data_9BXY
# 
_entry.id   9BXY 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9BXY         pdb_00009bxy 10.2210/pdb9bxy/pdb 
WWPDB D_1000284355 ?            ?                   
# 
_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       2025-04-02 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BXY 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-23 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              marzena.pazgier@usuhs.edu 
_pdbx_contact_author.name_first         Marzena 
_pdbx_contact_author.name_last          Pazgier 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0594-5057 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Tolbert, W.D.' 1 ? 
'Niu, L.'       2 ? 
'Pazgier, M.'   3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acs Med.Chem.Lett.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1948-5875 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                1961 
_citation.page_last                 1969 
_citation.title                     
'Optimization of a Piperidine CD4-Mimetic Scaffold Sensitizing HIV-1 Infected Cells to Antibody-Dependent Cellular Cytotoxicity.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acsmedchemlett.4c00403 
_citation.pdbx_database_id_PubMed   39563795 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Lee, D.'                1  ?                   
primary 'Niu, L.'                2  ?                   
primary 'Ding, S.'               3  ?                   
primary 'Zhu, H.'                4  ?                   
primary 'Tolbert, W.D.'          5  ?                   
primary 'Medjahed, H.'           6  ?                   
primary 'Beaudoin-Bussieres, G.' 7  ?                   
primary 'Abrams, C.'             8  0000-0002-1240-0816 
primary 'Finzi, A.'              9  ?                   
primary 'Pazgier, M.'            10 ?                   
primary 'Smith 3rd, A.B.'        11 0000-0002-1712-8567 
# 
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 'HIV-1 LM/HS clade A/E CRF01 gp120 core' 39452.723 1  ? 'H61Y, Q105H, V108I, H375S, N474D, I475M, K476R' ? ? 
2 non-polymer man 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208   9  ? ?                                                ? ? 
3 non-polymer syn '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' 238.305   1  ? ? ? ? 
4 non-polymer syn 
'(3S,5R)-1-[4-(1-carbamimidoyl-L-prolyl)piperazine-1-carbonyl]-N-(4-chloro-3-fluorophenyl)-5-(hydroxymethyl)piperidine-3-carboxamide' 
538.015   1  ? ?                                                ? ? 
5 water       nat water 18.015    60 ? ?                                                ? ? 
# 
_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       
;VPVWKDADTTLFCASDAKAYETEVHNVWATHACVPTDPNPQEIHLENVTENFNMWKNNMVEQMHEDIISLWDQSLQPCVK
LTGGSVIKQACPKISFDPIPIHYCTPAGYVILKCNDKNFNGTGPCKNVSSVQCTHGIKPVVSTQLLLNGSLAEEEIIIRS
ENLTNNAKTIIVHLNKSVEINCTRPSNGGSGSGGDIRKAYCEINGTKWNKVLKQVTEKLKEHFNNKTIIFQPPSGGDLEI
TMHSFNCRGEFFYCNTTQLFNNTCIGNETMKGCNGTITLPCKIKQIINMWQGTGQAMYAPPIDGKINCVSNITGILLTRD
GGANNTSNETFRPGGGDMRDNWRSELYKYKVVQIE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;VPVWKDADTTLFCASDAKAYETEVHNVWATHACVPTDPNPQEIHLENVTENFNMWKNNMVEQMHEDIISLWDQSLQPCVK
LTGGSVIKQACPKISFDPIPIHYCTPAGYVILKCNDKNFNGTGPCKNVSSVQCTHGIKPVVSTQLLLNGSLAEEEIIIRS
ENLTNNAKTIIVHLNKSVEINCTRPSNGGSGSGGDIRKAYCEINGTKWNKVLKQVTEKLKEHFNNKTIIFQPPSGGDLEI
TMHSFNCRGEFFYCNTTQLFNNTCIGNETMKGCNGTITLPCKIKQIINMWQGTGQAMYAPPIDGKINCVSNITGILLTRD
GGANNTSNETFRPGGGDMRDNWRSELYKYKVVQIE
;
_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 2-acetamido-2-deoxy-beta-D-glucopyranose NAG   
3 '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' EPE   
4 
'(3S,5R)-1-[4-(1-carbamimidoyl-L-prolyl)piperazine-1-carbonyl]-N-(4-chloro-3-fluorophenyl)-5-(hydroxymethyl)piperidine-3-carboxamide' 
A1ATE 
5 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   VAL n 
1 2   PRO n 
1 3   VAL n 
1 4   TRP n 
1 5   LYS n 
1 6   ASP n 
1 7   ALA n 
1 8   ASP n 
1 9   THR n 
1 10  THR n 
1 11  LEU n 
1 12  PHE n 
1 13  CYS n 
1 14  ALA n 
1 15  SER n 
1 16  ASP n 
1 17  ALA n 
1 18  LYS n 
1 19  ALA n 
1 20  TYR n 
1 21  GLU n 
1 22  THR n 
1 23  GLU n 
1 24  VAL n 
1 25  HIS n 
1 26  ASN n 
1 27  VAL n 
1 28  TRP n 
1 29  ALA n 
1 30  THR n 
1 31  HIS n 
1 32  ALA n 
1 33  CYS n 
1 34  VAL n 
1 35  PRO n 
1 36  THR n 
1 37  ASP n 
1 38  PRO n 
1 39  ASN n 
1 40  PRO n 
1 41  GLN n 
1 42  GLU n 
1 43  ILE n 
1 44  HIS n 
1 45  LEU n 
1 46  GLU n 
1 47  ASN n 
1 48  VAL n 
1 49  THR n 
1 50  GLU n 
1 51  ASN n 
1 52  PHE n 
1 53  ASN n 
1 54  MET n 
1 55  TRP n 
1 56  LYS n 
1 57  ASN n 
1 58  ASN n 
1 59  MET n 
1 60  VAL n 
1 61  GLU n 
1 62  GLN n 
1 63  MET n 
1 64  HIS n 
1 65  GLU n 
1 66  ASP n 
1 67  ILE n 
1 68  ILE n 
1 69  SER n 
1 70  LEU n 
1 71  TRP n 
1 72  ASP n 
1 73  GLN n 
1 74  SER n 
1 75  LEU n 
1 76  GLN n 
1 77  PRO n 
1 78  CYS n 
1 79  VAL n 
1 80  LYS n 
1 81  LEU n 
1 82  THR n 
1 83  GLY n 
1 84  GLY n 
1 85  SER n 
1 86  VAL n 
1 87  ILE n 
1 88  LYS n 
1 89  GLN n 
1 90  ALA n 
1 91  CYS n 
1 92  PRO n 
1 93  LYS n 
1 94  ILE n 
1 95  SER n 
1 96  PHE n 
1 97  ASP n 
1 98  PRO n 
1 99  ILE n 
1 100 PRO n 
1 101 ILE n 
1 102 HIS n 
1 103 TYR n 
1 104 CYS n 
1 105 THR n 
1 106 PRO n 
1 107 ALA n 
1 108 GLY n 
1 109 TYR n 
1 110 VAL n 
1 111 ILE n 
1 112 LEU n 
1 113 LYS n 
1 114 CYS n 
1 115 ASN n 
1 116 ASP n 
1 117 LYS n 
1 118 ASN n 
1 119 PHE n 
1 120 ASN n 
1 121 GLY n 
1 122 THR n 
1 123 GLY n 
1 124 PRO n 
1 125 CYS n 
1 126 LYS n 
1 127 ASN n 
1 128 VAL n 
1 129 SER n 
1 130 SER n 
1 131 VAL n 
1 132 GLN n 
1 133 CYS n 
1 134 THR n 
1 135 HIS n 
1 136 GLY n 
1 137 ILE n 
1 138 LYS n 
1 139 PRO n 
1 140 VAL n 
1 141 VAL n 
1 142 SER n 
1 143 THR n 
1 144 GLN n 
1 145 LEU n 
1 146 LEU n 
1 147 LEU n 
1 148 ASN n 
1 149 GLY n 
1 150 SER n 
1 151 LEU n 
1 152 ALA n 
1 153 GLU n 
1 154 GLU n 
1 155 GLU n 
1 156 ILE n 
1 157 ILE n 
1 158 ILE n 
1 159 ARG n 
1 160 SER n 
1 161 GLU n 
1 162 ASN n 
1 163 LEU n 
1 164 THR n 
1 165 ASN n 
1 166 ASN n 
1 167 ALA n 
1 168 LYS n 
1 169 THR n 
1 170 ILE n 
1 171 ILE n 
1 172 VAL n 
1 173 HIS n 
1 174 LEU n 
1 175 ASN n 
1 176 LYS n 
1 177 SER n 
1 178 VAL n 
1 179 GLU n 
1 180 ILE n 
1 181 ASN n 
1 182 CYS n 
1 183 THR n 
1 184 ARG n 
1 185 PRO n 
1 186 SER n 
1 187 ASN n 
1 188 GLY n 
1 189 GLY n 
1 190 SER n 
1 191 GLY n 
1 192 SER n 
1 193 GLY n 
1 194 GLY n 
1 195 ASP n 
1 196 ILE n 
1 197 ARG n 
1 198 LYS n 
1 199 ALA n 
1 200 TYR n 
1 201 CYS n 
1 202 GLU n 
1 203 ILE n 
1 204 ASN n 
1 205 GLY n 
1 206 THR n 
1 207 LYS n 
1 208 TRP n 
1 209 ASN n 
1 210 LYS n 
1 211 VAL n 
1 212 LEU n 
1 213 LYS n 
1 214 GLN n 
1 215 VAL n 
1 216 THR n 
1 217 GLU n 
1 218 LYS n 
1 219 LEU n 
1 220 LYS n 
1 221 GLU n 
1 222 HIS n 
1 223 PHE n 
1 224 ASN n 
1 225 ASN n 
1 226 LYS n 
1 227 THR n 
1 228 ILE n 
1 229 ILE n 
1 230 PHE n 
1 231 GLN n 
1 232 PRO n 
1 233 PRO n 
1 234 SER n 
1 235 GLY n 
1 236 GLY n 
1 237 ASP n 
1 238 LEU n 
1 239 GLU n 
1 240 ILE n 
1 241 THR n 
1 242 MET n 
1 243 HIS n 
1 244 SER n 
1 245 PHE n 
1 246 ASN n 
1 247 CYS n 
1 248 ARG n 
1 249 GLY n 
1 250 GLU n 
1 251 PHE n 
1 252 PHE n 
1 253 TYR n 
1 254 CYS n 
1 255 ASN n 
1 256 THR n 
1 257 THR n 
1 258 GLN n 
1 259 LEU n 
1 260 PHE n 
1 261 ASN n 
1 262 ASN n 
1 263 THR n 
1 264 CYS n 
1 265 ILE n 
1 266 GLY n 
1 267 ASN n 
1 268 GLU n 
1 269 THR n 
1 270 MET n 
1 271 LYS n 
1 272 GLY n 
1 273 CYS n 
1 274 ASN n 
1 275 GLY n 
1 276 THR n 
1 277 ILE n 
1 278 THR n 
1 279 LEU n 
1 280 PRO n 
1 281 CYS n 
1 282 LYS n 
1 283 ILE n 
1 284 LYS n 
1 285 GLN n 
1 286 ILE n 
1 287 ILE n 
1 288 ASN n 
1 289 MET n 
1 290 TRP n 
1 291 GLN n 
1 292 GLY n 
1 293 THR n 
1 294 GLY n 
1 295 GLN n 
1 296 ALA n 
1 297 MET n 
1 298 TYR n 
1 299 ALA n 
1 300 PRO n 
1 301 PRO n 
1 302 ILE n 
1 303 ASP n 
1 304 GLY n 
1 305 LYS n 
1 306 ILE n 
1 307 ASN n 
1 308 CYS n 
1 309 VAL n 
1 310 SER n 
1 311 ASN n 
1 312 ILE n 
1 313 THR n 
1 314 GLY n 
1 315 ILE n 
1 316 LEU n 
1 317 LEU n 
1 318 THR n 
1 319 ARG n 
1 320 ASP n 
1 321 GLY n 
1 322 GLY n 
1 323 ALA n 
1 324 ASN n 
1 325 ASN n 
1 326 THR n 
1 327 SER n 
1 328 ASN n 
1 329 GLU n 
1 330 THR n 
1 331 PHE n 
1 332 ARG n 
1 333 PRO n 
1 334 GLY n 
1 335 GLY n 
1 336 GLY n 
1 337 ASP n 
1 338 MET n 
1 339 ARG n 
1 340 ASP n 
1 341 ASN n 
1 342 TRP n 
1 343 ARG n 
1 344 SER n 
1 345 GLU n 
1 346 LEU n 
1 347 TYR n 
1 348 LYS n 
1 349 TYR n 
1 350 LYS n 
1 351 VAL n 
1 352 VAL n 
1 353 GLN n 
1 354 ILE n 
1 355 GLU 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                   355 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'HIV-1 Env' 
_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      'Human immunodeficiency virus 1' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     11676 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     9606 
_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            'HEK 293 GnT1-' 
_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          plasmid 
_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 
A1ATE non-polymer                  . 
'(3S,5R)-1-[4-(1-carbamimidoyl-L-prolyl)piperazine-1-carbonyl]-N-(4-chloro-3-fluorophenyl)-5-(hydroxymethyl)piperidine-3-carboxamide' 
? 'C24 H33 Cl F N7 O4' 538.015 
ALA   'L-peptide linking'          y ALANINE ? 'C3 H7 N O2'         89.093  
ARG   'L-peptide linking'          y ARGININE ? 'C6 H15 N4 O2 1'     175.209 
ASN   'L-peptide linking'          y ASPARAGINE ? 'C4 H8 N2 O3'        132.118 
ASP   'L-peptide linking'          y 'ASPARTIC ACID' ? 'C4 H7 N O4'         133.103 
CYS   'L-peptide linking'          y CYSTEINE ? 'C3 H7 N O2 S'       121.158 
EPE   non-polymer                  . '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' HEPES 'C8 H18 N2 O4 S'     238.305 
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 
NAG   'D-saccharide, beta linking' . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'        221.208 
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_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
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   VAL 1   42  ?   ?   ?   A . n 
A 1 2   PRO 2   43  43  PRO PRO A . n 
A 1 3   VAL 3   44  44  VAL VAL A . n 
A 1 4   TRP 4   45  45  TRP TRP A . n 
A 1 5   LYS 5   46  46  LYS LYS A . n 
A 1 6   ASP 6   47  47  ASP ASP A . n 
A 1 7   ALA 7   48  48  ALA ALA A . n 
A 1 8   ASP 8   49  49  ASP ASP A . n 
A 1 9   THR 9   50  50  THR THR A . n 
A 1 10  THR 10  51  51  THR THR A . n 
A 1 11  LEU 11  52  52  LEU LEU A . n 
A 1 12  PHE 12  53  53  PHE PHE A . n 
A 1 13  CYS 13  54  54  CYS CYS A . n 
A 1 14  ALA 14  55  55  ALA ALA A . n 
A 1 15  SER 15  56  56  SER SER A . n 
A 1 16  ASP 16  57  57  ASP ASP A . n 
A 1 17  ALA 17  58  58  ALA ALA A . n 
A 1 18  LYS 18  59  59  LYS LYS A . n 
A 1 19  ALA 19  60  60  ALA ALA A . n 
A 1 20  TYR 20  61  61  TYR TYR A . n 
A 1 21  GLU 21  62  62  GLU GLU A . n 
A 1 22  THR 22  63  63  THR THR A . n 
A 1 23  GLU 23  64  64  GLU GLU A . n 
A 1 24  VAL 24  65  65  VAL VAL A . n 
A 1 25  HIS 25  66  66  HIS HIS A . n 
A 1 26  ASN 26  67  67  ASN ASN A . n 
A 1 27  VAL 27  68  68  VAL VAL A . n 
A 1 28  TRP 28  69  69  TRP TRP A . n 
A 1 29  ALA 29  70  70  ALA ALA A . n 
A 1 30  THR 30  71  71  THR THR A . n 
A 1 31  HIS 31  72  72  HIS HIS A . n 
A 1 32  ALA 32  73  73  ALA ALA A . n 
A 1 33  CYS 33  74  74  CYS CYS A . n 
A 1 34  VAL 34  75  75  VAL VAL A . n 
A 1 35  PRO 35  76  76  PRO PRO A . n 
A 1 36  THR 36  77  77  THR THR A . n 
A 1 37  ASP 37  78  78  ASP ASP A . n 
A 1 38  PRO 38  79  79  PRO PRO A . n 
A 1 39  ASN 39  80  80  ASN ASN A . n 
A 1 40  PRO 40  81  81  PRO PRO A . n 
A 1 41  GLN 41  82  82  GLN GLN A . n 
A 1 42  GLU 42  83  83  GLU GLU A . n 
A 1 43  ILE 43  84  84  ILE ILE A . n 
A 1 44  HIS 44  85  85  HIS HIS A . n 
A 1 45  LEU 45  86  86  LEU LEU A . n 
A 1 46  GLU 46  87  87  GLU GLU A . n 
A 1 47  ASN 47  88  88  ASN ASN A . n 
A 1 48  VAL 48  89  89  VAL VAL A . n 
A 1 49  THR 49  90  90  THR THR A . n 
A 1 50  GLU 50  91  91  GLU GLU A . n 
A 1 51  ASN 51  92  92  ASN ASN A . n 
A 1 52  PHE 52  93  93  PHE PHE A . n 
A 1 53  ASN 53  94  94  ASN ASN A . n 
A 1 54  MET 54  95  95  MET MET A . n 
A 1 55  TRP 55  96  96  TRP TRP A . n 
A 1 56  LYS 56  97  97  LYS LYS A . n 
A 1 57  ASN 57  98  98  ASN ASN A . n 
A 1 58  ASN 58  99  99  ASN ASN A . n 
A 1 59  MET 59  100 100 MET MET A . n 
A 1 60  VAL 60  101 101 VAL VAL A . n 
A 1 61  GLU 61  102 102 GLU GLU A . n 
A 1 62  GLN 62  103 103 GLN GLN A . n 
A 1 63  MET 63  104 104 MET MET A . n 
A 1 64  HIS 64  105 105 HIS HIS A . n 
A 1 65  GLU 65  106 106 GLU GLU A . n 
A 1 66  ASP 66  107 107 ASP ASP A . n 
A 1 67  ILE 67  108 108 ILE ILE A . n 
A 1 68  ILE 68  109 109 ILE ILE A . n 
A 1 69  SER 69  110 110 SER SER A . n 
A 1 70  LEU 70  111 111 LEU LEU A . n 
A 1 71  TRP 71  112 112 TRP TRP A . n 
A 1 72  ASP 72  113 113 ASP ASP A . n 
A 1 73  GLN 73  114 114 GLN GLN A . n 
A 1 74  SER 74  115 115 SER SER A . n 
A 1 75  LEU 75  116 116 LEU LEU A . n 
A 1 76  GLN 76  117 117 GLN GLN A . n 
A 1 77  PRO 77  118 118 PRO PRO A . n 
A 1 78  CYS 78  119 119 CYS CYS A . n 
A 1 79  VAL 79  120 120 VAL VAL A . n 
A 1 80  LYS 80  121 121 LYS LYS A . n 
A 1 81  LEU 81  122 122 LEU LEU A . n 
A 1 82  THR 82  123 123 THR THR A . n 
A 1 83  GLY 83  124 124 GLY GLY A . n 
A 1 84  GLY 84  198 198 GLY GLY A . n 
A 1 85  SER 85  199 199 SER SER A . n 
A 1 86  VAL 86  200 200 VAL VAL A . n 
A 1 87  ILE 87  201 201 ILE ILE A . n 
A 1 88  LYS 88  202 202 LYS LYS A . n 
A 1 89  GLN 89  203 203 GLN GLN A . n 
A 1 90  ALA 90  204 204 ALA ALA A . n 
A 1 91  CYS 91  205 205 CYS CYS A . n 
A 1 92  PRO 92  206 206 PRO PRO A . n 
A 1 93  LYS 93  207 207 LYS LYS A . n 
A 1 94  ILE 94  208 208 ILE ILE A . n 
A 1 95  SER 95  209 209 SER SER A . n 
A 1 96  PHE 96  210 210 PHE PHE A . n 
A 1 97  ASP 97  211 211 ASP ASP A . n 
A 1 98  PRO 98  212 212 PRO PRO A . n 
A 1 99  ILE 99  213 213 ILE ILE A . n 
A 1 100 PRO 100 214 214 PRO PRO A . n 
A 1 101 ILE 101 215 215 ILE ILE A . n 
A 1 102 HIS 102 216 216 HIS HIS A . n 
A 1 103 TYR 103 217 217 TYR TYR A . n 
A 1 104 CYS 104 218 218 CYS CYS A . n 
A 1 105 THR 105 219 219 THR THR A . n 
A 1 106 PRO 106 220 220 PRO PRO A . n 
A 1 107 ALA 107 221 221 ALA ALA A . n 
A 1 108 GLY 108 222 222 GLY GLY A . n 
A 1 109 TYR 109 223 223 TYR TYR A . n 
A 1 110 VAL 110 224 224 VAL VAL A . n 
A 1 111 ILE 111 225 225 ILE ILE A . n 
A 1 112 LEU 112 226 226 LEU LEU A . n 
A 1 113 LYS 113 227 227 LYS LYS A . n 
A 1 114 CYS 114 228 228 CYS CYS A . n 
A 1 115 ASN 115 229 229 ASN ASN A . n 
A 1 116 ASP 116 230 230 ASP ASP A . n 
A 1 117 LYS 117 231 231 LYS LYS A . n 
A 1 118 ASN 118 232 232 ASN ASN A . n 
A 1 119 PHE 119 233 233 PHE PHE A . n 
A 1 120 ASN 120 234 234 ASN ASN A . n 
A 1 121 GLY 121 235 235 GLY GLY A . n 
A 1 122 THR 122 236 236 THR THR A . n 
A 1 123 GLY 123 237 237 GLY GLY A . n 
A 1 124 PRO 124 238 238 PRO PRO A . n 
A 1 125 CYS 125 239 239 CYS CYS A . n 
A 1 126 LYS 126 240 240 LYS LYS A . n 
A 1 127 ASN 127 241 241 ASN ASN A . n 
A 1 128 VAL 128 242 242 VAL VAL A . n 
A 1 129 SER 129 243 243 SER SER A . n 
A 1 130 SER 130 244 244 SER SER A . n 
A 1 131 VAL 131 245 245 VAL VAL A . n 
A 1 132 GLN 132 246 246 GLN GLN A . n 
A 1 133 CYS 133 247 247 CYS CYS A . n 
A 1 134 THR 134 248 248 THR THR A . n 
A 1 135 HIS 135 249 249 HIS HIS A . n 
A 1 136 GLY 136 250 250 GLY GLY A . n 
A 1 137 ILE 137 251 251 ILE ILE A . n 
A 1 138 LYS 138 252 252 LYS LYS A . n 
A 1 139 PRO 139 253 253 PRO PRO A . n 
A 1 140 VAL 140 254 254 VAL VAL A . n 
A 1 141 VAL 141 255 255 VAL VAL A . n 
A 1 142 SER 142 256 256 SER SER A . n 
A 1 143 THR 143 257 257 THR THR A . n 
A 1 144 GLN 144 258 258 GLN GLN A . n 
A 1 145 LEU 145 259 259 LEU LEU A . n 
A 1 146 LEU 146 260 260 LEU LEU A . n 
A 1 147 LEU 147 261 261 LEU LEU A . n 
A 1 148 ASN 148 262 262 ASN ASN A . n 
A 1 149 GLY 149 263 263 GLY GLY A . n 
A 1 150 SER 150 264 264 SER SER A . n 
A 1 151 LEU 151 265 265 LEU LEU A . n 
A 1 152 ALA 152 266 266 ALA ALA A . n 
A 1 153 GLU 153 267 267 GLU GLU A . n 
A 1 154 GLU 154 268 268 GLU GLU A . n 
A 1 155 GLU 155 269 269 GLU GLU A . n 
A 1 156 ILE 156 270 270 ILE ILE A . n 
A 1 157 ILE 157 271 271 ILE ILE A . n 
A 1 158 ILE 158 272 272 ILE ILE A . n 
A 1 159 ARG 159 273 273 ARG ARG A . n 
A 1 160 SER 160 274 274 SER SER A . n 
A 1 161 GLU 161 275 275 GLU GLU A . n 
A 1 162 ASN 162 276 276 ASN ASN A . n 
A 1 163 LEU 163 277 277 LEU LEU A . n 
A 1 164 THR 164 278 278 THR THR A . n 
A 1 165 ASN 165 279 279 ASN ASN A . n 
A 1 166 ASN 166 280 280 ASN ASN A . n 
A 1 167 ALA 167 281 281 ALA ALA A . n 
A 1 168 LYS 168 282 282 LYS LYS A . n 
A 1 169 THR 169 283 283 THR THR A . n 
A 1 170 ILE 170 284 284 ILE ILE A . n 
A 1 171 ILE 171 285 285 ILE ILE A . n 
A 1 172 VAL 172 286 286 VAL VAL A . n 
A 1 173 HIS 173 287 287 HIS HIS A . n 
A 1 174 LEU 174 288 288 LEU LEU A . n 
A 1 175 ASN 175 289 289 ASN ASN A . n 
A 1 176 LYS 176 290 290 LYS LYS A . n 
A 1 177 SER 177 291 291 SER SER A . n 
A 1 178 VAL 178 292 292 VAL VAL A . n 
A 1 179 GLU 179 293 293 GLU GLU A . n 
A 1 180 ILE 180 294 294 ILE ILE A . n 
A 1 181 ASN 181 295 295 ASN ASN A . n 
A 1 182 CYS 182 296 296 CYS CYS A . n 
A 1 183 THR 183 297 297 THR THR A . n 
A 1 184 ARG 184 298 298 ARG ARG A . n 
A 1 185 PRO 185 299 299 PRO PRO A . n 
A 1 186 SER 186 300 300 SER SER A . n 
A 1 187 ASN 187 301 301 ASN ASN A . n 
A 1 188 GLY 188 318 ?   ?   ?   A . n 
A 1 189 GLY 189 319 ?   ?   ?   A . n 
A 1 190 SER 190 320 ?   ?   ?   A . n 
A 1 191 GLY 191 321 ?   ?   ?   A . n 
A 1 192 SER 192 322 ?   ?   ?   A . n 
A 1 193 GLY 193 323 ?   ?   ?   A . n 
A 1 194 GLY 194 324 ?   ?   ?   A . n 
A 1 195 ASP 195 325 325 ASP ASP A . n 
A 1 196 ILE 196 326 326 ILE ILE A . n 
A 1 197 ARG 197 327 327 ARG ARG A . n 
A 1 198 LYS 198 328 328 LYS LYS A . n 
A 1 199 ALA 199 329 329 ALA ALA A . n 
A 1 200 TYR 200 330 330 TYR TYR A . n 
A 1 201 CYS 201 331 331 CYS CYS A . n 
A 1 202 GLU 202 332 332 GLU GLU A . n 
A 1 203 ILE 203 333 333 ILE ILE A . n 
A 1 204 ASN 204 334 334 ASN ASN A . n 
A 1 205 GLY 205 335 335 GLY GLY A . n 
A 1 206 THR 206 336 336 THR THR A . n 
A 1 207 LYS 207 337 337 LYS LYS A . n 
A 1 208 TRP 208 338 338 TRP TRP A . n 
A 1 209 ASN 209 339 339 ASN ASN A . n 
A 1 210 LYS 210 340 340 LYS LYS A . n 
A 1 211 VAL 211 341 341 VAL VAL A . n 
A 1 212 LEU 212 342 342 LEU LEU A . n 
A 1 213 LYS 213 343 343 LYS LYS A . n 
A 1 214 GLN 214 344 344 GLN GLN A . n 
A 1 215 VAL 215 345 345 VAL VAL A . n 
A 1 216 THR 216 346 346 THR THR A . n 
A 1 217 GLU 217 347 347 GLU GLU A . n 
A 1 218 LYS 218 348 348 LYS LYS A . n 
A 1 219 LEU 219 349 349 LEU LEU A . n 
A 1 220 LYS 220 350 350 LYS LYS A . n 
A 1 221 GLU 221 351 351 GLU GLU A . n 
A 1 222 HIS 222 352 352 HIS HIS A . n 
A 1 223 PHE 223 353 353 PHE PHE A . n 
A 1 224 ASN 224 354 354 ASN ASN A . n 
A 1 225 ASN 225 355 355 ASN ASN A . n 
A 1 226 LYS 226 357 357 LYS LYS A . n 
A 1 227 THR 227 358 358 THR THR A . n 
A 1 228 ILE 228 359 359 ILE ILE A . n 
A 1 229 ILE 229 360 360 ILE ILE A . n 
A 1 230 PHE 230 361 361 PHE PHE A . n 
A 1 231 GLN 231 362 362 GLN GLN A . n 
A 1 232 PRO 232 363 363 PRO PRO A . n 
A 1 233 PRO 233 364 364 PRO PRO A . n 
A 1 234 SER 234 365 365 SER SER A . n 
A 1 235 GLY 235 366 366 GLY GLY A . n 
A 1 236 GLY 236 367 367 GLY GLY A . n 
A 1 237 ASP 237 368 368 ASP ASP A . n 
A 1 238 LEU 238 369 369 LEU LEU A . n 
A 1 239 GLU 239 370 370 GLU GLU A . n 
A 1 240 ILE 240 371 371 ILE ILE A . n 
A 1 241 THR 241 372 372 THR THR A . n 
A 1 242 MET 242 373 373 MET MET A . n 
A 1 243 HIS 243 374 374 HIS HIS A . n 
A 1 244 SER 244 375 375 SER SER A . n 
A 1 245 PHE 245 376 376 PHE PHE A . n 
A 1 246 ASN 246 377 377 ASN ASN A . n 
A 1 247 CYS 247 378 378 CYS CYS A . n 
A 1 248 ARG 248 379 379 ARG ARG A . n 
A 1 249 GLY 249 380 380 GLY GLY A . n 
A 1 250 GLU 250 381 381 GLU GLU A . n 
A 1 251 PHE 251 382 382 PHE PHE A . n 
A 1 252 PHE 252 383 383 PHE PHE A . n 
A 1 253 TYR 253 384 384 TYR TYR A . n 
A 1 254 CYS 254 385 385 CYS CYS A . n 
A 1 255 ASN 255 386 386 ASN ASN A . n 
A 1 256 THR 256 387 387 THR THR A . n 
A 1 257 THR 257 388 388 THR THR A . n 
A 1 258 GLN 258 389 389 GLN GLN A . n 
A 1 259 LEU 259 390 390 LEU LEU A . n 
A 1 260 PHE 260 391 391 PHE PHE A . n 
A 1 261 ASN 261 392 392 ASN ASN A . n 
A 1 262 ASN 262 393 393 ASN ASN A . n 
A 1 263 THR 263 394 394 THR THR A . n 
A 1 264 CYS 264 395 395 CYS CYS A . n 
A 1 265 ILE 265 402 ?   ?   ?   A . n 
A 1 266 GLY 266 403 ?   ?   ?   A . n 
A 1 267 ASN 267 404 ?   ?   ?   A . n 
A 1 268 GLU 268 405 ?   ?   ?   A . n 
A 1 269 THR 269 406 ?   ?   ?   A . n 
A 1 270 MET 270 407 ?   ?   ?   A . n 
A 1 271 LYS 271 408 408 LYS LYS A . n 
A 1 272 GLY 272 409 409 GLY GLY A . n 
A 1 273 CYS 273 410 410 CYS CYS A . n 
A 1 274 ASN 274 411 411 ASN ASN A . n 
A 1 275 GLY 275 412 412 GLY GLY A . n 
A 1 276 THR 276 413 413 THR THR A . n 
A 1 277 ILE 277 414 414 ILE ILE A . n 
A 1 278 THR 278 415 415 THR THR A . n 
A 1 279 LEU 279 416 416 LEU LEU A . n 
A 1 280 PRO 280 417 417 PRO PRO A . n 
A 1 281 CYS 281 418 418 CYS CYS A . n 
A 1 282 LYS 282 419 419 LYS LYS A . n 
A 1 283 ILE 283 420 420 ILE ILE A . n 
A 1 284 LYS 284 421 421 LYS LYS A . n 
A 1 285 GLN 285 422 422 GLN GLN A . n 
A 1 286 ILE 286 423 423 ILE ILE A . n 
A 1 287 ILE 287 424 424 ILE ILE A . n 
A 1 288 ASN 288 425 425 ASN ASN A . n 
A 1 289 MET 289 426 426 MET MET A . n 
A 1 290 TRP 290 427 427 TRP TRP A . n 
A 1 291 GLN 291 428 428 GLN GLN A . n 
A 1 292 GLY 292 429 429 GLY GLY A . n 
A 1 293 THR 293 430 430 THR THR A . n 
A 1 294 GLY 294 431 431 GLY GLY A . n 
A 1 295 GLN 295 432 432 GLN GLN A . n 
A 1 296 ALA 296 433 433 ALA ALA A . n 
A 1 297 MET 297 434 434 MET MET A . n 
A 1 298 TYR 298 435 435 TYR TYR A . n 
A 1 299 ALA 299 436 436 ALA ALA A . n 
A 1 300 PRO 300 437 437 PRO PRO A . n 
A 1 301 PRO 301 438 438 PRO PRO A . n 
A 1 302 ILE 302 439 439 ILE ILE A . n 
A 1 303 ASP 303 440 440 ASP ASP A . n 
A 1 304 GLY 304 441 441 GLY GLY A . n 
A 1 305 LYS 305 442 442 LYS LYS A . n 
A 1 306 ILE 306 443 443 ILE ILE A . n 
A 1 307 ASN 307 444 444 ASN ASN A . n 
A 1 308 CYS 308 445 445 CYS CYS A . n 
A 1 309 VAL 309 446 446 VAL VAL A . n 
A 1 310 SER 310 447 447 SER SER A . n 
A 1 311 ASN 311 448 448 ASN ASN A . n 
A 1 312 ILE 312 449 449 ILE ILE A . n 
A 1 313 THR 313 450 450 THR THR A . n 
A 1 314 GLY 314 451 451 GLY GLY A . n 
A 1 315 ILE 315 452 452 ILE ILE A . n 
A 1 316 LEU 316 453 453 LEU LEU A . n 
A 1 317 LEU 317 454 454 LEU LEU A . n 
A 1 318 THR 318 455 455 THR THR A . n 
A 1 319 ARG 319 456 456 ARG ARG A . n 
A 1 320 ASP 320 457 457 ASP ASP A . n 
A 1 321 GLY 321 458 458 GLY GLY A . n 
A 1 322 GLY 322 459 459 GLY GLY A . n 
A 1 323 ALA 323 460 460 ALA ALA A . n 
A 1 324 ASN 324 461 461 ASN ASN A . n 
A 1 325 ASN 325 462 462 ASN ASN A . n 
A 1 326 THR 326 463 463 THR THR A . n 
A 1 327 SER 327 464 464 SER SER A . n 
A 1 328 ASN 328 465 465 ASN ASN A . n 
A 1 329 GLU 329 466 466 GLU GLU A . n 
A 1 330 THR 330 467 467 THR THR A . n 
A 1 331 PHE 331 468 468 PHE PHE A . n 
A 1 332 ARG 332 469 469 ARG ARG A . n 
A 1 333 PRO 333 470 470 PRO PRO A . n 
A 1 334 GLY 334 471 471 GLY GLY A . n 
A 1 335 GLY 335 472 472 GLY GLY A . n 
A 1 336 GLY 336 473 473 GLY GLY A . n 
A 1 337 ASP 337 474 474 ASP ASP A . n 
A 1 338 MET 338 475 475 MET MET A . n 
A 1 339 ARG 339 476 476 ARG ARG A . n 
A 1 340 ASP 340 477 477 ASP ASP A . n 
A 1 341 ASN 341 478 478 ASN ASN A . n 
A 1 342 TRP 342 479 479 TRP TRP A . n 
A 1 343 ARG 343 480 480 ARG ARG A . n 
A 1 344 SER 344 481 481 SER SER A . n 
A 1 345 GLU 345 482 482 GLU GLU A . n 
A 1 346 LEU 346 483 483 LEU LEU A . n 
A 1 347 TYR 347 484 484 TYR TYR A . n 
A 1 348 LYS 348 485 485 LYS LYS A . n 
A 1 349 TYR 349 486 486 TYR TYR A . n 
A 1 350 LYS 350 487 487 LYS LYS A . n 
A 1 351 VAL 351 488 488 VAL VAL A . n 
A 1 352 VAL 352 489 489 VAL VAL A . n 
A 1 353 GLN 353 490 490 GLN GLN A . n 
A 1 354 ILE 354 491 491 ILE ILE A . n 
A 1 355 GLU 355 492 492 GLU GLU A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1ATE 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ATE 
_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 NAG   1  501 501 NAG   NAG A . 
C 2 NAG   1  502 502 NAG   NAG A . 
D 2 NAG   1  503 503 NAG   NAG A . 
E 2 NAG   1  504 504 NAG   NAG A . 
F 2 NAG   1  505 505 NAG   NAG A . 
G 2 NAG   1  506 506 NAG   NAG A . 
H 2 NAG   1  507 507 NAG   NAG A . 
I 2 NAG   1  508 508 NAG   NAG A . 
J 2 NAG   1  509 510 NAG   NAG A . 
K 3 EPE   1  510 512 EPE   EPE A . 
L 4 A1ATE 1  511 1   A1ATE MW5 A . 
M 5 HOH   1  601 17  HOH   HOH A . 
M 5 HOH   2  602 21  HOH   HOH A . 
M 5 HOH   3  603 43  HOH   HOH A . 
M 5 HOH   4  604 75  HOH   HOH A . 
M 5 HOH   5  605 41  HOH   HOH A . 
M 5 HOH   6  606 15  HOH   HOH A . 
M 5 HOH   7  607 53  HOH   HOH A . 
M 5 HOH   8  608 6   HOH   HOH A . 
M 5 HOH   9  609 29  HOH   HOH A . 
M 5 HOH   10 610 7   HOH   HOH A . 
M 5 HOH   11 611 10  HOH   HOH A . 
M 5 HOH   12 612 32  HOH   HOH A . 
M 5 HOH   13 613 8   HOH   HOH A . 
M 5 HOH   14 614 50  HOH   HOH A . 
M 5 HOH   15 615 5   HOH   HOH A . 
M 5 HOH   16 616 25  HOH   HOH A . 
M 5 HOH   17 617 19  HOH   HOH A . 
M 5 HOH   18 618 73  HOH   HOH A . 
M 5 HOH   19 619 46  HOH   HOH A . 
M 5 HOH   20 620 37  HOH   HOH A . 
M 5 HOH   21 621 55  HOH   HOH A . 
M 5 HOH   22 622 38  HOH   HOH A . 
M 5 HOH   23 623 70  HOH   HOH A . 
M 5 HOH   24 624 12  HOH   HOH A . 
M 5 HOH   25 625 1   HOH   HOH A . 
M 5 HOH   26 626 11  HOH   HOH A . 
M 5 HOH   27 627 9   HOH   HOH A . 
M 5 HOH   28 628 26  HOH   HOH A . 
M 5 HOH   29 629 24  HOH   HOH A . 
M 5 HOH   30 630 16  HOH   HOH A . 
M 5 HOH   31 631 13  HOH   HOH A . 
M 5 HOH   32 632 28  HOH   HOH A . 
M 5 HOH   33 633 33  HOH   HOH A . 
M 5 HOH   34 634 47  HOH   HOH A . 
M 5 HOH   35 635 30  HOH   HOH A . 
M 5 HOH   36 636 31  HOH   HOH A . 
M 5 HOH   37 637 14  HOH   HOH A . 
M 5 HOH   38 638 2   HOH   HOH A . 
M 5 HOH   39 639 27  HOH   HOH A . 
M 5 HOH   40 640 54  HOH   HOH A . 
M 5 HOH   41 641 52  HOH   HOH A . 
M 5 HOH   42 642 64  HOH   HOH A . 
M 5 HOH   43 643 71  HOH   HOH A . 
M 5 HOH   44 644 4   HOH   HOH A . 
M 5 HOH   45 645 39  HOH   HOH A . 
M 5 HOH   46 646 76  HOH   HOH A . 
M 5 HOH   47 647 3   HOH   HOH A . 
M 5 HOH   48 648 23  HOH   HOH A . 
M 5 HOH   49 649 34  HOH   HOH A . 
M 5 HOH   50 650 51  HOH   HOH A . 
M 5 HOH   51 651 40  HOH   HOH A . 
M 5 HOH   52 652 62  HOH   HOH A . 
M 5 HOH   53 653 35  HOH   HOH A . 
M 5 HOH   54 654 48  HOH   HOH A . 
M 5 HOH   55 655 72  HOH   HOH A . 
M 5 HOH   56 656 18  HOH   HOH A . 
M 5 HOH   57 657 36  HOH   HOH A . 
M 5 HOH   58 658 74  HOH   HOH A . 
M 5 HOH   59 659 58  HOH   HOH A . 
M 5 HOH   60 660 56  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       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.20.1_4487: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BXY 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     66.467 
_cell.length_a_esd                 ? 
_cell.length_b                     67.686 
_cell.length_b_esd                 ? 
_cell.length_c                     87.389 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9BXY 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   9BXY 
_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             2.49 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.63 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;10% PEG 3350
5% PEG 400
0.1 M HEPES pH 7.5
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            294 
# 
_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 EIGER2 S 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-03-18 
_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                    'Si(111)' 
_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   0.97946 
_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                        'SSRL BEAMLINE BL12-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97946 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL12-2 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9BXY 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.1 
_reflns.d_resolution_low                               50 
_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                                     18965 
_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                           82.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          24.7 
_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                                0.039 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.0 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.078 
_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                                    2.1 
_reflns_shell.d_res_low                                     2.14 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             944 
_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                               3.7 
_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                               0.57 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.5 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          84.2 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9BXY 
_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                            2.11 
_refine.ls_d_res_low                             36.71 
_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                     18941 
_refine.ls_number_reflns_R_free                  934 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    81.77 
_refine.ls_percent_reflns_R_free                 4.93 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1985 
_refine.ls_R_factor_R_free                       0.2525 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1959 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.37 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 28.43 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.36 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2675 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         178 
_refine_hist.number_atoms_solvent             60 
_refine_hist.number_atoms_total               2913 
_refine_hist.d_res_high                       2.11 
_refine_hist.d_res_low                        36.71 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.009  ? 2913 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.206  ? 3956 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 11.880 ? 431  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.062  ? 464  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 495  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.11 2.23  . . 119 2459 80.00 . . . . 0.3276 . . . . . . . . . . . 0.3719 
'X-RAY DIFFRACTION' 2.23 2.36  . . 141 2623 85.00 . . . . 0.2825 . . . . . . . . . . . 0.3581 
'X-RAY DIFFRACTION' 2.37 2.55  . . 167 2505 82.00 . . . . 0.2684 . . . . . . . . . . . 0.3387 
'X-RAY DIFFRACTION' 2.55 2.80  . . 131 2621 84.00 . . . . 0.2380 . . . . . . . . . . . 0.2772 
'X-RAY DIFFRACTION' 2.80 3.21  . . 108 2666 84.00 . . . . 0.2157 . . . . . . . . . . . 0.2554 
'X-RAY DIFFRACTION' 3.21 4.04  . . 144 2590 82.00 . . . . 0.1805 . . . . . . . . . . . 0.2581 
'X-RAY DIFFRACTION' 4.04 36.71 . . 124 2543 76.00 . . . . 0.1574 . . . . . . . . . . . 0.1962 
# 
_struct.entry_id                     9BXY 
_struct.title                        'CRYSTAL STRUCTURE OF HIV-1 LM/HS CLADE A/E CRF01 GP120 CORE IN COMPLEX WITH DL-III-117' 
_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        9BXY 
_struct_keywords.text            'HIV-1 GP120, CLADE A/E CF01, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
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 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 2 ? 
K N N 3 ? 
L N N 4 ? 
M N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A0M3KKW9_9HIV1 
_struct_ref.pdbx_db_accession          A0A0M3KKW9 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VWKDADTTLFCASDAKAHETEVHNVWATHACVPTDPNPQEIHLENVTENFNMWKNNMVEQMQEDVISLWDQSLQPCVKLT
GGSVIKQACPKISFDPIPIHYCTPAGYVILKCNDKNFNGTGPCKNVSSVQCTHGIKPVVSTQLLLNGSLAEEEIIIRSEN
LTNNAKTIIVHLNKSVEINCTRPSNGGSGSGGDIRKAYCEINGTKWNKVLKQVTEKLKEHFNNKTIIFQPPSGGDLEITM
HHFNCRGEFFYCNTTQLFNNTCIGNETMKGCNGTITLPCKIKQIINMWQGTGQAMYAPPIDGKINCVSNITGILLTRDGG
ANNTSNETFRPGGGNIKDNWRSELYKYKVVQIE
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9BXY 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 3 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 355 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A0M3KKW9 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  353 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       44 
_struct_ref_seq.pdbx_auth_seq_align_end       492 
# 
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 9BXY VAL A 1   ? UNP A0A0M3KKW9 ?   ?   'expression tag'      42  1 
1 9BXY PRO A 2   ? UNP A0A0M3KKW9 ?   ?   'expression tag'      43  2 
1 9BXY TYR A 20  ? UNP A0A0M3KKW9 HIS 18  'engineered mutation' 61  3 
1 9BXY HIS A 64  ? UNP A0A0M3KKW9 GLN 62  'engineered mutation' 105 4 
1 9BXY ILE A 67  ? UNP A0A0M3KKW9 VAL 65  'engineered mutation' 108 5 
1 9BXY SER A 244 ? UNP A0A0M3KKW9 HIS 242 'engineered mutation' 375 6 
1 9BXY ASP A 337 ? UNP A0A0M3KKW9 ASN 335 'engineered mutation' 474 7 
1 9BXY MET A 338 ? UNP A0A0M3KKW9 ILE 336 'engineered mutation' 475 8 
1 9BXY ARG A 339 ? UNP A0A0M3KKW9 LYS 337 'engineered mutation' 476 9 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M 
# 
_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 GLU A 23  ? CYS A 33  ? GLU A 64  CYS A 74  1 ? 11 
HELX_P HELX_P2 AA2 ASN A 57  ? LEU A 75  ? ASN A 98  LEU A 116 1 ? 19 
HELX_P HELX_P3 AA3 GLY A 205 ? PHE A 223 ? GLY A 335 PHE A 353 1 ? 19 
HELX_P HELX_P4 AA4 ASP A 237 ? MET A 242 ? ASP A 368 MET A 373 1 ? 6  
HELX_P HELX_P5 AA5 MET A 338 ? TYR A 347 ? MET A 475 TYR A 484 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ?   ? A CYS 13  SG  ? ? ? 1_555 A CYS 33  SG ? ? A CYS 54  A CYS 74  1_555 ? ? ? ? ? ? ? 2.048 ? ?               
disulf2 disulf ?   ? A CYS 78  SG  ? ? ? 1_555 A CYS 91  SG ? ? A CYS 119 A CYS 205 1_555 ? ? ? ? ? ? ? 2.038 ? ?               
disulf3 disulf ?   ? A CYS 104 SG  ? ? ? 1_555 A CYS 133 SG ? ? A CYS 218 A CYS 247 1_555 ? ? ? ? ? ? ? 2.082 ? ?               
disulf4 disulf ?   ? A CYS 114 SG  ? ? ? 1_555 A CYS 125 SG ? ? A CYS 228 A CYS 239 1_555 ? ? ? ? ? ? ? 2.062 ? ?               
disulf5 disulf ?   ? A CYS 182 SG  ? ? ? 1_555 A CYS 201 SG ? ? A CYS 296 A CYS 331 1_555 ? ? ? ? ? ? ? 2.084 ? ?               
disulf6 disulf ?   ? A CYS 247 SG  ? ? ? 1_555 A CYS 308 SG ? ? A CYS 378 A CYS 445 1_555 ? ? ? ? ? ? ? 2.051 ? ?               
disulf7 disulf ?   ? A CYS 254 SG  ? ? ? 1_555 A CYS 281 SG ? ? A CYS 385 A CYS 418 1_555 ? ? ? ? ? ? ? 2.043 ? ?               
disulf8 disulf ?   ? A CYS 264 SG  ? ? ? 1_555 A CYS 273 SG ? ? A CYS 395 A CYS 410 1_555 ? ? ? ? ? ? ? 1.986 ? ?               
covale1 covale one ? A ASN 120 ND2 ? ? ? 1_555 B NAG .   C1 ? ? A ASN 234 A NAG 501 1_555 ? ? ? ? ? ? ? 1.427 ? N-Glycosylation 
covale2 covale one ? A ASN 127 ND2 ? ? ? 1_555 C NAG .   C1 ? ? A ASN 241 A NAG 502 1_555 ? ? ? ? ? ? ? 1.435 ? N-Glycosylation 
covale3 covale one ? A ASN 148 ND2 ? ? ? 1_555 D NAG .   C1 ? ? A ASN 262 A NAG 503 1_555 ? ? ? ? ? ? ? 1.431 ? N-Glycosylation 
covale4 covale one ? A ASN 162 ND2 ? ? ? 1_555 E NAG .   C1 ? ? A ASN 276 A NAG 504 1_555 ? ? ? ? ? ? ? 1.449 ? N-Glycosylation 
covale5 covale one ? A ASN 175 ND2 ? ? ? 1_555 F NAG .   C1 ? ? A ASN 289 A NAG 505 1_555 ? ? ? ? ? ? ? 1.445 ? N-Glycosylation 
covale6 covale one ? A ASN 181 ND2 ? ? ? 1_555 G NAG .   C1 ? ? A ASN 295 A NAG 506 1_555 ? ? ? ? ? ? ? 1.437 ? N-Glycosylation 
covale7 covale one ? A ASN 204 ND2 ? ? ? 1_555 H NAG .   C1 ? ? A ASN 334 A NAG 507 1_555 ? ? ? ? ? ? ? 1.421 ? N-Glycosylation 
covale8 covale one ? A ASN 255 ND2 ? ? ? 1_555 I NAG .   C1 ? ? A ASN 386 A NAG 508 1_555 ? ? ? ? ? ? ? 1.435 ? N-Glycosylation 
covale9 covale one ? A ASN 311 ND2 ? ? ? 1_555 J NAG .   C1 ? ? A ASN 448 A NAG 509 1_555 ? ? ? ? ? ? ? 1.436 ? N-Glycosylation 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  NAG B .   ? ASN A 120 ? NAG A 501 ? 1_555 ASN A 234 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2  NAG C .   ? ASN A 127 ? NAG A 502 ? 1_555 ASN A 241 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3  NAG D .   ? ASN A 148 ? NAG A 503 ? 1_555 ASN A 262 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4  NAG E .   ? ASN A 162 ? NAG A 504 ? 1_555 ASN A 276 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5  NAG F .   ? ASN A 175 ? NAG A 505 ? 1_555 ASN A 289 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
6  NAG G .   ? ASN A 181 ? NAG A 506 ? 1_555 ASN A 295 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
7  NAG H .   ? ASN A 204 ? NAG A 507 ? 1_555 ASN A 334 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
8  NAG I .   ? ASN A 255 ? NAG A 508 ? 1_555 ASN A 386 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
9  NAG J .   ? ASN A 311 ? NAG A 509 ? 1_555 ASN A 448 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
10 CYS A 13  ? CYS A 33  ? CYS A 54  ? 1_555 CYS A 74  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
11 CYS A 78  ? CYS A 91  ? CYS A 119 ? 1_555 CYS A 205 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
12 CYS A 104 ? CYS A 133 ? CYS A 218 ? 1_555 CYS A 247 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
13 CYS A 114 ? CYS A 125 ? CYS A 228 ? 1_555 CYS A 239 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
14 CYS A 182 ? CYS A 201 ? CYS A 296 ? 1_555 CYS A 331 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
15 CYS A 247 ? CYS A 308 ? CYS A 378 ? 1_555 CYS A 445 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
16 CYS A 254 ? CYS A 281 ? CYS A 385 ? 1_555 CYS A 418 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
17 CYS A 264 ? CYS A 273 ? CYS A 395 ? 1_555 CYS A 410 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 4 ? 
AA5 ? 5 ? 
AA6 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 4 5 ? parallel      
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA6 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TRP A 4   ? ASP A 6   ? TRP A 45  ASP A 47  
AA1 2 TYR A 349 ? ILE A 354 ? TYR A 486 ILE A 491 
AA1 3 TYR A 109 ? CYS A 114 ? TYR A 223 CYS A 228 
AA1 4 VAL A 128 ? VAL A 131 ? VAL A 242 VAL A 245 
AA1 5 ILE A 43  ? HIS A 44  ? ILE A 84  HIS A 85  
AA2 1 VAL A 34  ? PRO A 35  ? VAL A 75  PRO A 76  
AA2 2 PHE A 12  ? SER A 15  ? PHE A 53  SER A 56  
AA2 3 HIS A 102 ? CYS A 104 ? HIS A 216 CYS A 218 
AA3 1 GLU A 50  ? ASN A 53  ? GLU A 91  ASN A 94  
AA3 2 THR A 122 ? CYS A 125 ? THR A 236 CYS A 239 
AA4 1 SER A 85  ? LYS A 88  ? SER A 199 LYS A 202 
AA4 2 VAL A 79  ? THR A 82  ? VAL A 120 THR A 123 
AA4 3 GLN A 295 ? MET A 297 ? GLN A 432 MET A 434 
AA4 4 ILE A 286 ? ASN A 288 ? ILE A 423 ASN A 425 
AA5 1 LEU A 145 ? LEU A 147 ? LEU A 259 LEU A 261 
AA5 2 ILE A 306 ? ARG A 319 ? ILE A 443 ARG A 456 
AA5 3 ILE A 170 ? ARG A 184 ? ILE A 284 ARG A 298 
AA5 4 ASN A 328 ? PRO A 333 ? ASN A 465 PRO A 470 
AA5 5 THR A 227 ? PHE A 230 ? THR A 358 PHE A 361 
AA6 1 ILE A 157 ? ARG A 159 ? ILE A 271 ARG A 273 
AA6 2 ILE A 170 ? ARG A 184 ? ILE A 284 ARG A 298 
AA6 3 ILE A 306 ? ARG A 319 ? ILE A 443 ARG A 456 
AA6 4 LYS A 198 ? ASN A 204 ? LYS A 328 ASN A 334 
AA6 5 THR A 276 ? LYS A 284 ? THR A 413 LYS A 421 
AA6 6 GLU A 250 ? CYS A 254 ? GLU A 381 CYS A 385 
AA6 7 HIS A 243 ? CYS A 247 ? HIS A 374 CYS A 378 
# 
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 LYS A 5   ? N LYS A 46  O GLN A 353 ? O GLN A 490 
AA1 2 3 O LYS A 350 ? O LYS A 487 N LEU A 112 ? N LEU A 226 
AA1 3 4 N LYS A 113 ? N LYS A 227 O SER A 129 ? O SER A 243 
AA1 4 5 O SER A 130 ? O SER A 244 N ILE A 43  ? N ILE A 84  
AA2 1 2 O VAL A 34  ? O VAL A 75  N CYS A 13  ? N CYS A 54  
AA2 2 3 N ALA A 14  ? N ALA A 55  O HIS A 102 ? O HIS A 216 
AA3 1 2 N GLU A 50  ? N GLU A 91  O CYS A 125 ? O CYS A 239 
AA4 1 2 O SER A 85  ? O SER A 199 N THR A 82  ? N THR A 123 
AA4 2 3 N LEU A 81  ? N LEU A 122 O GLN A 295 ? O GLN A 432 
AA4 3 4 O ALA A 296 ? O ALA A 433 N ILE A 287 ? N ILE A 424 
AA5 1 2 N LEU A 146 ? N LEU A 260 O THR A 313 ? O THR A 450 
AA5 2 3 O LEU A 317 ? O LEU A 454 N ILE A 170 ? N ILE A 284 
AA5 4 5 O GLU A 329 ? O GLU A 466 N THR A 227 ? N THR A 358 
AA6 1 2 N ARG A 159 ? N ARG A 273 O ILE A 171 ? O ILE A 285 
AA6 2 3 N ILE A 170 ? N ILE A 284 O LEU A 317 ? O LEU A 454 
AA6 4 5 N CYS A 201 ? N CYS A 331 O LEU A 279 ? O LEU A 416 
AA6 5 6 O LYS A 282 ? O LYS A 419 N TYR A 253 ? N TYR A 384 
AA6 6 7 O CYS A 254 ? O CYS A 385 N HIS A 243 ? N HIS A 374 
# 
_pdbx_entry_details.entry_id                   9BXY 
_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   Y 
# 
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 ASN A 88  ? ? 35.72   46.58   
2  1 SER A 115 ? ? -122.99 -57.35  
3  1 GLN A 203 ? ? -118.56 -160.36 
4  1 ASP A 211 ? ? -166.69 97.42   
5  1 GLN A 258 ? ? 68.14   -49.71  
6  1 GLU A 268 ? ? -122.58 -98.86  
7  1 ASN A 276 ? ? -170.33 98.29   
8  1 SER A 365 ? ? -95.31  55.09   
9  1 PHE A 391 ? ? -110.13 50.40   
10 1 ASN A 411 ? ? -159.15 37.63   
11 1 GLN A 428 ? ? -73.08  -78.54  
12 1 ALA A 460 ? ? -165.76 42.48   
# 
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 VAL 42  ? A VAL 1   
2  1 Y 1 A GLY 318 ? A GLY 188 
3  1 Y 1 A GLY 319 ? A GLY 189 
4  1 Y 1 A SER 320 ? A SER 190 
5  1 Y 1 A GLY 321 ? A GLY 191 
6  1 Y 1 A SER 322 ? A SER 192 
7  1 Y 1 A GLY 323 ? A GLY 193 
8  1 Y 1 A GLY 324 ? A GLY 194 
9  1 Y 1 A ILE 402 ? A ILE 265 
10 1 Y 1 A GLY 403 ? A GLY 266 
11 1 Y 1 A ASN 404 ? A ASN 267 
12 1 Y 1 A GLU 405 ? A GLU 268 
13 1 Y 1 A THR 406 ? A THR 269 
14 1 Y 1 A MET 407 ? A MET 270 
# 
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 
A1ATE C10  C  N N 1   
A1ATE CG   C  N S 2   
A1ATE ND1  N  N N 3   
A1ATE CD2  C  N N 4   
A1ATE CE1  C  N N 5   
A1ATE CE2  C  N N 6   
A1ATE CZ   C  N N 7   
A1ATE NH1  N  N N 8   
A1ATE NH2  N  N N 9   
A1ATE C01  C  N N 10  
A1ATE C03  C  N N 11  
A1ATE C04  C  N N 12  
A1ATE C06  C  N N 13  
A1ATE C08  C  N N 14  
A1ATE C09  C  N S 15  
A1ATE C13  C  Y N 16  
A1ATE C14  C  Y N 17  
A1ATE C15  C  Y N 18  
A1ATE C17  C  Y N 19  
A1ATE C19  C  Y N 20  
A1ATE C20  C  Y N 21  
A1ATE C21  C  N N 22  
A1ATE C22  C  N R 23  
A1ATE C23  C  N N 24  
A1ATE C25  C  N N 25  
A1ATE C26  C  N N 26  
A1ATE C27  C  N N 27  
A1ATE F16  F  N N 28  
A1ATE N02  N  N N 29  
A1ATE N05  N  N N 30  
A1ATE N07  N  N N 31  
A1ATE N12  N  N N 32  
A1ATE O11  O  N N 33  
A1ATE O24  O  N N 34  
A1ATE O27  O  N N 35  
A1ATE O28  O  N N 36  
A1ATE CL1  CL N N 37  
A1ATE H1   H  N N 38  
A1ATE H2   H  N N 39  
A1ATE H3   H  N N 40  
A1ATE H4   H  N N 41  
A1ATE H5   H  N N 42  
A1ATE H6   H  N N 43  
A1ATE H7   H  N N 44  
A1ATE H8   H  N N 45  
A1ATE H9   H  N N 46  
A1ATE H10  H  N N 47  
A1ATE H11  H  N N 48  
A1ATE H12  H  N N 49  
A1ATE H13  H  N N 50  
A1ATE H14  H  N N 51  
A1ATE H15  H  N N 52  
A1ATE H16  H  N N 53  
A1ATE H17  H  N N 54  
A1ATE H18  H  N N 55  
A1ATE H19  H  N N 56  
A1ATE H20  H  N N 57  
A1ATE H21  H  N N 58  
A1ATE H22  H  N N 59  
A1ATE H23  H  N N 60  
A1ATE H24  H  N N 61  
A1ATE H25  H  N N 62  
A1ATE H26  H  N N 63  
A1ATE H27  H  N N 64  
A1ATE H28  H  N N 65  
A1ATE H29  H  N N 66  
A1ATE H30  H  N N 67  
A1ATE H31  H  N N 68  
A1ATE H32  H  N N 69  
A1ATE H33  H  N N 70  
ALA   N    N  N N 71  
ALA   CA   C  N S 72  
ALA   C    C  N N 73  
ALA   O    O  N N 74  
ALA   CB   C  N N 75  
ALA   OXT  O  N N 76  
ALA   H    H  N N 77  
ALA   H2   H  N N 78  
ALA   HA   H  N N 79  
ALA   HB1  H  N N 80  
ALA   HB2  H  N N 81  
ALA   HB3  H  N N 82  
ALA   HXT  H  N N 83  
ARG   N    N  N N 84  
ARG   CA   C  N S 85  
ARG   C    C  N N 86  
ARG   O    O  N N 87  
ARG   CB   C  N N 88  
ARG   CG   C  N N 89  
ARG   CD   C  N N 90  
ARG   NE   N  N N 91  
ARG   CZ   C  N N 92  
ARG   NH1  N  N N 93  
ARG   NH2  N  N N 94  
ARG   OXT  O  N N 95  
ARG   H    H  N N 96  
ARG   H2   H  N N 97  
ARG   HA   H  N N 98  
ARG   HB2  H  N N 99  
ARG   HB3  H  N N 100 
ARG   HG2  H  N N 101 
ARG   HG3  H  N N 102 
ARG   HD2  H  N N 103 
ARG   HD3  H  N N 104 
ARG   HE   H  N N 105 
ARG   HH11 H  N N 106 
ARG   HH12 H  N N 107 
ARG   HH21 H  N N 108 
ARG   HH22 H  N N 109 
ARG   HXT  H  N N 110 
ASN   N    N  N N 111 
ASN   CA   C  N S 112 
ASN   C    C  N N 113 
ASN   O    O  N N 114 
ASN   CB   C  N N 115 
ASN   CG   C  N N 116 
ASN   OD1  O  N N 117 
ASN   ND2  N  N N 118 
ASN   OXT  O  N N 119 
ASN   H    H  N N 120 
ASN   H2   H  N N 121 
ASN   HA   H  N N 122 
ASN   HB2  H  N N 123 
ASN   HB3  H  N N 124 
ASN   HD21 H  N N 125 
ASN   HD22 H  N N 126 
ASN   HXT  H  N N 127 
ASP   N    N  N N 128 
ASP   CA   C  N S 129 
ASP   C    C  N N 130 
ASP   O    O  N N 131 
ASP   CB   C  N N 132 
ASP   CG   C  N N 133 
ASP   OD1  O  N N 134 
ASP   OD2  O  N N 135 
ASP   OXT  O  N N 136 
ASP   H    H  N N 137 
ASP   H2   H  N N 138 
ASP   HA   H  N N 139 
ASP   HB2  H  N N 140 
ASP   HB3  H  N N 141 
ASP   HD2  H  N N 142 
ASP   HXT  H  N N 143 
CYS   N    N  N N 144 
CYS   CA   C  N R 145 
CYS   C    C  N N 146 
CYS   O    O  N N 147 
CYS   CB   C  N N 148 
CYS   SG   S  N N 149 
CYS   OXT  O  N N 150 
CYS   H    H  N N 151 
CYS   H2   H  N N 152 
CYS   HA   H  N N 153 
CYS   HB2  H  N N 154 
CYS   HB3  H  N N 155 
CYS   HG   H  N N 156 
CYS   HXT  H  N N 157 
EPE   N1   N  N N 158 
EPE   C2   C  N N 159 
EPE   C3   C  N N 160 
EPE   N4   N  N N 161 
EPE   C5   C  N N 162 
EPE   C6   C  N N 163 
EPE   C7   C  N N 164 
EPE   C8   C  N N 165 
EPE   O8   O  N N 166 
EPE   C9   C  N N 167 
EPE   C10  C  N N 168 
EPE   S    S  N N 169 
EPE   O1S  O  N N 170 
EPE   O2S  O  N N 171 
EPE   O3S  O  N N 172 
EPE   H21  H  N N 173 
EPE   H22  H  N N 174 
EPE   H31  H  N N 175 
EPE   H32  H  N N 176 
EPE   H51  H  N N 177 
EPE   H52  H  N N 178 
EPE   H61  H  N N 179 
EPE   H62  H  N N 180 
EPE   H71  H  N N 181 
EPE   H72  H  N N 182 
EPE   H81  H  N N 183 
EPE   H82  H  N N 184 
EPE   HO8  H  N N 185 
EPE   H91  H  N N 186 
EPE   H92  H  N N 187 
EPE   H101 H  N N 188 
EPE   H102 H  N N 189 
EPE   HOS3 H  N N 190 
GLN   N    N  N N 191 
GLN   CA   C  N S 192 
GLN   C    C  N N 193 
GLN   O    O  N N 194 
GLN   CB   C  N N 195 
GLN   CG   C  N N 196 
GLN   CD   C  N N 197 
GLN   OE1  O  N N 198 
GLN   NE2  N  N N 199 
GLN   OXT  O  N N 200 
GLN   H    H  N N 201 
GLN   H2   H  N N 202 
GLN   HA   H  N N 203 
GLN   HB2  H  N N 204 
GLN   HB3  H  N N 205 
GLN   HG2  H  N N 206 
GLN   HG3  H  N N 207 
GLN   HE21 H  N N 208 
GLN   HE22 H  N N 209 
GLN   HXT  H  N N 210 
GLU   N    N  N N 211 
GLU   CA   C  N S 212 
GLU   C    C  N N 213 
GLU   O    O  N N 214 
GLU   CB   C  N N 215 
GLU   CG   C  N N 216 
GLU   CD   C  N N 217 
GLU   OE1  O  N N 218 
GLU   OE2  O  N N 219 
GLU   OXT  O  N N 220 
GLU   H    H  N N 221 
GLU   H2   H  N N 222 
GLU   HA   H  N N 223 
GLU   HB2  H  N N 224 
GLU   HB3  H  N N 225 
GLU   HG2  H  N N 226 
GLU   HG3  H  N N 227 
GLU   HE2  H  N N 228 
GLU   HXT  H  N N 229 
GLY   N    N  N N 230 
GLY   CA   C  N N 231 
GLY   C    C  N N 232 
GLY   O    O  N N 233 
GLY   OXT  O  N N 234 
GLY   H    H  N N 235 
GLY   H2   H  N N 236 
GLY   HA2  H  N N 237 
GLY   HA3  H  N N 238 
GLY   HXT  H  N N 239 
HIS   N    N  N N 240 
HIS   CA   C  N S 241 
HIS   C    C  N N 242 
HIS   O    O  N N 243 
HIS   CB   C  N N 244 
HIS   CG   C  Y N 245 
HIS   ND1  N  Y N 246 
HIS   CD2  C  Y N 247 
HIS   CE1  C  Y N 248 
HIS   NE2  N  Y N 249 
HIS   OXT  O  N N 250 
HIS   H    H  N N 251 
HIS   H2   H  N N 252 
HIS   HA   H  N N 253 
HIS   HB2  H  N N 254 
HIS   HB3  H  N N 255 
HIS   HD1  H  N N 256 
HIS   HD2  H  N N 257 
HIS   HE1  H  N N 258 
HIS   HE2  H  N N 259 
HIS   HXT  H  N N 260 
HOH   O    O  N N 261 
HOH   H1   H  N N 262 
HOH   H2   H  N N 263 
ILE   N    N  N N 264 
ILE   CA   C  N S 265 
ILE   C    C  N N 266 
ILE   O    O  N N 267 
ILE   CB   C  N S 268 
ILE   CG1  C  N N 269 
ILE   CG2  C  N N 270 
ILE   CD1  C  N N 271 
ILE   OXT  O  N N 272 
ILE   H    H  N N 273 
ILE   H2   H  N N 274 
ILE   HA   H  N N 275 
ILE   HB   H  N N 276 
ILE   HG12 H  N N 277 
ILE   HG13 H  N N 278 
ILE   HG21 H  N N 279 
ILE   HG22 H  N N 280 
ILE   HG23 H  N N 281 
ILE   HD11 H  N N 282 
ILE   HD12 H  N N 283 
ILE   HD13 H  N N 284 
ILE   HXT  H  N N 285 
LEU   N    N  N N 286 
LEU   CA   C  N S 287 
LEU   C    C  N N 288 
LEU   O    O  N N 289 
LEU   CB   C  N N 290 
LEU   CG   C  N N 291 
LEU   CD1  C  N N 292 
LEU   CD2  C  N N 293 
LEU   OXT  O  N N 294 
LEU   H    H  N N 295 
LEU   H2   H  N N 296 
LEU   HA   H  N N 297 
LEU   HB2  H  N N 298 
LEU   HB3  H  N N 299 
LEU   HG   H  N N 300 
LEU   HD11 H  N N 301 
LEU   HD12 H  N N 302 
LEU   HD13 H  N N 303 
LEU   HD21 H  N N 304 
LEU   HD22 H  N N 305 
LEU   HD23 H  N N 306 
LEU   HXT  H  N N 307 
LYS   N    N  N N 308 
LYS   CA   C  N S 309 
LYS   C    C  N N 310 
LYS   O    O  N N 311 
LYS   CB   C  N N 312 
LYS   CG   C  N N 313 
LYS   CD   C  N N 314 
LYS   CE   C  N N 315 
LYS   NZ   N  N N 316 
LYS   OXT  O  N N 317 
LYS   H    H  N N 318 
LYS   H2   H  N N 319 
LYS   HA   H  N N 320 
LYS   HB2  H  N N 321 
LYS   HB3  H  N N 322 
LYS   HG2  H  N N 323 
LYS   HG3  H  N N 324 
LYS   HD2  H  N N 325 
LYS   HD3  H  N N 326 
LYS   HE2  H  N N 327 
LYS   HE3  H  N N 328 
LYS   HZ1  H  N N 329 
LYS   HZ2  H  N N 330 
LYS   HZ3  H  N N 331 
LYS   HXT  H  N N 332 
MET   N    N  N N 333 
MET   CA   C  N S 334 
MET   C    C  N N 335 
MET   O    O  N N 336 
MET   CB   C  N N 337 
MET   CG   C  N N 338 
MET   SD   S  N N 339 
MET   CE   C  N N 340 
MET   OXT  O  N N 341 
MET   H    H  N N 342 
MET   H2   H  N N 343 
MET   HA   H  N N 344 
MET   HB2  H  N N 345 
MET   HB3  H  N N 346 
MET   HG2  H  N N 347 
MET   HG3  H  N N 348 
MET   HE1  H  N N 349 
MET   HE2  H  N N 350 
MET   HE3  H  N N 351 
MET   HXT  H  N N 352 
NAG   C1   C  N R 353 
NAG   C2   C  N R 354 
NAG   C3   C  N R 355 
NAG   C4   C  N S 356 
NAG   C5   C  N R 357 
NAG   C6   C  N N 358 
NAG   C7   C  N N 359 
NAG   C8   C  N N 360 
NAG   N2   N  N N 361 
NAG   O1   O  N N 362 
NAG   O3   O  N N 363 
NAG   O4   O  N N 364 
NAG   O5   O  N N 365 
NAG   O6   O  N N 366 
NAG   O7   O  N N 367 
NAG   H1   H  N N 368 
NAG   H2   H  N N 369 
NAG   H3   H  N N 370 
NAG   H4   H  N N 371 
NAG   H5   H  N N 372 
NAG   H61  H  N N 373 
NAG   H62  H  N N 374 
NAG   H81  H  N N 375 
NAG   H82  H  N N 376 
NAG   H83  H  N N 377 
NAG   HN2  H  N N 378 
NAG   HO1  H  N N 379 
NAG   HO3  H  N N 380 
NAG   HO4  H  N N 381 
NAG   HO6  H  N N 382 
PHE   N    N  N N 383 
PHE   CA   C  N S 384 
PHE   C    C  N N 385 
PHE   O    O  N N 386 
PHE   CB   C  N N 387 
PHE   CG   C  Y N 388 
PHE   CD1  C  Y N 389 
PHE   CD2  C  Y N 390 
PHE   CE1  C  Y N 391 
PHE   CE2  C  Y N 392 
PHE   CZ   C  Y N 393 
PHE   OXT  O  N N 394 
PHE   H    H  N N 395 
PHE   H2   H  N N 396 
PHE   HA   H  N N 397 
PHE   HB2  H  N N 398 
PHE   HB3  H  N N 399 
PHE   HD1  H  N N 400 
PHE   HD2  H  N N 401 
PHE   HE1  H  N N 402 
PHE   HE2  H  N N 403 
PHE   HZ   H  N N 404 
PHE   HXT  H  N N 405 
PRO   N    N  N N 406 
PRO   CA   C  N S 407 
PRO   C    C  N N 408 
PRO   O    O  N N 409 
PRO   CB   C  N N 410 
PRO   CG   C  N N 411 
PRO   CD   C  N N 412 
PRO   OXT  O  N N 413 
PRO   H    H  N N 414 
PRO   HA   H  N N 415 
PRO   HB2  H  N N 416 
PRO   HB3  H  N N 417 
PRO   HG2  H  N N 418 
PRO   HG3  H  N N 419 
PRO   HD2  H  N N 420 
PRO   HD3  H  N N 421 
PRO   HXT  H  N N 422 
SER   N    N  N N 423 
SER   CA   C  N S 424 
SER   C    C  N N 425 
SER   O    O  N N 426 
SER   CB   C  N N 427 
SER   OG   O  N N 428 
SER   OXT  O  N N 429 
SER   H    H  N N 430 
SER   H2   H  N N 431 
SER   HA   H  N N 432 
SER   HB2  H  N N 433 
SER   HB3  H  N N 434 
SER   HG   H  N N 435 
SER   HXT  H  N N 436 
THR   N    N  N N 437 
THR   CA   C  N S 438 
THR   C    C  N N 439 
THR   O    O  N N 440 
THR   CB   C  N R 441 
THR   OG1  O  N N 442 
THR   CG2  C  N N 443 
THR   OXT  O  N N 444 
THR   H    H  N N 445 
THR   H2   H  N N 446 
THR   HA   H  N N 447 
THR   HB   H  N N 448 
THR   HG1  H  N N 449 
THR   HG21 H  N N 450 
THR   HG22 H  N N 451 
THR   HG23 H  N N 452 
THR   HXT  H  N N 453 
TRP   N    N  N N 454 
TRP   CA   C  N S 455 
TRP   C    C  N N 456 
TRP   O    O  N N 457 
TRP   CB   C  N N 458 
TRP   CG   C  Y N 459 
TRP   CD1  C  Y N 460 
TRP   CD2  C  Y N 461 
TRP   NE1  N  Y N 462 
TRP   CE2  C  Y N 463 
TRP   CE3  C  Y N 464 
TRP   CZ2  C  Y N 465 
TRP   CZ3  C  Y N 466 
TRP   CH2  C  Y N 467 
TRP   OXT  O  N N 468 
TRP   H    H  N N 469 
TRP   H2   H  N N 470 
TRP   HA   H  N N 471 
TRP   HB2  H  N N 472 
TRP   HB3  H  N N 473 
TRP   HD1  H  N N 474 
TRP   HE1  H  N N 475 
TRP   HE3  H  N N 476 
TRP   HZ2  H  N N 477 
TRP   HZ3  H  N N 478 
TRP   HH2  H  N N 479 
TRP   HXT  H  N N 480 
TYR   N    N  N N 481 
TYR   CA   C  N S 482 
TYR   C    C  N N 483 
TYR   O    O  N N 484 
TYR   CB   C  N N 485 
TYR   CG   C  Y N 486 
TYR   CD1  C  Y N 487 
TYR   CD2  C  Y N 488 
TYR   CE1  C  Y N 489 
TYR   CE2  C  Y N 490 
TYR   CZ   C  Y N 491 
TYR   OH   O  N N 492 
TYR   OXT  O  N N 493 
TYR   H    H  N N 494 
TYR   H2   H  N N 495 
TYR   HA   H  N N 496 
TYR   HB2  H  N N 497 
TYR   HB3  H  N N 498 
TYR   HD1  H  N N 499 
TYR   HD2  H  N N 500 
TYR   HE1  H  N N 501 
TYR   HE2  H  N N 502 
TYR   HH   H  N N 503 
TYR   HXT  H  N N 504 
VAL   N    N  N N 505 
VAL   CA   C  N S 506 
VAL   C    C  N N 507 
VAL   O    O  N N 508 
VAL   CB   C  N N 509 
VAL   CG1  C  N N 510 
VAL   CG2  C  N N 511 
VAL   OXT  O  N N 512 
VAL   H    H  N N 513 
VAL   H2   H  N N 514 
VAL   HA   H  N N 515 
VAL   HB   H  N N 516 
VAL   HG11 H  N N 517 
VAL   HG12 H  N N 518 
VAL   HG13 H  N N 519 
VAL   HG21 H  N N 520 
VAL   HG22 H  N N 521 
VAL   HG23 H  N N 522 
VAL   HXT  H  N N 523 
# 
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 
A1ATE CL1 C17  sing N N 1   
A1ATE C19 C17  doub Y N 2   
A1ATE C19 C20  sing Y N 3   
A1ATE C17 C15  sing Y N 4   
A1ATE C20 C13  doub Y N 5   
A1ATE C15 F16  sing N N 6   
A1ATE C15 C14  doub Y N 7   
A1ATE C13 C14  sing Y N 8   
A1ATE C13 N12  sing N N 9   
A1ATE N12 C10  sing N N 10  
A1ATE C10 O11  doub N N 11  
A1ATE C10 C09  sing N N 12  
A1ATE C21 C09  sing N N 13  
A1ATE C21 C22  sing N N 14  
A1ATE C09 C08  sing N N 15  
A1ATE C22 C27  sing N N 16  
A1ATE C22 C23  sing N N 17  
A1ATE C27 O28  sing N N 18  
A1ATE C08 N07  sing N N 19  
A1ATE N07 C23  sing N N 20  
A1ATE N07 C06  sing N N 21  
A1ATE C25 N05  sing N N 22  
A1ATE C25 C26  sing N N 23  
A1ATE C06 N05  sing N N 24  
A1ATE C06 O24  doub N N 25  
A1ATE N05 C04  sing N N 26  
A1ATE C04 C03  sing N N 27  
A1ATE C26 N02  sing N N 28  
A1ATE C03 N02  sing N N 29  
A1ATE N02 C01  sing N N 30  
A1ATE NH1 CZ   doub N N 31  
A1ATE C01 O27  doub N N 32  
A1ATE C01 CG   sing N N 33  
A1ATE CZ  NH2  sing N N 34  
A1ATE CZ  ND1  sing N N 35  
A1ATE CG  ND1  sing N N 36  
A1ATE CG  CD2  sing N N 37  
A1ATE ND1 CE2  sing N N 38  
A1ATE CD2 CE1  sing N N 39  
A1ATE CE2 CE1  sing N N 40  
A1ATE CG  H1   sing N N 41  
A1ATE CD2 H2   sing N N 42  
A1ATE CD2 H3   sing N N 43  
A1ATE CE1 H4   sing N N 44  
A1ATE CE1 H5   sing N N 45  
A1ATE CE2 H6   sing N N 46  
A1ATE CE2 H7   sing N N 47  
A1ATE NH1 H8   sing N N 48  
A1ATE NH2 H9   sing N N 49  
A1ATE NH2 H10  sing N N 50  
A1ATE C03 H11  sing N N 51  
A1ATE C03 H12  sing N N 52  
A1ATE C04 H13  sing N N 53  
A1ATE C04 H14  sing N N 54  
A1ATE C08 H15  sing N N 55  
A1ATE C08 H16  sing N N 56  
A1ATE C09 H17  sing N N 57  
A1ATE C14 H18  sing N N 58  
A1ATE C19 H19  sing N N 59  
A1ATE C20 H20  sing N N 60  
A1ATE C21 H21  sing N N 61  
A1ATE C21 H22  sing N N 62  
A1ATE C22 H23  sing N N 63  
A1ATE C23 H24  sing N N 64  
A1ATE C23 H25  sing N N 65  
A1ATE C25 H26  sing N N 66  
A1ATE C25 H27  sing N N 67  
A1ATE C26 H28  sing N N 68  
A1ATE C26 H29  sing N N 69  
A1ATE C27 H30  sing N N 70  
A1ATE C27 H31  sing N N 71  
A1ATE N12 H32  sing N N 72  
A1ATE O28 H33  sing N N 73  
ALA   N   CA   sing N N 74  
ALA   N   H    sing N N 75  
ALA   N   H2   sing N N 76  
ALA   CA  C    sing N N 77  
ALA   CA  CB   sing N N 78  
ALA   CA  HA   sing N N 79  
ALA   C   O    doub N N 80  
ALA   C   OXT  sing N N 81  
ALA   CB  HB1  sing N N 82  
ALA   CB  HB2  sing N N 83  
ALA   CB  HB3  sing N N 84  
ALA   OXT HXT  sing N N 85  
ARG   N   CA   sing N N 86  
ARG   N   H    sing N N 87  
ARG   N   H2   sing N N 88  
ARG   CA  C    sing N N 89  
ARG   CA  CB   sing N N 90  
ARG   CA  HA   sing N N 91  
ARG   C   O    doub N N 92  
ARG   C   OXT  sing N N 93  
ARG   CB  CG   sing N N 94  
ARG   CB  HB2  sing N N 95  
ARG   CB  HB3  sing N N 96  
ARG   CG  CD   sing N N 97  
ARG   CG  HG2  sing N N 98  
ARG   CG  HG3  sing N N 99  
ARG   CD  NE   sing N N 100 
ARG   CD  HD2  sing N N 101 
ARG   CD  HD3  sing N N 102 
ARG   NE  CZ   sing N N 103 
ARG   NE  HE   sing N N 104 
ARG   CZ  NH1  sing N N 105 
ARG   CZ  NH2  doub N N 106 
ARG   NH1 HH11 sing N N 107 
ARG   NH1 HH12 sing N N 108 
ARG   NH2 HH21 sing N N 109 
ARG   NH2 HH22 sing N N 110 
ARG   OXT HXT  sing N N 111 
ASN   N   CA   sing N N 112 
ASN   N   H    sing N N 113 
ASN   N   H2   sing N N 114 
ASN   CA  C    sing N N 115 
ASN   CA  CB   sing N N 116 
ASN   CA  HA   sing N N 117 
ASN   C   O    doub N N 118 
ASN   C   OXT  sing N N 119 
ASN   CB  CG   sing N N 120 
ASN   CB  HB2  sing N N 121 
ASN   CB  HB3  sing N N 122 
ASN   CG  OD1  doub N N 123 
ASN   CG  ND2  sing N N 124 
ASN   ND2 HD21 sing N N 125 
ASN   ND2 HD22 sing N N 126 
ASN   OXT HXT  sing N N 127 
ASP   N   CA   sing N N 128 
ASP   N   H    sing N N 129 
ASP   N   H2   sing N N 130 
ASP   CA  C    sing N N 131 
ASP   CA  CB   sing N N 132 
ASP   CA  HA   sing N N 133 
ASP   C   O    doub N N 134 
ASP   C   OXT  sing N N 135 
ASP   CB  CG   sing N N 136 
ASP   CB  HB2  sing N N 137 
ASP   CB  HB3  sing N N 138 
ASP   CG  OD1  doub N N 139 
ASP   CG  OD2  sing N N 140 
ASP   OD2 HD2  sing N N 141 
ASP   OXT HXT  sing N N 142 
CYS   N   CA   sing N N 143 
CYS   N   H    sing N N 144 
CYS   N   H2   sing N N 145 
CYS   CA  C    sing N N 146 
CYS   CA  CB   sing N N 147 
CYS   CA  HA   sing N N 148 
CYS   C   O    doub N N 149 
CYS   C   OXT  sing N N 150 
CYS   CB  SG   sing N N 151 
CYS   CB  HB2  sing N N 152 
CYS   CB  HB3  sing N N 153 
CYS   SG  HG   sing N N 154 
CYS   OXT HXT  sing N N 155 
EPE   N1  C2   sing N N 156 
EPE   N1  C6   sing N N 157 
EPE   N1  C9   sing N N 158 
EPE   C2  C3   sing N N 159 
EPE   C2  H21  sing N N 160 
EPE   C2  H22  sing N N 161 
EPE   C3  N4   sing N N 162 
EPE   C3  H31  sing N N 163 
EPE   C3  H32  sing N N 164 
EPE   N4  C5   sing N N 165 
EPE   N4  C7   sing N N 166 
EPE   C5  C6   sing N N 167 
EPE   C5  H51  sing N N 168 
EPE   C5  H52  sing N N 169 
EPE   C6  H61  sing N N 170 
EPE   C6  H62  sing N N 171 
EPE   C7  C8   sing N N 172 
EPE   C7  H71  sing N N 173 
EPE   C7  H72  sing N N 174 
EPE   C8  O8   sing N N 175 
EPE   C8  H81  sing N N 176 
EPE   C8  H82  sing N N 177 
EPE   O8  HO8  sing N N 178 
EPE   C9  C10  sing N N 179 
EPE   C9  H91  sing N N 180 
EPE   C9  H92  sing N N 181 
EPE   C10 S    sing N N 182 
EPE   C10 H101 sing N N 183 
EPE   C10 H102 sing N N 184 
EPE   S   O1S  doub N N 185 
EPE   S   O2S  doub N N 186 
EPE   S   O3S  sing N N 187 
EPE   O3S HOS3 sing N N 188 
GLN   N   CA   sing N N 189 
GLN   N   H    sing N N 190 
GLN   N   H2   sing N N 191 
GLN   CA  C    sing N N 192 
GLN   CA  CB   sing N N 193 
GLN   CA  HA   sing N N 194 
GLN   C   O    doub N N 195 
GLN   C   OXT  sing N N 196 
GLN   CB  CG   sing N N 197 
GLN   CB  HB2  sing N N 198 
GLN   CB  HB3  sing N N 199 
GLN   CG  CD   sing N N 200 
GLN   CG  HG2  sing N N 201 
GLN   CG  HG3  sing N N 202 
GLN   CD  OE1  doub N N 203 
GLN   CD  NE2  sing N N 204 
GLN   NE2 HE21 sing N N 205 
GLN   NE2 HE22 sing N N 206 
GLN   OXT HXT  sing N N 207 
GLU   N   CA   sing N N 208 
GLU   N   H    sing N N 209 
GLU   N   H2   sing N N 210 
GLU   CA  C    sing N N 211 
GLU   CA  CB   sing N N 212 
GLU   CA  HA   sing N N 213 
GLU   C   O    doub N N 214 
GLU   C   OXT  sing N N 215 
GLU   CB  CG   sing N N 216 
GLU   CB  HB2  sing N N 217 
GLU   CB  HB3  sing N N 218 
GLU   CG  CD   sing N N 219 
GLU   CG  HG2  sing N N 220 
GLU   CG  HG3  sing N N 221 
GLU   CD  OE1  doub N N 222 
GLU   CD  OE2  sing N N 223 
GLU   OE2 HE2  sing N N 224 
GLU   OXT HXT  sing N N 225 
GLY   N   CA   sing N N 226 
GLY   N   H    sing N N 227 
GLY   N   H2   sing N N 228 
GLY   CA  C    sing N N 229 
GLY   CA  HA2  sing N N 230 
GLY   CA  HA3  sing N N 231 
GLY   C   O    doub N N 232 
GLY   C   OXT  sing N N 233 
GLY   OXT HXT  sing N N 234 
HIS   N   CA   sing N N 235 
HIS   N   H    sing N N 236 
HIS   N   H2   sing N N 237 
HIS   CA  C    sing N N 238 
HIS   CA  CB   sing N N 239 
HIS   CA  HA   sing N N 240 
HIS   C   O    doub N N 241 
HIS   C   OXT  sing N N 242 
HIS   CB  CG   sing N N 243 
HIS   CB  HB2  sing N N 244 
HIS   CB  HB3  sing N N 245 
HIS   CG  ND1  sing Y N 246 
HIS   CG  CD2  doub Y N 247 
HIS   ND1 CE1  doub Y N 248 
HIS   ND1 HD1  sing N N 249 
HIS   CD2 NE2  sing Y N 250 
HIS   CD2 HD2  sing N N 251 
HIS   CE1 NE2  sing Y N 252 
HIS   CE1 HE1  sing N N 253 
HIS   NE2 HE2  sing N N 254 
HIS   OXT HXT  sing N N 255 
HOH   O   H1   sing N N 256 
HOH   O   H2   sing N N 257 
ILE   N   CA   sing N N 258 
ILE   N   H    sing N N 259 
ILE   N   H2   sing N N 260 
ILE   CA  C    sing N N 261 
ILE   CA  CB   sing N N 262 
ILE   CA  HA   sing N N 263 
ILE   C   O    doub N N 264 
ILE   C   OXT  sing N N 265 
ILE   CB  CG1  sing N N 266 
ILE   CB  CG2  sing N N 267 
ILE   CB  HB   sing N N 268 
ILE   CG1 CD1  sing N N 269 
ILE   CG1 HG12 sing N N 270 
ILE   CG1 HG13 sing N N 271 
ILE   CG2 HG21 sing N N 272 
ILE   CG2 HG22 sing N N 273 
ILE   CG2 HG23 sing N N 274 
ILE   CD1 HD11 sing N N 275 
ILE   CD1 HD12 sing N N 276 
ILE   CD1 HD13 sing N N 277 
ILE   OXT HXT  sing N N 278 
LEU   N   CA   sing N N 279 
LEU   N   H    sing N N 280 
LEU   N   H2   sing N N 281 
LEU   CA  C    sing N N 282 
LEU   CA  CB   sing N N 283 
LEU   CA  HA   sing N N 284 
LEU   C   O    doub N N 285 
LEU   C   OXT  sing N N 286 
LEU   CB  CG   sing N N 287 
LEU   CB  HB2  sing N N 288 
LEU   CB  HB3  sing N N 289 
LEU   CG  CD1  sing N N 290 
LEU   CG  CD2  sing N N 291 
LEU   CG  HG   sing N N 292 
LEU   CD1 HD11 sing N N 293 
LEU   CD1 HD12 sing N N 294 
LEU   CD1 HD13 sing N N 295 
LEU   CD2 HD21 sing N N 296 
LEU   CD2 HD22 sing N N 297 
LEU   CD2 HD23 sing N N 298 
LEU   OXT HXT  sing N N 299 
LYS   N   CA   sing N N 300 
LYS   N   H    sing N N 301 
LYS   N   H2   sing N N 302 
LYS   CA  C    sing N N 303 
LYS   CA  CB   sing N N 304 
LYS   CA  HA   sing N N 305 
LYS   C   O    doub N N 306 
LYS   C   OXT  sing N N 307 
LYS   CB  CG   sing N N 308 
LYS   CB  HB2  sing N N 309 
LYS   CB  HB3  sing N N 310 
LYS   CG  CD   sing N N 311 
LYS   CG  HG2  sing N N 312 
LYS   CG  HG3  sing N N 313 
LYS   CD  CE   sing N N 314 
LYS   CD  HD2  sing N N 315 
LYS   CD  HD3  sing N N 316 
LYS   CE  NZ   sing N N 317 
LYS   CE  HE2  sing N N 318 
LYS   CE  HE3  sing N N 319 
LYS   NZ  HZ1  sing N N 320 
LYS   NZ  HZ2  sing N N 321 
LYS   NZ  HZ3  sing N N 322 
LYS   OXT HXT  sing N N 323 
MET   N   CA   sing N N 324 
MET   N   H    sing N N 325 
MET   N   H2   sing N N 326 
MET   CA  C    sing N N 327 
MET   CA  CB   sing N N 328 
MET   CA  HA   sing N N 329 
MET   C   O    doub N N 330 
MET   C   OXT  sing N N 331 
MET   CB  CG   sing N N 332 
MET   CB  HB2  sing N N 333 
MET   CB  HB3  sing N N 334 
MET   CG  SD   sing N N 335 
MET   CG  HG2  sing N N 336 
MET   CG  HG3  sing N N 337 
MET   SD  CE   sing N N 338 
MET   CE  HE1  sing N N 339 
MET   CE  HE2  sing N N 340 
MET   CE  HE3  sing N N 341 
MET   OXT HXT  sing N N 342 
NAG   C1  C2   sing N N 343 
NAG   C1  O1   sing N N 344 
NAG   C1  O5   sing N N 345 
NAG   C1  H1   sing N N 346 
NAG   C2  C3   sing N N 347 
NAG   C2  N2   sing N N 348 
NAG   C2  H2   sing N N 349 
NAG   C3  C4   sing N N 350 
NAG   C3  O3   sing N N 351 
NAG   C3  H3   sing N N 352 
NAG   C4  C5   sing N N 353 
NAG   C4  O4   sing N N 354 
NAG   C4  H4   sing N N 355 
NAG   C5  C6   sing N N 356 
NAG   C5  O5   sing N N 357 
NAG   C5  H5   sing N N 358 
NAG   C6  O6   sing N N 359 
NAG   C6  H61  sing N N 360 
NAG   C6  H62  sing N N 361 
NAG   C7  C8   sing N N 362 
NAG   C7  N2   sing N N 363 
NAG   C7  O7   doub N N 364 
NAG   C8  H81  sing N N 365 
NAG   C8  H82  sing N N 366 
NAG   C8  H83  sing N N 367 
NAG   N2  HN2  sing N N 368 
NAG   O1  HO1  sing N N 369 
NAG   O3  HO3  sing N N 370 
NAG   O4  HO4  sing N N 371 
NAG   O6  HO6  sing N N 372 
PHE   N   CA   sing N N 373 
PHE   N   H    sing N N 374 
PHE   N   H2   sing N N 375 
PHE   CA  C    sing N N 376 
PHE   CA  CB   sing N N 377 
PHE   CA  HA   sing N N 378 
PHE   C   O    doub N N 379 
PHE   C   OXT  sing N N 380 
PHE   CB  CG   sing N N 381 
PHE   CB  HB2  sing N N 382 
PHE   CB  HB3  sing N N 383 
PHE   CG  CD1  doub Y N 384 
PHE   CG  CD2  sing Y N 385 
PHE   CD1 CE1  sing Y N 386 
PHE   CD1 HD1  sing N N 387 
PHE   CD2 CE2  doub Y N 388 
PHE   CD2 HD2  sing N N 389 
PHE   CE1 CZ   doub Y N 390 
PHE   CE1 HE1  sing N N 391 
PHE   CE2 CZ   sing Y N 392 
PHE   CE2 HE2  sing N N 393 
PHE   CZ  HZ   sing N N 394 
PHE   OXT HXT  sing N N 395 
PRO   N   CA   sing N N 396 
PRO   N   CD   sing N N 397 
PRO   N   H    sing N N 398 
PRO   CA  C    sing N N 399 
PRO   CA  CB   sing N N 400 
PRO   CA  HA   sing N N 401 
PRO   C   O    doub N N 402 
PRO   C   OXT  sing N N 403 
PRO   CB  CG   sing N N 404 
PRO   CB  HB2  sing N N 405 
PRO   CB  HB3  sing N N 406 
PRO   CG  CD   sing N N 407 
PRO   CG  HG2  sing N N 408 
PRO   CG  HG3  sing N N 409 
PRO   CD  HD2  sing N N 410 
PRO   CD  HD3  sing N N 411 
PRO   OXT HXT  sing N N 412 
SER   N   CA   sing N N 413 
SER   N   H    sing N N 414 
SER   N   H2   sing N N 415 
SER   CA  C    sing N N 416 
SER   CA  CB   sing N N 417 
SER   CA  HA   sing N N 418 
SER   C   O    doub N N 419 
SER   C   OXT  sing N N 420 
SER   CB  OG   sing N N 421 
SER   CB  HB2  sing N N 422 
SER   CB  HB3  sing N N 423 
SER   OG  HG   sing N N 424 
SER   OXT HXT  sing N N 425 
THR   N   CA   sing N N 426 
THR   N   H    sing N N 427 
THR   N   H2   sing N N 428 
THR   CA  C    sing N N 429 
THR   CA  CB   sing N N 430 
THR   CA  HA   sing N N 431 
THR   C   O    doub N N 432 
THR   C   OXT  sing N N 433 
THR   CB  OG1  sing N N 434 
THR   CB  CG2  sing N N 435 
THR   CB  HB   sing N N 436 
THR   OG1 HG1  sing N N 437 
THR   CG2 HG21 sing N N 438 
THR   CG2 HG22 sing N N 439 
THR   CG2 HG23 sing N N 440 
THR   OXT HXT  sing N N 441 
TRP   N   CA   sing N N 442 
TRP   N   H    sing N N 443 
TRP   N   H2   sing N N 444 
TRP   CA  C    sing N N 445 
TRP   CA  CB   sing N N 446 
TRP   CA  HA   sing N N 447 
TRP   C   O    doub N N 448 
TRP   C   OXT  sing N N 449 
TRP   CB  CG   sing N N 450 
TRP   CB  HB2  sing N N 451 
TRP   CB  HB3  sing N N 452 
TRP   CG  CD1  doub Y N 453 
TRP   CG  CD2  sing Y N 454 
TRP   CD1 NE1  sing Y N 455 
TRP   CD1 HD1  sing N N 456 
TRP   CD2 CE2  doub Y N 457 
TRP   CD2 CE3  sing Y N 458 
TRP   NE1 CE2  sing Y N 459 
TRP   NE1 HE1  sing N N 460 
TRP   CE2 CZ2  sing Y N 461 
TRP   CE3 CZ3  doub Y N 462 
TRP   CE3 HE3  sing N N 463 
TRP   CZ2 CH2  doub Y N 464 
TRP   CZ2 HZ2  sing N N 465 
TRP   CZ3 CH2  sing Y N 466 
TRP   CZ3 HZ3  sing N N 467 
TRP   CH2 HH2  sing N N 468 
TRP   OXT HXT  sing N N 469 
TYR   N   CA   sing N N 470 
TYR   N   H    sing N N 471 
TYR   N   H2   sing N N 472 
TYR   CA  C    sing N N 473 
TYR   CA  CB   sing N N 474 
TYR   CA  HA   sing N N 475 
TYR   C   O    doub N N 476 
TYR   C   OXT  sing N N 477 
TYR   CB  CG   sing N N 478 
TYR   CB  HB2  sing N N 479 
TYR   CB  HB3  sing N N 480 
TYR   CG  CD1  doub Y N 481 
TYR   CG  CD2  sing Y N 482 
TYR   CD1 CE1  sing Y N 483 
TYR   CD1 HD1  sing N N 484 
TYR   CD2 CE2  doub Y N 485 
TYR   CD2 HD2  sing N N 486 
TYR   CE1 CZ   doub Y N 487 
TYR   CE1 HE1  sing N N 488 
TYR   CE2 CZ   sing Y N 489 
TYR   CE2 HE2  sing N N 490 
TYR   CZ  OH   sing N N 491 
TYR   OH  HH   sing N N 492 
TYR   OXT HXT  sing N N 493 
VAL   N   CA   sing N N 494 
VAL   N   H    sing N N 495 
VAL   N   H2   sing N N 496 
VAL   CA  C    sing N N 497 
VAL   CA  CB   sing N N 498 
VAL   CA  HA   sing N N 499 
VAL   C   O    doub N N 500 
VAL   C   OXT  sing N N 501 
VAL   CB  CG1  sing N N 502 
VAL   CB  CG2  sing N N 503 
VAL   CB  HB   sing N N 504 
VAL   CG1 HG11 sing N N 505 
VAL   CG1 HG12 sing N N 506 
VAL   CG1 HG13 sing N N 507 
VAL   CG2 HG21 sing N N 508 
VAL   CG2 HG22 sing N N 509 
VAL   CG2 HG23 sing N N 510 
VAL   OXT HXT  sing N N 511 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States' 'R01 AI174908' 1 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States' 'P01 AI162242' 2 
# 
_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   6ONF 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9BXY 
_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]   0.015045 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014774 
_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]   0.011443 
_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  
CL 
F  
N  
O  
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   . PRO   A 1 2   ? -27.404 -19.764 -2.943  1.00 84.62  ? 43  PRO   A N   1 
ATOM   2    C  CA  . PRO   A 1 2   ? -26.839 -18.413 -3.205  1.00 89.14  ? 43  PRO   A CA  1 
ATOM   3    C  C   . PRO   A 1 2   ? -26.250 -17.718 -1.996  1.00 92.42  ? 43  PRO   A C   1 
ATOM   4    O  O   . PRO   A 1 2   ? -26.871 -16.711 -1.583  1.00 89.56  ? 43  PRO   A O   1 
ATOM   5    C  CB  . PRO   A 1 2   ? -28.064 -17.580 -3.676  1.00 73.17  ? 43  PRO   A CB  1 
ATOM   6    C  CG  . PRO   A 1 2   ? -29.333 -18.452 -3.223  1.00 70.76  ? 43  PRO   A CG  1 
ATOM   7    C  CD  . PRO   A 1 2   ? -28.807 -19.868 -3.436  1.00 77.32  ? 43  PRO   A CD  1 
ATOM   8    N  N   . VAL   A 1 3   ? -25.077 -18.089 -1.487  1.00 72.88  ? 44  VAL   A N   1 
ATOM   9    C  CA  . VAL   A 1 3   ? -24.460 -17.335 -0.398  1.00 76.80  ? 44  VAL   A CA  1 
ATOM   10   C  C   . VAL   A 1 3   ? -23.167 -16.679 -0.880  1.00 66.71  ? 44  VAL   A C   1 
ATOM   11   O  O   . VAL   A 1 3   ? -22.402 -17.294 -1.632  1.00 65.51  ? 44  VAL   A O   1 
ATOM   12   C  CB  . VAL   A 1 3   ? -24.223 -18.248 0.824   1.00 77.38  ? 44  VAL   A CB  1 
ATOM   13   C  CG1 . VAL   A 1 3   ? -23.006 -19.145 0.605   1.00 74.90  ? 44  VAL   A CG1 1 
ATOM   14   C  CG2 . VAL   A 1 3   ? -24.080 -17.412 2.095   1.00 70.21  ? 44  VAL   A CG2 1 
ATOM   15   N  N   . TRP   A 1 4   ? -22.930 -15.423 -0.457  1.00 61.88  ? 45  TRP   A N   1 
ATOM   16   C  CA  . TRP   A 1 4   ? -21.730 -14.667 -0.829  1.00 68.48  ? 45  TRP   A CA  1 
ATOM   17   C  C   . TRP   A 1 4   ? -21.255 -13.795 0.333   1.00 64.75  ? 45  TRP   A C   1 
ATOM   18   O  O   . TRP   A 1 4   ? -21.994 -13.523 1.284   1.00 63.47  ? 45  TRP   A O   1 
ATOM   19   C  CB  . TRP   A 1 4   ? -21.970 -13.775 -2.060  1.00 56.97  ? 45  TRP   A CB  1 
ATOM   20   C  CG  . TRP   A 1 4   ? -22.985 -12.703 -1.782  1.00 58.58  ? 45  TRP   A CG  1 
ATOM   21   C  CD1 . TRP   A 1 4   ? -22.779 -11.510 -1.133  1.00 52.50  ? 45  TRP   A CD1 1 
ATOM   22   C  CD2 . TRP   A 1 4   ? -24.382 -12.758 -2.080  1.00 51.74  ? 45  TRP   A CD2 1 
ATOM   23   N  NE1 . TRP   A 1 4   ? -23.959 -10.820 -1.028  1.00 55.84  ? 45  TRP   A NE1 1 
ATOM   24   C  CE2 . TRP   A 1 4   ? -24.958 -11.560 -1.607  1.00 57.02  ? 45  TRP   A CE2 1 
ATOM   25   C  CE3 . TRP   A 1 4   ? -25.204 -13.704 -2.710  1.00 55.68  ? 45  TRP   A CE3 1 
ATOM   26   C  CZ2 . TRP   A 1 4   ? -26.319 -11.284 -1.741  1.00 61.54  ? 45  TRP   A CZ2 1 
ATOM   27   C  CZ3 . TRP   A 1 4   ? -26.550 -13.428 -2.852  1.00 51.36  ? 45  TRP   A CZ3 1 
ATOM   28   C  CH2 . TRP   A 1 4   ? -27.098 -12.229 -2.368  1.00 55.69  ? 45  TRP   A CH2 1 
ATOM   29   N  N   . LYS   A 1 5   ? -20.009 -13.318 0.215   1.00 61.18  ? 46  LYS   A N   1 
ATOM   30   C  CA  . LYS   A 1 5   ? -19.402 -12.386 1.153   1.00 60.22  ? 46  LYS   A CA  1 
ATOM   31   C  C   . LYS   A 1 5   ? -18.571 -11.373 0.375   1.00 61.72  ? 46  LYS   A C   1 
ATOM   32   O  O   . LYS   A 1 5   ? -18.034 -11.671 -0.698  1.00 55.98  ? 46  LYS   A O   1 
ATOM   33   C  CB  . LYS   A 1 5   ? -18.539 -13.118 2.203   1.00 62.85  ? 46  LYS   A CB  1 
ATOM   34   C  CG  . LYS   A 1 5   ? -17.018 -13.081 1.982   1.00 69.22  ? 46  LYS   A CG  1 
ATOM   35   C  CD  . LYS   A 1 5   ? -16.290 -14.128 2.850   1.00 75.16  ? 46  LYS   A CD  1 
ATOM   36   C  CE  . LYS   A 1 5   ? -15.019 -14.683 2.171   1.00 74.90  ? 46  LYS   A CE  1 
ATOM   37   N  NZ  . LYS   A 1 5   ? -14.285 -15.745 2.948   1.00 78.96  ? 46  LYS   A NZ  1 
ATOM   38   N  N   . ASP   A 1 6   ? -18.503 -10.160 0.918   1.00 52.37  ? 47  ASP   A N   1 
ATOM   39   C  CA  . ASP   A 1 6   ? -17.650 -9.123  0.365   1.00 61.73  ? 47  ASP   A CA  1 
ATOM   40   C  C   . ASP   A 1 6   ? -16.235 -9.667  0.192   1.00 65.86  ? 47  ASP   A C   1 
ATOM   41   O  O   . ASP   A 1 6   ? -15.695 -10.325 1.087   1.00 58.05  ? 47  ASP   A O   1 
ATOM   42   C  CB  . ASP   A 1 6   ? -17.651 -7.901  1.291   1.00 67.57  ? 47  ASP   A CB  1 
ATOM   43   C  CG  . ASP   A 1 6   ? -18.851 -6.991  1.070   1.00 79.24  ? 47  ASP   A CG  1 
ATOM   44   O  OD1 . ASP   A 1 6   ? -19.826 -7.427  0.416   1.00 75.01  ? 47  ASP   A OD1 1 
ATOM   45   O  OD2 . ASP   A 1 6   ? -18.812 -5.825  1.533   1.00 85.57  ? 47  ASP   A OD2 1 
ATOM   46   N  N   . ALA   A 1 7   ? -15.648 -9.423  -0.977  1.00 58.40  ? 48  ALA   A N   1 
ATOM   47   C  CA  . ALA   A 1 7   ? -14.290 -9.875  -1.246  1.00 56.90  ? 48  ALA   A CA  1 
ATOM   48   C  C   . ALA   A 1 7   ? -13.689 -9.015  -2.342  1.00 62.55  ? 48  ALA   A C   1 
ATOM   49   O  O   . ALA   A 1 7   ? -14.398 -8.315  -3.075  1.00 58.29  ? 48  ALA   A O   1 
ATOM   50   C  CB  . ALA   A 1 7   ? -14.245 -11.351 -1.662  1.00 56.68  ? 48  ALA   A CB  1 
ATOM   51   N  N   . ASP   A 1 8   ? -12.365 -9.093  -2.443  1.00 57.74  ? 49  ASP   A N   1 
ATOM   52   C  CA  . ASP   A 1 8   ? -11.590 -8.440  -3.484  1.00 55.55  ? 49  ASP   A CA  1 
ATOM   53   C  C   . ASP   A 1 8   ? -10.825 -9.506  -4.250  1.00 60.52  ? 49  ASP   A C   1 
ATOM   54   O  O   . ASP   A 1 8   ? -10.369 -10.493 -3.667  1.00 61.12  ? 49  ASP   A O   1 
ATOM   55   C  CB  . ASP   A 1 8   ? -10.593 -7.422  -2.917  1.00 54.94  ? 49  ASP   A CB  1 
ATOM   56   C  CG  . ASP   A 1 8   ? -11.260 -6.138  -2.407  1.00 73.52  ? 49  ASP   A CG  1 
ATOM   57   O  OD1 . ASP   A 1 8   ? -10.518 -5.213  -1.982  1.00 65.21  ? 49  ASP   A OD1 1 
ATOM   58   O  OD2 . ASP   A 1 8   ? -12.513 -6.058  -2.399  1.00 65.31  ? 49  ASP   A OD2 1 
ATOM   59   N  N   . THR   A 1 9   ? -10.672 -9.294  -5.550  1.00 54.06  ? 50  THR   A N   1 
ATOM   60   C  CA  . THR   A 1 9   ? -9.976  -10.247 -6.392  1.00 57.65  ? 50  THR   A CA  1 
ATOM   61   C  C   . THR   A 1 9   ? -9.560  -9.517  -7.658  1.00 49.99  ? 50  THR   A C   1 
ATOM   62   O  O   . THR   A 1 9   ? -10.077 -8.443  -7.961  1.00 52.20  ? 50  THR   A O   1 
ATOM   63   C  CB  . THR   A 1 9   ? -10.860 -11.463 -6.703  1.00 61.95  ? 50  THR   A CB  1 
ATOM   64   O  OG1 . THR   A 1 9   ? -10.038 -12.549 -7.139  1.00 61.83  ? 50  THR   A OG1 1 
ATOM   65   C  CG2 . THR   A 1 9   ? -11.894 -11.125 -7.785  1.00 46.78  ? 50  THR   A CG2 1 
ATOM   66   N  N   . THR   A 1 10  ? -8.588  -10.087 -8.371  1.00 50.33  ? 51  THR   A N   1 
ATOM   67   C  CA  . THR   A 1 10  ? -8.176  -9.529  -9.654  1.00 48.85  ? 51  THR   A CA  1 
ATOM   68   C  C   . THR   A 1 10  ? -9.261  -9.753  -10.691 1.00 53.67  ? 51  THR   A C   1 
ATOM   69   O  O   . THR   A 1 10  ? -9.701  -10.886 -10.904 1.00 48.33  ? 51  THR   A O   1 
ATOM   70   C  CB  . THR   A 1 10  ? -6.888  -10.183 -10.132 1.00 51.06  ? 51  THR   A CB  1 
ATOM   71   O  OG1 . THR   A 1 10  ? -5.866  -9.980  -9.151  1.00 63.34  ? 51  THR   A OG1 1 
ATOM   72   C  CG2 . THR   A 1 10  ? -6.462  -9.616  -11.475 1.00 46.02  ? 51  THR   A CG2 1 
ATOM   73   N  N   . LEU   A 1 11  ? -9.701  -8.678  -11.327 1.00 42.94  ? 52  LEU   A N   1 
ATOM   74   C  CA  . LEU   A 1 11  ? -10.669 -8.781  -12.403 1.00 46.04  ? 52  LEU   A CA  1 
ATOM   75   C  C   . LEU   A 1 11  ? -9.934  -9.036  -13.718 1.00 38.36  ? 52  LEU   A C   1 
ATOM   76   O  O   . LEU   A 1 11  ? -8.704  -8.923  -13.803 1.00 50.29  ? 52  LEU   A O   1 
ATOM   77   C  CB  . LEU   A 1 11  ? -11.510 -7.503  -12.467 1.00 39.94  ? 52  LEU   A CB  1 
ATOM   78   C  CG  . LEU   A 1 11  ? -12.300 -7.208  -11.180 1.00 49.33  ? 52  LEU   A CG  1 
ATOM   79   C  CD1 . LEU   A 1 11  ? -13.201 -6.018  -11.327 1.00 48.84  ? 52  LEU   A CD1 1 
ATOM   80   C  CD2 . LEU   A 1 11  ? -13.124 -8.392  -10.714 1.00 50.09  ? 52  LEU   A CD2 1 
ATOM   81   N  N   . PHE   A 1 12  ? -10.692 -9.411  -14.743 1.00 35.10  ? 53  PHE   A N   1 
ATOM   82   C  CA  . PHE   A 1 12  ? -10.209 -9.353  -16.118 1.00 41.28  ? 53  PHE   A CA  1 
ATOM   83   C  C   . PHE   A 1 12  ? -11.136 -8.464  -16.943 1.00 43.93  ? 53  PHE   A C   1 
ATOM   84   O  O   . PHE   A 1 12  ? -12.222 -8.076  -16.491 1.00 43.34  ? 53  PHE   A O   1 
ATOM   85   C  CB  . PHE   A 1 12  ? -10.055 -10.759 -16.750 1.00 43.14  ? 53  PHE   A CB  1 
ATOM   86   C  CG  . PHE   A 1 12  ? -11.366 -11.477 -17.064 1.00 50.19  ? 53  PHE   A CG  1 
ATOM   87   C  CD1 . PHE   A 1 12  ? -12.100 -11.213 -18.226 1.00 46.47  ? 53  PHE   A CD1 1 
ATOM   88   C  CD2 . PHE   A 1 12  ? -11.844 -12.445 -16.187 1.00 50.98  ? 53  PHE   A CD2 1 
ATOM   89   C  CE1 . PHE   A 1 12  ? -13.295 -11.911 -18.499 1.00 41.56  ? 53  PHE   A CE1 1 
ATOM   90   C  CE2 . PHE   A 1 12  ? -13.024 -13.130 -16.449 1.00 50.10  ? 53  PHE   A CE2 1 
ATOM   91   C  CZ  . PHE   A 1 12  ? -13.751 -12.860 -17.599 1.00 49.52  ? 53  PHE   A CZ  1 
ATOM   92   N  N   . CYS   A 1 13  ? -10.687 -8.113  -18.150 1.00 33.91  ? 54  CYS   A N   1 
ATOM   93   C  CA  . CYS   A 1 13  ? -11.412 -7.142  -18.953 1.00 38.98  ? 54  CYS   A CA  1 
ATOM   94   C  C   . CYS   A 1 13  ? -11.825 -7.754  -20.278 1.00 37.73  ? 54  CYS   A C   1 
ATOM   95   O  O   . CYS   A 1 13  ? -11.228 -8.721  -20.757 1.00 42.34  ? 54  CYS   A O   1 
ATOM   96   C  CB  . CYS   A 1 13  ? -10.583 -5.868  -19.200 1.00 39.49  ? 54  CYS   A CB  1 
ATOM   97   S  SG  . CYS   A 1 13  ? -8.982  -6.146  -20.064 1.00 60.93  ? 54  CYS   A SG  1 
ATOM   98   N  N   . ALA   A 1 14  ? -12.861 -7.151  -20.862 1.00 34.09  ? 55  ALA   A N   1 
ATOM   99   C  CA  . ALA   A 1 14  ? -13.457 -7.619  -22.094 1.00 37.74  ? 55  ALA   A CA  1 
ATOM   100  C  C   . ALA   A 1 14  ? -13.887 -6.418  -22.909 1.00 35.26  ? 55  ALA   A C   1 
ATOM   101  O  O   . ALA   A 1 14  ? -14.341 -5.410  -22.354 1.00 41.39  ? 55  ALA   A O   1 
ATOM   102  C  CB  . ALA   A 1 14  ? -14.663 -8.523  -21.829 1.00 34.35  ? 55  ALA   A CB  1 
ATOM   103  N  N   . SER   A 1 15  ? -13.735 -6.525  -24.226 1.00 40.00  ? 56  SER   A N   1 
ATOM   104  C  CA  . SER   A 1 15  ? -14.028 -5.413  -25.115 1.00 42.20  ? 56  SER   A CA  1 
ATOM   105  C  C   . SER   A 1 15  ? -14.346 -5.946  -26.498 1.00 44.41  ? 56  SER   A C   1 
ATOM   106  O  O   . SER   A 1 15  ? -14.049 -7.096  -26.833 1.00 39.37  ? 56  SER   A O   1 
ATOM   107  C  CB  . SER   A 1 15  ? -12.856 -4.434  -25.203 1.00 40.66  ? 56  SER   A CB  1 
ATOM   108  O  OG  . SER   A 1 15  ? -12.135 -4.678  -26.388 1.00 49.77  ? 56  SER   A OG  1 
ATOM   109  N  N   . ASP   A 1 16  ? -14.953 -5.074  -27.302 1.00 41.09  ? 57  ASP   A N   1 
ATOM   110  C  CA  . ASP   A 1 16  ? -15.183 -5.310  -28.716 1.00 47.43  ? 57  ASP   A CA  1 
ATOM   111  C  C   . ASP   A 1 16  ? -14.054 -4.771  -29.578 1.00 38.30  ? 57  ASP   A C   1 
ATOM   112  O  O   . ASP   A 1 16  ? -14.283 -4.444  -30.742 1.00 53.14  ? 57  ASP   A O   1 
ATOM   113  C  CB  . ASP   A 1 16  ? -16.509 -4.677  -29.137 1.00 49.03  ? 57  ASP   A CB  1 
ATOM   114  C  CG  . ASP   A 1 16  ? -17.687 -5.336  -28.466 1.00 60.31  ? 57  ASP   A CG  1 
ATOM   115  O  OD1 . ASP   A 1 16  ? -17.607 -6.559  -28.205 1.00 68.97  ? 57  ASP   A OD1 1 
ATOM   116  O  OD2 . ASP   A 1 16  ? -18.687 -4.640  -28.197 1.00 66.54  ? 57  ASP   A OD2 1 
ATOM   117  N  N   . ALA   A 1 17  ? -12.845 -4.646  -29.028 1.00 38.44  ? 58  ALA   A N   1 
ATOM   118  C  CA  . ALA   A 1 17  ? -11.718 -4.142  -29.807 1.00 39.00  ? 58  ALA   A CA  1 
ATOM   119  C  C   . ALA   A 1 17  ? -11.640 -4.837  -31.164 1.00 43.23  ? 58  ALA   A C   1 
ATOM   120  O  O   . ALA   A 1 17  ? -11.899 -6.040  -31.286 1.00 48.04  ? 58  ALA   A O   1 
ATOM   121  C  CB  . ALA   A 1 17  ? -10.410 -4.354  -29.042 1.00 41.55  ? 58  ALA   A CB  1 
ATOM   122  N  N   . LYS   A 1 18  ? -11.273 -4.068  -32.186 1.00 42.22  ? 59  LYS   A N   1 
ATOM   123  C  CA  . LYS   A 1 18  ? -11.052 -4.590  -33.531 1.00 42.60  ? 59  LYS   A CA  1 
ATOM   124  C  C   . LYS   A 1 18  ? -9.561  -4.870  -33.733 1.00 50.10  ? 59  LYS   A C   1 
ATOM   125  O  O   . LYS   A 1 18  ? -8.723  -3.991  -33.511 1.00 44.28  ? 59  LYS   A O   1 
ATOM   126  C  CB  . LYS   A 1 18  ? -11.568 -3.590  -34.563 1.00 56.09  ? 59  LYS   A CB  1 
ATOM   127  C  CG  . LYS   A 1 18  ? -13.052 -3.270  -34.379 1.00 65.44  ? 59  LYS   A CG  1 
ATOM   128  C  CD  . LYS   A 1 18  ? -13.799 -3.188  -35.714 1.00 81.58  ? 59  LYS   A CD  1 
ATOM   129  C  CE  . LYS   A 1 18  ? -14.410 -4.542  -36.169 1.00 82.20  ? 59  LYS   A CE  1 
ATOM   130  N  NZ  . LYS   A 1 18  ? -15.256 -4.433  -37.424 1.00 71.62  ? 59  LYS   A NZ  1 
ATOM   131  N  N   . ALA   A 1 19  ? -9.228  -6.104  -34.139 1.00 54.87  ? 60  ALA   A N   1 
ATOM   132  C  CA  . ALA   A 1 19  ? -7.826  -6.503  -34.253 1.00 50.26  ? 60  ALA   A CA  1 
ATOM   133  C  C   . ALA   A 1 19  ? -7.103  -5.795  -35.395 1.00 44.73  ? 60  ALA   A C   1 
ATOM   134  O  O   . ALA   A 1 19  ? -5.878  -5.666  -35.356 1.00 74.28  ? 60  ALA   A O   1 
ATOM   135  C  CB  . ALA   A 1 19  ? -7.729  -8.016  -34.424 1.00 50.84  ? 60  ALA   A CB  1 
ATOM   136  N  N   . TYR   A 1 20  ? -7.829  -5.335  -36.400 1.00 51.30  ? 61  TYR   A N   1 
ATOM   137  C  CA  . TYR   A 1 20  ? -7.246  -4.597  -37.509 1.00 51.32  ? 61  TYR   A CA  1 
ATOM   138  C  C   . TYR   A 1 20  ? -7.058  -3.112  -37.223 1.00 65.43  ? 61  TYR   A C   1 
ATOM   139  O  O   . TYR   A 1 20  ? -6.361  -2.430  -37.983 1.00 66.53  ? 61  TYR   A O   1 
ATOM   140  C  CB  . TYR   A 1 20  ? -8.126  -4.764  -38.734 1.00 50.24  ? 61  TYR   A CB  1 
ATOM   141  C  CG  . TYR   A 1 20  ? -9.503  -4.162  -38.618 1.00 51.93  ? 61  TYR   A CG  1 
ATOM   142  C  CD1 . TYR   A 1 20  ? -9.704  -2.803  -38.774 1.00 59.60  ? 61  TYR   A CD1 1 
ATOM   143  C  CD2 . TYR   A 1 20  ? -10.609 -4.961  -38.385 1.00 61.32  ? 61  TYR   A CD2 1 
ATOM   144  C  CE1 . TYR   A 1 20  ? -10.970 -2.249  -38.702 1.00 65.05  ? 61  TYR   A CE1 1 
ATOM   145  C  CE2 . TYR   A 1 20  ? -11.882 -4.425  -38.306 1.00 61.00  ? 61  TYR   A CE2 1 
ATOM   146  C  CZ  . TYR   A 1 20  ? -12.055 -3.064  -38.467 1.00 65.88  ? 61  TYR   A CZ  1 
ATOM   147  O  OH  . TYR   A 1 20  ? -13.318 -2.513  -38.392 1.00 64.31  ? 61  TYR   A OH  1 
ATOM   148  N  N   . GLU   A 1 21  ? -7.653  -2.593  -36.156 1.00 62.51  ? 62  GLU   A N   1 
ATOM   149  C  CA  . GLU   A 1 21  ? -7.608  -1.161  -35.891 1.00 58.31  ? 62  GLU   A CA  1 
ATOM   150  C  C   . GLU   A 1 21  ? -6.247  -0.773  -35.324 1.00 50.41  ? 62  GLU   A C   1 
ATOM   151  O  O   . GLU   A 1 21  ? -5.672  -1.495  -34.505 1.00 50.95  ? 62  GLU   A O   1 
ATOM   152  C  CB  . GLU   A 1 21  ? -8.722  -0.788  -34.909 1.00 46.89  ? 62  GLU   A CB  1 
ATOM   153  C  CG  . GLU   A 1 21  ? -8.921  0.688   -34.642 1.00 62.29  ? 62  GLU   A CG  1 
ATOM   154  C  CD  . GLU   A 1 21  ? -9.241  1.481   -35.882 1.00 63.07  ? 62  GLU   A CD  1 
ATOM   155  O  OE1 . GLU   A 1 21  ? -8.289  1.913   -36.572 1.00 65.49  ? 62  GLU   A OE1 1 
ATOM   156  O  OE2 . GLU   A 1 21  ? -10.441 1.641   -36.189 1.00 71.16  ? 62  GLU   A OE2 1 
ATOM   157  N  N   . THR   A 1 22  ? -5.736  0.392   -35.752 1.00 57.87  ? 63  THR   A N   1 
ATOM   158  C  CA  . THR   A 1 22  ? -4.509  0.973   -35.209 1.00 48.73  ? 63  THR   A CA  1 
ATOM   159  C  C   . THR   A 1 22  ? -4.763  1.899   -34.017 1.00 54.90  ? 63  THR   A C   1 
ATOM   160  O  O   . THR   A 1 22  ? -3.826  2.173   -33.255 1.00 47.37  ? 63  THR   A O   1 
ATOM   161  C  CB  . THR   A 1 22  ? -3.754  1.741   -36.320 1.00 67.89  ? 63  THR   A CB  1 
ATOM   162  O  OG1 . THR   A 1 22  ? -4.697  2.392   -37.198 1.00 56.29  ? 63  THR   A OG1 1 
ATOM   163  C  CG2 . THR   A 1 22  ? -2.905  0.779   -37.155 1.00 62.02  ? 63  THR   A CG2 1 
ATOM   164  N  N   . GLU   A 1 23  ? -6.002  2.377   -33.838 1.00 54.28  ? 64  GLU   A N   1 
ATOM   165  C  CA  . GLU   A 1 23  ? -6.379  3.180   -32.674 1.00 50.83  ? 64  GLU   A CA  1 
ATOM   166  C  C   . GLU   A 1 23  ? -5.900  2.491   -31.399 1.00 48.82  ? 64  GLU   A C   1 
ATOM   167  O  O   . GLU   A 1 23  ? -6.034  1.273   -31.258 1.00 52.29  ? 64  GLU   A O   1 
ATOM   168  C  CB  . GLU   A 1 23  ? -7.900  3.383   -32.665 1.00 43.82  ? 64  GLU   A CB  1 
ATOM   169  C  CG  . GLU   A 1 23  ? -8.414  4.440   -31.718 1.00 45.99  ? 64  GLU   A CG  1 
ATOM   170  C  CD  . GLU   A 1 23  ? -8.283  4.018   -30.266 1.00 51.06  ? 64  GLU   A CD  1 
ATOM   171  O  OE1 . GLU   A 1 23  ? -8.610  2.837   -29.965 1.00 42.66  ? 64  GLU   A OE1 1 
ATOM   172  O  OE2 . GLU   A 1 23  ? -7.861  4.863   -29.428 1.00 50.46  ? 64  GLU   A OE2 1 
ATOM   173  N  N   . VAL   A 1 24  ? -5.340  3.274   -30.469 1.00 42.58  ? 65  VAL   A N   1 
ATOM   174  C  CA  . VAL   A 1 24  ? -4.512  2.698   -29.408 1.00 42.95  ? 65  VAL   A CA  1 
ATOM   175  C  C   . VAL   A 1 24  ? -5.325  2.010   -28.316 1.00 48.62  ? 65  VAL   A C   1 
ATOM   176  O  O   . VAL   A 1 24  ? -4.781  1.175   -27.583 1.00 41.35  ? 65  VAL   A O   1 
ATOM   177  C  CB  . VAL   A 1 24  ? -3.607  3.793   -28.808 1.00 54.77  ? 65  VAL   A CB  1 
ATOM   178  C  CG1 . VAL   A 1 24  ? -2.686  4.360   -29.868 1.00 47.16  ? 65  VAL   A CG1 1 
ATOM   179  C  CG2 . VAL   A 1 24  ? -4.456  4.895   -28.198 1.00 42.14  ? 65  VAL   A CG2 1 
ATOM   180  N  N   . HIS   A 1 25  ? -6.599  2.385   -28.130 1.00 44.74  ? 66  HIS   A N   1 
ATOM   181  C  CA  . HIS   A 1 25  ? -7.428  1.662   -27.169 1.00 38.89  ? 66  HIS   A CA  1 
ATOM   182  C  C   . HIS   A 1 25  ? -7.765  0.271   -27.711 1.00 38.54  ? 66  HIS   A C   1 
ATOM   183  O  O   . HIS   A 1 25  ? -7.716  -0.720  -26.967 1.00 43.90  ? 66  HIS   A O   1 
ATOM   184  C  CB  . HIS   A 1 25  ? -8.700  2.464   -26.851 1.00 39.84  ? 66  HIS   A CB  1 
ATOM   185  C  CG  . HIS   A 1 25  ? -8.460  3.730   -26.079 1.00 36.63  ? 66  HIS   A CG  1 
ATOM   186  N  ND1 . HIS   A 1 25  ? -8.230  4.945   -26.685 1.00 42.31  ? 66  HIS   A ND1 1 
ATOM   187  C  CD2 . HIS   A 1 25  ? -8.468  3.976   -24.744 1.00 37.97  ? 66  HIS   A CD2 1 
ATOM   188  C  CE1 . HIS   A 1 25  ? -8.067  5.876   -25.757 1.00 43.85  ? 66  HIS   A CE1 1 
ATOM   189  N  NE2 . HIS   A 1 25  ? -8.216  5.316   -24.570 1.00 41.31  ? 66  HIS   A NE2 1 
ATOM   190  N  N   . ASN   A 1 26  ? -8.079  0.173   -29.010 1.00 40.29  ? 67  ASN   A N   1 
ATOM   191  C  CA  . ASN   A 1 26  ? -8.292  -1.148  -29.607 1.00 47.57  ? 67  ASN   A CA  1 
ATOM   192  C  C   . ASN   A 1 26  ? -7.022  -1.996  -29.502 1.00 50.93  ? 67  ASN   A C   1 
ATOM   193  O  O   . ASN   A 1 26  ? -7.068  -3.151  -29.063 1.00 48.95  ? 67  ASN   A O   1 
ATOM   194  C  CB  . ASN   A 1 26  ? -8.745  -1.041  -31.065 1.00 40.40  ? 67  ASN   A CB  1 
ATOM   195  C  CG  . ASN   A 1 26  ? -10.150 -0.429  -31.222 1.00 44.43  ? 67  ASN   A CG  1 
ATOM   196  O  OD1 . ASN   A 1 26  ? -11.139 -1.134  -31.422 1.00 38.88  ? 67  ASN   A OD1 1 
ATOM   197  N  ND2 . ASN   A 1 26  ? -10.217 0.894   -31.212 1.00 43.04  ? 67  ASN   A ND2 1 
ATOM   198  N  N   . VAL   A 1 27  ? -5.869  -1.427  -29.862 1.00 39.54  ? 68  VAL   A N   1 
ATOM   199  C  CA  . VAL   A 1 27  ? -4.611  -2.166  -29.743 1.00 45.01  ? 68  VAL   A CA  1 
ATOM   200  C  C   . VAL   A 1 27  ? -4.451  -2.721  -28.337 1.00 54.98  ? 68  VAL   A C   1 
ATOM   201  O  O   . VAL   A 1 27  ? -4.137  -3.905  -28.146 1.00 47.69  ? 68  VAL   A O   1 
ATOM   202  C  CB  . VAL   A 1 27  ? -3.414  -1.276  -30.125 1.00 44.00  ? 68  VAL   A CB  1 
ATOM   203  C  CG1 . VAL   A 1 27  ? -2.090  -1.952  -29.786 1.00 50.15  ? 68  VAL   A CG1 1 
ATOM   204  C  CG2 . VAL   A 1 27  ? -3.465  -0.937  -31.584 1.00 41.42  ? 68  VAL   A CG2 1 
ATOM   205  N  N   . TRP   A 1 28  ? -4.658  -1.870  -27.331 1.00 50.24  ? 69  TRP   A N   1 
ATOM   206  C  CA  . TRP   A 1 28  ? -4.473  -2.289  -25.950 1.00 44.01  ? 69  TRP   A CA  1 
ATOM   207  C  C   . TRP   A 1 28  ? -5.468  -3.372  -25.547 1.00 48.42  ? 69  TRP   A C   1 
ATOM   208  O  O   . TRP   A 1 28  ? -5.105  -4.304  -24.819 1.00 44.13  ? 69  TRP   A O   1 
ATOM   209  C  CB  . TRP   A 1 28  ? -4.593  -1.085  -25.020 1.00 41.67  ? 69  TRP   A CB  1 
ATOM   210  C  CG  . TRP   A 1 28  ? -4.395  -1.454  -23.606 1.00 37.30  ? 69  TRP   A CG  1 
ATOM   211  C  CD1 . TRP   A 1 28  ? -3.205  -1.561  -22.947 1.00 43.27  ? 69  TRP   A CD1 1 
ATOM   212  C  CD2 . TRP   A 1 28  ? -5.404  -1.804  -22.666 1.00 38.96  ? 69  TRP   A CD2 1 
ATOM   213  N  NE1 . TRP   A 1 28  ? -3.413  -1.942  -21.654 1.00 38.43  ? 69  TRP   A NE1 1 
ATOM   214  C  CE2 . TRP   A 1 28  ? -4.760  -2.100  -21.454 1.00 44.08  ? 69  TRP   A CE2 1 
ATOM   215  C  CE3 . TRP   A 1 28  ? -6.792  -1.896  -22.728 1.00 41.95  ? 69  TRP   A CE3 1 
ATOM   216  C  CZ2 . TRP   A 1 28  ? -5.462  -2.485  -20.314 1.00 39.81  ? 69  TRP   A CZ2 1 
ATOM   217  C  CZ3 . TRP   A 1 28  ? -7.479  -2.251  -21.603 1.00 34.75  ? 69  TRP   A CZ3 1 
ATOM   218  C  CH2 . TRP   A 1 28  ? -6.821  -2.545  -20.413 1.00 37.13  ? 69  TRP   A CH2 1 
ATOM   219  N  N   . ALA   A 1 29  ? -6.729  -3.253  -25.986 1.00 41.93  ? 70  ALA   A N   1 
ATOM   220  C  CA  . ALA   A 1 29  ? -7.759  -4.188  -25.551 1.00 37.03  ? 70  ALA   A CA  1 
ATOM   221  C  C   . ALA   A 1 29  ? -7.592  -5.529  -26.234 1.00 44.15  ? 70  ALA   A C   1 
ATOM   222  O  O   . ALA   A 1 29  ? -7.934  -6.575  -25.660 1.00 41.04  ? 70  ALA   A O   1 
ATOM   223  C  CB  . ALA   A 1 29  ? -9.140  -3.619  -25.846 1.00 45.65  ? 70  ALA   A CB  1 
ATOM   224  N  N   . THR   A 1 30  ? -7.074  -5.502  -27.461 1.00 49.55  ? 71  THR   A N   1 
ATOM   225  C  CA  . THR   A 1 30  ? -6.831  -6.724  -28.208 1.00 46.13  ? 71  THR   A CA  1 
ATOM   226  C  C   . THR   A 1 30  ? -5.892  -7.652  -27.460 1.00 51.65  ? 71  THR   A C   1 
ATOM   227  O  O   . THR   A 1 30  ? -6.146  -8.859  -27.385 1.00 49.46  ? 71  THR   A O   1 
ATOM   228  C  CB  . THR   A 1 30  ? -6.264  -6.380  -29.570 1.00 49.83  ? 71  THR   A CB  1 
ATOM   229  O  OG1 . THR   A 1 30  ? -7.330  -5.908  -30.414 1.00 51.37  ? 71  THR   A OG1 1 
ATOM   230  C  CG2 . THR   A 1 30  ? -5.657  -7.605  -30.200 1.00 48.92  ? 71  THR   A CG2 1 
ATOM   231  N  N   . HIS   A 1 31  ? -4.826  -7.110  -26.861 1.00 47.60  ? 72  HIS   A N   1 
ATOM   232  C  CA  . HIS   A 1 31  ? -3.829  -7.958  -26.233 1.00 44.45  ? 72  HIS   A CA  1 
ATOM   233  C  C   . HIS   A 1 31  ? -3.939  -8.045  -24.715 1.00 51.33  ? 72  HIS   A C   1 
ATOM   234  O  O   . HIS   A 1 31  ? -3.227  -8.862  -24.111 1.00 51.91  ? 72  HIS   A O   1 
ATOM   235  C  CB  . HIS   A 1 31  ? -2.424  -7.494  -26.607 1.00 56.13  ? 72  HIS   A CB  1 
ATOM   236  C  CG  . HIS   A 1 31  ? -1.978  -6.276  -25.874 1.00 56.63  ? 72  HIS   A CG  1 
ATOM   237  N  ND1 . HIS   A 1 31  ? -1.368  -6.336  -24.641 1.00 64.75  ? 72  HIS   A ND1 1 
ATOM   238  C  CD2 . HIS   A 1 31  ? -2.012  -4.968  -26.219 1.00 67.13  ? 72  HIS   A CD2 1 
ATOM   239  C  CE1 . HIS   A 1 31  ? -1.071  -5.114  -24.242 1.00 64.22  ? 72  HIS   A CE1 1 
ATOM   240  N  NE2 . HIS   A 1 31  ? -1.452  -4.265  -25.180 1.00 81.43  ? 72  HIS   A NE2 1 
ATOM   241  N  N   . ALA   A 1 32  ? -4.811  -7.261  -24.077 1.00 46.98  ? 73  ALA   A N   1 
ATOM   242  C  CA  . ALA   A 1 32  ? -4.970  -7.335  -22.635 1.00 40.53  ? 73  ALA   A CA  1 
ATOM   243  C  C   . ALA   A 1 32  ? -6.384  -7.690  -22.187 1.00 44.67  ? 73  ALA   A C   1 
ATOM   244  O  O   . ALA   A 1 32  ? -6.596  -7.902  -20.987 1.00 40.96  ? 73  ALA   A O   1 
ATOM   245  C  CB  . ALA   A 1 32  ? -4.542  -6.014  -21.976 1.00 41.86  ? 73  ALA   A CB  1 
ATOM   246  N  N   . CYS   A 1 33  ? -7.349  -7.764  -23.101 1.00 47.77  ? 74  CYS   A N   1 
ATOM   247  C  CA  . CYS   A 1 33  ? -8.714  -8.149  -22.782 1.00 49.27  ? 74  CYS   A CA  1 
ATOM   248  C  C   . CYS   A 1 33  ? -9.129  -9.289  -23.704 1.00 53.96  ? 74  CYS   A C   1 
ATOM   249  O  O   . CYS   A 1 33  ? -8.545  -9.497  -24.771 1.00 51.56  ? 74  CYS   A O   1 
ATOM   250  C  CB  . CYS   A 1 33  ? -9.696  -6.957  -22.937 1.00 35.98  ? 74  CYS   A CB  1 
ATOM   251  S  SG  . CYS   A 1 33  ? -9.255  -5.472  -21.979 1.00 46.92  ? 74  CYS   A SG  1 
ATOM   252  N  N   . VAL   A 1 34  ? -10.172 -10.007 -23.298 1.00 46.28  ? 75  VAL   A N   1 
ATOM   253  C  CA  . VAL   A 1 34  ? -10.780 -11.050 -24.124 1.00 46.47  ? 75  VAL   A CA  1 
ATOM   254  C  C   . VAL   A 1 34  ? -11.997 -10.438 -24.808 1.00 43.47  ? 75  VAL   A C   1 
ATOM   255  O  O   . VAL   A 1 34  ? -12.379 -9.310  -24.474 1.00 44.94  ? 75  VAL   A O   1 
ATOM   256  C  CB  . VAL   A 1 34  ? -11.176 -12.275 -23.277 1.00 56.76  ? 75  VAL   A CB  1 
ATOM   257  C  CG1 . VAL   A 1 34  ? -9.938  -12.980 -22.721 1.00 44.45  ? 75  VAL   A CG1 1 
ATOM   258  C  CG2 . VAL   A 1 34  ? -12.108 -11.891 -22.147 1.00 36.98  ? 75  VAL   A CG2 1 
ATOM   259  N  N   . PRO   A 1 35  ? -12.639 -11.121 -25.749 1.00 43.41  ? 76  PRO   A N   1 
ATOM   260  C  CA  . PRO   A 1 35  ? -13.835 -10.551 -26.387 1.00 42.80  ? 76  PRO   A CA  1 
ATOM   261  C  C   . PRO   A 1 35  ? -14.983 -10.417 -25.394 1.00 45.70  ? 76  PRO   A C   1 
ATOM   262  O  O   . PRO   A 1 35  ? -15.059 -11.146 -24.399 1.00 39.69  ? 76  PRO   A O   1 
ATOM   263  C  CB  . PRO   A 1 35  ? -14.159 -11.566 -27.486 1.00 43.03  ? 76  PRO   A CB  1 
ATOM   264  C  CG  . PRO   A 1 35  ? -12.832 -12.231 -27.762 1.00 45.81  ? 76  PRO   A CG  1 
ATOM   265  C  CD  . PRO   A 1 35  ? -12.191 -12.350 -26.423 1.00 46.56  ? 76  PRO   A CD  1 
ATOM   266  N  N   . THR   A 1 36  ? -15.888 -9.470  -25.664 1.00 48.04  ? 77  THR   A N   1 
ATOM   267  C  CA  . THR   A 1 36  ? -16.972 -9.275  -24.711 1.00 56.91  ? 77  THR   A CA  1 
ATOM   268  C  C   . THR   A 1 36  ? -17.909 -10.470 -24.716 1.00 47.17  ? 77  THR   A C   1 
ATOM   269  O  O   . THR   A 1 36  ? -18.019 -11.207 -25.697 1.00 56.62  ? 77  THR   A O   1 
ATOM   270  C  CB  . THR   A 1 36  ? -17.765 -8.004  -25.004 1.00 45.46  ? 77  THR   A CB  1 
ATOM   271  O  OG1 . THR   A 1 36  ? -18.414 -8.130  -26.274 1.00 67.01  ? 77  THR   A OG1 1 
ATOM   272  C  CG2 . THR   A 1 36  ? -16.862 -6.813  -25.019 1.00 46.77  ? 77  THR   A CG2 1 
ATOM   273  N  N   . ASP   A 1 37  ? -18.567 -10.664 -23.588 1.00 61.81  ? 78  ASP   A N   1 
ATOM   274  C  CA  . ASP   A 1 37  ? -19.505 -11.748 -23.338 1.00 60.52  ? 78  ASP   A CA  1 
ATOM   275  C  C   . ASP   A 1 37  ? -20.505 -11.822 -24.487 1.00 59.20  ? 78  ASP   A C   1 
ATOM   276  O  O   . ASP   A 1 37  ? -21.275 -10.879 -24.686 1.00 59.56  ? 78  ASP   A O   1 
ATOM   277  C  CB  . ASP   A 1 37  ? -20.202 -11.504 -21.991 1.00 62.21  ? 78  ASP   A CB  1 
ATOM   278  C  CG  . ASP   A 1 37  ? -20.860 -12.742 -21.428 1.00 78.93  ? 78  ASP   A CG  1 
ATOM   279  O  OD1 . ASP   A 1 37  ? -21.190 -13.652 -22.225 1.00 75.66  ? 78  ASP   A OD1 1 
ATOM   280  O  OD2 . ASP   A 1 37  ? -21.031 -12.805 -20.179 1.00 72.99  ? 78  ASP   A OD2 1 
ATOM   281  N  N   . PRO   A 1 38  ? -20.507 -12.891 -25.290 1.00 63.33  ? 79  PRO   A N   1 
ATOM   282  C  CA  . PRO   A 1 38  ? -21.504 -12.968 -26.372 1.00 64.49  ? 79  PRO   A CA  1 
ATOM   283  C  C   . PRO   A 1 38  ? -22.934 -13.031 -25.864 1.00 70.13  ? 79  PRO   A C   1 
ATOM   284  O  O   . PRO   A 1 38  ? -23.822 -12.424 -26.472 1.00 58.41  ? 79  PRO   A O   1 
ATOM   285  C  CB  . PRO   A 1 38  ? -21.100 -14.233 -27.149 1.00 59.02  ? 79  PRO   A CB  1 
ATOM   286  C  CG  . PRO   A 1 38  ? -20.146 -14.975 -26.290 1.00 58.87  ? 79  PRO   A CG  1 
ATOM   287  C  CD  . PRO   A 1 38  ? -19.520 -13.981 -25.355 1.00 66.68  ? 79  PRO   A CD  1 
ATOM   288  N  N   . ASN   A 1 39  ? -23.194 -13.721 -24.757 1.00 67.12  ? 80  ASN   A N   1 
ATOM   289  C  CA  . ASN   A 1 39  ? -24.545 -13.821 -24.207 1.00 74.07  ? 80  ASN   A CA  1 
ATOM   290  C  C   . ASN   A 1 39  ? -24.538 -13.410 -22.739 1.00 74.27  ? 80  ASN   A C   1 
ATOM   291  O  O   . ASN   A 1 39  ? -24.491 -14.264 -21.845 1.00 65.59  ? 80  ASN   A O   1 
ATOM   292  C  CB  . ASN   A 1 39  ? -25.109 -15.233 -24.372 1.00 76.06  ? 80  ASN   A CB  1 
ATOM   293  C  CG  . ASN   A 1 39  ? -26.486 -15.368 -23.768 1.00 81.77  ? 80  ASN   A CG  1 
ATOM   294  O  OD1 . ASN   A 1 39  ? -27.337 -14.486 -23.929 1.00 77.68  ? 80  ASN   A OD1 1 
ATOM   295  N  ND2 . ASN   A 1 39  ? -26.711 -16.463 -23.045 1.00 75.34  ? 80  ASN   A ND2 1 
ATOM   296  N  N   . PRO   A 1 40  ? -24.590 -12.106 -22.455 1.00 70.30  ? 81  PRO   A N   1 
ATOM   297  C  CA  . PRO   A 1 40  ? -24.519 -11.654 -21.059 1.00 72.76  ? 81  PRO   A CA  1 
ATOM   298  C  C   . PRO   A 1 40  ? -25.828 -11.946 -20.344 1.00 67.28  ? 81  PRO   A C   1 
ATOM   299  O  O   . PRO   A 1 40  ? -26.906 -11.792 -20.922 1.00 68.26  ? 81  PRO   A O   1 
ATOM   300  C  CB  . PRO   A 1 40  ? -24.250 -10.149 -21.194 1.00 60.03  ? 81  PRO   A CB  1 
ATOM   301  C  CG  . PRO   A 1 40  ? -24.838 -9.789  -22.511 1.00 62.77  ? 81  PRO   A CG  1 
ATOM   302  C  CD  . PRO   A 1 40  ? -24.535 -10.972 -23.389 1.00 65.80  ? 81  PRO   A CD  1 
ATOM   303  N  N   . GLN   A 1 41  ? -25.728 -12.427 -19.102 1.00 65.73  ? 82  GLN   A N   1 
ATOM   304  C  CA  . GLN   A 1 41  ? -26.889 -12.858 -18.325 1.00 74.72  ? 82  GLN   A CA  1 
ATOM   305  C  C   . GLN   A 1 41  ? -26.941 -12.076 -17.019 1.00 67.78  ? 82  GLN   A C   1 
ATOM   306  O  O   . GLN   A 1 41  ? -25.920 -11.921 -16.345 1.00 61.23  ? 82  GLN   A O   1 
ATOM   307  C  CB  . GLN   A 1 41  ? -26.852 -14.367 -18.039 1.00 76.82  ? 82  GLN   A CB  1 
ATOM   308  C  CG  . GLN   A 1 41  ? -27.600 -15.258 -19.058 1.00 87.27  ? 82  GLN   A CG  1 
ATOM   309  C  CD  . GLN   A 1 41  ? -28.886 -14.637 -19.615 1.00 86.08  ? 82  GLN   A CD  1 
ATOM   310  O  OE1 . GLN   A 1 41  ? -28.855 -13.894 -20.603 1.00 85.86  ? 82  GLN   A OE1 1 
ATOM   311  N  NE2 . GLN   A 1 41  ? -30.020 -14.960 -19.000 1.00 82.48  ? 82  GLN   A NE2 1 
ATOM   312  N  N   . GLU   A 1 42  ? -28.118 -11.558 -16.679 1.00 67.65  ? 83  GLU   A N   1 
ATOM   313  C  CA  . GLU   A 1 42  ? -28.303 -10.754 -15.474 1.00 68.11  ? 83  GLU   A CA  1 
ATOM   314  C  C   . GLU   A 1 42  ? -29.374 -11.408 -14.615 1.00 64.35  ? 83  GLU   A C   1 
ATOM   315  O  O   . GLU   A 1 42  ? -30.560 -11.372 -14.958 1.00 68.46  ? 83  GLU   A O   1 
ATOM   316  C  CB  . GLU   A 1 42  ? -28.700 -9.323  -15.810 1.00 60.51  ? 83  GLU   A CB  1 
ATOM   317  C  CG  . GLU   A 1 42  ? -28.642 -8.395  -14.611 1.00 58.10  ? 83  GLU   A CG  1 
ATOM   318  C  CD  . GLU   A 1 42  ? -28.780 -6.934  -15.001 1.00 85.70  ? 83  GLU   A CD  1 
ATOM   319  O  OE1 . GLU   A 1 42  ? -27.912 -6.421  -15.755 1.00 76.72  ? 83  GLU   A OE1 1 
ATOM   320  O  OE2 . GLU   A 1 42  ? -29.749 -6.293  -14.531 1.00 90.50  ? 83  GLU   A OE2 1 
ATOM   321  N  N   . ILE   A 1 43  ? -28.955 -11.994 -13.502 1.00 55.65  ? 84  ILE   A N   1 
ATOM   322  C  CA  . ILE   A 1 43  ? -29.852 -12.683 -12.584 1.00 63.42  ? 84  ILE   A CA  1 
ATOM   323  C  C   . ILE   A 1 43  ? -30.307 -11.702 -11.508 1.00 67.23  ? 84  ILE   A C   1 
ATOM   324  O  O   . ILE   A 1 43  ? -29.482 -11.133 -10.780 1.00 67.12  ? 84  ILE   A O   1 
ATOM   325  C  CB  . ILE   A 1 43  ? -29.159 -13.892 -11.947 1.00 55.77  ? 84  ILE   A CB  1 
ATOM   326  C  CG1 . ILE   A 1 43  ? -28.604 -14.818 -13.031 1.00 58.69  ? 84  ILE   A CG1 1 
ATOM   327  C  CG2 . ILE   A 1 43  ? -30.139 -14.595 -11.033 1.00 57.38  ? 84  ILE   A CG2 1 
ATOM   328  C  CD1 . ILE   A 1 43  ? -27.900 -16.077 -12.495 1.00 61.19  ? 84  ILE   A CD1 1 
ATOM   329  N  N   . HIS   A 1 44  ? -31.616 -11.516 -11.393 1.00 61.01  ? 85  HIS   A N   1 
ATOM   330  C  CA  . HIS   A 1 44  ? -32.163 -10.728 -10.303 1.00 65.62  ? 85  HIS   A CA  1 
ATOM   331  C  C   . HIS   A 1 44  ? -32.183 -11.554 -9.017  1.00 60.02  ? 85  HIS   A C   1 
ATOM   332  O  O   . HIS   A 1 44  ? -32.353 -12.777 -9.045  1.00 67.52  ? 85  HIS   A O   1 
ATOM   333  C  CB  . HIS   A 1 44  ? -33.567 -10.253 -10.636 1.00 55.13  ? 85  HIS   A CB  1 
ATOM   334  C  CG  . HIS   A 1 44  ? -34.193 -9.451  -9.544  1.00 64.54  ? 85  HIS   A CG  1 
ATOM   335  N  ND1 . HIS   A 1 44  ? -34.945 -10.016 -8.537  1.00 67.36  ? 85  HIS   A ND1 1 
ATOM   336  C  CD2 . HIS   A 1 44  ? -34.159 -8.122  -9.290  1.00 68.36  ? 85  HIS   A CD2 1 
ATOM   337  C  CE1 . HIS   A 1 44  ? -35.358 -9.065  -7.716  1.00 70.99  ? 85  HIS   A CE1 1 
ATOM   338  N  NE2 . HIS   A 1 44  ? -34.895 -7.908  -8.150  1.00 64.67  ? 85  HIS   A NE2 1 
ATOM   339  N  N   . LEU   A 1 45  ? -31.995 -10.872 -7.888  1.00 57.49  ? 86  LEU   A N   1 
ATOM   340  C  CA  . LEU   A 1 45  ? -31.918 -11.489 -6.567  1.00 70.51  ? 86  LEU   A CA  1 
ATOM   341  C  C   . LEU   A 1 45  ? -33.168 -11.091 -5.780  1.00 69.01  ? 86  LEU   A C   1 
ATOM   342  O  O   . LEU   A 1 45  ? -33.353 -9.913  -5.460  1.00 71.88  ? 86  LEU   A O   1 
ATOM   343  C  CB  . LEU   A 1 45  ? -30.646 -11.045 -5.844  1.00 67.88  ? 86  LEU   A CB  1 
ATOM   344  C  CG  . LEU   A 1 45  ? -29.287 -11.363 -6.475  1.00 65.55  ? 86  LEU   A CG  1 
ATOM   345  C  CD1 . LEU   A 1 45  ? -28.143 -11.036 -5.507  1.00 60.70  ? 86  LEU   A CD1 1 
ATOM   346  C  CD2 . LEU   A 1 45  ? -29.240 -12.819 -6.898  1.00 61.52  ? 86  LEU   A CD2 1 
ATOM   347  N  N   . GLU   A 1 46  ? -34.024 -12.063 -5.470  1.00 69.72  ? 87  GLU   A N   1 
ATOM   348  C  CA  . GLU   A 1 46  ? -35.313 -11.743 -4.867  1.00 79.41  ? 87  GLU   A CA  1 
ATOM   349  C  C   . GLU   A 1 46  ? -35.137 -11.298 -3.417  1.00 78.78  ? 87  GLU   A C   1 
ATOM   350  O  O   . GLU   A 1 46  ? -34.354 -11.889 -2.667  1.00 65.59  ? 87  GLU   A O   1 
ATOM   351  C  CB  . GLU   A 1 46  ? -36.257 -12.940 -4.965  1.00 73.60  ? 87  GLU   A CB  1 
ATOM   352  C  CG  . GLU   A 1 46  ? -37.132 -12.892 -6.212  1.00 85.01  ? 87  GLU   A CG  1 
ATOM   353  C  CD  . GLU   A 1 46  ? -37.883 -11.571 -6.361  1.00 87.27  ? 87  GLU   A CD  1 
ATOM   354  O  OE1 . GLU   A 1 46  ? -37.705 -10.660 -5.519  1.00 87.48  ? 87  GLU   A OE1 1 
ATOM   355  O  OE2 . GLU   A 1 46  ? -38.681 -11.452 -7.317  1.00 94.75  ? 87  GLU   A OE2 1 
ATOM   356  N  N   . ASN   A 1 47  ? -35.853 -10.227 -3.044  1.00 74.12  ? 88  ASN   A N   1 
ATOM   357  C  CA  . ASN   A 1 47  ? -35.841 -9.619  -1.699  1.00 77.74  ? 88  ASN   A CA  1 
ATOM   358  C  C   . ASN   A 1 47  ? -34.461 -9.670  -1.042  1.00 72.54  ? 88  ASN   A C   1 
ATOM   359  O  O   . ASN   A 1 47  ? -34.306 -10.028 0.130   1.00 70.34  ? 88  ASN   A O   1 
ATOM   360  C  CB  . ASN   A 1 47  ? -36.903 -10.249 -0.799  1.00 82.79  ? 88  ASN   A CB  1 
ATOM   361  C  CG  . ASN   A 1 47  ? -36.635 -11.705 -0.519  1.00 85.90  ? 88  ASN   A CG  1 
ATOM   362  O  OD1 . ASN   A 1 47  ? -35.637 -12.055 0.115   1.00 85.10  ? 88  ASN   A OD1 1 
ATOM   363  N  ND2 . ASN   A 1 47  ? -37.531 -12.574 -0.994  1.00 90.96  ? 88  ASN   A ND2 1 
ATOM   364  N  N   . VAL   A 1 48  ? -33.446 -9.298  -1.806  1.00 59.52  ? 89  VAL   A N   1 
ATOM   365  C  CA  . VAL   A 1 48  ? -32.095 -9.155  -1.287  1.00 62.21  ? 89  VAL   A CA  1 
ATOM   366  C  C   . VAL   A 1 48  ? -31.806 -7.675  -1.115  1.00 63.07  ? 89  VAL   A C   1 
ATOM   367  O  O   . VAL   A 1 48  ? -32.079 -6.874  -2.016  1.00 63.42  ? 89  VAL   A O   1 
ATOM   368  C  CB  . VAL   A 1 48  ? -31.054 -9.794  -2.218  1.00 62.08  ? 89  VAL   A CB  1 
ATOM   369  C  CG1 . VAL   A 1 48  ? -29.722 -9.069  -2.064  1.00 61.73  ? 89  VAL   A CG1 1 
ATOM   370  C  CG2 . VAL   A 1 48  ? -30.915 -11.279 -1.929  1.00 61.20  ? 89  VAL   A CG2 1 
ATOM   371  N  N   . THR   A 1 49  ? -31.250 -7.305  0.032   1.00 61.27  ? 90  THR   A N   1 
ATOM   372  C  CA  . THR   A 1 49  ? -30.758 -5.951  0.252   1.00 62.13  ? 90  THR   A CA  1 
ATOM   373  C  C   . THR   A 1 49  ? -29.272 -6.025  0.542   1.00 66.56  ? 90  THR   A C   1 
ATOM   374  O  O   . THR   A 1 49  ? -28.859 -6.753  1.453   1.00 67.78  ? 90  THR   A O   1 
ATOM   375  C  CB  . THR   A 1 49  ? -31.469 -5.256  1.407   1.00 71.88  ? 90  THR   A CB  1 
ATOM   376  O  OG1 . THR   A 1 49  ? -32.724 -4.751  0.939   1.00 70.78  ? 90  THR   A OG1 1 
ATOM   377  C  CG2 . THR   A 1 49  ? -30.601 -4.094  1.922   1.00 58.68  ? 90  THR   A CG2 1 
ATOM   378  N  N   . GLU   A 1 50  ? -28.476 -5.272  -0.220  1.00 49.07  ? 91  GLU   A N   1 
ATOM   379  C  CA  . GLU   A 1 50  ? -27.031 -5.279  -0.079  1.00 55.74  ? 91  GLU   A CA  1 
ATOM   380  C  C   . GLU   A 1 50  ? -26.558 -3.853  0.132   1.00 54.96  ? 91  GLU   A C   1 
ATOM   381  O  O   . GLU   A 1 50  ? -27.203 -2.894  -0.304  1.00 57.71  ? 91  GLU   A O   1 
ATOM   382  C  CB  . GLU   A 1 50  ? -26.342 -5.871  -1.310  1.00 49.33  ? 91  GLU   A CB  1 
ATOM   383  C  CG  . GLU   A 1 50  ? -26.027 -7.352  -1.194  1.00 65.81  ? 91  GLU   A CG  1 
ATOM   384  C  CD  . GLU   A 1 50  ? -24.846 -7.687  -0.285  1.00 68.70  ? 91  GLU   A CD  1 
ATOM   385  O  OE1 . GLU   A 1 50  ? -23.775 -7.042  -0.388  1.00 64.06  ? 91  GLU   A OE1 1 
ATOM   386  O  OE2 . GLU   A 1 50  ? -25.003 -8.613  0.548   1.00 71.45  ? 91  GLU   A OE2 1 
ATOM   387  N  N   . ASN   A 1 51  ? -25.409 -3.724  0.785   1.00 50.85  ? 92  ASN   A N   1 
ATOM   388  C  CA  . ASN   A 1 51  ? -24.820 -2.429  1.062   1.00 52.62  ? 92  ASN   A CA  1 
ATOM   389  C  C   . ASN   A 1 51  ? -23.637 -2.207  0.136   1.00 49.66  ? 92  ASN   A C   1 
ATOM   390  O  O   . ASN   A 1 51  ? -22.776 -3.078  -0.011  1.00 56.69  ? 92  ASN   A O   1 
ATOM   391  C  CB  . ASN   A 1 51  ? -24.417 -2.325  2.529   1.00 56.80  ? 92  ASN   A CB  1 
ATOM   392  C  CG  . ASN   A 1 51  ? -25.618 -2.075  3.414   1.00 73.01  ? 92  ASN   A CG  1 
ATOM   393  O  OD1 . ASN   A 1 51  ? -26.439 -2.982  3.634   1.00 68.22  ? 92  ASN   A OD1 1 
ATOM   394  N  ND2 . ASN   A 1 51  ? -25.757 -0.839  3.898   1.00 70.74  ? 92  ASN   A ND2 1 
ATOM   395  N  N   . PHE   A 1 52  ? -23.619 -1.053  -0.505  1.00 51.40  ? 93  PHE   A N   1 
ATOM   396  C  CA  . PHE   A 1 52  ? -22.565 -0.666  -1.419  1.00 53.64  ? 93  PHE   A CA  1 
ATOM   397  C  C   . PHE   A 1 52  ? -21.835 0.530   -0.833  1.00 41.38  ? 93  PHE   A C   1 
ATOM   398  O  O   . PHE   A 1 52  ? -22.333 1.213   0.068   1.00 51.38  ? 93  PHE   A O   1 
ATOM   399  C  CB  . PHE   A 1 52  ? -23.123 -0.318  -2.803  1.00 49.14  ? 93  PHE   A CB  1 
ATOM   400  C  CG  . PHE   A 1 52  ? -23.783 -1.474  -3.502  1.00 43.31  ? 93  PHE   A CG  1 
ATOM   401  C  CD1 . PHE   A 1 52  ? -24.933 -2.047  -2.993  1.00 43.29  ? 93  PHE   A CD1 1 
ATOM   402  C  CD2 . PHE   A 1 52  ? -23.275 -1.956  -4.687  1.00 42.68  ? 93  PHE   A CD2 1 
ATOM   403  C  CE1 . PHE   A 1 52  ? -25.535 -3.102  -3.635  1.00 44.44  ? 93  PHE   A CE1 1 
ATOM   404  C  CE2 . PHE   A 1 52  ? -23.873 -3.006  -5.342  1.00 43.48  ? 93  PHE   A CE2 1 
ATOM   405  C  CZ  . PHE   A 1 52  ? -25.008 -3.582  -4.813  1.00 44.06  ? 93  PHE   A CZ  1 
ATOM   406  N  N   . ASN   A 1 53  ? -20.634 0.770   -1.351  1.00 49.99  ? 94  ASN   A N   1 
ATOM   407  C  CA  . ASN   A 1 53  ? -19.834 1.922   -0.956  1.00 48.68  ? 94  ASN   A CA  1 
ATOM   408  C  C   . ASN   A 1 53  ? -18.931 2.249   -2.138  1.00 37.36  ? 94  ASN   A C   1 
ATOM   409  O  O   . ASN   A 1 53  ? -17.898 1.601   -2.327  1.00 44.66  ? 94  ASN   A O   1 
ATOM   410  C  CB  . ASN   A 1 53  ? -19.025 1.647   0.300   1.00 49.82  ? 94  ASN   A CB  1 
ATOM   411  C  CG  . ASN   A 1 53  ? -18.265 2.873   0.754   1.00 52.53  ? 94  ASN   A CG  1 
ATOM   412  O  OD1 . ASN   A 1 53  ? -18.262 3.902   0.067   1.00 45.44  ? 94  ASN   A OD1 1 
ATOM   413  N  ND2 . ASN   A 1 53  ? -17.617 2.776   1.898   1.00 63.97  ? 94  ASN   A ND2 1 
ATOM   414  N  N   . MET   A 1 54  ? -19.342 3.226   -2.941  1.00 37.80  ? 95  MET   A N   1 
ATOM   415  C  CA  . MET   A 1 54  ? -18.587 3.541   -4.144  1.00 36.75  ? 95  MET   A CA  1 
ATOM   416  C  C   . MET   A 1 54  ? -17.253 4.197   -3.830  1.00 40.62  ? 95  MET   A C   1 
ATOM   417  O  O   . MET   A 1 54  ? -16.389 4.256   -4.704  1.00 39.61  ? 95  MET   A O   1 
ATOM   418  C  CB  . MET   A 1 54  ? -19.419 4.438   -5.062  1.00 33.75  ? 95  MET   A CB  1 
ATOM   419  C  CG  . MET   A 1 54  ? -19.534 5.865   -4.542  1.00 40.99  ? 95  MET   A CG  1 
ATOM   420  S  SD  . MET   A 1 54  ? -20.663 6.910   -5.475  1.00 43.86  ? 95  MET   A SD  1 
ATOM   421  C  CE  . MET   A 1 54  ? -19.400 7.760   -6.435  1.00 33.32  ? 95  MET   A CE  1 
ATOM   422  N  N   . TRP   A 1 55  ? -17.066 4.692   -2.608  1.00 40.57  ? 96  TRP   A N   1 
ATOM   423  C  CA  . TRP   A 1 55  ? -15.828 5.372   -2.262  1.00 40.67  ? 96  TRP   A CA  1 
ATOM   424  C  C   . TRP   A 1 55  ? -14.790 4.401   -1.732  1.00 46.09  ? 96  TRP   A C   1 
ATOM   425  O  O   . TRP   A 1 55  ? -13.624 4.777   -1.592  1.00 56.98  ? 96  TRP   A O   1 
ATOM   426  C  CB  . TRP   A 1 55  ? -16.132 6.501   -1.261  1.00 41.22  ? 96  TRP   A CB  1 
ATOM   427  C  CG  . TRP   A 1 55  ? -17.190 7.427   -1.810  1.00 43.75  ? 96  TRP   A CG  1 
ATOM   428  C  CD1 . TRP   A 1 55  ? -18.544 7.405   -1.544  1.00 35.06  ? 96  TRP   A CD1 1 
ATOM   429  C  CD2 . TRP   A 1 55  ? -16.985 8.485   -2.756  1.00 39.88  ? 96  TRP   A CD2 1 
ATOM   430  N  NE1 . TRP   A 1 55  ? -19.177 8.383   -2.269  1.00 41.44  ? 96  TRP   A NE1 1 
ATOM   431  C  CE2 . TRP   A 1 55  ? -18.243 9.058   -3.020  1.00 37.17  ? 96  TRP   A CE2 1 
ATOM   432  C  CE3 . TRP   A 1 55  ? -15.854 9.004   -3.400  1.00 38.45  ? 96  TRP   A CE3 1 
ATOM   433  C  CZ2 . TRP   A 1 55  ? -18.399 10.118  -3.886  1.00 35.85  ? 96  TRP   A CZ2 1 
ATOM   434  C  CZ3 . TRP   A 1 55  ? -16.016 10.047  -4.281  1.00 39.72  ? 96  TRP   A CZ3 1 
ATOM   435  C  CH2 . TRP   A 1 55  ? -17.279 10.597  -4.518  1.00 39.39  ? 96  TRP   A CH2 1 
ATOM   436  N  N   . LYS   A 1 56  ? -15.195 3.149   -1.487  1.00 48.46  ? 97  LYS   A N   1 
ATOM   437  C  CA  . LYS   A 1 56  ? -14.349 2.101   -0.934  1.00 48.89  ? 97  LYS   A CA  1 
ATOM   438  C  C   . LYS   A 1 56  ? -14.598 0.836   -1.758  1.00 43.06  ? 97  LYS   A C   1 
ATOM   439  O  O   . LYS   A 1 56  ? -15.179 -0.158  -1.305  1.00 53.49  ? 97  LYS   A O   1 
ATOM   440  C  CB  . LYS   A 1 56  ? -14.642 1.892   0.547   1.00 48.73  ? 97  LYS   A CB  1 
ATOM   441  C  CG  . LYS   A 1 56  ? -14.438 3.151   1.404   1.00 51.55  ? 97  LYS   A CG  1 
ATOM   442  C  CD  . LYS   A 1 56  ? -12.977 3.611   1.410   1.00 55.69  ? 97  LYS   A CD  1 
ATOM   443  C  CE  . LYS   A 1 56  ? -11.995 2.479   1.116   1.00 62.72  ? 97  LYS   A CE  1 
ATOM   444  N  NZ  . LYS   A 1 56  ? -10.590 2.978   0.973   1.00 77.04  ? 97  LYS   A NZ  1 
ATOM   445  N  N   . ASN   A 1 57  ? -14.162 0.887   -3.005  1.00 45.74  ? 98  ASN   A N   1 
ATOM   446  C  CA  . ASN   A 1 57  ? -14.507 -0.109  -4.009  1.00 40.44  ? 98  ASN   A CA  1 
ATOM   447  C  C   . ASN   A 1 57  ? -13.249 -0.406  -4.793  1.00 48.56  ? 98  ASN   A C   1 
ATOM   448  O  O   . ASN   A 1 57  ? -12.801 0.427   -5.600  1.00 36.26  ? 98  ASN   A O   1 
ATOM   449  C  CB  . ASN   A 1 57  ? -15.605 0.405   -4.937  1.00 38.91  ? 98  ASN   A CB  1 
ATOM   450  C  CG  . ASN   A 1 57  ? -16.011 -0.612  -5.996  1.00 44.95  ? 98  ASN   A CG  1 
ATOM   451  O  OD1 . ASN   A 1 57  ? -15.415 -1.691  -6.117  1.00 40.90  ? 98  ASN   A OD1 1 
ATOM   452  N  ND2 . ASN   A 1 57  ? -16.984 -0.238  -6.817  1.00 35.56  ? 98  ASN   A ND2 1 
ATOM   453  N  N   . ASN   A 1 58  ? -12.692 -1.594  -4.544  1.00 39.76  ? 99  ASN   A N   1 
ATOM   454  C  CA  . ASN   A 1 58  ? -11.425 -1.977  -5.142  1.00 35.41  ? 99  ASN   A CA  1 
ATOM   455  C  C   . ASN   A 1 58  ? -11.499 -2.058  -6.663  1.00 42.21  ? 99  ASN   A C   1 
ATOM   456  O  O   . ASN   A 1 58  ? -10.451 -2.024  -7.329  1.00 40.79  ? 99  ASN   A O   1 
ATOM   457  C  CB  . ASN   A 1 58  ? -10.962 -3.313  -4.541  1.00 40.75  ? 99  ASN   A CB  1 
ATOM   458  C  CG  . ASN   A 1 58  ? -9.616  -3.742  -5.071  1.00 55.12  ? 99  ASN   A CG  1 
ATOM   459  O  OD1 . ASN   A 1 58  ? -9.509  -4.733  -5.779  1.00 44.38  ? 99  ASN   A OD1 1 
ATOM   460  N  ND2 . ASN   A 1 58  ? -8.587  -2.937  -4.799  1.00 56.74  ? 99  ASN   A ND2 1 
ATOM   461  N  N   . MET   A 1 59  ? -12.705 -2.162  -7.244  1.00 40.59  ? 100 MET   A N   1 
ATOM   462  C  CA  . MET   A 1 59  ? -12.780 -2.163  -8.700  1.00 37.47  ? 100 MET   A CA  1 
ATOM   463  C  C   . MET   A 1 59  ? -12.240 -0.861  -9.267  1.00 36.67  ? 100 MET   A C   1 
ATOM   464  O  O   . MET   A 1 59  ? -11.602 -0.854  -10.325 1.00 34.92  ? 100 MET   A O   1 
ATOM   465  C  CB  . MET   A 1 59  ? -14.208 -2.378  -9.156  1.00 42.49  ? 100 MET   A CB  1 
ATOM   466  C  CG  . MET   A 1 59  ? -14.861 -3.642  -8.635  1.00 47.20  ? 100 MET   A CG  1 
ATOM   467  S  SD  . MET   A 1 59  ? -16.600 -3.655  -9.152  1.00 50.67  ? 100 MET   A SD  1 
ATOM   468  C  CE  . MET   A 1 59  ? -16.420 -4.081  -10.881 1.00 39.34  ? 100 MET   A CE  1 
ATOM   469  N  N   . VAL   A 1 60  ? -12.489 0.257   -8.581  1.00 39.87  ? 101 VAL   A N   1 
ATOM   470  C  CA  . VAL   A 1 60  ? -11.978 1.534   -9.068  1.00 41.74  ? 101 VAL   A CA  1 
ATOM   471  C  C   . VAL   A 1 60  ? -10.462 1.484   -9.171  1.00 41.51  ? 101 VAL   A C   1 
ATOM   472  O  O   . VAL   A 1 60  ? -9.879  1.880   -10.188 1.00 33.90  ? 101 VAL   A O   1 
ATOM   473  C  CB  . VAL   A 1 60  ? -12.435 2.684   -8.155  1.00 40.86  ? 101 VAL   A CB  1 
ATOM   474  C  CG1 . VAL   A 1 60  ? -11.634 3.919   -8.449  1.00 36.68  ? 101 VAL   A CG1 1 
ATOM   475  C  CG2 . VAL   A 1 60  ? -13.926 2.933   -8.334  1.00 35.38  ? 101 VAL   A CG2 1 
ATOM   476  N  N   . GLU   A 1 61  ? -9.806  0.956   -8.119  1.00 49.06  ? 102 GLU   A N   1 
ATOM   477  C  CA  . GLU   A 1 61  ? -8.347  0.910   -8.088  1.00 39.24  ? 102 GLU   A CA  1 
ATOM   478  C  C   . GLU   A 1 61  ? -7.796  0.085   -9.248  1.00 38.30  ? 102 GLU   A C   1 
ATOM   479  O  O   . GLU   A 1 61  ? -6.778  0.452   -9.850  1.00 45.30  ? 102 GLU   A O   1 
ATOM   480  C  CB  . GLU   A 1 61  ? -7.887  0.378   -6.729  1.00 45.59  ? 102 GLU   A CB  1 
ATOM   481  C  CG  . GLU   A 1 61  ? -7.457  1.453   -5.739  1.00 59.80  ? 102 GLU   A CG  1 
ATOM   482  C  CD  . GLU   A 1 61  ? -8.599  2.377   -5.320  1.00 69.39  ? 102 GLU   A CD  1 
ATOM   483  O  OE1 . GLU   A 1 61  ? -9.770  1.965   -5.467  1.00 69.09  ? 102 GLU   A OE1 1 
ATOM   484  O  OE2 . GLU   A 1 61  ? -8.336  3.522   -4.855  1.00 63.26  ? 102 GLU   A OE2 1 
ATOM   485  N  N   . GLN   A 1 62  ? -8.494  -1.005  -9.617  1.00 43.18  ? 103 GLN   A N   1 
ATOM   486  C  CA  . GLN   A 1 62  ? -8.033  -1.879  -10.691 1.00 32.53  ? 103 GLN   A CA  1 
ATOM   487  C  C   . GLN   A 1 62  ? -8.206  -1.243  -12.060 1.00 36.76  ? 103 GLN   A C   1 
ATOM   488  O  O   . GLN   A 1 62  ? -7.345  -1.406  -12.938 1.00 42.51  ? 103 GLN   A O   1 
ATOM   489  C  CB  . GLN   A 1 62  ? -8.791  -3.196  -10.616 1.00 47.58  ? 103 GLN   A CB  1 
ATOM   490  C  CG  . GLN   A 1 62  ? -8.295  -4.134  -9.549  1.00 47.47  ? 103 GLN   A CG  1 
ATOM   491  C  CD  . GLN   A 1 62  ? -8.998  -5.465  -9.625  1.00 50.50  ? 103 GLN   A CD  1 
ATOM   492  O  OE1 . GLN   A 1 62  ? -8.780  -6.233  -10.566 1.00 49.05  ? 103 GLN   A OE1 1 
ATOM   493  N  NE2 . GLN   A 1 62  ? -9.816  -5.767  -8.621  1.00 42.32  ? 103 GLN   A NE2 1 
ATOM   494  N  N   . MET   A 1 63  ? -9.329  -0.556  -12.283 1.00 37.82  ? 104 MET   A N   1 
ATOM   495  C  CA  . MET   A 1 63  ? -9.495  0.177   -13.533 1.00 42.82  ? 104 MET   A CA  1 
ATOM   496  C  C   . MET   A 1 63  ? -8.426  1.251   -13.683 1.00 38.59  ? 104 MET   A C   1 
ATOM   497  O  O   . MET   A 1 63  ? -7.904  1.470   -14.785 1.00 37.38  ? 104 MET   A O   1 
ATOM   498  C  CB  . MET   A 1 63  ? -10.887 0.796   -13.606 1.00 30.84  ? 104 MET   A CB  1 
ATOM   499  C  CG  . MET   A 1 63  ? -11.095 1.581   -14.893 1.00 36.18  ? 104 MET   A CG  1 
ATOM   500  S  SD  . MET   A 1 63  ? -12.833 1.980   -15.180 1.00 45.41  ? 104 MET   A SD  1 
ATOM   501  C  CE  . MET   A 1 63  ? -12.721 2.727   -16.820 1.00 50.29  ? 104 MET   A CE  1 
ATOM   502  N  N   . HIS   A 1 64  ? -8.096  1.930   -12.583 1.00 38.64  ? 105 HIS   A N   1 
ATOM   503  C  CA  . HIS   A 1 64  ? -7.084  2.977   -12.633 1.00 37.16  ? 105 HIS   A CA  1 
ATOM   504  C  C   . HIS   A 1 64  ? -5.772  2.430   -13.179 1.00 47.44  ? 105 HIS   A C   1 
ATOM   505  O  O   . HIS   A 1 64  ? -5.146  3.038   -14.066 1.00 44.16  ? 105 HIS   A O   1 
ATOM   506  C  CB  . HIS   A 1 64  ? -6.911  3.548   -11.237 1.00 40.19  ? 105 HIS   A CB  1 
ATOM   507  C  CG  . HIS   A 1 64  ? -6.261  4.890   -11.190 1.00 50.23  ? 105 HIS   A CG  1 
ATOM   508  N  ND1 . HIS   A 1 64  ? -6.533  5.884   -12.101 1.00 43.13  ? 105 HIS   A ND1 1 
ATOM   509  C  CD2 . HIS   A 1 64  ? -5.367  5.410   -10.317 1.00 44.60  ? 105 HIS   A CD2 1 
ATOM   510  C  CE1 . HIS   A 1 64  ? -5.821  6.954   -11.799 1.00 48.18  ? 105 HIS   A CE1 1 
ATOM   511  N  NE2 . HIS   A 1 64  ? -5.107  6.692   -10.720 1.00 40.66  ? 105 HIS   A NE2 1 
ATOM   512  N  N   . GLU   A 1 65  ? -5.369  1.247   -12.687 1.00 41.72  ? 106 GLU   A N   1 
ATOM   513  C  CA  . GLU   A 1 65  ? -4.131  0.617   -13.137 1.00 40.24  ? 106 GLU   A CA  1 
ATOM   514  C  C   . GLU   A 1 65  ? -4.198  0.249   -14.607 1.00 43.20  ? 106 GLU   A C   1 
ATOM   515  O  O   . GLU   A 1 65  ? -3.205  0.401   -15.333 1.00 49.14  ? 106 GLU   A O   1 
ATOM   516  C  CB  . GLU   A 1 65  ? -3.847  -0.623  -12.292 1.00 48.81  ? 106 GLU   A CB  1 
ATOM   517  C  CG  . GLU   A 1 65  ? -2.375  -1.021  -12.189 1.00 61.70  ? 106 GLU   A CG  1 
ATOM   518  C  CD  . GLU   A 1 65  ? -2.030  -1.685  -10.847 1.00 87.18  ? 106 GLU   A CD  1 
ATOM   519  O  OE1 . GLU   A 1 65  ? -1.061  -2.491  -10.804 1.00 85.98  ? 106 GLU   A OE1 1 
ATOM   520  O  OE2 . GLU   A 1 65  ? -2.724  -1.401  -9.836  1.00 88.38  ? 106 GLU   A OE2 1 
ATOM   521  N  N   . ASP   A 1 66  ? -5.358  -0.223  -15.072 1.00 38.77  ? 107 ASP   A N   1 
ATOM   522  C  CA  . ASP   A 1 66  ? -5.493  -0.533  -16.492 1.00 41.67  ? 107 ASP   A CA  1 
ATOM   523  C  C   . ASP   A 1 66  ? -5.269  0.717   -17.326 1.00 39.61  ? 107 ASP   A C   1 
ATOM   524  O  O   . ASP   A 1 66  ? -4.455  0.720   -18.256 1.00 48.93  ? 107 ASP   A O   1 
ATOM   525  C  CB  . ASP   A 1 66  ? -6.867  -1.137  -16.775 1.00 39.08  ? 107 ASP   A CB  1 
ATOM   526  C  CG  . ASP   A 1 66  ? -6.972  -2.584  -16.307 1.00 47.29  ? 107 ASP   A CG  1 
ATOM   527  O  OD1 . ASP   A 1 66  ? -5.941  -3.133  -15.860 1.00 56.84  ? 107 ASP   A OD1 1 
ATOM   528  O  OD2 . ASP   A 1 66  ? -8.089  -3.161  -16.349 1.00 48.14  ? 107 ASP   A OD2 1 
ATOM   529  N  N   . ILE   A 1 67  ? -5.958  1.808   -16.982 1.00 45.55  ? 108 ILE   A N   1 
ATOM   530  C  CA  . ILE   A 1 67  ? -5.889  3.007   -17.808 1.00 42.65  ? 108 ILE   A CA  1 
ATOM   531  C  C   . ILE   A 1 67  ? -4.482  3.599   -17.763 1.00 34.57  ? 108 ILE   A C   1 
ATOM   532  O  O   . ILE   A 1 67  ? -3.937  4.005   -18.791 1.00 43.93  ? 108 ILE   A O   1 
ATOM   533  C  CB  . ILE   A 1 67  ? -6.987  4.008   -17.379 1.00 50.19  ? 108 ILE   A CB  1 
ATOM   534  C  CG1 . ILE   A 1 67  ? -8.387  3.334   -17.374 1.00 37.30  ? 108 ILE   A CG1 1 
ATOM   535  C  CG2 . ILE   A 1 67  ? -7.011  5.233   -18.279 1.00 40.62  ? 108 ILE   A CG2 1 
ATOM   536  C  CD1 . ILE   A 1 67  ? -8.626  2.339   -18.546 1.00 38.76  ? 108 ILE   A CD1 1 
ATOM   537  N  N   . ILE   A 1 68  ? -3.849  3.590   -16.595 1.00 34.33  ? 109 ILE   A N   1 
ATOM   538  C  CA  . ILE   A 1 68  ? -2.441  3.973   -16.516 1.00 45.37  ? 109 ILE   A CA  1 
ATOM   539  C  C   . ILE   A 1 68  ? -1.621  3.180   -17.521 1.00 51.78  ? 109 ILE   A C   1 
ATOM   540  O  O   . ILE   A 1 68  ? -0.888  3.747   -18.344 1.00 53.49  ? 109 ILE   A O   1 
ATOM   541  C  CB  . ILE   A 1 68  ? -1.916  3.766   -15.087 1.00 44.00  ? 109 ILE   A CB  1 
ATOM   542  C  CG1 . ILE   A 1 68  ? -2.579  4.772   -14.137 1.00 43.41  ? 109 ILE   A CG1 1 
ATOM   543  C  CG2 . ILE   A 1 68  ? -0.396  3.833   -15.075 1.00 50.48  ? 109 ILE   A CG2 1 
ATOM   544  C  CD1 . ILE   A 1 68  ? -1.789  5.073   -12.929 1.00 56.72  ? 109 ILE   A CD1 1 
ATOM   545  N  N   . SER   A 1 69  ? -1.754  1.847   -17.478 1.00 52.22  ? 110 SER   A N   1 
ATOM   546  C  CA  . SER   A 1 69  ? -1.005  0.984   -18.383 1.00 43.24  ? 110 SER   A CA  1 
ATOM   547  C  C   . SER   A 1 69  ? -1.346  1.279   -19.826 1.00 47.62  ? 110 SER   A C   1 
ATOM   548  O  O   . SER   A 1 69  ? -0.442  1.399   -20.659 1.00 51.35  ? 110 SER   A O   1 
ATOM   549  C  CB  . SER   A 1 69  ? -1.267  -0.485  -18.059 1.00 44.40  ? 110 SER   A CB  1 
ATOM   550  O  OG  . SER   A 1 69  ? -0.638  -1.309  -19.012 1.00 51.66  ? 110 SER   A OG  1 
ATOM   551  N  N   . LEU   A 1 70  ? -2.644  1.399   -20.139 1.00 46.44  ? 111 LEU   A N   1 
ATOM   552  C  CA  . LEU   A 1 70  ? -3.069  1.804   -21.475 1.00 44.70  ? 111 LEU   A CA  1 
ATOM   553  C  C   . LEU   A 1 70  ? -2.343  3.073   -21.925 1.00 49.89  ? 111 LEU   A C   1 
ATOM   554  O  O   . LEU   A 1 70  ? -1.730  3.097   -22.999 1.00 52.71  ? 111 LEU   A O   1 
ATOM   555  C  CB  . LEU   A 1 70  ? -4.589  1.996   -21.484 1.00 45.64  ? 111 LEU   A CB  1 
ATOM   556  C  CG  . LEU   A 1 70  ? -5.410  2.100   -22.775 1.00 43.40  ? 111 LEU   A CG  1 
ATOM   557  C  CD1 . LEU   A 1 70  ? -6.858  1.638   -22.558 1.00 39.93  ? 111 LEU   A CD1 1 
ATOM   558  C  CD2 . LEU   A 1 70  ? -5.397  3.530   -23.255 1.00 47.64  ? 111 LEU   A CD2 1 
ATOM   559  N  N   . TRP   A 1 71  ? -2.393  4.140   -21.108 1.00 50.57  ? 112 TRP   A N   1 
ATOM   560  C  CA  . TRP   A 1 71  ? -1.763  5.399   -21.518 1.00 56.94  ? 112 TRP   A CA  1 
ATOM   561  C  C   . TRP   A 1 71  ? -0.248  5.234   -21.681 1.00 48.82  ? 112 TRP   A C   1 
ATOM   562  O  O   . TRP   A 1 71  ? 0.328   5.746   -22.646 1.00 52.38  ? 112 TRP   A O   1 
ATOM   563  C  CB  . TRP   A 1 71  ? -2.125  6.530   -20.530 1.00 52.26  ? 112 TRP   A CB  1 
ATOM   564  C  CG  . TRP   A 1 71  ? -3.440  7.176   -20.872 1.00 51.34  ? 112 TRP   A CG  1 
ATOM   565  C  CD1 . TRP   A 1 71  ? -4.605  6.525   -21.094 1.00 44.99  ? 112 TRP   A CD1 1 
ATOM   566  C  CD2 . TRP   A 1 71  ? -3.727  8.583   -21.045 1.00 50.37  ? 112 TRP   A CD2 1 
ATOM   567  N  NE1 . TRP   A 1 71  ? -5.602  7.419   -21.406 1.00 48.87  ? 112 TRP   A NE1 1 
ATOM   568  C  CE2 . TRP   A 1 71  ? -5.084  8.689   -21.384 1.00 56.13  ? 112 TRP   A CE2 1 
ATOM   569  C  CE3 . TRP   A 1 71  ? -2.979  9.758   -20.911 1.00 57.85  ? 112 TRP   A CE3 1 
ATOM   570  C  CZ2 . TRP   A 1 71  ? -5.709  9.922   -21.616 1.00 45.64  ? 112 TRP   A CZ2 1 
ATOM   571  C  CZ3 . TRP   A 1 71  ? -3.591  10.988  -21.189 1.00 54.01  ? 112 TRP   A CZ3 1 
ATOM   572  C  CH2 . TRP   A 1 71  ? -4.951  11.055  -21.518 1.00 44.11  ? 112 TRP   A CH2 1 
ATOM   573  N  N   . ASP   A 1 72  ? 0.402   4.469   -20.787 1.00 59.38  ? 113 ASP   A N   1 
ATOM   574  C  CA  . ASP   A 1 72  ? 1.858   4.300   -20.819 1.00 56.16  ? 113 ASP   A CA  1 
ATOM   575  C  C   . ASP   A 1 72  ? 2.358   3.608   -22.098 1.00 71.71  ? 113 ASP   A C   1 
ATOM   576  O  O   . ASP   A 1 72  ? 3.503   3.826   -22.512 1.00 70.64  ? 113 ASP   A O   1 
ATOM   577  C  CB  . ASP   A 1 72  ? 2.283   3.523   -19.576 1.00 60.28  ? 113 ASP   A CB  1 
ATOM   578  C  CG  . ASP   A 1 72  ? 3.769   3.611   -19.295 1.00 83.20  ? 113 ASP   A CG  1 
ATOM   579  O  OD1 . ASP   A 1 72  ? 4.488   4.276   -20.071 1.00 87.37  ? 113 ASP   A OD1 1 
ATOM   580  O  OD2 . ASP   A 1 72  ? 4.212   3.028   -18.278 1.00 91.97  ? 113 ASP   A OD2 1 
ATOM   581  N  N   . GLN   A 1 73  ? 1.541   2.769   -22.739 1.00 69.13  ? 114 GLN   A N   1 
ATOM   582  C  CA  . GLN   A 1 73  ? 1.947   2.081   -23.957 1.00 57.48  ? 114 GLN   A CA  1 
ATOM   583  C  C   . GLN   A 1 73  ? 1.352   2.697   -25.205 1.00 54.32  ? 114 GLN   A C   1 
ATOM   584  O  O   . GLN   A 1 73  ? 1.548   2.161   -26.294 1.00 62.95  ? 114 GLN   A O   1 
ATOM   585  C  CB  . GLN   A 1 73  ? 1.547   0.607   -23.898 1.00 62.93  ? 114 GLN   A CB  1 
ATOM   586  C  CG  . GLN   A 1 73  ? 1.495   -0.018  -22.527 1.00 58.41  ? 114 GLN   A CG  1 
ATOM   587  C  CD  . GLN   A 1 73  ? 0.895   -1.403  -22.596 1.00 69.23  ? 114 GLN   A CD  1 
ATOM   588  O  OE1 . GLN   A 1 73  ? 0.239   -1.742  -23.587 1.00 69.26  ? 114 GLN   A OE1 1 
ATOM   589  N  NE2 . GLN   A 1 73  ? 1.070   -2.199  -21.533 1.00 68.79  ? 114 GLN   A NE2 1 
ATOM   590  N  N   . SER   A 1 74  ? 0.613   3.791   -25.081 1.00 52.65  ? 115 SER   A N   1 
ATOM   591  C  CA  . SER   A 1 74  ? -0.101  4.332   -26.225 1.00 52.58  ? 115 SER   A CA  1 
ATOM   592  C  C   . SER   A 1 74  ? 0.280   5.773   -26.509 1.00 59.72  ? 115 SER   A C   1 
ATOM   593  O  O   . SER   A 1 74  ? 0.719   6.078   -27.623 1.00 63.27  ? 115 SER   A O   1 
ATOM   594  C  CB  . SER   A 1 74  ? -1.603  4.158   -25.994 1.00 60.07  ? 115 SER   A CB  1 
ATOM   595  O  OG  . SER   A 1 74  ? -1.838  2.913   -25.343 1.00 56.51  ? 115 SER   A OG  1 
ATOM   596  N  N   . LEU   A 1 75  ? 0.110   6.654   -25.533 1.00 65.25  ? 116 LEU   A N   1 
ATOM   597  C  CA  . LEU   A 1 75  ? 0.542   8.051   -25.755 1.00 64.34  ? 116 LEU   A CA  1 
ATOM   598  C  C   . LEU   A 1 75  ? 1.966   8.162   -25.243 1.00 72.51  ? 116 LEU   A C   1 
ATOM   599  O  O   . LEU   A 1 75  ? 2.160   8.498   -24.092 1.00 82.70  ? 116 LEU   A O   1 
ATOM   600  C  CB  . LEU   A 1 75  ? -0.349  9.035   -24.998 1.00 61.15  ? 116 LEU   A CB  1 
ATOM   601  C  CG  . LEU   A 1 75  ? -0.879  8.551   -23.657 1.00 62.99  ? 116 LEU   A CG  1 
ATOM   602  C  CD1 . LEU   A 1 75  ? 0.031   8.963   -22.520 1.00 66.11  ? 116 LEU   A CD1 1 
ATOM   603  C  CD2 . LEU   A 1 75  ? -2.277  9.094   -23.418 1.00 83.32  ? 116 LEU   A CD2 1 
ATOM   604  N  N   . GLN   A 1 76  ? 2.942   7.822   -26.052 1.00 65.08  ? 117 GLN   A N   1 
ATOM   605  C  CA  . GLN   A 1 76  ? 4.252   8.035   -25.483 1.00 82.77  ? 117 GLN   A CA  1 
ATOM   606  C  C   . GLN   A 1 76  ? 4.692   9.476   -25.747 1.00 80.62  ? 117 GLN   A C   1 
ATOM   607  O  O   . GLN   A 1 76  ? 4.526   9.976   -26.862 1.00 69.89  ? 117 GLN   A O   1 
ATOM   608  C  CB  . GLN   A 1 76  ? 5.226   7.016   -26.015 1.00 83.84  ? 117 GLN   A CB  1 
ATOM   609  C  CG  . GLN   A 1 76  ? 5.449   5.882   -25.017 1.00 85.44  ? 117 GLN   A CG  1 
ATOM   610  C  CD  . GLN   A 1 76  ? 5.609   6.345   -23.540 1.00 94.39  ? 117 GLN   A CD  1 
ATOM   611  O  OE1 . GLN   A 1 76  ? 4.645   6.389   -22.763 1.00 89.59  ? 117 GLN   A OE1 1 
ATOM   612  N  NE2 . GLN   A 1 76  ? 6.843   6.679   -23.160 1.00 88.99  ? 117 GLN   A NE2 1 
ATOM   613  N  N   . PRO   A 1 77  ? 5.172   10.190  -24.736 1.00 72.20  ? 118 PRO   A N   1 
ATOM   614  C  CA  . PRO   A 1 77  ? 5.514   11.602  -24.918 1.00 77.88  ? 118 PRO   A CA  1 
ATOM   615  C  C   . PRO   A 1 77  ? 6.936   11.785  -25.419 1.00 70.97  ? 118 PRO   A C   1 
ATOM   616  O  O   . PRO   A 1 77  ? 7.820   10.969  -25.156 1.00 80.14  ? 118 PRO   A O   1 
ATOM   617  C  CB  . PRO   A 1 77  ? 5.349   12.151  -23.495 1.00 71.91  ? 118 PRO   A CB  1 
ATOM   618  C  CG  . PRO   A 1 77  ? 5.860   11.032  -22.655 1.00 72.49  ? 118 PRO   A CG  1 
ATOM   619  C  CD  . PRO   A 1 77  ? 5.357   9.773   -23.334 1.00 76.76  ? 118 PRO   A CD  1 
ATOM   620  N  N   . CYS   A 1 78  ? 7.147   12.875  -26.175 1.00 66.96  ? 119 CYS   A N   1 
ATOM   621  C  CA  . CYS   A 1 78  ? 8.480   13.159  -26.706 1.00 69.39  ? 119 CYS   A CA  1 
ATOM   622  C  C   . CYS   A 1 78  ? 9.527   13.225  -25.607 1.00 76.54  ? 119 CYS   A C   1 
ATOM   623  O  O   . CYS   A 1 78  ? 10.677  12.824  -25.826 1.00 69.27  ? 119 CYS   A O   1 
ATOM   624  C  CB  . CYS   A 1 78  ? 8.493   14.467  -27.486 1.00 76.91  ? 119 CYS   A CB  1 
ATOM   625  S  SG  . CYS   A 1 78  ? 7.225   14.632  -28.736 1.00 105.41 ? 119 CYS   A SG  1 
ATOM   626  N  N   . VAL   A 1 79  ? 9.164   13.747  -24.431 1.00 74.07  ? 120 VAL   A N   1 
ATOM   627  C  CA  . VAL   A 1 79  ? 10.088  13.841  -23.303 1.00 72.72  ? 120 VAL   A CA  1 
ATOM   628  C  C   . VAL   A 1 79  ? 9.322   13.774  -21.994 1.00 64.17  ? 120 VAL   A C   1 
ATOM   629  O  O   . VAL   A 1 79  ? 8.422   14.584  -21.745 1.00 67.00  ? 120 VAL   A O   1 
ATOM   630  C  CB  . VAL   A 1 79  ? 10.913  15.140  -23.333 1.00 74.97  ? 120 VAL   A CB  1 
ATOM   631  C  CG1 . VAL   A 1 79  ? 12.068  15.046  -22.347 1.00 70.97  ? 120 VAL   A CG1 1 
ATOM   632  C  CG2 . VAL   A 1 79  ? 11.394  15.462  -24.747 1.00 73.06  ? 120 VAL   A CG2 1 
ATOM   633  N  N   . LYS   A 1 80  ? 9.702   12.836  -21.138 1.00 67.39  ? 121 LYS   A N   1 
ATOM   634  C  CA  . LYS   A 1 80  ? 9.125   12.696  -19.810 1.00 76.04  ? 121 LYS   A CA  1 
ATOM   635  C  C   . LYS   A 1 80  ? 10.126  13.245  -18.801 1.00 74.50  ? 121 LYS   A C   1 
ATOM   636  O  O   . LYS   A 1 80  ? 11.305  12.887  -18.834 1.00 80.88  ? 121 LYS   A O   1 
ATOM   637  C  CB  . LYS   A 1 80  ? 8.789   11.229  -19.503 1.00 72.61  ? 121 LYS   A CB  1 
ATOM   638  C  CG  . LYS   A 1 80  ? 7.440   11.030  -18.815 1.00 76.45  ? 121 LYS   A CG  1 
ATOM   639  C  CD  . LYS   A 1 80  ? 7.136   9.555   -18.494 1.00 83.01  ? 121 LYS   A CD  1 
ATOM   640  C  CE  . LYS   A 1 80  ? 5.822   9.079   -19.152 1.00 95.08  ? 121 LYS   A CE  1 
ATOM   641  N  NZ  . LYS   A 1 80  ? 5.533   7.597   -19.043 1.00 79.93  ? 121 LYS   A NZ  1 
ATOM   642  N  N   . LEU   A 1 81  ? 9.672   14.131  -17.926 1.00 68.88  ? 122 LEU   A N   1 
ATOM   643  C  CA  . LEU   A 1 81  ? 10.512  14.712  -16.884 1.00 74.93  ? 122 LEU   A CA  1 
ATOM   644  C  C   . LEU   A 1 81  ? 10.006  14.201  -15.534 1.00 82.84  ? 122 LEU   A C   1 
ATOM   645  O  O   . LEU   A 1 81  ? 8.882   14.535  -15.136 1.00 85.72  ? 122 LEU   A O   1 
ATOM   646  C  CB  . LEU   A 1 81  ? 10.470  16.247  -16.970 1.00 73.75  ? 122 LEU   A CB  1 
ATOM   647  C  CG  . LEU   A 1 81  ? 11.105  16.839  -18.239 1.00 70.75  ? 122 LEU   A CG  1 
ATOM   648  C  CD1 . LEU   A 1 81  ? 10.072  17.558  -19.088 1.00 79.57  ? 122 LEU   A CD1 1 
ATOM   649  C  CD2 . LEU   A 1 81  ? 12.244  17.784  -17.913 1.00 65.90  ? 122 LEU   A CD2 1 
ATOM   650  N  N   . THR   A 1 82  ? 10.826  13.399  -14.834 1.00 88.16  ? 123 THR   A N   1 
ATOM   651  C  CA  . THR   A 1 82  ? 10.363  12.688  -13.646 1.00 95.95  ? 123 THR   A CA  1 
ATOM   652  C  C   . THR   A 1 82  ? 11.487  12.601  -12.621 1.00 98.35  ? 123 THR   A C   1 
ATOM   653  O  O   . THR   A 1 82  ? 12.610  12.212  -12.973 1.00 94.67  ? 123 THR   A O   1 
ATOM   654  C  CB  . THR   A 1 82  ? 9.863   11.283  -14.020 1.00 98.45  ? 123 THR   A CB  1 
ATOM   655  O  OG1 . THR   A 1 82  ? 10.897  10.560  -14.724 1.00 96.81  ? 123 THR   A OG1 1 
ATOM   656  C  CG2 . THR   A 1 82  ? 8.596   11.325  -14.904 1.00 83.05  ? 123 THR   A CG2 1 
ATOM   657  N  N   . GLY   A 1 83  ? 11.195  12.970  -11.355 1.00 105.06 ? 124 GLY   A N   1 
ATOM   658  C  CA  . GLY   A 1 83  ? 12.168  12.800  -10.259 1.00 92.75  ? 124 GLY   A CA  1 
ATOM   659  C  C   . GLY   A 1 83  ? 13.650  13.014  -10.610 1.00 99.87  ? 124 GLY   A C   1 
ATOM   660  O  O   . GLY   A 1 83  ? 14.480  12.135  -10.327 1.00 99.76  ? 124 GLY   A O   1 
ATOM   661  N  N   . GLY   A 1 84  ? 14.003  14.167  -11.218 1.00 97.93  ? 198 GLY   A N   1 
ATOM   662  C  CA  . GLY   A 1 84  ? 15.374  14.485  -11.584 1.00 98.79  ? 198 GLY   A CA  1 
ATOM   663  C  C   . GLY   A 1 84  ? 15.860  13.919  -12.900 1.00 104.34 ? 198 GLY   A C   1 
ATOM   664  O  O   . GLY   A 1 84  ? 16.828  14.449  -13.456 1.00 102.34 ? 198 GLY   A O   1 
ATOM   665  N  N   . SER   A 1 85  ? 15.226  12.868  -13.418 1.00 99.48  ? 199 SER   A N   1 
ATOM   666  C  CA  . SER   A 1 85  ? 15.652  12.211  -14.643 1.00 91.21  ? 199 SER   A CA  1 
ATOM   667  C  C   . SER   A 1 85  ? 14.781  12.671  -15.809 1.00 94.74  ? 199 SER   A C   1 
ATOM   668  O  O   . SER   A 1 85  ? 13.583  12.922  -15.644 1.00 95.65  ? 199 SER   A O   1 
ATOM   669  C  CB  . SER   A 1 85  ? 15.565  10.697  -14.466 1.00 88.04  ? 199 SER   A CB  1 
ATOM   670  O  OG  . SER   A 1 85  ? 16.809  10.077  -14.729 1.00 93.31  ? 199 SER   A OG  1 
ATOM   671  N  N   . VAL   A 1 86  ? 15.385  12.800  -16.986 1.00 85.09  ? 200 VAL   A N   1 
ATOM   672  C  CA  . VAL   A 1 86  ? 14.654  13.127  -18.203 1.00 86.99  ? 200 VAL   A CA  1 
ATOM   673  C  C   . VAL   A 1 86  ? 14.911  12.030  -19.220 1.00 89.65  ? 200 VAL   A C   1 
ATOM   674  O  O   . VAL   A 1 86  ? 16.035  11.531  -19.337 1.00 91.04  ? 200 VAL   A O   1 
ATOM   675  C  CB  . VAL   A 1 86  ? 15.058  14.496  -18.786 1.00 83.95  ? 200 VAL   A CB  1 
ATOM   676  C  CG1 . VAL   A 1 86  ? 15.444  15.449  -17.674 1.00 81.49  ? 200 VAL   A CG1 1 
ATOM   677  C  CG2 . VAL   A 1 86  ? 16.174  14.352  -19.843 1.00 88.63  ? 200 VAL   A CG2 1 
ATOM   678  N  N   . ILE   A 1 87  ? 13.870  11.657  -19.958 1.00 77.90  ? 201 ILE   A N   1 
ATOM   679  C  CA  . ILE   A 1 87  ? 13.925  10.573  -20.931 1.00 79.35  ? 201 ILE   A CA  1 
ATOM   680  C  C   . ILE   A 1 87  ? 13.288  11.069  -22.220 1.00 81.56  ? 201 ILE   A C   1 
ATOM   681  O  O   . ILE   A 1 87  ? 12.129  11.495  -22.217 1.00 80.87  ? 201 ILE   A O   1 
ATOM   682  C  CB  . ILE   A 1 87  ? 13.210  9.305   -20.419 1.00 87.11  ? 201 ILE   A CB  1 
ATOM   683  C  CG1 . ILE   A 1 87  ? 13.610  8.091   -21.258 1.00 85.81  ? 201 ILE   A CG1 1 
ATOM   684  C  CG2 . ILE   A 1 87  ? 11.690  9.486   -20.375 1.00 85.77  ? 201 ILE   A CG2 1 
ATOM   685  C  CD1 . ILE   A 1 87  ? 14.968  8.238   -21.914 1.00 81.88  ? 201 ILE   A CD1 1 
ATOM   686  N  N   . LYS   A 1 88  ? 14.046  11.058  -23.311 1.00 78.61  ? 202 LYS   A N   1 
ATOM   687  C  CA  . LYS   A 1 88  ? 13.511  11.408  -24.619 1.00 84.28  ? 202 LYS   A CA  1 
ATOM   688  C  C   . LYS   A 1 88  ? 13.166  10.103  -25.331 1.00 90.31  ? 202 LYS   A C   1 
ATOM   689  O  O   . LYS   A 1 88  ? 13.985  9.181   -25.373 1.00 92.92  ? 202 LYS   A O   1 
ATOM   690  C  CB  . LYS   A 1 88  ? 14.488  12.297  -25.413 1.00 86.17  ? 202 LYS   A CB  1 
ATOM   691  C  CG  . LYS   A 1 88  ? 15.957  11.837  -25.568 1.00 84.44  ? 202 LYS   A CG  1 
ATOM   692  C  CD  . LYS   A 1 88  ? 16.076  10.540  -26.357 1.00 92.91  ? 202 LYS   A CD  1 
ATOM   693  C  CE  . LYS   A 1 88  ? 17.468  10.286  -26.926 1.00 95.10  ? 202 LYS   A CE  1 
ATOM   694  N  NZ  . LYS   A 1 88  ? 17.353  9.363   -28.103 1.00 87.64  ? 202 LYS   A NZ  1 
ATOM   695  N  N   . GLN   A 1 89  ? 11.920  9.982   -25.793 1.00 89.73  ? 203 GLN   A N   1 
ATOM   696  C  CA  . GLN   A 1 89  ? 11.457  8.755   -26.434 1.00 82.58  ? 203 GLN   A CA  1 
ATOM   697  C  C   . GLN   A 1 89  ? 11.056  9.078   -27.864 1.00 87.76  ? 203 GLN   A C   1 
ATOM   698  O  O   . GLN   A 1 89  ? 11.483  10.100  -28.407 1.00 84.09  ? 203 GLN   A O   1 
ATOM   699  C  CB  . GLN   A 1 89  ? 10.291  8.142   -25.644 1.00 76.03  ? 203 GLN   A CB  1 
ATOM   700  C  CG  . GLN   A 1 89  ? 10.035  6.640   -25.863 1.00 85.57  ? 203 GLN   A CG  1 
ATOM   701  C  CD  . GLN   A 1 89  ? 11.291  5.805   -26.180 1.00 89.59  ? 203 GLN   A CD  1 
ATOM   702  O  OE1 . GLN   A 1 89  ? 12.347  5.971   -25.560 1.00 96.50  ? 203 GLN   A OE1 1 
ATOM   703  N  NE2 . GLN   A 1 89  ? 11.165  4.896   -27.146 1.00 80.28  ? 203 GLN   A NE2 1 
ATOM   704  N  N   . ALA   A 1 90  ? 10.253  8.224   -28.485 1.00 94.30  ? 204 ALA   A N   1 
ATOM   705  C  CA  . ALA   A 1 90  ? 9.640   8.542   -29.764 1.00 87.60  ? 204 ALA   A CA  1 
ATOM   706  C  C   . ALA   A 1 90  ? 8.182   8.887   -29.507 1.00 81.93  ? 204 ALA   A C   1 
ATOM   707  O  O   . ALA   A 1 90  ? 7.537   8.276   -28.649 1.00 83.26  ? 204 ALA   A O   1 
ATOM   708  C  CB  . ALA   A 1 90  ? 9.747   7.381   -30.753 1.00 89.48  ? 204 ALA   A CB  1 
ATOM   709  N  N   . CYS   A 1 91  ? 7.672   9.882   -30.237 1.00 81.32  ? 205 CYS   A N   1 
ATOM   710  C  CA  . CYS   A 1 91  ? 6.335   10.426  -29.993 1.00 84.87  ? 205 CYS   A CA  1 
ATOM   711  C  C   . CYS   A 1 91  ? 5.647   10.708  -31.328 1.00 86.82  ? 205 CYS   A C   1 
ATOM   712  O  O   . CYS   A 1 91  ? 5.369   11.857  -31.668 1.00 71.07  ? 205 CYS   A O   1 
ATOM   713  C  CB  . CYS   A 1 91  ? 6.420   11.699  -29.149 1.00 83.88  ? 205 CYS   A CB  1 
ATOM   714  S  SG  . CYS   A 1 91  ? 7.468   12.980  -29.905 1.00 100.61 ? 205 CYS   A SG  1 
ATOM   715  N  N   . PRO   A 1 92  ? 5.372   9.668   -32.111 1.00 87.95  ? 206 PRO   A N   1 
ATOM   716  C  CA  . PRO   A 1 92  ? 4.571   9.858   -33.329 1.00 75.28  ? 206 PRO   A CA  1 
ATOM   717  C  C   . PRO   A 1 92  ? 3.118   10.154  -32.985 1.00 67.70  ? 206 PRO   A C   1 
ATOM   718  O  O   . PRO   A 1 92  ? 2.601   9.738   -31.945 1.00 66.80  ? 206 PRO   A O   1 
ATOM   719  C  CB  . PRO   A 1 92  ? 4.692   8.507   -34.040 1.00 67.82  ? 206 PRO   A CB  1 
ATOM   720  C  CG  . PRO   A 1 92  ? 5.915   7.866   -33.451 1.00 69.19  ? 206 PRO   A CG  1 
ATOM   721  C  CD  . PRO   A 1 92  ? 5.941   8.316   -32.032 1.00 75.73  ? 206 PRO   A CD  1 
ATOM   722  N  N   . LYS   A 1 93  ? 2.460   10.883  -33.888 1.00 60.00  ? 207 LYS   A N   1 
ATOM   723  C  CA  . LYS   A 1 93  ? 1.033   11.154  -33.755 1.00 61.29  ? 207 LYS   A CA  1 
ATOM   724  C  C   . LYS   A 1 93  ? 0.252   9.841   -33.836 1.00 70.36  ? 207 LYS   A C   1 
ATOM   725  O  O   . LYS   A 1 93  ? 0.493   9.003   -34.711 1.00 53.11  ? 207 LYS   A O   1 
ATOM   726  C  CB  . LYS   A 1 93  ? 0.580   12.134  -34.846 1.00 47.19  ? 207 LYS   A CB  1 
ATOM   727  C  CG  . LYS   A 1 93  ? 0.157   13.517  -34.341 1.00 49.65  ? 207 LYS   A CG  1 
ATOM   728  C  CD  . LYS   A 1 93  ? 1.177   14.070  -33.316 1.00 66.52  ? 207 LYS   A CD  1 
ATOM   729  C  CE  . LYS   A 1 93  ? 0.579   15.063  -32.289 1.00 72.05  ? 207 LYS   A CE  1 
ATOM   730  N  NZ  . LYS   A 1 93  ? 1.458   15.270  -31.062 1.00 71.50  ? 207 LYS   A NZ  1 
ATOM   731  N  N   . ILE   A 1 94  ? -0.684  9.660   -32.910 1.00 70.59  ? 208 ILE   A N   1 
ATOM   732  C  CA  . ILE   A 1 94  ? -1.391  8.394   -32.737 1.00 59.90  ? 208 ILE   A CA  1 
ATOM   733  C  C   . ILE   A 1 94  ? -2.857  8.584   -33.095 1.00 56.79  ? 208 ILE   A C   1 
ATOM   734  O  O   . ILE   A 1 94  ? -3.328  9.697   -33.337 1.00 59.31  ? 208 ILE   A O   1 
ATOM   735  C  CB  . ILE   A 1 94  ? -1.249  7.834   -31.299 1.00 58.21  ? 208 ILE   A CB  1 
ATOM   736  C  CG1 . ILE   A 1 94  ? -1.843  8.809   -30.258 1.00 56.21  ? 208 ILE   A CG1 1 
ATOM   737  C  CG2 . ILE   A 1 94  ? 0.200   7.463   -30.981 1.00 56.99  ? 208 ILE   A CG2 1 
ATOM   738  C  CD1 . ILE   A 1 94  ? -2.760  8.152   -29.191 1.00 62.20  ? 208 ILE   A CD1 1 
ATOM   739  N  N   . SER   A 1 95  ? -3.581  7.470   -33.138 1.00 50.63  ? 209 SER   A N   1 
ATOM   740  C  CA  . SER   A 1 95  ? -5.028  7.468   -33.301 1.00 60.11  ? 209 SER   A CA  1 
ATOM   741  C  C   . SER   A 1 95  ? -5.648  7.158   -31.941 1.00 58.03  ? 209 SER   A C   1 
ATOM   742  O  O   . SER   A 1 95  ? -5.318  6.135   -31.324 1.00 54.43  ? 209 SER   A O   1 
ATOM   743  C  CB  . SER   A 1 95  ? -5.462  6.444   -34.346 1.00 54.36  ? 209 SER   A CB  1 
ATOM   744  O  OG  . SER   A 1 95  ? -6.868  6.426   -34.434 1.00 73.92  ? 209 SER   A OG  1 
ATOM   745  N  N   . PHE   A 1 96  ? -6.520  8.050   -31.462 1.00 45.15  ? 210 PHE   A N   1 
ATOM   746  C  CA  . PHE   A 1 96  ? -6.960  8.039   -30.071 1.00 48.35  ? 210 PHE   A CA  1 
ATOM   747  C  C   . PHE   A 1 96  ? -8.456  8.304   -30.037 1.00 56.14  ? 210 PHE   A C   1 
ATOM   748  O  O   . PHE   A 1 96  ? -8.920  9.350   -30.507 1.00 52.31  ? 210 PHE   A O   1 
ATOM   749  C  CB  . PHE   A 1 96  ? -6.185  9.069   -29.250 1.00 42.02  ? 210 PHE   A CB  1 
ATOM   750  C  CG  . PHE   A 1 96  ? -6.455  9.009   -27.758 1.00 53.36  ? 210 PHE   A CG  1 
ATOM   751  C  CD1 . PHE   A 1 96  ? -7.568  9.630   -27.209 1.00 52.71  ? 210 PHE   A CD1 1 
ATOM   752  C  CD2 . PHE   A 1 96  ? -5.576  8.369   -26.898 1.00 43.68  ? 210 PHE   A CD2 1 
ATOM   753  C  CE1 . PHE   A 1 96  ? -7.810  9.594   -25.842 1.00 47.24  ? 210 PHE   A CE1 1 
ATOM   754  C  CE2 . PHE   A 1 96  ? -5.813  8.333   -25.536 1.00 46.58  ? 210 PHE   A CE2 1 
ATOM   755  C  CZ  . PHE   A 1 96  ? -6.940  8.937   -25.006 1.00 51.55  ? 210 PHE   A CZ  1 
ATOM   756  N  N   . ASP   A 1 97  ? -9.206  7.343   -29.495 1.00 45.79  ? 211 ASP   A N   1 
ATOM   757  C  CA  . ASP   A 1 97  ? -10.654 7.414   -29.376 1.00 47.15  ? 211 ASP   A CA  1 
ATOM   758  C  C   . ASP   A 1 97  ? -11.131 6.312   -28.423 1.00 47.38  ? 211 ASP   A C   1 
ATOM   759  O  O   . ASP   A 1 97  ? -11.281 5.155   -28.840 1.00 50.66  ? 211 ASP   A O   1 
ATOM   760  C  CB  . ASP   A 1 97  ? -11.313 7.266   -30.744 1.00 44.80  ? 211 ASP   A CB  1 
ATOM   761  C  CG  . ASP   A 1 97  ? -12.752 7.691   -30.730 1.00 58.90  ? 211 ASP   A CG  1 
ATOM   762  O  OD1 . ASP   A 1 97  ? -13.125 8.553   -29.893 1.00 59.47  ? 211 ASP   A OD1 1 
ATOM   763  O  OD2 . ASP   A 1 97  ? -13.519 7.145   -31.545 1.00 67.75  ? 211 ASP   A OD2 1 
ATOM   764  N  N   . PRO   A 1 98  ? -11.362 6.628   -27.152 1.00 40.35  ? 212 PRO   A N   1 
ATOM   765  C  CA  . PRO   A 1 98  ? -11.580 5.582   -26.144 1.00 44.54  ? 212 PRO   A CA  1 
ATOM   766  C  C   . PRO   A 1 98  ? -12.755 4.675   -26.515 1.00 51.62  ? 212 PRO   A C   1 
ATOM   767  O  O   . PRO   A 1 98  ? -13.713 5.098   -27.175 1.00 43.35  ? 212 PRO   A O   1 
ATOM   768  C  CB  . PRO   A 1 98  ? -11.842 6.390   -24.866 1.00 43.61  ? 212 PRO   A CB  1 
ATOM   769  C  CG  . PRO   A 1 98  ? -11.730 7.870   -25.269 1.00 51.63  ? 212 PRO   A CG  1 
ATOM   770  C  CD  . PRO   A 1 98  ? -11.002 7.915   -26.541 1.00 53.14  ? 212 PRO   A CD  1 
ATOM   771  N  N   . ILE   A 1 99  ? -12.649 3.403   -26.128 1.00 45.97  ? 213 ILE   A N   1 
ATOM   772  C  CA  . ILE   A 1 99  ? -13.692 2.410   -26.386 1.00 35.58  ? 213 ILE   A CA  1 
ATOM   773  C  C   . ILE   A 1 99  ? -14.173 1.821   -25.063 1.00 39.48  ? 213 ILE   A C   1 
ATOM   774  O  O   . ILE   A 1 99  ? -13.443 1.861   -24.064 1.00 36.97  ? 213 ILE   A O   1 
ATOM   775  C  CB  . ILE   A 1 99  ? -13.178 1.323   -27.334 1.00 33.06  ? 213 ILE   A CB  1 
ATOM   776  C  CG1 . ILE   A 1 99  ? -12.093 0.484   -26.648 1.00 35.03  ? 213 ILE   A CG1 1 
ATOM   777  C  CG2 . ILE   A 1 99  ? -12.631 1.963   -28.566 1.00 36.12  ? 213 ILE   A CG2 1 
ATOM   778  C  CD1 . ILE   A 1 99  ? -11.752 -0.816  -27.371 1.00 42.99  ? 213 ILE   A CD1 1 
ATOM   779  N  N   . PRO   A 1 100 ? -15.385 1.282   -24.998 1.00 45.88  ? 214 PRO   A N   1 
ATOM   780  C  CA  . PRO   A 1 100 ? -15.884 0.750   -23.722 1.00 37.98  ? 214 PRO   A CA  1 
ATOM   781  C  C   . PRO   A 1 100 ? -15.098 -0.489  -23.292 1.00 35.60  ? 214 PRO   A C   1 
ATOM   782  O  O   . PRO   A 1 100 ? -14.800 -1.363  -24.119 1.00 40.53  ? 214 PRO   A O   1 
ATOM   783  C  CB  . PRO   A 1 100 ? -17.350 0.410   -24.042 1.00 41.97  ? 214 PRO   A CB  1 
ATOM   784  C  CG  . PRO   A 1 100 ? -17.685 1.148   -25.317 1.00 34.34  ? 214 PRO   A CG  1 
ATOM   785  C  CD  . PRO   A 1 100 ? -16.393 1.189   -26.071 1.00 43.69  ? 214 PRO   A CD  1 
ATOM   786  N  N   . ILE   A 1 101 ? -14.753 -0.549  -21.992 1.00 35.92  ? 215 ILE   A N   1 
ATOM   787  C  CA  . ILE   A 1 101 ? -14.114 -1.717  -21.408 1.00 37.92  ? 215 ILE   A CA  1 
ATOM   788  C  C   . ILE   A 1 101 ? -15.070 -2.310  -20.390 1.00 35.43  ? 215 ILE   A C   1 
ATOM   789  O  O   . ILE   A 1 101 ? -15.598 -1.569  -19.553 1.00 43.72  ? 215 ILE   A O   1 
ATOM   790  C  CB  . ILE   A 1 101 ? -12.769 -1.370  -20.736 1.00 41.33  ? 215 ILE   A CB  1 
ATOM   791  C  CG1 . ILE   A 1 101 ? -11.802 -0.676  -21.659 1.00 42.14  ? 215 ILE   A CG1 1 
ATOM   792  C  CG2 . ILE   A 1 101 ? -12.142 -2.630  -20.109 1.00 44.76  ? 215 ILE   A CG2 1 
ATOM   793  C  CD1 . ILE   A 1 101 ? -11.500 -1.435  -22.933 1.00 48.62  ? 215 ILE   A CD1 1 
ATOM   794  N  N   . HIS   A 1 102 ? -15.274 -3.631  -20.462 1.00 32.74  ? 216 HIS   A N   1 
ATOM   795  C  CA  . HIS   A 1 102 ? -16.024 -4.383  -19.459 1.00 37.74  ? 216 HIS   A CA  1 
ATOM   796  C  C   . HIS   A 1 102 ? -15.074 -5.016  -18.453 1.00 35.61  ? 216 HIS   A C   1 
ATOM   797  O  O   . HIS   A 1 102 ? -14.024 -5.527  -18.842 1.00 44.11  ? 216 HIS   A O   1 
ATOM   798  C  CB  . HIS   A 1 102 ? -16.811 -5.496  -20.117 1.00 33.00  ? 216 HIS   A CB  1 
ATOM   799  C  CG  . HIS   A 1 102 ? -17.748 -5.025  -21.183 1.00 39.36  ? 216 HIS   A CG  1 
ATOM   800  N  ND1 . HIS   A 1 102 ? -19.089 -4.812  -20.949 1.00 39.55  ? 216 HIS   A ND1 1 
ATOM   801  C  CD2 . HIS   A 1 102 ? -17.532 -4.689  -22.480 1.00 36.18  ? 216 HIS   A CD2 1 
ATOM   802  C  CE1 . HIS   A 1 102 ? -19.664 -4.379  -22.060 1.00 45.51  ? 216 HIS   A CE1 1 
ATOM   803  N  NE2 . HIS   A 1 102 ? -18.742 -4.300  -23.004 1.00 40.04  ? 216 HIS   A NE2 1 
ATOM   804  N  N   . TYR   A 1 103 ? -15.464 -5.014  -17.173 1.00 31.61  ? 217 TYR   A N   1 
ATOM   805  C  CA  . TYR   A 1 103 ? -14.724 -5.629  -16.078 1.00 43.39  ? 217 TYR   A CA  1 
ATOM   806  C  C   . TYR   A 1 103 ? -15.538 -6.824  -15.585 1.00 46.77  ? 217 TYR   A C   1 
ATOM   807  O  O   . TYR   A 1 103 ? -16.773 -6.740  -15.473 1.00 37.97  ? 217 TYR   A O   1 
ATOM   808  C  CB  . TYR   A 1 103 ? -14.447 -4.610  -14.959 1.00 37.59  ? 217 TYR   A CB  1 
ATOM   809  C  CG  . TYR   A 1 103 ? -13.361 -3.651  -15.396 1.00 47.70  ? 217 TYR   A CG  1 
ATOM   810  C  CD1 . TYR   A 1 103 ? -12.024 -4.018  -15.296 1.00 41.08  ? 217 TYR   A CD1 1 
ATOM   811  C  CD2 . TYR   A 1 103 ? -13.668 -2.428  -15.998 1.00 46.63  ? 217 TYR   A CD2 1 
ATOM   812  C  CE1 . TYR   A 1 103 ? -11.018 -3.182  -15.746 1.00 46.81  ? 217 TYR   A CE1 1 
ATOM   813  C  CE2 . TYR   A 1 103 ? -12.660 -1.558  -16.441 1.00 41.61  ? 217 TYR   A CE2 1 
ATOM   814  C  CZ  . TYR   A 1 103 ? -11.338 -1.965  -16.314 1.00 44.97  ? 217 TYR   A CZ  1 
ATOM   815  O  OH  . TYR   A 1 103 ? -10.316 -1.175  -16.760 1.00 47.26  ? 217 TYR   A OH  1 
ATOM   816  N  N   . CYS   A 1 104 ? -14.842 -7.937  -15.315 1.00 35.51  ? 218 CYS   A N   1 
ATOM   817  C  CA  . CYS   A 1 104 ? -15.444 -9.264  -15.226 1.00 39.60  ? 218 CYS   A CA  1 
ATOM   818  C  C   . CYS   A 1 104 ? -14.779 -10.072 -14.129 1.00 44.78  ? 218 CYS   A C   1 
ATOM   819  O  O   . CYS   A 1 104 ? -13.561 -9.989  -13.933 1.00 47.12  ? 218 CYS   A O   1 
ATOM   820  C  CB  . CYS   A 1 104 ? -15.312 -10.046 -16.547 1.00 40.20  ? 218 CYS   A CB  1 
ATOM   821  S  SG  . CYS   A 1 104 ? -15.945 -9.215  -18.047 1.00 53.31  ? 218 CYS   A SG  1 
ATOM   822  N  N   . THR   A 1 105 ? -15.570 -10.873 -13.457 1.00 43.39  ? 219 THR   A N   1 
ATOM   823  C  CA  . THR   A 1 105 ? -15.015 -11.607 -12.333 1.00 46.59  ? 219 THR   A CA  1 
ATOM   824  C  C   . THR   A 1 105 ? -14.625 -13.013 -12.769 1.00 43.85  ? 219 THR   A C   1 
ATOM   825  O  O   . THR   A 1 105 ? -15.266 -13.596 -13.645 1.00 39.98  ? 219 THR   A O   1 
ATOM   826  C  CB  . THR   A 1 105 ? -16.026 -11.679 -11.195 1.00 50.66  ? 219 THR   A CB  1 
ATOM   827  O  OG1 . THR   A 1 105 ? -17.314 -12.007 -11.731 1.00 57.03  ? 219 THR   A OG1 1 
ATOM   828  C  CG2 . THR   A 1 105 ? -16.118 -10.327 -10.506 1.00 47.23  ? 219 THR   A CG2 1 
ATOM   829  N  N   . PRO   A 1 106 ? -13.557 -13.558 -12.208 1.00 50.59  ? 220 PRO   A N   1 
ATOM   830  C  CA  . PRO   A 1 106 ? -13.168 -14.935 -12.511 1.00 45.95  ? 220 PRO   A CA  1 
ATOM   831  C  C   . PRO   A 1 106 ? -14.045 -15.893 -11.715 1.00 44.94  ? 220 PRO   A C   1 
ATOM   832  O  O   . PRO   A 1 106 ? -14.932 -15.491 -10.953 1.00 47.15  ? 220 PRO   A O   1 
ATOM   833  C  CB  . PRO   A 1 106 ? -11.712 -14.990 -12.053 1.00 46.80  ? 220 PRO   A CB  1 
ATOM   834  C  CG  . PRO   A 1 106 ? -11.666 -14.048 -10.915 1.00 50.61  ? 220 PRO   A CG  1 
ATOM   835  C  CD  . PRO   A 1 106 ? -12.617 -12.924 -11.268 1.00 41.55  ? 220 PRO   A CD  1 
ATOM   836  N  N   . ALA   A 1 107 ? -13.792 -17.182 -11.910 1.00 49.89  ? 221 ALA   A N   1 
ATOM   837  C  CA  . ALA   A 1 107 ? -14.590 -18.212 -11.257 1.00 52.77  ? 221 ALA   A CA  1 
ATOM   838  C  C   . ALA   A 1 107 ? -14.488 -18.097 -9.738  1.00 57.90  ? 221 ALA   A C   1 
ATOM   839  O  O   . ALA   A 1 107 ? -13.410 -17.862 -9.185  1.00 60.07  ? 221 ALA   A O   1 
ATOM   840  C  CB  . ALA   A 1 107 ? -14.130 -19.602 -11.713 1.00 48.27  ? 221 ALA   A CB  1 
ATOM   841  N  N   . GLY   A 1 108 ? -15.624 -18.273 -9.062  1.00 48.78  ? 222 GLY   A N   1 
ATOM   842  C  CA  . GLY   A 1 108 ? -15.701 -18.168 -7.629  1.00 49.25  ? 222 GLY   A CA  1 
ATOM   843  C  C   . GLY   A 1 108 ? -16.197 -16.827 -7.136  1.00 59.27  ? 222 GLY   A C   1 
ATOM   844  O  O   . GLY   A 1 108 ? -16.507 -16.692 -5.942  1.00 54.74  ? 222 GLY   A O   1 
ATOM   845  N  N   . TYR   A 1 109 ? -16.283 -15.837 -8.026  1.00 55.58  ? 223 TYR   A N   1 
ATOM   846  C  CA  . TYR   A 1 109 ? -16.713 -14.493 -7.680  1.00 45.48  ? 223 TYR   A CA  1 
ATOM   847  C  C   . TYR   A 1 109 ? -17.808 -14.046 -8.638  1.00 46.81  ? 223 TYR   A C   1 
ATOM   848  O  O   . TYR   A 1 109 ? -17.952 -14.565 -9.753  1.00 47.94  ? 223 TYR   A O   1 
ATOM   849  C  CB  . TYR   A 1 109 ? -15.554 -13.500 -7.729  1.00 46.61  ? 223 TYR   A CB  1 
ATOM   850  C  CG  . TYR   A 1 109 ? -14.389 -13.842 -6.823  1.00 54.29  ? 223 TYR   A CG  1 
ATOM   851  C  CD1 . TYR   A 1 109 ? -13.463 -14.800 -7.184  1.00 57.43  ? 223 TYR   A CD1 1 
ATOM   852  C  CD2 . TYR   A 1 109 ? -14.216 -13.193 -5.601  1.00 56.86  ? 223 TYR   A CD2 1 
ATOM   853  C  CE1 . TYR   A 1 109 ? -12.381 -15.120 -6.350  1.00 59.11  ? 223 TYR   A CE1 1 
ATOM   854  C  CE2 . TYR   A 1 109 ? -13.144 -13.497 -4.762  1.00 67.07  ? 223 TYR   A CE2 1 
ATOM   855  C  CZ  . TYR   A 1 109 ? -12.228 -14.466 -5.146  1.00 64.47  ? 223 TYR   A CZ  1 
ATOM   856  O  OH  . TYR   A 1 109 ? -11.159 -14.771 -4.320  1.00 64.97  ? 223 TYR   A OH  1 
ATOM   857  N  N   . VAL   A 1 110 ? -18.579 -13.054 -8.194  1.00 45.34  ? 224 VAL   A N   1 
ATOM   858  C  CA  . VAL   A 1 110 ? -19.624 -12.452 -9.011  1.00 42.56  ? 224 VAL   A CA  1 
ATOM   859  C  C   . VAL   A 1 110 ? -19.613 -10.952 -8.744  1.00 44.04  ? 224 VAL   A C   1 
ATOM   860  O  O   . VAL   A 1 110 ? -19.036 -10.483 -7.770  1.00 45.72  ? 224 VAL   A O   1 
ATOM   861  C  CB  . VAL   A 1 110 ? -21.009 -13.076 -8.698  1.00 45.36  ? 224 VAL   A CB  1 
ATOM   862  C  CG1 . VAL   A 1 110 ? -21.581 -12.496 -7.419  1.00 44.97  ? 224 VAL   A CG1 1 
ATOM   863  C  CG2 . VAL   A 1 110 ? -21.981 -12.903 -9.844  1.00 45.54  ? 224 VAL   A CG2 1 
ATOM   864  N  N   . ILE   A 1 111 ? -20.217 -10.195 -9.644  1.00 37.25  ? 225 ILE   A N   1 
ATOM   865  C  CA  . ILE   A 1 111 ? -20.397 -8.767  -9.468  1.00 39.88  ? 225 ILE   A CA  1 
ATOM   866  C  C   . ILE   A 1 111 ? -21.856 -8.523  -9.111  1.00 41.33  ? 225 ILE   A C   1 
ATOM   867  O  O   . ILE   A 1 111 ? -22.761 -8.973  -9.824  1.00 42.82  ? 225 ILE   A O   1 
ATOM   868  C  CB  . ILE   A 1 111 ? -20.003 -7.979  -10.733 1.00 34.56  ? 225 ILE   A CB  1 
ATOM   869  C  CG1 . ILE   A 1 111 ? -18.514 -8.164  -11.051 1.00 41.13  ? 225 ILE   A CG1 1 
ATOM   870  C  CG2 . ILE   A 1 111 ? -20.359 -6.524  -10.557 1.00 35.79  ? 225 ILE   A CG2 1 
ATOM   871  C  CD1 . ILE   A 1 111 ? -18.114 -7.716  -12.476 1.00 39.14  ? 225 ILE   A CD1 1 
ATOM   872  N  N   . LEU   A 1 112 ? -22.087 -7.822  -8.009  1.00 35.08  ? 226 LEU   A N   1 
ATOM   873  C  CA  . LEU   A 1 112 ? -23.428 -7.426  -7.618  1.00 36.08  ? 226 LEU   A CA  1 
ATOM   874  C  C   . LEU   A 1 112 ? -23.711 -6.046  -8.198  1.00 38.11  ? 226 LEU   A C   1 
ATOM   875  O  O   . LEU   A 1 112 ? -22.863 -5.153  -8.138  1.00 37.87  ? 226 LEU   A O   1 
ATOM   876  C  CB  . LEU   A 1 112 ? -23.545 -7.416  -6.096  1.00 39.19  ? 226 LEU   A CB  1 
ATOM   877  C  CG  . LEU   A 1 112 ? -23.480 -8.777  -5.370  1.00 49.28  ? 226 LEU   A CG  1 
ATOM   878  C  CD1 . LEU   A 1 112 ? -24.216 -8.751  -4.042  1.00 48.57  ? 226 LEU   A CD1 1 
ATOM   879  C  CD2 . LEU   A 1 112 ? -24.027 -9.902  -6.255  1.00 40.95  ? 226 LEU   A CD2 1 
ATOM   880  N  N   . LYS   A 1 113 ? -24.900 -5.877  -8.762  1.00 39.14  ? 227 LYS   A N   1 
ATOM   881  C  CA  . LYS   A 1 113 ? -25.285 -4.653  -9.452  1.00 43.80  ? 227 LYS   A CA  1 
ATOM   882  C  C   . LYS   A 1 113 ? -26.500 -4.028  -8.773  1.00 43.01  ? 227 LYS   A C   1 
ATOM   883  O  O   . LYS   A 1 113 ? -27.547 -4.678  -8.631  1.00 40.44  ? 227 LYS   A O   1 
ATOM   884  C  CB  . LYS   A 1 113 ? -25.590 -4.933  -10.923 1.00 39.37  ? 227 LYS   A CB  1 
ATOM   885  C  CG  . LYS   A 1 113 ? -25.437 -3.720  -11.767 1.00 47.68  ? 227 LYS   A CG  1 
ATOM   886  C  CD  . LYS   A 1 113 ? -25.805 -3.982  -13.202 1.00 60.66  ? 227 LYS   A CD  1 
ATOM   887  C  CE  . LYS   A 1 113 ? -27.286 -3.842  -13.410 1.00 59.77  ? 227 LYS   A CE  1 
ATOM   888  N  NZ  . LYS   A 1 113 ? -27.525 -3.119  -14.675 1.00 62.57  ? 227 LYS   A NZ  1 
ATOM   889  N  N   . CYS   A 1 114 ? -26.360 -2.767  -8.375  1.00 37.06  ? 228 CYS   A N   1 
ATOM   890  C  CA  . CYS   A 1 114 ? -27.411 -2.041  -7.674  1.00 40.36  ? 228 CYS   A CA  1 
ATOM   891  C  C   . CYS   A 1 114 ? -28.331 -1.366  -8.679  1.00 41.11  ? 228 CYS   A C   1 
ATOM   892  O  O   . CYS   A 1 114 ? -27.876 -0.569  -9.495  1.00 52.17  ? 228 CYS   A O   1 
ATOM   893  C  CB  . CYS   A 1 114 ? -26.784 -1.011  -6.735  1.00 51.25  ? 228 CYS   A CB  1 
ATOM   894  S  SG  . CYS   A 1 114 ? -27.983 0.036   -5.900  1.00 57.58  ? 228 CYS   A SG  1 
ATOM   895  N  N   . ASN   A 1 115 ? -29.622 -1.654  -8.620  1.00 45.04  ? 229 ASN   A N   1 
ATOM   896  C  CA  . ASN   A 1 115 ? -30.541 -1.162  -9.640  1.00 53.58  ? 229 ASN   A CA  1 
ATOM   897  C  C   . ASN   A 1 115 ? -31.521 -0.128  -9.096  1.00 59.86  ? 229 ASN   A C   1 
ATOM   898  O  O   . ASN   A 1 115 ? -32.539 0.159   -9.742  1.00 51.90  ? 229 ASN   A O   1 
ATOM   899  C  CB  . ASN   A 1 115 ? -31.274 -2.345  -10.278 1.00 55.95  ? 229 ASN   A CB  1 
ATOM   900  C  CG  . ASN   A 1 115 ? -30.332 -3.264  -11.028 1.00 55.86  ? 229 ASN   A CG  1 
ATOM   901  O  OD1 . ASN   A 1 115 ? -29.692 -2.838  -11.986 1.00 60.05  ? 229 ASN   A OD1 1 
ATOM   902  N  ND2 . ASN   A 1 115 ? -30.217 -4.512  -10.584 1.00 49.64  ? 229 ASN   A ND2 1 
ATOM   903  N  N   . ASP   A 1 116 ? -31.237 0.434   -7.921  1.00 51.80  ? 230 ASP   A N   1 
ATOM   904  C  CA  . ASP   A 1 116 ? -32.077 1.475   -7.350  1.00 55.07  ? 230 ASP   A CA  1 
ATOM   905  C  C   . ASP   A 1 116 ? -31.816 2.767   -8.111  1.00 49.15  ? 230 ASP   A C   1 
ATOM   906  O  O   . ASP   A 1 116 ? -30.687 3.261   -8.124  1.00 54.79  ? 230 ASP   A O   1 
ATOM   907  C  CB  . ASP   A 1 116 ? -31.774 1.642   -5.858  1.00 62.71  ? 230 ASP   A CB  1 
ATOM   908  C  CG  . ASP   A 1 116 ? -32.212 0.437   -5.013  1.00 63.40  ? 230 ASP   A CG  1 
ATOM   909  O  OD1 . ASP   A 1 116 ? -32.567 -0.627  -5.584  1.00 63.27  ? 230 ASP   A OD1 1 
ATOM   910  O  OD2 . ASP   A 1 116 ? -32.188 0.559   -3.770  1.00 55.67  ? 230 ASP   A OD2 1 
ATOM   911  N  N   . LYS   A 1 117 ? -32.856 3.328   -8.728  1.00 55.39  ? 231 LYS   A N   1 
ATOM   912  C  CA  . LYS   A 1 117 ? -32.667 4.454   -9.635  1.00 52.27  ? 231 LYS   A CA  1 
ATOM   913  C  C   . LYS   A 1 117 ? -32.139 5.701   -8.936  1.00 55.97  ? 231 LYS   A C   1 
ATOM   914  O  O   . LYS   A 1 117 ? -31.533 6.556   -9.590  1.00 60.78  ? 231 LYS   A O   1 
ATOM   915  C  CB  . LYS   A 1 117 ? -33.982 4.762   -10.336 1.00 64.32  ? 231 LYS   A CB  1 
ATOM   916  C  CG  . LYS   A 1 117 ? -34.524 3.588   -11.120 1.00 71.48  ? 231 LYS   A CG  1 
ATOM   917  C  CD  . LYS   A 1 117 ? -35.617 4.053   -12.064 1.00 72.65  ? 231 LYS   A CD  1 
ATOM   918  C  CE  . LYS   A 1 117 ? -36.332 2.892   -12.748 1.00 79.72  ? 231 LYS   A CE  1 
ATOM   919  N  NZ  . LYS   A 1 117 ? -35.396 2.023   -13.520 1.00 73.60  ? 231 LYS   A NZ  1 
ATOM   920  N  N   . ASN   A 1 118 ? -32.375 5.839   -7.627  1.00 52.33  ? 232 ASN   A N   1 
ATOM   921  C  CA  . ASN   A 1 118 ? -31.978 7.011   -6.847  1.00 59.32  ? 232 ASN   A CA  1 
ATOM   922  C  C   . ASN   A 1 118 ? -30.702 6.785   -6.039  1.00 57.48  ? 232 ASN   A C   1 
ATOM   923  O  O   . ASN   A 1 118 ? -30.237 7.713   -5.367  1.00 54.80  ? 232 ASN   A O   1 
ATOM   924  C  CB  . ASN   A 1 118 ? -33.116 7.433   -5.897  1.00 53.99  ? 232 ASN   A CB  1 
ATOM   925  C  CG  . ASN   A 1 118 ? -33.617 6.281   -4.991  1.00 70.15  ? 232 ASN   A CG  1 
ATOM   926  O  OD1 . ASN   A 1 118 ? -33.680 5.112   -5.399  1.00 66.28  ? 232 ASN   A OD1 1 
ATOM   927  N  ND2 . ASN   A 1 118 ? -33.999 6.628   -3.762  1.00 72.03  ? 232 ASN   A ND2 1 
ATOM   928  N  N   . PHE   A 1 119 ? -30.136 5.580   -6.094  1.00 49.32  ? 233 PHE   A N   1 
ATOM   929  C  CA  . PHE   A 1 119 ? -28.946 5.226   -5.332  1.00 42.77  ? 233 PHE   A CA  1 
ATOM   930  C  C   . PHE   A 1 119 ? -27.856 6.287   -5.437  1.00 44.92  ? 233 PHE   A C   1 
ATOM   931  O  O   . PHE   A 1 119 ? -27.511 6.740   -6.528  1.00 46.28  ? 233 PHE   A O   1 
ATOM   932  C  CB  . PHE   A 1 119 ? -28.410 3.892   -5.843  1.00 49.04  ? 233 PHE   A CB  1 
ATOM   933  C  CG  . PHE   A 1 119 ? -27.242 3.389   -5.069  1.00 54.89  ? 233 PHE   A CG  1 
ATOM   934  C  CD1 . PHE   A 1 119 ? -27.303 3.286   -3.684  1.00 52.10  ? 233 PHE   A CD1 1 
ATOM   935  C  CD2 . PHE   A 1 119 ? -26.078 3.038   -5.715  1.00 51.25  ? 233 PHE   A CD2 1 
ATOM   936  C  CE1 . PHE   A 1 119 ? -26.212 2.824   -2.960  1.00 58.09  ? 233 PHE   A CE1 1 
ATOM   937  C  CE2 . PHE   A 1 119 ? -24.983 2.584   -4.998  1.00 60.19  ? 233 PHE   A CE2 1 
ATOM   938  C  CZ  . PHE   A 1 119 ? -25.050 2.472   -3.622  1.00 50.39  ? 233 PHE   A CZ  1 
ATOM   939  N  N   . ASN   A 1 120 ? -27.280 6.671   -4.309  1.00 50.11  ? 234 ASN   A N   1 
ATOM   940  C  CA  . ASN   A 1 120 ? -26.289 7.738   -4.340  1.00 48.79  ? 234 ASN   A CA  1 
ATOM   941  C  C   . ASN   A 1 120 ? -24.853 7.245   -4.209  1.00 47.22  ? 234 ASN   A C   1 
ATOM   942  O  O   . ASN   A 1 120 ? -23.937 8.072   -4.161  1.00 46.87  ? 234 ASN   A O   1 
ATOM   943  C  CB  . ASN   A 1 120 ? -26.602 8.766   -3.252  1.00 49.32  ? 234 ASN   A CB  1 
ATOM   944  C  CG  . ASN   A 1 120 ? -26.382 8.224   -1.869  1.00 48.27  ? 234 ASN   A CG  1 
ATOM   945  O  OD1 . ASN   A 1 120 ? -25.774 7.182   -1.688  1.00 53.14  ? 234 ASN   A OD1 1 
ATOM   946  N  ND2 . ASN   A 1 120 ? -26.873 8.927   -0.890  1.00 54.31  ? 234 ASN   A ND2 1 
ATOM   947  N  N   . GLY   A 1 121 ? -24.628 5.929   -4.169  1.00 44.25  ? 235 GLY   A N   1 
ATOM   948  C  CA  . GLY   A 1 121 ? -23.300 5.347   -4.151  1.00 51.70  ? 235 GLY   A CA  1 
ATOM   949  C  C   . GLY   A 1 121 ? -22.931 4.693   -2.832  1.00 51.92  ? 235 GLY   A C   1 
ATOM   950  O  O   . GLY   A 1 121 ? -22.116 3.760   -2.821  1.00 50.15  ? 235 GLY   A O   1 
ATOM   951  N  N   . THR   A 1 122 ? -23.512 5.163   -1.722  1.00 43.87  ? 236 THR   A N   1 
ATOM   952  C  CA  . THR   A 1 122 ? -23.265 4.606   -0.402  1.00 56.75  ? 236 THR   A CA  1 
ATOM   953  C  C   . THR   A 1 122 ? -24.598 4.230   0.228   1.00 54.73  ? 236 THR   A C   1 
ATOM   954  O  O   . THR   A 1 122 ? -25.612 4.917   0.059   1.00 52.27  ? 236 THR   A O   1 
ATOM   955  C  CB  . THR   A 1 122 ? -22.488 5.581   0.536   1.00 50.11  ? 236 THR   A CB  1 
ATOM   956  O  OG1 . THR   A 1 122 ? -23.371 6.603   1.008   1.00 69.89  ? 236 THR   A OG1 1 
ATOM   957  C  CG2 . THR   A 1 122 ? -21.334 6.253   -0.183  1.00 50.00  ? 236 THR   A CG2 1 
ATOM   958  N  N   . GLY   A 1 123 ? -24.593 3.106   0.924   1.00 54.02  ? 237 GLY   A N   1 
ATOM   959  C  CA  . GLY   A 1 123 ? -25.754 2.707   1.669   1.00 60.01  ? 237 GLY   A CA  1 
ATOM   960  C  C   . GLY   A 1 123 ? -26.396 1.477   1.092   1.00 57.48  ? 237 GLY   A C   1 
ATOM   961  O  O   . GLY   A 1 123 ? -25.841 0.805   0.225   1.00 50.68  ? 237 GLY   A O   1 
ATOM   962  N  N   . PRO   A 1 124 ? -27.584 1.154   1.576   1.00 60.91  ? 238 PRO   A N   1 
ATOM   963  C  CA  . PRO   A 1 124 ? -28.211 -0.108  1.206   1.00 54.88  ? 238 PRO   A CA  1 
ATOM   964  C  C   . PRO   A 1 124 ? -28.931 0.011   -0.118  1.00 50.40  ? 238 PRO   A C   1 
ATOM   965  O  O   . PRO   A 1 124 ? -29.591 1.010   -0.410  1.00 53.48  ? 238 PRO   A O   1 
ATOM   966  C  CB  . PRO   A 1 124 ? -29.193 -0.348  2.355   1.00 62.12  ? 238 PRO   A CB  1 
ATOM   967  C  CG  . PRO   A 1 124 ? -29.612 1.023   2.739   1.00 54.29  ? 238 PRO   A CG  1 
ATOM   968  C  CD  . PRO   A 1 124 ? -28.371 1.876   2.589   1.00 69.74  ? 238 PRO   A CD  1 
ATOM   969  N  N   . CYS   A 1 125 ? -28.753 -1.007  -0.942  1.00 54.53  ? 239 CYS   A N   1 
ATOM   970  C  CA  . CYS   A 1 125 ? -29.463 -1.111  -2.199  1.00 49.10  ? 239 CYS   A CA  1 
ATOM   971  C  C   . CYS   A 1 125 ? -30.545 -2.162  -2.058  1.00 57.42  ? 239 CYS   A C   1 
ATOM   972  O  O   . CYS   A 1 125 ? -30.292 -3.256  -1.550  1.00 49.53  ? 239 CYS   A O   1 
ATOM   973  C  CB  . CYS   A 1 125 ? -28.519 -1.491  -3.330  1.00 54.06  ? 239 CYS   A CB  1 
ATOM   974  S  SG  . CYS   A 1 125 ? -29.259 -1.276  -4.951  1.00 67.18  ? 239 CYS   A SG  1 
ATOM   975  N  N   . LYS   A 1 126 ? -31.742 -1.847  -2.536  1.00 51.34  ? 240 LYS   A N   1 
ATOM   976  C  CA  . LYS   A 1 126 ? -32.857 -2.772  -2.390  1.00 67.37  ? 240 LYS   A CA  1 
ATOM   977  C  C   . LYS   A 1 126 ? -33.180 -3.562  -3.657  1.00 69.51  ? 240 LYS   A C   1 
ATOM   978  O  O   . LYS   A 1 126 ? -33.937 -4.536  -3.580  1.00 59.03  ? 240 LYS   A O   1 
ATOM   979  C  CB  . LYS   A 1 126 ? -34.103 -2.013  -1.926  1.00 67.20  ? 240 LYS   A CB  1 
ATOM   980  C  CG  . LYS   A 1 126 ? -34.144 -1.814  -0.414  1.00 77.20  ? 240 LYS   A CG  1 
ATOM   981  C  CD  . LYS   A 1 126 ? -35.576 -1.716  0.092   1.00 82.08  ? 240 LYS   A CD  1 
ATOM   982  C  CE  . LYS   A 1 126 ? -35.684 -2.137  1.549   1.00 79.51  ? 240 LYS   A CE  1 
ATOM   983  N  NZ  . LYS   A 1 126 ? -35.590 -0.954  2.451   1.00 72.01  ? 240 LYS   A NZ  1 
ATOM   984  N  N   . ASN   A 1 127 ? -32.632 -3.182  -4.813  1.00 67.59  ? 241 ASN   A N   1 
ATOM   985  C  CA  . ASN   A 1 127 ? -32.877 -3.871  -6.083  1.00 54.70  ? 241 ASN   A CA  1 
ATOM   986  C  C   . ASN   A 1 127 ? -31.530 -4.321  -6.636  1.00 57.30  ? 241 ASN   A C   1 
ATOM   987  O  O   . ASN   A 1 127 ? -30.904 -3.613  -7.430  1.00 49.17  ? 241 ASN   A O   1 
ATOM   988  C  CB  . ASN   A 1 127 ? -33.621 -2.962  -7.058  1.00 61.84  ? 241 ASN   A CB  1 
ATOM   989  C  CG  . ASN   A 1 127 ? -33.998 -3.659  -8.365  1.00 63.53  ? 241 ASN   A CG  1 
ATOM   990  O  OD1 . ASN   A 1 127 ? -33.614 -4.804  -8.628  1.00 59.66  ? 241 ASN   A OD1 1 
ATOM   991  N  ND2 . ASN   A 1 127 ? -34.762 -2.954  -9.192  1.00 67.74  ? 241 ASN   A ND2 1 
ATOM   992  N  N   . VAL   A 1 128 ? -31.091 -5.498  -6.201  1.00 49.53  ? 242 VAL   A N   1 
ATOM   993  C  CA  . VAL   A 1 128 ? -29.773 -6.021  -6.520  1.00 44.34  ? 242 VAL   A CA  1 
ATOM   994  C  C   . VAL   A 1 128 ? -29.904 -7.110  -7.563  1.00 50.86  ? 242 VAL   A C   1 
ATOM   995  O  O   . VAL   A 1 128 ? -30.809 -7.950  -7.487  1.00 49.39  ? 242 VAL   A O   1 
ATOM   996  C  CB  . VAL   A 1 128 ? -29.071 -6.567  -5.268  1.00 50.17  ? 242 VAL   A CB  1 
ATOM   997  C  CG1 . VAL   A 1 128 ? -27.623 -6.908  -5.577  1.00 51.77  ? 242 VAL   A CG1 1 
ATOM   998  C  CG2 . VAL   A 1 128 ? -29.137 -5.540  -4.165  1.00 49.78  ? 242 VAL   A CG2 1 
ATOM   999  N  N   . SER   A 1 129 ? -28.992 -7.099  -8.539  1.00 52.90  ? 243 SER   A N   1 
ATOM   1000 C  CA  . SER   A 1 129 ? -28.818 -8.205  -9.464  1.00 51.63  ? 243 SER   A CA  1 
ATOM   1001 C  C   . SER   A 1 129 ? -27.367 -8.657  -9.435  1.00 49.89  ? 243 SER   A C   1 
ATOM   1002 O  O   . SER   A 1 129 ? -26.502 -8.002  -8.842  1.00 43.98  ? 243 SER   A O   1 
ATOM   1003 C  CB  . SER   A 1 129 ? -29.232 -7.812  -10.879 1.00 44.15  ? 243 SER   A CB  1 
ATOM   1004 O  OG  . SER   A 1 129 ? -28.355 -6.831  -11.382 1.00 62.20  ? 243 SER   A OG  1 
ATOM   1005 N  N   . SER   A 1 130 ? -27.115 -9.802  -10.068 1.00 45.11  ? 244 SER   A N   1 
ATOM   1006 C  CA  . SER   A 1 130 ? -25.766 -10.309 -10.256 1.00 51.00  ? 244 SER   A CA  1 
ATOM   1007 C  C   . SER   A 1 130 ? -25.455 -10.377 -11.742 1.00 45.76  ? 244 SER   A C   1 
ATOM   1008 O  O   . SER   A 1 130 ? -26.346 -10.586 -12.569 1.00 43.59  ? 244 SER   A O   1 
ATOM   1009 C  CB  . SER   A 1 130 ? -25.569 -11.694 -9.642  1.00 50.68  ? 244 SER   A CB  1 
ATOM   1010 O  OG  . SER   A 1 130 ? -26.693 -12.512 -9.889  1.00 70.15  ? 244 SER   A OG  1 
ATOM   1011 N  N   . VAL   A 1 131 ? -24.175 -10.202 -12.061 1.00 44.14  ? 245 VAL   A N   1 
ATOM   1012 C  CA  . VAL   A 1 131 ? -23.689 -10.141 -13.430 1.00 43.01  ? 245 VAL   A CA  1 
ATOM   1013 C  C   . VAL   A 1 131 ? -22.269 -10.674 -13.418 1.00 43.01  ? 245 VAL   A C   1 
ATOM   1014 O  O   . VAL   A 1 131 ? -21.592 -10.667 -12.391 1.00 42.73  ? 245 VAL   A O   1 
ATOM   1015 C  CB  . VAL   A 1 131 ? -23.728 -8.705  -13.993 1.00 48.95  ? 245 VAL   A CB  1 
ATOM   1016 C  CG1 . VAL   A 1 131 ? -25.148 -8.163  -13.966 1.00 47.20  ? 245 VAL   A CG1 1 
ATOM   1017 C  CG2 . VAL   A 1 131 ? -22.756 -7.784  -13.250 1.00 39.30  ? 245 VAL   A CG2 1 
ATOM   1018 N  N   . GLN   A 1 132 ? -21.844 -11.194 -14.564 1.00 44.73  ? 246 GLN   A N   1 
ATOM   1019 C  CA  . GLN   A 1 132 ? -20.485 -11.672 -14.733 1.00 47.05  ? 246 GLN   A CA  1 
ATOM   1020 C  C   . GLN   A 1 132 ? -19.540 -10.534 -15.092 1.00 43.43  ? 246 GLN   A C   1 
ATOM   1021 O  O   . GLN   A 1 132 ? -18.349 -10.590 -14.766 1.00 42.90  ? 246 GLN   A O   1 
ATOM   1022 C  CB  . GLN   A 1 132 ? -20.481 -12.765 -15.805 1.00 46.06  ? 246 GLN   A CB  1 
ATOM   1023 C  CG  . GLN   A 1 132 ? -20.308 -14.182 -15.256 1.00 75.54  ? 246 GLN   A CG  1 
ATOM   1024 C  CD  . GLN   A 1 132 ? -21.481 -14.655 -14.397 1.00 66.62  ? 246 GLN   A CD  1 
ATOM   1025 O  OE1 . GLN   A 1 132 ? -22.652 -14.496 -14.754 1.00 69.07  ? 246 GLN   A OE1 1 
ATOM   1026 N  NE2 . GLN   A 1 132 ? -21.162 -15.229 -13.246 1.00 68.89  ? 246 GLN   A NE2 1 
ATOM   1027 N  N   . CYS   A 1 133 ? -20.070 -9.483  -15.705 1.00 41.92  ? 247 CYS   A N   1 
ATOM   1028 C  CA  . CYS   A 1 133 ? -19.293 -8.358  -16.203 1.00 45.14  ? 247 CYS   A CA  1 
ATOM   1029 C  C   . CYS   A 1 133 ? -20.091 -7.084  -15.978 1.00 47.94  ? 247 CYS   A C   1 
ATOM   1030 O  O   . CYS   A 1 133 ? -21.327 -7.103  -15.921 1.00 39.60  ? 247 CYS   A O   1 
ATOM   1031 C  CB  . CYS   A 1 133 ? -18.955 -8.511  -17.712 1.00 43.33  ? 247 CYS   A CB  1 
ATOM   1032 S  SG  . CYS   A 1 133 ? -17.884 -9.959  -18.188 1.00 58.62  ? 247 CYS   A SG  1 
ATOM   1033 N  N   . THR   A 1 134 ? -19.369 -5.974  -15.842 1.00 33.41  ? 248 THR   A N   1 
ATOM   1034 C  CA  . THR   A 1 134 ? -20.015 -4.676  -15.867 1.00 40.23  ? 248 THR   A CA  1 
ATOM   1035 C  C   . THR   A 1 134 ? -20.443 -4.340  -17.294 1.00 40.85  ? 248 THR   A C   1 
ATOM   1036 O  O   . THR   A 1 134 ? -19.997 -4.961  -18.269 1.00 36.96  ? 248 THR   A O   1 
ATOM   1037 C  CB  . THR   A 1 134 ? -19.076 -3.586  -15.362 1.00 42.19  ? 248 THR   A CB  1 
ATOM   1038 O  OG1 . THR   A 1 134 ? -18.000 -3.406  -16.295 1.00 38.46  ? 248 THR   A OG1 1 
ATOM   1039 C  CG2 . THR   A 1 134 ? -18.496 -3.958  -14.041 1.00 35.98  ? 248 THR   A CG2 1 
ATOM   1040 N  N   . HIS   A 1 135 ? -21.308 -3.337  -17.427 1.00 37.09  ? 249 HIS   A N   1 
ATOM   1041 C  CA  . HIS   A 1 135 ? -21.475 -2.732  -18.740 1.00 43.01  ? 249 HIS   A CA  1 
ATOM   1042 C  C   . HIS   A 1 135 ? -20.138 -2.145  -19.222 1.00 40.57  ? 249 HIS   A C   1 
ATOM   1043 O  O   . HIS   A 1 135 ? -19.121 -2.172  -18.519 1.00 40.05  ? 249 HIS   A O   1 
ATOM   1044 C  CB  . HIS   A 1 135 ? -22.593 -1.677  -18.722 1.00 38.56  ? 249 HIS   A CB  1 
ATOM   1045 C  CG  . HIS   A 1 135 ? -22.232 -0.367  -18.091 1.00 39.37  ? 249 HIS   A CG  1 
ATOM   1046 N  ND1 . HIS   A 1 135 ? -22.382 -0.121  -16.745 1.00 45.49  ? 249 HIS   A ND1 1 
ATOM   1047 C  CD2 . HIS   A 1 135 ? -21.824 0.805   -18.643 1.00 46.67  ? 249 HIS   A CD2 1 
ATOM   1048 C  CE1 . HIS   A 1 135 ? -22.037 1.128   -16.488 1.00 54.50  ? 249 HIS   A CE1 1 
ATOM   1049 N  NE2 . HIS   A 1 135 ? -21.696 1.713   -17.624 1.00 40.94  ? 249 HIS   A NE2 1 
ATOM   1050 N  N   . GLY   A 1 136 ? -20.143 -1.604  -20.441 1.00 43.16  ? 250 GLY   A N   1 
ATOM   1051 C  CA  . GLY   A 1 136 ? -18.910 -1.120  -21.041 1.00 41.29  ? 250 GLY   A CA  1 
ATOM   1052 C  C   . GLY   A 1 136 ? -18.664 0.326   -20.672 1.00 44.25  ? 250 GLY   A C   1 
ATOM   1053 O  O   . GLY   A 1 136 ? -19.520 1.200   -20.917 1.00 47.78  ? 250 GLY   A O   1 
ATOM   1054 N  N   . ILE   A 1 137 ? -17.507 0.624   -20.099 1.00 39.75  ? 251 ILE   A N   1 
ATOM   1055 C  CA  . ILE   A 1 137 ? -17.210 1.946   -19.580 1.00 41.48  ? 251 ILE   A CA  1 
ATOM   1056 C  C   . ILE   A 1 137 ? -16.089 2.545   -20.413 1.00 40.20  ? 251 ILE   A C   1 
ATOM   1057 O  O   . ILE   A 1 137 ? -15.008 1.955   -20.516 1.00 43.37  ? 251 ILE   A O   1 
ATOM   1058 C  CB  . ILE   A 1 137 ? -16.807 1.892   -18.097 1.00 47.56  ? 251 ILE   A CB  1 
ATOM   1059 C  CG1 . ILE   A 1 137 ? -17.997 1.424   -17.247 1.00 48.97  ? 251 ILE   A CG1 1 
ATOM   1060 C  CG2 . ILE   A 1 137 ? -16.334 3.251   -17.635 1.00 32.21  ? 251 ILE   A CG2 1 
ATOM   1061 C  CD1 . ILE   A 1 137 ? -17.635 0.464   -16.141 1.00 38.90  ? 251 ILE   A CD1 1 
ATOM   1062 N  N   . LYS   A 1 138 ? -16.325 3.717   -20.970 1.00 33.76  ? 252 LYS   A N   1 
ATOM   1063 C  CA  . LYS   A 1 138 ? -15.289 4.409   -21.728 1.00 37.42  ? 252 LYS   A CA  1 
ATOM   1064 C  C   . LYS   A 1 138 ? -14.348 5.108   -20.768 1.00 40.13  ? 252 LYS   A C   1 
ATOM   1065 O  O   . LYS   A 1 138 ? -14.800 5.928   -19.957 1.00 41.63  ? 252 LYS   A O   1 
ATOM   1066 C  CB  . LYS   A 1 138 ? -15.914 5.418   -22.666 1.00 37.93  ? 252 LYS   A CB  1 
ATOM   1067 C  CG  . LYS   A 1 138 ? -16.467 4.833   -23.930 1.00 46.53  ? 252 LYS   A CG  1 
ATOM   1068 C  CD  . LYS   A 1 138 ? -17.206 5.913   -24.691 1.00 49.48  ? 252 LYS   A CD  1 
ATOM   1069 C  CE  . LYS   A 1 138 ? -17.344 5.575   -26.177 1.00 48.77  ? 252 LYS   A CE  1 
ATOM   1070 N  NZ  . LYS   A 1 138 ? -17.489 6.831   -27.039 1.00 55.29  ? 252 LYS   A NZ  1 
ATOM   1071 N  N   . PRO   A 1 139 ? -13.051 4.815   -20.790 1.00 39.00  ? 253 PRO   A N   1 
ATOM   1072 C  CA  . PRO   A 1 139 ? -12.074 5.429   -19.860 1.00 40.98  ? 253 PRO   A CA  1 
ATOM   1073 C  C   . PRO   A 1 139 ? -11.666 6.824   -20.321 1.00 39.99  ? 253 PRO   A C   1 
ATOM   1074 O  O   . PRO   A 1 139 ? -10.576 7.062   -20.820 1.00 40.44  ? 253 PRO   A O   1 
ATOM   1075 C  CB  . PRO   A 1 139 ? -10.897 4.454   -19.913 1.00 42.88  ? 253 PRO   A CB  1 
ATOM   1076 C  CG  . PRO   A 1 139 ? -10.926 3.920   -21.323 1.00 34.51  ? 253 PRO   A CG  1 
ATOM   1077 C  CD  . PRO   A 1 139 ? -12.411 3.825   -21.678 1.00 34.50  ? 253 PRO   A CD  1 
ATOM   1078 N  N   . VAL   A 1 140 ? -12.578 7.769   -20.153 1.00 35.38  ? 254 VAL   A N   1 
ATOM   1079 C  CA  . VAL   A 1 140 ? -12.381 9.144   -20.588 1.00 39.28  ? 254 VAL   A CA  1 
ATOM   1080 C  C   . VAL   A 1 140 ? -11.639 9.911   -19.494 1.00 37.04  ? 254 VAL   A C   1 
ATOM   1081 O  O   . VAL   A 1 140 ? -12.127 10.033  -18.368 1.00 41.29  ? 254 VAL   A O   1 
ATOM   1082 C  CB  . VAL   A 1 140 ? -13.735 9.786   -20.916 1.00 48.75  ? 254 VAL   A CB  1 
ATOM   1083 C  CG1 . VAL   A 1 140 ? -13.566 11.198  -21.428 1.00 39.47  ? 254 VAL   A CG1 1 
ATOM   1084 C  CG2 . VAL   A 1 140 ? -14.453 8.903   -21.944 1.00 38.67  ? 254 VAL   A CG2 1 
ATOM   1085 N  N   . VAL   A 1 141 ? -10.456 10.423  -19.815 1.00 41.82  ? 255 VAL   A N   1 
ATOM   1086 C  CA  . VAL   A 1 141 ? -9.658  11.194  -18.858 1.00 42.91  ? 255 VAL   A CA  1 
ATOM   1087 C  C   . VAL   A 1 141 ? -10.022 12.665  -18.997 1.00 39.12  ? 255 VAL   A C   1 
ATOM   1088 O  O   . VAL   A 1 141 ? -9.911  13.218  -20.094 1.00 40.55  ? 255 VAL   A O   1 
ATOM   1089 C  CB  . VAL   A 1 141 ? -8.152  10.991  -19.094 1.00 51.60  ? 255 VAL   A CB  1 
ATOM   1090 C  CG1 . VAL   A 1 141 ? -7.306  12.047  -18.310 1.00 39.33  ? 255 VAL   A CG1 1 
ATOM   1091 C  CG2 . VAL   A 1 141 ? -7.749  9.572   -18.740 1.00 41.88  ? 255 VAL   A CG2 1 
ATOM   1092 N  N   . SER   A 1 142 ? -10.438 13.303  -17.897 1.00 33.21  ? 256 SER   A N   1 
ATOM   1093 C  CA  . SER   A 1 142 ? -10.816 14.717  -17.927 1.00 38.42  ? 256 SER   A CA  1 
ATOM   1094 C  C   . SER   A 1 142 ? -10.873 15.293  -16.522 1.00 38.45  ? 256 SER   A C   1 
ATOM   1095 O  O   . SER   A 1 142 ? -10.929 14.562  -15.529 1.00 39.09  ? 256 SER   A O   1 
ATOM   1096 C  CB  . SER   A 1 142 ? -12.171 14.934  -18.587 1.00 30.80  ? 256 SER   A CB  1 
ATOM   1097 O  OG  . SER   A 1 142 ? -13.188 14.532  -17.698 1.00 37.36  ? 256 SER   A OG  1 
ATOM   1098 N  N   . THR   A 1 143 ? -10.918 16.634  -16.470 1.00 34.10  ? 257 THR   A N   1 
ATOM   1099 C  CA  . THR   A 1 143 ? -11.159 17.392  -15.245 1.00 38.11  ? 257 THR   A CA  1 
ATOM   1100 C  C   . THR   A 1 143 ? -12.424 18.235  -15.389 1.00 35.22  ? 257 THR   A C   1 
ATOM   1101 O  O   . THR   A 1 143 ? -12.894 18.502  -16.502 1.00 39.34  ? 257 THR   A O   1 
ATOM   1102 C  CB  . THR   A 1 143 ? -9.957  18.289  -14.905 1.00 37.93  ? 257 THR   A CB  1 
ATOM   1103 O  OG1 . THR   A 1 143 ? -9.777  19.267  -15.945 1.00 39.93  ? 257 THR   A OG1 1 
ATOM   1104 C  CG2 . THR   A 1 143 ? -8.695  17.434  -14.815 1.00 43.33  ? 257 THR   A CG2 1 
ATOM   1105 N  N   . GLN   A 1 144 ? -12.993 18.600  -14.234 1.00 37.80  ? 258 GLN   A N   1 
ATOM   1106 C  CA  . GLN   A 1 144 ? -14.138 19.494  -14.052 1.00 36.87  ? 258 GLN   A CA  1 
ATOM   1107 C  C   . GLN   A 1 144 ? -15.452 18.905  -14.572 1.00 39.36  ? 258 GLN   A C   1 
ATOM   1108 O  O   . GLN   A 1 144 ? -16.462 18.915  -13.847 1.00 36.31  ? 258 GLN   A O   1 
ATOM   1109 C  CB  . GLN   A 1 144 ? -13.879 20.851  -14.717 1.00 41.07  ? 258 GLN   A CB  1 
ATOM   1110 C  CG  . GLN   A 1 144 ? -12.600 21.570  -14.299 1.00 36.61  ? 258 GLN   A CG  1 
ATOM   1111 C  CD  . GLN   A 1 144 ? -12.700 23.071  -14.601 1.00 46.32  ? 258 GLN   A CD  1 
ATOM   1112 O  OE1 . GLN   A 1 144 ? -13.724 23.529  -15.105 1.00 35.70  ? 258 GLN   A OE1 1 
ATOM   1113 N  NE2 . GLN   A 1 144 ? -11.641 23.830  -14.304 1.00 39.59  ? 258 GLN   A NE2 1 
ATOM   1114 N  N   . LEU   A 1 145 ? -15.447 18.398  -15.814 1.00 37.68  ? 259 LEU   A N   1 
ATOM   1115 C  CA  . LEU   A 1 145 ? -16.615 17.780  -16.446 1.00 37.76  ? 259 LEU   A CA  1 
ATOM   1116 C  C   . LEU   A 1 145 ? -16.327 16.326  -16.778 1.00 36.09  ? 259 LEU   A C   1 
ATOM   1117 O  O   . LEU   A 1 145 ? -15.279 16.008  -17.348 1.00 42.11  ? 259 LEU   A O   1 
ATOM   1118 C  CB  . LEU   A 1 145 ? -17.011 18.476  -17.741 1.00 33.34  ? 259 LEU   A CB  1 
ATOM   1119 C  CG  . LEU   A 1 145 ? -17.199 19.978  -17.625 1.00 37.90  ? 259 LEU   A CG  1 
ATOM   1120 C  CD1 . LEU   A 1 145 ? -17.322 20.586  -19.023 1.00 35.78  ? 259 LEU   A CD1 1 
ATOM   1121 C  CD2 . LEU   A 1 145 ? -18.408 20.282  -16.760 1.00 37.01  ? 259 LEU   A CD2 1 
ATOM   1122 N  N   . LEU   A 1 146 ? -17.276 15.458  -16.452 1.00 35.45  ? 260 LEU   A N   1 
ATOM   1123 C  CA  . LEU   A 1 146 ? -17.239 14.062  -16.838 1.00 32.48  ? 260 LEU   A CA  1 
ATOM   1124 C  C   . LEU   A 1 146 ? -17.909 13.930  -18.201 1.00 38.48  ? 260 LEU   A C   1 
ATOM   1125 O  O   . LEU   A 1 146 ? -19.053 14.375  -18.386 1.00 36.09  ? 260 LEU   A O   1 
ATOM   1126 C  CB  . LEU   A 1 146 ? -17.964 13.212  -15.796 1.00 33.41  ? 260 LEU   A CB  1 
ATOM   1127 C  CG  . LEU   A 1 146 ? -17.424 13.318  -14.358 1.00 36.50  ? 260 LEU   A CG  1 
ATOM   1128 C  CD1 . LEU   A 1 146 ? -18.150 12.363  -13.409 1.00 39.64  ? 260 LEU   A CD1 1 
ATOM   1129 C  CD2 . LEU   A 1 146 ? -15.924 13.085  -14.350 1.00 35.97  ? 260 LEU   A CD2 1 
ATOM   1130 N  N   . LEU   A 1 147 ? -17.203 13.319  -19.148 1.00 35.16  ? 261 LEU   A N   1 
ATOM   1131 C  CA  . LEU   A 1 147 ? -17.623 13.284  -20.541 1.00 39.57  ? 261 LEU   A CA  1 
ATOM   1132 C  C   . LEU   A 1 147 ? -17.906 11.860  -21.009 1.00 42.36  ? 261 LEU   A C   1 
ATOM   1133 O  O   . LEU   A 1 147 ? -17.218 10.900  -20.636 1.00 37.24  ? 261 LEU   A O   1 
ATOM   1134 C  CB  . LEU   A 1 147 ? -16.574 13.883  -21.446 1.00 37.20  ? 261 LEU   A CB  1 
ATOM   1135 C  CG  . LEU   A 1 147 ? -16.084 15.276  -21.068 1.00 42.13  ? 261 LEU   A CG  1 
ATOM   1136 C  CD1 . LEU   A 1 147 ? -14.903 15.540  -21.975 1.00 44.10  ? 261 LEU   A CD1 1 
ATOM   1137 C  CD2 . LEU   A 1 147 ? -17.170 16.362  -21.234 1.00 39.06  ? 261 LEU   A CD2 1 
ATOM   1138 N  N   . ASN   A 1 148 ? -18.919 11.745  -21.864 1.00 35.44  ? 262 ASN   A N   1 
ATOM   1139 C  CA  . ASN   A 1 148 ? -19.186 10.519  -22.591 1.00 38.72  ? 262 ASN   A CA  1 
ATOM   1140 C  C   . ASN   A 1 148 ? -19.542 9.356   -21.668 1.00 44.93  ? 262 ASN   A C   1 
ATOM   1141 O  O   . ASN   A 1 148 ? -19.394 8.198   -22.036 1.00 43.60  ? 262 ASN   A O   1 
ATOM   1142 C  CB  . ASN   A 1 148 ? -17.993 10.170  -23.474 1.00 34.51  ? 262 ASN   A CB  1 
ATOM   1143 C  CG  . ASN   A 1 148 ? -18.022 10.931  -24.764 1.00 45.28  ? 262 ASN   A CG  1 
ATOM   1144 O  OD1 . ASN   A 1 148 ? -18.927 11.742  -24.995 1.00 43.33  ? 262 ASN   A OD1 1 
ATOM   1145 N  ND2 . ASN   A 1 148 ? -17.046 10.688  -25.618 1.00 42.30  ? 262 ASN   A ND2 1 
ATOM   1146 N  N   . GLY   A 1 149 ? -20.026 9.652   -20.472 1.00 44.82  ? 263 GLY   A N   1 
ATOM   1147 C  CA  . GLY   A 1 149 ? -20.390 8.643   -19.508 1.00 47.24  ? 263 GLY   A CA  1 
ATOM   1148 C  C   . GLY   A 1 149 ? -21.844 8.239   -19.632 1.00 53.99  ? 263 GLY   A C   1 
ATOM   1149 O  O   . GLY   A 1 149 ? -22.533 8.569   -20.611 1.00 43.69  ? 263 GLY   A O   1 
ATOM   1150 N  N   . SER   A 1 150 ? -22.316 7.491   -18.638 1.00 38.76  ? 264 SER   A N   1 
ATOM   1151 C  CA  . SER   A 1 150 ? -23.724 7.163   -18.476 1.00 45.86  ? 264 SER   A CA  1 
ATOM   1152 C  C   . SER   A 1 150 ? -24.445 8.260   -17.701 1.00 49.95  ? 264 SER   A C   1 
ATOM   1153 O  O   . SER   A 1 150 ? -23.832 9.030   -16.964 1.00 47.22  ? 264 SER   A O   1 
ATOM   1154 C  CB  . SER   A 1 150 ? -23.886 5.839   -17.738 1.00 58.79  ? 264 SER   A CB  1 
ATOM   1155 O  OG  . SER   A 1 150 ? -24.961 5.925   -16.827 1.00 72.75  ? 264 SER   A OG  1 
ATOM   1156 N  N   . LEU   A 1 151 ? -25.765 8.305   -17.846 1.00 41.74  ? 265 LEU   A N   1 
ATOM   1157 C  CA  . LEU   A 1 151 ? -26.578 9.284   -17.137 1.00 50.92  ? 265 LEU   A CA  1 
ATOM   1158 C  C   . LEU   A 1 151 ? -27.279 8.635   -15.943 1.00 52.15  ? 265 LEU   A C   1 
ATOM   1159 O  O   . LEU   A 1 151 ? -27.450 7.412   -15.879 1.00 47.81  ? 265 LEU   A O   1 
ATOM   1160 C  CB  . LEU   A 1 151 ? -27.623 9.908   -18.076 1.00 45.31  ? 265 LEU   A CB  1 
ATOM   1161 C  CG  . LEU   A 1 151 ? -27.102 10.803  -19.208 1.00 49.88  ? 265 LEU   A CG  1 
ATOM   1162 C  CD1 . LEU   A 1 151 ? -28.205 11.135  -20.248 1.00 54.30  ? 265 LEU   A CD1 1 
ATOM   1163 C  CD2 . LEU   A 1 151 ? -26.438 12.079  -18.680 1.00 40.23  ? 265 LEU   A CD2 1 
ATOM   1164 N  N   . ALA   A 1 152 ? -27.669 9.472   -14.981 1.00 45.48  ? 266 ALA   A N   1 
ATOM   1165 C  CA  . ALA   A 1 152 ? -28.563 9.021   -13.918 1.00 52.64  ? 266 ALA   A CA  1 
ATOM   1166 C  C   . ALA   A 1 152 ? -29.963 8.849   -14.495 1.00 52.97  ? 266 ALA   A C   1 
ATOM   1167 O  O   . ALA   A 1 152 ? -30.360 9.580   -15.404 1.00 56.47  ? 266 ALA   A O   1 
ATOM   1168 C  CB  . ALA   A 1 152 ? -28.577 10.014  -12.752 1.00 40.00  ? 266 ALA   A CB  1 
ATOM   1169 N  N   . GLU   A 1 153 ? -30.714 7.874   -13.968 1.00 55.32  ? 267 GLU   A N   1 
ATOM   1170 C  CA  . GLU   A 1 153 ? -31.947 7.436   -14.622 1.00 61.71  ? 267 GLU   A CA  1 
ATOM   1171 C  C   . GLU   A 1 153 ? -33.182 8.237   -14.206 1.00 61.73  ? 267 GLU   A C   1 
ATOM   1172 O  O   . GLU   A 1 153 ? -34.187 8.227   -14.927 1.00 56.66  ? 267 GLU   A O   1 
ATOM   1173 C  CB  . GLU   A 1 153 ? -32.181 5.951   -14.350 1.00 52.71  ? 267 GLU   A CB  1 
ATOM   1174 C  CG  . GLU   A 1 153 ? -31.599 5.007   -15.398 1.00 74.63  ? 267 GLU   A CG  1 
ATOM   1175 C  CD  . GLU   A 1 153 ? -30.079 4.862   -15.331 1.00 83.79  ? 267 GLU   A CD  1 
ATOM   1176 O  OE1 . GLU   A 1 153 ? -29.492 5.068   -14.243 1.00 84.60  ? 267 GLU   A OE1 1 
ATOM   1177 O  OE2 . GLU   A 1 153 ? -29.468 4.524   -16.377 1.00 93.26  ? 267 GLU   A OE2 1 
ATOM   1178 N  N   . GLU   A 1 154 ? -33.155 8.909   -13.052 1.00 57.09  ? 268 GLU   A N   1 
ATOM   1179 C  CA  . GLU   A 1 154 ? -34.315 9.648   -12.578 1.00 61.97  ? 268 GLU   A CA  1 
ATOM   1180 C  C   . GLU   A 1 154 ? -33.894 11.085  -12.383 1.00 54.45  ? 268 GLU   A C   1 
ATOM   1181 O  O   . GLU   A 1 154 ? -33.845 11.877  -13.332 1.00 49.69  ? 268 GLU   A O   1 
ATOM   1182 C  CB  . GLU   A 1 154 ? -34.874 9.060   -11.282 1.00 63.64  ? 268 GLU   A CB  1 
ATOM   1183 C  CG  . GLU   A 1 154 ? -36.189 8.308   -11.378 1.00 64.82  ? 268 GLU   A CG  1 
ATOM   1184 C  CD  . GLU   A 1 154 ? -36.583 7.683   -10.036 1.00 84.22  ? 268 GLU   A CD  1 
ATOM   1185 O  OE1 . GLU   A 1 154 ? -35.956 8.035   -9.010  1.00 83.39  ? 268 GLU   A OE1 1 
ATOM   1186 O  OE2 . GLU   A 1 154 ? -37.521 6.850   -9.995  1.00 88.49  ? 268 GLU   A OE2 1 
ATOM   1187 N  N   . GLU   A 1 155 ? -33.591 11.476  -11.145 1.00 50.04  ? 269 GLU   A N   1 
ATOM   1188 C  CA  . GLU   A 1 155 ? -33.213 12.824  -10.798 1.00 56.78  ? 269 GLU   A CA  1 
ATOM   1189 C  C   . GLU   A 1 155 ? -31.702 12.947  -10.843 1.00 53.63  ? 269 GLU   A C   1 
ATOM   1190 O  O   . GLU   A 1 155 ? -30.972 11.947  -10.870 1.00 47.41  ? 269 GLU   A O   1 
ATOM   1191 C  CB  . GLU   A 1 155 ? -33.740 13.171  -9.408  1.00 50.84  ? 269 GLU   A CB  1 
ATOM   1192 C  CG  . GLU   A 1 155 ? -35.156 12.690  -9.168  1.00 60.30  ? 269 GLU   A CG  1 
ATOM   1193 C  CD  . GLU   A 1 155 ? -35.993 13.668  -8.355  1.00 75.95  ? 269 GLU   A CD  1 
ATOM   1194 O  OE1 . GLU   A 1 155 ? -35.471 14.739  -7.980  1.00 82.27  ? 269 GLU   A OE1 1 
ATOM   1195 O  OE2 . GLU   A 1 155 ? -37.183 13.369  -8.091  1.00 85.00  ? 269 GLU   A OE2 1 
ATOM   1196 N  N   . ILE   A 1 156 ? -31.233 14.195  -10.892 1.00 52.20  ? 270 ILE   A N   1 
ATOM   1197 C  CA  . ILE   A 1 156 ? -29.816 14.456  -10.688 1.00 51.02  ? 270 ILE   A CA  1 
ATOM   1198 C  C   . ILE   A 1 156 ? -29.420 13.875  -9.342  1.00 50.02  ? 270 ILE   A C   1 
ATOM   1199 O  O   . ILE   A 1 156 ? -30.155 14.017  -8.357  1.00 50.76  ? 270 ILE   A O   1 
ATOM   1200 C  CB  . ILE   A 1 156 ? -29.529 15.963  -10.753 1.00 48.67  ? 270 ILE   A CB  1 
ATOM   1201 C  CG1 . ILE   A 1 156 ? -29.833 16.484  -12.162 1.00 50.20  ? 270 ILE   A CG1 1 
ATOM   1202 C  CG2 . ILE   A 1 156 ? -28.085 16.216  -10.382 1.00 50.13  ? 270 ILE   A CG2 1 
ATOM   1203 C  CD1 . ILE   A 1 156 ? -29.422 17.904  -12.430 1.00 53.91  ? 270 ILE   A CD1 1 
ATOM   1204 N  N   . ILE   A 1 157 ? -28.273 13.203  -9.288  1.00 44.86  ? 271 ILE   A N   1 
ATOM   1205 C  CA  . ILE   A 1 157 ? -27.760 12.596  -8.061  1.00 47.49  ? 271 ILE   A CA  1 
ATOM   1206 C  C   . ILE   A 1 157 ? -26.508 13.343  -7.624  1.00 37.33  ? 271 ILE   A C   1 
ATOM   1207 O  O   . ILE   A 1 157 ? -25.598 13.572  -8.430  1.00 39.19  ? 271 ILE   A O   1 
ATOM   1208 C  CB  . ILE   A 1 157 ? -27.443 11.092  -8.242  1.00 52.05  ? 271 ILE   A CB  1 
ATOM   1209 C  CG1 . ILE   A 1 157 ? -28.650 10.347  -8.776  1.00 43.41  ? 271 ILE   A CG1 1 
ATOM   1210 C  CG2 . ILE   A 1 157 ? -26.973 10.435  -6.908  1.00 39.81  ? 271 ILE   A CG2 1 
ATOM   1211 C  CD1 . ILE   A 1 157 ? -29.715 10.208  -7.758  1.00 51.73  ? 271 ILE   A CD1 1 
ATOM   1212 N  N   . ILE   A 1 158 ? -26.450 13.692  -6.343  1.00 39.54  ? 272 ILE   A N   1 
ATOM   1213 C  CA  . ILE   A 1 158 ? -25.248 14.227  -5.712  1.00 41.69  ? 272 ILE   A CA  1 
ATOM   1214 C  C   . ILE   A 1 158 ? -24.549 13.078  -4.998  1.00 50.55  ? 272 ILE   A C   1 
ATOM   1215 O  O   . ILE   A 1 158 ? -25.170 12.391  -4.175  1.00 49.32  ? 272 ILE   A O   1 
ATOM   1216 C  CB  . ILE   A 1 158 ? -25.587 15.349  -4.720  1.00 42.93  ? 272 ILE   A CB  1 
ATOM   1217 C  CG1 . ILE   A 1 158 ? -26.425 16.419  -5.415  1.00 42.06  ? 272 ILE   A CG1 1 
ATOM   1218 C  CG2 . ILE   A 1 158 ? -24.303 15.964  -4.197  1.00 52.51  ? 272 ILE   A CG2 1 
ATOM   1219 C  CD1 . ILE   A 1 158 ? -25.877 16.798  -6.758  1.00 36.59  ? 272 ILE   A CD1 1 
ATOM   1220 N  N   . ARG   A 1 159 ? -23.267 12.862  -5.314  1.00 39.14  ? 273 ARG   A N   1 
ATOM   1221 C  CA  . ARG   A 1 159 ? -22.463 11.777  -4.749  1.00 36.44  ? 273 ARG   A CA  1 
ATOM   1222 C  C   . ARG   A 1 159 ? -21.249 12.343  -4.022  1.00 37.76  ? 273 ARG   A C   1 
ATOM   1223 O  O   . ARG   A 1 159 ? -20.476 13.121  -4.595  1.00 39.16  ? 273 ARG   A O   1 
ATOM   1224 C  CB  . ARG   A 1 159 ? -21.979 10.796  -5.840  1.00 40.50  ? 273 ARG   A CB  1 
ATOM   1225 C  CG  . ARG   A 1 159 ? -23.103 10.245  -6.724  1.00 41.55  ? 273 ARG   A CG  1 
ATOM   1226 C  CD  . ARG   A 1 159 ? -22.606 9.357   -7.854  1.00 39.70  ? 273 ARG   A CD  1 
ATOM   1227 N  NE  . ARG   A 1 159 ? -23.657 9.060   -8.826  1.00 35.25  ? 273 ARG   A NE  1 
ATOM   1228 C  CZ  . ARG   A 1 159 ? -24.647 8.197   -8.620  1.00 40.88  ? 273 ARG   A CZ  1 
ATOM   1229 N  NH1 . ARG   A 1 159 ? -24.781 7.548   -7.473  1.00 42.46  ? 273 ARG   A NH1 1 
ATOM   1230 N  NH2 . ARG   A 1 159 ? -25.529 7.976   -9.583  1.00 44.52  ? 273 ARG   A NH2 1 
ATOM   1231 N  N   . SER   A 1 160 ? -21.060 11.914  -2.778  1.00 42.96  ? 274 SER   A N   1 
ATOM   1232 C  CA  . SER   A 1 160 ? -19.902 12.300  -1.985  1.00 43.38  ? 274 SER   A CA  1 
ATOM   1233 C  C   . SER   A 1 160 ? -19.691 11.280  -0.884  1.00 40.88  ? 274 SER   A C   1 
ATOM   1234 O  O   . SER   A 1 160 ? -20.667 10.827  -0.279  1.00 39.01  ? 274 SER   A O   1 
ATOM   1235 C  CB  . SER   A 1 160 ? -20.073 13.691  -1.348  1.00 46.52  ? 274 SER   A CB  1 
ATOM   1236 O  OG  . SER   A 1 160 ? -18.970 13.954  -0.498  1.00 42.36  ? 274 SER   A OG  1 
ATOM   1237 N  N   . GLU   A 1 161 ? -18.414 10.962  -0.601  1.00 43.72  ? 275 GLU   A N   1 
ATOM   1238 C  CA  . GLU   A 1 161 ? -18.091 10.139  0.563   1.00 43.87  ? 275 GLU   A CA  1 
ATOM   1239 C  C   . GLU   A 1 161 ? -18.628 10.761  1.835   1.00 43.84  ? 275 GLU   A C   1 
ATOM   1240 O  O   . GLU   A 1 161 ? -19.016 10.043  2.755   1.00 47.80  ? 275 GLU   A O   1 
ATOM   1241 C  CB  . GLU   A 1 161 ? -16.583 9.941   0.711   1.00 39.19  ? 275 GLU   A CB  1 
ATOM   1242 C  CG  . GLU   A 1 161 ? -16.243 8.886   1.781   1.00 44.82  ? 275 GLU   A CG  1 
ATOM   1243 C  CD  . GLU   A 1 161 ? -14.791 8.390   1.720   1.00 57.93  ? 275 GLU   A CD  1 
ATOM   1244 O  OE1 . GLU   A 1 161 ? -13.920 9.169   1.269   1.00 55.63  ? 275 GLU   A OE1 1 
ATOM   1245 O  OE2 . GLU   A 1 161 ? -14.523 7.213   2.093   1.00 59.63  ? 275 GLU   A OE2 1 
ATOM   1246 N  N   . ASN   A 1 162 ? -18.696 12.090  1.889   1.00 45.75  ? 276 ASN   A N   1 
ATOM   1247 C  CA  . ASN   A 1 162 ? -19.148 12.782  3.088   1.00 50.17  ? 276 ASN   A CA  1 
ATOM   1248 C  C   . ASN   A 1 162 ? -19.358 14.267  2.810   1.00 45.05  ? 276 ASN   A C   1 
ATOM   1249 O  O   . ASN   A 1 162 ? -18.406 15.050  2.838   1.00 43.77  ? 276 ASN   A O   1 
ATOM   1250 C  CB  . ASN   A 1 162 ? -18.153 12.579  4.233   1.00 47.52  ? 276 ASN   A CB  1 
ATOM   1251 C  CG  . ASN   A 1 162 ? -18.554 13.328  5.482   1.00 61.94  ? 276 ASN   A CG  1 
ATOM   1252 O  OD1 . ASN   A 1 162 ? -19.608 13.967  5.514   1.00 59.39  ? 276 ASN   A OD1 1 
ATOM   1253 N  ND2 . ASN   A 1 162 ? -17.723 13.253  6.524   1.00 65.41  ? 276 ASN   A ND2 1 
ATOM   1254 N  N   . LEU   A 1 163 ? -20.616 14.644  2.567   1.00 43.39  ? 277 LEU   A N   1 
ATOM   1255 C  CA  . LEU   A 1 163 ? -20.969 15.998  2.154   1.00 46.55  ? 277 LEU   A CA  1 
ATOM   1256 C  C   . LEU   A 1 163 ? -20.501 17.039  3.157   1.00 52.60  ? 277 LEU   A C   1 
ATOM   1257 O  O   . LEU   A 1 163 ? -20.139 18.157  2.774   1.00 60.36  ? 277 LEU   A O   1 
ATOM   1258 C  CB  . LEU   A 1 163 ? -22.487 16.081  1.972   1.00 43.15  ? 277 LEU   A CB  1 
ATOM   1259 C  CG  . LEU   A 1 163 ? -23.014 16.604  0.637   1.00 52.10  ? 277 LEU   A CG  1 
ATOM   1260 C  CD1 . LEU   A 1 163 ? -22.106 16.094  -0.470  1.00 53.52  ? 277 LEU   A CD1 1 
ATOM   1261 C  CD2 . LEU   A 1 163 ? -24.461 16.169  0.389   1.00 49.82  ? 277 LEU   A CD2 1 
ATOM   1262 N  N   . THR   A 1 164 ? -20.502 16.693  4.444   1.00 55.02  ? 278 THR   A N   1 
ATOM   1263 C  CA  . THR   A 1 164 ? -20.171 17.665  5.479   1.00 57.06  ? 278 THR   A CA  1 
ATOM   1264 C  C   . THR   A 1 164 ? -18.699 18.041  5.442   1.00 64.62  ? 278 THR   A C   1 
ATOM   1265 O  O   . THR   A 1 164 ? -18.327 19.127  5.907   1.00 60.32  ? 278 THR   A O   1 
ATOM   1266 C  CB  . THR   A 1 164 ? -20.531 17.108  6.854   1.00 52.98  ? 278 THR   A CB  1 
ATOM   1267 O  OG1 . THR   A 1 164 ? -21.957 17.133  7.030   1.00 63.98  ? 278 THR   A OG1 1 
ATOM   1268 C  CG2 . THR   A 1 164 ? -19.875 17.931  7.942   1.00 67.30  ? 278 THR   A CG2 1 
ATOM   1269 N  N   . ASN   A 1 165 ? -17.850 17.150  4.922   1.00 50.74  ? 279 ASN   A N   1 
ATOM   1270 C  CA  . ASN   A 1 165 ? -16.418 17.410  4.843   1.00 49.13  ? 279 ASN   A CA  1 
ATOM   1271 C  C   . ASN   A 1 165 ? -16.133 18.109  3.517   1.00 57.52  ? 279 ASN   A C   1 
ATOM   1272 O  O   . ASN   A 1 165 ? -16.440 17.582  2.439   1.00 64.13  ? 279 ASN   A O   1 
ATOM   1273 C  CB  . ASN   A 1 165 ? -15.619 16.115  4.966   1.00 47.14  ? 279 ASN   A CB  1 
ATOM   1274 C  CG  . ASN   A 1 165 ? -14.115 16.342  4.913   1.00 50.98  ? 279 ASN   A CG  1 
ATOM   1275 O  OD1 . ASN   A 1 165 ? -13.637 17.385  4.458   1.00 53.38  ? 279 ASN   A OD1 1 
ATOM   1276 N  ND2 . ASN   A 1 165 ? -13.357 15.342  5.359   1.00 51.18  ? 279 ASN   A ND2 1 
ATOM   1277 N  N   . ASN   A 1 166 ? -15.546 19.298  3.598   1.00 58.04  ? 280 ASN   A N   1 
ATOM   1278 C  CA  . ASN   A 1 166 ? -15.410 20.156  2.432   1.00 68.04  ? 280 ASN   A CA  1 
ATOM   1279 C  C   . ASN   A 1 166 ? -14.317 19.673  1.500   1.00 60.78  ? 280 ASN   A C   1 
ATOM   1280 O  O   . ASN   A 1 166 ? -14.364 19.974  0.303   1.00 65.80  ? 280 ASN   A O   1 
ATOM   1281 C  CB  . ASN   A 1 166 ? -15.129 21.580  2.906   1.00 64.29  ? 280 ASN   A CB  1 
ATOM   1282 C  CG  . ASN   A 1 166 ? -13.717 21.725  3.417   1.00 69.23  ? 280 ASN   A CG  1 
ATOM   1283 O  OD1 . ASN   A 1 166 ? -12.813 22.140  2.688   1.00 81.40  ? 280 ASN   A OD1 1 
ATOM   1284 N  ND2 . ASN   A 1 166 ? -13.497 21.279  4.649   1.00 62.59  ? 280 ASN   A ND2 1 
ATOM   1285 N  N   . ALA   A 1 167 ? -13.332 18.942  2.013   1.00 57.19  ? 281 ALA   A N   1 
ATOM   1286 C  CA  . ALA   A 1 167 ? -12.286 18.412  1.152   1.00 63.28  ? 281 ALA   A CA  1 
ATOM   1287 C  C   . ALA   A 1 167 ? -12.727 17.180  0.372   1.00 60.28  ? 281 ALA   A C   1 
ATOM   1288 O  O   . ALA   A 1 167 ? -11.909 16.604  -0.343  1.00 71.71  ? 281 ALA   A O   1 
ATOM   1289 C  CB  . ALA   A 1 167 ? -11.033 18.080  1.975   1.00 52.24  ? 281 ALA   A CB  1 
ATOM   1290 N  N   . LYS   A 1 168 ? -13.979 16.748  0.491   1.00 55.63  ? 282 LYS   A N   1 
ATOM   1291 C  CA  . LYS   A 1 168 ? -14.442 15.551  -0.208  1.00 57.10  ? 282 LYS   A CA  1 
ATOM   1292 C  C   . LYS   A 1 168 ? -15.034 15.967  -1.554  1.00 49.00  ? 282 LYS   A C   1 
ATOM   1293 O  O   . LYS   A 1 168 ? -15.993 16.751  -1.592  1.00 52.55  ? 282 LYS   A O   1 
ATOM   1294 C  CB  . LYS   A 1 168 ? -15.476 14.789  0.633   1.00 51.77  ? 282 LYS   A CB  1 
ATOM   1295 C  CG  . LYS   A 1 168 ? -14.901 13.767  1.641   1.00 48.04  ? 282 LYS   A CG  1 
ATOM   1296 C  CD  . LYS   A 1 168 ? -13.745 12.958  1.029   1.00 70.92  ? 282 LYS   A CD  1 
ATOM   1297 C  CE  . LYS   A 1 168 ? -12.766 12.385  2.071   1.00 66.41  ? 282 LYS   A CE  1 
ATOM   1298 N  NZ  . LYS   A 1 168 ? -12.079 11.156  1.537   1.00 54.62  ? 282 LYS   A NZ  1 
ATOM   1299 N  N   . THR   A 1 169 ? -14.460 15.460  -2.655  1.00 57.35  ? 283 THR   A N   1 
ATOM   1300 C  CA  . THR   A 1 169 ? -14.947 15.814  -3.989  1.00 40.22  ? 283 THR   A CA  1 
ATOM   1301 C  C   . THR   A 1 169 ? -16.405 15.408  -4.118  1.00 46.30  ? 283 THR   A C   1 
ATOM   1302 O  O   . THR   A 1 169 ? -16.802 14.337  -3.651  1.00 40.12  ? 283 THR   A O   1 
ATOM   1303 C  CB  . THR   A 1 169 ? -14.141 15.106  -5.085  1.00 54.48  ? 283 THR   A CB  1 
ATOM   1304 O  OG1 . THR   A 1 169 ? -12.767 14.980  -4.708  1.00 65.11  ? 283 THR   A OG1 1 
ATOM   1305 C  CG2 . THR   A 1 169 ? -14.224 15.857  -6.407  1.00 53.01  ? 283 THR   A CG2 1 
ATOM   1306 N  N   . ILE   A 1 170 ? -17.205 16.258  -4.761  1.00 35.01  ? 284 ILE   A N   1 
ATOM   1307 C  CA  . ILE   A 1 170 ? -18.610 15.965  -5.018  1.00 41.09  ? 284 ILE   A CA  1 
ATOM   1308 C  C   . ILE   A 1 170 ? -18.769 15.600  -6.488  1.00 45.82  ? 284 ILE   A C   1 
ATOM   1309 O  O   . ILE   A 1 170 ? -18.218 16.277  -7.364  1.00 37.53  ? 284 ILE   A O   1 
ATOM   1310 C  CB  . ILE   A 1 170 ? -19.516 17.149  -4.652  1.00 41.71  ? 284 ILE   A CB  1 
ATOM   1311 C  CG1 . ILE   A 1 170 ? -19.441 17.404  -3.152  1.00 38.09  ? 284 ILE   A CG1 1 
ATOM   1312 C  CG2 . ILE   A 1 170 ? -20.970 16.893  -5.118  1.00 42.01  ? 284 ILE   A CG2 1 
ATOM   1313 C  CD1 . ILE   A 1 170 ? -19.888 18.805  -2.799  1.00 44.73  ? 284 ILE   A CD1 1 
ATOM   1314 N  N   . ILE   A 1 171 ? -19.494 14.516  -6.759  1.00 44.28  ? 285 ILE   A N   1 
ATOM   1315 C  CA  . ILE   A 1 171 ? -19.824 14.105  -8.122  1.00 38.88  ? 285 ILE   A CA  1 
ATOM   1316 C  C   . ILE   A 1 171 ? -21.290 14.409  -8.324  1.00 43.03  ? 285 ILE   A C   1 
ATOM   1317 O  O   . ILE   A 1 171 ? -22.141 13.853  -7.622  1.00 40.61  ? 285 ILE   A O   1 
ATOM   1318 C  CB  . ILE   A 1 171 ? -19.604 12.611  -8.374  1.00 36.35  ? 285 ILE   A CB  1 
ATOM   1319 C  CG1 . ILE   A 1 171 ? -18.160 12.236  -8.134  1.00 37.38  ? 285 ILE   A CG1 1 
ATOM   1320 C  CG2 . ILE   A 1 171 ? -19.995 12.299  -9.844  1.00 34.94  ? 285 ILE   A CG2 1 
ATOM   1321 C  CD1 . ILE   A 1 171 ? -17.822 10.814  -8.596  1.00 42.61  ? 285 ILE   A CD1 1 
ATOM   1322 N  N   . VAL   A 1 172 ? -21.583 15.274  -9.275  1.00 36.06  ? 286 VAL   A N   1 
ATOM   1323 C  CA  . VAL   A 1 172 ? -22.948 15.504  -9.717  1.00 38.63  ? 286 VAL   A CA  1 
ATOM   1324 C  C   . VAL   A 1 172 ? -23.177 14.624  -10.932 1.00 36.34  ? 286 VAL   A C   1 
ATOM   1325 O  O   . VAL   A 1 172 ? -22.489 14.769  -11.942 1.00 40.17  ? 286 VAL   A O   1 
ATOM   1326 C  CB  . VAL   A 1 172 ? -23.181 16.978  -10.074 1.00 35.82  ? 286 VAL   A CB  1 
ATOM   1327 C  CG1 . VAL   A 1 172 ? -24.546 17.140  -10.663 1.00 34.95  ? 286 VAL   A CG1 1 
ATOM   1328 C  CG2 . VAL   A 1 172 ? -22.966 17.867  -8.868  1.00 35.82  ? 286 VAL   A CG2 1 
ATOM   1329 N  N   . HIS   A 1 173 ? -24.143 13.732  -10.843 1.00 39.88  ? 287 HIS   A N   1 
ATOM   1330 C  CA  . HIS   A 1 173 ? -24.513 12.855  -11.939 1.00 38.30  ? 287 HIS   A CA  1 
ATOM   1331 C  C   . HIS   A 1 173 ? -25.753 13.444  -12.612 1.00 35.21  ? 287 HIS   A C   1 
ATOM   1332 O  O   . HIS   A 1 173 ? -26.834 13.460  -12.021 1.00 41.44  ? 287 HIS   A O   1 
ATOM   1333 C  CB  . HIS   A 1 173 ? -24.759 11.441  -11.409 1.00 31.79  ? 287 HIS   A CB  1 
ATOM   1334 C  CG  . HIS   A 1 173 ? -24.641 10.382  -12.451 1.00 40.04  ? 287 HIS   A CG  1 
ATOM   1335 N  ND1 . HIS   A 1 173 ? -24.943 9.058   -12.205 1.00 49.88  ? 287 HIS   A ND1 1 
ATOM   1336 C  CD2 . HIS   A 1 173 ? -24.258 10.447  -13.746 1.00 36.99  ? 287 HIS   A CD2 1 
ATOM   1337 C  CE1 . HIS   A 1 173 ? -24.743 8.354   -13.306 1.00 49.40  ? 287 HIS   A CE1 1 
ATOM   1338 N  NE2 . HIS   A 1 173 ? -24.319 9.173   -14.252 1.00 42.43  ? 287 HIS   A NE2 1 
ATOM   1339 N  N   . LEU   A 1 174 ? -25.599 13.926  -13.845 1.00 41.97  ? 288 LEU   A N   1 
ATOM   1340 C  CA  . LEU   A 1 174 ? -26.709 14.523  -14.585 1.00 44.75  ? 288 LEU   A CA  1 
ATOM   1341 C  C   . LEU   A 1 174 ? -27.685 13.445  -15.049 1.00 43.94  ? 288 LEU   A C   1 
ATOM   1342 O  O   . LEU   A 1 174 ? -27.316 12.278  -15.210 1.00 43.08  ? 288 LEU   A O   1 
ATOM   1343 C  CB  . LEU   A 1 174 ? -26.177 15.320  -15.790 1.00 34.88  ? 288 LEU   A CB  1 
ATOM   1344 C  CG  . LEU   A 1 174 ? -25.199 16.451  -15.440 1.00 40.15  ? 288 LEU   A CG  1 
ATOM   1345 C  CD1 . LEU   A 1 174 ? -24.704 17.193  -16.659 1.00 35.96  ? 288 LEU   A CD1 1 
ATOM   1346 C  CD2 . LEU   A 1 174 ? -25.846 17.452  -14.433 1.00 43.97  ? 288 LEU   A CD2 1 
ATOM   1347 N  N   . ASN   A 1 175 ? -28.949 13.838  -15.242 1.00 42.40  ? 289 ASN   A N   1 
ATOM   1348 C  CA  . ASN   A 1 175 ? -29.929 12.994  -15.926 1.00 51.95  ? 289 ASN   A CA  1 
ATOM   1349 C  C   . ASN   A 1 175 ? -30.204 13.447  -17.356 1.00 45.32  ? 289 ASN   A C   1 
ATOM   1350 O  O   . ASN   A 1 175 ? -31.015 12.821  -18.048 1.00 47.30  ? 289 ASN   A O   1 
ATOM   1351 C  CB  . ASN   A 1 175 ? -31.258 12.931  -15.159 1.00 49.21  ? 289 ASN   A CB  1 
ATOM   1352 C  CG  . ASN   A 1 175 ? -31.887 14.308  -14.930 1.00 58.74  ? 289 ASN   A CG  1 
ATOM   1353 O  OD1 . ASN   A 1 175 ? -31.414 15.320  -15.450 1.00 49.39  ? 289 ASN   A OD1 1 
ATOM   1354 N  ND2 . ASN   A 1 175 ? -32.975 14.338  -14.150 1.00 53.72  ? 289 ASN   A ND2 1 
ATOM   1355 N  N   . LYS   A 1 176 ? -29.559 14.515  -17.814 1.00 46.20  ? 290 LYS   A N   1 
ATOM   1356 C  CA  . LYS   A 1 176 ? -29.713 14.965  -19.192 1.00 50.22  ? 290 LYS   A CA  1 
ATOM   1357 C  C   . LYS   A 1 176 ? -28.366 15.448  -19.689 1.00 42.18  ? 290 LYS   A C   1 
ATOM   1358 O  O   . LYS   A 1 176 ? -27.771 16.340  -19.087 1.00 46.72  ? 290 LYS   A O   1 
ATOM   1359 C  CB  . LYS   A 1 176 ? -30.761 16.077  -19.324 1.00 54.75  ? 290 LYS   A CB  1 
ATOM   1360 C  CG  . LYS   A 1 176 ? -30.760 16.769  -20.695 1.00 65.34  ? 290 LYS   A CG  1 
ATOM   1361 C  CD  . LYS   A 1 176 ? -32.009 16.445  -21.503 1.00 72.72  ? 290 LYS   A CD  1 
ATOM   1362 C  CE  . LYS   A 1 176 ? -32.348 17.569  -22.470 1.00 70.14  ? 290 LYS   A CE  1 
ATOM   1363 N  NZ  . LYS   A 1 176 ? -32.648 17.036  -23.818 1.00 77.97  ? 290 LYS   A NZ  1 
ATOM   1364 N  N   . SER   A 1 177 ? -27.888 14.873  -20.783 1.00 44.75  ? 291 SER   A N   1 
ATOM   1365 C  CA  . SER   A 1 177 ? -26.564 15.234  -21.242 1.00 44.56  ? 291 SER   A CA  1 
ATOM   1366 C  C   . SER   A 1 177 ? -26.608 16.574  -21.959 1.00 49.66  ? 291 SER   A C   1 
ATOM   1367 O  O   . SER   A 1 177 ? -27.636 16.985  -22.502 1.00 49.25  ? 291 SER   A O   1 
ATOM   1368 C  CB  . SER   A 1 177 ? -25.979 14.128  -22.125 1.00 53.73  ? 291 SER   A CB  1 
ATOM   1369 O  OG  . SER   A 1 177 ? -26.548 14.074  -23.405 1.00 57.34  ? 291 SER   A OG  1 
ATOM   1370 N  N   . VAL   A 1 178 ? -25.502 17.297  -21.876 1.00 42.84  ? 292 VAL   A N   1 
ATOM   1371 C  CA  . VAL   A 1 178 ? -25.327 18.565  -22.555 1.00 45.92  ? 292 VAL   A CA  1 
ATOM   1372 C  C   . VAL   A 1 178 ? -24.125 18.406  -23.455 1.00 48.64  ? 292 VAL   A C   1 
ATOM   1373 O  O   . VAL   A 1 178 ? -23.034 18.075  -22.976 1.00 39.58  ? 292 VAL   A O   1 
ATOM   1374 C  CB  . VAL   A 1 178 ? -25.086 19.712  -21.575 1.00 46.30  ? 292 VAL   A CB  1 
ATOM   1375 C  CG1 . VAL   A 1 178 ? -24.699 20.936  -22.353 1.00 44.91  ? 292 VAL   A CG1 1 
ATOM   1376 C  CG2 . VAL   A 1 178 ? -26.311 19.926  -20.712 1.00 51.07  ? 292 VAL   A CG2 1 
ATOM   1377 N  N   . GLU   A 1 179 ? -24.319 18.639  -24.749 1.00 43.14  ? 293 GLU   A N   1 
ATOM   1378 C  CA  . GLU   A 1 179 ? -23.233 18.488  -25.704 1.00 43.72  ? 293 GLU   A CA  1 
ATOM   1379 C  C   . GLU   A 1 179 ? -22.214 19.598  -25.523 1.00 43.32  ? 293 GLU   A C   1 
ATOM   1380 O  O   . GLU   A 1 179 ? -22.568 20.750  -25.255 1.00 44.16  ? 293 GLU   A O   1 
ATOM   1381 C  CB  . GLU   A 1 179 ? -23.766 18.530  -27.132 1.00 43.12  ? 293 GLU   A CB  1 
ATOM   1382 C  CG  . GLU   A 1 179 ? -23.851 17.199  -27.792 1.00 62.60  ? 293 GLU   A CG  1 
ATOM   1383 C  CD  . GLU   A 1 179 ? -24.805 17.191  -28.971 1.00 75.97  ? 293 GLU   A CD  1 
ATOM   1384 O  OE1 . GLU   A 1 179 ? -24.594 18.012  -29.890 1.00 64.93  ? 293 GLU   A OE1 1 
ATOM   1385 O  OE2 . GLU   A 1 179 ? -25.737 16.347  -28.994 1.00 74.63  ? 293 GLU   A OE2 1 
ATOM   1386 N  N   . ILE   A 1 180 ? -20.939 19.249  -25.667 1.00 41.51  ? 294 ILE   A N   1 
ATOM   1387 C  CA  . ILE   A 1 180 ? -19.859 20.223  -25.758 1.00 37.69  ? 294 ILE   A CA  1 
ATOM   1388 C  C   . ILE   A 1 180 ? -19.063 19.890  -27.019 1.00 44.58  ? 294 ILE   A C   1 
ATOM   1389 O  O   . ILE   A 1 180 ? -18.561 18.765  -27.176 1.00 45.73  ? 294 ILE   A O   1 
ATOM   1390 C  CB  . ILE   A 1 180 ? -18.960 20.231  -24.506 1.00 41.53  ? 294 ILE   A CB  1 
ATOM   1391 C  CG1 . ILE   A 1 180 ? -17.835 21.261  -24.662 1.00 36.11  ? 294 ILE   A CG1 1 
ATOM   1392 C  CG2 . ILE   A 1 180 ? -18.403 18.833  -24.226 1.00 38.33  ? 294 ILE   A CG2 1 
ATOM   1393 C  CD1 . ILE   A 1 180 ? -17.114 21.550  -23.394 1.00 37.63  ? 294 ILE   A CD1 1 
ATOM   1394 N  N   . ASN   A 1 181 ? -18.973 20.855  -27.924 1.00 38.66  ? 295 ASN   A N   1 
ATOM   1395 C  CA  . ASN   A 1 181 ? -18.417 20.668  -29.259 1.00 45.47  ? 295 ASN   A CA  1 
ATOM   1396 C  C   . ASN   A 1 181 ? -17.137 21.496  -29.344 1.00 48.98  ? 295 ASN   A C   1 
ATOM   1397 O  O   . ASN   A 1 181 ? -17.202 22.733  -29.358 1.00 40.42  ? 295 ASN   A O   1 
ATOM   1398 C  CB  . ASN   A 1 181 ? -19.456 21.084  -30.314 1.00 47.65  ? 295 ASN   A CB  1 
ATOM   1399 C  CG  . ASN   A 1 181 ? -18.916 21.061  -31.727 1.00 46.82  ? 295 ASN   A CG  1 
ATOM   1400 O  OD1 . ASN   A 1 181 ? -17.844 20.519  -31.994 1.00 51.00  ? 295 ASN   A OD1 1 
ATOM   1401 N  ND2 . ASN   A 1 181 ? -19.675 21.640  -32.653 1.00 60.50  ? 295 ASN   A ND2 1 
ATOM   1402 N  N   . CYS   A 1 182 ? -15.980 20.822  -29.384 1.00 39.61  ? 296 CYS   A N   1 
ATOM   1403 C  CA  . CYS   A 1 182 ? -14.671 21.474  -29.322 1.00 44.62  ? 296 CYS   A CA  1 
ATOM   1404 C  C   . CYS   A 1 182 ? -13.970 21.369  -30.671 1.00 43.70  ? 296 CYS   A C   1 
ATOM   1405 O  O   . CYS   A 1 182 ? -13.938 20.284  -31.265 1.00 43.22  ? 296 CYS   A O   1 
ATOM   1406 C  CB  . CYS   A 1 182 ? -13.807 20.840  -28.232 1.00 37.11  ? 296 CYS   A CB  1 
ATOM   1407 S  SG  . CYS   A 1 182 ? -14.582 20.931  -26.580 1.00 60.38  ? 296 CYS   A SG  1 
ATOM   1408 N  N   . THR   A 1 183 ? -13.359 22.475  -31.126 1.00 40.52  ? 297 THR   A N   1 
ATOM   1409 C  CA  . THR   A 1 183 ? -12.749 22.552  -32.454 1.00 48.61  ? 297 THR   A CA  1 
ATOM   1410 C  C   . THR   A 1 183 ? -11.492 23.418  -32.459 1.00 49.84  ? 297 THR   A C   1 
ATOM   1411 O  O   . THR   A 1 183 ? -11.527 24.555  -31.986 1.00 47.08  ? 297 THR   A O   1 
ATOM   1412 C  CB  . THR   A 1 183 ? -13.742 23.142  -33.479 1.00 57.88  ? 297 THR   A CB  1 
ATOM   1413 O  OG1 . THR   A 1 183 ? -14.985 22.438  -33.425 1.00 57.20  ? 297 THR   A OG1 1 
ATOM   1414 C  CG2 . THR   A 1 183 ? -13.195 23.091  -34.891 1.00 52.75  ? 297 THR   A CG2 1 
ATOM   1415 N  N   . ARG   A 1 184 ? -10.392 22.898  -33.029 1.00 55.36  ? 298 ARG   A N   1 
ATOM   1416 C  CA  . ARG   A 1 184 ? -9.219  23.691  -33.416 1.00 56.66  ? 298 ARG   A CA  1 
ATOM   1417 C  C   . ARG   A 1 184 ? -9.307  23.869  -34.928 1.00 59.03  ? 298 ARG   A C   1 
ATOM   1418 O  O   . ARG   A 1 184 ? -8.931  22.953  -35.672 1.00 54.55  ? 298 ARG   A O   1 
ATOM   1419 C  CB  . ARG   A 1 184 ? -7.912  22.977  -33.038 1.00 52.88  ? 298 ARG   A CB  1 
ATOM   1420 C  CG  . ARG   A 1 184 ? -6.580  23.772  -33.192 1.00 55.20  ? 298 ARG   A CG  1 
ATOM   1421 C  CD  . ARG   A 1 184 ? -6.246  24.311  -34.606 1.00 58.64  ? 298 ARG   A CD  1 
ATOM   1422 N  NE  . ARG   A 1 184 ? -6.000  23.281  -35.617 1.00 58.48  ? 298 ARG   A NE  1 
ATOM   1423 C  CZ  . ARG   A 1 184 ? -4.885  22.563  -35.758 1.00 62.79  ? 298 ARG   A CZ  1 
ATOM   1424 N  NH1 . ARG   A 1 184 ? -3.845  22.699  -34.938 1.00 52.75  ? 298 ARG   A NH1 1 
ATOM   1425 N  NH2 . ARG   A 1 184 ? -4.808  21.681  -36.753 1.00 51.59  ? 298 ARG   A NH2 1 
ATOM   1426 N  N   . PRO   A 1 185 ? -9.813  25.013  -35.450 1.00 60.03  ? 299 PRO   A N   1 
ATOM   1427 C  CA  . PRO   A 1 185 ? -10.118 25.087  -36.887 1.00 54.87  ? 299 PRO   A CA  1 
ATOM   1428 C  C   . PRO   A 1 185 ? -8.884  24.834  -37.736 1.00 63.94  ? 299 PRO   A C   1 
ATOM   1429 O  O   . PRO   A 1 185 ? -7.744  25.010  -37.271 1.00 61.66  ? 299 PRO   A O   1 
ATOM   1430 C  CB  . PRO   A 1 185 ? -10.637 26.516  -37.066 1.00 46.75  ? 299 PRO   A CB  1 
ATOM   1431 C  CG  . PRO   A 1 185 ? -10.090 27.264  -35.910 1.00 52.31  ? 299 PRO   A CG  1 
ATOM   1432 C  CD  . PRO   A 1 185 ? -10.091 26.288  -34.779 1.00 51.14  ? 299 PRO   A CD  1 
ATOM   1433 N  N   . SER   A 1 186 ? -9.101  24.393  -38.977 1.00 72.92  ? 300 SER   A N   1 
ATOM   1434 C  CA  . SER   A 1 186 ? -7.978  24.069  -39.849 1.00 79.67  ? 300 SER   A CA  1 
ATOM   1435 C  C   . SER   A 1 186 ? -7.105  25.313  -40.048 1.00 88.94  ? 300 SER   A C   1 
ATOM   1436 O  O   . SER   A 1 186 ? -5.940  25.357  -39.611 1.00 95.38  ? 300 SER   A O   1 
ATOM   1437 C  CB  . SER   A 1 186 ? -8.505  23.532  -41.189 1.00 74.76  ? 300 SER   A CB  1 
ATOM   1438 O  OG  . SER   A 1 186 ? -7.454  23.019  -41.997 1.00 85.05  ? 300 SER   A OG  1 
ATOM   1439 N  N   . ASN   A 1 187 ? -7.678  26.353  -40.679 1.00 88.17  ? 301 ASN   A N   1 
ATOM   1440 C  CA  . ASN   A 1 187 ? -7.008  27.653  -40.837 1.00 95.98  ? 301 ASN   A CA  1 
ATOM   1441 C  C   . ASN   A 1 187 ? -8.016  28.771  -40.902 1.00 96.60  ? 301 ASN   A C   1 
ATOM   1442 O  O   . ASN   A 1 187 ? -8.919  28.854  -40.064 1.00 92.78  ? 301 ASN   A O   1 
ATOM   1443 C  CB  . ASN   A 1 187 ? -6.157  27.663  -42.113 1.00 97.16  ? 301 ASN   A CB  1 
ATOM   1444 C  CG  . ASN   A 1 187 ? -5.005  26.690  -42.074 1.00 104.27 ? 301 ASN   A CG  1 
ATOM   1445 O  OD1 . ASN   A 1 187 ? -4.812  25.928  -43.027 1.00 103.80 ? 301 ASN   A OD1 1 
ATOM   1446 N  ND2 . ASN   A 1 187 ? -4.228  26.710  -40.991 1.00 96.58  ? 301 ASN   A ND2 1 
ATOM   1447 N  N   . ASP   A 1 195 ? -2.531  30.859  -35.082 1.00 61.30  ? 325 ASP   A N   1 
ATOM   1448 C  CA  . ASP   A 1 195 ? -2.239  30.153  -33.847 1.00 69.76  ? 325 ASP   A CA  1 
ATOM   1449 C  C   . ASP   A 1 195 ? -2.813  28.755  -33.923 1.00 67.68  ? 325 ASP   A C   1 
ATOM   1450 O  O   . ASP   A 1 195 ? -4.022  28.543  -33.826 1.00 73.00  ? 325 ASP   A O   1 
ATOM   1451 C  CB  . ASP   A 1 195 ? -2.799  30.904  -32.626 1.00 79.20  ? 325 ASP   A CB  1 
ATOM   1452 C  CG  . ASP   A 1 195 ? -2.158  30.458  -31.305 1.00 78.69  ? 325 ASP   A CG  1 
ATOM   1453 O  OD1 . ASP   A 1 195 ? -1.248  29.593  -31.328 1.00 77.08  ? 325 ASP   A OD1 1 
ATOM   1454 O  OD2 . ASP   A 1 195 ? -2.563  30.976  -30.236 1.00 74.55  ? 325 ASP   A OD2 1 
ATOM   1455 N  N   . ILE   A 1 196 ? -1.927  27.789  -34.139 1.00 64.15  ? 326 ILE   A N   1 
ATOM   1456 C  CA  . ILE   A 1 196 ? -2.389  26.426  -34.307 1.00 66.08  ? 326 ILE   A CA  1 
ATOM   1457 C  C   . ILE   A 1 196 ? -2.837  25.822  -32.983 1.00 67.98  ? 326 ILE   A C   1 
ATOM   1458 O  O   . ILE   A 1 196 ? -3.523  24.795  -32.987 1.00 61.38  ? 326 ILE   A O   1 
ATOM   1459 C  CB  . ILE   A 1 196 ? -1.284  25.596  -34.970 1.00 57.49  ? 326 ILE   A CB  1 
ATOM   1460 C  CG1 . ILE   A 1 196 ? -0.074  25.495  -34.051 1.00 59.36  ? 326 ILE   A CG1 1 
ATOM   1461 C  CG2 . ILE   A 1 196 ? -0.874  26.269  -36.250 1.00 64.12  ? 326 ILE   A CG2 1 
ATOM   1462 C  CD1 . ILE   A 1 196 ? 1.008   24.607  -34.588 1.00 58.94  ? 326 ILE   A CD1 1 
ATOM   1463 N  N   . ARG   A 1 197 ? -2.487  26.438  -31.851 1.00 56.70  ? 327 ARG   A N   1 
ATOM   1464 C  CA  . ARG   A 1 197 ? -2.887  25.903  -30.557 1.00 54.68  ? 327 ARG   A CA  1 
ATOM   1465 C  C   . ARG   A 1 197 ? -4.203  26.474  -30.068 1.00 55.34  ? 327 ARG   A C   1 
ATOM   1466 O  O   . ARG   A 1 197 ? -4.806  25.896  -29.160 1.00 59.34  ? 327 ARG   A O   1 
ATOM   1467 C  CB  . ARG   A 1 197 ? -1.787  26.154  -29.518 1.00 49.50  ? 327 ARG   A CB  1 
ATOM   1468 C  CG  . ARG   A 1 197 ? -0.557  25.276  -29.748 1.00 58.51  ? 327 ARG   A CG  1 
ATOM   1469 C  CD  . ARG   A 1 197 ? 0.647   25.641  -28.889 1.00 59.71  ? 327 ARG   A CD  1 
ATOM   1470 N  NE  . ARG   A 1 197 ? 1.862   25.347  -29.638 1.00 73.82  ? 327 ARG   A NE  1 
ATOM   1471 C  CZ  . ARG   A 1 197 ? 2.335   26.112  -30.616 1.00 61.11  ? 327 ARG   A CZ  1 
ATOM   1472 N  NH1 . ARG   A 1 197 ? 1.756   27.257  -30.947 1.00 63.45  ? 327 ARG   A NH1 1 
ATOM   1473 N  NH2 . ARG   A 1 197 ? 3.413   25.718  -31.283 1.00 69.41  ? 327 ARG   A NH2 1 
ATOM   1474 N  N   . LYS   A 1 198 ? -4.673  27.571  -30.664 1.00 54.39  ? 328 LYS   A N   1 
ATOM   1475 C  CA  . LYS   A 1 198 ? -5.913  28.204  -30.225 1.00 52.43  ? 328 LYS   A CA  1 
ATOM   1476 C  C   . LYS   A 1 198 ? -7.112  27.390  -30.694 1.00 57.82  ? 328 LYS   A C   1 
ATOM   1477 O  O   . LYS   A 1 198 ? -7.182  26.995  -31.863 1.00 54.76  ? 328 LYS   A O   1 
ATOM   1478 C  CB  . LYS   A 1 198 ? -6.007  29.625  -30.773 1.00 56.89  ? 328 LYS   A CB  1 
ATOM   1479 C  CG  . LYS   A 1 198 ? -7.429  30.115  -31.064 1.00 61.39  ? 328 LYS   A CG  1 
ATOM   1480 C  CD  . LYS   A 1 198 ? -7.442  31.203  -32.166 1.00 77.45  ? 328 LYS   A CD  1 
ATOM   1481 C  CE  . LYS   A 1 198 ? -8.561  30.997  -33.201 1.00 70.61  ? 328 LYS   A CE  1 
ATOM   1482 N  NZ  . LYS   A 1 198 ? -9.931  31.316  -32.680 1.00 83.80  ? 328 LYS   A NZ  1 
ATOM   1483 N  N   . ALA   A 1 199 ? -8.051  27.133  -29.783 1.00 48.95  ? 329 ALA   A N   1 
ATOM   1484 C  CA  . ALA   A 1 199 ? -9.256  26.372  -30.088 1.00 51.09  ? 329 ALA   A CA  1 
ATOM   1485 C  C   . ALA   A 1 199 ? -10.385 26.918  -29.232 1.00 46.94  ? 329 ALA   A C   1 
ATOM   1486 O  O   . ALA   A 1 199 ? -10.201 27.855  -28.448 1.00 50.29  ? 329 ALA   A O   1 
ATOM   1487 C  CB  . ALA   A 1 199 ? -9.058  24.867  -29.843 1.00 45.82  ? 329 ALA   A CB  1 
ATOM   1488 N  N   . TYR   A 1 200 ? -11.555 26.305  -29.359 1.00 43.15  ? 330 TYR   A N   1 
ATOM   1489 C  CA  . TYR   A 1 200 ? -12.715 26.749  -28.594 1.00 46.37  ? 330 TYR   A CA  1 
ATOM   1490 C  C   . TYR   A 1 200 ? -13.708 25.599  -28.497 1.00 46.64  ? 330 TYR   A C   1 
ATOM   1491 O  O   . TYR   A 1 200 ? -13.666 24.658  -29.296 1.00 49.29  ? 330 TYR   A O   1 
ATOM   1492 C  CB  . TYR   A 1 200 ? -13.374 27.975  -29.243 1.00 44.13  ? 330 TYR   A CB  1 
ATOM   1493 C  CG  . TYR   A 1 200 ? -13.769 27.759  -30.690 1.00 47.47  ? 330 TYR   A CG  1 
ATOM   1494 C  CD1 . TYR   A 1 200 ? -15.091 27.513  -31.044 1.00 60.10  ? 330 TYR   A CD1 1 
ATOM   1495 C  CD2 . TYR   A 1 200 ? -12.821 27.800  -31.705 1.00 60.64  ? 330 TYR   A CD2 1 
ATOM   1496 C  CE1 . TYR   A 1 200 ? -15.464 27.305  -32.376 1.00 62.71  ? 330 TYR   A CE1 1 
ATOM   1497 C  CE2 . TYR   A 1 200 ? -13.179 27.597  -33.050 1.00 65.82  ? 330 TYR   A CE2 1 
ATOM   1498 C  CZ  . TYR   A 1 200 ? -14.499 27.351  -33.371 1.00 69.30  ? 330 TYR   A CZ  1 
ATOM   1499 O  OH  . TYR   A 1 200 ? -14.855 27.157  -34.690 1.00 75.39  ? 330 TYR   A OH  1 
ATOM   1500 N  N   . CYS   A 1 201 ? -14.594 25.681  -27.497 1.00 46.11  ? 331 CYS   A N   1 
ATOM   1501 C  CA  . CYS   A 1 201 ? -15.679 24.725  -27.303 1.00 47.07  ? 331 CYS   A CA  1 
ATOM   1502 C  C   . CYS   A 1 201 ? -16.996 25.476  -27.312 1.00 46.48  ? 331 CYS   A C   1 
ATOM   1503 O  O   . CYS   A 1 201 ? -17.117 26.533  -26.691 1.00 52.38  ? 331 CYS   A O   1 
ATOM   1504 C  CB  . CYS   A 1 201 ? -15.545 23.937  -25.988 1.00 46.69  ? 331 CYS   A CB  1 
ATOM   1505 S  SG  . CYS   A 1 201 ? -14.092 22.829  -25.873 1.00 60.01  ? 331 CYS   A SG  1 
ATOM   1506 N  N   . GLU   A 1 202 ? -17.980 24.920  -28.002 1.00 49.28  ? 332 GLU   A N   1 
ATOM   1507 C  CA  . GLU   A 1 202 ? -19.304 25.516  -28.122 1.00 48.17  ? 332 GLU   A CA  1 
ATOM   1508 C  C   . GLU   A 1 202 ? -20.306 24.678  -27.339 1.00 41.98  ? 332 GLU   A C   1 
ATOM   1509 O  O   . GLU   A 1 202 ? -20.385 23.459  -27.515 1.00 44.86  ? 332 GLU   A O   1 
ATOM   1510 C  CB  . GLU   A 1 202 ? -19.695 25.624  -29.592 1.00 43.79  ? 332 GLU   A CB  1 
ATOM   1511 C  CG  . GLU   A 1 202 ? -18.826 26.638  -30.289 1.00 53.09  ? 332 GLU   A CG  1 
ATOM   1512 C  CD  . GLU   A 1 202 ? -19.516 27.388  -31.410 1.00 71.67  ? 332 GLU   A CD  1 
ATOM   1513 O  OE1 . GLU   A 1 202 ? -19.459 26.887  -32.554 1.00 61.35  ? 332 GLU   A OE1 1 
ATOM   1514 O  OE2 . GLU   A 1 202 ? -20.087 28.480  -31.157 1.00 80.50  ? 332 GLU   A OE2 1 
ATOM   1515 N  N   . ILE   A 1 203 ? -21.023 25.326  -26.437 1.00 45.48  ? 333 ILE   A N   1 
ATOM   1516 C  CA  . ILE   A 1 203 ? -22.036 24.701  -25.604 1.00 44.17  ? 333 ILE   A CA  1 
ATOM   1517 C  C   . ILE   A 1 203 ? -23.315 25.490  -25.806 1.00 50.95  ? 333 ILE   A C   1 
ATOM   1518 O  O   . ILE   A 1 203 ? -23.277 26.723  -25.851 1.00 52.36  ? 333 ILE   A O   1 
ATOM   1519 C  CB  . ILE   A 1 203 ? -21.656 24.713  -24.107 1.00 44.52  ? 333 ILE   A CB  1 
ATOM   1520 C  CG1 . ILE   A 1 203 ? -20.348 23.965  -23.831 1.00 47.01  ? 333 ILE   A CG1 1 
ATOM   1521 C  CG2 . ILE   A 1 203 ? -22.777 24.123  -23.304 1.00 51.48  ? 333 ILE   A CG2 1 
ATOM   1522 C  CD1 . ILE   A 1 203 ? -19.110 24.826  -23.966 1.00 55.24  ? 333 ILE   A CD1 1 
ATOM   1523 N  N   . ASN   A 1 204 ? -24.440 24.793  -25.914 1.00 44.15  ? 334 ASN   A N   1 
ATOM   1524 C  CA  . ASN   A 1 204 ? -25.738 25.449  -25.960 1.00 43.86  ? 334 ASN   A CA  1 
ATOM   1525 C  C   . ASN   A 1 204 ? -26.040 26.038  -24.583 1.00 51.71  ? 334 ASN   A C   1 
ATOM   1526 O  O   . ASN   A 1 204 ? -26.420 25.317  -23.655 1.00 46.30  ? 334 ASN   A O   1 
ATOM   1527 C  CB  . ASN   A 1 204 ? -26.781 24.435  -26.407 1.00 45.42  ? 334 ASN   A CB  1 
ATOM   1528 C  CG  . ASN   A 1 204 ? -28.180 25.001  -26.449 1.00 55.34  ? 334 ASN   A CG  1 
ATOM   1529 O  OD1 . ASN   A 1 204 ? -28.529 25.947  -25.736 1.00 55.25  ? 334 ASN   A OD1 1 
ATOM   1530 N  ND2 . ASN   A 1 204 ? -28.996 24.415  -27.274 1.00 54.86  ? 334 ASN   A ND2 1 
ATOM   1531 N  N   . GLY   A 1 205 ? -25.852 27.356  -24.437 1.00 46.59  ? 335 GLY   A N   1 
ATOM   1532 C  CA  . GLY   A 1 205 ? -25.982 27.968  -23.123 1.00 47.39  ? 335 GLY   A CA  1 
ATOM   1533 C  C   . GLY   A 1 205 ? -27.370 27.802  -22.544 1.00 49.61  ? 335 GLY   A C   1 
ATOM   1534 O  O   . GLY   A 1 205 ? -27.541 27.717  -21.320 1.00 44.48  ? 335 GLY   A O   1 
ATOM   1535 N  N   . THR   A 1 206 ? -28.384 27.755  -23.416 1.00 55.43  ? 336 THR   A N   1 
ATOM   1536 C  CA  . THR   A 1 206 ? -29.747 27.509  -22.966 1.00 54.16  ? 336 THR   A CA  1 
ATOM   1537 C  C   . THR   A 1 206 ? -29.837 26.158  -22.287 1.00 58.43  ? 336 THR   A C   1 
ATOM   1538 O  O   . THR   A 1 206 ? -30.399 26.047  -21.193 1.00 64.07  ? 336 THR   A O   1 
ATOM   1539 C  CB  . THR   A 1 206 ? -30.722 27.580  -24.145 1.00 51.98  ? 336 THR   A CB  1 
ATOM   1540 O  OG1 . THR   A 1 206 ? -30.668 28.888  -24.722 1.00 58.25  ? 336 THR   A OG1 1 
ATOM   1541 C  CG2 . THR   A 1 206 ? -32.141 27.307  -23.689 1.00 47.41  ? 336 THR   A CG2 1 
ATOM   1542 N  N   . LYS   A 1 207 ? -29.303 25.116  -22.943 1.00 51.98  ? 337 LYS   A N   1 
ATOM   1543 C  CA  . LYS   A 1 207 ? -29.244 23.782  -22.354 1.00 61.50  ? 337 LYS   A CA  1 
ATOM   1544 C  C   . LYS   A 1 207 ? -28.445 23.793  -21.059 1.00 52.38  ? 337 LYS   A C   1 
ATOM   1545 O  O   . LYS   A 1 207 ? -28.904 23.286  -20.029 1.00 50.40  ? 337 LYS   A O   1 
ATOM   1546 C  CB  . LYS   A 1 207 ? -28.620 22.802  -23.350 1.00 57.11  ? 337 LYS   A CB  1 
ATOM   1547 C  CG  . LYS   A 1 207 ? -29.619 21.866  -24.019 1.00 68.10  ? 337 LYS   A CG  1 
ATOM   1548 C  CD  . LYS   A 1 207 ? -29.061 21.215  -25.311 1.00 61.35  ? 337 LYS   A CD  1 
ATOM   1549 C  CE  . LYS   A 1 207 ? -27.857 20.300  -25.051 1.00 60.87  ? 337 LYS   A CE  1 
ATOM   1550 N  NZ  . LYS   A 1 207 ? -26.952 20.075  -26.221 1.00 55.34  ? 337 LYS   A NZ  1 
ATOM   1551 N  N   . TRP   A 1 208 ? -27.252 24.387  -21.091 1.00 56.05  ? 338 TRP   A N   1 
ATOM   1552 C  CA  . TRP   A 1 208 ? -26.364 24.328  -19.938 1.00 48.12  ? 338 TRP   A CA  1 
ATOM   1553 C  C   . TRP   A 1 208 ? -26.976 25.024  -18.740 1.00 55.49  ? 338 TRP   A C   1 
ATOM   1554 O  O   . TRP   A 1 208 ? -27.131 24.417  -17.670 1.00 49.62  ? 338 TRP   A O   1 
ATOM   1555 C  CB  . TRP   A 1 208 ? -25.025 24.956  -20.281 1.00 43.96  ? 338 TRP   A CB  1 
ATOM   1556 C  CG  . TRP   A 1 208 ? -24.146 25.093  -19.094 1.00 48.80  ? 338 TRP   A CG  1 
ATOM   1557 C  CD1 . TRP   A 1 208 ? -23.830 26.249  -18.442 1.00 49.43  ? 338 TRP   A CD1 1 
ATOM   1558 C  CD2 . TRP   A 1 208 ? -23.467 24.040  -18.402 1.00 47.13  ? 338 TRP   A CD2 1 
ATOM   1559 N  NE1 . TRP   A 1 208 ? -22.982 25.985  -17.393 1.00 51.53  ? 338 TRP   A NE1 1 
ATOM   1560 C  CE2 . TRP   A 1 208 ? -22.750 24.634  -17.347 1.00 44.09  ? 338 TRP   A CE2 1 
ATOM   1561 C  CE3 . TRP   A 1 208 ? -23.398 22.648  -18.572 1.00 52.05  ? 338 TRP   A CE3 1 
ATOM   1562 C  CZ2 . TRP   A 1 208 ? -21.967 23.891  -16.470 1.00 43.12  ? 338 TRP   A CZ2 1 
ATOM   1563 C  CZ3 . TRP   A 1 208 ? -22.623 21.912  -17.702 1.00 45.81  ? 338 TRP   A CZ3 1 
ATOM   1564 C  CH2 . TRP   A 1 208 ? -21.911 22.543  -16.659 1.00 47.67  ? 338 TRP   A CH2 1 
ATOM   1565 N  N   . ASN   A 1 209 ? -27.332 26.312  -18.907 1.00 55.67  ? 339 ASN   A N   1 
ATOM   1566 C  CA  . ASN   A 1 209 ? -27.812 27.106  -17.781 1.00 51.63  ? 339 ASN   A CA  1 
ATOM   1567 C  C   . ASN   A 1 209 ? -29.040 26.466  -17.137 1.00 55.14  ? 339 ASN   A C   1 
ATOM   1568 O  O   . ASN   A 1 209 ? -29.164 26.465  -15.906 1.00 52.19  ? 339 ASN   A O   1 
ATOM   1569 C  CB  . ASN   A 1 209 ? -28.086 28.540  -18.225 1.00 52.31  ? 339 ASN   A CB  1 
ATOM   1570 C  CG  . ASN   A 1 209 ? -26.809 29.278  -18.617 1.00 62.33  ? 339 ASN   A CG  1 
ATOM   1571 O  OD1 . ASN   A 1 209 ? -25.784 29.148  -17.947 1.00 59.04  ? 339 ASN   A OD1 1 
ATOM   1572 N  ND2 . ASN   A 1 209 ? -26.867 30.057  -19.697 1.00 53.39  ? 339 ASN   A ND2 1 
ATOM   1573 N  N   . LYS   A 1 210 ? -29.927 25.865  -17.943 1.00 44.08  ? 340 LYS   A N   1 
ATOM   1574 C  CA  . LYS   A 1 210 ? -31.105 25.207  -17.384 1.00 51.41  ? 340 LYS   A CA  1 
ATOM   1575 C  C   . LYS   A 1 210 ? -30.701 24.013  -16.522 1.00 60.11  ? 340 LYS   A C   1 
ATOM   1576 O  O   . LYS   A 1 210 ? -31.128 23.895  -15.365 1.00 62.97  ? 340 LYS   A O   1 
ATOM   1577 C  CB  . LYS   A 1 210 ? -32.053 24.809  -18.521 1.00 49.45  ? 340 LYS   A CB  1 
ATOM   1578 C  CG  . LYS   A 1 210 ? -32.977 23.625  -18.248 1.00 63.02  ? 340 LYS   A CG  1 
ATOM   1579 C  CD  . LYS   A 1 210 ? -33.715 23.764  -16.935 1.00 60.23  ? 340 LYS   A CD  1 
ATOM   1580 C  CE  . LYS   A 1 210 ? -34.978 22.914  -16.944 1.00 73.10  ? 340 LYS   A CE  1 
ATOM   1581 N  NZ  . LYS   A 1 210 ? -35.871 23.257  -15.787 1.00 68.39  ? 340 LYS   A NZ  1 
ATOM   1582 N  N   . VAL   A 1 211 ? -29.853 23.131  -17.063 1.00 59.55  ? 341 VAL   A N   1 
ATOM   1583 C  CA  . VAL   A 1 211 ? -29.345 22.002  -16.284 1.00 50.36  ? 341 VAL   A CA  1 
ATOM   1584 C  C   . VAL   A 1 211 ? -28.620 22.500  -15.040 1.00 46.06  ? 341 VAL   A C   1 
ATOM   1585 O  O   . VAL   A 1 211 ? -28.720 21.895  -13.965 1.00 54.25  ? 341 VAL   A O   1 
ATOM   1586 C  CB  . VAL   A 1 211 ? -28.423 21.123  -17.151 1.00 38.93  ? 341 VAL   A CB  1 
ATOM   1587 C  CG1 . VAL   A 1 211 ? -27.305 20.525  -16.300 1.00 47.27  ? 341 VAL   A CG1 1 
ATOM   1588 C  CG2 . VAL   A 1 211 ? -29.216 20.066  -17.874 1.00 43.58  ? 341 VAL   A CG2 1 
ATOM   1589 N  N   . LEU   A 1 212 ? -27.884 23.612  -15.160 1.00 44.42  ? 342 LEU   A N   1 
ATOM   1590 C  CA  . LEU   A 1 212 ? -27.127 24.103  -14.015 1.00 49.28  ? 342 LEU   A CA  1 
ATOM   1591 C  C   . LEU   A 1 212 ? -28.050 24.667  -12.946 1.00 56.80  ? 342 LEU   A C   1 
ATOM   1592 O  O   . LEU   A 1 212 ? -27.753 24.549  -11.752 1.00 62.69  ? 342 LEU   A O   1 
ATOM   1593 C  CB  . LEU   A 1 212 ? -26.107 25.149  -14.454 1.00 43.95  ? 342 LEU   A CB  1 
ATOM   1594 C  CG  . LEU   A 1 212 ? -24.997 25.500  -13.463 1.00 52.43  ? 342 LEU   A CG  1 
ATOM   1595 C  CD1 . LEU   A 1 212 ? -24.313 24.240  -12.903 1.00 55.96  ? 342 LEU   A CD1 1 
ATOM   1596 C  CD2 . LEU   A 1 212 ? -23.990 26.447  -14.103 1.00 47.97  ? 342 LEU   A CD2 1 
ATOM   1597 N  N   . LYS   A 1 213 ? -29.172 25.266  -13.353 1.00 51.78  ? 343 LYS   A N   1 
ATOM   1598 C  CA  . LYS   A 1 213 ? -30.204 25.625  -12.390 1.00 56.82  ? 343 LYS   A CA  1 
ATOM   1599 C  C   . LYS   A 1 213 ? -30.701 24.395  -11.634 1.00 66.20  ? 343 LYS   A C   1 
ATOM   1600 O  O   . LYS   A 1 213 ? -30.858 24.435  -10.406 1.00 54.17  ? 343 LYS   A O   1 
ATOM   1601 C  CB  . LYS   A 1 213 ? -31.359 26.316  -13.103 1.00 57.37  ? 343 LYS   A CB  1 
ATOM   1602 C  CG  . LYS   A 1 213 ? -32.420 26.896  -12.172 1.00 73.68  ? 343 LYS   A CG  1 
ATOM   1603 C  CD  . LYS   A 1 213 ? -32.713 28.339  -12.577 1.00 74.45  ? 343 LYS   A CD  1 
ATOM   1604 C  CE  . LYS   A 1 213 ? -34.156 28.749  -12.298 1.00 80.56  ? 343 LYS   A CE  1 
ATOM   1605 N  NZ  . LYS   A 1 213 ? -34.348 29.384  -10.951 1.00 73.45  ? 343 LYS   A NZ  1 
ATOM   1606 N  N   . GLN   A 1 214 ? -30.938 23.284  -12.347 1.00 56.52  ? 344 GLN   A N   1 
ATOM   1607 C  CA  . GLN   A 1 214 ? -31.459 22.101  -11.671 1.00 59.51  ? 344 GLN   A CA  1 
ATOM   1608 C  C   . GLN   A 1 214 ? -30.441 21.509  -10.730 1.00 54.44  ? 344 GLN   A C   1 
ATOM   1609 O  O   . GLN   A 1 214 ? -30.813 20.809  -9.786  1.00 62.73  ? 344 GLN   A O   1 
ATOM   1610 C  CB  . GLN   A 1 214 ? -31.870 21.033  -12.662 1.00 57.95  ? 344 GLN   A CB  1 
ATOM   1611 C  CG  . GLN   A 1 214 ? -33.250 21.177  -13.172 1.00 54.07  ? 344 GLN   A CG  1 
ATOM   1612 C  CD  . GLN   A 1 214 ? -33.445 20.308  -14.372 1.00 59.97  ? 344 GLN   A CD  1 
ATOM   1613 O  OE1 . GLN   A 1 214 ? -34.374 20.496  -15.141 1.00 65.76  ? 344 GLN   A OE1 1 
ATOM   1614 N  NE2 . GLN   A 1 214 ? -32.553 19.339  -14.547 1.00 61.31  ? 344 GLN   A NE2 1 
ATOM   1615 N  N   . VAL   A 1 215 ? -29.159 21.734  -11.000 1.00 58.85  ? 345 VAL   A N   1 
ATOM   1616 C  CA  . VAL   A 1 215 ? -28.128 21.253  -10.098 1.00 45.73  ? 345 VAL   A CA  1 
ATOM   1617 C  C   . VAL   A 1 215 ? -28.165 22.059  -8.819  1.00 51.05  ? 345 VAL   A C   1 
ATOM   1618 O  O   . VAL   A 1 215 ? -28.023 21.517  -7.712  1.00 49.36  ? 345 VAL   A O   1 
ATOM   1619 C  CB  . VAL   A 1 215 ? -26.743 21.335  -10.764 1.00 45.82  ? 345 VAL   A CB  1 
ATOM   1620 C  CG1 . VAL   A 1 215 ? -25.633 21.133  -9.720  1.00 41.96  ? 345 VAL   A CG1 1 
ATOM   1621 C  CG2 . VAL   A 1 215 ? -26.617 20.350  -11.917 1.00 40.53  ? 345 VAL   A CG2 1 
ATOM   1622 N  N   . THR   A 1 216 ? -28.351 23.366  -8.950  1.00 47.01  ? 346 THR   A N   1 
ATOM   1623 C  CA  . THR   A 1 216 ? -28.412 24.199  -7.763  1.00 56.55  ? 346 THR   A CA  1 
ATOM   1624 C  C   . THR   A 1 216 ? -29.591 23.795  -6.895  1.00 53.59  ? 346 THR   A C   1 
ATOM   1625 O  O   . THR   A 1 216 ? -29.449 23.646  -5.679  1.00 51.43  ? 346 THR   A O   1 
ATOM   1626 C  CB  . THR   A 1 216 ? -28.493 25.659  -8.167  1.00 54.33  ? 346 THR   A CB  1 
ATOM   1627 O  OG1 . THR   A 1 216 ? -29.515 25.798  -9.161  1.00 63.85  ? 346 THR   A OG1 1 
ATOM   1628 C  CG2 . THR   A 1 216 ? -27.186 26.087  -8.742  1.00 50.02  ? 346 THR   A CG2 1 
ATOM   1629 N  N   . GLU   A 1 217 ? -30.757 23.588  -7.510  1.00 55.16  ? 347 GLU   A N   1 
ATOM   1630 C  CA  . GLU   A 1 217 ? -31.894 23.045  -6.779  1.00 60.05  ? 347 GLU   A CA  1 
ATOM   1631 C  C   . GLU   A 1 217 ? -31.497 21.815  -5.970  1.00 65.91  ? 347 GLU   A C   1 
ATOM   1632 O  O   . GLU   A 1 217 ? -31.782 21.733  -4.771  1.00 69.03  ? 347 GLU   A O   1 
ATOM   1633 C  CB  . GLU   A 1 217 ? -33.030 22.712  -7.746  1.00 56.74  ? 347 GLU   A CB  1 
ATOM   1634 C  CG  . GLU   A 1 217 ? -34.102 21.849  -7.112  1.00 78.59  ? 347 GLU   A CG  1 
ATOM   1635 C  CD  . GLU   A 1 217 ? -34.177 20.429  -7.685  1.00 91.82  ? 347 GLU   A CD  1 
ATOM   1636 O  OE1 . GLU   A 1 217 ? -35.016 19.647  -7.174  1.00 88.20  ? 347 GLU   A OE1 1 
ATOM   1637 O  OE2 . GLU   A 1 217 ? -33.429 20.091  -8.638  1.00 89.59  ? 347 GLU   A OE2 1 
ATOM   1638 N  N   . LYS   A 1 218 ? -30.832 20.850  -6.613  1.00 61.34  ? 348 LYS   A N   1 
ATOM   1639 C  CA  . LYS   A 1 218 ? -30.488 19.609  -5.932  1.00 54.13  ? 348 LYS   A CA  1 
ATOM   1640 C  C   . LYS   A 1 218 ? -29.503 19.853  -4.809  1.00 51.65  ? 348 LYS   A C   1 
ATOM   1641 O  O   . LYS   A 1 218 ? -29.603 19.219  -3.752  1.00 52.53  ? 348 LYS   A O   1 
ATOM   1642 C  CB  . LYS   A 1 218 ? -29.932 18.592  -6.932  1.00 55.56  ? 348 LYS   A CB  1 
ATOM   1643 C  CG  . LYS   A 1 218 ? -29.712 17.179  -6.369  1.00 62.57  ? 348 LYS   A CG  1 
ATOM   1644 C  CD  . LYS   A 1 218 ? -30.976 16.620  -5.718  1.00 57.49  ? 348 LYS   A CD  1 
ATOM   1645 C  CE  . LYS   A 1 218 ? -32.156 16.675  -6.669  1.00 61.67  ? 348 LYS   A CE  1 
ATOM   1646 N  NZ  . LYS   A 1 218 ? -33.101 15.554  -6.405  1.00 55.89  ? 348 LYS   A NZ  1 
ATOM   1647 N  N   . LEU   A 1 219 ? -28.545 20.764  -5.019  1.00 45.13  ? 349 LEU   A N   1 
ATOM   1648 C  CA  . LEU   A 1 219 ? -27.566 21.097  -3.989  1.00 48.86  ? 349 LEU   A CA  1 
ATOM   1649 C  C   . LEU   A 1 219 ? -28.223 21.835  -2.827  1.00 57.20  ? 349 LEU   A C   1 
ATOM   1650 O  O   . LEU   A 1 219 ? -27.815 21.655  -1.675  1.00 53.27  ? 349 LEU   A O   1 
ATOM   1651 C  CB  . LEU   A 1 219 ? -26.441 21.942  -4.600  1.00 49.76  ? 349 LEU   A CB  1 
ATOM   1652 C  CG  . LEU   A 1 219 ? -25.309 21.243  -5.363  1.00 59.55  ? 349 LEU   A CG  1 
ATOM   1653 C  CD1 . LEU   A 1 219 ? -24.320 22.290  -5.910  1.00 46.03  ? 349 LEU   A CD1 1 
ATOM   1654 C  CD2 . LEU   A 1 219 ? -24.605 20.187  -4.508  1.00 41.78  ? 349 LEU   A CD2 1 
ATOM   1655 N  N   . LYS   A 1 220 ? -29.223 22.679  -3.127  1.00 60.02  ? 350 LYS   A N   1 
ATOM   1656 C  CA  . LYS   A 1 220 ? -30.068 23.292  -2.105  1.00 60.21  ? 350 LYS   A CA  1 
ATOM   1657 C  C   . LYS   A 1 220 ? -30.605 22.245  -1.137  1.00 66.14  ? 350 LYS   A C   1 
ATOM   1658 O  O   . LYS   A 1 220 ? -30.454 22.383  0.084   1.00 60.37  ? 350 LYS   A O   1 
ATOM   1659 C  CB  . LYS   A 1 220 ? -31.229 24.020  -2.776  1.00 59.86  ? 350 LYS   A CB  1 
ATOM   1660 C  CG  . LYS   A 1 220 ? -30.968 25.464  -3.146  1.00 64.25  ? 350 LYS   A CG  1 
ATOM   1661 C  CD  . LYS   A 1 220 ? -32.258 26.147  -3.568  1.00 67.27  ? 350 LYS   A CD  1 
ATOM   1662 C  CE  . LYS   A 1 220 ? -32.118 27.662  -3.641  1.00 73.91  ? 350 LYS   A CE  1 
ATOM   1663 N  NZ  . LYS   A 1 220 ? -31.022 28.191  -2.786  1.00 75.38  ? 350 LYS   A NZ  1 
ATOM   1664 N  N   . GLU   A 1 221 ? -31.218 21.176  -1.676  1.00 66.28  ? 351 GLU   A N   1 
ATOM   1665 C  CA  . GLU   A 1 221 ? -31.823 20.133  -0.846  1.00 55.97  ? 351 GLU   A CA  1 
ATOM   1666 C  C   . GLU   A 1 221 ? -30.844 19.573  0.176   1.00 54.03  ? 351 GLU   A C   1 
ATOM   1667 O  O   . GLU   A 1 221 ? -31.200 19.358  1.339   1.00 66.99  ? 351 GLU   A O   1 
ATOM   1668 C  CB  . GLU   A 1 221 ? -32.352 19.000  -1.723  1.00 57.46  ? 351 GLU   A CB  1 
ATOM   1669 C  CG  . GLU   A 1 221 ? -33.256 19.421  -2.880  1.00 63.85  ? 351 GLU   A CG  1 
ATOM   1670 C  CD  . GLU   A 1 221 ? -33.984 18.236  -3.509  1.00 80.37  ? 351 GLU   A CD  1 
ATOM   1671 O  OE1 . GLU   A 1 221 ? -33.482 17.096  -3.380  1.00 82.23  ? 351 GLU   A OE1 1 
ATOM   1672 O  OE2 . GLU   A 1 221 ? -35.041 18.434  -4.148  1.00 87.06  ? 351 GLU   A OE2 1 
ATOM   1673 N  N   . HIS   A 1 222 ? -29.617 19.318  -0.234  1.00 51.76  ? 352 HIS   A N   1 
ATOM   1674 C  CA  . HIS   A 1 222 ? -28.633 18.743  0.667   1.00 54.60  ? 352 HIS   A CA  1 
ATOM   1675 C  C   . HIS   A 1 222 ? -28.007 19.764  1.603   1.00 59.74  ? 352 HIS   A C   1 
ATOM   1676 O  O   . HIS   A 1 222 ? -27.331 19.369  2.561   1.00 60.93  ? 352 HIS   A O   1 
ATOM   1677 C  CB  . HIS   A 1 222 ? -27.522 18.060  -0.131  1.00 56.08  ? 352 HIS   A CB  1 
ATOM   1678 C  CG  . HIS   A 1 222 ? -27.964 16.841  -0.873  1.00 62.41  ? 352 HIS   A CG  1 
ATOM   1679 N  ND1 . HIS   A 1 222 ? -28.627 16.901  -2.079  1.00 55.09  ? 352 HIS   A ND1 1 
ATOM   1680 C  CD2 . HIS   A 1 222 ? -27.817 15.525  -0.586  1.00 60.71  ? 352 HIS   A CD2 1 
ATOM   1681 C  CE1 . HIS   A 1 222 ? -28.866 15.672  -2.507  1.00 44.99  ? 352 HIS   A CE1 1 
ATOM   1682 N  NE2 . HIS   A 1 222 ? -28.385 14.820  -1.618  1.00 57.07  ? 352 HIS   A NE2 1 
ATOM   1683 N  N   . PHE   A 1 223 ? -28.206 21.054  1.351   1.00 61.12  ? 353 PHE   A N   1 
ATOM   1684 C  CA  . PHE   A 1 223 ? -27.507 22.108  2.068   1.00 65.74  ? 353 PHE   A CA  1 
ATOM   1685 C  C   . PHE   A 1 223 ? -28.485 23.110  2.663   1.00 66.67  ? 353 PHE   A C   1 
ATOM   1686 O  O   . PHE   A 1 223 ? -28.209 24.309  2.733   1.00 69.25  ? 353 PHE   A O   1 
ATOM   1687 C  CB  . PHE   A 1 223 ? -26.489 22.787  1.160   1.00 62.53  ? 353 PHE   A CB  1 
ATOM   1688 C  CG  . PHE   A 1 223 ? -25.232 21.997  0.993   1.00 56.93  ? 353 PHE   A CG  1 
ATOM   1689 C  CD1 . PHE   A 1 223 ? -24.300 21.923  2.018   1.00 55.88  ? 353 PHE   A CD1 1 
ATOM   1690 C  CD2 . PHE   A 1 223 ? -24.982 21.314  -0.184  1.00 62.01  ? 353 PHE   A CD2 1 
ATOM   1691 C  CE1 . PHE   A 1 223 ? -23.137 21.185  1.864   1.00 62.07  ? 353 PHE   A CE1 1 
ATOM   1692 C  CE2 . PHE   A 1 223 ? -23.823 20.570  -0.342  1.00 50.78  ? 353 PHE   A CE2 1 
ATOM   1693 C  CZ  . PHE   A 1 223 ? -22.900 20.507  0.683   1.00 55.36  ? 353 PHE   A CZ  1 
ATOM   1694 N  N   . ASN   A 1 224 ? -29.647 22.611  3.099   1.00 57.40  ? 354 ASN   A N   1 
ATOM   1695 C  CA  . ASN   A 1 224 ? -30.563 23.362  3.951   1.00 71.21  ? 354 ASN   A CA  1 
ATOM   1696 C  C   . ASN   A 1 224 ? -31.157 24.564  3.231   1.00 71.61  ? 354 ASN   A C   1 
ATOM   1697 O  O   . ASN   A 1 224 ? -31.273 25.649  3.800   1.00 69.38  ? 354 ASN   A O   1 
ATOM   1698 C  CB  . ASN   A 1 224 ? -29.874 23.784  5.251   1.00 69.20  ? 354 ASN   A CB  1 
ATOM   1699 C  CG  . ASN   A 1 224 ? -29.770 22.651  6.212   1.00 74.48  ? 354 ASN   A CG  1 
ATOM   1700 O  OD1 . ASN   A 1 224 ? -30.770 21.979  6.464   1.00 73.74  ? 354 ASN   A OD1 1 
ATOM   1701 N  ND2 . ASN   A 1 224 ? -28.572 22.408  6.751   1.00 78.55  ? 354 ASN   A ND2 1 
ATOM   1702 N  N   . ASN   A 1 225 ? -31.538 24.372  1.969   1.00 68.60  ? 355 ASN   A N   1 
ATOM   1703 C  CA  . ASN   A 1 225 ? -32.173 25.438  1.196   1.00 79.74  ? 355 ASN   A CA  1 
ATOM   1704 C  C   . ASN   A 1 225 ? -31.334 26.717  1.201   1.00 70.62  ? 355 ASN   A C   1 
ATOM   1705 O  O   . ASN   A 1 225 ? -31.859 27.821  1.053   1.00 82.11  ? 355 ASN   A O   1 
ATOM   1706 C  CB  . ASN   A 1 225 ? -33.581 25.713  1.733   1.00 75.04  ? 355 ASN   A CB  1 
ATOM   1707 C  CG  . ASN   A 1 225 ? -34.593 25.927  0.635   1.00 81.44  ? 355 ASN   A CG  1 
ATOM   1708 O  OD1 . ASN   A 1 225 ? -34.730 25.108  -0.271  1.00 93.83  ? 355 ASN   A OD1 1 
ATOM   1709 N  ND2 . ASN   A 1 225 ? -35.292 27.050  0.695   1.00 81.98  ? 355 ASN   A ND2 1 
ATOM   1710 N  N   . LYS   A 1 226 ? -30.023 26.570  1.401   1.00 67.94  ? 357 LYS   A N   1 
ATOM   1711 C  CA  . LYS   A 1 226 ? -29.120 27.707  1.492   1.00 68.60  ? 357 LYS   A CA  1 
ATOM   1712 C  C   . LYS   A 1 226 ? -28.901 28.286  0.098   1.00 71.90  ? 357 LYS   A C   1 
ATOM   1713 O  O   . LYS   A 1 226 ? -29.449 27.799  -0.903  1.00 83.37  ? 357 LYS   A O   1 
ATOM   1714 C  CB  . LYS   A 1 226 ? -27.790 27.297  2.128   1.00 72.68  ? 357 LYS   A CB  1 
ATOM   1715 C  CG  . LYS   A 1 226 ? -27.720 27.557  3.627   1.00 61.93  ? 357 LYS   A CG  1 
ATOM   1716 C  CD  . LYS   A 1 226 ? -26.444 26.989  4.260   1.00 67.59  ? 357 LYS   A CD  1 
ATOM   1717 C  CE  . LYS   A 1 226 ? -25.187 27.534  3.593   1.00 76.04  ? 357 LYS   A CE  1 
ATOM   1718 N  NZ  . LYS   A 1 226 ? -24.156 28.000  4.559   1.00 75.80  ? 357 LYS   A NZ  1 
ATOM   1719 N  N   . THR   A 1 227 ? -28.081 29.333  0.022   1.00 73.74  ? 358 THR   A N   1 
ATOM   1720 C  CA  . THR   A 1 227 ? -27.794 29.988  -1.249  1.00 77.71  ? 358 THR   A CA  1 
ATOM   1721 C  C   . THR   A 1 227 ? -26.598 29.299  -1.904  1.00 70.90  ? 358 THR   A C   1 
ATOM   1722 O  O   . THR   A 1 227 ? -25.494 29.267  -1.339  1.00 61.00  ? 358 THR   A O   1 
ATOM   1723 C  CB  . THR   A 1 227 ? -27.526 31.480  -1.068  1.00 72.65  ? 358 THR   A CB  1 
ATOM   1724 O  OG1 . THR   A 1 227 ? -28.764 32.141  -0.803  1.00 80.60  ? 358 THR   A OG1 1 
ATOM   1725 C  CG2 . THR   A 1 227 ? -26.930 32.055  -2.337  1.00 69.94  ? 358 THR   A CG2 1 
ATOM   1726 N  N   . ILE   A 1 228 ? -26.825 28.745  -3.089  1.00 68.13  ? 359 ILE   A N   1 
ATOM   1727 C  CA  . ILE   A 1 228 ? -25.811 27.990  -3.812  1.00 58.86  ? 359 ILE   A CA  1 
ATOM   1728 C  C   . ILE   A 1 228 ? -25.163 28.923  -4.821  1.00 61.75  ? 359 ILE   A C   1 
ATOM   1729 O  O   . ILE   A 1 228 ? -25.856 29.561  -5.622  1.00 63.91  ? 359 ILE   A O   1 
ATOM   1730 C  CB  . ILE   A 1 228 ? -26.435 26.763  -4.501  1.00 66.71  ? 359 ILE   A CB  1 
ATOM   1731 C  CG1 . ILE   A 1 228 ? -27.023 25.791  -3.459  1.00 53.01  ? 359 ILE   A CG1 1 
ATOM   1732 C  CG2 . ILE   A 1 228 ? -25.420 26.054  -5.382  1.00 61.60  ? 359 ILE   A CG2 1 
ATOM   1733 C  CD1 . ILE   A 1 228 ? -26.108 25.506  -2.285  1.00 57.79  ? 359 ILE   A CD1 1 
ATOM   1734 N  N   . ILE   A 1 229 ? -23.839 29.014  -4.780  1.00 57.57  ? 360 ILE   A N   1 
ATOM   1735 C  CA  . ILE   A 1 229 ? -23.076 29.897  -5.654  1.00 61.81  ? 360 ILE   A CA  1 
ATOM   1736 C  C   . ILE   A 1 229 ? -21.936 29.117  -6.284  1.00 61.30  ? 360 ILE   A C   1 
ATOM   1737 O  O   . ILE   A 1 229 ? -21.231 28.383  -5.586  1.00 54.88  ? 360 ILE   A O   1 
ATOM   1738 C  CB  . ILE   A 1 229 ? -22.505 31.088  -4.868  1.00 64.35  ? 360 ILE   A CB  1 
ATOM   1739 C  CG1 . ILE   A 1 229 ? -23.592 31.715  -4.006  1.00 59.00  ? 360 ILE   A CG1 1 
ATOM   1740 C  CG2 . ILE   A 1 229 ? -21.844 32.072  -5.807  1.00 62.31  ? 360 ILE   A CG2 1 
ATOM   1741 C  CD1 . ILE   A 1 229 ? -23.079 32.193  -2.681  1.00 74.31  ? 360 ILE   A CD1 1 
ATOM   1742 N  N   . PHE   A 1 230 ? -21.726 29.301  -7.588  1.00 57.63  ? 361 PHE   A N   1 
ATOM   1743 C  CA  . PHE   A 1 230 ? -20.604 28.677  -8.278  1.00 49.80  ? 361 PHE   A CA  1 
ATOM   1744 C  C   . PHE   A 1 230 ? -19.483 29.687  -8.491  1.00 58.18  ? 361 PHE   A C   1 
ATOM   1745 O  O   . PHE   A 1 230 ? -19.727 30.879  -8.683  1.00 63.40  ? 361 PHE   A O   1 
ATOM   1746 C  CB  . PHE   A 1 230 ? -21.041 28.096  -9.626  1.00 57.15  ? 361 PHE   A CB  1 
ATOM   1747 C  CG  . PHE   A 1 230 ? -21.990 26.935  -9.503  1.00 61.92  ? 361 PHE   A CG  1 
ATOM   1748 C  CD1 . PHE   A 1 230 ? -21.521 25.675  -9.167  1.00 50.14  ? 361 PHE   A CD1 1 
ATOM   1749 C  CD2 . PHE   A 1 230 ? -23.353 27.103  -9.719  1.00 55.52  ? 361 PHE   A CD2 1 
ATOM   1750 C  CE1 . PHE   A 1 230 ? -22.389 24.605  -9.039  1.00 56.52  ? 361 PHE   A CE1 1 
ATOM   1751 C  CE2 . PHE   A 1 230 ? -24.225 26.036  -9.593  1.00 59.40  ? 361 PHE   A CE2 1 
ATOM   1752 C  CZ  . PHE   A 1 230 ? -23.744 24.781  -9.245  1.00 53.50  ? 361 PHE   A CZ  1 
ATOM   1753 N  N   . GLN   A 1 231 ? -18.244 29.206  -8.469  1.00 50.79  ? 362 GLN   A N   1 
ATOM   1754 C  CA  . GLN   A 1 231 ? -17.118 30.099  -8.678  1.00 52.37  ? 362 GLN   A CA  1 
ATOM   1755 C  C   . GLN   A 1 231 ? -15.975 29.329  -9.354  1.00 59.87  ? 362 GLN   A C   1 
ATOM   1756 O  O   . GLN   A 1 231 ? -15.884 28.115  -9.196  1.00 57.55  ? 362 GLN   A O   1 
ATOM   1757 C  CB  . GLN   A 1 231 ? -16.649 30.704  -7.352  1.00 62.94  ? 362 GLN   A CB  1 
ATOM   1758 C  CG  . GLN   A 1 231 ? -17.571 31.817  -6.894  1.00 68.65  ? 362 GLN   A CG  1 
ATOM   1759 C  CD  . GLN   A 1 231 ? -17.496 33.046  -7.786  1.00 70.67  ? 362 GLN   A CD  1 
ATOM   1760 O  OE1 . GLN   A 1 231 ? -16.591 33.864  -7.650  1.00 77.70  ? 362 GLN   A OE1 1 
ATOM   1761 N  NE2 . GLN   A 1 231 ? -18.431 33.161  -8.721  1.00 69.65  ? 362 GLN   A NE2 1 
ATOM   1762 N  N   . PRO   A 1 232 ? -15.142 30.019  -10.120 1.00 64.04  ? 363 PRO   A N   1 
ATOM   1763 C  CA  . PRO   A 1 232 ? -14.010 29.328  -10.769 1.00 51.38  ? 363 PRO   A CA  1 
ATOM   1764 C  C   . PRO   A 1 232 ? -13.044 28.775  -9.743  1.00 54.18  ? 363 PRO   A C   1 
ATOM   1765 O  O   . PRO   A 1 232 ? -13.145 29.096  -8.544  1.00 55.57  ? 363 PRO   A O   1 
ATOM   1766 C  CB  . PRO   A 1 232 ? -13.384 30.447  -11.624 1.00 52.66  ? 363 PRO   A CB  1 
ATOM   1767 C  CG  . PRO   A 1 232 ? -13.841 31.725  -10.966 1.00 66.96  ? 363 PRO   A CG  1 
ATOM   1768 C  CD  . PRO   A 1 232 ? -15.242 31.422  -10.542 1.00 68.00  ? 363 PRO   A CD  1 
ATOM   1769 N  N   . PRO   A 1 233 ? -12.138 27.878  -10.134 1.00 60.06  ? 364 PRO   A N   1 
ATOM   1770 C  CA  . PRO   A 1 233 ? -11.246 27.274  -9.147  1.00 65.90  ? 364 PRO   A CA  1 
ATOM   1771 C  C   . PRO   A 1 233 ? -10.339 28.338  -8.552  1.00 54.13  ? 364 PRO   A C   1 
ATOM   1772 O  O   . PRO   A 1 233 ? -10.003 29.326  -9.209  1.00 60.22  ? 364 PRO   A O   1 
ATOM   1773 C  CB  . PRO   A 1 233 ? -10.478 26.231  -9.962  1.00 52.47  ? 364 PRO   A CB  1 
ATOM   1774 C  CG  . PRO   A 1 233 ? -11.429 25.876  -11.044 1.00 55.06  ? 364 PRO   A CG  1 
ATOM   1775 C  CD  . PRO   A 1 233 ? -12.013 27.202  -11.438 1.00 55.92  ? 364 PRO   A CD  1 
ATOM   1776 N  N   . SER   A 1 234 ? -9.993  28.155  -7.279  1.00 63.94  ? 365 SER   A N   1 
ATOM   1777 C  CA  . SER   A 1 234 ? -9.286  29.183  -6.511  1.00 78.46  ? 365 SER   A CA  1 
ATOM   1778 C  C   . SER   A 1 234 ? -7.781  28.923  -6.549  1.00 83.75  ? 365 SER   A C   1 
ATOM   1779 O  O   . SER   A 1 234 ? -7.098  28.807  -5.528  1.00 88.91  ? 365 SER   A O   1 
ATOM   1780 C  CB  . SER   A 1 234 ? -9.813  29.245  -5.078  1.00 70.27  ? 365 SER   A CB  1 
ATOM   1781 O  OG  . SER   A 1 234 ? -9.524  28.087  -4.313  1.00 66.44  ? 365 SER   A OG  1 
ATOM   1782 N  N   . GLY   A 1 235 ? -7.274  28.828  -7.772  1.00 71.22  ? 366 GLY   A N   1 
ATOM   1783 C  CA  . GLY   A 1 235 ? -5.871  28.570  -7.998  1.00 68.01  ? 366 GLY   A CA  1 
ATOM   1784 C  C   . GLY   A 1 235 ? -5.621  27.103  -8.274  1.00 77.89  ? 366 GLY   A C   1 
ATOM   1785 O  O   . GLY   A 1 235 ? -6.513  26.244  -8.206  1.00 65.13  ? 366 GLY   A O   1 
ATOM   1786 N  N   . GLY   A 1 236 ? -4.360  26.837  -8.584  1.00 70.86  ? 367 GLY   A N   1 
ATOM   1787 C  CA  . GLY   A 1 236 ? -3.882  25.513  -8.892  1.00 53.00  ? 367 GLY   A CA  1 
ATOM   1788 C  C   . GLY   A 1 236 ? -3.224  25.514  -10.248 1.00 68.12  ? 367 GLY   A C   1 
ATOM   1789 O  O   . GLY   A 1 236 ? -2.983  26.563  -10.858 1.00 62.89  ? 367 GLY   A O   1 
ATOM   1790 N  N   . ASP   A 1 237 ? -2.923  24.314  -10.724 1.00 64.23  ? 368 ASP   A N   1 
ATOM   1791 C  CA  . ASP   A 1 237 ? -2.298  24.208  -12.025 1.00 55.91  ? 368 ASP   A CA  1 
ATOM   1792 C  C   . ASP   A 1 237 ? -3.371  24.197  -13.107 1.00 50.65  ? 368 ASP   A C   1 
ATOM   1793 O  O   . ASP   A 1 237 ? -4.568  24.074  -12.833 1.00 49.08  ? 368 ASP   A O   1 
ATOM   1794 C  CB  . ASP   A 1 237 ? -1.416  22.972  -12.083 1.00 67.70  ? 368 ASP   A CB  1 
ATOM   1795 C  CG  . ASP   A 1 237 ? -0.031  23.279  -12.606 1.00 79.60  ? 368 ASP   A CG  1 
ATOM   1796 O  OD1 . ASP   A 1 237 ? 0.079   24.044  -13.607 1.00 79.44  ? 368 ASP   A OD1 1 
ATOM   1797 O  OD2 . ASP   A 1 237 ? 0.946   22.776  -12.003 1.00 59.35  ? 368 ASP   A OD2 1 
ATOM   1798 N  N   . LEU   A 1 238 ? -2.925  24.342  -14.355 1.00 51.35  ? 369 LEU   A N   1 
ATOM   1799 C  CA  . LEU   A 1 238 ? -3.855  24.538  -15.460 1.00 53.22  ? 369 LEU   A CA  1 
ATOM   1800 C  C   . LEU   A 1 238 ? -4.782  23.347  -15.648 1.00 50.20  ? 369 LEU   A C   1 
ATOM   1801 O  O   . LEU   A 1 238 ? -5.920  23.529  -16.095 1.00 42.95  ? 369 LEU   A O   1 
ATOM   1802 C  CB  . LEU   A 1 238 ? -3.087  24.835  -16.747 1.00 50.63  ? 369 LEU   A CB  1 
ATOM   1803 C  CG  . LEU   A 1 238 ? -2.313  26.158  -16.813 1.00 56.58  ? 369 LEU   A CG  1 
ATOM   1804 C  CD1 . LEU   A 1 238 ? -1.301  26.179  -17.949 1.00 49.04  ? 369 LEU   A CD1 1 
ATOM   1805 C  CD2 . LEU   A 1 238 ? -3.311  27.274  -16.983 1.00 48.46  ? 369 LEU   A CD2 1 
ATOM   1806 N  N   . GLU   A 1 239 ? -4.333  22.132  -15.305 1.00 47.63  ? 370 GLU   A N   1 
ATOM   1807 C  CA  . GLU   A 1 239 ? -5.197  20.968  -15.477 1.00 50.74  ? 370 GLU   A CA  1 
ATOM   1808 C  C   . GLU   A 1 239 ? -6.399  21.031  -14.548 1.00 54.59  ? 370 GLU   A C   1 
ATOM   1809 O  O   . GLU   A 1 239 ? -7.436  20.429  -14.847 1.00 52.39  ? 370 GLU   A O   1 
ATOM   1810 C  CB  . GLU   A 1 239 ? -4.417  19.668  -15.258 1.00 46.47  ? 370 GLU   A CB  1 
ATOM   1811 C  CG  . GLU   A 1 239 ? -3.330  19.378  -16.301 1.00 55.17  ? 370 GLU   A CG  1 
ATOM   1812 C  CD  . GLU   A 1 239 ? -2.122  20.309  -16.173 1.00 58.10  ? 370 GLU   A CD  1 
ATOM   1813 O  OE1 . GLU   A 1 239 ? -1.996  20.987  -15.116 1.00 49.60  ? 370 GLU   A OE1 1 
ATOM   1814 O  OE2 . GLU   A 1 239 ? -1.288  20.349  -17.117 1.00 54.79  ? 370 GLU   A OE2 1 
ATOM   1815 N  N   . ILE   A 1 240 ? -6.287  21.757  -13.429 1.00 51.24  ? 371 ILE   A N   1 
ATOM   1816 C  CA  . ILE   A 1 240 ? -7.360  21.865  -12.442 1.00 53.96  ? 371 ILE   A CA  1 
ATOM   1817 C  C   . ILE   A 1 240 ? -8.112  23.180  -12.587 1.00 47.94  ? 371 ILE   A C   1 
ATOM   1818 O  O   . ILE   A 1 240 ? -9.317  23.244  -12.320 1.00 55.97  ? 371 ILE   A O   1 
ATOM   1819 C  CB  . ILE   A 1 240 ? -6.819  21.735  -11.007 1.00 66.29  ? 371 ILE   A CB  1 
ATOM   1820 C  CG1 . ILE   A 1 240 ? -5.893  20.521  -10.900 1.00 63.20  ? 371 ILE   A CG1 1 
ATOM   1821 C  CG2 . ILE   A 1 240 ? -7.981  21.646  -9.999  1.00 60.92  ? 371 ILE   A CG2 1 
ATOM   1822 C  CD1 . ILE   A 1 240 ? -4.431  20.892  -10.855 1.00 62.84  ? 371 ILE   A CD1 1 
ATOM   1823 N  N   . THR   A 1 241 ? -7.420  24.249  -12.987 1.00 42.58  ? 372 THR   A N   1 
ATOM   1824 C  CA  . THR   A 1 241 ? -8.146  25.493  -13.174 1.00 44.78  ? 372 THR   A CA  1 
ATOM   1825 C  C   . THR   A 1 241 ? -8.936  25.506  -14.477 1.00 45.26  ? 372 THR   A C   1 
ATOM   1826 O  O   . THR   A 1 241 ? -9.919  26.240  -14.569 1.00 48.22  ? 372 THR   A O   1 
ATOM   1827 C  CB  . THR   A 1 241 ? -7.186  26.684  -13.102 1.00 50.85  ? 372 THR   A CB  1 
ATOM   1828 O  OG1 . THR   A 1 241 ? -6.190  26.580  -14.132 1.00 45.17  ? 372 THR   A OG1 1 
ATOM   1829 C  CG2 . THR   A 1 241 ? -6.496  26.738  -11.752 1.00 49.60  ? 372 THR   A CG2 1 
ATOM   1830 N  N   . MET   A 1 242 ? -8.553  24.690  -15.463 1.00 42.92  ? 373 MET   A N   1 
ATOM   1831 C  CA  . MET   A 1 242 ? -9.248  24.558  -16.740 1.00 39.39  ? 373 MET   A CA  1 
ATOM   1832 C  C   . MET   A 1 242 ? -9.929  23.195  -16.861 1.00 45.76  ? 373 MET   A C   1 
ATOM   1833 O  O   . MET   A 1 242 ? -9.513  22.206  -16.241 1.00 38.12  ? 373 MET   A O   1 
ATOM   1834 C  CB  . MET   A 1 242 ? -8.291  24.692  -17.920 1.00 41.97  ? 373 MET   A CB  1 
ATOM   1835 C  CG  . MET   A 1 242 ? -7.350  25.887  -17.877 1.00 45.44  ? 373 MET   A CG  1 
ATOM   1836 S  SD  . MET   A 1 242 ? -8.083  27.310  -18.660 1.00 60.71  ? 373 MET   A SD  1 
ATOM   1837 C  CE  . MET   A 1 242 ? -9.072  27.965  -17.313 1.00 59.32  ? 373 MET   A CE  1 
ATOM   1838 N  N   . HIS   A 1 243 ? -10.974 23.143  -17.698 1.00 41.78  ? 374 HIS   A N   1 
ATOM   1839 C  CA  . HIS   A 1 243 ? -11.513 21.863  -18.142 1.00 35.48  ? 374 HIS   A CA  1 
ATOM   1840 C  C   . HIS   A 1 243 ? -10.484 21.276  -19.085 1.00 37.19  ? 374 HIS   A C   1 
ATOM   1841 O  O   . HIS   A 1 243 ? -10.204 21.835  -20.149 1.00 36.29  ? 374 HIS   A O   1 
ATOM   1842 C  CB  . HIS   A 1 243 ? -12.870 22.036  -18.817 1.00 34.10  ? 374 HIS   A CB  1 
ATOM   1843 C  CG  . HIS   A 1 243 ? -13.336 20.844  -19.590 1.00 38.34  ? 374 HIS   A CG  1 
ATOM   1844 N  ND1 . HIS   A 1 243 ? -13.264 19.560  -19.097 1.00 35.64  ? 374 HIS   A ND1 1 
ATOM   1845 C  CD2 . HIS   A 1 243 ? -13.894 20.745  -20.821 1.00 40.39  ? 374 HIS   A CD2 1 
ATOM   1846 C  CE1 . HIS   A 1 243 ? -13.752 18.722  -19.995 1.00 43.02  ? 374 HIS   A CE1 1 
ATOM   1847 N  NE2 . HIS   A 1 243 ? -14.145 19.417  -21.047 1.00 33.76  ? 374 HIS   A NE2 1 
ATOM   1848 N  N   . SER   A 1 244 ? -9.841  20.211  -18.660 1.00 37.17  ? 375 SER   A N   1 
ATOM   1849 C  CA  . SER   A 1 244 ? -8.786  19.592  -19.439 1.00 38.56  ? 375 SER   A CA  1 
ATOM   1850 C  C   . SER   A 1 244 ? -9.312  18.259  -19.965 1.00 32.49  ? 375 SER   A C   1 
ATOM   1851 O  O   . SER   A 1 244 ? -10.145 17.626  -19.316 1.00 40.22  ? 375 SER   A O   1 
ATOM   1852 C  CB  . SER   A 1 244 ? -7.547  19.423  -18.558 1.00 39.51  ? 375 SER   A CB  1 
ATOM   1853 O  OG  . SER   A 1 244 ? -6.485  18.806  -19.240 1.00 62.12  ? 375 SER   A OG  1 
ATOM   1854 N  N   . PHE   A 1 245 ? -8.884  17.854  -21.162 1.00 38.93  ? 376 PHE   A N   1 
ATOM   1855 C  CA  . PHE   A 1 245 ? -9.255  16.545  -21.711 1.00 38.97  ? 376 PHE   A CA  1 
ATOM   1856 C  C   . PHE   A 1 245 ? -8.419  16.289  -22.957 1.00 48.15  ? 376 PHE   A C   1 
ATOM   1857 O  O   . PHE   A 1 245 ? -7.776  17.197  -23.505 1.00 43.76  ? 376 PHE   A O   1 
ATOM   1858 C  CB  . PHE   A 1 245 ? -10.740 16.447  -22.066 1.00 33.15  ? 376 PHE   A CB  1 
ATOM   1859 C  CG  . PHE   A 1 245 ? -11.176 17.424  -23.121 1.00 43.25  ? 376 PHE   A CG  1 
ATOM   1860 C  CD1 . PHE   A 1 245 ? -11.378 18.761  -22.795 1.00 42.62  ? 376 PHE   A CD1 1 
ATOM   1861 C  CD2 . PHE   A 1 245 ? -11.382 17.015  -24.434 1.00 40.94  ? 376 PHE   A CD2 1 
ATOM   1862 C  CE1 . PHE   A 1 245 ? -11.785 19.671  -23.746 1.00 51.07  ? 376 PHE   A CE1 1 
ATOM   1863 C  CE2 . PHE   A 1 245 ? -11.785 17.924  -25.401 1.00 46.16  ? 376 PHE   A CE2 1 
ATOM   1864 C  CZ  . PHE   A 1 245 ? -11.989 19.260  -25.055 1.00 46.38  ? 376 PHE   A CZ  1 
ATOM   1865 N  N   . ASN   A 1 246 ? -8.473  15.052  -23.431 1.00 43.74  ? 377 ASN   A N   1 
ATOM   1866 C  CA  . ASN   A 1 246 ? -7.742  14.665  -24.626 1.00 46.00  ? 377 ASN   A CA  1 
ATOM   1867 C  C   . ASN   A 1 246 ? -8.719  14.408  -25.762 1.00 46.32  ? 377 ASN   A C   1 
ATOM   1868 O  O   . ASN   A 1 246 ? -9.748  13.746  -25.573 1.00 47.04  ? 377 ASN   A O   1 
ATOM   1869 C  CB  . ASN   A 1 246 ? -6.900  13.422  -24.395 1.00 45.07  ? 377 ASN   A CB  1 
ATOM   1870 C  CG  . ASN   A 1 246 ? -5.901  13.209  -25.501 1.00 47.89  ? 377 ASN   A CG  1 
ATOM   1871 O  OD1 . ASN   A 1 246 ? -6.265  12.893  -26.624 1.00 46.41  ? 377 ASN   A OD1 1 
ATOM   1872 N  ND2 . ASN   A 1 246 ? -4.630  13.394  -25.189 1.00 47.31  ? 377 ASN   A ND2 1 
ATOM   1873 N  N   . CYS   A 1 247 ? -8.368  14.919  -26.944 1.00 44.37  ? 378 CYS   A N   1 
ATOM   1874 C  CA  . CYS   A 1 247 ? -9.202  14.926  -28.142 1.00 41.50  ? 378 CYS   A CA  1 
ATOM   1875 C  C   . CYS   A 1 247 ? -8.330  14.476  -29.312 1.00 53.58  ? 378 CYS   A C   1 
ATOM   1876 O  O   . CYS   A 1 247 ? -7.426  15.209  -29.733 1.00 52.13  ? 378 CYS   A O   1 
ATOM   1877 C  CB  . CYS   A 1 247 ? -9.767  16.335  -28.393 1.00 59.18  ? 378 CYS   A CB  1 
ATOM   1878 S  SG  . CYS   A 1 247 ? -10.725 16.544  -29.931 1.00 63.92  ? 378 CYS   A SG  1 
ATOM   1879 N  N   . ARG   A 1 248 ? -8.587  13.279  -29.836 1.00 44.66  ? 379 ARG   A N   1 
ATOM   1880 C  CA  . ARG   A 1 248 ? -7.798  12.731  -30.938 1.00 49.53  ? 379 ARG   A CA  1 
ATOM   1881 C  C   . ARG   A 1 248 ? -6.300  12.769  -30.641 1.00 57.13  ? 379 ARG   A C   1 
ATOM   1882 O  O   . ARG   A 1 248 ? -5.482  12.998  -31.544 1.00 51.30  ? 379 ARG   A O   1 
ATOM   1883 C  CB  . ARG   A 1 248 ? -8.074  13.476  -32.248 1.00 49.18  ? 379 ARG   A CB  1 
ATOM   1884 C  CG  . ARG   A 1 248 ? -9.537  13.803  -32.454 1.00 64.56  ? 379 ARG   A CG  1 
ATOM   1885 C  CD  . ARG   A 1 248 ? -10.232 12.889  -33.445 1.00 66.33  ? 379 ARG   A CD  1 
ATOM   1886 N  NE  . ARG   A 1 248 ? -11.667 13.159  -33.453 1.00 73.68  ? 379 ARG   A NE  1 
ATOM   1887 C  CZ  . ARG   A 1 248 ? -12.494 12.872  -32.447 1.00 72.96  ? 379 ARG   A CZ  1 
ATOM   1888 N  NH1 . ARG   A 1 248 ? -12.067 12.290  -31.333 1.00 65.15  ? 379 ARG   A NH1 1 
ATOM   1889 N  NH2 . ARG   A 1 248 ? -13.787 13.170  -32.560 1.00 65.37  ? 379 ARG   A NH2 1 
ATOM   1890 N  N   . GLY   A 1 249 ? -5.922  12.590  -29.381 1.00 42.25  ? 380 GLY   A N   1 
ATOM   1891 C  CA  . GLY   A 1 249 ? -4.517  12.605  -29.033 1.00 54.30  ? 380 GLY   A CA  1 
ATOM   1892 C  C   . GLY   A 1 249 ? -3.957  13.953  -28.642 1.00 54.79  ? 380 GLY   A C   1 
ATOM   1893 O  O   . GLY   A 1 249 ? -2.814  14.009  -28.175 1.00 48.44  ? 380 GLY   A O   1 
ATOM   1894 N  N   . GLU   A 1 250 ? -4.729  15.030  -28.793 1.00 42.23  ? 381 GLU   A N   1 
ATOM   1895 C  CA  . GLU   A 1 250 ? -4.299  16.380  -28.449 1.00 45.18  ? 381 GLU   A CA  1 
ATOM   1896 C  C   . GLU   A 1 250 ? -4.894  16.789  -27.101 1.00 46.21  ? 381 GLU   A C   1 
ATOM   1897 O  O   . GLU   A 1 250 ? -6.068  16.523  -26.834 1.00 46.12  ? 381 GLU   A O   1 
ATOM   1898 C  CB  . GLU   A 1 250 ? -4.749  17.365  -29.534 1.00 48.67  ? 381 GLU   A CB  1 
ATOM   1899 C  CG  . GLU   A 1 250 ? -4.284  17.013  -30.938 1.00 48.57  ? 381 GLU   A CG  1 
ATOM   1900 C  CD  . GLU   A 1 250 ? -2.770  17.083  -31.087 1.00 62.15  ? 381 GLU   A CD  1 
ATOM   1901 O  OE1 . GLU   A 1 250 ? -2.101  17.692  -30.221 1.00 71.12  ? 381 GLU   A OE1 1 
ATOM   1902 O  OE2 . GLU   A 1 250 ? -2.235  16.489  -32.045 1.00 61.52  ? 381 GLU   A OE2 1 
ATOM   1903 N  N   . PHE   A 1 251 ? -4.094  17.460  -26.261 1.00 42.71  ? 382 PHE   A N   1 
ATOM   1904 C  CA  . PHE   A 1 251 ? -4.532  17.857  -24.923 1.00 40.85  ? 382 PHE   A CA  1 
ATOM   1905 C  C   . PHE   A 1 251 ? -5.155  19.254  -24.971 1.00 48.80  ? 382 PHE   A C   1 
ATOM   1906 O  O   . PHE   A 1 251 ? -4.464  20.256  -25.218 1.00 39.81  ? 382 PHE   A O   1 
ATOM   1907 C  CB  . PHE   A 1 251 ? -3.369  17.787  -23.935 1.00 41.45  ? 382 PHE   A CB  1 
ATOM   1908 C  CG  . PHE   A 1 251 ? -2.834  16.390  -23.736 1.00 50.87  ? 382 PHE   A CG  1 
ATOM   1909 C  CD1 . PHE   A 1 251 ? -1.837  15.888  -24.549 1.00 52.62  ? 382 PHE   A CD1 1 
ATOM   1910 C  CD2 . PHE   A 1 251 ? -3.363  15.563  -22.752 1.00 55.93  ? 382 PHE   A CD2 1 
ATOM   1911 C  CE1 . PHE   A 1 251 ? -1.355  14.603  -24.371 1.00 53.45  ? 382 PHE   A CE1 1 
ATOM   1912 C  CE2 . PHE   A 1 251 ? -2.893  14.279  -22.579 1.00 54.06  ? 382 PHE   A CE2 1 
ATOM   1913 C  CZ  . PHE   A 1 251 ? -1.887  13.800  -23.387 1.00 48.12  ? 382 PHE   A CZ  1 
ATOM   1914 N  N   . PHE   A 1 252 ? -6.459  19.324  -24.717 1.00 39.70  ? 383 PHE   A N   1 
ATOM   1915 C  CA  . PHE   A 1 252 ? -7.199  20.577  -24.757 1.00 41.87  ? 383 PHE   A CA  1 
ATOM   1916 C  C   . PHE   A 1 252 ? -7.349  21.113  -23.343 1.00 45.01  ? 383 PHE   A C   1 
ATOM   1917 O  O   . PHE   A 1 252 ? -7.583  20.341  -22.404 1.00 40.99  ? 383 PHE   A O   1 
ATOM   1918 C  CB  . PHE   A 1 252 ? -8.598  20.397  -25.361 1.00 44.74  ? 383 PHE   A CB  1 
ATOM   1919 C  CG  . PHE   A 1 252 ? -8.638  20.388  -26.866 1.00 42.57  ? 383 PHE   A CG  1 
ATOM   1920 C  CD1 . PHE   A 1 252 ? -7.890  19.481  -27.594 1.00 51.03  ? 383 PHE   A CD1 1 
ATOM   1921 C  CD2 . PHE   A 1 252 ? -9.446  21.278  -27.546 1.00 44.98  ? 383 PHE   A CD2 1 
ATOM   1922 C  CE1 . PHE   A 1 252 ? -7.946  19.460  -28.997 1.00 54.17  ? 383 PHE   A CE1 1 
ATOM   1923 C  CE2 . PHE   A 1 252 ? -9.517  21.274  -28.931 1.00 53.37  ? 383 PHE   A CE2 1 
ATOM   1924 C  CZ  . PHE   A 1 252 ? -8.767  20.367  -29.663 1.00 59.84  ? 383 PHE   A CZ  1 
ATOM   1925 N  N   . TYR   A 1 253 ? -7.198  22.431  -23.187 1.00 37.39  ? 384 TYR   A N   1 
ATOM   1926 C  CA  . TYR   A 1 253 ? -7.433  23.106  -21.918 1.00 37.78  ? 384 TYR   A CA  1 
ATOM   1927 C  C   . TYR   A 1 253 ? -8.427  24.223  -22.178 1.00 43.26  ? 384 TYR   A C   1 
ATOM   1928 O  O   . TYR   A 1 253 ? -8.127  25.153  -22.940 1.00 47.02  ? 384 TYR   A O   1 
ATOM   1929 C  CB  . TYR   A 1 253 ? -6.142  23.673  -21.333 1.00 41.26  ? 384 TYR   A CB  1 
ATOM   1930 C  CG  . TYR   A 1 253 ? -5.147  22.664  -20.805 1.00 38.80  ? 384 TYR   A CG  1 
ATOM   1931 C  CD1 . TYR   A 1 253 ? -4.588  21.699  -21.637 1.00 45.55  ? 384 TYR   A CD1 1 
ATOM   1932 C  CD2 . TYR   A 1 253 ? -4.691  22.748  -19.512 1.00 37.77  ? 384 TYR   A CD2 1 
ATOM   1933 C  CE1 . TYR   A 1 253 ? -3.655  20.806  -21.163 1.00 49.22  ? 384 TYR   A CE1 1 
ATOM   1934 C  CE2 . TYR   A 1 253 ? -3.753  21.873  -19.029 1.00 48.30  ? 384 TYR   A CE2 1 
ATOM   1935 C  CZ  . TYR   A 1 253 ? -3.242  20.903  -19.855 1.00 52.48  ? 384 TYR   A CZ  1 
ATOM   1936 O  OH  . TYR   A 1 253 ? -2.304  20.019  -19.359 1.00 68.49  ? 384 TYR   A OH  1 
ATOM   1937 N  N   . CYS   A 1 254 ? -9.597  24.151  -21.538 1.00 40.47  ? 385 CYS   A N   1 
ATOM   1938 C  CA  . CYS   A 1 254 ? -10.695 25.052  -21.863 1.00 45.52  ? 385 CYS   A CA  1 
ATOM   1939 C  C   . CYS   A 1 254 ? -11.116 25.845  -20.636 1.00 42.22  ? 385 CYS   A C   1 
ATOM   1940 O  O   . CYS   A 1 254 ? -11.427 25.272  -19.590 1.00 38.48  ? 385 CYS   A O   1 
ATOM   1941 C  CB  . CYS   A 1 254 ? -11.865 24.265  -22.468 1.00 37.87  ? 385 CYS   A CB  1 
ATOM   1942 S  SG  . CYS   A 1 254 ? -11.365 23.543  -24.078 1.00 53.55  ? 385 CYS   A SG  1 
ATOM   1943 N  N   . ASN   A 1 255 ? -11.112 27.162  -20.774 1.00 43.05  ? 386 ASN   A N   1 
ATOM   1944 C  CA  . ASN   A 1 255 ? -11.537 28.049  -19.701 1.00 41.29  ? 386 ASN   A CA  1 
ATOM   1945 C  C   . ASN   A 1 255 ? -13.047 27.956  -19.512 1.00 46.91  ? 386 ASN   A C   1 
ATOM   1946 O  O   . ASN   A 1 255 ? -13.812 28.329  -20.407 1.00 45.59  ? 386 ASN   A O   1 
ATOM   1947 C  CB  . ASN   A 1 255 ? -11.134 29.477  -20.031 1.00 49.70  ? 386 ASN   A CB  1 
ATOM   1948 C  CG  . ASN   A 1 255 ? -11.399 30.434  -18.893 1.00 52.14  ? 386 ASN   A CG  1 
ATOM   1949 O  OD1 . ASN   A 1 255 ? -12.428 30.358  -18.204 1.00 46.65  ? 386 ASN   A OD1 1 
ATOM   1950 N  ND2 . ASN   A 1 255 ? -10.460 31.336  -18.678 1.00 52.44  ? 386 ASN   A ND2 1 
ATOM   1951 N  N   . THR   A 1 256 ? -13.484 27.476  -18.349 1.00 35.20  ? 387 THR   A N   1 
ATOM   1952 C  CA  . THR   A 1 256 ? -14.900 27.253  -18.101 1.00 49.60  ? 387 THR   A CA  1 
ATOM   1953 C  C   . THR   A 1 256 ? -15.517 28.333  -17.231 1.00 42.89  ? 387 THR   A C   1 
ATOM   1954 O  O   . THR   A 1 256 ? -16.596 28.116  -16.668 1.00 45.49  ? 387 THR   A O   1 
ATOM   1955 C  CB  . THR   A 1 256 ? -15.132 25.894  -17.436 1.00 40.30  ? 387 THR   A CB  1 
ATOM   1956 O  OG1 . THR   A 1 256 ? -14.453 25.890  -16.175 1.00 45.41  ? 387 THR   A OG1 1 
ATOM   1957 C  CG2 . THR   A 1 256 ? -14.646 24.745  -18.325 1.00 36.89  ? 387 THR   A CG2 1 
ATOM   1958 N  N   . THR   A 1 257 ? -14.845 29.477  -17.077 1.00 46.33  ? 388 THR   A N   1 
ATOM   1959 C  CA  . THR   A 1 257 ? -15.433 30.547  -16.271 1.00 47.98  ? 388 THR   A CA  1 
ATOM   1960 C  C   . THR   A 1 257 ? -16.849 30.873  -16.726 1.00 48.78  ? 388 THR   A C   1 
ATOM   1961 O  O   . THR   A 1 257 ? -17.738 31.065  -15.896 1.00 56.79  ? 388 THR   A O   1 
ATOM   1962 C  CB  . THR   A 1 257 ? -14.541 31.782  -16.296 1.00 48.39  ? 388 THR   A CB  1 
ATOM   1963 O  OG1 . THR   A 1 257 ? -13.369 31.503  -15.524 1.00 57.90  ? 388 THR   A OG1 1 
ATOM   1964 C  CG2 . THR   A 1 257 ? -15.246 32.974  -15.666 1.00 60.70  ? 388 THR   A CG2 1 
ATOM   1965 N  N   . GLN   A 1 258 ? -17.091 30.893  -18.036 1.00 57.62  ? 389 GLN   A N   1 
ATOM   1966 C  CA  . GLN   A 1 258 ? -18.411 31.248  -18.543 1.00 52.37  ? 389 GLN   A CA  1 
ATOM   1967 C  C   . GLN   A 1 258 ? -19.451 30.208  -18.182 1.00 56.44  ? 389 GLN   A C   1 
ATOM   1968 O  O   . GLN   A 1 258 ? -20.647 30.515  -18.164 1.00 62.30  ? 389 GLN   A O   1 
ATOM   1969 C  CB  . GLN   A 1 258 ? -18.345 31.420  -20.048 1.00 56.47  ? 389 GLN   A CB  1 
ATOM   1970 C  CG  . GLN   A 1 258 ? -17.748 32.719  -20.507 1.00 41.66  ? 389 GLN   A CG  1 
ATOM   1971 C  CD  . GLN   A 1 258 ? -17.770 32.787  -22.005 1.00 50.08  ? 389 GLN   A CD  1 
ATOM   1972 O  OE1 . GLN   A 1 258 ? -18.807 33.055  -22.615 1.00 53.23  ? 389 GLN   A OE1 1 
ATOM   1973 N  NE2 . GLN   A 1 258 ? -16.626 32.507  -22.622 1.00 52.87  ? 389 GLN   A NE2 1 
ATOM   1974 N  N   . LEU   A 1 259 ? -19.029 28.970  -17.931 1.00 54.64  ? 390 LEU   A N   1 
ATOM   1975 C  CA  . LEU   A 1 259 ? -19.958 27.973  -17.430 1.00 55.79  ? 390 LEU   A CA  1 
ATOM   1976 C  C   . LEU   A 1 259 ? -20.289 28.203  -15.967 1.00 50.53  ? 390 LEU   A C   1 
ATOM   1977 O  O   . LEU   A 1 259 ? -21.441 28.015  -15.567 1.00 63.68  ? 390 LEU   A O   1 
ATOM   1978 C  CB  . LEU   A 1 259 ? -19.381 26.572  -17.597 1.00 53.43  ? 390 LEU   A CB  1 
ATOM   1979 C  CG  . LEU   A 1 259 ? -19.327 26.112  -19.038 1.00 58.88  ? 390 LEU   A CG  1 
ATOM   1980 C  CD1 . LEU   A 1 259 ? -18.351 24.959  -19.143 1.00 55.56  ? 390 LEU   A CD1 1 
ATOM   1981 C  CD2 . LEU   A 1 259 ? -20.716 25.719  -19.556 1.00 64.02  ? 390 LEU   A CD2 1 
ATOM   1982 N  N   . PHE   A 1 260 ? -19.309 28.597  -15.153 1.00 50.76  ? 391 PHE   A N   1 
ATOM   1983 C  CA  . PHE   A 1 260 ? -19.553 28.697  -13.717 1.00 55.95  ? 391 PHE   A CA  1 
ATOM   1984 C  C   . PHE   A 1 260 ? -19.568 30.149  -13.253 1.00 71.77  ? 391 PHE   A C   1 
ATOM   1985 O  O   . PHE   A 1 260 ? -18.886 30.519  -12.284 1.00 69.12  ? 391 PHE   A O   1 
ATOM   1986 C  CB  . PHE   A 1 260 ? -18.522 27.877  -12.941 1.00 53.74  ? 391 PHE   A CB  1 
ATOM   1987 C  CG  . PHE   A 1 260 ? -18.454 26.446  -13.379 1.00 50.14  ? 391 PHE   A CG  1 
ATOM   1988 C  CD1 . PHE   A 1 260 ? -19.468 25.560  -13.043 1.00 59.34  ? 391 PHE   A CD1 1 
ATOM   1989 C  CD2 . PHE   A 1 260 ? -17.411 26.000  -14.156 1.00 40.58  ? 391 PHE   A CD2 1 
ATOM   1990 C  CE1 . PHE   A 1 260 ? -19.420 24.252  -13.457 1.00 49.25  ? 391 PHE   A CE1 1 
ATOM   1991 C  CE2 . PHE   A 1 260 ? -17.363 24.720  -14.581 1.00 52.69  ? 391 PHE   A CE2 1 
ATOM   1992 C  CZ  . PHE   A 1 260 ? -18.368 23.835  -14.235 1.00 56.91  ? 391 PHE   A CZ  1 
ATOM   1993 N  N   . ASN   A 1 261 ? -20.354 30.968  -13.958 1.00 76.41  ? 392 ASN   A N   1 
ATOM   1994 C  CA  . ASN   A 1 261 ? -20.786 32.286  -13.505 1.00 78.61  ? 392 ASN   A CA  1 
ATOM   1995 C  C   . ASN   A 1 261 ? -22.287 32.246  -13.220 1.00 86.40  ? 392 ASN   A C   1 
ATOM   1996 O  O   . ASN   A 1 261 ? -23.079 31.729  -14.027 1.00 76.70  ? 392 ASN   A O   1 
ATOM   1997 C  CB  . ASN   A 1 261 ? -20.417 33.384  -14.520 1.00 75.92  ? 392 ASN   A CB  1 
ATOM   1998 C  CG  . ASN   A 1 261 ? -21.509 33.641  -15.575 1.00 81.24  ? 392 ASN   A CG  1 
ATOM   1999 O  OD1 . ASN   A 1 261 ? -22.384 32.811  -15.805 1.00 85.69  ? 392 ASN   A OD1 1 
ATOM   2000 N  ND2 . ASN   A 1 261 ? -21.441 34.802  -16.230 1.00 82.90  ? 392 ASN   A ND2 1 
ATOM   2001 N  N   . ASN   A 1 262 ? -22.662 32.755  -12.048 1.00 78.82  ? 393 ASN   A N   1 
ATOM   2002 C  CA  . ASN   A 1 262 ? -24.025 32.688  -11.544 1.00 78.22  ? 393 ASN   A CA  1 
ATOM   2003 C  C   . ASN   A 1 262 ? -24.961 33.700  -12.192 1.00 83.55  ? 393 ASN   A C   1 
ATOM   2004 O  O   . ASN   A 1 262 ? -26.165 33.671  -11.899 1.00 75.67  ? 393 ASN   A O   1 
ATOM   2005 C  CB  . ASN   A 1 262 ? -23.992 32.896  -10.032 1.00 68.88  ? 393 ASN   A CB  1 
ATOM   2006 C  CG  . ASN   A 1 262 ? -23.169 31.842  -9.329  1.00 61.80  ? 393 ASN   A CG  1 
ATOM   2007 O  OD1 . ASN   A 1 262 ? -23.694 30.825  -8.875  1.00 65.07  ? 393 ASN   A OD1 1 
ATOM   2008 N  ND2 . ASN   A 1 262 ? -21.867 32.071  -9.249  1.00 63.37  ? 393 ASN   A ND2 1 
ATOM   2009 N  N   . THR   A 1 263 ? -24.426 34.604  -13.023 1.00 86.32  ? 394 THR   A N   1 
ATOM   2010 C  CA  . THR   A 1 263 ? -25.216 35.573  -13.775 1.00 83.84  ? 394 THR   A CA  1 
ATOM   2011 C  C   . THR   A 1 263 ? -26.563 35.001  -14.156 1.00 77.78  ? 394 THR   A C   1 
ATOM   2012 O  O   . THR   A 1 263 ? -27.617 35.534  -13.801 1.00 69.58  ? 394 THR   A O   1 
ATOM   2013 C  CB  . THR   A 1 263 ? -24.442 35.976  -15.035 1.00 93.88  ? 394 THR   A CB  1 
ATOM   2014 O  OG1 . THR   A 1 263 ? -23.071 36.199  -14.685 1.00 99.14  ? 394 THR   A OG1 1 
ATOM   2015 C  CG2 . THR   A 1 263 ? -25.010 37.222  -15.663 1.00 87.22  ? 394 THR   A CG2 1 
ATOM   2016 N  N   . CYS   A 1 264 ? -26.510 33.894  -14.875 1.00 77.09  ? 395 CYS   A N   1 
ATOM   2017 C  CA  . CYS   A 1 264 ? -27.655 33.132  -15.303 1.00 76.61  ? 395 CYS   A CA  1 
ATOM   2018 C  C   . CYS   A 1 264 ? -28.088 32.074  -14.309 1.00 87.39  ? 395 CYS   A C   1 
ATOM   2019 O  O   . CYS   A 1 264 ? -29.266 31.706  -14.224 1.00 84.53  ? 395 CYS   A O   1 
ATOM   2020 C  CB  . CYS   A 1 264 ? -27.358 32.503  -16.695 1.00 83.09  ? 395 CYS   A CB  1 
ATOM   2021 S  SG  . CYS   A 1 264 ? -26.200 33.464  -17.775 1.00 80.89  ? 395 CYS   A SG  1 
ATOM   2022 N  N   . LYS   A 1 271 ? -31.764 37.125  -17.983 1.00 75.37  ? 408 LYS   A N   1 
ATOM   2023 C  CA  . LYS   A 1 271 ? -30.928 38.215  -18.480 1.00 70.72  ? 408 LYS   A CA  1 
ATOM   2024 C  C   . LYS   A 1 271 ? -30.719 37.848  -19.937 1.00 98.06  ? 408 LYS   A C   1 
ATOM   2025 O  O   . LYS   A 1 271 ? -31.215 36.737  -20.341 1.00 104.93 ? 408 LYS   A O   1 
ATOM   2026 C  CB  . LYS   A 1 271 ? -29.630 38.268  -17.680 1.00 77.81  ? 408 LYS   A CB  1 
ATOM   2027 C  CG  . LYS   A 1 271 ? -29.414 39.549  -16.930 1.00 82.41  ? 408 LYS   A CG  1 
ATOM   2028 C  CD  . LYS   A 1 271 ? -30.736 40.220  -16.473 1.00 82.67  ? 408 LYS   A CD  1 
ATOM   2029 C  CE  . LYS   A 1 271 ? -30.330 41.528  -15.779 1.00 74.93  ? 408 LYS   A CE  1 
ATOM   2030 N  NZ  . LYS   A 1 271 ? -31.286 42.712  -15.927 1.00 69.47  ? 408 LYS   A NZ  1 
ATOM   2031 N  N   . GLY   A 1 272 ? -29.982 38.674  -20.710 1.00 83.90  ? 409 GLY   A N   1 
ATOM   2032 C  CA  . GLY   A 1 272 ? -29.603 38.358  -22.087 1.00 78.60  ? 409 GLY   A CA  1 
ATOM   2033 C  C   . GLY   A 1 272 ? -28.383 37.459  -22.292 1.00 89.37  ? 409 GLY   A C   1 
ATOM   2034 O  O   . GLY   A 1 272 ? -27.491 37.784  -23.096 1.00 94.32  ? 409 GLY   A O   1 
ATOM   2035 N  N   . CYS   A 1 273 ? -28.362 36.320  -21.585 1.00 92.69  ? 410 CYS   A N   1 
ATOM   2036 C  CA  . CYS   A 1 273 ? -27.340 35.263  -21.625 1.00 90.18  ? 410 CYS   A CA  1 
ATOM   2037 C  C   . CYS   A 1 273 ? -27.949 33.897  -21.919 1.00 88.36  ? 410 CYS   A C   1 
ATOM   2038 O  O   . CYS   A 1 273 ? -28.073 33.053  -21.028 1.00 82.88  ? 410 CYS   A O   1 
ATOM   2039 C  CB  . CYS   A 1 273 ? -26.584 35.301  -20.285 1.00 102.76 ? 410 CYS   A CB  1 
ATOM   2040 S  SG  . CYS   A 1 273 ? -27.487 34.524  -18.854 1.00 118.89 ? 410 CYS   A SG  1 
ATOM   2041 N  N   . ASN   A 1 274 ? -28.302 33.658  -23.180 1.00 85.71  ? 411 ASN   A N   1 
ATOM   2042 C  CA  . ASN   A 1 274 ? -28.794 32.313  -23.442 1.00 75.13  ? 411 ASN   A CA  1 
ATOM   2043 C  C   . ASN   A 1 274 ? -28.692 31.955  -24.917 1.00 78.50  ? 411 ASN   A C   1 
ATOM   2044 O  O   . ASN   A 1 274 ? -29.543 31.253  -25.473 1.00 74.84  ? 411 ASN   A O   1 
ATOM   2045 C  CB  . ASN   A 1 274 ? -30.212 32.151  -22.876 1.00 79.19  ? 411 ASN   A CB  1 
ATOM   2046 C  CG  . ASN   A 1 274 ? -31.278 32.598  -23.824 1.00 84.31  ? 411 ASN   A CG  1 
ATOM   2047 O  OD1 . ASN   A 1 274 ? -31.065 33.499  -24.637 1.00 86.30  ? 411 ASN   A OD1 1 
ATOM   2048 N  ND2 . ASN   A 1 274 ? -32.451 31.978  -23.725 1.00 81.31  ? 411 ASN   A ND2 1 
ATOM   2049 N  N   . GLY   A 1 275 ? -27.617 32.404  -25.543 1.00 68.78  ? 412 GLY   A N   1 
ATOM   2050 C  CA  . GLY   A 1 275 ? -27.250 31.913  -26.852 1.00 61.96  ? 412 GLY   A CA  1 
ATOM   2051 C  C   . GLY   A 1 275 ? -26.264 30.768  -26.740 1.00 69.49  ? 412 GLY   A C   1 
ATOM   2052 O  O   . GLY   A 1 275 ? -26.337 29.937  -25.825 1.00 65.53  ? 412 GLY   A O   1 
ATOM   2053 N  N   . THR   A 1 276 ? -25.317 30.729  -27.665 1.00 63.58  ? 413 THR   A N   1 
ATOM   2054 C  CA  . THR   A 1 276 ? -24.249 29.752  -27.631 1.00 61.37  ? 413 THR   A CA  1 
ATOM   2055 C  C   . THR   A 1 276 ? -23.102 30.300  -26.793 1.00 60.75  ? 413 THR   A C   1 
ATOM   2056 O  O   . THR   A 1 276 ? -22.757 31.483  -26.884 1.00 56.69  ? 413 THR   A O   1 
ATOM   2057 C  CB  . THR   A 1 276 ? -23.774 29.420  -29.051 1.00 61.78  ? 413 THR   A CB  1 
ATOM   2058 O  OG1 . THR   A 1 276 ? -24.736 28.578  -29.701 1.00 58.48  ? 413 THR   A OG1 1 
ATOM   2059 C  CG2 . THR   A 1 276 ? -22.449 28.699  -29.012 1.00 61.23  ? 413 THR   A CG2 1 
ATOM   2060 N  N   . ILE   A 1 277 ? -22.535 29.435  -25.956 1.00 59.13  ? 414 ILE   A N   1 
ATOM   2061 C  CA  . ILE   A 1 277 ? -21.367 29.755  -25.144 1.00 50.71  ? 414 ILE   A CA  1 
ATOM   2062 C  C   . ILE   A 1 277 ? -20.147 29.208  -25.872 1.00 55.39  ? 414 ILE   A C   1 
ATOM   2063 O  O   . ILE   A 1 277 ? -20.045 27.994  -26.100 1.00 53.33  ? 414 ILE   A O   1 
ATOM   2064 C  CB  . ILE   A 1 277 ? -21.468 29.152  -23.733 1.00 53.44  ? 414 ILE   A CB  1 
ATOM   2065 C  CG1 . ILE   A 1 277 ? -22.583 29.813  -22.924 1.00 59.18  ? 414 ILE   A CG1 1 
ATOM   2066 C  CG2 . ILE   A 1 277 ? -20.146 29.324  -22.998 1.00 49.55  ? 414 ILE   A CG2 1 
ATOM   2067 C  CD1 . ILE   A 1 277 ? -23.113 28.954  -21.755 1.00 50.69  ? 414 ILE   A CD1 1 
ATOM   2068 N  N   . THR   A 1 278 ? -19.236 30.098  -26.254 1.00 48.63  ? 415 THR   A N   1 
ATOM   2069 C  CA  . THR   A 1 278 ? -17.941 29.726  -26.809 1.00 48.24  ? 415 THR   A CA  1 
ATOM   2070 C  C   . THR   A 1 278 ? -16.931 29.838  -25.665 1.00 57.71  ? 415 THR   A C   1 
ATOM   2071 O  O   . THR   A 1 278 ? -16.704 30.933  -25.135 1.00 52.29  ? 415 THR   A O   1 
ATOM   2072 C  CB  . THR   A 1 278 ? -17.584 30.644  -27.986 1.00 55.27  ? 415 THR   A CB  1 
ATOM   2073 O  OG1 . THR   A 1 278 ? -18.634 30.606  -28.949 1.00 61.69  ? 415 THR   A OG1 1 
ATOM   2074 C  CG2 . THR   A 1 278 ? -16.331 30.211  -28.684 1.00 49.25  ? 415 THR   A CG2 1 
ATOM   2075 N  N   . LEU   A 1 279 ? -16.362 28.691  -25.239 1.00 52.91  ? 416 LEU   A N   1 
ATOM   2076 C  CA  . LEU   A 1 279 ? -15.275 28.646  -24.264 1.00 52.10  ? 416 LEU   A CA  1 
ATOM   2077 C  C   . LEU   A 1 279 ? -13.937 28.788  -24.989 1.00 44.55  ? 416 LEU   A C   1 
ATOM   2078 O  O   . LEU   A 1 279 ? -13.711 28.098  -25.988 1.00 44.13  ? 416 LEU   A O   1 
ATOM   2079 C  CB  . LEU   A 1 279 ? -15.304 27.333  -23.482 1.00 43.40  ? 416 LEU   A CB  1 
ATOM   2080 C  CG  . LEU   A 1 279 ? -16.606 27.014  -22.717 1.00 55.46  ? 416 LEU   A CG  1 
ATOM   2081 C  CD1 . LEU   A 1 279 ? -16.538 25.626  -22.076 1.00 43.84  ? 416 LEU   A CD1 1 
ATOM   2082 C  CD2 . LEU   A 1 279 ? -16.988 28.086  -21.668 1.00 49.83  ? 416 LEU   A CD2 1 
ATOM   2083 N  N   . PRO   A 1 280 ? -13.040 29.667  -24.543 1.00 43.25  ? 417 PRO   A N   1 
ATOM   2084 C  CA  . PRO   A 1 280 ? -11.701 29.728  -25.150 1.00 42.99  ? 417 PRO   A CA  1 
ATOM   2085 C  C   . PRO   A 1 280 ? -10.827 28.580  -24.652 1.00 43.69  ? 417 PRO   A C   1 
ATOM   2086 O  O   . PRO   A 1 280 ? -10.800 28.278  -23.454 1.00 40.28  ? 417 PRO   A O   1 
ATOM   2087 C  CB  . PRO   A 1 280 ? -11.167 31.087  -24.681 1.00 33.26  ? 417 PRO   A CB  1 
ATOM   2088 C  CG  . PRO   A 1 280 ? -11.841 31.310  -23.383 1.00 37.38  ? 417 PRO   A CG  1 
ATOM   2089 C  CD  . PRO   A 1 280 ? -13.228 30.714  -23.523 1.00 38.37  ? 417 PRO   A CD  1 
ATOM   2090 N  N   . CYS   A 1 281 ? -10.108 27.948  -25.582 1.00 41.93  ? 418 CYS   A N   1 
ATOM   2091 C  CA  . CYS   A 1 281 ? -9.321  26.759  -25.303 1.00 45.95  ? 418 CYS   A CA  1 
ATOM   2092 C  C   . CYS   A 1 281 ? -7.928  26.911  -25.881 1.00 49.35  ? 418 CYS   A C   1 
ATOM   2093 O  O   . CYS   A 1 281 ? -7.675  27.755  -26.747 1.00 46.65  ? 418 CYS   A O   1 
ATOM   2094 C  CB  . CYS   A 1 281 ? -9.941  25.498  -25.914 1.00 53.43  ? 418 CYS   A CB  1 
ATOM   2095 S  SG  . CYS   A 1 281 ? -11.586 25.106  -25.375 1.00 54.00  ? 418 CYS   A SG  1 
ATOM   2096 N  N   . LYS   A 1 282 ? -7.048  26.018  -25.430 1.00 43.01  ? 419 LYS   A N   1 
ATOM   2097 C  CA  . LYS   A 1 282 ? -5.676  25.938  -25.906 1.00 38.42  ? 419 LYS   A CA  1 
ATOM   2098 C  C   . LYS   A 1 282 ? -5.276  24.476  -25.999 1.00 50.22  ? 419 LYS   A C   1 
ATOM   2099 O  O   . LYS   A 1 282 ? -5.592  23.684  -25.105 1.00 42.54  ? 419 LYS   A O   1 
ATOM   2100 C  CB  . LYS   A 1 282 ? -4.729  26.671  -24.950 1.00 56.61  ? 419 LYS   A CB  1 
ATOM   2101 C  CG  . LYS   A 1 282 ? -3.426  27.206  -25.561 1.00 70.71  ? 419 LYS   A CG  1 
ATOM   2102 C  CD  . LYS   A 1 282 ? -2.500  27.784  -24.455 1.00 74.23  ? 419 LYS   A CD  1 
ATOM   2103 C  CE  . LYS   A 1 282 ? -1.786  29.084  -24.901 1.00 79.23  ? 419 LYS   A CE  1 
ATOM   2104 N  NZ  . LYS   A 1 282 ? -0.609  29.510  -24.056 1.00 63.72  ? 419 LYS   A NZ  1 
ATOM   2105 N  N   . ILE   A 1 283 ? -4.579  24.121  -27.071 1.00 44.37  ? 420 ILE   A N   1 
ATOM   2106 C  CA  . ILE   A 1 283 ? -3.905  22.837  -27.143 1.00 41.24  ? 420 ILE   A CA  1 
ATOM   2107 C  C   . ILE   A 1 283 ? -2.535  23.043  -26.517 1.00 52.17  ? 420 ILE   A C   1 
ATOM   2108 O  O   . ILE   A 1 283 ? -1.739  23.862  -26.988 1.00 48.56  ? 420 ILE   A O   1 
ATOM   2109 C  CB  . ILE   A 1 283 ? -3.816  22.332  -28.582 1.00 44.38  ? 420 ILE   A CB  1 
ATOM   2110 C  CG1 . ILE   A 1 283 ? -5.227  22.064  -29.064 1.00 45.49  ? 420 ILE   A CG1 1 
ATOM   2111 C  CG2 . ILE   A 1 283 ? -3.032  21.054  -28.646 1.00 45.28  ? 420 ILE   A CG2 1 
ATOM   2112 C  CD1 . ILE   A 1 283 ? -5.277  21.430  -30.378 1.00 52.07  ? 420 ILE   A CD1 1 
ATOM   2113 N  N   . LYS   A 1 284 ? -2.289  22.350  -25.416 1.00 46.74  ? 421 LYS   A N   1 
ATOM   2114 C  CA  . LYS   A 1 284 ? -1.021  22.424  -24.712 1.00 51.90  ? 421 LYS   A CA  1 
ATOM   2115 C  C   . LYS   A 1 284 ? -0.144  21.257  -25.145 1.00 52.63  ? 421 LYS   A C   1 
ATOM   2116 O  O   . LYS   A 1 284 ? -0.643  20.176  -25.457 1.00 50.71  ? 421 LYS   A O   1 
ATOM   2117 C  CB  . LYS   A 1 284 ? -1.243  22.386  -23.198 1.00 45.64  ? 421 LYS   A CB  1 
ATOM   2118 C  CG  . LYS   A 1 284 ? -1.824  23.660  -22.619 1.00 51.26  ? 421 LYS   A CG  1 
ATOM   2119 C  CD  . LYS   A 1 284 ? -1.141  24.022  -21.309 1.00 64.28  ? 421 LYS   A CD  1 
ATOM   2120 C  CE  . LYS   A 1 284 ? 0.369   24.125  -21.495 1.00 55.32  ? 421 LYS   A CE  1 
ATOM   2121 N  NZ  . LYS   A 1 284 ? 1.083   24.011  -20.214 1.00 53.38  ? 421 LYS   A NZ  1 
ATOM   2122 N  N   . GLN   A 1 285 ? 1.170   21.500  -25.206 1.00 52.02  ? 422 GLN   A N   1 
ATOM   2123 C  CA  . GLN   A 1 285 ? 2.151   20.466  -25.516 1.00 55.37  ? 422 GLN   A CA  1 
ATOM   2124 C  C   . GLN   A 1 285 ? 2.841   19.943  -24.274 1.00 53.09  ? 422 GLN   A C   1 
ATOM   2125 O  O   . GLN   A 1 285 ? 3.287   18.797  -24.267 1.00 62.47  ? 422 GLN   A O   1 
ATOM   2126 C  CB  . GLN   A 1 285 ? 3.225   20.989  -26.493 1.00 55.81  ? 422 GLN   A CB  1 
ATOM   2127 C  CG  . GLN   A 1 285 ? 2.762   21.188  -27.931 1.00 49.20  ? 422 GLN   A CG  1 
ATOM   2128 C  CD  . GLN   A 1 285 ? 3.838   21.803  -28.830 1.00 67.04  ? 422 GLN   A CD  1 
ATOM   2129 O  OE1 . GLN   A 1 285 ? 3.743   22.967  -29.253 1.00 70.14  ? 422 GLN   A OE1 1 
ATOM   2130 N  NE2 . GLN   A 1 285 ? 4.847   21.005  -29.161 1.00 64.59  ? 422 GLN   A NE2 1 
ATOM   2131 N  N   . ILE   A 1 286 ? 2.930   20.758  -23.230 1.00 40.92  ? 423 ILE   A N   1 
ATOM   2132 C  CA  . ILE   A 1 286 ? 3.556   20.384  -21.966 1.00 55.01  ? 423 ILE   A CA  1 
ATOM   2133 C  C   . ILE   A 1 286 ? 2.451   20.147  -20.941 1.00 61.40  ? 423 ILE   A C   1 
ATOM   2134 O  O   . ILE   A 1 286 ? 1.677   21.059  -20.620 1.00 52.38  ? 423 ILE   A O   1 
ATOM   2135 C  CB  . ILE   A 1 286 ? 4.545   21.458  -21.479 1.00 46.70  ? 423 ILE   A CB  1 
ATOM   2136 C  CG1 . ILE   A 1 286 ? 5.634   21.705  -22.511 1.00 43.00  ? 423 ILE   A CG1 1 
ATOM   2137 C  CG2 . ILE   A 1 286 ? 5.177   21.079  -20.151 1.00 45.08  ? 423 ILE   A CG2 1 
ATOM   2138 C  CD1 . ILE   A 1 286 ? 6.556   22.806  -22.090 1.00 43.72  ? 423 ILE   A CD1 1 
ATOM   2139 N  N   . ILE   A 1 287 ? 2.409   18.932  -20.404 1.00 54.75  ? 424 ILE   A N   1 
ATOM   2140 C  CA  . ILE   A 1 287 ? 1.301   18.450  -19.599 1.00 55.38  ? 424 ILE   A CA  1 
ATOM   2141 C  C   . ILE   A 1 287 ? 1.831   18.022  -18.247 1.00 51.91  ? 424 ILE   A C   1 
ATOM   2142 O  O   . ILE   A 1 287 ? 2.934   17.481  -18.133 1.00 56.27  ? 424 ILE   A O   1 
ATOM   2143 C  CB  . ILE   A 1 287 ? 0.586   17.257  -20.281 1.00 52.04  ? 424 ILE   A CB  1 
ATOM   2144 C  CG1 . ILE   A 1 287 ? 0.252   17.582  -21.728 1.00 57.36  ? 424 ILE   A CG1 1 
ATOM   2145 C  CG2 . ILE   A 1 287 ? -0.683  16.878  -19.541 1.00 61.40  ? 424 ILE   A CG2 1 
ATOM   2146 C  CD1 . ILE   A 1 287 ? -0.746  18.667  -21.875 1.00 57.67  ? 424 ILE   A CD1 1 
ATOM   2147 N  N   . ASN   A 1 288 ? 1.015   18.232  -17.229 1.00 48.79  ? 425 ASN   A N   1 
ATOM   2148 C  CA  . ASN   A 1 288 ? 1.262   17.680  -15.906 1.00 49.62  ? 425 ASN   A CA  1 
ATOM   2149 C  C   . ASN   A 1 288 ? 0.514   16.355  -15.835 1.00 55.97  ? 425 ASN   A C   1 
ATOM   2150 O  O   . ASN   A 1 288 ? -0.720  16.324  -15.764 1.00 49.76  ? 425 ASN   A O   1 
ATOM   2151 C  CB  . ASN   A 1 288 ? 0.818   18.664  -14.836 1.00 50.01  ? 425 ASN   A CB  1 
ATOM   2152 C  CG  . ASN   A 1 288 ? 1.679   19.889  -14.820 1.00 58.84  ? 425 ASN   A CG  1 
ATOM   2153 O  OD1 . ASN   A 1 288 ? 2.896   19.782  -14.950 1.00 61.38  ? 425 ASN   A OD1 1 
ATOM   2154 N  ND2 . ASN   A 1 288 ? 1.072   21.057  -14.673 1.00 55.56  ? 425 ASN   A ND2 1 
ATOM   2155 N  N   . MET   A 1 289 ? 1.273   15.260  -15.893 1.00 63.40  ? 426 MET   A N   1 
ATOM   2156 C  CA  . MET   A 1 289 ? 0.706   13.922  -16.027 1.00 51.99  ? 426 MET   A CA  1 
ATOM   2157 C  C   . MET   A 1 289 ? -0.314  13.641  -14.945 1.00 43.49  ? 426 MET   A C   1 
ATOM   2158 O  O   . MET   A 1 289 ? -0.150  14.045  -13.797 1.00 48.58  ? 426 MET   A O   1 
ATOM   2159 C  CB  . MET   A 1 289 ? 1.810   12.888  -15.952 1.00 48.85  ? 426 MET   A CB  1 
ATOM   2160 C  CG  . MET   A 1 289 ? 2.835   13.134  -16.993 1.00 52.13  ? 426 MET   A CG  1 
ATOM   2161 S  SD  . MET   A 1 289 ? 3.513   11.590  -17.527 1.00 82.33  ? 426 MET   A SD  1 
ATOM   2162 C  CE  . MET   A 1 289 ? 5.179   11.819  -16.920 1.00 73.82  ? 426 MET   A CE  1 
ATOM   2163 N  N   . TRP   A 1 290 ? -1.389  12.956  -15.320 1.00 46.43  ? 427 TRP   A N   1 
ATOM   2164 C  CA  . TRP   A 1 290 ? -2.353  12.513  -14.328 1.00 44.85  ? 427 TRP   A CA  1 
ATOM   2165 C  C   . TRP   A 1 290 ? -2.005  11.145  -13.767 1.00 51.78  ? 427 TRP   A C   1 
ATOM   2166 O  O   . TRP   A 1 290 ? -2.480  10.800  -12.683 1.00 52.18  ? 427 TRP   A O   1 
ATOM   2167 C  CB  . TRP   A 1 290 ? -3.763  12.482  -14.928 1.00 41.59  ? 427 TRP   A CB  1 
ATOM   2168 C  CG  . TRP   A 1 290 ? -3.909  11.496  -16.027 1.00 46.13  ? 427 TRP   A CG  1 
ATOM   2169 C  CD1 . TRP   A 1 290 ? -3.711  11.723  -17.354 1.00 46.97  ? 427 TRP   A CD1 1 
ATOM   2170 C  CD2 . TRP   A 1 290 ? -4.279  10.117  -15.902 1.00 42.91  ? 427 TRP   A CD2 1 
ATOM   2171 N  NE1 . TRP   A 1 290 ? -3.938  10.575  -18.066 1.00 44.67  ? 427 TRP   A NE1 1 
ATOM   2172 C  CE2 . TRP   A 1 290 ? -4.288  9.574   -17.197 1.00 43.71  ? 427 TRP   A CE2 1 
ATOM   2173 C  CE3 . TRP   A 1 290 ? -4.594  9.282   -14.814 1.00 53.28  ? 427 TRP   A CE3 1 
ATOM   2174 C  CZ2 . TRP   A 1 290 ? -4.616  8.238   -17.442 1.00 47.72  ? 427 TRP   A CZ2 1 
ATOM   2175 C  CZ3 . TRP   A 1 290 ? -4.911  7.957   -15.061 1.00 43.17  ? 427 TRP   A CZ3 1 
ATOM   2176 C  CH2 . TRP   A 1 290 ? -4.916  7.450   -16.363 1.00 39.02  ? 427 TRP   A CH2 1 
ATOM   2177 N  N   . GLN   A 1 291 ? -1.183  10.366  -14.469 1.00 50.32  ? 428 GLN   A N   1 
ATOM   2178 C  CA  . GLN   A 1 291 ? -0.844  9.010   -14.048 1.00 61.68  ? 428 GLN   A CA  1 
ATOM   2179 C  C   . GLN   A 1 291 ? 0.099   9.066   -12.855 1.00 72.91  ? 428 GLN   A C   1 
ATOM   2180 O  O   . GLN   A 1 291 ? -0.313  8.878   -11.702 1.00 76.60  ? 428 GLN   A O   1 
ATOM   2181 C  CB  . GLN   A 1 291 ? -0.196  8.250   -15.203 1.00 49.31  ? 428 GLN   A CB  1 
ATOM   2182 C  CG  . GLN   A 1 291 ? -0.944  8.335   -16.523 1.00 48.25  ? 428 GLN   A CG  1 
ATOM   2183 C  CD  . GLN   A 1 291 ? -0.532  9.528   -17.389 1.00 57.01  ? 428 GLN   A CD  1 
ATOM   2184 O  OE1 . GLN   A 1 291 ? -0.690  10.687  -16.990 1.00 57.24  ? 428 GLN   A OE1 1 
ATOM   2185 N  NE2 . GLN   A 1 291 ? -0.035  9.250   -18.585 1.00 53.56  ? 428 GLN   A NE2 1 
ATOM   2186 N  N   . GLY   A 1 292 ? 1.372   9.329   -13.134 1.00 67.41  ? 429 GLY   A N   1 
ATOM   2187 C  CA  . GLY   A 1 292 ? 2.315   9.643   -12.083 1.00 73.71  ? 429 GLY   A CA  1 
ATOM   2188 C  C   . GLY   A 1 292 ? 2.802   11.081  -12.108 1.00 76.29  ? 429 GLY   A C   1 
ATOM   2189 O  O   . GLY   A 1 292 ? 2.740   11.772  -13.135 1.00 75.05  ? 429 GLY   A O   1 
ATOM   2190 N  N   . THR   A 1 293 ? 3.294   11.542  -10.961 1.00 80.00  ? 430 THR   A N   1 
ATOM   2191 C  CA  . THR   A 1 293 ? 3.804   12.897  -10.860 1.00 68.62  ? 430 THR   A CA  1 
ATOM   2192 C  C   . THR   A 1 293 ? 4.888   13.116  -11.901 1.00 71.38  ? 430 THR   A C   1 
ATOM   2193 O  O   . THR   A 1 293 ? 5.858   12.359  -11.972 1.00 76.85  ? 430 THR   A O   1 
ATOM   2194 C  CB  . THR   A 1 293 ? 4.348   13.142  -9.455  1.00 74.44  ? 430 THR   A CB  1 
ATOM   2195 O  OG1 . THR   A 1 293 ? 3.396   13.915  -8.723  1.00 64.02  ? 430 THR   A OG1 1 
ATOM   2196 C  CG2 . THR   A 1 293 ? 5.657   13.917  -9.515  1.00 77.27  ? 430 THR   A CG2 1 
ATOM   2197 N  N   . GLY   A 1 294 ? 4.698   14.122  -12.740 1.00 60.49  ? 431 GLY   A N   1 
ATOM   2198 C  CA  . GLY   A 1 294 ? 5.724   14.469  -13.702 1.00 68.84  ? 431 GLY   A CA  1 
ATOM   2199 C  C   . GLY   A 1 294 ? 5.166   15.290  -14.839 1.00 62.19  ? 431 GLY   A C   1 
ATOM   2200 O  O   . GLY   A 1 294 ? 3.974   15.585  -14.903 1.00 59.64  ? 431 GLY   A O   1 
ATOM   2201 N  N   . GLN   A 1 295 ? 6.066   15.657  -15.755 1.00 57.13  ? 432 GLN   A N   1 
ATOM   2202 C  CA  . GLN   A 1 295 ? 5.764   16.520  -16.889 1.00 57.03  ? 432 GLN   A CA  1 
ATOM   2203 C  C   . GLN   A 1 295 ? 6.038   15.768  -18.180 1.00 61.55  ? 432 GLN   A C   1 
ATOM   2204 O  O   . GLN   A 1 295 ? 7.061   15.090  -18.302 1.00 67.73  ? 432 GLN   A O   1 
ATOM   2205 C  CB  . GLN   A 1 295 ? 6.612   17.788  -16.864 1.00 61.34  ? 432 GLN   A CB  1 
ATOM   2206 C  CG  . GLN   A 1 295 ? 5.808   19.089  -16.857 1.00 73.32  ? 432 GLN   A CG  1 
ATOM   2207 C  CD  . GLN   A 1 295 ? 6.685   20.337  -16.918 1.00 76.32  ? 432 GLN   A CD  1 
ATOM   2208 O  OE1 . GLN   A 1 295 ? 7.918   20.259  -16.868 1.00 69.19  ? 432 GLN   A OE1 1 
ATOM   2209 N  NE2 . GLN   A 1 295 ? 6.044   21.502  -17.029 1.00 81.85  ? 432 GLN   A NE2 1 
ATOM   2210 N  N   . ALA   A 1 296 ? 5.140   15.900  -19.153 1.00 49.32  ? 433 ALA   A N   1 
ATOM   2211 C  CA  . ALA   A 1 296 ? 5.323   15.245  -20.438 1.00 63.97  ? 433 ALA   A CA  1 
ATOM   2212 C  C   . ALA   A 1 296 ? 5.168   16.276  -21.542 1.00 64.88  ? 433 ALA   A C   1 
ATOM   2213 O  O   . ALA   A 1 296 ? 4.246   17.100  -21.508 1.00 54.45  ? 433 ALA   A O   1 
ATOM   2214 C  CB  . ALA   A 1 296 ? 4.334   14.090  -20.639 1.00 53.39  ? 433 ALA   A CB  1 
ATOM   2215 N  N   . MET   A 1 297 ? 6.070   16.231  -22.514 1.00 55.76  ? 434 MET   A N   1 
ATOM   2216 C  CA  . MET   A 1 297 ? 5.999   17.116  -23.662 1.00 59.76  ? 434 MET   A CA  1 
ATOM   2217 C  C   . MET   A 1 297 ? 5.704   16.292  -24.901 1.00 64.73  ? 434 MET   A C   1 
ATOM   2218 O  O   . MET   A 1 297 ? 6.470   15.380  -25.234 1.00 59.02  ? 434 MET   A O   1 
ATOM   2219 C  CB  . MET   A 1 297 ? 7.290   17.900  -23.864 1.00 54.69  ? 434 MET   A CB  1 
ATOM   2220 C  CG  . MET   A 1 297 ? 7.317   18.490  -25.250 1.00 67.42  ? 434 MET   A CG  1 
ATOM   2221 S  SD  . MET   A 1 297 ? 8.425   19.887  -25.443 1.00 77.96  ? 434 MET   A SD  1 
ATOM   2222 C  CE  . MET   A 1 297 ? 9.769   19.145  -26.381 1.00 58.79  ? 434 MET   A CE  1 
ATOM   2223 N  N   . TYR   A 1 298 ? 4.599   16.625  -25.572 1.00 68.31  ? 435 TYR   A N   1 
ATOM   2224 C  CA  . TYR   A 1 298 ? 4.137   15.986  -26.794 1.00 67.81  ? 435 TYR   A CA  1 
ATOM   2225 C  C   . TYR   A 1 298 ? 4.347   16.931  -27.970 1.00 67.73  ? 435 TYR   A C   1 
ATOM   2226 O  O   . TYR   A 1 298 ? 4.651   18.118  -27.808 1.00 67.66  ? 435 TYR   A O   1 
ATOM   2227 C  CB  . TYR   A 1 298 ? 2.655   15.577  -26.686 1.00 59.69  ? 435 TYR   A CB  1 
ATOM   2228 C  CG  . TYR   A 1 298 ? 2.330   14.678  -25.495 1.00 62.78  ? 435 TYR   A CG  1 
ATOM   2229 C  CD1 . TYR   A 1 298 ? 2.469   15.128  -24.190 1.00 55.44  ? 435 TYR   A CD1 1 
ATOM   2230 C  CD2 . TYR   A 1 298 ? 1.935   13.349  -25.682 1.00 68.31  ? 435 TYR   A CD2 1 
ATOM   2231 C  CE1 . TYR   A 1 298 ? 2.183   14.294  -23.090 1.00 66.74  ? 435 TYR   A CE1 1 
ATOM   2232 C  CE2 . TYR   A 1 298 ? 1.651   12.501  -24.588 1.00 58.59  ? 435 TYR   A CE2 1 
ATOM   2233 C  CZ  . TYR   A 1 298 ? 1.786   12.980  -23.298 1.00 62.36  ? 435 TYR   A CZ  1 
ATOM   2234 O  OH  . TYR   A 1 298 ? 1.518   12.166  -22.205 1.00 67.83  ? 435 TYR   A OH  1 
ATOM   2235 N  N   . ALA   A 1 299 ? 4.170   16.386  -29.162 1.00 66.07  ? 436 ALA   A N   1 
ATOM   2236 C  CA  . ALA   A 1 299 ? 4.421   17.109  -30.392 1.00 65.81  ? 436 ALA   A CA  1 
ATOM   2237 C  C   . ALA   A 1 299 ? 3.284   18.080  -30.684 1.00 53.71  ? 436 ALA   A C   1 
ATOM   2238 O  O   . ALA   A 1 299 ? 2.179   17.938  -30.172 1.00 68.21  ? 436 ALA   A O   1 
ATOM   2239 C  CB  . ALA   A 1 299 ? 4.588   16.127  -31.549 1.00 60.16  ? 436 ALA   A CB  1 
ATOM   2240 N  N   . PRO   A 1 300 ? 3.536   19.085  -31.504 1.00 55.23  ? 437 PRO   A N   1 
ATOM   2241 C  CA  . PRO   A 1 300 ? 2.488   20.050  -31.837 1.00 59.35  ? 437 PRO   A CA  1 
ATOM   2242 C  C   . PRO   A 1 300 ? 1.329   19.377  -32.543 1.00 55.17  ? 437 PRO   A C   1 
ATOM   2243 O  O   . PRO   A 1 300 ? 1.420   18.196  -32.928 1.00 56.45  ? 437 PRO   A O   1 
ATOM   2244 C  CB  . PRO   A 1 300 ? 3.226   21.054  -32.742 1.00 55.31  ? 437 PRO   A CB  1 
ATOM   2245 C  CG  . PRO   A 1 300 ? 4.658   20.948  -32.289 1.00 58.31  ? 437 PRO   A CG  1 
ATOM   2246 C  CD  . PRO   A 1 300 ? 4.847   19.483  -32.030 1.00 66.83  ? 437 PRO   A CD  1 
ATOM   2247 N  N   . PRO   A 1 301 ? 0.194   20.056  -32.671 1.00 52.91  ? 438 PRO   A N   1 
ATOM   2248 C  CA  . PRO   A 1 301 ? -1.019  19.366  -33.102 1.00 53.38  ? 438 PRO   A CA  1 
ATOM   2249 C  C   . PRO   A 1 301 ? -1.007  19.004  -34.580 1.00 69.18  ? 438 PRO   A C   1 
ATOM   2250 O  O   . PRO   A 1 301 ? -0.343  19.631  -35.416 1.00 60.12  ? 438 PRO   A O   1 
ATOM   2251 C  CB  . PRO   A 1 301 ? -2.135  20.356  -32.762 1.00 59.44  ? 438 PRO   A CB  1 
ATOM   2252 C  CG  . PRO   A 1 301 ? -1.467  21.644  -32.386 1.00 49.33  ? 438 PRO   A CG  1 
ATOM   2253 C  CD  . PRO   A 1 301 ? -0.098  21.303  -31.938 1.00 60.99  ? 438 PRO   A CD  1 
ATOM   2254 N  N   . ILE   A 1 302 ? -1.748  17.934  -34.885 1.00 64.88  ? 439 ILE   A N   1 
ATOM   2255 C  CA  . ILE   A 1 302 ? -1.921  17.539  -36.273 1.00 64.77  ? 439 ILE   A CA  1 
ATOM   2256 C  C   . ILE   A 1 302 ? -2.531  18.688  -37.075 1.00 56.30  ? 439 ILE   A C   1 
ATOM   2257 O  O   . ILE   A 1 302 ? -3.079  19.651  -36.528 1.00 53.98  ? 439 ILE   A O   1 
ATOM   2258 C  CB  . ILE   A 1 302 ? -2.770  16.257  -36.355 1.00 63.12  ? 439 ILE   A CB  1 
ATOM   2259 C  CG1 . ILE   A 1 302 ? -4.211  16.497  -35.905 1.00 63.18  ? 439 ILE   A CG1 1 
ATOM   2260 C  CG2 . ILE   A 1 302 ? -2.209  15.207  -35.440 1.00 54.09  ? 439 ILE   A CG2 1 
ATOM   2261 C  CD1 . ILE   A 1 302 ? -5.225  15.559  -36.543 1.00 60.17  ? 439 ILE   A CD1 1 
ATOM   2262 N  N   . ASP   A 1 303 ? -2.383  18.609  -38.395 1.00 66.01  ? 440 ASP   A N   1 
ATOM   2263 C  CA  . ASP   A 1 303 ? -2.969  19.605  -39.285 1.00 68.19  ? 440 ASP   A CA  1 
ATOM   2264 C  C   . ASP   A 1 303 ? -4.473  19.363  -39.443 1.00 68.64  ? 440 ASP   A C   1 
ATOM   2265 O  O   . ASP   A 1 303 ? -4.998  18.291  -39.128 1.00 65.57  ? 440 ASP   A O   1 
ATOM   2266 C  CB  . ASP   A 1 303 ? -2.289  19.582  -40.659 1.00 75.80  ? 440 ASP   A CB  1 
ATOM   2267 C  CG  . ASP   A 1 303 ? -0.816  20.010  -40.609 1.00 84.30  ? 440 ASP   A CG  1 
ATOM   2268 O  OD1 . ASP   A 1 303 ? -0.516  21.068  -40.012 1.00 83.90  ? 440 ASP   A OD1 1 
ATOM   2269 O  OD2 . ASP   A 1 303 ? 0.041   19.303  -41.190 1.00 81.59  ? 440 ASP   A OD2 1 
ATOM   2270 N  N   . GLY   A 1 304 ? -5.170  20.390  -39.935 1.00 65.97  ? 441 GLY   A N   1 
ATOM   2271 C  CA  . GLY   A 1 304 ? -6.586  20.281  -40.226 1.00 71.32  ? 441 GLY   A CA  1 
ATOM   2272 C  C   . GLY   A 1 304 ? -7.485  20.531  -39.031 1.00 70.67  ? 441 GLY   A C   1 
ATOM   2273 O  O   . GLY   A 1 304 ? -7.045  20.778  -37.908 1.00 60.97  ? 441 GLY   A O   1 
ATOM   2274 N  N   . LYS   A 1 305 ? -8.789  20.469  -39.310 1.00 65.46  ? 442 LYS   A N   1 
ATOM   2275 C  CA  . LYS   A 1 305 ? -9.823  20.626  -38.294 1.00 62.25  ? 442 LYS   A CA  1 
ATOM   2276 C  C   . LYS   A 1 305 ? -9.767  19.463  -37.314 1.00 61.64  ? 442 LYS   A C   1 
ATOM   2277 O  O   . LYS   A 1 305 ? -9.982  18.308  -37.697 1.00 71.25  ? 442 LYS   A O   1 
ATOM   2278 C  CB  . LYS   A 1 305 ? -11.199 20.694  -38.951 1.00 61.53  ? 442 LYS   A CB  1 
ATOM   2279 C  CG  . LYS   A 1 305 ? -12.343 20.792  -37.982 1.00 62.89  ? 442 LYS   A CG  1 
ATOM   2280 C  CD  . LYS   A 1 305 ? -13.585 21.331  -38.659 1.00 59.82  ? 442 LYS   A CD  1 
ATOM   2281 C  CE  . LYS   A 1 305 ? -14.689 20.287  -38.705 1.00 67.41  ? 442 LYS   A CE  1 
ATOM   2282 N  NZ  . LYS   A 1 305 ? -16.058 20.883  -38.775 1.00 72.52  ? 442 LYS   A NZ  1 
ATOM   2283 N  N   . ILE   A 1 306 ? -9.444  19.763  -36.061 1.00 58.77  ? 443 ILE   A N   1 
ATOM   2284 C  CA  . ILE   A 1 306 ? -9.512  18.813  -34.956 1.00 51.69  ? 443 ILE   A CA  1 
ATOM   2285 C  C   . ILE   A 1 306 ? -10.814 19.087  -34.213 1.00 55.05  ? 443 ILE   A C   1 
ATOM   2286 O  O   . ILE   A 1 306 ? -11.016 20.194  -33.699 1.00 48.69  ? 443 ILE   A O   1 
ATOM   2287 C  CB  . ILE   A 1 306 ? -8.298  18.969  -34.025 1.00 57.19  ? 443 ILE   A CB  1 
ATOM   2288 C  CG1 . ILE   A 1 306 ? -6.998  18.873  -34.831 1.00 52.99  ? 443 ILE   A CG1 1 
ATOM   2289 C  CG2 . ILE   A 1 306 ? -8.345  17.970  -32.901 1.00 47.90  ? 443 ILE   A CG2 1 
ATOM   2290 C  CD1 . ILE   A 1 306 ? -5.749  19.121  -34.022 1.00 51.08  ? 443 ILE   A CD1 1 
ATOM   2291 N  N   . ASN   A 1 307 ? -11.700 18.091  -34.154 1.00 50.87  ? 444 ASN   A N   1 
ATOM   2292 C  CA  . ASN   A 1 307 ? -13.036 18.281  -33.600 1.00 47.37  ? 444 ASN   A CA  1 
ATOM   2293 C  C   . ASN   A 1 307 ? -13.429 17.071  -32.760 1.00 49.56  ? 444 ASN   A C   1 
ATOM   2294 O  O   . ASN   A 1 307 ? -13.159 15.934  -33.154 1.00 53.24  ? 444 ASN   A O   1 
ATOM   2295 C  CB  . ASN   A 1 307 ? -14.051 18.500  -34.725 1.00 47.34  ? 444 ASN   A CB  1 
ATOM   2296 C  CG  . ASN   A 1 307 ? -15.470 18.547  -34.231 1.00 52.23  ? 444 ASN   A CG  1 
ATOM   2297 O  OD1 . ASN   A 1 307 ? -16.200 17.542  -34.245 1.00 52.61  ? 444 ASN   A OD1 1 
ATOM   2298 N  ND2 . ASN   A 1 307 ? -15.887 19.724  -33.805 1.00 46.12  ? 444 ASN   A ND2 1 
ATOM   2299 N  N   . CYS   A 1 308 ? -14.048 17.331  -31.599 1.00 39.80  ? 445 CYS   A N   1 
ATOM   2300 C  CA  . CYS   A 1 308 ? -14.598 16.334  -30.679 1.00 50.77  ? 445 CYS   A CA  1 
ATOM   2301 C  C   . CYS   A 1 308 ? -15.936 16.827  -30.161 1.00 40.49  ? 445 CYS   A C   1 
ATOM   2302 O  O   . CYS   A 1 308 ? -16.005 17.898  -29.554 1.00 42.27  ? 445 CYS   A O   1 
ATOM   2303 C  CB  . CYS   A 1 308 ? -13.700 16.079  -29.464 1.00 46.37  ? 445 CYS   A CB  1 
ATOM   2304 S  SG  . CYS   A 1 308 ? -12.201 15.132  -29.748 1.00 80.82  ? 445 CYS   A SG  1 
ATOM   2305 N  N   . VAL   A 1 309 ? -16.979 16.038  -30.365 1.00 38.01  ? 446 VAL   A N   1 
ATOM   2306 C  CA  . VAL   A 1 309 ? -18.308 16.318  -29.841 1.00 45.83  ? 446 VAL   A CA  1 
ATOM   2307 C  C   . VAL   A 1 309 ? -18.569 15.289  -28.754 1.00 42.32  ? 446 VAL   A C   1 
ATOM   2308 O  O   . VAL   A 1 309 ? -18.624 14.091  -29.038 1.00 40.66  ? 446 VAL   A O   1 
ATOM   2309 C  CB  . VAL   A 1 309 ? -19.389 16.240  -30.929 1.00 53.10  ? 446 VAL   A CB  1 
ATOM   2310 C  CG1 . VAL   A 1 309 ? -20.740 16.623  -30.353 1.00 41.62  ? 446 VAL   A CG1 1 
ATOM   2311 C  CG2 . VAL   A 1 309 ? -19.015 17.107  -32.125 1.00 55.89  ? 446 VAL   A CG2 1 
ATOM   2312 N  N   . SER   A 1 310 ? -18.712 15.747  -27.510 1.00 40.30  ? 447 SER   A N   1 
ATOM   2313 C  CA  . SER   A 1 310 ? -18.858 14.869  -26.360 1.00 41.97  ? 447 SER   A CA  1 
ATOM   2314 C  C   . SER   A 1 310 ? -20.125 15.214  -25.584 1.00 41.68  ? 447 SER   A C   1 
ATOM   2315 O  O   . SER   A 1 310 ? -20.711 16.287  -25.749 1.00 40.24  ? 447 SER   A O   1 
ATOM   2316 C  CB  . SER   A 1 310 ? -17.631 14.958  -25.424 1.00 41.68  ? 447 SER   A CB  1 
ATOM   2317 O  OG  . SER   A 1 310 ? -16.415 15.090  -26.142 1.00 43.48  ? 447 SER   A OG  1 
ATOM   2318 N  N   . ASN   A 1 311 ? -20.530 14.301  -24.714 1.00 39.58  ? 448 ASN   A N   1 
ATOM   2319 C  CA  . ASN   A 1 311 ? -21.659 14.517  -23.817 1.00 40.70  ? 448 ASN   A CA  1 
ATOM   2320 C  C   . ASN   A 1 311 ? -21.122 14.851  -22.428 1.00 37.45  ? 448 ASN   A C   1 
ATOM   2321 O  O   . ASN   A 1 311 ? -20.413 14.039  -21.834 1.00 41.19  ? 448 ASN   A O   1 
ATOM   2322 C  CB  . ASN   A 1 311 ? -22.526 13.264  -23.718 1.00 33.46  ? 448 ASN   A CB  1 
ATOM   2323 C  CG  . ASN   A 1 311 ? -23.508 13.100  -24.857 1.00 52.40  ? 448 ASN   A CG  1 
ATOM   2324 O  OD1 . ASN   A 1 311 ? -23.909 14.046  -25.530 1.00 42.74  ? 448 ASN   A OD1 1 
ATOM   2325 N  ND2 . ASN   A 1 311 ? -23.910 11.851  -25.064 1.00 64.24  ? 448 ASN   A ND2 1 
ATOM   2326 N  N   . ILE   A 1 312 ? -21.466 16.022  -21.902 1.00 38.46  ? 449 ILE   A N   1 
ATOM   2327 C  CA  . ILE   A 1 312 ? -21.239 16.297  -20.488 1.00 44.24  ? 449 ILE   A CA  1 
ATOM   2328 C  C   . ILE   A 1 312 ? -22.262 15.469  -19.732 1.00 43.98  ? 449 ILE   A C   1 
ATOM   2329 O  O   . ILE   A 1 312 ? -23.461 15.732  -19.837 1.00 40.40  ? 449 ILE   A O   1 
ATOM   2330 C  CB  . ILE   A 1 312 ? -21.395 17.783  -20.152 1.00 37.41  ? 449 ILE   A CB  1 
ATOM   2331 C  CG1 . ILE   A 1 312 ? -20.297 18.612  -20.812 1.00 33.58  ? 449 ILE   A CG1 1 
ATOM   2332 C  CG2 . ILE   A 1 312 ? -21.316 17.973  -18.658 1.00 34.00  ? 449 ILE   A CG2 1 
ATOM   2333 C  CD1 . ILE   A 1 312 ? -20.568 20.099  -20.818 1.00 32.27  ? 449 ILE   A CD1 1 
ATOM   2334 N  N   . THR   A 1 313 ? -21.801 14.468  -18.980 1.00 34.08  ? 450 THR   A N   1 
ATOM   2335 C  CA  . THR   A 1 313 ? -22.687 13.611  -18.204 1.00 38.54  ? 450 THR   A CA  1 
ATOM   2336 C  C   . THR   A 1 313 ? -22.541 13.809  -16.703 1.00 34.42  ? 450 THR   A C   1 
ATOM   2337 O  O   . THR   A 1 313 ? -23.298 13.213  -15.926 1.00 36.97  ? 450 THR   A O   1 
ATOM   2338 C  CB  . THR   A 1 313 ? -22.430 12.138  -18.554 1.00 44.57  ? 450 THR   A CB  1 
ATOM   2339 O  OG1 . THR   A 1 313 ? -21.005 11.883  -18.562 1.00 41.73  ? 450 THR   A OG1 1 
ATOM   2340 C  CG2 . THR   A 1 313 ? -22.987 11.847  -19.944 1.00 46.96  ? 450 THR   A CG2 1 
ATOM   2341 N  N   . GLY   A 1 314 ? -21.586 14.603  -16.264 1.00 37.78  ? 451 GLY   A N   1 
ATOM   2342 C  CA  . GLY   A 1 314 ? -21.414 14.837  -14.843 1.00 34.32  ? 451 GLY   A CA  1 
ATOM   2343 C  C   . GLY   A 1 314 ? -20.469 15.983  -14.613 1.00 35.78  ? 451 GLY   A C   1 
ATOM   2344 O  O   . GLY   A 1 314 ? -19.781 16.448  -15.541 1.00 31.21  ? 451 GLY   A O   1 
ATOM   2345 N  N   . ILE   A 1 315 ? -20.440 16.448  -13.357 1.00 33.48  ? 452 ILE   A N   1 
ATOM   2346 C  CA  . ILE   A 1 315 ? -19.626 17.570  -12.903 1.00 35.66  ? 452 ILE   A CA  1 
ATOM   2347 C  C   . ILE   A 1 315 ? -18.884 17.164  -11.640 1.00 36.81  ? 452 ILE   A C   1 
ATOM   2348 O  O   . ILE   A 1 315 ? -19.470 16.543  -10.747 1.00 35.68  ? 452 ILE   A O   1 
ATOM   2349 C  CB  . ILE   A 1 315 ? -20.479 18.826  -12.624 1.00 35.64  ? 452 ILE   A CB  1 
ATOM   2350 C  CG1 . ILE   A 1 315 ? -21.438 19.106  -13.777 1.00 43.24  ? 452 ILE   A CG1 1 
ATOM   2351 C  CG2 . ILE   A 1 315 ? -19.603 20.035  -12.349 1.00 40.08  ? 452 ILE   A CG2 1 
ATOM   2352 C  CD1 . ILE   A 1 315 ? -22.372 20.255  -13.495 1.00 38.67  ? 452 ILE   A CD1 1 
ATOM   2353 N  N   . LEU   A 1 316 ? -17.603 17.523  -11.566 1.00 39.15  ? 453 LEU   A N   1 
ATOM   2354 C  CA  . LEU   A 1 316 ? -16.753 17.341  -10.394 1.00 36.85  ? 453 LEU   A CA  1 
ATOM   2355 C  C   . LEU   A 1 316 ? -16.681 18.676  -9.639  1.00 42.41  ? 453 LEU   A C   1 
ATOM   2356 O  O   . LEU   A 1 316 ? -16.230 19.692  -10.193 1.00 40.46  ? 453 LEU   A O   1 
ATOM   2357 C  CB  . LEU   A 1 316 ? -15.358 16.876  -10.826 1.00 37.58  ? 453 LEU   A CB  1 
ATOM   2358 C  CG  . LEU   A 1 316 ? -15.260 15.415  -11.311 1.00 40.18  ? 453 LEU   A CG  1 
ATOM   2359 C  CD1 . LEU   A 1 316 ? -13.977 15.156  -12.074 1.00 48.71  ? 453 LEU   A CD1 1 
ATOM   2360 C  CD2 . LEU   A 1 316 ? -15.404 14.415  -10.188 1.00 35.96  ? 453 LEU   A CD2 1 
ATOM   2361 N  N   . LEU   A 1 317 ? -17.120 18.681  -8.384  1.00 40.07  ? 454 LEU   A N   1 
ATOM   2362 C  CA  . LEU   A 1 317 ? -17.244 19.912  -7.611  1.00 37.32  ? 454 LEU   A CA  1 
ATOM   2363 C  C   . LEU   A 1 317 ? -16.526 19.786  -6.273  1.00 47.51  ? 454 LEU   A C   1 
ATOM   2364 O  O   . LEU   A 1 317 ? -16.545 18.725  -5.632  1.00 48.29  ? 454 LEU   A O   1 
ATOM   2365 C  CB  . LEU   A 1 317 ? -18.696 20.260  -7.356  1.00 39.48  ? 454 LEU   A CB  1 
ATOM   2366 C  CG  . LEU   A 1 317 ? -19.526 20.657  -8.563  1.00 38.09  ? 454 LEU   A CG  1 
ATOM   2367 C  CD1 . LEU   A 1 317 ? -20.922 20.921  -8.083  1.00 39.18  ? 454 LEU   A CD1 1 
ATOM   2368 C  CD2 . LEU   A 1 317 ? -18.928 21.871  -9.268  1.00 41.50  ? 454 LEU   A CD2 1 
ATOM   2369 N  N   . THR   A 1 318 ? -15.899 20.885  -5.857  1.00 49.51  ? 455 THR   A N   1 
ATOM   2370 C  CA  . THR   A 1 318 ? -15.253 21.005  -4.557  1.00 50.56  ? 455 THR   A CA  1 
ATOM   2371 C  C   . THR   A 1 318 ? -15.877 22.182  -3.824  1.00 56.52  ? 455 THR   A C   1 
ATOM   2372 O  O   . THR   A 1 318 ? -15.971 23.283  -4.385  1.00 52.22  ? 455 THR   A O   1 
ATOM   2373 C  CB  . THR   A 1 318 ? -13.749 21.237  -4.690  1.00 56.33  ? 455 THR   A CB  1 
ATOM   2374 O  OG1 . THR   A 1 318 ? -13.090 19.985  -4.908  1.00 62.35  ? 455 THR   A OG1 1 
ATOM   2375 C  CG2 . THR   A 1 318 ? -13.216 21.860  -3.415  1.00 59.09  ? 455 THR   A CG2 1 
ATOM   2376 N  N   . ARG   A 1 319 ? -16.287 21.953  -2.578  1.00 48.71  ? 456 ARG   A N   1 
ATOM   2377 C  CA  . ARG   A 1 319 ? -16.988 22.966  -1.802  1.00 61.63  ? 456 ARG   A CA  1 
ATOM   2378 C  C   . ARG   A 1 319 ? -16.004 23.806  -1.004  1.00 57.32  ? 456 ARG   A C   1 
ATOM   2379 O  O   . ARG   A 1 319 ? -15.033 23.286  -0.441  1.00 59.92  ? 456 ARG   A O   1 
ATOM   2380 C  CB  . ARG   A 1 319 ? -18.009 22.347  -0.844  1.00 61.36  ? 456 ARG   A CB  1 
ATOM   2381 C  CG  . ARG   A 1 319 ? -18.838 23.386  -0.078  1.00 61.04  ? 456 ARG   A CG  1 
ATOM   2382 C  CD  . ARG   A 1 319 ? -20.109 22.803  0.553   1.00 53.12  ? 456 ARG   A CD  1 
ATOM   2383 N  NE  . ARG   A 1 319 ? -19.805 21.771  1.535   1.00 62.12  ? 456 ARG   A NE  1 
ATOM   2384 C  CZ  . ARG   A 1 319 ? -19.599 21.998  2.827   1.00 68.34  ? 456 ARG   A CZ  1 
ATOM   2385 N  NH1 . ARG   A 1 319 ? -19.725 23.216  3.352   1.00 56.73  ? 456 ARG   A NH1 1 
ATOM   2386 N  NH2 . ARG   A 1 319 ? -19.250 20.980  3.613   1.00 51.38  ? 456 ARG   A NH2 1 
ATOM   2387 N  N   . ASP   A 1 320 ? -16.270 25.116  -0.967  1.00 55.34  ? 457 ASP   A N   1 
ATOM   2388 C  CA  . ASP   A 1 320 ? -15.470 26.050  -0.183  1.00 60.51  ? 457 ASP   A CA  1 
ATOM   2389 C  C   . ASP   A 1 320 ? -15.629 25.750  1.302   1.00 59.04  ? 457 ASP   A C   1 
ATOM   2390 O  O   . ASP   A 1 320 ? -16.754 25.719  1.817   1.00 57.53  ? 457 ASP   A O   1 
ATOM   2391 C  CB  . ASP   A 1 320 ? -15.886 27.491  -0.474  1.00 70.13  ? 457 ASP   A CB  1 
ATOM   2392 C  CG  . ASP   A 1 320 ? -15.223 28.065  -1.727  1.00 75.06  ? 457 ASP   A CG  1 
ATOM   2393 O  OD1 . ASP   A 1 320 ? -14.186 27.524  -2.179  1.00 70.39  ? 457 ASP   A OD1 1 
ATOM   2394 O  OD2 . ASP   A 1 320 ? -15.712 29.108  -2.223  1.00 68.52  ? 457 ASP   A OD2 1 
ATOM   2395 N  N   . GLY   A 1 321 ? -14.488 25.534  1.990   1.00 58.58  ? 458 GLY   A N   1 
ATOM   2396 C  CA  . GLY   A 1 321 ? -14.480 25.305  3.420   1.00 76.95  ? 458 GLY   A CA  1 
ATOM   2397 C  C   . GLY   A 1 321 ? -14.491 26.595  4.252   1.00 84.77  ? 458 GLY   A C   1 
ATOM   2398 O  O   . GLY   A 1 321 ? -14.254 27.699  3.753   1.00 83.11  ? 458 GLY   A O   1 
ATOM   2399 N  N   . GLY   A 1 322 ? -14.785 26.420  5.540   1.00 76.61  ? 459 GLY   A N   1 
ATOM   2400 C  CA  . GLY   A 1 322 ? -14.764 27.491  6.515   1.00 85.84  ? 459 GLY   A CA  1 
ATOM   2401 C  C   . GLY   A 1 322 ? -15.814 28.568  6.315   1.00 85.53  ? 459 GLY   A C   1 
ATOM   2402 O  O   . GLY   A 1 322 ? -15.475 29.737  6.115   1.00 90.86  ? 459 GLY   A O   1 
ATOM   2403 N  N   . ALA   A 1 323 ? -17.093 28.199  6.378   1.00 88.72  ? 460 ALA   A N   1 
ATOM   2404 C  CA  . ALA   A 1 323 ? -18.168 29.158  6.145   1.00 84.33  ? 460 ALA   A CA  1 
ATOM   2405 C  C   . ALA   A 1 323 ? -19.509 28.599  6.609   1.00 85.23  ? 460 ALA   A C   1 
ATOM   2406 O  O   . ALA   A 1 323 ? -20.528 28.742  5.919   1.00 86.94  ? 460 ALA   A O   1 
ATOM   2407 C  CB  . ALA   A 1 323 ? -18.228 29.536  4.662   1.00 87.45  ? 460 ALA   A CB  1 
ATOM   2408 N  N   . ASN   A 1 324 ? -19.514 27.951  7.777   1.00 94.51  ? 461 ASN   A N   1 
ATOM   2409 C  CA  . ASN   A 1 324 ? -20.757 27.419  8.323   1.00 93.71  ? 461 ASN   A CA  1 
ATOM   2410 C  C   . ASN   A 1 324 ? -21.722 28.522  8.748   1.00 99.33  ? 461 ASN   A C   1 
ATOM   2411 O  O   . ASN   A 1 324 ? -22.944 28.335  8.632   1.00 108.14 ? 461 ASN   A O   1 
ATOM   2412 C  CB  . ASN   A 1 324 ? -20.471 26.469  9.495   1.00 87.47  ? 461 ASN   A CB  1 
ATOM   2413 C  CG  . ASN   A 1 324 ? -19.188 25.674  9.316   1.00 91.21  ? 461 ASN   A CG  1 
ATOM   2414 O  OD1 . ASN   A 1 324 ? -18.102 26.119  9.693   1.00 96.13  ? 461 ASN   A OD1 1 
ATOM   2415 N  ND2 . ASN   A 1 324 ? -19.310 24.496  8.709   1.00 86.19  ? 461 ASN   A ND2 1 
ATOM   2416 N  N   . ASN   A 1 325 ? -21.210 29.673  9.210   1.00 94.84  ? 462 ASN   A N   1 
ATOM   2417 C  CA  . ASN   A 1 325 ? -22.061 30.785  9.631   1.00 95.40  ? 462 ASN   A CA  1 
ATOM   2418 C  C   . ASN   A 1 325 ? -22.163 31.878  8.569   1.00 94.19  ? 462 ASN   A C   1 
ATOM   2419 O  O   . ASN   A 1 325 ? -22.554 33.018  8.885   1.00 89.64  ? 462 ASN   A O   1 
ATOM   2420 C  CB  . ASN   A 1 325 ? -21.552 31.383  10.945  1.00 98.51  ? 462 ASN   A CB  1 
ATOM   2421 C  CG  . ASN   A 1 325 ? -22.197 30.742  12.171  1.00 100.63 ? 462 ASN   A CG  1 
ATOM   2422 O  OD1 . ASN   A 1 325 ? -23.327 30.236  12.107  1.00 107.99 ? 462 ASN   A OD1 1 
ATOM   2423 N  ND2 . ASN   A 1 325 ? -21.485 30.757  13.289  1.00 94.30  ? 462 ASN   A ND2 1 
ATOM   2424 N  N   . THR   A 1 326 ? -21.787 31.553  7.332   1.00 84.59  ? 463 THR   A N   1 
ATOM   2425 C  CA  . THR   A 1 326 ? -22.138 32.304  6.142   1.00 89.05  ? 463 THR   A CA  1 
ATOM   2426 C  C   . THR   A 1 326 ? -23.546 31.901  5.691   1.00 88.69  ? 463 THR   A C   1 
ATOM   2427 O  O   . THR   A 1 326 ? -24.093 30.883  6.131   1.00 82.80  ? 463 THR   A O   1 
ATOM   2428 C  CB  . THR   A 1 326 ? -21.119 32.035  5.039   1.00 90.45  ? 463 THR   A CB  1 
ATOM   2429 O  OG1 . THR   A 1 326 ? -21.155 30.639  4.718   1.00 91.83  ? 463 THR   A OG1 1 
ATOM   2430 C  CG2 . THR   A 1 326 ? -19.730 32.380  5.514   1.00 89.10  ? 463 THR   A CG2 1 
ATOM   2431 N  N   . SER   A 1 327 ? -24.138 32.708  4.799   1.00 79.42  ? 464 SER   A N   1 
ATOM   2432 C  CA  . SER   A 1 327 ? -25.506 32.480  4.337   1.00 86.99  ? 464 SER   A CA  1 
ATOM   2433 C  C   . SER   A 1 327 ? -25.580 31.620  3.085   1.00 82.65  ? 464 SER   A C   1 
ATOM   2434 O  O   . SER   A 1 327 ? -26.684 31.388  2.573   1.00 81.53  ? 464 SER   A O   1 
ATOM   2435 C  CB  . SER   A 1 327 ? -26.233 33.815  4.077   1.00 77.64  ? 464 SER   A CB  1 
ATOM   2436 O  OG  . SER   A 1 327 ? -25.377 34.832  3.590   1.00 84.74  ? 464 SER   A OG  1 
ATOM   2437 N  N   . ASN   A 1 328 ? -24.445 31.131  2.593   1.00 73.67  ? 465 ASN   A N   1 
ATOM   2438 C  CA  . ASN   A 1 328 ? -24.435 30.456  1.309   1.00 79.16  ? 465 ASN   A CA  1 
ATOM   2439 C  C   . ASN   A 1 328 ? -23.212 29.556  1.205   1.00 79.12  ? 465 ASN   A C   1 
ATOM   2440 O  O   . ASN   A 1 328 ? -22.215 29.731  1.913   1.00 80.80  ? 465 ASN   A O   1 
ATOM   2441 C  CB  . ASN   A 1 328 ? -24.460 31.475  0.166   1.00 77.37  ? 465 ASN   A CB  1 
ATOM   2442 C  CG  . ASN   A 1 328 ? -23.663 32.718  0.483   1.00 71.27  ? 465 ASN   A CG  1 
ATOM   2443 O  OD1 . ASN   A 1 328 ? -22.581 32.642  1.060   1.00 80.52  ? 465 ASN   A OD1 1 
ATOM   2444 N  ND2 . ASN   A 1 328 ? -24.203 33.877  0.118   1.00 62.33  ? 465 ASN   A ND2 1 
ATOM   2445 N  N   . GLU   A 1 329 ? -23.306 28.580  0.309   1.00 69.55  ? 466 GLU   A N   1 
ATOM   2446 C  CA  . GLU   A 1 329 ? -22.221 27.650  0.048   1.00 68.79  ? 466 GLU   A CA  1 
ATOM   2447 C  C   . GLU   A 1 329 ? -21.809 27.837  -1.400  1.00 60.87  ? 466 GLU   A C   1 
ATOM   2448 O  O   . GLU   A 1 329 ? -22.657 27.890  -2.297  1.00 53.76  ? 466 GLU   A O   1 
ATOM   2449 C  CB  . GLU   A 1 329 ? -22.624 26.192  0.322   1.00 58.61  ? 466 GLU   A CB  1 
ATOM   2450 C  CG  . GLU   A 1 329 ? -23.138 25.929  1.742   1.00 62.62  ? 466 GLU   A CG  1 
ATOM   2451 C  CD  . GLU   A 1 329 ? -22.060 25.938  2.832   1.00 74.50  ? 466 GLU   A CD  1 
ATOM   2452 O  OE1 . GLU   A 1 329 ? -20.964 25.364  2.635   1.00 68.59  ? 466 GLU   A OE1 1 
ATOM   2453 O  OE2 . GLU   A 1 329 ? -22.316 26.539  3.909   1.00 86.28  ? 466 GLU   A OE2 1 
ATOM   2454 N  N   . THR   A 1 330 ? -20.513 27.976  -1.608  1.00 53.49  ? 467 THR   A N   1 
ATOM   2455 C  CA  . THR   A 1 330 ? -19.927 28.103  -2.926  1.00 61.64  ? 467 THR   A CA  1 
ATOM   2456 C  C   . THR   A 1 330 ? -19.271 26.793  -3.333  1.00 62.88  ? 467 THR   A C   1 
ATOM   2457 O  O   . THR   A 1 330 ? -18.687 26.093  -2.501  1.00 56.47  ? 467 THR   A O   1 
ATOM   2458 C  CB  . THR   A 1 330 ? -18.899 29.223  -2.929  1.00 63.20  ? 467 THR   A CB  1 
ATOM   2459 O  OG1 . THR   A 1 330 ? -17.956 28.985  -1.870  1.00 72.89  ? 467 THR   A OG1 1 
ATOM   2460 C  CG2 . THR   A 1 330 ? -19.607 30.547  -2.733  1.00 70.50  ? 467 THR   A CG2 1 
ATOM   2461 N  N   . PHE   A 1 331 ? -19.371 26.476  -4.620  1.00 52.71  ? 468 PHE   A N   1 
ATOM   2462 C  CA  . PHE   A 1 331 ? -18.809 25.276  -5.214  1.00 42.95  ? 468 PHE   A CA  1 
ATOM   2463 C  C   . PHE   A 1 331 ? -17.899 25.689  -6.364  1.00 46.76  ? 468 PHE   A C   1 
ATOM   2464 O  O   . PHE   A 1 331 ? -18.172 26.672  -7.052  1.00 46.24  ? 468 PHE   A O   1 
ATOM   2465 C  CB  . PHE   A 1 331 ? -19.939 24.353  -5.679  1.00 45.12  ? 468 PHE   A CB  1 
ATOM   2466 C  CG  . PHE   A 1 331 ? -20.809 23.873  -4.551  1.00 55.47  ? 468 PHE   A CG  1 
ATOM   2467 C  CD1 . PHE   A 1 331 ? -21.829 24.674  -4.054  1.00 55.57  ? 468 PHE   A CD1 1 
ATOM   2468 C  CD2 . PHE   A 1 331 ? -20.588 22.636  -3.963  1.00 52.70  ? 468 PHE   A CD2 1 
ATOM   2469 C  CE1 . PHE   A 1 331 ? -22.616 24.248  -2.998  1.00 57.08  ? 468 PHE   A CE1 1 
ATOM   2470 C  CE2 . PHE   A 1 331 ? -21.373 22.199  -2.900  1.00 50.36  ? 468 PHE   A CE2 1 
ATOM   2471 C  CZ  . PHE   A 1 331 ? -22.393 23.001  -2.420  1.00 59.91  ? 468 PHE   A CZ  1 
ATOM   2472 N  N   . ARG   A 1 332 ? -16.802 24.967  -6.549  1.00 47.44  ? 469 ARG   A N   1 
ATOM   2473 C  CA  . ARG   A 1 332 ? -15.896 25.223  -7.661  1.00 48.34  ? 469 ARG   A CA  1 
ATOM   2474 C  C   . ARG   A 1 332 ? -15.593 23.926  -8.386  1.00 39.63  ? 469 ARG   A C   1 
ATOM   2475 O  O   . ARG   A 1 332 ? -15.617 22.862  -7.772  1.00 45.38  ? 469 ARG   A O   1 
ATOM   2476 C  CB  . ARG   A 1 332 ? -14.576 25.840  -7.198  1.00 52.23  ? 469 ARG   A CB  1 
ATOM   2477 C  CG  . ARG   A 1 332 ? -14.752 27.076  -6.400  1.00 57.91  ? 469 ARG   A CG  1 
ATOM   2478 C  CD  . ARG   A 1 332 ? -13.704 27.175  -5.324  1.00 60.97  ? 469 ARG   A CD  1 
ATOM   2479 N  NE  . ARG   A 1 332 ? -13.304 28.555  -5.078  1.00 73.34  ? 469 ARG   A NE  1 
ATOM   2480 C  CZ  . ARG   A 1 332 ? -14.120 29.519  -4.670  1.00 65.20  ? 469 ARG   A CZ  1 
ATOM   2481 N  NH1 . ARG   A 1 332 ? -15.411 29.301  -4.460  1.00 79.18  ? 469 ARG   A NH1 1 
ATOM   2482 N  NH2 . ARG   A 1 332 ? -13.633 30.736  -4.476  1.00 66.56  ? 469 ARG   A NH2 1 
ATOM   2483 N  N   . PRO   A 1 333 ? -15.320 23.979  -9.684  1.00 39.89  ? 470 PRO   A N   1 
ATOM   2484 C  CA  . PRO   A 1 333 ? -14.996 22.744  -10.412 1.00 46.45  ? 470 PRO   A CA  1 
ATOM   2485 C  C   . PRO   A 1 333 ? -13.595 22.272  -10.060 1.00 51.61  ? 470 PRO   A C   1 
ATOM   2486 O  O   . PRO   A 1 333 ? -12.671 23.075  -9.904  1.00 50.85  ? 470 PRO   A O   1 
ATOM   2487 C  CB  . PRO   A 1 333 ? -15.104 23.152  -11.889 1.00 36.21  ? 470 PRO   A CB  1 
ATOM   2488 C  CG  . PRO   A 1 333 ? -14.910 24.629  -11.909 1.00 44.05  ? 470 PRO   A CG  1 
ATOM   2489 C  CD  . PRO   A 1 333 ? -15.444 25.142  -10.579 1.00 53.67  ? 470 PRO   A CD  1 
ATOM   2490 N  N   . GLY   A 1 334 ? -13.438 20.953  -9.919  1.00 54.92  ? 471 GLY   A N   1 
ATOM   2491 C  CA  . GLY   A 1 334 ? -12.136 20.451  -9.532  1.00 59.13  ? 471 GLY   A CA  1 
ATOM   2492 C  C   . GLY   A 1 334 ? -11.911 18.964  -9.677  1.00 55.58  ? 471 GLY   A C   1 
ATOM   2493 O  O   . GLY   A 1 334 ? -12.439 18.169  -8.892  1.00 68.47  ? 471 GLY   A O   1 
ATOM   2494 N  N   . GLY   A 1 335 ? -11.121 18.565  -10.666 1.00 58.88  ? 472 GLY   A N   1 
ATOM   2495 C  CA  . GLY   A 1 335 ? -10.734 17.167  -10.744 1.00 57.42  ? 472 GLY   A CA  1 
ATOM   2496 C  C   . GLY   A 1 335 ? -9.266  16.920  -10.445 1.00 58.11  ? 472 GLY   A C   1 
ATOM   2497 O  O   . GLY   A 1 335 ? -8.681  17.512  -9.531  1.00 51.44  ? 472 GLY   A O   1 
ATOM   2498 N  N   . GLY   A 1 336 ? -8.662  16.044  -11.241 1.00 54.61  ? 473 GLY   A N   1 
ATOM   2499 C  CA  . GLY   A 1 336 ? -7.267  15.704  -11.081 1.00 49.06  ? 473 GLY   A CA  1 
ATOM   2500 C  C   . GLY   A 1 336 ? -7.048  14.255  -10.694 1.00 47.56  ? 473 GLY   A C   1 
ATOM   2501 O  O   . GLY   A 1 336 ? -6.177  13.598  -11.277 1.00 55.37  ? 473 GLY   A O   1 
ATOM   2502 N  N   . ASP   A 1 337 ? -7.797  13.752  -9.703  1.00 47.79  ? 474 ASP   A N   1 
ATOM   2503 C  CA  . ASP   A 1 337 ? -7.721  12.339  -9.320  1.00 52.01  ? 474 ASP   A CA  1 
ATOM   2504 C  C   . ASP   A 1 337 ? -8.653  11.538  -10.217 1.00 46.03  ? 474 ASP   A C   1 
ATOM   2505 O  O   . ASP   A 1 337 ? -9.869  11.487  -9.976  1.00 45.65  ? 474 ASP   A O   1 
ATOM   2506 C  CB  . ASP   A 1 337 ? -8.084  12.123  -7.850  1.00 49.15  ? 474 ASP   A CB  1 
ATOM   2507 C  CG  . ASP   A 1 337 ? -7.921  10.650  -7.412  1.00 57.56  ? 474 ASP   A CG  1 
ATOM   2508 O  OD1 . ASP   A 1 337 ? -7.235  9.874   -8.107  1.00 52.93  ? 474 ASP   A OD1 1 
ATOM   2509 O  OD2 . ASP   A 1 337 ? -8.457  10.267  -6.351  1.00 69.27  ? 474 ASP   A OD2 1 
ATOM   2510 N  N   . MET   A 1 338 ? -8.086  10.905  -11.250 1.00 42.71  ? 475 MET   A N   1 
ATOM   2511 C  CA  . MET   A 1 338 ? -8.901  10.214  -12.234 1.00 41.37  ? 475 MET   A CA  1 
ATOM   2512 C  C   . MET   A 1 338 ? -9.727  9.097   -11.647 1.00 44.81  ? 475 MET   A C   1 
ATOM   2513 O  O   . MET   A 1 338 ? -10.616 8.601   -12.349 1.00 46.86  ? 475 MET   A O   1 
ATOM   2514 C  CB  . MET   A 1 338 ? -8.033  9.650   -13.363 1.00 44.02  ? 475 MET   A CB  1 
ATOM   2515 C  CG  . MET   A 1 338 ? -7.580  10.698  -14.369 1.00 53.39  ? 475 MET   A CG  1 
ATOM   2516 S  SD  . MET   A 1 338 ? -8.823  11.940  -14.740 1.00 105.20 ? 475 MET   A SD  1 
ATOM   2517 C  CE  . MET   A 1 338 ? -7.776  13.373  -14.860 1.00 52.36  ? 475 MET   A CE  1 
ATOM   2518 N  N   . ARG   A 1 339 ? -9.435  8.652   -10.418 1.00 39.21  ? 476 ARG   A N   1 
ATOM   2519 C  CA  . ARG   A 1 339 ? -10.210 7.548   -9.859  1.00 42.74  ? 476 ARG   A CA  1 
ATOM   2520 C  C   . ARG   A 1 339 ? -11.672 7.941   -9.713  1.00 40.44  ? 476 ARG   A C   1 
ATOM   2521 O  O   . ARG   A 1 339 ? -12.567 7.097   -9.864  1.00 41.12  ? 476 ARG   A O   1 
ATOM   2522 C  CB  . ARG   A 1 339 ? -9.642  7.104   -8.511  1.00 45.68  ? 476 ARG   A CB  1 
ATOM   2523 C  CG  . ARG   A 1 339 ? -8.410  6.224   -8.598  1.00 48.24  ? 476 ARG   A CG  1 
ATOM   2524 C  CD  . ARG   A 1 339 ? -7.912  5.860   -7.202  1.00 55.92  ? 476 ARG   A CD  1 
ATOM   2525 N  NE  . ARG   A 1 339 ? -7.109  6.948   -6.659  1.00 60.20  ? 476 ARG   A NE  1 
ATOM   2526 C  CZ  . ARG   A 1 339 ? -5.814  6.863   -6.386  1.00 68.42  ? 476 ARG   A CZ  1 
ATOM   2527 N  NH1 . ARG   A 1 339 ? -5.146  5.720   -6.511  1.00 66.08  ? 476 ARG   A NH1 1 
ATOM   2528 N  NH2 . ARG   A 1 339 ? -5.168  7.950   -5.982  1.00 66.48  ? 476 ARG   A NH2 1 
ATOM   2529 N  N   . ASP   A 1 340 ? -11.928 9.225   -9.435  1.00 38.62  ? 477 ASP   A N   1 
ATOM   2530 C  CA  . ASP   A 1 340 ? -13.303 9.701   -9.351  1.00 41.85  ? 477 ASP   A CA  1 
ATOM   2531 C  C   . ASP   A 1 340 ? -14.023 9.571   -10.693 1.00 43.96  ? 477 ASP   A C   1 
ATOM   2532 O  O   . ASP   A 1 340 ? -15.242 9.321   -10.709 1.00 41.24  ? 477 ASP   A O   1 
ATOM   2533 C  CB  . ASP   A 1 340 ? -13.334 11.146  -8.856  1.00 49.55  ? 477 ASP   A CB  1 
ATOM   2534 C  CG  . ASP   A 1 340 ? -12.840 11.290  -7.416  1.00 51.92  ? 477 ASP   A CG  1 
ATOM   2535 O  OD1 . ASP   A 1 340 ? -12.850 10.298  -6.652  1.00 50.20  ? 477 ASP   A OD1 1 
ATOM   2536 O  OD2 . ASP   A 1 340 ? -12.485 12.431  -7.041  1.00 69.04  ? 477 ASP   A OD2 1 
ATOM   2537 N  N   . ASN   A 1 341 ? -13.291 9.712   -11.818 1.00 38.43  ? 478 ASN   A N   1 
ATOM   2538 C  CA  . ASN   A 1 341 ? -13.889 9.482   -13.140 1.00 39.52  ? 478 ASN   A CA  1 
ATOM   2539 C  C   . ASN   A 1 341 ? -14.363 8.044   -13.264 1.00 39.94  ? 478 ASN   A C   1 
ATOM   2540 O  O   . ASN   A 1 341 ? -15.498 7.792   -13.693 1.00 36.73  ? 478 ASN   A O   1 
ATOM   2541 C  CB  . ASN   A 1 341 ? -12.905 9.835   -14.265 1.00 34.59  ? 478 ASN   A CB  1 
ATOM   2542 C  CG  . ASN   A 1 341 ? -12.690 11.340  -14.388 1.00 44.35  ? 478 ASN   A CG  1 
ATOM   2543 O  OD1 . ASN   A 1 341 ? -12.577 12.011  -13.382 1.00 40.74  ? 478 ASN   A OD1 1 
ATOM   2544 N  ND2 . ASN   A 1 341 ? -12.619 11.865  -15.621 1.00 39.69  ? 478 ASN   A ND2 1 
ATOM   2545 N  N   . TRP   A 1 342 ? -13.513 7.086   -12.849 1.00 37.54  ? 479 TRP   A N   1 
ATOM   2546 C  CA  . TRP   A 1 342 ? -13.902 5.679   -12.870 1.00 34.44  ? 479 TRP   A CA  1 
ATOM   2547 C  C   . TRP   A 1 342 ? -15.041 5.414   -11.889 1.00 35.28  ? 479 TRP   A C   1 
ATOM   2548 O  O   . TRP   A 1 342 ? -16.007 4.710   -12.229 1.00 38.16  ? 479 TRP   A O   1 
ATOM   2549 C  CB  . TRP   A 1 342 ? -12.694 4.772   -12.576 1.00 36.46  ? 479 TRP   A CB  1 
ATOM   2550 C  CG  . TRP   A 1 342 ? -11.371 5.245   -13.167 1.00 40.46  ? 479 TRP   A CG  1 
ATOM   2551 C  CD1 . TRP   A 1 342 ? -10.136 5.107   -12.600 1.00 40.37  ? 479 TRP   A CD1 1 
ATOM   2552 C  CD2 . TRP   A 1 342 ? -11.165 5.929   -14.410 1.00 39.00  ? 479 TRP   A CD2 1 
ATOM   2553 N  NE1 . TRP   A 1 342 ? -9.187  5.665   -13.404 1.00 41.13  ? 479 TRP   A NE1 1 
ATOM   2554 C  CE2 . TRP   A 1 342 ? -9.785  6.175   -14.522 1.00 34.13  ? 479 TRP   A CE2 1 
ATOM   2555 C  CE3 . TRP   A 1 342 ? -12.014 6.372   -15.433 1.00 36.18  ? 479 TRP   A CE3 1 
ATOM   2556 C  CZ2 . TRP   A 1 342 ? -9.229  6.830   -15.617 1.00 42.08  ? 479 TRP   A CZ2 1 
ATOM   2557 C  CZ3 . TRP   A 1 342 ? -11.451 7.030   -16.532 1.00 32.72  ? 479 TRP   A CZ3 1 
ATOM   2558 C  CH2 . TRP   A 1 342 ? -10.080 7.252   -16.607 1.00 39.33  ? 479 TRP   A CH2 1 
ATOM   2559 N  N   . ARG   A 1 343 ? -14.963 6.005   -10.691 1.00 28.84  ? 480 ARG   A N   1 
ATOM   2560 C  CA  . ARG   A 1 343 ? -16.005 5.833   -9.678  1.00 36.34  ? 480 ARG   A CA  1 
ATOM   2561 C  C   . ARG   A 1 343 ? -17.384 6.249   -10.184 1.00 45.21  ? 480 ARG   A C   1 
ATOM   2562 O  O   . ARG   A 1 343 ? -18.399 5.664   -9.782  1.00 38.90  ? 480 ARG   A O   1 
ATOM   2563 C  CB  . ARG   A 1 343 ? -15.640 6.666   -8.459  1.00 34.15  ? 480 ARG   A CB  1 
ATOM   2564 C  CG  . ARG   A 1 343 ? -15.713 6.012   -7.145  1.00 41.68  ? 480 ARG   A CG  1 
ATOM   2565 C  CD  . ARG   A 1 343 ? -15.299 7.051   -6.074  1.00 43.23  ? 480 ARG   A CD  1 
ATOM   2566 N  NE  . ARG   A 1 343 ? -13.860 7.285   -6.015  1.00 48.91  ? 480 ARG   A NE  1 
ATOM   2567 C  CZ  . ARG   A 1 343 ? -12.983 6.428   -5.499  1.00 47.10  ? 480 ARG   A CZ  1 
ATOM   2568 N  NH1 . ARG   A 1 343 ? -13.359 5.252   -5.021  1.00 44.49  ? 480 ARG   A NH1 1 
ATOM   2569 N  NH2 . ARG   A 1 343 ? -11.696 6.759   -5.456  1.00 56.93  ? 480 ARG   A NH2 1 
ATOM   2570 N  N   . SER   A 1 344 ? -17.450 7.278   -11.029 1.00 39.78  ? 481 SER   A N   1 
ATOM   2571 C  CA  . SER   A 1 344 ? -18.748 7.791   -11.438 1.00 37.88  ? 481 SER   A CA  1 
ATOM   2572 C  C   . SER   A 1 344 ? -19.495 6.801   -12.332 1.00 45.87  ? 481 SER   A C   1 
ATOM   2573 O  O   . SER   A 1 344 ? -20.699 6.980   -12.555 1.00 40.81  ? 481 SER   A O   1 
ATOM   2574 C  CB  . SER   A 1 344 ? -18.590 9.151   -12.116 1.00 36.55  ? 481 SER   A CB  1 
ATOM   2575 O  OG  . SER   A 1 344 ? -17.882 9.059   -13.330 1.00 41.05  ? 481 SER   A OG  1 
ATOM   2576 N  N   . GLU   A 1 345 ? -18.817 5.749   -12.804 1.00 33.06  ? 482 GLU   A N   1 
ATOM   2577 C  CA  . GLU   A 1 345 ? -19.425 4.653   -13.550 1.00 42.19  ? 482 GLU   A CA  1 
ATOM   2578 C  C   . GLU   A 1 345 ? -19.435 3.314   -12.810 1.00 42.40  ? 482 GLU   A C   1 
ATOM   2579 O  O   . GLU   A 1 345 ? -20.301 2.484   -13.096 1.00 42.83  ? 482 GLU   A O   1 
ATOM   2580 C  CB  . GLU   A 1 345 ? -18.710 4.477   -14.894 1.00 40.72  ? 482 GLU   A CB  1 
ATOM   2581 C  CG  . GLU   A 1 345 ? -18.780 5.685   -15.834 1.00 43.06  ? 482 GLU   A CG  1 
ATOM   2582 C  CD  . GLU   A 1 345 ? -20.159 5.924   -16.428 1.00 48.61  ? 482 GLU   A CD  1 
ATOM   2583 O  OE1 . GLU   A 1 345 ? -20.875 4.940   -16.697 1.00 59.61  ? 482 GLU   A OE1 1 
ATOM   2584 O  OE2 . GLU   A 1 345 ? -20.512 7.105   -16.682 1.00 46.04  ? 482 GLU   A OE2 1 
ATOM   2585 N  N   . LEU   A 1 346 ? -18.496 3.060   -11.880 1.00 36.08  ? 483 LEU   A N   1 
ATOM   2586 C  CA  . LEU   A 1 346 ? -18.459 1.791   -11.147 1.00 43.43  ? 483 LEU   A CA  1 
ATOM   2587 C  C   . LEU   A 1 346 ? -19.314 1.829   -9.899  1.00 35.75  ? 483 LEU   A C   1 
ATOM   2588 O  O   . LEU   A 1 346 ? -19.419 0.810   -9.209  1.00 39.69  ? 483 LEU   A O   1 
ATOM   2589 C  CB  . LEU   A 1 346 ? -17.013 1.434   -10.755 1.00 33.61  ? 483 LEU   A CB  1 
ATOM   2590 C  CG  . LEU   A 1 346 ? -16.176 1.135   -11.992 1.00 34.54  ? 483 LEU   A CG  1 
ATOM   2591 C  CD1 . LEU   A 1 346 ? -14.710 1.155   -11.620 1.00 38.79  ? 483 LEU   A CD1 1 
ATOM   2592 C  CD2 . LEU   A 1 346 ? -16.574 -0.243  -12.546 1.00 36.39  ? 483 LEU   A CD2 1 
ATOM   2593 N  N   . TYR   A 1 347 ? -19.916 2.985   -9.600  1.00 33.35  ? 484 TYR   A N   1 
ATOM   2594 C  CA  . TYR   A 1 347 ? -20.559 3.190   -8.312  1.00 37.27  ? 484 TYR   A CA  1 
ATOM   2595 C  C   . TYR   A 1 347 ? -21.635 2.157   -8.018  1.00 45.98  ? 484 TYR   A C   1 
ATOM   2596 O  O   . TYR   A 1 347 ? -22.000 1.975   -6.853  1.00 42.58  ? 484 TYR   A O   1 
ATOM   2597 C  CB  . TYR   A 1 347 ? -21.174 4.580   -8.259  1.00 31.90  ? 484 TYR   A CB  1 
ATOM   2598 C  CG  . TYR   A 1 347 ? -22.371 4.724   -9.158  1.00 43.83  ? 484 TYR   A CG  1 
ATOM   2599 C  CD1 . TYR   A 1 347 ? -22.202 4.974   -10.523 1.00 39.99  ? 484 TYR   A CD1 1 
ATOM   2600 C  CD2 . TYR   A 1 347 ? -23.662 4.587   -8.673  1.00 40.72  ? 484 TYR   A CD2 1 
ATOM   2601 C  CE1 . TYR   A 1 347 ? -23.269 5.085   -11.369 1.00 34.98  ? 484 TYR   A CE1 1 
ATOM   2602 C  CE2 . TYR   A 1 347 ? -24.756 4.700   -9.529  1.00 41.62  ? 484 TYR   A CE2 1 
ATOM   2603 C  CZ  . TYR   A 1 347 ? -24.545 4.958   -10.874 1.00 39.98  ? 484 TYR   A CZ  1 
ATOM   2604 O  OH  . TYR   A 1 347 ? -25.609 5.090   -11.750 1.00 48.88  ? 484 TYR   A OH  1 
ATOM   2605 N  N   . LYS   A 1 348 ? -22.213 1.532   -9.040  1.00 40.45  ? 485 LYS   A N   1 
ATOM   2606 C  CA  . LYS   A 1 348 ? -23.302 0.592   -8.815  1.00 39.78  ? 485 LYS   A CA  1 
ATOM   2607 C  C   . LYS   A 1 348 ? -22.826 -0.858  -8.738  1.00 40.32  ? 485 LYS   A C   1 
ATOM   2608 O  O   . LYS   A 1 348 ? -23.641 -1.768  -8.542  1.00 38.39  ? 485 LYS   A O   1 
ATOM   2609 C  CB  . LYS   A 1 348 ? -24.373 0.775   -9.907  1.00 44.17  ? 485 LYS   A CB  1 
ATOM   2610 C  CG  . LYS   A 1 348 ? -23.908 0.553   -11.338 1.00 48.60  ? 485 LYS   A CG  1 
ATOM   2611 C  CD  . LYS   A 1 348 ? -25.047 0.068   -12.260 1.00 50.74  ? 485 LYS   A CD  1 
ATOM   2612 C  CE  . LYS   A 1 348 ? -26.015 1.187   -12.592 1.00 54.31  ? 485 LYS   A CE  1 
ATOM   2613 N  NZ  . LYS   A 1 348 ? -26.314 1.225   -14.059 1.00 68.22  ? 485 LYS   A NZ  1 
ATOM   2614 N  N   . TYR   A 1 349 ? -21.529 -1.096  -8.822  1.00 32.70  ? 486 TYR   A N   1 
ATOM   2615 C  CA  . TYR   A 1 349 ? -21.012 -2.455  -8.805  1.00 33.45  ? 486 TYR   A CA  1 
ATOM   2616 C  C   . TYR   A 1 349 ? -20.179 -2.725  -7.550  1.00 43.14  ? 486 TYR   A C   1 
ATOM   2617 O  O   . TYR   A 1 349 ? -19.611 -1.808  -6.938  1.00 35.91  ? 486 TYR   A O   1 
ATOM   2618 C  CB  . TYR   A 1 349 ? -20.170 -2.707  -10.062 1.00 33.99  ? 486 TYR   A CB  1 
ATOM   2619 C  CG  . TYR   A 1 349 ? -20.895 -2.523  -11.400 1.00 38.40  ? 486 TYR   A CG  1 
ATOM   2620 C  CD1 . TYR   A 1 349 ? -21.850 -3.442  -11.822 1.00 40.16  ? 486 TYR   A CD1 1 
ATOM   2621 C  CD2 . TYR   A 1 349 ? -20.573 -1.479  -12.268 1.00 43.01  ? 486 TYR   A CD2 1 
ATOM   2622 C  CE1 . TYR   A 1 349 ? -22.495 -3.314  -13.044 1.00 38.80  ? 486 TYR   A CE1 1 
ATOM   2623 C  CE2 . TYR   A 1 349 ? -21.210 -1.338  -13.515 1.00 42.21  ? 486 TYR   A CE2 1 
ATOM   2624 C  CZ  . TYR   A 1 349 ? -22.169 -2.264  -13.891 1.00 47.22  ? 486 TYR   A CZ  1 
ATOM   2625 O  OH  . TYR   A 1 349 ? -22.829 -2.170  -15.104 1.00 40.97  ? 486 TYR   A OH  1 
ATOM   2626 N  N   . LYS   A 1 350 ? -20.086 -4.004  -7.191  1.00 45.39  ? 487 LYS   A N   1 
ATOM   2627 C  CA  . LYS   A 1 350 ? -19.224 -4.451  -6.107  1.00 47.94  ? 487 LYS   A CA  1 
ATOM   2628 C  C   . LYS   A 1 350 ? -18.979 -5.948  -6.258  1.00 43.36  ? 487 LYS   A C   1 
ATOM   2629 O  O   . LYS   A 1 350 ? -19.852 -6.694  -6.716  1.00 45.06  ? 487 LYS   A O   1 
ATOM   2630 C  CB  . LYS   A 1 350 ? -19.839 -4.139  -4.747  1.00 37.84  ? 487 LYS   A CB  1 
ATOM   2631 C  CG  . LYS   A 1 350 ? -20.721 -5.226  -4.218  1.00 49.77  ? 487 LYS   A CG  1 
ATOM   2632 C  CD  . LYS   A 1 350 ? -20.563 -5.349  -2.716  1.00 66.19  ? 487 LYS   A CD  1 
ATOM   2633 C  CE  . LYS   A 1 350 ? -21.861 -5.770  -2.054  1.00 60.80  ? 487 LYS   A CE  1 
ATOM   2634 N  NZ  . LYS   A 1 350 ? -21.833 -5.483  -0.577  1.00 68.56  ? 487 LYS   A NZ  1 
ATOM   2635 N  N   . VAL   A 1 351 ? -17.800 -6.367  -5.911  1.00 45.73  ? 488 VAL   A N   1 
ATOM   2636 C  CA  . VAL   A 1 351 ? -17.403 -7.755  -6.097  1.00 46.36  ? 488 VAL   A CA  1 
ATOM   2637 C  C   . VAL   A 1 351 ? -17.675 -8.537  -4.817  1.00 45.95  ? 488 VAL   A C   1 
ATOM   2638 O  O   . VAL   A 1 351 ? -17.491 -8.027  -3.704  1.00 42.63  ? 488 VAL   A O   1 
ATOM   2639 C  CB  . VAL   A 1 351 ? -15.923 -7.845  -6.483  1.00 44.21  ? 488 VAL   A CB  1 
ATOM   2640 C  CG1 . VAL   A 1 351 ? -15.440 -9.279  -6.329  1.00 46.74  ? 488 VAL   A CG1 1 
ATOM   2641 C  CG2 . VAL   A 1 351 ? -15.730 -7.341  -7.893  1.00 37.74  ? 488 VAL   A CG2 1 
ATOM   2642 N  N   . VAL   A 1 352 ? -18.123 -9.779  -4.975  1.00 45.97  ? 489 VAL   A N   1 
ATOM   2643 C  CA  . VAL   A 1 352 ? -18.403 -10.661 -3.853  1.00 44.99  ? 489 VAL   A CA  1 
ATOM   2644 C  C   . VAL   A 1 352 ? -17.920 -12.051 -4.204  1.00 50.20  ? 489 VAL   A C   1 
ATOM   2645 O  O   . VAL   A 1 352 ? -17.955 -12.462 -5.365  1.00 48.97  ? 489 VAL   A O   1 
ATOM   2646 C  CB  . VAL   A 1 352 ? -19.899 -10.702 -3.487  1.00 46.27  ? 489 VAL   A CB  1 
ATOM   2647 C  CG1 . VAL   A 1 352 ? -20.378 -9.326  -3.050  1.00 43.26  ? 489 VAL   A CG1 1 
ATOM   2648 C  CG2 . VAL   A 1 352 ? -20.739 -11.254 -4.652  1.00 43.71  ? 489 VAL   A CG2 1 
ATOM   2649 N  N   . GLN   A 1 353 ? -17.458 -12.772 -3.189  1.00 52.86  ? 490 GLN   A N   1 
ATOM   2650 C  CA  . GLN   A 1 353 ? -17.015 -14.150 -3.326  1.00 55.77  ? 490 GLN   A CA  1 
ATOM   2651 C  C   . GLN   A 1 353 ? -18.190 -15.057 -3.011  1.00 56.07  ? 490 GLN   A C   1 
ATOM   2652 O  O   . GLN   A 1 353 ? -18.863 -14.872 -1.991  1.00 50.95  ? 490 GLN   A O   1 
ATOM   2653 C  CB  . GLN   A 1 353 ? -15.849 -14.449 -2.380  1.00 54.62  ? 490 GLN   A CB  1 
ATOM   2654 C  CG  . GLN   A 1 353 ? -15.313 -15.876 -2.470  1.00 62.12  ? 490 GLN   A CG  1 
ATOM   2655 C  CD  . GLN   A 1 353 ? -14.006 -16.072 -1.709  1.00 67.67  ? 490 GLN   A CD  1 
ATOM   2656 O  OE1 . GLN   A 1 353 ? -13.813 -15.533 -0.617  1.00 81.37  ? 490 GLN   A OE1 1 
ATOM   2657 N  NE2 . GLN   A 1 353 ? -13.097 -16.842 -2.294  1.00 76.36  ? 490 GLN   A NE2 1 
ATOM   2658 N  N   . ILE   A 1 354 ? -18.451 -16.016 -3.896  1.00 62.84  ? 491 ILE   A N   1 
ATOM   2659 C  CA  . ILE   A 1 354 ? -19.513 -16.982 -3.654  1.00 56.19  ? 491 ILE   A CA  1 
ATOM   2660 C  C   . ILE   A 1 354 ? -19.053 -17.900 -2.530  1.00 66.40  ? 491 ILE   A C   1 
ATOM   2661 O  O   . ILE   A 1 354 ? -18.212 -18.776 -2.742  1.00 71.85  ? 491 ILE   A O   1 
ATOM   2662 C  CB  . ILE   A 1 354 ? -19.861 -17.766 -4.919  1.00 64.63  ? 491 ILE   A CB  1 
ATOM   2663 C  CG1 . ILE   A 1 354 ? -20.742 -16.903 -5.818  1.00 57.22  ? 491 ILE   A CG1 1 
ATOM   2664 C  CG2 . ILE   A 1 354 ? -20.552 -19.072 -4.567  1.00 65.58  ? 491 ILE   A CG2 1 
ATOM   2665 C  CD1 . ILE   A 1 354 ? -21.892 -16.275 -5.085  1.00 51.58  ? 491 ILE   A CD1 1 
ATOM   2666 N  N   . GLU   A 1 355 ? -19.570 -17.673 -1.326  1.00 69.58  ? 492 GLU   A N   1 
ATOM   2667 C  CA  . GLU   A 1 355 ? -19.223 -18.477 -0.162  1.00 77.46  ? 492 GLU   A CA  1 
ATOM   2668 C  C   . GLU   A 1 355 ? -20.142 -19.693 -0.111  1.00 83.30  ? 492 GLU   A C   1 
ATOM   2669 O  O   . GLU   A 1 355 ? -20.244 -20.368 0.914   1.00 89.77  ? 492 GLU   A O   1 
ATOM   2670 C  CB  . GLU   A 1 355 ? -19.316 -17.630 1.129   1.00 73.47  ? 492 GLU   A CB  1 
ATOM   2671 C  CG  . GLU   A 1 355 ? -18.065 -17.667 2.031   1.00 75.78  ? 492 GLU   A CG  1 
ATOM   2672 C  CD  . GLU   A 1 355 ? -18.300 -17.041 3.410   1.00 91.42  ? 492 GLU   A CD  1 
ATOM   2673 O  OE1 . GLU   A 1 355 ? -19.335 -16.362 3.595   1.00 83.22  ? 492 GLU   A OE1 1 
ATOM   2674 O  OE2 . GLU   A 1 355 ? -17.457 -17.247 4.319   1.00 97.23  ? 492 GLU   A OE2 1 
ATOM   2675 O  OXT . GLU   A 1 355 ? -20.821 -20.040 -1.093  1.00 83.89  ? 492 GLU   A OXT 1 
HETATM 2676 C  C1  . NAG   B 2 .   ? -26.680 8.494   0.456   1.00 55.80  ? 501 NAG   A C1  1 
HETATM 2677 C  C2  . NAG   B 2 .   ? -26.458 9.720   1.325   1.00 57.52  ? 501 NAG   A C2  1 
HETATM 2678 C  C3  . NAG   B 2 .   ? -26.177 9.289   2.764   1.00 65.74  ? 501 NAG   A C3  1 
HETATM 2679 C  C4  . NAG   B 2 .   ? -27.305 8.401   3.272   1.00 63.70  ? 501 NAG   A C4  1 
HETATM 2680 C  C5  . NAG   B 2 .   ? -27.538 7.237   2.308   1.00 60.59  ? 501 NAG   A C5  1 
HETATM 2681 C  C6  . NAG   B 2 .   ? -28.740 6.398   2.671   1.00 57.05  ? 501 NAG   A C6  1 
HETATM 2682 C  C7  . NAG   B 2 .   ? -25.575 11.604  0.004   1.00 57.51  ? 501 NAG   A C7  1 
HETATM 2683 C  C8  . NAG   B 2 .   ? -24.346 12.327  -0.461  1.00 47.04  ? 501 NAG   A C8  1 
HETATM 2684 N  N2  . NAG   B 2 .   ? -25.375 10.542  0.799   1.00 59.30  ? 501 NAG   A N2  1 
HETATM 2685 O  O3  . NAG   B 2 .   ? -26.053 10.428  3.607   1.00 64.75  ? 501 NAG   A O3  1 
HETATM 2686 O  O4  . NAG   B 2 .   ? -26.982 7.912   4.569   1.00 58.89  ? 501 NAG   A O4  1 
HETATM 2687 O  O5  . NAG   B 2 .   ? -27.765 7.727   0.976   1.00 57.62  ? 501 NAG   A O5  1 
HETATM 2688 O  O6  . NAG   B 2 .   ? -28.372 5.036   2.842   1.00 69.58  ? 501 NAG   A O6  1 
HETATM 2689 O  O7  . NAG   B 2 .   ? -26.698 11.970  -0.320  1.00 62.01  ? 501 NAG   A O7  1 
HETATM 2690 C  C1  . NAG   C 2 .   ? -35.183 -3.495  -10.453 1.00 73.52  ? 502 NAG   A C1  1 
HETATM 2691 C  C2  . NAG   C 2 .   ? -36.528 -2.921  -10.926 1.00 73.98  ? 502 NAG   A C2  1 
HETATM 2692 C  C3  . NAG   C 2 .   ? -36.435 -2.382  -12.368 1.00 82.95  ? 502 NAG   A C3  1 
HETATM 2693 C  C4  . NAG   C 2 .   ? -35.734 -3.355  -13.318 1.00 88.64  ? 502 NAG   A C4  1 
HETATM 2694 C  C5  . NAG   C 2 .   ? -34.560 -4.046  -12.636 1.00 93.20  ? 502 NAG   A C5  1 
HETATM 2695 C  C6  . NAG   C 2 .   ? -33.318 -4.138  -13.494 1.00 80.50  ? 502 NAG   A C6  1 
HETATM 2696 C  C7  . NAG   C 2 .   ? -37.864 -4.573  -9.684  1.00 88.14  ? 502 NAG   A C7  1 
HETATM 2697 C  C8  . NAG   C 2 .   ? -38.971 -5.579  -9.767  1.00 84.04  ? 502 NAG   A C8  1 
HETATM 2698 N  N2  . NAG   C 2 .   ? -37.580 -3.920  -10.818 1.00 85.06  ? 502 NAG   A N2  1 
HETATM 2699 O  O3  . NAG   C 2 .   ? -35.771 -1.122  -12.375 1.00 91.62  ? 502 NAG   A O3  1 
HETATM 2700 O  O4  . NAG   C 2 .   ? -36.640 -4.359  -13.761 1.00 84.35  ? 502 NAG   A O4  1 
HETATM 2701 O  O5  . NAG   C 2 .   ? -34.210 -3.318  -11.455 1.00 92.47  ? 502 NAG   A O5  1 
HETATM 2702 O  O6  . NAG   C 2 .   ? -32.577 -5.314  -13.190 1.00 78.28  ? 502 NAG   A O6  1 
HETATM 2703 O  O7  . NAG   C 2 .   ? -37.257 -4.360  -8.636  1.00 94.25  ? 502 NAG   A O7  1 
HETATM 2704 C  C1  . NAG   D 2 .   ? -17.022 11.338  -26.893 1.00 46.69  ? 503 NAG   A C1  1 
HETATM 2705 C  C2  . NAG   D 2 .   ? -15.593 11.658  -27.337 1.00 49.34  ? 503 NAG   A C2  1 
HETATM 2706 C  C3  . NAG   D 2 .   ? -15.573 12.106  -28.794 1.00 48.17  ? 503 NAG   A C3  1 
HETATM 2707 C  C4  . NAG   D 2 .   ? -16.229 11.048  -29.673 1.00 50.72  ? 503 NAG   A C4  1 
HETATM 2708 C  C5  . NAG   D 2 .   ? -17.654 10.834  -29.175 1.00 57.55  ? 503 NAG   A C5  1 
HETATM 2709 C  C6  . NAG   D 2 .   ? -18.457 9.820   -29.970 1.00 52.61  ? 503 NAG   A C6  1 
HETATM 2710 C  C7  . NAG   D 2 .   ? -13.943 12.395  -25.698 1.00 47.98  ? 503 NAG   A C7  1 
HETATM 2711 C  C8  . NAG   D 2 .   ? -13.407 13.535  -24.878 1.00 47.48  ? 503 NAG   A C8  1 
HETATM 2712 N  N2  . NAG   D 2 .   ? -14.984 12.667  -26.483 1.00 45.99  ? 503 NAG   A N2  1 
HETATM 2713 O  O3  . NAG   D 2 .   ? -14.229 12.349  -29.190 1.00 49.40  ? 503 NAG   A O3  1 
HETATM 2714 O  O4  . NAG   D 2 .   ? -16.251 11.471  -31.030 1.00 58.69  ? 503 NAG   A O4  1 
HETATM 2715 O  O5  . NAG   D 2 .   ? -17.617 10.390  -27.809 1.00 49.29  ? 503 NAG   A O5  1 
HETATM 2716 O  O6  . NAG   D 2 .   ? -18.013 8.481   -29.791 1.00 50.48  ? 503 NAG   A O6  1 
HETATM 2717 O  O7  . NAG   D 2 .   ? -13.464 11.278  -25.643 1.00 49.53  ? 503 NAG   A O7  1 
HETATM 2718 C  C1  . NAG   E 2 .   ? -17.973 13.949  7.770   1.00 67.63  ? 504 NAG   A C1  1 
HETATM 2719 C  C2  . NAG   E 2 .   ? -17.756 13.071  9.012   1.00 59.19  ? 504 NAG   A C2  1 
HETATM 2720 C  C3  . NAG   E 2 .   ? -17.874 13.902  10.293  1.00 70.10  ? 504 NAG   A C3  1 
HETATM 2721 C  C4  . NAG   E 2 .   ? -16.929 15.096  10.237  1.00 69.92  ? 504 NAG   A C4  1 
HETATM 2722 C  C5  . NAG   E 2 .   ? -17.265 15.925  9.003   1.00 69.05  ? 504 NAG   A C5  1 
HETATM 2723 C  C6  . NAG   E 2 .   ? -16.424 17.177  8.842   1.00 58.83  ? 504 NAG   A C6  1 
HETATM 2724 C  C7  . NAG   E 2 .   ? -18.290 10.688  8.912   1.00 74.52  ? 504 NAG   A C7  1 
HETATM 2725 C  C8  . NAG   E 2 .   ? -19.372 9.653   8.959   1.00 63.49  ? 504 NAG   A C8  1 
HETATM 2726 N  N2  . NAG   E 2 .   ? -18.688 11.957  9.038   1.00 64.00  ? 504 NAG   A N2  1 
HETATM 2727 O  O3  . NAG   E 2 .   ? -17.589 13.087  11.426  1.00 71.42  ? 504 NAG   A O3  1 
HETATM 2728 O  O4  . NAG   E 2 .   ? -17.073 15.904  11.399  1.00 69.47  ? 504 NAG   A O4  1 
HETATM 2729 O  O5  . NAG   E 2 .   ? -17.089 15.114  7.829   1.00 72.48  ? 504 NAG   A O5  1 
HETATM 2730 O  O6  . NAG   E 2 .   ? -15.130 16.927  8.305   1.00 62.71  ? 504 NAG   A O6  1 
HETATM 2731 O  O7  . NAG   E 2 .   ? -17.103 10.390  8.759   1.00 63.97  ? 504 NAG   A O7  1 
HETATM 2732 C  C1  . NAG   F 2 .   ? -33.661 15.563  -13.810 1.00 56.68  ? 505 NAG   A C1  1 
HETATM 2733 C  C2  . NAG   F 2 .   ? -35.090 15.646  -14.359 1.00 66.89  ? 505 NAG   A C2  1 
HETATM 2734 C  C3  . NAG   F 2 .   ? -35.758 16.940  -13.895 1.00 71.09  ? 505 NAG   A C3  1 
HETATM 2735 C  C4  . NAG   F 2 .   ? -35.695 17.051  -12.377 1.00 70.01  ? 505 NAG   A C4  1 
HETATM 2736 C  C5  . NAG   F 2 .   ? -34.250 16.940  -11.906 1.00 66.32  ? 505 NAG   A C5  1 
HETATM 2737 C  C6  . NAG   F 2 .   ? -34.129 16.942  -10.399 1.00 68.62  ? 505 NAG   A C6  1 
HETATM 2738 C  C7  . NAG   F 2 .   ? -35.185 14.399  -16.466 1.00 65.66  ? 505 NAG   A C7  1 
HETATM 2739 C  C8  . NAG   F 2 .   ? -35.164 14.485  -17.960 1.00 64.63  ? 505 NAG   A C8  1 
HETATM 2740 N  N2  . NAG   F 2 .   ? -35.095 15.559  -15.810 1.00 58.71  ? 505 NAG   A N2  1 
HETATM 2741 O  O3  . NAG   F 2 .   ? -37.109 16.979  -14.344 1.00 81.80  ? 505 NAG   A O3  1 
HETATM 2742 O  O4  . NAG   F 2 .   ? -36.206 18.307  -11.950 1.00 79.79  ? 505 NAG   A O4  1 
HETATM 2743 O  O5  . NAG   F 2 .   ? -33.683 15.707  -12.373 1.00 59.94  ? 505 NAG   A O5  1 
HETATM 2744 O  O6  . NAG   F 2 .   ? -32.781 16.792  -9.976  1.00 63.35  ? 505 NAG   A O6  1 
HETATM 2745 O  O7  . NAG   F 2 .   ? -35.280 13.325  -15.878 1.00 77.63  ? 505 NAG   A O7  1 
HETATM 2746 C  C1  . NAG   G 2 .   ? -19.235 21.678  -34.020 1.00 57.33  ? 506 NAG   A C1  1 
HETATM 2747 C  C2  . NAG   G 2 .   ? -20.320 21.336  -35.054 1.00 66.56  ? 506 NAG   A C2  1 
HETATM 2748 C  C3  . NAG   G 2 .   ? -19.778 21.535  -36.473 1.00 74.72  ? 506 NAG   A C3  1 
HETATM 2749 C  C4  . NAG   G 2 .   ? -19.189 22.930  -36.635 1.00 73.17  ? 506 NAG   A C4  1 
HETATM 2750 C  C5  . NAG   G 2 .   ? -18.125 23.149  -35.567 1.00 65.90  ? 506 NAG   A C5  1 
HETATM 2751 C  C6  . NAG   G 2 .   ? -17.501 24.524  -35.613 1.00 62.25  ? 506 NAG   A C6  1 
HETATM 2752 C  C7  . NAG   G 2 .   ? -21.958 19.661  -34.285 1.00 67.99  ? 506 NAG   A C7  1 
HETATM 2753 C  C8  . NAG   G 2 .   ? -22.294 18.200  -34.232 1.00 61.77  ? 506 NAG   A C8  1 
HETATM 2754 N  N2  . NAG   G 2 .   ? -20.805 19.974  -34.889 1.00 66.51  ? 506 NAG   A N2  1 
HETATM 2755 O  O3  . NAG   G 2 .   ? -20.808 21.313  -37.430 1.00 75.80  ? 506 NAG   A O3  1 
HETATM 2756 O  O4  . NAG   G 2 .   ? -18.597 23.068  -37.922 1.00 77.29  ? 506 NAG   A O4  1 
HETATM 2757 O  O5  . NAG   G 2 .   ? -18.723 22.997  -34.272 1.00 69.12  ? 506 NAG   A O5  1 
HETATM 2758 O  O6  . NAG   G 2 .   ? -18.224 25.450  -34.814 1.00 74.60  ? 506 NAG   A O6  1 
HETATM 2759 O  O7  . NAG   G 2 .   ? -22.687 20.516  -33.787 1.00 73.43  ? 506 NAG   A O7  1 
HETATM 2760 C  C1  . NAG   H 2 .   ? -30.332 24.897  -27.318 1.00 69.13  ? 507 NAG   A C1  1 
HETATM 2761 C  C2  . NAG   H 2 .   ? -30.838 24.865  -28.773 1.00 79.57  ? 507 NAG   A C2  1 
HETATM 2762 C  C3  . NAG   H 2 .   ? -32.357 25.049  -28.836 1.00 76.89  ? 507 NAG   A C3  1 
HETATM 2763 C  C4  . NAG   H 2 .   ? -33.051 24.072  -27.897 1.00 80.46  ? 507 NAG   A C4  1 
HETATM 2764 C  C5  . NAG   H 2 .   ? -32.518 24.299  -26.494 1.00 77.49  ? 507 NAG   A C5  1 
HETATM 2765 C  C6  . NAG   H 2 .   ? -33.165 23.421  -25.447 1.00 83.48  ? 507 NAG   A C6  1 
HETATM 2766 C  C7  . NAG   H 2 .   ? -29.442 25.613  -30.652 1.00 77.52  ? 507 NAG   A C7  1 
HETATM 2767 C  C8  . NAG   H 2 .   ? -28.803 26.787  -31.332 1.00 86.62  ? 507 NAG   A C8  1 
HETATM 2768 N  N2  . NAG   H 2 .   ? -30.164 25.887  -29.562 1.00 77.40  ? 507 NAG   A N2  1 
HETATM 2769 O  O3  . NAG   H 2 .   ? -32.800 24.844  -30.173 1.00 85.72  ? 507 NAG   A O3  1 
HETATM 2770 O  O4  . NAG   H 2 .   ? -34.462 24.249  -27.905 1.00 88.95  ? 507 NAG   A O4  1 
HETATM 2771 O  O5  . NAG   H 2 .   ? -31.118 24.004  -26.499 1.00 66.24  ? 507 NAG   A O5  1 
HETATM 2772 O  O6  . NAG   H 2 .   ? -32.410 22.244  -25.190 1.00 81.87  ? 507 NAG   A O6  1 
HETATM 2773 O  O7  . NAG   H 2 .   ? -29.320 24.472  -31.076 1.00 72.52  ? 507 NAG   A O7  1 
HETATM 2774 C  C1  . NAG   I 2 .   ? -10.611 32.312  -17.637 1.00 62.95  ? 508 NAG   A C1  1 
HETATM 2775 C  C2  . NAG   I 2 .   ? -9.283  32.670  -16.948 1.00 66.26  ? 508 NAG   A C2  1 
HETATM 2776 C  C3  . NAG   I 2 .   ? -9.495  33.819  -15.961 1.00 75.28  ? 508 NAG   A C3  1 
HETATM 2777 C  C4  . NAG   I 2 .   ? -10.129 35.007  -16.670 1.00 59.74  ? 508 NAG   A C4  1 
HETATM 2778 C  C5  . NAG   I 2 .   ? -11.447 34.559  -17.287 1.00 64.36  ? 508 NAG   A C5  1 
HETATM 2779 C  C6  . NAG   I 2 .   ? -12.157 35.657  -18.044 1.00 75.68  ? 508 NAG   A C6  1 
HETATM 2780 C  C7  . NAG   I 2 .   ? -7.459  31.116  -16.404 1.00 71.73  ? 508 NAG   A C7  1 
HETATM 2781 C  C8  . NAG   I 2 .   ? -7.063  29.899  -15.622 1.00 71.87  ? 508 NAG   A C8  1 
HETATM 2782 N  N2  . NAG   I 2 .   ? -8.728  31.513  -16.263 1.00 66.27  ? 508 NAG   A N2  1 
HETATM 2783 O  O3  . NAG   I 2 .   ? -8.264  34.174  -15.339 1.00 71.42  ? 508 NAG   A O3  1 
HETATM 2784 O  O4  . NAG   I 2 .   ? -10.392 36.060  -15.751 1.00 85.67  ? 508 NAG   A O4  1 
HETATM 2785 O  O5  . NAG   I 2 .   ? -11.196 33.501  -18.223 1.00 58.54  ? 508 NAG   A O5  1 
HETATM 2786 O  O6  . NAG   I 2 .   ? -11.544 35.906  -19.303 1.00 68.97  ? 508 NAG   A O6  1 
HETATM 2787 O  O7  . NAG   I 2 .   ? -6.669  31.704  -17.138 1.00 76.95  ? 508 NAG   A O7  1 
HETATM 2788 C  C1  . NAG   J 2 .   ? -24.854 11.461  -26.073 1.00 74.10  ? 509 NAG   A C1  1 
HETATM 2789 C  C2  . NAG   J 2 .   ? -24.542 10.033  -26.553 1.00 75.39  ? 509 NAG   A C2  1 
HETATM 2790 C  C3  . NAG   J 2 .   ? -25.661 9.503   -27.452 1.00 70.74  ? 509 NAG   A C3  1 
HETATM 2791 C  C4  . NAG   J 2 .   ? -27.014 9.660   -26.770 1.00 78.85  ? 509 NAG   A C4  1 
HETATM 2792 C  C5  . NAG   J 2 .   ? -27.216 11.115  -26.359 1.00 78.95  ? 509 NAG   A C5  1 
HETATM 2793 C  C6  . NAG   J 2 .   ? -28.504 11.353  -25.607 1.00 81.60  ? 509 NAG   A C6  1 
HETATM 2794 C  C7  . NAG   J 2 .   ? -22.167 9.431   -26.740 1.00 66.09  ? 509 NAG   A C7  1 
HETATM 2795 C  C8  . NAG   J 2 .   ? -20.933 9.511   -27.591 1.00 60.17  ? 509 NAG   A C8  1 
HETATM 2796 N  N2  . NAG   J 2 .   ? -23.266 9.999   -27.249 1.00 69.21  ? 509 NAG   A N2  1 
HETATM 2797 O  O3  . NAG   J 2 .   ? -25.424 8.125   -27.712 1.00 87.61  ? 509 NAG   A O3  1 
HETATM 2798 O  O4  . NAG   J 2 .   ? -28.065 9.243   -27.637 1.00 95.14  ? 509 NAG   A O4  1 
HETATM 2799 O  O5  . NAG   J 2 .   ? -26.154 11.500  -25.476 1.00 72.28  ? 509 NAG   A O5  1 
HETATM 2800 O  O6  . NAG   J 2 .   ? -28.264 12.027  -24.378 1.00 81.71  ? 509 NAG   A O6  1 
HETATM 2801 O  O7  . NAG   J 2 .   ? -22.169 8.873   -25.645 1.00 64.22  ? 509 NAG   A O7  1 
HETATM 2802 N  N1  . EPE   K 3 .   ? -4.972  -7.047  -16.968 1.00 58.69  ? 510 EPE   A N1  1 
HETATM 2803 C  C2  . EPE   K 3 .   ? -4.638  -6.526  -15.635 1.00 51.66  ? 510 EPE   A C2  1 
HETATM 2804 C  C3  . EPE   K 3 .   ? -5.894  -6.531  -14.771 1.00 49.80  ? 510 EPE   A C3  1 
HETATM 2805 N  N4  . EPE   K 3 .   ? -7.048  -5.990  -15.472 1.00 47.83  ? 510 EPE   A N4  1 
HETATM 2806 C  C5  . EPE   K 3 .   ? -7.197  -6.258  -16.893 1.00 41.51  ? 510 EPE   A C5  1 
HETATM 2807 C  C6  . EPE   K 3 .   ? -5.878  -6.105  -17.634 1.00 41.04  ? 510 EPE   A C6  1 
HETATM 2808 C  C7  . EPE   K 3 .   ? -8.222  -5.598  -14.707 1.00 45.55  ? 510 EPE   A C7  1 
HETATM 2809 C  C8  . EPE   K 3 .   ? -7.928  -4.596  -13.595 1.00 51.34  ? 510 EPE   A C8  1 
HETATM 2810 O  O8  . EPE   K 3 .   ? -7.476  -5.245  -12.424 1.00 50.43  ? 510 EPE   A O8  1 
HETATM 2811 C  C9  . EPE   K 3 .   ? -3.760  -7.310  -17.750 1.00 51.24  ? 510 EPE   A C9  1 
HETATM 2812 C  C10 . EPE   K 3 .   ? -3.872  -8.643  -18.480 1.00 57.09  ? 510 EPE   A C10 1 
HETATM 2813 S  S   . EPE   K 3 .   ? -2.318  -9.074  -19.312 1.00 55.99  ? 510 EPE   A S   1 
HETATM 2814 O  O1S . EPE   K 3 .   ? -1.807  -7.926  -20.047 1.00 58.49  ? 510 EPE   A O1S 1 
HETATM 2815 O  O2S . EPE   K 3 .   ? -1.357  -9.420  -18.267 1.00 62.88  ? 510 EPE   A O2S 1 
HETATM 2816 O  O3S . EPE   K 3 .   ? -2.516  -10.190 -20.213 1.00 45.68  ? 510 EPE   A O3S 1 
HETATM 2817 C  C10 . A1ATE L 4 .   ? -4.126  15.987  -13.914 1.00 40.78  ? 511 A1ATE A C10 1 
HETATM 2818 C  CG  . A1ATE L 4 .   ? -2.512  10.420  -6.751  1.00 78.01  ? 511 A1ATE A CG  1 
HETATM 2819 N  ND1 . A1ATE L 4 .   ? -2.527  9.137   -6.481  1.00 82.75  ? 511 A1ATE A ND1 1 
HETATM 2820 C  CD2 . A1ATE L 4 .   ? -2.631  11.259  -5.328  1.00 73.75  ? 511 A1ATE A CD2 1 
HETATM 2821 C  CE1 . A1ATE L 4 .   ? -3.033  10.436  -4.417  1.00 71.70  ? 511 A1ATE A CE1 1 
HETATM 2822 C  CE2 . A1ATE L 4 .   ? -2.502  9.064   -4.900  1.00 71.65  ? 511 A1ATE A CE2 1 
HETATM 2823 C  CZ  . A1ATE L 4 .   ? -2.535  7.975   -7.408  1.00 84.43  ? 511 A1ATE A CZ  1 
HETATM 2824 N  NH1 . A1ATE L 4 .   ? -2.549  8.097   -8.670  1.00 77.45  ? 511 A1ATE A NH1 1 
HETATM 2825 N  NH2 . A1ATE L 4 .   ? -2.537  6.807   -6.923  1.00 77.52  ? 511 A1ATE A NH2 1 
HETATM 2826 C  C01 . A1ATE L 4 .   ? -1.178  10.716  -7.470  1.00 80.16  ? 511 A1ATE A C01 1 
HETATM 2827 C  C03 . A1ATE L 4 .   ? 0.180   11.684  -9.408  1.00 73.32  ? 511 A1ATE A C03 1 
HETATM 2828 C  C04 . A1ATE L 4 .   ? 0.425   13.101  -9.905  1.00 81.51  ? 511 A1ATE A C04 1 
HETATM 2829 C  C06 . A1ATE L 4 .   ? -0.796  15.202  -10.401 1.00 66.57  ? 511 A1ATE A C06 1 
HETATM 2830 C  C08 . A1ATE L 4 .   ? -3.356  15.860  -11.264 1.00 58.23  ? 511 A1ATE A C08 1 
HETATM 2831 C  C09 . A1ATE L 4 .   ? -3.083  16.137  -12.759 1.00 51.76  ? 511 A1ATE A C09 1 
HETATM 2832 C  C13 . A1ATE L 4 .   ? -4.258  15.768  -16.466 1.00 43.33  ? 511 A1ATE A C13 1 
HETATM 2833 C  C14 . A1ATE L 4 .   ? -5.637  15.638  -16.445 1.00 42.42  ? 511 A1ATE A C14 1 
HETATM 2834 C  C15 . A1ATE L 4 .   ? -6.308  15.509  -17.631 1.00 45.30  ? 511 A1ATE A C15 1 
HETATM 2835 C  C17 . A1ATE L 4 .   ? -5.607  15.500  -18.823 1.00 46.11  ? 511 A1ATE A C17 1 
HETATM 2836 C  C19 . A1ATE L 4 .   ? -4.238  15.629  -18.842 1.00 42.98  ? 511 A1ATE A C19 1 
HETATM 2837 C  C20 . A1ATE L 4 .   ? -3.558  15.768  -17.653 1.00 43.55  ? 511 A1ATE A C20 1 
HETATM 2838 C  C21 . A1ATE L 4 .   ? -2.638  17.577  -12.937 1.00 57.96  ? 511 A1ATE A C21 1 
HETATM 2839 C  C22 . A1ATE L 4 .   ? -1.443  18.082  -12.193 1.00 60.92  ? 511 A1ATE A C22 1 
HETATM 2840 C  C23 . A1ATE L 4 .   ? -1.486  17.492  -10.751 1.00 62.45  ? 511 A1ATE A C23 1 
HETATM 2841 C  C25 . A1ATE L 4 .   ? -1.880  12.882  -10.622 1.00 64.71  ? 511 A1ATE A C25 1 
HETATM 2842 C  C26 . A1ATE L 4 .   ? -2.242  11.993  -9.445  1.00 68.83  ? 511 A1ATE A C26 1 
HETATM 2843 C  C27 . A1ATE L 4 .   ? -1.278  19.604  -11.878 1.00 68.19  ? 511 A1ATE A C27 1 
HETATM 2844 F  F16 . A1ATE L 4 .   ? -7.654  15.405  -17.611 1.00 49.77  ? 511 A1ATE A F16 1 
HETATM 2845 N  N02 . A1ATE L 4 .   ? -1.091  11.450  -8.742  1.00 70.47  ? 511 A1ATE A N02 1 
HETATM 2846 N  N05 . A1ATE L 4 .   ? -0.788  13.759  -10.316 1.00 70.05  ? 511 A1ATE A N05 1 
HETATM 2847 N  N07 . A1ATE L 4 .   ? -1.918  16.074  -10.764 1.00 72.39  ? 511 A1ATE A N07 1 
HETATM 2848 N  N12 . A1ATE L 4 .   ? -3.508  15.907  -15.247 1.00 42.54  ? 511 A1ATE A N12 1 
HETATM 2849 O  O11 . A1ATE L 4 .   ? -5.285  15.946  -13.725 1.00 46.36  ? 511 A1ATE A O11 1 
HETATM 2850 O  O24 . A1ATE L 4 .   ? 0.231   15.699  -10.096 1.00 80.68  ? 511 A1ATE A O24 1 
HETATM 2851 O  O27 . A1ATE L 4 .   ? -0.174  10.320  -6.982  1.00 85.23  ? 511 A1ATE A O27 1 
HETATM 2852 O  O28 . A1ATE L 4 .   ? -0.020  19.724  -11.226 1.00 77.04  ? 511 A1ATE A O28 1 
HETATM 2853 CL CL1 . A1ATE L 4 .   ? -6.428  15.314  -20.389 1.00 83.63  ? 511 A1ATE A CL1 1 
HETATM 2854 O  O   . HOH   M 5 .   ? -0.623  -1.427  -25.631 1.00 57.04  ? 601 HOH   A O   1 
HETATM 2855 O  O   . HOH   M 5 .   ? -29.973 31.796  -12.019 1.00 60.29  ? 602 HOH   A O   1 
HETATM 2856 O  O   . HOH   M 5 .   ? -19.091 18.495  -35.412 1.00 65.86  ? 603 HOH   A O   1 
HETATM 2857 O  O   . HOH   M 5 .   ? -20.853 34.626  -18.502 1.00 76.24  ? 604 HOH   A O   1 
HETATM 2858 O  O   . HOH   M 5 .   ? -3.509  13.527  -32.717 1.00 50.95  ? 605 HOH   A O   1 
HETATM 2859 O  O   . HOH   M 5 .   ? -15.467 17.302  -26.582 1.00 53.92  ? 606 HOH   A O   1 
HETATM 2860 O  O   . HOH   M 5 .   ? -24.473 22.320  -25.949 1.00 53.61  ? 607 HOH   A O   1 
HETATM 2861 O  O   . HOH   M 5 .   ? -15.141 7.527   -27.484 1.00 46.33  ? 608 HOH   A O   1 
HETATM 2862 O  O   . HOH   M 5 .   ? -31.881 17.669  -16.267 1.00 48.44  ? 609 HOH   A O   1 
HETATM 2863 O  O   . HOH   M 5 .   ? -8.126  -10.409 -27.153 1.00 55.70  ? 610 HOH   A O   1 
HETATM 2864 O  O   . HOH   M 5 .   ? -10.118 9.080   -4.846  1.00 56.08  ? 611 HOH   A O   1 
HETATM 2865 O  O   . HOH   M 5 .   ? -31.560 9.416   -11.145 1.00 53.85  ? 612 HOH   A O   1 
HETATM 2866 O  O   . HOH   M 5 .   ? -15.271 8.842   -25.527 1.00 45.45  ? 613 HOH   A O   1 
HETATM 2867 O  O   . HOH   M 5 .   ? -10.199 17.761  -7.465  1.00 69.96  ? 614 HOH   A O   1 
HETATM 2868 O  O   . HOH   M 5 .   ? -19.688 0.497   -5.737  1.00 39.55  ? 615 HOH   A O   1 
HETATM 2869 O  O   . HOH   M 5 .   ? -19.046 9.226   -16.272 1.00 43.24  ? 616 HOH   A O   1 
HETATM 2870 O  O   . HOH   M 5 .   ? -1.095  12.437  -18.889 1.00 50.45  ? 617 HOH   A O   1 
HETATM 2871 O  O   . HOH   M 5 .   ? -19.063 -13.926 -18.840 1.00 67.97  ? 618 HOH   A O   1 
HETATM 2872 O  O   . HOH   M 5 .   ? -17.007 6.905   -18.901 1.00 45.78  ? 619 HOH   A O   1 
HETATM 2873 O  O   . HOH   M 5 .   ? -14.493 8.896   -17.836 1.00 49.35  ? 620 HOH   A O   1 
HETATM 2874 O  O   . HOH   M 5 .   ? -4.828  9.925   -9.299  1.00 57.03  ? 621 HOH   A O   1 
HETATM 2875 O  O   . HOH   M 5 .   ? -1.077  17.898  -26.850 1.00 44.94  ? 622 HOH   A O   1 
HETATM 2876 O  O   . HOH   M 5 .   ? -32.141 12.449  -20.508 1.00 66.10  ? 623 HOH   A O   1 
HETATM 2877 O  O   . HOH   M 5 .   ? -10.919 11.081  -24.651 1.00 42.17  ? 624 HOH   A O   1 
HETATM 2878 O  O   . HOH   M 5 .   ? -8.258  7.124   -22.326 1.00 44.03  ? 625 HOH   A O   1 
HETATM 2879 O  O   . HOH   M 5 .   ? -15.919 -4.326  -5.400  1.00 42.10  ? 626 HOH   A O   1 
HETATM 2880 O  O   . HOH   M 5 .   ? -14.858 12.113  -18.250 1.00 39.30  ? 627 HOH   A O   1 
HETATM 2881 O  O   . HOH   M 5 .   ? -37.884 27.276  -0.329  1.00 68.07  ? 628 HOH   A O   1 
HETATM 2882 O  O   . HOH   M 5 .   ? -22.394 9.981   -23.021 1.00 50.16  ? 629 HOH   A O   1 
HETATM 2883 O  O   . HOH   M 5 .   ? -24.127 -4.459  -16.123 1.00 52.05  ? 630 HOH   A O   1 
HETATM 2884 O  O   . HOH   M 5 .   ? -12.216 2.738   -4.084  1.00 48.55  ? 631 HOH   A O   1 
HETATM 2885 O  O   . HOH   M 5 .   ? -16.043 -2.364  -26.468 1.00 49.41  ? 632 HOH   A O   1 
HETATM 2886 O  O   . HOH   M 5 .   ? -18.806 4.992   -20.436 1.00 44.79  ? 633 HOH   A O   1 
HETATM 2887 O  O   . HOH   M 5 .   ? 2.825   23.245  -15.133 1.00 64.79  ? 634 HOH   A O   1 
HETATM 2888 O  O   . HOH   M 5 .   ? -5.242  10.905  -11.478 1.00 54.92  ? 635 HOH   A O   1 
HETATM 2889 O  O   . HOH   M 5 .   ? -11.088 14.257  -8.743  1.00 48.25  ? 636 HOH   A O   1 
HETATM 2890 O  O   . HOH   M 5 .   ? -16.990 9.496   -18.143 1.00 42.70  ? 637 HOH   A O   1 
HETATM 2891 O  O   . HOH   M 5 .   ? -21.802 9.232   -11.028 1.00 40.37  ? 638 HOH   A O   1 
HETATM 2892 O  O   . HOH   M 5 .   ? -23.177 -10.666 -17.077 1.00 53.73  ? 639 HOH   A O   1 
HETATM 2893 O  O   . HOH   M 5 .   ? -18.786 19.415  0.168   1.00 49.35  ? 640 HOH   A O   1 
HETATM 2894 O  O   . HOH   M 5 .   ? -15.869 12.091  -2.049  1.00 41.61  ? 641 HOH   A O   1 
HETATM 2895 O  O   . HOH   M 5 .   ? -1.970  0.534   -27.159 1.00 47.94  ? 642 HOH   A O   1 
HETATM 2896 O  O   . HOH   M 5 .   ? -7.967  -9.040  -18.656 1.00 41.97  ? 643 HOH   A O   1 
HETATM 2897 O  O   . HOH   M 5 .   ? 2.168   22.457  -17.969 1.00 62.69  ? 644 HOH   A O   1 
HETATM 2898 O  O   . HOH   M 5 .   ? -30.246 13.166  -22.490 1.00 54.37  ? 645 HOH   A O   1 
HETATM 2899 O  O   . HOH   M 5 .   ? -10.917 15.754  -35.803 1.00 58.99  ? 646 HOH   A O   1 
HETATM 2900 O  O   . HOH   M 5 .   ? -9.538  9.794   -22.571 1.00 38.56  ? 647 HOH   A O   1 
HETATM 2901 O  O   . HOH   M 5 .   ? -19.746 32.944  -25.437 1.00 57.56  ? 648 HOH   A O   1 
HETATM 2902 O  O   . HOH   M 5 .   ? -23.792 -6.029  2.436   1.00 54.00  ? 649 HOH   A O   1 
HETATM 2903 O  O   . HOH   M 5 .   ? -27.566 36.820  4.253   1.00 81.70  ? 650 HOH   A O   1 
HETATM 2904 O  O   . HOH   M 5 .   ? -12.823 2.146   -32.254 1.00 47.83  ? 651 HOH   A O   1 
HETATM 2905 O  O   . HOH   M 5 .   ? -11.905 13.060  -2.466  1.00 53.01  ? 652 HOH   A O   1 
HETATM 2906 O  O   . HOH   M 5 .   ? -22.421 32.545  -19.736 1.00 63.10  ? 653 HOH   A O   1 
HETATM 2907 O  O   . HOH   M 5 .   ? -14.663 12.506  5.818   1.00 62.59  ? 654 HOH   A O   1 
HETATM 2908 O  O   . HOH   M 5 .   ? -2.451  -6.044  -29.933 1.00 57.66  ? 655 HOH   A O   1 
HETATM 2909 O  O   . HOH   M 5 .   ? -16.030 -13.740 -21.159 1.00 57.70  ? 656 HOH   A O   1 
HETATM 2910 O  O   . HOH   M 5 .   ? -8.591  13.965  -36.321 1.00 56.84  ? 657 HOH   A O   1 
HETATM 2911 O  O   . HOH   M 5 .   ? -23.950 37.376  -18.939 1.00 84.44  ? 658 HOH   A O   1 
HETATM 2912 O  O   . HOH   M 5 .   ? -17.495 31.041  -34.648 1.00 65.67  ? 659 HOH   A O   1 
HETATM 2913 O  O   . HOH   M 5 .   ? -15.486 32.093  -32.763 1.00 61.66  ? 660 HOH   A O   1 
# 
