data_9BXB
# 
_entry.id   9BXB 
# 
_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   9BXB         pdb_00009bxb 10.2210/pdb9bxb/pdb 
WWPDB D_1000284333 ?            ?                   
# 
_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                        9BXB 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-22 
_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 
'Niu, L.'       1 ? 
'Tolbert, W.D.' 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   10 ? ? ? ? 
3 non-polymer syn '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID'                                238.305   1  ? ? ? ? 
4 non-polymer syn '(3S)-1-(N-carbamimidoylglycyl)-N-(4-chloro-3-fluorophenyl)piperidine-3-carboxamide' 355.795   1  ? ? ? ? 
5 water       nat water                                                                                18.015    21 ? ? ? ? 
# 
_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)-1-(N-carbamimidoylglycyl)-N-(4-chloro-3-fluorophenyl)piperidine-3-carboxamide' A1AS5 
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 
A1AS5 non-polymer                  . '(3S)-1-(N-carbamimidoylglycyl)-N-(4-chloro-3-fluorophenyl)piperidine-3-carboxamide' ? 
'C15 H19 Cl F N5 O2' 355.795 
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  ?   ?   ?   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  195 ?   ?   ?   A . n 
A 1 82  THR 82  196 ?   ?   ?   A . n 
A 1 83  GLY 83  197 ?   ?   ?   A . n 
A 1 84  GLY 84  198 ?   ?   ?   A . n 
A 1 85  SER 85  199 ?   ?   ?   A . n 
A 1 86  VAL 86  200 ?   ?   ?   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 192 322 322 SER SER A . n 
A 1 193 GLY 193 323 323 GLY GLY A . n 
A 1 194 GLY 194 324 324 GLY GLY 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        A1AS5 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AS5 
_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 2 NAG   1  510 511 NAG   NAG A . 
L 3 EPE   1  511 512 EPE   EPE A . 
M 4 A1AS5 1  512 1   A1AS5 MW5 A . 
N 5 HOH   1  601 2   HOH   HOH A . 
N 5 HOH   2  602 12  HOH   HOH A . 
N 5 HOH   3  603 4   HOH   HOH A . 
N 5 HOH   4  604 27  HOH   HOH A . 
N 5 HOH   5  605 8   HOH   HOH A . 
N 5 HOH   6  606 24  HOH   HOH A . 
N 5 HOH   7  607 17  HOH   HOH A . 
N 5 HOH   8  608 7   HOH   HOH A . 
N 5 HOH   9  609 22  HOH   HOH A . 
N 5 HOH   10 610 9   HOH   HOH A . 
N 5 HOH   11 611 14  HOH   HOH A . 
N 5 HOH   12 612 11  HOH   HOH A . 
N 5 HOH   13 613 16  HOH   HOH A . 
N 5 HOH   14 614 26  HOH   HOH A . 
N 5 HOH   15 615 1   HOH   HOH A . 
N 5 HOH   16 616 28  HOH   HOH A . 
N 5 HOH   17 617 13  HOH   HOH A . 
N 5 HOH   18 618 15  HOH   HOH A . 
N 5 HOH   19 619 20  HOH   HOH A . 
N 5 HOH   20 620 10  HOH   HOH A . 
N 5 HOH   21 621 5   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                     9BXB 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     55.836 
_cell.length_a_esd                 ? 
_cell.length_b                     65.373 
_cell.length_b_esd                 ? 
_cell.length_c                     84.045 
_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                         9BXB 
_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                   9BXB 
_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             1.94 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          36.73 
_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         2024-02-02 
_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 BL12-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97946 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL12-1 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9BXB 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.5 
_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                                     10949 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.105 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.97 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.169 
_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                                    2.5 
_reflns_shell.d_res_low                                     2.54 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.3 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             517 
_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                               3.5 
_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                               0.612 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.48 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          94 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.894 
_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                                 9BXB 
_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                            2.50 
_refine.ls_d_res_low                             42.46 
_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                     10904 
_refine.ls_number_reflns_R_free                  524 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.08 
_refine.ls_percent_reflns_R_free                 4.81 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2272 
_refine.ls_R_factor_R_free                       0.2662 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2252 
_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                          1.34 
_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                 25.68 
_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                            0.29 
_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        2646 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         179 
_refine_hist.number_atoms_solvent             21 
_refine_hist.number_atoms_total               2846 
_refine_hist.d_res_high                       2.50 
_refine_hist.d_res_low                        42.46 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008  ? 2893 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.144  ? 3925 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.328 ? 429  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.066  ? 461  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 493  ? 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' 2.50 2.75  . . 113 2552 98.00 . . . . 0.2795 . . . . . . . . . . . 0.3121 
'X-RAY DIFFRACTION' 2.75 3.15  . . 135 2575 99.00 . . . . 0.2491 . . . . . . . . . . . 0.2591 
'X-RAY DIFFRACTION' 3.15 3.97  . . 136 2549 97.00 . . . . 0.2185 . . . . . . . . . . . 0.2657 
'X-RAY DIFFRACTION' 3.97 42.46 . . 140 2704 98.00 . . . . 0.2098 . . . . . . . . . . . 0.2606 
# 
_struct.entry_id                     9BXB 
_struct.title                        'CRYSTAL STRUCTURE OF HIV-1 LM/HS CLADE A/E CRF01 GP120 CORE IN COMPLEX WITH DL-III-14' 
_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        9BXB 
_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 2 ? 
L N N 3 ? 
M N N 4 ? 
N 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              9BXB 
_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 9BXB VAL A 1   ? UNP A0A0M3KKW9 ?   ?   'expression tag'      42  1 
1 9BXB PRO A 2   ? UNP A0A0M3KKW9 ?   ?   'expression tag'      43  2 
1 9BXB TYR A 20  ? UNP A0A0M3KKW9 HIS 18  'engineered mutation' 61  3 
1 9BXB HIS A 64  ? UNP A0A0M3KKW9 GLN 62  'engineered mutation' 105 4 
1 9BXB ILE A 67  ? UNP A0A0M3KKW9 VAL 65  'engineered mutation' 108 5 
1 9BXB SER A 244 ? UNP A0A0M3KKW9 HIS 242 'engineered mutation' 375 6 
1 9BXB ASP A 337 ? UNP A0A0M3KKW9 ASN 335 'engineered mutation' 474 7 
1 9BXB MET A 338 ? UNP A0A0M3KKW9 ILE 336 'engineered mutation' 475 8 
1 9BXB 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,N 
# 
_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 ? ? ? ? ? ? ? 2.030 ? ?               
disulf2  disulf ?   ? A CYS 78  SG  ? ? ? 1_555 A CYS 91  SG ? ? A CYS 119 A CYS 205 1_555 ? ? ? ? ? ? ? 2.031 ? ?               
disulf3  disulf ?   ? A CYS 104 SG  ? ? ? 1_555 A CYS 133 SG ? ? A CYS 218 A CYS 247 1_555 ? ? ? ? ? ? ? 2.039 ? ?               
disulf4  disulf ?   ? A CYS 114 SG  ? ? ? 1_555 A CYS 125 SG ? ? A CYS 228 A CYS 239 1_555 ? ? ? ? ? ? ? 2.038 ? ?               
disulf5  disulf ?   ? A CYS 182 SG  ? ? ? 1_555 A CYS 201 SG ? ? A CYS 296 A CYS 331 1_555 ? ? ? ? ? ? ? 2.034 ? ?               
disulf6  disulf ?   ? A CYS 247 SG  ? ? ? 1_555 A CYS 308 SG ? ? A CYS 378 A CYS 445 1_555 ? ? ? ? ? ? ? 2.038 ? ?               
disulf7  disulf ?   ? A CYS 254 SG  ? ? ? 1_555 A CYS 281 SG ? ? A CYS 385 A CYS 418 1_555 ? ? ? ? ? ? ? 2.039 ? ?               
disulf8  disulf ?   ? A CYS 264 SG  ? ? ? 1_555 A CYS 273 SG ? ? A CYS 395 A CYS 410 1_555 ? ? ? ? ? ? ? 2.018 ? ?               
covale1  covale one ? A ASN 120 ND2 ? ? ? 1_555 B NAG .   C1 ? ? A ASN 234 A NAG 501 1_555 ? ? ? ? ? ? ? 1.434 ? N-Glycosylation 
covale2  covale one ? A ASN 127 ND2 ? ? ? 1_555 C NAG .   C1 ? ? A ASN 241 A NAG 502 1_555 ? ? ? ? ? ? ? 1.439 ? 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 ? ? ? ? ? ? ? 1.445 ? N-Glycosylation 
covale5  covale one ? A ASN 175 ND2 ? ? ? 1_555 F NAG .   C1 ? ? A ASN 289 A NAG 505 1_555 ? ? ? ? ? ? ? 1.454 ? N-Glycosylation 
covale6  covale one ? A ASN 181 ND2 ? ? ? 1_555 G NAG .   C1 ? ? A ASN 295 A NAG 506 1_555 ? ? ? ? ? ? ? 1.442 ? N-Glycosylation 
covale7  covale one ? A ASN 204 ND2 ? ? ? 1_555 H NAG .   C1 ? ? A ASN 334 A NAG 507 1_555 ? ? ? ? ? ? ? 1.441 ? N-Glycosylation 
covale8  covale one ? A ASN 225 ND2 ? ? ? 1_555 K NAG .   C1 ? ? A ASN 355 A NAG 510 1_555 ? ? ? ? ? ? ? 1.421 ? N-Glycosylation 
covale9  covale one ? A ASN 255 ND2 ? ? ? 1_555 I NAG .   C1 ? ? A ASN 386 A NAG 508 1_555 ? ? ? ? ? ? ? 1.439 ? N-Glycosylation 
covale10 covale one ? A ASN 311 ND2 ? ? ? 1_555 J NAG .   C1 ? ? A ASN 448 A NAG 509 1_555 ? ? ? ? ? ? ? 1.432 ? 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 NAG K .   ? ASN A 225 ? NAG A 510 ? 1_555 ASN A 355 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
11 CYS A 13  ? CYS A 33  ? CYS A 54  ? 1_555 CYS A 74  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
12 CYS A 78  ? CYS A 91  ? CYS A 119 ? 1_555 CYS A 205 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
13 CYS A 104 ? CYS A 133 ? CYS A 218 ? 1_555 CYS A 247 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
14 CYS A 114 ? CYS A 125 ? CYS A 228 ? 1_555 CYS A 239 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
15 CYS A 182 ? CYS A 201 ? CYS A 296 ? 1_555 CYS A 331 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
16 CYS A 247 ? CYS A 308 ? CYS A 378 ? 1_555 CYS A 445 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
17 CYS A 254 ? CYS A 281 ? CYS A 385 ? 1_555 CYS A 418 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
18 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 ? 2 ? 
AA2 ? 4 ? 
AA3 ? 2 ? 
AA4 ? 5 ? 
AA5 ? 7 ? 
AA6 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 4 5 ? parallel      
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA5 6 7 ? anti-parallel 
AA6 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 PHE A 12  ? ALA A 14  ? PHE A 53  ALA A 55  
AA1 2 HIS A 102 ? CYS A 104 ? HIS A 216 CYS A 218 
AA2 1 ILE A 43  ? HIS A 44  ? ILE A 84  HIS A 85  
AA2 2 VAL A 128 ? VAL A 131 ? VAL A 242 VAL A 245 
AA2 3 TYR A 109 ? CYS A 114 ? TYR A 223 CYS A 228 
AA2 4 TYR A 349 ? GLN A 353 ? TYR A 486 GLN A 490 
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 LEU A 145 ? LEU A 147 ? LEU A 259 LEU A 261 
AA4 2 ILE A 306 ? ARG A 319 ? ILE A 443 ARG A 456 
AA4 3 ILE A 170 ? ARG A 184 ? ILE A 284 ARG A 298 
AA4 4 ASN A 328 ? PRO A 333 ? ASN A 465 PRO A 470 
AA4 5 THR A 227 ? PHE A 230 ? THR A 358 PHE A 361 
AA5 1 ILE A 157 ? SER A 160 ? ILE A 271 SER A 274 
AA5 2 ILE A 170 ? ARG A 184 ? ILE A 284 ARG A 298 
AA5 3 ILE A 306 ? ARG A 319 ? ILE A 443 ARG A 456 
AA5 4 LYS A 198 ? ASN A 204 ? LYS A 328 ASN A 334 
AA5 5 THR A 276 ? LYS A 284 ? THR A 413 LYS A 421 
AA5 6 GLU A 250 ? CYS A 254 ? GLU A 381 CYS A 385 
AA5 7 HIS A 243 ? CYS A 247 ? HIS A 374 CYS A 378 
AA6 1 ILE A 286 ? ASN A 288 ? ILE A 423 ASN A 425 
AA6 2 GLN A 295 ? MET A 297 ? GLN A 432 MET A 434 
# 
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 ALA A 14  ? N ALA A 55  O HIS A 102 ? O HIS A 216 
AA2 1 2 N ILE A 43  ? N ILE A 84  O SER A 130 ? O SER A 244 
AA2 2 3 O SER A 129 ? O SER A 243 N LYS A 113 ? N LYS A 227 
AA2 3 4 N LEU A 112 ? N LEU A 226 O LYS A 350 ? O LYS A 487 
AA3 1 2 N PHE A 52  ? N PHE A 93  O GLY A 123 ? O GLY A 237 
AA4 1 2 N LEU A 146 ? N LEU A 260 O THR A 313 ? O THR A 450 
AA4 2 3 O ILE A 315 ? O ILE A 452 N VAL A 172 ? N VAL A 286 
AA4 4 5 O PHE A 331 ? O PHE A 468 N ILE A 229 ? N ILE A 360 
AA5 1 2 N ILE A 157 ? N ILE A 271 O HIS A 173 ? O HIS A 287 
AA5 2 3 N VAL A 172 ? N VAL A 286 O ILE A 315 ? O ILE A 452 
AA5 4 5 N CYS A 201 ? N CYS A 331 O LEU A 279 ? O LEU A 416 
AA5 5 6 O LYS A 282 ? O LYS A 419 N TYR A 253 ? N TYR A 384 
AA5 6 7 O CYS A 254 ? O CYS A 385 N HIS A 243 ? N HIS A 374 
AA6 1 2 N ILE A 287 ? N ILE A 424 O ALA A 296 ? O ALA A 433 
# 
_pdbx_entry_details.entry_id                   9BXB 
_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 TRP A 45  ? ? -76.47  -162.38 
2  1 LYS A 46  ? ? -174.79 134.97  
3  1 ASP A 57  ? ? -93.53  42.87   
4  1 PRO A 76  ? ? -63.88  -114.16 
5  1 THR A 77  ? ? 62.05   -54.16  
6  1 ASP A 78  ? ? 78.60   75.06   
7  1 CYS A 205 ? ? -160.55 74.64   
8  1 GLN A 258 ? ? 66.46   -57.92  
9  1 GLU A 268 ? ? -122.70 -92.23  
10 1 ASN A 276 ? ? -166.55 110.55  
11 1 PHE A 353 ? ? -118.79 50.61   
12 1 ASN A 354 ? ? 37.64   63.29   
13 1 ASN A 355 ? ? 38.33   93.24   
14 1 SER A 365 ? ? -99.40  -66.13  
15 1 PHE A 391 ? ? -111.59 50.47   
16 1 CYS A 410 ? ? -175.56 56.62   
17 1 ASN A 411 ? ? -158.38 43.09   
18 1 LYS A 487 ? ? -172.78 136.17  
# 
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 PRO 43  ? A PRO 2   
3  1 Y 1 A LEU 195 ? A LEU 81  
4  1 Y 1 A THR 196 ? A THR 82  
5  1 Y 1 A GLY 197 ? A GLY 83  
6  1 Y 1 A GLY 198 ? A GLY 84  
7  1 Y 1 A SER 199 ? A SER 85  
8  1 Y 1 A VAL 200 ? A VAL 86  
9  1 Y 1 A GLY 318 ? A GLY 188 
10 1 Y 1 A GLY 319 ? A GLY 189 
11 1 Y 1 A SER 320 ? A SER 190 
12 1 Y 1 A GLY 321 ? A GLY 191 
13 1 Y 1 A ILE 402 ? A ILE 265 
14 1 Y 1 A GLY 403 ? A GLY 266 
15 1 Y 1 A ASN 404 ? A ASN 267 
16 1 Y 1 A GLU 405 ? A GLU 268 
17 1 Y 1 A THR 406 ? A THR 269 
18 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 
A1AS5 C10  C  N N 1   
A1AS5 CD   C  N N 2   
A1AS5 NE   N  N N 3   
A1AS5 CZ   C  N N 4   
A1AS5 NH1  N  N N 5   
A1AS5 NH2  N  N N 6   
A1AS5 C06  C  N N 7   
A1AS5 C08  C  N N 8   
A1AS5 C09  C  N S 9   
A1AS5 C13  C  Y N 10  
A1AS5 C14  C  Y N 11  
A1AS5 C15  C  Y N 12  
A1AS5 C17  C  Y N 13  
A1AS5 C19  C  Y N 14  
A1AS5 C20  C  Y N 15  
A1AS5 C21  C  N N 16  
A1AS5 C22  C  N N 17  
A1AS5 C23  C  N N 18  
A1AS5 F16  F  N N 19  
A1AS5 N07  N  N N 20  
A1AS5 N12  N  N N 21  
A1AS5 O11  O  N N 22  
A1AS5 O24  O  N N 23  
A1AS5 CL1  CL N N 24  
A1AS5 H1   H  N N 25  
A1AS5 H2   H  N N 26  
A1AS5 H3   H  N N 27  
A1AS5 H4   H  N N 28  
A1AS5 H5   H  N N 29  
A1AS5 H6   H  N N 30  
A1AS5 H7   H  N N 31  
A1AS5 H8   H  N N 32  
A1AS5 H9   H  N N 33  
A1AS5 H10  H  N N 34  
A1AS5 H11  H  N N 35  
A1AS5 H12  H  N N 36  
A1AS5 H13  H  N N 37  
A1AS5 H14  H  N N 38  
A1AS5 H15  H  N N 39  
A1AS5 H16  H  N N 40  
A1AS5 H17  H  N N 41  
A1AS5 H18  H  N N 42  
A1AS5 H19  H  N N 43  
ALA   N    N  N N 44  
ALA   CA   C  N S 45  
ALA   C    C  N N 46  
ALA   O    O  N N 47  
ALA   CB   C  N N 48  
ALA   OXT  O  N N 49  
ALA   H    H  N N 50  
ALA   H2   H  N N 51  
ALA   HA   H  N N 52  
ALA   HB1  H  N N 53  
ALA   HB2  H  N N 54  
ALA   HB3  H  N N 55  
ALA   HXT  H  N N 56  
ARG   N    N  N N 57  
ARG   CA   C  N S 58  
ARG   C    C  N N 59  
ARG   O    O  N N 60  
ARG   CB   C  N N 61  
ARG   CG   C  N N 62  
ARG   CD   C  N N 63  
ARG   NE   N  N N 64  
ARG   CZ   C  N N 65  
ARG   NH1  N  N N 66  
ARG   NH2  N  N N 67  
ARG   OXT  O  N N 68  
ARG   H    H  N N 69  
ARG   H2   H  N N 70  
ARG   HA   H  N N 71  
ARG   HB2  H  N N 72  
ARG   HB3  H  N N 73  
ARG   HG2  H  N N 74  
ARG   HG3  H  N N 75  
ARG   HD2  H  N N 76  
ARG   HD3  H  N N 77  
ARG   HE   H  N N 78  
ARG   HH11 H  N N 79  
ARG   HH12 H  N N 80  
ARG   HH21 H  N N 81  
ARG   HH22 H  N N 82  
ARG   HXT  H  N N 83  
ASN   N    N  N N 84  
ASN   CA   C  N S 85  
ASN   C    C  N N 86  
ASN   O    O  N N 87  
ASN   CB   C  N N 88  
ASN   CG   C  N N 89  
ASN   OD1  O  N N 90  
ASN   ND2  N  N N 91  
ASN   OXT  O  N N 92  
ASN   H    H  N N 93  
ASN   H2   H  N N 94  
ASN   HA   H  N N 95  
ASN   HB2  H  N N 96  
ASN   HB3  H  N N 97  
ASN   HD21 H  N N 98  
ASN   HD22 H  N N 99  
ASN   HXT  H  N N 100 
ASP   N    N  N N 101 
ASP   CA   C  N S 102 
ASP   C    C  N N 103 
ASP   O    O  N N 104 
ASP   CB   C  N N 105 
ASP   CG   C  N N 106 
ASP   OD1  O  N N 107 
ASP   OD2  O  N N 108 
ASP   OXT  O  N N 109 
ASP   H    H  N N 110 
ASP   H2   H  N N 111 
ASP   HA   H  N N 112 
ASP   HB2  H  N N 113 
ASP   HB3  H  N N 114 
ASP   HD2  H  N N 115 
ASP   HXT  H  N N 116 
CYS   N    N  N N 117 
CYS   CA   C  N R 118 
CYS   C    C  N N 119 
CYS   O    O  N N 120 
CYS   CB   C  N N 121 
CYS   SG   S  N N 122 
CYS   OXT  O  N N 123 
CYS   H    H  N N 124 
CYS   H2   H  N N 125 
CYS   HA   H  N N 126 
CYS   HB2  H  N N 127 
CYS   HB3  H  N N 128 
CYS   HG   H  N N 129 
CYS   HXT  H  N N 130 
EPE   N1   N  N N 131 
EPE   C2   C  N N 132 
EPE   C3   C  N N 133 
EPE   N4   N  N N 134 
EPE   C5   C  N N 135 
EPE   C6   C  N N 136 
EPE   C7   C  N N 137 
EPE   C8   C  N N 138 
EPE   O8   O  N N 139 
EPE   C9   C  N N 140 
EPE   C10  C  N N 141 
EPE   S    S  N N 142 
EPE   O1S  O  N N 143 
EPE   O2S  O  N N 144 
EPE   O3S  O  N N 145 
EPE   H21  H  N N 146 
EPE   H22  H  N N 147 
EPE   H31  H  N N 148 
EPE   H32  H  N N 149 
EPE   H51  H  N N 150 
EPE   H52  H  N N 151 
EPE   H61  H  N N 152 
EPE   H62  H  N N 153 
EPE   H71  H  N N 154 
EPE   H72  H  N N 155 
EPE   H81  H  N N 156 
EPE   H82  H  N N 157 
EPE   HO8  H  N N 158 
EPE   H91  H  N N 159 
EPE   H92  H  N N 160 
EPE   H101 H  N N 161 
EPE   H102 H  N N 162 
EPE   HOS3 H  N N 163 
GLN   N    N  N N 164 
GLN   CA   C  N S 165 
GLN   C    C  N N 166 
GLN   O    O  N N 167 
GLN   CB   C  N N 168 
GLN   CG   C  N N 169 
GLN   CD   C  N N 170 
GLN   OE1  O  N N 171 
GLN   NE2  N  N N 172 
GLN   OXT  O  N N 173 
GLN   H    H  N N 174 
GLN   H2   H  N N 175 
GLN   HA   H  N N 176 
GLN   HB2  H  N N 177 
GLN   HB3  H  N N 178 
GLN   HG2  H  N N 179 
GLN   HG3  H  N N 180 
GLN   HE21 H  N N 181 
GLN   HE22 H  N N 182 
GLN   HXT  H  N N 183 
GLU   N    N  N N 184 
GLU   CA   C  N S 185 
GLU   C    C  N N 186 
GLU   O    O  N N 187 
GLU   CB   C  N N 188 
GLU   CG   C  N N 189 
GLU   CD   C  N N 190 
GLU   OE1  O  N N 191 
GLU   OE2  O  N N 192 
GLU   OXT  O  N N 193 
GLU   H    H  N N 194 
GLU   H2   H  N N 195 
GLU   HA   H  N N 196 
GLU   HB2  H  N N 197 
GLU   HB3  H  N N 198 
GLU   HG2  H  N N 199 
GLU   HG3  H  N N 200 
GLU   HE2  H  N N 201 
GLU   HXT  H  N N 202 
GLY   N    N  N N 203 
GLY   CA   C  N N 204 
GLY   C    C  N N 205 
GLY   O    O  N N 206 
GLY   OXT  O  N N 207 
GLY   H    H  N N 208 
GLY   H2   H  N N 209 
GLY   HA2  H  N N 210 
GLY   HA3  H  N N 211 
GLY   HXT  H  N N 212 
HIS   N    N  N N 213 
HIS   CA   C  N S 214 
HIS   C    C  N N 215 
HIS   O    O  N N 216 
HIS   CB   C  N N 217 
HIS   CG   C  Y N 218 
HIS   ND1  N  Y N 219 
HIS   CD2  C  Y N 220 
HIS   CE1  C  Y N 221 
HIS   NE2  N  Y N 222 
HIS   OXT  O  N N 223 
HIS   H    H  N N 224 
HIS   H2   H  N N 225 
HIS   HA   H  N N 226 
HIS   HB2  H  N N 227 
HIS   HB3  H  N N 228 
HIS   HD1  H  N N 229 
HIS   HD2  H  N N 230 
HIS   HE1  H  N N 231 
HIS   HE2  H  N N 232 
HIS   HXT  H  N N 233 
HOH   O    O  N N 234 
HOH   H1   H  N N 235 
HOH   H2   H  N N 236 
ILE   N    N  N N 237 
ILE   CA   C  N S 238 
ILE   C    C  N N 239 
ILE   O    O  N N 240 
ILE   CB   C  N S 241 
ILE   CG1  C  N N 242 
ILE   CG2  C  N N 243 
ILE   CD1  C  N N 244 
ILE   OXT  O  N N 245 
ILE   H    H  N N 246 
ILE   H2   H  N N 247 
ILE   HA   H  N N 248 
ILE   HB   H  N N 249 
ILE   HG12 H  N N 250 
ILE   HG13 H  N N 251 
ILE   HG21 H  N N 252 
ILE   HG22 H  N N 253 
ILE   HG23 H  N N 254 
ILE   HD11 H  N N 255 
ILE   HD12 H  N N 256 
ILE   HD13 H  N N 257 
ILE   HXT  H  N N 258 
LEU   N    N  N N 259 
LEU   CA   C  N S 260 
LEU   C    C  N N 261 
LEU   O    O  N N 262 
LEU   CB   C  N N 263 
LEU   CG   C  N N 264 
LEU   CD1  C  N N 265 
LEU   CD2  C  N N 266 
LEU   OXT  O  N N 267 
LEU   H    H  N N 268 
LEU   H2   H  N N 269 
LEU   HA   H  N N 270 
LEU   HB2  H  N N 271 
LEU   HB3  H  N N 272 
LEU   HG   H  N N 273 
LEU   HD11 H  N N 274 
LEU   HD12 H  N N 275 
LEU   HD13 H  N N 276 
LEU   HD21 H  N N 277 
LEU   HD22 H  N N 278 
LEU   HD23 H  N N 279 
LEU   HXT  H  N N 280 
LYS   N    N  N N 281 
LYS   CA   C  N S 282 
LYS   C    C  N N 283 
LYS   O    O  N N 284 
LYS   CB   C  N N 285 
LYS   CG   C  N N 286 
LYS   CD   C  N N 287 
LYS   CE   C  N N 288 
LYS   NZ   N  N N 289 
LYS   OXT  O  N N 290 
LYS   H    H  N N 291 
LYS   H2   H  N N 292 
LYS   HA   H  N N 293 
LYS   HB2  H  N N 294 
LYS   HB3  H  N N 295 
LYS   HG2  H  N N 296 
LYS   HG3  H  N N 297 
LYS   HD2  H  N N 298 
LYS   HD3  H  N N 299 
LYS   HE2  H  N N 300 
LYS   HE3  H  N N 301 
LYS   HZ1  H  N N 302 
LYS   HZ2  H  N N 303 
LYS   HZ3  H  N N 304 
LYS   HXT  H  N N 305 
MET   N    N  N N 306 
MET   CA   C  N S 307 
MET   C    C  N N 308 
MET   O    O  N N 309 
MET   CB   C  N N 310 
MET   CG   C  N N 311 
MET   SD   S  N N 312 
MET   CE   C  N N 313 
MET   OXT  O  N N 314 
MET   H    H  N N 315 
MET   H2   H  N N 316 
MET   HA   H  N N 317 
MET   HB2  H  N N 318 
MET   HB3  H  N N 319 
MET   HG2  H  N N 320 
MET   HG3  H  N N 321 
MET   HE1  H  N N 322 
MET   HE2  H  N N 323 
MET   HE3  H  N N 324 
MET   HXT  H  N N 325 
NAG   C1   C  N R 326 
NAG   C2   C  N R 327 
NAG   C3   C  N R 328 
NAG   C4   C  N S 329 
NAG   C5   C  N R 330 
NAG   C6   C  N N 331 
NAG   C7   C  N N 332 
NAG   C8   C  N N 333 
NAG   N2   N  N N 334 
NAG   O1   O  N N 335 
NAG   O3   O  N N 336 
NAG   O4   O  N N 337 
NAG   O5   O  N N 338 
NAG   O6   O  N N 339 
NAG   O7   O  N N 340 
NAG   H1   H  N N 341 
NAG   H2   H  N N 342 
NAG   H3   H  N N 343 
NAG   H4   H  N N 344 
NAG   H5   H  N N 345 
NAG   H61  H  N N 346 
NAG   H62  H  N N 347 
NAG   H81  H  N N 348 
NAG   H82  H  N N 349 
NAG   H83  H  N N 350 
NAG   HN2  H  N N 351 
NAG   HO1  H  N N 352 
NAG   HO3  H  N N 353 
NAG   HO4  H  N N 354 
NAG   HO6  H  N N 355 
PHE   N    N  N N 356 
PHE   CA   C  N S 357 
PHE   C    C  N N 358 
PHE   O    O  N N 359 
PHE   CB   C  N N 360 
PHE   CG   C  Y N 361 
PHE   CD1  C  Y N 362 
PHE   CD2  C  Y N 363 
PHE   CE1  C  Y N 364 
PHE   CE2  C  Y N 365 
PHE   CZ   C  Y N 366 
PHE   OXT  O  N N 367 
PHE   H    H  N N 368 
PHE   H2   H  N N 369 
PHE   HA   H  N N 370 
PHE   HB2  H  N N 371 
PHE   HB3  H  N N 372 
PHE   HD1  H  N N 373 
PHE   HD2  H  N N 374 
PHE   HE1  H  N N 375 
PHE   HE2  H  N N 376 
PHE   HZ   H  N N 377 
PHE   HXT  H  N N 378 
PRO   N    N  N N 379 
PRO   CA   C  N S 380 
PRO   C    C  N N 381 
PRO   O    O  N N 382 
PRO   CB   C  N N 383 
PRO   CG   C  N N 384 
PRO   CD   C  N N 385 
PRO   OXT  O  N N 386 
PRO   H    H  N N 387 
PRO   HA   H  N N 388 
PRO   HB2  H  N N 389 
PRO   HB3  H  N N 390 
PRO   HG2  H  N N 391 
PRO   HG3  H  N N 392 
PRO   HD2  H  N N 393 
PRO   HD3  H  N N 394 
PRO   HXT  H  N N 395 
SER   N    N  N N 396 
SER   CA   C  N S 397 
SER   C    C  N N 398 
SER   O    O  N N 399 
SER   CB   C  N N 400 
SER   OG   O  N N 401 
SER   OXT  O  N N 402 
SER   H    H  N N 403 
SER   H2   H  N N 404 
SER   HA   H  N N 405 
SER   HB2  H  N N 406 
SER   HB3  H  N N 407 
SER   HG   H  N N 408 
SER   HXT  H  N N 409 
THR   N    N  N N 410 
THR   CA   C  N S 411 
THR   C    C  N N 412 
THR   O    O  N N 413 
THR   CB   C  N R 414 
THR   OG1  O  N N 415 
THR   CG2  C  N N 416 
THR   OXT  O  N N 417 
THR   H    H  N N 418 
THR   H2   H  N N 419 
THR   HA   H  N N 420 
THR   HB   H  N N 421 
THR   HG1  H  N N 422 
THR   HG21 H  N N 423 
THR   HG22 H  N N 424 
THR   HG23 H  N N 425 
THR   HXT  H  N N 426 
TRP   N    N  N N 427 
TRP   CA   C  N S 428 
TRP   C    C  N N 429 
TRP   O    O  N N 430 
TRP   CB   C  N N 431 
TRP   CG   C  Y N 432 
TRP   CD1  C  Y N 433 
TRP   CD2  C  Y N 434 
TRP   NE1  N  Y N 435 
TRP   CE2  C  Y N 436 
TRP   CE3  C  Y N 437 
TRP   CZ2  C  Y N 438 
TRP   CZ3  C  Y N 439 
TRP   CH2  C  Y N 440 
TRP   OXT  O  N N 441 
TRP   H    H  N N 442 
TRP   H2   H  N N 443 
TRP   HA   H  N N 444 
TRP   HB2  H  N N 445 
TRP   HB3  H  N N 446 
TRP   HD1  H  N N 447 
TRP   HE1  H  N N 448 
TRP   HE3  H  N N 449 
TRP   HZ2  H  N N 450 
TRP   HZ3  H  N N 451 
TRP   HH2  H  N N 452 
TRP   HXT  H  N N 453 
TYR   N    N  N N 454 
TYR   CA   C  N S 455 
TYR   C    C  N N 456 
TYR   O    O  N N 457 
TYR   CB   C  N N 458 
TYR   CG   C  Y N 459 
TYR   CD1  C  Y N 460 
TYR   CD2  C  Y N 461 
TYR   CE1  C  Y N 462 
TYR   CE2  C  Y N 463 
TYR   CZ   C  Y N 464 
TYR   OH   O  N N 465 
TYR   OXT  O  N N 466 
TYR   H    H  N N 467 
TYR   H2   H  N N 468 
TYR   HA   H  N N 469 
TYR   HB2  H  N N 470 
TYR   HB3  H  N N 471 
TYR   HD1  H  N N 472 
TYR   HD2  H  N N 473 
TYR   HE1  H  N N 474 
TYR   HE2  H  N N 475 
TYR   HH   H  N N 476 
TYR   HXT  H  N N 477 
VAL   N    N  N N 478 
VAL   CA   C  N S 479 
VAL   C    C  N N 480 
VAL   O    O  N N 481 
VAL   CB   C  N N 482 
VAL   CG1  C  N N 483 
VAL   CG2  C  N N 484 
VAL   OXT  O  N N 485 
VAL   H    H  N N 486 
VAL   H2   H  N N 487 
VAL   HA   H  N N 488 
VAL   HB   H  N N 489 
VAL   HG11 H  N N 490 
VAL   HG12 H  N N 491 
VAL   HG13 H  N N 492 
VAL   HG21 H  N N 493 
VAL   HG22 H  N N 494 
VAL   HG23 H  N N 495 
VAL   HXT  H  N N 496 
# 
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 
A1AS5 CL1 C17  sing N N 1   
A1AS5 C19 C17  doub Y N 2   
A1AS5 C19 C20  sing Y N 3   
A1AS5 C17 C15  sing Y N 4   
A1AS5 C20 C13  doub Y N 5   
A1AS5 C15 F16  sing N N 6   
A1AS5 C15 C14  doub Y N 7   
A1AS5 C13 C14  sing Y N 8   
A1AS5 C13 N12  sing N N 9   
A1AS5 N12 C10  sing N N 10  
A1AS5 C10 O11  doub N N 11  
A1AS5 C10 C09  sing N N 12  
A1AS5 C09 C21  sing N N 13  
A1AS5 C09 C08  sing N N 14  
A1AS5 C21 C22  sing N N 15  
A1AS5 C08 N07  sing N N 16  
A1AS5 C22 C23  sing N N 17  
A1AS5 N07 C23  sing N N 18  
A1AS5 N07 C06  sing N N 19  
A1AS5 CD  C06  sing N N 20  
A1AS5 CD  NE   sing N N 21  
A1AS5 C06 O24  doub N N 22  
A1AS5 NE  CZ   sing N N 23  
A1AS5 NH2 CZ   doub N N 24  
A1AS5 CZ  NH1  sing N N 25  
A1AS5 CD  H1   sing N N 26  
A1AS5 CD  H2   sing N N 27  
A1AS5 NE  H3   sing N N 28  
A1AS5 NH1 H4   sing N N 29  
A1AS5 NH1 H5   sing N N 30  
A1AS5 NH2 H6   sing N N 31  
A1AS5 C08 H7   sing N N 32  
A1AS5 C08 H8   sing N N 33  
A1AS5 C09 H9   sing N N 34  
A1AS5 C14 H10  sing N N 35  
A1AS5 C19 H11  sing N N 36  
A1AS5 C20 H12  sing N N 37  
A1AS5 C21 H13  sing N N 38  
A1AS5 C21 H14  sing N N 39  
A1AS5 C22 H15  sing N N 40  
A1AS5 C22 H16  sing N N 41  
A1AS5 C23 H17  sing N N 42  
A1AS5 C23 H18  sing N N 43  
A1AS5 N12 H19  sing N N 44  
ALA   N   CA   sing N N 45  
ALA   N   H    sing N N 46  
ALA   N   H2   sing N N 47  
ALA   CA  C    sing N N 48  
ALA   CA  CB   sing N N 49  
ALA   CA  HA   sing N N 50  
ALA   C   O    doub N N 51  
ALA   C   OXT  sing N N 52  
ALA   CB  HB1  sing N N 53  
ALA   CB  HB2  sing N N 54  
ALA   CB  HB3  sing N N 55  
ALA   OXT HXT  sing N N 56  
ARG   N   CA   sing N N 57  
ARG   N   H    sing N N 58  
ARG   N   H2   sing N N 59  
ARG   CA  C    sing N N 60  
ARG   CA  CB   sing N N 61  
ARG   CA  HA   sing N N 62  
ARG   C   O    doub N N 63  
ARG   C   OXT  sing N N 64  
ARG   CB  CG   sing N N 65  
ARG   CB  HB2  sing N N 66  
ARG   CB  HB3  sing N N 67  
ARG   CG  CD   sing N N 68  
ARG   CG  HG2  sing N N 69  
ARG   CG  HG3  sing N N 70  
ARG   CD  NE   sing N N 71  
ARG   CD  HD2  sing N N 72  
ARG   CD  HD3  sing N N 73  
ARG   NE  CZ   sing N N 74  
ARG   NE  HE   sing N N 75  
ARG   CZ  NH1  sing N N 76  
ARG   CZ  NH2  doub N N 77  
ARG   NH1 HH11 sing N N 78  
ARG   NH1 HH12 sing N N 79  
ARG   NH2 HH21 sing N N 80  
ARG   NH2 HH22 sing N N 81  
ARG   OXT HXT  sing N N 82  
ASN   N   CA   sing N N 83  
ASN   N   H    sing N N 84  
ASN   N   H2   sing N N 85  
ASN   CA  C    sing N N 86  
ASN   CA  CB   sing N N 87  
ASN   CA  HA   sing N N 88  
ASN   C   O    doub N N 89  
ASN   C   OXT  sing N N 90  
ASN   CB  CG   sing N N 91  
ASN   CB  HB2  sing N N 92  
ASN   CB  HB3  sing N N 93  
ASN   CG  OD1  doub N N 94  
ASN   CG  ND2  sing N N 95  
ASN   ND2 HD21 sing N N 96  
ASN   ND2 HD22 sing N N 97  
ASN   OXT HXT  sing N N 98  
ASP   N   CA   sing N N 99  
ASP   N   H    sing N N 100 
ASP   N   H2   sing N N 101 
ASP   CA  C    sing N N 102 
ASP   CA  CB   sing N N 103 
ASP   CA  HA   sing N N 104 
ASP   C   O    doub N N 105 
ASP   C   OXT  sing N N 106 
ASP   CB  CG   sing N N 107 
ASP   CB  HB2  sing N N 108 
ASP   CB  HB3  sing N N 109 
ASP   CG  OD1  doub N N 110 
ASP   CG  OD2  sing N N 111 
ASP   OD2 HD2  sing N N 112 
ASP   OXT HXT  sing N N 113 
CYS   N   CA   sing N N 114 
CYS   N   H    sing N N 115 
CYS   N   H2   sing N N 116 
CYS   CA  C    sing N N 117 
CYS   CA  CB   sing N N 118 
CYS   CA  HA   sing N N 119 
CYS   C   O    doub N N 120 
CYS   C   OXT  sing N N 121 
CYS   CB  SG   sing N N 122 
CYS   CB  HB2  sing N N 123 
CYS   CB  HB3  sing N N 124 
CYS   SG  HG   sing N N 125 
CYS   OXT HXT  sing N N 126 
EPE   N1  C2   sing N N 127 
EPE   N1  C6   sing N N 128 
EPE   N1  C9   sing N N 129 
EPE   C2  C3   sing N N 130 
EPE   C2  H21  sing N N 131 
EPE   C2  H22  sing N N 132 
EPE   C3  N4   sing N N 133 
EPE   C3  H31  sing N N 134 
EPE   C3  H32  sing N N 135 
EPE   N4  C5   sing N N 136 
EPE   N4  C7   sing N N 137 
EPE   C5  C6   sing N N 138 
EPE   C5  H51  sing N N 139 
EPE   C5  H52  sing N N 140 
EPE   C6  H61  sing N N 141 
EPE   C6  H62  sing N N 142 
EPE   C7  C8   sing N N 143 
EPE   C7  H71  sing N N 144 
EPE   C7  H72  sing N N 145 
EPE   C8  O8   sing N N 146 
EPE   C8  H81  sing N N 147 
EPE   C8  H82  sing N N 148 
EPE   O8  HO8  sing N N 149 
EPE   C9  C10  sing N N 150 
EPE   C9  H91  sing N N 151 
EPE   C9  H92  sing N N 152 
EPE   C10 S    sing N N 153 
EPE   C10 H101 sing N N 154 
EPE   C10 H102 sing N N 155 
EPE   S   O1S  doub N N 156 
EPE   S   O2S  doub N N 157 
EPE   S   O3S  sing N N 158 
EPE   O3S HOS3 sing N N 159 
GLN   N   CA   sing N N 160 
GLN   N   H    sing N N 161 
GLN   N   H2   sing N N 162 
GLN   CA  C    sing N N 163 
GLN   CA  CB   sing N N 164 
GLN   CA  HA   sing N N 165 
GLN   C   O    doub N N 166 
GLN   C   OXT  sing N N 167 
GLN   CB  CG   sing N N 168 
GLN   CB  HB2  sing N N 169 
GLN   CB  HB3  sing N N 170 
GLN   CG  CD   sing N N 171 
GLN   CG  HG2  sing N N 172 
GLN   CG  HG3  sing N N 173 
GLN   CD  OE1  doub N N 174 
GLN   CD  NE2  sing N N 175 
GLN   NE2 HE21 sing N N 176 
GLN   NE2 HE22 sing N N 177 
GLN   OXT HXT  sing N N 178 
GLU   N   CA   sing N N 179 
GLU   N   H    sing N N 180 
GLU   N   H2   sing N N 181 
GLU   CA  C    sing N N 182 
GLU   CA  CB   sing N N 183 
GLU   CA  HA   sing N N 184 
GLU   C   O    doub N N 185 
GLU   C   OXT  sing N N 186 
GLU   CB  CG   sing N N 187 
GLU   CB  HB2  sing N N 188 
GLU   CB  HB3  sing N N 189 
GLU   CG  CD   sing N N 190 
GLU   CG  HG2  sing N N 191 
GLU   CG  HG3  sing N N 192 
GLU   CD  OE1  doub N N 193 
GLU   CD  OE2  sing N N 194 
GLU   OE2 HE2  sing N N 195 
GLU   OXT HXT  sing N N 196 
GLY   N   CA   sing N N 197 
GLY   N   H    sing N N 198 
GLY   N   H2   sing N N 199 
GLY   CA  C    sing N N 200 
GLY   CA  HA2  sing N N 201 
GLY   CA  HA3  sing N N 202 
GLY   C   O    doub N N 203 
GLY   C   OXT  sing N N 204 
GLY   OXT HXT  sing N N 205 
HIS   N   CA   sing N N 206 
HIS   N   H    sing N N 207 
HIS   N   H2   sing N N 208 
HIS   CA  C    sing N N 209 
HIS   CA  CB   sing N N 210 
HIS   CA  HA   sing N N 211 
HIS   C   O    doub N N 212 
HIS   C   OXT  sing N N 213 
HIS   CB  CG   sing N N 214 
HIS   CB  HB2  sing N N 215 
HIS   CB  HB3  sing N N 216 
HIS   CG  ND1  sing Y N 217 
HIS   CG  CD2  doub Y N 218 
HIS   ND1 CE1  doub Y N 219 
HIS   ND1 HD1  sing N N 220 
HIS   CD2 NE2  sing Y N 221 
HIS   CD2 HD2  sing N N 222 
HIS   CE1 NE2  sing Y N 223 
HIS   CE1 HE1  sing N N 224 
HIS   NE2 HE2  sing N N 225 
HIS   OXT HXT  sing N N 226 
HOH   O   H1   sing N N 227 
HOH   O   H2   sing N N 228 
ILE   N   CA   sing N N 229 
ILE   N   H    sing N N 230 
ILE   N   H2   sing N N 231 
ILE   CA  C    sing N N 232 
ILE   CA  CB   sing N N 233 
ILE   CA  HA   sing N N 234 
ILE   C   O    doub N N 235 
ILE   C   OXT  sing N N 236 
ILE   CB  CG1  sing N N 237 
ILE   CB  CG2  sing N N 238 
ILE   CB  HB   sing N N 239 
ILE   CG1 CD1  sing N N 240 
ILE   CG1 HG12 sing N N 241 
ILE   CG1 HG13 sing N N 242 
ILE   CG2 HG21 sing N N 243 
ILE   CG2 HG22 sing N N 244 
ILE   CG2 HG23 sing N N 245 
ILE   CD1 HD11 sing N N 246 
ILE   CD1 HD12 sing N N 247 
ILE   CD1 HD13 sing N N 248 
ILE   OXT HXT  sing N N 249 
LEU   N   CA   sing N N 250 
LEU   N   H    sing N N 251 
LEU   N   H2   sing N N 252 
LEU   CA  C    sing N N 253 
LEU   CA  CB   sing N N 254 
LEU   CA  HA   sing N N 255 
LEU   C   O    doub N N 256 
LEU   C   OXT  sing N N 257 
LEU   CB  CG   sing N N 258 
LEU   CB  HB2  sing N N 259 
LEU   CB  HB3  sing N N 260 
LEU   CG  CD1  sing N N 261 
LEU   CG  CD2  sing N N 262 
LEU   CG  HG   sing N N 263 
LEU   CD1 HD11 sing N N 264 
LEU   CD1 HD12 sing N N 265 
LEU   CD1 HD13 sing N N 266 
LEU   CD2 HD21 sing N N 267 
LEU   CD2 HD22 sing N N 268 
LEU   CD2 HD23 sing N N 269 
LEU   OXT HXT  sing N N 270 
LYS   N   CA   sing N N 271 
LYS   N   H    sing N N 272 
LYS   N   H2   sing N N 273 
LYS   CA  C    sing N N 274 
LYS   CA  CB   sing N N 275 
LYS   CA  HA   sing N N 276 
LYS   C   O    doub N N 277 
LYS   C   OXT  sing N N 278 
LYS   CB  CG   sing N N 279 
LYS   CB  HB2  sing N N 280 
LYS   CB  HB3  sing N N 281 
LYS   CG  CD   sing N N 282 
LYS   CG  HG2  sing N N 283 
LYS   CG  HG3  sing N N 284 
LYS   CD  CE   sing N N 285 
LYS   CD  HD2  sing N N 286 
LYS   CD  HD3  sing N N 287 
LYS   CE  NZ   sing N N 288 
LYS   CE  HE2  sing N N 289 
LYS   CE  HE3  sing N N 290 
LYS   NZ  HZ1  sing N N 291 
LYS   NZ  HZ2  sing N N 292 
LYS   NZ  HZ3  sing N N 293 
LYS   OXT HXT  sing N N 294 
MET   N   CA   sing N N 295 
MET   N   H    sing N N 296 
MET   N   H2   sing N N 297 
MET   CA  C    sing N N 298 
MET   CA  CB   sing N N 299 
MET   CA  HA   sing N N 300 
MET   C   O    doub N N 301 
MET   C   OXT  sing N N 302 
MET   CB  CG   sing N N 303 
MET   CB  HB2  sing N N 304 
MET   CB  HB3  sing N N 305 
MET   CG  SD   sing N N 306 
MET   CG  HG2  sing N N 307 
MET   CG  HG3  sing N N 308 
MET   SD  CE   sing N N 309 
MET   CE  HE1  sing N N 310 
MET   CE  HE2  sing N N 311 
MET   CE  HE3  sing N N 312 
MET   OXT HXT  sing N N 313 
NAG   C1  C2   sing N N 314 
NAG   C1  O1   sing N N 315 
NAG   C1  O5   sing N N 316 
NAG   C1  H1   sing N N 317 
NAG   C2  C3   sing N N 318 
NAG   C2  N2   sing N N 319 
NAG   C2  H2   sing N N 320 
NAG   C3  C4   sing N N 321 
NAG   C3  O3   sing N N 322 
NAG   C3  H3   sing N N 323 
NAG   C4  C5   sing N N 324 
NAG   C4  O4   sing N N 325 
NAG   C4  H4   sing N N 326 
NAG   C5  C6   sing N N 327 
NAG   C5  O5   sing N N 328 
NAG   C5  H5   sing N N 329 
NAG   C6  O6   sing N N 330 
NAG   C6  H61  sing N N 331 
NAG   C6  H62  sing N N 332 
NAG   C7  C8   sing N N 333 
NAG   C7  N2   sing N N 334 
NAG   C7  O7   doub N N 335 
NAG   C8  H81  sing N N 336 
NAG   C8  H82  sing N N 337 
NAG   C8  H83  sing N N 338 
NAG   N2  HN2  sing N N 339 
NAG   O1  HO1  sing N N 340 
NAG   O3  HO3  sing N N 341 
NAG   O4  HO4  sing N N 342 
NAG   O6  HO6  sing N N 343 
PHE   N   CA   sing N N 344 
PHE   N   H    sing N N 345 
PHE   N   H2   sing N N 346 
PHE   CA  C    sing N N 347 
PHE   CA  CB   sing N N 348 
PHE   CA  HA   sing N N 349 
PHE   C   O    doub N N 350 
PHE   C   OXT  sing N N 351 
PHE   CB  CG   sing N N 352 
PHE   CB  HB2  sing N N 353 
PHE   CB  HB3  sing N N 354 
PHE   CG  CD1  doub Y N 355 
PHE   CG  CD2  sing Y N 356 
PHE   CD1 CE1  sing Y N 357 
PHE   CD1 HD1  sing N N 358 
PHE   CD2 CE2  doub Y N 359 
PHE   CD2 HD2  sing N N 360 
PHE   CE1 CZ   doub Y N 361 
PHE   CE1 HE1  sing N N 362 
PHE   CE2 CZ   sing Y N 363 
PHE   CE2 HE2  sing N N 364 
PHE   CZ  HZ   sing N N 365 
PHE   OXT HXT  sing N N 366 
PRO   N   CA   sing N N 367 
PRO   N   CD   sing N N 368 
PRO   N   H    sing N N 369 
PRO   CA  C    sing N N 370 
PRO   CA  CB   sing N N 371 
PRO   CA  HA   sing N N 372 
PRO   C   O    doub N N 373 
PRO   C   OXT  sing N N 374 
PRO   CB  CG   sing N N 375 
PRO   CB  HB2  sing N N 376 
PRO   CB  HB3  sing N N 377 
PRO   CG  CD   sing N N 378 
PRO   CG  HG2  sing N N 379 
PRO   CG  HG3  sing N N 380 
PRO   CD  HD2  sing N N 381 
PRO   CD  HD3  sing N N 382 
PRO   OXT HXT  sing N N 383 
SER   N   CA   sing N N 384 
SER   N   H    sing N N 385 
SER   N   H2   sing N N 386 
SER   CA  C    sing N N 387 
SER   CA  CB   sing N N 388 
SER   CA  HA   sing N N 389 
SER   C   O    doub N N 390 
SER   C   OXT  sing N N 391 
SER   CB  OG   sing N N 392 
SER   CB  HB2  sing N N 393 
SER   CB  HB3  sing N N 394 
SER   OG  HG   sing N N 395 
SER   OXT HXT  sing N N 396 
THR   N   CA   sing N N 397 
THR   N   H    sing N N 398 
THR   N   H2   sing N N 399 
THR   CA  C    sing N N 400 
THR   CA  CB   sing N N 401 
THR   CA  HA   sing N N 402 
THR   C   O    doub N N 403 
THR   C   OXT  sing N N 404 
THR   CB  OG1  sing N N 405 
THR   CB  CG2  sing N N 406 
THR   CB  HB   sing N N 407 
THR   OG1 HG1  sing N N 408 
THR   CG2 HG21 sing N N 409 
THR   CG2 HG22 sing N N 410 
THR   CG2 HG23 sing N N 411 
THR   OXT HXT  sing N N 412 
TRP   N   CA   sing N N 413 
TRP   N   H    sing N N 414 
TRP   N   H2   sing N N 415 
TRP   CA  C    sing N N 416 
TRP   CA  CB   sing N N 417 
TRP   CA  HA   sing N N 418 
TRP   C   O    doub N N 419 
TRP   C   OXT  sing N N 420 
TRP   CB  CG   sing N N 421 
TRP   CB  HB2  sing N N 422 
TRP   CB  HB3  sing N N 423 
TRP   CG  CD1  doub Y N 424 
TRP   CG  CD2  sing Y N 425 
TRP   CD1 NE1  sing Y N 426 
TRP   CD1 HD1  sing N N 427 
TRP   CD2 CE2  doub Y N 428 
TRP   CD2 CE3  sing Y N 429 
TRP   NE1 CE2  sing Y N 430 
TRP   NE1 HE1  sing N N 431 
TRP   CE2 CZ2  sing Y N 432 
TRP   CE3 CZ3  doub Y N 433 
TRP   CE3 HE3  sing N N 434 
TRP   CZ2 CH2  doub Y N 435 
TRP   CZ2 HZ2  sing N N 436 
TRP   CZ3 CH2  sing Y N 437 
TRP   CZ3 HZ3  sing N N 438 
TRP   CH2 HH2  sing N N 439 
TRP   OXT HXT  sing N N 440 
TYR   N   CA   sing N N 441 
TYR   N   H    sing N N 442 
TYR   N   H2   sing N N 443 
TYR   CA  C    sing N N 444 
TYR   CA  CB   sing N N 445 
TYR   CA  HA   sing N N 446 
TYR   C   O    doub N N 447 
TYR   C   OXT  sing N N 448 
TYR   CB  CG   sing N N 449 
TYR   CB  HB2  sing N N 450 
TYR   CB  HB3  sing N N 451 
TYR   CG  CD1  doub Y N 452 
TYR   CG  CD2  sing Y N 453 
TYR   CD1 CE1  sing Y N 454 
TYR   CD1 HD1  sing N N 455 
TYR   CD2 CE2  doub Y N 456 
TYR   CD2 HD2  sing N N 457 
TYR   CE1 CZ   doub Y N 458 
TYR   CE1 HE1  sing N N 459 
TYR   CE2 CZ   sing Y N 460 
TYR   CE2 HE2  sing N N 461 
TYR   CZ  OH   sing N N 462 
TYR   OH  HH   sing N N 463 
TYR   OXT HXT  sing N N 464 
VAL   N   CA   sing N N 465 
VAL   N   H    sing N N 466 
VAL   N   H2   sing N N 467 
VAL   CA  C    sing N N 468 
VAL   CA  CB   sing N N 469 
VAL   CA  HA   sing N N 470 
VAL   C   O    doub N N 471 
VAL   C   OXT  sing N N 472 
VAL   CB  CG1  sing N N 473 
VAL   CB  CG2  sing N N 474 
VAL   CB  HB   sing N N 475 
VAL   CG1 HG11 sing N N 476 
VAL   CG1 HG12 sing N N 477 
VAL   CG1 HG13 sing N N 478 
VAL   CG2 HG21 sing N N 479 
VAL   CG2 HG22 sing N N 480 
VAL   CG2 HG23 sing N N 481 
VAL   OXT HXT  sing N N 482 
# 
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                    9BXB 
_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]   0.017910 
_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]   0.015297 
_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]   0.011898 
_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   . VAL   A 1 3   ? -23.523 -15.561 1.772   1.00 84.28  ? 44  VAL   A N   1 
ATOM   2    C  CA  . VAL   A 1 3   ? -23.571 -14.562 2.834   1.00 80.09  ? 44  VAL   A CA  1 
ATOM   3    C  C   . VAL   A 1 3   ? -22.190 -13.919 3.065   1.00 78.79  ? 44  VAL   A C   1 
ATOM   4    O  O   . VAL   A 1 3   ? -21.316 -14.468 3.739   1.00 77.23  ? 44  VAL   A O   1 
ATOM   5    C  CB  . VAL   A 1 3   ? -24.145 -15.176 4.111   1.00 71.51  ? 44  VAL   A CB  1 
ATOM   6    C  CG1 . VAL   A 1 3   ? -24.642 -14.081 5.034   1.00 72.00  ? 44  VAL   A CG1 1 
ATOM   7    C  CG2 . VAL   A 1 3   ? -25.304 -16.121 3.762   1.00 66.38  ? 44  VAL   A CG2 1 
ATOM   8    N  N   . TRP   A 1 4   ? -22.046 -12.711 2.520   1.00 81.90  ? 45  TRP   A N   1 
ATOM   9    C  CA  . TRP   A 1 4   ? -20.761 -12.094 2.197   1.00 79.12  ? 45  TRP   A CA  1 
ATOM   10   C  C   . TRP   A 1 4   ? -19.951 -11.518 3.356   1.00 79.12  ? 45  TRP   A C   1 
ATOM   11   O  O   . TRP   A 1 4   ? -20.159 -11.866 4.526   1.00 80.49  ? 45  TRP   A O   1 
ATOM   12   C  CB  . TRP   A 1 4   ? -21.011 -11.007 1.149   1.00 73.43  ? 45  TRP   A CB  1 
ATOM   13   C  CG  . TRP   A 1 4   ? -22.016 -10.010 1.603   1.00 75.93  ? 45  TRP   A CG  1 
ATOM   14   C  CD1 . TRP   A 1 4   ? -21.778 -8.823  2.228   1.00 74.08  ? 45  TRP   A CD1 1 
ATOM   15   C  CD2 . TRP   A 1 4   ? -23.441 -10.116 1.465   1.00 76.55  ? 45  TRP   A CD2 1 
ATOM   16   N  NE1 . TRP   A 1 4   ? -22.966 -8.183  2.494   1.00 73.32  ? 45  TRP   A NE1 1 
ATOM   17   C  CE2 . TRP   A 1 4   ? -24.001 -8.955  2.034   1.00 74.60  ? 45  TRP   A CE2 1 
ATOM   18   C  CE3 . TRP   A 1 4   ? -24.297 -11.080 0.917   1.00 79.64  ? 45  TRP   A CE3 1 
ATOM   19   C  CZ2 . TRP   A 1 4   ? -25.378 -8.729  2.072   1.00 72.75  ? 45  TRP   A CZ2 1 
ATOM   20   C  CZ3 . TRP   A 1 4   ? -25.664 -10.853 0.954   1.00 78.32  ? 45  TRP   A CZ3 1 
ATOM   21   C  CH2 . TRP   A 1 4   ? -26.190 -9.686  1.528   1.00 75.51  ? 45  TRP   A CH2 1 
ATOM   22   N  N   . LYS   A 1 5   ? -18.993 -10.659 3.005   1.00 75.43  ? 46  LYS   A N   1 
ATOM   23   C  CA  . LYS   A 1 5   ? -18.039 -10.038 3.913   1.00 79.02  ? 46  LYS   A CA  1 
ATOM   24   C  C   . LYS   A 1 5   ? -17.216 -9.035  3.115   1.00 73.02  ? 46  LYS   A C   1 
ATOM   25   O  O   . LYS   A 1 5   ? -16.767 -9.335  2.005   1.00 68.03  ? 46  LYS   A O   1 
ATOM   26   C  CB  . LYS   A 1 5   ? -17.119 -11.079 4.571   1.00 79.74  ? 46  LYS   A CB  1 
ATOM   27   C  CG  . LYS   A 1 5   ? -15.990 -10.486 5.418   1.00 78.89  ? 46  LYS   A CG  1 
ATOM   28   C  CD  . LYS   A 1 5   ? -15.839 -11.242 6.747   1.00 79.34  ? 46  LYS   A CD  1 
ATOM   29   C  CE  . LYS   A 1 5   ? -14.814 -10.592 7.700   1.00 76.55  ? 46  LYS   A CE  1 
ATOM   30   N  NZ  . LYS   A 1 5   ? -15.394 -9.596  8.659   1.00 71.78  ? 46  LYS   A NZ  1 
ATOM   31   N  N   . ASP   A 1 6   ? -17.029 -7.848  3.682   1.00 75.24  ? 47  ASP   A N   1 
ATOM   32   C  CA  . ASP   A 1 6   ? -16.288 -6.807  2.984   1.00 70.93  ? 47  ASP   A CA  1 
ATOM   33   C  C   . ASP   A 1 6   ? -14.857 -7.244  2.687   1.00 71.01  ? 47  ASP   A C   1 
ATOM   34   O  O   . ASP   A 1 6   ? -14.045 -7.420  3.607   1.00 74.90  ? 47  ASP   A O   1 
ATOM   35   C  CB  . ASP   A 1 6   ? -16.304 -5.511  3.794   1.00 72.41  ? 47  ASP   A CB  1 
ATOM   36   C  CG  . ASP   A 1 6   ? -17.582 -4.699  3.584   1.00 67.64  ? 47  ASP   A CG  1 
ATOM   37   O  OD1 . ASP   A 1 6   ? -18.424 -5.086  2.741   1.00 65.85  ? 47  ASP   A OD1 1 
ATOM   38   O  OD2 . ASP   A 1 6   ? -17.737 -3.666  4.272   1.00 64.42  ? 47  ASP   A OD2 1 
ATOM   39   N  N   . ALA   A 1 7   ? -14.551 -7.425  1.399   1.00 66.96  ? 48  ALA   A N   1 
ATOM   40   C  CA  . ALA   A 1 7   ? -13.251 -7.903  0.952   1.00 65.25  ? 48  ALA   A CA  1 
ATOM   41   C  C   . ALA   A 1 7   ? -12.778 -7.125  -0.270  1.00 62.68  ? 48  ALA   A C   1 
ATOM   42   O  O   . ALA   A 1 7   ? -13.530 -6.372  -0.894  1.00 60.63  ? 48  ALA   A O   1 
ATOM   43   C  CB  . ALA   A 1 7   ? -13.292 -9.403  0.621   1.00 65.45  ? 48  ALA   A CB  1 
ATOM   44   N  N   . ASP   A 1 8   ? -11.520 -7.368  -0.639  1.00 62.50  ? 49  ASP   A N   1 
ATOM   45   C  CA  . ASP   A 1 8   ? -10.884 -6.740  -1.796  1.00 63.46  ? 49  ASP   A CA  1 
ATOM   46   C  C   . ASP   A 1 8   ? -10.318 -7.846  -2.678  1.00 63.28  ? 49  ASP   A C   1 
ATOM   47   O  O   . ASP   A 1 8   ? -9.303  -8.457  -2.329  1.00 65.24  ? 49  ASP   A O   1 
ATOM   48   C  CB  . ASP   A 1 8   ? -9.763  -5.772  -1.381  1.00 60.42  ? 49  ASP   A CB  1 
ATOM   49   C  CG  . ASP   A 1 8   ? -10.218 -4.711  -0.387  1.00 64.33  ? 49  ASP   A CG  1 
ATOM   50   O  OD1 . ASP   A 1 8   ? -11.423 -4.668  -0.063  1.00 63.74  ? 49  ASP   A OD1 1 
ATOM   51   O  OD2 . ASP   A 1 8   ? -9.369  -3.887  0.034   1.00 64.93  ? 49  ASP   A OD2 1 
ATOM   52   N  N   . THR   A 1 9   ? -10.965 -8.120  -3.808  1.00 58.89  ? 50  THR   A N   1 
ATOM   53   C  CA  . THR   A 1 9   ? -10.412 -9.055  -4.778  1.00 58.52  ? 50  THR   A CA  1 
ATOM   54   C  C   . THR   A 1 9   ? -9.907  -8.303  -5.999  1.00 56.02  ? 50  THR   A C   1 
ATOM   55   O  O   . THR   A 1 9   ? -10.490 -7.296  -6.410  1.00 53.95  ? 50  THR   A O   1 
ATOM   56   C  CB  . THR   A 1 9   ? -11.428 -10.105 -5.228  1.00 57.30  ? 50  THR   A CB  1 
ATOM   57   O  OG1 . THR   A 1 9   ? -10.717 -11.250 -5.721  1.00 57.72  ? 50  THR   A OG1 1 
ATOM   58   C  CG2 . THR   A 1 9   ? -12.303 -9.559  -6.347  1.00 50.77  ? 50  THR   A CG2 1 
ATOM   59   N  N   . THR   A 1 10  ? -8.793  -8.774  -6.553  1.00 56.55  ? 51  THR   A N   1 
ATOM   60   C  CA  . THR   A 1 10  ? -8.330  -8.234  -7.826  1.00 51.65  ? 51  THR   A CA  1 
ATOM   61   C  C   . THR   A 1 10  ? -9.411  -8.413  -8.879  1.00 48.13  ? 51  THR   A C   1 
ATOM   62   O  O   . THR   A 1 10  ? -9.921  -9.517  -9.081  1.00 51.04  ? 51  THR   A O   1 
ATOM   63   C  CB  . THR   A 1 10  ? -7.050  -8.923  -8.285  1.00 50.79  ? 51  THR   A CB  1 
ATOM   64   O  OG1 . THR   A 1 10  ? -6.027  -8.740  -7.303  1.00 55.75  ? 51  THR   A OG1 1 
ATOM   65   C  CG2 . THR   A 1 10  ? -6.593  -8.329  -9.593  1.00 48.79  ? 51  THR   A CG2 1 
ATOM   66   N  N   . LEU   A 1 11  ? -9.762  -7.323  -9.545  1.00 47.34  ? 52  LEU   A N   1 
ATOM   67   C  CA  . LEU   A 1 11  ? -10.877 -7.346  -10.467 1.00 42.68  ? 52  LEU   A CA  1 
ATOM   68   C  C   . LEU   A 1 11  ? -10.388 -7.709  -11.866 1.00 40.15  ? 52  LEU   A C   1 
ATOM   69   O  O   . LEU   A 1 11  ? -9.205  -7.962  -12.103 1.00 35.67  ? 52  LEU   A O   1 
ATOM   70   C  CB  . LEU   A 1 11  ? -11.590 -5.993  -10.471 1.00 41.43  ? 52  LEU   A CB  1 
ATOM   71   C  CG  . LEU   A 1 11  ? -12.403 -5.564  -9.251  1.00 41.15  ? 52  LEU   A CG  1 
ATOM   72   C  CD1 . LEU   A 1 11  ? -12.812 -4.100  -9.383  1.00 40.28  ? 52  LEU   A CD1 1 
ATOM   73   C  CD2 . LEU   A 1 11  ? -13.625 -6.456  -9.106  1.00 42.97  ? 52  LEU   A CD2 1 
ATOM   74   N  N   . PHE   A 1 12  ? -11.322 -7.736  -12.808 1.00 37.88  ? 53  PHE   A N   1 
ATOM   75   C  CA  . PHE   A 1 12  ? -10.982 -7.893  -14.211 1.00 40.03  ? 53  PHE   A CA  1 
ATOM   76   C  C   . PHE   A 1 12  ? -11.931 -7.013  -15.009 1.00 38.29  ? 53  PHE   A C   1 
ATOM   77   O  O   . PHE   A 1 12  ? -12.974 -6.594  -14.508 1.00 35.89  ? 53  PHE   A O   1 
ATOM   78   C  CB  . PHE   A 1 12  ? -11.017 -9.383  -14.646 1.00 36.74  ? 53  PHE   A CB  1 
ATOM   79   C  CG  . PHE   A 1 12  ? -12.395 -9.943  -14.836 1.00 40.28  ? 53  PHE   A CG  1 
ATOM   80   C  CD1 . PHE   A 1 12  ? -13.070 -9.779  -16.031 1.00 41.69  ? 53  PHE   A CD1 1 
ATOM   81   C  CD2 . PHE   A 1 12  ? -13.013 -10.648 -13.817 1.00 42.15  ? 53  PHE   A CD2 1 
ATOM   82   C  CE1 . PHE   A 1 12  ? -14.328 -10.293 -16.206 1.00 41.13  ? 53  PHE   A CE1 1 
ATOM   83   C  CE2 . PHE   A 1 12  ? -14.288 -11.166 -13.984 1.00 40.97  ? 53  PHE   A CE2 1 
ATOM   84   C  CZ  . PHE   A 1 12  ? -14.941 -10.990 -15.181 1.00 43.05  ? 53  PHE   A CZ  1 
ATOM   85   N  N   . CYS   A 1 13  ? -11.545 -6.673  -16.229 1.00 37.84  ? 54  CYS   A N   1 
ATOM   86   C  CA  . CYS   A 1 13  ? -12.332 -5.718  -16.992 1.00 39.11  ? 54  CYS   A CA  1 
ATOM   87   C  C   . CYS   A 1 13  ? -12.895 -6.370  -18.242 1.00 39.39  ? 54  CYS   A C   1 
ATOM   88   O  O   . CYS   A 1 13  ? -12.335 -7.325  -18.785 1.00 40.79  ? 54  CYS   A O   1 
ATOM   89   C  CB  . CYS   A 1 13  ? -11.523 -4.453  -17.363 1.00 32.43  ? 54  CYS   A CB  1 
ATOM   90   S  SG  . CYS   A 1 13  ? -10.021 -4.726  -18.379 1.00 31.16  ? 54  CYS   A SG  1 
ATOM   91   N  N   . ALA   A 1 14  ? -14.018 -5.828  -18.690 1.00 42.00  ? 55  ALA   A N   1 
ATOM   92   C  CA  . ALA   A 1 14  ? -14.640 -6.236  -19.931 1.00 38.72  ? 55  ALA   A CA  1 
ATOM   93   C  C   . ALA   A 1 14  ? -15.110 -4.982  -20.642 1.00 40.14  ? 55  ALA   A C   1 
ATOM   94   O  O   . ALA   A 1 14  ? -15.498 -4.000  -20.002 1.00 39.77  ? 55  ALA   A O   1 
ATOM   95   C  CB  . ALA   A 1 14  ? -15.817 -7.182  -19.697 1.00 43.84  ? 55  ALA   A CB  1 
ATOM   96   N  N   . SER   A 1 15  ? -15.078 -5.027  -21.969 1.00 39.07  ? 56  SER   A N   1 
ATOM   97   C  CA  . SER   A 1 15  ? -15.515 -3.900  -22.773 1.00 41.59  ? 56  SER   A CA  1 
ATOM   98   C  C   . SER   A 1 15  ? -15.827 -4.411  -24.167 1.00 44.75  ? 56  SER   A C   1 
ATOM   99   O  O   . SER   A 1 15  ? -15.443 -5.515  -24.556 1.00 50.32  ? 56  SER   A O   1 
ATOM   100  C  CB  . SER   A 1 15  ? -14.467 -2.773  -22.830 1.00 39.80  ? 56  SER   A CB  1 
ATOM   101  O  OG  . SER   A 1 15  ? -13.383 -3.104  -23.679 1.00 41.19  ? 56  SER   A OG  1 
ATOM   102  N  N   . ASP   A 1 16  ? -16.521 -3.576  -24.918 1.00 46.63  ? 57  ASP   A N   1 
ATOM   103  C  CA  . ASP   A 1 16  ? -16.829 -3.865  -26.310 1.00 46.60  ? 57  ASP   A CA  1 
ATOM   104  C  C   . ASP   A 1 16  ? -15.780 -3.253  -27.228 1.00 43.86  ? 57  ASP   A C   1 
ATOM   105  O  O   . ASP   A 1 16  ? -16.098 -2.659  -28.250 1.00 44.22  ? 57  ASP   A O   1 
ATOM   106  C  CB  . ASP   A 1 16  ? -18.236 -3.371  -26.639 1.00 49.67  ? 57  ASP   A CB  1 
ATOM   107  C  CG  . ASP   A 1 16  ? -19.326 -4.233  -25.979 1.00 53.31  ? 57  ASP   A CG  1 
ATOM   108  O  OD1 . ASP   A 1 16  ? -19.281 -5.460  -26.198 1.00 59.14  ? 57  ASP   A OD1 1 
ATOM   109  O  OD2 . ASP   A 1 16  ? -20.222 -3.717  -25.263 1.00 57.67  ? 57  ASP   A OD2 1 
ATOM   110  N  N   . ALA   A 1 17  ? -14.509 -3.374  -26.854 1.00 43.86  ? 58  ALA   A N   1 
ATOM   111  C  CA  . ALA   A 1 17  ? -13.447 -2.809  -27.670 1.00 43.90  ? 58  ALA   A CA  1 
ATOM   112  C  C   . ALA   A 1 17  ? -13.275 -3.597  -28.959 1.00 44.51  ? 58  ALA   A C   1 
ATOM   113  O  O   . ALA   A 1 17  ? -13.314 -4.832  -28.961 1.00 45.55  ? 58  ALA   A O   1 
ATOM   114  C  CB  . ALA   A 1 17  ? -12.127 -2.782  -26.900 1.00 42.58  ? 58  ALA   A CB  1 
ATOM   115  N  N   . LYS   A 1 18  ? -13.047 -2.860  -30.050 1.00 44.16  ? 59  LYS   A N   1 
ATOM   116  C  CA  . LYS   A 1 18  ? -12.804 -3.426  -31.371 1.00 45.79  ? 59  LYS   A CA  1 
ATOM   117  C  C   . LYS   A 1 18  ? -11.332 -3.801  -31.503 1.00 50.65  ? 59  LYS   A C   1 
ATOM   118  O  O   . LYS   A 1 18  ? -10.449 -2.948  -31.342 1.00 51.67  ? 59  LYS   A O   1 
ATOM   119  C  CB  . LYS   A 1 18  ? -13.181 -2.413  -32.447 1.00 47.06  ? 59  LYS   A CB  1 
ATOM   120  C  CG  . LYS   A 1 18  ? -14.663 -2.130  -32.563 1.00 47.43  ? 59  LYS   A CG  1 
ATOM   121  C  CD  . LYS   A 1 18  ? -14.939 -1.125  -33.693 1.00 57.27  ? 59  LYS   A CD  1 
ATOM   122  C  CE  . LYS   A 1 18  ? -15.512 0.192   -33.162 1.00 61.00  ? 59  LYS   A CE  1 
ATOM   123  N  NZ  . LYS   A 1 18  ? -15.950 1.156   -34.229 1.00 64.04  ? 59  LYS   A NZ  1 
ATOM   124  N  N   . ALA   A 1 19  ? -11.068 -5.077  -31.774 1.00 48.70  ? 60  ALA   A N   1 
ATOM   125  C  CA  . ALA   A 1 19  ? -9.722  -5.498  -32.127 1.00 51.79  ? 60  ALA   A CA  1 
ATOM   126  C  C   . ALA   A 1 19  ? -9.343  -4.915  -33.483 1.00 56.03  ? 60  ALA   A C   1 
ATOM   127  O  O   . ALA   A 1 19  ? -10.188 -4.710  -34.357 1.00 61.14  ? 60  ALA   A O   1 
ATOM   128  C  CB  . ALA   A 1 19  ? -9.618  -7.023  -32.171 1.00 51.74  ? 60  ALA   A CB  1 
ATOM   129  N  N   . TYR   A 1 20  ? -8.053  -4.667  -33.666 1.00 56.14  ? 61  TYR   A N   1 
ATOM   130  C  CA  . TYR   A 1 20  ? -7.529  -4.079  -34.891 1.00 56.99  ? 61  TYR   A CA  1 
ATOM   131  C  C   . TYR   A 1 20  ? -8.014  -2.657  -35.128 1.00 58.03  ? 61  TYR   A C   1 
ATOM   132  O  O   . TYR   A 1 20  ? -7.962  -2.160  -36.265 1.00 62.12  ? 61  TYR   A O   1 
ATOM   133  C  CB  . TYR   A 1 20  ? -7.841  -4.948  -36.112 1.00 57.07  ? 61  TYR   A CB  1 
ATOM   134  C  CG  . TYR   A 1 20  ? -7.569  -6.421  -35.907 1.00 56.43  ? 61  TYR   A CG  1 
ATOM   135  C  CD1 . TYR   A 1 20  ? -6.288  -6.857  -35.587 1.00 57.30  ? 61  TYR   A CD1 1 
ATOM   136  C  CD2 . TYR   A 1 20  ? -8.555  -7.378  -36.117 1.00 61.89  ? 61  TYR   A CD2 1 
ATOM   137  C  CE1 . TYR   A 1 20  ? -6.008  -8.193  -35.424 1.00 55.84  ? 61  TYR   A CE1 1 
ATOM   138  C  CE2 . TYR   A 1 20  ? -8.281  -8.724  -35.961 1.00 65.98  ? 61  TYR   A CE2 1 
ATOM   139  C  CZ  . TYR   A 1 20  ? -7.003  -9.121  -35.612 1.00 61.14  ? 61  TYR   A CZ  1 
ATOM   140  O  OH  . TYR   A 1 20  ? -6.711  -10.454 -35.451 1.00 63.52  ? 61  TYR   A OH  1 
ATOM   141  N  N   . GLU   A 1 21  ? -8.486  -1.992  -34.082 1.00 57.67  ? 62  GLU   A N   1 
ATOM   142  C  CA  . GLU   A 1 21  ? -8.762  -0.570  -34.140 1.00 52.70  ? 62  GLU   A CA  1 
ATOM   143  C  C   . GLU   A 1 21  ? -7.546  0.175   -33.621 1.00 51.24  ? 62  GLU   A C   1 
ATOM   144  O  O   . GLU   A 1 21  ? -6.823  -0.317  -32.751 1.00 48.37  ? 62  GLU   A O   1 
ATOM   145  C  CB  . GLU   A 1 21  ? -9.983  -0.208  -33.297 1.00 52.37  ? 62  GLU   A CB  1 
ATOM   146  C  CG  . GLU   A 1 21  ? -10.214 1.303   -33.158 1.00 52.28  ? 62  GLU   A CG  1 
ATOM   147  C  CD  . GLU   A 1 21  ? -10.788 1.925   -34.417 1.00 56.93  ? 62  GLU   A CD  1 
ATOM   148  O  OE1 . GLU   A 1 21  ? -11.699 1.302   -35.009 1.00 63.21  ? 62  GLU   A OE1 1 
ATOM   149  O  OE2 . GLU   A 1 21  ? -10.355 3.034   -34.795 1.00 56.86  ? 62  GLU   A OE2 1 
ATOM   150  N  N   . THR   A 1 22  ? -7.327  1.375   -34.154 1.00 52.71  ? 63  THR   A N   1 
ATOM   151  C  CA  . THR   A 1 22  ? -6.110  2.110   -33.845 1.00 47.85  ? 63  THR   A CA  1 
ATOM   152  C  C   . THR   A 1 22  ? -6.234  2.985   -32.599 1.00 43.70  ? 63  THR   A C   1 
ATOM   153  O  O   . THR   A 1 22  ? -5.214  3.462   -32.087 1.00 41.88  ? 63  THR   A O   1 
ATOM   154  C  CB  . THR   A 1 22  ? -5.711  2.954   -35.056 1.00 51.08  ? 63  THR   A CB  1 
ATOM   155  O  OG1 . THR   A 1 22  ? -4.447  3.574   -34.802 1.00 52.54  ? 63  THR   A OG1 1 
ATOM   156  C  CG2 . THR   A 1 22  ? -6.767  4.017   -35.343 1.00 51.31  ? 63  THR   A CG2 1 
ATOM   157  N  N   . GLU   A 1 23  ? -7.451  3.198   -32.098 1.00 43.64  ? 64  GLU   A N   1 
ATOM   158  C  CA  . GLU   A 1 23  ? -7.645  3.982   -30.887 1.00 40.48  ? 64  GLU   A CA  1 
ATOM   159  C  C   . GLU   A 1 23  ? -7.076  3.269   -29.668 1.00 41.63  ? 64  GLU   A C   1 
ATOM   160  O  O   . GLU   A 1 23  ? -7.337  2.084   -29.443 1.00 38.59  ? 64  GLU   A O   1 
ATOM   161  C  CB  . GLU   A 1 23  ? -9.126  4.251   -30.669 1.00 41.68  ? 64  GLU   A CB  1 
ATOM   162  C  CG  . GLU   A 1 23  ? -9.373  5.462   -29.819 1.00 38.39  ? 64  GLU   A CG  1 
ATOM   163  C  CD  . GLU   A 1 23  ? -9.510  5.097   -28.361 1.00 37.12  ? 64  GLU   A CD  1 
ATOM   164  O  OE1 . GLU   A 1 23  ? -10.088 4.027   -28.078 1.00 40.22  ? 64  GLU   A OE1 1 
ATOM   165  O  OE2 . GLU   A 1 23  ? -9.075  5.886   -27.496 1.00 39.10  ? 64  GLU   A OE2 1 
ATOM   166  N  N   . VAL   A 1 24  ? -6.324  4.018   -28.855 1.00 39.70  ? 65  VAL   A N   1 
ATOM   167  C  CA  . VAL   A 1 24  ? -5.547  3.425   -27.768 1.00 40.19  ? 65  VAL   A CA  1 
ATOM   168  C  C   . VAL   A 1 24  ? -6.436  2.765   -26.711 1.00 39.71  ? 65  VAL   A C   1 
ATOM   169  O  O   . VAL   A 1 24  ? -6.026  1.779   -26.075 1.00 38.17  ? 65  VAL   A O   1 
ATOM   170  C  CB  . VAL   A 1 24  ? -4.627  4.499   -27.154 1.00 40.80  ? 65  VAL   A CB  1 
ATOM   171  C  CG1 . VAL   A 1 24  ? -3.509  4.859   -28.130 1.00 39.34  ? 65  VAL   A CG1 1 
ATOM   172  C  CG2 . VAL   A 1 24  ? -5.444  5.770   -26.738 1.00 36.73  ? 65  VAL   A CG2 1 
ATOM   173  N  N   . HIS   A 1 25  ? -7.638  3.293   -26.472 1.00 37.04  ? 66  HIS   A N   1 
ATOM   174  C  CA  . HIS   A 1 25  ? -8.505  2.648   -25.491 1.00 37.37  ? 66  HIS   A CA  1 
ATOM   175  C  C   . HIS   A 1 25  ? -8.940  1.279   -25.981 1.00 38.83  ? 66  HIS   A C   1 
ATOM   176  O  O   . HIS   A 1 25  ? -8.991  0.320   -25.201 1.00 38.96  ? 66  HIS   A O   1 
ATOM   177  C  CB  . HIS   A 1 25  ? -9.712  3.535   -25.170 1.00 34.31  ? 66  HIS   A CB  1 
ATOM   178  C  CG  . HIS   A 1 25  ? -9.359  4.776   -24.410 1.00 35.67  ? 66  HIS   A CG  1 
ATOM   179  N  ND1 . HIS   A 1 25  ? -8.842  5.900   -25.017 1.00 36.86  ? 66  HIS   A ND1 1 
ATOM   180  C  CD2 . HIS   A 1 25  ? -9.448  5.069   -23.091 1.00 36.15  ? 66  HIS   A CD2 1 
ATOM   181  C  CE1 . HIS   A 1 25  ? -8.628  6.831   -24.105 1.00 36.31  ? 66  HIS   A CE1 1 
ATOM   182  N  NE2 . HIS   A 1 25  ? -8.987  6.353   -22.928 1.00 36.39  ? 66  HIS   A NE2 1 
ATOM   183  N  N   . ASN   A 1 26  ? -9.230  1.165   -27.280 1.00 35.95  ? 67  ASN   A N   1 
ATOM   184  C  CA  . ASN   A 1 26  ? -9.580  -0.127  -27.857 1.00 36.04  ? 67  ASN   A CA  1 
ATOM   185  C  C   . ASN   A 1 26  ? -8.386  -1.078  -27.841 1.00 39.31  ? 67  ASN   A C   1 
ATOM   186  O  O   . ASN   A 1 26  ? -8.542  -2.276  -27.567 1.00 41.26  ? 67  ASN   A O   1 
ATOM   187  C  CB  . ASN   A 1 26  ? -10.126 0.078   -29.276 1.00 38.31  ? 67  ASN   A CB  1 
ATOM   188  C  CG  . ASN   A 1 26  ? -11.569 0.599   -29.280 1.00 39.40  ? 67  ASN   A CG  1 
ATOM   189  O  OD1 . ASN   A 1 26  ? -12.538 -0.172  -29.272 1.00 36.49  ? 67  ASN   A OD1 1 
ATOM   190  N  ND2 . ASN   A 1 26  ? -11.709 1.917   -29.228 1.00 39.55  ? 67  ASN   A ND2 1 
ATOM   191  N  N   . VAL   A 1 27  ? -7.183  -0.568  -28.109 1.00 36.21  ? 68  VAL   A N   1 
ATOM   192  C  CA  . VAL   A 1 27  ? -6.018  -1.448  -28.113 1.00 38.95  ? 68  VAL   A CA  1 
ATOM   193  C  C   . VAL   A 1 27  ? -5.739  -1.968  -26.707 1.00 37.35  ? 68  VAL   A C   1 
ATOM   194  O  O   . VAL   A 1 27  ? -5.534  -3.170  -26.507 1.00 37.66  ? 68  VAL   A O   1 
ATOM   195  C  CB  . VAL   A 1 27  ? -4.800  -0.732  -28.725 1.00 38.85  ? 68  VAL   A CB  1 
ATOM   196  C  CG1 . VAL   A 1 27  ? -3.614  -1.664  -28.746 1.00 38.29  ? 68  VAL   A CG1 1 
ATOM   197  C  CG2 . VAL   A 1 27  ? -5.107  -0.289  -30.152 1.00 40.81  ? 68  VAL   A CG2 1 
ATOM   198  N  N   . TRP   A 1 28  ? -5.769  -1.088  -25.707 1.00 39.21  ? 69  TRP   A N   1 
ATOM   199  C  CA  . TRP   A 1 28  ? -5.551  -1.534  -24.338 1.00 39.52  ? 69  TRP   A CA  1 
ATOM   200  C  C   . TRP   A 1 28  ? -6.631  -2.514  -23.907 1.00 39.24  ? 69  TRP   A C   1 
ATOM   201  O  O   . TRP   A 1 28  ? -6.332  -3.565  -23.332 1.00 38.44  ? 69  TRP   A O   1 
ATOM   202  C  CB  . TRP   A 1 28  ? -5.490  -0.331  -23.400 1.00 37.57  ? 69  TRP   A CB  1 
ATOM   203  C  CG  . TRP   A 1 28  ? -5.282  -0.709  -21.973 1.00 36.14  ? 69  TRP   A CG  1 
ATOM   204  C  CD1 . TRP   A 1 28  ? -4.085  -0.877  -21.343 1.00 37.39  ? 69  TRP   A CD1 1 
ATOM   205  C  CD2 . TRP   A 1 28  ? -6.292  -0.928  -20.980 1.00 34.72  ? 69  TRP   A CD2 1 
ATOM   206  N  NE1 . TRP   A 1 28  ? -4.283  -1.217  -20.028 1.00 38.12  ? 69  TRP   A NE1 1 
ATOM   207  C  CE2 . TRP   A 1 28  ? -5.629  -1.253  -19.779 1.00 34.30  ? 69  TRP   A CE2 1 
ATOM   208  C  CE3 . TRP   A 1 28  ? -7.687  -0.891  -20.991 1.00 33.93  ? 69  TRP   A CE3 1 
ATOM   209  C  CZ2 . TRP   A 1 28  ? -6.310  -1.534  -18.607 1.00 36.01  ? 69  TRP   A CZ2 1 
ATOM   210  C  CZ3 . TRP   A 1 28  ? -8.366  -1.178  -19.828 1.00 36.84  ? 69  TRP   A CZ3 1 
ATOM   211  C  CH2 . TRP   A 1 28  ? -7.678  -1.497  -18.649 1.00 39.39  ? 69  TRP   A CH2 1 
ATOM   212  N  N   . ALA   A 1 29  ? -7.899  -2.206  -24.201 1.00 40.50  ? 70  ALA   A N   1 
ATOM   213  C  CA  . ALA   A 1 29  ? -8.979  -3.111  -23.801 1.00 41.72  ? 70  ALA   A CA  1 
ATOM   214  C  C   . ALA   A 1 29  ? -8.880  -4.461  -24.508 1.00 39.67  ? 70  ALA   A C   1 
ATOM   215  O  O   . ALA   A 1 29  ? -9.346  -5.475  -23.983 1.00 40.39  ? 70  ALA   A O   1 
ATOM   216  C  CB  . ALA   A 1 29  ? -10.342 -2.473  -24.081 1.00 37.90  ? 70  ALA   A CB  1 
ATOM   217  N  N   . THR   A 1 30  ? -8.277  -4.494  -25.697 1.00 41.19  ? 71  THR   A N   1 
ATOM   218  C  CA  . THR   A 1 30  ? -8.215  -5.723  -26.489 1.00 41.54  ? 71  THR   A CA  1 
ATOM   219  C  C   . THR   A 1 30  ? -7.226  -6.717  -25.914 1.00 40.70  ? 71  THR   A C   1 
ATOM   220  O  O   . THR   A 1 30  ? -7.466  -7.927  -25.952 1.00 41.75  ? 71  THR   A O   1 
ATOM   221  C  CB  . THR   A 1 30  ? -7.803  -5.414  -27.921 1.00 43.36  ? 71  THR   A CB  1 
ATOM   222  O  OG1 . THR   A 1 30  ? -8.909  -4.845  -28.631 1.00 40.84  ? 71  THR   A OG1 1 
ATOM   223  C  CG2 . THR   A 1 30  ? -7.323  -6.701  -28.610 1.00 42.51  ? 71  THR   A CG2 1 
ATOM   224  N  N   A HIS   A 1 31  ? -6.096  -6.224  -25.390 0.50 41.02  ? 72  HIS   A N   1 
ATOM   225  N  N   B HIS   A 1 31  ? -6.133  -6.222  -25.355 0.50 42.54  ? 72  HIS   A N   1 
ATOM   226  C  CA  A HIS   A 1 31  ? -5.084  -7.043  -24.725 0.50 41.59  ? 72  HIS   A CA  1 
ATOM   227  C  CA  B HIS   A 1 31  ? -5.112  -7.046  -24.726 0.50 42.42  ? 72  HIS   A CA  1 
ATOM   228  C  C   A HIS   A 1 31  ? -5.228  -7.038  -23.203 0.50 41.01  ? 72  HIS   A C   1 
ATOM   229  C  C   B HIS   A 1 31  ? -5.192  -7.000  -23.202 0.50 42.14  ? 72  HIS   A C   1 
ATOM   230  O  O   A HIS   A 1 31  ? -4.543  -7.810  -22.523 0.50 41.60  ? 72  HIS   A O   1 
ATOM   231  O  O   B HIS   A 1 31  ? -4.434  -7.698  -22.522 0.50 41.84  ? 72  HIS   A O   1 
ATOM   232  C  CB  A HIS   A 1 31  ? -3.666  -6.587  -25.131 0.50 36.65  ? 72  HIS   A CB  1 
ATOM   233  C  CB  B HIS   A 1 31  ? -3.723  -6.600  -25.179 0.50 38.51  ? 72  HIS   A CB  1 
ATOM   234  C  CG  A HIS   A 1 31  ? -3.068  -5.510  -24.258 0.50 40.99  ? 72  HIS   A CG  1 
ATOM   235  C  CG  B HIS   A 1 31  ? -3.546  -6.559  -26.665 0.50 40.08  ? 72  HIS   A CG  1 
ATOM   236  N  ND1 A HIS   A 1 31  ? -2.543  -5.752  -23.004 0.50 42.78  ? 72  HIS   A ND1 1 
ATOM   237  N  ND1 B HIS   A 1 31  ? -3.496  -5.372  -27.359 0.50 40.13  ? 72  HIS   A ND1 1 
ATOM   238  C  CD2 A HIS   A 1 31  ? -2.915  -4.180  -24.468 0.50 41.70  ? 72  HIS   A CD2 1 
ATOM   239  C  CD2 B HIS   A 1 31  ? -3.401  -7.539  -27.589 0.50 40.06  ? 72  HIS   A CD2 1 
ATOM   240  C  CE1 A HIS   A 1 31  ? -2.088  -4.624  -22.485 0.50 41.16  ? 72  HIS   A CE1 1 
ATOM   241  C  CE1 B HIS   A 1 31  ? -3.330  -5.618  -28.645 0.50 40.72  ? 72  HIS   A CE1 1 
ATOM   242  N  NE2 A HIS   A 1 31  ? -2.307  -3.654  -23.352 0.50 41.34  ? 72  HIS   A NE2 1 
ATOM   243  N  NE2 B HIS   A 1 31  ? -3.268  -6.926  -28.813 0.50 40.25  ? 72  HIS   A NE2 1 
ATOM   244  N  N   . ALA   A 1 32  ? -6.079  -6.192  -22.629 1.00 40.22  ? 73  ALA   A N   1 
ATOM   245  C  CA  . ALA   A 1 32  ? -6.166  -6.204  -21.166 1.00 43.42  ? 73  ALA   A CA  1 
ATOM   246  C  C   . ALA   A 1 32  ? -7.528  -6.561  -20.574 1.00 41.15  ? 73  ALA   A C   1 
ATOM   247  O  O   . ALA   A 1 32  ? -7.605  -6.753  -19.354 1.00 43.62  ? 73  ALA   A O   1 
ATOM   248  C  CB  . ALA   A 1 32  ? -5.709  -4.863  -20.584 1.00 36.05  ? 73  ALA   A CB  1 
ATOM   249  N  N   . CYS   A 1 33  ? -8.604  -6.631  -21.340 1.00 36.24  ? 74  CYS   A N   1 
ATOM   250  C  CA  . CYS   A 1 33  ? -9.895  -6.991  -20.777 1.00 42.81  ? 74  CYS   A CA  1 
ATOM   251  C  C   . CYS   A 1 33  ? -10.349 -8.326  -21.351 1.00 47.63  ? 74  CYS   A C   1 
ATOM   252  O  O   . CYS   A 1 33  ? -9.837  -8.794  -22.374 1.00 46.32  ? 74  CYS   A O   1 
ATOM   253  C  CB  . CYS   A 1 33  ? -10.938 -5.900  -21.034 1.00 42.35  ? 74  CYS   A CB  1 
ATOM   254  S  SG  . CYS   A 1 33  ? -10.514 -4.305  -20.303 1.00 37.63  ? 74  CYS   A SG  1 
ATOM   255  N  N   . VAL   A 1 34  ? -11.309 -8.943  -20.680 1.00 47.94  ? 75  VAL   A N   1 
ATOM   256  C  CA  . VAL   A 1 34  ? -11.674 -10.315 -21.023 1.00 55.66  ? 75  VAL   A CA  1 
ATOM   257  C  C   . VAL   A 1 34  ? -12.095 -10.423 -22.484 1.00 61.71  ? 75  VAL   A C   1 
ATOM   258  O  O   . VAL   A 1 34  ? -12.884 -9.596  -22.978 1.00 58.91  ? 75  VAL   A O   1 
ATOM   259  C  CB  . VAL   A 1 34  ? -12.802 -10.829 -20.127 1.00 55.43  ? 75  VAL   A CB  1 
ATOM   260  C  CG1 . VAL   A 1 34  ? -12.230 -11.276 -18.817 1.00 50.62  ? 75  VAL   A CG1 1 
ATOM   261  C  CG2 . VAL   A 1 34  ? -13.839 -9.729  -19.936 1.00 51.19  ? 75  VAL   A CG2 1 
ATOM   262  N  N   . PRO   A 1 35  ? -11.596 -11.431 -23.214 1.00 66.79  ? 76  PRO   A N   1 
ATOM   263  C  CA  . PRO   A 1 35  ? -12.231 -11.781 -24.499 1.00 71.83  ? 76  PRO   A CA  1 
ATOM   264  C  C   . PRO   A 1 35  ? -13.646 -12.267 -24.266 1.00 76.31  ? 76  PRO   A C   1 
ATOM   265  O  O   . PRO   A 1 35  ? -14.530 -11.514 -23.843 1.00 80.48  ? 76  PRO   A O   1 
ATOM   266  C  CB  . PRO   A 1 35  ? -11.344 -12.903 -25.055 1.00 73.77  ? 76  PRO   A CB  1 
ATOM   267  C  CG  . PRO   A 1 35  ? -10.137 -12.972 -24.183 1.00 68.83  ? 76  PRO   A CG  1 
ATOM   268  C  CD  . PRO   A 1 35  ? -10.275 -12.072 -23.017 1.00 63.77  ? 76  PRO   A CD  1 
ATOM   269  N  N   . THR   A 1 36  ? -13.858 -13.541 -24.566 1.00 80.02  ? 77  THR   A N   1 
ATOM   270  C  CA  . THR   A 1 36  ? -14.956 -14.274 -23.947 1.00 85.97  ? 77  THR   A CA  1 
ATOM   271  C  C   . THR   A 1 36  ? -16.331 -13.712 -24.267 1.00 88.59  ? 77  THR   A C   1 
ATOM   272  O  O   . THR   A 1 36  ? -17.214 -14.460 -24.700 1.00 86.95  ? 77  THR   A O   1 
ATOM   273  C  CB  . THR   A 1 36  ? -14.772 -14.292 -22.435 1.00 83.63  ? 77  THR   A CB  1 
ATOM   274  O  OG1 . THR   A 1 36  ? -13.424 -14.680 -22.135 1.00 78.85  ? 77  THR   A OG1 1 
ATOM   275  C  CG2 . THR   A 1 36  ? -15.738 -15.269 -21.812 1.00 88.02  ? 77  THR   A CG2 1 
ATOM   276  N  N   . ASP   A 1 37  ? -16.541 -12.415 -24.012 1.00 88.05  ? 78  ASP   A N   1 
ATOM   277  C  CA  . ASP   A 1 37  ? -17.793 -11.790 -24.417 1.00 91.15  ? 78  ASP   A CA  1 
ATOM   278  C  C   . ASP   A 1 37  ? -18.880 -12.161 -23.419 1.00 92.07  ? 78  ASP   A C   1 
ATOM   279  O  O   . ASP   A 1 37  ? -19.724 -13.016 -23.716 1.00 93.98  ? 78  ASP   A O   1 
ATOM   280  C  CB  . ASP   A 1 37  ? -18.191 -12.256 -25.818 1.00 91.07  ? 78  ASP   A CB  1 
ATOM   281  C  CG  . ASP   A 1 37  ? -19.543 -11.706 -26.259 1.00 87.87  ? 78  ASP   A CG  1 
ATOM   282  O  OD1 . ASP   A 1 37  ? -20.619 -12.159 -25.780 1.00 86.90  ? 78  ASP   A OD1 1 
ATOM   283  O  OD2 . ASP   A 1 37  ? -19.502 -10.758 -27.071 1.00 85.21  ? 78  ASP   A OD2 1 
ATOM   284  N  N   . PRO   A 1 38  ? -18.885 -11.572 -22.229 1.00 92.00  ? 79  PRO   A N   1 
ATOM   285  C  CA  . PRO   A 1 38  ? -19.577 -12.208 -21.104 1.00 91.89  ? 79  PRO   A CA  1 
ATOM   286  C  C   . PRO   A 1 38  ? -21.039 -11.791 -21.001 1.00 89.31  ? 79  PRO   A C   1 
ATOM   287  O  O   . PRO   A 1 38  ? -21.564 -10.980 -21.765 1.00 86.44  ? 79  PRO   A O   1 
ATOM   288  C  CB  . PRO   A 1 38  ? -18.748 -11.759 -19.895 1.00 89.84  ? 79  PRO   A CB  1 
ATOM   289  C  CG  . PRO   A 1 38  ? -18.217 -10.442 -20.296 1.00 90.51  ? 79  PRO   A CG  1 
ATOM   290  C  CD  . PRO   A 1 38  ? -17.919 -10.555 -21.776 1.00 90.58  ? 79  PRO   A CD  1 
ATOM   291  N  N   . ASN   A 1 39  ? -21.716 -12.413 -20.047 1.00 87.83  ? 80  ASN   A N   1 
ATOM   292  C  CA  . ASN   A 1 39  ? -23.146 -12.210 -19.833 1.00 85.10  ? 80  ASN   A CA  1 
ATOM   293  C  C   . ASN   A 1 39  ? -23.336 -12.078 -18.325 1.00 86.64  ? 80  ASN   A C   1 
ATOM   294  O  O   . ASN   A 1 39  ? -23.790 -13.007 -17.664 1.00 84.90  ? 80  ASN   A O   1 
ATOM   295  C  CB  . ASN   A 1 39  ? -23.964 -13.374 -20.412 1.00 82.87  ? 80  ASN   A CB  1 
ATOM   296  C  CG  . ASN   A 1 39  ? -25.423 -13.263 -20.091 1.00 81.50  ? 80  ASN   A CG  1 
ATOM   297  O  OD1 . ASN   A 1 39  ? -25.827 -13.115 -18.930 1.00 81.56  ? 80  ASN   A OD1 1 
ATOM   298  N  ND2 . ASN   A 1 39  ? -26.233 -13.282 -21.129 1.00 80.50  ? 80  ASN   A ND2 1 
ATOM   299  N  N   . PRO   A 1 40  ? -22.954 -10.949 -17.734 1.00 85.31  ? 81  PRO   A N   1 
ATOM   300  C  CA  . PRO   A 1 40  ? -23.073 -10.848 -16.273 1.00 83.47  ? 81  PRO   A CA  1 
ATOM   301  C  C   . PRO   A 1 40  ? -24.540 -10.624 -15.925 1.00 79.01  ? 81  PRO   A C   1 
ATOM   302  O  O   . PRO   A 1 40  ? -25.310 -10.172 -16.764 1.00 82.34  ? 81  PRO   A O   1 
ATOM   303  C  CB  . PRO   A 1 40  ? -22.187 -9.641  -15.932 1.00 79.47  ? 81  PRO   A CB  1 
ATOM   304  C  CG  . PRO   A 1 40  ? -22.017 -8.889  -17.140 1.00 79.82  ? 81  PRO   A CG  1 
ATOM   305  C  CD  . PRO   A 1 40  ? -22.539 -9.668  -18.329 1.00 80.16  ? 81  PRO   A CD  1 
ATOM   306  N  N   . GLN   A 1 41  ? -24.974 -10.987 -14.733 1.00 74.48  ? 82  GLN   A N   1 
ATOM   307  C  CA  . GLN   A 1 41  ? -26.387 -10.827 -14.505 1.00 70.60  ? 82  GLN   A CA  1 
ATOM   308  C  C   . GLN   A 1 41  ? -26.629 -10.316 -13.085 1.00 66.37  ? 82  GLN   A C   1 
ATOM   309  O  O   . GLN   A 1 41  ? -25.817 -10.516 -12.168 1.00 61.66  ? 82  GLN   A O   1 
ATOM   310  C  CB  . GLN   A 1 41  ? -27.115 -12.181 -14.780 1.00 68.78  ? 82  GLN   A CB  1 
ATOM   311  C  CG  . GLN   A 1 41  ? -28.510 -11.897 -15.065 1.00 68.75  ? 82  GLN   A CG  1 
ATOM   312  C  CD  . GLN   A 1 41  ? -28.506 -10.657 -15.875 1.00 74.40  ? 82  GLN   A CD  1 
ATOM   313  O  OE1 . GLN   A 1 41  ? -29.013 -9.638  -15.454 1.00 69.57  ? 82  GLN   A OE1 1 
ATOM   314  N  NE2 . GLN   A 1 41  ? -27.953 -10.745 -17.106 1.00 73.32  ? 82  GLN   A NE2 1 
ATOM   315  N  N   . GLU   A 1 42  ? -27.827 -9.800  -12.894 1.00 62.92  ? 83  GLU   A N   1 
ATOM   316  C  CA  . GLU   A 1 42  ? -28.200 -9.129  -11.673 1.00 60.66  ? 83  GLU   A CA  1 
ATOM   317  C  C   . GLU   A 1 42  ? -29.149 -9.979  -10.839 1.00 58.71  ? 83  GLU   A C   1 
ATOM   318  O  O   . GLU   A 1 42  ? -29.881 -10.836 -11.331 1.00 56.56  ? 83  GLU   A O   1 
ATOM   319  C  CB  . GLU   A 1 42  ? -28.826 -7.778  -12.011 1.00 58.28  ? 83  GLU   A CB  1 
ATOM   320  C  CG  . GLU   A 1 42  ? -28.585 -6.711  -10.901 1.00 56.82  ? 83  GLU   A CG  1 
ATOM   321  C  CD  . GLU   A 1 42  ? -29.625 -5.565  -10.873 1.00 62.52  ? 83  GLU   A CD  1 
ATOM   322  O  OE1 . GLU   A 1 42  ? -30.419 -5.464  -11.832 1.00 69.24  ? 83  GLU   A OE1 1 
ATOM   323  O  OE2 . GLU   A 1 42  ? -29.636 -4.747  -9.914  1.00 58.23  ? 83  GLU   A OE2 1 
ATOM   324  N  N   . ILE   A 1 43  ? -29.122 -9.715  -9.548  1.00 56.23  ? 84  ILE   A N   1 
ATOM   325  C  CA  . ILE   A 1 43  ? -30.024 -10.353 -8.600  1.00 56.17  ? 84  ILE   A CA  1 
ATOM   326  C  C   . ILE   A 1 43  ? -30.416 -9.409  -7.464  1.00 55.88  ? 84  ILE   A C   1 
ATOM   327  O  O   . ILE   A 1 43  ? -29.564 -8.938  -6.697  1.00 54.06  ? 84  ILE   A O   1 
ATOM   328  C  CB  . ILE   A 1 43  ? -29.385 -11.627 -8.031  1.00 56.77  ? 84  ILE   A CB  1 
ATOM   329  C  CG1 . ILE   A 1 43  ? -29.137 -12.620 -9.161  1.00 55.68  ? 84  ILE   A CG1 1 
ATOM   330  C  CG2 . ILE   A 1 43  ? -30.266 -12.238 -6.964  1.00 55.67  ? 84  ILE   A CG2 1 
ATOM   331  C  CD1 . ILE   A 1 43  ? -29.171 -14.122 -8.804  1.00 56.82  ? 84  ILE   A CD1 1 
ATOM   332  N  N   . HIS   A 1 44  ? -31.715 -9.134  -7.334  1.00 57.12  ? 85  HIS   A N   1 
ATOM   333  C  CA  . HIS   A 1 44  ? -32.186 -8.252  -6.271  1.00 57.16  ? 85  HIS   A CA  1 
ATOM   334  C  C   . HIS   A 1 44  ? -32.082 -8.944  -4.916  1.00 57.28  ? 85  HIS   A C   1 
ATOM   335  O  O   . HIS   A 1 44  ? -32.397 -10.131 -4.774  1.00 57.69  ? 85  HIS   A O   1 
ATOM   336  C  CB  . HIS   A 1 44  ? -33.634 -7.792  -6.492  1.00 54.57  ? 85  HIS   A CB  1 
ATOM   337  C  CG  . HIS   A 1 44  ? -34.102 -6.814  -5.455  1.00 59.31  ? 85  HIS   A CG  1 
ATOM   338  N  ND1 . HIS   A 1 44  ? -33.313 -5.773  -5.014  1.00 59.19  ? 85  HIS   A ND1 1 
ATOM   339  C  CD2 . HIS   A 1 44  ? -35.262 -6.725  -4.761  1.00 60.63  ? 85  HIS   A CD2 1 
ATOM   340  C  CE1 . HIS   A 1 44  ? -33.969 -5.080  -4.100  1.00 61.78  ? 85  HIS   A CE1 1 
ATOM   341  N  NE2 . HIS   A 1 44  ? -35.154 -5.637  -3.929  1.00 64.87  ? 85  HIS   A NE2 1 
ATOM   342  N  N   . LEU   A 1 45  ? -31.656 -8.180  -3.913  1.00 58.64  ? 86  LEU   A N   1 
ATOM   343  C  CA  . LEU   A 1 45  ? -31.508 -8.682  -2.546  1.00 57.89  ? 86  LEU   A CA  1 
ATOM   344  C  C   . LEU   A 1 45  ? -32.694 -8.169  -1.734  1.00 60.21  ? 86  LEU   A C   1 
ATOM   345  O  O   . LEU   A 1 45  ? -32.638 -7.109  -1.105  1.00 62.94  ? 86  LEU   A O   1 
ATOM   346  C  CB  . LEU   A 1 45  ? -30.170 -8.258  -1.950  1.00 55.53  ? 86  LEU   A CB  1 
ATOM   347  C  CG  . LEU   A 1 45  ? -28.937 -8.477  -2.833  1.00 53.76  ? 86  LEU   A CG  1 
ATOM   348  C  CD1 . LEU   A 1 45  ? -27.685 -7.884  -2.206  1.00 53.78  ? 86  LEU   A CD1 1 
ATOM   349  C  CD2 . LEU   A 1 45  ? -28.758 -9.963  -3.127  1.00 55.83  ? 86  LEU   A CD2 1 
ATOM   350  N  N   . GLU   A 1 46  ? -33.776 -8.946  -1.757  1.00 62.88  ? 87  GLU   A N   1 
ATOM   351  C  CA  . GLU   A 1 46  ? -35.049 -8.524  -1.183  1.00 63.89  ? 87  GLU   A CA  1 
ATOM   352  C  C   . GLU   A 1 46  ? -34.890 -8.253  0.308   1.00 63.28  ? 87  GLU   A C   1 
ATOM   353  O  O   . GLU   A 1 46  ? -34.211 -9.000  1.015   1.00 60.09  ? 87  GLU   A O   1 
ATOM   354  C  CB  . GLU   A 1 46  ? -36.099 -9.614  -1.425  1.00 66.58  ? 87  GLU   A CB  1 
ATOM   355  C  CG  . GLU   A 1 46  ? -37.514 -9.295  -1.002  1.00 67.23  ? 87  GLU   A CG  1 
ATOM   356  C  CD  . GLU   A 1 46  ? -37.986 -7.921  -1.465  1.00 71.58  ? 87  GLU   A CD  1 
ATOM   357  O  OE1 . GLU   A 1 46  ? -38.415 -7.121  -0.600  1.00 72.70  ? 87  GLU   A OE1 1 
ATOM   358  O  OE2 . GLU   A 1 46  ? -37.928 -7.638  -2.687  1.00 71.91  ? 87  GLU   A OE2 1 
ATOM   359  N  N   . ASN   A 1 47  ? -35.503 -7.165  0.782   1.00 65.81  ? 88  ASN   A N   1 
ATOM   360  C  CA  . ASN   A 1 47  ? -35.521 -6.826  2.214   1.00 65.74  ? 88  ASN   A CA  1 
ATOM   361  C  C   . ASN   A 1 47  ? -34.128 -6.577  2.785   1.00 63.14  ? 88  ASN   A C   1 
ATOM   362  O  O   . ASN   A 1 47  ? -33.903 -6.730  3.990   1.00 61.75  ? 88  ASN   A O   1 
ATOM   363  C  CB  . ASN   A 1 47  ? -36.232 -7.905  3.047   1.00 67.63  ? 88  ASN   A CB  1 
ATOM   364  C  CG  . ASN   A 1 47  ? -37.544 -8.365  2.432   1.00 68.74  ? 88  ASN   A CG  1 
ATOM   365  O  OD1 . ASN   A 1 47  ? -38.282 -7.550  1.881   1.00 71.85  ? 88  ASN   A OD1 1 
ATOM   366  N  ND2 . ASN   A 1 47  ? -37.864 -9.659  2.564   1.00 66.89  ? 88  ASN   A ND2 1 
ATOM   367  N  N   . VAL   A 1 48  ? -33.174 -6.188  1.951   1.00 62.50  ? 89  VAL   A N   1 
ATOM   368  C  CA  . VAL   A 1 48  ? -31.786 -6.133  2.380   1.00 59.76  ? 89  VAL   A CA  1 
ATOM   369  C  C   . VAL   A 1 48  ? -31.286 -4.700  2.325   1.00 58.63  ? 89  VAL   A C   1 
ATOM   370  O  O   . VAL   A 1 48  ? -31.597 -3.953  1.391   1.00 56.39  ? 89  VAL   A O   1 
ATOM   371  C  CB  . VAL   A 1 48  ? -30.896 -7.054  1.530   1.00 59.64  ? 89  VAL   A CB  1 
ATOM   372  C  CG1 . VAL   A 1 48  ? -29.442 -6.723  1.780   1.00 61.80  ? 89  VAL   A CG1 1 
ATOM   373  C  CG2 . VAL   A 1 48  ? -31.174 -8.504  1.878   1.00 59.87  ? 89  VAL   A CG2 1 
ATOM   374  N  N   . THR   A 1 49  ? -30.508 -4.323  3.338   1.00 58.91  ? 90  THR   A N   1 
ATOM   375  C  CA  . THR   A 1 49  ? -29.893 -3.008  3.418   1.00 56.33  ? 90  THR   A CA  1 
ATOM   376  C  C   . THR   A 1 49  ? -28.425 -3.165  3.784   1.00 58.23  ? 90  THR   A C   1 
ATOM   377  O  O   . THR   A 1 49  ? -28.054 -4.070  4.544   1.00 58.07  ? 90  THR   A O   1 
ATOM   378  C  CB  . THR   A 1 49  ? -30.590 -2.120  4.439   1.00 57.03  ? 90  THR   A CB  1 
ATOM   379  O  OG1 . THR   A 1 49  ? -30.308 -2.600  5.760   1.00 53.68  ? 90  THR   A OG1 1 
ATOM   380  C  CG2 . THR   A 1 49  ? -32.091 -2.125  4.205   1.00 55.44  ? 90  THR   A CG2 1 
ATOM   381  N  N   . GLU   A 1 50  ? -27.597 -2.273  3.236   1.00 58.28  ? 91  GLU   A N   1 
ATOM   382  C  CA  . GLU   A 1 50  ? -26.147 -2.377  3.334   1.00 54.18  ? 91  GLU   A CA  1 
ATOM   383  C  C   . GLU   A 1 50  ? -25.542 -0.979  3.296   1.00 51.25  ? 91  GLU   A C   1 
ATOM   384  O  O   . GLU   A 1 50  ? -26.090 -0.063  2.678   1.00 50.39  ? 91  GLU   A O   1 
ATOM   385  C  CB  . GLU   A 1 50  ? -25.573 -3.233  2.189   1.00 55.06  ? 91  GLU   A CB  1 
ATOM   386  C  CG  . GLU   A 1 50  ? -24.048 -3.413  2.191   1.00 57.55  ? 91  GLU   A CG  1 
ATOM   387  C  CD  . GLU   A 1 50  ? -23.588 -4.598  3.047   1.00 58.56  ? 91  GLU   A CD  1 
ATOM   388  O  OE1 . GLU   A 1 50  ? -24.468 -5.321  3.557   1.00 59.78  ? 91  GLU   A OE1 1 
ATOM   389  O  OE2 . GLU   A 1 50  ? -22.361 -4.836  3.175   1.00 57.43  ? 91  GLU   A OE2 1 
ATOM   390  N  N   . ASN   A 1 51  ? -24.405 -0.826  3.964   1.00 50.77  ? 92  ASN   A N   1 
ATOM   391  C  CA  . ASN   A 1 51  ? -23.711 0.451   4.045   1.00 49.51  ? 92  ASN   A CA  1 
ATOM   392  C  C   . ASN   A 1 51  ? -22.645 0.535   2.962   1.00 48.43  ? 92  ASN   A C   1 
ATOM   393  O  O   . ASN   A 1 51  ? -21.990 -0.462  2.645   1.00 50.95  ? 92  ASN   A O   1 
ATOM   394  C  CB  . ASN   A 1 51  ? -23.062 0.627   5.417   1.00 50.67  ? 92  ASN   A CB  1 
ATOM   395  C  CG  . ASN   A 1 51  ? -23.735 1.686   6.255   1.00 53.58  ? 92  ASN   A CG  1 
ATOM   396  O  OD1 . ASN   A 1 51  ? -24.958 1.814   6.263   1.00 55.77  ? 92  ASN   A OD1 1 
ATOM   397  N  ND2 . ASN   A 1 51  ? -22.926 2.475   6.956   1.00 56.44  ? 92  ASN   A ND2 1 
ATOM   398  N  N   . PHE   A 1 52  ? -22.484 1.729   2.388   1.00 45.26  ? 93  PHE   A N   1 
ATOM   399  C  CA  . PHE   A 1 52  ? -21.524 1.984   1.323   1.00 41.91  ? 93  PHE   A CA  1 
ATOM   400  C  C   . PHE   A 1 52  ? -20.648 3.157   1.732   1.00 42.13  ? 93  PHE   A C   1 
ATOM   401  O  O   . PHE   A 1 52  ? -21.061 4.003   2.530   1.00 44.92  ? 93  PHE   A O   1 
ATOM   402  C  CB  . PHE   A 1 52  ? -22.239 2.277   -0.024  1.00 44.39  ? 93  PHE   A CB  1 
ATOM   403  C  CG  . PHE   A 1 52  ? -22.824 1.051   -0.671  1.00 40.74  ? 93  PHE   A CG  1 
ATOM   404  C  CD1 . PHE   A 1 52  ? -23.913 0.417   -0.107  1.00 44.48  ? 93  PHE   A CD1 1 
ATOM   405  C  CD2 . PHE   A 1 52  ? -22.268 0.516   -1.817  1.00 41.39  ? 93  PHE   A CD2 1 
ATOM   406  C  CE1 . PHE   A 1 52  ? -24.454 -0.734  -0.681  1.00 45.73  ? 93  PHE   A CE1 1 
ATOM   407  C  CE2 . PHE   A 1 52  ? -22.803 -0.633  -2.406  1.00 41.05  ? 93  PHE   A CE2 1 
ATOM   408  C  CZ  . PHE   A 1 52  ? -23.897 -1.258  -1.838  1.00 43.70  ? 93  PHE   A CZ  1 
ATOM   409  N  N   . ASN   A 1 53  ? -19.417 3.184   1.223   1.00 41.12  ? 94  ASN   A N   1 
ATOM   410  C  CA  . ASN   A 1 53  ? -18.553 4.355   1.377   1.00 43.71  ? 94  ASN   A CA  1 
ATOM   411  C  C   . ASN   A 1 53  ? -17.787 4.560   0.082   1.00 40.50  ? 94  ASN   A C   1 
ATOM   412  O  O   . ASN   A 1 53  ? -16.781 3.889   -0.160  1.00 41.24  ? 94  ASN   A O   1 
ATOM   413  C  CB  . ASN   A 1 53  ? -17.583 4.222   2.550   1.00 42.51  ? 94  ASN   A CB  1 
ATOM   414  C  CG  . ASN   A 1 53  ? -16.853 5.527   2.834   1.00 43.97  ? 94  ASN   A CG  1 
ATOM   415  O  OD1 . ASN   A 1 53  ? -16.939 6.489   2.053   1.00 43.62  ? 94  ASN   A OD1 1 
ATOM   416  N  ND2 . ASN   A 1 53  ? -16.165 5.585   3.970   1.00 44.40  ? 94  ASN   A ND2 1 
ATOM   417  N  N   . MET   A 1 54  ? -18.259 5.488   -0.742  1.00 40.83  ? 95  MET   A N   1 
ATOM   418  C  CA  . MET   A 1 54  ? -17.617 5.772   -2.018  1.00 41.84  ? 95  MET   A CA  1 
ATOM   419  C  C   . MET   A 1 54  ? -16.222 6.364   -1.857  1.00 41.42  ? 95  MET   A C   1 
ATOM   420  O  O   . MET   A 1 54  ? -15.445 6.339   -2.813  1.00 41.26  ? 95  MET   A O   1 
ATOM   421  C  CB  . MET   A 1 54  ? -18.481 6.743   -2.807  1.00 38.91  ? 95  MET   A CB  1 
ATOM   422  C  CG  . MET   A 1 54  ? -18.587 8.064   -2.103  1.00 41.57  ? 95  MET   A CG  1 
ATOM   423  S  SD  . MET   A 1 54  ? -19.547 9.193   -3.085  1.00 37.17  ? 95  MET   A SD  1 
ATOM   424  C  CE  . MET   A 1 54  ? -18.325 9.633   -4.331  1.00 38.10  ? 95  MET   A CE  1 
ATOM   425  N  N   . TRP   A 1 55  ? -15.891 6.909   -0.684  1.00 41.62  ? 96  TRP   A N   1 
ATOM   426  C  CA  . TRP   A 1 55  ? -14.576 7.493   -0.438  1.00 41.18  ? 96  TRP   A CA  1 
ATOM   427  C  C   . TRP   A 1 55  ? -13.574 6.481   0.089   1.00 41.62  ? 96  TRP   A C   1 
ATOM   428  O  O   . TRP   A 1 55  ? -12.373 6.762   0.111   1.00 44.15  ? 96  TRP   A O   1 
ATOM   429  C  CB  . TRP   A 1 55  ? -14.719 8.663   0.539   1.00 44.46  ? 96  TRP   A CB  1 
ATOM   430  C  CG  . TRP   A 1 55  ? -15.742 9.575   0.017   1.00 45.58  ? 96  TRP   A CG  1 
ATOM   431  C  CD1 . TRP   A 1 55  ? -17.055 9.608   0.374   1.00 44.24  ? 96  TRP   A CD1 1 
ATOM   432  C  CD2 . TRP   A 1 55  ? -15.569 10.577  -0.986  1.00 42.65  ? 96  TRP   A CD2 1 
ATOM   433  N  NE1 . TRP   A 1 55  ? -17.717 10.565  -0.345  1.00 42.75  ? 96  TRP   A NE1 1 
ATOM   434  C  CE2 . TRP   A 1 55  ? -16.832 11.179  -1.188  1.00 41.42  ? 96  TRP   A CE2 1 
ATOM   435  C  CE3 . TRP   A 1 55  ? -14.475 11.028  -1.729  1.00 40.86  ? 96  TRP   A CE3 1 
ATOM   436  C  CZ2 . TRP   A 1 55  ? -17.037 12.204  -2.109  1.00 42.77  ? 96  TRP   A CZ2 1 
ATOM   437  C  CZ3 . TRP   A 1 55  ? -14.677 12.054  -2.644  1.00 42.94  ? 96  TRP   A CZ3 1 
ATOM   438  C  CH2 . TRP   A 1 55  ? -15.951 12.631  -2.826  1.00 43.83  ? 96  TRP   A CH2 1 
ATOM   439  N  N   . LYS   A 1 56  ? -14.040 5.311   0.500   1.00 43.97  ? 97  LYS   A N   1 
ATOM   440  C  CA  . LYS   A 1 56  ? -13.189 4.223   0.954   1.00 41.49  ? 97  LYS   A CA  1 
ATOM   441  C  C   . LYS   A 1 56  ? -13.557 2.982   0.146   1.00 38.86  ? 97  LYS   A C   1 
ATOM   442  O  O   . LYS   A 1 56  ? -14.171 2.043   0.652   1.00 40.27  ? 97  LYS   A O   1 
ATOM   443  C  CB  . LYS   A 1 56  ? -13.372 3.967   2.450   1.00 45.05  ? 97  LYS   A CB  1 
ATOM   444  C  CG  . LYS   A 1 56  ? -12.220 4.377   3.340   1.00 45.88  ? 97  LYS   A CG  1 
ATOM   445  C  CD  . LYS   A 1 56  ? -12.344 5.845   3.722   1.00 47.62  ? 97  LYS   A CD  1 
ATOM   446  C  CE  . LYS   A 1 56  ? -10.990 6.546   3.796   1.00 51.75  ? 97  LYS   A CE  1 
ATOM   447  N  NZ  . LYS   A 1 56  ? -10.988 7.870   3.105   1.00 55.32  ? 97  LYS   A NZ  1 
ATOM   448  N  N   . ASN   A 1 57  ? -13.222 3.004   -1.141  1.00 37.22  ? 98  ASN   A N   1 
ATOM   449  C  CA  . ASN   A 1 57  ? -13.644 1.973   -2.083  1.00 40.17  ? 98  ASN   A CA  1 
ATOM   450  C  C   . ASN   A 1 57  ? -12.437 1.466   -2.853  1.00 38.97  ? 98  ASN   A C   1 
ATOM   451  O  O   . ASN   A 1 57  ? -11.801 2.224   -3.589  1.00 38.09  ? 98  ASN   A O   1 
ATOM   452  C  CB  . ASN   A 1 57  ? -14.708 2.510   -3.043  1.00 39.41  ? 98  ASN   A CB  1 
ATOM   453  C  CG  . ASN   A 1 57  ? -15.302 1.435   -3.909  1.00 38.06  ? 98  ASN   A CG  1 
ATOM   454  O  OD1 . ASN   A 1 57  ? -14.825 0.292   -3.928  1.00 42.49  ? 98  ASN   A OD1 1 
ATOM   455  N  ND2 . ASN   A 1 57  ? -16.381 1.774   -4.604  1.00 36.95  ? 98  ASN   A ND2 1 
ATOM   456  N  N   . ASN   A 1 58  ? -12.126 0.185   -2.685  1.00 41.45  ? 99  ASN   A N   1 
ATOM   457  C  CA  . ASN   A 1 58  ? -10.972 -0.374  -3.365  1.00 40.59  ? 99  ASN   A CA  1 
ATOM   458  C  C   . ASN   A 1 58  ? -11.154 -0.433  -4.876  1.00 39.81  ? 99  ASN   A C   1 
ATOM   459  O  O   . ASN   A 1 58  ? -10.156 -0.420  -5.603  1.00 38.20  ? 99  ASN   A O   1 
ATOM   460  C  CB  . ASN   A 1 58  ? -10.668 -1.759  -2.817  1.00 43.11  ? 99  ASN   A CB  1 
ATOM   461  C  CG  . ASN   A 1 58  ? -9.262  -2.201  -3.147  1.00 49.61  ? 99  ASN   A CG  1 
ATOM   462  O  OD1 . ASN   A 1 58  ? -9.061  -3.249  -3.778  1.00 50.59  ? 99  ASN   A OD1 1 
ATOM   463  N  ND2 . ASN   A 1 58  ? -8.275  -1.397  -2.744  1.00 47.61  ? 99  ASN   A ND2 1 
ATOM   464  N  N   . MET   A 1 59  ? -12.397 -0.480  -5.364  1.00 38.94  ? 100 MET   A N   1 
ATOM   465  C  CA  . MET   A 1 59  ? -12.618 -0.448  -6.804  1.00 39.14  ? 100 MET   A CA  1 
ATOM   466  C  C   . MET   A 1 59  ? -12.084 0.842   -7.409  1.00 38.43  ? 100 MET   A C   1 
ATOM   467  O  O   . MET   A 1 59  ? -11.635 0.845   -8.562  1.00 32.34  ? 100 MET   A O   1 
ATOM   468  C  CB  . MET   A 1 59  ? -14.107 -0.603  -7.118  1.00 37.62  ? 100 MET   A CB  1 
ATOM   469  C  CG  . MET   A 1 59  ? -14.694 -1.951  -6.792  1.00 37.78  ? 100 MET   A CG  1 
ATOM   470  S  SD  . MET   A 1 59  ? -16.482 -1.820  -6.844  1.00 35.26  ? 100 MET   A SD  1 
ATOM   471  C  CE  . MET   A 1 59  ? -16.840 -2.552  -8.438  1.00 33.61  ? 100 MET   A CE  1 
ATOM   472  N  N   . VAL   A 1 60  ? -12.120 1.942   -6.649  1.00 38.06  ? 101 VAL   A N   1 
ATOM   473  C  CA  . VAL   A 1 60  ? -11.571 3.206   -7.137  1.00 40.36  ? 101 VAL   A CA  1 
ATOM   474  C  C   . VAL   A 1 60  ? -10.086 3.052   -7.448  1.00 39.78  ? 101 VAL   A C   1 
ATOM   475  O  O   . VAL   A 1 60  ? -9.614  3.455   -8.517  1.00 36.77  ? 101 VAL   A O   1 
ATOM   476  C  CB  . VAL   A 1 60  ? -11.820 4.333   -6.117  1.00 39.92  ? 101 VAL   A CB  1 
ATOM   477  C  CG1 . VAL   A 1 60  ? -11.205 5.654   -6.611  1.00 37.67  ? 101 VAL   A CG1 1 
ATOM   478  C  CG2 . VAL   A 1 60  ? -13.303 4.518   -5.888  1.00 37.44  ? 101 VAL   A CG2 1 
ATOM   479  N  N   . GLU   A 1 61  ? -9.327  2.462   -6.519  1.00 37.99  ? 102 GLU   A N   1 
ATOM   480  C  CA  . GLU   A 1 61  ? -7.892  2.297   -6.740  1.00 42.25  ? 102 GLU   A CA  1 
ATOM   481  C  C   . GLU   A 1 61  ? -7.569  1.237   -7.783  1.00 38.34  ? 102 GLU   A C   1 
ATOM   482  O  O   . GLU   A 1 61  ? -6.519  1.332   -8.420  1.00 37.45  ? 102 GLU   A O   1 
ATOM   483  C  CB  . GLU   A 1 61  ? -7.176  1.964   -5.434  1.00 46.02  ? 102 GLU   A CB  1 
ATOM   484  C  CG  . GLU   A 1 61  ? -6.649  3.191   -4.738  1.00 47.51  ? 102 GLU   A CG  1 
ATOM   485  C  CD  . GLU   A 1 61  ? -7.721  3.888   -3.932  1.00 49.73  ? 102 GLU   A CD  1 
ATOM   486  O  OE1 . GLU   A 1 61  ? -8.838  3.332   -3.806  1.00 49.33  ? 102 GLU   A OE1 1 
ATOM   487  O  OE2 . GLU   A 1 61  ? -7.444  4.988   -3.416  1.00 52.33  ? 102 GLU   A OE2 1 
ATOM   488  N  N   . GLN   A 1 62  ? -8.480  0.289   -7.992  1.00 40.09  ? 103 GLN   A N   1 
ATOM   489  C  CA  . GLN   A 1 62  ? -8.310  -0.765  -9.022  1.00 38.83  ? 103 GLN   A CA  1 
ATOM   490  C  C   . GLN   A 1 62  ? -8.401  -0.098  -10.390 1.00 38.14  ? 103 GLN   A C   1 
ATOM   491  O  O   . GLN   A 1 62  ? -7.546  -0.342  -11.220 1.00 34.52  ? 103 GLN   A O   1 
ATOM   492  C  CB  . GLN   A 1 62  ? -9.350  -1.860  -8.841  1.00 36.55  ? 103 GLN   A CB  1 
ATOM   493  C  CG  . GLN   A 1 62  ? -9.162  -2.636  -7.559  1.00 42.89  ? 103 GLN   A CG  1 
ATOM   494  C  CD  . GLN   A 1 62  ? -9.281  -4.119  -7.759  1.00 44.86  ? 103 GLN   A CD  1 
ATOM   495  O  OE1 . GLN   A 1 62  ? -9.784  -4.817  -6.900  1.00 43.00  ? 103 GLN   A OE1 1 
ATOM   496  N  NE2 . GLN   A 1 62  ? -8.810  -4.606  -8.894  1.00 43.09  ? 103 GLN   A NE2 1 
ATOM   497  N  N   . MET   A 1 63  ? -9.447  0.688   -10.596 1.00 38.35  ? 104 MET   A N   1 
ATOM   498  C  CA  . MET   A 1 63  ? -9.564  1.473   -11.817 1.00 37.67  ? 104 MET   A CA  1 
ATOM   499  C  C   . MET   A 1 63  ? -8.360  2.382   -11.992 1.00 37.62  ? 104 MET   A C   1 
ATOM   500  O  O   . MET   A 1 63  ? -7.798  2.477   -13.090 1.00 33.12  ? 104 MET   A O   1 
ATOM   501  C  CB  . MET   A 1 63  ? -10.842 2.306   -11.809 1.00 34.64  ? 104 MET   A CB  1 
ATOM   502  C  CG  . MET   A 1 63  ? -11.419 2.470   -13.204 1.00 36.98  ? 104 MET   A CG  1 
ATOM   503  S  SD  . MET   A 1 63  ? -12.845 3.545   -13.193 1.00 28.29  ? 104 MET   A SD  1 
ATOM   504  C  CE  . MET   A 1 63  ? -12.432 4.587   -14.588 1.00 31.72  ? 104 MET   A CE  1 
ATOM   505  N  N   . HIS   A 1 64  ? -7.964  3.074   -10.918 1.00 33.34  ? 105 HIS   A N   1 
ATOM   506  C  CA  . HIS   A 1 64  ? -6.821  3.975   -11.000 1.00 36.21  ? 105 HIS   A CA  1 
ATOM   507  C  C   . HIS   A 1 64  ? -5.583  3.249   -11.502 1.00 38.66  ? 105 HIS   A C   1 
ATOM   508  O  O   . HIS   A 1 64  ? -4.848  3.787   -12.335 1.00 33.50  ? 105 HIS   A O   1 
ATOM   509  C  CB  . HIS   A 1 64  ? -6.563  4.636   -9.648  1.00 37.54  ? 105 HIS   A CB  1 
ATOM   510  C  CG  . HIS   A 1 64  ? -5.829  5.941   -9.735  1.00 38.80  ? 105 HIS   A CG  1 
ATOM   511  N  ND1 . HIS   A 1 64  ? -6.345  7.043   -10.380 1.00 35.31  ? 105 HIS   A ND1 1 
ATOM   512  C  CD2 . HIS   A 1 64  ? -4.644  6.334   -9.209  1.00 39.49  ? 105 HIS   A CD2 1 
ATOM   513  C  CE1 . HIS   A 1 64  ? -5.492  8.047   -10.282 1.00 35.41  ? 105 HIS   A CE1 1 
ATOM   514  N  NE2 . HIS   A 1 64  ? -4.454  7.644   -9.571  1.00 37.35  ? 105 HIS   A NE2 1 
ATOM   515  N  N   . GLU   A 1 65  ? -5.348  2.016   -11.035 1.00 39.71  ? 106 GLU   A N   1 
ATOM   516  C  CA  . GLU   A 1 65  ? -4.222  1.252   -11.553 1.00 36.18  ? 106 GLU   A CA  1 
ATOM   517  C  C   . GLU   A 1 65  ? -4.365  0.997   -13.055 1.00 37.43  ? 106 GLU   A C   1 
ATOM   518  O  O   . GLU   A 1 65  ? -3.380  1.105   -13.792 1.00 39.33  ? 106 GLU   A O   1 
ATOM   519  C  CB  . GLU   A 1 65  ? -4.073  -0.034  -10.734 1.00 42.41  ? 106 GLU   A CB  1 
ATOM   520  C  CG  . GLU   A 1 65  ? -2.927  0.070   -9.706  1.00 45.69  ? 106 GLU   A CG  1 
ATOM   521  C  CD  . GLU   A 1 65  ? -2.886  -1.068  -8.685  1.00 50.94  ? 106 GLU   A CD  1 
ATOM   522  O  OE1 . GLU   A 1 65  ? -2.859  -2.251  -9.092  1.00 50.92  ? 106 GLU   A OE1 1 
ATOM   523  O  OE2 . GLU   A 1 65  ? -2.829  -0.769  -7.466  1.00 54.52  ? 106 GLU   A OE2 1 
ATOM   524  N  N   . ASP   A 1 66  ? -5.582  0.735   -13.547 1.00 34.50  ? 107 ASP   A N   1 
ATOM   525  C  CA  . ASP   A 1 66  ? -5.740  0.492   -14.980 1.00 35.23  ? 107 ASP   A CA  1 
ATOM   526  C  C   . ASP   A 1 66  ? -5.412  1.734   -15.808 1.00 33.63  ? 107 ASP   A C   1 
ATOM   527  O  O   . ASP   A 1 66  ? -4.572  1.673   -16.711 1.00 33.18  ? 107 ASP   A O   1 
ATOM   528  C  CB  . ASP   A 1 66  ? -7.159  -0.006  -15.294 1.00 37.25  ? 107 ASP   A CB  1 
ATOM   529  C  CG  . ASP   A 1 66  ? -7.412  -1.425  -14.780 1.00 38.43  ? 107 ASP   A CG  1 
ATOM   530  O  OD1 . ASP   A 1 66  ? -6.426  -2.155  -14.535 1.00 36.34  ? 107 ASP   A OD1 1 
ATOM   531  O  OD2 . ASP   A 1 66  ? -8.596  -1.805  -14.627 1.00 37.27  ? 107 ASP   A OD2 1 
ATOM   532  N  N   . ILE   A 1 67  ? -6.063  2.866   -15.514 1.00 32.67  ? 108 ILE   A N   1 
ATOM   533  C  CA  . ILE   A 1 67  ? -5.909  4.071   -16.328 1.00 32.48  ? 108 ILE   A CA  1 
ATOM   534  C  C   . ILE   A 1 67  ? -4.452  4.528   -16.371 1.00 32.77  ? 108 ILE   A C   1 
ATOM   535  O  O   . ILE   A 1 67  ? -3.934  4.861   -17.442 1.00 31.64  ? 108 ILE   A O   1 
ATOM   536  C  CB  . ILE   A 1 67  ? -6.855  5.177   -15.821 1.00 34.58  ? 108 ILE   A CB  1 
ATOM   537  C  CG1 . ILE   A 1 67  ? -8.258  4.616   -15.562 1.00 34.04  ? 108 ILE   A CG1 1 
ATOM   538  C  CG2 . ILE   A 1 67  ? -6.988  6.279   -16.850 1.00 29.71  ? 108 ILE   A CG2 1 
ATOM   539  C  CD1 . ILE   A 1 67  ? -8.720  3.639   -16.646 1.00 30.26  ? 108 ILE   A CD1 1 
ATOM   540  N  N   . ILE   A 1 68  ? -3.767  4.545   -15.218 1.00 35.70  ? 109 ILE   A N   1 
ATOM   541  C  CA  . ILE   A 1 68  ? -2.331  4.837   -15.184 1.00 37.29  ? 109 ILE   A CA  1 
ATOM   542  C  C   . ILE   A 1 68  ? -1.561  3.916   -16.137 1.00 41.18  ? 109 ILE   A C   1 
ATOM   543  O  O   . ILE   A 1 68  ? -0.708  4.371   -16.915 1.00 37.02  ? 109 ILE   A O   1 
ATOM   544  C  CB  . ILE   A 1 68  ? -1.793  4.711   -13.747 1.00 38.22  ? 109 ILE   A CB  1 
ATOM   545  C  CG1 . ILE   A 1 68  ? -2.447  5.740   -12.823 1.00 39.39  ? 109 ILE   A CG1 1 
ATOM   546  C  CG2 . ILE   A 1 68  ? -0.280  4.947   -13.730 1.00 39.29  ? 109 ILE   A CG2 1 
ATOM   547  C  CD1 . ILE   A 1 68  ? -1.796  5.818   -11.460 1.00 37.53  ? 109 ILE   A CD1 1 
ATOM   548  N  N   . SER   A 1 69  ? -1.835  2.607   -16.075 1.00 35.73  ? 110 SER   A N   1 
ATOM   549  C  CA  . SER   A 1 69  ? -1.204  1.672   -16.996 1.00 35.80  ? 110 SER   A CA  1 
ATOM   550  C  C   . SER   A 1 69  ? -1.614  1.949   -18.440 1.00 40.99  ? 110 SER   A C   1 
ATOM   551  O  O   . SER   A 1 69  ? -0.790  1.818   -19.351 1.00 41.74  ? 110 SER   A O   1 
ATOM   552  C  CB  . SER   A 1 69  ? -1.538  0.230   -16.588 1.00 40.00  ? 110 SER   A CB  1 
ATOM   553  O  OG  . SER   A 1 69  ? -1.129  -0.697  -17.577 1.00 42.90  ? 110 SER   A OG  1 
ATOM   554  N  N   . LEU   A 1 70  ? -2.881  2.324   -18.676 1.00 38.08  ? 111 LEU   A N   1 
ATOM   555  C  CA  . LEU   A 1 70  ? -3.339  2.603   -20.040 1.00 36.63  ? 111 LEU   A CA  1 
ATOM   556  C  C   . LEU   A 1 70  ? -2.649  3.836   -20.630 1.00 40.36  ? 111 LEU   A C   1 
ATOM   557  O  O   . LEU   A 1 70  ? -2.301  3.849   -21.818 1.00 41.75  ? 111 LEU   A O   1 
ATOM   558  C  CB  . LEU   A 1 70  ? -4.867  2.780   -20.061 1.00 35.71  ? 111 LEU   A CB  1 
ATOM   559  C  CG  . LEU   A 1 70  ? -5.634  2.841   -21.400 1.00 35.42  ? 111 LEU   A CG  1 
ATOM   560  C  CD1 . LEU   A 1 70  ? -7.111  2.559   -21.179 1.00 31.70  ? 111 LEU   A CD1 1 
ATOM   561  C  CD2 . LEU   A 1 70  ? -5.463  4.183   -22.095 1.00 37.04  ? 111 LEU   A CD2 1 
ATOM   562  N  N   . TRP   A 1 71  ? -2.457  4.887   -19.831 1.00 38.76  ? 112 TRP   A N   1 
ATOM   563  C  CA  . TRP   A 1 71  ? -1.886  6.117   -20.365 1.00 35.56  ? 112 TRP   A CA  1 
ATOM   564  C  C   . TRP   A 1 71  ? -0.384  5.991   -20.582 1.00 43.24  ? 112 TRP   A C   1 
ATOM   565  O  O   . TRP   A 1 71  ? 0.156   6.584   -21.524 1.00 45.64  ? 112 TRP   A O   1 
ATOM   566  C  CB  . TRP   A 1 71  ? -2.176  7.273   -19.422 1.00 35.39  ? 112 TRP   A CB  1 
ATOM   567  C  CG  . TRP   A 1 71  ? -3.488  7.912   -19.654 1.00 37.63  ? 112 TRP   A CG  1 
ATOM   568  C  CD1 . TRP   A 1 71  ? -4.706  7.294   -19.713 1.00 33.95  ? 112 TRP   A CD1 1 
ATOM   569  C  CD2 . TRP   A 1 71  ? -3.736  9.305   -19.820 1.00 39.03  ? 112 TRP   A CD2 1 
ATOM   570  N  NE1 . TRP   A 1 71  ? -5.690  8.216   -19.925 1.00 33.60  ? 112 TRP   A NE1 1 
ATOM   571  C  CE2 . TRP   A 1 71  ? -5.123  9.462   -19.991 1.00 37.46  ? 112 TRP   A CE2 1 
ATOM   572  C  CE3 . TRP   A 1 71  ? -2.919  10.433  -19.846 1.00 34.08  ? 112 TRP   A CE3 1 
ATOM   573  C  CZ2 . TRP   A 1 71  ? -5.706  10.701  -20.187 1.00 34.33  ? 112 TRP   A CZ2 1 
ATOM   574  C  CZ3 . TRP   A 1 71  ? -3.491  11.646  -20.039 1.00 33.77  ? 112 TRP   A CZ3 1 
ATOM   575  C  CH2 . TRP   A 1 71  ? -4.876  11.780  -20.207 1.00 36.81  ? 112 TRP   A CH2 1 
ATOM   576  N  N   . ASP   A 1 72  ? 0.299   5.218   -19.733 1.00 43.20  ? 113 ASP   A N   1 
ATOM   577  C  CA  . ASP   A 1 72  ? 1.734   5.018   -19.893 1.00 42.86  ? 113 ASP   A CA  1 
ATOM   578  C  C   . ASP   A 1 72  ? 2.052   4.237   -21.162 1.00 43.15  ? 113 ASP   A C   1 
ATOM   579  O  O   . ASP   A 1 72  ? 3.070   4.510   -21.804 1.00 46.90  ? 113 ASP   A O   1 
ATOM   580  C  CB  . ASP   A 1 72  ? 2.311   4.303   -18.666 1.00 40.24  ? 113 ASP   A CB  1 
ATOM   581  C  CG  . ASP   A 1 72  ? 2.285   5.173   -17.396 1.00 45.78  ? 113 ASP   A CG  1 
ATOM   582  O  OD1 . ASP   A 1 72  ? 1.770   6.317   -17.430 1.00 47.20  ? 113 ASP   A OD1 1 
ATOM   583  O  OD2 . ASP   A 1 72  ? 2.800   4.706   -16.357 1.00 51.96  ? 113 ASP   A OD2 1 
ATOM   584  N  N   . GLN   A 1 73  ? 1.191   3.289   -21.554 1.00 41.73  ? 114 GLN   A N   1 
ATOM   585  C  CA  . GLN   A 1 73  ? 1.400   2.465   -22.744 1.00 44.15  ? 114 GLN   A CA  1 
ATOM   586  C  C   . GLN   A 1 73  ? 0.973   3.155   -24.039 1.00 46.35  ? 114 GLN   A C   1 
ATOM   587  O  O   . GLN   A 1 73  ? 1.438   2.765   -25.119 1.00 42.17  ? 114 GLN   A O   1 
ATOM   588  C  CB  . GLN   A 1 73  ? 0.632   1.131   -22.615 1.00 43.26  ? 114 GLN   A CB  1 
ATOM   589  C  CG  . GLN   A 1 73  ? 1.096   0.202   -21.470 1.00 46.04  ? 114 GLN   A CG  1 
ATOM   590  C  CD  . GLN   A 1 73  ? 0.065   -0.876  -21.098 1.00 47.77  ? 114 GLN   A CD  1 
ATOM   591  O  OE1 . GLN   A 1 73  ? -1.004  -0.973  -21.718 1.00 46.73  ? 114 GLN   A OE1 1 
ATOM   592  N  NE2 . GLN   A 1 73  ? 0.384   -1.684  -20.074 1.00 45.91  ? 114 GLN   A NE2 1 
ATOM   593  N  N   . SER   A 1 74  ? 0.104   4.164   -23.953 1.00 47.59  ? 115 SER   A N   1 
ATOM   594  C  CA  . SER   A 1 74  ? -0.579  4.742   -25.105 1.00 46.91  ? 115 SER   A CA  1 
ATOM   595  C  C   . SER   A 1 74  ? -0.172  6.180   -25.381 1.00 46.74  ? 115 SER   A C   1 
ATOM   596  O  O   . SER   A 1 74  ? -0.001  6.566   -26.544 1.00 45.44  ? 115 SER   A O   1 
ATOM   597  C  CB  . SER   A 1 74  ? -2.102  4.677   -24.891 1.00 43.54  ? 115 SER   A CB  1 
ATOM   598  O  OG  . SER   A 1 74  ? -2.511  3.378   -24.475 1.00 49.98  ? 115 SER   A OG  1 
ATOM   599  N  N   . LEU   A 1 75  ? -0.037  6.989   -24.334 1.00 47.73  ? 116 LEU   A N   1 
ATOM   600  C  CA  . LEU   A 1 75  ? 0.248   8.414   -24.456 1.00 45.47  ? 116 LEU   A CA  1 
ATOM   601  C  C   . LEU   A 1 75  ? 1.649   8.626   -23.898 1.00 47.40  ? 116 LEU   A C   1 
ATOM   602  O  O   . LEU   A 1 75  ? 1.837   8.992   -22.739 1.00 47.73  ? 116 LEU   A O   1 
ATOM   603  C  CB  . LEU   A 1 75  ? -0.804  9.216   -23.726 1.00 45.84  ? 116 LEU   A CB  1 
ATOM   604  C  CG  . LEU   A 1 75  ? -1.042  10.672  -24.130 1.00 44.35  ? 116 LEU   A CG  1 
ATOM   605  C  CD1 . LEU   A 1 75  ? -1.352  10.833  -25.616 1.00 42.21  ? 116 LEU   A CD1 1 
ATOM   606  C  CD2 . LEU   A 1 75  ? -2.179  11.226  -23.294 1.00 40.12  ? 116 LEU   A CD2 1 
ATOM   607  N  N   . GLN   A 1 76  ? 2.625   8.329   -24.708 1.00 49.72  ? 117 GLN   A N   1 
ATOM   608  C  CA  . GLN   A 1 76  ? 4.001   8.432   -24.239 1.00 50.36  ? 117 GLN   A CA  1 
ATOM   609  C  C   . GLN   A 1 76  ? 4.548   9.830   -24.508 1.00 48.91  ? 117 GLN   A C   1 
ATOM   610  O  O   . GLN   A 1 76  ? 4.457   10.316  -25.646 1.00 45.57  ? 117 GLN   A O   1 
ATOM   611  C  CB  . GLN   A 1 76  ? 4.887   7.386   -24.910 1.00 50.82  ? 117 GLN   A CB  1 
ATOM   612  C  CG  . GLN   A 1 76  ? 4.148   6.137   -25.415 1.00 54.43  ? 117 GLN   A CG  1 
ATOM   613  C  CD  . GLN   A 1 76  ? 5.046   4.889   -25.436 1.00 57.63  ? 117 GLN   A CD  1 
ATOM   614  O  OE1 . GLN   A 1 76  ? 6.282   4.991   -25.405 1.00 59.84  ? 117 GLN   A OE1 1 
ATOM   615  N  NE2 . GLN   A 1 76  ? 4.424   3.709   -25.461 1.00 53.88  ? 117 GLN   A NE2 1 
ATOM   616  N  N   . PRO   A 1 77  ? 5.098   10.501  -23.494 1.00 48.13  ? 118 PRO   A N   1 
ATOM   617  C  CA  . PRO   A 1 77  ? 5.719   11.807  -23.716 1.00 52.19  ? 118 PRO   A CA  1 
ATOM   618  C  C   . PRO   A 1 77  ? 7.084   11.665  -24.360 1.00 55.06  ? 118 PRO   A C   1 
ATOM   619  O  O   . PRO   A 1 77  ? 7.824   10.709  -24.116 1.00 54.59  ? 118 PRO   A O   1 
ATOM   620  C  CB  . PRO   A 1 77  ? 5.854   12.379  -22.299 1.00 53.30  ? 118 PRO   A CB  1 
ATOM   621  C  CG  . PRO   A 1 77  ? 6.017   11.170  -21.461 1.00 51.12  ? 118 PRO   A CG  1 
ATOM   622  C  CD  . PRO   A 1 77  ? 5.088   10.151  -22.066 1.00 49.22  ? 118 PRO   A CD  1 
ATOM   623  N  N   . CYS   A 1 78  ? 7.405   12.651  -25.195 1.00 54.05  ? 119 CYS   A N   1 
ATOM   624  C  CA  . CYS   A 1 78  ? 8.716   12.710  -25.826 1.00 55.75  ? 119 CYS   A CA  1 
ATOM   625  C  C   . CYS   A 1 78  ? 9.835   12.818  -24.792 1.00 58.35  ? 119 CYS   A C   1 
ATOM   626  O  O   . CYS   A 1 78  ? 10.924  12.265  -24.988 1.00 60.71  ? 119 CYS   A O   1 
ATOM   627  C  CB  . CYS   A 1 78  ? 8.766   13.897  -26.791 1.00 55.59  ? 119 CYS   A CB  1 
ATOM   628  S  SG  . CYS   A 1 78  ? 7.278   14.136  -27.820 1.00 62.52  ? 119 CYS   A SG  1 
ATOM   629  N  N   . VAL   A 1 79  ? 9.606   13.544  -23.700 1.00 57.14  ? 120 VAL   A N   1 
ATOM   630  C  CA  . VAL   A 1 79  ? 10.629  13.741  -22.678 1.00 60.56  ? 120 VAL   A CA  1 
ATOM   631  C  C   . VAL   A 1 79  ? 9.999   13.618  -21.297 1.00 62.12  ? 120 VAL   A C   1 
ATOM   632  O  O   . VAL   A 1 79  ? 8.898   14.124  -21.056 1.00 59.86  ? 120 VAL   A O   1 
ATOM   633  C  CB  . VAL   A 1 79  ? 11.333  15.105  -22.820 1.00 62.87  ? 120 VAL   A CB  1 
ATOM   634  C  CG1 . VAL   A 1 79  ? 12.697  15.051  -22.152 1.00 65.13  ? 120 VAL   A CG1 1 
ATOM   635  C  CG2 . VAL   A 1 79  ? 11.461  15.499  -24.274 1.00 60.59  ? 120 VAL   A CG2 1 
ATOM   636  N  N   . LYS   A 1 80  ? 10.717  12.971  -20.382 1.00 69.09  ? 121 LYS   A N   1 
ATOM   637  C  CA  . LYS   A 1 80  ? 10.219  12.723  -19.032 1.00 69.46  ? 121 LYS   A CA  1 
ATOM   638  C  C   . LYS   A 1 80  ? 11.164  13.269  -17.975 1.00 74.86  ? 121 LYS   A C   1 
ATOM   639  O  O   . LYS   A 1 80  ? 12.050  12.552  -17.513 1.00 76.75  ? 121 LYS   A O   1 
ATOM   640  C  CB  . LYS   A 1 80  ? 10.017  11.225  -18.808 1.00 72.49  ? 121 LYS   A CB  1 
ATOM   641  C  CG  . LYS   A 1 80  ? 9.282   10.873  -17.526 1.00 72.53  ? 121 LYS   A CG  1 
ATOM   642  C  CD  . LYS   A 1 80  ? 7.868   11.427  -17.511 1.00 69.54  ? 121 LYS   A CD  1 
ATOM   643  C  CE  . LYS   A 1 80  ? 7.470   11.889  -16.119 1.00 71.45  ? 121 LYS   A CE  1 
ATOM   644  N  NZ  . LYS   A 1 80  ? 7.942   13.273  -15.831 1.00 63.46  ? 121 LYS   A NZ  1 
ATOM   645  N  N   . ILE   A 1 87  ? 14.781  10.879  -19.759 1.00 79.89  ? 201 ILE   A N   1 
ATOM   646  C  CA  . ILE   A 1 87  ? 14.104  9.971   -20.679 1.00 72.84  ? 201 ILE   A CA  1 
ATOM   647  C  C   . ILE   A 1 87  ? 13.688  10.695  -21.962 1.00 69.64  ? 201 ILE   A C   1 
ATOM   648  O  O   . ILE   A 1 87  ? 12.824  11.571  -21.952 1.00 65.17  ? 201 ILE   A O   1 
ATOM   649  C  CB  . ILE   A 1 87  ? 12.891  9.311   -20.006 1.00 72.52  ? 201 ILE   A CB  1 
ATOM   650  C  CG1 . ILE   A 1 87  ? 13.355  8.437   -18.835 1.00 73.27  ? 201 ILE   A CG1 1 
ATOM   651  C  CG2 . ILE   A 1 87  ? 12.136  8.463   -21.000 1.00 70.00  ? 201 ILE   A CG2 1 
ATOM   652  C  CD1 . ILE   A 1 87  ? 12.447  7.264   -18.524 1.00 69.95  ? 201 ILE   A CD1 1 
ATOM   653  N  N   . LYS   A 1 88  ? 14.309  10.314  -23.073 1.00 68.12  ? 202 LYS   A N   1 
ATOM   654  C  CA  . LYS   A 1 88  ? 14.050  10.923  -24.373 1.00 64.03  ? 202 LYS   A CA  1 
ATOM   655  C  C   . LYS   A 1 88  ? 13.689  9.803   -25.338 1.00 62.05  ? 202 LYS   A C   1 
ATOM   656  O  O   . LYS   A 1 88  ? 14.557  9.017   -25.730 1.00 63.06  ? 202 LYS   A O   1 
ATOM   657  C  CB  . LYS   A 1 88  ? 15.262  11.718  -24.855 1.00 61.38  ? 202 LYS   A CB  1 
ATOM   658  C  CG  . LYS   A 1 88  ? 15.486  11.689  -26.374 1.00 62.72  ? 202 LYS   A CG  1 
ATOM   659  C  CD  . LYS   A 1 88  ? 14.289  12.254  -27.155 1.00 61.28  ? 202 LYS   A CD  1 
ATOM   660  C  CE  . LYS   A 1 88  ? 14.561  12.261  -28.670 1.00 58.91  ? 202 LYS   A CE  1 
ATOM   661  N  NZ  . LYS   A 1 88  ? 13.338  11.977  -29.506 1.00 55.18  ? 202 LYS   A NZ  1 
ATOM   662  N  N   . GLN   A 1 89  ? 12.411  9.718   -25.702 1.00 61.40  ? 203 GLN   A N   1 
ATOM   663  C  CA  . GLN   A 1 89  ? 11.901  8.559   -26.421 1.00 58.47  ? 203 GLN   A CA  1 
ATOM   664  C  C   . GLN   A 1 89  ? 10.949  9.025   -27.517 1.00 56.96  ? 203 GLN   A C   1 
ATOM   665  O  O   . GLN   A 1 89  ? 10.744  10.225  -27.734 1.00 56.06  ? 203 GLN   A O   1 
ATOM   666  C  CB  . GLN   A 1 89  ? 11.184  7.599   -25.463 1.00 59.96  ? 203 GLN   A CB  1 
ATOM   667  C  CG  . GLN   A 1 89  ? 9.729   7.975   -25.251 1.00 59.75  ? 203 GLN   A CG  1 
ATOM   668  C  CD  . GLN   A 1 89  ? 9.221   7.794   -23.834 1.00 60.53  ? 203 GLN   A CD  1 
ATOM   669  O  OE1 . GLN   A 1 89  ? 9.891   7.219   -22.974 1.00 68.39  ? 203 GLN   A OE1 1 
ATOM   670  N  NE2 . GLN   A 1 89  ? 8.007   8.282   -23.591 1.00 57.39  ? 203 GLN   A NE2 1 
ATOM   671  N  N   . ALA   A 1 90  ? 10.339  8.044   -28.180 1.00 59.11  ? 204 ALA   A N   1 
ATOM   672  C  CA  . ALA   A 1 90  ? 9.293   8.272   -29.167 1.00 55.20  ? 204 ALA   A CA  1 
ATOM   673  C  C   . ALA   A 1 90  ? 8.029   8.824   -28.519 1.00 54.87  ? 204 ALA   A C   1 
ATOM   674  O  O   . ALA   A 1 90  ? 7.774   8.631   -27.326 1.00 52.68  ? 204 ALA   A O   1 
ATOM   675  C  CB  . ALA   A 1 90  ? 8.946   6.973   -29.896 1.00 51.69  ? 204 ALA   A CB  1 
ATOM   676  N  N   . CYS   A 1 91  ? 7.225   9.503   -29.333 1.00 53.14  ? 205 CYS   A N   1 
ATOM   677  C  CA  . CYS   A 1 91  ? 5.946   10.058  -28.911 1.00 51.11  ? 205 CYS   A CA  1 
ATOM   678  C  C   . CYS   A 1 91  ? 5.089   10.330  -30.136 1.00 47.64  ? 205 CYS   A C   1 
ATOM   679  O  O   . CYS   A 1 91  ? 4.949   11.487  -30.551 1.00 45.98  ? 205 CYS   A O   1 
ATOM   680  C  CB  . CYS   A 1 91  ? 6.153   11.348  -28.126 1.00 50.70  ? 205 CYS   A CB  1 
ATOM   681  S  SG  . CYS   A 1 91  ? 7.240   12.487  -29.005 1.00 55.32  ? 205 CYS   A SG  1 
ATOM   682  N  N   . PRO   A 1 92  ? 4.527   9.309   -30.766 1.00 44.63  ? 206 PRO   A N   1 
ATOM   683  C  CA  . PRO   A 1 92  ? 3.731   9.562   -31.966 1.00 44.45  ? 206 PRO   A CA  1 
ATOM   684  C  C   . PRO   A 1 92  ? 2.402   10.192  -31.592 1.00 42.08  ? 206 PRO   A C   1 
ATOM   685  O  O   . PRO   A 1 92  ? 1.953   10.128  -30.447 1.00 43.30  ? 206 PRO   A O   1 
ATOM   686  C  CB  . PRO   A 1 92  ? 3.532   8.166   -32.570 1.00 44.91  ? 206 PRO   A CB  1 
ATOM   687  C  CG  . PRO   A 1 92  ? 4.529   7.287   -31.849 1.00 47.97  ? 206 PRO   A CG  1 
ATOM   688  C  CD  . PRO   A 1 92  ? 4.623   7.869   -30.479 1.00 47.58  ? 206 PRO   A CD  1 
ATOM   689  N  N   . LYS   A 1 93  ? 1.771   10.812  -32.583 1.00 38.45  ? 207 LYS   A N   1 
ATOM   690  C  CA  . LYS   A 1 93  ? 0.383   11.208  -32.418 1.00 41.52  ? 207 LYS   A CA  1 
ATOM   691  C  C   . LYS   A 1 93  ? -0.487  9.957   -32.458 1.00 41.46  ? 207 LYS   A C   1 
ATOM   692  O  O   . LYS   A 1 93  ? -0.226  9.025   -33.234 1.00 38.14  ? 207 LYS   A O   1 
ATOM   693  C  CB  . LYS   A 1 93  ? -0.046  12.185  -33.510 1.00 39.80  ? 207 LYS   A CB  1 
ATOM   694  C  CG  . LYS   A 1 93  ? 0.473   13.602  -33.319 1.00 41.76  ? 207 LYS   A CG  1 
ATOM   695  C  CD  . LYS   A 1 93  ? 0.638   13.961  -31.847 1.00 45.88  ? 207 LYS   A CD  1 
ATOM   696  C  CE  . LYS   A 1 93  ? 1.351   15.306  -31.685 1.00 45.75  ? 207 LYS   A CE  1 
ATOM   697  N  NZ  . LYS   A 1 93  ? 0.701   16.202  -30.683 1.00 45.84  ? 207 LYS   A NZ  1 
ATOM   698  N  N   . ILE   A 1 94  ? -1.518  9.938   -31.606 1.00 35.71  ? 208 ILE   A N   1 
ATOM   699  C  CA  . ILE   A 1 94  ? -2.301  8.744   -31.335 1.00 38.06  ? 208 ILE   A CA  1 
ATOM   700  C  C   . ILE   A 1 94  ? -3.783  9.058   -31.497 1.00 37.82  ? 208 ILE   A C   1 
ATOM   701  O  O   . ILE   A 1 94  ? -4.214  10.215  -31.446 1.00 35.48  ? 208 ILE   A O   1 
ATOM   702  C  CB  . ILE   A 1 94  ? -2.021  8.176   -29.920 1.00 40.26  ? 208 ILE   A CB  1 
ATOM   703  C  CG1 . ILE   A 1 94  ? -2.396  9.182   -28.817 1.00 39.42  ? 208 ILE   A CG1 1 
ATOM   704  C  CG2 . ILE   A 1 94  ? -0.554  7.769   -29.771 1.00 38.18  ? 208 ILE   A CG2 1 
ATOM   705  C  CD1 . ILE   A 1 94  ? -3.141  8.544   -27.632 1.00 41.81  ? 208 ILE   A CD1 1 
ATOM   706  N  N   . SER   A 1 95  ? -4.553  7.993   -31.727 1.00 38.15  ? 209 SER   A N   1 
ATOM   707  C  CA  . SER   A 1 95  ? -6.011  8.025   -31.723 1.00 38.08  ? 209 SER   A CA  1 
ATOM   708  C  C   . SER   A 1 95  ? -6.525  7.879   -30.294 1.00 37.67  ? 209 SER   A C   1 
ATOM   709  O  O   . SER   A 1 95  ? -6.203  6.895   -29.618 1.00 38.11  ? 209 SER   A O   1 
ATOM   710  C  CB  . SER   A 1 95  ? -6.561  6.900   -32.596 1.00 38.20  ? 209 SER   A CB  1 
ATOM   711  O  OG  . SER   A 1 95  ? -7.917  7.127   -32.898 1.00 36.66  ? 209 SER   A OG  1 
ATOM   712  N  N   . PHE   A 1 96  ? -7.358  8.826   -29.854 1.00 38.97  ? 210 PHE   A N   1 
ATOM   713  C  CA  . PHE   A 1 96  ? -7.746  8.937   -28.450 1.00 39.84  ? 210 PHE   A CA  1 
ATOM   714  C  C   . PHE   A 1 96  ? -9.225  9.294   -28.344 1.00 39.80  ? 210 PHE   A C   1 
ATOM   715  O  O   . PHE   A 1 96  ? -9.603  10.432  -28.628 1.00 43.70  ? 210 PHE   A O   1 
ATOM   716  C  CB  . PHE   A 1 96  ? -6.891  9.998   -27.745 1.00 38.12  ? 210 PHE   A CB  1 
ATOM   717  C  CG  . PHE   A 1 96  ? -6.946  9.904   -26.270 1.00 36.74  ? 210 PHE   A CG  1 
ATOM   718  C  CD1 . PHE   A 1 96  ? -6.033  9.114   -25.601 1.00 39.27  ? 210 PHE   A CD1 1 
ATOM   719  C  CD2 . PHE   A 1 96  ? -7.912  10.573  -25.541 1.00 38.71  ? 210 PHE   A CD2 1 
ATOM   720  C  CE1 . PHE   A 1 96  ? -6.085  8.977   -24.232 1.00 36.75  ? 210 PHE   A CE1 1 
ATOM   721  C  CE2 . PHE   A 1 96  ? -7.960  10.447  -24.162 1.00 34.03  ? 210 PHE   A CE2 1 
ATOM   722  C  CZ  . PHE   A 1 96  ? -7.045  9.647   -23.512 1.00 32.96  ? 210 PHE   A CZ  1 
ATOM   723  N  N   . ASP   A 1 97  ? -10.061 8.333   -27.940 1.00 37.44  ? 211 ASP   A N   1 
ATOM   724  C  CA  . ASP   A 1 97  ? -11.458 8.604   -27.600 1.00 37.52  ? 211 ASP   A CA  1 
ATOM   725  C  C   . ASP   A 1 97  ? -11.955 7.612   -26.554 1.00 37.98  ? 211 ASP   A C   1 
ATOM   726  O  O   . ASP   A 1 97  ? -12.259 6.465   -26.906 1.00 38.65  ? 211 ASP   A O   1 
ATOM   727  C  CB  . ASP   A 1 97  ? -12.345 8.518   -28.838 1.00 39.33  ? 211 ASP   A CB  1 
ATOM   728  C  CG  . ASP   A 1 97  ? -13.754 9.009   -28.573 1.00 43.87  ? 211 ASP   A CG  1 
ATOM   729  O  OD1 . ASP   A 1 97  ? -13.926 9.785   -27.606 1.00 46.59  ? 211 ASP   A OD1 1 
ATOM   730  O  OD2 . ASP   A 1 97  ? -14.680 8.610   -29.319 1.00 42.22  ? 211 ASP   A OD2 1 
ATOM   731  N  N   . PRO   A 1 98  ? -12.045 7.992   -25.277 1.00 36.16  ? 212 PRO   A N   1 
ATOM   732  C  CA  . PRO   A 1 98  ? -12.290 6.992   -24.229 1.00 33.70  ? 212 PRO   A CA  1 
ATOM   733  C  C   . PRO   A 1 98  ? -13.527 6.155   -24.528 1.00 35.81  ? 212 PRO   A C   1 
ATOM   734  O  O   . PRO   A 1 98  ? -14.534 6.664   -25.025 1.00 38.56  ? 212 PRO   A O   1 
ATOM   735  C  CB  . PRO   A 1 98  ? -12.482 7.854   -22.979 1.00 36.91  ? 212 PRO   A CB  1 
ATOM   736  C  CG  . PRO   A 1 98  ? -11.609 9.005   -23.220 1.00 35.68  ? 212 PRO   A CG  1 
ATOM   737  C  CD  . PRO   A 1 98  ? -11.754 9.313   -24.694 1.00 34.29  ? 212 PRO   A CD  1 
ATOM   738  N  N   . ILE   A 1 99  ? -13.442 4.857   -24.239 1.00 35.97  ? 213 ILE   A N   1 
ATOM   739  C  CA  . ILE   A 1 99  ? -14.568 3.930   -24.377 1.00 36.84  ? 213 ILE   A CA  1 
ATOM   740  C  C   . ILE   A 1 99  ? -15.001 3.443   -23.000 1.00 37.65  ? 213 ILE   A C   1 
ATOM   741  O  O   . ILE   A 1 99  ? -14.210 3.500   -22.047 1.00 35.07  ? 213 ILE   A O   1 
ATOM   742  C  CB  . ILE   A 1 99  ? -14.204 2.732   -25.260 1.00 37.78  ? 213 ILE   A CB  1 
ATOM   743  C  CG1 . ILE   A 1 99  ? -12.974 2.032   -24.701 1.00 38.43  ? 213 ILE   A CG1 1 
ATOM   744  C  CG2 . ILE   A 1 99  ? -13.950 3.184   -26.670 1.00 38.73  ? 213 ILE   A CG2 1 
ATOM   745  C  CD1 . ILE   A 1 99  ? -13.017 0.527   -24.837 1.00 39.27  ? 213 ILE   A CD1 1 
ATOM   746  N  N   . PRO   A 1 100 ? -16.228 2.952   -22.842 1.00 38.65  ? 214 PRO   A N   1 
ATOM   747  C  CA  . PRO   A 1 100 ? -16.662 2.467   -21.521 1.00 38.03  ? 214 PRO   A CA  1 
ATOM   748  C  C   . PRO   A 1 100 ? -15.919 1.202   -21.105 1.00 37.84  ? 214 PRO   A C   1 
ATOM   749  O  O   . PRO   A 1 100 ? -15.608 0.342   -21.931 1.00 40.73  ? 214 PRO   A O   1 
ATOM   750  C  CB  . PRO   A 1 100 ? -18.159 2.194   -21.720 1.00 37.02  ? 214 PRO   A CB  1 
ATOM   751  C  CG  . PRO   A 1 100 ? -18.518 2.945   -22.950 1.00 37.05  ? 214 PRO   A CG  1 
ATOM   752  C  CD  . PRO   A 1 100 ? -17.317 2.902   -23.827 1.00 35.38  ? 214 PRO   A CD  1 
ATOM   753  N  N   . ILE   A 1 101 ? -15.619 1.100   -19.812 1.00 37.21  ? 215 ILE   A N   1 
ATOM   754  C  CA  . ILE   A 1 101 ? -14.961 -0.072  -19.246 1.00 39.39  ? 215 ILE   A CA  1 
ATOM   755  C  C   . ILE   A 1 101 ? -15.846 -0.610  -18.135 1.00 39.32  ? 215 ILE   A C   1 
ATOM   756  O  O   . ILE   A 1 101 ? -16.288 0.151   -17.268 1.00 36.73  ? 215 ILE   A O   1 
ATOM   757  C  CB  . ILE   A 1 101 ? -13.557 0.244   -18.692 1.00 38.07  ? 215 ILE   A CB  1 
ATOM   758  C  CG1 . ILE   A 1 101 ? -12.635 0.819   -19.777 1.00 36.29  ? 215 ILE   A CG1 1 
ATOM   759  C  CG2 . ILE   A 1 101 ? -12.941 -1.024  -18.143 1.00 37.70  ? 215 ILE   A CG2 1 
ATOM   760  C  CD1 . ILE   A 1 101 ? -12.630 -0.006  -21.074 1.00 38.91  ? 215 ILE   A CD1 1 
ATOM   761  N  N   . HIS   A 1 102 ? -16.109 -1.910  -18.170 1.00 40.61  ? 216 HIS   A N   1 
ATOM   762  C  CA  . HIS   A 1 102 ? -16.847 -2.586  -17.117 1.00 40.03  ? 216 HIS   A CA  1 
ATOM   763  C  C   . HIS   A 1 102 ? -15.880 -3.330  -16.207 1.00 37.21  ? 216 HIS   A C   1 
ATOM   764  O  O   . HIS   A 1 102 ? -14.945 -3.984  -16.686 1.00 33.67  ? 216 HIS   A O   1 
ATOM   765  C  CB  . HIS   A 1 102 ? -17.872 -3.568  -17.683 1.00 36.64  ? 216 HIS   A CB  1 
ATOM   766  C  CG  . HIS   A 1 102 ? -18.744 -2.999  -18.755 1.00 40.50  ? 216 HIS   A CG  1 
ATOM   767  N  ND1 . HIS   A 1 102 ? -18.266 -2.603  -19.986 1.00 42.31  ? 216 HIS   A ND1 1 
ATOM   768  C  CD2 . HIS   A 1 102 ? -20.068 -2.713  -18.757 1.00 39.98  ? 216 HIS   A CD2 1 
ATOM   769  C  CE1 . HIS   A 1 102 ? -19.267 -2.138  -20.715 1.00 40.55  ? 216 HIS   A CE1 1 
ATOM   770  N  NE2 . HIS   A 1 102 ? -20.369 -2.189  -19.990 1.00 39.67  ? 216 HIS   A NE2 1 
ATOM   771  N  N   . TYR   A 1 103 ? -16.125 -3.232  -14.897 1.00 37.82  ? 217 TYR   A N   1 
ATOM   772  C  CA  . TYR   A 1 103 ? -15.347 -3.931  -13.881 1.00 39.32  ? 217 TYR   A CA  1 
ATOM   773  C  C   . TYR   A 1 103 ? -16.149 -5.085  -13.297 1.00 39.04  ? 217 TYR   A C   1 
ATOM   774  O  O   . TYR   A 1 103 ? -17.325 -4.929  -12.950 1.00 39.47  ? 217 TYR   A O   1 
ATOM   775  C  CB  . TYR   A 1 103 ? -14.907 -2.977  -12.774 1.00 37.09  ? 217 TYR   A CB  1 
ATOM   776  C  CG  . TYR   A 1 103 ? -13.746 -2.149  -13.264 1.00 39.48  ? 217 TYR   A CG  1 
ATOM   777  C  CD1 . TYR   A 1 103 ? -13.956 -0.951  -13.917 1.00 40.25  ? 217 TYR   A CD1 1 
ATOM   778  C  CD2 . TYR   A 1 103 ? -12.440 -2.605  -13.128 1.00 36.60  ? 217 TYR   A CD2 1 
ATOM   779  C  CE1 . TYR   A 1 103 ? -12.889 -0.204  -14.401 1.00 37.19  ? 217 TYR   A CE1 1 
ATOM   780  C  CE2 . TYR   A 1 103 ? -11.378 -1.876  -13.602 1.00 37.31  ? 217 TYR   A CE2 1 
ATOM   781  C  CZ  . TYR   A 1 103 ? -11.608 -0.681  -14.242 1.00 38.85  ? 217 TYR   A CZ  1 
ATOM   782  O  OH  . TYR   A 1 103 ? -10.541 0.033   -14.715 1.00 41.44  ? 217 TYR   A OH  1 
ATOM   783  N  N   . CYS   A 1 104 ? -15.506 -6.248  -13.203 1.00 38.86  ? 218 CYS   A N   1 
ATOM   784  C  CA  . CYS   A 1 104 ? -16.171 -7.490  -12.837 1.00 39.88  ? 218 CYS   A CA  1 
ATOM   785  C  C   . CYS   A 1 104 ? -15.344 -8.259  -11.824 1.00 40.96  ? 218 CYS   A C   1 
ATOM   786  O  O   . CYS   A 1 104 ? -14.107 -8.294  -11.908 1.00 38.23  ? 218 CYS   A O   1 
ATOM   787  C  CB  . CYS   A 1 104 ? -16.399 -8.377  -14.055 1.00 43.04  ? 218 CYS   A CB  1 
ATOM   788  S  SG  . CYS   A 1 104 ? -16.964 -7.527  -15.527 1.00 42.93  ? 218 CYS   A SG  1 
ATOM   789  N  N   . THR   A 1 105 ? -16.039 -8.876  -10.874 1.00 40.63  ? 219 THR   A N   1 
ATOM   790  C  CA  . THR   A 1 105 ? -15.541 -9.733  -9.816  1.00 44.23  ? 219 THR   A CA  1 
ATOM   791  C  C   . THR   A 1 105 ? -15.329 -11.149 -10.339 1.00 44.01  ? 219 THR   A C   1 
ATOM   792  O  O   . THR   A 1 105 ? -16.100 -11.634 -11.170 1.00 44.49  ? 219 THR   A O   1 
ATOM   793  C  CB  . THR   A 1 105 ? -16.507 -9.720  -8.625  1.00 44.72  ? 219 THR   A CB  1 
ATOM   794  O  OG1 . THR   A 1 105 ? -17.843 -10.034 -9.049  1.00 43.67  ? 219 THR   A OG1 1 
ATOM   795  C  CG2 . THR   A 1 105 ? -16.488 -8.345  -7.974  1.00 46.50  ? 219 THR   A CG2 1 
ATOM   796  N  N   . PRO   A 1 106 ? -14.240 -11.809 -9.968  1.00 44.57  ? 220 PRO   A N   1 
ATOM   797  C  CA  . PRO   A 1 106 ? -14.106 -13.222 -10.335 1.00 42.44  ? 220 PRO   A CA  1 
ATOM   798  C  C   . PRO   A 1 106 ? -14.976 -14.101 -9.457  1.00 47.20  ? 220 PRO   A C   1 
ATOM   799  O  O   . PRO   A 1 106 ? -15.722 -13.599 -8.608  1.00 45.14  ? 220 PRO   A O   1 
ATOM   800  C  CB  . PRO   A 1 106 ? -12.611 -13.495 -10.142 1.00 43.45  ? 220 PRO   A CB  1 
ATOM   801  C  CG  . PRO   A 1 106 ? -12.227 -12.565 -9.032  1.00 47.45  ? 220 PRO   A CG  1 
ATOM   802  C  CD  . PRO   A 1 106 ? -13.042 -11.302 -9.270  1.00 46.77  ? 220 PRO   A CD  1 
ATOM   803  N  N   . ALA   A 1 107 ? -14.893 -15.411 -9.676  1.00 47.31  ? 221 ALA   A N   1 
ATOM   804  C  CA  . ALA   A 1 107 ? -15.686 -16.371 -8.922  1.00 48.04  ? 221 ALA   A CA  1 
ATOM   805  C  C   . ALA   A 1 107 ? -15.388 -16.284 -7.428  1.00 49.68  ? 221 ALA   A C   1 
ATOM   806  O  O   . ALA   A 1 107 ? -14.245 -16.065 -7.015  1.00 47.01  ? 221 ALA   A O   1 
ATOM   807  C  CB  . ALA   A 1 107 ? -15.403 -17.785 -9.435  1.00 51.57  ? 221 ALA   A CB  1 
ATOM   808  N  N   . GLY   A 1 108 ? -16.423 -16.494 -6.615  1.00 49.18  ? 222 GLY   A N   1 
ATOM   809  C  CA  . GLY   A 1 108 ? -16.308 -16.314 -5.181  1.00 50.98  ? 222 GLY   A CA  1 
ATOM   810  C  C   . GLY   A 1 108 ? -16.383 -14.875 -4.731  1.00 53.33  ? 222 GLY   A C   1 
ATOM   811  O  O   . GLY   A 1 108 ? -15.961 -14.565 -3.612  1.00 54.95  ? 222 GLY   A O   1 
ATOM   812  N  N   . TYR   A 1 109 ? -16.876 -13.976 -5.580  1.00 52.19  ? 223 TYR   A N   1 
ATOM   813  C  CA  . TYR   A 1 109 ? -16.902 -12.559 -5.260  1.00 51.29  ? 223 TYR   A CA  1 
ATOM   814  C  C   . TYR   A 1 109 ? -18.055 -11.913 -6.003  1.00 49.59  ? 223 TYR   A C   1 
ATOM   815  O  O   . TYR   A 1 109 ? -18.345 -12.264 -7.148  1.00 48.96  ? 223 TYR   A O   1 
ATOM   816  C  CB  . TYR   A 1 109 ? -15.605 -11.851 -5.659  1.00 50.97  ? 223 TYR   A CB  1 
ATOM   817  C  CG  . TYR   A 1 109 ? -14.429 -12.108 -4.757  1.00 51.92  ? 223 TYR   A CG  1 
ATOM   818  C  CD1 . TYR   A 1 109 ? -14.287 -11.449 -3.547  1.00 56.37  ? 223 TYR   A CD1 1 
ATOM   819  C  CD2 . TYR   A 1 109 ? -13.457 -13.019 -5.121  1.00 53.61  ? 223 TYR   A CD2 1 
ATOM   820  C  CE1 . TYR   A 1 109 ? -13.191 -11.694 -2.722  1.00 56.92  ? 223 TYR   A CE1 1 
ATOM   821  C  CE2 . TYR   A 1 109 ? -12.372 -13.271 -4.315  1.00 54.00  ? 223 TYR   A CE2 1 
ATOM   822  C  CZ  . TYR   A 1 109 ? -12.239 -12.610 -3.116  1.00 57.44  ? 223 TYR   A CZ  1 
ATOM   823  O  OH  . TYR   A 1 109 ? -11.149 -12.867 -2.314  1.00 66.57  ? 223 TYR   A OH  1 
ATOM   824  N  N   . VAL   A 1 110 ? -18.690 -10.937 -5.364  1.00 48.70  ? 224 VAL   A N   1 
ATOM   825  C  CA  . VAL   A 1 110 ? -19.784 -10.220 -5.999  1.00 49.62  ? 224 VAL   A CA  1 
ATOM   826  C  C   . VAL   A 1 110 ? -19.603 -8.733  -5.759  1.00 49.72  ? 224 VAL   A C   1 
ATOM   827  O  O   . VAL   A 1 110 ? -19.002 -8.303  -4.773  1.00 49.49  ? 224 VAL   A O   1 
ATOM   828  C  CB  . VAL   A 1 110 ? -21.176 -10.668 -5.499  1.00 50.12  ? 224 VAL   A CB  1 
ATOM   829  C  CG1 . VAL   A 1 110 ? -21.558 -12.007 -6.123  1.00 48.56  ? 224 VAL   A CG1 1 
ATOM   830  C  CG2 . VAL   A 1 110 ? -21.237 -10.708 -3.966  1.00 51.70  ? 224 VAL   A CG2 1 
ATOM   831  N  N   . ILE   A 1 111 ? -20.114 -7.955  -6.706  1.00 46.52  ? 225 ILE   A N   1 
ATOM   832  C  CA  . ILE   A 1 111 ? -20.287 -6.518  -6.562  1.00 44.47  ? 225 ILE   A CA  1 
ATOM   833  C  C   . ILE   A 1 111 ? -21.671 -6.273  -5.984  1.00 46.55  ? 225 ILE   A C   1 
ATOM   834  O  O   . ILE   A 1 111 ? -22.662 -6.849  -6.463  1.00 46.88  ? 225 ILE   A O   1 
ATOM   835  C  CB  . ILE   A 1 111 ? -20.124 -5.807  -7.916  1.00 42.26  ? 225 ILE   A CB  1 
ATOM   836  C  CG1 . ILE   A 1 111 ? -18.861 -6.306  -8.607  1.00 44.68  ? 225 ILE   A CG1 1 
ATOM   837  C  CG2 . ILE   A 1 111 ? -20.013 -4.334  -7.720  1.00 42.10  ? 225 ILE   A CG2 1 
ATOM   838  C  CD1 . ILE   A 1 111 ? -18.547 -5.628  -9.913  1.00 41.78  ? 225 ILE   A CD1 1 
ATOM   839  N  N   . LEU   A 1 112 ? -21.738 -5.440  -4.941  1.00 44.84  ? 226 LEU   A N   1 
ATOM   840  C  CA  . LEU   A 1 112 ? -23.003 -4.933  -4.425  1.00 42.57  ? 226 LEU   A CA  1 
ATOM   841  C  C   . LEU   A 1 112 ? -23.239 -3.543  -5.003  1.00 44.36  ? 226 LEU   A C   1 
ATOM   842  O  O   . LEU   A 1 112 ? -22.345 -2.688  -4.984  1.00 42.18  ? 226 LEU   A O   1 
ATOM   843  C  CB  . LEU   A 1 112 ? -23.008 -4.877  -2.894  1.00 45.30  ? 226 LEU   A CB  1 
ATOM   844  C  CG  . LEU   A 1 112 ? -23.073 -6.240  -2.190  1.00 48.05  ? 226 LEU   A CG  1 
ATOM   845  C  CD1 . LEU   A 1 112 ? -23.342 -6.119  -0.680  1.00 51.70  ? 226 LEU   A CD1 1 
ATOM   846  C  CD2 . LEU   A 1 112 ? -24.033 -7.223  -2.887  1.00 48.67  ? 226 LEU   A CD2 1 
ATOM   847  N  N   . LYS   A 1 113 ? -24.450 -3.330  -5.523  1.00 46.46  ? 227 LYS   A N   1 
ATOM   848  C  CA  . LYS   A 1 113 ? -24.813 -2.136  -6.276  1.00 43.11  ? 227 LYS   A CA  1 
ATOM   849  C  C   . LYS   A 1 113 ? -26.018 -1.469  -5.635  1.00 42.87  ? 227 LYS   A C   1 
ATOM   850  O  O   . LYS   A 1 113 ? -26.981 -2.138  -5.260  1.00 45.10  ? 227 LYS   A O   1 
ATOM   851  C  CB  . LYS   A 1 113 ? -25.132 -2.472  -7.743  1.00 44.32  ? 227 LYS   A CB  1 
ATOM   852  C  CG  . LYS   A 1 113 ? -25.941 -1.407  -8.493  1.00 44.08  ? 227 LYS   A CG  1 
ATOM   853  C  CD  . LYS   A 1 113 ? -25.976 -1.711  -10.001 1.00 45.32  ? 227 LYS   A CD  1 
ATOM   854  C  CE  . LYS   A 1 113 ? -26.551 -0.529  -10.818 1.00 48.95  ? 227 LYS   A CE  1 
ATOM   855  N  NZ  . LYS   A 1 113 ? -25.610 -0.049  -11.889 1.00 46.16  ? 227 LYS   A NZ  1 
ATOM   856  N  N   . CYS   A 1 114 ? -25.963 -0.151  -5.519  1.00 43.45  ? 228 CYS   A N   1 
ATOM   857  C  CA  . CYS   A 1 114 ? -27.016 0.603   -4.854  1.00 47.69  ? 228 CYS   A CA  1 
ATOM   858  C  C   . CYS   A 1 114 ? -27.943 1.176   -5.917  1.00 47.82  ? 228 CYS   A C   1 
ATOM   859  O  O   . CYS   A 1 114 ? -27.492 1.869   -6.841  1.00 48.32  ? 228 CYS   A O   1 
ATOM   860  C  CB  . CYS   A 1 114 ? -26.433 1.713   -3.977  1.00 45.33  ? 228 CYS   A CB  1 
ATOM   861  S  SG  . CYS   A 1 114 ? -27.653 2.656   -3.020  1.00 55.48  ? 228 CYS   A SG  1 
ATOM   862  N  N   . ASN   A 1 115 ? -29.226 0.848   -5.809  1.00 46.70  ? 229 ASN   A N   1 
ATOM   863  C  CA  . ASN   A 1 115 ? -30.226 1.293   -6.759  1.00 48.98  ? 229 ASN   A CA  1 
ATOM   864  C  C   . ASN   A 1 115 ? -31.057 2.443   -6.214  1.00 50.86  ? 229 ASN   A C   1 
ATOM   865  O  O   . ASN   A 1 115 ? -31.955 2.925   -6.905  1.00 55.94  ? 229 ASN   A O   1 
ATOM   866  C  CB  . ASN   A 1 115 ? -31.125 0.115   -7.151  1.00 56.76  ? 229 ASN   A CB  1 
ATOM   867  C  CG  . ASN   A 1 115 ? -30.326 -1.119  -7.565  1.00 53.66  ? 229 ASN   A CG  1 
ATOM   868  O  OD1 . ASN   A 1 115 ? -29.228 -1.007  -8.119  1.00 51.53  ? 229 ASN   A OD1 1 
ATOM   869  N  ND2 . ASN   A 1 115 ? -30.860 -2.301  -7.261  1.00 53.65  ? 229 ASN   A ND2 1 
ATOM   870  N  N   . ASP   A 1 116 ? -30.780 2.894   -4.993  1.00 52.46  ? 230 ASP   A N   1 
ATOM   871  C  CA  . ASP   A 1 116 ? -31.434 4.089   -4.482  1.00 51.27  ? 230 ASP   A CA  1 
ATOM   872  C  C   . ASP   A 1 116 ? -31.180 5.232   -5.454  1.00 50.10  ? 230 ASP   A C   1 
ATOM   873  O  O   . ASP   A 1 116 ? -30.030 5.529   -5.781  1.00 51.72  ? 230 ASP   A O   1 
ATOM   874  C  CB  . ASP   A 1 116 ? -30.897 4.452   -3.091  1.00 52.24  ? 230 ASP   A CB  1 
ATOM   875  C  CG  . ASP   A 1 116 ? -31.532 3.634   -1.974  1.00 55.25  ? 230 ASP   A CG  1 
ATOM   876  O  OD1 . ASP   A 1 116 ? -32.352 2.739   -2.270  1.00 56.45  ? 230 ASP   A OD1 1 
ATOM   877  O  OD2 . ASP   A 1 116 ? -31.234 3.915   -0.791  1.00 53.68  ? 230 ASP   A OD2 1 
ATOM   878  N  N   . LYS   A 1 117 ? -32.240 5.868   -5.941  1.00 51.18  ? 231 LYS   A N   1 
ATOM   879  C  CA  . LYS   A 1 117 ? -32.000 6.886   -6.960  1.00 55.03  ? 231 LYS   A CA  1 
ATOM   880  C  C   . LYS   A 1 117 ? -31.568 8.240   -6.400  1.00 53.50  ? 231 LYS   A C   1 
ATOM   881  O  O   . LYS   A 1 117 ? -31.167 9.105   -7.185  1.00 55.07  ? 231 LYS   A O   1 
ATOM   882  C  CB  . LYS   A 1 117 ? -33.226 7.057   -7.860  1.00 57.48  ? 231 LYS   A CB  1 
ATOM   883  C  CG  . LYS   A 1 117 ? -33.129 6.176   -9.112  1.00 59.75  ? 231 LYS   A CG  1 
ATOM   884  C  CD  . LYS   A 1 117 ? -34.481 5.853   -9.710  1.00 61.19  ? 231 LYS   A CD  1 
ATOM   885  C  CE  . LYS   A 1 117 ? -34.308 5.534   -11.181 1.00 56.74  ? 231 LYS   A CE  1 
ATOM   886  N  NZ  . LYS   A 1 117 ? -34.545 4.102   -11.489 1.00 58.69  ? 231 LYS   A NZ  1 
ATOM   887  N  N   . ASN   A 1 118 ? -31.605 8.446   -5.079  1.00 49.98  ? 232 ASN   A N   1 
ATOM   888  C  CA  . ASN   A 1 118 ? -30.997 9.628   -4.477  1.00 48.86  ? 232 ASN   A CA  1 
ATOM   889  C  C   . ASN   A 1 118 ? -29.846 9.266   -3.546  1.00 46.34  ? 232 ASN   A C   1 
ATOM   890  O  O   . ASN   A 1 118 ? -29.550 10.017  -2.603  1.00 41.46  ? 232 ASN   A O   1 
ATOM   891  C  CB  . ASN   A 1 118 ? -32.008 10.456  -3.686  1.00 51.60  ? 232 ASN   A CB  1 
ATOM   892  C  CG  . ASN   A 1 118 ? -33.016 11.173  -4.571  1.00 57.01  ? 232 ASN   A CG  1 
ATOM   893  O  OD1 . ASN   A 1 118 ? -34.230 11.036  -4.383  1.00 53.57  ? 232 ASN   A OD1 1 
ATOM   894  N  ND2 . ASN   A 1 118 ? -32.522 11.850  -5.608  1.00 52.97  ? 232 ASN   A ND2 1 
ATOM   895  N  N   . PHE   A 1 119 ? -29.242 8.100   -3.740  1.00 45.20  ? 233 PHE   A N   1 
ATOM   896  C  CA  . PHE   A 1 119 ? -28.085 7.729   -2.943  1.00 43.97  ? 233 PHE   A CA  1 
ATOM   897  C  C   . PHE   A 1 119 ? -27.002 8.793   -3.097  1.00 43.91  ? 233 PHE   A C   1 
ATOM   898  O  O   . PHE   A 1 119 ? -26.761 9.291   -4.201  1.00 41.34  ? 233 PHE   A O   1 
ATOM   899  C  CB  . PHE   A 1 119 ? -27.579 6.368   -3.405  1.00 44.91  ? 233 PHE   A CB  1 
ATOM   900  C  CG  . PHE   A 1 119 ? -26.465 5.809   -2.576  1.00 42.34  ? 233 PHE   A CG  1 
ATOM   901  C  CD1 . PHE   A 1 119 ? -26.554 5.743   -1.194  1.00 43.96  ? 233 PHE   A CD1 1 
ATOM   902  C  CD2 . PHE   A 1 119 ? -25.339 5.314   -3.190  1.00 40.59  ? 233 PHE   A CD2 1 
ATOM   903  C  CE1 . PHE   A 1 119 ? -25.524 5.211   -0.454  1.00 43.00  ? 233 PHE   A CE1 1 
ATOM   904  C  CE2 . PHE   A 1 119 ? -24.311 4.784   -2.456  1.00 37.56  ? 233 PHE   A CE2 1 
ATOM   905  C  CZ  . PHE   A 1 119 ? -24.404 4.732   -1.088  1.00 41.04  ? 233 PHE   A CZ  1 
ATOM   906  N  N   . ASN   A 1 120 ? -26.361 9.166   -1.984  1.00 42.19  ? 234 ASN   A N   1 
ATOM   907  C  CA  . ASN   A 1 120 ? -25.308 10.180  -2.009  1.00 42.11  ? 234 ASN   A CA  1 
ATOM   908  C  C   . ASN   A 1 120 ? -23.902 9.604   -1.888  1.00 36.81  ? 234 ASN   A C   1 
ATOM   909  O  O   . ASN   A 1 120 ? -22.926 10.358  -1.965  1.00 39.79  ? 234 ASN   A O   1 
ATOM   910  C  CB  . ASN   A 1 120 ? -25.524 11.221  -0.902  1.00 39.62  ? 234 ASN   A CB  1 
ATOM   911  C  CG  . ASN   A 1 120 ? -25.292 10.665  0.485   1.00 40.98  ? 234 ASN   A CG  1 
ATOM   912  O  OD1 . ASN   A 1 120 ? -25.041 9.476   0.656   1.00 43.46  ? 234 ASN   A OD1 1 
ATOM   913  N  ND2 . ASN   A 1 120 ? -25.386 11.526  1.486   1.00 40.01  ? 234 ASN   A ND2 1 
ATOM   914  N  N   . GLY   A 1 121 ? -23.764 8.306   -1.686  1.00 37.61  ? 235 GLY   A N   1 
ATOM   915  C  CA  . GLY   A 1 121 ? -22.448 7.706   -1.753  1.00 40.60  ? 235 GLY   A CA  1 
ATOM   916  C  C   . GLY   A 1 121 ? -22.019 7.019   -0.478  1.00 41.50  ? 235 GLY   A C   1 
ATOM   917  O  O   . GLY   A 1 121 ? -21.504 5.899   -0.524  1.00 43.32  ? 235 GLY   A O   1 
ATOM   918  N  N   . THR   A 1 122 ? -22.225 7.672   0.663   1.00 46.01  ? 236 THR   A N   1 
ATOM   919  C  CA  . THR   A 1 122 ? -21.939 7.098   1.969   1.00 46.94  ? 236 THR   A CA  1 
ATOM   920  C  C   . THR   A 1 122 ? -23.249 6.791   2.681   1.00 46.74  ? 236 THR   A C   1 
ATOM   921  O  O   . THR   A 1 122 ? -24.243 7.499   2.512   1.00 49.00  ? 236 THR   A O   1 
ATOM   922  C  CB  . THR   A 1 122 ? -21.083 8.054   2.816   1.00 49.55  ? 236 THR   A CB  1 
ATOM   923  O  OG1 . THR   A 1 122 ? -21.820 9.254   3.102   1.00 52.66  ? 236 THR   A OG1 1 
ATOM   924  C  CG2 . THR   A 1 122 ? -19.837 8.448   2.045   1.00 48.11  ? 236 THR   A CG2 1 
ATOM   925  N  N   . GLY   A 1 123 ? -23.256 5.707   3.451   1.00 49.53  ? 237 GLY   A N   1 
ATOM   926  C  CA  . GLY   A 1 123 ? -24.377 5.397   4.300   1.00 49.80  ? 237 GLY   A CA  1 
ATOM   927  C  C   . GLY   A 1 123 ? -25.203 4.236   3.805   1.00 47.50  ? 237 GLY   A C   1 
ATOM   928  O  O   . GLY   A 1 123 ? -24.795 3.486   2.917   1.00 46.48  ? 237 GLY   A O   1 
ATOM   929  N  N   . PRO   A 1 124 ? -26.396 4.080   4.375   1.00 48.94  ? 238 PRO   A N   1 
ATOM   930  C  CA  . PRO   A 1 124 ? -27.209 2.898   4.081   1.00 47.95  ? 238 PRO   A CA  1 
ATOM   931  C  C   . PRO   A 1 124 ? -27.969 3.041   2.770   1.00 49.18  ? 238 PRO   A C   1 
ATOM   932  O  O   . PRO   A 1 124 ? -28.385 4.133   2.371   1.00 52.07  ? 238 PRO   A O   1 
ATOM   933  C  CB  . PRO   A 1 124 ? -28.161 2.814   5.284   1.00 50.44  ? 238 PRO   A CB  1 
ATOM   934  C  CG  . PRO   A 1 124 ? -27.656 3.896   6.285   1.00 51.66  ? 238 PRO   A CG  1 
ATOM   935  C  CD  . PRO   A 1 124 ? -26.975 4.906   5.450   1.00 49.98  ? 238 PRO   A CD  1 
ATOM   936  N  N   . CYS   A 1 125 ? -28.099 1.911   2.085   1.00 49.23  ? 239 CYS   A N   1 
ATOM   937  C  CA  . CYS   A 1 125 ? -28.799 1.780   0.819   1.00 52.16  ? 239 CYS   A CA  1 
ATOM   938  C  C   . CYS   A 1 125 ? -29.895 0.733   0.958   1.00 53.71  ? 239 CYS   A C   1 
ATOM   939  O  O   . CYS   A 1 125 ? -29.665 -0.354  1.497   1.00 53.87  ? 239 CYS   A O   1 
ATOM   940  C  CB  . CYS   A 1 125 ? -27.848 1.366   -0.298  1.00 51.01  ? 239 CYS   A CB  1 
ATOM   941  S  SG  . CYS   A 1 125 ? -28.638 1.264   -1.904  1.00 57.13  ? 239 CYS   A SG  1 
ATOM   942  N  N   . LYS   A 1 126 ? -31.084 1.058   0.461   1.00 54.56  ? 240 LYS   A N   1 
ATOM   943  C  CA  . LYS   A 1 126 ? -32.224 0.167   0.619   1.00 56.34  ? 240 LYS   A CA  1 
ATOM   944  C  C   . LYS   A 1 126 ? -32.369 -0.775  -0.567  1.00 56.57  ? 240 LYS   A C   1 
ATOM   945  O  O   . LYS   A 1 126 ? -32.651 -1.965  -0.388  1.00 55.40  ? 240 LYS   A O   1 
ATOM   946  C  CB  . LYS   A 1 126 ? -33.508 0.980   0.763   1.00 56.87  ? 240 LYS   A CB  1 
ATOM   947  C  CG  . LYS   A 1 126 ? -33.301 2.420   1.169   1.00 58.01  ? 240 LYS   A CG  1 
ATOM   948  C  CD  . LYS   A 1 126 ? -34.642 3.130   1.155   1.00 57.71  ? 240 LYS   A CD  1 
ATOM   949  C  CE  . LYS   A 1 126 ? -35.459 2.732   -0.076  1.00 60.82  ? 240 LYS   A CE  1 
ATOM   950  N  NZ  . LYS   A 1 126 ? -36.653 3.611   -0.272  1.00 60.26  ? 240 LYS   A NZ  1 
ATOM   951  N  N   . ASN   A 1 127 ? -32.189 -0.250  -1.781  1.00 56.79  ? 241 ASN   A N   1 
ATOM   952  C  CA  . ASN   A 1 127 ? -32.372 -1.013  -3.011  1.00 57.60  ? 241 ASN   A CA  1 
ATOM   953  C  C   . ASN   A 1 127 ? -31.016 -1.589  -3.412  1.00 53.76  ? 241 ASN   A C   1 
ATOM   954  O  O   . ASN   A 1 127 ? -30.299 -1.042  -4.253  1.00 52.49  ? 241 ASN   A O   1 
ATOM   955  C  CB  . ASN   A 1 127 ? -32.952 -0.125  -4.108  1.00 57.32  ? 241 ASN   A CB  1 
ATOM   956  C  CG  . ASN   A 1 127 ? -33.642 -0.923  -5.184  1.00 62.13  ? 241 ASN   A CG  1 
ATOM   957  O  OD1 . ASN   A 1 127 ? -33.707 -2.150  -5.112  1.00 63.04  ? 241 ASN   A OD1 1 
ATOM   958  N  ND2 . ASN   A 1 127 ? -34.182 -0.235  -6.178  1.00 65.58  ? 241 ASN   A ND2 1 
ATOM   959  N  N   . VAL   A 1 128 ? -30.656 -2.715  -2.802  1.00 51.58  ? 242 VAL   A N   1 
ATOM   960  C  CA  . VAL   A 1 128 ? -29.342 -3.316  -3.012  1.00 52.00  ? 242 VAL   A CA  1 
ATOM   961  C  C   . VAL   A 1 128 ? -29.485 -4.557  -3.885  1.00 50.56  ? 242 VAL   A C   1 
ATOM   962  O  O   . VAL   A 1 128 ? -30.387 -5.378  -3.674  1.00 50.72  ? 242 VAL   A O   1 
ATOM   963  C  CB  . VAL   A 1 128 ? -28.655 -3.644  -1.678  1.00 51.74  ? 242 VAL   A CB  1 
ATOM   964  C  CG1 . VAL   A 1 128 ? -27.169 -3.865  -1.892  1.00 48.67  ? 242 VAL   A CG1 1 
ATOM   965  C  CG2 . VAL   A 1 128 ? -28.884 -2.504  -0.691  1.00 52.82  ? 242 VAL   A CG2 1 
ATOM   966  N  N   . SER   A 1 129 ? -28.600 -4.687  -4.873  1.00 52.21  ? 243 SER   A N   1 
ATOM   967  C  CA  . SER   A 1 129 ? -28.585 -5.857  -5.741  1.00 52.05  ? 243 SER   A CA  1 
ATOM   968  C  C   . SER   A 1 129 ? -27.147 -6.312  -5.921  1.00 47.99  ? 243 SER   A C   1 
ATOM   969  O  O   . SER   A 1 129 ? -26.197 -5.576  -5.629  1.00 46.25  ? 243 SER   A O   1 
ATOM   970  C  CB  . SER   A 1 129 ? -29.248 -5.585  -7.108  1.00 52.02  ? 243 SER   A CB  1 
ATOM   971  O  OG  . SER   A 1 129 ? -28.384 -4.899  -7.989  1.00 49.36  ? 243 SER   A OG  1 
ATOM   972  N  N   . SER   A 1 130 ? -26.992 -7.542  -6.401  1.00 49.31  ? 244 SER   A N   1 
ATOM   973  C  CA  . SER   A 1 130 ? -25.676 -8.123  -6.629  1.00 50.17  ? 244 SER   A CA  1 
ATOM   974  C  C   . SER   A 1 130 ? -25.492 -8.370  -8.119  1.00 49.87  ? 244 SER   A C   1 
ATOM   975  O  O   . SER   A 1 130 ? -26.329 -9.017  -8.757  1.00 52.45  ? 244 SER   A O   1 
ATOM   976  C  CB  . SER   A 1 130 ? -25.487 -9.421  -5.845  1.00 47.23  ? 244 SER   A CB  1 
ATOM   977  O  OG  . SER   A 1 130 ? -25.942 -10.536 -6.581  1.00 52.41  ? 244 SER   A OG  1 
ATOM   978  N  N   . VAL   A 1 131 ? -24.399 -7.843  -8.666  1.00 47.66  ? 245 VAL   A N   1 
ATOM   979  C  CA  . VAL   A 1 131 ? -24.114 -7.877  -10.092 1.00 49.17  ? 245 VAL   A CA  1 
ATOM   980  C  C   . VAL   A 1 131 ? -22.715 -8.440  -10.285 1.00 47.59  ? 245 VAL   A C   1 
ATOM   981  O  O   . VAL   A 1 131 ? -21.885 -8.428  -9.374  1.00 46.90  ? 245 VAL   A O   1 
ATOM   982  C  CB  . VAL   A 1 131 ? -24.236 -6.480  -10.738 1.00 49.13  ? 245 VAL   A CB  1 
ATOM   983  C  CG1 . VAL   A 1 131 ? -25.598 -5.901  -10.461 1.00 49.02  ? 245 VAL   A CG1 1 
ATOM   984  C  CG2 . VAL   A 1 131 ? -23.158 -5.536  -10.189 1.00 42.90  ? 245 VAL   A CG2 1 
ATOM   985  N  N   . GLN   A 1 132 ? -22.464 -8.959  -11.482 1.00 47.27  ? 246 GLN   A N   1 
ATOM   986  C  CA  . GLN   A 1 132 ? -21.137 -9.478  -11.765 1.00 49.55  ? 246 GLN   A CA  1 
ATOM   987  C  C   . GLN   A 1 132 ? -20.214 -8.396  -12.305 1.00 50.93  ? 246 GLN   A C   1 
ATOM   988  O  O   . GLN   A 1 132 ? -19.001 -8.454  -12.074 1.00 45.82  ? 246 GLN   A O   1 
ATOM   989  C  CB  . GLN   A 1 132 ? -21.223 -10.640 -12.755 1.00 54.51  ? 246 GLN   A CB  1 
ATOM   990  C  CG  . GLN   A 1 132 ? -19.933 -10.916 -13.522 1.00 54.72  ? 246 GLN   A CG  1 
ATOM   991  C  CD  . GLN   A 1 132 ? -19.099 -12.012 -12.867 1.00 56.28  ? 246 GLN   A CD  1 
ATOM   992  O  OE1 . GLN   A 1 132 ? -19.169 -12.218 -11.651 1.00 63.66  ? 246 GLN   A OE1 1 
ATOM   993  N  NE2 . GLN   A 1 132 ? -18.320 -12.733 -13.673 1.00 55.10  ? 246 GLN   A NE2 1 
ATOM   994  N  N   . CYS   A 1 133 ? -20.766 -7.394  -12.989 1.00 47.76  ? 247 CYS   A N   1 
ATOM   995  C  CA  . CYS   A 1 133 ? -19.989 -6.303  -13.540 1.00 43.57  ? 247 CYS   A CA  1 
ATOM   996  C  C   . CYS   A 1 133 ? -20.657 -4.972  -13.238 1.00 43.99  ? 247 CYS   A C   1 
ATOM   997  O  O   . CYS   A 1 133 ? -21.862 -4.889  -12.989 1.00 45.47  ? 247 CYS   A O   1 
ATOM   998  C  CB  . CYS   A 1 133 ? -19.798 -6.460  -15.055 1.00 45.77  ? 247 CYS   A CB  1 
ATOM   999  S  SG  . CYS   A 1 133 ? -18.950 -7.988  -15.548 1.00 45.78  ? 247 CYS   A SG  1 
ATOM   1000 N  N   . THR   A 1 134 ? -19.844 -3.925  -13.259 1.00 42.16  ? 248 THR   A N   1 
ATOM   1001 C  CA  . THR   A 1 134 ? -20.337 -2.563  -13.154 1.00 40.67  ? 248 THR   A CA  1 
ATOM   1002 C  C   . THR   A 1 134 ? -20.902 -2.157  -14.512 1.00 41.29  ? 248 THR   A C   1 
ATOM   1003 O  O   . THR   A 1 134 ? -20.847 -2.923  -15.479 1.00 38.30  ? 248 THR   A O   1 
ATOM   1004 C  CB  . THR   A 1 134 ? -19.219 -1.628  -12.708 1.00 40.98  ? 248 THR   A CB  1 
ATOM   1005 O  OG1 . THR   A 1 134 ? -18.138 -1.702  -13.648 1.00 39.53  ? 248 THR   A OG1 1 
ATOM   1006 C  CG2 . THR   A 1 134 ? -18.701 -2.039  -11.356 1.00 37.60  ? 248 THR   A CG2 1 
ATOM   1007 N  N   . HIS   A 1 135 ? -21.462 -0.944  -14.599 1.00 39.94  ? 249 HIS   A N   1 
ATOM   1008 C  CA  . HIS   A 1 135 ? -21.858 -0.370  -15.874 1.00 40.07  ? 249 HIS   A CA  1 
ATOM   1009 C  C   . HIS   A 1 135 ? -20.603 0.051   -16.629 1.00 37.08  ? 249 HIS   A C   1 
ATOM   1010 O  O   . HIS   A 1 135 ? -19.484 -0.056  -16.124 1.00 37.56  ? 249 HIS   A O   1 
ATOM   1011 C  CB  . HIS   A 1 135 ? -22.832 0.805   -15.682 1.00 37.96  ? 249 HIS   A CB  1 
ATOM   1012 C  CG  . HIS   A 1 135 ? -22.209 2.044   -15.115 1.00 37.50  ? 249 HIS   A CG  1 
ATOM   1013 N  ND1 . HIS   A 1 135 ? -22.136 2.283   -13.760 1.00 40.37  ? 249 HIS   A ND1 1 
ATOM   1014 C  CD2 . HIS   A 1 135 ? -21.653 3.125   -15.716 1.00 39.61  ? 249 HIS   A CD2 1 
ATOM   1015 C  CE1 . HIS   A 1 135 ? -21.545 3.446   -13.548 1.00 39.54  ? 249 HIS   A CE1 1 
ATOM   1016 N  NE2 . HIS   A 1 135 ? -21.237 3.976   -14.719 1.00 39.32  ? 249 HIS   A NE2 1 
ATOM   1017 N  N   . GLY   A 1 136 ? -20.792 0.530   -17.855 1.00 37.18  ? 250 GLY   A N   1 
ATOM   1018 C  CA  . GLY   A 1 136 ? -19.705 1.010   -18.682 1.00 36.92  ? 250 GLY   A CA  1 
ATOM   1019 C  C   . GLY   A 1 136 ? -19.192 2.355   -18.230 1.00 37.16  ? 250 GLY   A C   1 
ATOM   1020 O  O   . GLY   A 1 136 ? -19.920 3.353   -18.271 1.00 41.89  ? 250 GLY   A O   1 
ATOM   1021 N  N   . ILE   A 1 137 ? -17.945 2.400   -17.774 1.00 35.00  ? 251 ILE   A N   1 
ATOM   1022 C  CA  . ILE   A 1 137 ? -17.354 3.630   -17.267 1.00 36.45  ? 251 ILE   A CA  1 
ATOM   1023 C  C   . ILE   A 1 137 ? -16.306 4.120   -18.260 1.00 37.52  ? 251 ILE   A C   1 
ATOM   1024 O  O   . ILE   A 1 137 ? -15.305 3.434   -18.510 1.00 35.80  ? 251 ILE   A O   1 
ATOM   1025 C  CB  . ILE   A 1 137 ? -16.748 3.436   -15.870 1.00 38.71  ? 251 ILE   A CB  1 
ATOM   1026 C  CG1 . ILE   A 1 137 ? -17.793 2.856   -14.912 1.00 39.20  ? 251 ILE   A CG1 1 
ATOM   1027 C  CG2 . ILE   A 1 137 ? -16.256 4.764   -15.337 1.00 33.78  ? 251 ILE   A CG2 1 
ATOM   1028 C  CD1 . ILE   A 1 137 ? -17.280 2.614   -13.503 1.00 37.93  ? 251 ILE   A CD1 1 
ATOM   1029 N  N   . LYS   A 1 138 ? -16.546 5.304   -18.828 1.00 38.83  ? 252 LYS   A N   1 
ATOM   1030 C  CA  . LYS   A 1 138 ? -15.571 5.988   -19.679 1.00 36.37  ? 252 LYS   A CA  1 
ATOM   1031 C  C   . LYS   A 1 138 ? -14.500 6.658   -18.828 1.00 33.66  ? 252 LYS   A C   1 
ATOM   1032 O  O   . LYS   A 1 138 ? -14.817 7.584   -18.077 1.00 35.93  ? 252 LYS   A O   1 
ATOM   1033 C  CB  . LYS   A 1 138 ? -16.260 7.049   -20.521 1.00 35.80  ? 252 LYS   A CB  1 
ATOM   1034 C  CG  . LYS   A 1 138 ? -16.801 6.580   -21.851 1.00 35.50  ? 252 LYS   A CG  1 
ATOM   1035 C  CD  . LYS   A 1 138 ? -17.655 7.688   -22.480 1.00 33.98  ? 252 LYS   A CD  1 
ATOM   1036 C  CE  . LYS   A 1 138 ? -18.069 7.321   -23.904 1.00 39.72  ? 252 LYS   A CE  1 
ATOM   1037 N  NZ  . LYS   A 1 138 ? -18.114 8.509   -24.826 1.00 39.76  ? 252 LYS   A NZ  1 
ATOM   1038 N  N   . PRO   A 1 139 ? -13.225 6.269   -18.950 1.00 36.39  ? 253 PRO   A N   1 
ATOM   1039 C  CA  . PRO   A 1 139 ? -12.177 6.849   -18.082 1.00 33.37  ? 253 PRO   A CA  1 
ATOM   1040 C  C   . PRO   A 1 139 ? -11.691 8.210   -18.570 1.00 32.34  ? 253 PRO   A C   1 
ATOM   1041 O  O   . PRO   A 1 139 ? -10.603 8.362   -19.108 1.00 29.64  ? 253 PRO   A O   1 
ATOM   1042 C  CB  . PRO   A 1 139 ? -11.067 5.803   -18.163 1.00 31.68  ? 253 PRO   A CB  1 
ATOM   1043 C  CG  . PRO   A 1 139 ? -11.160 5.326   -19.575 1.00 35.47  ? 253 PRO   A CG  1 
ATOM   1044 C  CD  . PRO   A 1 139 ? -12.662 5.268   -19.875 1.00 35.26  ? 253 PRO   A CD  1 
ATOM   1045 N  N   . VAL   A 1 140 ? -12.524 9.228   -18.385 1.00 32.59  ? 254 VAL   A N   1 
ATOM   1046 C  CA  . VAL   A 1 140 ? -12.230 10.573  -18.870 1.00 33.53  ? 254 VAL   A CA  1 
ATOM   1047 C  C   . VAL   A 1 140 ? -11.449 11.337  -17.812 1.00 34.59  ? 254 VAL   A C   1 
ATOM   1048 O  O   . VAL   A 1 140 ? -11.927 11.541  -16.690 1.00 32.79  ? 254 VAL   A O   1 
ATOM   1049 C  CB  . VAL   A 1 140 ? -13.514 11.321  -19.238 1.00 31.77  ? 254 VAL   A CB  1 
ATOM   1050 C  CG1 . VAL   A 1 140 ? -13.164 12.615  -19.929 1.00 34.36  ? 254 VAL   A CG1 1 
ATOM   1051 C  CG2 . VAL   A 1 140 ? -14.360 10.461  -20.126 1.00 33.32  ? 254 VAL   A CG2 1 
ATOM   1052 N  N   . VAL   A 1 141 ? -10.256 11.782  -18.169 1.00 33.97  ? 255 VAL   A N   1 
ATOM   1053 C  CA  . VAL   A 1 141 ? -9.402  12.487  -17.227 1.00 33.02  ? 255 VAL   A CA  1 
ATOM   1054 C  C   . VAL   A 1 141 ? -9.659  13.978  -17.400 1.00 36.26  ? 255 VAL   A C   1 
ATOM   1055 O  O   . VAL   A 1 141 ? -9.577  14.500  -18.517 1.00 39.27  ? 255 VAL   A O   1 
ATOM   1056 C  CB  . VAL   A 1 141 ? -7.928  12.147  -17.463 1.00 35.55  ? 255 VAL   A CB  1 
ATOM   1057 C  CG1 . VAL   A 1 141 ? -7.034  13.107  -16.686 1.00 37.15  ? 255 VAL   A CG1 1 
ATOM   1058 C  CG2 . VAL   A 1 141 ? -7.670  10.705  -17.109 1.00 33.48  ? 255 VAL   A CG2 1 
ATOM   1059 N  N   . SER   A 1 142 ? -10.002 14.662  -16.310 1.00 35.78  ? 256 SER   A N   1 
ATOM   1060 C  CA  . SER   A 1 142 ? -10.265 16.091  -16.399 1.00 39.30  ? 256 SER   A CA  1 
ATOM   1061 C  C   . SER   A 1 142 ? -10.218 16.710  -15.012 1.00 33.43  ? 256 SER   A C   1 
ATOM   1062 O  O   . SER   A 1 142 ? -10.270 16.014  -14.000 1.00 32.39  ? 256 SER   A O   1 
ATOM   1063 C  CB  . SER   A 1 142 ? -11.633 16.384  -17.031 1.00 38.97  ? 256 SER   A CB  1 
ATOM   1064 O  OG  . SER   A 1 142 ? -12.653 16.168  -16.078 1.00 35.35  ? 256 SER   A OG  1 
ATOM   1065 N  N   . THR   A 1 143 ? -10.162 18.037  -14.986 1.00 35.67  ? 257 THR   A N   1 
ATOM   1066 C  CA  . THR   A 1 143 ? -10.196 18.811  -13.757 1.00 35.96  ? 257 THR   A CA  1 
ATOM   1067 C  C   . THR   A 1 143 ? -11.376 19.769  -13.782 1.00 35.90  ? 257 THR   A C   1 
ATOM   1068 O  O   . THR   A 1 143 ? -11.841 20.181  -14.847 1.00 34.44  ? 257 THR   A O   1 
ATOM   1069 C  CB  . THR   A 1 143 ? -8.907  19.612  -13.540 1.00 37.02  ? 257 THR   A CB  1 
ATOM   1070 O  OG1 . THR   A 1 143 ? -8.541  20.306  -14.741 1.00 37.86  ? 257 THR   A OG1 1 
ATOM   1071 C  CG2 . THR   A 1 143 ? -7.773  18.707  -13.133 1.00 35.35  ? 257 THR   A CG2 1 
ATOM   1072 N  N   . GLN   A 1 144 ? -11.824 20.133  -12.581 1.00 38.43  ? 258 GLN   A N   1 
ATOM   1073 C  CA  . GLN   A 1 144 ? -12.953 21.015  -12.301 1.00 36.95  ? 258 GLN   A CA  1 
ATOM   1074 C  C   . GLN   A 1 144 ? -14.282 20.401  -12.732 1.00 35.91  ? 258 GLN   A C   1 
ATOM   1075 O  O   . GLN   A 1 144 ? -15.192 20.239  -11.905 1.00 32.31  ? 258 GLN   A O   1 
ATOM   1076 C  CB  . GLN   A 1 144 ? -12.776 22.394  -12.943 1.00 35.27  ? 258 GLN   A CB  1 
ATOM   1077 C  CG  . GLN   A 1 144 ? -11.399 22.963  -12.843 1.00 36.23  ? 258 GLN   A CG  1 
ATOM   1078 C  CD  . GLN   A 1 144 ? -11.356 24.452  -13.088 1.00 37.61  ? 258 GLN   A CD  1 
ATOM   1079 O  OE1 . GLN   A 1 144 ? -12.262 25.037  -13.700 1.00 38.05  ? 258 GLN   A OE1 1 
ATOM   1080 N  NE2 . GLN   A 1 144 ? -10.284 25.077  -12.628 1.00 36.46  ? 258 GLN   A NE2 1 
ATOM   1081 N  N   . LEU   A 1 145 ? -14.422 20.056  -14.010 1.00 35.60  ? 259 LEU   A N   1 
ATOM   1082 C  CA  . LEU   A 1 145 ? -15.678 19.507  -14.503 1.00 35.94  ? 259 LEU   A CA  1 
ATOM   1083 C  C   . LEU   A 1 145 ? -15.511 18.051  -14.910 1.00 36.87  ? 259 LEU   A C   1 
ATOM   1084 O  O   . LEU   A 1 145 ? -14.531 17.687  -15.576 1.00 37.67  ? 259 LEU   A O   1 
ATOM   1085 C  CB  . LEU   A 1 145 ? -16.242 20.304  -15.689 1.00 36.35  ? 259 LEU   A CB  1 
ATOM   1086 C  CG  . LEU   A 1 145 ? -16.167 21.828  -15.735 1.00 33.98  ? 259 LEU   A CG  1 
ATOM   1087 C  CD1 . LEU   A 1 145 ? -16.201 22.333  -17.175 1.00 36.33  ? 259 LEU   A CD1 1 
ATOM   1088 C  CD2 . LEU   A 1 145 ? -17.295 22.434  -14.926 1.00 36.56  ? 259 LEU   A CD2 1 
ATOM   1089 N  N   . LEU   A 1 146 ? -16.494 17.229  -14.521 1.00 38.13  ? 260 LEU   A N   1 
ATOM   1090 C  CA  . LEU   A 1 146 ? -16.543 15.816  -14.897 1.00 35.24  ? 260 LEU   A CA  1 
ATOM   1091 C  C   . LEU   A 1 146 ? -17.256 15.685  -16.240 1.00 37.15  ? 260 LEU   A C   1 
ATOM   1092 O  O   . LEU   A 1 146 ? -18.397 16.150  -16.401 1.00 35.24  ? 260 LEU   A O   1 
ATOM   1093 C  CB  . LEU   A 1 146 ? -17.244 14.971  -13.829 1.00 33.33  ? 260 LEU   A CB  1 
ATOM   1094 C  CG  . LEU   A 1 146 ? -16.453 14.906  -12.514 1.00 36.03  ? 260 LEU   A CG  1 
ATOM   1095 C  CD1 . LEU   A 1 146 ? -17.328 14.494  -11.336 1.00 35.19  ? 260 LEU   A CD1 1 
ATOM   1096 C  CD2 . LEU   A 1 146 ? -15.222 14.040  -12.648 1.00 31.86  ? 260 LEU   A CD2 1 
ATOM   1097 N  N   . LEU   A 1 147 ? -16.586 15.060  -17.205 1.00 36.56  ? 261 LEU   A N   1 
ATOM   1098 C  CA  . LEU   A 1 147 ? -17.062 15.042  -18.581 1.00 34.70  ? 261 LEU   A CA  1 
ATOM   1099 C  C   . LEU   A 1 147 ? -17.495 13.640  -18.992 1.00 37.03  ? 261 LEU   A C   1 
ATOM   1100 O  O   . LEU   A 1 147 ? -16.831 12.644  -18.676 1.00 34.04  ? 261 LEU   A O   1 
ATOM   1101 C  CB  . LEU   A 1 147 ? -15.995 15.560  -19.558 1.00 32.95  ? 261 LEU   A CB  1 
ATOM   1102 C  CG  . LEU   A 1 147 ? -15.380 16.931  -19.239 1.00 37.53  ? 261 LEU   A CG  1 
ATOM   1103 C  CD1 . LEU   A 1 147 ? -14.123 17.225  -20.081 1.00 39.36  ? 261 LEU   A CD1 1 
ATOM   1104 C  CD2 . LEU   A 1 147 ? -16.411 18.060  -19.344 1.00 33.37  ? 261 LEU   A CD2 1 
ATOM   1105 N  N   . ASN   A 1 148 ? -18.613 13.577  -19.712 1.00 35.15  ? 262 ASN   A N   1 
ATOM   1106 C  CA  . ASN   A 1 148 ? -19.053 12.361  -20.383 1.00 37.48  ? 262 ASN   A CA  1 
ATOM   1107 C  C   . ASN   A 1 148 ? -19.411 11.251  -19.402 1.00 34.06  ? 262 ASN   A C   1 
ATOM   1108 O  O   . ASN   A 1 148 ? -19.347 10.071  -19.744 1.00 35.12  ? 262 ASN   A O   1 
ATOM   1109 C  CB  . ASN   A 1 148 ? -17.994 11.861  -21.367 1.00 37.61  ? 262 ASN   A CB  1 
ATOM   1110 C  CG  . ASN   A 1 148 ? -18.075 12.559  -22.706 1.00 40.50  ? 262 ASN   A CG  1 
ATOM   1111 O  OD1 . ASN   A 1 148 ? -18.961 13.389  -22.938 1.00 36.93  ? 262 ASN   A OD1 1 
ATOM   1112 N  ND2 . ASN   A 1 148 ? -17.155 12.218  -23.605 1.00 40.51  ? 262 ASN   A ND2 1 
ATOM   1113 N  N   . GLY   A 1 149 ? -19.775 11.603  -18.183 1.00 34.68  ? 263 GLY   A N   1 
ATOM   1114 C  CA  . GLY   A 1 149 ? -20.162 10.628  -17.186 1.00 38.00  ? 263 GLY   A CA  1 
ATOM   1115 C  C   . GLY   A 1 149 ? -21.649 10.363  -17.204 1.00 40.67  ? 263 GLY   A C   1 
ATOM   1116 O  O   . GLY   A 1 149 ? -22.355 10.670  -18.170 1.00 38.33  ? 263 GLY   A O   1 
ATOM   1117 N  N   . SER   A 1 150 ? -22.127 9.775   -16.113 1.00 40.17  ? 264 SER   A N   1 
ATOM   1118 C  CA  . SER   A 1 150 ? -23.542 9.492   -15.974 1.00 40.01  ? 264 SER   A CA  1 
ATOM   1119 C  C   . SER   A 1 150 ? -24.209 10.593  -15.158 1.00 38.54  ? 264 SER   A C   1 
ATOM   1120 O  O   . SER   A 1 150 ? -23.560 11.352  -14.436 1.00 39.85  ? 264 SER   A O   1 
ATOM   1121 C  CB  . SER   A 1 150 ? -23.761 8.125   -15.329 1.00 42.65  ? 264 SER   A CB  1 
ATOM   1122 O  OG  . SER   A 1 150 ? -24.265 8.261   -14.017 1.00 47.47  ? 264 SER   A OG  1 
ATOM   1123 N  N   . LEU   A 1 151 ? -25.523 10.686  -15.300 1.00 43.24  ? 265 LEU   A N   1 
ATOM   1124 C  CA  . LEU   A 1 151 ? -26.294 11.736  -14.657 1.00 44.02  ? 265 LEU   A CA  1 
ATOM   1125 C  C   . LEU   A 1 151 ? -27.043 11.174  -13.455 1.00 43.68  ? 265 LEU   A C   1 
ATOM   1126 O  O   . LEU   A 1 151 ? -27.433 9.999   -13.431 1.00 40.53  ? 265 LEU   A O   1 
ATOM   1127 C  CB  . LEU   A 1 151 ? -27.289 12.358  -15.635 1.00 42.51  ? 265 LEU   A CB  1 
ATOM   1128 C  CG  . LEU   A 1 151 ? -26.724 13.210  -16.772 1.00 43.03  ? 265 LEU   A CG  1 
ATOM   1129 C  CD1 . LEU   A 1 151 ? -27.832 13.522  -17.773 1.00 43.66  ? 265 LEU   A CD1 1 
ATOM   1130 C  CD2 . LEU   A 1 151 ? -26.070 14.476  -16.241 1.00 42.47  ? 265 LEU   A CD2 1 
ATOM   1131 N  N   . ALA   A 1 152 ? -27.223 12.039  -12.452 1.00 43.24  ? 266 ALA   A N   1 
ATOM   1132 C  CA  . ALA   A 1 152 ? -28.055 11.727  -11.298 1.00 42.23  ? 266 ALA   A CA  1 
ATOM   1133 C  C   . ALA   A 1 152 ? -29.489 11.499  -11.748 1.00 46.59  ? 266 ALA   A C   1 
ATOM   1134 O  O   . ALA   A 1 152 ? -30.027 12.276  -12.542 1.00 46.47  ? 266 ALA   A O   1 
ATOM   1135 C  CB  . ALA   A 1 152 ? -28.003 12.861  -10.279 1.00 39.20  ? 266 ALA   A CB  1 
ATOM   1136 N  N   . GLU   A 1 153 ? -30.113 10.437  -11.227 1.00 51.76  ? 267 GLU   A N   1 
ATOM   1137 C  CA  . GLU   A 1 153 ? -31.417 10.010  -11.728 1.00 51.20  ? 267 GLU   A CA  1 
ATOM   1138 C  C   . GLU   A 1 153 ? -32.530 10.985  -11.355 1.00 50.89  ? 267 GLU   A C   1 
ATOM   1139 O  O   . GLU   A 1 153 ? -33.447 11.218  -12.154 1.00 49.10  ? 267 GLU   A O   1 
ATOM   1140 C  CB  . GLU   A 1 153 ? -31.735 8.602   -11.217 1.00 55.65  ? 267 GLU   A CB  1 
ATOM   1141 C  CG  . GLU   A 1 153 ? -31.016 7.498   -11.977 1.00 60.87  ? 267 GLU   A CG  1 
ATOM   1142 C  CD  . GLU   A 1 153 ? -29.978 6.773   -11.137 1.00 64.64  ? 267 GLU   A CD  1 
ATOM   1143 O  OE1 . GLU   A 1 153 ? -29.322 7.422   -10.282 1.00 60.40  ? 267 GLU   A OE1 1 
ATOM   1144 O  OE2 . GLU   A 1 153 ? -29.840 5.543   -11.329 1.00 62.37  ? 267 GLU   A OE2 1 
ATOM   1145 N  N   . GLU   A 1 154 ? -32.483 11.559  -10.150 1.00 50.07  ? 268 GLU   A N   1 
ATOM   1146 C  CA  . GLU   A 1 154 ? -33.572 12.394  -9.696  1.00 49.58  ? 268 GLU   A CA  1 
ATOM   1147 C  C   . GLU   A 1 154 ? -32.979 13.784  -9.359  1.00 47.03  ? 268 GLU   A C   1 
ATOM   1148 O  O   . GLU   A 1 154 ? -32.887 14.632  -10.255 1.00 46.02  ? 268 GLU   A O   1 
ATOM   1149 C  CB  . GLU   A 1 154 ? -34.299 11.739  -8.513  1.00 53.94  ? 268 GLU   A CB  1 
ATOM   1150 C  CG  . GLU   A 1 154 ? -35.304 10.594  -8.838  1.00 54.25  ? 268 GLU   A CG  1 
ATOM   1151 C  CD  . GLU   A 1 154 ? -35.842 9.920   -7.565  1.00 60.76  ? 268 GLU   A CD  1 
ATOM   1152 O  OE1 . GLU   A 1 154 ? -35.452 10.344  -6.449  1.00 60.97  ? 268 GLU   A OE1 1 
ATOM   1153 O  OE2 . GLU   A 1 154 ? -36.663 8.979   -7.679  1.00 63.50  ? 268 GLU   A OE2 1 
ATOM   1154 N  N   . GLU   A 1 155 ? -32.586 14.030  -8.124  1.00 52.34  ? 269 GLU   A N   1 
ATOM   1155 C  CA  . GLU   A 1 155 ? -32.098 15.354  -7.756  1.00 47.26  ? 269 GLU   A CA  1 
ATOM   1156 C  C   . GLU   A 1 155 ? -30.623 15.504  -8.086  1.00 42.67  ? 269 GLU   A C   1 
ATOM   1157 O  O   . GLU   A 1 155 ? -29.913 14.536  -8.348  1.00 41.15  ? 269 GLU   A O   1 
ATOM   1158 C  CB  . GLU   A 1 155 ? -32.310 15.593  -6.269  1.00 49.45  ? 269 GLU   A CB  1 
ATOM   1159 C  CG  . GLU   A 1 155 ? -33.695 16.048  -5.974  1.00 53.60  ? 269 GLU   A CG  1 
ATOM   1160 C  CD  . GLU   A 1 155 ? -34.282 15.224  -4.852  1.00 61.15  ? 269 GLU   A CD  1 
ATOM   1161 O  OE1 . GLU   A 1 155 ? -33.655 15.040  -3.785  1.00 59.50  ? 269 GLU   A OE1 1 
ATOM   1162 O  OE2 . GLU   A 1 155 ? -35.335 14.622  -5.107  1.00 59.45  ? 269 GLU   A OE2 1 
ATOM   1163 N  N   . ILE   A 1 156 ? -30.154 16.749  -8.021  1.00 45.14  ? 270 ILE   A N   1 
ATOM   1164 C  CA  . ILE   A 1 156 ? -28.722 16.996  -7.978  1.00 41.61  ? 270 ILE   A CA  1 
ATOM   1165 C  C   . ILE   A 1 156 ? -28.191 16.482  -6.647  1.00 40.87  ? 270 ILE   A C   1 
ATOM   1166 O  O   . ILE   A 1 156 ? -28.779 16.735  -5.587  1.00 40.90  ? 270 ILE   A O   1 
ATOM   1167 C  CB  . ILE   A 1 156 ? -28.431 18.493  -8.155  1.00 40.72  ? 270 ILE   A CB  1 
ATOM   1168 C  CG1 . ILE   A 1 156 ? -28.603 18.890  -9.619  1.00 42.37  ? 270 ILE   A CG1 1 
ATOM   1169 C  CG2 . ILE   A 1 156 ? -26.996 18.796  -7.739  1.00 37.84  ? 270 ILE   A CG2 1 
ATOM   1170 C  CD1 . ILE   A 1 156 ? -28.648 20.360  -9.838  1.00 42.74  ? 270 ILE   A CD1 1 
ATOM   1171 N  N   . ILE   A 1 157 ? -27.092 15.734  -6.694  1.00 36.84  ? 271 ILE   A N   1 
ATOM   1172 C  CA  . ILE   A 1 157 ? -26.515 15.090  -5.517  1.00 41.00  ? 271 ILE   A CA  1 
ATOM   1173 C  C   . ILE   A 1 157 ? -25.209 15.777  -5.149  1.00 34.73  ? 271 ILE   A C   1 
ATOM   1174 O  O   . ILE   A 1 157 ? -24.323 15.923  -5.995  1.00 33.61  ? 271 ILE   A O   1 
ATOM   1175 C  CB  . ILE   A 1 157 ? -26.258 13.596  -5.763  1.00 38.15  ? 271 ILE   A CB  1 
ATOM   1176 C  CG1 . ILE   A 1 157 ? -27.469 12.952  -6.441  1.00 38.79  ? 271 ILE   A CG1 1 
ATOM   1177 C  CG2 . ILE   A 1 157 ? -25.909 12.900  -4.468  1.00 35.47  ? 271 ILE   A CG2 1 
ATOM   1178 C  CD1 . ILE   A 1 157 ? -28.627 12.765  -5.518  1.00 42.19  ? 271 ILE   A CD1 1 
ATOM   1179 N  N   . ILE   A 1 158 ? -25.074 16.153  -3.881  1.00 39.45  ? 272 ILE   A N   1 
ATOM   1180 C  CA  . ILE   A 1 158 ? -23.813 16.635  -3.326  1.00 39.96  ? 272 ILE   A CA  1 
ATOM   1181 C  C   . ILE   A 1 158 ? -23.127 15.463  -2.636  1.00 39.14  ? 272 ILE   A C   1 
ATOM   1182 O  O   . ILE   A 1 158 ? -23.709 14.845  -1.733  1.00 36.87  ? 272 ILE   A O   1 
ATOM   1183 C  CB  . ILE   A 1 158 ? -24.035 17.789  -2.340  1.00 34.28  ? 272 ILE   A CB  1 
ATOM   1184 C  CG1 . ILE   A 1 158 ? -24.933 18.862  -2.971  1.00 38.81  ? 272 ILE   A CG1 1 
ATOM   1185 C  CG2 . ILE   A 1 158 ? -22.707 18.311  -1.882  1.00 38.62  ? 272 ILE   A CG2 1 
ATOM   1186 C  CD1 . ILE   A 1 158 ? -24.299 19.559  -4.160  1.00 39.52  ? 272 ILE   A CD1 1 
ATOM   1187 N  N   . ARG   A 1 159 ? -21.896 15.153  -3.056  1.00 40.88  ? 273 ARG   A N   1 
ATOM   1188 C  CA  . ARG   A 1 159 ? -21.133 14.037  -2.512  1.00 40.64  ? 273 ARG   A CA  1 
ATOM   1189 C  C   . ARG   A 1 159 ? -19.898 14.546  -1.786  1.00 39.65  ? 273 ARG   A C   1 
ATOM   1190 O  O   . ARG   A 1 159 ? -19.196 15.436  -2.274  1.00 43.46  ? 273 ARG   A O   1 
ATOM   1191 C  CB  . ARG   A 1 159 ? -20.710 13.055  -3.610  1.00 39.47  ? 273 ARG   A CB  1 
ATOM   1192 C  CG  . ARG   A 1 159 ? -21.880 12.483  -4.400  1.00 37.31  ? 273 ARG   A CG  1 
ATOM   1193 C  CD  . ARG   A 1 159 ? -21.434 11.533  -5.509  1.00 37.22  ? 273 ARG   A CD  1 
ATOM   1194 N  NE  . ARG   A 1 159 ? -22.509 11.302  -6.464  1.00 36.89  ? 273 ARG   A NE  1 
ATOM   1195 C  CZ  . ARG   A 1 159 ? -23.570 10.545  -6.219  1.00 34.54  ? 273 ARG   A CZ  1 
ATOM   1196 N  NH1 . ARG   A 1 159 ? -23.766 9.990   -5.034  1.00 33.69  ? 273 ARG   A NH1 1 
ATOM   1197 N  NH2 . ARG   A 1 159 ? -24.478 10.373  -7.173  1.00 35.05  ? 273 ARG   A NH2 1 
ATOM   1198 N  N   . SER   A 1 160 ? -19.625 13.951  -0.634  1.00 43.78  ? 274 SER   A N   1 
ATOM   1199 C  CA  . SER   A 1 160 ? -18.537 14.391  0.225   1.00 46.93  ? 274 SER   A CA  1 
ATOM   1200 C  C   . SER   A 1 160 ? -18.306 13.313  1.270   1.00 47.89  ? 274 SER   A C   1 
ATOM   1201 O  O   . SER   A 1 160 ? -19.264 12.826  1.874   1.00 44.50  ? 274 SER   A O   1 
ATOM   1202 C  CB  . SER   A 1 160 ? -18.865 15.730  0.904   1.00 46.66  ? 274 SER   A CB  1 
ATOM   1203 O  OG  . SER   A 1 160 ? -17.719 16.264  1.540   1.00 45.10  ? 274 SER   A OG  1 
ATOM   1204 N  N   . GLU   A 1 161 ? -17.035 12.943  1.474   1.00 47.30  ? 275 GLU   A N   1 
ATOM   1205 C  CA  . GLU   A 1 161 ? -16.708 11.993  2.535   1.00 48.13  ? 275 GLU   A CA  1 
ATOM   1206 C  C   . GLU   A 1 161 ? -17.221 12.488  3.882   1.00 52.14  ? 275 GLU   A C   1 
ATOM   1207 O  O   . GLU   A 1 161 ? -17.575 11.687  4.753   1.00 52.29  ? 275 GLU   A O   1 
ATOM   1208 C  CB  . GLU   A 1 161 ? -15.199 11.772  2.590   1.00 49.00  ? 275 GLU   A CB  1 
ATOM   1209 C  CG  . GLU   A 1 161 ? -14.716 11.077  3.846   1.00 50.48  ? 275 GLU   A CG  1 
ATOM   1210 C  CD  . GLU   A 1 161 ? -13.458 10.255  3.600   1.00 55.55  ? 275 GLU   A CD  1 
ATOM   1211 O  OE1 . GLU   A 1 161 ? -12.528 10.798  2.955   1.00 55.20  ? 275 GLU   A OE1 1 
ATOM   1212 O  OE2 . GLU   A 1 161 ? -13.396 9.084   4.051   1.00 54.18  ? 275 GLU   A OE2 1 
ATOM   1213 N  N   . ASN   A 1 162 ? -17.290 13.804  4.050   1.00 54.62  ? 276 ASN   A N   1 
ATOM   1214 C  CA  . ASN   A 1 162 ? -17.896 14.464  5.196   1.00 56.86  ? 276 ASN   A CA  1 
ATOM   1215 C  C   . ASN   A 1 162 ? -18.073 15.940  4.859   1.00 58.49  ? 276 ASN   A C   1 
ATOM   1216 O  O   . ASN   A 1 162 ? -17.088 16.681  4.756   1.00 57.04  ? 276 ASN   A O   1 
ATOM   1217 C  CB  . ASN   A 1 162 ? -17.044 14.288  6.458   1.00 65.19  ? 276 ASN   A CB  1 
ATOM   1218 C  CG  . ASN   A 1 162 ? -17.735 14.824  7.714   1.00 71.47  ? 276 ASN   A CG  1 
ATOM   1219 O  OD1 . ASN   A 1 162 ? -18.776 15.484  7.628   1.00 69.26  ? 276 ASN   A OD1 1 
ATOM   1220 N  ND2 . ASN   A 1 162 ? -17.164 14.537  8.885   1.00 79.61  ? 276 ASN   A ND2 1 
ATOM   1221 N  N   . LEU   A 1 163 ? -19.326 16.379  4.690   1.00 57.02  ? 277 LEU   A N   1 
ATOM   1222 C  CA  . LEU   A 1 163 ? -19.573 17.747  4.241   1.00 56.14  ? 277 LEU   A CA  1 
ATOM   1223 C  C   . LEU   A 1 163 ? -19.212 18.784  5.295   1.00 59.62  ? 277 LEU   A C   1 
ATOM   1224 O  O   . LEU   A 1 163 ? -19.010 19.954  4.952   1.00 59.14  ? 277 LEU   A O   1 
ATOM   1225 C  CB  . LEU   A 1 163 ? -21.034 17.931  3.830   1.00 53.60  ? 277 LEU   A CB  1 
ATOM   1226 C  CG  . LEU   A 1 163 ? -21.269 18.510  2.436   1.00 49.39  ? 277 LEU   A CG  1 
ATOM   1227 C  CD1 . LEU   A 1 163 ? -22.713 19.004  2.283   1.00 46.30  ? 277 LEU   A CD1 1 
ATOM   1228 C  CD2 . LEU   A 1 163 ? -20.275 19.620  2.172   1.00 48.98  ? 277 LEU   A CD2 1 
ATOM   1229 N  N   . THR   A 1 164 ? -19.140 18.387  6.568   1.00 63.42  ? 278 THR   A N   1 
ATOM   1230 C  CA  . THR   A 1 164 ? -18.694 19.299  7.618   1.00 64.14  ? 278 THR   A CA  1 
ATOM   1231 C  C   . THR   A 1 164 ? -17.208 19.631  7.507   1.00 66.01  ? 278 THR   A C   1 
ATOM   1232 O  O   . THR   A 1 164 ? -16.809 20.769  7.784   1.00 67.35  ? 278 THR   A O   1 
ATOM   1233 C  CB  . THR   A 1 164 ? -19.000 18.709  9.000   1.00 67.67  ? 278 THR   A CB  1 
ATOM   1234 O  OG1 . THR   A 1 164 ? -20.379 18.930  9.332   1.00 65.67  ? 278 THR   A OG1 1 
ATOM   1235 C  CG2 . THR   A 1 164 ? -18.115 19.348  10.060  1.00 77.24  ? 278 THR   A CG2 1 
ATOM   1236 N  N   . ASN   A 1 165 ? -16.380 18.665  7.111   1.00 66.46  ? 279 ASN   A N   1 
ATOM   1237 C  CA  . ASN   A 1 165 ? -14.942 18.888  6.982   1.00 65.07  ? 279 ASN   A CA  1 
ATOM   1238 C  C   . ASN   A 1 165 ? -14.639 19.548  5.636   1.00 64.49  ? 279 ASN   A C   1 
ATOM   1239 O  O   . ASN   A 1 165 ? -14.982 19.008  4.576   1.00 62.46  ? 279 ASN   A O   1 
ATOM   1240 C  CB  . ASN   A 1 165 ? -14.191 17.558  7.132   1.00 65.95  ? 279 ASN   A CB  1 
ATOM   1241 C  CG  . ASN   A 1 165 ? -12.672 17.702  7.009   1.00 65.54  ? 279 ASN   A CG  1 
ATOM   1242 O  OD1 . ASN   A 1 165 ? -12.149 18.767  6.661   1.00 63.57  ? 279 ASN   A OD1 1 
ATOM   1243 N  ND2 . ASN   A 1 165 ? -11.956 16.614  7.306   1.00 66.66  ? 279 ASN   A ND2 1 
ATOM   1244 N  N   . ASN   A 1 166 ? -14.016 20.734  5.691   1.00 64.87  ? 280 ASN   A N   1 
ATOM   1245 C  CA  . ASN   A 1 166 ? -13.683 21.556  4.529   1.00 63.10  ? 280 ASN   A CA  1 
ATOM   1246 C  C   . ASN   A 1 166 ? -12.547 20.984  3.692   1.00 62.81  ? 280 ASN   A C   1 
ATOM   1247 O  O   . ASN   A 1 166 ? -12.290 21.486  2.590   1.00 66.78  ? 280 ASN   A O   1 
ATOM   1248 C  CB  . ASN   A 1 166 ? -13.305 22.968  4.990   1.00 63.51  ? 280 ASN   A CB  1 
ATOM   1249 C  CG  . ASN   A 1 166 ? -12.164 22.961  5.987   1.00 64.52  ? 280 ASN   A CG  1 
ATOM   1250 O  OD1 . ASN   A 1 166 ? -12.394 23.047  7.194   1.00 67.82  ? 280 ASN   A OD1 1 
ATOM   1251 N  ND2 . ASN   A 1 166 ? -10.927 22.833  5.495   1.00 61.42  ? 280 ASN   A ND2 1 
ATOM   1252 N  N   . ALA   A 1 167 ? -11.856 19.968  4.199   1.00 63.98  ? 281 ALA   A N   1 
ATOM   1253 C  CA  . ALA   A 1 167 ? -10.669 19.402  3.576   1.00 62.60  ? 281 ALA   A CA  1 
ATOM   1254 C  C   . ALA   A 1 167 ? -10.999 18.323  2.572   1.00 61.69  ? 281 ALA   A C   1 
ATOM   1255 O  O   . ALA   A 1 167 ? -10.098 17.857  1.862   1.00 61.07  ? 281 ALA   A O   1 
ATOM   1256 C  CB  . ALA   A 1 167 ? -9.750  18.810  4.640   1.00 59.83  ? 281 ALA   A CB  1 
ATOM   1257 N  N   . LYS   A 1 168 ? -12.264 17.940  2.497   1.00 59.21  ? 282 LYS   A N   1 
ATOM   1258 C  CA  . LYS   A 1 168 ? -12.693 16.794  1.725   1.00 57.90  ? 282 LYS   A CA  1 
ATOM   1259 C  C   . LYS   A 1 168 ? -13.392 17.266  0.469   1.00 56.28  ? 282 LYS   A C   1 
ATOM   1260 O  O   . LYS   A 1 168 ? -14.298 18.107  0.524   1.00 55.02  ? 282 LYS   A O   1 
ATOM   1261 C  CB  . LYS   A 1 168 ? -13.617 15.902  2.545   1.00 56.91  ? 282 LYS   A CB  1 
ATOM   1262 C  CG  . LYS   A 1 168 ? -13.080 15.684  3.923   1.00 60.03  ? 282 LYS   A CG  1 
ATOM   1263 C  CD  . LYS   A 1 168 ? -13.665 14.444  4.577   1.00 56.21  ? 282 LYS   A CD  1 
ATOM   1264 C  CE  . LYS   A 1 168 ? -12.692 13.246  4.446   1.00 55.42  ? 282 LYS   A CE  1 
ATOM   1265 N  NZ  . LYS   A 1 168 ? -11.302 13.400  4.975   1.00 54.44  ? 282 LYS   A NZ  1 
ATOM   1266 N  N   . THR   A 1 169 ? -12.968 16.723  -0.656  1.00 52.86  ? 283 THR   A N   1 
ATOM   1267 C  CA  . THR   A 1 169 ? -13.509 17.177  -1.918  1.00 50.62  ? 283 THR   A CA  1 
ATOM   1268 C  C   . THR   A 1 169 ? -15.009 16.924  -2.004  1.00 48.68  ? 283 THR   A C   1 
ATOM   1269 O  O   . THR   A 1 169 ? -15.535 15.986  -1.393  1.00 48.68  ? 283 THR   A O   1 
ATOM   1270 C  CB  . THR   A 1 169 ? -12.803 16.480  -3.058  1.00 46.40  ? 283 THR   A CB  1 
ATOM   1271 O  OG1 . THR   A 1 169 ? -11.843 17.384  -3.607  1.00 50.78  ? 283 THR   A OG1 1 
ATOM   1272 C  CG2 . THR   A 1 169 ? -13.819 16.119  -4.116  1.00 43.62  ? 283 THR   A CG2 1 
ATOM   1273 N  N   . ILE   A 1 170 ? -15.692 17.766  -2.781  1.00 43.23  ? 284 ILE   A N   1 
ATOM   1274 C  CA  . ILE   A 1 170 ? -17.122 17.640  -3.047  1.00 43.26  ? 284 ILE   A CA  1 
ATOM   1275 C  C   . ILE   A 1 170 ? -17.317 17.293  -4.520  1.00 45.18  ? 284 ILE   A C   1 
ATOM   1276 O  O   . ILE   A 1 170 ? -16.688 17.903  -5.397  1.00 43.03  ? 284 ILE   A O   1 
ATOM   1277 C  CB  . ILE   A 1 170 ? -17.875 18.933  -2.696  1.00 44.83  ? 284 ILE   A CB  1 
ATOM   1278 C  CG1 . ILE   A 1 170 ? -18.226 18.967  -1.203  1.00 45.76  ? 284 ILE   A CG1 1 
ATOM   1279 C  CG2 . ILE   A 1 170 ? -19.141 19.035  -3.519  1.00 42.90  ? 284 ILE   A CG2 1 
ATOM   1280 C  CD1 . ILE   A 1 170 ? -18.325 20.371  -0.619  1.00 47.04  ? 284 ILE   A CD1 1 
ATOM   1281 N  N   . ILE   A 1 171 ? -18.181 16.315  -4.791  1.00 42.01  ? 285 ILE   A N   1 
ATOM   1282 C  CA  . ILE   A 1 171 ? -18.556 15.940  -6.150  1.00 37.74  ? 285 ILE   A CA  1 
ATOM   1283 C  C   . ILE   A 1 171 ? -20.013 16.327  -6.330  1.00 38.22  ? 285 ILE   A C   1 
ATOM   1284 O  O   . ILE   A 1 171 ? -20.899 15.802  -5.641  1.00 37.94  ? 285 ILE   A O   1 
ATOM   1285 C  CB  . ILE   A 1 171 ? -18.349 14.446  -6.424  1.00 38.55  ? 285 ILE   A CB  1 
ATOM   1286 C  CG1 . ILE   A 1 171 ? -16.877 14.145  -6.688  1.00 39.92  ? 285 ILE   A CG1 1 
ATOM   1287 C  CG2 . ILE   A 1 171 ? -19.141 14.010  -7.642  1.00 38.57  ? 285 ILE   A CG2 1 
ATOM   1288 C  CD1 . ILE   A 1 171 ? -16.438 12.771  -6.225  1.00 37.98  ? 285 ILE   A CD1 1 
ATOM   1289 N  N   . VAL   A 1 172 ? -20.263 17.267  -7.227  1.00 38.05  ? 286 VAL   A N   1 
ATOM   1290 C  CA  . VAL   A 1 172 ? -21.623 17.657  -7.583  1.00 38.64  ? 286 VAL   A CA  1 
ATOM   1291 C  C   . VAL   A 1 172 ? -22.055 16.777  -8.748  1.00 37.45  ? 286 VAL   A C   1 
ATOM   1292 O  O   . VAL   A 1 172 ? -21.434 16.806  -9.819  1.00 34.59  ? 286 VAL   A O   1 
ATOM   1293 C  CB  . VAL   A 1 172 ? -21.700 19.145  -7.960  1.00 38.38  ? 286 VAL   A CB  1 
ATOM   1294 C  CG1 . VAL   A 1 172 ? -23.040 19.458  -8.590  1.00 32.79  ? 286 VAL   A CG1 1 
ATOM   1295 C  CG2 . VAL   A 1 172 ? -21.408 20.054  -6.741  1.00 36.08  ? 286 VAL   A CG2 1 
ATOM   1296 N  N   . HIS   A 1 173 ? -23.104 15.990  -8.538  1.00 33.91  ? 287 HIS   A N   1 
ATOM   1297 C  CA  . HIS   A 1 173 ? -23.627 15.084  -9.555  1.00 36.90  ? 287 HIS   A CA  1 
ATOM   1298 C  C   . HIS   A 1 173 ? -24.851 15.730  -10.183 1.00 38.08  ? 287 HIS   A C   1 
ATOM   1299 O  O   . HIS   A 1 173 ? -25.943 15.686  -9.612  1.00 37.10  ? 287 HIS   A O   1 
ATOM   1300 C  CB  . HIS   A 1 173 ? -23.993 13.729  -8.961  1.00 35.89  ? 287 HIS   A CB  1 
ATOM   1301 C  CG  . HIS   A 1 173 ? -24.034 12.638  -9.975  1.00 36.48  ? 287 HIS   A CG  1 
ATOM   1302 N  ND1 . HIS   A 1 173 ? -24.248 11.317  -9.649  1.00 37.84  ? 287 HIS   A ND1 1 
ATOM   1303 C  CD2 . HIS   A 1 173 ? -23.851 12.671  -11.314 1.00 36.77  ? 287 HIS   A CD2 1 
ATOM   1304 C  CE1 . HIS   A 1 173 ? -24.207 10.583  -10.746 1.00 39.01  ? 287 HIS   A CE1 1 
ATOM   1305 N  NE2 . HIS   A 1 173 ? -23.967 11.381  -11.771 1.00 37.78  ? 287 HIS   A NE2 1 
ATOM   1306 N  N   . LEU   A 1 174 ? -24.670 16.309  -11.369 1.00 41.00  ? 288 LEU   A N   1 
ATOM   1307 C  CA  . LEU   A 1 174 ? -25.759 16.971  -12.077 1.00 39.88  ? 288 LEU   A CA  1 
ATOM   1308 C  C   . LEU   A 1 174 ? -26.787 15.943  -12.540 1.00 39.98  ? 288 LEU   A C   1 
ATOM   1309 O  O   . LEU   A 1 174 ? -26.437 14.831  -12.951 1.00 41.64  ? 288 LEU   A O   1 
ATOM   1310 C  CB  . LEU   A 1 174 ? -25.200 17.759  -13.273 1.00 36.67  ? 288 LEU   A CB  1 
ATOM   1311 C  CG  . LEU   A 1 174 ? -24.109 18.801  -12.996 1.00 36.00  ? 288 LEU   A CG  1 
ATOM   1312 C  CD1 . LEU   A 1 174 ? -23.837 19.610  -14.241 1.00 36.52  ? 288 LEU   A CD1 1 
ATOM   1313 C  CD2 . LEU   A 1 174 ? -24.516 19.730  -11.850 1.00 35.75  ? 288 LEU   A CD2 1 
ATOM   1314 N  N   . ASN   A 1 175 ? -28.065 16.306  -12.446 1.00 43.59  ? 289 ASN   A N   1 
ATOM   1315 C  CA  . ASN   A 1 175 ? -29.143 15.470  -12.963 1.00 46.52  ? 289 ASN   A CA  1 
ATOM   1316 C  C   . ASN   A 1 175 ? -29.502 15.812  -14.402 1.00 46.80  ? 289 ASN   A C   1 
ATOM   1317 O  O   . ASN   A 1 175 ? -30.503 15.295  -14.920 1.00 48.08  ? 289 ASN   A O   1 
ATOM   1318 C  CB  . ASN   A 1 175 ? -30.397 15.605  -12.096 1.00 44.19  ? 289 ASN   A CB  1 
ATOM   1319 C  CG  . ASN   A 1 175 ? -30.831 17.036  -11.956 1.00 46.63  ? 289 ASN   A CG  1 
ATOM   1320 O  OD1 . ASN   A 1 175 ? -30.180 17.933  -12.492 1.00 46.33  ? 289 ASN   A OD1 1 
ATOM   1321 N  ND2 . ASN   A 1 175 ? -31.938 17.270  -11.243 1.00 48.68  ? 289 ASN   A ND2 1 
ATOM   1322 N  N   . LYS   A 1 176 ? -28.732 16.687  -15.045 1.00 46.29  ? 290 LYS   A N   1 
ATOM   1323 C  CA  . LYS   A 1 176 ? -28.949 17.020  -16.446 1.00 47.08  ? 290 LYS   A CA  1 
ATOM   1324 C  C   . LYS   A 1 176 ? -27.660 17.617  -16.993 1.00 46.55  ? 290 LYS   A C   1 
ATOM   1325 O  O   . LYS   A 1 176 ? -26.988 18.404  -16.314 1.00 43.84  ? 290 LYS   A O   1 
ATOM   1326 C  CB  . LYS   A 1 176 ? -30.156 17.965  -16.608 1.00 52.39  ? 290 LYS   A CB  1 
ATOM   1327 C  CG  . LYS   A 1 176 ? -29.968 19.228  -17.438 1.00 60.63  ? 290 LYS   A CG  1 
ATOM   1328 C  CD  . LYS   A 1 176 ? -30.992 20.256  -16.954 1.00 77.60  ? 290 LYS   A CD  1 
ATOM   1329 C  CE  . LYS   A 1 176 ? -30.954 21.551  -17.731 1.00 85.25  ? 290 LYS   A CE  1 
ATOM   1330 N  NZ  . LYS   A 1 176 ? -30.150 21.411  -18.963 1.00 73.09  ? 290 LYS   A NZ  1 
ATOM   1331 N  N   . SER   A 1 177 ? -27.305 17.209  -18.207 1.00 42.38  ? 291 SER   A N   1 
ATOM   1332 C  CA  . SER   A 1 177 ? -26.007 17.530  -18.771 1.00 45.85  ? 291 SER   A CA  1 
ATOM   1333 C  C   . SER   A 1 177 ? -26.052 18.859  -19.520 1.00 46.77  ? 291 SER   A C   1 
ATOM   1334 O  O   . SER   A 1 177 ? -27.083 19.262  -20.066 1.00 47.67  ? 291 SER   A O   1 
ATOM   1335 C  CB  . SER   A 1 177 ? -25.525 16.406  -19.697 1.00 45.41  ? 291 SER   A CB  1 
ATOM   1336 O  OG  . SER   A 1 177 ? -26.353 16.247  -20.835 1.00 47.68  ? 291 SER   A OG  1 
ATOM   1337 N  N   . VAL   A 1 178 ? -24.911 19.543  -19.533 1.00 43.08  ? 292 VAL   A N   1 
ATOM   1338 C  CA  . VAL   A 1 178 ? -24.748 20.809  -20.237 1.00 44.66  ? 292 VAL   A CA  1 
ATOM   1339 C  C   . VAL   A 1 178 ? -23.622 20.617  -21.249 1.00 44.53  ? 292 VAL   A C   1 
ATOM   1340 O  O   . VAL   A 1 178 ? -22.468 20.443  -20.831 1.00 43.42  ? 292 VAL   A O   1 
ATOM   1341 C  CB  . VAL   A 1 178 ? -24.420 21.959  -19.270 1.00 43.77  ? 292 VAL   A CB  1 
ATOM   1342 C  CG1 . VAL   A 1 178 ? -24.288 23.259  -20.050 1.00 42.01  ? 292 VAL   A CG1 1 
ATOM   1343 C  CG2 . VAL   A 1 178 ? -25.481 22.077  -18.184 1.00 39.94  ? 292 VAL   A CG2 1 
ATOM   1344 N  N   . GLU   A 1 179 ? -23.938 20.641  -22.546 1.00 47.77  ? 293 GLU   A N   1 
ATOM   1345 C  CA  . GLU   A 1 179 ? -22.919 20.374  -23.601 1.00 45.42  ? 293 GLU   A CA  1 
ATOM   1346 C  C   . GLU   A 1 179 ? -21.875 21.495  -23.704 1.00 42.91  ? 293 GLU   A C   1 
ATOM   1347 O  O   . GLU   A 1 179 ? -22.273 22.674  -23.780 1.00 41.78  ? 293 GLU   A O   1 
ATOM   1348 C  CB  . GLU   A 1 179 ? -23.604 20.151  -24.952 1.00 49.68  ? 293 GLU   A CB  1 
ATOM   1349 C  CG  . GLU   A 1 179 ? -23.182 21.150  -26.014 1.00 58.30  ? 293 GLU   A CG  1 
ATOM   1350 C  CD  . GLU   A 1 179 ? -23.534 20.747  -27.436 1.00 66.66  ? 293 GLU   A CD  1 
ATOM   1351 O  OE1 . GLU   A 1 179 ? -22.852 19.859  -27.983 1.00 68.68  ? 293 GLU   A OE1 1 
ATOM   1352 O  OE2 . GLU   A 1 179 ? -24.490 21.323  -27.992 1.00 69.18  ? 293 GLU   A OE2 1 
ATOM   1353 N  N   . ILE   A 1 180 ? -20.587 21.120  -23.706 1.00 40.84  ? 294 ILE   A N   1 
ATOM   1354 C  CA  . ILE   A 1 180 ? -19.486 22.049  -23.892 1.00 39.38  ? 294 ILE   A CA  1 
ATOM   1355 C  C   . ILE   A 1 180 ? -18.727 21.605  -25.140 1.00 37.90  ? 294 ILE   A C   1 
ATOM   1356 O  O   . ILE   A 1 180 ? -18.380 20.430  -25.271 1.00 36.42  ? 294 ILE   A O   1 
ATOM   1357 C  CB  . ILE   A 1 180 ? -18.569 22.056  -22.659 1.00 37.67  ? 294 ILE   A CB  1 
ATOM   1358 C  CG1 . ILE   A 1 180 ? -17.469 23.112  -22.807 1.00 37.60  ? 294 ILE   A CG1 1 
ATOM   1359 C  CG2 . ILE   A 1 180 ? -18.029 20.647  -22.428 1.00 35.66  ? 294 ILE   A CG2 1 
ATOM   1360 C  CD1 . ILE   A 1 180 ? -16.562 23.224  -21.615 1.00 35.34  ? 294 ILE   A CD1 1 
ATOM   1361 N  N   . ASN   A 1 181 ? -18.478 22.528  -26.061 1.00 38.90  ? 295 ASN   A N   1 
ATOM   1362 C  CA  . ASN   A 1 181 ? -17.949 22.194  -27.382 1.00 37.29  ? 295 ASN   A CA  1 
ATOM   1363 C  C   . ASN   A 1 181 ? -16.592 22.869  -27.578 1.00 38.15  ? 295 ASN   A C   1 
ATOM   1364 O  O   . ASN   A 1 181 ? -16.527 24.074  -27.834 1.00 41.03  ? 295 ASN   A O   1 
ATOM   1365 C  CB  . ASN   A 1 181 ? -18.950 22.615  -28.457 1.00 38.03  ? 295 ASN   A CB  1 
ATOM   1366 C  CG  . ASN   A 1 181 ? -18.416 22.436  -29.848 1.00 39.26  ? 295 ASN   A CG  1 
ATOM   1367 O  OD1 . ASN   A 1 181 ? -17.426 21.740  -30.058 1.00 41.32  ? 295 ASN   A OD1 1 
ATOM   1368 N  ND2 . ASN   A 1 181 ? -19.071 23.049  -30.815 1.00 40.53  ? 295 ASN   A ND2 1 
ATOM   1369 N  N   . CYS   A 1 182 ? -15.507 22.105  -27.478 1.00 36.74  ? 296 CYS   A N   1 
ATOM   1370 C  CA  . CYS   A 1 182 ? -14.157 22.668  -27.501 1.00 37.90  ? 296 CYS   A CA  1 
ATOM   1371 C  C   . CYS   A 1 182 ? -13.494 22.441  -28.855 1.00 39.30  ? 296 CYS   A C   1 
ATOM   1372 O  O   . CYS   A 1 182 ? -13.540 21.331  -29.400 1.00 35.89  ? 296 CYS   A O   1 
ATOM   1373 C  CB  . CYS   A 1 182 ? -13.321 22.060  -26.380 1.00 35.17  ? 296 CYS   A CB  1 
ATOM   1374 S  SG  . CYS   A 1 182 ? -14.141 22.332  -24.783 1.00 37.43  ? 296 CYS   A SG  1 
ATOM   1375 N  N   . THR   A 1 183 ? -12.884 23.495  -29.399 1.00 39.60  ? 297 THR   A N   1 
ATOM   1376 C  CA  . THR   A 1 183 ? -12.336 23.441  -30.745 1.00 36.31  ? 297 THR   A CA  1 
ATOM   1377 C  C   . THR   A 1 183 ? -10.989 24.142  -30.792 1.00 38.59  ? 297 THR   A C   1 
ATOM   1378 O  O   . THR   A 1 183 ? -10.786 25.155  -30.119 1.00 40.45  ? 297 THR   A O   1 
ATOM   1379 C  CB  . THR   A 1 183 ? -13.322 24.059  -31.751 1.00 39.63  ? 297 THR   A CB  1 
ATOM   1380 O  OG1 . THR   A 1 183 ? -14.603 23.419  -31.627 1.00 39.99  ? 297 THR   A OG1 1 
ATOM   1381 C  CG2 . THR   A 1 183 ? -12.828 23.916  -33.158 1.00 41.85  ? 297 THR   A CG2 1 
ATOM   1382 N  N   . ARG   A 1 184 ? -10.074 23.586  -31.595 1.00 39.45  ? 298 ARG   A N   1 
ATOM   1383 C  CA  . ARG   A 1 184 ? -8.803  24.208  -31.966 1.00 39.42  ? 298 ARG   A CA  1 
ATOM   1384 C  C   . ARG   A 1 184 ? -8.816  24.190  -33.488 1.00 44.06  ? 298 ARG   A C   1 
ATOM   1385 O  O   . ARG   A 1 184 ? -8.446  23.184  -34.115 1.00 41.19  ? 298 ARG   A O   1 
ATOM   1386 C  CB  . ARG   A 1 184 ? -7.597  23.453  -31.403 1.00 39.97  ? 298 ARG   A CB  1 
ATOM   1387 C  CG  . ARG   A 1 184 ? -6.220  24.166  -31.545 1.00 38.07  ? 298 ARG   A CG  1 
ATOM   1388 C  CD  . ARG   A 1 184 ? -5.950  24.728  -32.956 1.00 40.38  ? 298 ARG   A CD  1 
ATOM   1389 N  NE  . ARG   A 1 184 ? -5.676  23.673  -33.923 1.00 39.66  ? 298 ARG   A NE  1 
ATOM   1390 C  CZ  . ARG   A 1 184 ? -4.483  23.130  -34.118 1.00 40.41  ? 298 ARG   A CZ  1 
ATOM   1391 N  NH1 . ARG   A 1 184 ? -3.425  23.520  -33.428 1.00 41.76  ? 298 ARG   A NH1 1 
ATOM   1392 N  NH2 . ARG   A 1 184 ? -4.353  22.154  -35.011 1.00 45.18  ? 298 ARG   A NH2 1 
ATOM   1393 N  N   . PRO   A 1 185 ? -9.259  25.267  -34.123 1.00 45.55  ? 299 PRO   A N   1 
ATOM   1394 C  CA  . PRO   A 1 185 ? -9.520  25.226  -35.567 1.00 44.87  ? 299 PRO   A CA  1 
ATOM   1395 C  C   . PRO   A 1 185 ? -8.245  25.021  -36.371 1.00 48.04  ? 299 PRO   A C   1 
ATOM   1396 O  O   . PRO   A 1 185 ? -7.132  24.999  -35.838 1.00 48.75  ? 299 PRO   A O   1 
ATOM   1397 C  CB  . PRO   A 1 185 ? -10.154 26.592  -35.854 1.00 44.02  ? 299 PRO   A CB  1 
ATOM   1398 C  CG  . PRO   A 1 185 ? -9.804  27.436  -34.659 1.00 48.37  ? 299 PRO   A CG  1 
ATOM   1399 C  CD  . PRO   A 1 185 ? -9.750  26.501  -33.497 1.00 42.64  ? 299 PRO   A CD  1 
ATOM   1400 N  N   . SER   A 1 186 ? -8.422  24.859  -37.680 1.00 50.58  ? 300 SER   A N   1 
ATOM   1401 C  CA  . SER   A 1 186 ? -7.327  24.414  -38.528 1.00 52.63  ? 300 SER   A CA  1 
ATOM   1402 C  C   . SER   A 1 186 ? -6.527  25.613  -39.043 1.00 53.91  ? 300 SER   A C   1 
ATOM   1403 O  O   . SER   A 1 186 ? -6.880  26.774  -38.811 1.00 53.72  ? 300 SER   A O   1 
ATOM   1404 C  CB  . SER   A 1 186 ? -7.874  23.570  -39.680 1.00 53.82  ? 300 SER   A CB  1 
ATOM   1405 O  OG  . SER   A 1 186 ? -9.292  23.654  -39.689 1.00 55.21  ? 300 SER   A OG  1 
ATOM   1406 N  N   . ASN   A 1 187 ? -5.428  25.320  -39.735 1.00 55.71  ? 301 ASN   A N   1 
ATOM   1407 C  CA  . ASN   A 1 187 ? -4.524  26.352  -40.247 1.00 55.83  ? 301 ASN   A CA  1 
ATOM   1408 C  C   . ASN   A 1 187 ? -3.983  27.228  -39.121 1.00 56.15  ? 301 ASN   A C   1 
ATOM   1409 O  O   . ASN   A 1 187 ? -2.792  27.189  -38.801 1.00 57.04  ? 301 ASN   A O   1 
ATOM   1410 C  CB  . ASN   A 1 187 ? -5.220  27.235  -41.292 1.00 58.72  ? 301 ASN   A CB  1 
ATOM   1411 C  CG  . ASN   A 1 187 ? -6.053  26.437  -42.292 1.00 63.48  ? 301 ASN   A CG  1 
ATOM   1412 O  OD1 . ASN   A 1 187 ? -5.632  25.381  -42.771 1.00 67.39  ? 301 ASN   A OD1 1 
ATOM   1413 N  ND2 . ASN   A 1 187 ? -7.224  26.967  -42.642 1.00 57.98  ? 301 ASN   A ND2 1 
ATOM   1414 N  N   . SER   A 1 192 ? 0.605   26.106  -39.798 1.00 54.45  ? 322 SER   A N   1 
ATOM   1415 C  CA  . SER   A 1 192 ? 1.606   26.957  -40.434 1.00 59.36  ? 322 SER   A CA  1 
ATOM   1416 C  C   . SER   A 1 192 ? 1.059   28.369  -40.640 1.00 60.40  ? 322 SER   A C   1 
ATOM   1417 O  O   . SER   A 1 192 ? 0.755   28.786  -41.761 1.00 60.36  ? 322 SER   A O   1 
ATOM   1418 C  CB  . SER   A 1 192 ? 2.059   26.356  -41.770 1.00 62.56  ? 322 SER   A CB  1 
ATOM   1419 O  OG  . SER   A 1 192 ? 2.411   27.367  -42.700 1.00 62.25  ? 322 SER   A OG  1 
ATOM   1420 N  N   . GLY   A 1 193 ? 0.946   29.107  -39.544 1.00 58.92  ? 323 GLY   A N   1 
ATOM   1421 C  CA  . GLY   A 1 193 ? 0.359   30.429  -39.585 1.00 54.39  ? 323 GLY   A CA  1 
ATOM   1422 C  C   . GLY   A 1 193 ? -0.479  30.674  -38.352 1.00 50.33  ? 323 GLY   A C   1 
ATOM   1423 O  O   . GLY   A 1 193 ? -1.520  30.033  -38.170 1.00 49.11  ? 323 GLY   A O   1 
ATOM   1424 N  N   . GLY   A 1 194 ? -0.023  31.582  -37.488 1.00 47.56  ? 324 GLY   A N   1 
ATOM   1425 C  CA  . GLY   A 1 194 ? -0.734  31.893  -36.266 1.00 47.65  ? 324 GLY   A CA  1 
ATOM   1426 C  C   . GLY   A 1 194 ? -0.368  30.966  -35.134 1.00 49.51  ? 324 GLY   A C   1 
ATOM   1427 O  O   . GLY   A 1 194 ? 0.416   30.023  -35.286 1.00 50.50  ? 324 GLY   A O   1 
ATOM   1428 N  N   . ASP   A 1 195 ? -0.937  31.261  -33.959 1.00 46.34  ? 325 ASP   A N   1 
ATOM   1429 C  CA  . ASP   A 1 195 ? -0.730  30.444  -32.761 1.00 43.74  ? 325 ASP   A CA  1 
ATOM   1430 C  C   . ASP   A 1 195 ? -1.619  29.213  -32.834 1.00 43.55  ? 325 ASP   A C   1 
ATOM   1431 O  O   . ASP   A 1 195 ? -2.800  29.261  -32.480 1.00 38.96  ? 325 ASP   A O   1 
ATOM   1432 C  CB  . ASP   A 1 195 ? -1.028  31.223  -31.488 1.00 47.51  ? 325 ASP   A CB  1 
ATOM   1433 C  CG  . ASP   A 1 195 ? -0.506  30.508  -30.242 1.00 47.69  ? 325 ASP   A CG  1 
ATOM   1434 O  OD1 . ASP   A 1 195 ? -0.345  29.270  -30.312 1.00 41.57  ? 325 ASP   A OD1 1 
ATOM   1435 O  OD2 . ASP   A 1 195 ? -0.299  31.161  -29.195 1.00 47.56  ? 325 ASP   A OD2 1 
ATOM   1436 N  N   . ILE   A 1 196 ? -1.037  28.097  -33.266 1.00 42.21  ? 326 ILE   A N   1 
ATOM   1437 C  CA  . ILE   A 1 196 ? -1.754  26.839  -33.424 1.00 43.39  ? 326 ILE   A CA  1 
ATOM   1438 C  C   . ILE   A 1 196 ? -2.153  26.246  -32.071 1.00 41.59  ? 326 ILE   A C   1 
ATOM   1439 O  O   . ILE   A 1 196 ? -2.830  25.215  -32.013 1.00 38.68  ? 326 ILE   A O   1 
ATOM   1440 C  CB  . ILE   A 1 196 ? -0.897  25.858  -34.241 1.00 44.36  ? 326 ILE   A CB  1 
ATOM   1441 C  CG1 . ILE   A 1 196 ? 0.395   25.537  -33.508 1.00 42.79  ? 326 ILE   A CG1 1 
ATOM   1442 C  CG2 . ILE   A 1 196 ? -0.559  26.457  -35.608 1.00 45.31  ? 326 ILE   A CG2 1 
ATOM   1443 C  CD1 . ILE   A 1 196 ? 1.540   25.279  -34.444 1.00 47.74  ? 326 ILE   A CD1 1 
ATOM   1444 N  N   . ARG   A 1 197 ? -1.755  26.893  -30.974 1.00 41.42  ? 327 ARG   A N   1 
ATOM   1445 C  CA  . ARG   A 1 197 ? -2.117  26.426  -29.642 1.00 41.36  ? 327 ARG   A CA  1 
ATOM   1446 C  C   . ARG   A 1 197 ? -3.404  27.055  -29.125 1.00 41.11  ? 327 ARG   A C   1 
ATOM   1447 O  O   . ARG   A 1 197 ? -4.068  26.462  -28.270 1.00 39.17  ? 327 ARG   A O   1 
ATOM   1448 C  CB  . ARG   A 1 197 ? -0.966  26.712  -28.672 1.00 41.61  ? 327 ARG   A CB  1 
ATOM   1449 C  CG  . ARG   A 1 197 ? -0.182  25.464  -28.304 1.00 42.17  ? 327 ARG   A CG  1 
ATOM   1450 C  CD  . ARG   A 1 197 ? 1.246   25.807  -27.914 1.00 41.11  ? 327 ARG   A CD  1 
ATOM   1451 N  NE  . ARG   A 1 197 ? 2.218   25.210  -28.826 1.00 42.33  ? 327 ARG   A NE  1 
ATOM   1452 C  CZ  . ARG   A 1 197 ? 2.696   25.802  -29.915 1.00 44.48  ? 327 ARG   A CZ  1 
ATOM   1453 N  NH1 . ARG   A 1 197 ? 2.330   27.031  -30.260 1.00 46.63  ? 327 ARG   A NH1 1 
ATOM   1454 N  NH2 . ARG   A 1 197 ? 3.583   25.155  -30.665 1.00 43.62  ? 327 ARG   A NH2 1 
ATOM   1455 N  N   . LYS   A 1 198 ? -3.780  28.221  -29.647 1.00 40.71  ? 328 LYS   A N   1 
ATOM   1456 C  CA  . LYS   A 1 198 ? -5.024  28.860  -29.247 1.00 40.83  ? 328 LYS   A CA  1 
ATOM   1457 C  C   . LYS   A 1 198 ? -6.190  27.922  -29.520 1.00 43.18  ? 328 LYS   A C   1 
ATOM   1458 O  O   . LYS   A 1 198 ? -6.289  27.341  -30.607 1.00 40.86  ? 328 LYS   A O   1 
ATOM   1459 C  CB  . LYS   A 1 198 ? -5.210  30.163  -30.019 1.00 45.17  ? 328 LYS   A CB  1 
ATOM   1460 C  CG  . LYS   A 1 198 ? -5.072  31.422  -29.180 1.00 44.93  ? 328 LYS   A CG  1 
ATOM   1461 C  CD  . LYS   A 1 198 ? -4.516  32.551  -30.043 1.00 40.70  ? 328 LYS   A CD  1 
ATOM   1462 C  CE  . LYS   A 1 198 ? -3.145  33.029  -29.550 1.00 45.58  ? 328 LYS   A CE  1 
ATOM   1463 N  NZ  . LYS   A 1 198 ? -3.040  34.516  -29.494 1.00 46.81  ? 328 LYS   A NZ  1 
ATOM   1464 N  N   . ALA   A 1 199 ? -7.074  27.776  -28.530 1.00 42.06  ? 329 ALA   A N   1 
ATOM   1465 C  CA  . ALA   A 1 199 ? -8.282  26.961  -28.652 1.00 42.12  ? 329 ALA   A CA  1 
ATOM   1466 C  C   . ALA   A 1 199 ? -9.423  27.667  -27.925 1.00 41.40  ? 329 ALA   A C   1 
ATOM   1467 O  O   . ALA   A 1 199 ? -9.215  28.691  -27.266 1.00 38.33  ? 329 ALA   A O   1 
ATOM   1468 C  CB  . ALA   A 1 199 ? -8.073  25.548  -28.078 1.00 38.39  ? 329 ALA   A CB  1 
ATOM   1469 N  N   . TYR   A 1 200 ? -10.631 27.093  -28.006 1.00 39.92  ? 330 TYR   A N   1 
ATOM   1470 C  CA  . TYR   A 1 200 ? -11.778 27.634  -27.277 1.00 40.73  ? 330 TYR   A CA  1 
ATOM   1471 C  C   . TYR   A 1 200 ? -12.871 26.575  -27.087 1.00 41.15  ? 330 TYR   A C   1 
ATOM   1472 O  O   . TYR   A 1 200 ? -13.009 25.643  -27.887 1.00 37.01  ? 330 TYR   A O   1 
ATOM   1473 C  CB  . TYR   A 1 200 ? -12.357 28.863  -27.988 1.00 40.56  ? 330 TYR   A CB  1 
ATOM   1474 C  CG  . TYR   A 1 200 ? -12.988 28.568  -29.332 1.00 42.17  ? 330 TYR   A CG  1 
ATOM   1475 C  CD1 . TYR   A 1 200 ? -14.279 28.059  -29.424 1.00 42.14  ? 330 TYR   A CD1 1 
ATOM   1476 C  CD2 . TYR   A 1 200 ? -12.289 28.789  -30.509 1.00 43.67  ? 330 TYR   A CD2 1 
ATOM   1477 C  CE1 . TYR   A 1 200 ? -14.854 27.784  -30.645 1.00 44.29  ? 330 TYR   A CE1 1 
ATOM   1478 C  CE2 . TYR   A 1 200 ? -12.858 28.513  -31.742 1.00 41.41  ? 330 TYR   A CE2 1 
ATOM   1479 C  CZ  . TYR   A 1 200 ? -14.138 28.013  -31.804 1.00 43.17  ? 330 TYR   A CZ  1 
ATOM   1480 O  OH  . TYR   A 1 200 ? -14.702 27.742  -33.028 1.00 46.61  ? 330 TYR   A OH  1 
ATOM   1481 N  N   . CYS   A 1 201 ? -13.637 26.735  -26.006 1.00 37.23  ? 331 CYS   A N   1 
ATOM   1482 C  CA  . CYS   A 1 201 ? -14.837 25.952  -25.728 1.00 38.46  ? 331 CYS   A CA  1 
ATOM   1483 C  C   . CYS   A 1 201 ? -16.033 26.891  -25.718 1.00 43.08  ? 331 CYS   A C   1 
ATOM   1484 O  O   . CYS   A 1 201 ? -15.959 27.989  -25.152 1.00 41.37  ? 331 CYS   A O   1 
ATOM   1485 C  CB  . CYS   A 1 201 ? -14.770 25.247  -24.375 1.00 36.70  ? 331 CYS   A CB  1 
ATOM   1486 S  SG  . CYS   A 1 201 ? -13.419 24.123  -24.145 1.00 34.64  ? 331 CYS   A SG  1 
ATOM   1487 N  N   . GLU   A 1 202 ? -17.135 26.454  -26.315 1.00 39.97  ? 332 GLU   A N   1 
ATOM   1488 C  CA  . GLU   A 1 202 ? -18.364 27.231  -26.341 1.00 43.26  ? 332 GLU   A CA  1 
ATOM   1489 C  C   . GLU   A 1 202 ? -19.403 26.549  -25.463 1.00 42.16  ? 332 GLU   A C   1 
ATOM   1490 O  O   . GLU   A 1 202 ? -19.557 25.324  -25.508 1.00 42.30  ? 332 GLU   A O   1 
ATOM   1491 C  CB  . GLU   A 1 202 ? -18.869 27.394  -27.774 1.00 46.10  ? 332 GLU   A CB  1 
ATOM   1492 C  CG  . GLU   A 1 202 ? -18.068 28.437  -28.559 1.00 51.26  ? 332 GLU   A CG  1 
ATOM   1493 C  CD  . GLU   A 1 202 ? -18.611 28.682  -29.957 1.00 60.21  ? 332 GLU   A CD  1 
ATOM   1494 O  OE1 . GLU   A 1 202 ? -18.249 29.719  -30.559 1.00 62.29  ? 332 GLU   A OE1 1 
ATOM   1495 O  OE2 . GLU   A 1 202 ? -19.387 27.832  -30.455 1.00 62.02  ? 332 GLU   A OE2 1 
ATOM   1496 N  N   . ILE   A 1 203 ? -20.084 27.336  -24.639 1.00 44.57  ? 333 ILE   A N   1 
ATOM   1497 C  CA  . ILE   A 1 203 ? -21.086 26.825  -23.715 1.00 45.68  ? 333 ILE   A CA  1 
ATOM   1498 C  C   . ILE   A 1 203 ? -22.309 27.720  -23.809 1.00 43.15  ? 333 ILE   A C   1 
ATOM   1499 O  O   . ILE   A 1 203 ? -22.197 28.919  -24.077 1.00 43.94  ? 333 ILE   A O   1 
ATOM   1500 C  CB  . ILE   A 1 203 ? -20.536 26.757  -22.271 1.00 44.87  ? 333 ILE   A CB  1 
ATOM   1501 C  CG1 . ILE   A 1 203 ? -19.432 25.703  -22.175 1.00 42.97  ? 333 ILE   A CG1 1 
ATOM   1502 C  CG2 . ILE   A 1 203 ? -21.616 26.420  -21.268 1.00 44.31  ? 333 ILE   A CG2 1 
ATOM   1503 C  CD1 . ILE   A 1 203 ? -19.313 25.111  -20.771 1.00 45.87  ? 333 ILE   A CD1 1 
ATOM   1504 N  N   . ASN   A 1 204 ? -23.483 27.123  -23.620 1.00 42.35  ? 334 ASN   A N   1 
ATOM   1505 C  CA  . ASN   A 1 204 ? -24.704 27.906  -23.497 1.00 46.17  ? 334 ASN   A CA  1 
ATOM   1506 C  C   . ASN   A 1 204 ? -24.742 28.506  -22.095 1.00 44.74  ? 334 ASN   A C   1 
ATOM   1507 O  O   . ASN   A 1 204 ? -24.790 27.775  -21.103 1.00 43.55  ? 334 ASN   A O   1 
ATOM   1508 C  CB  . ASN   A 1 204 ? -25.931 27.039  -23.782 1.00 49.03  ? 334 ASN   A CB  1 
ATOM   1509 C  CG  . ASN   A 1 204 ? -27.232 27.824  -23.719 1.00 48.81  ? 334 ASN   A CG  1 
ATOM   1510 O  OD1 . ASN   A 1 204 ? -27.318 28.860  -23.055 1.00 48.55  ? 334 ASN   A OD1 1 
ATOM   1511 N  ND2 . ASN   A 1 204 ? -28.247 27.336  -24.413 1.00 48.93  ? 334 ASN   A ND2 1 
ATOM   1512 N  N   . GLY   A 1 205 ? -24.675 29.834  -22.014 1.00 47.10  ? 335 GLY   A N   1 
ATOM   1513 C  CA  . GLY   A 1 205 ? -24.672 30.485  -20.717 1.00 48.01  ? 335 GLY   A CA  1 
ATOM   1514 C  C   . GLY   A 1 205 ? -26.010 30.382  -20.018 1.00 48.26  ? 335 GLY   A C   1 
ATOM   1515 O  O   . GLY   A 1 205 ? -26.070 30.216  -18.798 1.00 46.02  ? 335 GLY   A O   1 
ATOM   1516 N  N   . THR   A 1 206 ? -27.103 30.478  -20.782 1.00 49.04  ? 336 THR   A N   1 
ATOM   1517 C  CA  . THR   A 1 206 ? -28.424 30.298  -20.188 1.00 50.31  ? 336 THR   A CA  1 
ATOM   1518 C  C   . THR   A 1 206 ? -28.570 28.909  -19.578 1.00 48.39  ? 336 THR   A C   1 
ATOM   1519 O  O   . THR   A 1 206 ? -28.967 28.778  -18.415 1.00 45.94  ? 336 THR   A O   1 
ATOM   1520 C  CB  . THR   A 1 206 ? -29.528 30.570  -21.214 1.00 52.57  ? 336 THR   A CB  1 
ATOM   1521 O  OG1 . THR   A 1 206 ? -29.637 31.985  -21.440 1.00 53.85  ? 336 THR   A OG1 1 
ATOM   1522 C  CG2 . THR   A 1 206 ? -30.857 30.034  -20.713 1.00 50.63  ? 336 THR   A CG2 1 
ATOM   1523 N  N   . LYS   A 1 207 ? -28.242 27.860  -20.338 1.00 48.45  ? 337 LYS   A N   1 
ATOM   1524 C  CA  . LYS   A 1 207 ? -28.302 26.506  -19.792 1.00 48.54  ? 337 LYS   A CA  1 
ATOM   1525 C  C   . LYS   A 1 207 ? -27.409 26.376  -18.564 1.00 47.41  ? 337 LYS   A C   1 
ATOM   1526 O  O   . LYS   A 1 207 ? -27.870 25.984  -17.485 1.00 46.04  ? 337 LYS   A O   1 
ATOM   1527 C  CB  . LYS   A 1 207 ? -27.903 25.497  -20.863 1.00 49.19  ? 337 LYS   A CB  1 
ATOM   1528 C  CG  . LYS   A 1 207 ? -28.188 24.049  -20.514 1.00 52.81  ? 337 LYS   A CG  1 
ATOM   1529 C  CD  . LYS   A 1 207 ? -28.286 23.216  -21.783 1.00 60.26  ? 337 LYS   A CD  1 
ATOM   1530 C  CE  . LYS   A 1 207 ? -29.213 23.875  -22.794 1.00 63.94  ? 337 LYS   A CE  1 
ATOM   1531 N  NZ  . LYS   A 1 207 ? -30.419 23.040  -23.045 1.00 73.92  ? 337 LYS   A NZ  1 
ATOM   1532 N  N   . TRP   A 1 208 ? -26.133 26.746  -18.701 1.00 43.06  ? 338 TRP   A N   1 
ATOM   1533 C  CA  . TRP   A 1 208 ? -25.171 26.521  -17.630 1.00 43.90  ? 338 TRP   A CA  1 
ATOM   1534 C  C   . TRP   A 1 208 ? -25.570 27.238  -16.351 1.00 45.31  ? 338 TRP   A C   1 
ATOM   1535 O  O   . TRP   A 1 208 ? -25.502 26.656  -15.260 1.00 41.84  ? 338 TRP   A O   1 
ATOM   1536 C  CB  . TRP   A 1 208 ? -23.777 26.964  -18.067 1.00 42.90  ? 338 TRP   A CB  1 
ATOM   1537 C  CG  . TRP   A 1 208 ? -22.799 27.013  -16.931 1.00 44.80  ? 338 TRP   A CG  1 
ATOM   1538 C  CD1 . TRP   A 1 208 ? -22.359 28.131  -16.281 1.00 43.89  ? 338 TRP   A CD1 1 
ATOM   1539 C  CD2 . TRP   A 1 208 ? -22.189 25.898  -16.265 1.00 41.81  ? 338 TRP   A CD2 1 
ATOM   1540 N  NE1 . TRP   A 1 208 ? -21.485 27.785  -15.282 1.00 43.24  ? 338 TRP   A NE1 1 
ATOM   1541 C  CE2 . TRP   A 1 208 ? -21.369 26.420  -15.246 1.00 41.18  ? 338 TRP   A CE2 1 
ATOM   1542 C  CE3 . TRP   A 1 208 ? -22.241 24.516  -16.445 1.00 44.40  ? 338 TRP   A CE3 1 
ATOM   1543 C  CZ2 . TRP   A 1 208 ? -20.617 25.610  -14.403 1.00 42.26  ? 338 TRP   A CZ2 1 
ATOM   1544 C  CZ3 . TRP   A 1 208 ? -21.494 23.711  -15.604 1.00 43.87  ? 338 TRP   A CZ3 1 
ATOM   1545 C  CH2 . TRP   A 1 208 ? -20.685 24.265  -14.598 1.00 40.80  ? 338 TRP   A CH2 1 
ATOM   1546 N  N   . ASN   A 1 209 ? -25.966 28.508  -16.459 1.00 46.42  ? 339 ASN   A N   1 
ATOM   1547 C  CA  . ASN   A 1 209 ? -26.298 29.287  -15.272 1.00 45.26  ? 339 ASN   A CA  1 
ATOM   1548 C  C   . ASN   A 1 209 ? -27.605 28.814  -14.636 1.00 44.02  ? 339 ASN   A C   1 
ATOM   1549 O  O   . ASN   A 1 209 ? -27.805 29.002  -13.432 1.00 40.62  ? 339 ASN   A O   1 
ATOM   1550 C  CB  . ASN   A 1 209 ? -26.376 30.775  -15.635 1.00 45.95  ? 339 ASN   A CB  1 
ATOM   1551 C  CG  . ASN   A 1 209 ? -25.003 31.428  -15.789 1.00 47.50  ? 339 ASN   A CG  1 
ATOM   1552 O  OD1 . ASN   A 1 209 ? -24.077 31.146  -15.033 1.00 50.88  ? 339 ASN   A OD1 1 
ATOM   1553 N  ND2 . ASN   A 1 209 ? -24.874 32.309  -16.782 1.00 50.94  ? 339 ASN   A ND2 1 
ATOM   1554 N  N   . LYS   A 1 210 ? -28.509 28.211  -15.420 1.00 47.35  ? 340 LYS   A N   1 
ATOM   1555 C  CA  . LYS   A 1 210 ? -29.694 27.593  -14.830 1.00 44.87  ? 340 LYS   A CA  1 
ATOM   1556 C  C   . LYS   A 1 210 ? -29.292 26.428  -13.945 1.00 43.94  ? 340 LYS   A C   1 
ATOM   1557 O  O   . LYS   A 1 210 ? -29.787 26.285  -12.823 1.00 44.68  ? 340 LYS   A O   1 
ATOM   1558 C  CB  . LYS   A 1 210 ? -30.660 27.140  -15.929 1.00 46.28  ? 340 LYS   A CB  1 
ATOM   1559 C  CG  . LYS   A 1 210 ? -32.070 26.726  -15.456 1.00 48.59  ? 340 LYS   A CG  1 
ATOM   1560 C  CD  . LYS   A 1 210 ? -32.329 25.244  -15.736 1.00 51.96  ? 340 LYS   A CD  1 
ATOM   1561 C  CE  . LYS   A 1 210 ? -33.828 24.960  -15.956 1.00 59.16  ? 340 LYS   A CE  1 
ATOM   1562 N  NZ  . LYS   A 1 210 ? -34.741 25.472  -14.887 1.00 60.17  ? 340 LYS   A NZ  1 
ATOM   1563 N  N   . VAL   A 1 211 ? -28.367 25.605  -14.427 1.00 43.08  ? 341 VAL   A N   1 
ATOM   1564 C  CA  . VAL   A 1 211 ? -27.921 24.470  -13.644 1.00 45.58  ? 341 VAL   A CA  1 
ATOM   1565 C  C   . VAL   A 1 211 ? -27.096 24.933  -12.452 1.00 42.78  ? 341 VAL   A C   1 
ATOM   1566 O  O   . VAL   A 1 211 ? -27.166 24.337  -11.369 1.00 44.25  ? 341 VAL   A O   1 
ATOM   1567 C  CB  . VAL   A 1 211 ? -27.140 23.501  -14.546 1.00 41.28  ? 341 VAL   A CB  1 
ATOM   1568 C  CG1 . VAL   A 1 211 ? -26.074 22.798  -13.751 1.00 36.95  ? 341 VAL   A CG1 1 
ATOM   1569 C  CG2 . VAL   A 1 211 ? -28.088 22.501  -15.182 1.00 43.64  ? 341 VAL   A CG2 1 
ATOM   1570 N  N   . LEU   A 1 212 ? -26.298 25.985  -12.621 1.00 38.09  ? 342 LEU   A N   1 
ATOM   1571 C  CA  . LEU   A 1 212 ? -25.468 26.453  -11.520 1.00 42.34  ? 342 LEU   A CA  1 
ATOM   1572 C  C   . LEU   A 1 212 ? -26.312 27.076  -10.409 1.00 43.54  ? 342 LEU   A C   1 
ATOM   1573 O  O   . LEU   A 1 212 ? -25.938 27.009  -9.234  1.00 39.24  ? 342 LEU   A O   1 
ATOM   1574 C  CB  . LEU   A 1 212 ? -24.426 27.433  -12.053 1.00 41.48  ? 342 LEU   A CB  1 
ATOM   1575 C  CG  . LEU   A 1 212 ? -23.215 27.750  -11.170 1.00 42.94  ? 342 LEU   A CG  1 
ATOM   1576 C  CD1 . LEU   A 1 212 ? -22.326 26.529  -10.883 1.00 39.55  ? 342 LEU   A CD1 1 
ATOM   1577 C  CD2 . LEU   A 1 212 ? -22.426 28.855  -11.840 1.00 42.61  ? 342 LEU   A CD2 1 
ATOM   1578 N  N   . LYS   A 1 213 ? -27.456 27.672  -10.762 1.00 43.30  ? 343 LYS   A N   1 
ATOM   1579 C  CA  . LYS   A 1 213 ? -28.405 28.151  -9.764  1.00 43.12  ? 343 LYS   A CA  1 
ATOM   1580 C  C   . LYS   A 1 213 ? -29.072 26.991  -9.031  1.00 44.12  ? 343 LYS   A C   1 
ATOM   1581 O  O   . LYS   A 1 213 ? -29.388 27.105  -7.841  1.00 45.18  ? 343 LYS   A O   1 
ATOM   1582 C  CB  . LYS   A 1 213 ? -29.460 29.036  -10.435 1.00 46.17  ? 343 LYS   A CB  1 
ATOM   1583 C  CG  . LYS   A 1 213 ? -30.295 29.905  -9.490  1.00 46.92  ? 343 LYS   A CG  1 
ATOM   1584 C  CD  . LYS   A 1 213 ? -30.301 31.360  -9.991  1.00 52.91  ? 343 LYS   A CD  1 
ATOM   1585 C  CE  . LYS   A 1 213 ? -30.409 32.395  -8.861  1.00 51.17  ? 343 LYS   A CE  1 
ATOM   1586 N  NZ  . LYS   A 1 213 ? -30.928 33.732  -9.326  1.00 58.80  ? 343 LYS   A NZ  1 
ATOM   1587 N  N   . GLN   A 1 214 ? -29.278 25.867  -9.717  1.00 43.84  ? 344 GLN   A N   1 
ATOM   1588 C  CA  . GLN   A 1 214 ? -29.827 24.687  -9.062  1.00 45.85  ? 344 GLN   A CA  1 
ATOM   1589 C  C   . GLN   A 1 214 ? -28.800 24.041  -8.143  1.00 46.39  ? 344 GLN   A C   1 
ATOM   1590 O  O   . GLN   A 1 214 ? -29.156 23.562  -7.060  1.00 46.82  ? 344 GLN   A O   1 
ATOM   1591 C  CB  . GLN   A 1 214 ? -30.337 23.706  -10.119 1.00 44.62  ? 344 GLN   A CB  1 
ATOM   1592 C  CG  . GLN   A 1 214 ? -31.809 23.889  -10.437 1.00 47.68  ? 344 GLN   A CG  1 
ATOM   1593 C  CD  . GLN   A 1 214 ? -32.176 23.414  -11.822 1.00 46.87  ? 344 GLN   A CD  1 
ATOM   1594 O  OE1 . GLN   A 1 214 ? -31.415 23.604  -12.766 1.00 46.95  ? 344 GLN   A OE1 1 
ATOM   1595 N  NE2 . GLN   A 1 214 ? -33.334 22.784  -11.951 1.00 48.58  ? 344 GLN   A NE2 1 
ATOM   1596 N  N   . VAL   A 1 215 ? -27.525 24.054  -8.540  1.00 45.27  ? 345 VAL   A N   1 
ATOM   1597 C  CA  . VAL   A 1 215 ? -26.469 23.594  -7.647  1.00 43.84  ? 345 VAL   A CA  1 
ATOM   1598 C  C   . VAL   A 1 215 ? -26.369 24.530  -6.455  1.00 44.20  ? 345 VAL   A C   1 
ATOM   1599 O  O   . VAL   A 1 215 ? -26.205 24.096  -5.304  1.00 45.01  ? 345 VAL   A O   1 
ATOM   1600 C  CB  . VAL   A 1 215 ? -25.134 23.493  -8.414  1.00 43.40  ? 345 VAL   A CB  1 
ATOM   1601 C  CG1 . VAL   A 1 215 ? -23.940 23.674  -7.477  1.00 38.38  ? 345 VAL   A CG1 1 
ATOM   1602 C  CG2 . VAL   A 1 215 ? -25.038 22.168  -9.147  1.00 42.88  ? 345 VAL   A CG2 1 
ATOM   1603 N  N   . THR   A 1 216 ? -26.488 25.832  -6.713  1.00 44.62  ? 346 THR   A N   1 
ATOM   1604 C  CA  . THR   A 1 216 ? -26.484 26.807  -5.631  1.00 45.00  ? 346 THR   A CA  1 
ATOM   1605 C  C   . THR   A 1 216 ? -27.654 26.587  -4.684  1.00 45.57  ? 346 THR   A C   1 
ATOM   1606 O  O   . THR   A 1 216 ? -27.497 26.701  -3.463  1.00 46.18  ? 346 THR   A O   1 
ATOM   1607 C  CB  . THR   A 1 216 ? -26.513 28.221  -6.201  1.00 41.25  ? 346 THR   A CB  1 
ATOM   1608 O  OG1 . THR   A 1 216 ? -25.168 28.698  -6.304  1.00 40.52  ? 346 THR   A OG1 1 
ATOM   1609 C  CG2 . THR   A 1 216 ? -27.284 29.148  -5.276  1.00 43.72  ? 346 THR   A CG2 1 
ATOM   1610 N  N   . GLU   A 1 217 ? -28.837 26.281  -5.230  1.00 45.31  ? 347 GLU   A N   1 
ATOM   1611 C  CA  . GLU   A 1 217 ? -30.009 26.030  -4.397  1.00 48.23  ? 347 GLU   A CA  1 
ATOM   1612 C  C   . GLU   A 1 217 ? -29.828 24.764  -3.569  1.00 48.23  ? 347 GLU   A C   1 
ATOM   1613 O  O   . GLU   A 1 217 ? -30.208 24.731  -2.392  1.00 46.36  ? 347 GLU   A O   1 
ATOM   1614 C  CB  . GLU   A 1 217 ? -31.264 25.941  -5.274  1.00 49.68  ? 347 GLU   A CB  1 
ATOM   1615 C  CG  . GLU   A 1 217 ? -32.029 27.259  -5.481  1.00 54.15  ? 347 GLU   A CG  1 
ATOM   1616 C  CD  . GLU   A 1 217 ? -33.468 27.030  -5.969  1.00 62.93  ? 347 GLU   A CD  1 
ATOM   1617 O  OE1 . GLU   A 1 217 ? -34.084 26.022  -5.554  1.00 61.64  ? 347 GLU   A OE1 1 
ATOM   1618 O  OE2 . GLU   A 1 217 ? -33.973 27.847  -6.780  1.00 62.66  ? 347 GLU   A OE2 1 
ATOM   1619 N  N   . LYS   A 1 218 ? -29.230 23.719  -4.161  1.00 46.24  ? 348 LYS   A N   1 
ATOM   1620 C  CA  . LYS   A 1 218 ? -29.004 22.456  -3.457  1.00 47.25  ? 348 LYS   A CA  1 
ATOM   1621 C  C   . LYS   A 1 218 ? -27.912 22.583  -2.400  1.00 44.62  ? 348 LYS   A C   1 
ATOM   1622 O  O   . LYS   A 1 218 ? -27.996 21.951  -1.344  1.00 42.27  ? 348 LYS   A O   1 
ATOM   1623 C  CB  . LYS   A 1 218 ? -28.651 21.352  -4.467  1.00 44.84  ? 348 LYS   A CB  1 
ATOM   1624 C  CG  . LYS   A 1 218 ? -28.365 19.981  -3.856  1.00 41.90  ? 348 LYS   A CG  1 
ATOM   1625 C  CD  . LYS   A 1 218 ? -29.572 19.447  -3.118  1.00 41.61  ? 348 LYS   A CD  1 
ATOM   1626 C  CE  . LYS   A 1 218 ? -30.715 19.103  -4.072  1.00 46.74  ? 348 LYS   A CE  1 
ATOM   1627 N  NZ  . LYS   A 1 218 ? -31.845 18.370  -3.387  1.00 52.19  ? 348 LYS   A NZ  1 
ATOM   1628 N  N   . LEU   A 1 219 ? -26.888 23.395  -2.667  1.00 44.44  ? 349 LEU   A N   1 
ATOM   1629 C  CA  . LEU   A 1 219 ? -25.847 23.645  -1.679  1.00 43.29  ? 349 LEU   A CA  1 
ATOM   1630 C  C   . LEU   A 1 219 ? -26.415 24.418  -0.502  1.00 46.57  ? 349 LEU   A C   1 
ATOM   1631 O  O   . LEU   A 1 219 ? -25.999 24.209  0.644   1.00 47.92  ? 349 LEU   A O   1 
ATOM   1632 C  CB  . LEU   A 1 219 ? -24.698 24.409  -2.338  1.00 44.42  ? 349 LEU   A CB  1 
ATOM   1633 C  CG  . LEU   A 1 219 ? -23.605 23.587  -3.045  1.00 46.71  ? 349 LEU   A CG  1 
ATOM   1634 C  CD1 . LEU   A 1 219 ? -22.693 24.515  -3.856  1.00 43.03  ? 349 LEU   A CD1 1 
ATOM   1635 C  CD2 . LEU   A 1 219 ? -22.795 22.731  -2.083  1.00 43.31  ? 349 LEU   A CD2 1 
ATOM   1636 N  N   . LYS   A 1 220 ? -27.400 25.279  -0.768  1.00 46.15  ? 350 LYS   A N   1 
ATOM   1637 C  CA  . LYS   A 1 220 ? -28.040 26.039  0.296   1.00 46.35  ? 350 LYS   A CA  1 
ATOM   1638 C  C   . LYS   A 1 220 ? -28.721 25.120  1.294   1.00 48.25  ? 350 LYS   A C   1 
ATOM   1639 O  O   . LYS   A 1 220 ? -28.785 25.430  2.489   1.00 50.16  ? 350 LYS   A O   1 
ATOM   1640 C  CB  . LYS   A 1 220 ? -29.048 26.997  -0.318  1.00 48.25  ? 350 LYS   A CB  1 
ATOM   1641 C  CG  . LYS   A 1 220 ? -28.453 28.339  -0.572  1.00 50.33  ? 350 LYS   A CG  1 
ATOM   1642 C  CD  . LYS   A 1 220 ? -29.470 29.247  -1.204  1.00 52.80  ? 350 LYS   A CD  1 
ATOM   1643 C  CE  . LYS   A 1 220 ? -28.972 30.678  -1.244  1.00 49.30  ? 350 LYS   A CE  1 
ATOM   1644 N  NZ  . LYS   A 1 220 ? -28.269 31.023  0.017   1.00 51.14  ? 350 LYS   A NZ  1 
ATOM   1645 N  N   . GLU   A 1 221 ? -29.250 23.997  0.821   1.00 48.39  ? 351 GLU   A N   1 
ATOM   1646 C  CA  . GLU   A 1 221 ? -29.897 23.068  1.731   1.00 48.91  ? 351 GLU   A CA  1 
ATOM   1647 C  C   . GLU   A 1 221 ? -28.906 22.548  2.754   1.00 47.95  ? 351 GLU   A C   1 
ATOM   1648 O  O   . GLU   A 1 221 ? -29.226 22.428  3.942   1.00 47.23  ? 351 GLU   A O   1 
ATOM   1649 C  CB  . GLU   A 1 221 ? -30.508 21.919  0.944   1.00 47.38  ? 351 GLU   A CB  1 
ATOM   1650 C  CG  . GLU   A 1 221 ? -31.513 22.342  -0.097  1.00 47.67  ? 351 GLU   A CG  1 
ATOM   1651 C  CD  . GLU   A 1 221 ? -32.202 21.141  -0.716  1.00 51.47  ? 351 GLU   A CD  1 
ATOM   1652 O  OE1 . GLU   A 1 221 ? -31.930 20.021  -0.235  1.00 46.86  ? 351 GLU   A OE1 1 
ATOM   1653 O  OE2 . GLU   A 1 221 ? -32.999 21.306  -1.672  1.00 56.97  ? 351 GLU   A OE2 1 
ATOM   1654 N  N   . HIS   A 1 222 ? -27.685 22.271  2.318   1.00 47.05  ? 352 HIS   A N   1 
ATOM   1655 C  CA  . HIS   A 1 222 ? -26.725 21.657  3.214   1.00 47.41  ? 352 HIS   A CA  1 
ATOM   1656 C  C   . HIS   A 1 222 ? -26.102 22.646  4.192   1.00 47.42  ? 352 HIS   A C   1 
ATOM   1657 O  O   . HIS   A 1 222 ? -25.618 22.228  5.249   1.00 46.80  ? 352 HIS   A O   1 
ATOM   1658 C  CB  . HIS   A 1 222 ? -25.651 20.927  2.402   1.00 47.15  ? 352 HIS   A CB  1 
ATOM   1659 C  CG  . HIS   A 1 222 ? -26.155 19.704  1.695   1.00 45.49  ? 352 HIS   A CG  1 
ATOM   1660 N  ND1 . HIS   A 1 222 ? -26.309 18.489  2.328   1.00 44.46  ? 352 HIS   A ND1 1 
ATOM   1661 C  CD2 . HIS   A 1 222 ? -26.537 19.509  0.409   1.00 43.58  ? 352 HIS   A CD2 1 
ATOM   1662 C  CE1 . HIS   A 1 222 ? -26.763 17.598  1.463   1.00 41.50  ? 352 HIS   A CE1 1 
ATOM   1663 N  NE2 . HIS   A 1 222 ? -26.908 18.192  0.291   1.00 43.76  ? 352 HIS   A NE2 1 
ATOM   1664 N  N   . PHE   A 1 223 ? -26.124 23.941  3.886   1.00 49.10  ? 353 PHE   A N   1 
ATOM   1665 C  CA  . PHE   A 1 223 ? -25.411 24.907  4.709   1.00 48.25  ? 353 PHE   A CA  1 
ATOM   1666 C  C   . PHE   A 1 223 ? -26.390 25.908  5.297   1.00 49.73  ? 353 PHE   A C   1 
ATOM   1667 O  O   . PHE   A 1 223 ? -26.196 27.123  5.183   1.00 47.58  ? 353 PHE   A O   1 
ATOM   1668 C  CB  . PHE   A 1 223 ? -24.320 25.577  3.881   1.00 47.47  ? 353 PHE   A CB  1 
ATOM   1669 C  CG  . PHE   A 1 223 ? -23.241 24.620  3.469   1.00 48.41  ? 353 PHE   A CG  1 
ATOM   1670 C  CD1 . PHE   A 1 223 ? -23.362 23.875  2.303   1.00 47.49  ? 353 PHE   A CD1 1 
ATOM   1671 C  CD2 . PHE   A 1 223 ? -22.127 24.426  4.270   1.00 45.67  ? 353 PHE   A CD2 1 
ATOM   1672 C  CE1 . PHE   A 1 223 ? -22.379 22.962  1.941   1.00 47.67  ? 353 PHE   A CE1 1 
ATOM   1673 C  CE2 . PHE   A 1 223 ? -21.149 23.517  3.909   1.00 49.43  ? 353 PHE   A CE2 1 
ATOM   1674 C  CZ  . PHE   A 1 223 ? -21.275 22.782  2.743   1.00 44.24  ? 353 PHE   A CZ  1 
ATOM   1675 N  N   . ASN   A 1 224 ? -27.453 25.381  5.911   1.00 51.05  ? 354 ASN   A N   1 
ATOM   1676 C  CA  . ASN   A 1 224 ? -28.411 26.170  6.682   1.00 54.89  ? 354 ASN   A CA  1 
ATOM   1677 C  C   . ASN   A 1 224 ? -28.641 27.513  6.009   1.00 53.26  ? 354 ASN   A C   1 
ATOM   1678 O  O   . ASN   A 1 224 ? -28.300 28.575  6.530   1.00 49.09  ? 354 ASN   A O   1 
ATOM   1679 C  CB  . ASN   A 1 224 ? -27.951 26.347  8.134   1.00 50.51  ? 354 ASN   A CB  1 
ATOM   1680 C  CG  . ASN   A 1 224 ? -28.160 25.101  8.960   1.00 49.67  ? 354 ASN   A CG  1 
ATOM   1681 O  OD1 . ASN   A 1 224 ? -29.153 25.007  9.680   1.00 51.32  ? 354 ASN   A OD1 1 
ATOM   1682 N  ND2 . ASN   A 1 224 ? -27.226 24.147  8.878   1.00 49.29  ? 354 ASN   A ND2 1 
ATOM   1683 N  N   . ASN   A 1 225 ? -29.186 27.439  4.800   1.00 54.56  ? 355 ASN   A N   1 
ATOM   1684 C  CA  . ASN   A 1 225 ? -29.485 28.607  3.984   1.00 51.78  ? 355 ASN   A CA  1 
ATOM   1685 C  C   . ASN   A 1 225 ? -28.415 29.701  4.090   1.00 52.65  ? 355 ASN   A C   1 
ATOM   1686 O  O   . ASN   A 1 225 ? -28.434 30.536  4.996   1.00 64.43  ? 355 ASN   A O   1 
ATOM   1687 C  CB  . ASN   A 1 225 ? -30.841 29.156  4.382   1.00 53.74  ? 355 ASN   A CB  1 
ATOM   1688 C  CG  . ASN   A 1 225 ? -31.599 29.800  3.196   1.00 58.32  ? 355 ASN   A CG  1 
ATOM   1689 O  OD1 . ASN   A 1 225 ? -32.192 29.140  2.304   1.00 56.21  ? 355 ASN   A OD1 1 
ATOM   1690 N  ND2 . ASN   A 1 225 ? -31.535 31.114  3.179   1.00 55.76  ? 355 ASN   A ND2 1 
ATOM   1691 N  N   . LYS   A 1 226 ? -27.447 29.690  3.189   1.00 48.66  ? 357 LYS   A N   1 
ATOM   1692 C  CA  . LYS   A 1 226 ? -26.252 30.505  3.343   1.00 46.23  ? 357 LYS   A CA  1 
ATOM   1693 C  C   . LYS   A 1 226 ? -25.764 31.017  1.984   1.00 45.95  ? 357 LYS   A C   1 
ATOM   1694 O  O   . LYS   A 1 226 ? -25.769 30.276  0.988   1.00 44.28  ? 357 LYS   A O   1 
ATOM   1695 C  CB  . LYS   A 1 226 ? -25.185 29.660  4.017   1.00 47.92  ? 357 LYS   A CB  1 
ATOM   1696 C  CG  . LYS   A 1 226 ? -24.735 30.209  5.335   1.00 45.84  ? 357 LYS   A CG  1 
ATOM   1697 C  CD  . LYS   A 1 226 ? -23.226 30.442  5.405   1.00 48.68  ? 357 LYS   A CD  1 
ATOM   1698 C  CE  . LYS   A 1 226 ? -22.777 30.022  6.785   1.00 50.64  ? 357 LYS   A CE  1 
ATOM   1699 N  NZ  . LYS   A 1 226 ? -23.273 28.646  7.147   1.00 53.47  ? 357 LYS   A NZ  1 
ATOM   1700 N  N   . THR   A 1 227 ? -25.382 32.293  1.914   1.00 43.51  ? 358 THR   A N   1 
ATOM   1701 C  CA  . THR   A 1 227 ? -24.959 32.861  0.642   1.00 45.06  ? 358 THR   A CA  1 
ATOM   1702 C  C   . THR   A 1 227 ? -23.884 31.954  0.071   1.00 42.25  ? 358 THR   A C   1 
ATOM   1703 O  O   . THR   A 1 227 ? -22.841 31.748  0.690   1.00 42.20  ? 358 THR   A O   1 
ATOM   1704 C  CB  . THR   A 1 227 ? -24.464 34.299  0.810   1.00 45.45  ? 358 THR   A CB  1 
ATOM   1705 O  OG1 . THR   A 1 227 ? -25.585 35.122  1.140   1.00 49.06  ? 358 THR   A OG1 1 
ATOM   1706 C  CG2 . THR   A 1 227 ? -23.875 34.810  -0.480  1.00 41.48  ? 358 THR   A CG2 1 
ATOM   1707 N  N   . ILE   A 1 228 ? -24.162 31.352  -1.071  1.00 44.11  ? 359 ILE   A N   1 
ATOM   1708 C  CA  . ILE   A 1 228 ? -23.228 30.433  -1.701  1.00 45.89  ? 359 ILE   A CA  1 
ATOM   1709 C  C   . ILE   A 1 228 ? -22.442 31.225  -2.734  1.00 45.66  ? 359 ILE   A C   1 
ATOM   1710 O  O   . ILE   A 1 228 ? -23.031 31.807  -3.653  1.00 44.48  ? 359 ILE   A O   1 
ATOM   1711 C  CB  . ILE   A 1 228 ? -23.966 29.246  -2.340  1.00 44.13  ? 359 ILE   A CB  1 
ATOM   1712 C  CG1 . ILE   A 1 228 ? -24.722 28.425  -1.284  1.00 45.29  ? 359 ILE   A CG1 1 
ATOM   1713 C  CG2 . ILE   A 1 228 ? -22.997 28.371  -3.114  1.00 43.03  ? 359 ILE   A CG2 1 
ATOM   1714 C  CD1 . ILE   A 1 228 ? -23.850 27.870  -0.159  1.00 44.70  ? 359 ILE   A CD1 1 
ATOM   1715 N  N   . ILE   A 1 229 ? -21.116 31.269  -2.568  1.00 43.34  ? 360 ILE   A N   1 
ATOM   1716 C  CA  . ILE   A 1 229 ? -20.244 32.055  -3.434  1.00 48.26  ? 360 ILE   A CA  1 
ATOM   1717 C  C   . ILE   A 1 229 ? -19.239 31.137  -4.121  1.00 49.58  ? 360 ILE   A C   1 
ATOM   1718 O  O   . ILE   A 1 229 ? -18.754 30.164  -3.533  1.00 48.63  ? 360 ILE   A O   1 
ATOM   1719 C  CB  . ILE   A 1 229 ? -19.497 33.161  -2.661  1.00 51.67  ? 360 ILE   A CB  1 
ATOM   1720 C  CG1 . ILE   A 1 229 ? -20.446 34.302  -2.309  1.00 49.07  ? 360 ILE   A CG1 1 
ATOM   1721 C  CG2 . ILE   A 1 229 ? -18.358 33.716  -3.509  1.00 49.27  ? 360 ILE   A CG2 1 
ATOM   1722 C  CD1 . ILE   A 1 229 ? -19.901 35.236  -1.246  1.00 51.36  ? 360 ILE   A CD1 1 
ATOM   1723 N  N   . PHE   A 1 230 ? -18.906 31.477  -5.367  1.00 49.41  ? 361 PHE   A N   1 
ATOM   1724 C  CA  . PHE   A 1 230 ? -17.953 30.723  -6.177  1.00 49.56  ? 361 PHE   A CA  1 
ATOM   1725 C  C   . PHE   A 1 230 ? -16.727 31.584  -6.455  1.00 52.00  ? 361 PHE   A C   1 
ATOM   1726 O  O   . PHE   A 1 230 ? -16.856 32.748  -6.843  1.00 53.60  ? 361 PHE   A O   1 
ATOM   1727 C  CB  . PHE   A 1 230 ? -18.582 30.281  -7.502  1.00 46.77  ? 361 PHE   A CB  1 
ATOM   1728 C  CG  . PHE   A 1 230 ? -19.581 29.170  -7.364  1.00 45.69  ? 361 PHE   A CG  1 
ATOM   1729 C  CD1 . PHE   A 1 230 ? -19.155 27.869  -7.147  1.00 45.11  ? 361 PHE   A CD1 1 
ATOM   1730 C  CD2 . PHE   A 1 230 ? -20.943 29.416  -7.484  1.00 41.80  ? 361 PHE   A CD2 1 
ATOM   1731 C  CE1 . PHE   A 1 230 ? -20.070 26.835  -7.026  1.00 42.42  ? 361 PHE   A CE1 1 
ATOM   1732 C  CE2 . PHE   A 1 230 ? -21.861 28.396  -7.367  1.00 38.98  ? 361 PHE   A CE2 1 
ATOM   1733 C  CZ  . PHE   A 1 230 ? -21.425 27.098  -7.135  1.00 41.68  ? 361 PHE   A CZ  1 
ATOM   1734 N  N   . GLN   A 1 231 ? -15.541 31.010  -6.278  1.00 53.30  ? 362 GLN   A N   1 
ATOM   1735 C  CA  . GLN   A 1 231 ? -14.301 31.755  -6.449  1.00 57.22  ? 362 GLN   A CA  1 
ATOM   1736 C  C   . GLN   A 1 231 ? -13.342 30.918  -7.265  1.00 56.97  ? 362 GLN   A C   1 
ATOM   1737 O  O   . GLN   A 1 231 ? -13.119 29.731  -6.950  1.00 57.10  ? 362 GLN   A O   1 
ATOM   1738 C  CB  . GLN   A 1 231 ? -13.694 32.147  -5.082  1.00 58.56  ? 362 GLN   A CB  1 
ATOM   1739 C  CG  . GLN   A 1 231 ? -14.421 33.303  -4.369  1.00 60.59  ? 362 GLN   A CG  1 
ATOM   1740 C  CD  . GLN   A 1 231 ? -13.818 34.677  -4.688  1.00 60.15  ? 362 GLN   A CD  1 
ATOM   1741 O  OE1 . GLN   A 1 231 ? -14.232 35.344  -5.638  1.00 59.97  ? 362 GLN   A OE1 1 
ATOM   1742 N  NE2 . GLN   A 1 231 ? -12.820 35.087  -3.904  1.00 60.40  ? 362 GLN   A NE2 1 
ATOM   1743 N  N   . PRO   A 1 232 ? -12.806 31.441  -8.370  1.00 60.67  ? 363 PRO   A N   1 
ATOM   1744 C  CA  . PRO   A 1 232 ? -11.787 30.708  -9.136  1.00 58.15  ? 363 PRO   A CA  1 
ATOM   1745 C  C   . PRO   A 1 232 ? -10.608 30.333  -8.250  1.00 57.21  ? 363 PRO   A C   1 
ATOM   1746 O  O   . PRO   A 1 232 ? -10.287 31.043  -7.287  1.00 57.34  ? 363 PRO   A O   1 
ATOM   1747 C  CB  . PRO   A 1 232 ? -11.383 31.696  -10.240 1.00 59.05  ? 363 PRO   A CB  1 
ATOM   1748 C  CG  . PRO   A 1 232 ? -12.625 32.519  -10.458 1.00 57.81  ? 363 PRO   A CG  1 
ATOM   1749 C  CD  . PRO   A 1 232 ? -13.357 32.586  -9.123  1.00 61.12  ? 363 PRO   A CD  1 
ATOM   1750 N  N   . PRO   A 1 233 ? -9.967  29.200  -8.525  1.00 59.12  ? 364 PRO   A N   1 
ATOM   1751 C  CA  . PRO   A 1 233 ? -8.978  28.683  -7.575  1.00 59.02  ? 364 PRO   A CA  1 
ATOM   1752 C  C   . PRO   A 1 233 ? -7.756  29.585  -7.518  1.00 63.18  ? 364 PRO   A C   1 
ATOM   1753 O  O   . PRO   A 1 233 ? -7.363  30.207  -8.508  1.00 58.93  ? 364 PRO   A O   1 
ATOM   1754 C  CB  . PRO   A 1 233 ? -8.627  27.296  -8.134  1.00 54.29  ? 364 PRO   A CB  1 
ATOM   1755 C  CG  . PRO   A 1 233 ? -9.669  27.008  -9.194  1.00 49.18  ? 364 PRO   A CG  1 
ATOM   1756 C  CD  . PRO   A 1 233 ? -10.118 28.332  -9.704  1.00 53.84  ? 364 PRO   A CD  1 
ATOM   1757 N  N   . SER   A 1 234 ? -7.170  29.665  -6.324  1.00 65.82  ? 365 SER   A N   1 
ATOM   1758 C  CA  . SER   A 1 234 ? -5.897  30.341  -6.097  1.00 65.58  ? 365 SER   A CA  1 
ATOM   1759 C  C   . SER   A 1 234 ? -4.739  29.348  -6.039  1.00 63.32  ? 365 SER   A C   1 
ATOM   1760 O  O   . SER   A 1 234 ? -3.860  29.353  -6.910  1.00 60.79  ? 365 SER   A O   1 
ATOM   1761 C  CB  . SER   A 1 234 ? -5.988  31.151  -4.801  1.00 62.47  ? 365 SER   A CB  1 
ATOM   1762 O  OG  . SER   A 1 234 ? -6.331  30.287  -3.737  1.00 66.22  ? 365 SER   A OG  1 
ATOM   1763 N  N   . GLY   A 1 235 ? -4.727  28.492  -5.014  1.00 63.75  ? 366 GLY   A N   1 
ATOM   1764 C  CA  . GLY   A 1 235 ? -3.725  27.453  -4.927  1.00 62.12  ? 366 GLY   A CA  1 
ATOM   1765 C  C   . GLY   A 1 235 ? -3.818  26.477  -6.082  1.00 62.65  ? 366 GLY   A C   1 
ATOM   1766 O  O   . GLY   A 1 235 ? -4.813  26.421  -6.813  1.00 60.51  ? 366 GLY   A O   1 
ATOM   1767 N  N   . GLY   A 1 236 ? -2.743  25.715  -6.260  1.00 56.17  ? 367 GLY   A N   1 
ATOM   1768 C  CA  . GLY   A 1 236 ? -2.703  24.674  -7.265  1.00 54.22  ? 367 GLY   A CA  1 
ATOM   1769 C  C   . GLY   A 1 236 ? -1.955  25.113  -8.511  1.00 52.19  ? 367 GLY   A C   1 
ATOM   1770 O  O   . GLY   A 1 236 ? -1.532  26.263  -8.657  1.00 53.68  ? 367 GLY   A O   1 
ATOM   1771 N  N   . ASP   A 1 237 ? -1.773  24.158  -9.417  1.00 48.48  ? 368 ASP   A N   1 
ATOM   1772 C  CA  . ASP   A 1 237 ? -0.989  24.390  -10.617 1.00 46.10  ? 368 ASP   A CA  1 
ATOM   1773 C  C   . ASP   A 1 237 ? -1.912  24.569  -11.812 1.00 43.51  ? 368 ASP   A C   1 
ATOM   1774 O  O   . ASP   A 1 237 ? -3.136  24.497  -11.698 1.00 43.77  ? 368 ASP   A O   1 
ATOM   1775 C  CB  . ASP   A 1 237 ? -0.011  23.244  -10.859 1.00 47.35  ? 368 ASP   A CB  1 
ATOM   1776 C  CG  . ASP   A 1 237 ? 0.115   22.309  -9.659  1.00 49.87  ? 368 ASP   A CG  1 
ATOM   1777 O  OD1 . ASP   A 1 237 ? -0.890  22.069  -8.946  1.00 50.83  ? 368 ASP   A OD1 1 
ATOM   1778 O  OD2 . ASP   A 1 237 ? 1.235   21.815  -9.423  1.00 51.15  ? 368 ASP   A OD2 1 
ATOM   1779 N  N   . LEU   A 1 238 ? -1.316  24.794  -12.982 1.00 39.67  ? 369 LEU   A N   1 
ATOM   1780 C  CA  . LEU   A 1 238 ? -2.105  25.181  -14.143 1.00 41.17  ? 369 LEU   A CA  1 
ATOM   1781 C  C   . LEU   A 1 238 ? -3.272  24.230  -14.376 1.00 40.16  ? 369 LEU   A C   1 
ATOM   1782 O  O   . LEU   A 1 238 ? -4.363  24.665  -14.754 1.00 35.42  ? 369 LEU   A O   1 
ATOM   1783 C  CB  . LEU   A 1 238 ? -1.210  25.244  -15.377 1.00 42.13  ? 369 LEU   A CB  1 
ATOM   1784 C  CG  . LEU   A 1 238 ? -1.250  26.579  -16.104 1.00 40.60  ? 369 LEU   A CG  1 
ATOM   1785 C  CD1 . LEU   A 1 238 ? -1.451  27.718  -15.111 1.00 39.90  ? 369 LEU   A CD1 1 
ATOM   1786 C  CD2 . LEU   A 1 238 ? 0.052   26.737  -16.831 1.00 40.62  ? 369 LEU   A CD2 1 
ATOM   1787 N  N   . GLU   A 1 239 ? -3.054  22.928  -14.170 1.00 40.17  ? 370 GLU   A N   1 
ATOM   1788 C  CA  . GLU   A 1 239 ? -4.060  21.919  -14.494 1.00 39.21  ? 370 GLU   A CA  1 
ATOM   1789 C  C   . GLU   A 1 239 ? -5.269  21.950  -13.562 1.00 37.96  ? 370 GLU   A C   1 
ATOM   1790 O  O   . GLU   A 1 239 ? -6.309  21.357  -13.889 1.00 35.92  ? 370 GLU   A O   1 
ATOM   1791 C  CB  . GLU   A 1 239 ? -3.431  20.522  -14.477 1.00 36.43  ? 370 GLU   A CB  1 
ATOM   1792 C  CG  . GLU   A 1 239 ? -2.288  20.312  -15.466 1.00 40.19  ? 370 GLU   A CG  1 
ATOM   1793 C  CD  . GLU   A 1 239 ? -0.963  20.898  -14.993 1.00 43.51  ? 370 GLU   A CD  1 
ATOM   1794 O  OE1 . GLU   A 1 239 ? -0.844  21.219  -13.785 1.00 44.90  ? 370 GLU   A OE1 1 
ATOM   1795 O  OE2 . GLU   A 1 239 ? -0.027  20.977  -15.830 1.00 42.67  ? 370 GLU   A OE2 1 
ATOM   1796 N  N   . ILE   A 1 240 ? -5.165  22.614  -12.420 1.00 36.46  ? 371 ILE   A N   1 
ATOM   1797 C  CA  . ILE   A 1 240 ? -6.282  22.697  -11.495 1.00 40.93  ? 371 ILE   A CA  1 
ATOM   1798 C  C   . ILE   A 1 240 ? -6.870  24.106  -11.405 1.00 36.15  ? 371 ILE   A C   1 
ATOM   1799 O  O   . ILE   A 1 240 ? -8.047  24.246  -11.046 1.00 38.56  ? 371 ILE   A O   1 
ATOM   1800 C  CB  . ILE   A 1 240 ? -5.885  22.169  -10.098 1.00 40.78  ? 371 ILE   A CB  1 
ATOM   1801 C  CG1 . ILE   A 1 240 ? -5.325  20.738  -10.213 1.00 41.24  ? 371 ILE   A CG1 1 
ATOM   1802 C  CG2 . ILE   A 1 240 ? -7.069  22.190  -9.167  1.00 37.10  ? 371 ILE   A CG2 1 
ATOM   1803 C  CD1 . ILE   A 1 240 ? -4.509  20.260  -9.007  1.00 43.45  ? 371 ILE   A CD1 1 
ATOM   1804 N  N   . THR   A 1 241 ? -6.104  25.146  -11.713 1.00 38.65  ? 372 THR   A N   1 
ATOM   1805 C  CA  . THR   A 1 241 ? -6.714  26.455  -11.896 1.00 42.27  ? 372 THR   A CA  1 
ATOM   1806 C  C   . THR   A 1 241 ? -7.484  26.528  -13.209 1.00 40.40  ? 372 THR   A C   1 
ATOM   1807 O  O   . THR   A 1 241 ? -8.525  27.193  -13.281 1.00 37.96  ? 372 THR   A O   1 
ATOM   1808 C  CB  . THR   A 1 241 ? -5.636  27.536  -11.829 1.00 39.69  ? 372 THR   A CB  1 
ATOM   1809 O  OG1 . THR   A 1 241 ? -4.726  27.346  -12.919 1.00 41.91  ? 372 THR   A OG1 1 
ATOM   1810 C  CG2 . THR   A 1 241 ? -4.855  27.442  -10.522 1.00 43.30  ? 372 THR   A CG2 1 
ATOM   1811 N  N   . MET   A 1 242 ? -7.011  25.828  -14.233 1.00 36.72  ? 373 MET   A N   1 
ATOM   1812 C  CA  . MET   A 1 242 ? -7.668  25.731  -15.529 1.00 38.03  ? 373 MET   A CA  1 
ATOM   1813 C  C   . MET   A 1 242 ? -8.452  24.432  -15.612 1.00 41.20  ? 373 MET   A C   1 
ATOM   1814 O  O   . MET   A 1 242 ? -8.098  23.418  -14.995 1.00 41.48  ? 373 MET   A O   1 
ATOM   1815 C  CB  . MET   A 1 242 ? -6.650  25.767  -16.678 1.00 41.36  ? 373 MET   A CB  1 
ATOM   1816 C  CG  . MET   A 1 242 ? -5.848  27.051  -16.846 1.00 39.54  ? 373 MET   A CG  1 
ATOM   1817 S  SD  . MET   A 1 242 ? -6.767  28.397  -17.611 1.00 51.67  ? 373 MET   A SD  1 
ATOM   1818 C  CE  . MET   A 1 242 ? -5.569  29.055  -18.786 1.00 48.87  ? 373 MET   A CE  1 
ATOM   1819 N  N   . HIS   A 1 243 ? -9.521  24.463  -16.405 1.00 37.96  ? 374 HIS   A N   1 
ATOM   1820 C  CA  . HIS   A 1 243 ? -10.253 23.238  -16.705 1.00 36.95  ? 374 HIS   A CA  1 
ATOM   1821 C  C   . HIS   A 1 243 ? -9.417  22.459  -17.710 1.00 36.68  ? 374 HIS   A C   1 
ATOM   1822 O  O   . HIS   A 1 243 ? -9.246  22.897  -18.855 1.00 34.39  ? 374 HIS   A O   1 
ATOM   1823 C  CB  . HIS   A 1 243 ? -11.647 23.526  -17.259 1.00 38.50  ? 374 HIS   A CB  1 
ATOM   1824 C  CG  . HIS   A 1 243 ? -12.261 22.352  -17.962 1.00 39.20  ? 374 HIS   A CG  1 
ATOM   1825 N  ND1 . HIS   A 1 243 ? -12.266 21.084  -17.411 1.00 40.12  ? 374 HIS   A ND1 1 
ATOM   1826 C  CD2 . HIS   A 1 243 ? -12.892 22.245  -19.156 1.00 35.70  ? 374 HIS   A CD2 1 
ATOM   1827 C  CE1 . HIS   A 1 243 ? -12.872 20.249  -18.237 1.00 37.66  ? 374 HIS   A CE1 1 
ATOM   1828 N  NE2 . HIS   A 1 243 ? -13.260 20.927  -19.303 1.00 38.33  ? 374 HIS   A NE2 1 
ATOM   1829 N  N   . SER   A 1 244 ? -8.869  21.328  -17.275 1.00 35.86  ? 375 SER   A N   1 
ATOM   1830 C  CA  . SER   A 1 244 ? -7.969  20.518  -18.082 1.00 34.65  ? 375 SER   A CA  1 
ATOM   1831 C  C   . SER   A 1 244 ? -8.658  19.237  -18.532 1.00 38.72  ? 375 SER   A C   1 
ATOM   1832 O  O   . SER   A 1 244 ? -9.517  18.689  -17.827 1.00 37.07  ? 375 SER   A O   1 
ATOM   1833 C  CB  . SER   A 1 244 ? -6.700  20.178  -17.302 1.00 38.20  ? 375 SER   A CB  1 
ATOM   1834 O  OG  . SER   A 1 244 ? -5.874  21.324  -17.181 1.00 40.70  ? 375 SER   A OG  1 
ATOM   1835 N  N   . PHE   A 1 245 ? -8.269  18.762  -19.713 1.00 34.18  ? 376 PHE   A N   1 
ATOM   1836 C  CA  . PHE   A 1 245 ? -8.810  17.521  -20.257 1.00 37.68  ? 376 PHE   A CA  1 
ATOM   1837 C  C   . PHE   A 1 245 ? -8.049  17.199  -21.530 1.00 35.72  ? 376 PHE   A C   1 
ATOM   1838 O  O   . PHE   A 1 245 ? -7.509  18.097  -22.186 1.00 35.63  ? 376 PHE   A O   1 
ATOM   1839 C  CB  . PHE   A 1 245 ? -10.306 17.636  -20.550 1.00 36.34  ? 376 PHE   A CB  1 
ATOM   1840 C  CG  . PHE   A 1 245 ? -10.630 18.665  -21.589 1.00 37.68  ? 376 PHE   A CG  1 
ATOM   1841 C  CD1 . PHE   A 1 245 ? -10.674 18.331  -22.938 1.00 35.59  ? 376 PHE   A CD1 1 
ATOM   1842 C  CD2 . PHE   A 1 245 ? -10.839 19.988  -21.222 1.00 35.58  ? 376 PHE   A CD2 1 
ATOM   1843 C  CE1 . PHE   A 1 245 ? -10.964 19.303  -23.901 1.00 36.59  ? 376 PHE   A CE1 1 
ATOM   1844 C  CE2 . PHE   A 1 245 ? -11.120 20.946  -22.164 1.00 34.83  ? 376 PHE   A CE2 1 
ATOM   1845 C  CZ  . PHE   A 1 245 ? -11.185 20.609  -23.506 1.00 34.27  ? 376 PHE   A CZ  1 
ATOM   1846 N  N   . ASN   A 1 246 ? -8.017  15.912  -21.878 1.00 33.77  ? 377 ASN   A N   1 
ATOM   1847 C  CA  . ASN   A 1 246 ? -7.410  15.478  -23.131 1.00 36.30  ? 377 ASN   A CA  1 
ATOM   1848 C  C   . ASN   A 1 246 ? -8.486  15.366  -24.203 1.00 34.78  ? 377 ASN   A C   1 
ATOM   1849 O  O   . ASN   A 1 246 ? -9.573  14.832  -23.953 1.00 36.15  ? 377 ASN   A O   1 
ATOM   1850 C  CB  . ASN   A 1 246 ? -6.691  14.143  -22.975 1.00 37.12  ? 377 ASN   A CB  1 
ATOM   1851 C  CG  . ASN   A 1 246 ? -5.816  13.821  -24.173 1.00 37.52  ? 377 ASN   A CG  1 
ATOM   1852 O  OD1 . ASN   A 1 246 ? -6.307  13.568  -25.272 1.00 34.54  ? 377 ASN   A OD1 1 
ATOM   1853 N  ND2 . ASN   A 1 246 ? -4.503  13.885  -23.973 1.00 37.03  ? 377 ASN   A ND2 1 
ATOM   1854 N  N   . CYS   A 1 247 ? -8.185  15.882  -25.388 1.00 36.95  ? 378 CYS   A N   1 
ATOM   1855 C  CA  . CYS   A 1 247 ? -9.131  15.918  -26.497 1.00 37.84  ? 378 CYS   A CA  1 
ATOM   1856 C  C   . CYS   A 1 247 ? -8.410  15.387  -27.730 1.00 37.69  ? 378 CYS   A C   1 
ATOM   1857 O  O   . CYS   A 1 247 ? -7.502  16.039  -28.253 1.00 37.03  ? 378 CYS   A O   1 
ATOM   1858 C  CB  . CYS   A 1 247 ? -9.646  17.335  -26.728 1.00 38.90  ? 378 CYS   A CB  1 
ATOM   1859 S  SG  . CYS   A 1 247 ? -10.670 17.494  -28.203 1.00 46.24  ? 378 CYS   A SG  1 
ATOM   1860 N  N   . ARG   A 1 248 ? -8.791  14.199  -28.180 1.00 42.32  ? 379 ARG   A N   1 
ATOM   1861 C  CA  . ARG   A 1 248 ? -8.224  13.615  -29.391 1.00 41.99  ? 379 ARG   A CA  1 
ATOM   1862 C  C   . ARG   A 1 248 ? -6.718  13.403  -29.277 1.00 40.32  ? 379 ARG   A C   1 
ATOM   1863 O  O   . ARG   A 1 248 ? -6.022  13.329  -30.295 1.00 39.92  ? 379 ARG   A O   1 
ATOM   1864 C  CB  . ARG   A 1 248 ? -8.521  14.481  -30.621 1.00 41.51  ? 379 ARG   A CB  1 
ATOM   1865 C  CG  . ARG   A 1 248 ? -9.990  14.680  -30.921 1.00 42.55  ? 379 ARG   A CG  1 
ATOM   1866 C  CD  . ARG   A 1 248 ? -10.711 13.375  -31.222 1.00 49.92  ? 379 ARG   A CD  1 
ATOM   1867 N  NE  . ARG   A 1 248 ? -12.041 13.635  -31.758 1.00 53.18  ? 379 ARG   A NE  1 
ATOM   1868 C  CZ  . ARG   A 1 248 ? -13.167 13.592  -31.057 1.00 52.14  ? 379 ARG   A CZ  1 
ATOM   1869 N  NH1 . ARG   A 1 248 ? -13.180 13.226  -29.787 1.00 50.94  ? 379 ARG   A NH1 1 
ATOM   1870 N  NH2 . ARG   A 1 248 ? -14.311 13.935  -31.644 1.00 52.53  ? 379 ARG   A NH2 1 
ATOM   1871 N  N   . GLY   A 1 249 ? -6.187  13.322  -28.059 1.00 37.17  ? 380 GLY   A N   1 
ATOM   1872 C  CA  . GLY   A 1 249 ? -4.767  13.185  -27.845 1.00 37.08  ? 380 GLY   A CA  1 
ATOM   1873 C  C   . GLY   A 1 249 ? -4.073  14.439  -27.352 1.00 37.89  ? 380 GLY   A C   1 
ATOM   1874 O  O   . GLY   A 1 249 ? -2.970  14.341  -26.801 1.00 37.18  ? 380 GLY   A O   1 
ATOM   1875 N  N   . GLU   A 1 250 ? -4.689  15.608  -27.519 1.00 37.35  ? 381 GLU   A N   1 
ATOM   1876 C  CA  . GLU   A 1 250 ? -4.057  16.863  -27.136 1.00 39.31  ? 381 GLU   A CA  1 
ATOM   1877 C  C   . GLU   A 1 250 ? -4.533  17.316  -25.753 1.00 37.74  ? 381 GLU   A C   1 
ATOM   1878 O  O   . GLU   A 1 250 ? -5.699  17.124  -25.373 1.00 34.27  ? 381 GLU   A O   1 
ATOM   1879 C  CB  . GLU   A 1 250 ? -4.366  17.966  -28.153 1.00 38.12  ? 381 GLU   A CB  1 
ATOM   1880 C  CG  . GLU   A 1 250 ? -3.818  17.779  -29.561 1.00 41.69  ? 381 GLU   A CG  1 
ATOM   1881 C  CD  . GLU   A 1 250 ? -2.334  17.453  -29.570 1.00 44.77  ? 381 GLU   A CD  1 
ATOM   1882 O  OE1 . GLU   A 1 250 ? -1.664  17.718  -28.550 1.00 45.66  ? 381 GLU   A OE1 1 
ATOM   1883 O  OE2 . GLU   A 1 250 ? -1.821  16.980  -30.610 1.00 46.59  ? 381 GLU   A OE2 1 
ATOM   1884 N  N   . PHE   A 1 251 ? -3.631  17.969  -25.023 1.00 31.42  ? 382 PHE   A N   1 
ATOM   1885 C  CA  . PHE   A 1 251 ? -3.914  18.470  -23.683 1.00 39.14  ? 382 PHE   A CA  1 
ATOM   1886 C  C   . PHE   A 1 251 ? -4.469  19.896  -23.766 1.00 38.33  ? 382 PHE   A C   1 
ATOM   1887 O  O   . PHE   A 1 251 ? -3.801  20.799  -24.280 1.00 42.25  ? 382 PHE   A O   1 
ATOM   1888 C  CB  . PHE   A 1 251 ? -2.640  18.413  -22.833 1.00 39.43  ? 382 PHE   A CB  1 
ATOM   1889 C  CG  . PHE   A 1 251 ? -2.201  17.009  -22.497 1.00 36.99  ? 382 PHE   A CG  1 
ATOM   1890 C  CD1 . PHE   A 1 251 ? -2.746  16.321  -21.420 1.00 38.78  ? 382 PHE   A CD1 1 
ATOM   1891 C  CD2 . PHE   A 1 251 ? -1.279  16.355  -23.299 1.00 36.96  ? 382 PHE   A CD2 1 
ATOM   1892 C  CE1 . PHE   A 1 251 ? -2.351  15.019  -21.137 1.00 38.32  ? 382 PHE   A CE1 1 
ATOM   1893 C  CE2 . PHE   A 1 251 ? -0.890  15.059  -23.028 1.00 39.37  ? 382 PHE   A CE2 1 
ATOM   1894 C  CZ  . PHE   A 1 251 ? -1.428  14.387  -21.938 1.00 38.42  ? 382 PHE   A CZ  1 
ATOM   1895 N  N   . PHE   A 1 252 ? -5.679  20.092  -23.238 1.00 34.60  ? 383 PHE   A N   1 
ATOM   1896 C  CA  . PHE   A 1 252 ? -6.430  21.342  -23.301 1.00 36.60  ? 383 PHE   A CA  1 
ATOM   1897 C  C   . PHE   A 1 252 ? -6.464  21.993  -21.921 1.00 35.09  ? 383 PHE   A C   1 
ATOM   1898 O  O   . PHE   A 1 252 ? -6.773  21.329  -20.931 1.00 35.18  ? 383 PHE   A O   1 
ATOM   1899 C  CB  . PHE   A 1 252 ? -7.868  21.080  -23.789 1.00 37.13  ? 383 PHE   A CB  1 
ATOM   1900 C  CG  . PHE   A 1 252 ? -8.054  21.233  -25.285 1.00 36.78  ? 383 PHE   A CG  1 
ATOM   1901 C  CD1 . PHE   A 1 252 ? -7.540  20.293  -26.156 1.00 37.93  ? 383 PHE   A CD1 1 
ATOM   1902 C  CD2 . PHE   A 1 252 ? -8.789  22.291  -25.815 1.00 35.86  ? 383 PHE   A CD2 1 
ATOM   1903 C  CE1 . PHE   A 1 252 ? -7.710  20.425  -27.532 1.00 40.48  ? 383 PHE   A CE1 1 
ATOM   1904 C  CE2 . PHE   A 1 252 ? -8.968  22.421  -27.190 1.00 37.46  ? 383 PHE   A CE2 1 
ATOM   1905 C  CZ  . PHE   A 1 252 ? -8.427  21.490  -28.048 1.00 39.88  ? 383 PHE   A CZ  1 
ATOM   1906 N  N   . TYR   A 1 253 ? -6.156  23.289  -21.854 1.00 40.60  ? 384 TYR   A N   1 
ATOM   1907 C  CA  . TYR   A 1 253 ? -6.255  24.069  -20.620 1.00 37.87  ? 384 TYR   A CA  1 
ATOM   1908 C  C   . TYR   A 1 253 ? -7.189  25.232  -20.885 1.00 37.36  ? 384 TYR   A C   1 
ATOM   1909 O  O   . TYR   A 1 253 ? -6.887  26.091  -21.720 1.00 38.68  ? 384 TYR   A O   1 
ATOM   1910 C  CB  . TYR   A 1 253 ? -4.900  24.602  -20.149 1.00 36.93  ? 384 TYR   A CB  1 
ATOM   1911 C  CG  . TYR   A 1 253 ? -3.954  23.556  -19.650 1.00 36.42  ? 384 TYR   A CG  1 
ATOM   1912 C  CD1 . TYR   A 1 253 ? -3.470  22.569  -20.498 1.00 38.40  ? 384 TYR   A CD1 1 
ATOM   1913 C  CD2 . TYR   A 1 253 ? -3.534  23.552  -18.329 1.00 39.37  ? 384 TYR   A CD2 1 
ATOM   1914 C  CE1 . TYR   A 1 253 ? -2.587  21.598  -20.036 1.00 40.10  ? 384 TYR   A CE1 1 
ATOM   1915 C  CE2 . TYR   A 1 253 ? -2.656  22.594  -17.858 1.00 37.36  ? 384 TYR   A CE2 1 
ATOM   1916 C  CZ  . TYR   A 1 253 ? -2.181  21.622  -18.715 1.00 38.21  ? 384 TYR   A CZ  1 
ATOM   1917 O  OH  . TYR   A 1 253 ? -1.313  20.659  -18.246 1.00 42.45  ? 384 TYR   A OH  1 
ATOM   1918 N  N   . CYS   A 1 254 ? -8.302  25.268  -20.169 1.00 39.25  ? 385 CYS   A N   1 
ATOM   1919 C  CA  . CYS   A 1 254 ? -9.371  26.210  -20.444 1.00 42.38  ? 385 CYS   A CA  1 
ATOM   1920 C  C   . CYS   A 1 254 ? -9.660  27.024  -19.196 1.00 39.57  ? 385 CYS   A C   1 
ATOM   1921 O  O   . CYS   A 1 254 ? -9.788  26.473  -18.097 1.00 40.69  ? 385 CYS   A O   1 
ATOM   1922 C  CB  . CYS   A 1 254 ? -10.621 25.473  -20.922 1.00 38.07  ? 385 CYS   A CB  1 
ATOM   1923 S  SG  . CYS   A 1 254 ? -10.272 24.597  -22.446 1.00 40.98  ? 385 CYS   A SG  1 
ATOM   1924 N  N   . ASN   A 1 255 ? -9.767  28.329  -19.379 1.00 40.48  ? 386 ASN   A N   1 
ATOM   1925 C  CA  . ASN   A 1 255 ? -10.076 29.259  -18.301 1.00 44.78  ? 386 ASN   A CA  1 
ATOM   1926 C  C   . ASN   A 1 255 ? -11.575 29.228  -18.016 1.00 41.95  ? 386 ASN   A C   1 
ATOM   1927 O  O   . ASN   A 1 255 ? -12.389 29.594  -18.869 1.00 40.86  ? 386 ASN   A O   1 
ATOM   1928 C  CB  . ASN   A 1 255 ? -9.568  30.646  -18.692 1.00 45.48  ? 386 ASN   A CB  1 
ATOM   1929 C  CG  . ASN   A 1 255 ? -9.860  31.686  -17.661 1.00 47.51  ? 386 ASN   A CG  1 
ATOM   1930 O  OD1 . ASN   A 1 255 ? -10.823 31.563  -16.908 1.00 47.52  ? 386 ASN   A OD1 1 
ATOM   1931 N  ND2 . ASN   A 1 255 ? -9.016  32.714  -17.589 1.00 50.73  ? 386 ASN   A ND2 1 
ATOM   1932 N  N   . THR   A 1 256 ? -11.946 28.785  -16.815 1.00 42.54  ? 387 THR   A N   1 
ATOM   1933 C  CA  . THR   A 1 256 ? -13.350 28.619  -16.450 1.00 43.55  ? 387 THR   A CA  1 
ATOM   1934 C  C   . THR   A 1 256 ? -13.871 29.774  -15.602 1.00 39.67  ? 387 THR   A C   1 
ATOM   1935 O  O   . THR   A 1 256 ? -14.810 29.601  -14.820 1.00 42.18  ? 387 THR   A O   1 
ATOM   1936 C  CB  . THR   A 1 256 ? -13.567 27.296  -15.713 1.00 40.17  ? 387 THR   A CB  1 
ATOM   1937 O  OG1 . THR   A 1 256 ? -12.801 27.276  -14.495 1.00 39.01  ? 387 THR   A OG1 1 
ATOM   1938 C  CG2 . THR   A 1 256 ? -13.158 26.151  -16.577 1.00 36.00  ? 387 THR   A CG2 1 
ATOM   1939 N  N   . THR   A 1 257 ? -13.278 30.955  -15.743 1.00 40.53  ? 388 THR   A N   1 
ATOM   1940 C  CA  . THR   A 1 257 ? -13.678 32.073  -14.900 1.00 45.08  ? 388 THR   A CA  1 
ATOM   1941 C  C   . THR   A 1 257 ? -15.109 32.510  -15.185 1.00 43.81  ? 388 THR   A C   1 
ATOM   1942 O  O   . THR   A 1 257 ? -15.816 32.958  -14.277 1.00 45.72  ? 388 THR   A O   1 
ATOM   1943 C  CB  . THR   A 1 257 ? -12.713 33.243  -15.092 1.00 46.88  ? 388 THR   A CB  1 
ATOM   1944 O  OG1 . THR   A 1 257 ? -11.491 32.950  -14.402 1.00 48.45  ? 388 THR   A OG1 1 
ATOM   1945 C  CG2 . THR   A 1 257 ? -13.309 34.499  -14.479 1.00 45.65  ? 388 THR   A CG2 1 
ATOM   1946 N  N   . GLN   A 1 258 ? -15.550 32.386  -16.427 1.00 40.04  ? 389 GLN   A N   1 
ATOM   1947 C  CA  . GLN   A 1 258 ? -16.874 32.832  -16.811 1.00 43.49  ? 389 GLN   A CA  1 
ATOM   1948 C  C   . GLN   A 1 258 ? -17.960 31.900  -16.314 1.00 46.19  ? 389 GLN   A C   1 
ATOM   1949 O  O   . GLN   A 1 258 ? -19.121 32.315  -16.246 1.00 47.20  ? 389 GLN   A O   1 
ATOM   1950 C  CB  . GLN   A 1 258 ? -16.957 32.965  -18.337 1.00 46.04  ? 389 GLN   A CB  1 
ATOM   1951 C  CG  . GLN   A 1 258 ? -16.516 34.344  -18.862 1.00 43.33  ? 389 GLN   A CG  1 
ATOM   1952 C  CD  . GLN   A 1 258 ? -16.374 34.369  -20.370 1.00 46.88  ? 389 GLN   A CD  1 
ATOM   1953 O  OE1 . GLN   A 1 258 ? -17.243 34.882  -21.082 1.00 48.30  ? 389 GLN   A OE1 1 
ATOM   1954 N  NE2 . GLN   A 1 258 ? -15.278 33.797  -20.870 1.00 47.48  ? 389 GLN   A NE2 1 
ATOM   1955 N  N   . LEU   A 1 259 ? -17.616 30.659  -15.968 1.00 42.79  ? 390 LEU   A N   1 
ATOM   1956 C  CA  . LEU   A 1 259 ? -18.609 29.717  -15.471 1.00 39.73  ? 390 LEU   A CA  1 
ATOM   1957 C  C   . LEU   A 1 259 ? -18.908 29.918  -13.997 1.00 39.68  ? 390 LEU   A C   1 
ATOM   1958 O  O   . LEU   A 1 259 ? -20.021 29.641  -13.553 1.00 39.86  ? 390 LEU   A O   1 
ATOM   1959 C  CB  . LEU   A 1 259 ? -18.148 28.278  -15.704 1.00 42.88  ? 390 LEU   A CB  1 
ATOM   1960 C  CG  . LEU   A 1 259 ? -17.934 27.841  -17.147 1.00 41.67  ? 390 LEU   A CG  1 
ATOM   1961 C  CD1 . LEU   A 1 259 ? -17.580 26.360  -17.202 1.00 40.68  ? 390 LEU   A CD1 1 
ATOM   1962 C  CD2 . LEU   A 1 259 ? -19.178 28.147  -17.959 1.00 41.72  ? 390 LEU   A CD2 1 
ATOM   1963 N  N   . PHE   A 1 260 ? -17.948 30.414  -13.234 1.00 46.50  ? 391 PHE   A N   1 
ATOM   1964 C  CA  . PHE   A 1 260 ? -18.140 30.635  -11.810 1.00 45.78  ? 391 PHE   A CA  1 
ATOM   1965 C  C   . PHE   A 1 260 ? -18.148 32.133  -11.554 1.00 51.60  ? 391 PHE   A C   1 
ATOM   1966 O  O   . PHE   A 1 260 ? -17.406 32.647  -10.708 1.00 53.30  ? 391 PHE   A O   1 
ATOM   1967 C  CB  . PHE   A 1 260 ? -17.056 29.884  -11.042 1.00 46.81  ? 391 PHE   A CB  1 
ATOM   1968 C  CG  . PHE   A 1 260 ? -17.052 28.409  -11.347 1.00 43.58  ? 391 PHE   A CG  1 
ATOM   1969 C  CD1 . PHE   A 1 260 ? -17.977 27.566  -10.762 1.00 41.45  ? 391 PHE   A CD1 1 
ATOM   1970 C  CD2 . PHE   A 1 260 ? -16.187 27.886  -12.290 1.00 44.36  ? 391 PHE   A CD2 1 
ATOM   1971 C  CE1 . PHE   A 1 260 ? -17.997 26.221  -11.070 1.00 43.26  ? 391 PHE   A CE1 1 
ATOM   1972 C  CE2 . PHE   A 1 260 ? -16.207 26.539  -12.597 1.00 41.50  ? 391 PHE   A CE2 1 
ATOM   1973 C  CZ  . PHE   A 1 260 ? -17.111 25.708  -11.990 1.00 39.24  ? 391 PHE   A CZ  1 
ATOM   1974 N  N   . ASN   A 1 261 ? -18.972 32.828  -12.342 1.00 53.82  ? 392 ASN   A N   1 
ATOM   1975 C  CA  . ASN   A 1 261 ? -19.236 34.257  -12.208 1.00 56.57  ? 392 ASN   A CA  1 
ATOM   1976 C  C   . ASN   A 1 261 ? -20.383 34.424  -11.229 1.00 57.98  ? 392 ASN   A C   1 
ATOM   1977 O  O   . ASN   A 1 261 ? -21.535 34.139  -11.570 1.00 58.78  ? 392 ASN   A O   1 
ATOM   1978 C  CB  . ASN   A 1 261 ? -19.611 34.863  -13.559 1.00 60.40  ? 392 ASN   A CB  1 
ATOM   1979 C  CG  . ASN   A 1 261 ? -18.945 36.185  -13.809 1.00 64.32  ? 392 ASN   A CG  1 
ATOM   1980 O  OD1 . ASN   A 1 261 ? -17.941 36.510  -13.176 1.00 68.25  ? 392 ASN   A OD1 1 
ATOM   1981 N  ND2 . ASN   A 1 261 ? -19.496 36.966  -14.745 1.00 67.71  ? 392 ASN   A ND2 1 
ATOM   1982 N  N   . ASN   A 1 262 ? -20.085 34.894  -10.020 1.00 58.51  ? 393 ASN   A N   1 
ATOM   1983 C  CA  . ASN   A 1 262 ? -21.164 35.048  -9.056  1.00 57.18  ? 393 ASN   A CA  1 
ATOM   1984 C  C   . ASN   A 1 262 ? -22.206 36.060  -9.503  1.00 60.03  ? 393 ASN   A C   1 
ATOM   1985 O  O   . ASN   A 1 262 ? -23.259 36.165  -8.865  1.00 56.46  ? 393 ASN   A O   1 
ATOM   1986 C  CB  . ASN   A 1 262 ? -20.603 35.421  -7.689  1.00 57.30  ? 393 ASN   A CB  1 
ATOM   1987 C  CG  . ASN   A 1 262 ? -20.221 34.208  -6.887  1.00 57.48  ? 393 ASN   A CG  1 
ATOM   1988 O  OD1 . ASN   A 1 262 ? -19.093 33.733  -6.978  1.00 53.92  ? 393 ASN   A OD1 1 
ATOM   1989 N  ND2 . ASN   A 1 262 ? -21.169 33.676  -6.112  1.00 57.39  ? 393 ASN   A ND2 1 
ATOM   1990 N  N   . THR   A 1 263 ? -21.962 36.780  -10.598 1.00 63.65  ? 394 THR   A N   1 
ATOM   1991 C  CA  . THR   A 1 263 ? -22.945 37.750  -11.065 1.00 64.89  ? 394 THR   A CA  1 
ATOM   1992 C  C   . THR   A 1 263 ? -24.190 37.060  -11.593 1.00 64.86  ? 394 THR   A C   1 
ATOM   1993 O  O   . THR   A 1 263 ? -25.314 37.527  -11.371 1.00 66.47  ? 394 THR   A O   1 
ATOM   1994 C  CB  . THR   A 1 263 ? -22.335 38.646  -12.143 1.00 70.07  ? 394 THR   A CB  1 
ATOM   1995 O  OG1 . THR   A 1 263 ? -21.085 39.161  -11.673 1.00 77.00  ? 394 THR   A OG1 1 
ATOM   1996 C  CG2 . THR   A 1 263 ? -23.260 39.802  -12.498 1.00 66.82  ? 394 THR   A CG2 1 
ATOM   1997 N  N   . CYS   A 1 264 ? -24.009 35.938  -12.278 1.00 62.00  ? 395 CYS   A N   1 
ATOM   1998 C  CA  . CYS   A 1 264 ? -25.075 35.358  -13.070 1.00 63.30  ? 395 CYS   A CA  1 
ATOM   1999 C  C   . CYS   A 1 264 ? -25.737 34.218  -12.322 1.00 62.62  ? 395 CYS   A C   1 
ATOM   2000 O  O   . CYS   A 1 264 ? -26.573 34.428  -11.442 1.00 61.47  ? 395 CYS   A O   1 
ATOM   2001 C  CB  . CYS   A 1 264 ? -24.525 34.863  -14.406 1.00 60.41  ? 395 CYS   A CB  1 
ATOM   2002 S  SG  . CYS   A 1 264 ? -23.857 36.188  -15.488 1.00 67.87  ? 395 CYS   A SG  1 
ATOM   2003 N  N   . LYS   A 1 271 ? -30.848 37.868  -16.904 1.00 65.92  ? 408 LYS   A N   1 
ATOM   2004 C  CA  . LYS   A 1 271 ? -29.427 38.092  -16.657 1.00 68.37  ? 408 LYS   A CA  1 
ATOM   2005 C  C   . LYS   A 1 271 ? -28.879 38.639  -17.964 1.00 67.19  ? 408 LYS   A C   1 
ATOM   2006 O  O   . LYS   A 1 271 ? -28.888 37.931  -18.969 1.00 69.00  ? 408 LYS   A O   1 
ATOM   2007 C  CB  . LYS   A 1 271 ? -28.748 36.803  -16.181 1.00 66.12  ? 408 LYS   A CB  1 
ATOM   2008 C  CG  . LYS   A 1 271 ? -29.245 36.251  -14.854 1.00 67.53  ? 408 LYS   A CG  1 
ATOM   2009 C  CD  . LYS   A 1 271 ? -28.246 36.514  -13.728 1.00 67.89  ? 408 LYS   A CD  1 
ATOM   2010 C  CE  . LYS   A 1 271 ? -28.928 36.553  -12.363 1.00 64.23  ? 408 LYS   A CE  1 
ATOM   2011 N  NZ  . LYS   A 1 271 ? -28.901 35.225  -11.664 1.00 62.70  ? 408 LYS   A NZ  1 
ATOM   2012 N  N   . GLY   A 1 272 ? -28.369 39.871  -17.965 1.00 67.07  ? 409 GLY   A N   1 
ATOM   2013 C  CA  . GLY   A 1 272 ? -27.722 40.394  -19.158 1.00 67.10  ? 409 GLY   A CA  1 
ATOM   2014 C  C   . GLY   A 1 272 ? -26.445 39.634  -19.459 1.00 66.86  ? 409 GLY   A C   1 
ATOM   2015 O  O   . GLY   A 1 272 ? -25.394 40.241  -19.677 1.00 65.06  ? 409 GLY   A O   1 
ATOM   2016 N  N   . CYS   A 1 273 ? -26.515 38.301  -19.447 1.00 67.26  ? 410 CYS   A N   1 
ATOM   2017 C  CA  . CYS   A 1 273 ? -25.311 37.483  -19.366 1.00 67.36  ? 410 CYS   A CA  1 
ATOM   2018 C  C   . CYS   A 1 273 ? -25.672 36.013  -19.480 1.00 66.39  ? 410 CYS   A C   1 
ATOM   2019 O  O   . CYS   A 1 273 ? -25.357 35.222  -18.581 1.00 64.90  ? 410 CYS   A O   1 
ATOM   2020 C  CB  . CYS   A 1 273 ? -24.579 37.637  -18.027 1.00 67.90  ? 410 CYS   A CB  1 
ATOM   2021 S  SG  . CYS   A 1 273 ? -25.409 37.038  -16.459 1.00 72.94  ? 410 CYS   A SG  1 
ATOM   2022 N  N   . ASN   A 1 274 ? -26.341 35.631  -20.556 1.00 62.76  ? 411 ASN   A N   1 
ATOM   2023 C  CA  . ASN   A 1 274 ? -26.775 34.250  -20.666 1.00 58.91  ? 411 ASN   A CA  1 
ATOM   2024 C  C   . ASN   A 1 274 ? -27.028 33.887  -22.122 1.00 56.31  ? 411 ASN   A C   1 
ATOM   2025 O  O   . ASN   A 1 274 ? -28.017 33.227  -22.463 1.00 56.29  ? 411 ASN   A O   1 
ATOM   2026 C  CB  . ASN   A 1 274 ? -27.984 34.020  -19.750 1.00 59.42  ? 411 ASN   A CB  1 
ATOM   2027 C  CG  . ASN   A 1 274 ? -29.224 34.741  -20.217 1.00 57.33  ? 411 ASN   A CG  1 
ATOM   2028 O  OD1 . ASN   A 1 274 ? -29.237 35.356  -21.283 1.00 59.84  ? 411 ASN   A OD1 1 
ATOM   2029 N  ND2 . ASN   A 1 274 ? -30.275 34.690  -19.404 1.00 54.85  ? 411 ASN   A ND2 1 
ATOM   2030 N  N   . GLY   A 1 275 ? -26.118 34.324  -22.978 1.00 55.17  ? 412 GLY   A N   1 
ATOM   2031 C  CA  . GLY   A 1 275 ? -25.964 33.796  -24.314 1.00 53.44  ? 412 GLY   A CA  1 
ATOM   2032 C  C   . GLY   A 1 275 ? -24.851 32.770  -24.357 1.00 50.79  ? 412 GLY   A C   1 
ATOM   2033 O  O   . GLY   A 1 275 ? -24.626 32.030  -23.391 1.00 48.60  ? 412 GLY   A O   1 
ATOM   2034 N  N   . THR   A 1 276 ? -24.110 32.761  -25.468 1.00 51.53  ? 413 THR   A N   1 
ATOM   2035 C  CA  . THR   A 1 276 ? -23.043 31.787  -25.701 1.00 49.09  ? 413 THR   A CA  1 
ATOM   2036 C  C   . THR   A 1 276 ? -21.750 32.248  -25.030 1.00 48.09  ? 413 THR   A C   1 
ATOM   2037 O  O   . THR   A 1 276 ? -21.152 33.247  -25.443 1.00 48.28  ? 413 THR   A O   1 
ATOM   2038 C  CB  . THR   A 1 276 ? -22.803 31.573  -27.195 1.00 49.15  ? 413 THR   A CB  1 
ATOM   2039 O  OG1 . THR   A 1 276 ? -23.796 30.692  -27.735 1.00 55.88  ? 413 THR   A OG1 1 
ATOM   2040 C  CG2 . THR   A 1 276 ? -21.443 30.929  -27.414 1.00 51.05  ? 413 THR   A CG2 1 
ATOM   2041 N  N   . ILE   A 1 277 ? -21.298 31.488  -24.028 1.00 45.91  ? 414 ILE   A N   1 
ATOM   2042 C  CA  . ILE   A 1 277 ? -20.049 31.751  -23.319 1.00 46.95  ? 414 ILE   A CA  1 
ATOM   2043 C  C   . ILE   A 1 277 ? -18.897 31.119  -24.091 1.00 45.17  ? 414 ILE   A C   1 
ATOM   2044 O  O   . ILE   A 1 277 ? -18.990 29.960  -24.513 1.00 46.94  ? 414 ILE   A O   1 
ATOM   2045 C  CB  . ILE   A 1 277 ? -20.121 31.180  -21.887 1.00 46.33  ? 414 ILE   A CB  1 
ATOM   2046 C  CG1 . ILE   A 1 277 ? -21.226 31.855  -21.061 1.00 48.17  ? 414 ILE   A CG1 1 
ATOM   2047 C  CG2 . ILE   A 1 277 ? -18.782 31.310  -21.202 1.00 47.22  ? 414 ILE   A CG2 1 
ATOM   2048 C  CD1 . ILE   A 1 277 ? -21.512 31.191  -19.696 1.00 46.62  ? 414 ILE   A CD1 1 
ATOM   2049 N  N   . THR   A 1 278 ? -17.794 31.848  -24.260 1.00 41.24  ? 415 THR   A N   1 
ATOM   2050 C  CA  . THR   A 1 278 ? -16.621 31.309  -24.946 1.00 43.63  ? 415 THR   A CA  1 
ATOM   2051 C  C   . THR   A 1 278 ? -15.441 31.268  -23.988 1.00 41.23  ? 415 THR   A C   1 
ATOM   2052 O  O   . THR   A 1 278 ? -14.867 32.308  -23.660 1.00 42.28  ? 415 THR   A O   1 
ATOM   2053 C  CB  . THR   A 1 278 ? -16.288 32.123  -26.193 1.00 45.68  ? 415 THR   A CB  1 
ATOM   2054 O  OG1 . THR   A 1 278 ? -17.500 32.458  -26.867 1.00 49.93  ? 415 THR   A OG1 1 
ATOM   2055 C  CG2 . THR   A 1 278 ? -15.393 31.348  -27.128 1.00 42.76  ? 415 THR   A CG2 1 
ATOM   2056 N  N   . LEU   A 1 279 ? -15.078 30.065  -23.552 1.00 44.21  ? 416 LEU   A N   1 
ATOM   2057 C  CA  . LEU   A 1 279 ? -13.926 29.912  -22.673 1.00 44.04  ? 416 LEU   A CA  1 
ATOM   2058 C  C   . LEU   A 1 279 ? -12.643 29.942  -23.494 1.00 40.27  ? 416 LEU   A C   1 
ATOM   2059 O  O   . LEU   A 1 279 ? -12.538 29.233  -24.496 1.00 38.89  ? 416 LEU   A O   1 
ATOM   2060 C  CB  . LEU   A 1 279 ? -14.007 28.610  -21.887 1.00 43.28  ? 416 LEU   A CB  1 
ATOM   2061 C  CG  . LEU   A 1 279 ? -15.223 28.459  -20.984 1.00 41.15  ? 416 LEU   A CG  1 
ATOM   2062 C  CD1 . LEU   A 1 279 ? -14.989 27.310  -20.045 1.00 40.53  ? 416 LEU   A CD1 1 
ATOM   2063 C  CD2 . LEU   A 1 279 ? -15.465 29.756  -20.247 1.00 43.05  ? 416 LEU   A CD2 1 
ATOM   2064 N  N   . PRO   A 1 280 ? -11.662 30.756  -23.117 1.00 42.95  ? 417 PRO   A N   1 
ATOM   2065 C  CA  . PRO   A 1 280 ? -10.362 30.701  -23.797 1.00 42.92  ? 417 PRO   A CA  1 
ATOM   2066 C  C   . PRO   A 1 280 ? -9.593  29.450  -23.400 1.00 40.68  ? 417 PRO   A C   1 
ATOM   2067 O  O   . PRO   A 1 280 ? -9.491  29.113  -22.218 1.00 39.76  ? 417 PRO   A O   1 
ATOM   2068 C  CB  . PRO   A 1 280 ? -9.663  31.977  -23.317 1.00 43.15  ? 417 PRO   A CB  1 
ATOM   2069 C  CG  . PRO   A 1 280 ? -10.270 32.244  -21.986 1.00 42.60  ? 417 PRO   A CG  1 
ATOM   2070 C  CD  . PRO   A 1 280 ? -11.713 31.843  -22.122 1.00 40.89  ? 417 PRO   A CD  1 
ATOM   2071 N  N   . CYS   A 1 281 ? -9.060  28.748  -24.397 1.00 40.75  ? 418 CYS   A N   1 
ATOM   2072 C  CA  . CYS   A 1 281 ? -8.279  27.550  -24.133 1.00 38.88  ? 418 CYS   A CA  1 
ATOM   2073 C  C   . CYS   A 1 281 ? -6.896  27.657  -24.746 1.00 42.47  ? 418 CYS   A C   1 
ATOM   2074 O  O   . CYS   A 1 281 ? -6.597  28.533  -25.570 1.00 43.84  ? 418 CYS   A O   1 
ATOM   2075 C  CB  . CYS   A 1 281 ? -8.931  26.274  -24.673 1.00 40.75  ? 418 CYS   A CB  1 
ATOM   2076 S  SG  . CYS   A 1 281 ? -10.550 25.929  -23.964 1.00 43.90  ? 418 CYS   A SG  1 
ATOM   2077 N  N   . LYS   A 1 282 ? -6.064  26.715  -24.335 1.00 36.47  ? 419 LYS   A N   1 
ATOM   2078 C  CA  . LYS   A 1 282 ? -4.730  26.570  -24.872 1.00 36.79  ? 419 LYS   A CA  1 
ATOM   2079 C  C   . LYS   A 1 282 ? -4.437  25.081  -24.934 1.00 40.77  ? 419 LYS   A C   1 
ATOM   2080 O  O   . LYS   A 1 282 ? -4.942  24.301  -24.119 1.00 41.64  ? 419 LYS   A O   1 
ATOM   2081 C  CB  . LYS   A 1 282 ? -3.709  27.301  -23.993 1.00 39.40  ? 419 LYS   A CB  1 
ATOM   2082 C  CG  . LYS   A 1 282 ? -2.607  28.027  -24.728 1.00 41.68  ? 419 LYS   A CG  1 
ATOM   2083 C  CD  . LYS   A 1 282 ? -3.121  29.019  -25.772 1.00 41.02  ? 419 LYS   A CD  1 
ATOM   2084 C  CE  . LYS   A 1 282 ? -2.022  29.372  -26.771 1.00 43.28  ? 419 LYS   A CE  1 
ATOM   2085 N  NZ  . LYS   A 1 282 ? -0.927  30.133  -26.105 1.00 47.08  ? 419 LYS   A NZ  1 
ATOM   2086 N  N   . ILE   A 1 283 ? -3.654  24.680  -25.919 1.00 35.65  ? 420 ILE   A N   1 
ATOM   2087 C  CA  . ILE   A 1 283 ? -3.142  23.322  -25.980 1.00 37.68  ? 420 ILE   A CA  1 
ATOM   2088 C  C   . ILE   A 1 283 ? -1.725  23.368  -25.444 1.00 40.50  ? 420 ILE   A C   1 
ATOM   2089 O  O   . ILE   A 1 283 ? -0.876  24.087  -25.988 1.00 39.54  ? 420 ILE   A O   1 
ATOM   2090 C  CB  . ILE   A 1 283 ? -3.160  22.766  -27.405 1.00 39.56  ? 420 ILE   A CB  1 
ATOM   2091 C  CG1 . ILE   A 1 283 ? -4.606  22.636  -27.877 1.00 38.07  ? 420 ILE   A CG1 1 
ATOM   2092 C  CG2 . ILE   A 1 283 ? -2.518  21.408  -27.381 1.00 39.18  ? 420 ILE   A CG2 1 
ATOM   2093 C  CD1 . ILE   A 1 283 ? -4.783  22.001  -29.194 1.00 38.12  ? 420 ILE   A CD1 1 
ATOM   2094 N  N   . LYS   A 1 284 ? -1.478  22.619  -24.373 1.00 37.03  ? 421 LYS   A N   1 
ATOM   2095 C  CA  . LYS   A 1 284 ? -0.172  22.593  -23.740 1.00 39.02  ? 421 LYS   A CA  1 
ATOM   2096 C  C   . LYS   A 1 284 ? 0.624   21.375  -24.186 1.00 39.93  ? 421 LYS   A C   1 
ATOM   2097 O  O   . LYS   A 1 284 ? 0.083   20.314  -24.518 1.00 38.28  ? 421 LYS   A O   1 
ATOM   2098 C  CB  . LYS   A 1 284 ? -0.283  22.610  -22.211 1.00 39.06  ? 421 LYS   A CB  1 
ATOM   2099 C  CG  . LYS   A 1 284 ? -0.798  23.932  -21.663 1.00 40.23  ? 421 LYS   A CG  1 
ATOM   2100 C  CD  . LYS   A 1 284 ? -0.068  24.299  -20.382 1.00 40.32  ? 421 LYS   A CD  1 
ATOM   2101 C  CE  . LYS   A 1 284 ? 1.288   23.584  -20.379 1.00 42.23  ? 421 LYS   A CE  1 
ATOM   2102 N  NZ  . LYS   A 1 284 ? 2.429   24.520  -20.547 1.00 38.55  ? 421 LYS   A NZ  1 
ATOM   2103 N  N   . GLN   A 1 285 ? 1.935   21.562  -24.193 1.00 41.47  ? 422 GLN   A N   1 
ATOM   2104 C  CA  . GLN   A 1 285 ? 2.920   20.559  -24.555 1.00 41.72  ? 422 GLN   A CA  1 
ATOM   2105 C  C   . GLN   A 1 285 ? 3.613   19.971  -23.344 1.00 42.53  ? 422 GLN   A C   1 
ATOM   2106 O  O   . GLN   A 1 285 ? 3.966   18.791  -23.351 1.00 42.23  ? 422 GLN   A O   1 
ATOM   2107 C  CB  . GLN   A 1 285 ? 3.955   21.202  -25.474 1.00 42.61  ? 422 GLN   A CB  1 
ATOM   2108 C  CG  . GLN   A 1 285 ? 4.000   20.613  -26.852 1.00 46.39  ? 422 GLN   A CG  1 
ATOM   2109 C  CD  . GLN   A 1 285 ? 5.010   21.317  -27.713 1.00 44.24  ? 422 GLN   A CD  1 
ATOM   2110 O  OE1 . GLN   A 1 285 ? 4.758   22.430  -28.191 1.00 49.22  ? 422 GLN   A OE1 1 
ATOM   2111 N  NE2 . GLN   A 1 285 ? 6.147   20.673  -27.947 1.00 44.94  ? 422 GLN   A NE2 1 
ATOM   2112 N  N   . ILE   A 1 286 ? 3.825   20.781  -22.310 1.00 41.13  ? 423 ILE   A N   1 
ATOM   2113 C  CA  . ILE   A 1 286 ? 4.529   20.362  -21.106 1.00 42.28  ? 423 ILE   A CA  1 
ATOM   2114 C  C   . ILE   A 1 286 ? 3.485   20.287  -20.000 1.00 43.96  ? 423 ILE   A C   1 
ATOM   2115 O  O   . ILE   A 1 286 ? 2.874   21.297  -19.627 1.00 40.78  ? 423 ILE   A O   1 
ATOM   2116 C  CB  . ILE   A 1 286 ? 5.680   21.314  -20.748 1.00 42.33  ? 423 ILE   A CB  1 
ATOM   2117 C  CG1 . ILE   A 1 286 ? 6.484   21.694  -21.992 1.00 45.15  ? 423 ILE   A CG1 1 
ATOM   2118 C  CG2 . ILE   A 1 286 ? 6.625   20.665  -19.720 1.00 45.00  ? 423 ILE   A CG2 1 
ATOM   2119 C  CD1 . ILE   A 1 286 ? 7.743   22.492  -21.682 1.00 44.39  ? 423 ILE   A CD1 1 
ATOM   2120 N  N   . ILE   A 1 287 ? 3.278   19.078  -19.494 1.00 43.66  ? 424 ILE   A N   1 
ATOM   2121 C  CA  . ILE   A 1 287 ? 2.164   18.742  -18.623 1.00 44.95  ? 424 ILE   A CA  1 
ATOM   2122 C  C   . ILE   A 1 287 ? 2.710   18.241  -17.296 1.00 44.09  ? 424 ILE   A C   1 
ATOM   2123 O  O   . ILE   A 1 287 ? 3.646   17.436  -17.261 1.00 42.92  ? 424 ILE   A O   1 
ATOM   2124 C  CB  . ILE   A 1 287 ? 1.259   17.667  -19.266 1.00 42.00  ? 424 ILE   A CB  1 
ATOM   2125 C  CG1 . ILE   A 1 287 ? 1.134   17.867  -20.775 1.00 39.61  ? 424 ILE   A CG1 1 
ATOM   2126 C  CG2 . ILE   A 1 287 ? -0.119  17.709  -18.666 1.00 41.69  ? 424 ILE   A CG2 1 
ATOM   2127 C  CD1 . ILE   A 1 287 ? 0.394   19.136  -21.150 1.00 42.29  ? 424 ILE   A CD1 1 
ATOM   2128 N  N   . ASN   A 1 288 ? 2.119   18.707  -16.208 1.00 44.33  ? 425 ASN   A N   1 
ATOM   2129 C  CA  . ASN   A 1 288 ? 2.380   18.128  -14.899 1.00 45.13  ? 425 ASN   A CA  1 
ATOM   2130 C  C   . ASN   A 1 288 ? 1.411   16.954  -14.780 1.00 45.03  ? 425 ASN   A C   1 
ATOM   2131 O  O   . ASN   A 1 288 ? 0.197   17.149  -14.723 1.00 44.70  ? 425 ASN   A O   1 
ATOM   2132 C  CB  . ASN   A 1 288 ? 2.168   19.183  -13.828 1.00 43.53  ? 425 ASN   A CB  1 
ATOM   2133 C  CG  . ASN   A 1 288 ? 2.872   18.865  -12.547 1.00 49.14  ? 425 ASN   A CG  1 
ATOM   2134 O  OD1 . ASN   A 1 288 ? 3.079   19.753  -11.716 1.00 48.29  ? 425 ASN   A OD1 1 
ATOM   2135 N  ND2 . ASN   A 1 288 ? 3.269   17.602  -12.372 1.00 48.94  ? 425 ASN   A ND2 1 
ATOM   2136 N  N   . MET   A 1 289 ? 1.939   15.728  -14.804 1.00 46.33  ? 426 MET   A N   1 
ATOM   2137 C  CA  . MET   A 1 289 ? 1.124   14.535  -15.034 1.00 46.63  ? 426 MET   A CA  1 
ATOM   2138 C  C   . MET   A 1 289 ? 0.156   14.272  -13.889 1.00 43.55  ? 426 MET   A C   1 
ATOM   2139 O  O   . MET   A 1 289 ? 0.520   14.336  -12.711 1.00 45.36  ? 426 MET   A O   1 
ATOM   2140 C  CB  . MET   A 1 289 ? 2.014   13.306  -15.215 1.00 45.29  ? 426 MET   A CB  1 
ATOM   2141 C  CG  . MET   A 1 289 ? 3.083   13.480  -16.257 1.00 48.55  ? 426 MET   A CG  1 
ATOM   2142 S  SD  . MET   A 1 289 ? 2.448   12.968  -17.855 1.00 53.26  ? 426 MET   A SD  1 
ATOM   2143 C  CE  . MET   A 1 289 ? 1.819   14.513  -18.497 1.00 45.80  ? 426 MET   A CE  1 
ATOM   2144 N  N   . TRP   A 1 290 ? -1.089  13.935  -14.247 1.00 40.73  ? 427 TRP   A N   1 
ATOM   2145 C  CA  . TRP   A 1 290 ? -2.054  13.548  -13.225 1.00 42.32  ? 427 TRP   A CA  1 
ATOM   2146 C  C   . TRP   A 1 290 ? -1.637  12.270  -12.513 1.00 41.32  ? 427 TRP   A C   1 
ATOM   2147 O  O   . TRP   A 1 290 ? -2.123  12.010  -11.405 1.00 43.61  ? 427 TRP   A O   1 
ATOM   2148 C  CB  . TRP   A 1 290 ? -3.453  13.350  -13.814 1.00 39.28  ? 427 TRP   A CB  1 
ATOM   2149 C  CG  . TRP   A 1 290 ? -3.527  12.278  -14.814 1.00 38.44  ? 427 TRP   A CG  1 
ATOM   2150 C  CD1 . TRP   A 1 290 ? -3.369  12.413  -16.157 1.00 36.47  ? 427 TRP   A CD1 1 
ATOM   2151 C  CD2 . TRP   A 1 290 ? -3.839  10.894  -14.583 1.00 37.39  ? 427 TRP   A CD2 1 
ATOM   2152 N  NE1 . TRP   A 1 290 ? -3.526  11.203  -16.776 1.00 35.11  ? 427 TRP   A NE1 1 
ATOM   2153 C  CE2 . TRP   A 1 290 ? -3.826  10.256  -15.834 1.00 35.87  ? 427 TRP   A CE2 1 
ATOM   2154 C  CE3 . TRP   A 1 290 ? -4.123  10.137  -13.445 1.00 38.43  ? 427 TRP   A CE3 1 
ATOM   2155 C  CZ2 . TRP   A 1 290 ? -4.086  8.905   -15.981 1.00 36.79  ? 427 TRP   A CZ2 1 
ATOM   2156 C  CZ3 . TRP   A 1 290 ? -4.385  8.788   -13.601 1.00 38.64  ? 427 TRP   A CZ3 1 
ATOM   2157 C  CH2 . TRP   A 1 290 ? -4.364  8.191   -14.857 1.00 34.71  ? 427 TRP   A CH2 1 
ATOM   2158 N  N   . GLN   A 1 291 ? -0.743  11.479  -13.113 1.00 37.10  ? 428 GLN   A N   1 
ATOM   2159 C  CA  . GLN   A 1 291 ? -0.250  10.263  -12.475 1.00 42.73  ? 428 GLN   A CA  1 
ATOM   2160 C  C   . GLN   A 1 291 ? 0.795   10.520  -11.405 1.00 43.97  ? 428 GLN   A C   1 
ATOM   2161 O  O   . GLN   A 1 291 ? 1.298   9.558   -10.823 1.00 45.15  ? 428 GLN   A O   1 
ATOM   2162 C  CB  . GLN   A 1 291 ? 0.348   9.322   -13.517 1.00 39.71  ? 428 GLN   A CB  1 
ATOM   2163 C  CG  . GLN   A 1 291 ? -0.616  9.075   -14.612 1.00 36.90  ? 428 GLN   A CG  1 
ATOM   2164 C  CD  . GLN   A 1 291 ? -0.186  9.768   -15.881 1.00 36.64  ? 428 GLN   A CD  1 
ATOM   2165 O  OE1 . GLN   A 1 291 ? -0.148  11.000  -15.942 1.00 41.65  ? 428 GLN   A OE1 1 
ATOM   2166 N  NE2 . GLN   A 1 291 ? 0.090   8.997   -16.913 1.00 35.53  ? 428 GLN   A NE2 1 
ATOM   2167 N  N   . GLY   A 1 292 ? 1.170   11.763  -11.143 1.00 44.83  ? 429 GLY   A N   1 
ATOM   2168 C  CA  . GLY   A 1 292 ? 2.182   11.961  -10.126 1.00 49.61  ? 429 GLY   A CA  1 
ATOM   2169 C  C   . GLY   A 1 292 ? 3.621   11.932  -10.595 1.00 49.93  ? 429 GLY   A C   1 
ATOM   2170 O  O   . GLY   A 1 292 ? 4.518   12.286  -9.822  1.00 51.59  ? 429 GLY   A O   1 
ATOM   2171 N  N   . THR   A 1 293 ? 3.873   11.538  -11.835 1.00 48.36  ? 430 THR   A N   1 
ATOM   2172 C  CA  . THR   A 1 293 ? 5.216   11.270  -12.323 1.00 53.45  ? 430 THR   A CA  1 
ATOM   2173 C  C   . THR   A 1 293 ? 5.976   12.517  -12.745 1.00 53.78  ? 430 THR   A C   1 
ATOM   2174 O  O   . THR   A 1 293 ? 7.117   12.397  -13.205 1.00 60.85  ? 430 THR   A O   1 
ATOM   2175 C  CB  . THR   A 1 293 ? 5.114   10.288  -13.475 1.00 59.08  ? 430 THR   A CB  1 
ATOM   2176 O  OG1 . THR   A 1 293 ? 4.472   10.934  -14.580 1.00 61.81  ? 430 THR   A OG1 1 
ATOM   2177 C  CG2 . THR   A 1 293 ? 4.276   9.107   -13.037 1.00 50.65  ? 430 THR   A CG2 1 
ATOM   2178 N  N   . GLY   A 1 294 ? 5.389   13.693  -12.572 1.00 54.23  ? 431 GLY   A N   1 
ATOM   2179 C  CA  . GLY   A 1 294 ? 6.059   14.954  -12.788 1.00 56.57  ? 431 GLY   A CA  1 
ATOM   2180 C  C   . GLY   A 1 294 ? 5.670   15.607  -14.100 1.00 53.85  ? 431 GLY   A C   1 
ATOM   2181 O  O   . GLY   A 1 294 ? 4.579   15.403  -14.639 1.00 48.95  ? 431 GLY   A O   1 
ATOM   2182 N  N   . GLN   A 1 295 ? 6.601   16.407  -14.624 1.00 57.37  ? 432 GLN   A N   1 
ATOM   2183 C  CA  . GLN   A 1 295 ? 6.412   17.135  -15.874 1.00 55.94  ? 432 GLN   A CA  1 
ATOM   2184 C  C   . GLN   A 1 295 ? 6.867   16.290  -17.054 1.00 53.60  ? 432 GLN   A C   1 
ATOM   2185 O  O   . GLN   A 1 295 ? 7.884   15.593  -16.980 1.00 55.16  ? 432 GLN   A O   1 
ATOM   2186 C  CB  . GLN   A 1 295 ? 7.183   18.463  -15.865 1.00 57.32  ? 432 GLN   A CB  1 
ATOM   2187 C  CG  . GLN   A 1 295 ? 6.323   19.703  -15.675 1.00 53.42  ? 432 GLN   A CG  1 
ATOM   2188 C  CD  . GLN   A 1 295 ? 7.137   20.935  -15.327 1.00 57.35  ? 432 GLN   A CD  1 
ATOM   2189 O  OE1 . GLN   A 1 295 ? 8.122   20.850  -14.596 1.00 63.24  ? 432 GLN   A OE1 1 
ATOM   2190 N  NE2 . GLN   A 1 295 ? 6.725   22.091  -15.845 1.00 50.04  ? 432 GLN   A NE2 1 
ATOM   2191 N  N   . ALA   A 1 296 ? 6.110   16.365  -18.147 1.00 50.46  ? 433 ALA   A N   1 
ATOM   2192 C  CA  . ALA   A 1 296 ? 6.424   15.619  -19.356 1.00 49.72  ? 433 ALA   A CA  1 
ATOM   2193 C  C   . ALA   A 1 296 ? 6.039   16.452  -20.565 1.00 48.80  ? 433 ALA   A C   1 
ATOM   2194 O  O   . ALA   A 1 296 ? 5.013   17.138  -20.551 1.00 47.02  ? 433 ALA   A O   1 
ATOM   2195 C  CB  . ALA   A 1 296 ? 5.696   14.266  -19.402 1.00 50.63  ? 433 ALA   A CB  1 
ATOM   2196 N  N   . MET   A 1 297 ? 6.847   16.360  -21.619 1.00 49.83  ? 434 MET   A N   1 
ATOM   2197 C  CA  . MET   A 1 297 ? 6.706   17.194  -22.803 1.00 47.90  ? 434 MET   A CA  1 
ATOM   2198 C  C   . MET   A 1 297 ? 6.301   16.342  -23.992 1.00 47.15  ? 434 MET   A C   1 
ATOM   2199 O  O   . MET   A 1 297 ? 6.934   15.322  -24.274 1.00 50.09  ? 434 MET   A O   1 
ATOM   2200 C  CB  . MET   A 1 297 ? 8.007   17.939  -23.106 1.00 50.92  ? 434 MET   A CB  1 
ATOM   2201 C  CG  . MET   A 1 297 ? 7.856   19.080  -24.115 1.00 48.41  ? 434 MET   A CG  1 
ATOM   2202 S  SD  . MET   A 1 297 ? 9.417   19.668  -24.832 1.00 54.28  ? 434 MET   A SD  1 
ATOM   2203 C  CE  . MET   A 1 297 ? 9.112   21.439  -24.906 1.00 49.92  ? 434 MET   A CE  1 
ATOM   2204 N  N   . TYR   A 1 298 ? 5.255   16.781  -24.681 1.00 46.71  ? 435 TYR   A N   1 
ATOM   2205 C  CA  . TYR   A 1 298 ? 4.668   16.148  -25.846 1.00 43.64  ? 435 TYR   A CA  1 
ATOM   2206 C  C   . TYR   A 1 298 ? 4.933   17.009  -27.074 1.00 46.09  ? 435 TYR   A C   1 
ATOM   2207 O  O   . TYR   A 1 298 ? 5.427   18.139  -26.984 1.00 43.76  ? 435 TYR   A O   1 
ATOM   2208 C  CB  . TYR   A 1 298 ? 3.160   15.960  -25.639 1.00 46.46  ? 435 TYR   A CB  1 
ATOM   2209 C  CG  . TYR   A 1 298 ? 2.854   14.932  -24.584 1.00 45.68  ? 435 TYR   A CG  1 
ATOM   2210 C  CD1 . TYR   A 1 298 ? 2.879   15.265  -23.235 1.00 43.26  ? 435 TYR   A CD1 1 
ATOM   2211 C  CD2 . TYR   A 1 298 ? 2.610   13.606  -24.933 1.00 43.72  ? 435 TYR   A CD2 1 
ATOM   2212 C  CE1 . TYR   A 1 298 ? 2.627   14.305  -22.256 1.00 45.97  ? 435 TYR   A CE1 1 
ATOM   2213 C  CE2 . TYR   A 1 298 ? 2.354   12.645  -23.973 1.00 45.02  ? 435 TYR   A CE2 1 
ATOM   2214 C  CZ  . TYR   A 1 298 ? 2.367   12.997  -22.634 1.00 46.71  ? 435 TYR   A CZ  1 
ATOM   2215 O  OH  . TYR   A 1 298 ? 2.123   12.056  -21.658 1.00 46.82  ? 435 TYR   A OH  1 
ATOM   2216 N  N   . ALA   A 1 299 ? 4.589   16.454  -28.228 1.00 48.16  ? 436 ALA   A N   1 
ATOM   2217 C  CA  . ALA   A 1 299 ? 4.852   17.091  -29.501 1.00 47.43  ? 436 ALA   A CA  1 
ATOM   2218 C  C   . ALA   A 1 299 ? 3.816   18.175  -29.766 1.00 46.48  ? 436 ALA   A C   1 
ATOM   2219 O  O   . ALA   A 1 299 ? 2.779   18.232  -29.100 1.00 46.13  ? 436 ALA   A O   1 
ATOM   2220 C  CB  . ALA   A 1 299 ? 4.839   16.051  -30.617 1.00 46.49  ? 436 ALA   A CB  1 
ATOM   2221 N  N   . PRO   A 1 300 ? 4.089   19.071  -30.709 1.00 46.22  ? 437 PRO   A N   1 
ATOM   2222 C  CA  . PRO   A 1 300 ? 3.160   20.175  -30.973 1.00 47.40  ? 437 PRO   A CA  1 
ATOM   2223 C  C   . PRO   A 1 300 ? 1.869   19.666  -31.596 1.00 48.24  ? 437 PRO   A C   1 
ATOM   2224 O  O   . PRO   A 1 300 ? 1.818   18.541  -32.110 1.00 48.89  ? 437 PRO   A O   1 
ATOM   2225 C  CB  . PRO   A 1 300 ? 3.945   21.086  -31.928 1.00 47.80  ? 437 PRO   A CB  1 
ATOM   2226 C  CG  . PRO   A 1 300 ? 5.397   20.754  -31.659 1.00 46.56  ? 437 PRO   A CG  1 
ATOM   2227 C  CD  . PRO   A 1 300 ? 5.395   19.275  -31.362 1.00 47.64  ? 437 PRO   A CD  1 
ATOM   2228 N  N   . PRO   A 1 301 ? 0.793   20.445  -31.510 1.00 47.46  ? 438 PRO   A N   1 
ATOM   2229 C  CA  . PRO   A 1 301 ? -0.523  19.930  -31.909 1.00 48.96  ? 438 PRO   A CA  1 
ATOM   2230 C  C   . PRO   A 1 301 ? -0.544  19.407  -33.339 1.00 51.04  ? 438 PRO   A C   1 
ATOM   2231 O  O   . PRO   A 1 301 ? 0.116   19.938  -34.238 1.00 52.32  ? 438 PRO   A O   1 
ATOM   2232 C  CB  . PRO   A 1 301 ? -1.449  21.141  -31.742 1.00 43.29  ? 438 PRO   A CB  1 
ATOM   2233 C  CG  . PRO   A 1 301 ? -0.547  22.315  -31.557 1.00 48.39  ? 438 PRO   A CG  1 
ATOM   2234 C  CD  . PRO   A 1 301 ? 0.732   21.824  -31.008 1.00 43.46  ? 438 PRO   A CD  1 
ATOM   2235 N  N   . ILE   A 1 302 ? -1.325  18.346  -33.539 1.00 52.12  ? 439 ILE   A N   1 
ATOM   2236 C  CA  . ILE   A 1 302 ? -1.625  17.908  -34.886 1.00 56.72  ? 439 ILE   A CA  1 
ATOM   2237 C  C   . ILE   A 1 302 ? -2.258  19.055  -35.663 1.00 57.20  ? 439 ILE   A C   1 
ATOM   2238 O  O   . ILE   A 1 302 ? -2.793  20.016  -35.090 1.00 53.99  ? 439 ILE   A O   1 
ATOM   2239 C  CB  . ILE   A 1 302 ? -2.565  16.697  -34.866 1.00 58.02  ? 439 ILE   A CB  1 
ATOM   2240 C  CG1 . ILE   A 1 302 ? -3.609  16.867  -33.756 1.00 55.89  ? 439 ILE   A CG1 1 
ATOM   2241 C  CG2 . ILE   A 1 302 ? -1.767  15.457  -34.639 1.00 56.56  ? 439 ILE   A CG2 1 
ATOM   2242 C  CD1 . ILE   A 1 302 ? -4.891  16.056  -33.964 1.00 54.78  ? 439 ILE   A CD1 1 
ATOM   2243 N  N   . ASP   A 1 303 ? -2.213  18.938  -36.990 1.00 59.39  ? 440 ASP   A N   1 
ATOM   2244 C  CA  . ASP   A 1 303 ? -2.835  19.917  -37.866 1.00 60.07  ? 440 ASP   A CA  1 
ATOM   2245 C  C   . ASP   A 1 303 ? -4.250  19.491  -38.217 1.00 59.95  ? 440 ASP   A C   1 
ATOM   2246 O  O   . ASP   A 1 303 ? -4.541  18.308  -38.406 1.00 64.86  ? 440 ASP   A O   1 
ATOM   2247 C  CB  . ASP   A 1 303 ? -2.024  20.113  -39.143 1.00 62.42  ? 440 ASP   A CB  1 
ATOM   2248 C  CG  . ASP   A 1 303 ? -0.683  20.758  -38.878 1.00 64.53  ? 440 ASP   A CG  1 
ATOM   2249 O  OD1 . ASP   A 1 303 ? -0.647  22.000  -38.676 1.00 61.43  ? 440 ASP   A OD1 1 
ATOM   2250 O  OD2 . ASP   A 1 303 ? 0.329   20.015  -38.869 1.00 63.69  ? 440 ASP   A OD2 1 
ATOM   2251 N  N   . GLY   A 1 304 ? -5.131  20.472  -38.284 1.00 57.65  ? 441 GLY   A N   1 
ATOM   2252 C  CA  . GLY   A 1 304 ? -6.524  20.250  -38.603 1.00 54.17  ? 441 GLY   A CA  1 
ATOM   2253 C  C   . GLY   A 1 304 ? -7.410  20.614  -37.427 1.00 50.26  ? 441 GLY   A C   1 
ATOM   2254 O  O   . GLY   A 1 304 ? -6.951  21.069  -36.378 1.00 49.21  ? 441 GLY   A O   1 
ATOM   2255 N  N   . LYS   A 1 305 ? -8.706  20.397  -37.632 1.00 49.91  ? 442 LYS   A N   1 
ATOM   2256 C  CA  . LYS   A 1 305 ? -9.724  20.756  -36.653 1.00 48.52  ? 442 LYS   A CA  1 
ATOM   2257 C  C   . LYS   A 1 305 ? -9.742  19.715  -35.537 1.00 46.49  ? 442 LYS   A C   1 
ATOM   2258 O  O   . LYS   A 1 305 ? -10.018 18.535  -35.784 1.00 50.91  ? 442 LYS   A O   1 
ATOM   2259 C  CB  . LYS   A 1 305 ? -11.086 20.865  -37.339 1.00 46.12  ? 442 LYS   A CB  1 
ATOM   2260 C  CG  . LYS   A 1 305 ? -12.305 20.656  -36.431 1.00 45.29  ? 442 LYS   A CG  1 
ATOM   2261 C  CD  . LYS   A 1 305 ? -13.550 21.416  -36.943 1.00 46.23  ? 442 LYS   A CD  1 
ATOM   2262 C  CE  . LYS   A 1 305 ? -14.799 21.098  -36.138 1.00 43.10  ? 442 LYS   A CE  1 
ATOM   2263 N  NZ  . LYS   A 1 305 ? -15.366 19.771  -36.516 1.00 48.96  ? 442 LYS   A NZ  1 
ATOM   2264 N  N   . ILE   A 1 306 ? -9.410  20.144  -34.324 1.00 40.50  ? 443 ILE   A N   1 
ATOM   2265 C  CA  . ILE   A 1 306 ? -9.457  19.306  -33.134 1.00 40.86  ? 443 ILE   A CA  1 
ATOM   2266 C  C   . ILE   A 1 306 ? -10.715 19.708  -32.375 1.00 42.22  ? 443 ILE   A C   1 
ATOM   2267 O  O   . ILE   A 1 306 ? -10.760 20.786  -31.765 1.00 38.82  ? 443 ILE   A O   1 
ATOM   2268 C  CB  . ILE   A 1 306 ? -8.211  19.486  -32.265 1.00 42.37  ? 443 ILE   A CB  1 
ATOM   2269 C  CG1 . ILE   A 1 306 ? -6.947  19.571  -33.118 1.00 42.86  ? 443 ILE   A CG1 1 
ATOM   2270 C  CG2 . ILE   A 1 306 ? -8.082  18.340  -31.290 1.00 42.69  ? 443 ILE   A CG2 1 
ATOM   2271 C  CD1 . ILE   A 1 306 ? -5.674  19.571  -32.293 1.00 44.71  ? 443 ILE   A CD1 1 
ATOM   2272 N  N   . ASN   A 1 307 ? -11.743 18.846  -32.405 1.00 40.33  ? 444 ASN   A N   1 
ATOM   2273 C  CA  . ASN   A 1 307 ? -13.029 19.162  -31.799 1.00 38.60  ? 444 ASN   A CA  1 
ATOM   2274 C  C   . ASN   A 1 307 ? -13.468 18.018  -30.895 1.00 40.94  ? 444 ASN   A C   1 
ATOM   2275 O  O   . ASN   A 1 307 ? -13.290 16.847  -31.235 1.00 45.45  ? 444 ASN   A O   1 
ATOM   2276 C  CB  . ASN   A 1 307 ? -14.096 19.420  -32.858 1.00 38.22  ? 444 ASN   A CB  1 
ATOM   2277 C  CG  . ASN   A 1 307 ? -15.484 19.400  -32.287 1.00 41.54  ? 444 ASN   A CG  1 
ATOM   2278 O  OD1 . ASN   A 1 307 ? -15.982 20.434  -31.815 1.00 40.35  ? 444 ASN   A OD1 1 
ATOM   2279 N  ND2 . ASN   A 1 307 ? -16.126 18.234  -32.308 1.00 42.81  ? 444 ASN   A ND2 1 
ATOM   2280 N  N   . CYS   A 1 308 ? -14.019 18.374  -29.734 1.00 39.50  ? 445 CYS   A N   1 
ATOM   2281 C  CA  . CYS   A 1 308 ? -14.585 17.448  -28.755 1.00 41.19  ? 445 CYS   A CA  1 
ATOM   2282 C  C   . CYS   A 1 308 ? -15.855 18.084  -28.215 1.00 40.33  ? 445 CYS   A C   1 
ATOM   2283 O  O   . CYS   A 1 308 ? -15.801 19.181  -27.647 1.00 34.53  ? 445 CYS   A O   1 
ATOM   2284 C  CB  . CYS   A 1 308 ? -13.635 17.178  -27.577 1.00 40.47  ? 445 CYS   A CB  1 
ATOM   2285 S  SG  . CYS   A 1 308 ? -12.162 16.155  -27.837 1.00 49.08  ? 445 CYS   A SG  1 
ATOM   2286 N  N   . VAL   A 1 309 ? -16.989 17.419  -28.376 1.00 38.41  ? 446 VAL   A N   1 
ATOM   2287 C  CA  . VAL   A 1 309 ? -18.217 17.888  -27.745 1.00 40.16  ? 446 VAL   A CA  1 
ATOM   2288 C  C   . VAL   A 1 309 ? -18.568 16.899  -26.645 1.00 39.68  ? 446 VAL   A C   1 
ATOM   2289 O  O   . VAL   A 1 309 ? -18.748 15.696  -26.893 1.00 37.82  ? 446 VAL   A O   1 
ATOM   2290 C  CB  . VAL   A 1 309 ? -19.365 18.079  -28.741 1.00 38.44  ? 446 VAL   A CB  1 
ATOM   2291 C  CG1 . VAL   A 1 309 ? -20.515 18.758  -28.040 1.00 40.91  ? 446 VAL   A CG1 1 
ATOM   2292 C  CG2 . VAL   A 1 309 ? -18.879 18.921  -29.903 1.00 39.01  ? 446 VAL   A CG2 1 
ATOM   2293 N  N   . SER   A 1 310 ? -18.621 17.410  -25.423 1.00 32.42  ? 447 SER   A N   1 
ATOM   2294 C  CA  . SER   A 1 310 ? -18.780 16.588  -24.245 1.00 36.27  ? 447 SER   A CA  1 
ATOM   2295 C  C   . SER   A 1 310 ? -19.965 17.063  -23.421 1.00 39.30  ? 447 SER   A C   1 
ATOM   2296 O  O   . SER   A 1 310 ? -20.455 18.192  -23.549 1.00 35.89  ? 447 SER   A O   1 
ATOM   2297 C  CB  . SER   A 1 310 ? -17.493 16.571  -23.401 1.00 38.72  ? 447 SER   A CB  1 
ATOM   2298 O  OG  . SER   A 1 310 ? -16.333 16.403  -24.218 1.00 36.47  ? 447 SER   A OG  1 
ATOM   2299 N  N   . ASN   A 1 311 ? -20.410 16.152  -22.575 1.00 35.98  ? 448 ASN   A N   1 
ATOM   2300 C  CA  . ASN   A 1 311 ? -21.422 16.407  -21.572 1.00 32.95  ? 448 ASN   A CA  1 
ATOM   2301 C  C   . ASN   A 1 311 ? -20.724 16.772  -20.276 1.00 37.19  ? 448 ASN   A C   1 
ATOM   2302 O  O   . ASN   A 1 311 ? -19.912 15.992  -19.769 1.00 35.27  ? 448 ASN   A O   1 
ATOM   2303 C  CB  . ASN   A 1 311 ? -22.260 15.162  -21.318 1.00 38.54  ? 448 ASN   A CB  1 
ATOM   2304 C  CG  . ASN   A 1 311 ? -23.356 14.960  -22.321 1.00 44.54  ? 448 ASN   A CG  1 
ATOM   2305 O  OD1 . ASN   A 1 311 ? -23.833 15.895  -22.968 1.00 47.11  ? 448 ASN   A OD1 1 
ATOM   2306 N  ND2 . ASN   A 1 311 ? -23.779 13.706  -22.444 1.00 47.20  ? 448 ASN   A ND2 1 
ATOM   2307 N  N   . ILE   A 1 312 ? -21.038 17.940  -19.732 1.00 40.57  ? 449 ILE   A N   1 
ATOM   2308 C  CA  . ILE   A 1 312 ? -20.697 18.228  -18.347 1.00 38.91  ? 449 ILE   A CA  1 
ATOM   2309 C  C   . ILE   A 1 312 ? -21.722 17.487  -17.501 1.00 39.65  ? 449 ILE   A C   1 
ATOM   2310 O  O   . ILE   A 1 312 ? -22.922 17.764  -17.585 1.00 40.49  ? 449 ILE   A O   1 
ATOM   2311 C  CB  . ILE   A 1 312 ? -20.700 19.726  -18.038 1.00 36.25  ? 449 ILE   A CB  1 
ATOM   2312 C  CG1 . ILE   A 1 312 ? -19.516 20.399  -18.734 1.00 33.81  ? 449 ILE   A CG1 1 
ATOM   2313 C  CG2 . ILE   A 1 312 ? -20.595 19.905  -16.537 1.00 33.86  ? 449 ILE   A CG2 1 
ATOM   2314 C  CD1 . ILE   A 1 312 ? -19.665 21.888  -18.928 1.00 35.40  ? 449 ILE   A CD1 1 
ATOM   2315 N  N   . THR   A 1 313 ? -21.251 16.528  -16.699 1.00 38.79  ? 450 THR   A N   1 
ATOM   2316 C  CA  . THR   A 1 313 ? -22.123 15.737  -15.851 1.00 37.80  ? 450 THR   A CA  1 
ATOM   2317 C  C   . THR   A 1 313 ? -21.792 15.875  -14.374 1.00 36.73  ? 450 THR   A C   1 
ATOM   2318 O  O   . THR   A 1 313 ? -22.524 15.334  -13.540 1.00 33.49  ? 450 THR   A O   1 
ATOM   2319 C  CB  . THR   A 1 313 ? -22.057 14.261  -16.269 1.00 37.70  ? 450 THR   A CB  1 
ATOM   2320 O  OG1 . THR   A 1 313 ? -20.687 13.839  -16.325 1.00 36.28  ? 450 THR   A OG1 1 
ATOM   2321 C  CG2 . THR   A 1 313 ? -22.630 14.106  -17.665 1.00 35.65  ? 450 THR   A CG2 1 
ATOM   2322 N  N   . GLY   A 1 314 ? -20.725 16.589  -14.024 1.00 38.77  ? 451 GLY   A N   1 
ATOM   2323 C  CA  . GLY   A 1 314 ? -20.448 16.857  -12.627 1.00 37.75  ? 451 GLY   A CA  1 
ATOM   2324 C  C   . GLY   A 1 314 ? -19.437 17.966  -12.453 1.00 39.95  ? 451 GLY   A C   1 
ATOM   2325 O  O   . GLY   A 1 314 ? -18.795 18.414  -13.414 1.00 35.81  ? 451 GLY   A O   1 
ATOM   2326 N  N   . ILE   A 1 315 ? -19.284 18.391  -11.193 1.00 41.06  ? 452 ILE   A N   1 
ATOM   2327 C  CA  . ILE   A 1 315 ? -18.371 19.466  -10.816 1.00 37.01  ? 452 ILE   A CA  1 
ATOM   2328 C  C   . ILE   A 1 315 ? -17.577 19.056  -9.582  1.00 39.25  ? 452 ILE   A C   1 
ATOM   2329 O  O   . ILE   A 1 315 ? -18.102 18.392  -8.680  1.00 37.50  ? 452 ILE   A O   1 
ATOM   2330 C  CB  . ILE   A 1 315 ? -19.123 20.788  -10.553 1.00 38.13  ? 452 ILE   A CB  1 
ATOM   2331 C  CG1 . ILE   A 1 315 ? -20.012 21.156  -11.740 1.00 39.29  ? 452 ILE   A CG1 1 
ATOM   2332 C  CG2 . ILE   A 1 315 ? -18.144 21.918  -10.278 1.00 38.16  ? 452 ILE   A CG2 1 
ATOM   2333 C  CD1 . ILE   A 1 315 ? -20.832 22.439  -11.521 1.00 39.66  ? 452 ILE   A CD1 1 
ATOM   2334 N  N   . LEU   A 1 316 ? -16.314 19.480  -9.535  1.00 41.29  ? 453 LEU   A N   1 
ATOM   2335 C  CA  . LEU   A 1 316 ? -15.409 19.212  -8.420  1.00 38.64  ? 453 LEU   A CA  1 
ATOM   2336 C  C   . LEU   A 1 316 ? -15.153 20.516  -7.677  1.00 42.07  ? 453 LEU   A C   1 
ATOM   2337 O  O   . LEU   A 1 316 ? -14.725 21.505  -8.284  1.00 44.34  ? 453 LEU   A O   1 
ATOM   2338 C  CB  . LEU   A 1 316 ? -14.095 18.608  -8.910  1.00 38.98  ? 453 LEU   A CB  1 
ATOM   2339 C  CG  . LEU   A 1 316 ? -14.257 17.299  -9.689  1.00 39.10  ? 453 LEU   A CG  1 
ATOM   2340 C  CD1 . LEU   A 1 316 ? -12.955 16.902  -10.380 1.00 36.29  ? 453 LEU   A CD1 1 
ATOM   2341 C  CD2 . LEU   A 1 316 ? -14.756 16.194  -8.756  1.00 36.34  ? 453 LEU   A CD2 1 
ATOM   2342 N  N   . LEU   A 1 317 ? -15.436 20.529  -6.375  1.00 41.03  ? 454 LEU   A N   1 
ATOM   2343 C  CA  . LEU   A 1 317 ? -15.352 21.755  -5.592  1.00 41.31  ? 454 LEU   A CA  1 
ATOM   2344 C  C   . LEU   A 1 317 ? -14.607 21.525  -4.286  1.00 42.41  ? 454 LEU   A C   1 
ATOM   2345 O  O   . LEU   A 1 317 ? -14.636 20.431  -3.710  1.00 43.47  ? 454 LEU   A O   1 
ATOM   2346 C  CB  . LEU   A 1 317 ? -16.742 22.331  -5.268  1.00 41.65  ? 454 LEU   A CB  1 
ATOM   2347 C  CG  . LEU   A 1 317 ? -17.585 22.804  -6.459  1.00 41.28  ? 454 LEU   A CG  1 
ATOM   2348 C  CD1 . LEU   A 1 317 ? -19.067 22.901  -6.092  1.00 39.12  ? 454 LEU   A CD1 1 
ATOM   2349 C  CD2 . LEU   A 1 317 ? -17.078 24.117  -7.025  1.00 41.46  ? 454 LEU   A CD2 1 
ATOM   2350 N  N   . THR   A 1 318 ? -13.923 22.577  -3.845  1.00 43.19  ? 455 THR   A N   1 
ATOM   2351 C  CA  . THR   A 1 318 ? -13.383 22.694  -2.502  1.00 44.42  ? 455 THR   A CA  1 
ATOM   2352 C  C   . THR   A 1 318 ? -14.166 23.775  -1.779  1.00 43.96  ? 455 THR   A C   1 
ATOM   2353 O  O   . THR   A 1 318 ? -14.587 24.758  -2.396  1.00 45.26  ? 455 THR   A O   1 
ATOM   2354 C  CB  . THR   A 1 318 ? -11.901 23.070  -2.520  1.00 46.98  ? 455 THR   A CB  1 
ATOM   2355 O  OG1 . THR   A 1 318 ? -11.317 22.706  -3.778  1.00 49.39  ? 455 THR   A OG1 1 
ATOM   2356 C  CG2 . THR   A 1 318 ? -11.183 22.355  -1.412  1.00 45.86  ? 455 THR   A CG2 1 
ATOM   2357 N  N   . ARG   A 1 319 ? -14.382 23.589  -0.483  1.00 48.20  ? 456 ARG   A N   1 
ATOM   2358 C  CA  . ARG   A 1 319 ? -15.085 24.574  0.321   1.00 49.89  ? 456 ARG   A CA  1 
ATOM   2359 C  C   . ARG   A 1 319 ? -14.088 25.283  1.216   1.00 51.64  ? 456 ARG   A C   1 
ATOM   2360 O  O   . ARG   A 1 319 ? -13.371 24.636  1.987   1.00 52.49  ? 456 ARG   A O   1 
ATOM   2361 C  CB  . ARG   A 1 319 ? -16.177 23.960  1.187   1.00 50.94  ? 456 ARG   A CB  1 
ATOM   2362 C  CG  . ARG   A 1 319 ? -16.881 25.041  1.987   1.00 50.08  ? 456 ARG   A CG  1 
ATOM   2363 C  CD  . ARG   A 1 319 ? -18.147 24.555  2.639   1.00 48.81  ? 456 ARG   A CD  1 
ATOM   2364 N  NE  . ARG   A 1 319 ? -17.904 23.508  3.622   1.00 53.42  ? 456 ARG   A NE  1 
ATOM   2365 C  CZ  . ARG   A 1 319 ? -17.616 23.739  4.896   1.00 55.65  ? 456 ARG   A CZ  1 
ATOM   2366 N  NH1 . ARG   A 1 319 ? -17.485 24.971  5.361   1.00 57.77  ? 456 ARG   A NH1 1 
ATOM   2367 N  NH2 . ARG   A 1 319 ? -17.450 22.711  5.721   1.00 57.60  ? 456 ARG   A NH2 1 
ATOM   2368 N  N   . ASP   A 1 320 ? -14.057 26.609  1.110   1.00 51.99  ? 457 ASP   A N   1 
ATOM   2369 C  CA  . ASP   A 1 320 ? -13.124 27.433  1.863   1.00 56.29  ? 457 ASP   A CA  1 
ATOM   2370 C  C   . ASP   A 1 320 ? -13.302 27.217  3.366   1.00 58.38  ? 457 ASP   A C   1 
ATOM   2371 O  O   . ASP   A 1 320 ? -14.395 26.910  3.848   1.00 58.26  ? 457 ASP   A O   1 
ATOM   2372 C  CB  . ASP   A 1 320 ? -13.339 28.911  1.515   1.00 56.55  ? 457 ASP   A CB  1 
ATOM   2373 C  CG  . ASP   A 1 320 ? -12.406 29.411  0.414   1.00 57.00  ? 457 ASP   A CG  1 
ATOM   2374 O  OD1 . ASP   A 1 320 ? -11.889 28.598  -0.381  1.00 56.90  ? 457 ASP   A OD1 1 
ATOM   2375 O  OD2 . ASP   A 1 320 ? -12.176 30.637  0.364   1.00 55.09  ? 457 ASP   A OD2 1 
ATOM   2376 N  N   . GLY   A 1 321 ? -12.208 27.377  4.113   1.00 60.12  ? 458 GLY   A N   1 
ATOM   2377 C  CA  . GLY   A 1 321 ? -12.262 27.351  5.557   1.00 61.88  ? 458 GLY   A CA  1 
ATOM   2378 C  C   . GLY   A 1 321 ? -12.500 28.736  6.146   1.00 62.07  ? 458 GLY   A C   1 
ATOM   2379 O  O   . GLY   A 1 321 ? -12.460 29.751  5.460   1.00 61.08  ? 458 GLY   A O   1 
ATOM   2380 N  N   . GLY   A 1 322 ? -12.753 28.751  7.452   1.00 63.47  ? 459 GLY   A N   1 
ATOM   2381 C  CA  . GLY   A 1 322 ? -12.916 29.983  8.198   1.00 65.62  ? 459 GLY   A CA  1 
ATOM   2382 C  C   . GLY   A 1 322 ? -14.194 30.738  7.880   1.00 67.40  ? 459 GLY   A C   1 
ATOM   2383 O  O   . GLY   A 1 322 ? -14.185 31.974  7.803   1.00 66.89  ? 459 GLY   A O   1 
ATOM   2384 N  N   . ALA   A 1 323 ? -15.307 30.008  7.681   1.00 65.44  ? 460 ALA   A N   1 
ATOM   2385 C  CA  . ALA   A 1 323 ? -16.602 30.621  7.388   1.00 64.65  ? 460 ALA   A CA  1 
ATOM   2386 C  C   . ALA   A 1 323 ? -17.651 30.321  8.459   1.00 63.62  ? 460 ALA   A C   1 
ATOM   2387 O  O   . ALA   A 1 323 ? -18.851 30.438  8.194   1.00 60.02  ? 460 ALA   A O   1 
ATOM   2388 C  CB  . ALA   A 1 323 ? -17.124 30.180  6.012   1.00 60.41  ? 460 ALA   A CB  1 
ATOM   2389 N  N   . ASN   A 1 324 ? -17.227 29.943  9.664   1.00 65.81  ? 461 ASN   A N   1 
ATOM   2390 C  CA  . ASN   A 1 324 ? -18.126 29.545  10.745  1.00 64.36  ? 461 ASN   A CA  1 
ATOM   2391 C  C   . ASN   A 1 324 ? -18.744 30.721  11.482  1.00 60.74  ? 461 ASN   A C   1 
ATOM   2392 O  O   . ASN   A 1 324 ? -19.615 30.520  12.342  1.00 62.28  ? 461 ASN   A O   1 
ATOM   2393 C  CB  . ASN   A 1 324 ? -17.352 28.674  11.725  1.00 69.76  ? 461 ASN   A CB  1 
ATOM   2394 C  CG  . ASN   A 1 324 ? -15.837 28.821  11.559  1.00 71.43  ? 461 ASN   A CG  1 
ATOM   2395 O  OD1 . ASN   A 1 324 ? -15.286 29.934  11.593  1.00 70.18  ? 461 ASN   A OD1 1 
ATOM   2396 N  ND2 . ASN   A 1 324 ? -15.163 27.692  11.341  1.00 74.90  ? 461 ASN   A ND2 1 
ATOM   2397 N  N   . ASN   A 1 325 ? -18.313 31.933  11.169  1.00 58.87  ? 462 ASN   A N   1 
ATOM   2398 C  CA  . ASN   A 1 325 ? -18.845 33.130  11.801  1.00 56.55  ? 462 ASN   A CA  1 
ATOM   2399 C  C   . ASN   A 1 325 ? -19.329 34.130  10.766  1.00 51.74  ? 462 ASN   A C   1 
ATOM   2400 O  O   . ASN   A 1 325 ? -19.319 35.334  10.990  1.00 51.00  ? 462 ASN   A O   1 
ATOM   2401 C  CB  . ASN   A 1 325 ? -17.782 33.731  12.703  1.00 52.70  ? 462 ASN   A CB  1 
ATOM   2402 C  CG  . ASN   A 1 325 ? -17.788 33.082  14.064  1.00 50.54  ? 462 ASN   A CG  1 
ATOM   2403 O  OD1 . ASN   A 1 325 ? -16.771 32.589  14.559  1.00 50.54  ? 462 ASN   A OD1 1 
ATOM   2404 N  ND2 . ASN   A 1 325 ? -18.953 33.084  14.684  1.00 50.72  ? 462 ASN   A ND2 1 
ATOM   2405 N  N   . THR   A 1 326 ? -19.708 33.633  9.605   1.00 51.42  ? 463 THR   A N   1 
ATOM   2406 C  CA  . THR   A 1 326 ? -20.149 34.474  8.516   1.00 50.99  ? 463 THR   A CA  1 
ATOM   2407 C  C   . THR   A 1 326 ? -21.478 33.935  8.015   1.00 48.28  ? 463 THR   A C   1 
ATOM   2408 O  O   . THR   A 1 326 ? -22.030 32.967  8.542   1.00 46.72  ? 463 THR   A O   1 
ATOM   2409 C  CB  . THR   A 1 326 ? -19.135 34.503  7.365   1.00 50.23  ? 463 THR   A CB  1 
ATOM   2410 O  OG1 . THR   A 1 326 ? -18.976 33.175  6.843   1.00 52.15  ? 463 THR   A OG1 1 
ATOM   2411 C  CG2 . THR   A 1 326 ? -17.789 34.939  7.902   1.00 50.58  ? 463 THR   A CG2 1 
ATOM   2412 N  N   . SER   A 1 327 ? -22.025 34.638  7.035   1.00 46.23  ? 464 SER   A N   1 
ATOM   2413 C  CA  . SER   A 1 327 ? -23.258 34.256  6.365   1.00 48.68  ? 464 SER   A CA  1 
ATOM   2414 C  C   . SER   A 1 327 ? -22.962 33.681  4.984   1.00 48.00  ? 464 SER   A C   1 
ATOM   2415 O  O   . SER   A 1 327 ? -23.882 33.491  4.182   1.00 43.21  ? 464 SER   A O   1 
ATOM   2416 C  CB  . SER   A 1 327 ? -24.245 35.439  6.256   1.00 44.68  ? 464 SER   A CB  1 
ATOM   2417 O  OG  . SER   A 1 327 ? -23.754 36.642  5.664   1.00 45.58  ? 464 SER   A OG  1 
ATOM   2418 N  N   . ASN   A 1 328 ? -21.689 33.419  4.666   1.00 47.26  ? 465 ASN   A N   1 
ATOM   2419 C  CA  . ASN   A 1 328 ? -21.343 32.949  3.328   1.00 48.87  ? 465 ASN   A CA  1 
ATOM   2420 C  C   . ASN   A 1 328 ? -20.567 31.638  3.396   1.00 47.04  ? 465 ASN   A C   1 
ATOM   2421 O  O   . ASN   A 1 328 ? -19.822 31.390  4.347   1.00 48.59  ? 465 ASN   A O   1 
ATOM   2422 C  CB  . ASN   A 1 328 ? -20.550 34.031  2.562   1.00 47.48  ? 465 ASN   A CB  1 
ATOM   2423 C  CG  . ASN   A 1 328 ? -21.076 35.421  2.842   1.00 51.31  ? 465 ASN   A CG  1 
ATOM   2424 O  OD1 . ASN   A 1 328 ? -22.237 35.741  2.535   1.00 51.31  ? 465 ASN   A OD1 1 
ATOM   2425 N  ND2 . ASN   A 1 328 ? -20.231 36.262  3.428   1.00 50.73  ? 465 ASN   A ND2 1 
ATOM   2426 N  N   . GLU   A 1 329 ? -20.791 30.779  2.398   1.00 45.94  ? 466 GLU   A N   1 
ATOM   2427 C  CA  . GLU   A 1 329 ? -19.941 29.627  2.110   1.00 45.94  ? 466 GLU   A CA  1 
ATOM   2428 C  C   . GLU   A 1 329 ? -19.370 29.899  0.726   1.00 44.88  ? 466 GLU   A C   1 
ATOM   2429 O  O   . GLU   A 1 329 ? -20.110 30.328  -0.169  1.00 43.23  ? 466 GLU   A O   1 
ATOM   2430 C  CB  . GLU   A 1 329 ? -20.734 28.307  2.123   1.00 47.18  ? 466 GLU   A CB  1 
ATOM   2431 C  CG  . GLU   A 1 329 ? -20.936 27.682  3.495   1.00 47.41  ? 466 GLU   A CG  1 
ATOM   2432 C  CD  . GLU   A 1 329 ? -19.712 27.731  4.393   1.00 49.13  ? 466 GLU   A CD  1 
ATOM   2433 O  OE1 . GLU   A 1 329 ? -18.568 27.615  3.895   1.00 52.68  ? 466 GLU   A OE1 1 
ATOM   2434 O  OE2 . GLU   A 1 329 ? -19.902 27.897  5.615   1.00 54.26  ? 466 GLU   A OE2 1 
ATOM   2435 N  N   . THR   A 1 330 ? -18.060 29.716  0.562   1.00 47.05  ? 467 THR   A N   1 
ATOM   2436 C  CA  . THR   A 1 330 ? -17.376 29.982  -0.698  1.00 47.79  ? 467 THR   A CA  1 
ATOM   2437 C  C   . THR   A 1 330 ? -16.772 28.699  -1.255  1.00 48.94  ? 467 THR   A C   1 
ATOM   2438 O  O   . THR   A 1 330 ? -16.034 27.997  -0.554  1.00 49.90  ? 467 THR   A O   1 
ATOM   2439 C  CB  . THR   A 1 330 ? -16.286 31.036  -0.519  1.00 50.51  ? 467 THR   A CB  1 
ATOM   2440 O  OG1 . THR   A 1 330 ? -15.130 30.673  -1.294  1.00 52.74  ? 467 THR   A OG1 1 
ATOM   2441 C  CG2 . THR   A 1 330 ? -15.910 31.139  0.931   1.00 51.14  ? 467 THR   A CG2 1 
ATOM   2442 N  N   . PHE   A 1 331 ? -17.058 28.427  -2.527  1.00 45.57  ? 468 PHE   A N   1 
ATOM   2443 C  CA  . PHE   A 1 331 ? -16.683 27.190  -3.193  1.00 46.21  ? 468 PHE   A CA  1 
ATOM   2444 C  C   . PHE   A 1 331 ? -15.817 27.482  -4.416  1.00 45.53  ? 468 PHE   A C   1 
ATOM   2445 O  O   . PHE   A 1 331 ? -16.067 28.441  -5.155  1.00 45.25  ? 468 PHE   A O   1 
ATOM   2446 C  CB  . PHE   A 1 331 ? -17.931 26.398  -3.618  1.00 43.93  ? 468 PHE   A CB  1 
ATOM   2447 C  CG  . PHE   A 1 331 ? -18.745 25.853  -2.466  1.00 46.69  ? 468 PHE   A CG  1 
ATOM   2448 C  CD1 . PHE   A 1 331 ? -19.616 26.663  -1.746  1.00 44.89  ? 468 PHE   A CD1 1 
ATOM   2449 C  CD2 . PHE   A 1 331 ? -18.650 24.511  -2.117  1.00 45.50  ? 468 PHE   A CD2 1 
ATOM   2450 C  CE1 . PHE   A 1 331 ? -20.374 26.134  -0.697  1.00 44.91  ? 468 PHE   A CE1 1 
ATOM   2451 C  CE2 . PHE   A 1 331 ? -19.397 23.986  -1.074  1.00 45.31  ? 468 PHE   A CE2 1 
ATOM   2452 C  CZ  . PHE   A 1 331 ? -20.258 24.795  -0.361  1.00 44.19  ? 468 PHE   A CZ  1 
ATOM   2453 N  N   . ARG   A 1 332 ? -14.814 26.628  -4.642  1.00 47.62  ? 469 ARG   A N   1 
ATOM   2454 C  CA  . ARG   A 1 332 ? -13.857 26.789  -5.726  1.00 49.49  ? 469 ARG   A CA  1 
ATOM   2455 C  C   . ARG   A 1 332 ? -13.765 25.498  -6.524  1.00 43.64  ? 469 ARG   A C   1 
ATOM   2456 O  O   . ARG   A 1 332 ? -13.764 24.416  -5.933  1.00 41.70  ? 469 ARG   A O   1 
ATOM   2457 C  CB  . ARG   A 1 332 ? -12.461 27.161  -5.188  1.00 48.00  ? 469 ARG   A CB  1 
ATOM   2458 C  CG  . ARG   A 1 332 ? -12.421 28.494  -4.446  1.00 53.84  ? 469 ARG   A CG  1 
ATOM   2459 C  CD  . ARG   A 1 332 ? -11.181 28.636  -3.550  1.00 55.40  ? 469 ARG   A CD  1 
ATOM   2460 N  NE  . ARG   A 1 332 ? -11.244 29.843  -2.730  1.00 57.13  ? 469 ARG   A NE  1 
ATOM   2461 C  CZ  . ARG   A 1 332 ? -10.667 31.001  -3.034  1.00 59.45  ? 469 ARG   A CZ  1 
ATOM   2462 N  NH1 . ARG   A 1 332 ? -9.917  31.144  -4.118  1.00 56.97  ? 469 ARG   A NH1 1 
ATOM   2463 N  NH2 . ARG   A 1 332 ? -10.839 32.043  -2.226  1.00 60.30  ? 469 ARG   A NH2 1 
ATOM   2464 N  N   . PRO   A 1 333 ? -13.710 25.570  -7.855  1.00 46.48  ? 470 PRO   A N   1 
ATOM   2465 C  CA  . PRO   A 1 333 ? -13.560 24.345  -8.651  1.00 43.65  ? 470 PRO   A CA  1 
ATOM   2466 C  C   . PRO   A 1 333 ? -12.222 23.686  -8.373  1.00 40.35  ? 470 PRO   A C   1 
ATOM   2467 O  O   . PRO   A 1 333 ? -11.171 24.327  -8.404  1.00 42.81  ? 470 PRO   A O   1 
ATOM   2468 C  CB  . PRO   A 1 333 ? -13.654 24.850  -10.096 1.00 41.44  ? 470 PRO   A CB  1 
ATOM   2469 C  CG  . PRO   A 1 333 ? -13.282 26.276  -10.013 1.00 40.76  ? 470 PRO   A CG  1 
ATOM   2470 C  CD  . PRO   A 1 333 ? -13.850 26.750  -8.720  1.00 44.80  ? 470 PRO   A CD  1 
ATOM   2471 N  N   . GLY   A 1 334 ? -12.264 22.398  -8.087  1.00 42.15  ? 471 GLY   A N   1 
ATOM   2472 C  CA  . GLY   A 1 334 ? -11.035 21.712  -7.764  1.00 42.52  ? 471 GLY   A CA  1 
ATOM   2473 C  C   . GLY   A 1 334 ? -10.604 20.688  -8.788  1.00 42.10  ? 471 GLY   A C   1 
ATOM   2474 O  O   . GLY   A 1 334 ? -10.831 20.844  -9.991  1.00 38.24  ? 471 GLY   A O   1 
ATOM   2475 N  N   . GLY   A 1 335 ? -10.003 19.617  -8.306  1.00 42.44  ? 472 GLY   A N   1 
ATOM   2476 C  CA  . GLY   A 1 335 ? -9.576  18.528  -9.142  1.00 39.96  ? 472 GLY   A CA  1 
ATOM   2477 C  C   . GLY   A 1 335 ? -8.184  18.139  -8.761  1.00 41.52  ? 472 GLY   A C   1 
ATOM   2478 O  O   . GLY   A 1 335 ? -7.653  18.592  -7.742  1.00 44.42  ? 472 GLY   A O   1 
ATOM   2479 N  N   . GLY   A 1 336 ? -7.587  17.298  -9.594  1.00 42.87  ? 473 GLY   A N   1 
ATOM   2480 C  CA  . GLY   A 1 336 ? -6.207  16.924  -9.394  1.00 40.71  ? 473 GLY   A CA  1 
ATOM   2481 C  C   . GLY   A 1 336 ? -6.042  15.459  -9.080  1.00 40.86  ? 473 GLY   A C   1 
ATOM   2482 O  O   . GLY   A 1 336 ? -5.140  14.810  -9.614  1.00 44.62  ? 473 GLY   A O   1 
ATOM   2483 N  N   . ASP   A 1 337 ? -6.882  14.937  -8.188  1.00 42.10  ? 474 ASP   A N   1 
ATOM   2484 C  CA  . ASP   A 1 337 ? -6.899  13.512  -7.873  1.00 38.86  ? 474 ASP   A CA  1 
ATOM   2485 C  C   . ASP   A 1 337 ? -7.926  12.846  -8.774  1.00 37.09  ? 474 ASP   A C   1 
ATOM   2486 O  O   . ASP   A 1 337 ? -9.130  13.078  -8.622  1.00 34.84  ? 474 ASP   A O   1 
ATOM   2487 C  CB  . ASP   A 1 337 ? -7.231  13.262  -6.399  1.00 37.71  ? 474 ASP   A CB  1 
ATOM   2488 C  CG  . ASP   A 1 337 ? -6.924  11.815  -5.951  1.00 38.87  ? 474 ASP   A CG  1 
ATOM   2489 O  OD1 . ASP   A 1 337 ? -6.604  10.970  -6.805  1.00 37.22  ? 474 ASP   A OD1 1 
ATOM   2490 O  OD2 . ASP   A 1 337 ? -6.983  11.525  -4.736  1.00 45.26  ? 474 ASP   A OD2 1 
ATOM   2491 N  N   . MET   A 1 338 ? -7.445  12.068  -9.742  1.00 35.58  ? 475 MET   A N   1 
ATOM   2492 C  CA  . MET   A 1 338 ? -8.319  11.396  -10.692 1.00 36.19  ? 475 MET   A CA  1 
ATOM   2493 C  C   . MET   A 1 338 ? -9.177  10.327  -10.041 1.00 35.27  ? 475 MET   A C   1 
ATOM   2494 O  O   . MET   A 1 338 ? -10.165 9.907   -10.645 1.00 32.85  ? 475 MET   A O   1 
ATOM   2495 C  CB  . MET   A 1 338 ? -7.497  10.769  -11.823 1.00 35.45  ? 475 MET   A CB  1 
ATOM   2496 C  CG  . MET   A 1 338 ? -6.937  11.804  -12.765 1.00 36.94  ? 475 MET   A CG  1 
ATOM   2497 S  SD  . MET   A 1 338 ? -8.157  13.074  -13.121 1.00 37.70  ? 475 MET   A SD  1 
ATOM   2498 C  CE  . MET   A 1 338 ? -7.117  14.549  -13.167 1.00 40.79  ? 475 MET   A CE  1 
ATOM   2499 N  N   . ARG   A 1 339 ? -8.826  9.867   -8.839  1.00 35.92  ? 476 ARG   A N   1 
ATOM   2500 C  CA  . ARG   A 1 339 ? -9.675  8.880   -8.185  1.00 36.17  ? 476 ARG   A CA  1 
ATOM   2501 C  C   . ARG   A 1 339 ? -11.052 9.456   -7.917  1.00 35.96  ? 476 ARG   A C   1 
ATOM   2502 O  O   . ARG   A 1 339 ? -12.049 8.725   -7.927  1.00 33.44  ? 476 ARG   A O   1 
ATOM   2503 C  CB  . ARG   A 1 339 ? -9.031  8.400   -6.892  1.00 37.04  ? 476 ARG   A CB  1 
ATOM   2504 C  CG  . ARG   A 1 339 ? -8.073  7.258   -7.112  1.00 41.07  ? 476 ARG   A CG  1 
ATOM   2505 C  CD  . ARG   A 1 339 ? -6.825  7.468   -6.288  1.00 42.25  ? 476 ARG   A CD  1 
ATOM   2506 N  NE  . ARG   A 1 339 ? -7.119  7.921   -4.937  1.00 40.26  ? 476 ARG   A NE  1 
ATOM   2507 C  CZ  . ARG   A 1 339 ? -6.215  8.455   -4.130  1.00 45.12  ? 476 ARG   A CZ  1 
ATOM   2508 N  NH1 . ARG   A 1 339 ? -4.958  8.630   -4.520  1.00 48.09  ? 476 ARG   A NH1 1 
ATOM   2509 N  NH2 . ARG   A 1 339 ? -6.572  8.807   -2.899  1.00 43.60  ? 476 ARG   A NH2 1 
ATOM   2510 N  N   . ASP   A 1 340 ? -11.127 10.765  -7.687  1.00 36.47  ? 477 ASP   A N   1 
ATOM   2511 C  CA  . ASP   A 1 340 ? -12.433 11.376  -7.529  1.00 35.70  ? 477 ASP   A CA  1 
ATOM   2512 C  C   . ASP   A 1 340 ? -13.262 11.201  -8.793  1.00 36.22  ? 477 ASP   A C   1 
ATOM   2513 O  O   . ASP   A 1 340 ? -14.481 11.026  -8.704  1.00 34.70  ? 477 ASP   A O   1 
ATOM   2514 C  CB  . ASP   A 1 340 ? -12.279 12.847  -7.138  1.00 36.92  ? 477 ASP   A CB  1 
ATOM   2515 C  CG  . ASP   A 1 340 ? -11.435 13.034  -5.873  1.00 36.89  ? 477 ASP   A CG  1 
ATOM   2516 O  OD1 . ASP   A 1 340 ? -11.240 12.028  -5.163  1.00 40.37  ? 477 ASP   A OD1 1 
ATOM   2517 O  OD2 . ASP   A 1 340 ? -10.989 14.180  -5.577  1.00 35.32  ? 477 ASP   A OD2 1 
ATOM   2518 N  N   . ASN   A 1 341 ? -12.617 11.190  -9.969  1.00 33.83  ? 478 ASN   A N   1 
ATOM   2519 C  CA  . ASN   A 1 341 ? -13.345 10.999  -11.218 1.00 31.88  ? 478 ASN   A CA  1 
ATOM   2520 C  C   . ASN   A 1 341 ? -13.893 9.587   -11.319 1.00 35.05  ? 478 ASN   A C   1 
ATOM   2521 O  O   . ASN   A 1 341 ? -15.095 9.408   -11.551 1.00 37.04  ? 478 ASN   A O   1 
ATOM   2522 C  CB  . ASN   A 1 341 ? -12.447 11.301  -12.415 1.00 36.04  ? 478 ASN   A CB  1 
ATOM   2523 C  CG  . ASN   A 1 341 ? -11.899 12.700  -12.388 1.00 34.87  ? 478 ASN   A CG  1 
ATOM   2524 O  OD1 . ASN   A 1 341 ? -11.532 13.204  -11.331 1.00 33.95  ? 478 ASN   A OD1 1 
ATOM   2525 N  ND2 . ASN   A 1 341 ? -11.837 13.340  -13.560 1.00 33.59  ? 478 ASN   A ND2 1 
ATOM   2526 N  N   . TRP   A 1 342 ? -13.026 8.581   -11.139 1.00 33.27  ? 479 TRP   A N   1 
ATOM   2527 C  CA  . TRP   A 1 342 ? -13.490 7.201   -11.066 1.00 37.69  ? 479 TRP   A CA  1 
ATOM   2528 C  C   . TRP   A 1 342 ? -14.509 7.048   -9.945  1.00 36.26  ? 479 TRP   A C   1 
ATOM   2529 O  O   . TRP   A 1 342 ? -15.493 6.315   -10.086 1.00 37.09  ? 479 TRP   A O   1 
ATOM   2530 C  CB  . TRP   A 1 342 ? -12.306 6.244   -10.847 1.00 33.36  ? 479 TRP   A CB  1 
ATOM   2531 C  CG  . TRP   A 1 342 ? -10.998 6.680   -11.460 1.00 33.43  ? 479 TRP   A CG  1 
ATOM   2532 C  CD1 . TRP   A 1 342 ? -9.773  6.640   -10.862 1.00 35.24  ? 479 TRP   A CD1 1 
ATOM   2533 C  CD2 . TRP   A 1 342 ? -10.792 7.273   -12.754 1.00 29.89  ? 479 TRP   A CD2 1 
ATOM   2534 N  NE1 . TRP   A 1 342 ? -8.810  7.132   -11.710 1.00 32.10  ? 479 TRP   A NE1 1 
ATOM   2535 C  CE2 . TRP   A 1 342 ? -9.407  7.535   -12.875 1.00 28.37  ? 479 TRP   A CE2 1 
ATOM   2536 C  CE3 . TRP   A 1 342 ? -11.637 7.602   -13.817 1.00 29.51  ? 479 TRP   A CE3 1 
ATOM   2537 C  CZ2 . TRP   A 1 342 ? -8.848  8.110   -14.010 1.00 25.56  ? 479 TRP   A CZ2 1 
ATOM   2538 C  CZ3 . TRP   A 1 342 ? -11.078 8.182   -14.956 1.00 34.86  ? 479 TRP   A CZ3 1 
ATOM   2539 C  CH2 . TRP   A 1 342 ? -9.689  8.424   -15.040 1.00 32.62  ? 479 TRP   A CH2 1 
ATOM   2540 N  N   . ARG   A 1 343 ? -14.289 7.747   -8.832  1.00 34.46  ? 480 ARG   A N   1 
ATOM   2541 C  CA  . ARG   A 1 343 ? -15.157 7.624   -7.668  1.00 37.68  ? 480 ARG   A CA  1 
ATOM   2542 C  C   . ARG   A 1 343 ? -16.567 8.097   -7.987  1.00 37.71  ? 480 ARG   A C   1 
ATOM   2543 O  O   . ARG   A 1 343 ? -17.543 7.561   -7.451  1.00 38.33  ? 480 ARG   A O   1 
ATOM   2544 C  CB  . ARG   A 1 343 ? -14.548 8.431   -6.525  1.00 34.60  ? 480 ARG   A CB  1 
ATOM   2545 C  CG  . ARG   A 1 343 ? -15.316 8.439   -5.256  1.00 39.57  ? 480 ARG   A CG  1 
ATOM   2546 C  CD  . ARG   A 1 343 ? -14.606 9.380   -4.294  1.00 40.84  ? 480 ARG   A CD  1 
ATOM   2547 N  NE  . ARG   A 1 343 ? -13.151 9.257   -4.320  1.00 38.00  ? 480 ARG   A NE  1 
ATOM   2548 C  CZ  . ARG   A 1 343 ? -12.472 8.190   -3.919  1.00 38.67  ? 480 ARG   A CZ  1 
ATOM   2549 N  NH1 . ARG   A 1 343 ? -13.083 7.092   -3.501  1.00 37.91  ? 480 ARG   A NH1 1 
ATOM   2550 N  NH2 . ARG   A 1 343 ? -11.143 8.234   -3.911  1.00 41.12  ? 480 ARG   A NH2 1 
ATOM   2551 N  N   . SER   A 1 344 ? -16.686 9.081   -8.877  1.00 37.26  ? 481 SER   A N   1 
ATOM   2552 C  CA  . SER   A 1 344 ? -17.972 9.656   -9.248  1.00 37.98  ? 481 SER   A CA  1 
ATOM   2553 C  C   . SER   A 1 344 ? -18.857 8.687   -10.023 1.00 36.28  ? 481 SER   A C   1 
ATOM   2554 O  O   . SER   A 1 344 ? -20.073 8.884   -10.092 1.00 38.85  ? 481 SER   A O   1 
ATOM   2555 C  CB  . SER   A 1 344 ? -17.725 10.905  -10.088 1.00 34.39  ? 481 SER   A CB  1 
ATOM   2556 O  OG  . SER   A 1 344 ? -17.686 10.527  -11.451 1.00 34.83  ? 481 SER   A OG  1 
ATOM   2557 N  N   . GLU   A 1 345 ? -18.278 7.670   -10.641 1.00 34.81  ? 482 GLU   A N   1 
ATOM   2558 C  CA  . GLU   A 1 345 ? -19.037 6.699   -11.407 1.00 36.67  ? 482 GLU   A CA  1 
ATOM   2559 C  C   . GLU   A 1 345 ? -19.153 5.365   -10.678 1.00 33.76  ? 482 GLU   A C   1 
ATOM   2560 O  O   . GLU   A 1 345 ? -20.053 4.582   -10.983 1.00 34.17  ? 482 GLU   A O   1 
ATOM   2561 C  CB  . GLU   A 1 345 ? -18.371 6.503   -12.783 1.00 37.82  ? 482 GLU   A CB  1 
ATOM   2562 C  CG  . GLU   A 1 345 ? -18.781 7.522   -13.895 1.00 35.82  ? 482 GLU   A CG  1 
ATOM   2563 C  CD  . GLU   A 1 345 ? -20.145 7.239   -14.528 1.00 41.17  ? 482 GLU   A CD  1 
ATOM   2564 O  OE1 . GLU   A 1 345 ? -21.187 7.608   -13.942 1.00 44.53  ? 482 GLU   A OE1 1 
ATOM   2565 O  OE2 . GLU   A 1 345 ? -20.177 6.615   -15.613 1.00 42.81  ? 482 GLU   A OE2 1 
ATOM   2566 N  N   . LEU   A 1 346 ? -18.305 5.120   -9.689  1.00 31.67  ? 483 LEU   A N   1 
ATOM   2567 C  CA  . LEU   A 1 346 ? -18.243 3.858   -8.974  1.00 37.81  ? 483 LEU   A CA  1 
ATOM   2568 C  C   . LEU   A 1 346 ? -18.892 3.948   -7.598  1.00 36.49  ? 483 LEU   A C   1 
ATOM   2569 O  O   . LEU   A 1 346 ? -18.810 3.001   -6.819  1.00 30.44  ? 483 LEU   A O   1 
ATOM   2570 C  CB  . LEU   A 1 346 ? -16.785 3.453   -8.821  1.00 37.48  ? 483 LEU   A CB  1 
ATOM   2571 C  CG  . LEU   A 1 346 ? -16.164 2.870   -10.069 1.00 35.49  ? 483 LEU   A CG  1 
ATOM   2572 C  CD1 . LEU   A 1 346 ? -14.710 2.591   -9.760  1.00 35.40  ? 483 LEU   A CD1 1 
ATOM   2573 C  CD2 . LEU   A 1 346 ? -16.901 1.615   -10.518 1.00 38.28  ? 483 LEU   A CD2 1 
ATOM   2574 N  N   . TYR   A 1 347 ? -19.503 5.085   -7.281  1.00 37.91  ? 484 TYR   A N   1 
ATOM   2575 C  CA  . TYR   A 1 347 ? -20.007 5.335   -5.939  1.00 37.89  ? 484 TYR   A CA  1 
ATOM   2576 C  C   . TYR   A 1 347 ? -21.054 4.311   -5.506  1.00 32.63  ? 484 TYR   A C   1 
ATOM   2577 O  O   . TYR   A 1 347 ? -21.234 4.087   -4.307  1.00 30.78  ? 484 TYR   A O   1 
ATOM   2578 C  CB  . TYR   A 1 347 ? -20.570 6.766   -5.884  1.00 38.18  ? 484 TYR   A CB  1 
ATOM   2579 C  CG  . TYR   A 1 347 ? -21.854 6.945   -6.679  1.00 37.00  ? 484 TYR   A CG  1 
ATOM   2580 C  CD1 . TYR   A 1 347 ? -23.083 6.579   -6.141  1.00 37.88  ? 484 TYR   A CD1 1 
ATOM   2581 C  CD2 . TYR   A 1 347 ? -21.835 7.471   -7.964  1.00 35.24  ? 484 TYR   A CD2 1 
ATOM   2582 C  CE1 . TYR   A 1 347 ? -24.252 6.729   -6.857  1.00 39.61  ? 484 TYR   A CE1 1 
ATOM   2583 C  CE2 . TYR   A 1 347 ? -23.010 7.629   -8.696  1.00 35.68  ? 484 TYR   A CE2 1 
ATOM   2584 C  CZ  . TYR   A 1 347 ? -24.209 7.251   -8.135  1.00 36.76  ? 484 TYR   A CZ  1 
ATOM   2585 O  OH  . TYR   A 1 347 ? -25.381 7.398   -8.834  1.00 41.52  ? 484 TYR   A OH  1 
ATOM   2586 N  N   . LYS   A 1 348 ? -21.769 3.696   -6.449  1.00 34.32  ? 485 LYS   A N   1 
ATOM   2587 C  CA  . LYS   A 1 348 ? -22.853 2.778   -6.113  1.00 39.19  ? 485 LYS   A CA  1 
ATOM   2588 C  C   . LYS   A 1 348 ? -22.406 1.324   -6.008  1.00 39.64  ? 485 LYS   A C   1 
ATOM   2589 O  O   . LYS   A 1 348 ? -23.247 0.415   -6.050  1.00 39.57  ? 485 LYS   A O   1 
ATOM   2590 C  CB  . LYS   A 1 348 ? -24.001 2.892   -7.122  1.00 39.40  ? 485 LYS   A CB  1 
ATOM   2591 C  CG  . LYS   A 1 348 ? -23.654 3.042   -8.601  1.00 38.97  ? 485 LYS   A CG  1 
ATOM   2592 C  CD  . LYS   A 1 348 ? -24.889 3.620   -9.334  1.00 41.45  ? 485 LYS   A CD  1 
ATOM   2593 C  CE  . LYS   A 1 348 ? -24.959 3.207   -10.787 1.00 47.61  ? 485 LYS   A CE  1 
ATOM   2594 N  NZ  . LYS   A 1 348 ? -24.400 4.275   -11.677 1.00 52.74  ? 485 LYS   A NZ  1 
ATOM   2595 N  N   . TYR   A 1 349 ? -21.114 1.077   -5.856  1.00 36.11  ? 486 TYR   A N   1 
ATOM   2596 C  CA  . TYR   A 1 349 ? -20.624 -0.285  -5.891  1.00 39.63  ? 486 TYR   A CA  1 
ATOM   2597 C  C   . TYR   A 1 349 ? -19.737 -0.554  -4.692  1.00 39.80  ? 486 TYR   A C   1 
ATOM   2598 O  O   . TYR   A 1 349 ? -19.268 0.362   -4.006  1.00 37.21  ? 486 TYR   A O   1 
ATOM   2599 C  CB  . TYR   A 1 349 ? -19.848 -0.577  -7.182  1.00 38.32  ? 486 TYR   A CB  1 
ATOM   2600 C  CG  . TYR   A 1 349 ? -20.623 -0.346  -8.455  1.00 37.69  ? 486 TYR   A CG  1 
ATOM   2601 C  CD1 . TYR   A 1 349 ? -21.531 -1.288  -8.911  1.00 39.81  ? 486 TYR   A CD1 1 
ATOM   2602 C  CD2 . TYR   A 1 349 ? -20.439 0.808   -9.201  1.00 34.19  ? 486 TYR   A CD2 1 
ATOM   2603 C  CE1 . TYR   A 1 349 ? -22.238 -1.093  -10.079 1.00 40.62  ? 486 TYR   A CE1 1 
ATOM   2604 C  CE2 . TYR   A 1 349 ? -21.131 1.021   -10.366 1.00 38.54  ? 486 TYR   A CE2 1 
ATOM   2605 C  CZ  . TYR   A 1 349 ? -22.038 0.067   -10.810 1.00 41.41  ? 486 TYR   A CZ  1 
ATOM   2606 O  OH  . TYR   A 1 349 ? -22.744 0.279   -11.979 1.00 40.53  ? 486 TYR   A OH  1 
ATOM   2607 N  N   . LYS   A 1 350 ? -19.486 -1.843  -4.493  1.00 40.10  ? 487 LYS   A N   1 
ATOM   2608 C  CA  . LYS   A 1 350 ? -18.596 -2.342  -3.460  1.00 41.94  ? 487 LYS   A CA  1 
ATOM   2609 C  C   . LYS   A 1 350 ? -18.436 -3.838  -3.673  1.00 42.76  ? 487 LYS   A C   1 
ATOM   2610 O  O   . LYS   A 1 350 ? -19.406 -4.534  -3.994  1.00 43.65  ? 487 LYS   A O   1 
ATOM   2611 C  CB  . LYS   A 1 350 ? -19.145 -2.015  -2.063  1.00 42.24  ? 487 LYS   A CB  1 
ATOM   2612 C  CG  . LYS   A 1 350 ? -19.390 -3.190  -1.145  1.00 44.50  ? 487 LYS   A CG  1 
ATOM   2613 C  CD  . LYS   A 1 350 ? -19.758 -2.649  0.233   1.00 45.16  ? 487 LYS   A CD  1 
ATOM   2614 C  CE  . LYS   A 1 350 ? -20.988 -3.307  0.818   1.00 49.11  ? 487 LYS   A CE  1 
ATOM   2615 N  NZ  . LYS   A 1 350 ? -20.972 -3.291  2.320   1.00 54.62  ? 487 LYS   A NZ  1 
ATOM   2616 N  N   . VAL   A 1 351 ? -17.222 -4.308  -3.568  1.00 43.16  ? 488 VAL   A N   1 
ATOM   2617 C  CA  . VAL   A 1 351 ? -16.950 -5.725  -3.758  1.00 46.04  ? 488 VAL   A CA  1 
ATOM   2618 C  C   . VAL   A 1 351 ? -17.014 -6.410  -2.411  1.00 48.70  ? 488 VAL   A C   1 
ATOM   2619 O  O   . VAL   A 1 351 ? -16.587 -5.857  -1.395  1.00 51.35  ? 488 VAL   A O   1 
ATOM   2620 C  CB  . VAL   A 1 351 ? -15.584 -5.960  -4.419  1.00 45.18  ? 488 VAL   A CB  1 
ATOM   2621 C  CG1 . VAL   A 1 351 ? -15.229 -7.438  -4.343  1.00 45.27  ? 488 VAL   A CG1 1 
ATOM   2622 C  CG2 . VAL   A 1 351 ? -15.603 -5.474  -5.855  1.00 42.23  ? 488 VAL   A CG2 1 
ATOM   2623 N  N   . VAL   A 1 352 ? -17.540 -7.628  -2.403  1.00 53.84  ? 489 VAL   A N   1 
ATOM   2624 C  CA  . VAL   A 1 352 ? -17.699 -8.402  -1.181  1.00 58.35  ? 489 VAL   A CA  1 
ATOM   2625 C  C   . VAL   A 1 352 ? -17.407 -9.858  -1.503  1.00 57.87  ? 489 VAL   A C   1 
ATOM   2626 O  O   . VAL   A 1 352 ? -17.923 -10.406 -2.482  1.00 54.64  ? 489 VAL   A O   1 
ATOM   2627 C  CB  . VAL   A 1 352 ? -19.109 -8.238  -0.581  1.00 59.74  ? 489 VAL   A CB  1 
ATOM   2628 C  CG1 . VAL   A 1 352 ? -19.520 -6.765  -0.588  1.00 55.02  ? 489 VAL   A CG1 1 
ATOM   2629 C  CG2 . VAL   A 1 352 ? -20.122 -9.099  -1.342  1.00 59.52  ? 489 VAL   A CG2 1 
ATOM   2630 N  N   . GLN   A 1 353 ? -16.552 -10.463 -0.690  1.00 63.32  ? 490 GLN   A N   1 
ATOM   2631 C  CA  . GLN   A 1 353 ? -16.189 -11.861 -0.834  1.00 62.95  ? 490 GLN   A CA  1 
ATOM   2632 C  C   . GLN   A 1 353 ? -17.337 -12.739 -0.369  1.00 65.46  ? 490 GLN   A C   1 
ATOM   2633 O  O   . GLN   A 1 353 ? -17.851 -12.569 0.741   1.00 68.22  ? 490 GLN   A O   1 
ATOM   2634 C  CB  . GLN   A 1 353 ? -14.932 -12.143 -0.016  1.00 62.97  ? 490 GLN   A CB  1 
ATOM   2635 C  CG  . GLN   A 1 353 ? -14.546 -13.600 0.076   1.00 64.78  ? 490 GLN   A CG  1 
ATOM   2636 C  CD  . GLN   A 1 353 ? -13.169 -13.791 0.677   1.00 65.94  ? 490 GLN   A CD  1 
ATOM   2637 O  OE1 . GLN   A 1 353 ? -12.313 -12.901 0.611   1.00 64.14  ? 490 GLN   A OE1 1 
ATOM   2638 N  NE2 . GLN   A 1 353 ? -12.941 -14.960 1.258   1.00 69.80  ? 490 GLN   A NE2 1 
ATOM   2639 N  N   . ILE   A 1 354 ? -17.739 -13.676 -1.217  1.00 63.95  ? 491 ILE   A N   1 
ATOM   2640 C  CA  . ILE   A 1 354 ? -18.836 -14.574 -0.882  1.00 65.81  ? 491 ILE   A CA  1 
ATOM   2641 C  C   . ILE   A 1 354 ? -18.322 -15.608 0.104   1.00 67.58  ? 491 ILE   A C   1 
ATOM   2642 O  O   . ILE   A 1 354 ? -17.452 -16.416 -0.235  1.00 63.82  ? 491 ILE   A O   1 
ATOM   2643 C  CB  . ILE   A 1 354 ? -19.414 -15.240 -2.134  1.00 64.14  ? 491 ILE   A CB  1 
ATOM   2644 C  CG1 . ILE   A 1 354 ? -20.584 -14.411 -2.630  1.00 61.17  ? 491 ILE   A CG1 1 
ATOM   2645 C  CG2 . ILE   A 1 354 ? -19.888 -16.639 -1.800  1.00 64.81  ? 491 ILE   A CG2 1 
ATOM   2646 C  CD1 . ILE   A 1 354 ? -21.159 -13.557 -1.529  1.00 66.68  ? 491 ILE   A CD1 1 
ATOM   2647 N  N   . GLU   A 1 355 ? -18.854 -15.571 1.326   1.00 70.76  ? 492 GLU   A N   1 
ATOM   2648 C  CA  . GLU   A 1 355 ? -18.442 -16.470 2.397   1.00 71.34  ? 492 GLU   A CA  1 
ATOM   2649 C  C   . GLU   A 1 355 ? -19.272 -17.756 2.358   1.00 69.04  ? 492 GLU   A C   1 
ATOM   2650 O  O   . GLU   A 1 355 ? -20.421 -17.715 2.801   1.00 71.45  ? 492 GLU   A O   1 
ATOM   2651 C  CB  . GLU   A 1 355 ? -18.596 -15.776 3.755   1.00 72.01  ? 492 GLU   A CB  1 
ATOM   2652 C  CG  . GLU   A 1 355 ? -17.723 -14.540 3.922   1.00 75.83  ? 492 GLU   A CG  1 
ATOM   2653 C  CD  . GLU   A 1 355 ? -16.318 -14.875 4.370   1.00 76.85  ? 492 GLU   A CD  1 
ATOM   2654 O  OE1 . GLU   A 1 355 ? -16.060 -14.878 5.596   1.00 75.34  ? 492 GLU   A OE1 1 
ATOM   2655 O  OE2 . GLU   A 1 355 ? -15.487 -15.166 3.485   1.00 75.59  ? 492 GLU   A OE2 1 
ATOM   2656 O  OXT . GLU   A 1 355 ? -18.845 -18.827 1.894   1.00 62.23  ? 492 GLU   A OXT 1 
HETATM 2657 C  C1  . NAG   B 2 .   ? -25.191 11.076  2.834   1.00 45.80  ? 501 NAG   A C1  1 
HETATM 2658 C  C2  . NAG   B 2 .   ? -24.838 12.199  3.786   1.00 45.95  ? 501 NAG   A C2  1 
HETATM 2659 C  C3  . NAG   B 2 .   ? -24.518 11.626  5.153   1.00 47.73  ? 501 NAG   A C3  1 
HETATM 2660 C  C4  . NAG   B 2 .   ? -25.701 10.800  5.646   1.00 49.42  ? 501 NAG   A C4  1 
HETATM 2661 C  C5  . NAG   B 2 .   ? -26.130 9.769   4.594   1.00 49.28  ? 501 NAG   A C5  1 
HETATM 2662 C  C6  . NAG   B 2 .   ? -27.431 9.077   4.933   1.00 48.56  ? 501 NAG   A C6  1 
HETATM 2663 C  C7  . NAG   B 2 .   ? -23.938 14.045  2.463   1.00 46.37  ? 501 NAG   A C7  1 
HETATM 2664 C  C8  . NAG   B 2 .   ? -22.708 14.783  2.021   1.00 46.81  ? 501 NAG   A C8  1 
HETATM 2665 N  N2  . NAG   B 2 .   ? -23.740 13.006  3.283   1.00 44.29  ? 501 NAG   A N2  1 
HETATM 2666 O  O3  . NAG   B 2 .   ? -24.237 12.697  6.047   1.00 51.09  ? 501 NAG   A O3  1 
HETATM 2667 O  O4  . NAG   B 2 .   ? -25.355 10.121  6.848   1.00 52.76  ? 501 NAG   A O4  1 
HETATM 2668 O  O5  . NAG   B 2 .   ? -26.329 10.393  3.315   1.00 48.02  ? 501 NAG   A O5  1 
HETATM 2669 O  O6  . NAG   B 2 .   ? -27.233 8.004   5.841   1.00 52.35  ? 501 NAG   A O6  1 
HETATM 2670 O  O7  . NAG   B 2 .   ? -25.065 14.377  2.095   1.00 42.87  ? 501 NAG   A O7  1 
HETATM 2671 C  C1  . NAG   C 2 .   ? -34.916 -0.872  -7.239  1.00 69.97  ? 502 NAG   A C1  1 
HETATM 2672 C  C2  . NAG   C 2 .   ? -36.389 -0.480  -7.049  1.00 76.74  ? 502 NAG   A C2  1 
HETATM 2673 C  C3  . NAG   C 2 .   ? -36.889 0.390   -8.212  1.00 78.12  ? 502 NAG   A C3  1 
HETATM 2674 C  C4  . NAG   C 2 .   ? -36.655 -0.294  -9.554  1.00 77.04  ? 502 NAG   A C4  1 
HETATM 2675 C  C5  . NAG   C 2 .   ? -35.289 -0.976  -9.582  1.00 74.81  ? 502 NAG   A C5  1 
HETATM 2676 C  C6  . NAG   C 2 .   ? -34.533 -0.722  -10.867 1.00 72.57  ? 502 NAG   A C6  1 
HETATM 2677 C  C7  . NAG   C 2 .   ? -37.263 -2.389  -5.767  1.00 72.98  ? 502 NAG   A C7  1 
HETATM 2678 C  C8  . NAG   C 2 .   ? -38.194 -3.565  -5.779  1.00 72.43  ? 502 NAG   A C8  1 
HETATM 2679 N  N2  . NAG   C 2 .   ? -37.230 -1.656  -6.887  1.00 73.08  ? 502 NAG   A N2  1 
HETATM 2680 O  O3  . NAG   C 2 .   ? -36.268 1.674   -8.192  1.00 74.73  ? 502 NAG   A O3  1 
HETATM 2681 O  O4  . NAG   C 2 .   ? -37.685 -1.250  -9.785  1.00 74.07  ? 502 NAG   A O4  1 
HETATM 2682 O  O5  . NAG   C 2 .   ? -34.475 -0.466  -8.517  1.00 70.74  ? 502 NAG   A O5  1 
HETATM 2683 O  O6  . NAG   C 2 .   ? -33.127 -0.711  -10.655 1.00 72.39  ? 502 NAG   A O6  1 
HETATM 2684 O  O7  . NAG   C 2 .   ? -36.573 -2.116  -4.789  1.00 73.92  ? 502 NAG   A O7  1 
HETATM 2685 C  C1  . NAG   D 2 .   ? -17.189 12.829  -24.899 1.00 36.99  ? 503 NAG   A C1  1 
HETATM 2686 C  C2  . NAG   D 2 .   ? -15.784 13.046  -25.485 1.00 38.96  ? 503 NAG   A C2  1 
HETATM 2687 C  C3  . NAG   D 2 .   ? -15.870 13.525  -26.936 1.00 41.21  ? 503 NAG   A C3  1 
HETATM 2688 C  C4  . NAG   D 2 .   ? -16.802 12.656  -27.768 1.00 43.36  ? 503 NAG   A C4  1 
HETATM 2689 C  C5  . NAG   D 2 .   ? -18.148 12.518  -27.071 1.00 40.97  ? 503 NAG   A C5  1 
HETATM 2690 C  C6  . NAG   D 2 .   ? -19.090 11.580  -27.785 1.00 41.43  ? 503 NAG   A C6  1 
HETATM 2691 C  C7  . NAG   D 2 .   ? -13.889 13.782  -24.090 1.00 38.77  ? 503 NAG   A C7  1 
HETATM 2692 C  C8  . NAG   D 2 .   ? -13.289 14.938  -23.347 1.00 34.91  ? 503 NAG   A C8  1 
HETATM 2693 N  N2  . NAG   D 2 .   ? -15.056 14.025  -24.693 1.00 41.24  ? 503 NAG   A N2  1 
HETATM 2694 O  O3  . NAG   D 2 .   ? -14.570 13.540  -27.517 1.00 38.98  ? 503 NAG   A O3  1 
HETATM 2695 O  O4  . NAG   D 2 .   ? -17.007 13.286  -29.027 1.00 41.42  ? 503 NAG   A O4  1 
HETATM 2696 O  O5  . NAG   D 2 .   ? -17.949 11.980  -25.758 1.00 37.95  ? 503 NAG   A O5  1 
HETATM 2697 O  O6  . NAG   D 2 .   ? -18.769 10.228  -27.497 1.00 39.99  ? 503 NAG   A O6  1 
HETATM 2698 O  O7  . NAG   D 2 .   ? -13.350 12.676  -24.125 1.00 37.58  ? 503 NAG   A O7  1 
HETATM 2699 C  C1  . NAG   E 2 .   ? -17.788 15.054  10.081  1.00 87.61  ? 504 NAG   A C1  1 
HETATM 2700 C  C2  . NAG   E 2 .   ? -17.758 14.155  11.304  1.00 94.21  ? 504 NAG   A C2  1 
HETATM 2701 C  C3  . NAG   E 2 .   ? -18.303 14.915  12.499  1.00 98.94  ? 504 NAG   A C3  1 
HETATM 2702 C  C4  . NAG   E 2 .   ? -17.381 16.070  12.865  1.00 101.86 ? 504 NAG   A C4  1 
HETATM 2703 C  C5  . NAG   E 2 .   ? -16.538 16.539  11.674  1.00 98.66  ? 504 NAG   A C5  1 
HETATM 2704 C  C6  . NAG   E 2 .   ? -15.187 15.863  11.575  1.00 102.66 ? 504 NAG   A C6  1 
HETATM 2705 C  C7  . NAG   E 2 .   ? -18.090 11.871  10.428  1.00 91.93  ? 504 NAG   A C7  1 
HETATM 2706 C  C8  . NAG   E 2 .   ? -19.057 10.732  10.308  1.00 86.65  ? 504 NAG   A C8  1 
HETATM 2707 N  N2  . NAG   E 2 .   ? -18.540 12.949  11.081  1.00 92.10  ? 504 NAG   A N2  1 
HETATM 2708 O  O3  . NAG   E 2 .   ? -18.452 14.029  13.602  1.00 95.73  ? 504 NAG   A O3  1 
HETATM 2709 O  O4  . NAG   E 2 .   ? -18.158 17.168  13.330  1.00 101.55 ? 504 NAG   A O4  1 
HETATM 2710 O  O5  . NAG   E 2 .   ? -17.208 16.363  10.410  1.00 90.65  ? 504 NAG   A O5  1 
HETATM 2711 O  O6  . NAG   E 2 .   ? -14.129 16.811  11.647  1.00 102.28 ? 504 NAG   A O6  1 
HETATM 2712 O  O7  . NAG   E 2 .   ? -16.959 11.817  9.954   1.00 95.42  ? 504 NAG   A O7  1 
HETATM 2713 C  C1  . NAG   F 2 .   ? -32.497 18.588  -10.989 1.00 46.72  ? 505 NAG   A C1  1 
HETATM 2714 C  C2  . NAG   F 2 .   ? -33.933 18.647  -11.524 1.00 49.42  ? 505 NAG   A C2  1 
HETATM 2715 C  C3  . NAG   F 2 .   ? -34.634 19.918  -11.055 1.00 51.20  ? 505 NAG   A C3  1 
HETATM 2716 C  C4  . NAG   F 2 .   ? -34.583 20.021  -9.541  1.00 49.93  ? 505 NAG   A C4  1 
HETATM 2717 C  C5  . NAG   F 2 .   ? -33.136 20.003  -9.080  1.00 49.93  ? 505 NAG   A C5  1 
HETATM 2718 C  C6  . NAG   F 2 .   ? -33.021 20.001  -7.571  1.00 49.46  ? 505 NAG   A C6  1 
HETATM 2719 C  C7  . NAG   F 2 .   ? -34.370 17.510  -13.661 1.00 52.80  ? 505 NAG   A C7  1 
HETATM 2720 C  C8  . NAG   F 2 .   ? -34.285 17.620  -15.154 1.00 61.78  ? 505 NAG   A C8  1 
HETATM 2721 N  N2  . NAG   F 2 .   ? -33.940 18.574  -12.975 1.00 50.26  ? 505 NAG   A N2  1 
HETATM 2722 O  O3  . NAG   F 2 .   ? -35.992 19.899  -11.479 1.00 53.11  ? 505 NAG   A O3  1 
HETATM 2723 O  O4  . NAG   F 2 .   ? -35.190 21.235  -9.113  1.00 48.93  ? 505 NAG   A O4  1 
HETATM 2724 O  O5  . NAG   F 2 .   ? -32.495 18.807  -9.550  1.00 47.12  ? 505 NAG   A O5  1 
HETATM 2725 O  O6  . NAG   F 2 .   ? -31.673 20.099  -7.131  1.00 51.02  ? 505 NAG   A O6  1 
HETATM 2726 O  O7  . NAG   F 2 .   ? -34.795 16.499  -13.103 1.00 49.18  ? 505 NAG   A O7  1 
HETATM 2727 C  C1  . NAG   G 2 .   ? -18.598 22.937  -32.173 1.00 43.99  ? 506 NAG   A C1  1 
HETATM 2728 C  C2  . NAG   G 2 .   ? -19.705 22.702  -33.192 1.00 47.74  ? 506 NAG   A C2  1 
HETATM 2729 C  C3  . NAG   G 2 .   ? -19.124 22.667  -34.603 1.00 48.69  ? 506 NAG   A C3  1 
HETATM 2730 C  C4  . NAG   G 2 .   ? -18.358 23.950  -34.878 1.00 47.32  ? 506 NAG   A C4  1 
HETATM 2731 C  C5  . NAG   G 2 .   ? -17.281 24.138  -33.816 1.00 47.51  ? 506 NAG   A C5  1 
HETATM 2732 C  C6  . NAG   G 2 .   ? -16.552 25.455  -33.945 1.00 47.35  ? 506 NAG   A C6  1 
HETATM 2733 C  C7  . NAG   G 2 .   ? -21.757 21.466  -32.703 1.00 51.55  ? 506 NAG   A C7  1 
HETATM 2734 C  C8  . NAG   G 2 .   ? -22.366 20.125  -32.427 1.00 54.84  ? 506 NAG   A C8  1 
HETATM 2735 N  N2  . NAG   G 2 .   ? -20.437 21.479  -32.909 1.00 48.43  ? 506 NAG   A N2  1 
HETATM 2736 O  O3  . NAG   G 2 .   ? -20.172 22.514  -35.555 1.00 51.72  ? 506 NAG   A O3  1 
HETATM 2737 O  O4  . NAG   G 2 .   ? -17.771 23.901  -36.172 1.00 48.69  ? 506 NAG   A O4  1 
HETATM 2738 O  O5  . NAG   G 2 .   ? -17.878 24.133  -32.510 1.00 48.75  ? 506 NAG   A O5  1 
HETATM 2739 O  O6  . NAG   G 2 .   ? -17.441 26.556  -33.809 1.00 52.68  ? 506 NAG   A O6  1 
HETATM 2740 O  O7  . NAG   G 2 .   ? -22.431 22.496  -32.731 1.00 51.73  ? 506 NAG   A O7  1 
HETATM 2741 C  C1  . NAG   H 2 .   ? -29.549 27.954  -24.440 1.00 51.44  ? 507 NAG   A C1  1 
HETATM 2742 C  C2  . NAG   H 2 .   ? -30.219 27.820  -25.827 1.00 51.29  ? 507 NAG   A C2  1 
HETATM 2743 C  C3  . NAG   H 2 .   ? -31.701 28.207  -25.778 1.00 50.49  ? 507 NAG   A C3  1 
HETATM 2744 C  C4  . NAG   H 2 .   ? -32.415 27.508  -24.634 1.00 55.48  ? 507 NAG   A C4  1 
HETATM 2745 C  C5  . NAG   H 2 .   ? -31.683 27.802  -23.334 1.00 54.17  ? 507 NAG   A C5  1 
HETATM 2746 C  C6  . NAG   H 2 .   ? -32.312 27.135  -22.135 1.00 55.63  ? 507 NAG   A C6  1 
HETATM 2747 C  C7  . NAG   H 2 .   ? -29.004 28.103  -27.937 1.00 55.01  ? 507 NAG   A C7  1 
HETATM 2748 C  C8  . NAG   H 2 .   ? -28.352 29.079  -28.876 1.00 54.41  ? 507 NAG   A C8  1 
HETATM 2749 N  N2  . NAG   H 2 .   ? -29.528 28.623  -26.823 1.00 53.63  ? 507 NAG   A N2  1 
HETATM 2750 O  O3  . NAG   H 2 .   ? -32.325 27.813  -26.994 1.00 49.22  ? 507 NAG   A O3  1 
HETATM 2751 O  O4  . NAG   H 2 .   ? -33.767 27.951  -24.573 1.00 55.05  ? 507 NAG   A O4  1 
HETATM 2752 O  O5  . NAG   H 2 .   ? -30.349 27.289  -23.443 1.00 56.29  ? 507 NAG   A O5  1 
HETATM 2753 O  O6  . NAG   H 2 .   ? -33.502 26.453  -22.502 1.00 57.07  ? 507 NAG   A O6  1 
HETATM 2754 O  O7  . NAG   H 2 .   ? -29.043 26.897  -28.170 1.00 55.00  ? 507 NAG   A O7  1 
HETATM 2755 C  C1  . NAG   I 2 .   ? -9.301  33.760  -16.643 1.00 54.77  ? 508 NAG   A C1  1 
HETATM 2756 C  C2  . NAG   I 2 .   ? -8.147  34.476  -15.926 1.00 56.72  ? 508 NAG   A C2  1 
HETATM 2757 C  C3  . NAG   I 2 .   ? -8.675  35.685  -15.143 1.00 55.72  ? 508 NAG   A C3  1 
HETATM 2758 C  C4  . NAG   I 2 .   ? -9.541  36.576  -16.024 1.00 57.09  ? 508 NAG   A C4  1 
HETATM 2759 C  C5  . NAG   I 2 .   ? -10.617 35.748  -16.711 1.00 56.35  ? 508 NAG   A C5  1 
HETATM 2760 C  C6  . NAG   I 2 .   ? -11.414 36.528  -17.726 1.00 59.65  ? 508 NAG   A C6  1 
HETATM 2761 C  C7  . NAG   I 2 .   ? -6.119  33.580  -14.876 1.00 64.94  ? 508 NAG   A C7  1 
HETATM 2762 C  C8  . NAG   I 2 .   ? -5.560  32.578  -13.903 1.00 64.01  ? 508 NAG   A C8  1 
HETATM 2763 N  N2  . NAG   I 2 .   ? -7.447  33.568  -15.033 1.00 58.64  ? 508 NAG   A N2  1 
HETATM 2764 O  O3  . NAG   I 2 .   ? -7.590  36.443  -14.620 1.00 58.05  ? 508 NAG   A O3  1 
HETATM 2765 O  O4  . NAG   I 2 .   ? -10.165 37.578  -15.230 1.00 57.72  ? 508 NAG   A O4  1 
HETATM 2766 O  O5  . NAG   I 2 .   ? -10.003 34.681  -17.441 1.00 59.11  ? 508 NAG   A O5  1 
HETATM 2767 O  O6  . NAG   I 2 .   ? -11.435 35.827  -18.963 1.00 67.38  ? 508 NAG   A O6  1 
HETATM 2768 O  O7  . NAG   I 2 .   ? -5.400  34.359  -15.495 1.00 66.79  ? 508 NAG   A O7  1 
HETATM 2769 C  C1  . NAG   J 2 .   ? -24.831 13.261  -23.307 1.00 47.72  ? 509 NAG   A C1  1 
HETATM 2770 C  C2  . NAG   J 2 .   ? -24.632 11.791  -23.700 1.00 50.10  ? 509 NAG   A C2  1 
HETATM 2771 C  C3  . NAG   J 2 .   ? -25.857 11.267  -24.452 1.00 51.83  ? 509 NAG   A C3  1 
HETATM 2772 C  C4  . NAG   J 2 .   ? -27.113 11.526  -23.631 1.00 53.39  ? 509 NAG   A C4  1 
HETATM 2773 C  C5  . NAG   J 2 .   ? -27.203 13.014  -23.328 1.00 50.29  ? 509 NAG   A C5  1 
HETATM 2774 C  C6  . NAG   J 2 .   ? -28.412 13.389  -22.506 1.00 51.57  ? 509 NAG   A C6  1 
HETATM 2775 C  C7  . NAG   J 2 .   ? -22.314 11.050  -24.019 1.00 48.75  ? 509 NAG   A C7  1 
HETATM 2776 C  C8  . NAG   J 2 .   ? -21.150 10.990  -24.958 1.00 45.25  ? 509 NAG   A C8  1 
HETATM 2777 N  N2  . NAG   J 2 .   ? -23.422 11.631  -24.492 1.00 50.97  ? 509 NAG   A N2  1 
HETATM 2778 O  O3  . NAG   J 2 .   ? -25.727 9.872   -24.707 1.00 55.24  ? 509 NAG   A O3  1 
HETATM 2779 O  O4  . NAG   J 2 .   ? -28.285 11.103  -24.318 1.00 52.92  ? 509 NAG   A O4  1 
HETATM 2780 O  O5  . NAG   J 2 .   ? -26.048 13.403  -22.577 1.00 48.67  ? 509 NAG   A O5  1 
HETATM 2781 O  O6  . NAG   J 2 .   ? -28.064 14.285  -21.460 1.00 52.13  ? 509 NAG   A O6  1 
HETATM 2782 O  O7  . NAG   J 2 .   ? -22.257 10.588  -22.885 1.00 47.60  ? 509 NAG   A O7  1 
HETATM 2783 C  C1  . NAG   K 2 .   ? -32.131 31.922  2.174   1.00 59.15  ? 510 NAG   A C1  1 
HETATM 2784 C  C2  . NAG   K 2 .   ? -32.233 33.364  2.645   1.00 57.80  ? 510 NAG   A C2  1 
HETATM 2785 C  C3  . NAG   K 2 .   ? -32.997 34.182  1.616   1.00 58.19  ? 510 NAG   A C3  1 
HETATM 2786 C  C4  . NAG   K 2 .   ? -32.358 34.033  0.241   1.00 61.91  ? 510 NAG   A C4  1 
HETATM 2787 C  C5  . NAG   K 2 .   ? -32.221 32.559  -0.126  1.00 60.68  ? 510 NAG   A C5  1 
HETATM 2788 C  C6  . NAG   K 2 .   ? -31.554 32.325  -1.462  1.00 62.65  ? 510 NAG   A C6  1 
HETATM 2789 C  C7  . NAG   K 2 .   ? -32.347 34.073  4.992   1.00 55.03  ? 510 NAG   A C7  1 
HETATM 2790 C  C8  . NAG   K 2 .   ? -33.162 34.062  6.251   1.00 49.97  ? 510 NAG   A C8  1 
HETATM 2791 N  N2  . NAG   K 2 .   ? -32.882 33.445  3.942   1.00 56.11  ? 510 NAG   A N2  1 
HETATM 2792 O  O3  . NAG   K 2 .   ? -33.004 35.549  2.006   1.00 57.80  ? 510 NAG   A O3  1 
HETATM 2793 O  O4  . NAG   K 2 .   ? -33.164 34.686  -0.734  1.00 63.46  ? 510 NAG   A O4  1 
HETATM 2794 O  O5  . NAG   K 2 .   ? -31.457 31.876  0.882   1.00 66.30  ? 510 NAG   A O5  1 
HETATM 2795 O  O6  . NAG   K 2 .   ? -31.904 31.049  -1.985  1.00 65.85  ? 510 NAG   A O6  1 
HETATM 2796 O  O7  . NAG   K 2 .   ? -31.256 34.624  4.929   1.00 58.24  ? 510 NAG   A O7  1 
HETATM 2797 N  N1  . EPE   L 3 .   ? -5.844  -6.134  -15.580 1.00 39.52  ? 511 EPE   A N1  1 
HETATM 2798 C  C2  . EPE   L 3 .   ? -5.326  -5.662  -14.281 1.00 41.59  ? 511 EPE   A C2  1 
HETATM 2799 C  C3  . EPE   L 3 .   ? -6.464  -5.597  -13.257 1.00 38.09  ? 511 EPE   A C3  1 
HETATM 2800 N  N4  . EPE   L 3 .   ? -7.610  -4.882  -13.782 1.00 38.94  ? 511 EPE   A N4  1 
HETATM 2801 C  C5  . EPE   L 3 .   ? -8.000  -5.111  -15.163 1.00 40.32  ? 511 EPE   A C5  1 
HETATM 2802 C  C6  . EPE   L 3 .   ? -6.813  -5.173  -16.110 1.00 33.90  ? 511 EPE   A C6  1 
HETATM 2803 C  C7  . EPE   L 3 .   ? -8.665  -4.478  -12.882 1.00 36.80  ? 511 EPE   A C7  1 
HETATM 2804 C  C8  . EPE   L 3 .   ? -8.170  -3.477  -11.861 1.00 38.30  ? 511 EPE   A C8  1 
HETATM 2805 O  O8  . EPE   L 3 .   ? -7.687  -4.197  -10.756 1.00 42.00  ? 511 EPE   A O8  1 
HETATM 2806 C  C9  . EPE   L 3 .   ? -4.733  -6.250  -16.523 1.00 39.41  ? 511 EPE   A C9  1 
HETATM 2807 C  C10 . EPE   L 3 .   ? -4.753  -7.618  -17.186 1.00 38.61  ? 511 EPE   A C10 1 
HETATM 2808 S  S   . EPE   L 3 .   ? -3.275  -7.765  -18.215 1.00 38.16  ? 511 EPE   A S   1 
HETATM 2809 O  O1S . EPE   L 3 .   ? -3.070  -6.550  -18.994 1.00 38.28  ? 511 EPE   A O1S 1 
HETATM 2810 O  O2S . EPE   L 3 .   ? -2.165  -7.936  -17.287 1.00 42.01  ? 511 EPE   A O2S 1 
HETATM 2811 O  O3S . EPE   L 3 .   ? -3.362  -8.905  -19.111 1.00 40.26  ? 511 EPE   A O3S 1 
HETATM 2812 C  C10 . A1AS5 M 4 .   ? -2.438  16.709  -12.651 1.00 42.51  ? 512 A1AS5 A C10 1 
HETATM 2813 C  CD  . A1AS5 M 4 .   ? 0.415   13.851  -8.623  1.00 50.93  ? 512 A1AS5 A CD  1 
HETATM 2814 N  NE  . A1AS5 M 4 .   ? 0.423   13.139  -7.314  1.00 56.62  ? 512 A1AS5 A NE  1 
HETATM 2815 C  CZ  . A1AS5 M 4 .   ? 1.442   13.512  -6.348  1.00 52.63  ? 512 A1AS5 A CZ  1 
HETATM 2816 N  NH1 . A1AS5 M 4 .   ? 1.439   12.950  -5.246  1.00 51.99  ? 512 A1AS5 A NH1 1 
HETATM 2817 N  NH2 . A1AS5 M 4 .   ? 2.302   14.368  -6.602  1.00 53.74  ? 512 A1AS5 A NH2 1 
HETATM 2818 C  C06 . A1AS5 M 4 .   ? -0.117  15.302  -8.352  1.00 49.18  ? 512 A1AS5 A C06 1 
HETATM 2819 C  C08 . A1AS5 M 4 .   ? -1.510  15.521  -10.666 1.00 49.08  ? 512 A1AS5 A C08 1 
HETATM 2820 C  C09 . A1AS5 M 4 .   ? -1.120  16.616  -11.772 1.00 47.57  ? 512 A1AS5 A C09 1 
HETATM 2821 C  C13 . A1AS5 M 4 .   ? -3.161  16.709  -15.156 1.00 39.71  ? 512 A1AS5 A C13 1 
HETATM 2822 C  C14 . A1AS5 M 4 .   ? -4.478  16.589  -14.974 1.00 40.52  ? 512 A1AS5 A C14 1 
HETATM 2823 C  C15 . A1AS5 M 4 .   ? -5.337  16.513  -16.129 1.00 39.08  ? 512 A1AS5 A C15 1 
HETATM 2824 C  C17 . A1AS5 M 4 .   ? -4.812  16.509  -17.396 1.00 37.83  ? 512 A1AS5 A C17 1 
HETATM 2825 C  C19 . A1AS5 M 4 .   ? -3.487  16.582  -17.570 1.00 38.31  ? 512 A1AS5 A C19 1 
HETATM 2826 C  C20 . A1AS5 M 4 .   ? -2.643  16.656  -16.445 1.00 41.83  ? 512 A1AS5 A C20 1 
HETATM 2827 C  C21 . A1AS5 M 4 .   ? -0.309  17.695  -11.203 1.00 48.77  ? 512 A1AS5 A C21 1 
HETATM 2828 C  C22 . A1AS5 M 4 .   ? -0.255  17.918  -9.764  1.00 48.09  ? 512 A1AS5 A C22 1 
HETATM 2829 C  C23 . A1AS5 M 4 .   ? -1.531  17.371  -9.155  1.00 48.72  ? 512 A1AS5 A C23 1 
HETATM 2830 F  F16 . A1AS5 M 4 .   ? -6.726  16.445  -16.001 1.00 36.64  ? 512 A1AS5 A F16 1 
HETATM 2831 N  N07 . A1AS5 M 4 .   ? -1.057  15.984  -9.322  1.00 47.79  ? 512 A1AS5 A N07 1 
HETATM 2832 N  N12 . A1AS5 M 4 .   ? -2.175  16.749  -14.088 1.00 41.64  ? 512 A1AS5 A N12 1 
HETATM 2833 O  O11 . A1AS5 M 4 .   ? -3.585  16.604  -12.192 1.00 40.60  ? 512 A1AS5 A O11 1 
HETATM 2834 O  O24 . A1AS5 M 4 .   ? 0.226   15.908  -7.292  1.00 49.68  ? 512 A1AS5 A O24 1 
HETATM 2835 CL CL1 . A1AS5 M 4 .   ? -5.860  16.409  -18.773 1.00 54.08  ? 512 A1AS5 A CL1 1 
HETATM 2836 O  O   . HOH   N 5 .   ? -18.732 2.190   -2.864  1.00 39.19  ? 601 HOH   A O   1 
HETATM 2837 O  O   . HOH   N 5 .   ? -25.856 42.286  -20.607 1.00 52.28  ? 602 HOH   A O   1 
HETATM 2838 O  O   . HOH   N 5 .   ? -16.939 -0.380  -23.756 1.00 39.82  ? 603 HOH   A O   1 
HETATM 2839 O  O   . HOH   N 5 .   ? -27.895 4.839   -6.672  1.00 43.63  ? 604 HOH   A O   1 
HETATM 2840 O  O   . HOH   N 5 .   ? 2.974   15.278  -11.749 1.00 44.32  ? 605 HOH   A O   1 
HETATM 2841 O  O   . HOH   N 5 .   ? -32.903 26.840  1.907   1.00 50.95  ? 606 HOH   A O   1 
HETATM 2842 O  O   . HOH   N 5 .   ? 1.126   23.876  -40.937 1.00 52.28  ? 607 HOH   A O   1 
HETATM 2843 O  O   . HOH   N 5 .   ? -11.039 4.545   -2.736  1.00 40.25  ? 608 HOH   A O   1 
HETATM 2844 O  O   . HOH   N 5 .   ? -16.762 -16.254 7.704   1.00 46.90  ? 609 HOH   A O   1 
HETATM 2845 O  O   . HOH   N 5 .   ? -8.840  -10.595 -12.249 1.00 37.04  ? 610 HOH   A O   1 
HETATM 2846 O  O   . HOH   N 5 .   ? -31.351 25.525  -28.162 1.00 54.47  ? 611 HOH   A O   1 
HETATM 2847 O  O   . HOH   N 5 .   ? -16.533 15.491  -32.640 1.00 41.15  ? 612 HOH   A O   1 
HETATM 2848 O  O   . HOH   N 5 .   ? -5.366  27.550  -33.295 1.00 38.84  ? 613 HOH   A O   1 
HETATM 2849 O  O   . HOH   N 5 .   ? -16.750 10.023  -30.872 1.00 49.35  ? 614 HOH   A O   1 
HETATM 2850 O  O   . HOH   N 5 .   ? -14.913 -2.248  -2.379  1.00 38.58  ? 615 HOH   A O   1 
HETATM 2851 O  O   . HOH   N 5 .   ? 1.218   17.350  -37.627 1.00 56.08  ? 616 HOH   A O   1 
HETATM 2852 O  O   . HOH   N 5 .   ? -11.134 12.374  -26.768 1.00 42.93  ? 617 HOH   A O   1 
HETATM 2853 O  O   . HOH   N 5 .   ? -0.185  14.084  -28.143 1.00 42.05  ? 618 HOH   A O   1 
HETATM 2854 O  O   . HOH   N 5 .   ? -23.248 25.987  9.054   1.00 47.84  ? 619 HOH   A O   1 
HETATM 2855 O  O   . HOH   N 5 .   ? -2.727  32.920  -25.443 1.00 44.84  ? 620 HOH   A O   1 
HETATM 2856 O  O   . HOH   N 5 .   ? -15.696 10.135  -15.970 1.00 39.37  ? 621 HOH   A O   1 
# 
