data_8RQV
# 
_entry.id   8RQV 
# 
_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   8RQV         pdb_00008rqv 10.2210/pdb8rqv/pdb 
WWPDB D_1292135845 ?            ?                   
# 
_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                        8RQV 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-19 
_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 . 4S31 unspecified 
PDB . 4S32 unspecified 
PDB . 8RLX 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'          42200.484 1  2.7.11.24 ? ? ? 
2 non-polymer syn 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' 506.196   1  ?         ? ? ? 
3 water       nat water                                         18.015    76 ?         ? ? ? 
# 
_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
LLNTTCDLKICDFGLARVADPDHDHTGFLTEYVAARWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLD
QLNHILGILGSPSQEDLNCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQ
YYDPSDEPIAEAPFKFDMELDDLPKEKLKELIFEETARFQPGYRS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;AHHHHHHMAAAAAAGPEMVRGQVFDVGPRYTNLSYIGEGAYGMVCSAYDNLNKVRVAIKKISPFEHQTYCQRTLREIKIL
LRFRHENIIGINDIIRAPTIEQMKDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNL
LLNTTCDLKICDFGLARVADPDHDHTGFLTEYVAARWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLD
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 ALA 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   8   GLY GLY A . n 
A 1 16  PRO 16  9   9   PRO PRO 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 ALA 195 188 188 ALA ALA 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 82  HOH HOH A . 
C 3 HOH 2  602 51  HOH HOH A . 
C 3 HOH 3  603 7   HOH HOH A . 
C 3 HOH 4  604 58  HOH HOH A . 
C 3 HOH 5  605 40  HOH HOH A . 
C 3 HOH 6  606 9   HOH HOH A . 
C 3 HOH 7  607 76  HOH HOH A . 
C 3 HOH 8  608 21  HOH HOH A . 
C 3 HOH 9  609 43  HOH HOH A . 
C 3 HOH 10 610 50  HOH HOH A . 
C 3 HOH 11 611 84  HOH HOH A . 
C 3 HOH 12 612 22  HOH HOH A . 
C 3 HOH 13 613 77  HOH HOH A . 
C 3 HOH 14 614 28  HOH HOH A . 
C 3 HOH 15 615 14  HOH HOH A . 
C 3 HOH 16 616 44  HOH HOH A . 
C 3 HOH 17 617 3   HOH HOH A . 
C 3 HOH 18 618 1   HOH HOH A . 
C 3 HOH 19 619 13  HOH HOH A . 
C 3 HOH 20 620 17  HOH HOH A . 
C 3 HOH 21 621 25  HOH HOH A . 
C 3 HOH 22 622 47  HOH HOH A . 
C 3 HOH 23 623 79  HOH HOH A . 
C 3 HOH 24 624 52  HOH HOH A . 
C 3 HOH 25 625 33  HOH HOH A . 
C 3 HOH 26 626 8   HOH HOH A . 
C 3 HOH 27 627 2   HOH HOH A . 
C 3 HOH 28 628 18  HOH HOH A . 
C 3 HOH 29 629 31  HOH HOH A . 
C 3 HOH 30 630 71  HOH HOH A . 
C 3 HOH 31 631 5   HOH HOH A . 
C 3 HOH 32 632 34  HOH HOH A . 
C 3 HOH 33 633 73  HOH HOH A . 
C 3 HOH 34 634 57  HOH HOH A . 
C 3 HOH 35 635 4   HOH HOH A . 
C 3 HOH 36 636 45  HOH HOH A . 
C 3 HOH 37 637 20  HOH HOH A . 
C 3 HOH 38 638 81  HOH HOH A . 
C 3 HOH 39 639 55  HOH HOH A . 
C 3 HOH 40 640 35  HOH HOH A . 
C 3 HOH 41 641 80  HOH HOH A . 
C 3 HOH 42 642 62  HOH HOH A . 
C 3 HOH 43 643 65  HOH HOH A . 
C 3 HOH 44 644 6   HOH HOH A . 
C 3 HOH 45 645 10  HOH HOH A . 
C 3 HOH 46 646 78  HOH HOH A . 
C 3 HOH 47 647 59  HOH HOH A . 
C 3 HOH 48 648 67  HOH HOH A . 
C 3 HOH 49 649 12  HOH HOH A . 
C 3 HOH 50 650 70  HOH HOH A . 
C 3 HOH 51 651 61  HOH HOH A . 
C 3 HOH 52 652 36  HOH HOH A . 
C 3 HOH 53 653 24  HOH HOH A . 
C 3 HOH 54 654 32  HOH HOH A . 
C 3 HOH 55 655 60  HOH HOH A . 
C 3 HOH 56 656 23  HOH HOH A . 
C 3 HOH 57 657 16  HOH HOH A . 
C 3 HOH 58 658 29  HOH HOH A . 
C 3 HOH 59 659 39  HOH HOH A . 
C 3 HOH 60 660 69  HOH HOH A . 
C 3 HOH 61 661 15  HOH HOH A . 
C 3 HOH 62 662 30  HOH HOH A . 
C 3 HOH 63 663 49  HOH HOH A . 
C 3 HOH 64 664 19  HOH HOH A . 
C 3 HOH 65 665 64  HOH HOH A . 
C 3 HOH 66 666 74  HOH HOH A . 
C 3 HOH 67 667 27  HOH HOH A . 
C 3 HOH 68 668 75  HOH HOH A . 
C 3 HOH 69 669 37  HOH HOH A . 
C 3 HOH 70 670 48  HOH HOH A . 
C 3 HOH 71 671 42  HOH HOH A . 
C 3 HOH 72 672 38  HOH HOH A . 
C 3 HOH 73 673 41  HOH HOH A . 
C 3 HOH 74 674 53  HOH HOH A . 
C 3 HOH 75 675 68  HOH HOH A . 
C 3 HOH 76 676 66  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'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   109.39 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8RQV 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     48.757 
_cell.length_a_esd                 ? 
_cell.length_b                     70.279 
_cell.length_b_esd                 ? 
_cell.length_c                     59.889 
_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                         8RQV 
_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                   8RQV 
_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             2.42 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.18 
_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  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         2022-02-26 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   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                                       8RQV 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.19 
_reflns.d_resolution_low                               44.07 
_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                                     19524 
_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                           98.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.7 
_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                                   0.972 
_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                                    2.19 
_reflns_shell.d_res_low                                     2.26 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1647 
_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                                  0.402 
_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]                            0.01 
_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                               24.761 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.896 
_refine.correlation_coeff_Fo_to_Fc_free          0.873 
_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                                 8RQV 
_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                            2.19 
_refine.ls_d_res_low                             44.07 
_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                     18487 
_refine.ls_number_reflns_R_free                  1015 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.78 
_refine.ls_percent_reflns_R_free                 5.2 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.21970 
_refine.ls_R_factor_R_free                       0.26801 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.21709 
_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                       0.319 
_refine.pdbx_overall_ESU_R_Free                  0.239 
_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                             7.000 
_refine.overall_SU_ML                            0.176 
_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                       2.19 
_refine_hist.d_res_low                        44.07 
_refine_hist.number_atoms_solvent             76 
_refine_hist.number_atoms_total               2921 
_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        2814 
_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  2919 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.017  2704 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.663  1.648  3966 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.297  1.576  6291 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.649  5.000  346  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 38.391 22.628 156  ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 18.663 15.000 511  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 23.805 15.000 17   ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.077  0.200  380  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  3197 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  593  ? 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' ? 2.345  2.525  1384 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.344  2.524  1383 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.679  3.771  1727 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.678  3.772  1728 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.523  2.842  1535 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.523  2.842  1535 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.022  4.189  2239 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 8.035  29.650 3279 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 8.038  29.660 3273 ? 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                       2.190 
_refine_ls_shell.d_res_low                        2.247 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             80 
_refine_ls_shell.number_reflns_R_work             1336 
_refine_ls_shell.percent_reflns_obs               98.20 
_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                  0.232 
_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                  0.271 
# 
_struct.entry_id                     8RQV 
_struct.title                        'Erk2 MAP kinase (T188A) 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        8RQV 
_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              8RQV 
_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 8RQV ALA A 1   ? UNP P63086 ?   ?   'expression tag'      -6  1 
1 8RQV HIS A 2   ? UNP P63086 ?   ?   'expression tag'      -5  2 
1 8RQV HIS A 3   ? UNP P63086 ?   ?   'expression tag'      -4  3 
1 8RQV HIS A 4   ? UNP P63086 ?   ?   'expression tag'      -3  4 
1 8RQV HIS A 5   ? UNP P63086 ?   ?   'expression tag'      -2  5 
1 8RQV HIS A 6   ? UNP P63086 ?   ?   'expression tag'      -1  6 
1 8RQV HIS A 7   ? UNP P63086 ?   ?   'expression tag'      0   7 
1 8RQV ALA 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)' 790   ? 
1 MORE         -1    ? 
1 'SSA (A^2)'  16430 ? 
# 
_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 ? LYS A 122 ? LEU A 110 LYS A 115 1 ? 6  
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 ALA A 195 ? ARG A 199 ? ALA 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 ? ILE A 260 ? SER A 246 ILE A 253 1 ? 8  
HELX_P HELX_P11 AB2 ASN A 262 ? SER A 271 ? ASN A 255 SER A 264 1 ? 10 
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 ? HIS A 315 ? GLU A 301 HIS A 308 1 ? 8  
HELX_P HELX_P15 AB6 PRO A 316 ? GLU A 319 ? PRO A 309 GLU A 312 5 ? 4  
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  ? TYR A 35  ? TYR A 23  TYR A 28  
AA1 2 VAL A 44  ? ASP A 49  ? VAL A 37  ASP A 42  
AA1 3 ARG A 55  ? ILE A 61  ? ARG A 48  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                   8RQV 
_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 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   ARG 
_pdbx_validate_close_contact.auth_seq_id_1    22 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   ND2 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   ASN 
_pdbx_validate_close_contact.auth_seq_id_2    43 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.03 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     663 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     675 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_656 
_pdbx_validate_symm_contact.dist              2.06 
# 
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 GLU A 31  ? ? -146.81 -148.97 
2  1 ALA A 40  ? ? -170.94 144.85  
3  1 LYS A 46  ? ? 49.51   81.25   
4  1 VAL A 47  ? ? 177.45  136.25  
5  1 ASP A 165 ? ? 63.15   70.39   
6  1 ASP A 173 ? ? -156.53 62.81   
7  1 ASN A 199 ? ? -158.25 15.68   
8  1 SER A 221 ? ? -142.53 -3.12   
9  1 ASN A 222 ? ? 54.13   18.94   
10 1 LEU A 292 ? ? -103.42 59.24   
11 1 LYS A 338 ? ? -53.89  -8.99   
# 
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 GLU 10  ? A GLU 17  
12 1 Y 1 A MET 11  ? A MET 18  
13 1 Y 1 A VAL 12  ? A VAL 19  
14 1 Y 1 A ARG 13  ? A ARG 20  
15 1 Y 1 A GLY 14  ? A GLY 21  
16 1 Y 1 A GLY 355 ? A GLY 362 
17 1 Y 1 A TYR 356 ? A TYR 363 
18 1 Y 1 A ARG 357 ? A ARG 364 
19 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   8RLX 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8RQV 
_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]   0.020510 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.007219 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014229 
_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]   0.017702 
_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  ? -12.118 22.018  -8.363  1.00 48.66  ? 4   ALA A N     1 
ATOM   2    C CA    . ALA A 1 11  ? -11.286 21.566  -7.210  1.00 48.04  ? 4   ALA A CA    1 
ATOM   3    C C     . ALA A 1 11  ? -11.861 22.129  -5.903  1.00 49.44  ? 4   ALA A C     1 
ATOM   4    O O     . ALA A 1 11  ? -11.858 23.358  -5.759  1.00 46.50  ? 4   ALA A O     1 
ATOM   5    C CB    . ALA A 1 11  ? -9.865  22.025  -7.417  1.00 48.92  ? 4   ALA A CB    1 
ATOM   6    N N     . ALA A 1 12  ? -12.322 21.280  -4.972  1.00 50.63  ? 5   ALA A N     1 
ATOM   7    C CA    . ALA A 1 12  ? -12.760 21.714  -3.621  1.00 47.07  ? 5   ALA A CA    1 
ATOM   8    C C     . ALA A 1 12  ? -11.630 22.518  -2.962  1.00 45.49  ? 5   ALA A C     1 
ATOM   9    O O     . ALA A 1 12  ? -10.439 22.125  -3.081  1.00 38.01  ? 5   ALA A O     1 
ATOM   10   C CB    . ALA A 1 12  ? -13.171 20.536  -2.775  1.00 49.04  ? 5   ALA A CB    1 
ATOM   11   N N     . ALA A 1 13  ? -11.979 23.644  -2.338  1.00 45.52  ? 6   ALA A N     1 
ATOM   12   C CA    . ALA A 1 13  ? -11.037 24.511  -1.590  1.00 45.18  ? 6   ALA A CA    1 
ATOM   13   C C     . ALA A 1 13  ? -11.372 24.421  -0.099  1.00 44.07  ? 6   ALA A C     1 
ATOM   14   O O     . ALA A 1 13  ? -12.518 24.146  0.239   1.00 41.27  ? 6   ALA A O     1 
ATOM   15   C CB    . ALA A 1 13  ? -11.101 25.932  -2.099  1.00 42.57  ? 6   ALA A CB    1 
ATOM   16   N N     . ALA A 1 14  ? -10.376 24.618  0.754   1.00 45.83  ? 7   ALA A N     1 
ATOM   17   C CA    . ALA A 1 14  ? -10.492 24.510  2.221   1.00 46.97  ? 7   ALA A CA    1 
ATOM   18   C C     . ALA A 1 14  ? -9.673  25.645  2.838   1.00 46.53  ? 7   ALA A C     1 
ATOM   19   O O     . ALA A 1 14  ? -8.463  25.743  2.499   1.00 37.20  ? 7   ALA A O     1 
ATOM   20   C CB    . ALA A 1 14  ? -10.035 23.144  2.676   1.00 48.19  ? 7   ALA A CB    1 
ATOM   21   N N     . GLY A 1 15  ? -10.325 26.463  3.686   1.00 49.81  ? 8   GLY A N     1 
ATOM   22   C CA    . GLY A 1 15  ? -9.869  27.819  4.037   1.00 52.37  ? 8   GLY A CA    1 
ATOM   23   C C     . GLY A 1 15  ? -9.299  28.475  2.784   1.00 54.49  ? 8   GLY A C     1 
ATOM   24   O O     . GLY A 1 15  ? -8.106  28.763  2.734   1.00 44.97  ? 8   GLY A O     1 
ATOM   25   N N     . PRO A 1 16  ? -10.142 28.699  1.741   1.00 66.06  ? 9   PRO A N     1 
ATOM   26   C CA    . PRO A 1 16  ? -9.678  28.788  0.349   1.00 67.76  ? 9   PRO A CA    1 
ATOM   27   C C     . PRO A 1 16  ? -8.340  29.519  0.146   1.00 65.34  ? 9   PRO A C     1 
ATOM   28   O O     . PRO A 1 16  ? -7.375  28.829  -0.158  1.00 61.98  ? 9   PRO A O     1 
ATOM   29   C CB    . PRO A 1 16  ? -10.832 29.539  -0.337  1.00 68.95  ? 9   PRO A CB    1 
ATOM   30   C CG    . PRO A 1 16  ? -12.066 29.069  0.417   1.00 67.48  ? 9   PRO A CG    1 
ATOM   31   C CD    . PRO A 1 16  ? -11.599 28.915  1.852   1.00 67.41  ? 9   PRO A CD    1 
ATOM   32   N N     . GLN A 1 22  ? -6.704  26.748  0.580   1.00 44.83  ? 15  GLN A N     1 
ATOM   33   C CA    . GLN A 1 22  ? -5.952  26.213  -0.587  1.00 43.24  ? 15  GLN A CA    1 
ATOM   34   C C     . GLN A 1 22  ? -6.774  25.126  -1.291  1.00 38.30  ? 15  GLN A C     1 
ATOM   35   O O     . GLN A 1 22  ? -7.927  24.837  -0.895  1.00 42.04  ? 15  GLN A O     1 
ATOM   36   C CB    . GLN A 1 22  ? -4.593  25.646  -0.144  1.00 47.38  ? 15  GLN A CB    1 
ATOM   37   C CG    . GLN A 1 22  ? -3.375  26.454  -0.597  1.00 54.57  ? 15  GLN A CG    1 
ATOM   38   C CD    . GLN A 1 22  ? -2.828  26.132  -1.975  1.00 57.90  ? 15  GLN A CD    1 
ATOM   39   O OE1   . GLN A 1 22  ? -2.121  26.937  -2.585  1.00 56.33  ? 15  GLN A OE1   1 
ATOM   40   N NE2   . GLN A 1 22  ? -3.121  24.941  -2.476  1.00 57.09  ? 15  GLN A NE2   1 
ATOM   41   N N     . VAL A 1 23  ? -6.172  24.529  -2.305  1.00 33.43  ? 16  VAL A N     1 
ATOM   42   C CA    . VAL A 1 23  ? -6.639  23.269  -2.937  1.00 32.73  ? 16  VAL A CA    1 
ATOM   43   C C     . VAL A 1 23  ? -6.645  22.147  -1.890  1.00 30.40  ? 16  VAL A C     1 
ATOM   44   O O     . VAL A 1 23  ? -5.610  21.937  -1.223  1.00 28.65  ? 16  VAL A O     1 
ATOM   45   C CB    . VAL A 1 23  ? -5.730  22.904  -4.124  1.00 34.48  ? 16  VAL A CB    1 
ATOM   46   C CG1   . VAL A 1 23  ? -6.189  21.626  -4.805  1.00 36.61  ? 16  VAL A CG1   1 
ATOM   47   C CG2   . VAL A 1 23  ? -5.645  24.047  -5.120  1.00 36.34  ? 16  VAL A CG2   1 
ATOM   48   N N     . PHE A 1 24  ? -7.762  21.436  -1.782  1.00 28.34  ? 17  PHE A N     1 
ATOM   49   C CA    . PHE A 1 24  ? -7.918  20.188  -0.998  1.00 28.35  ? 17  PHE A CA    1 
ATOM   50   C C     . PHE A 1 24  ? -8.752  19.224  -1.857  1.00 28.54  ? 17  PHE A C     1 
ATOM   51   O O     . PHE A 1 24  ? -9.928  18.947  -1.561  1.00 28.21  ? 17  PHE A O     1 
ATOM   52   C CB    . PHE A 1 24  ? -8.510  20.492  0.380   1.00 28.67  ? 17  PHE A CB    1 
ATOM   53   C CG    . PHE A 1 24  ? -8.316  19.372  1.373   1.00 27.98  ? 17  PHE A CG    1 
ATOM   54   C CD1   . PHE A 1 24  ? -9.035  18.190  1.265   1.00 27.96  ? 17  PHE A CD1   1 
ATOM   55   C CD2   . PHE A 1 24  ? -7.379  19.485  2.384   1.00 27.55  ? 17  PHE A CD2   1 
ATOM   56   C CE1   . PHE A 1 24  ? -8.832  17.153  2.159   1.00 27.87  ? 17  PHE A CE1   1 
ATOM   57   C CE2   . PHE A 1 24  ? -7.182  18.452  3.283   1.00 28.76  ? 17  PHE A CE2   1 
ATOM   58   C CZ    . PHE A 1 24  ? -7.900  17.285  3.159   1.00 29.42  ? 17  PHE A CZ    1 
ATOM   59   N N     . ASP A 1 25  ? -8.124  18.737  -2.921  1.00 26.56  ? 18  ASP A N     1 
ATOM   60   C CA    . ASP A 1 25  ? -8.775  18.087  -4.081  1.00 26.33  ? 18  ASP A CA    1 
ATOM   61   C C     . ASP A 1 25  ? -8.905  16.585  -3.830  1.00 25.79  ? 18  ASP A C     1 
ATOM   62   O O     . ASP A 1 25  ? -8.222  15.783  -4.456  1.00 24.87  ? 18  ASP A O     1 
ATOM   63   C CB    . ASP A 1 25  ? -7.997  18.377  -5.365  1.00 27.77  ? 18  ASP A CB    1 
ATOM   64   C CG    . ASP A 1 25  ? -8.667  17.800  -6.582  1.00 26.69  ? 18  ASP A CG    1 
ATOM   65   O OD1   . ASP A 1 25  ? -9.911  17.612  -6.544  1.00 28.06  ? 18  ASP A OD1   1 
ATOM   66   O OD2   . ASP A 1 25  ? -7.932  17.491  -7.523  1.00 33.37  ? 18  ASP A OD2   1 
ATOM   67   N N     . VAL A 1 26  ? -9.811  16.226  -2.947  1.00 30.41  ? 19  VAL A N     1 
ATOM   68   C CA    . VAL A 1 26  ? -10.127 14.808  -2.640  1.00 33.58  ? 19  VAL A CA    1 
ATOM   69   C C     . VAL A 1 26  ? -11.346 14.502  -3.501  1.00 40.18  ? 19  VAL A C     1 
ATOM   70   O O     . VAL A 1 26  ? -12.135 13.624  -3.131  1.00 39.46  ? 19  VAL A O     1 
ATOM   71   C CB    . VAL A 1 26  ? -10.298 14.586  -1.124  1.00 31.11  ? 19  VAL A CB    1 
ATOM   72   C CG1   . VAL A 1 26  ? -8.963  14.749  -0.419  1.00 28.59  ? 19  VAL A CG1   1 
ATOM   73   C CG2   . VAL A 1 26  ? -11.338 15.511  -0.491  1.00 33.31  ? 19  VAL A CG2   1 
ATOM   74   N N     . GLY A 1 27  ? -11.443 15.245  -4.622  1.00 53.26  ? 20  GLY A N     1 
ATOM   75   C CA    . GLY A 1 27  ? -12.410 15.070  -5.726  1.00 50.76  ? 20  GLY A CA    1 
ATOM   76   C C     . GLY A 1 27  ? -13.772 14.672  -5.177  1.00 52.78  ? 20  GLY A C     1 
ATOM   77   O O     . GLY A 1 27  ? -14.074 14.949  -4.020  1.00 50.62  ? 20  GLY A O     1 
ATOM   78   N N     . PRO A 1 28  ? -14.622 13.979  -5.961  1.00 51.25  ? 21  PRO A N     1 
ATOM   79   C CA    . PRO A 1 28  ? -15.997 13.734  -5.524  1.00 43.72  ? 21  PRO A CA    1 
ATOM   80   C C     . PRO A 1 28  ? -16.201 12.744  -4.352  1.00 38.45  ? 21  PRO A C     1 
ATOM   81   O O     . PRO A 1 28  ? -17.217 12.877  -3.679  1.00 33.99  ? 21  PRO A O     1 
ATOM   82   C CB    . PRO A 1 28  ? -16.647 13.203  -6.821  1.00 47.48  ? 21  PRO A CB    1 
ATOM   83   C CG    . PRO A 1 28  ? -15.508 12.541  -7.569  1.00 47.52  ? 21  PRO A CG    1 
ATOM   84   C CD    . PRO A 1 28  ? -14.316 13.432  -7.297  1.00 47.32  ? 21  PRO A CD    1 
ATOM   85   N N     . ARG A 1 29  ? -15.318 11.757  -4.130  1.00 33.98  ? 22  ARG A N     1 
ATOM   86   C CA    . ARG A 1 29  ? -15.615 10.659  -3.159  1.00 32.29  ? 22  ARG A CA    1 
ATOM   87   C C     . ARG A 1 29  ? -15.713 11.241  -1.739  1.00 31.64  ? 22  ARG A C     1 
ATOM   88   O O     . ARG A 1 29  ? -16.546 10.754  -0.940  1.00 33.55  ? 22  ARG A O     1 
ATOM   89   C CB    . ARG A 1 29  ? -14.582 9.535   -3.185  1.00 29.59  ? 22  ARG A CB    1 
ATOM   90   C CG    . ARG A 1 29  ? -14.730 8.559   -2.028  1.00 30.25  ? 22  ARG A CG    1 
ATOM   91   C CD    . ARG A 1 29  ? -14.033 7.240   -2.256  1.00 29.90  ? 22  ARG A CD    1 
ATOM   92   N NE    . ARG A 1 29  ? -13.961 6.434   -1.058  1.00 29.31  ? 22  ARG A NE    1 
ATOM   93   C CZ    . ARG A 1 29  ? -13.293 5.286   -0.943  1.00 30.24  ? 22  ARG A CZ    1 
ATOM   94   N NH1   . ARG A 1 29  ? -12.608 4.803   -1.959  1.00 31.76  ? 22  ARG A NH1   1 
ATOM   95   N NH2   . ARG A 1 29  ? -13.295 4.624   0.196   1.00 30.81  ? 22  ARG A NH2   1 
ATOM   96   N N     . TYR A 1 30  ? -14.918 12.257  -1.438  1.00 28.78  ? 23  TYR A N     1 
ATOM   97   C CA    . TYR A 1 30  ? -14.781 12.813  -0.074  1.00 33.02  ? 23  TYR A CA    1 
ATOM   98   C C     . TYR A 1 30  ? -15.282 14.274  -0.084  1.00 34.43  ? 23  TYR A C     1 
ATOM   99   O O     . TYR A 1 30  ? -14.654 15.144  -0.762  1.00 34.08  ? 23  TYR A O     1 
ATOM   100  C CB    . TYR A 1 30  ? -13.340 12.579  0.409   1.00 30.54  ? 23  TYR A CB    1 
ATOM   101  C CG    . TYR A 1 30  ? -12.854 11.140  0.384   1.00 29.61  ? 23  TYR A CG    1 
ATOM   102  C CD1   . TYR A 1 30  ? -13.224 10.219  1.360   1.00 27.51  ? 23  TYR A CD1   1 
ATOM   103  C CD2   . TYR A 1 30  ? -11.960 10.706  -0.588  1.00 27.23  ? 23  TYR A CD2   1 
ATOM   104  C CE1   . TYR A 1 30  ? -12.752 8.911   1.344   1.00 26.68  ? 23  TYR A CE1   1 
ATOM   105  C CE2   . TYR A 1 30  ? -11.485 9.405   -0.621  1.00 26.32  ? 23  TYR A CE2   1 
ATOM   106  C CZ    . TYR A 1 30  ? -11.866 8.505   0.358   1.00 26.03  ? 23  TYR A CZ    1 
ATOM   107  O OH    . TYR A 1 30  ? -11.357 7.241   0.317   1.00 21.34  ? 23  TYR A OH    1 
ATOM   108  N N     . THR A 1 31  ? -16.365 14.540  0.665   1.00 34.60  ? 24  THR A N     1 
ATOM   109  C CA    . THR A 1 31  ? -17.142 15.818  0.632   1.00 40.27  ? 24  THR A CA    1 
ATOM   110  C C     . THR A 1 31  ? -17.244 16.439  2.030   1.00 36.69  ? 24  THR A C     1 
ATOM   111  O O     . THR A 1 31  ? -16.683 15.876  2.959   1.00 29.18  ? 24  THR A O     1 
ATOM   112  C CB    . THR A 1 31  ? -18.546 15.614  0.037   1.00 39.80  ? 24  THR A CB    1 
ATOM   113  O OG1   . THR A 1 31  ? -18.807 14.219  -0.112  1.00 39.15  ? 24  THR A OG1   1 
ATOM   114  C CG2   . THR A 1 31  ? -18.697 16.274  -1.315  1.00 44.40  ? 24  THR A CG2   1 
ATOM   115  N N     . ASN A 1 32  ? -17.911 17.592  2.139   1.00 40.42  ? 25  ASN A N     1 
ATOM   116  C CA    . ASN A 1 32  ? -18.236 18.257  3.433   1.00 42.93  ? 25  ASN A CA    1 
ATOM   117  C C     . ASN A 1 32  ? -16.945 18.366  4.254   1.00 41.20  ? 25  ASN A C     1 
ATOM   118  O O     . ASN A 1 32  ? -16.897 17.857  5.389   1.00 37.20  ? 25  ASN A O     1 
ATOM   119  C CB    . ASN A 1 32  ? -19.371 17.516  4.147   1.00 43.28  ? 25  ASN A CB    1 
ATOM   120  C CG    . ASN A 1 32  ? -20.495 17.188  3.189   1.00 44.22  ? 25  ASN A CG    1 
ATOM   121  O OD1   . ASN A 1 32  ? -21.316 18.043  2.875   1.00 42.41  ? 25  ASN A OD1   1 
ATOM   122  N ND2   . ASN A 1 32  ? -20.520 15.962  2.693   1.00 51.91  ? 25  ASN A ND2   1 
ATOM   123  N N     . LEU A 1 33  ? -15.923 18.966  3.649   1.00 38.79  ? 26  LEU A N     1 
ATOM   124  C CA    . LEU A 1 33  ? -14.605 19.217  4.275   1.00 41.90  ? 26  LEU A CA    1 
ATOM   125  C C     . LEU A 1 33  ? -14.796 20.200  5.431   1.00 43.30  ? 26  LEU A C     1 
ATOM   126  O O     . LEU A 1 33  ? -15.736 21.012  5.365   1.00 48.36  ? 26  LEU A O     1 
ATOM   127  C CB    . LEU A 1 33  ? -13.642 19.788  3.229   1.00 40.64  ? 26  LEU A CB    1 
ATOM   128  C CG    . LEU A 1 33  ? -12.934 18.791  2.310   1.00 38.92  ? 26  LEU A CG    1 
ATOM   129  C CD1   . LEU A 1 33  ? -13.781 17.555  2.056   1.00 37.93  ? 26  LEU A CD1   1 
ATOM   130  C CD2   . LEU A 1 33  ? -12.551 19.472  0.999   1.00 37.30  ? 26  LEU A CD2   1 
ATOM   131  N N     . SER A 1 34  ? -13.939 20.112  6.445   1.00 39.59  ? 27  SER A N     1 
ATOM   132  C CA    . SER A 1 34  ? -13.802 21.121  7.524   1.00 40.05  ? 27  SER A CA    1 
ATOM   133  C C     . SER A 1 34  ? -12.386 21.057  8.109   1.00 38.35  ? 27  SER A C     1 
ATOM   134  O O     . SER A 1 34  ? -11.872 19.940  8.349   1.00 39.49  ? 27  SER A O     1 
ATOM   135  C CB    . SER A 1 34  ? -14.871 20.947  8.572   1.00 41.19  ? 27  SER A CB    1 
ATOM   136  O OG    . SER A 1 34  ? -16.054 21.620  8.167   1.00 45.68  ? 27  SER A OG    1 
ATOM   137  N N     . TYR A 1 35  ? -11.778 22.226  8.288   1.00 38.89  ? 28  TYR A N     1 
ATOM   138  C CA    . TYR A 1 35  ? -10.472 22.415  8.954   1.00 41.68  ? 28  TYR A CA    1 
ATOM   139  C C     . TYR A 1 35  ? -10.497 21.656  10.285  1.00 47.57  ? 28  TYR A C     1 
ATOM   140  O O     . TYR A 1 35  ? -11.495 21.810  11.055  1.00 42.10  ? 28  TYR A O     1 
ATOM   141  C CB    . TYR A 1 35  ? -10.224 23.907  9.175   1.00 43.76  ? 28  TYR A CB    1 
ATOM   142  C CG    . TYR A 1 35  ? -8.787  24.315  9.394   1.00 45.65  ? 28  TYR A CG    1 
ATOM   143  C CD1   . TYR A 1 35  ? -7.856  24.200  8.379   1.00 43.87  ? 28  TYR A CD1   1 
ATOM   144  C CD2   . TYR A 1 35  ? -8.370  24.879  10.594  1.00 48.22  ? 28  TYR A CD2   1 
ATOM   145  C CE1   . TYR A 1 35  ? -6.541  24.591  8.558   1.00 43.97  ? 28  TYR A CE1   1 
ATOM   146  C CE2   . TYR A 1 35  ? -7.062  25.293  10.788  1.00 44.80  ? 28  TYR A CE2   1 
ATOM   147  C CZ    . TYR A 1 35  ? -6.144  25.144  9.763   1.00 47.27  ? 28  TYR A CZ    1 
ATOM   148  O OH    . TYR A 1 35  ? -4.847  25.540  9.923   1.00 46.64  ? 28  TYR A OH    1 
ATOM   149  N N     . ILE A 1 36  ? -9.464  20.841  10.531  1.00 45.10  ? 29  ILE A N     1 
ATOM   150  C CA    . ILE A 1 36  ? -9.093  20.358  11.893  1.00 47.26  ? 29  ILE A CA    1 
ATOM   151  C C     . ILE A 1 36  ? -7.565  20.372  12.010  1.00 48.77  ? 29  ILE A C     1 
ATOM   152  O O     . ILE A 1 36  ? -6.984  19.291  12.183  1.00 52.20  ? 29  ILE A O     1 
ATOM   153  C CB    . ILE A 1 36  ? -9.709  18.973  12.199  1.00 45.80  ? 29  ILE A CB    1 
ATOM   154  C CG1   . ILE A 1 36  ? -9.666  18.043  10.991  1.00 42.31  ? 29  ILE A CG1   1 
ATOM   155  C CG2   . ILE A 1 36  ? -11.127 19.112  12.736  1.00 48.44  ? 29  ILE A CG2   1 
ATOM   156  C CD1   . ILE A 1 36  ? -10.041 16.616  11.300  1.00 41.67  ? 29  ILE A CD1   1 
ATOM   157  N N     . GLY A 1 37  ? -6.954  21.557  11.898  1.00 49.72  ? 30  GLY A N     1 
ATOM   158  C CA    . GLY A 1 37  ? -5.512  21.791  12.126  1.00 52.64  ? 30  GLY A CA    1 
ATOM   159  C C     . GLY A 1 37  ? -4.687  21.749  10.847  1.00 50.98  ? 30  GLY A C     1 
ATOM   160  O O     . GLY A 1 37  ? -5.275  21.512  9.771   1.00 56.24  ? 30  GLY A O     1 
ATOM   161  N N     . GLU A 1 38  ? -3.369  21.960  10.973  1.00 52.68  ? 31  GLU A N     1 
ATOM   162  C CA    . GLU A 1 38  ? -2.388  22.145  9.860   1.00 56.60  ? 31  GLU A CA    1 
ATOM   163  C C     . GLU A 1 38  ? -1.040  21.543  10.297  1.00 57.30  ? 31  GLU A C     1 
ATOM   164  O O     . GLU A 1 38  ? -1.064  20.569  11.080  1.00 55.56  ? 31  GLU A O     1 
ATOM   165  C CB    . GLU A 1 38  ? -2.283  23.636  9.509   1.00 58.55  ? 31  GLU A CB    1 
ATOM   166  C CG    . GLU A 1 38  ? -2.142  23.925  8.021   1.00 60.96  ? 31  GLU A CG    1 
ATOM   167  C CD    . GLU A 1 38  ? -2.551  25.330  7.597   1.00 60.43  ? 31  GLU A CD    1 
ATOM   168  O OE1   . GLU A 1 38  ? -3.346  25.459  6.636   1.00 57.22  ? 31  GLU A OE1   1 
ATOM   169  O OE2   . GLU A 1 38  ? -2.074  26.294  8.227   1.00 56.51  ? 31  GLU A OE2   1 
ATOM   170  N N     . GLY A 1 39  ? 0.094   22.083  9.832   1.00 57.97  ? 32  GLY A N     1 
ATOM   171  C CA    . GLY A 1 39  ? 1.427   21.615  10.265  1.00 61.71  ? 32  GLY A CA    1 
ATOM   172  C C     . GLY A 1 39  ? 2.553   22.147  9.398   1.00 67.71  ? 32  GLY A C     1 
ATOM   173  O O     . GLY A 1 39  ? 2.448   23.302  8.929   1.00 70.42  ? 32  GLY A O     1 
ATOM   174  N N     . ALA A 1 40  ? 3.602   21.339  9.205   1.00 70.37  ? 33  ALA A N     1 
ATOM   175  C CA    . ALA A 1 40  ? 4.844   21.715  8.488   1.00 72.23  ? 33  ALA A CA    1 
ATOM   176  C C     . ALA A 1 40  ? 4.922   20.988  7.143   1.00 79.80  ? 33  ALA A C     1 
ATOM   177  O O     . ALA A 1 40  ? 5.906   21.263  6.406   1.00 85.28  ? 33  ALA A O     1 
ATOM   178  C CB    . ALA A 1 40  ? 6.056   21.408  9.336   1.00 71.81  ? 33  ALA A CB    1 
ATOM   179  N N     . TYR A 1 41  ? 3.958   20.099  6.836   1.00 76.18  ? 34  TYR A N     1 
ATOM   180  C CA    . TYR A 1 41  ? 3.902   19.307  5.571   1.00 67.29  ? 34  TYR A CA    1 
ATOM   181  C C     . TYR A 1 41  ? 2.635   19.646  4.777   1.00 56.56  ? 34  TYR A C     1 
ATOM   182  O O     . TYR A 1 41  ? 2.742   19.890  3.548   1.00 43.01  ? 34  TYR A O     1 
ATOM   183  C CB    . TYR A 1 41  ? 4.045   17.816  5.874   1.00 68.97  ? 34  TYR A CB    1 
ATOM   184  C CG    . TYR A 1 41  ? 5.473   17.420  6.145   1.00 73.99  ? 34  TYR A CG    1 
ATOM   185  C CD1   . TYR A 1 41  ? 6.323   18.286  6.815   1.00 76.13  ? 34  TYR A CD1   1 
ATOM   186  C CD2   . TYR A 1 41  ? 5.985   16.197  5.748   1.00 72.15  ? 34  TYR A CD2   1 
ATOM   187  C CE1   . TYR A 1 41  ? 7.639   17.962  7.079   1.00 80.44  ? 34  TYR A CE1   1 
ATOM   188  C CE2   . TYR A 1 41  ? 7.300   15.848  6.018   1.00 74.47  ? 34  TYR A CE2   1 
ATOM   189  C CZ    . TYR A 1 41  ? 8.130   16.735  6.685   1.00 75.51  ? 34  TYR A CZ    1 
ATOM   190  O OH    . TYR A 1 41  ? 9.434   16.452  6.969   1.00 80.15  ? 34  TYR A OH    1 
ATOM   191  N N     . GLY A 1 42  ? 1.482   19.682  5.451   1.00 45.05  ? 35  GLY A N     1 
ATOM   192  C CA    . GLY A 1 42  ? 0.240   20.207  4.855   1.00 43.90  ? 35  GLY A CA    1 
ATOM   193  C C     . GLY A 1 42  ? -0.882  20.323  5.866   1.00 39.70  ? 35  GLY A C     1 
ATOM   194  O O     . GLY A 1 42  ? -0.591  20.397  7.060   1.00 40.17  ? 35  GLY A O     1 
ATOM   195  N N     . MET A 1 43  ? -2.125  20.341  5.392   1.00 40.01  ? 36  MET A N     1 
ATOM   196  C CA    . MET A 1 43  ? -3.308  20.620  6.235   1.00 41.33  ? 36  MET A CA    1 
ATOM   197  C C     . MET A 1 43  ? -4.152  19.347  6.379   1.00 39.40  ? 36  MET A C     1 
ATOM   198  O O     . MET A 1 43  ? -4.095  18.468  5.517   1.00 37.78  ? 36  MET A O     1 
ATOM   199  C CB    . MET A 1 43  ? -4.141  21.786  5.685   1.00 42.40  ? 36  MET A CB    1 
ATOM   200  C CG    . MET A 1 43  ? -5.093  21.426  4.571   1.00 46.66  ? 36  MET A CG    1 
ATOM   201  S SD    . MET A 1 43  ? -6.526  22.529  4.515   1.00 58.06  ? 36  MET A SD    1 
ATOM   202  C CE    . MET A 1 43  ? -5.785  23.996  3.796   1.00 59.20  ? 36  MET A CE    1 
ATOM   203  N N     . VAL A 1 44  ? -4.870  19.259  7.489   1.00 39.56  ? 37  VAL A N     1 
ATOM   204  C CA    . VAL A 1 44  ? -5.717  18.098  7.855   1.00 39.11  ? 37  VAL A CA    1 
ATOM   205  C C     . VAL A 1 44  ? -7.165  18.572  7.845   1.00 38.53  ? 37  VAL A C     1 
ATOM   206  O O     . VAL A 1 44  ? -7.431  19.723  8.253   1.00 39.44  ? 37  VAL A O     1 
ATOM   207  C CB    . VAL A 1 44  ? -5.307  17.519  9.216   1.00 37.41  ? 37  VAL A CB    1 
ATOM   208  C CG1   . VAL A 1 44  ? -6.250  16.407  9.652   1.00 37.40  ? 37  VAL A CG1   1 
ATOM   209  C CG2   . VAL A 1 44  ? -3.868  17.035  9.174   1.00 36.87  ? 37  VAL A CG2   1 
ATOM   210  N N     . CYS A 1 45  ? -8.042  17.719  7.343   1.00 38.10  ? 38  CYS A N     1 
ATOM   211  C CA    . CYS A 1 45  ? -9.481  18.000  7.185   1.00 37.46  ? 38  CYS A CA    1 
ATOM   212  C C     . CYS A 1 45  ? -10.274 16.786  7.627   1.00 36.32  ? 38  CYS A C     1 
ATOM   213  O O     . CYS A 1 45  ? -9.761  15.672  7.470   1.00 37.35  ? 38  CYS A O     1 
ATOM   214  C CB    . CYS A 1 45  ? -9.808  18.306  5.736   1.00 38.49  ? 38  CYS A CB    1 
ATOM   215  S SG    . CYS A 1 45  ? -9.668  20.071  5.388   1.00 40.66  ? 38  CYS A SG    1 
ATOM   216  N N     . SER A 1 46  ? -11.463 17.022  8.173   1.00 35.20  ? 39  SER A N     1 
ATOM   217  C CA    . SER A 1 46  ? -12.561 16.025  8.281   1.00 35.82  ? 39  SER A CA    1 
ATOM   218  C C     . SER A 1 46  ? -13.222 15.954  6.896   1.00 33.68  ? 39  SER A C     1 
ATOM   219  O O     . SER A 1 46  ? -13.079 16.921  6.157   1.00 26.87  ? 39  SER A O     1 
ATOM   220  C CB    . SER A 1 46  ? -13.537 16.450  9.357   1.00 33.91  ? 39  SER A CB    1 
ATOM   221  O OG    . SER A 1 46  ? -13.702 17.872  9.313   1.00 32.55  ? 39  SER A OG    1 
ATOM   222  N N     . ALA A 1 47  ? -13.936 14.886  6.559   1.00 33.76  ? 40  ALA A N     1 
ATOM   223  C CA    . ALA A 1 47  ? -14.600 14.783  5.242   1.00 36.48  ? 40  ALA A CA    1 
ATOM   224  C C     . ALA A 1 47  ? -15.515 13.569  5.230   1.00 39.84  ? 40  ALA A C     1 
ATOM   225  O O     . ALA A 1 47  ? -15.141 12.558  5.853   1.00 38.15  ? 40  ALA A O     1 
ATOM   226  C CB    . ALA A 1 47  ? -13.575 14.672  4.141   1.00 37.37  ? 40  ALA A CB    1 
ATOM   227  N N     . TYR A 1 48  ? -16.652 13.685  4.535   1.00 40.85  ? 41  TYR A N     1 
ATOM   228  C CA    . TYR A 1 48  ? -17.653 12.604  4.363   1.00 39.49  ? 41  TYR A CA    1 
ATOM   229  C C     . TYR A 1 48  ? -17.195 11.685  3.233   1.00 38.76  ? 41  TYR A C     1 
ATOM   230  O O     . TYR A 1 48  ? -16.991 12.196  2.110   1.00 34.07  ? 41  TYR A O     1 
ATOM   231  C CB    . TYR A 1 48  ? -19.048 13.174  4.087   1.00 44.99  ? 41  TYR A CB    1 
ATOM   232  C CG    . TYR A 1 48  ? -20.124 12.116  4.064   1.00 49.28  ? 41  TYR A CG    1 
ATOM   233  C CD1   . TYR A 1 48  ? -20.370 11.333  5.179   1.00 51.92  ? 41  TYR A CD1   1 
ATOM   234  C CD2   . TYR A 1 48  ? -20.860 11.858  2.918   1.00 52.03  ? 41  TYR A CD2   1 
ATOM   235  C CE1   . TYR A 1 48  ? -21.330 10.335  5.166   1.00 53.68  ? 41  TYR A CE1   1 
ATOM   236  C CE2   . TYR A 1 48  ? -21.824 10.867  2.886   1.00 49.56  ? 41  TYR A CE2   1 
ATOM   237  C CZ    . TYR A 1 48  ? -22.063 10.109  4.016   1.00 53.62  ? 41  TYR A CZ    1 
ATOM   238  O OH    . TYR A 1 48  ? -23.016 9.134   4.001   1.00 59.52  ? 41  TYR A OH    1 
ATOM   239  N N     . ASP A 1 49  ? -17.025 10.391  3.534   1.00 38.21  ? 42  ASP A N     1 
ATOM   240  C CA    . ASP A 1 49  ? -16.681 9.338   2.546   1.00 36.28  ? 42  ASP A CA    1 
ATOM   241  C C     . ASP A 1 49  ? -17.985 8.826   1.949   1.00 39.80  ? 42  ASP A C     1 
ATOM   242  O O     . ASP A 1 49  ? -18.658 8.010   2.614   1.00 39.94  ? 42  ASP A O     1 
ATOM   243  C CB    . ASP A 1 49  ? -15.913 8.160   3.151   1.00 38.83  ? 42  ASP A CB    1 
ATOM   244  C CG    . ASP A 1 49  ? -15.656 7.027   2.163   1.00 40.74  ? 42  ASP A CG    1 
ATOM   245  O OD1   . ASP A 1 49  ? -16.123 7.147   0.997   1.00 39.87  ? 42  ASP A OD1   1 
ATOM   246  O OD2   . ASP A 1 49  ? -14.976 6.034   2.554   1.00 39.34  ? 42  ASP A OD2   1 
ATOM   247  N N     . ASN A 1 50  ? -18.282 9.248   0.718   1.00 42.24  ? 43  ASN A N     1 
ATOM   248  C CA    . ASN A 1 50  ? -19.554 8.959   0.001   1.00 41.82  ? 43  ASN A CA    1 
ATOM   249  C C     . ASN A 1 50  ? -19.613 7.473   -0.396  1.00 44.28  ? 43  ASN A C     1 
ATOM   250  O O     . ASN A 1 50  ? -20.598 7.095   -1.026  1.00 53.74  ? 43  ASN A O     1 
ATOM   251  C CB    . ASN A 1 50  ? -19.732 9.864   -1.223  1.00 39.63  ? 43  ASN A CB    1 
ATOM   252  C CG    . ASN A 1 50  ? -19.530 11.338  -0.926  1.00 43.16  ? 43  ASN A CG    1 
ATOM   253  O OD1   . ASN A 1 50  ? -20.476 12.114  -0.911  1.00 48.60  ? 43  ASN A OD1   1 
ATOM   254  N ND2   . ASN A 1 50  ? -18.300 11.752  -0.682  1.00 45.06  ? 43  ASN A ND2   1 
ATOM   255  N N     . LEU A 1 51  ? -18.628 6.648   -0.034  1.00 46.91  ? 44  LEU A N     1 
ATOM   256  C CA    . LEU A 1 51  ? -18.582 5.212   -0.423  1.00 49.86  ? 44  LEU A CA    1 
ATOM   257  C C     . LEU A 1 51  ? -18.824 4.337   0.808   1.00 54.48  ? 44  LEU A C     1 
ATOM   258  O O     . LEU A 1 51  ? -19.437 3.267   0.642   1.00 55.64  ? 44  LEU A O     1 
ATOM   259  C CB    . LEU A 1 51  ? -17.219 4.914   -1.060  1.00 54.43  ? 44  LEU A CB    1 
ATOM   260  C CG    . LEU A 1 51  ? -17.084 3.619   -1.869  1.00 57.64  ? 44  LEU A CG    1 
ATOM   261  C CD1   . LEU A 1 51  ? -16.520 2.478   -1.033  1.00 58.01  ? 44  LEU A CD1   1 
ATOM   262  C CD2   . LEU A 1 51  ? -18.400 3.207   -2.507  1.00 60.54  ? 44  LEU A CD2   1 
ATOM   263  N N     . ASN A 1 52  ? -18.346 4.765   1.984   1.00 51.74  ? 45  ASN A N     1 
ATOM   264  C CA    . ASN A 1 52  ? -18.481 4.015   3.261   1.00 47.64  ? 45  ASN A CA    1 
ATOM   265  C C     . ASN A 1 52  ? -19.445 4.708   4.222   1.00 47.47  ? 45  ASN A C     1 
ATOM   266  O O     . ASN A 1 52  ? -19.723 4.125   5.284   1.00 46.27  ? 45  ASN A O     1 
ATOM   267  C CB    . ASN A 1 52  ? -17.131 3.844   3.942   1.00 47.62  ? 45  ASN A CB    1 
ATOM   268  C CG    . ASN A 1 52  ? -16.222 2.943   3.146   1.00 47.63  ? 45  ASN A CG    1 
ATOM   269  O OD1   . ASN A 1 52  ? -15.124 2.635   3.596   1.00 51.71  ? 45  ASN A OD1   1 
ATOM   270  N ND2   . ASN A 1 52  ? -16.686 2.500   1.985   1.00 41.96  ? 45  ASN A ND2   1 
ATOM   271  N N     . LYS A 1 53  ? -19.926 5.900   3.876   1.00 48.65  ? 46  LYS A N     1 
ATOM   272  C CA    . LYS A 1 53  ? -20.927 6.637   4.687   1.00 50.41  ? 46  LYS A CA    1 
ATOM   273  C C     . LYS A 1 53  ? -20.427 6.654   6.134   1.00 52.12  ? 46  LYS A C     1 
ATOM   274  O O     . LYS A 1 53  ? -20.867 5.814   6.945   1.00 59.26  ? 46  LYS A O     1 
ATOM   275  C CB    . LYS A 1 53  ? -22.301 5.985   4.516   1.00 50.07  ? 46  LYS A CB    1 
ATOM   276  C CG    . LYS A 1 53  ? -22.584 5.439   3.121   1.00 52.06  ? 46  LYS A CG    1 
ATOM   277  C CD    . LYS A 1 53  ? -22.375 6.436   1.985   1.00 53.50  ? 46  LYS A CD    1 
ATOM   278  C CE    . LYS A 1 53  ? -23.642 6.753   1.213   1.00 54.12  ? 46  LYS A CE    1 
ATOM   279  N NZ    . LYS A 1 53  ? -24.171 5.544   0.538   1.00 53.27  ? 46  LYS A NZ    1 
ATOM   280  N N     . VAL A 1 54  ? -19.516 7.584   6.405   1.00 47.90  ? 47  VAL A N     1 
ATOM   281  C CA    . VAL A 1 54  ? -18.671 7.701   7.627   1.00 41.96  ? 47  VAL A CA    1 
ATOM   282  C C     . VAL A 1 54  ? -17.766 8.906   7.379   1.00 37.74  ? 47  VAL A C     1 
ATOM   283  O O     . VAL A 1 54  ? -17.264 9.044   6.243   1.00 37.30  ? 47  VAL A O     1 
ATOM   284  C CB    . VAL A 1 54  ? -17.813 6.448   7.874   1.00 43.28  ? 47  VAL A CB    1 
ATOM   285  C CG1   . VAL A 1 54  ? -18.625 5.251   8.365   1.00 43.75  ? 47  VAL A CG1   1 
ATOM   286  C CG2   . VAL A 1 54  ? -16.990 6.091   6.641   1.00 43.59  ? 47  VAL A CG2   1 
ATOM   287  N N     . ARG A 1 55  ? -17.588 9.771   8.368   1.00 35.52  ? 48  ARG A N     1 
ATOM   288  C CA    . ARG A 1 55  ? -16.618 10.881  8.251   1.00 34.05  ? 48  ARG A CA    1 
ATOM   289  C C     . ARG A 1 55  ? -15.236 10.248  8.426   1.00 32.31  ? 48  ARG A C     1 
ATOM   290  O O     . ARG A 1 55  ? -15.161 9.080   8.875   1.00 29.10  ? 48  ARG A O     1 
ATOM   291  C CB    . ARG A 1 55  ? -17.007 12.037  9.178   1.00 35.27  ? 48  ARG A CB    1 
ATOM   292  C CG    . ARG A 1 55  ? -18.280 12.739  8.709   1.00 34.32  ? 48  ARG A CG    1 
ATOM   293  C CD    . ARG A 1 55  ? -18.588 14.069  9.382   1.00 32.22  ? 48  ARG A CD    1 
ATOM   294  N NE    . ARG A 1 55  ? -17.631 15.151  9.145   1.00 31.85  ? 48  ARG A NE    1 
ATOM   295  C CZ    . ARG A 1 55  ? -17.355 15.712  7.959   1.00 31.89  ? 48  ARG A CZ    1 
ATOM   296  N NH1   . ARG A 1 55  ? -17.913 15.259  6.844   1.00 35.07  ? 48  ARG A NH1   1 
ATOM   297  N NH2   . ARG A 1 55  ? -16.489 16.713  7.888   1.00 28.82  ? 48  ARG A NH2   1 
ATOM   298  N N     . VAL A 1 56  ? -14.209 10.915  7.909   1.00 29.67  ? 49  VAL A N     1 
ATOM   299  C CA    . VAL A 1 56  ? -12.828 10.373  7.841   1.00 28.08  ? 49  VAL A CA    1 
ATOM   300  C C     . VAL A 1 56  ? -11.897 11.566  7.957   1.00 25.76  ? 49  VAL A C     1 
ATOM   301  O O     . VAL A 1 56  ? -12.390 12.680  7.762   1.00 25.49  ? 49  VAL A O     1 
ATOM   302  C CB    . VAL A 1 56  ? -12.598 9.521   6.578   1.00 27.74  ? 49  VAL A CB    1 
ATOM   303  C CG1   . VAL A 1 56  ? -13.648 8.432   6.456   1.00 29.07  ? 49  VAL A CG1   1 
ATOM   304  C CG2   . VAL A 1 56  ? -12.549 10.340  5.298   1.00 29.59  ? 49  VAL A CG2   1 
ATOM   305  N N     . ALA A 1 57  ? -10.637 11.334  8.320   1.00 24.24  ? 50  ALA A N     1 
ATOM   306  C CA    . ALA A 1 57  ? -9.595  12.380  8.375   1.00 25.16  ? 50  ALA A CA    1 
ATOM   307  C C     . ALA A 1 57  ? -8.821  12.335  7.054   1.00 23.33  ? 50  ALA A C     1 
ATOM   308  O O     . ALA A 1 57  ? -8.618  11.209  6.526   1.00 23.91  ? 50  ALA A O     1 
ATOM   309  C CB    . ALA A 1 57  ? -8.691  12.151  9.563   1.00 23.94  ? 50  ALA A CB    1 
ATOM   310  N N     . ILE A 1 58  ? -8.400  13.482  6.524   1.00 22.15  ? 51  ILE A N     1 
ATOM   311  C CA    . ILE A 1 58  ? -7.525  13.477  5.317   1.00 22.54  ? 51  ILE A CA    1 
ATOM   312  C C     . ILE A 1 58  ? -6.408  14.475  5.553   1.00 24.78  ? 51  ILE A C     1 
ATOM   313  O O     . ILE A 1 58  ? -6.726  15.610  6.012   1.00 23.72  ? 51  ILE A O     1 
ATOM   314  C CB    . ILE A 1 58  ? -8.282  13.727  3.998   1.00 21.19  ? 51  ILE A CB    1 
ATOM   315  C CG1   . ILE A 1 58  ? -9.515  12.836  3.870   1.00 21.42  ? 51  ILE A CG1   1 
ATOM   316  C CG2   . ILE A 1 58  ? -7.349  13.505  2.825   1.00 21.83  ? 51  ILE A CG2   1 
ATOM   317  C CD1   . ILE A 1 58  ? -10.358 13.110  2.641   1.00 21.63  ? 51  ILE A CD1   1 
ATOM   318  N N     . LYS A 1 59  ? -5.173  14.004  5.339   1.00 23.25  ? 52  LYS A N     1 
ATOM   319  C CA    . LYS A 1 59  ? -3.932  14.798  5.484   1.00 26.73  ? 52  LYS A CA    1 
ATOM   320  C C     . LYS A 1 59  ? -3.449  15.100  4.066   1.00 25.14  ? 52  LYS A C     1 
ATOM   321  O O     . LYS A 1 59  ? -3.048  14.167  3.371   1.00 22.04  ? 52  LYS A O     1 
ATOM   322  C CB    . LYS A 1 59  ? -2.842  14.070  6.287   1.00 30.49  ? 52  LYS A CB    1 
ATOM   323  C CG    . LYS A 1 59  ? -3.172  13.734  7.746   1.00 36.35  ? 52  LYS A CG    1 
ATOM   324  C CD    . LYS A 1 59  ? -2.052  14.026  8.776   1.00 37.19  ? 52  LYS A CD    1 
ATOM   325  C CE    . LYS A 1 59  ? -1.412  12.804  9.405   1.00 39.67  ? 52  LYS A CE    1 
ATOM   326  N NZ    . LYS A 1 59  ? -0.327  12.234  8.566   1.00 45.85  ? 52  LYS A NZ    1 
ATOM   327  N N     . LYS A 1 60  ? -3.517  16.357  3.655   1.00 24.41  ? 53  LYS A N     1 
ATOM   328  C CA    . LYS A 1 60  ? -2.840  16.829  2.424   1.00 26.39  ? 53  LYS A CA    1 
ATOM   329  C C     . LYS A 1 60  ? -1.358  16.989  2.741   1.00 24.15  ? 53  LYS A C     1 
ATOM   330  O O     . LYS A 1 60  ? -1.021  17.758  3.652   1.00 24.54  ? 53  LYS A O     1 
ATOM   331  C CB    . LYS A 1 60  ? -3.449  18.144  1.933   1.00 27.31  ? 53  LYS A CB    1 
ATOM   332  C CG    . LYS A 1 60  ? -2.664  18.827  0.829   1.00 27.74  ? 53  LYS A CG    1 
ATOM   333  C CD    . LYS A 1 60  ? -3.499  19.800  0.045   1.00 28.99  ? 53  LYS A CD    1 
ATOM   334  C CE    . LYS A 1 60  ? -2.663  20.846  -0.659  1.00 30.01  ? 53  LYS A CE    1 
ATOM   335  N NZ    . LYS A 1 60  ? -3.436  22.097  -0.855  1.00 31.87  ? 53  LYS A NZ    1 
ATOM   336  N N     . ILE A 1 61  ? -0.504  16.280  2.026   1.00 23.54  ? 54  ILE A N     1 
ATOM   337  C CA    . ILE A 1 61  ? 0.965   16.388  2.214   1.00 24.47  ? 54  ILE A CA    1 
ATOM   338  C C     . ILE A 1 61  ? 1.538   16.879  0.897   1.00 24.94  ? 54  ILE A C     1 
ATOM   339  O O     . ILE A 1 61  ? 1.274   16.235  -0.137  1.00 25.46  ? 54  ILE A O     1 
ATOM   340  C CB    . ILE A 1 61  ? 1.587   15.046  2.639   1.00 25.63  ? 54  ILE A CB    1 
ATOM   341  C CG1   . ILE A 1 61  ? 0.854   14.451  3.839   1.00 27.63  ? 54  ILE A CG1   1 
ATOM   342  C CG2   . ILE A 1 61  ? 3.077   15.187  2.903   1.00 24.76  ? 54  ILE A CG2   1 
ATOM   343  C CD1   . ILE A 1 61  ? 1.381   13.113  4.214   1.00 28.94  ? 54  ILE A CD1   1 
ATOM   344  N N     . SER A 1 62  ? 2.304   17.954  0.982   1.00 24.80  ? 55  SER A N     1 
ATOM   345  C CA    . SER A 1 62  ? 3.033   18.595  -0.135  1.00 26.65  ? 55  SER A CA    1 
ATOM   346  C C     . SER A 1 62  ? 4.499   18.712  0.259   1.00 25.48  ? 55  SER A C     1 
ATOM   347  O O     . SER A 1 62  ? 4.923   19.757  0.725   1.00 28.07  ? 55  SER A O     1 
ATOM   348  C CB    . SER A 1 62  ? 2.405   19.927  -0.463  1.00 27.78  ? 55  SER A CB    1 
ATOM   349  O OG    . SER A 1 62  ? 0.988   19.890  -0.270  1.00 26.67  ? 55  SER A OG    1 
ATOM   350  N N     . PRO A 1 63  ? 5.294   17.624  0.129   1.00 26.39  ? 56  PRO A N     1 
ATOM   351  C CA    . PRO A 1 63  ? 6.710   17.603  0.516   1.00 25.39  ? 56  PRO A CA    1 
ATOM   352  C C     . PRO A 1 63  ? 7.807   17.571  -0.565  1.00 24.67  ? 56  PRO A C     1 
ATOM   353  O O     . PRO A 1 63  ? 8.985   17.468  -0.206  1.00 24.71  ? 56  PRO A O     1 
ATOM   354  C CB    . PRO A 1 63  ? 6.738   16.194  1.120   1.00 25.75  ? 56  PRO A CB    1 
ATOM   355  C CG    . PRO A 1 63  ? 5.950   15.380  0.121   1.00 24.71  ? 56  PRO A CG    1 
ATOM   356  C CD    . PRO A 1 63  ? 4.847   16.303  -0.347  1.00 24.88  ? 56  PRO A CD    1 
ATOM   357  N N     . PHE A 1 64  ? 7.431   17.589  -1.847  1.00 25.41  ? 57  PHE A N     1 
ATOM   358  C CA    . PHE A 1 64  ? 8.325   17.162  -2.965  1.00 28.11  ? 57  PHE A CA    1 
ATOM   359  C C     . PHE A 1 64  ? 9.403   18.222  -3.221  1.00 30.95  ? 57  PHE A C     1 
ATOM   360  O O     . PHE A 1 64  ? 10.390  17.857  -3.883  1.00 29.98  ? 57  PHE A O     1 
ATOM   361  C CB    . PHE A 1 64  ? 7.543   16.797  -4.234  1.00 26.77  ? 57  PHE A CB    1 
ATOM   362  C CG    . PHE A 1 64  ? 6.522   15.703  -4.030  1.00 27.02  ? 57  PHE A CG    1 
ATOM   363  C CD1   . PHE A 1 64  ? 6.915   14.411  -3.710  1.00 28.93  ? 57  PHE A CD1   1 
ATOM   364  C CD2   . PHE A 1 64  ? 5.166   15.970  -4.125  1.00 26.62  ? 57  PHE A CD2   1 
ATOM   365  C CE1   . PHE A 1 64  ? 5.975   13.412  -3.509  1.00 26.05  ? 57  PHE A CE1   1 
ATOM   366  C CE2   . PHE A 1 64  ? 4.225   14.975  -3.919  1.00 24.41  ? 57  PHE A CE2   1 
ATOM   367  C CZ    . PHE A 1 64  ? 4.635   13.700  -3.627  1.00 27.30  ? 57  PHE A CZ    1 
ATOM   368  N N     . GLU A 1 65  ? 9.224   19.443  -2.694  1.00 34.58  ? 58  GLU A N     1 
ATOM   369  C CA    . GLU A 1 65  ? 10.180  20.587  -2.796  1.00 41.69  ? 58  GLU A CA    1 
ATOM   370  C C     . GLU A 1 65  ? 11.476  20.290  -2.015  1.00 45.68  ? 58  GLU A C     1 
ATOM   371  O O     . GLU A 1 65  ? 12.564  20.649  -2.539  1.00 40.37  ? 58  GLU A O     1 
ATOM   372  C CB    . GLU A 1 65  ? 9.545   21.885  -2.266  1.00 40.91  ? 58  GLU A CB    1 
ATOM   373  C CG    . GLU A 1 65  ? 8.352   22.392  -3.076  1.00 44.76  ? 58  GLU A CG    1 
ATOM   374  C CD    . GLU A 1 65  ? 8.655   23.064  -4.419  1.00 50.48  ? 58  GLU A CD    1 
ATOM   375  O OE1   . GLU A 1 65  ? 9.659   22.676  -5.085  1.00 51.95  ? 58  GLU A OE1   1 
ATOM   376  O OE2   . GLU A 1 65  ? 7.891   23.986  -4.805  1.00 45.52  ? 58  GLU A OE2   1 
ATOM   377  N N     . HIS A 1 66  ? 11.366  19.685  -0.816  1.00 48.93  ? 59  HIS A N     1 
ATOM   378  C CA    . HIS A 1 66  ? 12.478  19.496  0.160   1.00 48.35  ? 59  HIS A CA    1 
ATOM   379  C C     . HIS A 1 66  ? 12.702  18.008  0.441   1.00 46.65  ? 59  HIS A C     1 
ATOM   380  O O     . HIS A 1 66  ? 11.733  17.296  0.790   1.00 43.55  ? 59  HIS A O     1 
ATOM   381  C CB    . HIS A 1 66  ? 12.203  20.294  1.440   1.00 54.79  ? 59  HIS A CB    1 
ATOM   382  C CG    . HIS A 1 66  ? 12.203  21.768  1.215   1.00 58.54  ? 59  HIS A CG    1 
ATOM   383  N ND1   . HIS A 1 66  ? 11.129  22.572  1.562   1.00 65.30  ? 59  HIS A ND1   1 
ATOM   384  C CD2   . HIS A 1 66  ? 13.119  22.578  0.644   1.00 59.68  ? 59  HIS A CD2   1 
ATOM   385  C CE1   . HIS A 1 66  ? 11.392  23.821  1.233   1.00 63.26  ? 59  HIS A CE1   1 
ATOM   386  N NE2   . HIS A 1 66  ? 12.608  23.849  0.666   1.00 64.65  ? 59  HIS A NE2   1 
ATOM   387  N N     . GLN A 1 67  ? 13.948  17.572  0.277   1.00 44.26  ? 60  GLN A N     1 
ATOM   388  C CA    . GLN A 1 67  ? 14.419  16.177  0.483   1.00 44.27  ? 60  GLN A CA    1 
ATOM   389  C C     . GLN A 1 67  ? 13.992  15.678  1.874   1.00 40.93  ? 60  GLN A C     1 
ATOM   390  O O     . GLN A 1 67  ? 13.563  14.494  1.992   1.00 35.96  ? 60  GLN A O     1 
ATOM   391  C CB    . GLN A 1 67  ? 15.937  16.149  0.287   1.00 44.85  ? 60  GLN A CB    1 
ATOM   392  C CG    . GLN A 1 67  ? 16.491  14.780  -0.077  1.00 45.11  ? 60  GLN A CG    1 
ATOM   393  C CD    . GLN A 1 67  ? 17.093  14.029  1.086   1.00 45.53  ? 60  GLN A CD    1 
ATOM   394  O OE1   . GLN A 1 67  ? 17.073  12.805  1.133   1.00 45.67  ? 60  GLN A OE1   1 
ATOM   395  N NE2   . GLN A 1 67  ? 17.660  14.756  2.032   1.00 44.01  ? 60  GLN A NE2   1 
ATOM   396  N N     . THR A 1 68  ? 14.072  16.550  2.884   1.00 41.00  ? 61  THR A N     1 
ATOM   397  C CA    . THR A 1 68  ? 13.701  16.260  4.300   1.00 39.55  ? 61  THR A CA    1 
ATOM   398  C C     . THR A 1 68  ? 12.236  15.806  4.366   1.00 37.76  ? 61  THR A C     1 
ATOM   399  O O     . THR A 1 68  ? 11.958  14.753  4.975   1.00 35.11  ? 61  THR A O     1 
ATOM   400  C CB    . THR A 1 68  ? 13.997  17.461  5.212   1.00 41.09  ? 61  THR A CB    1 
ATOM   401  O OG1   . THR A 1 68  ? 15.375  17.372  5.579   1.00 40.68  ? 61  THR A OG1   1 
ATOM   402  C CG2   . THR A 1 68  ? 13.188  17.493  6.490   1.00 45.21  ? 61  THR A CG2   1 
ATOM   403  N N     . TYR A 1 69  ? 11.328  16.574  3.776   1.00 37.85  ? 62  TYR A N     1 
ATOM   404  C CA    . TYR A 1 69  ? 9.872   16.304  3.835   1.00 37.83  ? 62  TYR A CA    1 
ATOM   405  C C     . TYR A 1 69  ? 9.571   14.986  3.118   1.00 34.01  ? 62  TYR A C     1 
ATOM   406  O O     . TYR A 1 69  ? 8.702   14.268  3.602   1.00 29.12  ? 62  TYR A O     1 
ATOM   407  C CB    . TYR A 1 69  ? 9.060   17.468  3.258   1.00 44.23  ? 62  TYR A CB    1 
ATOM   408  C CG    . TYR A 1 69  ? 9.237   18.809  3.930   1.00 48.92  ? 62  TYR A CG    1 
ATOM   409  C CD1   . TYR A 1 69  ? 9.950   18.959  5.113   1.00 52.11  ? 62  TYR A CD1   1 
ATOM   410  C CD2   . TYR A 1 69  ? 8.655   19.941  3.379   1.00 50.70  ? 62  TYR A CD2   1 
ATOM   411  C CE1   . TYR A 1 69  ? 10.084  20.197  5.720   1.00 54.33  ? 62  TYR A CE1   1 
ATOM   412  C CE2   . TYR A 1 69  ? 8.786   21.188  3.964   1.00 52.51  ? 62  TYR A CE2   1 
ATOM   413  C CZ    . TYR A 1 69  ? 9.501   21.314  5.141   1.00 58.39  ? 62  TYR A CZ    1 
ATOM   414  O OH    . TYR A 1 69  ? 9.633   22.545  5.709   1.00 66.12  ? 62  TYR A OH    1 
ATOM   415  N N     . CYS A 1 70  ? 10.285  14.676  2.027   1.00 31.15  ? 63  CYS A N     1 
ATOM   416  C CA    . CYS A 1 70  ? 10.077  13.464  1.195   1.00 30.53  ? 63  CYS A CA    1 
ATOM   417  C C     . CYS A 1 70  ? 10.488  12.207  1.974   1.00 28.76  ? 63  CYS A C     1 
ATOM   418  O O     . CYS A 1 70  ? 9.882   11.132  1.773   1.00 22.91  ? 63  CYS A O     1 
ATOM   419  C CB    . CYS A 1 70  ? 10.881  13.534  -0.094  1.00 32.38  ? 63  CYS A CB    1 
ATOM   420  S SG    . CYS A 1 70  ? 10.142  14.618  -1.344  1.00 34.54  ? 63  CYS A SG    1 
ATOM   421  N N     . GLN A 1 71  ? 11.567  12.318  2.744   1.00 28.02  ? 64  GLN A N     1 
ATOM   422  C CA    . GLN A 1 71  ? 12.088  11.229  3.594   1.00 25.54  ? 64  GLN A CA    1 
ATOM   423  C C     . GLN A 1 71  ? 11.034  10.893  4.645   1.00 22.66  ? 64  GLN A C     1 
ATOM   424  O O     . GLN A 1 71  ? 10.682  9.735   4.774   1.00 21.44  ? 64  GLN A O     1 
ATOM   425  C CB    . GLN A 1 71  ? 13.360  11.667  4.307   1.00 28.14  ? 64  GLN A CB    1 
ATOM   426  C CG    . GLN A 1 71  ? 14.611  11.462  3.488   1.00 30.23  ? 64  GLN A CG    1 
ATOM   427  C CD    . GLN A 1 71  ? 15.808  11.749  4.354   1.00 32.91  ? 64  GLN A CD    1 
ATOM   428  O OE1   . GLN A 1 71  ? 16.225  10.900  5.136   1.00 34.05  ? 64  GLN A OE1   1 
ATOM   429  N NE2   . GLN A 1 71  ? 16.345  12.958  4.232   1.00 31.63  ? 64  GLN A NE2   1 
ATOM   430  N N     . ARG A 1 72  ? 10.566  11.885  5.388   1.00 21.72  ? 65  ARG A N     1 
ATOM   431  C CA    . ARG A 1 72  ? 9.659   11.618  6.536   1.00 22.99  ? 65  ARG A CA    1 
ATOM   432  C C     . ARG A 1 72  ? 8.356   11.052  5.954   1.00 20.63  ? 65  ARG A C     1 
ATOM   433  O O     . ARG A 1 72  ? 7.877   10.038  6.464   1.00 22.48  ? 65  ARG A O     1 
ATOM   434  C CB    . ARG A 1 72  ? 9.536   12.871  7.404   1.00 25.49  ? 65  ARG A CB    1 
ATOM   435  C CG    . ARG A 1 72  ? 10.884  13.544  7.659   1.00 28.68  ? 65  ARG A CG    1 
ATOM   436  C CD    . ARG A 1 72  ? 11.143  14.214  8.993   1.00 30.84  ? 65  ARG A CD    1 
ATOM   437  N NE    . ARG A 1 72  ? 12.590  14.387  9.230   1.00 35.73  ? 65  ARG A NE    1 
ATOM   438  C CZ    . ARG A 1 72  ? 13.463  13.435  9.596   1.00 35.12  ? 65  ARG A CZ    1 
ATOM   439  N NH1   . ARG A 1 72  ? 13.087  12.177  9.760   1.00 37.58  ? 65  ARG A NH1   1 
ATOM   440  N NH2   . ARG A 1 72  ? 14.727  13.751  9.813   1.00 37.57  ? 65  ARG A NH2   1 
ATOM   441  N N     . THR A 1 73  ? 7.853   11.626  4.855   1.00 18.69  ? 66  THR A N     1 
ATOM   442  C CA    . THR A 1 73  ? 6.654   11.125  4.144   1.00 16.24  ? 66  THR A CA    1 
ATOM   443  C C     . THR A 1 73  ? 6.957   9.694   3.681   1.00 15.15  ? 66  THR A C     1 
ATOM   444  O O     . THR A 1 73  ? 6.146   8.810   3.981   1.00 12.02  ? 66  THR A O     1 
ATOM   445  C CB    . THR A 1 73  ? 6.234   12.007  2.958   1.00 16.88  ? 66  THR A CB    1 
ATOM   446  O OG1   . THR A 1 73  ? 6.097   13.394  3.276   1.00 15.63  ? 66  THR A OG1   1 
ATOM   447  C CG2   . THR A 1 73  ? 4.901   11.549  2.403   1.00 17.31  ? 66  THR A CG2   1 
ATOM   448  N N     . LEU A 1 74  ? 8.088   9.437   3.012   1.00 14.94  ? 67  LEU A N     1 
ATOM   449  C CA    . LEU A 1 74  ? 8.315   8.060   2.503   1.00 16.73  ? 67  LEU A CA    1 
ATOM   450  C C     . LEU A 1 74  ? 8.313   7.114   3.712   1.00 17.72  ? 67  LEU A C     1 
ATOM   451  O O     . LEU A 1 74  ? 7.567   6.117   3.703   1.00 15.24  ? 67  LEU A O     1 
ATOM   452  C CB    . LEU A 1 74  ? 9.604   7.935   1.678   1.00 17.36  ? 67  LEU A CB    1 
ATOM   453  C CG    . LEU A 1 74  ? 9.936   6.497   1.273   1.00 16.72  ? 67  LEU A CG    1 
ATOM   454  C CD1   . LEU A 1 74  ? 8.709   5.814   0.673   1.00 17.94  ? 67  LEU A CD1   1 
ATOM   455  C CD2   . LEU A 1 74  ? 11.105  6.440   0.313   1.00 18.08  ? 67  LEU A CD2   1 
ATOM   456  N N     . ARG A 1 75  ? 9.076   7.473   4.745   1.00 22.70  ? 68  ARG A N     1 
ATOM   457  C CA    . ARG A 1 75  ? 9.189   6.740   6.037   1.00 25.31  ? 68  ARG A CA    1 
ATOM   458  C C     . ARG A 1 75  ? 7.799   6.374   6.555   1.00 24.29  ? 68  ARG A C     1 
ATOM   459  O O     . ARG A 1 75  ? 7.557   5.168   6.795   1.00 24.66  ? 68  ARG A O     1 
ATOM   460  C CB    . ARG A 1 75  ? 9.871   7.595   7.109   1.00 28.23  ? 68  ARG A CB    1 
ATOM   461  C CG    . ARG A 1 75  ? 11.119  6.964   7.689   1.00 30.78  ? 68  ARG A CG    1 
ATOM   462  C CD    . ARG A 1 75  ? 11.691  7.788   8.826   1.00 33.26  ? 68  ARG A CD    1 
ATOM   463  N NE    . ARG A 1 75  ? 12.592  8.832   8.373   1.00 38.87  ? 68  ARG A NE    1 
ATOM   464  C CZ    . ARG A 1 75  ? 13.800  8.623   7.850   1.00 39.64  ? 68  ARG A CZ    1 
ATOM   465  N NH1   . ARG A 1 75  ? 14.280  7.394   7.704   1.00 42.83  ? 68  ARG A NH1   1 
ATOM   466  N NH2   . ARG A 1 75  ? 14.525  9.660   7.473   1.00 38.76  ? 68  ARG A NH2   1 
ATOM   467  N N     . GLU A 1 76  ? 6.918   7.363   6.701   1.00 23.55  ? 69  GLU A N     1 
ATOM   468  C CA    . GLU A 1 76  ? 5.649   7.171   7.454   1.00 25.10  ? 69  GLU A CA    1 
ATOM   469  C C     . GLU A 1 76  ? 4.715   6.271   6.647   1.00 23.03  ? 69  GLU A C     1 
ATOM   470  O O     . GLU A 1 76  ? 4.136   5.335   7.235   1.00 22.27  ? 69  GLU A O     1 
ATOM   471  C CB    . GLU A 1 76  ? 4.969   8.497   7.784   1.00 27.03  ? 69  GLU A CB    1 
ATOM   472  C CG    . GLU A 1 76  ? 3.768   8.334   8.717   1.00 28.80  ? 69  GLU A CG    1 
ATOM   473  C CD    . GLU A 1 76  ? 3.385   9.577   9.505   1.00 31.93  ? 69  GLU A CD    1 
ATOM   474  O OE1   . GLU A 1 76  ? 4.040   10.631  9.310   1.00 39.34  ? 69  GLU A OE1   1 
ATOM   475  O OE2   . GLU A 1 76  ? 2.446   9.500   10.329  1.00 32.57  ? 69  GLU A OE2   1 
ATOM   476  N N     . ILE A 1 77  ? 4.578   6.544   5.357   1.00 21.09  ? 70  ILE A N     1 
ATOM   477  C CA    . ILE A 1 77  ? 3.747   5.735   4.426   1.00 20.84  ? 70  ILE A CA    1 
ATOM   478  C C     . ILE A 1 77  ? 4.251   4.282   4.446   1.00 17.87  ? 70  ILE A C     1 
ATOM   479  O O     . ILE A 1 77  ? 3.442   3.417   4.708   1.00 14.90  ? 70  ILE A O     1 
ATOM   480  C CB    . ILE A 1 77  ? 3.735   6.364   3.010   1.00 23.62  ? 70  ILE A CB    1 
ATOM   481  C CG1   . ILE A 1 77  ? 3.028   7.728   3.005   1.00 23.10  ? 70  ILE A CG1   1 
ATOM   482  C CG2   . ILE A 1 77  ? 3.113   5.400   1.998   1.00 24.17  ? 70  ILE A CG2   1 
ATOM   483  C CD1   . ILE A 1 77  ? 3.168   8.488   1.723   1.00 23.53  ? 70  ILE A CD1   1 
ATOM   484  N N     . LYS A 1 78  ? 5.550   4.018   4.296   1.00 18.67  ? 71  LYS A N     1 
ATOM   485  C CA    . LYS A 1 78  ? 6.072   2.620   4.272   1.00 19.48  ? 71  LYS A CA    1 
ATOM   486  C C     . LYS A 1 78  ? 5.629   1.906   5.548   1.00 18.51  ? 71  LYS A C     1 
ATOM   487  O O     . LYS A 1 78  ? 5.044   0.790   5.458   1.00 18.63  ? 71  LYS A O     1 
ATOM   488  C CB    . LYS A 1 78  ? 7.594   2.565   4.170   1.00 22.26  ? 71  LYS A CB    1 
ATOM   489  C CG    . LYS A 1 78  ? 8.150   2.809   2.780   1.00 25.80  ? 71  LYS A CG    1 
ATOM   490  C CD    . LYS A 1 78  ? 9.664   2.645   2.713   1.00 29.32  ? 71  LYS A CD    1 
ATOM   491  C CE    . LYS A 1 78  ? 10.110  1.389   1.989   1.00 33.39  ? 71  LYS A CE    1 
ATOM   492  N NZ    . LYS A 1 78  ? 10.237  1.618   0.528   1.00 34.19  ? 71  LYS A NZ    1 
ATOM   493  N N     . ILE A 1 79  ? 5.872   2.538   6.696   1.00 16.78  ? 72  ILE A N     1 
ATOM   494  C CA    . ILE A 1 79  ? 5.591   1.913   8.013   1.00 17.64  ? 72  ILE A CA    1 
ATOM   495  C C     . ILE A 1 79  ? 4.078   1.684   8.168   1.00 18.21  ? 72  ILE A C     1 
ATOM   496  O O     . ILE A 1 79  ? 3.654   0.572   8.601   1.00 17.56  ? 72  ILE A O     1 
ATOM   497  C CB    . ILE A 1 79  ? 6.188   2.745   9.162   1.00 17.13  ? 72  ILE A CB    1 
ATOM   498  C CG1   . ILE A 1 79  ? 7.727   2.714   9.151   1.00 17.26  ? 72  ILE A CG1   1 
ATOM   499  C CG2   . ILE A 1 79  ? 5.608   2.246   10.474  1.00 16.69  ? 72  ILE A CG2   1 
ATOM   500  C CD1   . ILE A 1 79  ? 8.388   3.785   9.990   1.00 16.41  ? 72  ILE A CD1   1 
ATOM   501  N N     . LEU A 1 80  ? 3.275   2.693   7.860   1.00 19.05  ? 73  LEU A N     1 
ATOM   502  C CA    . LEU A 1 80  ? 1.822   2.644   8.133   1.00 20.09  ? 73  LEU A CA    1 
ATOM   503  C C     . LEU A 1 80  ? 1.175   1.585   7.240   1.00 19.90  ? 73  LEU A C     1 
ATOM   504  O O     . LEU A 1 80  ? 0.259   0.909   7.758   1.00 19.14  ? 73  LEU A O     1 
ATOM   505  C CB    . LEU A 1 80  ? 1.218   4.036   7.963   1.00 21.15  ? 73  LEU A CB    1 
ATOM   506  C CG    . LEU A 1 80  ? 1.605   4.989   9.091   1.00 23.86  ? 73  LEU A CG    1 
ATOM   507  C CD1   . LEU A 1 80  ? 0.761   6.257   9.087   1.00 25.17  ? 73  LEU A CD1   1 
ATOM   508  C CD2   . LEU A 1 80  ? 1.474   4.289   10.436  1.00 26.35  ? 73  LEU A CD2   1 
ATOM   509  N N     . LEU A 1 81  ? 1.680   1.391   6.015   1.00 19.55  ? 74  LEU A N     1 
ATOM   510  C CA    . LEU A 1 81  ? 1.204   0.330   5.077   1.00 22.18  ? 74  LEU A CA    1 
ATOM   511  C C     . LEU A 1 81  ? 1.621   -1.056  5.590   1.00 21.76  ? 74  LEU A C     1 
ATOM   512  O O     . LEU A 1 81  ? 0.942   -2.021  5.297   1.00 21.11  ? 74  LEU A O     1 
ATOM   513  C CB    . LEU A 1 81  ? 1.745   0.541   3.650   1.00 21.19  ? 74  LEU A CB    1 
ATOM   514  C CG    . LEU A 1 81  ? 1.208   1.758   2.909   1.00 21.38  ? 74  LEU A CG    1 
ATOM   515  C CD1   . LEU A 1 81  ? 1.448   1.611   1.414   1.00 23.60  ? 74  LEU A CD1   1 
ATOM   516  C CD2   . LEU A 1 81  ? -0.284  1.966   3.180   1.00 22.01  ? 74  LEU A CD2   1 
ATOM   517  N N     . ARG A 1 82  ? 2.739   -1.166  6.281   1.00 25.69  ? 75  ARG A N     1 
ATOM   518  C CA    . ARG A 1 82  ? 3.268   -2.490  6.699   1.00 26.11  ? 75  ARG A CA    1 
ATOM   519  C C     . ARG A 1 82  ? 2.516   -2.899  7.979   1.00 23.69  ? 75  ARG A C     1 
ATOM   520  O O     . ARG A 1 82  ? 2.289   -4.111  8.223   1.00 21.94  ? 75  ARG A O     1 
ATOM   521  C CB    . ARG A 1 82  ? 4.792   -2.362  6.825   1.00 28.62  ? 75  ARG A CB    1 
ATOM   522  C CG    . ARG A 1 82  ? 5.532   -3.675  7.010   1.00 30.85  ? 75  ARG A CG    1 
ATOM   523  C CD    . ARG A 1 82  ? 6.294   -4.143  5.775   1.00 32.07  ? 75  ARG A CD    1 
ATOM   524  N NE    . ARG A 1 82  ? 7.572   -4.726  6.182   1.00 32.33  ? 75  ARG A NE    1 
ATOM   525  C CZ    . ARG A 1 82  ? 8.718   -4.657  5.509   1.00 31.28  ? 75  ARG A CZ    1 
ATOM   526  N NH1   . ARG A 1 82  ? 8.784   -4.057  4.327   1.00 31.11  ? 75  ARG A NH1   1 
ATOM   527  N NH2   . ARG A 1 82  ? 9.797   -5.238  6.011   1.00 33.17  ? 75  ARG A NH2   1 
ATOM   528  N N     . PHE A 1 83  ? 2.135   -1.912  8.782   1.00 21.63  ? 76  PHE A N     1 
ATOM   529  C CA    . PHE A 1 83  ? 1.563   -2.118  10.131  1.00 19.30  ? 76  PHE A CA    1 
ATOM   530  C C     . PHE A 1 83  ? 0.072   -2.351  9.989   1.00 21.17  ? 76  PHE A C     1 
ATOM   531  O O     . PHE A 1 83  ? -0.608  -1.608  9.221   1.00 20.54  ? 76  PHE A O     1 
ATOM   532  C CB    . PHE A 1 83  ? 1.895   -0.934  11.028  1.00 18.34  ? 76  PHE A CB    1 
ATOM   533  C CG    . PHE A 1 83  ? 3.312   -0.897  11.550  1.00 17.40  ? 76  PHE A CG    1 
ATOM   534  C CD1   . PHE A 1 83  ? 4.248   -1.846  11.203  1.00 17.16  ? 76  PHE A CD1   1 
ATOM   535  C CD2   . PHE A 1 83  ? 3.697   0.093   12.435  1.00 18.71  ? 76  PHE A CD2   1 
ATOM   536  C CE1   . PHE A 1 83  ? 5.542   -1.793  11.710  1.00 19.46  ? 76  PHE A CE1   1 
ATOM   537  C CE2   . PHE A 1 83  ? 4.975   0.136   12.966  1.00 19.07  ? 76  PHE A CE2   1 
ATOM   538  C CZ    . PHE A 1 83  ? 5.915   -0.790  12.580  1.00 18.88  ? 76  PHE A CZ    1 
ATOM   539  N N     . ARG A 1 84  ? -0.390  -3.386  10.685  1.00 22.50  ? 77  ARG A N     1 
ATOM   540  C CA    . ARG A 1 84  ? -1.820  -3.664  10.928  1.00 24.46  ? 77  ARG A CA    1 
ATOM   541  C C     . ARG A 1 84  ? -2.029  -3.896  12.424  1.00 20.74  ? 77  ARG A C     1 
ATOM   542  O O     . ARG A 1 84  ? -1.747  -5.001  12.889  1.00 20.23  ? 77  ARG A O     1 
ATOM   543  C CB    . ARG A 1 84  ? -2.277  -4.908  10.161  1.00 27.06  ? 77  ARG A CB    1 
ATOM   544  C CG    . ARG A 1 84  ? -3.752  -5.203  10.393  1.00 32.41  ? 77  ARG A CG    1 
ATOM   545  C CD    . ARG A 1 84  ? -4.456  -5.802  9.184   1.00 39.15  ? 77  ARG A CD    1 
ATOM   546  N NE    . ARG A 1 84  ? -5.895  -5.999  9.383   1.00 43.05  ? 77  ARG A NE    1 
ATOM   547  C CZ    . ARG A 1 84  ? -6.876  -5.455  8.651   1.00 49.99  ? 77  ARG A CZ    1 
ATOM   548  N NH1   . ARG A 1 84  ? -6.615  -4.648  7.629   1.00 54.24  ? 77  ARG A NH1   1 
ATOM   549  N NH2   . ARG A 1 84  ? -8.135  -5.745  8.935   1.00 50.25  ? 77  ARG A NH2   1 
ATOM   550  N N     . HIS A 1 85  ? -2.561  -2.921  13.138  1.00 17.71  ? 78  HIS A N     1 
ATOM   551  C CA    . HIS A 1 85  ? -2.774  -3.028  14.605  1.00 17.05  ? 78  HIS A CA    1 
ATOM   552  C C     . HIS A 1 85  ? -3.848  -2.054  15.049  1.00 16.42  ? 78  HIS A C     1 
ATOM   553  O O     . HIS A 1 85  ? -3.806  -0.910  14.608  1.00 17.63  ? 78  HIS A O     1 
ATOM   554  C CB    . HIS A 1 85  ? -1.455  -2.747  15.333  1.00 15.80  ? 78  HIS A CB    1 
ATOM   555  C CG    . HIS A 1 85  ? -1.462  -3.114  16.774  1.00 14.89  ? 78  HIS A CG    1 
ATOM   556  N ND1   . HIS A 1 85  ? -0.848  -4.259  17.250  1.00 13.75  ? 78  HIS A ND1   1 
ATOM   557  C CD2   . HIS A 1 85  ? -1.909  -2.450  17.852  1.00 14.11  ? 78  HIS A CD2   1 
ATOM   558  C CE1   . HIS A 1 85  ? -0.949  -4.295  18.549  1.00 14.19  ? 78  HIS A CE1   1 
ATOM   559  N NE2   . HIS A 1 85  ? -1.614  -3.214  18.949  1.00 14.88  ? 78  HIS A NE2   1 
ATOM   560  N N     . GLU A 1 86  ? -4.706  -2.483  15.961  1.00 17.81  ? 79  GLU A N     1 
ATOM   561  C CA    . GLU A 1 86  ? -5.805  -1.675  16.546  1.00 18.29  ? 79  GLU A CA    1 
ATOM   562  C C     . GLU A 1 86  ? -5.326  -0.345  17.118  1.00 15.62  ? 79  GLU A C     1 
ATOM   563  O O     . GLU A 1 86  ? -6.132  0.585   17.080  1.00 15.50  ? 79  GLU A O     1 
ATOM   564  C CB    . GLU A 1 86  ? -6.464  -2.412  17.704  1.00 21.12  ? 79  GLU A CB    1 
ATOM   565  C CG    . GLU A 1 86  ? -7.583  -3.308  17.263  1.00 25.76  ? 79  GLU A CG    1 
ATOM   566  C CD    . GLU A 1 86  ? -7.644  -4.607  18.035  1.00 28.81  ? 79  GLU A CD    1 
ATOM   567  O OE1   . GLU A 1 86  ? -7.519  -4.544  19.278  1.00 33.30  ? 79  GLU A OE1   1 
ATOM   568  O OE2   . GLU A 1 86  ? -7.737  -5.681  17.381  1.00 33.03  ? 79  GLU A OE2   1 
ATOM   569  N N     . ASN A 1 87  ? -4.160  -0.303  17.772  1.00 13.83  ? 80  ASN A N     1 
ATOM   570  C CA    . ASN A 1 87  ? -3.653  0.910   18.465  1.00 12.94  ? 80  ASN A CA    1 
ATOM   571  C C     . ASN A 1 87  ? -2.577  1.648   17.637  1.00 13.08  ? 80  ASN A C     1 
ATOM   572  O O     . ASN A 1 87  ? -1.874  2.516   18.197  1.00 11.98  ? 80  ASN A O     1 
ATOM   573  C CB    . ASN A 1 87  ? -3.079  0.590   19.832  1.00 12.25  ? 80  ASN A CB    1 
ATOM   574  C CG    . ASN A 1 87  ? -4.026  -0.201  20.687  1.00 12.43  ? 80  ASN A CG    1 
ATOM   575  O OD1   . ASN A 1 87  ? -3.734  -1.358  20.989  1.00 12.25  ? 80  ASN A OD1   1 
ATOM   576  N ND2   . ASN A 1 87  ? -5.137  0.414   21.062  1.00 11.21  ? 80  ASN A ND2   1 
ATOM   577  N N     . ILE A 1 88  ? -2.543  1.429   16.339  1.00 12.44  ? 81  ILE A N     1 
ATOM   578  C CA    . ILE A 1 88  ? -1.713  2.236   15.414  1.00 14.14  ? 81  ILE A CA    1 
ATOM   579  C C     . ILE A 1 88  ? -2.595  2.702   14.263  1.00 15.95  ? 81  ILE A C     1 
ATOM   580  O O     . ILE A 1 88  ? -3.275  1.829   13.658  1.00 16.23  ? 81  ILE A O     1 
ATOM   581  C CB    . ILE A 1 88  ? -0.518  1.444   14.888  1.00 13.35  ? 81  ILE A CB    1 
ATOM   582  C CG1   . ILE A 1 88  ? 0.308   0.806   16.013  1.00 13.13  ? 81  ILE A CG1   1 
ATOM   583  C CG2   . ILE A 1 88  ? 0.300   2.358   14.028  1.00 12.90  ? 81  ILE A CG2   1 
ATOM   584  C CD1   . ILE A 1 88  ? 1.592   0.139   15.503  1.00 13.38  ? 81  ILE A CD1   1 
ATOM   585  N N     . ILE A 1 89  ? -2.567  4.005   13.952  1.00 16.78  ? 82  ILE A N     1 
ATOM   586  C CA    . ILE A 1 89  ? -3.460  4.571   12.902  1.00 18.23  ? 82  ILE A CA    1 
ATOM   587  C C     . ILE A 1 89  ? -3.183  3.840   11.595  1.00 19.12  ? 82  ILE A C     1 
ATOM   588  O O     . ILE A 1 89  ? -1.997  3.580   11.292  1.00 22.49  ? 82  ILE A O     1 
ATOM   589  C CB    . ILE A 1 89  ? -3.309  6.094   12.726  1.00 18.81  ? 82  ILE A CB    1 
ATOM   590  C CG1   . ILE A 1 89  ? -4.430  6.628   11.835  1.00 19.19  ? 82  ILE A CG1   1 
ATOM   591  C CG2   . ILE A 1 89  ? -1.944  6.462   12.178  1.00 17.98  ? 82  ILE A CG2   1 
ATOM   592  C CD1   . ILE A 1 89  ? -5.809  6.293   12.337  1.00 20.74  ? 82  ILE A CD1   1 
ATOM   593  N N     . GLY A 1 90  ? -4.237  3.544   10.846  1.00 20.22  ? 83  GLY A N     1 
ATOM   594  C CA    . GLY A 1 90  ? -4.134  2.886   9.535   1.00 21.12  ? 83  GLY A CA    1 
ATOM   595  C C     . GLY A 1 90  ? -4.203  3.903   8.408   1.00 22.97  ? 83  GLY A C     1 
ATOM   596  O O     . GLY A 1 90  ? -4.700  5.028   8.623   1.00 21.36  ? 83  GLY A O     1 
ATOM   597  N N     . ILE A 1 91  ? -3.756  3.518   7.216   1.00 22.16  ? 84  ILE A N     1 
ATOM   598  C CA    . ILE A 1 91  ? -4.109  4.269   5.980   1.00 21.75  ? 84  ILE A CA    1 
ATOM   599  C C     . ILE A 1 91  ? -5.280  3.534   5.340   1.00 19.59  ? 84  ILE A C     1 
ATOM   600  O O     . ILE A 1 91  ? -5.131  2.363   5.115   1.00 19.88  ? 84  ILE A O     1 
ATOM   601  C CB    . ILE A 1 91  ? -2.883  4.450   5.057   1.00 22.04  ? 84  ILE A CB    1 
ATOM   602  C CG1   . ILE A 1 91  ? -1.803  5.303   5.744   1.00 20.97  ? 84  ILE A CG1   1 
ATOM   603  C CG2   . ILE A 1 91  ? -3.312  5.053   3.724   1.00 22.76  ? 84  ILE A CG2   1 
ATOM   604  C CD1   . ILE A 1 91  ? -0.422  5.170   5.139   1.00 21.86  ? 84  ILE A CD1   1 
ATOM   605  N N     . ASN A 1 92  ? -6.397  4.222   5.093   1.00 19.45  ? 85  ASN A N     1 
ATOM   606  C CA    . ASN A 1 92  ? -7.611  3.660   4.434   1.00 21.10  ? 85  ASN A CA    1 
ATOM   607  C C     . ASN A 1 92  ? -7.498  3.833   2.912   1.00 20.53  ? 85  ASN A C     1 
ATOM   608  O O     . ASN A 1 92  ? -7.981  2.970   2.179   1.00 18.22  ? 85  ASN A O     1 
ATOM   609  C CB    . ASN A 1 92  ? -8.886  4.337   4.940   1.00 22.27  ? 85  ASN A CB    1 
ATOM   610  C CG    . ASN A 1 92  ? -9.082  4.209   6.437   1.00 24.40  ? 85  ASN A CG    1 
ATOM   611  O OD1   . ASN A 1 92  ? -9.998  4.820   6.988   1.00 26.35  ? 85  ASN A OD1   1 
ATOM   612  N ND2   . ASN A 1 92  ? -8.272  3.397   7.099   1.00 23.93  ? 85  ASN A ND2   1 
ATOM   613  N N     . ASP A 1 93  ? -6.830  4.904   2.472   1.00 20.69  ? 86  ASP A N     1 
ATOM   614  C CA    . ASP A 1 93  ? -6.761  5.293   1.043   1.00 19.76  ? 86  ASP A CA    1 
ATOM   615  C C     . ASP A 1 93  ? -5.650  6.326   0.858   1.00 18.85  ? 86  ASP A C     1 
ATOM   616  O O     . ASP A 1 93  ? -5.304  7.057   1.828   1.00 17.59  ? 86  ASP A O     1 
ATOM   617  C CB    . ASP A 1 93  ? -8.132  5.817   0.634   1.00 19.53  ? 86  ASP A CB    1 
ATOM   618  C CG    . ASP A 1 93  ? -8.378  5.988   -0.845  1.00 21.00  ? 86  ASP A CG    1 
ATOM   619  O OD1   . ASP A 1 93  ? -7.493  5.607   -1.665  1.00 18.88  ? 86  ASP A OD1   1 
ATOM   620  O OD2   . ASP A 1 93  ? -9.447  6.560   -1.144  1.00 22.12  ? 86  ASP A OD2   1 
ATOM   621  N N     . ILE A 1 94  ? -5.108  6.398   -0.350  1.00 18.32  ? 87  ILE A N     1 
ATOM   622  C CA    . ILE A 1 94  ? -4.193  7.504   -0.742  1.00 17.11  ? 87  ILE A CA    1 
ATOM   623  C C     . ILE A 1 94  ? -4.641  8.043   -2.097  1.00 17.71  ? 87  ILE A C     1 
ATOM   624  O O     . ILE A 1 94  ? -4.827  7.262   -3.032  1.00 17.93  ? 87  ILE A O     1 
ATOM   625  C CB    . ILE A 1 94  ? -2.725  7.060   -0.725  1.00 17.12  ? 87  ILE A CB    1 
ATOM   626  C CG1   . ILE A 1 94  ? -2.323  6.419   0.605   1.00 16.86  ? 87  ILE A CG1   1 
ATOM   627  C CG2   . ILE A 1 94  ? -1.809  8.232   -1.062  1.00 17.09  ? 87  ILE A CG2   1 
ATOM   628  C CD1   . ILE A 1 94  ? -0.940  5.817   0.573   1.00 17.39  ? 87  ILE A CD1   1 
ATOM   629  N N     . ILE A 1 95  ? -4.883  9.344   -2.143  1.00 19.77  ? 88  ILE A N     1 
ATOM   630  C CA    . ILE A 1 95  ? -5.272  10.097  -3.353  1.00 19.91  ? 88  ILE A CA    1 
ATOM   631  C C     . ILE A 1 95  ? -4.013  10.808  -3.856  1.00 20.83  ? 88  ILE A C     1 
ATOM   632  O O     . ILE A 1 95  ? -3.442  11.608  -3.102  1.00 18.91  ? 88  ILE A O     1 
ATOM   633  C CB    . ILE A 1 95  ? -6.408  11.071  -3.034  1.00 22.58  ? 88  ILE A CB    1 
ATOM   634  C CG1   . ILE A 1 95  ? -7.649  10.334  -2.522  1.00 24.53  ? 88  ILE A CG1   1 
ATOM   635  C CG2   . ILE A 1 95  ? -6.743  11.926  -4.244  1.00 23.77  ? 88  ILE A CG2   1 
ATOM   636  C CD1   . ILE A 1 95  ? -8.684  11.266  -1.967  1.00 25.28  ? 88  ILE A CD1   1 
ATOM   637  N N     . ARG A 1 96  ? -3.578  10.462  -5.062  1.00 18.81  ? 89  ARG A N     1 
ATOM   638  C CA    . ARG A 1 96  ? -2.506  11.194  -5.781  1.00 20.19  ? 89  ARG A CA    1 
ATOM   639  C C     . ARG A 1 96  ? -2.768  11.113  -7.288  1.00 18.31  ? 89  ARG A C     1 
ATOM   640  O O     . ARG A 1 96  ? -3.505  10.216  -7.746  1.00 17.71  ? 89  ARG A O     1 
ATOM   641  C CB    . ARG A 1 96  ? -1.117  10.648  -5.428  1.00 21.44  ? 89  ARG A CB    1 
ATOM   642  C CG    . ARG A 1 96  ? -1.040  9.134   -5.343  1.00 22.03  ? 89  ARG A CG    1 
ATOM   643  C CD    . ARG A 1 96  ? 0.174   8.516   -6.026  1.00 23.20  ? 89  ARG A CD    1 
ATOM   644  N NE    . ARG A 1 96  ? -0.216  8.118   -7.347  1.00 25.28  ? 89  ARG A NE    1 
ATOM   645  C CZ    . ARG A 1 96  ? 0.098   6.999   -7.982  1.00 21.96  ? 89  ARG A CZ    1 
ATOM   646  N NH1   . ARG A 1 96  ? 0.865   6.072   -7.451  1.00 21.84  ? 89  ARG A NH1   1 
ATOM   647  N NH2   . ARG A 1 96  ? -0.384  6.828   -9.191  1.00 24.36  ? 89  ARG A NH2   1 
ATOM   648  N N     . ALA A 1 97  ? -2.200  12.056  -8.025  1.00 18.37  ? 90  ALA A N     1 
ATOM   649  C CA    . ALA A 1 97  ? -2.231  12.100  -9.497  1.00 17.55  ? 90  ALA A CA    1 
ATOM   650  C C     . ALA A 1 97  ? -1.773  10.750  -10.018 1.00 17.30  ? 90  ALA A C     1 
ATOM   651  O O     . ALA A 1 97  ? -0.952  10.098  -9.382  1.00 19.43  ? 90  ALA A O     1 
ATOM   652  C CB    . ALA A 1 97  ? -1.370  13.218  -9.998  1.00 17.45  ? 90  ALA A CB    1 
ATOM   653  N N     . PRO A 1 98  ? -2.294  10.296  -11.181 1.00 17.22  ? 91  PRO A N     1 
ATOM   654  C CA    . PRO A 1 98  ? -1.877  9.023   -11.770 1.00 17.18  ? 91  PRO A CA    1 
ATOM   655  C C     . PRO A 1 98  ? -0.454  9.046   -12.334 1.00 16.22  ? 91  PRO A C     1 
ATOM   656  O O     . PRO A 1 98  ? 0.045   8.015   -12.658 1.00 17.15  ? 91  PRO A O     1 
ATOM   657  C CB    . PRO A 1 98  ? -2.894  8.776   -12.904 1.00 18.02  ? 91  PRO A CB    1 
ATOM   658  C CG    . PRO A 1 98  ? -3.417  10.184  -13.272 1.00 16.88  ? 91  PRO A CG    1 
ATOM   659  C CD    . PRO A 1 98  ? -3.262  11.026  -12.025 1.00 16.79  ? 91  PRO A CD    1 
ATOM   660  N N     . THR A 1 99  ? 0.172   10.210  -12.441 1.00 16.32  ? 92  THR A N     1 
ATOM   661  C CA    . THR A 1 99  ? 1.541   10.349  -12.981 1.00 16.35  ? 92  THR A CA    1 
ATOM   662  C C     . THR A 1 99  ? 2.389   11.172  -12.011 1.00 18.03  ? 92  THR A C     1 
ATOM   663  O O     . THR A 1 99  ? 1.838   12.039  -11.306 1.00 18.04  ? 92  THR A O     1 
ATOM   664  C CB    . THR A 1 99  ? 1.512   10.976  -14.379 1.00 16.61  ? 92  THR A CB    1 
ATOM   665  O OG1   . THR A 1 99  ? 1.138   12.361  -14.311 1.00 15.39  ? 92  THR A OG1   1 
ATOM   666  C CG2   . THR A 1 99  ? 0.568   10.232  -15.290 1.00 15.94  ? 92  THR A CG2   1 
ATOM   667  N N     . ILE A 1 100 ? 3.684   10.893  -12.009 1.00 21.07  ? 93  ILE A N     1 
ATOM   668  C CA    . ILE A 1 100 ? 4.735   11.582  -11.205 1.00 25.05  ? 93  ILE A CA    1 
ATOM   669  C C     . ILE A 1 100 ? 4.737   13.080  -11.542 1.00 25.22  ? 93  ILE A C     1 
ATOM   670  O O     . ILE A 1 100 ? 4.740   13.901  -10.589 1.00 24.89  ? 93  ILE A O     1 
ATOM   671  C CB    . ILE A 1 100 ? 6.079   10.870  -11.451 1.00 26.85  ? 93  ILE A CB    1 
ATOM   672  C CG1   . ILE A 1 100 ? 6.092   9.536   -10.709 1.00 26.68  ? 93  ILE A CG1   1 
ATOM   673  C CG2   . ILE A 1 100 ? 7.276   11.740  -11.092 1.00 28.46  ? 93  ILE A CG2   1 
ATOM   674  C CD1   . ILE A 1 100 ? 7.218   8.594   -11.110 1.00 29.43  ? 93  ILE A CD1   1 
ATOM   675  N N     . GLU A 1 101 ? 4.634   13.418  -12.832 1.00 26.39  ? 94  GLU A N     1 
ATOM   676  C CA    . GLU A 1 101 ? 4.676   14.817  -13.344 1.00 26.43  ? 94  GLU A CA    1 
ATOM   677  C C     . GLU A 1 101 ? 3.477   15.610  -12.802 1.00 26.57  ? 94  GLU A C     1 
ATOM   678  O O     . GLU A 1 101 ? 3.668   16.747  -12.356 1.00 31.36  ? 94  GLU A O     1 
ATOM   679  C CB    . GLU A 1 101 ? 4.660   14.805  -14.872 1.00 28.62  ? 94  GLU A CB    1 
ATOM   680  C CG    . GLU A 1 101 ? 5.896   14.165  -15.484 1.00 30.69  ? 94  GLU A CG    1 
ATOM   681  C CD    . GLU A 1 101 ? 5.889   12.650  -15.617 1.00 32.68  ? 94  GLU A CD    1 
ATOM   682  O OE1   . GLU A 1 101 ? 5.023   11.977  -14.971 1.00 35.72  ? 94  GLU A OE1   1 
ATOM   683  O OE2   . GLU A 1 101 ? 6.773   12.140  -16.345 1.00 33.36  ? 94  GLU A OE2   1 
ATOM   684  N N     . GLN A 1 102 ? 2.285   15.017  -12.809 1.00 22.80  ? 95  GLN A N     1 
ATOM   685  C CA    . GLN A 1 102 ? 1.040   15.659  -12.298 1.00 22.41  ? 95  GLN A CA    1 
ATOM   686  C C     . GLN A 1 102 ? 0.957   15.652  -10.765 1.00 22.49  ? 95  GLN A C     1 
ATOM   687  O O     . GLN A 1 102 ? 0.154   16.441  -10.217 1.00 21.02  ? 95  GLN A O     1 
ATOM   688  C CB    . GLN A 1 102 ? -0.174  14.965  -12.901 1.00 21.03  ? 95  GLN A CB    1 
ATOM   689  C CG    . GLN A 1 102 ? -0.221  15.125  -14.414 1.00 19.42  ? 95  GLN A CG    1 
ATOM   690  C CD    . GLN A 1 102 ? -1.378  14.371  -15.018 1.00 18.99  ? 95  GLN A CD    1 
ATOM   691  O OE1   . GLN A 1 102 ? -1.417  13.130  -14.999 1.00 17.71  ? 95  GLN A OE1   1 
ATOM   692  N NE2   . GLN A 1 102 ? -2.321  15.127  -15.574 1.00 17.00  ? 95  GLN A NE2   1 
ATOM   693  N N     . MET A 1 103 ? 1.755   14.825  -10.077 1.00 24.85  ? 96  MET A N     1 
ATOM   694  C CA    . MET A 1 103 ? 1.616   14.617  -8.601  1.00 23.44  ? 96  MET A CA    1 
ATOM   695  C C     . MET A 1 103 ? 2.391   15.710  -7.866  1.00 21.89  ? 96  MET A C     1 
ATOM   696  O O     . MET A 1 103 ? 3.597   15.658  -7.871  1.00 20.65  ? 96  MET A O     1 
ATOM   697  C CB    . MET A 1 103 ? 2.149   13.249  -8.161  1.00 24.16  ? 96  MET A CB    1 
ATOM   698  C CG    . MET A 1 103 ? 2.270   13.129  -6.642  1.00 24.92  ? 96  MET A CG    1 
ATOM   699  S SD    . MET A 1 103 ? 2.591   11.463  -6.028  1.00 24.42  ? 96  MET A SD    1 
ATOM   700  C CE    . MET A 1 103 ? 4.338   11.341  -6.428  1.00 24.47  ? 96  MET A CE    1 
ATOM   701  N N     . LYS A 1 104 ? 1.698   16.619  -7.197  1.00 24.65  ? 97  LYS A N     1 
ATOM   702  C CA    . LYS A 1 104 ? 2.289   17.744  -6.424  1.00 25.09  ? 97  LYS A CA    1 
ATOM   703  C C     . LYS A 1 104 ? 2.030   17.483  -4.953  1.00 23.86  ? 97  LYS A C     1 
ATOM   704  O O     . LYS A 1 104 ? 2.877   17.809  -4.154  1.00 23.02  ? 97  LYS A O     1 
ATOM   705  C CB    . LYS A 1 104 ? 1.620   19.061  -6.832  1.00 28.10  ? 97  LYS A CB    1 
ATOM   706  C CG    . LYS A 1 104 ? 1.736   19.414  -8.320  1.00 32.21  ? 97  LYS A CG    1 
ATOM   707  C CD    . LYS A 1 104 ? 2.941   20.280  -8.647  1.00 34.66  ? 97  LYS A CD    1 
ATOM   708  C CE    . LYS A 1 104 ? 3.617   20.002  -9.986  1.00 37.92  ? 97  LYS A CE    1 
ATOM   709  N NZ    . LYS A 1 104 ? 2.730   19.407  -11.018 1.00 36.45  ? 97  LYS A NZ    1 
ATOM   710  N N     . ASP A 1 105 ? 0.833   16.981  -4.661  1.00 24.28  ? 98  ASP A N     1 
ATOM   711  C CA    . ASP A 1 105 ? 0.299   16.663  -3.319  1.00 23.54  ? 98  ASP A CA    1 
ATOM   712  C C     . ASP A 1 105 ? -0.063  15.186  -3.259  1.00 24.70  ? 98  ASP A C     1 
ATOM   713  O O     . ASP A 1 105 ? -0.414  14.605  -4.331  1.00 22.41  ? 98  ASP A O     1 
ATOM   714  C CB    . ASP A 1 105 ? -0.987  17.429  -3.036  1.00 23.47  ? 98  ASP A CB    1 
ATOM   715  C CG    . ASP A 1 105 ? -0.854  18.897  -3.383  1.00 24.91  ? 98  ASP A CG    1 
ATOM   716  O OD1   . ASP A 1 105 ? 0.196   19.489  -3.048  1.00 25.21  ? 98  ASP A OD1   1 
ATOM   717  O OD2   . ASP A 1 105 ? -1.767  19.419  -4.032  1.00 29.30  ? 98  ASP A OD2   1 
ATOM   718  N N     . VAL A 1 106 ? -0.039  14.640  -2.042  1.00 22.54  ? 99  VAL A N     1 
ATOM   719  C CA    . VAL A 1 106 ? -0.629  13.318  -1.715  1.00 22.36  ? 99  VAL A CA    1 
ATOM   720  C C     . VAL A 1 106 ? -1.612  13.511  -0.564  1.00 21.21  ? 99  VAL A C     1 
ATOM   721  O O     . VAL A 1 106 ? -1.309  14.315  0.330   1.00 21.49  ? 99  VAL A O     1 
ATOM   722  C CB    . VAL A 1 106 ? 0.502   12.356  -1.350  1.00 24.85  ? 99  VAL A CB    1 
ATOM   723  C CG1   . VAL A 1 106 ? -0.019  11.012  -0.861  1.00 25.10  ? 99  VAL A CG1   1 
ATOM   724  C CG2   . VAL A 1 106 ? 1.457   12.218  -2.520  1.00 25.58  ? 99  VAL A CG2   1 
ATOM   725  N N     . TYR A 1 107 ? -2.737  12.800  -0.592  1.00 18.87  ? 100 TYR A N     1 
ATOM   726  C CA    . TYR A 1 107 ? -3.778  12.855  0.454   1.00 19.38  ? 100 TYR A CA    1 
ATOM   727  C C     . TYR A 1 107 ? -3.884  11.494  1.135   1.00 20.12  ? 100 TYR A C     1 
ATOM   728  O O     . TYR A 1 107 ? -4.124  10.477  0.455   1.00 19.40  ? 100 TYR A O     1 
ATOM   729  C CB    . TYR A 1 107 ? -5.129  13.252  -0.120  1.00 20.09  ? 100 TYR A CB    1 
ATOM   730  C CG    . TYR A 1 107 ? -5.163  14.589  -0.812  1.00 21.60  ? 100 TYR A CG    1 
ATOM   731  C CD1   . TYR A 1 107 ? -4.699  14.759  -2.104  1.00 21.94  ? 100 TYR A CD1   1 
ATOM   732  C CD2   . TYR A 1 107 ? -5.692  15.688  -0.167  1.00 23.43  ? 100 TYR A CD2   1 
ATOM   733  C CE1   . TYR A 1 107 ? -4.764  15.991  -2.739  1.00 24.25  ? 100 TYR A CE1   1 
ATOM   734  C CE2   . TYR A 1 107 ? -5.761  16.927  -0.782  1.00 24.87  ? 100 TYR A CE2   1 
ATOM   735  C CZ    . TYR A 1 107 ? -5.305  17.085  -2.079  1.00 25.38  ? 100 TYR A CZ    1 
ATOM   736  O OH    . TYR A 1 107 ? -5.432  18.320  -2.665  1.00 24.69  ? 100 TYR A OH    1 
ATOM   737  N N     . ILE A 1 108 ? -3.700  11.478  2.450   1.00 18.91  ? 101 ILE A N     1 
ATOM   738  C CA    . ILE A 1 108 ? -3.726  10.213  3.223   1.00 20.56  ? 101 ILE A CA    1 
ATOM   739  C C     . ILE A 1 108 ? -5.089  10.160  3.893   1.00 20.46  ? 101 ILE A C     1 
ATOM   740  O O     . ILE A 1 108 ? -5.471  11.133  4.523   1.00 20.73  ? 101 ILE A O     1 
ATOM   741  C CB    . ILE A 1 108 ? -2.507  10.169  4.156   1.00 21.15  ? 101 ILE A CB    1 
ATOM   742  C CG1   . ILE A 1 108 ? -1.235  10.110  3.300   1.00 22.36  ? 101 ILE A CG1   1 
ATOM   743  C CG2   . ILE A 1 108 ? -2.578  9.013   5.124   1.00 21.13  ? 101 ILE A CG2   1 
ATOM   744  C CD1   . ILE A 1 108 ? 0.015   10.318  4.087   1.00 23.30  ? 101 ILE A CD1   1 
ATOM   745  N N     . VAL A 1 109 ? -5.845  9.105   3.643   1.00 19.44  ? 102 VAL A N     1 
ATOM   746  C CA    . VAL A 1 109 ? -7.169  8.937   4.292   1.00 20.06  ? 102 VAL A CA    1 
ATOM   747  C C     . VAL A 1 109 ? -6.968  7.989   5.473   1.00 21.25  ? 102 VAL A C     1 
ATOM   748  O O     . VAL A 1 109 ? -6.263  6.943   5.295   1.00 20.19  ? 102 VAL A O     1 
ATOM   749  C CB    . VAL A 1 109 ? -8.231  8.405   3.319   1.00 19.37  ? 102 VAL A CB    1 
ATOM   750  C CG1   . VAL A 1 109 ? -9.577  8.243   4.014   1.00 20.15  ? 102 VAL A CG1   1 
ATOM   751  C CG2   . VAL A 1 109 ? -8.338  9.273   2.088   1.00 18.55  ? 102 VAL A CG2   1 
ATOM   752  N N     . GLN A 1 110 ? -7.583  8.354   6.595   1.00 21.39  ? 103 GLN A N     1 
ATOM   753  C CA    . GLN A 1 110 ? -7.412  7.712   7.918   1.00 23.98  ? 103 GLN A CA    1 
ATOM   754  C C     . GLN A 1 110 ? -8.737  7.735   8.681   1.00 25.35  ? 103 GLN A C     1 
ATOM   755  O O     . GLN A 1 110 ? -9.520  8.706   8.515   1.00 25.10  ? 103 GLN A O     1 
ATOM   756  C CB    . GLN A 1 110 ? -6.383  8.492   8.724   1.00 22.75  ? 103 GLN A CB    1 
ATOM   757  C CG    . GLN A 1 110 ? -4.950  8.127   8.387   1.00 24.86  ? 103 GLN A CG    1 
ATOM   758  C CD    . GLN A 1 110 ? -3.982  8.992   9.152   1.00 25.97  ? 103 GLN A CD    1 
ATOM   759  O OE1   . GLN A 1 110 ? -4.377  9.906   9.872   1.00 25.16  ? 103 GLN A OE1   1 
ATOM   760  N NE2   . GLN A 1 110 ? -2.706  8.701   9.003   1.00 27.70  ? 103 GLN A NE2   1 
ATOM   761  N N     . ASP A 1 111 ? -8.937  6.755   9.558   1.00 26.58  ? 104 ASP A N     1 
ATOM   762  C CA    . ASP A 1 111 ? -10.073 6.780   10.513  1.00 26.53  ? 104 ASP A CA    1 
ATOM   763  C C     . ASP A 1 111 ? -10.139 8.169   11.132  1.00 24.86  ? 104 ASP A C     1 
ATOM   764  O O     . ASP A 1 111 ? -9.077  8.727   11.495  1.00 24.35  ? 104 ASP A O     1 
ATOM   765  C CB    . ASP A 1 111 ? -9.966  5.672   11.555  1.00 27.25  ? 104 ASP A CB    1 
ATOM   766  C CG    . ASP A 1 111 ? -10.198 4.320   10.921  1.00 28.93  ? 104 ASP A CG    1 
ATOM   767  O OD1   . ASP A 1 111 ? -9.967  4.224   9.706   1.00 29.81  ? 104 ASP A OD1   1 
ATOM   768  O OD2   . ASP A 1 111 ? -10.635 3.388   11.630  1.00 34.84  ? 104 ASP A OD2   1 
ATOM   769  N N     . LEU A 1 112 ? -11.346 8.719   11.199  1.00 24.46  ? 105 LEU A N     1 
ATOM   770  C CA    . LEU A 1 112 ? -11.581 9.998   11.891  1.00 24.71  ? 105 LEU A CA    1 
ATOM   771  C C     . LEU A 1 112 ? -11.422 9.753   13.392  1.00 25.39  ? 105 LEU A C     1 
ATOM   772  O O     . LEU A 1 112 ? -12.171 8.901   13.940  1.00 23.69  ? 105 LEU A O     1 
ATOM   773  C CB    . LEU A 1 112 ? -12.984 10.513  11.577  1.00 25.61  ? 105 LEU A CB    1 
ATOM   774  C CG    . LEU A 1 112 ? -13.306 11.883  12.171  1.00 24.68  ? 105 LEU A CG    1 
ATOM   775  C CD1   . LEU A 1 112 ? -12.254 12.917  11.790  1.00 22.62  ? 105 LEU A CD1   1 
ATOM   776  C CD2   . LEU A 1 112 ? -14.698 12.340  11.753  1.00 26.06  ? 105 LEU A CD2   1 
ATOM   777  N N     . MET A 1 113 ? -10.483 10.446  14.027  1.00 22.65  ? 106 MET A N     1 
ATOM   778  C CA    . MET A 1 113 ? -10.336 10.391  15.498  1.00 26.68  ? 106 MET A CA    1 
ATOM   779  C C     . MET A 1 113 ? -10.798 11.723  16.078  1.00 27.09  ? 106 MET A C     1 
ATOM   780  O O     . MET A 1 113 ? -10.371 12.766  15.577  1.00 34.66  ? 106 MET A O     1 
ATOM   781  C CB    . MET A 1 113 ? -8.882  10.118  15.874  1.00 25.46  ? 106 MET A CB    1 
ATOM   782  C CG    . MET A 1 113 ? -8.355  8.854   15.260  1.00 25.33  ? 106 MET A CG    1 
ATOM   783  S SD    . MET A 1 113 ? -9.134  7.351   15.915  1.00 24.75  ? 106 MET A SD    1 
ATOM   784  C CE    . MET A 1 113 ? -8.320  7.264   17.511  1.00 23.49  ? 106 MET A CE    1 
ATOM   785  N N     . GLU A 1 114 ? -11.623 11.699  17.109  1.00 28.15  ? 107 GLU A N     1 
ATOM   786  C CA    . GLU A 1 114 ? -12.328 12.928  17.543  1.00 31.85  ? 107 GLU A CA    1 
ATOM   787  C C     . GLU A 1 114 ? -11.372 13.874  18.279  1.00 29.49  ? 107 GLU A C     1 
ATOM   788  O O     . GLU A 1 114 ? -11.692 15.060  18.314  1.00 27.50  ? 107 GLU A O     1 
ATOM   789  C CB    . GLU A 1 114 ? -13.591 12.562  18.324  1.00 36.60  ? 107 GLU A CB    1 
ATOM   790  C CG    . GLU A 1 114 ? -14.782 12.345  17.389  1.00 41.17  ? 107 GLU A CG    1 
ATOM   791  C CD    . GLU A 1 114 ? -14.658 11.199  16.388  1.00 47.32  ? 107 GLU A CD    1 
ATOM   792  O OE1   . GLU A 1 114 ? -15.190 11.348  15.258  1.00 49.19  ? 107 GLU A OE1   1 
ATOM   793  O OE2   . GLU A 1 114 ? -14.037 10.149  16.736  1.00 50.63  ? 107 GLU A OE2   1 
ATOM   794  N N     . THR A 1 115 ? -10.243 13.396  18.820  1.00 26.10  ? 108 THR A N     1 
ATOM   795  C CA    . THR A 1 115 ? -9.335  14.222  19.657  1.00 24.14  ? 108 THR A CA    1 
ATOM   796  C C     . THR A 1 115 ? -7.961  13.541  19.769  1.00 23.14  ? 108 THR A C     1 
ATOM   797  O O     . THR A 1 115 ? -7.733  12.516  19.127  1.00 22.05  ? 108 THR A O     1 
ATOM   798  C CB    . THR A 1 115 ? -10.009 14.511  21.011  1.00 23.16  ? 108 THR A CB    1 
ATOM   799  O OG1   . THR A 1 115 ? -9.272  15.466  21.758  1.00 23.31  ? 108 THR A OG1   1 
ATOM   800  C CG2   . THR A 1 115 ? -10.134 13.304  21.900  1.00 24.25  ? 108 THR A CG2   1 
ATOM   801  N N     . ASP A 1 116 ? -7.066  14.106  20.565  1.00 22.42  ? 109 ASP A N     1 
ATOM   802  C CA    . ASP A 1 116 ? -5.773  13.461  20.909  1.00 22.44  ? 109 ASP A CA    1 
ATOM   803  C C     . ASP A 1 116 ? -5.486  13.727  22.381  1.00 21.12  ? 109 ASP A C     1 
ATOM   804  O O     . ASP A 1 116 ? -6.219  14.521  23.037  1.00 19.15  ? 109 ASP A O     1 
ATOM   805  C CB    . ASP A 1 116 ? -4.637  13.932  20.008  1.00 21.73  ? 109 ASP A CB    1 
ATOM   806  C CG    . ASP A 1 116 ? -4.397  15.424  20.063  1.00 24.40  ? 109 ASP A CG    1 
ATOM   807  O OD1   . ASP A 1 116 ? -4.207  15.971  21.191  1.00 20.57  ? 109 ASP A OD1   1 
ATOM   808  O OD2   . ASP A 1 116 ? -4.392  16.026  18.971  1.00 27.92  ? 109 ASP A OD2   1 
ATOM   809  N N     . LEU A 1 117 ? -4.466  13.062  22.889  1.00 19.11  ? 110 LEU A N     1 
ATOM   810  C CA    . LEU A 1 117 ? -4.186  13.098  24.334  1.00 18.72  ? 110 LEU A CA    1 
ATOM   811  C C     . LEU A 1 117 ? -3.747  14.519  24.725  1.00 19.24  ? 110 LEU A C     1 
ATOM   812  O O     . LEU A 1 117 ? -4.006  14.921  25.883  1.00 19.34  ? 110 LEU A O     1 
ATOM   813  C CB    . LEU A 1 117 ? -3.135  12.033  24.641  1.00 17.25  ? 110 LEU A CB    1 
ATOM   814  C CG    . LEU A 1 117 ? -2.924  11.726  26.113  1.00 15.77  ? 110 LEU A CG    1 
ATOM   815  C CD1   . LEU A 1 117 ? -4.239  11.499  26.805  1.00 15.51  ? 110 LEU A CD1   1 
ATOM   816  C CD2   . LEU A 1 117 ? -2.012  10.528  26.258  1.00 15.76  ? 110 LEU A CD2   1 
ATOM   817  N N     . TYR A 1 118 ? -3.090  15.250  23.825  1.00 21.13  ? 111 TYR A N     1 
ATOM   818  C CA    . TYR A 1 118 ? -2.633  16.636  24.104  1.00 24.04  ? 111 TYR A CA    1 
ATOM   819  C C     . TYR A 1 118 ? -3.892  17.476  24.408  1.00 22.86  ? 111 TYR A C     1 
ATOM   820  O O     . TYR A 1 118 ? -4.046  17.906  25.529  1.00 20.48  ? 111 TYR A O     1 
ATOM   821  C CB    . TYR A 1 118 ? -1.723  17.161  22.987  1.00 25.34  ? 111 TYR A CB    1 
ATOM   822  C CG    . TYR A 1 118 ? -1.368  18.615  23.143  1.00 30.85  ? 111 TYR A CG    1 
ATOM   823  C CD1   . TYR A 1 118 ? -0.281  19.022  23.904  1.00 32.03  ? 111 TYR A CD1   1 
ATOM   824  C CD2   . TYR A 1 118 ? -2.169  19.593  22.573  1.00 35.44  ? 111 TYR A CD2   1 
ATOM   825  C CE1   . TYR A 1 118 ? 0.008   20.365  24.089  1.00 33.72  ? 111 TYR A CE1   1 
ATOM   826  C CE2   . TYR A 1 118 ? -1.881  20.937  22.724  1.00 37.78  ? 111 TYR A CE2   1 
ATOM   827  C CZ    . TYR A 1 118 ? -0.796  21.326  23.490  1.00 40.58  ? 111 TYR A CZ    1 
ATOM   828  O OH    . TYR A 1 118 ? -0.551  22.663  23.634  1.00 46.62  ? 111 TYR A OH    1 
ATOM   829  N N     . LYS A 1 119 ? -4.808  17.572  23.448  1.00 26.39  ? 112 LYS A N     1 
ATOM   830  C CA    . LYS A 1 119 ? -6.101  18.317  23.511  1.00 26.30  ? 112 LYS A CA    1 
ATOM   831  C C     . LYS A 1 119 ? -6.927  17.835  24.700  1.00 26.64  ? 112 LYS A C     1 
ATOM   832  O O     . LYS A 1 119 ? -7.541  18.675  25.379  1.00 31.59  ? 112 LYS A O     1 
ATOM   833  C CB    . LYS A 1 119 ? -6.887  18.148  22.209  1.00 27.55  ? 112 LYS A CB    1 
ATOM   834  C CG    . LYS A 1 119 ? -6.130  18.572  20.960  1.00 30.90  ? 112 LYS A CG    1 
ATOM   835  C CD    . LYS A 1 119 ? -7.010  19.226  19.909  1.00 34.79  ? 112 LYS A CD    1 
ATOM   836  C CE    . LYS A 1 119 ? -6.228  20.117  18.963  1.00 37.50  ? 112 LYS A CE    1 
ATOM   837  N NZ    . LYS A 1 119 ? -7.059  20.558  17.814  1.00 40.97  ? 112 LYS A NZ    1 
ATOM   838  N N     . LEU A 1 120 ? -6.877  16.543  25.009  1.00 25.63  ? 113 LEU A N     1 
ATOM   839  C CA    . LEU A 1 120 ? -7.625  15.973  26.151  1.00 24.27  ? 113 LEU A CA    1 
ATOM   840  C C     . LEU A 1 120 ? -7.004  16.457  27.467  1.00 25.72  ? 113 LEU A C     1 
ATOM   841  O O     . LEU A 1 120 ? -7.766  16.745  28.415  1.00 25.28  ? 113 LEU A O     1 
ATOM   842  C CB    . LEU A 1 120 ? -7.630  14.448  26.018  1.00 24.81  ? 113 LEU A CB    1 
ATOM   843  C CG    . LEU A 1 120 ? -8.812  13.703  26.638  1.00 25.56  ? 113 LEU A CG    1 
ATOM   844  C CD1   . LEU A 1 120 ? -10.151 14.265  26.218  1.00 25.62  ? 113 LEU A CD1   1 
ATOM   845  C CD2   . LEU A 1 120 ? -8.768  12.241  26.264  1.00 27.77  ? 113 LEU A CD2   1 
ATOM   846  N N     . LEU A 1 121 ? -5.674  16.534  27.567  1.00 27.00  ? 114 LEU A N     1 
ATOM   847  C CA    . LEU A 1 121 ? -5.023  16.790  28.888  1.00 26.22  ? 114 LEU A CA    1 
ATOM   848  C C     . LEU A 1 121 ? -5.136  18.273  29.277  1.00 25.84  ? 114 LEU A C     1 
ATOM   849  O O     . LEU A 1 121 ? -5.015  18.587  30.475  1.00 23.94  ? 114 LEU A O     1 
ATOM   850  C CB    . LEU A 1 121 ? -3.562  16.362  28.840  1.00 24.95  ? 114 LEU A CB    1 
ATOM   851  C CG    . LEU A 1 121 ? -3.360  14.856  28.836  1.00 27.34  ? 114 LEU A CG    1 
ATOM   852  C CD1   . LEU A 1 121 ? -1.918  14.502  28.472  1.00 25.08  ? 114 LEU A CD1   1 
ATOM   853  C CD2   . LEU A 1 121 ? -3.774  14.255  30.175  1.00 27.13  ? 114 LEU A CD2   1 
ATOM   854  N N     . LYS A 1 122 ? -5.354  19.150  28.315  1.00 25.68  ? 115 LYS A N     1 
ATOM   855  C CA    . LYS A 1 122 ? -5.450  20.604  28.605  1.00 31.52  ? 115 LYS A CA    1 
ATOM   856  C C     . LYS A 1 122 ? -6.782  20.917  29.298  1.00 29.47  ? 115 LYS A C     1 
ATOM   857  O O     . LYS A 1 122 ? -6.842  21.962  29.941  1.00 31.21  ? 115 LYS A O     1 
ATOM   858  C CB    . LYS A 1 122 ? -5.376  21.440  27.326  1.00 33.39  ? 115 LYS A CB    1 
ATOM   859  C CG    . LYS A 1 122 ? -4.207  21.129  26.410  1.00 34.33  ? 115 LYS A CG    1 
ATOM   860  C CD    . LYS A 1 122 ? -4.625  21.123  24.947  1.00 36.09  ? 115 LYS A CD    1 
ATOM   861  C CE    . LYS A 1 122 ? -4.497  22.466  24.249  1.00 36.52  ? 115 LYS A CE    1 
ATOM   862  N NZ    . LYS A 1 122 ? -5.159  22.431  22.921  1.00 37.18  ? 115 LYS A NZ    1 
ATOM   863  N N     . THR A 1 123 ? -7.808  20.073  29.128  1.00 27.49  ? 116 THR A N     1 
ATOM   864  C CA    . THR A 1 123 ? -9.202  20.379  29.536  1.00 27.47  ? 116 THR A CA    1 
ATOM   865  C C     . THR A 1 123 ? -9.789  19.252  30.406  1.00 27.17  ? 116 THR A C     1 
ATOM   866  O O     . THR A 1 123 ? -10.685 19.554  31.223  1.00 32.11  ? 116 THR A O     1 
ATOM   867  C CB    . THR A 1 123 ? -10.044 20.710  28.294  1.00 29.47  ? 116 THR A CB    1 
ATOM   868  O OG1   . THR A 1 123 ? -10.157 19.547  27.474  1.00 30.69  ? 116 THR A OG1   1 
ATOM   869  C CG2   . THR A 1 123 ? -9.466  21.837  27.455  1.00 30.62  ? 116 THR A CG2   1 
ATOM   870  N N     . GLN A 1 124 ? -9.358  17.991  30.270  1.00 23.92  ? 117 GLN A N     1 
ATOM   871  C CA    . GLN A 1 124 ? -10.041 16.887  30.997  1.00 21.25  ? 117 GLN A CA    1 
ATOM   872  C C     . GLN A 1 124 ? -9.127  16.323  32.097  1.00 21.69  ? 117 GLN A C     1 
ATOM   873  O O     . GLN A 1 124 ? -7.942  15.968  31.823  1.00 20.49  ? 117 GLN A O     1 
ATOM   874  C CB    . GLN A 1 124 ? -10.535 15.789  30.040  1.00 19.43  ? 117 GLN A CB    1 
ATOM   875  C CG    . GLN A 1 124 ? -11.352 16.282  28.845  1.00 19.79  ? 117 GLN A CG    1 
ATOM   876  C CD    . GLN A 1 124 ? -12.595 17.050  29.227  1.00 20.78  ? 117 GLN A CD    1 
ATOM   877  O OE1   . GLN A 1 124 ? -13.211 16.775  30.256  1.00 21.02  ? 117 GLN A OE1   1 
ATOM   878  N NE2   . GLN A 1 124 ? -12.941 18.053  28.432  1.00 18.51  ? 117 GLN A NE2   1 
ATOM   879  N N     . HIS A 1 125 ? -9.691  16.195  33.291  1.00 19.29  ? 118 HIS A N     1 
ATOM   880  C CA    . HIS A 1 125 ? -9.227  15.268  34.339  1.00 22.61  ? 118 HIS A CA    1 
ATOM   881  C C     . HIS A 1 125 ? -9.464  13.827  33.853  1.00 22.53  ? 118 HIS A C     1 
ATOM   882  O O     . HIS A 1 125 ? -10.601 13.520  33.402  1.00 17.68  ? 118 HIS A O     1 
ATOM   883  C CB    . HIS A 1 125 ? -9.968  15.594  35.641  1.00 25.76  ? 118 HIS A CB    1 
ATOM   884  C CG    . HIS A 1 125 ? -9.648  14.621  36.721  1.00 32.26  ? 118 HIS A CG    1 
ATOM   885  N ND1   . HIS A 1 125 ? -10.541 13.634  37.119  1.00 35.43  ? 118 HIS A ND1   1 
ATOM   886  C CD2   . HIS A 1 125 ? -8.524  14.446  37.454  1.00 34.37  ? 118 HIS A CD2   1 
ATOM   887  C CE1   . HIS A 1 125 ? -9.987  12.898  38.058  1.00 35.54  ? 118 HIS A CE1   1 
ATOM   888  N NE2   . HIS A 1 125 ? -8.745  13.374  38.281  1.00 39.09  ? 118 HIS A NE2   1 
ATOM   889  N N     . LEU A 1 126 ? -8.446  12.959  33.909  1.00 23.30  ? 119 LEU A N     1 
ATOM   890  C CA    . LEU A 1 126 ? -8.625  11.503  33.622  1.00 22.74  ? 119 LEU A CA    1 
ATOM   891  C C     . LEU A 1 126 ? -8.895  10.796  34.953  1.00 20.59  ? 119 LEU A C     1 
ATOM   892  O O     . LEU A 1 126 ? -8.177  11.088  35.895  1.00 20.95  ? 119 LEU A O     1 
ATOM   893  C CB    . LEU A 1 126 ? -7.378  10.922  32.946  1.00 25.11  ? 119 LEU A CB    1 
ATOM   894  C CG    . LEU A 1 126 ? -7.185  11.224  31.457  1.00 27.56  ? 119 LEU A CG    1 
ATOM   895  C CD1   . LEU A 1 126 ? -7.368  12.686  31.147  1.00 27.71  ? 119 LEU A CD1   1 
ATOM   896  C CD2   . LEU A 1 126 ? -5.815  10.752  30.971  1.00 28.68  ? 119 LEU A CD2   1 
ATOM   897  N N     . SER A 1 127 ? -9.908  9.924   35.033  1.00 19.77  ? 120 SER A N     1 
ATOM   898  C CA    . SER A 1 127 ? -10.037 8.901   36.100  1.00 19.75  ? 120 SER A CA    1 
ATOM   899  C C     . SER A 1 127 ? -8.821  7.980   36.004  1.00 17.99  ? 120 SER A C     1 
ATOM   900  O O     . SER A 1 127 ? -8.225  7.942   34.917  1.00 17.00  ? 120 SER A O     1 
ATOM   901  C CB    . SER A 1 127 ? -11.311 8.099   35.975  1.00 20.36  ? 120 SER A CB    1 
ATOM   902  O OG    . SER A 1 127 ? -11.338 7.359   34.754  1.00 21.03  ? 120 SER A OG    1 
ATOM   903  N N     . ASN A 1 128 ? -8.543  7.233   37.072  1.00 18.65  ? 121 ASN A N     1 
ATOM   904  C CA    . ASN A 1 128 ? -7.509  6.158   37.145  1.00 20.55  ? 121 ASN A CA    1 
ATOM   905  C C     . ASN A 1 128 ? -7.837  5.041   36.130  1.00 19.35  ? 121 ASN A C     1 
ATOM   906  O O     . ASN A 1 128 ? -6.879  4.468   35.586  1.00 20.62  ? 121 ASN A O     1 
ATOM   907  C CB    . ASN A 1 128 ? -7.279  5.655   38.583  1.00 19.56  ? 121 ASN A CB    1 
ATOM   908  C CG    . ASN A 1 128 ? -6.094  4.706   38.709  1.00 22.63  ? 121 ASN A CG    1 
ATOM   909  O OD1   . ASN A 1 128 ? -6.179  3.670   39.390  1.00 25.05  ? 121 ASN A OD1   1 
ATOM   910  N ND2   . ASN A 1 128 ? -4.990  4.998   38.031  1.00 18.95  ? 121 ASN A ND2   1 
ATOM   911  N N     . ASP A 1 129 ? -9.114  4.774   35.821  1.00 17.07  ? 122 ASP A N     1 
ATOM   912  C CA    . ASP A 1 129 ? -9.492  3.724   34.837  1.00 17.38  ? 122 ASP A CA    1 
ATOM   913  C C     . ASP A 1 129 ? -9.031  4.162   33.443  1.00 15.53  ? 122 ASP A C     1 
ATOM   914  O O     . ASP A 1 129 ? -8.454  3.339   32.697  1.00 12.51  ? 122 ASP A O     1 
ATOM   915  C CB    . ASP A 1 129 ? -10.984 3.377   34.948  1.00 18.42  ? 122 ASP A CB    1 
ATOM   916  C CG    . ASP A 1 129 ? -11.227 2.624   36.244  1.00 20.93  ? 122 ASP A CG    1 
ATOM   917  O OD1   . ASP A 1 129 ? -10.415 1.742   36.549  1.00 25.43  ? 122 ASP A OD1   1 
ATOM   918  O OD2   . ASP A 1 129 ? -12.120 2.993   36.983  1.00 22.79  ? 122 ASP A OD2   1 
ATOM   919  N N     . HIS A 1 130 ? -9.277  5.420   33.100  1.00 15.81  ? 123 HIS A N     1 
ATOM   920  C CA    . HIS A 1 130 ? -8.860  5.997   31.802  1.00 15.56  ? 123 HIS A CA    1 
ATOM   921  C C     . HIS A 1 130 ? -7.331  5.960   31.697  1.00 15.16  ? 123 HIS A C     1 
ATOM   922  O O     . HIS A 1 130 ? -6.825  5.573   30.621  1.00 15.06  ? 123 HIS A O     1 
ATOM   923  C CB    . HIS A 1 130 ? -9.395  7.407   31.650  1.00 17.49  ? 123 HIS A CB    1 
ATOM   924  C CG    . HIS A 1 130 ? -10.855 7.453   31.361  1.00 19.14  ? 123 HIS A CG    1 
ATOM   925  N ND1   . HIS A 1 130 ? -11.799 7.583   32.373  1.00 17.43  ? 123 HIS A ND1   1 
ATOM   926  C CD2   . HIS A 1 130 ? -11.525 7.388   30.181  1.00 20.07  ? 123 HIS A CD2   1 
ATOM   927  C CE1   . HIS A 1 130 ? -12.994 7.581   31.827  1.00 19.31  ? 123 HIS A CE1   1 
ATOM   928  N NE2   . HIS A 1 130 ? -12.854 7.481   30.464  1.00 18.30  ? 123 HIS A NE2   1 
ATOM   929  N N     . ILE A 1 131 ? -6.620  6.353   32.752  1.00 14.43  ? 124 ILE A N     1 
ATOM   930  C CA    . ILE A 1 131 ? -5.140  6.453   32.666  1.00 15.00  ? 124 ILE A CA    1 
ATOM   931  C C     . ILE A 1 131 ? -4.615  5.044   32.375  1.00 13.58  ? 124 ILE A C     1 
ATOM   932  O O     . ILE A 1 131 ? -3.801  4.894   31.455  1.00 12.96  ? 124 ILE A O     1 
ATOM   933  C CB    . ILE A 1 131 ? -4.515  7.060   33.930  1.00 15.70  ? 124 ILE A CB    1 
ATOM   934  C CG1   . ILE A 1 131 ? -4.833  8.554   34.043  1.00 16.71  ? 124 ILE A CG1   1 
ATOM   935  C CG2   . ILE A 1 131 ? -3.012  6.829   33.941  1.00 15.94  ? 124 ILE A CG2   1 
ATOM   936  C CD1   . ILE A 1 131 ? -4.560  9.139   35.427  1.00 17.78  ? 124 ILE A CD1   1 
ATOM   937  N N     . CYS A 1 132 ? -5.084  4.078   33.139  1.00 13.33  ? 125 CYS A N     1 
ATOM   938  C CA    . CYS A 1 132 ? -4.785  2.628   33.016  1.00 15.03  ? 125 CYS A CA    1 
ATOM   939  C C     . CYS A 1 132 ? -4.974  2.182   31.564  1.00 14.23  ? 125 CYS A C     1 
ATOM   940  O O     . CYS A 1 132 ? -4.009  1.668   30.969  1.00 14.21  ? 125 CYS A O     1 
ATOM   941  C CB    . CYS A 1 132 ? -5.653  1.808   33.959  1.00 15.36  ? 125 CYS A CB    1 
ATOM   942  S SG    . CYS A 1 132 ? -4.954  0.187   34.343  1.00 17.71  ? 125 CYS A SG    1 
ATOM   943  N N     . TYR A 1 133 ? -6.157  2.435   31.011  1.00 14.65  ? 126 TYR A N     1 
ATOM   944  C CA    . TYR A 1 133 ? -6.601  1.891   29.709  1.00 15.19  ? 126 TYR A CA    1 
ATOM   945  C C     . TYR A 1 133 ? -5.759  2.549   28.598  1.00 13.62  ? 126 TYR A C     1 
ATOM   946  O O     . TYR A 1 133 ? -5.358  1.858   27.675  1.00 12.66  ? 126 TYR A O     1 
ATOM   947  C CB    . TYR A 1 133 ? -8.115  2.067   29.539  1.00 15.40  ? 126 TYR A CB    1 
ATOM   948  C CG    . TYR A 1 133 ? -8.697  1.574   28.234  1.00 16.23  ? 126 TYR A CG    1 
ATOM   949  C CD1   . TYR A 1 133 ? -8.460  0.288   27.774  1.00 16.56  ? 126 TYR A CD1   1 
ATOM   950  C CD2   . TYR A 1 133 ? -9.526  2.387   27.467  1.00 17.69  ? 126 TYR A CD2   1 
ATOM   951  C CE1   . TYR A 1 133 ? -9.030  -0.176  26.599  1.00 17.24  ? 126 TYR A CE1   1 
ATOM   952  C CE2   . TYR A 1 133 ? -10.100 1.945   26.283  1.00 16.76  ? 126 TYR A CE2   1 
ATOM   953  C CZ    . TYR A 1 133 ? -9.850  0.657   25.850  1.00 17.88  ? 126 TYR A CZ    1 
ATOM   954  O OH    . TYR A 1 133 ? -10.393 0.216   24.676  1.00 19.83  ? 126 TYR A OH    1 
ATOM   955  N N     . PHE A 1 134 ? -5.528  3.853   28.704  1.00 13.26  ? 127 PHE A N     1 
ATOM   956  C CA    . PHE A 1 134 ? -4.733  4.659   27.743  1.00 13.31  ? 127 PHE A CA    1 
ATOM   957  C C     . PHE A 1 134 ? -3.315  4.116   27.713  1.00 11.58  ? 127 PHE A C     1 
ATOM   958  O O     . PHE A 1 134 ? -2.837  3.829   26.641  1.00 11.44  ? 127 PHE A O     1 
ATOM   959  C CB    . PHE A 1 134 ? -4.738  6.143   28.140  1.00 15.25  ? 127 PHE A CB    1 
ATOM   960  C CG    . PHE A 1 134 ? -6.064  6.823   27.918  1.00 16.01  ? 127 PHE A CG    1 
ATOM   961  C CD1   . PHE A 1 134 ? -7.076  6.201   27.216  1.00 16.82  ? 127 PHE A CD1   1 
ATOM   962  C CD2   . PHE A 1 134 ? -6.293  8.100   28.388  1.00 18.05  ? 127 PHE A CD2   1 
ATOM   963  C CE1   . PHE A 1 134 ? -8.303  6.806   27.023  1.00 16.80  ? 127 PHE A CE1   1 
ATOM   964  C CE2   . PHE A 1 134 ? -7.511  8.726   28.156  1.00 17.87  ? 127 PHE A CE2   1 
ATOM   965  C CZ    . PHE A 1 134 ? -8.512  8.076   27.486  1.00 17.81  ? 127 PHE A CZ    1 
ATOM   966  N N     . LEU A 1 135 ? -2.700  3.958   28.881  1.00 10.72  ? 128 LEU A N     1 
ATOM   967  C CA    . LEU A 1 135 ? -1.334  3.407   29.027  1.00 10.51  ? 128 LEU A CA    1 
ATOM   968  C C     . LEU A 1 135 ? -1.278  1.978   28.475  1.00 10.40  ? 128 LEU A C     1 
ATOM   969  O O     . LEU A 1 135 ? -0.263  1.656   27.814  1.00 10.38  ? 128 LEU A O     1 
ATOM   970  C CB    . LEU A 1 135 ? -0.888  3.471   30.493  1.00 10.15  ? 128 LEU A CB    1 
ATOM   971  C CG    . LEU A 1 135 ? 0.504   2.919   30.804  1.00 10.12  ? 128 LEU A CG    1 
ATOM   972  C CD1   . LEU A 1 135 ? 1.604   3.791   30.218  1.00 10.33  ? 128 LEU A CD1   1 
ATOM   973  C CD2   . LEU A 1 135 ? 0.730   2.718   32.310  1.00 10.15  ? 128 LEU A CD2   1 
ATOM   974  N N     . TYR A 1 136 ? -2.274  1.144   28.774  1.00 10.76  ? 129 TYR A N     1 
ATOM   975  C CA    . TYR A 1 136 ? -2.369  -0.233  28.237  1.00 11.09  ? 129 TYR A CA    1 
ATOM   976  C C     . TYR A 1 136 ? -2.314  -0.172  26.705  1.00 11.18  ? 129 TYR A C     1 
ATOM   977  O O     . TYR A 1 136 ? -1.480  -0.885  26.080  1.00 11.12  ? 129 TYR A O     1 
ATOM   978  C CB    . TYR A 1 136 ? -3.631  -0.964  28.686  1.00 11.92  ? 129 TYR A CB    1 
ATOM   979  C CG    . TYR A 1 136 ? -3.743  -2.311  28.028  1.00 12.85  ? 129 TYR A CG    1 
ATOM   980  C CD1   . TYR A 1 136 ? -2.823  -3.299  28.321  1.00 12.42  ? 129 TYR A CD1   1 
ATOM   981  C CD2   . TYR A 1 136 ? -4.701  -2.571  27.049  1.00 12.94  ? 129 TYR A CD2   1 
ATOM   982  C CE1   . TYR A 1 136 ? -2.889  -4.531  27.705  1.00 12.28  ? 129 TYR A CE1   1 
ATOM   983  C CE2   . TYR A 1 136 ? -4.803  -3.820  26.459  1.00 12.49  ? 129 TYR A CE2   1 
ATOM   984  C CZ    . TYR A 1 136 ? -3.881  -4.790  26.785  1.00 12.42  ? 129 TYR A CZ    1 
ATOM   985  O OH    . TYR A 1 136 ? -3.876  -5.987  26.143  1.00 14.90  ? 129 TYR A OH    1 
ATOM   986  N N     . GLN A 1 137 ? -3.124  0.697   26.107  1.00 10.65  ? 130 GLN A N     1 
ATOM   987  C CA    . GLN A 1 137 ? -3.244  0.726   24.630  1.00 10.60  ? 130 GLN A CA    1 
ATOM   988  C C     . GLN A 1 137 ? -1.940  1.271   24.049  1.00 10.08  ? 130 GLN A C     1 
ATOM   989  O O     . GLN A 1 137 ? -1.551  0.793   22.989  1.00 9.39   ? 130 GLN A O     1 
ATOM   990  C CB    . GLN A 1 137 ? -4.435  1.580   24.203  1.00 10.93  ? 130 GLN A CB    1 
ATOM   991  C CG    . GLN A 1 137 ? -5.778  0.950   24.525  1.00 10.96  ? 130 GLN A CG    1 
ATOM   992  C CD    . GLN A 1 137 ? -6.906  1.839   24.057  1.00 11.44  ? 130 GLN A CD    1 
ATOM   993  O OE1   . GLN A 1 137 ? -7.340  1.747   22.913  1.00 12.93  ? 130 GLN A OE1   1 
ATOM   994  N NE2   . GLN A 1 137 ? -7.332  2.759   24.910  1.00 10.57  ? 130 GLN A NE2   1 
ATOM   995  N N     . ILE A 1 138 ? -1.331  2.275   24.697  1.00 10.12  ? 131 ILE A N     1 
ATOM   996  C CA    . ILE A 1 138 ? -0.029  2.856   24.236  1.00 9.98   ? 131 ILE A CA    1 
ATOM   997  C C     . ILE A 1 138 ? 0.994   1.714   24.199  1.00 9.92   ? 131 ILE A C     1 
ATOM   998  O O     . ILE A 1 138 ? 1.653   1.591   23.194  1.00 10.09  ? 131 ILE A O     1 
ATOM   999  C CB    . ILE A 1 138 ? 0.485   3.998   25.133  1.00 9.43   ? 131 ILE A CB    1 
ATOM   1000 C CG1   . ILE A 1 138 ? -0.421  5.230   25.107  1.00 9.78   ? 131 ILE A CG1   1 
ATOM   1001 C CG2   . ILE A 1 138 ? 1.913   4.362   24.749  1.00 9.60   ? 131 ILE A CG2   1 
ATOM   1002 C CD1   . ILE A 1 138 ? -0.225  6.191   26.307  1.00 9.29   ? 131 ILE A CD1   1 
ATOM   1003 N N     . LEU A 1 139 ? 1.155   0.948   25.292  1.00 9.87   ? 132 LEU A N     1 
ATOM   1004 C CA    . LEU A 1 139 ? 2.170   -0.145  25.350  1.00 9.33   ? 132 LEU A CA    1 
ATOM   1005 C C     . LEU A 1 139 ? 1.762   -1.308  24.439  1.00 9.50   ? 132 LEU A C     1 
ATOM   1006 O O     . LEU A 1 139 ? 2.637   -1.949  23.843  1.00 8.54   ? 132 LEU A O     1 
ATOM   1007 C CB    . LEU A 1 139 ? 2.358   -0.597  26.783  1.00 9.51   ? 132 LEU A CB    1 
ATOM   1008 C CG    . LEU A 1 139 ? 2.927   0.455   27.713  1.00 9.85   ? 132 LEU A CG    1 
ATOM   1009 C CD1   . LEU A 1 139 ? 2.597   0.117   29.163  1.00 10.04  ? 132 LEU A CD1   1 
ATOM   1010 C CD2   . LEU A 1 139 ? 4.420   0.619   27.509  1.00 10.48  ? 132 LEU A CD2   1 
ATOM   1011 N N     . ARG A 1 140 ? 0.473   -1.524  24.210  1.00 10.48  ? 133 ARG A N     1 
ATOM   1012 C CA    . ARG A 1 140 ? 0.057   -2.640  23.310  1.00 10.57  ? 133 ARG A CA    1 
ATOM   1013 C C     . ARG A 1 140 ? 0.470   -2.286  21.885  1.00 10.03  ? 133 ARG A C     1 
ATOM   1014 O O     . ARG A 1 140 ? 0.950   -3.182  21.173  1.00 9.80   ? 133 ARG A O     1 
ATOM   1015 C CB    . ARG A 1 140 ? -1.433  -2.929  23.467  1.00 10.80  ? 133 ARG A CB    1 
ATOM   1016 C CG    . ARG A 1 140 ? -1.917  -4.153  22.716  1.00 10.61  ? 133 ARG A CG    1 
ATOM   1017 C CD    . ARG A 1 140 ? -3.408  -4.139  22.874  1.00 11.28  ? 133 ARG A CD    1 
ATOM   1018 N NE    . ARG A 1 140 ? -4.031  -5.286  22.259  1.00 11.56  ? 133 ARG A NE    1 
ATOM   1019 C CZ    . ARG A 1 140 ? -4.818  -5.205  21.219  1.00 12.25  ? 133 ARG A CZ    1 
ATOM   1020 N NH1   . ARG A 1 140 ? -5.090  -4.028  20.690  1.00 13.53  ? 133 ARG A NH1   1 
ATOM   1021 N NH2   . ARG A 1 140 ? -5.377  -6.287  20.737  1.00 13.44  ? 133 ARG A NH2   1 
ATOM   1022 N N     . GLY A 1 141 ? 0.317   -1.010  21.502  1.00 9.79   ? 134 GLY A N     1 
ATOM   1023 C CA    . GLY A 1 141 ? 0.730   -0.499  20.188  1.00 9.37   ? 134 GLY A CA    1 
ATOM   1024 C C     . GLY A 1 141 ? 2.246   -0.521  20.094  1.00 9.26   ? 134 GLY A C     1 
ATOM   1025 O O     . GLY A 1 141 ? 2.797   -1.036  19.071  1.00 8.43   ? 134 GLY A O     1 
ATOM   1026 N N     . LEU A 1 142 ? 2.906   -0.053  21.158  1.00 8.87   ? 135 LEU A N     1 
ATOM   1027 C CA    . LEU A 1 142 ? 4.384   0.003   21.172  1.00 9.18   ? 135 LEU A CA    1 
ATOM   1028 C C     . LEU A 1 142 ? 4.971   -1.406  21.153  1.00 8.58   ? 135 LEU A C     1 
ATOM   1029 O O     . LEU A 1 142 ? 6.006   -1.575  20.529  1.00 9.64   ? 135 LEU A O     1 
ATOM   1030 C CB    . LEU A 1 142 ? 4.916   0.847   22.324  1.00 9.03   ? 135 LEU A CB    1 
ATOM   1031 C CG    . LEU A 1 142 ? 6.409   1.149   22.227  1.00 9.03   ? 135 LEU A CG    1 
ATOM   1032 C CD1   . LEU A 1 142 ? 6.739   2.051   21.039  1.00 8.99   ? 135 LEU A CD1   1 
ATOM   1033 C CD2   . LEU A 1 142 ? 6.890   1.758   23.522  1.00 9.02   ? 135 LEU A CD2   1 
ATOM   1034 N N     . LYS A 1 143 ? 4.326   -2.403  21.741  1.00 9.24   ? 136 LYS A N     1 
ATOM   1035 C CA    . LYS A 1 143 ? 4.851   -3.793  21.689  1.00 8.92   ? 136 LYS A CA    1 
ATOM   1036 C C     . LYS A 1 143 ? 4.928   -4.231  20.216  1.00 9.82   ? 136 LYS A C     1 
ATOM   1037 O O     . LYS A 1 143 ? 5.978   -4.765  19.814  1.00 10.71  ? 136 LYS A O     1 
ATOM   1038 C CB    . LYS A 1 143 ? 4.020   -4.766  22.488  1.00 8.39   ? 136 LYS A CB    1 
ATOM   1039 C CG    . LYS A 1 143 ? 4.489   -6.205  22.401  1.00 8.27   ? 136 LYS A CG    1 
ATOM   1040 C CD    . LYS A 1 143 ? 3.501   -7.166  23.000  1.00 8.31   ? 136 LYS A CD    1 
ATOM   1041 C CE    . LYS A 1 143 ? 3.912   -8.621  22.794  1.00 8.40   ? 136 LYS A CE    1 
ATOM   1042 N NZ    . LYS A 1 143 ? 2.901   -9.554  23.346  1.00 8.29   ? 136 LYS A NZ    1 
ATOM   1043 N N     . TYR A 1 144 ? 3.895   -3.973  19.427  1.00 9.95   ? 137 TYR A N     1 
ATOM   1044 C CA    . TYR A 1 144 ? 3.875   -4.332  17.986  1.00 10.35  ? 137 TYR A CA    1 
ATOM   1045 C C     . TYR A 1 144 ? 5.004   -3.625  17.230  1.00 9.71   ? 137 TYR A C     1 
ATOM   1046 O O     . TYR A 1 144 ? 5.784   -4.281  16.441  1.00 9.42   ? 137 TYR A O     1 
ATOM   1047 C CB    . TYR A 1 144 ? 2.484   -4.010  17.442  1.00 10.71  ? 137 TYR A CB    1 
ATOM   1048 C CG    . TYR A 1 144 ? 2.282   -4.389  15.994  1.00 11.57  ? 137 TYR A CG    1 
ATOM   1049 C CD1   . TYR A 1 144 ? 1.909   -5.677  15.640  1.00 11.41  ? 137 TYR A CD1   1 
ATOM   1050 C CD2   . TYR A 1 144 ? 2.472   -3.466  14.984  1.00 11.37  ? 137 TYR A CD2   1 
ATOM   1051 C CE1   . TYR A 1 144 ? 1.653   -6.015  14.326  1.00 11.88  ? 137 TYR A CE1   1 
ATOM   1052 C CE2   . TYR A 1 144 ? 2.264   -3.811  13.647  1.00 11.93  ? 137 TYR A CE2   1 
ATOM   1053 C CZ    . TYR A 1 144 ? 1.866   -5.085  13.318  1.00 11.46  ? 137 TYR A CZ    1 
ATOM   1054 O OH    . TYR A 1 144 ? 1.616   -5.418  12.028  1.00 12.25  ? 137 TYR A OH    1 
ATOM   1055 N N     . ILE A 1 145 ? 5.068   -2.306  17.408  1.00 9.86   ? 138 ILE A N     1 
ATOM   1056 C CA    . ILE A 1 145 ? 6.091   -1.394  16.795  1.00 9.86   ? 138 ILE A CA    1 
ATOM   1057 C C     . ILE A 1 145 ? 7.476   -1.961  17.105  1.00 10.02  ? 138 ILE A C     1 
ATOM   1058 O O     . ILE A 1 145 ? 8.279   -2.250  16.172  1.00 9.90   ? 138 ILE A O     1 
ATOM   1059 C CB    . ILE A 1 145 ? 5.963   0.046   17.340  1.00 9.98   ? 138 ILE A CB    1 
ATOM   1060 C CG1   . ILE A 1 145 ? 4.582   0.659   17.088  1.00 9.98   ? 138 ILE A CG1   1 
ATOM   1061 C CG2   . ILE A 1 145 ? 7.050   0.927   16.757  1.00 10.18  ? 138 ILE A CG2   1 
ATOM   1062 C CD1   . ILE A 1 145 ? 4.394   2.047   17.672  1.00 10.03  ? 138 ILE A CD1   1 
ATOM   1063 N N     . HIS A 1 146 ? 7.784   -2.125  18.387  1.00 10.37  ? 139 HIS A N     1 
ATOM   1064 C CA    . HIS A 1 146 ? 9.120   -2.653  18.761  1.00 10.97  ? 139 HIS A CA    1 
ATOM   1065 C C     . HIS A 1 146 ? 9.331   -4.061  18.160  1.00 10.56  ? 139 HIS A C     1 
ATOM   1066 O O     . HIS A 1 146 ? 10.476  -4.369  17.804  1.00 9.56   ? 139 HIS A O     1 
ATOM   1067 C CB    . HIS A 1 146 ? 9.330   -2.591  20.274  1.00 10.96  ? 139 HIS A CB    1 
ATOM   1068 C CG    . HIS A 1 146 ? 9.576   -1.190  20.721  1.00 11.64  ? 139 HIS A CG    1 
ATOM   1069 N ND1   . HIS A 1 146 ? 9.747   -0.855  22.072  1.00 11.38  ? 139 HIS A ND1   1 
ATOM   1070 C CD2   . HIS A 1 146 ? 9.600   -0.028  20.028  1.00 11.42  ? 139 HIS A CD2   1 
ATOM   1071 C CE1   . HIS A 1 146 ? 9.952   0.439   22.158  1.00 11.36  ? 139 HIS A CE1   1 
ATOM   1072 N NE2   . HIS A 1 146 ? 9.860   0.970   20.925  1.00 11.14  ? 139 HIS A NE2   1 
ATOM   1073 N N     . SER A 1 147 ? 8.285   -4.870  18.001  1.00 10.17  ? 140 SER A N     1 
ATOM   1074 C CA    . SER A 1 147 ? 8.449   -6.251  17.473  1.00 11.38  ? 140 SER A CA    1 
ATOM   1075 C C     . SER A 1 147 ? 8.806   -6.161  15.972  1.00 12.13  ? 140 SER A C     1 
ATOM   1076 O O     . SER A 1 147 ? 9.410   -7.060  15.457  1.00 11.67  ? 140 SER A O     1 
ATOM   1077 C CB    . SER A 1 147 ? 7.231   -7.092  17.737  1.00 11.18  ? 140 SER A CB    1 
ATOM   1078 O OG    . SER A 1 147 ? 6.163   -6.665  16.898  1.00 11.86  ? 140 SER A OG    1 
ATOM   1079 N N     . ALA A 1 148 ? 8.500   -5.050  15.316  1.00 12.83  ? 141 ALA A N     1 
ATOM   1080 C CA    . ALA A 1 148 ? 8.802   -4.815  13.889  1.00 13.45  ? 141 ALA A CA    1 
ATOM   1081 C C     . ALA A 1 148 ? 10.250  -4.301  13.749  1.00 13.94  ? 141 ALA A C     1 
ATOM   1082 O O     . ALA A 1 148 ? 10.623  -3.987  12.633  1.00 14.06  ? 141 ALA A O     1 
ATOM   1083 C CB    . ALA A 1 148 ? 7.789   -3.833  13.344  1.00 13.40  ? 141 ALA A CB    1 
ATOM   1084 N N     . ASN A 1 149 ? 11.015  -4.232  14.848  1.00 14.62  ? 142 ASN A N     1 
ATOM   1085 C CA    . ASN A 1 149 ? 12.385  -3.642  14.963  1.00 16.51  ? 142 ASN A CA    1 
ATOM   1086 C C     . ASN A 1 149 ? 12.354  -2.151  14.593  1.00 16.04  ? 142 ASN A C     1 
ATOM   1087 O O     . ASN A 1 149 ? 13.333  -1.606  14.077  1.00 16.54  ? 142 ASN A O     1 
ATOM   1088 C CB    . ASN A 1 149 ? 13.445  -4.386  14.134  1.00 18.81  ? 142 ASN A CB    1 
ATOM   1089 C CG    . ASN A 1 149 ? 14.846  -4.192  14.696  1.00 21.70  ? 142 ASN A CG    1 
ATOM   1090 O OD1   . ASN A 1 149 ? 15.057  -4.319  15.907  1.00 24.10  ? 142 ASN A OD1   1 
ATOM   1091 N ND2   . ASN A 1 149 ? 15.813  -3.882  13.842  1.00 24.01  ? 142 ASN A ND2   1 
ATOM   1092 N N     . VAL A 1 150 ? 11.224  -1.510  14.790  1.00 15.78  ? 143 VAL A N     1 
ATOM   1093 C CA    . VAL A 1 150 ? 11.057  -0.060  14.513  1.00 15.46  ? 143 VAL A CA    1 
ATOM   1094 C C     . VAL A 1 150 ? 11.082  0.696   15.844  1.00 15.06  ? 143 VAL A C     1 
ATOM   1095 O O     . VAL A 1 150 ? 10.562  0.163   16.838  1.00 14.45  ? 143 VAL A O     1 
ATOM   1096 C CB    . VAL A 1 150 ? 9.735   0.139   13.763  1.00 15.11  ? 143 VAL A CB    1 
ATOM   1097 C CG1   . VAL A 1 150 ? 9.259   1.579   13.788  1.00 15.56  ? 143 VAL A CG1   1 
ATOM   1098 C CG2   . VAL A 1 150 ? 9.853   -0.399  12.344  1.00 14.58  ? 143 VAL A CG2   1 
ATOM   1099 N N     . LEU A 1 151 ? 11.603  1.914   15.835  1.00 13.97  ? 144 LEU A N     1 
ATOM   1100 C CA    . LEU A 1 151 ? 11.528  2.867   16.967  1.00 15.62  ? 144 LEU A CA    1 
ATOM   1101 C C     . LEU A 1 151 ? 10.696  4.036   16.501  1.00 14.52  ? 144 LEU A C     1 
ATOM   1102 O O     . LEU A 1 151 ? 11.048  4.535   15.464  1.00 15.63  ? 144 LEU A O     1 
ATOM   1103 C CB    . LEU A 1 151 ? 12.931  3.355   17.341  1.00 16.52  ? 144 LEU A CB    1 
ATOM   1104 C CG    . LEU A 1 151 ? 13.974  2.249   17.452  1.00 17.89  ? 144 LEU A CG    1 
ATOM   1105 C CD1   . LEU A 1 151 ? 15.381  2.825   17.545  1.00 19.71  ? 144 LEU A CD1   1 
ATOM   1106 C CD2   . LEU A 1 151 ? 13.692  1.392   18.660  1.00 18.30  ? 144 LEU A CD2   1 
ATOM   1107 N N     . HIS A 1 152 ? 9.662   4.427   17.246  1.00 12.68  ? 145 HIS A N     1 
ATOM   1108 C CA    . HIS A 1 152 ? 8.790   5.573   16.903  1.00 12.81  ? 145 HIS A CA    1 
ATOM   1109 C C     . HIS A 1 152 ? 9.588   6.892   17.020  1.00 12.77  ? 145 HIS A C     1 
ATOM   1110 O O     . HIS A 1 152 ? 9.628   7.652   16.041  1.00 12.24  ? 145 HIS A O     1 
ATOM   1111 C CB    . HIS A 1 152 ? 7.515   5.500   17.768  1.00 12.88  ? 145 HIS A CB    1 
ATOM   1112 C CG    . HIS A 1 152 ? 6.528   6.568   17.450  1.00 12.22  ? 145 HIS A CG    1 
ATOM   1113 N ND1   . HIS A 1 152 ? 6.768   7.893   17.757  1.00 11.63  ? 145 HIS A ND1   1 
ATOM   1114 C CD2   . HIS A 1 152 ? 5.326   6.526   16.847  1.00 12.34  ? 145 HIS A CD2   1 
ATOM   1115 C CE1   . HIS A 1 152 ? 5.737   8.613   17.368  1.00 11.73  ? 145 HIS A CE1   1 
ATOM   1116 N NE2   . HIS A 1 152 ? 4.854   7.812   16.767  1.00 11.40  ? 145 HIS A NE2   1 
ATOM   1117 N N     . ARG A 1 153 ? 10.188  7.135   18.186  1.00 13.45  ? 146 ARG A N     1 
ATOM   1118 C CA    . ARG A 1 153 ? 11.139  8.226   18.503  1.00 14.50  ? 146 ARG A CA    1 
ATOM   1119 C C     . ARG A 1 153 ? 10.449  9.594   18.600  1.00 15.17  ? 146 ARG A C     1 
ATOM   1120 O O     . ARG A 1 153 ? 11.193  10.582  18.842  1.00 13.41  ? 146 ARG A O     1 
ATOM   1121 C CB    . ARG A 1 153 ? 12.282  8.284   17.478  1.00 16.37  ? 146 ARG A CB    1 
ATOM   1122 C CG    . ARG A 1 153 ? 13.054  6.974   17.334  1.00 16.62  ? 146 ARG A CG    1 
ATOM   1123 C CD    . ARG A 1 153 ? 13.928  7.016   16.099  1.00 17.41  ? 146 ARG A CD    1 
ATOM   1124 N NE    . ARG A 1 153 ? 15.163  7.748   16.277  1.00 19.71  ? 146 ARG A NE    1 
ATOM   1125 C CZ    . ARG A 1 153 ? 15.532  8.844   15.606  1.00 22.63  ? 146 ARG A CZ    1 
ATOM   1126 N NH1   . ARG A 1 153 ? 14.728  9.383   14.710  1.00 25.28  ? 146 ARG A NH1   1 
ATOM   1127 N NH2   . ARG A 1 153 ? 16.703  9.413   15.842  1.00 22.77  ? 146 ARG A NH2   1 
ATOM   1128 N N     . ASP A 1 154 ? 9.116   9.693   18.462  1.00 15.93  ? 147 ASP A N     1 
ATOM   1129 C CA    . ASP A 1 154 ? 8.411   10.979  18.739  1.00 17.34  ? 147 ASP A CA    1 
ATOM   1130 C C     . ASP A 1 154 ? 7.108   10.742  19.502  1.00 17.09  ? 147 ASP A C     1 
ATOM   1131 O O     . ASP A 1 154 ? 6.162   11.481  19.289  1.00 18.13  ? 147 ASP A O     1 
ATOM   1132 C CB    . ASP A 1 154 ? 8.144   11.790  17.470  1.00 17.23  ? 147 ASP A CB    1 
ATOM   1133 C CG    . ASP A 1 154 ? 7.897   13.279  17.699  1.00 18.24  ? 147 ASP A CG    1 
ATOM   1134 O OD1   . ASP A 1 154 ? 8.322   13.806  18.753  1.00 15.77  ? 147 ASP A OD1   1 
ATOM   1135 O OD2   . ASP A 1 154 ? 7.324   13.922  16.775  1.00 20.46  ? 147 ASP A OD2   1 
ATOM   1136 N N     . LEU A 1 155 ? 7.080   9.784   20.410  1.00 16.98  ? 148 LEU A N     1 
ATOM   1137 C CA    . LEU A 1 155 ? 5.890   9.541   21.246  1.00 15.83  ? 148 LEU A CA    1 
ATOM   1138 C C     . LEU A 1 155 ? 5.673   10.760  22.145  1.00 15.59  ? 148 LEU A C     1 
ATOM   1139 O O     . LEU A 1 155 ? 6.589   11.143  22.879  1.00 16.17  ? 148 LEU A O     1 
ATOM   1140 C CB    . LEU A 1 155 ? 6.075   8.255   22.046  1.00 15.43  ? 148 LEU A CB    1 
ATOM   1141 C CG    . LEU A 1 155 ? 6.120   6.986   21.205  1.00 15.78  ? 148 LEU A CG    1 
ATOM   1142 C CD1   . LEU A 1 155 ? 6.401   5.771   22.072  1.00 15.49  ? 148 LEU A CD1   1 
ATOM   1143 C CD2   . LEU A 1 155 ? 4.834   6.801   20.416  1.00 15.96  ? 148 LEU A CD2   1 
ATOM   1144 N N     . LYS A 1 156 ? 4.508   11.383  22.019  1.00 15.45  ? 149 LYS A N     1 
ATOM   1145 C CA    . LYS A 1 156 ? 4.052   12.526  22.857  1.00 16.48  ? 149 LYS A CA    1 
ATOM   1146 C C     . LYS A 1 156 ? 2.533   12.587  22.709  1.00 16.72  ? 149 LYS A C     1 
ATOM   1147 O O     . LYS A 1 156 ? 1.974   11.975  21.785  1.00 17.47  ? 149 LYS A O     1 
ATOM   1148 C CB    . LYS A 1 156 ? 4.723   13.832  22.437  1.00 16.76  ? 149 LYS A CB    1 
ATOM   1149 C CG    . LYS A 1 156 ? 4.430   14.260  21.016  1.00 17.53  ? 149 LYS A CG    1 
ATOM   1150 C CD    . LYS A 1 156 ? 5.015   15.602  20.641  1.00 20.65  ? 149 LYS A CD    1 
ATOM   1151 C CE    . LYS A 1 156 ? 5.158   15.743  19.133  1.00 25.15  ? 149 LYS A CE    1 
ATOM   1152 N NZ    . LYS A 1 156 ? 5.383   17.157  18.711  1.00 29.98  ? 149 LYS A NZ    1 
ATOM   1153 N N     . PRO A 1 157 ? 1.828   13.273  23.630  1.00 15.99  ? 150 PRO A N     1 
ATOM   1154 C CA    . PRO A 1 157 ? 0.363   13.268  23.638  1.00 16.24  ? 150 PRO A CA    1 
ATOM   1155 C C     . PRO A 1 157 ? -0.319  13.589  22.295  1.00 15.88  ? 150 PRO A C     1 
ATOM   1156 O O     . PRO A 1 157 ? -1.219  12.885  21.938  1.00 15.51  ? 150 PRO A O     1 
ATOM   1157 C CB    . PRO A 1 157 ? 0.043   14.298  24.729  1.00 15.86  ? 150 PRO A CB    1 
ATOM   1158 C CG    . PRO A 1 157 ? 1.200   14.168  25.692  1.00 15.95  ? 150 PRO A CG    1 
ATOM   1159 C CD    . PRO A 1 157 ? 2.403   13.984  24.784  1.00 16.13  ? 150 PRO A CD    1 
ATOM   1160 N N     . SER A 1 158 ? 0.148   14.582  21.541  1.00 16.73  ? 151 SER A N     1 
ATOM   1161 C CA    . SER A 1 158 ? -0.452  14.953  20.227  1.00 17.02  ? 151 SER A CA    1 
ATOM   1162 C C     . SER A 1 158 ? -0.318  13.791  19.226  1.00 16.28  ? 151 SER A C     1 
ATOM   1163 O O     . SER A 1 158 ? -1.110  13.760  18.286  1.00 15.62  ? 151 SER A O     1 
ATOM   1164 C CB    . SER A 1 158 ? 0.138   16.217  19.683  1.00 16.42  ? 151 SER A CB    1 
ATOM   1165 O OG    . SER A 1 158 ? 1.525   16.107  19.690  1.00 17.57  ? 151 SER A OG    1 
ATOM   1166 N N     . ASN A 1 159 ? 0.561   12.812  19.480  1.00 15.17  ? 152 ASN A N     1 
ATOM   1167 C CA    . ASN A 1 159 ? 0.794   11.677  18.555  1.00 15.22  ? 152 ASN A CA    1 
ATOM   1168 C C     . ASN A 1 159 ? -0.048  10.487  19.025  1.00 15.01  ? 152 ASN A C     1 
ATOM   1169 O O     . ASN A 1 159 ? -0.002  9.427   18.386  1.00 16.24  ? 152 ASN A O     1 
ATOM   1170 C CB    . ASN A 1 159 ? 2.294   11.413  18.372  1.00 14.75  ? 152 ASN A CB    1 
ATOM   1171 C CG    . ASN A 1 159 ? 2.988   12.466  17.506  1.00 16.54  ? 152 ASN A CG    1 
ATOM   1172 O OD1   . ASN A 1 159 ? 4.209   12.653  17.590  1.00 15.47  ? 152 ASN A OD1   1 
ATOM   1173 N ND2   . ASN A 1 159 ? 2.246   13.119  16.618  1.00 14.81  ? 152 ASN A ND2   1 
ATOM   1174 N N     . LEU A 1 160 ? -0.824  10.650  20.095  1.00 14.94  ? 153 LEU A N     1 
ATOM   1175 C CA    . LEU A 1 160 ? -1.776  9.607   20.532  1.00 14.34  ? 153 LEU A CA    1 
ATOM   1176 C C     . LEU A 1 160 ? -3.183  10.113  20.251  1.00 14.62  ? 153 LEU A C     1 
ATOM   1177 O O     . LEU A 1 160 ? -3.654  10.998  20.963  1.00 19.00  ? 153 LEU A O     1 
ATOM   1178 C CB    . LEU A 1 160 ? -1.527  9.273   22.011  1.00 14.48  ? 153 LEU A CB    1 
ATOM   1179 C CG    . LEU A 1 160 ? -0.086  8.918   22.383  1.00 14.38  ? 153 LEU A CG    1 
ATOM   1180 C CD1   . LEU A 1 160 ? 0.061   8.702   23.886  1.00 14.21  ? 153 LEU A CD1   1 
ATOM   1181 C CD2   . LEU A 1 160 ? 0.415   7.683   21.626  1.00 14.73  ? 153 LEU A CD2   1 
ATOM   1182 N N     . LEU A 1 161 ? -3.845  9.557   19.252  1.00 15.44  ? 154 LEU A N     1 
ATOM   1183 C CA    . LEU A 1 161 ? -5.239  9.916   18.893  1.00 16.68  ? 154 LEU A CA    1 
ATOM   1184 C C     . LEU A 1 161 ? -6.235  9.018   19.633  1.00 16.58  ? 154 LEU A C     1 
ATOM   1185 O O     . LEU A 1 161 ? -5.917  7.836   19.871  1.00 13.87  ? 154 LEU A O     1 
ATOM   1186 C CB    . LEU A 1 161 ? -5.474  9.725   17.399  1.00 17.68  ? 154 LEU A CB    1 
ATOM   1187 C CG    . LEU A 1 161 ? -4.448  10.372  16.483  1.00 19.12  ? 154 LEU A CG    1 
ATOM   1188 C CD1   . LEU A 1 161 ? -4.568  9.785   15.091  1.00 20.32  ? 154 LEU A CD1   1 
ATOM   1189 C CD2   . LEU A 1 161 ? -4.626  11.878  16.470  1.00 19.66  ? 154 LEU A CD2   1 
ATOM   1190 N N     . LEU A 1 162 ? -7.400  9.601   19.927  1.00 17.48  ? 155 LEU A N     1 
ATOM   1191 C CA    . LEU A 1 162 ? -8.553  9.007   20.644  1.00 19.75  ? 155 LEU A CA    1 
ATOM   1192 C C     . LEU A 1 162 ? -9.842  9.297   19.879  1.00 21.05  ? 155 LEU A C     1 
ATOM   1193 O O     . LEU A 1 162 ? -9.923  10.362  19.272  1.00 18.97  ? 155 LEU A O     1 
ATOM   1194 C CB    . LEU A 1 162 ? -8.615  9.644   22.025  1.00 21.77  ? 155 LEU A CB    1 
ATOM   1195 C CG    . LEU A 1 162 ? -7.397  9.367   22.895  1.00 22.55  ? 155 LEU A CG    1 
ATOM   1196 C CD1   . LEU A 1 162 ? -7.043  10.609  23.711  1.00 23.47  ? 155 LEU A CD1   1 
ATOM   1197 C CD2   . LEU A 1 162 ? -7.667  8.155   23.778  1.00 23.42  ? 155 LEU A CD2   1 
ATOM   1198 N N     . ASN A 1 163 ? -10.786 8.358   19.911  1.00 25.03  ? 156 ASN A N     1 
ATOM   1199 C CA    . ASN A 1 163 ? -12.161 8.529   19.371  1.00 28.19  ? 156 ASN A CA    1 
ATOM   1200 C C     . ASN A 1 163 ? -13.096 8.691   20.579  1.00 29.16  ? 156 ASN A C     1 
ATOM   1201 O O     . ASN A 1 163 ? -12.579 8.703   21.715  1.00 31.26  ? 156 ASN A O     1 
ATOM   1202 C CB    . ASN A 1 163 ? -12.500 7.404   18.390  1.00 26.56  ? 156 ASN A CB    1 
ATOM   1203 C CG    . ASN A 1 163 ? -12.514 6.040   19.029  1.00 26.94  ? 156 ASN A CG    1 
ATOM   1204 O OD1   . ASN A 1 163 ? -12.345 5.898   20.239  1.00 27.55  ? 156 ASN A OD1   1 
ATOM   1205 N ND2   . ASN A 1 163 ? -12.729 5.023   18.217  1.00 27.36  ? 156 ASN A ND2   1 
ATOM   1206 N N     . THR A 1 164 ? -14.406 8.861   20.367  1.00 31.49  ? 157 THR A N     1 
ATOM   1207 C CA    . THR A 1 164 ? -15.347 9.224   21.463  1.00 30.31  ? 157 THR A CA    1 
ATOM   1208 C C     . THR A 1 164 ? -15.520 8.049   22.430  1.00 27.81  ? 157 THR A C     1 
ATOM   1209 O O     . THR A 1 164 ? -16.041 8.299   23.511  1.00 26.54  ? 157 THR A O     1 
ATOM   1210 C CB    . THR A 1 164 ? -16.717 9.699   20.964  1.00 31.47  ? 157 THR A CB    1 
ATOM   1211 O OG1   . THR A 1 164 ? -17.200 8.722   20.048  1.00 34.42  ? 157 THR A OG1   1 
ATOM   1212 C CG2   . THR A 1 164 ? -16.670 11.068  20.333  1.00 31.60  ? 157 THR A CG2   1 
ATOM   1213 N N     . THR A 1 165 ? -15.081 6.837   22.059  1.00 27.04  ? 158 THR A N     1 
ATOM   1214 C CA    . THR A 1 165 ? -15.144 5.620   22.910  1.00 26.51  ? 158 THR A CA    1 
ATOM   1215 C C     . THR A 1 165 ? -13.729 5.273   23.407  1.00 26.86  ? 158 THR A C     1 
ATOM   1216 O O     . THR A 1 165 ? -13.481 4.080   23.725  1.00 30.63  ? 158 THR A O     1 
ATOM   1217 C CB    . THR A 1 165 ? -15.770 4.425   22.177  1.00 24.57  ? 158 THR A CB    1 
ATOM   1218 O OG1   . THR A 1 165 ? -14.848 3.982   21.189  1.00 26.15  ? 158 THR A OG1   1 
ATOM   1219 C CG2   . THR A 1 165 ? -17.088 4.747   21.520  1.00 25.13  ? 158 THR A CG2   1 
ATOM   1220 N N     . CYS A 1 166 ? -12.816 6.242   23.438  1.00 22.99  ? 159 CYS A N     1 
ATOM   1221 C CA    . CYS A 1 166 ? -11.519 6.110   24.151  1.00 23.16  ? 159 CYS A CA    1 
ATOM   1222 C C     . CYS A 1 166 ? -10.659 4.977   23.526  1.00 20.99  ? 159 CYS A C     1 
ATOM   1223 O O     . CYS A 1 166 ? -9.735  4.515   24.207  1.00 20.56  ? 159 CYS A O     1 
ATOM   1224 C CB    . CYS A 1 166 ? -11.792 5.967   25.656  1.00 24.66  ? 159 CYS A CB    1 
ATOM   1225 S SG    . CYS A 1 166 ? -12.445 7.488   26.426  1.00 30.28  ? 159 CYS A SG    1 
ATOM   1226 N N     . ASP A 1 167 ? -10.852 4.602   22.249  1.00 18.11  ? 160 ASP A N     1 
ATOM   1227 C CA    . ASP A 1 167 ? -9.885  3.737   21.520  1.00 19.25  ? 160 ASP A CA    1 
ATOM   1228 C C     . ASP A 1 167 ? -8.686  4.618   21.175  1.00 17.69  ? 160 ASP A C     1 
ATOM   1229 O O     . ASP A 1 167 ? -8.909  5.755   20.658  1.00 17.48  ? 160 ASP A O     1 
ATOM   1230 C CB    . ASP A 1 167 ? -10.412 3.141   20.207  1.00 21.40  ? 160 ASP A CB    1 
ATOM   1231 C CG    . ASP A 1 167 ? -11.615 2.216   20.332  1.00 24.31  ? 160 ASP A CG    1 
ATOM   1232 O OD1   . ASP A 1 167 ? -11.617 1.360   21.253  1.00 23.31  ? 160 ASP A OD1   1 
ATOM   1233 O OD2   . ASP A 1 167 ? -12.562 2.388   19.512  1.00 26.00  ? 160 ASP A OD2   1 
ATOM   1234 N N     . LEU A 1 168 ? -7.471  4.144   21.425  1.00 14.79  ? 161 LEU A N     1 
ATOM   1235 C CA    . LEU A 1 168 ? -6.266  5.020   21.305  1.00 15.14  ? 161 LEU A CA    1 
ATOM   1236 C C     . LEU A 1 168 ? -5.406  4.470   20.167  1.00 14.16  ? 161 LEU A C     1 
ATOM   1237 O O     . LEU A 1 168 ? -5.259  3.249   20.060  1.00 15.89  ? 161 LEU A O     1 
ATOM   1238 C CB    . LEU A 1 168 ? -5.551  5.137   22.667  1.00 14.44  ? 161 LEU A CB    1 
ATOM   1239 C CG    . LEU A 1 168 ? -4.175  5.816   22.682  1.00 14.13  ? 161 LEU A CG    1 
ATOM   1240 C CD1   . LEU A 1 168 ? -3.769  6.212   24.079  1.00 12.91  ? 161 LEU A CD1   1 
ATOM   1241 C CD2   . LEU A 1 168 ? -3.095  4.905   22.081  1.00 13.55  ? 161 LEU A CD2   1 
ATOM   1242 N N     . LYS A 1 169 ? -4.958  5.333   19.275  1.00 14.52  ? 162 LYS A N     1 
ATOM   1243 C CA    . LYS A 1 169 ? -4.161  4.936   18.090  1.00 14.69  ? 162 LYS A CA    1 
ATOM   1244 C C     . LYS A 1 169 ? -2.916  5.820   18.032  1.00 14.44  ? 162 LYS A C     1 
ATOM   1245 O O     . LYS A 1 169 ? -3.063  7.036   18.131  1.00 12.75  ? 162 LYS A O     1 
ATOM   1246 C CB    . LYS A 1 169 ? -5.010  5.044   16.823  1.00 16.23  ? 162 LYS A CB    1 
ATOM   1247 C CG    . LYS A 1 169 ? -6.048  3.929   16.611  1.00 17.10  ? 162 LYS A CG    1 
ATOM   1248 C CD    . LYS A 1 169 ? -6.837  4.139   15.317  1.00 18.37  ? 162 LYS A CD    1 
ATOM   1249 C CE    . LYS A 1 169 ? -7.921  3.124   15.003  1.00 19.00  ? 162 LYS A CE    1 
ATOM   1250 N NZ    . LYS A 1 169 ? -7.467  1.755   15.317  1.00 19.92  ? 162 LYS A NZ    1 
ATOM   1251 N N     . ILE A 1 170 ? -1.741  5.203   17.886  1.00 13.89  ? 163 ILE A N     1 
ATOM   1252 C CA    . ILE A 1 170 ? -0.436  5.911   17.789  1.00 14.62  ? 163 ILE A CA    1 
ATOM   1253 C C     . ILE A 1 170 ? -0.287  6.390   16.349  1.00 14.43  ? 163 ILE A C     1 
ATOM   1254 O O     . ILE A 1 170 ? -0.568  5.606   15.502  1.00 13.27  ? 163 ILE A O     1 
ATOM   1255 C CB    . ILE A 1 170 ? 0.701   4.952   18.168  1.00 14.44  ? 163 ILE A CB    1 
ATOM   1256 C CG1   . ILE A 1 170 ? 0.564   4.516   19.621  1.00 13.61  ? 163 ILE A CG1   1 
ATOM   1257 C CG2   . ILE A 1 170 ? 2.071   5.567   17.853  1.00 13.67  ? 163 ILE A CG2   1 
ATOM   1258 C CD1   . ILE A 1 170 ? 1.659   3.613   20.066  1.00 14.86  ? 163 ILE A CD1   1 
ATOM   1259 N N     . CYS A 1 171 ? 0.083   7.639   16.113  1.00 16.38  ? 164 CYS A N     1 
ATOM   1260 C CA    . CYS A 1 171 ? 0.357   8.179   14.748  1.00 18.27  ? 164 CYS A CA    1 
ATOM   1261 C C     . CYS A 1 171 ? 1.715   8.901   14.696  1.00 17.63  ? 164 CYS A C     1 
ATOM   1262 O O     . CYS A 1 171 ? 2.479   8.795   15.652  1.00 16.64  ? 164 CYS A O     1 
ATOM   1263 C CB    . CYS A 1 171 ? -0.771  9.102   14.302  1.00 18.28  ? 164 CYS A CB    1 
ATOM   1264 S SG    . CYS A 1 171 ? -0.805  10.632  15.258  1.00 20.26  ? 164 CYS A SG    1 
ATOM   1265 N N     . ASP A 1 172 ? 2.035   9.507   13.545  1.00 20.98  ? 165 ASP A N     1 
ATOM   1266 C CA    . ASP A 1 172 ? 3.243   10.347  13.259  1.00 20.59  ? 165 ASP A CA    1 
ATOM   1267 C C     . ASP A 1 172 ? 4.547   9.539   13.383  1.00 17.75  ? 165 ASP A C     1 
ATOM   1268 O O     . ASP A 1 172 ? 5.362   9.833   14.264  1.00 18.51  ? 165 ASP A O     1 
ATOM   1269 C CB    . ASP A 1 172 ? 3.294   11.597  14.136  1.00 24.44  ? 165 ASP A CB    1 
ATOM   1270 C CG    . ASP A 1 172 ? 4.435   12.525  13.736  1.00 30.62  ? 165 ASP A CG    1 
ATOM   1271 O OD1   . ASP A 1 172 ? 5.065   12.265  12.665  1.00 35.91  ? 165 ASP A OD1   1 
ATOM   1272 O OD2   . ASP A 1 172 ? 4.720   13.489  14.497  1.00 34.26  ? 165 ASP A OD2   1 
ATOM   1273 N N     . PHE A 1 173 ? 4.781   8.627   12.447  1.00 16.56  ? 166 PHE A N     1 
ATOM   1274 C CA    . PHE A 1 173 ? 6.021   7.823   12.293  1.00 15.83  ? 166 PHE A CA    1 
ATOM   1275 C C     . PHE A 1 173 ? 7.031   8.547   11.394  1.00 16.54  ? 166 PHE A C     1 
ATOM   1276 O O     . PHE A 1 173 ? 7.868   7.890   10.816  1.00 15.75  ? 166 PHE A O     1 
ATOM   1277 C CB    . PHE A 1 173 ? 5.662   6.435   11.768  1.00 14.99  ? 166 PHE A CB    1 
ATOM   1278 C CG    . PHE A 1 173 ? 4.940   5.566   12.764  1.00 16.02  ? 166 PHE A CG    1 
ATOM   1279 C CD1   . PHE A 1 173 ? 3.594   5.763   13.048  1.00 15.27  ? 166 PHE A CD1   1 
ATOM   1280 C CD2   . PHE A 1 173 ? 5.608   4.543   13.434  1.00 16.03  ? 166 PHE A CD2   1 
ATOM   1281 C CE1   . PHE A 1 173 ? 2.941   4.974   13.994  1.00 14.81  ? 166 PHE A CE1   1 
ATOM   1282 C CE2   . PHE A 1 173 ? 4.949   3.759   14.373  1.00 14.38  ? 166 PHE A CE2   1 
ATOM   1283 C CZ    . PHE A 1 173 ? 3.621   3.984   14.662  1.00 14.38  ? 166 PHE A CZ    1 
ATOM   1284 N N     . GLY A 1 174 ? 7.023   9.877   11.354  1.00 19.30  ? 167 GLY A N     1 
ATOM   1285 C CA    . GLY A 1 174 ? 7.940   10.640  10.479  1.00 21.11  ? 167 GLY A CA    1 
ATOM   1286 C C     . GLY A 1 174 ? 9.388   10.497  10.923  1.00 23.22  ? 167 GLY A C     1 
ATOM   1287 O O     . GLY A 1 174 ? 10.288  10.394  10.037  1.00 24.45  ? 167 GLY A O     1 
ATOM   1288 N N     . LEU A 1 175 ? 9.627   10.473  12.242  1.00 22.06  ? 168 LEU A N     1 
ATOM   1289 C CA    . LEU A 1 175 ? 10.991  10.386  12.813  1.00 22.21  ? 168 LEU A CA    1 
ATOM   1290 C C     . LEU A 1 175 ? 11.363  8.935   13.165  1.00 20.04  ? 168 LEU A C     1 
ATOM   1291 O O     . LEU A 1 175 ? 12.391  8.767   13.799  1.00 21.23  ? 168 LEU A O     1 
ATOM   1292 C CB    . LEU A 1 175 ? 11.026  11.292  14.047  1.00 25.67  ? 168 LEU A CB    1 
ATOM   1293 C CG    . LEU A 1 175 ? 10.533  12.725  13.830  1.00 29.20  ? 168 LEU A CG    1 
ATOM   1294 C CD1   . LEU A 1 175 ? 10.979  13.620  14.978  1.00 30.51  ? 168 LEU A CD1   1 
ATOM   1295 C CD2   . LEU A 1 175 ? 11.041  13.295  12.522  1.00 30.47  ? 168 LEU A CD2   1 
ATOM   1296 N N     . ALA A 1 176 ? 10.551  7.933   12.830  1.00 18.14  ? 169 ALA A N     1 
ATOM   1297 C CA    . ALA A 1 176 ? 10.801  6.511   13.177  1.00 18.44  ? 169 ALA A CA    1 
ATOM   1298 C C     . ALA A 1 176 ? 12.031  5.976   12.441  1.00 19.73  ? 169 ALA A C     1 
ATOM   1299 O O     . ALA A 1 176 ? 12.147  6.254   11.240  1.00 19.24  ? 169 ALA A O     1 
ATOM   1300 C CB    . ALA A 1 176 ? 9.605   5.661   12.847  1.00 16.59  ? 169 ALA A CB    1 
ATOM   1301 N N     . ARG A 1 177 ? 12.831  5.132   13.112  1.00 20.31  ? 170 ARG A N     1 
ATOM   1302 C CA    . ARG A 1 177 ? 14.012  4.452   12.524  1.00 21.99  ? 170 ARG A CA    1 
ATOM   1303 C C     . ARG A 1 177 ? 13.898  2.952   12.758  1.00 20.27  ? 170 ARG A C     1 
ATOM   1304 O O     . ARG A 1 177 ? 13.170  2.571   13.653  1.00 14.56  ? 170 ARG A O     1 
ATOM   1305 C CB    . ARG A 1 177 ? 15.314  4.925   13.178  1.00 25.12  ? 170 ARG A CB    1 
ATOM   1306 C CG    . ARG A 1 177 ? 15.636  6.387   12.927  1.00 29.99  ? 170 ARG A CG    1 
ATOM   1307 C CD    . ARG A 1 177 ? 16.302  6.610   11.582  1.00 37.77  ? 170 ARG A CD    1 
ATOM   1308 N NE    . ARG A 1 177 ? 16.628  8.016   11.388  1.00 43.66  ? 170 ARG A NE    1 
ATOM   1309 C CZ    . ARG A 1 177 ? 15.750  8.978   11.104  1.00 46.35  ? 170 ARG A CZ    1 
ATOM   1310 N NH1   . ARG A 1 177 ? 14.457  8.700   10.963  1.00 42.88  ? 170 ARG A NH1   1 
ATOM   1311 N NH2   . ARG A 1 177 ? 16.186  10.224  10.971  1.00 46.60  ? 170 ARG A NH2   1 
ATOM   1312 N N     . VAL A 1 178 ? 14.672  2.161   12.009  1.00 20.05  ? 171 VAL A N     1 
ATOM   1313 C CA    . VAL A 1 178 ? 14.950  0.745   12.373  1.00 21.96  ? 171 VAL A CA    1 
ATOM   1314 C C     . VAL A 1 178 ? 15.862  0.756   13.601  1.00 20.45  ? 171 VAL A C     1 
ATOM   1315 O O     . VAL A 1 178 ? 16.780  1.557   13.612  1.00 20.98  ? 171 VAL A O     1 
ATOM   1316 C CB    . VAL A 1 178 ? 15.528  -0.044  11.180  1.00 22.82  ? 171 VAL A CB    1 
ATOM   1317 C CG1   . VAL A 1 178 ? 15.762  -1.504  11.525  1.00 23.06  ? 171 VAL A CG1   1 
ATOM   1318 C CG2   . VAL A 1 178 ? 14.616  0.061   9.959   1.00 22.84  ? 171 VAL A CG2   1 
ATOM   1319 N N     . ALA A 1 179 ? 15.557  -0.022  14.646  1.00 21.00  ? 172 ALA A N     1 
ATOM   1320 C CA    . ALA A 1 179 ? 16.471  -0.208  15.799  1.00 21.59  ? 172 ALA A CA    1 
ATOM   1321 C C     . ALA A 1 179 ? 17.886  -0.534  15.289  1.00 23.50  ? 172 ALA A C     1 
ATOM   1322 O O     . ALA A 1 179 ? 18.046  -1.256  14.272  1.00 20.32  ? 172 ALA A O     1 
ATOM   1323 C CB    . ALA A 1 179 ? 15.979  -1.271  16.736  1.00 21.33  ? 172 ALA A CB    1 
ATOM   1324 N N     . ASP A 1 180 ? 18.895  0.055   15.928  1.00 27.08  ? 173 ASP A N     1 
ATOM   1325 C CA    . ASP A 1 180 ? 20.323  -0.105  15.539  1.00 27.82  ? 173 ASP A CA    1 
ATOM   1326 C C     . ASP A 1 180 ? 21.143  0.195   16.780  1.00 30.27  ? 173 ASP A C     1 
ATOM   1327 O O     . ASP A 1 180 ? 21.883  1.191   16.801  1.00 32.00  ? 173 ASP A O     1 
ATOM   1328 C CB    . ASP A 1 180 ? 20.715  0.800   14.365  1.00 27.24  ? 173 ASP A CB    1 
ATOM   1329 C CG    . ASP A 1 180 ? 22.125  0.564   13.836  1.00 25.54  ? 173 ASP A CG    1 
ATOM   1330 O OD1   . ASP A 1 180 ? 22.775  -0.358  14.334  1.00 24.12  ? 173 ASP A OD1   1 
ATOM   1331 O OD2   . ASP A 1 180 ? 22.576  1.330   12.950  1.00 26.04  ? 173 ASP A OD2   1 
ATOM   1332 N N     . PRO A 1 181 ? 20.971  -0.626  17.844  1.00 30.46  ? 174 PRO A N     1 
ATOM   1333 C CA    . PRO A 1 181 ? 21.610  -0.375  19.138  1.00 33.48  ? 174 PRO A CA    1 
ATOM   1334 C C     . PRO A 1 181 ? 23.148  -0.475  19.098  1.00 35.95  ? 174 PRO A C     1 
ATOM   1335 O O     . PRO A 1 181 ? 23.779  0.133   19.951  1.00 39.00  ? 174 PRO A O     1 
ATOM   1336 C CB    . PRO A 1 181 ? 20.995  -1.444  20.074  1.00 32.19  ? 174 PRO A CB    1 
ATOM   1337 C CG    . PRO A 1 181 ? 20.507  -2.546  19.147  1.00 32.23  ? 174 PRO A CG    1 
ATOM   1338 C CD    . PRO A 1 181 ? 20.143  -1.844  17.854  1.00 32.78  ? 174 PRO A CD    1 
ATOM   1339 N N     . ASP A 1 182 ? 23.718  -1.205  18.132  1.00 34.08  ? 175 ASP A N     1 
ATOM   1340 C CA    . ASP A 1 182 ? 25.197  -1.322  17.954  1.00 37.32  ? 175 ASP A CA    1 
ATOM   1341 C C     . ASP A 1 182 ? 25.835  0.027   17.578  1.00 37.97  ? 175 ASP A C     1 
ATOM   1342 O O     . ASP A 1 182 ? 27.024  0.200   17.908  1.00 40.92  ? 175 ASP A O     1 
ATOM   1343 C CB    . ASP A 1 182 ? 25.568  -2.350  16.883  1.00 36.59  ? 175 ASP A CB    1 
ATOM   1344 C CG    . ASP A 1 182 ? 25.000  -3.723  17.157  1.00 36.85  ? 175 ASP A CG    1 
ATOM   1345 O OD1   . ASP A 1 182 ? 25.378  -4.327  18.175  1.00 33.40  ? 175 ASP A OD1   1 
ATOM   1346 O OD2   . ASP A 1 182 ? 24.136  -4.140  16.380  1.00 44.06  ? 175 ASP A OD2   1 
ATOM   1347 N N     . HIS A 1 183 ? 25.093  0.923   16.908  1.00 38.77  ? 176 HIS A N     1 
ATOM   1348 C CA    . HIS A 1 183 ? 25.552  2.235   16.357  1.00 39.18  ? 176 HIS A CA    1 
ATOM   1349 C C     . HIS A 1 183 ? 24.815  3.394   17.056  1.00 36.11  ? 176 HIS A C     1 
ATOM   1350 O O     . HIS A 1 183 ? 24.648  4.459   16.431  1.00 29.85  ? 176 HIS A O     1 
ATOM   1351 C CB    . HIS A 1 183 ? 25.389  2.248   14.819  1.00 42.91  ? 176 HIS A CB    1 
ATOM   1352 C CG    . HIS A 1 183 ? 26.207  1.201   14.129  1.00 47.85  ? 176 HIS A CG    1 
ATOM   1353 N ND1   . HIS A 1 183 ? 25.733  -0.089  13.898  1.00 52.45  ? 176 HIS A ND1   1 
ATOM   1354 C CD2   . HIS A 1 183 ? 27.478  1.221   13.669  1.00 50.48  ? 176 HIS A CD2   1 
ATOM   1355 C CE1   . HIS A 1 183 ? 26.673  -0.813  13.326  1.00 50.62  ? 176 HIS A CE1   1 
ATOM   1356 N NE2   . HIS A 1 183 ? 27.752  -0.025  13.162  1.00 54.93  ? 176 HIS A NE2   1 
ATOM   1357 N N     . ASP A 1 184 ? 24.408  3.198   18.321  1.00 36.44  ? 177 ASP A N     1 
ATOM   1358 C CA    . ASP A 1 184 ? 23.683  4.208   19.154  1.00 33.08  ? 177 ASP A CA    1 
ATOM   1359 C C     . ASP A 1 184 ? 24.647  5.264   19.730  1.00 31.32  ? 177 ASP A C     1 
ATOM   1360 O O     . ASP A 1 184 ? 24.208  6.413   19.909  1.00 30.88  ? 177 ASP A O     1 
ATOM   1361 C CB    . ASP A 1 184 ? 22.911  3.557   20.312  1.00 31.25  ? 177 ASP A CB    1 
ATOM   1362 C CG    . ASP A 1 184 ? 22.017  4.515   21.099  1.00 30.96  ? 177 ASP A CG    1 
ATOM   1363 O OD1   . ASP A 1 184 ? 20.996  4.961   20.538  1.00 27.54  ? 177 ASP A OD1   1 
ATOM   1364 O OD2   . ASP A 1 184 ? 22.365  4.827   22.256  1.00 28.75  ? 177 ASP A OD2   1 
ATOM   1365 N N     . HIS A 1 185 ? 25.890  4.913   20.064  1.00 32.14  ? 178 HIS A N     1 
ATOM   1366 C CA    . HIS A 1 185 ? 26.789  5.831   20.817  1.00 35.16  ? 178 HIS A CA    1 
ATOM   1367 C C     . HIS A 1 185 ? 27.124  7.071   19.978  1.00 33.23  ? 178 HIS A C     1 
ATOM   1368 O O     . HIS A 1 185 ? 27.119  6.991   18.731  1.00 40.49  ? 178 HIS A O     1 
ATOM   1369 C CB    . HIS A 1 185 ? 28.050  5.154   21.344  1.00 37.92  ? 178 HIS A CB    1 
ATOM   1370 C CG    . HIS A 1 185 ? 28.660  5.969   22.428  1.00 43.26  ? 178 HIS A CG    1 
ATOM   1371 N ND1   . HIS A 1 185 ? 29.563  6.991   22.171  1.00 49.18  ? 178 HIS A ND1   1 
ATOM   1372 C CD2   . HIS A 1 185 ? 28.453  5.979   23.760  1.00 47.79  ? 178 HIS A CD2   1 
ATOM   1373 C CE1   . HIS A 1 185 ? 29.908  7.571   23.304  1.00 46.14  ? 178 HIS A CE1   1 
ATOM   1374 N NE2   . HIS A 1 185 ? 29.253  6.966   24.292  1.00 50.52  ? 178 HIS A NE2   1 
ATOM   1375 N N     . THR A 1 186 ? 27.319  8.202   20.655  1.00 30.49  ? 179 THR A N     1 
ATOM   1376 C CA    . THR A 1 186 ? 27.657  9.520   20.063  1.00 27.12  ? 179 THR A CA    1 
ATOM   1377 C C     . THR A 1 186 ? 28.178  10.416  21.194  1.00 26.91  ? 179 THR A C     1 
ATOM   1378 O O     . THR A 1 186 ? 28.065  10.010  22.368  1.00 21.67  ? 179 THR A O     1 
ATOM   1379 C CB    . THR A 1 186 ? 26.436  10.131  19.364  1.00 27.05  ? 179 THR A CB    1 
ATOM   1380 O OG1   . THR A 1 186 ? 26.929  11.149  18.497  1.00 24.80  ? 179 THR A OG1   1 
ATOM   1381 C CG2   . THR A 1 186 ? 25.402  10.696  20.325  1.00 25.37  ? 179 THR A CG2   1 
ATOM   1382 N N     . GLY A 1 187 ? 28.682  11.595  20.836  1.00 25.07  ? 180 GLY A N     1 
ATOM   1383 C CA    . GLY A 1 187 ? 29.248  12.574  21.769  1.00 25.14  ? 180 GLY A CA    1 
ATOM   1384 C C     . GLY A 1 187 ? 28.203  13.236  22.660  1.00 25.47  ? 180 GLY A C     1 
ATOM   1385 O O     . GLY A 1 187 ? 27.039  12.790  22.731  1.00 24.48  ? 180 GLY A O     1 
ATOM   1386 N N     . PHE A 1 188 ? 28.653  14.275  23.355  1.00 26.34  ? 181 PHE A N     1 
ATOM   1387 C CA    . PHE A 1 188 ? 27.869  15.117  24.293  1.00 25.50  ? 181 PHE A CA    1 
ATOM   1388 C C     . PHE A 1 188 ? 27.237  16.262  23.495  1.00 24.78  ? 181 PHE A C     1 
ATOM   1389 O O     . PHE A 1 188 ? 27.904  16.810  22.595  1.00 22.52  ? 181 PHE A O     1 
ATOM   1390 C CB    . PHE A 1 188 ? 28.806  15.578  25.409  1.00 22.87  ? 181 PHE A CB    1 
ATOM   1391 C CG    . PHE A 1 188 ? 28.186  16.480  26.438  1.00 22.54  ? 181 PHE A CG    1 
ATOM   1392 C CD1   . PHE A 1 188 ? 26.972  16.153  27.021  1.00 21.40  ? 181 PHE A CD1   1 
ATOM   1393 C CD2   . PHE A 1 188 ? 28.820  17.652  26.830  1.00 20.80  ? 181 PHE A CD2   1 
ATOM   1394 C CE1   . PHE A 1 188 ? 26.421  16.969  27.991  1.00 20.00  ? 181 PHE A CE1   1 
ATOM   1395 C CE2   . PHE A 1 188 ? 28.279  18.453  27.818  1.00 18.95  ? 181 PHE A CE2   1 
ATOM   1396 C CZ    . PHE A 1 188 ? 27.068  18.127  28.371  1.00 20.75  ? 181 PHE A CZ    1 
ATOM   1397 N N     . LEU A 1 189 ? 25.985  16.597  23.806  1.00 27.48  ? 182 LEU A N     1 
ATOM   1398 C CA    . LEU A 1 189 ? 25.228  17.710  23.176  1.00 29.84  ? 182 LEU A CA    1 
ATOM   1399 C C     . LEU A 1 189 ? 25.112  17.467  21.665  1.00 31.85  ? 182 LEU A C     1 
ATOM   1400 O O     . LEU A 1 189 ? 25.296  18.442  20.904  1.00 32.84  ? 182 LEU A O     1 
ATOM   1401 C CB    . LEU A 1 189 ? 25.947  19.037  23.443  1.00 32.97  ? 182 LEU A CB    1 
ATOM   1402 C CG    . LEU A 1 189 ? 26.281  19.342  24.904  1.00 36.70  ? 182 LEU A CG    1 
ATOM   1403 C CD1   . LEU A 1 189 ? 27.154  20.585  25.021  1.00 37.69  ? 182 LEU A CD1   1 
ATOM   1404 C CD2   . LEU A 1 189 ? 25.020  19.493  25.744  1.00 37.67  ? 182 LEU A CD2   1 
ATOM   1405 N N     . THR A 1 190 ? 24.853  16.225  21.237  1.00 30.37  ? 183 THR A N     1 
ATOM   1406 C CA    . THR A 1 190 ? 24.629  15.874  19.805  1.00 31.96  ? 183 THR A CA    1 
ATOM   1407 C C     . THR A 1 190 ? 23.227  16.351  19.407  1.00 35.30  ? 183 THR A C     1 
ATOM   1408 O O     . THR A 1 190 ? 22.293  16.099  20.185  1.00 31.11  ? 183 THR A O     1 
ATOM   1409 C CB    . THR A 1 190 ? 24.818  14.372  19.540  1.00 31.29  ? 183 THR A CB    1 
ATOM   1410 O OG1   . THR A 1 190 ? 26.211  14.083  19.644  1.00 31.27  ? 183 THR A OG1   1 
ATOM   1411 C CG2   . THR A 1 190 ? 24.294  13.940  18.185  1.00 31.22  ? 183 THR A CG2   1 
ATOM   1412 N N     . GLU A 1 191 ? 23.062  17.001  18.244  1.00 41.77  ? 184 GLU A N     1 
ATOM   1413 C CA    . GLU A 1 191 ? 21.744  17.604  17.870  1.00 48.40  ? 184 GLU A CA    1 
ATOM   1414 C C     . GLU A 1 191 ? 20.701  16.471  17.717  1.00 48.26  ? 184 GLU A C     1 
ATOM   1415 O O     . GLU A 1 191 ? 21.111  15.296  17.560  1.00 52.70  ? 184 GLU A O     1 
ATOM   1416 C CB    . GLU A 1 191 ? 21.882  18.561  16.672  1.00 45.55  ? 184 GLU A CB    1 
ATOM   1417 C CG    . GLU A 1 191 ? 22.756  19.805  16.940  1.00 48.40  ? 184 GLU A CG    1 
ATOM   1418 C CD    . GLU A 1 191 ? 22.386  20.798  18.056  1.00 50.95  ? 184 GLU A CD    1 
ATOM   1419 O OE1   . GLU A 1 191 ? 21.429  20.545  18.842  1.00 47.27  ? 184 GLU A OE1   1 
ATOM   1420 O OE2   . GLU A 1 191 ? 23.077  21.846  18.160  1.00 47.23  ? 184 GLU A OE2   1 
ATOM   1421 N N     . TYR A 1 192 ? 19.405  16.793  17.837  1.00 44.67  ? 185 TYR A N     1 
ATOM   1422 C CA    . TYR A 1 192 ? 18.269  15.830  17.868  1.00 43.55  ? 185 TYR A CA    1 
ATOM   1423 C C     . TYR A 1 192 ? 16.978  16.603  17.559  1.00 43.48  ? 185 TYR A C     1 
ATOM   1424 O O     . TYR A 1 192 ? 16.870  17.747  18.036  1.00 36.47  ? 185 TYR A O     1 
ATOM   1425 C CB    . TYR A 1 192 ? 18.225  15.098  19.223  1.00 42.38  ? 185 TYR A CB    1 
ATOM   1426 C CG    . TYR A 1 192 ? 17.396  13.832  19.275  1.00 40.79  ? 185 TYR A CG    1 
ATOM   1427 C CD1   . TYR A 1 192 ? 17.835  12.639  18.705  1.00 40.04  ? 185 TYR A CD1   1 
ATOM   1428 C CD2   . TYR A 1 192 ? 16.179  13.814  19.940  1.00 39.35  ? 185 TYR A CD2   1 
ATOM   1429 C CE1   . TYR A 1 192 ? 17.072  11.477  18.768  1.00 39.09  ? 185 TYR A CE1   1 
ATOM   1430 C CE2   . TYR A 1 192 ? 15.405  12.667  20.010  1.00 38.09  ? 185 TYR A CE2   1 
ATOM   1431 C CZ    . TYR A 1 192 ? 15.851  11.492  19.428  1.00 41.45  ? 185 TYR A CZ    1 
ATOM   1432 O OH    . TYR A 1 192 ? 15.062  10.375  19.520  1.00 44.54  ? 185 TYR A OH    1 
ATOM   1433 N N     . VAL A 1 193 ? 16.032  15.967  16.852  1.00 44.40  ? 186 VAL A N     1 
ATOM   1434 C CA    . VAL A 1 193 ? 14.828  16.592  16.209  1.00 47.58  ? 186 VAL A CA    1 
ATOM   1435 C C     . VAL A 1 193 ? 13.538  16.382  17.047  1.00 42.52  ? 186 VAL A C     1 
ATOM   1436 O O     . VAL A 1 193 ? 12.637  17.259  16.959  1.00 43.48  ? 186 VAL A O     1 
ATOM   1437 C CB    . VAL A 1 193 ? 14.663  16.047  14.769  1.00 45.69  ? 186 VAL A CB    1 
ATOM   1438 C CG1   . VAL A 1 193 ? 13.429  16.611  14.070  1.00 48.78  ? 186 VAL A CG1   1 
ATOM   1439 C CG2   . VAL A 1 193 ? 15.904  16.297  13.917  1.00 45.08  ? 186 VAL A CG2   1 
ATOM   1440 N N     . ALA A 1 194 ? 13.410  15.277  17.797  1.00 35.89  ? 187 ALA A N     1 
ATOM   1441 C CA    . ALA A 1 194 ? 12.124  14.807  18.393  1.00 37.60  ? 187 ALA A CA    1 
ATOM   1442 C C     . ALA A 1 194 ? 11.786  15.638  19.631  1.00 31.80  ? 187 ALA A C     1 
ATOM   1443 O O     . ALA A 1 194 ? 12.713  16.216  20.186  1.00 33.58  ? 187 ALA A O     1 
ATOM   1444 C CB    . ALA A 1 194 ? 12.181  13.333  18.744  1.00 35.72  ? 187 ALA A CB    1 
ATOM   1445 N N     . ALA A 1 195 ? 10.513  15.652  20.052  1.00 29.73  ? 188 ALA A N     1 
ATOM   1446 C CA    . ALA A 1 195 ? 9.963   16.577  21.067  1.00 25.05  ? 188 ALA A CA    1 
ATOM   1447 C C     . ALA A 1 195 ? 10.858  16.559  22.303  1.00 23.68  ? 188 ALA A C     1 
ATOM   1448 O O     . ALA A 1 195 ? 11.026  15.459  22.880  1.00 20.84  ? 188 ALA A O     1 
ATOM   1449 C CB    . ALA A 1 195 ? 8.546   16.208  21.430  1.00 26.23  ? 188 ALA A CB    1 
ATOM   1450 N N     . ARG A 1 196 ? 11.335  17.742  22.717  1.00 20.49  ? 189 ARG A N     1 
ATOM   1451 C CA    . ARG A 1 196 ? 12.262  17.930  23.859  1.00 20.05  ? 189 ARG A CA    1 
ATOM   1452 C C     . ARG A 1 196 ? 11.728  17.294  25.148  1.00 17.42  ? 189 ARG A C     1 
ATOM   1453 O O     . ARG A 1 196 ? 12.490  16.641  25.819  1.00 17.98  ? 189 ARG A O     1 
ATOM   1454 C CB    . ARG A 1 196 ? 12.499  19.415  24.148  1.00 19.88  ? 189 ARG A CB    1 
ATOM   1455 C CG    . ARG A 1 196 ? 13.728  19.637  25.006  1.00 19.78  ? 189 ARG A CG    1 
ATOM   1456 C CD    . ARG A 1 196 ? 13.925  21.094  25.382  1.00 22.46  ? 189 ARG A CD    1 
ATOM   1457 N NE    . ARG A 1 196 ? 14.271  21.908  24.221  1.00 24.37  ? 189 ARG A NE    1 
ATOM   1458 C CZ    . ARG A 1 196 ? 13.514  22.858  23.660  1.00 26.60  ? 189 ARG A CZ    1 
ATOM   1459 N NH1   . ARG A 1 196 ? 12.314  23.153  24.141  1.00 24.66  ? 189 ARG A NH1   1 
ATOM   1460 N NH2   . ARG A 1 196 ? 13.977  23.509  22.593  1.00 27.52  ? 189 ARG A NH2   1 
ATOM   1461 N N     . TRP A 1 197 ? 10.488  17.548  25.525  1.00 16.18  ? 190 TRP A N     1 
ATOM   1462 C CA    . TRP A 1 197 ? 9.962   17.166  26.868  1.00 15.59  ? 190 TRP A CA    1 
ATOM   1463 C C     . TRP A 1 197 ? 9.943   15.641  27.074  1.00 14.06  ? 190 TRP A C     1 
ATOM   1464 O O     . TRP A 1 197 ? 9.906   15.220  28.234  1.00 13.98  ? 190 TRP A O     1 
ATOM   1465 C CB    . TRP A 1 197 ? 8.578   17.779  27.073  1.00 16.19  ? 190 TRP A CB    1 
ATOM   1466 C CG    . TRP A 1 197 ? 8.565   19.276  27.067  1.00 16.49  ? 190 TRP A CG    1 
ATOM   1467 C CD1   . TRP A 1 197 ? 9.645   20.105  27.138  1.00 17.06  ? 190 TRP A CD1   1 
ATOM   1468 C CD2   . TRP A 1 197 ? 7.406   20.123  27.115  1.00 15.95  ? 190 TRP A CD2   1 
ATOM   1469 N NE1   . TRP A 1 197 ? 9.242   21.414  27.175  1.00 17.21  ? 190 TRP A NE1   1 
ATOM   1470 C CE2   . TRP A 1 197 ? 7.871   21.454  27.172  1.00 17.85  ? 190 TRP A CE2   1 
ATOM   1471 C CE3   . TRP A 1 197 ? 6.028   19.897  27.075  1.00 16.63  ? 190 TRP A CE3   1 
ATOM   1472 C CZ2   . TRP A 1 197 ? 7.001   22.546  27.207  1.00 17.32  ? 190 TRP A CZ2   1 
ATOM   1473 C CZ3   . TRP A 1 197 ? 5.166   20.970  27.112  1.00 16.28  ? 190 TRP A CZ3   1 
ATOM   1474 C CH2   . TRP A 1 197 ? 5.651   22.278  27.157  1.00 16.53  ? 190 TRP A CH2   1 
ATOM   1475 N N     . TYR A 1 198 ? 9.978   14.843  26.009  1.00 13.63  ? 191 TYR A N     1 
ATOM   1476 C CA    . TYR A 1 198 ? 9.799   13.365  26.050  1.00 13.67  ? 191 TYR A CA    1 
ATOM   1477 C C     . TYR A 1 198 ? 11.112  12.670  25.643  1.00 14.59  ? 191 TYR A C     1 
ATOM   1478 O O     . TYR A 1 198 ? 11.099  11.433  25.403  1.00 13.38  ? 191 TYR A O     1 
ATOM   1479 C CB    . TYR A 1 198 ? 8.574   12.995  25.214  1.00 13.46  ? 191 TYR A CB    1 
ATOM   1480 C CG    . TYR A 1 198 ? 7.344   13.816  25.567  1.00 13.64  ? 191 TYR A CG    1 
ATOM   1481 C CD1   . TYR A 1 198 ? 6.506   13.449  26.604  1.00 13.64  ? 191 TYR A CD1   1 
ATOM   1482 C CD2   . TYR A 1 198 ? 7.092   15.021  24.942  1.00 13.52  ? 191 TYR A CD2   1 
ATOM   1483 C CE1   . TYR A 1 198 ? 5.426   14.228  26.986  1.00 14.45  ? 191 TYR A CE1   1 
ATOM   1484 C CE2   . TYR A 1 198 ? 6.025   15.823  25.309  1.00 14.57  ? 191 TYR A CE2   1 
ATOM   1485 C CZ    . TYR A 1 198 ? 5.187   15.415  26.323  1.00 13.86  ? 191 TYR A CZ    1 
ATOM   1486 O OH    . TYR A 1 198 ? 4.143   16.183  26.659  1.00 14.91  ? 191 TYR A OH    1 
ATOM   1487 N N     . ARG A 1 199 ? 12.214  13.436  25.562  1.00 15.72  ? 192 ARG A N     1 
ATOM   1488 C CA    . ARG A 1 199 ? 13.555  12.940  25.137  1.00 17.07  ? 192 ARG A CA    1 
ATOM   1489 C C     . ARG A 1 199 ? 14.259  12.266  26.313  1.00 15.30  ? 192 ARG A C     1 
ATOM   1490 O O     . ARG A 1 199 ? 14.358  12.872  27.403  1.00 15.67  ? 192 ARG A O     1 
ATOM   1491 C CB    . ARG A 1 199 ? 14.485  14.080  24.721  1.00 20.87  ? 192 ARG A CB    1 
ATOM   1492 C CG    . ARG A 1 199 ? 14.326  14.568  23.295  1.00 24.91  ? 192 ARG A CG    1 
ATOM   1493 C CD    . ARG A 1 199 ? 15.268  15.752  23.072  1.00 28.55  ? 192 ARG A CD    1 
ATOM   1494 N NE    . ARG A 1 199 ? 14.759  16.687  22.075  1.00 32.22  ? 192 ARG A NE    1 
ATOM   1495 C CZ    . ARG A 1 199 ? 15.313  17.853  21.773  1.00 38.57  ? 192 ARG A CZ    1 
ATOM   1496 N NH1   . ARG A 1 199 ? 16.424  18.257  22.376  1.00 41.59  ? 192 ARG A NH1   1 
ATOM   1497 N NH2   . ARG A 1 199 ? 14.752  18.613  20.852  1.00 40.31  ? 192 ARG A NH2   1 
ATOM   1498 N N     . ALA A 1 200 ? 14.758  11.060  26.134  1.00 14.65  ? 193 ALA A N     1 
ATOM   1499 C CA    . ALA A 1 200 ? 15.425  10.346  27.246  1.00 15.05  ? 193 ALA A CA    1 
ATOM   1500 C C     . ALA A 1 200 ? 16.727  11.069  27.578  1.00 15.28  ? 193 ALA A C     1 
ATOM   1501 O O     . ALA A 1 200 ? 17.313  11.719  26.713  1.00 15.60  ? 193 ALA A O     1 
ATOM   1502 C CB    . ALA A 1 200 ? 15.646  8.904   26.892  1.00 14.58  ? 193 ALA A CB    1 
ATOM   1503 N N     . PRO A 1 201 ? 17.186  10.997  28.850  1.00 14.74  ? 194 PRO A N     1 
ATOM   1504 C CA    . PRO A 1 201 ? 18.385  11.699  29.282  1.00 14.43  ? 194 PRO A CA    1 
ATOM   1505 C C     . PRO A 1 201 ? 19.598  11.306  28.447  1.00 15.63  ? 194 PRO A C     1 
ATOM   1506 O O     . PRO A 1 201 ? 20.398  12.168  28.206  1.00 18.11  ? 194 PRO A O     1 
ATOM   1507 C CB    . PRO A 1 201 ? 18.588  11.227  30.725  1.00 14.50  ? 194 PRO A CB    1 
ATOM   1508 C CG    . PRO A 1 201 ? 17.791  9.969   30.807  1.00 13.68  ? 194 PRO A CG    1 
ATOM   1509 C CD    . PRO A 1 201 ? 16.597  10.193  29.922  1.00 13.36  ? 194 PRO A CD    1 
ATOM   1510 N N     . GLU A 1 202 ? 19.706  10.044  28.028  1.00 15.38  ? 195 GLU A N     1 
ATOM   1511 C CA    . GLU A 1 202 ? 20.888  9.579   27.259  1.00 16.13  ? 195 GLU A CA    1 
ATOM   1512 C C     . GLU A 1 202 ? 20.954  10.332  25.925  1.00 17.75  ? 195 GLU A C     1 
ATOM   1513 O O     . GLU A 1 202 ? 22.074  10.464  25.396  1.00 18.42  ? 195 GLU A O     1 
ATOM   1514 C CB    . GLU A 1 202 ? 20.930  8.061   27.061  1.00 15.22  ? 195 GLU A CB    1 
ATOM   1515 C CG    . GLU A 1 202 ? 19.744  7.503   26.311  1.00 16.42  ? 195 GLU A CG    1 
ATOM   1516 C CD    . GLU A 1 202 ? 18.588  7.136   27.212  1.00 15.91  ? 195 GLU A CD    1 
ATOM   1517 O OE1   . GLU A 1 202 ? 18.493  7.690   28.354  1.00 15.16  ? 195 GLU A OE1   1 
ATOM   1518 O OE2   . GLU A 1 202 ? 17.786  6.317   26.778  1.00 15.93  ? 195 GLU A OE2   1 
ATOM   1519 N N     . ILE A 1 203 ? 19.830  10.831  25.404  1.00 18.30  ? 196 ILE A N     1 
ATOM   1520 C CA    . ILE A 1 203 ? 19.844  11.612  24.127  1.00 20.62  ? 196 ILE A CA    1 
ATOM   1521 C C     . ILE A 1 203 ? 20.792  12.810  24.306  1.00 22.58  ? 196 ILE A C     1 
ATOM   1522 O O     . ILE A 1 203 ? 21.528  13.163  23.363  1.00 21.48  ? 196 ILE A O     1 
ATOM   1523 C CB    . ILE A 1 203 ? 18.432  12.065  23.703  1.00 20.79  ? 196 ILE A CB    1 
ATOM   1524 C CG1   . ILE A 1 203 ? 17.479  10.904  23.402  1.00 20.93  ? 196 ILE A CG1   1 
ATOM   1525 C CG2   . ILE A 1 203 ? 18.506  13.031  22.533  1.00 22.00  ? 196 ILE A CG2   1 
ATOM   1526 C CD1   . ILE A 1 203 ? 17.930  10.031  22.248  1.00 21.63  ? 196 ILE A CD1   1 
ATOM   1527 N N     . MET A 1 204 ? 20.757  13.459  25.464  1.00 23.99  ? 197 MET A N     1 
ATOM   1528 C CA    . MET A 1 204 ? 21.553  14.686  25.677  1.00 25.91  ? 197 MET A CA    1 
ATOM   1529 C C     . MET A 1 204 ? 23.000  14.299  25.955  1.00 27.11  ? 197 MET A C     1 
ATOM   1530 O O     . MET A 1 204 ? 23.878  15.189  25.770  1.00 28.50  ? 197 MET A O     1 
ATOM   1531 C CB    . MET A 1 204 ? 20.995  15.525  26.820  1.00 26.63  ? 197 MET A CB    1 
ATOM   1532 C CG    . MET A 1 204 ? 19.735  16.276  26.399  1.00 28.74  ? 197 MET A CG    1 
ATOM   1533 S SD    . MET A 1 204 ? 18.309  15.162  26.236  1.00 28.64  ? 197 MET A SD    1 
ATOM   1534 C CE    . MET A 1 204 ? 17.727  15.207  27.930  1.00 25.45  ? 197 MET A CE    1 
ATOM   1535 N N     . LEU A 1 205 ? 23.231  13.031  26.318  1.00 22.65  ? 198 LEU A N     1 
ATOM   1536 C CA    . LEU A 1 205 ? 24.496  12.594  26.932  1.00 23.20  ? 198 LEU A CA    1 
ATOM   1537 C C     . LEU A 1 205 ? 25.347  11.833  25.918  1.00 25.20  ? 198 LEU A C     1 
ATOM   1538 O O     . LEU A 1 205 ? 26.480  12.294  25.689  1.00 25.33  ? 198 LEU A O     1 
ATOM   1539 C CB    . LEU A 1 205 ? 24.190  11.765  28.177  1.00 22.56  ? 198 LEU A CB    1 
ATOM   1540 C CG    . LEU A 1 205 ? 23.628  12.573  29.339  1.00 25.13  ? 198 LEU A CG    1 
ATOM   1541 C CD1   . LEU A 1 205 ? 23.279  11.693  30.527  1.00 24.89  ? 198 LEU A CD1   1 
ATOM   1542 C CD2   . LEU A 1 205 ? 24.611  13.657  29.766  1.00 26.63  ? 198 LEU A CD2   1 
ATOM   1543 N N     . ASN A 1 206 ? 24.854  10.719  25.352  1.00 26.18  ? 199 ASN A N     1 
ATOM   1544 C CA    . ASN A 1 206 ? 25.708  9.801   24.547  1.00 24.56  ? 199 ASN A CA    1 
ATOM   1545 C C     . ASN A 1 206 ? 24.930  8.908   23.568  1.00 23.77  ? 199 ASN A C     1 
ATOM   1546 O O     . ASN A 1 206 ? 25.577  7.963   23.053  1.00 21.22  ? 199 ASN A O     1 
ATOM   1547 C CB    . ASN A 1 206 ? 26.508  8.880   25.470  1.00 24.96  ? 199 ASN A CB    1 
ATOM   1548 C CG    . ASN A 1 206 ? 25.629  7.882   26.198  1.00 26.25  ? 199 ASN A CG    1 
ATOM   1549 O OD1   . ASN A 1 206 ? 24.398  7.942   26.132  1.00 25.96  ? 199 ASN A OD1   1 
ATOM   1550 N ND2   . ASN A 1 206 ? 26.247  6.940   26.886  1.00 26.60  ? 199 ASN A ND2   1 
ATOM   1551 N N     . SER A 1 207 ? 23.659  9.209   23.266  1.00 23.77  ? 200 SER A N     1 
ATOM   1552 C CA    . SER A 1 207 ? 22.741  8.335   22.475  1.00 25.35  ? 200 SER A CA    1 
ATOM   1553 C C     . SER A 1 207 ? 22.194  9.062   21.239  1.00 25.26  ? 200 SER A C     1 
ATOM   1554 O O     . SER A 1 207 ? 21.711  10.239  21.359  1.00 24.14  ? 200 SER A O     1 
ATOM   1555 C CB    . SER A 1 207 ? 21.590  7.807   23.332  1.00 27.05  ? 200 SER A CB    1 
ATOM   1556 O OG    . SER A 1 207 ? 20.772  6.880   22.612  1.00 23.62  ? 200 SER A OG    1 
ATOM   1557 N N     . LYS A 1 208 ? 22.202  8.356   20.107  1.00 23.90  ? 201 LYS A N     1 
ATOM   1558 C CA    . LYS A 1 208 ? 21.567  8.794   18.840  1.00 24.22  ? 201 LYS A CA    1 
ATOM   1559 C C     . LYS A 1 208 ? 20.071  8.436   18.842  1.00 21.40  ? 201 LYS A C     1 
ATOM   1560 O O     . LYS A 1 208 ? 19.379  8.800   17.892  1.00 20.70  ? 201 LYS A O     1 
ATOM   1561 C CB    . LYS A 1 208 ? 22.315  8.152   17.666  1.00 26.44  ? 201 LYS A CB    1 
ATOM   1562 C CG    . LYS A 1 208 ? 23.609  8.845   17.270  1.00 29.61  ? 201 LYS A CG    1 
ATOM   1563 C CD    . LYS A 1 208 ? 24.319  8.209   16.076  1.00 31.96  ? 201 LYS A CD    1 
ATOM   1564 C CE    . LYS A 1 208 ? 25.143  9.190   15.264  1.00 36.18  ? 201 LYS A CE    1 
ATOM   1565 N NZ    . LYS A 1 208 ? 25.386  8.688   13.886  1.00 39.30  ? 201 LYS A NZ    1 
ATOM   1566 N N     . GLY A 1 209 ? 19.583  7.710   19.844  1.00 19.50  ? 202 GLY A N     1 
ATOM   1567 C CA    . GLY A 1 209 ? 18.146  7.423   19.981  1.00 19.87  ? 202 GLY A CA    1 
ATOM   1568 C C     . GLY A 1 209 ? 17.744  6.221   19.165  1.00 19.05  ? 202 GLY A C     1 
ATOM   1569 O O     . GLY A 1 209 ? 16.663  6.237   18.642  1.00 18.68  ? 202 GLY A O     1 
ATOM   1570 N N     . TYR A 1 210 ? 18.592  5.192   19.133  1.00 19.75  ? 203 TYR A N     1 
ATOM   1571 C CA    . TYR A 1 210 ? 18.586  4.060   18.172  1.00 21.00  ? 203 TYR A CA    1 
ATOM   1572 C C     . TYR A 1 210 ? 18.347  2.756   18.940  1.00 20.88  ? 203 TYR A C     1 
ATOM   1573 O O     . TYR A 1 210 ? 18.533  1.632   18.386  1.00 19.02  ? 203 TYR A O     1 
ATOM   1574 C CB    . TYR A 1 210 ? 19.914  4.051   17.398  1.00 23.99  ? 203 TYR A CB    1 
ATOM   1575 C CG    . TYR A 1 210 ? 20.083  5.100   16.315  1.00 25.32  ? 203 TYR A CG    1 
ATOM   1576 C CD1   . TYR A 1 210 ? 19.129  6.074   16.095  1.00 29.17  ? 203 TYR A CD1   1 
ATOM   1577 C CD2   . TYR A 1 210 ? 21.218  5.137   15.516  1.00 27.33  ? 203 TYR A CD2   1 
ATOM   1578 C CE1   . TYR A 1 210 ? 19.280  7.037   15.109  1.00 34.83  ? 203 TYR A CE1   1 
ATOM   1579 C CE2   . TYR A 1 210 ? 21.393  6.103   14.530  1.00 30.22  ? 203 TYR A CE2   1 
ATOM   1580 C CZ    . TYR A 1 210 ? 20.415  7.060   14.317  1.00 33.29  ? 203 TYR A CZ    1 
ATOM   1581 O OH    . TYR A 1 210 ? 20.513  8.037   13.358  1.00 37.51  ? 203 TYR A OH    1 
ATOM   1582 N N     . THR A 1 211 ? 17.962  2.856   20.215  1.00 20.30  ? 204 THR A N     1 
ATOM   1583 C CA    . THR A 1 211 ? 17.528  1.653   20.953  1.00 21.51  ? 204 THR A CA    1 
ATOM   1584 C C     . THR A 1 211 ? 16.110  1.900   21.447  1.00 19.56  ? 204 THR A C     1 
ATOM   1585 O O     . THR A 1 211 ? 15.741  3.074   21.612  1.00 20.06  ? 204 THR A O     1 
ATOM   1586 C CB    . THR A 1 211 ? 18.553  1.232   22.020  1.00 24.02  ? 204 THR A CB    1 
ATOM   1587 O OG1   . THR A 1 211 ? 17.991  1.364   23.331  1.00 27.86  ? 204 THR A OG1   1 
ATOM   1588 C CG2   . THR A 1 211 ? 19.835  2.022   21.903  1.00 22.80  ? 204 THR A CG2   1 
ATOM   1589 N N     . LYS A 1 212 ? 15.393  0.795   21.656  1.00 16.91  ? 205 LYS A N     1 
ATOM   1590 C CA    . LYS A 1 212 ? 13.974  0.689   22.096  1.00 15.30  ? 205 LYS A CA    1 
ATOM   1591 C C     . LYS A 1 212 ? 13.701  1.506   23.370  1.00 15.01  ? 205 LYS A C     1 
ATOM   1592 O O     . LYS A 1 212 ? 12.572  2.009   23.524  1.00 13.39  ? 205 LYS A O     1 
ATOM   1593 C CB    . LYS A 1 212 ? 13.656  -0.796  22.297  1.00 14.70  ? 205 LYS A CB    1 
ATOM   1594 C CG    . LYS A 1 212 ? 13.310  -1.517  20.999  1.00 14.77  ? 205 LYS A CG    1 
ATOM   1595 C CD    . LYS A 1 212 ? 13.376  -3.019  21.047  1.00 14.59  ? 205 LYS A CD    1 
ATOM   1596 C CE    . LYS A 1 212 ? 13.417  -3.585  19.631  1.00 15.29  ? 205 LYS A CE    1 
ATOM   1597 N NZ    . LYS A 1 212 ? 12.818  -4.946  19.580  1.00 16.28  ? 205 LYS A NZ    1 
ATOM   1598 N N     . SER A 1 213 ? 14.678  1.637   24.266  1.00 15.00  ? 206 SER A N     1 
ATOM   1599 C CA    . SER A 1 213 ? 14.469  2.273   25.592  1.00 14.71  ? 206 SER A CA    1 
ATOM   1600 C C     . SER A 1 213 ? 14.118  3.763   25.479  1.00 13.22  ? 206 SER A C     1 
ATOM   1601 O O     . SER A 1 213 ? 13.556  4.280   26.451  1.00 12.44  ? 206 SER A O     1 
ATOM   1602 C CB    . SER A 1 213 ? 15.639  2.042   26.490  1.00 15.22  ? 206 SER A CB    1 
ATOM   1603 O OG    . SER A 1 213 ? 16.824  2.217   25.775  1.00 16.74  ? 206 SER A OG    1 
ATOM   1604 N N     . ILE A 1 214 ? 14.421  4.435   24.369  1.00 13.10  ? 207 ILE A N     1 
ATOM   1605 C CA    . ILE A 1 214 ? 14.042  5.872   24.195  1.00 14.11  ? 207 ILE A CA    1 
ATOM   1606 C C     . ILE A 1 214 ? 12.514  6.024   24.111  1.00 12.36  ? 207 ILE A C     1 
ATOM   1607 O O     . ILE A 1 214 ? 12.038  7.025   24.609  1.00 11.93  ? 207 ILE A O     1 
ATOM   1608 C CB    . ILE A 1 214 ? 14.748  6.558   23.010  1.00 15.88  ? 207 ILE A CB    1 
ATOM   1609 C CG1   . ILE A 1 214 ? 14.248  6.042   21.673  1.00 16.34  ? 207 ILE A CG1   1 
ATOM   1610 C CG2   . ILE A 1 214 ? 16.263  6.521   23.132  1.00 17.52  ? 207 ILE A CG2   1 
ATOM   1611 C CD1   . ILE A 1 214 ? 13.430  7.100   20.974  1.00 18.38  ? 207 ILE A CD1   1 
ATOM   1612 N N     . ASP A 1 215 ? 11.787  5.035   23.594  1.00 11.62  ? 208 ASP A N     1 
ATOM   1613 C CA    . ASP A 1 215 ? 10.305  5.054   23.484  1.00 11.87  ? 208 ASP A CA    1 
ATOM   1614 C C     . ASP A 1 215 ? 9.694   4.847   24.871  1.00 11.44  ? 208 ASP A C     1 
ATOM   1615 O O     . ASP A 1 215 ? 8.703   5.488   25.201  1.00 10.93  ? 208 ASP A O     1 
ATOM   1616 C CB    . ASP A 1 215 ? 9.792   3.994   22.513  1.00 12.22  ? 208 ASP A CB    1 
ATOM   1617 C CG    . ASP A 1 215 ? 9.948   4.369   21.050  1.00 12.97  ? 208 ASP A CG    1 
ATOM   1618 O OD1   . ASP A 1 215 ? 9.989   5.593   20.727  1.00 14.06  ? 208 ASP A OD1   1 
ATOM   1619 O OD2   . ASP A 1 215 ? 10.037  3.450   20.223  1.00 14.55  ? 208 ASP A OD2   1 
ATOM   1620 N N     . ILE A 1 216 ? 10.260  3.954   25.666  1.00 11.21  ? 209 ILE A N     1 
ATOM   1621 C CA    . ILE A 1 216 ? 9.699   3.675   27.009  1.00 11.17  ? 209 ILE A CA    1 
ATOM   1622 C C     . ILE A 1 216 ? 9.815   4.934   27.876  1.00 10.92  ? 209 ILE A C     1 
ATOM   1623 O O     . ILE A 1 216 ? 8.919   5.159   28.674  1.00 10.53  ? 209 ILE A O     1 
ATOM   1624 C CB    . ILE A 1 216 ? 10.384  2.478   27.646  1.00 11.30  ? 209 ILE A CB    1 
ATOM   1625 C CG1   . ILE A 1 216 ? 10.033  1.184   26.903  1.00 11.90  ? 209 ILE A CG1   1 
ATOM   1626 C CG2   . ILE A 1 216 ? 10.077  2.459   29.121  1.00 11.83  ? 209 ILE A CG2   1 
ATOM   1627 C CD1   . ILE A 1 216 ? 8.623   0.725   27.011  1.00 12.76  ? 209 ILE A CD1   1 
ATOM   1628 N N     . TRP A 1 217 ? 10.918  5.665   27.755  1.00 11.13  ? 210 TRP A N     1 
ATOM   1629 C CA    . TRP A 1 217 ? 11.132  6.947   28.483  1.00 10.81  ? 210 TRP A CA    1 
ATOM   1630 C C     . TRP A 1 217 ? 9.974   7.881   28.143  1.00 10.05  ? 210 TRP A C     1 
ATOM   1631 O O     . TRP A 1 217 ? 9.405   8.467   29.068  1.00 9.09   ? 210 TRP A O     1 
ATOM   1632 C CB    . TRP A 1 217 ? 12.471  7.596   28.103  1.00 10.88  ? 210 TRP A CB    1 
ATOM   1633 C CG    . TRP A 1 217 ? 12.610  8.900   28.809  1.00 11.22  ? 210 TRP A CG    1 
ATOM   1634 C CD1   . TRP A 1 217 ? 12.137  10.112  28.391  1.00 10.99  ? 210 TRP A CD1   1 
ATOM   1635 C CD2   . TRP A 1 217 ? 13.151  9.099   30.126  1.00 10.89  ? 210 TRP A CD2   1 
ATOM   1636 N NE1   . TRP A 1 217 ? 12.386  11.060  29.344  1.00 11.24  ? 210 TRP A NE1   1 
ATOM   1637 C CE2   . TRP A 1 217 ? 12.983  10.464  30.430  1.00 11.19  ? 210 TRP A CE2   1 
ATOM   1638 C CE3   . TRP A 1 217 ? 13.777  8.266   31.056  1.00 11.05  ? 210 TRP A CE3   1 
ATOM   1639 C CZ2   . TRP A 1 217 ? 13.437  11.014  31.621  1.00 10.95  ? 210 TRP A CZ2   1 
ATOM   1640 C CZ3   . TRP A 1 217 ? 14.241  8.809   32.222  1.00 11.08  ? 210 TRP A CZ3   1 
ATOM   1641 C CH2   . TRP A 1 217 ? 14.066  10.166  32.496  1.00 11.27  ? 210 TRP A CH2   1 
ATOM   1642 N N     . SER A 1 218 ? 9.677   8.023   26.844  1.00 9.22   ? 211 SER A N     1 
ATOM   1643 C CA    . SER A 1 218 ? 8.628   8.935   26.336  1.00 9.27   ? 211 SER A CA    1 
ATOM   1644 C C     . SER A 1 218 ? 7.309   8.460   26.929  1.00 9.04   ? 211 SER A C     1 
ATOM   1645 O O     . SER A 1 218 ? 6.555   9.271   27.434  1.00 8.86   ? 211 SER A O     1 
ATOM   1646 C CB    . SER A 1 218 ? 8.543   8.964   24.820  1.00 9.45   ? 211 SER A CB    1 
ATOM   1647 O OG    . SER A 1 218 ? 9.801   9.275   24.237  1.00 10.29  ? 211 SER A OG    1 
ATOM   1648 N N     . VAL A 1 219 ? 7.078   7.156   26.947  1.00 9.46   ? 212 VAL A N     1 
ATOM   1649 C CA    . VAL A 1 219 ? 5.794   6.624   27.483  1.00 9.57   ? 212 VAL A CA    1 
ATOM   1650 C C     . VAL A 1 219 ? 5.701   7.016   28.959  1.00 10.34  ? 212 VAL A C     1 
ATOM   1651 O O     . VAL A 1 219 ? 4.599   7.377   29.384  1.00 11.44  ? 212 VAL A O     1 
ATOM   1652 C CB    . VAL A 1 219 ? 5.656   5.109   27.256  1.00 9.28   ? 212 VAL A CB    1 
ATOM   1653 C CG1   . VAL A 1 219 ? 4.449   4.523   27.962  1.00 9.38   ? 212 VAL A CG1   1 
ATOM   1654 C CG2   . VAL A 1 219 ? 5.573   4.804   25.772  1.00 9.40   ? 212 VAL A CG2   1 
ATOM   1655 N N     . GLY A 1 220 ? 6.797   6.880   29.709  1.00 10.24  ? 213 GLY A N     1 
ATOM   1656 C CA    . GLY A 1 220 ? 6.852   7.229   31.134  1.00 10.53  ? 213 GLY A CA    1 
ATOM   1657 C C     . GLY A 1 220 ? 6.527   8.708   31.347  1.00 10.75  ? 213 GLY A C     1 
ATOM   1658 O O     . GLY A 1 220 ? 5.694   9.027   32.230  1.00 10.46  ? 213 GLY A O     1 
ATOM   1659 N N     . CYS A 1 221 ? 7.122   9.597   30.553  1.00 10.36  ? 214 CYS A N     1 
ATOM   1660 C CA    . CYS A 1 221 ? 6.757   11.043  30.551  1.00 10.69  ? 214 CYS A CA    1 
ATOM   1661 C C     . CYS A 1 221 ? 5.246   11.201  30.321  1.00 10.78  ? 214 CYS A C     1 
ATOM   1662 O O     . CYS A 1 221 ? 4.637   12.075  30.923  1.00 10.90  ? 214 CYS A O     1 
ATOM   1663 C CB    . CYS A 1 221 ? 7.585   11.754  29.483  1.00 10.66  ? 214 CYS A CB    1 
ATOM   1664 S SG    . CYS A 1 221 ? 9.343   11.752  29.939  1.00 11.25  ? 214 CYS A SG    1 
ATOM   1665 N N     . ILE A 1 222 ? 4.670   10.421  29.406  1.00 11.41  ? 215 ILE A N     1 
ATOM   1666 C CA    . ILE A 1 222 ? 3.228   10.527  29.073  1.00 12.48  ? 215 ILE A CA    1 
ATOM   1667 C C     . ILE A 1 222 ? 2.383   10.061  30.263  1.00 12.42  ? 215 ILE A C     1 
ATOM   1668 O O     . ILE A 1 222 ? 1.388   10.733  30.508  1.00 13.01  ? 215 ILE A O     1 
ATOM   1669 C CB    . ILE A 1 222 ? 2.908   9.831   27.746  1.00 12.55  ? 215 ILE A CB    1 
ATOM   1670 C CG1   . ILE A 1 222 ? 3.582   10.608  26.609  1.00 13.87  ? 215 ILE A CG1   1 
ATOM   1671 C CG2   . ILE A 1 222 ? 1.398   9.703   27.528  1.00 11.94  ? 215 ILE A CG2   1 
ATOM   1672 C CD1   . ILE A 1 222 ? 3.672   9.857   25.298  1.00 14.09  ? 215 ILE A CD1   1 
ATOM   1673 N N     . LEU A 1 223 ? 2.826   9.031   30.999  1.00 12.79  ? 216 LEU A N     1 
ATOM   1674 C CA    . LEU A 1 223 ? 2.132   8.483   32.189  1.00 13.45  ? 216 LEU A CA    1 
ATOM   1675 C C     . LEU A 1 223 ? 2.044   9.600   33.235  1.00 14.20  ? 216 LEU A C     1 
ATOM   1676 O O     . LEU A 1 223 ? 0.924   9.957   33.570  1.00 11.98  ? 216 LEU A O     1 
ATOM   1677 C CB    . LEU A 1 223 ? 2.847   7.261   32.758  1.00 13.09  ? 216 LEU A CB    1 
ATOM   1678 C CG    . LEU A 1 223 ? 2.265   6.721   34.072  1.00 13.14  ? 216 LEU A CG    1 
ATOM   1679 C CD1   . LEU A 1 223 ? 0.775   6.468   33.946  1.00 12.36  ? 216 LEU A CD1   1 
ATOM   1680 C CD2   . LEU A 1 223 ? 2.973   5.449   34.489  1.00 13.27  ? 216 LEU A CD2   1 
ATOM   1681 N N     . ALA A 1 224 ? 3.202   10.120  33.649  1.00 14.66  ? 217 ALA A N     1 
ATOM   1682 C CA    . ALA A 1 224 ? 3.382   11.301  34.522  1.00 16.50  ? 217 ALA A CA    1 
ATOM   1683 C C     . ALA A 1 224 ? 2.475   12.451  34.055  1.00 16.47  ? 217 ALA A C     1 
ATOM   1684 O O     . ALA A 1 224 ? 1.864   13.084  34.895  1.00 16.92  ? 217 ALA A O     1 
ATOM   1685 C CB    . ALA A 1 224 ? 4.848   11.708  34.573  1.00 16.35  ? 217 ALA A CB    1 
ATOM   1686 N N     . GLU A 1 225 ? 2.349   12.700  32.760  1.00 17.42  ? 218 GLU A N     1 
ATOM   1687 C CA    . GLU A 1 225 ? 1.512   13.823  32.284  1.00 18.59  ? 218 GLU A CA    1 
ATOM   1688 C C     . GLU A 1 225 ? 0.035   13.502  32.566  1.00 19.94  ? 218 GLU A C     1 
ATOM   1689 O O     . GLU A 1 225 ? -0.697  14.385  33.047  1.00 19.40  ? 218 GLU A O     1 
ATOM   1690 C CB    . GLU A 1 225 ? 1.808   14.085  30.815  1.00 19.40  ? 218 GLU A CB    1 
ATOM   1691 C CG    . GLU A 1 225 ? 1.487   15.496  30.418  1.00 20.08  ? 218 GLU A CG    1 
ATOM   1692 C CD    . GLU A 1 225 ? 2.164   15.978  29.145  1.00 18.77  ? 218 GLU A CD    1 
ATOM   1693 O OE1   . GLU A 1 225 ? 3.224   15.452  28.762  1.00 17.25  ? 218 GLU A OE1   1 
ATOM   1694 O OE2   . GLU A 1 225 ? 1.596   16.872  28.540  1.00 19.71  ? 218 GLU A OE2   1 
ATOM   1695 N N     . MET A 1 226 ? -0.374  12.254  32.320  1.00 19.91  ? 219 MET A N     1 
ATOM   1696 C CA    . MET A 1 226 ? -1.768  11.764  32.510  1.00 18.20  ? 219 MET A CA    1 
ATOM   1697 C C     . MET A 1 226 ? -2.173  11.820  33.989  1.00 19.07  ? 219 MET A C     1 
ATOM   1698 O O     . MET A 1 226 ? -3.373  12.037  34.255  1.00 22.14  ? 219 MET A O     1 
ATOM   1699 C CB    . MET A 1 226 ? -1.921  10.340  31.971  1.00 16.86  ? 219 MET A CB    1 
ATOM   1700 C CG    . MET A 1 226 ? -2.114  10.333  30.491  1.00 17.01  ? 219 MET A CG    1 
ATOM   1701 S SD    . MET A 1 226 ? -2.641  8.766   29.837  1.00 16.68  ? 219 MET A SD    1 
ATOM   1702 C CE    . MET A 1 226 ? -1.216  7.735   30.170  1.00 17.18  ? 219 MET A CE    1 
ATOM   1703 N N     . LEU A 1 227 ? -1.220  11.703  34.906  1.00 18.38  ? 220 LEU A N     1 
ATOM   1704 C CA    . LEU A 1 227 ? -1.453  11.781  36.367  1.00 19.63  ? 220 LEU A CA    1 
ATOM   1705 C C     . LEU A 1 227 ? -1.654  13.213  36.871  1.00 20.30  ? 220 LEU A C     1 
ATOM   1706 O O     . LEU A 1 227 ? -2.123  13.342  37.953  1.00 19.88  ? 220 LEU A O     1 
ATOM   1707 C CB    . LEU A 1 227 ? -0.246  11.161  37.056  1.00 22.52  ? 220 LEU A CB    1 
ATOM   1708 C CG    . LEU A 1 227 ? 0.009   9.686   36.760  1.00 22.49  ? 220 LEU A CG    1 
ATOM   1709 C CD1   . LEU A 1 227 ? 1.322   9.245   37.386  1.00 23.72  ? 220 LEU A CD1   1 
ATOM   1710 C CD2   . LEU A 1 227 ? -1.131  8.842   37.294  1.00 23.77  ? 220 LEU A CD2   1 
ATOM   1711 N N     . SER A 1 228 ? -1.292  14.267  36.148  1.00 24.05  ? 221 SER A N     1 
ATOM   1712 C CA    . SER A 1 228 ? -1.227  15.640  36.734  1.00 24.73  ? 221 SER A CA    1 
ATOM   1713 C C     . SER A 1 228 ? -1.694  16.721  35.752  1.00 23.12  ? 221 SER A C     1 
ATOM   1714 O O     . SER A 1 228 ? -1.672  17.921  36.148  1.00 22.58  ? 221 SER A O     1 
ATOM   1715 C CB    . SER A 1 228 ? 0.177   15.918  37.162  1.00 24.76  ? 221 SER A CB    1 
ATOM   1716 O OG    . SER A 1 228 ? 0.999   16.003  36.014  1.00 24.86  ? 221 SER A OG    1 
ATOM   1717 N N     . ASN A 1 229 ? -2.024  16.318  34.521  1.00 23.42  ? 222 ASN A N     1 
ATOM   1718 C CA    . ASN A 1 229 ? -2.302  17.200  33.359  1.00 24.28  ? 222 ASN A CA    1 
ATOM   1719 C C     . ASN A 1 229 ? -1.151  18.189  33.089  1.00 24.76  ? 222 ASN A C     1 
ATOM   1720 O O     . ASN A 1 229 ? -1.415  19.156  32.374  1.00 25.22  ? 222 ASN A O     1 
ATOM   1721 C CB    . ASN A 1 229 ? -3.654  17.913  33.542  1.00 23.01  ? 222 ASN A CB    1 
ATOM   1722 C CG    . ASN A 1 229 ? -4.809  16.936  33.530  1.00 23.82  ? 222 ASN A CG    1 
ATOM   1723 O OD1   . ASN A 1 229 ? -5.025  16.209  34.498  1.00 24.85  ? 222 ASN A OD1   1 
ATOM   1724 N ND2   . ASN A 1 229 ? -5.532  16.877  32.425  1.00 24.04  ? 222 ASN A ND2   1 
ATOM   1725 N N     . ARG A 1 230 ? 0.075   17.975  33.579  1.00 26.38  ? 223 ARG A N     1 
ATOM   1726 C CA    . ARG A 1 230 ? 1.245   18.841  33.224  1.00 27.93  ? 223 ARG A CA    1 
ATOM   1727 C C     . ARG A 1 230 ? 2.398   17.961  32.759  1.00 23.85  ? 223 ARG A C     1 
ATOM   1728 O O     . ARG A 1 230 ? 2.590   16.884  33.319  1.00 21.42  ? 223 ARG A O     1 
ATOM   1729 C CB    . ARG A 1 230 ? 1.809   19.688  34.372  1.00 33.13  ? 223 ARG A CB    1 
ATOM   1730 C CG    . ARG A 1 230 ? 0.952   19.819  35.626  1.00 39.62  ? 223 ARG A CG    1 
ATOM   1731 C CD    . ARG A 1 230 ? 1.798   20.185  36.846  1.00 44.15  ? 223 ARG A CD    1 
ATOM   1732 N NE    . ARG A 1 230 ? 1.321   19.514  38.064  1.00 52.75  ? 223 ARG A NE    1 
ATOM   1733 C CZ    . ARG A 1 230 ? 1.997   18.638  38.838  1.00 50.70  ? 223 ARG A CZ    1 
ATOM   1734 N NH1   . ARG A 1 230 ? 3.251   18.286  38.588  1.00 51.48  ? 223 ARG A NH1   1 
ATOM   1735 N NH2   . ARG A 1 230 ? 1.392   18.121  39.892  1.00 46.88  ? 223 ARG A NH2   1 
ATOM   1736 N N     . PRO A 1 231 ? 3.220   18.422  31.779  1.00 22.65  ? 224 PRO A N     1 
ATOM   1737 C CA    . PRO A 1 231 ? 4.372   17.673  31.292  1.00 19.64  ? 224 PRO A CA    1 
ATOM   1738 C C     . PRO A 1 231 ? 5.305   17.633  32.491  1.00 19.87  ? 224 PRO A C     1 
ATOM   1739 O O     . PRO A 1 231 ? 5.477   18.675  33.129  1.00 22.60  ? 224 PRO A O     1 
ATOM   1740 C CB    . PRO A 1 231 ? 5.009   18.521  30.187  1.00 21.18  ? 224 PRO A CB    1 
ATOM   1741 C CG    . PRO A 1 231 ? 4.560   19.914  30.533  1.00 22.73  ? 224 PRO A CG    1 
ATOM   1742 C CD    . PRO A 1 231 ? 3.190   19.769  31.186  1.00 22.69  ? 224 PRO A CD    1 
ATOM   1743 N N     . ILE A 1 232 ? 5.841   16.466  32.819  1.00 17.62  ? 225 ILE A N     1 
ATOM   1744 C CA    . ILE A 1 232 ? 6.650   16.348  34.060  1.00 17.24  ? 225 ILE A CA    1 
ATOM   1745 C C     . ILE A 1 232 ? 8.018   17.034  33.890  1.00 14.80  ? 225 ILE A C     1 
ATOM   1746 O O     . ILE A 1 232 ? 8.602   17.413  34.879  1.00 14.58  ? 225 ILE A O     1 
ATOM   1747 C CB    . ILE A 1 232 ? 6.812   14.882  34.498  1.00 18.35  ? 225 ILE A CB    1 
ATOM   1748 C CG1   . ILE A 1 232 ? 7.587   14.874  35.818  1.00 18.87  ? 225 ILE A CG1   1 
ATOM   1749 C CG2   . ILE A 1 232 ? 7.460   14.033  33.395  1.00 17.05  ? 225 ILE A CG2   1 
ATOM   1750 C CD1   . ILE A 1 232 ? 7.422   13.659  36.621  1.00 21.05  ? 225 ILE A CD1   1 
ATOM   1751 N N     . PHE A 1 233 ? 8.564   17.119  32.694  1.00 15.72  ? 226 PHE A N     1 
ATOM   1752 C CA    . PHE A 1 233 ? 9.926   17.671  32.490  1.00 16.25  ? 226 PHE A CA    1 
ATOM   1753 C C     . PHE A 1 233 ? 9.884   18.786  31.453  1.00 18.25  ? 226 PHE A C     1 
ATOM   1754 O O     . PHE A 1 233 ? 10.398  18.601  30.351  1.00 17.22  ? 226 PHE A O     1 
ATOM   1755 C CB    . PHE A 1 233 ? 10.853  16.558  32.017  1.00 15.32  ? 226 PHE A CB    1 
ATOM   1756 C CG    . PHE A 1 233 ? 10.979  15.387  32.949  1.00 13.97  ? 226 PHE A CG    1 
ATOM   1757 C CD1   . PHE A 1 233 ? 11.313  15.564  34.279  1.00 12.77  ? 226 PHE A CD1   1 
ATOM   1758 C CD2   . PHE A 1 233 ? 10.826  14.092  32.475  1.00 13.95  ? 226 PHE A CD2   1 
ATOM   1759 C CE1   . PHE A 1 233 ? 11.438  14.465  35.118  1.00 13.37  ? 226 PHE A CE1   1 
ATOM   1760 C CE2   . PHE A 1 233 ? 10.928  12.996  33.330  1.00 12.92  ? 226 PHE A CE2   1 
ATOM   1761 C CZ    . PHE A 1 233 ? 11.278  13.180  34.642  1.00 12.75  ? 226 PHE A CZ    1 
ATOM   1762 N N     . PRO A 1 234 ? 9.257   19.951  31.763  1.00 20.91  ? 227 PRO A N     1 
ATOM   1763 C CA    . PRO A 1 234 ? 9.148   21.051  30.793  1.00 23.42  ? 227 PRO A CA    1 
ATOM   1764 C C     . PRO A 1 234 ? 10.425  21.906  30.651  1.00 27.12  ? 227 PRO A C     1 
ATOM   1765 O O     . PRO A 1 234 ? 10.415  23.083  31.073  1.00 31.04  ? 227 PRO A O     1 
ATOM   1766 C CB    . PRO A 1 234 ? 7.980   21.861  31.365  1.00 21.04  ? 227 PRO A CB    1 
ATOM   1767 C CG    . PRO A 1 234 ? 8.110   21.681  32.854  1.00 21.75  ? 227 PRO A CG    1 
ATOM   1768 C CD    . PRO A 1 234 ? 8.590   20.253  33.041  1.00 21.40  ? 227 PRO A CD    1 
ATOM   1769 N N     . GLY A 1 235 ? 11.504  21.318  30.111  1.00 27.27  ? 228 GLY A N     1 
ATOM   1770 C CA    . GLY A 1 235 ? 12.776  22.022  29.828  1.00 28.75  ? 228 GLY A CA    1 
ATOM   1771 C C     . GLY A 1 235 ? 12.620  22.999  28.676  1.00 29.90  ? 228 GLY A C     1 
ATOM   1772 O O     . GLY A 1 235 ? 11.995  22.610  27.666  1.00 30.37  ? 228 GLY A O     1 
ATOM   1773 N N     . LYS A 1 236 ? 13.148  24.226  28.780  1.00 32.56  ? 229 LYS A N     1 
ATOM   1774 C CA    . LYS A 1 236 ? 12.926  25.260  27.720  1.00 32.62  ? 229 LYS A CA    1 
ATOM   1775 C C     . LYS A 1 236 ? 13.960  25.080  26.602  1.00 31.39  ? 229 LYS A C     1 
ATOM   1776 O O     . LYS A 1 236 ? 13.757  25.591  25.501  1.00 30.07  ? 229 LYS A O     1 
ATOM   1777 C CB    . LYS A 1 236 ? 12.954  26.671  28.297  1.00 33.91  ? 229 LYS A CB    1 
ATOM   1778 C CG    . LYS A 1 236 ? 11.914  26.933  29.374  1.00 38.15  ? 229 LYS A CG    1 
ATOM   1779 C CD    . LYS A 1 236 ? 12.078  28.290  30.049  1.00 38.86  ? 229 LYS A CD    1 
ATOM   1780 C CE    . LYS A 1 236 ? 11.446  28.376  31.424  1.00 40.00  ? 229 LYS A CE    1 
ATOM   1781 N NZ    . LYS A 1 236 ? 12.244  27.653  32.441  1.00 39.46  ? 229 LYS A NZ    1 
ATOM   1782 N N     . HIS A 1 237 ? 15.028  24.343  26.867  1.00 30.52  ? 230 HIS A N     1 
ATOM   1783 C CA    . HIS A 1 237 ? 16.103  24.125  25.881  1.00 32.95  ? 230 HIS A CA    1 
ATOM   1784 C C     . HIS A 1 237 ? 16.914  22.911  26.318  1.00 34.28  ? 230 HIS A C     1 
ATOM   1785 O O     . HIS A 1 237 ? 16.646  22.359  27.405  1.00 39.84  ? 230 HIS A O     1 
ATOM   1786 C CB    . HIS A 1 237 ? 16.925  25.416  25.721  1.00 36.20  ? 230 HIS A CB    1 
ATOM   1787 C CG    . HIS A 1 237 ? 17.419  25.965  27.015  1.00 33.19  ? 230 HIS A CG    1 
ATOM   1788 N ND1   . HIS A 1 237 ? 18.540  25.475  27.629  1.00 34.30  ? 230 HIS A ND1   1 
ATOM   1789 C CD2   . HIS A 1 237 ? 16.948  26.954  27.810  1.00 37.30  ? 230 HIS A CD2   1 
ATOM   1790 C CE1   . HIS A 1 237 ? 18.731  26.113  28.766  1.00 35.88  ? 230 HIS A CE1   1 
ATOM   1791 N NE2   . HIS A 1 237 ? 17.779  27.041  28.895  1.00 34.85  ? 230 HIS A NE2   1 
ATOM   1792 N N     . TYR A 1 238 ? 17.926  22.603  25.534  1.00 32.69  ? 231 TYR A N     1 
ATOM   1793 C CA    . TYR A 1 238 ? 18.474  21.254  25.329  1.00 36.54  ? 231 TYR A CA    1 
ATOM   1794 C C     . TYR A 1 238 ? 19.049  20.739  26.649  1.00 38.97  ? 231 TYR A C     1 
ATOM   1795 O O     . TYR A 1 238 ? 18.681  19.612  27.081  1.00 39.69  ? 231 TYR A O     1 
ATOM   1796 C CB    . TYR A 1 238 ? 19.429  21.377  24.144  1.00 39.33  ? 231 TYR A CB    1 
ATOM   1797 C CG    . TYR A 1 238 ? 20.076  20.091  23.734  1.00 37.12  ? 231 TYR A CG    1 
ATOM   1798 C CD1   . TYR A 1 238 ? 21.123  19.588  24.478  1.00 37.60  ? 231 TYR A CD1   1 
ATOM   1799 C CD2   . TYR A 1 238 ? 19.644  19.387  22.624  1.00 35.67  ? 231 TYR A CD2   1 
ATOM   1800 C CE1   . TYR A 1 238 ? 21.749  18.411  24.112  1.00 41.89  ? 231 TYR A CE1   1 
ATOM   1801 C CE2   . TYR A 1 238 ? 20.265  18.206  22.246  1.00 33.93  ? 231 TYR A CE2   1 
ATOM   1802 C CZ    . TYR A 1 238 ? 21.328  17.727  22.985  1.00 36.28  ? 231 TYR A CZ    1 
ATOM   1803 O OH    . TYR A 1 238 ? 21.954  16.559  22.677  1.00 37.90  ? 231 TYR A OH    1 
ATOM   1804 N N     . LEU A 1 239 ? 19.870  21.555  27.320  1.00 43.17  ? 232 LEU A N     1 
ATOM   1805 C CA    . LEU A 1 239 ? 20.573  21.160  28.574  1.00 40.19  ? 232 LEU A CA    1 
ATOM   1806 C C     . LEU A 1 239 ? 19.651  21.335  29.784  1.00 41.19  ? 232 LEU A C     1 
ATOM   1807 O O     . LEU A 1 239 ? 19.837  20.590  30.803  1.00 39.80  ? 232 LEU A O     1 
ATOM   1808 C CB    . LEU A 1 239 ? 21.843  22.004  28.723  1.00 42.39  ? 232 LEU A CB    1 
ATOM   1809 C CG    . LEU A 1 239 ? 23.024  21.318  29.395  1.00 37.42  ? 232 LEU A CG    1 
ATOM   1810 C CD1   . LEU A 1 239 ? 23.326  19.998  28.724  1.00 36.72  ? 232 LEU A CD1   1 
ATOM   1811 C CD2   . LEU A 1 239 ? 24.230  22.227  29.351  1.00 41.47  ? 232 LEU A CD2   1 
ATOM   1812 N N     . ASP A 1 240 ? 18.723  22.300  29.713  1.00 38.67  ? 233 ASP A N     1 
ATOM   1813 C CA    . ASP A 1 240 ? 17.677  22.520  30.758  1.00 30.45  ? 233 ASP A CA    1 
ATOM   1814 C C     . ASP A 1 240 ? 16.710  21.331  30.738  1.00 28.35  ? 233 ASP A C     1 
ATOM   1815 O O     . ASP A 1 240 ? 15.955  21.198  31.712  1.00 29.96  ? 233 ASP A O     1 
ATOM   1816 C CB    . ASP A 1 240 ? 16.923  23.836  30.551  1.00 26.81  ? 233 ASP A CB    1 
ATOM   1817 C CG    . ASP A 1 240 ? 15.898  24.164  31.625  1.00 26.11  ? 233 ASP A CG    1 
ATOM   1818 O OD1   . ASP A 1 240 ? 16.302  24.356  32.778  1.00 25.36  ? 233 ASP A OD1   1 
ATOM   1819 O OD2   . ASP A 1 240 ? 14.691  24.227  31.297  1.00 25.49  ? 233 ASP A OD2   1 
ATOM   1820 N N     . GLN A 1 241 ? 16.688  20.531  29.663  1.00 24.45  ? 234 GLN A N     1 
ATOM   1821 C CA    . GLN A 1 241 ? 15.930  19.246  29.676  1.00 26.93  ? 234 GLN A CA    1 
ATOM   1822 C C     . GLN A 1 241 ? 16.591  18.331  30.717  1.00 25.32  ? 234 GLN A C     1 
ATOM   1823 O O     . GLN A 1 241 ? 15.896  17.916  31.663  1.00 25.39  ? 234 GLN A O     1 
ATOM   1824 C CB    . GLN A 1 241 ? 15.823  18.622  28.278  1.00 24.31  ? 234 GLN A CB    1 
ATOM   1825 C CG    . GLN A 1 241 ? 14.793  17.497  28.165  1.00 21.27  ? 234 GLN A CG    1 
ATOM   1826 C CD    . GLN A 1 241 ? 13.433  17.815  28.737  1.00 19.68  ? 234 GLN A CD    1 
ATOM   1827 O OE1   . GLN A 1 241 ? 12.982  18.953  28.701  1.00 18.52  ? 234 GLN A OE1   1 
ATOM   1828 N NE2   . GLN A 1 241 ? 12.748  16.801  29.254  1.00 18.10  ? 234 GLN A NE2   1 
ATOM   1829 N N     . LEU A 1 242 ? 17.905  18.148  30.635  1.00 25.31  ? 235 LEU A N     1 
ATOM   1830 C CA    . LEU A 1 242 ? 18.662  17.265  31.560  1.00 27.71  ? 235 LEU A CA    1 
ATOM   1831 C C     . LEU A 1 242 ? 18.472  17.699  33.021  1.00 26.78  ? 235 LEU A C     1 
ATOM   1832 O O     . LEU A 1 242 ? 18.231  16.790  33.866  1.00 26.29  ? 235 LEU A O     1 
ATOM   1833 C CB    . LEU A 1 242 ? 20.127  17.245  31.130  1.00 30.33  ? 235 LEU A CB    1 
ATOM   1834 C CG    . LEU A 1 242 ? 20.963  16.061  31.615  1.00 31.08  ? 235 LEU A CG    1 
ATOM   1835 C CD1   . LEU A 1 242 ? 20.145  14.784  31.735  1.00 29.63  ? 235 LEU A CD1   1 
ATOM   1836 C CD2   . LEU A 1 242 ? 22.147  15.845  30.685  1.00 32.40  ? 235 LEU A CD2   1 
ATOM   1837 N N     . ASN A 1 243 ? 18.505  19.010  33.298  1.00 28.15  ? 236 ASN A N     1 
ATOM   1838 C CA    . ASN A 1 243 ? 18.317  19.637  34.638  1.00 29.43  ? 236 ASN A CA    1 
ATOM   1839 C C     . ASN A 1 243 ? 16.959  19.248  35.232  1.00 28.15  ? 236 ASN A C     1 
ATOM   1840 O O     . ASN A 1 243 ? 16.897  19.003  36.466  1.00 24.44  ? 236 ASN A O     1 
ATOM   1841 C CB    . ASN A 1 243 ? 18.364  21.171  34.588  1.00 37.49  ? 236 ASN A CB    1 
ATOM   1842 C CG    . ASN A 1 243 ? 19.767  21.750  34.595  1.00 45.33  ? 236 ASN A CG    1 
ATOM   1843 O OD1   . ASN A 1 243 ? 20.338  22.026  33.533  1.00 49.63  ? 236 ASN A OD1   1 
ATOM   1844 N ND2   . ASN A 1 243 ? 20.334  21.941  35.780  1.00 44.45  ? 236 ASN A ND2   1 
ATOM   1845 N N     . HIS A 1 244 ? 15.907  19.221  34.403  1.00 24.41  ? 237 HIS A N     1 
ATOM   1846 C CA    . HIS A 1 244 ? 14.536  18.840  34.838  1.00 24.24  ? 237 HIS A CA    1 
ATOM   1847 C C     . HIS A 1 244 ? 14.510  17.365  35.228  1.00 20.32  ? 237 HIS A C     1 
ATOM   1848 O O     . HIS A 1 244 ? 13.880  17.012  36.265  1.00 20.32  ? 237 HIS A O     1 
ATOM   1849 C CB    . HIS A 1 244 ? 13.496  19.166  33.754  1.00 26.53  ? 237 HIS A CB    1 
ATOM   1850 C CG    . HIS A 1 244 ? 12.929  20.536  33.885  1.00 30.51  ? 237 HIS A CG    1 
ATOM   1851 N ND1   . HIS A 1 244 ? 13.427  21.609  33.173  1.00 31.32  ? 237 HIS A ND1   1 
ATOM   1852 C CD2   . HIS A 1 244 ? 11.937  21.017  34.673  1.00 32.44  ? 237 HIS A CD2   1 
ATOM   1853 C CE1   . HIS A 1 244 ? 12.749  22.696  33.499  1.00 33.61  ? 237 HIS A CE1   1 
ATOM   1854 N NE2   . HIS A 1 244 ? 11.836  22.360  34.422  1.00 32.89  ? 237 HIS A NE2   1 
ATOM   1855 N N     . ILE A 1 245 ? 15.157  16.502  34.459  1.00 17.88  ? 238 ILE A N     1 
ATOM   1856 C CA    . ILE A 1 245 ? 15.095  15.029  34.744  1.00 17.34  ? 238 ILE A CA    1 
ATOM   1857 C C     . ILE A 1 245 ? 15.784  14.763  36.092  1.00 17.90  ? 238 ILE A C     1 
ATOM   1858 O O     . ILE A 1 245 ? 15.122  14.271  37.018  1.00 16.89  ? 238 ILE A O     1 
ATOM   1859 C CB    . ILE A 1 245 ? 15.641  14.225  33.557  1.00 17.56  ? 238 ILE A CB    1 
ATOM   1860 C CG1   . ILE A 1 245 ? 14.744  14.425  32.331  1.00 16.92  ? 238 ILE A CG1   1 
ATOM   1861 C CG2   . ILE A 1 245 ? 15.817  12.756  33.890  1.00 16.49  ? 238 ILE A CG2   1 
ATOM   1862 C CD1   . ILE A 1 245 ? 15.403  14.049  31.005  1.00 16.97  ? 238 ILE A CD1   1 
ATOM   1863 N N     . LEU A 1 246 ? 17.015  15.231  36.252  1.00 19.27  ? 239 LEU A N     1 
ATOM   1864 C CA    . LEU A 1 246 ? 17.837  15.029  37.476  1.00 19.15  ? 239 LEU A CA    1 
ATOM   1865 C C     . LEU A 1 246 ? 17.276  15.899  38.604  1.00 18.84  ? 239 LEU A C     1 
ATOM   1866 O O     . LEU A 1 246 ? 17.581  15.638  39.734  1.00 21.14  ? 239 LEU A O     1 
ATOM   1867 C CB    . LEU A 1 246 ? 19.288  15.418  37.159  1.00 19.24  ? 239 LEU A CB    1 
ATOM   1868 C CG    . LEU A 1 246 ? 19.831  14.812  35.874  1.00 19.34  ? 239 LEU A CG    1 
ATOM   1869 C CD1   . LEU A 1 246 ? 21.159  15.439  35.503  1.00 21.11  ? 239 LEU A CD1   1 
ATOM   1870 C CD2   . LEU A 1 246 ? 19.938  13.306  35.999  1.00 18.14  ? 239 LEU A CD2   1 
ATOM   1871 N N     . GLY A 1 247 ? 16.518  16.935  38.294  1.00 20.52  ? 240 GLY A N     1 
ATOM   1872 C CA    . GLY A 1 247 ? 15.774  17.676  39.327  1.00 22.30  ? 240 GLY A CA    1 
ATOM   1873 C C     . GLY A 1 247 ? 14.890  16.731  40.114  1.00 23.37  ? 240 GLY A C     1 
ATOM   1874 O O     . GLY A 1 247 ? 14.705  17.002  41.290  1.00 24.81  ? 240 GLY A O     1 
ATOM   1875 N N     . ILE A 1 248 ? 14.421  15.632  39.497  1.00 21.62  ? 241 ILE A N     1 
ATOM   1876 C CA    . ILE A 1 248 ? 13.434  14.683  40.091  1.00 20.58  ? 241 ILE A CA    1 
ATOM   1877 C C     . ILE A 1 248 ? 14.059  13.318  40.354  1.00 20.45  ? 241 ILE A C     1 
ATOM   1878 O O     . ILE A 1 248 ? 13.754  12.738  41.428  1.00 22.50  ? 241 ILE A O     1 
ATOM   1879 C CB    . ILE A 1 248 ? 12.199  14.570  39.194  1.00 21.19  ? 241 ILE A CB    1 
ATOM   1880 C CG1   . ILE A 1 248 ? 11.308  15.810  39.328  1.00 24.17  ? 241 ILE A CG1   1 
ATOM   1881 C CG2   . ILE A 1 248 ? 11.447  13.300  39.516  1.00 21.62  ? 241 ILE A CG2   1 
ATOM   1882 C CD1   . ILE A 1 248 ? 10.651  16.232  38.019  1.00 25.99  ? 241 ILE A CD1   1 
ATOM   1883 N N     . LEU A 1 249 ? 14.861  12.782  39.425  1.00 19.60  ? 242 LEU A N     1 
ATOM   1884 C CA    . LEU A 1 249 ? 15.498  11.451  39.635  1.00 18.61  ? 242 LEU A CA    1 
ATOM   1885 C C     . LEU A 1 249 ? 16.624  11.594  40.657  1.00 17.98  ? 242 LEU A C     1 
ATOM   1886 O O     . LEU A 1 249 ? 16.930  10.611  41.385  1.00 17.26  ? 242 LEU A O     1 
ATOM   1887 C CB    . LEU A 1 249 ? 16.044  10.878  38.324  1.00 18.64  ? 242 LEU A CB    1 
ATOM   1888 C CG    . LEU A 1 249 ? 15.045  10.565  37.208  1.00 18.29  ? 242 LEU A CG    1 
ATOM   1889 C CD1   . LEU A 1 249 ? 15.735  9.786   36.085  1.00 16.76  ? 242 LEU A CD1   1 
ATOM   1890 C CD2   . LEU A 1 249 ? 13.824  9.834   37.703  1.00 18.35  ? 242 LEU A CD2   1 
ATOM   1891 N N     . GLY A 1 250 ? 17.207  12.784  40.737  1.00 17.90  ? 243 GLY A N     1 
ATOM   1892 C CA    . GLY A 1 250 ? 18.325  13.042  41.660  1.00 18.23  ? 243 GLY A CA    1 
ATOM   1893 C C     . GLY A 1 250 ? 19.606  12.691  40.949  1.00 17.04  ? 243 GLY A C     1 
ATOM   1894 O O     . GLY A 1 250 ? 19.522  12.378  39.767  1.00 20.46  ? 243 GLY A O     1 
ATOM   1895 N N     . SER A 1 251 ? 20.736  12.701  41.628  1.00 15.50  ? 244 SER A N     1 
ATOM   1896 C CA    . SER A 1 251 ? 22.053  12.564  40.968  1.00 16.15  ? 244 SER A CA    1 
ATOM   1897 C C     . SER A 1 251 ? 22.192  11.129  40.505  1.00 15.89  ? 244 SER A C     1 
ATOM   1898 O O     . SER A 1 251 ? 21.856  10.236  41.247  1.00 16.77  ? 244 SER A O     1 
ATOM   1899 C CB    . SER A 1 251 ? 23.183  12.994  41.857  1.00 15.07  ? 244 SER A CB    1 
ATOM   1900 O OG    . SER A 1 251 ? 23.076  14.370  42.127  1.00 14.97  ? 244 SER A OG    1 
ATOM   1901 N N     . PRO A 1 252 ? 22.620  10.872  39.249  1.00 16.98  ? 245 PRO A N     1 
ATOM   1902 C CA    . PRO A 1 252 ? 22.984  9.519   38.836  1.00 15.99  ? 245 PRO A CA    1 
ATOM   1903 C C     . PRO A 1 252 ? 24.025  8.844   39.755  1.00 16.12  ? 245 PRO A C     1 
ATOM   1904 O O     . PRO A 1 252 ? 25.094  9.411   40.076  1.00 12.91  ? 245 PRO A O     1 
ATOM   1905 C CB    . PRO A 1 252 ? 23.591  9.720   37.440  1.00 17.00  ? 245 PRO A CB    1 
ATOM   1906 C CG    . PRO A 1 252 ? 22.959  10.984  36.935  1.00 18.76  ? 245 PRO A CG    1 
ATOM   1907 C CD    . PRO A 1 252 ? 22.727  11.854  38.158  1.00 17.19  ? 245 PRO A CD    1 
ATOM   1908 N N     . SER A 1 253 ? 23.734  7.590   40.086  1.00 16.29  ? 246 SER A N     1 
ATOM   1909 C CA    . SER A 1 253 ? 24.604  6.710   40.896  1.00 17.05  ? 246 SER A CA    1 
ATOM   1910 C C     . SER A 1 253 ? 25.926  6.462   40.173  1.00 19.22  ? 246 SER A C     1 
ATOM   1911 O O     . SER A 1 253 ? 26.036  6.689   38.910  1.00 20.01  ? 246 SER A O     1 
ATOM   1912 C CB    . SER A 1 253 ? 23.910  5.406   41.207  1.00 16.08  ? 246 SER A CB    1 
ATOM   1913 O OG    . SER A 1 253 ? 23.854  4.616   40.044  1.00 14.56  ? 246 SER A OG    1 
ATOM   1914 N N     . GLN A 1 254 ? 26.899  5.988   40.940  1.00 21.63  ? 247 GLN A N     1 
ATOM   1915 C CA    . GLN A 1 254 ? 28.250  5.680   40.418  1.00 25.89  ? 247 GLN A CA    1 
ATOM   1916 C C     . GLN A 1 254 ? 28.089  4.635   39.315  1.00 26.57  ? 247 GLN A C     1 
ATOM   1917 O O     . GLN A 1 254 ? 28.689  4.822   38.252  1.00 22.98  ? 247 GLN A O     1 
ATOM   1918 C CB    . GLN A 1 254 ? 29.153  5.156   41.534  1.00 27.87  ? 247 GLN A CB    1 
ATOM   1919 C CG    . GLN A 1 254 ? 30.610  5.010   41.111  1.00 31.70  ? 247 GLN A CG    1 
ATOM   1920 C CD    . GLN A 1 254 ? 31.435  4.253   42.123  1.00 34.84  ? 247 GLN A CD    1 
ATOM   1921 O OE1   . GLN A 1 254 ? 30.949  3.807   43.171  1.00 36.00  ? 247 GLN A OE1   1 
ATOM   1922 N NE2   . GLN A 1 254 ? 32.705  4.087   41.795  1.00 40.17  ? 247 GLN A NE2   1 
ATOM   1923 N N     . GLU A 1 255 ? 27.304  3.587   39.607  1.00 27.52  ? 248 GLU A N     1 
ATOM   1924 C CA    . GLU A 1 255 ? 26.955  2.510   38.654  1.00 32.48  ? 248 GLU A CA    1 
ATOM   1925 C C     . GLU A 1 255 ? 26.490  3.137   37.340  1.00 33.96  ? 248 GLU A C     1 
ATOM   1926 O O     . GLU A 1 255 ? 27.070  2.792   36.309  1.00 36.34  ? 248 GLU A O     1 
ATOM   1927 C CB    . GLU A 1 255 ? 25.856  1.594   39.184  1.00 34.40  ? 248 GLU A CB    1 
ATOM   1928 C CG    . GLU A 1 255 ? 25.390  0.606   38.127  1.00 39.71  ? 248 GLU A CG    1 
ATOM   1929 C CD    . GLU A 1 255 ? 24.771  -0.682  38.639  1.00 42.82  ? 248 GLU A CD    1 
ATOM   1930 O OE1   . GLU A 1 255 ? 24.900  -1.701  37.933  1.00 49.08  ? 248 GLU A OE1   1 
ATOM   1931 O OE2   . GLU A 1 255 ? 24.169  -0.667  39.732  1.00 43.89  ? 248 GLU A OE2   1 
ATOM   1932 N N     . ASP A 1 256 ? 25.476  4.009   37.376  1.00 30.03  ? 249 ASP A N     1 
ATOM   1933 C CA    . ASP A 1 256 ? 24.894  4.583   36.132  1.00 29.30  ? 249 ASP A CA    1 
ATOM   1934 C C     . ASP A 1 256 ? 25.944  5.483   35.447  1.00 27.60  ? 249 ASP A C     1 
ATOM   1935 O O     . ASP A 1 256 ? 26.064  5.429   34.216  1.00 26.35  ? 249 ASP A O     1 
ATOM   1936 C CB    . ASP A 1 256 ? 23.532  5.194   36.454  1.00 29.72  ? 249 ASP A CB    1 
ATOM   1937 C CG    . ASP A 1 256 ? 22.504  4.136   36.862  1.00 30.70  ? 249 ASP A CG    1 
ATOM   1938 O OD1   . ASP A 1 256 ? 22.792  2.908   36.714  1.00 28.62  ? 249 ASP A OD1   1 
ATOM   1939 O OD2   . ASP A 1 256 ? 21.427  4.524   37.324  1.00 28.85  ? 249 ASP A OD2   1 
ATOM   1940 N N     . LEU A 1 257 ? 26.764  6.209   36.203  1.00 27.36  ? 250 LEU A N     1 
ATOM   1941 C CA    . LEU A 1 257 ? 27.891  6.981   35.608  1.00 30.46  ? 250 LEU A CA    1 
ATOM   1942 C C     . LEU A 1 257 ? 28.882  6.021   34.963  1.00 33.13  ? 250 LEU A C     1 
ATOM   1943 O O     . LEU A 1 257 ? 29.369  6.370   33.881  1.00 36.99  ? 250 LEU A O     1 
ATOM   1944 C CB    . LEU A 1 257 ? 28.612  7.818   36.664  1.00 30.02  ? 250 LEU A CB    1 
ATOM   1945 C CG    . LEU A 1 257 ? 28.058  9.210   36.931  1.00 30.63  ? 250 LEU A CG    1 
ATOM   1946 C CD1   . LEU A 1 257 ? 29.162  10.100  37.461  1.00 30.74  ? 250 LEU A CD1   1 
ATOM   1947 C CD2   . LEU A 1 257 ? 27.446  9.839   35.687  1.00 32.29  ? 250 LEU A CD2   1 
ATOM   1948 N N     . ASN A 1 258 ? 29.160  4.872   35.597  1.00 38.24  ? 251 ASN A N     1 
ATOM   1949 C CA    . ASN A 1 258 ? 30.132  3.857   35.096  1.00 41.64  ? 251 ASN A CA    1 
ATOM   1950 C C     . ASN A 1 258 ? 29.789  3.505   33.641  1.00 44.13  ? 251 ASN A C     1 
ATOM   1951 O O     . ASN A 1 258 ? 30.738  3.262   32.835  1.00 39.45  ? 251 ASN A O     1 
ATOM   1952 C CB    . ASN A 1 258 ? 30.194  2.577   35.944  1.00 43.37  ? 251 ASN A CB    1 
ATOM   1953 C CG    . ASN A 1 258 ? 30.908  2.729   37.275  1.00 46.12  ? 251 ASN A CG    1 
ATOM   1954 O OD1   . ASN A 1 258 ? 30.827  1.848   38.143  1.00 45.74  ? 251 ASN A OD1   1 
ATOM   1955 N ND2   . ASN A 1 258 ? 31.623  3.829   37.450  1.00 42.57  ? 251 ASN A ND2   1 
ATOM   1956 N N     . CYS A 1 259 ? 28.496  3.483   33.304  1.00 43.73  ? 252 CYS A N     1 
ATOM   1957 C CA    . CYS A 1 259 ? 28.013  3.114   31.944  1.00 44.79  ? 252 CYS A CA    1 
ATOM   1958 C C     . CYS A 1 259 ? 28.316  4.234   30.933  1.00 37.42  ? 252 CYS A C     1 
ATOM   1959 O O     . CYS A 1 259 ? 28.480  3.904   29.753  1.00 38.27  ? 252 CYS A O     1 
ATOM   1960 C CB    . CYS A 1 259 ? 26.531  2.747   31.956  1.00 49.80  ? 252 CYS A CB    1 
ATOM   1961 S SG    . CYS A 1 259 ? 26.231  0.962   31.861  1.00 63.31  ? 252 CYS A SG    1 
ATOM   1962 N N     . ILE A 1 260 ? 28.400  5.499   31.366  1.00 33.49  ? 253 ILE A N     1 
ATOM   1963 C CA    . ILE A 1 260 ? 28.734  6.670   30.495  1.00 30.86  ? 253 ILE A CA    1 
ATOM   1964 C C     . ILE A 1 260 ? 30.258  6.788   30.381  1.00 29.83  ? 253 ILE A C     1 
ATOM   1965 O O     . ILE A 1 260 ? 30.919  7.323   31.290  1.00 26.45  ? 253 ILE A O     1 
ATOM   1966 C CB    . ILE A 1 260 ? 28.113  7.980   31.020  1.00 30.00  ? 253 ILE A CB    1 
ATOM   1967 C CG1   . ILE A 1 260 ? 26.585  7.879   31.137  1.00 29.04  ? 253 ILE A CG1   1 
ATOM   1968 C CG2   . ILE A 1 260 ? 28.565  9.147   30.144  1.00 27.43  ? 253 ILE A CG2   1 
ATOM   1969 C CD1   . ILE A 1 260 ? 25.969  8.944   32.015  1.00 29.93  ? 253 ILE A CD1   1 
ATOM   1970 N N     . ILE A 1 261 ? 30.816  6.323   29.279  1.00 31.76  ? 254 ILE A N     1 
ATOM   1971 C CA    . ILE A 1 261 ? 32.296  6.269   29.145  1.00 33.39  ? 254 ILE A CA    1 
ATOM   1972 C C     . ILE A 1 261 ? 32.797  7.584   28.531  1.00 30.13  ? 254 ILE A C     1 
ATOM   1973 O O     . ILE A 1 261 ? 33.987  7.913   28.735  1.00 28.41  ? 254 ILE A O     1 
ATOM   1974 C CB    . ILE A 1 261 ? 32.668  5.002   28.370  1.00 35.48  ? 254 ILE A CB    1 
ATOM   1975 C CG1   . ILE A 1 261 ? 32.277  5.101   26.899  1.00 37.51  ? 254 ILE A CG1   1 
ATOM   1976 C CG2   . ILE A 1 261 ? 32.019  3.801   29.044  1.00 38.53  ? 254 ILE A CG2   1 
ATOM   1977 C CD1   . ILE A 1 261 ? 33.282  5.857   26.081  1.00 42.61  ? 254 ILE A CD1   1 
ATOM   1978 N N     . ASN A 1 262 ? 31.923  8.322   27.846  1.00 26.09  ? 255 ASN A N     1 
ATOM   1979 C CA    . ASN A 1 262 ? 32.297  9.560   27.115  1.00 27.12  ? 255 ASN A CA    1 
ATOM   1980 C C     . ASN A 1 262 ? 32.563  10.661  28.149  1.00 26.84  ? 255 ASN A C     1 
ATOM   1981 O O     . ASN A 1 262 ? 31.683  10.922  29.018  1.00 19.54  ? 255 ASN A O     1 
ATOM   1982 C CB    . ASN A 1 262 ? 31.243  9.911   26.070  1.00 31.63  ? 255 ASN A CB    1 
ATOM   1983 C CG    . ASN A 1 262 ? 30.841  11.369  26.056  1.00 35.83  ? 255 ASN A CG    1 
ATOM   1984 O OD1   . ASN A 1 262 ? 29.660  11.654  26.235  1.00 40.02  ? 255 ASN A OD1   1 
ATOM   1985 N ND2   . ASN A 1 262 ? 31.775  12.280  25.801  1.00 30.94  ? 255 ASN A ND2   1 
ATOM   1986 N N     . LEU A 1 263 ? 33.756  11.253  28.090  1.00 24.07  ? 256 LEU A N     1 
ATOM   1987 C CA    . LEU A 1 263 ? 34.282  12.081  29.205  1.00 23.13  ? 256 LEU A CA    1 
ATOM   1988 C C     . LEU A 1 263 ? 33.566  13.424  29.309  1.00 20.95  ? 256 LEU A C     1 
ATOM   1989 O O     . LEU A 1 263 ? 33.409  13.894  30.453  1.00 21.60  ? 256 LEU A O     1 
ATOM   1990 C CB    . LEU A 1 263 ? 35.796  12.211  29.051  1.00 23.06  ? 256 LEU A CB    1 
ATOM   1991 C CG    . LEU A 1 263 ? 36.487  10.942  29.551  1.00 25.36  ? 256 LEU A CG    1 
ATOM   1992 C CD1   . LEU A 1 263 ? 37.834  10.736  28.893  1.00 26.10  ? 256 LEU A CD1   1 
ATOM   1993 C CD2   . LEU A 1 263 ? 36.597  10.958  31.072  1.00 25.02  ? 256 LEU A CD2   1 
ATOM   1994 N N     . LYS A 1 264 ? 33.130  14.010  28.199  1.00 18.57  ? 257 LYS A N     1 
ATOM   1995 C CA    . LYS A 1 264 ? 32.380  15.281  28.250  1.00 19.38  ? 257 LYS A CA    1 
ATOM   1996 C C     . LYS A 1 264 ? 31.047  15.044  28.976  1.00 17.47  ? 257 LYS A C     1 
ATOM   1997 O O     . LYS A 1 264 ? 30.753  15.808  29.889  1.00 15.73  ? 257 LYS A O     1 
ATOM   1998 C CB    . LYS A 1 264 ? 32.129  15.869  26.868  1.00 21.21  ? 257 LYS A CB    1 
ATOM   1999 C CG    . LYS A 1 264 ? 33.279  16.662  26.262  1.00 25.47  ? 257 LYS A CG    1 
ATOM   2000 C CD    . LYS A 1 264 ? 32.778  17.546  25.135  1.00 27.47  ? 257 LYS A CD    1 
ATOM   2001 C CE    . LYS A 1 264 ? 33.780  17.863  24.051  1.00 29.30  ? 257 LYS A CE    1 
ATOM   2002 N NZ    . LYS A 1 264 ? 33.041  18.040  22.776  1.00 33.08  ? 257 LYS A NZ    1 
ATOM   2003 N N     . ALA A 1 265 ? 30.268  14.032  28.595  1.00 16.44  ? 258 ALA A N     1 
ATOM   2004 C CA    . ALA A 1 265 ? 28.981  13.712  29.278  1.00 16.72  ? 258 ALA A CA    1 
ATOM   2005 C C     . ALA A 1 265 ? 29.223  13.441  30.764  1.00 16.87  ? 258 ALA A C     1 
ATOM   2006 O O     . ALA A 1 265 ? 28.507  14.034  31.616  1.00 16.35  ? 258 ALA A O     1 
ATOM   2007 C CB    . ALA A 1 265 ? 28.293  12.538  28.636  1.00 16.06  ? 258 ALA A CB    1 
ATOM   2008 N N     . ARG A 1 266 ? 30.197  12.576  31.056  1.00 17.92  ? 259 ARG A N     1 
ATOM   2009 C CA    . ARG A 1 266 ? 30.540  12.149  32.429  1.00 20.62  ? 259 ARG A CA    1 
ATOM   2010 C C     . ARG A 1 266 ? 30.903  13.379  33.270  1.00 18.00  ? 259 ARG A C     1 
ATOM   2011 O O     . ARG A 1 266 ? 30.288  13.544  34.305  1.00 17.72  ? 259 ARG A O     1 
ATOM   2012 C CB    . ARG A 1 266 ? 31.671  11.118  32.420  1.00 25.67  ? 259 ARG A CB    1 
ATOM   2013 C CG    . ARG A 1 266 ? 32.354  10.965  33.773  1.00 29.59  ? 259 ARG A CG    1 
ATOM   2014 C CD    . ARG A 1 266 ? 33.535  10.046  33.646  1.00 32.56  ? 259 ARG A CD    1 
ATOM   2015 N NE    . ARG A 1 266 ? 32.978  8.778   33.230  1.00 36.30  ? 259 ARG A NE    1 
ATOM   2016 C CZ    . ARG A 1 266 ? 32.481  7.876   34.059  1.00 36.78  ? 259 ARG A CZ    1 
ATOM   2017 N NH1   . ARG A 1 266 ? 32.517  8.090   35.363  1.00 36.48  ? 259 ARG A NH1   1 
ATOM   2018 N NH2   . ARG A 1 266 ? 31.976  6.752   33.577  1.00 37.33  ? 259 ARG A NH2   1 
ATOM   2019 N N     . ASN A 1 267 ? 31.829  14.222  32.812  1.00 17.10  ? 260 ASN A N     1 
ATOM   2020 C CA    . ASN A 1 267 ? 32.332  15.394  33.580  1.00 16.45  ? 260 ASN A CA    1 
ATOM   2021 C C     . ASN A 1 267 ? 31.219  16.427  33.722  1.00 15.42  ? 260 ASN A C     1 
ATOM   2022 O O     . ASN A 1 267 ? 31.125  17.012  34.813  1.00 14.55  ? 260 ASN A O     1 
ATOM   2023 C CB    . ASN A 1 267 ? 33.625  15.993  32.999  1.00 16.39  ? 260 ASN A CB    1 
ATOM   2024 C CG    . ASN A 1 267 ? 34.810  15.066  33.184  1.00 16.98  ? 260 ASN A CG    1 
ATOM   2025 O OD1   . ASN A 1 267 ? 35.681  14.981  32.305  1.00 18.59  ? 260 ASN A OD1   1 
ATOM   2026 N ND2   . ASN A 1 267 ? 34.821  14.314  34.277  1.00 15.24  ? 260 ASN A ND2   1 
ATOM   2027 N N     . TYR A 1 268 ? 30.368  16.636  32.709  1.00 14.95  ? 261 TYR A N     1 
ATOM   2028 C CA    . TYR A 1 268 ? 29.168  17.486  32.932  1.00 15.21  ? 261 TYR A CA    1 
ATOM   2029 C C     . TYR A 1 268 ? 28.393  16.986  34.170  1.00 14.51  ? 261 TYR A C     1 
ATOM   2030 O O     . TYR A 1 268 ? 28.068  17.779  35.034  1.00 13.69  ? 261 TYR A O     1 
ATOM   2031 C CB    . TYR A 1 268 ? 28.250  17.567  31.709  1.00 15.36  ? 261 TYR A CB    1 
ATOM   2032 C CG    . TYR A 1 268 ? 27.081  18.465  32.006  1.00 16.16  ? 261 TYR A CG    1 
ATOM   2033 C CD1   . TYR A 1 268 ? 27.260  19.839  32.116  1.00 15.67  ? 261 TYR A CD1   1 
ATOM   2034 C CD2   . TYR A 1 268 ? 25.827  17.939  32.280  1.00 15.79  ? 261 TYR A CD2   1 
ATOM   2035 C CE1   . TYR A 1 268 ? 26.197  20.673  32.416  1.00 15.37  ? 261 TYR A CE1   1 
ATOM   2036 C CE2   . TYR A 1 268 ? 24.754  18.765  32.570  1.00 15.95  ? 261 TYR A CE2   1 
ATOM   2037 C CZ    . TYR A 1 268 ? 24.946  20.132  32.652  1.00 15.96  ? 261 TYR A CZ    1 
ATOM   2038 O OH    . TYR A 1 268 ? 23.910  20.927  33.043  1.00 17.09  ? 261 TYR A OH    1 
ATOM   2039 N N     . LEU A 1 269 ? 28.084  15.689  34.251  1.00 14.76  ? 262 LEU A N     1 
ATOM   2040 C CA    . LEU A 1 269 ? 27.196  15.111  35.316  1.00 14.00  ? 262 LEU A CA    1 
ATOM   2041 C C     . LEU A 1 269 ? 27.903  15.229  36.675  1.00 14.42  ? 262 LEU A C     1 
ATOM   2042 O O     . LEU A 1 269 ? 27.223  15.479  37.712  1.00 14.10  ? 262 LEU A O     1 
ATOM   2043 C CB    . LEU A 1 269 ? 26.874  13.633  35.017  1.00 13.75  ? 262 LEU A CB    1 
ATOM   2044 C CG    . LEU A 1 269 ? 25.895  13.388  33.879  1.00 13.50  ? 262 LEU A CG    1 
ATOM   2045 C CD1   . LEU A 1 269 ? 25.702  11.924  33.589  1.00 12.88  ? 262 LEU A CD1   1 
ATOM   2046 C CD2   . LEU A 1 269 ? 24.541  14.018  34.197  1.00 14.41  ? 262 LEU A CD2   1 
ATOM   2047 N N     . LEU A 1 270 ? 29.220  15.083  36.669  1.00 13.74  ? 263 LEU A N     1 
ATOM   2048 C CA    . LEU A 1 270 ? 30.062  15.232  37.885  1.00 14.91  ? 263 LEU A CA    1 
ATOM   2049 C C     . LEU A 1 270 ? 30.121  16.688  38.375  1.00 14.21  ? 263 LEU A C     1 
ATOM   2050 O O     . LEU A 1 270 ? 30.309  16.886  39.569  1.00 15.53  ? 263 LEU A O     1 
ATOM   2051 C CB    . LEU A 1 270 ? 31.455  14.679  37.570  1.00 14.68  ? 263 LEU A CB    1 
ATOM   2052 C CG    . LEU A 1 270 ? 31.519  13.154  37.465  1.00 14.91  ? 263 LEU A CG    1 
ATOM   2053 C CD1   . LEU A 1 270 ? 32.961  12.669  37.429  1.00 15.04  ? 263 LEU A CD1   1 
ATOM   2054 C CD2   . LEU A 1 270 ? 30.777  12.515  38.634  1.00 16.13  ? 263 LEU A CD2   1 
ATOM   2055 N N     . SER A 1 271 ? 29.902  17.659  37.504  1.00 14.15  ? 264 SER A N     1 
ATOM   2056 C CA    . SER A 1 271 ? 30.060  19.111  37.772  1.00 14.54  ? 264 SER A CA    1 
ATOM   2057 C C     . SER A 1 271 ? 28.854  19.636  38.539  1.00 14.61  ? 264 SER A C     1 
ATOM   2058 O O     . SER A 1 271 ? 28.920  20.746  39.066  1.00 16.12  ? 264 SER A O     1 
ATOM   2059 C CB    . SER A 1 271 ? 30.230  19.873  36.466  1.00 14.51  ? 264 SER A CB    1 
ATOM   2060 O OG    . SER A 1 271 ? 28.973  19.991  35.788  1.00 13.38  ? 264 SER A OG    1 
ATOM   2061 N N     . LEU A 1 272 ? 27.773  18.864  38.554  1.00 17.03  ? 265 LEU A N     1 
ATOM   2062 C CA    . LEU A 1 272 ? 26.441  19.274  39.052  1.00 15.95  ? 265 LEU A CA    1 
ATOM   2063 C C     . LEU A 1 272 ? 26.379  19.045  40.556  1.00 15.06  ? 265 LEU A C     1 
ATOM   2064 O O     . LEU A 1 272 ? 26.868  18.036  41.048  1.00 13.51  ? 265 LEU A O     1 
ATOM   2065 C CB    . LEU A 1 272 ? 25.363  18.454  38.332  1.00 15.91  ? 265 LEU A CB    1 
ATOM   2066 C CG    . LEU A 1 272 ? 25.301  18.639  36.816  1.00 14.93  ? 265 LEU A CG    1 
ATOM   2067 C CD1   . LEU A 1 272 ? 24.214  17.780  36.206  1.00 14.86  ? 265 LEU A CD1   1 
ATOM   2068 C CD2   . LEU A 1 272 ? 25.071  20.086  36.428  1.00 14.95  ? 265 LEU A CD2   1 
ATOM   2069 N N     . PRO A 1 273 ? 25.691  19.917  41.319  1.00 16.16  ? 266 PRO A N     1 
ATOM   2070 C CA    . PRO A 1 273 ? 25.504  19.685  42.748  1.00 17.39  ? 266 PRO A CA    1 
ATOM   2071 C C     . PRO A 1 273 ? 24.776  18.356  42.955  1.00 17.39  ? 266 PRO A C     1 
ATOM   2072 O O     . PRO A 1 273 ? 24.053  17.957  42.066  1.00 16.69  ? 266 PRO A O     1 
ATOM   2073 C CB    . PRO A 1 273 ? 24.631  20.834  43.253  1.00 17.36  ? 266 PRO A CB    1 
ATOM   2074 C CG    . PRO A 1 273 ? 24.669  21.857  42.139  1.00 18.91  ? 266 PRO A CG    1 
ATOM   2075 C CD    . PRO A 1 273 ? 24.976  21.110  40.854  1.00 17.25  ? 266 PRO A CD    1 
ATOM   2076 N N     . HIS A 1 274 ? 25.037  17.702  44.087  1.00 18.61  ? 267 HIS A N     1 
ATOM   2077 C CA    . HIS A 1 274 ? 24.288  16.509  44.560  1.00 19.05  ? 267 HIS A CA    1 
ATOM   2078 C C     . HIS A 1 274 ? 22.803  16.852  44.665  1.00 18.05  ? 267 HIS A C     1 
ATOM   2079 O O     . HIS A 1 274 ? 22.512  17.901  45.284  1.00 17.08  ? 267 HIS A O     1 
ATOM   2080 C CB    . HIS A 1 274 ? 24.813  15.998  45.908  1.00 18.71  ? 267 HIS A CB    1 
ATOM   2081 C CG    . HIS A 1 274 ? 24.011  14.832  46.380  1.00 19.22  ? 267 HIS A CG    1 
ATOM   2082 N ND1   . HIS A 1 274 ? 23.444  14.791  47.615  1.00 19.79  ? 267 HIS A ND1   1 
ATOM   2083 C CD2   . HIS A 1 274 ? 23.606  13.714  45.731  1.00 20.04  ? 267 HIS A CD2   1 
ATOM   2084 C CE1   . HIS A 1 274 ? 22.729  13.680  47.727  1.00 21.87  ? 267 HIS A CE1   1 
ATOM   2085 N NE2   . HIS A 1 274 ? 22.820  13.001  46.576  1.00 21.90  ? 267 HIS A NE2   1 
ATOM   2086 N N     . LYS A 1 275 ? 21.915  16.017  44.106  1.00 18.28  ? 268 LYS A N     1 
ATOM   2087 C CA    . LYS A 1 275 ? 20.440  16.127  44.381  1.00 21.88  ? 268 LYS A CA    1 
ATOM   2088 C C     . LYS A 1 275 ? 19.849  14.751  44.720  1.00 20.32  ? 268 LYS A C     1 
ATOM   2089 O O     . LYS A 1 275 ? 20.076  13.812  43.993  1.00 19.77  ? 268 LYS A O     1 
ATOM   2090 C CB    . LYS A 1 275 ? 19.710  16.832  43.229  1.00 23.46  ? 268 LYS A CB    1 
ATOM   2091 C CG    . LYS A 1 275 ? 19.948  18.338  43.144  1.00 25.20  ? 268 LYS A CG    1 
ATOM   2092 C CD    . LYS A 1 275 ? 20.002  18.896  41.720  1.00 29.04  ? 268 LYS A CD    1 
ATOM   2093 C CE    . LYS A 1 275 ? 21.410  19.032  41.136  1.00 29.92  ? 268 LYS A CE    1 
ATOM   2094 N NZ    . LYS A 1 275 ? 21.834  17.867  40.313  1.00 28.74  ? 268 LYS A NZ    1 
ATOM   2095 N N     . ASN A 1 276 ? 19.102  14.655  45.815  1.00 23.58  ? 269 ASN A N     1 
ATOM   2096 C CA    . ASN A 1 276 ? 18.452  13.390  46.270  1.00 25.09  ? 269 ASN A CA    1 
ATOM   2097 C C     . ASN A 1 276 ? 17.274  13.096  45.334  1.00 25.62  ? 269 ASN A C     1 
ATOM   2098 O O     . ASN A 1 276 ? 16.782  14.040  44.680  1.00 25.34  ? 269 ASN A O     1 
ATOM   2099 C CB    . ASN A 1 276 ? 18.038  13.475  47.741  1.00 26.00  ? 269 ASN A CB    1 
ATOM   2100 C CG    . ASN A 1 276 ? 19.210  13.437  48.699  1.00 26.73  ? 269 ASN A CG    1 
ATOM   2101 O OD1   . ASN A 1 276 ? 20.006  12.498  48.693  1.00 30.14  ? 269 ASN A OD1   1 
ATOM   2102 N ND2   . ASN A 1 276 ? 19.326  14.456  49.529  1.00 30.54  ? 269 ASN A ND2   1 
ATOM   2103 N N     . LYS A 1 277 ? 16.885  11.830  45.218  1.00 28.48  ? 270 LYS A N     1 
ATOM   2104 C CA    . LYS A 1 277 ? 15.767  11.379  44.338  1.00 30.80  ? 270 LYS A CA    1 
ATOM   2105 C C     . LYS A 1 277 ? 14.478  11.963  44.911  1.00 32.32  ? 270 LYS A C     1 
ATOM   2106 O O     . LYS A 1 277 ? 14.281  11.791  46.121  1.00 36.62  ? 270 LYS A O     1 
ATOM   2107 C CB    . LYS A 1 277 ? 15.705  9.842   44.268  1.00 32.36  ? 270 LYS A CB    1 
ATOM   2108 C CG    . LYS A 1 277 ? 14.301  9.251   44.120  1.00 33.74  ? 270 LYS A CG    1 
ATOM   2109 C CD    . LYS A 1 277 ? 14.243  7.758   43.843  1.00 34.06  ? 270 LYS A CD    1 
ATOM   2110 C CE    . LYS A 1 277 ? 13.070  7.364   42.958  1.00 34.19  ? 270 LYS A CE    1 
ATOM   2111 N NZ    . LYS A 1 277 ? 13.287  7.755   41.540  1.00 33.00  ? 270 LYS A NZ    1 
ATOM   2112 N N     . VAL A 1 278 ? 13.638  12.625  44.111  1.00 32.03  ? 271 VAL A N     1 
ATOM   2113 C CA    . VAL A 1 278 ? 12.314  13.091  44.612  1.00 32.35  ? 271 VAL A CA    1 
ATOM   2114 C C     . VAL A 1 278 ? 11.291  12.000  44.327  1.00 34.96  ? 271 VAL A C     1 
ATOM   2115 O O     . VAL A 1 278 ? 11.012  11.668  43.179  1.00 33.20  ? 271 VAL A O     1 
ATOM   2116 C CB    . VAL A 1 278 ? 11.876  14.443  44.044  1.00 29.72  ? 271 VAL A CB    1 
ATOM   2117 C CG1   . VAL A 1 278 ? 10.536  14.848  44.616  1.00 29.12  ? 271 VAL A CG1   1 
ATOM   2118 C CG2   . VAL A 1 278 ? 12.924  15.515  44.306  1.00 30.79  ? 271 VAL A CG2   1 
ATOM   2119 N N     . PRO A 1 279 ? 10.651  11.453  45.381  1.00 37.89  ? 272 PRO A N     1 
ATOM   2120 C CA    . PRO A 1 279 ? 9.982   10.160  45.275  1.00 35.19  ? 272 PRO A CA    1 
ATOM   2121 C C     . PRO A 1 279 ? 8.588   10.463  44.698  1.00 30.08  ? 272 PRO A C     1 
ATOM   2122 O O     . PRO A 1 279 ? 8.078   11.542  44.948  1.00 27.08  ? 272 PRO A O     1 
ATOM   2123 C CB    . PRO A 1 279 ? 10.036  9.715   46.741  1.00 38.25  ? 272 PRO A CB    1 
ATOM   2124 C CG    . PRO A 1 279 ? 9.724   11.018  47.493  1.00 39.56  ? 272 PRO A CG    1 
ATOM   2125 C CD    . PRO A 1 279 ? 10.375  12.117  46.669  1.00 36.49  ? 272 PRO A CD    1 
ATOM   2126 N N     . TRP A 1 280 ? 8.031   9.554   43.896  1.00 27.40  ? 273 TRP A N     1 
ATOM   2127 C CA    . TRP A 1 280 ? 6.890   9.852   42.988  1.00 26.08  ? 273 TRP A CA    1 
ATOM   2128 C C     . TRP A 1 280 ? 5.635   10.236  43.789  1.00 27.94  ? 273 TRP A C     1 
ATOM   2129 O O     . TRP A 1 280 ? 4.823   11.101  43.302  1.00 25.56  ? 273 TRP A O     1 
ATOM   2130 C CB    . TRP A 1 280 ? 6.658   8.676   42.038  1.00 24.46  ? 273 TRP A CB    1 
ATOM   2131 C CG    . TRP A 1 280 ? 7.803   8.498   41.090  1.00 21.83  ? 273 TRP A CG    1 
ATOM   2132 C CD1   . TRP A 1 280 ? 8.728   7.500   41.052  1.00 21.16  ? 273 TRP A CD1   1 
ATOM   2133 C CD2   . TRP A 1 280 ? 8.140   9.399   40.030  1.00 21.06  ? 273 TRP A CD2   1 
ATOM   2134 N NE1   . TRP A 1 280 ? 9.635   7.742   40.054  1.00 23.00  ? 273 TRP A NE1   1 
ATOM   2135 C CE2   . TRP A 1 280 ? 9.296   8.896   39.411  1.00 20.36  ? 273 TRP A CE2   1 
ATOM   2136 C CE3   . TRP A 1 280 ? 7.611   10.616  39.607  1.00 21.91  ? 273 TRP A CE3   1 
ATOM   2137 C CZ2   . TRP A 1 280 ? 9.902   9.549   38.353  1.00 21.53  ? 273 TRP A CZ2   1 
ATOM   2138 C CZ3   . TRP A 1 280 ? 8.207   11.257  38.546  1.00 22.81  ? 273 TRP A CZ3   1 
ATOM   2139 C CH2   . TRP A 1 280 ? 9.348   10.736  37.939  1.00 21.23  ? 273 TRP A CH2   1 
ATOM   2140 N N     . ASN A 1 281 ? 5.487   9.660   44.985  1.00 30.71  ? 274 ASN A N     1 
ATOM   2141 C CA    . ASN A 1 281 ? 4.284   9.854   45.835  1.00 35.38  ? 274 ASN A CA    1 
ATOM   2142 C C     . ASN A 1 281 ? 4.190   11.337  46.213  1.00 36.67  ? 274 ASN A C     1 
ATOM   2143 O O     . ASN A 1 281 ? 3.056   11.872  46.217  1.00 38.81  ? 274 ASN A O     1 
ATOM   2144 C CB    . ASN A 1 281 ? 4.238   8.876   47.012  1.00 35.62  ? 274 ASN A CB    1 
ATOM   2145 C CG    . ASN A 1 281 ? 5.173   9.232   48.149  1.00 38.29  ? 274 ASN A CG    1 
ATOM   2146 O OD1   . ASN A 1 281 ? 4.731   9.343   49.288  1.00 43.04  ? 274 ASN A OD1   1 
ATOM   2147 N ND2   . ASN A 1 281 ? 6.457   9.389   47.872  1.00 33.11  ? 274 ASN A ND2   1 
ATOM   2148 N N     . ARG A 1 282 ? 5.312   12.019  46.445  1.00 39.96  ? 275 ARG A N     1 
ATOM   2149 C CA    . ARG A 1 282 ? 5.233   13.461  46.811  1.00 43.60  ? 275 ARG A CA    1 
ATOM   2150 C C     . ARG A 1 282 ? 4.930   14.310  45.565  1.00 38.16  ? 275 ARG A C     1 
ATOM   2151 O O     . ARG A 1 282 ? 4.356   15.373  45.742  1.00 39.36  ? 275 ARG A O     1 
ATOM   2152 C CB    . ARG A 1 282 ? 6.450   13.968  47.596  1.00 49.17  ? 275 ARG A CB    1 
ATOM   2153 C CG    . ARG A 1 282 ? 6.031   14.831  48.789  1.00 54.77  ? 275 ARG A CG    1 
ATOM   2154 C CD    . ARG A 1 282 ? 6.794   16.122  49.062  1.00 55.21  ? 275 ARG A CD    1 
ATOM   2155 N NE    . ARG A 1 282 ? 7.546   16.070  50.310  1.00 56.80  ? 275 ARG A NE    1 
ATOM   2156 C CZ    . ARG A 1 282 ? 8.852   15.815  50.416  1.00 59.45  ? 275 ARG A CZ    1 
ATOM   2157 N NH1   . ARG A 1 282 ? 9.597   15.586  49.345  1.00 54.09  ? 275 ARG A NH1   1 
ATOM   2158 N NH2   . ARG A 1 282 ? 9.415   15.793  51.613  1.00 61.09  ? 275 ARG A NH2   1 
ATOM   2159 N N     . LEU A 1 283 ? 5.248   13.860  44.348  1.00 37.40  ? 276 LEU A N     1 
ATOM   2160 C CA    . LEU A 1 283 ? 4.857   14.584  43.103  1.00 32.64  ? 276 LEU A CA    1 
ATOM   2161 C C     . LEU A 1 283 ? 3.381   14.318  42.783  1.00 32.58  ? 276 LEU A C     1 
ATOM   2162 O O     . LEU A 1 283 ? 2.732   15.219  42.204  1.00 24.85  ? 276 LEU A O     1 
ATOM   2163 C CB    . LEU A 1 283 ? 5.740   14.148  41.928  1.00 31.81  ? 276 LEU A CB    1 
ATOM   2164 C CG    . LEU A 1 283 ? 7.124   14.796  41.813  1.00 32.14  ? 276 LEU A CG    1 
ATOM   2165 C CD1   . LEU A 1 283 ? 7.940   14.071  40.758  1.00 30.39  ? 276 LEU A CD1   1 
ATOM   2166 C CD2   . LEU A 1 283 ? 7.032   16.288  41.473  1.00 32.70  ? 276 LEU A CD2   1 
ATOM   2167 N N     . PHE A 1 284 ? 2.900   13.098  43.074  1.00 35.47  ? 277 PHE A N     1 
ATOM   2168 C CA    . PHE A 1 284 ? 1.549   12.605  42.694  1.00 35.64  ? 277 PHE A CA    1 
ATOM   2169 C C     . PHE A 1 284 ? 0.931   11.868  43.872  1.00 37.47  ? 277 PHE A C     1 
ATOM   2170 O O     . PHE A 1 284 ? 0.879   10.637  43.875  1.00 32.58  ? 277 PHE A O     1 
ATOM   2171 C CB    . PHE A 1 284 ? 1.640   11.658  41.496  1.00 37.17  ? 277 PHE A CB    1 
ATOM   2172 C CG    . PHE A 1 284 ? 2.435   12.171  40.320  1.00 34.92  ? 277 PHE A CG    1 
ATOM   2173 C CD1   . PHE A 1 284 ? 1.887   13.094  39.440  1.00 33.87  ? 277 PHE A CD1   1 
ATOM   2174 C CD2   . PHE A 1 284 ? 3.704   11.683  40.057  1.00 30.74  ? 277 PHE A CD2   1 
ATOM   2175 C CE1   . PHE A 1 284 ? 2.602   13.528  38.330  1.00 32.81  ? 277 PHE A CE1   1 
ATOM   2176 C CE2   . PHE A 1 284 ? 4.415   12.126  38.946  1.00 34.54  ? 277 PHE A CE2   1 
ATOM   2177 C CZ    . PHE A 1 284 ? 3.868   13.053  38.091  1.00 31.81  ? 277 PHE A CZ    1 
ATOM   2178 N N     . PRO A 1 285 ? 0.443   12.601  44.902  1.00 42.93  ? 278 PRO A N     1 
ATOM   2179 C CA    . PRO A 1 285 ? -0.105  11.976  46.112  1.00 41.31  ? 278 PRO A CA    1 
ATOM   2180 C C     . PRO A 1 285 ? -1.462  11.282  45.883  1.00 37.33  ? 278 PRO A C     1 
ATOM   2181 O O     . PRO A 1 285 ? -1.796  10.441  46.671  1.00 39.37  ? 278 PRO A O     1 
ATOM   2182 C CB    . PRO A 1 285 ? -0.206  13.169  47.087  1.00 42.17  ? 278 PRO A CB    1 
ATOM   2183 C CG    . PRO A 1 285 ? -0.477  14.360  46.184  1.00 42.65  ? 278 PRO A CG    1 
ATOM   2184 C CD    . PRO A 1 285 ? 0.314   14.070  44.920  1.00 44.42  ? 278 PRO A CD    1 
ATOM   2185 N N     . ASN A 1 286 ? -2.181  11.637  44.809  1.00 38.37  ? 279 ASN A N     1 
ATOM   2186 C CA    . ASN A 1 286 ? -3.503  11.060  44.423  1.00 41.72  ? 279 ASN A CA    1 
ATOM   2187 C C     . ASN A 1 286 ? -3.370  9.825   43.516  1.00 36.63  ? 279 ASN A C     1 
ATOM   2188 O O     . ASN A 1 286 ? -4.422  9.256   43.195  1.00 43.13  ? 279 ASN A O     1 
ATOM   2189 C CB    . ASN A 1 286 ? -4.396  11.991  43.594  1.00 45.81  ? 279 ASN A CB    1 
ATOM   2190 C CG    . ASN A 1 286 ? -4.374  13.445  44.003  1.00 52.43  ? 279 ASN A CG    1 
ATOM   2191 O OD1   . ASN A 1 286 ? -4.600  14.329  43.167  1.00 52.87  ? 279 ASN A OD1   1 
ATOM   2192 N ND2   . ASN A 1 286 ? -4.109  13.698  45.275  1.00 54.44  ? 279 ASN A ND2   1 
ATOM   2193 N N     . ALA A 1 287 ? -2.169  9.437   43.080  1.00 31.51  ? 280 ALA A N     1 
ATOM   2194 C CA    . ALA A 1 287 ? -1.981  8.351   42.080  1.00 27.92  ? 280 ALA A CA    1 
ATOM   2195 C C     . ALA A 1 287 ? -2.065  6.958   42.738  1.00 23.82  ? 280 ALA A C     1 
ATOM   2196 O O     . ALA A 1 287 ? -1.702  6.783   43.899  1.00 19.52  ? 280 ALA A O     1 
ATOM   2197 C CB    . ALA A 1 287 ? -0.684  8.534   41.352  1.00 25.76  ? 280 ALA A CB    1 
ATOM   2198 N N     . ASP A 1 288 ? -2.565  6.006   41.975  1.00 23.59  ? 281 ASP A N     1 
ATOM   2199 C CA    . ASP A 1 288 ? -2.445  4.544   42.208  1.00 26.38  ? 281 ASP A CA    1 
ATOM   2200 C C     . ASP A 1 288 ? -0.969  4.208   42.466  1.00 25.29  ? 281 ASP A C     1 
ATOM   2201 O O     . ASP A 1 288 ? -0.129  4.548   41.621  1.00 26.94  ? 281 ASP A O     1 
ATOM   2202 C CB    . ASP A 1 288 ? -2.990  3.812   40.979  1.00 28.68  ? 281 ASP A CB    1 
ATOM   2203 C CG    . ASP A 1 288 ? -3.279  2.345   41.198  1.00 30.45  ? 281 ASP A CG    1 
ATOM   2204 O OD1   . ASP A 1 288 ? -2.594  1.732   42.030  1.00 31.14  ? 281 ASP A OD1   1 
ATOM   2205 O OD2   . ASP A 1 288 ? -4.156  1.829   40.487  1.00 32.26  ? 281 ASP A OD2   1 
ATOM   2206 N N     . SER A 1 289 ? -0.654  3.580   43.593  1.00 21.88  ? 282 SER A N     1 
ATOM   2207 C CA    . SER A 1 289 ? 0.734   3.215   43.948  1.00 21.69  ? 282 SER A CA    1 
ATOM   2208 C C     . SER A 1 289 ? 1.319   2.291   42.865  1.00 20.36  ? 282 SER A C     1 
ATOM   2209 O O     . SER A 1 289 ? 2.524   2.328   42.672  1.00 20.28  ? 282 SER A O     1 
ATOM   2210 C CB    . SER A 1 289 ? 0.770   2.572   45.295  1.00 20.77  ? 282 SER A CB    1 
ATOM   2211 O OG    . SER A 1 289 ? -0.266  1.589   45.378  1.00 23.27  ? 282 SER A OG    1 
ATOM   2212 N N     . LYS A 1 290 ? 0.515   1.436   42.235  1.00 20.54  ? 283 LYS A N     1 
ATOM   2213 C CA    . LYS A 1 290 ? 1.035   0.503   41.192  1.00 22.00  ? 283 LYS A CA    1 
ATOM   2214 C C     . LYS A 1 290 ? 1.447   1.344   39.976  1.00 18.69  ? 283 LYS A C     1 
ATOM   2215 O O     . LYS A 1 290 ? 2.487   1.050   39.382  1.00 17.85  ? 283 LYS A O     1 
ATOM   2216 C CB    . LYS A 1 290 ? 0.006   -0.593  40.906  1.00 23.10  ? 283 LYS A CB    1 
ATOM   2217 C CG    . LYS A 1 290 ? -0.370  -1.380  42.154  1.00 27.00  ? 283 LYS A CG    1 
ATOM   2218 C CD    . LYS A 1 290 ? -1.215  -2.611  41.923  1.00 29.58  ? 283 LYS A CD    1 
ATOM   2219 C CE    . LYS A 1 290 ? -1.544  -3.298  43.233  1.00 33.66  ? 283 LYS A CE    1 
ATOM   2220 N NZ    . LYS A 1 290 ? -2.624  -4.314  43.104  1.00 36.85  ? 283 LYS A NZ    1 
ATOM   2221 N N     . ALA A 1 291 ? 0.707   2.412   39.681  1.00 17.71  ? 284 ALA A N     1 
ATOM   2222 C CA    . ALA A 1 291 ? 1.030   3.374   38.594  1.00 18.39  ? 284 ALA A CA    1 
ATOM   2223 C C     . ALA A 1 291 ? 2.398   4.023   38.836  1.00 18.01  ? 284 ALA A C     1 
ATOM   2224 O O     . ALA A 1 291 ? 3.193   4.148   37.845  1.00 17.15  ? 284 ALA A O     1 
ATOM   2225 C CB    . ALA A 1 291 ? -0.046  4.419   38.466  1.00 18.57  ? 284 ALA A CB    1 
ATOM   2226 N N     . LEU A 1 292 ? 2.659   4.439   40.081  1.00 15.80  ? 285 LEU A N     1 
ATOM   2227 C CA    . LEU A 1 292 ? 3.897   5.165   40.471  1.00 15.02  ? 285 LEU A CA    1 
ATOM   2228 C C     . LEU A 1 292 ? 5.061   4.186   40.413  1.00 14.48  ? 285 LEU A C     1 
ATOM   2229 O O     . LEU A 1 292 ? 6.151   4.551   40.031  1.00 13.50  ? 285 LEU A O     1 
ATOM   2230 C CB    . LEU A 1 292 ? 3.723   5.740   41.882  1.00 14.78  ? 285 LEU A CB    1 
ATOM   2231 C CG    . LEU A 1 292 ? 2.660   6.833   42.012  1.00 14.54  ? 285 LEU A CG    1 
ATOM   2232 C CD1   . LEU A 1 292 ? 2.835   7.653   43.303  1.00 13.91  ? 285 LEU A CD1   1 
ATOM   2233 C CD2   . LEU A 1 292 ? 2.679   7.748   40.827  1.00 14.25  ? 285 LEU A CD2   1 
ATOM   2234 N N     . ASP A 1 293 ? 4.800   2.945   40.771  1.00 15.39  ? 286 ASP A N     1 
ATOM   2235 C CA    . ASP A 1 293 ? 5.804   1.875   40.649  1.00 15.90  ? 286 ASP A CA    1 
ATOM   2236 C C     . ASP A 1 293 ? 6.207   1.688   39.180  1.00 16.22  ? 286 ASP A C     1 
ATOM   2237 O O     . ASP A 1 293 ? 7.415   1.495   38.921  1.00 17.70  ? 286 ASP A O     1 
ATOM   2238 C CB    . ASP A 1 293 ? 5.261   0.584   41.238  1.00 16.47  ? 286 ASP A CB    1 
ATOM   2239 C CG    . ASP A 1 293 ? 6.390   -0.407  41.343  1.00 16.98  ? 286 ASP A CG    1 
ATOM   2240 O OD1   . ASP A 1 293 ? 7.108   -0.296  42.315  1.00 18.13  ? 286 ASP A OD1   1 
ATOM   2241 O OD2   . ASP A 1 293 ? 6.582   -1.207  40.388  1.00 16.77  ? 286 ASP A OD2   1 
ATOM   2242 N N     . LEU A 1 294 ? 5.245   1.681   38.257  1.00 15.53  ? 287 LEU A N     1 
ATOM   2243 C CA    . LEU A 1 294 ? 5.540   1.430   36.829  1.00 16.10  ? 287 LEU A CA    1 
ATOM   2244 C C     . LEU A 1 294 ? 6.227   2.680   36.264  1.00 15.52  ? 287 LEU A C     1 
ATOM   2245 O O     . LEU A 1 294 ? 7.210   2.553   35.501  1.00 14.32  ? 287 LEU A O     1 
ATOM   2246 C CB    . LEU A 1 294 ? 4.250   1.097   36.081  1.00 16.06  ? 287 LEU A CB    1 
ATOM   2247 C CG    . LEU A 1 294 ? 4.430   0.903   34.575  1.00 16.14  ? 287 LEU A CG    1 
ATOM   2248 C CD1   . LEU A 1 294 ? 5.595   -0.043  34.266  1.00 17.12  ? 287 LEU A CD1   1 
ATOM   2249 C CD2   . LEU A 1 294 ? 3.159   0.348   33.963  1.00 15.91  ? 287 LEU A CD2   1 
ATOM   2250 N N     . LEU A 1 295 ? 5.763   3.854   36.693  1.00 15.57  ? 288 LEU A N     1 
ATOM   2251 C CA    . LEU A 1 295 ? 6.338   5.153   36.276  1.00 15.07  ? 288 LEU A CA    1 
ATOM   2252 C C     . LEU A 1 295 ? 7.830   5.095   36.564  1.00 15.36  ? 288 LEU A C     1 
ATOM   2253 O O     . LEU A 1 295 ? 8.610   5.421   35.669  1.00 16.04  ? 288 LEU A O     1 
ATOM   2254 C CB    . LEU A 1 295 ? 5.669   6.306   37.023  1.00 14.87  ? 288 LEU A CB    1 
ATOM   2255 C CG    . LEU A 1 295 ? 6.220   7.700   36.710  1.00 14.91  ? 288 LEU A CG    1 
ATOM   2256 C CD1   . LEU A 1 295 ? 6.010   8.028   35.242  1.00 15.47  ? 288 LEU A CD1   1 
ATOM   2257 C CD2   . LEU A 1 295 ? 5.576   8.763   37.600  1.00 14.53  ? 288 LEU A CD2   1 
ATOM   2258 N N     . ASP A 1 296 ? 8.190   4.588   37.743  1.00 16.33  ? 289 ASP A N     1 
ATOM   2259 C CA    . ASP A 1 296 ? 9.577   4.591   38.278  1.00 16.03  ? 289 ASP A CA    1 
ATOM   2260 C C     . ASP A 1 296 ? 10.469  3.795   37.316  1.00 16.88  ? 289 ASP A C     1 
ATOM   2261 O O     . ASP A 1 296 ? 11.541  4.302   36.970  1.00 16.23  ? 289 ASP A O     1 
ATOM   2262 C CB    . ASP A 1 296 ? 9.556   4.032   39.698  1.00 16.92  ? 289 ASP A CB    1 
ATOM   2263 C CG    . ASP A 1 296 ? 10.905  4.058   40.382  1.00 17.37  ? 289 ASP A CG    1 
ATOM   2264 O OD1   . ASP A 1 296 ? 11.420  5.157   40.602  1.00 18.98  ? 289 ASP A OD1   1 
ATOM   2265 O OD2   . ASP A 1 296 ? 11.446  2.977   40.632  1.00 19.25  ? 289 ASP A OD2   1 
ATOM   2266 N N     . LYS A 1 297 ? 9.998   2.612   36.884  1.00 15.67  ? 290 LYS A N     1 
ATOM   2267 C CA    . LYS A 1 297 ? 10.737  1.649   36.045  1.00 15.90  ? 290 LYS A CA    1 
ATOM   2268 C C     . LYS A 1 297 ? 10.896  2.201   34.624  1.00 15.65  ? 290 LYS A C     1 
ATOM   2269 O O     . LYS A 1 297 ? 11.923  1.925   33.996  1.00 14.78  ? 290 LYS A O     1 
ATOM   2270 C CB    . LYS A 1 297 ? 10.018  0.304   36.058  1.00 16.27  ? 290 LYS A CB    1 
ATOM   2271 C CG    . LYS A 1 297 ? 10.167  -0.450  37.377  1.00 17.41  ? 290 LYS A CG    1 
ATOM   2272 C CD    . LYS A 1 297 ? 9.014   -1.414  37.596  1.00 18.61  ? 290 LYS A CD    1 
ATOM   2273 C CE    . LYS A 1 297 ? 9.406   -2.687  38.294  1.00 20.07  ? 290 LYS A CE    1 
ATOM   2274 N NZ    . LYS A 1 297 ? 10.093  -2.443  39.583  1.00 21.85  ? 290 LYS A NZ    1 
ATOM   2275 N N     . MET A 1 298 ? 9.936   3.015   34.190  1.00 14.91  ? 291 MET A N     1 
ATOM   2276 C CA    . MET A 1 298 ? 9.900   3.614   32.846  1.00 14.74  ? 291 MET A CA    1 
ATOM   2277 C C     . MET A 1 298 ? 10.842  4.819   32.855  1.00 15.24  ? 291 MET A C     1 
ATOM   2278 O O     . MET A 1 298 ? 11.600  5.028   31.859  1.00 15.11  ? 291 MET A O     1 
ATOM   2279 C CB    . MET A 1 298 ? 8.475   4.019   32.480  1.00 15.59  ? 291 MET A CB    1 
ATOM   2280 C CG    . MET A 1 298 ? 7.540   2.822   32.338  1.00 16.56  ? 291 MET A CG    1 
ATOM   2281 S SD    . MET A 1 298 ? 6.010   3.272   31.551  1.00 18.60  ? 291 MET A SD    1 
ATOM   2282 C CE    . MET A 1 298 ? 5.795   1.887   30.453  1.00 20.84  ? 291 MET A CE    1 
ATOM   2283 N N     . LEU A 1 299 ? 10.871  5.554   33.960  1.00 14.01  ? 292 LEU A N     1 
ATOM   2284 C CA    . LEU A 1 299 ? 11.750  6.736   34.060  1.00 13.69  ? 292 LEU A CA    1 
ATOM   2285 C C     . LEU A 1 299 ? 12.960  6.371   34.917  1.00 14.48  ? 292 LEU A C     1 
ATOM   2286 O O     . LEU A 1 299 ? 13.147  7.003   35.958  1.00 15.21  ? 292 LEU A O     1 
ATOM   2287 C CB    . LEU A 1 299 ? 10.935  7.901   34.613  1.00 13.62  ? 292 LEU A CB    1 
ATOM   2288 C CG    . LEU A 1 299 ? 9.777   8.310   33.714  1.00 13.38  ? 292 LEU A CG    1 
ATOM   2289 C CD1   . LEU A 1 299 ? 8.996   9.464   34.311  1.00 13.33  ? 292 LEU A CD1   1 
ATOM   2290 C CD2   . LEU A 1 299 ? 10.284  8.667   32.323  1.00 13.49  ? 292 LEU A CD2   1 
ATOM   2291 N N     . THR A 1 300 ? 13.701  5.361   34.468  1.00 14.81  ? 293 THR A N     1 
ATOM   2292 C CA    . THR A 1 300 ? 15.008  4.936   34.996  1.00 15.79  ? 293 THR A CA    1 
ATOM   2293 C C     . THR A 1 300 ? 16.039  5.705   34.195  1.00 15.75  ? 293 THR A C     1 
ATOM   2294 O O     . THR A 1 300 ? 15.906  5.778   32.954  1.00 14.69  ? 293 THR A O     1 
ATOM   2295 C CB    . THR A 1 300 ? 15.207  3.418   34.901  1.00 16.91  ? 293 THR A CB    1 
ATOM   2296 O OG1   . THR A 1 300 ? 14.083  2.829   35.540  1.00 19.50  ? 293 THR A OG1   1 
ATOM   2297 C CG2   . THR A 1 300 ? 16.439  2.912   35.606  1.00 17.52  ? 293 THR A CG2   1 
ATOM   2298 N N     . PHE A 1 301 ? 16.996  6.299   34.887  1.00 15.77  ? 294 PHE A N     1 
ATOM   2299 C CA    . PHE A 1 301 ? 18.074  7.090   34.255  1.00 17.06  ? 294 PHE A CA    1 
ATOM   2300 C C     . PHE A 1 301 ? 18.834  6.170   33.290  1.00 16.96  ? 294 PHE A C     1 
ATOM   2301 O O     . PHE A 1 301 ? 19.048  6.547   32.132  1.00 15.43  ? 294 PHE A O     1 
ATOM   2302 C CB    . PHE A 1 301 ? 19.007  7.679   35.311  1.00 17.64  ? 294 PHE A CB    1 
ATOM   2303 C CG    . PHE A 1 301 ? 20.153  8.415   34.686  1.00 18.98  ? 294 PHE A CG    1 
ATOM   2304 C CD1   . PHE A 1 301 ? 19.999  9.740   34.295  1.00 18.30  ? 294 PHE A CD1   1 
ATOM   2305 C CD2   . PHE A 1 301 ? 21.340  7.745   34.391  1.00 18.98  ? 294 PHE A CD2   1 
ATOM   2306 C CE1   . PHE A 1 301 ? 21.050  10.413  33.698  1.00 18.95  ? 294 PHE A CE1   1 
ATOM   2307 C CE2   . PHE A 1 301 ? 22.378  8.413   33.767  1.00 19.45  ? 294 PHE A CE2   1 
ATOM   2308 C CZ    . PHE A 1 301 ? 22.228  9.744   33.422  1.00 20.01  ? 294 PHE A CZ    1 
ATOM   2309 N N     . ASN A 1 302 ? 19.124  4.955   33.754  1.00 17.75  ? 295 ASN A N     1 
ATOM   2310 C CA    . ASN A 1 302 ? 19.954  3.960   33.033  1.00 18.55  ? 295 ASN A CA    1 
ATOM   2311 C C     . ASN A 1 302 ? 19.087  3.224   32.026  1.00 18.26  ? 295 ASN A C     1 
ATOM   2312 O O     . ASN A 1 302 ? 18.190  2.466   32.399  1.00 17.28  ? 295 ASN A O     1 
ATOM   2313 C CB    . ASN A 1 302 ? 20.611  2.944   33.960  1.00 18.50  ? 295 ASN A CB    1 
ATOM   2314 C CG    . ASN A 1 302 ? 21.681  2.138   33.258  1.00 21.04  ? 295 ASN A CG    1 
ATOM   2315 O OD1   . ASN A 1 302 ? 21.653  1.956   32.045  1.00 20.58  ? 295 ASN A OD1   1 
ATOM   2316 N ND2   . ASN A 1 302 ? 22.655  1.669   34.017  1.00 23.21  ? 295 ASN A ND2   1 
ATOM   2317 N N     . PRO A 1 303 ? 19.374  3.415   30.726  1.00 16.87  ? 296 PRO A N     1 
ATOM   2318 C CA    . PRO A 1 303 ? 18.583  2.781   29.681  1.00 18.71  ? 296 PRO A CA    1 
ATOM   2319 C C     . PRO A 1 303 ? 18.580  1.245   29.785  1.00 18.77  ? 296 PRO A C     1 
ATOM   2320 O O     . PRO A 1 303 ? 17.611  0.654   29.406  1.00 19.86  ? 296 PRO A O     1 
ATOM   2321 C CB    . PRO A 1 303 ? 19.191  3.245   28.342  1.00 17.07  ? 296 PRO A CB    1 
ATOM   2322 C CG    . PRO A 1 303 ? 20.413  4.094   28.704  1.00 17.56  ? 296 PRO A CG    1 
ATOM   2323 C CD    . PRO A 1 303 ? 20.468  4.250   30.214  1.00 16.92  ? 296 PRO A CD    1 
ATOM   2324 N N     . HIS A 1 304 ? 19.663  0.647   30.276  1.00 18.40  ? 297 HIS A N     1 
ATOM   2325 C CA    . HIS A 1 304 ? 19.834  -0.817  30.371  1.00 19.44  ? 297 HIS A CA    1 
ATOM   2326 C C     . HIS A 1 304 ? 18.950  -1.334  31.531  1.00 18.70  ? 297 HIS A C     1 
ATOM   2327 O O     . HIS A 1 304 ? 18.503  -2.459  31.470  1.00 21.12  ? 297 HIS A O     1 
ATOM   2328 C CB    . HIS A 1 304 ? 21.339  -1.136  30.511  1.00 22.34  ? 297 HIS A CB    1 
ATOM   2329 C CG    . HIS A 1 304 ? 22.210  -0.659  29.389  1.00 25.07  ? 297 HIS A CG    1 
ATOM   2330 N ND1   . HIS A 1 304 ? 22.910  0.553   29.439  1.00 28.05  ? 297 HIS A ND1   1 
ATOM   2331 C CD2   . HIS A 1 304 ? 22.532  -1.219  28.194  1.00 27.52  ? 297 HIS A CD2   1 
ATOM   2332 C CE1   . HIS A 1 304 ? 23.616  0.712   28.331  1.00 27.53  ? 297 HIS A CE1   1 
ATOM   2333 N NE2   . HIS A 1 304 ? 23.404  -0.353  27.545  1.00 27.29  ? 297 HIS A NE2   1 
ATOM   2334 N N     . LYS A 1 305 ? 18.634  -0.506  32.517  1.00 16.82  ? 298 LYS A N     1 
ATOM   2335 C CA    . LYS A 1 305 ? 17.798  -0.883  33.698  1.00 17.46  ? 298 LYS A CA    1 
ATOM   2336 C C     . LYS A 1 305 ? 16.327  -0.550  33.465  1.00 14.86  ? 298 LYS A C     1 
ATOM   2337 O O     . LYS A 1 305 ? 15.496  -1.005  34.252  1.00 15.46  ? 298 LYS A O     1 
ATOM   2338 C CB    . LYS A 1 305 ? 18.270  -0.139  34.942  1.00 17.42  ? 298 LYS A CB    1 
ATOM   2339 C CG    . LYS A 1 305 ? 19.675  -0.516  35.373  1.00 19.43  ? 298 LYS A CG    1 
ATOM   2340 C CD    . LYS A 1 305 ? 19.963  -0.111  36.798  1.00 21.18  ? 298 LYS A CD    1 
ATOM   2341 C CE    . LYS A 1 305 ? 21.433  -0.140  37.152  1.00 22.30  ? 298 LYS A CE    1 
ATOM   2342 N NZ    . LYS A 1 305 ? 21.741  0.921   38.138  1.00 25.07  ? 298 LYS A NZ    1 
ATOM   2343 N N     . ARG A 1 306 ? 16.035  0.185   32.403  1.00 12.88  ? 299 ARG A N     1 
ATOM   2344 C CA    . ARG A 1 306 ? 14.690  0.695   32.088  1.00 12.64  ? 299 ARG A CA    1 
ATOM   2345 C C     . ARG A 1 306 ? 13.859  -0.507  31.652  1.00 12.90  ? 299 ARG A C     1 
ATOM   2346 O O     . ARG A 1 306 ? 14.379  -1.308  30.903  1.00 13.02  ? 299 ARG A O     1 
ATOM   2347 C CB    . ARG A 1 306 ? 14.778  1.774   31.005  1.00 12.04  ? 299 ARG A CB    1 
ATOM   2348 C CG    . ARG A 1 306 ? 13.582  2.712   30.958  1.00 12.57  ? 299 ARG A CG    1 
ATOM   2349 C CD    . ARG A 1 306 ? 13.797  3.818   29.944  1.00 12.04  ? 299 ARG A CD    1 
ATOM   2350 N NE    . ARG A 1 306 ? 14.866  4.673   30.394  1.00 12.00  ? 299 ARG A NE    1 
ATOM   2351 C CZ    . ARG A 1 306 ? 15.743  5.293   29.621  1.00 12.45  ? 299 ARG A CZ    1 
ATOM   2352 N NH1   . ARG A 1 306 ? 15.681  5.204   28.300  1.00 13.00  ? 299 ARG A NH1   1 
ATOM   2353 N NH2   . ARG A 1 306 ? 16.714  5.981   30.190  1.00 12.55  ? 299 ARG A NH2   1 
ATOM   2354 N N     . ILE A 1 307 ? 12.643  -0.628  32.179  1.00 13.17  ? 300 ILE A N     1 
ATOM   2355 C CA    . ILE A 1 307 ? 11.644  -1.672  31.832  1.00 13.54  ? 300 ILE A CA    1 
ATOM   2356 C C     . ILE A 1 307 ? 11.412  -1.638  30.318  1.00 15.25  ? 300 ILE A C     1 
ATOM   2357 O O     . ILE A 1 307 ? 11.401  -0.510  29.742  1.00 14.87  ? 300 ILE A O     1 
ATOM   2358 C CB    . ILE A 1 307 ? 10.355  -1.442  32.629  1.00 13.27  ? 300 ILE A CB    1 
ATOM   2359 C CG1   . ILE A 1 307 ? 9.448   -2.676  32.596  1.00 13.78  ? 300 ILE A CG1   1 
ATOM   2360 C CG2   . ILE A 1 307 ? 9.618   -0.179  32.176  1.00 12.95  ? 300 ILE A CG2   1 
ATOM   2361 C CD1   . ILE A 1 307 ? 8.375   -2.663  33.677  1.00 14.22  ? 300 ILE A CD1   1 
ATOM   2362 N N     . GLU A 1 308 ? 11.299  -2.822  29.701  1.00 15.66  ? 301 GLU A N     1 
ATOM   2363 C CA    . GLU A 1 308 ? 10.941  -2.978  28.271  1.00 17.57  ? 301 GLU A CA    1 
ATOM   2364 C C     . GLU A 1 308 ? 9.436   -3.145  28.170  1.00 15.35  ? 301 GLU A C     1 
ATOM   2365 O O     . GLU A 1 308 ? 8.765   -3.313  29.201  1.00 15.19  ? 301 GLU A O     1 
ATOM   2366 C CB    . GLU A 1 308 ? 11.656  -4.149  27.587  1.00 22.54  ? 301 GLU A CB    1 
ATOM   2367 C CG    . GLU A 1 308 ? 13.086  -4.374  28.063  1.00 26.01  ? 301 GLU A CG    1 
ATOM   2368 C CD    . GLU A 1 308 ? 14.114  -4.517  26.952  1.00 32.96  ? 301 GLU A CD    1 
ATOM   2369 O OE1   . GLU A 1 308 ? 15.338  -4.495  27.245  1.00 33.50  ? 301 GLU A OE1   1 
ATOM   2370 O OE2   . GLU A 1 308 ? 13.692  -4.602  25.789  1.00 44.34  ? 301 GLU A OE2   1 
ATOM   2371 N N     . VAL A 1 309 ? 8.930   -3.091  26.947  1.00 14.19  ? 302 VAL A N     1 
ATOM   2372 C CA    . VAL A 1 309 ? 7.486   -2.899  26.654  1.00 14.32  ? 302 VAL A CA    1 
ATOM   2373 C C     . VAL A 1 309 ? 6.702   -4.084  27.225  1.00 14.94  ? 302 VAL A C     1 
ATOM   2374 O O     . VAL A 1 309 ? 5.627   -3.870  27.818  1.00 15.55  ? 302 VAL A O     1 
ATOM   2375 C CB    . VAL A 1 309 ? 7.238   -2.649  25.151  1.00 13.49  ? 302 VAL A CB    1 
ATOM   2376 C CG1   . VAL A 1 309 ? 7.601   -3.844  24.269  1.00 14.59  ? 302 VAL A CG1   1 
ATOM   2377 C CG2   . VAL A 1 309 ? 5.808   -2.227  24.887  1.00 13.47  ? 302 VAL A CG2   1 
ATOM   2378 N N     . GLU A 1 310 ? 7.241   -5.293  27.129  1.00 16.48  ? 303 GLU A N     1 
ATOM   2379 C CA    . GLU A 1 310 ? 6.475   -6.506  27.508  1.00 18.83  ? 303 GLU A CA    1 
ATOM   2380 C C     . GLU A 1 310 ? 6.402   -6.568  29.040  1.00 17.94  ? 303 GLU A C     1 
ATOM   2381 O O     . GLU A 1 310 ? 5.355   -6.980  29.561  1.00 15.63  ? 303 GLU A O     1 
ATOM   2382 C CB    . GLU A 1 310 ? 7.051   -7.718  26.775  1.00 22.52  ? 303 GLU A CB    1 
ATOM   2383 C CG    . GLU A 1 310 ? 6.953   -7.566  25.260  1.00 25.66  ? 303 GLU A CG    1 
ATOM   2384 C CD    . GLU A 1 310 ? 7.777   -8.530  24.435  1.00 31.85  ? 303 GLU A CD    1 
ATOM   2385 O OE1   . GLU A 1 310 ? 7.499   -9.763  24.506  1.00 32.29  ? 303 GLU A OE1   1 
ATOM   2386 O OE2   . GLU A 1 310 ? 8.689   -8.049  23.715  1.00 35.76  ? 303 GLU A OE2   1 
ATOM   2387 N N     . GLN A 1 311 ? 7.446   -6.101  29.734  1.00 16.72  ? 304 GLN A N     1 
ATOM   2388 C CA    . GLN A 1 311 ? 7.472   -6.105  31.207  1.00 16.73  ? 304 GLN A CA    1 
ATOM   2389 C C     . GLN A 1 311 ? 6.455   -5.068  31.680  1.00 16.01  ? 304 GLN A C     1 
ATOM   2390 O O     . GLN A 1 311 ? 5.679   -5.388  32.563  1.00 15.33  ? 304 GLN A O     1 
ATOM   2391 C CB    . GLN A 1 311 ? 8.852   -5.743  31.745  1.00 19.00  ? 304 GLN A CB    1 
ATOM   2392 C CG    . GLN A 1 311 ? 9.961   -6.696  31.367  1.00 21.05  ? 304 GLN A CG    1 
ATOM   2393 C CD    . GLN A 1 311 ? 11.300  -6.086  31.715  1.00 23.29  ? 304 GLN A CD    1 
ATOM   2394 O OE1   . GLN A 1 311 ? 11.799  -5.175  31.040  1.00 20.51  ? 304 GLN A OE1   1 
ATOM   2395 N NE2   . GLN A 1 311 ? 11.862  -6.565  32.820  1.00 25.27  ? 304 GLN A NE2   1 
ATOM   2396 N N     . ALA A 1 312 ? 6.426   -3.865  31.076  1.00 15.73  ? 305 ALA A N     1 
ATOM   2397 C CA    . ALA A 1 312 ? 5.387   -2.847  31.370  1.00 13.65  ? 305 ALA A CA    1 
ATOM   2398 C C     . ALA A 1 312 ? 3.981   -3.491  31.298  1.00 13.66  ? 305 ALA A C     1 
ATOM   2399 O O     . ALA A 1 312 ? 3.215   -3.385  32.278  1.00 12.91  ? 305 ALA A O     1 
ATOM   2400 C CB    . ALA A 1 312 ? 5.541   -1.670  30.449  1.00 13.66  ? 305 ALA A CB    1 
ATOM   2401 N N     . LEU A 1 313 ? 3.659   -4.188  30.213  1.00 13.40  ? 306 LEU A N     1 
ATOM   2402 C CA    . LEU A 1 313 ? 2.318   -4.801  29.977  1.00 14.62  ? 306 LEU A CA    1 
ATOM   2403 C C     . LEU A 1 313 ? 1.958   -5.796  31.093  1.00 15.06  ? 306 LEU A C     1 
ATOM   2404 O O     . LEU A 1 313 ? 0.755   -5.873  31.435  1.00 16.47  ? 306 LEU A O     1 
ATOM   2405 C CB    . LEU A 1 313 ? 2.301   -5.465  28.585  1.00 14.72  ? 306 LEU A CB    1 
ATOM   2406 C CG    . LEU A 1 313 ? 2.308   -4.477  27.416  1.00 14.23  ? 306 LEU A CG    1 
ATOM   2407 C CD1   . LEU A 1 313 ? 2.675   -5.140  26.109  1.00 15.27  ? 306 LEU A CD1   1 
ATOM   2408 C CD2   . LEU A 1 313 ? 0.962   -3.798  27.279  1.00 14.78  ? 306 LEU A CD2   1 
ATOM   2409 N N     . ALA A 1 314 ? 2.949   -6.509  31.640  1.00 15.26  ? 307 ALA A N     1 
ATOM   2410 C CA    . ALA A 1 314 ? 2.833   -7.503  32.739  1.00 14.53  ? 307 ALA A CA    1 
ATOM   2411 C C     . ALA A 1 314 ? 2.829   -6.819  34.113  1.00 14.58  ? 307 ALA A C     1 
ATOM   2412 O O     . ALA A 1 314 ? 2.608   -7.529  35.113  1.00 15.17  ? 307 ALA A O     1 
ATOM   2413 C CB    . ALA A 1 314 ? 3.979   -8.479  32.635  1.00 14.31  ? 307 ALA A CB    1 
ATOM   2414 N N     . HIS A 1 315 ? 3.083   -5.508  34.211  1.00 13.31  ? 308 HIS A N     1 
ATOM   2415 C CA    . HIS A 1 315 ? 3.069   -4.810  35.527  1.00 13.09  ? 308 HIS A CA    1 
ATOM   2416 C C     . HIS A 1 315 ? 1.690   -4.965  36.190  1.00 13.74  ? 308 HIS A C     1 
ATOM   2417 O O     . HIS A 1 315 ? 0.653   -4.847  35.514  1.00 12.16  ? 308 HIS A O     1 
ATOM   2418 C CB    . HIS A 1 315 ? 3.454   -3.334  35.380  1.00 12.94  ? 308 HIS A CB    1 
ATOM   2419 C CG    . HIS A 1 315 ? 3.845   -2.714  36.676  1.00 13.27  ? 308 HIS A CG    1 
ATOM   2420 N ND1   . HIS A 1 315 ? 2.927   -2.118  37.515  1.00 11.92  ? 308 HIS A ND1   1 
ATOM   2421 C CD2   . HIS A 1 315 ? 5.042   -2.646  37.311  1.00 13.57  ? 308 HIS A CD2   1 
ATOM   2422 C CE1   . HIS A 1 315 ? 3.520   -1.697  38.609  1.00 11.50  ? 308 HIS A CE1   1 
ATOM   2423 N NE2   . HIS A 1 315 ? 4.819   -2.006  38.518  1.00 13.28  ? 308 HIS A NE2   1 
ATOM   2424 N N     . PRO A 1 316 ? 1.628   -5.183  37.532  1.00 14.71  ? 309 PRO A N     1 
ATOM   2425 C CA    . PRO A 1 316 ? 0.355   -5.270  38.269  1.00 14.79  ? 309 PRO A CA    1 
ATOM   2426 C C     . PRO A 1 316 ? -0.639  -4.125  37.967  1.00 14.96  ? 309 PRO A C     1 
ATOM   2427 O O     . PRO A 1 316 ? -1.827  -4.323  37.990  1.00 16.85  ? 309 PRO A O     1 
ATOM   2428 C CB    . PRO A 1 316 ? 0.829   -5.262  39.734  1.00 14.30  ? 309 PRO A CB    1 
ATOM   2429 C CG    . PRO A 1 316 ? 2.144   -5.963  39.693  1.00 14.41  ? 309 PRO A CG    1 
ATOM   2430 C CD    . PRO A 1 316 ? 2.781   -5.384  38.435  1.00 15.37  ? 309 PRO A CD    1 
ATOM   2431 N N     . TYR A 1 317 ? -0.155  -2.942  37.628  1.00 14.98  ? 310 TYR A N     1 
ATOM   2432 C CA    . TYR A 1 317 ? -1.027  -1.779  37.339  1.00 14.58  ? 310 TYR A CA    1 
ATOM   2433 C C     . TYR A 1 317 ? -1.985  -2.082  36.188  1.00 14.18  ? 310 TYR A C     1 
ATOM   2434 O O     . TYR A 1 317 ? -3.114  -1.532  36.163  1.00 12.93  ? 310 TYR A O     1 
ATOM   2435 C CB    . TYR A 1 317 ? -0.180  -0.549  37.024  1.00 14.35  ? 310 TYR A CB    1 
ATOM   2436 C CG    . TYR A 1 317 ? -1.031  0.651   36.719  1.00 14.00  ? 310 TYR A CG    1 
ATOM   2437 C CD1   . TYR A 1 317 ? -1.940  1.144   37.647  1.00 14.13  ? 310 TYR A CD1   1 
ATOM   2438 C CD2   . TYR A 1 317 ? -0.919  1.303   35.511  1.00 13.61  ? 310 TYR A CD2   1 
ATOM   2439 C CE1   . TYR A 1 317 ? -2.708  2.270   37.386  1.00 13.42  ? 310 TYR A CE1   1 
ATOM   2440 C CE2   . TYR A 1 317 ? -1.690  2.417   35.227  1.00 13.84  ? 310 TYR A CE2   1 
ATOM   2441 C CZ    . TYR A 1 317 ? -2.576  2.906   36.165  1.00 14.39  ? 310 TYR A CZ    1 
ATOM   2442 O OH    . TYR A 1 317 ? -3.320  3.998   35.827  1.00 16.86  ? 310 TYR A OH    1 
ATOM   2443 N N     . LEU A 1 318 ? -1.558  -2.950  35.262  1.00 15.43  ? 311 LEU A N     1 
ATOM   2444 C CA    . LEU A 1 318 ? -2.257  -3.204  33.973  1.00 16.33  ? 311 LEU A CA    1 
ATOM   2445 C C     . LEU A 1 318 ? -2.901  -4.585  33.993  1.00 15.79  ? 311 LEU A C     1 
ATOM   2446 O O     . LEU A 1 318 ? -3.339  -5.032  32.948  1.00 14.20  ? 311 LEU A O     1 
ATOM   2447 C CB    . LEU A 1 318 ? -1.265  -3.093  32.802  1.00 16.71  ? 311 LEU A CB    1 
ATOM   2448 C CG    . LEU A 1 318 ? -0.723  -1.689  32.553  1.00 17.50  ? 311 LEU A CG    1 
ATOM   2449 C CD1   . LEU A 1 318 ? 0.225   -1.673  31.368  1.00 17.98  ? 311 LEU A CD1   1 
ATOM   2450 C CD2   . LEU A 1 318 ? -1.859  -0.711  32.345  1.00 18.25  ? 311 LEU A CD2   1 
ATOM   2451 N N     . GLU A 1 319 ? -2.983  -5.228  35.143  1.00 20.16  ? 312 GLU A N     1 
ATOM   2452 C CA    . GLU A 1 319 ? -3.442  -6.638  35.209  1.00 21.33  ? 312 GLU A CA    1 
ATOM   2453 C C     . GLU A 1 319 ? -4.903  -6.761  34.759  1.00 20.16  ? 312 GLU A C     1 
ATOM   2454 O O     . GLU A 1 319 ? -5.245  -7.822  34.259  1.00 21.79  ? 312 GLU A O     1 
ATOM   2455 C CB    . GLU A 1 319 ? -3.130  -7.230  36.577  1.00 24.50  ? 312 GLU A CB    1 
ATOM   2456 C CG    . GLU A 1 319 ? -3.904  -6.649  37.730  1.00 27.71  ? 312 GLU A CG    1 
ATOM   2457 C CD    . GLU A 1 319 ? -3.417  -7.239  39.050  1.00 31.05  ? 312 GLU A CD    1 
ATOM   2458 O OE1   . GLU A 1 319 ? -3.387  -8.493  39.157  1.00 29.67  ? 312 GLU A OE1   1 
ATOM   2459 O OE2   . GLU A 1 319 ? -3.018  -6.446  39.945  1.00 33.92  ? 312 GLU A OE2   1 
ATOM   2460 N N     . GLN A 1 320 ? -5.737  -5.725  34.813  1.00 18.45  ? 313 GLN A N     1 
ATOM   2461 C CA    . GLN A 1 320 ? -7.133  -5.904  34.336  1.00 18.45  ? 313 GLN A CA    1 
ATOM   2462 C C     . GLN A 1 320 ? -7.161  -6.087  32.815  1.00 18.44  ? 313 GLN A C     1 
ATOM   2463 O O     . GLN A 1 320 ? -8.196  -6.559  32.322  1.00 16.69  ? 313 GLN A O     1 
ATOM   2464 C CB    . GLN A 1 320 ? -8.031  -4.733  34.719  1.00 19.44  ? 313 GLN A CB    1 
ATOM   2465 C CG    . GLN A 1 320 ? -8.230  -4.594  36.210  1.00 20.03  ? 313 GLN A CG    1 
ATOM   2466 C CD    . GLN A 1 320 ? -8.679  -3.187  36.516  1.00 23.34  ? 313 GLN A CD    1 
ATOM   2467 O OE1   . GLN A 1 320 ? -7.958  -2.203  36.276  1.00 24.28  ? 313 GLN A OE1   1 
ATOM   2468 N NE2   . GLN A 1 320 ? -9.900  -3.084  37.013  1.00 22.11  ? 313 GLN A NE2   1 
ATOM   2469 N N     . TYR A 1 321 ? -6.106  -5.666  32.094  1.00 18.07  ? 314 TYR A N     1 
ATOM   2470 C CA    . TYR A 1 321 ? -6.049  -5.671  30.608  1.00 17.40  ? 314 TYR A CA    1 
ATOM   2471 C C     . TYR A 1 321 ? -5.073  -6.739  30.108  1.00 16.43  ? 314 TYR A C     1 
ATOM   2472 O O     . TYR A 1 321 ? -5.277  -7.186  29.001  1.00 17.92  ? 314 TYR A O     1 
ATOM   2473 C CB    . TYR A 1 321 ? -5.691  -4.280  30.074  1.00 18.03  ? 314 TYR A CB    1 
ATOM   2474 C CG    . TYR A 1 321 ? -6.654  -3.208  30.507  1.00 18.44  ? 314 TYR A CG    1 
ATOM   2475 C CD1   . TYR A 1 321 ? -7.936  -3.145  29.989  1.00 21.31  ? 314 TYR A CD1   1 
ATOM   2476 C CD2   . TYR A 1 321 ? -6.308  -2.299  31.477  1.00 17.45  ? 314 TYR A CD2   1 
ATOM   2477 C CE1   . TYR A 1 321 ? -8.853  -2.201  30.435  1.00 21.44  ? 314 TYR A CE1   1 
ATOM   2478 C CE2   . TYR A 1 321 ? -7.196  -1.345  31.922  1.00 19.72  ? 314 TYR A CE2   1 
ATOM   2479 C CZ    . TYR A 1 321 ? -8.477  -1.296  31.404  1.00 21.69  ? 314 TYR A CZ    1 
ATOM   2480 O OH    . TYR A 1 321 ? -9.337  -0.329  31.835  1.00 22.88  ? 314 TYR A OH    1 
ATOM   2481 N N     . TYR A 1 322 ? -4.047  -7.093  30.876  1.00 16.45  ? 315 TYR A N     1 
ATOM   2482 C CA    . TYR A 1 322 ? -2.864  -7.879  30.416  1.00 17.92  ? 315 TYR A CA    1 
ATOM   2483 C C     . TYR A 1 322 ? -3.303  -9.215  29.831  1.00 16.41  ? 315 TYR A C     1 
ATOM   2484 O O     . TYR A 1 322 ? -3.910  -10.006 30.513  1.00 14.45  ? 315 TYR A O     1 
ATOM   2485 C CB    . TYR A 1 322 ? -1.839  -8.172  31.523  1.00 18.11  ? 315 TYR A CB    1 
ATOM   2486 C CG    . TYR A 1 322 ? -0.567  -8.840  31.045  1.00 17.46  ? 315 TYR A CG    1 
ATOM   2487 C CD1   . TYR A 1 322 ? 0.120   -8.366  29.936  1.00 18.28  ? 315 TYR A CD1   1 
ATOM   2488 C CD2   . TYR A 1 322 ? -0.042  -9.942  31.701  1.00 17.19  ? 315 TYR A CD2   1 
ATOM   2489 C CE1   . TYR A 1 322 ? 1.280   -8.976  29.479  1.00 17.73  ? 315 TYR A CE1   1 
ATOM   2490 C CE2   . TYR A 1 322 ? 1.093   -10.590 31.241  1.00 17.21  ? 315 TYR A CE2   1 
ATOM   2491 C CZ    . TYR A 1 322 ? 1.775   -10.089 30.142  1.00 18.99  ? 315 TYR A CZ    1 
ATOM   2492 O OH    . TYR A 1 322 ? 2.927   -10.686 29.707  1.00 19.30  ? 315 TYR A OH    1 
ATOM   2493 N N     . ASP A 1 323 ? -2.962  -9.432  28.570  1.00 18.15  ? 316 ASP A N     1 
ATOM   2494 C CA    . ASP A 1 323 ? -3.322  -10.663 27.824  1.00 19.32  ? 316 ASP A CA    1 
ATOM   2495 C C     . ASP A 1 323 ? -2.354  -10.762 26.654  1.00 17.77  ? 316 ASP A C     1 
ATOM   2496 O O     . ASP A 1 323 ? -2.577  -10.161 25.623  1.00 16.98  ? 316 ASP A O     1 
ATOM   2497 C CB    . ASP A 1 323 ? -4.794  -10.639 27.411  1.00 20.09  ? 316 ASP A CB    1 
ATOM   2498 C CG    . ASP A 1 323 ? -5.247  -11.882 26.674  1.00 21.67  ? 316 ASP A CG    1 
ATOM   2499 O OD1   . ASP A 1 323 ? -4.417  -12.809 26.485  1.00 24.05  ? 316 ASP A OD1   1 
ATOM   2500 O OD2   . ASP A 1 323 ? -6.419  -11.902 26.288  1.00 22.41  ? 316 ASP A OD2   1 
ATOM   2501 N N     . PRO A 1 324 ? -1.223  -11.471 26.833  1.00 17.73  ? 317 PRO A N     1 
ATOM   2502 C CA    . PRO A 1 324 ? -0.164  -11.505 25.825  1.00 18.41  ? 317 PRO A CA    1 
ATOM   2503 C C     . PRO A 1 324 ? -0.634  -12.147 24.507  1.00 16.95  ? 317 PRO A C     1 
ATOM   2504 O O     . PRO A 1 324 ? -0.149  -11.732 23.494  1.00 16.69  ? 317 PRO A O     1 
ATOM   2505 C CB    . PRO A 1 324 ? 1.001   -12.229 26.538  1.00 18.05  ? 317 PRO A CB    1 
ATOM   2506 C CG    . PRO A 1 324 ? 0.369   -12.955 27.679  1.00 18.04  ? 317 PRO A CG    1 
ATOM   2507 C CD    . PRO A 1 324 ? -0.853  -12.161 28.078  1.00 18.35  ? 317 PRO A CD    1 
ATOM   2508 N N     . SER A 1 325 ? -1.626  -13.047 24.575  1.00 16.19  ? 318 SER A N     1 
ATOM   2509 C CA    A SER A 1 325 ? -2.280  -13.688 23.402  0.50 15.38  ? 318 SER A CA    1 
ATOM   2510 C CA    B SER A 1 325 ? -2.297  -13.687 23.410  0.50 15.99  ? 318 SER A CA    1 
ATOM   2511 C C     . SER A 1 325 ? -3.032  -12.634 22.590  1.00 15.35  ? 318 SER A C     1 
ATOM   2512 O O     . SER A 1 325 ? -3.279  -12.893 21.408  1.00 15.43  ? 318 SER A O     1 
ATOM   2513 C CB    A SER A 1 325 ? -3.216  -14.818 23.823  0.50 14.50  ? 318 SER A CB    1 
ATOM   2514 C CB    B SER A 1 325 ? -3.272  -14.769 23.843  0.50 15.71  ? 318 SER A CB    1 
ATOM   2515 O OG    A SER A 1 325 ? -4.339  -14.317 24.534  0.50 12.85  ? 318 SER A OG    1 
ATOM   2516 O OG    B SER A 1 325 ? -2.576  -15.903 24.322  0.50 15.50  ? 318 SER A OG    1 
ATOM   2517 N N     . ASP A 1 326 ? -3.392  -11.524 23.228  1.00 15.39  ? 319 ASP A N     1 
ATOM   2518 C CA    . ASP A 1 326 ? -4.201  -10.439 22.623  1.00 16.16  ? 319 ASP A CA    1 
ATOM   2519 C C     . ASP A 1 326 ? -3.347  -9.177  22.453  1.00 15.91  ? 319 ASP A C     1 
ATOM   2520 O O     . ASP A 1 326 ? -3.927  -8.101  22.295  1.00 14.41  ? 319 ASP A O     1 
ATOM   2521 C CB    . ASP A 1 326 ? -5.414  -10.142 23.500  1.00 16.74  ? 319 ASP A CB    1 
ATOM   2522 C CG    . ASP A 1 326 ? -6.491  -9.338  22.802  1.00 17.22  ? 319 ASP A CG    1 
ATOM   2523 O OD1   . ASP A 1 326 ? -6.775  -9.636  21.631  1.00 16.57  ? 319 ASP A OD1   1 
ATOM   2524 O OD2   . ASP A 1 326 ? -7.041  -8.410  23.454  1.00 20.41  ? 319 ASP A OD2   1 
ATOM   2525 N N     . GLU A 1 327 ? -2.024  -9.337  22.421  1.00 15.49  ? 320 GLU A N     1 
ATOM   2526 C CA    . GLU A 1 327 ? -1.015  -8.246  22.249  1.00 14.61  ? 320 GLU A CA    1 
ATOM   2527 C C     . GLU A 1 327 ? -0.063  -8.748  21.175  1.00 13.48  ? 320 GLU A C     1 
ATOM   2528 O O     . GLU A 1 327 ? 0.991   -9.333  21.441  1.00 11.97  ? 320 GLU A O     1 
ATOM   2529 C CB    . GLU A 1 327 ? -0.360  -7.907  23.595  1.00 14.41  ? 320 GLU A CB    1 
ATOM   2530 C CG    . GLU A 1 327 ? -1.369  -7.326  24.580  1.00 14.96  ? 320 GLU A CG    1 
ATOM   2531 C CD    . GLU A 1 327 ? -1.025  -7.561  26.030  1.00 15.40  ? 320 GLU A CD    1 
ATOM   2532 O OE1   . GLU A 1 327 ? 0.130   -7.962  26.267  1.00 16.23  ? 320 GLU A OE1   1 
ATOM   2533 O OE2   . GLU A 1 327 ? -1.916  -7.393  26.895  1.00 15.01  ? 320 GLU A OE2   1 
ATOM   2534 N N     . PRO A 1 328 ? -0.525  -8.644  19.917  1.00 13.68  ? 321 PRO A N     1 
ATOM   2535 C CA    . PRO A 1 328 ? 0.153   -9.252  18.788  1.00 13.58  ? 321 PRO A CA    1 
ATOM   2536 C C     . PRO A 1 328 ? 1.477   -8.561  18.461  1.00 14.24  ? 321 PRO A C     1 
ATOM   2537 O O     . PRO A 1 328 ? 1.641   -7.404  18.793  1.00 12.69  ? 321 PRO A O     1 
ATOM   2538 C CB    . PRO A 1 328 ? -0.875  -9.095  17.655  1.00 14.13  ? 321 PRO A CB    1 
ATOM   2539 C CG    . PRO A 1 328 ? -1.669  -7.894  18.041  1.00 13.90  ? 321 PRO A CG    1 
ATOM   2540 C CD    . PRO A 1 328 ? -1.811  -8.048  19.540  1.00 14.13  ? 321 PRO A CD    1 
ATOM   2541 N N     . ILE A 1 329 ? 2.400   -9.326  17.877  1.00 15.54  ? 322 ILE A N     1 
ATOM   2542 C CA    . ILE A 1 329 ? 3.696   -8.821  17.352  1.00 16.52  ? 322 ILE A CA    1 
ATOM   2543 C C     . ILE A 1 329 ? 3.568   -8.788  15.829  1.00 17.31  ? 322 ILE A C     1 
ATOM   2544 O O     . ILE A 1 329 ? 2.619   -9.383  15.323  1.00 18.06  ? 322 ILE A O     1 
ATOM   2545 C CB    . ILE A 1 329 ? 4.877   -9.661  17.862  1.00 17.48  ? 322 ILE A CB    1 
ATOM   2546 C CG1   . ILE A 1 329 ? 4.841   -11.125 17.431  1.00 19.22  ? 322 ILE A CG1   1 
ATOM   2547 C CG2   . ILE A 1 329 ? 4.992   -9.562  19.360  1.00 17.62  ? 322 ILE A CG2   1 
ATOM   2548 C CD1   . ILE A 1 329 ? 6.092   -11.881 17.870  1.00 21.67  ? 322 ILE A CD1   1 
ATOM   2549 N N     . ALA A 1 330 ? 4.497   -8.140  15.134  1.00 17.47  ? 323 ALA A N     1 
ATOM   2550 C CA    . ALA A 1 330 ? 4.463   -7.927  13.676  1.00 19.24  ? 323 ALA A CA    1 
ATOM   2551 C C     . ALA A 1 330 ? 4.855   -9.224  12.950  1.00 21.79  ? 323 ALA A C     1 
ATOM   2552 O O     . ALA A 1 330 ? 5.774   -9.884  13.416  1.00 20.39  ? 323 ALA A O     1 
ATOM   2553 C CB    . ALA A 1 330 ? 5.399   -6.789  13.332  1.00 18.47  ? 323 ALA A CB    1 
ATOM   2554 N N     . GLU A 1 331 ? 4.197   -9.544  11.834  1.00 24.46  ? 324 GLU A N     1 
ATOM   2555 C CA    . GLU A 1 331 ? 4.530   -10.715 10.991  1.00 30.23  ? 324 GLU A CA    1 
ATOM   2556 C C     . GLU A 1 331 ? 5.867   -10.440 10.300  1.00 31.22  ? 324 GLU A C     1 
ATOM   2557 O O     . GLU A 1 331 ? 6.713   -11.342 10.309  1.00 29.55  ? 324 GLU A O     1 
ATOM   2558 C CB    . GLU A 1 331 ? 3.381   -10.991 10.021  1.00 34.30  ? 324 GLU A CB    1 
ATOM   2559 C CG    . GLU A 1 331 ? 2.091   -11.353 10.745  1.00 39.77  ? 324 GLU A CG    1 
ATOM   2560 C CD    . GLU A 1 331 ? 0.920   -11.765 9.865   1.00 43.81  ? 324 GLU A CD    1 
ATOM   2561 O OE1   . GLU A 1 331 ? 1.150   -12.011 8.667   1.00 43.95  ? 324 GLU A OE1   1 
ATOM   2562 O OE2   . GLU A 1 331 ? -0.227  -11.823 10.384  1.00 45.97  ? 324 GLU A OE2   1 
ATOM   2563 N N     . ALA A 1 332 ? 6.061   -9.207  9.807   1.00 33.33  ? 325 ALA A N     1 
ATOM   2564 C CA    . ALA A 1 332 ? 7.150   -8.824  8.881   1.00 33.32  ? 325 ALA A CA    1 
ATOM   2565 C C     . ALA A 1 332 ? 7.891   -7.598  9.415   1.00 34.24  ? 325 ALA A C     1 
ATOM   2566 O O     . ALA A 1 332 ? 7.637   -6.466  8.985   1.00 32.66  ? 325 ALA A O     1 
ATOM   2567 C CB    . ALA A 1 332 ? 6.587   -8.584  7.496   1.00 34.53  ? 325 ALA A CB    1 
ATOM   2568 N N     . PRO A 1 333 ? 8.881   -7.827  10.312  1.00 32.88  ? 326 PRO A N     1 
ATOM   2569 C CA    . PRO A 1 333 ? 9.730   -6.766  10.854  1.00 34.28  ? 326 PRO A CA    1 
ATOM   2570 C C     . PRO A 1 333 ? 10.750  -6.198  9.851   1.00 33.93  ? 326 PRO A C     1 
ATOM   2571 O O     . PRO A 1 333 ? 11.148  -6.914  8.966   1.00 35.96  ? 326 PRO A O     1 
ATOM   2572 C CB    . PRO A 1 333 ? 10.447  -7.495  12.003  1.00 35.69  ? 326 PRO A CB    1 
ATOM   2573 C CG    . PRO A 1 333 ? 10.571  -8.920  11.502  1.00 35.36  ? 326 PRO A CG    1 
ATOM   2574 C CD    . PRO A 1 333 ? 9.253   -9.162  10.809  1.00 34.00  ? 326 PRO A CD    1 
ATOM   2575 N N     . PHE A 1 334 ? 11.118  -4.921  9.987   1.00 32.88  ? 327 PHE A N     1 
ATOM   2576 C CA    . PHE A 1 334 ? 12.134  -4.251  9.131   1.00 34.75  ? 327 PHE A CA    1 
ATOM   2577 C C     . PHE A 1 334 ? 13.512  -4.779  9.537   1.00 35.13  ? 327 PHE A C     1 
ATOM   2578 O O     . PHE A 1 334 ? 13.862  -4.639  10.699  1.00 31.91  ? 327 PHE A O     1 
ATOM   2579 C CB    . PHE A 1 334 ? 12.035  -2.733  9.279   1.00 33.93  ? 327 PHE A CB    1 
ATOM   2580 C CG    . PHE A 1 334 ? 10.795  -2.136  8.669   1.00 33.20  ? 327 PHE A CG    1 
ATOM   2581 C CD1   . PHE A 1 334 ? 9.594   -2.129  9.357   1.00 31.68  ? 327 PHE A CD1   1 
ATOM   2582 C CD2   . PHE A 1 334 ? 10.828  -1.599  7.391   1.00 33.70  ? 327 PHE A CD2   1 
ATOM   2583 C CE1   . PHE A 1 334 ? 8.450   -1.601  8.780   1.00 34.91  ? 327 PHE A CE1   1 
ATOM   2584 C CE2   . PHE A 1 334 ? 9.688   -1.053  6.817   1.00 35.81  ? 327 PHE A CE2   1 
ATOM   2585 C CZ    . PHE A 1 334 ? 8.496   -1.062  7.508   1.00 36.88  ? 327 PHE A CZ    1 
ATOM   2586 N N     . LYS A 1 335 ? 14.268  -5.418  8.644   1.00 42.95  ? 328 LYS A N     1 
ATOM   2587 C CA    . LYS A 1 335 ? 15.496  -6.124  9.107   1.00 52.18  ? 328 LYS A CA    1 
ATOM   2588 C C     . LYS A 1 335 ? 16.746  -5.367  8.669   1.00 54.30  ? 328 LYS A C     1 
ATOM   2589 O O     . LYS A 1 335 ? 17.860  -5.850  8.981   1.00 59.03  ? 328 LYS A O     1 
ATOM   2590 C CB    . LYS A 1 335 ? 15.526  -7.590  8.662   1.00 57.45  ? 328 LYS A CB    1 
ATOM   2591 C CG    . LYS A 1 335 ? 16.263  -8.525  9.620   1.00 59.66  ? 328 LYS A CG    1 
ATOM   2592 C CD    . LYS A 1 335 ? 15.755  -8.523  11.067  1.00 59.21  ? 328 LYS A CD    1 
ATOM   2593 C CE    . LYS A 1 335 ? 16.712  -9.203  12.030  1.00 59.63  ? 328 LYS A CE    1 
ATOM   2594 N NZ    . LYS A 1 335 ? 16.048  -10.258 12.837  1.00 56.83  ? 328 LYS A NZ    1 
ATOM   2595 N N     . PHE A 1 336 ? 16.567  -4.213  8.026   1.00 55.05  ? 329 PHE A N     1 
ATOM   2596 C CA    . PHE A 1 336 ? 17.674  -3.349  7.554   1.00 57.18  ? 329 PHE A CA    1 
ATOM   2597 C C     . PHE A 1 336 ? 17.196  -1.898  7.566   1.00 59.25  ? 329 PHE A C     1 
ATOM   2598 O O     . PHE A 1 336 ? 15.994  -1.637  7.295   1.00 55.21  ? 329 PHE A O     1 
ATOM   2599 C CB    . PHE A 1 336 ? 18.152  -3.783  6.162   1.00 60.72  ? 329 PHE A CB    1 
ATOM   2600 C CG    . PHE A 1 336 ? 18.687  -5.193  6.070   1.00 61.62  ? 329 PHE A CG    1 
ATOM   2601 C CD1   . PHE A 1 336 ? 20.027  -5.465  6.303   1.00 64.11  ? 329 PHE A CD1   1 
ATOM   2602 C CD2   . PHE A 1 336 ? 17.855  -6.252  5.739   1.00 63.59  ? 329 PHE A CD2   1 
ATOM   2603 C CE1   . PHE A 1 336 ? 20.519  -6.760  6.211   1.00 63.73  ? 329 PHE A CE1   1 
ATOM   2604 C CE2   . PHE A 1 336 ? 18.348  -7.547  5.653   1.00 65.32  ? 329 PHE A CE2   1 
ATOM   2605 C CZ    . PHE A 1 336 ? 19.679  -7.799  5.890   1.00 64.81  ? 329 PHE A CZ    1 
ATOM   2606 N N     . ASP A 1 337 ? 18.123  -0.985  7.863   1.00 63.59  ? 330 ASP A N     1 
ATOM   2607 C CA    . ASP A 1 337 ? 17.860  0.477   7.945   1.00 68.86  ? 330 ASP A CA    1 
ATOM   2608 C C     . ASP A 1 337 ? 17.317  0.920   6.577   1.00 71.93  ? 330 ASP A C     1 
ATOM   2609 O O     . ASP A 1 337 ? 17.686  0.282   5.553   1.00 74.88  ? 330 ASP A O     1 
ATOM   2610 C CB    . ASP A 1 337 ? 19.119  1.238   8.398   1.00 73.03  ? 330 ASP A CB    1 
ATOM   2611 C CG    . ASP A 1 337 ? 19.953  0.540   9.472   1.00 68.02  ? 330 ASP A CG    1 
ATOM   2612 O OD1   . ASP A 1 337 ? 19.492  0.470   10.635  1.00 62.83  ? 330 ASP A OD1   1 
ATOM   2613 O OD2   . ASP A 1 337 ? 21.059  0.059   9.136   1.00 63.87  ? 330 ASP A OD2   1 
ATOM   2614 N N     . MET A 1 338 ? 16.468  1.952   6.550   1.00 69.37  ? 331 MET A N     1 
ATOM   2615 C CA    . MET A 1 338 ? 15.841  2.478   5.302   1.00 69.32  ? 331 MET A CA    1 
ATOM   2616 C C     . MET A 1 338 ? 16.809  3.500   4.671   1.00 73.07  ? 331 MET A C     1 
ATOM   2617 O O     . MET A 1 338 ? 16.865  4.656   5.161   1.00 77.62  ? 331 MET A O     1 
ATOM   2618 C CB    . MET A 1 338 ? 14.474  3.117   5.589   1.00 65.91  ? 331 MET A CB    1 
ATOM   2619 C CG    . MET A 1 338 ? 13.802  2.628   6.885   1.00 63.12  ? 331 MET A CG    1 
ATOM   2620 S SD    . MET A 1 338 ? 11.971  2.612   6.860   1.00 58.79  ? 331 MET A SD    1 
ATOM   2621 C CE    . MET A 1 338 ? 11.624  3.637   5.432   1.00 61.75  ? 331 MET A CE    1 
ATOM   2622 N N     . GLU A 1 339 ? 17.570  3.084   3.648   1.00 67.26  ? 332 GLU A N     1 
ATOM   2623 C CA    . GLU A 1 339 ? 18.776  3.805   3.141   1.00 67.15  ? 332 GLU A CA    1 
ATOM   2624 C C     . GLU A 1 339 ? 18.349  5.025   2.322   1.00 67.79  ? 332 GLU A C     1 
ATOM   2625 O O     . GLU A 1 339 ? 18.463  4.959   1.077   1.00 64.46  ? 332 GLU A O     1 
ATOM   2626 C CB    . GLU A 1 339 ? 19.651  2.877   2.297   1.00 65.22  ? 332 GLU A CB    1 
ATOM   2627 C CG    . GLU A 1 339 ? 20.403  1.848   3.119   1.00 64.12  ? 332 GLU A CG    1 
ATOM   2628 C CD    . GLU A 1 339 ? 20.773  0.614   2.320   1.00 62.07  ? 332 GLU A CD    1 
ATOM   2629 O OE1   . GLU A 1 339 ? 19.839  -0.064  1.839   1.00 56.72  ? 332 GLU A OE1   1 
ATOM   2630 O OE2   . GLU A 1 339 ? 21.987  0.347   2.166   1.00 55.57  ? 332 GLU A OE2   1 
ATOM   2631 N N     . LEU A 1 340 ? 17.951  6.101   3.019   1.00 61.77  ? 333 LEU A N     1 
ATOM   2632 C CA    . LEU A 1 340 ? 17.138  7.241   2.501   1.00 57.77  ? 333 LEU A CA    1 
ATOM   2633 C C     . LEU A 1 340 ? 17.897  8.565   2.620   1.00 55.33  ? 333 LEU A C     1 
ATOM   2634 O O     . LEU A 1 340 ? 17.408  9.559   2.076   1.00 57.03  ? 333 LEU A O     1 
ATOM   2635 C CB    . LEU A 1 340 ? 15.864  7.341   3.354   1.00 52.52  ? 333 LEU A CB    1 
ATOM   2636 C CG    . LEU A 1 340 ? 14.532  7.035   2.678   1.00 48.32  ? 333 LEU A CG    1 
ATOM   2637 C CD1   . LEU A 1 340 ? 14.526  5.643   2.066   1.00 46.26  ? 333 LEU A CD1   1 
ATOM   2638 C CD2   . LEU A 1 340 ? 13.387  7.197   3.678   1.00 47.84  ? 333 LEU A CD2   1 
ATOM   2639 N N     . ASP A 1 341 ? 19.008  8.584   3.357   1.00 56.77  ? 334 ASP A N     1 
ATOM   2640 C CA    . ASP A 1 341 ? 19.492  9.784   4.093   1.00 54.88  ? 334 ASP A CA    1 
ATOM   2641 C C     . ASP A 1 341 ? 20.036  10.815  3.107   1.00 54.74  ? 334 ASP A C     1 
ATOM   2642 O O     . ASP A 1 341 ? 19.953  12.008  3.420   1.00 57.45  ? 334 ASP A O     1 
ATOM   2643 C CB    . ASP A 1 341 ? 20.530  9.384   5.140   1.00 55.62  ? 334 ASP A CB    1 
ATOM   2644 C CG    . ASP A 1 341 ? 20.106  8.154   5.927   1.00 59.46  ? 334 ASP A CG    1 
ATOM   2645 O OD1   . ASP A 1 341 ? 19.720  7.145   5.287   1.00 54.96  ? 334 ASP A OD1   1 
ATOM   2646 O OD2   . ASP A 1 341 ? 20.135  8.219   7.173   1.00 68.08  ? 334 ASP A OD2   1 
ATOM   2647 N N     . ASP A 1 342 ? 20.576  10.363  1.971   1.00 57.78  ? 335 ASP A N     1 
ATOM   2648 C CA    . ASP A 1 342 ? 21.066  11.256  0.888   1.00 58.92  ? 335 ASP A CA    1 
ATOM   2649 C C     . ASP A 1 342 ? 20.732  10.597  -0.467  1.00 61.37  ? 335 ASP A C     1 
ATOM   2650 O O     . ASP A 1 342 ? 21.656  10.347  -1.280  1.00 58.93  ? 335 ASP A O     1 
ATOM   2651 C CB    . ASP A 1 342 ? 22.524  11.680  1.146   1.00 58.18  ? 335 ASP A CB    1 
ATOM   2652 C CG    . ASP A 1 342 ? 23.549  10.553  1.234   1.00 58.72  ? 335 ASP A CG    1 
ATOM   2653 O OD1   . ASP A 1 342 ? 23.674  9.913   2.304   1.00 52.00  ? 335 ASP A OD1   1 
ATOM   2654 O OD2   . ASP A 1 342 ? 24.236  10.337  0.232   1.00 65.06  ? 335 ASP A OD2   1 
ATOM   2655 N N     . LEU A 1 343 ? 19.419  10.442  -0.696  1.00 57.53  ? 336 LEU A N     1 
ATOM   2656 C CA    . LEU A 1 343 ? 18.768  10.111  -1.992  1.00 46.94  ? 336 LEU A CA    1 
ATOM   2657 C C     . LEU A 1 343 ? 18.156  11.443  -2.431  1.00 40.74  ? 336 LEU A C     1 
ATOM   2658 O O     . LEU A 1 343 ? 17.587  12.139  -1.590  1.00 34.69  ? 336 LEU A O     1 
ATOM   2659 C CB    . LEU A 1 343 ? 17.615  9.117   -1.812  1.00 45.81  ? 336 LEU A CB    1 
ATOM   2660 C CG    . LEU A 1 343 ? 17.859  7.775   -1.132  1.00 43.99  ? 336 LEU A CG    1 
ATOM   2661 C CD1   . LEU A 1 343 ? 16.922  6.742   -1.677  1.00 41.36  ? 336 LEU A CD1   1 
ATOM   2662 C CD2   . LEU A 1 343 ? 19.281  7.286   -1.271  1.00 48.17  ? 336 LEU A CD2   1 
ATOM   2663 N N     . PRO A 1 344 ? 18.219  11.845  -3.708  1.00 39.18  ? 337 PRO A N     1 
ATOM   2664 C CA    . PRO A 1 344 ? 17.597  13.088  -4.107  1.00 38.54  ? 337 PRO A CA    1 
ATOM   2665 C C     . PRO A 1 344 ? 16.066  13.074  -3.988  1.00 36.38  ? 337 PRO A C     1 
ATOM   2666 O O     . PRO A 1 344 ? 15.471  12.089  -4.167  1.00 32.58  ? 337 PRO A O     1 
ATOM   2667 C CB    . PRO A 1 344 ? 18.090  13.237  -5.545  1.00 41.54  ? 337 PRO A CB    1 
ATOM   2668 C CG    . PRO A 1 344 ? 18.312  11.828  -6.017  1.00 40.78  ? 337 PRO A CG    1 
ATOM   2669 C CD    . PRO A 1 344 ? 18.880  11.150  -4.796  1.00 40.19  ? 337 PRO A CD    1 
ATOM   2670 N N     . LYS A 1 345 ? 15.504  14.220  -3.649  1.00 37.49  ? 338 LYS A N     1 
ATOM   2671 C CA    . LYS A 1 345 ? 14.048  14.399  -3.529  1.00 42.25  ? 338 LYS A CA    1 
ATOM   2672 C C     . LYS A 1 345 ? 13.297  13.969  -4.801  1.00 42.16  ? 338 LYS A C     1 
ATOM   2673 O O     . LYS A 1 345 ? 12.087  13.955  -4.724  1.00 41.87  ? 338 LYS A O     1 
ATOM   2674 C CB    . LYS A 1 345 ? 13.761  15.854  -3.197  1.00 47.79  ? 338 LYS A CB    1 
ATOM   2675 C CG    . LYS A 1 345 ? 14.317  16.844  -4.196  1.00 49.88  ? 338 LYS A CG    1 
ATOM   2676 C CD    . LYS A 1 345 ? 14.078  18.250  -3.749  1.00 50.09  ? 338 LYS A CD    1 
ATOM   2677 C CE    . LYS A 1 345 ? 14.836  19.253  -4.580  1.00 54.15  ? 338 LYS A CE    1 
ATOM   2678 N NZ    . LYS A 1 345 ? 14.847  18.861  -6.004  1.00 56.05  ? 338 LYS A NZ    1 
ATOM   2679 N N     . GLU A 1 346 ? 13.997  13.670  -5.906  1.00 38.42  ? 339 GLU A N     1 
ATOM   2680 C CA    . GLU A 1 346 ? 13.441  13.165  -7.195  1.00 35.39  ? 339 GLU A CA    1 
ATOM   2681 C C     . GLU A 1 346 ? 13.315  11.642  -7.163  1.00 32.26  ? 339 GLU A C     1 
ATOM   2682 O O     . GLU A 1 346 ? 12.311  11.132  -7.657  1.00 25.03  ? 339 GLU A O     1 
ATOM   2683 C CB    . GLU A 1 346 ? 14.351  13.504  -8.378  1.00 40.73  ? 339 GLU A CB    1 
ATOM   2684 C CG    . GLU A 1 346 ? 14.440  14.992  -8.662  1.00 43.05  ? 339 GLU A CG    1 
ATOM   2685 C CD    . GLU A 1 346 ? 15.599  15.699  -7.985  1.00 41.54  ? 339 GLU A CD    1 
ATOM   2686 O OE1   . GLU A 1 346 ? 16.729  15.175  -8.070  1.00 41.07  ? 339 GLU A OE1   1 
ATOM   2687 O OE2   . GLU A 1 346 ? 15.359  16.771  -7.383  1.00 44.88  ? 339 GLU A OE2   1 
ATOM   2688 N N     . LYS A 1 347 ? 14.323  10.935  -6.641  1.00 29.53  ? 340 LYS A N     1 
ATOM   2689 C CA    . LYS A 1 347 ? 14.201  9.476   -6.392  1.00 30.77  ? 340 LYS A CA    1 
ATOM   2690 C C     . LYS A 1 347 ? 13.131  9.267   -5.310  1.00 28.09  ? 340 LYS A C     1 
ATOM   2691 O O     . LYS A 1 347 ? 12.445  8.252   -5.387  1.00 27.17  ? 340 LYS A O     1 
ATOM   2692 C CB    . LYS A 1 347 ? 15.542  8.847   -6.007  1.00 32.86  ? 340 LYS A CB    1 
ATOM   2693 C CG    . LYS A 1 347 ? 15.569  7.324   -6.048  1.00 37.00  ? 340 LYS A CG    1 
ATOM   2694 C CD    . LYS A 1 347 ? 15.603  6.743   -7.472  1.00 40.21  ? 340 LYS A CD    1 
ATOM   2695 C CE    . LYS A 1 347 ? 17.002  6.570   -8.036  1.00 39.37  ? 340 LYS A CE    1 
ATOM   2696 N NZ    . LYS A 1 347 ? 17.017  6.762   -9.508  1.00 42.64  ? 340 LYS A NZ    1 
ATOM   2697 N N     . LEU A 1 348 ? 13.016  10.185  -4.348  1.00 26.24  ? 341 LEU A N     1 
ATOM   2698 C CA    . LEU A 1 348 ? 12.114  10.061  -3.162  1.00 29.15  ? 341 LEU A CA    1 
ATOM   2699 C C     . LEU A 1 348 ? 10.646  10.225  -3.582  1.00 27.37  ? 341 LEU A C     1 
ATOM   2700 O O     . LEU A 1 348 ? 9.817   9.452   -3.086  1.00 25.44  ? 341 LEU A O     1 
ATOM   2701 C CB    . LEU A 1 348 ? 12.496  11.100  -2.103  1.00 28.27  ? 341 LEU A CB    1 
ATOM   2702 C CG    . LEU A 1 348 ? 13.757  10.774  -1.306  1.00 30.85  ? 341 LEU A CG    1 
ATOM   2703 C CD1   . LEU A 1 348 ? 13.939  11.746  -0.146  1.00 32.26  ? 341 LEU A CD1   1 
ATOM   2704 C CD2   . LEU A 1 348 ? 13.717  9.330   -0.800  1.00 30.91  ? 341 LEU A CD2   1 
ATOM   2705 N N     . LYS A 1 349 ? 10.357  11.192  -4.462  1.00 28.09  ? 342 LYS A N     1 
ATOM   2706 C CA    . LYS A 1 349 ? 9.044   11.315  -5.150  1.00 27.44  ? 342 LYS A CA    1 
ATOM   2707 C C     . LYS A 1 349 ? 8.740   9.998   -5.885  1.00 28.91  ? 342 LYS A C     1 
ATOM   2708 O O     . LYS A 1 349 ? 7.676   9.421   -5.616  1.00 25.30  ? 342 LYS A O     1 
ATOM   2709 C CB    . LYS A 1 349 ? 9.093   12.515  -6.078  1.00 27.89  ? 342 LYS A CB    1 
ATOM   2710 C CG    . LYS A 1 349 ? 7.787   12.915  -6.735  1.00 26.82  ? 342 LYS A CG    1 
ATOM   2711 C CD    . LYS A 1 349 ? 7.997   14.100  -7.645  1.00 25.53  ? 342 LYS A CD    1 
ATOM   2712 C CE    . LYS A 1 349 ? 7.022   14.131  -8.788  1.00 27.61  ? 342 LYS A CE    1 
ATOM   2713 N NZ    . LYS A 1 349 ? 5.877   15.021  -8.521  1.00 28.11  ? 342 LYS A NZ    1 
ATOM   2714 N N     . GLU A 1 350 ? 9.658   9.502   -6.727  1.00 29.39  ? 343 GLU A N     1 
ATOM   2715 C CA    . GLU A 1 350 ? 9.506   8.169   -7.382  1.00 32.95  ? 343 GLU A CA    1 
ATOM   2716 C C     . GLU A 1 350 ? 9.136   7.094   -6.341  1.00 31.55  ? 343 GLU A C     1 
ATOM   2717 O O     . GLU A 1 350 ? 8.207   6.312   -6.609  1.00 32.68  ? 343 GLU A O     1 
ATOM   2718 C CB    . GLU A 1 350 ? 10.784  7.701   -8.077  1.00 35.33  ? 343 GLU A CB    1 
ATOM   2719 C CG    . GLU A 1 350 ? 10.996  8.276   -9.459  1.00 40.52  ? 343 GLU A CG    1 
ATOM   2720 C CD    . GLU A 1 350 ? 12.467  8.233   -9.848  1.00 43.86  ? 343 GLU A CD    1 
ATOM   2721 O OE1   . GLU A 1 350 ? 12.936  9.144   -10.587 1.00 48.02  ? 343 GLU A OE1   1 
ATOM   2722 O OE2   . GLU A 1 350 ? 13.153  7.309   -9.376  1.00 41.84  ? 343 GLU A OE2   1 
ATOM   2723 N N     . LEU A 1 351 ? 9.868   6.994   -5.226  1.00 28.20  ? 344 LEU A N     1 
ATOM   2724 C CA    . LEU A 1 351 ? 9.619   5.932   -4.217  1.00 28.65  ? 344 LEU A CA    1 
ATOM   2725 C C     . LEU A 1 351 ? 8.224   6.123   -3.612  1.00 23.25  ? 344 LEU A C     1 
ATOM   2726 O O     . LEU A 1 351 ? 7.565   5.146   -3.386  1.00 21.67  ? 344 LEU A O     1 
ATOM   2727 C CB    . LEU A 1 351 ? 10.675  5.964   -3.104  1.00 32.27  ? 344 LEU A CB    1 
ATOM   2728 C CG    . LEU A 1 351 ? 11.939  5.119   -3.295  1.00 32.19  ? 344 LEU A CG    1 
ATOM   2729 C CD1   . LEU A 1 351 ? 11.754  3.984   -4.298  1.00 31.64  ? 344 LEU A CD1   1 
ATOM   2730 C CD2   . LEU A 1 351 ? 13.100  6.006   -3.697  1.00 31.92  ? 344 LEU A CD2   1 
ATOM   2731 N N     . ILE A 1 352 ? 7.804   7.352   -3.357  1.00 22.39  ? 345 ILE A N     1 
ATOM   2732 C CA    . ILE A 1 352 ? 6.448   7.660   -2.806  1.00 23.79  ? 345 ILE A CA    1 
ATOM   2733 C C     . ILE A 1 352 ? 5.382   7.270   -3.850  1.00 24.16  ? 345 ILE A C     1 
ATOM   2734 O O     . ILE A 1 352 ? 4.323   6.707   -3.448  1.00 19.93  ? 345 ILE A O     1 
ATOM   2735 C CB    . ILE A 1 352 ? 6.390   9.145   -2.408  1.00 24.00  ? 345 ILE A CB    1 
ATOM   2736 C CG1   . ILE A 1 352 ? 7.231   9.391   -1.150  1.00 24.74  ? 345 ILE A CG1   1 
ATOM   2737 C CG2   . ILE A 1 352 ? 4.955   9.611   -2.260  1.00 25.77  ? 345 ILE A CG2   1 
ATOM   2738 C CD1   . ILE A 1 352 ? 7.685   10.823  -0.957  1.00 23.59  ? 345 ILE A CD1   1 
ATOM   2739 N N     . PHE A 1 353 ? 5.636   7.585   -5.135  1.00 21.73  ? 346 PHE A N     1 
ATOM   2740 C CA    . PHE A 1 353 ? 4.692   7.324   -6.255  1.00 21.33  ? 346 PHE A CA    1 
ATOM   2741 C C     . PHE A 1 353 ? 4.380   5.831   -6.187  1.00 21.83  ? 346 PHE A C     1 
ATOM   2742 O O     . PHE A 1 353 ? 3.176   5.434   -6.056  1.00 19.33  ? 346 PHE A O     1 
ATOM   2743 C CB    . PHE A 1 353 ? 5.288   7.753   -7.610  1.00 20.36  ? 346 PHE A CB    1 
ATOM   2744 C CG    . PHE A 1 353 ? 4.357   7.550   -8.780  1.00 19.55  ? 346 PHE A CG    1 
ATOM   2745 C CD1   . PHE A 1 353 ? 3.292   8.427   -8.998  1.00 18.97  ? 346 PHE A CD1   1 
ATOM   2746 C CD2   . PHE A 1 353 ? 4.500   6.451   -9.612  1.00 18.03  ? 346 PHE A CD2   1 
ATOM   2747 C CE1   . PHE A 1 353 ? 2.438   8.239   -10.074 1.00 18.40  ? 346 PHE A CE1   1 
ATOM   2748 C CE2   . PHE A 1 353 ? 3.614   6.235   -10.662 1.00 18.94  ? 346 PHE A CE2   1 
ATOM   2749 C CZ    . PHE A 1 353 ? 2.593   7.139   -10.897 1.00 18.50  ? 346 PHE A CZ    1 
ATOM   2750 N N     . GLU A 1 354 ? 5.476   5.067   -6.163  1.00 21.33  ? 347 GLU A N     1 
ATOM   2751 C CA    . GLU A 1 354 ? 5.516   3.585   -6.159  1.00 25.02  ? 347 GLU A CA    1 
ATOM   2752 C C     . GLU A 1 354 ? 4.863   3.012   -4.897  1.00 23.66  ? 347 GLU A C     1 
ATOM   2753 O O     . GLU A 1 354 ? 4.062   2.103   -5.054  1.00 22.76  ? 347 GLU A O     1 
ATOM   2754 C CB    . GLU A 1 354 ? 6.962   3.123   -6.301  1.00 27.69  ? 347 GLU A CB    1 
ATOM   2755 C CG    . GLU A 1 354 ? 7.539   3.421   -7.660  1.00 32.31  ? 347 GLU A CG    1 
ATOM   2756 C CD    . GLU A 1 354 ? 8.813   2.666   -7.974  1.00 39.50  ? 347 GLU A CD    1 
ATOM   2757 O OE1   . GLU A 1 354 ? 9.779   2.795   -7.176  1.00 39.06  ? 347 GLU A OE1   1 
ATOM   2758 O OE2   . GLU A 1 354 ? 8.823   1.931   -9.004  1.00 45.22  ? 347 GLU A OE2   1 
ATOM   2759 N N     . GLU A 1 355 ? 5.138   3.577   -3.712  1.00 24.74  ? 348 GLU A N     1 
ATOM   2760 C CA    . GLU A 1 355 ? 4.546   3.148   -2.416  1.00 23.39  ? 348 GLU A CA    1 
ATOM   2761 C C     . GLU A 1 355 ? 3.034   3.399   -2.406  1.00 21.90  ? 348 GLU A C     1 
ATOM   2762 O O     . GLU A 1 355 ? 2.378   2.774   -1.573  1.00 22.90  ? 348 GLU A O     1 
ATOM   2763 C CB    . GLU A 1 355 ? 5.098   3.952   -1.231  1.00 25.77  ? 348 GLU A CB    1 
ATOM   2764 C CG    . GLU A 1 355 ? 6.241   3.322   -0.469  1.00 28.59  ? 348 GLU A CG    1 
ATOM   2765 C CD    . GLU A 1 355 ? 6.245   1.812   -0.363  1.00 30.18  ? 348 GLU A CD    1 
ATOM   2766 O OE1   . GLU A 1 355 ? 5.480   1.256   0.453   1.00 31.78  ? 348 GLU A OE1   1 
ATOM   2767 O OE2   . GLU A 1 355 ? 7.015   1.202   -1.112  1.00 33.12  ? 348 GLU A OE2   1 
ATOM   2768 N N     . THR A 1 356 ? 2.514   4.311   -3.236  1.00 21.02  ? 349 THR A N     1 
ATOM   2769 C CA    . THR A 1 356 ? 1.080   4.755   -3.233  1.00 20.08  ? 349 THR A CA    1 
ATOM   2770 C C     . THR A 1 356 ? 0.230   4.090   -4.349  1.00 20.79  ? 349 THR A C     1 
ATOM   2771 O O     . THR A 1 356 ? -1.016  4.281   -4.366  1.00 19.06  ? 349 THR A O     1 
ATOM   2772 C CB    . THR A 1 356 ? 1.020   6.298   -3.238  1.00 19.08  ? 349 THR A CB    1 
ATOM   2773 O OG1   . THR A 1 356 ? 1.797   6.845   -4.305  1.00 17.57  ? 349 THR A OG1   1 
ATOM   2774 C CG2   . THR A 1 356 ? 1.512   6.885   -1.927  1.00 18.29  ? 349 THR A CG2   1 
ATOM   2775 N N     . ALA A 1 357 ? 0.842   3.290   -5.217  1.00 21.69  ? 350 ALA A N     1 
ATOM   2776 C CA    . ALA A 1 357 ? 0.259   2.687   -6.445  1.00 23.38  ? 350 ALA A CA    1 
ATOM   2777 C C     . ALA A 1 357 ? -0.971  1.797   -6.141  1.00 24.81  ? 350 ALA A C     1 
ATOM   2778 O O     . ALA A 1 357 ? -1.897  1.731   -6.974  1.00 20.68  ? 350 ALA A O     1 
ATOM   2779 C CB    . ALA A 1 357 ? 1.341   1.903   -7.130  1.00 20.82  ? 350 ALA A CB    1 
ATOM   2780 N N     . ARG A 1 358 ? -0.997  1.117   -4.995  1.00 28.27  ? 351 ARG A N     1 
ATOM   2781 C CA    . ARG A 1 358 ? -2.014  0.069   -4.718  1.00 30.37  ? 351 ARG A CA    1 
ATOM   2782 C C     . ARG A 1 358 ? -3.380  0.732   -4.516  1.00 28.78  ? 351 ARG A C     1 
ATOM   2783 O O     . ARG A 1 358 ? -4.376  0.025   -4.651  1.00 29.65  ? 351 ARG A O     1 
ATOM   2784 C CB    . ARG A 1 358 ? -1.612  -0.823  -3.535  1.00 33.23  ? 351 ARG A CB    1 
ATOM   2785 C CG    . ARG A 1 358 ? -1.566  -0.126  -2.182  1.00 37.06  ? 351 ARG A CG    1 
ATOM   2786 C CD    . ARG A 1 358 ? -0.763  -0.924  -1.163  1.00 41.28  ? 351 ARG A CD    1 
ATOM   2787 N NE    . ARG A 1 358 ? 0.654   -0.907  -1.534  1.00 47.53  ? 351 ARG A NE    1 
ATOM   2788 C CZ    . ARG A 1 358 ? 1.676   -1.309  -0.768  1.00 46.58  ? 351 ARG A CZ    1 
ATOM   2789 N NH1   . ARG A 1 358 ? 1.463   -1.774  0.456   1.00 41.02  ? 351 ARG A NH1   1 
ATOM   2790 N NH2   . ARG A 1 358 ? 2.915   -1.211  -1.237  1.00 42.83  ? 351 ARG A NH2   1 
ATOM   2791 N N     . PHE A 1 359 ? -3.429  2.033   -4.218  1.00 26.28  ? 352 PHE A N     1 
ATOM   2792 C CA    . PHE A 1 359 ? -4.697  2.766   -3.987  1.00 27.59  ? 352 PHE A CA    1 
ATOM   2793 C C     . PHE A 1 359 ? -5.239  3.361   -5.294  1.00 29.06  ? 352 PHE A C     1 
ATOM   2794 O O     . PHE A 1 359 ? -6.253  4.088   -5.218  1.00 26.37  ? 352 PHE A O     1 
ATOM   2795 C CB    . PHE A 1 359 ? -4.509  3.824   -2.899  1.00 26.39  ? 352 PHE A CB    1 
ATOM   2796 C CG    . PHE A 1 359 ? -4.295  3.216   -1.540  1.00 25.61  ? 352 PHE A CG    1 
ATOM   2797 C CD1   . PHE A 1 359 ? -5.361  2.699   -0.823  1.00 24.86  ? 352 PHE A CD1   1 
ATOM   2798 C CD2   . PHE A 1 359 ? -3.026  3.115   -1.002  1.00 25.60  ? 352 PHE A CD2   1 
ATOM   2799 C CE1   . PHE A 1 359 ? -5.164  2.105   0.411   1.00 24.92  ? 352 PHE A CE1   1 
ATOM   2800 C CE2   . PHE A 1 359 ? -2.828  2.530   0.242   1.00 26.61  ? 352 PHE A CE2   1 
ATOM   2801 C CZ    . PHE A 1 359 ? -3.898  2.030   0.950   1.00 24.83  ? 352 PHE A CZ    1 
ATOM   2802 N N     . GLN A 1 360 ? -4.596  3.108   -6.443  1.00 30.99  ? 353 GLN A N     1 
ATOM   2803 C CA    . GLN A 1 360 ? -5.027  3.699   -7.741  1.00 34.63  ? 353 GLN A CA    1 
ATOM   2804 C C     . GLN A 1 360 ? -5.956  2.710   -8.438  1.00 35.74  ? 353 GLN A C     1 
ATOM   2805 O O     . GLN A 1 360 ? -5.654  1.520   -8.462  1.00 35.28  ? 353 GLN A O     1 
ATOM   2806 C CB    . GLN A 1 360 ? -3.835  4.063   -8.636  1.00 33.83  ? 353 GLN A CB    1 
ATOM   2807 C CG    . GLN A 1 360 ? -3.002  5.237   -8.131  1.00 33.55  ? 353 GLN A CG    1 
ATOM   2808 C CD    . GLN A 1 360 ? -3.750  6.552   -8.109  1.00 37.24  ? 353 GLN A CD    1 
ATOM   2809 O OE1   . GLN A 1 360 ? -4.049  7.115   -7.039  1.00 28.27  ? 353 GLN A OE1   1 
ATOM   2810 N NE2   . GLN A 1 360 ? -4.080  7.039   -9.306  1.00 34.94  ? 353 GLN A NE2   1 
ATOM   2811 N N     . PRO A 1 361 ? -7.085  3.173   -9.031  1.00 38.94  ? 354 PRO A N     1 
ATOM   2812 C CA    . PRO A 1 361 ? -8.005  2.292   -9.761  1.00 39.68  ? 354 PRO A CA    1 
ATOM   2813 C C     . PRO A 1 361 ? -7.461  1.791   -11.108 1.00 36.83  ? 354 PRO A C     1 
ATOM   2814 O O     . PRO A 1 361 ? -6.290  1.499   -11.262 1.00 37.81  ? 354 PRO A O     1 
ATOM   2815 C CB    . PRO A 1 361 ? -9.247  3.168   -10.024 1.00 40.30  ? 354 PRO A CB    1 
ATOM   2816 C CG    . PRO A 1 361 ? -9.068  4.392   -9.143  1.00 42.15  ? 354 PRO A CG    1 
ATOM   2817 C CD    . PRO A 1 361 ? -7.568  4.565   -9.006  1.00 41.05  ? 354 PRO A CD    1 
HETATM 2818 P PG    . ANP B 2 .   ? 1.799   14.431  12.190  1.00 132.33 ? 501 ANP A PG    1 
HETATM 2819 O O1G   . ANP B 2 .   ? 2.802   13.485  11.588  1.00 132.75 ? 501 ANP A O1G   1 
HETATM 2820 O O2G   . ANP B 2 .   ? 0.466   13.736  12.031  1.00 133.25 ? 501 ANP A O2G   1 
HETATM 2821 O O3G   . ANP B 2 .   ? 2.077   14.515  13.678  1.00 129.07 ? 501 ANP A O3G   1 
HETATM 2822 P PB    . ANP B 2 .   ? 1.231   17.368  11.769  1.00 111.58 ? 501 ANP A PB    1 
HETATM 2823 O O1B   . ANP B 2 .   ? 2.205   18.316  12.416  1.00 103.07 ? 501 ANP A O1B   1 
HETATM 2824 O O2B   . ANP B 2 .   ? 0.336   17.913  10.682  1.00 101.46 ? 501 ANP A O2B   1 
HETATM 2825 N N3B   . ANP B 2 .   ? 1.891   15.892  11.409  1.00 119.20 ? 501 ANP A N3B   1 
HETATM 2826 P PA    . ANP B 2 .   ? -1.161  16.203  12.928  1.00 78.39  ? 501 ANP A PA    1 
HETATM 2827 O O1A   . ANP B 2 .   ? -1.480  15.892  11.503  1.00 83.57  ? 501 ANP A O1A   1 
HETATM 2828 O O2A   . ANP B 2 .   ? -1.241  15.105  13.943  1.00 81.16  ? 501 ANP A O2A   1 
HETATM 2829 O O3A   . ANP B 2 .   ? 0.285   16.889  12.969  1.00 92.67  ? 501 ANP A O3A   1 
HETATM 2830 O "O5'" . ANP B 2 .   ? -2.015  17.469  13.425  1.00 70.14  ? 501 ANP A "O5'" 1 
HETATM 2831 C "C5'" . ANP B 2 .   ? -2.927  18.220  12.580  1.00 52.13  ? 501 ANP A "C5'" 1 
HETATM 2832 C "C4'" . ANP B 2 .   ? -4.269  18.226  13.259  1.00 46.80  ? 501 ANP A "C4'" 1 
HETATM 2833 O "O4'" . ANP B 2 .   ? -5.089  17.165  12.695  1.00 44.06  ? 501 ANP A "O4'" 1 
HETATM 2834 C "C3'" . ANP B 2 .   ? -4.211  17.961  14.771  1.00 44.01  ? 501 ANP A "C3'" 1 
HETATM 2835 O "O3'" . ANP B 2 .   ? -5.154  18.770  15.457  1.00 42.78  ? 501 ANP A "O3'" 1 
HETATM 2836 C "C2'" . ANP B 2 .   ? -4.462  16.447  14.847  1.00 44.34  ? 501 ANP A "C2'" 1 
HETATM 2837 O "O2'" . ANP B 2 .   ? -4.923  16.024  16.118  1.00 41.58  ? 501 ANP A "O2'" 1 
HETATM 2838 C "C1'" . ANP B 2 .   ? -5.457  16.239  13.696  1.00 43.73  ? 501 ANP A "C1'" 1 
HETATM 2839 N N9    . ANP B 2 .   ? -5.456  14.846  13.135  1.00 40.74  ? 501 ANP A N9    1 
HETATM 2840 C C8    . ANP B 2 .   ? -4.386  14.130  12.611  1.00 40.81  ? 501 ANP A C8    1 
HETATM 2841 N N7    . ANP B 2 .   ? -4.719  12.907  12.253  1.00 38.40  ? 501 ANP A N7    1 
HETATM 2842 C C5    . ANP B 2 .   ? -6.065  12.786  12.588  1.00 35.76  ? 501 ANP A C5    1 
HETATM 2843 C C6    . ANP B 2 .   ? -6.992  11.720  12.470  1.00 32.74  ? 501 ANP A C6    1 
HETATM 2844 N N6    . ANP B 2 .   ? -6.707  10.508  11.978  1.00 26.06  ? 501 ANP A N6    1 
HETATM 2845 N N1    . ANP B 2 .   ? -8.248  11.956  12.909  1.00 30.87  ? 501 ANP A N1    1 
HETATM 2846 C C2    . ANP B 2 .   ? -8.545  13.167  13.402  1.00 33.95  ? 501 ANP A C2    1 
HETATM 2847 N N3    . ANP B 2 .   ? -7.763  14.233  13.565  1.00 36.71  ? 501 ANP A N3    1 
HETATM 2848 C C4    . ANP B 2 .   ? -6.519  13.975  13.132  1.00 37.41  ? 501 ANP A C4    1 
HETATM 2849 O O     . HOH C 3 .   ? 12.113  9.617   41.127  1.00 36.93  ? 601 HOH A O     1 
HETATM 2850 O O     . HOH C 3 .   ? -3.054  -11.862 19.316  1.00 24.45  ? 602 HOH A O     1 
HETATM 2851 O O     . HOH C 3 .   ? 25.321  14.177  38.317  1.00 15.96  ? 603 HOH A O     1 
HETATM 2852 O O     . HOH C 3 .   ? -0.119  5.532   -11.220 1.00 27.19  ? 604 HOH A O     1 
HETATM 2853 O O     . HOH C 3 .   ? -2.773  6.387   -5.045  1.00 30.10  ? 605 HOH A O     1 
HETATM 2854 O O     . HOH C 3 .   ? 19.081  4.182   36.510  1.00 16.61  ? 606 HOH A O     1 
HETATM 2855 O O     . HOH C 3 .   ? -1.522  18.182  -10.939 1.00 20.98  ? 607 HOH A O     1 
HETATM 2856 O O     . HOH C 3 .   ? 4.105   -9.197  28.022  1.00 18.65  ? 608 HOH A O     1 
HETATM 2857 O O     . HOH C 3 .   ? 7.156   20.611  -0.140  1.00 28.54  ? 609 HOH A O     1 
HETATM 2858 O O     . HOH C 3 .   ? 11.109  12.928  22.603  1.00 26.60  ? 610 HOH A O     1 
HETATM 2859 O O     . HOH C 3 .   ? 20.288  10.512  16.226  1.00 32.57  ? 611 HOH A O     1 
HETATM 2860 O O     . HOH C 3 .   ? -6.008  13.882  34.889  1.00 14.48  ? 612 HOH A O     1 
HETATM 2861 O O     . HOH C 3 .   ? 21.149  6.351   39.097  1.00 31.44  ? 613 HOH A O     1 
HETATM 2862 O O     . HOH C 3 .   ? 21.625  19.799  33.335  1.00 35.13  ? 614 HOH A O     1 
HETATM 2863 O O     . HOH C 3 .   ? -1.463  14.594  -6.676  1.00 10.25  ? 615 HOH A O     1 
HETATM 2864 O O     . HOH C 3 .   ? -7.221  4.868   9.866   1.00 27.63  ? 616 HOH A O     1 
HETATM 2865 O O     . HOH C 3 .   ? 12.953  9.430   24.517  1.00 5.25   ? 617 HOH A O     1 
HETATM 2866 O O     . HOH C 3 .   ? -2.988  12.024  -16.719 1.00 10.47  ? 618 HOH A O     1 
HETATM 2867 O O     . HOH C 3 .   ? -5.210  -2.946  35.655  1.00 13.88  ? 619 HOH A O     1 
HETATM 2868 O O     . HOH C 3 .   ? 17.072  18.031  24.865  1.00 17.80  ? 620 HOH A O     1 
HETATM 2869 O O     . HOH C 3 .   ? 9.636   8.504   21.777  1.00 11.96  ? 621 HOH A O     1 
HETATM 2870 O O     . HOH C 3 .   ? -5.986  8.725   -6.459  1.00 16.37  ? 622 HOH A O     1 
HETATM 2871 O O     . HOH C 3 .   ? -3.461  -0.270  43.418  1.00 42.58  ? 623 HOH A O     1 
HETATM 2872 O O     . HOH C 3 .   ? -8.470  0.242   35.561  1.00 24.09  ? 624 HOH A O     1 
HETATM 2873 O O     . HOH C 3 .   ? 31.509  13.836  23.726  1.00 22.06  ? 625 HOH A O     1 
HETATM 2874 O O     . HOH C 3 .   ? -0.097  -6.711  33.765  1.00 18.01  ? 626 HOH A O     1 
HETATM 2875 O O     . HOH C 3 .   ? 0.453   -5.730  20.718  1.00 6.10   ? 627 HOH A O     1 
HETATM 2876 O O     . HOH C 3 .   ? -2.604  -0.125  12.005  1.00 8.12   ? 628 HOH A O     1 
HETATM 2877 O O     . HOH C 3 .   ? 2.616   -9.014  25.927  1.00 14.95  ? 629 HOH A O     1 
HETATM 2878 O O     . HOH C 3 .   ? -0.546  18.203  29.375  1.00 29.32  ? 630 HOH A O     1 
HETATM 2879 O O     . HOH C 3 .   ? 23.075  15.618  39.632  1.00 24.44  ? 631 HOH A O     1 
HETATM 2880 O O     . HOH C 3 .   ? 31.083  22.277  39.355  1.00 20.25  ? 632 HOH A O     1 
HETATM 2881 O O     . HOH C 3 .   ? 3.815   22.490  5.254   1.00 30.66  ? 633 HOH A O     1 
HETATM 2882 O O     . HOH C 3 .   ? 18.805  5.063   22.385  1.00 32.03  ? 634 HOH A O     1 
HETATM 2883 O O     . HOH C 3 .   ? 5.363   14.619  30.425  1.00 14.27  ? 635 HOH A O     1 
HETATM 2884 O O     . HOH C 3 .   ? 8.337   12.962  21.319  1.00 18.69  ? 636 HOH A O     1 
HETATM 2885 O O     . HOH C 3 .   ? 8.026   9.436   14.500  1.00 13.51  ? 637 HOH A O     1 
HETATM 2886 O O     . HOH C 3 .   ? 15.286  9.595   -9.307  1.00 57.34  ? 638 HOH A O     1 
HETATM 2887 O O     . HOH C 3 .   ? 1.194   -8.052  11.524  1.00 35.55  ? 639 HOH A O     1 
HETATM 2888 O O     . HOH C 3 .   ? 4.776   -6.822  10.024  1.00 29.07  ? 640 HOH A O     1 
HETATM 2889 O O     . HOH C 3 .   ? -8.089  -9.431  25.745  1.00 25.30  ? 641 HOH A O     1 
HETATM 2890 O O     . HOH C 3 .   ? -12.017 12.195  -5.451  1.00 26.09  ? 642 HOH A O     1 
HETATM 2891 O O     . HOH C 3 .   ? 36.025  11.919  34.784  1.00 17.68  ? 643 HOH A O     1 
HETATM 2892 O O     . HOH C 3 .   ? 12.170  13.867  28.967  1.00 16.93  ? 644 HOH A O     1 
HETATM 2893 O O     . HOH C 3 .   ? 17.004  6.200   37.648  1.00 10.63  ? 645 HOH A O     1 
HETATM 2894 O O     . HOH C 3 .   ? -13.422 7.133   10.246  1.00 24.37  ? 646 HOH A O     1 
HETATM 2895 O O     . HOH C 3 .   ? 24.961  23.124  34.468  1.00 26.21  ? 647 HOH A O     1 
HETATM 2896 O O     . HOH C 3 .   ? 10.851  20.099  21.240  1.00 29.70  ? 648 HOH A O     1 
HETATM 2897 O O     . HOH C 3 .   ? 7.788   15.683  30.374  1.00 24.35  ? 649 HOH A O     1 
HETATM 2898 O O     . HOH C 3 .   ? -1.606  13.030  42.380  1.00 26.80  ? 650 HOH A O     1 
HETATM 2899 O O     . HOH C 3 .   ? 5.559   -0.749  3.100   1.00 29.87  ? 651 HOH A O     1 
HETATM 2900 O O     . HOH C 3 .   ? 13.595  0.047   27.984  1.00 18.23  ? 652 HOH A O     1 
HETATM 2901 O O     . HOH C 3 .   ? 1.079   -12.446 21.004  1.00 20.56  ? 653 HOH A O     1 
HETATM 2902 O O     . HOH C 3 .   ? 10.638  -5.582  21.334  1.00 18.73  ? 654 HOH A O     1 
HETATM 2903 O O     . HOH C 3 .   ? 18.000  16.857  47.290  1.00 20.09  ? 655 HOH A O     1 
HETATM 2904 O O     . HOH C 3 .   ? 2.332   16.496  22.418  1.00 12.86  ? 656 HOH A O     1 
HETATM 2905 O O     . HOH C 3 .   ? -0.821  1.096   10.436  1.00 9.27   ? 657 HOH A O     1 
HETATM 2906 O O     . HOH C 3 .   ? 18.987  28.859  30.783  1.00 25.23  ? 658 HOH A O     1 
HETATM 2907 O O     . HOH C 3 .   ? 27.175  22.870  38.076  1.00 16.86  ? 659 HOH A O     1 
HETATM 2908 O O     . HOH C 3 .   ? -2.012  -6.721  15.240  1.00 27.10  ? 660 HOH A O     1 
HETATM 2909 O O     . HOH C 3 .   ? -4.575  -5.258  16.933  1.00 19.84  ? 661 HOH A O     1 
HETATM 2910 O O     . HOH C 3 .   ? 10.602  -1.976  24.759  1.00 15.30  ? 662 HOH A O     1 
HETATM 2911 O O     . HOH C 3 .   ? 21.377  24.071  26.615  1.00 26.82  ? 663 HOH A O     1 
HETATM 2912 O O     . HOH C 3 .   ? 16.796  -1.790  20.913  1.00 25.95  ? 664 HOH A O     1 
HETATM 2913 O O     . HOH C 3 .   ? 33.869  18.006  36.101  1.00 25.71  ? 665 HOH A O     1 
HETATM 2914 O O     . HOH C 3 .   ? -10.802 7.909   39.277  1.00 34.79  ? 666 HOH A O     1 
HETATM 2915 O O     . HOH C 3 .   ? -7.537  -1.489  22.083  1.00 32.74  ? 667 HOH A O     1 
HETATM 2916 O O     . HOH C 3 .   ? 26.171  5.310   44.025  1.00 26.53  ? 668 HOH A O     1 
HETATM 2917 O O     . HOH C 3 .   ? -1.554  16.939  -6.918  1.00 19.54  ? 669 HOH A O     1 
HETATM 2918 O O     . HOH C 3 .   ? -0.542  -8.719  35.215  1.00 24.07  ? 670 HOH A O     1 
HETATM 2919 O O     . HOH C 3 .   ? -11.580 9.722   24.811  1.00 27.32  ? 671 HOH A O     1 
HETATM 2920 O O     . HOH C 3 .   ? 16.137  20.207  -0.183  1.00 40.47  ? 672 HOH A O     1 
HETATM 2921 O O     . HOH C 3 .   ? 0.283   -1.874  45.243  1.00 46.39  ? 673 HOH A O     1 
HETATM 2922 O O     . HOH C 3 .   ? 12.594  -1.173  25.782  1.00 19.02  ? 674 HOH A O     1 
HETATM 2923 O O     . HOH C 3 .   ? 6.106   -11.468 31.339  1.00 24.36  ? 675 HOH A O     1 
HETATM 2924 O O     . HOH C 3 .   ? 10.758  14.335  -9.735  1.00 23.08  ? 676 HOH A O     1 
# 
