB    . LEU A 1 175 ? 10.775  11.281  14.043  1.00 33.92  ? 168 LEU A CB    1 
ATOM   1282 C CG    . LEU A 1 175 ? 10.717  12.758  13.667  1.00 39.11  ? 168 LEU A CG    1 
ATOM   1283 C CD1   . LEU A 1 175 ? 10.424  13.622  14.889  1.00 39.57  ? 168 LEU A CD1   1 
ATOM   1284 C CD2   . LEU A 1 175 ? 12.018  13.178  13.008  1.00 40.81  ? 168 LEU A CD2   1 
ATOM   1285 N N     . ALA A 1 176 ? 10.346  7.927   12.792  1.00 25.16  ? 169 ALA A N     1 
ATOM   1286 C CA    . ALA A 1 176 ? 10.567  6.521   13.168  1.00 24.61  ? 169 ALA A CA    1 
ATOM   1287 C C     . ALA A 1 176 ? 11.839  6.009   12.489  1.00 30.43  ? 169 ALA A C     1 
ATOM   1288 O O     . ALA A 1 176 ? 12.221  6.537   11.409  1.00 31.39  ? 169 ALA A O     1 
ATOM   1289 C CB    . ALA A 1 176 ? 9.360   5.697   12.825  1.00 24.30  ? 169 ALA A CB    1 
ATOM   1290 N N     . ARG A 1 177 ? 12.537  5.074   13.125  1.00 26.03  ? 170 ARG A N     1 
ATOM   1291 C CA    . ARG A 1 177 ? 13.731  4.421   12.528  1.00 28.11  ? 170 ARG A CA    1 
ATOM   1292 C C     . ARG A 1 177 ? 13.684  2.923   12.832  1.00 26.44  ? 170 ARG A C     1 
ATOM   1293 O O     . ARG A 1 177 ? 13.042  2.544   13.800  1.00 24.12  ? 170 ARG A O     1 
ATOM   1294 C CB    . ARG A 1 177 ? 15.027  5.021   13.091  1.00 33.07  ? 170 ARG A CB    1 
ATOM   1295 C CG    . ARG A 1 177 ? 15.212  6.517   12.859  1.00 38.69  ? 170 ARG A CG    1 
ATOM   1296 C CD    . ARG A 1 177 ? 15.860  6.780   11.504  1.00 45.59  ? 170 ARG A CD    1 
ATOM   1297 N NE    . ARG A 1 177 ? 16.373  8.144   11.441  1.00 50.86  ? 170 ARG A NE    1 
ATOM   1298 C CZ    . ARG A 1 177 ? 15.619  9.232   11.277  1.00 53.83  ? 170 ARG A CZ    1 
ATOM   1299 N NH1   . ARG A 1 177 ? 14.303  9.132   11.129  1.00 49.44  ? 170 ARG A NH1   1 
ATOM   1300 N NH2   . ARG A 1 177 ? 16.196  10.424  11.270  1.00 53.56  ? 170 ARG A NH2   1 
ATOM   1301 N N     . VAL A 1 178 ? 14.440  2.125   12.076  1.00 27.02  ? 171 VAL A N     1 
ATOM   1302 C CA    . VAL A 1 178 ? 14.743  0.720   12.437  1.00 26.37  ? 171 VAL A CA    1 
ATOM   1303 C C     . VAL A 1 178 ? 15.707  0.745   13.610  1.00 27.32  ? 171 VAL A C     1 
ATOM   1304 O O     . VAL A 1 178 ? 16.616  1.585   13.600  1.00 27.85  ? 171 VAL A O     1 
ATOM   1305 C CB    . VAL A 1 178 ? 15.277  -0.056  11.224  1.00 31.16  ? 171 VAL A CB    1 
ATOM   1306 C CG1   . VAL A 1 178 ? 15.561  -1.500  11.564  1.00 32.65  ? 171 VAL A CG1   1 
ATOM   1307 C CG2   . VAL A 1 178 ? 14.275  0.013   10.089  1.00 34.56  ? 171 VAL A CG2   1 
ATOM   1308 N N     . ALA A 1 179 ? 15.474  -0.042  14.653  1.00 24.87  ? 172 ALA A N     1 
ATOM   1309 C CA    . ALA A 1 179 ? 16.326  -0.023  15.860  1.00 27.20  ? 172 ALA A CA    1 
ATOM   1310 C C     . ALA A 1 179 ? 17.760  -0.384  15.455  1.00 32.12  ? 172 ALA A C     1 
ATOM   1311 O O     . ALA A 1 179 ? 17.925  -1.180  14.517  1.00 27.84  ? 172 ALA A O     1 
ATOM   1312 C CB    . ALA A 1 179 ? 15.798  -0.969  16.907  1.00 30.08  ? 172 ALA A CB    1 
ATOM   1313 N N     . ASP A 1 180 ? 18.768  0.209   16.106  1.00 35.20  ? 173 ASP A N     1 
ATOM   1314 C CA    . ASP A 1 180 ? 20.196  -0.089  15.810  1.00 34.89  ? 173 ASP A CA    1 
ATOM   1315 C C     . ASP A 1 180 ? 21.042  0.189   17.039  1.00 34.17  ? 173 ASP A C     1 
ATOM   1316 O O     . ASP A 1 180 ? 21.779  1.185   17.067  1.00 33.21  ? 173 ASP A O     1 
ATOM   1317 C CB    . ASP A 1 180 ? 20.669  0.727   14.621  1.00 34.50  ? 173 ASP A CB    1 
ATOM   1318 C CG    . ASP A 1 180 ? 22.059  0.368   14.110  1.00 36.74  ? 173 ASP A CG    1 
ATOM   1319 O OD1   . ASP A 1 180 ? 22.627  -0.650  14.562  1.00 36.10  ? 173 ASP A OD1   1 
ATOM   1320 O OD2   . ASP A 1 180 ? 22.546  1.112   13.252  1.00 38.96  ? 173 ASP A OD2   1 
ATOM   1321 N N     . PRO A 1 181 ? 20.929  -0.675  18.073  1.00 37.04  ? 174 PRO A N     1 
ATOM   1322 C CA    . PRO A 1 181 ? 21.628  -0.480  19.348  1.00 39.43  ? 174 PRO A CA    1 
ATOM   1323 C C     . PRO A 1 181 ? 23.158  -0.453  19.235  1.00 44.52  ? 174 PRO A C     1 
ATOM   1324 O O     . PRO A 1 181 ? 23.788  0.254   20.007  1.00 48.29  ? 174 PRO A O     1 
ATOM   1325 C CB    . PRO A 1 181 ? 21.178  -1.662  20.239  1.00 39.34  ? 174 PRO A CB    1 
ATOM   1326 C CG    . PRO A 1 181 ? 20.423  -2.606  19.333  1.00 40.09  ? 174 PRO A CG    1 
ATOM   1327 C CD    . PRO A 1 181 ? 19.997  -1.813  18.122  1.00 41.19  ? 174 PRO A CD    1 
ATOM   1328 N N     . ASP A 1 182 ? 23.711  -1.200  18.277  1.00 43.69  ? 175 ASP A N     1 
ATOM   1329 C CA    . ASP A 1 182 ? 25.172  -1.295  18.023  1.00 49.97  ? 175 ASP A CA    1 
ATOM   1330 C C     . ASP A 1 182 ? 25.735  0.076   17.641  1.00 47.17  ? 175 ASP A C     1 
ATOM   1331 O O     . ASP A 1 182 ? 26.952  0.252   17.806  1.00 49.91  ? 175 ASP A O     1 
ATOM   1332 C CB    . ASP A 1 182 ? 25.488  -2.291  16.899  1.00 55.80  ? 175 ASP A CB    1 
ATOM   1333 C CG    . ASP A 1 182 ? 24.981  -3.705  17.136  1.00 53.30  ? 175 ASP A CG    1 
ATOM   1334 O OD1   . ASP A 1 182 ? 24.834  -4.097  18.305  1.00 56.41  ? 175 ASP A OD1   1 
ATOM   1335 O OD2   . ASP A 1 182 ? 24.719  -4.395  16.138  1.00 65.49  ? 175 ASP A OD2   1 
ATOM   1336 N N     . HIS A 1 183 ? 24.902  0.979   17.112  1.00 42.92  ? 176 HIS A N     1 
ATOM   1337 C CA    . HIS A 1 183 ? 25.312  2.291   16.537  1.00 43.26  ? 176 HIS A CA    1 
ATOM   1338 C C     . HIS A 1 183 ? 24.659  3.480   17.285  1.00 38.87  ? 176 HIS A C     1 
ATOM   1339 O O     . HIS A 1 183 ? 24.613  4.597   16.725  1.00 38.19  ? 176 HIS A O     1 
ATOM   1340 C CB    . HIS A 1 183 ? 24.989  2.298   15.038  1.00 47.03  ? 176 HIS A CB    1 
ATOM   1341 C CG    . HIS A 1 183 ? 25.810  1.342   14.234  1.00 54.21  ? 176 HIS A CG    1 
ATOM   1342 N ND1   . HIS A 1 183 ? 25.557  -0.023  14.208  1.00 58.51  ? 176 HIS A ND1   1 
ATOM   1343 C CD2   . HIS A 1 183 ? 26.849  1.554   13.395  1.00 55.02  ? 176 HIS A CD2   1 
ATOM   1344 C CE1   . HIS A 1 183 ? 26.422  -0.608  13.408  1.00 57.27  ? 176 HIS A CE1   1 
ATOM   1345 N NE2   . HIS A 1 183 ? 27.222  0.344   12.891  1.00 55.88  ? 176 HIS A NE2   1 
ATOM   1346 N N     . ASP A 1 184 ? 24.245  3.287   18.538  1.00 32.67  ? 177 ASP A N     1 
ATOM   1347 C CA    . ASP A 1 184 ? 23.491  4.289   19.350  1.00 30.18  ? 177 ASP A CA    1 
ATOM   1348 C C     . ASP A 1 184 ? 24.441  5.333   19.973  1.00 30.84  ? 177 ASP A C     1 
ATOM   1349 O O     . ASP A 1 184 ? 24.001  6.453   20.294  1.00 30.10  ? 177 ASP A O     1 
ATOM   1350 C CB    . ASP A 1 184 ? 22.726  3.566   20.452  1.00 32.04  ? 177 ASP A CB    1 
ATOM   1351 C CG    . ASP A 1 184 ? 21.816  4.485   21.237  1.00 29.92  ? 177 ASP A CG    1 
ATOM   1352 O OD1   . ASP A 1 184 ? 20.934  5.008   20.631  1.00 34.10  ? 177 ASP A OD1   1 
ATOM   1353 O OD2   . ASP A 1 184 ? 22.069  4.700   22.422  1.00 32.37  ? 177 ASP A OD2   1 
ATOM   1354 N N     . HIS A 1 185 ? 25.722  5.019   20.150  1.00 33.26  ? 178 HIS A N     1 
ATOM   1355 C CA    . HIS A 1 185 ? 26.614  5.864   20.985  1.00 36.67  ? 178 HIS A CA    1 
ATOM   1356 C C     . HIS A 1 185 ? 27.021  7.111   20.199  1.00 38.86  ? 178 HIS A C     1 
ATOM   1357 O O     . HIS A 1 185 ? 27.182  7.034   18.970  1.00 39.34  ? 178 HIS A O     1 
ATOM   1358 C CB    . HIS A 1 185 ? 27.825  5.111   21.520  1.00 39.59  ? 178 HIS A CB    1 
ATOM   1359 C CG    . HIS A 1 185 ? 28.552  5.932   22.528  1.00 48.17  ? 178 HIS A CG    1 
ATOM   1360 N ND1   . HIS A 1 185 ? 29.379  6.993   22.170  1.00 52.95  ? 178 HIS A ND1   1 
ATOM   1361 C CD2   . HIS A 1 185 ? 28.566  5.893   23.884  1.00 54.23  ? 178 HIS A CD2   1 
ATOM   1362 C CE1   . HIS A 1 185 ? 29.862  7.565   23.264  1.00 43.94  ? 178 HIS A CE1   1 
ATOM   1363 N NE2   . HIS A 1 185 ? 29.400  6.902   24.320  1.00 48.44  ? 178 HIS A NE2   1 
ATOM   1364 N N     . THR A 1 186 ? 27.137  8.241   20.895  1.00 36.36  ? 179 THR A N     1 
ATOM   1365 C CA    . THR A 1 186 ? 27.565  9.531   20.314  1.00 35.36  ? 179 THR A CA    1 
ATOM   1366 C C     . THR A 1 186 ? 28.094  10.419  21.450  1.00 35.10  ? 179 THR A C     1 
ATOM   1367 O O     . THR A 1 186 ? 28.157  9.956   22.600  1.00 33.77  ? 179 THR A O     1 
ATOM   1368 C CB    . THR A 1 186 ? 26.407  10.153  19.520  1.00 35.84  ? 179 THR A CB    1 
ATOM   1369 O OG1   . THR A 1 186 ? 26.992  11.200  18.744  1.00 40.56  ? 179 THR A OG1   1 
ATOM   1370 C CG2   . THR A 1 186 ? 25.286  10.680  20.398  1.00 36.01  ? 179 THR A CG2   1 
ATOM   1371 N N     . GLY A 1 187 ? 28.476  11.644  21.106  1.00 34.08  ? 180 GLY A N     1 
ATOM   1372 C CA    . GLY A 1 187 ? 29.072  12.614  22.030  1.00 32.02  ? 180 GLY A CA    1 
ATOM   1373 C C     . GLY A 1 187 ? 28.008  13.380  22.780  1.00 30.11  ? 180 GLY A C     1 
ATOM   1374 O O     . GLY A 1 187 ? 26.802  13.178  22.539  1.00 29.01  ? 180 GLY A O     1 
ATOM   1375 N N     . PHE A 1 188 ? 28.471  14.232  23.687  1.00 28.55  ? 181 PHE A N     1 
ATOM   1376 C CA    . PHE A 1 188 ? 27.655  15.090  24.575  1.00 28.76  ? 181 PHE A CA    1 
ATOM   1377 C C     . PHE A 1 188 ? 26.988  16.183  23.740  1.00 26.70  ? 181 PHE A C     1 
ATOM   1378 O O     . PHE A 1 188 ? 27.671  16.776  22.888  1.00 26.72  ? 181 PHE A O     1 
ATOM   1379 C CB    . PHE A 1 188 ? 28.594  15.600  25.668  1.00 29.11  ? 181 PHE A CB    1 
ATOM   1380 C CG    . PHE A 1 188 ? 28.009  16.549  26.671  1.00 30.82  ? 181 PHE A CG    1 
ATOM   1381 C CD1   . PHE A 1 188 ? 26.882  16.211  27.400  1.00 31.57  ? 181 PHE A CD1   1 
ATOM   1382 C CD2   . PHE A 1 188 ? 28.638  17.753  26.943  1.00 30.09  ? 181 PHE A CD2   1 
ATOM   1383 C CE1   . PHE A 1 188 ? 26.379  17.070  28.359  1.00 29.95  ? 181 PHE A CE1   1 
ATOM   1384 C CE2   . PHE A 1 188 ? 28.125  18.611  27.897  1.00 29.72  ? 181 PHE A CE2   1 
ATOM   1385 C CZ    . PHE A 1 188 ? 26.976  18.286  28.581  1.00 29.75  ? 181 PHE A CZ    1 
ATOM   1386 N N     . LEU A 1 189 ? 25.730  16.493  24.046  1.00 27.87  ? 182 LEU A N     1 
ATOM   1387 C CA    . LEU A 1 189 ? 24.986  17.649  23.483  1.00 30.57  ? 182 LEU A CA    1 
ATOM   1388 C C     . LEU A 1 189 ? 24.911  17.550  21.941  1.00 33.90  ? 182 LEU A C     1 
ATOM   1389 O O     . LEU A 1 189 ? 25.031  18.595  21.255  1.00 36.99  ? 182 LEU A O     1 
ATOM   1390 C CB    . LEU A 1 189 ? 25.671  18.950  23.929  1.00 37.47  ? 182 LEU A CB    1 
ATOM   1391 C CG    . LEU A 1 189 ? 25.767  19.209  25.439  1.00 37.56  ? 182 LEU A CG    1 
ATOM   1392 C CD1   . LEU A 1 189 ? 26.431  20.548  25.704  1.00 41.84  ? 182 LEU A CD1   1 
ATOM   1393 C CD2   . LEU A 1 189 ? 24.420  19.140  26.140  1.00 39.72  ? 182 LEU A CD2   1 
ATOM   1394 N N     . THR A 1 190 ? 24.711  16.348  21.400  1.00 34.95  ? 183 THR A N     1 
ATOM   1395 C CA    . THR A 1 190 ? 24.523  16.089  19.942  1.00 38.27  ? 183 THR A CA    1 
ATOM   1396 C C     . THR A 1 190 ? 23.076  16.431  19.594  1.00 41.58  ? 183 THR A C     1 
ATOM   1397 O O     . THR A 1 190 ? 22.166  15.997  20.341  1.00 38.32  ? 183 THR A O     1 
ATOM   1398 C CB    . THR A 1 190 ? 24.811  14.631  19.563  1.00 43.00  ? 183 THR A CB    1 
ATOM   1399 O OG1   . THR A 1 190 ? 26.160  14.324  19.909  1.00 46.75  ? 183 THR A OG1   1 
ATOM   1400 C CG2   . THR A 1 190 ? 24.608  14.347  18.092  1.00 47.04  ? 183 THR A CG2   1 
ATOM   1401 N N     . GLU A 1 191 ? 22.866  17.156  18.503  1.00 41.74  ? 184 GLU A N     1 
ATOM   1402 C CA    . GLU A 1 191 ? 21.572  17.826  18.207  1.00 46.22  ? 184 GLU A CA    1 
ATOM   1403 C C     . GLU A 1 191 ? 20.534  16.735  17.870  1.00 53.73  ? 184 GLU A C     1 
ATOM   1404 O O     . GLU A 1 191 ? 20.942  15.632  17.420  1.00 54.86  ? 184 GLU A O     1 
ATOM   1405 C CB    . GLU A 1 191 ? 21.809  18.893  17.127  1.00 55.56  ? 184 GLU A CB    1 
ATOM   1406 C CG    . GLU A 1 191 ? 22.769  20.019  17.554  1.00 59.11  ? 184 GLU A CG    1 
ATOM   1407 C CD    . GLU A 1 191 ? 22.446  20.759  18.857  1.00 61.60  ? 184 GLU A CD    1 
ATOM   1408 O OE1   . GLU A 1 191 ? 21.251  20.985  19.133  1.00 54.93  ? 184 GLU A OE1   1 
ATOM   1409 O OE2   . GLU A 1 191 ? 23.394  21.102  19.620  1.00 68.31  ? 184 GLU A OE2   1 
ATOM   1410 N N     . TYR A 1 192 ? 19.247  16.991  18.129  1.00 53.63  ? 185 TYR A N     1 
ATOM   1411 C CA    . TYR A 1 192 ? 18.157  15.986  18.015  1.00 53.83  ? 185 TYR A CA    1 
ATOM   1412 C C     . TYR A 1 192 ? 16.865  16.673  17.567  1.00 53.30  ? 185 TYR A C     1 
ATOM   1413 O O     . TYR A 1 192 ? 16.801  17.898  17.712  1.00 49.53  ? 185 TYR A O     1 
ATOM   1414 C CB    . TYR A 1 192 ? 17.958  15.296  19.359  1.00 47.74  ? 185 TYR A CB    1 
ATOM   1415 C CG    . TYR A 1 192 ? 17.287  13.946  19.295  1.00 47.68  ? 185 TYR A CG    1 
ATOM   1416 C CD1   . TYR A 1 192 ? 17.961  12.828  18.803  1.00 46.43  ? 185 TYR A CD1   1 
ATOM   1417 C CD2   . TYR A 1 192 ? 16.005  13.768  19.799  1.00 50.45  ? 185 TYR A CD2   1 
ATOM   1418 C CE1   . TYR A 1 192 ? 17.368  11.574  18.791  1.00 43.26  ? 185 TYR A CE1   1 
ATOM   1419 C CE2   . TYR A 1 192 ? 15.396  12.525  19.785  1.00 47.94  ? 185 TYR A CE2   1 
ATOM   1420 C CZ    . TYR A 1 192 ? 16.079  11.429  19.289  1.00 45.82  ? 185 TYR A CZ    1 
ATOM   1421 O OH    . TYR A 1 192 ? 15.456  10.218  19.295  1.00 49.59  ? 185 TYR A OH    1 
ATOM   1422 N N     . VAL A 1 193 ? 15.869  15.898  17.117  1.00 54.23  ? 186 VAL A N     1 
ATOM   1423 C CA    . VAL A 1 193 ? 14.669  16.401  16.369  1.00 58.08  ? 186 VAL A CA    1 
ATOM   1424 C C     . VAL A 1 193 ? 13.377  16.277  17.211  1.00 52.67  ? 186 VAL A C     1 
ATOM   1425 O O     . VAL A 1 193 ? 12.558  17.254  17.200  1.00 51.24  ? 186 VAL A O     1 
ATOM   1426 C CB    . VAL A 1 193 ? 14.549  15.683  15.008  1.00 55.87  ? 186 VAL A CB    1 
ATOM   1427 C CG1   . VAL A 1 193 ? 13.506  16.339  14.109  1.00 61.54  ? 186 VAL A CG1   1 
ATOM   1428 C CG2   . VAL A 1 193 ? 15.891  15.620  14.292  1.00 59.18  ? 186 VAL A CG2   1 
ATOM   1429 N N     . ALA A 1 194 ? 13.183  15.145  17.899  1.00 43.23  ? 187 ALA A N     1 
ATOM   1430 C CA    . ALA A 1 194 ? 11.941  14.764  18.629  1.00 46.69  ? 187 ALA A CA    1 
ATOM   1431 C C     . ALA A 1 194 ? 11.708  15.693  19.823  1.00 41.48  ? 187 ALA A C     1 
ATOM   1432 O O     . ALA A 1 194 ? 12.694  16.182  20.343  1.00 34.25  ? 187 ALA A O     1 
ATOM   1433 C CB    . ALA A 1 194 ? 12.040  13.333  19.115  1.00 45.37  ? 187 ALA A CB    1 
ATOM   1434 N N     . GLU A 1 195 ? 10.451  15.824  20.279  1.00 40.07  ? 188 GLU A N     1 
ATOM   1435 C CA    . GLU A 1 195 ? 9.988   16.887  21.197  1.00 35.67  ? 188 GLU A CA    1 
ATOM   1436 C C     . GLU A 1 195 ? 10.798  16.811  22.498  1.00 33.77  ? 188 GLU A C     1 
ATOM   1437 O O     . GLU A 1 195 ? 10.851  15.735  23.131  1.00 28.78  ? 188 GLU A O     1 
ATOM   1438 C CB    . GLU A 1 195 ? 8.478   16.779  21.423  1.00 39.77  ? 188 GLU A CB    1 
ATOM   1439 C CG    . GLU A 1 195 ? 7.958   17.591  22.598  1.00 45.51  ? 188 GLU A CG    1 
ATOM   1440 C CD    . GLU A 1 195 ? 8.257   19.083  22.586  1.00 59.00  ? 188 GLU A CD    1 
ATOM   1441 O OE1   . GLU A 1 195 ? 8.100   19.659  21.483  1.00 58.02  ? 188 GLU A OE1   1 
ATOM   1442 O OE2   . GLU A 1 195 ? 8.660   19.672  23.691  1.00 46.20  ? 188 GLU A OE2   1 
ATOM   1443 N N     . ARG A 1 196 ? 11.343  17.958  22.924  1.00 31.34  ? 189 ARG A N     1 
ATOM   1444 C CA    . ARG A 1 196 ? 12.293  18.077  24.049  1.00 28.25  ? 189 ARG A CA    1 
ATOM   1445 C C     . ARG A 1 196 ? 11.733  17.450  25.333  1.00 25.28  ? 189 ARG A C     1 
ATOM   1446 O O     . ARG A 1 196 ? 12.459  16.775  26.052  1.00 22.94  ? 189 ARG A O     1 
ATOM   1447 C CB    . ARG A 1 196 ? 12.530  19.575  24.281  1.00 31.26  ? 189 ARG A CB    1 
ATOM   1448 C CG    . ARG A 1 196 ? 13.459  19.871  25.431  1.00 31.00  ? 189 ARG A CG    1 
ATOM   1449 C CD    . ARG A 1 196 ? 13.613  21.366  25.679  1.00 37.40  ? 189 ARG A CD    1 
ATOM   1450 N NE    . ARG A 1 196 ? 13.838  22.092  24.438  1.00 34.93  ? 189 ARG A NE    1 
ATOM   1451 C CZ    . ARG A 1 196 ? 13.098  23.095  23.977  1.00 38.96  ? 189 ARG A CZ    1 
ATOM   1452 N NH1   . ARG A 1 196 ? 12.053  23.568  24.643  1.00 34.02  ? 189 ARG A NH1   1 
ATOM   1453 N NH2   . ARG A 1 196 ? 13.437  23.636  22.818  1.00 45.98  ? 189 ARG A NH2   1 
ATOM   1454 N N     . TRP A 1 197 ? 10.490  17.757  25.662  1.00 22.34  ? 190 TRP A N     1 
ATOM   1455 C CA    . TRP A 1 197 ? 9.879   17.370  26.953  1.00 24.99  ? 190 TRP A CA    1 
ATOM   1456 C C     . TRP A 1 197 ? 9.785   15.839  27.105  1.00 20.26  ? 190 TRP A C     1 
ATOM   1457 O O     . TRP A 1 197 ? 9.699   15.437  28.214  1.00 19.75  ? 190 TRP A O     1 
ATOM   1458 C CB    . TRP A 1 197 ? 8.494   17.999  27.120  1.00 24.43  ? 190 TRP A CB    1 
ATOM   1459 C CG    . TRP A 1 197 ? 8.497   19.500  27.167  1.00 27.49  ? 190 TRP A CG    1 
ATOM   1460 C CD1   . TRP A 1 197 ? 9.576   20.319  27.232  1.00 29.33  ? 190 TRP A CD1   1 
ATOM   1461 C CD2   . TRP A 1 197 ? 7.342   20.357  27.182  1.00 28.63  ? 190 TRP A CD2   1 
ATOM   1462 N NE1   . TRP A 1 197 ? 9.169   21.628  27.292  1.00 31.05  ? 190 TRP A NE1   1 
ATOM   1463 C CE2   . TRP A 1 197 ? 7.808   21.684  27.282  1.00 28.91  ? 190 TRP A CE2   1 
ATOM   1464 C CE3   . TRP A 1 197 ? 5.969   20.135  27.127  1.00 29.53  ? 190 TRP A CE3   1 
ATOM   1465 C CZ2   . TRP A 1 197 ? 6.944   22.787  27.300  1.00 30.65  ? 190 TRP A CZ2   1 
ATOM   1466 C CZ3   . TRP A 1 197 ? 5.108   21.214  27.177  1.00 30.32  ? 190 TRP A CZ3   1 
ATOM   1467 C CH2   . TRP A 1 197 ? 5.595   22.517  27.260  1.00 30.79  ? 190 TRP A CH2   1 
ATOM   1468 N N     . TYR A 1 198 ? 9.816   15.057  26.033  1.00 22.16  ? 191 TYR A N     1 
ATOM   1469 C CA    . TYR A 1 198 ? 9.646   13.583  26.088  1.00 20.53  ? 191 TYR A CA    1 
ATOM   1470 C C     . TYR A 1 198 ? 10.970  12.900  25.728  1.00 21.83  ? 191 TYR A C     1 
ATOM   1471 O O     . TYR A 1 198 ? 10.976  11.671  25.526  1.00 20.97  ? 191 TYR A O     1 
ATOM   1472 C CB    . TYR A 1 198 ? 8.481   13.174  25.164  1.00 22.02  ? 191 TYR A CB    1 
ATOM   1473 C CG    . TYR A 1 198 ? 7.238   13.984  25.493  1.00 23.64  ? 191 TYR A CG    1 
ATOM   1474 C CD1   . TYR A 1 198 ? 6.382   13.599  26.510  1.00 22.68  ? 191 TYR A CD1   1 
ATOM   1475 C CD2   . TYR A 1 198 ? 7.006   15.207  24.885  1.00 24.06  ? 191 TYR A CD2   1 
ATOM   1476 C CE1   . TYR A 1 198 ? 5.326   14.402  26.914  1.00 22.36  ? 191 TYR A CE1   1 
ATOM   1477 C CE2   . TYR A 1 198 ? 5.938   16.007  25.254  1.00 23.25  ? 191 TYR A CE2   1 
ATOM   1478 C CZ    . TYR A 1 198 ? 5.108   15.612  26.280  1.00 23.20  ? 191 TYR A CZ    1 
ATOM   1479 O OH    . TYR A 1 198 ? 4.050   16.384  26.654  1.00 22.37  ? 191 TYR A OH    1 
ATOM   1480 N N     . ARG A 1 199 ? 12.079  13.654  25.677  1.00 20.91  ? 192 ARG A N     1 
ATOM   1481 C CA    . ARG A 1 199 ? 13.421  13.124  25.342  1.00 24.17  ? 192 ARG A CA    1 
ATOM   1482 C C     . ARG A 1 199 ? 14.116  12.486  26.537  1.00 21.01  ? 192 ARG A C     1 
ATOM   1483 O O     . ARG A 1 199 ? 14.250  13.167  27.529  1.00 21.33  ? 192 ARG A O     1 
ATOM   1484 C CB    . ARG A 1 199 ? 14.372  14.264  24.995  1.00 28.75  ? 192 ARG A CB    1 
ATOM   1485 C CG    . ARG A 1 199 ? 14.553  14.471  23.517  1.00 34.53  ? 192 ARG A CG    1 
ATOM   1486 C CD    . ARG A 1 199 ? 15.437  15.702  23.353  1.00 34.04  ? 192 ARG A CD    1 
ATOM   1487 N NE    . ARG A 1 199 ? 14.926  16.399  22.202  1.00 33.14  ? 192 ARG A NE    1 
ATOM   1488 C CZ    . ARG A 1 199 ? 15.166  17.660  21.913  1.00 39.88  ? 192 ARG A CZ    1 
ATOM   1489 N NH1   . ARG A 1 199 ? 15.919  18.403  22.711  1.00 33.42  ? 192 ARG A NH1   1 
ATOM   1490 N NH2   . ARG A 1 199 ? 14.625  18.167  20.821  1.00 40.80  ? 192 ARG A NH2   1 
ATOM   1491 N N     . ALA A 1 200 ? 14.605  11.259  26.376  1.00 20.96  ? 193 ALA A N     1 
ATOM   1492 C CA    . ALA A 1 200 ? 15.263  10.472  27.432  1.00 20.35  ? 193 ALA A CA    1 
ATOM   1493 C C     . ALA A 1 200 ? 16.600  11.144  27.747  1.00 22.26  ? 193 ALA A C     1 
ATOM   1494 O O     . ALA A 1 200 ? 17.160  11.835  26.890  1.00 23.11  ? 193 ALA A O     1 
ATOM   1495 C CB    . ALA A 1 200 ? 15.422  9.072   26.968  1.00 21.74  ? 193 ALA A CB    1 
ATOM   1496 N N     . PRO A 1 201 ? 17.080  11.065  29.007  1.00 22.42  ? 194 PRO A N     1 
ATOM   1497 C CA    . PRO A 1 201 ? 18.271  11.814  29.413  1.00 21.98  ? 194 PRO A CA    1 
ATOM   1498 C C     . PRO A 1 201 ? 19.504  11.471  28.563  1.00 24.35  ? 194 PRO A C     1 
ATOM   1499 O O     . PRO A 1 201 ? 20.325  12.390  28.277  1.00 26.49  ? 194 PRO A O     1 
ATOM   1500 C CB    . PRO A 1 201 ? 18.431  11.437  30.890  1.00 22.80  ? 194 PRO A CB    1 
ATOM   1501 C CG    . PRO A 1 201 ? 17.648  10.164  31.046  1.00 24.53  ? 194 PRO A CG    1 
ATOM   1502 C CD    . PRO A 1 201 ? 16.489  10.299  30.095  1.00 20.72  ? 194 PRO A CD    1 
ATOM   1503 N N     . GLU A 1 202 ? 19.611  10.212  28.152  1.00 20.84  ? 195 GLU A N     1 
ATOM   1504 C CA    . GLU A 1 202 ? 20.778  9.715   27.380  1.00 24.81  ? 195 GLU A CA    1 
ATOM   1505 C C     . GLU A 1 202 ? 20.862  10.473  26.041  1.00 27.61  ? 195 GLU A C     1 
ATOM   1506 O O     . GLU A 1 202 ? 21.990  10.612  25.516  1.00 26.04  ? 195 GLU A O     1 
ATOM   1507 C CB    . GLU A 1 202 ? 20.749  8.191   27.306  1.00 21.96  ? 195 GLU A CB    1 
ATOM   1508 C CG    . GLU A 1 202 ? 19.600  7.578   26.521  1.00 23.70  ? 195 GLU A CG    1 
ATOM   1509 C CD    . GLU A 1 202 ? 18.372  7.214   27.360  1.00 25.41  ? 195 GLU A CD    1 
ATOM   1510 O OE1   . GLU A 1 202 ? 18.228  7.756   28.471  1.00 22.54  ? 195 GLU A OE1   1 
ATOM   1511 O OE2   . GLU A 1 202 ? 17.552  6.421   26.876  1.00 23.87  ? 195 GLU A OE2   1 
ATOM   1512 N N     . ILE A 1 203 ? 19.752  11.035  25.525  1.00 25.70  ? 196 ILE A N     1 
ATOM   1513 C CA    . ILE A 1 203 ? 19.800  11.792  24.227  1.00 26.57  ? 196 ILE A CA    1 
ATOM   1514 C C     . ILE A 1 203 ? 20.784  12.959  24.378  1.00 30.66  ? 196 ILE A C     1 
ATOM   1515 O O     . ILE A 1 203 ? 21.538  13.254  23.424  1.00 30.61  ? 196 ILE A O     1 
ATOM   1516 C CB    . ILE A 1 203 ? 18.411  12.293  23.795  1.00 26.60  ? 196 ILE A CB    1 
ATOM   1517 C CG1   . ILE A 1 203 ? 17.451  11.131  23.529  1.00 26.18  ? 196 ILE A CG1   1 
ATOM   1518 C CG2   . ILE A 1 203 ? 18.531  13.262  22.616  1.00 26.58  ? 196 ILE A CG2   1 
ATOM   1519 C CD1   . ILE A 1 203 ? 17.931  10.174  22.504  1.00 26.70  ? 196 ILE A CD1   1 
ATOM   1520 N N     . MET A 1 204 ? 20.757  13.635  25.521  1.00 28.24  ? 197 MET A N     1 
ATOM   1521 C CA    . MET A 1 204 ? 21.592  14.832  25.758  1.00 29.71  ? 197 MET A CA    1 
ATOM   1522 C C     . MET A 1 204 ? 23.008  14.390  26.126  1.00 28.68  ? 197 MET A C     1 
ATOM   1523 O O     . MET A 1 204 ? 23.905  15.249  26.084  1.00 30.99  ? 197 MET A O     1 
ATOM   1524 C CB    . MET A 1 204 ? 21.007  15.702  26.873  1.00 29.56  ? 197 MET A CB    1 
ATOM   1525 C CG    . MET A 1 204 ? 19.769  16.473  26.426  1.00 32.67  ? 197 MET A CG    1 
ATOM   1526 S SD    . MET A 1 204 ? 18.237  15.494  26.238  1.00 32.86  ? 197 MET A SD    1 
ATOM   1527 C CE    . MET A 1 204 ? 17.772  15.249  27.951  1.00 29.21  ? 197 MET A CE    1 
ATOM   1528 N N     . LEU A 1 205 ? 23.192  13.118  26.467  1.00 27.08  ? 198 LEU A N     1 
ATOM   1529 C CA    . LEU A 1 205 ? 24.453  12.643  27.077  1.00 24.65  ? 198 LEU A CA    1 
ATOM   1530 C C     . LEU A 1 205 ? 25.307  11.852  26.093  1.00 29.24  ? 198 LEU A C     1 
ATOM   1531 O O     . LEU A 1 205 ? 26.515  12.244  25.947  1.00 29.05  ? 198 LEU A O     1 
ATOM   1532 C CB    . LEU A 1 205 ? 24.124  11.838  28.320  1.00 24.11  ? 198 LEU A CB    1 
ATOM   1533 C CG    . LEU A 1 205 ? 23.528  12.672  29.443  1.00 25.84  ? 198 LEU A CG    1 
ATOM   1534 C CD1   . LEU A 1 205 ? 22.964  11.791  30.518  1.00 23.66  ? 198 LEU A CD1   1 
ATOM   1535 C CD2   . LEU A 1 205 ? 24.558  13.639  30.022  1.00 26.59  ? 198 LEU A CD2   1 
ATOM   1536 N N     . ASN A 1 206 ? 24.762  10.796  25.467  1.00 27.66  ? 199 ASN A N     1 
ATOM   1537 C CA    . ASN A 1 206 ? 25.600  9.856   24.667  1.00 27.64  ? 199 ASN A CA    1 
ATOM   1538 C C     . ASN A 1 206 ? 24.800  9.000   23.681  1.00 29.53  ? 199 ASN A C     1 
ATOM   1539 O O     . ASN A 1 206 ? 25.371  8.021   23.203  1.00 26.62  ? 199 ASN A O     1 
ATOM   1540 C CB    . ASN A 1 206 ? 26.371  8.929   25.603  1.00 29.71  ? 199 ASN A CB    1 
ATOM   1541 C CG    . ASN A 1 206 ? 25.485  7.988   26.403  1.00 31.18  ? 199 ASN A CG    1 
ATOM   1542 O OD1   . ASN A 1 206 ? 24.252  7.994   26.305  1.00 28.08  ? 199 ASN A OD1   1 
ATOM   1543 N ND2   . ASN A 1 206 ? 26.115  7.143   27.203  1.00 33.21  ? 199 ASN A ND2   1 
ATOM   1544 N N     . SER A 1 207 ? 23.548  9.328   23.373  1.00 27.59  ? 200 SER A N     1 
ATOM   1545 C CA    . SER A 1 207 ? 22.635  8.434   22.607  1.00 27.28  ? 200 SER A CA    1 
ATOM   1546 C C     . SER A 1 207 ? 22.067  9.164   21.391  1.00 26.00  ? 200 SER A C     1 
ATOM   1547 O O     . SER A 1 207 ? 21.548  10.283  21.561  1.00 24.39  ? 200 SER A O     1 
ATOM   1548 C CB    . SER A 1 207 ? 21.484  7.898   23.463  1.00 28.58  ? 200 SER A CB    1 
ATOM   1549 O OG    . SER A 1 207 ? 20.584  7.081   22.690  1.00 26.40  ? 200 SER A OG    1 
ATOM   1550 N N     . LYS A 1 208 ? 22.078  8.494   20.241  1.00 26.18  ? 201 LYS A N     1 
ATOM   1551 C CA    . LYS A 1 208 ? 21.376  8.892   18.987  1.00 28.36  ? 201 LYS A CA    1 
ATOM   1552 C C     . LYS A 1 208 ? 19.894  8.509   19.011  1.00 27.53  ? 201 LYS A C     1 
ATOM   1553 O O     . LYS A 1 208 ? 19.208  8.799   18.027  1.00 29.21  ? 201 LYS A O     1 
ATOM   1554 C CB    . LYS A 1 208 ? 22.015  8.173   17.795  1.00 32.36  ? 201 LYS A CB    1 
ATOM   1555 C CG    . LYS A 1 208 ? 23.468  8.572   17.594  1.00 36.19  ? 201 LYS A CG    1 
ATOM   1556 C CD    . LYS A 1 208 ? 24.101  8.032   16.340  1.00 44.97  ? 201 LYS A CD    1 
ATOM   1557 C CE    . LYS A 1 208 ? 25.295  8.858   15.917  1.00 52.14  ? 201 LYS A CE    1 
ATOM   1558 N NZ    . LYS A 1 208 ? 25.540  8.749   14.460  1.00 61.67  ? 201 LYS A NZ    1 
ATOM   1559 N N     . GLY A 1 209 ? 19.440  7.782   20.029  1.00 27.46  ? 202 GLY A N     1 
ATOM   1560 C CA    . GLY A 1 209 ? 18.015  7.387   20.127  1.00 29.75  ? 202 GLY A CA    1 
ATOM   1561 C C     . GLY A 1 209 ? 17.679  6.274   19.157  1.00 26.54  ? 202 GLY A C     1 
ATOM   1562 O O     . GLY A 1 209 ? 16.576  6.281   18.596  1.00 27.74  ? 202 GLY A O     1 
ATOM   1563 N N     . TYR A 1 210 ? 18.575  5.306   19.033  1.00 23.40  ? 203 TYR A N     1 
ATOM   1564 C CA    . TYR A 1 210 ? 18.432  4.123   18.158  1.00 24.92  ? 203 TYR A CA    1 
ATOM   1565 C C     . TYR A 1 210 ? 18.102  2.887   18.996  1.00 26.11  ? 203 TYR A C     1 
ATOM   1566 O O     . TYR A 1 210 ? 18.285  1.754   18.466  1.00 28.46  ? 203 TYR A O     1 
ATOM   1567 C CB    . TYR A 1 210 ? 19.721  3.904   17.357  1.00 28.14  ? 203 TYR A CB    1 
ATOM   1568 C CG    . TYR A 1 210 ? 20.031  4.976   16.335  1.00 29.72  ? 203 TYR A CG    1 
ATOM   1569 C CD1   . TYR A 1 210 ? 19.097  5.931   15.977  1.00 34.31  ? 203 TYR A CD1   1 
ATOM   1570 C CD2   . TYR A 1 210 ? 21.279  5.041   15.725  1.00 36.93  ? 203 TYR A CD2   1 
ATOM   1571 C CE1   . TYR A 1 210 ? 19.380  6.921   15.048  1.00 37.75  ? 203 TYR A CE1   1 
ATOM   1572 C CE2   . TYR A 1 210 ? 21.575  6.015   14.776  1.00 39.29  ? 203 TYR A CE2   1 
ATOM   1573 C CZ    . TYR A 1 210 ? 20.622  6.963   14.440  1.00 40.77  ? 203 TYR A CZ    1 
ATOM   1574 O OH    . TYR A 1 210 ? 20.868  7.948   13.519  1.00 52.83  ? 203 TYR A OH    1 
ATOM   1575 N N     . THR A 1 211 ? 17.650  3.046   20.242  1.00 22.51  ? 204 THR A N     1 
ATOM   1576 C CA    . THR A 1 211 ? 17.249  1.872   21.058  1.00 25.39  ? 204 THR A CA    1 
ATOM   1577 C C     . THR A 1 211 ? 15.809  2.038   21.524  1.00 23.73  ? 204 THR A C     1 
ATOM   1578 O O     . THR A 1 211 ? 15.367  3.183   21.697  1.00 24.99  ? 204 THR A O     1 
ATOM   1579 C CB    . THR A 1 211 ? 18.179  1.603   22.253  1.00 31.28  ? 204 THR A CB    1 
ATOM   1580 O OG1   . THR A 1 211 ? 18.077  2.699   23.158  1.00 36.86  ? 204 THR A OG1   1 
ATOM   1581 C CG2   . THR A 1 211 ? 19.628  1.438   21.860  1.00 32.55  ? 204 THR A CG2   1 
ATOM   1582 N N     . LYS A 1 212 ? 15.151  0.903   21.782  1.00 22.92  ? 205 LYS A N     1 
ATOM   1583 C CA    . LYS A 1 212 ? 13.728  0.854   22.179  1.00 21.90  ? 205 LYS A CA    1 
ATOM   1584 C C     . LYS A 1 212 ? 13.494  1.612   23.498  1.00 20.53  ? 205 LYS A C     1 
ATOM   1585 O O     . LYS A 1 212 ? 12.375  2.132   23.689  1.00 21.18  ? 205 LYS A O     1 
ATOM   1586 C CB    . LYS A 1 212 ? 13.304  -0.603  22.304  1.00 23.60  ? 205 LYS A CB    1 
ATOM   1587 C CG    . LYS A 1 212 ? 13.110  -1.304  20.971  1.00 23.43  ? 205 LYS A CG    1 
ATOM   1588 C CD    . LYS A 1 212 ? 13.092  -2.798  21.101  1.00 23.80  ? 205 LYS A CD    1 
ATOM   1589 C CE    . LYS A 1 212 ? 13.105  -3.419  19.710  1.00 25.93  ? 205 LYS A CE    1 
ATOM   1590 N NZ    . LYS A 1 212 ? 12.671  -4.832  19.722  1.00 26.20  ? 205 LYS A NZ    1 
ATOM   1591 N N     . SER A 1 213 ? 14.503  1.702   24.375  1.00 20.95  ? 206 SER A N     1 
ATOM   1592 C CA    . SER A 1 213 ? 14.353  2.360   25.687  1.00 22.10  ? 206 SER A CA    1 
ATOM   1593 C C     . SER A 1 213 ? 13.995  3.845   25.491  1.00 20.61  ? 206 SER A C     1 
ATOM   1594 O O     . SER A 1 213 ? 13.450  4.495   26.457  1.00 22.24  ? 206 SER A O     1 
ATOM   1595 C CB    . SER A 1 213 ? 15.602  2.182   26.520  1.00 24.62  ? 206 SER A CB    1 
ATOM   1596 O OG    . SER A 1 213 ? 16.676  2.783   25.843  1.00 27.46  ? 206 SER A OG    1 
ATOM   1597 N N     . ILE A 1 214 ? 14.265  4.444   24.336  1.00 20.63  ? 207 ILE A N     1 
ATOM   1598 C CA    . ILE A 1 214 ? 13.925  5.892   24.218  1.00 20.98  ? 207 ILE A CA    1 
ATOM   1599 C C     . ILE A 1 214 ? 12.389  6.049   24.156  1.00 20.10  ? 207 ILE A C     1 
ATOM   1600 O O     . ILE A 1 214 ? 11.888  7.079   24.620  1.00 18.20  ? 207 ILE A O     1 
ATOM   1601 C CB    . ILE A 1 214 ? 14.649  6.617   23.082  1.00 28.28  ? 207 ILE A CB    1 
ATOM   1602 C CG1   . ILE A 1 214 ? 14.265  6.084   21.713  1.00 30.69  ? 207 ILE A CG1   1 
ATOM   1603 C CG2   . ILE A 1 214 ? 16.158  6.684   23.320  1.00 30.67  ? 207 ILE A CG2   1 
ATOM   1604 C CD1   . ILE A 1 214 ? 13.456  7.073   20.963  1.00 40.09  ? 207 ILE A CD1   1 
ATOM   1605 N N     . ASP A 1 215 ? 11.673  5.068   23.608  1.00 16.58  ? 208 ASP A N     1 
ATOM   1606 C CA    . ASP A 1 215 ? 10.192  5.145   23.496  1.00 17.75  ? 208 ASP A CA    1 
ATOM   1607 C C     . ASP A 1 215 ? 9.585   4.936   24.879  1.00 17.91  ? 208 ASP A C     1 
ATOM   1608 O O     . ASP A 1 215 ? 8.566   5.550   25.190  1.00 17.32  ? 208 ASP A O     1 
ATOM   1609 C CB    . ASP A 1 215 ? 9.661   4.144   22.493  1.00 16.40  ? 208 ASP A CB    1 
ATOM   1610 C CG    . ASP A 1 215 ? 9.866   4.506   21.031  1.00 19.99  ? 208 ASP A CG    1 
ATOM   1611 O OD1   . ASP A 1 215 ? 9.925   5.706   20.728  1.00 20.79  ? 208 ASP A OD1   1 
ATOM   1612 O OD2   . ASP A 1 215 ? 9.843   3.563   20.191  1.00 21.41  ? 208 ASP A OD2   1 
ATOM   1613 N N     . ILE A 1 216 ? 10.177  4.065   25.687  1.00 19.53  ? 209 ILE A N     1 
ATOM   1614 C CA    . ILE A 1 216 ? 9.649   3.762   27.032  1.00 18.88  ? 209 ILE A CA    1 
ATOM   1615 C C     . ILE A 1 216 ? 9.757   5.002   27.921  1.00 19.31  ? 209 ILE A C     1 
ATOM   1616 O O     . ILE A 1 216 ? 8.795   5.296   28.642  1.00 16.32  ? 209 ILE A O     1 
ATOM   1617 C CB    . ILE A 1 216 ? 10.353  2.556   27.650  1.00 21.24  ? 209 ILE A CB    1 
ATOM   1618 C CG1   . ILE A 1 216 ? 10.072  1.281   26.857  1.00 21.93  ? 209 ILE A CG1   1 
ATOM   1619 C CG2   . ILE A 1 216 ? 9.977   2.479   29.102  1.00 20.06  ? 209 ILE A CG2   1 
ATOM   1620 C CD1   . ILE A 1 216 ? 8.638   0.826   26.866  1.00 25.72  ? 209 ILE A CD1   1 
ATOM   1621 N N     . TRP A 1 217 ? 10.852  5.744   27.812  1.00 18.19  ? 210 TRP A N     1 
ATOM   1622 C CA    . TRP A 1 217 ? 10.999  7.044   28.513  1.00 18.09  ? 210 TRP A CA    1 
ATOM   1623 C C     . TRP A 1 217 ? 9.815   7.940   28.132  1.00 17.33  ? 210 TRP A C     1 
ATOM   1624 O O     . TRP A 1 217 ? 9.213   8.504   29.022  1.00 16.99  ? 210 TRP A O     1 
ATOM   1625 C CB    . TRP A 1 217 ? 12.329  7.714   28.175  1.00 18.46  ? 210 TRP A CB    1 
ATOM   1626 C CG    . TRP A 1 217 ? 12.464  9.011   28.906  1.00 19.01  ? 210 TRP A CG    1 
ATOM   1627 C CD1   . TRP A 1 217 ? 12.064  10.244  28.487  1.00 19.34  ? 210 TRP A CD1   1 
ATOM   1628 C CD2   . TRP A 1 217 ? 12.977  9.176   30.229  1.00 18.79  ? 210 TRP A CD2   1 
ATOM   1629 N NE1   . TRP A 1 217 ? 12.294  11.161  29.471  1.00 19.70  ? 210 TRP A NE1   1 
ATOM   1630 C CE2   . TRP A 1 217 ? 12.854  10.542  30.548  1.00 19.33  ? 210 TRP A CE2   1 
ATOM   1631 C CE3   . TRP A 1 217 ? 13.541  8.305   31.163  1.00 17.21  ? 210 TRP A CE3   1 
ATOM   1632 C CZ2   . TRP A 1 217 ? 13.285  11.055  31.763  1.00 18.83  ? 210 TRP A CZ2   1 
ATOM   1633 C CZ3   . TRP A 1 217 ? 13.969  8.815   32.362  1.00 17.78  ? 210 TRP A CZ3   1 
ATOM   1634 C CH2   . TRP A 1 217 ? 13.835  10.177  32.652  1.00 18.78  ? 210 TRP A CH2   1 
ATOM   1635 N N     . SER A 1 218 ? 9.527   8.081   26.833  1.00 16.30  ? 211 SER A N     1 
ATOM   1636 C CA    . SER A 1 218 ? 8.478   8.995   26.352  1.00 18.24  ? 211 SER A CA    1 
ATOM   1637 C C     . SER A 1 218 ? 7.148   8.545   26.950  1.00 17.39  ? 211 SER A C     1 
ATOM   1638 O O     . SER A 1 218 ? 6.400   9.395   27.446  1.00 17.94  ? 211 SER A O     1 
ATOM   1639 C CB    . SER A 1 218 ? 8.424   9.064   24.812  1.00 18.72  ? 211 SER A CB    1 
ATOM   1640 O OG    . SER A 1 218 ? 9.663   9.503   24.280  1.00 21.92  ? 211 SER A OG    1 
ATOM   1641 N N     . VAL A 1 219 ? 6.897   7.240   26.978  1.00 15.83  ? 212 VAL A N     1 
ATOM   1642 C CA    . VAL A 1 219 ? 5.619   6.720   27.556  1.00 18.65  ? 212 VAL A CA    1 
ATOM   1643 C C     . VAL A 1 219 ? 5.548   7.097   29.045  1.00 17.52  ? 212 VAL A C     1 
ATOM   1644 O O     . VAL A 1 219 ? 4.480   7.519   29.507  1.00 17.62  ? 212 VAL A O     1 
ATOM   1645 C CB    . VAL A 1 219 ? 5.449   5.216   27.323  1.00 17.25  ? 212 VAL A CB    1 
ATOM   1646 C CG1   . VAL A 1 219 ? 4.199   4.692   27.992  1.00 19.96  ? 212 VAL A CG1   1 
ATOM   1647 C CG2   . VAL A 1 219 ? 5.423   4.915   25.826  1.00 17.94  ? 212 VAL A CG2   1 
ATOM   1648 N N     . GLY A 1 220 ? 6.654   6.954   29.777  1.00 16.10  ? 213 GLY A N     1 
ATOM   1649 C CA    . GLY A 1 220 ? 6.695   7.317   31.199  1.00 16.12  ? 213 GLY A CA    1 
ATOM   1650 C C     . GLY A 1 220 ? 6.361   8.795   31.363  1.00 17.16  ? 213 GLY A C     1 
ATOM   1651 O O     . GLY A 1 220 ? 5.562   9.155   32.312  1.00 18.53  ? 213 GLY A O     1 
ATOM   1652 N N     . CYS A 1 221 ? 6.897   9.661   30.490  1.00 17.62  ? 214 CYS A N     1 
ATOM   1653 C CA    . CYS A 1 221 ? 6.564   11.111  30.545  1.00 17.33  ? 214 CYS A CA    1 
ATOM   1654 C C     . CYS A 1 221 ? 5.033   11.296  30.319  1.00 18.69  ? 214 CYS A C     1 
ATOM   1655 O O     . CYS A 1 221 ? 4.414   12.169  30.924  1.00 19.71  ? 214 CYS A O     1 
ATOM   1656 C CB    . CYS A 1 221 ? 7.350   11.866  29.499  1.00 18.94  ? 214 CYS A CB    1 
ATOM   1657 S SG    . CYS A 1 221 ? 9.139   11.943  29.809  1.00 20.69  ? 214 CYS A SG    1 
ATOM   1658 N N     . ILE A 1 222 ? 4.456   10.577  29.376  1.00 17.95  ? 215 ILE A N     1 
ATOM   1659 C CA    . ILE A 1 222 ? 3.002   10.648  29.061  1.00 19.70  ? 215 ILE A CA    1 
ATOM   1660 C C     . ILE A 1 222 ? 2.190   10.183  30.280  1.00 19.51  ? 215 ILE A C     1 
ATOM   1661 O O     . ILE A 1 222 ? 1.173   10.867  30.606  1.00 19.76  ? 215 ILE A O     1 
ATOM   1662 C CB    . ILE A 1 222 ? 2.686   9.900   27.754  1.00 20.73  ? 215 ILE A CB    1 
ATOM   1663 C CG1   . ILE A 1 222 ? 3.383   10.568  26.564  1.00 22.62  ? 215 ILE A CG1   1 
ATOM   1664 C CG2   . ILE A 1 222 ? 1.183   9.783   27.526  1.00 20.06  ? 215 ILE A CG2   1 
ATOM   1665 C CD1   . ILE A 1 222 ? 3.492   9.683   25.359  1.00 25.19  ? 215 ILE A CD1   1 
ATOM   1666 N N     . LEU A 1 223 ? 2.586   9.089   30.924  1.00 18.97  ? 216 LEU A N     1 
ATOM   1667 C CA    . LEU A 1 223 ? 1.927   8.587   32.143  1.00 20.45  ? 216 LEU A CA    1 
ATOM   1668 C C     . LEU A 1 223 ? 1.937   9.687   33.220  1.00 22.36  ? 216 LEU A C     1 
ATOM   1669 O O     . LEU A 1 223 ? 0.845   10.019  33.806  1.00 20.56  ? 216 LEU A O     1 
ATOM   1670 C CB    . LEU A 1 223 ? 2.585   7.293   32.621  1.00 19.78  ? 216 LEU A CB    1 
ATOM   1671 C CG    . LEU A 1 223 ? 2.050   6.776   33.963  1.00 21.44  ? 216 LEU A CG    1 
ATOM   1672 C CD1   . LEU A 1 223 ? 0.520   6.664   33.905  1.00 20.11  ? 216 LEU A CD1   1 
ATOM   1673 C CD2   . LEU A 1 223 ? 2.713   5.439   34.330  1.00 20.00  ? 216 LEU A CD2   1 
ATOM   1674 N N     . ALA A 1 224 ? 3.088   10.303  33.457  1.00 20.13  ? 217 ALA A N     1 
ATOM   1675 C CA    . ALA A 1 224 ? 3.200   11.362  34.490  1.00 23.59  ? 217 ALA A CA    1 
ATOM   1676 C C     . ALA A 1 224 ? 2.236   12.511  34.146  1.00 23.32  ? 217 ALA A C     1 
ATOM   1677 O O     . ALA A 1 224 ? 1.609   13.077  35.048  1.00 25.88  ? 217 ALA A O     1 
ATOM   1678 C CB    . ALA A 1 224 ? 4.635   11.839  34.614  1.00 22.66  ? 217 ALA A CB    1 
ATOM   1679 N N     . GLU A 1 225 ? 2.092   12.814  32.862  1.00 23.07  ? 218 GLU A N     1 
ATOM   1680 C CA    . GLU A 1 225 ? 1.295   13.934  32.357  1.00 24.13  ? 218 GLU A CA    1 
ATOM   1681 C C     . GLU A 1 225 ? -0.197  13.594  32.495  1.00 26.60  ? 218 GLU A C     1 
ATOM   1682 O O     . GLU A 1 225 ? -0.968  14.500  32.834  1.00 23.64  ? 218 GLU A O     1 
ATOM   1683 C CB    . GLU A 1 225 ? 1.759   14.211  30.952  1.00 26.98  ? 218 GLU A CB    1 
ATOM   1684 C CG    . GLU A 1 225 ? 1.019   15.309  30.289  1.00 28.55  ? 218 GLU A CG    1 
ATOM   1685 C CD    . GLU A 1 225 ? 1.818   16.053  29.238  1.00 27.11  ? 218 GLU A CD    1 
ATOM   1686 O OE1   . GLU A 1 225 ? 2.920   15.616  28.878  1.00 24.85  ? 218 GLU A OE1   1 
ATOM   1687 O OE2   . GLU A 1 225 ? 1.291   17.037  28.770  1.00 27.33  ? 218 GLU A OE2   1 
ATOM   1688 N N     . MET A 1 226 ? -0.562  12.317  32.366  1.00 24.25  ? 219 MET A N     1 
ATOM   1689 C CA    . MET A 1 226 ? -1.967  11.853  32.560  1.00 24.76  ? 219 MET A CA    1 
ATOM   1690 C C     . MET A 1 226 ? -2.332  11.975  34.049  1.00 24.85  ? 219 MET A C     1 
ATOM   1691 O O     . MET A 1 226 ? -3.478  12.370  34.329  1.00 29.19  ? 219 MET A O     1 
ATOM   1692 C CB    . MET A 1 226 ? -2.156  10.430  32.034  1.00 26.19  ? 219 MET A CB    1 
ATOM   1693 C CG    . MET A 1 226 ? -2.293  10.367  30.522  1.00 23.96  ? 219 MET A CG    1 
ATOM   1694 S SD    . MET A 1 226 ? -2.812  8.764   29.932  1.00 25.95  ? 219 MET A SD    1 
ATOM   1695 C CE    . MET A 1 226 ? -1.419  7.724   30.392  1.00 24.99  ? 219 MET A CE    1 
ATOM   1696 N N     . LEU A 1 227 ? -1.402  11.754  34.975  1.00 23.40  ? 220 LEU A N     1 
ATOM   1697 C CA    . LEU A 1 227 ? -1.656  11.866  36.438  1.00 28.40  ? 220 LEU A CA    1 
ATOM   1698 C C     . LEU A 1 227 ? -1.850  13.324  36.931  1.00 32.00  ? 220 LEU A C     1 
ATOM   1699 O O     . LEU A 1 227 ? -2.400  13.484  38.015  1.00 35.14  ? 220 LEU A O     1 
ATOM   1700 C CB    . LEU A 1 227 ? -0.511  11.232  37.209  1.00 28.14  ? 220 LEU A CB    1 
ATOM   1701 C CG    . LEU A 1 227 ? -0.271  9.748   36.951  1.00 28.41  ? 220 LEU A CG    1 
ATOM   1702 C CD1   . LEU A 1 227 ? 1.068   9.353   37.536  1.00 30.82  ? 220 LEU A CD1   1 
ATOM   1703 C CD2   . LEU A 1 227 ? -1.383  8.906   37.532  1.00 29.35  ? 220 LEU A CD2   1 
ATOM   1704 N N     . SER A 1 228 ? -1.361  14.341  36.231  1.00 29.70  ? 221 SER A N     1 
ATOM   1705 C CA    . SER A 1 228 ? -1.313  15.738  36.739  1.00 33.78  ? 221 SER A CA    1 
ATOM   1706 C C     . SER A 1 228 ? -1.952  16.729  35.761  1.00 30.85  ? 221 SER A C     1 
ATOM   1707 O O     . SER A 1 228 ? -2.154  17.889  36.167  1.00 29.67  ? 221 SER A O     1 
ATOM   1708 C CB    . SER A 1 228 ? 0.130   16.132  36.978  1.00 34.60  ? 221 SER A CB    1 
ATOM   1709 O OG    . SER A 1 228 ? 0.817   16.094  35.728  1.00 30.83  ? 221 SER A OG    1 
ATOM   1710 N N     . ASN A 1 229 ? -2.146  16.338  34.502  1.00 26.96  ? 222 ASN A N     1 
ATOM   1711 C CA    . ASN A 1 229 ? -2.496  17.229  33.363  1.00 28.37  ? 222 ASN A CA    1 
ATOM   1712 C C     . ASN A 1 229 ? -1.410  18.279  33.141  1.00 33.03  ? 222 ASN A C     1 
ATOM   1713 O O     . ASN A 1 229 ? -1.735  19.345  32.648  1.00 33.66  ? 222 ASN A O     1 
ATOM   1714 C CB    . ASN A 1 229 ? -3.816  17.988  33.582  1.00 27.97  ? 222 ASN A CB    1 
ATOM   1715 C CG    . ASN A 1 229 ? -4.986  17.038  33.609  1.00 27.68  ? 222 ASN A CG    1 
ATOM   1716 O OD1   . ASN A 1 229 ? -5.205  16.375  34.618  1.00 29.48  ? 222 ASN A OD1   1 
ATOM   1717 N ND2   . ASN A 1 229 ? -5.679  16.924  32.491  1.00 25.19  ? 222 ASN A ND2   1 
ATOM   1718 N N     . ARG A 1 230 ? -0.155  18.032  33.492  1.00 31.52  ? 223 ARG A N     1 
ATOM   1719 C CA    . ARG A 1 230 ? 0.901   18.933  32.974  1.00 35.59  ? 223 ARG A CA    1 
ATOM   1720 C C     . ARG A 1 230 ? 2.170   18.136  32.695  1.00 31.35  ? 223 ARG A C     1 
ATOM   1721 O O     . ARG A 1 230 ? 2.388   17.108  33.326  1.00 27.50  ? 223 ARG A O     1 
ATOM   1722 C CB    . ARG A 1 230 ? 1.134   20.082  33.956  1.00 41.39  ? 223 ARG A CB    1 
ATOM   1723 C CG    . ARG A 1 230 ? 1.656   19.664  35.319  1.00 45.25  ? 223 ARG A CG    1 
ATOM   1724 C CD    . ARG A 1 230 ? 2.408   20.835  35.941  1.00 55.92  ? 223 ARG A CD    1 
ATOM   1725 N NE    . ARG A 1 230 ? 3.816   20.541  36.242  1.00 64.35  ? 223 ARG A NE    1 
ATOM   1726 C CZ    . ARG A 1 230 ? 4.870   20.726  35.425  1.00 64.77  ? 223 ARG A CZ    1 
ATOM   1727 N NH1   . ARG A 1 230 ? 4.724   21.190  34.189  1.00 49.08  ? 223 ARG A NH1   1 
ATOM   1728 N NH2   . ARG A 1 230 ? 6.085   20.418  35.860  1.00 68.35  ? 223 ARG A NH2   1 
ATOM   1729 N N     . PRO A 1 231 ? 3.034   18.623  31.784  1.00 27.73  ? 224 PRO A N     1 
ATOM   1730 C CA    . PRO A 1 231 ? 4.281   17.926  31.460  1.00 27.10  ? 224 PRO A CA    1 
ATOM   1731 C C     . PRO A 1 231 ? 5.185   17.800  32.700  1.00 25.72  ? 224 PRO A C     1 
ATOM   1732 O O     . PRO A 1 231 ? 5.362   18.740  33.464  1.00 23.95  ? 224 PRO A O     1 
ATOM   1733 C CB    . PRO A 1 231 ? 4.890   18.781  30.340  1.00 29.20  ? 224 PRO A CB    1 
ATOM   1734 C CG    . PRO A 1 231 ? 4.259   20.157  30.496  1.00 31.62  ? 224 PRO A CG    1 
ATOM   1735 C CD    . PRO A 1 231 ? 2.866   19.869  31.017  1.00 30.46  ? 224 PRO A CD    1 
ATOM   1736 N N     . ILE A 1 232 ? 5.778   16.635  32.910  1.00 23.03  ? 225 ILE A N     1 
ATOM   1737 C CA    . ILE A 1 232 ? 6.604   16.404  34.123  1.00 22.61  ? 225 ILE A CA    1 
ATOM   1738 C C     . ILE A 1 232 ? 7.995   17.055  33.976  1.00 19.67  ? 225 ILE A C     1 
ATOM   1739 O O     . ILE A 1 232 ? 8.490   17.542  34.976  1.00 24.04  ? 225 ILE A O     1 
ATOM   1740 C CB    . ILE A 1 232 ? 6.681   14.896  34.468  1.00 25.48  ? 225 ILE A CB    1 
ATOM   1741 C CG1   . ILE A 1 232 ? 7.330   14.733  35.845  1.00 28.70  ? 225 ILE A CG1   1 
ATOM   1742 C CG2   . ILE A 1 232 ? 7.326   14.078  33.348  1.00 21.81  ? 225 ILE A CG2   1 
ATOM   1743 C CD1   . ILE A 1 232 ? 7.763   13.351  36.168  1.00 35.08  ? 225 ILE A CD1   1 
ATOM   1744 N N     . PHE A 1 233 ? 8.550   17.156  32.778  1.00 20.06  ? 226 PHE A N     1 
ATOM   1745 C CA    . PHE A 1 233 ? 9.903   17.721  32.519  1.00 21.58  ? 226 PHE A CA    1 
ATOM   1746 C C     . PHE A 1 233 ? 9.840   18.799  31.432  1.00 21.17  ? 226 PHE A C     1 
ATOM   1747 O O     . PHE A 1 233 ? 10.263  18.569  30.290  1.00 20.84  ? 226 PHE A O     1 
ATOM   1748 C CB    . PHE A 1 233 ? 10.855  16.607  32.094  1.00 20.00  ? 226 PHE A CB    1 
ATOM   1749 C CG    . PHE A 1 233 ? 10.905  15.430  33.030  1.00 21.22  ? 226 PHE A CG    1 
ATOM   1750 C CD1   . PHE A 1 233 ? 11.199  15.592  34.379  1.00 20.02  ? 226 PHE A CD1   1 
ATOM   1751 C CD2   . PHE A 1 233 ? 10.708  14.135  32.544  1.00 20.66  ? 226 PHE A CD2   1 
ATOM   1752 C CE1   . PHE A 1 233 ? 11.301  14.484  35.214  1.00 21.91  ? 226 PHE A CE1   1 
ATOM   1753 C CE2   . PHE A 1 233 ? 10.817  13.033  33.384  1.00 17.66  ? 226 PHE A CE2   1 
ATOM   1754 C CZ    . PHE A 1 233 ? 11.138  13.212  34.708  1.00 18.86  ? 226 PHE A CZ    1 
ATOM   1755 N N     . PRO A 1 234 ? 9.212   19.966  31.717  1.00 23.59  ? 227 PRO A N     1 
ATOM   1756 C CA    . PRO A 1 234 ? 9.008   21.006  30.707  1.00 27.36  ? 227 PRO A CA    1 
ATOM   1757 C C     . PRO A 1 234 ? 10.232  21.922  30.556  1.00 28.70  ? 227 PRO A C     1 
ATOM   1758 O O     . PRO A 1 234 ? 10.152  23.075  30.980  1.00 30.57  ? 227 PRO A O     1 
ATOM   1759 C CB    . PRO A 1 234 ? 7.835   21.802  31.298  1.00 25.80  ? 227 PRO A CB    1 
ATOM   1760 C CG    . PRO A 1 234 ? 8.070   21.727  32.754  1.00 25.33  ? 227 PRO A CG    1 
ATOM   1761 C CD    . PRO A 1 234 ? 8.549   20.310  32.983  1.00 26.73  ? 227 PRO A CD    1 
ATOM   1762 N N     . GLY A 1 235 ? 11.349  21.369  30.085  1.00 28.94  ? 228 GLY A N     1 
ATOM   1763 C CA    . GLY A 1 235 ? 12.610  22.102  29.854  1.00 31.90  ? 228 GLY A CA    1 
ATOM   1764 C C     . GLY A 1 235 ? 12.447  23.210  28.821  1.00 36.68  ? 228 GLY A C     1 
ATOM   1765 O O     . GLY A 1 235 ? 11.704  23.013  27.835  1.00 31.84  ? 228 GLY A O     1 
ATOM   1766 N N     . LYS A 1 236 ? 13.121  24.354  28.996  1.00 36.16  ? 229 LYS A N     1 
ATOM   1767 C CA    . LYS A 1 236 ? 12.933  25.498  28.052  1.00 41.59  ? 229 LYS A CA    1 
ATOM   1768 C C     . LYS A 1 236 ? 13.952  25.409  26.918  1.00 42.67  ? 229 LYS A C     1 
ATOM   1769 O O     . LYS A 1 236 ? 13.803  26.139  25.942  1.00 54.28  ? 229 LYS A O     1 
ATOM   1770 C CB    . LYS A 1 236 ? 12.981  26.825  28.813  1.00 43.53  ? 229 LYS A CB    1 
ATOM   1771 C CG    . LYS A 1 236 ? 11.953  26.933  29.934  1.00 49.04  ? 229 LYS A CG    1 
ATOM   1772 C CD    . LYS A 1 236 ? 11.929  28.293  30.594  1.00 54.89  ? 229 LYS A CD    1 
ATOM   1773 C CE    . LYS A 1 236 ? 11.329  28.278  31.982  1.00 60.73  ? 229 LYS A CE    1 
ATOM   1774 N NZ    . LYS A 1 236 ? 12.381  28.201  33.025  1.00 64.33  ? 229 LYS A NZ    1 
ATOM   1775 N N     . HIS A 1 237 ? 14.956  24.549  27.030  1.00 40.02  ? 230 HIS A N     1 
ATOM   1776 C CA    . HIS A 1 237 ? 15.978  24.360  25.978  1.00 42.90  ? 230 HIS A CA    1 
ATOM   1777 C C     . HIS A 1 237 ? 16.706  23.041  26.203  1.00 51.97  ? 230 HIS A C     1 
ATOM   1778 O O     . HIS A 1 237 ? 16.648  22.491  27.332  1.00 47.05  ? 230 HIS A O     1 
ATOM   1779 C CB    . HIS A 1 237 ? 16.990  25.530  25.933  1.00 42.27  ? 230 HIS A CB    1 
ATOM   1780 C CG    . HIS A 1 237 ? 17.345  26.118  27.255  1.00 34.26  ? 230 HIS A CG    1 
ATOM   1781 N ND1   . HIS A 1 237 ? 18.392  25.664  28.013  1.00 34.73  ? 230 HIS A ND1   1 
ATOM   1782 C CD2   . HIS A 1 237 ? 16.818  27.176  27.923  1.00 36.84  ? 230 HIS A CD2   1 
ATOM   1783 C CE1   . HIS A 1 237 ? 18.462  26.345  29.137  1.00 36.41  ? 230 HIS A CE1   1 
ATOM   1784 N NE2   . HIS A 1 237 ? 17.525  27.315  29.096  1.00 35.85  ? 230 HIS A NE2   1 
ATOM   1785 N N     . TYR A 1 238 ? 17.403  22.603  25.157  1.00 50.62  ? 231 TYR A N     1 
ATOM   1786 C CA    . TYR A 1 238 ? 18.185  21.351  25.113  1.00 50.93  ? 231 TYR A CA    1 
ATOM   1787 C C     . TYR A 1 238 ? 18.717  20.992  26.511  1.00 45.30  ? 231 TYR A C     1 
ATOM   1788 O O     . TYR A 1 238 ? 18.350  19.930  27.009  1.00 51.21  ? 231 TYR A O     1 
ATOM   1789 C CB    . TYR A 1 238 ? 19.258  21.491  24.034  1.00 49.46  ? 231 TYR A CB    1 
ATOM   1790 C CG    . TYR A 1 238 ? 19.949  20.200  23.717  1.00 47.00  ? 231 TYR A CG    1 
ATOM   1791 C CD1   . TYR A 1 238 ? 20.983  19.742  24.513  1.00 48.66  ? 231 TYR A CD1   1 
ATOM   1792 C CD2   . TYR A 1 238 ? 19.528  19.409  22.665  1.00 47.75  ? 231 TYR A CD2   1 
ATOM   1793 C CE1   . TYR A 1 238 ? 21.615  18.541  24.245  1.00 50.26  ? 231 TYR A CE1   1 
ATOM   1794 C CE2   . TYR A 1 238 ? 20.164  18.214  22.374  1.00 43.26  ? 231 TYR A CE2   1 
ATOM   1795 C CZ    . TYR A 1 238 ? 21.220  17.786  23.156  1.00 42.37  ? 231 TYR A CZ    1 
ATOM   1796 O OH    . TYR A 1 238 ? 21.847  16.604  22.896  1.00 44.67  ? 231 TYR A OH    1 
ATOM   1797 N N     . LEU A 1 239 ? 19.559  21.814  27.152  1.00 53.48  ? 232 LEU A N     1 
ATOM   1798 C CA    . LEU A 1 239 ? 20.256  21.402  28.412  1.00 46.92  ? 232 LEU A CA    1 
ATOM   1799 C C     . LEU A 1 239 ? 19.401  21.670  29.649  1.00 46.81  ? 232 LEU A C     1 
ATOM   1800 O O     . LEU A 1 239 ? 19.640  20.963  30.679  1.00 47.12  ? 232 LEU A O     1 
ATOM   1801 C CB    . LEU A 1 239 ? 21.613  22.101  28.536  1.00 51.90  ? 232 LEU A CB    1 
ATOM   1802 C CG    . LEU A 1 239 ? 22.535  21.611  29.653  1.00 47.14  ? 232 LEU A CG    1 
ATOM   1803 C CD1   . LEU A 1 239 ? 22.900  20.169  29.464  1.00 46.21  ? 232 LEU A CD1   1 
ATOM   1804 C CD2   . LEU A 1 239 ? 23.815  22.436  29.694  1.00 48.68  ? 232 LEU A CD2   1 
ATOM   1805 N N     . ASP A 1 240 ? 18.433  22.599  29.584  1.00 40.91  ? 233 ASP A N     1 
ATOM   1806 C CA    . ASP A 1 240 ? 17.453  22.774  30.701  1.00 35.54  ? 233 ASP A CA    1 
ATOM   1807 C C     . ASP A 1 240 ? 16.677  21.463  30.874  1.00 30.44  ? 233 ASP A C     1 
ATOM   1808 O O     . ASP A 1 240 ? 16.198  21.215  31.959  1.00 30.90  ? 233 ASP A O     1 
ATOM   1809 C CB    . ASP A 1 240 ? 16.423  23.873  30.435  1.00 31.38  ? 233 ASP A CB    1 
ATOM   1810 C CG    . ASP A 1 240 ? 15.616  24.286  31.654  1.00 34.85  ? 233 ASP A CG    1 
ATOM   1811 O OD1   . ASP A 1 240 ? 16.182  24.327  32.738  1.00 32.64  ? 233 ASP A OD1   1 
ATOM   1812 O OD2   . ASP A 1 240 ? 14.380  24.531  31.504  1.00 36.20  ? 233 ASP A OD2   1 
ATOM   1813 N N     . GLN A 1 241 ? 16.525  20.697  29.799  1.00 26.61  ? 234 GLN A N     1 
ATOM   1814 C CA    . GLN A 1 241 ? 15.762  19.425  29.822  1.00 30.20  ? 234 GLN A CA    1 
ATOM   1815 C C     . GLN A 1 241 ? 16.395  18.500  30.859  1.00 28.45  ? 234 GLN A C     1 
ATOM   1816 O O     . GLN A 1 241 ? 15.660  17.993  31.731  1.00 27.03  ? 234 GLN A O     1 
ATOM   1817 C CB    . GLN A 1 241 ? 15.714  18.750  28.452  1.00 26.45  ? 234 GLN A CB    1 
ATOM   1818 C CG    . GLN A 1 241 ? 14.690  17.607  28.384  1.00 25.10  ? 234 GLN A CG    1 
ATOM   1819 C CD    . GLN A 1 241 ? 13.316  18.027  28.862  1.00 25.37  ? 234 GLN A CD    1 
ATOM   1820 O OE1   . GLN A 1 241 ? 12.891  19.128  28.558  1.00 23.23  ? 234 GLN A OE1   1 
ATOM   1821 N NE2   . GLN A 1 241 ? 12.594  17.151  29.568  1.00 21.58  ? 234 GLN A NE2   1 
ATOM   1822 N N     . LEU A 1 242 ? 17.729  18.408  30.877  1.00 29.24  ? 235 LEU A N     1 
ATOM   1823 C CA    . LEU A 1 242 ? 18.476  17.570  31.868  1.00 31.05  ? 235 LEU A CA    1 
ATOM   1824 C C     . LEU A 1 242 ? 18.347  18.129  33.299  1.00 31.59  ? 235 LEU A C     1 
ATOM   1825 O O     . LEU A 1 242 ? 18.133  17.327  34.242  1.00 30.57  ? 235 LEU A O     1 
ATOM   1826 C CB    . LEU A 1 242 ? 19.930  17.466  31.380  1.00 32.97  ? 235 LEU A CB    1 
ATOM   1827 C CG    . LEU A 1 242 ? 20.708  16.215  31.779  1.00 36.30  ? 235 LEU A CG    1 
ATOM   1828 C CD1   . LEU A 1 242 ? 20.024  14.934  31.289  1.00 32.88  ? 235 LEU A CD1   1 
ATOM   1829 C CD2   . LEU A 1 242 ? 22.131  16.298  31.226  1.00 35.75  ? 235 LEU A CD2   1 
ATOM   1830 N N     . ASN A 1 243 ? 18.467  19.443  33.490  1.00 31.03  ? 236 ASN A N     1 
ATOM   1831 C CA    . ASN A 1 243 ? 18.165  20.119  34.776  1.00 33.71  ? 236 ASN A CA    1 
ATOM   1832 C C     . ASN A 1 243 ? 16.859  19.506  35.305  1.00 31.61  ? 236 ASN A C     1 
ATOM   1833 O O     . ASN A 1 243 ? 16.792  19.116  36.488  1.00 29.26  ? 236 ASN A O     1 
ATOM   1834 C CB    . ASN A 1 243 ? 17.986  21.648  34.636  1.00 38.89  ? 236 ASN A CB    1 
ATOM   1835 C CG    . ASN A 1 243 ? 19.199  22.471  34.197  1.00 50.57  ? 236 ASN A CG    1 
ATOM   1836 O OD1   . ASN A 1 243 ? 19.066  23.607  33.688  1.00 44.96  ? 236 ASN A OD1   1 
ATOM   1837 N ND2   . ASN A 1 243 ? 20.397  21.937  34.395  1.00 51.36  ? 236 ASN A ND2   1 
ATOM   1838 N N     . HIS A 1 244 ? 15.812  19.483  34.463  1.00 29.97  ? 237 HIS A N     1 
ATOM   1839 C CA    . HIS A 1 244 ? 14.443  19.098  34.886  1.00 29.85  ? 237 HIS A CA    1 
ATOM   1840 C C     . HIS A 1 244 ? 14.460  17.634  35.324  1.00 24.39  ? 237 HIS A C     1 
ATOM   1841 O O     . HIS A 1 244 ? 13.920  17.313  36.388  1.00 25.04  ? 237 HIS A O     1 
ATOM   1842 C CB    . HIS A 1 244 ? 13.403  19.405  33.793  1.00 31.62  ? 237 HIS A CB    1 
ATOM   1843 C CG    . HIS A 1 244 ? 12.799  20.764  33.916  1.00 36.84  ? 237 HIS A CG    1 
ATOM   1844 N ND1   . HIS A 1 244 ? 13.417  21.913  33.423  1.00 44.06  ? 237 HIS A ND1   1 
ATOM   1845 C CD2   . HIS A 1 244 ? 11.643  21.174  34.474  1.00 38.45  ? 237 HIS A CD2   1 
ATOM   1846 C CE1   . HIS A 1 244 ? 12.656  22.963  33.684  1.00 38.86  ? 237 HIS A CE1   1 
ATOM   1847 N NE2   . HIS A 1 244 ? 11.568  22.535  34.316  1.00 45.23  ? 237 HIS A NE2   1 
ATOM   1848 N N     . ILE A 1 245 ? 14.978  16.761  34.479  1.00 22.70  ? 238 ILE A N     1 
ATOM   1849 C CA    . ILE A 1 245 ? 14.941  15.300  34.752  1.00 22.70  ? 238 ILE A CA    1 
ATOM   1850 C C     . ILE A 1 245 ? 15.691  15.038  36.063  1.00 23.78  ? 238 ILE A C     1 
ATOM   1851 O O     . ILE A 1 245 ? 15.185  14.344  36.945  1.00 23.77  ? 238 ILE A O     1 
ATOM   1852 C CB    . ILE A 1 245 ? 15.493  14.539  33.532  1.00 21.92  ? 238 ILE A CB    1 
ATOM   1853 C CG1   . ILE A 1 245 ? 14.606  14.750  32.294  1.00 21.92  ? 238 ILE A CG1   1 
ATOM   1854 C CG2   . ILE A 1 245 ? 15.700  13.088  33.877  1.00 23.40  ? 238 ILE A CG2   1 
ATOM   1855 C CD1   . ILE A 1 245 ? 15.237  14.320  30.987  1.00 23.68  ? 238 ILE A CD1   1 
ATOM   1856 N N     . LEU A 1 246 ? 16.900  15.588  36.207  1.00 25.89  ? 239 LEU A N     1 
ATOM   1857 C CA    . LEU A 1 246 ? 17.761  15.297  37.380  1.00 28.00  ? 239 LEU A CA    1 
ATOM   1858 C C     . LEU A 1 246 ? 17.191  15.961  38.634  1.00 28.62  ? 239 LEU A C     1 
ATOM   1859 O O     . LEU A 1 246 ? 17.431  15.425  39.683  1.00 28.52  ? 239 LEU A O     1 
ATOM   1860 C CB    . LEU A 1 246 ? 19.189  15.777  37.074  1.00 30.09  ? 239 LEU A CB    1 
ATOM   1861 C CG    . LEU A 1 246 ? 19.808  15.110  35.847  1.00 31.70  ? 239 LEU A CG    1 
ATOM   1862 C CD1   . LEU A 1 246 ? 21.145  15.721  35.499  1.00 34.98  ? 239 LEU A CD1   1 
ATOM   1863 C CD2   . LEU A 1 246 ? 19.947  13.617  36.061  1.00 33.74  ? 239 LEU A CD2   1 
ATOM   1864 N N     . GLY A 1 247 ? 16.485  17.089  38.527  1.00 29.17  ? 240 GLY A N     1 
ATOM   1865 C CA    . GLY A 1 247 ? 15.810  17.701  39.687  1.00 31.64  ? 240 GLY A CA    1 
ATOM   1866 C C     . GLY A 1 247 ? 14.819  16.728  40.318  1.00 35.49  ? 240 GLY A C     1 
ATOM   1867 O O     . GLY A 1 247 ? 14.550  16.833  41.524  1.00 33.14  ? 240 GLY A O     1 
ATOM   1868 N N     . ILE A 1 248 ? 14.254  15.794  39.545  1.00 29.77  ? 241 ILE A N     1 
ATOM   1869 C CA    . ILE A 1 248 ? 13.261  14.845  40.111  1.00 29.13  ? 241 ILE A CA    1 
ATOM   1870 C C     . ILE A 1 248 ? 13.926  13.504  40.421  1.00 27.66  ? 241 ILE A C     1 
ATOM   1871 O O     . ILE A 1 248 ? 13.708  12.995  41.537  1.00 31.37  ? 241 ILE A O     1 
ATOM   1872 C CB    . ILE A 1 248 ? 12.024  14.747  39.204  1.00 31.55  ? 241 ILE A CB    1 
ATOM   1873 C CG1   . ILE A 1 248 ? 11.162  16.005  39.367  1.00 34.03  ? 241 ILE A CG1   1 
ATOM   1874 C CG2   . ILE A 1 248 ? 11.245  13.482  39.501  1.00 32.25  ? 241 ILE A CG2   1 
ATOM   1875 C CD1   . ILE A 1 248 ? 10.215  16.246  38.227  1.00 36.97  ? 241 ILE A CD1   1 
ATOM   1876 N N     . LEU A 1 249 ? 14.696  12.941  39.484  1.00 25.63  ? 242 LEU A N     1 
ATOM   1877 C CA    . LEU A 1 249 ? 15.319  11.613  39.681  1.00 28.92  ? 242 LEU A CA    1 
ATOM   1878 C C     . LEU A 1 249 ? 16.447  11.747  40.705  1.00 27.37  ? 242 LEU A C     1 
ATOM   1879 O O     . LEU A 1 249 ? 16.800  10.735  41.238  1.00 29.53  ? 242 LEU A O     1 
ATOM   1880 C CB    . LEU A 1 249 ? 15.906  11.076  38.370  1.00 25.85  ? 242 LEU A CB    1 
ATOM   1881 C CG    . LEU A 1 249 ? 14.892  10.767  37.276  1.00 25.46  ? 242 LEU A CG    1 
ATOM   1882 C CD1   . LEU A 1 249 ? 15.484  9.813   36.245  1.00 27.73  ? 242 LEU A CD1   1 
ATOM   1883 C CD2   . LEU A 1 249 ? 13.603  10.249  37.835  1.00 28.14  ? 242 LEU A CD2   1 
ATOM   1884 N N     . GLY A 1 250 ? 17.042  12.937  40.829  1.00 30.02  ? 243 GLY A N     1 
ATOM   1885 C CA    . GLY A 1 250 ? 18.223  13.153  41.682  1.00 28.43  ? 243 GLY A CA    1 
ATOM   1886 C C     . GLY A 1 250 ? 19.500  12.770  40.960  1.00 28.39  ? 243 GLY A C     1 
ATOM   1887 O O     . GLY A 1 250 ? 19.461  12.335  39.780  1.00 28.85  ? 243 GLY A O     1 
ATOM   1888 N N     . SER A 1 251 ? 20.619  12.915  41.644  1.00 24.67  ? 244 SER A N     1 
ATOM   1889 C CA    . SER A 1 251 ? 21.960  12.701  41.062  1.00 25.41  ? 244 SER A CA    1 
ATOM   1890 C C     . SER A 1 251 ? 22.059  11.241  40.660  1.00 26.33  ? 244 SER A C     1 
ATOM   1891 O O     . SER A 1 251 ? 21.644  10.376  41.407  1.00 25.78  ? 244 SER A O     1 
ATOM   1892 C CB    . SER A 1 251 ? 23.049  13.103  42.021  1.00 23.65  ? 244 SER A CB    1 
ATOM   1893 O OG    . SER A 1 251 ? 22.843  14.431  42.428  1.00 22.86  ? 244 SER A OG    1 
ATOM   1894 N N     . PRO A 1 252 ? 22.519  10.930  39.436  1.00 26.54  ? 245 PRO A N     1 
ATOM   1895 C CA    . PRO A 1 252 ? 22.756  9.537   39.072  1.00 26.99  ? 245 PRO A CA    1 
ATOM   1896 C C     . PRO A 1 252 ? 23.816  8.881   39.975  1.00 28.98  ? 245 PRO A C     1 
ATOM   1897 O O     . PRO A 1 252 ? 24.816  9.511   40.399  1.00 22.81  ? 245 PRO A O     1 
ATOM   1898 C CB    . PRO A 1 252 ? 23.201  9.571   37.605  1.00 29.22  ? 245 PRO A CB    1 
ATOM   1899 C CG    . PRO A 1 252 ? 23.260  11.031  37.201  1.00 29.59  ? 245 PRO A CG    1 
ATOM   1900 C CD    . PRO A 1 252 ? 22.685  11.871  38.320  1.00 27.88  ? 245 PRO A CD    1 
ATOM   1901 N N     . SER A 1 253 ? 23.553  7.609   40.252  1.00 28.93  ? 246 SER A N     1 
ATOM   1902 C CA    . SER A 1 253 ? 24.395  6.705   41.060  1.00 28.38  ? 246 SER A CA    1 
ATOM   1903 C C     . SER A 1 253 ? 25.754  6.536   40.388  1.00 30.31  ? 246 SER A C     1 
ATOM   1904 O O     . SER A 1 253 ? 25.911  6.755   39.128  1.00 26.82  ? 246 SER A O     1 
ATOM   1905 C CB    . SER A 1 253 ? 23.708  5.380   41.276  1.00 32.03  ? 246 SER A CB    1 
ATOM   1906 O OG    . SER A 1 253 ? 23.748  4.592   40.102  1.00 31.41  ? 246 SER A OG    1 
ATOM   1907 N N     . GLN A 1 254 ? 26.731  6.135   41.189  1.00 30.25  ? 247 GLN A N     1 
ATOM   1908 C CA    . GLN A 1 254 ? 28.078  5.816   40.677  1.00 33.11  ? 247 GLN A CA    1 
ATOM   1909 C C     . GLN A 1 254 ? 27.933  4.753   39.587  1.00 31.32  ? 247 GLN A C     1 
ATOM   1910 O O     . GLN A 1 254 ? 28.504  4.943   38.490  1.00 35.48  ? 247 GLN A O     1 
ATOM   1911 C CB    . GLN A 1 254 ? 28.978  5.360   41.826  1.00 36.96  ? 247 GLN A CB    1 
ATOM   1912 C CG    . GLN A 1 254 ? 30.399  5.073   41.387  1.00 41.62  ? 247 GLN A CG    1 
ATOM   1913 C CD    . GLN A 1 254 ? 31.236  4.753   42.595  1.00 42.99  ? 247 GLN A CD    1 
ATOM   1914 O OE1   . GLN A 1 254 ? 30.843  3.961   43.453  1.00 46.83  ? 247 GLN A OE1   1 
ATOM   1915 N NE2   . GLN A 1 254 ? 32.369  5.417   42.684  1.00 46.31  ? 247 GLN A NE2   1 
ATOM   1916 N N     . GLU A 1 255 ? 27.127  3.714   39.829  1.00 30.48  ? 248 GLU A N     1 
ATOM   1917 C CA    . GLU A 1 255 ? 26.936  2.634   38.827  1.00 35.85  ? 248 GLU A CA    1 
ATOM   1918 C C     . GLU A 1 255 ? 26.443  3.253   37.512  1.00 38.44  ? 248 GLU A C     1 
ATOM   1919 O O     . GLU A 1 255 ? 27.046  2.946   36.481  1.00 41.69  ? 248 GLU A O     1 
ATOM   1920 C CB    . GLU A 1 255 ? 25.950  1.553   39.279  1.00 40.67  ? 248 GLU A CB    1 
ATOM   1921 C CG    . GLU A 1 255 ? 25.631  0.573   38.162  1.00 46.54  ? 248 GLU A CG    1 
ATOM   1922 C CD    . GLU A 1 255 ? 24.817  -0.638  38.579  1.00 53.03  ? 248 GLU A CD    1 
ATOM   1923 O OE1   . GLU A 1 255 ? 25.031  -1.709  37.988  1.00 60.29  ? 248 GLU A OE1   1 
ATOM   1924 O OE2   . GLU A 1 255 ? 23.960  -0.498  39.475  1.00 56.68  ? 248 GLU A OE2   1 
ATOM   1925 N N     . ASP A 1 256 ? 25.397  4.086   37.547  1.00 32.90  ? 249 ASP A N     1 
ATOM   1926 C CA    . ASP A 1 256 ? 24.817  4.692   36.318  1.00 34.67  ? 249 ASP A CA    1 
ATOM   1927 C C     . ASP A 1 256 ? 25.839  5.620   35.630  1.00 31.92  ? 249 ASP A C     1 
ATOM   1928 O O     . ASP A 1 256 ? 25.891  5.658   34.371  1.00 31.45  ? 249 ASP A O     1 
ATOM   1929 C CB    . ASP A 1 256 ? 23.477  5.340   36.653  1.00 36.20  ? 249 ASP A CB    1 
ATOM   1930 C CG    . ASP A 1 256 ? 22.392  4.316   36.990  1.00 39.63  ? 249 ASP A CG    1 
ATOM   1931 O OD1   . ASP A 1 256 ? 22.626  3.067   36.815  1.00 37.90  ? 249 ASP A OD1   1 
ATOM   1932 O OD2   . ASP A 1 256 ? 21.326  4.758   37.417  1.00 38.95  ? 249 ASP A OD2   1 
ATOM   1933 N N     . LEU A 1 257 ? 26.647  6.354   36.379  1.00 29.95  ? 250 LEU A N     1 
ATOM   1934 C CA    . LEU A 1 257 ? 27.730  7.183   35.771  1.00 34.87  ? 250 LEU A CA    1 
ATOM   1935 C C     . LEU A 1 257 ? 28.780  6.288   35.116  1.00 41.31  ? 250 LEU A C     1 
ATOM   1936 O O     . LEU A 1 257 ? 29.265  6.669   34.034  1.00 42.96  ? 250 LEU A O     1 
ATOM   1937 C CB    . LEU A 1 257 ? 28.392  8.066   36.821  1.00 37.60  ? 250 LEU A CB    1 
ATOM   1938 C CG    . LEU A 1 257 ? 27.714  9.406   37.032  1.00 42.44  ? 250 LEU A CG    1 
ATOM   1939 C CD1   . LEU A 1 257 ? 28.398  10.150  38.155  1.00 48.88  ? 250 LEU A CD1   1 
ATOM   1940 C CD2   . LEU A 1 257 ? 27.742  10.234  35.766  1.00 44.82  ? 250 LEU A CD2   1 
ATOM   1941 N N     . ASN A 1 258 ? 29.087  5.134   35.715  1.00 45.60  ? 251 ASN A N     1 
ATOM   1942 C CA    . ASN A 1 258 ? 30.131  4.213   35.186  1.00 50.82  ? 251 ASN A CA    1 
ATOM   1943 C C     . ASN A 1 258 ? 29.721  3.684   33.811  1.00 49.23  ? 251 ASN A C     1 
ATOM   1944 O O     . ASN A 1 258 ? 30.636  3.422   33.003  1.00 55.18  ? 251 ASN A O     1 
ATOM   1945 C CB    . ASN A 1 258 ? 30.478  3.090   36.163  1.00 51.93  ? 251 ASN A CB    1 
ATOM   1946 C CG    . ASN A 1 258 ? 31.207  3.619   37.377  1.00 52.72  ? 251 ASN A CG    1 
ATOM   1947 O OD1   . ASN A 1 258 ? 31.163  3.008   38.441  1.00 56.28  ? 251 ASN A OD1   1 
ATOM   1948 N ND2   . ASN A 1 258 ? 31.830  4.781   37.238  1.00 50.09  ? 251 ASN A ND2   1 
ATOM   1949 N N     . CYS A 1 259 ? 28.421  3.603   33.519  1.00 47.41  ? 252 CYS A N     1 
ATOM   1950 C CA    . CYS A 1 259 ? 27.908  3.253   32.168  1.00 45.66  ? 252 CYS A CA    1 
ATOM   1951 C C     . CYS A 1 259 ? 28.095  4.394   31.146  1.00 39.86  ? 252 CYS A C     1 
ATOM   1952 O O     . CYS A 1 259 ? 27.944  4.115   29.956  1.00 44.99  ? 252 CYS A O     1 
ATOM   1953 C CB    . CYS A 1 259 ? 26.458  2.794   32.241  1.00 52.64  ? 252 CYS A CB    1 
ATOM   1954 S SG    . CYS A 1 259 ? 26.328  1.049   32.716  1.00 69.32  ? 252 CYS A SG    1 
ATOM   1955 N N     . ILE A 1 260 ? 28.427  5.625   31.552  1.00 30.49  ? 253 ILE A N     1 
ATOM   1956 C CA    . ILE A 1 260 ? 28.632  6.774   30.625  1.00 32.90  ? 253 ILE A CA    1 
ATOM   1957 C C     . ILE A 1 260 ? 30.138  6.963   30.447  1.00 35.10  ? 253 ILE A C     1 
ATOM   1958 O O     . ILE A 1 260 ? 30.775  7.543   31.362  1.00 37.26  ? 253 ILE A O     1 
ATOM   1959 C CB    . ILE A 1 260 ? 27.977  8.059   31.165  1.00 30.37  ? 253 ILE A CB    1 
ATOM   1960 C CG1   . ILE A 1 260 ? 26.469  7.901   31.372  1.00 30.09  ? 253 ILE A CG1   1 
ATOM   1961 C CG2   . ILE A 1 260 ? 28.303  9.228   30.266  1.00 29.75  ? 253 ILE A CG2   1 
ATOM   1962 C CD1   . ILE A 1 260 ? 25.838  9.031   32.143  1.00 32.83  ? 253 ILE A CD1   1 
ATOM   1963 N N     . ILE A 1 261 ? 30.708  6.514   29.333  1.00 30.60  ? 254 ILE A N     1 
ATOM   1964 C CA    . ILE A 1 261 ? 32.196  6.490   29.219  1.00 32.81  ? 254 ILE A CA    1 
ATOM   1965 C C     . ILE A 1 261 ? 32.691  7.787   28.572  1.00 31.09  ? 254 ILE A C     1 
ATOM   1966 O O     . ILE A 1 261 ? 33.881  8.125   28.719  1.00 31.51  ? 254 ILE A O     1 
ATOM   1967 C CB    . ILE A 1 261 ? 32.694  5.188   28.550  1.00 38.07  ? 254 ILE A CB    1 
ATOM   1968 C CG1   . ILE A 1 261 ? 32.390  5.015   27.059  1.00 37.06  ? 254 ILE A CG1   1 
ATOM   1969 C CG2   . ILE A 1 261 ? 32.125  4.005   29.328  1.00 45.07  ? 254 ILE A CG2   1 
ATOM   1970 C CD1   . ILE A 1 261 ? 32.084  6.243   26.283  1.00 42.59  ? 254 ILE A CD1   1 
ATOM   1971 N N     . ASN A 1 262 ? 31.801  8.515   27.913  1.00 28.52  ? 255 ASN A N     1 
ATOM   1972 C CA    . ASN A 1 262 ? 32.115  9.771   27.198  1.00 31.05  ? 255 ASN A CA    1 
ATOM   1973 C C     . ASN A 1 262 ? 32.518  10.784  28.283  1.00 28.39  ? 255 ASN A C     1 
ATOM   1974 O O     . ASN A 1 262 ? 31.710  11.045  29.183  1.00 26.85  ? 255 ASN A O     1 
ATOM   1975 C CB    . ASN A 1 262 ? 30.914  10.025  26.278  1.00 40.14  ? 255 ASN A CB    1 
ATOM   1976 C CG    . ASN A 1 262 ? 30.459  11.452  26.106  1.00 48.51  ? 255 ASN A CG    1 
ATOM   1977 O OD1   . ASN A 1 262 ? 29.292  11.651  25.778  1.00 55.44  ? 255 ASN A OD1   1 
ATOM   1978 N ND2   . ASN A 1 262 ? 31.358  12.420  26.235  1.00 49.40  ? 255 ASN A ND2   1 
ATOM   1979 N N     . LEU A 1 263 ? 33.747  11.299  28.256  1.00 27.15  ? 256 LEU A N     1 
ATOM   1980 C CA    . LEU A 1 263 ? 34.236  12.175  29.347  1.00 27.07  ? 256 LEU A CA    1 
ATOM   1981 C C     . LEU A 1 263 ? 33.427  13.476  29.421  1.00 25.17  ? 256 LEU A C     1 
ATOM   1982 O O     . LEU A 1 263 ? 33.269  13.963  30.537  1.00 23.82  ? 256 LEU A O     1 
ATOM   1983 C CB    . LEU A 1 263 ? 35.744  12.391  29.175  1.00 28.44  ? 256 LEU A CB    1 
ATOM   1984 C CG    . LEU A 1 263 ? 36.562  11.199  29.667  1.00 33.06  ? 256 LEU A CG    1 
ATOM   1985 C CD1   . LEU A 1 263 ? 37.928  11.135  28.990  1.00 40.99  ? 256 LEU A CD1   1 
ATOM   1986 C CD2   . LEU A 1 263 ? 36.695  11.220  31.173  1.00 31.21  ? 256 LEU A CD2   1 
ATOM   1987 N N     . LYS A 1 264 ? 32.978  14.065  28.306  1.00 22.03  ? 257 LYS A N     1 
ATOM   1988 C CA    . LYS A 1 264 ? 32.276  15.383  28.366  1.00 28.11  ? 257 LYS A CA    1 
ATOM   1989 C C     . LYS A 1 264 ? 30.965  15.205  29.144  1.00 24.36  ? 257 LYS A C     1 
ATOM   1990 O O     . LYS A 1 264 ? 30.662  16.003  30.039  1.00 22.06  ? 257 LYS A O     1 
ATOM   1991 C CB    . LYS A 1 264 ? 31.955  15.949  26.975  1.00 28.26  ? 257 LYS A CB    1 
ATOM   1992 C CG    . LYS A 1 264 ? 33.082  16.713  26.295  1.00 35.07  ? 257 LYS A CG    1 
ATOM   1993 C CD    . LYS A 1 264 ? 32.593  17.494  25.095  1.00 36.97  ? 257 LYS A CD    1 
ATOM   1994 C CE    . LYS A 1 264 ? 33.616  17.647  24.001  1.00 45.41  ? 257 LYS A CE    1 
ATOM   1995 N NZ    . LYS A 1 264 ? 34.036  19.051  23.807  1.00 47.11  ? 257 LYS A NZ    1 
ATOM   1996 N N     . ALA A 1 265 ? 30.219  14.155  28.829  1.00 24.23  ? 258 ALA A N     1 
ATOM   1997 C CA    . ALA A 1 265 ? 28.923  13.867  29.479  1.00 23.76  ? 258 ALA A CA    1 
ATOM   1998 C C     . ALA A 1 265 ? 29.175  13.536  30.947  1.00 23.51  ? 258 ALA A C     1 
ATOM   1999 O O     . ALA A 1 265 ? 28.500  14.109  31.814  1.00 21.79  ? 258 ALA A O     1 
ATOM   2000 C CB    . ALA A 1 265 ? 28.252  12.723  28.769  1.00 25.86  ? 258 ALA A CB    1 
ATOM   2001 N N     . ARG A 1 266 ? 30.132  12.640  31.241  1.00 21.72  ? 259 ARG A N     1 
ATOM   2002 C CA    . ARG A 1 266 ? 30.407  12.225  32.639  1.00 24.55  ? 259 ARG A CA    1 
ATOM   2003 C C     . ARG A 1 266 ? 30.800  13.446  33.490  1.00 22.65  ? 259 ARG A C     1 
ATOM   2004 O O     . ARG A 1 266 ? 30.296  13.573  34.596  1.00 22.82  ? 259 ARG A O     1 
ATOM   2005 C CB    . ARG A 1 266 ? 31.525  11.167  32.688  1.00 31.74  ? 259 ARG A CB    1 
ATOM   2006 C CG    . ARG A 1 266 ? 32.036  10.905  34.103  1.00 36.19  ? 259 ARG A CG    1 
ATOM   2007 C CD    . ARG A 1 266 ? 33.349  10.144  34.156  1.00 45.30  ? 259 ARG A CD    1 
ATOM   2008 N NE    . ARG A 1 266 ? 33.087  8.866   33.544  1.00 52.37  ? 259 ARG A NE    1 
ATOM   2009 C CZ    . ARG A 1 266 ? 32.558  7.829   34.164  1.00 49.85  ? 259 ARG A CZ    1 
ATOM   2010 N NH1   . ARG A 1 266 ? 32.289  7.893   35.455  1.00 50.02  ? 259 ARG A NH1   1 
ATOM   2011 N NH2   . ARG A 1 266 ? 32.345  6.720   33.481  1.00 53.08  ? 259 ARG A NH2   1 
ATOM   2012 N N     . ASN A 1 267 ? 31.738  14.274  33.023  1.00 21.29  ? 260 ASN A N     1 
ATOM   2013 C CA    . ASN A 1 267 ? 32.287  15.411  33.793  1.00 20.81  ? 260 ASN A CA    1 
ATOM   2014 C C     . ASN A 1 267 ? 31.216  16.476  33.953  1.00 20.11  ? 260 ASN A C     1 
ATOM   2015 O O     . ASN A 1 267 ? 31.167  17.096  35.011  1.00 20.74  ? 260 ASN A O     1 
ATOM   2016 C CB    . ASN A 1 267 ? 33.570  15.961  33.164  1.00 23.04  ? 260 ASN A CB    1 
ATOM   2017 C CG    . ASN A 1 267 ? 34.734  15.033  33.407  1.00 23.52  ? 260 ASN A CG    1 
ATOM   2018 O OD1   . ASN A 1 267 ? 35.655  14.936  32.584  1.00 26.73  ? 260 ASN A OD1   1 
ATOM   2019 N ND2   . ASN A 1 267 ? 34.657  14.319  34.510  1.00 22.28  ? 260 ASN A ND2   1 
ATOM   2020 N N     . TYR A 1 268 ? 30.350  16.656  32.958  1.00 21.31  ? 261 TYR A N     1 
ATOM   2021 C CA    . TYR A 1 268 ? 29.160  17.519  33.128  1.00 20.26  ? 261 TYR A CA    1 
ATOM   2022 C C     . TYR A 1 268 ? 28.342  17.029  34.329  1.00 19.59  ? 261 TYR A C     1 
ATOM   2023 O O     . TYR A 1 268 ? 28.029  17.782  35.227  1.00 19.96  ? 261 TYR A O     1 
ATOM   2024 C CB    . TYR A 1 268 ? 28.292  17.590  31.879  1.00 19.83  ? 261 TYR A CB    1 
ATOM   2025 C CG    . TYR A 1 268 ? 27.085  18.441  32.182  1.00 20.14  ? 261 TYR A CG    1 
ATOM   2026 C CD1   . TYR A 1 268 ? 27.247  19.800  32.384  1.00 22.74  ? 261 TYR A CD1   1 
ATOM   2027 C CD2   . TYR A 1 268 ? 25.826  17.908  32.340  1.00 21.79  ? 261 TYR A CD2   1 
ATOM   2028 C CE1   . TYR A 1 268 ? 26.180  20.624  32.703  1.00 25.06  ? 261 TYR A CE1   1 
ATOM   2029 C CE2   . TYR A 1 268 ? 24.734  18.727  32.640  1.00 22.82  ? 261 TYR A CE2   1 
ATOM   2030 C CZ    . TYR A 1 268 ? 24.917  20.087  32.830  1.00 25.11  ? 261 TYR A CZ    1 
ATOM   2031 O OH    . TYR A 1 268 ? 23.897  20.931  33.176  1.00 27.20  ? 261 TYR A OH    1 
ATOM   2032 N N     . LEU A 1 269 ? 27.961  15.761  34.352  1.00 20.19  ? 262 LEU A N     1 
ATOM   2033 C CA    . LEU A 1 269 ? 27.134  15.246  35.464  1.00 20.49  ? 262 LEU A CA    1 
ATOM   2034 C C     . LEU A 1 269 ? 27.863  15.391  36.799  1.00 20.83  ? 262 LEU A C     1 
ATOM   2035 O O     . LEU A 1 269 ? 27.211  15.741  37.817  1.00 19.50  ? 262 LEU A O     1 
ATOM   2036 C CB    . LEU A 1 269 ? 26.768  13.796  35.190  1.00 22.67  ? 262 LEU A CB    1 
ATOM   2037 C CG    . LEU A 1 269 ? 25.789  13.584  34.064  1.00 22.37  ? 262 LEU A CG    1 
ATOM   2038 C CD1   . LEU A 1 269 ? 25.664  12.098  33.818  1.00 23.13  ? 262 LEU A CD1   1 
ATOM   2039 C CD2   . LEU A 1 269 ? 24.438  14.208  34.373  1.00 25.66  ? 262 LEU A CD2   1 
ATOM   2040 N N     . LEU A 1 270 ? 29.178  15.143  36.813  1.00 20.83  ? 263 LEU A N     1 
ATOM   2041 C CA    . LEU A 1 270 ? 29.953  15.247  38.064  1.00 21.84  ? 263 LEU A CA    1 
ATOM   2042 C C     . LEU A 1 270 ? 30.040  16.704  38.537  1.00 20.85  ? 263 LEU A C     1 
ATOM   2043 O O     . LEU A 1 270 ? 30.307  16.899  39.721  1.00 22.05  ? 263 LEU A O     1 
ATOM   2044 C CB    . LEU A 1 270 ? 31.350  14.673  37.847  1.00 24.24  ? 263 LEU A CB    1 
ATOM   2045 C CG    . LEU A 1 270 ? 31.407  13.155  37.766  1.00 26.13  ? 263 LEU A CG    1 
ATOM   2046 C CD1   . LEU A 1 270 ? 32.853  12.707  37.600  1.00 28.13  ? 263 LEU A CD1   1 
ATOM   2047 C CD2   . LEU A 1 270 ? 30.767  12.526  38.981  1.00 26.01  ? 263 LEU A CD2   1 
ATOM   2048 N N     . SER A 1 271 ? 29.879  17.677  37.657  1.00 19.44  ? 264 SER A N     1 
ATOM   2049 C CA    . SER A 1 271 ? 30.025  19.118  37.987  1.00 21.71  ? 264 SER A CA    1 
ATOM   2050 C C     . SER A 1 271 ? 28.774  19.604  38.723  1.00 22.38  ? 264 SER A C     1 
ATOM   2051 O O     . SER A 1 271 ? 28.810  20.682  39.317  1.00 22.46  ? 264 SER A O     1 
ATOM   2052 C CB    . SER A 1 271 ? 30.274  19.927  36.738  1.00 23.04  ? 264 SER A CB    1 
ATOM   2053 O OG    . SER A 1 271 ? 29.042  20.160  36.036  1.00 19.48  ? 264 SER A OG    1 
ATOM   2054 N N     . LEU A 1 272 ? 27.688  18.836  38.681  1.00 22.96  ? 265 LEU A N     1 
ATOM   2055 C CA    . LEU A 1 272 ? 26.389  19.309  39.213  1.00 22.14  ? 265 LEU A CA    1 
ATOM   2056 C C     . LEU A 1 272 ? 26.368  19.074  40.723  1.00 23.30  ? 265 LEU A C     1 
ATOM   2057 O O     . LEU A 1 272 ? 26.900  18.066  41.228  1.00 21.89  ? 265 LEU A O     1 
ATOM   2058 C CB    . LEU A 1 272 ? 25.239  18.567  38.539  1.00 22.13  ? 265 LEU A CB    1 
ATOM   2059 C CG    . LEU A 1 272 ? 25.130  18.732  37.027  1.00 21.80  ? 265 LEU A CG    1 
ATOM   2060 C CD1   . LEU A 1 272 ? 23.937  17.945  36.514  1.00 21.78  ? 265 LEU A CD1   1 
ATOM   2061 C CD2   . LEU A 1 272 ? 25.003  20.189  36.628  1.00 22.12  ? 265 LEU A CD2   1 
ATOM   2062 N N     . PRO A 1 273 ? 25.627  19.925  41.468  1.00 24.75  ? 266 PRO A N     1 
ATOM   2063 C CA    . PRO A 1 273 ? 25.424  19.721  42.901  1.00 25.24  ? 266 PRO A CA    1 
ATOM   2064 C C     . PRO A 1 273 ? 24.591  18.454  43.128  1.00 25.04  ? 266 PRO A C     1 
ATOM   2065 O O     . PRO A 1 273 ? 23.758  18.116  42.320  1.00 22.90  ? 266 PRO A O     1 
ATOM   2066 C CB    . PRO A 1 273 ? 24.594  20.932  43.370  1.00 26.78  ? 266 PRO A CB    1 
ATOM   2067 C CG    . PRO A 1 273 ? 24.762  21.934  42.254  1.00 30.00  ? 266 PRO A CG    1 
ATOM   2068 C CD    . PRO A 1 273 ? 24.885  21.099  40.990  1.00 27.22  ? 266 PRO A CD    1 
ATOM   2069 N N     . HIS A 1 274 ? 24.862  17.779  44.231  1.00 25.86  ? 267 HIS A N     1 
ATOM   2070 C CA    . HIS A 1 274 ? 24.101  16.606  44.705  1.00 29.46  ? 267 HIS A CA    1 
ATOM   2071 C C     . HIS A 1 274 ? 22.628  16.976  44.827  1.00 29.68  ? 267 HIS A C     1 
ATOM   2072 O O     . HIS A 1 274 ? 22.348  18.072  45.377  1.00 28.97  ? 267 HIS A O     1 
ATOM   2073 C CB    . HIS A 1 274 ? 24.621  16.123  46.072  1.00 28.58  ? 267 HIS A CB    1 
ATOM   2074 C CG    . HIS A 1 274 ? 23.850  14.947  46.543  1.00 28.92  ? 267 HIS A CG    1 
ATOM   2075 N ND1   . HIS A 1 274 ? 23.197  14.920  47.744  1.00 31.68  ? 267 HIS A ND1   1 
ATOM   2076 C CD2   . HIS A 1 274 ? 23.550  13.795  45.911  1.00 31.62  ? 267 HIS A CD2   1 
ATOM   2077 C CE1   . HIS A 1 274 ? 22.538  13.784  47.852  1.00 32.51  ? 267 HIS A CE1   1 
ATOM   2078 N NE2   . HIS A 1 274 ? 22.734  13.080  46.741  1.00 33.74  ? 267 HIS A NE2   1 
ATOM   2079 N N     . LYS A 1 275 ? 21.733  16.105  44.342  1.00 27.63  ? 268 LYS A N     1 
ATOM   2080 C CA    . LYS A 1 275 ? 20.267  16.244  44.556  1.00 31.82  ? 268 LYS A CA    1 
ATOM   2081 C C     . LYS A 1 275 ? 19.728  14.855  44.868  1.00 29.87  ? 268 LYS A C     1 
ATOM   2082 O O     . LYS A 1 275 ? 20.104  13.917  44.167  1.00 27.22  ? 268 LYS A O     1 
ATOM   2083 C CB    . LYS A 1 275 ? 19.492  16.798  43.359  1.00 38.06  ? 268 LYS A CB    1 
ATOM   2084 C CG    . LYS A 1 275 ? 19.508  18.309  43.165  1.00 43.57  ? 268 LYS A CG    1 
ATOM   2085 C CD    . LYS A 1 275 ? 20.570  18.773  42.200  1.00 52.78  ? 268 LYS A CD    1 
ATOM   2086 C CE    . LYS A 1 275 ? 20.914  17.781  41.093  1.00 55.70  ? 268 LYS A CE    1 
ATOM   2087 N NZ    . LYS A 1 275 ? 22.043  18.252  40.260  1.00 48.99  ? 268 LYS A NZ    1 
ATOM   2088 N N     . ASN A 1 276 ? 18.961  14.738  45.945  1.00 32.39  ? 269 ASN A N     1 
ATOM   2089 C CA    . ASN A 1 276 ? 18.273  13.481  46.350  1.00 33.17  ? 269 ASN A CA    1 
ATOM   2090 C C     . ASN A 1 276 ? 17.064  13.318  45.425  1.00 31.67  ? 269 ASN A C     1 
ATOM   2091 O O     . ASN A 1 276 ? 16.520  14.326  44.995  1.00 29.17  ? 269 ASN A O     1 
ATOM   2092 C CB    . ASN A 1 276 ? 17.868  13.516  47.832  1.00 33.53  ? 269 ASN A CB    1 
ATOM   2093 C CG    . ASN A 1 276 ? 19.054  13.480  48.773  1.00 39.28  ? 269 ASN A CG    1 
ATOM   2094 O OD1   . ASN A 1 276 ? 19.927  12.624  48.636  1.00 42.81  ? 269 ASN A OD1   1 
ATOM   2095 N ND2   . ASN A 1 276 ? 19.110  14.394  49.736  1.00 39.00  ? 269 ASN A ND2   1 
ATOM   2096 N N     . LYS A 1 277 ? 16.637  12.090  45.182  1.00 34.73  ? 270 LYS A N     1 
ATOM   2097 C CA    . LYS A 1 277 ? 15.384  11.763  44.437  1.00 37.13  ? 270 LYS A CA    1 
ATOM   2098 C C     . LYS A 1 277 ? 14.176  12.455  45.086  1.00 41.70  ? 270 LYS A C     1 
ATOM   2099 O O     . LYS A 1 277 ? 14.079  12.442  46.328  1.00 48.71  ? 270 LYS A O     1 
ATOM   2100 C CB    . LYS A 1 277 ? 15.250  10.237  44.438  1.00 38.12  ? 270 LYS A CB    1 
ATOM   2101 C CG    . LYS A 1 277 ? 14.038  9.649   43.731  1.00 38.93  ? 270 LYS A CG    1 
ATOM   2102 C CD    . LYS A 1 277 ? 14.214  8.171   43.411  1.00 41.49  ? 270 LYS A CD    1 
ATOM   2103 C CE    . LYS A 1 277 ? 13.081  7.577   42.585  1.00 42.69  ? 270 LYS A CE    1 
ATOM   2104 N NZ    . LYS A 1 277 ? 12.982  8.151   41.220  1.00 36.59  ? 270 LYS A NZ    1 
ATOM   2105 N N     . VAL A 1 278 ? 13.286  13.050  44.293  1.00 38.04  ? 271 VAL A N     1 
ATOM   2106 C CA    . VAL A 1 278 ? 11.943  13.510  44.741  1.00 40.02  ? 271 VAL A CA    1 
ATOM   2107 C C     . VAL A 1 278 ? 11.014  12.321  44.536  1.00 44.14  ? 271 VAL A C     1 
ATOM   2108 O O     . VAL A 1 278 ? 10.817  11.866  43.405  1.00 37.04  ? 271 VAL A O     1 
ATOM   2109 C CB    . VAL A 1 278 ? 11.443  14.761  44.001  1.00 43.86  ? 271 VAL A CB    1 
ATOM   2110 C CG1   . VAL A 1 278 ? 10.132  15.274  44.566  1.00 46.96  ? 271 VAL A CG1   1 
ATOM   2111 C CG2   . VAL A 1 278 ? 12.461  15.884  44.002  1.00 47.46  ? 271 VAL A CG2   1 
ATOM   2112 N N     . PRO A 1 279 ? 10.404  11.791  45.618  1.00 45.24  ? 272 PRO A N     1 
ATOM   2113 C CA    . PRO A 1 279 ? 9.681   10.525  45.532  1.00 43.60  ? 272 PRO A CA    1 
ATOM   2114 C C     . PRO A 1 279 ? 8.368   10.812  44.797  1.00 32.51  ? 272 PRO A C     1 
ATOM   2115 O O     . PRO A 1 279 ? 7.782   11.852  44.985  1.00 34.66  ? 272 PRO A O     1 
ATOM   2116 C CB    . PRO A 1 279 ? 9.533   10.112  47.005  1.00 45.48  ? 272 PRO A CB    1 
ATOM   2117 C CG    . PRO A 1 279 ? 9.436   11.443  47.742  1.00 44.52  ? 272 PRO A CG    1 
ATOM   2118 C CD    . PRO A 1 279 ? 10.280  12.417  46.945  1.00 44.36  ? 272 PRO A CD    1 
ATOM   2119 N N     . TRP A 1 280 ? 7.947   9.895   43.928  1.00 33.08  ? 273 TRP A N     1 
ATOM   2120 C CA    . TRP A 1 280 ? 6.773   10.094  43.036  1.00 31.75  ? 273 TRP A CA    1 
ATOM   2121 C C     . TRP A 1 280 ? 5.509   10.405  43.845  1.00 34.06  ? 273 TRP A C     1 
ATOM   2122 O O     . TRP A 1 280 ? 4.635   11.163  43.347  1.00 34.04  ? 273 TRP A O     1 
ATOM   2123 C CB    . TRP A 1 280 ? 6.590   8.847   42.166  1.00 30.81  ? 273 TRP A CB    1 
ATOM   2124 C CG    . TRP A 1 280 ? 7.709   8.663   41.199  1.00 30.09  ? 273 TRP A CG    1 
ATOM   2125 C CD1   . TRP A 1 280 ? 8.628   7.657   41.173  1.00 31.19  ? 273 TRP A CD1   1 
ATOM   2126 C CD2   . TRP A 1 280 ? 8.054   9.546   40.130  1.00 26.15  ? 273 TRP A CD2   1 
ATOM   2127 N NE1   . TRP A 1 280 ? 9.500   7.855   40.138  1.00 28.49  ? 273 TRP A NE1   1 
ATOM   2128 C CE2   . TRP A 1 280 ? 9.183   9.005   39.493  1.00 27.62  ? 273 TRP A CE2   1 
ATOM   2129 C CE3   . TRP A 1 280 ? 7.535   10.744  39.676  1.00 28.67  ? 273 TRP A CE3   1 
ATOM   2130 C CZ2   . TRP A 1 280 ? 9.755   9.596   38.385  1.00 28.07  ? 273 TRP A CZ2   1 
ATOM   2131 C CZ3   . TRP A 1 280 ? 8.134   11.365  38.615  1.00 30.98  ? 273 TRP A CZ3   1 
ATOM   2132 C CH2   . TRP A 1 280 ? 9.226   10.794  37.979  1.00 30.41  ? 273 TRP A CH2   1 
ATOM   2133 N N     . ASN A 1 281 ? 5.400   9.841   45.053  1.00 37.41  ? 274 ASN A N     1 
ATOM   2134 C CA    . ASN A 1 281 ? 4.211   10.046  45.921  1.00 42.40  ? 274 ASN A CA    1 
ATOM   2135 C C     . ASN A 1 281 ? 4.213   11.498  46.428  1.00 40.53  ? 274 ASN A C     1 
ATOM   2136 O O     . ASN A 1 281 ? 3.144   12.004  46.732  1.00 44.16  ? 274 ASN A O     1 
ATOM   2137 C CB    . ASN A 1 281 ? 4.103   8.961   46.998  1.00 44.04  ? 274 ASN A CB    1 
ATOM   2138 C CG    . ASN A 1 281 ? 5.169   9.035   48.075  1.00 50.23  ? 274 ASN A CG    1 
ATOM   2139 O OD1   . ASN A 1 281 ? 5.195   8.201   48.970  1.00 57.90  ? 274 ASN A OD1   1 
ATOM   2140 N ND2   . ASN A 1 281 ? 6.065   10.001  47.996  1.00 50.44  ? 274 ASN A ND2   1 
ATOM   2141 N N     . ARG A 1 282 ? 5.349   12.183  46.440  1.00 45.43  ? 275 ARG A N     1 
ATOM   2142 C CA    . ARG A 1 282 ? 5.385   13.639  46.754  1.00 47.53  ? 275 ARG A CA    1 
ATOM   2143 C C     . ARG A 1 282 ? 4.764   14.407  45.579  1.00 46.04  ? 275 ARG A C     1 
ATOM   2144 O O     . ARG A 1 282 ? 3.986   15.338  45.817  1.00 42.54  ? 275 ARG A O     1 
ATOM   2145 C CB    . ARG A 1 282 ? 6.819   14.134  47.000  1.00 55.87  ? 275 ARG A CB    1 
ATOM   2146 C CG    . ARG A 1 282 ? 6.940   15.196  48.090  1.00 63.53  ? 275 ARG A CG    1 
ATOM   2147 C CD    . ARG A 1 282 ? 7.572   14.737  49.408  1.00 69.93  ? 275 ARG A CD    1 
ATOM   2148 N NE    . ARG A 1 282 ? 7.328   13.334  49.759  1.00 71.81  ? 275 ARG A NE    1 
ATOM   2149 C CZ    . ARG A 1 282 ? 7.997   12.629  50.680  1.00 69.67  ? 275 ARG A CZ    1 
ATOM   2150 N NH1   . ARG A 1 282 ? 8.982   13.171  51.383  1.00 62.79  ? 275 ARG A NH1   1 
ATOM   2151 N NH2   . ARG A 1 282 ? 7.677   11.361  50.882  1.00 68.94  ? 275 ARG A NH2   1 
ATOM   2152 N N     . LEU A 1 283 ? 5.082   14.025  44.339  1.00 37.30  ? 276 LEU A N     1 
ATOM   2153 C CA    . LEU A 1 283 ? 4.616   14.774  43.152  1.00 35.11  ? 276 LEU A CA    1 
ATOM   2154 C C     . LEU A 1 283 ? 3.152   14.455  42.879  1.00 34.81  ? 276 LEU A C     1 
ATOM   2155 O O     . LEU A 1 283 ? 2.499   15.337  42.329  1.00 32.88  ? 276 LEU A O     1 
ATOM   2156 C CB    . LEU A 1 283 ? 5.470   14.427  41.929  1.00 34.78  ? 276 LEU A CB    1 
ATOM   2157 C CG    . LEU A 1 283 ? 6.869   15.030  41.900  1.00 37.46  ? 276 LEU A CG    1 
ATOM   2158 C CD1   . LEU A 1 283 ? 7.770   14.226  40.985  1.00 39.20  ? 276 LEU A CD1   1 
ATOM   2159 C CD2   . LEU A 1 283 ? 6.831   16.499  41.462  1.00 41.71  ? 276 LEU A CD2   1 
ATOM   2160 N N     . PHE A 1 284 ? 2.696   13.229  43.173  1.00 34.04  ? 277 PHE A N     1 
ATOM   2161 C CA    . PHE A 1 284 ? 1.384   12.679  42.720  1.00 35.60  ? 277 PHE A CA    1 
ATOM   2162 C C     . PHE A 1 284 ? 0.691   11.995  43.893  1.00 38.86  ? 277 PHE A C     1 
ATOM   2163 O O     . PHE A 1 284 ? 0.557   10.761  43.942  1.00 35.88  ? 277 PHE A O     1 
ATOM   2164 C CB    . PHE A 1 284 ? 1.592   11.687  41.568  1.00 36.37  ? 277 PHE A CB    1 
ATOM   2165 C CG    . PHE A 1 284 ? 2.283   12.249  40.353  1.00 34.17  ? 277 PHE A CG    1 
ATOM   2166 C CD1   . PHE A 1 284 ? 1.660   13.189  39.541  1.00 39.21  ? 277 PHE A CD1   1 
ATOM   2167 C CD2   . PHE A 1 284 ? 3.549   11.817  40.005  1.00 30.22  ? 277 PHE A CD2   1 
ATOM   2168 C CE1   . PHE A 1 284 ? 2.309   13.693  38.424  1.00 36.61  ? 277 PHE A CE1   1 
ATOM   2169 C CE2   . PHE A 1 284 ? 4.182   12.308  38.873  1.00 30.92  ? 277 PHE A CE2   1 
ATOM   2170 C CZ    . PHE A 1 284 ? 3.555   13.237  38.085  1.00 32.45  ? 277 PHE A CZ    1 
ATOM   2171 N N     . PRO A 1 285 ? 0.260   12.779  44.908  1.00 44.78  ? 278 PRO A N     1 
ATOM   2172 C CA    . PRO A 1 285 ? -0.125  12.202  46.198  1.00 43.92  ? 278 PRO A CA    1 
ATOM   2173 C C     . PRO A 1 285 ? -1.457  11.432  46.144  1.00 41.61  ? 278 PRO A C     1 
ATOM   2174 O O     . PRO A 1 285 ? -1.676  10.624  47.015  1.00 49.07  ? 278 PRO A O     1 
ATOM   2175 C CB    . PRO A 1 285 ? -0.127  13.437  47.138  1.00 45.57  ? 278 PRO A CB    1 
ATOM   2176 C CG    . PRO A 1 285 ? -0.460  14.609  46.224  1.00 45.48  ? 278 PRO A CG    1 
ATOM   2177 C CD    . PRO A 1 285 ? 0.153   14.250  44.878  1.00 44.00  ? 278 PRO A CD    1 
ATOM   2178 N N     . ASN A 1 286 ? -2.282  11.670  45.119  1.00 45.79  ? 279 ASN A N     1 
ATOM   2179 C CA    . ASN A 1 286 ? -3.560  10.950  44.867  1.00 47.02  ? 279 ASN A CA    1 
ATOM   2180 C C     . ASN A 1 286 ? -3.415  9.856   43.791  1.00 44.93  ? 279 ASN A C     1 
ATOM   2181 O O     . ASN A 1 286 ? -4.416  9.241   43.474  1.00 39.75  ? 279 ASN A O     1 
ATOM   2182 C CB    . ASN A 1 286 ? -4.652  11.903  44.390  1.00 53.61  ? 279 ASN A CB    1 
ATOM   2183 C CG    . ASN A 1 286 ? -4.604  13.223  45.118  1.00 62.27  ? 279 ASN A CG    1 
ATOM   2184 O OD1   . ASN A 1 286 ? -4.757  14.280  44.506  1.00 73.93  ? 279 ASN A OD1   1 
ATOM   2185 N ND2   . ASN A 1 286 ? -4.325  13.163  46.411  1.00 60.45  ? 279 ASN A ND2   1 
ATOM   2186 N N     . ALA A 1 287 ? -2.235  9.627   43.212  1.00 39.35  ? 280 ALA A N     1 
ATOM   2187 C CA    . ALA A 1 287 ? -2.046  8.597   42.157  1.00 31.55  ? 280 ALA A CA    1 
ATOM   2188 C C     . ALA A 1 287 ? -2.188  7.214   42.781  1.00 29.27  ? 280 ALA A C     1 
ATOM   2189 O O     . ALA A 1 287 ? -1.864  7.030   43.951  1.00 29.73  ? 280 ALA A O     1 
ATOM   2190 C CB    . ALA A 1 287 ? -0.694  8.782   41.504  1.00 28.09  ? 280 ALA A CB    1 
ATOM   2191 N N     . ASP A 1 288 ? -2.680  6.264   42.014  1.00 29.09  ? 281 ASP A N     1 
ATOM   2192 C CA    . ASP A 1 288 ? -2.628  4.825   42.334  1.00 30.07  ? 281 ASP A CA    1 
ATOM   2193 C C     . ASP A 1 288 ? -1.172  4.439   42.586  1.00 30.58  ? 281 ASP A C     1 
ATOM   2194 O O     . ASP A 1 288 ? -0.327  4.774   41.733  1.00 30.31  ? 281 ASP A O     1 
ATOM   2195 C CB    . ASP A 1 288 ? -3.194  4.086   41.133  1.00 31.82  ? 281 ASP A CB    1 
ATOM   2196 C CG    . ASP A 1 288 ? -3.313  2.596   41.307  1.00 32.84  ? 281 ASP A CG    1 
ATOM   2197 O OD1   . ASP A 1 288 ? -2.459  2.029   41.969  1.00 34.86  ? 281 ASP A OD1   1 
ATOM   2198 O OD2   . ASP A 1 288 ? -4.245  2.039   40.717  1.00 33.96  ? 281 ASP A OD2   1 
ATOM   2199 N N     . SER A 1 289 ? -0.867  3.745   43.674  1.00 27.30  ? 282 SER A N     1 
ATOM   2200 C CA    . SER A 1 289 ? 0.539   3.438   44.035  1.00 29.00  ? 282 SER A CA    1 
ATOM   2201 C C     . SER A 1 289 ? 1.134   2.466   42.997  1.00 25.74  ? 282 SER A C     1 
ATOM   2202 O O     . SER A 1 289 ? 2.367   2.480   42.805  1.00 24.98  ? 282 SER A O     1 
ATOM   2203 C CB    . SER A 1 289 ? 0.650   2.887   45.427  1.00 31.34  ? 282 SER A CB    1 
ATOM   2204 O OG    . SER A 1 289 ? -0.089  1.675   45.511  1.00 35.37  ? 282 SER A OG    1 
ATOM   2205 N N     . LYS A 1 290 ? 0.307   1.639   42.354  1.00 27.19  ? 283 LYS A N     1 
ATOM   2206 C CA    . LYS A 1 290 ? 0.771   0.729   41.270  1.00 28.92  ? 283 LYS A CA    1 
ATOM   2207 C C     . LYS A 1 290 ? 1.179   1.579   40.063  1.00 24.49  ? 283 LYS A C     1 
ATOM   2208 O O     . LYS A 1 290 ? 2.188   1.248   39.468  1.00 22.33  ? 283 LYS A O     1 
ATOM   2209 C CB    . LYS A 1 290 ? -0.293  -0.315  40.917  1.00 30.04  ? 283 LYS A CB    1 
ATOM   2210 C CG    . LYS A 1 290 ? -0.553  -1.326  42.018  1.00 33.03  ? 283 LYS A CG    1 
ATOM   2211 C CD    . LYS A 1 290 ? -1.662  -2.320  41.706  1.00 33.90  ? 283 LYS A CD    1 
ATOM   2212 C CE    . LYS A 1 290 ? -2.114  -3.051  42.960  1.00 37.80  ? 283 LYS A CE    1 
ATOM   2213 N NZ    . LYS A 1 290 ? -3.004  -4.193  42.618  1.00 40.55  ? 283 LYS A NZ    1 
ATOM   2214 N N     . ALA A 1 291 ? 0.439   2.653   39.753  1.00 24.71  ? 284 ALA A N     1 
ATOM   2215 C CA    . ALA A 1 291 ? 0.778   3.567   38.626  1.00 25.93  ? 284 ALA A CA    1 
ATOM   2216 C C     . ALA A 1 291 ? 2.156   4.194   38.870  1.00 25.68  ? 284 ALA A C     1 
ATOM   2217 O O     . ALA A 1 291 ? 2.948   4.312   37.905  1.00 21.41  ? 284 ALA A O     1 
ATOM   2218 C CB    . ALA A 1 291 ? -0.294  4.622   38.438  1.00 26.24  ? 284 ALA A CB    1 
ATOM   2219 N N     . LEU A 1 292 ? 2.436   4.599   40.118  1.00 23.46  ? 285 LEU A N     1 
ATOM   2220 C CA    . LEU A 1 292 ? 3.703   5.273   40.490  1.00 23.55  ? 285 LEU A CA    1 
ATOM   2221 C C     . LEU A 1 292 ? 4.847   4.247   40.477  1.00 23.46  ? 285 LEU A C     1 
ATOM   2222 O O     . LEU A 1 292 ? 5.934   4.596   40.140  1.00 21.40  ? 285 LEU A O     1 
ATOM   2223 C CB    . LEU A 1 292 ? 3.544   5.915   41.875  1.00 24.03  ? 285 LEU A CB    1 
ATOM   2224 C CG    . LEU A 1 292 ? 2.493   7.021   41.968  1.00 25.47  ? 285 LEU A CG    1 
ATOM   2225 C CD1   . LEU A 1 292 ? 2.607   7.742   43.310  1.00 27.08  ? 285 LEU A CD1   1 
ATOM   2226 C CD2   . LEU A 1 292 ? 2.623   8.009   40.827  1.00 27.10  ? 285 LEU A CD2   1 
ATOM   2227 N N     . ASP A 1 293 ? 4.590   2.991   40.792  1.00 24.00  ? 286 ASP A N     1 
ATOM   2228 C CA    . ASP A 1 293 ? 5.634   1.954   40.750  1.00 24.98  ? 286 ASP A CA    1 
ATOM   2229 C C     . ASP A 1 293 ? 6.030   1.738   39.278  1.00 23.56  ? 286 ASP A C     1 
ATOM   2230 O O     . ASP A 1 293 ? 7.259   1.693   38.972  1.00 23.76  ? 286 ASP A O     1 
ATOM   2231 C CB    . ASP A 1 293 ? 5.163   0.658   41.403  1.00 26.72  ? 286 ASP A CB    1 
ATOM   2232 C CG    . ASP A 1 293 ? 6.306   -0.316  41.427  1.00 29.33  ? 286 ASP A CG    1 
ATOM   2233 O OD1   . ASP A 1 293 ? 7.219   -0.123  42.250  1.00 34.07  ? 286 ASP A OD1   1 
ATOM   2234 O OD2   . ASP A 1 293 ? 6.352   -1.151  40.531  1.00 31.90  ? 286 ASP A OD2   1 
ATOM   2235 N N     . LEU A 1 294 ? 5.049   1.719   38.384  1.00 21.63  ? 287 LEU A N     1 
ATOM   2236 C CA    . LEU A 1 294 ? 5.343   1.510   36.943  1.00 21.43  ? 287 LEU A CA    1 
ATOM   2237 C C     . LEU A 1 294 ? 6.025   2.761   36.391  1.00 21.63  ? 287 LEU A C     1 
ATOM   2238 O O     . LEU A 1 294 ? 7.003   2.620   35.621  1.00 21.67  ? 287 LEU A O     1 
ATOM   2239 C CB    . LEU A 1 294 ? 4.058   1.163   36.200  1.00 20.20  ? 287 LEU A CB    1 
ATOM   2240 C CG    . LEU A 1 294 ? 4.202   1.016   34.684  1.00 20.21  ? 287 LEU A CG    1 
ATOM   2241 C CD1   . LEU A 1 294 ? 5.369   0.089   34.338  1.00 20.18  ? 287 LEU A CD1   1 
ATOM   2242 C CD2   . LEU A 1 294 ? 2.908   0.470   34.125  1.00 21.07  ? 287 LEU A CD2   1 
ATOM   2243 N N     . LEU A 1 295 ? 5.549   3.949   36.783  1.00 21.05  ? 288 LEU A N     1 
ATOM   2244 C CA    . LEU A 1 295 ? 6.159   5.242   36.369  1.00 21.03  ? 288 LEU A CA    1 
ATOM   2245 C C     . LEU A 1 295 ? 7.645   5.239   36.697  1.00 20.85  ? 288 LEU A C     1 
ATOM   2246 O O     . LEU A 1 295 ? 8.449   5.686   35.846  1.00 20.70  ? 288 LEU A O     1 
ATOM   2247 C CB    . LEU A 1 295 ? 5.449   6.417   37.048  1.00 22.19  ? 288 LEU A CB    1 
ATOM   2248 C CG    . LEU A 1 295 ? 5.991   7.817   36.725  1.00 22.74  ? 288 LEU A CG    1 
ATOM   2249 C CD1   . LEU A 1 295 ? 5.804   8.156   35.256  1.00 23.29  ? 288 LEU A CD1   1 
ATOM   2250 C CD2   . LEU A 1 295 ? 5.294   8.867   37.596  1.00 22.55  ? 288 LEU A CD2   1 
ATOM   2251 N N     . ASP A 1 296 ? 7.986   4.776   37.892  1.00 21.35  ? 289 ASP A N     1 
ATOM   2252 C CA    . ASP A 1 296 ? 9.366   4.759   38.434  1.00 23.07  ? 289 ASP A CA    1 
ATOM   2253 C C     . ASP A 1 296 ? 10.222  3.926   37.480  1.00 23.45  ? 289 ASP A C     1 
ATOM   2254 O O     . ASP A 1 296 ? 11.346  4.359   37.145  1.00 20.40  ? 289 ASP A O     1 
ATOM   2255 C CB    . ASP A 1 296 ? 9.370   4.251   39.874  1.00 25.32  ? 289 ASP A CB    1 
ATOM   2256 C CG    . ASP A 1 296 ? 10.750  4.313   40.514  1.00 27.56  ? 289 ASP A CG    1 
ATOM   2257 O OD1   . ASP A 1 296 ? 11.333  5.361   40.492  1.00 29.67  ? 289 ASP A OD1   1 
ATOM   2258 O OD2   . ASP A 1 296 ? 11.245  3.269   40.935  1.00 35.11  ? 289 ASP A OD2   1 
ATOM   2259 N N     . LYS A 1 297 ? 9.653   2.829   37.002  1.00 21.06  ? 290 LYS A N     1 
ATOM   2260 C CA    . LYS A 1 297 ? 10.352  1.807   36.195  1.00 21.68  ? 290 LYS A CA    1 
ATOM   2261 C C     . LYS A 1 297 ? 10.518  2.316   34.766  1.00 20.66  ? 290 LYS A C     1 
ATOM   2262 O O     . LYS A 1 297 ? 11.519  1.975   34.133  1.00 22.70  ? 290 LYS A O     1 
ATOM   2263 C CB    . LYS A 1 297 ? 9.577   0.497   36.330  1.00 22.00  ? 290 LYS A CB    1 
ATOM   2264 C CG    . LYS A 1 297 ? 9.869   -0.243  37.642  1.00 25.27  ? 290 LYS A CG    1 
ATOM   2265 C CD    . LYS A 1 297 ? 9.027   -1.506  37.771  1.00 28.98  ? 290 LYS A CD    1 
ATOM   2266 C CE    . LYS A 1 297 ? 9.501   -2.452  38.845  1.00 32.06  ? 290 LYS A CE    1 
ATOM   2267 N NZ    . LYS A 1 297 ? 9.517   -1.766  40.144  1.00 37.34  ? 290 LYS A NZ    1 
ATOM   2268 N N     . MET A 1 298 ? 9.597   3.146   34.296  1.00 18.97  ? 291 MET A N     1 
ATOM   2269 C CA    . MET A 1 298 ? 9.690   3.750   32.950  1.00 19.87  ? 291 MET A CA    1 
ATOM   2270 C C     . MET A 1 298 ? 10.621  4.978   32.960  1.00 21.01  ? 291 MET A C     1 
ATOM   2271 O O     . MET A 1 298 ? 11.356  5.155   31.979  1.00 22.27  ? 291 MET A O     1 
ATOM   2272 C CB    . MET A 1 298 ? 8.297   4.127   32.472  1.00 20.71  ? 291 MET A CB    1 
ATOM   2273 C CG    . MET A 1 298 ? 7.423   2.923   32.264  1.00 23.06  ? 291 MET A CG    1 
ATOM   2274 S SD    . MET A 1 298 ? 5.792   3.479   31.700  1.00 27.04  ? 291 MET A SD    1 
ATOM   2275 C CE    . MET A 1 298 ? 5.340   2.049   30.751  1.00 31.73  ? 291 MET A CE    1 
ATOM   2276 N N     . LEU A 1 299 ? 10.677  5.735   34.060  1.00 19.24  ? 292 LEU A N     1 
ATOM   2277 C CA    . LEU A 1 299 ? 11.558  6.923   34.145  1.00 20.44  ? 292 LEU A CA    1 
ATOM   2278 C C     . LEU A 1 299 ? 12.803  6.584   34.974  1.00 21.93  ? 292 LEU A C     1 
ATOM   2279 O O     . LEU A 1 299 ? 13.116  7.254   35.960  1.00 25.70  ? 292 LEU A O     1 
ATOM   2280 C CB    . LEU A 1 299 ? 10.733  8.092   34.673  1.00 20.68  ? 292 LEU A CB    1 
ATOM   2281 C CG    . LEU A 1 299 ? 9.554   8.521   33.798  1.00 19.93  ? 292 LEU A CG    1 
ATOM   2282 C CD1   . LEU A 1 299 ? 8.823   9.687   34.434  1.00 19.76  ? 292 LEU A CD1   1 
ATOM   2283 C CD2   . LEU A 1 299 ? 9.977   8.879   32.381  1.00 19.65  ? 292 LEU A CD2   1 
ATOM   2284 N N     . THR A 1 300 ? 13.466  5.515   34.573  1.00 22.58  ? 293 THR A N     1 
ATOM   2285 C CA    . THR A 1 300 ? 14.779  5.092   35.089  1.00 24.33  ? 293 THR A CA    1 
ATOM   2286 C C     . THR A 1 300 ? 15.837  5.818   34.285  1.00 22.93  ? 293 THR A C     1 
ATOM   2287 O O     . THR A 1 300 ? 15.761  5.829   33.042  1.00 21.80  ? 293 THR A O     1 
ATOM   2288 C CB    . THR A 1 300 ? 14.872  3.569   35.062  1.00 28.18  ? 293 THR A CB    1 
ATOM   2289 O OG1   . THR A 1 300 ? 13.884  3.152   36.005  1.00 28.71  ? 293 THR A OG1   1 
ATOM   2290 C CG2   . THR A 1 300 ? 16.239  3.062   35.407  1.00 30.62  ? 293 THR A CG2   1 
ATOM   2291 N N     . PHE A 1 301 ? 16.799  6.423   34.967  1.00 22.65  ? 294 PHE A N     1 
ATOM   2292 C CA    . PHE A 1 301 ? 17.884  7.204   34.315  1.00 22.64  ? 294 PHE A CA    1 
ATOM   2293 C C     . PHE A 1 301 ? 18.649  6.300   33.328  1.00 22.71  ? 294 PHE A C     1 
ATOM   2294 O O     . PHE A 1 301 ? 18.905  6.709   32.173  1.00 21.78  ? 294 PHE A O     1 
ATOM   2295 C CB    . PHE A 1 301 ? 18.767  7.827   35.393  1.00 24.73  ? 294 PHE A CB    1 
ATOM   2296 C CG    . PHE A 1 301 ? 19.925  8.571   34.810  1.00 26.08  ? 294 PHE A CG    1 
ATOM   2297 C CD1   . PHE A 1 301 ? 19.755  9.852   34.326  1.00 24.73  ? 294 PHE A CD1   1 
ATOM   2298 C CD2   . PHE A 1 301 ? 21.158  7.934   34.658  1.00 27.32  ? 294 PHE A CD2   1 
ATOM   2299 C CE1   . PHE A 1 301 ? 20.829  10.524  33.773  1.00 26.60  ? 294 PHE A CE1   1 
ATOM   2300 C CE2   . PHE A 1 301 ? 22.226  8.609   34.088  1.00 27.22  ? 294 PHE A CE2   1 
ATOM   2301 C CZ    . PHE A 1 301 ? 22.058  9.902   33.661  1.00 27.77  ? 294 PHE A CZ    1 
ATOM   2302 N N     . ASN A 1 302 ? 19.007  5.096   33.773  1.00 22.95  ? 295 ASN A N     1 
ATOM   2303 C CA    . ASN A 1 302 ? 19.902  4.173   33.034  1.00 23.75  ? 295 ASN A CA    1 
ATOM   2304 C C     . ASN A 1 302 ? 19.036  3.376   32.070  1.00 21.43  ? 295 ASN A C     1 
ATOM   2305 O O     . ASN A 1 302 ? 18.138  2.660   32.515  1.00 20.86  ? 295 ASN A O     1 
ATOM   2306 C CB    . ASN A 1 302 ? 20.654  3.228   33.966  1.00 24.04  ? 295 ASN A CB    1 
ATOM   2307 C CG    . ASN A 1 302 ? 21.655  2.361   33.240  1.00 29.50  ? 295 ASN A CG    1 
ATOM   2308 O OD1   . ASN A 1 302 ? 21.560  2.160   32.035  1.00 27.94  ? 295 ASN A OD1   1 
ATOM   2309 N ND2   . ASN A 1 302 ? 22.611  1.828   33.992  1.00 32.52  ? 295 ASN A ND2   1 
ATOM   2310 N N     . PRO A 1 303 ? 19.198  3.572   30.743  1.00 24.56  ? 296 PRO A N     1 
ATOM   2311 C CA    . PRO A 1 303 ? 18.337  2.892   29.771  1.00 25.64  ? 296 PRO A CA    1 
ATOM   2312 C C     . PRO A 1 303 ? 18.429  1.354   29.842  1.00 28.04  ? 296 PRO A C     1 
ATOM   2313 O O     . PRO A 1 303 ? 17.473  0.678   29.464  1.00 25.15  ? 296 PRO A O     1 
ATOM   2314 C CB    . PRO A 1 303 ? 18.787  3.429   28.388  1.00 24.94  ? 296 PRO A CB    1 
ATOM   2315 C CG    . PRO A 1 303 ? 20.076  4.167   28.635  1.00 27.16  ? 296 PRO A CG    1 
ATOM   2316 C CD    . PRO A 1 303 ? 20.109  4.531   30.111  1.00 25.12  ? 296 PRO A CD    1 
ATOM   2317 N N     . HIS A 1 304 ? 19.558  0.811   30.310  1.00 27.85  ? 297 HIS A N     1 
ATOM   2318 C CA    . HIS A 1 304 ? 19.774  -0.655  30.488  1.00 27.25  ? 297 HIS A CA    1 
ATOM   2319 C C     . HIS A 1 304 ? 18.919  -1.186  31.638  1.00 28.55  ? 297 HIS A C     1 
ATOM   2320 O O     . HIS A 1 304 ? 18.549  -2.352  31.594  1.00 32.10  ? 297 HIS A O     1 
ATOM   2321 C CB    . HIS A 1 304 ? 21.266  -0.978  30.671  1.00 32.16  ? 297 HIS A CB    1 
ATOM   2322 C CG    . HIS A 1 304 ? 22.117  -0.495  29.546  1.00 36.82  ? 297 HIS A CG    1 
ATOM   2323 N ND1   . HIS A 1 304 ? 22.899  0.640   29.652  1.00 43.42  ? 297 HIS A ND1   1 
ATOM   2324 C CD2   . HIS A 1 304 ? 22.286  -0.954  28.287  1.00 40.03  ? 297 HIS A CD2   1 
ATOM   2325 C CE1   . HIS A 1 304 ? 23.547  0.833   28.526  1.00 41.99  ? 297 HIS A CE1   1 
ATOM   2326 N NE2   . HIS A 1 304 ? 23.181  -0.117  27.672  1.00 42.27  ? 297 HIS A NE2   1 
ATOM   2327 N N     . LYS A 1 305 ? 18.540  -0.358  32.607  1.00 24.62  ? 298 LYS A N     1 
ATOM   2328 C CA    . LYS A 1 305 ? 17.683  -0.796  33.733  1.00 26.33  ? 298 LYS A CA    1 
ATOM   2329 C C     . LYS A 1 305 ? 16.214  -0.444  33.470  1.00 23.03  ? 298 LYS A C     1 
ATOM   2330 O O     . LYS A 1 305 ? 15.367  -0.916  34.200  1.00 25.32  ? 298 LYS A O     1 
ATOM   2331 C CB    . LYS A 1 305 ? 18.179  -0.178  35.032  1.00 28.31  ? 298 LYS A CB    1 
ATOM   2332 C CG    . LYS A 1 305 ? 19.606  -0.562  35.411  1.00 33.95  ? 298 LYS A CG    1 
ATOM   2333 C CD    . LYS A 1 305 ? 20.012  0.122   36.677  1.00 37.82  ? 298 LYS A CD    1 
ATOM   2334 C CE    . LYS A 1 305 ? 21.436  -0.168  37.122  1.00 42.88  ? 298 LYS A CE    1 
ATOM   2335 N NZ    . LYS A 1 305 ? 21.837  0.791   38.185  1.00 47.80  ? 298 LYS A NZ    1 
ATOM   2336 N N     . ARG A 1 306 ? 15.928  0.302   32.420  1.00 23.18  ? 299 ARG A N     1 
ATOM   2337 C CA    . ARG A 1 306 ? 14.565  0.830   32.164  1.00 21.88  ? 299 ARG A CA    1 
ATOM   2338 C C     . ARG A 1 306 ? 13.674  -0.347  31.773  1.00 22.25  ? 299 ARG A C     1 
ATOM   2339 O O     . ARG A 1 306 ? 14.163  -1.216  31.068  1.00 22.35  ? 299 ARG A O     1 
ATOM   2340 C CB    . ARG A 1 306 ? 14.633  1.902   31.087  1.00 21.80  ? 299 ARG A CB    1 
ATOM   2341 C CG    . ARG A 1 306 ? 13.386  2.774   30.956  1.00 21.07  ? 299 ARG A CG    1 
ATOM   2342 C CD    . ARG A 1 306 ? 13.640  3.953   30.014  1.00 20.53  ? 299 ARG A CD    1 
ATOM   2343 N NE    . ARG A 1 306 ? 14.715  4.828   30.460  1.00 20.18  ? 299 ARG A NE    1 
ATOM   2344 C CZ    . ARG A 1 306 ? 15.515  5.515   29.676  1.00 18.90  ? 299 ARG A CZ    1 
ATOM   2345 N NH1   . ARG A 1 306 ? 15.382  5.447   28.373  1.00 19.61  ? 299 ARG A NH1   1 
ATOM   2346 N NH2   . ARG A 1 306 ? 16.506  6.216   30.183  1.00 20.89  ? 299 ARG A NH2   1 
ATOM   2347 N N     . ILE A 1 307 ? 12.416  -0.340  32.176  1.00 21.23  ? 300 ILE A N     1 
ATOM   2348 C CA    . ILE A 1 307 ? 11.493  -1.470  31.928  1.00 19.92  ? 300 ILE A CA    1 
ATOM   2349 C C     . ILE A 1 307 ? 11.275  -1.539  30.409  1.00 20.47  ? 300 ILE A C     1 
ATOM   2350 O O     . ILE A 1 307 ? 11.265  -0.480  29.747  1.00 22.78  ? 300 ILE A O     1 
ATOM   2351 C CB    . ILE A 1 307 ? 10.211  -1.328  32.749  1.00 20.66  ? 300 ILE A CB    1 
ATOM   2352 C CG1   . ILE A 1 307 ? 9.357   -2.603  32.701  1.00 22.00  ? 300 ILE A CG1   1 
ATOM   2353 C CG2   . ILE A 1 307 ? 9.424   -0.097  32.341  1.00 19.72  ? 300 ILE A CG2   1 
ATOM   2354 C CD1   . ILE A 1 307 ? 8.213   -2.565  33.679  1.00 21.67  ? 300 ILE A CD1   1 
ATOM   2355 N N     . GLU A 1 308 ? 11.119  -2.744  29.874  1.00 20.35  ? 301 GLU A N     1 
ATOM   2356 C CA    . GLU A 1 308 ? 10.781  -2.943  28.443  1.00 21.68  ? 301 GLU A CA    1 
ATOM   2357 C C     . GLU A 1 308 ? 9.279   -3.104  28.259  1.00 19.68  ? 301 GLU A C     1 
ATOM   2358 O O     . GLU A 1 308 ? 8.569   -3.267  29.230  1.00 19.67  ? 301 GLU A O     1 
ATOM   2359 C CB    . GLU A 1 308 ? 11.508  -4.158  27.893  1.00 27.78  ? 301 GLU A CB    1 
ATOM   2360 C CG    . GLU A 1 308 ? 12.975  -3.864  27.840  1.00 30.64  ? 301 GLU A CG    1 
ATOM   2361 C CD    . GLU A 1 308 ? 13.772  -4.886  27.084  1.00 40.10  ? 301 GLU A CD    1 
ATOM   2362 O OE1   . GLU A 1 308 ? 13.145  -5.822  26.547  1.00 43.67  ? 301 GLU A OE1   1 
ATOM   2363 O OE2   . GLU A 1 308 ? 15.027  -4.728  27.045  1.00 49.35  ? 301 GLU A OE2   1 
ATOM   2364 N N     . VAL A 1 309 ? 8.824   -2.960  27.024  1.00 17.55  ? 302 VAL A N     1 
ATOM   2365 C CA    . VAL A 1 309 ? 7.376   -2.806  26.737  1.00 18.44  ? 302 VAL A CA    1 
ATOM   2366 C C     . VAL A 1 309 ? 6.638   -4.038  27.261  1.00 19.25  ? 302 VAL A C     1 
ATOM   2367 O O     . VAL A 1 309 ? 5.589   -3.859  27.898  1.00 18.29  ? 302 VAL A O     1 
ATOM   2368 C CB    . VAL A 1 309 ? 7.085   -2.507  25.255  1.00 19.43  ? 302 VAL A CB    1 
ATOM   2369 C CG1   . VAL A 1 309 ? 7.465   -3.604  24.300  1.00 23.73  ? 302 VAL A CG1   1 
ATOM   2370 C CG2   . VAL A 1 309 ? 5.613   -2.183  25.078  1.00 19.97  ? 302 VAL A CG2   1 
ATOM   2371 N N     . GLU A 1 310 ? 7.202   -5.235  27.073  1.00 20.93  ? 303 GLU A N     1 
ATOM   2372 C CA    . GLU A 1 310 ? 6.505   -6.479  27.494  1.00 25.18  ? 303 GLU A CA    1 
ATOM   2373 C C     . GLU A 1 310 ? 6.438   -6.571  29.022  1.00 23.85  ? 303 GLU A C     1 
ATOM   2374 O O     . GLU A 1 310 ? 5.397   -7.040  29.542  1.00 22.14  ? 303 GLU A O     1 
ATOM   2375 C CB    . GLU A 1 310 ? 7.128   -7.691  26.811  1.00 30.36  ? 303 GLU A CB    1 
ATOM   2376 C CG    . GLU A 1 310 ? 6.621   -7.817  25.401  1.00 34.64  ? 303 GLU A CG    1 
ATOM   2377 C CD    . GLU A 1 310 ? 7.591   -8.401  24.398  1.00 49.53  ? 303 GLU A CD    1 
ATOM   2378 O OE1   . GLU A 1 310 ? 7.694   -9.667  24.313  1.00 47.64  ? 303 GLU A OE1   1 
ATOM   2379 O OE2   . GLU A 1 310 ? 8.225   -7.587  23.692  1.00 58.12  ? 303 GLU A OE2   1 
ATOM   2380 N N     . GLN A 1 311 ? 7.459   -6.100  29.735  1.00 21.78  ? 304 GLN A N     1 
ATOM   2381 C CA    . GLN A 1 311 ? 7.425   -6.102  31.210  1.00 22.52  ? 304 GLN A CA    1 
ATOM   2382 C C     . GLN A 1 311 ? 6.412   -5.080  31.673  1.00 21.26  ? 304 GLN A C     1 
ATOM   2383 O O     . GLN A 1 311 ? 5.746   -5.347  32.654  1.00 19.89  ? 304 GLN A O     1 
ATOM   2384 C CB    . GLN A 1 311 ? 8.778   -5.784  31.803  1.00 25.16  ? 304 GLN A CB    1 
ATOM   2385 C CG    . GLN A 1 311 ? 9.858   -6.781  31.483  1.00 28.12  ? 304 GLN A CG    1 
ATOM   2386 C CD    . GLN A 1 311 ? 11.169  -6.162  31.915  1.00 29.39  ? 304 GLN A CD    1 
ATOM   2387 O OE1   . GLN A 1 311 ? 11.685  -5.226  31.299  1.00 28.29  ? 304 GLN A OE1   1 
ATOM   2388 N NE2   . GLN A 1 311 ? 11.677  -6.654  33.026  1.00 25.97  ? 304 GLN A NE2   1 
ATOM   2389 N N     . ALA A 1 312 ? 6.315   -3.922  31.001  1.00 20.87  ? 305 ALA A N     1 
ATOM   2390 C CA    . ALA A 1 312 ? 5.338   -2.881  31.379  1.00 19.44  ? 305 ALA A CA    1 
ATOM   2391 C C     . ALA A 1 312 ? 3.912   -3.437  31.272  1.00 19.44  ? 305 ALA A C     1 
ATOM   2392 O O     . ALA A 1 312 ? 3.097   -3.230  32.205  1.00 21.28  ? 305 ALA A O     1 
ATOM   2393 C CB    . ALA A 1 312 ? 5.518   -1.640  30.541  1.00 19.47  ? 305 ALA A CB    1 
ATOM   2394 N N     . LEU A 1 313 ? 3.593   -4.165  30.198  1.00 18.20  ? 306 LEU A N     1 
ATOM   2395 C CA    . LEU A 1 313 ? 2.246   -4.715  30.024  1.00 18.02  ? 306 LEU A CA    1 
ATOM   2396 C C     . LEU A 1 313 ? 1.879   -5.634  31.202  1.00 18.51  ? 306 LEU A C     1 
ATOM   2397 O O     . LEU A 1 313 ? 0.682   -5.655  31.539  1.00 20.19  ? 306 LEU A O     1 
ATOM   2398 C CB    . LEU A 1 313 ? 2.166   -5.411  28.674  1.00 19.10  ? 306 LEU A CB    1 
ATOM   2399 C CG    . LEU A 1 313 ? 2.023   -4.437  27.503  1.00 19.34  ? 306 LEU A CG    1 
ATOM   2400 C CD1   . LEU A 1 313 ? 2.318   -5.100  26.183  1.00 21.28  ? 306 LEU A CD1   1 
ATOM   2401 C CD2   . LEU A 1 313 ? 0.636   -3.832  27.498  1.00 20.77  ? 306 LEU A CD2   1 
ATOM   2402 N N     . ALA A 1 314 ? 2.844   -6.422  31.699  1.00 21.48  ? 307 ALA A N     1 
ATOM   2403 C CA    . ALA A 1 314 ? 2.713   -7.440  32.770  1.00 20.21  ? 307 ALA A CA    1 
ATOM   2404 C C     . ALA A 1 314 ? 2.730   -6.794  34.164  1.00 23.24  ? 307 ALA A C     1 
ATOM   2405 O O     . ALA A 1 314 ? 2.550   -7.507  35.179  1.00 23.23  ? 307 ALA A O     1 
ATOM   2406 C CB    . ALA A 1 314 ? 3.830   -8.446  32.607  1.00 22.67  ? 307 ALA A CB    1 
ATOM   2407 N N     . HIS A 1 315 ? 2.904   -5.484  34.266  1.00 21.08  ? 308 HIS A N     1 
ATOM   2408 C CA    . HIS A 1 315 ? 2.920   -4.790  35.576  1.00 20.55  ? 308 HIS A CA    1 
ATOM   2409 C C     . HIS A 1 315 ? 1.542   -4.854  36.242  1.00 21.95  ? 308 HIS A C     1 
ATOM   2410 O O     . HIS A 1 315 ? 0.493   -4.727  35.585  1.00 20.18  ? 308 HIS A O     1 
ATOM   2411 C CB    . HIS A 1 315 ? 3.376   -3.352  35.409  1.00 21.41  ? 308 HIS A CB    1 
ATOM   2412 C CG    . HIS A 1 315 ? 3.686   -2.699  36.713  1.00 22.24  ? 308 HIS A CG    1 
ATOM   2413 N ND1   . HIS A 1 315 ? 2.724   -2.118  37.471  1.00 23.00  ? 308 HIS A ND1   1 
ATOM   2414 C CD2   . HIS A 1 315 ? 4.857   -2.547  37.362  1.00 22.62  ? 308 HIS A CD2   1 
ATOM   2415 C CE1   . HIS A 1 315 ? 3.271   -1.632  38.574  1.00 23.11  ? 308 HIS A CE1   1 
ATOM   2416 N NE2   . HIS A 1 315 ? 4.610   -1.841  38.508  1.00 24.96  ? 308 HIS A NE2   1 
ATOM   2417 N N     . PRO A 1 316 ? 1.491   -5.011  37.589  1.00 22.95  ? 309 PRO A N     1 
ATOM   2418 C CA    . PRO A 1 316 ? 0.224   -5.000  38.328  1.00 23.65  ? 309 PRO A CA    1 
ATOM   2419 C C     . PRO A 1 316 ? -0.742  -3.847  38.053  1.00 22.77  ? 309 PRO A C     1 
ATOM   2420 O O     . PRO A 1 316 ? -1.961  -4.043  38.064  1.00 21.78  ? 309 PRO A O     1 
ATOM   2421 C CB    . PRO A 1 316 ? 0.700   -4.976  39.790  1.00 25.24  ? 309 PRO A CB    1 
ATOM   2422 C CG    . PRO A 1 316 ? 1.947   -5.802  39.750  1.00 25.72  ? 309 PRO A CG    1 
ATOM   2423 C CD    . PRO A 1 316 ? 2.625   -5.346  38.468  1.00 25.74  ? 309 PRO A CD    1 
ATOM   2424 N N     . TYR A 1 317 ? -0.234  -2.671  37.697  1.00 21.80  ? 310 TYR A N     1 
ATOM   2425 C CA    . TYR A 1 317 ? -1.140  -1.563  37.361  1.00 22.96  ? 310 TYR A CA    1 
ATOM   2426 C C     . TYR A 1 317 ? -2.089  -1.986  36.242  1.00 22.63  ? 310 TYR A C     1 
ATOM   2427 O O     . TYR A 1 317 ? -3.242  -1.477  36.235  1.00 23.43  ? 310 TYR A O     1 
ATOM   2428 C CB    . TYR A 1 317 ? -0.361  -0.287  37.003  1.00 21.43  ? 310 TYR A CB    1 
ATOM   2429 C CG    . TYR A 1 317 ? -1.261  0.894   36.725  1.00 23.87  ? 310 TYR A CG    1 
ATOM   2430 C CD1   . TYR A 1 317 ? -2.186  1.322   37.671  1.00 23.35  ? 310 TYR A CD1   1 
ATOM   2431 C CD2   . TYR A 1 317 ? -1.153  1.629   35.557  1.00 21.70  ? 310 TYR A CD2   1 
ATOM   2432 C CE1   . TYR A 1 317 ? -3.011  2.413   37.450  1.00 22.34  ? 310 TYR A CE1   1 
ATOM   2433 C CE2   . TYR A 1 317 ? -1.940  2.749   35.339  1.00 23.62  ? 310 TYR A CE2   1 
ATOM   2434 C CZ    . TYR A 1 317 ? -2.880  3.132   36.278  1.00 24.66  ? 310 TYR A CZ    1 
ATOM   2435 O OH    . TYR A 1 317 ? -3.679  4.202   36.027  1.00 24.68  ? 310 TYR A OH    1 
ATOM   2436 N N     . LEU A 1 318 ? -1.611  -2.816  35.290  1.00 22.91  ? 311 LEU A N     1 
ATOM   2437 C CA    . LEU A 1 318 ? -2.359  -3.111  34.035  1.00 20.72  ? 311 LEU A CA    1 
ATOM   2438 C C     . LEU A 1 318 ? -3.024  -4.494  34.085  1.00 21.73  ? 311 LEU A C     1 
ATOM   2439 O O     . LEU A 1 318 ? -3.433  -4.937  33.038  1.00 21.17  ? 311 LEU A O     1 
ATOM   2440 C CB    . LEU A 1 318 ? -1.409  -3.009  32.844  1.00 21.72  ? 311 LEU A CB    1 
ATOM   2441 C CG    . LEU A 1 318 ? -0.884  -1.590  32.592  1.00 22.37  ? 311 LEU A CG    1 
ATOM   2442 C CD1   . LEU A 1 318 ? 0.054   -1.568  31.436  1.00 25.84  ? 311 LEU A CD1   1 
ATOM   2443 C CD2   . LEU A 1 318 ? -2.014  -0.608  32.351  1.00 24.14  ? 311 LEU A CD2   1 
ATOM   2444 N N     . GLU A 1 319 ? -3.172  -5.109  35.260  1.00 23.70  ? 312 GLU A N     1 
ATOM   2445 C CA    . GLU A 1 319 ? -3.618  -6.533  35.390  1.00 27.26  ? 312 GLU A CA    1 
ATOM   2446 C C     . GLU A 1 319 ? -5.071  -6.691  34.921  1.00 27.62  ? 312 GLU A C     1 
ATOM   2447 O O     . GLU A 1 319 ? -5.403  -7.774  34.448  1.00 27.22  ? 312 GLU A O     1 
ATOM   2448 C CB    . GLU A 1 319 ? -3.386  -7.069  36.813  1.00 30.60  ? 312 GLU A CB    1 
ATOM   2449 C CG    . GLU A 1 319 ? -4.025  -6.265  37.921  1.00 38.06  ? 312 GLU A CG    1 
ATOM   2450 C CD    . GLU A 1 319 ? -3.406  -6.548  39.291  1.00 45.27  ? 312 GLU A CD    1 
ATOM   2451 O OE1   . GLU A 1 319 ? -3.102  -7.761  39.535  1.00 45.89  ? 312 GLU A OE1   1 
ATOM   2452 O OE2   . GLU A 1 319 ? -3.159  -5.556  40.078  1.00 36.97  ? 312 GLU A OE2   1 
ATOM   2453 N N     . GLN A 1 320 ? -5.914  -5.655  34.933  1.00 26.54  ? 313 GLN A N     1 
ATOM   2454 C CA    . GLN A 1 320 ? -7.308  -5.806  34.422  1.00 25.76  ? 313 GLN A CA    1 
ATOM   2455 C C     . GLN A 1 320 ? -7.298  -5.999  32.906  1.00 26.02  ? 313 GLN A C     1 
ATOM   2456 O O     . GLN A 1 320 ? -8.272  -6.549  32.381  1.00 22.75  ? 313 GLN A O     1 
ATOM   2457 C CB    . GLN A 1 320 ? -8.189  -4.615  34.785  1.00 30.16  ? 313 GLN A CB    1 
ATOM   2458 C CG    . GLN A 1 320 ? -8.314  -4.402  36.281  1.00 35.13  ? 313 GLN A CG    1 
ATOM   2459 C CD    . GLN A 1 320 ? -8.745  -2.992  36.592  1.00 39.43  ? 313 GLN A CD    1 
ATOM   2460 O OE1   . GLN A 1 320 ? -8.192  -2.008  36.077  1.00 36.63  ? 313 GLN A OE1   1 
ATOM   2461 N NE2   . GLN A 1 320 ? -9.781  -2.894  37.403  1.00 42.71  ? 313 GLN A NE2   1 
ATOM   2462 N N     . TYR A 1 321 ? -6.243  -5.579  32.205  1.00 22.50  ? 314 TYR A N     1 
ATOM   2463 C CA    . TYR A 1 321 ? -6.226  -5.591  30.722  1.00 24.11  ? 314 TYR A CA    1 
ATOM   2464 C C     . TYR A 1 321 ? -5.267  -6.671  30.181  1.00 22.68  ? 314 TYR A C     1 
ATOM   2465 O O     . TYR A 1 321 ? -5.421  -7.157  29.028  1.00 18.86  ? 314 TYR A O     1 
ATOM   2466 C CB    . TYR A 1 321 ? -5.838  -4.195  30.216  1.00 24.59  ? 314 TYR A CB    1 
ATOM   2467 C CG    . TYR A 1 321 ? -6.820  -3.116  30.597  1.00 26.76  ? 314 TYR A CG    1 
ATOM   2468 C CD1   . TYR A 1 321 ? -8.039  -2.977  29.961  1.00 30.28  ? 314 TYR A CD1   1 
ATOM   2469 C CD2   . TYR A 1 321 ? -6.539  -2.277  31.659  1.00 27.69  ? 314 TYR A CD2   1 
ATOM   2470 C CE1   . TYR A 1 321 ? -8.967  -2.040  30.396  1.00 32.85  ? 314 TYR A CE1   1 
ATOM   2471 C CE2   . TYR A 1 321 ? -7.429  -1.311  32.076  1.00 28.87  ? 314 TYR A CE2   1 
ATOM   2472 C CZ    . TYR A 1 321 ? -8.647  -1.202  31.452  1.00 30.40  ? 314 TYR A CZ    1 
ATOM   2473 O OH    . TYR A 1 321 ? -9.468  -0.236  31.943  1.00 38.22  ? 314 TYR A OH    1 
ATOM   2474 N N     . TYR A 1 322 ? -4.230  -6.980  30.944  1.00 25.12  ? 315 TYR A N     1 
ATOM   2475 C CA    . TYR A 1 322 ? -3.049  -7.729  30.438  1.00 24.57  ? 315 TYR A CA    1 
ATOM   2476 C C     . TYR A 1 322 ? -3.491  -9.091  29.925  1.00 25.47  ? 315 TYR A C     1 
ATOM   2477 O O     . TYR A 1 322 ? -4.111  -9.853  30.690  1.00 23.24  ? 315 TYR A O     1 
ATOM   2478 C CB    . TYR A 1 322 ? -2.009  -7.952  31.534  1.00 23.52  ? 315 TYR A CB    1 
ATOM   2479 C CG    . TYR A 1 322 ? -0.794  -8.731  31.101  1.00 22.16  ? 315 TYR A CG    1 
ATOM   2480 C CD1   . TYR A 1 322 ? -0.074  -8.389  29.966  1.00 22.92  ? 315 TYR A CD1   1 
ATOM   2481 C CD2   . TYR A 1 322 ? -0.295  -9.756  31.891  1.00 22.39  ? 315 TYR A CD2   1 
ATOM   2482 C CE1   . TYR A 1 322 ? 1.076   -9.079  29.599  1.00 22.11  ? 315 TYR A CE1   1 
ATOM   2483 C CE2   . TYR A 1 322 ? 0.853   -10.456 31.538  1.00 22.47  ? 315 TYR A CE2   1 
ATOM   2484 C CZ    . TYR A 1 322 ? 1.523   -10.142 30.375  1.00 22.84  ? 315 TYR A CZ    1 
ATOM   2485 O OH    . TYR A 1 322 ? 2.664   -10.817 30.030  1.00 23.98  ? 315 TYR A OH    1 
ATOM   2486 N N     . ASP A 1 323 ? -3.178  -9.367  28.673  1.00 22.89  ? 316 ASP A N     1 
ATOM   2487 C CA    . ASP A 1 323 ? -3.490  -10.655 28.014  1.00 24.50  ? 316 ASP A CA    1 
ATOM   2488 C C     . ASP A 1 323 ? -2.530  -10.794 26.839  1.00 21.37  ? 316 ASP A C     1 
ATOM   2489 O O     . ASP A 1 323 ? -2.786  -10.292 25.761  1.00 20.95  ? 316 ASP A O     1 
ATOM   2490 C CB    . ASP A 1 323 ? -4.974  -10.715 27.644  1.00 24.93  ? 316 ASP A CB    1 
ATOM   2491 C CG    . ASP A 1 323 ? -5.350  -11.943 26.826  1.00 26.56  ? 316 ASP A CG    1 
ATOM   2492 O OD1   . ASP A 1 323 ? -4.498  -12.832 26.681  1.00 28.59  ? 316 ASP A OD1   1 
ATOM   2493 O OD2   . ASP A 1 323 ? -6.464  -11.945 26.261  1.00 28.63  ? 316 ASP A OD2   1 
ATOM   2494 N N     . PRO A 1 324 ? -1.380  -11.468 27.000  1.00 23.01  ? 317 PRO A N     1 
ATOM   2495 C CA    . PRO A 1 324 ? -0.347  -11.426 25.964  1.00 22.16  ? 317 PRO A CA    1 
ATOM   2496 C C     . PRO A 1 324 ? -0.782  -12.155 24.682  1.00 22.90  ? 317 PRO A C     1 
ATOM   2497 O O     . PRO A 1 324 ? -0.328  -11.800 23.636  1.00 22.02  ? 317 PRO A O     1 
ATOM   2498 C CB    . PRO A 1 324 ? 0.884   -12.091 26.598  1.00 25.30  ? 317 PRO A CB    1 
ATOM   2499 C CG    . PRO A 1 324 ? 0.487   -12.511 27.987  1.00 24.80  ? 317 PRO A CG    1 
ATOM   2500 C CD    . PRO A 1 324 ? -0.967  -12.168 28.222  1.00 24.26  ? 317 PRO A CD    1 
ATOM   2501 N N     . SER A 1 325 ? -1.727  -13.100 24.769  1.00 20.95  ? 318 SER A N     1 
ATOM   2502 C CA    A SER A 1 325 ? -2.382  -13.712 23.581  0.50 19.35  ? 318 SER A CA    1 
ATOM   2503 C CA    B SER A 1 325 ? -2.392  -13.701 23.581  0.50 21.50  ? 318 SER A CA    1 
ATOM   2504 C C     . SER A 1 325 ? -3.146  -12.654 22.764  1.00 20.76  ? 318 SER A C     1 
ATOM   2505 O O     . SER A 1 325 ? -3.402  -12.935 21.565  1.00 21.93  ? 318 SER A O     1 
ATOM   2506 C CB    A SER A 1 325 ? -3.285  -14.895 23.972  0.50 18.28  ? 318 SER A CB    1 
ATOM   2507 C CB    B SER A 1 325 ? -3.354  -14.789 23.962  0.50 23.01  ? 318 SER A CB    1 
ATOM   2508 O OG    A SER A 1 325 ? -4.500  -14.466 24.596  0.50 14.91  ? 318 SER A OG    1 
ATOM   2509 O OG    B SER A 1 325 ? -2.646  -15.903 24.417  0.50 24.48  ? 318 SER A OG    1 
ATOM   2510 N N     . ASP A 1 326 ? -3.550  -11.548 23.387  1.00 20.44  ? 319 ASP A N     1 
ATOM   2511 C CA    . ASP A 1 326 ? -4.338  -10.488 22.741  1.00 22.12  ? 319 ASP A CA    1 
ATOM   2512 C C     . ASP A 1 326 ? -3.493  -9.216  22.559  1.00 22.24  ? 319 ASP A C     1 
ATOM   2513 O O     . ASP A 1 326 ? -4.098  -8.121  22.400  1.00 21.70  ? 319 ASP A O     1 
ATOM   2514 C CB    . ASP A 1 326 ? -5.577  -10.174 23.566  1.00 24.00  ? 319 ASP A CB    1 
ATOM   2515 C CG    . ASP A 1 326 ? -6.609  -9.384  22.793  1.00 27.30  ? 319 ASP A CG    1 
ATOM   2516 O OD1   . ASP A 1 326 ? -6.677  -9.573  21.548  1.00 30.38  ? 319 ASP A OD1   1 
ATOM   2517 O OD2   . ASP A 1 326 ? -7.268  -8.538  23.430  1.00 29.89  ? 319 ASP A OD2   1 
ATOM   2518 N N     . GLU A 1 327 ? -2.172  -9.389  22.569  1.00 19.85  ? 320 GLU A N     1 
ATOM   2519 C CA    . GLU A 1 327 ? -1.170  -8.302  22.389  1.00 21.47  ? 320 GLU A CA    1 
ATOM   2520 C C     . GLU A 1 327 ? -0.259  -8.784  21.285  1.00 19.77  ? 320 GLU A C     1 
ATOM   2521 O O     . GLU A 1 327 ? 0.831   -9.276  21.522  1.00 21.26  ? 320 GLU A O     1 
ATOM   2522 C CB    . GLU A 1 327 ? -0.493  -7.977  23.719  1.00 20.44  ? 320 GLU A CB    1 
ATOM   2523 C CG    . GLU A 1 327 ? -1.463  -7.430  24.768  1.00 20.23  ? 320 GLU A CG    1 
ATOM   2524 C CD    . GLU A 1 327 ? -1.038  -7.635  26.204  1.00 19.55  ? 320 GLU A CD    1 
ATOM   2525 O OE1   . GLU A 1 327 ? 0.100   -8.112  26.428  1.00 20.95  ? 320 GLU A OE1   1 
ATOM   2526 O OE2   . GLU A 1 327 ? -1.865  -7.349  27.078  1.00 21.79  ? 320 GLU A OE2   1 
ATOM   2527 N N     . PRO A 1 328 ? -0.723  -8.679  20.044  1.00 19.99  ? 321 PRO A N     1 
ATOM   2528 C CA    . PRO A 1 328 ? -0.019  -9.268  18.918  1.00 22.18  ? 321 PRO A CA    1 
ATOM   2529 C C     . PRO A 1 328 ? 1.299   -8.564  18.593  1.00 23.61  ? 321 PRO A C     1 
ATOM   2530 O O     . PRO A 1 328 ? 1.463   -7.342  18.891  1.00 22.60  ? 321 PRO A O     1 
ATOM   2531 C CB    . PRO A 1 328 ? -0.985  -9.080  17.731  1.00 24.58  ? 321 PRO A CB    1 
ATOM   2532 C CG    . PRO A 1 328 ? -1.937  -8.007  18.157  1.00 25.02  ? 321 PRO A CG    1 
ATOM   2533 C CD    . PRO A 1 328 ? -2.003  -8.074  19.669  1.00 23.15  ? 321 PRO A CD    1 
ATOM   2534 N N     . ILE A 1 329 ? 2.186   -9.336  17.978  1.00 21.18  ? 322 ILE A N     1 
ATOM   2535 C CA    . ILE A 1 329 ? 3.490   -8.868  17.450  1.00 23.12  ? 322 ILE A CA    1 
ATOM   2536 C C     . ILE A 1 329 ? 3.406   -8.894  15.922  1.00 23.35  ? 322 ILE A C     1 
ATOM   2537 O O     . ILE A 1 329 ? 2.499   -9.529  15.387  1.00 23.36  ? 322 ILE A O     1 
ATOM   2538 C CB    . ILE A 1 329 ? 4.648   -9.694  18.023  1.00 24.67  ? 322 ILE A CB    1 
ATOM   2539 C CG1   . ILE A 1 329 ? 4.614   -11.175 17.633  1.00 24.81  ? 322 ILE A CG1   1 
ATOM   2540 C CG2   . ILE A 1 329 ? 4.699   -9.555  19.533  1.00 27.68  ? 322 ILE A CG2   1 
ATOM   2541 C CD1   . ILE A 1 329 ? 5.901   -11.912 18.034  1.00 27.51  ? 322 ILE A CD1   1 
ATOM   2542 N N     . ALA A 1 330 ? 4.337   -8.221  15.271  1.00 22.10  ? 323 ALA A N     1 
ATOM   2543 C CA    . ALA A 1 330 ? 4.418   -8.034  13.810  1.00 23.54  ? 323 ALA A CA    1 
ATOM   2544 C C     . ALA A 1 330 ? 4.856   -9.337  13.124  1.00 26.40  ? 323 ALA A C     1 
ATOM   2545 O O     . ALA A 1 330 ? 5.760   -10.001 13.645  1.00 23.26  ? 323 ALA A O     1 
ATOM   2546 C CB    . ALA A 1 330 ? 5.408   -6.932  13.538  1.00 23.12  ? 323 ALA A CB    1 
ATOM   2547 N N     . GLU A 1 331 ? 4.243   -9.665  11.993  1.00 28.02  ? 324 GLU A N     1 
ATOM   2548 C CA    . GLU A 1 331 ? 4.598   -10.853 11.173  1.00 38.49  ? 324 GLU A CA    1 
ATOM   2549 C C     . GLU A 1 331 ? 5.936   -10.597 10.481  1.00 40.42  ? 324 GLU A C     1 
ATOM   2550 O O     . GLU A 1 331 ? 6.801   -11.478 10.546  1.00 43.58  ? 324 GLU A O     1 
ATOM   2551 C CB    . GLU A 1 331 ? 3.458   -11.125 10.192  1.00 40.83  ? 324 GLU A CB    1 
ATOM   2552 C CG    . GLU A 1 331 ? 2.202   -11.549 10.923  1.00 49.47  ? 324 GLU A CG    1 
ATOM   2553 C CD    . GLU A 1 331 ? 0.986   -11.765 10.053  1.00 55.26  ? 324 GLU A CD    1 
ATOM   2554 O OE1   . GLU A 1 331 ? 1.111   -11.534 8.831   1.00 59.08  ? 324 GLU A OE1   1 
ATOM   2555 O OE2   . GLU A 1 331 ? -0.079  -12.164 10.607  1.00 59.04  ? 324 GLU A OE2   1 
ATOM   2556 N N     . ALA A 1 332 ? 6.125   -9.376  9.961   1.00 42.85  ? 325 ALA A N     1 
ATOM   2557 C CA    . ALA A 1 332 ? 7.237   -8.989  9.065   1.00 42.70  ? 325 ALA A CA    1 
ATOM   2558 C C     . ALA A 1 332 ? 7.971   -7.780  9.639   1.00 42.67  ? 325 ALA A C     1 
ATOM   2559 O O     . ALA A 1 332 ? 7.692   -6.640  9.249   1.00 42.06  ? 325 ALA A O     1 
ATOM   2560 C CB    . ALA A 1 332 ? 6.673   -8.715  7.690   1.00 43.33  ? 325 ALA A CB    1 
ATOM   2561 N N     . PRO A 1 333 ? 8.902   -7.997  10.601  1.00 36.81  ? 326 PRO A N     1 
ATOM   2562 C CA    . PRO A 1 333 ? 9.804   -6.943  11.069  1.00 40.86  ? 326 PRO A CA    1 
ATOM   2563 C C     . PRO A 1 333 ? 10.639  -6.306  9.951   1.00 39.93  ? 326 PRO A C     1 
ATOM   2564 O O     . PRO A 1 333 ? 10.917  -6.977  8.983   1.00 34.10  ? 326 PRO A O     1 
ATOM   2565 C CB    . PRO A 1 333 ? 10.779  -7.646  12.020  1.00 41.79  ? 326 PRO A CB    1 
ATOM   2566 C CG    . PRO A 1 333 ? 10.056  -8.913  12.424  1.00 43.79  ? 326 PRO A CG    1 
ATOM   2567 C CD    . PRO A 1 333 ? 9.165   -9.282  11.257  1.00 39.45  ? 326 PRO A CD    1 
ATOM   2568 N N     . PHE A 1 334 ? 10.992  -5.032  10.112  1.00 36.14  ? 327 PHE A N     1 
ATOM   2569 C CA    . PHE A 1 334 ? 11.980  -4.321  9.269   1.00 40.90  ? 327 PHE A CA    1 
ATOM   2570 C C     . PHE A 1 334 ? 13.367  -4.825  9.685   1.00 49.77  ? 327 PHE A C     1 
ATOM   2571 O O     . PHE A 1 334 ? 13.755  -4.655  10.863  1.00 51.88  ? 327 PHE A O     1 
ATOM   2572 C CB    . PHE A 1 334 ? 11.814  -2.810  9.429   1.00 44.44  ? 327 PHE A CB    1 
ATOM   2573 C CG    . PHE A 1 334 ? 10.573  -2.253  8.785   1.00 42.51  ? 327 PHE A CG    1 
ATOM   2574 C CD1   . PHE A 1 334 ? 9.366   -2.240  9.459   1.00 40.37  ? 327 PHE A CD1   1 
ATOM   2575 C CD2   . PHE A 1 334 ? 10.608  -1.777  7.483   1.00 48.65  ? 327 PHE A CD2   1 
ATOM   2576 C CE1   . PHE A 1 334 ? 8.221   -1.749  8.857   1.00 42.74  ? 327 PHE A CE1   1 
ATOM   2577 C CE2   . PHE A 1 334 ? 9.458   -1.293  6.873   1.00 47.52  ? 327 PHE A CE2   1 
ATOM   2578 C CZ    . PHE A 1 334 ? 8.265   -1.280  7.565   1.00 46.43  ? 327 PHE A CZ    1 
ATOM   2579 N N     . LYS A 1 335 ? 14.076  -5.495  8.776   1.00 53.84  ? 328 LYS A N     1 
ATOM   2580 C CA    . LYS A 1 335 ? 15.370  -6.149  9.098   1.00 61.97  ? 328 LYS A CA    1 
ATOM   2581 C C     . LYS A 1 335 ? 16.483  -5.087  9.071   1.00 61.02  ? 328 LYS A C     1 
ATOM   2582 O O     . LYS A 1 335 ? 17.302  -5.064  10.003  1.00 62.14  ? 328 LYS A O     1 
ATOM   2583 C CB    . LYS A 1 335 ? 15.604  -7.345  8.165   1.00 67.11  ? 328 LYS A CB    1 
ATOM   2584 C CG    . LYS A 1 335 ? 16.260  -8.556  8.823   1.00 77.20  ? 328 LYS A CG    1 
ATOM   2585 C CD    . LYS A 1 335 ? 15.428  -9.219  9.925   1.00 85.13  ? 328 LYS A CD    1 
ATOM   2586 C CE    . LYS A 1 335 ? 16.252  -10.032 10.910  1.00 85.41  ? 328 LYS A CE    1 
ATOM   2587 N NZ    . LYS A 1 335 ? 15.508  -10.350 12.157  1.00 79.10  ? 328 LYS A NZ    1 
ATOM   2588 N N     . PHE A 1 336 ? 16.489  -4.201  8.076   1.00 58.89  ? 329 PHE A N     1 
ATOM   2589 C CA    . PHE A 1 336 ? 17.548  -3.177  7.882   1.00 64.77  ? 329 PHE A CA    1 
ATOM   2590 C C     . PHE A 1 336 ? 16.872  -1.812  7.767   1.00 62.24  ? 329 PHE A C     1 
ATOM   2591 O O     . PHE A 1 336 ? 15.675  -1.799  7.409   1.00 54.98  ? 329 PHE A O     1 
ATOM   2592 C CB    . PHE A 1 336 ? 18.381  -3.519  6.641   1.00 77.31  ? 329 PHE A CB    1 
ATOM   2593 C CG    . PHE A 1 336 ? 18.474  -4.992  6.319   1.00 87.68  ? 329 PHE A CG    1 
ATOM   2594 C CD1   . PHE A 1 336 ? 19.352  -5.819  7.006   1.00 92.57  ? 329 PHE A CD1   1 
ATOM   2595 C CD2   . PHE A 1 336 ? 17.680  -5.557  5.328   1.00 92.75  ? 329 PHE A CD2   1 
ATOM   2596 C CE1   . PHE A 1 336 ? 19.433  -7.173  6.712   1.00 96.88  ? 329 PHE A CE1   1 
ATOM   2597 C CE2   . PHE A 1 336 ? 17.767  -6.911  5.030   1.00 97.63  ? 329 PHE A CE2   1 
ATOM   2598 C CZ    . PHE A 1 336 ? 18.640  -7.718  5.726   1.00 98.90  ? 329 PHE A CZ    1 
ATOM   2599 N N     . ASP A 1 337 ? 17.591  -0.715  8.046   1.00 62.73  ? 330 ASP A N     1 
ATOM   2600 C CA    . ASP A 1 337 ? 17.016  0.655   7.922   1.00 65.34  ? 330 ASP A CA    1 
ATOM   2601 C C     . ASP A 1 337 ? 16.806  0.937   6.435   1.00 70.77  ? 330 ASP A C     1 
ATOM   2602 O O     . ASP A 1 337 ? 17.414  0.245   5.572   1.00 65.36  ? 330 ASP A O     1 
ATOM   2603 C CB    . ASP A 1 337 ? 17.837  1.776   8.583   1.00 63.29  ? 330 ASP A CB    1 
ATOM   2604 C CG    . ASP A 1 337 ? 17.042  2.699   9.518   1.00 66.12  ? 330 ASP A CG    1 
ATOM   2605 O OD1   . ASP A 1 337 ? 15.998  3.278   9.096   1.00 59.57  ? 330 ASP A OD1   1 
ATOM   2606 O OD2   . ASP A 1 337 ? 17.461  2.833   10.693  1.00 66.99  ? 330 ASP A OD2   1 
ATOM   2607 N N     . MET A 1 338 ? 15.943  1.911   6.177   1.00 71.62  ? 331 MET A N     1 
ATOM   2608 C CA    . MET A 1 338 ? 15.622  2.423   4.829   1.00 77.44  ? 331 MET A CA    1 
ATOM   2609 C C     . MET A 1 338 ? 16.689  3.476   4.488   1.00 81.67  ? 331 MET A C     1 
ATOM   2610 O O     . MET A 1 338 ? 16.707  4.548   5.134   1.00 92.49  ? 331 MET A O     1 
ATOM   2611 C CB    . MET A 1 338 ? 14.190  2.984   4.787   1.00 82.29  ? 331 MET A CB    1 
ATOM   2612 C CG    . MET A 1 338 ? 13.569  3.338   6.149   1.00 86.66  ? 331 MET A CG    1 
ATOM   2613 S SD    . MET A 1 338 ? 11.848  2.768   6.326   1.00 81.90  ? 331 MET A SD    1 
ATOM   2614 C CE    . MET A 1 338 ? 12.105  1.240   7.223   1.00 81.46  ? 331 MET A CE    1 
ATOM   2615 N N     . GLU A 1 339 ? 17.601  3.152   3.568   1.00 74.48  ? 332 GLU A N     1 
ATOM   2616 C CA    . GLU A 1 339 ? 18.777  3.999   3.227   1.00 78.31  ? 332 GLU A CA    1 
ATOM   2617 C C     . GLU A 1 339 ? 18.316  5.221   2.426   1.00 74.30  ? 332 GLU A C     1 
ATOM   2618 O O     . GLU A 1 339 ? 18.741  5.353   1.265   1.00 69.23  ? 332 GLU A O     1 
ATOM   2619 C CB    . GLU A 1 339 ? 19.797  3.227   2.389   1.00 83.48  ? 332 GLU A CB    1 
ATOM   2620 C CG    . GLU A 1 339 ? 20.306  1.953   3.029   1.00 88.65  ? 332 GLU A CG    1 
ATOM   2621 C CD    . GLU A 1 339 ? 21.325  1.255   2.149   1.00 92.53  ? 332 GLU A CD    1 
ATOM   2622 O OE1   . GLU A 1 339 ? 22.298  1.923   1.746   1.00 90.79  ? 332 GLU A OE1   1 
ATOM   2623 O OE2   . GLU A 1 339 ? 21.122  0.064   1.835   1.00 97.14  ? 332 GLU A OE2   1 
ATOM   2624 N N     . LEU A 1 340 ? 17.504  6.084   3.045   1.00 72.73  ? 333 LEU A N     1 
ATOM   2625 C CA    . LEU A 1 340 ? 16.869  7.282   2.424   1.00 68.14  ? 333 LEU A CA    1 
ATOM   2626 C C     . LEU A 1 340 ? 17.795  8.485   2.589   1.00 68.55  ? 333 LEU A C     1 
ATOM   2627 O O     . LEU A 1 340 ? 17.471  9.561   2.036   1.00 65.83  ? 333 LEU A O     1 
ATOM   2628 C CB    . LEU A 1 340 ? 15.535  7.571   3.129   1.00 61.06  ? 333 LEU A CB    1 
ATOM   2629 C CG    . LEU A 1 340 ? 14.300  6.839   2.605   1.00 57.26  ? 333 LEU A CG    1 
ATOM   2630 C CD1   . LEU A 1 340 ? 14.609  5.387   2.305   1.00 52.59  ? 333 LEU A CD1   1 
ATOM   2631 C CD2   . LEU A 1 340 ? 13.143  6.962   3.593   1.00 58.08  ? 333 LEU A CD2   1 
ATOM   2632 N N     . ASP A 1 341 ? 18.877  8.304   3.354   1.00 70.88  ? 334 ASP A N     1 
ATOM   2633 C CA    . ASP A 1 341 ? 19.661  9.396   3.988   1.00 72.82  ? 334 ASP A CA    1 
ATOM   2634 C C     . ASP A 1 341 ? 20.030  10.432  2.929   1.00 67.69  ? 334 ASP A C     1 
ATOM   2635 O O     . ASP A 1 341 ? 19.784  11.626  3.166   1.00 66.76  ? 334 ASP A O     1 
ATOM   2636 C CB    . ASP A 1 341 ? 20.911  8.844   4.678   1.00 78.30  ? 334 ASP A CB    1 
ATOM   2637 C CG    . ASP A 1 341 ? 20.635  7.741   5.690   1.00 81.46  ? 334 ASP A CG    1 
ATOM   2638 O OD1   . ASP A 1 341 ? 19.443  7.392   5.893   1.00 75.41  ? 334 ASP A OD1   1 
ATOM   2639 O OD2   . ASP A 1 341 ? 21.619  7.233   6.267   1.00 87.51  ? 334 ASP A OD2   1 
ATOM   2640 N N     . ASP A 1 342 ? 20.584  9.978   1.802   1.00 67.13  ? 335 ASP A N     1 
ATOM   2641 C CA    . ASP A 1 342 ? 21.092  10.863  0.718   1.00 71.62  ? 335 ASP A CA    1 
ATOM   2642 C C     . ASP A 1 342 ? 20.554  10.358  -0.626  1.00 70.58  ? 335 ASP A C     1 
ATOM   2643 O O     . ASP A 1 342 ? 21.365  10.080  -1.537  1.00 66.90  ? 335 ASP A O     1 
ATOM   2644 C CB    . ASP A 1 342 ? 22.623  10.965  0.766   1.00 80.93  ? 335 ASP A CB    1 
ATOM   2645 C CG    . ASP A 1 342 ? 23.303  9.651   1.111   1.00 80.63  ? 335 ASP A CG    1 
ATOM   2646 O OD1   . ASP A 1 342 ? 22.761  8.601   0.719   1.00 85.19  ? 335 ASP A OD1   1 
ATOM   2647 O OD2   . ASP A 1 342 ? 24.343  9.687   1.795   1.00 69.18  ? 335 ASP A OD2   1 
ATOM   2648 N N     . LEU A 1 343 ? 19.229  10.235  -0.742  1.00 60.05  ? 336 LEU A N     1 
ATOM   2649 C CA    . LEU A 1 343 ? 18.548  10.084  -2.054  1.00 53.66  ? 336 LEU A CA    1 
ATOM   2650 C C     . LEU A 1 343 ? 18.105  11.465  -2.514  1.00 44.29  ? 336 LEU A C     1 
ATOM   2651 O O     . LEU A 1 343 ? 17.584  12.239  -1.720  1.00 47.83  ? 336 LEU A O     1 
ATOM   2652 C CB    . LEU A 1 343 ? 17.357  9.131   -1.916  1.00 56.60  ? 336 LEU A CB    1 
ATOM   2653 C CG    . LEU A 1 343 ? 17.701  7.731   -1.419  1.00 54.97  ? 336 LEU A CG    1 
ATOM   2654 C CD1   . LEU A 1 343 ? 16.499  6.812   -1.531  1.00 53.08  ? 336 LEU A CD1   1 
ATOM   2655 C CD2   . LEU A 1 343 ? 18.887  7.161   -2.183  1.00 60.09  ? 336 LEU A CD2   1 
ATOM   2656 N N     . PRO A 1 344 ? 18.298  11.818  -3.799  1.00 43.65  ? 337 PRO A N     1 
ATOM   2657 C CA    . PRO A 1 344 ? 17.771  13.072  -4.321  1.00 49.78  ? 337 PRO A CA    1 
ATOM   2658 C C     . PRO A 1 344 ? 16.250  13.015  -4.095  1.00 48.91  ? 337 PRO A C     1 
ATOM   2659 O O     . PRO A 1 344 ? 15.698  11.924  -4.182  1.00 48.24  ? 337 PRO A O     1 
ATOM   2660 C CB    . PRO A 1 344 ? 18.187  13.095  -5.805  1.00 48.55  ? 337 PRO A CB    1 
ATOM   2661 C CG    . PRO A 1 344 ? 18.648  11.682  -6.147  1.00 46.10  ? 337 PRO A CG    1 
ATOM   2662 C CD    . PRO A 1 344 ? 18.945  10.991  -4.833  1.00 48.50  ? 337 PRO A CD    1 
ATOM   2663 N N     . LYS A 1 345 ? 15.632  14.138  -3.731  1.00 49.97  ? 338 LYS A N     1 
ATOM   2664 C CA    . LYS A 1 345 ? 14.162  14.254  -3.538  1.00 53.05  ? 338 LYS A CA    1 
ATOM   2665 C C     . LYS A 1 345 ? 13.425  13.626  -4.735  1.00 57.00  ? 338 LYS A C     1 
ATOM   2666 O O     . LYS A 1 345 ? 12.283  13.111  -4.542  1.00 47.33  ? 338 LYS A O     1 
ATOM   2667 C CB    . LYS A 1 345 ? 13.765  15.718  -3.346  1.00 59.80  ? 338 LYS A CB    1 
ATOM   2668 C CG    . LYS A 1 345 ? 14.142  16.641  -4.495  1.00 62.49  ? 338 LYS A CG    1 
ATOM   2669 C CD    . LYS A 1 345 ? 13.785  18.097  -4.262  1.00 63.08  ? 338 LYS A CD    1 
ATOM   2670 C CE    . LYS A 1 345 ? 14.794  19.059  -4.862  1.00 66.52  ? 338 LYS A CE    1 
ATOM   2671 N NZ    . LYS A 1 345 ? 15.184  18.677  -6.244  1.00 64.09  ? 338 LYS A NZ    1 
ATOM   2672 N N     . GLU A 1 346 ? 14.048  13.649  -5.919  1.00 53.14  ? 339 GLU A N     1 
ATOM   2673 C CA    . GLU A 1 346 ? 13.438  13.138  -7.173  1.00 53.43  ? 339 GLU A CA    1 
ATOM   2674 C C     . GLU A 1 346 ? 13.315  11.615  -7.082  1.00 49.27  ? 339 GLU A C     1 
ATOM   2675 O O     . GLU A 1 346 ? 12.293  11.094  -7.533  1.00 40.83  ? 339 GLU A O     1 
ATOM   2676 C CB    . GLU A 1 346 ? 14.262  13.518  -8.401  1.00 57.67  ? 339 GLU A CB    1 
ATOM   2677 C CG    . GLU A 1 346 ? 14.555  15.010  -8.522  1.00 62.75  ? 339 GLU A CG    1 
ATOM   2678 C CD    . GLU A 1 346 ? 15.851  15.472  -7.863  1.00 61.17  ? 339 GLU A CD    1 
ATOM   2679 O OE1   . GLU A 1 346 ? 16.929  14.875  -8.153  1.00 60.94  ? 339 GLU A OE1   1 
ATOM   2680 O OE2   . GLU A 1 346 ? 15.774  16.405  -7.034  1.00 61.58  ? 339 GLU A OE2   1 
ATOM   2681 N N     . LYS A 1 347 ? 14.315  10.922  -6.530  1.00 41.14  ? 340 LYS A N     1 
ATOM   2682 C CA    . LYS A 1 347 ? 14.237  9.451   -6.338  1.00 44.48  ? 340 LYS A CA    1 
ATOM   2683 C C     . LYS A 1 347 ? 13.206  9.155   -5.237  1.00 39.26  ? 340 LYS A C     1 
ATOM   2684 O O     . LYS A 1 347 ? 12.555  8.127   -5.318  1.00 38.54  ? 340 LYS A O     1 
ATOM   2685 C CB    . LYS A 1 347 ? 15.588  8.829   -5.978  1.00 48.24  ? 340 LYS A CB    1 
ATOM   2686 C CG    . LYS A 1 347 ? 15.878  7.550   -6.740  1.00 56.22  ? 340 LYS A CG    1 
ATOM   2687 C CD    . LYS A 1 347 ? 16.205  7.814   -8.209  1.00 59.85  ? 340 LYS A CD    1 
ATOM   2688 C CE    . LYS A 1 347 ? 16.842  6.628   -8.901  1.00 61.46  ? 340 LYS A CE    1 
ATOM   2689 N NZ    . LYS A 1 347 ? 17.272  6.970   -10.276 1.00 56.87  ? 340 LYS A NZ    1 
ATOM   2690 N N     . LEU A 1 348 ? 13.086  10.040  -4.252  1.00 40.05  ? 341 LEU A N     1 
ATOM   2691 C CA    . LEU A 1 348 ? 12.152  9.861   -3.106  1.00 41.36  ? 341 LEU A CA    1 
ATOM   2692 C C     . LEU A 1 348 ? 10.711  10.073  -3.596  1.00 39.52  ? 341 LEU A C     1 
ATOM   2693 O O     . LEU A 1 348 ? 9.851   9.300   -3.191  1.00 34.98  ? 341 LEU A O     1 
ATOM   2694 C CB    . LEU A 1 348 ? 12.516  10.832  -1.983  1.00 40.55  ? 341 LEU A CB    1 
ATOM   2695 C CG    . LEU A 1 348 ? 13.813  10.479  -1.252  1.00 44.88  ? 341 LEU A CG    1 
ATOM   2696 C CD1   . LEU A 1 348 ? 14.172  11.550  -0.230  1.00 45.02  ? 341 LEU A CD1   1 
ATOM   2697 C CD2   . LEU A 1 348 ? 13.702  9.112   -0.593  1.00 44.82  ? 341 LEU A CD2   1 
ATOM   2698 N N     . LYS A 1 349 ? 10.493  11.051  -4.473  1.00 40.08  ? 342 LYS A N     1 
ATOM   2699 C CA    . LYS A 1 349 ? 9.188   11.250  -5.151  1.00 40.37  ? 342 LYS A CA    1 
ATOM   2700 C C     . LYS A 1 349 ? 8.805   9.977   -5.929  1.00 35.45  ? 342 LYS A C     1 
ATOM   2701 O O     . LYS A 1 349 ? 7.639   9.527   -5.771  1.00 34.86  ? 342 LYS A O     1 
ATOM   2702 C CB    . LYS A 1 349 ? 9.238   12.483  -6.052  1.00 39.55  ? 342 LYS A CB    1 
ATOM   2703 C CG    . LYS A 1 349 ? 7.930   12.704  -6.795  1.00 39.35  ? 342 LYS A CG    1 
ATOM   2704 C CD    . LYS A 1 349 ? 7.814   13.983  -7.578  1.00 38.99  ? 342 LYS A CD    1 
ATOM   2705 C CE    . LYS A 1 349 ? 6.361   14.256  -7.884  1.00 37.86  ? 342 LYS A CE    1 
ATOM   2706 N NZ    . LYS A 1 349 ? 6.168   15.261  -8.951  1.00 39.55  ? 342 LYS A NZ    1 
ATOM   2707 N N     . GLU A 1 350 ? 9.722   9.403   -6.715  1.00 35.64  ? 343 GLU A N     1 
ATOM   2708 C CA    . GLU A 1 350 ? 9.539   8.091   -7.410  1.00 39.09  ? 343 GLU A CA    1 
ATOM   2709 C C     . GLU A 1 350 ? 9.221   6.958   -6.402  1.00 38.95  ? 343 GLU A C     1 
ATOM   2710 O O     . GLU A 1 350 ? 8.388   6.090   -6.739  1.00 34.21  ? 343 GLU A O     1 
ATOM   2711 C CB    . GLU A 1 350 ? 10.757  7.670   -8.245  1.00 44.86  ? 343 GLU A CB    1 
ATOM   2712 C CG    . GLU A 1 350 ? 11.150  8.614   -9.379  1.00 53.08  ? 343 GLU A CG    1 
ATOM   2713 C CD    . GLU A 1 350 ? 12.536  8.363   -9.992  1.00 62.50  ? 343 GLU A CD    1 
ATOM   2714 O OE1   . GLU A 1 350 ? 13.200  9.340   -10.443 1.00 69.24  ? 343 GLU A OE1   1 
ATOM   2715 O OE2   . GLU A 1 350 ? 12.972  7.190   -10.019 1.00 60.25  ? 343 GLU A OE2   1 
ATOM   2716 N N     . LEU A 1 351 ? 9.870   6.887   -5.230  1.00 33.18  ? 344 LEU A N     1 
ATOM   2717 C CA    . LEU A 1 351 ? 9.559   5.820   -4.225  1.00 31.60  ? 344 LEU A CA    1 
ATOM   2718 C C     . LEU A 1 351 ? 8.169   6.041   -3.620  1.00 25.95  ? 344 LEU A C     1 
ATOM   2719 O O     . LEU A 1 351 ? 7.427   5.058   -3.446  1.00 26.90  ? 344 LEU A O     1 
ATOM   2720 C CB    . LEU A 1 351 ? 10.618  5.811   -3.117  1.00 35.91  ? 344 LEU A CB    1 
ATOM   2721 C CG    . LEU A 1 351 ? 11.782  4.824   -3.240  1.00 36.80  ? 344 LEU A CG    1 
ATOM   2722 C CD1   . LEU A 1 351 ? 11.983  4.283   -4.635  1.00 35.43  ? 344 LEU A CD1   1 
ATOM   2723 C CD2   . LEU A 1 351 ? 13.048  5.481   -2.716  1.00 40.83  ? 344 LEU A CD2   1 
ATOM   2724 N N     . ILE A 1 352 ? 7.820   7.286   -3.305  1.00 26.44  ? 345 ILE A N     1 
ATOM   2725 C CA    . ILE A 1 352 ? 6.457   7.646   -2.807  1.00 29.18  ? 345 ILE A CA    1 
ATOM   2726 C C     . ILE A 1 352 ? 5.407   7.251   -3.864  1.00 29.97  ? 345 ILE A C     1 
ATOM   2727 O O     . ILE A 1 352 ? 4.346   6.659   -3.508  1.00 29.17  ? 345 ILE A O     1 
ATOM   2728 C CB    . ILE A 1 352 ? 6.399   9.133   -2.419  1.00 27.16  ? 345 ILE A CB    1 
ATOM   2729 C CG1   . ILE A 1 352 ? 7.277   9.409   -1.194  1.00 31.87  ? 345 ILE A CG1   1 
ATOM   2730 C CG2   . ILE A 1 352 ? 4.968   9.588   -2.198  1.00 28.08  ? 345 ILE A CG2   1 
ATOM   2731 C CD1   . ILE A 1 352 ? 7.572   10.866  -0.942  1.00 28.47  ? 345 ILE A CD1   1 
ATOM   2732 N N     . PHE A 1 353 ? 5.662   7.591   -5.128  1.00 32.35  ? 346 PHE A N     1 
ATOM   2733 C CA    . PHE A 1 353 ? 4.799   7.194   -6.275  1.00 32.60  ? 346 PHE A CA    1 
ATOM   2734 C C     . PHE A 1 353 ? 4.582   5.672   -6.258  1.00 30.85  ? 346 PHE A C     1 
ATOM   2735 O O     . PHE A 1 353 ? 3.433   5.216   -6.224  1.00 29.47  ? 346 PHE A O     1 
ATOM   2736 C CB    . PHE A 1 353 ? 5.415   7.644   -7.605  1.00 31.73  ? 346 PHE A CB    1 
ATOM   2737 C CG    . PHE A 1 353 ? 4.452   7.518   -8.755  1.00 30.28  ? 346 PHE A CG    1 
ATOM   2738 C CD1   . PHE A 1 353 ? 3.463   8.484   -8.954  1.00 32.30  ? 346 PHE A CD1   1 
ATOM   2739 C CD2   . PHE A 1 353 ? 4.511   6.428   -9.613  1.00 31.11  ? 346 PHE A CD2   1 
ATOM   2740 C CE1   . PHE A 1 353 ? 2.584   8.394   -10.026 1.00 30.06  ? 346 PHE A CE1   1 
ATOM   2741 C CE2   . PHE A 1 353 ? 3.611   6.324   -10.669 1.00 32.15  ? 346 PHE A CE2   1 
ATOM   2742 C CZ    . PHE A 1 353 ? 2.653   7.305   -10.871 1.00 29.71  ? 346 PHE A CZ    1 
ATOM   2743 N N     . GLU A 1 354 ? 5.660   4.893   -6.258  1.00 28.86  ? 347 GLU A N     1 
ATOM   2744 C CA    . GLU A 1 354 ? 5.567   3.402   -6.255  1.00 32.23  ? 347 GLU A CA    1 
ATOM   2745 C C     . GLU A 1 354 ? 4.846   2.875   -5.003  1.00 30.81  ? 347 GLU A C     1 
ATOM   2746 O O     . GLU A 1 354 ? 3.998   1.991   -5.151  1.00 31.28  ? 347 GLU A O     1 
ATOM   2747 C CB    . GLU A 1 354 ? 6.966   2.800   -6.347  1.00 37.18  ? 347 GLU A CB    1 
ATOM   2748 C CG    . GLU A 1 354 ? 7.643   3.068   -7.671  1.00 44.37  ? 347 GLU A CG    1 
ATOM   2749 C CD    . GLU A 1 354 ? 9.033   2.467   -7.772  1.00 57.05  ? 347 GLU A CD    1 
ATOM   2750 O OE1   . GLU A 1 354 ? 9.125   1.252   -8.058  1.00 66.05  ? 347 GLU A OE1   1 
ATOM   2751 O OE2   . GLU A 1 354 ? 10.016  3.212   -7.553  1.00 62.97  ? 347 GLU A OE2   1 
ATOM   2752 N N     . GLU A 1 355 ? 5.107   3.433   -3.815  1.00 31.40  ? 348 GLU A N     1 
ATOM   2753 C CA    . GLU A 1 355 ? 4.514   2.934   -2.543  1.00 31.34  ? 348 GLU A CA    1 
ATOM   2754 C C     . GLU A 1 355 ? 3.008   3.195   -2.534  1.00 32.26  ? 348 GLU A C     1 
ATOM   2755 O O     . GLU A 1 355 ? 2.302   2.458   -1.808  1.00 33.31  ? 348 GLU A O     1 
ATOM   2756 C CB    . GLU A 1 355 ? 5.068   3.644   -1.302  1.00 35.24  ? 348 GLU A CB    1 
ATOM   2757 C CG    . GLU A 1 355 ? 6.344   3.083   -0.739  1.00 38.46  ? 348 GLU A CG    1 
ATOM   2758 C CD    . GLU A 1 355 ? 6.325   1.620   -0.386  1.00 37.38  ? 348 GLU A CD    1 
ATOM   2759 O OE1   . GLU A 1 355 ? 5.504   1.199   0.459   1.00 43.92  ? 348 GLU A OE1   1 
ATOM   2760 O OE2   . GLU A 1 355 ? 7.119   0.914   -0.987  1.00 43.61  ? 348 GLU A OE2   1 
ATOM   2761 N N     . THR A 1 356 ? 2.522   4.217   -3.264  1.00 31.66  ? 349 THR A N     1 
ATOM   2762 C CA    . THR A 1 356 ? 1.094   4.637   -3.233  1.00 27.77  ? 349 THR A CA    1 
ATOM   2763 C C     . THR A 1 356 ? 0.284   4.005   -4.400  1.00 30.21  ? 349 THR A C     1 
ATOM   2764 O O     . THR A 1 356 ? -0.927  4.259   -4.466  1.00 28.88  ? 349 THR A O     1 
ATOM   2765 C CB    . THR A 1 356 ? 0.979   6.167   -3.177  1.00 27.67  ? 349 THR A CB    1 
ATOM   2766 O OG1   . THR A 1 356 ? 1.662   6.748   -4.288  1.00 25.81  ? 349 THR A OG1   1 
ATOM   2767 C CG2   . THR A 1 356 ? 1.556   6.751   -1.907  1.00 27.67  ? 349 THR A CG2   1 
ATOM   2768 N N     . ALA A 1 357 ? 0.904   3.203   -5.261  1.00 30.01  ? 350 ALA A N     1 
ATOM   2769 C CA    . ALA A 1 357 ? 0.324   2.684   -6.524  1.00 29.95  ? 350 ALA A CA    1 
ATOM   2770 C C     . ALA A 1 357 ? -0.890  1.790   -6.228  1.00 36.92  ? 350 ALA A C     1 
ATOM   2771 O O     . ALA A 1 357 ? -1.848  1.797   -7.021  1.00 36.41  ? 350 ALA A O     1 
ATOM   2772 C CB    . ALA A 1 357 ? 1.380   1.953   -7.315  1.00 29.56  ? 350 ALA A CB    1 
ATOM   2773 N N     . ARG A 1 358 ? -0.903  1.092   -5.092  1.00 36.95  ? 351 ARG A N     1 
ATOM   2774 C CA    . ARG A 1 358 ? -1.904  0.033   -4.829  1.00 39.01  ? 351 ARG A CA    1 
ATOM   2775 C C     . ARG A 1 358 ? -3.272  0.682   -4.608  1.00 36.45  ? 351 ARG A C     1 
ATOM   2776 O O     . ARG A 1 358 ? -4.264  -0.051  -4.651  1.00 37.29  ? 351 ARG A O     1 
ATOM   2777 C CB    . ARG A 1 358 ? -1.445  -0.874  -3.671  1.00 45.18  ? 351 ARG A CB    1 
ATOM   2778 C CG    . ARG A 1 358 ? -1.682  -0.329  -2.265  1.00 51.55  ? 351 ARG A CG    1 
ATOM   2779 C CD    . ARG A 1 358 ? -0.822  -0.983  -1.181  1.00 52.78  ? 351 ARG A CD    1 
ATOM   2780 N NE    . ARG A 1 358 ? 0.605   -0.713  -1.370  1.00 59.07  ? 351 ARG A NE    1 
ATOM   2781 C CZ    . ARG A 1 358 ? 1.609   -1.214  -0.633  1.00 60.42  ? 351 ARG A CZ    1 
ATOM   2782 N NH1   . ARG A 1 358 ? 1.362   -2.033  0.380   1.00 52.44  ? 351 ARG A NH1   1 
ATOM   2783 N NH2   . ARG A 1 358 ? 2.864   -0.882  -0.916  1.00 55.82  ? 351 ARG A NH2   1 
ATOM   2784 N N     . PHE A 1 359 ? -3.351  1.995   -4.388  1.00 31.11  ? 352 PHE A N     1 
ATOM   2785 C CA    . PHE A 1 359 ? -4.646  2.689   -4.178  1.00 33.07  ? 352 PHE A CA    1 
ATOM   2786 C C     . PHE A 1 359 ? -5.184  3.284   -5.487  1.00 32.58  ? 352 PHE A C     1 
ATOM   2787 O O     . PHE A 1 359 ? -6.238  3.965   -5.445  1.00 30.51  ? 352 PHE A O     1 
ATOM   2788 C CB    . PHE A 1 359 ? -4.514  3.766   -3.106  1.00 35.17  ? 352 PHE A CB    1 
ATOM   2789 C CG    . PHE A 1 359 ? -4.161  3.197   -1.759  1.00 35.27  ? 352 PHE A CG    1 
ATOM   2790 C CD1   . PHE A 1 359 ? -5.149  2.713   -0.913  1.00 37.17  ? 352 PHE A CD1   1 
ATOM   2791 C CD2   . PHE A 1 359 ? -2.840  3.080   -1.375  1.00 38.05  ? 352 PHE A CD2   1 
ATOM   2792 C CE1   . PHE A 1 359 ? -4.812  2.146   0.302   1.00 37.41  ? 352 PHE A CE1   1 
ATOM   2793 C CE2   . PHE A 1 359 ? -2.508  2.509   -0.159  1.00 40.63  ? 352 PHE A CE2   1 
ATOM   2794 C CZ    . PHE A 1 359 ? -3.494  2.051   0.676   1.00 36.56  ? 352 PHE A CZ    1 
ATOM   2795 N N     . GLN A 1 360 ? -4.491  3.074   -6.596  1.00 34.52  ? 353 GLN A N     1 
ATOM   2796 C CA    . GLN A 1 360 ? -4.851  3.697   -7.900  1.00 40.72  ? 353 GLN A CA    1 
ATOM   2797 C C     . GLN A 1 360 ? -5.889  2.838   -8.619  1.00 45.31  ? 353 GLN A C     1 
ATOM   2798 O O     . GLN A 1 360 ? -5.705  1.624   -8.700  1.00 42.63  ? 353 GLN A O     1 
ATOM   2799 C CB    . GLN A 1 360 ? -3.609  3.864   -8.780  1.00 41.66  ? 353 GLN A CB    1 
ATOM   2800 C CG    . GLN A 1 360 ? -2.769  5.068   -8.385  1.00 40.90  ? 353 GLN A CG    1 
ATOM   2801 C CD    . GLN A 1 360 ? -3.604  6.324   -8.352  1.00 43.84  ? 353 GLN A CD    1 
ATOM   2802 O OE1   . GLN A 1 360 ? -3.808  6.946   -7.298  1.00 37.13  ? 353 GLN A OE1   1 
ATOM   2803 N NE2   . GLN A 1 360 ? -4.123  6.689   -9.519  1.00 36.57  ? 353 GLN A NE2   1 
ATOM   2804 N N     . PRO A 1 361 ? -6.984  3.449   -9.141  1.00 55.06  ? 354 PRO A N     1 
ATOM   2805 C CA    . PRO A 1 361 ? -7.956  2.738   -9.976  1.00 60.16  ? 354 PRO A CA    1 
ATOM   2806 C C     . PRO A 1 361 ? -7.474  2.603   -11.427 1.00 57.21  ? 354 PRO A C     1 
ATOM   2807 O O     . PRO A 1 361 ? -6.733  1.660   -11.705 1.00 65.41  ? 354 PRO A O     1 
ATOM   2808 C CB    . PRO A 1 361 ? -9.231  3.598   -9.876  1.00 60.62  ? 354 PRO A CB    1 
ATOM   2809 C CG    . PRO A 1 361 ? -8.742  5.004   -9.562  1.00 59.18  ? 354 PRO A CG    1 
ATOM   2810 C CD    . PRO A 1 361 ? -7.380  4.852   -8.906  1.00 55.01  ? 354 PRO A CD    1 
HETATM 2811 P PG    . ANP B 2 .   ? 0.542   18.289  13.787  1.00 129.81 ? 501 ANP A PG    1 
HETATM 2812 O O1G   . ANP B 2 .   ? 0.506   19.594  13.030  1.00 133.27 ? 501 ANP A O1G   1 
HETATM 2813 O O2G   . ANP B 2 .   ? 1.783   18.266  14.650  1.00 131.41 ? 501 ANP A O2G   1 
HETATM 2814 O O3G   . ANP B 2 .   ? -0.647  18.295  14.718  1.00 123.16 ? 501 ANP A O3G   1 
HETATM 2815 P PB    . ANP B 2 .   ? 1.711   15.907  12.478  1.00 118.62 ? 501 ANP A PB    1 
HETATM 2816 O O1B   . ANP B 2 .   ? 2.355   15.518  13.781  1.00 126.14 ? 501 ANP A O1B   1 
HETATM 2817 O O2B   . ANP B 2 .   ? 2.584   16.198  11.290  1.00 113.43 ? 501 ANP A O2B   1 
HETATM 2818 N N3B   . ANP B 2 .   ? 0.542   17.041  12.719  1.00 128.28 ? 501 ANP A N3B   1 
HETATM 2819 P PA    . ANP B 2 .   ? -0.491  14.026  12.624  1.00 104.31 ? 501 ANP A PA    1 
HETATM 2820 O O1A   . ANP B 2 .   ? -0.256  13.656  14.051  1.00 101.83 ? 501 ANP A O1A   1 
HETATM 2821 O O2A   . ANP B 2 .   ? -1.025  12.975  11.705  1.00 106.55 ? 501 ANP A O2A   1 
HETATM 2822 O O3A   . ANP B 2 .   ? 0.894   14.596  12.055  1.00 117.90 ? 501 ANP A O3A   1 
HETATM 2823 O "O5'" . ANP B 2 .   ? -1.399  15.362  12.523  1.00 94.75  ? 501 ANP A "O5'" 1 
HETATM 2824 C "C5'" . ANP B 2 .   ? -2.020  15.826  13.745  1.00 85.06  ? 501 ANP A "C5'" 1 
HETATM 2825 C "C4'" . ANP B 2 .   ? -3.022  16.937  13.502  1.00 79.66  ? 501 ANP A "C4'" 1 
HETATM 2826 O "O4'" . ANP B 2 .   ? -4.120  16.497  12.658  1.00 77.05  ? 501 ANP A "O4'" 1 
HETATM 2827 C "C3'" . ANP B 2 .   ? -3.785  17.340  14.762  1.00 76.73  ? 501 ANP A "C3'" 1 
HETATM 2828 O "O3'" . ANP B 2 .   ? -4.652  18.450  14.563  1.00 68.72  ? 501 ANP A "O3'" 1 
HETATM 2829 C "C2'" . ANP B 2 .   ? -4.598  16.055  14.922  1.00 72.21  ? 501 ANP A "C2'" 1 
HETATM 2830 O "O2'" . ANP B 2 .   ? -5.502  16.189  15.998  1.00 70.88  ? 501 ANP A "O2'" 1 
HETATM 2831 C "C1'" . ANP B 2 .   ? -5.117  15.914  13.478  1.00 62.68  ? 501 ANP A "C1'" 1 
HETATM 2832 N N9    . ANP B 2 .   ? -5.280  14.534  13.024  1.00 50.54  ? 501 ANP A N9    1 
HETATM 2833 C C8    . ANP B 2 .   ? -4.297  13.717  12.520  1.00 45.79  ? 501 ANP A C8    1 
HETATM 2834 N N7    . ANP B 2 .   ? -4.741  12.520  12.211  1.00 51.31  ? 501 ANP A N7    1 
HETATM 2835 C C5    . ANP B 2 .   ? -6.092  12.550  12.535  1.00 38.73  ? 501 ANP A C5    1 
HETATM 2836 C C6    . ANP B 2 .   ? -7.110  11.578  12.438  1.00 36.08  ? 501 ANP A C6    1 
HETATM 2837 N N6    . ANP B 2 .   ? -6.931  10.356  11.931  1.00 30.09  ? 501 ANP A N6    1 
HETATM 2838 N N1    . ANP B 2 .   ? -8.347  11.943  12.853  1.00 31.88  ? 501 ANP A N1    1 
HETATM 2839 C C2    . ANP B 2 .   ? -8.528  13.196  13.298  1.00 33.38  ? 501 ANP A C2    1 
HETATM 2840 N N3    . ANP B 2 .   ? -7.645  14.191  13.431  1.00 40.00  ? 501 ANP A N3    1 
HETATM 2841 C C4    . ANP B 2 .   ? -6.432  13.795  13.021  1.00 42.58  ? 501 ANP A C4    1 
HETATM 2842 O O     . HOH C 3 .   ? 22.443  -2.435  15.917  1.00 44.07  ? 601 HOH A O     1 
HETATM 2843 O O     . HOH C 3 .   ? 31.525  13.700  24.322  1.00 42.31  ? 602 HOH A O     1 
HETATM 2844 O O     . HOH C 3 .   ? 21.449  20.035  33.590  1.00 34.04  ? 603 HOH A O     1 
HETATM 2845 O O     . HOH C 3 .   ? 12.827  6.821   38.268  1.00 34.18  ? 604 HOH A O     1 
HETATM 2846 O O     . HOH C 3 .   ? 18.676  4.954   22.512  1.00 38.19  ? 605 HOH A O     1 
HETATM 2847 O O     . HOH C 3 .   ? -2.382  0.812   7.079   1.00 31.65  ? 606 HOH A O     1 
HETATM 2848 O O     . HOH C 3 .   ? 15.855  -1.079  28.706  1.00 26.19  ? 607 HOH A O     1 
HETATM 2849 O O     . HOH C 3 .   ? -4.322  -9.992  33.199  1.00 39.04  ? 608 HOH A O     1 
HETATM 2850 O O     . HOH C 3 .   ? -6.208  -6.646  24.740  1.00 38.24  ? 609 HOH A O     1 
HETATM 2851 O O     . HOH C 3 .   ? 2.456   -8.973  26.026  1.00 22.63  ? 610 HOH A O     1 
HETATM 2852 O O     . HOH C 3 .   ? -1.226  14.367  -6.704  1.00 24.58  ? 611 HOH A O     1 
HETATM 2853 O O     . HOH C 3 .   ? 18.939  4.363   36.594  1.00 23.45  ? 612 HOH A O     1 
HETATM 2854 O O     . HOH C 3 .   ? 21.015  6.595   39.193  1.00 31.86  ? 613 HOH A O     1 
HETATM 2855 O O     . HOH C 3 .   ? 31.902  18.255  30.173  1.00 33.67  ? 614 HOH A O     1 
HETATM 2856 O O     . HOH C 3 .   ? -2.684  6.325   -5.060  1.00 35.24  ? 615 HOH A O     1 
HETATM 2857 O O     . HOH C 3 .   ? 11.567  10.296  41.482  1.00 41.31  ? 616 HOH A O     1 
HETATM 2858 O O     . HOH C 3 .   ? 13.545  -5.766  17.273  1.00 34.11  ? 617 HOH A O     1 
HETATM 2859 O O     . HOH C 3 .   ? 2.895   17.934  24.933  1.00 41.28  ? 618 HOH A O     1 
HETATM 2860 O O     . HOH C 3 .   ? -0.549  5.632   -11.251 1.00 33.80  ? 619 HOH A O     1 
HETATM 2861 O O     . HOH C 3 .   ? 4.236   3.132   44.507  1.00 37.45  ? 620 HOH A O     1 
HETATM 2862 O O     . HOH C 3 .   ? 4.562   18.929  -2.653  1.00 41.04  ? 621 HOH A O     1 
HETATM 2863 O O     . HOH C 3 .   ? -6.142  -16.511 24.672  1.00 38.94  ? 622 HOH A O     1 
HETATM 2864 O O     . HOH C 3 .   ? -9.689  7.173   -3.868  1.00 33.82  ? 623 HOH A O     1 
HETATM 2865 O O     . HOH C 3 .   ? -4.012  18.354  -5.105  1.00 35.14  ? 624 HOH A O     1 
HETATM 2866 O O     . HOH C 3 .   ? 25.055  14.441  38.608  1.00 22.83  ? 625 HOH A O     1 
HETATM 2867 O O     . HOH C 3 .   ? 12.538  18.899  37.987  1.00 41.12  ? 626 HOH A O     1 
HETATM 2868 O O     . HOH C 3 .   ? 28.931  7.123   26.914  1.00 34.59  ? 627 HOH A O     1 
HETATM 2869 O O     . HOH C 3 .   ? -7.890  -9.547  25.802  1.00 39.24  ? 628 HOH A O     1 
HETATM 2870 O O     . HOH C 3 .   ? -3.005  -11.551 19.338  1.00 37.26  ? 629 HOH A O     1 
HETATM 2871 O O     . HOH C 3 .   ? -2.752  12.031  -16.935 1.00 27.50  ? 630 HOH A O     1 
HETATM 2872 O O     . HOH C 3 .   ? 18.343  4.713   25.007  1.00 36.82  ? 631 HOH A O     1 
HETATM 2873 O O     . HOH C 3 .   ? -2.699  10.895  11.586  1.00 47.88  ? 632 HOH A O     1 
HETATM 2874 O O     . HOH C 3 .   ? -1.193  18.284  -11.279 1.00 29.18  ? 633 HOH A O     1 
HETATM 2875 O O     . HOH C 3 .   ? 24.103  14.067  22.667  1.00 30.15  ? 634 HOH A O     1 
HETATM 2876 O O     . HOH C 3 .   ? -0.403  -6.632  33.919  1.00 19.44  ? 635 HOH A O     1 
HETATM 2877 O O     . HOH C 3 .   ? 16.879  18.308  25.221  1.00 28.67  ? 636 HOH A O     1 
HETATM 2878 O O     . HOH C 3 .   ? 4.135   -9.341  28.319  1.00 24.57  ? 637 HOH A O     1 
HETATM 2879 O O     . HOH C 3 .   ? 12.762  9.636   24.576  1.00 21.02  ? 638 HOH A O     1 
HETATM 2880 O O     . HOH C 3 .   ? 30.903  22.362  39.667  1.00 35.30  ? 639 HOH A O     1 
HETATM 2881 O O     . HOH C 3 .   ? 10.707  11.652  -9.658  1.00 37.79  ? 640 HOH A O     1 
HETATM 2882 O O     . HOH C 3 .   ? -5.260  -9.775  19.244  1.00 35.45  ? 641 HOH A O     1 
HETATM 2883 O O     . HOH C 3 .   ? 6.387   -6.021  35.206  1.00 37.25  ? 642 HOH A O     1 
HETATM 2884 O O     . HOH C 3 .   ? -3.967  7.103   39.496  1.00 32.58  ? 643 HOH A O     1 
HETATM 2885 O O     . HOH C 3 .   ? -0.939  18.484  29.339  1.00 39.13  ? 644 HOH A O     1 
HETATM 2886 O O     . HOH C 3 .   ? -5.509  -2.859  35.643  1.00 24.88  ? 645 HOH A O     1 
HETATM 2887 O O     . HOH C 3 .   ? 23.187  15.799  39.980  1.00 32.78  ? 646 HOH A O     1 
HETATM 2888 O O     . HOH C 3 .   ? 13.269  0.197   28.020  1.00 26.19  ? 647 HOH A O     1 
HETATM 2889 O O     . HOH C 3 .   ? -5.956  13.748  34.555  1.00 34.36  ? 648 HOH A O     1 
HETATM 2890 O O     . HOH C 3 .   ? -7.186  2.889   11.871  1.00 41.80  ? 649 HOH A O     1 
HETATM 2891 O O     . HOH C 3 .   ? 5.207   -0.449  2.984   1.00 40.24  ? 650 HOH A O     1 
HETATM 2892 O O     . HOH C 3 .   ? 27.760  22.557  35.690  1.00 28.82  ? 651 HOH A O     1 
HETATM 2893 O O     . HOH C 3 .   ? 20.589  8.269   30.664  1.00 34.09  ? 652 HOH A O     1 
HETATM 2894 O O     . HOH C 3 .   ? 0.179   -5.687  20.696  1.00 18.49  ? 653 HOH A O     1 
HETATM 2895 O O     . HOH C 3 .   ? 7.855   9.268   14.472  1.00 24.19  ? 654 HOH A O     1 
HETATM 2896 O O     . HOH C 3 .   ? 8.143   13.089  21.458  1.00 29.11  ? 655 HOH A O     1 
HETATM 2897 O O     . HOH C 3 .   ? -12.164 17.792  34.180  1.00 32.43  ? 656 HOH A O     1 
HETATM 2898 O O     . HOH C 3 .   ? -7.298  4.547   9.593   1.00 37.12  ? 657 HOH A O     1 
HETATM 2899 O O     . HOH C 3 .   ? 5.162   14.856  30.358  1.00 22.83  ? 658 HOH A O     1 
HETATM 2900 O O     . HOH C 3 .   ? 35.801  11.813  34.988  1.00 38.72  ? 659 HOH A O     1 
HETATM 2901 O O     . HOH C 3 .   ? 7.719   -9.717  15.624  1.00 34.48  ? 660 HOH A O     1 
HETATM 2902 O O     . HOH C 3 .   ? 21.710  2.787   40.773  1.00 40.09  ? 661 HOH A O     1 
HETATM 2903 O O     . HOH C 3 .   ? 10.475  19.277  35.942  1.00 38.63  ? 662 HOH A O     1 
HETATM 2904 O O     . HOH C 3 .   ? -5.833  8.704   -6.462  1.00 31.22  ? 663 HOH A O     1 
HETATM 2905 O O     . HOH C 3 .   ? 23.424  5.469   33.041  1.00 34.04  ? 664 HOH A O     1 
HETATM 2906 O O     . HOH C 3 .   ? 7.855   -5.906  21.467  1.00 28.42  ? 665 HOH A O     1 
HETATM 2907 O O     . HOH C 3 .   ? 3.654   -12.022 22.313  1.00 27.13  ? 666 HOH A O     1 
HETATM 2908 O O     . HOH C 3 .   ? 16.867  6.429   37.787  1.00 24.04  ? 667 HOH A O     1 
HETATM 2909 O O     . HOH C 3 .   ? -0.938  1.020   10.455  1.00 26.19  ? 668 HOH A O     1 
HETATM 2910 O O     . HOH C 3 .   ? 19.735  10.537  13.595  1.00 43.53  ? 669 HOH A O     1 
HETATM 2911 O O     . HOH C 3 .   ? 9.681   -6.169  25.668  1.00 32.28  ? 670 HOH A O     1 
HETATM 2912 O O     . HOH C 3 .   ? 8.235   14.921  -10.893 1.00 41.84  ? 671 HOH A O     1 
HETATM 2913 O O     . HOH C 3 .   ? 9.535   7.623   44.624  1.00 50.54  ? 672 HOH A O     1 
HETATM 2914 O O     . HOH C 3 .   ? -2.874  -0.356  11.881  1.00 22.70  ? 673 HOH A O     1 
HETATM 2915 O O     . HOH C 3 .   ? 12.048  14.026  29.139  1.00 22.71  ? 674 HOH A O     1 
HETATM 2916 O O     . HOH C 3 .   ? 7.789   15.957  30.279  1.00 22.83  ? 675 HOH A O     1 
HETATM 2917 O O     . HOH C 3 .   ? -13.583 6.909   10.106  1.00 35.80  ? 676 HOH A O     1 
HETATM 2918 O O     . HOH C 3 .   ? 18.125  17.009  47.474  1.00 36.19  ? 677 HOH A O     1 
HETATM 2919 O O     . HOH C 3 .   ? 9.336   8.375   21.623  1.00 20.16  ? 678 HOH A O     1 
HETATM 2920 O O     . HOH C 3 .   ? -2.943  11.813  40.302  1.00 42.42  ? 679 HOH A O     1 
HETATM 2921 O O     . HOH C 3 .   ? -7.942  1.922   19.116  1.00 38.48  ? 680 HOH A O     1 
HETATM 2922 O O     . HOH C 3 .   ? 1.498   -8.099  11.335  1.00 38.81  ? 681 HOH A O     1 
HETATM 2923 O O     . HOH C 3 .   ? 26.058  2.809   42.382  1.00 34.09  ? 682 HOH A O     1 
HETATM 2924 O O     . HOH C 3 .   ? 12.806  -0.363  35.478  1.00 30.48  ? 683 HOH A O     1 
HETATM 2925 O O     . HOH C 3 .   ? -1.914  -6.856  15.177  1.00 30.89  ? 684 HOH A O     1 
HETATM 2926 O O     . HOH C 3 .   ? 10.532  -5.622  21.560  1.00 29.51  ? 685 HOH A O     1 
HETATM 2927 O O     . HOH C 3 .   ? 11.322  20.040  20.861  1.00 37.65  ? 686 HOH A O     1 
HETATM 2928 O O     . HOH C 3 .   ? -0.143  9.358   11.056  1.00 41.43  ? 687 HOH A O     1 
HETATM 2929 O O     . HOH C 3 .   ? 10.459  -2.117  24.730  1.00 22.84  ? 688 HOH A O     1 
HETATM 2930 O O     . HOH C 3 .   ? 2.091   16.640  22.534  1.00 22.34  ? 689 HOH A O     1 
HETATM 2931 O O     . HOH C 3 .   ? 27.256  23.040  38.477  1.00 28.38  ? 690 HOH A O     1 
HETATM 2932 O O     . HOH C 3 .   ? 19.513  10.034  37.919  1.00 41.80  ? 691 HOH A O     1 
HETATM 2933 O O     . HOH C 3 .   ? 26.156  5.404   44.000  1.00 37.62  ? 692 HOH A O     1 
HETATM 2934 O O     . HOH C 3 .   ? 21.043  4.263   25.176  1.00 40.00  ? 693 HOH A O     1 
HETATM 2935 O O     . HOH C 3 .   ? 16.740  -1.475  20.918  1.00 25.94  ? 694 HOH A O     1 
HETATM 2936 O O     . HOH C 3 .   ? 4.604   8.503   -13.932 1.00 41.60  ? 695 HOH A O     1 
HETATM 2937 O O     . HOH C 3 .   ? 16.576  -0.462  24.537  1.00 35.24  ? 696 HOH A O     1 
HETATM 2938 O O     . HOH C 3 .   ? -4.520  -5.419  16.918  1.00 32.64  ? 697 HOH A O     1 
HETATM 2939 O O     . HOH C 3 .   ? 11.361  12.933  22.078  1.00 49.41  ? 698 HOH A O     1 
HETATM 2940 O O     . HOH C 3 .   ? 4.715   -6.675  10.193  1.00 40.21  ? 699 HOH A O     1 
HETATM 2941 O O     . HOH C 3 .   ? -1.233  17.108  -7.080  1.00 36.59  ? 700 HOH A O     1 
HETATM 2942 O O     . HOH C 3 .   ? -10.311 8.253   39.597  1.00 41.32  ? 701 HOH A O     1 
HETATM 2943 O O     . HOH C 3 .   ? 13.476  29.348  35.687  1.00 36.61  ? 702 HOH A O     1 
HETATM 2944 O O     . HOH C 3 .   ? -7.611  -1.505  22.098  1.00 37.73  ? 703 HOH A O     1 
HETATM 2945 O O     . HOH C 3 .   ? -13.054 5.991   15.359  1.00 40.75  ? 704 HOH A O     1 
HETATM 2946 O O     . HOH C 3 .   ? -1.807  13.289  42.388  1.00 36.16  ? 705 HOH A O     1 
HETATM 2947 O O     . HOH C 3 .   ? -7.349  0.614   38.930  1.00 45.29  ? 706 HOH A O     1 
HETATM 2948 O O     . HOH C 3 .   ? 11.221  -4.708  24.038  1.00 26.61  ? 707 HOH A O     1 
HETATM 2949 O O     . HOH C 3 .   ? 2.946   -0.619  43.984  1.00 48.57  ? 708 HOH A O     1 
HETATM 2950 O O     . HOH C 3 .   ? -5.497  -0.968  38.715  1.00 42.93  ? 709 HOH A O     1 
HETATM 2951 O O     . HOH C 3 .   ? -0.623  -8.932  35.187  1.00 29.21  ? 710 HOH A O     1 
HETATM 2952 O O     . HOH C 3 .   ? 12.687  -1.039  25.723  1.00 24.74  ? 711 HOH A O     1 
HETATM 2953 O O     . HOH C 3 .   ? 3.529   18.621  21.029  1.00 48.24  ? 712 HOH A O     1 
HETATM 2954 O O     . HOH C 3 .   ? 2.882   -2.432  41.696  1.00 35.80  ? 713 HOH A O     1 
HETATM 2955 O O     . HOH C 3 .   ? -4.641  9.736   39.634  1.00 39.58  ? 714 HOH A O     1 
HETATM 2956 O O     . HOH C 3 .   ? 12.186  -3.205  35.370  1.00 40.79  ? 715 HOH A O     1 
HETATM 2957 O O     . HOH C 3 .   ? -2.267  -10.700 34.787  1.00 34.73  ? 716 HOH A O     1 
HETATM 2958 O O     . HOH C 3 .   ? 7.656   -4.627  36.839  1.00 38.41  ? 717 HOH A O     1 
# 
